data_9GKZ
# 
_entry.id   9GKZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9GKZ         pdb_00009gkz 10.2210/pdb9gkz/pdb 
WWPDB D_1292141043 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ISSN'         
4 2 'Structure model' '_citation.journal_volume'          
5 2 'Structure model' '_citation.page_first'              
6 2 'Structure model' '_citation.page_last'               
7 2 'Structure model' '_citation.pdbx_database_id_DOI'    
8 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
9 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GKZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michael.lammers@uni-greifswald.de 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Lammers 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4168-4640 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Graf, L.G.'  1 0009-0007-7269-1743 
'Schulze, S.' 2 0000-0002-0122-5688 
'Palm, G.J.'  3 0000-0003-0329-0413 
'Lammers, M.' 4 0000-0003-4168-4640 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                9496 
_citation.page_last                 9496 
_citation.title                     'Distribution and diversity of classical deacylases in bacteria.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-53903-0 
_citation.pdbx_database_id_PubMed   39489725 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Graf, L.G.'        1  0009-0007-7269-1743 
primary 'Moreno-Yruela, C.' 2  0000-0003-2450-6519 
primary 'Qin, C.'           3  ?                   
primary 'Schulze, S.'       4  0000-0002-0122-5688 
primary 'Palm, G.J.'        5  0000-0003-0329-0413 
primary 'Schmoker, O.'      6  ?                   
primary 'Wang, N.'          7  0000-0001-7623-1858 
primary 'Hocking, D.M.'     8  0000-0002-3485-0586 
primary 'Jebeli, L.'        9  0000-0003-4240-9528 
primary 'Girbardt, B.'      10 ?                   
primary 'Berndt, L.'        11 ?                   
primary 'Dorre, B.'         12 ?                   
primary 'Weis, D.M.'        13 ?                   
primary 'Janetzky, M.'      14 ?                   
primary 'Albrecht, D.'      15 ?                   
primary 'Zuhlke, D.'        16 ?                   
primary 'Sievers, S.'       17 0000-0002-5457-2552 
primary 'Strugnell, R.A.'   18 0000-0003-0614-5641 
primary 'Olsen, C.A.'       19 0000-0002-2953-8942 
primary 'Hofmann, K.'       20 0000-0002-2289-9083 
primary 'Lammers, M.'       21 0000-0003-4168-4640 
# 
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 'Acetylpolyamine amidohydrolase' 38977.312 2   ? ? ? 'His6-tagged truncated (1-342) fusion-ptotein' 
2 non-polymer syn 'TRIETHYLENE GLYCOL'             150.173   1   ? ? ? ?                                              
3 non-polymer syn 'POTASSIUM ION'                  39.098    6   ? ? ? ?                                              
4 non-polymer syn 'ZINC ION'                       65.409    2   ? ? ? ?                                              
5 non-polymer syn 'CHLORIDE ION'                   35.453    1   ? ? ? ?                                              
6 non-polymer syn 'ACETATE ION'                    59.044    1   ? ? ? ?                                              
7 non-polymer syn 'DI(HYDROXYETHYL)ETHER'          106.120   1   ? ? ? ?                                              
8 water       nat water                            18.015    129 ? ? ? ?                                              
# 
_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       
;MAHHHHHHVGTMLTIYSDDHHLHHGSCELIDGKLMPCFEMPKRADHILQRVKDRNIGEIREPQDFGRDPIQRIHTAEYLN
FFEGAWARWQEQDGTGDLLPYTWPARTLSQRLPTSLHGQLGYYSFDAGAPITAGTWQAAYSAAQVALTAQHEITNGAHSA
FALCRPPGHHAASDVMGGYCYLNNAAIAAQAFIDQGHKRVAILDVDYHHGNGTQSIFYSRSDVLFTSIHGDPKFEFPFFL
GHADEHGEGTGEGFNINYPLPAGSAWDSWGAALDDACKRINAFDAEVVIVSLGVDTYKEDPISQFKLDSPDYLSMGERIA
AMGLPTLFVMEGGYAVEAIGVNAVNVLEGFENV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHVGTMLTIYSDDHHLHHGSCELIDGKLMPCFEMPKRADHILQRVKDRNIGEIREPQDFGRDPIQRIHTAEYLN
FFEGAWARWQEQDGTGDLLPYTWPARTLSQRLPTSLHGQLGYYSFDAGAPITAGTWQAAYSAAQVALTAQHEITNGAHSA
FALCRPPGHHAASDVMGGYCYLNNAAIAAQAFIDQGHKRVAILDVDYHHGNGTQSIFYSRSDVLFTSIHGDPKFEFPFFL
GHADEHGEGTGEGFNINYPLPAGSAWDSWGAALDDACKRINAFDAEVVIVSLGVDTYKEDPISQFKLDSPDYLSMGERIA
AMGLPTLFVMEGGYAVEAIGVNAVNVLEGFENV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'TRIETHYLENE GLYCOL'    PGE 
3 'POTASSIUM ION'         K   
4 'ZINC ION'              ZN  
5 'CHLORIDE ION'          CL  
6 'ACETATE ION'           ACT 
7 'DI(HYDROXYETHYL)ETHER' PEG 
8 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   VAL n 
1 10  GLY n 
1 11  THR n 
1 12  MET n 
1 13  LEU n 
1 14  THR n 
1 15  ILE n 
1 16  TYR n 
1 17  SER n 
1 18  ASP n 
1 19  ASP n 
1 20  HIS n 
1 21  HIS n 
1 22  LEU n 
1 23  HIS n 
1 24  HIS n 
1 25  GLY n 
1 26  SER n 
1 27  CYS n 
1 28  GLU n 
1 29  LEU n 
1 30  ILE n 
1 31  ASP n 
1 32  GLY n 
1 33  LYS n 
1 34  LEU n 
1 35  MET n 
1 36  PRO n 
1 37  CYS n 
1 38  PHE n 
1 39  GLU n 
1 40  MET n 
1 41  PRO n 
1 42  LYS n 
1 43  ARG n 
1 44  ALA n 
1 45  ASP n 
1 46  HIS n 
1 47  ILE n 
1 48  LEU n 
1 49  GLN n 
1 50  ARG n 
1 51  VAL n 
1 52  LYS n 
1 53  ASP n 
1 54  ARG n 
1 55  ASN n 
1 56  ILE n 
1 57  GLY n 
1 58  GLU n 
1 59  ILE n 
1 60  ARG n 
1 61  GLU n 
1 62  PRO n 
1 63  GLN n 
1 64  ASP n 
1 65  PHE n 
1 66  GLY n 
1 67  ARG n 
1 68  ASP n 
1 69  PRO n 
1 70  ILE n 
1 71  GLN n 
1 72  ARG n 
1 73  ILE n 
1 74  HIS n 
1 75  THR n 
1 76  ALA n 
1 77  GLU n 
1 78  TYR n 
1 79  LEU n 
1 80  ASN n 
1 81  PHE n 
1 82  PHE n 
1 83  GLU n 
1 84  GLY n 
1 85  ALA n 
1 86  TRP n 
1 87  ALA n 
1 88  ARG n 
1 89  TRP n 
1 90  GLN n 
1 91  GLU n 
1 92  GLN n 
1 93  ASP n 
1 94  GLY n 
1 95  THR n 
1 96  GLY n 
1 97  ASP n 
1 98  LEU n 
1 99  LEU n 
1 100 PRO n 
1 101 TYR n 
1 102 THR n 
1 103 TRP n 
1 104 PRO n 
1 105 ALA n 
1 106 ARG n 
1 107 THR n 
1 108 LEU n 
1 109 SER n 
1 110 GLN n 
1 111 ARG n 
1 112 LEU n 
1 113 PRO n 
1 114 THR n 
1 115 SER n 
1 116 LEU n 
1 117 HIS n 
1 118 GLY n 
1 119 GLN n 
1 120 LEU n 
1 121 GLY n 
1 122 TYR n 
1 123 TYR n 
1 124 SER n 
1 125 PHE n 
1 126 ASP n 
1 127 ALA n 
1 128 GLY n 
1 129 ALA n 
1 130 PRO n 
1 131 ILE n 
1 132 THR n 
1 133 ALA n 
1 134 GLY n 
1 135 THR n 
1 136 TRP n 
1 137 GLN n 
1 138 ALA n 
1 139 ALA n 
1 140 TYR n 
1 141 SER n 
1 142 ALA n 
1 143 ALA n 
1 144 GLN n 
1 145 VAL n 
1 146 ALA n 
1 147 LEU n 
1 148 THR n 
1 149 ALA n 
1 150 GLN n 
1 151 HIS n 
1 152 GLU n 
1 153 ILE n 
1 154 THR n 
1 155 ASN n 
1 156 GLY n 
1 157 ALA n 
1 158 HIS n 
1 159 SER n 
1 160 ALA n 
1 161 PHE n 
1 162 ALA n 
1 163 LEU n 
1 164 CYS n 
1 165 ARG n 
1 166 PRO n 
1 167 PRO n 
1 168 GLY n 
1 169 HIS n 
1 170 HIS n 
1 171 ALA n 
1 172 ALA n 
1 173 SER n 
1 174 ASP n 
1 175 VAL n 
1 176 MET n 
1 177 GLY n 
1 178 GLY n 
1 179 TYR n 
1 180 CYS n 
1 181 TYR n 
1 182 LEU n 
1 183 ASN n 
1 184 ASN n 
1 185 ALA n 
1 186 ALA n 
1 187 ILE n 
1 188 ALA n 
1 189 ALA n 
1 190 GLN n 
1 191 ALA n 
1 192 PHE n 
1 193 ILE n 
1 194 ASP n 
1 195 GLN n 
1 196 GLY n 
1 197 HIS n 
1 198 LYS n 
1 199 ARG n 
1 200 VAL n 
1 201 ALA n 
1 202 ILE n 
1 203 LEU n 
1 204 ASP n 
1 205 VAL n 
1 206 ASP n 
1 207 TYR n 
1 208 HIS n 
1 209 HIS n 
1 210 GLY n 
1 211 ASN n 
1 212 GLY n 
1 213 THR n 
1 214 GLN n 
1 215 SER n 
1 216 ILE n 
1 217 PHE n 
1 218 TYR n 
1 219 SER n 
1 220 ARG n 
1 221 SER n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PHE n 
1 226 THR n 
1 227 SER n 
1 228 ILE n 
1 229 HIS n 
1 230 GLY n 
1 231 ASP n 
1 232 PRO n 
1 233 LYS n 
1 234 PHE n 
1 235 GLU n 
1 236 PHE n 
1 237 PRO n 
1 238 PHE n 
1 239 PHE n 
1 240 LEU n 
1 241 GLY n 
1 242 HIS n 
1 243 ALA n 
1 244 ASP n 
1 245 GLU n 
1 246 HIS n 
1 247 GLY n 
1 248 GLU n 
1 249 GLY n 
1 250 THR n 
1 251 GLY n 
1 252 GLU n 
1 253 GLY n 
1 254 PHE n 
1 255 ASN n 
1 256 ILE n 
1 257 ASN n 
1 258 TYR n 
1 259 PRO n 
1 260 LEU n 
1 261 PRO n 
1 262 ALA n 
1 263 GLY n 
1 264 SER n 
1 265 ALA n 
1 266 TRP n 
1 267 ASP n 
1 268 SER n 
1 269 TRP n 
1 270 GLY n 
1 271 ALA n 
1 272 ALA n 
1 273 LEU n 
1 274 ASP n 
1 275 ASP n 
1 276 ALA n 
1 277 CYS n 
1 278 LYS n 
1 279 ARG n 
1 280 ILE n 
1 281 ASN n 
1 282 ALA n 
1 283 PHE n 
1 284 ASP n 
1 285 ALA n 
1 286 GLU n 
1 287 VAL n 
1 288 VAL n 
1 289 ILE n 
1 290 VAL n 
1 291 SER n 
1 292 LEU n 
1 293 GLY n 
1 294 VAL n 
1 295 ASP n 
1 296 THR n 
1 297 TYR n 
1 298 LYS n 
1 299 GLU n 
1 300 ASP n 
1 301 PRO n 
1 302 ILE n 
1 303 SER n 
1 304 GLN n 
1 305 PHE n 
1 306 LYS n 
1 307 LEU n 
1 308 ASP n 
1 309 SER n 
1 310 PRO n 
1 311 ASP n 
1 312 TYR n 
1 313 LEU n 
1 314 SER n 
1 315 MET n 
1 316 GLY n 
1 317 GLU n 
1 318 ARG n 
1 319 ILE n 
1 320 ALA n 
1 321 ALA n 
1 322 MET n 
1 323 GLY n 
1 324 LEU n 
1 325 PRO n 
1 326 THR n 
1 327 LEU n 
1 328 PHE n 
1 329 VAL n 
1 330 MET n 
1 331 GLU n 
1 332 GLY n 
1 333 GLY n 
1 334 TYR n 
1 335 ALA n 
1 336 VAL n 
1 337 GLU n 
1 338 ALA n 
1 339 ILE n 
1 340 GLY n 
1 341 VAL n 
1 342 ASN n 
1 343 ALA n 
1 344 VAL n 
1 345 ASN n 
1 346 VAL n 
1 347 LEU n 
1 348 GLU n 
1 349 GLY n 
1 350 PHE n 
1 351 GLU n 
1 352 ASN n 
1 353 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   353 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 B9K09_22070 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    M30-35 
_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      'Pseudomonas sp. M30-35' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1981174 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET-45b(+)' 
_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 
ACT non-polymer         . 'ACETATE ION'           ? 'C2 H3 O2 -1'    59.044  
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 
CL  non-polymer         . 'CHLORIDE ION'          ? 'Cl -1'          35.453  
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 
K   non-polymer         . 'POTASSIUM ION'         ? 'K 1'            39.098  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'    ? 'C6 H14 O4'      150.173 
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   MET 1   -10 ?   ?   ?   A . n 
A 1 2   ALA 2   -9  ?   ?   ?   A . n 
A 1 3   HIS 3   -8  ?   ?   ?   A . n 
A 1 4   HIS 4   -7  ?   ?   ?   A . n 
A 1 5   HIS 5   -6  ?   ?   ?   A . n 
A 1 6   HIS 6   -5  ?   ?   ?   A . n 
A 1 7   HIS 7   -4  ?   ?   ?   A . n 
A 1 8   HIS 8   -3  ?   ?   ?   A . n 
A 1 9   VAL 9   -2  -2  VAL ALA A . n 
A 1 10  GLY 10  -1  -1  GLY ALA A . n 
A 1 11  THR 11  0   0   THR THR A . n 
A 1 12  MET 12  1   1   MET MET A . n 
A 1 13  LEU 13  2   2   LEU LEU A . n 
A 1 14  THR 14  3   3   THR THR A . n 
A 1 15  ILE 15  4   4   ILE ILE A . n 
A 1 16  TYR 16  5   5   TYR TYR A . n 
A 1 17  SER 17  6   6   SER SER A . n 
A 1 18  ASP 18  7   ?   ?   ?   A . n 
A 1 19  ASP 19  8   ?   ?   ?   A . n 
A 1 20  HIS 20  9   ?   ?   ?   A . n 
A 1 21  HIS 21  10  ?   ?   ?   A . n 
A 1 22  LEU 22  11  ?   ?   ?   A . n 
A 1 23  HIS 23  12  ?   ?   ?   A . n 
A 1 24  HIS 24  13  ?   ?   ?   A . n 
A 1 25  GLY 25  14  ?   ?   ?   A . n 
A 1 26  SER 26  15  ?   ?   ?   A . n 
A 1 27  CYS 27  16  ?   ?   ?   A . n 
A 1 28  GLU 28  17  ?   ?   ?   A . n 
A 1 29  LEU 29  18  ?   ?   ?   A . n 
A 1 30  ILE 30  19  ?   ?   ?   A . n 
A 1 31  ASP 31  20  ?   ?   ?   A . n 
A 1 32  GLY 32  21  ?   ?   ?   A . n 
A 1 33  LYS 33  22  ?   ?   ?   A . n 
A 1 34  LEU 34  23  ?   ?   ?   A . n 
A 1 35  MET 35  24  ?   ?   ?   A . n 
A 1 36  PRO 36  25  ?   ?   ?   A . n 
A 1 37  CYS 37  26  ?   ?   ?   A . n 
A 1 38  PHE 38  27  ?   ?   ?   A . n 
A 1 39  GLU 39  28  ?   ?   ?   A . n 
A 1 40  MET 40  29  ?   ?   ?   A . n 
A 1 41  PRO 41  30  ?   ?   ?   A . n 
A 1 42  LYS 42  31  31  LYS LYS A . n 
A 1 43  ARG 43  32  32  ARG ARG A . n 
A 1 44  ALA 44  33  33  ALA ALA A . n 
A 1 45  ASP 45  34  34  ASP ASP A . n 
A 1 46  HIS 46  35  35  HIS HIS A . n 
A 1 47  ILE 47  36  36  ILE ILE A . n 
A 1 48  LEU 48  37  37  LEU LEU A . n 
A 1 49  GLN 49  38  38  GLN GLN A . n 
A 1 50  ARG 50  39  39  ARG ARG A . n 
A 1 51  VAL 51  40  40  VAL VAL A . n 
A 1 52  LYS 52  41  41  LYS LYS A . n 
A 1 53  ASP 53  42  42  ASP ASP A . n 
A 1 54  ARG 54  43  43  ARG ARG A . n 
A 1 55  ASN 55  44  44  ASN ASN A . n 
A 1 56  ILE 56  45  45  ILE ILE A . n 
A 1 57  GLY 57  46  46  GLY GLY A . n 
A 1 58  GLU 58  47  47  GLU GLU A . n 
A 1 59  ILE 59  48  48  ILE ILE A . n 
A 1 60  ARG 60  49  49  ARG ARG A . n 
A 1 61  GLU 61  50  50  GLU GLU A . n 
A 1 62  PRO 62  51  51  PRO PRO A . n 
A 1 63  GLN 63  52  52  GLN GLN A . n 
A 1 64  ASP 64  53  53  ASP ASP A . n 
A 1 65  PHE 65  54  54  PHE PHE A . n 
A 1 66  GLY 66  55  55  GLY GLY A . n 
A 1 67  ARG 67  56  56  ARG ARG A . n 
A 1 68  ASP 68  57  57  ASP ASP A . n 
A 1 69  PRO 69  58  58  PRO PRO A . n 
A 1 70  ILE 70  59  59  ILE ILE A . n 
A 1 71  GLN 71  60  60  GLN GLN A . n 
A 1 72  ARG 72  61  61  ARG ARG A . n 
A 1 73  ILE 73  62  62  ILE ILE A . n 
A 1 74  HIS 74  63  63  HIS HIS A . n 
A 1 75  THR 75  64  64  THR THR A . n 
A 1 76  ALA 76  65  65  ALA ALA A . n 
A 1 77  GLU 77  66  66  GLU GLU A . n 
A 1 78  TYR 78  67  67  TYR TYR A . n 
A 1 79  LEU 79  68  68  LEU LEU A . n 
A 1 80  ASN 80  69  69  ASN ASN A . n 
A 1 81  PHE 81  70  70  PHE PHE A . n 
A 1 82  PHE 82  71  71  PHE PHE A . n 
A 1 83  GLU 83  72  72  GLU GLU A . n 
A 1 84  GLY 84  73  73  GLY GLY A . n 
A 1 85  ALA 85  74  74  ALA ALA A . n 
A 1 86  TRP 86  75  75  TRP TRP A . n 
A 1 87  ALA 87  76  76  ALA ALA A . n 
A 1 88  ARG 88  77  77  ARG ARG A . n 
A 1 89  TRP 89  78  78  TRP TRP A . n 
A 1 90  GLN 90  79  79  GLN GLN A . n 
A 1 91  GLU 91  80  80  GLU GLU A . n 
A 1 92  GLN 92  81  81  GLN GLN A . n 
A 1 93  ASP 93  82  82  ASP ASP A . n 
A 1 94  GLY 94  83  83  GLY GLY A . n 
A 1 95  THR 95  84  84  THR THR A . n 
A 1 96  GLY 96  85  85  GLY GLY A . n 
A 1 97  ASP 97  86  86  ASP ASP A . n 
A 1 98  LEU 98  87  87  LEU LEU A . n 
A 1 99  LEU 99  88  88  LEU LEU A . n 
A 1 100 PRO 100 89  89  PRO PRO A . n 
A 1 101 TYR 101 90  90  TYR TYR A . n 
A 1 102 THR 102 91  91  THR THR A . n 
A 1 103 TRP 103 92  92  TRP TRP A . n 
A 1 104 PRO 104 93  93  PRO PRO A . n 
A 1 105 ALA 105 94  94  ALA ALA A . n 
A 1 106 ARG 106 95  95  ARG ARG A . n 
A 1 107 THR 107 96  96  THR THR A . n 
A 1 108 LEU 108 97  97  LEU LEU A . n 
A 1 109 SER 109 98  98  SER SER A . n 
A 1 110 GLN 110 99  99  GLN GLN A . n 
A 1 111 ARG 111 100 100 ARG ARG A . n 
A 1 112 LEU 112 101 101 LEU LEU A . n 
A 1 113 PRO 113 102 102 PRO PRO A . n 
A 1 114 THR 114 103 103 THR THR A . n 
A 1 115 SER 115 104 104 SER SER A . n 
A 1 116 LEU 116 105 105 LEU LEU A . n 
A 1 117 HIS 117 106 106 HIS HIS A . n 
A 1 118 GLY 118 107 107 GLY GLY A . n 
A 1 119 GLN 119 108 108 GLN GLN A . n 
A 1 120 LEU 120 109 109 LEU LEU A . n 
A 1 121 GLY 121 110 110 GLY GLY A . n 
A 1 122 TYR 122 111 111 TYR TYR A . n 
A 1 123 TYR 123 112 112 TYR TYR A . n 
A 1 124 SER 124 113 113 SER SER A . n 
A 1 125 PHE 125 114 114 PHE PHE A . n 
A 1 126 ASP 126 115 115 ASP ASP A . n 
A 1 127 ALA 127 116 116 ALA ALA A . n 
A 1 128 GLY 128 117 117 GLY GLY A . n 
A 1 129 ALA 129 118 118 ALA ALA A . n 
A 1 130 PRO 130 119 119 PRO PRO A . n 
A 1 131 ILE 131 120 120 ILE ILE A . n 
A 1 132 THR 132 121 121 THR THR A . n 
A 1 133 ALA 133 122 122 ALA ALA A . n 
A 1 134 GLY 134 123 123 GLY GLY A . n 
A 1 135 THR 135 124 124 THR THR A . n 
A 1 136 TRP 136 125 125 TRP TRP A . n 
A 1 137 GLN 137 126 126 GLN GLN A . n 
A 1 138 ALA 138 127 127 ALA ALA A . n 
A 1 139 ALA 139 128 128 ALA ALA A . n 
A 1 140 TYR 140 129 129 TYR TYR A . n 
A 1 141 SER 141 130 130 SER SER A . n 
A 1 142 ALA 142 131 131 ALA ALA A . n 
A 1 143 ALA 143 132 132 ALA ALA A . n 
A 1 144 GLN 144 133 133 GLN GLN A . n 
A 1 145 VAL 145 134 134 VAL VAL A . n 
A 1 146 ALA 146 135 135 ALA ALA A . n 
A 1 147 LEU 147 136 136 LEU LEU A . n 
A 1 148 THR 148 137 137 THR THR A . n 
A 1 149 ALA 149 138 138 ALA ALA A . n 
A 1 150 GLN 150 139 139 GLN GLN A . n 
A 1 151 HIS 151 140 140 HIS HIS A . n 
A 1 152 GLU 152 141 141 GLU GLU A . n 
A 1 153 ILE 153 142 142 ILE ILE A . n 
A 1 154 THR 154 143 143 THR THR A . n 
A 1 155 ASN 155 144 144 ASN ASN A . n 
A 1 156 GLY 156 145 145 GLY GLY A . n 
A 1 157 ALA 157 146 146 ALA ALA A . n 
A 1 158 HIS 158 147 147 HIS HIS A . n 
A 1 159 SER 159 148 148 SER SER A . n 
A 1 160 ALA 160 149 149 ALA ALA A . n 
A 1 161 PHE 161 150 150 PHE PHE A . n 
A 1 162 ALA 162 151 151 ALA ALA A . n 
A 1 163 LEU 163 152 152 LEU LEU A . n 
A 1 164 CYS 164 153 153 CYS CYS A . n 
A 1 165 ARG 165 154 154 ARG ARG A . n 
A 1 166 PRO 166 155 155 PRO PRO A . n 
A 1 167 PRO 167 156 156 PRO PRO A . n 
A 1 168 GLY 168 157 157 GLY GLY A . n 
A 1 169 HIS 169 158 158 HIS HIS A . n 
A 1 170 HIS 170 159 159 HIS HIS A . n 
A 1 171 ALA 171 160 160 ALA ALA A . n 
A 1 172 ALA 172 161 161 ALA ALA A . n 
A 1 173 SER 173 162 162 SER SER A . n 
A 1 174 ASP 174 163 163 ASP ASP A . n 
A 1 175 VAL 175 164 164 VAL VAL A . n 
A 1 176 MET 176 165 165 MET MET A . n 
A 1 177 GLY 177 166 166 GLY GLY A . n 
A 1 178 GLY 178 167 167 GLY GLY A . n 
A 1 179 TYR 179 168 168 TYR TYR A . n 
A 1 180 CYS 180 169 169 CYS CYS A . n 
A 1 181 TYR 181 170 170 TYR TYR A . n 
A 1 182 LEU 182 171 171 LEU LEU A . n 
A 1 183 ASN 183 172 172 ASN ASN A . n 
A 1 184 ASN 184 173 173 ASN ASN A . n 
A 1 185 ALA 185 174 174 ALA ALA A . n 
A 1 186 ALA 186 175 175 ALA ALA A . n 
A 1 187 ILE 187 176 176 ILE ILE A . n 
A 1 188 ALA 188 177 177 ALA ALA A . n 
A 1 189 ALA 189 178 178 ALA ALA A . n 
A 1 190 GLN 190 179 179 GLN GLN A . n 
A 1 191 ALA 191 180 180 ALA ALA A . n 
A 1 192 PHE 192 181 181 PHE PHE A . n 
A 1 193 ILE 193 182 182 ILE ILE A . n 
A 1 194 ASP 194 183 183 ASP ASP A . n 
A 1 195 GLN 195 184 184 GLN GLN A . n 
A 1 196 GLY 196 185 185 GLY GLY A . n 
A 1 197 HIS 197 186 186 HIS HIS A . n 
A 1 198 LYS 198 187 187 LYS LYS A . n 
A 1 199 ARG 199 188 188 ARG ARG A . n 
A 1 200 VAL 200 189 189 VAL VAL A . n 
A 1 201 ALA 201 190 190 ALA ALA A . n 
A 1 202 ILE 202 191 191 ILE ILE A . n 
A 1 203 LEU 203 192 192 LEU LEU A . n 
A 1 204 ASP 204 193 193 ASP ASP A . n 
A 1 205 VAL 205 194 194 VAL VAL A . n 
A 1 206 ASP 206 195 195 ASP ASP A . n 
A 1 207 TYR 207 196 196 TYR TYR A . n 
A 1 208 HIS 208 197 197 HIS HIS A . n 
A 1 209 HIS 209 198 198 HIS HIS A . n 
A 1 210 GLY 210 199 199 GLY GLY A . n 
A 1 211 ASN 211 200 200 ASN ASN A . n 
A 1 212 GLY 212 201 201 GLY GLY A . n 
A 1 213 THR 213 202 202 THR THR A . n 
A 1 214 GLN 214 203 203 GLN GLN A . n 
A 1 215 SER 215 204 204 SER SER A . n 
A 1 216 ILE 216 205 205 ILE ILE A . n 
A 1 217 PHE 217 206 206 PHE PHE A . n 
A 1 218 TYR 218 207 207 TYR TYR A . n 
A 1 219 SER 219 208 208 SER SER A . n 
A 1 220 ARG 220 209 209 ARG ARG A . n 
A 1 221 SER 221 210 210 SER SER A . n 
A 1 222 ASP 222 211 211 ASP ASP A . n 
A 1 223 VAL 223 212 212 VAL VAL A . n 
A 1 224 LEU 224 213 213 LEU LEU A . n 
A 1 225 PHE 225 214 214 PHE PHE A . n 
A 1 226 THR 226 215 215 THR THR A . n 
A 1 227 SER 227 216 216 SER SER A . n 
A 1 228 ILE 228 217 217 ILE ILE A . n 
A 1 229 HIS 229 218 218 HIS HIS A . n 
A 1 230 GLY 230 219 219 GLY GLY A . n 
A 1 231 ASP 231 220 220 ASP ASP A . n 
A 1 232 PRO 232 221 221 PRO PRO A . n 
A 1 233 LYS 233 222 222 LYS LYS A . n 
A 1 234 PHE 234 223 223 PHE PHE A . n 
A 1 235 GLU 235 224 224 GLU GLU A . n 
A 1 236 PHE 236 225 225 PHE PHE A . n 
A 1 237 PRO 237 226 226 PRO PRO A . n 
A 1 238 PHE 238 227 227 PHE PHE A . n 
A 1 239 PHE 239 228 228 PHE PHE A . n 
A 1 240 LEU 240 229 229 LEU LEU A . n 
A 1 241 GLY 241 230 230 GLY GLY A . n 
A 1 242 HIS 242 231 231 HIS HIS A . n 
A 1 243 ALA 243 232 232 ALA ALA A . n 
A 1 244 ASP 244 233 233 ASP ASP A . n 
A 1 245 GLU 245 234 234 GLU GLU A . n 
A 1 246 HIS 246 235 235 HIS HIS A . n 
A 1 247 GLY 247 236 236 GLY GLY A . n 
A 1 248 GLU 248 237 237 GLU GLU A . n 
A 1 249 GLY 249 238 238 GLY GLY A . n 
A 1 250 THR 250 239 239 THR THR A . n 
A 1 251 GLY 251 240 240 GLY GLY A . n 
A 1 252 GLU 252 241 241 GLU GLU A . n 
A 1 253 GLY 253 242 242 GLY GLY A . n 
A 1 254 PHE 254 243 243 PHE PHE A . n 
A 1 255 ASN 255 244 244 ASN ASN A . n 
A 1 256 ILE 256 245 245 ILE ILE A . n 
A 1 257 ASN 257 246 246 ASN ASN A . n 
A 1 258 TYR 258 247 247 TYR TYR A . n 
A 1 259 PRO 259 248 248 PRO PRO A . n 
A 1 260 LEU 260 249 249 LEU LEU A . n 
A 1 261 PRO 261 250 250 PRO PRO A . n 
A 1 262 ALA 262 251 251 ALA ALA A . n 
A 1 263 GLY 263 252 252 GLY GLY A . n 
A 1 264 SER 264 253 253 SER SER A . n 
A 1 265 ALA 265 254 254 ALA ALA A . n 
A 1 266 TRP 266 255 255 TRP TRP A . n 
A 1 267 ASP 267 256 256 ASP ASP A . n 
A 1 268 SER 268 257 257 SER SER A . n 
A 1 269 TRP 269 258 258 TRP TRP A . n 
A 1 270 GLY 270 259 259 GLY GLY A . n 
A 1 271 ALA 271 260 260 ALA ALA A . n 
A 1 272 ALA 272 261 261 ALA ALA A . n 
A 1 273 LEU 273 262 262 LEU LEU A . n 
A 1 274 ASP 274 263 263 ASP ASP A . n 
A 1 275 ASP 275 264 264 ASP ASP A . n 
A 1 276 ALA 276 265 265 ALA ALA A . n 
A 1 277 CYS 277 266 266 CYS CYS A . n 
A 1 278 LYS 278 267 267 LYS LYS A . n 
A 1 279 ARG 279 268 268 ARG ARG A . n 
A 1 280 ILE 280 269 269 ILE ILE A . n 
A 1 281 ASN 281 270 270 ASN ASN A . n 
A 1 282 ALA 282 271 271 ALA ALA A . n 
A 1 283 PHE 283 272 272 PHE PHE A . n 
A 1 284 ASP 284 273 273 ASP ASP A . n 
A 1 285 ALA 285 274 274 ALA ALA A . n 
A 1 286 GLU 286 275 275 GLU GLU A . n 
A 1 287 VAL 287 276 276 VAL VAL A . n 
A 1 288 VAL 288 277 277 VAL VAL A . n 
A 1 289 ILE 289 278 278 ILE ILE A . n 
A 1 290 VAL 290 279 279 VAL VAL A . n 
A 1 291 SER 291 280 280 SER SER A . n 
A 1 292 LEU 292 281 281 LEU LEU A . n 
A 1 293 GLY 293 282 282 GLY GLY A . n 
A 1 294 VAL 294 283 283 VAL VAL A . n 
A 1 295 ASP 295 284 284 ASP ASP A . n 
A 1 296 THR 296 285 285 THR THR A . n 
A 1 297 TYR 297 286 286 TYR TYR A . n 
A 1 298 LYS 298 287 287 LYS LYS A . n 
A 1 299 GLU 299 288 288 GLU GLU A . n 
A 1 300 ASP 300 289 289 ASP ASP A . n 
A 1 301 PRO 301 290 290 PRO PRO A . n 
A 1 302 ILE 302 291 291 ILE ILE A . n 
A 1 303 SER 303 292 292 SER SER A . n 
A 1 304 GLN 304 293 293 GLN GLN A . n 
A 1 305 PHE 305 294 294 PHE PHE A . n 
A 1 306 LYS 306 295 295 LYS LYS A . n 
A 1 307 LEU 307 296 296 LEU LEU A . n 
A 1 308 ASP 308 297 297 ASP ASP A . n 
A 1 309 SER 309 298 298 SER SER A . n 
A 1 310 PRO 310 299 299 PRO PRO A . n 
A 1 311 ASP 311 300 300 ASP ASP A . n 
A 1 312 TYR 312 301 301 TYR TYR A . n 
A 1 313 LEU 313 302 302 LEU LEU A . n 
A 1 314 SER 314 303 303 SER SER A . n 
A 1 315 MET 315 304 304 MET MET A . n 
A 1 316 GLY 316 305 305 GLY GLY A . n 
A 1 317 GLU 317 306 306 GLU GLU A . n 
A 1 318 ARG 318 307 307 ARG ARG A . n 
A 1 319 ILE 319 308 308 ILE ILE A . n 
A 1 320 ALA 320 309 309 ALA ALA A . n 
A 1 321 ALA 321 310 310 ALA ALA A . n 
A 1 322 MET 322 311 311 MET MET A . n 
A 1 323 GLY 323 312 312 GLY GLY A . n 
A 1 324 LEU 324 313 313 LEU LEU A . n 
A 1 325 PRO 325 314 314 PRO PRO A . n 
A 1 326 THR 326 315 315 THR THR A . n 
A 1 327 LEU 327 316 316 LEU LEU A . n 
A 1 328 PHE 328 317 317 PHE PHE A . n 
A 1 329 VAL 329 318 318 VAL VAL A . n 
A 1 330 MET 330 319 319 MET MET A . n 
A 1 331 GLU 331 320 320 GLU GLU A . n 
A 1 332 GLY 332 321 321 GLY GLY A . n 
A 1 333 GLY 333 322 322 GLY GLY A . n 
A 1 334 TYR 334 323 323 TYR TYR A . n 
A 1 335 ALA 335 324 324 ALA ALA A . n 
A 1 336 VAL 336 325 325 VAL VAL A . n 
A 1 337 GLU 337 326 326 GLU GLU A . n 
A 1 338 ALA 338 327 327 ALA ALA A . n 
A 1 339 ILE 339 328 328 ILE ILE A . n 
A 1 340 GLY 340 329 329 GLY GLY A . n 
A 1 341 VAL 341 330 330 VAL VAL A . n 
A 1 342 ASN 342 331 331 ASN ASN A . n 
A 1 343 ALA 343 332 332 ALA ALA A . n 
A 1 344 VAL 344 333 333 VAL VAL A . n 
A 1 345 ASN 345 334 334 ASN ASN A . n 
A 1 346 VAL 346 335 335 VAL VAL A . n 
A 1 347 LEU 347 336 336 LEU LEU A . n 
A 1 348 GLU 348 337 337 GLU GLU A . n 
A 1 349 GLY 349 338 338 GLY GLY A . n 
A 1 350 PHE 350 339 339 PHE PHE A . n 
A 1 351 GLU 351 340 340 GLU GLU A . n 
A 1 352 ASN 352 341 341 ASN ASN A . n 
A 1 353 VAL 353 342 342 VAL VAL A . n 
B 1 1   MET 1   -10 ?   ?   ?   B . n 
B 1 2   ALA 2   -9  ?   ?   ?   B . n 
B 1 3   HIS 3   -8  ?   ?   ?   B . n 
B 1 4   HIS 4   -7  ?   ?   ?   B . n 
B 1 5   HIS 5   -6  ?   ?   ?   B . n 
B 1 6   HIS 6   -5  ?   ?   ?   B . n 
B 1 7   HIS 7   -4  ?   ?   ?   B . n 
B 1 8   HIS 8   -3  ?   ?   ?   B . n 
B 1 9   VAL 9   -2  ?   ?   ?   B . n 
B 1 10  GLY 10  -1  -1  GLY GLY B . n 
B 1 11  THR 11  0   0   THR THR B . n 
B 1 12  MET 12  1   1   MET MET B . n 
B 1 13  LEU 13  2   2   LEU LEU B . n 
B 1 14  THR 14  3   3   THR THR B . n 
B 1 15  ILE 15  4   4   ILE ILE B . n 
B 1 16  TYR 16  5   5   TYR TYR B . n 
B 1 17  SER 17  6   6   SER SER B . n 
B 1 18  ASP 18  7   7   ASP ASP B . n 
B 1 19  ASP 19  8   ?   ?   ?   B . n 
B 1 20  HIS 20  9   ?   ?   ?   B . n 
B 1 21  HIS 21  10  ?   ?   ?   B . n 
B 1 22  LEU 22  11  ?   ?   ?   B . n 
B 1 23  HIS 23  12  ?   ?   ?   B . n 
B 1 24  HIS 24  13  ?   ?   ?   B . n 
B 1 25  GLY 25  14  ?   ?   ?   B . n 
B 1 26  SER 26  15  ?   ?   ?   B . n 
B 1 27  CYS 27  16  ?   ?   ?   B . n 
B 1 28  GLU 28  17  ?   ?   ?   B . n 
B 1 29  LEU 29  18  ?   ?   ?   B . n 
B 1 30  ILE 30  19  ?   ?   ?   B . n 
B 1 31  ASP 31  20  ?   ?   ?   B . n 
B 1 32  GLY 32  21  ?   ?   ?   B . n 
B 1 33  LYS 33  22  ?   ?   ?   B . n 
B 1 34  LEU 34  23  ?   ?   ?   B . n 
B 1 35  MET 35  24  ?   ?   ?   B . n 
B 1 36  PRO 36  25  ?   ?   ?   B . n 
B 1 37  CYS 37  26  ?   ?   ?   B . n 
B 1 38  PHE 38  27  ?   ?   ?   B . n 
B 1 39  GLU 39  28  ?   ?   ?   B . n 
B 1 40  MET 40  29  ?   ?   ?   B . n 
B 1 41  PRO 41  30  ?   ?   ?   B . n 
B 1 42  LYS 42  31  31  LYS LYS B . n 
B 1 43  ARG 43  32  32  ARG ARG B . n 
B 1 44  ALA 44  33  33  ALA ALA B . n 
B 1 45  ASP 45  34  34  ASP ASP B . n 
B 1 46  HIS 46  35  35  HIS HIS B . n 
B 1 47  ILE 47  36  36  ILE ILE B . n 
B 1 48  LEU 48  37  37  LEU LEU B . n 
B 1 49  GLN 49  38  38  GLN GLN B . n 
B 1 50  ARG 50  39  39  ARG ARG B . n 
B 1 51  VAL 51  40  40  VAL VAL B . n 
B 1 52  LYS 52  41  41  LYS LYS B . n 
B 1 53  ASP 53  42  42  ASP ASP B . n 
B 1 54  ARG 54  43  43  ARG ARG B . n 
B 1 55  ASN 55  44  44  ASN ASN B . n 
B 1 56  ILE 56  45  45  ILE ILE B . n 
B 1 57  GLY 57  46  46  GLY GLY B . n 
B 1 58  GLU 58  47  47  GLU GLU B . n 
B 1 59  ILE 59  48  48  ILE ILE B . n 
B 1 60  ARG 60  49  49  ARG ARG B . n 
B 1 61  GLU 61  50  50  GLU GLU B . n 
B 1 62  PRO 62  51  51  PRO PRO B . n 
B 1 63  GLN 63  52  52  GLN GLN B . n 
B 1 64  ASP 64  53  53  ASP ASP B . n 
B 1 65  PHE 65  54  54  PHE PHE B . n 
B 1 66  GLY 66  55  55  GLY GLY B . n 
B 1 67  ARG 67  56  56  ARG ARG B . n 
B 1 68  ASP 68  57  57  ASP ASP B . n 
B 1 69  PRO 69  58  58  PRO PRO B . n 
B 1 70  ILE 70  59  59  ILE ILE B . n 
B 1 71  GLN 71  60  60  GLN GLN B . n 
B 1 72  ARG 72  61  61  ARG ARG B . n 
B 1 73  ILE 73  62  62  ILE ILE B . n 
B 1 74  HIS 74  63  63  HIS HIS B . n 
B 1 75  THR 75  64  64  THR THR B . n 
B 1 76  ALA 76  65  65  ALA ALA B . n 
B 1 77  GLU 77  66  66  GLU GLU B . n 
B 1 78  TYR 78  67  67  TYR TYR B . n 
B 1 79  LEU 79  68  68  LEU LEU B . n 
B 1 80  ASN 80  69  69  ASN ASN B . n 
B 1 81  PHE 81  70  70  PHE PHE B . n 
B 1 82  PHE 82  71  71  PHE PHE B . n 
B 1 83  GLU 83  72  72  GLU GLU B . n 
B 1 84  GLY 84  73  73  GLY GLY B . n 
B 1 85  ALA 85  74  74  ALA ALA B . n 
B 1 86  TRP 86  75  75  TRP TRP B . n 
B 1 87  ALA 87  76  76  ALA ALA B . n 
B 1 88  ARG 88  77  77  ARG ARG B . n 
B 1 89  TRP 89  78  78  TRP TRP B . n 
B 1 90  GLN 90  79  79  GLN GLN B . n 
B 1 91  GLU 91  80  80  GLU GLU B . n 
B 1 92  GLN 92  81  81  GLN GLN B . n 
B 1 93  ASP 93  82  82  ASP ASP B . n 
B 1 94  GLY 94  83  83  GLY GLY B . n 
B 1 95  THR 95  84  84  THR THR B . n 
B 1 96  GLY 96  85  85  GLY GLY B . n 
B 1 97  ASP 97  86  86  ASP ASP B . n 
B 1 98  LEU 98  87  87  LEU LEU B . n 
B 1 99  LEU 99  88  88  LEU LEU B . n 
B 1 100 PRO 100 89  89  PRO PRO B . n 
B 1 101 TYR 101 90  90  TYR TYR B . n 
B 1 102 THR 102 91  91  THR THR B . n 
B 1 103 TRP 103 92  92  TRP TRP B . n 
B 1 104 PRO 104 93  93  PRO PRO B . n 
B 1 105 ALA 105 94  94  ALA ALA B . n 
B 1 106 ARG 106 95  95  ARG ARG B . n 
B 1 107 THR 107 96  96  THR THR B . n 
B 1 108 LEU 108 97  97  LEU LEU B . n 
B 1 109 SER 109 98  98  SER SER B . n 
B 1 110 GLN 110 99  99  GLN GLN B . n 
B 1 111 ARG 111 100 100 ARG ARG B . n 
B 1 112 LEU 112 101 101 LEU LEU B . n 
B 1 113 PRO 113 102 102 PRO PRO B . n 
B 1 114 THR 114 103 103 THR THR B . n 
B 1 115 SER 115 104 104 SER SER B . n 
B 1 116 LEU 116 105 105 LEU LEU B . n 
B 1 117 HIS 117 106 106 HIS HIS B . n 
B 1 118 GLY 118 107 107 GLY GLY B . n 
B 1 119 GLN 119 108 108 GLN GLN B . n 
B 1 120 LEU 120 109 109 LEU LEU B . n 
B 1 121 GLY 121 110 110 GLY GLY B . n 
B 1 122 TYR 122 111 111 TYR TYR B . n 
B 1 123 TYR 123 112 112 TYR TYR B . n 
B 1 124 SER 124 113 113 SER SER B . n 
B 1 125 PHE 125 114 114 PHE PHE B . n 
B 1 126 ASP 126 115 115 ASP ASP B . n 
B 1 127 ALA 127 116 116 ALA ALA B . n 
B 1 128 GLY 128 117 117 GLY GLY B . n 
B 1 129 ALA 129 118 118 ALA ALA B . n 
B 1 130 PRO 130 119 119 PRO PRO B . n 
B 1 131 ILE 131 120 120 ILE ILE B . n 
B 1 132 THR 132 121 121 THR THR B . n 
B 1 133 ALA 133 122 122 ALA ALA B . n 
B 1 134 GLY 134 123 123 GLY GLY B . n 
B 1 135 THR 135 124 124 THR THR B . n 
B 1 136 TRP 136 125 125 TRP TRP B . n 
B 1 137 GLN 137 126 126 GLN GLN B . n 
B 1 138 ALA 138 127 127 ALA ALA B . n 
B 1 139 ALA 139 128 128 ALA ALA B . n 
B 1 140 TYR 140 129 129 TYR TYR B . n 
B 1 141 SER 141 130 130 SER SER B . n 
B 1 142 ALA 142 131 131 ALA ALA B . n 
B 1 143 ALA 143 132 132 ALA ALA B . n 
B 1 144 GLN 144 133 133 GLN GLN B . n 
B 1 145 VAL 145 134 134 VAL VAL B . n 
B 1 146 ALA 146 135 135 ALA ALA B . n 
B 1 147 LEU 147 136 136 LEU LEU B . n 
B 1 148 THR 148 137 137 THR THR B . n 
B 1 149 ALA 149 138 138 ALA ALA B . n 
B 1 150 GLN 150 139 139 GLN GLN B . n 
B 1 151 HIS 151 140 140 HIS HIS B . n 
B 1 152 GLU 152 141 141 GLU GLU B . n 
B 1 153 ILE 153 142 142 ILE ILE B . n 
B 1 154 THR 154 143 143 THR THR B . n 
B 1 155 ASN 155 144 144 ASN ASN B . n 
B 1 156 GLY 156 145 145 GLY GLY B . n 
B 1 157 ALA 157 146 146 ALA ALA B . n 
B 1 158 HIS 158 147 147 HIS HIS B . n 
B 1 159 SER 159 148 148 SER SER B . n 
B 1 160 ALA 160 149 149 ALA ALA B . n 
B 1 161 PHE 161 150 150 PHE PHE B . n 
B 1 162 ALA 162 151 151 ALA ALA B . n 
B 1 163 LEU 163 152 152 LEU LEU B . n 
B 1 164 CYS 164 153 153 CYS CYS B . n 
B 1 165 ARG 165 154 154 ARG ARG B . n 
B 1 166 PRO 166 155 155 PRO PRO B . n 
B 1 167 PRO 167 156 156 PRO PRO B . n 
B 1 168 GLY 168 157 157 GLY GLY B . n 
B 1 169 HIS 169 158 158 HIS HIS B . n 
B 1 170 HIS 170 159 159 HIS HIS B . n 
B 1 171 ALA 171 160 160 ALA ALA B . n 
B 1 172 ALA 172 161 161 ALA ALA B . n 
B 1 173 SER 173 162 162 SER SER B . n 
B 1 174 ASP 174 163 163 ASP ASP B . n 
B 1 175 VAL 175 164 164 VAL VAL B . n 
B 1 176 MET 176 165 165 MET MET B . n 
B 1 177 GLY 177 166 166 GLY GLY B . n 
B 1 178 GLY 178 167 167 GLY GLY B . n 
B 1 179 TYR 179 168 168 TYR TYR B . n 
B 1 180 CYS 180 169 169 CYS CYS B . n 
B 1 181 TYR 181 170 170 TYR TYR B . n 
B 1 182 LEU 182 171 171 LEU LEU B . n 
B 1 183 ASN 183 172 172 ASN ASN B . n 
B 1 184 ASN 184 173 173 ASN ASN B . n 
B 1 185 ALA 185 174 174 ALA ALA B . n 
B 1 186 ALA 186 175 175 ALA ALA B . n 
B 1 187 ILE 187 176 176 ILE ILE B . n 
B 1 188 ALA 188 177 177 ALA ALA B . n 
B 1 189 ALA 189 178 178 ALA ALA B . n 
B 1 190 GLN 190 179 179 GLN GLN B . n 
B 1 191 ALA 191 180 180 ALA ALA B . n 
B 1 192 PHE 192 181 181 PHE PHE B . n 
B 1 193 ILE 193 182 182 ILE ILE B . n 
B 1 194 ASP 194 183 183 ASP ASP B . n 
B 1 195 GLN 195 184 184 GLN GLN B . n 
B 1 196 GLY 196 185 185 GLY GLY B . n 
B 1 197 HIS 197 186 186 HIS HIS B . n 
B 1 198 LYS 198 187 187 LYS LYS B . n 
B 1 199 ARG 199 188 188 ARG ARG B . n 
B 1 200 VAL 200 189 189 VAL VAL B . n 
B 1 201 ALA 201 190 190 ALA ALA B . n 
B 1 202 ILE 202 191 191 ILE ILE B . n 
B 1 203 LEU 203 192 192 LEU LEU B . n 
B 1 204 ASP 204 193 193 ASP ASP B . n 
B 1 205 VAL 205 194 194 VAL VAL B . n 
B 1 206 ASP 206 195 195 ASP ASP B . n 
B 1 207 TYR 207 196 196 TYR TYR B . n 
B 1 208 HIS 208 197 197 HIS HIS B . n 
B 1 209 HIS 209 198 198 HIS HIS B . n 
B 1 210 GLY 210 199 199 GLY GLY B . n 
B 1 211 ASN 211 200 200 ASN ASN B . n 
B 1 212 GLY 212 201 201 GLY GLY B . n 
B 1 213 THR 213 202 202 THR THR B . n 
B 1 214 GLN 214 203 203 GLN GLN B . n 
B 1 215 SER 215 204 204 SER SER B . n 
B 1 216 ILE 216 205 205 ILE ILE B . n 
B 1 217 PHE 217 206 206 PHE PHE B . n 
B 1 218 TYR 218 207 207 TYR TYR B . n 
B 1 219 SER 219 208 208 SER SER B . n 
B 1 220 ARG 220 209 209 ARG ARG B . n 
B 1 221 SER 221 210 210 SER SER B . n 
B 1 222 ASP 222 211 211 ASP ASP B . n 
B 1 223 VAL 223 212 212 VAL VAL B . n 
B 1 224 LEU 224 213 213 LEU LEU B . n 
B 1 225 PHE 225 214 214 PHE PHE B . n 
B 1 226 THR 226 215 215 THR THR B . n 
B 1 227 SER 227 216 216 SER SER B . n 
B 1 228 ILE 228 217 217 ILE ILE B . n 
B 1 229 HIS 229 218 218 HIS HIS B . n 
B 1 230 GLY 230 219 219 GLY GLY B . n 
B 1 231 ASP 231 220 220 ASP ASP B . n 
B 1 232 PRO 232 221 221 PRO PRO B . n 
B 1 233 LYS 233 222 222 LYS LYS B . n 
B 1 234 PHE 234 223 223 PHE PHE B . n 
B 1 235 GLU 235 224 224 GLU GLU B . n 
B 1 236 PHE 236 225 225 PHE PHE B . n 
B 1 237 PRO 237 226 226 PRO PRO B . n 
B 1 238 PHE 238 227 227 PHE PHE B . n 
B 1 239 PHE 239 228 228 PHE PHE B . n 
B 1 240 LEU 240 229 229 LEU LEU B . n 
B 1 241 GLY 241 230 230 GLY GLY B . n 
B 1 242 HIS 242 231 231 HIS HIS B . n 
B 1 243 ALA 243 232 232 ALA ALA B . n 
B 1 244 ASP 244 233 233 ASP ASP B . n 
B 1 245 GLU 245 234 234 GLU GLU B . n 
B 1 246 HIS 246 235 235 HIS HIS B . n 
B 1 247 GLY 247 236 236 GLY GLY B . n 
B 1 248 GLU 248 237 237 GLU GLU B . n 
B 1 249 GLY 249 238 238 GLY GLY B . n 
B 1 250 THR 250 239 239 THR THR B . n 
B 1 251 GLY 251 240 240 GLY GLY B . n 
B 1 252 GLU 252 241 241 GLU GLU B . n 
B 1 253 GLY 253 242 242 GLY GLY B . n 
B 1 254 PHE 254 243 243 PHE PHE B . n 
B 1 255 ASN 255 244 244 ASN ASN B . n 
B 1 256 ILE 256 245 245 ILE ILE B . n 
B 1 257 ASN 257 246 246 ASN ASN B . n 
B 1 258 TYR 258 247 247 TYR TYR B . n 
B 1 259 PRO 259 248 248 PRO PRO B . n 
B 1 260 LEU 260 249 249 LEU LEU B . n 
B 1 261 PRO 261 250 250 PRO PRO B . n 
B 1 262 ALA 262 251 251 ALA ALA B . n 
B 1 263 GLY 263 252 252 GLY GLY B . n 
B 1 264 SER 264 253 253 SER SER B . n 
B 1 265 ALA 265 254 254 ALA ALA B . n 
B 1 266 TRP 266 255 255 TRP TRP B . n 
B 1 267 ASP 267 256 256 ASP ASP B . n 
B 1 268 SER 268 257 257 SER SER B . n 
B 1 269 TRP 269 258 258 TRP TRP B . n 
B 1 270 GLY 270 259 259 GLY GLY B . n 
B 1 271 ALA 271 260 260 ALA ALA B . n 
B 1 272 ALA 272 261 261 ALA ALA B . n 
B 1 273 LEU 273 262 262 LEU LEU B . n 
B 1 274 ASP 274 263 263 ASP ASP B . n 
B 1 275 ASP 275 264 264 ASP ASP B . n 
B 1 276 ALA 276 265 265 ALA ALA B . n 
B 1 277 CYS 277 266 266 CYS CYS B . n 
B 1 278 LYS 278 267 267 LYS LYS B . n 
B 1 279 ARG 279 268 268 ARG ARG B . n 
B 1 280 ILE 280 269 269 ILE ILE B . n 
B 1 281 ASN 281 270 270 ASN ASN B . n 
B 1 282 ALA 282 271 271 ALA ALA B . n 
B 1 283 PHE 283 272 272 PHE PHE B . n 
B 1 284 ASP 284 273 273 ASP ASP B . n 
B 1 285 ALA 285 274 274 ALA ALA B . n 
B 1 286 GLU 286 275 275 GLU GLU B . n 
B 1 287 VAL 287 276 276 VAL VAL B . n 
B 1 288 VAL 288 277 277 VAL VAL B . n 
B 1 289 ILE 289 278 278 ILE ILE B . n 
B 1 290 VAL 290 279 279 VAL VAL B . n 
B 1 291 SER 291 280 280 SER SER B . n 
B 1 292 LEU 292 281 281 LEU LEU B . n 
B 1 293 GLY 293 282 282 GLY GLY B . n 
B 1 294 VAL 294 283 283 VAL VAL B . n 
B 1 295 ASP 295 284 284 ASP ASP B . n 
B 1 296 THR 296 285 285 THR THR B . n 
B 1 297 TYR 297 286 286 TYR TYR B . n 
B 1 298 LYS 298 287 287 LYS LYS B . n 
B 1 299 GLU 299 288 288 GLU GLU B . n 
B 1 300 ASP 300 289 289 ASP ASP B . n 
B 1 301 PRO 301 290 290 PRO PRO B . n 
B 1 302 ILE 302 291 291 ILE ILE B . n 
B 1 303 SER 303 292 292 SER SER B . n 
B 1 304 GLN 304 293 293 GLN GLN B . n 
B 1 305 PHE 305 294 294 PHE PHE B . n 
B 1 306 LYS 306 295 295 LYS LYS B . n 
B 1 307 LEU 307 296 296 LEU LEU B . n 
B 1 308 ASP 308 297 297 ASP ASP B . n 
B 1 309 SER 309 298 298 SER SER B . n 
B 1 310 PRO 310 299 299 PRO PRO B . n 
B 1 311 ASP 311 300 300 ASP ASP B . n 
B 1 312 TYR 312 301 301 TYR TYR B . n 
B 1 313 LEU 313 302 302 LEU LEU B . n 
B 1 314 SER 314 303 303 SER SER B . n 
B 1 315 MET 315 304 304 MET MET B . n 
B 1 316 GLY 316 305 305 GLY GLY B . n 
B 1 317 GLU 317 306 306 GLU GLU B . n 
B 1 318 ARG 318 307 307 ARG ARG B . n 
B 1 319 ILE 319 308 308 ILE ILE B . n 
B 1 320 ALA 320 309 309 ALA ALA B . n 
B 1 321 ALA 321 310 310 ALA ALA B . n 
B 1 322 MET 322 311 311 MET MET B . n 
B 1 323 GLY 323 312 312 GLY GLY B . n 
B 1 324 LEU 324 313 313 LEU LEU B . n 
B 1 325 PRO 325 314 314 PRO PRO B . n 
B 1 326 THR 326 315 315 THR THR B . n 
B 1 327 LEU 327 316 316 LEU LEU B . n 
B 1 328 PHE 328 317 317 PHE PHE B . n 
B 1 329 VAL 329 318 318 VAL VAL B . n 
B 1 330 MET 330 319 319 MET MET B . n 
B 1 331 GLU 331 320 320 GLU GLU B . n 
B 1 332 GLY 332 321 321 GLY GLY B . n 
B 1 333 GLY 333 322 322 GLY GLY B . n 
B 1 334 TYR 334 323 323 TYR TYR B . n 
B 1 335 ALA 335 324 324 ALA ALA B . n 
B 1 336 VAL 336 325 325 VAL VAL B . n 
B 1 337 GLU 337 326 326 GLU GLU B . n 
B 1 338 ALA 338 327 327 ALA ALA B . n 
B 1 339 ILE 339 328 328 ILE ILE B . n 
B 1 340 GLY 340 329 329 GLY GLY B . n 
B 1 341 VAL 341 330 330 VAL VAL B . n 
B 1 342 ASN 342 331 331 ASN ASN B . n 
B 1 343 ALA 343 332 332 ALA ALA B . n 
B 1 344 VAL 344 333 333 VAL VAL B . n 
B 1 345 ASN 345 334 334 ASN ASN B . n 
B 1 346 VAL 346 335 335 VAL VAL B . n 
B 1 347 LEU 347 336 336 LEU LEU B . n 
B 1 348 GLU 348 337 337 GLU GLU B . n 
B 1 349 GLY 349 338 338 GLY GLY B . n 
B 1 350 PHE 350 339 339 PHE PHE B . n 
B 1 351 GLU 351 340 340 GLU GLU B . n 
B 1 352 ASN 352 341 341 ASN ASN B . n 
B 1 353 VAL 353 342 342 VAL VAL B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_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 
C 2 PGE 1  401 402 PGE PGE A . 
D 3 K   1  402 1   K   K   A . 
E 3 K   1  403 4   K   K   A . 
F 3 K   1  404 6   K   K   A . 
G 4 ZN  1  405 1   ZN  ZN  A . 
H 5 CL  1  406 1   CL  CL  A . 
I 6 ACT 1  401 401 ACT ACT B . 
J 7 PEG 1  402 402 PEG PEG B . 
K 3 K   1  403 2   K   K   B . 
L 3 K   1  404 3   K   K   B . 
M 3 K   1  405 5   K   K   B . 
N 4 ZN  1  406 2   ZN  ZN  B . 
O 8 HOH 1  501 56  HOH HOH A . 
O 8 HOH 2  502 84  HOH HOH A . 
O 8 HOH 3  503 68  HOH HOH A . 
O 8 HOH 4  504 19  HOH HOH A . 
O 8 HOH 5  505 21  HOH HOH A . 
O 8 HOH 6  506 20  HOH HOH A . 
O 8 HOH 7  507 135 HOH HOH A . 
O 8 HOH 8  508 60  HOH HOH A . 
O 8 HOH 9  509 78  HOH HOH A . 
O 8 HOH 10 510 130 HOH HOH A . 
O 8 HOH 11 511 89  HOH HOH A . 
O 8 HOH 12 512 103 HOH HOH A . 
O 8 HOH 13 513 137 HOH HOH A . 
O 8 HOH 14 514 8   HOH HOH A . 
O 8 HOH 15 515 146 HOH HOH A . 
O 8 HOH 16 516 3   HOH HOH A . 
O 8 HOH 17 517 113 HOH HOH A . 
O 8 HOH 18 518 55  HOH HOH A . 
O 8 HOH 19 519 46  HOH HOH A . 
O 8 HOH 20 520 93  HOH HOH A . 
O 8 HOH 21 521 58  HOH HOH A . 
O 8 HOH 22 522 116 HOH HOH A . 
O 8 HOH 23 523 140 HOH HOH A . 
O 8 HOH 24 524 131 HOH HOH A . 
O 8 HOH 25 525 152 HOH HOH A . 
O 8 HOH 26 526 16  HOH HOH A . 
O 8 HOH 27 527 133 HOH HOH A . 
O 8 HOH 28 528 4   HOH HOH A . 
O 8 HOH 29 529 155 HOH HOH A . 
O 8 HOH 30 530 95  HOH HOH A . 
O 8 HOH 31 531 96  HOH HOH A . 
O 8 HOH 32 532 75  HOH HOH A . 
O 8 HOH 33 533 90  HOH HOH A . 
O 8 HOH 34 534 12  HOH HOH A . 
O 8 HOH 35 535 91  HOH HOH A . 
O 8 HOH 36 536 66  HOH HOH A . 
O 8 HOH 37 537 123 HOH HOH A . 
O 8 HOH 38 538 101 HOH HOH A . 
O 8 HOH 39 539 37  HOH HOH A . 
O 8 HOH 40 540 138 HOH HOH A . 
O 8 HOH 41 541 71  HOH HOH A . 
O 8 HOH 42 542 11  HOH HOH A . 
O 8 HOH 43 543 49  HOH HOH A . 
O 8 HOH 44 544 13  HOH HOH A . 
O 8 HOH 45 545 45  HOH HOH A . 
O 8 HOH 46 546 29  HOH HOH A . 
O 8 HOH 47 547 119 HOH HOH A . 
O 8 HOH 48 548 72  HOH HOH A . 
O 8 HOH 49 549 107 HOH HOH A . 
O 8 HOH 50 550 105 HOH HOH A . 
O 8 HOH 51 551 83  HOH HOH A . 
O 8 HOH 52 552 10  HOH HOH A . 
O 8 HOH 53 553 28  HOH HOH A . 
O 8 HOH 54 554 154 HOH HOH A . 
O 8 HOH 55 555 156 HOH HOH A . 
O 8 HOH 56 556 87  HOH HOH A . 
O 8 HOH 57 557 24  HOH HOH A . 
O 8 HOH 58 558 23  HOH HOH A . 
O 8 HOH 59 559 147 HOH HOH A . 
O 8 HOH 60 560 139 HOH HOH A . 
O 8 HOH 61 561 145 HOH HOH A . 
O 8 HOH 62 562 124 HOH HOH A . 
O 8 HOH 63 563 141 HOH HOH A . 
O 8 HOH 64 564 115 HOH HOH A . 
O 8 HOH 65 565 142 HOH HOH A . 
P 8 HOH 1  501 150 HOH HOH B . 
P 8 HOH 2  502 134 HOH HOH B . 
P 8 HOH 3  503 76  HOH HOH B . 
P 8 HOH 4  504 102 HOH HOH B . 
P 8 HOH 5  505 151 HOH HOH B . 
P 8 HOH 6  506 148 HOH HOH B . 
P 8 HOH 7  507 52  HOH HOH B . 
P 8 HOH 8  508 99  HOH HOH B . 
P 8 HOH 9  509 9   HOH HOH B . 
P 8 HOH 10 510 31  HOH HOH B . 
P 8 HOH 11 511 120 HOH HOH B . 
P 8 HOH 12 512 127 HOH HOH B . 
P 8 HOH 13 513 92  HOH HOH B . 
P 8 HOH 14 514 50  HOH HOH B . 
P 8 HOH 15 515 7   HOH HOH B . 
P 8 HOH 16 516 77  HOH HOH B . 
P 8 HOH 17 517 112 HOH HOH B . 
P 8 HOH 18 518 117 HOH HOH B . 
P 8 HOH 19 519 6   HOH HOH B . 
P 8 HOH 20 520 36  HOH HOH B . 
P 8 HOH 21 521 48  HOH HOH B . 
P 8 HOH 22 522 100 HOH HOH B . 
P 8 HOH 23 523 108 HOH HOH B . 
P 8 HOH 24 524 54  HOH HOH B . 
P 8 HOH 25 525 2   HOH HOH B . 
P 8 HOH 26 526 51  HOH HOH B . 
P 8 HOH 27 527 53  HOH HOH B . 
P 8 HOH 28 528 159 HOH HOH B . 
P 8 HOH 29 529 44  HOH HOH B . 
P 8 HOH 30 530 34  HOH HOH B . 
P 8 HOH 31 531 65  HOH HOH B . 
P 8 HOH 32 532 104 HOH HOH B . 
P 8 HOH 33 533 47  HOH HOH B . 
P 8 HOH 34 534 111 HOH HOH B . 
P 8 HOH 35 535 149 HOH HOH B . 
P 8 HOH 36 536 97  HOH HOH B . 
P 8 HOH 37 537 5   HOH HOH B . 
P 8 HOH 38 538 15  HOH HOH B . 
P 8 HOH 39 539 110 HOH HOH B . 
P 8 HOH 40 540 74  HOH HOH B . 
P 8 HOH 41 541 157 HOH HOH B . 
P 8 HOH 42 542 57  HOH HOH B . 
P 8 HOH 43 543 17  HOH HOH B . 
P 8 HOH 44 544 25  HOH HOH B . 
P 8 HOH 45 545 59  HOH HOH B . 
P 8 HOH 46 546 73  HOH HOH B . 
P 8 HOH 47 547 158 HOH HOH B . 
P 8 HOH 48 548 88  HOH HOH B . 
P 8 HOH 49 549 106 HOH HOH B . 
P 8 HOH 50 550 30  HOH HOH B . 
P 8 HOH 51 551 26  HOH HOH B . 
P 8 HOH 52 552 62  HOH HOH B . 
P 8 HOH 53 553 125 HOH HOH B . 
P 8 HOH 54 554 136 HOH HOH B . 
P 8 HOH 55 555 132 HOH HOH B . 
P 8 HOH 56 556 94  HOH HOH B . 
P 8 HOH 57 557 69  HOH HOH B . 
P 8 HOH 58 558 38  HOH HOH B . 
P 8 HOH 59 559 82  HOH HOH B . 
P 8 HOH 60 560 126 HOH HOH B . 
P 8 HOH 61 561 153 HOH HOH B . 
P 8 HOH 62 562 143 HOH HOH B . 
P 8 HOH 63 563 128 HOH HOH B . 
P 8 HOH 64 564 144 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A VAL -2 ? CG1 ? A VAL 9 CG1 
2 1 Y 1 A VAL -2 ? CG2 ? A VAL 9 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425                        1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Jan 10, 2022 (BUILT 20220220)' 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? 'Jan 10, 2022 (BUILT 20220220)' 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? v3.60.0                         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GKZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     147.342 
_cell.length_a_esd                 ? 
_cell.length_b                     48.858 
_cell.length_b_esd                 ? 
_cell.length_c                     82.249 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GKZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GKZ 
_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             1.91 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.67 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    
;0.1M sodium acetate pH 4.5 
20% (w/v) PEG3000
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979510 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979510 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GKZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.716 
_reflns.d_resolution_low                               73.671 
_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                                     16673 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.251 
_reflns.pdbx_Rpim_I_all                                0.081 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.237 
_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.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.Rmerge_I_obs                                  1.024 
_reflns_shell.d_res_high                                    2.716 
_reflns_shell.d_res_low                                     2.763 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.number_unique_obs                             795 
_reflns_shell.pdbx_CC_half                                  0.731 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_Rpim_I_all                               0.372 
_reflns_shell.pdbx_Rrim_I_all                               1.092 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_diffrn_id                                ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy                               8.6 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.percent_possible_obs                          ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GKZ 
_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                            2.72 
_refine.ls_d_res_low                             73.67 
_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                     16666 
_refine.ls_number_reflns_R_free                  833 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1595 
_refine.ls_R_factor_R_free                       0.2326 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1557 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.83 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4974 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             129 
_refine_hist.number_atoms_total               5133 
_refine_hist.d_res_high                       2.72 
_refine_hist.d_res_low                        73.67 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 5144 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.927 ? 6993 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.689 ? 707  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051 ? 728  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 931  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.72 2.89  . . 123 2585 100.00 . . . . 0.2163 . . . . . . . . . . . 0.2973 
'X-RAY DIFFRACTION' 2.89 3.11  . . 140 2582 100.00 . . . . 0.1989 . . . . . . . . . . . 0.3003 
'X-RAY DIFFRACTION' 3.11 3.42  . . 153 2592 100.00 . . . . 0.1793 . . . . . . . . . . . 0.2420 
'X-RAY DIFFRACTION' 3.42 3.92  . . 121 2632 100.00 . . . . 0.1429 . . . . . . . . . . . 0.2573 
'X-RAY DIFFRACTION' 3.92 4.93  . . 135 2667 100.00 . . . . 0.1196 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 4.94 73.67 . . 161 2775 100.00 . . . . 0.1504 . . . . . . . . . . . 0.1979 
# 
_struct.entry_id                     9GKZ 
_struct.title                        'Crystal Structure of Acetylpolyamine amidohydrolase (ApaH) from Pseudomonas sp. M30-35' 
_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        9GKZ 
_struct_keywords.text            'Acetylpolyamine amidohydrolase, Polyamine deacetylase, Deacetylase, Deacylase, 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
J N N 7 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 4 ? 
O N N 8 ? 
P N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1Y0KY79_9PSED 
_struct_ref.pdbx_db_accession          A0A1Y0KY79 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLTIYSDDHHLHHGSCELIDGKLMPCFEMPKRADHILQRVKDRNIGEIREPQDFGRDPIQRIHTAEYLNFFEGAWARWQE
QDGTGDLLPYTWPARTLSQRLPTSLHGQLGYYSFDAGAPITAGTWQAAYSAAQVALTAQHEITNGAHSAFALCRPPGHHA
ASDVMGGYCYLNNAAIAAQAFIDQGHKRVAILDVDYHHGNGTQSIFYSRSDVLFTSIHGDPKFEFPFFLGHADEHGEGTG
EGFNINYPLPAGSAWDSWGAALDDACKRINAFDAEVVIVSLGVDTYKEDPISQFKLDSPDYLSMGERIAAMGLPTLFVME
GGYAVEAIGVNAVNVLEGFENV
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GKZ A 12 ? 353 ? A0A1Y0KY79 1 ? 342 ? 1 342 
2 1 9GKZ B 12 ? 353 ? A0A1Y0KY79 1 ? 342 ? 1 342 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GKZ MET A 1  ? UNP A0A1Y0KY79 ? ? 'initiating methionine' -10 1  
1 9GKZ ALA A 2  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -9  2  
1 9GKZ HIS A 3  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -8  3  
1 9GKZ HIS A 4  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -7  4  
1 9GKZ HIS A 5  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -6  5  
1 9GKZ HIS A 6  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -5  6  
1 9GKZ HIS A 7  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -4  7  
1 9GKZ HIS A 8  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -3  8  
1 9GKZ VAL A 9  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -2  9  
1 9GKZ GLY A 10 ? UNP A0A1Y0KY79 ? ? 'expression tag'        -1  10 
1 9GKZ THR A 11 ? UNP A0A1Y0KY79 ? ? 'expression tag'        0   11 
2 9GKZ MET B 1  ? UNP A0A1Y0KY79 ? ? 'initiating methionine' -10 12 
2 9GKZ ALA B 2  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -9  13 
2 9GKZ HIS B 3  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -8  14 
2 9GKZ HIS B 4  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -7  15 
2 9GKZ HIS B 5  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -6  16 
2 9GKZ HIS B 6  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -5  17 
2 9GKZ HIS B 7  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -4  18 
2 9GKZ HIS B 8  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -3  19 
2 9GKZ VAL B 9  ? UNP A0A1Y0KY79 ? ? 'expression tag'        -2  20 
2 9GKZ GLY B 10 ? UNP A0A1Y0KY79 ? ? 'expression tag'        -1  21 
2 9GKZ THR B 11 ? UNP A0A1Y0KY79 ? ? 'expression tag'        0   22 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5790  ? 
1 MORE         -107  ? 
1 'SSA (A^2)'  22600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ARG A 43  ? ARG A 54  ? ARG A 32  ARG A 43  1 ? 12 
HELX_P HELX_P2  AA2 ARG A 67  ? ARG A 72  ? ARG A 56  ARG A 61  1 ? 6  
HELX_P HELX_P3  AA3 THR A 75  ? GLU A 91  ? THR A 64  GLU A 80  1 ? 17 
HELX_P HELX_P4  AA4 SER A 115 ? TYR A 123 ? SER A 104 TYR A 112 1 ? 9  
HELX_P HELX_P5  AA5 GLY A 134 ? ASN A 155 ? GLY A 123 ASN A 144 1 ? 22 
HELX_P HELX_P6  AA6 ASN A 183 ? GLN A 195 ? ASN A 172 GLN A 184 1 ? 13 
HELX_P HELX_P7  AA7 GLY A 210 ? TYR A 218 ? GLY A 199 TYR A 207 1 ? 9  
HELX_P HELX_P8  AA8 GLU A 248 ? GLU A 252 ? GLU A 237 GLU A 241 5 ? 5  
HELX_P HELX_P9  AA9 ALA A 265 ? PHE A 283 ? ALA A 254 PHE A 272 1 ? 19 
HELX_P HELX_P10 AB1 ASP A 308 ? ALA A 321 ? ASP A 297 ALA A 310 1 ? 14 
HELX_P HELX_P11 AB2 ALA A 338 ? VAL A 353 ? ALA A 327 VAL A 342 1 ? 16 
HELX_P HELX_P12 AB3 ARG B 43  ? ARG B 54  ? ARG B 32  ARG B 43  1 ? 12 
HELX_P HELX_P13 AB4 GLY B 66  ? ARG B 72  ? GLY B 55  ARG B 61  1 ? 7  
HELX_P HELX_P14 AB5 THR B 75  ? GLN B 92  ? THR B 64  GLN B 81  1 ? 18 
HELX_P HELX_P15 AB6 SER B 115 ? TYR B 123 ? SER B 104 TYR B 112 1 ? 9  
HELX_P HELX_P16 AB7 GLY B 134 ? ASN B 155 ? GLY B 123 ASN B 144 1 ? 22 
HELX_P HELX_P17 AB8 ASN B 183 ? GLN B 195 ? ASN B 172 GLN B 184 1 ? 13 
HELX_P HELX_P18 AB9 GLY B 210 ? PHE B 217 ? GLY B 199 PHE B 206 1 ? 8  
HELX_P HELX_P19 AC1 GLU B 248 ? GLU B 252 ? GLU B 237 GLU B 241 5 ? 5  
HELX_P HELX_P20 AC2 ALA B 265 ? PHE B 283 ? ALA B 254 PHE B 272 1 ? 19 
HELX_P HELX_P21 AC3 ASP B 308 ? MET B 322 ? ASP B 297 MET B 311 1 ? 15 
HELX_P HELX_P22 AC4 ALA B 338 ? ASN B 352 ? ALA B 327 ASN B 341 1 ? 15 
# 
_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 PRO 167 O   ? ? ? 1_555 E K   . K  ? ? A PRO 156 A K   403 1_555 ? ? ? ? ? ? ? 2.969 ? ? 
metalc2  metalc ? ? A LEU 182 O   ? ? ? 1_555 E K   . K  ? ? A LEU 171 A K   403 1_555 ? ? ? ? ? ? ? 3.426 ? ? 
metalc3  metalc ? ? A ASP 204 O   ? ? ? 1_555 D K   . K  ? ? A ASP 193 A K   402 1_555 ? ? ? ? ? ? ? 2.775 ? ? 
metalc4  metalc ? ? A ASP 204 OD1 ? ? ? 1_555 D K   . K  ? ? A ASP 193 A K   402 1_555 ? ? ? ? ? ? ? 2.699 ? ? 
metalc5  metalc ? ? A ASP 206 O   ? ? ? 1_555 D K   . K  ? ? A ASP 195 A K   402 1_555 ? ? ? ? ? ? ? 2.627 ? ? 
metalc6  metalc ? ? A ASP 206 OD1 ? ? ? 1_555 G ZN  . ZN ? ? A ASP 195 A ZN  405 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc7  metalc ? ? A HIS 208 O   ? ? ? 1_555 D K   . K  ? ? A HIS 197 A K   402 1_555 ? ? ? ? ? ? ? 2.769 ? ? 
metalc8  metalc ? ? A HIS 208 ND1 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 197 A ZN  405 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc9  metalc ? ? A PHE 217 O   ? ? ? 1_555 F K   . K  ? ? A PHE 206 A K   404 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc10 metalc ? ? A ARG 220 O   ? ? ? 1_555 F K   . K  ? ? A ARG 209 A K   404 1_555 ? ? ? ? ? ? ? 2.843 ? ? 
metalc11 metalc ? ? A VAL 223 O   ? ? ? 1_555 F K   . K  ? ? A VAL 212 A K   404 1_555 ? ? ? ? ? ? ? 2.693 ? ? 
metalc12 metalc ? ? A SER 227 OG  ? ? ? 1_555 D K   . K  ? ? A SER 216 A K   402 1_555 ? ? ? ? ? ? ? 2.853 ? ? 
metalc13 metalc ? ? A ILE 228 O   ? ? ? 1_555 D K   . K  ? ? A ILE 217 A K   402 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc14 metalc ? ? A PHE 254 O   ? ? ? 1_555 F K   . K  ? ? A PHE 243 A K   404 1_555 ? ? ? ? ? ? ? 3.083 ? ? 
metalc15 metalc ? ? A ASP 295 OD2 ? ? ? 1_555 G ZN  . ZN ? ? A ASP 284 A ZN  405 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc16 metalc ? ? E K   .   K   ? ? ? 1_555 O HOH . O  ? ? A K   403 A HOH 521 1_555 ? ? ? ? ? ? ? 3.081 ? ? 
metalc17 metalc ? ? F K   .   K   ? ? ? 1_555 O HOH . O  ? ? A K   404 A HOH 519 1_555 ? ? ? ? ? ? ? 2.791 ? ? 
metalc18 metalc ? ? F K   .   K   ? ? ? 1_555 O HOH . O  ? ? A K   404 A HOH 526 1_555 ? ? ? ? ? ? ? 3.351 ? ? 
metalc19 metalc ? ? B ASP 204 O   ? ? ? 1_555 K K   . K  ? ? B ASP 193 B K   403 1_555 ? ? ? ? ? ? ? 2.692 ? ? 
metalc20 metalc ? ? B ASP 204 OD1 ? ? ? 1_555 K K   . K  ? ? B ASP 193 B K   403 1_555 ? ? ? ? ? ? ? 2.575 ? ? 
metalc21 metalc ? ? B ASP 204 OD2 ? ? ? 1_555 M K   . K  ? ? B ASP 193 B K   405 1_555 ? ? ? ? ? ? ? 2.714 ? ? 
metalc22 metalc ? ? B ASP 206 O   ? ? ? 1_555 K K   . K  ? ? B ASP 195 B K   403 1_555 ? ? ? ? ? ? ? 2.669 ? ? 
metalc23 metalc ? ? B ASP 206 OD2 ? ? ? 1_555 N ZN  . ZN ? ? B ASP 195 B ZN  406 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
metalc24 metalc ? ? B HIS 208 O   ? ? ? 1_555 K K   . K  ? ? B HIS 197 B K   403 1_555 ? ? ? ? ? ? ? 2.743 ? ? 
metalc25 metalc ? ? B HIS 208 ND1 ? ? ? 1_555 N ZN  . ZN ? ? B HIS 197 B ZN  406 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc26 metalc ? ? B THR 213 OG1 ? ? ? 1_555 M K   . K  ? ? B THR 202 B K   405 1_555 ? ? ? ? ? ? ? 3.018 ? ? 
metalc27 metalc ? ? B PHE 217 O   ? ? ? 1_555 L K   . K  ? ? B PHE 206 B K   404 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc28 metalc ? ? B ARG 220 O   ? ? ? 1_555 L K   . K  ? ? B ARG 209 B K   404 1_555 ? ? ? ? ? ? ? 2.760 ? ? 
metalc29 metalc ? ? B VAL 223 O   ? ? ? 1_555 L K   . K  ? ? B VAL 212 B K   404 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc30 metalc ? ? B SER 227 OG  ? ? ? 1_555 K K   . K  ? ? B SER 216 B K   403 1_555 ? ? ? ? ? ? ? 2.744 ? ? 
metalc31 metalc ? ? B ILE 228 O   ? ? ? 1_555 K K   . K  ? ? B ILE 217 B K   403 1_555 ? ? ? ? ? ? ? 2.817 ? ? 
metalc32 metalc ? ? B PHE 254 O   ? ? ? 1_555 L K   . K  ? ? B PHE 243 B K   404 1_555 ? ? ? ? ? ? ? 3.148 ? ? 
metalc33 metalc ? ? B SER 291 OG  ? ? ? 1_555 M K   . K  ? ? B SER 280 B K   405 1_555 ? ? ? ? ? ? ? 3.018 ? ? 
metalc34 metalc ? ? B ASP 295 OD2 ? ? ? 1_555 N ZN  . ZN ? ? B ASP 284 B ZN  406 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc35 metalc ? ? I ACT .   O   ? ? ? 1_555 N ZN  . ZN ? ? B ACT 401 B ZN  406 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc36 metalc ? ? L K   .   K   ? ? ? 1_555 P HOH . O  ? ? B K   404 B HOH 509 1_555 ? ? ? ? ? ? ? 3.203 ? ? 
metalc37 metalc ? ? L K   .   K   ? ? ? 1_555 P HOH . O  ? ? B K   404 B HOH 529 1_555 ? ? ? ? ? ? ? 2.593 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A PRO 167 ? A PRO 156 ? 1_555 K  ? E K  . ? A K  403 ? 1_555 O   ? A LEU 182 ? A LEU 171 ? 1_555 79.4  ? 
2  O   ? A PRO 167 ? A PRO 156 ? 1_555 K  ? E K  . ? A K  403 ? 1_555 O   ? O HOH .   ? A HOH 521 ? 1_555 111.4 ? 
3  O   ? A LEU 182 ? A LEU 171 ? 1_555 K  ? E K  . ? A K  403 ? 1_555 O   ? O HOH .   ? A HOH 521 ? 1_555 68.2  ? 
4  O   ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 OD1 ? A ASP 204 ? A ASP 193 ? 1_555 67.4  ? 
5  O   ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ASP 206 ? A ASP 195 ? 1_555 101.4 ? 
6  OD1 ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ASP 206 ? A ASP 195 ? 1_555 100.2 ? 
7  O   ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A HIS 208 ? A HIS 197 ? 1_555 157.7 ? 
8  OD1 ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A HIS 208 ? A HIS 197 ? 1_555 90.4  ? 
9  O   ? A ASP 206 ? A ASP 195 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A HIS 208 ? A HIS 197 ? 1_555 79.8  ? 
10 O   ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 OG  ? A SER 227 ? A SER 216 ? 1_555 86.8  ? 
11 OD1 ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 OG  ? A SER 227 ? A SER 216 ? 1_555 102.1 ? 
12 O   ? A ASP 206 ? A ASP 195 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 OG  ? A SER 227 ? A SER 216 ? 1_555 157.7 ? 
13 O   ? A HIS 208 ? A HIS 197 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 OG  ? A SER 227 ? A SER 216 ? 1_555 100.4 ? 
14 O   ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ILE 228 ? A ILE 217 ? 1_555 81.1  ? 
15 OD1 ? A ASP 204 ? A ASP 193 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ILE 228 ? A ILE 217 ? 1_555 139.7 ? 
16 O   ? A ASP 206 ? A ASP 195 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ILE 228 ? A ILE 217 ? 1_555 61.0  ? 
17 O   ? A HIS 208 ? A HIS 197 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ILE 228 ? A ILE 217 ? 1_555 117.6 ? 
18 OG  ? A SER 227 ? A SER 216 ? 1_555 K  ? D K  . ? A K  402 ? 1_555 O   ? A ILE 228 ? A ILE 217 ? 1_555 100.5 ? 
19 OD1 ? A ASP 206 ? A ASP 195 ? 1_555 ZN ? G ZN . ? A ZN 405 ? 1_555 ND1 ? A HIS 208 ? A HIS 197 ? 1_555 107.3 ? 
20 OD1 ? A ASP 206 ? A ASP 195 ? 1_555 ZN ? G ZN . ? A ZN 405 ? 1_555 OD2 ? A ASP 295 ? A ASP 284 ? 1_555 100.3 ? 
21 ND1 ? A HIS 208 ? A HIS 197 ? 1_555 ZN ? G ZN . ? A ZN 405 ? 1_555 OD2 ? A ASP 295 ? A ASP 284 ? 1_555 87.4  ? 
22 O   ? A PHE 217 ? A PHE 206 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A ARG 220 ? A ARG 209 ? 1_555 82.6  ? 
23 O   ? A PHE 217 ? A PHE 206 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A VAL 223 ? A VAL 212 ? 1_555 121.4 ? 
24 O   ? A ARG 220 ? A ARG 209 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A VAL 223 ? A VAL 212 ? 1_555 89.0  ? 
25 O   ? A PHE 217 ? A PHE 206 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A PHE 254 ? A PHE 243 ? 1_555 150.5 ? 
26 O   ? A ARG 220 ? A ARG 209 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A PHE 254 ? A PHE 243 ? 1_555 114.3 ? 
27 O   ? A VAL 223 ? A VAL 212 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? A PHE 254 ? A PHE 243 ? 1_555 84.4  ? 
28 O   ? A PHE 217 ? A PHE 206 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 519 ? 1_555 83.3  ? 
29 O   ? A ARG 220 ? A ARG 209 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 519 ? 1_555 86.7  ? 
30 O   ? A VAL 223 ? A VAL 212 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 519 ? 1_555 154.2 ? 
31 O   ? A PHE 254 ? A PHE 243 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 519 ? 1_555 74.3  ? 
32 O   ? A PHE 217 ? A PHE 206 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 526 ? 1_555 71.3  ? 
33 O   ? A ARG 220 ? A ARG 209 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 526 ? 1_555 148.5 ? 
34 O   ? A VAL 223 ? A VAL 212 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 526 ? 1_555 119.4 ? 
35 O   ? A PHE 254 ? A PHE 243 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 526 ? 1_555 83.9  ? 
36 O   ? O HOH .   ? A HOH 519 ? 1_555 K  ? F K  . ? A K  404 ? 1_555 O   ? O HOH .   ? A HOH 526 ? 1_555 73.1  ? 
37 O   ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 OD1 ? B ASP 204 ? B ASP 193 ? 1_555 72.4  ? 
38 O   ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ASP 206 ? B ASP 195 ? 1_555 100.2 ? 
39 OD1 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ASP 206 ? B ASP 195 ? 1_555 103.1 ? 
40 O   ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B HIS 208 ? B HIS 197 ? 1_555 159.6 ? 
41 OD1 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B HIS 208 ? B HIS 197 ? 1_555 87.2  ? 
42 O   ? B ASP 206 ? B ASP 195 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B HIS 208 ? B HIS 197 ? 1_555 83.7  ? 
43 O   ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 OG  ? B SER 227 ? B SER 216 ? 1_555 81.1  ? 
44 OD1 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 OG  ? B SER 227 ? B SER 216 ? 1_555 98.2  ? 
45 O   ? B ASP 206 ? B ASP 195 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 OG  ? B SER 227 ? B SER 216 ? 1_555 158.0 ? 
46 O   ? B HIS 208 ? B HIS 197 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 OG  ? B SER 227 ? B SER 216 ? 1_555 102.9 ? 
47 O   ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ILE 228 ? B ILE 217 ? 1_555 80.9  ? 
48 OD1 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ILE 228 ? B ILE 217 ? 1_555 147.2 ? 
49 O   ? B ASP 206 ? B ASP 195 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ILE 228 ? B ILE 217 ? 1_555 62.9  ? 
50 O   ? B HIS 208 ? B HIS 197 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ILE 228 ? B ILE 217 ? 1_555 118.1 ? 
51 OG  ? B SER 227 ? B SER 216 ? 1_555 K  ? K K  . ? B K  403 ? 1_555 O   ? B ILE 228 ? B ILE 217 ? 1_555 96.0  ? 
52 OD2 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? M K  . ? B K  405 ? 1_555 OG1 ? B THR 213 ? B THR 202 ? 1_555 121.8 ? 
53 OD2 ? B ASP 204 ? B ASP 193 ? 1_555 K  ? M K  . ? B K  405 ? 1_555 OG  ? B SER 291 ? B SER 280 ? 1_555 100.6 ? 
54 OG1 ? B THR 213 ? B THR 202 ? 1_555 K  ? M K  . ? B K  405 ? 1_555 OG  ? B SER 291 ? B SER 280 ? 1_555 122.2 ? 
55 OD2 ? B ASP 206 ? B ASP 195 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 ND1 ? B HIS 208 ? B HIS 197 ? 1_555 104.2 ? 
56 OD2 ? B ASP 206 ? B ASP 195 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 OD2 ? B ASP 295 ? B ASP 284 ? 1_555 104.9 ? 
57 ND1 ? B HIS 208 ? B HIS 197 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 OD2 ? B ASP 295 ? B ASP 284 ? 1_555 87.0  ? 
58 OD2 ? B ASP 206 ? B ASP 195 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 O   ? I ACT .   ? B ACT 401 ? 1_555 89.1  ? 
59 ND1 ? B HIS 208 ? B HIS 197 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 O   ? I ACT .   ? B ACT 401 ? 1_555 101.7 ? 
60 OD2 ? B ASP 295 ? B ASP 284 ? 1_555 ZN ? N ZN . ? B ZN 406 ? 1_555 O   ? I ACT .   ? B ACT 401 ? 1_555 161.3 ? 
61 O   ? B PHE 217 ? B PHE 206 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B ARG 220 ? B ARG 209 ? 1_555 81.3  ? 
62 O   ? B PHE 217 ? B PHE 206 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B VAL 223 ? B VAL 212 ? 1_555 109.7 ? 
63 O   ? B ARG 220 ? B ARG 209 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B VAL 223 ? B VAL 212 ? 1_555 86.8  ? 
64 O   ? B PHE 217 ? B PHE 206 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B PHE 254 ? B PHE 243 ? 1_555 161.4 ? 
65 O   ? B ARG 220 ? B ARG 209 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B PHE 254 ? B PHE 243 ? 1_555 110.2 ? 
66 O   ? B VAL 223 ? B VAL 212 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? B PHE 254 ? B PHE 243 ? 1_555 86.1  ? 
