data_9EFR
# 
_entry.id   9EFR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EFR         pdb_00009efr 10.2210/pdb9efr/pdb 
WWPDB D_1000290329 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-12-04 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EFR 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              patrick.gunning@utoronto.ca 
_pdbx_contact_author.name_first         Patrick 
_pdbx_contact_author.name_last          Gunning 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0654-735X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Erdogan, F.'     1 0000-0002-6968-4821 
'Seo, H.-S.'      2 0000-0003-0646-2102 
'Dhe-Paganon, S.' 3 0000-0003-0824-5929 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Bisected Cap Group Modifications Provides Basis for Improved Pharmacokinetics of HDAC Inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Olaoye, O.'    1 ? 
primary 'Erdogan, F.'   2 ? 
primary 'Gunning, P.T.' 3 ? 
# 
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 'Hdac6 protein'                                                                  39724.973 2   ? ? 
'catalytic domain 2 (UNP residues 290-646)' ? 
2 non-polymer syn 'N-hydroxy-4-({(propane-2-sulfonyl)[(pyridin-3-yl)methyl]amino}methyl)benzamide' 363.431   2   ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                       65.409    2   ? ? ? ? 
4 non-polymer syn 'POTASSIUM ION'                                                                  39.098    5   ? ? ? ? 
5 water       nat water                                                                            18.015    788 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Histone Deacetylase 6' 
# 
_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       
;PITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRD
LNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITR
ESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAA
FHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSML
LGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRD
LNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITR
ESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAA
FHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSML
LGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_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 'N-hydroxy-4-({(propane-2-sulfonyl)[(pyridin-3-yl)methyl]amino}methyl)benzamide' A1BHX 
3 'ZINC ION'                                                                       ZN    
4 'POTASSIUM ION'                                                                  K     
5 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   ILE n 
1 3   THR n 
1 4   GLY n 
1 5   LEU n 
1 6   VAL n 
1 7   TYR n 
1 8   ASP n 
1 9   GLN n 
1 10  ARG n 
1 11  MET n 
1 12  MET n 
1 13  LEU n 
1 14  HIS n 
1 15  HIS n 
1 16  ASN n 
1 17  MET n 
1 18  TRP n 
1 19  ASP n 
1 20  SER n 
1 21  HIS n 
1 22  HIS n 
1 23  PRO n 
1 24  GLU n 
1 25  LEU n 
1 26  PRO n 
1 27  GLN n 
1 28  ARG n 
1 29  ILE n 
1 30  SER n 
1 31  ARG n 
1 32  ILE n 
1 33  PHE n 
1 34  SER n 
1 35  ARG n 
1 36  HIS n 
1 37  GLU n 
1 38  GLU n 
1 39  LEU n 
1 40  ARG n 
1 41  LEU n 
1 42  LEU n 
1 43  SER n 
1 44  ARG n 
1 45  CYS n 
1 46  HIS n 
1 47  ARG n 
1 48  ILE n 
1 49  PRO n 
1 50  ALA n 
1 51  ARG n 
1 52  LEU n 
1 53  ALA n 
1 54  THR n 
1 55  GLU n 
1 56  GLU n 
1 57  GLU n 
1 58  LEU n 
1 59  ALA n 
1 60  LEU n 
1 61  CYS n 
1 62  HIS n 
1 63  SER n 
1 64  SER n 
1 65  LYS n 
1 66  HIS n 
1 67  ILE n 
1 68  SER n 
1 69  ILE n 
1 70  ILE n 
1 71  LYS n 
1 72  SER n 
1 73  SER n 
1 74  GLU n 
1 75  HIS n 
1 76  MET n 
1 77  LYS n 
1 78  PRO n 
1 79  ARG n 
1 80  ASP n 
1 81  LEU n 
1 82  ASN n 
1 83  ARG n 
1 84  LEU n 
1 85  GLY n 
1 86  ASP n 
1 87  GLU n 
1 88  TYR n 
1 89  ASN n 
1 90  SER n 
1 91  ILE n 
1 92  PHE n 
1 93  ILE n 
1 94  SER n 
1 95  ASN n 
1 96  GLU n 
1 97  SER n 
1 98  TYR n 
1 99  THR n 
1 100 CYS n 
1 101 ALA n 
1 102 LEU n 
1 103 LEU n 
1 104 ALA n 
1 105 ALA n 
1 106 GLY n 
1 107 SER n 
1 108 CYS n 
1 109 PHE n 
1 110 ASN n 
1 111 SER n 
1 112 ALA n 
1 113 GLN n 
1 114 ALA n 
1 115 ILE n 
1 116 LEU n 
1 117 THR n 
1 118 GLY n 
1 119 GLN n 
1 120 VAL n 
1 121 ARG n 
1 122 ASN n 
1 123 ALA n 
1 124 VAL n 
1 125 ALA n 
1 126 ILE n 
1 127 VAL n 
1 128 ARG n 
1 129 PRO n 
1 130 PRO n 
1 131 GLY n 
1 132 HIS n 
1 133 HIS n 
1 134 ALA n 
1 135 GLU n 
1 136 LYS n 
1 137 ASP n 
1 138 THR n 
1 139 ALA n 
1 140 CYS n 
1 141 GLY n 
1 142 PHE n 
1 143 CYS n 
1 144 PHE n 
1 145 PHE n 
1 146 ASN n 
1 147 THR n 
1 148 ALA n 
1 149 ALA n 
1 150 LEU n 
1 151 THR n 
1 152 ALA n 
1 153 ARG n 
1 154 TYR n 
1 155 ALA n 
1 156 GLN n 
1 157 SER n 
1 158 ILE n 
1 159 THR n 
1 160 ARG n 
1 161 GLU n 
1 162 SER n 
1 163 LEU n 
1 164 ARG n 
1 165 VAL n 
1 166 LEU n 
1 167 ILE n 
1 168 VAL n 
1 169 ASP n 
1 170 TRP n 
1 171 ASP n 
1 172 VAL n 
1 173 HIS n 
1 174 HIS n 
1 175 GLY n 
1 176 ASN n 
1 177 GLY n 
1 178 THR n 
1 179 GLN n 
1 180 HIS n 
1 181 ILE n 
1 182 PHE n 
1 183 GLU n 
1 184 GLU n 
1 185 ASP n 
1 186 ASP n 
1 187 SER n 
1 188 VAL n 
1 189 LEU n 
1 190 TYR n 
1 191 ILE n 
1 192 SER n 
1 193 LEU n 
1 194 HIS n 
1 195 ARG n 
1 196 TYR n 
1 197 GLU n 
1 198 ASP n 
1 199 GLY n 
1 200 ALA n 
1 201 PHE n 
1 202 PHE n 
1 203 PRO n 
1 204 ASN n 
1 205 SER n 
1 206 GLU n 
1 207 ASP n 
1 208 ALA n 
1 209 ASN n 
1 210 TYR n 
1 211 ASP n 
1 212 LYS n 
1 213 VAL n 
1 214 GLY n 
1 215 LEU n 
1 216 GLY n 
1 217 LYS n 
1 218 GLY n 
1 219 ARG n 
1 220 GLY n 
1 221 TYR n 
1 222 ASN n 
1 223 VAL n 
1 224 ASN n 
1 225 ILE n 
1 226 PRO n 
1 227 TRP n 
1 228 ASN n 
1 229 GLY n 
1 230 GLY n 
1 231 LYS n 
1 232 MET n 
1 233 GLY n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 TYR n 
1 238 MET n 
1 239 ALA n 
1 240 ALA n 
1 241 PHE n 
1 242 HIS n 
1 243 HIS n 
1 244 LEU n 
1 245 VAL n 
1 246 MET n 
1 247 PRO n 
1 248 ILE n 
1 249 ALA n 
1 250 ARG n 
1 251 GLU n 
1 252 PHE n 
1 253 ALA n 
1 254 PRO n 
1 255 GLU n 
1 256 LEU n 
1 257 VAL n 
1 258 LEU n 
1 259 VAL n 
1 260 SER n 
1 261 ALA n 
1 262 GLY n 
1 263 PHE n 
1 264 ASP n 
1 265 ALA n 
1 266 ALA n 
1 267 ARG n 
1 268 GLY n 
1 269 ASP n 
1 270 PRO n 
1 271 LEU n 
1 272 GLY n 
1 273 GLY n 
1 274 PHE n 
1 275 GLN n 
1 276 VAL n 
1 277 THR n 
1 278 PRO n 
1 279 GLU n 
1 280 GLY n 
1 281 TYR n 
1 282 ALA n 
1 283 HIS n 
1 284 LEU n 
1 285 THR n 
1 286 HIS n 
1 287 GLN n 
1 288 LEU n 
1 289 MET n 
1 290 SER n 
1 291 LEU n 
1 292 ALA n 
1 293 ALA n 
1 294 GLY n 
1 295 ARG n 
1 296 VAL n 
1 297 LEU n 
1 298 ILE n 
1 299 ILE n 
1 300 LEU n 
1 301 GLU n 
1 302 GLY n 
1 303 GLY n 
1 304 TYR n 
1 305 ASN n 
1 306 LEU n 
1 307 THR n 
1 308 SER n 
1 309 ILE n 
1 310 SER n 
1 311 GLU n 
1 312 SER n 
1 313 MET n 
1 314 SER n 
1 315 MET n 
1 316 CYS n 
1 317 THR n 
1 318 SER n 
1 319 MET n 
1 320 LEU n 
1 321 LEU n 
1 322 GLY n 
1 323 ASP n 
1 324 SER n 
1 325 PRO n 
1 326 PRO n 
1 327 SER n 
1 328 LEU n 
1 329 ASP n 
1 330 HIS n 
1 331 LEU n 
1 332 THR n 
1 333 PRO n 
1 334 LEU n 
1 335 LYS n 
1 336 THR n 
1 337 SER n 
1 338 ALA n 
1 339 THR n 
1 340 VAL n 
1 341 SER n 
1 342 ILE n 
1 343 ASN n 
1 344 ASN n 
1 345 VAL n 
1 346 LEU n 
1 347 ARG n 
1 348 ALA n 
1 349 HIS n 
1 350 ALA n 
1 351 PRO n 
1 352 PHE n 
1 353 TRP n 
1 354 SER n 
1 355 SER n 
1 356 LEU n 
1 357 ARG 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                   357 
_entity_src_gen.gene_src_common_name               zebrafish 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 hdac6 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Danio rerio' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7955 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BHX non-polymer         . 'N-hydroxy-4-({(propane-2-sulfonyl)[(pyridin-3-yl)methyl]amino}methyl)benzamide' ? 'C17 H21 N3 O4 S' 
363.431 
ALA   'L-peptide linking' y ALANINE                                                                          ? 'C3 H7 N O2'      
89.093  
ARG   'L-peptide linking' y ARGININE                                                                         ? 'C6 H15 N4 O2 1'  
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                       ? 'C4 H8 N2 O3'     
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                  ? 'C4 H7 N O4'      
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'    
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'    
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'      
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'      
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1'  
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'            
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'     
131.173 
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 
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   PRO 1   442 442 PRO PRO A . n 
A 1 2   ILE 2   443 443 ILE ILE A . n 
A 1 3   THR 3   444 444 THR THR A . n 
A 1 4   GLY 4   445 445 GLY GLY A . n 
A 1 5   LEU 5   446 446 LEU LEU A . n 
A 1 6   VAL 6   447 447 VAL VAL A . n 
A 1 7   TYR 7   448 448 TYR TYR A . n 
A 1 8   ASP 8   449 449 ASP ASP A . n 
A 1 9   GLN 9   450 450 GLN GLN A . n 
A 1 10  ARG 10  451 451 ARG ARG A . n 
A 1 11  MET 11  452 452 MET MET A . n 
A 1 12  MET 12  453 453 MET MET A . n 
A 1 13  LEU 13  454 454 LEU LEU A . n 
A 1 14  HIS 14  455 455 HIS HIS A . n 
A 1 15  HIS 15  456 456 HIS HIS A . n 
A 1 16  ASN 16  457 457 ASN ASN A . n 
A 1 17  MET 17  458 458 MET MET A . n 
A 1 18  TRP 18  459 459 TRP TRP A . n 
A 1 19  ASP 19  460 460 ASP ASP A . n 
A 1 20  SER 20  461 461 SER SER A . n 
A 1 21  HIS 21  462 462 HIS HIS A . n 
A 1 22  HIS 22  463 463 HIS HIS A . n 
A 1 23  PRO 23  464 464 PRO PRO A . n 
A 1 24  GLU 24  465 465 GLU GLU A . n 
A 1 25  LEU 25  466 466 LEU LEU A . n 
A 1 26  PRO 26  467 467 PRO PRO A . n 
A 1 27  GLN 27  468 468 GLN GLN A . n 
A 1 28  ARG 28  469 469 ARG ARG A . n 
A 1 29  ILE 29  470 470 ILE ILE A . n 
A 1 30  SER 30  471 471 SER SER A . n 
A 1 31  ARG 31  472 472 ARG ARG A . n 
A 1 32  ILE 32  473 473 ILE ILE A . n 
A 1 33  PHE 33  474 474 PHE PHE A . n 
A 1 34  SER 34  475 475 SER SER A . n 
A 1 35  ARG 35  476 476 ARG ARG A . n 
A 1 36  HIS 36  477 477 HIS HIS A . n 
A 1 37  GLU 37  478 478 GLU GLU A . n 
A 1 38  GLU 38  479 479 GLU GLU A . n 
A 1 39  LEU 39  480 480 LEU LEU A . n 
A 1 40  ARG 40  481 481 ARG ARG A . n 
A 1 41  LEU 41  482 482 LEU LEU A . n 
A 1 42  LEU 42  483 483 LEU LEU A . n 
A 1 43  SER 43  484 484 SER SER A . n 
A 1 44  ARG 44  485 485 ARG ARG A . n 
A 1 45  CYS 45  486 486 CYS CYS A . n 
A 1 46  HIS 46  487 487 HIS HIS A . n 
A 1 47  ARG 47  488 488 ARG ARG A . n 
A 1 48  ILE 48  489 489 ILE ILE A . n 
A 1 49  PRO 49  490 490 PRO PRO A . n 
A 1 50  ALA 50  491 491 ALA ALA A . n 
A 1 51  ARG 51  492 492 ARG ARG A . n 
A 1 52  LEU 52  493 493 LEU LEU A . n 
A 1 53  ALA 53  494 494 ALA ALA A . n 
A 1 54  THR 54  495 495 THR THR A . n 
A 1 55  GLU 55  496 496 GLU GLU A . n 
A 1 56  GLU 56  497 497 GLU GLU A . n 
A 1 57  GLU 57  498 498 GLU GLU A . n 
A 1 58  LEU 58  499 499 LEU LEU A . n 
A 1 59  ALA 59  500 500 ALA ALA A . n 
A 1 60  LEU 60  501 501 LEU LEU A . n 
A 1 61  CYS 61  502 502 CYS CYS A . n 
A 1 62  HIS 62  503 503 HIS HIS A . n 
A 1 63  SER 63  504 504 SER SER A . n 
A 1 64  SER 64  505 505 SER SER A . n 
A 1 65  LYS 65  506 506 LYS LYS A . n 
A 1 66  HIS 66  507 507 HIS HIS A . n 
A 1 67  ILE 67  508 508 ILE ILE A . n 
A 1 68  SER 68  509 509 SER SER A . n 
A 1 69  ILE 69  510 510 ILE ILE A . n 
A 1 70  ILE 70  511 511 ILE ILE A . n 
A 1 71  LYS 71  512 512 LYS LYS A . n 
A 1 72  SER 72  513 513 SER SER A . n 
A 1 73  SER 73  514 514 SER SER A . n 
A 1 74  GLU 74  515 515 GLU GLU A . n 
A 1 75  HIS 75  516 516 HIS HIS A . n 
A 1 76  MET 76  517 517 MET MET A . n 
A 1 77  LYS 77  518 518 LYS LYS A . n 
A 1 78  PRO 78  519 519 PRO PRO A . n 
A 1 79  ARG 79  520 520 ARG ARG A . n 
A 1 80  ASP 80  521 521 ASP ASP A . n 
A 1 81  LEU 81  522 522 LEU LEU A . n 
A 1 82  ASN 82  523 523 ASN ASN A . n 
A 1 83  ARG 83  524 524 ARG ARG A . n 
A 1 84  LEU 84  525 525 LEU LEU A . n 
A 1 85  GLY 85  526 526 GLY GLY A . n 
A 1 86  ASP 86  527 527 ASP ASP A . n 
A 1 87  GLU 87  528 528 GLU GLU A . n 
A 1 88  TYR 88  529 529 TYR TYR A . n 
A 1 89  ASN 89  530 530 ASN ASN A . n 
A 1 90  SER 90  531 531 SER SER A . n 
A 1 91  ILE 91  532 532 ILE ILE A . n 
A 1 92  PHE 92  533 533 PHE PHE A . n 
A 1 93  ILE 93  534 534 ILE ILE A . n 
A 1 94  SER 94  535 535 SER SER A . n 
A 1 95  ASN 95  536 536 ASN ASN A . n 
A 1 96  GLU 96  537 537 GLU GLU A . n 
A 1 97  SER 97  538 538 SER SER A . n 
A 1 98  TYR 98  539 539 TYR TYR A . n 
A 1 99  THR 99  540 540 THR THR A . n 
A 1 100 CYS 100 541 541 CYS CYS A . n 
A 1 101 ALA 101 542 542 ALA ALA A . n 
A 1 102 LEU 102 543 543 LEU LEU A . n 
A 1 103 LEU 103 544 544 LEU LEU A . n 
A 1 104 ALA 104 545 545 ALA ALA A . n 
A 1 105 ALA 105 546 546 ALA ALA A . n 
A 1 106 GLY 106 547 547 GLY GLY A . n 
A 1 107 SER 107 548 548 SER SER A . n 
A 1 108 CYS 108 549 549 CYS CYS A . n 
A 1 109 PHE 109 550 550 PHE PHE A . n 
A 1 110 ASN 110 551 551 ASN ASN A . n 
A 1 111 SER 111 552 552 SER SER A . n 
A 1 112 ALA 112 553 553 ALA ALA A . n 
A 1 113 GLN 113 554 554 GLN GLN A . n 
A 1 114 ALA 114 555 555 ALA ALA A . n 
A 1 115 ILE 115 556 556 ILE ILE A . n 
A 1 116 LEU 116 557 557 LEU LEU A . n 
A 1 117 THR 117 558 558 THR THR A . n 
A 1 118 GLY 118 559 559 GLY GLY A . n 
A 1 119 GLN 119 560 560 GLN GLN A . n 
A 1 120 VAL 120 561 561 VAL VAL A . n 
A 1 121 ARG 121 562 562 ARG ARG A . n 
A 1 122 ASN 122 563 563 ASN ASN A . n 
A 1 123 ALA 123 564 564 ALA ALA A . n 
A 1 124 VAL 124 565 565 VAL VAL A . n 
A 1 125 ALA 125 566 566 ALA ALA A . n 
A 1 126 ILE 126 567 567 ILE ILE A . n 
A 1 127 VAL 127 568 568 VAL VAL A . n 
A 1 128 ARG 128 569 569 ARG ARG A . n 
A 1 129 PRO 129 570 570 PRO PRO A . n 
A 1 130 PRO 130 571 571 PRO PRO A . n 
A 1 131 GLY 131 572 572 GLY GLY A . n 
A 1 132 HIS 132 573 573 HIS HIS A . n 
A 1 133 HIS 133 574 574 HIS HIS A . n 
A 1 134 ALA 134 575 575 ALA ALA A . n 
A 1 135 GLU 135 576 576 GLU GLU A . n 
A 1 136 LYS 136 577 577 LYS LYS A . n 
A 1 137 ASP 137 578 578 ASP ASP A . n 
A 1 138 THR 138 579 579 THR THR A . n 
A 1 139 ALA 139 580 580 ALA ALA A . n 
A 1 140 CYS 140 581 581 CYS CYS A . n 
A 1 141 GLY 141 582 582 GLY GLY A . n 
A 1 142 PHE 142 583 583 PHE PHE A . n 
A 1 143 CYS 143 584 584 CYS CYS A . n 
A 1 144 PHE 144 585 585 PHE PHE A . n 
A 1 145 PHE 145 586 586 PHE PHE A . n 
A 1 146 ASN 146 587 587 ASN ASN A . n 
A 1 147 THR 147 588 588 THR THR A . n 
A 1 148 ALA 148 589 589 ALA ALA A . n 
A 1 149 ALA 149 590 590 ALA ALA A . n 
A 1 150 LEU 150 591 591 LEU LEU A . n 
A 1 151 THR 151 592 592 THR THR A . n 
A 1 152 ALA 152 593 593 ALA ALA A . n 
A 1 153 ARG 153 594 594 ARG ARG A . n 
A 1 154 TYR 154 595 595 TYR TYR A . n 
A 1 155 ALA 155 596 596 ALA ALA A . n 
A 1 156 GLN 156 597 597 GLN GLN A . n 
A 1 157 SER 157 598 598 SER SER A . n 
A 1 158 ILE 158 599 599 ILE ILE A . n 
A 1 159 THR 159 600 600 THR THR A . n 
A 1 160 ARG 160 601 601 ARG ARG A . n 
A 1 161 GLU 161 602 602 GLU GLU A . n 
A 1 162 SER 162 603 603 SER SER A . n 
A 1 163 LEU 163 604 604 LEU LEU A . n 
A 1 164 ARG 164 605 605 ARG ARG A . n 
A 1 165 VAL 165 606 606 VAL VAL A . n 
A 1 166 LEU 166 607 607 LEU LEU A . n 
A 1 167 ILE 167 608 608 ILE ILE A . n 
A 1 168 VAL 168 609 609 VAL VAL A . n 
A 1 169 ASP 169 610 610 ASP ASP A . n 
A 1 170 TRP 170 611 611 TRP TRP A . n 
A 1 171 ASP 171 612 612 ASP ASP A . n 
A 1 172 VAL 172 613 613 VAL VAL A . n 
A 1 173 HIS 173 614 614 HIS HIS A . n 
A 1 174 HIS 174 615 615 HIS HIS A . n 
A 1 175 GLY 175 616 616 GLY GLY A . n 
A 1 176 ASN 176 617 617 ASN ASN A . n 
A 1 177 GLY 177 618 618 GLY GLY A . n 
A 1 178 THR 178 619 619 THR THR A . n 
A 1 179 GLN 179 620 620 GLN GLN A . n 
A 1 180 HIS 180 621 621 HIS HIS A . n 
A 1 181 ILE 181 622 622 ILE ILE A . n 
A 1 182 PHE 182 623 623 PHE PHE A . n 
A 1 183 GLU 183 624 624 GLU GLU A . n 
A 1 184 GLU 184 625 625 GLU GLU A . n 
A 1 185 ASP 185 626 626 ASP ASP A . n 
A 1 186 ASP 186 627 627 ASP ASP A . n 
A 1 187 SER 187 628 628 SER SER A . n 
A 1 188 VAL 188 629 629 VAL VAL A . n 
A 1 189 LEU 189 630 630 LEU LEU A . n 
A 1 190 TYR 190 631 631 TYR TYR A . n 
A 1 191 ILE 191 632 632 ILE ILE A . n 
A 1 192 SER 192 633 633 SER SER A . n 
A 1 193 LEU 193 634 634 LEU LEU A . n 
A 1 194 HIS 194 635 635 HIS HIS A . n 
A 1 195 ARG 195 636 636 ARG ARG A . n 
A 1 196 TYR 196 637 637 TYR TYR A . n 
A 1 197 GLU 197 638 638 GLU GLU A . n 
A 1 198 ASP 198 639 639 ASP ASP A . n 
A 1 199 GLY 199 640 640 GLY GLY A . n 
A 1 200 ALA 200 641 641 ALA ALA A . n 
A 1 201 PHE 201 642 642 PHE PHE A . n 
A 1 202 PHE 202 643 643 PHE PHE A . n 
A 1 203 PRO 203 644 644 PRO PRO A . n 
A 1 204 ASN 204 645 645 ASN ASN A . n 
A 1 205 SER 205 646 646 SER SER A . n 
A 1 206 GLU 206 647 647 GLU GLU A . n 
A 1 207 ASP 207 648 648 ASP ASP A . n 
A 1 208 ALA 208 649 649 ALA ALA A . n 
A 1 209 ASN 209 650 650 ASN ASN A . n 
A 1 210 TYR 210 651 651 TYR TYR A . n 
A 1 211 ASP 211 652 652 ASP ASP A . n 
A 1 212 LYS 212 653 653 LYS LYS A . n 
A 1 213 VAL 213 654 654 VAL VAL A . n 
A 1 214 GLY 214 655 655 GLY GLY A . n 
A 1 215 LEU 215 656 656 LEU LEU A . n 
A 1 216 GLY 216 657 657 GLY GLY A . n 
A 1 217 LYS 217 658 658 LYS LYS A . n 
A 1 218 GLY 218 659 659 GLY GLY A . n 
A 1 219 ARG 219 660 660 ARG ARG A . n 
A 1 220 GLY 220 661 661 GLY GLY A . n 
A 1 221 TYR 221 662 662 TYR TYR A . n 
A 1 222 ASN 222 663 663 ASN ASN A . n 
A 1 223 VAL 223 664 664 VAL VAL A . n 
A 1 224 ASN 224 665 665 ASN ASN A . n 
A 1 225 ILE 225 666 666 ILE ILE A . n 
A 1 226 PRO 226 667 667 PRO PRO A . n 
A 1 227 TRP 227 668 668 TRP TRP A . n 
A 1 228 ASN 228 669 669 ASN ASN A . n 
A 1 229 GLY 229 670 670 GLY GLY A . n 
A 1 230 GLY 230 671 671 GLY GLY A . n 
A 1 231 LYS 231 672 672 LYS LYS A . n 
A 1 232 MET 232 673 673 MET MET A . n 
A 1 233 GLY 233 674 674 GLY GLY A . n 
A 1 234 ASP 234 675 675 ASP ASP A . n 
A 1 235 PRO 235 676 676 PRO PRO A . n 
A 1 236 GLU 236 677 677 GLU GLU A . n 
A 1 237 TYR 237 678 678 TYR TYR A . n 
A 1 238 MET 238 679 679 MET MET A . n 
A 1 239 ALA 239 680 680 ALA ALA A . n 
A 1 240 ALA 240 681 681 ALA ALA A . n 
A 1 241 PHE 241 682 682 PHE PHE A . n 
A 1 242 HIS 242 683 683 HIS HIS A . n 
A 1 243 HIS 243 684 684 HIS HIS A . n 
A 1 244 LEU 244 685 685 LEU LEU A . n 
A 1 245 VAL 245 686 686 VAL VAL A . n 
A 1 246 MET 246 687 687 MET MET A . n 
A 1 247 PRO 247 688 688 PRO PRO A . n 