67 O   ? B PHE 217 ? B PHE 206 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 509 ? 1_555 65.2  ? 
68 O   ? B ARG 220 ? B ARG 209 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 509 ? 1_555 142.2 ? 
69 O   ? B VAL 223 ? B VAL 212 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 509 ? 1_555 119.8 ? 
70 O   ? B PHE 254 ? B PHE 243 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 509 ? 1_555 98.8  ? 
71 O   ? B PHE 217 ? B PHE 206 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 529 ? 1_555 88.9  ? 
72 O   ? B ARG 220 ? B ARG 209 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 529 ? 1_555 85.6  ? 
73 O   ? B VAL 223 ? B VAL 212 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 529 ? 1_555 158.6 ? 
74 O   ? B PHE 254 ? B PHE 243 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 529 ? 1_555 77.9  ? 
75 O   ? P HOH .   ? B HOH 509 ? 1_555 K  ? L K  . ? B K  404 ? 1_555 O   ? P HOH .   ? B HOH 529 ? 1_555 77.2  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ARG 165 A . ? ARG 154 A PRO 166 A ? PRO 155 A 1 0.18  
2 PHE 236 A . ? PHE 225 A PRO 237 A ? PRO 226 A 1 5.88  
3 ARG 165 B . ? ARG 154 B PRO 166 B ? PRO 155 B 1 -4.60 
4 PHE 236 B . ? PHE 225 B PRO 237 B ? PRO 226 B 1 15.65 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 59  ? ARG A 60  ? ILE A 48  ARG A 49  
AA1 2 LEU A 13  ? ILE A 15  ? LEU A 2   ILE A 4   
AA1 3 SER A 159 ? ALA A 162 ? SER A 148 ALA A 151 
AA1 4 THR A 326 ? MET A 330 ? THR A 315 MET A 319 
AA1 5 VAL A 288 ? LEU A 292 ? VAL A 277 LEU A 281 
AA1 6 VAL A 200 ? ASP A 204 ? VAL A 189 ASP A 193 
AA1 7 VAL A 223 ? GLY A 230 ? VAL A 212 GLY A 219 
AA1 8 ASN A 255 ? LEU A 260 ? ASN A 244 LEU A 249 
AA2 1 ILE B 59  ? ARG B 60  ? ILE B 48  ARG B 49  
AA2 2 LEU B 13  ? TYR B 16  ? LEU B 2   TYR B 5   
AA2 3 SER B 159 ? LEU B 163 ? SER B 148 LEU B 152 
AA2 4 THR B 326 ? MET B 330 ? THR B 315 MET B 319 
AA2 5 VAL B 287 ? LEU B 292 ? VAL B 276 LEU B 281 
AA2 6 VAL B 200 ? ASP B 204 ? VAL B 189 ASP B 193 
AA2 7 VAL B 223 ? GLY B 230 ? VAL B 212 GLY B 219 
AA2 8 ASN B 255 ? LEU B 260 ? ASN B 244 LEU B 249 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 60  ? O ARG A 49  N THR A 14  ? N THR A 3   
AA1 2 3 N ILE A 15  ? N ILE A 4   O PHE A 161 ? O PHE A 150 
AA1 3 4 N ALA A 162 ? N ALA A 151 O PHE A 328 ? O PHE A 317 
AA1 4 5 O LEU A 327 ? O LEU A 316 N VAL A 290 ? N VAL A 279 
AA1 5 6 O ILE A 289 ? O ILE A 278 N ALA A 201 ? N ALA A 190 
AA1 6 7 N ILE A 202 ? N ILE A 191 O LEU A 224 ? O LEU A 213 
AA1 7 8 N PHE A 225 ? N PHE A 214 O ILE A 256 ? O ILE A 245 
AA2 1 2 O ARG B 60  ? O ARG B 49  N THR B 14  ? N THR B 3   
AA2 2 3 N ILE B 15  ? N ILE B 4   O PHE B 161 ? O PHE B 150 
AA2 3 4 N ALA B 162 ? N ALA B 151 O PHE B 328 ? O PHE B 317 
AA2 4 5 O LEU B 327 ? O LEU B 316 N VAL B 290 ? N VAL B 279 
AA2 5 6 O ILE B 289 ? O ILE B 278 N ALA B 201 ? N ALA B 190 
AA2 6 7 N ILE B 202 ? N ILE B 191 O LEU B 224 ? O LEU B 213 
AA2 7 8 N SER B 227 ? N SER B 216 O TYR B 258 ? O TYR B 247 
# 
_pdbx_entry_details.entry_id                   9GKZ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 94  ? ? -94.35  -156.85 
2  1 THR A 96  ? ? 80.87   -3.21   
3  1 ALA A 118 ? ? -113.33 72.98   
4  1 THR A 121 ? ? -126.74 -165.15 
5  1 ASP A 163 ? ? -144.37 40.23   
6  1 PHE A 227 ? ? 71.41   -40.44  
7  1 TYR A 247 ? ? -118.49 77.71   
8  1 GLU A 320 ? ? -114.03 -121.89 
9  1 ALA A 324 ? ? -67.81  55.12   
10 1 SER B 6   ? ? -94.03  -106.68 
11 1 ASP B 82  ? ? 35.06   61.98   
12 1 ALA B 94  ? ? -88.93  -156.95 
13 1 THR B 96  ? ? 80.41   -3.94   
14 1 THR B 121 ? ? -129.91 -165.54 
15 1 PRO B 156 ? ? -68.16  -176.23 
16 1 ASP B 163 ? ? -145.22 41.40   
17 1 ASP B 195 ? ? -47.05  151.09  
18 1 PHE B 227 ? ? 74.79   -43.04  
19 1 ALA B 254 ? ? -120.65 -168.95 
20 1 GLU B 320 ? ? -125.38 -122.22 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     551 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   P 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -10 ? A MET 1  
2  1 Y 1 A ALA -9  ? A ALA 2  
3  1 Y 1 A HIS -8  ? A HIS 3  
4  1 Y 1 A HIS -7  ? A HIS 4  
5  1 Y 1 A HIS -6  ? A HIS 5  
6  1 Y 1 A HIS -5  ? A HIS 6  
7  1 Y 1 A HIS -4  ? A HIS 7  
8  1 Y 1 A HIS -3  ? A HIS 8  
9  1 Y 1 A ASP 7   ? A ASP 18 
10 1 Y 1 A ASP 8   ? A ASP 19 
11 1 Y 1 A HIS 9   ? A HIS 20 
12 1 Y 1 A HIS 10  ? A HIS 21 
13 1 Y 1 A LEU 11  ? A LEU 22 
14 1 Y 1 A HIS 12  ? A HIS 23 
15 1 Y 1 A HIS 13  ? A HIS 24 
16 1 Y 1 A GLY 14  ? A GLY 25 
17 1 Y 1 A SER 15  ? A SER 26 
18 1 Y 1 A CYS 16  ? A CYS 27 
19 1 Y 1 A GLU 17  ? A GLU 28 
20 1 Y 1 A LEU 18  ? A LEU 29 
21 1 Y 1 A ILE 19  ? A ILE 30 
22 1 Y 1 A ASP 20  ? A ASP 31 
23 1 Y 1 A GLY 21  ? A GLY 32 
24 1 Y 1 A LYS 22  ? A LYS 33 
25 1 Y 1 A LEU 23  ? A LEU 34 
26 1 Y 1 A MET 24  ? A MET 35 
27 1 Y 1 A PRO 25  ? A PRO 36 
28 1 Y 1 A CYS 26  ? A CYS 37 
29 1 Y 1 A PHE 27  ? A PHE 38 
30 1 Y 1 A GLU 28  ? A GLU 39 
31 1 Y 1 A MET 29  ? A MET 40 
32 1 Y 1 A PRO 30  ? A PRO 41 
33 1 Y 1 B MET -10 ? B MET 1  
34 1 Y 1 B ALA -9  ? B ALA 2  
35 1 Y 1 B HIS -8  ? B HIS 3  
36 1 Y 1 B HIS -7  ? B HIS 4  
37 1 Y 1 B HIS -6  ? B HIS 5  
38 1 Y 1 B HIS -5  ? B HIS 6  
39 1 Y 1 B HIS -4  ? B HIS 7  
40 1 Y 1 B HIS -3  ? B HIS 8  
41 1 Y 1 B VAL -2  ? B VAL 9  
42 1 Y 1 B ASP 8   ? B ASP 19 
43 1 Y 1 B HIS 9   ? B HIS 20 
44 1 Y 1 B HIS 10  ? B HIS 21 
45 1 Y 1 B LEU 11  ? B LEU 22 
46 1 Y 1 B HIS 12  ? B HIS 23 
47 1 Y 1 B HIS 13  ? B HIS 24 
48 1 Y 1 B GLY 14  ? B GLY 25 
49 1 Y 1 B SER 15  ? B SER 26 
50 1 Y 1 B CYS 16  ? B CYS 27 
51 1 Y 1 B GLU 17  ? B GLU 28 
52 1 Y 1 B LEU 18  ? B LEU 29 
53 1 Y 1 B ILE 19  ? B ILE 30 
54 1 Y 1 B ASP 20  ? B ASP 31 
55 1 Y 1 B GLY 21  ? B GLY 32 
56 1 Y 1 B LYS 22  ? B LYS 33 
57 1 Y 1 B LEU 23  ? B LEU 34 
58 1 Y 1 B MET 24  ? B MET 35 
59 1 Y 1 B PRO 25  ? B PRO 36 
60 1 Y 1 B CYS 26  ? B CYS 37 
61 1 Y 1 B PHE 27  ? B PHE 38 
62 1 Y 1 B GLU 28  ? B GLU 39 
63 1 Y 1 B MET 29  ? B MET 40 
64 1 Y 1 B PRO 30  ? B PRO 41 
# 
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 
ACT C    C  N N 1   
ACT O    O  N N 2   
ACT OXT  O  N N 3   
ACT CH3  C  N N 4   
ACT H1   H  N N 5   
ACT H2   H  N N 6   
ACT H3   H  N N 7   
ALA N    N  N N 8   
ALA CA   C  N S 9   
ALA C    C  N N 10  
ALA O    O  N N 11  
ALA CB   C  N N 12  
ALA OXT  O  N N 13  
ALA H    H  N N 14  
ALA H2   H  N N 15  
ALA HA   H  N N 16  
ALA HB1  H  N N 17  
ALA HB2  H  N N 18  
ALA HB3  H  N N 19  
ALA HXT  H  N N 20  
ARG N    N  N N 21  
ARG CA   C  N S 22  
ARG C    C  N N 23  
ARG O    O  N N 24  
ARG CB   C  N N 25  
ARG CG   C  N N 26  
ARG CD   C  N N 27  
ARG NE   N  N N 28  
ARG CZ   C  N N 29  
ARG NH1  N  N N 30  
ARG NH2  N  N N 31  
ARG OXT  O  N N 32  
ARG H    H  N N 33  
ARG H2   H  N N 34  
ARG HA   H  N N 35  
ARG HB2  H  N N 36  
ARG HB3  H  N N 37  
ARG HG2  H  N N 38  
ARG HG3  H  N N 39  
ARG HD2  H  N N 40  
ARG HD3  H  N N 41  
ARG HE   H  N N 42  
ARG HH11 H  N N 43  
ARG HH12 H  N N 44  
ARG HH21 H  N N 45  
ARG HH22 H  N N 46  
ARG HXT  H  N N 47  
ASN N    N  N N 48  
ASN CA   C  N S 49  
ASN C    C  N N 50  
ASN O    O  N N 51  
ASN CB   C  N N 52  
ASN CG   C  N N 53  
ASN OD1  O  N N 54  
ASN ND2  N  N N 55  
ASN OXT  O  N N 56  
ASN H    H  N N 57  
ASN H2   H  N N 58  
ASN HA   H  N N 59  
ASN HB2  H  N N 60  
ASN HB3  H  N N 61  
ASN HD21 H  N N 62  
ASN HD22 H  N N 63  
ASN HXT  H  N N 64  
ASP N    N  N N 65  
ASP CA   C  N S 66  
ASP C    C  N N 67  
ASP O    O  N N 68  
ASP CB   C  N N 69  
ASP CG   C  N N 70  
ASP OD1  O  N N 71  
ASP OD2  O  N N 72  
ASP OXT  O  N N 73  
ASP H    H  N N 74  
ASP H2   H  N N 75  
ASP HA   H  N N 76  
ASP HB2  H  N N 77  
ASP HB3  H  N N 78  
ASP HD2  H  N N 79  
ASP HXT  H  N N 80  
CL  CL   CL N N 81  
CYS N    N  N N 82  
CYS CA   C  N R 83  
CYS C    C  N N 84  
CYS O    O  N N 85  
CYS CB   C  N N 86  
CYS SG   S  N N 87  
CYS OXT  O  N N 88  
CYS H    H  N N 89  
CYS H2   H  N N 90  
CYS HA   H  N N 91  
CYS HB2  H  N N 92  
CYS HB3  H  N N 93  
CYS HG   H  N N 94  
CYS HXT  H  N N 95  
GLN N    N  N N 96  
GLN CA   C  N S 97  
GLN C    C  N N 98  
GLN O    O  N N 99  
GLN CB   C  N N 100 
GLN CG   C  N N 101 
GLN CD   C  N N 102 
GLN OE1  O  N N 103 
GLN NE2  N  N N 104 
GLN OXT  O  N N 105 
GLN H    H  N N 106 
GLN H2   H  N N 107 
GLN HA   H  N N 108 
GLN HB2  H  N N 109 
GLN HB3  H  N N 110 
GLN HG2  H  N N 111 
GLN HG3  H  N N 112 
GLN HE21 H  N N 113 
GLN HE22 H  N N 114 
GLN HXT  H  N N 115 
GLU N    N  N N 116 
GLU CA   C  N S 117 
GLU C    C  N N 118 
GLU O    O  N N 119 
GLU CB   C  N N 120 
GLU CG   C  N N 121 
GLU CD   C  N N 122 
GLU OE1  O  N N 123 
GLU OE2  O  N N 124 
GLU OXT  O  N N 125 
GLU H    H  N N 126 
GLU H2   H  N N 127 
GLU HA   H  N N 128 
GLU HB2  H  N N 129 
GLU HB3  H  N N 130 
GLU HG2  H  N N 131 
GLU HG3  H  N N 132 
GLU HE2  H  N N 133 
GLU HXT  H  N N 134 
GLY N    N  N N 135 
GLY CA   C  N N 136 
GLY C    C  N N 137 
GLY O    O  N N 138 
GLY OXT  O  N N 139 
GLY H    H  N N 140 
GLY H2   H  N N 141 
GLY HA2  H  N N 142 
GLY HA3  H  N N 143 
GLY HXT  H  N N 144 
HIS N    N  N N 145 
HIS CA   C  N S 146 
HIS C    C  N N 147 
HIS O    O  N N 148 
HIS CB   C  N N 149 
HIS CG   C  Y N 150 
HIS ND1  N  Y N 151 
HIS CD2  C  Y N 152 
HIS CE1  C  Y N 153 
HIS NE2  N  Y N 154 
HIS OXT  O  N N 155 
HIS H    H  N N 156 
HIS H2   H  N N 157 
HIS HA   H  N N 158 
HIS HB2  H  N N 159 
HIS HB3  H  N N 160 
HIS HD1  H  N N 161 
HIS HD2  H  N N 162 
HIS HE1  H  N N 163 
HIS HE2  H  N N 164 
HIS HXT  H  N N 165 
HOH O    O  N N 166 
HOH H1   H  N N 167 
HOH H2   H  N N 168 
ILE N    N  N N 169 
ILE CA   C  N S 170 
ILE C    C  N N 171 
ILE O    O  N N 172 
ILE CB   C  N S 173 
ILE CG1  C  N N 174 
ILE CG2  C  N N 175 
ILE CD1  C  N N 176 
ILE OXT  O  N N 177 
ILE H    H  N N 178 
ILE H2   H  N N 179 
ILE HA   H  N N 180 
ILE HB   H  N N 181 
ILE HG12 H  N N 182 
ILE HG13 H  N N 183 
ILE HG21 H  N N 184 
ILE HG22 H  N N 185 
ILE HG23 H  N N 186 
ILE HD11 H  N N 187 
ILE HD12 H  N N 188 
ILE HD13 H  N N 189 
ILE HXT  H  N N 190 
K   K    K  N N 191 
LEU N    N  N N 192 
LEU CA   C  N S 193 
LEU C    C  N N 194 
LEU O    O  N N 195 
LEU CB   C  N N 196 
LEU CG   C  N N 197 
LEU CD1  C  N N 198 
LEU CD2  C  N N 199 
LEU OXT  O  N N 200 
LEU H    H  N N 201 
LEU H2   H  N N 202 
LEU HA   H  N N 203 
LEU HB2  H  N N 204 
LEU HB3  H  N N 205 
LEU HG   H  N N 206 
LEU HD11 H  N N 207 
LEU HD12 H  N N 208 
LEU HD13 H  N N 209 
LEU HD21 H  N N 210 
LEU HD22 H  N N 211 
LEU HD23 H  N N 212 
LEU HXT  H  N N 213 
LYS N    N  N N 214 
LYS CA   C  N S 215 
LYS C    C  N N 216 
LYS O    O  N N 217 
LYS CB   C  N N 218 
LYS CG   C  N N 219 
LYS CD   C  N N 220 
LYS CE   C  N N 221 
LYS NZ   N  N N 222 
LYS OXT  O  N N 223 
LYS H    H  N N 224 
LYS H2   H  N N 225 
LYS HA   H  N N 226 
LYS HB2  H  N N 227 
LYS HB3  H  N N 228 
LYS HG2  H  N N 229 
LYS HG3  H  N N 230 
LYS HD2  H  N N 231 
LYS HD3  H  N N 232 
LYS HE2  H  N N 233 
LYS HE3  H  N N 234 
LYS HZ1  H  N N 235 
LYS HZ2  H  N N 236 
LYS HZ3  H  N N 237 
LYS HXT  H  N N 238 
MET N    N  N N 239 
MET CA   C  N S 240 
MET C    C  N N 241 
MET O    O  N N 242 
MET CB   C  N N 243 
MET CG   C  N N 244 
MET SD   S  N N 245 
MET CE   C  N N 246 
MET OXT  O  N N 247 
MET H    H  N N 248 
MET H2   H  N N 249 
MET HA   H  N N 250 
MET HB2  H  N N 251 
MET HB3  H  N N 252 
MET HG2  H  N N 253 
MET HG3  H  N N 254 
MET HE1  H  N N 255 
MET HE2  H  N N 256 
MET HE3  H  N N 257 
MET HXT  H  N N 258 
PEG C1   C  N N 259 
PEG O1   O  N N 260 
PEG C2   C  N N 261 
PEG O2   O  N N 262 
PEG C3   C  N N 263 
PEG C4   C  N N 264 
PEG O4   O  N N 265 
PEG H11  H  N N 266 
PEG H12  H  N N 267 
PEG HO1  H  N N 268 
PEG H21  H  N N 269 
PEG H22  H  N N 270 
PEG H31  H  N N 271 
PEG H32  H  N N 272 
PEG H41  H  N N 273 
PEG H42  H  N N 274 
PEG HO4  H  N N 275 
PGE C1   C  N N 276 
PGE O1   O  N N 277 
PGE C2   C  N N 278 
PGE O2   O  N N 279 
PGE C3   C  N N 280 
PGE C4   C  N N 281 
PGE O4   O  N N 282 
PGE C6   C  N N 283 
PGE C5   C  N N 284 
PGE O3   O  N N 285 
PGE H1   H  N N 286 
PGE H12  H  N N 287 
PGE HO1  H  N N 288 
PGE H2   H  N N 289 
PGE H22  H  N N 290 
PGE H3   H  N N 291 
PGE H32  H  N N 292 
PGE H4   H  N N 293 
PGE H42  H  N N 294 
PGE HO4  H  N N 295 
PGE H6   H  N N 296 
PGE H62  H  N N 297 
PGE H5   H  N N 298 
PGE H52  H  N N 299 
PHE N    N  N N 300 
PHE CA   C  N S 301 
PHE C    C  N N 302 
PHE O    O  N N 303 
PHE CB   C  N N 304 
PHE CG   C  Y N 305 
PHE CD1  C  Y N 306 
PHE CD2  C  Y N 307 
PHE CE1  C  Y N 308 
PHE CE2  C  Y N 309 
PHE CZ   C  Y N 310 
PHE OXT  O  N N 311 
PHE H    H  N N 312 
PHE H2   H  N N 313 
PHE HA   H  N N 314 
PHE HB2  H  N N 315 
PHE HB3  H  N N 316 
PHE HD1  H  N N 317 
PHE HD2  H  N N 318 
PHE HE1  H  N N 319 
PHE HE2  H  N N 320 
PHE HZ   H  N N 321 
PHE HXT  H  N N 322 
PRO N    N  N N 323 
PRO CA   C  N S 324 
PRO C    C  N N 325 
PRO O    O  N N 326 
PRO CB   C  N N 327 
PRO CG   C  N N 328 
PRO CD   C  N N 329 
PRO OXT  O  N N 330 
PRO H    H  N N 331 
PRO HA   H  N N 332 
PRO HB2  H  N N 333 
PRO HB3  H  N N 334 
PRO HG2  H  N N 335 
PRO HG3  H  N N 336 
PRO HD2  H  N N 337 
PRO HD3  H  N N 338 
PRO HXT  H  N N 339 
SER N    N  N N 340 
SER CA   C  N S 341 
SER C    C  N N 342 
SER O    O  N N 343 
SER CB   C  N N 344 
SER OG   O  N N 345 
SER OXT  O  N N 346 
SER H    H  N N 347 
SER H2   H  N N 348 
SER HA   H  N N 349 
SER HB2  H  N N 350 
SER HB3  H  N N 351 
SER HG   H  N N 352 
SER HXT  H  N N 353 
THR N    N  N N 354 
THR CA   C  N S 355 
THR C    C  N N 356 
THR O    O  N N 357 
THR CB   C  N R 358 
THR OG1  O  N N 359 
THR CG2  C  N N 360 
THR OXT  O  N N 361 
THR H    H  N N 362 
THR H2   H  N N 363 
THR HA   H  N N 364 
THR HB   H  N N 365 
THR HG1  H  N N 366 
THR HG21 H  N N 367 
THR HG22 H  N N 368 
THR HG23 H  N N 369 
THR HXT  H  N N 370 
TRP N    N  N N 371 
TRP CA   C  N S 372 
TRP C    C  N N 373 
TRP O    O  N N 374 
TRP CB   C  N N 375 
TRP CG   C  Y N 376 
TRP CD1  C  Y N 377 
TRP CD2  C  Y N 378 
TRP NE1  N  Y N 379 
TRP CE2  C  Y N 380 
TRP CE3  C  Y N 381 
TRP CZ2  C  Y N 382 
TRP CZ3  C  Y N 383 
TRP CH2  C  Y N 384 
TRP OXT  O  N N 385 
TRP H    H  N N 386 
TRP H2   H  N N 387 
TRP HA   H  N N 388 
TRP HB2  H  N N 389 
TRP HB3  H  N N 390 
TRP HD1  H  N N 391 
TRP HE1  H  N N 392 
TRP HE3  H  N N 393 
TRP HZ2  H  N N 394 
TRP HZ3  H  N N 395 
TRP HH2  H  N N 396 
TRP HXT  H  N N 397 
TYR N    N  N N 398 
TYR CA   C  N S 399 
TYR C    C  N N 400 
TYR O    O  N N 401 
TYR CB   C  N N 402 
TYR CG   C  Y N 403 
TYR CD1  C  Y N 404 
TYR CD2  C  Y N 405 
TYR CE1  C  Y N 406 
TYR CE2  C  Y N 407 
TYR CZ   C  Y N 408 
TYR OH   O  N N 409 
TYR OXT  O  N N 410 
TYR H    H  N N 411 
TYR H2   H  N N 412 
TYR HA   H  N N 413 
TYR HB2  H  N N 414 
TYR HB3  H  N N 415 
TYR HD1  H  N N 416 
TYR HD2  H  N N 417 
TYR HE1  H  N N 418 
TYR HE2  H  N N 419 
TYR HH   H  N N 420 
TYR HXT  H  N N 421 
VAL N    N  N N 422 
VAL CA   C  N S 423 
VAL C    C  N N 424 
VAL O    O  N N 425 
VAL CB   C  N N 426 
VAL CG1  C  N N 427 
VAL CG2  C  N N 428 
VAL OXT  O  N N 429 
VAL H    H  N N 430 
VAL H2   H  N N 431 
VAL HA   H  N N 432 
VAL HB   H  N N 433 
VAL HG11 H  N N 434 
VAL HG12 H  N N 435 
VAL HG13 H  N N 436 
VAL HG21 H  N N 437 
VAL HG22 H  N N 438 
VAL HG23 H  N N 439 
VAL HXT  H  N N 440 
ZN  ZN   ZN N N 441 
# 
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 
ACT C   O    doub N N 1   
ACT C   OXT  sing N N 2   
ACT C   CH3  sing N N 3   
ACT CH3 H1   sing N N 4   
ACT CH3 H2   sing N N 5   
ACT CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
HIS N   CA   sing N N 135 
HIS N   H    sing N N 136 
HIS N   H2   sing N N 137 
HIS CA  C    sing N N 138 
HIS CA  CB   sing N N 139 
HIS CA  HA   sing N N 140 
HIS C   O    doub N N 141 
HIS C   OXT  sing N N 142 
HIS CB  CG   sing N N 143 
HIS CB  HB2  sing N N 144 
HIS CB  HB3  sing N N 145 
HIS CG  ND1  sing Y N 146 
HIS CG  CD2  doub Y N 147 
HIS ND1 CE1  doub Y N 148 
HIS ND1 HD1  sing N N 149 
HIS CD2 NE2  sing Y N 150 
HIS CD2 HD2  sing N N 151 
HIS CE1 NE2  sing Y N 152 
HIS CE1 HE1  sing N N 153 
HIS NE2 HE2  sing N N 154 
HIS OXT HXT  sing N N 155 
HOH O   H1   sing N N 156 
HOH O   H2   sing N N 157 
ILE N   CA   sing N N 158 
ILE N   H    sing N N 159 
ILE N   H2   sing N N 160 
ILE CA  C    sing N N 161 
ILE CA  CB   sing N N 162 
ILE CA  HA   sing N N 163 
ILE C   O    doub N N 164 
ILE C   OXT  sing N N 165 
ILE CB  CG1  sing N N 166 
ILE CB  CG2  sing N N 167 
ILE CB  HB   sing N N 168 
ILE CG1 CD1  sing N N 169 
ILE CG1 HG12 sing N N 170 
ILE CG1 HG13 sing N N 171 
ILE CG2 HG21 sing N N 172 
ILE CG2 HG22 sing N N 173 
ILE CG2 HG23 sing N N 174 
ILE CD1 HD11 sing N N 175 
ILE CD1 HD12 sing N N 176 
ILE CD1 HD13 sing N N 177 
ILE OXT HXT  sing N N 178 
LEU N   CA   sing N N 179 
LEU N   H    sing N N 180 
LEU N   H2   sing N N 181 
LEU CA  C    sing N N 182 
LEU CA  CB   sing N N 183 
LEU CA  HA   sing N N 184 
LEU C   O    doub N N 185 
LEU C   OXT  sing N N 186 
LEU CB  CG   sing N N 187 
LEU CB  HB2  sing N N 188 
LEU CB  HB3  sing N N 189 
LEU CG  CD1  sing N N 190 
LEU CG  CD2  sing N N 191 
LEU CG  HG   sing N N 192 
LEU CD1 HD11 sing N N 193 
LEU CD1 HD12 sing N N 194 
LEU CD1 HD13 sing N N 195 
LEU CD2 HD21 sing N N 196 
LEU CD2 HD22 sing N N 197 
LEU CD2 HD23 sing N N 198 
LEU OXT HXT  sing N N 199 
LYS N   CA   sing N N 200 
LYS N   H    sing N N 201 
LYS N   H2   sing N N 202 
LYS CA  C    sing N N 203 
LYS CA  CB   sing N N 204 
LYS CA  HA   sing N N 205 
LYS C   O    doub N N 206 
LYS C   OXT  sing N N 207 
LYS CB  CG   sing N N 208 
LYS CB  HB2  sing N N 209 
LYS CB  HB3  sing N N 210 
LYS CG  CD   sing N N 211 
LYS CG  HG2  sing N N 212 
LYS CG  HG3  sing N N 213 
LYS CD  CE   sing N N 214 
LYS CD  HD2  sing N N 215 
LYS CD  HD3  sing N N 216 
LYS CE  NZ   sing N N 217 
LYS CE  HE2  sing N N 218 
LYS CE  HE3  sing N N 219 
LYS NZ  HZ1  sing N N 220 
LYS NZ  HZ2  sing N N 221 
LYS NZ  HZ3  sing N N 222 
LYS OXT HXT  sing N N 223 
MET N   CA   sing N N 224 
MET N   H    sing N N 225 
MET N   H2   sing N N 226 
MET CA  C    sing N N 227 
MET CA  CB   sing N N 228 
MET CA  HA   sing N N 229 
MET C   O    doub N N 230 
MET C   OXT  sing N N 231 
MET CB  CG   sing N N 232 
MET CB  HB2  sing N N 233 
MET CB  HB3  sing N N 234 
MET CG  SD   sing N N 235 
MET CG  HG2  sing N N 236 
MET CG  HG3  sing N N 237 
MET SD  CE   sing N N 238 
MET CE  HE1  sing N N 239 
MET CE  HE2  sing N N 240 
MET CE  HE3  sing N N 241 
MET OXT HXT  sing N N 242 
PEG C1  O1   sing N N 243 
PEG C1  C2   sing N N 244 
PEG C1  H11  sing N N 245 
PEG C1  H12  sing N N 246 
PEG O1  HO1  sing N N 247 
PEG C2  O2   sing N N 248 
PEG C2  H21  sing N N 249 
PEG C2  H22  sing N N 250 
PEG O2  C3   sing N N 251 
PEG C3  C4   sing N N 252 
PEG C3  H31  sing N N 253 
PEG C3  H32  sing N N 254 
PEG C4  O4   sing N N 255 
PEG C4  H41  sing N N 256 
PEG C4  H42  sing N N 257 
PEG O4  HO4  sing N N 258 
PGE C1  O1   sing N N 259 
PGE C1  C2   sing N N 260 
PGE C1  H1   sing N N 261 
PGE C1  H12  sing N N 262 
PGE O1  HO1  sing N N 263 
PGE C2  O2   sing N N 264 
PGE C2  H2   sing N N 265 
PGE C2  H22  sing N N 266 
PGE O2  C3   sing N N 267 
PGE C3  C4   sing N N 268 
PGE C3  H3   sing N N 269 
PGE C3  H32  sing N N 270 
PGE C4  O3   sing N N 271 
PGE C4  H4   sing N N 272 
PGE C4  H42  sing N N 273 
PGE O4  C6   sing N N 274 
PGE O4  HO4  sing N N 275 
PGE C6  C5   sing N N 276 
PGE C6  H6   sing N N 277 
PGE C6  H62  sing N N 278 
PGE C5  O3   sing N N 279 
PGE C5  H5   sing N N 280 
PGE C5  H52  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Research Foundation (DFG)' Germany LA2984/6-1 1 
'German Research Foundation (DFG)' Germany LA2984/8-1 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-A0A1Y0KY79-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GKZ 
_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]   0.006787 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020467 
_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]   0.012158 
_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 
K  
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   . VAL A 1 9   ? -17.690 13.150  -56.412 1.00 42.97 ? -2  VAL A N   1 
ATOM   2    C  CA  . VAL A 1 9   ? -18.367 14.132  -55.558 1.00 63.05 ? -2  VAL A CA  1 
ATOM   3    C  C   . VAL A 1 9   ? -17.419 14.668  -54.451 1.00 70.83 ? -2  VAL A C   1 
ATOM   4    O  O   . VAL A 1 9   ? -16.812 13.880  -53.721 1.00 67.62 ? -2  VAL A O   1 
ATOM   5    C  CB  . VAL A 1 9   ? -19.658 13.513  -54.940 1.00 35.36 ? -2  VAL A CB  1 
ATOM   6    N  N   . GLY A 1 10  ? -17.273 16.003  -54.354 1.00 69.00 ? -1  GLY A N   1 
ATOM   7    C  CA  . GLY A 1 10  ? -16.497 16.652  -53.290 1.00 55.94 ? -1  GLY A CA  1 
ATOM   8    C  C   . GLY A 1 10  ? -17.442 17.317  -52.297 1.00 55.27 ? -1  GLY A C   1 
ATOM   9    O  O   . GLY A 1 10  ? -17.254 18.471  -51.898 1.00 49.87 ? -1  GLY A O   1 
ATOM   10   N  N   . THR A 1 11  ? -18.451 16.566  -51.879 1.00 62.44 ? 0   THR A N   1 
ATOM   11   C  CA  . THR A 1 11  ? -19.674 17.109  -51.317 1.00 55.47 ? 0   THR A CA  1 
ATOM   12   C  C   . THR A 1 11  ? -19.816 16.894  -49.828 1.00 48.33 ? 0   THR A C   1 
ATOM   13   O  O   . THR A 1 11  ? -20.462 17.704  -49.168 1.00 66.18 ? 0   THR A O   1 
ATOM   14   C  CB  . THR A 1 11  ? -20.875 16.478  -52.022 1.00 54.96 ? 0   THR A CB  1 
ATOM   15   O  OG1 . THR A 1 11  ? -20.453 15.235  -52.595 1.00 55.96 ? 0   THR A OG1 1 
ATOM   16   C  CG2 . THR A 1 11  ? -21.380 17.382  -53.132 1.00 52.64 ? 0   THR A CG2 1 
ATOM   17   N  N   . MET A 1 12  ? -19.248 15.834  -49.280 1.00 38.48 ? 1   MET A N   1 
ATOM   18   C  CA  . MET A 1 12  ? -19.395 15.598  -47.855 1.00 36.95 ? 1   MET A CA  1 
ATOM   19   C  C   . MET A 1 12  ? -18.451 16.509  -47.070 1.00 34.65 ? 1   MET A C   1 
ATOM   20   O  O   . MET A 1 12  ? -17.285 16.673  -47.423 1.00 36.93 ? 1   MET A O   1 
ATOM   21   C  CB  . MET A 1 12  ? -19.138 14.127  -47.550 1.00 36.82 ? 1   MET A CB  1 
ATOM   22   C  CG  . MET A 1 12  ? -19.228 13.748  -46.103 1.00 33.37 ? 1   MET A CG  1 
ATOM   23   S  SD  . MET A 1 12  ? -19.128 11.978  -45.856 1.00 39.60 ? 1   MET A SD  1 
ATOM   24   C  CE  . MET A 1 12  ? -19.134 11.298  -47.515 1.00 34.92 ? 1   MET A CE  1 
ATOM   25   N  N   . LEU A 1 13  ? -18.969 17.111  -46.011 1.00 35.69 ? 2   LEU A N   1 
ATOM   26   C  CA  . LEU A 1 13  ? -18.236 18.045  -45.168 1.00 33.12 ? 2   LEU A CA  1 
ATOM   27   C  C   . LEU A 1 13  ? -17.766 17.327  -43.905 1.00 27.08 ? 2   LEU A C   1 
ATOM   28   O  O   . LEU A 1 13  ? -18.539 16.604  -43.277 1.00 30.53 ? 2   LEU A O   1 
ATOM   29   C  CB  . LEU A 1 13  ? -19.151 19.228  -44.822 1.00 29.04 ? 2   LEU A CB  1 
ATOM   30   C  CG  . LEU A 1 13  ? -18.697 20.490  -44.101 1.00 39.46 ? 2   LEU A CG  1 
ATOM   31   C  CD1 . LEU A 1 13  ? -17.450 21.048  -44.744 1.00 47.52 ? 2   LEU A CD1 1 
ATOM   32   C  CD2 . LEU A 1 13  ? -19.794 21.524  -44.134 1.00 36.53 ? 2   LEU A CD2 1 
ATOM   33   N  N   . THR A 1 14  ? -16.506 17.515  -43.538 1.00 31.36 ? 3   THR A N   1 
ATOM   34   C  CA  . THR A 1 14  ? -15.947 16.945  -42.315 1.00 34.39 ? 3   THR A CA  1 
ATOM   35   C  C   . THR A 1 14  ? -15.897 18.009  -41.221 1.00 36.35 ? 3   THR A C   1 
ATOM   36   O  O   . THR A 1 14  ? -15.529 19.157  -41.484 1.00 38.27 ? 3   THR A O   1 
ATOM   37   C  CB  . THR A 1 14  ? -14.530 16.403  -42.555 1.00 30.37 ? 3   THR A CB  1 
ATOM   38   O  OG1 . THR A 1 14  ? -14.554 15.404  -43.576 1.00 28.51 ? 3   THR A OG1 1 
ATOM   39   C  CG2 . THR A 1 14  ? -13.966 15.802  -41.291 1.00 28.24 ? 3   THR A CG2 1 
ATOM   40   N  N   . ILE A 1 15  ? -16.248 17.626  -39.991 1.00 31.87 ? 4   ILE A N   1 
ATOM   41   C  CA  . ILE A 1 15  ? -16.176 18.522  -38.840 1.00 33.65 ? 4   ILE A CA  1 
ATOM   42   C  C   . ILE A 1 15  ? -15.160 17.966  -37.850 1.00 31.00 ? 4   ILE A C   1 
ATOM   43   O  O   . ILE A 1 15  ? -15.229 16.789  -37.482 1.00 31.81 ? 4   ILE A O   1 
ATOM   44   C  CB  . ILE A 1 15  ? -17.550 18.718  -38.173 1.00 27.89 ? 4   ILE A CB  1 
ATOM   45   C  CG1 . ILE A 1 15  ? -18.545 19.190  -39.213 1.00 24.62 ? 4   ILE A CG1 1 
ATOM   46   C  CG2 . ILE A 1 15  ? -17.459 19.741  -37.052 1.00 23.96 ? 4   ILE A CG2 1 
ATOM   47   C  CD1 . ILE A 1 15  ? -18.057 20.383  -39.972 1.00 30.45 ? 4   ILE A CD1 1 
ATOM   48   N  N   . TYR A 1 16  ? -14.236 18.826  -37.408 1.00 34.53 ? 5   TYR A N   1 
ATOM   49   C  CA  . TYR A 1 16  ? -13.104 18.451  -36.571 1.00 33.80 ? 5   TYR A CA  1 
ATOM   50   C  C   . TYR A 1 16  ? -12.774 19.572  -35.589 1.00 38.02 ? 5   TYR A C   1 
ATOM   51   O  O   . TYR A 1 16  ? -12.822 20.752  -35.949 1.00 35.05 ? 5   TYR A O   1 
ATOM   52   C  CB  . TYR A 1 16  ? -11.859 18.148  -37.420 1.00 31.63 ? 5   TYR A CB  1 
ATOM   53   C  CG  . TYR A 1 16  ? -10.634 17.842  -36.575 1.00 46.20 ? 5   TYR A CG  1 
ATOM   54   C  CD1 . TYR A 1 16  ? -10.580 16.685  -35.794 1.00 44.00 ? 5   TYR A CD1 1 
ATOM   55   C  CD2 . TYR A 1 16  ? -9.545  18.716  -36.525 1.00 42.63 ? 5   TYR A CD2 1 
ATOM   56   C  CE1 . TYR A 1 16  ? -9.476  16.394  -35.001 1.00 43.70 ? 5   TYR A CE1 1 
ATOM   57   C  CE2 . TYR A 1 16  ? -8.431  18.429  -35.733 1.00 43.54 ? 5   TYR A CE2 1 
ATOM   58   C  CZ  . TYR A 1 16  ? -8.402  17.262  -34.974 1.00 48.72 ? 5   TYR A CZ  1 
ATOM   59   O  OH  . TYR A 1 16  ? -7.310  16.952  -34.180 1.00 51.99 ? 5   TYR A OH  1 
ATOM   60   N  N   . SER A 1 17  ? -12.408 19.196  -34.360 1.00 39.18 ? 6   SER A N   1 
ATOM   61   C  CA  . SER A 1 17  ? -11.818 20.139  -33.401 1.00 38.51 ? 6   SER A CA  1 
ATOM   62   C  C   . SER A 1 17  ? -10.323 19.965  -33.300 1.00 43.14 ? 6   SER A C   1 
ATOM   63   O  O   . SER A 1 17  ? -9.858  19.173  -32.479 1.00 49.07 ? 6   SER A O   1 
ATOM   64   C  CB  . SER A 1 17  ? -12.410 19.947  -32.026 1.00 35.98 ? 6   SER A CB  1 
ATOM   65   O  OG  . SER A 1 17  ? -13.788 19.700  -32.139 1.00 44.97 ? 6   SER A OG  1 
ATOM   66   N  N   . LYS A 1 42  ? -2.463  12.248  -33.349 1.00 66.86 ? 31  LYS A N   1 
ATOM   67   C  CA  . LYS A 1 42  ? -1.805  11.202  -34.125 1.00 67.87 ? 31  LYS A CA  1 
ATOM   68   C  C   . LYS A 1 42  ? -2.819  10.504  -35.029 1.00 69.59 ? 31  LYS A C   1 
ATOM   69   O  O   . LYS A 1 42  ? -2.538  10.182  -36.189 1.00 58.22 ? 31  LYS A O   1 
ATOM   70   C  CB  . LYS A 1 42  ? -1.116  10.177  -33.198 1.00 85.96 ? 31  LYS A CB  1 
ATOM   71   C  CG  . LYS A 1 42  ? -2.069  9.259   -32.390 1.00 81.28 ? 31  LYS A CG  1 
ATOM   72   C  CD  . LYS A 1 42  ? -1.322  8.201   -31.581 1.00 84.20 ? 31  LYS A CD  1 
ATOM   73   C  CE  . LYS A 1 42  ? -2.071  7.868   -30.299 1.00 97.02 ? 31  LYS A CE  1 
ATOM   74   N  NZ  . LYS A 1 42  ? -2.354  9.103   -29.511 1.00 96.70 ? 31  LYS A NZ  1 
ATOM   75   N  N   . ARG A 1 43  ? -4.014  10.287  -34.483 1.00 69.58 ? 32  ARG A N   1 
ATOM   76   C  CA  . ARG A 1 43  ? -4.991  9.406   -35.102 1.00 56.57 ? 32  ARG A CA  1 
ATOM   77   C  C   . ARG A 1 43  ? -5.918  10.167  -36.042 1.00 62.24 ? 32  ARG A C   1 
ATOM   78   O  O   . ARG A 1 43  ? -6.143  9.736   -37.180 1.00 56.62 ? 32  ARG A O   1 
ATOM   79   C  CB  . ARG A 1 43  ? -5.765  8.675   -34.004 1.00 62.36 ? 32  ARG A CB  1 
ATOM   80   C  CG  . ARG A 1 43  ? -6.954  7.862   -34.461 1.00 55.67 ? 32  ARG A CG  1 
ATOM   81   C  CD  . ARG A 1 43  ? -7.711  7.395   -33.244 1.00 58.97 ? 32  ARG A CD  1 
ATOM   82   N  NE  . ARG A 1 43  ? -8.889  6.599   -33.559 1.00 56.34 ? 32  ARG A NE  1 
ATOM   83   C  CZ  . ARG A 1 43  ? -10.126 7.079   -33.567 1.00 48.78 ? 32  ARG A CZ  1 
ATOM   84   N  NH1 . ARG A 1 43  ? -10.368 8.365   -33.364 1.00 41.19 ? 32  ARG A NH1 1 
ATOM   85   N  NH2 . ARG A 1 43  ? -11.144 6.244   -33.768 1.00 42.21 ? 32  ARG A NH2 1 
ATOM   86   N  N   . ALA A 1 44  ? -6.447  11.307  -35.581 1.00 72.20 ? 33  ALA A N   1 
ATOM   87   C  CA  . ALA A 1 44  ? -7.137  12.250  -36.448 1.00 46.08 ? 33  ALA A CA  1 
ATOM   88   C  C   . ALA A 1 44  ? -6.205  12.843  -37.485 1.00 49.76 ? 33  ALA A C   1 
ATOM   89   O  O   . ALA A 1 44  ? -6.674  13.423  -38.472 1.00 55.22 ? 33  ALA A O   1 
ATOM   90   C  CB  . ALA A 1 44  ? -7.771  13.362  -35.615 1.00 47.85 ? 33  ALA A CB  1 
ATOM   91   N  N   . ASP A 1 45  ? -4.900  12.712  -37.286 1.00 47.69 ? 34  ASP A N   1 
ATOM   92   C  CA  . ASP A 1 45  ? -3.955  13.060  -38.335 1.00 51.43 ? 34  ASP A CA  1 
ATOM   93   C  C   . ASP A 1 45  ? -4.214  12.233  -39.592 1.00 45.07 ? 34  ASP A C   1 
ATOM   94   O  O   . ASP A 1 45  ? -4.467  12.780  -40.672 1.00 39.08 ? 34  ASP A O   1 
ATOM   95   C  CB  . ASP A 1 45  ? -2.534  12.841  -37.820 1.00 62.42 ? 34  ASP A CB  1 
ATOM   96   C  CG  . ASP A 1 45  ? -1.645  14.036  -38.034 1.00 66.89 ? 34  ASP A CG  1 
ATOM   97   O  OD1 . ASP A 1 45  ? -0.558  14.090  -37.407 1.00 72.39 ? 34  ASP A OD1 1 
ATOM   98   O  OD2 . ASP A 1 45  ? -2.040  14.924  -38.820 1.00 81.16 ? 34  ASP A OD2 1 
ATOM   99   N  N   . HIS A 1 46  ? -4.172  10.898  -39.459 1.00 42.80 ? 35  HIS A N   1 
ATOM   100  C  CA  . HIS A 1 46  ? -4.298  10.021  -40.621 1.00 38.31 ? 35  HIS A CA  1 
ATOM   101  C  C   . HIS A 1 46  ? -5.660  10.160  -41.280 1.00 38.05 ? 35  HIS A C   1 
ATOM   102  O  O   . HIS A 1 46  ? -5.771  10.111  -42.510 1.00 32.82 ? 35  HIS A O   1 
ATOM   103  C  CB  . HIS A 1 46  ? -4.066  8.567   -40.217 1.00 48.65 ? 35  HIS A CB  1 
ATOM   104  C  CG  . HIS A 1 46  ? -2.634  8.230   -39.976 1.00 52.92 ? 35  HIS A CG  1 
ATOM   105  N  ND1 . HIS A 1 46  ? -1.977  8.574   -38.815 1.00 54.75 ? 35  HIS A ND1 1 
ATOM   106  C  CD2 . HIS A 1 46  ? -1.726  7.592   -40.750 1.00 55.37 ? 35  HIS A CD2 1 
ATOM   107  C  CE1 . HIS A 1 46  ? -0.724  8.162   -38.884 1.00 52.63 ? 35  HIS A CE1 1 
ATOM   108  N  NE2 . HIS A 1 46  ? -0.548  7.559   -40.046 1.00 54.32 ? 35  HIS A NE2 1 
ATOM   109  N  N   . ILE A 1 47  ? -6.712  10.306  -40.475 1.00 37.65 ? 36  ILE A N   1 
ATOM   110  C  CA  . ILE A 1 47  ? -8.045  10.486  -41.029 1.00 36.32 ? 36  ILE A CA  1 
ATOM   111  C  C   . ILE A 1 47  ? -8.117  11.800  -41.798 1.00 39.41 ? 36  ILE A C   1 
ATOM   112  O  O   . ILE A 1 47  ? -8.463  11.828  -42.986 1.00 40.53 ? 36  ILE A O   1 
ATOM   113  C  CB  . ILE A 1 47  ? -9.107  10.432  -39.920 1.00 42.40 ? 36  ILE A CB  1 
ATOM   114  C  CG1 . ILE A 1 47  ? -9.324  9.000   -39.432 1.00 39.08 ? 36  ILE A CG1 1 
ATOM   115  C  CG2 . ILE A 1 47  ? -10.423 10.996  -40.440 1.00 40.83 ? 36  ILE A CG2 1 
ATOM   116  C  CD1 . ILE A 1 47  ? -9.825  8.931   -38.029 1.00 30.23 ? 36  ILE A CD1 1 
ATOM   117  N  N   . LEU A 1 48  ? -7.778  12.912  -41.135 1.00 35.46 ? 37  LEU A N   1 
ATOM   118  C  CA  . LEU A 1 48  ? -7.920  14.213  -41.789 1.00 41.71 ? 37  LEU A CA  1 
ATOM   119  C  C   . LEU A 1 48  ? -7.041  14.322  -43.029 1.00 39.30 ? 37  LEU A C   1 
ATOM   120  O  O   . LEU A 1 48  ? -7.474  14.875  -44.049 1.00 34.12 ? 37  LEU A O   1 
ATOM   121  C  CB  . LEU A 1 48  ? -7.605  15.346  -40.819 1.00 44.34 ? 37  LEU A CB  1 
ATOM   122  C  CG  . LEU A 1 48  ? -8.751  15.646  -39.859 1.00 42.34 ? 37  LEU A CG  1 
ATOM   123  C  CD1 . LEU A 1 48  ? -8.242  16.512  -38.743 1.00 38.03 ? 37  LEU A CD1 1 
ATOM   124  C  CD2 . LEU A 1 48  ? -9.925  16.278  -40.584 1.00 31.42 ? 37  LEU A CD2 1 
ATOM   125  N  N   . GLN A 1 49  ? -5.809  13.797  -42.960 1.00 36.88 ? 38  GLN A N   1 
ATOM   126  C  CA  . GLN A 1 49  ? -4.923  13.789  -44.124 1.00 35.86 ? 38  GLN A CA  1 
ATOM   127  C  C   . GLN A 1 49  ? -5.578  13.074  -45.303 1.00 38.99 ? 38  GLN A C   1 
ATOM   128  O  O   . GLN A 1 49  ? -5.596  13.586  -46.430 1.00 34.32 ? 38  GLN A O   1 
ATOM   129  C  CB  . GLN A 1 49  ? -3.590  13.133  -43.752 1.00 36.14 ? 38  GLN A CB  1 
ATOM   130  C  CG  . GLN A 1 49  ? -2.452  13.256  -44.786 1.00 45.40 ? 38  GLN A CG  1 
ATOM   131  C  CD  . GLN A 1 49  ? -2.145  14.695  -45.215 1.00 52.73 ? 38  GLN A CD  1 
ATOM   132  O  OE1 . GLN A 1 49  ? -2.499  15.113  -46.321 1.00 54.56 ? 38  GLN A OE1 1 
ATOM   133  N  NE2 . GLN A 1 49  ? -1.467  15.448  -44.346 1.00 52.14 ? 38  GLN A NE2 1 
ATOM   134  N  N   . ARG A 1 50  ? -6.158  11.900  -45.050 1.00 37.76 ? 39  ARG A N   1 
ATOM   135  C  CA  . ARG A 1 50  ? -6.811  11.154  -46.115 1.00 34.94 ? 39  ARG A CA  1 
ATOM   136  C  C   . ARG A 1 50  ? -8.076  11.849  -46.622 1.00 34.35 ? 39  ARG A C   1 
ATOM   137  O  O   . ARG A 1 50  ? -8.439  11.671  -47.789 1.00 30.93 ? 39  ARG A O   1 
ATOM   138  C  CB  . ARG A 1 50  ? -7.122  9.747   -45.623 1.00 34.72 ? 39  ARG A CB  1 
ATOM   139  C  CG  . ARG A 1 50  ? -7.581  8.809   -46.716 1.00 40.35 ? 39  ARG A CG  1 
ATOM   140  C  CD  . ARG A 1 50  ? -6.434  8.065   -47.336 1.00 34.79 ? 39  ARG A CD  1 
ATOM   141  N  NE  . ARG A 1 50  ? -6.926  7.028   -48.229 1.00 37.45 ? 39  ARG A NE  1 
ATOM   142  C  CZ  . ARG A 1 50  ? -6.266  6.580   -49.286 1.00 40.85 ? 39  ARG A CZ  1 
ATOM   143  N  NH1 . ARG A 1 50  ? -5.065  7.044   -49.600 1.00 35.50 ? 39  ARG A NH1 1 
ATOM   144  N  NH2 . ARG A 1 50  ? -6.826  5.646   -50.049 1.00 47.73 ? 39  ARG A NH2 1 
ATOM   145  N  N   . VAL A 1 51  ? -8.744  12.653  -45.779 1.00 36.18 ? 40  VAL A N   1 
ATOM   146  C  CA  . VAL A 1 51  ? -9.924  13.406  -46.220 1.00 32.29 ? 40  VAL A CA  1 
ATOM   147  C  C   . VAL A 1 51  ? -9.543  14.445  -47.278 1.00 34.61 ? 40  VAL A C   1 
ATOM   148  O  O   . VAL A 1 51  ? -10.189 14.545  -48.331 1.00 33.33 ? 40  VAL A O   1 
ATOM   149  C  CB  . VAL A 1 51  ? -10.639 14.046  -45.013 1.00 30.73 ? 40  VAL A CB  1 
ATOM   150  C  CG1 . VAL A 1 51  ? -11.516 15.209  -45.441 1.00 26.86 ? 40  VAL A CG1 1 
ATOM   151  C  CG2 . VAL A 1 51  ? -11.478 13.019  -44.299 1.00 26.57 ? 40  VAL A CG2 1 
ATOM   152  N  N   . LYS A 1 52  ? -8.482  15.228  -47.027 1.00 34.83 ? 41  LYS A N   1 
ATOM   153  C  CA  . LYS A 1 52  ? -7.964  16.114  -48.074 1.00 37.30 ? 41  LYS A CA  1 
ATOM   154  C  C   . LYS A 1 52  ? -7.464  15.320  -49.283 1.00 41.60 ? 41  LYS A C   1 
ATOM   155  O  O   . LYS A 1 52  ? -7.913  15.547  -50.412 1.00 40.20 ? 41  LYS A O   1 
ATOM   156  C  CB  . LYS A 1 52  ? -6.852  17.018  -47.531 1.00 38.54 ? 41  LYS A CB  1 
ATOM   157  C  CG  . LYS A 1 52  ? -6.689  17.022  -46.020 1.00 45.31 ? 41  LYS A CG  1 
ATOM   158  C  CD  . LYS A 1 52  ? -5.921  18.258  -45.525 1.00 43.52 ? 41  LYS A CD  1 
ATOM   159  C  CE  . LYS A 1 52  ? -5.834  18.325  -43.989 1.00 43.56 ? 41  LYS A CE  1 
ATOM   160  N  NZ  . LYS A 1 52  ? -5.326  19.648  -43.482 1.00 45.95 ? 41  LYS A NZ  1 
ATOM   161  N  N   . ASP A 1 53  ? -6.552  14.363  -49.049 1.00 39.06 ? 42  ASP A N   1 
ATOM   162  C  CA  . ASP A 1 53  ? -5.929  13.576  -50.114 1.00 35.27 ? 42  ASP A CA  1 
ATOM   163  C  C   . ASP A 1 53  ? -6.950  12.969  -51.066 1.00 44.75 ? 42  ASP A C   1 
ATOM   164  O  O   . ASP A 1 53  ? -6.745  12.952  -52.285 1.00 44.25 ? 42  ASP A O   1 
ATOM   165  C  CB  . ASP A 1 53  ? -5.084  12.455  -49.504 1.00 40.24 ? 42  ASP A CB  1 
ATOM   166  C  CG  . ASP A 1 53  ? -3.677  12.903  -49.161 1.00 52.20 ? 42  ASP A CG  1 
ATOM   167  O  OD1 . ASP A 1 53  ? -3.448  14.138  -49.036 1.00 50.88 ? 42  ASP A OD1 1 
ATOM   168  O  OD2 . ASP A 1 53  ? -2.795  12.021  -49.028 1.00 57.49 ? 42  ASP A OD2 1 
ATOM   169  N  N   . ARG A 1 54  ? -8.041  12.430  -50.535 1.00 42.38 ? 43  ARG A N   1 
ATOM   170  C  CA  . ARG A 1 54  ? -9.054  11.820  -51.382 1.00 44.84 ? 43  ARG A CA  1 
ATOM   171  C  C   . ARG A 1 54  ? -10.196 12.774  -51.698 1.00 48.35 ? 43  ARG A C   1 
ATOM   172  O  O   . ARG A 1 54  ? -11.184 12.357  -52.318 1.00 43.51 ? 43  ARG A O   1 
ATOM   173  C  CB  . ARG A 1 54  ? -9.577  10.534  -50.742 1.00 41.83 ? 43  ARG A CB  1 
ATOM   174  C  CG  . ARG A 1 54  ? -8.471  9.537   -50.481 1.00 39.77 ? 43  ARG A CG  1 
ATOM   175  C  CD  . ARG A 1 54  ? -7.650  9.344   -51.740 1.00 42.09 ? 43  ARG A CD  1 
ATOM   176  N  NE  . ARG A 1 54  ? -8.376  8.596   -52.760 1.00 48.12 ? 43  ARG A NE  1 
ATOM   177  C  CZ  . ARG A 1 54  ? -7.804  7.919   -53.749 1.00 44.84 ? 43  ARG A CZ  1 
ATOM   178  N  NH1 . ARG A 1 54  ? -6.493  7.946   -53.939 1.00 40.43 ? 43  ARG A NH1 1 
ATOM   179  N  NH2 . ARG A 1 54  ? -8.567  7.190   -54.561 1.00 29.94 ? 43  ARG A NH2 1 
ATOM   180  N  N   . ASN A 1 55  ? -10.080 14.043  -51.284 1.00 46.91 ? 44  ASN A N   1 
ATOM   181  C  CA  . ASN A 1 55  ? -10.985 15.099  -51.735 1.00 50.00 ? 44  ASN A CA  1 
ATOM   182  C  C   . ASN A 1 55  ? -12.439 14.797  -51.344 1.00 46.06 ? 44  ASN A C   1 
ATOM   183  O  O   . ASN A 1 55  ? -13.382 15.068  -52.096 1.00 45.55 ? 44  ASN A O   1 
ATOM   184  C  CB  . ASN A 1 55  ? -10.823 15.314  -53.250 1.00 50.24 ? 44  ASN A CB  1 
ATOM   185  C  CG  . ASN A 1 55  ? -11.470 16.605  -53.756 1.00 67.19 ? 44  ASN A CG  1 
ATOM   186  O  OD1 . ASN A 1 55  ? -11.874 17.480  -52.975 1.00 73.68 ? 44  ASN A OD1 1 
ATOM   187  N  ND2 . ASN A 1 55  ? -11.568 16.726  -55.077 1.00 62.06 ? 44  ASN A ND2 1 
ATOM   188  N  N   . ILE A 1 56  ? -12.617 14.223  -50.147 1.00 40.85 ? 45  ILE A N   1 
ATOM   189  C  CA  . ILE A 1 56  ? -13.955 13.988  -49.605 1.00 36.11 ? 45  ILE A CA  1 
ATOM   190  C  C   . ILE A 1 56  ? -14.734 15.300  -49.547 1.00 41.95 ? 45  ILE A C   1 
ATOM   191  O  O   . ILE A 1 56  ? -15.869 15.404  -50.037 1.00 38.27 ? 45  ILE A O   1 
ATOM   192  C  CB  . ILE A 1 56  ? -13.854 13.323  -48.218 1.00 37.93 ? 45  ILE A CB  1 
ATOM   193  C  CG1 . ILE A 1 56  ? -13.333 11.871  -48.314 1.00 37.85 ? 45  ILE A CG1 1 
ATOM   194  C  CG2 . ILE A 1 56  ? -15.180 13.418  -47.453 1.00 33.14 ? 45  ILE A CG2 1 
ATOM   195  C  CD1 . ILE A 1 56  ? -13.756 11.097  -49.570 1.00 34.43 ? 45  ILE A CD1 1 
ATOM   196  N  N   . GLY A 1 57  ? -14.119 16.328  -48.978 1.00 39.07 ? 46  GLY A N   1 
ATOM   197  C  CA  . GLY A 1 57  ? -14.753 17.625  -48.893 1.00 38.06 ? 46  GLY A CA  1 
ATOM   198  C  C   . GLY A 1 57  ? -13.937 18.549  -48.012 1.00 41.84 ? 46  GLY A C   1 
ATOM   199  O  O   . GLY A 1 57  ? -12.775 18.271  -47.699 1.00 41.48 ? 46  GLY A O   1 
ATOM   200  N  N   . GLU A 1 58  ? -14.565 19.652  -47.620 1.00 41.21 ? 47  GLU A N   1 
ATOM   201  C  CA  . GLU A 1 58  ? -13.838 20.608  -46.802 1.00 44.94 ? 47  GLU A CA  1 
ATOM   202  C  C   . GLU A 1 58  ? -13.906 20.207  -45.340 1.00 42.69 ? 47  GLU A C   1 
ATOM   203  O  O   . GLU A 1 58  ? -14.791 19.463  -44.914 1.00 44.39 ? 47  GLU A O   1 
ATOM   204  C  CB  . GLU A 1 58  ? -14.380 22.029  -46.984 1.00 46.50 ? 47  GLU A CB  1 
ATOM   205  C  CG  . GLU A 1 58  ? -14.379 22.495  -48.434 1.00 58.74 ? 47  GLU A CG  1 
ATOM   206  C  CD  . GLU A 1 58  ? -14.977 23.877  -48.622 1.00 73.26 ? 47  GLU A CD  1 
ATOM   207  O  OE1 . GLU A 1 58  ? -16.047 24.148  -48.025 1.00 66.97 ? 47  GLU A OE1 1 
ATOM   208  O  OE2 . GLU A 1 58  ? -14.376 24.684  -49.378 1.00 77.07 ? 47  GLU A OE2 1 
ATOM   209  N  N   . ILE A 1 59  ? -12.946 20.705  -44.572 1.00 41.02 ? 48  ILE A N   1 
ATOM   210  C  CA  . ILE A 1 59  ? -12.905 20.528  -43.128 1.00 37.83 ? 48  ILE A CA  1 
ATOM   211  C  C   . ILE A 1 59  ? -13.294 21.849  -42.475 1.00 38.85 ? 48  ILE A C   1 
ATOM   212  O  O   . ILE A 1 59  ? -12.871 22.916  -42.928 1.00 46.90 ? 48  ILE A O   1 
ATOM   213  C  CB  . ILE A 1 59  ? -11.505 20.066  -42.683 1.00 33.80 ? 48  ILE A CB  1 
ATOM   214  C  CG1 . ILE A 1 59  ? -11.054 18.868  -43.525 1.00 39.34 ? 48  ILE A CG1 1 
ATOM   215  C  CG2 . ILE A 1 59  ? -11.504 19.722  -41.224 1.00 35.28 ? 48  ILE A CG2 1 
ATOM   216  C  CD1 . ILE A 1 59  ? -9.533  18.740  -43.702 1.00 38.26 ? 48  ILE A CD1 1 
ATOM   217  N  N   . ARG A 1 60  ? -14.135 21.786  -41.442 1.00 36.36 ? 49  ARG A N   1 
ATOM   218  C  CA  . ARG A 1 60  ? -14.455 22.956  -40.633 1.00 39.18 ? 49  ARG A CA  1 
ATOM   219  C  C   . ARG A 1 60  ? -14.457 22.576  -39.154 1.00 40.21 ? 49  ARG A C   1 
ATOM   220  O  O   . ARG A 1 60  ? -14.699 21.423  -38.791 1.00 33.37 ? 49  ARG A O   1 
ATOM   221  C  CB  . ARG A 1 60  ? -15.817 23.584  -41.003 1.00 47.88 ? 49  ARG A CB  1 
ATOM   222  C  CG  . ARG A 1 60  ? -16.204 23.530  -42.474 1.00 50.79 ? 49  ARG A CG  1 
ATOM   223  C  CD  . ARG A 1 60  ? -16.420 24.930  -43.084 1.00 55.44 ? 49  ARG A CD  1 
ATOM   224  N  NE  . ARG A 1 60  ? -16.498 24.857  -44.542 1.00 55.46 ? 49  ARG A NE  1 
ATOM   225  C  CZ  . ARG A 1 60  ? -17.625 24.939  -45.244 1.00 63.16 ? 49  ARG A CZ  1 
ATOM   226  N  NH1 . ARG A 1 60  ? -18.790 25.212  -44.667 1.00 52.96 ? 49  ARG A NH1 1 
ATOM   227  N  NH2 . ARG A 1 60  ? -17.585 24.733  -46.560 1.00 58.93 ? 49  ARG A NH2 1 
ATOM   228  N  N   . GLU A 1 61  ? -14.169 23.558  -38.302 1.00 37.73 ? 50  GLU A N   1 
ATOM   229  C  CA  . GLU A 1 61  ? -14.274 23.368  -36.864 1.00 43.46 ? 50  GLU A CA  1 
ATOM   230  C  C   . GLU A 1 61  ? -15.745 23.472  -36.436 1.00 42.47 ? 50  GLU A C   1 
ATOM   231  O  O   . GLU A 1 61  ? -16.592 23.932  -37.210 1.00 44.38 ? 50  GLU A O   1 
ATOM   232  C  CB  . GLU A 1 61  ? -13.394 24.392  -36.138 1.00 42.65 ? 50  GLU A CB  1 
ATOM   233  C  CG  . GLU A 1 61  ? -11.884 24.209  -36.370 1.00 45.20 ? 50  GLU A CG  1 
ATOM   234  C  CD  . GLU A 1 61  ? -11.086 23.915  -35.084 1.00 68.33 ? 50  GLU A CD  1 
ATOM   235  O  OE1 . GLU A 1 61  ? -11.622 24.148  -33.973 1.00 66.56 ? 50  GLU A OE1 1 
ATOM   236  O  OE2 . GLU A 1 61  ? -9.921  23.441  -35.183 1.00 67.91 ? 50  GLU A OE2 1 
ATOM   237  N  N   . PRO A 1 62  ? -16.092 23.017  -35.231 1.00 33.76 ? 51  PRO A N   1 
ATOM   238  C  CA  . PRO A 1 62  ? -17.507 22.986  -34.833 1.00 35.36 ? 51  PRO A CA  1 
ATOM   239  C  C   . PRO A 1 62  ? -18.037 24.340  -34.369 1.00 36.28 ? 51  PRO A C   1 
ATOM   240  O  O   . PRO A 1 62  ? -17.306 25.300  -34.135 1.00 43.13 ? 51  PRO A O   1 
ATOM   241  C  CB  . PRO A 1 62  ? -17.531 21.980  -33.676 1.00 34.02 ? 51  PRO A CB  1 
ATOM   242  C  CG  . PRO A 1 62  ? -16.153 21.995  -33.139 1.00 31.80 ? 51  PRO A CG  1 
ATOM   243  C  CD  . PRO A 1 62  ? -15.238 22.276  -34.283 1.00 30.64 ? 51  PRO A CD  1 
ATOM   244  N  N   . GLN A 1 63  ? -19.351 24.395  -34.231 1.00 34.43 ? 52  GLN A N   1 
ATOM   245  C  CA  . GLN A 1 63  ? -20.020 25.468  -33.521 1.00 34.21 ? 52  GLN A CA  1 
ATOM   246  C  C   . GLN A 1 63  ? -20.601 24.927  -32.224 1.00 38.50 ? 52  GLN A C   1 
ATOM   247  O  O   . GLN A 1 63  ? -20.751 23.712  -32.046 1.00 37.25 ? 52  GLN A O   1 
ATOM   248  C  CB  . GLN A 1 63  ? -21.123 26.084  -34.368 1.00 30.06 ? 52  GLN A CB  1 
ATOM   249  C  CG  . GLN A 1 63  ? -20.886 25.897  -35.831 1.00 40.96 ? 52  GLN A CG  1 
ATOM   250  C  CD  . GLN A 1 63  ? -22.050 26.389  -36.645 1.00 52.21 ? 52  GLN A CD  1 
ATOM   251  O  OE1 . GLN A 1 63  ? -22.193 27.592  -36.872 1.00 53.12 ? 52  GLN A OE1 1 
ATOM   252  N  NE2 . GLN A 1 63  ? -22.913 25.460  -37.073 1.00 46.21 ? 52  GLN A NE2 1 
ATOM   253  N  N   . ASP A 1 64  ? -20.940 25.846  -31.319 1.00 38.35 ? 53  ASP A N   1 
ATOM   254  C  CA  . ASP A 1 64  ? -21.434 25.491  -29.995 1.00 35.88 ? 53  ASP A CA  1 
ATOM   255  C  C   . ASP A 1 64  ? -22.948 25.671  -29.937 1.00 34.12 ? 53  ASP A C   1 
ATOM   256  O  O   . ASP A 1 64  ? -23.439 26.797  -29.856 1.00 38.91 ? 53  ASP A O   1 
ATOM   257  C  CB  . ASP A 1 64  ? -20.746 26.324  -28.922 1.00 29.51 ? 53  ASP A CB  1 
ATOM   258  C  CG  . ASP A 1 64  ? -20.995 25.790  -27.528 1.00 37.27 ? 53  ASP A CG  1 
ATOM   259  O  OD1 . ASP A 1 64  ? -21.699 24.759  -27.390 1.00 37.59 ? 53  ASP A OD1 1 
ATOM   260  O  OD2 . ASP A 1 64  ? -20.501 26.410  -26.563 1.00 43.68 ? 53  ASP A OD2 1 
ATOM   261  N  N   . PHE A 1 65  ? -23.676 24.550  -29.950 1.00 38.55 ? 54  PHE A N   1 
ATOM   262  C  CA  . PHE A 1 65  ? -25.128 24.495  -29.829 1.00 34.74 ? 54  PHE A CA  1 
ATOM   263  C  C   . PHE A 1 65  ? -25.595 24.327  -28.400 1.00 27.97 ? 54  PHE A C   1 
ATOM   264  O  O   . PHE A 1 65  ? -26.772 24.035  -28.185 1.00 25.35 ? 54  PHE A O   1 
ATOM   265  C  CB  . PHE A 1 65  ? -25.702 23.339  -30.660 1.00 33.24 ? 54  PHE A CB  1 
ATOM   266  C  CG  . PHE A 1 65  ? -25.401 23.435  -32.121 1.00 36.52 ? 54  PHE A CG  1 
ATOM   267  C  CD1 . PHE A 1 65  ? -24.206 22.949  -32.630 1.00 36.14 ? 54  PHE A CD1 1 
ATOM   268  C  CD2 . PHE A 1 65  ? -26.309 24.013  -32.991 1.00 31.71 ? 54  PHE A CD2 1 
ATOM   269  C  CE1 . PHE A 1 65  ? -23.922 23.036  -33.989 1.00 32.84 ? 54  PHE A CE1 1 
ATOM   270  C  CE2 . PHE A 1 65  ? -26.025 24.103  -34.343 1.00 31.80 ? 54  PHE A CE2 1 
ATOM   271  C  CZ  . PHE A 1 65  ? -24.830 23.608  -34.839 1.00 33.06 ? 54  PHE A CZ  1 
ATOM   272  N  N   . GLY A 1 66  ? -24.698 24.444  -27.430 1.00 30.93 ? 55  GLY A N   1 
ATOM   273  C  CA  . GLY A 1 66  ? -25.087 24.396  -26.036 1.00 28.15 ? 55  GLY A CA  1 
ATOM   274  C  C   . GLY A 1 66  ? -25.247 23.001  -25.449 1.00 32.63 ? 55  GLY A C   1 
ATOM   275  O  O   . GLY A 1 66  ? -24.927 21.967  -26.047 1.00 33.38 ? 55  GLY A O   1 
ATOM   276  N  N   . ARG A 1 67  ? -25.760 22.992  -24.222 1.00 35.76 ? 56  ARG A N   1 
ATOM   277  C  CA  . ARG A 1 67  ? -25.939 21.752  -23.494 1.00 34.31 ? 56  ARG A CA  1 
ATOM   278  C  C   . ARG A 1 67  ? -27.309 21.138  -23.719 1.00 33.99 ? 56  ARG A C   1 
ATOM   279  O  O   . ARG A 1 67  ? -27.471 19.931  -23.505 1.00 33.57 ? 56  ARG A O   1 
ATOM   280  C  CB  . ARG A 1 67  ? -25.710 21.971  -21.995 1.00 27.99 ? 56  ARG A CB  1 
ATOM   281  C  CG  . ARG A 1 67  ? -25.338 20.677  -21.269 1.00 34.92 ? 56  ARG A CG  1 
ATOM   282  C  CD  . ARG A 1 67  ? -25.247 20.851  -19.766 1.00 40.30 ? 56  ARG A CD  1 
ATOM   283  N  NE  . ARG A 1 67  ? -26.470 20.472  -19.065 1.00 30.67 ? 56  ARG A NE  1 
ATOM   284  C  CZ  . ARG A 1 67  ? -26.501 20.109  -17.789 1.00 34.39 ? 56  ARG A CZ  1 
ATOM   285  N  NH1 . ARG A 1 67  ? -25.393 20.051  -17.061 1.00 31.14 ? 56  ARG A NH1 1 
ATOM   286  N  NH2 . ARG A 1 67  ? -27.668 19.788  -17.229 1.00 32.29 ? 56  ARG A NH2 1 
ATOM   287  N  N   . ASP A 1 68  ? -28.284 21.933  -24.160 1.00 38.51 ? 57  ASP A N   1 
ATOM   288  C  CA  . ASP A 1 68  ? -29.642 21.416  -24.327 1.00 34.80 ? 57  ASP A CA  1 
ATOM   289  C  C   . ASP A 1 68  ? -29.693 20.192  -25.230 1.00 35.83 ? 57  ASP A C   1 
ATOM   290  O  O   . ASP A 1 68  ? -30.251 19.168  -24.797 1.00 37.58 ? 57  ASP A O   1 
ATOM   291  C  CB  . ASP A 1 68  ? -30.564 22.535  -24.822 1.00 40.53 ? 57  ASP A CB  1 
ATOM   292  C  CG  . ASP A 1 68  ? -30.766 23.635  -23.780 1.00 47.72 ? 57  ASP A CG  1 
ATOM   293  O  OD1 . ASP A 1 68  ? -30.449 23.403  -22.600 1.00 41.06 ? 57  ASP A OD1 1 
ATOM   294  O  OD2 . ASP A 1 68  ? -31.229 24.741  -24.137 1.00 51.09 ? 57  ASP A OD2 1 
ATOM   295  N  N   . PRO A 1 69  ? -29.117 20.193  -26.446 1.00 31.19 ? 58  PRO A N   1 
ATOM   296  C  CA  . PRO A 1 69  ? -29.224 18.988  -27.281 1.00 32.66 ? 58  PRO A CA  1 
ATOM   297  C  C   . PRO A 1 69  ? -28.589 17.756  -26.653 1.00 34.94 ? 58  PRO A C   1 
ATOM   298  O  O   . PRO A 1 69  ? -29.109 16.651  -26.844 1.00 36.43 ? 58  PRO A O   1 
ATOM   299  C  CB  . PRO A 1 69  ? -28.514 19.399  -28.582 1.00 28.62 ? 58  PRO A CB  1 
ATOM   300  C  CG  . PRO A 1 69  ? -28.507 20.841  -28.575 1.00 31.62 ? 58  PRO A CG  1 
ATOM   301  C  CD  . PRO A 1 69  ? -28.326 21.217  -27.141 1.00 33.73 ? 58  PRO A CD  1 
ATOM   302  N  N   . ILE A 1 70  ? -27.482 17.906  -25.915 1.00 28.88 ? 59  ILE A N   1 
ATOM   303  C  CA  . ILE A 1 70  ? -26.907 16.766  -25.202 1.00 29.21 ? 59  ILE A CA  1 
ATOM   304  C  C   . ILE A 1 70  ? -27.875 16.263  -24.136 1.00 34.01 ? 59  ILE A C   1 
ATOM   305  O  O   . ILE A 1 70  ? -28.046 15.047  -23.949 1.00 28.68 ? 59  ILE A O   1 
ATOM   306  C  CB  . ILE A 1 70  ? -25.538 17.137  -24.605 1.00 27.50 ? 59  ILE A CB  1 
ATOM   307  C  CG1 . ILE A 1 70  ? -24.550 17.462  -25.734 1.00 33.30 ? 59  ILE A CG1 1 
ATOM   308  C  CG2 . ILE A 1 70  ? -25.004 16.005  -23.744 1.00 21.99 ? 59  ILE A CG2 1 
ATOM   309  C  CD1 . ILE A 1 70  ? -23.361 18.301  -25.328 1.00 30.72 ? 59  ILE A CD1 1 
ATOM   310  N  N   . GLN A 1 71  ? -28.550 17.189  -23.446 1.00 35.71 ? 60  GLN A N   1 
ATOM   311  C  CA  . GLN A 1 71  ? -29.524 16.832  -22.421 1.00 35.39 ? 60  GLN A CA  1 
ATOM   312  C  C   . GLN A 1 71  ? -30.833 16.321  -22.994 1.00 30.37 ? 60  GLN A C   1 
ATOM   313  O  O   . GLN A 1 71  ? -31.674 15.836  -22.233 1.00 32.44 ? 60  GLN A O   1 
ATOM   314  C  CB  . GLN A 1 71  ? -29.813 18.017  -21.500 1.00 28.09 ? 60  GLN A CB  1 
ATOM   315  C  CG  . GLN A 1 71  ? -30.252 17.562  -20.137 1.00 28.36 ? 60  GLN A CG  1 
ATOM   316  C  CD  . GLN A 1 71  ? -30.357 18.688  -19.151 1.00 36.67 ? 60  GLN A CD  1 
ATOM   317  O  OE1 . GLN A 1 71  ? -29.514 19.592  -19.137 1.00 38.55 ? 60  GLN A OE1 1 
ATOM   318  N  NE2 . GLN A 1 71  ? -31.388 18.642  -18.302 1.00 26.07 ? 60  GLN A NE2 1 
ATOM   319  N  N   . ARG A 1 72  ? -31.035 16.431  -24.303 1.00 27.56 ? 61  ARG A N   1 
ATOM   320  C  CA  . ARG A 1 72  ? -32.115 15.687  -24.926 1.00 31.34 ? 61  ARG A CA  1 
ATOM   321  C  C   . ARG A 1 72  ? -31.880 14.172  -24.871 1.00 33.81 ? 61  ARG A C   1 
ATOM   322  O  O   . ARG A 1 72  ? -32.826 13.407  -25.094 1.00 35.76 ? 61  ARG A O   1 
ATOM   323  C  CB  . ARG A 1 72  ? -32.298 16.159  -26.378 1.00 30.71 ? 61  ARG A CB  1 
ATOM   324  C  CG  . ARG A 1 72  ? -32.811 17.594  -26.551 1.00 28.91 ? 61  ARG A CG  1 
ATOM   325  C  CD  . ARG A 1 72  ? -34.197 17.828  -25.921 1.00 28.19 ? 61  ARG A CD  1 
ATOM   326  N  NE  . ARG A 1 72  ? -35.279 17.193  -26.672 1.00 31.62 ? 61  ARG A NE  1 
ATOM   327  C  CZ  . ARG A 1 72  ? -36.321 16.582  -26.120 1.00 33.31 ? 61  ARG A CZ  1 
ATOM   328  N  NH1 . ARG A 1 72  ? -36.472 16.528  -24.810 1.00 39.65 ? 61  ARG A NH1 1 
ATOM   329  N  NH2 . ARG A 1 72  ? -37.236 16.013  -26.903 1.00 27.07 ? 61  ARG A NH2 1 
ATOM   330  N  N   . ILE A 1 73  ? -30.657 13.724  -24.557 1.00 32.43 ? 62  ILE A N   1 
ATOM   331  C  CA  . ILE A 1 73  ? -30.315 12.308  -24.488 1.00 32.08 ? 62  ILE A CA  1 
ATOM   332  C  C   . ILE A 1 73  ? -29.841 11.902  -23.095 1.00 28.43 ? 62  ILE A C   1 
ATOM   333  O  O   . ILE A 1 73  ? -30.212 10.836  -22.589 1.00 24.15 ? 62  ILE A O   1 
ATOM   334  C  CB  . ILE A 1 73  ? -29.241 11.947  -25.550 1.00 34.45 ? 62  ILE A CB  1 
ATOM   335  C  CG1 . ILE A 1 73  ? -29.803 12.071  -26.967 1.00 31.13 ? 62  ILE A CG1 1 
ATOM   336  C  CG2 . ILE A 1 73  ? -28.697 10.542  -25.338 1.00 21.70 ? 62  ILE A CG2 1 
ATOM   337  C  CD1 . ILE A 1 73  ? -30.673 10.896  -27.350 1.00 33.60 ? 62  ILE A CD1 1 
ATOM   338  N  N   . HIS A 1 74  ? -29.024 12.731  -22.456 1.00 30.80 ? 63  HIS A N   1 
ATOM   339  C  CA  . HIS A 1 74  ? -28.400 12.390  -21.185 1.00 28.94 ? 63  HIS A CA  1 
ATOM   340  C  C   . HIS A 1 74  ? -29.109 13.126  -20.060 1.00 26.14 ? 63  HIS A C   1 
ATOM   341  O  O   . HIS A 1 74  ? -29.472 14.296  -20.205 1.00 32.52 ? 63  HIS A O   1 
ATOM   342  C  CB  . HIS A 1 74  ? -26.900 12.729  -21.211 1.00 26.65 ? 63  HIS A CB  1 
ATOM   343  C  CG  . HIS A 1 74  ? -26.135 11.957  -22.243 1.00 30.04 ? 63  HIS A CG  1 
ATOM   344  N  ND1 . HIS A 1 74  ? -26.049 10.580  -22.231 1.00 31.09 ? 63  HIS A ND1 1 
ATOM   345  C  CD2 . HIS A 1 74  ? -25.452 12.364  -23.340 1.00 33.20 ? 63  HIS A CD2 1 
ATOM   346  C  CE1 . HIS A 1 74  ? -25.338 10.175  -23.270 1.00 29.34 ? 63  HIS A CE1 1 
ATOM   347  N  NE2 . HIS A 1 74  ? -24.964 11.236  -23.959 1.00 26.99 ? 63  HIS A NE2 1 
ATOM   348  N  N   . THR A 1 75  ? -29.323 12.436  -18.946 1.00 21.70 ? 64  THR A N   1 
ATOM   349  C  CA  . THR A 1 75  ? -30.083 13.051  -17.873 1.00 28.79 ? 64  THR A CA  1 
ATOM   350  C  C   . THR A 1 75  ? -29.301 14.215  -17.258 1.00 34.89 ? 64  THR A C   1 
ATOM   351  O  O   . THR A 1 75  ? -28.070 14.296  -17.342 1.00 31.58 ? 64  THR A O   1 
ATOM   352  C  CB  . THR A 1 75  ? -30.468 12.011  -16.811 1.00 27.66 ? 64  THR A CB  1 
ATOM   353  O  OG1 . THR A 1 75  ? -29.340 11.694  -15.988 1.00 33.39 ? 64  THR A OG1 1 
ATOM   354  C  CG2 . THR A 1 75  ? -31.002 10.742  -17.468 1.00 19.78 ? 64  THR A CG2 1 
ATOM   355  N  N   . ALA A 1 76  ? -30.048 15.153  -16.668 1.00 34.40 ? 65  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 76  ? -29.424 16.321  -16.057 1.00 33.99 ? 65  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 76  ? -28.497 15.921  -14.913 1.00 32.74 ? 65  ALA A C   1 
ATOM   358  O  O   . ALA A 1 76  ? -27.411 16.485  -14.751 1.00 27.90 ? 65  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 76  ? -30.502 17.276  -15.563 1.00 31.74 ? 65  ALA A CB  1 
ATOM   360  N  N   . GLU A 1 77  ? -28.911 14.944  -14.112 1.00 34.32 ? 66  GLU A N   1 
ATOM   361  C  CA  . GLU A 1 77  ? -28.052 14.440  -13.048 1.00 35.45 ? 66  GLU A CA  1 
ATOM   362  C  C   . GLU A 1 77  ? -26.725 13.925  -13.606 1.00 33.63 ? 66  GLU A C   1 
ATOM   363  O  O   . GLU A 1 77  ? -25.646 14.252  -13.095 1.00 34.00 ? 66  GLU A O   1 
ATOM   364  C  CB  . GLU A 1 77  ? -28.787 13.347  -12.265 1.00 26.99 ? 66  GLU A CB  1 
ATOM   365  C  CG  . GLU A 1 77  ? -30.020 13.803  -11.461 1.00 35.71 ? 66  GLU A CG  1 
ATOM   366  C  CD  . GLU A 1 77  ? -31.195 14.315  -12.321 1.00 56.29 ? 66  GLU A CD  1 
ATOM   367  O  OE1 . GLU A 1 77  ? -31.176 14.108  -13.562 1.00 53.78 ? 66  GLU A OE1 1 
ATOM   368  O  OE2 . GLU A 1 77  ? -32.135 14.931  -11.752 1.00 51.15 ? 66  GLU A OE2 1 
ATOM   369  N  N   . TYR A 1 78  ? -26.788 13.128  -14.669 1.00 31.28 ? 67  TYR A N   1 
ATOM   370  C  CA  . TYR A 1 78  ? -25.577 12.555  -15.232 1.00 28.36 ? 67  TYR A CA  1 
ATOM   371  C  C   . TYR A 1 78  ? -24.647 13.639  -15.760 1.00 29.98 ? 67  TYR A C   1 
ATOM   372  O  O   . TYR A 1 78  ? -23.435 13.601  -15.508 1.00 27.77 ? 67  TYR A O   1 
ATOM   373  C  CB  . TYR A 1 78  ? -25.958 11.571  -16.328 1.00 28.78 ? 67  TYR A CB  1 
ATOM   374  C  CG  . TYR A 1 78  ? -24.808 11.018  -17.128 1.00 34.06 ? 67  TYR A CG  1 
ATOM   375  C  CD1 . TYR A 1 78  ? -24.012 9.993   -16.620 1.00 30.01 ? 67  TYR A CD1 1 
ATOM   376  C  CD2 . TYR A 1 78  ? -24.527 11.510  -18.405 1.00 32.38 ? 67  TYR A CD2 1 
ATOM   377  C  CE1 . TYR A 1 78  ? -22.971 9.476   -17.358 1.00 30.89 ? 67  TYR A CE1 1 
ATOM   378  C  CE2 . TYR A 1 78  ? -23.476 11.009  -19.146 1.00 33.18 ? 67  TYR A CE2 1 
ATOM   379  C  CZ  . TYR A 1 78  ? -22.708 9.985   -18.620 1.00 31.45 ? 67  TYR A CZ  1 
ATOM   380  O  OH  . TYR A 1 78  ? -21.677 9.467   -19.362 1.00 27.38 ? 67  TYR A OH  1 
ATOM   381  N  N   . LEU A 1 79  ? -25.204 14.622  -16.485 1.00 34.79 ? 68  LEU A N   1 
ATOM   382  C  CA  . LEU A 1 79  ? -24.405 15.725  -17.028 1.00 29.85 ? 68  LEU A CA  1 
ATOM   383  C  C   . LEU A 1 79  ? -23.831 16.590  -15.913 1.00 31.24 ? 68  LEU A C   1 
ATOM   384  O  O   . LEU A 1 79  ? -22.660 16.989  -15.970 1.00 31.98 ? 68  LEU A O   1 
ATOM   385  C  CB  . LEU A 1 79  ? -25.240 16.562  -17.999 1.00 24.84 ? 68  LEU A CB  1 
ATOM   386  C  CG  . LEU A 1 79  ? -25.696 15.780  -19.237 1.00 28.43 ? 68  LEU A CG  1 
ATOM   387  C  CD1 . LEU A 1 79  ? -26.595 16.591  -20.162 1.00 30.36 ? 68  LEU A CD1 1 
ATOM   388  C  CD2 . LEU A 1 79  ? -24.480 15.302  -19.989 1.00 31.48 ? 68  LEU A CD2 1 
ATOM   389  N  N   . ASN A 1 80  ? -24.630 16.852  -14.875 1.00 30.82 ? 69  ASN A N   1 
ATOM   390  C  CA  . ASN A 1 80  ? -24.141 17.582  -13.708 1.00 34.41 ? 69  ASN A CA  1 
ATOM   391  C  C   . ASN A 1 80  ? -23.041 16.814  -12.992 1.00 35.21 ? 69  ASN A C   1 
ATOM   392  O  O   . ASN A 1 80  ? -22.000 17.386  -12.638 1.00 34.77 ? 69  ASN A O   1 
ATOM   393  C  CB  . ASN A 1 80  ? -25.294 17.868  -12.746 1.00 28.51 ? 69  ASN A CB  1 
ATOM   394  C  CG  . ASN A 1 80  ? -26.353 18.702  -13.377 1.00 27.34 ? 69  ASN A CG  1 
ATOM   395  O  OD1 . ASN A 1 80  ? -26.113 19.379  -14.381 1.00 33.41 ? 69  ASN A OD1 1 
ATOM   396  N  ND2 . ASN A 1 80  ? -27.541 18.642  -12.827 1.00 26.52 ? 69  ASN A ND2 1 
ATOM   397  N  N   . PHE A 1 81  ? -23.265 15.518  -12.739 1.00 33.96 ? 70  PHE A N   1 
ATOM   398  C  CA  . PHE A 1 81  ? -22.210 14.721  -12.130 1.00 32.63 ? 70  PHE A CA  1 
ATOM   399  C  C   . PHE A 1 81  ? -20.937 14.805  -12.960 1.00 32.24 ? 70  PHE A C   1 
ATOM   400  O  O   . PHE A 1 81  ? -19.840 15.025  -12.433 1.00 33.57 ? 70  PHE A O   1 
ATOM   401  C  CB  . PHE A 1 81  ? -22.642 13.269  -11.973 1.00 22.67 ? 70  PHE A CB  1 
ATOM   402  C  CG  . PHE A 1 81  ? -21.501 12.371  -11.620 1.00 30.66 ? 70  PHE A CG  1 
ATOM   403  C  CD1 . PHE A 1 81  ? -21.045 12.292  -10.312 1.00 27.51 ? 70  PHE A CD1 1 
ATOM   404  C  CD2 . PHE A 1 81  ? -20.838 11.634  -12.606 1.00 29.33 ? 70  PHE A CD2 1 
ATOM   405  C  CE1 . PHE A 1 81  ? -19.977 11.463  -9.990  1.00 29.44 ? 70  PHE A CE1 1 
ATOM   406  C  CE2 . PHE A 1 81  ? -19.756 10.814  -12.289 1.00 25.01 ? 70  PHE A CE2 1 
ATOM   407  C  CZ  . PHE A 1 81  ? -19.327 10.726  -10.992 1.00 27.11 ? 70  PHE A CZ  1 
ATOM   408  N  N   . PHE A 1 82  ? -21.081 14.662  -14.270 1.00 27.02 ? 71  PHE A N   1 
ATOM   409  C  CA  . PHE A 1 82  ? -19.938 14.636  -15.163 1.00 26.97 ? 71  PHE A CA  1 
ATOM   410  C  C   . PHE A 1 82  ? -19.204 15.972  -15.162 1.00 35.24 ? 71  PHE A C   1 
ATOM   411  O  O   . PHE A 1 82  ? -17.972 15.997  -15.266 1.00 36.82 ? 71  PHE A O   1 
ATOM   412  C  CB  . PHE A 1 82  ? -20.462 14.247  -16.547 1.00 33.67 ? 71  PHE A CB  1 
ATOM   413  C  CG  . PHE A 1 82  ? -19.411 13.921  -17.558 1.00 30.57 ? 71  PHE A CG  1 
ATOM   414  C  CD1 . PHE A 1 82  ? -18.102 13.682  -17.188 1.00 27.88 ? 71  PHE A CD1 1 
ATOM   415  C  CD2 . PHE A 1 82  ? -19.760 13.848  -18.908 1.00 27.59 ? 71  PHE A CD2 1 
ATOM   416  C  CE1 . PHE A 1 82  ? -17.153 13.385  -18.154 1.00 30.55 ? 71  PHE A CE1 1 
ATOM   417  C  CE2 . PHE A 1 82  ? -18.823 13.561  -19.871 1.00 27.57 ? 71  PHE A CE2 1 
ATOM   418  C  CZ  . PHE A 1 82  ? -17.514 13.332  -19.498 1.00 29.97 ? 71  PHE A CZ  1 
ATOM   419  N  N   . GLU A 1 83  ? -19.936 17.089  -15.019 1.00 34.74 ? 72  GLU A N   1 
ATOM   420  C  CA  . GLU A 1 83  ? -19.315 18.417  -15.067 1.00 31.54 ? 72  GLU A CA  1 
ATOM   421  C  C   . GLU A 1 83  ? -18.427 18.654  -13.858 1.00 31.77 ? 72  GLU A C   1 
ATOM   422  O  O   . GLU A 1 83  ? -17.379 19.304  -13.964 1.00 36.37 ? 72  GLU A O   1 
ATOM   423  C  CB  . GLU A 1 83  ? -20.382 19.514  -15.121 1.00 33.28 ? 72  GLU A CB  1 
ATOM   424  C  CG  . GLU A 1 83  ? -20.574 20.214  -16.463 1.00 35.44 ? 72  GLU A CG  1 
ATOM   425  C  CD  . GLU A 1 83  ? -21.984 20.801  -16.614 1.00 43.59 ? 72  GLU A CD  1 
ATOM   426  O  OE1 . GLU A 1 83  ? -22.501 21.401  -15.637 1.00 49.48 ? 72  GLU A OE1 1 
ATOM   427  O  OE2 . GLU A 1 83  ? -22.590 20.643  -17.703 1.00 40.88 ? 72  GLU A OE2 1 
ATOM   428  N  N   . GLY A 1 84  ? -18.842 18.161  -12.694 1.00 32.77 ? 73  GLY A N   1 
ATOM   429  C  CA  . GLY A 1 84  ? -18.150 18.439  -11.454 1.00 32.12 ? 73  GLY A CA  1 
ATOM   430  C  C   . GLY A 1 84  ? -17.377 17.276  -10.887 1.00 34.95 ? 73  GLY A C   1 
ATOM   431  O  O   . GLY A 1 84  ? -16.815 17.407  -9.789  1.00 33.79 ? 73  GLY A O   1 
ATOM   432  N  N   . ALA A 1 85  ? -17.303 16.143  -11.596 1.00 30.40 ? 74  ALA A N   1 
ATOM   433  C  CA  . ALA A 1 85  ? -16.688 14.950  -11.032 1.00 30.58 ? 74  ALA A CA  1 
ATOM   434  C  C   . ALA A 1 85  ? -15.176 15.118  -10.861 1.00 32.98 ? 74  ALA A C   1 
ATOM   435  O  O   . ALA A 1 85  ? -14.613 14.689  -9.844  1.00 32.48 ? 74  ALA A O   1 
ATOM   436  C  CB  . ALA A 1 85  ? -17.013 13.732  -11.904 1.00 33.10 ? 74  ALA A CB  1 
ATOM   437  N  N   . TRP A 1 86  ? -14.494 15.733  -11.834 1.00 27.41 ? 75  TRP A N   1 
ATOM   438  C  CA  . TRP A 1 86  ? -13.056 15.935  -11.671 1.00 27.43 ? 75  TRP A CA  1 
ATOM   439  C  C   . TRP A 1 86  ? -12.751 17.033  -10.661 1.00 32.58 ? 75  TRP A C   1 
ATOM   440  O  O   . TRP A 1 86  ? -11.776 16.925  -9.911  1.00 34.74 ? 75  TRP A O   1 
ATOM   441  C  CB  . TRP A 1 86  ? -12.395 16.256  -13.003 1.00 32.08 ? 75  TRP A CB  1 
ATOM   442  C  CG  . TRP A 1 86  ? -10.921 16.621  -12.887 1.00 35.34 ? 75  TRP A CG  1 
ATOM   443  C  CD1 . TRP A 1 86  ? -10.379 17.879  -12.865 1.00 28.38 ? 75  TRP A CD1 1 
ATOM   444  C  CD2 . TRP A 1 86  ? -9.812  15.711  -12.796 1.00 35.44 ? 75  TRP A CD2 1 
ATOM   445  N  NE1 . TRP A 1 86  ? -9.010  17.806  -12.756 1.00 29.13 ? 75  TRP A NE1 1 
ATOM   446  C  CE2 . TRP A 1 86  ? -8.635  16.489  -12.719 1.00 31.10 ? 75  TRP A CE2 1 
ATOM   447  C  CE3 . TRP A 1 86  ? -9.698  14.315  -12.777 1.00 32.97 ? 75  TRP A CE3 1 
ATOM   448  C  CZ2 . TRP A 1 86  ? -7.371  15.919  -12.629 1.00 31.73 ? 75  TRP A CZ2 1 
ATOM   449  C  CZ3 . TRP A 1 86  ? -8.427  13.749  -12.676 1.00 32.21 ? 75  TRP A CZ3 1 
ATOM   450  C  CH2 . TRP A 1 86  ? -7.288  14.548  -12.599 1.00 29.07 ? 75  TRP A CH2 1 
ATOM   451  N  N   . ALA A 1 87  ? -13.554 18.106  -10.629 1.00 32.71 ? 76  ALA A N   1 
ATOM   452  C  CA  . ALA A 1 87  ? -13.337 19.142  -9.617  1.00 32.87 ? 76  ALA A CA  1 
ATOM   453  C  C   . ALA A 1 87  ? -13.472 18.566  -8.211  1.00 33.07 ? 76  ALA A C   1 
ATOM   454  O  O   . ALA A 1 87  ? -12.651 18.858  -7.329  1.00 26.91 ? 76  ALA A O   1 
ATOM   455  C  CB  . ALA A 1 87  ? -14.312 20.303  -9.825  1.00 26.38 ? 76  ALA A CB  1 
ATOM   456  N  N   . ARG A 1 88  ? -14.493 17.720  -8.001  1.00 31.97 ? 77  ARG A N   1 
ATOM   457  C  CA  . ARG A 1 88  ? -14.678 17.033  -6.722  1.00 37.68 ? 77  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 88  ? -13.485 16.147  -6.380  1.00 35.36 ? 77  ARG A C   1 
ATOM   459  O  O   . ARG A 1 88  ? -13.129 16.001  -5.203  1.00 25.52 ? 77  ARG A O   1 
ATOM   460  C  CB  . ARG A 1 88  ? -15.957 16.188  -6.754  1.00 27.89 ? 77  ARG A CB  1 
ATOM   461  C  CG  . ARG A 1 88  ? -17.220 16.986  -6.580  1.00 29.47 ? 77  ARG A CG  1 
ATOM   462  C  CD  . ARG A 1 88  ? -18.438 16.200  -7.008  1.00 28.31 ? 77  ARG A CD  1 
ATOM   463  N  NE  . ARG A 1 88  ? -18.853 15.257  -5.978  1.00 27.04 ? 77  ARG A NE  1 
ATOM   464  C  CZ  . ARG A 1 88  ? -19.679 14.244  -6.187  1.00 26.00 ? 77  ARG A CZ  1 
ATOM   465  N  NH1 . ARG A 1 88  ? -20.231 14.037  -7.370  1.00 25.36 ? 77  ARG A NH1 1 
ATOM   466  N  NH2 . ARG A 1 88  ? -19.945 13.407  -5.190  1.00 30.84 ? 77  ARG A NH2 1 
ATOM   467  N  N   . TRP A 1 89  ? -12.870 15.538  -7.407  1.00 35.86 ? 78  TRP A N   1 
ATOM   468  C  CA  . TRP A 1 89  ? -11.741 14.623  -7.231  1.00 34.69 ? 78  TRP A CA  1 
ATOM   469  C  C   . TRP A 1 89  ? -10.456 15.373  -6.904  1.00 37.36 ? 78  TRP A C   1 
ATOM   470  O  O   . TRP A 1 89  ? -9.592  14.846  -6.186  1.00 34.32 ? 78  TRP A O   1 
ATOM   471  C  CB  . TRP A 1 89  ? -11.586 13.775  -8.497  1.00 28.68 ? 78  TRP A CB  1 
ATOM   472  C  CG  . TRP A 1 89  ? -10.381 12.879  -8.595  1.00 31.84 ? 78  TRP A CG  1 
ATOM   473  C  CD1 . TRP A 1 89  ? -9.452  12.876  -9.594  1.00 31.10 ? 78  TRP A CD1 1 
ATOM   474  C  CD2 . TRP A 1 89  ? -10.003 11.815  -7.698  1.00 36.18 ? 78  TRP A CD2 1 
ATOM   475  N  NE1 . TRP A 1 89  ? -8.512  11.891  -9.375  1.00 33.50 ? 78  TRP A NE1 1 
ATOM   476  C  CE2 . TRP A 1 89  ? -8.827  11.225  -8.219  1.00 32.81 ? 78  TRP A CE2 1 
ATOM   477  C  CE3 . TRP A 1 89  ? -10.539 11.308  -6.509  1.00 33.19 ? 78  TRP A CE3 1 
ATOM   478  C  CZ2 . TRP A 1 89  ? -8.185  10.165  -7.593  1.00 24.37 ? 78  TRP A CZ2 1 
ATOM   479  C  CZ3 . TRP A 1 89  ? -9.898  10.261  -5.897  1.00 32.25 ? 78  TRP A CZ3 1 
ATOM   480  C  CH2 . TRP A 1 89  ? -8.734  9.701   -6.442  1.00 29.10 ? 78  TRP A CH2 1 
ATOM   481  N  N   . GLN A 1 90  ? -10.320 16.608  -7.403  1.00 35.84 ? 79  GLN A N   1 
ATOM   482  C  CA  . GLN A 1 90  ? -9.228  17.463  -6.961  1.00 36.10 ? 79  GLN A CA  1 
ATOM   483  C  C   . GLN A 1 90  ? -9.471  18.047  -5.566  1.00 38.84 ? 79  GLN A C   1 
ATOM   484  O  O   . GLN A 1 90  ? -8.503  18.349  -4.863  1.00 39.55 ? 79  GLN A O   1 
ATOM   485  C  CB  . GLN A 1 90  ? -8.979  18.578  -7.981  1.00 28.54 ? 79  GLN A CB  1 
ATOM   486  C  CG  . GLN A 1 90  ? -8.557  18.114  -9.358  1.00 27.37 ? 79  GLN A CG  1 
ATOM   487  C  CD  . GLN A 1 90  ? -7.364  17.175  -9.340  1.00 30.90 ? 79  GLN A CD  1 
ATOM   488  O  OE1 . GLN A 1 90  ? -6.222  17.605  -9.255  1.00 30.64 ? 79  GLN A OE1 1 
ATOM   489  N  NE2 . GLN A 1 90  ? -7.629  15.879  -9.441  1.00 38.20 ? 79  GLN A NE2 1 
ATOM   490  N  N   . GLU A 1 91  ? -10.731 18.178  -5.133  1.00 36.59 ? 80  GLU A N   1 
ATOM   491  C  CA  . GLU A 1 91  ? -11.004 18.599  -3.761  1.00 35.91 ? 80  GLU A CA  1 
ATOM   492  C  C   . GLU A 1 91  ? -10.510 17.592  -2.717  1.00 40.27 ? 80  GLU A C   1 
ATOM   493  O  O   . GLU A 1 91  ? -10.408 17.941  -1.535  1.00 46.11 ? 80  GLU A O   1 
ATOM   494  C  CB  . GLU A 1 91  ? -12.503 18.835  -3.569  1.00 36.67 ? 80  GLU A CB  1 
ATOM   495  C  CG  . GLU A 1 91  ? -13.068 20.092  -4.237  1.00 40.68 ? 80  GLU A CG  1 
ATOM   496  C  CD  . GLU A 1 91  ? -14.604 20.097  -4.271  1.00 43.35 ? 80  GLU A CD  1 
ATOM   497  O  OE1 . GLU A 1 91  ? -15.225 19.113  -3.796  1.00 47.32 ? 80  GLU A OE1 1 
ATOM   498  O  OE2 . GLU A 1 91  ? -15.194 21.073  -4.779  1.00 35.71 ? 80  GLU A OE2 1 
ATOM   499  N  N   . GLN A 1 92  ? -10.209 16.355  -3.109  1.00 39.44 ? 81  GLN A N   1 
ATOM   500  C  CA  . GLN A 1 92  ? -9.683  15.362  -2.179  1.00 44.12 ? 81  GLN A CA  1 
ATOM   501  C  C   . GLN A 1 92  ? -8.215  15.035  -2.452  1.00 46.72 ? 81  GLN A C   1 
ATOM   502  O  O   . GLN A 1 92  ? -7.732  13.978  -2.033  1.00 42.36 ? 81  GLN A O   1 
ATOM   503  C  CB  . GLN A 1 92  ? -10.510 14.079  -2.240  1.00 42.36 ? 81  GLN A CB  1 
ATOM   504  C  CG  . GLN A 1 92  ? -11.908 14.252  -2.767  1.00 40.77 ? 81  GLN A CG  1 
ATOM   505  C  CD  . GLN A 1 92  ? -12.611 12.924  -2.998  1.00 42.55 ? 81  GLN A CD  1 
ATOM   506  O  OE1 . GLN A 1 92  ? -11.965 11.911  -3.282  1.00 40.77 ? 81  GLN A OE1 1 
ATOM   507  N  NE2 . GLN A 1 92  ? -13.949 12.936  -2.943  1.00 40.19 ? 81  GLN A NE2 1 
ATOM   508  N  N   . ASP A 1 93  ? -7.500  15.922  -3.153  1.00 49.67 ? 82  ASP A N   1 
ATOM   509  C  CA  . ASP A 1 93  ? -6.110  15.689  -3.562  1.00 47.71 ? 82  ASP A CA  1 
ATOM   510  C  C   . ASP A 1 93  ? -5.981  14.347  -4.263  1.00 47.27 ? 82  ASP A C   1 
ATOM   511  O  O   . ASP A 1 93  ? -5.000  13.618  -4.091  1.00 55.52 ? 82  ASP A O   1 
ATOM   512  C  CB  . ASP A 1 93  ? -5.146  15.774  -2.377  1.00 48.53 ? 82  ASP A CB  1 
ATOM   513  C  CG  . ASP A 1 93  ? -5.507  16.885  -1.403  1.00 71.57 ? 82  ASP A CG  1 
ATOM   514  O  OD1 . ASP A 1 93  ? -5.862  18.007  -1.857  1.00 72.63 ? 82  ASP A OD1 1 
ATOM   515  O  OD2 . ASP A 1 93  ? -5.453  16.621  -0.177  1.00 71.35 ? 82  ASP A OD2 1 
ATOM   516  N  N   . GLY A 1 94  ? -7.004  14.002  -5.039  1.00 47.02 ? 83  GLY A N   1 
ATOM   517  C  CA  . GLY A 1 94  ? -6.976  12.748  -5.767  1.00 41.18 ? 83  GLY A CA  1 
ATOM   518  C  C   . GLY A 1 94  ? -5.937  12.811  -6.864  1.00 46.54 ? 83  GLY A C   1 
ATOM   519  O  O   . GLY A 1 94  ? -5.917  13.754  -7.670  1.00 49.81 ? 83  GLY A O   1 
ATOM   520  N  N   . THR A 1 95  ? -5.054  11.818  -6.899  1.00 45.27 ? 84  THR A N   1 
ATOM   521  C  CA  . THR A 1 95  ? -3.986  11.793  -7.887  1.00 58.78 ? 84  THR A CA  1 
ATOM   522  C  C   . THR A 1 95  ? -4.258  10.725  -8.939  1.00 53.05 ? 84  THR A C   1 
ATOM   523  O  O   . THR A 1 95  ? -4.670  9.601   -8.618  1.00 44.46 ? 84  THR A O   1 
ATOM   524  C  CB  . THR A 1 95  ? -2.623  11.572  -7.228  1.00 65.98 ? 84  THR A CB  1 
ATOM   525  O  OG1 . THR A 1 95  ? -2.791  10.880  -5.977  1.00 58.83 ? 84  THR A OG1 1 
ATOM   526  C  CG2 . THR A 1 95  ? -1.944  12.931  -7.001  1.00 59.25 ? 84  THR A CG2 1 
ATOM   527  N  N   . GLY A 1 96  ? -4.031  11.102  -10.197 1.00 47.77 ? 85  GLY A N   1 
ATOM   528  C  CA  . GLY A 1 96  ? -4.353  10.251  -11.320 1.00 44.75 ? 85  GLY A CA  1 
ATOM   529  C  C   . GLY A 1 96  ? -5.805  10.365  -11.753 1.00 41.76 ? 85  GLY A C   1 
ATOM   530  O  O   . GLY A 1 96  ? -6.609  11.123  -11.205 1.00 41.26 ? 85  GLY A O   1 
ATOM   531  N  N   . ASP A 1 97  ? -6.132  9.569   -12.771 1.00 37.85 ? 86  ASP A N   1 
ATOM   532  C  CA  . ASP A 1 97  ? -7.487  9.482   -13.290 1.00 37.29 ? 86  ASP A CA  1 
ATOM   533  C  C   . ASP A 1 97  ? -8.505  9.223   -12.183 1.00 37.16 ? 86  ASP A C   1 
ATOM   534  O  O   . ASP A 1 97  ? -8.245  8.521   -11.204 1.00 33.98 ? 86  ASP A O   1 
ATOM   535  C  CB  . ASP A 1 97  ? -7.574  8.359   -14.330 1.00 47.34 ? 86  ASP A CB  1 
ATOM   536  C  CG  . ASP A 1 97  ? -6.650  8.583   -15.512 1.00 45.97 ? 86  ASP A CG  1 
ATOM   537  O  OD1 . ASP A 1 97  ? -6.023  9.652   -15.542 1.00 44.91 ? 86  ASP A OD1 1 
ATOM   538  O  OD2 . ASP A 1 97  ? -6.558  7.704   -16.406 1.00 44.24 ? 86  ASP A OD2 1 
ATOM   539  N  N   . LEU A 1 98  ? -9.676  9.807   -12.348 1.00 34.69 ? 87  LEU A N   1 
ATOM   540  C  CA  . LEU A 1 98  ? -10.831 9.416   -11.569 1.00 30.17 ? 87  LEU A CA  1 
ATOM   541  C  C   . LEU A 1 98  ? -11.445 8.173   -12.210 1.00 32.21 ? 87  LEU A C   1 
ATOM   542  O  O   . LEU A 1 98  ? -11.716 8.158   -13.411 1.00 28.70 ? 87  LEU A O   1 