A 1 248 ILE 248 689 689 ILE ILE A . n 
A 1 249 ALA 249 690 690 ALA ALA A . n 
A 1 250 ARG 250 691 691 ARG ARG A . n 
A 1 251 GLU 251 692 692 GLU GLU A . n 
A 1 252 PHE 252 693 693 PHE PHE A . n 
A 1 253 ALA 253 694 694 ALA ALA A . n 
A 1 254 PRO 254 695 695 PRO PRO A . n 
A 1 255 GLU 255 696 696 GLU GLU A . n 
A 1 256 LEU 256 697 697 LEU LEU A . n 
A 1 257 VAL 257 698 698 VAL VAL A . n 
A 1 258 LEU 258 699 699 LEU LEU A . n 
A 1 259 VAL 259 700 700 VAL VAL A . n 
A 1 260 SER 260 701 701 SER SER A . n 
A 1 261 ALA 261 702 702 ALA ALA A . n 
A 1 262 GLY 262 703 703 GLY GLY A . n 
A 1 263 PHE 263 704 704 PHE PHE A . n 
A 1 264 ASP 264 705 705 ASP ASP A . n 
A 1 265 ALA 265 706 706 ALA ALA A . n 
A 1 266 ALA 266 707 707 ALA ALA A . n 
A 1 267 ARG 267 708 708 ARG ARG A . n 
A 1 268 GLY 268 709 709 GLY GLY A . n 
A 1 269 ASP 269 710 710 ASP ASP A . n 
A 1 270 PRO 270 711 711 PRO PRO A . n 
A 1 271 LEU 271 712 712 LEU LEU A . n 
A 1 272 GLY 272 713 713 GLY GLY A . n 
A 1 273 GLY 273 714 714 GLY GLY A . n 
A 1 274 PHE 274 715 715 PHE PHE A . n 
A 1 275 GLN 275 716 716 GLN GLN A . n 
A 1 276 VAL 276 717 717 VAL VAL A . n 
A 1 277 THR 277 718 718 THR THR A . n 
A 1 278 PRO 278 719 719 PRO PRO A . n 
A 1 279 GLU 279 720 720 GLU GLU A . n 
A 1 280 GLY 280 721 721 GLY GLY A . n 
A 1 281 TYR 281 722 722 TYR TYR A . n 
A 1 282 ALA 282 723 723 ALA ALA A . n 
A 1 283 HIS 283 724 724 HIS HIS A . n 
A 1 284 LEU 284 725 725 LEU LEU A . n 
A 1 285 THR 285 726 726 THR THR A . n 
A 1 286 HIS 286 727 727 HIS HIS A . n 
A 1 287 GLN 287 728 728 GLN GLN A . n 
A 1 288 LEU 288 729 729 LEU LEU A . n 
A 1 289 MET 289 730 730 MET MET A . n 
A 1 290 SER 290 731 731 SER SER A . n 
A 1 291 LEU 291 732 732 LEU LEU A . n 
A 1 292 ALA 292 733 733 ALA ALA A . n 
A 1 293 ALA 293 734 734 ALA ALA A . n 
A 1 294 GLY 294 735 735 GLY GLY A . n 
A 1 295 ARG 295 736 736 ARG ARG A . n 
A 1 296 VAL 296 737 737 VAL VAL A . n 
A 1 297 LEU 297 738 738 LEU LEU A . n 
A 1 298 ILE 298 739 739 ILE ILE A . n 
A 1 299 ILE 299 740 740 ILE ILE A . n 
A 1 300 LEU 300 741 741 LEU LEU A . n 
A 1 301 GLU 301 742 742 GLU GLU A . n 
A 1 302 GLY 302 743 743 GLY GLY A . n 
A 1 303 GLY 303 744 744 GLY GLY A . n 
A 1 304 TYR 304 745 745 TYR TYR A . n 
A 1 305 ASN 305 746 746 ASN ASN A . n 
A 1 306 LEU 306 747 747 LEU LEU A . n 
A 1 307 THR 307 748 748 THR THR A . n 
A 1 308 SER 308 749 749 SER SER A . n 
A 1 309 ILE 309 750 750 ILE ILE A . n 
A 1 310 SER 310 751 751 SER SER A . n 
A 1 311 GLU 311 752 752 GLU GLU A . n 
A 1 312 SER 312 753 753 SER SER A . n 
A 1 313 MET 313 754 754 MET MET A . n 
A 1 314 SER 314 755 755 SER SER A . n 
A 1 315 MET 315 756 756 MET MET A . n 
A 1 316 CYS 316 757 757 CYS CYS A . n 
A 1 317 THR 317 758 758 THR THR A . n 
A 1 318 SER 318 759 759 SER SER A . n 
A 1 319 MET 319 760 760 MET MET A . n 
A 1 320 LEU 320 761 761 LEU LEU A . n 
A 1 321 LEU 321 762 762 LEU LEU A . n 
A 1 322 GLY 322 763 763 GLY GLY A . n 
A 1 323 ASP 323 764 764 ASP ASP A . n 
A 1 324 SER 324 765 765 SER SER A . n 
A 1 325 PRO 325 766 766 PRO PRO A . n 
A 1 326 PRO 326 767 767 PRO PRO A . n 
A 1 327 SER 327 768 768 SER SER A . n 
A 1 328 LEU 328 769 769 LEU LEU A . n 
A 1 329 ASP 329 770 ?   ?   ?   A . n 
A 1 330 HIS 330 771 ?   ?   ?   A . n 
A 1 331 LEU 331 772 ?   ?   ?   A . n 
A 1 332 THR 332 773 773 THR THR A . n 
A 1 333 PRO 333 774 774 PRO PRO A . n 
A 1 334 LEU 334 775 775 LEU LEU A . n 
A 1 335 LYS 335 776 776 LYS LYS A . n 
A 1 336 THR 336 777 777 THR THR A . n 
A 1 337 SER 337 778 778 SER SER A . n 
A 1 338 ALA 338 779 779 ALA ALA A . n 
A 1 339 THR 339 780 780 THR THR A . n 
A 1 340 VAL 340 781 781 VAL VAL A . n 
A 1 341 SER 341 782 782 SER SER A . n 
A 1 342 ILE 342 783 783 ILE ILE A . n 
A 1 343 ASN 343 784 784 ASN ASN A . n 
A 1 344 ASN 344 785 785 ASN ASN A . n 
A 1 345 VAL 345 786 786 VAL VAL A . n 
A 1 346 LEU 346 787 787 LEU LEU A . n 
A 1 347 ARG 347 788 788 ARG ARG A . n 
A 1 348 ALA 348 789 789 ALA ALA A . n 
A 1 349 HIS 349 790 790 HIS HIS A . n 
A 1 350 ALA 350 791 791 ALA ALA A . n 
A 1 351 PRO 351 792 792 PRO PRO A . n 
A 1 352 PHE 352 793 793 PHE PHE A . n 
A 1 353 TRP 353 794 794 TRP TRP A . n 
A 1 354 SER 354 795 795 SER SER A . n 
A 1 355 SER 355 796 796 SER SER A . n 
A 1 356 LEU 356 797 797 LEU LEU A . n 
A 1 357 ARG 357 798 798 ARG ARG A . n 
B 1 1   PRO 1   442 442 PRO PRO B . n 
B 1 2   ILE 2   443 443 ILE ILE B . n 
B 1 3   THR 3   444 444 THR THR B . n 
B 1 4   GLY 4   445 445 GLY GLY B . n 
B 1 5   LEU 5   446 446 LEU LEU B . n 
B 1 6   VAL 6   447 447 VAL VAL B . n 
B 1 7   TYR 7   448 448 TYR TYR B . n 
B 1 8   ASP 8   449 449 ASP ASP B . n 
B 1 9   GLN 9   450 450 GLN GLN B . n 
B 1 10  ARG 10  451 451 ARG ARG B . n 
B 1 11  MET 11  452 452 MET MET B . n 
B 1 12  MET 12  453 453 MET MET B . n 
B 1 13  LEU 13  454 454 LEU LEU B . n 
B 1 14  HIS 14  455 455 HIS HIS B . n 
B 1 15  HIS 15  456 456 HIS HIS B . n 
B 1 16  ASN 16  457 457 ASN ASN B . n 
B 1 17  MET 17  458 458 MET MET B . n 
B 1 18  TRP 18  459 459 TRP TRP B . n 
B 1 19  ASP 19  460 460 ASP ASP B . n 
B 1 20  SER 20  461 461 SER SER B . n 
B 1 21  HIS 21  462 462 HIS HIS B . n 
B 1 22  HIS 22  463 463 HIS HIS B . n 
B 1 23  PRO 23  464 464 PRO PRO B . n 
B 1 24  GLU 24  465 465 GLU GLU B . n 
B 1 25  LEU 25  466 466 LEU LEU B . n 
B 1 26  PRO 26  467 467 PRO PRO B . n 
B 1 27  GLN 27  468 468 GLN GLN B . n 
B 1 28  ARG 28  469 469 ARG ARG B . n 
B 1 29  ILE 29  470 470 ILE ILE B . n 
B 1 30  SER 30  471 471 SER SER B . n 
B 1 31  ARG 31  472 472 ARG ARG B . n 
B 1 32  ILE 32  473 473 ILE ILE B . n 
B 1 33  PHE 33  474 474 PHE PHE B . n 
B 1 34  SER 34  475 475 SER SER B . n 
B 1 35  ARG 35  476 476 ARG ARG B . n 
B 1 36  HIS 36  477 477 HIS HIS B . n 
B 1 37  GLU 37  478 478 GLU GLU B . n 
B 1 38  GLU 38  479 479 GLU GLU B . n 
B 1 39  LEU 39  480 480 LEU LEU B . n 
B 1 40  ARG 40  481 481 ARG ARG B . n 
B 1 41  LEU 41  482 482 LEU LEU B . n 
B 1 42  LEU 42  483 483 LEU LEU B . n 
B 1 43  SER 43  484 484 SER SER B . n 
B 1 44  ARG 44  485 485 ARG ARG B . n 
B 1 45  CYS 45  486 486 CYS CYS B . n 
B 1 46  HIS 46  487 487 HIS HIS B . n 
B 1 47  ARG 47  488 488 ARG ARG B . n 
B 1 48  ILE 48  489 489 ILE ILE B . n 
B 1 49  PRO 49  490 490 PRO PRO B . n 
B 1 50  ALA 50  491 491 ALA ALA B . n 
B 1 51  ARG 51  492 492 ARG ARG B . n 
B 1 52  LEU 52  493 493 LEU LEU B . n 
B 1 53  ALA 53  494 494 ALA ALA B . n 
B 1 54  THR 54  495 495 THR THR B . n 
B 1 55  GLU 55  496 496 GLU GLU B . n 
B 1 56  GLU 56  497 497 GLU GLU B . n 
B 1 57  GLU 57  498 498 GLU GLU B . n 
B 1 58  LEU 58  499 499 LEU LEU B . n 
B 1 59  ALA 59  500 500 ALA ALA B . n 
B 1 60  LEU 60  501 501 LEU LEU B . n 
B 1 61  CYS 61  502 502 CYS CYS B . n 
B 1 62  HIS 62  503 503 HIS HIS B . n 
B 1 63  SER 63  504 504 SER SER B . n 
B 1 64  SER 64  505 505 SER SER B . n 
B 1 65  LYS 65  506 506 LYS LYS B . n 
B 1 66  HIS 66  507 507 HIS HIS B . n 
B 1 67  ILE 67  508 508 ILE ILE B . n 
B 1 68  SER 68  509 509 SER SER B . n 
B 1 69  ILE 69  510 510 ILE ILE B . n 
B 1 70  ILE 70  511 511 ILE ILE B . n 
B 1 71  LYS 71  512 512 LYS LYS B . n 
B 1 72  SER 72  513 513 SER SER B . n 
B 1 73  SER 73  514 514 SER SER B . n 
B 1 74  GLU 74  515 515 GLU GLU B . n 
B 1 75  HIS 75  516 516 HIS HIS B . n 
B 1 76  MET 76  517 517 MET MET B . n 
B 1 77  LYS 77  518 518 LYS LYS B . n 
B 1 78  PRO 78  519 519 PRO PRO B . n 
B 1 79  ARG 79  520 520 ARG ARG B . n 
B 1 80  ASP 80  521 521 ASP ASP B . n 
B 1 81  LEU 81  522 522 LEU LEU B . n 
B 1 82  ASN 82  523 523 ASN ASN B . n 
B 1 83  ARG 83  524 524 ARG ARG B . n 
B 1 84  LEU 84  525 525 LEU LEU B . n 
B 1 85  GLY 85  526 526 GLY GLY B . n 
B 1 86  ASP 86  527 527 ASP ASP B . n 
B 1 87  GLU 87  528 528 GLU GLU B . n 
B 1 88  TYR 88  529 529 TYR TYR B . n 
B 1 89  ASN 89  530 530 ASN ASN B . n 
B 1 90  SER 90  531 531 SER SER B . n 
B 1 91  ILE 91  532 532 ILE ILE B . n 
B 1 92  PHE 92  533 533 PHE PHE B . n 
B 1 93  ILE 93  534 534 ILE ILE B . n 
B 1 94  SER 94  535 535 SER SER B . n 
B 1 95  ASN 95  536 536 ASN ASN B . n 
B 1 96  GLU 96  537 537 GLU GLU B . n 
B 1 97  SER 97  538 538 SER SER B . n 
B 1 98  TYR 98  539 539 TYR TYR B . n 
B 1 99  THR 99  540 540 THR THR B . n 
B 1 100 CYS 100 541 541 CYS CYS B . n 
B 1 101 ALA 101 542 542 ALA ALA B . n 
B 1 102 LEU 102 543 543 LEU LEU B . n 
B 1 103 LEU 103 544 544 LEU LEU B . n 
B 1 104 ALA 104 545 545 ALA ALA B . n 
B 1 105 ALA 105 546 546 ALA ALA B . n 
B 1 106 GLY 106 547 547 GLY GLY B . n 
B 1 107 SER 107 548 548 SER SER B . n 
B 1 108 CYS 108 549 549 CYS CYS B . n 
B 1 109 PHE 109 550 550 PHE PHE B . n 
B 1 110 ASN 110 551 551 ASN ASN B . n 
B 1 111 SER 111 552 552 SER SER B . n 
B 1 112 ALA 112 553 553 ALA ALA B . n 
B 1 113 GLN 113 554 554 GLN GLN B . n 
B 1 114 ALA 114 555 555 ALA ALA B . n 
B 1 115 ILE 115 556 556 ILE ILE B . n 
B 1 116 LEU 116 557 557 LEU LEU B . n 
B 1 117 THR 117 558 558 THR THR B . n 
B 1 118 GLY 118 559 559 GLY GLY B . n 
B 1 119 GLN 119 560 560 GLN GLN B . n 
B 1 120 VAL 120 561 561 VAL VAL B . n 
B 1 121 ARG 121 562 562 ARG ARG B . n 
B 1 122 ASN 122 563 563 ASN ASN B . n 
B 1 123 ALA 123 564 564 ALA ALA B . n 
B 1 124 VAL 124 565 565 VAL VAL B . n 
B 1 125 ALA 125 566 566 ALA ALA B . n 
B 1 126 ILE 126 567 567 ILE ILE B . n 
B 1 127 VAL 127 568 568 VAL VAL B . n 
B 1 128 ARG 128 569 569 ARG ARG B . n 
B 1 129 PRO 129 570 570 PRO PRO B . n 
B 1 130 PRO 130 571 571 PRO PRO B . n 
B 1 131 GLY 131 572 572 GLY GLY B . n 
B 1 132 HIS 132 573 573 HIS HIS B . n 
B 1 133 HIS 133 574 574 HIS HIS B . n 
B 1 134 ALA 134 575 575 ALA ALA B . n 
B 1 135 GLU 135 576 576 GLU GLU B . n 
B 1 136 LYS 136 577 577 LYS LYS B . n 
B 1 137 ASP 137 578 578 ASP ASP B . n 
B 1 138 THR 138 579 579 THR THR B . n 
B 1 139 ALA 139 580 580 ALA ALA B . n 
B 1 140 CYS 140 581 581 CYS CYS B . n 
B 1 141 GLY 141 582 582 GLY GLY B . n 
B 1 142 PHE 142 583 583 PHE PHE B . n 
B 1 143 CYS 143 584 584 CYS CYS B . n 
B 1 144 PHE 144 585 585 PHE PHE B . n 
B 1 145 PHE 145 586 586 PHE PHE B . n 
B 1 146 ASN 146 587 587 ASN ASN B . n 
B 1 147 THR 147 588 588 THR THR B . n 
B 1 148 ALA 148 589 589 ALA ALA B . n 
B 1 149 ALA 149 590 590 ALA ALA B . n 
B 1 150 LEU 150 591 591 LEU LEU B . n 
B 1 151 THR 151 592 592 THR THR B . n 
B 1 152 ALA 152 593 593 ALA ALA B . n 
B 1 153 ARG 153 594 594 ARG ARG B . n 
B 1 154 TYR 154 595 595 TYR TYR B . n 
B 1 155 ALA 155 596 596 ALA ALA B . n 
B 1 156 GLN 156 597 597 GLN GLN B . n 
B 1 157 SER 157 598 598 SER SER B . n 
B 1 158 ILE 158 599 599 ILE ILE B . n 
B 1 159 THR 159 600 600 THR THR B . n 
B 1 160 ARG 160 601 601 ARG ARG B . n 
B 1 161 GLU 161 602 602 GLU GLU B . n 
B 1 162 SER 162 603 603 SER SER B . n 
B 1 163 LEU 163 604 604 LEU LEU B . n 
B 1 164 ARG 164 605 605 ARG ARG B . n 
B 1 165 VAL 165 606 606 VAL VAL B . n 
B 1 166 LEU 166 607 607 LEU LEU B . n 
B 1 167 ILE 167 608 608 ILE ILE B . n 
B 1 168 VAL 168 609 609 VAL VAL B . n 
B 1 169 ASP 169 610 610 ASP ASP B . n 
B 1 170 TRP 170 611 611 TRP TRP B . n 
B 1 171 ASP 171 612 612 ASP ASP B . n 
B 1 172 VAL 172 613 613 VAL VAL B . n 
B 1 173 HIS 173 614 614 HIS HIS B . n 
B 1 174 HIS 174 615 615 HIS HIS B . n 
B 1 175 GLY 175 616 616 GLY GLY B . n 
B 1 176 ASN 176 617 617 ASN ASN B . n 
B 1 177 GLY 177 618 618 GLY GLY B . n 
B 1 178 THR 178 619 619 THR THR B . n 
B 1 179 GLN 179 620 620 GLN GLN B . n 
B 1 180 HIS 180 621 621 HIS HIS B . n 
B 1 181 ILE 181 622 622 ILE ILE B . n 
B 1 182 PHE 182 623 623 PHE PHE B . n 
B 1 183 GLU 183 624 624 GLU GLU B . n 
B 1 184 GLU 184 625 625 GLU GLU B . n 
B 1 185 ASP 185 626 626 ASP ASP B . n 
B 1 186 ASP 186 627 627 ASP ASP B . n 
B 1 187 SER 187 628 628 SER SER B . n 
B 1 188 VAL 188 629 629 VAL VAL B . n 
B 1 189 LEU 189 630 630 LEU LEU B . n 
B 1 190 TYR 190 631 631 TYR TYR B . n 
B 1 191 ILE 191 632 632 ILE ILE B . n 
B 1 192 SER 192 633 633 SER SER B . n 
B 1 193 LEU 193 634 634 LEU LEU B . n 
B 1 194 HIS 194 635 635 HIS HIS B . n 
B 1 195 ARG 195 636 636 ARG ARG B . n 
B 1 196 TYR 196 637 637 TYR TYR B . n 
B 1 197 GLU 197 638 638 GLU GLU B . n 
B 1 198 ASP 198 639 639 ASP ASP B . n 
B 1 199 GLY 199 640 640 GLY GLY B . n 
B 1 200 ALA 200 641 641 ALA ALA B . n 
B 1 201 PHE 201 642 642 PHE PHE B . n 
B 1 202 PHE 202 643 643 PHE PHE B . n 
B 1 203 PRO 203 644 644 PRO PRO B . n 
B 1 204 ASN 204 645 645 ASN ASN B . n 
B 1 205 SER 205 646 646 SER SER B . n 
B 1 206 GLU 206 647 647 GLU GLU B . n 
B 1 207 ASP 207 648 648 ASP ASP B . n 
B 1 208 ALA 208 649 649 ALA ALA B . n 
B 1 209 ASN 209 650 650 ASN ASN B . n 
B 1 210 TYR 210 651 651 TYR TYR B . n 
B 1 211 ASP 211 652 652 ASP ASP B . n 
B 1 212 LYS 212 653 653 LYS LYS B . n 
B 1 213 VAL 213 654 654 VAL VAL B . n 
B 1 214 GLY 214 655 655 GLY GLY B . n 
B 1 215 LEU 215 656 656 LEU LEU B . n 
B 1 216 GLY 216 657 657 GLY GLY B . n 
B 1 217 LYS 217 658 658 LYS LYS B . n 
B 1 218 GLY 218 659 659 GLY GLY B . n 
B 1 219 ARG 219 660 660 ARG ARG B . n 
B 1 220 GLY 220 661 661 GLY GLY B . n 
B 1 221 TYR 221 662 662 TYR TYR B . n 
B 1 222 ASN 222 663 663 ASN ASN B . n 
B 1 223 VAL 223 664 664 VAL VAL B . n 
B 1 224 ASN 224 665 665 ASN ASN B . n 
B 1 225 ILE 225 666 666 ILE ILE B . n 
B 1 226 PRO 226 667 667 PRO PRO B . n 
B 1 227 TRP 227 668 668 TRP TRP B . n 
B 1 228 ASN 228 669 669 ASN ASN B . n 
B 1 229 GLY 229 670 670 GLY GLY B . n 
B 1 230 GLY 230 671 671 GLY GLY B . n 
B 1 231 LYS 231 672 672 LYS LYS B . n 
B 1 232 MET 232 673 673 MET MET B . n 
B 1 233 GLY 233 674 674 GLY GLY B . n 
B 1 234 ASP 234 675 675 ASP ASP B . n 
B 1 235 PRO 235 676 676 PRO PRO B . n 
B 1 236 GLU 236 677 677 GLU GLU B . n 
B 1 237 TYR 237 678 678 TYR TYR B . n 
B 1 238 MET 238 679 679 MET MET B . n 
B 1 239 ALA 239 680 680 ALA ALA B . n 
B 1 240 ALA 240 681 681 ALA ALA B . n 
B 1 241 PHE 241 682 682 PHE PHE B . n 
B 1 242 HIS 242 683 683 HIS HIS B . n 
B 1 243 HIS 243 684 684 HIS HIS B . n 
B 1 244 LEU 244 685 685 LEU LEU B . n 
B 1 245 VAL 245 686 686 VAL VAL B . n 
B 1 246 MET 246 687 687 MET MET B . n 
B 1 247 PRO 247 688 688 PRO PRO B . n 
B 1 248 ILE 248 689 689 ILE ILE B . n 
B 1 249 ALA 249 690 690 ALA ALA B . n 
B 1 250 ARG 250 691 691 ARG ARG B . n 
B 1 251 GLU 251 692 692 GLU GLU B . n 
B 1 252 PHE 252 693 693 PHE PHE B . n 
B 1 253 ALA 253 694 694 ALA ALA B . n 
B 1 254 PRO 254 695 695 PRO PRO B . n 
B 1 255 GLU 255 696 696 GLU GLU B . n 
B 1 256 LEU 256 697 697 LEU LEU B . n 
B 1 257 VAL 257 698 698 VAL VAL B . n 
B 1 258 LEU 258 699 699 LEU LEU B . n 
B 1 259 VAL 259 700 700 VAL VAL B . n 
B 1 260 SER 260 701 701 SER SER B . n 
B 1 261 ALA 261 702 702 ALA ALA B . n 
B 1 262 GLY 262 703 703 GLY GLY B . n 
B 1 263 PHE 263 704 704 PHE PHE B . n 
B 1 264 ASP 264 705 705 ASP ASP B . n 
B 1 265 ALA 265 706 706 ALA ALA B . n 
B 1 266 ALA 266 707 707 ALA ALA B . n 
B 1 267 ARG 267 708 708 ARG ARG B . n 
B 1 268 GLY 268 709 709 GLY GLY B . n 
B 1 269 ASP 269 710 710 ASP ASP B . n 
B 1 270 PRO 270 711 711 PRO PRO B . n 
B 1 271 LEU 271 712 712 LEU LEU B . n 
B 1 272 GLY 272 713 713 GLY GLY B . n 
B 1 273 GLY 273 714 714 GLY GLY B . n 
B 1 274 PHE 274 715 715 PHE PHE B . n 
B 1 275 GLN 275 716 716 GLN GLN B . n 
B 1 276 VAL 276 717 717 VAL VAL B . n 
B 1 277 THR 277 718 718 THR THR B . n 
B 1 278 PRO 278 719 719 PRO PRO B . n 
B 1 279 GLU 279 720 720 GLU GLU B . n 
B 1 280 GLY 280 721 721 GLY GLY B . n 
B 1 281 TYR 281 722 722 TYR TYR B . n 
B 1 282 ALA 282 723 723 ALA ALA B . n 
B 1 283 HIS 283 724 724 HIS HIS B . n 
B 1 284 LEU 284 725 725 LEU LEU B . n 
B 1 285 THR 285 726 726 THR THR B . n 
B 1 286 HIS 286 727 727 HIS HIS B . n 
B 1 287 GLN 287 728 728 GLN GLN B . n 
B 1 288 LEU 288 729 729 LEU LEU B . n 
B 1 289 MET 289 730 730 MET MET B . n 
B 1 290 SER 290 731 731 SER SER B . n 
B 1 291 LEU 291 732 732 LEU LEU B . n 
B 1 292 ALA 292 733 733 ALA ALA B . n 
B 1 293 ALA 293 734 734 ALA ALA B . n 
B 1 294 GLY 294 735 735 GLY GLY B . n 
B 1 295 ARG 295 736 736 ARG ARG B . n 
B 1 296 VAL 296 737 737 VAL VAL B . n 
B 1 297 LEU 297 738 738 LEU LEU B . n 
B 1 298 ILE 298 739 739 ILE ILE B . n 
B 1 299 ILE 299 740 740 ILE ILE B . n 
B 1 300 LEU 300 741 741 LEU LEU B . n 
B 1 301 GLU 301 742 742 GLU GLU B . n 
B 1 302 GLY 302 743 743 GLY GLY B . n 
B 1 303 GLY 303 744 744 GLY GLY B . n 
B 1 304 TYR 304 745 745 TYR TYR B . n 
B 1 305 ASN 305 746 746 ASN ASN B . n 
B 1 306 LEU 306 747 747 LEU LEU B . n 
B 1 307 THR 307 748 748 THR THR B . n 
B 1 308 SER 308 749 749 SER SER B . n 
B 1 309 ILE 309 750 750 ILE ILE B . n 
B 1 310 SER 310 751 751 SER SER B . n 
B 1 311 GLU 311 752 752 GLU GLU B . n 
B 1 312 SER 312 753 753 SER SER B . n 
B 1 313 MET 313 754 754 MET MET B . n 
B 1 314 SER 314 755 755 SER SER B . n 
B 1 315 MET 315 756 756 MET MET B . n 
B 1 316 CYS 316 757 757 CYS CYS B . n 
B 1 317 THR 317 758 758 THR THR B . n 
B 1 318 SER 318 759 759 SER SER B . n 
B 1 319 MET 319 760 760 MET MET B . n 
B 1 320 LEU 320 761 761 LEU LEU B . n 
B 1 321 LEU 321 762 762 LEU LEU B . n 
B 1 322 GLY 322 763 763 GLY GLY B . n 
B 1 323 ASP 323 764 764 ASP ASP B . n 
B 1 324 SER 324 765 765 SER SER B . n 
B 1 325 PRO 325 766 766 PRO PRO B . n 
B 1 326 PRO 326 767 767 PRO PRO B . n 
B 1 327 SER 327 768 768 SER SER B . n 
B 1 328 LEU 328 769 769 LEU LEU B . n 
B 1 329 ASP 329 770 770 ASP ASP B . n 
B 1 330 HIS 330 771 771 HIS HIS B . n 
B 1 331 LEU 331 772 772 LEU LEU B . n 
B 1 332 THR 332 773 773 THR THR B . n 
B 1 333 PRO 333 774 774 PRO PRO B . n 
B 1 334 LEU 334 775 775 LEU LEU B . n 
B 1 335 LYS 335 776 776 LYS LYS B . n 
B 1 336 THR 336 777 777 THR THR B . n 
B 1 337 SER 337 778 778 SER SER B . n 
B 1 338 ALA 338 779 779 ALA ALA B . n 
B 1 339 THR 339 780 780 THR THR B . n 
B 1 340 VAL 340 781 781 VAL VAL B . n 
B 1 341 SER 341 782 782 SER SER B . n 
B 1 342 ILE 342 783 783 ILE ILE B . n 
B 1 343 ASN 343 784 784 ASN ASN B . n 
B 1 344 ASN 344 785 785 ASN ASN B . n 
B 1 345 VAL 345 786 786 VAL VAL B . n 
B 1 346 LEU 346 787 787 LEU LEU B . n 
B 1 347 ARG 347 788 788 ARG ARG B . n 
B 1 348 ALA 348 789 789 ALA ALA B . n 
B 1 349 HIS 349 790 790 HIS HIS B . n 
B 1 350 ALA 350 791 791 ALA ALA B . n 
B 1 351 PRO 351 792 792 PRO PRO B . n 
B 1 352 PHE 352 793 793 PHE PHE B . n 
B 1 353 TRP 353 794 794 TRP TRP B . n 
B 1 354 SER 354 795 795 SER SER B . n 
B 1 355 SER 355 796 796 SER SER B . n 
B 1 356 LEU 356 797 797 LEU LEU B . n 
B 1 357 ARG 357 798 798 ARG ARG B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BHX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BHX 
_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 A1BHX 1   801  1   A1BHX LIG A . 