ATOM   543  C  CB  . LEU A 1 98  ? -11.824 10.570  -11.540 1.00 30.74 ? 87  LEU A CB  1 
ATOM   544  C  CG  . LEU A 1 98  ? -13.106 10.257  -10.802 1.00 30.20 ? 87  LEU A CG  1 
ATOM   545  C  CD1 . LEU A 1 98  ? -12.801 10.109  -9.323  1.00 26.82 ? 87  LEU A CD1 1 
ATOM   546  C  CD2 . LEU A 1 98  ? -14.184 11.303  -11.100 1.00 27.44 ? 87  LEU A CD2 1 
ATOM   547  N  N   . LEU A 1 99  ? -11.649 7.126   -11.418 1.00 35.22 ? 88  LEU A N   1 
ATOM   548  C  CA  . LEU A 1 99  ? -12.063 5.824   -11.922 1.00 33.51 ? 88  LEU A CA  1 
ATOM   549  C  C   . LEU A 1 99  ? -12.962 5.126   -10.911 1.00 38.98 ? 88  LEU A C   1 
ATOM   550  O  O   . LEU A 1 99  ? -12.765 5.261   -9.694  1.00 34.72 ? 88  LEU A O   1 
ATOM   551  C  CB  . LEU A 1 99  ? -10.857 4.914   -12.207 1.00 27.56 ? 88  LEU A CB  1 
ATOM   552  C  CG  . LEU A 1 99  ? -10.164 5.132   -13.534 1.00 35.02 ? 88  LEU A CG  1 
ATOM   553  C  CD1 . LEU A 1 99  ? -8.757  4.609   -13.428 1.00 36.23 ? 88  LEU A CD1 1 
ATOM   554  C  CD2 . LEU A 1 99  ? -10.946 4.458   -14.645 1.00 27.75 ? 88  LEU A CD2 1 
ATOM   555  N  N   . PRO A 1 100 ? -13.950 4.367   -11.385 1.00 29.94 ? 89  PRO A N   1 
ATOM   556  C  CA  . PRO A 1 100 ? -14.784 3.567   -10.482 1.00 31.96 ? 89  PRO A CA  1 
ATOM   557  C  C   . PRO A 1 100 ? -14.146 2.224   -10.164 1.00 34.04 ? 89  PRO A C   1 
ATOM   558  O  O   . PRO A 1 100 ? -13.458 1.613   -10.987 1.00 32.55 ? 89  PRO A O   1 
ATOM   559  C  CB  . PRO A 1 100 ? -16.089 3.384   -11.274 1.00 26.37 ? 89  PRO A CB  1 
ATOM   560  C  CG  . PRO A 1 100 ? -15.733 3.661   -12.713 1.00 24.46 ? 89  PRO A CG  1 
ATOM   561  C  CD  . PRO A 1 100 ? -14.367 4.258   -12.793 1.00 26.35 ? 89  PRO A CD  1 
ATOM   562  N  N   . TYR A 1 101 ? -14.375 1.763   -8.933  1.00 28.20 ? 90  TYR A N   1 
ATOM   563  C  CA  . TYR A 1 101 ? -13.839 0.472   -8.528  1.00 32.06 ? 90  TYR A CA  1 
ATOM   564  C  C   . TYR A 1 101 ? -14.919 -0.459  -7.991  1.00 32.29 ? 90  TYR A C   1 
ATOM   565  O  O   . TYR A 1 101 ? -14.586 -1.525  -7.467  1.00 33.16 ? 90  TYR A O   1 
ATOM   566  C  CB  . TYR A 1 101 ? -12.708 0.642   -7.497  1.00 27.46 ? 90  TYR A CB  1 
ATOM   567  C  CG  . TYR A 1 101 ? -13.137 1.319   -6.215  1.00 39.55 ? 90  TYR A CG  1 
ATOM   568  C  CD1 . TYR A 1 101 ? -13.685 0.584   -5.161  1.00 38.18 ? 90  TYR A CD1 1 
ATOM   569  C  CD2 . TYR A 1 101 ? -12.994 2.701   -6.052  1.00 42.60 ? 90  TYR A CD2 1 
ATOM   570  C  CE1 . TYR A 1 101 ? -14.088 1.204   -3.981  1.00 40.73 ? 90  TYR A CE1 1 
ATOM   571  C  CE2 . TYR A 1 101 ? -13.384 3.329   -4.874  1.00 41.94 ? 90  TYR A CE2 1 
ATOM   572  C  CZ  . TYR A 1 101 ? -13.939 2.579   -3.841  1.00 48.64 ? 90  TYR A CZ  1 
ATOM   573  O  OH  . TYR A 1 101 ? -14.340 3.206   -2.672  1.00 50.58 ? 90  TYR A OH  1 
ATOM   574  N  N   . THR A 1 102 ? -16.194 -0.088  -8.124  1.00 28.76 ? 91  THR A N   1 
ATOM   575  C  CA  . THR A 1 102 ? -17.330 -0.903  -7.714  1.00 28.46 ? 91  THR A CA  1 
ATOM   576  C  C   . THR A 1 102 ? -18.496 -0.553  -8.633  1.00 29.52 ? 91  THR A C   1 
ATOM   577  O  O   . THR A 1 102 ? -18.621 0.603   -9.045  1.00 30.60 ? 91  THR A O   1 
ATOM   578  C  CB  . THR A 1 102 ? -17.668 -0.658  -6.223  1.00 30.44 ? 91  THR A CB  1 
ATOM   579  O  OG1 . THR A 1 102 ? -16.586 -1.123  -5.411  1.00 39.80 ? 91  THR A OG1 1 
ATOM   580  C  CG2 . THR A 1 102 ? -18.938 -1.382  -5.769  1.00 26.89 ? 91  THR A CG2 1 
ATOM   581  N  N   . TRP A 1 103 ? -19.328 -1.544  -8.977  1.00 24.69 ? 92  TRP A N   1 
ATOM   582  C  CA  . TRP A 1 103 ? -20.474 -1.300  -9.846  1.00 28.86 ? 92  TRP A CA  1 
ATOM   583  C  C   . TRP A 1 103 ? -21.739 -1.936  -9.292  1.00 28.83 ? 92  TRP A C   1 
ATOM   584  O  O   . TRP A 1 103 ? -21.661 -2.910  -8.539  1.00 30.66 ? 92  TRP A O   1 
ATOM   585  C  CB  . TRP A 1 103 ? -20.206 -1.837  -11.260 1.00 29.05 ? 92  TRP A CB  1 
ATOM   586  C  CG  . TRP A 1 103 ? -19.098 -1.120  -11.885 1.00 28.25 ? 92  TRP A CG  1 
ATOM   587  C  CD1 . TRP A 1 103 ? -19.182 -0.057  -12.719 1.00 26.14 ? 92  TRP A CD1 1 
ATOM   588  C  CD2 . TRP A 1 103 ? -17.707 -1.373  -11.686 1.00 31.33 ? 92  TRP A CD2 1 
ATOM   589  N  NE1 . TRP A 1 103 ? -17.928 0.362   -13.070 1.00 28.11 ? 92  TRP A NE1 1 
ATOM   590  C  CE2 . TRP A 1 103 ? -17.003 -0.431  -12.451 1.00 27.85 ? 92  TRP A CE2 1 
ATOM   591  C  CE3 . TRP A 1 103 ? -16.987 -2.320  -10.944 1.00 30.87 ? 92  TRP A CE3 1 
ATOM   592  C  CZ2 . TRP A 1 103 ? -15.618 -0.400  -12.497 1.00 29.72 ? 92  TRP A CZ2 1 
ATOM   593  C  CZ3 . TRP A 1 103 ? -15.618 -2.280  -10.981 1.00 27.08 ? 92  TRP A CZ3 1 
ATOM   594  C  CH2 . TRP A 1 103 ? -14.944 -1.329  -11.754 1.00 29.19 ? 92  TRP A CH2 1 
ATOM   595  N  N   . PRO A 1 104 ? -22.930 -1.412  -9.651  1.00 25.75 ? 93  PRO A N   1 
ATOM   596  C  CA  . PRO A 1 104 ? -24.169 -2.056  -9.152  1.00 28.95 ? 93  PRO A CA  1 
ATOM   597  C  C   . PRO A 1 104 ? -24.559 -3.251  -10.021 1.00 31.66 ? 93  PRO A C   1 
ATOM   598  O  O   . PRO A 1 104 ? -25.435 -3.215  -10.888 1.00 35.71 ? 93  PRO A O   1 
ATOM   599  C  CB  . PRO A 1 104 ? -25.193 -0.915  -9.210  1.00 28.56 ? 93  PRO A CB  1 
ATOM   600  C  CG  . PRO A 1 104 ? -24.749 -0.043  -10.344 1.00 24.46 ? 93  PRO A CG  1 
ATOM   601  C  CD  . PRO A 1 104 ? -23.221 -0.216  -10.465 1.00 30.03 ? 93  PRO A CD  1 
ATOM   602  N  N   . ALA A 1 105 ? -23.878 -4.359  -9.794  1.00 31.04 ? 94  ALA A N   1 
ATOM   603  C  CA  . ALA A 1 105 ? -24.037 -5.520  -10.650 1.00 31.02 ? 94  ALA A CA  1 
ATOM   604  C  C   . ALA A 1 105 ? -25.083 -6.439  -10.020 1.00 32.27 ? 94  ALA A C   1 
ATOM   605  O  O   . ALA A 1 105 ? -25.934 -5.986  -9.254  1.00 35.59 ? 94  ALA A O   1 
ATOM   606  C  CB  . ALA A 1 105 ? -22.677 -6.178  -10.885 1.00 33.04 ? 94  ALA A CB  1 
ATOM   607  N  N   . ARG A 1 106 ? -25.056 -7.725  -10.347 1.00 32.93 ? 95  ARG A N   1 
ATOM   608  C  CA  . ARG A 1 106 ? -26.109 -8.616  -9.884  1.00 33.96 ? 95  ARG A CA  1 
ATOM   609  C  C   . ARG A 1 106 ? -26.091 -8.739  -8.364  1.00 32.29 ? 95  ARG A C   1 
ATOM   610  O  O   . ARG A 1 106 ? -25.028 -8.770  -7.741  1.00 32.25 ? 95  ARG A O   1 
ATOM   611  C  CB  . ARG A 1 106 ? -25.954 -9.991  -10.525 1.00 33.52 ? 95  ARG A CB  1 
ATOM   612  C  CG  . ARG A 1 106 ? -26.082 -9.986  -12.024 1.00 32.22 ? 95  ARG A CG  1 
ATOM   613  C  CD  . ARG A 1 106 ? -25.748 -11.351 -12.564 1.00 30.23 ? 95  ARG A CD  1 
ATOM   614  N  NE  . ARG A 1 106 ? -26.063 -12.346 -11.555 1.00 34.08 ? 95  ARG A NE  1 
ATOM   615  C  CZ  . ARG A 1 106 ? -25.213 -13.257 -11.111 1.00 37.75 ? 95  ARG A CZ  1 
ATOM   616  N  NH1 . ARG A 1 106 ? -23.995 -13.369 -11.610 1.00 37.99 ? 95  ARG A NH1 1 
ATOM   617  N  NH2 . ARG A 1 106 ? -25.589 -14.068 -10.130 1.00 38.99 ? 95  ARG A NH2 1 
ATOM   618  N  N   . THR A 1 107 ? -27.288 -8.827  -7.779  1.00 31.55 ? 96  THR A N   1 
ATOM   619  C  CA  . THR A 1 107 ? -27.632 -8.947  -6.356  1.00 33.53 ? 96  THR A CA  1 
ATOM   620  C  C   . THR A 1 107 ? -27.600 -7.599  -5.640  1.00 36.13 ? 96  THR A C   1 
ATOM   621  O  O   . THR A 1 107 ? -27.947 -7.531  -4.437  1.00 37.58 ? 96  THR A O   1 
ATOM   622  C  CB  . THR A 1 107 ? -26.746 -9.928  -5.573  1.00 29.82 ? 96  THR A CB  1 
ATOM   623  O  OG1 . THR A 1 107 ? -25.423 -9.392  -5.468  1.00 35.04 ? 96  THR A OG1 1 
ATOM   624  C  CG2 . THR A 1 107 ? -26.710 -11.291 -6.246  1.00 30.08 ? 96  THR A CG2 1 
ATOM   625  N  N   . LEU A 1 108 ? -27.222 -6.526  -6.314  1.00 29.52 ? 97  LEU A N   1 
ATOM   626  C  CA  . LEU A 1 108 ? -27.126 -5.243  -5.651  1.00 37.85 ? 97  LEU A CA  1 
ATOM   627  C  C   . LEU A 1 108 ? -28.265 -4.360  -6.126  1.00 38.30 ? 97  LEU A C   1 
ATOM   628  O  O   . LEU A 1 108 ? -28.911 -4.635  -7.140  1.00 35.31 ? 97  LEU A O   1 
ATOM   629  C  CB  . LEU A 1 108 ? -25.763 -4.577  -5.899  1.00 36.11 ? 97  LEU A CB  1 
ATOM   630  C  CG  . LEU A 1 108 ? -24.568 -5.334  -5.287  1.00 37.13 ? 97  LEU A CG  1 
ATOM   631  C  CD1 . LEU A 1 108 ? -23.301 -5.048  -6.064  1.00 33.77 ? 97  LEU A CD1 1 
ATOM   632  C  CD2 . LEU A 1 108 ? -24.377 -5.050  -3.794  1.00 29.63 ? 97  LEU A CD2 1 
ATOM   633  N  N   . SER A 1 109 ? -28.540 -3.327  -5.342  1.00 34.22 ? 98  SER A N   1 
ATOM   634  C  CA  . SER A 1 109 ? -29.599 -2.396  -5.660  1.00 31.04 ? 98  SER A CA  1 
ATOM   635  C  C   . SER A 1 109 ? -29.025 -1.302  -6.545  1.00 34.21 ? 98  SER A C   1 
ATOM   636  O  O   . SER A 1 109 ? -27.885 -0.861  -6.355  1.00 33.61 ? 98  SER A O   1 
ATOM   637  C  CB  . SER A 1 109 ? -30.220 -1.825  -4.383  1.00 35.95 ? 98  SER A CB  1 
ATOM   638  O  OG  . SER A 1 109 ? -30.046 -0.424  -4.296  1.00 43.36 ? 98  SER A OG  1 
ATOM   639  N  N   . GLN A 1 110 ? -29.798 -0.916  -7.554  1.00 30.39 ? 99  GLN A N   1 
ATOM   640  C  CA  . GLN A 1 110 ? -29.354 0.077   -8.526  1.00 34.24 ? 99  GLN A CA  1 
ATOM   641  C  C   . GLN A 1 110 ? -29.716 1.483   -8.046  1.00 37.24 ? 99  GLN A C   1 
ATOM   642  O  O   . GLN A 1 110 ? -30.508 2.202   -8.650  1.00 39.04 ? 99  GLN A O   1 
ATOM   643  C  CB  . GLN A 1 110 ? -29.961 -0.233  -9.885  1.00 37.81 ? 99  GLN A CB  1 
ATOM   644  C  CG  . GLN A 1 110 ? -29.477 -1.551  -10.450 1.00 37.26 ? 99  GLN A CG  1 
ATOM   645  C  CD  . GLN A 1 110 ? -29.893 -1.727  -11.894 1.00 45.21 ? 99  GLN A CD  1 
ATOM   646  O  OE1 . GLN A 1 110 ? -29.241 -2.452  -12.654 1.00 46.29 ? 99  GLN A OE1 1 
ATOM   647  N  NE2 . GLN A 1 110 ? -30.990 -1.070  -12.285 1.00 35.96 ? 99  GLN A NE2 1 
ATOM   648  N  N   . ARG A 1 111 ? -29.110 1.860   -6.924  1.00 34.71 ? 100 ARG A N   1 
ATOM   649  C  CA  . ARG A 1 111 ? -29.513 3.020   -6.151  1.00 33.05 ? 100 ARG A CA  1 
ATOM   650  C  C   . ARG A 1 111 ? -28.346 3.986   -6.047  1.00 32.79 ? 100 ARG A C   1 
ATOM   651  O  O   . ARG A 1 111 ? -27.221 3.572   -5.764  1.00 35.94 ? 100 ARG A O   1 
ATOM   652  C  CB  . ARG A 1 111 ? -29.982 2.591   -4.760  1.00 39.82 ? 100 ARG A CB  1 
ATOM   653  C  CG  . ARG A 1 111 ? -30.182 3.722   -3.768  1.00 42.43 ? 100 ARG A CG  1 
ATOM   654  C  CD  . ARG A 1 111 ? -31.401 3.418   -2.956  1.00 51.04 ? 100 ARG A CD  1 
ATOM   655  N  NE  . ARG A 1 111 ? -31.437 4.098   -1.668  1.00 57.34 ? 100 ARG A NE  1 
ATOM   656  C  CZ  . ARG A 1 111 ? -32.008 3.584   -0.586  1.00 51.22 ? 100 ARG A CZ  1 
ATOM   657  N  NH1 . ARG A 1 111 ? -32.530 2.360   -0.596  1.00 43.16 ? 100 ARG A NH1 1 
ATOM   658  N  NH2 . ARG A 1 111 ? -32.065 4.316   0.528   1.00 42.68 ? 100 ARG A NH2 1 
ATOM   659  N  N   . LEU A 1 112 ? -28.628 5.277   -6.236  1.00 37.36 ? 101 LEU A N   1 
ATOM   660  C  CA  . LEU A 1 112 ? -27.576 6.286   -6.382  1.00 31.55 ? 101 LEU A CA  1 
ATOM   661  C  C   . LEU A 1 112 ? -26.968 6.668   -5.036  1.00 35.84 ? 101 LEU A C   1 
ATOM   662  O  O   . LEU A 1 112 ? -27.671 7.231   -4.183  1.00 34.92 ? 101 LEU A O   1 
ATOM   663  C  CB  . LEU A 1 112 ? -28.132 7.526   -7.059  1.00 29.01 ? 101 LEU A CB  1 
ATOM   664  C  CG  . LEU A 1 112 ? -27.190 8.712   -7.249  1.00 27.56 ? 101 LEU A CG  1 
ATOM   665  C  CD1 . LEU A 1 112 ? -25.894 8.327   -7.956  1.00 31.97 ? 101 LEU A CD1 1 
ATOM   666  C  CD2 . LEU A 1 112 ? -27.906 9.776   -8.025  1.00 24.93 ? 101 LEU A CD2 1 
ATOM   667  N  N   . PRO A 1 113 ? -25.669 6.408   -4.814  1.00 36.06 ? 102 PRO A N   1 
ATOM   668  C  CA  . PRO A 1 113 ? -24.993 6.934   -3.619  1.00 32.94 ? 102 PRO A CA  1 
ATOM   669  C  C   . PRO A 1 113 ? -24.692 8.424   -3.744  1.00 36.96 ? 102 PRO A C   1 
ATOM   670  O  O   . PRO A 1 113 ? -25.112 9.069   -4.715  1.00 36.08 ? 102 PRO A O   1 
ATOM   671  C  CB  . PRO A 1 113 ? -23.702 6.104   -3.545  1.00 32.66 ? 102 PRO A CB  1 
ATOM   672  C  CG  . PRO A 1 113 ? -23.758 5.110   -4.715  1.00 33.25 ? 102 PRO A CG  1 
ATOM   673  C  CD  . PRO A 1 113 ? -24.752 5.649   -5.684  1.00 34.64 ? 102 PRO A CD  1 
ATOM   674  N  N   . THR A 1 114 ? -23.972 8.988   -2.766  1.00 35.74 ? 103 THR A N   1 
ATOM   675  C  CA  . THR A 1 114 ? -23.610 10.403  -2.770  1.00 33.15 ? 103 THR A CA  1 
ATOM   676  C  C   . THR A 1 114 ? -22.107 10.660  -2.798  1.00 34.59 ? 103 THR A C   1 
ATOM   677  O  O   . THR A 1 114 ? -21.692 11.728  -3.259  1.00 42.28 ? 103 THR A O   1 
ATOM   678  C  CB  . THR A 1 114 ? -24.205 11.132  -1.546  1.00 35.70 ? 103 THR A CB  1 
ATOM   679  O  OG1 . THR A 1 114 ? -23.373 10.910  -0.403  1.00 37.79 ? 103 THR A OG1 1 
ATOM   680  C  CG2 . THR A 1 114 ? -25.607 10.659  -1.237  1.00 30.93 ? 103 THR A CG2 1 
ATOM   681  N  N   . SER A 1 115 ? -21.288 9.732   -2.302  1.00 36.76 ? 104 SER A N   1 
ATOM   682  C  CA  . SER A 1 115 ? -19.843 9.833   -2.452  1.00 34.05 ? 104 SER A CA  1 
ATOM   683  C  C   . SER A 1 115 ? -19.464 9.795   -3.927  1.00 33.18 ? 104 SER A C   1 
ATOM   684  O  O   . SER A 1 115 ? -20.173 9.224   -4.760  1.00 32.07 ? 104 SER A O   1 
ATOM   685  C  CB  . SER A 1 115 ? -19.145 8.690   -1.719  1.00 38.11 ? 104 SER A CB  1 
ATOM   686  O  OG  . SER A 1 115 ? -18.868 7.619   -2.601  1.00 35.92 ? 104 SER A OG  1 
ATOM   687  N  N   . LEU A 1 116 ? -18.312 10.389  -4.244  1.00 32.98 ? 105 LEU A N   1 
ATOM   688  C  CA  . LEU A 1 116 ? -17.967 10.607  -5.643  1.00 30.78 ? 105 LEU A CA  1 
ATOM   689  C  C   . LEU A 1 116 ? -17.670 9.295   -6.363  1.00 33.90 ? 105 LEU A C   1 
ATOM   690  O  O   . LEU A 1 116 ? -18.072 9.109   -7.518  1.00 34.54 ? 105 LEU A O   1 
ATOM   691  C  CB  . LEU A 1 116 ? -16.790 11.564  -5.732  1.00 24.88 ? 105 LEU A CB  1 
ATOM   692  C  CG  . LEU A 1 116 ? -15.985 11.576  -7.012  1.00 27.29 ? 105 LEU A CG  1 
ATOM   693  C  CD1 . LEU A 1 116 ? -16.731 12.331  -8.092  1.00 29.30 ? 105 LEU A CD1 1 
ATOM   694  C  CD2 . LEU A 1 116 ? -14.630 12.200  -6.731  1.00 29.68 ? 105 LEU A CD2 1 
ATOM   695  N  N   . HIS A 1 117 ? -16.983 8.362   -5.703  1.00 34.76 ? 106 HIS A N   1 
ATOM   696  C  CA  . HIS A 1 117 ? -16.705 7.100   -6.373  1.00 28.38 ? 106 HIS A CA  1 
ATOM   697  C  C   . HIS A 1 117 ? -17.945 6.219   -6.413  1.00 33.86 ? 106 HIS A C   1 
ATOM   698  O  O   . HIS A 1 117 ? -18.168 5.515   -7.404  1.00 35.82 ? 106 HIS A O   1 
ATOM   699  C  CB  . HIS A 1 117 ? -15.545 6.385   -5.690  1.00 29.90 ? 106 HIS A CB  1 
ATOM   700  C  CG  . HIS A 1 117 ? -14.212 7.010   -5.958  1.00 33.32 ? 106 HIS A CG  1 
ATOM   701  N  ND1 . HIS A 1 117 ? -13.194 6.348   -6.606  1.00 38.02 ? 106 HIS A ND1 1 
ATOM   702  C  CD2 . HIS A 1 117 ? -13.740 8.250   -5.687  1.00 36.92 ? 106 HIS A CD2 1 
ATOM   703  C  CE1 . HIS A 1 117 ? -12.148 7.147   -6.712  1.00 30.51 ? 106 HIS A CE1 1 
ATOM   704  N  NE2 . HIS A 1 117 ? -12.455 8.309   -6.167  1.00 33.62 ? 106 HIS A NE2 1 
ATOM   705  N  N   . GLY A 1 118 ? -18.759 6.256   -5.345  1.00 33.78 ? 107 GLY A N   1 
ATOM   706  C  CA  . GLY A 1 118 ? -20.036 5.556   -5.351  1.00 25.78 ? 107 GLY A CA  1 
ATOM   707  C  C   . GLY A 1 118 ? -20.929 5.972   -6.507  1.00 29.85 ? 107 GLY A C   1 
ATOM   708  O  O   . GLY A 1 118 ? -21.558 5.130   -7.156  1.00 28.11 ? 107 GLY A O   1 
ATOM   709  N  N   . GLN A 1 119 ? -20.979 7.271   -6.797  1.00 26.04 ? 108 GLN A N   1 
ATOM   710  C  CA  . GLN A 1 119 ? -21.750 7.724   -7.944  1.00 28.75 ? 108 GLN A CA  1 
ATOM   711  C  C   . GLN A 1 119 ? -21.076 7.355   -9.259  1.00 31.67 ? 108 GLN A C   1 
ATOM   712  O  O   . GLN A 1 119 ? -21.755 6.985   -10.228 1.00 29.82 ? 108 GLN A O   1 
ATOM   713  C  CB  . GLN A 1 119 ? -21.969 9.223   -7.856  1.00 30.25 ? 108 GLN A CB  1 
ATOM   714  C  CG  . GLN A 1 119 ? -22.749 9.590   -6.645  1.00 31.37 ? 108 GLN A CG  1 
ATOM   715  C  CD  . GLN A 1 119 ? -22.943 11.069  -6.515  1.00 30.89 ? 108 GLN A CD  1 
ATOM   716  O  OE1 . GLN A 1 119 ? -22.037 11.862  -6.781  1.00 28.26 ? 108 GLN A OE1 1 
ATOM   717  N  NE2 . GLN A 1 119 ? -24.138 11.459  -6.102  1.00 34.26 ? 108 GLN A NE2 1 
ATOM   718  N  N   . LEU A 1 120 ? -19.746 7.454   -9.319  1.00 28.28 ? 109 LEU A N   1 
ATOM   719  C  CA  . LEU A 1 120 ? -19.049 7.093   -10.548 1.00 27.02 ? 109 LEU A CA  1 
ATOM   720  C  C   . LEU A 1 120 ? -19.361 5.653   -10.955 1.00 29.79 ? 109 LEU A C   1 
ATOM   721  O  O   . LEU A 1 120 ? -19.554 5.363   -12.139 1.00 29.63 ? 109 LEU A O   1 
ATOM   722  C  CB  . LEU A 1 120 ? -17.548 7.314   -10.375 1.00 25.33 ? 109 LEU A CB  1 
ATOM   723  C  CG  . LEU A 1 120 ? -16.655 7.304   -11.621 1.00 28.56 ? 109 LEU A CG  1 
ATOM   724  C  CD1 . LEU A 1 120 ? -17.124 8.258   -12.711 1.00 26.62 ? 109 LEU A CD1 1 
ATOM   725  C  CD2 . LEU A 1 120 ? -15.233 7.610   -11.231 1.00 28.82 ? 109 LEU A CD2 1 
ATOM   726  N  N   . GLY A 1 121 ? -19.461 4.741   -9.988  1.00 29.55 ? 110 GLY A N   1 
ATOM   727  C  CA  . GLY A 1 121 ? -19.901 3.397   -10.314 1.00 28.67 ? 110 GLY A CA  1 
ATOM   728  C  C   . GLY A 1 121 ? -21.337 3.365   -10.809 1.00 33.67 ? 110 GLY A C   1 
ATOM   729  O  O   . GLY A 1 121 ? -21.636 2.763   -11.845 1.00 27.94 ? 110 GLY A O   1 
ATOM   730  N  N   . TYR A 1 122 ? -22.242 4.017   -10.073 1.00 30.40 ? 111 TYR A N   1 
ATOM   731  C  CA  . TYR A 1 122 ? -23.625 4.127   -10.511 1.00 28.29 ? 111 TYR A CA  1 
ATOM   732  C  C   . TYR A 1 122 ? -23.727 4.534   -11.979 1.00 30.63 ? 111 TYR A C   1 
ATOM   733  O  O   . TYR A 1 122 ? -24.555 3.990   -12.723 1.00 30.88 ? 111 TYR A O   1 
ATOM   734  C  CB  . TYR A 1 122 ? -24.372 5.132   -9.625  1.00 34.65 ? 111 TYR A CB  1 
ATOM   735  C  CG  . TYR A 1 122 ? -25.856 5.253   -9.952  1.00 35.64 ? 111 TYR A CG  1 
ATOM   736  C  CD1 . TYR A 1 122 ? -26.308 6.141   -10.930 1.00 31.15 ? 111 TYR A CD1 1 
ATOM   737  C  CD2 . TYR A 1 122 ? -26.804 4.473   -9.284  1.00 34.27 ? 111 TYR A CD2 1 
ATOM   738  C  CE1 . TYR A 1 122 ? -27.652 6.238   -11.232 1.00 32.76 ? 111 TYR A CE1 1 
ATOM   739  C  CE2 . TYR A 1 122 ? -28.157 4.575   -9.568  1.00 29.09 ? 111 TYR A CE2 1 
ATOM   740  C  CZ  . TYR A 1 122 ? -28.572 5.453   -10.543 1.00 34.26 ? 111 TYR A CZ  1 
ATOM   741  O  OH  . TYR A 1 122 ? -29.906 5.557   -10.842 1.00 31.68 ? 111 TYR A OH  1 
ATOM   742  N  N   . TYR A 1 123 ? -22.894 5.488   -12.415 1.00 30.05 ? 112 TYR A N   1 
ATOM   743  C  CA  . TYR A 1 123 ? -22.962 6.059   -13.760 1.00 29.90 ? 112 TYR A CA  1 
ATOM   744  C  C   . TYR A 1 123 ? -22.029 5.370   -14.745 1.00 29.73 ? 112 TYR A C   1 
ATOM   745  O  O   . TYR A 1 123 ? -21.758 5.922   -15.818 1.00 33.82 ? 112 TYR A O   1 
ATOM   746  C  CB  . TYR A 1 123 ? -22.641 7.564   -13.734 1.00 29.61 ? 112 TYR A CB  1 
ATOM   747  C  CG  . TYR A 1 123 ? -23.663 8.422   -13.023 1.00 33.09 ? 112 TYR A CG  1 
ATOM   748  C  CD1 . TYR A 1 123 ? -24.987 8.424   -13.437 1.00 33.27 ? 112 TYR A CD1 1 
ATOM   749  C  CD2 . TYR A 1 123 ? -23.315 9.204   -11.920 1.00 29.42 ? 112 TYR A CD2 1 
ATOM   750  C  CE1 . TYR A 1 123 ? -25.947 9.184   -12.797 1.00 31.37 ? 112 TYR A CE1 1 
ATOM   751  C  CE2 . TYR A 1 123 ? -24.271 9.974   -11.264 1.00 32.66 ? 112 TYR A CE2 1 
ATOM   752  C  CZ  . TYR A 1 123 ? -25.596 9.966   -11.720 1.00 34.58 ? 112 TYR A CZ  1 
ATOM   753  O  OH  . TYR A 1 123 ? -26.586 10.724  -11.115 1.00 25.32 ? 112 TYR A OH  1 
ATOM   754  N  N   . SER A 1 124 ? -21.523 4.188   -14.411 1.00 32.54 ? 113 SER A N   1 
ATOM   755  C  CA  . SER A 1 124 ? -20.562 3.499   -15.261 1.00 32.81 ? 113 SER A CA  1 
ATOM   756  C  C   . SER A 1 124 ? -20.872 2.013   -15.271 1.00 27.31 ? 113 SER A C   1 
ATOM   757  O  O   . SER A 1 124 ? -21.656 1.521   -14.455 1.00 29.76 ? 113 SER A O   1 
ATOM   758  C  CB  . SER A 1 124 ? -19.128 3.725   -14.781 1.00 35.29 ? 113 SER A CB  1 
ATOM   759  O  OG  . SER A 1 124 ? -19.076 3.593   -13.372 1.00 38.42 ? 113 SER A OG  1 
ATOM   760  N  N   . PHE A 1 125 ? -20.227 1.295   -16.211 1.00 31.82 ? 114 PHE A N   1 
ATOM   761  C  CA  . PHE A 1 125 ? -20.350 -0.159  -16.291 1.00 31.29 ? 114 PHE A CA  1 
ATOM   762  C  C   . PHE A 1 125 ? -19.017 -0.867  -16.519 1.00 34.42 ? 114 PHE A C   1 
ATOM   763  O  O   . PHE A 1 125 ? -19.012 -2.087  -16.721 1.00 41.85 ? 114 PHE A O   1 
ATOM   764  C  CB  . PHE A 1 125 ? -21.375 -0.580  -17.380 1.00 29.91 ? 114 PHE A CB  1 
ATOM   765  C  CG  . PHE A 1 125 ? -20.861 -0.518  -18.805 1.00 33.29 ? 114 PHE A CG  1 
ATOM   766  C  CD1 . PHE A 1 125 ? -20.248 -1.626  -19.395 1.00 34.62 ? 114 PHE A CD1 1 
ATOM   767  C  CD2 . PHE A 1 125 ? -21.058 0.623   -19.583 1.00 32.12 ? 114 PHE A CD2 1 
ATOM   768  C  CE1 . PHE A 1 125 ? -19.798 -1.583  -20.713 1.00 31.11 ? 114 PHE A CE1 1 
ATOM   769  C  CE2 . PHE A 1 125 ? -20.602 0.686   -20.902 1.00 28.26 ? 114 PHE A CE2 1 
ATOM   770  C  CZ  . PHE A 1 125 ? -19.974 -0.423  -21.467 1.00 33.84 ? 114 PHE A CZ  1 
ATOM   771  N  N   . ASP A 1 126 ? -17.895 -0.150  -16.496 1.00 34.92 ? 115 ASP A N   1 
ATOM   772  C  CA  . ASP A 1 126 ? -16.561 -0.742  -16.540 1.00 33.98 ? 115 ASP A CA  1 
ATOM   773  C  C   . ASP A 1 126 ? -15.588 0.332   -16.062 1.00 37.51 ? 115 ASP A C   1 
ATOM   774  O  O   . ASP A 1 126 ? -16.006 1.432   -15.682 1.00 32.94 ? 115 ASP A O   1 
ATOM   775  C  CB  . ASP A 1 126 ? -16.229 -1.308  -17.940 1.00 32.70 ? 115 ASP A CB  1 
ATOM   776  C  CG  . ASP A 1 126 ? -15.964 -0.227  -19.021 1.00 37.97 ? 115 ASP A CG  1 
ATOM   777  O  OD1 . ASP A 1 126 ? -16.132 0.991   -18.774 1.00 35.25 ? 115 ASP A OD1 1 
ATOM   778  O  OD2 . ASP A 1 126 ? -15.593 -0.622  -20.157 1.00 33.37 ? 115 ASP A OD2 1 
ATOM   779  N  N   . ALA A 1 127 ? -14.289 0.004   -16.040 1.00 33.90 ? 116 ALA A N   1 
ATOM   780  C  CA  . ALA A 1 127 ? -13.268 0.990   -15.697 1.00 37.68 ? 116 ALA A CA  1 
ATOM   781  C  C   . ALA A 1 127 ? -12.631 1.601   -16.935 1.00 40.17 ? 116 ALA A C   1 
ATOM   782  O  O   . ALA A 1 127 ? -11.516 2.122   -16.852 1.00 39.60 ? 116 ALA A O   1 
ATOM   783  C  CB  . ALA A 1 127 ? -12.184 0.390   -14.801 1.00 24.05 ? 116 ALA A CB  1 
ATOM   784  N  N   . GLY A 1 128 ? -13.313 1.538   -18.078 1.00 34.25 ? 117 GLY A N   1 
ATOM   785  C  CA  . GLY A 1 128 ? -12.816 2.041   -19.336 1.00 30.33 ? 117 GLY A CA  1 
ATOM   786  C  C   . GLY A 1 128 ? -13.094 3.498   -19.629 1.00 33.85 ? 117 GLY A C   1 
ATOM   787  O  O   . GLY A 1 128 ? -12.629 4.012   -20.648 1.00 33.90 ? 117 GLY A O   1 
ATOM   788  N  N   . ALA A 1 129 ? -13.844 4.197   -18.787 1.00 35.40 ? 118 ALA A N   1 
ATOM   789  C  CA  . ALA A 1 129 ? -14.082 5.609   -19.065 1.00 35.55 ? 118 ALA A CA  1 
ATOM   790  C  C   . ALA A 1 129 ? -13.401 6.460   -17.990 1.00 38.20 ? 118 ALA A C   1 
ATOM   791  O  O   . ALA A 1 129 ? -14.070 7.039   -17.123 1.00 34.49 ? 118 ALA A O   1 
ATOM   792  C  CB  . ALA A 1 129 ? -15.583 5.899   -19.161 1.00 26.54 ? 118 ALA A CB  1 
ATOM   793  N  N   . PRO A 1 130 ? -12.074 6.562   -18.011 1.00 35.80 ? 119 PRO A N   1 
ATOM   794  C  CA  . PRO A 1 130 ? -11.397 7.343   -16.980 1.00 37.51 ? 119 PRO A CA  1 
ATOM   795  C  C   . PRO A 1 130 ? -11.699 8.829   -17.146 1.00 42.00 ? 119 PRO A C   1 
ATOM   796  O  O   . PRO A 1 130 ? -11.795 9.348   -18.265 1.00 41.70 ? 119 PRO A O   1 
ATOM   797  C  CB  . PRO A 1 130 ? -9.915  7.028   -17.223 1.00 39.51 ? 119 PRO A CB  1 
ATOM   798  C  CG  . PRO A 1 130 ? -9.832  6.827   -18.694 1.00 23.88 ? 119 PRO A CG  1 
ATOM   799  C  CD  . PRO A 1 130 ? -11.141 6.174   -19.091 1.00 36.59 ? 119 PRO A CD  1 
ATOM   800  N  N   . ILE A 1 131 ? -11.863 9.507   -16.015 1.00 35.32 ? 120 ILE A N   1 
ATOM   801  C  CA  . ILE A 1 131 ? -12.126 10.939  -15.983 1.00 35.57 ? 120 ILE A CA  1 
ATOM   802  C  C   . ILE A 1 131 ? -10.834 11.649  -15.579 1.00 37.83 ? 120 ILE A C   1 
ATOM   803  O  O   . ILE A 1 131 ? -10.215 11.311  -14.560 1.00 38.91 ? 120 ILE A O   1 
ATOM   804  C  CB  . ILE A 1 131 ? -13.291 11.253  -15.030 1.00 35.14 ? 120 ILE A CB  1 
ATOM   805  C  CG1 . ILE A 1 131 ? -14.515 10.445  -15.466 1.00 28.92 ? 120 ILE A CG1 1 
ATOM   806  C  CG2 . ILE A 1 131 ? -13.595 12.764  -14.954 1.00 27.25 ? 120 ILE A CG2 1 
ATOM   807  C  CD1 . ILE A 1 131 ? -15.808 10.906  -14.867 1.00 26.23 ? 120 ILE A CD1 1 
ATOM   808  N  N   . THR A 1 132 ? -10.399 12.601  -16.398 1.00 31.64 ? 121 THR A N   1 
ATOM   809  C  CA  . THR A 1 132 ? -9.237  13.422  -16.080 1.00 29.53 ? 121 THR A CA  1 
ATOM   810  C  C   . THR A 1 132 ? -9.634  14.885  -16.192 1.00 29.32 ? 121 THR A C   1 
ATOM   811  O  O   . THR A 1 132 ? -10.817 15.226  -16.289 1.00 32.16 ? 121 THR A O   1 
ATOM   812  C  CB  . THR A 1 132 ? -8.026  13.176  -16.986 1.00 33.42 ? 121 THR A CB  1 
ATOM   813  O  OG1 . THR A 1 132 ? -8.396  13.398  -18.357 1.00 35.53 ? 121 THR A OG1 1 
ATOM   814  C  CG2 . THR A 1 132 ? -7.499  11.788  -16.805 1.00 35.60 ? 121 THR A CG2 1 
ATOM   815  N  N   . ALA A 1 133 ? -8.619  15.748  -16.235 1.00 30.74 ? 122 ALA A N   1 
ATOM   816  C  CA  . ALA A 1 133 ? -8.842  17.181  -16.110 1.00 27.97 ? 122 ALA A CA  1 
ATOM   817  C  C   . ALA A 1 133 ? -9.604  17.738  -17.306 1.00 27.83 ? 122 ALA A C   1 
ATOM   818  O  O   . ALA A 1 133 ? -10.458 18.618  -17.139 1.00 32.75 ? 122 ALA A O   1 
ATOM   819  C  CB  . ALA A 1 133 ? -7.504  17.892  -15.925 1.00 26.28 ? 122 ALA A CB  1 
ATOM   820  N  N   . GLY A 1 134 ? -9.327  17.238  -18.510 1.00 25.68 ? 123 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 134 ? -10.010 17.686  -19.709 1.00 26.81 ? 123 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 134 ? -11.088 16.773  -20.271 1.00 30.17 ? 123 GLY A C   1 
ATOM   823  O  O   . GLY A 1 134 ? -11.582 17.033  -21.376 1.00 28.37 ? 123 GLY A O   1 
ATOM   824  N  N   . THR A 1 135 ? -11.469 15.709  -19.557 1.00 30.33 ? 124 THR A N   1 
ATOM   825  C  CA  . THR A 1 135 ? -12.435 14.765  -20.109 1.00 31.30 ? 124 THR A CA  1 
ATOM   826  C  C   . THR A 1 135 ? -13.773 15.431  -20.430 1.00 32.95 ? 124 THR A C   1 
ATOM   827  O  O   . THR A 1 135 ? -14.340 15.183  -21.497 1.00 35.10 ? 124 THR A O   1 
ATOM   828  C  CB  . THR A 1 135 ? -12.638 13.585  -19.164 1.00 30.25 ? 124 THR A CB  1 
ATOM   829  O  OG1 . THR A 1 135 ? -11.379 12.943  -18.958 1.00 35.99 ? 124 THR A OG1 1 
ATOM   830  C  CG2 . THR A 1 135 ? -13.607 12.582  -19.780 1.00 28.46 ? 124 THR A CG2 1 
ATOM   831  N  N   . TRP A 1 136 ? -14.299 16.277  -19.535 1.00 32.62 ? 125 TRP A N   1 
ATOM   832  C  CA  . TRP A 1 136 ? -15.607 16.876  -19.807 1.00 29.76 ? 125 TRP A CA  1 
ATOM   833  C  C   . TRP A 1 136 ? -15.552 17.777  -21.035 1.00 30.18 ? 125 TRP A C   1 
ATOM   834  O  O   . TRP A 1 136 ? -16.344 17.617  -21.971 1.00 28.29 ? 125 TRP A O   1 
ATOM   835  C  CB  . TRP A 1 136 ? -16.130 17.656  -18.604 1.00 30.18 ? 125 TRP A CB  1 
ATOM   836  C  CG  . TRP A 1 136 ? -17.190 18.650  -18.992 1.00 35.76 ? 125 TRP A CG  1 
ATOM   837  C  CD1 . TRP A 1 136 ? -17.028 19.994  -19.163 1.00 37.82 ? 125 TRP A CD1 1 
ATOM   838  C  CD2 . TRP A 1 136 ? -18.573 18.374  -19.293 1.00 42.14 ? 125 TRP A CD2 1 
ATOM   839  N  NE1 . TRP A 1 136 ? -18.219 20.576  -19.554 1.00 35.92 ? 125 TRP A NE1 1 
ATOM   840  C  CE2 . TRP A 1 136 ? -19.181 19.606  -19.641 1.00 38.35 ? 125 TRP A CE2 1 
ATOM   841  C  CE3 . TRP A 1 136 ? -19.349 17.208  -19.321 1.00 39.24 ? 125 TRP A CE3 1 
ATOM   842  C  CZ2 . TRP A 1 136 ? -20.533 19.705  -19.995 1.00 37.65 ? 125 TRP A CZ2 1 
ATOM   843  C  CZ3 . TRP A 1 136 ? -20.701 17.308  -19.674 1.00 43.52 ? 125 TRP A CZ3 1 
ATOM   844  C  CH2 . TRP A 1 136 ? -21.277 18.553  -19.996 1.00 42.33 ? 125 TRP A CH2 1 
ATOM   845  N  N   . GLN A 1 137 ? -14.623 18.736  -21.052 1.00 35.32 ? 126 GLN A N   1 
ATOM   846  C  CA  . GLN A 1 137 ? -14.489 19.579  -22.236 1.00 33.63 ? 126 GLN A CA  1 
ATOM   847  C  C   . GLN A 1 137 ? -14.343 18.723  -23.480 1.00 29.46 ? 126 GLN A C   1 
ATOM   848  O  O   . GLN A 1 137 ? -15.021 18.958  -24.486 1.00 30.75 ? 126 GLN A O   1 
ATOM   849  C  CB  . GLN A 1 137 ? -13.312 20.551  -22.089 1.00 31.02 ? 126 GLN A CB  1 
ATOM   850  C  CG  . GLN A 1 137 ? -13.097 21.037  -20.656 1.00 42.57 ? 126 GLN A CG  1 
ATOM   851  C  CD  . GLN A 1 137 ? -11.826 21.866  -20.471 1.00 63.35 ? 126 GLN A CD  1 
ATOM   852  O  OE1 . GLN A 1 137 ? -11.887 23.099  -20.397 1.00 68.30 ? 126 GLN A OE1 1 
ATOM   853  N  NE2 . GLN A 1 137 ? -10.672 21.195  -20.387 1.00 60.45 ? 126 GLN A NE2 1 
ATOM   854  N  N   . ALA A 1 138 ? -13.507 17.688  -23.407 1.00 32.72 ? 127 ALA A N   1 
ATOM   855  C  CA  . ALA A 1 138 ? -13.269 16.863  -24.581 1.00 27.25 ? 127 ALA A CA  1 
ATOM   856  C  C   . ALA A 1 138 ? -14.549 16.175  -25.015 1.00 30.05 ? 127 ALA A C   1 
ATOM   857  O  O   . ALA A 1 138 ? -14.859 16.125  -26.209 1.00 28.72 ? 127 ALA A O   1 
ATOM   858  C  CB  . ALA A 1 138 ? -12.168 15.848  -24.294 1.00 24.93 ? 127 ALA A CB  1 
ATOM   859  N  N   . ALA A 1 139 ? -15.325 15.676  -24.051 1.00 29.97 ? 128 ALA A N   1 
ATOM   860  C  CA  . ALA A 1 139 ? -16.565 14.979  -24.371 1.00 33.02 ? 128 ALA A CA  1 
ATOM   861  C  C   . ALA A 1 139 ? -17.627 15.947  -24.885 1.00 30.38 ? 128 ALA A C   1 
ATOM   862  O  O   . ALA A 1 139 ? -18.338 15.649  -25.858 1.00 27.88 ? 128 ALA A O   1 
ATOM   863  C  CB  . ALA A 1 139 ? -17.064 14.221  -23.139 1.00 27.55 ? 128 ALA A CB  1 
ATOM   864  N  N   . TYR A 1 140 ? -17.739 17.111  -24.242 1.00 30.28 ? 129 TYR A N   1 
ATOM   865  C  CA  . TYR A 1 140 ? -18.661 18.143  -24.698 1.00 29.53 ? 129 TYR A CA  1 
ATOM   866  C  C   . TYR A 1 140 ? -18.365 18.541  -26.137 1.00 32.63 ? 129 TYR A C   1 
ATOM   867  O  O   . TYR A 1 140 ? -19.279 18.662  -26.969 1.00 33.94 ? 129 TYR A O   1 
ATOM   868  C  CB  . TYR A 1 140 ? -18.554 19.354  -23.769 1.00 30.41 ? 129 TYR A CB  1 
ATOM   869  C  CG  . TYR A 1 140 ? -19.445 20.505  -24.166 1.00 36.49 ? 129 TYR A CG  1 
ATOM   870  C  CD1 . TYR A 1 140 ? -18.987 21.503  -25.003 1.00 30.36 ? 129 TYR A CD1 1 
ATOM   871  C  CD2 . TYR A 1 140 ? -20.757 20.584  -23.712 1.00 35.61 ? 129 TYR A CD2 1 
ATOM   872  C  CE1 . TYR A 1 140 ? -19.799 22.544  -25.369 1.00 33.12 ? 129 TYR A CE1 1 
ATOM   873  C  CE2 . TYR A 1 140 ? -21.571 21.633  -24.067 1.00 31.22 ? 129 TYR A CE2 1 
ATOM   874  C  CZ  . TYR A 1 140 ? -21.086 22.612  -24.894 1.00 34.10 ? 129 TYR A CZ  1 
ATOM   875  O  OH  . TYR A 1 140 ? -21.903 23.660  -25.271 1.00 37.62 ? 129 TYR A OH  1 
ATOM   876  N  N   . SER A 1 141 ? -17.082 18.729  -26.441 1.00 30.11 ? 130 SER A N   1 
ATOM   877  C  CA  . SER A 1 141 ? -16.647 19.148  -27.765 1.00 27.79 ? 130 SER A CA  1 
ATOM   878  C  C   . SER A 1 141 ? -17.037 18.136  -28.842 1.00 26.58 ? 130 SER A C   1 
ATOM   879  O  O   . SER A 1 141 ? -17.452 18.518  -29.939 1.00 31.63 ? 130 SER A O   1 
ATOM   880  C  CB  . SER A 1 141 ? -15.133 19.355  -27.721 1.00 30.93 ? 130 SER A CB  1 
ATOM   881  O  OG  . SER A 1 141 ? -14.710 20.420  -28.540 1.00 43.45 ? 130 SER A OG  1 
ATOM   882  N  N   . ALA A 1 142 ? -16.888 16.841  -28.560 1.00 27.96 ? 131 ALA A N   1 
ATOM   883  C  CA  . ALA A 1 142 ? -17.217 15.809  -29.545 1.00 28.42 ? 131 ALA A CA  1 
ATOM   884  C  C   . ALA A 1 142 ? -18.695 15.837  -29.911 1.00 33.58 ? 131 ALA A C   1 
ATOM   885  O  O   . ALA A 1 142 ? -19.062 15.680  -31.088 1.00 26.21 ? 131 ALA A O   1 
ATOM   886  C  CB  . ALA A 1 142 ? -16.845 14.430  -29.003 1.00 25.64 ? 131 ALA A CB  1 
ATOM   887  N  N   . ALA A 1 143 ? -19.558 16.006  -28.903 1.00 33.04 ? 132 ALA A N   1 
ATOM   888  C  CA  . ALA A 1 143 ? -20.988 16.126  -29.143 1.00 28.44 ? 132 ALA A CA  1 
ATOM   889  C  C   . ALA A 1 143 ? -21.311 17.327  -30.036 1.00 32.97 ? 132 ALA A C   1 
ATOM   890  O  O   . ALA A 1 143 ? -22.253 17.263  -30.842 1.00 31.71 ? 132 ALA A O   1 
ATOM   891  C  CB  . ALA A 1 143 ? -21.719 16.214  -27.801 1.00 23.42 ? 132 ALA A CB  1 
ATOM   892  N  N   . GLN A 1 144 ? -20.534 18.419  -29.923 1.00 27.45 ? 133 GLN A N   1 
ATOM   893  C  CA  . GLN A 1 144 ? -20.750 19.588  -30.776 1.00 26.51 ? 133 GLN A CA  1 
ATOM   894  C  C   . GLN A 1 144 ? -20.343 19.310  -32.219 1.00 28.20 ? 133 GLN A C   1 
ATOM   895  O  O   . GLN A 1 144 ? -21.051 19.700  -33.159 1.00 26.61 ? 133 GLN A O   1 
ATOM   896  C  CB  . GLN A 1 144 ? -19.985 20.796  -30.223 1.00 24.47 ? 133 GLN A CB  1 
ATOM   897  C  CG  . GLN A 1 144 ? -20.505 21.354  -28.890 1.00 26.19 ? 133 GLN A CG  1 
ATOM   898  C  CD  . GLN A 1 144 ? -22.026 21.352  -28.773 1.00 28.99 ? 133 GLN A CD  1 
ATOM   899  O  OE1 . GLN A 1 144 ? -22.758 21.588  -29.740 1.00 32.27 ? 133 GLN A OE1 1 
ATOM   900  N  NE2 . GLN A 1 144 ? -22.503 21.097  -27.582 1.00 28.14 ? 133 GLN A NE2 1 
ATOM   901  N  N   . VAL A 1 145 ? -19.195 18.653  -32.407 1.00 30.18 ? 134 VAL A N   1 
ATOM   902  C  CA  . VAL A 1 145 ? -18.776 18.176  -33.724 1.00 29.94 ? 134 VAL A CA  1 
ATOM   903  C  C   . VAL A 1 145 ? -19.898 17.359  -34.368 1.00 30.43 ? 134 VAL A C   1 
ATOM   904  O  O   . VAL A 1 145 ? -20.287 17.585  -35.526 1.00 25.37 ? 134 VAL A O   1 
ATOM   905  C  CB  . VAL A 1 145 ? -17.464 17.373  -33.586 1.00 27.68 ? 134 VAL A CB  1 
ATOM   906  C  CG1 . VAL A 1 145 ? -17.114 16.598  -34.865 1.00 22.55 ? 134 VAL A CG1 1 
ATOM   907  C  CG2 . VAL A 1 145 ? -16.337 18.301  -33.181 1.00 21.20 ? 134 VAL A CG2 1 
ATOM   908  N  N   . ALA A 1 146 ? -20.461 16.420  -33.603 1.00 28.25 ? 135 ALA A N   1 
ATOM   909  C  CA  . ALA A 1 146 ? -21.590 15.647  -34.102 1.00 27.15 ? 135 ALA A CA  1 
ATOM   910  C  C   . ALA A 1 146 ? -22.759 16.555  -34.436 1.00 31.07 ? 135 ALA A C   1 
ATOM   911  O  O   . ALA A 1 146 ? -23.384 16.407  -35.492 1.00 30.62 ? 135 ALA A O   1 
ATOM   912  C  CB  . ALA A 1 146 ? -22.012 14.585  -33.085 1.00 23.48 ? 135 ALA A CB  1 
ATOM   913  N  N   . LEU A 1 147 ? -23.074 17.504  -33.538 1.00 28.16 ? 136 LEU A N   1 
ATOM   914  C  CA  . LEU A 1 147 ? -24.229 18.374  -33.749 1.00 25.03 ? 136 LEU A CA  1 
ATOM   915  C  C   . LEU A 1 147 ? -24.000 19.324  -34.913 1.00 29.31 ? 136 LEU A C   1 
ATOM   916  O  O   . LEU A 1 147 ? -24.917 19.569  -35.709 1.00 31.34 ? 136 LEU A O   1 
ATOM   917  C  CB  . LEU A 1 147 ? -24.538 19.168  -32.487 1.00 27.23 ? 136 LEU A CB  1 
ATOM   918  C  CG  . LEU A 1 147 ? -25.220 18.417  -31.355 1.00 26.41 ? 136 LEU A CG  1 
ATOM   919  C  CD1 . LEU A 1 147 ? -24.894 19.107  -30.065 1.00 25.60 ? 136 LEU A CD1 1 
ATOM   920  C  CD2 . LEU A 1 147 ? -26.728 18.322  -31.583 1.00 23.85 ? 136 LEU A CD2 1 
ATOM   921  N  N   . THR A 1 148 ? -22.788 19.869  -35.031 1.00 25.07 ? 137 THR A N   1 
ATOM   922  C  CA  . THR A 1 148 ? -22.459 20.672  -36.202 1.00 33.42 ? 137 THR A CA  1 
ATOM   923  C  C   . THR A 1 148 ? -22.727 19.883  -37.478 1.00 35.28 ? 137 THR A C   1 
ATOM   924  O  O   . THR A 1 148 ? -23.549 20.287  -38.314 1.00 36.05 ? 137 THR A O   1 
ATOM   925  C  CB  . THR A 1 148 ? -20.995 21.141  -36.145 1.00 30.41 ? 137 THR A CB  1 
ATOM   926  O  OG1 . THR A 1 148 ? -20.793 21.973  -34.997 1.00 30.03 ? 137 THR A OG1 1 
ATOM   927  C  CG2 . THR A 1 148 ? -20.612 21.905  -37.407 1.00 21.97 ? 137 THR A CG2 1 
ATOM   928  N  N   . ALA A 1 149 ? -22.052 18.730  -37.626 1.00 31.21 ? 138 ALA A N   1 
ATOM   929  C  CA  . ALA A 1 149 ? -22.219 17.907  -38.823 1.00 32.09 ? 138 ALA A CA  1 
ATOM   930  C  C   . ALA A 1 149 ? -23.683 17.536  -39.035 1.00 29.05 ? 138 ALA A C   1 
ATOM   931  O  O   . ALA A 1 149 ? -24.163 17.475  -40.173 1.00 32.15 ? 138 ALA A O   1 
ATOM   932  C  CB  . ALA A 1 149 ? -21.345 16.654  -38.720 1.00 28.60 ? 138 ALA A CB  1 
ATOM   933  N  N   . GLN A 1 150 ? -24.402 17.297  -37.942 1.00 28.12 ? 139 GLN A N   1 
ATOM   934  C  CA  . GLN A 1 150 ? -25.842 17.096  -38.000 1.00 32.86 ? 139 GLN A CA  1 
ATOM   935  C  C   . GLN A 1 150 ? -26.531 18.285  -38.664 1.00 34.40 ? 139 GLN A C   1 
ATOM   936  O  O   . GLN A 1 150 ? -27.395 18.118  -39.536 1.00 31.59 ? 139 GLN A O   1 
ATOM   937  C  CB  . GLN A 1 150 ? -26.366 16.880  -36.575 1.00 31.29 ? 139 GLN A CB  1 
ATOM   938  C  CG  . GLN A 1 150 ? -27.787 16.390  -36.475 1.00 30.78 ? 139 GLN A CG  1 
ATOM   939  C  CD  . GLN A 1 150 ? -28.811 17.496  -36.630 1.00 34.05 ? 139 GLN A CD  1 
ATOM   940  O  OE1 . GLN A 1 150 ? -28.669 18.585  -36.073 1.00 33.77 ? 139 GLN A OE1 1 
ATOM   941  N  NE2 . GLN A 1 150 ? -29.854 17.220  -37.397 1.00 36.09 ? 139 GLN A NE2 1 
ATOM   942  N  N   . HIS A 1 151 ? -26.148 19.499  -38.271 1.00 30.55 ? 140 HIS A N   1 
ATOM   943  C  CA  . HIS A 1 151 ? -26.850 20.682  -38.759 1.00 36.47 ? 140 HIS A CA  1 
ATOM   944  C  C   . HIS A 1 151 ? -26.547 20.964  -40.221 1.00 37.53 ? 140 HIS A C   1 
ATOM   945  O  O   . HIS A 1 151 ? -27.372 21.585  -40.905 1.00 35.96 ? 140 HIS A O   1 
ATOM   946  C  CB  . HIS A 1 151 ? -26.503 21.882  -37.881 1.00 38.68 ? 140 HIS A CB  1 
ATOM   947  C  CG  . HIS A 1 151 ? -27.342 21.958  -36.645 1.00 44.09 ? 140 HIS A CG  1 
ATOM   948  N  ND1 . HIS A 1 151 ? -28.321 22.913  -36.467 1.00 40.23 ? 140 HIS A ND1 1 
ATOM   949  C  CD2 . HIS A 1 151 ? -27.392 21.155  -35.551 1.00 41.87 ? 140 HIS A CD2 1 
ATOM   950  C  CE1 . HIS A 1 151 ? -28.919 22.710  -35.303 1.00 50.25 ? 140 HIS A CE1 1 
ATOM   951  N  NE2 . HIS A 1 151 ? -28.376 21.648  -34.728 1.00 45.29 ? 140 HIS A NE2 1 
ATOM   952  N  N   . GLU A 1 152 ? -25.380 20.517  -40.706 1.00 30.06 ? 141 GLU A N   1 
ATOM   953  C  CA  . GLU A 1 152 ? -25.085 20.549  -42.134 1.00 31.98 ? 141 GLU A CA  1 
ATOM   954  C  C   . GLU A 1 152 ? -26.150 19.823  -42.949 1.00 35.01 ? 141 GLU A C   1 
ATOM   955  O  O   . GLU A 1 152 ? -26.561 20.299  -44.014 1.00 27.70 ? 141 GLU A O   1 
ATOM   956  C  CB  . GLU A 1 152 ? -23.721 19.908  -42.394 1.00 42.03 ? 141 GLU A CB  1 
ATOM   957  C  CG  . GLU A 1 152 ? -22.543 20.572  -41.692 1.00 45.33 ? 141 GLU A CG  1 
ATOM   958  C  CD  . GLU A 1 152 ? -22.412 22.053  -42.025 1.00 58.92 ? 141 GLU A CD  1 
ATOM   959  O  OE1 . GLU A 1 152 ? -22.944 22.481  -43.085 1.00 44.26 ? 141 GLU A OE1 1 
ATOM   960  O  OE2 . GLU A 1 152 ? -21.763 22.783  -41.229 1.00 65.16 ? 141 GLU A OE2 1 
ATOM   961  N  N   . ILE A 1 153 ? -26.580 18.646  -42.487 1.00 34.69 ? 142 ILE A N   1 
ATOM   962  C  CA  . ILE A 1 153 ? -27.578 17.895  -43.238 1.00 35.62 ? 142 ILE A CA  1 
ATOM   963  C  C   . ILE A 1 153 ? -28.929 18.596  -43.168 1.00 37.31 ? 142 ILE A C   1 
ATOM   964  O  O   . ILE A 1 153 ? -29.678 18.628  -44.152 1.00 36.31 ? 142 ILE A O   1 
ATOM   965  C  CB  . ILE A 1 153 ? -27.650 16.440  -42.738 1.00 33.42 ? 142 ILE A CB  1 
ATOM   966  C  CG1 . ILE A 1 153 ? -26.475 15.648  -43.294 1.00 26.15 ? 142 ILE A CG1 1 
ATOM   967  C  CG2 . ILE A 1 153 ? -28.979 15.775  -43.127 1.00 28.62 ? 142 ILE A CG2 1 
ATOM   968  C  CD1 . ILE A 1 153 ? -25.986 14.619  -42.351 1.00 30.30 ? 142 ILE A CD1 1 
ATOM   969  N  N   . THR A 1 154 ? -29.250 19.191  -42.014 1.00 38.73 ? 143 THR A N   1 
ATOM   970  C  CA  . THR A 1 154 ? -30.500 19.939  -41.886 1.00 34.68 ? 143 THR A CA  1 
ATOM   971  C  C   . THR A 1 154 ? -30.509 21.147  -42.804 1.00 30.99 ? 143 THR A C   1 
ATOM   972  O  O   . THR A 1 154 ? -31.553 21.504  -43.359 1.00 32.75 ? 143 THR A O   1 
ATOM   973  C  CB  . THR A 1 154 ? -30.715 20.379  -40.438 1.00 34.99 ? 143 THR A CB  1 
ATOM   974  O  OG1 . THR A 1 154 ? -30.697 19.229  -39.589 1.00 34.79 ? 143 THR A OG1 1 
ATOM   975  C  CG2 . THR A 1 154 ? -32.052 21.107  -40.282 1.00 27.99 ? 143 THR A CG2 1 
ATOM   976  N  N   . ASN A 1 155 ? -29.355 21.786  -42.983 1.00 28.27 ? 144 ASN A N   1 
ATOM   977  C  CA  . ASN A 1 155 ? -29.238 22.945  -43.852 1.00 30.17 ? 144 ASN A CA  1 
ATOM   978  C  C   . ASN A 1 155 ? -29.013 22.571  -45.320 1.00 30.93 ? 144 ASN A C   1 
ATOM   979  O  O   . ASN A 1 155 ? -28.515 23.391  -46.100 1.00 35.79 ? 144 ASN A O   1 
ATOM   980  C  CB  . ASN A 1 155 ? -28.129 23.869  -43.342 1.00 26.94 ? 144 ASN A CB  1 
ATOM   981  C  CG  . ASN A 1 155 ? -28.688 25.152  -42.754 1.00 45.32 ? 144 ASN A CG  1 
ATOM   982  O  OD1 . ASN A 1 155 ? -29.763 25.626  -43.157 1.00 46.95 ? 144 ASN A OD1 1 
ATOM   983  N  ND2 . ASN A 1 155 ? -27.988 25.705  -41.770 1.00 53.12 ? 144 ASN A ND2 1 
ATOM   984  N  N   . GLY A 1 156 ? -29.375 21.362  -45.722 1.00 29.92 ? 145 GLY A N   1 
ATOM   985  C  CA  . GLY A 1 156 ? -29.407 20.991  -47.121 1.00 33.87 ? 145 GLY A CA  1 
ATOM   986  C  C   . GLY A 1 156 ? -28.426 19.913  -47.527 1.00 34.17 ? 145 GLY A C   1 
ATOM   987  O  O   . GLY A 1 156 ? -28.648 19.256  -48.553 1.00 33.30 ? 145 GLY A O   1 
ATOM   988  N  N   . ALA A 1 157 ? -27.352 19.693  -46.776 1.00 31.30 ? 146 ALA A N   1 
ATOM   989  C  CA  . ALA A 1 157 ? -26.350 18.748  -47.244 1.00 28.18 ? 146 ALA A CA  1 
ATOM   990  C  C   . ALA A 1 157 ? -26.902 17.333  -47.203 1.00 31.98 ? 146 ALA A C   1 
ATOM   991  O  O   . ALA A 1 157 ? -27.788 17.004  -46.410 1.00 33.34 ? 146 ALA A O   1 
ATOM   992  C  CB  . ALA A 1 157 ? -25.073 18.836  -46.414 1.00 26.14 ? 146 ALA A CB  1 
ATOM   993  N  N   . HIS A 1 158 ? -26.383 16.501  -48.089 1.00 32.01 ? 147 HIS A N   1 
ATOM   994  C  CA  . HIS A 1 158 ? -26.816 15.124  -48.164 1.00 26.58 ? 147 HIS A CA  1 
ATOM   995  C  C   . HIS A 1 158 ? -26.038 14.224  -47.220 1.00 36.36 ? 147 HIS A C   1 
ATOM   996  O  O   . HIS A 1 158 ? -26.552 13.170  -46.820 1.00 34.04 ? 147 HIS A O   1 
ATOM   997  C  CB  . HIS A 1 158 ? -26.675 14.628  -49.599 1.00 27.24 ? 147 HIS A CB  1 
ATOM   998  C  CG  . HIS A 1 158 ? -27.143 13.221  -49.798 1.00 42.95 ? 147 HIS A CG  1 
ATOM   999  N  ND1 . HIS A 1 158 ? -28.476 12.867  -49.736 1.00 39.13 ? 147 HIS A ND1 1 
ATOM   1000 C  CD2 . HIS A 1 158 ? -26.458 12.080  -50.057 1.00 35.64 ? 147 HIS A CD2 1 
ATOM   1001 C  CE1 . HIS A 1 158 ? -28.591 11.568  -49.958 1.00 33.33 ? 147 HIS A CE1 1 
ATOM   1002 N  NE2 . HIS A 1 158 ? -27.382 11.068  -50.150 1.00 39.22 ? 147 HIS A NE2 1 
ATOM   1003 N  N   . SER A 1 159 ? -24.820 14.613  -46.849 1.00 35.10 ? 148 SER A N   1 
ATOM   1004 C  CA  . SER A 1 159 ? -24.021 13.806  -45.939 1.00 32.96 ? 148 SER A CA  1 
ATOM   1005 C  C   . SER A 1 159 ? -23.022 14.700  -45.228 1.00 36.42 ? 148 SER A C   1 
ATOM   1006 O  O   . SER A 1 159 ? -22.693 15.799  -45.690 1.00 37.52 ? 148 SER A O   1 
ATOM   1007 C  CB  . SER A 1 159 ? -23.290 12.675  -46.667 1.00 33.01 ? 148 SER A CB  1 
ATOM   1008 O  OG  . SER A 1 159 ? -22.303 13.184  -47.547 1.00 32.97 ? 148 SER A OG  1 
ATOM   1009 N  N   . ALA A 1 160 ? -22.535 14.207  -44.096 1.00 38.37 ? 149 ALA A N   1 
ATOM   1010 C  CA  . ALA A 1 160 ? -21.486 14.895  -43.362 1.00 38.72 ? 149 ALA A CA  1 
ATOM   1011 C  C   . ALA A 1 160 ? -20.653 13.853  -42.631 1.00 33.65 ? 149 ALA A C   1 
ATOM   1012 O  O   . ALA A 1 160 ? -21.032 12.683  -42.531 1.00 32.42 ? 149 ALA A O   1 
ATOM   1013 C  CB  . ALA A 1 160 ? -22.064 15.926  -42.388 1.00 34.35 ? 149 ALA A CB  1 
ATOM   1014 N  N   . PHE A 1 161 ? -19.515 14.292  -42.108 1.00 30.52 ? 150 PHE A N   1 
ATOM   1015 C  CA  . PHE A 1 161 ? -18.630 13.427  -41.340 1.00 29.55 ? 150 PHE A CA  1 
ATOM   1016 C  C   . PHE A 1 161 ? -18.291 14.123  -40.023 1.00 30.96 ? 150 PHE A C   1 
ATOM   1017 O  O   . PHE A 1 161 ? -17.548 15.114  -40.010 1.00 30.61 ? 150 PHE A O   1 
ATOM   1018 C  CB  . PHE A 1 161 ? -17.373 13.080  -42.147 1.00 24.83 ? 150 PHE A CB  1 
ATOM   1019 C  CG  . PHE A 1 161 ? -16.392 12.208  -41.401 1.00 29.15 ? 150 PHE A CG  1 
ATOM   1020 C  CD1 . PHE A 1 161 ? -16.843 11.232  -40.506 1.00 28.08 ? 150 PHE A CD1 1 
ATOM   1021 C  CD2 . PHE A 1 161 ? -15.017 12.379  -41.575 1.00 25.48 ? 150 PHE A CD2 1 
ATOM   1022 C  CE1 . PHE A 1 161 ? -15.943 10.447  -39.797 1.00 27.79 ? 150 PHE A CE1 1 
ATOM   1023 C  CE2 . PHE A 1 161 ? -14.118 11.605  -40.884 1.00 23.70 ? 150 PHE A CE2 1 
ATOM   1024 C  CZ  . PHE A 1 161 ? -14.578 10.632  -39.984 1.00 28.42 ? 150 PHE A CZ  1 
ATOM   1025 N  N   . ALA A 1 162 ? -18.834 13.601  -38.918 1.00 23.52 ? 151 ALA A N   1 
ATOM   1026 C  CA  . ALA A 1 162 ? -18.474 14.055  -37.573 1.00 29.06 ? 151 ALA A CA  1 
ATOM   1027 C  C   . ALA A 1 162 ? -17.290 13.229  -37.078 1.00 27.08 ? 151 ALA A C   1 
ATOM   1028 O  O   . ALA A 1 162 ? -17.447 12.083  -36.652 1.00 27.76 ? 151 ALA A O   1 
ATOM   1029 C  CB  . ALA A 1 162 ? -19.657 13.949  -36.617 1.00 19.95 ? 151 ALA A CB  1 
ATOM   1030 N  N   . LEU A 1 163 ? -16.095 13.812  -37.139 1.00 25.74 ? 152 LEU A N   1 
ATOM   1031 C  CA  . LEU A 1 163 ? -14.879 13.157  -36.645 1.00 28.69 ? 152 LEU A CA  1 
ATOM   1032 C  C   . LEU A 1 163 ? -14.760 13.351  -35.128 1.00 25.38 ? 152 LEU A C   1 
ATOM   1033 O  O   . LEU A 1 163 ? -14.037 14.215  -34.624 1.00 27.41 ? 152 LEU A O   1 
ATOM   1034 C  CB  . LEU A 1 163 ? -13.663 13.697  -37.388 1.00 27.90 ? 152 LEU A CB  1 
ATOM   1035 C  CG  . LEU A 1 163 ? -12.292 13.121  -37.031 1.00 30.60 ? 152 LEU A CG  1 
ATOM   1036 C  CD1 . LEU A 1 163 ? -12.285 11.591  -36.966 1.00 25.32 ? 152 LEU A CD1 1 
ATOM   1037 C  CD2 . LEU A 1 163 ? -11.291 13.623  -38.033 1.00 29.85 ? 152 LEU A CD2 1 
ATOM   1038 N  N   . CYS A 1 164 ? -15.472 12.500  -34.389 1.00 26.45 ? 153 CYS A N   1 
ATOM   1039 C  CA  . CYS A 1 164 ? -15.610 12.610  -32.940 1.00 21.31 ? 153 CYS A CA  1 
ATOM   1040 C  C   . CYS A 1 164 ? -14.545 11.797  -32.222 1.00 23.76 ? 153 CYS A C   1 
ATOM   1041 O  O   . CYS A 1 164 ? -14.331 10.622  -32.540 1.00 30.64 ? 153 CYS A O   1 
ATOM   1042 C  CB  . CYS A 1 164 ? -16.977 12.097  -32.483 1.00 29.59 ? 153 CYS A CB  1 
ATOM   1043 S  SG  . CYS A 1 164 ? -18.428 13.031  -32.961 1.00 28.86 ? 153 CYS A SG  1 
ATOM   1044 N  N   . ARG A 1 165 ? -13.908 12.417  -31.230 1.00 22.84 ? 154 ARG A N   1 
ATOM   1045 C  CA  . ARG A 1 165 ? -13.067 11.774  -30.229 1.00 28.52 ? 154 ARG A CA  1 
ATOM   1046 C  C   . ARG A 1 165 ? -13.345 12.557  -28.942 1.00 36.05 ? 154 ARG A C   1 
ATOM   1047 O  O   . ARG A 1 165 ? -13.240 13.804  -28.936 1.00 36.21 ? 154 ARG A O   1 
ATOM   1048 C  CB  . ARG A 1 165 ? -11.570 11.794  -30.589 1.00 31.21 ? 154 ARG A CB  1 
ATOM   1049 C  CG  . ARG A 1 165 ? -10.770 10.541  -30.148 1.00 45.85 ? 154 ARG A CG  1 
ATOM   1050 C  CD  . ARG A 1 165 ? -9.406  10.908  -29.514 1.00 62.70 ? 154 ARG A CD  1 
ATOM   1051 N  NE  . ARG A 1 165 ? -9.571  11.845  -28.401 1.00 69.88 ? 154 ARG A NE  1 
ATOM   1052 C  CZ  . ARG A 1 165 ? -8.819  12.918  -28.175 1.00 67.74 ? 154 ARG A CZ  1 
ATOM   1053 N  NH1 . ARG A 1 165 ? -7.767  13.206  -28.932 1.00 67.93 ? 154 ARG A NH1 1 
ATOM   1054 N  NH2 . ARG A 1 165 ? -9.138  13.732  -27.170 1.00 59.11 ? 154 ARG A NH2 1 
ATOM   1055 N  N   . PRO A 1 166 ? -13.738 11.894  -27.849 1.00 31.43 ? 155 PRO A N   1 
ATOM   1056 C  CA  . PRO A 1 166 ? -13.955 10.445  -27.677 1.00 33.76 ? 155 PRO A CA  1 
ATOM   1057 C  C   . PRO A 1 166 ? -15.160 9.881   -28.442 1.00 29.51 ? 155 PRO A C   1 
ATOM   1058 O  O   . PRO A 1 166 ? -16.080 10.604  -28.825 1.00 24.41 ? 155 PRO A O   1 
ATOM   1059 C  CB  . PRO A 1 166 ? -14.134 10.309  -26.155 1.00 35.37 ? 155 PRO A CB  1 
ATOM   1060 C  CG  . PRO A 1 166 ? -14.604 11.659  -25.696 1.00 36.96 ? 155 PRO A CG  1 
ATOM   1061 C  CD  . PRO A 1 166 ? -13.912 12.639  -26.593 1.00 27.14 ? 155 PRO A CD  1 
ATOM   1062 N  N   . PRO A 1 167 ? -15.169 8.572   -28.701 1.00 34.98 ? 156 PRO A N   1 
ATOM   1063 C  CA  . PRO A 1 167 ? -16.363 7.947   -29.292 1.00 33.58 ? 156 PRO A CA  1 
ATOM   1064 C  C   . PRO A 1 167 ? -17.512 7.968   -28.289 1.00 32.28 ? 156 PRO A C   1 
ATOM   1065 O  O   . PRO A 1 167 ? -17.347 8.351   -27.127 1.00 27.51 ? 156 PRO A O   1 
ATOM   1066 C  CB  . PRO A 1 167 ? -15.900 6.521   -29.609 1.00 31.57 ? 156 PRO A CB  1 
ATOM   1067 C  CG  . PRO A 1 167 ? -14.873 6.245   -28.561 1.00 33.31 ? 156 PRO A CG  1 
ATOM   1068 C  CD  . PRO A 1 167 ? -14.145 7.569   -28.347 1.00 28.20 ? 156 PRO A CD  1 
ATOM   1069 N  N   . GLY A 1 168 ? -18.693 7.542   -28.748 1.00 31.39 ? 157 GLY A N   1 
ATOM   1070 C  CA  . GLY A 1 168 ? -19.886 7.669   -27.931 1.00 24.68 ? 157 GLY A CA  1 
ATOM   1071 C  C   . GLY A 1 168 ? -20.806 6.472   -27.804 1.00 25.14 ? 157 GLY A C   1 
ATOM   1072 O  O   . GLY A 1 168 ? -21.581 6.423   -26.853 1.00 26.55 ? 157 GLY A O   1 
ATOM   1073 N  N   . HIS A 1 169 ? -20.723 5.486   -28.704 1.00 26.93 ? 158 HIS A N   1 
ATOM   1074 C  CA  . HIS A 1 169 ? -21.781 4.480   -28.822 1.00 28.72 ? 158 HIS A CA  1 
ATOM   1075 C  C   . HIS A 1 169 ? -21.858 3.492   -27.652 1.00 30.14 ? 158 HIS A C   1 
ATOM   1076 O  O   . HIS A 1 169 ? -22.860 2.767   -27.563 1.00 26.99 ? 158 HIS A O   1 
ATOM   1077 C  CB  . HIS A 1 169 ? -21.649 3.723   -30.155 1.00 26.97 ? 158 HIS A CB  1 
ATOM   1078 C  CG  . HIS A 1 169 ? -20.594 2.652   -30.174 1.00 28.49 ? 158 HIS A CG  1 
ATOM   1079 N  ND1 . HIS A 1 169 ? -20.669 1.556   -31.009 1.00 28.96 ? 158 HIS A ND1 1 
ATOM   1080 C  CD2 . HIS A 1 169 ? -19.432 2.520   -29.492 1.00 32.81 ? 158 HIS A CD2 1 
ATOM   1081 C  CE1 . HIS A 1 169 ? -19.611 0.787   -30.829 1.00 27.06 ? 158 HIS A CE1 1 
ATOM   1082 N  NE2 . HIS A 1 169 ? -18.840 1.350   -29.916 1.00 33.71 ? 158 HIS A NE2 1 
ATOM   1083 N  N   . HIS A 1 170 ? -20.864 3.448   -26.749 1.00 22.65 ? 159 HIS A N   1 
ATOM   1084 C  CA  . HIS A 1 170 ? -21.001 2.656   -25.526 1.00 22.21 ? 159 HIS A CA  1 
ATOM   1085 C  C   . HIS A 1 170 ? -21.650 3.424   -24.382 1.00 23.39 ? 159 HIS A C   1 
ATOM   1086 O  O   . HIS A 1 170 ? -21.925 2.828   -23.334 1.00 26.10 ? 159 HIS A O   1 
ATOM   1087 C  CB  . HIS A 1 170 ? -19.645 2.118   -25.027 1.00 24.67 ? 159 HIS A CB  1 
ATOM   1088 C  CG  . HIS A 1 170 ? -18.946 1.201   -25.988 1.00 28.97 ? 159 HIS A CG  1 
ATOM   1089 N  ND1 . HIS A 1 170 ? -19.530 0.060   -26.497 1.00 25.24 ? 159 HIS A ND1 1 
ATOM   1090 C  CD2 . HIS A 1 170 ? -17.704 1.261   -26.530 1.00 32.02 ? 159 HIS A CD2 1 
ATOM   1091 C  CE1 . HIS A 1 170 ? -18.687 -0.533  -27.321 1.00 28.35 ? 159 HIS A CE1 1 
ATOM   1092 N  NE2 . HIS A 1 170 ? -17.569 0.173   -27.357 1.00 31.77 ? 159 HIS A NE2 1 
ATOM   1093 N  N   . ALA A 1 171 ? -21.894 4.718   -24.543 1.00 24.01 ? 160 ALA A N   1 
ATOM   1094 C  CA  . ALA A 1 171 ? -22.506 5.521   -23.490 1.00 30.29 ? 160 ALA A CA  1 
ATOM   1095 C  C   . ALA A 1 171 ? -24.028 5.450   -23.588 1.00 28.42 ? 160 ALA A C   1 
ATOM   1096 O  O   . ALA A 1 171 ? -24.591 5.629   -24.672 1.00 24.35 ? 160 ALA A O   1 
ATOM   1097 C  CB  . ALA A 1 171 ? -22.033 6.972   -23.582 1.00 25.89 ? 160 ALA A CB  1 
ATOM   1098 N  N   . ALA A 1 172 ? -24.685 5.164   -22.461 1.00 25.88 ? 161 ALA A N   1 
ATOM   1099 C  CA  . ALA A 1 172 ? -26.140 5.165   -22.403 1.00 28.25 ? 161 ALA A CA  1 
ATOM   1100 C  C   . ALA A 1 172 ? -26.582 6.527   -21.889 1.00 28.24 ? 161 ALA A C   1 
ATOM   1101 O  O   . ALA A 1 172 ? -25.790 7.468   -21.837 1.00 26.86 ? 161 ALA A O   1 
ATOM   1102 C  CB  . ALA A 1 172 ? -26.680 4.017   -21.546 1.00 22.44 ? 161 ALA A CB  1 
ATOM   1103 N  N   . SER A 1 173 ? -27.859 6.648   -21.510 1.00 37.57 ? 162 SER A N   1 
ATOM   1104 C  CA  . SER A 1 173 ? -28.389 7.936   -21.068 1.00 31.99 ? 162 SER A CA  1 
ATOM   1105 C  C   . SER A 1 173 ? -27.699 8.430   -19.796 1.00 35.08 ? 162 SER A C   1 
ATOM   1106 O  O   . SER A 1 173 ? -27.449 9.633   -19.650 1.00 36.02 ? 162 SER A O   1 
ATOM   1107 C  CB  . SER A 1 173 ? -29.891 7.839   -20.849 1.00 28.40 ? 162 SER A CB  1 
ATOM   1108 O  OG  . SER A 1 173 ? -30.382 9.083   -20.378 1.00 40.62 ? 162 SER A OG  1 
ATOM   1109 N  N   . ASP A 1 174 ? -27.380 7.530   -18.863 1.00 27.82 ? 163 ASP A N   1 
ATOM   1110 C  CA  . ASP A 1 174 ? -26.615 7.932   -17.687 1.00 27.43 ? 163 ASP A CA  1 
ATOM   1111 C  C   . ASP A 1 174 ? -25.658 6.832   -17.256 1.00 30.05 ? 163 ASP A C   1 
ATOM   1112 O  O   . ASP A 1 174 ? -25.485 6.568   -16.063 1.00 32.45 ? 163 ASP A O   1 
ATOM   1113 C  CB  . ASP A 1 174 ? -27.533 8.329   -16.538 1.00 27.78 ? 163 ASP A CB  1 
ATOM   1114 C  CG  . ASP A 1 174 ? -28.536 7.259   -16.212 1.00 33.29 ? 163 ASP A CG  1 
ATOM   1115 O  OD1 . ASP A 1 174 ? -28.488 6.190   -16.867 1.00 36.65 ? 163 ASP A OD1 1 
ATOM   1116 O  OD2 . ASP A 1 174 ? -29.374 7.466   -15.303 1.00 30.05 ? 163 ASP A OD2 1 
ATOM   1117 N  N   . VAL A 1 175 ? -25.026 6.172   -18.224 1.00 26.86 ? 164 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 175 ? -23.957 5.212   -17.979 1.00 24.18 ? 164 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 175 ? -22.836 5.484   -18.969 1.00 26.28 ? 164 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 175 ? -23.071 5.528   -20.179 1.00 30.55 ? 164 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 175 ? -24.441 3.756   -18.118 1.00 27.06 ? 164 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 175 ? -23.481 2.807   -17.405 1.00 28.16 ? 164 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 175 ? -25.872 3.592   -17.591 1.00 26.40 ? 164 VAL A CG2 1 
ATOM   1124 N  N   . MET A 1 176 ? -21.623 5.655   -18.468 1.00 28.87 ? 165 MET A N   1 
ATOM   1125 C  CA  . MET A 1 176 ? -20.454 5.798   -19.327 1.00 30.96 ? 165 MET A CA  1 
ATOM   1126 C  C   . MET A 1 176 ? -19.626 4.518   -19.334 1.00 31.45 ? 165 MET A C   1 
ATOM   1127 O  O   . MET A 1 176 ? -19.680 3.703   -18.411 1.00 31.84 ? 165 MET A O   1 
ATOM   1128 C  CB  . MET A 1 176 ? -19.574 6.951   -18.855 1.00 31.67 ? 165 MET A CB  1 
ATOM   1129 C  CG  . MET A 1 176 ? -19.067 6.724   -17.453 1.00 30.69 ? 165 MET A CG  1 
ATOM   1130 S  SD  . MET A 1 176 ? -18.046 8.059   -16.868 1.00 32.45 ? 165 MET A SD  1 
ATOM   1131 C  CE  . MET A 1 176 ? -19.305 9.287   -16.416 1.00 30.79 ? 165 MET A CE  1 
ATOM   1132 N  N   . GLY A 1 177 ? -18.821 4.368   -20.372 1.00 28.71 ? 166 GLY A N   1 
ATOM   1133 C  CA  . GLY A 1 177 ? -17.962 3.207   -20.448 1.00 29.74 ? 166 GLY A CA  1 
ATOM   1134 C  C   . GLY A 1 177 ? -17.332 3.026   -21.812 1.00 32.75 ? 166 GLY A C   1 
ATOM   1135 O  O   . GLY A 1 177 ? -17.797 3.615   -22.798 1.00 25.48 ? 166 GLY A O   1 
ATOM   1136 N  N   . GLY A 1 178 ? -16.270 2.214   -21.873 1.00 33.25 ? 167 GLY A N   1 
ATOM   1137 C  CA  . GLY A 1 178 ? -15.566 1.930   -23.111 1.00 30.22 ? 167 GLY A CA  1 
ATOM   1138 C  C   . GLY A 1 178 ? -15.102 3.159   -23.870 1.00 37.20 ? 167 GLY A C   1 
ATOM   1139 O  O   . GLY A 1 178 ? -15.355 3.270   -25.074 1.00 34.05 ? 167 GLY A O   1 
ATOM   1140 N  N   . TYR A 1 179 ? -14.425 4.081   -23.173 1.00 32.20 ? 168 TYR A N   1 
ATOM   1141 C  CA  . TYR A 1 179 ? -14.000 5.375   -23.703 1.00 34.76 ? 168 TYR A CA  1 
ATOM   1142 C  C   . TYR A 1 179 ? -15.166 6.194   -24.290 1.00 32.12 ? 168 TYR A C   1 
ATOM   1143 O  O   . TYR A 1 179 ? -14.960 7.093   -25.115 1.00 29.55 ? 168 TYR A O   1 
ATOM   1144 C  CB  . TYR A 1 179 ? -12.869 5.208   -24.731 1.00 43.26 ? 168 TYR A CB  1 
ATOM   1145 C  CG  . TYR A 1 179 ? -12.027 6.478   -24.947 1.00 58.40 ? 168 TYR A CG  1 
ATOM   1146 C  CD1 . TYR A 1 179 ? -11.898 7.453   -23.938 1.00 48.06 ? 168 TYR A CD1 1 
ATOM   1147 C  CD2 . TYR A 1 179 ? -11.375 6.708   -26.172 1.00 63.35 ? 168 TYR A CD2 1 
ATOM   1148 C  CE1 . TYR A 1 179 ? -11.142 8.611   -24.143 1.00 51.36 ? 168 TYR A CE1 1 
ATOM   1149 C  CE2 . TYR A 1 179 ? -10.610 7.861   -26.388 1.00 62.54 ? 168 TYR A CE2 1 
ATOM   1150 C  CZ  . TYR A 1 179 ? -10.499 8.809   -25.373 1.00 69.16 ? 168 TYR A CZ  1 
ATOM   1151 O  OH  . TYR A 1 179 ? -9.742  9.947   -25.600 1.00 65.82 ? 168 TYR A OH  1 
ATOM   1152 N  N   . CYS A 1 180 ? -16.393 5.947   -23.846 1.00 33.73 ? 169 CYS A N   1 
ATOM   1153 C  CA  . CYS A 1 180 ? -17.551 6.713   -24.290 1.00 32.47 ? 169 CYS A CA  1 
ATOM   1154 C  C   . CYS A 1 180 ? -18.165 7.443   -23.104 1.00 31.17 ? 169 CYS A C   1 
ATOM   1155 O  O   . CYS A 1 180 ? -18.513 6.818   -22.095 1.00 30.88 ? 169 CYS A O   1 
ATOM   1156 C  CB  . CYS A 1 180 ? -18.581 5.809   -24.960 1.00 28.14 ? 169 CYS A CB  1 
ATOM   1157 S  SG  . CYS A 1 180 ? -17.984 5.076   -26.488 1.00 28.24 ? 169 CYS A SG  1 
ATOM   1158 N  N   . TYR A 1 181 ? -18.292 8.762   -23.227 1.00 28.44 ? 170 TYR A N   1 
ATOM   1159 C  CA  . TYR A 1 181 ? -18.859 9.603   -22.179 1.00 26.49 ? 170 TYR A CA  1 
ATOM   1160 C  C   . TYR A 1 181 ? -20.213 10.182  -22.546 1.00 25.57 ? 170 TYR A C   1 
ATOM   1161 O  O   . TYR A 1 181 ? -21.130 10.150  -21.728 1.00 26.75 ? 170 TYR A O   1 
ATOM   1162 C  CB  . TYR A 1 181 ? -17.883 10.733  -21.833 1.00 28.21 ? 170 TYR A CB  1 
ATOM   1163 C  CG  . TYR A 1 181 ? -16.534 10.203  -21.435 1.00 28.28 ? 170 TYR A CG  1 
ATOM   1164 C  CD1 . TYR A 1 181 ? -16.296 9.777   -20.139 1.00 29.22 ? 170 TYR A CD1 1 
ATOM   1165 C  CD2 . TYR A 1 181 ? -15.515 10.080  -22.361 1.00 30.87 ? 170 TYR A CD2 1 
ATOM   1166 C  CE1 . TYR A 1 181 ? -15.078 9.271   -19.770 1.00 31.27 ? 170 TYR A CE1 1 
ATOM   1167 C  CE2 . TYR A 1 181 ? -14.295 9.564   -21.999 1.00 31.39 ? 170 TYR A CE2 1 
ATOM   1168 C  CZ  . TYR A 1 181 ? -14.084 9.160   -20.704 1.00 29.39 ? 170 TYR A CZ  1 
ATOM   1169 O  OH  . TYR A 1 181 ? -12.874 8.637   -20.332 1.00 33.07 ? 170 TYR A OH  1 
ATOM   1170 N  N   . LEU A 1 182 ? -20.363 10.686  -23.770 1.00 31.95 ? 171 LEU A N   1 
ATOM   1171 C  CA  . LEU A 1 182 ? -21.642 11.127  -24.317 1.00 28.64 ? 171 LEU A CA  1 
ATOM   1172 C  C   . LEU A 1 182 ? -21.879 10.421  -25.641 1.00 23.05 ? 171 LEU A C   1 
ATOM   1173 O  O   . LEU A 1 182 ? -20.942 10.182  -26.404 1.00 20.49 ? 171 LEU A O   1 
ATOM   1174 C  CB  . LEU A 1 182 ? -21.686 12.660  -24.514 1.00 28.23 ? 171 LEU A CB  1 
ATOM   1175 C  CG  . LEU A 1 182 ? -21.243 13.547  -23.348 1.00 24.50 ? 171 LEU A CG  1 
ATOM   1176 C  CD1 . LEU A 1 182 ? -21.151 14.981  -23.824 1.00 24.92 ? 171 LEU A CD1 1 
ATOM   1177 C  CD2 . LEU A 1 182 ? -22.201 13.410  -22.165 1.00 23.42 ? 171 LEU A CD2 1 
ATOM   1178 N  N   . ASN A 1 183 ? -23.134 10.086  -25.917 1.00 25.52 ? 172 ASN A N   1 
ATOM   1179 C  CA  . ASN A 1 183 ? -23.452 9.335   -27.130 1.00 24.89 ? 172 ASN A CA  1 
ATOM   1180 C  C   . ASN A 1 183 ? -23.693 10.290  -28.295 1.00 30.33 ? 172 ASN A C   1 
ATOM   1181 O  O   . ASN A 1 183 ? -24.831 10.656  -28.606 1.00 33.34 ? 172 ASN A O   1 
ATOM   1182 C  CB  . ASN A 1 183 ? -24.645 8.422   -26.901 1.00 26.13 ? 172 ASN A CB  1 
ATOM   1183 C  CG  . ASN A 1 183 ? -24.699 7.311   -27.913 1.00 28.73 ? 172 ASN A CG  1 
ATOM   1184 O  OD1 . ASN A 1 183 ? -24.396 7.533   -29.083 1.00 26.41 ? 172 ASN A OD1 1 
ATOM   1185 N  ND2 . ASN A 1 183 ? -25.058 6.104   -27.474 1.00 28.97 ? 172 ASN A ND2 1 
ATOM   1186 N  N   . ASN A 1 184 ? -22.597 10.649  -28.978 1.00 30.06 ? 173 ASN A N   1 
ATOM   1187 C  CA  . ASN A 1 184 ? -22.638 11.573  -30.113 1.00 29.63 ? 173 ASN A CA  1 
ATOM   1188 C  C   . ASN A 1 184 ? -23.667 11.159  -31.172 1.00 28.15 ? 173 ASN A C   1 
ATOM   1189 O  O   . ASN A 1 184 ? -24.516 11.966  -31.573 1.00 27.99 ? 173 ASN A O   1 
ATOM   1190 C  CB  . ASN A 1 184 ? -21.239 11.680  -30.741 1.00 31.91 ? 173 ASN A CB  1 
ATOM   1191 C  CG  . ASN A 1 184 ? -20.145 11.856  -29.706 1.00 26.81 ? 173 ASN A CG  1 
ATOM   1192 O  OD1 . ASN A 1 184 ? -20.262 12.680  -28.817 1.00 28.19 ? 173 ASN A OD1 1 
ATOM   1193 N  ND2 . ASN A 1 184 ? -19.081 11.072  -29.815 1.00 29.86 ? 173 ASN A ND2 1 
ATOM   1194 N  N   . ALA A 1 185 ? -23.592 9.909   -31.647 1.00 23.37 ? 174 ALA A N   1 
ATOM   1195 C  CA  . ALA A 1 185 ? -24.546 9.418   -32.647 1.00 27.22 ? 174 ALA A CA  1 
ATOM   1196 C  C   . ALA A 1 185 ? -25.994 9.511   -32.158 1.00 31.37 ? 174 ALA A C   1 
ATOM   1197 O  O   . ALA A 1 185 ? -26.909 9.813   -32.942 1.00 28.44 ? 174 ALA A O   1 
ATOM   1198 C  CB  . ALA A 1 185 ? -24.215 7.976   -33.038 1.00 16.97 ? 174 ALA A CB  1 
ATOM   1199 N  N   . ALA A 1 186 ? -26.235 9.231   -30.874 1.00 26.71 ? 175 ALA A N   1 
ATOM   1200 C  CA  . ALA A 1 186 ? -27.605 9.303   -30.390 1.00 24.56 ? 175 ALA A CA  1 
ATOM   1201 C  C   . ALA A 1 186 ? -28.044 10.751  -30.248 1.00 33.74 ? 175 ALA A C   1 
ATOM   1202 O  O   . ALA A 1 186 ? -29.224 11.074  -30.460 1.00 28.74 ? 175 ALA A O   1 
ATOM   1203 C  CB  . ALA A 1 186 ? -27.728 8.557   -29.065 1.00 23.27 ? 175 ALA A CB  1 
ATOM   1204 N  N   . ILE A 1 187 ? -27.098 11.636  -29.903 1.00 31.10 ? 176 ILE A N   1 
ATOM   1205 C  CA  . ILE A 1 187 ? -27.410 13.051  -29.768 1.00 27.44 ? 176 ILE A CA  1 
ATOM   1206 C  C   . ILE A 1 187 ? -27.726 13.651  -31.140 1.00 28.52 ? 176 ILE A C   1 
ATOM   1207 O  O   . ILE A 1 187 ? -28.676 14.430  -31.294 1.00 29.61 ? 176 ILE A O   1 
ATOM   1208 C  CB  . ILE A 1 187 ? -26.247 13.764  -29.046 1.00 25.91 ? 176 ILE A CB  1 
ATOM   1209 C  CG1 . ILE A 1 187 ? -26.189 13.318  -27.579 1.00 24.45 ? 176 ILE A CG1 1 
ATOM   1210 C  CG2 . ILE A 1 187 ? -26.351 15.303  -29.169 1.00 23.24 ? 176 ILE A CG2 1 
ATOM   1211 C  CD1 . ILE A 1 187 ? -24.819 13.406  -26.901 1.00 19.58 ? 176 ILE A CD1 1 
ATOM   1212 N  N   . ALA A 1 188 ? -26.966 13.266  -32.163 1.00 30.51 ? 177 ALA A N   1 
ATOM   1213 C  CA  . ALA A 1 188 ? -27.251 13.725  -33.515 1.00 26.35 ? 177 ALA A CA  1 
ATOM   1214 C  C   . ALA A 1 188 ? -28.578 13.164  -34.022 1.00 26.45 ? 177 ALA A C   1 
ATOM   1215 O  O   . ALA A 1 188 ? -29.345 13.874  -34.677 1.00 26.41 ? 177 ALA A O   1 
ATOM   1216 C  CB  . ALA A 1 188 ? -26.099 13.338  -34.442 1.00 20.66 ? 177 ALA A CB  1 
ATOM   1217 N  N   . ALA A 1 189 ? -28.868 11.891  -33.731 1.00 27.91 ? 178 ALA A N   1 
ATOM   1218 C  CA  . ALA A 1 189 ? -30.142 11.308  -34.142 1.00 25.75 ? 178 ALA A CA  1 
ATOM   1219 C  C   . ALA A 1 189 ? -31.304 12.018  -33.468 1.00 29.54 ? 178 ALA A C   1 
ATOM   1220 O  O   . ALA A 1 189 ? -32.290 12.384  -34.121 1.00 32.55 ? 178 ALA A O   1 
ATOM   1221 C  CB  . ALA A 1 189 ? -30.179 9.814   -33.828 1.00 22.56 ? 178 ALA A CB  1 
ATOM   1222 N  N   . GLN A 1 190 ? -31.204 12.225  -32.153 1.00 29.01 ? 179 GLN A N   1 
ATOM   1223 C  CA  . GLN A 1 190 ? -32.264 12.943  -31.456 1.00 33.51 ? 179 GLN A CA  1 
ATOM   1224 C  C   . GLN A 1 190 ? -32.456 14.345  -32.027 1.00 29.92 ? 179 GLN A C   1 
ATOM   1225 O  O   . GLN A 1 190 ? -33.586 14.846  -32.078 1.00 29.42 ? 179 GLN A O   1 
ATOM   1226 C  CB  . GLN A 1 190 ? -31.977 13.015  -29.960 1.00 30.60 ? 179 GLN A CB  1 
ATOM   1227 C  CG  . GLN A 1 190 ? -33.115 13.677  -29.198 1.00 30.70 ? 179 GLN A CG  1 
ATOM   1228 C  CD  . GLN A 1 190 ? -34.408 12.904  -29.353 1.00 28.97 ? 179 GLN A CD  1 
ATOM   1229 O  OE1 . GLN A 1 190 ? -34.393 11.676  -29.314 1.00 23.53 ? 179 GLN A OE1 1 
ATOM   1230 N  NE2 . GLN A 1 190 ? -35.528 13.612  -29.544 1.00 25.39 ? 179 GLN A NE2 1 
ATOM   1231 N  N   . ALA A 1 191 ? -31.364 14.995  -32.453 1.00 28.21 ? 180 ALA A N   1 
ATOM   1232 C  CA  . ALA A 1 191 ? -31.483 16.305  -33.085 1.00 31.23 ? 180 ALA A CA  1 
ATOM   1233 C  C   . ALA A 1 191 ? -32.364 16.235  -34.326 1.00 30.42 ? 180 ALA A C   1 
ATOM   1234 O  O   . ALA A 1 191 ? -33.265 17.061  -34.494 1.00 28.75 ? 180 ALA A O   1 
ATOM   1235 C  CB  . ALA A 1 191 ? -30.104 16.870  -33.420 1.00 25.97 ? 180 ALA A CB  1 
ATOM   1236 N  N   . PHE A 1 192 ? -32.173 15.208  -35.163 1.00 32.82 ? 181 PHE A N   1 
ATOM   1237 C  CA  . PHE A 1 192 ? -32.977 15.053  -36.381 1.00 35.15 ? 181 PHE A CA  1 
ATOM   1238 C  C   . PHE A 1 192 ? -34.473 14.908  -36.077 1.00 31.90 ? 181 PHE A C   1 
ATOM   1239 O  O   . PHE A 1 192 ? -35.312 15.424  -36.823 1.00 32.60 ? 181 PHE A O   1 
ATOM   1240 C  CB  . PHE A 1 192 ? -32.476 13.851  -37.193 1.00 29.02 ? 181 PHE A CB  1 
ATOM   1241 C  CG  . PHE A 1 192 ? -31.269 14.148  -38.035 1.00 31.81 ? 181 PHE A CG  1 
ATOM   1242 C  CD1 . PHE A 1 192 ? -31.332 15.084  -39.060 1.00 30.51 ? 181 PHE A CD1 1 
ATOM   1243 C  CD2 . PHE A 1 192 ? -30.067 13.499  -37.801 1.00 30.27 ? 181 PHE A CD2 1 
ATOM   1244 C  CE1 . PHE A 1 192 ? -30.223 15.372  -39.839 1.00 28.30 ? 181 PHE A CE1 1 
ATOM   1245 C  CE2 . PHE A 1 192 ? -28.951 13.780  -38.581 1.00 30.61 ? 181 PHE A CE2 1 
ATOM   1246 C  CZ  . PHE A 1 192 ? -29.034 14.720  -39.605 1.00 31.70 ? 181 PHE A CZ  1 
ATOM   1247 N  N   . ILE A 1 193 ? -34.823 14.200  -34.994 1.00 30.48 ? 182 ILE A N   1 
ATOM   1248 C  CA  . ILE A 1 193 ? -36.224 14.030  -34.600 1.00 31.57 ? 182 ILE A CA  1 
ATOM   1249 C  C   . ILE A 1 193 ? -36.807 15.344  -34.069 1.00 35.73 ? 182 ILE A C   1 
ATOM   1250 O  O   . ILE A 1 193 ? -37.945 15.722  -34.394 1.00 31.13 ? 182 ILE A O   1 
ATOM   1251 C  CB  . ILE A 1 193 ? -36.337 12.907  -33.552 1.00 30.86 ? 182 ILE A CB  1 
ATOM   1252 C  CG1 . ILE A 1 193 ? -35.727 11.597  -34.079 1.00 33.04 ? 182 ILE A CG1 1 
ATOM   1253 C  CG2 . ILE A 1 193 ? -37.765 12.727  -33.129 1.00 22.75 ? 182 ILE A CG2 1 
ATOM   1254 C  CD1 . ILE A 1 193 ? -36.687 10.744  -34.887 1.00 29.57 ? 182 ILE A CD1 1 
ATOM   1255 N  N   . ASP A 1 194 ? -36.041 16.052  -33.230 1.00 36.76 ? 183 ASP A N   1 
ATOM   1256 C  CA  . ASP A 1 194 ? -36.483 17.331  -32.683 1.00 34.14 ? 183 ASP A CA  1 
ATOM   1257 C  C   . ASP A 1 194 ? -36.632 18.387  -33.761 1.00 29.74 ? 183 ASP A C   1 
ATOM   1258 O  O   . ASP A 1 194 ? -37.358 19.363  -33.561 1.00 31.46 ? 183 ASP A O   1 
ATOM   1259 C  CB  . ASP A 1 194 ? -35.506 17.810  -31.611 1.00 23.53 ? 183 ASP A CB  1 
ATOM   1260 C  CG  . ASP A 1 194 ? -35.675 17.063  -30.299 1.00 32.43 ? 183 ASP A CG  1 
ATOM   1261 O  OD1 . ASP A 1 194 ? -36.807 16.607  -29.986 1.00 30.17 ? 183 ASP A OD1 1 
ATOM   1262 O  OD2 . ASP A 1 194 ? -34.667 16.925  -29.579 1.00 36.32 ? 183 ASP A OD2 1 
ATOM   1263 N  N   . GLN A 1 195 ? -35.981 18.197  -34.901 1.00 31.23 ? 184 GLN A N   1 
ATOM   1264 C  CA  . GLN A 1 195 ? -36.041 19.109  -36.030 1.00 32.54 ? 184 GLN A CA  1 
ATOM   1265 C  C   . GLN A 1 195 ? -37.109 18.717  -37.063 1.00 32.06 ? 184 GLN A C   1 
ATOM   1266 O  O   . GLN A 1 195 ? -37.138 19.290  -38.155 1.00 33.89 ? 184 GLN A O   1 
ATOM   1267 C  CB  . GLN A 1 195 ? -34.652 19.196  -36.678 1.00 31.55 ? 184 GLN A CB  1 
ATOM   1268 C  CG  . GLN A 1 195 ? -33.581 19.838  -35.745 1.00 28.30 ? 184 GLN A CG  1 
ATOM   1269 C  CD  . GLN A 1 195 ? -32.151 19.656  -36.260 1.00 36.81 ? 184 GLN A CD  1 
ATOM   1270 O  OE1 . GLN A 1 195 ? -31.946 19.172  -37.367 1.00 39.04 ? 184 GLN A OE1 1 
ATOM   1271 N  NE2 . GLN A 1 195 ? -31.162 20.037  -35.454 1.00 36.05 ? 184 GLN A NE2 1 
ATOM   1272 N  N   . GLY A 1 196 ? -37.984 17.762  -36.751 1.00 28.04 ? 185 GLY A N   1 
ATOM   1273 C  CA  . GLY A 1 196 ? -39.138 17.505  -37.586 1.00 33.45 ? 185 GLY A CA  1 
ATOM   1274 C  C   . GLY A 1 196 ? -39.135 16.203  -38.359 1.00 31.56 ? 185 GLY A C   1 
ATOM   1275 O  O   . GLY A 1 196 ? -40.082 15.947  -39.111 1.00 27.81 ? 185 GLY A O   1 
ATOM   1276 N  N   . HIS A 1 197 ? -38.116 15.374  -38.217 1.00 32.60 ? 186 HIS A N   1 
ATOM   1277 C  CA  . HIS A 1 197 ? -38.121 14.100  -38.915 1.00 35.50 ? 186 HIS A CA  1 
ATOM   1278 C  C   . HIS A 1 197 ? -38.963 13.089  -38.136 1.00 34.70 ? 186 HIS A C   1 
ATOM   1279 O  O   . HIS A 1 197 ? -38.775 12.904  -36.930 1.00 34.43 ? 186 HIS A O   1 
ATOM   1280 C  CB  . HIS A 1 197 ? -36.692 13.596  -39.127 1.00 32.78 ? 186 HIS A CB  1 
ATOM   1281 C  CG  . HIS A 1 197 ? -35.895 14.404  -40.113 1.00 40.78 ? 186 HIS A CG  1 
ATOM   1282 N  ND1 . HIS A 1 197 ? -36.110 14.343  -41.476 1.00 39.95 ? 186 HIS A ND1 1 
ATOM   1283 C  CD2 . HIS A 1 197 ? -34.866 15.271  -39.936 1.00 37.89 ? 186 HIS A CD2 1 
ATOM   1284 C  CE1 . HIS A 1 197 ? -35.265 15.153  -42.091 1.00 36.03 ? 186 HIS A CE1 1 
ATOM   1285 N  NE2 . HIS A 1 197 ? -34.492 15.721  -41.181 1.00 33.59 ? 186 HIS A NE2 1 
ATOM   1286 N  N   . LYS A 1 198 ? -39.911 12.455  -38.830 1.00 36.27 ? 187 LYS A N   1 
ATOM   1287 C  CA  . LYS A 1 198 ? -40.747 11.435  -38.208 1.00 34.52 ? 187 LYS A CA  1 
ATOM   1288 C  C   . LYS A 1 198 ? -39.911 10.253  -37.733 1.00 35.25 ? 187 LYS A C   1 
ATOM   1289 O  O   . LYS A 1 198 ? -40.016 9.843   -36.574 1.00 44.46 ? 187 LYS A O   1 
ATOM   1290 C  CB  . LYS A 1 198 ? -41.833 10.976  -39.186 1.00 37.68 ? 187 LYS A CB  1 
ATOM   1291 C  CG  . LYS A 1 198 ? -42.986 10.249  -38.519 1.00 44.61 ? 187 LYS A CG  1 
ATOM   1292 C  CD  . LYS A 1 198 ? -43.661 9.281   -39.476 1.00 55.01 ? 187 LYS A CD  1 
ATOM   1293 C  CE  . LYS A 1 198 ? -44.941 8.702   -38.884 1.00 61.25 ? 187 LYS A CE  1 
ATOM   1294 N  NZ  . LYS A 1 198 ? -44.804 7.214   -38.692 1.00 58.02 ? 187 LYS A NZ  1 
ATOM   1295 N  N   . ARG A 1 199 ? -39.062 9.698   -38.608 1.00 37.22 ? 188 ARG A N   1 
ATOM   1296 C  CA  . ARG A 1 199 ? -38.270 8.504   -38.304 1.00 35.43 ? 188 ARG A CA  1 
ATOM   1297 C  C   . ARG A 1 199 ? -36.827 8.687   -38.761 1.00 33.76 ? 188 ARG A C   1 
ATOM   1298 O  O   . ARG A 1 199 ? -36.572 9.335   -39.779 1.00 32.37 ? 188 ARG A O   1 
ATOM   1299 C  CB  . ARG A 1 199 ? -38.873 7.250   -38.973 1.00 26.78 ? 188 ARG A CB  1 
ATOM   1300 C  CG  . ARG A 1 199 ? -40.077 6.720   -38.247 1.00 34.42 ? 188 ARG A CG  1 
ATOM   1301 C  CD  . ARG A 1 199 ? -40.920 5.724   -39.042 1.00 42.68 ? 188 ARG A CD  1 
ATOM   1302 N  NE  . ARG A 1 199 ? -41.886 5.063   -38.157 1.00 60.07 ? 188 ARG A NE  1 
ATOM   1303 C  CZ  . ARG A 1 199 ? -42.374 3.835   -38.318 1.00 50.75 ? 188 ARG A CZ  1 
ATOM   1304 N  NH1 . ARG A 1 199 ? -42.053 3.090   -39.362 1.00 41.56 ? 188 ARG A NH1 1 
ATOM   1305 N  NH2 . ARG A 1 199 ? -43.204 3.340   -37.403 1.00 53.67 ? 188 ARG A NH2 1 
ATOM   1306 N  N   . VAL A 1 200 ? -35.883 8.124   -37.997 1.00 30.17 ? 189 VAL A N   1 
ATOM   1307 C  CA  . VAL A 1 200 ? -34.479 8.025   -38.397 1.00 32.87 ? 189 VAL A CA  1 
ATOM   1308 C  C   . VAL A 1 200 ? -33.947 6.682   -37.918 1.00 31.42 ? 189 VAL A C   1 
ATOM   1309 O  O   . VAL A 1 200 ? -34.601 5.961   -37.161 1.00 31.04 ? 189 VAL A O   1 
ATOM   1310 C  CB  . VAL A 1 200 ? -33.580 9.154   -37.840 1.00 32.64 ? 189 VAL A CB  1 
ATOM   1311 C  CG1 . VAL A 1 200 ? -33.922 10.548  -38.455 1.00 24.21 ? 189 VAL A CG1 1 
ATOM   1312 C  CG2 . VAL A 1 200 ? -33.635 9.161   -36.319 1.00 29.80 ? 189 VAL A CG2 1 
ATOM   1313 N  N   . ALA A 1 201 ? -32.731 6.366   -38.354 1.00 28.29 ? 190 ALA A N   1 
ATOM   1314 C  CA  . ALA A 1 201 ? -32.149 5.049   -38.139 1.00 26.29 ? 190 ALA A CA  1 
ATOM   1315 C  C   . ALA A 1 201 ? -30.653 5.154   -37.884 1.00 34.46 ? 190 ALA A C   1 
ATOM   1316 O  O   . ALA A 1 201 ? -29.938 5.877   -38.592 1.00 31.01 ? 190 ALA A O   1 
ATOM   1317 C  CB  . ALA A 1 201 ? -32.389 4.130   -39.342 1.00 27.26 ? 190 ALA A CB  1 
ATOM   1318 N  N   . ILE A 1 202 ? -30.179 4.409   -36.884 1.00 29.46 ? 191 ILE A N   1 
ATOM   1319 C  CA  . ILE A 1 202 ? -28.756 4.311   -36.602 1.00 29.20 ? 191 ILE A CA  1 
ATOM   1320 C  C   . ILE A 1 202 ? -28.241 2.961   -37.093 1.00 32.28 ? 191 ILE A C   1 
ATOM   1321 O  O   . ILE A 1 202 ? -28.819 1.914   -36.776 1.00 33.28 ? 191 ILE A O   1 
ATOM   1322 C  CB  . ILE A 1 202 ? -28.474 4.529   -35.108 1.00 31.90 ? 191 ILE A CB  1 
ATOM   1323 C  CG1 . ILE A 1 202 ? -28.783 5.989   -34.762 1.00 29.28 ? 191 ILE A CG1 1 
ATOM   1324 C  CG2 . ILE A 1 202 ? -27.002 4.214   -34.785 1.00 29.17 ? 191 ILE A CG2 1 
ATOM   1325 C  CD1 . ILE A 1 202 ? -29.430 6.205   -33.455 1.00 25.09 ? 191 ILE A CD1 1 
ATOM   1326 N  N   . LEU A 1 203 ? -27.180 2.990   -37.902 1.00 30.64 ? 192 LEU A N   1 
ATOM   1327 C  CA  . LEU A 1 203 ? -26.465 1.795   -38.340 1.00 29.40 ? 192 LEU A CA  1 
ATOM   1328 C  C   . LEU A 1 203 ? -25.061 1.853   -37.750 1.00 27.73 ? 192 LEU A C   1 
ATOM   1329 O  O   . LEU A 1 203 ? -24.305 2.800   -38.007 1.00 30.63 ? 192 LEU A O   1 
ATOM   1330 C  CB  . LEU A 1 203 ? -26.420 1.703   -39.867 1.00 30.50 ? 192 LEU A CB  1 
ATOM   1331 C  CG  . LEU A 1 203 ? -25.441 0.716   -40.505 1.00 32.38 ? 192 LEU A CG  1 
ATOM   1332 C  CD1 . LEU A 1 203 ? -26.021 -0.696  -40.571 1.00 28.92 ? 192 LEU A CD1 1 
ATOM   1333 C  CD2 . LEU A 1 203 ? -25.063 1.200   -41.885 1.00 27.04 ? 192 LEU A CD2 1 
ATOM   1334 N  N   . ASP A 1 204 ? -24.727 0.861   -36.962 1.00 23.89 ? 193 ASP A N   1 
ATOM   1335 C  CA  . ASP A 1 204 ? -23.523 0.857   -36.140 1.00 25.19 ? 193 ASP A CA  1 
ATOM   1336 C  C   . ASP A 1 204 ? -22.573 -0.208  -36.676 1.00 28.09 ? 193 ASP A C   1 
ATOM   1337 O  O   . ASP A 1 204 ? -22.712 -1.391  -36.353 1.00 27.36 ? 193 ASP A O   1 
ATOM   1338 C  CB  . ASP A 1 204 ? -23.900 0.583   -34.695 1.00 26.08 ? 193 ASP A CB  1 
ATOM   1339 C  CG  . ASP A 1 204 ? -22.756 0.766   -33.758 1.00 27.16 ? 193 ASP A CG  1 
ATOM   1340 O  OD1 . ASP A 1 204 ? -21.631 0.333   -34.096 1.00 29.25 ? 193 ASP A OD1 1 
ATOM   1341 O  OD2 . ASP A 1 204 ? -22.990 1.342   -32.676 1.00 24.12 ? 193 ASP A OD2 1 
ATOM   1342 N  N   . VAL A 1 205 ? -21.599 0.224   -37.485 1.00 25.76 ? 194 VAL A N   1 
ATOM   1343 C  CA  . VAL A 1 205 ? -20.657 -0.681  -38.133 1.00 22.91 ? 194 VAL A CA  1 
ATOM   1344 C  C   . VAL A 1 205 ? -19.396 -0.894  -37.303 1.00 31.26 ? 194 VAL A C   1 
ATOM   1345 O  O   . VAL A 1 205 ? -18.488 -1.621  -37.741 1.00 30.76 ? 194 VAL A O   1 
ATOM   1346 C  CB  . VAL A 1 205 ? -20.297 -0.151  -39.536 1.00 24.70 ? 194 VAL A CB  1 
ATOM   1347 C  CG1 . VAL A 1 205 ? -21.553 0.043   -40.368 1.00 24.58 ? 194 VAL A CG1 1 
ATOM   1348 C  CG2 . VAL A 1 205 ? -19.549 1.152   -39.425 1.00 20.30 ? 194 VAL A CG2 1 
ATOM   1349 N  N   . ASP A 1 206 ? -19.313 -0.285  -36.116 1.00 30.83 ? 195 ASP A N   1 
ATOM   1350 C  CA  . ASP A 1 206 ? -18.208 -0.529  -35.197 1.00 30.31 ? 195 ASP A CA  1 
ATOM   1351 C  C   . ASP A 1 206 ? -18.081 -2.023  -34.866 1.00 29.15 ? 195 ASP A C   1 
ATOM   1352 O  O   . ASP A 1 206 ? -19.070 -2.768  -34.825 1.00 25.05 ? 195 ASP A O   1 
ATOM   1353 C  CB  . ASP A 1 206 ? -18.425 0.281   -33.916 1.00 22.81 ? 195 ASP A CB  1 
ATOM   1354 C  CG  . ASP A 1 206 ? -17.154 0.468   -33.131 1.00 29.60 ? 195 ASP A CG  1 
ATOM   1355 O  OD1 . ASP A 1 206 ? -16.781 -0.413  -32.319 1.00 32.17 ? 195 ASP A OD1 1 
ATOM   1356 O  OD2 . ASP A 1 206 ? -16.501 1.500   -33.340 1.00 31.48 ? 195 ASP A OD2 1 
ATOM   1357 N  N   . TYR A 1 207 ? -16.849 -2.463  -34.600 1.00 24.22 ? 196 TYR A N   1 
ATOM   1358 C  CA  . TYR A 1 207 ? -16.654 -3.861  -34.220 1.00 26.43 ? 196 TYR A CA  1 
ATOM   1359 C  C   . TYR A 1 207 ? -17.423 -4.227  -32.952 1.00 27.46 ? 196 TYR A C   1 
ATOM   1360 O  O   . TYR A 1 207 ? -17.761 -5.402  -32.757 1.00 27.62 ? 196 TYR A O   1 
ATOM   1361 C  CB  . TYR A 1 207 ? -15.163 -4.176  -34.041 1.00 24.28 ? 196 TYR A CB  1 
ATOM   1362 C  CG  . TYR A 1 207 ? -14.933 -5.532  -33.439 1.00 29.18 ? 196 TYR A CG  1 
ATOM   1363 C  CD1 . TYR A 1 207 ? -15.389 -6.678  -34.069 1.00 27.99 ? 196 TYR A CD1 1 
ATOM   1364 C  CD2 . TYR A 1 207 ? -14.303 -5.671  -32.218 1.00 35.23 ? 196 TYR A CD2 1 
ATOM   1365 C  CE1 . TYR A 1 207 ? -15.202 -7.933  -33.503 1.00 30.32 ? 196 TYR A CE1 1 
ATOM   1366 C  CE2 . TYR A 1 207 ? -14.117 -6.922  -31.638 1.00 32.69 ? 196 TYR A CE2 1 
ATOM   1367 C  CZ  . TYR A 1 207 ? -14.566 -8.052  -32.286 1.00 33.39 ? 196 TYR A CZ  1 
ATOM   1368 O  OH  . TYR A 1 207 ? -14.369 -9.300  -31.713 1.00 31.99 ? 196 TYR A OH  1 
ATOM   1369 N  N   . HIS A 1 208 ? -17.739 -3.251  -32.107 1.00 26.45 ? 197 HIS A N   1 
ATOM   1370 C  CA  . HIS A 1 208 ? -18.322 -3.509  -30.801 1.00 26.70 ? 197 HIS A CA  1 
ATOM   1371 C  C   . HIS A 1 208 ? -19.792 -3.124  -30.804 1.00 30.35 ? 197 HIS A C   1 
ATOM   1372 O  O   . HIS A 1 208 ? -20.227 -2.283  -31.596 1.00 33.63 ? 197 HIS A O   1 
ATOM   1373 C  CB  . HIS A 1 208 ? -17.594 -2.728  -29.709 1.00 26.48 ? 197 HIS A CB  1 
ATOM   1374 C  CG  . HIS A 1 208 ? -16.173 -3.139  -29.504 1.00 28.59 ? 197 HIS A CG  1 
ATOM   1375 N  ND1 . HIS A 1 208 ? -15.131 -2.575  -30.201 1.00 33.57 ? 197 HIS A ND1 1 
ATOM   1376 C  CD2 . HIS A 1 208 ? -15.618 -4.041  -28.666 1.00 31.27 ? 197 HIS A CD2 1 
ATOM   1377 C  CE1 . HIS A 1 208 ? -13.995 -3.126  -29.819 1.00 31.39 ? 197 HIS A CE1 1 
ATOM   1378 N  NE2 . HIS A 1 208 ? -14.263 -4.014  -28.882 1.00 30.44 ? 197 HIS A NE2 1 
ATOM   1379 N  N   . HIS A 1 209 ? -20.557 -3.734  -29.897 1.00 28.25 ? 198 HIS A N   1 
ATOM   1380 C  CA  . HIS A 1 209 ? -21.968 -3.372  -29.780 1.00 31.74 ? 198 HIS A CA  1 
ATOM   1381 C  C   . HIS A 1 209 ? -22.122 -1.918  -29.353 1.00 26.78 ? 198 HIS A C   1 
ATOM   1382 O  O   . HIS A 1 209 ? -21.367 -1.417  -28.514 1.00 27.51 ? 198 HIS A O   1 
ATOM   1383 C  CB  . HIS A 1 209 ? -22.699 -4.276  -28.781 1.00 26.35 ? 198 HIS A CB  1 
ATOM   1384 C  CG  . HIS A 1 209 ? -24.190 -4.109  -28.800 1.00 28.58 ? 198 HIS A CG  1 
ATOM   1385 N  ND1 . HIS A 1 209 ? -24.915 -3.724  -27.691 1.00 27.41 ? 198 HIS A ND1 1 
ATOM   1386 C  CD2 . HIS A 1 209 ? -25.092 -4.267  -29.798 1.00 28.50 ? 198 HIS A CD2 1 
ATOM   1387 C  CE1 . HIS A 1 209 ? -26.197 -3.664  -28.000 1.00 23.61 ? 198 HIS A CE1 1 
ATOM   1388 N  NE2 . HIS A 1 209 ? -26.332 -3.992  -29.272 1.00 28.83 ? 198 HIS A NE2 1 
ATOM   1389 N  N   . GLY A 1 210 ? -23.107 -1.238  -29.947 1.00 29.64 ? 199 GLY A N   1 
ATOM   1390 C  CA  . GLY A 1 210 ? -23.531 0.064   -29.458 1.00 26.51 ? 199 GLY A CA  1 
ATOM   1391 C  C   . GLY A 1 210 ? -24.514 -0.055  -28.301 1.00 28.27 ? 199 GLY A C   1 
ATOM   1392 O  O   . GLY A 1 210 ? -25.656 0.411   -28.400 1.00 29.76 ? 199 GLY A O   1 
ATOM   1393 N  N   . ASN A 1 211 ? -24.077 -0.674  -27.197 1.00 22.62 ? 200 ASN A N   1 
ATOM   1394 C  CA  . ASN A 1 211 ? -24.971 -0.950  -26.076 1.00 24.73 ? 200 ASN A CA  1 
ATOM   1395 C  C   . ASN A 1 211 ? -25.636 0.316   -25.539 1.00 28.37 ? 200 ASN A C   1 
ATOM   1396 O  O   . ASN A 1 211 ? -26.804 0.283   -25.126 1.00 28.61 ? 200 ASN A O   1 
ATOM   1397 C  CB  . ASN A 1 211 ? -24.202 -1.633  -24.962 1.00 20.87 ? 200 ASN A CB  1 
ATOM   1398 C  CG  . ASN A 1 211 ? -23.026 -0.832  -24.526 1.00 25.31 ? 200 ASN A CG  1 
ATOM   1399 O  OD1 . ASN A 1 211 ? -22.014 -0.759  -25.216 1.00 23.10 ? 200 ASN A OD1 1 
ATOM   1400 N  ND2 . ASN A 1 211 ? -23.160 -0.181  -23.380 1.00 31.71 ? 200 ASN A ND2 1 
ATOM   1401 N  N   . GLY A 1 212 ? -24.909 1.435   -25.518 1.00 25.52 ? 201 GLY A N   1 
ATOM   1402 C  CA  . GLY A 1 212 ? -25.516 2.683   -25.087 1.00 28.82 ? 201 GLY A CA  1 
ATOM   1403 C  C   . GLY A 1 212 ? -26.573 3.185   -26.057 1.00 28.62 ? 201 GLY A C   1 
ATOM   1404 O  O   . GLY A 1 212 ? -27.672 3.580   -25.650 1.00 20.38 ? 201 GLY A O   1 
ATOM   1405 N  N   . THR A 1 213 ? -26.250 3.179   -27.356 1.00 29.34 ? 202 THR A N   1 
ATOM   1406 C  CA  . THR A 1 213 ? -27.216 3.615   -28.362 1.00 26.76 ? 202 THR A CA  1 
ATOM   1407 C  C   . THR A 1 213 ? -28.459 2.744   -28.344 1.00 27.05 ? 202 THR A C   1 
ATOM   1408 O  O   . THR A 1 213 ? -29.579 3.260   -28.389 1.00 28.27 ? 202 THR A O   1 
ATOM   1409 C  CB  . THR A 1 213 ? -26.593 3.600   -29.751 1.00 22.88 ? 202 THR A CB  1 
ATOM   1410 O  OG1 . THR A 1 213 ? -25.282 4.179   -29.698 1.00 24.05 ? 202 THR A OG1 1 
ATOM   1411 C  CG2 . THR A 1 213 ? -27.457 4.393   -30.695 1.00 24.71 ? 202 THR A CG2 1 
ATOM   1412 N  N   . GLN A 1 214 ? -28.277 1.419   -28.270 1.00 28.77 ? 203 GLN A N   1 
ATOM   1413 C  CA  . GLN A 1 214 ? -29.396 0.493   -28.083 1.00 31.12 ? 203 GLN A CA  1 
ATOM   1414 C  C   . GLN A 1 214 ? -30.235 0.845   -26.844 1.00 30.15 ? 203 GLN A C   1 
ATOM   1415 O  O   . GLN A 1 214 ? -31.464 0.962   -26.915 1.00 22.02 ? 203 GLN A O   1 
ATOM   1416 C  CB  . GLN A 1 214 ? -28.859 -0.938  -27.973 1.00 24.99 ? 203 GLN A CB  1 
ATOM   1417 C  CG  . GLN A 1 214 ? -29.822 -1.886  -27.262 1.00 29.91 ? 203 GLN A CG  1 
ATOM   1418 C  CD  . GLN A 1 214 ? -29.678 -3.327  -27.715 1.00 35.32 ? 203 GLN A CD  1 
ATOM   1419 O  OE1 . GLN A 1 214 ? -29.310 -3.600  -28.865 1.00 34.22 ? 203 GLN A OE1 1 
ATOM   1420 N  NE2 . GLN A 1 214 ? -29.961 -4.264  -26.809 1.00 32.70 ? 203 GLN A NE2 1 
ATOM   1421 N  N   . SER A 1 215 ? -29.581 1.003   -25.691 1.00 31.53 ? 204 SER A N   1 
ATOM   1422 C  CA  . SER A 1 215 ? -30.304 1.281   -24.455 1.00 29.23 ? 204 SER A CA  1 
ATOM   1423 C  C   . SER A 1 215 ? -31.089 2.596   -24.532 1.00 35.17 ? 204 SER A C   1 
ATOM   1424 O  O   . SER A 1 215 ? -32.198 2.701   -23.987 1.00 32.90 ? 204 SER A O   1 
ATOM   1425 C  CB  . SER A 1 215 ? -29.314 1.302   -23.297 1.00 24.82 ? 204 SER A CB  1 
ATOM   1426 O  OG  . SER A 1 215 ? -29.761 2.159   -22.263 1.00 31.29 ? 204 SER A OG  1 
ATOM   1427 N  N   . ILE A 1 216 ? -30.538 3.602   -25.222 1.00 33.81 ? 205 ILE A N   1 
ATOM   1428 C  CA  . ILE A 1 216 ? -31.154 4.927   -25.286 1.00 30.57 ? 205 ILE A CA  1 
ATOM   1429 C  C   . ILE A 1 216 ? -32.486 4.889   -26.047 1.00 33.86 ? 205 ILE A C   1 
ATOM   1430 O  O   . ILE A 1 216 ? -33.470 5.528   -25.642 1.00 28.92 ? 205 ILE A O   1 
ATOM   1431 C  CB  . ILE A 1 216 ? -30.157 5.918   -25.914 1.00 25.77 ? 205 ILE A CB  1 
ATOM   1432 C  CG1 . ILE A 1 216 ? -29.064 6.289   -24.904 1.00 26.43 ? 205 ILE A CG1 1 
ATOM   1433 C  CG2 . ILE A 1 216 ? -30.863 7.139   -26.437 1.00 21.62 ? 205 ILE A CG2 1 
ATOM   1434 C  CD1 . ILE A 1 216 ? -27.908 7.085   -25.490 1.00 21.75 ? 205 ILE A CD1 1 
ATOM   1435 N  N   . PHE A 1 217 ? -32.552 4.128   -27.145 1.00 30.00 ? 206 PHE A N   1 
ATOM   1436 C  CA  . PHE A 1 217 ? -33.749 4.072   -27.977 1.00 30.22 ? 206 PHE A CA  1 
ATOM   1437 C  C   . PHE A 1 217 ? -34.520 2.757   -27.841 1.00 34.58 ? 206 PHE A C   1 
ATOM   1438 O  O   . PHE A 1 217 ? -35.423 2.499   -28.647 1.00 32.02 ? 206 PHE A O   1 
ATOM   1439 C  CB  . PHE A 1 217 ? -33.374 4.323   -29.434 1.00 26.45 ? 206 PHE A CB  1 
ATOM   1440 C  CG  . PHE A 1 217 ? -32.633 5.606   -29.645 1.00 32.39 ? 206 PHE A CG  1 
ATOM   1441 C  CD1 . PHE A 1 217 ? -33.320 6.810   -29.762 1.00 29.18 ? 206 PHE A CD1 1 
ATOM   1442 C  CD2 . PHE A 1 217 ? -31.241 5.621   -29.710 1.00 30.57 ? 206 PHE A CD2 1 
ATOM   1443 C  CE1 . PHE A 1 217 ? -32.622 8.012   -29.945 1.00 28.09 ? 206 PHE A CE1 1 
ATOM   1444 C  CE2 . PHE A 1 217 ? -30.547 6.809   -29.886 1.00 27.28 ? 206 PHE A CE2 1 
ATOM   1445 C  CZ  . PHE A 1 217 ? -31.237 8.009   -30.008 1.00 25.74 ? 206 PHE A CZ  1 
ATOM   1446 N  N   . TYR A 1 218 ? -34.227 1.953   -26.807 1.00 29.08 ? 207 TYR A N   1 
ATOM   1447 C  CA  . TYR A 1 218 ? -34.700 0.576   -26.782 1.00 25.87 ? 207 TYR A CA  1 
ATOM   1448 C  C   . TYR A 1 218 ? -36.215 0.477   -26.787 1.00 36.31 ? 207 TYR A C   1 
ATOM   1449 O  O   . TYR A 1 218 ? -36.765 -0.536  -27.236 1.00 36.08 ? 207 TYR A O   1 
ATOM   1450 C  CB  . TYR A 1 218 ? -34.163 -0.167  -25.568 1.00 28.68 ? 207 TYR A CB  1 
ATOM   1451 C  CG  . TYR A 1 218 ? -34.234 -1.658  -25.775 1.00 30.08 ? 207 TYR A CG  1 
ATOM   1452 C  CD1 . TYR A 1 218 ? -33.546 -2.271  -26.827 1.00 32.14 ? 207 TYR A CD1 1 
ATOM   1453 C  CD2 . TYR A 1 218 ? -34.993 -2.448  -24.948 1.00 33.62 ? 207 TYR A CD2 1 
ATOM   1454 C  CE1 . TYR A 1 218 ? -33.619 -3.620  -27.030 1.00 33.34 ? 207 TYR A CE1 1 
ATOM   1455 C  CE2 . TYR A 1 218 ? -35.079 -3.804  -25.139 1.00 36.26 ? 207 TYR A CE2 1 
ATOM   1456 C  CZ  . TYR A 1 218 ? -34.393 -4.386  -26.177 1.00 35.30 ? 207 TYR A CZ  1 
ATOM   1457 O  OH  . TYR A 1 218 ? -34.493 -5.740  -26.358 1.00 36.46 ? 207 TYR A OH  1 
ATOM   1458 N  N   . SER A 1 219 ? -36.907 1.499   -26.288 1.00 40.48 ? 208 SER A N   1 
ATOM   1459 C  CA  . SER A 1 219 ? -38.357 1.457   -26.163 1.00 38.62 ? 208 SER A CA  1 
ATOM   1460 C  C   . SER A 1 219 ? -39.034 2.502   -27.045 1.00 38.42 ? 208 SER A C   1 
ATOM   1461 O  O   . SER A 1 219 ? -40.165 2.926   -26.758 1.00 37.09 ? 208 SER A O   1 
ATOM   1462 C  CB  . SER A 1 219 ? -38.752 1.647   -24.703 1.00 31.43 ? 208 SER A CB  1 
ATOM   1463 O  OG  . SER A 1 219 ? -38.238 2.885   -24.271 1.00 41.59 ? 208 SER A OG  1 
ATOM   1464 N  N   . ARG A 1 220 ? -38.368 2.922   -28.115 1.00 35.17 ? 209 ARG A N   1 
ATOM   1465 C  CA  . ARG A 1 220 ? -38.917 3.903   -29.036 1.00 38.17 ? 209 ARG A CA  1 
ATOM   1466 C  C   . ARG A 1 220 ? -39.026 3.303   -30.428 1.00 35.16 ? 209 ARG A C   1 
ATOM   1467 O  O   . ARG A 1 220 ? -38.266 2.399   -30.794 1.00 34.73 ? 209 ARG A O   1 
ATOM   1468 C  CB  . ARG A 1 220 ? -38.054 5.164   -29.074 1.00 33.37 ? 209 ARG A CB  1 
ATOM   1469 C  CG  . ARG A 1 220 ? -38.136 5.941   -27.800 1.00 28.77 ? 209 ARG A CG  1 
ATOM   1470 C  CD  . ARG A 1 220 ? -37.025 6.897   -27.731 1.00 30.96 ? 209 ARG A CD  1 
ATOM   1471 N  NE  . ARG A 1 220 ? -37.129 7.901   -28.778 1.00 30.55 ? 209 ARG A NE  1 
ATOM   1472 C  CZ  . ARG A 1 220 ? -36.353 8.974   -28.853 1.00 25.99 ? 209 ARG A CZ  1 
ATOM   1473 N  NH1 . ARG A 1 220 ? -35.444 9.229   -27.929 1.00 23.08 ? 209 ARG A NH1 1 
ATOM   1474 N  NH2 . ARG A 1 220 ? -36.484 9.800   -29.886 1.00 21.84 ? 209 ARG A NH2 1 
ATOM   1475 N  N   . SER A 1 221 ? -39.985 3.803   -31.206 1.00 33.57 ? 210 SER A N   1 
ATOM   1476 C  CA  . SER A 1 221 ? -40.136 3.332   -32.576 1.00 39.22 ? 210 SER A CA  1 
ATOM   1477 C  C   . SER A 1 221 ? -39.836 4.401   -33.620 1.00 32.86 ? 210 SER A C   1 
ATOM   1478 O  O   . SER A 1 221 ? -39.909 4.106   -34.820 1.00 36.67 ? 210 SER A O   1 
ATOM   1479 C  CB  . SER A 1 221 ? -41.538 2.734   -32.793 1.00 33.92 ? 210 SER A CB  1 
ATOM   1480 O  OG  . SER A 1 221 ? -42.524 3.734   -32.965 1.00 40.24 ? 210 SER A OG  1 
ATOM   1481 N  N   . ASP A 1 222 ? -39.467 5.613   -33.208 1.00 27.60 ? 211 ASP A N   1 
ATOM   1482 C  CA  . ASP A 1 222 ? -39.050 6.642   -34.153 1.00 36.18 ? 211 ASP A CA  1 
ATOM   1483 C  C   . ASP A 1 222 ? -37.565 6.581   -34.490 1.00 38.43 ? 211 ASP A C   1 
ATOM   1484 O  O   . ASP A 1 222 ? -37.115 7.323   -35.375 1.00 37.20 ? 211 ASP A O   1 
ATOM   1485 C  CB  . ASP A 1 222 ? -39.383 8.038   -33.615 1.00 31.03 ? 211 ASP A CB  1 
ATOM   1486 C  CG  . ASP A 1 222 ? -38.899 8.246   -32.198 1.00 33.51 ? 211 ASP A CG  1 
ATOM   1487 O  OD1 . ASP A 1 222 ? -38.645 7.245   -31.504 1.00 37.17 ? 211 ASP A OD1 1 
ATOM   1488 O  OD2 . ASP A 1 222 ? -38.779 9.413   -31.768 1.00 43.27 ? 211 ASP A OD2 1 
ATOM   1489 N  N   . VAL A 1 223 ? -36.793 5.741   -33.800 1.00 33.25 ? 212 VAL A N   1 
ATOM   1490 C  CA  . VAL A 1 223 ? -35.380 5.530   -34.104 1.00 34.42 ? 212 VAL A CA  1 
ATOM   1491 C  C   . VAL A 1 223 ? -35.139 4.034   -34.147 1.00 32.45 ? 212 VAL A C   1 
ATOM   1492 O  O   . VAL A 1 223 ? -35.317 3.342   -33.138 1.00 33.20 ? 212 VAL A O   1 
ATOM   1493 C  CB  . VAL A 1 223 ? -34.439 6.192   -33.080 1.00 32.07 ? 212 VAL A CB  1 
ATOM   1494 C  CG1 . VAL A 1 223 ? -33.001 5.975   -33.482 1.00 23.25 ? 212 VAL A CG1 1 
ATOM   1495 C  CG2 . VAL A 1 223 ? -34.735 7.682   -32.960 1.00 32.39 ? 212 VAL A CG2 1 
ATOM   1496 N  N   . LEU A 1 224 ? -34.748 3.536   -35.305 1.00 35.15 ? 213 LEU A N   1 
ATOM   1497 C  CA  . LEU A 1 224 ? -34.353 2.142   -35.451 1.00 34.38 ? 213 LEU A CA  1 
ATOM   1498 C  C   . LEU A 1 224 ? -32.852 2.026   -35.212 1.00 33.67 ? 213 LEU A C   1 
ATOM   1499 O  O   . LEU A 1 224 ? -32.078 2.876   -35.664 1.00 35.12 ? 213 LEU A O   1 
ATOM   1500 C  CB  . LEU A 1 224 ? -34.730 1.634   -36.845 1.00 31.27 ? 213 LEU A CB  1 
ATOM   1501 C  CG  . LEU A 1 224 ? -34.119 0.337   -37.355 1.00 41.85 ? 213 LEU A CG  1 
ATOM   1502 C  CD1 . LEU A 1 224 ? -34.534 -0.818  -36.458 1.00 40.18 ? 213 LEU A CD1 1 
ATOM   1503 C  CD2 . LEU A 1 224 ? -34.554 0.092   -38.797 1.00 34.28 ? 213 LEU A CD2 1 
ATOM   1504 N  N   . PHE A 1 225 ? -32.447 1.003   -34.456 1.00 33.45 ? 214 PHE A N   1 
ATOM   1505 C  CA  . PHE A 1 225 ? -31.038 0.754   -34.156 1.00 31.81 ? 214 PHE A CA  1 
ATOM   1506 C  C   . PHE A 1 225 ? -30.628 -0.587  -34.746 1.00 33.35 ? 214 PHE A C   1 
ATOM   1507 O  O   . PHE A 1 225 ? -31.170 -1.629  -34.361 1.00 34.18 ? 214 PHE A O   1 
ATOM   1508 C  CB  . PHE A 1 225 ? -30.762 0.768   -32.646 1.00 33.66 ? 214 PHE A CB  1 
ATOM   1509 C  CG  . PHE A 1 225 ? -29.296 0.520   -32.285 1.00 30.75 ? 214 PHE A CG  1 
ATOM   1510 C  CD1 . PHE A 1 225 ? -28.322 1.469   -32.563 1.00 29.51 ? 214 PHE A CD1 1 
ATOM   1511 C  CD2 . PHE A 1 225 ? -28.905 -0.667  -31.685 1.00 30.50 ? 214 PHE A CD2 1 
ATOM   1512 C  CE1 . PHE A 1 225 ? -27.009 1.240   -32.240 1.00 28.08 ? 214 PHE A CE1 1 
ATOM   1513 C  CE2 . PHE A 1 225 ? -27.593 -0.902  -31.364 1.00 26.24 ? 214 PHE A CE2 1 
ATOM   1514 C  CZ  . PHE A 1 225 ? -26.647 0.047   -31.639 1.00 30.31 ? 214 PHE A CZ  1 
ATOM   1515 N  N   . THR A 1 226 ? -29.675 -0.557  -35.675 1.00 28.60 ? 215 THR A N   1 
ATOM   1516 C  CA  . THR A 1 226 ? -29.045 -1.760  -36.198 1.00 28.84 ? 215 THR A CA  1 
ATOM   1517 C  C   . THR A 1 226 ? -27.567 -1.722  -35.832 1.00 29.07 ? 215 THR A C   1 
ATOM   1518 O  O   . THR A 1 226 ? -26.966 -0.648  -35.713 1.00 29.71 ? 215 THR A O   1 
ATOM   1519 C  CB  . THR A 1 226 ? -29.222 -1.900  -37.730 1.00 30.00 ? 215 THR A CB  1 
ATOM   1520 O  OG1 . THR A 1 226 ? -28.925 -0.654  -38.372 1.00 35.39 ? 215 THR A OG1 1 
ATOM   1521 C  CG2 . THR A 1 226 ? -30.633 -2.301  -38.092 1.00 32.32 ? 215 THR A CG2 1 
ATOM   1522 N  N   . SER A 1 227 ? -26.989 -2.902  -35.624 1.00 26.27 ? 216 SER A N   1 
ATOM   1523 C  CA  . SER A 1 227 ? -25.608 -3.008  -35.171 1.00 30.12 ? 216 SER A CA  1 
ATOM   1524 C  C   . SER A 1 227 ? -25.029 -4.322  -35.666 1.00 29.51 ? 216 SER A C   1 
ATOM   1525 O  O   . SER A 1 227 ? -25.698 -5.357  -35.583 1.00 31.76 ? 216 SER A O   1 
ATOM   1526 C  CB  . SER A 1 227 ? -25.519 -2.931  -33.636 1.00 31.72 ? 216 SER A CB  1 
ATOM   1527 O  OG  . SER A 1 227 ? -24.180 -3.028  -33.172 1.00 31.64 ? 216 SER A OG  1 
ATOM   1528 N  N   . ILE A 1 228 ? -23.811 -4.273  -36.197 1.00 23.32 ? 217 ILE A N   1 
ATOM   1529 C  CA  . ILE A 1 228 ? -23.035 -5.459  -36.523 1.00 21.57 ? 217 ILE A CA  1 
ATOM   1530 C  C   . ILE A 1 228 ? -21.810 -5.420  -35.625 1.00 25.84 ? 217 ILE A C   1 
ATOM   1531 O  O   . ILE A 1 228 ? -21.009 -4.481  -35.697 1.00 31.99 ? 217 ILE A O   1 
ATOM   1532 C  CB  . ILE A 1 228 ? -22.647 -5.493  -38.012 1.00 25.31 ? 217 ILE A CB  1 
ATOM   1533 C  CG1 . ILE A 1 228 ? -23.846 -5.110  -38.880 1.00 27.87 ? 217 ILE A CG1 1 
ATOM   1534 C  CG2 . ILE A 1 228 ? -22.093 -6.859  -38.432 1.00 21.76 ? 217 ILE A CG2 1 
ATOM   1535 C  CD1 . ILE A 1 228 ? -23.504 -4.844  -40.342 1.00 25.24 ? 217 ILE A CD1 1 
ATOM   1536 N  N   . HIS A 1 229 ? -21.664 -6.411  -34.771 1.00 23.10 ? 218 HIS A N   1 
ATOM   1537 C  CA  . HIS A 1 229 ? -20.597 -6.392  -33.779 1.00 29.86 ? 218 HIS A CA  1 
ATOM   1538 C  C   . HIS A 1 229 ? -20.050 -7.803  -33.617 1.00 33.14 ? 218 HIS A C   1 
ATOM   1539 O  O   . HIS A 1 229 ? -20.614 -8.771  -34.141 1.00 31.59 ? 218 HIS A O   1 
ATOM   1540 C  CB  . HIS A 1 229 ? -21.131 -5.876  -32.438 1.00 30.66 ? 218 HIS A CB  1 
ATOM   1541 C  CG  . HIS A 1 229 ? -22.509 -6.376  -32.146 1.00 29.19 ? 218 HIS A CG  1 
ATOM   1542 N  ND1 . HIS A 1 229 ? -23.632 -5.825  -32.723 1.00 28.80 ? 218 HIS A ND1 1 
ATOM   1543 C  CD2 . HIS A 1 229 ? -22.941 -7.428  -31.413 1.00 29.08 ? 218 HIS A CD2 1 
ATOM   1544 C  CE1 . HIS A 1 229 ? -24.700 -6.494  -32.332 1.00 27.50 ? 218 HIS A CE1 1 
ATOM   1545 N  NE2 . HIS A 1 229 ? -24.310 -7.471  -31.535 1.00 28.99 ? 218 HIS A NE2 1 
ATOM   1546 N  N   . GLY A 1 230 ? -18.962 -7.926  -32.860 1.00 30.47 ? 219 GLY A N   1 
ATOM   1547 C  CA  . GLY A 1 230 ? -18.583 -9.233  -32.355 1.00 31.65 ? 219 GLY A CA  1 
ATOM   1548 C  C   . GLY A 1 230 ? -19.618 -9.709  -31.350 1.00 32.31 ? 219 GLY A C   1 
ATOM   1549 O  O   . GLY A 1 230 ? -20.119 -8.928  -30.537 1.00 28.98 ? 219 GLY A O   1 
ATOM   1550 N  N   . ASP A 1 231 ? -19.972 -11.002 -31.446 1.00 30.62 ? 220 ASP A N   1 
ATOM   1551 C  CA  . ASP A 1 231 ? -20.966 -11.639 -30.585 1.00 28.22 ? 220 ASP A CA  1 
ATOM   1552 C  C   . ASP A 1 231 ? -20.639 -11.375 -29.121 1.00 30.33 ? 220 ASP A C   1 
ATOM   1553 O  O   . ASP A 1 231 ? -19.560 -11.774 -28.658 1.00 35.12 ? 220 ASP A O   1 
ATOM   1554 C  CB  . ASP A 1 231 ? -21.005 -13.149 -30.826 1.00 31.55 ? 220 ASP A CB  1 
ATOM   1555 C  CG  . ASP A 1 231 ? -22.268 -13.819 -30.255 1.00 39.10 ? 220 ASP A CG  1 
ATOM   1556 O  OD1 . ASP A 1 231 ? -22.866 -13.316 -29.283 1.00 38.91 ? 220 ASP A OD1 1 
ATOM   1557 O  OD2 . ASP A 1 231 ? -22.679 -14.873 -30.787 1.00 49.35 ? 220 ASP A OD2 1 
ATOM   1558 N  N   . PRO A 1 232 ? -21.531 -10.732 -28.361 1.00 31.73 ? 221 PRO A N   1 
ATOM   1559 C  CA  . PRO A 1 232 ? -21.252 -10.502 -26.930 1.00 31.16 ? 221 PRO A CA  1 
ATOM   1560 C  C   . PRO A 1 232 ? -21.028 -11.781 -26.121 1.00 32.26 ? 221 PRO A C   1 
ATOM   1561 O  O   . PRO A 1 232 ? -20.564 -11.687 -24.972 1.00 33.95 ? 221 PRO A O   1 
ATOM   1562 C  CB  . PRO A 1 232 ? -22.494 -9.747  -26.445 1.00 28.61 ? 221 PRO A CB  1 
ATOM   1563 C  CG  . PRO A 1 232 ? -23.548 -10.056 -27.461 1.00 31.34 ? 221 PRO A CG  1 
ATOM   1564 C  CD  . PRO A 1 232 ? -22.824 -10.161 -28.765 1.00 29.89 ? 221 PRO A CD  1 
ATOM   1565 N  N   . LYS A 1 233 ? -21.326 -12.961 -26.679 1.00 27.48 ? 222 LYS A N   1 
ATOM   1566 C  CA  . LYS A 1 233 ? -20.947 -14.218 -26.030 1.00 36.85 ? 222 LYS A CA  1 
ATOM   1567 C  C   . LYS A 1 233 ? -19.454 -14.264 -25.700 1.00 38.63 ? 222 LYS A C   1 
ATOM   1568 O  O   . LYS A 1 233 ? -19.054 -14.788 -24.649 1.00 33.23 ? 222 LYS A O   1 
ATOM   1569 C  CB  . LYS A 1 233 ? -21.312 -15.408 -26.920 1.00 34.31 ? 222 LYS A CB  1 
ATOM   1570 C  CG  . LYS A 1 233 ? -22.457 -16.243 -26.405 1.00 33.40 ? 222 LYS A CG  1 
ATOM   1571 C  CD  . LYS A 1 233 ? -23.120 -16.941 -27.550 1.00 29.42 ? 222 LYS A CD  1 
ATOM   1572 C  CE  . LYS A 1 233 ? -24.606 -16.913 -27.364 1.00 37.66 ? 222 LYS A CE  1 
ATOM   1573 N  NZ  . LYS A 1 233 ? -25.296 -17.527 -28.521 1.00 48.16 ? 222 LYS A NZ  1 
ATOM   1574 N  N   . PHE A 1 234 ? -18.613 -13.736 -26.599 1.00 32.36 ? 223 PHE A N   1 
ATOM   1575 C  CA  . PHE A 1 234 ? -17.175 -13.716 -26.400 1.00 27.93 ? 223 PHE A CA  1 
ATOM   1576 C  C   . PHE A 1 234 ? -16.589 -12.314 -26.356 1.00 31.73 ? 223 PHE A C   1 
ATOM   1577 O  O   . PHE A 1 234 ? -15.473 -12.153 -25.859 1.00 31.24 ? 223 PHE A O   1 
ATOM   1578 C  CB  . PHE A 1 234 ? -16.464 -14.540 -27.498 1.00 24.82 ? 223 PHE A CB  1 
ATOM   1579 C  CG  . PHE A 1 234 ? -16.517 -13.925 -28.874 1.00 32.42 ? 223 PHE A CG  1 
ATOM   1580 C  CD1 . PHE A 1 234 ? -15.567 -12.970 -29.274 1.00 33.39 ? 223 PHE A CD1 1 
ATOM   1581 C  CD2 . PHE A 1 234 ? -17.504 -14.306 -29.782 1.00 32.14 ? 223 PHE A CD2 1 
ATOM   1582 C  CE1 . PHE A 1 234 ? -15.618 -12.402 -30.543 1.00 31.25 ? 223 PHE A CE1 1 
ATOM   1583 C  CE2 . PHE A 1 234 ? -17.561 -13.739 -31.054 1.00 29.88 ? 223 PHE A CE2 1 
ATOM   1584 C  CZ  . PHE A 1 234 ? -16.617 -12.788 -31.432 1.00 31.06 ? 223 PHE A CZ  1 
ATOM   1585 N  N   . GLU A 1 235 ? -17.321 -11.297 -26.807 1.00 35.14 ? 224 GLU A N   1 
ATOM   1586 C  CA  . GLU A 1 235 ? -16.767 -9.982  -27.096 1.00 33.48 ? 224 GLU A CA  1 
ATOM   1587 C  C   . GLU A 1 235 ? -17.367 -8.910  -26.195 1.00 34.43 ? 224 GLU A C   1 
ATOM   1588 O  O   . GLU A 1 235 ? -18.549 -8.962  -25.847 1.00 35.32 ? 224 GLU A O   1 
ATOM   1589 C  CB  . GLU A 1 235 ? -17.013 -9.598  -28.569 1.00 31.09 ? 224 GLU A CB  1 
ATOM   1590 C  CG  . GLU A 1 235 ? -16.151 -8.446  -29.058 1.00 35.33 ? 224 GLU A CG  1 
ATOM   1591 C  CD  . GLU A 1 235 ? -14.725 -8.503  -28.507 1.00 41.04 ? 224 GLU A CD  1 
ATOM   1592 O  OE1 . GLU A 1 235 ? -13.830 -9.101  -29.169 1.00 40.97 ? 224 GLU A OE1 1 
ATOM   1593 O  OE2 . GLU A 1 235 ? -14.504 -7.946  -27.402 1.00 37.78 ? 224 GLU A OE2 1 
ATOM   1594 N  N   . PHE A 1 236 ? -16.533 -7.935  -25.830 1.00 37.76 ? 225 PHE A N   1 
ATOM   1595 C  CA  . PHE A 1 236 ? -17.013 -6.690  -25.238 1.00 32.75 ? 225 PHE A CA  1 
ATOM   1596 C  C   . PHE A 1 236 ? -18.169 -6.126  -26.063 1.00 30.18 ? 225 PHE A C   1 
ATOM   1597 O  O   . PHE A 1 236 ? -18.080 -6.080  -27.297 1.00 31.05 ? 225 PHE A O   1 
ATOM   1598 C  CB  . PHE A 1 236 ? -15.881 -5.661  -25.176 1.00 28.96 ? 225 PHE A CB  1 
ATOM   1599 C  CG  . PHE A 1 236 ? -16.197 -4.477  -24.328 1.00 30.90 ? 225 PHE A CG  1 
ATOM   1600 C  CD1 . PHE A 1 236 ? -16.013 -4.523  -22.966 1.00 34.51 ? 225 PHE A CD1 1 
ATOM   1601 C  CD2 . PHE A 1 236 ? -16.707 -3.320  -24.890 1.00 34.59 ? 225 PHE A CD2 1 
ATOM   1602 C  CE1 . PHE A 1 236 ? -16.322 -3.429  -22.175 1.00 36.57 ? 225 PHE A CE1 1 
ATOM   1603 C  CE2 . PHE A 1 236 ? -17.014 -2.230  -24.111 1.00 28.54 ? 225 PHE A CE2 1 
ATOM   1604 C  CZ  . PHE A 1 236 ? -16.823 -2.287  -22.751 1.00 32.85 ? 225 PHE A CZ  1 
ATOM   1605 N  N   . PRO A 1 237 ? -19.254 -5.661  -25.429 1.00 30.45 ? 226 PRO A N   1 
ATOM   1606 C  CA  . PRO A 1 237 ? -19.488 -5.492  -23.984 1.00 32.15 ? 226 PRO A CA  1 
ATOM   1607 C  C   . PRO A 1 237 ? -20.155 -6.665  -23.212 1.00 31.61 ? 226 PRO A C   1 
ATOM   1608 O  O   . PRO A 1 237 ? -20.611 -6.467  -22.084 1.00 27.85 ? 226 PRO A O   1 
ATOM   1609 C  CB  . PRO A 1 237 ? -20.387 -4.250  -23.965 1.00 29.73 ? 226 PRO A CB  1 
ATOM   1610 C  CG  . PRO A 1 237 ? -21.231 -4.414  -25.183 1.00 25.62 ? 226 PRO A CG  1 
ATOM   1611 C  CD  . PRO A 1 237 ? -20.339 -5.057  -26.218 1.00 26.73 ? 226 PRO A CD  1 
ATOM   1612 N  N   . PHE A 1 238 ? -20.244 -7.869  -23.783 1.00 32.38 ? 227 PHE A N   1 
ATOM   1613 C  CA  . PHE A 1 238 ? -20.670 -9.089  -23.087 1.00 32.94 ? 227 PHE A CA  1 
ATOM   1614 C  C   . PHE A 1 238 ? -22.165 -9.130  -22.743 1.00 32.73 ? 227 PHE A C   1 
ATOM   1615 O  O   . PHE A 1 238 ? -22.805 -10.184 -22.864 1.00 36.66 ? 227 PHE A O   1 
ATOM   1616 C  CB  . PHE A 1 238 ? -19.847 -9.300  -21.800 1.00 33.60 ? 227 PHE A CB  1 
ATOM   1617 C  CG  . PHE A 1 238 ? -18.353 -9.392  -22.024 1.00 34.32 ? 227 PHE A CG  1 
ATOM   1618 C  CD1 . PHE A 1 238 ? -17.815 -10.337 -22.893 1.00 33.97 ? 227 PHE A CD1 1 
ATOM   1619 C  CD2 . PHE A 1 238 ? -17.488 -8.549  -21.353 1.00 29.96 ? 227 PHE A CD2 1 
ATOM   1620 C  CE1 . PHE A 1 238 ? -16.451 -10.423 -23.092 1.00 31.61 ? 227 PHE A CE1 1 
ATOM   1621 C  CE2 . PHE A 1 238 ? -16.117 -8.636  -21.554 1.00 33.23 ? 227 PHE A CE2 1 
ATOM   1622 C  CZ  . PHE A 1 238 ? -15.604 -9.569  -22.425 1.00 31.35 ? 227 PHE A CZ  1 
ATOM   1623 N  N   . PHE A 1 239 ? -22.741 -8.010  -22.306 1.00 28.15 ? 228 PHE A N   1 
ATOM   1624 C  CA  . PHE A 1 239 ? -24.045 -8.029  -21.652 1.00 31.71 ? 228 PHE A CA  1 
ATOM   1625 C  C   . PHE A 1 239 ? -25.142 -7.339  -22.468 1.00 31.63 ? 228 PHE A C   1 
ATOM   1626 O  O   . PHE A 1 239 ? -26.258 -7.168  -21.974 1.00 28.16 ? 228 PHE A O   1 
ATOM   1627 C  CB  . PHE A 1 239 ? -23.918 -7.423  -20.248 1.00 29.23 ? 228 PHE A CB  1 
ATOM   1628 C  CG  . PHE A 1 239 ? -22.755 -7.985  -19.455 1.00 32.84 ? 228 PHE A CG  1 
ATOM   1629 C  CD1 . PHE A 1 239 ? -22.807 -9.262  -18.930 1.00 27.34 ? 228 PHE A CD1 1 
ATOM   1630 C  CD2 . PHE A 1 239 ? -21.596 -7.237  -19.259 1.00 36.79 ? 228 PHE A CD2 1 
ATOM   1631 C  CE1 . PHE A 1 239 ? -21.752 -9.775  -18.219 1.00 35.09 ? 228 PHE A CE1 1 
ATOM   1632 C  CE2 . PHE A 1 239 ? -20.527 -7.756  -18.543 1.00 30.20 ? 228 PHE A CE2 1 
ATOM   1633 C  CZ  . PHE A 1 239 ? -20.604 -9.021  -18.028 1.00 30.53 ? 228 PHE A CZ  1 
ATOM   1634 N  N   . LEU A 1 240 ? -24.852 -6.953  -23.706 1.00 28.25 ? 229 LEU A N   1 
ATOM   1635 C  CA  . LEU A 1 240 ? -25.872 -6.552  -24.656 1.00 28.46 ? 229 LEU A CA  1 
ATOM   1636 C  C   . LEU A 1 240 ? -25.368 -6.870  -26.061 1.00 32.62 ? 229 LEU A C   1 
ATOM   1637 O  O   . LEU A 1 240 ? -24.180 -7.118  -26.279 1.00 28.00 ? 229 LEU A O   1 
ATOM   1638 C  CB  . LEU A 1 240 ? -26.221 -5.072  -24.512 1.00 29.05 ? 229 LEU A CB  1 
ATOM   1639 C  CG  . LEU A 1 240 ? -27.686 -4.646  -24.383 1.00 33.08 ? 229 LEU A CG  1 
ATOM   1640 C  CD1 . LEU A 1 240 ? -28.476 -5.494  -23.363 1.00 26.72 ? 229 LEU A CD1 1 
ATOM   1641 C  CD2 . LEU A 1 240 ? -27.730 -3.148  -24.025 1.00 25.80 ? 229 LEU A CD2 1 
ATOM   1642 N  N   . GLY A 1 241 ? -26.290 -6.873  -27.017 1.00 32.99 ? 230 GLY A N   1 
ATOM   1643 C  CA  . GLY A 1 241 ? -25.951 -7.160  -28.392 1.00 30.38 ? 230 GLY A CA  1 
ATOM   1644 C  C   . GLY A 1 241 ? -26.382 -8.520  -28.876 1.00 36.48 ? 230 GLY A C   1 
ATOM   1645 O  O   . GLY A 1 241 ? -26.110 -8.858  -30.042 1.00 35.67 ? 230 GLY A O   1 
ATOM   1646 N  N   . HIS A 1 242 ? -27.038 -9.313  -28.028 1.00 31.62 ? 231 HIS A N   1 
ATOM   1647 C  CA  . HIS A 1 242 ? -27.617 -10.560 -28.492 1.00 29.99 ? 231 HIS A CA  1 
ATOM   1648 C  C   . HIS A 1 242 ? -28.711 -10.277 -29.516 1.00 31.31 ? 231 HIS A C   1 
ATOM   1649 O  O   . HIS A 1 242 ? -29.380 -9.237  -29.483 1.00 26.60 ? 231 HIS A O   1 
ATOM   1650 C  CB  . HIS A 1 242 ? -28.175 -11.367 -27.313 1.00 35.99 ? 231 HIS A CB  1 
ATOM   1651 C  CG  . HIS A 1 242 ? -27.143 -11.737 -26.301 1.00 33.40 ? 231 HIS A CG  1 
ATOM   1652 N  ND1 . HIS A 1 242 ? -26.167 -12.678 -26.545 1.00 32.82 ? 231 HIS A ND1 1 
ATOM   1653 C  CD2 . HIS A 1 242 ? -26.912 -11.269 -25.053 1.00 34.95 ? 231 HIS A CD2 1 
ATOM   1654 C  CE1 . HIS A 1 242 ? -25.393 -12.794 -25.482 1.00 32.84 ? 231 HIS A CE1 1 
ATOM   1655 N  NE2 . HIS A 1 242 ? -25.821 -11.948 -24.564 1.00 35.92 ? 231 HIS A NE2 1 
ATOM   1656 N  N   . ALA A 1 243 ? -28.886 -11.231 -30.435 1.00 36.85 ? 232 ALA A N   1 
ATOM   1657 C  CA  . ALA A 1 243 ? -29.839 -11.087 -31.530 1.00 30.57 ? 232 ALA A CA  1 
ATOM   1658 C  C   . ALA A 1 243 ? -31.294 -11.089 -31.066 1.00 29.35 ? 232 ALA A C   1 
ATOM   1659 O  O   . ALA A 1 243 ? -32.176 -10.675 -31.829 1.00 26.55 ? 232 ALA A O   1 
ATOM   1660 C  CB  . ALA A 1 243 ? -29.601 -12.205 -32.543 1.00 25.92 ? 232 ALA A CB  1 
ATOM   1661 N  N   . ASP A 1 244 ? -31.564 -11.536 -29.839 1.00 30.17 ? 233 ASP A N   1 
ATOM   1662 C  CA  . ASP A 1 244 ? -32.916 -11.629 -29.309 1.00 32.86 ? 233 ASP A CA  1 
ATOM   1663 C  C   . ASP A 1 244 ? -33.303 -10.405 -28.487 1.00 36.48 ? 233 ASP A C   1 
ATOM   1664 O  O   . ASP A 1 244 ? -34.209 -10.487 -27.643 1.00 37.16 ? 233 ASP A O   1 
ATOM   1665 C  CB  . ASP A 1 244 ? -33.075 -12.909 -28.482 1.00 33.80 ? 233 ASP A CB  1 
ATOM   1666 C  CG  . ASP A 1 244 ? -32.346 -12.843 -27.161 1.00 40.14 ? 233 ASP A CG  1 
ATOM   1667 O  OD1 . ASP A 1 244 ? -31.294 -12.162 -27.085 1.00 40.56 ? 233 ASP A OD1 1 
ATOM   1668 O  OD2 . ASP A 1 244 ? -32.819 -13.477 -26.194 1.00 37.76 ? 233 ASP A OD2 1 
ATOM   1669 N  N   . GLU A 1 245 ? -32.634 -9.277  -28.715 1.00 32.87 ? 234 GLU A N   1 
ATOM   1670 C  CA  . GLU A 1 245 ? -33.009 -7.985  -28.144 1.00 34.03 ? 234 GLU A CA  1 
ATOM   1671 C  C   . GLU A 1 245 ? -33.642 -7.153  -29.267 1.00 30.73 ? 234 GLU A C   1 
ATOM   1672 O  O   . GLU A 1 245 ? -32.946 -6.489  -30.035 1.00 30.27 ? 234 GLU A O   1 
ATOM   1673 C  CB  . GLU A 1 245 ? -31.788 -7.307  -27.497 1.00 32.97 ? 234 GLU A CB  1 
ATOM   1674 C  CG  . GLU A 1 245 ? -31.102 -8.178  -26.424 1.00 33.25 ? 234 GLU A CG  1 
ATOM   1675 C  CD  . GLU A 1 245 ? -29.590 -7.909  -26.274 1.00 38.79 ? 234 GLU A CD  1 
ATOM   1676 O  OE1 . GLU A 1 245 ? -29.097 -6.883  -26.807 1.00 34.41 ? 234 GLU A OE1 1 
ATOM   1677 O  OE2 . GLU A 1 245 ? -28.892 -8.726  -25.613 1.00 36.58 ? 234 GLU A OE2 1 
ATOM   1678 N  N   . HIS A 1 246 ? -34.978 -7.205  -29.359 1.00 29.15 ? 235 HIS A N   1 
ATOM   1679 C  CA  . HIS A 1 246 ? -35.745 -6.577  -30.434 1.00 31.67 ? 235 HIS A CA  1 
ATOM   1680 C  C   . HIS A 1 246 ? -36.405 -5.265  -30.021 1.00 30.65 ? 235 HIS A C   1 
ATOM   1681 O  O   . HIS A 1 246 ? -37.157 -4.686  -30.811 1.00 27.17 ? 235 HIS A O   1 
ATOM   1682 C  CB  . HIS A 1 246 ? -36.853 -7.520  -30.947 1.00 31.14 ? 235 HIS A CB  1 
ATOM   1683 C  CG  . HIS A 1 246 ? -36.404 -8.918  -31.250 1.00 34.19 ? 235 HIS A CG  1 
ATOM   1684 N  ND1 . HIS A 1 246 ? -35.559 -9.224  -32.296 1.00 32.67 ? 235 HIS A ND1 1 
ATOM   1685 C  CD2 . HIS A 1 246 ? -36.729 -10.102 -30.671 1.00 32.66 ? 235 HIS A CD2 1 
ATOM   1686 C  CE1 . HIS A 1 246 ? -35.371 -10.533 -32.338 1.00 29.27 ? 235 HIS A CE1 1 
ATOM   1687 N  NE2 . HIS A 1 246 ? -36.074 -11.088 -31.367 1.00 25.41 ? 235 HIS A NE2 1 
ATOM   1688 N  N   . GLY A 1 247 ? -36.194 -4.812  -28.799 1.00 31.17 ? 236 GLY A N   1 
ATOM   1689 C  CA  . GLY A 1 247 ? -36.914 -3.675  -28.265 1.00 35.88 ? 236 GLY A CA  1 
ATOM   1690 C  C   . GLY A 1 247 ? -37.862 -4.085  -27.151 1.00 37.94 ? 236 GLY A C   1 
ATOM   1691 O  O   . GLY A 1 247 ? -38.151 -5.262  -26.930 1.00 41.78 ? 236 GLY A O   1 
ATOM   1692 N  N   . GLU A 1 248 ? -38.327 -3.076  -26.418 1.00 32.41 ? 237 GLU A N   1 
ATOM   1693 C  CA  . GLU A 1 248 ? -39.378 -3.277  -25.437 1.00 41.37 ? 237 GLU A CA  1 
ATOM   1694 C  C   . GLU A 1 248 ? -40.461 -2.241  -25.666 1.00 41.49 ? 237 GLU A C   1 
ATOM   1695 O  O   . GLU A 1 248 ? -40.222 -1.177  -26.245 1.00 37.91 ? 237 GLU A O   1 
ATOM   1696 C  CB  . GLU A 1 248 ? -38.870 -3.196  -23.988 1.00 36.96 ? 237 GLU A CB  1 
ATOM   1697 C  CG  . GLU A 1 248 ? -38.031 -1.996  -23.668 1.00 51.41 ? 237 GLU A CG  1 
ATOM   1698 C  CD  . GLU A 1 248 ? -38.096 -1.607  -22.194 1.00 70.00 ? 237 GLU A CD  1 
ATOM   1699 O  OE1 . GLU A 1 248 ? -37.018 -1.341  -21.592 1.00 61.72 ? 237 GLU A OE1 1 
ATOM   1700 O  OE2 . GLU A 1 248 ? -39.218 -1.577  -21.641 1.00 75.60 ? 237 GLU A OE2 1 
ATOM   1701 N  N   . GLY A 1 249 ? -41.663 -2.582  -25.217 1.00 41.00 ? 238 GLY A N   1 
ATOM   1702 C  CA  . GLY A 1 249 ? -42.764 -1.649  -25.319 1.00 31.15 ? 238 GLY A CA  1 
ATOM   1703 C  C   . GLY A 1 249 ? -43.040 -1.338  -26.768 1.00 35.83 ? 238 GLY A C   1 
ATOM   1704 O  O   . GLY A 1 249 ? -43.092 -2.236  -27.616 1.00 32.11 ? 238 GLY A O   1 
ATOM   1705 N  N   . THR A 1 250 ? -43.217 -0.047  -27.063 1.00 39.84 ? 239 THR A N   1 
ATOM   1706 C  CA  . THR A 1 250 ? -43.514 0.376   -28.424 1.00 30.72 ? 239 THR A CA  1 
ATOM   1707 C  C   . THR A 1 250 ? -42.290 0.295   -29.320 1.00 37.53 ? 239 THR A C   1 
ATOM   1708 O  O   . THR A 1 250 ? -42.427 0.386   -30.545 1.00 39.19 ? 239 THR A O   1 
ATOM   1709 C  CB  . THR A 1 250 ? -44.054 1.802   -28.432 1.00 28.69 ? 239 THR A CB  1 
ATOM   1710 O  OG1 . THR A 1 250 ? -42.995 2.685   -28.786 1.00 47.16 ? 239 THR A OG1 1 
ATOM   1711 C  CG2 . THR A 1 250 ? -44.520 2.206   -27.039 1.00 36.22 ? 239 THR A CG2 1 
ATOM   1712 N  N   . GLY A 1 251 ? -41.101 0.137   -28.745 1.00 33.43 ? 240 GLY A N   1 
ATOM   1713 C  CA  . GLY A 1 251 ? -39.932 -0.041  -29.564 1.00 34.88 ? 240 GLY A CA  1 
ATOM   1714 C  C   . GLY A 1 251 ? -39.684 -1.460  -29.996 1.00 33.55 ? 240 GLY A C   1 
ATOM   1715 O  O   . GLY A 1 251 ? -38.624 -1.763  -30.550 1.00 32.72 ? 240 GLY A O   1 
ATOM   1716 N  N   . GLU A 1 252 ? -40.631 -2.351  -29.735 1.00 36.32 ? 241 GLU A N   1 
ATOM   1717 C  CA  . GLU A 1 252 ? -40.500 -3.733  -30.167 1.00 40.92 ? 241 GLU A CA  1 
ATOM   1718 C  C   . GLU A 1 252 ? -40.574 -3.817  -31.684 1.00 34.71 ? 241 GLU A C   1 
ATOM   1719 O  O   . GLU A 1 252 ? -41.544 -3.356  -32.295 1.00 41.40 ? 241 GLU A O   1 
ATOM   1720 C  CB  . GLU A 1 252 ? -41.575 -4.610  -29.538 1.00 35.90 ? 241 GLU A CB  1 
ATOM   1721 C  CG  . GLU A 1 252 ? -41.448 -6.023  -30.053 1.00 49.15 ? 241 GLU A CG  1 
ATOM   1722 C  CD  . GLU A 1 252 ? -41.274 -7.037  -28.956 1.00 58.99 ? 241 GLU A CD  1 
ATOM   1723 O  OE1 . GLU A 1 252 ? -40.872 -8.182  -29.272 1.00 66.43 ? 241 GLU A OE1 1 
ATOM   1724 O  OE2 . GLU A 1 252 ? -41.551 -6.690  -27.787 1.00 66.33 ? 241 GLU A OE2 1 
ATOM   1725 N  N   . GLY A 1 253 ? -39.551 -4.415  -32.280 1.00 28.94 ? 242 GLY A N   1 
ATOM   1726 C  CA  . GLY A 1 253 ? -39.412 -4.516  -33.713 1.00 33.75 ? 242 GLY A CA  1 
ATOM   1727 C  C   . GLY A 1 253 ? -38.368 -3.595  -34.278 1.00 33.20 ? 242 GLY A C   1 
ATOM   1728 O  O   . GLY A 1 253 ? -37.967 -3.764  -35.439 1.00 33.67 ? 242 GLY A O   1 
ATOM   1729 N  N   . PHE A 1 254 ? -37.907 -2.631  -33.480 1.00 38.86 ? 243 PHE A N   1 
ATOM   1730 C  CA  . PHE A 1 254 ? -37.038 -1.552  -33.933 1.00 36.78 ? 243 PHE A CA  1 
ATOM   1731 C  C   . PHE A 1 254 ? -35.683 -1.563  -33.222 1.00 34.77 ? 243 PHE A C   1 
ATOM   1732 O  O   . PHE A 1 254 ? -35.008 -0.537  -33.151 1.00 34.78 ? 243 PHE A O   1 
ATOM   1733 C  CB  . PHE A 1 254 ? -37.791 -0.233  -33.779 1.00 29.57 ? 243 PHE A CB  1 
ATOM   1734 C  CG  . PHE A 1 254 ? -39.150 -0.275  -34.428 1.00 38.27 ? 243 PHE A CG  1 
ATOM   1735 C  CD1 . PHE A 1 254 ? -39.276 -0.199  -35.812 1.00 42.85 ? 243 PHE A CD1 1 
ATOM   1736 C  CD2 . PHE A 1 254 ? -40.295 -0.461  -33.679 1.00 34.88 ? 243 PHE A CD2 1 
ATOM   1737 C  CE1 . PHE A 1 254 ? -40.525 -0.272  -36.425 1.00 33.22 ? 243 PHE A CE1 1 
ATOM   1738 C  CE2 . PHE A 1 254 ? -41.532 -0.530  -34.288 1.00 33.95 ? 243 PHE A CE2 1 
ATOM   1739 C  CZ  . PHE A 1 254 ? -41.644 -0.433  -35.662 1.00 31.26 ? 243 PHE A CZ  1 
ATOM   1740 N  N   . ASN A 1 255 ? -35.267 -2.725  -32.720 1.00 31.27 ? 244 ASN A N   1 
ATOM   1741 C  CA  . ASN A 1 255 ? -33.887 -2.992  -32.346 1.00 33.38 ? 244 ASN A CA  1 
ATOM   1742 C  C   . ASN A 1 255 ? -33.450 -4.262  -33.067 1.00 33.32 ? 244 ASN A C   1 
ATOM   1743 O  O   . ASN A 1 255 ? -34.056 -5.321  -32.864 1.00 31.60 ? 244 ASN A O   1 
ATOM   1744 C  CB  . ASN A 1 255 ? -33.747 -3.145  -30.828 1.00 32.48 ? 244 ASN A CB  1 
ATOM   1745 C  CG  . ASN A 1 255 ? -32.291 -3.099  -30.366 1.00 38.18 ? 244 ASN A CG  1 
ATOM   1746 O  OD1 . ASN A 1 255 ? -31.787 -2.039  -29.973 1.00 33.96 ? 244 ASN A OD1 1 
ATOM   1747 N  ND2 . ASN A 1 255 ? -31.605 -4.258  -30.416 1.00 31.82 ? 244 ASN A ND2 1 
ATOM   1748 N  N   . ILE A 1 256 ? -32.408 -4.164  -33.904 1.00 27.79 ? 245 ILE A N   1 
ATOM   1749 C  CA  . ILE A 1 256 ? -31.931 -5.295  -34.716 1.00 30.99 ? 245 ILE A CA  1 
ATOM   1750 C  C   . ILE A 1 256 ? -30.428 -5.464  -34.525 1.00 28.92 ? 245 ILE A C   1 
ATOM   1751 O  O   . ILE A 1 256 ? -29.638 -4.674  -35.060 1.00 31.95 ? 245 ILE A O   1 
ATOM   1752 C  CB  . ILE A 1 256 ? -32.260 -5.132  -36.212 1.00 33.44 ? 245 ILE A CB  1 
ATOM   1753 C  CG1 . ILE A 1 256 ? -33.683 -4.592  -36.415 1.00 37.20 ? 245 ILE A CG1 1 
ATOM   1754 C  CG2 . ILE A 1 256 ? -32.091 -6.450  -36.938 1.00 26.30 ? 245 ILE A CG2 1 
ATOM   1755 C  CD1 . ILE A 1 256 ? -33.944 -4.094  -37.812 1.00 35.96 ? 245 ILE A CD1 1 
ATOM   1756 N  N   . ASN A 1 257 ? -30.032 -6.525  -33.820 1.00 29.79 ? 246 ASN A N   1 
ATOM   1757 C  CA  . ASN A 1 257 ? -28.632 -6.873  -33.588 1.00 26.94 ? 246 ASN A CA  1 
ATOM   1758 C  C   . ASN A 1 257 ? -28.169 -7.955  -34.564 1.00 27.50 ? 246 ASN A C   1 
ATOM   1759 O  O   . ASN A 1 257 ? -28.889 -8.921  -34.826 1.00 21.54 ? 246 ASN A O   1 
ATOM   1760 C  CB  . ASN A 1 257 ? -28.438 -7.364  -32.152 1.00 27.51 ? 246 ASN A CB  1 
ATOM   1761 C  CG  . ASN A 1 257 ? -28.430 -6.227  -31.131 1.00 33.33 ? 246 ASN A CG  1 
ATOM   1762 O  OD1 . ASN A 1 257 ? -27.959 -5.118  -31.409 1.00 34.53 ? 246 ASN A OD1 1 
ATOM   1763 N  ND2 . ASN A 1 257 ? -28.935 -6.507  -29.937 1.00 30.28 ? 246 ASN A ND2 1 
ATOM   1764 N  N   . TYR A 1 258 ? -26.961 -7.780  -35.115 1.00 31.99 ? 247 TYR A N   1 
ATOM   1765 C  CA  . TYR A 1 258 ? -26.318 -8.761  -35.993 1.00 25.52 ? 247 TYR A CA  1 
ATOM   1766 C  C   . TYR A 1 258 ? -25.015 -9.218  -35.333 1.00 30.11 ? 247 TYR A C   1 
ATOM   1767 O  O   . TYR A 1 258 ? -23.915 -8.782  -35.720 1.00 28.26 ? 247 TYR A O   1 
ATOM   1768 C  CB  . TYR A 1 258 ? -26.069 -8.189  -37.395 1.00 27.20 ? 247 TYR A CB  1 
ATOM   1769 C  CG  . TYR A 1 258 ? -27.336 -7.768  -38.132 1.00 31.46 ? 247 TYR A CG  1 
ATOM   1770 C  CD1 . TYR A 1 258 ? -28.069 -8.682  -38.899 1.00 25.58 ? 247 TYR A CD1 1 
ATOM   1771 C  CD2 . TYR A 1 258 ? -27.802 -6.451  -38.056 1.00 30.35 ? 247 TYR A CD2 1 
ATOM   1772 C  CE1 . TYR A 1 258 ? -29.235 -8.299  -39.557 1.00 29.70 ? 247 TYR A CE1 1 
ATOM   1773 C  CE2 . TYR A 1 258 ? -28.962 -6.049  -38.714 1.00 31.31 ? 247 TYR A CE2 1 
ATOM   1774 C  CZ  . TYR A 1 258 ? -29.686 -6.976  -39.459 1.00 35.15 ? 247 TYR A CZ  1 
ATOM   1775 O  OH  . TYR A 1 258 ? -30.851 -6.574  -40.107 1.00 31.07 ? 247 TYR A OH  1 
ATOM   1776 N  N   . PRO A 1 259 ? -25.092 -10.104 -34.333 1.00 35.79 ? 248 PRO A N   1 
ATOM   1777 C  CA  . PRO A 1 259 ? -23.855 -10.638 -33.749 1.00 29.39 ? 248 PRO A CA  1 
ATOM   1778 C  C   . PRO A 1 259 ? -23.248 -11.649 -34.703 1.00 26.65 ? 248 PRO A C   1 
ATOM   1779 O  O   . PRO A 1 259 ? -23.943 -12.518 -35.228 1.00 34.02 ? 248 PRO A O   1 
ATOM   1780 C  CB  . PRO A 1 259 ? -24.325 -11.287 -32.442 1.00 27.74 ? 248 PRO A CB  1 
ATOM   1781 C  CG  . PRO A 1 259 ? -25.719 -11.690 -32.722 1.00 27.09 ? 248 PRO A CG  1 
ATOM   1782 C  CD  . PRO A 1 259 ? -26.291 -10.706 -33.714 1.00 30.22 ? 248 PRO A CD  1 
ATOM   1783 N  N   . LEU A 1 260 ? -21.961 -11.499 -34.963 1.00 27.68 ? 249 LEU A N   1 
ATOM   1784 C  CA  . LEU A 1 260 ? -21.232 -12.400 -35.835 1.00 29.84 ? 249 LEU A CA  1 
ATOM   1785 C  C   . LEU A 1 260 ? -20.113 -13.082 -35.066 1.00 31.34 ? 249 LEU A C   1 
ATOM   1786 O  O   . LEU A 1 260 ? -19.592 -12.530 -34.088 1.00 35.14 ? 249 LEU A O   1 
ATOM   1787 C  CB  . LEU A 1 260 ? -20.633 -11.663 -37.036 1.00 32.07 ? 249 LEU A CB  1 
ATOM   1788 C  CG  . LEU A 1 260 ? -21.637 -10.987 -37.962 1.00 31.98 ? 249 LEU A CG  1 
ATOM   1789 C  CD1 . LEU A 1 260 ? -20.879 -10.245 -39.053 1.00 32.32 ? 249 LEU A CD1 1 
ATOM   1790 C  CD2 . LEU A 1 260 ? -22.542 -12.022 -38.544 1.00 19.61 ? 249 LEU A CD2 1 
ATOM   1791 N  N   . PRO A 1 261 ? -19.733 -14.285 -35.476 1.00 28.88 ? 250 PRO A N   1 
ATOM   1792 C  CA  . PRO A 1 261 ? -18.660 -15.005 -34.784 1.00 32.25 ? 250 PRO A CA  1 
ATOM   1793 C  C   . PRO A 1 261 ? -17.285 -14.450 -35.119 1.00 35.20 ? 250 PRO A C   1 
ATOM   1794 O  O   . PRO A 1 261 ? -17.063 -13.890 -36.198 1.00 33.31 ? 250 PRO A O   1 
ATOM   1795 C  CB  . PRO A 1 261 ? -18.804 -16.440 -35.310 1.00 26.17 ? 250 PRO A CB  1 
ATOM   1796 C  CG  . PRO A 1 261 ? -19.469 -16.296 -36.604 1.00 29.63 ? 250 PRO A CG  1 
ATOM   1797 C  CD  . PRO A 1 261 ? -20.410 -15.126 -36.471 1.00 27.52 ? 250 PRO A CD  1 
ATOM   1798 N  N   . ALA A 1 262 ? -16.354 -14.629 -34.169 1.00 31.23 ? 251 ALA A N   1 
ATOM   1799 C  CA  . ALA A 1 262 ? -14.956 -14.293 -34.416 1.00 32.67 ? 251 ALA A CA  1 
ATOM   1800 C  C   . ALA A 1 262 ? -14.469 -14.963 -35.693 1.00 35.31 ? 251 ALA A C   1 
ATOM   1801 O  O   . ALA A 1 262 ? -14.915 -16.064 -36.047 1.00 33.85 ? 251 ALA A O   1 
ATOM   1802 C  CB  . ALA A 1 262 ? -14.079 -14.723 -33.241 1.00 34.18 ? 251 ALA A CB  1 
ATOM   1803 N  N   . GLY A 1 263 ? -13.554 -14.282 -36.394 1.00 28.59 ? 252 GLY A N   1 
ATOM   1804 C  CA  . GLY A 1 263 ? -13.091 -14.744 -37.689 1.00 26.95 ? 252 GLY A CA  1 
ATOM   1805 C  C   . GLY A 1 263 ? -13.956 -14.333 -38.862 1.00 31.07 ? 252 GLY A C   1 
ATOM   1806 O  O   . GLY A 1 263 ? -13.676 -14.734 -39.996 1.00 30.07 ? 252 GLY A O   1 
ATOM   1807 N  N   . SER A 1 264 ? -14.984 -13.526 -38.631 1.00 33.51 ? 253 SER A N   1 
ATOM   1808 C  CA  . SER A 1 264 ? -15.893 -13.130 -39.691 1.00 28.79 ? 253 SER A CA  1 
ATOM   1809 C  C   . SER A 1 264 ? -15.175 -12.275 -40.732 1.00 32.00 ? 253 SER A C   1 
ATOM   1810 O  O   . SER A 1 264 ? -14.338 -11.425 -40.407 1.00 31.60 ? 253 SER A O   1 
ATOM   1811 C  CB  . SER A 1 264 ? -17.081 -12.372 -39.091 1.00 31.89 ? 253 SER A CB  1 
ATOM   1812 O  OG  . SER A 1 264 ? -18.174 -13.250 -38.841 1.00 35.14 ? 253 SER A OG  1 
ATOM   1813 N  N   . ALA A 1 265 ? -15.500 -12.513 -41.993 1.00 29.76 ? 254 ALA A N   1 
ATOM   1814 C  CA  . ALA A 1 265 ? -14.983 -11.724 -43.099 1.00 32.15 ? 254 ALA A CA  1 
ATOM   1815 C  C   . ALA A 1 265 ? -16.171 -11.096 -43.852 1.00 33.91 ? 254 ALA A C   1 
ATOM   1816 O  O   . ALA A 1 265 ? -17.322 -11.154 -43.401 1.00 30.45 ? 254 ALA A O   1 
ATOM   1817 C  CB  . ALA A 1 265 ? -14.080 -12.596 -43.974 1.00 19.45 ? 254 ALA A CB  1 
ATOM   1818 N  N   . TRP A 1 266 ? -15.886 -10.491 -45.010 1.00 29.07 ? 255 TRP A N   1 
ATOM   1819 C  CA  . TRP A 1 266 ? -16.878 -9.649  -45.672 1.00 28.29 ? 255 TRP A CA  1 
ATOM   1820 C  C   . TRP A 1 266 ? -18.103 -10.436 -46.162 1.00 33.88 ? 255 TRP A C   1 
ATOM   1821 O  O   . TRP A 1 266 ? -19.204 -9.872  -46.278 1.00 25.81 ? 255 TRP A O   1 
ATOM   1822 C  CB  . TRP A 1 266 ? -16.215 -8.904  -46.828 1.00 30.32 ? 255 TRP A CB  1 
ATOM   1823 C  CG  . TRP A 1 266 ? -17.162 -8.017  -47.551 1.00 36.33 ? 255 TRP A CG  1 
ATOM   1824 C  CD1 . TRP A 1 266 ? -17.697 -8.226  -48.784 1.00 30.81 ? 255 TRP A CD1 1 
ATOM   1825 C  CD2 . TRP A 1 266 ? -17.727 -6.792  -47.066 1.00 34.85 ? 255 TRP A CD2 1 
ATOM   1826 N  NE1 . TRP A 1 266 ? -18.544 -7.202  -49.103 1.00 31.02 ? 255 TRP A NE1 1 
ATOM   1827 C  CE2 . TRP A 1 266 ? -18.589 -6.311  -48.063 1.00 27.38 ? 255 TRP A CE2 1 
ATOM   1828 C  CE3 . TRP A 1 266 ? -17.583 -6.055  -45.881 1.00 34.78 ? 255 TRP A CE3 1 
ATOM   1829 C  CZ2 . TRP A 1 266 ? -19.303 -5.117  -47.928 1.00 28.00 ? 255 TRP A CZ2 1 
ATOM   1830 C  CZ3 . TRP A 1 266 ? -18.298 -4.867  -45.749 1.00 33.79 ? 255 TRP A CZ3 1 
ATOM   1831 C  CH2 . TRP A 1 266 ? -19.143 -4.411  -46.771 1.00 27.77 ? 255 TRP A CH2 1 
ATOM   1832 N  N   . ASP A 1 267 ? -17.944 -11.723 -46.462 1.00 32.52 ? 256 ASP A N   1 
ATOM   1833 C  CA  . ASP A 1 267 ? -19.080 -12.492 -46.956 1.00 32.95 ? 256 ASP A CA  1 
ATOM   1834 C  C   . ASP A 1 267 ? -20.188 -12.587 -45.906 1.00 41.07 ? 256 ASP A C   1 
ATOM   1835 O  O   . ASP A 1 267 ? -21.380 -12.488 -46.235 1.00 37.49 ? 256 ASP A O   1 
ATOM   1836 C  CB  . ASP A 1 267 ? -18.617 -13.877 -47.384 1.00 30.47 ? 256 ASP A CB  1 
ATOM   1837 C  CG  . ASP A 1 267 ? -17.878 -14.608 -46.275 1.00 41.95 ? 256 ASP A CG  1 
ATOM   1838 O  OD1 . ASP A 1 267 ? -17.075 -13.968 -45.554 1.00 39.95 ? 256 ASP A OD1 1 
ATOM   1839 O  OD2 . ASP A 1 267 ? -18.091 -15.829 -46.131 1.00 42.65 ? 256 ASP A OD2 1 
ATOM   1840 N  N   . SER A 1 268 ? -19.818 -12.773 -44.635 1.00 33.07 ? 257 SER A N   1 
ATOM   1841 C  CA  . SER A 1 268 ? -20.820 -12.722 -43.578 1.00 31.85 ? 257 SER A CA  1 
ATOM   1842 C  C   . SER A 1 268 ? -21.152 -11.285 -43.211 1.00 32.26 ? 257 SER A C   1 
ATOM   1843 O  O   . SER A 1 268 ? -22.325 -10.899 -43.194 1.00 32.21 ? 257 SER A O   1 
ATOM   1844 C  CB  . SER A 1 268 ? -20.334 -13.470 -42.343 1.00 29.39 ? 257 SER A CB  1 
ATOM   1845 O  OG  . SER A 1 268 ? -18.999 -13.864 -42.512 1.00 37.27 ? 257 SER A OG  1 
ATOM   1846 N  N   . TRP A 1 269 ? -20.121 -10.486 -42.923 1.00 29.86 ? 258 TRP A N   1 
ATOM   1847 C  CA  . TRP A 1 269 ? -20.325 -9.117  -42.457 1.00 33.41 ? 258 TRP A CA  1 
ATOM   1848 C  C   . TRP A 1 269 ? -21.186 -8.320  -43.435 1.00 29.07 ? 258 TRP A C   1 
ATOM   1849 O  O   . TRP A 1 269 ? -22.187 -7.708  -43.050 1.00 27.31 ? 258 TRP A O   1 
ATOM   1850 C  CB  . TRP A 1 269 ? -18.964 -8.444  -42.239 1.00 28.99 ? 258 TRP A CB  1 
ATOM   1851 C  CG  . TRP A 1 269 ? -19.009 -7.270  -41.315 1.00 28.53 ? 258 TRP A CG  1 
ATOM   1852 C  CD1 . TRP A 1 269 ? -18.627 -7.244  -39.998 1.00 30.02 ? 258 TRP A CD1 1 
ATOM   1853 C  CD2 . TRP A 1 269 ? -19.452 -5.942  -41.633 1.00 29.85 ? 258 TRP A CD2 1 
ATOM   1854 N  NE1 . TRP A 1 269 ? -18.814 -5.988  -39.477 1.00 33.38 ? 258 TRP A NE1 1 
ATOM   1855 C  CE2 . TRP A 1 269 ? -19.317 -5.166  -40.457 1.00 33.46 ? 258 TRP A CE2 1 
ATOM   1856 C  CE3 . TRP A 1 269 ? -19.941 -5.329  -42.799 1.00 27.58 ? 258 TRP A CE3 1 
ATOM   1857 C  CZ2 . TRP A 1 269 ? -19.660 -3.804  -40.411 1.00 26.83 ? 258 TRP A CZ2 1 
ATOM   1858 C  CZ3 . TRP A 1 269 ? -20.282 -3.980  -42.750 1.00 25.94 ? 258 TRP A CZ3 1 
ATOM   1859 C  CH2 . TRP A 1 269 ? -20.142 -3.236  -41.560 1.00 25.28 ? 258 TRP A CH2 1 
ATOM   1860 N  N   . GLY A 1 270 ? -20.822 -8.340  -44.713 1.00 27.48 ? 259 GLY A N   1 
ATOM   1861 C  CA  . GLY A 1 270 ? -21.595 -7.628  -45.703 1.00 27.04 ? 259 GLY A CA  1 
ATOM   1862 C  C   . GLY A 1 270 ? -22.963 -8.218  -45.973 1.00 27.01 ? 259 GLY A C   1 
ATOM   1863 O  O   . GLY A 1 270 ? -23.814 -7.525  -46.538 1.00 28.40 ? 259 GLY A O   1 
ATOM   1864 N  N   . ALA A 1 271 ? -23.196 -9.488  -45.615 1.00 25.09 ? 260 ALA A N   1 
ATOM   1865 C  CA  . ALA A 1 271 ? -24.566 -9.984  -45.720 1.00 25.73 ? 260 ALA A CA  1 
ATOM   1866 C  C   . ALA A 1 271 ? -25.416 -9.444  -44.569 1.00 28.66 ? 260 ALA A C   1 
ATOM   1867 O  O   . ALA A 1 271 ? -26.588 -9.104  -44.764 1.00 25.01 ? 260 ALA A O   1 
ATOM   1868 C  CB  . ALA A 1 271 ? -24.593 -11.516 -45.792 1.00 16.97 ? 260 ALA A CB  1 
ATOM   1869 N  N   . ALA A 1 272 ? -24.823 -9.300  -43.378 1.00 27.46 ? 261 ALA A N   1 
ATOM   1870 C  CA  . ALA A 1 272 ? -25.482 -8.547  -42.319 1.00 27.33 ? 261 ALA A CA  1 
ATOM   1871 C  C   . ALA A 1 272 ? -25.729 -7.105  -42.749 1.00 30.16 ? 261 ALA A C   1 
ATOM   1872 O  O   . ALA A 1 272 ? -26.820 -6.565  -42.534 1.00 33.37 ? 261 ALA A O   1 
ATOM   1873 C  CB  . ALA A 1 272 ? -24.657 -8.587  -41.035 1.00 26.76 ? 261 ALA A CB  1 
ATOM   1874 N  N   . LEU A 1 273 ? -24.728 -6.460  -43.357 1.00 27.83 ? 262 LEU A N   1 
ATOM   1875 C  CA  . LEU A 1 273 ? -24.915 -5.073  -43.772 1.00 33.90 ? 262 LEU A CA  1 
ATOM   1876 C  C   . LEU A 1 273 ? -26.084 -4.949  -44.745 1.00 34.49 ? 262 LEU A C   1 
ATOM   1877 O  O   . LEU A 1 273 ? -26.907 -4.031  -44.636 1.00 30.34 ? 262 LEU A O   1 
ATOM   1878 C  CB  . LEU A 1 273 ? -23.634 -4.514  -44.396 1.00 27.70 ? 262 LEU A CB  1 
ATOM   1879 C  CG  . LEU A 1 273 ? -23.785 -3.128  -45.049 1.00 31.68 ? 262 LEU A CG  1 
ATOM   1880 C  CD1 . LEU A 1 273 ? -24.099 -2.049  -44.003 1.00 26.60 ? 262 LEU A CD1 1 
ATOM   1881 C  CD2 . LEU A 1 273 ? -22.550 -2.750  -45.887 1.00 27.55 ? 262 LEU A CD2 1 
ATOM   1882 N  N   . ASP A 1 274 ? -26.194 -5.889  -45.679 1.00 32.29 ? 263 ASP A N   1 
ATOM   1883 C  CA  . ASP A 1 274 ? -27.274 -5.836  -46.653 1.00 31.36 ? 263 ASP A CA  1 
ATOM   1884 C  C   . ASP A 1 274 ? -28.627 -5.959  -45.962 1.00 35.99 ? 263 ASP A C   1 
ATOM   1885 O  O   . ASP A 1 274 ? -29.534 -5.145  -46.188 1.00 36.21 ? 263 ASP A O   1 
ATOM   1886 C  CB  . ASP A 1 274 ? -27.067 -6.935  -47.688 1.00 27.12 ? 263 ASP A CB  1 
ATOM   1887 C  CG  . ASP A 1 274 ? -28.175 -7.007  -48.684 1.00 34.97 ? 263 ASP A CG  1 
ATOM   1888 O  OD1 . ASP A 1 274 ? -28.474 -5.970  -49.331 1.00 31.14 ? 263 ASP A OD1 1 
ATOM   1889 O  OD2 . ASP A 1 274 ? -28.732 -8.120  -48.827 1.00 40.15 ? 263 ASP A OD2 1 
ATOM   1890 N  N   . ASP A 1 275 ? -28.763 -6.944  -45.068 1.00 34.92 ? 264 ASP A N   1 
ATOM   1891 C  CA  . ASP A 1 275 ? -30.019 -7.106  -44.345 1.00 30.24 ? 264 ASP A CA  1 
ATOM   1892 C  C   . ASP A 1 275 ? -30.351 -5.862  -43.521 1.00 31.71 ? 264 ASP A C   1 
ATOM   1893 O  O   . ASP A 1 275 ? -31.504 -5.407  -43.508 1.00 29.51 ? 264 ASP A O   1 
ATOM   1894 C  CB  . ASP A 1 275 ? -29.954 -8.363  -43.477 1.00 26.72 ? 264 ASP A CB  1 
ATOM   1895 C  CG  . ASP A 1 275 ? -29.889 -9.660  -44.314 1.00 40.21 ? 264 ASP A CG  1 
ATOM   1896 O  OD1 . ASP A 1 275 ? -30.223 -9.631  -45.525 1.00 40.55 ? 264 ASP A OD1 1 
ATOM   1897 O  OD2 . ASP A 1 275 ? -29.499 -10.718 -43.761 1.00 46.05 ? 264 ASP A OD2 1 
ATOM   1898 N  N   . ALA A 1 276 ? -29.342 -5.273  -42.868 1.00 28.71 ? 265 ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 276 ? -29.562 -4.094  -42.037 1.00 25.82 ? 265 ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 276 ? -30.053 -2.906  -42.857 1.00 29.82 ? 265 ALA A C   1 
ATOM   1901 O  O   . ALA A 1 276 ? -30.975 -2.196  -42.442 1.00 31.38 ? 265 ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 276 ? -28.275 -3.733  -41.297 1.00 28.36 ? 265 ALA A CB  1 
ATOM   1903 N  N   . CYS A 1 277 ? -29.448 -2.670  -44.025 1.00 31.18 ? 266 CYS A N   1 
ATOM   1904 C  CA  . CYS A 1 277 ? -29.827 -1.518  -44.839 1.00 28.02 ? 266 CYS A CA  1 
ATOM   1905 C  C   . CYS A 1 277 ? -31.232 -1.683  -45.410 1.00 33.46 ? 266 CYS A C   1 
ATOM   1906 O  O   . CYS A 1 277 ? -32.003 -0.712  -45.491 1.00 28.01 ? 266 CYS A O   1 
ATOM   1907 C  CB  . CYS A 1 277 ? -28.812 -1.320  -45.964 1.00 26.52 ? 266 CYS A CB  1 
ATOM   1908 S  SG  . CYS A 1 277 ? -27.235 -0.591  -45.440 1.00 36.35 ? 266 CYS A SG  1 
ATOM   1909 N  N   . LYS A 1 278 ? -31.576 -2.905  -45.822 1.00 27.29 ? 267 LYS A N   1 
ATOM   1910 C  CA  . LYS A 1 278 ? -32.937 -3.159  -46.266 1.00 29.52 ? 267 LYS A CA  1 
ATOM   1911 C  C   . LYS A 1 278 ? -33.939 -2.847  -45.162 1.00 31.01 ? 267 LYS A C   1 
ATOM   1912 O  O   . LYS A 1 278 ? -35.014 -2.301  -45.431 1.00 32.25 ? 267 LYS A O   1 
ATOM   1913 C  CB  . LYS A 1 278 ? -33.074 -4.608  -46.729 1.00 30.99 ? 267 LYS A CB  1 
ATOM   1914 C  CG  . LYS A 1 278 ? -32.176 -4.996  -47.887 1.00 31.38 ? 267 LYS A CG  1 
ATOM   1915 C  CD  . LYS A 1 278 ? -32.921 -5.886  -48.834 1.00 29.74 ? 267 LYS A CD  1 
ATOM   1916 C  CE  . LYS A 1 278 ? -32.099 -7.105  -49.192 1.00 30.20 ? 267 LYS A CE  1 
ATOM   1917 N  NZ  . LYS A 1 278 ? -32.919 -8.335  -48.972 1.00 36.24 ? 267 LYS A NZ  1 
ATOM   1918 N  N   . ARG A 1 279 ? -33.599 -3.188  -43.915 1.00 31.09 ? 268 ARG A N   1 
ATOM   1919 C  CA  . ARG A 1 279 ? -34.483 -2.910  -42.788 1.00 31.60 ? 268 ARG A CA  1 
ATOM   1920 C  C   . ARG A 1 279 ? -34.659 -1.417  -42.590 1.00 33.82 ? 268 ARG A C   1 
ATOM   1921 O  O   . ARG A 1 279 ? -35.783 -0.927  -42.408 1.00 32.48 ? 268 ARG A O   1 
ATOM   1922 C  CB  . ARG A 1 279 ? -33.928 -3.540  -41.512 1.00 29.77 ? 268 ARG A CB  1 
ATOM   1923 C  CG  . ARG A 1 279 ? -33.981 -5.037  -41.518 1.00 32.24 ? 268 ARG A CG  1 
ATOM   1924 C  CD  . ARG A 1 279 ? -35.324 -5.549  -41.033 1.00 33.52 ? 268 ARG A CD  1 
ATOM   1925 N  NE  . ARG A 1 279 ? -35.111 -6.784  -40.298 1.00 39.96 ? 268 ARG A NE  1 
ATOM   1926 C  CZ  . ARG A 1 279 ? -35.655 -7.072  -39.128 1.00 41.84 ? 268 ARG A CZ  1 
ATOM   1927 N  NH1 . ARG A 1 279 ? -36.495 -6.238  -38.533 1.00 35.43 ? 268 ARG A NH1 1 
ATOM   1928 N  NH2 . ARG A 1 279 ? -35.357 -8.234  -38.547 1.00 45.02 ? 268 ARG A NH2 1 
ATOM   1929 N  N   . ILE A 1 280 ? -33.543 -0.685  -42.588 1.00 32.19 ? 269 ILE A N   1 
ATOM   1930 C  CA  . ILE A 1 280 ? -33.589 0.768   -42.484 1.00 31.29 ? 269 ILE A CA  1 
ATOM   1931 C  C   . ILE A 1 280 ? -34.523 1.350   -43.548 1.00 32.41 ? 269 ILE A C   1 
ATOM   1932 O  O   . ILE A 1 280 ? -35.330 2.242   -43.265 1.00 26.77 ? 269 ILE A O   1 
ATOM   1933 C  CB  . ILE A 1 280 ? -32.159 1.332   -42.585 1.00 24.66 ? 269 ILE A CB  1 
ATOM   1934 C  CG1 . ILE A 1 280 ? -31.336 0.848   -41.404 1.00 21.76 ? 269 ILE A CG1 1 
ATOM   1935 C  CG2 . ILE A 1 280 ? -32.168 2.857   -42.691 1.00 25.33 ? 269 ILE A CG2 1 
ATOM   1936 C  CD1 . ILE A 1 280 ? -29.943 1.381   -41.370 1.00 22.07 ? 269 ILE A CD1 1 
ATOM   1937 N  N   . ASN A 1 281 ? -34.461 0.816   -44.776 1.00 30.16 ? 270 ASN A N   1 
ATOM   1938 C  CA  . ASN A 1 281 ? -35.248 1.371   -45.872 1.00 26.81 ? 270 ASN A CA  1 
ATOM   1939 C  C   . ASN A 1 281 ? -36.730 1.047   -45.728 1.00 25.57 ? 270 ASN A C   1 
ATOM   1940 O  O   . ASN A 1 281 ? -37.587 1.858   -46.085 1.00 29.34 ? 270 ASN A O   1 
ATOM   1941 C  CB  . ASN A 1 281 ? -34.710 0.858   -47.206 1.00 28.91 ? 270 ASN A CB  1 
ATOM   1942 C  CG  . ASN A 1 281 ? -33.666 1.784   -47.818 1.00 25.35 ? 270 ASN A CG  1 
ATOM   1943 O  OD1 . ASN A 1 281 ? -32.658 1.337   -48.320 1.00 31.16 ? 270 ASN A OD1 1 
ATOM   1944 N  ND2 . ASN A 1 281 ? -33.913 3.071   -47.770 1.00 28.25 ? 270 ASN A ND2 1 
ATOM   1945 N  N   . ALA A 1 282 ? -37.058 -0.129  -45.209 1.00 32.11 ? 271 ALA A N   1 
ATOM   1946 C  CA  . ALA A 1 282 ? -38.462 -0.472  -44.991 1.00 32.49 ? 271 ALA A CA  1 
ATOM   1947 C  C   . ALA A 1 282 ? -39.045 0.243   -43.775 1.00 30.92 ? 271 ALA A C   1 
ATOM   1948 O  O   . ALA A 1 282 ? -40.261 0.424   -43.688 1.00 39.16 ? 271 ALA A O   1 
ATOM   1949 C  CB  . ALA A 1 282 ? -38.609 -1.978  -44.823 1.00 25.81 ? 271 ALA A CB  1 
ATOM   1950 N  N   . PHE A 1 283 ? -38.210 0.625   -42.816 1.00 25.44 ? 272 PHE A N   1 
ATOM   1951 C  CA  . PHE A 1 283 ? -38.635 1.450   -41.697 1.00 29.88 ? 272 PHE A CA  1 
ATOM   1952 C  C   . PHE A 1 283 ? -38.930 2.890   -42.118 1.00 34.95 ? 272 PHE A C   1 
ATOM   1953 O  O   . PHE A 1 283 ? -39.492 3.654   -41.322 1.00 34.54 ? 272 PHE A O   1 
ATOM   1954 C  CB  . PHE A 1 283 ? -37.538 1.357   -40.628 1.00 29.03 ? 272 PHE A CB  1 
ATOM   1955 C  CG  . PHE A 1 283 ? -37.648 2.337   -39.488 1.00 27.89 ? 272 PHE A CG  1 
ATOM   1956 C  CD1 . PHE A 1 283 ? -38.468 2.081   -38.410 1.00 28.51 ? 272 PHE A CD1 1 
ATOM   1957 C  CD2 . PHE A 1 283 ? -36.835 3.470   -39.454 1.00 30.05 ? 272 PHE A CD2 1 
ATOM   1958 C  CE1 . PHE A 1 283 ? -38.515 2.962   -37.339 1.00 36.36 ? 272 PHE A CE1 1 
ATOM   1959 C  CE2 . PHE A 1 283 ? -36.874 4.339   -38.392 1.00 27.19 ? 272 PHE A CE2 1 
ATOM   1960 C  CZ  . PHE A 1 283 ? -37.716 4.094   -37.334 1.00 28.53 ? 272 PHE A CZ  1 
ATOM   1961 N  N   . ASP A 1 284 ? -38.606 3.257   -43.361 1.00 30.71 ? 273 ASP A N   1 
ATOM   1962 C  CA  . ASP A 1 284 ? -38.827 4.602   -43.887 1.00 39.76 ? 273 ASP A CA  1 
ATOM   1963 C  C   . ASP A 1 284 ? -38.065 5.651   -43.102 1.00 41.75 ? 273 ASP A C   1 
ATOM   1964 O  O   . ASP A 1 284 ? -38.560 6.767   -42.906 1.00 43.57 ? 273 ASP A O   1 
ATOM   1965 C  CB  . ASP A 1 284 ? -40.306 4.970   -43.924 1.00 44.39 ? 273 ASP A CB  1 
ATOM   1966 C  CG  . ASP A 1 284 ? -40.918 4.661   -45.235 1.00 54.35 ? 273 ASP A CG  1 
ATOM   1967 O  OD1 . ASP A 1 284 ? -40.464 3.656   -45.843 1.00 46.58 ? 273 ASP A OD1 1 
ATOM   1968 O  OD2 . ASP A 1 284 ? -41.827 5.419   -45.654 1.00 59.27 ? 273 ASP A OD2 1 
ATOM   1969 N  N   . ALA A 1 285 ? -36.885 5.281   -42.614 1.00 34.04 ? 274 ALA A N   1 
ATOM   1970 C  CA  . ALA A 1 285 ? -35.963 6.270   -42.095 1.00 33.58 ? 274 ALA A CA  1 
ATOM   1971 C  C   . ALA A 1 285 ? -35.801 7.387   -43.118 1.00 39.56 ? 274 ALA A C   1 
ATOM   1972 O  O   . ALA A 1 285 ? -35.718 7.133   -44.323 1.00 43.26 ? 274 ALA A O   1 
ATOM   1973 C  CB  . ALA A 1 285 ? -34.615 5.620   -41.783 1.00 30.01 ? 274 ALA A CB  1 
ATOM   1974 N  N   . GLU A 1 286 ? -35.803 8.630   -42.629 1.00 34.38 ? 275 GLU A N   1 
ATOM   1975 C  CA  . GLU A 1 286 ? -35.604 9.822   -43.441 1.00 32.29 ? 275 GLU A CA  1 
ATOM   1976 C  C   . GLU A 1 286 ? -34.160 10.308  -43.451 1.00 40.78 ? 275 GLU A C   1 
ATOM   1977 O  O   . GLU A 1 286 ? -33.761 11.043  -44.367 1.00 37.00 ? 275 GLU A O   1 
ATOM   1978 C  CB  . GLU A 1 286 ? -36.496 10.941  -42.913 1.00 35.53 ? 275 GLU A CB  1 
ATOM   1979 C  CG  . GLU A 1 286 ? -37.872 10.477  -42.517 1.00 35.26 ? 275 GLU A CG  1 
ATOM   1980 C  CD  . GLU A 1 286 ? -38.675 11.609  -41.937 1.00 43.55 ? 275 GLU A CD  1 
ATOM   1981 O  OE1 . GLU A 1 286 ? -38.087 12.704  -41.772 1.00 41.15 ? 275 GLU A OE1 1 
ATOM   1982 O  OE2 . GLU A 1 286 ? -39.878 11.415  -41.651 1.00 42.15 ? 275 GLU A OE2 1 
ATOM   1983 N  N   . VAL A 1 287 ? -33.405 9.963   -42.416 1.00 33.31 ? 276 VAL A N   1 
ATOM   1984 C  CA  . VAL A 1 287 ? -31.973 10.166  -42.329 1.00 29.10 ? 276 VAL A CA  1 
ATOM   1985 C  C   . VAL A 1 287 ? -31.441 8.882   -41.713 1.00 37.60 ? 276 VAL A C   1 
ATOM   1986 O  O   . VAL A 1 287 ? -32.144 8.202   -40.958 1.00 35.09 ? 276 VAL A O   1 
ATOM   1987 C  CB  . VAL A 1 287 ? -31.592 11.402  -41.463 1.00 27.49 ? 276 VAL A CB  1 
ATOM   1988 C  CG1 . VAL A 1 287 ? -30.117 11.713  -41.573 1.00 28.50 ? 276 VAL A CG1 1 
ATOM   1989 C  CG2 . VAL A 1 287 ? -32.395 12.613  -41.853 1.00 32.89 ? 276 VAL A CG2 1 
ATOM   1990 N  N   . VAL A 1 288 ? -30.200 8.537   -42.044 1.00 34.63 ? 277 VAL A N   1 
ATOM   1991 C  CA  . VAL A 1 288 ? -29.498 7.462   -41.361 1.00 31.99 ? 277 VAL A CA  1 
ATOM   1992 C  C   . VAL A 1 288 ? -28.226 8.050   -40.756 1.00 31.85 ? 277 VAL A C   1 
ATOM   1993 O  O   . VAL A 1 288 ? -27.531 8.848   -41.396 1.00 27.73 ? 277 VAL A O   1 
ATOM   1994 C  CB  . VAL A 1 288 ? -29.223 6.261   -42.295 1.00 31.94 ? 277 VAL A CB  1 
ATOM   1995 C  CG1 . VAL A 1 288 ? -28.666 6.717   -43.605 1.00 29.66 ? 277 VAL A CG1 1 
ATOM   1996 C  CG2 . VAL A 1 288 ? -28.299 5.228   -41.630 1.00 28.29 ? 277 VAL A CG2 1 
ATOM   1997 N  N   . ILE A 1 289 ? -27.975 7.701   -39.496 1.00 29.57 ? 278 ILE A N   1 
ATOM   1998 C  CA  . ILE A 1 289 ? -26.822 8.140   -38.728 1.00 24.45 ? 278 ILE A CA  1 
ATOM   1999 C  C   . ILE A 1 289 ? -25.906 6.927   -38.598 1.00 29.14 ? 278 ILE A C   1 
ATOM   2000 O  O   . ILE A 1 289 ? -26.266 5.920   -37.975 1.00 32.61 ? 278 ILE A O   1 
ATOM   2001 C  CB  . ILE A 1 289 ? -27.249 8.690   -37.361 1.00 26.24 ? 278 ILE A CB  1 
ATOM   2002 C  CG1 . ILE A 1 289 ? -28.109 9.941   -37.554 1.00 23.66 ? 278 ILE A CG1 1 
ATOM   2003 C  CG2 . ILE A 1 289 ? -26.055 8.940   -36.436 1.00 23.89 ? 278 ILE A CG2 1 
ATOM   2004 C  CD1 . ILE A 1 289 ? -29.577 9.693   -37.319 1.00 25.50 ? 278 ILE A CD1 1 
ATOM   2005 N  N   . VAL A 1 290 ? -24.740 6.990   -39.224 1.00 28.02 ? 279 VAL A N   1 
ATOM   2006 C  CA  . VAL A 1 290 ? -23.823 5.862   -39.274 1.00 29.60 ? 279 VAL A CA  1 
ATOM   2007 C  C   . VAL A 1 290 ? -22.811 6.036   -38.154 1.00 29.51 ? 279 VAL A C   1 
ATOM   2008 O  O   . VAL A 1 290 ? -22.076 7.034   -38.125 1.00 26.99 ? 279 VAL A O   1 
ATOM   2009 C  CB  . VAL A 1 290 ? -23.133 5.755   -40.644 1.00 29.31 ? 279 VAL A CB  1 
ATOM   2010 C  CG1 . VAL A 1 290 ? -22.327 4.481   -40.711 1.00 25.67 ? 279 VAL A CG1 1 
ATOM   2011 C  CG2 . VAL A 1 290 ? -24.156 5.804   -41.775 1.00 20.89 ? 279 VAL A CG2 1 
ATOM   2012 N  N   . SER A 1 291 ? -22.798 5.078   -37.218 1.00 32.10 ? 280 SER A N   1 
ATOM   2013 C  CA  . SER A 1 291 ? -21.783 4.973   -36.161 1.00 30.01 ? 280 SER A CA  1 
ATOM   2014 C  C   . SER A 1 291 ? -20.562 4.263   -36.734 1.00 26.85 ? 280 SER A C   1 
ATOM   2015 O  O   . SER A 1 291 ? -20.453 3.043   -36.680 1.00 25.92 ? 280 SER A O   1 
ATOM   2016 C  CB  . SER A 1 291 ? -22.326 4.219   -34.954 1.00 26.45 ? 280 SER A CB  1 
ATOM   2017 O  OG  . SER A 1 291 ? -22.813 5.097   -33.976 1.00 25.54 ? 280 SER A OG  1 
ATOM   2018 N  N   . LEU A 1 292 ? -19.626 5.047   -37.274 1.00 29.24 ? 281 LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 292 ? -18.533 4.548   -38.113 1.00 26.82 ? 281 LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 292 ? -17.303 4.258   -37.259 1.00 27.91 ? 281 LEU A C   1 
ATOM   2021 O  O   . LEU A 1 292 ? -16.462 5.126   -37.020 1.00 29.76 ? 281 LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 292 ? -18.216 5.549   -39.214 1.00 20.53 ? 281 LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 292 ? -17.033 5.195   -40.107 1.00 24.80 ? 281 LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 292 ? -17.344 3.946   -40.871 1.00 33.15 ? 281 LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 292 ? -16.722 6.315   -41.072 1.00 30.16 ? 281 LEU A CD2 1 
ATOM   2026 N  N   . GLY A 1 293 ? -17.197 3.017   -36.796 1.00 28.47 ? 282 GLY A N   1 
ATOM   2027 C  CA  . GLY A 1 293 ? -15.952 2.486   -36.258 1.00 30.82 ? 282 GLY A CA  1 
ATOM   2028 C  C   . GLY A 1 293 ? -15.297 1.578   -37.282 1.00 30.71 ? 282 GLY A C   1 
ATOM   2029 O  O   . GLY A 1 293 ? -15.979 0.835   -37.987 1.00 32.83 ? 282 GLY A O   1 
ATOM   2030 N  N   . VAL A 1 294 ? -13.965 1.656   -37.385 1.00 31.45 ? 283 VAL A N   1 
ATOM   2031 C  CA  . VAL A 1 294 ? -13.264 0.813   -38.355 1.00 35.67 ? 283 VAL A CA  1 
ATOM   2032 C  C   . VAL A 1 294 ? -12.304 -0.120  -37.636 1.00 34.10 ? 283 VAL A C   1 
ATOM   2033 O  O   . VAL A 1 294 ? -11.269 -0.510  -38.193 1.00 30.75 ? 283 VAL A O   1 
ATOM   2034 C  CB  . VAL A 1 294 ? -12.532 1.637   -39.432 1.00 32.17 ? 283 VAL A CB  1 
ATOM   2035 C  CG1 . VAL A 1 294 ? -13.564 2.200   -40.423 1.00 32.74 ? 283 VAL A CG1 1 
ATOM   2036 C  CG2 . VAL A 1 294 ? -11.654 2.746   -38.813 1.00 30.90 ? 283 VAL A CG2 1 
ATOM   2037 N  N   . ASP A 1 295 ? -12.655 -0.491  -36.394 1.00 33.55 ? 284 ASP A N   1 
ATOM   2038 C  CA  . ASP A 1 295 ? -11.928 -1.505  -35.641 1.00 31.38 ? 284 ASP A CA  1 
ATOM   2039 C  C   . ASP A 1 295 ? -12.365 -2.930  -36.001 1.00 30.19 ? 284 ASP A C   1 
ATOM   2040 O  O   . ASP A 1 295 ? -12.038 -3.865  -35.268 1.00 31.54 ? 284 ASP A O   1 
ATOM   2041 C  CB  . ASP A 1 295 ? -12.048 -1.256  -34.124 1.00 26.06 ? 284 ASP A CB  1 
ATOM   2042 C  CG  . ASP A 1 295 ? -13.484 -1.116  -33.641 1.00 29.30 ? 284 ASP A CG  1 
ATOM   2043 O  OD1 . ASP A 1 295 ? -14.411 -1.060  -34.474 1.00 29.43 ? 284 ASP A OD1 1 
ATOM   2044 O  OD2 . ASP A 1 295 ? -13.684 -1.053  -32.405 1.00 31.99 ? 284 ASP A OD2 1 
ATOM   2045 N  N   . THR A 1 296 ? -13.100 -3.097  -37.103 1.00 28.66 ? 285 THR A N   1 
ATOM   2046 C  CA  . THR A 1 296 ? -13.321 -4.394  -37.727 1.00 27.80 ? 285 THR A CA  1 
ATOM   2047 C  C   . THR A 1 296 ? -12.126 -4.859  -38.557 1.00 32.23 ? 285 THR A C   1 
ATOM   2048 O  O   . THR A 1 296 ? -12.107 -6.026  -38.966 1.00 36.68 ? 285 THR A O   1 
ATOM   2049 C  CB  . THR A 1 296 ? -14.556 -4.355  -38.646 1.00 26.18 ? 285 THR A CB  1 
ATOM   2050 O  OG1 . THR A 1 296 ? -14.545 -3.148  -39.414 1.00 33.23 ? 285 THR A OG1 1 
ATOM   2051 C  CG2 . THR A 1 296 ? -15.851 -4.450  -37.882 1.00 22.30 ? 285 THR A CG2 1 
ATOM   2052 N  N   . TYR A 1 297 ? -11.159 -3.969  -38.828 1.00 32.12 ? 286 TYR A N   1 
ATOM   2053 C  CA  . TYR A 1 297 ? -10.003 -4.244  -39.688 1.00 28.15 ? 286 TYR A CA  1 
ATOM   2054 C  C   . TYR A 1 297 ? -9.205  -5.438  -39.189 1.00 32.76 ? 286 TYR A C   1 
ATOM   2055 O  O   . TYR A 1 297 ? -9.011  -5.599  -37.984 1.00 34.84 ? 286 TYR A O   1 
ATOM   2056 C  CB  . TYR A 1 297 ? -9.109  -3.011  -39.704 1.00 30.67 ? 286 TYR A CB  1 
ATOM   2057 C  CG  . TYR A 1 297 ? -7.929  -3.007  -40.645 1.00 30.31 ? 286 TYR A CG  1 
ATOM   2058 C  CD1 . TYR A 1 297 ? -8.047  -3.447  -41.949 1.00 28.26 ? 286 TYR A CD1 1 
ATOM   2059 C  CD2 . TYR A 1 297 ? -6.704  -2.496  -40.230 1.00 28.50 ? 286 TYR A CD2 1 
ATOM   2060 C  CE1 . TYR A 1 297 ? -6.976  -3.401  -42.806 1.00 32.01 ? 286 TYR A CE1 1 
ATOM   2061 C  CE2 . TYR A 1 297 ? -5.636  -2.441  -41.069 1.00 28.76 ? 286 TYR A CE2 1 
ATOM   2062 C  CZ  . TYR A 1 297 ? -5.766  -2.903  -42.360 1.00 35.61 ? 286 TYR A CZ  1 
ATOM   2063 O  OH  . TYR A 1 297 ? -4.684  -2.861  -43.211 1.00 35.53 ? 286 TYR A OH  1 
ATOM   2064 N  N   . LYS A 1 298 ? -8.713  -6.267  -40.120 1.00 36.03 ? 287 LYS A N   1 
ATOM   2065 C  CA  . LYS A 1 298 ? -7.978  -7.460  -39.698 1.00 36.40 ? 287 LYS A CA  1 
ATOM   2066 C  C   . LYS A 1 298 ? -6.696  -7.102  -38.954 1.00 37.81 ? 287 LYS A C   1 
ATOM   2067 O  O   . LYS A 1 298 ? -6.265  -7.853  -38.068 1.00 37.28 ? 287 LYS A O   1 
ATOM   2068 C  CB  . LYS A 1 298 ? -7.636  -8.381  -40.876 1.00 37.77 ? 287 LYS A CB  1 
ATOM   2069 C  CG  . LYS A 1 298 ? -7.139  -7.745  -42.164 1.00 42.94 ? 287 LYS A CG  1 
ATOM   2070 C  CD  . LYS A 1 298 ? -7.029  -8.828  -43.249 1.00 45.02 ? 287 LYS A CD  1 
ATOM   2071 C  CE  . LYS A 1 298 ? -5.912  -8.536  -44.267 1.00 51.03 ? 287 LYS A CE  1 
ATOM   2072 N  NZ  . LYS A 1 298 ? -6.260  -9.025  -45.646 1.00 51.74 ? 287 LYS A NZ  1 
ATOM   2073 N  N   . GLU A 1 299 ? -6.084  -5.961  -39.271 1.00 32.10 ? 288 GLU A N   1 
ATOM   2074 C  CA  . GLU A 1 299 ? -4.877  -5.557  -38.570 1.00 29.76 ? 288 GLU A CA  1 