D 3 ZN    1   802  2   ZN    ZN  A . 
E 4 K     1   803  2   K     K   A . 
F 4 K     1   804  6   K     K   A . 
G 2 A1BHX 1   801  2   A1BHX LIG B . 
H 3 ZN    1   802  1   ZN    ZN  B . 
I 4 K     1   803  1   K     K   B . 
J 4 K     1   804  3   K     K   B . 
K 4 K     1   805  4   K     K   B . 
L 5 HOH   1   901  807 HOH   HOH A . 
L 5 HOH   2   902  459 HOH   HOH A . 
L 5 HOH   3   903  286 HOH   HOH A . 
L 5 HOH   4   904  695 HOH   HOH A . 
L 5 HOH   5   905  763 HOH   HOH A . 
L 5 HOH   6   906  615 HOH   HOH A . 
L 5 HOH   7   907  333 HOH   HOH A . 
L 5 HOH   8   908  607 HOH   HOH A . 
L 5 HOH   9   909  514 HOH   HOH A . 
L 5 HOH   10  910  507 HOH   HOH A . 
L 5 HOH   11  911  860 HOH   HOH A . 
L 5 HOH   12  912  829 HOH   HOH A . 
L 5 HOH   13  913  597 HOH   HOH A . 
L 5 HOH   14  914  576 HOH   HOH A . 
L 5 HOH   15  915  111 HOH   HOH A . 
L 5 HOH   16  916  157 HOH   HOH A . 
L 5 HOH   17  917  163 HOH   HOH A . 
L 5 HOH   18  918  775 HOH   HOH A . 
L 5 HOH   19  919  268 HOH   HOH A . 
L 5 HOH   20  920  821 HOH   HOH A . 
L 5 HOH   21  921  177 HOH   HOH A . 
L 5 HOH   22  922  304 HOH   HOH A . 
L 5 HOH   23  923  735 HOH   HOH A . 
L 5 HOH   24  924  706 HOH   HOH A . 
L 5 HOH   25  925  377 HOH   HOH A . 
L 5 HOH   26  926  172 HOH   HOH A . 
L 5 HOH   27  927  707 HOH   HOH A . 
L 5 HOH   28  928  468 HOH   HOH A . 
L 5 HOH   29  929  309 HOH   HOH A . 
L 5 HOH   30  930  475 HOH   HOH A . 
L 5 HOH   31  931  569 HOH   HOH A . 
L 5 HOH   32  932  7   HOH   HOH A . 
L 5 HOH   33  933  190 HOH   HOH A . 
L 5 HOH   34  934  759 HOH   HOH A . 
L 5 HOH   35  935  247 HOH   HOH A . 
L 5 HOH   36  936  347 HOH   HOH A . 
L 5 HOH   37  937  384 HOH   HOH A . 
L 5 HOH   38  938  14  HOH   HOH A . 
L 5 HOH   39  939  444 HOH   HOH A . 
L 5 HOH   40  940  343 HOH   HOH A . 
L 5 HOH   41  941  19  HOH   HOH A . 
L 5 HOH   42  942  685 HOH   HOH A . 
L 5 HOH   43  943  536 HOH   HOH A . 
L 5 HOH   44  944  312 HOH   HOH A . 
L 5 HOH   45  945  269 HOH   HOH A . 
L 5 HOH   46  946  438 HOH   HOH A . 
L 5 HOH   47  947  676 HOH   HOH A . 
L 5 HOH   48  948  590 HOH   HOH A . 
L 5 HOH   49  949  117 HOH   HOH A . 
L 5 HOH   50  950  483 HOH   HOH A . 
L 5 HOH   51  951  712 HOH   HOH A . 
L 5 HOH   52  952  456 HOH   HOH A . 
L 5 HOH   53  953  518 HOH   HOH A . 
L 5 HOH   54  954  92  HOH   HOH A . 
L 5 HOH   55  955  496 HOH   HOH A . 
L 5 HOH   56  956  291 HOH   HOH A . 
L 5 HOH   57  957  680 HOH   HOH A . 
L 5 HOH   58  958  259 HOH   HOH A . 
L 5 HOH   59  959  135 HOH   HOH A . 
L 5 HOH   60  960  35  HOH   HOH A . 
L 5 HOH   61  961  137 HOH   HOH A . 
L 5 HOH   62  962  54  HOH   HOH A . 
L 5 HOH   63  963  455 HOH   HOH A . 
L 5 HOH   64  964  45  HOH   HOH A . 
L 5 HOH   65  965  60  HOH   HOH A . 
L 5 HOH   66  966  283 HOH   HOH A . 
L 5 HOH   67  967  692 HOH   HOH A . 
L 5 HOH   68  968  758 HOH   HOH A . 
L 5 HOH   69  969  17  HOH   HOH A . 
L 5 HOH   70  970  125 HOH   HOH A . 
L 5 HOH   71  971  10  HOH   HOH A . 
L 5 HOH   72  972  127 HOH   HOH A . 
L 5 HOH   73  973  522 HOH   HOH A . 
L 5 HOH   74  974  72  HOH   HOH A . 
L 5 HOH   75  975  61  HOH   HOH A . 
L 5 HOH   76  976  718 HOH   HOH A . 
L 5 HOH   77  977  410 HOH   HOH A . 
L 5 HOH   78  978  290 HOH   HOH A . 
L 5 HOH   79  979  11  HOH   HOH A . 
L 5 HOH   80  980  187 HOH   HOH A . 
L 5 HOH   81  981  136 HOH   HOH A . 
L 5 HOH   82  982  158 HOH   HOH A . 
L 5 HOH   83  983  282 HOH   HOH A . 
L 5 HOH   84  984  66  HOH   HOH A . 
L 5 HOH   85  985  774 HOH   HOH A . 
L 5 HOH   86  986  341 HOH   HOH A . 
L 5 HOH   87  987  836 HOH   HOH A . 
L 5 HOH   88  988  681 HOH   HOH A . 
L 5 HOH   89  989  65  HOH   HOH A . 
L 5 HOH   90  990  479 HOH   HOH A . 
L 5 HOH   91  991  667 HOH   HOH A . 
L 5 HOH   92  992  285 HOH   HOH A . 
L 5 HOH   93  993  64  HOH   HOH A . 
L 5 HOH   94  994  209 HOH   HOH A . 
L 5 HOH   95  995  27  HOH   HOH A . 
L 5 HOH   96  996  62  HOH   HOH A . 
L 5 HOH   97  997  178 HOH   HOH A . 
L 5 HOH   98  998  215 HOH   HOH A . 
L 5 HOH   99  999  79  HOH   HOH A . 
L 5 HOH   100 1000 184 HOH   HOH A . 
L 5 HOH   101 1001 206 HOH   HOH A . 
L 5 HOH   102 1002 287 HOH   HOH A . 
L 5 HOH   103 1003 328 HOH   HOH A . 
L 5 HOH   104 1004 168 HOH   HOH A . 
L 5 HOH   105 1005 389 HOH   HOH A . 
L 5 HOH   106 1006 478 HOH   HOH A . 
L 5 HOH   107 1007 105 HOH   HOH A . 
L 5 HOH   108 1008 211 HOH   HOH A . 
L 5 HOH   109 1009 48  HOH   HOH A . 
L 5 HOH   110 1010 114 HOH   HOH A . 
L 5 HOH   111 1011 691 HOH   HOH A . 
L 5 HOH   112 1012 335 HOH   HOH A . 
L 5 HOH   113 1013 679 HOH   HOH A . 
L 5 HOH   114 1014 371 HOH   HOH A . 
L 5 HOH   115 1015 71  HOH   HOH A . 
L 5 HOH   116 1016 464 HOH   HOH A . 
L 5 HOH   117 1017 598 HOH   HOH A . 
L 5 HOH   118 1018 106 HOH   HOH A . 
L 5 HOH   119 1019 254 HOH   HOH A . 
L 5 HOH   120 1020 688 HOH   HOH A . 
L 5 HOH   121 1021 115 HOH   HOH A . 
L 5 HOH   122 1022 318 HOH   HOH A . 
L 5 HOH   123 1023 354 HOH   HOH A . 
L 5 HOH   124 1024 3   HOH   HOH A . 
L 5 HOH   125 1025 450 HOH   HOH A . 
L 5 HOH   126 1026 25  HOH   HOH A . 
L 5 HOH   127 1027 376 HOH   HOH A . 
L 5 HOH   128 1028 8   HOH   HOH A . 
L 5 HOH   129 1029 232 HOH   HOH A . 
L 5 HOH   130 1030 281 HOH   HOH A . 
L 5 HOH   131 1031 266 HOH   HOH A . 
L 5 HOH   132 1032 710 HOH   HOH A . 
L 5 HOH   133 1033 570 HOH   HOH A . 
L 5 HOH   134 1034 601 HOH   HOH A . 
L 5 HOH   135 1035 602 HOH   HOH A . 
L 5 HOH   136 1036 762 HOH   HOH A . 
L 5 HOH   137 1037 50  HOH   HOH A . 
L 5 HOH   138 1038 725 HOH   HOH A . 
L 5 HOH   139 1039 144 HOH   HOH A . 
L 5 HOH   140 1040 161 HOH   HOH A . 
L 5 HOH   141 1041 199 HOH   HOH A . 
L 5 HOH   142 1042 449 HOH   HOH A . 
L 5 HOH   143 1043 129 HOH   HOH A . 
L 5 HOH   144 1044 299 HOH   HOH A . 
L 5 HOH   145 1045 51  HOH   HOH A . 
L 5 HOH   146 1046 34  HOH   HOH A . 
L 5 HOH   147 1047 511 HOH   HOH A . 
L 5 HOH   148 1048 160 HOH   HOH A . 
L 5 HOH   149 1049 658 HOH   HOH A . 
L 5 HOH   150 1050 23  HOH   HOH A . 
L 5 HOH   151 1051 471 HOH   HOH A . 
L 5 HOH   152 1052 356 HOH   HOH A . 
L 5 HOH   153 1053 124 HOH   HOH A . 
L 5 HOH   154 1054 166 HOH   HOH A . 
L 5 HOH   155 1055 164 HOH   HOH A . 
L 5 HOH   156 1056 556 HOH   HOH A . 
L 5 HOH   157 1057 191 HOH   HOH A . 
L 5 HOH   158 1058 213 HOH   HOH A . 
L 5 HOH   159 1059 227 HOH   HOH A . 
L 5 HOH   160 1060 24  HOH   HOH A . 
L 5 HOH   161 1061 280 HOH   HOH A . 
L 5 HOH   162 1062 82  HOH   HOH A . 
L 5 HOH   163 1063 2   HOH   HOH A . 
L 5 HOH   164 1064 626 HOH   HOH A . 
L 5 HOH   165 1065 745 HOH   HOH A . 
L 5 HOH   166 1066 39  HOH   HOH A . 
L 5 HOH   167 1067 495 HOH   HOH A . 
L 5 HOH   168 1068 119 HOH   HOH A . 
L 5 HOH   169 1069 63  HOH   HOH A . 
L 5 HOH   170 1070 746 HOH   HOH A . 
L 5 HOH   171 1071 497 HOH   HOH A . 
L 5 HOH   172 1072 240 HOH   HOH A . 
L 5 HOH   173 1073 56  HOH   HOH A . 
L 5 HOH   174 1074 321 HOH   HOH A . 
L 5 HOH   175 1075 589 HOH   HOH A . 
L 5 HOH   176 1076 403 HOH   HOH A . 
L 5 HOH   177 1077 67  HOH   HOH A . 
L 5 HOH   178 1078 204 HOH   HOH A . 
L 5 HOH   179 1079 176 HOH   HOH A . 
L 5 HOH   180 1080 95  HOH   HOH A . 
L 5 HOH   181 1081 297 HOH   HOH A . 
L 5 HOH   182 1082 588 HOH   HOH A . 
L 5 HOH   183 1083 270 HOH   HOH A . 
L 5 HOH   184 1084 96  HOH   HOH A . 
L 5 HOH   185 1085 454 HOH   HOH A . 
L 5 HOH   186 1086 57  HOH   HOH A . 
L 5 HOH   187 1087 843 HOH   HOH A . 
L 5 HOH   188 1088 292 HOH   HOH A . 
L 5 HOH   189 1089 545 HOH   HOH A . 
L 5 HOH   190 1090 302 HOH   HOH A . 
L 5 HOH   191 1091 413 HOH   HOH A . 
L 5 HOH   192 1092 764 HOH   HOH A . 
L 5 HOH   193 1093 682 HOH   HOH A . 
L 5 HOH   194 1094 16  HOH   HOH A . 
L 5 HOH   195 1095 719 HOH   HOH A . 
L 5 HOH   196 1096 155 HOH   HOH A . 
L 5 HOH   197 1097 428 HOH   HOH A . 
L 5 HOH   198 1098 156 HOH   HOH A . 
L 5 HOH   199 1099 303 HOH   HOH A . 
L 5 HOH   200 1100 147 HOH   HOH A . 
L 5 HOH   201 1101 49  HOH   HOH A . 
L 5 HOH   202 1102 130 HOH   HOH A . 
L 5 HOH   203 1103 419 HOH   HOH A . 
L 5 HOH   204 1104 118 HOH   HOH A . 
L 5 HOH   205 1105 714 HOH   HOH A . 
L 5 HOH   206 1106 151 HOH   HOH A . 
L 5 HOH   207 1107 360 HOH   HOH A . 
L 5 HOH   208 1108 108 HOH   HOH A . 
L 5 HOH   209 1109 345 HOH   HOH A . 
L 5 HOH   210 1110 225 HOH   HOH A . 
L 5 HOH   211 1111 476 HOH   HOH A . 
L 5 HOH   212 1112 43  HOH   HOH A . 
L 5 HOH   213 1113 98  HOH   HOH A . 
L 5 HOH   214 1114 316 HOH   HOH A . 
L 5 HOH   215 1115 402 HOH   HOH A . 
L 5 HOH   216 1116 275 HOH   HOH A . 
L 5 HOH   217 1117 640 HOH   HOH A . 
L 5 HOH   218 1118 499 HOH   HOH A . 
L 5 HOH   219 1119 579 HOH   HOH A . 
L 5 HOH   220 1120 81  HOH   HOH A . 
L 5 HOH   221 1121 188 HOH   HOH A . 
L 5 HOH   222 1122 195 HOH   HOH A . 
L 5 HOH   223 1123 558 HOH   HOH A . 
L 5 HOH   224 1124 782 HOH   HOH A . 
L 5 HOH   225 1125 404 HOH   HOH A . 
L 5 HOH   226 1126 331 HOH   HOH A . 
L 5 HOH   227 1127 801 HOH   HOH A . 
L 5 HOH   228 1128 70  HOH   HOH A . 
L 5 HOH   229 1129 207 HOH   HOH A . 
L 5 HOH   230 1130 104 HOH   HOH A . 
L 5 HOH   231 1131 84  HOH   HOH A . 
L 5 HOH   232 1132 250 HOH   HOH A . 
L 5 HOH   233 1133 440 HOH   HOH A . 
L 5 HOH   234 1134 772 HOH   HOH A . 
L 5 HOH   235 1135 278 HOH   HOH A . 
L 5 HOH   236 1136 234 HOH   HOH A . 
L 5 HOH   237 1137 484 HOH   HOH A . 
L 5 HOH   238 1138 41  HOH   HOH A . 
L 5 HOH   239 1139 816 HOH   HOH A . 
L 5 HOH   240 1140 110 HOH   HOH A . 
L 5 HOH   241 1141 634 HOH   HOH A . 
L 5 HOH   242 1142 339 HOH   HOH A . 
L 5 HOH   243 1143 740 HOH   HOH A . 
L 5 HOH   244 1144 337 HOH   HOH A . 
L 5 HOH   245 1145 173 HOH   HOH A . 
L 5 HOH   246 1146 244 HOH   HOH A . 
L 5 HOH   247 1147 826 HOH   HOH A . 
L 5 HOH   248 1148 488 HOH   HOH A . 
L 5 HOH   249 1149 185 HOH   HOH A . 
L 5 HOH   250 1150 189 HOH   HOH A . 
L 5 HOH   251 1151 840 HOH   HOH A . 
L 5 HOH   252 1152 756 HOH   HOH A . 
L 5 HOH   253 1153 308 HOH   HOH A . 
L 5 HOH   254 1154 89  HOH   HOH A . 
L 5 HOH   255 1155 179 HOH   HOH A . 
L 5 HOH   256 1156 122 HOH   HOH A . 
L 5 HOH   257 1157 353 HOH   HOH A . 
L 5 HOH   258 1158 480 HOH   HOH A . 
L 5 HOH   259 1159 183 HOH   HOH A . 
L 5 HOH   260 1160 839 HOH   HOH A . 
L 5 HOH   261 1161 623 HOH   HOH A . 
L 5 HOH   262 1162 47  HOH   HOH A . 
L 5 HOH   263 1163 703 HOH   HOH A . 
L 5 HOH   264 1164 100 HOH   HOH A . 
L 5 HOH   265 1165 284 HOH   HOH A . 
L 5 HOH   266 1166 572 HOH   HOH A . 
L 5 HOH   267 1167 506 HOH   HOH A . 
L 5 HOH   268 1168 350 HOH   HOH A . 
L 5 HOH   269 1169 202 HOH   HOH A . 
L 5 HOH   270 1170 409 HOH   HOH A . 
L 5 HOH   271 1171 741 HOH   HOH A . 
L 5 HOH   272 1172 429 HOH   HOH A . 
L 5 HOH   273 1173 777 HOH   HOH A . 
L 5 HOH   274 1174 642 HOH   HOH A . 
L 5 HOH   275 1175 289 HOH   HOH A . 
L 5 HOH   276 1176 687 HOH   HOH A . 
L 5 HOH   277 1177 392 HOH   HOH A . 
L 5 HOH   278 1178 633 HOH   HOH A . 
L 5 HOH   279 1179 537 HOH   HOH A . 
L 5 HOH   280 1180 591 HOH   HOH A . 
L 5 HOH   281 1181 523 HOH   HOH A . 
L 5 HOH   282 1182 770 HOH   HOH A . 
L 5 HOH   283 1183 492 HOH   HOH A . 
L 5 HOH   284 1184 533 HOH   HOH A . 
L 5 HOH   285 1185 433 HOH   HOH A . 
L 5 HOH   286 1186 592 HOH   HOH A . 
L 5 HOH   287 1187 415 HOH   HOH A . 
L 5 HOH   288 1188 849 HOH   HOH A . 
L 5 HOH   289 1189 749 HOH   HOH A . 
L 5 HOH   290 1190 723 HOH   HOH A . 
L 5 HOH   291 1191 298 HOH   HOH A . 
L 5 HOH   292 1192 461 HOH   HOH A . 
L 5 HOH   293 1193 547 HOH   HOH A . 
L 5 HOH   294 1194 837 HOH   HOH A . 
L 5 HOH   295 1195 336 HOH   HOH A . 
L 5 HOH   296 1196 344 HOH   HOH A . 
L 5 HOH   297 1197 726 HOH   HOH A . 
L 5 HOH   298 1198 494 HOH   HOH A . 
L 5 HOH   299 1199 534 HOH   HOH A . 
L 5 HOH   300 1200 201 HOH   HOH A . 
L 5 HOH   301 1201 405 HOH   HOH A . 
L 5 HOH   302 1202 841 HOH   HOH A . 
L 5 HOH   303 1203 603 HOH   HOH A . 
L 5 HOH   304 1204 387 HOH   HOH A . 
L 5 HOH   305 1205 609 HOH   HOH A . 
L 5 HOH   306 1206 877 HOH   HOH A . 
L 5 HOH   307 1207 90  HOH   HOH A . 
L 5 HOH   308 1208 565 HOH   HOH A . 
L 5 HOH   309 1209 220 HOH   HOH A . 
L 5 HOH   310 1210 586 HOH   HOH A . 
L 5 HOH   311 1211 457 HOH   HOH A . 
L 5 HOH   312 1212 627 HOH   HOH A . 
L 5 HOH   313 1213 734 HOH   HOH A . 
L 5 HOH   314 1214 713 HOH   HOH A . 
L 5 HOH   315 1215 883 HOH   HOH A . 
L 5 HOH   316 1216 133 HOH   HOH A . 
L 5 HOH   317 1217 857 HOH   HOH A . 
L 5 HOH   318 1218 727 HOH   HOH A . 
L 5 HOH   319 1219 854 HOH   HOH A . 
L 5 HOH   320 1220 728 HOH   HOH A . 
L 5 HOH   321 1221 368 HOH   HOH A . 
L 5 HOH   322 1222 624 HOH   HOH A . 
L 5 HOH   323 1223 761 HOH   HOH A . 
L 5 HOH   324 1224 783 HOH   HOH A . 
L 5 HOH   325 1225 401 HOH   HOH A . 
L 5 HOH   326 1226 482 HOH   HOH A . 
L 5 HOH   327 1227 896 HOH   HOH A . 
L 5 HOH   328 1228 509 HOH   HOH A . 
L 5 HOH   329 1229 319 HOH   HOH A . 
L 5 HOH   330 1230 649 HOH   HOH A . 
L 5 HOH   331 1231 630 HOH   HOH A . 
L 5 HOH   332 1232 351 HOH   HOH A . 
L 5 HOH   333 1233 794 HOH   HOH A . 
L 5 HOH   334 1234 856 HOH   HOH A . 
L 5 HOH   335 1235 831 HOH   HOH A . 
L 5 HOH   336 1236 458 HOH   HOH A . 
L 5 HOH   337 1237 720 HOH   HOH A . 
L 5 HOH   338 1238 226 HOH   HOH A . 
L 5 HOH   339 1239 504 HOH   HOH A . 
L 5 HOH   340 1240 635 HOH   HOH A . 
L 5 HOH   341 1241 898 HOH   HOH A . 
L 5 HOH   342 1242 175 HOH   HOH A . 
L 5 HOH   343 1243 561 HOH   HOH A . 
L 5 HOH   344 1244 357 HOH   HOH A . 
L 5 HOH   345 1245 697 HOH   HOH A . 
L 5 HOH   346 1246 863 HOH   HOH A . 
L 5 HOH   347 1247 421 HOH   HOH A . 
L 5 HOH   348 1248 757 HOH   HOH A . 
L 5 HOH   349 1249 622 HOH   HOH A . 
L 5 HOH   350 1250 870 HOH   HOH A . 
L 5 HOH   351 1251 559 HOH   HOH A . 
L 5 HOH   352 1252 686 HOH   HOH A . 
L 5 HOH   353 1253 888 HOH   HOH A . 
L 5 HOH   354 1254 192 HOH   HOH A . 
L 5 HOH   355 1255 584 HOH   HOH A . 
L 5 HOH   356 1256 424 HOH   HOH A . 
L 5 HOH   357 1257 466 HOH   HOH A . 
L 5 HOH   358 1258 671 HOH   HOH A . 
L 5 HOH   359 1259 141 HOH   HOH A . 
L 5 HOH   360 1260 485 HOH   HOH A . 
L 5 HOH   361 1261 453 HOH   HOH A . 
L 5 HOH   362 1262 795 HOH   HOH A . 
L 5 HOH   363 1263 430 HOH   HOH A . 
L 5 HOH   364 1264 397 HOH   HOH A . 
L 5 HOH   365 1265 621 HOH   HOH A . 
L 5 HOH   366 1266 342 HOH   HOH A . 
L 5 HOH   367 1267 395 HOH   HOH A . 
L 5 HOH   368 1268 314 HOH   HOH A . 
L 5 HOH   369 1269 778 HOH   HOH A . 
L 5 HOH   370 1270 293 HOH   HOH A . 
L 5 HOH   371 1271 862 HOH   HOH A . 
L 5 HOH   372 1272 322 HOH   HOH A . 
L 5 HOH   373 1273 542 HOH   HOH A . 
L 5 HOH   374 1274 469 HOH   HOH A . 
L 5 HOH   375 1275 340 HOH   HOH A . 
L 5 HOH   376 1276 205 HOH   HOH A . 
L 5 HOH   377 1277 612 HOH   HOH A . 
L 5 HOH   378 1278 673 HOH   HOH A . 
L 5 HOH   379 1279 832 HOH   HOH A . 
L 5 HOH   380 1280 845 HOH   HOH A . 
L 5 HOH   381 1281 645 HOH   HOH A . 
L 5 HOH   382 1282 787 HOH   HOH A . 
L 5 HOH   383 1283 851 HOH   HOH A . 
L 5 HOH   384 1284 895 HOH   HOH A . 
L 5 HOH   385 1285 334 HOH   HOH A . 
L 5 HOH   386 1286 886 HOH   HOH A . 
L 5 HOH   387 1287 169 HOH   HOH A . 
L 5 HOH   388 1288 182 HOH   HOH A . 
L 5 HOH   389 1289 604 HOH   HOH A . 
L 5 HOH   390 1290 721 HOH   HOH A . 
L 5 HOH   391 1291 581 HOH   HOH A . 
L 5 HOH   392 1292 414 HOH   HOH A . 
L 5 HOH   393 1293 897 HOH   HOH A . 
M 5 HOH   1   901  835 HOH   HOH B . 
M 5 HOH   2   902  850 HOH   HOH B . 
M 5 HOH   3   903  800 HOH   HOH B . 
M 5 HOH   4   904  820 HOH   HOH B . 
M 5 HOH   5   905  699 HOH   HOH B . 
M 5 HOH   6   906  332 HOH   HOH B . 
M 5 HOH   7   907  380 HOH   HOH B . 
M 5 HOH   8   908  452 HOH   HOH B . 
M 5 HOH   9   909  406 HOH   HOH B . 
M 5 HOH   10  910  431 HOH   HOH B . 
M 5 HOH   11  911  577 HOH   HOH B . 
M 5 HOH   12  912  400 HOH   HOH B . 
M 5 HOH   13  913  436 HOH   HOH B . 
M 5 HOH   14  914  724 HOH   HOH B . 
M 5 HOH   15  915  580 HOH   HOH B . 
M 5 HOH   16  916  631 HOH   HOH B . 
M 5 HOH   17  917  196 HOH   HOH B . 
M 5 HOH   18  918  784 HOH   HOH B . 
M 5 HOH   19  919  362 HOH   HOH B . 
M 5 HOH   20  920  711 HOH   HOH B . 
M 5 HOH   21  921  465 HOH   HOH B . 
M 5 HOH   22  922  422 HOH   HOH B . 
M 5 HOH   23  923  145 HOH   HOH B . 
M 5 HOH   24  924  830 HOH   HOH B . 
M 5 HOH   25  925  730 HOH   HOH B . 
M 5 HOH   26  926  647 HOH   HOH B . 
M 5 HOH   27  927  535 HOH   HOH B . 
M 5 HOH   28  928  30  HOH   HOH B . 
M 5 HOH   29  929  4   HOH   HOH B . 
M 5 HOH   30  930  524 HOH   HOH B . 
M 5 HOH   31  931  393 HOH   HOH B . 
M 5 HOH   32  932  477 HOH   HOH B . 
M 5 HOH   33  933  515 HOH   HOH B . 
M 5 HOH   34  934  148 HOH   HOH B . 
M 5 HOH   35  935  434 HOH   HOH B . 
M 5 HOH   36  936  731 HOH   HOH B . 
M 5 HOH   37  937  443 HOH   HOH B . 
M 5 HOH   38  938  472 HOH   HOH B . 
M 5 HOH   39  939  256 HOH   HOH B . 
M 5 HOH   40  940  87  HOH   HOH B . 
M 5 HOH   41  941  568 HOH   HOH B . 
M 5 HOH   42  942  171 HOH   HOH B . 
M 5 HOH   43  943  348 HOH   HOH B . 
M 5 HOH   44  944  272 HOH   HOH B . 
M 5 HOH   45  945  99  HOH   HOH B . 
M 5 HOH   46  946  861 HOH   HOH B . 
M 5 HOH   47  947  678 HOH   HOH B . 
M 5 HOH   48  948  693 HOH   HOH B . 
M 5 HOH   49  949  154 HOH   HOH B . 
M 5 HOH   50  950  78  HOH   HOH B . 
M 5 HOH   51  951  313 HOH   HOH B . 
M 5 HOH   52  952  208 HOH   HOH B . 
M 5 HOH   53  953  197 HOH   HOH B . 
M 5 HOH   54  954  221 HOH   HOH B . 
M 5 HOH   55  955  40  HOH   HOH B . 
M 5 HOH   56  956  359 HOH   HOH B . 
M 5 HOH   57  957  541 HOH   HOH B . 
M 5 HOH   58  958  91  HOH   HOH B . 
M 5 HOH   59  959  140 HOH   HOH B . 
M 5 HOH   60  960  785 HOH   HOH B . 
M 5 HOH   61  961  181 HOH   HOH B . 
M 5 HOH   62  962  446 HOH   HOH B . 
M 5 HOH   63  963  139 HOH   HOH B . 
M 5 HOH   64  964  844 HOH   HOH B . 
M 5 HOH   65  965  848 HOH   HOH B . 
M 5 HOH   66  966  198 HOH   HOH B . 
M 5 HOH   67  967  264 HOH   HOH B . 
M 5 HOH   68  968  174 HOH   HOH B . 
M 5 HOH   69  969  68  HOH   HOH B . 
M 5 HOH   70  970  58  HOH   HOH B . 
M 5 HOH   71  971  501 HOH   HOH B . 
M 5 HOH   72  972  538 HOH   HOH B . 
M 5 HOH   73  973  750 HOH   HOH B . 
M 5 HOH   74  974  258 HOH   HOH B . 
M 5 HOH   75  975  165 HOH   HOH B . 
M 5 HOH   76  976  412 HOH   HOH B . 
M 5 HOH   77  977  779 HOH   HOH B . 
M 5 HOH   78  978  295 HOH   HOH B . 
M 5 HOH   79  979  599 HOH   HOH B . 
M 5 HOH   80  980  218 HOH   HOH B . 
M 5 HOH   81  981  1   HOH   HOH B . 
M 5 HOH   82  982  20  HOH   HOH B . 
M 5 HOH   83  983  267 HOH   HOH B . 
M 5 HOH   84  984  46  HOH   HOH B . 
M 5 HOH   85  985  6   HOH   HOH B . 
M 5 HOH   86  986  13  HOH   HOH B . 
M 5 HOH   87  987  53  HOH   HOH B . 
M 5 HOH   88  988  26  HOH   HOH B . 
M 5 HOH   89  989  241 HOH   HOH B . 
M 5 HOH   90  990  193 HOH   HOH B . 
M 5 HOH   91  991  200 HOH   HOH B . 
M 5 HOH   92  992  463 HOH   HOH B . 
M 5 HOH   93  993  194 HOH   HOH B . 
M 5 HOH   94  994  372 HOH   HOH B . 
M 5 HOH   95  995  230 HOH   HOH B . 
M 5 HOH   96  996  28  HOH   HOH B . 
M 5 HOH   97  997  614 HOH   HOH B . 
M 5 HOH   98  998  22  HOH   HOH B . 
M 5 HOH   99  999  153 HOH   HOH B . 
M 5 HOH   100 1000 33  HOH   HOH B . 
M 5 HOH   101 1001 5   HOH   HOH B . 
M 5 HOH   102 1002 52  HOH   HOH B . 
M 5 HOH   103 1003 875 HOH   HOH B . 
M 5 HOH   104 1004 815 HOH   HOH B . 
M 5 HOH   105 1005 255 HOH   HOH B . 
M 5 HOH   106 1006 222 HOH   HOH B . 
M 5 HOH   107 1007 42  HOH   HOH B . 
M 5 HOH   108 1008 32  HOH   HOH B . 
M 5 HOH   109 1009 93  HOH   HOH B . 
M 5 HOH   110 1010 246 HOH   HOH B . 
M 5 HOH   111 1011 271 HOH   HOH B . 
M 5 HOH   112 1012 760 HOH   HOH B . 
M 5 HOH   113 1013 134 HOH   HOH B . 
M 5 HOH   114 1014 15  HOH   HOH B . 
M 5 HOH   115 1015 126 HOH   HOH B . 
M 5 HOH   116 1016 663 HOH   HOH B . 
M 5 HOH   117 1017 388 HOH   HOH B . 
M 5 HOH   118 1018 18  HOH   HOH B . 
M 5 HOH   119 1019 441 HOH   HOH B . 
M 5 HOH   120 1020 38  HOH   HOH B . 
M 5 HOH   121 1021 74  HOH   HOH B . 
M 5 HOH   122 1022 365 HOH   HOH B . 
M 5 HOH   123 1023 86  HOH   HOH B . 
M 5 HOH   124 1024 236 HOH   HOH B . 
M 5 HOH   125 1025 123 HOH   HOH B . 
M 5 HOH   126 1026 77  HOH   HOH B . 
M 5 HOH   127 1027 382 HOH   HOH B . 
M 5 HOH   128 1028 257 HOH   HOH B . 
M 5 HOH   129 1029 120 HOH   HOH B . 
M 5 HOH   130 1030 398 HOH   HOH B . 
M 5 HOH   131 1031 212 HOH   HOH B . 
M 5 HOH   132 1032 481 HOH   HOH B . 
M 5 HOH   133 1033 529 HOH   HOH B . 
M 5 HOH   134 1034 742 HOH   HOH B . 
M 5 HOH   135 1035 12  HOH   HOH B . 
M 5 HOH   136 1036 338 HOH   HOH B . 
M 5 HOH   137 1037 510 HOH   HOH B . 
M 5 HOH   138 1038 142 HOH   HOH B . 
M 5 HOH   139 1039 214 HOH   HOH B . 
M 5 HOH   140 1040 765 HOH   HOH B . 
M 5 HOH   141 1041 219 HOH   HOH B . 
M 5 HOH   142 1042 498 HOH   HOH B . 
M 5 HOH   143 1043 242 HOH   HOH B . 
M 5 HOH   144 1044 674 HOH   HOH B . 
M 5 HOH   145 1045 83  HOH   HOH B . 
M 5 HOH   146 1046 85  HOH   HOH B . 
M 5 HOH   147 1047 21  HOH   HOH B . 
M 5 HOH   148 1048 276 HOH   HOH B . 
M 5 HOH   149 1049 128 HOH   HOH B . 
M 5 HOH   150 1050 390 HOH   HOH B . 
M 5 HOH   151 1051 263 HOH   HOH B . 
M 5 HOH   152 1052 94  HOH   HOH B . 
M 5 HOH   153 1053 300 HOH   HOH B . 
M 5 HOH   154 1054 307 HOH   HOH B . 
M 5 HOH   155 1055 167 HOH   HOH B . 
M 5 HOH   156 1056 228 HOH   HOH B . 
M 5 HOH   157 1057 75  HOH   HOH B . 
M 5 HOH   158 1058 323 HOH   HOH B . 
M 5 HOH   159 1059 650 HOH   HOH B . 
M 5 HOH   160 1060 811 HOH   HOH B . 
M 5 HOH   161 1061 296 HOH   HOH B . 
M 5 HOH   162 1062 107 HOH   HOH B . 
M 5 HOH   163 1063 743 HOH   HOH B . 
M 5 HOH   164 1064 451 HOH   HOH B . 
M 5 HOH   165 1065 722 HOH   HOH B . 
M 5 HOH   166 1066 112 HOH   HOH B . 
M 5 HOH   167 1067 9   HOH   HOH B . 
M 5 HOH   168 1068 620 HOH   HOH B . 
M 5 HOH   169 1069 689 HOH   HOH B . 
M 5 HOH   170 1070 44  HOH   HOH B . 
M 5 HOH   171 1071 131 HOH   HOH B . 
M 5 HOH   172 1072 55  HOH   HOH B . 
M 5 HOH   173 1073 520 HOH   HOH B . 
M 5 HOH   174 1074 361 HOH   HOH B . 
M 5 HOH   175 1075 878 HOH   HOH B . 
M 5 HOH   176 1076 306 HOH   HOH B . 
M 5 HOH   177 1077 69  HOH   HOH B . 
M 5 HOH   178 1078 274 HOH   HOH B . 
M 5 HOH   179 1079 396 HOH   HOH B . 
M 5 HOH   180 1080 31  HOH   HOH B . 
M 5 HOH   181 1081 88  HOH   HOH B . 
M 5 HOH   182 1082 654 HOH   HOH B . 
M 5 HOH   183 1083 551 HOH   HOH B . 
M 5 HOH   184 1084 97  HOH   HOH B . 
M 5 HOH   185 1085 102 HOH   HOH B . 
M 5 HOH   186 1086 817 HOH   HOH B . 
M 5 HOH   187 1087 567 HOH   HOH B . 
M 5 HOH   188 1088 329 HOH   HOH B . 
M 5 HOH   189 1089 59  HOH   HOH B . 
M 5 HOH   190 1090 37  HOH   HOH B . 
M 5 HOH   191 1091 661 HOH   HOH B . 
M 5 HOH   192 1092 216 HOH   HOH B . 
M 5 HOH   193 1093 869 HOH   HOH B . 
M 5 HOH   194 1094 381 HOH   HOH B . 
M 5 HOH   195 1095 310 HOH   HOH B . 
M 5 HOH   196 1096 239 HOH   HOH B . 
M 5 HOH   197 1097 548 HOH   HOH B . 
M 5 HOH   198 1098 573 HOH   HOH B . 
M 5 HOH   199 1099 814 HOH   HOH B . 
M 5 HOH   200 1100 715 HOH   HOH B . 
M 5 HOH   201 1101 36  HOH   HOH B . 
M 5 HOH   202 1102 613 HOH   HOH B . 
M 5 HOH   203 1103 224 HOH   HOH B . 
M 5 HOH   204 1104 416 HOH   HOH B . 
M 5 HOH   205 1105 80  HOH   HOH B . 
M 5 HOH   206 1106 349 HOH   HOH B . 
M 5 HOH   207 1107 369 HOH   HOH B . 
M 5 HOH   208 1108 235 HOH   HOH B . 
M 5 HOH   209 1109 399 HOH   HOH B . 
M 5 HOH   210 1110 245 HOH   HOH B . 
M 5 HOH   211 1111 729 HOH   HOH B . 
M 5 HOH   212 1112 702 HOH   HOH B . 
M 5 HOH   213 1113 355 HOH   HOH B . 
M 5 HOH   214 1114 217 HOH   HOH B . 
M 5 HOH   215 1115 852 HOH   HOH B . 
M 5 HOH   216 1116 73  HOH   HOH B . 
M 5 HOH   217 1117 320 HOH   HOH B . 
M 5 HOH   218 1118 248 HOH   HOH B . 
M 5 HOH   219 1119 460 HOH   HOH B . 
M 5 HOH   220 1120 330 HOH   HOH B . 
M 5 HOH   221 1121 474 HOH   HOH B . 
M 5 HOH   222 1122 521 HOH   HOH B . 
M 5 HOH   223 1123 708 HOH   HOH B . 
M 5 HOH   224 1124 113 HOH   HOH B . 
M 5 HOH   225 1125 489 HOH   HOH B . 
M 5 HOH   226 1126 859 HOH   HOH B . 
M 5 HOH   227 1127 379 HOH   HOH B . 
M 5 HOH   228 1128 238 HOH   HOH B . 
M 5 HOH   229 1129 824 HOH   HOH B . 
M 5 HOH   230 1130 753 HOH   HOH B . 
M 5 HOH   231 1131 294 HOH   HOH B . 
M 5 HOH   232 1132 486 HOH   HOH B . 
M 5 HOH   233 1133 698 HOH   HOH B . 
M 5 HOH   234 1134 311 HOH   HOH B . 
M 5 HOH   235 1135 683 HOH   HOH B . 
M 5 HOH   236 1136 367 HOH   HOH B . 
M 5 HOH   237 1137 467 HOH   HOH B . 
M 5 HOH   238 1138 490 HOH   HOH B . 
M 5 HOH   239 1139 798 HOH   HOH B . 
M 5 HOH   240 1140 29  HOH   HOH B . 
M 5 HOH   241 1141 546 HOH   HOH B . 
M 5 HOH   242 1142 103 HOH   HOH B . 
M 5 HOH   243 1143 539 HOH   HOH B . 
M 5 HOH   244 1144 159 HOH   HOH B . 
M 5 HOH   245 1145 526 HOH   HOH B . 
M 5 HOH   246 1146 138 HOH   HOH B . 
M 5 HOH   247 1147 587 HOH   HOH B . 
M 5 HOH   248 1148 871 HOH   HOH B . 
M 5 HOH   249 1149 260 HOH   HOH B . 
M 5 HOH   250 1150 327 HOH   HOH B . 
M 5 HOH   251 1151 265 HOH   HOH B . 
M 5 HOH   252 1152 867 HOH   HOH B . 
M 5 HOH   253 1153 252 HOH   HOH B . 
M 5 HOH   254 1154 606 HOH   HOH B . 
M 5 HOH   255 1155 132 HOH   HOH B . 
M 5 HOH   256 1156 261 HOH   HOH B . 
M 5 HOH   257 1157 512 HOH   HOH B . 
M 5 HOH   258 1158 786 HOH   HOH B . 
M 5 HOH   259 1159 629 HOH   HOH B . 
M 5 HOH   260 1160 425 HOH   HOH B . 
M 5 HOH   261 1161 632 HOH   HOH B . 
M 5 HOH   262 1162 639 HOH   HOH B . 
M 5 HOH   263 1163 767 HOH   HOH B . 
M 5 HOH   264 1164 223 HOH   HOH B . 
M 5 HOH   265 1165 552 HOH   HOH B . 
M 5 HOH   266 1166 803 HOH   HOH B . 
M 5 HOH   267 1167 121 HOH   HOH B . 
M 5 HOH   268 1168 378 HOH   HOH B . 
M 5 HOH   269 1169 370 HOH   HOH B . 
M 5 HOH   270 1170 411 HOH   HOH B . 
M 5 HOH   271 1171 738 HOH   HOH B . 
M 5 HOH   272 1172 874 HOH   HOH B . 
M 5 HOH   273 1173 531 HOH   HOH B . 
M 5 HOH   274 1174 373 HOH   HOH B . 
M 5 HOH   275 1175 865 HOH   HOH B . 
M 5 HOH   276 1176 391 HOH   HOH B . 
M 5 HOH   277 1177 574 HOH   HOH B . 
M 5 HOH   278 1178 447 HOH   HOH B . 
M 5 HOH   279 1179 583 HOH   HOH B . 
M 5 HOH   280 1180 516 HOH   HOH B . 
M 5 HOH   281 1181 868 HOH   HOH B . 
M 5 HOH   282 1182 325 HOH   HOH B . 
M 5 HOH   283 1183 616 HOH   HOH B . 
M 5 HOH   284 1184 437 HOH   HOH B . 
M 5 HOH   285 1185 420 HOH   HOH B . 
M 5 HOH   286 1186 822 HOH   HOH B . 
M 5 HOH   287 1187 585 HOH   HOH B . 
M 5 HOH   288 1188 641 HOH   HOH B . 
M 5 HOH   289 1189 780 HOH   HOH B . 
M 5 HOH   290 1190 842 HOH   HOH B . 
M 5 HOH   291 1191 273 HOH   HOH B . 
M 5 HOH   292 1192 652 HOH   HOH B . 
M 5 HOH   293 1193 855 HOH   HOH B . 
M 5 HOH   294 1194 737 HOH   HOH B . 
M 5 HOH   295 1195 666 HOH   HOH B . 
M 5 HOH   296 1196 180 HOH   HOH B . 
M 5 HOH   297 1197 769 HOH   HOH B . 
M 5 HOH   298 1198 324 HOH   HOH B . 
M 5 HOH   299 1199 288 HOH   HOH B . 
M 5 HOH   300 1200 788 HOH   HOH B . 
M 5 HOH   301 1201 423 HOH   HOH B . 
M 5 HOH   302 1202 637 HOH   HOH B . 
M 5 HOH   303 1203 76  HOH   HOH B . 
M 5 HOH   304 1204 305 HOH   HOH B . 
M 5 HOH   305 1205 346 HOH   HOH B . 
M 5 HOH   306 1206 611 HOH   HOH B . 
M 5 HOH   307 1207 653 HOH   HOH B . 
M 5 HOH   308 1208 439 HOH   HOH B . 
M 5 HOH   309 1209 375 HOH   HOH B . 
M 5 HOH   310 1210 229 HOH   HOH B . 
M 5 HOH   311 1211 644 HOH   HOH B . 
M 5 HOH   312 1212 643 HOH   HOH B . 
M 5 HOH   313 1213 625 HOH   HOH B . 
M 5 HOH   314 1214 513 HOH   HOH B . 
M 5 HOH   315 1215 557 HOH   HOH B . 
M 5 HOH   316 1216 636 HOH   HOH B . 
M 5 HOH   317 1217 690 HOH   HOH B . 
M 5 HOH   318 1218 659 HOH   HOH B . 
M 5 HOH   319 1219 887 HOH   HOH B . 
M 5 HOH   320 1220 407 HOH   HOH B . 
M 5 HOH   321 1221 828 HOH   HOH B . 
M 5 HOH   322 1222 808 HOH   HOH B . 
M 5 HOH   323 1223 562 HOH   HOH B . 
M 5 HOH   324 1224 704 HOH   HOH B . 
M 5 HOH   325 1225 279 HOH   HOH B . 
M 5 HOH   326 1226 491 HOH   HOH B . 
M 5 HOH   327 1227 237 HOH   HOH B . 
M 5 HOH   328 1228 487 HOH   HOH B . 
M 5 HOH   329 1229 143 HOH   HOH B . 
M 5 HOH   330 1230 847 HOH   HOH B . 
M 5 HOH   331 1231 600 HOH   HOH B . 
M 5 HOH   332 1232 435 HOH   HOH B . 
M 5 HOH   333 1233 315 HOH   HOH B . 
M 5 HOH   334 1234 146 HOH   HOH B . 
M 5 HOH   335 1235 846 HOH   HOH B . 
M 5 HOH   336 1236 253 HOH   HOH B . 
M 5 HOH   337 1237 768 HOH   HOH B . 
M 5 HOH   338 1238 109 HOH   HOH B . 
M 5 HOH   339 1239 563 HOH   HOH B . 
M 5 HOH   340 1240 566 HOH   HOH B . 
M 5 HOH   341 1241 664 HOH   HOH B . 
M 5 HOH   342 1242 116 HOH   HOH B . 
M 5 HOH   343 1243 755 HOH   HOH B . 
M 5 HOH   344 1244 426 HOH   HOH B . 
M 5 HOH   345 1245 802 HOH   HOH B . 
M 5 HOH   346 1246 610 HOH   HOH B . 
M 5 HOH   347 1247 819 HOH   HOH B . 
M 5 HOH   348 1248 892 HOH   HOH B . 
M 5 HOH   349 1249 448 HOH   HOH B . 
M 5 HOH   350 1250 578 HOH   HOH B . 
M 5 HOH   351 1251 301 HOH   HOH B . 
M 5 HOH   352 1252 326 HOH   HOH B . 
M 5 HOH   353 1253 493 HOH   HOH B . 
M 5 HOH   354 1254 858 HOH   HOH B . 
M 5 HOH   355 1255 262 HOH   HOH B . 
M 5 HOH   356 1256 543 HOH   HOH B . 
M 5 HOH   357 1257 540 HOH   HOH B . 
M 5 HOH   358 1258 791 HOH   HOH B . 
M 5 HOH   359 1259 732 HOH   HOH B . 
M 5 HOH   360 1260 628 HOH   HOH B . 
M 5 HOH   361 1261 445 HOH   HOH B . 
M 5 HOH   362 1262 186 HOH   HOH B . 
M 5 HOH   363 1263 792 HOH   HOH B . 
M 5 HOH   364 1264 813 HOH   HOH B . 
M 5 HOH   365 1265 789 HOH   HOH B . 
M 5 HOH   366 1266 700 HOH   HOH B . 
M 5 HOH   367 1267 618 HOH   HOH B . 
M 5 HOH   368 1268 442 HOH   HOH B . 
M 5 HOH   369 1269 553 HOH   HOH B . 
M 5 HOH   370 1270 672 HOH   HOH B . 
M 5 HOH   371 1271 619 HOH   HOH B . 
M 5 HOH   372 1272 527 HOH   HOH B . 
M 5 HOH   373 1273 879 HOH   HOH B . 
M 5 HOH   374 1274 638 HOH   HOH B . 
M 5 HOH   375 1275 646 HOH   HOH B . 
M 5 HOH   376 1276 771 HOH   HOH B . 
M 5 HOH   377 1277 427 HOH   HOH B . 
M 5 HOH   378 1278 544 HOH   HOH B . 
M 5 HOH   379 1279 364 HOH   HOH B . 
M 5 HOH   380 1280 885 HOH   HOH B . 
M 5 HOH   381 1281 503 HOH   HOH B . 
M 5 HOH   382 1282 733 HOH   HOH B . 
M 5 HOH   383 1283 651 HOH   HOH B . 
M 5 HOH   384 1284 317 HOH   HOH B . 
M 5 HOH   385 1285 884 HOH   HOH B . 
M 5 HOH   386 1286 500 HOH   HOH B . 
M 5 HOH   387 1287 894 HOH   HOH B . 
M 5 HOH   388 1288 793 HOH   HOH B . 
M 5 HOH   389 1289 838 HOH   HOH B . 
M 5 HOH   390 1290 810 HOH   HOH B . 
M 5 HOH   391 1291 705 HOH   HOH B . 
M 5 HOH   392 1292 564 HOH   HOH B . 
M 5 HOH   393 1293 677 HOH   HOH B . 
M 5 HOH   394 1294 608 HOH   HOH B . 
M 5 HOH   395 1295 716 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 THR 773 ? OG1 ? A THR 332 OG1 
2 1 Y 1 A THR 773 ? CG2 ? A THR 332 CG2 
3 1 Y 1 B ARG 524 ? CG  ? B ARG 83  CG  
4 1 Y 1 B ARG 524 ? CD  ? B ARG 83  CD  
5 1 Y 1 B ARG 524 ? NE  ? B ARG 83  NE  
6 1 Y 1 B ARG 524 ? CZ  ? B ARG 83  CZ  
7 1 Y 1 B ARG 524 ? NH1 ? B ARG 83  NH1 
8 1 Y 1 B ARG 524 ? NH2 ? B ARG 83  NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20_4459 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EFR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.140 
_cell.length_a_esd                 ? 
_cell.length_b                     92.600 
_cell.length_b_esd                 ? 