ATOM   2075 C  C   . GLU A 1 299 ? -5.146  -4.737  -37.318 1.00 35.23 ? 288 GLU A C   1 
ATOM   2076 O  O   . GLU A 1 299 ? -4.190  -4.315  -36.667 1.00 40.47 ? 288 GLU A O   1 
ATOM   2077 C  CB  . GLU A 1 299 ? -3.955  -4.768  -39.498 1.00 38.83 ? 288 GLU A CB  1 
ATOM   2078 C  CG  . GLU A 1 299 ? -3.631  -5.451  -40.813 1.00 39.86 ? 288 GLU A CG  1 
ATOM   2079 C  CD  . GLU A 1 299 ? -3.221  -6.888  -40.626 1.00 41.70 ? 288 GLU A CD  1 
ATOM   2080 O  OE1 . GLU A 1 299 ? -2.478  -7.187  -39.667 1.00 47.26 ? 288 GLU A OE1 1 
ATOM   2081 O  OE2 . GLU A 1 299 ? -3.647  -7.729  -41.438 1.00 55.01 ? 288 GLU A OE2 1 
ATOM   2082 N  N   . ASP A 1 300 ? -6.400  -4.477  -36.969 1.00 36.69 ? 289 ASP A N   1 
ATOM   2083 C  CA  . ASP A 1 300 ? -6.680  -3.776  -35.724 1.00 31.96 ? 289 ASP A CA  1 
ATOM   2084 C  C   . ASP A 1 300 ? -6.416  -4.724  -34.561 1.00 36.93 ? 289 ASP A C   1 
ATOM   2085 O  O   . ASP A 1 300 ? -6.821  -5.891  -34.625 1.00 38.75 ? 289 ASP A O   1 
ATOM   2086 C  CB  . ASP A 1 300 ? -8.119  -3.290  -35.713 1.00 33.91 ? 289 ASP A CB  1 
ATOM   2087 C  CG  . ASP A 1 300 ? -8.357  -2.162  -34.725 1.00 37.10 ? 289 ASP A CG  1 
ATOM   2088 O  OD1 . ASP A 1 300 ? -8.341  -2.428  -33.495 1.00 35.03 ? 289 ASP A OD1 1 
ATOM   2089 O  OD2 . ASP A 1 300 ? -8.593  -1.017  -35.189 1.00 35.37 ? 289 ASP A OD2 1 
ATOM   2090 N  N   . PRO A 1 301 ? -5.724  -4.285  -33.501 1.00 41.13 ? 290 PRO A N   1 
ATOM   2091 C  CA  . PRO A 1 301 ? -5.383  -5.230  -32.424 1.00 40.14 ? 290 PRO A CA  1 
ATOM   2092 C  C   . PRO A 1 301 ? -6.594  -5.712  -31.641 1.00 46.54 ? 290 PRO A C   1 
ATOM   2093 O  O   . PRO A 1 301 ? -6.596  -6.860  -31.173 1.00 43.52 ? 290 PRO A O   1 
ATOM   2094 C  CB  . PRO A 1 301 ? -4.417  -4.437  -31.528 1.00 33.11 ? 290 PRO A CB  1 
ATOM   2095 C  CG  . PRO A 1 301 ? -4.503  -3.029  -31.954 1.00 41.50 ? 290 PRO A CG  1 
ATOM   2096 C  CD  . PRO A 1 301 ? -5.418  -2.896  -33.128 1.00 45.51 ? 290 PRO A CD  1 
ATOM   2097 N  N   . ILE A 1 302 ? -7.628  -4.878  -31.490 1.00 39.96 ? 291 ILE A N   1 
ATOM   2098 C  CA  . ILE A 1 302 ? -8.802  -5.299  -30.734 1.00 40.59 ? 291 ILE A CA  1 
ATOM   2099 C  C   . ILE A 1 302 ? -9.795  -6.068  -31.587 1.00 43.85 ? 291 ILE A C   1 
ATOM   2100 O  O   . ILE A 1 302 ? -10.739 -6.668  -31.050 1.00 43.23 ? 291 ILE A O   1 
ATOM   2101 C  CB  . ILE A 1 302 ? -9.454  -4.065  -30.090 1.00 46.49 ? 291 ILE A CB  1 
ATOM   2102 C  CG1 . ILE A 1 302 ? -9.903  -4.413  -28.666 1.00 52.54 ? 291 ILE A CG1 1 
ATOM   2103 C  CG2 . ILE A 1 302 ? -10.583 -3.528  -30.970 1.00 36.04 ? 291 ILE A CG2 1 
ATOM   2104 C  CD1 . ILE A 1 302 ? -8.746  -4.598  -27.646 1.00 48.49 ? 291 ILE A CD1 1 
ATOM   2105 N  N   . SER A 1 303 ? -9.579  -6.103  -32.897 1.00 43.50 ? 292 SER A N   1 
ATOM   2106 C  CA  . SER A 1 303 ? -10.502 -6.755  -33.809 1.00 38.26 ? 292 SER A CA  1 
ATOM   2107 C  C   . SER A 1 303 ? -10.415 -8.271  -33.717 1.00 32.48 ? 292 SER A C   1 
ATOM   2108 O  O   . SER A 1 303 ? -9.363  -8.846  -33.439 1.00 39.40 ? 292 SER A O   1 
ATOM   2109 C  CB  . SER A 1 303 ? -10.207 -6.323  -35.238 1.00 34.04 ? 292 SER A CB  1 
ATOM   2110 O  OG  . SER A 1 303 ? -10.976 -7.081  -36.149 1.00 37.36 ? 292 SER A OG  1 
ATOM   2111 N  N   . GLN A 1 304 ? -11.540 -8.920  -33.983 1.00 34.70 ? 293 GLN A N   1 
ATOM   2112 C  CA  . GLN A 1 304 ? -11.541 -10.342 -34.295 1.00 37.95 ? 293 GLN A CA  1 
ATOM   2113 C  C   . GLN A 1 304 ? -12.257 -10.641 -35.610 1.00 37.68 ? 293 GLN A C   1 
ATOM   2114 O  O   . GLN A 1 304 ? -12.494 -11.815 -35.926 1.00 39.40 ? 293 GLN A O   1 
ATOM   2115 C  CB  . GLN A 1 304 ? -12.153 -11.145 -33.148 1.00 35.11 ? 293 GLN A CB  1 
ATOM   2116 C  CG  . GLN A 1 304 ? -11.140 -11.498 -32.071 1.00 35.33 ? 293 GLN A CG  1 
ATOM   2117 C  CD  . GLN A 1 304 ? -11.768 -12.249 -30.916 1.00 51.58 ? 293 GLN A CD  1 
ATOM   2118 O  OE1 . GLN A 1 304 ? -12.064 -11.670 -29.872 1.00 56.45 ? 293 GLN A OE1 1 
ATOM   2119 N  NE2 . GLN A 1 304 ? -11.978 -13.550 -31.097 1.00 60.08 ? 293 GLN A NE2 1 
ATOM   2120 N  N   . PHE A 1 305 ? -12.599 -9.614  -36.384 1.00 33.62 ? 294 PHE A N   1 
ATOM   2121 C  CA  . PHE A 1 305 ? -13.111 -9.756  -37.736 1.00 29.16 ? 294 PHE A CA  1 
ATOM   2122 C  C   . PHE A 1 305 ? -11.955 -9.663  -38.740 1.00 32.30 ? 294 PHE A C   1 
ATOM   2123 O  O   . PHE A 1 305 ? -10.834 -9.289  -38.400 1.00 37.46 ? 294 PHE A O   1 
ATOM   2124 C  CB  . PHE A 1 305 ? -14.183 -8.694  -37.990 1.00 27.48 ? 294 PHE A CB  1 
ATOM   2125 C  CG  . PHE A 1 305 ? -15.479 -8.932  -37.214 1.00 32.77 ? 294 PHE A CG  1 
ATOM   2126 C  CD1 . PHE A 1 305 ? -15.681 -10.128 -36.504 1.00 30.27 ? 294 PHE A CD1 1 
ATOM   2127 C  CD2 . PHE A 1 305 ? -16.500 -7.972  -37.207 1.00 25.47 ? 294 PHE A CD2 1 
ATOM   2128 C  CE1 . PHE A 1 305 ? -16.858 -10.359 -35.790 1.00 27.53 ? 294 PHE A CE1 1 
ATOM   2129 C  CE2 . PHE A 1 305 ? -17.684 -8.193  -36.495 1.00 26.70 ? 294 PHE A CE2 1 
ATOM   2130 C  CZ  . PHE A 1 305 ? -17.861 -9.394  -35.785 1.00 29.52 ? 294 PHE A CZ  1 
ATOM   2131 N  N   . LYS A 1 306 ? -12.218 -10.036 -39.989 1.00 31.51 ? 295 LYS A N   1 
ATOM   2132 C  CA  . LYS A 1 306 ? -11.122 -10.075 -40.956 1.00 37.79 ? 295 LYS A CA  1 
ATOM   2133 C  C   . LYS A 1 306 ? -11.398 -9.170  -42.160 1.00 38.58 ? 295 LYS A C   1 
ATOM   2134 O  O   . LYS A 1 306 ? -11.264 -9.602  -43.311 1.00 39.39 ? 295 LYS A O   1 
ATOM   2135 C  CB  . LYS A 1 306 ? -10.853 -11.519 -41.442 1.00 35.31 ? 295 LYS A CB  1 
ATOM   2136 C  CG  . LYS A 1 306 ? -10.535 -12.575 -40.374 1.00 30.77 ? 295 LYS A CG  1 
ATOM   2137 C  CD  . LYS A 1 306 ? -9.347  -12.210 -39.469 1.00 46.16 ? 295 LYS A CD  1 
ATOM   2138 C  CE  . LYS A 1 306 ? -7.995  -12.638 -40.070 1.00 57.86 ? 295 LYS A CE  1 
ATOM   2139 N  NZ  . LYS A 1 306 ? -6.813  -11.929 -39.476 1.00 52.32 ? 295 LYS A NZ  1 
ATOM   2140 N  N   . LEU A 1 307 ? -11.770 -7.915  -41.914 1.00 37.39 ? 296 LEU A N   1 
ATOM   2141 C  CA  . LEU A 1 307 ? -12.071 -6.988  -42.999 1.00 33.76 ? 296 LEU A CA  1 
ATOM   2142 C  C   . LEU A 1 307 ? -10.788 -6.368  -43.530 1.00 36.70 ? 296 LEU A C   1 
ATOM   2143 O  O   . LEU A 1 307 ? -9.858  -6.090  -42.769 1.00 39.52 ? 296 LEU A O   1 
ATOM   2144 C  CB  . LEU A 1 307 ? -13.019 -5.894  -42.516 1.00 30.44 ? 296 LEU A CB  1 
ATOM   2145 C  CG  . LEU A 1 307 ? -14.503 -6.044  -42.833 1.00 32.40 ? 296 LEU A CG  1 
ATOM   2146 C  CD1 . LEU A 1 307 ? -15.017 -7.458  -42.606 1.00 31.05 ? 296 LEU A CD1 1 
ATOM   2147 C  CD2 . LEU A 1 307 ? -15.310 -5.027  -42.056 1.00 33.01 ? 296 LEU A CD2 1 
ATOM   2148 N  N   . ASP A 1 308 ? -10.728 -6.161  -44.841 1.00 36.97 ? 297 ASP A N   1 
ATOM   2149 C  CA  . ASP A 1 308 ? -9.594  -5.470  -45.437 1.00 38.61 ? 297 ASP A CA  1 
ATOM   2150 C  C   . ASP A 1 308 ? -10.006 -4.079  -45.899 1.00 38.76 ? 297 ASP A C   1 
ATOM   2151 O  O   . ASP A 1 308 ? -11.191 -3.770  -46.031 1.00 41.57 ? 297 ASP A O   1 
ATOM   2152 C  CB  . ASP A 1 308 ? -8.989  -6.249  -46.612 1.00 35.25 ? 297 ASP A CB  1 
ATOM   2153 C  CG  . ASP A 1 308 ? -7.447  -6.088  -46.680 1.00 53.70 ? 297 ASP A CG  1 
ATOM   2154 O  OD1 . ASP A 1 308 ? -6.911  -5.167  -46.014 1.00 55.22 ? 297 ASP A OD1 1 
ATOM   2155 O  OD2 . ASP A 1 308 ? -6.763  -6.885  -47.374 1.00 58.73 ? 297 ASP A OD2 1 
ATOM   2156 N  N   . SER A 1 309 ? -9.010  -3.231  -46.131 1.00 37.89 ? 298 SER A N   1 
ATOM   2157 C  CA  . SER A 1 309 ? -9.298  -1.874  -46.583 1.00 33.97 ? 298 SER A CA  1 
ATOM   2158 C  C   . SER A 1 309 ? -10.238 -1.829  -47.783 1.00 31.66 ? 298 SER A C   1 
ATOM   2159 O  O   . SER A 1 309 ? -11.124 -0.958  -47.796 1.00 33.52 ? 298 SER A O   1 
ATOM   2160 C  CB  . SER A 1 309 ? -7.982  -1.137  -46.867 1.00 30.87 ? 298 SER A CB  1 
ATOM   2161 O  OG  . SER A 1 309 ? -7.220  -0.989  -45.678 1.00 35.89 ? 298 SER A OG  1 
ATOM   2162 N  N   . PRO A 1 310 ? -10.131 -2.702  -48.792 1.00 33.18 ? 299 PRO A N   1 
ATOM   2163 C  CA  . PRO A 1 310 ? -11.148 -2.695  -49.860 1.00 31.35 ? 299 PRO A CA  1 
ATOM   2164 C  C   . PRO A 1 310 ? -12.571 -2.862  -49.354 1.00 31.84 ? 299 PRO A C   1 
ATOM   2165 O  O   . PRO A 1 310 ? -13.495 -2.255  -49.913 1.00 24.06 ? 299 PRO A O   1 
ATOM   2166 C  CB  . PRO A 1 310 ? -10.717 -3.876  -50.736 1.00 29.05 ? 299 PRO A CB  1 
ATOM   2167 C  CG  . PRO A 1 310 ? -9.236  -3.838  -50.628 1.00 25.63 ? 299 PRO A CG  1 
ATOM   2168 C  CD  . PRO A 1 310 ? -8.950  -3.490  -49.194 1.00 32.37 ? 299 PRO A CD  1 
ATOM   2169 N  N   . ASP A 1 311 ? -12.762 -3.655  -48.295 1.00 31.40 ? 300 ASP A N   1 
ATOM   2170 C  CA  . ASP A 1 311 ? -14.093 -3.879  -47.753 1.00 25.70 ? 300 ASP A CA  1 
ATOM   2171 C  C   . ASP A 1 311 ? -14.770 -2.576  -47.343 1.00 29.80 ? 300 ASP A C   1 
ATOM   2172 O  O   . ASP A 1 311 ? -16.005 -2.489  -47.373 1.00 30.25 ? 300 ASP A O   1 
ATOM   2173 C  CB  . ASP A 1 311 ? -14.019 -4.844  -46.568 1.00 29.57 ? 300 ASP A CB  1 
ATOM   2174 C  CG  . ASP A 1 311 ? -13.644 -6.279  -46.981 1.00 35.18 ? 300 ASP A CG  1 
ATOM   2175 O  OD1 . ASP A 1 311 ? -13.882 -6.650  -48.152 1.00 31.62 ? 300 ASP A OD1 1 
ATOM   2176 O  OD2 . ASP A 1 311 ? -13.117 -7.038  -46.126 1.00 34.38 ? 300 ASP A OD2 1 
ATOM   2177 N  N   . TYR A 1 312 ? -13.994 -1.547  -46.987 1.00 26.34 ? 301 TYR A N   1 
ATOM   2178 C  CA  . TYR A 1 312 ? -14.604 -0.312  -46.502 1.00 26.27 ? 301 TYR A CA  1 
ATOM   2179 C  C   . TYR A 1 312 ? -15.205 0.515   -47.641 1.00 29.28 ? 301 TYR A C   1 
ATOM   2180 O  O   . TYR A 1 312 ? -16.259 1.139   -47.465 1.00 27.33 ? 301 TYR A O   1 
ATOM   2181 C  CB  . TYR A 1 312 ? -13.579 0.476   -45.684 1.00 23.43 ? 301 TYR A CB  1 
ATOM   2182 C  CG  . TYR A 1 312 ? -13.189 -0.308  -44.461 1.00 25.86 ? 301 TYR A CG  1 
ATOM   2183 C  CD1 . TYR A 1 312 ? -14.072 -0.430  -43.404 1.00 27.53 ? 301 TYR A CD1 1 
ATOM   2184 C  CD2 . TYR A 1 312 ? -11.973 -0.989  -44.386 1.00 29.20 ? 301 TYR A CD2 1 
ATOM   2185 C  CE1 . TYR A 1 312 ? -13.766 -1.178  -42.298 1.00 29.48 ? 301 TYR A CE1 1 
ATOM   2186 C  CE2 . TYR A 1 312 ? -11.643 -1.745  -43.261 1.00 28.56 ? 301 TYR A CE2 1 
ATOM   2187 C  CZ  . TYR A 1 312 ? -12.559 -1.837  -42.225 1.00 30.63 ? 301 TYR A CZ  1 
ATOM   2188 O  OH  . TYR A 1 312 ? -12.305 -2.571  -41.094 1.00 29.62 ? 301 TYR A OH  1 
ATOM   2189 N  N   . LEU A 1 313 ? -14.568 0.519   -48.817 1.00 29.98 ? 302 LEU A N   1 
ATOM   2190 C  CA  . LEU A 1 313 ? -15.210 1.077   -50.008 1.00 27.08 ? 302 LEU A CA  1 
ATOM   2191 C  C   . LEU A 1 313 ? -16.559 0.429   -50.251 1.00 29.13 ? 302 LEU A C   1 
ATOM   2192 O  O   . LEU A 1 313 ? -17.563 1.109   -50.492 1.00 26.90 ? 302 LEU A O   1 
ATOM   2193 C  CB  . LEU A 1 313 ? -14.331 0.861   -51.224 1.00 20.80 ? 302 LEU A CB  1 
ATOM   2194 C  CG  . LEU A 1 313 ? -13.117 1.754   -51.220 1.00 27.03 ? 302 LEU A CG  1 
ATOM   2195 C  CD1 . LEU A 1 313 ? -12.084 1.165   -52.164 1.00 14.85 ? 302 LEU A CD1 1 
ATOM   2196 C  CD2 . LEU A 1 313 ? -13.542 3.200   -51.589 1.00 24.26 ? 302 LEU A CD2 1 
ATOM   2197 N  N   . SER A 1 314 ? -16.587 -0.903  -50.196 1.00 32.87 ? 303 SER A N   1 
ATOM   2198 C  CA  . SER A 1 314 ? -17.807 -1.658  -50.427 1.00 28.44 ? 303 SER A CA  1 
ATOM   2199 C  C   . SER A 1 314 ? -18.869 -1.322  -49.402 1.00 28.34 ? 303 SER A C   1 
ATOM   2200 O  O   . SER A 1 314 ? -20.063 -1.310  -49.722 1.00 28.74 ? 303 SER A O   1 
ATOM   2201 C  CB  . SER A 1 314 ? -17.480 -3.141  -50.401 1.00 26.50 ? 303 SER A CB  1 
ATOM   2202 O  OG  . SER A 1 314 ? -16.487 -3.406  -51.371 1.00 35.79 ? 303 SER A OG  1 
ATOM   2203 N  N   . MET A 1 315 ? -18.443 -1.041  -48.174 1.00 31.82 ? 304 MET A N   1 
ATOM   2204 C  CA  . MET A 1 315 ? -19.366 -0.655  -47.117 1.00 28.30 ? 304 MET A CA  1 
ATOM   2205 C  C   . MET A 1 315 ? -19.937 0.730   -47.380 1.00 28.05 ? 304 MET A C   1 
ATOM   2206 O  O   . MET A 1 315 ? -21.108 0.994   -47.078 1.00 28.59 ? 304 MET A O   1 
ATOM   2207 C  CB  . MET A 1 315 ? -18.630 -0.713  -45.785 1.00 26.84 ? 304 MET A CB  1 
ATOM   2208 C  CG  . MET A 1 315 ? -19.473 -0.622  -44.554 1.00 26.33 ? 304 MET A CG  1 
ATOM   2209 S  SD  . MET A 1 315 ? -18.368 -0.105  -43.243 1.00 26.85 ? 304 MET A SD  1 
ATOM   2210 C  CE  . MET A 1 315 ? -17.494 -1.667  -42.968 1.00 25.76 ? 304 MET A CE  1 
ATOM   2211 N  N   . GLY A 1 316 ? -19.127 1.617   -47.966 1.00 29.14 ? 305 GLY A N   1 
ATOM   2212 C  CA  . GLY A 1 316 ? -19.633 2.919   -48.362 1.00 30.33 ? 305 GLY A CA  1 
ATOM   2213 C  C   . GLY A 1 316 ? -20.574 2.838   -49.551 1.00 28.62 ? 305 GLY A C   1 
ATOM   2214 O  O   . GLY A 1 316 ? -21.565 3.572   -49.627 1.00 27.47 ? 305 GLY A O   1 
ATOM   2215 N  N   . GLU A 1 317 ? -20.285 1.943   -50.493 1.00 30.32 ? 306 GLU A N   1 
ATOM   2216 C  CA  . GLU A 1 317 ? -21.132 1.832   -51.676 1.00 29.77 ? 306 GLU A CA  1 
ATOM   2217 C  C   . GLU A 1 317 ? -22.493 1.259   -51.320 1.00 28.42 ? 306 GLU A C   1 
ATOM   2218 O  O   . GLU A 1 317 ? -23.515 1.648   -51.903 1.00 27.26 ? 306 GLU A O   1 
ATOM   2219 C  CB  . GLU A 1 317 ? -20.442 0.977   -52.727 1.00 25.43 ? 306 GLU A CB  1 
ATOM   2220 C  CG  . GLU A 1 317 ? -19.156 1.564   -53.182 1.00 29.49 ? 306 GLU A CG  1 
ATOM   2221 C  CD  . GLU A 1 317 ? -18.851 1.228   -54.602 1.00 34.04 ? 306 GLU A CD  1 
ATOM   2222 O  OE1 . GLU A 1 317 ? -19.177 0.093   -55.016 1.00 36.23 ? 306 GLU A OE1 1 
ATOM   2223 O  OE2 . GLU A 1 317 ? -18.275 2.093   -55.301 1.00 35.90 ? 306 GLU A OE2 1 
ATOM   2224 N  N   . ARG A 1 318 ? -22.526 0.338   -50.360 1.00 26.61 ? 307 ARG A N   1 
ATOM   2225 C  CA  . ARG A 1 318 ? -23.797 -0.227  -49.934 1.00 27.13 ? 307 ARG A CA  1 
ATOM   2226 C  C   . ARG A 1 318 ? -24.578 0.761   -49.077 1.00 30.95 ? 307 ARG A C   1 
ATOM   2227 O  O   . ARG A 1 318 ? -25.808 0.840   -49.179 1.00 32.77 ? 307 ARG A O   1 
ATOM   2228 C  CB  . ARG A 1 318 ? -23.571 -1.529  -49.179 1.00 21.49 ? 307 ARG A CB  1 
ATOM   2229 C  CG  . ARG A 1 318 ? -24.852 -2.126  -48.698 1.00 26.94 ? 307 ARG A CG  1 
ATOM   2230 C  CD  . ARG A 1 318 ? -25.750 -2.454  -49.865 1.00 26.20 ? 307 ARG A CD  1 
ATOM   2231 N  NE  . ARG A 1 318 ? -27.016 -3.049  -49.454 1.00 30.78 ? 307 ARG A NE  1 
ATOM   2232 C  CZ  . ARG A 1 318 ? -28.119 -2.355  -49.217 1.00 28.97 ? 307 ARG A CZ  1 
ATOM   2233 N  NH1 . ARG A 1 318 ? -28.131 -1.033  -49.298 1.00 35.51 ? 307 ARG A NH1 1 
ATOM   2234 N  NH2 . ARG A 1 318 ? -29.232 -2.998  -48.882 1.00 26.78 ? 307 ARG A NH2 1 
ATOM   2235 N  N   . ILE A 1 319 ? -23.891 1.520   -48.218 1.00 27.93 ? 308 ILE A N   1 
ATOM   2236 C  CA  . ILE A 1 319 ? -24.623 2.477   -47.406 1.00 28.01 ? 308 ILE A CA  1 
ATOM   2237 C  C   . ILE A 1 319 ? -25.244 3.527   -48.306 1.00 30.48 ? 308 ILE A C   1 
ATOM   2238 O  O   . ILE A 1 319 ? -26.406 3.911   -48.122 1.00 33.95 ? 308 ILE A O   1 
ATOM   2239 C  CB  . ILE A 1 319 ? -23.719 3.091   -46.319 1.00 30.54 ? 308 ILE A CB  1 
ATOM   2240 C  CG1 . ILE A 1 319 ? -23.561 2.093   -45.158 1.00 26.55 ? 308 ILE A CG1 1 
ATOM   2241 C  CG2 . ILE A 1 319 ? -24.307 4.442   -45.818 1.00 21.75 ? 308 ILE A CG2 1 
ATOM   2242 C  CD1 . ILE A 1 319 ? -22.359 2.322   -44.279 1.00 23.22 ? 308 ILE A CD1 1 
ATOM   2243 N  N   . ALA A 1 320 ? -24.500 3.960   -49.331 1.00 31.02 ? 309 ALA A N   1 
ATOM   2244 C  CA  . ALA A 1 320 ? -25.012 4.924   -50.297 1.00 30.82 ? 309 ALA A CA  1 
ATOM   2245 C  C   . ALA A 1 320 ? -26.203 4.378   -51.068 1.00 34.49 ? 309 ALA A C   1 
ATOM   2246 O  O   . ALA A 1 320 ? -27.035 5.165   -51.531 1.00 33.14 ? 309 ALA A O   1 
ATOM   2247 C  CB  . ALA A 1 320 ? -23.914 5.345   -51.276 1.00 27.35 ? 309 ALA A CB  1 
ATOM   2248 N  N   . ALA A 1 321 ? -26.319 3.049   -51.185 1.00 32.51 ? 310 ALA A N   1 
ATOM   2249 C  CA  . ALA A 1 321 ? -27.409 2.426   -51.932 1.00 29.61 ? 310 ALA A CA  1 
ATOM   2250 C  C   . ALA A 1 321 ? -28.768 2.628   -51.286 1.00 33.23 ? 310 ALA A C   1 
ATOM   2251 O  O   . ALA A 1 321 ? -29.780 2.243   -51.888 1.00 36.04 ? 310 ALA A O   1 
ATOM   2252 C  CB  . ALA A 1 321 ? -27.166 0.927   -52.088 1.00 22.84 ? 310 ALA A CB  1 
ATOM   2253 N  N   . MET A 1 322 ? -28.818 3.178   -50.072 1.00 30.37 ? 311 MET A N   1 
ATOM   2254 C  CA  . MET A 1 322 ? -30.097 3.405   -49.415 1.00 28.73 ? 311 MET A CA  1 
ATOM   2255 C  C   . MET A 1 322 ? -30.788 4.662   -49.909 1.00 27.25 ? 311 MET A C   1 
ATOM   2256 O  O   . MET A 1 322 ? -31.975 4.829   -49.640 1.00 28.99 ? 311 MET A O   1 
ATOM   2257 C  CB  . MET A 1 322 ? -29.920 3.494   -47.895 1.00 26.92 ? 311 MET A CB  1 
ATOM   2258 C  CG  . MET A 1 322 ? -29.515 2.197   -47.241 1.00 29.73 ? 311 MET A CG  1 
ATOM   2259 S  SD  . MET A 1 322 ? -29.580 2.283   -45.438 1.00 29.88 ? 311 MET A SD  1 
ATOM   2260 C  CE  . MET A 1 322 ? -27.911 2.862   -45.065 1.00 23.94 ? 311 MET A CE  1 
ATOM   2261 N  N   . GLY A 1 323 ? -30.067 5.561   -50.584 1.00 30.39 ? 312 GLY A N   1 
ATOM   2262 C  CA  . GLY A 1 323 ? -30.637 6.804   -51.084 1.00 18.44 ? 312 GLY A CA  1 
ATOM   2263 C  C   . GLY A 1 323 ? -31.116 7.788   -50.046 1.00 23.55 ? 312 GLY A C   1 
ATOM   2264 O  O   . GLY A 1 323 ? -31.963 8.621   -50.353 1.00 31.11 ? 312 GLY A O   1 
ATOM   2265 N  N   . LEU A 1 324 ? -30.601 7.732   -48.821 1.00 30.13 ? 313 LEU A N   1 
ATOM   2266 C  CA  . LEU A 1 324 ? -31.042 8.658   -47.780 1.00 27.94 ? 313 LEU A CA  1 
ATOM   2267 C  C   . LEU A 1 324 ? -29.929 9.642   -47.398 1.00 29.72 ? 313 LEU A C   1 
ATOM   2268 O  O   . LEU A 1 324 ? -28.740 9.355   -47.591 1.00 25.47 ? 313 LEU A O   1 
ATOM   2269 C  CB  . LEU A 1 324 ? -31.487 7.887   -46.530 1.00 28.23 ? 313 LEU A CB  1 
ATOM   2270 C  CG  . LEU A 1 324 ? -32.514 6.794   -46.814 1.00 30.74 ? 313 LEU A CG  1 
ATOM   2271 C  CD1 . LEU A 1 324 ? -32.361 5.620   -45.883 1.00 31.83 ? 313 LEU A CD1 1 
ATOM   2272 C  CD2 . LEU A 1 324 ? -33.878 7.395   -46.678 1.00 32.31 ? 313 LEU A CD2 1 
ATOM   2273 N  N   . PRO A 1 325 ? -30.277 10.818  -46.870 1.00 31.46 ? 314 PRO A N   1 
ATOM   2274 C  CA  . PRO A 1 325 ? -29.255 11.640  -46.212 1.00 30.59 ? 314 PRO A CA  1 
ATOM   2275 C  C   . PRO A 1 325 ? -28.569 10.828  -45.121 1.00 31.80 ? 314 PRO A C   1 
ATOM   2276 O  O   . PRO A 1 325 ? -29.214 10.089  -44.368 1.00 27.17 ? 314 PRO A O   1 
ATOM   2277 C  CB  . PRO A 1 325 ? -30.044 12.827  -45.647 1.00 29.04 ? 314 PRO A CB  1 
ATOM   2278 C  CG  . PRO A 1 325 ? -31.438 12.704  -46.203 1.00 23.76 ? 314 PRO A CG  1 
ATOM   2279 C  CD  . PRO A 1 325 ? -31.549 11.536  -47.070 1.00 22.73 ? 314 PRO A CD  1 
ATOM   2280 N  N   . THR A 1 326 ? -27.241 10.943  -45.057 1.00 32.64 ? 315 THR A N   1 
ATOM   2281 C  CA  . THR A 1 326 ? -26.435 10.033  -44.248 1.00 33.15 ? 315 THR A CA  1 
ATOM   2282 C  C   . THR A 1 326 ? -25.397 10.816  -43.457 1.00 31.11 ? 315 THR A C   1 
ATOM   2283 O  O   . THR A 1 326 ? -24.573 11.518  -44.044 1.00 35.62 ? 315 THR A O   1 
ATOM   2284 C  CB  . THR A 1 326 ? -25.768 8.973   -45.140 1.00 31.82 ? 315 THR A CB  1 
ATOM   2285 O  OG1 . THR A 1 326 ? -26.757 8.047   -45.623 1.00 25.48 ? 315 THR A OG1 1 
ATOM   2286 C  CG2 . THR A 1 326 ? -24.713 8.215   -44.376 1.00 32.16 ? 315 THR A CG2 1 
ATOM   2287 N  N   . LEU A 1 327 ? -25.441 10.698  -42.131 1.00 25.69 ? 316 LEU A N   1 
ATOM   2288 C  CA  . LEU A 1 327 ? -24.465 11.315  -41.244 1.00 26.50 ? 316 LEU A CA  1 
ATOM   2289 C  C   . LEU A 1 327 ? -23.536 10.229  -40.732 1.00 29.31 ? 316 LEU A C   1 
ATOM   2290 O  O   . LEU A 1 327 ? -24.001 9.252   -40.144 1.00 30.32 ? 316 LEU A O   1 
ATOM   2291 C  CB  . LEU A 1 327 ? -25.139 12.027  -40.068 1.00 25.47 ? 316 LEU A CB  1 
ATOM   2292 C  CG  . LEU A 1 327 ? -24.202 12.597  -38.983 1.00 28.71 ? 316 LEU A CG  1 
ATOM   2293 C  CD1 . LEU A 1 327 ? -23.236 13.663  -39.497 1.00 20.03 ? 316 LEU A CD1 1 
ATOM   2294 C  CD2 . LEU A 1 327 ? -25.001 13.117  -37.804 1.00 27.23 ? 316 LEU A CD2 1 
ATOM   2295 N  N   . PHE A 1 328 ? -22.233 10.400  -40.956 1.00 30.04 ? 317 PHE A N   1 
ATOM   2296 C  CA  . PHE A 1 328 ? -21.212 9.483   -40.460 1.00 27.66 ? 317 PHE A CA  1 
ATOM   2297 C  C   . PHE A 1 328 ? -20.610 10.050  -39.182 1.00 32.58 ? 317 PHE A C   1 
ATOM   2298 O  O   . PHE A 1 328 ? -20.142 11.197  -39.164 1.00 31.45 ? 317 PHE A O   1 
ATOM   2299 C  CB  . PHE A 1 328 ? -20.095 9.283   -41.485 1.00 30.07 ? 317 PHE A CB  1 
ATOM   2300 C  CG  . PHE A 1 328 ? -20.543 8.655   -42.781 1.00 35.55 ? 317 PHE A CG  1 
ATOM   2301 C  CD1 . PHE A 1 328 ? -20.576 7.265   -42.923 1.00 28.80 ? 317 PHE A CD1 1 
ATOM   2302 C  CD2 . PHE A 1 328 ? -20.901 9.448   -43.863 1.00 28.96 ? 317 PHE A CD2 1 
ATOM   2303 C  CE1 . PHE A 1 328 ? -20.964 6.680   -44.101 1.00 20.48 ? 317 PHE A CE1 1 
ATOM   2304 C  CE2 . PHE A 1 328 ? -21.304 8.861   -45.052 1.00 33.57 ? 317 PHE A CE2 1 
ATOM   2305 C  CZ  . PHE A 1 328 ? -21.326 7.469   -45.168 1.00 28.49 ? 317 PHE A CZ  1 
ATOM   2306 N  N   . VAL A 1 329 ? -20.585 9.240   -38.129 1.00 28.42 ? 318 VAL A N   1 
ATOM   2307 C  CA  . VAL A 1 329 ? -20.080 9.669   -36.829 1.00 30.44 ? 318 VAL A CA  1 
ATOM   2308 C  C   . VAL A 1 329 ? -18.960 8.724   -36.405 1.00 29.83 ? 318 VAL A C   1 
ATOM   2309 O  O   . VAL A 1 329 ? -19.197 7.529   -36.196 1.00 29.20 ? 318 VAL A O   1 
ATOM   2310 C  CB  . VAL A 1 329 ? -21.202 9.712   -35.776 1.00 28.89 ? 318 VAL A CB  1 
ATOM   2311 C  CG1 . VAL A 1 329 ? -20.693 10.337  -34.495 1.00 28.94 ? 318 VAL A CG1 1 
ATOM   2312 C  CG2 . VAL A 1 329 ? -22.414 10.504  -36.310 1.00 26.72 ? 318 VAL A CG2 1 
ATOM   2313 N  N   . MET A 1 330 ? -17.750 9.260   -36.246 1.00 28.45 ? 319 MET A N   1 
ATOM   2314 C  CA  . MET A 1 330 ? -16.620 8.417   -35.870 1.00 30.65 ? 319 MET A CA  1 
ATOM   2315 C  C   . MET A 1 330 ? -16.829 7.740   -34.514 1.00 32.39 ? 319 MET A C   1 
ATOM   2316 O  O   . MET A 1 330 ? -17.151 8.391   -33.513 1.00 32.06 ? 319 MET A O   1 
ATOM   2317 C  CB  . MET A 1 330 ? -15.330 9.233   -35.839 1.00 28.16 ? 319 MET A CB  1 
ATOM   2318 C  CG  . MET A 1 330 ? -14.071 8.345   -35.840 1.00 32.61 ? 319 MET A CG  1 
ATOM   2319 S  SD  . MET A 1 330 ? -13.781 7.615   -37.483 1.00 33.87 ? 319 MET A SD  1 
ATOM   2320 C  CE  . MET A 1 330 ? -12.912 6.094   -37.117 1.00 35.99 ? 319 MET A CE  1 
ATOM   2321 N  N   . GLU A 1 331 ? -16.630 6.423   -34.489 1.00 33.19 ? 320 GLU A N   1 
ATOM   2322 C  CA  . GLU A 1 331 ? -16.563 5.652   -33.255 1.00 31.34 ? 320 GLU A CA  1 
ATOM   2323 C  C   . GLU A 1 331 ? -15.153 5.091   -33.083 1.00 29.60 ? 320 GLU A C   1 
ATOM   2324 O  O   . GLU A 1 331 ? -14.185 5.850   -33.102 1.00 33.60 ? 320 GLU A O   1 
ATOM   2325 C  CB  . GLU A 1 331 ? -17.597 4.520   -33.249 1.00 25.51 ? 320 GLU A CB  1 
ATOM   2326 C  CG  . GLU A 1 331 ? -19.021 4.949   -33.473 1.00 29.59 ? 320 GLU A CG  1 
ATOM   2327 C  CD  . GLU A 1 331 ? -19.661 5.585   -32.240 1.00 36.19 ? 320 GLU A CD  1 
ATOM   2328 O  OE1 . GLU A 1 331 ? -19.011 5.571   -31.164 1.00 32.50 ? 320 GLU A OE1 1 
ATOM   2329 O  OE2 . GLU A 1 331 ? -20.820 6.085   -32.347 1.00 29.48 ? 320 GLU A OE2 1 
ATOM   2330 N  N   . GLY A 1 332 ? -15.027 3.757   -32.979 1.00 31.67 ? 321 GLY A N   1 
ATOM   2331 C  CA  . GLY A 1 332 ? -13.785 3.123   -32.587 1.00 30.59 ? 321 GLY A CA  1 
ATOM   2332 C  C   . GLY A 1 332 ? -12.779 2.885   -33.716 1.00 32.86 ? 321 GLY A C   1 
ATOM   2333 O  O   . GLY A 1 332 ? -13.030 3.051   -34.908 1.00 28.02 ? 321 GLY A O   1 
ATOM   2334 N  N   . GLY A 1 333 ? -11.588 2.469   -33.302 1.00 36.31 ? 322 GLY A N   1 
ATOM   2335 C  CA  . GLY A 1 333 ? -10.533 2.117   -34.227 1.00 37.42 ? 322 GLY A CA  1 
ATOM   2336 C  C   . GLY A 1 333 ? -9.179  2.472   -33.660 1.00 41.41 ? 322 GLY A C   1 
ATOM   2337 O  O   . GLY A 1 333 ? -8.929  3.639   -33.356 1.00 43.13 ? 322 GLY A O   1 
ATOM   2338 N  N   . TYR A 1 334 ? -8.308  1.479   -33.490 1.00 48.69 ? 323 TYR A N   1 
ATOM   2339 C  CA  . TYR A 1 334 ? -6.947  1.749   -33.040 1.00 50.19 ? 323 TYR A CA  1 
ATOM   2340 C  C   . TYR A 1 334 ? -6.194  2.558   -34.089 1.00 54.21 ? 323 TYR A C   1 
ATOM   2341 O  O   . TYR A 1 334 ? -6.353  2.346   -35.294 1.00 58.31 ? 323 TYR A O   1 
ATOM   2342 C  CB  . TYR A 1 334 ? -6.214  0.436   -32.745 1.00 54.74 ? 323 TYR A CB  1 
ATOM   2343 C  CG  . TYR A 1 334 ? -5.012  0.561   -31.812 1.00 65.56 ? 323 TYR A CG  1 
ATOM   2344 C  CD1 . TYR A 1 334 ? -3.843  1.198   -32.219 1.00 62.45 ? 323 TYR A CD1 1 
ATOM   2345 C  CD2 . TYR A 1 334 ? -5.061  0.063   -30.512 1.00 67.78 ? 323 TYR A CD2 1 
ATOM   2346 C  CE1 . TYR A 1 334 ? -2.752  1.320   -31.363 1.00 69.01 ? 323 TYR A CE1 1 
ATOM   2347 C  CE2 . TYR A 1 334 ? -3.975  0.180   -29.649 1.00 68.92 ? 323 TYR A CE2 1 
ATOM   2348 C  CZ  . TYR A 1 334 ? -2.824  0.809   -30.078 1.00 73.22 ? 323 TYR A CZ  1 
ATOM   2349 O  OH  . TYR A 1 334 ? -1.742  0.930   -29.228 1.00 82.03 ? 323 TYR A OH  1 
ATOM   2350 N  N   . ALA A 1 335 ? -5.360  3.489   -33.619 1.00 55.04 ? 324 ALA A N   1 
ATOM   2351 C  CA  . ALA A 1 335 ? -4.611  4.380   -34.498 1.00 58.26 ? 324 ALA A CA  1 
ATOM   2352 C  C   . ALA A 1 335 ? -3.555  3.625   -35.303 1.00 56.83 ? 324 ALA A C   1 
ATOM   2353 O  O   . ALA A 1 335 ? -2.371  3.977   -35.271 1.00 53.68 ? 324 ALA A O   1 
ATOM   2354 C  CB  . ALA A 1 335 ? -3.962  5.506   -33.686 1.00 57.39 ? 324 ALA A CB  1 
ATOM   2355 N  N   . VAL A 1 336 ? -3.975  2.590   -36.035 1.00 54.96 ? 325 VAL A N   1 
ATOM   2356 C  CA  . VAL A 1 336 ? -3.085  1.855   -36.926 1.00 50.70 ? 325 VAL A CA  1 
ATOM   2357 C  C   . VAL A 1 336 ? -2.701  2.783   -38.071 1.00 45.52 ? 325 VAL A C   1 
ATOM   2358 O  O   . VAL A 1 336 ? -3.267  3.875   -38.204 1.00 43.09 ? 325 VAL A O   1 
ATOM   2359 C  CB  . VAL A 1 336 ? -3.746  0.559   -37.431 1.00 44.14 ? 325 VAL A CB  1 
ATOM   2360 C  CG1 . VAL A 1 336 ? -4.117  -0.336  -36.266 1.00 43.20 ? 325 VAL A CG1 1 
ATOM   2361 C  CG2 . VAL A 1 336 ? -4.971  0.885   -38.257 1.00 44.79 ? 325 VAL A CG2 1 
ATOM   2362 N  N   . GLU A 1 337 ? -1.730  2.374   -38.896 1.00 41.23 ? 326 GLU A N   1 
ATOM   2363 C  CA  . GLU A 1 337 ? -1.330  3.239   -40.000 1.00 44.00 ? 326 GLU A CA  1 
ATOM   2364 C  C   . GLU A 1 337 ? -2.458  3.418   -41.006 1.00 48.16 ? 326 GLU A C   1 
ATOM   2365 O  O   . GLU A 1 337 ? -2.530  4.455   -41.674 1.00 42.77 ? 326 GLU A O   1 
ATOM   2366 C  CB  . GLU A 1 337 ? -0.087  2.701   -40.711 1.00 52.43 ? 326 GLU A CB  1 
ATOM   2367 C  CG  . GLU A 1 337 ? 0.936   1.980   -39.828 1.00 61.99 ? 326 GLU A CG  1 
ATOM   2368 C  CD  . GLU A 1 337 ? 2.099   1.406   -40.647 1.00 61.77 ? 326 GLU A CD  1 
ATOM   2369 O  OE1 . GLU A 1 337 ? 2.667   0.356   -40.240 1.00 54.87 ? 326 GLU A OE1 1 
ATOM   2370 O  OE2 . GLU A 1 337 ? 2.452   2.031   -41.689 1.00 58.99 ? 326 GLU A OE2 1 
ATOM   2371 N  N   . ALA A 1 338 ? -3.359  2.439   -41.110 1.00 50.29 ? 327 ALA A N   1 
ATOM   2372 C  CA  . ALA A 1 338 ? -4.393  2.435   -42.133 1.00 35.49 ? 327 ALA A CA  1 
ATOM   2373 C  C   . ALA A 1 338 ? -5.735  2.975   -41.649 1.00 36.66 ? 327 ALA A C   1 
ATOM   2374 O  O   . ALA A 1 338 ? -6.728  2.832   -42.364 1.00 37.41 ? 327 ALA A O   1 
ATOM   2375 C  CB  . ALA A 1 338 ? -4.571  1.021   -42.690 1.00 29.07 ? 327 ALA A CB  1 
ATOM   2376 N  N   . ILE A 1 339 ? -5.797  3.609   -40.473 1.00 36.29 ? 328 ILE A N   1 
ATOM   2377 C  CA  . ILE A 1 339 ? -7.093  4.073   -39.978 1.00 33.93 ? 328 ILE A CA  1 
ATOM   2378 C  C   . ILE A 1 339 ? -7.682  5.144   -40.900 1.00 32.09 ? 328 ILE A C   1 
ATOM   2379 O  O   . ILE A 1 339 ? -8.888  5.155   -41.159 1.00 35.27 ? 328 ILE A O   1 
ATOM   2380 C  CB  . ILE A 1 339 ? -6.984  4.554   -38.515 1.00 38.24 ? 328 ILE A CB  1 
ATOM   2381 C  CG1 . ILE A 1 339 ? -8.390  4.710   -37.911 1.00 35.30 ? 328 ILE A CG1 1 
ATOM   2382 C  CG2 . ILE A 1 339 ? -6.135  5.832   -38.391 1.00 36.41 ? 328 ILE A CG2 1 
ATOM   2383 C  CD1 . ILE A 1 339 ? -8.399  5.057   -36.438 1.00 38.82 ? 328 ILE A CD1 1 
ATOM   2384 N  N   . GLY A 1 340 ? -6.850  6.044   -41.426 1.00 31.74 ? 329 GLY A N   1 
ATOM   2385 C  CA  . GLY A 1 340 ? -7.351  7.004   -42.393 1.00 30.24 ? 329 GLY A CA  1 
ATOM   2386 C  C   . GLY A 1 340 ? -7.868  6.342   -43.660 1.00 31.22 ? 329 GLY A C   1 
ATOM   2387 O  O   . GLY A 1 340 ? -8.932  6.693   -44.170 1.00 33.79 ? 329 GLY A O   1 
ATOM   2388 N  N   . VAL A 1 341 ? -7.129  5.371   -44.180 1.00 28.95 ? 330 VAL A N   1 
ATOM   2389 C  CA  . VAL A 1 341 ? -7.559  4.678   -45.387 1.00 33.04 ? 330 VAL A CA  1 
ATOM   2390 C  C   . VAL A 1 341 ? -8.884  3.958   -45.144 1.00 31.16 ? 330 VAL A C   1 
ATOM   2391 O  O   . VAL A 1 341 ? -9.807  4.018   -45.965 1.00 32.39 ? 330 VAL A O   1 
ATOM   2392 C  CB  . VAL A 1 341 ? -6.454  3.708   -45.853 1.00 31.34 ? 330 VAL A CB  1 
ATOM   2393 C  CG1 . VAL A 1 341 ? -7.043  2.519   -46.629 1.00 22.61 ? 330 VAL A CG1 1 
ATOM   2394 C  CG2 . VAL A 1 341 ? -5.436  4.448   -46.679 1.00 28.07 ? 330 VAL A CG2 1 
ATOM   2395 N  N   . ASN A 1 342 ? -8.985  3.254   -44.015 1.00 28.28 ? 331 ASN A N   1 
ATOM   2396 C  CA  . ASN A 1 342 ? -10.175 2.474   -43.719 1.00 25.85 ? 331 ASN A CA  1 
ATOM   2397 C  C   . ASN A 1 342 ? -11.389 3.379   -43.552 1.00 29.89 ? 331 ASN A C   1 
ATOM   2398 O  O   . ASN A 1 342 ? -12.459 3.119   -44.118 1.00 33.10 ? 331 ASN A O   1 
ATOM   2399 C  CB  . ASN A 1 342 ? -9.952  1.637   -42.453 1.00 31.11 ? 331 ASN A CB  1 
ATOM   2400 C  CG  . ASN A 1 342 ? -8.925  0.502   -42.644 1.00 30.78 ? 331 ASN A CG  1 
ATOM   2401 O  OD1 . ASN A 1 342 ? -8.722  -0.010  -43.747 1.00 25.18 ? 331 ASN A OD1 1 
ATOM   2402 N  ND2 . ASN A 1 342 ? -8.290  0.102   -41.542 1.00 28.66 ? 331 ASN A ND2 1 
ATOM   2403 N  N   . ALA A 1 343 ? -11.245 4.453   -42.779 1.00 26.80 ? 332 ALA A N   1 
ATOM   2404 C  CA  . ALA A 1 343 ? -12.389 5.309   -42.503 1.00 27.71 ? 332 ALA A CA  1 
ATOM   2405 C  C   . ALA A 1 343 ? -12.812 6.092   -43.750 1.00 33.29 ? 332 ALA A C   1 
ATOM   2406 O  O   . ALA A 1 343 ? -14.008 6.169   -44.075 1.00 30.94 ? 332 ALA A O   1 
ATOM   2407 C  CB  . ALA A 1 343 ? -12.058 6.241   -41.341 1.00 25.62 ? 332 ALA A CB  1 
ATOM   2408 N  N   . VAL A 1 344 ? -11.843 6.668   -44.469 1.00 28.21 ? 333 VAL A N   1 
ATOM   2409 C  CA  . VAL A 1 344 ? -12.152 7.487   -45.637 1.00 31.10 ? 333 VAL A CA  1 
ATOM   2410 C  C   . VAL A 1 344 ? -12.584 6.633   -46.838 1.00 33.40 ? 333 VAL A C   1 
ATOM   2411 O  O   . VAL A 1 344 ? -13.226 7.148   -47.768 1.00 29.82 ? 333 VAL A O   1 
ATOM   2412 C  CB  . VAL A 1 344 ? -10.931 8.389   -45.936 1.00 38.04 ? 333 VAL A CB  1 
ATOM   2413 C  CG1 . VAL A 1 344 ? -11.142 9.274   -47.176 1.00 33.77 ? 333 VAL A CG1 1 
ATOM   2414 C  CG2 . VAL A 1 344 ? -10.601 9.256   -44.706 1.00 33.90 ? 333 VAL A CG2 1 
ATOM   2415 N  N   . ASN A 1 345 ? -12.275 5.331   -46.834 1.00 27.23 ? 334 ASN A N   1 
ATOM   2416 C  CA  . ASN A 1 345 ? -12.814 4.453   -47.862 1.00 26.70 ? 334 ASN A CA  1 
ATOM   2417 C  C   . ASN A 1 345 ? -14.330 4.364   -47.776 1.00 29.16 ? 334 ASN A C   1 
ATOM   2418 O  O   . ASN A 1 345 ? -15.014 4.306   -48.806 1.00 30.03 ? 334 ASN A O   1 
ATOM   2419 C  CB  . ASN A 1 345 ? -12.191 3.072   -47.757 1.00 27.44 ? 334 ASN A CB  1 
ATOM   2420 C  CG  . ASN A 1 345 ? -10.965 2.942   -48.621 1.00 30.08 ? 334 ASN A CG  1 
ATOM   2421 O  OD1 . ASN A 1 345 ? -10.607 3.875   -49.345 1.00 31.06 ? 334 ASN A OD1 1 
ATOM   2422 N  ND2 . ASN A 1 345 ? -10.308 1.793   -48.553 1.00 24.18 ? 334 ASN A ND2 1 
ATOM   2423 N  N   . VAL A 1 346 ? -14.880 4.368   -46.561 1.00 27.39 ? 335 VAL A N   1 
ATOM   2424 C  CA  . VAL A 1 346 ? -16.335 4.388   -46.421 1.00 28.81 ? 335 VAL A CA  1 
ATOM   2425 C  C   . VAL A 1 346 ? -16.909 5.657   -47.053 1.00 31.31 ? 335 VAL A C   1 
ATOM   2426 O  O   . VAL A 1 346 ? -17.831 5.602   -47.882 1.00 31.53 ? 335 VAL A O   1 
ATOM   2427 C  CB  . VAL A 1 346 ? -16.735 4.236   -44.941 1.00 26.36 ? 335 VAL A CB  1 
ATOM   2428 C  CG1 . VAL A 1 346 ? -18.239 4.239   -44.793 1.00 21.17 ? 335 VAL A CG1 1 
ATOM   2429 C  CG2 . VAL A 1 346 ? -16.181 2.936   -44.383 1.00 28.66 ? 335 VAL A CG2 1 
ATOM   2430 N  N   . LEU A 1 347 ? -16.350 6.818   -46.695 1.00 30.64 ? 336 LEU A N   1 
ATOM   2431 C  CA  . LEU A 1 347 ? -16.779 8.078   -47.296 1.00 29.50 ? 336 LEU A CA  1 
ATOM   2432 C  C   . LEU A 1 347 ? -16.519 8.091   -48.800 1.00 28.09 ? 336 LEU A C   1 
ATOM   2433 O  O   . LEU A 1 347 ? -17.379 8.508   -49.582 1.00 28.00 ? 336 LEU A O   1 
ATOM   2434 C  CB  . LEU A 1 347 ? -16.065 9.245   -46.610 1.00 32.47 ? 336 LEU A CB  1 
ATOM   2435 C  CG  . LEU A 1 347 ? -16.015 9.226   -45.079 1.00 30.13 ? 336 LEU A CG  1 
ATOM   2436 C  CD1 . LEU A 1 347 ? -15.373 10.489  -44.597 1.00 25.91 ? 336 LEU A CD1 1 
ATOM   2437 C  CD2 . LEU A 1 347 ? -17.399 9.073   -44.455 1.00 28.86 ? 336 LEU A CD2 1 
ATOM   2438 N  N   . GLU A 1 348 ? -15.334 7.645   -49.229 1.00 26.76 ? 337 GLU A N   1 
ATOM   2439 C  CA  . GLU A 1 348 ? -15.059 7.549   -50.661 1.00 30.09 ? 337 GLU A CA  1 
ATOM   2440 C  C   . GLU A 1 348 ? -16.130 6.734   -51.369 1.00 33.35 ? 337 GLU A C   1 
ATOM   2441 O  O   . GLU A 1 348 ? -16.809 7.228   -52.278 1.00 26.35 ? 337 GLU A O   1 
ATOM   2442 C  CB  . GLU A 1 348 ? -13.699 6.911   -50.901 1.00 28.72 ? 337 GLU A CB  1 
ATOM   2443 C  CG  . GLU A 1 348 ? -12.637 7.867   -51.352 1.00 38.37 ? 337 GLU A CG  1 
ATOM   2444 C  CD  . GLU A 1 348 ? -11.495 7.161   -52.047 1.00 40.38 ? 337 GLU A CD  1 
ATOM   2445 O  OE1 . GLU A 1 348 ? -11.674 6.860   -53.242 1.00 34.85 ? 337 GLU A OE1 1 
ATOM   2446 O  OE2 . GLU A 1 348 ? -10.441 6.892   -51.399 1.00 40.67 ? 337 GLU A OE2 1 
ATOM   2447 N  N   . GLY A 1 349 ? -16.286 5.467   -50.947 1.00 29.18 ? 338 GLY A N   1 
ATOM   2448 C  CA  . GLY A 1 349 ? -17.320 4.614   -51.508 1.00 25.78 ? 338 GLY A CA  1 
ATOM   2449 C  C   . GLY A 1 349 ? -18.695 5.252   -51.476 1.00 33.23 ? 338 GLY A C   1 
ATOM   2450 O  O   . GLY A 1 349 ? -19.460 5.145   -52.438 1.00 34.00 ? 338 GLY A O   1 
ATOM   2451 N  N   . PHE A 1 350 ? -19.025 5.941   -50.380 1.00 28.66 ? 339 PHE A N   1 
ATOM   2452 C  CA  . PHE A 1 350 ? -20.320 6.601   -50.316 1.00 25.58 ? 339 PHE A CA  1 
ATOM   2453 C  C   . PHE A 1 350 ? -20.468 7.603   -51.445 1.00 25.72 ? 339 PHE A C   1 
ATOM   2454 O  O   . PHE A 1 350 ? -21.497 7.635   -52.130 1.00 26.77 ? 339 PHE A O   1 
ATOM   2455 C  CB  . PHE A 1 350 ? -20.519 7.284   -48.963 1.00 28.76 ? 339 PHE A CB  1 
ATOM   2456 C  CG  . PHE A 1 350 ? -21.899 7.876   -48.784 1.00 28.77 ? 339 PHE A CG  1 
ATOM   2457 C  CD1 . PHE A 1 350 ? -22.207 9.128   -49.284 1.00 25.37 ? 339 PHE A CD1 1 
ATOM   2458 C  CD2 . PHE A 1 350 ? -22.896 7.164   -48.128 1.00 33.04 ? 339 PHE A CD2 1 
ATOM   2459 C  CE1 . PHE A 1 350 ? -23.473 9.661   -49.131 1.00 28.40 ? 339 PHE A CE1 1 
ATOM   2460 C  CE2 . PHE A 1 350 ? -24.166 7.698   -47.963 1.00 26.72 ? 339 PHE A CE2 1 
ATOM   2461 C  CZ  . PHE A 1 350 ? -24.455 8.947   -48.468 1.00 24.46 ? 339 PHE A CZ  1 
ATOM   2462 N  N   . GLU A 1 351 ? -19.450 8.443   -51.647 1.00 28.85 ? 340 GLU A N   1 
ATOM   2463 C  CA  . GLU A 1 351 ? -19.545 9.470   -52.676 1.00 26.77 ? 340 GLU A CA  1 
ATOM   2464 C  C   . GLU A 1 351 ? -19.385 8.879   -54.060 1.00 28.72 ? 340 GLU A C   1 
ATOM   2465 O  O   . GLU A 1 351 ? -19.753 9.525   -55.042 1.00 31.80 ? 340 GLU A O   1 
ATOM   2466 C  CB  . GLU A 1 351 ? -18.498 10.552  -52.459 1.00 28.51 ? 340 GLU A CB  1 
ATOM   2467 C  CG  . GLU A 1 351 ? -18.669 11.393  -51.220 1.00 30.65 ? 340 GLU A CG  1 
ATOM   2468 C  CD  . GLU A 1 351 ? -17.536 12.396  -51.080 1.00 40.60 ? 340 GLU A CD  1 
ATOM   2469 O  OE1 . GLU A 1 351 ? -16.469 12.158  -51.680 1.00 39.62 ? 340 GLU A OE1 1 
ATOM   2470 O  OE2 . GLU A 1 351 ? -17.698 13.424  -50.391 1.00 44.17 ? 340 GLU A OE2 1 
ATOM   2471 N  N   . ASN A 1 352 ? -18.855 7.656   -54.150 1.00 30.62 ? 341 ASN A N   1 
ATOM   2472 C  CA  . ASN A 1 352 ? -18.746 6.957   -55.423 1.00 31.07 ? 341 ASN A CA  1 
ATOM   2473 C  C   . ASN A 1 352 ? -20.097 6.644   -56.039 1.00 33.03 ? 341 ASN A C   1 
ATOM   2474 O  O   . ASN A 1 352 ? -20.169 6.380   -57.244 1.00 33.99 ? 341 ASN A O   1 
ATOM   2475 C  CB  . ASN A 1 352 ? -18.005 5.638   -55.240 1.00 37.24 ? 341 ASN A CB  1 
ATOM   2476 C  CG  . ASN A 1 352 ? -16.570 5.728   -55.605 1.00 39.42 ? 341 ASN A CG  1 
ATOM   2477 O  OD1 . ASN A 1 352 ? -16.025 6.825   -55.730 1.00 40.00 ? 341 ASN A OD1 1 
ATOM   2478 N  ND2 . ASN A 1 352 ? -15.922 4.566   -55.758 1.00 37.83 ? 341 ASN A ND2 1 
ATOM   2479 N  N   . VAL A 1 353 ? -21.158 6.612   -55.246 1.00 30.72 ? 342 VAL A N   1 
ATOM   2480 C  CA  . VAL A 1 353 ? -22.411 6.128   -55.773 1.00 32.41 ? 342 VAL A CA  1 
ATOM   2481 C  C   . VAL A 1 353 ? -23.423 7.238   -55.818 1.00 28.82 ? 342 VAL A C   1 
ATOM   2482 O  O   . VAL A 1 353 ? -23.936 7.519   -56.896 1.00 39.06 ? 342 VAL A O   1 
ATOM   2483 C  CB  . VAL A 1 353 ? -22.919 4.927   -54.971 1.00 36.35 ? 342 VAL A CB  1 
ATOM   2484 C  CG1 . VAL A 1 353 ? -24.431 4.792   -55.097 1.00 31.65 ? 342 VAL A CG1 1 
ATOM   2485 C  CG2 . VAL A 1 353 ? -22.208 3.664   -55.458 1.00 36.96 ? 342 VAL A CG2 1 
ATOM   2486 N  N   . GLY B 1 10  ? -8.678  -21.248 28.901  1.00 55.68 ? -1  GLY B N   1 
ATOM   2487 C  CA  . GLY B 1 10  ? -9.473  -20.893 27.737  1.00 56.96 ? -1  GLY B CA  1 
ATOM   2488 C  C   . GLY B 1 10  ? -10.574 -21.879 27.379  1.00 60.33 ? -1  GLY B C   1 
ATOM   2489 O  O   . GLY B 1 10  ? -10.367 -23.088 27.419  1.00 56.45 ? -1  GLY B O   1 
ATOM   2490 N  N   . THR B 1 11  ? -11.744 -21.350 27.010  1.00 63.28 ? 0   THR B N   1 
ATOM   2491 C  CA  . THR B 1 11  ? -12.929 -22.138 26.700  1.00 50.23 ? 0   THR B CA  1 
ATOM   2492 C  C   . THR B 1 11  ? -13.334 -22.058 25.236  1.00 47.97 ? 0   THR B C   1 
ATOM   2493 O  O   . THR B 1 11  ? -14.287 -22.734 24.835  1.00 53.10 ? 0   THR B O   1 
ATOM   2494 C  CB  . THR B 1 11  ? -14.111 -21.676 27.569  1.00 60.63 ? 0   THR B CB  1 
ATOM   2495 O  OG1 . THR B 1 11  ? -13.730 -20.524 28.352  1.00 56.41 ? 0   THR B OG1 1 
ATOM   2496 C  CG2 . THR B 1 11  ? -14.586 -22.801 28.481  1.00 52.62 ? 0   THR B CG2 1 
ATOM   2497 N  N   . MET B 1 12  ? -12.658 -21.236 24.435  1.00 48.21 ? 1   MET B N   1 
ATOM   2498 C  CA  . MET B 1 12  ? -13.068 -20.945 23.061  1.00 53.55 ? 1   MET B CA  1 
ATOM   2499 C  C   . MET B 1 12  ? -11.980 -21.373 22.079  1.00 52.44 ? 1   MET B C   1 
ATOM   2500 O  O   . MET B 1 12  ? -10.866 -20.826 22.077  1.00 41.88 ? 1   MET B O   1 
ATOM   2501 C  CB  . MET B 1 12  ? -13.409 -19.461 22.911  1.00 49.60 ? 1   MET B CB  1 
ATOM   2502 C  CG  . MET B 1 12  ? -13.156 -18.837 21.558  1.00 42.90 ? 1   MET B CG  1 
ATOM   2503 S  SD  . MET B 1 12  ? -14.406 -17.610 21.161  1.00 37.43 ? 1   MET B SD  1 
ATOM   2504 C  CE  . MET B 1 12  ? -14.340 -16.546 22.593  1.00 35.01 ? 1   MET B CE  1 
ATOM   2505 N  N   . LEU B 1 13  ? -12.311 -22.356 21.254  1.00 45.81 ? 2   LEU B N   1 
ATOM   2506 C  CA  . LEU B 1 13  ? -11.365 -22.931 20.321  1.00 43.95 ? 2   LEU B CA  1 
ATOM   2507 C  C   . LEU B 1 13  ? -11.195 -22.017 19.106  1.00 44.34 ? 2   LEU B C   1 
ATOM   2508 O  O   . LEU B 1 13  ? -12.129 -21.324 18.688  1.00 39.41 ? 2   LEU B O   1 
ATOM   2509 C  CB  . LEU B 1 13  ? -11.868 -24.309 19.904  1.00 48.32 ? 2   LEU B CB  1 
ATOM   2510 C  CG  . LEU B 1 13  ? -10.897 -25.377 19.418  1.00 55.34 ? 2   LEU B CG  1 
ATOM   2511 C  CD1 . LEU B 1 13  ? -11.370 -26.746 19.887  1.00 52.47 ? 2   LEU B CD1 1 
ATOM   2512 C  CD2 . LEU B 1 13  ? -10.820 -25.318 17.925  1.00 54.31 ? 2   LEU B CD2 1 
ATOM   2513 N  N   . THR B 1 14  ? -9.987  -22.010 18.542  1.00 42.07 ? 3   THR B N   1 
ATOM   2514 C  CA  . THR B 1 14  ? -9.669  -21.260 17.329  1.00 38.18 ? 3   THR B CA  1 
ATOM   2515 C  C   . THR B 1 14  ? -9.303  -22.236 16.212  1.00 43.31 ? 3   THR B C   1 
ATOM   2516 O  O   . THR B 1 14  ? -8.496  -23.151 16.419  1.00 45.83 ? 3   THR B O   1 
ATOM   2517 C  CB  . THR B 1 14  ? -8.514  -20.278 17.585  1.00 37.80 ? 3   THR B CB  1 
ATOM   2518 O  OG1 . THR B 1 14  ? -8.991  -19.156 18.342  1.00 35.59 ? 3   THR B OG1 1 
ATOM   2519 C  CG2 . THR B 1 14  ? -7.882  -19.793 16.282  1.00 29.96 ? 3   THR B CG2 1 
ATOM   2520 N  N   . ILE B 1 15  ? -9.898  -22.063 15.035  1.00 34.62 ? 4   ILE B N   1 
ATOM   2521 C  CA  . ILE B 1 15  ? -9.535  -22.854 13.864  1.00 38.74 ? 4   ILE B CA  1 
ATOM   2522 C  C   . ILE B 1 15  ? -8.742  -21.963 12.926  1.00 44.19 ? 4   ILE B C   1 
ATOM   2523 O  O   . ILE B 1 15  ? -9.164  -20.838 12.633  1.00 46.02 ? 4   ILE B O   1 
ATOM   2524 C  CB  . ILE B 1 15  ? -10.769 -23.436 13.162  1.00 38.24 ? 4   ILE B CB  1 
ATOM   2525 C  CG1 . ILE B 1 15  ? -11.526 -24.331 14.142  1.00 44.91 ? 4   ILE B CG1 1 
ATOM   2526 C  CG2 . ILE B 1 15  ? -10.356 -24.213 11.924  1.00 32.22 ? 4   ILE B CG2 1 
ATOM   2527 C  CD1 . ILE B 1 15  ? -10.748 -25.557 14.544  1.00 42.21 ? 4   ILE B CD1 1 
ATOM   2528 N  N   . TYR B 1 16  ? -7.597  -22.457 12.457  1.00 43.34 ? 5   TYR B N   1 
ATOM   2529 C  CA  . TYR B 1 16  ? -6.723  -21.652 11.620  1.00 45.09 ? 5   TYR B CA  1 
ATOM   2530 C  C   . TYR B 1 16  ? -6.038  -22.550 10.594  1.00 46.61 ? 5   TYR B C   1 
ATOM   2531 O  O   . TYR B 1 16  ? -5.696  -23.701 10.880  1.00 43.10 ? 5   TYR B O   1 
ATOM   2532 C  CB  . TYR B 1 16  ? -5.690  -20.908 12.478  1.00 41.58 ? 5   TYR B CB  1 
ATOM   2533 C  CG  . TYR B 1 16  ? -4.520  -20.375 11.687  1.00 54.24 ? 5   TYR B CG  1 
ATOM   2534 C  CD1 . TYR B 1 16  ? -4.703  -19.389 10.710  1.00 57.61 ? 5   TYR B CD1 1 
ATOM   2535 C  CD2 . TYR B 1 16  ? -3.237  -20.873 11.884  1.00 49.01 ? 5   TYR B CD2 1 
ATOM   2536 C  CE1 . TYR B 1 16  ? -3.630  -18.898 9.973   1.00 54.55 ? 5   TYR B CE1 1 
ATOM   2537 C  CE2 . TYR B 1 16  ? -2.161  -20.387 11.150  1.00 52.54 ? 5   TYR B CE2 1 
ATOM   2538 C  CZ  . TYR B 1 16  ? -2.367  -19.402 10.195  1.00 58.23 ? 5   TYR B CZ  1 
ATOM   2539 O  OH  . TYR B 1 16  ? -1.308  -18.917 9.455   1.00 73.31 ? 5   TYR B OH  1 
ATOM   2540 N  N   . SER B 1 17  ? -5.809  -22.004 9.402   1.00 56.90 ? 6   SER B N   1 
ATOM   2541 C  CA  . SER B 1 17  ? -5.172  -22.775 8.338   1.00 58.13 ? 6   SER B CA  1 
ATOM   2542 C  C   . SER B 1 17  ? -3.656  -22.601 8.256   1.00 62.57 ? 6   SER B C   1 
ATOM   2543 O  O   . SER B 1 17  ? -2.918  -23.155 9.080   1.00 71.76 ? 6   SER B O   1 
ATOM   2544 C  CB  . SER B 1 17  ? -5.794  -22.414 6.993   1.00 61.52 ? 6   SER B CB  1 
ATOM   2545 O  OG  . SER B 1 17  ? -6.027  -23.588 6.244   1.00 50.44 ? 6   SER B OG  1 
ATOM   2546 N  N   . ASP B 1 18  ? -3.175  -21.875 7.246   1.00 64.56 ? 7   ASP B N   1 
ATOM   2547 C  CA  . ASP B 1 18  ? -1.740  -21.873 6.925   1.00 70.09 ? 7   ASP B CA  1 
ATOM   2548 C  C   . ASP B 1 18  ? -1.273  -20.492 6.487   1.00 74.82 ? 7   ASP B C   1 
ATOM   2549 O  O   . ASP B 1 18  ? -0.079  -20.259 6.297   1.00 82.05 ? 7   ASP B O   1 
ATOM   2550 C  CB  . ASP B 1 18  ? -1.411  -22.918 5.828   1.00 71.23 ? 7   ASP B CB  1 
ATOM   2551 C  CG  . ASP B 1 18  ? -1.723  -22.425 4.393   1.00 80.40 ? 7   ASP B CG  1 
ATOM   2552 O  OD1 . ASP B 1 18  ? -0.862  -21.738 3.799   1.00 89.32 ? 7   ASP B OD1 1 
ATOM   2553 O  OD2 . ASP B 1 18  ? -2.800  -22.750 3.837   1.00 68.06 ? 7   ASP B OD2 1 
ATOM   2554 N  N   . LYS B 1 42  ? -0.430  -12.597 7.476   1.00 72.16 ? 31  LYS B N   1 
ATOM   2555 C  CA  . LYS B 1 42  ? 0.398   -11.728 8.325   1.00 88.23 ? 31  LYS B CA  1 
ATOM   2556 C  C   . LYS B 1 42  ? -0.389  -11.128 9.503   1.00 78.46 ? 31  LYS B C   1 
ATOM   2557 O  O   . LYS B 1 42  ? 0.179   -10.870 10.586  1.00 62.64 ? 31  LYS B O   1 
ATOM   2558 C  CB  . LYS B 1 42  ? 1.028   -10.589 7.501   1.00 83.61 ? 31  LYS B CB  1 
ATOM   2559 C  CG  . LYS B 1 42  ? 2.530   -10.726 7.263   1.00 77.77 ? 31  LYS B CG  1 
ATOM   2560 C  CD  . LYS B 1 42  ? 3.282   -11.024 8.555   1.00 72.76 ? 31  LYS B CD  1 
ATOM   2561 C  CE  . LYS B 1 42  ? 3.021   -9.988  9.636   1.00 74.58 ? 31  LYS B CE  1 
ATOM   2562 N  NZ  . LYS B 1 42  ? 3.888   -10.241 10.811  1.00 74.16 ? 31  LYS B NZ  1 
ATOM   2563 N  N   . ARG B 1 43  ? -1.686  -10.878 9.268   1.00 69.58 ? 32  ARG B N   1 
ATOM   2564 C  CA  . ARG B 1 43  ? -2.591  -10.559 10.369  1.00 64.68 ? 32  ARG B CA  1 
ATOM   2565 C  C   . ARG B 1 43  ? -2.747  -11.753 11.300  1.00 62.09 ? 32  ARG B C   1 
ATOM   2566 O  O   . ARG B 1 43  ? -2.832  -11.590 12.525  1.00 59.55 ? 32  ARG B O   1 
ATOM   2567 C  CB  . ARG B 1 43  ? -3.974  -10.144 9.849   1.00 65.58 ? 32  ARG B CB  1 
ATOM   2568 C  CG  . ARG B 1 43  ? -4.024  -9.418  8.505   1.00 71.93 ? 32  ARG B CG  1 
ATOM   2569 C  CD  . ARG B 1 43  ? -5.477  -9.076  8.138   1.00 61.72 ? 32  ARG B CD  1 
ATOM   2570 N  NE  . ARG B 1 43  ? -6.353  -10.210 8.420   1.00 75.33 ? 32  ARG B NE  1 
ATOM   2571 C  CZ  . ARG B 1 43  ? -7.681  -10.202 8.356   1.00 64.38 ? 32  ARG B CZ  1 
ATOM   2572 N  NH1 . ARG B 1 43  ? -8.359  -9.114  8.003   1.00 45.01 ? 32  ARG B NH1 1 
ATOM   2573 N  NH2 . ARG B 1 43  ? -8.347  -11.318 8.653   1.00 53.62 ? 32  ARG B NH2 1 
ATOM   2574 N  N   . ALA B 1 44  ? -2.806  -12.962 10.732  1.00 57.89 ? 33  ALA B N   1 
ATOM   2575 C  CA  . ALA B 1 44  ? -2.995  -14.149 11.554  1.00 51.61 ? 33  ALA B CA  1 
ATOM   2576 C  C   . ALA B 1 44  ? -1.924  -14.238 12.625  1.00 52.67 ? 33  ALA B C   1 
ATOM   2577 O  O   . ALA B 1 44  ? -2.212  -14.618 13.762  1.00 59.16 ? 33  ALA B O   1 
ATOM   2578 C  CB  . ALA B 1 44  ? -3.000  -15.408 10.684  1.00 56.28 ? 33  ALA B CB  1 
ATOM   2579 N  N   . ASP B 1 45  ? -0.688  -13.862 12.287  1.00 58.17 ? 34  ASP B N   1 
ATOM   2580 C  CA  . ASP B 1 45  ? 0.394   -13.834 13.266  1.00 54.08 ? 34  ASP B CA  1 
ATOM   2581 C  C   . ASP B 1 45  ? 0.008   -13.035 14.504  1.00 53.51 ? 34  ASP B C   1 
ATOM   2582 O  O   . ASP B 1 45  ? 0.061   -13.542 15.634  1.00 47.40 ? 34  ASP B O   1 
ATOM   2583 C  CB  . ASP B 1 45  ? 1.652   -13.250 12.627  1.00 70.94 ? 34  ASP B CB  1 
ATOM   2584 C  CG  . ASP B 1 45  ? 2.827   -14.200 12.692  1.00 75.00 ? 34  ASP B CG  1 
ATOM   2585 O  OD1 . ASP B 1 45  ? 2.601   -15.422 12.555  1.00 59.76 ? 34  ASP B OD1 1 
ATOM   2586 O  OD2 . ASP B 1 45  ? 3.973   -13.718 12.877  1.00 82.02 ? 34  ASP B OD2 1 
ATOM   2587 N  N   . HIS B 1 46  ? -0.389  -11.776 14.309  1.00 43.88 ? 35  HIS B N   1 
ATOM   2588 C  CA  . HIS B 1 46  ? -0.752  -10.961 15.457  1.00 42.97 ? 35  HIS B CA  1 
ATOM   2589 C  C   . HIS B 1 46  ? -1.955  -11.535 16.185  1.00 44.16 ? 35  HIS B C   1 
ATOM   2590 O  O   . HIS B 1 46  ? -2.006  -11.512 17.420  1.00 43.54 ? 35  HIS B O   1 
ATOM   2591 C  CB  . HIS B 1 46  ? -1.011  -9.527  15.023  1.00 42.32 ? 35  HIS B CB  1 
ATOM   2592 C  CG  . HIS B 1 46  ? 0.240   -8.786  14.690  1.00 52.64 ? 35  HIS B CG  1 
ATOM   2593 N  ND1 . HIS B 1 46  ? 1.480   -9.209  15.118  1.00 56.81 ? 35  HIS B ND1 1 
ATOM   2594 C  CD2 . HIS B 1 46  ? 0.451   -7.656  13.977  1.00 51.02 ? 35  HIS B CD2 1 
ATOM   2595 C  CE1 . HIS B 1 46  ? 2.403   -8.370  14.685  1.00 50.97 ? 35  HIS B CE1 1 
ATOM   2596 N  NE2 . HIS B 1 46  ? 1.804   -7.419  13.992  1.00 54.38 ? 35  HIS B NE2 1 
ATOM   2597 N  N   . ILE B 1 47  ? -2.920  -12.078 15.441  1.00 41.12 ? 36  ILE B N   1 
ATOM   2598 C  CA  . ILE B 1 47  ? -4.159  -12.532 16.065  1.00 44.64 ? 36  ILE B CA  1 
ATOM   2599 C  C   . ILE B 1 47  ? -3.920  -13.809 16.864  1.00 44.27 ? 36  ILE B C   1 
ATOM   2600 O  O   . ILE B 1 47  ? -4.355  -13.927 18.016  1.00 42.93 ? 36  ILE B O   1 
ATOM   2601 C  CB  . ILE B 1 47  ? -5.267  -12.714 15.009  1.00 44.12 ? 36  ILE B CB  1 
ATOM   2602 C  CG1 . ILE B 1 47  ? -5.717  -11.354 14.471  1.00 40.96 ? 36  ILE B CG1 1 
ATOM   2603 C  CG2 . ILE B 1 47  ? -6.458  -13.459 15.599  1.00 34.28 ? 36  ILE B CG2 1 
ATOM   2604 C  CD1 . ILE B 1 47  ? -6.643  -11.443 13.270  1.00 36.83 ? 36  ILE B CD1 1 
ATOM   2605 N  N   . LEU B 1 48  ? -3.227  -14.786 16.268  1.00 45.14 ? 37  LEU B N   1 
ATOM   2606 C  CA  . LEU B 1 48  ? -2.926  -16.024 16.984  1.00 39.10 ? 37  LEU B CA  1 
ATOM   2607 C  C   . LEU B 1 48  ? -2.044  -15.757 18.187  1.00 39.98 ? 37  LEU B C   1 
ATOM   2608 O  O   . LEU B 1 48  ? -2.239  -16.350 19.256  1.00 33.08 ? 37  LEU B O   1 
ATOM   2609 C  CB  . LEU B 1 48  ? -2.249  -17.021 16.054  1.00 32.74 ? 37  LEU B CB  1 
ATOM   2610 C  CG  . LEU B 1 48  ? -3.150  -17.464 14.918  1.00 36.26 ? 37  LEU B CG  1 
ATOM   2611 C  CD1 . LEU B 1 48  ? -2.314  -17.944 13.756  1.00 34.16 ? 37  LEU B CD1 1 
ATOM   2612 C  CD2 . LEU B 1 48  ? -4.092  -18.539 15.424  1.00 35.27 ? 37  LEU B CD2 1 
ATOM   2613 N  N   . GLN B 1 49  ? -1.061  -14.865 18.026  1.00 49.36 ? 38  GLN B N   1 
ATOM   2614 C  CA  . GLN B 1 49  ? -0.185  -14.527 19.137  1.00 43.96 ? 38  GLN B CA  1 
ATOM   2615 C  C   . GLN B 1 49  ? -0.989  -13.970 20.299  1.00 45.51 ? 38  GLN B C   1 
ATOM   2616 O  O   . GLN B 1 49  ? -0.789  -14.375 21.450  1.00 46.40 ? 38  GLN B O   1 
ATOM   2617 C  CB  . GLN B 1 49  ? 0.882   -13.532 18.686  1.00 44.71 ? 38  GLN B CB  1 
ATOM   2618 C  CG  . GLN B 1 49  ? 1.758   -13.051 19.826  1.00 53.10 ? 38  GLN B CG  1 
ATOM   2619 C  CD  . GLN B 1 49  ? 2.577   -14.199 20.428  1.00 61.22 ? 38  GLN B CD  1 
ATOM   2620 O  OE1 . GLN B 1 49  ? 2.594   -14.394 21.639  1.00 55.74 ? 38  GLN B OE1 1 
ATOM   2621 N  NE2 . GLN B 1 49  ? 3.214   -14.992 19.571  1.00 65.90 ? 38  GLN B NE2 1 
ATOM   2622 N  N   . ARG B 1 50  ? -1.948  -13.085 20.006  1.00 35.40 ? 39  ARG B N   1 
ATOM   2623 C  CA  . ARG B 1 50  ? -2.811  -12.550 21.053  1.00 39.60 ? 39  ARG B CA  1 
ATOM   2624 C  C   . ARG B 1 50  ? -3.808  -13.591 21.568  1.00 40.86 ? 39  ARG B C   1 
ATOM   2625 O  O   . ARG B 1 50  ? -4.212  -13.529 22.732  1.00 41.36 ? 39  ARG B O   1 
ATOM   2626 C  CB  . ARG B 1 50  ? -3.535  -11.302 20.541  1.00 43.29 ? 39  ARG B CB  1 
ATOM   2627 C  CG  . ARG B 1 50  ? -4.291  -10.532 21.607  1.00 40.76 ? 39  ARG B CG  1 
ATOM   2628 C  CD  . ARG B 1 50  ? -3.426  -9.484  22.262  1.00 37.82 ? 39  ARG B CD  1 
ATOM   2629 N  NE  . ARG B 1 50  ? -4.119  -8.845  23.371  1.00 44.05 ? 39  ARG B NE  1 
ATOM   2630 C  CZ  . ARG B 1 50  ? -3.535  -8.075  24.279  1.00 43.13 ? 39  ARG B CZ  1 
ATOM   2631 N  NH1 . ARG B 1 50  ? -2.236  -7.828  24.239  1.00 35.90 ? 39  ARG B NH1 1 
ATOM   2632 N  NH2 . ARG B 1 50  ? -4.273  -7.539  25.251  1.00 42.44 ? 39  ARG B NH2 1 
ATOM   2633 N  N   . VAL B 1 51  ? -4.208  -14.556 20.732  1.00 46.44 ? 40  VAL B N   1 
ATOM   2634 C  CA  . VAL B 1 51  ? -5.063  -15.653 21.192  1.00 39.32 ? 40  VAL B CA  1 
ATOM   2635 C  C   . VAL B 1 51  ? -4.302  -16.563 22.155  1.00 43.35 ? 40  VAL B C   1 
ATOM   2636 O  O   . VAL B 1 51  ? -4.848  -17.002 23.176  1.00 46.80 ? 40  VAL B O   1 
ATOM   2637 C  CB  . VAL B 1 51  ? -5.618  -16.425 19.980  1.00 36.47 ? 40  VAL B CB  1 
ATOM   2638 C  CG1 . VAL B 1 51  ? -5.933  -17.874 20.329  1.00 41.51 ? 40  VAL B CG1 1 
ATOM   2639 C  CG2 . VAL B 1 51  ? -6.850  -15.738 19.454  1.00 40.51 ? 40  VAL B CG2 1 
ATOM   2640 N  N   . LYS B 1 52  ? -3.030  -16.857 21.850  1.00 43.54 ? 41  LYS B N   1 
ATOM   2641 C  CA  . LYS B 1 52  ? -2.167  -17.577 22.791  1.00 45.57 ? 41  LYS B CA  1 
ATOM   2642 C  C   . LYS B 1 52  ? -1.990  -16.801 24.092  1.00 46.27 ? 41  LYS B C   1 
ATOM   2643 O  O   . LYS B 1 52  ? -2.225  -17.339 25.179  1.00 42.83 ? 41  LYS B O   1 
ATOM   2644 C  CB  . LYS B 1 52  ? -0.802  -17.850 22.152  1.00 41.61 ? 41  LYS B CB  1 
ATOM   2645 C  CG  . LYS B 1 52  ? -0.770  -19.036 21.195  1.00 43.50 ? 41  LYS B CG  1 
ATOM   2646 C  CD  . LYS B 1 52  ? 0.467   -19.007 20.313  1.00 45.73 ? 41  LYS B CD  1 
ATOM   2647 C  CE  . LYS B 1 52  ? 0.240   -19.687 18.970  1.00 41.78 ? 41  LYS B CE  1 
ATOM   2648 N  NZ  . LYS B 1 52  ? 1.487   -19.669 18.136  1.00 53.53 ? 41  LYS B NZ  1 
ATOM   2649 N  N   . ASP B 1 53  ? -1.584  -15.523 23.991  1.00 47.95 ? 42  ASP B N   1 
ATOM   2650 C  CA  . ASP B 1 53  ? -1.240  -14.716 25.167  1.00 46.87 ? 42  ASP B CA  1 
ATOM   2651 C  C   . ASP B 1 53  ? -2.424  -14.524 26.098  1.00 48.34 ? 42  ASP B C   1 
ATOM   2652 O  O   . ASP B 1 53  ? -2.271  -14.565 27.324  1.00 54.47 ? 42  ASP B O   1 
ATOM   2653 C  CB  . ASP B 1 53  ? -0.710  -13.349 24.743  1.00 40.78 ? 42  ASP B CB  1 
ATOM   2654 C  CG  . ASP B 1 53  ? 0.493   -13.457 23.842  1.00 58.14 ? 42  ASP B CG  1 
ATOM   2655 O  OD1 . ASP B 1 53  ? 0.881   -14.605 23.540  1.00 61.79 ? 42  ASP B OD1 1 
ATOM   2656 O  OD2 . ASP B 1 53  ? 1.037   -12.415 23.417  1.00 66.29 ? 42  ASP B OD2 1 
ATOM   2657 N  N   . ARG B 1 54  ? -3.598  -14.264 25.549  1.00 45.37 ? 43  ARG B N   1 
ATOM   2658 C  CA  . ARG B 1 54  ? -4.738  -14.038 26.418  1.00 48.26 ? 43  ARG B CA  1 
ATOM   2659 C  C   . ARG B 1 54  ? -5.410  -15.329 26.843  1.00 52.93 ? 43  ARG B C   1 
ATOM   2660 O  O   . ARG B 1 54  ? -6.429  -15.265 27.536  1.00 61.05 ? 43  ARG B O   1 
ATOM   2661 C  CB  . ARG B 1 54  ? -5.746  -13.118 25.741  1.00 44.17 ? 43  ARG B CB  1 
ATOM   2662 C  CG  . ARG B 1 54  ? -5.088  -11.905 25.113  1.00 53.51 ? 43  ARG B CG  1 
ATOM   2663 C  CD  . ARG B 1 54  ? -4.229  -11.172 26.105  1.00 47.18 ? 43  ARG B CD  1 
ATOM   2664 N  NE  . ARG B 1 54  ? -5.036  -10.777 27.249  1.00 52.55 ? 43  ARG B NE  1 
ATOM   2665 C  CZ  . ARG B 1 54  ? -4.590  -10.087 28.290  1.00 57.93 ? 43  ARG B CZ  1 
ATOM   2666 N  NH1 . ARG B 1 54  ? -3.322  -9.699  28.378  1.00 48.91 ? 43  ARG B NH1 1 
ATOM   2667 N  NH2 . ARG B 1 54  ? -5.438  -9.782  29.270  1.00 45.25 ? 43  ARG B NH2 1 
ATOM   2668 N  N   . ASN B 1 55  ? -4.868  -16.486 26.453  1.00 51.63 ? 44  ASN B N   1 
ATOM   2669 C  CA  . ASN B 1 55  ? -5.380  -17.783 26.897  1.00 54.98 ? 44  ASN B CA  1 
ATOM   2670 C  C   . ASN B 1 55  ? -6.820  -17.988 26.428  1.00 45.02 ? 44  ASN B C   1 
ATOM   2671 O  O   . ASN B 1 55  ? -7.700  -18.390 27.188  1.00 50.15 ? 44  ASN B O   1 
ATOM   2672 C  CB  . ASN B 1 55  ? -5.249  -17.910 28.424  1.00 62.14 ? 44  ASN B CB  1 
ATOM   2673 C  CG  . ASN B 1 55  ? -5.725  -19.266 28.971  1.00 72.90 ? 44  ASN B CG  1 
ATOM   2674 O  OD1 . ASN B 1 55  ? -6.052  -20.196 28.220  1.00 65.87 ? 44  ASN B OD1 1 
ATOM   2675 N  ND2 . ASN B 1 55  ? -5.754  -19.375 30.299  1.00 76.16 ? 44  ASN B ND2 1 
ATOM   2676 N  N   . ILE B 1 56  ? -7.068  -17.687 25.157  1.00 42.40 ? 45  ILE B N   1 
ATOM   2677 C  CA  . ILE B 1 56  ? -8.444  -17.735 24.679  1.00 42.67 ? 45  ILE B CA  1 
ATOM   2678 C  C   . ILE B 1 56  ? -8.907  -19.179 24.559  1.00 48.39 ? 45  ILE B C   1 
ATOM   2679 O  O   . ILE B 1 56  ? -10.050 -19.513 24.897  1.00 43.93 ? 45  ILE B O   1 
ATOM   2680 C  CB  . ILE B 1 56  ? -8.568  -16.966 23.353  1.00 44.82 ? 45  ILE B CB  1 
ATOM   2681 C  CG1 . ILE B 1 56  ? -8.294  -15.482 23.593  1.00 45.69 ? 45  ILE B CG1 1 
ATOM   2682 C  CG2 . ILE B 1 56  ? -9.955  -17.155 22.725  1.00 40.92 ? 45  ILE B CG2 1 
ATOM   2683 C  CD1 . ILE B 1 56  ? -9.264  -14.845 24.566  1.00 43.56 ? 45  ILE B CD1 1 
ATOM   2684 N  N   . GLY B 1 57  ? -8.020  -20.054 24.115  1.00 45.11 ? 46  GLY B N   1 
ATOM   2685 C  CA  . GLY B 1 57  ? -8.311  -21.469 24.043  1.00 40.94 ? 46  GLY B CA  1 
ATOM   2686 C  C   . GLY B 1 57  ? -7.349  -22.144 23.091  1.00 42.05 ? 46  GLY B C   1 
ATOM   2687 O  O   . GLY B 1 57  ? -6.419  -21.534 22.570  1.00 46.29 ? 46  GLY B O   1 
ATOM   2688 N  N   . GLU B 1 58  ? -7.605  -23.427 22.864  1.00 42.90 ? 47  GLU B N   1 
ATOM   2689 C  CA  . GLU B 1 58  ? -6.769  -24.195 21.957  1.00 43.27 ? 47  GLU B CA  1 
ATOM   2690 C  C   . GLU B 1 58  ? -6.826  -23.617 20.546  1.00 42.00 ? 47  GLU B C   1 
ATOM   2691 O  O   . GLU B 1 58  ? -7.715  -22.840 20.189  1.00 40.66 ? 47  GLU B O   1 
ATOM   2692 C  CB  . GLU B 1 58  ? -7.209  -25.661 21.927  1.00 52.49 ? 47  GLU B CB  1 
ATOM   2693 C  CG  . GLU B 1 58  ? -6.744  -26.609 23.075  1.00 69.97 ? 47  GLU B CG  1 
ATOM   2694 C  CD  . GLU B 1 58  ? -5.238  -26.585 23.437  1.00 82.42 ? 47  GLU B CD  1 
ATOM   2695 O  OE1 . GLU B 1 58  ? -4.816  -27.528 24.140  1.00 81.67 ? 47  GLU B OE1 1 
ATOM   2696 O  OE2 . GLU B 1 58  ? -4.468  -25.665 23.059  1.00 82.00 ? 47  GLU B OE2 1 
ATOM   2697 N  N   . ILE B 1 59  ? -5.858  -24.021 19.733  1.00 43.98 ? 48  ILE B N   1 
ATOM   2698 C  CA  . ILE B 1 59  ? -5.805  -23.661 18.322  1.00 43.76 ? 48  ILE B CA  1 
ATOM   2699 C  C   . ILE B 1 59  ? -5.636  -24.944 17.525  1.00 47.51 ? 48  ILE B C   1 
ATOM   2700 O  O   . ILE B 1 59  ? -4.717  -25.727 17.792  1.00 47.48 ? 48  ILE B O   1 
ATOM   2701 C  CB  . ILE B 1 59  ? -4.662  -22.682 18.009  1.00 32.09 ? 48  ILE B CB  1 
ATOM   2702 C  CG1 . ILE B 1 59  ? -4.791  -21.421 18.849  1.00 30.49 ? 48  ILE B CG1 1 
ATOM   2703 C  CG2 . ILE B 1 59  ? -4.685  -22.328 16.554  1.00 35.30 ? 48  ILE B CG2 1 
ATOM   2704 C  CD1 . ILE B 1 59  ? -3.716  -20.432 18.566  1.00 29.37 ? 48  ILE B CD1 1 
ATOM   2705 N  N   . ARG B 1 60  ? -6.510  -25.152 16.543  1.00 46.95 ? 49  ARG B N   1 
ATOM   2706 C  CA  . ARG B 1 60  ? -6.599  -26.439 15.877  1.00 49.24 ? 49  ARG B CA  1 
ATOM   2707 C  C   . ARG B 1 60  ? -6.697  -26.254 14.374  1.00 43.03 ? 49  ARG B C   1 
ATOM   2708 O  O   . ARG B 1 60  ? -7.326  -25.308 13.898  1.00 51.73 ? 49  ARG B O   1 
ATOM   2709 C  CB  . ARG B 1 60  ? -7.808  -27.219 16.406  1.00 45.00 ? 49  ARG B CB  1 
ATOM   2710 C  CG  . ARG B 1 60  ? -7.558  -27.700 17.794  1.00 46.46 ? 49  ARG B CG  1 
ATOM   2711 C  CD  . ARG B 1 60  ? -7.981  -29.122 18.028  1.00 61.83 ? 49  ARG B CD  1 
ATOM   2712 N  NE  . ARG B 1 60  ? -8.486  -29.280 19.387  1.00 66.33 ? 49  ARG B NE  1 
ATOM   2713 C  CZ  . ARG B 1 60  ? -7.779  -29.057 20.491  1.00 69.83 ? 49  ARG B CZ  1 
ATOM   2714 N  NH1 . ARG B 1 60  ? -6.492  -28.736 20.445  1.00 63.70 ? 49  ARG B NH1 1 
ATOM   2715 N  NH2 . ARG B 1 60  ? -8.376  -29.168 21.675  1.00 75.63 ? 49  ARG B NH2 1 
ATOM   2716 N  N   . GLU B 1 61  ? -6.068  -27.160 13.636  1.00 43.67 ? 50  GLU B N   1 
ATOM   2717 C  CA  . GLU B 1 61  ? -6.215  -27.167 12.191  1.00 45.03 ? 50  GLU B CA  1 
ATOM   2718 C  C   . GLU B 1 61  ? -7.652  -27.533 11.822  1.00 40.28 ? 50  GLU B C   1 
ATOM   2719 O  O   . GLU B 1 61  ? -8.350  -28.175 12.614  1.00 38.36 ? 50  GLU B O   1 
ATOM   2720 C  CB  . GLU B 1 61  ? -5.234  -28.154 11.563  1.00 44.20 ? 50  GLU B CB  1 
ATOM   2721 C  CG  . GLU B 1 61  ? -3.798  -27.992 12.074  1.00 58.75 ? 50  GLU B CG  1 
ATOM   2722 C  CD  . GLU B 1 61  ? -2.833  -27.420 11.030  1.00 68.36 ? 50  GLU B CD  1 
ATOM   2723 O  OE1 . GLU B 1 61  ? -3.207  -26.435 10.346  1.00 65.51 ? 50  GLU B OE1 1 
ATOM   2724 O  OE2 . GLU B 1 61  ? -1.693  -27.941 10.917  1.00 67.35 ? 50  GLU B OE2 1 
ATOM   2725 N  N   . PRO B 1 62  ? -8.135  -27.100 10.619  1.00 35.54 ? 51  PRO B N   1 
ATOM   2726 C  CA  . PRO B 1 62  ? -9.507  -27.438 10.188  1.00 38.36 ? 51  PRO B CA  1 
ATOM   2727 C  C   . PRO B 1 62  ? -9.703  -28.894 9.784   1.00 35.56 ? 51  PRO B C   1 
ATOM   2728 O  O   . PRO B 1 62  ? -8.737  -29.653 9.721   1.00 38.42 ? 51  PRO B O   1 
ATOM   2729 C  CB  . PRO B 1 62  ? -9.726  -26.517 8.974   1.00 32.30 ? 51  PRO B CB  1 
ATOM   2730 C  CG  . PRO B 1 62  ? -8.365  -26.215 8.481   1.00 27.90 ? 51  PRO B CG  1 
ATOM   2731 C  CD  . PRO B 1 62  ? -7.496  -26.148 9.697   1.00 31.46 ? 51  PRO B CD  1 
ATOM   2732 N  N   . GLN B 1 63  ? -10.936 -29.292 9.477   1.00 38.20 ? 52  GLN B N   1 
ATOM   2733 C  CA  . GLN B 1 63  ? -11.172 -30.506 8.708   1.00 41.47 ? 52  GLN B CA  1 
ATOM   2734 C  C   . GLN B 1 63  ? -11.896 -30.200 7.404   1.00 42.89 ? 52  GLN B C   1 
ATOM   2735 O  O   . GLN B 1 63  ? -12.467 -29.119 7.207   1.00 41.70 ? 52  GLN B O   1 
ATOM   2736 C  CB  . GLN B 1 63  ? -11.978 -31.553 9.478   1.00 46.14 ? 52  GLN B CB  1 
ATOM   2737 C  CG  . GLN B 1 63  ? -11.276 -32.060 10.709  1.00 55.96 ? 52  GLN B CG  1 
ATOM   2738 C  CD  . GLN B 1 63  ? -12.144 -31.977 11.932  1.00 60.26 ? 52  GLN B CD  1 
ATOM   2739 O  OE1 . GLN B 1 63  ? -13.379 -32.043 11.840  1.00 56.22 ? 52  GLN B OE1 1 
ATOM   2740 N  NE2 . GLN B 1 63  ? -11.511 -31.814 13.095  1.00 73.76 ? 52  GLN B NE2 1 
ATOM   2741 N  N   . ASP B 1 64  ? -11.858 -31.176 6.507   1.00 38.65 ? 53  ASP B N   1 
ATOM   2742 C  CA  . ASP B 1 64  ? -12.541 -31.072 5.229   1.00 37.53 ? 53  ASP B CA  1 
ATOM   2743 C  C   . ASP B 1 64  ? -13.926 -31.658 5.414   1.00 31.97 ? 53  ASP B C   1 
ATOM   2744 O  O   . ASP B 1 64  ? -14.073 -32.864 5.606   1.00 37.02 ? 53  ASP B O   1 
ATOM   2745 C  CB  . ASP B 1 64  ? -11.768 -31.797 4.130   1.00 40.72 ? 53  ASP B CB  1 
ATOM   2746 C  CG  . ASP B 1 64  ? -12.250 -31.426 2.733   1.00 47.13 ? 53  ASP B CG  1 
ATOM   2747 O  OD1 . ASP B 1 64  ? -13.331 -30.801 2.627   1.00 39.93 ? 53  ASP B OD1 1 
ATOM   2748 O  OD2 . ASP B 1 64  ? -11.556 -31.760 1.740   1.00 47.03 ? 53  ASP B OD2 1 
ATOM   2749 N  N   . PHE B 1 65  ? -14.938 -30.809 5.387   1.00 32.32 ? 54  PHE B N   1 
ATOM   2750 C  CA  . PHE B 1 65  ? -16.311 -31.283 5.414   1.00 34.86 ? 54  PHE B CA  1 
ATOM   2751 C  C   . PHE B 1 65  ? -16.909 -31.408 4.018   1.00 35.85 ? 54  PHE B C   1 
ATOM   2752 O  O   . PHE B 1 65  ? -18.102 -31.709 3.893   1.00 33.59 ? 54  PHE B O   1 
ATOM   2753 C  CB  . PHE B 1 65  ? -17.160 -30.370 6.299   1.00 30.19 ? 54  PHE B CB  1 
ATOM   2754 C  CG  . PHE B 1 65  ? -16.788 -30.443 7.754   1.00 37.86 ? 54  PHE B CG  1 
ATOM   2755 C  CD1 . PHE B 1 65  ? -15.749 -29.681 8.259   1.00 34.45 ? 54  PHE B CD1 1 
ATOM   2756 C  CD2 . PHE B 1 65  ? -17.455 -31.307 8.612   1.00 41.06 ? 54  PHE B CD2 1 
ATOM   2757 C  CE1 . PHE B 1 65  ? -15.393 -29.765 9.590   1.00 37.10 ? 54  PHE B CE1 1 
ATOM   2758 C  CE2 . PHE B 1 65  ? -17.111 -31.383 9.955   1.00 42.43 ? 54  PHE B CE2 1 
ATOM   2759 C  CZ  . PHE B 1 65  ? -16.075 -30.614 10.442  1.00 41.66 ? 54  PHE B CZ  1 
ATOM   2760 N  N   . GLY B 1 66  ? -16.096 -31.197 2.973   1.00 37.52 ? 55  GLY B N   1 
ATOM   2761 C  CA  . GLY B 1 66  ? -16.510 -31.357 1.594   1.00 29.84 ? 55  GLY B CA  1 
ATOM   2762 C  C   . GLY B 1 66  ? -17.165 -30.138 0.962   1.00 39.73 ? 55  GLY B C   1 
ATOM   2763 O  O   . GLY B 1 66  ? -17.362 -29.073 1.560   1.00 37.72 ? 55  GLY B O   1 
ATOM   2764 N  N   . ARG B 1 67  ? -17.550 -30.355 -0.296  1.00 41.87 ? 56  ARG B N   1 
ATOM   2765 C  CA  . ARG B 1 67  ? -18.180 -29.336 -1.130  1.00 32.03 ? 56  ARG B CA  1 
ATOM   2766 C  C   . ARG B 1 67  ? -19.634 -29.090 -0.748  1.00 32.47 ? 56  ARG B C   1 
ATOM   2767 O  O   . ARG B 1 67  ? -20.125 -27.963 -0.853  1.00 38.88 ? 56  ARG B O   1 
ATOM   2768 C  CB  . ARG B 1 67  ? -18.092 -29.793 -2.578  1.00 41.34 ? 56  ARG B CB  1 
ATOM   2769 C  CG  . ARG B 1 67  ? -18.963 -29.066 -3.562  1.00 39.21 ? 56  ARG B CG  1 
ATOM   2770 C  CD  . ARG B 1 67  ? -18.122 -28.884 -4.778  1.00 34.89 ? 56  ARG B CD  1 
ATOM   2771 N  NE  . ARG B 1 67  ? -18.903 -28.765 -5.991  1.00 38.80 ? 56  ARG B NE  1 
ATOM   2772 C  CZ  . ARG B 1 67  ? -18.406 -28.313 -7.131  1.00 39.51 ? 56  ARG B CZ  1 
ATOM   2773 N  NH1 . ARG B 1 67  ? -17.127 -27.972 -7.241  1.00 30.68 ? 56  ARG B NH1 1 
ATOM   2774 N  NH2 . ARG B 1 67  ? -19.212 -28.185 -8.180  1.00 46.16 ? 56  ARG B NH2 1 
ATOM   2775 N  N   . ASP B 1 68  ? -20.342 -30.142 -0.350  1.00 38.66 ? 57  ASP B N   1 
ATOM   2776 C  CA  . ASP B 1 68  ? -21.785 -30.096 -0.110  1.00 35.73 ? 57  ASP B CA  1 
ATOM   2777 C  C   . ASP B 1 68  ? -22.235 -28.945 0.776   1.00 34.99 ? 57  ASP B C   1 
ATOM   2778 O  O   . ASP B 1 68  ? -23.228 -28.288 0.424   1.00 33.15 ? 57  ASP B O   1 
ATOM   2779 C  CB  . ASP B 1 68  ? -22.236 -31.432 0.504   1.00 41.99 ? 57  ASP B CB  1 
ATOM   2780 C  CG  . ASP B 1 68  ? -22.291 -32.560 -0.508  1.00 54.13 ? 57  ASP B CG  1 
ATOM   2781 O  OD1 . ASP B 1 68  ? -21.828 -32.368 -1.663  1.00 45.31 ? 57  ASP B OD1 1 
ATOM   2782 O  OD2 . ASP B 1 68  ? -22.774 -33.652 -0.129  1.00 66.52 ? 57  ASP B OD2 1 
ATOM   2783 N  N   . PRO B 1 69  ? -21.608 -28.670 1.934   1.00 33.94 ? 58  PRO B N   1 
ATOM   2784 C  CA  . PRO B 1 69  ? -22.062 -27.522 2.735   1.00 34.83 ? 58  PRO B CA  1 
ATOM   2785 C  C   . PRO B 1 69  ? -21.742 -26.171 2.092   1.00 34.44 ? 58  PRO B C   1 
ATOM   2786 O  O   . PRO B 1 69  ? -22.543 -25.235 2.210   1.00 33.58 ? 58  PRO B O   1 
ATOM   2787 C  CB  . PRO B 1 69  ? -21.336 -27.715 4.078   1.00 31.93 ? 58  PRO B CB  1 
ATOM   2788 C  CG  . PRO B 1 69  ? -20.207 -28.583 3.809   1.00 27.49 ? 58  PRO B CG  1 
ATOM   2789 C  CD  . PRO B 1 69  ? -20.507 -29.395 2.597   1.00 32.86 ? 58  PRO B CD  1 
ATOM   2790 N  N   . ILE B 1 70  ? -20.606 -26.042 1.402   1.00 31.80 ? 59  ILE B N   1 
ATOM   2791 C  CA  . ILE B 1 70  ? -20.373 -24.862 0.581   1.00 29.31 ? 59  ILE B CA  1 
ATOM   2792 C  C   . ILE B 1 70  ? -21.455 -24.734 -0.479  1.00 33.42 ? 59  ILE B C   1 
ATOM   2793 O  O   . ILE B 1 70  ? -21.876 -23.622 -0.834  1.00 31.26 ? 59  ILE B O   1 
ATOM   2794 C  CB  . ILE B 1 70  ? -18.976 -24.937 -0.048  1.00 26.06 ? 59  ILE B CB  1 
ATOM   2795 C  CG1 . ILE B 1 70  ? -17.939 -25.132 1.058   1.00 27.66 ? 59  ILE B CG1 1 
ATOM   2796 C  CG2 . ILE B 1 70  ? -18.715 -23.695 -0.903  1.00 20.60 ? 59  ILE B CG2 1 
ATOM   2797 C  CD1 . ILE B 1 70  ? -16.526 -25.323 0.550   1.00 31.38 ? 59  ILE B CD1 1 
ATOM   2798 N  N   . GLN B 1 71  ? -21.939 -25.858 -0.990  1.00 31.27 ? 60  GLN B N   1 
ATOM   2799 C  CA  . GLN B 1 71  ? -22.945 -25.780 -2.033  1.00 34.50 ? 60  GLN B CA  1 
ATOM   2800 C  C   . GLN B 1 71  ? -24.365 -25.588 -1.506  1.00 34.00 ? 60  GLN B C   1 
ATOM   2801 O  O   . GLN B 1 71  ? -25.268 -25.355 -2.312  1.00 32.88 ? 60  GLN B O   1 
ATOM   2802 C  CB  . GLN B 1 71  ? -22.879 -27.017 -2.916  1.00 35.48 ? 60  GLN B CB  1 
ATOM   2803 C  CG  . GLN B 1 71  ? -23.223 -26.716 -4.360  1.00 36.42 ? 60  GLN B CG  1 
ATOM   2804 C  CD  . GLN B 1 71  ? -23.356 -27.972 -5.180  1.00 37.87 ? 60  GLN B CD  1 
ATOM   2805 O  OE1 . GLN B 1 71  ? -24.452 -28.317 -5.609  1.00 38.45 ? 60  GLN B OE1 1 
ATOM   2806 N  NE2 . GLN B 1 71  ? -22.235 -28.673 -5.401  1.00 37.59 ? 60  GLN B NE2 1 
ATOM   2807 N  N   . ARG B 1 72  ? -24.601 -25.657 -0.195  1.00 27.77 ? 61  ARG B N   1 
ATOM   2808 C  CA  . ARG B 1 72  ? -25.922 -25.277 0.292   1.00 30.30 ? 61  ARG B CA  1 
ATOM   2809 C  C   . ARG B 1 72  ? -26.156 -23.776 0.212   1.00 35.08 ? 61  ARG B C   1 
ATOM   2810 O  O   . ARG B 1 72  ? -27.295 -23.331 0.411   1.00 35.99 ? 61  ARG B O   1 
ATOM   2811 C  CB  . ARG B 1 72  ? -26.126 -25.750 1.729   1.00 33.69 ? 61  ARG B CB  1 
ATOM   2812 C  CG  . ARG B 1 72  ? -25.943 -27.248 1.905   1.00 39.49 ? 61  ARG B CG  1 
ATOM   2813 C  CD  . ARG B 1 72  ? -27.164 -28.018 1.439   1.00 31.05 ? 61  ARG B CD  1 
ATOM   2814 N  NE  . ARG B 1 72  ? -28.284 -27.828 2.352   1.00 43.66 ? 61  ARG B NE  1 
ATOM   2815 C  CZ  . ARG B 1 72  ? -29.528 -27.586 1.959   1.00 45.23 ? 61  ARG B CZ  1 
ATOM   2816 N  NH1 . ARG B 1 72  ? -29.841 -27.508 0.675   1.00 44.62 ? 61  ARG B NH1 1 
ATOM   2817 N  NH2 . ARG B 1 72  ? -30.478 -27.417 2.877   1.00 30.81 ? 61  ARG B NH2 1 
ATOM   2818 N  N   . ILE B 1 73  ? -25.100 -23.003 -0.078  1.00 35.90 ? 62  ILE B N   1 
ATOM   2819 C  CA  . ILE B 1 73  ? -25.148 -21.550 -0.188  1.00 31.30 ? 62  ILE B CA  1 
ATOM   2820 C  C   . ILE B 1 73  ? -24.840 -21.096 -1.612  1.00 31.51 ? 62  ILE B C   1 
ATOM   2821 O  O   . ILE B 1 73  ? -25.572 -20.287 -2.192  1.00 31.96 ? 62  ILE B O   1 
ATOM   2822 C  CB  . ILE B 1 73  ? -24.180 -20.882 0.826   1.00 31.53 ? 62  ILE B CB  1 
ATOM   2823 C  CG1 . ILE B 1 73  ? -24.562 -21.243 2.268   1.00 23.24 ? 62  ILE B CG1 1 
ATOM   2824 C  CG2 . ILE B 1 73  ? -24.088 -19.361 0.610   1.00 26.79 ? 62  ILE B CG2 1 
ATOM   2825 C  CD1 . ILE B 1 73  ? -25.832 -20.573 2.747   1.00 25.04 ? 62  ILE B CD1 1 
ATOM   2826 N  N   . HIS B 1 74  ? -23.780 -21.641 -2.208  1.00 35.90 ? 63  HIS B N   1 
ATOM   2827 C  CA  . HIS B 1 74  ? -23.304 -21.215 -3.521  1.00 32.57 ? 63  HIS B CA  1 
ATOM   2828 C  C   . HIS B 1 74  ? -23.724 -22.179 -4.630  1.00 27.36 ? 63  HIS B C   1 
ATOM   2829 O  O   . HIS B 1 74  ? -23.753 -23.398 -4.441  1.00 30.48 ? 63  HIS B O   1 
ATOM   2830 C  CB  . HIS B 1 74  ? -21.782 -21.075 -3.502  1.00 28.80 ? 63  HIS B CB  1 
ATOM   2831 C  CG  . HIS B 1 74  ? -21.274 -20.087 -2.492  1.00 31.54 ? 63  HIS B CG  1 
ATOM   2832 N  ND1 . HIS B 1 74  ? -21.244 -18.726 -2.729  1.00 35.99 ? 63  HIS B ND1 1 
ATOM   2833 C  CD2 . HIS B 1 74  ? -20.751 -20.263 -1.255  1.00 28.72 ? 63  HIS B CD2 1 
ATOM   2834 C  CE1 . HIS B 1 74  ? -20.727 -18.108 -1.681  1.00 33.34 ? 63  HIS B CE1 1 
ATOM   2835 N  NE2 . HIS B 1 74  ? -20.414 -19.019 -0.776  1.00 33.26 ? 63  HIS B NE2 1 
ATOM   2836 N  N   . THR B 1 75  ? -24.031 -21.626 -5.798  1.00 31.48 ? 64  THR B N   1 
ATOM   2837 C  CA  . THR B 1 75  ? -24.478 -22.453 -6.908  1.00 26.81 ? 64  THR B CA  1 
ATOM   2838 C  C   . THR B 1 75  ? -23.333 -23.315 -7.415  1.00 27.40 ? 64  THR B C   1 
ATOM   2839 O  O   . THR B 1 75  ? -22.170 -22.909 -7.394  1.00 33.95 ? 64  THR B O   1 
ATOM   2840 C  CB  . THR B 1 75  ? -25.042 -21.595 -8.045  1.00 26.18 ? 64  THR B CB  1 
ATOM   2841 O  OG1 . THR B 1 75  ? -24.015 -20.780 -8.589  1.00 31.94 ? 64  THR B OG1 1 
ATOM   2842 C  CG2 . THR B 1 75  ? -26.160 -20.702 -7.562  1.00 22.11 ? 64  THR B CG2 1 