_cell.length_c                     96.490 
_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                         9EFR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9EFR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.78 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '15% PEG 3350, 0.2M magnesium formate dihydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-20 
_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   0.9792 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EFR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.24 
_reflns.d_resolution_low                               59.28 
_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                                     157108 
_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                           82.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.2 
_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                                0.060 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.055 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.24 
_reflns_shell.d_res_low                                     1.26 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2656 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.725 
_reflns_shell.pdbx_Rpim_I_all                               0.909 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.308 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.453 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EFR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.24 
_refine.ls_d_res_low                             59.28 
_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                     157037 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    82.47 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1984 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.24 
_refine_hist.d_res_low                        59.28 
_refine_hist.number_atoms_solvent             788 
_refine_hist.number_atoms_total               6391 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5546 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         57 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     9EFR 
_struct.title                        
'Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 complexed with TO-600' 
_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        9EFR 
_struct_keywords.text            
;potassium ion binding, alkali metal ion binding, ion binding, cation binding, metal ion binding, catalytic activity, hydrolase activity, deacetylase activity, protein deacetylase activity, acting on a protein, acting on carbon-nitrogen (but not peptide) bonds, in linear amides, tubulin deacetylase activity, zinc ion binding, transition metal ion binding, METAL BINDING PROTEIN
;
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
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 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A7YT55_DANRE 
_struct_ref.pdbx_db_accession          A7YT55 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRD
LNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITR
ESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAA
FHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSML
LGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_struct_ref.pdbx_align_begin           290 
# 
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 9EFR A 1 ? 357 ? A7YT55 290 ? 646 ? 442 798 
2 1 9EFR B 1 ? 357 ? A7YT55 290 ? 646 ? 442 798 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,L   
2 1 B,G,H,I,J,K,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 8   ? HIS A 14  ? ASP A 449 HIS A 455 5 ? 7  
HELX_P HELX_P2  AA2 PRO A 26  ? LEU A 39  ? PRO A 467 LEU A 480 1 ? 14 
HELX_P HELX_P3  AA3 LEU A 41  ? CYS A 45  ? LEU A 482 CYS A 486 5 ? 5  
HELX_P HELX_P4  AA4 THR A 54  ? ALA A 59  ? THR A 495 ALA A 500 1 ? 6  
HELX_P HELX_P5  AA5 SER A 63  ? SER A 73  ? SER A 504 SER A 514 1 ? 11 
HELX_P HELX_P6  AA6 GLU A 74  ? MET A 76  ? GLU A 515 MET A 517 5 ? 3  
HELX_P HELX_P7  AA7 LYS A 77  ? GLU A 87  ? LYS A 518 GLU A 528 1 ? 11 
HELX_P HELX_P8  AA8 GLU A 96  ? THR A 117 ? GLU A 537 THR A 558 1 ? 22 
HELX_P HELX_P9  AA9 ASN A 146 ? ILE A 158 ? ASN A 587 ILE A 599 1 ? 13 
HELX_P HELX_P10 AB1 GLY A 175 ? GLU A 183 ? GLY A 616 GLU A 624 1 ? 9  
HELX_P HELX_P11 AB2 SER A 205 ? ASN A 209 ? SER A 646 ASN A 650 5 ? 5  
HELX_P HELX_P12 AB3 LEU A 215 ? ARG A 219 ? LEU A 656 ARG A 660 5 ? 5  
HELX_P HELX_P13 AB4 GLY A 233 ? LEU A 244 ? GLY A 674 LEU A 685 1 ? 12 
HELX_P HELX_P14 AB5 LEU A 244 ? ALA A 253 ? LEU A 685 ALA A 694 1 ? 10 
HELX_P HELX_P15 AB6 THR A 277 ? MET A 289 ? THR A 718 MET A 730 1 ? 13 
HELX_P HELX_P16 AB7 SER A 290 ? GLY A 294 ? SER A 731 GLY A 735 5 ? 5  
HELX_P HELX_P17 AB8 ASN A 305 ? LEU A 321 ? ASN A 746 LEU A 762 1 ? 17 
HELX_P HELX_P18 AB9 LYS A 335 ? ALA A 350 ? LYS A 776 ALA A 791 1 ? 16 
HELX_P HELX_P19 AC1 TRP A 353 ? ARG A 357 ? TRP A 794 ARG A 798 5 ? 5  
HELX_P HELX_P20 AC2 ASP B 8   ? HIS B 14  ? ASP B 449 HIS B 455 5 ? 7  
HELX_P HELX_P21 AC3 PRO B 26  ? LEU B 39  ? PRO B 467 LEU B 480 1 ? 14 
HELX_P HELX_P22 AC4 LEU B 41  ? CYS B 45  ? LEU B 482 CYS B 486 5 ? 5  
HELX_P HELX_P23 AC5 THR B 54  ? ALA B 59  ? THR B 495 ALA B 500 1 ? 6  
HELX_P HELX_P24 AC6 SER B 63  ? SER B 73  ? SER B 504 SER B 514 1 ? 11 
HELX_P HELX_P25 AC7 GLU B 74  ? MET B 76  ? GLU B 515 MET B 517 5 ? 3  
HELX_P HELX_P26 AC8 LYS B 77  ? ASP B 86  ? LYS B 518 ASP B 527 1 ? 10 
HELX_P HELX_P27 AC9 GLU B 96  ? THR B 117 ? GLU B 537 THR B 558 1 ? 22 
HELX_P HELX_P28 AD1 ASN B 146 ? ILE B 158 ? ASN B 587 ILE B 599 1 ? 13 
HELX_P HELX_P29 AD2 GLY B 175 ? GLU B 183 ? GLY B 616 GLU B 624 1 ? 9  
HELX_P HELX_P30 AD3 GLU B 197 ? ALA B 200 ? GLU B 638 ALA B 641 5 ? 4  
HELX_P HELX_P31 AD4 SER B 205 ? ASN B 209 ? SER B 646 ASN B 650 5 ? 5  
HELX_P HELX_P32 AD5 LEU B 215 ? ARG B 219 ? LEU B 656 ARG B 660 5 ? 5  
HELX_P HELX_P33 AD6 GLY B 233 ? LEU B 244 ? GLY B 674 LEU B 685 1 ? 12 
HELX_P HELX_P34 AD7 LEU B 244 ? ALA B 253 ? LEU B 685 ALA B 694 1 ? 10 
HELX_P HELX_P35 AD8 THR B 277 ? MET B 289 ? THR B 718 MET B 730 1 ? 13 
HELX_P HELX_P36 AD9 SER B 290 ? GLY B 294 ? SER B 731 GLY B 735 5 ? 5  
HELX_P HELX_P37 AE1 ASN B 305 ? LEU B 321 ? ASN B 746 LEU B 762 1 ? 17 
HELX_P HELX_P38 AE2 LYS B 335 ? ALA B 350 ? LYS B 776 ALA B 791 1 ? 16 
HELX_P HELX_P39 AE3 TRP B 353 ? ARG B 357 ? TRP B 794 ARG B 798 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP   169 O   ? ? ? 1_555 E K   . K  ? ? A ASP   610 A K   803  1_555 ? ? ? ? ? ? ? 2.823 ? ? 
metalc2  metalc ? ? A ASP   169 OD1 ? ? ? 1_555 E K   . K  ? ? A ASP   610 A K   803  1_555 ? ? ? ? ? ? ? 2.761 ? ? 
metalc3  metalc ? ? A ASP   171 OD1 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   612 A ZN  802  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc4  metalc ? ? A ASP   171 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   612 A ZN  802  1_555 ? ? ? ? ? ? ? 2.586 ? ? 
metalc5  metalc ? ? A ASP   171 O   ? ? ? 1_555 E K   . K  ? ? A ASP   612 A K   803  1_555 ? ? ? ? ? ? ? 2.581 ? ? 
metalc6  metalc ? ? A HIS   173 ND1 ? ? ? 1_555 D ZN  . ZN ? ? A HIS   614 A ZN  802  1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc7  metalc ? ? A HIS   173 O   ? ? ? 1_555 E K   . K  ? ? A HIS   614 A K   803  1_555 ? ? ? ? ? ? ? 2.675 ? ? 
metalc8  metalc ? ? A PHE   182 O   ? ? ? 1_555 F K   . K  ? ? A PHE   623 A K   804  1_555 ? ? ? ? ? ? ? 2.669 ? ? 
metalc9  metalc ? ? A ASP   185 O   ? ? ? 1_555 F K   . K  ? ? A ASP   626 A K   804  1_555 ? ? ? ? ? ? ? 2.802 ? ? 
metalc10 metalc ? ? A VAL   188 O   ? ? ? 1_555 F K   . K  ? ? A VAL   629 A K   804  1_555 ? ? ? ? ? ? ? 2.810 ? ? 
metalc11 metalc ? ? A SER   192 OG  ? ? ? 1_555 E K   . K  ? ? A SER   633 A K   803  1_555 ? ? ? ? ? ? ? 2.785 ? ? 
metalc12 metalc ? ? A LEU   193 O   ? ? ? 1_555 E K   . K  ? ? A LEU   634 A K   803  1_555 ? ? ? ? ? ? ? 2.664 ? ? 
metalc13 metalc ? ? A TYR   221 O   ? ? ? 1_555 F K   . K  ? ? A TYR   662 A K   804  1_555 ? ? ? ? ? ? ? 2.722 ? ? 
metalc14 metalc ? ? A ASP   264 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   705 A ZN  802  1_555 ? ? ? ? ? ? ? 1.921 ? ? 
metalc15 metalc ? ? C A1BHX .   N03 ? ? ? 1_555 D ZN  . ZN ? ? A A1BHX 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.630 ? ? 
metalc16 metalc ? ? C A1BHX .   O01 ? ? ? 1_555 D ZN  . ZN ? ? A A1BHX 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc17 metalc ? ? C A1BHX .   O04 ? ? ? 1_555 D ZN  . ZN ? ? A A1BHX 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc18 metalc ? ? F K     .   K   ? ? ? 1_555 L HOH . O  ? ? A K     804 A HOH 1026 1_555 ? ? ? ? ? ? ? 2.907 ? ? 
metalc19 metalc ? ? F K     .   K   ? ? ? 1_555 L HOH . O  ? ? A K     804 A HOH 1069 1_555 ? ? ? ? ? ? ? 2.678 ? ? 
metalc20 metalc ? ? B ASP   169 O   ? ? ? 1_555 J K   . K  ? ? B ASP   610 B K   804  1_555 ? ? ? ? ? ? ? 2.836 ? ? 
metalc21 metalc ? ? B ASP   169 OD1 ? ? ? 1_555 J K   . K  ? ? B ASP   610 B K   804  1_555 ? ? ? ? ? ? ? 2.755 ? ? 
metalc22 metalc ? ? B TRP   170 O   ? ? ? 1_555 K K   . K  ? ? B TRP   611 B K   805  1_555 ? ? ? ? ? ? ? 2.826 ? ? 
metalc23 metalc ? ? B ASP   171 OD1 ? ? ? 1_555 H ZN  . ZN ? ? B ASP   612 B ZN  802  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc24 metalc ? ? B ASP   171 OD2 ? ? ? 1_555 H ZN  . ZN ? ? B ASP   612 B ZN  802  1_555 ? ? ? ? ? ? ? 2.605 ? ? 
metalc25 metalc ? ? B ASP   171 O   ? ? ? 1_555 J K   . K  ? ? B ASP   612 B K   804  1_555 ? ? ? ? ? ? ? 2.604 ? ? 
metalc26 metalc ? ? B HIS   173 ND1 ? ? ? 1_555 H ZN  . ZN ? ? B HIS   614 B ZN  802  1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc27 metalc ? ? B HIS   173 O   ? ? ? 1_555 J K   . K  ? ? B HIS   614 B K   804  1_555 ? ? ? ? ? ? ? 2.659 ? ? 
metalc28 metalc ? ? B PHE   182 O   ? ? ? 1_555 I K   . K  ? ? B PHE   623 B K   803  1_555 ? ? ? ? ? ? ? 2.709 ? ? 
metalc29 metalc ? ? B ASP   185 O   ? ? ? 1_555 I K   . K  ? ? B ASP   626 B K   803  1_555 ? ? ? ? ? ? ? 2.837 ? ? 
metalc30 metalc ? ? B VAL   188 O   ? ? ? 1_555 I K   . K  ? ? B VAL   629 B K   803  1_555 ? ? ? ? ? ? ? 2.679 ? ? 
metalc31 metalc ? ? B SER   192 OG  ? ? ? 1_555 J K   . K  ? ? B SER   633 B K   804  1_555 ? ? ? ? ? ? ? 2.762 ? ? 
metalc32 metalc ? ? B LEU   193 O   ? ? ? 1_555 J K   . K  ? ? B LEU   634 B K   804  1_555 ? ? ? ? ? ? ? 2.675 ? ? 
metalc33 metalc ? ? B TYR   221 O   ? ? ? 1_555 I K   . K  ? ? B TYR   662 B K   803  1_555 ? ? ? ? ? ? ? 2.756 ? ? 
metalc34 metalc ? ? B GLY   262 O   ? ? ? 1_555 K K   . K  ? ? B GLY   703 B K   805  1_555 ? ? ? ? ? ? ? 2.716 ? ? 
metalc35 metalc ? ? B ASP   264 OD2 ? ? ? 1_555 H ZN  . ZN ? ? B ASP   705 B ZN  802  1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc36 metalc ? ? B TYR   281 OH  ? ? ? 1_555 K K   . K  ? ? B TYR   722 B K   805  1_555 ? ? ? ? ? ? ? 2.684 ? ? 
metalc37 metalc ? ? G A1BHX .   N03 ? ? ? 1_555 H ZN  . ZN ? ? B A1BHX 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.616 ? ? 
metalc38 metalc ? ? G A1BHX .   O01 ? ? ? 1_555 H ZN  . ZN ? ? B A1BHX 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc39 metalc ? ? G A1BHX .   O04 ? ? ? 1_555 H ZN  . ZN ? ? B A1BHX 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc40 metalc ? ? I K     .   K   ? ? ? 1_555 M HOH . O  ? ? B K     803 B HOH 970  1_555 ? ? ? ? ? ? ? 2.703 ? ? 
metalc41 metalc ? ? I K     .   K   ? ? ? 1_555 M HOH . O  ? ? B K     803 B HOH 1000 1_555 ? ? ? ? ? ? ? 2.939 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O   ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 OD1 ? A ASP   169 ? A ASP   610  ? 1_555 70.2  ? 
2   O   ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A ASP   171 ? A ASP   612  ? 1_555 99.1  ? 
3   OD1 ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A ASP   171 ? A ASP   612  ? 1_555 97.7  ? 
4   O   ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A HIS   173 ? A HIS   614  ? 1_555 163.9 ? 
5   OD1 ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A HIS   173 ? A HIS   614  ? 1_555 93.7  ? 
6   O   ? A ASP   171 ? A ASP   612  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A HIS   173 ? A HIS   614  ? 1_555 80.8  ? 
7   O   ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 OG  ? A SER   192 ? A SER   633  ? 1_555 85.3  ? 
8   OD1 ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 OG  ? A SER   192 ? A SER   633  ? 1_555 110.2 ? 
9   O   ? A ASP   171 ? A ASP   612  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 OG  ? A SER   192 ? A SER   633  ? 1_555 151.5 ? 
10  O   ? A HIS   173 ? A HIS   614  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 OG  ? A SER   192 ? A SER   633  ? 1_555 102.6 ? 
11  O   ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A LEU   193 ? A LEU   634  ? 1_555 78.6  ? 
12  OD1 ? A ASP   169 ? A ASP   610  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A LEU   193 ? A LEU   634  ? 1_555 143.9 ? 
13  O   ? A ASP   171 ? A ASP   612  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A LEU   193 ? A LEU   634  ? 1_555 69.4  ? 
14  O   ? A HIS   173 ? A HIS   614  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A LEU   193 ? A LEU   634  ? 1_555 115.9 ? 
15  OG  ? A SER   192 ? A SER   633  ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A LEU   193 ? A LEU   634  ? 1_555 84.1  ? 
16  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP   171 ? A ASP   612  ? 1_555 53.1  ? 
17  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 ND1 ? A HIS   173 ? A HIS   614  ? 1_555 101.7 ? 
18  OD2 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 ND1 ? A HIS   173 ? A HIS   614  ? 1_555 154.7 ? 
19  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP   264 ? A ASP   705  ? 1_555 105.0 ? 
20  OD2 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP   264 ? A ASP   705  ? 1_555 85.5  ? 
21  ND1 ? A HIS   173 ? A HIS   614  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 OD2 ? A ASP   264 ? A ASP   705  ? 1_555 101.3 ? 
22  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 118.2 ? 
23  OD2 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 113.0 ? 
24  ND1 ? A HIS   173 ? A HIS   614  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 78.9  ? 
25  OD2 ? A ASP   264 ? A ASP   705  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 136.0 ? 
26  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 165.4 ? 
27  OD2 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 117.3 ? 
28  ND1 ? A HIS   173 ? A HIS   614  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 87.8  ? 
29  OD2 ? A ASP   264 ? A ASP   705  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 83.7  ? 
30  N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 52.3  ? 
31  OD1 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 90.6  ? 
32  OD2 ? A ASP   171 ? A ASP   612  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 83.0  ? 
33  ND1 ? A HIS   173 ? A HIS   614  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 101.2 ? 
34  OD2 ? A ASP   264 ? A ASP   705  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 149.3 ? 
35  N03 ? C A1BHX .   ? A A1BHX 801  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 32.5  ? 
36  O01 ? C A1BHX .   ? A A1BHX 801  ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BHX .   ? A A1BHX 801  ? 1_555 76.5  ? 
37  O   ? A PHE   182 ? A PHE   623  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A ASP   185 ? A ASP   626  ? 1_555 77.0  ? 
38  O   ? A PHE   182 ? A PHE   623  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A VAL   188 ? A VAL   629  ? 1_555 120.1 ? 
39  O   ? A ASP   185 ? A ASP   626  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A VAL   188 ? A VAL   629  ? 1_555 69.5  ? 
40  O   ? A PHE   182 ? A PHE   623  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 155.3 ? 
41  O   ? A ASP   185 ? A ASP   626  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 114.7 ? 
42  O   ? A VAL   188 ? A VAL   629  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 84.6  ? 
43  O   ? A PHE   182 ? A PHE   623  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1026 ? 1_555 69.7  ? 
44  O   ? A ASP   185 ? A ASP   626  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1026 ? 1_555 145.9 ? 
45  O   ? A VAL   188 ? A VAL   629  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1026 ? 1_555 134.5 ? 
46  O   ? A TYR   221 ? A TYR   662  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1026 ? 1_555 94.0  ? 
47  O   ? A PHE   182 ? A PHE   623  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1069 ? 1_555 78.2  ? 
48  O   ? A ASP   185 ? A ASP   626  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1069 ? 1_555 87.3  ? 
49  O   ? A VAL   188 ? A VAL   629  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1069 ? 1_555 144.0 ? 
50  O   ? A TYR   221 ? A TYR   662  ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1069 ? 1_555 80.6  ? 
51  O   ? L HOH   .   ? A HOH   1026 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? L HOH   .   ? A HOH   1069 ? 1_555 79.4  ? 
52  O   ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 OD1 ? B ASP   169 ? B ASP   610  ? 1_555 69.9  ? 
53  O   ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B ASP   171 ? B ASP   612  ? 1_555 99.5  ? 
54  OD1 ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B ASP   171 ? B ASP   612  ? 1_555 98.0  ? 
55  O   ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B HIS   173 ? B HIS   614  ? 1_555 163.9 ? 
56  OD1 ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B HIS   173 ? B HIS   614  ? 1_555 94.1  ? 
57  O   ? B ASP   171 ? B ASP   612  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B HIS   173 ? B HIS   614  ? 1_555 80.5  ? 
58  O   ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 OG  ? B SER   192 ? B SER   633  ? 1_555 84.9  ? 
59  OD1 ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 OG  ? B SER   192 ? B SER   633  ? 1_555 109.9 ? 
60  O   ? B ASP   171 ? B ASP   612  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 OG  ? B SER   192 ? B SER   633  ? 1_555 151.4 ? 
61  O   ? B HIS   173 ? B HIS   614  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 OG  ? B SER   192 ? B SER   633  ? 1_555 102.9 ? 
62  O   ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B LEU   193 ? B LEU   634  ? 1_555 78.3  ? 
63  OD1 ? B ASP   169 ? B ASP   610  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B LEU   193 ? B LEU   634  ? 1_555 143.0 ? 
64  O   ? B ASP   171 ? B ASP   612  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B LEU   193 ? B LEU   634  ? 1_555 68.6  ? 
65  O   ? B HIS   173 ? B HIS   614  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B LEU   193 ? B LEU   634  ? 1_555 116.0 ? 
66  OG  ? B SER   192 ? B SER   633  ? 1_555 K  ? J K  . ? B K  804 ? 1_555 O   ? B LEU   193 ? B LEU   634  ? 1_555 85.0  ? 
67  O   ? B TRP   170 ? B TRP   611  ? 1_555 K  ? K K  . ? B K  805 ? 1_555 O   ? B GLY   262 ? B GLY   703  ? 1_555 92.5  ? 
68  O   ? B TRP   170 ? B TRP   611  ? 1_555 K  ? K K  . ? B K  805 ? 1_555 OH  ? B TYR   281 ? B TYR   722  ? 1_555 130.0 ? 
69  O   ? B GLY   262 ? B GLY   703  ? 1_555 K  ? K K  . ? B K  805 ? 1_555 OH  ? B TYR   281 ? B TYR   722  ? 1_555 104.8 ? 
70  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   171 ? B ASP   612  ? 1_555 53.0  ? 
71  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 ND1 ? B HIS   173 ? B HIS   614  ? 1_555 101.2 ? 
72  OD2 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 ND1 ? B HIS   173 ? B HIS   614  ? 1_555 154.1 ? 
73  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   264 ? B ASP   705  ? 1_555 104.1 ? 
74  OD2 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   264 ? B ASP   705  ? 1_555 86.7  ? 
75  ND1 ? B HIS   173 ? B HIS   614  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   264 ? B ASP   705  ? 1_555 98.9  ? 
76  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 118.1 ? 
77  OD2 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 111.7 ? 
78  ND1 ? B HIS   173 ? B HIS   614  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 81.3  ? 
79  OD2 ? B ASP   264 ? B ASP   705  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 137.0 ? 
80  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 166.6 ? 
81  OD2 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 117.8 ? 
82  ND1 ? B HIS   173 ? B HIS   614  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 88.1  ? 
83  OD2 ? B ASP   264 ? B ASP   705  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 83.6  ? 
84  N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 53.4  ? 
85  OD1 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 90.3  ? 
86  OD2 ? B ASP   171 ? B ASP   612  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 81.6  ? 
87  ND1 ? B HIS   173 ? B HIS   614  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 103.5 ? 
88  OD2 ? B ASP   264 ? B ASP   705  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 150.4 ? 
89  N03 ? G A1BHX .   ? B A1BHX 801  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 32.6  ? 
90  O01 ? G A1BHX .   ? B A1BHX 801  ? 1_555 ZN ? H ZN . ? B ZN 802 ? 1_555 O04 ? G A1BHX .   ? B A1BHX 801  ? 1_555 78.1  ? 
91  O   ? B PHE   182 ? B PHE   623  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B ASP   185 ? B ASP   626  ? 1_555 74.4  ? 
92  O   ? B PHE   182 ? B PHE   623  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B VAL   188 ? B VAL   629  ? 1_555 118.0 ? 
93  O   ? B ASP   185 ? B ASP   626  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B VAL   188 ? B VAL   629  ? 1_555 77.4  ? 
94  O   ? B PHE   182 ? B PHE   623  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 155.0 ? 
95  O   ? B ASP   185 ? B ASP   626  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 116.2 ? 
96  O   ? B VAL   188 ? B VAL   629  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 86.9  ? 
97  O   ? B PHE   182 ? B PHE   623  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   970  ? 1_555 79.8  ? 
98  O   ? B ASP   185 ? B ASP   626  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   970  ? 1_555 87.2  ? 
99  O   ? B VAL   188 ? B VAL   629  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   970  ? 1_555 151.3 ? 
100 O   ? B TYR   221 ? B TYR   662  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   970  ? 1_555 78.3  ? 
101 O   ? B PHE   182 ? B PHE   623  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   1000 ? 1_555 71.7  ? 
102 O   ? B ASP   185 ? B ASP   626  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   1000 ? 1_555 145.7 ? 
103 O   ? B VAL   188 ? B VAL   629  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   1000 ? 1_555 123.6 ? 
104 O   ? B TYR   221 ? B TYR   662  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   1000 ? 1_555 93.4  ? 
105 O   ? M HOH   .   ? B HOH   970  ? 1_555 K  ? I K  . ? B K  803 ? 1_555 O   ? M HOH   .   ? B HOH   1000 ? 1_555 82.2  ? 
# 
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 128 A . ? ARG 569 A PRO 129 A ? PRO 570 A 1 -4.84 
2 PHE 202 A . ? PHE 643 A PRO 203 A ? PRO 644 A 1 7.42  
3 ARG 128 B . ? ARG 569 B PRO 129 B ? PRO 570 B 1 -3.84 
4 PHE 202 B . ? PHE 643 B PRO 203 B ? PRO 644 B 1 7.42  
# 
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 HIS A 46  ? ARG A 47  ? HIS A 487 ARG A 488 
AA1 2 THR A 3   ? VAL A 6   ? THR A 444 VAL A 447 
AA1 3 ASN A 122 ? ALA A 125 ? ASN A 563 ALA A 566 
AA1 4 VAL A 296 ? LEU A 300 ? VAL A 737 LEU A 741 
AA1 5 LEU A 256 ? ALA A 261 ? LEU A 697 ALA A 702 
AA1 6 VAL A 165 ? ASP A 169 ? VAL A 606 ASP A 610 
AA1 7 VAL A 188 ? ARG A 195 ? VAL A 629 ARG A 636 
AA1 8 ASN A 222 ? TRP A 227 ? ASN A 663 TRP A 668 
AA2 1 HIS B 46  ? ARG B 47  ? HIS B 487 ARG B 488 
AA2 2 THR B 3   ? VAL B 6   ? THR B 444 VAL B 447 
AA2 3 ASN B 122 ? ALA B 125 ? ASN B 563 ALA B 566 
AA2 4 VAL B 296 ? LEU B 300 ? VAL B 737 LEU B 741 
AA2 5 LEU B 256 ? ALA B 261 ? LEU B 697 ALA B 702 
AA2 6 VAL B 165 ? ASP B 169 ? VAL B 606 ASP B 610 
AA2 7 VAL B 188 ? ARG B 195 ? VAL B 629 ARG B 636 
AA2 8 ASN B 222 ? TRP B 227 ? ASN B 663 TRP B 668 
# 
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 HIS A 46  ? O HIS A 487 N THR A 3   ? N THR A 444 
AA1 2 3 N GLY A 4   ? N GLY A 445 O ASN A 122 ? O ASN A 563 
AA1 3 4 N ALA A 125 ? N ALA A 566 O ILE A 298 ? O ILE A 739 
AA1 4 5 O LEU A 297 ? O LEU A 738 N VAL A 259 ? N VAL A 700 
AA1 5 6 O LEU A 258 ? O LEU A 699 N LEU A 166 ? N LEU A 607 
AA1 6 7 N ILE A 167 ? N ILE A 608 O LEU A 189 ? O LEU A 630 
AA1 7 8 N TYR A 190 ? N TYR A 631 O VAL A 223 ? O VAL A 664 
AA2 1 2 O HIS B 46  ? O HIS B 487 N THR B 3   ? N THR B 444 
AA2 2 3 N GLY B 4   ? N GLY B 445 O ASN B 122 ? O ASN B 563 
AA2 3 4 N ALA B 125 ? N ALA B 566 O ILE B 298 ? O ILE B 739 
AA2 4 5 O LEU B 297 ? O LEU B 738 N VAL B 259 ? N VAL B 700 
AA2 5 6 O LEU B 258 ? O LEU B 699 N LEU B 166 ? N LEU B 607 
AA2 6 7 N ASP B 169 ? N ASP B 610 O ILE B 191 ? O ILE B 632 
AA2 7 8 N TYR B 190 ? N TYR B 631 O VAL B 223 ? O VAL B 664 
# 
_pdbx_entry_details.entry_id                   9EFR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 THR A 600 ? ? -125.74 -96.04  
2  1 ASN A 645 ? ? 71.91   35.33   
3  1 LEU A 685 ? ? -125.24 -62.56  
4  1 ALA A 702 ? ? -100.29 76.18   
5  1 GLN A 716 ? ? -145.64 35.18   
6  1 GLU A 742 ? ? -108.63 -112.99 
7  1 SER B 531 ? ? 61.98   62.69   
8  1 THR B 600 ? ? -127.11 -94.31  
9  1 ASN B 645 ? ? 71.62   34.93   
10 1 LEU B 685 ? ? -122.17 -64.85  
11 1 GLN B 716 ? ? -141.92 36.15   
12 1 GLU B 742 ? ? -109.21 -114.16 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1293 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.00 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASP 770 ? A ASP 329 
2 1 Y 1 A HIS 771 ? A HIS 330 
3 1 Y 1 A LEU 772 ? A LEU 331 
# 
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 
A1BHX C13  C  Y N 1   
A1BHX C15  C  Y N 2   
A1BHX C17  C  Y N 3   
A1BHX C20  C  N N 4   
A1BHX C21  C  N N 5   
A1BHX C22  C  N N 6   
A1BHX C24  C  Y N 7   
A1BHX C02  C  N N 8   
A1BHX C05  C  Y N 9   
A1BHX C06  C  Y N 10  
A1BHX C07  C  Y N 11  
A1BHX C08  C  Y N 12  
A1BHX C09  C  N N 13  
A1BHX C11  C  N N 14  
A1BHX C12  C  Y N 15  
A1BHX C14  C  Y N 16  
A1BHX C25  C  Y N 17  
A1BHX N03  N  N N 18  
A1BHX N10  N  N N 19  
A1BHX N16  N  Y N 20  
A1BHX O01  O  N N 21  
A1BHX O04  O  N N 22  
A1BHX O19  O  N N 23  
A1BHX O23  O  N N 24  
A1BHX S18  S  N N 25  
A1BHX H1   H  N N 26  
A1BHX H2   H  N N 27  
A1BHX H3   H  N N 28  
A1BHX H4   H  N N 29  
A1BHX H5   H  N N 30  
A1BHX H6   H  N N 31  
A1BHX H7   H  N N 32  
A1BHX H8   H  N N 33  
A1BHX H9   H  N N 34  
A1BHX H10  H  N N 35  
A1BHX H11  H  N N 36  
A1BHX H12  H  N N 37  
A1BHX H13  H  N N 38  
A1BHX H14  H  N N 39  
A1BHX H15  H  N N 40  
A1BHX H16  H  N N 41  
A1BHX H17  H  N N 42  
A1BHX H18  H  N N 43  
A1BHX H19  H  N N 44  
A1BHX H20  H  N N 45  
A1BHX H21  H  N N 46  
ALA   N    N  N N 47  
ALA   CA   C  N S 48  
ALA   C    C  N N 49  
ALA   O    O  N N 50  
ALA   CB   C  N N 51  
ALA   OXT  O  N N 52  
ALA   H    H  N N 53  
ALA   H2   H  N N 54  
ALA   HA   H  N N 55  
ALA   HB1  H  N N 56  
ALA   HB2  H  N N 57  
ALA   HB3  H  N N 58  
ALA   HXT  H  N N 59  
ARG   N    N  N N 60  
ARG   CA   C  N S 61  
ARG   C    C  N N 62  
ARG   O    O  N N 63  
ARG   CB   C  N N 64  
ARG   CG   C  N N 65  
ARG   CD   C  N N 66  
ARG   NE   N  N N 67  
ARG   CZ   C  N N 68  
ARG   NH1  N  N N 69  
ARG   NH2  N  N N 70  
ARG   OXT  O  N N 71  
ARG   H    H  N N 72  
ARG   H2   H  N N 73  
ARG   HA   H  N N 74  
ARG   HB2  H  N N 75  
ARG   HB3  H  N N 76  
ARG   HG2  H  N N 77  
ARG   HG3  H  N N 78  
ARG   HD2  H  N N 79  
ARG   HD3  H  N N 80  
ARG   HE   H  N N 81  
ARG   HH11 H  N N 82  
ARG   HH12 H  N N 83  
ARG   HH21 H  N N 84  
ARG   HH22 H  N N 85  
ARG   HXT  H  N N 86  
ASN   N    N  N N 87  
ASN   CA   C  N S 88  
ASN   C    C  N N 89  
ASN   O    O  N N 90  
ASN   CB   C  N N 91  
ASN   CG   C  N N 92  
ASN   OD1  O  N N 93  
ASN   ND2  N  N N 94  
ASN   OXT  O  N N 95  
ASN   H    H  N N 96  
ASN   H2   H  N N 97  
ASN   HA   H  N N 98  
ASN   HB2  H  N N 99  
ASN   HB3  H  N N 100 
ASN   HD21 H  N N 101 
ASN   HD22 H  N N 102 
ASN   HXT  H  N N 103 
ASP   N    N  N N 104 
ASP   CA   C  N S 105 
ASP   C    C  N N 106 
ASP   O    O  N N 107 
ASP   CB   C  N N 108 
ASP   CG   C  N N 109 
ASP   OD1  O  N N 110 
ASP   OD2  O  N N 111 
ASP   OXT  O  N N 112 
ASP   H    H  N N 113 
ASP   H2   H  N N 114 
ASP   HA   H  N N 115 
ASP   HB2  H  N N 116 
ASP   HB3  H  N N 117 
ASP   HD2  H  N N 118 
ASP   HXT  H  N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
K     K    K  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1BHX O01 C02  doub N N 1   
A1BHX O04 N03  sing N N 2   
A1BHX C02 N03  sing N N 3   
A1BHX C02 C05  sing N N 4   
A1BHX C25 C05  doub Y N 5   
A1BHX C25 C24  sing Y N 6   
A1BHX C05 C06  sing Y N 7   
A1BHX C24 C08  doub Y N 8   
A1BHX C06 C07  doub Y N 9   
A1BHX O19 S18  doub N N 10  
A1BHX C08 C07  sing Y N 11  
A1BHX C08 C09  sing N N 12  
A1BHX N16 C15  doub Y N 13  
A1BHX N16 C17  sing Y N 14  
A1BHX C15 C14  sing Y N 15  
A1BHX C09 N10  sing N N 16  
A1BHX S18 O23  doub N N 17  
A1BHX S18 N10  sing N N 18  
A1BHX S18 C20  sing N N 19  
A1BHX C17 C12  doub Y N 20  
A1BHX N10 C11  sing N N 21  
A1BHX C14 C13  doub Y N 22  
A1BHX C12 C13  sing Y N 23  
A1BHX C12 C11  sing N N 24  
A1BHX C22 C20  sing N N 25  
A1BHX C20 C21  sing N N 26  
A1BHX C13 H1   sing N N 27  
A1BHX C15 H2   sing N N 28  
A1BHX C17 H3   sing N N 29  
A1BHX C20 H4   sing N N 30  
A1BHX C21 H5   sing N N 31  
A1BHX C21 H6   sing N N 32  
A1BHX C21 H7   sing N N 33  
A1BHX C22 H8   sing N N 34  
A1BHX C22 H9   sing N N 35  
A1BHX C22 H10  sing N N 36  
A1BHX C24 H11  sing N N 37  
A1BHX C06 H12  sing N N 38  
A1BHX C07 H13  sing N N 39  
A1BHX C09 H14  sing N N 40  
A1BHX C09 H15  sing N N 41  
A1BHX C11 H16  sing N N 42  
A1BHX C11 H17  sing N N 43  
A1BHX C14 H18  sing N N 44  
A1BHX C25 H19  sing N N 45  
A1BHX N03 H20  sing N N 46  
A1BHX O04 H21  sing N N 47  
ALA   N   CA   sing N N 48  
ALA   N   H    sing N N 49  
ALA   N   H2   sing N N 50  
ALA   CA  C    sing N N 51  
ALA   CA  CB   sing N N 52  
ALA   CA  HA   sing N N 53  
ALA   C   O    doub N N 54  
ALA   C   OXT  sing N N 55  
ALA   CB  HB1  sing N N 56  
ALA   CB  HB2  sing N N 57  
ALA   CB  HB3  sing N N 58  
ALA   OXT HXT  sing N N 59  
ARG   N   CA   sing N N 60  
ARG   N   H    sing N N 61  
ARG   N   H2   sing N N 62  
ARG   CA  C    sing N N 63  
ARG   CA  CB   sing N N 64  
ARG   CA  HA   sing N N 65  
ARG   C   O    doub N N 66  
ARG   C   OXT  sing N N 67  
ARG   CB  CG   sing N N 68  
ARG   CB  HB2  sing N N 69  
ARG   CB  HB3  sing N N 70  
ARG   CG  CD   sing N N 71  
ARG   CG  HG2  sing N N 72  
ARG   CG  HG3  sing N N 73  
ARG   CD  NE   sing N N 74  
ARG   CD  HD2  sing N N 75  
ARG   CD  HD3  sing N N 76  
ARG   NE  CZ   sing N N 77  
ARG   NE  HE   sing N N 78  
ARG   CZ  NH1  sing N N 79  
ARG   CZ  NH2  doub N N 80  
ARG   NH1 HH11 sing N N 81  
ARG   NH1 HH12 sing N N 82  
ARG   NH2 HH21 sing N N 83  
ARG   NH2 HH22 sing N N 84  
ARG   OXT HXT  sing N N 85  
ASN   N   CA   sing N N 86  
ASN   N   H    sing N N 87  
ASN   N   H2   sing N N 88  
ASN   CA  C    sing N N 89  
ASN   CA  CB   sing N N 90  
ASN   CA  HA   sing N N 91  
ASN   C   O    doub N N 92  
ASN   C   OXT  sing N N 93  
ASN   CB  CG   sing N N 94  
ASN   CB  HB2  sing N N 95  
ASN   CB  HB3  sing N N 96  
ASN   CG  OD1  doub N N 97  
ASN   CG  ND2  sing N N 98  
ASN   ND2 HD21 sing N N 99  
ASN   ND2 HD22 sing N N 100 
ASN   OXT HXT  sing N N 101 
ASP   N   CA   sing N N 102 
ASP   N   H    sing N N 103 
ASP   N   H2   sing N N 104 
ASP   CA  C    sing N N 105 
ASP   CA  CB   sing N N 106 
ASP   CA  HA   sing N N 107 
ASP   C   O    doub N N 108 
ASP   C   OXT  sing N N 109 
ASP   CB  CG   sing N N 110 
ASP   CB  HB2  sing N N 111 
ASP   CB  HB3  sing N N 112 
ASP   CG  OD1  doub N N 113 
ASP   CG  OD2  sing N N 114 
ASP   OD2 HD2  sing N N 115 
ASP   OXT HXT  sing N N 116 
CYS   N   CA   sing N N 117 
CYS   N   H    sing N N 118 
CYS   N   H2   sing N N 119 
CYS   CA  C    sing N N 120 
CYS   CA  CB   sing N N 121 
CYS   CA  HA   sing N N 122 
CYS   C   O    doub N N 123 
CYS   C   OXT  sing N N 124 
CYS   CB  SG   sing N N 125 
CYS   CB  HB2  sing N N 126 
CYS   CB  HB3  sing N N 127 
CYS   SG  HG   sing N N 128 
CYS   OXT HXT  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Natural Sciences and Engineering Research Council (NSERC, Canada)' Canada RGPIN-2014-05767 1 
'Canadian Institutes of Health Research (CIHR)'                     Canada MOP-130424       2 
'Canada Research Chairs'                                            Canada 950-232042       3 
'Ontario Research Fund'                                             Canada 34876            4 
'Canada Foundation for Innovation'                                  Canada 33536            5 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6CSR 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EFR 
_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]   0.013308 
_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]   0.010799 
_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]   0.010364 
_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  
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   . PRO   A 1 1   ? 27.830  5.045   -47.092 1.00 46.88 ? 442  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 1   ? 27.302  4.864   -45.731 1.00 40.94 ? 442  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 1   ? 26.075  3.961   -45.724 1.00 31.22 ? 442  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 1   ? 25.016  4.334   -46.219 1.00 30.23 ? 442  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 1   ? 26.931  6.288   -45.294 1.00 41.75 ? 442  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 1   ? 26.777  7.052   -46.566 1.00 38.47 ? 442  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 1   ? 27.716  6.436   -47.557 1.00 45.13 ? 442  PRO   A CD  1 
ATOM   8    N  N   . ILE   A 1 2   ? 26.231  2.770   -45.160 1.00 26.54 ? 443  ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 2   ? 25.200  1.742   -45.176 1.00 21.77 ? 443  ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 2   ? 24.607  1.618   -43.777 1.00 20.64 ? 443  ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 2   ? 25.324  1.729   -42.776 1.00 19.98 ? 443  ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 2   ? 25.807  0.407   -45.650 1.00 23.58 ? 443  ILE   A CB  1 
ATOM   13   C  CG1 . ILE   A 1 2   ? 26.329  0.541   -47.084 1.00 34.26 ? 443  ILE   A CG1 1 
ATOM   14   C  CG2 . ILE   A 1 2   ? 24.793  -0.718  -45.567 1.00 25.24 ? 443  ILE   A CG2 1 
ATOM   15   C  CD1 . ILE   A 1 2   ? 27.103  -0.670  -47.570 1.00 40.17 ? 443  ILE   A CD1 1 
ATOM   16   N  N   . THR   A 1 3   ? 23.292  1.416   -43.704 1.00 16.36 ? 444  THR   A N   1 
ATOM   17   C  CA  . THR   A 1 3   ? 22.614  1.115   -42.445 1.00 16.37 ? 444  THR   A CA  1 
ATOM   18   C  C   . THR   A 1 3   ? 22.203  -0.349  -42.467 1.00 17.12 ? 444  THR   A C   1 
ATOM   19   O  O   . THR   A 1 3   ? 21.540  -0.794  -43.405 1.00 17.79 ? 444  THR   A O   1 
ATOM   20   C  CB  . THR   A 1 3   ? 21.368  1.987   -42.286 1.00 16.17 ? 444  THR   A CB  1 
ATOM   21   O  OG1 . THR   A 1 3   ? 21.749  3.358   -42.175 1.00 18.21 ? 444  THR   A OG1 1 
ATOM   22   C  CG2 . THR   A 1 3   ? 20.564  1.577   -41.051 1.00 15.10 ? 444  THR   A CG2 1 
ATOM   23   N  N   . GLY   A 1 4   ? 22.622  -1.101  -41.460 1.00 14.52 ? 445  GLY   A N   1 
ATOM   24   C  CA  . GLY   A 1 4   ? 22.178  -2.478  -41.316 1.00 15.43 ? 445  GLY   A CA  1 
ATOM   25   C  C   . GLY   A 1 4   ? 20.848  -2.585  -40.576 1.00 15.22 ? 445  GLY   A C   1 
ATOM   26   O  O   . GLY   A 1 4   ? 20.500  -1.738  -39.779 1.00 14.48 ? 445  GLY   A O   1 
ATOM   27   N  N   . LEU   A 1 5   ? 20.118  -3.659  -40.851 1.00 13.64 ? 446  LEU   A N   1 
ATOM   28   C  CA  . LEU   A 1 5   ? 18.919  -3.993  -40.096 1.00 13.49 ? 446  LEU   A CA  1 
ATOM   29   C  C   . LEU   A 1 5   ? 18.882  -5.496  -39.901 1.00 11.65 ? 446  LEU   A C   1 
ATOM   30   O  O   . LEU   A 1 5   ? 19.082  -6.260  -40.855 1.00 13.06 ? 446  LEU   A O   1 
ATOM   31   C  CB  . LEU   A 1 5   ? 17.685  -3.532  -40.872 1.00 15.21 ? 446  LEU   A CB  1 
ATOM   32   C  CG  . LEU   A 1 5   ? 16.300  -3.807  -40.280 1.00 14.20 ? 446  LEU   A CG  1 
ATOM   33   C  CD1 . LEU   A 1 5   ? 15.333  -2.726  -40.775 1.00 14.83 ? 446  LEU   A CD1 1 
ATOM   34   C  CD2 . LEU   A 1 5   ? 15.781  -5.205  -40.637 1.00 14.20 ? 446  LEU   A CD2 1 
ATOM   35   N  N   . VAL   A 1 6   ? 18.607  -5.930  -38.672 1.00 12.37 ? 447  VAL   A N   1 
ATOM   36   C  CA  . VAL   A 1 6   ? 18.444  -7.340  -38.364 1.00 11.67 ? 447  VAL   A CA  1 
ATOM   37   C  C   . VAL   A 1 6   ? 17.048  -7.559  -37.785 1.00 12.90 ? 447  VAL   A C   1 
ATOM   38   O  O   . VAL   A 1 6   ? 16.580  -6.776  -36.948 1.00 12.25 ? 447  VAL   A O   1 
ATOM   39   C  CB  . VAL   A 1 6   ? 19.573  -7.896  -37.459 1.00 14.27 ? 447  VAL   A CB  1 
ATOM   40   C  CG1 . VAL   A 1 6   ? 19.645  -7.169  -36.115 1.00 13.89 ? 447  VAL   A CG1 1 
ATOM   41   C  CG2 . VAL   A 1 6   ? 19.419  -9.386  -37.263 1.00 16.56 ? 447  VAL   A CG2 1 
ATOM   42   N  N   . TYR   A 1 7   ? 16.385  -8.603  -38.264 1.00 13.27 ? 448  TYR   A N   1 
ATOM   43   C  CA  . TYR   A 1 7   ? 15.052  -8.997  -37.826 1.00 14.24 ? 448  TYR   A CA  1 
ATOM   44   C  C   . TYR   A 1 7   ? 14.881  -10.464 -38.196 1.00 15.06 ? 448  TYR   A C   1 
ATOM   45   O  O   . TYR   A 1 7   ? 15.251  -10.866 -39.300 1.00 16.90 ? 448  TYR   A O   1 
ATOM   46   C  CB  . TYR   A 1 7   ? 13.954  -8.177  -38.526 1.00 13.50 ? 448  TYR   A CB  1 
ATOM   47   C  CG  . TYR   A 1 7   ? 12.581  -8.769  -38.315 1.00 13.31 ? 448  TYR   A CG  1 
ATOM   48   C  CD1 . TYR   A 1 7   ? 11.931  -8.633  -37.094 1.00 12.83 ? 448  TYR   A CD1 1 
ATOM   49   C  CD2 . TYR   A 1 7   ? 11.953  -9.507  -39.309 1.00 14.94 ? 448  TYR   A CD2 1 
ATOM   50   C  CE1 . TYR   A 1 7   ? 10.682  -9.183  -36.874 1.00 13.42 ? 448  TYR   A CE1 1 
ATOM   51   C  CE2 . TYR   A 1 7   ? 10.691  -10.056 -39.110 1.00 14.24 ? 448  TYR   A CE2 1 
ATOM   52   C  CZ  . TYR   A 1 7   ? 10.065  -9.902  -37.883 1.00 13.91 ? 448  TYR   A CZ  1 
ATOM   53   O  OH  . TYR   A 1 7   ? 8.805   -10.452 -37.667 1.00 16.53 ? 448  TYR   A OH  1 
ATOM   54   N  N   . ASP   A 1 8   ? 14.337  -11.262 -37.281 1.00 14.84 ? 449  ASP   A N   1 
ATOM   55   C  CA  . ASP   A 1 8   ? 14.020  -12.657 -37.580 1.00 16.19 ? 449  ASP   A CA  1 
ATOM   56   C  C   . ASP   A 1 8   ? 12.675  -12.986 -36.954 1.00 17.02 ? 449  ASP   A C   1 
ATOM   57   O  O   . ASP   A 1 8   ? 12.507  -12.837 -35.741 1.00 16.13 ? 449  ASP   A O   1 
ATOM   58   C  CB  . ASP   A 1 8   ? 15.132  -13.578 -37.061 1.00 18.62 ? 449  ASP   A CB  1 
ATOM   59   C  CG  . ASP   A 1 8   ? 15.051  -14.979 -37.626 1.00 20.97 ? 449  ASP   A CG  1 
ATOM   60   O  OD1 . ASP   A 1 8   ? 13.948  -15.550 -37.650 1.00 19.13 ? 449  ASP   A OD1 1 
ATOM   61   O  OD2 . ASP   A 1 8   ? 16.101  -15.523 -38.047 1.00 31.30 ? 449  ASP   A OD2 1 
ATOM   62   N  N   A GLN   A 1 9   ? 11.726  -13.444 -37.779 0.48 14.11 ? 450  GLN   A N   1 
ATOM   63   N  N   B GLN   A 1 9   ? 11.723  -13.426 -37.790 0.52 13.53 ? 450  GLN   A N   1 
ATOM   64   C  CA  A GLN   A 1 9   ? 10.402  -13.797 -37.276 0.48 14.91 ? 450  GLN   A CA  1 
ATOM   65   C  CA  B GLN   A 1 9   ? 10.363  -13.689 -37.324 0.52 15.64 ? 450  GLN   A CA  1 
ATOM   66   C  C   A GLN   A 1 9   ? 10.449  -14.931 -36.259 0.48 13.90 ? 450  GLN   A C   1 
ATOM   67   C  C   B GLN   A 1 9   ? 10.329  -14.731 -36.212 0.52 16.72 ? 450  GLN   A C   1 
ATOM   68   O  O   A GLN   A 1 9   ? 9.490   -15.108 -35.501 0.48 14.39 ? 450  GLN   A O   1 
ATOM   69   O  O   B GLN   A 1 9   ? 9.412   -14.721 -35.384 0.52 14.69 ? 450  GLN   A O   1 
ATOM   70   C  CB  A GLN   A 1 9   ? 9.472   -14.159 -38.437 0.48 17.35 ? 450  GLN   A CB  1 
ATOM   71   C  CB  B GLN   A 1 9   ? 9.479   -14.124 -38.502 0.52 16.14 ? 450  GLN   A CB  1 
ATOM   72   C  CG  A GLN   A 1 9   ? 9.834   -15.467 -39.117 0.48 16.12 ? 450  GLN   A CG  1 
ATOM   73   C  CG  B GLN   A 1 9   ? 8.019   -14.423 -38.149 0.52 18.00 ? 450  GLN   A CG  1 
ATOM   74   C  CD  A GLN   A 1 9   ? 9.004   -15.733 -40.365 0.48 28.49 ? 450  GLN   A CD  1 
ATOM   75   C  CD  B GLN   A 1 9   ? 7.809   -15.845 -37.636 0.52 28.82 ? 450  GLN   A CD  1 
ATOM   76   O  OE1 A GLN   A 1 9   ? 8.332   -14.840 -40.888 0.48 27.68 ? 450  GLN   A OE1 1 
ATOM   77   O  OE1 B GLN   A 1 9   ? 8.507   -16.772 -38.046 0.52 30.21 ? 450  GLN   A OE1 1 
ATOM   78   N  NE2 A GLN   A 1 9   ? 9.050   -16.968 -40.848 0.48 31.93 ? 450  GLN   A NE2 1 
ATOM   79   N  NE2 B GLN   A 1 9   ? 6.855   -16.016 -36.725 0.52 20.71 ? 450  GLN   A NE2 1 
ATOM   80   N  N   A ARG   A 1 10  ? 11.538  -15.697 -36.207 0.48 12.41 ? 451  ARG   A N   1 
ATOM   81   N  N   B ARG   A 1 10  ? 11.309  -15.629 -36.160 0.52 18.34 ? 451  ARG   A N   1 
ATOM   82   C  CA  A ARG   A 1 10  ? 11.640  -16.733 -35.183 0.48 16.82 ? 451  ARG   A CA  1 
ATOM   83   C  CA  B ARG   A 1 10  ? 11.266  -16.677 -35.146 0.52 14.26 ? 451  ARG   A CA  1 
ATOM   84   C  C   A ARG   A 1 10  ? 11.499  -16.163 -33.772 0.48 13.16 ? 451  ARG   A C   1 
ATOM   85   C  C   B ARG   A 1 10  ? 11.520  -16.174 -33.728 0.52 11.90 ? 451  ARG   A C   1 
ATOM   86   O  O   A ARG   A 1 10  ? 10.985  -16.845 -32.875 0.48 14.59 ? 451  ARG   A O   1 
ATOM   87   O  O   B ARG   A 1 10  ? 11.353  -16.950 -32.781 0.52 13.98 ? 451  ARG   A O   1 
ATOM   88   C  CB  A ARG   A 1 10  ? 12.962  -17.474 -35.318 0.48 18.13 ? 451  ARG   A CB  1 
ATOM   89   C  CB  B ARG   A 1 10  ? 12.232  -17.798 -35.500 0.52 15.28 ? 451  ARG   A CB  1 
ATOM   90   C  CG  A ARG   A 1 10  ? 13.053  -18.372 -36.535 0.48 21.77 ? 451  ARG   A CG  1 