ATOM   2843 N  N   . ALA B 1 76  ? -23.668 -24.526 -7.850  1.00 28.96 ? 65  ALA B N   1 
ATOM   2844 C  CA  . ALA B 1 76  ? -22.653 -25.395 -8.426  1.00 31.92 ? 65  ALA B CA  1 
ATOM   2845 C  C   . ALA B 1 76  ? -22.022 -24.775 -9.665  1.00 29.41 ? 65  ALA B C   1 
ATOM   2846 O  O   . ALA B 1 76  ? -20.834 -24.985 -9.910  1.00 36.33 ? 65  ALA B O   1 
ATOM   2847 C  CB  . ALA B 1 76  ? -23.248 -26.763 -8.752  1.00 27.53 ? 65  ALA B CB  1 
ATOM   2848 N  N   . GLU B 1 77  ? -22.786 -24.007 -10.449 1.00 31.37 ? 66  GLU B N   1 
ATOM   2849 C  CA  . GLU B 1 77  ? -22.203 -23.301 -11.593 1.00 35.54 ? 66  GLU B CA  1 
ATOM   2850 C  C   . GLU B 1 77  ? -21.161 -22.275 -11.142 1.00 33.81 ? 66  GLU B C   1 
ATOM   2851 O  O   . GLU B 1 77  ? -20.132 -22.087 -11.803 1.00 31.30 ? 66  GLU B O   1 
ATOM   2852 C  CB  . GLU B 1 77  ? -23.286 -22.609 -12.429 1.00 25.49 ? 66  GLU B CB  1 
ATOM   2853 C  CG  . GLU B 1 77  ? -24.507 -23.411 -12.800 1.00 31.41 ? 66  GLU B CG  1 
ATOM   2854 C  CD  . GLU B 1 77  ? -25.475 -23.644 -11.620 1.00 54.15 ? 66  GLU B CD  1 
ATOM   2855 O  OE1 . GLU B 1 77  ? -25.137 -24.394 -10.674 1.00 48.66 ? 66  GLU B OE1 1 
ATOM   2856 O  OE2 . GLU B 1 77  ? -26.579 -23.044 -11.629 1.00 63.87 ? 66  GLU B OE2 1 
ATOM   2857 N  N   . TYR B 1 78  ? -21.417 -21.602 -10.020 1.00 29.80 ? 67  TYR B N   1 
ATOM   2858 C  CA  . TYR B 1 78  ? -20.449 -20.671 -9.460  1.00 23.94 ? 67  TYR B CA  1 
ATOM   2859 C  C   . TYR B 1 78  ? -19.222 -21.392 -8.932  1.00 32.66 ? 67  TYR B C   1 
ATOM   2860 O  O   . TYR B 1 78  ? -18.090 -20.938 -9.145  1.00 33.98 ? 67  TYR B O   1 
ATOM   2861 C  CB  . TYR B 1 78  ? -21.098 -19.873 -8.342  1.00 31.61 ? 67  TYR B CB  1 
ATOM   2862 C  CG  . TYR B 1 78  ? -20.170 -18.903 -7.692  1.00 32.20 ? 67  TYR B CG  1 
ATOM   2863 C  CD1 . TYR B 1 78  ? -19.804 -17.724 -8.341  1.00 27.71 ? 67  TYR B CD1 1 
ATOM   2864 C  CD2 . TYR B 1 78  ? -19.660 -19.160 -6.425  1.00 27.88 ? 67  TYR B CD2 1 
ATOM   2865 C  CE1 . TYR B 1 78  ? -18.942 -16.835 -7.747  1.00 30.87 ? 67  TYR B CE1 1 
ATOM   2866 C  CE2 . TYR B 1 78  ? -18.796 -18.287 -5.819  1.00 30.45 ? 67  TYR B CE2 1 
ATOM   2867 C  CZ  . TYR B 1 78  ? -18.437 -17.119 -6.481  1.00 33.97 ? 67  TYR B CZ  1 
ATOM   2868 O  OH  . TYR B 1 78  ? -17.571 -16.244 -5.864  1.00 28.46 ? 67  TYR B OH  1 
ATOM   2869 N  N   . LEU B 1 79  ? -19.422 -22.514 -8.234  1.00 32.51 ? 68  LEU B N   1 
ATOM   2870 C  CA  . LEU B 1 79  ? -18.284 -23.247 -7.679  1.00 34.06 ? 68  LEU B CA  1 
ATOM   2871 C  C   . LEU B 1 79  ? -17.400 -23.844 -8.773  1.00 33.84 ? 68  LEU B C   1 
ATOM   2872 O  O   . LEU B 1 79  ? -16.166 -23.778 -8.680  1.00 34.75 ? 68  LEU B O   1 
ATOM   2873 C  CB  . LEU B 1 79  ? -18.771 -24.334 -6.725  1.00 32.30 ? 68  LEU B CB  1 
ATOM   2874 C  CG  . LEU B 1 79  ? -19.418 -23.734 -5.485  1.00 29.93 ? 68  LEU B CG  1 
ATOM   2875 C  CD1 . LEU B 1 79  ? -19.860 -24.835 -4.546  1.00 33.92 ? 68  LEU B CD1 1 
ATOM   2876 C  CD2 . LEU B 1 79  ? -18.415 -22.841 -4.824  1.00 24.44 ? 68  LEU B CD2 1 
ATOM   2877 N  N   . ASN B 1 80  ? -18.007 -24.424 -9.815  1.00 32.09 ? 69  ASN B N   1 
ATOM   2878 C  CA  . ASN B 1 80  ? -17.226 -24.940 -10.940 1.00 31.33 ? 69  ASN B CA  1 
ATOM   2879 C  C   . ASN B 1 80  ? -16.512 -23.821 -11.686 1.00 32.47 ? 69  ASN B C   1 
ATOM   2880 O  O   . ASN B 1 80  ? -15.340 -23.970 -12.053 1.00 38.49 ? 69  ASN B O   1 
ATOM   2881 C  CB  . ASN B 1 80  ? -18.118 -25.723 -11.899 1.00 29.63 ? 69  ASN B CB  1 
ATOM   2882 C  CG  . ASN B 1 80  ? -18.808 -26.868 -11.224 1.00 32.89 ? 69  ASN B CG  1 
ATOM   2883 O  OD1 . ASN B 1 80  ? -18.338 -27.347 -10.203 1.00 40.40 ? 69  ASN B OD1 1 
ATOM   2884 N  ND2 . ASN B 1 80  ? -19.929 -27.313 -11.776 1.00 34.47 ? 69  ASN B ND2 1 
ATOM   2885 N  N   . PHE B 1 81  ? -17.191 -22.696 -11.928 1.00 29.40 ? 70  PHE B N   1 
ATOM   2886 C  CA  . PHE B 1 81  ? -16.525 -21.600 -12.617 1.00 27.43 ? 70  PHE B CA  1 
ATOM   2887 C  C   . PHE B 1 81  ? -15.306 -21.141 -11.838 1.00 30.90 ? 70  PHE B C   1 
ATOM   2888 O  O   . PHE B 1 81  ? -14.201 -21.040 -12.388 1.00 27.49 ? 70  PHE B O   1 
ATOM   2889 C  CB  . PHE B 1 81  ? -17.474 -20.421 -12.838 1.00 23.03 ? 70  PHE B CB  1 
ATOM   2890 C  CG  . PHE B 1 81  ? -16.753 -19.170 -13.295 1.00 32.10 ? 70  PHE B CG  1 
ATOM   2891 C  CD1 . PHE B 1 81  ? -16.402 -19.003 -14.633 1.00 29.70 ? 70  PHE B CD1 1 
ATOM   2892 C  CD2 . PHE B 1 81  ? -16.361 -18.187 -12.374 1.00 27.90 ? 70  PHE B CD2 1 
ATOM   2893 C  CE1 . PHE B 1 81  ? -15.712 -17.859 -15.046 1.00 30.59 ? 70  PHE B CE1 1 
ATOM   2894 C  CE2 . PHE B 1 81  ? -15.660 -17.052 -12.777 1.00 23.41 ? 70  PHE B CE2 1 
ATOM   2895 C  CZ  . PHE B 1 81  ? -15.341 -16.880 -14.108 1.00 28.44 ? 70  PHE B CZ  1 
ATOM   2896 N  N   . PHE B 1 82  ? -15.505 -20.852 -10.546 1.00 32.85 ? 71  PHE B N   1 
ATOM   2897 C  CA  . PHE B 1 82  ? -14.450 -20.283 -9.711  1.00 33.81 ? 71  PHE B CA  1 
ATOM   2898 C  C   . PHE B 1 82  ? -13.258 -21.228 -9.626  1.00 34.38 ? 71  PHE B C   1 
ATOM   2899 O  O   . PHE B 1 82  ? -12.104 -20.790 -9.700  1.00 34.28 ? 71  PHE B O   1 
ATOM   2900 C  CB  . PHE B 1 82  ? -15.040 -19.959 -8.325  1.00 34.88 ? 71  PHE B CB  1 
ATOM   2901 C  CG  . PHE B 1 82  ? -14.027 -19.569 -7.266  1.00 33.92 ? 71  PHE B CG  1 
ATOM   2902 C  CD1 . PHE B 1 82  ? -12.936 -18.751 -7.563  1.00 35.24 ? 71  PHE B CD1 1 
ATOM   2903 C  CD2 . PHE B 1 82  ? -14.194 -20.001 -5.949  1.00 29.43 ? 71  PHE B CD2 1 
ATOM   2904 C  CE1 . PHE B 1 82  ? -12.002 -18.390 -6.569  1.00 28.75 ? 71  PHE B CE1 1 
ATOM   2905 C  CE2 . PHE B 1 82  ? -13.273 -19.650 -4.956  1.00 30.75 ? 71  PHE B CE2 1 
ATOM   2906 C  CZ  . PHE B 1 82  ? -12.175 -18.839 -5.270  1.00 32.87 ? 71  PHE B CZ  1 
ATOM   2907 N  N   . GLU B 1 83  ? -13.518 -22.536 -9.531  1.00 34.51 ? 72  GLU B N   1 
ATOM   2908 C  CA  . GLU B 1 83  ? -12.447 -23.511 -9.375  1.00 34.85 ? 72  GLU B CA  1 
ATOM   2909 C  C   . GLU B 1 83  ? -11.716 -23.829 -10.665 1.00 35.53 ? 72  GLU B C   1 
ATOM   2910 O  O   . GLU B 1 83  ? -10.574 -24.307 -10.605 1.00 37.23 ? 72  GLU B O   1 
ATOM   2911 C  CB  . GLU B 1 83  ? -12.998 -24.791 -8.777  1.00 36.37 ? 72  GLU B CB  1 
ATOM   2912 C  CG  . GLU B 1 83  ? -12.969 -24.730 -7.286  1.00 43.42 ? 72  GLU B CG  1 
ATOM   2913 C  CD  . GLU B 1 83  ? -13.973 -25.634 -6.657  1.00 40.81 ? 72  GLU B CD  1 
ATOM   2914 O  OE1 . GLU B 1 83  ? -14.532 -26.491 -7.376  1.00 38.76 ? 72  GLU B OE1 1 
ATOM   2915 O  OE2 . GLU B 1 83  ? -14.187 -25.473 -5.439  1.00 41.50 ? 72  GLU B OE2 1 
ATOM   2916 N  N   . GLY B 1 84  ? -12.334 -23.575 -11.818 1.00 31.59 ? 73  GLY B N   1 
ATOM   2917 C  CA  . GLY B 1 84  ? -11.677 -23.729 -13.091 1.00 26.92 ? 73  GLY B CA  1 
ATOM   2918 C  C   . GLY B 1 84  ? -11.185 -22.455 -13.730 1.00 31.38 ? 73  GLY B C   1 
ATOM   2919 O  O   . GLY B 1 84  ? -10.589 -22.513 -14.812 1.00 31.21 ? 73  GLY B O   1 
ATOM   2920 N  N   . ALA B 1 85  ? -11.405 -21.303 -13.096 1.00 29.77 ? 74  ALA B N   1 
ATOM   2921 C  CA  . ALA B 1 85  ? -11.098 -20.035 -13.751 1.00 35.75 ? 74  ALA B CA  1 
ATOM   2922 C  C   . ALA B 1 85  ? -9.599  -19.902 -14.004 1.00 36.20 ? 74  ALA B C   1 
ATOM   2923 O  O   . ALA B 1 85  ? -9.164  -19.736 -15.149 1.00 39.81 ? 74  ALA B O   1 
ATOM   2924 C  CB  . ALA B 1 85  ? -11.637 -18.858 -12.926 1.00 31.99 ? 74  ALA B CB  1 
ATOM   2925 N  N   . TRP B 1 86  ? -8.786  -20.009 -12.950 1.00 36.64 ? 75  TRP B N   1 
ATOM   2926 C  CA  . TRP B 1 86  ? -7.339  -19.914 -13.133 1.00 37.63 ? 75  TRP B CA  1 
ATOM   2927 C  C   . TRP B 1 86  ? -6.838  -20.863 -14.216 1.00 36.96 ? 75  TRP B C   1 
ATOM   2928 O  O   . TRP B 1 86  ? -5.967  -20.500 -15.016 1.00 38.76 ? 75  TRP B O   1 
ATOM   2929 C  CB  . TRP B 1 86  ? -6.605  -20.195 -11.822 1.00 37.99 ? 75  TRP B CB  1 
ATOM   2930 C  CG  . TRP B 1 86  ? -5.135  -19.956 -11.953 1.00 37.84 ? 75  TRP B CG  1 
ATOM   2931 C  CD1 . TRP B 1 86  ? -4.128  -20.886 -11.893 1.00 33.35 ? 75  TRP B CD1 1 
ATOM   2932 C  CD2 . TRP B 1 86  ? -4.505  -18.698 -12.211 1.00 42.38 ? 75  TRP B CD2 1 
ATOM   2933 N  NE1 . TRP B 1 86  ? -2.910  -20.272 -12.080 1.00 37.16 ? 75  TRP B NE1 1 
ATOM   2934 C  CE2 . TRP B 1 86  ? -3.115  -18.931 -12.277 1.00 39.69 ? 75  TRP B CE2 1 
ATOM   2935 C  CE3 . TRP B 1 86  ? -4.982  -17.389 -12.385 1.00 40.43 ? 75  TRP B CE3 1 
ATOM   2936 C  CZ2 . TRP B 1 86  ? -2.207  -17.910 -12.506 1.00 39.08 ? 75  TRP B CZ2 1 
ATOM   2937 C  CZ3 . TRP B 1 86  ? -4.070  -16.373 -12.612 1.00 37.32 ? 75  TRP B CZ3 1 
ATOM   2938 C  CH2 . TRP B 1 86  ? -2.705  -16.638 -12.674 1.00 38.77 ? 75  TRP B CH2 1 
ATOM   2939 N  N   . ALA B 1 87  ? -7.388  -22.077 -14.273 1.00 36.06 ? 76  ALA B N   1 
ATOM   2940 C  CA  . ALA B 1 87  ? -6.880  -23.052 -15.234 1.00 36.39 ? 76  ALA B CA  1 
ATOM   2941 C  C   . ALA B 1 87  ? -7.155  -22.627 -16.677 1.00 47.32 ? 76  ALA B C   1 
ATOM   2942 O  O   . ALA B 1 87  ? -6.289  -22.784 -17.548 1.00 52.99 ? 76  ALA B O   1 
ATOM   2943 C  CB  . ALA B 1 87  ? -7.475  -24.423 -14.947 1.00 25.39 ? 76  ALA B CB  1 
ATOM   2944 N  N   . ARG B 1 88  ? -8.347  -22.080 -16.954 1.00 43.26 ? 77  ARG B N   1 
ATOM   2945 C  CA  . ARG B 1 88  ? -8.652  -21.619 -18.309 1.00 36.28 ? 77  ARG B CA  1 
ATOM   2946 C  C   . ARG B 1 88  ? -7.782  -20.430 -18.697 1.00 45.90 ? 77  ARG B C   1 
ATOM   2947 O  O   . ARG B 1 88  ? -7.371  -20.302 -19.857 1.00 46.24 ? 77  ARG B O   1 
ATOM   2948 C  CB  . ARG B 1 88  ? -10.131 -21.244 -18.423 1.00 30.14 ? 77  ARG B CB  1 
ATOM   2949 C  CG  . ARG B 1 88  ? -11.099 -22.339 -18.051 1.00 28.35 ? 77  ARG B CG  1 
ATOM   2950 C  CD  . ARG B 1 88  ? -12.452 -21.758 -17.790 1.00 36.59 ? 77  ARG B CD  1 
ATOM   2951 N  NE  . ARG B 1 88  ? -12.932 -21.010 -18.946 1.00 42.14 ? 77  ARG B NE  1 
ATOM   2952 C  CZ  . ARG B 1 88  ? -14.064 -20.320 -18.986 1.00 29.05 ? 77  ARG B CZ  1 
ATOM   2953 N  NH1 . ARG B 1 88  ? -14.864 -20.245 -17.931 1.00 26.48 ? 77  ARG B NH1 1 
ATOM   2954 N  NH2 . ARG B 1 88  ? -14.392 -19.685 -20.109 1.00 26.11 ? 77  ARG B NH2 1 
ATOM   2955 N  N   . TRP B 1 89  ? -7.521  -19.536 -17.737 1.00 45.81 ? 78  TRP B N   1 
ATOM   2956 C  CA  . TRP B 1 89  ? -6.650  -18.391 -17.977 1.00 46.21 ? 78  TRP B CA  1 
ATOM   2957 C  C   . TRP B 1 89  ? -5.241  -18.835 -18.341 1.00 53.72 ? 78  TRP B C   1 
ATOM   2958 O  O   . TRP B 1 89  ? -4.608  -18.253 -19.228 1.00 60.03 ? 78  TRP B O   1 
ATOM   2959 C  CB  . TRP B 1 89  ? -6.628  -17.515 -16.733 1.00 42.11 ? 78  TRP B CB  1 
ATOM   2960 C  CG  . TRP B 1 89  ? -5.859  -16.234 -16.809 1.00 46.08 ? 78  TRP B CG  1 
ATOM   2961 C  CD1 . TRP B 1 89  ? -4.968  -15.772 -15.883 1.00 44.43 ? 78  TRP B CD1 1 
ATOM   2962 C  CD2 . TRP B 1 89  ? -5.957  -15.213 -17.816 1.00 50.86 ? 78  TRP B CD2 1 
ATOM   2963 N  NE1 . TRP B 1 89  ? -4.496  -14.539 -16.253 1.00 46.03 ? 78  TRP B NE1 1 
ATOM   2964 C  CE2 . TRP B 1 89  ? -5.088  -14.169 -17.434 1.00 48.97 ? 78  TRP B CE2 1 
ATOM   2965 C  CE3 . TRP B 1 89  ? -6.697  -15.075 -18.997 1.00 51.47 ? 78  TRP B CE3 1 
ATOM   2966 C  CZ2 . TRP B 1 89  ? -4.926  -13.005 -18.202 1.00 48.76 ? 78  TRP B CZ2 1 
ATOM   2967 C  CZ3 . TRP B 1 89  ? -6.533  -13.922 -19.755 1.00 46.75 ? 78  TRP B CZ3 1 
ATOM   2968 C  CH2 . TRP B 1 89  ? -5.653  -12.906 -19.354 1.00 42.78 ? 78  TRP B CH2 1 
ATOM   2969 N  N   . GLN B 1 90  ? -4.721  -19.856 -17.660 1.00 50.82 ? 79  GLN B N   1 
ATOM   2970 C  CA  . GLN B 1 90  ? -3.398  -20.334 -18.024 1.00 48.30 ? 79  GLN B CA  1 
ATOM   2971 C  C   . GLN B 1 90  ? -3.430  -21.143 -19.310 1.00 48.98 ? 79  GLN B C   1 
ATOM   2972 O  O   . GLN B 1 90  ? -2.391  -21.272 -19.958 1.00 61.75 ? 79  GLN B O   1 
ATOM   2973 C  CB  . GLN B 1 90  ? -2.784  -21.156 -16.884 1.00 44.61 ? 79  GLN B CB  1 
ATOM   2974 C  CG  . GLN B 1 90  ? -2.739  -20.436 -15.546 1.00 40.02 ? 79  GLN B CG  1 
ATOM   2975 C  CD  . GLN B 1 90  ? -1.731  -19.299 -15.505 1.00 52.07 ? 79  GLN B CD  1 
ATOM   2976 O  OE1 . GLN B 1 90  ? -2.013  -18.173 -15.937 1.00 58.76 ? 79  GLN B OE1 1 
ATOM   2977 N  NE2 . GLN B 1 90  ? -0.555  -19.579 -14.966 1.00 55.52 ? 79  GLN B NE2 1 
ATOM   2978 N  N   . GLU B 1 91  ? -4.593  -21.671 -19.708 1.00 46.83 ? 80  GLU B N   1 
ATOM   2979 C  CA  . GLU B 1 91  ? -4.662  -22.373 -20.986 1.00 51.66 ? 80  GLU B CA  1 
ATOM   2980 C  C   . GLU B 1 91  ? -4.650  -21.419 -22.174 1.00 53.25 ? 80  GLU B C   1 
ATOM   2981 O  O   . GLU B 1 91  ? -4.257  -21.829 -23.266 1.00 61.42 ? 80  GLU B O   1 
ATOM   2982 C  CB  . GLU B 1 91  ? -5.895  -23.283 -21.064 1.00 51.64 ? 80  GLU B CB  1 
ATOM   2983 C  CG  . GLU B 1 91  ? -5.780  -24.567 -20.225 1.00 72.13 ? 80  GLU B CG  1 
ATOM   2984 C  CD  . GLU B 1 91  ? -5.537  -25.848 -21.061 1.00 92.03 ? 80  GLU B CD  1 
ATOM   2985 O  OE1 . GLU B 1 91  ? -6.500  -26.357 -21.688 1.00 83.36 ? 80  GLU B OE1 1 
ATOM   2986 O  OE2 . GLU B 1 91  ? -4.382  -26.356 -21.074 1.00 81.62 ? 80  GLU B OE2 1 
ATOM   2987 N  N   . GLN B 1 92  ? -5.063  -20.165 -22.000 1.00 49.13 ? 81  GLN B N   1 
ATOM   2988 C  CA  . GLN B 1 92  ? -4.923  -19.155 -23.050 1.00 55.94 ? 81  GLN B CA  1 
ATOM   2989 C  C   . GLN B 1 92  ? -3.738  -18.231 -22.777 1.00 60.37 ? 81  GLN B C   1 
ATOM   2990 O  O   . GLN B 1 92  ? -3.805  -17.023 -23.045 1.00 53.57 ? 81  GLN B O   1 
ATOM   2991 C  CB  . GLN B 1 92  ? -6.216  -18.351 -23.211 1.00 52.34 ? 81  GLN B CB  1 
ATOM   2992 C  CG  . GLN B 1 92  ? -6.734  -17.702 -21.928 1.00 60.71 ? 81  GLN B CG  1 
ATOM   2993 C  CD  . GLN B 1 92  ? -7.884  -16.712 -22.147 1.00 61.99 ? 81  GLN B CD  1 
ATOM   2994 O  OE1 . GLN B 1 92  ? -7.668  -15.500 -22.264 1.00 65.71 ? 81  GLN B OE1 1 
ATOM   2995 N  NE2 . GLN B 1 92  ? -9.117  -17.229 -22.178 1.00 41.93 ? 81  GLN B NE2 1 
ATOM   2996 N  N   . ASP B 1 93  ? -2.639  -18.798 -22.261 1.00 52.42 ? 82  ASP B N   1 
ATOM   2997 C  CA  . ASP B 1 93  ? -1.454  -18.062 -21.834 1.00 54.41 ? 82  ASP B CA  1 
ATOM   2998 C  C   . ASP B 1 93  ? -1.806  -16.717 -21.233 1.00 58.08 ? 82  ASP B C   1 
ATOM   2999 O  O   . ASP B 1 93  ? -1.416  -15.674 -21.768 1.00 65.06 ? 82  ASP B O   1 
ATOM   3000 C  CB  . ASP B 1 93  ? -0.462  -17.858 -22.984 1.00 62.79 ? 82  ASP B CB  1 
ATOM   3001 C  CG  . ASP B 1 93  ? -0.311  -19.092 -23.852 1.00 72.79 ? 82  ASP B CG  1 
ATOM   3002 O  OD1 . ASP B 1 93  ? 0.020   -18.945 -25.056 1.00 74.09 ? 82  ASP B OD1 1 
ATOM   3003 O  OD2 . ASP B 1 93  ? -0.527  -20.207 -23.327 1.00 67.79 ? 82  ASP B OD2 1 
ATOM   3004 N  N   . GLY B 1 94  ? -2.554  -16.735 -20.134 1.00 56.93 ? 83  GLY B N   1 
ATOM   3005 C  CA  . GLY B 1 94  ? -2.878  -15.498 -19.451 1.00 54.72 ? 83  GLY B CA  1 
ATOM   3006 C  C   . GLY B 1 94  ? -1.653  -14.901 -18.779 1.00 59.14 ? 83  GLY B C   1 
ATOM   3007 O  O   . GLY B 1 94  ? -0.859  -15.605 -18.149 1.00 58.26 ? 83  GLY B O   1 
ATOM   3008 N  N   . THR B 1 95  ? -1.527  -13.572 -18.891 1.00 54.25 ? 84  THR B N   1 
ATOM   3009 C  CA  . THR B 1 95  ? -0.292  -12.886 -18.518 1.00 62.45 ? 84  THR B CA  1 
ATOM   3010 C  C   . THR B 1 95  ? -0.049  -12.936 -17.012 1.00 64.53 ? 84  THR B C   1 
ATOM   3011 O  O   . THR B 1 95  ? 0.980   -13.446 -16.555 1.00 68.94 ? 84  THR B O   1 
ATOM   3012 C  CB  . THR B 1 95  ? -0.327  -11.435 -19.007 1.00 64.72 ? 84  THR B CB  1 
ATOM   3013 O  OG1 . THR B 1 95  ? -0.639  -11.405 -20.405 1.00 71.60 ? 84  THR B OG1 1 
ATOM   3014 C  CG2 . THR B 1 95  ? 1.022   -10.773 -18.790 1.00 51.76 ? 84  THR B CG2 1 
ATOM   3015 N  N   . GLY B 1 96  ? -0.975  -12.394 -16.223 1.00 57.52 ? 85  GLY B N   1 
ATOM   3016 C  CA  . GLY B 1 96  ? -0.799  -12.362 -14.781 1.00 47.22 ? 85  GLY B CA  1 
ATOM   3017 C  C   . GLY B 1 96  ? -2.054  -12.735 -14.018 1.00 51.45 ? 85  GLY B C   1 
ATOM   3018 O  O   . GLY B 1 96  ? -2.624  -13.810 -14.241 1.00 52.16 ? 85  GLY B O   1 
ATOM   3019 N  N   . ASP B 1 97  ? -2.496  -11.857 -13.119 1.00 46.68 ? 86  ASP B N   1 
ATOM   3020 C  CA  . ASP B 1 97  ? -3.718  -12.102 -12.364 1.00 44.44 ? 86  ASP B CA  1 
ATOM   3021 C  C   . ASP B 1 97  ? -4.948  -12.018 -13.268 1.00 48.79 ? 86  ASP B C   1 
ATOM   3022 O  O   . ASP B 1 97  ? -5.010  -11.214 -14.203 1.00 48.33 ? 86  ASP B O   1 
ATOM   3023 C  CB  . ASP B 1 97  ? -3.863  -11.099 -11.221 1.00 40.84 ? 86  ASP B CB  1 
ATOM   3024 C  CG  . ASP B 1 97  ? -3.229  -11.576 -9.930  1.00 55.75 ? 86  ASP B CG  1 
ATOM   3025 O  OD1 . ASP B 1 97  ? -2.485  -12.588 -9.951  1.00 48.80 ? 86  ASP B OD1 1 
ATOM   3026 O  OD2 . ASP B 1 97  ? -3.488  -10.929 -8.885  1.00 62.29 ? 86  ASP B OD2 1 
ATOM   3027 N  N   . LEU B 1 98  ? -5.939  -12.856 -12.968 1.00 42.20 ? 87  LEU B N   1 
ATOM   3028 C  CA  . LEU B 1 98  ? -7.197  -12.879 -13.700 1.00 40.64 ? 87  LEU B CA  1 
ATOM   3029 C  C   . LEU B 1 98  ? -8.188  -11.939 -13.021 1.00 39.46 ? 87  LEU B C   1 
ATOM   3030 O  O   . LEU B 1 98  ? -8.515  -12.119 -11.841 1.00 43.15 ? 87  LEU B O   1 
ATOM   3031 C  CB  . LEU B 1 98  ? -7.759  -14.297 -13.760 1.00 37.54 ? 87  LEU B CB  1 
ATOM   3032 C  CG  . LEU B 1 98  ? -9.037  -14.394 -14.580 1.00 34.64 ? 87  LEU B CG  1 
ATOM   3033 C  CD1 . LEU B 1 98  ? -8.760  -13.982 -16.040 1.00 28.27 ? 87  LEU B CD1 1 
ATOM   3034 C  CD2 . LEU B 1 98  ? -9.600  -15.797 -14.471 1.00 31.34 ? 87  LEU B CD2 1 
ATOM   3035 N  N   . LEU B 1 99  ? -8.673  -10.950 -13.763 1.00 36.47 ? 88  LEU B N   1 
ATOM   3036 C  CA  . LEU B 1 99  ? -9.594  -9.959  -13.232 1.00 41.07 ? 88  LEU B CA  1 
ATOM   3037 C  C   . LEU B 1 99  ? -10.668 -9.617  -14.256 1.00 39.92 ? 88  LEU B C   1 
ATOM   3038 O  O   . LEU B 1 99  ? -10.436 -9.718  -15.470 1.00 35.08 ? 88  LEU B O   1 
ATOM   3039 C  CB  . LEU B 1 99  ? -8.849  -8.681  -12.817 1.00 38.87 ? 88  LEU B CB  1 
ATOM   3040 C  CG  . LEU B 1 99  ? -8.054  -8.844  -11.523 1.00 45.59 ? 88  LEU B CG  1 
ATOM   3041 C  CD1 . LEU B 1 99  ? -6.605  -8.444  -11.757 1.00 42.62 ? 88  LEU B CD1 1 
ATOM   3042 C  CD2 . LEU B 1 99  ? -8.701  -8.076  -10.344 1.00 38.90 ? 88  LEU B CD2 1 
ATOM   3043 N  N   . PRO B 1 100 ? -11.860 -9.243  -13.797 1.00 38.32 ? 89  PRO B N   1 
ATOM   3044 C  CA  . PRO B 1 100 ? -12.891 -8.749  -14.710 1.00 36.44 ? 89  PRO B CA  1 
ATOM   3045 C  C   . PRO B 1 100 ? -12.717 -7.261  -14.966 1.00 37.11 ? 89  PRO B C   1 
ATOM   3046 O  O   . PRO B 1 100 ? -12.133 -6.522  -14.166 1.00 36.57 ? 89  PRO B O   1 
ATOM   3047 C  CB  . PRO B 1 100 ? -14.200 -9.031  -13.954 1.00 31.78 ? 89  PRO B CB  1 
ATOM   3048 C  CG  . PRO B 1 100 ? -13.820 -8.981  -12.511 1.00 33.35 ? 89  PRO B CG  1 
ATOM   3049 C  CD  . PRO B 1 100 ? -12.335 -9.283  -12.400 1.00 37.37 ? 89  PRO B CD  1 
ATOM   3050 N  N   . TYR B 1 101 ? -13.229 -6.832  -16.119 1.00 38.46 ? 90  TYR B N   1 
ATOM   3051 C  CA  . TYR B 1 101 ? -13.140 -5.424  -16.485 1.00 33.49 ? 90  TYR B CA  1 
ATOM   3052 C  C   . TYR B 1 101 ? -14.438 -4.885  -17.071 1.00 32.88 ? 90  TYR B C   1 
ATOM   3053 O  O   . TYR B 1 101 ? -14.448 -3.741  -17.543 1.00 39.38 ? 90  TYR B O   1 
ATOM   3054 C  CB  . TYR B 1 101 ? -11.984 -5.205  -17.460 1.00 32.71 ? 90  TYR B CB  1 
ATOM   3055 C  CG  . TYR B 1 101 ? -12.151 -5.900  -18.790 1.00 36.74 ? 90  TYR B CG  1 
ATOM   3056 C  CD1 . TYR B 1 101 ? -11.890 -7.250  -18.930 1.00 43.18 ? 90  TYR B CD1 1 
ATOM   3057 C  CD2 . TYR B 1 101 ? -12.556 -5.199  -19.912 1.00 42.49 ? 90  TYR B CD2 1 
ATOM   3058 C  CE1 . TYR B 1 101 ? -12.034 -7.880  -20.152 1.00 43.77 ? 90  TYR B CE1 1 
ATOM   3059 C  CE2 . TYR B 1 101 ? -12.703 -5.823  -21.133 1.00 42.64 ? 90  TYR B CE2 1 
ATOM   3060 C  CZ  . TYR B 1 101 ? -12.444 -7.161  -21.245 1.00 39.73 ? 90  TYR B CZ  1 
ATOM   3061 O  OH  . TYR B 1 101 ? -12.592 -7.780  -22.460 1.00 42.95 ? 90  TYR B OH  1 
ATOM   3062 N  N   . THR B 1 102 ? -15.519 -5.676  -17.063 1.00 33.16 ? 91  THR B N   1 
ATOM   3063 C  CA  . THR B 1 102 ? -16.863 -5.283  -17.475 1.00 33.08 ? 91  THR B CA  1 
ATOM   3064 C  C   . THR B 1 102 ? -17.848 -5.933  -16.516 1.00 32.09 ? 91  THR B C   1 
ATOM   3065 O  O   . THR B 1 102 ? -17.599 -7.029  -16.021 1.00 33.26 ? 91  THR B O   1 
ATOM   3066 C  CB  . THR B 1 102 ? -17.194 -5.719  -18.917 1.00 32.20 ? 91  THR B CB  1 
ATOM   3067 O  OG1 . THR B 1 102 ? -16.022 -5.636  -19.731 1.00 34.95 ? 91  THR B OG1 1 
ATOM   3068 C  CG2 . THR B 1 102 ? -18.293 -4.846  -19.528 1.00 30.27 ? 91  THR B CG2 1 
ATOM   3069 N  N   . TRP B 1 103 ? -18.959 -5.259  -16.242 1.00 30.47 ? 92  TRP B N   1 
ATOM   3070 C  CA  . TRP B 1 103 ? -19.935 -5.802  -15.303 1.00 33.10 ? 92  TRP B CA  1 
ATOM   3071 C  C   . TRP B 1 103 ? -21.356 -5.587  -15.814 1.00 33.53 ? 92  TRP B C   1 
ATOM   3072 O  O   . TRP B 1 103 ? -21.638 -4.573  -16.467 1.00 30.23 ? 92  TRP B O   1 
ATOM   3073 C  CB  . TRP B 1 103 ? -19.779 -5.168  -13.911 1.00 30.76 ? 92  TRP B CB  1 
ATOM   3074 C  CG  . TRP B 1 103 ? -18.554 -5.628  -13.224 1.00 28.44 ? 92  TRP B CG  1 
ATOM   3075 C  CD1 . TRP B 1 103 ? -18.461 -6.643  -12.341 1.00 31.96 ? 92  TRP B CD1 1 
ATOM   3076 C  CD2 . TRP B 1 103 ? -17.232 -5.101  -13.377 1.00 26.71 ? 92  TRP B CD2 1 
ATOM   3077 N  NE1 . TRP B 1 103 ? -17.163 -6.797  -11.931 1.00 33.16 ? 92  TRP B NE1 1 
ATOM   3078 C  CE2 . TRP B 1 103 ? -16.389 -5.857  -12.554 1.00 26.77 ? 92  TRP B CE2 1 
ATOM   3079 C  CE3 . TRP B 1 103 ? -16.683 -4.065  -14.133 1.00 33.26 ? 92  TRP B CE3 1 
ATOM   3080 C  CZ2 . TRP B 1 103 ? -15.035 -5.615  -12.456 1.00 28.49 ? 92  TRP B CZ2 1 
ATOM   3081 C  CZ3 . TRP B 1 103 ? -15.340 -3.826  -14.042 1.00 32.18 ? 92  TRP B CZ3 1 
ATOM   3082 C  CH2 . TRP B 1 103 ? -14.528 -4.595  -13.205 1.00 32.58 ? 92  TRP B CH2 1 
ATOM   3083 N  N   . PRO B 1 104 ? -22.280 -6.533  -15.534 1.00 33.72 ? 93  PRO B N   1 
ATOM   3084 C  CA  . PRO B 1 104 ? -23.670 -6.323  -15.959 1.00 28.28 ? 93  PRO B CA  1 
ATOM   3085 C  C   . PRO B 1 104 ? -24.325 -5.256  -15.089 1.00 33.87 ? 93  PRO B C   1 
ATOM   3086 O  O   . PRO B 1 104 ? -25.133 -5.580  -14.213 1.00 33.23 ? 93  PRO B O   1 
ATOM   3087 C  CB  . PRO B 1 104 ? -24.304 -7.703  -15.765 1.00 27.91 ? 93  PRO B CB  1 
ATOM   3088 C  CG  . PRO B 1 104 ? -23.532 -8.304  -14.611 1.00 27.39 ? 93  PRO B CG  1 
ATOM   3089 C  CD  . PRO B 1 104 ? -22.122 -7.773  -14.739 1.00 32.19 ? 93  PRO B CD  1 
ATOM   3090 N  N   . ALA B 1 105 ? -23.967 -3.982  -15.303 1.00 30.41 ? 94  ALA B N   1 
ATOM   3091 C  CA  . ALA B 1 105 ? -24.444 -2.889  -14.467 1.00 28.45 ? 94  ALA B CA  1 
ATOM   3092 C  C   . ALA B 1 105 ? -25.763 -2.350  -15.033 1.00 27.95 ? 94  ALA B C   1 
ATOM   3093 O  O   . ALA B 1 105 ? -26.483 -3.047  -15.750 1.00 27.76 ? 94  ALA B O   1 
ATOM   3094 C  CB  . ALA B 1 105 ? -23.350 -1.823  -14.343 1.00 26.04 ? 94  ALA B CB  1 
ATOM   3095 N  N   . ARG B 1 106 ? -26.098 -1.107  -14.715 1.00 26.81 ? 95  ARG B N   1 
ATOM   3096 C  CA  . ARG B 1 106 ? -27.338 -0.512  -15.187 1.00 27.43 ? 95  ARG B CA  1 
ATOM   3097 C  C   . ARG B 1 106 ? -27.374 -0.449  -16.713 1.00 30.90 ? 95  ARG B C   1 
ATOM   3098 O  O   . ARG B 1 106 ? -26.388 -0.094  -17.362 1.00 32.77 ? 95  ARG B O   1 
ATOM   3099 C  CB  . ARG B 1 106 ? -27.499 0.885   -14.588 1.00 23.49 ? 95  ARG B CB  1 
ATOM   3100 C  CG  . ARG B 1 106 ? -27.681 0.917   -13.062 1.00 25.32 ? 95  ARG B CG  1 
ATOM   3101 C  CD  . ARG B 1 106 ? -27.513 2.346   -12.522 1.00 31.15 ? 95  ARG B CD  1 
ATOM   3102 N  NE  . ARG B 1 106 ? -28.337 3.253   -13.305 1.00 35.15 ? 95  ARG B NE  1 
ATOM   3103 C  CZ  . ARG B 1 106 ? -27.889 4.187   -14.133 1.00 31.83 ? 95  ARG B CZ  1 
ATOM   3104 N  NH1 . ARG B 1 106 ? -26.614 4.538   -14.163 1.00 30.53 ? 95  ARG B NH1 1 
ATOM   3105 N  NH2 . ARG B 1 106 ? -28.738 4.756   -14.976 1.00 27.01 ? 95  ARG B NH2 1 
ATOM   3106 N  N   . THR B 1 107 ? -28.530 -0.808  -17.276 1.00 29.91 ? 96  THR B N   1 
ATOM   3107 C  CA  . THR B 1 107 ? -28.941 -0.844  -18.694 1.00 31.49 ? 96  THR B CA  1 
ATOM   3108 C  C   . THR B 1 107 ? -28.437 -2.088  -19.415 1.00 26.40 ? 96  THR B C   1 
ATOM   3109 O  O   . THR B 1 107 ? -28.818 -2.296  -20.578 1.00 33.97 ? 96  THR B O   1 
ATOM   3110 C  CB  . THR B 1 107 ? -28.570 0.409   -19.531 1.00 25.84 ? 96  THR B CB  1 
ATOM   3111 O  OG1 . THR B 1 107 ? -27.175 0.433   -19.860 1.00 27.77 ? 96  THR B OG1 1 
ATOM   3112 C  CG2 . THR B 1 107 ? -28.970 1.679   -18.837 1.00 21.76 ? 96  THR B CG2 1 
ATOM   3113 N  N   . LEU B 1 108 ? -27.651 -2.938  -18.770 1.00 29.14 ? 97  LEU B N   1 
ATOM   3114 C  CA  . LEU B 1 108 ? -27.149 -4.170  -19.365 1.00 29.01 ? 97  LEU B CA  1 
ATOM   3115 C  C   . LEU B 1 108 ? -28.005 -5.364  -18.943 1.00 31.26 ? 97  LEU B C   1 
ATOM   3116 O  O   . LEU B 1 108 ? -28.752 -5.300  -17.966 1.00 31.67 ? 97  LEU B O   1 
ATOM   3117 C  CB  . LEU B 1 108 ? -25.686 -4.390  -18.967 1.00 26.30 ? 97  LEU B CB  1 
ATOM   3118 C  CG  . LEU B 1 108 ? -24.791 -3.260  -19.470 1.00 23.59 ? 97  LEU B CG  1 
ATOM   3119 C  CD1 . LEU B 1 108 ? -23.352 -3.553  -19.204 1.00 22.91 ? 97  LEU B CD1 1 
ATOM   3120 C  CD2 . LEU B 1 108 ? -25.015 -3.045  -20.970 1.00 28.87 ? 97  LEU B CD2 1 
ATOM   3121 N  N   . SER B 1 109 ? -27.909 -6.448  -19.719 1.00 32.54 ? 98  SER B N   1 
ATOM   3122 C  CA  . SER B 1 109 ? -28.563 -7.711  -19.391 1.00 25.69 ? 98  SER B CA  1 
ATOM   3123 C  C   . SER B 1 109 ? -27.731 -8.466  -18.376 1.00 32.69 ? 98  SER B C   1 
ATOM   3124 O  O   . SER B 1 109 ? -26.511 -8.570  -18.522 1.00 35.39 ? 98  SER B O   1 
ATOM   3125 C  CB  . SER B 1 109 ? -28.709 -8.606  -20.623 1.00 31.23 ? 98  SER B CB  1 
ATOM   3126 O  OG  . SER B 1 109 ? -29.819 -8.273  -21.426 1.00 48.23 ? 98  SER B OG  1 
ATOM   3127 N  N   . GLN B 1 110 ? -28.391 -9.026  -17.364 1.00 29.06 ? 99  GLN B N   1 
ATOM   3128 C  CA  . GLN B 1 110 ? -27.716 -9.954  -16.457 1.00 33.36 ? 99  GLN B CA  1 
ATOM   3129 C  C   . GLN B 1 110 ? -27.732 -11.372 -17.039 1.00 34.96 ? 99  GLN B C   1 
ATOM   3130 O  O   . GLN B 1 110 ? -28.324 -12.301 -16.492 1.00 33.24 ? 99  GLN B O   1 
ATOM   3131 C  CB  . GLN B 1 110 ? -28.357 -9.907  -15.077 1.00 29.42 ? 99  GLN B CB  1 
ATOM   3132 C  CG  . GLN B 1 110 ? -28.528 -8.509  -14.540 1.00 29.80 ? 99  GLN B CG  1 
ATOM   3133 C  CD  . GLN B 1 110 ? -29.018 -8.503  -13.116 1.00 31.12 ? 99  GLN B CD  1 
ATOM   3134 O  OE1 . GLN B 1 110 ? -29.649 -9.456  -12.656 1.00 39.62 ? 99  GLN B OE1 1 
ATOM   3135 N  NE2 . GLN B 1 110 ? -28.725 -7.433  -12.402 1.00 38.26 ? 99  GLN B NE2 1 
ATOM   3136 N  N   . ARG B 1 111 ? -27.054 -11.523 -18.177 1.00 33.94 ? 100 ARG B N   1 
ATOM   3137 C  CA  . ARG B 1 111 ? -27.075 -12.757 -18.953 1.00 32.77 ? 100 ARG B CA  1 
ATOM   3138 C  C   . ARG B 1 111 ? -25.647 -13.225 -19.193 1.00 35.11 ? 100 ARG B C   1 
ATOM   3139 O  O   . ARG B 1 111 ? -24.766 -12.421 -19.519 1.00 36.22 ? 100 ARG B O   1 
ATOM   3140 C  CB  . ARG B 1 111 ? -27.805 -12.556 -20.280 1.00 33.92 ? 100 ARG B CB  1 
ATOM   3141 C  CG  . ARG B 1 111 ? -28.004 -13.827 -21.056 1.00 44.07 ? 100 ARG B CG  1 
ATOM   3142 C  CD  . ARG B 1 111 ? -27.857 -13.598 -22.550 1.00 47.44 ? 100 ARG B CD  1 
ATOM   3143 N  NE  . ARG B 1 111 ? -29.068 -13.039 -23.142 1.00 54.33 ? 100 ARG B NE  1 
ATOM   3144 C  CZ  . ARG B 1 111 ? -29.618 -13.472 -24.270 1.00 49.67 ? 100 ARG B CZ  1 
ATOM   3145 N  NH1 . ARG B 1 111 ? -29.107 -14.497 -24.943 1.00 41.78 ? 100 ARG B NH1 1 
ATOM   3146 N  NH2 . ARG B 1 111 ? -30.708 -12.866 -24.729 1.00 39.90 ? 100 ARG B NH2 1 
ATOM   3147 N  N   . LEU B 1 112 ? -25.428 -14.530 -19.049 1.00 33.39 ? 101 LEU B N   1 
ATOM   3148 C  CA  . LEU B 1 112 ? -24.078 -15.065 -18.878 1.00 33.94 ? 101 LEU B CA  1 
ATOM   3149 C  C   . LEU B 1 112 ? -23.375 -15.270 -20.222 1.00 34.04 ? 101 LEU B C   1 
ATOM   3150 O  O   . LEU B 1 112 ? -23.900 -15.993 -21.077 1.00 32.52 ? 101 LEU B O   1 
ATOM   3151 C  CB  . LEU B 1 112 ? -24.150 -16.376 -18.109 1.00 32.66 ? 101 LEU B CB  1 
ATOM   3152 C  CG  . LEU B 1 112 ? -22.871 -17.202 -17.969 1.00 37.15 ? 101 LEU B CG  1 
ATOM   3153 C  CD1 . LEU B 1 112 ? -21.895 -16.568 -16.972 1.00 33.43 ? 101 LEU B CD1 1 
ATOM   3154 C  CD2 . LEU B 1 112 ? -23.218 -18.606 -17.580 1.00 19.24 ? 101 LEU B CD2 1 
ATOM   3155 N  N   . PRO B 1 113 ? -22.207 -14.654 -20.454 1.00 31.52 ? 102 PRO B N   1 
ATOM   3156 C  CA  . PRO B 1 113 ? -21.460 -14.882 -21.698 1.00 31.94 ? 102 PRO B CA  1 
ATOM   3157 C  C   . PRO B 1 113 ? -20.731 -16.214 -21.614 1.00 31.79 ? 102 PRO B C   1 
ATOM   3158 O  O   . PRO B 1 113 ? -20.784 -16.906 -20.604 1.00 33.30 ? 102 PRO B O   1 
ATOM   3159 C  CB  . PRO B 1 113 ? -20.465 -13.713 -21.765 1.00 30.68 ? 102 PRO B CB  1 
ATOM   3160 C  CG  . PRO B 1 113 ? -20.746 -12.845 -20.560 1.00 30.99 ? 102 PRO B CG  1 
ATOM   3161 C  CD  . PRO B 1 113 ? -21.566 -13.642 -19.595 1.00 31.38 ? 102 PRO B CD  1 
ATOM   3162 N  N   . THR B 1 114 ? -20.050 -16.578 -22.701 1.00 32.64 ? 103 THR B N   1 
ATOM   3163 C  CA  . THR B 1 114 ? -19.190 -17.755 -22.650 1.00 33.26 ? 103 THR B CA  1 
ATOM   3164 C  C   . THR B 1 114 ? -17.730 -17.404 -22.381 1.00 36.42 ? 103 THR B C   1 
ATOM   3165 O  O   . THR B 1 114 ? -17.011 -18.219 -21.788 1.00 43.91 ? 103 THR B O   1 
ATOM   3166 C  CB  . THR B 1 114 ? -19.302 -18.582 -23.944 1.00 32.36 ? 103 THR B CB  1 
ATOM   3167 O  OG1 . THR B 1 114 ? -18.762 -17.848 -25.046 1.00 41.01 ? 103 THR B OG1 1 
ATOM   3168 C  CG2 . THR B 1 114 ? -20.755 -18.949 -24.240 1.00 31.60 ? 103 THR B CG2 1 
ATOM   3169 N  N   . SER B 1 115 ? -17.307 -16.197 -22.770 1.00 33.41 ? 104 SER B N   1 
ATOM   3170 C  CA  . SER B 1 115 ? -15.959 -15.690 -22.534 1.00 29.87 ? 104 SER B CA  1 
ATOM   3171 C  C   . SER B 1 115 ? -15.556 -15.829 -21.070 1.00 34.36 ? 104 SER B C   1 
ATOM   3172 O  O   . SER B 1 115 ? -16.367 -15.623 -20.161 1.00 35.45 ? 104 SER B O   1 
ATOM   3173 C  CB  . SER B 1 115 ? -15.902 -14.213 -22.973 1.00 30.45 ? 104 SER B CB  1 
ATOM   3174 O  OG  . SER B 1 115 ? -14.818 -13.491 -22.401 1.00 34.94 ? 104 SER B OG  1 
ATOM   3175 N  N   . LEU B 1 116 ? -14.285 -16.186 -20.847 1.00 34.20 ? 105 LEU B N   1 
ATOM   3176 C  CA  . LEU B 1 116 ? -13.760 -16.248 -19.487 1.00 30.96 ? 105 LEU B CA  1 
ATOM   3177 C  C   . LEU B 1 116 ? -13.952 -14.919 -18.768 1.00 36.04 ? 105 LEU B C   1 
ATOM   3178 O  O   . LEU B 1 116 ? -14.468 -14.883 -17.647 1.00 37.84 ? 105 LEU B O   1 
ATOM   3179 C  CB  . LEU B 1 116 ? -12.276 -16.631 -19.494 1.00 31.69 ? 105 LEU B CB  1 
ATOM   3180 C  CG  . LEU B 1 116 ? -11.616 -16.699 -18.100 1.00 33.29 ? 105 LEU B CG  1 
ATOM   3181 C  CD1 . LEU B 1 116 ? -12.333 -17.708 -17.174 1.00 31.07 ? 105 LEU B CD1 1 
ATOM   3182 C  CD2 . LEU B 1 116 ? -10.099 -16.960 -18.133 1.00 29.60 ? 105 LEU B CD2 1 
ATOM   3183 N  N   . HIS B 1 117 ? -13.546 -13.807 -19.399 1.00 36.23 ? 106 HIS B N   1 
ATOM   3184 C  CA  . HIS B 1 117 ? -13.634 -12.511 -18.720 1.00 35.89 ? 106 HIS B CA  1 
ATOM   3185 C  C   . HIS B 1 117 ? -15.082 -12.035 -18.593 1.00 35.17 ? 106 HIS B C   1 
ATOM   3186 O  O   . HIS B 1 117 ? -15.453 -11.438 -17.575 1.00 30.87 ? 106 HIS B O   1 
ATOM   3187 C  CB  . HIS B 1 117 ? -12.779 -11.467 -19.448 1.00 36.99 ? 106 HIS B CB  1 
ATOM   3188 C  CG  . HIS B 1 117 ? -11.309 -11.608 -19.195 1.00 40.90 ? 106 HIS B CG  1 
ATOM   3189 N  ND1 . HIS B 1 117 ? -10.486 -12.379 -19.993 1.00 46.33 ? 106 HIS B ND1 1 
ATOM   3190 C  CD2 . HIS B 1 117 ? -10.518 -11.097 -18.221 1.00 34.88 ? 106 HIS B CD2 1 
ATOM   3191 C  CE1 . HIS B 1 117 ? -9.252  -12.329 -19.524 1.00 40.93 ? 106 HIS B CE1 1 
ATOM   3192 N  NE2 . HIS B 1 117 ? -9.243  -11.557 -18.452 1.00 38.32 ? 106 HIS B NE2 1 
ATOM   3193 N  N   . GLY B 1 118 ? -15.908 -12.271 -19.618 1.00 29.32 ? 107 GLY B N   1 
ATOM   3194 C  CA  . GLY B 1 118 ? -17.319 -11.959 -19.492 1.00 28.45 ? 107 GLY B CA  1 
ATOM   3195 C  C   . GLY B 1 118 ? -17.975 -12.722 -18.356 1.00 34.17 ? 107 GLY B C   1 
ATOM   3196 O  O   . GLY B 1 118 ? -18.701 -12.152 -17.533 1.00 33.51 ? 107 GLY B O   1 
ATOM   3197 N  N   . GLN B 1 119 ? -17.735 -14.032 -18.304 1.00 34.28 ? 108 GLN B N   1 
ATOM   3198 C  CA  . GLN B 1 119 ? -18.190 -14.824 -17.172 1.00 31.43 ? 108 GLN B CA  1 
ATOM   3199 C  C   . GLN B 1 119 ? -17.694 -14.241 -15.848 1.00 35.63 ? 108 GLN B C   1 
ATOM   3200 O  O   . GLN B 1 119 ? -18.457 -14.138 -14.878 1.00 37.49 ? 108 GLN B O   1 
ATOM   3201 C  CB  . GLN B 1 119 ? -17.731 -16.270 -17.351 1.00 26.45 ? 108 GLN B CB  1 
ATOM   3202 C  CG  . GLN B 1 119 ? -18.632 -17.017 -18.298 1.00 33.69 ? 108 GLN B CG  1 
ATOM   3203 C  CD  . GLN B 1 119 ? -18.243 -18.461 -18.533 1.00 34.20 ? 108 GLN B CD  1 
ATOM   3204 O  OE1 . GLN B 1 119 ? -17.215 -18.936 -18.061 1.00 34.29 ? 108 GLN B OE1 1 
ATOM   3205 N  NE2 . GLN B 1 119 ? -19.075 -19.166 -19.277 1.00 36.79 ? 108 GLN B NE2 1 
ATOM   3206 N  N   . LEU B 1 120 ? -16.424 -13.835 -15.789 1.00 29.01 ? 109 LEU B N   1 
ATOM   3207 C  CA  . LEU B 1 120 ? -15.879 -13.339 -14.534 1.00 28.28 ? 109 LEU B CA  1 
ATOM   3208 C  C   . LEU B 1 120 ? -16.613 -12.081 -14.073 1.00 36.53 ? 109 LEU B C   1 
ATOM   3209 O  O   . LEU B 1 120 ? -16.944 -11.948 -12.888 1.00 32.83 ? 109 LEU B O   1 
ATOM   3210 C  CB  . LEU B 1 120 ? -14.380 -13.083 -14.694 1.00 28.86 ? 109 LEU B CB  1 
ATOM   3211 C  CG  . LEU B 1 120 ? -13.526 -12.704 -13.485 1.00 33.33 ? 109 LEU B CG  1 
ATOM   3212 C  CD1 . LEU B 1 120 ? -13.694 -13.667 -12.283 1.00 25.67 ? 109 LEU B CD1 1 
ATOM   3213 C  CD2 . LEU B 1 120 ? -12.094 -12.669 -13.946 1.00 35.47 ? 109 LEU B CD2 1 
ATOM   3214 N  N   . GLY B 1 121 ? -16.885 -11.148 -14.994 1.00 32.63 ? 110 GLY B N   1 
ATOM   3215 C  CA  . GLY B 1 121 ? -17.607 -9.949  -14.613 1.00 26.92 ? 110 GLY B CA  1 
ATOM   3216 C  C   . GLY B 1 121 ? -19.052 -10.212 -14.297 1.00 31.97 ? 110 GLY B C   1 
ATOM   3217 O  O   . GLY B 1 121 ? -19.667 -9.442  -13.551 1.00 31.40 ? 110 GLY B O   1 
ATOM   3218 N  N   . TYR B 1 122 ? -19.606 -11.290 -14.860 1.00 35.22 ? 111 TYR B N   1 
ATOM   3219 C  CA  . TYR B 1 122 ? -20.951 -11.725 -14.512 1.00 27.31 ? 111 TYR B CA  1 
ATOM   3220 C  C   . TYR B 1 122 ? -21.015 -12.227 -13.071 1.00 31.24 ? 111 TYR B C   1 
ATOM   3221 O  O   . TYR B 1 122 ? -22.000 -11.978 -12.365 1.00 32.12 ? 111 TYR B O   1 
ATOM   3222 C  CB  . TYR B 1 122 ? -21.390 -12.803 -15.486 1.00 26.87 ? 111 TYR B CB  1 
ATOM   3223 C  CG  . TYR B 1 122 ? -22.716 -13.436 -15.149 1.00 34.73 ? 111 TYR B CG  1 
ATOM   3224 C  CD1 . TYR B 1 122 ? -23.902 -12.896 -15.623 1.00 35.71 ? 111 TYR B CD1 1 
ATOM   3225 C  CD2 . TYR B 1 122 ? -22.786 -14.576 -14.355 1.00 34.14 ? 111 TYR B CD2 1 
ATOM   3226 C  CE1 . TYR B 1 122 ? -25.106 -13.467 -15.317 1.00 34.50 ? 111 TYR B CE1 1 
ATOM   3227 C  CE2 . TYR B 1 122 ? -23.987 -15.150 -14.045 1.00 30.39 ? 111 TYR B CE2 1 
ATOM   3228 C  CZ  . TYR B 1 122 ? -25.142 -14.594 -14.534 1.00 33.53 ? 111 TYR B CZ  1 
ATOM   3229 O  OH  . TYR B 1 122 ? -26.346 -15.168 -14.241 1.00 33.79 ? 111 TYR B OH  1 
ATOM   3230 N  N   . TYR B 1 123 ? -19.969 -12.921 -12.613 1.00 33.42 ? 112 TYR B N   1 
ATOM   3231 C  CA  . TYR B 1 123 ? -19.880 -13.473 -11.267 1.00 27.49 ? 112 TYR B CA  1 
ATOM   3232 C  C   . TYR B 1 123 ? -19.189 -12.541 -10.285 1.00 28.48 ? 112 TYR B C   1 
ATOM   3233 O  O   . TYR B 1 123 ? -18.704 -13.002 -9.239  1.00 28.19 ? 112 TYR B O   1 
ATOM   3234 C  CB  . TYR B 1 123 ? -19.137 -14.810 -11.294 1.00 31.95 ? 112 TYR B CB  1 
ATOM   3235 C  CG  . TYR B 1 123 ? -19.922 -15.938 -11.919 1.00 31.80 ? 112 TYR B CG  1 
ATOM   3236 C  CD1 . TYR B 1 123 ? -21.057 -16.435 -11.310 1.00 30.09 ? 112 TYR B CD1 1 
ATOM   3237 C  CD2 . TYR B 1 123 ? -19.522 -16.503 -13.120 1.00 28.63 ? 112 TYR B CD2 1 
ATOM   3238 C  CE1 . TYR B 1 123 ? -21.767 -17.455 -11.878 1.00 30.51 ? 112 TYR B CE1 1 
ATOM   3239 C  CE2 . TYR B 1 123 ? -20.224 -17.518 -13.692 1.00 24.45 ? 112 TYR B CE2 1 
ATOM   3240 C  CZ  . TYR B 1 123 ? -21.344 -17.994 -13.071 1.00 25.62 ? 112 TYR B CZ  1 
ATOM   3241 O  OH  . TYR B 1 123 ? -22.060 -19.014 -13.646 1.00 27.12 ? 112 TYR B OH  1 
ATOM   3242 N  N   . SER B 1 124 ? -19.104 -11.255 -10.598 1.00 27.36 ? 113 SER B N   1 
ATOM   3243 C  CA  . SER B 1 124 ? -18.493 -10.299 -9.689  1.00 31.75 ? 113 SER B CA  1 
ATOM   3244 C  C   . SER B 1 124 ? -19.239 -8.976  -9.772  1.00 32.62 ? 113 SER B C   1 
ATOM   3245 O  O   . SER B 1 124 ? -20.041 -8.742  -10.682 1.00 33.29 ? 113 SER B O   1 
ATOM   3246 C  CB  . SER B 1 124 ? -17.007 -10.087 -9.993  1.00 29.53 ? 113 SER B CB  1 
ATOM   3247 O  OG  . SER B 1 124 ? -16.844 -9.646  -11.320 1.00 33.86 ? 113 SER B OG  1 
ATOM   3248 N  N   . PHE B 1 125 ? -18.963 -8.113  -8.788  1.00 33.16 ? 114 PHE B N   1 
ATOM   3249 C  CA  . PHE B 1 125 ? -19.501 -6.766  -8.746  1.00 30.03 ? 114 PHE B CA  1 
ATOM   3250 C  C   . PHE B 1 125 ? -18.426 -5.691  -8.605  1.00 26.76 ? 114 PHE B C   1 
ATOM   3251 O  O   . PHE B 1 125 ? -18.761 -4.506  -8.537  1.00 32.00 ? 114 PHE B O   1 
ATOM   3252 C  CB  . PHE B 1 125 ? -20.544 -6.652  -7.616  1.00 30.01 ? 114 PHE B CB  1 
ATOM   3253 C  CG  . PHE B 1 125 ? -19.964 -6.526  -6.220  1.00 32.04 ? 114 PHE B CG  1 
ATOM   3254 C  CD1 . PHE B 1 125 ? -19.674 -7.654  -5.465  1.00 29.37 ? 114 PHE B CD1 1 
ATOM   3255 C  CD2 . PHE B 1 125 ? -19.764 -5.269  -5.641  1.00 36.69 ? 114 PHE B CD2 1 
ATOM   3256 C  CE1 . PHE B 1 125 ? -19.166 -7.551  -4.179  1.00 28.13 ? 114 PHE B CE1 1 
ATOM   3257 C  CE2 . PHE B 1 125 ? -19.252 -5.150  -4.349  1.00 32.78 ? 114 PHE B CE2 1 
ATOM   3258 C  CZ  . PHE B 1 125 ? -18.952 -6.298  -3.620  1.00 33.33 ? 114 PHE B CZ  1 
ATOM   3259 N  N   . ASP B 1 126 ? -17.154 -6.060  -8.590  1.00 26.62 ? 115 ASP B N   1 
ATOM   3260 C  CA  . ASP B 1 126 ? -16.061 -5.100  -8.482  1.00 29.95 ? 115 ASP B CA  1 
ATOM   3261 C  C   . ASP B 1 126 ? -14.774 -5.812  -8.891  1.00 31.72 ? 115 ASP B C   1 
ATOM   3262 O  O   . ASP B 1 126 ? -14.782 -6.995  -9.251  1.00 33.96 ? 115 ASP B O   1 
ATOM   3263 C  CB  . ASP B 1 126 ? -15.988 -4.482  -7.069  1.00 30.25 ? 115 ASP B CB  1 
ATOM   3264 C  CG  . ASP B 1 126 ? -15.175 -5.326  -6.047  1.00 32.89 ? 115 ASP B CG  1 
ATOM   3265 O  OD1 . ASP B 1 126 ? -15.006 -6.563  -6.214  1.00 31.91 ? 115 ASP B OD1 1 
ATOM   3266 O  OD2 . ASP B 1 126 ? -14.730 -4.728  -5.032  1.00 31.78 ? 115 ASP B OD2 1 
ATOM   3267 N  N   . ALA B 1 127 ? -13.663 -5.080  -8.833  1.00 28.19 ? 116 ALA B N   1 
ATOM   3268 C  CA  . ALA B 1 127 ? -12.365 -5.590  -9.256  1.00 35.98 ? 116 ALA B CA  1 
ATOM   3269 C  C   . ALA B 1 127 ? -11.476 -5.973  -8.075  1.00 35.51 ? 116 ALA B C   1 
ATOM   3270 O  O   . ALA B 1 127 ? -10.251 -6.011  -8.212  1.00 32.60 ? 116 ALA B O   1 
ATOM   3271 C  CB  . ALA B 1 127 ? -11.664 -4.554  -10.139 1.00 30.59 ? 116 ALA B CB  1 
ATOM   3272 N  N   . GLY B 1 128 ? -12.069 -6.255  -6.921  1.00 33.82 ? 117 GLY B N   1 
ATOM   3273 C  CA  . GLY B 1 128 ? -11.301 -6.471  -5.714  1.00 32.26 ? 117 GLY B CA  1 
ATOM   3274 C  C   . GLY B 1 128 ? -11.318 -7.898  -5.220  1.00 37.19 ? 117 GLY B C   1 
ATOM   3275 O  O   . GLY B 1 128 ? -11.039 -8.163  -4.046  1.00 38.42 ? 117 GLY B O   1 
ATOM   3276 N  N   . ALA B 1 129 ? -11.664 -8.826  -6.107  1.00 34.99 ? 118 ALA B N   1 
ATOM   3277 C  CA  . ALA B 1 129 ? -11.558 -10.257 -5.847  1.00 30.22 ? 118 ALA B CA  1 
ATOM   3278 C  C   . ALA B 1 129 ? -10.809 -10.839 -7.036  1.00 37.03 ? 118 ALA B C   1 
ATOM   3279 O  O   . ALA B 1 129 ? -11.414 -11.387 -7.971  1.00 39.03 ? 118 ALA B O   1 
ATOM   3280 C  CB  . ALA B 1 129 ? -12.928 -10.901 -5.645  1.00 27.57 ? 118 ALA B CB  1 
ATOM   3281 N  N   . PRO B 1 130 ? -9.490  -10.707 -7.055  1.00 35.37 ? 119 PRO B N   1 
ATOM   3282 C  CA  . PRO B 1 130 ? -8.717  -11.263 -8.164  1.00 32.06 ? 119 PRO B CA  1 
ATOM   3283 C  C   . PRO B 1 130 ? -8.569  -12.760 -8.001  1.00 35.07 ? 119 PRO B C   1 
ATOM   3284 O  O   . PRO B 1 130 ? -8.635  -13.301 -6.895  1.00 35.52 ? 119 PRO B O   1 
ATOM   3285 C  CB  . PRO B 1 130 ? -7.370  -10.560 -8.030  1.00 31.50 ? 119 PRO B CB  1 
ATOM   3286 C  CG  . PRO B 1 130 ? -7.242  -10.374 -6.557  1.00 33.29 ? 119 PRO B CG  1 
ATOM   3287 C  CD  . PRO B 1 130 ? -8.625  -10.145 -6.006  1.00 31.26 ? 119 PRO B CD  1 
ATOM   3288 N  N   . ILE B 1 131 ? -8.375  -13.439 -9.122  1.00 38.09 ? 120 ILE B N   1 
ATOM   3289 C  CA  . ILE B 1 131 ? -8.148  -14.880 -9.120  1.00 37.04 ? 120 ILE B CA  1 
ATOM   3290 C  C   . ILE B 1 131 ? -6.733  -15.124 -9.611  1.00 35.38 ? 120 ILE B C   1 
ATOM   3291 O  O   . ILE B 1 131 ? -6.368  -14.703 -10.713 1.00 36.14 ? 120 ILE B O   1 
ATOM   3292 C  CB  . ILE B 1 131 ? -9.180  -15.621 -9.981  1.00 36.67 ? 120 ILE B CB  1 
ATOM   3293 C  CG1 . ILE B 1 131 ? -10.594 -15.201 -9.560  1.00 24.42 ? 120 ILE B CG1 1 
ATOM   3294 C  CG2 . ILE B 1 131 ? -8.955  -17.143 -9.893  1.00 30.40 ? 120 ILE B CG2 1 
ATOM   3295 C  CD1 . ILE B 1 131 ? -11.645 -15.967 -10.206 1.00 19.43 ? 120 ILE B CD1 1 
ATOM   3296 N  N   . THR B 1 132 ? -5.929  -15.774 -8.779  1.00 38.20 ? 121 THR B N   1 
ATOM   3297 C  CA  . THR B 1 132 ? -4.560  -16.115 -9.134  1.00 35.93 ? 121 THR B CA  1 
ATOM   3298 C  C   . THR B 1 132 ? -4.351  -17.598 -8.836  1.00 38.99 ? 121 THR B C   1 
ATOM   3299 O  O   . THR B 1 132 ? -5.300  -18.363 -8.613  1.00 37.98 ? 121 THR B O   1 
ATOM   3300 C  CB  . THR B 1 132 ? -3.563  -15.208 -8.399  1.00 43.22 ? 121 THR B CB  1 
ATOM   3301 O  OG1 . THR B 1 132 ? -2.236  -15.455 -8.895  1.00 40.85 ? 121 THR B OG1 1 
ATOM   3302 C  CG2 . THR B 1 132 ? -3.623  -15.432 -6.869  1.00 40.11 ? 121 THR B CG2 1 
ATOM   3303 N  N   . ALA B 1 133 ? -3.082  -18.012 -8.817  1.00 43.45 ? 122 ALA B N   1 
ATOM   3304 C  CA  . ALA B 1 133 ? -2.745  -19.430 -8.752  1.00 36.78 ? 122 ALA B CA  1 
ATOM   3305 C  C   . ALA B 1 133 ? -3.361  -20.114 -7.527  1.00 44.38 ? 122 ALA B C   1 
ATOM   3306 O  O   . ALA B 1 133 ? -3.977  -21.179 -7.655  1.00 50.28 ? 122 ALA B O   1 
ATOM   3307 C  CB  . ALA B 1 133 ? -1.229  -19.596 -8.782  1.00 26.15 ? 122 ALA B CB  1 
ATOM   3308 N  N   . GLY B 1 134 ? -3.234  -19.524 -6.334  1.00 34.83 ? 123 GLY B N   1 
ATOM   3309 C  CA  . GLY B 1 134 ? -3.735  -20.283 -5.200  1.00 30.52 ? 123 GLY B CA  1 
ATOM   3310 C  C   . GLY B 1 134 ? -5.149  -19.986 -4.719  1.00 33.99 ? 123 GLY B C   1 
ATOM   3311 O  O   . GLY B 1 134 ? -5.503  -20.383 -3.603  1.00 31.85 ? 123 GLY B O   1 
ATOM   3312 N  N   . THR B 1 135 ? -5.985  -19.321 -5.512  1.00 30.86 ? 124 THR B N   1 
ATOM   3313 C  CA  . THR B 1 135 ? -7.093  -18.592 -4.906  1.00 32.74 ? 124 THR B CA  1 
ATOM   3314 C  C   . THR B 1 135 ? -8.242  -19.508 -4.498  1.00 33.65 ? 124 THR B C   1 
ATOM   3315 O  O   . THR B 1 135 ? -8.739  -19.412 -3.368  1.00 32.18 ? 124 THR B O   1 
ATOM   3316 C  CB  . THR B 1 135 ? -7.572  -17.484 -5.849  1.00 36.44 ? 124 THR B CB  1 
ATOM   3317 O  OG1 . THR B 1 135 ? -6.463  -16.633 -6.173  1.00 36.95 ? 124 THR B OG1 1 
ATOM   3318 C  CG2 . THR B 1 135 ? -8.670  -16.653 -5.195  1.00 30.47 ? 124 THR B CG2 1 
ATOM   3319 N  N   . TRP B 1 136 ? -8.683  -20.404 -5.391  1.00 34.03 ? 125 TRP B N   1 
ATOM   3320 C  CA  . TRP B 1 136 ? -9.823  -21.242 -5.023  1.00 34.46 ? 125 TRP B CA  1 
ATOM   3321 C  C   . TRP B 1 136 ? -9.460  -22.197 -3.905  1.00 30.63 ? 125 TRP B C   1 
ATOM   3322 O  O   . TRP B 1 136 ? -10.304 -22.488 -3.059  1.00 34.73 ? 125 TRP B O   1 
ATOM   3323 C  CB  . TRP B 1 136 ? -10.401 -21.998 -6.239  1.00 36.62 ? 125 TRP B CB  1 
ATOM   3324 C  CG  . TRP B 1 136 ? -9.686  -23.251 -6.649  1.00 35.04 ? 125 TRP B CG  1 
ATOM   3325 C  CD1 . TRP B 1 136 ? -8.851  -23.395 -7.724  1.00 33.39 ? 125 TRP B CD1 1 
ATOM   3326 C  CD2 . TRP B 1 136 ? -9.755  -24.546 -6.017  1.00 41.45 ? 125 TRP B CD2 1 
ATOM   3327 N  NE1 . TRP B 1 136 ? -8.370  -24.685 -7.786  1.00 38.50 ? 125 TRP B NE1 1 
ATOM   3328 C  CE2 . TRP B 1 136 ? -8.910  -25.416 -6.756  1.00 45.86 ? 125 TRP B CE2 1 
ATOM   3329 C  CE3 . TRP B 1 136 ? -10.432 -25.053 -4.895  1.00 36.22 ? 125 TRP B CE3 1 
ATOM   3330 C  CZ2 . TRP B 1 136 ? -8.740  -26.773 -6.415  1.00 37.75 ? 125 TRP B CZ2 1 
ATOM   3331 C  CZ3 . TRP B 1 136 ? -10.253 -26.396 -4.555  1.00 38.20 ? 125 TRP B CZ3 1 
ATOM   3332 C  CH2 . TRP B 1 136 ? -9.418  -27.239 -5.317  1.00 39.43 ? 125 TRP B CH2 1 
ATOM   3333 N  N   . GLN B 1 137 ? -8.217  -22.680 -3.858  1.00 31.83 ? 126 GLN B N   1 
ATOM   3334 C  CA  . GLN B 1 137 ? -7.844  -23.536 -2.735  1.00 36.43 ? 126 GLN B CA  1 
ATOM   3335 C  C   . GLN B 1 137 ? -7.835  -22.751 -1.434  1.00 35.23 ? 126 GLN B C   1 
ATOM   3336 O  O   . GLN B 1 137 ? -8.181  -23.299 -0.379  1.00 33.75 ? 126 GLN B O   1 
ATOM   3337 C  CB  . GLN B 1 137 ? -6.484  -24.191 -2.970  1.00 31.10 ? 126 GLN B CB  1 
ATOM   3338 C  CG  . GLN B 1 137 ? -6.438  -25.065 -4.201  1.00 33.14 ? 126 GLN B CG  1 
ATOM   3339 C  CD  . GLN B 1 137 ? -5.828  -24.348 -5.395  1.00 37.85 ? 126 GLN B CD  1 
ATOM   3340 O  OE1 . GLN B 1 137 ? -6.022  -23.146 -5.577  1.00 39.75 ? 126 GLN B OE1 1 
ATOM   3341 N  NE2 . GLN B 1 137 ? -5.088  -25.082 -6.213  1.00 35.68 ? 126 GLN B NE2 1 
ATOM   3342 N  N   . ALA B 1 138 ? -7.482  -21.462 -1.502  1.00 30.89 ? 127 ALA B N   1 
ATOM   3343 C  CA  . ALA B 1 138 ? -7.474  -20.628 -0.307  1.00 30.95 ? 127 ALA B CA  1 
ATOM   3344 C  C   . ALA B 1 138 ? -8.890  -20.322 0.160   1.00 34.50 ? 127 ALA B C   1 
ATOM   3345 O  O   . ALA B 1 138 ? -9.178  -20.373 1.364   1.00 33.45 ? 127 ALA B O   1 
ATOM   3346 C  CB  . ALA B 1 138 ? -6.698  -19.341 -0.577  1.00 31.07 ? 127 ALA B CB  1 
ATOM   3347 N  N   . ALA B 1 139 ? -9.790  -20.003 -0.775  1.00 34.16 ? 128 ALA B N   1 
ATOM   3348 C  CA  . ALA B 1 139 ? -11.174 -19.743 -0.389  1.00 34.10 ? 128 ALA B CA  1 
ATOM   3349 C  C   . ALA B 1 139 ? -11.849 -21.011 0.129   1.00 36.81 ? 128 ALA B C   1 
ATOM   3350 O  O   . ALA B 1 139 ? -12.549 -20.977 1.156   1.00 34.26 ? 128 ALA B O   1 
ATOM   3351 C  CB  . ALA B 1 139 ? -11.950 -19.150 -1.563  1.00 27.71 ? 128 ALA B CB  1 
ATOM   3352 N  N   . TYR B 1 140 ? -11.649 -22.137 -0.570  1.00 30.87 ? 129 TYR B N   1 
ATOM   3353 C  CA  . TYR B 1 140 ? -12.154 -23.426 -0.101  1.00 31.64 ? 129 TYR B CA  1 
ATOM   3354 C  C   . TYR B 1 140 ? -11.701 -23.702 1.328   1.00 32.80 ? 129 TYR B C   1 
ATOM   3355 O  O   . TYR B 1 140 ? -12.475 -24.194 2.155   1.00 32.65 ? 129 TYR B O   1 
ATOM   3356 C  CB  . TYR B 1 140 ? -11.671 -24.536 -1.042  1.00 33.32 ? 129 TYR B CB  1 
ATOM   3357 C  CG  . TYR B 1 140 ? -12.157 -25.925 -0.700  1.00 36.08 ? 129 TYR B CG  1 
ATOM   3358 C  CD1 . TYR B 1 140 ? -11.448 -26.745 0.181   1.00 35.75 ? 129 TYR B CD1 1 
ATOM   3359 C  CD2 . TYR B 1 140 ? -13.322 -26.424 -1.263  1.00 35.14 ? 129 TYR B CD2 1 
ATOM   3360 C  CE1 . TYR B 1 140 ? -11.901 -28.027 0.496   1.00 36.35 ? 129 TYR B CE1 1 
ATOM   3361 C  CE2 . TYR B 1 140 ? -13.779 -27.691 -0.962  1.00 37.65 ? 129 TYR B CE2 1 
ATOM   3362 C  CZ  . TYR B 1 140 ? -13.070 -28.493 -0.087  1.00 40.56 ? 129 TYR B CZ  1 
ATOM   3363 O  OH  . TYR B 1 140 ? -13.556 -29.753 0.200   1.00 42.35 ? 129 TYR B OH  1 
ATOM   3364 N  N   . SER B 1 141 ? -10.448 -23.361 1.636   1.00 35.32 ? 130 SER B N   1 
ATOM   3365 C  CA  . SER B 1 141 ? -9.878  -23.649 2.945   1.00 31.57 ? 130 SER B CA  1 
ATOM   3366 C  C   . SER B 1 141 ? -10.496 -22.786 4.050   1.00 30.00 ? 130 SER B C   1 
ATOM   3367 O  O   . SER B 1 141 ? -10.678 -23.258 5.177   1.00 30.31 ? 130 SER B O   1 
ATOM   3368 C  CB  . SER B 1 141 ? -8.363  -23.467 2.876   1.00 33.08 ? 130 SER B CB  1 
ATOM   3369 O  OG  . SER B 1 141 ? -7.819  -23.209 4.161   1.00 46.77 ? 130 SER B OG  1 
ATOM   3370 N  N   . ALA B 1 142 ? -10.806 -21.519 3.764   1.00 32.72 ? 131 ALA B N   1 
ATOM   3371 C  CA  . ALA B 1 142 ? -11.482 -20.686 4.757   1.00 28.41 ? 131 ALA B CA  1 
ATOM   3372 C  C   . ALA B 1 142 ? -12.876 -21.223 5.058   1.00 28.76 ? 131 ALA B C   1 
ATOM   3373 O  O   . ALA B 1 142 ? -13.272 -21.331 6.223   1.00 33.04 ? 131 ALA B O   1 
ATOM   3374 C  CB  . ALA B 1 142 ? -11.551 -19.234 4.283   1.00 27.78 ? 131 ALA B CB  1 
ATOM   3375 N  N   . ALA B 1 143 ? -13.637 -21.574 4.021   1.00 26.33 ? 132 ALA B N   1 
ATOM   3376 C  CA  . ALA B 1 143 ? -14.941 -22.177 4.256   1.00 26.58 ? 132 ALA B CA  1 
ATOM   3377 C  C   . ALA B 1 143 ? -14.816 -23.422 5.128   1.00 31.47 ? 132 ALA B C   1 
ATOM   3378 O  O   . ALA B 1 143 ? -15.598 -23.618 6.068   1.00 30.18 ? 132 ALA B O   1 
ATOM   3379 C  CB  . ALA B 1 143 ? -15.613 -22.506 2.926   1.00 30.08 ? 132 ALA B CB  1 
ATOM   3380 N  N   . GLN B 1 144 ? -13.803 -24.251 4.861   1.00 29.95 ? 133 GLN B N   1 
ATOM   3381 C  CA  . GLN B 1 144 ? -13.553 -25.415 5.706   1.00 30.76 ? 133 GLN B CA  1 
ATOM   3382 C  C   . GLN B 1 144 ? -13.198 -25.012 7.136   1.00 27.89 ? 133 GLN B C   1 
ATOM   3383 O  O   . GLN B 1 144 ? -13.593 -25.686 8.089   1.00 28.43 ? 133 GLN B O   1 
ATOM   3384 C  CB  . GLN B 1 144 ? -12.446 -26.280 5.092   1.00 25.34 ? 133 GLN B CB  1 
ATOM   3385 C  CG  . GLN B 1 144 ? -12.838 -27.036 3.847   1.00 26.21 ? 133 GLN B CG  1 
ATOM   3386 C  CD  . GLN B 1 144 ? -14.248 -27.614 3.899   1.00 37.87 ? 133 GLN B CD  1 
ATOM   3387 O  OE1 . GLN B 1 144 ? -14.710 -28.084 4.946   1.00 42.59 ? 133 GLN B OE1 1 
ATOM   3388 N  NE2 . GLN B 1 144 ? -14.936 -27.596 2.759   1.00 31.83 ? 133 GLN B NE2 1 
ATOM   3389 N  N   . VAL B 1 145 ? -12.428 -23.935 7.305   1.00 28.13 ? 134 VAL B N   1 
ATOM   3390 C  CA  . VAL B 1 145 ? -12.115 -23.448 8.645   1.00 29.31 ? 134 VAL B CA  1 
ATOM   3391 C  C   . VAL B 1 145 ? -13.395 -23.042 9.360   1.00 31.39 ? 134 VAL B C   1 
ATOM   3392 O  O   . VAL B 1 145 ? -13.645 -23.439 10.508  1.00 32.76 ? 134 VAL B O   1 
ATOM   3393 C  CB  . VAL B 1 145 ? -11.113 -22.282 8.577   1.00 28.08 ? 134 VAL B CB  1 
ATOM   3394 C  CG1 . VAL B 1 145 ? -11.196 -21.440 9.838   1.00 30.61 ? 134 VAL B CG1 1 
ATOM   3395 C  CG2 . VAL B 1 145 ? -9.703  -22.792 8.367   1.00 26.14 ? 134 VAL B CG2 1 
ATOM   3396 N  N   . ALA B 1 146 ? -14.242 -22.270 8.676   1.00 29.73 ? 135 ALA B N   1 
ATOM   3397 C  CA  . ALA B 1 146 ? -15.527 -21.884 9.256   1.00 34.41 ? 135 ALA B CA  1 
ATOM   3398 C  C   . ALA B 1 146 ? -16.373 -23.102 9.617   1.00 36.18 ? 135 ALA B C   1 
ATOM   3399 O  O   . ALA B 1 146 ? -17.002 -23.134 10.682  1.00 40.15 ? 135 ALA B O   1 
ATOM   3400 C  CB  . ALA B 1 146 ? -16.290 -20.972 8.297   1.00 33.24 ? 135 ALA B CB  1 
ATOM   3401 N  N   . LEU B 1 147 ? -16.406 -24.115 8.747   1.00 32.92 ? 136 LEU B N   1 
ATOM   3402 C  CA  . LEU B 1 147 ? -17.253 -25.274 9.013   1.00 34.29 ? 136 LEU B CA  1 
ATOM   3403 C  C   . LEU B 1 147 ? -16.757 -26.078 10.207  1.00 37.15 ? 136 LEU B C   1 
ATOM   3404 O  O   . LEU B 1 147 ? -17.558 -26.721 10.899  1.00 38.48 ? 136 LEU B O   1 
ATOM   3405 C  CB  . LEU B 1 147 ? -17.326 -26.159 7.780   1.00 31.69 ? 136 LEU B CB  1 
ATOM   3406 C  CG  . LEU B 1 147 ? -18.262 -25.556 6.748   1.00 30.65 ? 136 LEU B CG  1 
ATOM   3407 C  CD1 . LEU B 1 147 ? -18.072 -26.280 5.426   1.00 29.64 ? 136 LEU B CD1 1 
ATOM   3408 C  CD2 . LEU B 1 147 ? -19.685 -25.635 7.255   1.00 25.39 ? 136 LEU B CD2 1 
ATOM   3409 N  N   . THR B 1 148 ? -15.449 -26.046 10.460  1.00 34.25 ? 137 THR B N   1 
ATOM   3410 C  CA  . THR B 1 148 ? -14.884 -26.774 11.587  1.00 33.64 ? 137 THR B CA  1 
ATOM   3411 C  C   . THR B 1 148 ? -15.254 -26.109 12.897  1.00 40.79 ? 137 THR B C   1 
ATOM   3412 O  O   . THR B 1 148 ? -15.546 -26.789 13.889  1.00 36.60 ? 137 THR B O   1 
ATOM   3413 C  CB  . THR B 1 148 ? -13.366 -26.844 11.442  1.00 36.51 ? 137 THR B CB  1 
ATOM   3414 O  OG1 . THR B 1 148 ? -13.040 -27.401 10.165  1.00 37.14 ? 137 THR B OG1 1 
ATOM   3415 C  CG2 . THR B 1 148 ? -12.754 -27.674 12.561  1.00 36.86 ? 137 THR B CG2 1 
ATOM   3416 N  N   . ALA B 1 149 ? -15.226 -24.772 12.920  1.00 41.15 ? 138 ALA B N   1 
ATOM   3417 C  CA  . ALA B 1 149 ? -15.608 -24.058 14.130  1.00 39.48 ? 138 ALA B CA  1 
ATOM   3418 C  C   . ALA B 1 149 ? -17.113 -24.148 14.356  1.00 36.91 ? 138 ALA B C   1 
ATOM   3419 O  O   . ALA B 1 149 ? -17.569 -24.305 15.495  1.00 32.30 ? 138 ALA B O   1 
ATOM   3420 C  CB  . ALA B 1 149 ? -15.132 -22.611 14.047  1.00 31.28 ? 138 ALA B CB  1 
ATOM   3421 N  N   . GLN B 1 150 ? -17.897 -24.062 13.279  1.00 36.35 ? 139 GLN B N   1 
ATOM   3422 C  CA  . GLN B 1 150 ? -19.321 -24.355 13.381  1.00 41.14 ? 139 GLN B CA  1 
ATOM   3423 C  C   . GLN B 1 150 ? -19.543 -25.731 13.994  1.00 41.62 ? 139 GLN B C   1 
ATOM   3424 O  O   . GLN B 1 150 ? -20.431 -25.912 14.840  1.00 36.20 ? 139 GLN B O   1 
ATOM   3425 C  CB  . GLN B 1 150 ? -19.971 -24.280 11.998  1.00 35.86 ? 139 GLN B CB  1 
ATOM   3426 C  CG  . GLN B 1 150 ? -21.456 -24.634 11.989  1.00 37.76 ? 139 GLN B CG  1 
ATOM   3427 C  CD  . GLN B 1 150 ? -21.726 -26.131 11.920  1.00 45.69 ? 139 GLN B CD  1 
ATOM   3428 O  OE1 . GLN B 1 150 ? -21.247 -26.843 11.020  1.00 38.02 ? 139 GLN B OE1 1 
ATOM   3429 N  NE2 . GLN B 1 150 ? -22.483 -26.621 12.899  1.00 45.13 ? 139 GLN B NE2 1 
ATOM   3430 N  N   . HIS B 1 151 ? -18.733 -26.711 13.572  1.00 39.08 ? 140 HIS B N   1 
ATOM   3431 C  CA  . HIS B 1 151 ? -18.884 -28.088 14.030  1.00 41.64 ? 140 HIS B CA  1 
ATOM   3432 C  C   . HIS B 1 151 ? -18.559 -28.235 15.514  1.00 49.86 ? 140 HIS B C   1 
ATOM   3433 O  O   . HIS B 1 151 ? -19.251 -28.969 16.229  1.00 54.51 ? 140 HIS B O   1 
ATOM   3434 C  CB  . HIS B 1 151 ? -18.000 -29.013 13.203  1.00 43.12 ? 140 HIS B CB  1 
ATOM   3435 C  CG  . HIS B 1 151 ? -18.386 -30.449 13.311  1.00 56.37 ? 140 HIS B CG  1 
ATOM   3436 N  ND1 . HIS B 1 151 ? -19.620 -30.916 12.907  1.00 61.79 ? 140 HIS B ND1 1 
ATOM   3437 C  CD2 . HIS B 1 151 ? -17.715 -31.522 13.794  1.00 62.29 ? 140 HIS B CD2 1 
ATOM   3438 C  CE1 . HIS B 1 151 ? -19.691 -32.217 13.133  1.00 58.01 ? 140 HIS B CE1 1 
ATOM   3439 N  NE2 . HIS B 1 151 ? -18.547 -32.610 13.667  1.00 57.66 ? 140 HIS B NE2 1 
ATOM   3440 N  N   . GLU B 1 152 ? -17.508 -27.562 15.995  1.00 41.46 ? 141 GLU B N   1 
ATOM   3441 C  CA  . GLU B 1 152 ? -17.207 -27.592 17.425  1.00 40.73 ? 141 GLU B CA  1 
ATOM   3442 C  C   . GLU B 1 152 ? -18.416 -27.167 18.252  1.00 40.15 ? 141 GLU B C   1 
ATOM   3443 O  O   . GLU B 1 152 ? -18.658 -27.703 19.339  1.00 43.50 ? 141 GLU B O   1 
ATOM   3444 C  CB  . GLU B 1 152 ? -16.005 -26.690 17.737  1.00 44.06 ? 141 GLU B CB  1 
ATOM   3445 C  CG  . GLU B 1 152 ? -14.641 -27.238 17.264  1.00 55.68 ? 141 GLU B CG  1 
ATOM   3446 C  CD  . GLU B 1 152 ? -14.485 -28.745 17.490  1.00 71.63 ? 141 GLU B CD  1 
ATOM   3447 O  OE1 . GLU B 1 152 ? -14.465 -29.507 16.490  1.00 77.87 ? 141 GLU B OE1 1 
ATOM   3448 O  OE2 . GLU B 1 152 ? -14.348 -29.165 18.663  1.00 79.68 ? 141 GLU B OE2 1 
ATOM   3449 N  N   . ILE B 1 153 ? -19.196 -26.214 17.745  1.00 34.93 ? 142 ILE B N   1 
ATOM   3450 C  CA  . ILE B 1 153 ? -20.311 -25.681 18.517  1.00 42.18 ? 142 ILE B CA  1 
ATOM   3451 C  C   . ILE B 1 153 ? -21.482 -26.649 18.494  1.00 47.00 ? 142 ILE B C   1 
ATOM   3452 O  O   . ILE B 1 153 ? -22.179 -26.827 19.504  1.00 43.99 ? 142 ILE B O   1 
ATOM   3453 C  CB  . ILE B 1 153 ? -20.707 -24.291 17.985  1.00 43.59 ? 142 ILE B CB  1 
ATOM   3454 C  CG1 . ILE B 1 153 ? -19.616 -23.277 18.304  1.00 35.56 ? 142 ILE B CG1 1 
ATOM   3455 C  CG2 . ILE B 1 153 ? -22.066 -23.844 18.531  1.00 34.25 ? 142 ILE B CG2 1 
ATOM   3456 C  CD1 . ILE B 1 153 ? -19.868 -21.934 17.679  1.00 32.56 ? 142 ILE B CD1 1 
ATOM   3457 N  N   . THR B 1 154 ? -21.711 -27.287 17.345  1.00 42.95 ? 143 THR B N   1 
ATOM   3458 C  CA  . THR B 1 154 ? -22.752 -28.304 17.244  1.00 42.69 ? 143 THR B CA  1 
ATOM   3459 C  C   . THR B 1 154 ? -22.500 -29.455 18.224  1.00 49.70 ? 143 THR B C   1 
ATOM   3460 O  O   . THR B 1 154 ? -23.444 -30.002 18.810  1.00 46.82 ? 143 THR B O   1 
ATOM   3461 C  CB  . THR B 1 154 ? -22.828 -28.810 15.801  1.00 43.27 ? 143 THR B CB  1 
ATOM   3462 O  OG1 . THR B 1 154 ? -23.554 -27.867 15.005  1.00 42.16 ? 143 THR B OG1 1 
ATOM   3463 C  CG2 . THR B 1 154 ? -23.546 -30.126 15.736  1.00 50.27 ? 143 THR B CG2 1 
ATOM   3464 N  N   . ASN B 1 155 ? -21.226 -29.806 18.444  1.00 47.79 ? 144 ASN B N   1 
ATOM   3465 C  CA  . ASN B 1 155 ? -20.810 -30.872 19.348  1.00 40.99 ? 144 ASN B CA  1 
ATOM   3466 C  C   . ASN B 1 155 ? -20.800 -30.454 20.812  1.00 46.58 ? 144 ASN B C   1 
ATOM   3467 O  O   . ASN B 1 155 ? -20.313 -31.222 21.648  1.00 49.20 ? 144 ASN B O   1 
ATOM   3468 C  CB  . ASN B 1 155 ? -19.417 -31.373 18.962  1.00 46.97 ? 144 ASN B CB  1 
ATOM   3469 C  CG  . ASN B 1 155 ? -19.414 -32.154 17.655  1.00 56.62 ? 144 ASN B CG  1 
ATOM   3470 O  OD1 . ASN B 1 155 ? -20.468 -32.464 17.097  1.00 56.45 ? 144 ASN B OD1 1 
ATOM   3471 N  ND2 . ASN B 1 155 ? -18.222 -32.469 17.159  1.00 62.14 ? 144 ASN B ND2 1 
ATOM   3472 N  N   . GLY B 1 156 ? -21.294 -29.266 21.148  1.00 45.56 ? 145 GLY B N   1 
ATOM   3473 C  CA  . GLY B 1 156 ? -21.441 -28.866 22.533  1.00 46.85 ? 145 GLY B CA  1 
ATOM   3474 C  C   . GLY B 1 156 ? -20.563 -27.729 23.029  1.00 44.64 ? 145 GLY B C   1 
ATOM   3475 O  O   . GLY B 1 156 ? -20.574 -27.446 24.231  1.00 47.74 ? 145 GLY B O   1 
ATOM   3476 N  N   . ALA B 1 157 ? -19.803 -27.073 22.167  1.00 44.13 ? 146 ALA B N   1 
ATOM   3477 C  CA  . ALA B 1 157 ? -19.067 -25.893 22.586  1.00 37.23 ? 146 ALA B CA  1 
ATOM   3478 C  C   . ALA B 1 157 ? -19.970 -24.675 22.472  1.00 42.45 ? 146 ALA B C   1 
ATOM   3479 O  O   . ALA B 1 157 ? -20.803 -24.577 21.558  1.00 39.42 ? 146 ALA B O   1 
ATOM   3480 C  CB  . ALA B 1 157 ? -17.805 -25.696 21.753  1.00 30.66 ? 146 ALA B CB  1 
ATOM   3481 N  N   . HIS B 1 158 ? -19.819 -23.762 23.434  1.00 35.98 ? 147 HIS B N   1 
ATOM   3482 C  CA  . HIS B 1 158 ? -20.657 -22.575 23.486  1.00 29.55 ? 147 HIS B CA  1 
ATOM   3483 C  C   . HIS B 1 158 ? -20.180 -21.530 22.487  1.00 35.66 ? 147 HIS B C   1 
ATOM   3484 O  O   . HIS B 1 158 ? -20.995 -20.741 21.998  1.00 36.04 ? 147 HIS B O   1 
ATOM   3485 C  CB  . HIS B 1 158 ? -20.682 -22.047 24.926  1.00 25.46 ? 147 HIS B CB  1 
ATOM   3486 C  CG  . HIS B 1 158 ? -21.502 -20.813 25.125  1.00 35.00 ? 147 HIS B CG  1 
ATOM   3487 N  ND1 . HIS B 1 158 ? -22.828 -20.726 24.760  1.00 40.39 ? 147 HIS B ND1 1 
ATOM   3488 C  CD2 . HIS B 1 158 ? -21.175 -19.602 25.641  1.00 36.49 ? 147 HIS B CD2 1 
ATOM   3489 C  CE1 . HIS B 1 158 ? -23.284 -19.517 25.046  1.00 38.53 ? 147 HIS B CE1 1 
ATOM   3490 N  NE2 . HIS B 1 158 ? -22.300 -18.814 25.576  1.00 35.12 ? 147 HIS B NE2 1 
ATOM   3491 N  N   . SER B 1 159 ? -18.885 -21.542 22.141  1.00 39.16 ? 148 SER B N   1 
ATOM   3492 C  CA  . SER B 1 159 ? -18.300 -20.597 21.188  1.00 39.72 ? 148 SER B CA  1 
ATOM   3493 C  C   . SER B 1 159 ? -17.071 -21.199 20.506  1.00 40.68 ? 148 SER B C   1 
ATOM   3494 O  O   . SER B 1 159 ? -16.484 -22.183 20.969  1.00 36.51 ? 148 SER B O   1 
ATOM   3495 C  CB  . SER B 1 159 ? -17.903 -19.272 21.856  1.00 37.62 ? 148 SER B CB  1 
ATOM   3496 O  OG  . SER B 1 159 ? -17.113 -19.513 23.008  1.00 40.42 ? 148 SER B OG  1 
ATOM   3497 N  N   . ALA B 1 160 ? -16.681 -20.565 19.399  1.00 38.83 ? 149 ALA B N   1 
ATOM   3498 C  CA  . ALA B 1 160 ? -15.558 -20.979 18.570  1.00 30.63 ? 149 ALA B CA  1 
ATOM   3499 C  C   . ALA B 1 160 ? -15.186 -19.809 17.665  1.00 33.79 ? 149 ALA B C   1 
ATOM   3500 O  O   . ALA B 1 160 ? -16.009 -18.936 17.378  1.00 33.04 ? 149 ALA B O   1 
ATOM   3501 C  CB  . ALA B 1 160 ? -15.892 -22.227 17.746  1.00 26.02 ? 149 ALA B CB  1 
ATOM   3502 N  N   . PHE B 1 161 ? -13.930 -19.788 17.231  1.00 34.53 ? 150 PHE B N   1 
ATOM   3503 C  CA  . PHE B 1 161 ? -13.414 -18.703 16.405  1.00 28.51 ? 150 PHE B CA  1 
ATOM   3504 C  C   . PHE B 1 161 ? -12.855 -19.288 15.116  1.00 33.13 ? 150 PHE B C   1 
ATOM   3505 O  O   . PHE B 1 161 ? -11.946 -20.129 15.151  1.00 35.67 ? 150 PHE B O   1 
ATOM   3506 C  CB  . PHE B 1 161 ? -12.347 -17.889 17.154  1.00 31.11 ? 150 PHE B CB  1 
ATOM   3507 C  CG  . PHE B 1 161 ? -11.801 -16.722 16.359  1.00 35.31 ? 150 PHE B CG  1 
ATOM   3508 C  CD1 . PHE B 1 161 ? -12.649 -15.917 15.598  1.00 34.03 ? 150 PHE B CD1 1 
ATOM   3509 C  CD2 . PHE B 1 161 ? -10.449 -16.439 16.355  1.00 26.90 ? 150 PHE B CD2 1 
ATOM   3510 C  CE1 . PHE B 1 161 ? -12.144 -14.874 14.861  1.00 27.93 ? 150 PHE B CE1 1 
ATOM   3511 C  CE2 . PHE B 1 161 ? -9.956  -15.397 15.627  1.00 22.33 ? 150 PHE B CE2 1 
ATOM   3512 C  CZ  . PHE B 1 161 ? -10.792 -14.622 14.882  1.00 25.82 ? 150 PHE B CZ  1 
ATOM   3513 N  N   . ALA B 1 162 ? -13.417 -18.858 13.983  1.00 30.97 ? 151 ALA B N   1 
ATOM   3514 C  CA  . ALA B 1 162 ? -12.946 -19.241 12.655  1.00 26.13 ? 151 ALA B CA  1 
ATOM   3515 C  C   . ALA B 1 162 ? -12.025 -18.132 12.146  1.00 30.31 ? 151 ALA B C   1 
ATOM   3516 O  O   . ALA B 1 162 ? -12.482 -17.061 11.740  1.00 33.45 ? 151 ALA B O   1 
ATOM   3517 C  CB  . ALA B 1 162 ? -14.121 -19.470 11.710  1.00 27.20 ? 151 ALA B CB  1 
ATOM   3518 N  N   . LEU B 1 163 ? -10.721 -18.382 12.162  1.00 28.86 ? 152 LEU B N   1 
ATOM   3519 C  CA  . LEU B 1 163 ? -9.765  -17.398 11.669  1.00 27.73 ? 152 LEU B CA  1 
ATOM   3520 C  C   . LEU B 1 163 ? -9.650  -17.557 10.154  1.00 31.43 ? 152 LEU B C   1 
ATOM   3521 O  O   . LEU B 1 163 ? -8.675  -18.092 9.624   1.00 34.70 ? 152 LEU B O   1 
ATOM   3522 C  CB  . LEU B 1 163 ? -8.426  -17.566 12.371  1.00 26.20 ? 152 LEU B CB  1 
ATOM   3523 C  CG  . LEU B 1 163 ? -7.370  -16.501 12.087  1.00 32.66 ? 152 LEU B CG  1 
ATOM   3524 C  CD1 . LEU B 1 163 ? -7.997  -15.137 11.991  1.00 28.78 ? 152 LEU B CD1 1 
ATOM   3525 C  CD2 . LEU B 1 163 ? -6.271  -16.509 13.135  1.00 36.47 ? 152 LEU B CD2 1 
ATOM   3526 N  N   . CYS B 1 164 ? -10.669 -17.067 9.444   1.00 29.87 ? 153 CYS B N   1 
ATOM   3527 C  CA  . CYS B 1 164 ? -10.748 -17.240 7.996   1.00 32.80 ? 153 CYS B CA  1 
ATOM   3528 C  C   . CYS B 1 164 ? -9.913  -16.198 7.266   1.00 31.37 ? 153 CYS B C   1 
ATOM   3529 O  O   . CYS B 1 164 ? -9.983  -15.005 7.574   1.00 26.12 ? 153 CYS B O   1 
ATOM   3530 C  CB  . CYS B 1 164 ? -12.193 -17.129 7.508   1.00 30.26 ? 153 CYS B CB  1 
ATOM   3531 S  SG  . CYS B 1 164 ? -13.340 -18.298 8.194   1.00 28.66 ? 153 CYS B SG  1 
ATOM   3532 N  N   . ARG B 1 165 ? -9.138  -16.650 6.279   1.00 29.85 ? 154 ARG B N   1 
ATOM   3533 C  CA  . ARG B 1 165 ? -8.657  -15.766 5.242   1.00 33.35 ? 154 ARG B CA  1 
ATOM   3534 C  C   . ARG B 1 165 ? -8.735  -16.594 3.963   1.00 35.80 ? 154 ARG B C   1 
ATOM   3535 O  O   . ARG B 1 165 ? -8.350  -17.780 3.974   1.00 38.89 ? 154 ARG B O   1 
ATOM   3536 C  CB  . ARG B 1 165 ? -7.237  -15.229 5.465   1.00 35.23 ? 154 ARG B CB  1 
ATOM   3537 C  CG  . ARG B 1 165 ? -7.129  -13.691 5.260   1.00 55.29 ? 154 ARG B CG  1 
ATOM   3538 C  CD  . ARG B 1 165 ? -5.807  -13.236 4.595   1.00 62.35 ? 154 ARG B CD  1 
ATOM   3539 N  NE  . ARG B 1 165 ? -5.634  -11.781 4.644   1.00 87.34 ? 154 ARG B NE  1 
ATOM   3540 C  CZ  . ARG B 1 165 ? -4.702  -11.099 3.982   1.00 82.33 ? 154 ARG B CZ  1 
ATOM   3541 N  NH1 . ARG B 1 165 ? -3.876  -11.697 3.136   1.00 77.89 ? 154 ARG B NH1 1 
ATOM   3542 N  NH2 . ARG B 1 165 ? -4.594  -9.783  4.178   1.00 59.73 ? 154 ARG B NH2 1 
ATOM   3543 N  N   . PRO B 1 166 ? -9.269  -16.039 2.857   1.00 34.33 ? 155 PRO B N   1 
ATOM   3544 C  CA  . PRO B 1 166 ? -9.902  -14.719 2.701   1.00 27.78 ? 155 PRO B CA  1 
ATOM   3545 C  C   . PRO B 1 166 ? -11.265 -14.593 3.389   1.00 30.68 ? 155 PRO B C   1 
ATOM   3546 O  O   . PRO B 1 166 ? -11.935 -15.589 3.640   1.00 33.19 ? 155 PRO B O   1 
ATOM   3547 C  CB  . PRO B 1 166 ? -10.035 -14.596 1.170   1.00 27.61 ? 155 PRO B CB  1 
ATOM   3548 C  CG  . PRO B 1 166 ? -10.139 -15.983 0.682   1.00 25.10 ? 155 PRO B CG  1 
ATOM   3549 C  CD  . PRO B 1 166 ? -9.207  -16.763 1.571   1.00 30.59 ? 155 PRO B CD  1 
ATOM   3550 N  N   . PRO B 1 167 ? -11.736 -13.367 3.661   1.00 33.54 ? 156 PRO B N   1 
ATOM   3551 C  CA  . PRO B 1 167 ? -13.066 -13.198 4.283   1.00 28.53 ? 156 PRO B CA  1 
ATOM   3552 C  C   . PRO B 1 167 ? -14.208 -13.595 3.360   1.00 28.08 ? 156 PRO B C   1 
ATOM   3553 O  O   . PRO B 1 167 ? -13.964 -14.032 2.233   1.00 30.35 ? 156 PRO B O   1 
ATOM   3554 C  CB  . PRO B 1 167 ? -13.110 -11.697 4.590   1.00 33.36 ? 156 PRO B CB  1 
ATOM   3555 C  CG  . PRO B 1 167 ? -12.290 -11.097 3.469   1.00 31.33 ? 156 PRO B CG  1 
ATOM   3556 C  CD  . PRO B 1 167 ? -11.152 -12.075 3.243   1.00 29.56 ? 156 PRO B CD  1 
ATOM   3557 N  N   . GLY B 1 168 ? -15.458 -13.412 3.788   1.00 31.26 ? 157 GLY B N   1 
ATOM   3558 C  CA  . GLY B 1 168 ? -16.556 -13.912 2.981   1.00 29.29 ? 157 GLY B CA  1 
ATOM   3559 C  C   . GLY B 1 168 ? -17.801 -13.069 2.775   1.00 33.55 ? 157 GLY B C   1 
ATOM   3560 O  O   . GLY B 1 168 ? -18.587 -13.376 1.872   1.00 30.77 ? 157 GLY B O   1 
ATOM   3561 N  N   . HIS B 1 169 ? -18.018 -12.018 3.570   1.00 31.34 ? 158 HIS B N   1 
ATOM   3562 C  CA  . HIS B 1 169 ? -19.361 -11.438 3.625   1.00 27.71 ? 158 HIS B CA  1 
ATOM   3563 C  C   . HIS B 1 169 ? -19.711 -10.556 2.427   1.00 30.91 ? 158 HIS B C   1 
ATOM   3564 O  O   . HIS B 1 169 ? -20.824 -10.025 2.378   1.00 30.47 ? 158 HIS B O   1 
ATOM   3565 C  CB  . HIS B 1 169 ? -19.540 -10.643 4.917   1.00 30.91 ? 158 HIS B CB  1 
ATOM   3566 C  CG  . HIS B 1 169 ? -18.725 -9.385  4.982   1.00 35.05 ? 158 HIS B CG  1 
ATOM   3567 N  ND1 . HIS B 1 169 ? -18.975 -8.386  5.899   1.00 35.22 ? 158 HIS B ND1 1 
ATOM   3568 C  CD2 . HIS B 1 169 ? -17.665 -8.964  4.249   1.00 33.27 ? 158 HIS B CD2 1 
ATOM   3569 C  CE1 . HIS B 1 169 ? -18.108 -7.404  5.728   1.00 33.38 ? 158 HIS B CE1 1 
ATOM   3570 N  NE2 . HIS B 1 169 ? -17.303 -7.730  4.732   1.00 36.82 ? 158 HIS B NE2 1 
ATOM   3571 N  N   . HIS B 1 170 ? -18.807 -10.359 1.471   1.00 29.65 ? 159 HIS B N   1 
ATOM   3572 C  CA  . HIS B 1 170 ? -19.188 -9.650  0.261   1.00 25.70 ? 159 HIS B CA  1 
ATOM   3573 C  C   . HIS B 1 170 ? -19.598 -10.600 -0.861  1.00 31.64 ? 159 HIS B C   1 
ATOM   3574 O  O   . HIS B 1 170 ? -20.066 -10.131 -1.906  1.00 31.84 ? 159 HIS B O   1 
ATOM   3575 C  CB  . HIS B 1 170 ? -18.048 -8.743  -0.227  1.00 25.02 ? 159 HIS B CB  1 
ATOM   3576 C  CG  . HIS B 1 170 ? -17.733 -7.602  0.690   1.00 29.43 ? 159 HIS B CG  1 
ATOM   3577 N  ND1 . HIS B 1 170 ? -18.640 -6.604  0.986   1.00 32.40 ? 159 HIS B ND1 1 
ATOM   3578 C  CD2 . HIS B 1 170 ? -16.600 -7.292  1.364   1.00 30.40 ? 159 HIS B CD2 1 
ATOM   3579 C  CE1 . HIS B 1 170 ? -18.087 -5.743  1.820   1.00 32.56 ? 159 HIS B CE1 1 
ATOM   3580 N  NE2 . HIS B 1 170 ? -16.848 -6.136  2.065   1.00 33.96 ? 159 HIS B NE2 1 
ATOM   3581 N  N   . ALA B 1 171 ? -19.448 -11.916 -0.679  1.00 29.02 ? 160 ALA B N   1 
ATOM   3582 C  CA  . ALA B 1 171 ? -19.833 -12.877 -1.709  1.00 30.86 ? 160 ALA B CA  1 
ATOM   3583 C  C   . ALA B 1 171 ? -21.301 -13.257 -1.547  1.00 31.41 ? 160 ALA B C   1 
ATOM   3584 O  O   . ALA B 1 171 ? -21.721 -13.689 -0.469  1.00 30.80 ? 160 ALA B O   1 
ATOM   3585 C  CB  . ALA B 1 171 ? -18.950 -14.120 -1.668  1.00 24.94 ? 160 ALA B CB  1 
ATOM   3586 N  N   . ALA B 1 172 ? -22.082 -13.075 -2.611  1.00 29.72 ? 161 ALA B N   1 
ATOM   3587 C  CA  . ALA B 1 172 ? -23.449 -13.579 -2.650  1.00 36.08 ? 161 ALA B CA  1 
ATOM   3588 C  C   . ALA B 1 172 ? -23.433 -15.046 -3.109  1.00 34.89 ? 161 ALA B C   1 
ATOM   3589 O  O   . ALA B 1 172 ? -22.381 -15.683 -3.205  1.00 36.02 ? 161 ALA B O   1 
ATOM   3590 C  CB  . ALA B 1 172 ? -24.310 -12.686 -3.537  1.00 32.31 ? 161 ALA B CB  1 
ATOM   3591 N  N   . SER B 1 173 ? -24.606 -15.615 -3.380  1.00 29.62 ? 162 SER B N   1 
ATOM   3592 C  CA  . SER B 1 173 ? -24.651 -17.009 -3.812  1.00 34.34 ? 162 SER B CA  1 
ATOM   3593 C  C   . SER B 1 173 ? -23.740 -17.267 -5.015  1.00 34.15 ? 162 SER B C   1 
ATOM   3594 O  O   . SER B 1 173 ? -23.049 -18.289 -5.069  1.00 32.22 ? 162 SER B O   1 
ATOM   3595 C  CB  . SER B 1 173 ? -26.087 -17.415 -4.140  1.00 32.36 ? 162 SER B CB  1 
ATOM   3596 O  OG  . SER B 1 173 ? -26.110 -18.628 -4.874  1.00 36.43 ? 162 SER B OG  1 
ATOM   3597 N  N   . ASP B 1 174 ? -23.722 -16.359 -5.988  1.00 31.32 ? 163 ASP B N   1 
ATOM   3598 C  CA  . ASP B 1 174 ? -22.832 -16.524 -7.130  1.00 32.32 ? 163 ASP B CA  1 
ATOM   3599 C  C   . ASP B 1 174 ? -22.323 -15.162 -7.610  1.00 34.01 ? 163 ASP B C   1 
ATOM   3600 O  O   . ASP B 1 174 ? -22.251 -14.896 -8.815  1.00 34.55 ? 163 ASP B O   1 
ATOM   3601 C  CB  . ASP B 1 174 ? -23.505 -17.311 -8.267  1.00 29.12 ? 163 ASP B CB  1 
ATOM   3602 C  CG  . ASP B 1 174 ? -24.820 -16.677 -8.753  1.00 34.34 ? 163 ASP B CG  1 
ATOM   3603 O  OD1 . ASP B 1 174 ? -25.086 -15.487 -8.439  1.00 24.40 ? 163 ASP B OD1 1 
ATOM   3604 O  OD2 . ASP B 1 174 ? -25.594 -17.385 -9.456  1.00 33.35 ? 163 ASP B OD2 1 
ATOM   3605 N  N   . VAL B 1 175 ? -21.979 -14.281 -6.672  1.00 30.09 ? 164 VAL B N   1 
ATOM   3606 C  CA  . VAL B 1 175 ? -21.240 -13.060 -6.979  1.00 29.41 ? 164 VAL B CA  1 
ATOM   3607 C  C   . VAL B 1 175 ? -20.083 -12.928 -5.997  1.00 31.24 ? 164 VAL B C   1 
ATOM   3608 O  O   . VAL B 1 175 ? -20.213 -13.235 -4.808  1.00 31.50 ? 164 VAL B O   1 
ATOM   3609 C  CB  . VAL B 1 175 ? -22.116 -11.793 -6.933  1.00 33.51 ? 164 VAL B CB  1 
ATOM   3610 C  CG1 . VAL B 1 175 ? -21.288 -10.579 -7.403  1.00 26.90 ? 164 VAL B CG1 1 
ATOM   3611 C  CG2 . VAL B 1 175 ? -23.417 -11.968 -7.758  1.00 33.38 ? 164 VAL B CG2 1 
ATOM   3612 N  N   . MET B 1 176 ? -18.957 -12.458 -6.498  1.00 33.36 ? 165 MET B N   1 
ATOM   3613 C  CA  . MET B 1 176 ? -17.730 -12.324 -5.732  1.00 35.13 ? 165 MET B CA  1 
ATOM   3614 C  C   . MET B 1 176 ? -17.270 -10.872 -5.806  1.00 31.69 ? 165 MET B C   1 
ATOM   3615 O  O   . MET B 1 176 ? -17.602 -10.150 -6.745  1.00 30.67 ? 165 MET B O   1 
ATOM   3616 C  CB  . MET B 1 176 ? -16.710 -13.349 -6.284  1.00 32.62 ? 165 MET B CB  1 
ATOM   3617 C  CG  . MET B 1 176 ? -16.054 -12.927 -7.583  1.00 34.69 ? 165 MET B CG  1 
ATOM   3618 S  SD  . MET B 1 176 ? -14.564 -13.810 -8.047  1.00 30.53 ? 165 MET B SD  1 
ATOM   3619 C  CE  . MET B 1 176 ? -15.337 -15.260 -8.805  1.00 31.01 ? 165 MET B CE  1 
ATOM   3620 N  N   . GLY B 1 177 ? -16.567 -10.435 -4.776  1.00 31.16 ? 166 GLY B N   1 
ATOM   3621 C  CA  . GLY B 1 177 ? -15.942 -9.128  -4.761  1.00 27.49 ? 166 GLY B CA  1 
ATOM   3622 C  C   . GLY B 1 177 ? -15.559 -8.755  -3.351  1.00 32.23 ? 166 GLY B C   1 
ATOM   3623 O  O   . GLY B 1 177 ? -15.987 -9.379  -2.377  1.00 27.93 ? 166 GLY B O   1 
ATOM   3624 N  N   . GLY B 1 178 ? -14.739 -7.711  -3.252  1.00 32.67 ? 167 GLY B N   1 
ATOM   3625 C  CA  . GLY B 1 178 ? -14.305 -7.240  -1.948  1.00 29.71 ? 167 GLY B CA  1 
ATOM   3626 C  C   . GLY B 1 178 ? -13.396 -8.204  -1.219  1.00 31.90 ? 167 GLY B C   1 
ATOM   3627 O  O   . GLY B 1 178 ? -13.465 -8.295  0.008   1.00 33.32 ? 167 GLY B O   1 
ATOM   3628 N  N   A TYR B 1 179 ? -12.525 -8.911  -1.951  0.54 32.51 ? 168 TYR B N   1 
ATOM   3629 N  N   B TYR B 1 179 ? -12.551 -8.927  -1.957  0.46 33.35 ? 168 TYR B N   1 
ATOM   3630 C  CA  A TYR B 1 179 ? -11.635 -9.972  -1.450  0.54 31.82 ? 168 TYR B CA  1 
ATOM   3631 C  CA  B TYR B 1 179 ? -11.650 -9.937  -1.404  0.46 32.11 ? 168 TYR B CA  1 
ATOM   3632 C  C   A TYR B 1 179 ? -12.390 -11.152 -0.846  0.54 32.44 ? 168 TYR B C   1 
ATOM   3633 C  C   B TYR B 1 179 ? -12.420 -11.092 -0.761  0.46 32.03 ? 168 TYR B C   1 
ATOM   3634 O  O   A TYR B 1 179 ? -11.838 -11.891 -0.028  0.54 33.02 ? 168 TYR B O   1 
ATOM   3635 O  O   B TYR B 1 179 ? -11.918 -11.754 0.149   0.46 33.08 ? 168 TYR B O   1 
ATOM   3636 C  CB  A TYR B 1 179 ? -10.614 -9.452  -0.432  0.54 34.42 ? 168 TYR B CB  1 
ATOM   3637 C  CB  B TYR B 1 179 ? -10.654 -9.300  -0.424  0.46 34.42 ? 168 TYR B CB  1 
ATOM   3638 C  CG  A TYR B 1 179 ? -9.365  -10.320 -0.349  0.54 37.29 ? 168 TYR B CG  1 
ATOM   3639 C  CG  B TYR B 1 179 ? -9.602  -8.467  -1.141  0.46 37.61 ? 168 TYR B CG  1 
ATOM   3640 C  CD1 A TYR B 1 179 ? -8.863  -10.962 -1.486  0.54 32.97 ? 168 TYR B CD1 1 
ATOM   3641 C  CD1 B TYR B 1 179 ? -8.433  -9.055  -1.620  0.46 37.38 ? 168 TYR B CD1 1 
ATOM   3642 C  CD2 A TYR B 1 179 ? -8.688  -10.496 0.860   0.54 34.96 ? 168 TYR B CD2 1 
ATOM   3643 C  CD2 B TYR B 1 179 ? -9.800  -7.112  -1.384  0.46 34.26 ? 168 TYR B CD2 1 
ATOM   3644 C  CE1 A TYR B 1 179 ? -7.727  -11.746 -1.423  0.54 31.77 ? 168 TYR B CE1 1 
ATOM   3645 C  CE1 B TYR B 1 179 ? -7.481  -8.315  -2.290  0.46 34.34 ? 168 TYR B CE1 1 
ATOM   3646 C  CE2 A TYR B 1 179 ? -7.549  -11.282 0.934   0.54 37.68 ? 168 TYR B CE2 1 
ATOM   3647 C  CE2 B TYR B 1 179 ? -8.849  -6.368  -2.064  0.46 36.32 ? 168 TYR B CE2 1 
ATOM   3648 C  CZ  A TYR B 1 179 ? -7.075  -11.907 -0.212  0.54 40.89 ? 168 TYR B CZ  1 
ATOM   3649 C  CZ  B TYR B 1 179 ? -7.694  -6.979  -2.513  0.46 35.26 ? 168 TYR B CZ  1 
ATOM   3650 O  OH  A TYR B 1 179 ? -5.940  -12.690 -0.147  0.54 43.68 ? 168 TYR B OH  1 
ATOM   3651 O  OH  B TYR B 1 179 ? -6.739  -6.256  -3.187  0.46 42.02 ? 168 TYR B OH  1 
ATOM   3652 N  N   . CYS B 1 180 ? -13.638 -11.358 -1.248  1.00 30.82 ? 169 CYS B N   1 
ATOM   3653 C  CA  . CYS B 1 180 ? -14.474 -12.441 -0.748  1.00 30.63 ? 169 CYS B CA  1 
ATOM   3654 C  C   . CYS B 1 180 ? -14.925 -13.314 -1.916  1.00 30.60 ? 169 CYS B C   1 
ATOM   3655 O  O   . CYS B 1 180 ? -15.515 -12.816 -2.878  1.00 27.45 ? 169 CYS B O   1 
ATOM   3656 C  CB  . CYS B 1 180 ? -15.698 -11.893 -0.004  1.00 29.99 ? 169 CYS B CB  1 
ATOM   3657 S  SG  . CYS B 1 180 ? -15.325 -10.773 1.352   1.00 28.26 ? 169 CYS B SG  1 
ATOM   3658 N  N   . TYR B 1 181 ? -14.670 -14.617 -1.819  1.00 32.64 ? 170 TYR B N   1 
ATOM   3659 C  CA  . TYR B 1 181 ? -15.031 -15.567 -2.871  1.00 32.56 ? 170 TYR B CA  1 
ATOM   3660 C  C   . TYR B 1 181 ? -16.101 -16.565 -2.454  1.00 31.61 ? 170 TYR B C   1 
ATOM   3661 O  O   . TYR B 1 181 ? -16.980 -16.903 -3.255  1.00 28.71 ? 170 TYR B O   1 
ATOM   3662 C  CB  . TYR B 1 181 ? -13.787 -16.329 -3.336  1.00 29.42 ? 170 TYR B CB  1 
ATOM   3663 C  CG  . TYR B 1 181 ? -12.610 -15.438 -3.665  1.00 30.03 ? 170 TYR B CG  1 
ATOM   3664 C  CD1 . TYR B 1 181 ? -11.729 -15.014 -2.670  1.00 27.72 ? 170 TYR B CD1 1 
ATOM   3665 C  CD2 . TYR B 1 181 ? -12.380 -15.022 -4.968  1.00 30.07 ? 170 TYR B CD2 1 
ATOM   3666 C  CE1 . TYR B 1 181 ? -10.662 -14.204 -2.965  1.00 26.19 ? 170 TYR B CE1 1 
ATOM   3667 C  CE2 . TYR B 1 181 ? -11.314 -14.207 -5.271  1.00 34.35 ? 170 TYR B CE2 1 
ATOM   3668 C  CZ  . TYR B 1 181 ? -10.458 -13.804 -4.265  1.00 29.48 ? 170 TYR B CZ  1 
ATOM   3669 O  OH  . TYR B 1 181 ? -9.394  -13.007 -4.577  1.00 32.98 ? 170 TYR B OH  1 
ATOM   3670 N  N   . LEU B 1 182 ? -16.038 -17.051 -1.222  1.00 24.95 ? 171 LEU B N   1 
ATOM   3671 C  CA  . LEU B 1 182 ? -17.034 -17.931 -0.658  1.00 22.16 ? 171 LEU B CA  1 
ATOM   3672 C  C   . LEU B 1 182 ? -17.465 -17.309 0.649   1.00 30.25 ? 171 LEU B C   1 
ATOM   3673 O  O   . LEU B 1 182 ? -16.617 -16.855 1.420   1.00 32.10 ? 171 LEU B O   1 
ATOM   3674 C  CB  . LEU B 1 182 ? -16.467 -19.334 -0.424  1.00 24.85 ? 171 LEU B CB  1 
ATOM   3675 C  CG  . LEU B 1 182 ? -15.945 -20.063 -1.664  1.00 24.26 ? 171 LEU B CG  1 
ATOM   3676 C  CD1 . LEU B 1 182 ? -14.948 -21.139 -1.324  1.00 21.69 ? 171 LEU B CD1 1 
ATOM   3677 C  CD2 . LEU B 1 182 ? -17.112 -20.671 -2.402  1.00 27.72 ? 171 LEU B CD2 1 
ATOM   3678 N  N   . ASN B 1 183 ? -18.775 -17.290 0.910   1.00 31.05 ? 172 ASN B N   1 
ATOM   3679 C  CA  . ASN B 1 183 ? -19.280 -16.644 2.125   1.00 31.29 ? 172 ASN B CA  1 
ATOM   3680 C  C   . ASN B 1 183 ? -19.137 -17.573 3.329   1.00 29.99 ? 172 ASN B C   1 
ATOM   3681 O  O   . ASN B 1 183 ? -20.047 -18.328 3.659   1.00 32.00 ? 172 ASN B O   1 
ATOM   3682 C  CB  . ASN B 1 183 ? -20.723 -16.213 1.937   1.00 28.51 ? 172 ASN B CB  1 
ATOM   3683 C  CG  . ASN B 1 183 ? -21.139 -15.162 2.941   1.00 30.17 ? 172 ASN B CG  1 
ATOM   3684 O  OD1 . ASN B 1 183 ? -21.153 -15.411 4.142   1.00 30.93 ? 172 ASN B OD1 1 
ATOM   3685 N  ND2 . ASN B 1 183 ? -21.457 -13.970 2.455   1.00 31.78 ? 172 ASN B ND2 1 
ATOM   3686 N  N   . ASN B 1 184 ? -17.998 -17.466 4.027   1.00 29.08 ? 173 ASN B N   1 
ATOM   3687 C  CA  . ASN B 1 184 ? -17.698 -18.336 5.166   1.00 30.53 ? 173 ASN B CA  1 
ATOM   3688 C  C   . ASN B 1 184 ? -18.810 -18.331 6.202   1.00 30.47 ? 173 ASN B C   1 
ATOM   3689 O  O   . ASN B 1 184 ? -19.333 -19.392 6.570   1.00 32.60 ? 173 ASN B O   1 
ATOM   3690 C  CB  . ASN B 1 184 ? -16.380 -17.925 5.824   1.00 27.55 ? 173 ASN B CB  1 
ATOM   3691 C  CG  . ASN B 1 184 ? -15.236 -17.931 4.853   1.00 32.96 ? 173 ASN B CG  1 
ATOM   3692 O  OD1 . ASN B 1 184 ? -15.114 -18.841 4.026   1.00 30.53 ? 173 ASN B OD1 1 
ATOM   3693 N  ND2 . ASN B 1 184 ? -14.396 -16.902 4.923   1.00 36.50 ? 173 ASN B ND2 1 
ATOM   3694 N  N   . ALA B 1 185 ? -19.162 -17.136 6.694   1.00 24.27 ? 174 ALA B N   1 
ATOM   3695 C  CA  . ALA B 1 185 ? -20.208 -16.990 7.708   1.00 26.67 ? 174 ALA B CA  1 
ATOM   3696 C  C   . ALA B 1 185 ? -21.532 -17.621 7.273   1.00 32.07 ? 174 ALA B C   1 
ATOM   3697 O  O   . ALA B 1 185 ? -22.196 -18.296 8.073   1.00 34.38 ? 174 ALA B O   1 
ATOM   3698 C  CB  . ALA B 1 185 ? -20.413 -15.510 8.030   1.00 25.68 ? 174 ALA B CB  1 
ATOM   3699 N  N   . ALA B 1 186 ? -21.941 -17.406 6.016   1.00 29.88 ? 175 ALA B N   1 
ATOM   3700 C  CA  . ALA B 1 186 ? -23.235 -17.922 5.572   1.00 32.56 ? 175 ALA B CA  1 
ATOM   3701 C  C   . ALA B 1 186 ? -23.215 -19.438 5.413   1.00 35.65 ? 175 ALA B C   1 
ATOM   3702 O  O   . ALA B 1 186 ? -24.250 -20.095 5.585   1.00 32.35 ? 175 ALA B O   1 
ATOM   3703 C  CB  . ALA B 1 186 ? -23.651 -17.262 4.257   1.00 26.74 ? 175 ALA B CB  1 
ATOM   3704 N  N   . ILE B 1 187 ? -22.058 -20.006 5.063   1.00 35.04 ? 176 ILE B N   1 
ATOM   3705 C  CA  . ILE B 1 187 ? -21.956 -21.450 4.922   1.00 32.75 ? 176 ILE B CA  1 
ATOM   3706 C  C   . ILE B 1 187 ? -22.128 -22.114 6.281   1.00 39.52 ? 176 ILE B C   1 
ATOM   3707 O  O   . ILE B 1 187 ? -22.829 -23.136 6.416   1.00 27.04 ? 176 ILE B O   1 
ATOM   3708 C  CB  . ILE B 1 187 ? -20.612 -21.813 4.264   1.00 30.51 ? 176 ILE B CB  1 
ATOM   3709 C  CG1 . ILE B 1 187 ? -20.659 -21.484 2.769   1.00 28.95 ? 176 ILE B CG1 1 
ATOM   3710 C  CG2 . ILE B 1 187 ? -20.236 -23.299 4.536   1.00 28.71 ? 176 ILE B CG2 1 
ATOM   3711 C  CD1 . ILE B 1 187 ? -19.352 -20.978 2.200   1.00 28.30 ? 176 ILE B CD1 1 
ATOM   3712 N  N   . ALA B 1 188 ? -21.504 -21.512 7.311   1.00 35.73 ? 177 ALA B N   1 
ATOM   3713 C  CA  . ALA B 1 188 ? -21.588 -22.016 8.674   1.00 27.00 ? 177 ALA B CA  1 
ATOM   3714 C  C   . ALA B 1 188 ? -22.968 -21.767 9.258   1.00 34.58 ? 177 ALA B C   1 
ATOM   3715 O  O   . ALA B 1 188 ? -23.486 -22.599 10.014  1.00 39.06 ? 177 ALA B O   1 
ATOM   3716 C  CB  . ALA B 1 188 ? -20.507 -21.368 9.532   1.00 22.34 ? 177 ALA B CB  1 
ATOM   3717 N  N   . ALA B 1 189 ? -23.578 -20.628 8.920   1.00 32.55 ? 178 ALA B N   1 
ATOM   3718 C  CA  . ALA B 1 189 ? -24.966 -20.395 9.296   1.00 33.40 ? 178 ALA B CA  1 
ATOM   3719 C  C   . ALA B 1 189 ? -25.850 -21.536 8.820   1.00 34.92 ? 178 ALA B C   1 
ATOM   3720 O  O   . ALA B 1 189 ? -26.613 -22.116 9.601   1.00 39.98 ? 178 ALA B O   1 
ATOM   3721 C  CB  . ALA B 1 189 ? -25.462 -19.067 8.718   1.00 35.20 ? 178 ALA B CB  1 
ATOM   3722 N  N   . GLN B 1 190 ? -25.746 -21.885 7.536   1.00 34.82 ? 179 GLN B N   1 
ATOM   3723 C  CA  . GLN B 1 190 ? -26.627 -22.907 6.971   1.00 37.88 ? 179 GLN B CA  1 
ATOM   3724 C  C   . GLN B 1 190 ? -26.330 -24.294 7.547   1.00 37.17 ? 179 GLN B C   1 
ATOM   3725 O  O   . GLN B 1 190 ? -27.242 -25.106 7.717   1.00 34.62 ? 179 GLN B O   1 
ATOM   3726 C  CB  . GLN B 1 190 ? -26.499 -22.897 5.449   1.00 26.39 ? 179 GLN B CB  1 
ATOM   3727 C  CG  . GLN B 1 190 ? -27.325 -23.928 4.737   1.00 31.49 ? 179 GLN B CG  1 
ATOM   3728 C  CD  . GLN B 1 190 ? -28.791 -23.593 4.740   1.00 34.28 ? 179 GLN B CD  1 
ATOM   3729 O  OE1 . GLN B 1 190 ? -29.186 -22.470 4.425   1.00 28.65 ? 179 GLN B OE1 1 
ATOM   3730 N  NE2 . GLN B 1 190 ? -29.617 -24.571 5.095   1.00 38.50 ? 179 GLN B NE2 1 
ATOM   3731 N  N   . ALA B 1 191 ? -25.069 -24.572 7.865   1.00 37.09 ? 180 ALA B N   1 
ATOM   3732 C  CA  . ALA B 1 191 ? -24.735 -25.821 8.525   1.00 35.57 ? 180 ALA B CA  1 
ATOM   3733 C  C   . ALA B 1 191 ? -25.482 -25.957 9.845   1.00 39.34 ? 180 ALA B C   1 
ATOM   3734 O  O   . ALA B 1 191 ? -25.994 -27.035 10.163  1.00 39.92 ? 180 ALA B O   1 
ATOM   3735 C  CB  . ALA B 1 191 ? -23.223 -25.908 8.730   1.00 36.99 ? 180 ALA B CB  1 
ATOM   3736 N  N   . PHE B 1 192 ? -25.565 -24.875 10.626  1.00 39.77 ? 181 PHE B N   1 
ATOM   3737 C  CA  . PHE B 1 192 ? -26.333 -24.926 11.870  1.00 39.56 ? 181 PHE B CA  1 
ATOM   3738 C  C   . PHE B 1 192 ? -27.783 -25.313 11.605  1.00 41.15 ? 181 PHE B C   1 
ATOM   3739 O  O   . PHE B 1 192 ? -28.370 -26.099 12.359  1.00 43.40 ? 181 PHE B O   1 
ATOM   3740 C  CB  . PHE B 1 192 ? -26.270 -23.583 12.597  1.00 35.12 ? 181 PHE B CB  1 
ATOM   3741 C  CG  . PHE B 1 192 ? -25.005 -23.372 13.358  1.00 39.31 ? 181 PHE B CG  1 
ATOM   3742 C  CD1 . PHE B 1 192 ? -24.667 -24.207 14.402  1.00 37.37 ? 181 PHE B CD1 1 
ATOM   3743 C  CD2 . PHE B 1 192 ? -24.142 -22.343 13.017  1.00 38.25 ? 181 PHE B CD2 1 
ATOM   3744 C  CE1 . PHE B 1 192 ? -23.494 -24.028 15.107  1.00 39.13 ? 181 PHE B CE1 1 
ATOM   3745 C  CE2 . PHE B 1 192 ? -22.968 -22.156 13.715  1.00 41.20 ? 181 PHE B CE2 1 
ATOM   3746 C  CZ  . PHE B 1 192 ? -22.644 -23.003 14.769  1.00 43.07 ? 181 PHE B CZ  1 
ATOM   3747 N  N   . ILE B 1 193 ? -28.376 -24.765 10.538  1.00 43.30 ? 182 ILE B N   1 
ATOM   3748 C  CA  . ILE B 1 193 ? -29.737 -25.135 10.148  1.00 41.97 ? 182 ILE B CA  1 
ATOM   3749 C  C   . ILE B 1 193 ? -29.794 -26.608 9.750   1.00 45.41 ? 182 ILE B C   1 
ATOM   3750 O  O   . ILE B 1 193 ? -30.578 -27.388 10.302  1.00 50.99 ? 182 ILE B O   1 
ATOM   3751 C  CB  . ILE B 1 193 ? -30.236 -24.244 9.001   1.00 41.57 ? 182 ILE B CB  1 
ATOM   3752 C  CG1 . ILE B 1 193 ? -30.200 -22.765 9.393   1.00 41.46 ? 182 ILE B CG1 1 
ATOM   3753 C  CG2 . ILE B 1 193 ? -31.618 -24.697 8.569   1.00 43.45 ? 182 ILE B CG2 1 
ATOM   3754 C  CD1 . ILE B 1 193 ? -31.498 -22.219 9.898   1.00 43.79 ? 182 ILE B CD1 1 
ATOM   3755 N  N   . ASP B 1 194 ? -28.961 -27.011 8.782   1.00 35.69 ? 183 ASP B N   1 
ATOM   3756 C  CA  . ASP B 1 194 ? -28.967 -28.400 8.326   1.00 36.54 ? 183 ASP B CA  1 
ATOM   3757 C  C   . ASP B 1 194 ? -28.716 -29.397 9.463   1.00 43.56 ? 183 ASP B C   1 
ATOM   3758 O  O   . ASP B 1 194 ? -29.136 -30.553 9.363   1.00 40.71 ? 183 ASP B O   1 
ATOM   3759 C  CB  . ASP B 1 194 ? -27.937 -28.593 7.205   1.00 27.37 ? 183 ASP B CB  1 
ATOM   3760 C  CG  . ASP B 1 194 ? -28.326 -27.869 5.916   1.00 36.86 ? 183 ASP B CG  1 
ATOM   3761 O  OD1 . ASP B 1 194 ? -29.487 -27.430 5.801   1.00 45.04 ? 183 ASP B OD1 1 
ATOM   3762 O  OD2 . ASP B 1 194 ? -27.479 -27.723 5.012   1.00 35.01 ? 183 ASP B OD2 1 
ATOM   3763 N  N   . GLN B 1 195 ? -28.073 -28.978 10.551  1.00 46.60 ? 184 GLN B N   1 
ATOM   3764 C  CA  . GLN B 1 195 ? -27.790 -29.853 11.677  1.00 40.00 ? 184 GLN B CA  1 
ATOM   3765 C  C   . GLN B 1 195 ? -28.830 -29.730 12.777  1.00 42.43 ? 184 GLN B C   1 
ATOM   3766 O  O   . GLN B 1 195 ? -28.552 -30.075 13.929  1.00 48.71 ? 184 GLN B O   1 
ATOM   3767 C  CB  . GLN B 1 195 ? -26.394 -29.558 12.224  1.00 39.37 ? 184 GLN B CB  1 
ATOM   3768 C  CG  . GLN B 1 195 ? -25.313 -30.418 11.595  1.00 46.71 ? 184 GLN B CG  1 
ATOM   3769 C  CD  . GLN B 1 195 ? -24.042 -29.632 11.297  1.00 52.37 ? 184 GLN B CD  1 
ATOM   3770 O  OE1 . GLN B 1 195 ? -23.428 -29.041 12.188  1.00 58.37 ? 184 GLN B OE1 1 
ATOM   3771 N  NE2 . GLN B 1 195 ? -23.670 -29.582 10.019  1.00 56.71 ? 184 GLN B NE2 1 
ATOM   3772 N  N   . GLY B 1 196 ? -30.011 -29.225 12.462  1.00 44.40 ? 185 GLY B N   1 
ATOM   3773 C  CA  . GLY B 1 196 ? -31.086 -29.278 13.430  1.00 49.75 ? 185 GLY B CA  1 
ATOM   3774 C  C   . GLY B 1 196 ? -31.809 -27.981 13.722  1.00 48.48 ? 185 GLY B C   1 
ATOM   3775 O  O   . GLY B 1 196 ? -33.015 -27.992 13.984  1.00 51.76 ? 185 GLY B O   1 
ATOM   3776 N  N   . HIS B 1 197 ? -31.097 -26.860 13.678  1.00 47.03 ? 186 HIS B N   1 
ATOM   3777 C  CA  . HIS B 1 197 ? -31.649 -25.614 14.192  1.00 46.32 ? 186 HIS B CA  1 
ATOM   3778 C  C   . HIS B 1 197 ? -32.734 -25.052 13.276  1.00 47.27 ? 186 HIS B C   1 
ATOM   3779 O  O   . HIS B 1 197 ? -32.651 -25.131 12.046  1.00 43.37 ? 186 HIS B O   1 
ATOM   3780 C  CB  . HIS B 1 197 ? -30.531 -24.594 14.401  1.00 41.93 ? 186 HIS B CB  1 
ATOM   3781 C  CG  . HIS B 1 197 ? -29.610 -24.946 15.527  1.00 39.02 ? 186 HIS B CG  1 
ATOM   3782 N  ND1 . HIS B 1 197 ? -29.952 -24.770 16.851  1.00 42.01 ? 186 HIS B ND1 1 
ATOM   3783 C  CD2 . HIS B 1 197 ? -28.376 -25.503 15.529  1.00 38.06 ? 186 HIS B CD2 1 
ATOM   3784 C  CE1 . HIS B 1 197 ? -28.960 -25.183 17.619  1.00 41.08 ? 186 HIS B CE1 1 
ATOM   3785 N  NE2 . HIS B 1 197 ? -27.990 -25.629 16.842  1.00 39.55 ? 186 HIS B NE2 1 
ATOM   3786 N  N   . LYS B 1 198 ? -33.771 -24.501 13.903  1.00 48.82 ? 187 LYS B N   1 
ATOM   3787 C  CA  . LYS B 1 198 ? -34.843 -23.814 13.193  1.00 46.26 ? 187 LYS B CA  1 
ATOM   3788 C  C   . LYS B 1 198 ? -34.424 -22.402 12.799  1.00 44.98 ? 187 LYS B C   1 
ATOM   3789 O  O   . LYS B 1 198 ? -34.640 -21.976 11.661  1.00 43.11 ? 187 LYS B O   1 
ATOM   3790 C  CB  . LYS B 1 198 ? -36.091 -23.774 14.084  1.00 56.02 ? 187 LYS B CB  1 
ATOM   3791 C  CG  . LYS B 1 198 ? -37.413 -23.454 13.400  1.00 59.11 ? 187 LYS B CG  1 
ATOM   3792 C  CD  . LYS B 1 198 ? -38.215 -24.713 13.180  1.00 60.08 ? 187 LYS B CD  1 
ATOM   3793 C  CE  . LYS B 1 198 ? -39.088 -25.027 14.378  1.00 65.21 ? 187 LYS B CE  1 
ATOM   3794 N  NZ  . LYS B 1 198 ? -40.000 -26.174 14.093  1.00 74.00 ? 187 LYS B NZ  1 
ATOM   3795 N  N   . ARG B 1 199 ? -33.822 -21.661 13.732  1.00 52.28 ? 188 ARG B N   1 
ATOM   3796 C  CA  . ARG B 1 199 ? -33.531 -20.241 13.562  1.00 47.95 ? 188 ARG B CA  1 
ATOM   3797 C  C   . ARG B 1 199 ? -32.092 -19.929 13.954  1.00 40.24 ? 188 ARG B C   1 
ATOM   3798 O  O   . ARG B 1 199 ? -31.613 -20.383 14.995  1.00 44.06 ? 188 ARG B O   1 
ATOM   3799 C  CB  . ARG B 1 199 ? -34.471 -19.386 14.416  1.00 40.68 ? 188 ARG B CB  1 
ATOM   3800 C  CG  . ARG B 1 199 ? -35.748 -18.992 13.734  1.00 42.00 ? 188 ARG B CG  1 
ATOM   3801 C  CD  . ARG B 1 199 ? -36.784 -18.533 14.752  1.00 50.40 ? 188 ARG B CD  1 
ATOM   3802 N  NE  . ARG B 1 199 ? -37.443 -19.654 15.407  1.00 67.15 ? 188 ARG B NE  1 
ATOM   3803 C  CZ  . ARG B 1 199 ? -38.709 -19.995 15.206  1.00 71.98 ? 188 ARG B CZ  1 
ATOM   3804 N  NH1 . ARG B 1 199 ? -39.503 -19.276 14.424  1.00 61.32 ? 188 ARG B NH1 1 
ATOM   3805 N  NH2 . ARG B 1 199 ? -39.188 -21.086 15.801  1.00 76.34 ? 188 ARG B NH2 1 
ATOM   3806 N  N   . VAL B 1 200 ? -31.413 -19.129 13.137  1.00 39.25 ? 189 VAL B N   1 
ATOM   3807 C  CA  . VAL B 1 200 ? -30.088 -18.610 13.466  1.00 40.50 ? 189 VAL B CA  1 
ATOM   3808 C  C   . VAL B 1 200 ? -30.066 -17.115 13.137  1.00 36.58 ? 189 VAL B C   1 
ATOM   3809 O  O   . VAL B 1 200 ? -30.951 -16.593 12.460  1.00 34.48 ? 189 VAL B O   1 
ATOM   3810 C  CB  . VAL B 1 200 ? -28.956 -19.377 12.731  1.00 37.01 ? 189 VAL B CB  1 
ATOM   3811 C  CG1 . VAL B 1 200 ? -28.648 -20.692 13.443  1.00 37.30 ? 189 VAL B CG1 1 
ATOM   3812 C  CG2 . VAL B 1 200 ? -29.344 -19.680 11.293  1.00 32.26 ? 189 VAL B CG2 1 
ATOM   3813 N  N   . ALA B 1 201 ? -29.059 -16.413 13.645  1.00 36.77 ? 190 ALA B N   1 
ATOM   3814 C  CA  . ALA B 1 201 ? -28.927 -14.996 13.325  1.00 28.82 ? 190 ALA B CA  1 
ATOM   3815 C  C   . ALA B 1 201 ? -27.473 -14.665 13.024  1.00 32.81 ? 190 ALA B C   1 
ATOM   3816 O  O   . ALA B 1 201 ? -26.557 -15.203 13.661  1.00 36.39 ? 190 ALA B O   1 
ATOM   3817 C  CB  . ALA B 1 201 ? -29.453 -14.107 14.463  1.00 31.41 ? 190 ALA B CB  1 
ATOM   3818 N  N   . ILE B 1 202 ? -27.262 -13.788 12.042  1.00 32.24 ? 191 ILE B N   1 
ATOM   3819 C  CA  . ILE B 1 202 ? -25.930 -13.323 11.669  1.00 29.16 ? 191 ILE B CA  1 
ATOM   3820 C  C   . ILE B 1 202 ? -25.769 -11.881 12.117  1.00 33.93 ? 191 ILE B C   1 
ATOM   3821 O  O   . ILE B 1 202 ? -26.595 -11.021 11.786  1.00 39.07 ? 191 ILE B O   1 
ATOM   3822 C  CB  . ILE B 1 202 ? -25.669 -13.448 10.160  1.00 33.53 ? 191 ILE B CB  1 
ATOM   3823 C  CG1 . ILE B 1 202 ? -25.853 -14.893 9.707   1.00 28.09 ? 191 ILE B CG1 1 
ATOM   3824 C  CG2 . ILE B 1 202 ? -24.259 -12.934 9.826   1.00 31.32 ? 191 ILE B CG2 1 
ATOM   3825 C  CD1 . ILE B 1 202 ? -25.230 -15.184 8.400   1.00 29.39 ? 191 ILE B CD1 1 
ATOM   3826 N  N   . LEU B 1 203 ? -24.702 -11.617 12.857  1.00 30.07 ? 192 LEU B N   1 
ATOM   3827 C  CA  . LEU B 1 203 ? -24.357 -10.275 13.293  1.00 32.37 ? 192 LEU B CA  1 
ATOM   3828 C  C   . LEU B 1 203 ? -23.062 -9.875  12.589  1.00 35.40 ? 192 LEU B C   1 
ATOM   3829 O  O   . LEU B 1 203 ? -22.005 -10.467 12.839  1.00 32.17 ? 192 LEU B O   1 
ATOM   3830 C  CB  . LEU B 1 203 ? -24.218 -10.237 14.810  1.00 33.06 ? 192 LEU B CB  1 
ATOM   3831 C  CG  . LEU B 1 203 ? -23.813 -8.915  15.442  1.00 29.86 ? 192 LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 1 203 ? -24.819 -7.836  15.080  1.00 23.52 ? 192 LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 1 203 ? -23.684 -9.116  16.946  1.00 29.44 ? 192 LEU B CD2 1 
ATOM   3834 N  N   . ASP B 1 204 ? -23.147 -8.866  11.713  1.00 28.62 ? 193 ASP B N   1 
ATOM   3835 C  CA  . ASP B 1 204 ? -22.021 -8.411  10.897  1.00 28.51 ? 193 ASP B CA  1 
ATOM   3836 C  C   . ASP B 1 204 ? -21.475 -7.101  11.466  1.00 31.27 ? 193 ASP B C   1 
ATOM   3837 O  O   . ASP B 1 204 ? -21.980 -6.019  11.144  1.00 34.98 ? 193 ASP B O   1 
ATOM   3838 C  CB  . ASP B 1 204 ? -22.460 -8.237  9.447   1.00 30.12 ? 193 ASP B CB  1 
ATOM   3839 C  CG  . ASP B 1 204 ? -21.296 -8.059  8.499   1.00 27.46 ? 193 ASP B CG  1 
ATOM   3840 O  OD1 . ASP B 1 204 ? -20.358 -7.306  8.823   1.00 25.50 ? 193 ASP B OD1 1 
ATOM   3841 O  OD2 . ASP B 1 204 ? -21.330 -8.659  7.407   1.00 28.98 ? 193 ASP B OD2 1 
ATOM   3842 N  N   . VAL B 1 205 ? -20.413 -7.202  12.281  1.00 25.86 ? 194 VAL B N   1 
ATOM   3843 C  CA  . VAL B 1 205 ? -19.818 -6.047  12.960  1.00 29.66 ? 194 VAL B CA  1 
ATOM   3844 C  C   . VAL B 1 205 ? -18.694 -5.386  12.162  1.00 33.83 ? 194 VAL B C   1 
ATOM   3845 O  O   . VAL B 1 205 ? -18.206 -4.314  12.567  1.00 29.80 ? 194 VAL B O   1 
ATOM   3846 C  CB  . VAL B 1 205 ? -19.279 -6.441  14.354  1.00 32.64 ? 194 VAL B CB  1 
ATOM   3847 C  CG1 . VAL B 1 205 ? -20.372 -7.097  15.206  1.00 25.19 ? 194 VAL B CG1 1 
ATOM   3848 C  CG2 . VAL B 1 205 ? -18.046 -7.349  14.231  1.00 28.94 ? 194 VAL B CG2 1 
ATOM   3849 N  N   . ASP B 1 206 ? -18.255 -5.999  11.059  1.00 31.52 ? 195 ASP B N   1 
ATOM   3850 C  CA  . ASP B 1 206 ? -17.304 -5.384  10.150  1.00 23.09 ? 195 ASP B CA  1 
ATOM   3851 C  C   . ASP B 1 206 ? -17.720 -3.954  9.839   1.00 27.71 ? 195 ASP B C   1 
ATOM   3852 O  O   . ASP B 1 206 ? -18.904 -3.609  9.866   1.00 29.16 ? 195 ASP B O   1 
ATOM   3853 C  CB  . ASP B 1 206 ? -17.235 -6.198  8.862   1.00 26.10 ? 195 ASP B CB  1 
ATOM   3854 C  CG  . ASP B 1 206 ? -16.007 -5.898  8.040   1.00 31.34 ? 195 ASP B CG  1 
ATOM   3855 O  OD1 . ASP B 1 206 ? -14.952 -6.474  8.358   1.00 32.51 ? 195 ASP B OD1 1 
ATOM   3856 O  OD2 . ASP B 1 206 ? -16.090 -5.114  7.068   1.00 27.83 ? 195 ASP B OD2 1 
ATOM   3857 N  N   . TYR B 1 207 ? -16.728 -3.111  9.551   1.00 29.00 ? 196 TYR B N   1 
ATOM   3858 C  CA  . TYR B 1 207 ? -17.012 -1.741  9.154   1.00 23.59 ? 196 TYR B CA  1 
ATOM   3859 C  C   . TYR B 1 207 ? -17.861 -1.675  7.872   1.00 28.48 ? 196 TYR B C   1 
ATOM   3860 O  O   . TYR B 1 207 ? -18.634 -0.727  7.686   1.00 27.61 ? 196 TYR B O   1 
ATOM   3861 C  CB  . TYR B 1 207 ? -15.696 -0.996  8.990   1.00 22.02 ? 196 TYR B CB  1 
ATOM   3862 C  CG  . TYR B 1 207 ? -15.870 0.343   8.343   1.00 32.59 ? 196 TYR B CG  1 
ATOM   3863 C  CD1 . TYR B 1 207 ? -16.567 1.366   8.990   1.00 30.86 ? 196 TYR B CD1 1 
ATOM   3864 C  CD2 . TYR B 1 207 ? -15.380 0.585   7.065   1.00 33.51 ? 196 TYR B CD2 1 
ATOM   3865 C  CE1 . TYR B 1 207 ? -16.761 2.586   8.382   1.00 28.95 ? 196 TYR B CE1 1 
ATOM   3866 C  CE2 . TYR B 1 207 ? -15.560 1.810   6.456   1.00 32.62 ? 196 TYR B CE2 1 
ATOM   3867 C  CZ  . TYR B 1 207 ? -16.254 2.804   7.122   1.00 32.32 ? 196 TYR B CZ  1 
ATOM   3868 O  OH  . TYR B 1 207 ? -16.443 4.025   6.521   1.00 37.28 ? 196 TYR B OH  1 
ATOM   3869 N  N   . HIS B 1 208 ? -17.763 -2.677  6.999   1.00 29.03 ? 197 HIS B N   1 
ATOM   3870 C  CA  . HIS B 1 208 ? -18.451 -2.694  5.715   1.00 25.29 ? 197 HIS B CA  1 
ATOM   3871 C  C   . HIS B 1 208 ? -19.726 -3.519  5.781   1.00 26.59 ? 197 HIS B C   1 
ATOM   3872 O  O   . HIS B 1 208 ? -19.805 -4.526  6.492   1.00 26.31 ? 197 HIS B O   1 
ATOM   3873 C  CB  . HIS B 1 208 ? -17.559 -3.280  4.622   1.00 24.74 ? 197 HIS B CB  1 
ATOM   3874 C  CG  . HIS B 1 208 ? -16.340 -2.473  4.346   1.00 24.29 ? 197 HIS B CG  1 
ATOM   3875 N  ND1 . HIS B 1 208 ? -15.157 -2.668  5.014   1.00 28.58 ? 197 HIS B ND1 1 
ATOM   3876 C  CD2 . HIS B 1 208 ? -16.117 -1.465  3.476   1.00 28.46 ? 197 HIS B CD2 1 
ATOM   3877 C  CE1 . HIS B 1 208 ? -14.251 -1.823  4.563   1.00 29.65 ? 197 HIS B CE1 1 
ATOM   3878 N  NE2 . HIS B 1 208 ? -14.811 -1.080  3.628   1.00 29.43 ? 197 HIS B NE2 1 
ATOM   3879 N  N   . HIS B 1 209 ? -20.710 -3.114  4.987   1.00 24.13 ? 198 HIS B N   1 
ATOM   3880 C  CA  . HIS B 1 209 ? -21.905 -3.927  4.848   1.00 27.97 ? 198 HIS B CA  1 
ATOM   3881 C  C   . HIS B 1 209 ? -21.563 -5.303  4.277   1.00 28.20 ? 198 HIS B C   1 
ATOM   3882 O  O   . HIS B 1 209 ? -20.810 -5.422  3.306   1.00 28.80 ? 198 HIS B O   1 
ATOM   3883 C  CB  . HIS B 1 209 ? -22.930 -3.239  3.952   1.00 25.15 ? 198 HIS B CB  1 
ATOM   3884 C  CG  . HIS B 1 209 ? -24.234 -3.972  3.887   1.00 31.13 ? 198 HIS B CG  1 
ATOM   3885 N  ND1 . HIS B 1 209 ? -24.721 -4.533  2.725   1.00 32.27 ? 198 HIS B ND1 1 
ATOM   3886 C  CD2 . HIS B 1 209 ? -25.136 -4.272  4.853   1.00 30.09 ? 198 HIS B CD2 1 
ATOM   3887 C  CE1 . HIS B 1 209 ? -25.877 -5.123  2.972   1.00 28.61 ? 198 HIS B CE1 1 
ATOM   3888 N  NE2 . HIS B 1 209 ? -26.150 -4.979  4.257   1.00 27.78 ? 198 HIS B NE2 1 
ATOM   3889 N  N   . GLY B 1 210 ? -22.127 -6.344  4.888   1.00 27.72 ? 199 GLY B N   1 
ATOM   3890 C  CA  . GLY B 1 210 ? -22.030 -7.696  4.364   1.00 31.38 ? 199 GLY B CA  1 
ATOM   3891 C  C   . GLY B 1 210 ? -23.073 -7.954  3.290   1.00 30.17 ? 199 GLY B C   1 
ATOM   3892 O  O   . GLY B 1 210 ? -24.032 -8.703  3.504   1.00 32.93 ? 199 GLY B O   1 
ATOM   3893 N  N   . ASN B 1 211 ? -22.872 -7.333  2.128   1.00 22.92 ? 200 ASN B N   1 
ATOM   3894 C  CA  . ASN B 1 211 ? -23.860 -7.355  1.054   1.00 28.93 ? 200 ASN B CA  1 
ATOM   3895 C  C   . ASN B 1 211 ? -24.161 -8.773  0.578   1.00 33.08 ? 200 ASN B C   1 
ATOM   3896 O  O   . ASN B 1 211 ? -25.321 -9.111  0.308   1.00 31.68 ? 200 ASN B O   1 
ATOM   3897 C  CB  . ASN B 1 211 ? -23.353 -6.509  -0.114  1.00 30.02 ? 200 ASN B CB  1 
ATOM   3898 C  CG  . ASN B 1 211 ? -21.994 -6.992  -0.619  1.00 33.96 ? 200 ASN B CG  1 
ATOM   3899 O  OD1 . ASN B 1 211 ? -20.968 -6.802  0.038   1.00 31.90 ? 200 ASN B OD1 1 
ATOM   3900 N  ND2 . ASN B 1 211 ? -21.989 -7.638  -1.777  1.00 33.01 ? 200 ASN B ND2 1 
ATOM   3901 N  N   . GLY B 1 212 ? -23.126 -9.610  0.432   1.00 31.06 ? 201 GLY B N   1 
ATOM   3902 C  CA  . GLY B 1 212 ? -23.352 -10.968 -0.034  1.00 31.86 ? 201 GLY B CA  1 
ATOM   3903 C  C   . GLY B 1 212 ? -24.158 -11.800 0.940   1.00 30.47 ? 201 GLY B C   1 
ATOM   3904 O  O   . GLY B 1 212 ? -24.964 -12.638 0.529   1.00 30.76 ? 201 GLY B O   1 
ATOM   3905 N  N   . THR B 1 213 ? -23.969 -11.566 2.234   1.00 28.39 ? 202 THR B N   1 
ATOM   3906 C  CA  . THR B 1 213 ? -24.722 -12.298 3.239   1.00 32.04 ? 202 THR B CA  1 
ATOM   3907 C  C   . THR B 1 213 ? -26.164 -11.827 3.297   1.00 31.59 ? 202 THR B C   1 
ATOM   3908 O  O   . THR B 1 213 ? -27.085 -12.646 3.424   1.00 35.23 ? 202 THR B O   1 
ATOM   3909 C  CB  . THR B 1 213 ? -24.047 -12.145 4.595   1.00 32.46 ? 202 THR B CB  1 
ATOM   3910 O  OG1 . THR B 1 213 ? -22.661 -12.481 4.454   1.00 32.34 ? 202 THR B OG1 1 
ATOM   3911 C  CG2 . THR B 1 213 ? -24.702 -13.064 5.634   1.00 26.86 ? 202 THR B CG2 1 
ATOM   3912 N  N   . GLN B 1 214 ? -26.382 -10.511 3.224   1.00 30.78 ? 203 GLN B N   1 
ATOM   3913 C  CA  . GLN B 1 214 ? -27.752 -10.013 3.125   1.00 38.44 ? 203 GLN B CA  1 
ATOM   3914 C  C   . GLN B 1 214 ? -28.448 -10.608 1.901   1.00 33.16 ? 203 GLN B C   1 
ATOM   3915 O  O   . GLN B 1 214 ? -29.597 -11.059 1.979   1.00 28.13 ? 203 GLN B O   1 
ATOM   3916 C  CB  . GLN B 1 214 ? -27.765 -8.480  3.078   1.00 26.76 ? 203 GLN B CB  1 
ATOM   3917 C  CG  . GLN B 1 214 ? -28.927 -7.926  2.266   1.00 29.35 ? 203 GLN B CG  1 
ATOM   3918 C  CD  . GLN B 1 214 ? -29.172 -6.455  2.517   1.00 31.02 ? 203 GLN B CD  1 
ATOM   3919 O  OE1 . GLN B 1 214 ? -28.684 -5.900  3.491   1.00 32.95 ? 203 GLN B OE1 1 
ATOM   3920 N  NE2 . GLN B 1 214 ? -29.946 -5.824  1.649   1.00 24.78 ? 203 GLN B NE2 1 
ATOM   3921 N  N   . SER B 1 215 ? -27.739 -10.664 0.778   1.00 31.51 ? 204 SER B N   1 
ATOM   3922 C  CA  . SER B 1 215 ? -28.306 -11.230 -0.432  1.00 29.77 ? 204 SER B CA  1 
ATOM   3923 C  C   . SER B 1 215 ? -28.664 -12.705 -0.246  1.00 30.63 ? 204 SER B C   1 
ATOM   3924 O  O   . SER B 1 215 ? -29.759 -13.130 -0.624  1.00 28.03 ? 204 SER B O   1 
ATOM   3925 C  CB  . SER B 1 215 ? -27.321 -11.026 -1.583  1.00 31.86 ? 204 SER B CB  1 
ATOM   3926 O  OG  . SER B 1 215 ? -27.636 -11.861 -2.681  1.00 43.64 ? 204 SER B OG  1 
ATOM   3927 N  N   . ILE B 1 216 ? -27.778 -13.489 0.379   1.00 31.88 ? 205 ILE B N   1 
ATOM   3928 C  CA  . ILE B 1 216 ? -27.967 -14.941 0.442   1.00 30.73 ? 205 ILE B CA  1 
ATOM   3929 C  C   . ILE B 1 216 ? -29.245 -15.300 1.206   1.00 33.10 ? 205 ILE B C   1 
ATOM   3930 O  O   . ILE B 1 216 ? -29.979 -16.220 0.814   1.00 29.71 ? 205 ILE B O   1 
ATOM   3931 C  CB  . ILE B 1 216 ? -26.712 -15.609 1.049   1.00 30.44 ? 205 ILE B CB  1 
ATOM   3932 C  CG1 . ILE B 1 216 ? -25.606 -15.740 -0.005  1.00 29.58 ? 205 ILE B CG1 1 
ATOM   3933 C  CG2 . ILE B 1 216 ? -27.021 -16.976 1.661   1.00 23.05 ? 205 ILE B CG2 1 
ATOM   3934 C  CD1 . ILE B 1 216 ? -24.196 -15.735 0.579   1.00 26.15 ? 205 ILE B CD1 1 
ATOM   3935 N  N   . PHE B 1 217 ? -29.545 -14.574 2.295   1.00 35.67 ? 206 PHE B N   1 
ATOM   3936 C  CA  . PHE B 1 217 ? -30.707 -14.860 3.140   1.00 34.29 ? 206 PHE B CA  1 
ATOM   3937 C  C   . PHE B 1 217 ? -31.815 -13.806 3.028   1.00 35.57 ? 206 PHE B C   1 
ATOM   3938 O  O   . PHE B 1 217 ? -32.617 -13.675 3.951   1.00 38.74 ? 206 PHE B O   1 
ATOM   3939 C  CB  . PHE B 1 217 ? -30.299 -15.008 4.611   1.00 29.89 ? 206 PHE B CB  1 
ATOM   3940 C  CG  . PHE B 1 217 ? -29.150 -15.960 4.844   1.00 36.74 ? 206 PHE B CG  1 
ATOM   3941 C  CD1 . PHE B 1 217 ? -29.309 -17.333 4.653   1.00 35.03 ? 206 PHE B CD1 1 
ATOM   3942 C  CD2 . PHE B 1 217 ? -27.906 -15.487 5.255   1.00 32.66 ? 206 PHE B CD2 1 
ATOM   3943 C  CE1 . PHE B 1 217 ? -28.244 -18.220 4.865   1.00 29.07 ? 206 PHE B CE1 1 
ATOM   3944 C  CE2 . PHE B 1 217 ? -26.835 -16.368 5.473   1.00 31.64 ? 206 PHE B CE2 1 
ATOM   3945 C  CZ  . PHE B 1 217 ? -27.012 -17.737 5.271   1.00 33.77 ? 206 PHE B CZ  1 
ATOM   3946 N  N   . TYR B 1 218 ? -31.916 -13.083 1.899   1.00 36.68 ? 207 TYR B N   1 
ATOM   3947 C  CA  . TYR B 1 218 ? -32.792 -11.907 1.851   1.00 32.67 ? 207 TYR B CA  1 
ATOM   3948 C  C   . TYR B 1 218 ? -34.269 -12.270 1.915   1.00 37.95 ? 207 TYR B C   1 
ATOM   3949 O  O   . TYR B 1 218 ? -35.063 -11.501 2.471   1.00 34.12 ? 207 TYR B O   1 
ATOM   3950 C  CB  . TYR B 1 218 ? -32.543 -11.069 0.599   1.00 31.32 ? 207 TYR B CB  1 
ATOM   3951 C  CG  . TYR B 1 218 ? -32.991 -9.619  0.755   1.00 33.79 ? 207 TYR B CG  1 
ATOM   3952 C  CD1 . TYR B 1 218 ? -32.595 -8.867  1.861   1.00 32.69 ? 207 TYR B CD1 1 
ATOM   3953 C  CD2 . TYR B 1 218 ? -33.808 -9.011  -0.185  1.00 30.51 ? 207 TYR B CD2 1 
ATOM   3954 C  CE1 . TYR B 1 218 ? -32.987 -7.570  2.023   1.00 29.19 ? 207 TYR B CE1 1 
ATOM   3955 C  CE2 . TYR B 1 218 ? -34.208 -7.697  -0.033  1.00 38.83 ? 207 TYR B CE2 1 
ATOM   3956 C  CZ  . TYR B 1 218 ? -33.797 -6.978  1.081   1.00 36.14 ? 207 TYR B CZ  1 
ATOM   3957 O  OH  . TYR B 1 218 ? -34.195 -5.667  1.255   1.00 28.61 ? 207 TYR B OH  1 
ATOM   3958 N  N   . SER B 1 219 ? -34.670 -13.401 1.315   1.00 38.76 ? 208 SER B N   1 
ATOM   3959 C  CA  . SER B 1 219 ? -36.066 -13.837 1.347   1.00 39.14 ? 208 SER B CA  1 
ATOM   3960 C  C   . SER B 1 219 ? -36.265 -15.002 2.299   1.00 40.55 ? 208 SER B C   1 
ATOM   3961 O  O   . SER B 1 219 ? -37.161 -15.832 2.104   1.00 40.71 ? 208 SER B O   1 
ATOM   3962 C  CB  . SER B 1 219 ? -36.593 -14.199 -0.043  1.00 34.14 ? 208 SER B CB  1 
ATOM   3963 O  OG  . SER B 1 219 ? -35.646 -13.907 -1.043  1.00 49.51 ? 208 SER B OG  1 
ATOM   3964 N  N   . ARG B 1 220 ? -35.438 -15.062 3.337   1.00 39.25 ? 209 ARG B N   1 
ATOM   3965 C  CA  . ARG B 1 220 ? -35.506 -16.114 4.332   1.00 39.31 ? 209 ARG B CA  1 
ATOM   3966 C  C   . ARG B 1 220 ? -35.724 -15.513 5.715   1.00 42.56 ? 209 ARG B C   1 
ATOM   3967 O  O   . ARG B 1 220 ? -35.319 -14.381 5.997   1.00 42.11 ? 209 ARG B O   1 
ATOM   3968 C  CB  . ARG B 1 220 ? -34.249 -16.974 4.270   1.00 31.21 ? 209 ARG B CB  1 
ATOM   3969 C  CG  . ARG B 1 220 ? -34.265 -17.811 3.018   1.00 32.74 ? 209 ARG B CG  1 
ATOM   3970 C  CD  . ARG B 1 220 ? -33.043 -18.615 2.867   1.00 29.07 ? 209 ARG B CD  1 
ATOM   3971 N  NE  . ARG B 1 220 ? -32.799 -19.399 4.062   1.00 28.20 ? 209 ARG B NE  1 
ATOM   3972 C  CZ  . ARG B 1 220 ? -31.812 -20.273 4.177   1.00 31.32 ? 209 ARG B CZ  1 
ATOM   3973 N  NH1 . ARG B 1 220 ? -30.996 -20.525 3.167   1.00 30.07 ? 209 ARG B NH1 1 
ATOM   3974 N  NH2 . ARG B 1 220 ? -31.628 -20.897 5.337   1.00 32.47 ? 209 ARG B NH2 1 
ATOM   3975 N  N   . SER B 1 221 ? -36.416 -16.261 6.564   1.00 37.62 ? 210 SER B N   1 
ATOM   3976 C  CA  . SER B 1 221 ? -36.705 -15.785 7.903   1.00 44.40 ? 210 SER B CA  1 
ATOM   3977 C  C   . SER B 1 221 ? -36.301 -16.780 8.980   1.00 41.94 ? 210 SER B C   1 
ATOM   3978 O  O   . SER B 1 221 ? -36.588 -16.543 10.160  1.00 45.39 ? 210 SER B O   1 
ATOM   3979 C  CB  . SER B 1 221 ? -38.194 -15.443 8.048   1.00 42.90 ? 210 SER B CB  1 
ATOM   3980 O  OG  . SER B 1 221 ? -38.869 -16.491 8.705   1.00 41.16 ? 210 SER B OG  1 
ATOM   3981 N  N   . ASP B 1 222 ? -35.668 -17.887 8.613   1.00 32.83 ? 211 ASP B N   1 
ATOM   3982 C  CA  . ASP B 1 222 ? -34.987 -18.714 9.592   1.00 41.00 ? 211 ASP B CA  1 
ATOM   3983 C  C   . ASP B 1 222 ? -33.567 -18.233 9.853   1.00 42.60 ? 211 ASP B C   1 
ATOM   3984 O  O   . ASP B 1 222 ? -32.905 -18.747 10.767  1.00 40.03 ? 211 ASP B O   1 
ATOM   3985 C  CB  . ASP B 1 222 ? -34.979 -20.184 9.140   1.00 42.01 ? 211 ASP B CB  1 
ATOM   3986 C  CG  . ASP B 1 222 ? -34.344 -20.389 7.774   1.00 40.23 ? 211 ASP B CG  1 
ATOM   3987 O  OD1 . ASP B 1 222 ? -34.177 -19.409 7.019   1.00 44.99 ? 211 ASP B OD1 1 
ATOM   3988 O  OD2 . ASP B 1 222 ? -34.011 -21.549 7.454   1.00 44.62 ? 211 ASP B OD2 1 
ATOM   3989 N  N   . VAL B 1 223 ? -33.096 -17.267 9.064   1.00 39.49 ? 212 VAL B N   1 
ATOM   3990 C  CA  . VAL B 1 223 ? -31.769 -16.681 9.198   1.00 39.14 ? 212 VAL B CA  1 
ATOM   3991 C  C   . VAL B 1 223 ? -31.974 -15.178 9.248   1.00 35.39 ? 212 VAL B C   1 
ATOM   3992 O  O   . VAL B 1 223 ? -32.221 -14.546 8.213   1.00 34.56 ? 212 VAL B O   1 
ATOM   3993 C  CB  . VAL B 1 223 ? -30.832 -17.068 8.052   1.00 37.23 ? 212 VAL B CB  1 
ATOM   3994 C  CG1 . VAL B 1 223 ? -29.416 -16.701 8.407   1.00 29.83 ? 212 VAL B CG1 1 
ATOM   3995 C  CG2 . VAL B 1 223 ? -30.950 -18.551 7.749   1.00 35.88 ? 212 VAL B CG2 1 
ATOM   3996 N  N   . LEU B 1 224 ? -31.892 -14.606 10.447  1.00 35.32 ? 213 LEU B N   1 
ATOM   3997 C  CA  . LEU B 1 224 ? -31.967 -13.163 10.635  1.00 34.45 ? 213 LEU B CA  1 
ATOM   3998 C  C   . LEU B 1 224 ? -30.591 -12.564 10.385  1.00 33.93 ? 213 LEU B C   1 
ATOM   3999 O  O   . LEU B 1 224 ? -29.626 -12.966 11.043  1.00 33.29 ? 213 LEU B O   1 
ATOM   4000 C  CB  . LEU B 1 224 ? -32.438 -12.843 12.053  1.00 31.22 ? 213 LEU B CB  1 
ATOM   4001 C  CG  . LEU B 1 224 ? -32.352 -11.386 12.508  1.00 34.62 ? 213 LEU B CG  1 
ATOM   4002 C  CD1 . LEU B 1 224 ? -33.287 -10.609 11.655  1.00 35.10 ? 213 LEU B CD1 1 
ATOM   4003 C  CD2 . LEU B 1 224 ? -32.696 -11.214 13.982  1.00 29.34 ? 213 LEU B CD2 1 
ATOM   4004 N  N   . PHE B 1 225 ? -30.493 -11.615 9.435   1.00 32.25 ? 214 PHE B N   1 
ATOM   4005 C  CA  . PHE B 1 225 ? -29.250 -10.883 9.170   1.00 35.18 ? 214 PHE B CA  1 
ATOM   4006 C  C   . PHE B 1 225 ? -29.311 -9.480  9.764   1.00 32.14 ? 214 PHE B C   1 
ATOM   4007 O  O   . PHE B 1 225 ? -30.280 -8.753  9.534   1.00 36.02 ? 214 PHE B O   1 
ATOM   4008 C  CB  . PHE B 1 225 ? -28.949 -10.778 7.668   1.00 29.95 ? 214 PHE B CB  1 
ATOM   4009 C  CG  . PHE B 1 225 ? -27.670 -10.011 7.357   1.00 34.49 ? 214 PHE B CG  1 
ATOM   4010 C  CD1 . PHE B 1 225 ? -26.410 -10.552 7.680   1.00 33.00 ? 214 PHE B CD1 1 
ATOM   4011 C  CD2 . PHE B 1 225 ? -27.716 -8.749  6.754   1.00 31.48 ? 214 PHE B CD2 1 
ATOM   4012 C  CE1 . PHE B 1 225 ? -25.221 -9.846  7.408   1.00 29.62 ? 214 PHE B CE1 1 
ATOM   4013 C  CE2 . PHE B 1 225 ? -26.532 -8.042  6.469   1.00 31.30 ? 214 PHE B CE2 1 
ATOM   4014 C  CZ  . PHE B 1 225 ? -25.282 -8.591  6.801   1.00 29.56 ? 214 PHE B CZ  1 
ATOM   4015 N  N   . THR B 1 226 ? -28.273 -9.101  10.516  1.00 26.93 ? 215 THR B N   1 
ATOM   4016 C  CA  . THR B 1 226 ? -28.094 -7.728  10.974  1.00 30.95 ? 215 THR B CA  1 
ATOM   4017 C  C   . THR B 1 226 ? -26.675 -7.287  10.668  1.00 32.47 ? 215 THR B C   1 
ATOM   4018 O  O   . THR B 1 226 ? -25.749 -8.101  10.667  1.00 31.19 ? 215 THR B O   1 
ATOM   4019 C  CB  . THR B 1 226 ? -28.334 -7.541  12.482  1.00 32.28 ? 215 THR B CB  1 
ATOM   4020 O  OG1 . THR B 1 226 ? -27.455 -8.402  13.216  1.00 42.12 ? 215 THR B OG1 1 
ATOM   4021 C  CG2 . THR B 1 226 ? -29.767 -7.849  12.856  1.00 40.07 ? 215 THR B CG2 1 
ATOM   4022 N  N   . SER B 1 227 ? -26.512 -5.982  10.443  1.00 29.97 ? 216 SER B N   1 
ATOM   4023 C  CA  . SER B 1 227 ? -25.230 -5.413  10.057  1.00 30.28 ? 216 SER B CA  1 
ATOM   4024 C  C   . SER B 1 227 ? -25.166 -3.965  10.516  1.00 30.61 ? 216 SER B C   1 
ATOM   4025 O  O   . SER B 1 227 ? -26.130 -3.217  10.350  1.00 33.15 ? 216 SER B O   1 
ATOM   4026 C  CB  . SER B 1 227 ? -25.026 -5.491  8.539   1.00 29.50 ? 216 SER B CB  1 
ATOM   4027 O  OG  . SER B 1 227 ? -23.698 -5.159  8.179   1.00 24.79 ? 216 SER B OG  1 
ATOM   4028 N  N   . ILE B 1 228 ? -24.024 -3.585  11.084  1.00 29.82 ? 217 ILE B N   1 
ATOM   4029 C  CA  . ILE B 1 228 ? -23.677 -2.202  11.398  1.00 30.84 ? 217 ILE B CA  1 
ATOM   4030 C  C   . ILE B 1 228 ? -22.480 -1.807  10.544  1.00 28.67 ? 217 ILE B C   1 
ATOM   4031 O  O   . ILE B 1 228 ? -21.486 -2.540  10.488  1.00 31.63 ? 217 ILE B O   1 
ATOM   4032 C  CB  . ILE B 1 228 ? -23.332 -2.030  12.887  1.00 33.38 ? 217 ILE B CB  1 
ATOM   4033 C  CG1 . ILE B 1 228 ? -24.411 -2.663  13.775  1.00 31.20 ? 217 ILE B CG1 1 
ATOM   4034 C  CG2 . ILE B 1 228 ? -23.030 -0.552  13.188  1.00 30.36 ? 217 ILE B CG2 1 
ATOM   4035 C  CD1 . ILE B 1 228 ? -23.867 -3.130  15.122  1.00 30.04 ? 217 ILE B CD1 1 
ATOM   4036 N  N   . HIS B 1 229 ? -22.537 -0.636  9.931   1.00 27.38 ? 218 HIS B N   1 
ATOM   4037 C  CA  . HIS B 1 229 ? -21.549 -0.370  8.892   1.00 31.03 ? 218 HIS B CA  1 
ATOM   4038 C  C   . HIS B 1 229 ? -21.594 1.099   8.498   1.00 30.11 ? 218 HIS B C   1 
ATOM   4039 O  O   . HIS B 1 229 ? -22.584 1.794   8.738   1.00 28.85 ? 218 HIS B O   1 
ATOM   4040 C  CB  . HIS B 1 229 ? -21.809 -1.254  7.666   1.00 28.57 ? 218 HIS B CB  1 
ATOM   4041 C  CG  . HIS B 1 229 ? -23.245 -1.273  7.253   1.00 29.13 ? 218 HIS B CG  1 
ATOM   4042 N  ND1 . HIS B 1 229 ? -24.124 -2.254  7.661   1.00 31.28 ? 218 HIS B ND1 1 
ATOM   4043 C  CD2 . HIS B 1 229 ? -23.967 -0.411  6.499   1.00 26.94 ? 218 HIS B CD2 1 
ATOM   4044 C  CE1 . HIS B 1 229 ? -25.321 -2.002  7.162   1.00 30.10 ? 218 HIS B CE1 1 
ATOM   4045 N  NE2 . HIS B 1 229 ? -25.252 -0.890  6.452   1.00 25.32 ? 218 HIS B NE2 1 
ATOM   4046 N  N   . GLY B 1 230 ? -20.509 1.558   7.880   1.00 26.29 ? 219 GLY B N   1 
ATOM   4047 C  CA  . GLY B 1 230 ? -20.526 2.861   7.253   1.00 28.95 ? 219 GLY B CA  1 
ATOM   4048 C  C   . GLY B 1 230 ? -21.638 2.946   6.226   1.00 35.66 ? 219 GLY B C   1 
ATOM   4049 O  O   . GLY B 1 230 ? -21.794 2.056   5.377   1.00 29.18 ? 219 GLY B O   1 
ATOM   4050 N  N   . ASP B 1 231 ? -22.428 4.010   6.314   1.00 38.45 ? 220 ASP B N   1 
ATOM   4051 C  CA  . ASP B 1 231 ? -23.559 4.233   5.430   1.00 36.00 ? 220 ASP B CA  1 
ATOM   4052 C  C   . ASP B 1 231 ? -23.166 3.989   3.973   1.00 34.96 ? 220 ASP B C   1 
ATOM   4053 O  O   . ASP B 1 231 ? -22.245 4.653   3.471   1.00 33.97 ? 220 ASP B O   1 
ATOM   4054 C  CB  . ASP B 1 231 ? -24.053 5.662   5.610   1.00 35.86 ? 220 ASP B CB  1 
ATOM   4055 C  CG  . ASP B 1 231 ? -25.469 5.846   5.141   1.00 36.45 ? 220 ASP B CG  1 
ATOM   4056 O  OD1 . ASP B 1 231 ? -25.889 5.153   4.197   1.00 35.93 ? 220 ASP B OD1 1 
ATOM   4057 O  OD2 . ASP B 1 231 ? -26.164 6.693   5.724   1.00 43.80 ? 220 ASP B OD2 1 
ATOM   4058 N  N   . PRO B 1 232 ? -23.824 3.057   3.268   1.00 36.93 ? 221 PRO B N   1 
ATOM   4059 C  CA  . PRO B 1 232 ? -23.418 2.760   1.876   1.00 31.59 ? 221 PRO B CA  1 
ATOM   4060 C  C   . PRO B 1 232 ? -23.577 3.934   0.935   1.00 31.37 ? 221 PRO B C   1 
ATOM   4061 O  O   . PRO B 1 232 ? -22.932 3.953   -0.118  1.00 30.58 ? 221 PRO B O   1 
ATOM   4062 C  CB  . PRO B 1 232 ? -24.338 1.600   1.471   1.00 28.31 ? 221 PRO B CB  1 
ATOM   4063 C  CG  . PRO B 1 232 ? -25.502 1.699   2.385   1.00 31.55 ? 221 PRO B CG  1 
ATOM   4064 C  CD  . PRO B 1 232 ? -24.979 2.249   3.693   1.00 29.42 ? 221 PRO B CD  1 
ATOM   4065 N  N   . LYS B 1 233 ? -24.412 4.916   1.279   1.00 30.13 ? 222 LYS B N   1 
ATOM   4066 C  CA  . LYS B 1 233 ? -24.457 6.151   0.512   1.00 36.51 ? 222 LYS B CA  1 
ATOM   4067 C  C   . LYS B 1 233 ? -23.058 6.782   0.331   1.00 36.12 ? 222 LYS B C   1 
ATOM   4068 O  O   . LYS B 1 233 ? -22.849 7.546   -0.621  1.00 33.68 ? 222 LYS B O   1 
ATOM   4069 C  CB  . LYS B 1 233 ? -25.494 7.101   1.174   1.00 36.25 ? 222 LYS B CB  1 
ATOM   4070 C  CG  . LYS B 1 233 ? -25.032 7.949   2.398   1.00 41.50 ? 222 LYS B CG  1 
ATOM   4071 C  CD  . LYS B 1 233 ? -24.362 9.294   1.988   1.00 45.60 ? 222 LYS B CD  1 
ATOM   4072 C  CE  . LYS B 1 233 ? -23.668 10.037  3.158   1.00 45.76 ? 222 LYS B CE  1 
ATOM   4073 N  NZ  . LYS B 1 233 ? -22.504 10.915  2.723   1.00 38.98 ? 222 LYS B NZ  1 
ATOM   4074 N  N   . PHE B 1 234 ? -22.079 6.459   1.186   1.00 30.53 ? 223 PHE B N   1 
ATOM   4075 C  CA  . PHE B 1 234 ? -20.701 6.886   0.940   1.00 33.30 ? 223 PHE B CA  1 
ATOM   4076 C  C   . PHE B 1 234 ? -19.657 5.772   1.023   1.00 35.14 ? 223 PHE B C   1 
ATOM   4077 O  O   . PHE B 1 234 ? -18.573 5.926   0.446   1.00 32.79 ? 223 PHE B O   1 
ATOM   4078 C  CB  . PHE B 1 234 ? -20.298 8.025   1.898   1.00 30.34 ? 223 PHE B CB  1 
ATOM   4079 C  CG  . PHE B 1 234 ? -20.098 7.603   3.333   1.00 26.75 ? 223 PHE B CG  1 
ATOM   4080 C  CD1 . PHE B 1 234 ? -18.878 7.102   3.767   1.00 24.35 ? 223 PHE B CD1 1 
ATOM   4081 C  CD2 . PHE B 1 234 ? -21.117 7.765   4.264   1.00 31.96 ? 223 PHE B CD2 1 
ATOM   4082 C  CE1 . PHE B 1 234 ? -18.690 6.722   5.085   1.00 29.28 ? 223 PHE B CE1 1 
ATOM   4083 C  CE2 . PHE B 1 234 ? -20.930 7.396   5.600   1.00 32.99 ? 223 PHE B CE2 1 
ATOM   4084 C  CZ  . PHE B 1 234 ? -19.710 6.870   6.004   1.00 31.94 ? 223 PHE B CZ  1 
ATOM   4085 N  N   . GLU B 1 235 ? -19.942 4.661   1.688   1.00 28.85 ? 224 GLU B N   1 
ATOM   4086 C  CA  . GLU B 1 235 ? -18.960 3.617   1.922   1.00 28.86 ? 224 GLU B CA  1 
ATOM   4087 C  C   . GLU B 1 235 ? -19.263 2.391   1.065   1.00 31.21 ? 224 GLU B C   1 
ATOM   4088 O  O   . GLU B 1 235 ? -20.429 2.073   0.810   1.00 32.22 ? 224 GLU B O   1 
ATOM   4089 C  CB  . GLU B 1 235 ? -18.944 3.244   3.412   1.00 34.65 ? 224 GLU B CB  1 
ATOM   4090 C  CG  . GLU B 1 235 ? -17.681 2.549   3.866   1.00 31.57 ? 224 GLU B CG  1 
ATOM   4091 C  CD  . GLU B 1 235 ? -16.437 3.275   3.396   1.00 38.43 ? 224 GLU B CD  1 
ATOM   4092 O  OE1 . GLU B 1 235 ? -16.029 4.239   4.099   1.00 38.04 ? 224 GLU B OE1 1 
ATOM   4093 O  OE2 . GLU B 1 235 ? -15.884 2.896   2.329   1.00 28.55 ? 224 GLU B OE2 1 
ATOM   4094 N  N   . PHE B 1 236 ? -18.202 1.725   0.617   1.00 30.03 ? 225 PHE B N   1 
ATOM   4095 C  CA  . PHE B 1 236 ? -18.290 0.435   -0.054  1.00 24.89 ? 225 PHE B CA  1 
ATOM   4096 C  C   . PHE B 1 236 ? -19.121 -0.526  0.792   1.00 28.92 ? 225 PHE B C   1 
ATOM   4097 O  O   . PHE B 1 236 ? -18.928 -0.592  2.012   1.00 30.61 ? 225 PHE B O   1 
ATOM   4098 C  CB  . PHE B 1 236 ? -16.865 -0.098  -0.256  1.00 28.72 ? 225 PHE B CB  1 
ATOM   4099 C  CG  . PHE B 1 236 ? -16.777 -1.461  -0.887  1.00 27.68 ? 225 PHE B CG  1 
ATOM   4100 C  CD1 . PHE B 1 236 ? -16.801 -2.613  -0.104  1.00 28.78 ? 225 PHE B CD1 1 
ATOM   4101 C  CD2 . PHE B 1 236 ? -16.614 -1.593  -2.254  1.00 24.62 ? 225 PHE B CD2 1 
ATOM   4102 C  CE1 . PHE B 1 236 ? -16.701 -3.869  -0.679  1.00 26.42 ? 225 PHE B CE1 1 
ATOM   4103 C  CE2 . PHE B 1 236 ? -16.515 -2.842  -2.833  1.00 24.96 ? 225 PHE B CE2 1 
ATOM   4104 C  CZ  . PHE B 1 236 ? -16.553 -3.983  -2.042  1.00 27.55 ? 225 PHE B CZ  1 
ATOM   4105 N  N   . PRO B 1 237 ? -20.015 -1.326  0.190   1.00 26.00 ? 226 PRO B N   1 
ATOM   4106 C  CA  . PRO B 1 237 ? -20.143 -1.669  -1.223  1.00 25.24 ? 226 PRO B CA  1 
ATOM   4107 C  C   . PRO B 1 237 ? -21.072 -0.758  -2.014  1.00 29.97 ? 226 PRO B C   1 
ATOM   4108 O  O   . PRO B 1 237 ? -21.367 -1.073  -3.170  1.00 29.13 ? 226 PRO B O   1 
ATOM   4109 C  CB  . PRO B 1 237 ? -20.688 -3.095  -1.148  1.00 28.51 ? 226 PRO B CB  1 
ATOM   4110 C  CG  . PRO B 1 237 ? -21.616 -3.052  0.076   1.00 30.13 ? 226 PRO B CG  1 
ATOM   4111 C  CD  . PRO B 1 237 ? -21.108 -1.927  0.969   1.00 25.89 ? 226 PRO B CD  1 
ATOM   4112 N  N   . PHE B 1 238 ? -21.532 0.342   -1.401  1.00 26.92 ? 227 PHE B N   1 
ATOM   4113 C  CA  . PHE B 1 238 ? -22.277 1.437   -2.033  1.00 29.33 ? 227 PHE B CA  1 
ATOM   4114 C  C   . PHE B 1 238 ? -23.727 1.089   -2.352  1.00 32.55 ? 227 PHE B C   1 
ATOM   4115 O  O   . PHE B 1 238 ? -24.625 1.907   -2.123  1.00 24.52 ? 227 PHE B O   1 
ATOM   4116 C  CB  . PHE B 1 238 ? -21.605 1.913   -3.327  1.00 28.58 ? 227 PHE B CB  1 
ATOM   4117 C  CG  . PHE B 1 238 ? -20.225 2.440   -3.136  1.00 29.79 ? 227 PHE B CG  1 
ATOM   4118 C  CD1 . PHE B 1 238 ? -20.011 3.603   -2.399  1.00 28.96 ? 227 PHE B CD1 1 
ATOM   4119 C  CD2 . PHE B 1 238 ? -19.133 1.768   -3.680  1.00 24.66 ? 227 PHE B CD2 1 
ATOM   4120 C  CE1 . PHE B 1 238 ? -18.734 4.102   -2.214  1.00 27.00 ? 227 PHE B CE1 1 
ATOM   4121 C  CE2 . PHE B 1 238 ? -17.854 2.255   -3.500  1.00 33.71 ? 227 PHE B CE2 1 
ATOM   4122 C  CZ  . PHE B 1 238 ? -17.650 3.440   -2.772  1.00 30.31 ? 227 PHE B CZ  1 
ATOM   4123 N  N   . PHE B 1 239 ? -23.967 -0.115  -2.883  1.00 29.77 ? 228 PHE B N   1 
ATOM   4124 C  CA  . PHE B 1 239 ? -25.231 -0.439  -3.530  1.00 32.51 ? 228 PHE B CA  1 
ATOM   4125 C  C   . PHE B 1 239 ? -26.078 -1.430  -2.730  1.00 34.16 ? 228 PHE B C   1 
ATOM   4126 O  O   . PHE B 1 239 ? -27.054 -1.973  -3.259  1.00 32.57 ? 228 PHE B O   1 
ATOM   4127 C  CB  . PHE B 1 239 ? -24.947 -0.941  -4.952  1.00 32.53 ? 228 PHE B CB  1 
ATOM   4128 C  CG  . PHE B 1 239 ? -24.058 -0.002  -5.754  1.00 31.48 ? 228 PHE B CG  1 
ATOM   4129 C  CD1 . PHE B 1 239 ? -24.505 1.272   -6.105  1.00 31.26 ? 228 PHE B CD1 1 
ATOM   4130 C  CD2 . PHE B 1 239 ? -22.762 -0.379  -6.123  1.00 29.97 ? 228 PHE B CD2 1 
ATOM   4131 C  CE1 . PHE B 1 239 ? -23.691 2.144   -6.821  1.00 30.40 ? 228 PHE B CE1 1 
ATOM   4132 C  CE2 . PHE B 1 239 ? -21.940 0.481   -6.847  1.00 27.27 ? 228 PHE B CE2 1 
ATOM   4133 C  CZ  . PHE B 1 239 ? -22.405 1.741   -7.202  1.00 31.40 ? 228 PHE B CZ  1 
ATOM   4134 N  N   . LEU B 1 240 ? -25.727 -1.664  -1.466  1.00 32.77 ? 229 LEU B N   1 
ATOM   4135 C  CA  . LEU B 1 240 ? -26.528 -2.423  -0.515  1.00 31.52 ? 229 LEU B CA  1 
ATOM   4136 C  C   . LEU B 1 240 ? -26.141 -1.958  0.885   1.00 33.00 ? 229 LEU B C   1 
ATOM   4137 O  O   . LEU B 1 240 ? -25.040 -1.450  1.096   1.00 30.42 ? 229 LEU B O   1 
ATOM   4138 C  CB  . LEU B 1 240 ? -26.323 -3.935  -0.664  1.00 30.27 ? 229 LEU B CB  1 
ATOM   4139 C  CG  . LEU B 1 240 ? -27.579 -4.798  -0.651  1.00 32.31 ? 229 LEU B CG  1 
ATOM   4140 C  CD1 . LEU B 1 240 ? -28.539 -4.327  -1.724  1.00 29.46 ? 229 LEU B CD1 1 
ATOM   4141 C  CD2 . LEU B 1 240 ? -27.233 -6.280  -0.815  1.00 22.97 ? 229 LEU B CD2 1 
ATOM   4142 N  N   . GLY B 1 241 ? -27.062 -2.105  1.837   1.00 35.49 ? 230 GLY B N   1 
ATOM   4143 C  CA  . GLY B 1 241 ? -26.801 -1.699  3.205   1.00 29.14 ? 230 GLY B CA  1 
ATOM   4144 C  C   . GLY B 1 241 ? -27.613 -0.531  3.710   1.00 29.16 ? 230 GLY B C   1 
ATOM   4145 O  O   . GLY B 1 241 ? -27.401 -0.107  4.851   1.00 31.03 ? 230 GLY B O   1 
ATOM   4146 N  N   . HIS B 1 242 ? -28.519 0.014   2.906   1.00 34.02 ? 231 HIS B N   1 
ATOM   4147 C  CA  . HIS B 1 242 ? -29.423 1.047   3.379   1.00 33.00 ? 231 HIS B CA  1 
ATOM   4148 C  C   . HIS B 1 242 ? -30.376 0.488   4.433   1.00 36.93 ? 231 HIS B C   1 
ATOM   4149 O  O   . HIS B 1 242 ? -30.679 -0.713  4.454   1.00 33.70 ? 231 HIS B O   1 
ATOM   4150 C  CB  . HIS B 1 242 ? -30.230 1.620   2.217   1.00 34.77 ? 231 HIS B CB  1 
ATOM   4151 C  CG  . HIS B 1 242 ? -29.396 2.134   1.088   1.00 37.38 ? 231 HIS B CG  1 
ATOM   4152 N  ND1 . HIS B 1 242 ? -28.942 3.433   1.033   1.00 38.15 ? 231 HIS B ND1 1 
ATOM   4153 C  CD2 . HIS B 1 242 ? -28.957 1.534   -0.045  1.00 42.20 ? 231 HIS B CD2 1 
ATOM   4154 C  CE1 . HIS B 1 242 ? -28.250 3.610   -0.080  1.00 39.90 ? 231 HIS B CE1 1 
ATOM   4155 N  NE2 . HIS B 1 242 ? -28.250 2.475   -0.756  1.00 40.18 ? 231 HIS B NE2 1 
ATOM   4156 N  N   . ALA B 1 243 ? -30.874 1.388   5.301   1.00 37.87 ? 232 ALA B N   1 
ATOM   4157 C  CA  . ALA B 1 243 ? -31.781 0.998   6.382   1.00 32.64 ? 232 ALA B CA  1 
ATOM   4158 C  C   . ALA B 1 243 ? -33.134 0.508   5.889   1.00 31.44 ? 232 ALA B C   1 
ATOM   4159 O  O   . ALA B 1 243 ? -33.817 -0.206  6.625   1.00 34.75 ? 232 ALA B O   1 
ATOM   4160 C  CB  . ALA B 1 243 ? -32.001 2.161   7.339   1.00 26.28 ? 232 ALA B CB  1 
ATOM   4161 N  N   . ASP B 1 244 ? -33.535 0.870   4.672   1.00 36.83 ? 233 ASP B N   1 
ATOM   4162 C  CA  . ASP B 1 244 ? -34.837 0.501   4.127   1.00 33.47 ? 233 ASP B CA  1 
ATOM   4163 C  C   . ASP B 1 244 ? -34.854 -0.882  3.490   1.00 34.74 ? 233 ASP B C   1 
ATOM   4164 O  O   . ASP B 1 244 ? -35.888 -1.277  2.946   1.00 41.01 ? 233 ASP B O   1 
ATOM   4165 C  CB  . ASP B 1 244 ? -35.297 1.562   3.114   1.00 33.59 ? 233 ASP B CB  1 
ATOM   4166 C  CG  . ASP B 1 244 ? -34.405 1.643   1.879   1.00 45.23 ? 233 ASP B CG  1 
ATOM   4167 O  OD1 . ASP B 1 244 ? -33.245 1.178   1.935   1.00 45.86 ? 233 ASP B OD1 1 
ATOM   4168 O  OD2 . ASP B 1 244 ? -34.862 2.187   0.845   1.00 46.17 ? 233 ASP B OD2 1 
ATOM   4169 N  N   . GLU B 1 245 ? -33.746 -1.624  3.543   1.00 38.24 ? 234 GLU B N   1 
ATOM   4170 C  CA  . GLU B 1 245 ? -33.660 -2.984  3.005   1.00 34.81 ? 234 GLU B CA  1 
ATOM   4171 C  C   . GLU B 1 245 ? -34.005 -3.932  4.143   1.00 32.30 ? 234 GLU B C   1 
ATOM   4172 O  O   . GLU B 1 245 ? -33.144 -4.320  4.933   1.00 34.89 ? 234 GLU B O   1 
ATOM   4173 C  CB  . GLU B 1 245 ? -32.271 -3.258  2.431   1.00 35.10 ? 234 GLU B CB  1 
ATOM   4174 C  CG  . GLU B 1 245 ? -31.865 -2.330  1.270   1.00 35.03 ? 234 GLU B CG  1 
ATOM   4175 C  CD  . GLU B 1 245 ? -30.344 -2.209  1.071   1.00 37.27 ? 234 GLU B CD  1 
ATOM   4176 O  OE1 . GLU B 1 245 ? -29.570 -2.859  1.808   1.00 35.18 ? 234 GLU B OE1 1 
ATOM   4177 O  OE2 . GLU B 1 245 ? -29.917 -1.450  0.172   1.00 36.71 ? 234 GLU B OE2 1 
ATOM   4178 N  N   . HIS B 1 246 ? -35.292 -4.276  4.250   1.00 35.27 ? 235 HIS B N   1 
ATOM   4179 C  CA  . HIS B 1 246 ? -35.803 -5.108  5.333   1.00 33.83 ? 235 HIS B CA  1 
ATOM   4180 C  C   . HIS B 1 246 ? -36.023 -6.559  4.925   1.00 44.96 ? 235 HIS B C   1 
ATOM   4181 O  O   . HIS B 1 246 ? -36.453 -7.362  5.761   1.00 49.83 ? 235 HIS B O   1 
ATOM   4182 C  CB  . HIS B 1 246 ? -37.135 -4.577  5.862   1.00 29.62 ? 235 HIS B CB  1 
ATOM   4183 C  CG  . HIS B 1 246 ? -37.139 -3.130  6.220   1.00 34.39 ? 235 HIS B CG  1 
ATOM   4184 N  ND1 . HIS B 1 246 ? -36.413 -2.620  7.274   1.00 39.56 ? 235 HIS B ND1 1 
ATOM   4185 C  CD2 . HIS B 1 246 ? -37.825 -2.085  5.691   1.00 36.62 ? 235 HIS B CD2 1 
ATOM   4186 C  CE1 . HIS B 1 246 ? -36.637 -1.319  7.366   1.00 38.32 ? 235 HIS B CE1 1 
ATOM   4187 N  NE2 . HIS B 1 246 ? -37.489 -0.969  6.417   1.00 35.40 ? 235 HIS B NE2 1 
ATOM   4188 N  N   . GLY B 1 247 ? -35.800 -6.909  3.669   1.00 41.21 ? 236 GLY B N   1 
ATOM   4189 C  CA  . GLY B 1 247 ? -36.022 -8.278  3.268   1.00 38.80 ? 236 GLY B CA  1 
ATOM   4190 C  C   . GLY B 1 247 ? -37.149 -8.399  2.257   1.00 45.07 ? 236 GLY B C   1 
ATOM   4191 O  O   . GLY B 1 247 ? -37.976 -7.500  2.081   1.00 46.36 ? 236 GLY B O   1 
ATOM   4192 N  N   . GLU B 1 248 ? -37.177 -9.552  1.604   1.00 43.25 ? 237 GLU B N   1 
ATOM   4193 C  CA  . GLU B 1 248 ? -38.061 -9.836  0.489   1.00 45.68 ? 237 GLU B CA  1 
ATOM   4194 C  C   . GLU B 1 248 ? -38.990 -10.985 0.866   1.00 51.10 ? 237 GLU B C   1 
ATOM   4195 O  O   . GLU B 1 248 ? -38.576 -11.928 1.551   1.00 46.71 ? 237 GLU B O   1 
ATOM   4196 C  CB  . GLU B 1 248 ? -37.218 -10.194 -0.750  1.00 49.52 ? 237 GLU B CB  1 
ATOM   4197 C  CG  . GLU B 1 248 ? -37.768 -9.744  -2.088  1.00 54.78 ? 237 GLU B CG  1 
ATOM   4198 C  CD  . GLU B 1 248 ? -38.931 -10.611 -2.558  1.00 70.32 ? 237 GLU B CD  1 
ATOM   4199 O  OE1 . GLU B 1 248 ? -38.793 -11.865 -2.544  1.00 61.72 ? 237 GLU B OE1 1 
ATOM   4200 O  OE2 . GLU B 1 248 ? -39.979 -10.034 -2.949  1.00 78.67 ? 237 GLU B OE2 1 
ATOM   4201 N  N   . GLY B 1 249 ? -40.250 -10.899 0.436   1.00 51.58 ? 238 GLY B N   1 
ATOM   4202 C  CA  . GLY B 1 249 ? -41.155 -12.032 0.590   1.00 44.87 ? 238 GLY B CA  1 
ATOM   4203 C  C   . GLY B 1 249 ? -41.281 -12.454 2.038   1.00 46.74 ? 238 GLY B C   1 
ATOM   4204 O  O   . GLY B 1 249 ? -41.440 -11.619 2.934   1.00 46.60 ? 238 GLY B O   1 
ATOM   4205 N  N   . THR B 1 250 ? -41.195 -13.766 2.293   1.00 44.75 ? 239 THR B N   1 
ATOM   4206 C  CA  . THR B 1 250 ? -41.247 -14.207 3.683   1.00 53.52 ? 239 THR B CA  1 
ATOM   4207 C  C   . THR B 1 250 ? -39.975 -13.870 4.454   1.00 55.78 ? 239 THR B C   1 
ATOM   4208 O  O   . THR B 1 250 ? -39.882 -14.231 5.635   1.00 58.75 ? 239 THR B O   1 
ATOM   4209 C  CB  . THR B 1 250 ? -41.532 -15.712 3.789   1.00 49.15 ? 239 THR B CB  1 
ATOM   4210 O  OG1 . THR B 1 250 ? -40.804 -16.419 2.786   1.00 46.14 ? 239 THR B OG1 1 
ATOM   4211 C  CG2 . THR B 1 250 ? -43.039 -15.993 3.649   1.00 44.19 ? 239 THR B CG2 1 
ATOM   4212 N  N   . GLY B 1 251 ? -39.001 -13.200 3.830   1.00 47.89 ? 240 GLY B N   1 
ATOM   4213 C  CA  . GLY B 1 251 ? -37.886 -12.636 4.553   1.00 40.60 ? 240 GLY B CA  1 
ATOM   4214 C  C   . GLY B 1 251 ? -38.128 -11.225 5.009   1.00 41.42 ? 240 GLY B C   1 
ATOM   4215 O  O   . GLY B 1 251 ? -37.237 -10.605 5.598   1.00 42.20 ? 240 GLY B O   1 
ATOM   4216 N  N   . GLU B 1 252 ? -39.326 -10.705 4.745   1.00 45.06 ? 241 GLU B N   1 
ATOM   4217 C  CA  . GLU B 1 252 ? -39.677 -9.326  5.064   1.00 44.58 ? 241 GLU B CA  1 
ATOM   4218 C  C   . GLU B 1 252 ? -39.623 -9.087  6.568   1.00 41.39 ? 241 GLU B C   1 
ATOM   4219 O  O   . GLU B 1 252 ? -40.270 -9.795  7.343   1.00 39.89 ? 241 GLU B O   1 
ATOM   4220 C  CB  . GLU B 1 252 ? -41.086 -9.023  4.550   1.00 45.85 ? 241 GLU B CB  1 
ATOM   4221 C  CG  . GLU B 1 252 ? -41.261 -7.890  3.536   1.00 50.01 ? 241 GLU B CG  1 
ATOM   4222 C  CD  . GLU B 1 252 ? -40.654 -6.564  3.955   1.00 58.09 ? 241 GLU B CD  1 
ATOM   4223 O  OE1 . GLU B 1 252 ? -40.112 -6.459  5.081   1.00 63.03 ? 241 GLU B OE1 1 
ATOM   4224 O  OE2 . GLU B 1 252 ? -40.745 -5.601  3.158   1.00 63.54 ? 241 GLU B OE2 1 
ATOM   4225 N  N   . GLY B 1 253 ? -38.861 -8.075  6.984   1.00 38.93 ? 242 GLY B N   1 
ATOM   4226 C  CA  . GLY B 1 253 ? -38.696 -7.784  8.396   1.00 37.59 ? 242 GLY B CA  1 
ATOM   4227 C  C   . GLY B 1 253 ? -37.616 -8.569  9.111   1.00 38.28 ? 242 GLY B C   1 
ATOM   4228 O  O   . GLY B 1 253 ? -37.453 -8.400  10.323  1.00 36.95 ? 242 GLY B O   1 
ATOM   4229 N  N   . PHE B 1 254 ? -36.870 -9.417  8.403   1.00 45.86 ? 243 PHE B N   1 
ATOM   4230 C  CA  . PHE B 1 254 ? -35.854 -10.275 8.997   1.00 41.80 ? 243 PHE B CA  1 
ATOM   4231 C  C   . PHE B 1 254 ? -34.457 -9.915  8.532   1.00 39.41 ? 243 PHE B C   1 
ATOM   4232 O  O   . PHE B 1 254 ? -33.541 -10.731 8.650   1.00 37.20 ? 243 PHE B O   1 
ATOM   4233 C  CB  . PHE B 1 254 ? -36.164 -11.738 8.698   1.00 41.36 ? 243 PHE B CB  1 
ATOM   4234 C  CG  . PHE B 1 254 ? -37.375 -12.219 9.413   1.00 53.04 ? 243 PHE B CG  1 
ATOM   4235 C  CD1 . PHE B 1 254 ? -37.275 -12.714 10.709  1.00 50.85 ? 243 PHE B CD1 1 
ATOM   4236 C  CD2 . PHE B 1 254 ? -38.625 -12.123 8.827   1.00 47.99 ? 243 PHE B CD2 1 
ATOM   4237 C  CE1 . PHE B 1 254 ? -38.399 -13.124 11.389  1.00 44.17 ? 243 PHE B CE1 1 
ATOM   4238 C  CE2 . PHE B 1 254 ? -39.747 -12.536 9.511   1.00 47.72 ? 243 PHE B CE2 1 
ATOM   4239 C  CZ  . PHE B 1 254 ? -39.634 -13.032 10.792  1.00 41.19 ? 243 PHE B CZ  1 
ATOM   4240 N  N   . ASN B 1 255 ? -34.289 -8.695  8.023   1.00 43.20 ? 244 ASN B N   1 
ATOM   4241 C  CA  . ASN B 1 255 ? -33.019 -8.134  7.580   1.00 36.15 ? 244 ASN B CA  1 
ATOM   4242 C  C   . ASN B 1 255 ? -32.945 -6.729  8.160   1.00 36.62 ? 244 ASN B C   1 
ATOM   4243 O  O   . ASN B 1 255 ? -33.783 -5.886  7.832   1.00 38.87 ? 244 ASN B O   1 
ATOM   4244 C  CB  . ASN B 1 255 ? -32.958 -8.096  6.050   1.00 29.83 ? 244 ASN B CB  1 
ATOM   4245 C  CG  . ASN B 1 255 ? -31.582 -7.791  5.524   1.00 36.00 ? 244 ASN B CG  1 
ATOM   4246 O  OD1 . ASN B 1 255 ? -30.753 -8.693  5.366   1.00 38.40 ? 244 ASN B OD1 1 
ATOM   4247 N  ND2 . ASN B 1 255 ? -31.326 -6.516  5.223   1.00 32.46 ? 244 ASN B ND2 1 
ATOM   4248 N  N   . ILE B 1 256 ? -31.973 -6.479  9.033   1.00 35.12 ? 245 ILE B N   1 
ATOM   4249 C  CA  . ILE B 1 256 ? -31.882 -5.220  9.769   1.00 33.69 ? 245 ILE B CA  1 
ATOM   4250 C  C   . ILE B 1 256 ? -30.513 -4.579  9.532   1.00 32.00 ? 245 ILE B C   1 
ATOM   4251 O  O   . ILE B 1 256 ? -29.504 -5.015  10.097  1.00 34.16 ? 245 ILE B O   1 
ATOM   4252 C  CB  . ILE B 1 256 ? -32.136 -5.424  11.265  1.00 31.56 ? 245 ILE B CB  1 
ATOM   4253 C  CG1 . ILE B 1 256 ? -33.415 -6.223  11.474  1.00 29.41 ? 245 ILE B CG1 1 
ATOM   4254 C  CG2 . ILE B 1 256 ? -32.249 -4.088  11.946  1.00 32.14 ? 245 ILE B CG2 1 
ATOM   4255 C  CD1 . ILE B 1 256 ? -33.276 -7.301  12.458  1.00 37.79 ? 245 ILE B CD1 1 
ATOM   4256 N  N   . ASN B 1 257 ? -30.485 -3.520  8.738   1.00 31.18 ? 246 ASN B N   1 
ATOM   4257 C  CA  . ASN B 1 257 ? -29.273 -2.763  8.459   1.00 31.10 ? 246 ASN B CA  1 
ATOM   4258 C  C   . ASN B 1 257 ? -29.175 -1.522  9.349   1.00 32.33 ? 246 ASN B C   1 
ATOM   4259 O  O   . ASN B 1 257 ? -30.130 -0.744  9.446   1.00 29.36 ? 246 ASN B O   1 
ATOM   4260 C  CB  . ASN B 1 257 ? -29.262 -2.340  6.996   1.00 32.89 ? 246 ASN B CB  1 
ATOM   4261 C  CG  . ASN B 1 257 ? -28.722 -3.406  6.086   1.00 30.41 ? 246 ASN B CG  1 
ATOM   4262 O  OD1 . ASN B 1 257 ? -27.822 -4.164  6.459   1.00 31.87 ? 246 ASN B OD1 1 
ATOM   4263 N  ND2 . ASN B 1 257 ? -29.241 -3.450  4.867   1.00 26.96 ? 246 ASN B ND2 1 
ATOM   4264 N  N   . TYR B 1 258 ? -28.009 -1.333  9.986   1.00 28.72 ? 247 TYR B N   1 
ATOM   4265 C  CA  . TYR B 1 258 ? -27.716 -0.141  10.774  1.00 28.46 ? 247 TYR B CA  1 
ATOM   4266 C  C   . TYR B 1 258 ? -26.597 0.666   10.125  1.00 31.70 ? 247 TYR B C   1 
ATOM   4267 O  O   . TYR B 1 258 ? -25.437 0.576   10.557  1.00 29.86 ? 247 TYR B O   1 
ATOM   4268 C  CB  . TYR B 1 258 ? -27.308 -0.505  12.202  1.00 26.40 ? 247 TYR B CB  1 
ATOM   4269 C  CG  . TYR B 1 258 ? -28.376 -1.223  12.996  1.00 33.03 ? 247 TYR B CG  1 
ATOM   4270 C  CD1 . TYR B 1 258 ? -28.588 -2.593  12.832  1.00 30.28 ? 247 TYR B CD1 1 
ATOM   4271 C  CD2 . TYR B 1 258 ? -29.161 -0.543  13.924  1.00 27.26 ? 247 TYR B CD2 1 
ATOM   4272 C  CE1 . TYR B 1 258 ? -29.542 -3.256  13.555  1.00 27.40 ? 247 TYR B CE1 1 
ATOM   4273 C  CE2 . TYR B 1 258 ? -30.130 -1.202  14.648  1.00 29.78 ? 247 TYR B CE2 1 
ATOM   4274 C  CZ  . TYR B 1 258 ? -30.327 -2.562  14.452  1.00 32.70 ? 247 TYR B CZ  1 
ATOM   4275 O  OH  . TYR B 1 258 ? -31.295 -3.237  15.179  1.00 39.25 ? 247 TYR B OH  1 
ATOM   4276 N  N   . PRO B 1 259 ? -26.897 1.464   9.100   1.00 30.43 ? 248 PRO B N   1 
ATOM   4277 C  CA  . PRO B 1 259 ? -25.868 2.341   8.520   1.00 32.49 ? 248 PRO B CA  1 
ATOM   4278 C  C   . PRO B 1 259 ? -25.562 3.524   9.431   1.00 30.38 ? 248 PRO B C   1 
ATOM   4279 O  O   . PRO B 1 259 ? -26.456 4.103   10.054  1.00 29.90 ? 248 PRO B O   1 
ATOM   4280 C  CB  . PRO B 1 259 ? -26.495 2.805   7.200   1.00 33.60 ? 248 PRO B CB  1 
ATOM   4281 C  CG  . PRO B 1 259 ? -27.964 2.763   7.457   1.00 36.12 ? 248 PRO B CG  1 
ATOM   4282 C  CD  . PRO B 1 259 ? -28.198 1.606   8.428   1.00 31.48 ? 248 PRO B CD  1 
ATOM   4283 N  N   . LEU B 1 260 ? -24.289 3.886   9.496   1.00 27.09 ? 249 LEU B N   1 
ATOM   4284 C  CA  . LEU B 1 260 ? -23.840 4.928   10.404  1.00 31.75 ? 249 LEU B CA  1 
ATOM   4285 C  C   . LEU B 1 260 ? -23.011 5.973   9.670   1.00 33.72 ? 249 LEU B C   1 
ATOM   4286 O  O   . LEU B 1 260 ? -22.298 5.658   8.706   1.00 34.55 ? 249 LEU B O   1 
ATOM   4287 C  CB  . LEU B 1 260 ? -23.015 4.343   11.566  1.00 37.65 ? 249 LEU B CB  1 
ATOM   4288 C  CG  . LEU B 1 260 ? -23.812 3.605   12.652  1.00 38.38 ? 249 LEU B CG  1 
ATOM   4289 C  CD1 . LEU B 1 260 ? -22.883 2.951   13.666  1.00 37.29 ? 249 LEU B CD1 1 
ATOM   4290 C  CD2 . LEU B 1 260 ? -24.772 4.548   13.351  1.00 34.89 ? 249 LEU B CD2 1 
ATOM   4291 N  N   . PRO B 1 261 ? -23.092 7.229   10.106  1.00 35.44 ? 250 PRO B N   1 
ATOM   4292 C  CA  . PRO B 1 261 ? -22.282 8.287   9.496   1.00 29.83 ? 250 PRO B CA  1 
ATOM   4293 C  C   . PRO B 1 261 ? -20.807 8.160   9.829   1.00 31.13 ? 250 PRO B C   1 
ATOM   4294 O  O   . PRO B 1 261 ? -20.406 7.573   10.841  1.00 30.85 ? 250 PRO B O   1 
ATOM   4295 C  CB  . PRO B 1 261 ? -22.860 9.562   10.106  1.00 25.45 ? 250 PRO B CB  1 
ATOM   4296 C  CG  . PRO B 1 261 ? -23.539 9.131   11.327  1.00 21.18 ? 250 PRO B CG  1 
ATOM   4297 C  CD  . PRO B 1 261 ? -24.050 7.772   11.082  1.00 29.19 ? 250 PRO B CD  1 
ATOM   4298 N  N   . ALA B 1 262 ? -19.997 8.751   8.953   1.00 33.10 ? 251 ALA B N   1 
ATOM   4299 C  CA  . ALA B 1 262 ? -18.565 8.856   9.201   1.00 33.39 ? 251 ALA B CA  1 
ATOM   4300 C  C   . ALA B 1 262 ? -18.313 9.558   10.533  1.00 31.03 ? 251 ALA B C   1 
ATOM   4301 O  O   . ALA B 1 262 ? -19.100 10.395  10.978  1.00 34.84 ? 251 ALA B O   1 
ATOM   4302 C  CB  . ALA B 1 262 ? -17.886 9.610   8.055   1.00 28.87 ? 251 ALA B CB  1 
ATOM   4303 N  N   . GLY B 1 263 ? -17.219 9.187   11.191  1.00 34.81 ? 252 GLY B N   1 
ATOM   4304 C  CA  . GLY B 1 263 ? -16.888 9.738   12.488  1.00 25.49 ? 252 GLY B CA  1 
ATOM   4305 C  C   . GLY B 1 263 ? -17.618 9.120   13.659  1.00 30.08 ? 252 GLY B C   1 
ATOM   4306 O  O   . GLY B 1 263 ? -17.377 9.539   14.796  1.00 28.35 ? 252 GLY B O   1 
ATOM   4307 N  N   . SER B 1 264 ? -18.484 8.127   13.425  1.00 34.88 ? 253 SER B N   1 
ATOM   4308 C  CA  . SER B 1 264 ? -19.213 7.477   14.510  1.00 28.67 ? 253 SER B CA  1 
ATOM   4309 C  C   . SER B 1 264 ? -18.249 6.859   15.510  1.00 35.32 ? 253 SER B C   1 
ATOM   4310 O  O   . SER B 1 264 ? -17.226 6.277   15.131  1.00 34.12 ? 253 SER B O   1 
ATOM   4311 C  CB  . SER B 1 264 ? -20.140 6.395   13.961  1.00 27.44 ? 253 SER B CB  1 
ATOM   4312 O  OG  . SER B 1 264 ? -21.363 6.947   13.509  1.00 33.03 ? 253 SER B OG  1 
ATOM   4313 N  N   . ALA B 1 265 ? -18.575 7.002   16.798  1.00 36.26 ? 254 ALA B N   1 
ATOM   4314 C  CA  . ALA B 1 265 ? -17.847 6.377   17.897  1.00 29.32 ? 254 ALA B CA  1 
ATOM   4315 C  C   . ALA B 1 265 ? -18.801 5.466   18.690  1.00 37.01 ? 254 ALA B C   1 
ATOM   4316 O  O   . ALA B 1 265 ? -19.938 5.178   18.265  1.00 31.69 ? 254 ALA B O   1 
ATOM   4317 C  CB  . ALA B 1 265 ? -17.185 7.435   18.783  1.00 19.88 ? 254 ALA B CB  1 
ATOM   4318 N  N   . TRP B 1 266 ? -18.324 5.012   19.858  1.00 34.69 ? 255 TRP B N   1 
ATOM   4319 C  CA  . TRP B 1 266 ? -18.996 3.949   20.597  1.00 30.76 ? 255 TRP B CA  1 
ATOM   4320 C  C   . TRP B 1 266 ? -20.383 4.353   21.121  1.00 32.87 ? 255 TRP B C   1 
ATOM   4321 O  O   . TRP B 1 266 ? -21.218 3.472   21.350  1.00 31.99 ? 255 TRP B O   1 
ATOM   4322 C  CB  . TRP B 1 266 ? -18.101 3.470   21.757  1.00 26.80 ? 255 TRP B CB  1 
ATOM   4323 C  CG  . TRP B 1 266 ? -18.751 2.397   22.551  1.00 25.35 ? 255 TRP B CG  1 
ATOM   4324 C  CD1 . TRP B 1 266 ? -19.363 2.536   23.751  1.00 27.55 ? 255 TRP B CD1 1 
ATOM   4325 C  CD2 . TRP B 1 266 ? -18.912 1.017   22.170  1.00 32.66 ? 255 TRP B CD2 1 
ATOM   4326 N  NE1 . TRP B 1 266 ? -19.900 1.334   24.155  1.00 32.41 ? 255 TRP B NE1 1 
ATOM   4327 C  CE2 . TRP B 1 266 ? -19.638 0.383   23.205  1.00 32.28 ? 255 TRP B CE2 1 
ATOM   4328 C  CE3 . TRP B 1 266 ? -18.516 0.259   21.055  1.00 26.21 ? 255 TRP B CE3 1 
ATOM   4329 C  CZ2 . TRP B 1 266 ? -19.960 -0.983  23.175  1.00 25.59 ? 255 TRP B CZ2 1 
ATOM   4330 C  CZ3 . TRP B 1 266 ? -18.852 -1.087  21.017  1.00 29.70 ? 255 TRP B CZ3 1 
ATOM   4331 C  CH2 . TRP B 1 266 ? -19.561 -1.698  22.077  1.00 26.77 ? 255 TRP B CH2 1 
ATOM   4332 N  N   . ASP B 1 267 ? -20.657 5.648   21.332  1.00 29.84 ? 256 ASP B N   1 
ATOM   4333 C  CA  . ASP B 1 267 ? -21.996 6.028   21.779  1.00 33.92 ? 256 ASP B CA  1 
ATOM   4334 C  C   . ASP B 1 267 ? -23.048 5.682   20.723  1.00 38.94 ? 256 ASP B C   1 
ATOM   4335 O  O   . ASP B 1 267 ? -24.158 5.241   21.058  1.00 35.90 ? 256 ASP B O   1 
ATOM   4336 C  CB  . ASP B 1 267 ? -22.050 7.518   22.166  1.00 31.65 ? 256 ASP B CB  1 
ATOM   4337 C  CG  . ASP B 1 267 ? -21.587 8.478   21.045  1.00 42.20 ? 256 ASP B CG  1 
ATOM   4338 O  OD1 . ASP B 1 267 ? -20.735 8.090   20.210  1.00 37.19 ? 256 ASP B OD1 1 
ATOM   4339 O  OD2 . ASP B 1 267 ? -22.066 9.650   21.024  1.00 42.17 ? 256 ASP B OD2 1 
ATOM   4340 N  N   . SER B 1 268 ? -22.699 5.826   19.444  1.00 35.62 ? 257 SER B N   1 
ATOM   4341 C  CA  . SER B 1 268 ? -23.564 5.466   18.330  1.00 34.24 ? 257 SER B CA  1 
ATOM   4342 C  C   . SER B 1 268 ? -23.412 4.000   17.955  1.00 34.38 ? 257 SER B C   1 
ATOM   4343 O  O   . SER B 1 268 ? -24.401 3.275   17.814  1.00 31.53 ? 257 SER B O   1 
ATOM   4344 C  CB  . SER B 1 268 ? -23.227 6.326   17.119  1.00 35.39 ? 257 SER B CB  1 
ATOM   4345 O  OG  . SER B 1 268 ? -22.478 7.450   17.525  1.00 41.52 ? 257 SER B OG  1 
ATOM   4346 N  N   . TRP B 1 269 ? -22.170 3.555   17.788  1.00 34.34 ? 258 TRP B N   1 
ATOM   4347 C  CA  . TRP B 1 269 ? -21.951 2.186   17.359  1.00 31.40 ? 258 TRP B CA  1 
ATOM   4348 C  C   . TRP B 1 269 ? -22.509 1.200   18.376  1.00 30.03 ? 258 TRP B C   1 
ATOM   4349 O  O   . TRP B 1 269 ? -23.244 0.273   18.014  1.00 35.51 ? 258 TRP B O   1 
ATOM   4350 C  CB  . TRP B 1 269 ? -20.467 1.951   17.105  1.00 32.41 ? 258 TRP B CB  1 
ATOM   4351 C  CG  . TRP B 1 269 ? -20.229 0.755   16.244  1.00 29.24 ? 258 TRP B CG  1 
ATOM   4352 C  CD1 . TRP B 1 269 ? -19.960 0.739   14.909  1.00 31.00 ? 258 TRP B CD1 1 
ATOM   4353 C  CD2 . TRP B 1 269 ? -20.264 -0.601  16.666  1.00 24.83 ? 258 TRP B CD2 1 
ATOM   4354 N  NE1 . TRP B 1 269 ? -19.808 -0.547  14.476  1.00 30.17 ? 258 TRP B NE1 1 
ATOM   4355 C  CE2 . TRP B 1 269 ? -19.999 -1.393  15.536  1.00 30.35 ? 258 TRP B CE2 1 
ATOM   4356 C  CE3 . TRP B 1 269 ? -20.475 -1.225  17.900  1.00 21.52 ? 258 TRP B CE3 1 
ATOM   4357 C  CZ2 . TRP B 1 269 ? -19.942 -2.788  15.596  1.00 34.36 ? 258 TRP B CZ2 1 
ATOM   4358 C  CZ3 . TRP B 1 269 ? -20.420 -2.595  17.963  1.00 29.08 ? 258 TRP B CZ3 1 
ATOM   4359 C  CH2 . TRP B 1 269 ? -20.161 -3.371  16.815  1.00 31.16 ? 258 TRP B CH2 1 
ATOM   4360 N  N   . GLY B 1 270 ? -22.193 1.395   19.659  1.00 26.64 ? 259 GLY B N   1 
ATOM   4361 C  CA  . GLY B 1 270 ? -22.761 0.539   20.697  1.00 27.28 ? 259 GLY B CA  1 
ATOM   4362 C  C   . GLY B 1 270 ? -24.278 0.622   20.811  1.00 27.02 ? 259 GLY B C   1 
ATOM   4363 O  O   . GLY B 1 270 ? -24.920 -0.310  21.288  1.00 23.57 ? 259 GLY B O   1 
ATOM   4364 N  N   . ALA B 1 271 ? -24.871 1.735   20.379  1.00 31.33 ? 260 ALA B N   1 
ATOM   4365 C  CA  . ALA B 1 271 ? -26.328 1.848   20.375  1.00 29.21 ? 260 ALA B CA  1 
ATOM   4366 C  C   . ALA B 1 271 ? -26.945 0.928   19.330  1.00 34.10 ? 260 ALA B C   1 
ATOM   4367 O  O   . ALA B 1 271 ? -27.878 0.169   19.629  1.00 35.31 ? 260 ALA B O   1 
ATOM   4368 C  CB  . ALA B 1 271 ? -26.736 3.297   20.126  1.00 32.16 ? 260 ALA B CB  1 
ATOM   4369 N  N   . ALA B 1 272 ? -26.439 0.989   18.092  1.00 33.64 ? 261 ALA B N   1 
ATOM   4370 C  CA  . ALA B 1 272 ? -26.820 0.017   17.071  1.00 33.39 ? 261 ALA B CA  1 
ATOM   4371 C  C   . ALA B 1 272 ? -26.663 -1.410  17.583  1.00 32.24 ? 261 ALA B C   1 
ATOM   4372 O  O   . ALA B 1 272 ? -27.600 -2.214  17.510  1.00 29.96 ? 261 ALA B O   1 
ATOM   4373 C  CB  . ALA B 1 272 ? -25.982 0.225   15.808  1.00 31.15 ? 261 ALA B CB  1 
ATOM   4374 N  N   . LEU B 1 273 ? -25.475 -1.741  18.101  1.00 30.83 ? 262 LEU B N   1 
ATOM   4375 C  CA  . LEU B 1 273 ? -25.228 -3.102  18.567  1.00 31.62 ? 262 LEU B CA  1 
ATOM   4376 C  C   . LEU B 1 273 ? -26.225 -3.495  19.639  1.00 34.03 ? 262 LEU B C   1 
ATOM   4377 O  O   . LEU B 1 273 ? -26.683 -4.640  19.691  1.00 36.21 ? 262 LEU B O   1 