ATOM   91   C  CG  B ARG   A 1 10  ? 11.719  -18.682 -36.604 0.52 15.54 ? 451  ARG   A CG  1 
ATOM   92   C  CD  A ARG   A 1 10  ? 14.246  -19.274 -36.391 0.48 28.02 ? 451  ARG   A CD  1 
ATOM   93   C  CD  B ARG   A 1 10  ? 12.688  -19.798 -36.868 0.52 17.87 ? 451  ARG   A CD  1 
ATOM   94   N  NE  A ARG   A 1 10  ? 15.454  -18.670 -36.938 0.48 23.78 ? 451  ARG   A NE  1 
ATOM   95   N  NE  B ARG   A 1 10  ? 12.984  -20.546 -35.656 0.52 23.17 ? 451  ARG   A NE  1 
ATOM   96   C  CZ  A ARG   A 1 10  ? 16.691  -18.993 -36.566 0.48 24.31 ? 451  ARG   A CZ  1 
ATOM   97   C  CZ  B ARG   A 1 10  ? 12.295  -21.604 -35.250 0.52 19.05 ? 451  ARG   A CZ  1 
ATOM   98   N  NH1 A ARG   A 1 10  ? 16.902  -19.912 -35.628 0.48 17.90 ? 451  ARG   A NH1 1 
ATOM   99   N  NH1 B ARG   A 1 10  ? 11.283  -22.051 -35.971 0.52 18.73 ? 451  ARG   A NH1 1 
ATOM   100  N  NH2 A ARG   A 1 10  ? 17.723  -18.383 -37.133 0.48 22.98 ? 451  ARG   A NH2 1 
ATOM   101  N  NH2 B ARG   A 1 10  ? 12.631  -22.210 -34.120 0.52 20.51 ? 451  ARG   A NH2 1 
ATOM   102  N  N   . MET   A 1 11  ? 11.935  -14.916 -33.560 1.00 14.50 ? 452  MET   A N   1 
ATOM   103  C  CA  . MET   A 1 11  ? 11.893  -14.327 -32.229 1.00 14.18 ? 452  MET   A CA  1 
ATOM   104  C  C   . MET   A 1 11  ? 10.461  -14.090 -31.762 1.00 14.62 ? 452  MET   A C   1 
ATOM   105  O  O   . MET   A 1 11  ? 10.254  -13.767 -30.592 1.00 14.47 ? 452  MET   A O   1 
ATOM   106  C  CB  . MET   A 1 11  ? 12.697  -13.029 -32.190 1.00 14.34 ? 452  MET   A CB  1 
ATOM   107  C  CG  . MET   A 1 11  ? 14.196  -13.254 -31.986 1.00 13.08 ? 452  MET   A CG  1 
ATOM   108  S  SD  . MET   A 1 11  ? 15.162  -11.734 -32.082 1.00 14.41 ? 452  MET   A SD  1 
ATOM   109  C  CE  . MET   A 1 11  ? 14.992  -11.324 -33.856 1.00 17.55 ? 452  MET   A CE  1 
ATOM   110  N  N   . MET   A 1 12  ? 9.469   -14.257 -32.641 1.00 14.40 ? 453  MET   A N   1 
ATOM   111  C  CA  . MET   A 1 12  ? 8.076   -14.199 -32.220 1.00 14.20 ? 453  MET   A CA  1 
ATOM   112  C  C   . MET   A 1 12  ? 7.633   -15.419 -31.430 1.00 16.14 ? 453  MET   A C   1 
ATOM   113  O  O   . MET   A 1 12  ? 6.550   -15.376 -30.842 1.00 16.71 ? 453  MET   A O   1 
ATOM   114  C  CB  . MET   A 1 12  ? 7.144   -14.062 -33.435 1.00 14.72 ? 453  MET   A CB  1 
ATOM   115  C  CG  . MET   A 1 12  ? 7.310   -12.759 -34.202 1.00 14.27 ? 453  MET   A CG  1 
ATOM   116  S  SD  . MET   A 1 12  ? 6.224   -12.665 -35.651 1.00 20.18 ? 453  MET   A SD  1 
ATOM   117  C  CE  . MET   A 1 12  ? 4.626   -12.580 -34.859 1.00 24.29 ? 453  MET   A CE  1 
ATOM   118  N  N   . LEU   A 1 13  ? 8.434   -16.491 -31.386 1.00 14.83 ? 454  LEU   A N   1 
ATOM   119  C  CA  . LEU   A 1 13  ? 7.935   -17.761 -30.849 1.00 16.74 ? 454  LEU   A CA  1 
ATOM   120  C  C   . LEU   A 1 13  ? 7.839   -17.754 -29.325 1.00 16.75 ? 454  LEU   A C   1 
ATOM   121  O  O   . LEU   A 1 13  ? 7.032   -18.496 -28.742 1.00 16.01 ? 454  LEU   A O   1 
ATOM   122  C  CB  . LEU   A 1 13  ? 8.801   -18.922 -31.337 1.00 17.27 ? 454  LEU   A CB  1 
ATOM   123  C  CG  . LEU   A 1 13  ? 8.705   -19.167 -32.842 1.00 16.64 ? 454  LEU   A CG  1 
ATOM   124  C  CD1 . LEU   A 1 13  ? 9.739   -20.176 -33.265 1.00 22.13 ? 454  LEU   A CD1 1 
ATOM   125  C  CD2 . LEU   A 1 13  ? 7.306   -19.640 -33.202 1.00 20.22 ? 454  LEU   A CD2 1 
ATOM   126  N  N   . HIS   A 1 14  ? 8.646   -16.933 -28.660 1.00 14.12 ? 455  HIS   A N   1 
ATOM   127  C  CA  . HIS   A 1 14  ? 8.520   -16.725 -27.223 1.00 13.93 ? 455  HIS   A CA  1 
ATOM   128  C  C   . HIS   A 1 14  ? 7.144   -16.140 -26.906 1.00 14.63 ? 455  HIS   A C   1 
ATOM   129  O  O   . HIS   A 1 14  ? 6.761   -15.112 -27.468 1.00 14.14 ? 455  HIS   A O   1 
ATOM   130  C  CB  . HIS   A 1 14  ? 9.645   -15.763 -26.826 1.00 12.51 ? 455  HIS   A CB  1 
ATOM   131  C  CG  . HIS   A 1 14  ? 9.510   -15.156 -25.463 1.00 11.30 ? 455  HIS   A CG  1 
ATOM   132  N  ND1 . HIS   A 1 14  ? 9.493   -15.903 -24.301 1.00 13.25 ? 455  HIS   A ND1 1 
ATOM   133  C  CD2 . HIS   A 1 14  ? 9.470   -13.856 -25.069 1.00 13.94 ? 455  HIS   A CD2 1 
ATOM   134  C  CE1 . HIS   A 1 14  ? 9.415   -15.092 -23.254 1.00 13.19 ? 455  HIS   A CE1 1 
ATOM   135  N  NE2 . HIS   A 1 14  ? 9.397   -13.844 -23.697 1.00 13.77 ? 455  HIS   A NE2 1 
ATOM   136  N  N   . HIS   A 1 15  ? 6.383   -16.799 -26.030 1.00 13.43 ? 456  HIS   A N   1 
ATOM   137  C  CA  . HIS   A 1 15  ? 4.998   -16.386 -25.815 1.00 14.92 ? 456  HIS   A CA  1 
ATOM   138  C  C   . HIS   A 1 15  ? 4.576   -16.767 -24.402 1.00 14.14 ? 456  HIS   A C   1 
ATOM   139  O  O   . HIS   A 1 15  ? 5.222   -17.578 -23.730 1.00 14.49 ? 456  HIS   A O   1 
ATOM   140  C  CB  . HIS   A 1 15  ? 4.048   -17.003 -26.854 1.00 14.60 ? 456  HIS   A CB  1 
ATOM   141  C  CG  . HIS   A 1 15  ? 3.878   -18.479 -26.694 1.00 15.18 ? 456  HIS   A CG  1 
ATOM   142  N  ND1 . HIS   A 1 15  ? 4.832   -19.387 -27.100 1.00 20.82 ? 456  HIS   A ND1 1 
ATOM   143  C  CD2 . HIS   A 1 15  ? 2.892   -19.203 -26.112 1.00 20.59 ? 456  HIS   A CD2 1 
ATOM   144  C  CE1 . HIS   A 1 15  ? 4.421   -20.611 -26.809 1.00 22.62 ? 456  HIS   A CE1 1 
ATOM   145  N  NE2 . HIS   A 1 15  ? 3.247   -20.527 -26.209 1.00 22.16 ? 456  HIS   A NE2 1 
ATOM   146  N  N   . ASN   A 1 16  ? 3.497   -16.130 -23.944 1.00 14.58 ? 457  ASN   A N   1 
ATOM   147  C  CA  . ASN   A 1 16  ? 2.962   -16.302 -22.591 1.00 15.92 ? 457  ASN   A CA  1 
ATOM   148  C  C   . ASN   A 1 16  ? 1.762   -17.246 -22.656 1.00 17.71 ? 457  ASN   A C   1 
ATOM   149  O  O   . ASN   A 1 16  ? 0.695   -16.879 -23.164 1.00 17.87 ? 457  ASN   A O   1 
ATOM   150  C  CB  . ASN   A 1 16  ? 2.567   -14.949 -22.008 1.00 14.61 ? 457  ASN   A CB  1 
ATOM   151  C  CG  . ASN   A 1 16  ? 2.181   -15.036 -20.547 1.00 16.36 ? 457  ASN   A CG  1 
ATOM   152  O  OD1 . ASN   A 1 16  ? 1.648   -16.051 -20.089 1.00 17.58 ? 457  ASN   A OD1 1 
ATOM   153  N  ND2 . ASN   A 1 16  ? 2.438   -13.975 -19.808 1.00 14.38 ? 457  ASN   A ND2 1 
ATOM   154  N  N   . MET   A 1 17  ? 1.950   -18.461 -22.147 1.00 16.61 ? 458  MET   A N   1 
ATOM   155  C  CA  . MET   A 1 17  ? 0.954   -19.514 -22.312 1.00 19.37 ? 458  MET   A CA  1 
ATOM   156  C  C   . MET   A 1 17  ? -0.269  -19.275 -21.430 1.00 21.86 ? 458  MET   A C   1 
ATOM   157  O  O   . MET   A 1 17  ? -1.358  -19.764 -21.745 1.00 25.06 ? 458  MET   A O   1 
ATOM   158  C  CB  . MET   A 1 17  ? 1.585   -20.866 -21.961 1.00 27.47 ? 458  MET   A CB  1 
ATOM   159  C  CG  . MET   A 1 17  ? 2.754   -21.327 -22.846 1.00 51.51 ? 458  MET   A CG  1 
ATOM   160  S  SD  . MET   A 1 17  ? 3.702   -22.630 -22.008 1.00 54.18 ? 458  MET   A SD  1 
ATOM   161  C  CE  . MET   A 1 17  ? 2.406   -23.319 -20.959 1.00 18.59 ? 458  MET   A CE  1 
ATOM   162  N  N   . TRP   A 1 18  ? -0.111  -18.557 -20.321 1.00 18.56 ? 459  TRP   A N   1 
ATOM   163  C  CA  . TRP   A 1 18  ? -1.212  -18.308 -19.392 1.00 19.15 ? 459  TRP   A CA  1 
ATOM   164  C  C   . TRP   A 1 18  ? -1.972  -17.023 -19.691 1.00 31.93 ? 459  TRP   A C   1 
ATOM   165  O  O   . TRP   A 1 18  ? -3.158  -16.921 -19.352 1.00 22.99 ? 459  TRP   A O   1 
ATOM   166  C  CB  . TRP   A 1 18  ? -0.689  -18.317 -17.946 1.00 25.81 ? 459  TRP   A CB  1 
ATOM   167  C  CG  . TRP   A 1 18  ? 0.137   -19.539 -17.683 1.00 44.11 ? 459  TRP   A CG  1 
ATOM   168  C  CD1 . TRP   A 1 18  ? -0.304  -20.740 -17.216 1.00 32.52 ? 459  TRP   A CD1 1 
ATOM   169  C  CD2 . TRP   A 1 18  ? 1.540   -19.697 -17.937 1.00 53.57 ? 459  TRP   A CD2 1 
ATOM   170  N  NE1 . TRP   A 1 18  ? 0.738   -21.638 -17.157 1.00 42.41 ? 459  TRP   A NE1 1 
ATOM   171  C  CE2 . TRP   A 1 18  ? 1.882   -21.017 -17.581 1.00 45.96 ? 459  TRP   A CE2 1 
ATOM   172  C  CE3 . TRP   A 1 18  ? 2.542   -18.843 -18.413 1.00 27.43 ? 459  TRP   A CE3 1 
ATOM   173  C  CZ2 . TRP   A 1 18  ? 3.179   -21.509 -17.701 1.00 41.52 ? 459  TRP   A CZ2 1 
ATOM   174  C  CZ3 . TRP   A 1 18  ? 3.832   -19.330 -18.518 1.00 28.95 ? 459  TRP   A CZ3 1 
ATOM   175  C  CH2 . TRP   A 1 18  ? 4.138   -20.653 -18.172 1.00 25.61 ? 459  TRP   A CH2 1 
ATOM   176  N  N   . ASP   A 1 19  ? -1.341  -16.066 -20.366 1.00 23.76 ? 460  ASP   A N   1 
ATOM   177  C  CA  . ASP   A 1 19  ? -1.906  -14.737 -20.598 1.00 18.88 ? 460  ASP   A CA  1 
ATOM   178  C  C   . ASP   A 1 19  ? -1.459  -14.310 -21.994 1.00 20.02 ? 460  ASP   A C   1 
ATOM   179  O  O   . ASP   A 1 19  ? -0.450  -13.611 -22.163 1.00 18.87 ? 460  ASP   A O   1 
ATOM   180  C  CB  . ASP   A 1 19  ? -1.417  -13.768 -19.529 1.00 17.64 ? 460  ASP   A CB  1 
ATOM   181  C  CG  . ASP   A 1 19  ? -1.873  -12.354 -19.770 1.00 18.95 ? 460  ASP   A CG  1 
ATOM   182  O  OD1 . ASP   A 1 19  ? -2.755  -12.124 -20.627 1.00 20.14 ? 460  ASP   A OD1 1 
ATOM   183  O  OD2 . ASP   A 1 19  ? -1.304  -11.476 -19.087 1.00 22.16 ? 460  ASP   A OD2 1 
ATOM   184  N  N   . SER   A 1 20  ? -2.208  -14.743 -23.005 1.00 21.38 ? 461  SER   A N   1 
ATOM   185  C  CA  . SER   A 1 20  ? -1.788  -14.501 -24.377 1.00 21.55 ? 461  SER   A CA  1 
ATOM   186  C  C   . SER   A 1 20  ? -1.879  -13.037 -24.781 1.00 24.00 ? 461  SER   A C   1 
ATOM   187  O  O   . SER   A 1 20  ? -1.316  -12.671 -25.816 1.00 22.02 ? 461  SER   A O   1 
ATOM   188  C  CB  . SER   A 1 20  ? -2.588  -15.361 -25.352 1.00 23.64 ? 461  SER   A CB  1 
ATOM   189  O  OG  . SER   A 1 20  ? -3.962  -15.036 -25.274 1.00 26.15 ? 461  SER   A OG  1 
ATOM   190  N  N   . HIS   A 1 21  ? -2.559  -12.200 -24.001 1.00 20.90 ? 462  HIS   A N   1 
ATOM   191  C  CA  . HIS   A 1 21  ? -2.611  -10.768 -24.252 1.00 17.79 ? 462  HIS   A CA  1 
ATOM   192  C  C   . HIS   A 1 21  ? -1.593  -9.987  -23.433 1.00 16.22 ? 462  HIS   A C   1 
ATOM   193  O  O   . HIS   A 1 21  ? -1.660  -8.754  -23.383 1.00 18.00 ? 462  HIS   A O   1 
ATOM   194  C  CB  . HIS   A 1 21  ? -4.023  -10.243 -24.004 1.00 20.43 ? 462  HIS   A CB  1 
ATOM   195  C  CG  . HIS   A 1 21  ? -5.044  -10.860 -24.901 1.00 32.01 ? 462  HIS   A CG  1 
ATOM   196  N  ND1 . HIS   A 1 21  ? -5.487  -10.249 -26.053 1.00 47.47 ? 462  HIS   A ND1 1 
ATOM   197  C  CD2 . HIS   A 1 21  ? -5.685  -12.050 -24.833 1.00 33.85 ? 462  HIS   A CD2 1 
ATOM   198  C  CE1 . HIS   A 1 21  ? -6.364  -11.032 -26.653 1.00 45.17 ? 462  HIS   A CE1 1 
ATOM   199  N  NE2 . HIS   A 1 21  ? -6.502  -12.131 -25.934 1.00 35.06 ? 462  HIS   A NE2 1 
ATOM   200  N  N   . HIS   A 1 22  ? -0.665  -10.676 -22.775 1.00 16.57 ? 463  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 22  ? 0.400   -9.990  -22.059 1.00 15.89 ? 463  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 22  ? 1.095   -9.003  -23.000 1.00 15.26 ? 463  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 22  ? 1.371   -9.347  -24.149 1.00 17.63 ? 463  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 22  ? 1.430   -11.017 -21.579 1.00 15.96 ? 463  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 22  ? 2.506   -10.441 -20.721 1.00 15.63 ? 463  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 22  ? 3.568   -9.714  -21.230 1.00 14.46 ? 463  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 22  ? 2.708   -10.511 -19.386 1.00 16.96 ? 463  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 22  ? 4.363   -9.352  -20.238 1.00 17.06 ? 463  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 22  ? 3.860   -9.819  -19.108 1.00 19.19 ? 463  HIS   A NE2 1 
ATOM   210  N  N   . PRO   A 1 23  ? 1.424   -7.794  -22.536 1.00 14.74 ? 464  PRO   A N   1 
ATOM   211  C  CA  . PRO   A 1 23  ? 1.889   -6.742  -23.464 1.00 14.87 ? 464  PRO   A CA  1 
ATOM   212  C  C   . PRO   A 1 23  ? 3.198   -7.032  -24.185 1.00 14.12 ? 464  PRO   A C   1 
ATOM   213  O  O   . PRO   A 1 23  ? 3.444   -6.413  -25.225 1.00 13.72 ? 464  PRO   A O   1 
ATOM   214  C  CB  . PRO   A 1 23  ? 2.012   -5.504  -22.560 1.00 20.93 ? 464  PRO   A CB  1 
ATOM   215  C  CG  . PRO   A 1 23  ? 2.133   -6.058  -21.164 1.00 18.75 ? 464  PRO   A CG  1 
ATOM   216  C  CD  . PRO   A 1 23  ? 1.181   -7.251  -21.189 1.00 16.94 ? 464  PRO   A CD  1 
ATOM   217  N  N   . GLU   A 1 24  ? 4.069   -7.901  -23.659 1.00 13.20 ? 465  GLU   A N   1 
ATOM   218  C  CA  . GLU   A 1 24  ? 5.329   -8.191  -24.350 1.00 12.62 ? 465  GLU   A CA  1 
ATOM   219  C  C   . GLU   A 1 24  ? 5.033   -9.233  -25.418 1.00 14.08 ? 465  GLU   A C   1 
ATOM   220  O  O   . GLU   A 1 24  ? 5.372   -10.415 -25.306 1.00 13.82 ? 465  GLU   A O   1 
ATOM   221  C  CB  . GLU   A 1 24  ? 6.383   -8.678  -23.370 1.00 12.23 ? 465  GLU   A CB  1 
ATOM   222  C  CG  . GLU   A 1 24  ? 7.847   -8.440  -23.829 1.00 13.69 ? 465  GLU   A CG  1 
ATOM   223  C  CD  . GLU   A 1 24  ? 8.245   -9.282  -25.031 1.00 13.78 ? 465  GLU   A CD  1 
ATOM   224  O  OE1 . GLU   A 1 24  ? 8.650   -10.454 -24.828 1.00 16.31 ? 465  GLU   A OE1 1 
ATOM   225  O  OE2 . GLU   A 1 24  ? 8.159   -8.794  -26.179 1.00 14.39 ? 465  GLU   A OE2 1 
ATOM   226  N  N   . LEU   A 1 25  ? 4.352   -8.767  -26.456 1.00 12.52 ? 466  LEU   A N   1 
ATOM   227  C  CA  . LEU   A 1 25  ? 3.733   -9.599  -27.480 1.00 13.70 ? 466  LEU   A CA  1 
ATOM   228  C  C   . LEU   A 1 25  ? 4.709   -9.994  -28.590 1.00 12.97 ? 466  LEU   A C   1 
ATOM   229  O  O   . LEU   A 1 25  ? 5.536   -9.181  -29.029 1.00 12.75 ? 466  LEU   A O   1 
ATOM   230  C  CB  . LEU   A 1 25  ? 2.596   -8.849  -28.154 1.00 15.38 ? 466  LEU   A CB  1 
ATOM   231  C  CG  . LEU   A 1 25  ? 1.315   -8.631  -27.349 1.00 16.54 ? 466  LEU   A CG  1 
ATOM   232  C  CD1 . LEU   A 1 25  ? 0.420   -7.654  -28.108 1.00 18.63 ? 466  LEU   A CD1 1 
ATOM   233  C  CD2 . LEU   A 1 25  ? 0.613   -9.957  -27.160 1.00 16.72 ? 466  LEU   A CD2 1 
ATOM   234  N  N   . PRO   A 1 26  ? 4.550   -11.207 -29.130 1.00 13.18 ? 467  PRO   A N   1 
ATOM   235  C  CA  . PRO   A 1 26  ? 5.242   -11.577 -30.373 1.00 15.26 ? 467  PRO   A CA  1 
ATOM   236  C  C   . PRO   A 1 26  ? 5.141   -10.524 -31.468 1.00 14.33 ? 467  PRO   A C   1 
ATOM   237  O  O   . PRO   A 1 26  ? 6.143   -10.244 -32.141 1.00 15.09 ? 467  PRO   A O   1 
ATOM   238  C  CB  . PRO   A 1 26  ? 4.532   -12.882 -30.766 1.00 14.97 ? 467  PRO   A CB  1 
ATOM   239  C  CG  . PRO   A 1 26  ? 4.122   -13.480 -29.454 1.00 15.49 ? 467  PRO   A CG  1 
ATOM   240  C  CD  . PRO   A 1 26  ? 3.739   -12.320 -28.591 1.00 14.18 ? 467  PRO   A CD  1 
ATOM   241  N  N   . GLN   A 1 27  ? 3.973   -9.900  -31.635 1.00 14.82 ? 468  GLN   A N   1 
ATOM   242  C  CA  . GLN   A 1 27  ? 3.794   -8.970  -32.732 1.00 14.65 ? 468  GLN   A CA  1 
ATOM   243  C  C   . GLN   A 1 27  ? 4.498   -7.637  -32.526 1.00 13.33 ? 468  GLN   A C   1 
ATOM   244  O  O   . GLN   A 1 27  ? 4.506   -6.829  -33.468 1.00 13.62 ? 468  GLN   A O   1 
ATOM   245  C  CB  . GLN   A 1 27  ? 2.309   -8.772  -33.052 1.00 17.33 ? 468  GLN   A CB  1 
ATOM   246  C  CG  . GLN   A 1 27  ? 1.410   -8.498  -31.884 1.00 25.08 ? 468  GLN   A CG  1 
ATOM   247  C  CD  . GLN   A 1 27  ? 0.754   -9.762  -31.340 1.00 35.25 ? 468  GLN   A CD  1 
ATOM   248  O  OE1 . GLN   A 1 27  ? 1.436   -10.748 -31.044 1.00 18.35 ? 468  GLN   A OE1 1 
ATOM   249  N  NE2 . GLN   A 1 27  ? -0.582  -9.739  -31.208 1.00 24.12 ? 468  GLN   A NE2 1 
ATOM   250  N  N   . ARG   A 1 28  ? 5.135   -7.393  -31.379 1.00 11.03 ? 469  ARG   A N   1 
ATOM   251  C  CA  . ARG   A 1 28  ? 5.913   -6.166  -31.244 1.00 10.83 ? 469  ARG   A CA  1 
ATOM   252  C  C   . ARG   A 1 28  ? 6.942   -6.066  -32.369 1.00 12.39 ? 469  ARG   A C   1 
ATOM   253  O  O   . ARG   A 1 28  ? 7.061   -5.026  -33.039 1.00 11.99 ? 469  ARG   A O   1 
ATOM   254  C  CB  . ARG   A 1 28  ? 6.594   -6.145  -29.872 1.00 11.50 ? 469  ARG   A CB  1 
ATOM   255  C  CG  . ARG   A 1 28  ? 5.634   -5.907  -28.711 1.00 12.83 ? 469  ARG   A CG  1 
ATOM   256  C  CD  . ARG   A 1 28  ? 6.324   -6.088  -27.364 1.00 12.56 ? 469  ARG   A CD  1 
ATOM   257  N  NE  . ARG   A 1 28  ? 7.298   -5.030  -27.193 1.00 13.60 ? 469  ARG   A NE  1 
ATOM   258  C  CZ  . ARG   A 1 28  ? 8.617   -5.198  -27.115 1.00 14.03 ? 469  ARG   A CZ  1 
ATOM   259  N  NH1 . ARG   A 1 28  ? 9.157   -6.420  -27.127 1.00 13.70 ? 469  ARG   A NH1 1 
ATOM   260  N  NH2 . ARG   A 1 28  ? 9.404   -4.122  -27.042 1.00 13.33 ? 469  ARG   A NH2 1 
ATOM   261  N  N   . ILE   A 1 29  ? 7.679   -7.156  -32.609 1.00 11.14 ? 470  ILE   A N   1 
ATOM   262  C  CA  . ILE   A 1 29  ? 8.741   -7.092  -33.607 1.00 11.72 ? 470  ILE   A CA  1 
ATOM   263  C  C   . ILE   A 1 29  ? 8.191   -7.157  -35.031 1.00 11.71 ? 470  ILE   A C   1 
ATOM   264  O  O   . ILE   A 1 29  ? 8.710   -6.496  -35.934 1.00 11.07 ? 470  ILE   A O   1 
ATOM   265  C  CB  . ILE   A 1 29  ? 9.859   -8.126  -33.352 1.00 14.22 ? 470  ILE   A CB  1 
ATOM   266  C  CG1 . ILE   A 1 29  ? 9.327   -9.577  -33.355 1.00 11.80 ? 470  ILE   A CG1 1 
ATOM   267  C  CG2 . ILE   A 1 29  ? 10.609  -7.759  -32.063 1.00 11.78 ? 470  ILE   A CG2 1 
ATOM   268  C  CD1 . ILE   A 1 29  ? 10.410  -10.622 -33.460 1.00 15.06 ? 470  ILE   A CD1 1 
ATOM   269  N  N   . SER   A 1 30  ? 7.175   -7.973  -35.279 1.00 12.42 ? 471  SER   A N   1 
ATOM   270  C  CA  . SER   A 1 30  ? 6.645   -8.016  -36.638 1.00 14.97 ? 471  SER   A CA  1 
ATOM   271  C  C   . SER   A 1 30  ? 5.998   -6.694  -37.027 1.00 12.72 ? 471  SER   A C   1 
ATOM   272  O  O   . SER   A 1 30  ? 6.073   -6.291  -38.190 1.00 12.75 ? 471  SER   A O   1 
ATOM   273  C  CB  . SER   A 1 30  ? 5.682   -9.188  -36.830 1.00 16.44 ? 471  SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 30  ? 4.611   -9.089  -35.925 1.00 17.99 ? 471  SER   A OG  1 
ATOM   275  N  N   . ARG   A 1 31  ? 5.396   -5.989  -36.067 1.00 12.80 ? 472  ARG   A N   1 
ATOM   276  C  CA  . ARG   A 1 31  ? 4.786   -4.702  -36.396 1.00 12.33 ? 472  ARG   A CA  1 
ATOM   277  C  C   . ARG   A 1 31  ? 5.844   -3.664  -36.736 1.00 11.88 ? 472  ARG   A C   1 
ATOM   278  O  O   . ARG   A 1 31  ? 5.684   -2.886  -37.685 1.00 11.93 ? 472  ARG   A O   1 
ATOM   279  C  CB  . ARG   A 1 31  ? 3.911   -4.227  -35.247 1.00 11.80 ? 472  ARG   A CB  1 
ATOM   280  C  CG  . ARG   A 1 31  ? 2.548   -4.956  -35.204 1.00 12.59 ? 472  ARG   A CG  1 
ATOM   281  C  CD  . ARG   A 1 31  ? 1.630   -4.493  -36.364 1.00 12.92 ? 472  ARG   A CD  1 
ATOM   282  N  NE  . ARG   A 1 31  ? 1.356   -3.063  -36.242 1.00 12.29 ? 472  ARG   A NE  1 
ATOM   283  C  CZ  . ARG   A 1 31  ? 0.420   -2.543  -35.450 1.00 13.49 ? 472  ARG   A CZ  1 
ATOM   284  N  NH1 . ARG   A 1 31  ? -0.358  -3.337  -34.719 1.00 12.79 ? 472  ARG   A NH1 1 
ATOM   285  N  NH2 . ARG   A 1 31  ? 0.271   -1.230  -35.377 1.00 14.89 ? 472  ARG   A NH2 1 
ATOM   286  N  N   . ILE   A 1 32  ? 6.936   -3.637  -35.973 1.00 12.18 ? 473  ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 32  ? 8.010   -2.698  -36.278 1.00 12.57 ? 473  ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 32  ? 8.594   -2.993  -37.654 1.00 11.47 ? 473  ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 32  ? 8.783   -2.087  -38.473 1.00 11.81 ? 473  ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 32  ? 9.081   -2.732  -35.173 1.00 11.10 ? 473  ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 32  ? 8.528   -2.181  -33.853 1.00 10.32 ? 473  ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 32  ? 10.308  -1.924  -35.607 1.00 14.65 ? 473  ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 32  ? 9.378   -2.596  -32.665 1.00 11.83 ? 473  ILE   A CD1 1 