ATOM   4378 C  CB  . LEU B 1 273 ? -23.809 -3.233  19.108  1.00 28.60 ? 262 LEU B CB  1 
ATOM   4379 C  CG  . LEU B 1 273 ? -23.449 -4.646  19.557  1.00 29.48 ? 262 LEU B CG  1 
ATOM   4380 C  CD1 . LEU B 1 273 ? -23.054 -5.458  18.346  1.00 33.59 ? 262 LEU B CD1 1 
ATOM   4381 C  CD2 . LEU B 1 273 ? -22.335 -4.642  20.572  1.00 28.70 ? 262 LEU B CD2 1 
ATOM   4382 N  N   . ASP B 1 274 ? -26.588 -2.548  20.492  1.00 36.98 ? 263 ASP B N   1 
ATOM   4383 C  CA  . ASP B 1 274 ? -27.538 -2.849  21.549  1.00 34.29 ? 263 ASP B CA  1 
ATOM   4384 C  C   . ASP B 1 274 ? -28.922 -3.086  20.976  1.00 33.38 ? 263 ASP B C   1 
ATOM   4385 O  O   . ASP B 1 274 ? -29.650 -3.964  21.445  1.00 37.24 ? 263 ASP B O   1 
ATOM   4386 C  CB  . ASP B 1 274 ? -27.543 -1.717  22.564  1.00 37.44 ? 263 ASP B CB  1 
ATOM   4387 C  CG  . ASP B 1 274 ? -28.471 -1.979  23.692  1.00 41.19 ? 263 ASP B CG  1 
ATOM   4388 O  OD1 . ASP B 1 274 ? -28.481 -3.132  24.165  1.00 36.42 ? 263 ASP B OD1 1 
ATOM   4389 O  OD2 . ASP B 1 274 ? -29.173 -1.027  24.108  1.00 53.79 ? 263 ASP B OD2 1 
ATOM   4390 N  N   . ASP B 1 275 ? -29.284 -2.351  19.926  1.00 33.57 ? 264 ASP B N   1 
ATOM   4391 C  CA  . ASP B 1 275 ? -30.568 -2.609  19.288  1.00 32.60 ? 264 ASP B CA  1 
ATOM   4392 C  C   . ASP B 1 275 ? -30.543 -3.905  18.489  1.00 33.36 ? 264 ASP B C   1 
ATOM   4393 O  O   . ASP B 1 275 ? -31.518 -4.662  18.493  1.00 31.28 ? 264 ASP B O   1 
ATOM   4394 C  CB  . ASP B 1 275 ? -30.959 -1.441  18.399  1.00 26.16 ? 264 ASP B CB  1 
ATOM   4395 C  CG  . ASP B 1 275 ? -32.400 -1.520  17.976  1.00 40.71 ? 264 ASP B CG  1 
ATOM   4396 O  OD1 . ASP B 1 275 ? -33.271 -1.014  18.730  1.00 37.96 ? 264 ASP B OD1 1 
ATOM   4397 O  OD2 . ASP B 1 275 ? -32.661 -2.097  16.894  1.00 43.40 ? 264 ASP B OD2 1 
ATOM   4398 N  N   . ALA B 1 276 ? -29.435 -4.175  17.799  1.00 36.10 ? 265 ALA B N   1 
ATOM   4399 C  CA  . ALA B 1 276 ? -29.329 -5.393  17.004  1.00 35.06 ? 265 ALA B CA  1 
ATOM   4400 C  C   . ALA B 1 276 ? -29.413 -6.636  17.884  1.00 37.08 ? 265 ALA B C   1 
ATOM   4401 O  O   . ALA B 1 276 ? -30.068 -7.621  17.524  1.00 37.38 ? 265 ALA B O   1 
ATOM   4402 C  CB  . ALA B 1 276 ? -28.022 -5.381  16.208  1.00 29.69 ? 265 ALA B CB  1 
ATOM   4403 N  N   . CYS B 1 277 ? -28.758 -6.607  19.046  1.00 34.04 ? 266 CYS B N   1 
ATOM   4404 C  CA  . CYS B 1 277 ? -28.755 -7.779  19.910  1.00 32.94 ? 266 CYS B CA  1 
ATOM   4405 C  C   . CYS B 1 277 ? -30.124 -7.997  20.531  1.00 36.03 ? 266 CYS B C   1 
ATOM   4406 O  O   . CYS B 1 277 ? -30.577 -9.137  20.668  1.00 34.64 ? 266 CYS B O   1 
ATOM   4407 C  CB  . CYS B 1 277 ? -27.691 -7.620  20.992  1.00 33.66 ? 266 CYS B CB  1 
ATOM   4408 S  SG  . CYS B 1 277 ? -26.018 -7.790  20.371  1.00 37.36 ? 266 CYS B SG  1 
ATOM   4409 N  N   . LYS B 1 278 ? -30.782 -6.906  20.931  1.00 40.67 ? 267 LYS B N   1 
ATOM   4410 C  CA  . LYS B 1 278 ? -32.172 -6.973  21.355  1.00 37.48 ? 267 LYS B CA  1 
ATOM   4411 C  C   . LYS B 1 278 ? -33.023 -7.692  20.320  1.00 37.65 ? 267 LYS B C   1 
ATOM   4412 O  O   . LYS B 1 278 ? -33.838 -8.558  20.662  1.00 35.10 ? 267 LYS B O   1 
ATOM   4413 C  CB  . LYS B 1 278 ? -32.699 -5.560  21.582  1.00 30.08 ? 267 LYS B CB  1 
ATOM   4414 C  CG  . LYS B 1 278 ? -32.676 -5.130  23.024  1.00 31.32 ? 267 LYS B CG  1 
ATOM   4415 C  CD  . LYS B 1 278 ? -33.090 -3.684  23.155  1.00 35.89 ? 267 LYS B CD  1 
ATOM   4416 C  CE  . LYS B 1 278 ? -32.007 -2.817  23.743  1.00 35.23 ? 267 LYS B CE  1 
ATOM   4417 N  NZ  . LYS B 1 278 ? -32.147 -1.405  23.296  1.00 48.94 ? 267 LYS B NZ  1 
ATOM   4418 N  N   . ARG B 1 279 ? -32.827 -7.357  19.044  1.00 29.25 ? 268 ARG B N   1 
ATOM   4419 C  CA  . ARG B 1 279 ? -33.679 -7.879  17.993  1.00 25.68 ? 268 ARG B CA  1 
ATOM   4420 C  C   . ARG B 1 279 ? -33.331 -9.303  17.623  1.00 36.27 ? 268 ARG B C   1 
ATOM   4421 O  O   . ARG B 1 279 ? -34.217 -10.056 17.221  1.00 46.64 ? 268 ARG B O   1 
ATOM   4422 C  CB  . ARG B 1 279 ? -33.585 -6.998  16.765  1.00 35.30 ? 268 ARG B CB  1 
ATOM   4423 C  CG  . ARG B 1 279 ? -34.523 -5.829  16.835  1.00 37.04 ? 268 ARG B CG  1 
ATOM   4424 C  CD  . ARG B 1 279 ? -34.244 -4.851  15.725  1.00 43.19 ? 268 ARG B CD  1 
ATOM   4425 N  NE  . ARG B 1 279 ? -34.950 -3.602  15.971  1.00 59.50 ? 268 ARG B NE  1 
ATOM   4426 C  CZ  . ARG B 1 279 ? -36.270 -3.471  15.933  1.00 62.07 ? 268 ARG B CZ  1 
ATOM   4427 N  NH1 . ARG B 1 279 ? -37.053 -4.475  15.560  1.00 55.23 ? 268 ARG B NH1 1 
ATOM   4428 N  NH2 . ARG B 1 279 ? -36.816 -2.304  16.278  1.00 54.04 ? 268 ARG B NH2 1 
ATOM   4429 N  N   . ILE B 1 280 ? -32.057 -9.688  17.715  1.00 39.93 ? 269 ILE B N   1 
ATOM   4430 C  CA  . ILE B 1 280 ? -31.700 -11.096 17.557  1.00 34.03 ? 269 ILE B CA  1 
ATOM   4431 C  C   . ILE B 1 280 ? -32.435 -11.938 18.592  1.00 36.58 ? 269 ILE B C   1 
ATOM   4432 O  O   . ILE B 1 280 ? -33.007 -12.993 18.276  1.00 34.15 ? 269 ILE B O   1 
ATOM   4433 C  CB  . ILE B 1 280 ? -30.171 -11.263 17.658  1.00 31.24 ? 269 ILE B CB  1 
ATOM   4434 C  CG1 . ILE B 1 280 ? -29.498 -10.718 16.402  1.00 34.57 ? 269 ILE B CG1 1 
ATOM   4435 C  CG2 . ILE B 1 280 ? -29.768 -12.706 17.902  1.00 28.18 ? 269 ILE B CG2 1 
ATOM   4436 C  CD1 . ILE B 1 280 ? -28.027 -10.447 16.589  1.00 29.65 ? 269 ILE B CD1 1 
ATOM   4437 N  N   . ASN B 1 281 ? -32.455 -11.459 19.840  1.00 35.19 ? 270 ASN B N   1 
ATOM   4438 C  CA  . ASN B 1 281 ? -33.072 -12.192 20.935  1.00 31.68 ? 270 ASN B CA  1 
ATOM   4439 C  C   . ASN B 1 281 ? -34.584 -12.241 20.789  1.00 35.34 ? 270 ASN B C   1 
ATOM   4440 O  O   . ASN B 1 281 ? -35.202 -13.281 21.044  1.00 40.57 ? 270 ASN B O   1 
ATOM   4441 C  CB  . ASN B 1 281 ? -32.657 -11.556 22.249  1.00 28.28 ? 270 ASN B CB  1 
ATOM   4442 C  CG  . ASN B 1 281 ? -31.405 -12.173 22.799  1.00 37.61 ? 270 ASN B CG  1 
ATOM   4443 O  OD1 . ASN B 1 281 ? -30.563 -11.503 23.407  1.00 37.74 ? 270 ASN B OD1 1 
ATOM   4444 N  ND2 . ASN B 1 281 ? -31.284 -13.482 22.619  1.00 44.27 ? 270 ASN B ND2 1 
ATOM   4445 N  N   . ALA B 1 282 ? -35.196 -11.137 20.355  1.00 34.56 ? 271 ALA B N   1 
ATOM   4446 C  CA  . ALA B 1 282 ? -36.615 -11.157 20.014  1.00 34.55 ? 271 ALA B CA  1 
ATOM   4447 C  C   . ALA B 1 282 ? -36.922 -12.173 18.927  1.00 37.99 ? 271 ALA B C   1 
ATOM   4448 O  O   . ALA B 1 282 ? -38.056 -12.650 18.847  1.00 42.22 ? 271 ALA B O   1 
ATOM   4449 C  CB  . ALA B 1 282 ? -37.077 -9.776  19.558  1.00 22.17 ? 271 ALA B CB  1 
ATOM   4450 N  N   . PHE B 1 283 ? -35.928 -12.520 18.109  1.00 35.86 ? 272 PHE B N   1 
ATOM   4451 C  CA  . PHE B 1 283 ? -36.056 -13.442 16.996  1.00 34.59 ? 272 PHE B CA  1 
ATOM   4452 C  C   . PHE B 1 283 ? -35.943 -14.904 17.414  1.00 44.72 ? 272 PHE B C   1 
ATOM   4453 O  O   . PHE B 1 283 ? -36.274 -15.783 16.611  1.00 48.21 ? 272 PHE B O   1 
ATOM   4454 C  CB  . PHE B 1 283 ? -34.995 -13.095 15.935  1.00 42.14 ? 272 PHE B CB  1 
ATOM   4455 C  CG  . PHE B 1 283 ? -34.877 -14.095 14.809  1.00 44.08 ? 272 PHE B CG  1 
ATOM   4456 C  CD1 . PHE B 1 283 ? -35.842 -14.158 13.811  1.00 40.62 ? 272 PHE B CD1 1 
ATOM   4457 C  CD2 . PHE B 1 283 ? -33.782 -14.957 14.739  1.00 36.89 ? 272 PHE B CD2 1 
ATOM   4458 C  CE1 . PHE B 1 283 ? -35.734 -15.074 12.780  1.00 41.75 ? 272 PHE B CE1 1 
ATOM   4459 C  CE2 . PHE B 1 283 ? -33.665 -15.874 13.710  1.00 36.06 ? 272 PHE B CE2 1 
ATOM   4460 C  CZ  . PHE B 1 283 ? -34.638 -15.934 12.726  1.00 38.42 ? 272 PHE B CZ  1 
ATOM   4461 N  N   . ASP B 1 284 ? -35.534 -15.192 18.653  1.00 42.83 ? 273 ASP B N   1 
ATOM   4462 C  CA  . ASP B 1 284 ? -35.272 -16.566 19.077  1.00 37.40 ? 273 ASP B CA  1 
ATOM   4463 C  C   . ASP B 1 284 ? -34.229 -17.221 18.184  1.00 39.15 ? 273 ASP B C   1 
ATOM   4464 O  O   . ASP B 1 284 ? -34.408 -18.336 17.689  1.00 46.84 ? 273 ASP B O   1 
ATOM   4465 C  CB  . ASP B 1 284 ? -36.551 -17.405 19.120  1.00 42.36 ? 273 ASP B CB  1 
ATOM   4466 C  CG  . ASP B 1 284 ? -37.179 -17.442 20.497  1.00 57.33 ? 273 ASP B CG  1 
ATOM   4467 O  OD1 . ASP B 1 284 ? -36.600 -18.113 21.384  1.00 61.95 ? 273 ASP B OD1 1 
ATOM   4468 O  OD2 . ASP B 1 284 ? -38.244 -16.822 20.699  1.00 64.85 ? 273 ASP B OD2 1 
ATOM   4469 N  N   . ALA B 1 285 ? -33.132 -16.510 17.961  1.00 39.83 ? 274 ALA B N   1 
ATOM   4470 C  CA  . ALA B 1 285 ? -31.960 -17.165 17.410  1.00 38.68 ? 274 ALA B CA  1 
ATOM   4471 C  C   . ALA B 1 285 ? -31.516 -18.248 18.382  1.00 40.60 ? 274 ALA B C   1 
ATOM   4472 O  O   . ALA B 1 285 ? -31.497 -18.033 19.597  1.00 40.83 ? 274 ALA B O   1 
ATOM   4473 C  CB  . ALA B 1 285 ? -30.840 -16.153 17.162  1.00 30.18 ? 274 ALA B CB  1 
ATOM   4474 N  N   . GLU B 1 286 ? -31.239 -19.437 17.851  1.00 39.97 ? 275 GLU B N   1 
ATOM   4475 C  CA  . GLU B 1 286 ? -30.653 -20.512 18.644  1.00 44.73 ? 275 GLU B CA  1 
ATOM   4476 C  C   . GLU B 1 286 ? -29.127 -20.484 18.608  1.00 48.30 ? 275 GLU B C   1 
ATOM   4477 O  O   . GLU B 1 286 ? -28.469 -20.904 19.575  1.00 39.91 ? 275 GLU B O   1 
ATOM   4478 C  CB  . GLU B 1 286 ? -31.162 -21.870 18.145  1.00 41.58 ? 275 GLU B CB  1 
ATOM   4479 C  CG  . GLU B 1 286 ? -32.667 -22.069 18.275  1.00 46.69 ? 275 GLU B CG  1 
ATOM   4480 C  CD  . GLU B 1 286 ? -33.265 -22.948 17.173  1.00 55.34 ? 275 GLU B CD  1 
ATOM   4481 O  OE1 . GLU B 1 286 ? -32.638 -23.973 16.803  1.00 44.50 ? 275 GLU B OE1 1 
ATOM   4482 O  OE2 . GLU B 1 286 ? -34.370 -22.598 16.677  1.00 56.32 ? 275 GLU B OE2 1 
ATOM   4483 N  N   . VAL B 1 287 ? -28.564 -20.018 17.494  1.00 37.46 ? 276 VAL B N   1 
ATOM   4484 C  CA  . VAL B 1 287 ? -27.144 -19.746 17.351  1.00 40.30 ? 276 VAL B CA  1 
ATOM   4485 C  C   . VAL B 1 287 ? -27.003 -18.365 16.731  1.00 44.59 ? 276 VAL B C   1 
ATOM   4486 O  O   . VAL B 1 287 ? -27.793 -17.985 15.855  1.00 46.10 ? 276 VAL B O   1 
ATOM   4487 C  CB  . VAL B 1 287 ? -26.437 -20.804 16.478  1.00 40.71 ? 276 VAL B CB  1 
ATOM   4488 C  CG1 . VAL B 1 287 ? -24.921 -20.675 16.620  1.00 36.94 ? 276 VAL B CG1 1 
ATOM   4489 C  CG2 . VAL B 1 287 ? -26.904 -22.206 16.843  1.00 36.93 ? 276 VAL B CG2 1 
ATOM   4490 N  N   . VAL B 1 288 ? -26.017 -17.599 17.189  1.00 35.78 ? 277 VAL B N   1 
ATOM   4491 C  CA  . VAL B 1 288 ? -25.670 -16.339 16.541  1.00 41.12 ? 277 VAL B CA  1 
ATOM   4492 C  C   . VAL B 1 288 ? -24.278 -16.496 15.935  1.00 42.46 ? 277 VAL B C   1 
ATOM   4493 O  O   . VAL B 1 288 ? -23.360 -17.017 16.591  1.00 34.31 ? 277 VAL B O   1 
ATOM   4494 C  CB  . VAL B 1 288 ? -25.767 -15.137 17.504  1.00 35.01 ? 277 VAL B CB  1 
ATOM   4495 C  CG1 . VAL B 1 288 ? -25.388 -15.530 18.910  1.00 39.78 ? 277 VAL B CG1 1 
ATOM   4496 C  CG2 . VAL B 1 288 ? -24.890 -13.995 17.025  1.00 34.32 ? 277 VAL B CG2 1 
ATOM   4497 N  N   . ILE B 1 289 ? -24.149 -16.120 14.657  1.00 35.64 ? 278 ILE B N   1 
ATOM   4498 C  CA  . ILE B 1 289 ? -22.877 -16.150 13.939  1.00 35.09 ? 278 ILE B CA  1 
ATOM   4499 C  C   . ILE B 1 289 ? -22.422 -14.716 13.778  1.00 33.12 ? 278 ILE B C   1 
ATOM   4500 O  O   . ILE B 1 289 ? -23.119 -13.909 13.156  1.00 37.36 ? 278 ILE B O   1 
ATOM   4501 C  CB  . ILE B 1 289 ? -22.996 -16.833 12.569  1.00 32.96 ? 278 ILE B CB  1 
ATOM   4502 C  CG1 . ILE B 1 289 ? -23.438 -18.275 12.734  1.00 28.14 ? 278 ILE B CG1 1 
ATOM   4503 C  CG2 . ILE B 1 289 ? -21.665 -16.776 11.820  1.00 30.54 ? 278 ILE B CG2 1 
ATOM   4504 C  CD1 . ILE B 1 289 ? -24.893 -18.476 12.411  1.00 34.62 ? 278 ILE B CD1 1 
ATOM   4505 N  N   . VAL B 1 290 ? -21.273 -14.382 14.345  1.00 30.45 ? 279 VAL B N   1 
ATOM   4506 C  CA  . VAL B 1 290 ? -20.750 -13.026 14.256  1.00 31.10 ? 279 VAL B CA  1 
ATOM   4507 C  C   . VAL B 1 290 ? -19.742 -12.962 13.123  1.00 33.35 ? 279 VAL B C   1 
ATOM   4508 O  O   . VAL B 1 290 ? -18.714 -13.651 13.149  1.00 30.71 ? 279 VAL B O   1 
ATOM   4509 C  CB  . VAL B 1 290 ? -20.118 -12.562 15.572  1.00 31.00 ? 279 VAL B CB  1 
ATOM   4510 C  CG1 . VAL B 1 290 ? -19.816 -11.062 15.481  1.00 30.07 ? 279 VAL B CG1 1 
ATOM   4511 C  CG2 . VAL B 1 290 ? -21.053 -12.881 16.748  1.00 31.09 ? 279 VAL B CG2 1 
ATOM   4512 N  N   . SER B 1 291 ? -20.040 -12.132 12.126  1.00 35.88 ? 280 SER B N   1 
ATOM   4513 C  CA  . SER B 1 291 ? -19.085 -11.834 11.072  1.00 30.62 ? 280 SER B CA  1 
ATOM   4514 C  C   . SER B 1 291 ? -18.166 -10.745 11.600  1.00 32.86 ? 280 SER B C   1 
ATOM   4515 O  O   . SER B 1 291 ? -18.489 -9.561  11.532  1.00 32.91 ? 280 SER B O   1 
ATOM   4516 C  CB  . SER B 1 291 ? -19.799 -11.429 9.795   1.00 26.80 ? 280 SER B CB  1 
ATOM   4517 O  OG  . SER B 1 291 ? -19.787 -12.520 8.887   1.00 28.84 ? 280 SER B OG  1 
ATOM   4518 N  N   . LEU B 1 292 ? -17.007 -11.164 12.123  1.00 36.08 ? 281 LEU B N   1 
ATOM   4519 C  CA  . LEU B 1 292 ? -16.121 -10.323 12.930  1.00 34.31 ? 281 LEU B CA  1 
ATOM   4520 C  C   . LEU B 1 292 ? -15.108 -9.620  12.023  1.00 34.81 ? 281 LEU B C   1 
ATOM   4521 O  O   . LEU B 1 292 ? -14.142 -10.228 11.547  1.00 30.87 ? 281 LEU B O   1 
ATOM   4522 C  CB  . LEU B 1 292 ? -15.429 -11.161 14.008  1.00 30.39 ? 281 LEU B CB  1 
ATOM   4523 C  CG  . LEU B 1 292 ? -14.450 -10.417 14.938  1.00 35.33 ? 281 LEU B CG  1 
ATOM   4524 C  CD1 . LEU B 1 292 ? -15.049 -9.089  15.396  1.00 37.71 ? 281 LEU B CD1 1 
ATOM   4525 C  CD2 . LEU B 1 292 ? -14.013 -11.224 16.151  1.00 26.82 ? 281 LEU B CD2 1 
ATOM   4526 N  N   . GLY B 1 293 ? -15.332 -8.331  11.791  1.00 36.20 ? 282 GLY B N   1 
ATOM   4527 C  CA  . GLY B 1 293 ? -14.327 -7.442  11.217  1.00 35.40 ? 282 GLY B CA  1 
ATOM   4528 C  C   . GLY B 1 293 ? -13.903 -6.401  12.240  1.00 34.86 ? 282 GLY B C   1 
ATOM   4529 O  O   . GLY B 1 293 ? -14.716 -5.948  13.052  1.00 38.51 ? 282 GLY B O   1 
ATOM   4530 N  N   . VAL B 1 294 ? -12.624 -6.041  12.215  1.00 33.84 ? 283 VAL B N   1 
ATOM   4531 C  CA  . VAL B 1 294 ? -12.085 -5.036  13.122  1.00 37.98 ? 283 VAL B CA  1 
ATOM   4532 C  C   . VAL B 1 294 ? -11.653 -3.778  12.379  1.00 34.58 ? 283 VAL B C   1 
ATOM   4533 O  O   . VAL B 1 294 ? -10.933 -2.954  12.942  1.00 36.48 ? 283 VAL B O   1 
ATOM   4534 C  CB  . VAL B 1 294 ? -10.924 -5.597  13.966  1.00 32.76 ? 283 VAL B CB  1 
ATOM   4535 C  CG1 . VAL B 1 294 ? -11.469 -6.396  15.115  1.00 33.43 ? 283 VAL B CG1 1 
ATOM   4536 C  CG2 . VAL B 1 294 ? -10.013 -6.459  13.112  1.00 28.66 ? 283 VAL B CG2 1 
ATOM   4537 N  N   . ASP B 1 295 ? -12.061 -3.618  11.119  1.00 32.72 ? 284 ASP B N   1 
ATOM   4538 C  CA  . ASP B 1 295 ? -11.757 -2.404  10.368  1.00 37.15 ? 284 ASP B CA  1 
ATOM   4539 C  C   . ASP B 1 295 ? -12.655 -1.225  10.769  1.00 34.29 ? 284 ASP B C   1 
ATOM   4540 O  O   . ASP B 1 295 ? -12.766 -0.260  10.014  1.00 28.95 ? 284 ASP B O   1 
ATOM   4541 C  CB  . ASP B 1 295 ? -11.865 -2.666  8.863   1.00 28.27 ? 284 ASP B CB  1 
ATOM   4542 C  CG  . ASP B 1 295 ? -13.129 -3.401  8.500   1.00 31.42 ? 284 ASP B CG  1 
ATOM   4543 O  OD1 . ASP B 1 295 ? -13.790 -3.924  9.424   1.00 28.57 ? 284 ASP B OD1 1 
ATOM   4544 O  OD2 . ASP B 1 295 ? -13.466 -3.446  7.298   1.00 32.19 ? 284 ASP B OD2 1 
ATOM   4545 N  N   . THR B 1 296 ? -13.324 -1.314  11.920  1.00 30.65 ? 285 THR B N   1 
ATOM   4546 C  CA  . THR B 1 296 ? -13.991 -0.178  12.537  1.00 31.07 ? 285 THR B CA  1 
ATOM   4547 C  C   . THR B 1 296 ? -13.029 0.647   13.381  1.00 37.58 ? 285 THR B C   1 
ATOM   4548 O  O   . THR B 1 296 ? -13.384 1.759   13.798  1.00 34.05 ? 285 THR B O   1 
ATOM   4549 C  CB  . THR B 1 296 ? -15.155 -0.662  13.420  1.00 31.80 ? 285 THR B CB  1 
ATOM   4550 O  OG1 . THR B 1 296 ? -14.735 -1.790  14.197  1.00 31.83 ? 285 THR B OG1 1 
ATOM   4551 C  CG2 . THR B 1 296 ? -16.338 -1.073  12.604  1.00 30.26 ? 285 THR B CG2 1 
ATOM   4552 N  N   . TYR B 1 297 ? -11.834 0.104   13.631  1.00 34.16 ? 286 TYR B N   1 
ATOM   4553 C  CA  . TYR B 1 297 ? -10.816 0.722   14.469  1.00 31.96 ? 286 TYR B CA  1 
ATOM   4554 C  C   . TYR B 1 297 ? -10.443 2.110   13.953  1.00 34.96 ? 286 TYR B C   1 
ATOM   4555 O  O   . TYR B 1 297 ? -10.379 2.349   12.743  1.00 35.71 ? 286 TYR B O   1 
ATOM   4556 C  CB  . TYR B 1 297 ? -9.589  -0.199  14.489  1.00 35.36 ? 286 TYR B CB  1 
ATOM   4557 C  CG  . TYR B 1 297 ? -8.493  0.174   15.443  1.00 36.28 ? 286 TYR B CG  1 
ATOM   4558 C  CD1 . TYR B 1 297 ? -8.781  0.527   16.753  1.00 40.85 ? 286 TYR B CD1 1 
ATOM   4559 C  CD2 . TYR B 1 297 ? -7.166  0.169   15.037  1.00 34.51 ? 286 TYR B CD2 1 
ATOM   4560 C  CE1 . TYR B 1 297 ? -7.780  0.873   17.644  1.00 40.21 ? 286 TYR B CE1 1 
ATOM   4561 C  CE2 . TYR B 1 297 ? -6.153  0.507   15.921  1.00 39.93 ? 286 TYR B CE2 1 
ATOM   4562 C  CZ  . TYR B 1 297 ? -6.470  0.860   17.225  1.00 42.23 ? 286 TYR B CZ  1 
ATOM   4563 O  OH  . TYR B 1 297 ? -5.485  1.191   18.125  1.00 36.14 ? 286 TYR B OH  1 
ATOM   4564 N  N   . LYS B 1 298 ? -10.194 3.034   14.883  1.00 36.54 ? 287 LYS B N   1 
ATOM   4565 C  CA  . LYS B 1 298 ? -9.877  4.404   14.491  1.00 36.94 ? 287 LYS B CA  1 
ATOM   4566 C  C   . LYS B 1 298 ? -8.593  4.466   13.672  1.00 39.74 ? 287 LYS B C   1 
ATOM   4567 O  O   . LYS B 1 298 ? -8.487  5.270   12.738  1.00 40.08 ? 287 LYS B O   1 
ATOM   4568 C  CB  . LYS B 1 298 ? -9.755  5.306   15.724  1.00 40.34 ? 287 LYS B CB  1 
ATOM   4569 C  CG  . LYS B 1 298 ? -8.775  4.836   16.797  1.00 39.88 ? 287 LYS B CG  1 
ATOM   4570 C  CD  . LYS B 1 298 ? -8.445  5.966   17.770  1.00 45.27 ? 287 LYS B CD  1 
ATOM   4571 C  CE  . LYS B 1 298 ? -9.650  6.856   18.032  1.00 49.74 ? 287 LYS B CE  1 
ATOM   4572 N  NZ  . LYS B 1 298 ? -10.552 6.288   19.087  1.00 60.91 ? 287 LYS B NZ  1 
ATOM   4573 N  N   . GLU B 1 299 ? -7.609  3.631   14.007  1.00 35.69 ? 288 GLU B N   1 
ATOM   4574 C  CA  . GLU B 1 299 ? -6.313  3.648   13.347  1.00 35.01 ? 288 GLU B CA  1 
ATOM   4575 C  C   . GLU B 1 299 ? -6.260  2.759   12.117  1.00 34.58 ? 288 GLU B C   1 
ATOM   4576 O  O   . GLU B 1 299 ? -5.198  2.663   11.494  1.00 39.06 ? 288 GLU B O   1 
ATOM   4577 C  CB  . GLU B 1 299 ? -5.195  3.226   14.319  1.00 43.69 ? 288 GLU B CB  1 
ATOM   4578 C  CG  . GLU B 1 299 ? -5.026  4.067   15.591  1.00 43.83 ? 288 GLU B CG  1 
ATOM   4579 C  CD  . GLU B 1 299 ? -5.006  5.567   15.328  1.00 51.66 ? 288 GLU B CD  1 
ATOM   4580 O  OE1 . GLU B 1 299 ? -4.615  5.981   14.217  1.00 53.35 ? 288 GLU B OE1 1 
ATOM   4581 O  OE2 . GLU B 1 299 ? -5.381  6.338   16.239  1.00 58.33 ? 288 GLU B OE2 1 
ATOM   4582 N  N   . ASP B 1 300 ? -7.362  2.092   11.766  1.00 38.89 ? 289 ASP B N   1 
ATOM   4583 C  CA  . ASP B 1 300 ? -7.423  1.304   10.537  1.00 33.97 ? 289 ASP B CA  1 
ATOM   4584 C  C   . ASP B 1 300 ? -7.565  2.248   9.355   1.00 35.28 ? 289 ASP B C   1 
ATOM   4585 O  O   . ASP B 1 300 ? -8.439  3.119   9.374   1.00 37.12 ? 289 ASP B O   1 
ATOM   4586 C  CB  . ASP B 1 300 ? -8.597  0.315   10.560  1.00 40.15 ? 289 ASP B CB  1 
ATOM   4587 C  CG  . ASP B 1 300 ? -8.483  -0.779  9.485   1.00 41.23 ? 289 ASP B CG  1 
ATOM   4588 O  OD1 . ASP B 1 300 ? -8.500  -0.449  8.289   1.00 37.95 ? 289 ASP B OD1 1 
ATOM   4589 O  OD2 . ASP B 1 300 ? -8.380  -1.978  9.838   1.00 45.88 ? 289 ASP B OD2 1 
ATOM   4590 N  N   . PRO B 1 301 ? -6.727  2.107   8.324   1.00 41.07 ? 290 PRO B N   1 
ATOM   4591 C  CA  . PRO B 1 301 ? -6.733  3.081   7.218   1.00 34.87 ? 290 PRO B CA  1 
ATOM   4592 C  C   . PRO B 1 301 ? -8.024  3.116   6.434   1.00 40.78 ? 290 PRO B C   1 
ATOM   4593 O  O   . PRO B 1 301 ? -8.298  4.129   5.785   1.00 44.89 ? 290 PRO B O   1 
ATOM   4594 C  CB  . PRO B 1 301 ? -5.575  2.615   6.339   1.00 32.54 ? 290 PRO B CB  1 
ATOM   4595 C  CG  . PRO B 1 301 ? -4.756  1.725   7.224   1.00 41.73 ? 290 PRO B CG  1 
ATOM   4596 C  CD  . PRO B 1 301 ? -5.694  1.076   8.154   1.00 41.69 ? 290 PRO B CD  1 
ATOM   4597 N  N   . ILE B 1 302 ? -8.829  2.056   6.476   1.00 37.04 ? 291 ILE B N   1 
ATOM   4598 C  CA  . ILE B 1 302 ? -10.071 2.030   5.720   1.00 37.11 ? 291 ILE B CA  1 
ATOM   4599 C  C   . ILE B 1 302 ? -11.239 2.583   6.528   1.00 38.38 ? 291 ILE B C   1 
ATOM   4600 O  O   . ILE B 1 302 ? -12.280 2.926   5.942   1.00 39.37 ? 291 ILE B O   1 
ATOM   4601 C  CB  . ILE B 1 302 ? -10.398 0.599   5.247   1.00 46.30 ? 291 ILE B CB  1 
ATOM   4602 C  CG1 . ILE B 1 302 ? -9.153  -0.102  4.687   1.00 44.98 ? 291 ILE B CG1 1 
ATOM   4603 C  CG2 . ILE B 1 302 ? -11.402 0.638   4.123   1.00 43.12 ? 291 ILE B CG2 1 
ATOM   4604 C  CD1 . ILE B 1 302 ? -8.682  -1.307  5.511   1.00 46.86 ? 291 ILE B CD1 1 
ATOM   4605 N  N   . SER B 1 303 ? -11.095 2.702   7.847   1.00 34.22 ? 292 SER B N   1 
ATOM   4606 C  CA  . SER B 1 303 ? -12.230 3.032   8.701   1.00 38.69 ? 292 SER B CA  1 
ATOM   4607 C  C   . SER B 1 303 ? -12.585 4.514   8.638   1.00 42.52 ? 292 SER B C   1 
ATOM   4608 O  O   . SER B 1 303 ? -11.713 5.383   8.537   1.00 39.27 ? 292 SER B O   1 
ATOM   4609 C  CB  . SER B 1 303 ? -11.947 2.664   10.155  1.00 31.71 ? 292 SER B CB  1 
ATOM   4610 O  OG  . SER B 1 303 ? -13.071 2.996   10.960  1.00 33.12 ? 292 SER B OG  1 
ATOM   4611 N  N   . GLN B 1 304 ? -13.882 4.798   8.717   1.00 36.59 ? 293 GLN B N   1 
ATOM   4612 C  CA  . GLN B 1 304 ? -14.353 6.140   9.014   1.00 35.69 ? 293 GLN B CA  1 
ATOM   4613 C  C   . GLN B 1 304 ? -15.126 6.157   10.326  1.00 40.28 ? 293 GLN B C   1 
ATOM   4614 O  O   . GLN B 1 304 ? -15.878 7.105   10.600  1.00 32.49 ? 293 GLN B O   1 
ATOM   4615 C  CB  . GLN B 1 304 ? -15.190 6.691   7.861   1.00 36.94 ? 293 GLN B CB  1 
ATOM   4616 C  CG  . GLN B 1 304 ? -14.416 7.658   6.983   1.00 36.98 ? 293 GLN B CG  1 
ATOM   4617 C  CD  . GLN B 1 304 ? -15.007 7.778   5.601   1.00 48.92 ? 293 GLN B CD  1 
ATOM   4618 O  OE1 . GLN B 1 304 ? -16.124 8.266   5.440   1.00 55.77 ? 293 GLN B OE1 1 
ATOM   4619 N  NE2 . GLN B 1 304 ? -14.259 7.348   4.588   1.00 49.06 ? 293 GLN B NE2 1 
ATOM   4620 N  N   . PHE B 1 305 ? -14.958 5.112   11.137  1.00 35.65 ? 294 PHE B N   1 
ATOM   4621 C  CA  . PHE B 1 305 ? -15.431 5.106   12.509  1.00 34.04 ? 294 PHE B CA  1 
ATOM   4622 C  C   . PHE B 1 305 ? -14.256 5.391   13.440  1.00 35.86 ? 294 PHE B C   1 
ATOM   4623 O  O   . PHE B 1 305 ? -13.091 5.329   13.037  1.00 38.83 ? 294 PHE B O   1 
ATOM   4624 C  CB  . PHE B 1 305 ? -16.092 3.768   12.847  1.00 30.72 ? 294 PHE B CB  1 
ATOM   4625 C  CG  . PHE B 1 305 ? -17.412 3.538   12.145  1.00 30.93 ? 294 PHE B CG  1 
ATOM   4626 C  CD1 . PHE B 1 305 ? -18.042 4.566   11.445  1.00 31.31 ? 294 PHE B CD1 1 
ATOM   4627 C  CD2 . PHE B 1 305 ? -18.022 2.285   12.177  1.00 32.36 ? 294 PHE B CD2 1 
ATOM   4628 C  CE1 . PHE B 1 305 ? -19.264 4.353   10.787  1.00 29.99 ? 294 PHE B CE1 1 
ATOM   4629 C  CE2 . PHE B 1 305 ? -19.238 2.061   11.527  1.00 32.18 ? 294 PHE B CE2 1 
ATOM   4630 C  CZ  . PHE B 1 305 ? -19.866 3.107   10.838  1.00 31.43 ? 294 PHE B CZ  1 
ATOM   4631 N  N   . LYS B 1 306 ? -14.574 5.742   14.687  1.00 35.03 ? 295 LYS B N   1 
ATOM   4632 C  CA  . LYS B 1 306 ? -13.541 6.013   15.689  1.00 40.88 ? 295 LYS B CA  1 
ATOM   4633 C  C   . LYS B 1 306 ? -13.671 5.077   16.892  1.00 36.65 ? 295 LYS B C   1 
ATOM   4634 O  O   . LYS B 1 306 ? -13.854 5.532   18.028  1.00 34.55 ? 295 LYS B O   1 
ATOM   4635 C  CB  . LYS B 1 306 ? -13.588 7.473   16.176  1.00 32.40 ? 295 LYS B CB  1 
ATOM   4636 C  CG  . LYS B 1 306 ? -14.240 8.492   15.246  1.00 32.64 ? 295 LYS B CG  1 
ATOM   4637 C  CD  . LYS B 1 306 ? -13.369 8.875   14.020  1.00 47.90 ? 295 LYS B CD  1 
ATOM   4638 C  CE  . LYS B 1 306 ? -11.881 9.138   14.346  1.00 53.15 ? 295 LYS B CE  1 
ATOM   4639 N  NZ  . LYS B 1 306 ? -11.085 9.581   13.145  1.00 54.67 ? 295 LYS B NZ  1 
ATOM   4640 N  N   . LEU B 1 307 ? -13.593 3.773   16.662  1.00 31.90 ? 296 LEU B N   1 
ATOM   4641 C  CA  . LEU B 1 307 ? -13.647 2.831   17.770  1.00 37.06 ? 296 LEU B CA  1 
ATOM   4642 C  C   . LEU B 1 307 ? -12.262 2.681   18.385  1.00 36.32 ? 296 LEU B C   1 
ATOM   4643 O  O   . LEU B 1 307 ? -11.238 2.791   17.707  1.00 37.95 ? 296 LEU B O   1 
ATOM   4644 C  CB  . LEU B 1 307 ? -14.189 1.470   17.309  1.00 34.69 ? 296 LEU B CB  1 
ATOM   4645 C  CG  . LEU B 1 307 ? -15.702 1.350   17.052  1.00 29.05 ? 296 LEU B CG  1 
ATOM   4646 C  CD1 . LEU B 1 307 ? -16.079 -0.083  16.762  1.00 31.01 ? 296 LEU B CD1 1 
ATOM   4647 C  CD2 . LEU B 1 307 ? -16.538 1.864   18.224  1.00 28.11 ? 296 LEU B CD2 1 
ATOM   4648 N  N   . ASP B 1 308 ? -12.234 2.456   19.688  1.00 36.93 ? 297 ASP B N   1 
ATOM   4649 C  CA  . ASP B 1 308 ? -10.986 2.333   20.418  1.00 40.14 ? 297 ASP B CA  1 
ATOM   4650 C  C   . ASP B 1 308 ? -10.774 0.883   20.813  1.00 35.03 ? 297 ASP B C   1 
ATOM   4651 O  O   . ASP B 1 308 ? -11.718 0.104   20.879  1.00 35.24 ? 297 ASP B O   1 
ATOM   4652 C  CB  . ASP B 1 308 ? -10.987 3.236   21.656  1.00 45.38 ? 297 ASP B CB  1 
ATOM   4653 C  CG  . ASP B 1 308 ? -9.673  3.984   21.828  1.00 62.22 ? 297 ASP B CG  1 
ATOM   4654 O  OD1 . ASP B 1 308 ? -9.696  5.112   22.378  1.00 66.42 ? 297 ASP B OD1 1 
ATOM   4655 O  OD2 . ASP B 1 308 ? -8.616  3.441   21.412  1.00 61.35 ? 297 ASP B OD2 1 
ATOM   4656 N  N   . SER B 1 309 ? -9.520  0.524   21.067  1.00 38.22 ? 298 SER B N   1 
ATOM   4657 C  CA  . SER B 1 309 ? -9.204  -0.827  21.535  1.00 42.17 ? 298 SER B CA  1 
ATOM   4658 C  C   . SER B 1 309 ? -10.104 -1.321  22.667  1.00 39.50 ? 298 SER B C   1 
ATOM   4659 O  O   . SER B 1 309 ? -10.643 -2.437  22.550  1.00 35.09 ? 298 SER B O   1 
ATOM   4660 C  CB  . SER B 1 309 ? -7.728  -0.887  21.948  1.00 35.44 ? 298 SER B CB  1 
ATOM   4661 O  OG  . SER B 1 309 ? -6.904  -1.103  20.823  1.00 38.09 ? 298 SER B OG  1 
ATOM   4662 N  N   . PRO B 1 310 ? -10.329 -0.569  23.755  1.00 38.10 ? 299 PRO B N   1 
ATOM   4663 C  CA  . PRO B 1 310 ? -11.234 -1.065  24.812  1.00 34.24 ? 299 PRO B CA  1 
ATOM   4664 C  C   . PRO B 1 310 ? -12.676 -1.263  24.352  1.00 35.65 ? 299 PRO B C   1 
ATOM   4665 O  O   . PRO B 1 310 ? -13.420 -2.020  24.998  1.00 31.81 ? 299 PRO B O   1 
ATOM   4666 C  CB  . PRO B 1 310 ? -11.144 0.028   25.889  1.00 25.52 ? 299 PRO B CB  1 
ATOM   4667 C  CG  . PRO B 1 310 ? -9.881  0.746   25.598  1.00 29.18 ? 299 PRO B CG  1 
ATOM   4668 C  CD  . PRO B 1 310 ? -9.789  0.757   24.111  1.00 37.51 ? 299 PRO B CD  1 
ATOM   4669 N  N   . ASP B 1 311 ? -13.092 -0.594  23.268  1.00 37.32 ? 300 ASP B N   1 
ATOM   4670 C  CA  . ASP B 1 311 ? -14.456 -0.733  22.767  1.00 33.05 ? 300 ASP B CA  1 
ATOM   4671 C  C   . ASP B 1 311 ? -14.767 -2.161  22.341  1.00 32.01 ? 300 ASP B C   1 
ATOM   4672 O  O   . ASP B 1 311 ? -15.928 -2.582  22.390  1.00 25.96 ? 300 ASP B O   1 
ATOM   4673 C  CB  . ASP B 1 311 ? -14.679 0.222   21.600  1.00 31.78 ? 300 ASP B CB  1 
ATOM   4674 C  CG  . ASP B 1 311 ? -14.921 1.634   22.056  1.00 38.05 ? 300 ASP B CG  1 
ATOM   4675 O  OD1 . ASP B 1 311 ? -15.444 1.794   23.190  1.00 36.55 ? 300 ASP B OD1 1 
ATOM   4676 O  OD2 . ASP B 1 311 ? -14.596 2.573   21.285  1.00 35.01 ? 300 ASP B OD2 1 
ATOM   4677 N  N   . TYR B 1 312 ? -13.752 -2.910  21.901  1.00 33.17 ? 301 TYR B N   1 
ATOM   4678 C  CA  . TYR B 1 312 ? -13.991 -4.264  21.429  1.00 29.37 ? 301 TYR B CA  1 
ATOM   4679 C  C   . TYR B 1 312 ? -14.246 -5.201  22.593  1.00 31.58 ? 301 TYR B C   1 
ATOM   4680 O  O   . TYR B 1 312 ? -14.942 -6.213  22.437  1.00 35.47 ? 301 TYR B O   1 
ATOM   4681 C  CB  . TYR B 1 312 ? -12.818 -4.732  20.575  1.00 28.00 ? 301 TYR B CB  1 
ATOM   4682 C  CG  . TYR B 1 312 ? -12.703 -3.924  19.314  1.00 31.44 ? 301 TYR B CG  1 
ATOM   4683 C  CD1 . TYR B 1 312 ? -13.466 -4.233  18.201  1.00 32.39 ? 301 TYR B CD1 1 
ATOM   4684 C  CD2 . TYR B 1 312 ? -11.854 -2.830  19.243  1.00 33.52 ? 301 TYR B CD2 1 
ATOM   4685 C  CE1 . TYR B 1 312 ? -13.378 -3.489  17.050  1.00 31.29 ? 301 TYR B CE1 1 
ATOM   4686 C  CE2 . TYR B 1 312 ? -11.755 -2.080  18.094  1.00 31.99 ? 301 TYR B CE2 1 
ATOM   4687 C  CZ  . TYR B 1 312 ? -12.521 -2.408  17.000  1.00 32.22 ? 301 TYR B CZ  1 
ATOM   4688 O  OH  . TYR B 1 312 ? -12.433 -1.657  15.849  1.00 31.64 ? 301 TYR B OH  1 
ATOM   4689 N  N   . LEU B 1 313 ? -13.716 -4.871  23.765  1.00 30.35 ? 302 LEU B N   1 
ATOM   4690 C  CA  . LEU B 1 313 ? -14.114 -5.587  24.967  1.00 28.40 ? 302 LEU B CA  1 
ATOM   4691 C  C   . LEU B 1 313 ? -15.603 -5.389  25.238  1.00 27.45 ? 302 LEU B C   1 
ATOM   4692 O  O   . LEU B 1 313 ? -16.355 -6.358  25.374  1.00 29.29 ? 302 LEU B O   1 
ATOM   4693 C  CB  . LEU B 1 313 ? -13.267 -5.125  26.148  1.00 22.38 ? 302 LEU B CB  1 
ATOM   4694 C  CG  . LEU B 1 313 ? -11.798 -5.521  26.215  1.00 25.20 ? 302 LEU B CG  1 
ATOM   4695 C  CD1 . LEU B 1 313 ? -11.110 -4.728  27.332  1.00 18.31 ? 302 LEU B CD1 1 
ATOM   4696 C  CD2 . LEU B 1 313 ? -11.661 -7.042  26.437  1.00 23.28 ? 302 LEU B CD2 1 
ATOM   4697 N  N   . SER B 1 314 ? -16.052 -4.136  25.288  1.00 27.40 ? 303 SER B N   1 
ATOM   4698 C  CA  . SER B 1 314 ? -17.469 -3.875  25.516  1.00 34.03 ? 303 SER B CA  1 
ATOM   4699 C  C   . SER B 1 314 ? -18.331 -4.598  24.485  1.00 32.66 ? 303 SER B C   1 
ATOM   4700 O  O   . SER B 1 314 ? -19.379 -5.166  24.820  1.00 27.80 ? 303 SER B O   1 
ATOM   4701 C  CB  . SER B 1 314 ? -17.734 -2.369  25.480  1.00 31.58 ? 303 SER B CB  1 
ATOM   4702 O  OG  . SER B 1 314 ? -16.699 -1.680  26.158  1.00 38.57 ? 303 SER B OG  1 
ATOM   4703 N  N   . MET B 1 315 ? -17.887 -4.596  23.227  1.00 31.44 ? 304 MET B N   1 
ATOM   4704 C  CA  . MET B 1 315 ? -18.562 -5.349  22.173  1.00 31.85 ? 304 MET B CA  1 
ATOM   4705 C  C   . MET B 1 315 ? -18.713 -6.822  22.537  1.00 29.08 ? 304 MET B C   1 
ATOM   4706 O  O   . MET B 1 315 ? -19.812 -7.379  22.437  1.00 26.16 ? 304 MET B O   1 
ATOM   4707 C  CB  . MET B 1 315 ? -17.807 -5.146  20.855  1.00 30.30 ? 304 MET B CB  1 
ATOM   4708 C  CG  . MET B 1 315 ? -18.616 -5.343  19.574  1.00 31.16 ? 304 MET B CG  1 
ATOM   4709 S  SD  . MET B 1 315 ? -17.572 -5.928  18.203  1.00 35.44 ? 304 MET B SD  1 
ATOM   4710 C  CE  . MET B 1 315 ? -17.028 -4.336  17.551  1.00 22.63 ? 304 MET B CE  1 
ATOM   4711 N  N   . GLY B 1 316 ? -17.630 -7.459  22.990  1.00 31.65 ? 305 GLY B N   1 
ATOM   4712 C  CA  . GLY B 1 316 ? -17.695 -8.875  23.310  1.00 30.36 ? 305 GLY B CA  1 
ATOM   4713 C  C   . GLY B 1 316 ? -18.667 -9.178  24.433  1.00 31.23 ? 305 GLY B C   1 
ATOM   4714 O  O   . GLY B 1 316 ? -19.440 -10.145 24.367  1.00 29.93 ? 305 GLY B O   1 
ATOM   4715 N  N   . GLU B 1 317 ? -18.659 -8.346  25.470  1.00 27.78 ? 306 GLU B N   1 
ATOM   4716 C  CA  . GLU B 1 317 ? -19.575 -8.550  26.588  1.00 31.11 ? 306 GLU B CA  1 
ATOM   4717 C  C   . GLU B 1 317 ? -21.030 -8.420  26.165  1.00 25.78 ? 306 GLU B C   1 
ATOM   4718 O  O   . GLU B 1 317 ? -21.901 -9.097  26.707  1.00 27.04 ? 306 GLU B O   1 
ATOM   4719 C  CB  . GLU B 1 317 ? -19.257 -7.546  27.689  1.00 31.71 ? 306 GLU B CB  1 
ATOM   4720 C  CG  . GLU B 1 317 ? -17.789 -7.403  27.867  1.00 34.59 ? 306 GLU B CG  1 
ATOM   4721 C  CD  . GLU B 1 317 ? -17.440 -7.072  29.266  1.00 37.77 ? 306 GLU B CD  1 
ATOM   4722 O  OE1 . GLU B 1 317 ? -18.168 -6.238  29.845  1.00 40.47 ? 306 GLU B OE1 1 
ATOM   4723 O  OE2 . GLU B 1 317 ? -16.456 -7.653  29.780  1.00 39.29 ? 306 GLU B OE2 1 
ATOM   4724 N  N   . ARG B 1 318 ? -21.316 -7.529  25.224  1.00 25.70 ? 307 ARG B N   1 
ATOM   4725 C  CA  . ARG B 1 318 ? -22.697 -7.270  24.844  1.00 28.46 ? 307 ARG B CA  1 
ATOM   4726 C  C   . ARG B 1 318 ? -23.254 -8.428  24.024  1.00 32.61 ? 307 ARG B C   1 
ATOM   4727 O  O   . ARG B 1 318 ? -24.415 -8.828  24.201  1.00 31.94 ? 307 ARG B O   1 
ATOM   4728 C  CB  . ARG B 1 318 ? -22.769 -5.946  24.077  1.00 26.67 ? 307 ARG B CB  1 
ATOM   4729 C  CG  . ARG B 1 318 ? -24.144 -5.499  23.727  1.00 24.36 ? 307 ARG B CG  1 
ATOM   4730 C  CD  . ARG B 1 318 ? -25.097 -5.770  24.849  1.00 25.58 ? 307 ARG B CD  1 
ATOM   4731 N  NE  . ARG B 1 318 ? -26.466 -5.437  24.479  1.00 30.54 ? 307 ARG B NE  1 
ATOM   4732 C  CZ  . ARG B 1 318 ? -27.402 -6.327  24.175  1.00 32.03 ? 307 ARG B CZ  1 
ATOM   4733 N  NH1 . ARG B 1 318 ? -27.158 -7.633  24.204  1.00 29.62 ? 307 ARG B NH1 1 
ATOM   4734 N  NH2 . ARG B 1 318 ? -28.613 -5.896  23.829  1.00 33.31 ? 307 ARG B NH2 1 
ATOM   4735 N  N   . ILE B 1 319 ? -22.429 -8.977  23.126  1.00 31.87 ? 308 ILE B N   1 
ATOM   4736 C  CA  . ILE B 1 319 ? -22.777 -10.200 22.409  1.00 31.41 ? 308 ILE B CA  1 
ATOM   4737 C  C   . ILE B 1 319 ? -22.972 -11.349 23.395  1.00 28.60 ? 308 ILE B C   1 
ATOM   4738 O  O   . ILE B 1 319 ? -23.936 -12.111 23.304  1.00 29.20 ? 308 ILE B O   1 
ATOM   4739 C  CB  . ILE B 1 319 ? -21.687 -10.528 21.369  1.00 29.30 ? 308 ILE B CB  1 
ATOM   4740 C  CG1 . ILE B 1 319 ? -21.427 -9.340  20.460  1.00 24.31 ? 308 ILE B CG1 1 
ATOM   4741 C  CG2 . ILE B 1 319 ? -22.054 -11.762 20.539  1.00 32.24 ? 308 ILE B CG2 1 
ATOM   4742 C  CD1 . ILE B 1 319 ? -20.345 -9.622  19.444  1.00 25.96 ? 308 ILE B CD1 1 
ATOM   4743 N  N   . ALA B 1 320 ? -22.040 -11.506 24.335  1.00 27.57 ? 309 ALA B N   1 
ATOM   4744 C  CA  . ALA B 1 320 ? -22.176 -12.558 25.331  1.00 27.06 ? 309 ALA B CA  1 
ATOM   4745 C  C   . ALA B 1 320 ? -23.405 -12.338 26.190  1.00 28.35 ? 309 ALA B C   1 
ATOM   4746 O  O   . ALA B 1 320 ? -24.012 -13.305 26.664  1.00 31.74 ? 309 ALA B O   1 
ATOM   4747 C  CB  . ALA B 1 320 ? -20.925 -12.635 26.199  1.00 27.63 ? 309 ALA B CB  1 
ATOM   4748 N  N   . ALA B 1 321 ? -23.812 -11.083 26.368  1.00 28.48 ? 310 ALA B N   1 
ATOM   4749 C  CA  . ALA B 1 321 ? -25.025 -10.792 27.129  1.00 27.97 ? 310 ALA B CA  1 
ATOM   4750 C  C   . ALA B 1 321 ? -26.242 -11.443 26.510  1.00 27.45 ? 310 ALA B C   1 
ATOM   4751 O  O   . ALA B 1 321 ? -27.205 -11.741 27.217  1.00 30.24 ? 310 ALA B O   1 
ATOM   4752 C  CB  . ALA B 1 321 ? -25.256 -9.282  27.225  1.00 31.01 ? 310 ALA B CB  1 
ATOM   4753 N  N   . MET B 1 322 ? -26.207 -11.687 25.196  1.00 33.64 ? 311 MET B N   1 
ATOM   4754 C  CA  . MET B 1 322 ? -27.342 -12.253 24.473  1.00 33.36 ? 311 MET B CA  1 
ATOM   4755 C  C   . MET B 1 322 ? -27.667 -13.670 24.931  1.00 35.16 ? 311 MET B C   1 
ATOM   4756 O  O   . MET B 1 322 ? -28.792 -14.133 24.719  1.00 39.04 ? 311 MET B O   1 
ATOM   4757 C  CB  . MET B 1 322 ? -27.033 -12.210 22.983  1.00 33.31 ? 311 MET B CB  1 
ATOM   4758 C  CG  . MET B 1 322 ? -27.738 -11.085 22.252  1.00 37.14 ? 311 MET B CG  1 
ATOM   4759 S  SD  . MET B 1 322 ? -27.385 -11.194 20.497  1.00 41.48 ? 311 MET B SD  1 
ATOM   4760 C  CE  . MET B 1 322 ? -25.615 -11.488 20.484  1.00 25.65 ? 311 MET B CE  1 
ATOM   4761 N  N   . GLY B 1 323 ? -26.719 -14.353 25.570  1.00 30.80 ? 312 GLY B N   1 
ATOM   4762 C  CA  . GLY B 1 323 ? -26.957 -15.653 26.144  1.00 26.97 ? 312 GLY B CA  1 
ATOM   4763 C  C   . GLY B 1 323 ? -26.903 -16.783 25.153  1.00 41.13 ? 312 GLY B C   1 
ATOM   4764 O  O   . GLY B 1 323 ? -27.335 -17.895 25.475  1.00 45.76 ? 312 GLY B O   1 
ATOM   4765 N  N   . LEU B 1 324 ? -26.385 -16.540 23.961  1.00 38.44 ? 313 LEU B N   1 
ATOM   4766 C  CA  . LEU B 1 324 ? -26.522 -17.543 22.937  1.00 36.53 ? 313 LEU B CA  1 
ATOM   4767 C  C   . LEU B 1 324 ? -25.188 -18.204 22.605  1.00 43.74 ? 313 LEU B C   1 
ATOM   4768 O  O   . LEU B 1 324 ? -24.126 -17.579 22.715  1.00 41.04 ? 313 LEU B O   1 
ATOM   4769 C  CB  . LEU B 1 324 ? -27.099 -16.911 21.672  1.00 39.60 ? 313 LEU B CB  1 
ATOM   4770 C  CG  . LEU B 1 324 ? -28.589 -17.082 21.389  1.00 47.77 ? 313 LEU B CG  1 
ATOM   4771 C  CD1 . LEU B 1 324 ? -29.456 -16.301 22.351  1.00 48.18 ? 313 LEU B CD1 1 
ATOM   4772 C  CD2 . LEU B 1 324 ? -28.810 -16.582 19.987  1.00 47.91 ? 313 LEU B CD2 1 
ATOM   4773 N  N   . PRO B 1 325 ? -25.210 -19.469 22.183  1.00 44.54 ? 314 PRO B N   1 
ATOM   4774 C  CA  . PRO B 1 325 ? -24.013 -20.040 21.549  1.00 38.60 ? 314 PRO B CA  1 
ATOM   4775 C  C   . PRO B 1 325 ? -23.651 -19.204 20.334  1.00 36.51 ? 314 PRO B C   1 
ATOM   4776 O  O   . PRO B 1 325 ? -24.526 -18.769 19.580  1.00 38.96 ? 314 PRO B O   1 
ATOM   4777 C  CB  . PRO B 1 325 ? -24.435 -21.463 21.166  1.00 36.27 ? 314 PRO B CB  1 
ATOM   4778 C  CG  . PRO B 1 325 ? -25.908 -21.564 21.442  1.00 32.66 ? 314 PRO B CG  1 
ATOM   4779 C  CD  . PRO B 1 325 ? -26.409 -20.322 22.069  1.00 35.69 ? 314 PRO B CD  1 
ATOM   4780 N  N   . THR B 1 326 ? -22.353 -18.949 20.170  1.00 39.06 ? 315 THR B N   1 
ATOM   4781 C  CA  . THR B 1 326 ? -21.865 -17.858 19.324  1.00 36.95 ? 315 THR B CA  1 
ATOM   4782 C  C   . THR B 1 326 ? -20.651 -18.328 18.535  1.00 37.79 ? 315 THR B C   1 
ATOM   4783 O  O   . THR B 1 326 ? -19.660 -18.773 19.126  1.00 36.16 ? 315 THR B O   1 
ATOM   4784 C  CB  . THR B 1 326 ? -21.499 -16.627 20.173  1.00 32.79 ? 315 THR B CB  1 
ATOM   4785 O  OG1 . THR B 1 326 ? -22.660 -16.122 20.843  1.00 30.21 ? 315 THR B OG1 1 
ATOM   4786 C  CG2 . THR B 1 326 ? -20.915 -15.539 19.315  1.00 32.67 ? 315 THR B CG2 1 
ATOM   4787 N  N   . LEU B 1 327 ? -20.720 -18.225 17.208  1.00 31.93 ? 316 LEU B N   1 
ATOM   4788 C  CA  . LEU B 1 327 ? -19.585 -18.537 16.343  1.00 32.43 ? 316 LEU B CA  1 
ATOM   4789 C  C   . LEU B 1 327 ? -19.027 -17.238 15.778  1.00 30.80 ? 316 LEU B C   1 
ATOM   4790 O  O   . LEU B 1 327 ? -19.757 -16.474 15.136  1.00 29.80 ? 316 LEU B O   1 
ATOM   4791 C  CB  . LEU B 1 327 ? -19.979 -19.486 15.208  1.00 32.86 ? 316 LEU B CB  1 
ATOM   4792 C  CG  . LEU B 1 327 ? -19.004 -19.594 14.028  1.00 30.12 ? 316 LEU B CG  1 
ATOM   4793 C  CD1 . LEU B 1 327 ? -17.733 -20.312 14.425  1.00 26.65 ? 316 LEU B CD1 1 
ATOM   4794 C  CD2 . LEU B 1 327 ? -19.677 -20.299 12.885  1.00 29.22 ? 316 LEU B CD2 1 
ATOM   4795 N  N   . PHE B 1 328 ? -17.738 -17.002 16.012  1.00 29.86 ? 317 PHE B N   1 
ATOM   4796 C  CA  . PHE B 1 328 ? -17.031 -15.826 15.516  1.00 28.94 ? 317 PHE B CA  1 
ATOM   4797 C  C   . PHE B 1 328 ? -16.264 -16.170 14.235  1.00 35.16 ? 317 PHE B C   1 
ATOM   4798 O  O   . PHE B 1 328 ? -15.429 -17.089 14.232  1.00 30.84 ? 317 PHE B O   1 
ATOM   4799 C  CB  . PHE B 1 328 ? -16.075 -15.303 16.582  1.00 31.12 ? 317 PHE B CB  1 
ATOM   4800 C  CG  . PHE B 1 328 ? -16.755 -14.609 17.737  1.00 34.76 ? 317 PHE B CG  1 
ATOM   4801 C  CD1 . PHE B 1 328 ? -17.183 -13.284 17.622  1.00 33.57 ? 317 PHE B CD1 1 
ATOM   4802 C  CD2 . PHE B 1 328 ? -16.921 -15.256 18.950  1.00 29.49 ? 317 PHE B CD2 1 
ATOM   4803 C  CE1 . PHE B 1 328 ? -17.777 -12.628 18.687  1.00 28.38 ? 317 PHE B CE1 1 
ATOM   4804 C  CE2 . PHE B 1 328 ? -17.516 -14.606 20.022  1.00 33.95 ? 317 PHE B CE2 1 
ATOM   4805 C  CZ  . PHE B 1 328 ? -17.949 -13.287 19.887  1.00 34.21 ? 317 PHE B CZ  1 
ATOM   4806 N  N   . VAL B 1 329 ? -16.535 -15.413 13.162  1.00 31.41 ? 318 VAL B N   1 
ATOM   4807 C  CA  . VAL B 1 329 ? -15.946 -15.612 11.839  1.00 28.96 ? 318 VAL B CA  1 
ATOM   4808 C  C   . VAL B 1 329 ? -15.172 -14.356 11.469  1.00 29.79 ? 318 VAL B C   1 
ATOM   4809 O  O   . VAL B 1 329 ? -15.773 -13.290 11.293  1.00 32.58 ? 318 VAL B O   1 
ATOM   4810 C  CB  . VAL B 1 329 ? -17.019 -15.894 10.770  1.00 32.51 ? 318 VAL B CB  1 
ATOM   4811 C  CG1 . VAL B 1 329 ? -16.367 -16.248 9.414   1.00 26.28 ? 318 VAL B CG1 1 
ATOM   4812 C  CG2 . VAL B 1 329 ? -17.983 -16.961 11.239  1.00 25.42 ? 318 VAL B CG2 1 
ATOM   4813 N  N   . MET B 1 330 ? -13.857 -14.489 11.295  1.00 30.74 ? 319 MET B N   1 
ATOM   4814 C  CA  . MET B 1 330 ? -13.024 -13.372 10.848  1.00 33.00 ? 319 MET B CA  1 
ATOM   4815 C  C   . MET B 1 330 ? -13.515 -12.795 9.517   1.00 32.27 ? 319 MET B C   1 
ATOM   4816 O  O   . MET B 1 330 ? -13.818 -13.534 8.571   1.00 31.73 ? 319 MET B O   1 
ATOM   4817 C  CB  . MET B 1 330 ? -11.576 -13.834 10.677  1.00 28.36 ? 319 MET B CB  1 
ATOM   4818 C  CG  . MET B 1 330 ? -10.526 -12.783 10.967  1.00 31.63 ? 319 MET B CG  1 
ATOM   4819 S  SD  . MET B 1 330 ? -10.951 -11.654 12.319  1.00 38.30 ? 319 MET B SD  1 
ATOM   4820 C  CE  . MET B 1 330 ? -9.848  -10.291 12.000  1.00 23.46 ? 319 MET B CE  1 
ATOM   4821 N  N   . GLU B 1 331 ? -13.572 -11.460 9.438   1.00 29.37 ? 320 GLU B N   1 
ATOM   4822 C  CA  . GLU B 1 331 ? -13.737 -10.777 8.153   1.00 33.11 ? 320 GLU B CA  1 
ATOM   4823 C  C   . GLU B 1 331 ? -12.613 -9.763  7.972   1.00 32.07 ? 320 GLU B C   1 
ATOM   4824 O  O   . GLU B 1 331 ? -11.434 -10.122 8.018   1.00 32.32 ? 320 GLU B O   1 
ATOM   4825 C  CB  . GLU B 1 331 ? -15.108 -10.075 8.022   1.00 30.01 ? 320 GLU B CB  1 
ATOM   4826 C  CG  . GLU B 1 331 ? -16.335 -10.941 8.351   1.00 30.60 ? 320 GLU B CG  1 
ATOM   4827 C  CD  . GLU B 1 331 ? -16.833 -11.810 7.194   1.00 31.30 ? 320 GLU B CD  1 
ATOM   4828 O  OE1 . GLU B 1 331 ? -16.200 -11.845 6.121   1.00 34.59 ? 320 GLU B OE1 1 
ATOM   4829 O  OE2 . GLU B 1 331 ? -17.864 -12.488 7.363   1.00 33.18 ? 320 GLU B OE2 1 
ATOM   4830 N  N   . GLY B 1 332 ? -12.969 -8.495  7.784   1.00 35.08 ? 321 GLY B N   1 
ATOM   4831 C  CA  . GLY B 1 332 ? -12.002 -7.452  7.518   1.00 33.08 ? 321 GLY B CA  1 
ATOM   4832 C  C   . GLY B 1 332 ? -11.232 -6.979  8.744   1.00 33.84 ? 321 GLY B C   1 
ATOM   4833 O  O   . GLY B 1 332 ? -11.453 -7.395  9.881   1.00 29.21 ? 321 GLY B O   1 
ATOM   4834 N  N   . GLY B 1 333 ? -10.303 -6.065  8.481   1.00 36.91 ? 322 GLY B N   1 
ATOM   4835 C  CA  . GLY B 1 333 ? -9.345  -5.603  9.461   1.00 34.90 ? 322 GLY B CA  1 
ATOM   4836 C  C   . GLY B 1 333 ? -7.962  -5.565  8.846   1.00 45.83 ? 322 GLY B C   1 
ATOM   4837 O  O   . GLY B 1 333 ? -7.286  -6.596  8.752   1.00 50.51 ? 322 GLY B O   1 
ATOM   4838 N  N   . TYR B 1 334 ? -7.543  -4.388  8.385   1.00 49.95 ? 323 TYR B N   1 
ATOM   4839 C  CA  . TYR B 1 334 ? -6.197  -4.233  7.846   1.00 50.60 ? 323 TYR B CA  1 
ATOM   4840 C  C   . TYR B 1 334 ? -5.157  -4.671  8.879   1.00 55.71 ? 323 TYR B C   1 
ATOM   4841 O  O   . TYR B 1 334 ? -5.398  -4.644  10.093  1.00 55.54 ? 323 TYR B O   1 
ATOM   4842 C  CB  . TYR B 1 334 ? -5.982  -2.782  7.412   1.00 51.38 ? 323 TYR B CB  1 
ATOM   4843 C  CG  . TYR B 1 334 ? -4.596  -2.437  6.907   1.00 54.48 ? 323 TYR B CG  1 
ATOM   4844 C  CD1 . TYR B 1 334 ? -3.538  -2.272  7.789   1.00 57.03 ? 323 TYR B CD1 1 
ATOM   4845 C  CD2 . TYR B 1 334 ? -4.354  -2.231  5.550   1.00 51.96 ? 323 TYR B CD2 1 
ATOM   4846 C  CE1 . TYR B 1 334 ? -2.275  -1.954  7.353   1.00 60.69 ? 323 TYR B CE1 1 
ATOM   4847 C  CE2 . TYR B 1 334 ? -3.084  -1.902  5.095   1.00 63.41 ? 323 TYR B CE2 1 
ATOM   4848 C  CZ  . TYR B 1 334 ? -2.044  -1.764  6.010   1.00 72.32 ? 323 TYR B CZ  1 
ATOM   4849 O  OH  . TYR B 1 334 ? -0.761  -1.438  5.608   1.00 80.97 ? 323 TYR B OH  1 
ATOM   4850 N  N   . ALA B 1 335 ? -3.993  -5.098  8.384   1.00 60.23 ? 324 ALA B N   1 
ATOM   4851 C  CA  . ALA B 1 335 ? -2.956  -5.681  9.232   1.00 55.81 ? 324 ALA B CA  1 
ATOM   4852 C  C   . ALA B 1 335 ? -2.170  -4.635  10.017  1.00 49.41 ? 324 ALA B C   1 
ATOM   4853 O  O   . ALA B 1 335 ? -0.939  -4.613  9.960   1.00 50.83 ? 324 ALA B O   1 
ATOM   4854 C  CB  . ALA B 1 335 ? -2.001  -6.522  8.382   1.00 58.42 ? 324 ALA B CB  1 
ATOM   4855 N  N   . VAL B 1 336 ? -2.871  -3.779  10.762  1.00 52.89 ? 325 VAL B N   1 
ATOM   4856 C  CA  . VAL B 1 336 ? -2.251  -2.798  11.647  1.00 46.01 ? 325 VAL B CA  1 
ATOM   4857 C  C   . VAL B 1 336 ? -1.647  -3.512  12.849  1.00 45.93 ? 325 VAL B C   1 
ATOM   4858 O  O   . VAL B 1 336 ? -1.811  -4.726  13.024  1.00 39.18 ? 325 VAL B O   1 
ATOM   4859 C  CB  . VAL B 1 336 ? -3.255  -1.719  12.112  1.00 50.49 ? 325 VAL B CB  1 
ATOM   4860 C  CG1 . VAL B 1 336 ? -3.868  -0.984  10.933  1.00 44.04 ? 325 VAL B CG1 1 
ATOM   4861 C  CG2 . VAL B 1 336 ? -4.355  -2.345  12.960  1.00 46.03 ? 325 VAL B CG2 1 
ATOM   4862 N  N   . GLU B 1 337 ? -0.940  -2.751  13.683  1.00 49.42 ? 326 GLU B N   1 
ATOM   4863 C  CA  . GLU B 1 337 ? -0.305  -3.328  14.859  1.00 46.99 ? 326 GLU B CA  1 
ATOM   4864 C  C   . GLU B 1 337 ? -1.328  -3.969  15.773  1.00 49.55 ? 326 GLU B C   1 
ATOM   4865 O  O   . GLU B 1 337 ? -1.123  -5.083  16.270  1.00 51.51 ? 326 GLU B O   1 
ATOM   4866 C  CB  . GLU B 1 337 ? 0.449   -2.241  15.611  1.00 48.23 ? 326 GLU B CB  1 
ATOM   4867 C  CG  . GLU B 1 337 ? 1.605   -2.732  16.422  1.00 48.15 ? 326 GLU B CG  1 
ATOM   4868 C  CD  . GLU B 1 337 ? 2.517   -1.592  16.791  1.00 56.99 ? 326 GLU B CD  1 
ATOM   4869 O  OE1 . GLU B 1 337 ? 2.402   -0.512  16.156  1.00 61.13 ? 326 GLU B OE1 1 
ATOM   4870 O  OE2 . GLU B 1 337 ? 3.336   -1.767  17.715  1.00 60.66 ? 326 GLU B OE2 1 
ATOM   4871 N  N   . ALA B 1 338 ? -2.447  -3.282  15.988  1.00 50.27 ? 327 ALA B N   1 
ATOM   4872 C  CA  . ALA B 1 338 ? -3.412  -3.630  17.015  1.00 45.15 ? 327 ALA B CA  1 
ATOM   4873 C  C   . ALA B 1 338 ? -4.489  -4.607  16.553  1.00 42.13 ? 327 ALA B C   1 
ATOM   4874 O  O   . ALA B 1 338 ? -5.417  -4.872  17.323  1.00 41.04 ? 327 ALA B O   1 
ATOM   4875 C  CB  . ALA B 1 338 ? -4.069  -2.359  17.544  1.00 41.94 ? 327 ALA B CB  1 
ATOM   4876 N  N   . ILE B 1 339 ? -4.394  -5.152  15.335  1.00 40.81 ? 328 ILE B N   1 
ATOM   4877 C  CA  . ILE B 1 339 ? -5.468  -6.009  14.828  1.00 41.89 ? 328 ILE B CA  1 
ATOM   4878 C  C   . ILE B 1 339 ? -5.667  -7.223  15.736  1.00 45.53 ? 328 ILE B C   1 
ATOM   4879 O  O   . ILE B 1 339 ? -6.808  -7.586  16.066  1.00 38.79 ? 328 ILE B O   1 
ATOM   4880 C  CB  . ILE B 1 339 ? -5.207  -6.420  13.364  1.00 41.85 ? 328 ILE B CB  1 
ATOM   4881 C  CG1 . ILE B 1 339 ? -6.479  -7.006  12.750  1.00 34.60 ? 328 ILE B CG1 1 
ATOM   4882 C  CG2 . ILE B 1 339 ? -4.042  -7.403  13.245  1.00 41.34 ? 328 ILE B CG2 1 
ATOM   4883 C  CD1 . ILE B 1 339 ? -6.237  -7.971  11.634  1.00 44.76 ? 328 ILE B CD1 1 
ATOM   4884 N  N   . GLY B 1 340 ? -4.566  -7.848  16.179  1.00 39.84 ? 329 GLY B N   1 
ATOM   4885 C  CA  . GLY B 1 340 ? -4.686  -8.966  17.098  1.00 36.93 ? 329 GLY B CA  1 
ATOM   4886 C  C   . GLY B 1 340 ? -5.286  -8.554  18.427  1.00 37.88 ? 329 GLY B C   1 
ATOM   4887 O  O   . GLY B 1 340 ? -6.106  -9.274  18.999  1.00 36.08 ? 329 GLY B O   1 
ATOM   4888 N  N   . VAL B 1 341 ? -4.902  -7.375  18.921  1.00 44.04 ? 330 VAL B N   1 
ATOM   4889 C  CA  . VAL B 1 341 ? -5.419  -6.873  20.194  1.00 37.91 ? 330 VAL B CA  1 
ATOM   4890 C  C   . VAL B 1 341 ? -6.923  -6.644  20.105  1.00 38.34 ? 330 VAL B C   1 
ATOM   4891 O  O   . VAL B 1 341 ? -7.695  -7.126  20.944  1.00 36.60 ? 330 VAL B O   1 
ATOM   4892 C  CB  . VAL B 1 341 ? -4.667  -5.590  20.595  1.00 30.85 ? 330 VAL B CB  1 
ATOM   4893 C  CG1 . VAL B 1 341 ? -5.500  -4.727  21.492  1.00 29.15 ? 330 VAL B CG1 1 
ATOM   4894 C  CG2 . VAL B 1 341 ? -3.415  -5.974  21.273  1.00 28.42 ? 330 VAL B CG2 1 
ATOM   4895 N  N   . ASN B 1 342 ? -7.356  -5.915  19.071  1.00 38.38 ? 331 ASN B N   1 
ATOM   4896 C  CA  . ASN B 1 342 ? -8.773  -5.617  18.894  1.00 34.07 ? 331 ASN B CA  1 
ATOM   4897 C  C   . ASN B 1 342 ? -9.596  -6.890  18.744  1.00 34.76 ? 331 ASN B C   1 
ATOM   4898 O  O   . ASN B 1 342 ? -10.555 -7.112  19.491  1.00 35.91 ? 331 ASN B O   1 
ATOM   4899 C  CB  . ASN B 1 342 ? -8.961  -4.700  17.683  1.00 33.38 ? 331 ASN B CB  1 
ATOM   4900 C  CG  . ASN B 1 342 ? -8.321  -3.331  17.881  1.00 36.38 ? 331 ASN B CG  1 
ATOM   4901 O  OD1 . ASN B 1 342 ? -8.078  -2.911  19.013  1.00 38.02 ? 331 ASN B OD1 1 
ATOM   4902 N  ND2 . ASN B 1 342 ? -8.049  -2.631  16.781  1.00 33.98 ? 331 ASN B ND2 1 
ATOM   4903 N  N   . ALA B 1 343 ? -9.232  -7.742  17.781  1.00 38.35 ? 332 ALA B N   1 
ATOM   4904 C  CA  . ALA B 1 343 ? -10.029 -8.932  17.496  1.00 33.98 ? 332 ALA B CA  1 
ATOM   4905 C  C   . ALA B 1 343 ? -10.167 -9.814  18.731  1.00 39.75 ? 332 ALA B C   1 
ATOM   4906 O  O   . ALA B 1 343 ? -11.265 -10.292 19.053  1.00 30.83 ? 332 ALA B O   1 
ATOM   4907 C  CB  . ALA B 1 343 ? -9.394  -9.714  16.348  1.00 34.37 ? 332 ALA B CB  1 
ATOM   4908 N  N   . VAL B 1 344 ? -9.051  -10.045 19.431  1.00 37.56 ? 333 VAL B N   1 
ATOM   4909 C  CA  . VAL B 1 344 ? -9.059  -10.921 20.594  1.00 36.91 ? 333 VAL B CA  1 
ATOM   4910 C  C   . VAL B 1 344 ? -9.756  -10.256 21.777  1.00 36.44 ? 333 VAL B C   1 
ATOM   4911 O  O   . VAL B 1 344 ? -10.202 -10.947 22.702  1.00 34.25 ? 333 VAL B O   1 
ATOM   4912 C  CB  . VAL B 1 344 ? -7.605  -11.352 20.904  1.00 41.26 ? 333 VAL B CB  1 
ATOM   4913 C  CG1 . VAL B 1 344 ? -7.498  -12.194 22.180  1.00 40.62 ? 333 VAL B CG1 1 
ATOM   4914 C  CG2 . VAL B 1 344 ? -7.036  -12.123 19.729  1.00 36.45 ? 333 VAL B CG2 1 
ATOM   4915 N  N   . ASN B 1 345 ? -9.893  -8.925  21.759  1.00 35.17 ? 334 ASN B N   1 
ATOM   4916 C  CA  . ASN B 1 345 ? -10.648 -8.258  22.817  1.00 35.75 ? 334 ASN B CA  1 
ATOM   4917 C  C   . ASN B 1 345 ? -12.126 -8.641  22.765  1.00 33.96 ? 334 ASN B C   1 
ATOM   4918 O  O   . ASN B 1 345 ? -12.759 -8.836  23.808  1.00 32.82 ? 334 ASN B O   1 
ATOM   4919 C  CB  . ASN B 1 345 ? -10.472 -6.743  22.713  1.00 33.87 ? 334 ASN B CB  1 
ATOM   4920 C  CG  . ASN B 1 345 ? -9.304  -6.235  23.530  1.00 29.55 ? 334 ASN B CG  1 
ATOM   4921 O  OD1 . ASN B 1 345 ? -8.663  -6.993  24.246  1.00 35.38 ? 334 ASN B OD1 1 
ATOM   4922 N  ND2 . ASN B 1 345 ? -8.996  -4.958  23.394  1.00 30.51 ? 334 ASN B ND2 1 
ATOM   4923 N  N   . VAL B 1 346 ? -12.687 -8.768  21.560  1.00 31.59 ? 335 VAL B N   1 
ATOM   4924 C  CA  . VAL B 1 346 ? -14.073 -9.205  21.430  1.00 30.65 ? 335 VAL B CA  1 
ATOM   4925 C  C   . VAL B 1 346 ? -14.245 -10.601 22.016  1.00 32.54 ? 335 VAL B C   1 
ATOM   4926 O  O   . VAL B 1 346 ? -15.243 -10.896 22.688  1.00 36.04 ? 335 VAL B O   1 
ATOM   4927 C  CB  . VAL B 1 346 ? -14.509 -9.150  19.952  1.00 37.07 ? 335 VAL B CB  1 
ATOM   4928 C  CG1 . VAL B 1 346 ? -15.959 -9.659  19.788  1.00 35.31 ? 335 VAL B CG1 1 
ATOM   4929 C  CG2 . VAL B 1 346 ? -14.331 -7.739  19.375  1.00 26.60 ? 335 VAL B CG2 1 
ATOM   4930 N  N   . LEU B 1 347 ? -13.272 -11.479 21.781  1.00 32.61 ? 336 LEU B N   1 
ATOM   4931 C  CA  . LEU B 1 347 ? -13.345 -12.826 22.339  1.00 34.14 ? 336 LEU B CA  1 
ATOM   4932 C  C   . LEU B 1 347 ? -13.113 -12.811 23.842  1.00 36.66 ? 336 LEU B C   1 
ATOM   4933 O  O   . LEU B 1 347 ? -13.780 -13.544 24.580  1.00 36.23 ? 336 LEU B O   1 
ATOM   4934 C  CB  . LEU B 1 347 ? -12.327 -13.747 21.654  1.00 33.07 ? 336 LEU B CB  1 
ATOM   4935 C  CG  . LEU B 1 347 ? -12.276 -13.756 20.128  1.00 25.94 ? 336 LEU B CG  1 
ATOM   4936 C  CD1 . LEU B 1 347 ? -11.275 -14.785 19.663  1.00 26.00 ? 336 LEU B CD1 1 
ATOM   4937 C  CD2 . LEU B 1 347 ? -13.651 -14.001 19.551  1.00 20.69 ? 336 LEU B CD2 1 
ATOM   4938 N  N   . GLU B 1 348 ? -12.158 -11.995 24.309  1.00 35.14 ? 337 GLU B N   1 
ATOM   4939 C  CA  . GLU B 1 348 ? -11.928 -11.860 25.740  1.00 29.88 ? 337 GLU B CA  1 
ATOM   4940 C  C   . GLU B 1 348 ? -13.178 -11.363 26.438  1.00 34.01 ? 337 GLU B C   1 
ATOM   4941 O  O   . GLU B 1 348 ? -13.650 -11.974 27.403  1.00 36.27 ? 337 GLU B O   1 
ATOM   4942 C  CB  . GLU B 1 348 ? -10.785 -10.893 26.000  1.00 39.11 ? 337 GLU B CB  1 
ATOM   4943 C  CG  . GLU B 1 348 ? -9.427  -11.512 26.060  1.00 47.47 ? 337 GLU B CG  1 
ATOM   4944 C  CD  . GLU B 1 348 ? -8.426  -10.548 26.638  1.00 52.88 ? 337 GLU B CD  1 
ATOM   4945 O  OE1 . GLU B 1 348 ? -8.410  -10.403 27.879  1.00 47.19 ? 337 GLU B OE1 1 
ATOM   4946 O  OE2 . GLU B 1 348 ? -7.683  -9.915  25.843  1.00 54.09 ? 337 GLU B OE2 1 
ATOM   4947 N  N   . GLY B 1 349 ? -13.721 -10.239 25.962  1.00 34.01 ? 338 GLY B N   1 
ATOM   4948 C  CA  . GLY B 1 349 ? -14.930 -9.692  26.544  1.00 31.44 ? 338 GLY B CA  1 
ATOM   4949 C  C   . GLY B 1 349 ? -16.113 -10.633 26.438  1.00 35.48 ? 338 GLY B C   1 
ATOM   4950 O  O   . GLY B 1 349 ? -16.954 -10.672 27.338  1.00 35.86 ? 338 GLY B O   1 
ATOM   4951 N  N   . PHE B 1 350 ? -16.202 -11.406 25.349  1.00 33.30 ? 339 PHE B N   1 
ATOM   4952 C  CA  . PHE B 1 350 ? -17.210 -12.465 25.299  1.00 34.25 ? 339 PHE B CA  1 
ATOM   4953 C  C   . PHE B 1 350 ? -17.023 -13.442 26.457  1.00 33.85 ? 339 PHE B C   1 
ATOM   4954 O  O   . PHE B 1 350 ? -17.993 -13.810 27.135  1.00 35.71 ? 339 PHE B O   1 
ATOM   4955 C  CB  . PHE B 1 350 ? -17.165 -13.199 23.950  1.00 33.74 ? 339 PHE B CB  1 
ATOM   4956 C  CG  . PHE B 1 350 ? -18.160 -14.339 23.832  1.00 35.75 ? 339 PHE B CG  1 
ATOM   4957 C  CD1 . PHE B 1 350 ? -19.459 -14.108 23.395  1.00 35.74 ? 339 PHE B CD1 1 
ATOM   4958 C  CD2 . PHE B 1 350 ? -17.793 -15.648 24.157  1.00 36.36 ? 339 PHE B CD2 1 
ATOM   4959 C  CE1 . PHE B 1 350 ? -20.378 -15.160 23.297  1.00 33.50 ? 339 PHE B CE1 1 
ATOM   4960 C  CE2 . PHE B 1 350 ? -18.702 -16.696 24.056  1.00 29.50 ? 339 PHE B CE2 1 
ATOM   4961 C  CZ  . PHE B 1 350 ? -19.991 -16.456 23.624  1.00 32.04 ? 339 PHE B CZ  1 
ATOM   4962 N  N   . GLU B 1 351 ? -15.774 -13.856 26.712  1.00 32.12 ? 340 GLU B N   1 
ATOM   4963 C  CA  . GLU B 1 351 ? -15.493 -14.870 27.721  1.00 34.81 ? 340 GLU B CA  1 
ATOM   4964 C  C   . GLU B 1 351 ? -15.536 -14.317 29.135  1.00 31.87 ? 340 GLU B C   1 
ATOM   4965 O  O   . GLU B 1 351 ? -15.561 -15.109 30.083  1.00 28.88 ? 340 GLU B O   1 
ATOM   4966 C  CB  . GLU B 1 351 ? -14.129 -15.512 27.477  1.00 34.70 ? 340 GLU B CB  1 
ATOM   4967 C  CG  . GLU B 1 351 ? -14.125 -16.731 26.595  1.00 33.88 ? 340 GLU B CG  1 
ATOM   4968 C  CD  . GLU B 1 351 ? -12.704 -17.216 26.312  1.00 51.23 ? 340 GLU B CD  1 
ATOM   4969 O  OE1 . GLU B 1 351 ? -11.739 -16.552 26.751  1.00 52.90 ? 340 GLU B OE1 1 
ATOM   4970 O  OE2 . GLU B 1 351 ? -12.536 -18.260 25.647  1.00 57.09 ? 340 GLU B OE2 1 
ATOM   4971 N  N   . ASN B 1 352 ? -15.523 -12.985 29.283  1.00 35.83 ? 341 ASN B N   1 
ATOM   4972 C  CA  . ASN B 1 352 ? -15.704 -12.269 30.546  1.00 31.03 ? 341 ASN B CA  1 
ATOM   4973 C  C   . ASN B 1 352 ? -17.120 -12.371 31.091  1.00 34.00 ? 341 ASN B C   1 
ATOM   4974 O  O   . ASN B 1 352 ? -17.346 -12.007 32.247  1.00 38.28 ? 341 ASN B O   1 
ATOM   4975 C  CB  . ASN B 1 352 ? -15.399 -10.782 30.364  1.00 33.96 ? 341 ASN B CB  1 
ATOM   4976 C  CG  . ASN B 1 352 ? -13.917 -10.473 30.343  1.00 40.67 ? 341 ASN B CG  1 
ATOM   4977 O  OD1 . ASN B 1 352 ? -13.071 -11.368 30.441  1.00 43.89 ? 341 ASN B OD1 1 
ATOM   4978 N  ND2 . ASN B 1 352 ? -13.592 -9.189  30.188  1.00 39.32 ? 341 ASN B ND2 1 
ATOM   4979 N  N   . VAL B 1 353 ? -18.075 -12.820 30.289  1.00 35.35 ? 342 VAL B N   1 
ATOM   4980 C  CA  . VAL B 1 353 ? -19.469 -12.775 30.668  1.00 32.31 ? 342 VAL B CA  1 
ATOM   4981 C  C   . VAL B 1 353 ? -20.006 -14.188 30.771  1.00 35.66 ? 342 VAL B C   1 
ATOM   4982 O  O   . VAL B 1 353 ? -20.460 -14.595 31.840  1.00 40.48 ? 342 VAL B O   1 
ATOM   4983 C  CB  . VAL B 1 353 ? -20.279 -11.927 29.671  1.00 29.93 ? 342 VAL B CB  1 
ATOM   4984 C  CG1 . VAL B 1 353 ? -21.749 -11.830 30.096  1.00 20.29 ? 342 VAL B CG1 1 
ATOM   4985 C  CG2 . VAL B 1 353 ? -19.638 -10.549 29.517  1.00 24.50 ? 342 VAL B CG2 1 
HETATM 4986 C  C1  . PGE C 2 .   ? -31.263 -5.782  -5.227  1.00 43.07 ? 401 PGE A C1  1 
HETATM 4987 O  O1  . PGE C 2 .   ? -31.886 -6.499  -6.277  1.00 41.42 ? 401 PGE A O1  1 
HETATM 4988 C  C2  . PGE C 2 .   ? -31.520 -6.380  -3.872  1.00 42.03 ? 401 PGE A C2  1 
HETATM 4989 O  O2  . PGE C 2 .   ? -32.768 -5.928  -3.360  1.00 48.09 ? 401 PGE A O2  1 
HETATM 4990 C  C3  . PGE C 2 .   ? -32.725 -4.590  -2.877  1.00 43.63 ? 401 PGE A C3  1 
HETATM 4991 C  C4  . PGE C 2 .   ? -34.109 -4.137  -2.505  1.00 51.23 ? 401 PGE A C4  1 
HETATM 4992 O  O4  . PGE C 2 .   ? -31.738 -0.474  -1.676  1.00 50.36 ? 401 PGE A O4  1 
HETATM 4993 C  C6  . PGE C 2 .   ? -33.138 -0.620  -1.907  1.00 64.45 ? 401 PGE A C6  1 
HETATM 4994 C  C5  . PGE C 2 .   ? -33.479 -1.852  -2.710  1.00 59.73 ? 401 PGE A C5  1 
HETATM 4995 O  O3  . PGE C 2 .   ? -34.043 -2.860  -1.875  1.00 60.22 ? 401 PGE A O3  1 
HETATM 4996 K  K   . K   D 3 .   ? -21.542 -2.364  -34.032 1.00 27.10 ? 402 K   A K   1 
HETATM 4997 K  K   . K   E 3 .   ? -17.761 10.562  -25.189 1.00 57.86 ? 403 K   A K   1 
HETATM 4998 K  K   . K   F 3 .   ? -35.534 1.656   -31.049 1.00 36.73 ? 404 K   A K   1 
HETATM 4999 ZN ZN  . ZN  G 4 .   ? -15.228 -0.468  -31.068 1.00 30.60 ? 405 ZN  A ZN  1 
HETATM 5000 CL CL  . CL  H 5 .   ? -15.166 1.611   -29.404 1.00 49.99 ? 406 CL  A CL  1 
HETATM 5001 C  C   . ACT I 6 .   ? -13.939 -6.660  4.274   1.00 37.40 ? 401 ACT B C   1 
HETATM 5002 O  O   . ACT I 6 .   ? -15.045 -6.104  4.538   1.00 34.87 ? 401 ACT B O   1 
HETATM 5003 O  OXT . ACT I 6 .   ? -12.768 -6.274  4.575   1.00 36.36 ? 401 ACT B OXT 1 
HETATM 5004 C  CH3 . ACT I 6 .   ? -14.019 -8.007  3.488   1.00 31.04 ? 401 ACT B CH3 1 
HETATM 5005 C  C1  . PEG J 7 .   ? -33.313 -6.889  -22.472 1.00 49.21 ? 402 PEG B C1  1 
HETATM 5006 O  O1  . PEG J 7 .   ? -32.876 -8.131  -23.010 1.00 47.30 ? 402 PEG B O1  1 
HETATM 5007 C  C2  . PEG J 7 .   ? -32.203 -5.873  -22.448 1.00 48.39 ? 402 PEG B C2  1 
HETATM 5008 O  O2  . PEG J 7 .   ? -32.584 -4.758  -21.645 1.00 59.05 ? 402 PEG B O2  1 
HETATM 5009 C  C3  . PEG J 7 .   ? -31.891 -4.691  -20.403 1.00 44.75 ? 402 PEG B C3  1 
HETATM 5010 C  C4  . PEG J 7 .   ? -32.818 -5.078  -19.293 1.00 46.73 ? 402 PEG B C4  1 
HETATM 5011 O  O4  . PEG J 7 .   ? -32.199 -4.900  -18.032 1.00 44.26 ? 402 PEG B O4  1 
HETATM 5012 K  K   . K   K 3 .   ? -21.072 -4.833  8.905   1.00 26.13 ? 403 K   B K   1 
HETATM 5013 K  K   . K   L 3 .   ? -33.111 -12.749 6.273   1.00 37.64 ? 404 K   B K   1 
HETATM 5014 K  K   . K   M 3 .   ? -21.909 -11.295 7.125   1.00 57.03 ? 405 K   B K   1 
HETATM 5015 ZN ZN  . ZN  N 4 .   ? -14.528 -4.589  6.052   1.00 31.86 ? 406 ZN  B ZN  1 
HETATM 5016 O  O   . HOH O 8 .   ? -28.477 24.069  -38.420 1.00 32.56 ? 501 HOH A O   1 
HETATM 5017 O  O   . HOH O 8 .   ? -34.421 7.540   -24.956 1.00 43.31 ? 502 HOH A O   1 
HETATM 5018 O  O   . HOH O 8 .   ? -29.659 10.114  -14.270 1.00 25.86 ? 503 HOH A O   1 
HETATM 5019 O  O   . HOH O 8 .   ? -19.089 -4.685  -37.092 1.00 26.72 ? 504 HOH A O   1 
HETATM 5020 O  O   . HOH O 8 .   ? -14.840 16.644  -45.616 1.00 27.81 ? 505 HOH A O   1 
HETATM 5021 O  O   . HOH O 8 .   ? -19.707 -6.620  -28.999 1.00 29.32 ? 506 HOH A O   1 
HETATM 5022 O  O   . HOH O 8 .   ? -10.833 12.179  -25.518 1.00 47.76 ? 507 HOH A O   1 
HETATM 5023 O  O   . HOH O 8 .   ? -9.678  6.663   -49.006 1.00 39.82 ? 508 HOH A O   1 
HETATM 5024 O  O   . HOH O 8 .   ? -46.073 5.063   -39.056 1.00 46.65 ? 509 HOH A O   1 
HETATM 5025 O  O   . HOH O 8 .   ? -27.762 6.416   -1.793  1.00 46.59 ? 510 HOH A O   1 
HETATM 5026 O  O   . HOH O 8 .   ? -34.717 -7.466  -34.033 1.00 28.77 ? 511 HOH A O   1 
HETATM 5027 O  O   . HOH O 8 .   ? -12.541 -5.807  -28.189 1.00 43.94 ? 512 HOH A O   1 
HETATM 5028 O  O   . HOH O 8 .   ? -15.119 -6.209  -50.380 1.00 28.71 ? 513 HOH A O   1 
HETATM 5029 O  O   . HOH O 8 .   ? -24.279 3.855   -32.079 1.00 30.53 ? 514 HOH A O   1 
HETATM 5030 O  O   . HOH O 8 .   ? -12.571 18.846  -18.655 1.00 31.04 ? 515 HOH A O   1 
HETATM 5031 O  O   . HOH O 8 .   ? -16.357 -1.287  -39.727 1.00 27.39 ? 516 HOH A O   1 
HETATM 5032 O  O   . HOH O 8 .   ? -16.627 -14.901 -42.921 1.00 29.00 ? 517 HOH A O   1 
HETATM 5033 O  O   . HOH O 8 .   ? -26.839 3.001   -3.205  1.00 31.09 ? 518 HOH A O   1 
HETATM 5034 O  O   . HOH O 8 .   ? -36.239 -0.751  -29.825 1.00 32.35 ? 519 HOH A O   1 
HETATM 5035 O  O   . HOH O 8 .   ? -21.192 23.013  -13.984 1.00 29.66 ? 520 HOH A O   1 
HETATM 5036 O  O   . HOH O 8 .   ? -18.761 13.115  -26.595 1.00 29.70 ? 521 HOH A O   1 
HETATM 5037 O  O   . HOH O 8 .   ? -16.816 19.882  -49.047 1.00 39.43 ? 522 HOH A O   1 
HETATM 5038 O  O   . HOH O 8 .   ? -13.200 -1.156  -21.233 1.00 34.21 ? 523 HOH A O   1 
HETATM 5039 O  O   . HOH O 8 .   ? -4.510  5.542   -43.125 1.00 35.64 ? 524 HOH A O   1 
HETATM 5040 O  O   . HOH O 8 .   ? -35.680 -7.278  -24.495 1.00 36.64 ? 525 HOH A O   1 
HETATM 5041 O  O   . HOH O 8 .   ? -32.758 0.446   -29.615 1.00 24.31 ? 526 HOH A O   1 
HETATM 5042 O  O   . HOH O 8 .   ? -15.639 6.359   -15.041 1.00 30.63 ? 527 HOH A O   1 
HETATM 5043 O  O   . HOH O 8 .   ? -19.099 8.722   -31.676 1.00 26.35 ? 528 HOH A O   1 
HETATM 5044 O  O   . HOH O 8 .   ? -31.963 -7.795  -32.215 1.00 30.94 ? 529 HOH A O   1 
HETATM 5045 O  O   . HOH O 8 .   ? -14.868 18.669  -13.082 1.00 25.45 ? 530 HOH A O   1 
HETATM 5046 O  O   . HOH O 8 .   ? -30.897 -0.823  -48.812 1.00 30.57 ? 531 HOH A O   1 
HETATM 5047 O  O   . HOH O 8 .   ? -20.048 15.456  -9.734  1.00 30.83 ? 532 HOH A O   1 
HETATM 5048 O  O   . HOH O 8 .   ? -29.175 21.231  -32.114 1.00 28.57 ? 533 HOH A O   1 
HETATM 5049 O  O   . HOH O 8 .   ? -21.955 7.799   -30.471 1.00 27.45 ? 534 HOH A O   1 
HETATM 5050 O  O   . HOH O 8 .   ? -35.751 4.007   -25.163 1.00 31.69 ? 535 HOH A O   1 
HETATM 5051 O  O   . HOH O 8 .   ? -21.613 -15.597 -33.275 1.00 30.26 ? 536 HOH A O   1 
HETATM 5052 O  O   . HOH O 8 .   ? -32.009 17.759  -29.992 1.00 30.08 ? 537 HOH A O   1 
HETATM 5053 O  O   . HOH O 8 .   ? -8.311  22.140  -33.255 1.00 55.02 ? 538 HOH A O   1 
HETATM 5054 O  O   . HOH O 8 .   ? -30.080 -14.275 -28.561 1.00 33.99 ? 539 HOH A O   1 
HETATM 5055 O  O   . HOH O 8 .   ? -12.684 16.231  -33.131 1.00 34.78 ? 540 HOH A O   1 
HETATM 5056 O  O   . HOH O 8 .   ? -30.400 4.813   -21.384 1.00 25.61 ? 541 HOH A O   1 
HETATM 5057 O  O   . HOH O 8 .   ? -32.694 19.464  -23.286 1.00 27.14 ? 542 HOH A O   1 
HETATM 5058 O  O   . HOH O 8 .   ? -15.401 4.208   -16.295 1.00 35.27 ? 543 HOH A O   1 
HETATM 5059 O  O   . HOH O 8 .   ? -16.618 2.896   -7.466  1.00 36.03 ? 544 HOH A O   1 
HETATM 5060 O  O   . HOH O 8 .   ? -24.452 1.138   -13.335 1.00 23.36 ? 545 HOH A O   1 
HETATM 5061 O  O   . HOH O 8 .   ? -26.033 13.923  -10.216 1.00 27.23 ? 546 HOH A O   1 
HETATM 5062 O  O   . HOH O 8 .   ? -14.551 15.283  -31.316 1.00 24.92 ? 547 HOH A O   1 
HETATM 5063 O  O   . HOH O 8 .   ? -33.508 18.242  -39.713 1.00 38.97 ? 548 HOH A O   1 
HETATM 5064 O  O   . HOH O 8 .   ? -18.122 7.126   -59.264 1.00 26.64 ? 549 HOH A O   1 
HETATM 5065 O  O   . HOH O 8 .   ? -23.786 9.250   -53.220 1.00 31.44 ? 550 HOH A O   1 
HETATM 5066 O  O   . HOH O 8 .   ? -17.055 12.136  -2.103  1.00 38.18 ? 551 HOH A O   1 
HETATM 5067 O  O   . HOH O 8 .   ? -8.494  0.677   -38.564 1.00 35.18 ? 552 HOH A O   1 
HETATM 5068 O  O   . HOH O 8 .   ? -10.939 1.253   -30.564 1.00 39.14 ? 553 HOH A O   1 
HETATM 5069 O  O   . HOH O 8 .   ? -31.271 -2.790  -24.434 1.00 31.03 ? 554 HOH A O   1 
HETATM 5070 O  O   . HOH O 8 .   ? -26.118 -13.824 -29.518 1.00 36.58 ? 555 HOH A O   1 
HETATM 5071 O  O   . HOH O 8 .   ? -17.123 -17.036 -32.219 1.00 27.39 ? 556 HOH A O   1 
HETATM 5072 O  O   . HOH O 8 .   ? -32.873 4.242   3.740   1.00 28.13 ? 557 HOH A O   1 
HETATM 5073 O  O   . HOH O 8 .   ? -25.067 -5.625  -50.269 1.00 32.96 ? 558 HOH A O   1 
HETATM 5074 O  O   . HOH O 8 .   ? -15.166 9.020   -2.946  1.00 25.84 ? 559 HOH A O   1 
HETATM 5075 O  O   . HOH O 8 .   ? -14.259 -0.509  -26.483 1.00 31.33 ? 560 HOH A O   1 
HETATM 5076 O  O   . HOH O 8 .   ? -11.152 6.740   -30.150 1.00 40.54 ? 561 HOH A O   1 
HETATM 5077 O  O   . HOH O 8 .   ? -25.024 28.067  -33.650 1.00 31.61 ? 562 HOH A O   1 
HETATM 5078 O  O   . HOH O 8 .   ? -13.133 -2.546  -23.521 1.00 39.61 ? 563 HOH A O   1 
HETATM 5079 O  O   . HOH O 8 .   ? -15.032 -17.078 -30.327 1.00 32.54 ? 564 HOH A O   1 
HETATM 5080 O  O   . HOH O 8 .   ? -10.253 -1.949  -20.874 1.00 42.79 ? 565 HOH A O   1 
HETATM 5081 O  O   . HOH P 8 .   ? -28.756 -5.018  -15.712 1.00 30.39 ? 501 HOH B O   1 
HETATM 5082 O  O   . HOH P 8 .   ? -10.312 -12.779 7.093   1.00 32.77 ? 502 HOH B O   1 
HETATM 5083 O  O   . HOH P 8 .   ? -6.114  -22.140 -7.914  1.00 35.70 ? 503 HOH B O   1 
HETATM 5084 O  O   . HOH P 8 .   ? -14.157 -19.009 30.137  1.00 36.78 ? 504 HOH B O   1 
HETATM 5085 O  O   . HOH P 8 .   ? -33.728 -10.407 -23.302 1.00 38.77 ? 505 HOH B O   1 
HETATM 5086 O  O   . HOH P 8 .   ? -40.270 -17.983 21.542  1.00 33.06 ? 506 HOH B O   1 
HETATM 5087 O  O   . HOH P 8 .   ? -26.007 -27.731 14.629  1.00 38.76 ? 507 HOH B O   1 
HETATM 5088 O  O   . HOH P 8 .   ? -24.339 -15.096 22.627  1.00 34.61 ? 508 HOH B O   1 
HETATM 5089 O  O   . HOH P 8 .   ? -30.984 -11.059 4.577   1.00 31.15 ? 509 HOH B O   1 
HETATM 5090 O  O   . HOH P 8 .   ? -20.743 -4.612  26.860  1.00 27.58 ? 510 HOH B O   1 
HETATM 5091 O  O   . HOH P 8 .   ? -27.062 -15.904 -24.474 1.00 36.72 ? 511 HOH B O   1 
HETATM 5092 O  O   . HOH P 8 .   ? -2.551  -10.261 -21.628 1.00 53.18 ? 512 HOH B O   1 
HETATM 5093 O  O   . HOH P 8 .   ? -20.216 8.897   17.323  1.00 31.95 ? 513 HOH B O   1 
HETATM 5094 O  O   . HOH P 8 .   ? -28.271 4.781   3.287   1.00 29.65 ? 514 HOH B O   1 
HETATM 5095 O  O   . HOH P 8 .   ? -15.947 -4.050  14.456  1.00 28.88 ? 515 HOH B O   1 
HETATM 5096 O  O   . HOH P 8 .   ? -6.750  -9.219  23.521  1.00 42.18 ? 516 HOH B O   1 
HETATM 5097 O  O   . HOH P 8 .   ? -26.121 0.415   -22.263 1.00 28.29 ? 517 HOH B O   1 
HETATM 5098 O  O   . HOH P 8 .   ? -20.869 11.556  0.771   1.00 35.02 ? 518 HOH B O   1 
HETATM 5099 O  O   . HOH P 8 .   ? -14.683 -8.705  -17.250 1.00 32.78 ? 519 HOH B O   1 
HETATM 5100 O  O   . HOH P 8 .   ? -9.514  -20.976 -10.609 1.00 31.42 ? 520 HOH B O   1 
HETATM 5101 O  O   . HOH P 8 .   ? -15.226 -14.541 6.555   1.00 35.27 ? 521 HOH B O   1 
HETATM 5102 O  O   . HOH P 8 .   ? -12.949 -8.849  -8.705  1.00 28.75 ? 522 HOH B O   1 
HETATM 5103 O  O   . HOH P 8 .   ? -13.214 -11.120 -9.919  1.00 34.01 ? 523 HOH B O   1 
HETATM 5104 O  O   . HOH P 8 .   ? -22.584 -9.313  -11.251 1.00 26.03 ? 524 HOH B O   1 
HETATM 5105 O  O   . HOH P 8 .   ? -13.539 -16.125 0.627   1.00 24.41 ? 525 HOH B O   1 
HETATM 5106 O  O   . HOH P 8 .   ? -8.440  -19.908 20.849  1.00 43.53 ? 526 HOH B O   1 
HETATM 5107 O  O   . HOH P 8 .   ? -13.723 -18.568 1.500   1.00 28.03 ? 527 HOH B O   1 
HETATM 5108 O  O   . HOH P 8 .   ? -15.586 4.992   20.580  1.00 28.37 ? 528 HOH B O   1 
HETATM 5109 O  O   . HOH P 8 .   ? -34.579 -10.916 5.173   1.00 36.70 ? 529 HOH B O   1 
HETATM 5110 O  O   . HOH P 8 .   ? -26.693 4.471   16.990  1.00 38.67 ? 530 HOH B O   1 
HETATM 5111 O  O   . HOH P 8 .   ? -27.019 -14.406 -3.729  1.00 27.74 ? 531 HOH B O   1 
HETATM 5112 O  O   . HOH P 8 .   ? -14.062 -21.229 -15.101 1.00 32.22 ? 532 HOH B O   1 
HETATM 5113 O  O   . HOH P 8 .   ? -18.577 -14.410 5.545   1.00 30.62 ? 533 HOH B O   1 
HETATM 5114 O  O   . HOH P 8 .   ? -33.227 -15.287 21.891  1.00 42.18 ? 534 HOH B O   1 
HETATM 5115 O  O   . HOH P 8 .   ? -27.545 -4.674  -13.242 1.00 29.97 ? 535 HOH B O   1 
HETATM 5116 O  O   . HOH P 8 .   ? -36.299 -4.935  -0.366  1.00 34.24 ? 536 HOH B O   1 
HETATM 5117 O  O   . HOH P 8 .   ? -20.774 -0.375  4.054   1.00 21.79 ? 537 HOH B O   1 
HETATM 5118 O  O   . HOH P 8 .   ? -19.204 -1.787  12.020  1.00 28.07 ? 538 HOH B O   1 
HETATM 5119 O  O   . HOH P 8 .   ? -25.391 -19.695 -10.980 1.00 30.57 ? 539 HOH B O   1 
HETATM 5120 O  O   . HOH P 8 .   ? -20.144 -29.398 10.540  1.00 34.00 ? 540 HOH B O   1 
HETATM 5121 O  O   . HOH P 8 .   ? -13.586 0.996   2.142   1.00 30.39 ? 541 HOH B O   1 
HETATM 5122 O  O   . HOH P 8 .   ? -24.033 -25.087 4.743   1.00 27.02 ? 542 HOH B O   1 
HETATM 5123 O  O   . HOH P 8 .   ? -8.155  -3.422  12.595  1.00 37.13 ? 543 HOH B O   1 
HETATM 5124 O  O   . HOH P 8 .   ? -11.468 -13.842 -22.241 1.00 30.05 ? 544 HOH B O   1 
HETATM 5125 O  O   . HOH P 8 .   ? -24.782 -9.099  -2.497  1.00 31.74 ? 545 HOH B O   1 
HETATM 5126 O  O   . HOH P 8 .   ? -23.741 -16.257 25.245  1.00 35.67 ? 546 HOH B O   1 
HETATM 5127 O  O   . HOH P 8 .   ? -11.182 6.860   11.492  1.00 35.97 ? 547 HOH B O   1 
HETATM 5128 O  O   . HOH P 8 .   ? -7.310  -10.600 -16.472 1.00 34.05 ? 548 HOH B O   1 
HETATM 5129 O  O   . HOH P 8 .   ? -14.270 -4.728  1.704   1.00 33.28 ? 549 HOH B O   1 
HETATM 5130 O  O   . HOH P 8 .   ? -7.645  -20.171 -8.244  1.00 31.88 ? 550 HOH B O   1 
HETATM 5131 O  O   . HOH P 8 .   ? 0.000   -0.000  12.957  0.50 30.31 ? 551 HOH B O   1 
HETATM 5132 O  O   . HOH P 8 .   ? -24.272 -2.278  23.490  1.00 29.82 ? 552 HOH B O   1 
HETATM 5133 O  O   . HOH P 8 .   ? -30.447 -7.452  -0.858  1.00 32.35 ? 553 HOH B O   1 
HETATM 5134 O  O   . HOH P 8 .   ? -10.140 -4.867  5.687   1.00 27.31 ? 554 HOH B O   1 
HETATM 5135 O  O   . HOH P 8 .   ? -30.579 4.401   4.773   1.00 32.99 ? 555 HOH B O   1 
HETATM 5136 O  O   . HOH P 8 .   ? -8.648  -19.709 6.812   1.00 34.19 ? 556 HOH B O   1 
HETATM 5137 O  O   . HOH P 8 .   ? -6.708  -15.724 -1.408  1.00 36.17 ? 557 HOH B O   1 
HETATM 5138 O  O   . HOH P 8 .   ? -23.441 -5.551  27.609  1.00 27.49 ? 558 HOH B O   1 
HETATM 5139 O  O   . HOH P 8 .   ? -25.708 -31.961 -5.701  1.00 22.43 ? 559 HOH B O   1 
HETATM 5140 O  O   . HOH P 8 .   ? -12.750 -17.361 31.644  1.00 27.49 ? 560 HOH B O   1 
HETATM 5141 O  O   . HOH P 8 .   ? -32.148 -11.347 -20.556 1.00 36.22 ? 561 HOH B O   1 
HETATM 5142 O  O   . HOH P 8 .   ? -9.358  -4.630  -21.838 1.00 39.10 ? 562 HOH B O   1 
HETATM 5143 O  O   . HOH P 8 .   ? -9.946  -1.500  28.601  1.00 31.25 ? 563 HOH B O   1 
HETATM 5144 O  O   . HOH P 8 .   ? -8.280  -5.855  -24.641 1.00 45.68 ? 564 HOH B O   1 
# 