ATOM   294  N  N   . PHE   A 1 33  ? 8.830   -4.275  -37.942 1.00 11.53 ? 474  PHE   A N   1 
ATOM   295  C  CA  . PHE   A 1 33  ? 9.362   -4.664  -39.248 1.00 12.49 ? 474  PHE   A CA  1 
ATOM   296  C  C   . PHE   A 1 33  ? 8.412   -4.242  -40.373 1.00 12.58 ? 474  PHE   A C   1 
ATOM   297  O  O   . PHE   A 1 33  ? 8.836   -3.672  -41.387 1.00 14.30 ? 474  PHE   A O   1 
ATOM   298  C  CB  . PHE   A 1 33  ? 9.588   -6.174  -39.274 1.00 13.21 ? 474  PHE   A CB  1 
ATOM   299  C  CG  . PHE   A 1 33  ? 10.241  -6.694  -40.550 1.00 14.63 ? 474  PHE   A CG  1 
ATOM   300  C  CD1 . PHE   A 1 33  ? 11.588  -6.508  -40.790 1.00 14.23 ? 474  PHE   A CD1 1 
ATOM   301  C  CD2 . PHE   A 1 33  ? 9.494   -7.384  -41.488 1.00 15.91 ? 474  PHE   A CD2 1 
ATOM   302  C  CE1 . PHE   A 1 33  ? 12.183  -7.001  -41.936 1.00 18.37 ? 474  PHE   A CE1 1 
ATOM   303  C  CE2 . PHE   A 1 33  ? 10.080  -7.877  -42.639 1.00 19.08 ? 474  PHE   A CE2 1 
ATOM   304  C  CZ  . PHE   A 1 33  ? 11.427  -7.681  -42.862 1.00 18.63 ? 474  PHE   A CZ  1 
ATOM   305  N  N   . SER   A 1 34  ? 7.106   -4.498  -40.185 1.00 13.92 ? 475  SER   A N   1 
ATOM   306  C  CA  . SER   A 1 34  ? 6.102   -4.137  -41.180 1.00 16.67 ? 475  SER   A CA  1 
ATOM   307  C  C   . SER   A 1 34  ? 6.101   -2.640  -41.443 1.00 12.84 ? 475  SER   A C   1 
ATOM   308  O  O   . SER   A 1 34  ? 6.003   -2.202  -42.593 1.00 13.36 ? 475  SER   A O   1 
ATOM   309  C  CB  . SER   A 1 34  ? 4.728   -4.571  -40.669 1.00 16.10 ? 475  SER   A CB  1 
ATOM   310  O  OG  . SER   A 1 34  ? 3.722   -4.119  -41.564 1.00 16.14 ? 475  SER   A OG  1 
ATOM   311  N  N   . ARG   A 1 35  ? 6.203   -1.834  -40.383 1.00 11.39 ? 476  ARG   A N   1 
ATOM   312  C  CA  . ARG   A 1 35  ? 6.231   -0.392  -40.584 1.00 13.63 ? 476  ARG   A CA  1 
ATOM   313  C  C   . ARG   A 1 35  ? 7.453   0.035   -41.402 1.00 13.11 ? 476  ARG   A C   1 
ATOM   314  O  O   . ARG   A 1 35  ? 7.360   0.936   -42.246 1.00 12.90 ? 476  ARG   A O   1 
ATOM   315  C  CB  . ARG   A 1 35  ? 6.121   0.343   -39.246 1.00 12.33 ? 476  ARG   A CB  1 
ATOM   316  C  CG  . ARG   A 1 35  ? 5.949   1.838   -39.366 1.00 13.19 ? 476  ARG   A CG  1 
ATOM   317  C  CD  . ARG   A 1 35  ? 4.564   2.214   -39.844 1.00 20.57 ? 476  ARG   A CD  1 
ATOM   318  N  NE  . ARG   A 1 35  ? 4.393   3.665   -39.871 1.00 18.84 ? 476  ARG   A NE  1 
ATOM   319  C  CZ  . ARG   A 1 35  ? 3.868   4.332   -40.893 1.00 16.47 ? 476  ARG   A CZ  1 
ATOM   320  N  NH1 . ARG   A 1 35  ? 3.455   3.678   -41.968 1.00 18.69 ? 476  ARG   A NH1 1 
ATOM   321  N  NH2 . ARG   A 1 35  ? 3.748   5.646   -40.825 1.00 19.22 ? 476  ARG   A NH2 1 
ATOM   322  N  N   . HIS   A 1 36  ? 8.606   -0.623  -41.199 1.00 12.40 ? 477  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 36  ? 9.777   -0.309  -42.011 1.00 12.88 ? 477  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 36  ? 9.517   -0.625  -43.488 1.00 14.36 ? 477  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 36  ? 9.930   0.131   -44.382 1.00 14.03 ? 477  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 36  ? 10.986  -1.109  -41.526 1.00 14.07 ? 477  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 36  ? 11.678  -0.529  -40.330 1.00 14.90 ? 477  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 36  ? 11.184  -0.667  -39.052 1.00 13.13 ? 477  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 36  ? 12.848  0.153   -40.216 1.00 14.25 ? 477  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 36  ? 12.020  -0.089  -38.200 1.00 13.46 ? 477  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 36  ? 13.033  0.426   -38.881 1.00 13.43 ? 477  HIS   A NE2 1 
ATOM   332  N  N   . GLU   A 1 37  ? 8.866   -1.756  -43.768 1.00 14.11 ? 478  GLU   A N   1 
ATOM   333  C  CA  . GLU   A 1 37  ? 8.518   -2.067  -45.153 1.00 15.91 ? 478  GLU   A CA  1 
ATOM   334  C  C   . GLU   A 1 37  ? 7.511   -1.072  -45.714 1.00 16.63 ? 478  GLU   A C   1 
ATOM   335  O  O   . GLU   A 1 37  ? 7.691   -0.563  -46.824 1.00 16.46 ? 478  GLU   A O   1 
ATOM   336  C  CB  . GLU   A 1 37  ? 8.007   -3.506  -45.258 1.00 17.09 ? 478  GLU   A CB  1 
ATOM   337  C  CG  . GLU   A 1 37  ? 7.935   -4.035  -46.682 1.00 22.20 ? 478  GLU   A CG  1 
ATOM   338  C  CD  . GLU   A 1 37  ? 7.347   -5.416  -46.782 1.00 55.73 ? 478  GLU   A CD  1 
ATOM   339  O  OE1 . GLU   A 1 37  ? 6.131   -5.568  -46.521 1.00 49.77 ? 478  GLU   A OE1 1 
ATOM   340  O  OE2 . GLU   A 1 37  ? 8.098   -6.351  -47.130 1.00 60.50 ? 478  GLU   A OE2 1 
ATOM   341  N  N   . GLU   A 1 38  ? 6.489   -0.738  -44.925 1.00 15.37 ? 479  GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 38  ? 5.431   0.175   -45.348 1.00 16.99 ? 479  GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 38  ? 5.975   1.549   -45.709 1.00 14.59 ? 479  GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 38  ? 5.482   2.188   -46.648 1.00 18.49 ? 479  GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 38  ? 4.467   0.324   -44.176 1.00 19.36 ? 479  GLU   A CB  1 
ATOM   346  C  CG  . GLU   A 1 38  ? 3.033   0.454   -44.457 1.00 30.04 ? 479  GLU   A CG  1 
ATOM   347  C  CD  . GLU   A 1 38  ? 2.264   0.286   -43.165 1.00 17.57 ? 479  GLU   A CD  1 
ATOM   348  O  OE1 . GLU   A 1 38  ? 2.655   0.916   -42.163 1.00 18.39 ? 479  GLU   A OE1 1 
ATOM   349  O  OE2 . GLU   A 1 38  ? 1.305   -0.494  -43.147 1.00 23.49 ? 479  GLU   A OE2 1 
ATOM   350  N  N   . LEU   A 1 39  ? 6.972   2.036   -44.964 1.00 15.08 ? 480  LEU   A N   1 
ATOM   351  C  CA  . LEU   A 1 39  ? 7.599   3.321   -45.234 1.00 15.82 ? 480  LEU   A CA  1 
ATOM   352  C  C   . LEU   A 1 39  ? 8.750   3.218   -46.237 1.00 16.78 ? 480  LEU   A C   1 
ATOM   353  O  O   . LEU   A 1 39  ? 9.422   4.228   -46.496 1.00 18.72 ? 480  LEU   A O   1 
ATOM   354  C  CB  . LEU   A 1 39  ? 8.117   3.945   -43.934 1.00 16.84 ? 480  LEU   A CB  1 
ATOM   355  C  CG  . LEU   A 1 39  ? 7.043   4.329   -42.908 1.00 14.47 ? 480  LEU   A CG  1 
ATOM   356  C  CD1 . LEU   A 1 39  ? 7.669   4.640   -41.551 1.00 16.43 ? 480  LEU   A CD1 1 
ATOM   357  C  CD2 . LEU   A 1 39  ? 6.267   5.537   -43.403 1.00 19.61 ? 480  LEU   A CD2 1 
ATOM   358  N  N   . ARG   A 1 40  ? 9.008   2.024   -46.779 1.00 15.59 ? 481  ARG   A N   1 
ATOM   359  C  CA  . ARG   A 1 40  ? 10.066  1.808   -47.781 1.00 14.91 ? 481  ARG   A CA  1 
ATOM   360  C  C   . ARG   A 1 40  ? 11.464  2.067   -47.217 1.00 20.18 ? 481  ARG   A C   1 
ATOM   361  O  O   . ARG   A 1 40  ? 12.399  2.385   -47.958 1.00 20.69 ? 481  ARG   A O   1 
ATOM   362  C  CB  . ARG   A 1 40  ? 9.809   2.576   -49.086 1.00 22.00 ? 481  ARG   A CB  1 
ATOM   363  C  CG  . ARG   A 1 40  ? 8.508   2.162   -49.754 1.00 21.24 ? 481  ARG   A CG  1 
ATOM   364  C  CD  . ARG   A 1 40  ? 8.300   2.899   -51.066 1.00 40.00 ? 481  ARG   A CD  1 
ATOM   365  N  NE  . ARG   A 1 40  ? 6.970   2.652   -51.611 1.00 41.89 ? 481  ARG   A NE  1 
ATOM   366  C  CZ  . ARG   A 1 40  ? 6.516   3.180   -52.742 1.00 38.53 ? 481  ARG   A CZ  1 
ATOM   367  N  NH1 . ARG   A 1 40  ? 7.284   3.989   -53.453 1.00 35.56 ? 481  ARG   A NH1 1 
ATOM   368  N  NH2 . ARG   A 1 40  ? 5.294   2.896   -53.161 1.00 44.59 ? 481  ARG   A NH2 1 
ATOM   369  N  N   . LEU   A 1 41  ? 11.606  1.924   -45.898 1.00 15.93 ? 482  LEU   A N   1 
ATOM   370  C  CA  . LEU   A 1 41  ? 12.897  2.005   -45.230 1.00 16.47 ? 482  LEU   A CA  1 
ATOM   371  C  C   . LEU   A 1 41  ? 13.648  0.685   -45.288 1.00 18.65 ? 482  LEU   A C   1 
ATOM   372  O  O   . LEU   A 1 41  ? 14.884  0.683   -45.315 1.00 16.66 ? 482  LEU   A O   1 
ATOM   373  C  CB  . LEU   A 1 41  ? 12.677  2.365   -43.759 1.00 15.54 ? 482  LEU   A CB  1 
ATOM   374  C  CG  . LEU   A 1 41  ? 12.055  3.739   -43.482 1.00 15.79 ? 482  LEU   A CG  1 
ATOM   375  C  CD1 . LEU   A 1 41  ? 11.603  3.900   -42.029 1.00 17.40 ? 482  LEU   A CD1 1 
ATOM   376  C  CD2 . LEU   A 1 41  ? 12.986  4.885   -43.870 1.00 19.14 ? 482  LEU   A CD2 1 
ATOM   377  N  N   . LEU   A 1 42  ? 12.937  -0.440  -45.292 1.00 15.26 ? 483  LEU   A N   1 
ATOM   378  C  CA  . LEU   A 1 42  ? 13.604  -1.729  -45.261 1.00 14.34 ? 483  LEU   A CA  1 
ATOM   379  C  C   . LEU   A 1 42  ? 14.495  -1.924  -46.481 1.00 14.59 ? 483  LEU   A C   1 
ATOM   380  O  O   . LEU   A 1 42  ? 15.629  -2.403  -46.359 1.00 18.97 ? 483  LEU   A O   1 
ATOM   381  C  CB  . LEU   A 1 42  ? 12.582  -2.854  -45.154 1.00 17.58 ? 483  LEU   A CB  1 
ATOM   382  C  CG  . LEU   A 1 42  ? 13.111  -4.280  -45.247 1.00 18.03 ? 483  LEU   A CG  1 
ATOM   383  C  CD1 . LEU   A 1 42  ? 14.024  -4.568  -44.044 1.00 17.94 ? 483  LEU   A CD1 1 
ATOM   384  C  CD2 . LEU   A 1 42  ? 11.938  -5.239  -45.259 1.00 18.91 ? 483  LEU   A CD2 1 
ATOM   385  N  N   . SER   A 1 43  ? 14.000  -1.567  -47.672 1.00 17.07 ? 484  SER   A N   1 
ATOM   386  C  CA  . SER   A 1 43  ? 14.798  -1.758  -48.880 1.00 20.97 ? 484  SER   A CA  1 
ATOM   387  C  C   . SER   A 1 43  ? 16.031  -0.859  -48.914 1.00 20.71 ? 484  SER   A C   1 
ATOM   388  O  O   . SER   A 1 43  ? 16.965  -1.135  -49.680 1.00 22.43 ? 484  SER   A O   1 
ATOM   389  C  CB  . SER   A 1 43  ? 13.934  -1.545  -50.130 1.00 28.81 ? 484  SER   A CB  1 
ATOM   390  O  OG  . SER   A 1 43  ? 13.334  -0.260  -50.123 1.00 33.23 ? 484  SER   A OG  1 
ATOM   391  N  N   . ARG   A 1 44  ? 16.061  0.200   -48.103 1.00 16.35 ? 485  ARG   A N   1 
ATOM   392  C  CA  . ARG   A 1 44  ? 17.191  1.111   -48.003 1.00 16.03 ? 485  ARG   A CA  1 
ATOM   393  C  C   . ARG   A 1 44  ? 18.296  0.614   -47.083 1.00 16.95 ? 485  ARG   A C   1 
ATOM   394  O  O   . ARG   A 1 44  ? 19.391  1.182   -47.106 1.00 19.79 ? 485  ARG   A O   1 
ATOM   395  C  CB  . ARG   A 1 44  ? 16.722  2.505   -47.575 1.00 18.12 ? 485  ARG   A CB  1 
ATOM   396  C  CG  . ARG   A 1 44  ? 15.736  3.122   -48.567 1.00 17.67 ? 485  ARG   A CG  1 
ATOM   397  C  CD  . ARG   A 1 44  ? 15.155  4.404   -48.044 1.00 18.51 ? 485  ARG   A CD  1 
ATOM   398  N  NE  . ARG   A 1 44  ? 16.189  5.400   -47.800 1.00 19.44 ? 485  ARG   A NE  1 
ATOM   399  C  CZ  . ARG   A 1 44  ? 16.044  6.469   -47.033 1.00 16.39 ? 485  ARG   A CZ  1 
ATOM   400  N  NH1 . ARG   A 1 44  ? 14.887  6.693   -46.399 1.00 18.43 ? 485  ARG   A NH1 1 
ATOM   401  N  NH2 . ARG   A 1 44  ? 17.070  7.300   -46.866 1.00 19.22 ? 485  ARG   A NH2 1 
ATOM   402  N  N   . CYS   A 1 45  ? 18.046  -0.438  -46.314 1.00 17.39 ? 486  CYS   A N   1 
ATOM   403  C  CA  . CYS   A 1 45  ? 18.994  -0.985  -45.360 1.00 15.55 ? 486  CYS   A CA  1 
ATOM   404  C  C   . CYS   A 1 45  ? 19.603  -2.257  -45.932 1.00 18.79 ? 486  CYS   A C   1 
ATOM   405  O  O   . CYS   A 1 45  ? 19.023  -2.927  -46.790 1.00 21.15 ? 486  CYS   A O   1 
ATOM   406  C  CB  . CYS   A 1 45  ? 18.213  -1.370  -44.103 1.00 17.10 ? 486  CYS   A CB  1 
ATOM   407  S  SG  . CYS   A 1 45  ? 17.561  0.008   -43.157 1.00 17.57 ? 486  CYS   A SG  1 
ATOM   408  N  N   . HIS   A 1 46  ? 20.796  -2.587  -45.444 1.00 17.40 ? 487  HIS   A N   1 
ATOM   409  C  CA  . HIS   A 1 46  ? 21.387  -3.887  -45.711 1.00 16.33 ? 487  HIS   A CA  1 
ATOM   410  C  C   . HIS   A 1 46  ? 20.903  -4.860  -44.641 1.00 14.96 ? 487  HIS   A C   1 
ATOM   411  O  O   . HIS   A 1 46  ? 21.069  -4.605  -43.444 1.00 16.75 ? 487  HIS   A O   1 
ATOM   412  C  CB  . HIS   A 1 46  ? 22.912  -3.824  -45.680 1.00 19.63 ? 487  HIS   A CB  1 
ATOM   413  C  CG  . HIS   A 1 46  ? 23.543  -5.153  -45.917 1.00 17.72 ? 487  HIS   A CG  1 
ATOM   414  N  ND1 . HIS   A 1 46  ? 23.486  -5.798  -47.136 1.00 23.63 ? 487  HIS   A ND1 1 
ATOM   415  C  CD2 . HIS   A 1 46  ? 24.175  -6.000  -45.072 1.00 21.96 ? 487  HIS   A CD2 1 
ATOM   416  C  CE1 . HIS   A 1 46  ? 24.095  -6.966  -47.041 1.00 31.11 ? 487  HIS   A CE1 1 
ATOM   417  N  NE2 . HIS   A 1 46  ? 24.523  -7.113  -45.800 1.00 29.01 ? 487  HIS   A NE2 1 
ATOM   418  N  N   . ARG   A 1 47  ? 20.352  -5.984  -45.063 1.00 14.56 ? 488  ARG   A N   1 
ATOM   419  C  CA  . ARG   A 1 47  ? 19.828  -6.961  -44.115 1.00 16.61 ? 488  ARG   A CA  1 
ATOM   420  C  C   . ARG   A 1 47  ? 20.979  -7.787  -43.538 1.00 19.16 ? 488  ARG   A C   1 
ATOM   421  O  O   . ARG   A 1 47  ? 21.696  -8.471  -44.281 1.00 24.55 ? 488  ARG   A O   1 
ATOM   422  C  CB  . ARG   A 1 47  ? 18.821  -7.857  -44.825 1.00 17.19 ? 488  ARG   A CB  1 
ATOM   423  C  CG  . ARG   A 1 47  ? 18.012  -8.719  -43.889 1.00 19.29 ? 488  ARG   A CG  1 
ATOM   424  C  CD  . ARG   A 1 47  ? 16.966  -7.923  -43.105 1.00 16.80 ? 488  ARG   A CD  1 
ATOM   425  N  NE  . ARG   A 1 47  ? 16.150  -8.874  -42.367 1.00 19.86 ? 488  ARG   A NE  1 
ATOM   426  C  CZ  . ARG   A 1 47  ? 15.018  -9.404  -42.815 1.00 16.75 ? 488  ARG   A CZ  1 
ATOM   427  N  NH1 . ARG   A 1 47  ? 14.511  -9.051  -43.994 1.00 19.18 ? 488  ARG   A NH1 1 
ATOM   428  N  NH2 . ARG   A 1 47  ? 14.382  -10.285 -42.063 1.00 23.75 ? 488  ARG   A NH2 1 
ATOM   429  N  N   . ILE   A 1 48  ? 21.160  -7.714  -42.225 1.00 15.28 ? 489  ILE   A N   1 
ATOM   430  C  CA  . ILE   A 1 48  ? 22.189  -8.459  -41.500 1.00 17.92 ? 489  ILE   A CA  1 
ATOM   431  C  C   . ILE   A 1 48  ? 21.544  -9.745  -41.005 1.00 16.93 ? 489  ILE   A C   1 
ATOM   432  O  O   . ILE   A 1 48  ? 20.456  -9.685  -40.416 1.00 18.04 ? 489  ILE   A O   1 
ATOM   433  C  CB  . ILE   A 1 48  ? 22.718  -7.610  -40.343 1.00 16.52 ? 489  ILE   A CB  1 
ATOM   434  C  CG1 . ILE   A 1 48  ? 23.511  -6.426  -40.890 1.00 18.35 ? 489  ILE   A CG1 1 
ATOM   435  C  CG2 . ILE   A 1 48  ? 23.500  -8.464  -39.343 1.00 18.85 ? 489  ILE   A CG2 1 
ATOM   436  C  CD1 . ILE   A 1 48  ? 23.905  -5.396  -39.845 1.00 21.58 ? 489  ILE   A CD1 1 
ATOM   437  N  N   . PRO   A 1 49  ? 22.135  -10.921 -41.232 1.00 18.71 ? 490  PRO   A N   1 
ATOM   438  C  CA  . PRO   A 1 49  ? 21.464  -12.158 -40.809 1.00 21.98 ? 490  PRO   A CA  1 
ATOM   439  C  C   . PRO   A 1 49  ? 21.468  -12.307 -39.296 1.00 24.08 ? 490  PRO   A C   1 
ATOM   440  O  O   . PRO   A 1 49  ? 22.412  -11.904 -38.618 1.00 19.68 ? 490  PRO   A O   1 
ATOM   441  C  CB  . PRO   A 1 49  ? 22.296  -13.257 -41.476 1.00 25.42 ? 490  PRO   A CB  1 
ATOM   442  C  CG  . PRO   A 1 49  ? 23.650  -12.640 -41.626 1.00 32.25 ? 490  PRO   A CG  1 
ATOM   443  C  CD  . PRO   A 1 49  ? 23.381  -11.197 -41.966 1.00 23.48 ? 490  PRO   A CD  1 
ATOM   444  N  N   . ALA   A 1 50  ? 20.378  -12.859 -38.765 1.00 19.09 ? 491  ALA   A N   1 
ATOM   445  C  CA  . ALA   A 1 50  ? 20.325  -13.241 -37.367 1.00 17.93 ? 491  ALA   A CA  1 
ATOM   446  C  C   . ALA   A 1 50  ? 21.104  -14.535 -37.153 1.00 18.47 ? 491  ALA   A C   1 
ATOM   447  O  O   . ALA   A 1 50  ? 21.318  -15.320 -38.077 1.00 22.89 ? 491  ALA   A O   1 
ATOM   448  C  CB  . ALA   A 1 50  ? 18.872  -13.463 -36.930 1.00 21.10 ? 491  ALA   A CB  1 
ATOM   449  N  N   . ARG   A 1 51  ? 21.523  -14.755 -35.912 1.00 17.87 ? 492  ARG   A N   1 
ATOM   450  C  CA  . ARG   A 1 51  ? 22.103  -16.033 -35.525 1.00 19.11 ? 492  ARG   A CA  1 
ATOM   451  C  C   . ARG   A 1 51  ? 21.870  -16.221 -34.041 1.00 17.15 ? 492  ARG   A C   1 
ATOM   452  O  O   . ARG   A 1 51  ? 21.603  -15.266 -33.310 1.00 17.79 ? 492  ARG   A O   1 
ATOM   453  C  CB  . ARG   A 1 51  ? 23.617  -16.121 -35.799 1.00 18.48 ? 492  ARG   A CB  1 
ATOM   454  C  CG  . ARG   A 1 51  ? 24.505  -15.254 -34.920 1.00 17.64 ? 492  ARG   A CG  1 
ATOM   455  C  CD  . ARG   A 1 51  ? 25.959  -15.664 -35.077 1.00 20.99 ? 492  ARG   A CD  1 
ATOM   456  N  NE  . ARG   A 1 51  ? 26.881  -14.742 -34.438 1.00 18.51 ? 492  ARG   A NE  1 
ATOM   457  C  CZ  . ARG   A 1 51  ? 27.355  -14.891 -33.203 1.00 18.11 ? 492  ARG   A CZ  1 
ATOM   458  N  NH1 . ARG   A 1 51  ? 26.926  -15.906 -32.454 1.00 22.66 ? 492  ARG   A NH1 1 
ATOM   459  N  NH2 . ARG   A 1 51  ? 28.224  -14.019 -32.704 1.00 17.74 ? 492  ARG   A NH2 1 
ATOM   460  N  N   . LEU   A 1 52  ? 22.061  -17.462 -33.590 1.00 18.16 ? 493  LEU   A N   1 
ATOM   461  C  CA  . LEU   A 1 52  ? 22.003  -17.765 -32.167 1.00 17.49 ? 493  LEU   A CA  1 
ATOM   462  C  C   . LEU   A 1 52  ? 23.316  -17.379 -31.494 1.00 18.50 ? 493  LEU   A C   1 
ATOM   463  O  O   . LEU   A 1 52  ? 24.394  -17.709 -31.994 1.00 17.95 ? 493  LEU   A O   1 
ATOM   464  C  CB  . LEU   A 1 52  ? 21.773  -19.263 -31.964 1.00 17.55 ? 493  LEU   A CB  1 
ATOM   465  C  CG  . LEU   A 1 52  ? 20.470  -19.868 -32.469 1.00 20.00 ? 493  LEU   A CG  1 
ATOM   466  C  CD1 . LEU   A 1 52  ? 20.427  -21.356 -32.151 1.00 35.16 ? 493  LEU   A CD1 1 
ATOM   467  C  CD2 . LEU   A 1 52  ? 19.271  -19.160 -31.864 1.00 24.52 ? 493  LEU   A CD2 1 
ATOM   468  N  N   . ALA   A 1 53  ? 23.233  -16.662 -30.380 1.00 17.35 ? 494  ALA   A N   1 
ATOM   469  C  CA  . ALA   A 1 53  ? 24.370  -16.556 -29.475 1.00 17.25 ? 494  ALA   A CA  1 
ATOM   470  C  C   . ALA   A 1 53  ? 24.767  -17.945 -28.975 1.00 17.46 ? 494  ALA   A C   1 
ATOM   471  O  O   . ALA   A 1 53  ? 23.933  -18.851 -28.870 1.00 19.22 ? 494  ALA   A O   1 
ATOM   472  C  CB  . ALA   A 1 53  ? 23.997  -15.674 -28.277 1.00 15.63 ? 494  ALA   A CB  1 
ATOM   473  N  N   . THR   A 1 54  ? 26.058  -18.120 -28.691 1.00 19.24 ? 495  THR   A N   1 
ATOM   474  C  CA  . THR   A 1 54  ? 26.525  -19.358 -28.087 1.00 16.90 ? 495  THR   A CA  1 
ATOM   475  C  C   . THR   A 1 54  ? 26.551  -19.241 -26.564 1.00 18.26 ? 495  THR   A C   1 
ATOM   476  O  O   . THR   A 1 54  ? 26.530  -18.147 -25.992 1.00 16.78 ? 495  THR   A O   1 
ATOM   477  C  CB  . THR   A 1 54  ? 27.937  -19.686 -28.556 1.00 20.05 ? 495  THR   A CB  1 
ATOM   478  O  OG1 . THR   A 1 54  ? 28.837  -18.701 -28.047 1.00 22.37 ? 495  THR   A OG1 1 
ATOM   479  C  CG2 . THR   A 1 54  ? 27.995  -19.696 -30.069 1.00 26.31 ? 495  THR   A CG2 1 
ATOM   480  N  N   . GLU   A 1 55  ? 26.649  -20.394 -25.904 1.00 21.72 ? 496  GLU   A N   1 
ATOM   481  C  CA  . GLU   A 1 55  ? 26.761  -20.363 -24.451 1.00 20.41 ? 496  GLU   A CA  1 
ATOM   482  C  C   . GLU   A 1 55  ? 28.026  -19.659 -24.004 1.00 16.47 ? 496  GLU   A C   1 
ATOM   483  O  O   . GLU   A 1 55  ? 28.027  -18.994 -22.959 1.00 19.29 ? 496  GLU   A O   1 
ATOM   484  C  CB  . GLU   A 1 55  ? 26.701  -21.771 -23.864 1.00 22.19 ? 496  GLU   A CB  1 
ATOM   485  C  CG  . GLU   A 1 55  ? 25.340  -22.416 -23.959 1.00 23.12 ? 496  GLU   A CG  1 
ATOM   486  C  CD  . GLU   A 1 55  ? 25.342  -23.861 -23.484 1.00 30.28 ? 496  GLU   A CD  1 
ATOM   487  O  OE1 . GLU   A 1 55  ? 25.867  -24.133 -22.381 1.00 33.83 ? 496  GLU   A OE1 1 
ATOM   488  O  OE2 . GLU   A 1 55  ? 24.807  -24.726 -24.207 1.00 32.21 ? 496  GLU   A OE2 1 
ATOM   489  N  N   . GLU   A 1 56  ? 29.117  -19.802 -24.766 1.00 20.66 ? 497  GLU   A N   1 
ATOM   490  C  CA  . GLU   A 1 56  ? 30.345  -19.106 -24.413 1.00 19.99 ? 497  GLU   A CA  1 
ATOM   491  C  C   . GLU   A 1 56  ? 30.157  -17.594 -24.494 1.00 17.09 ? 497  GLU   A C   1 
ATOM   492  O  O   . GLU   A 1 56  ? 30.629  -16.854 -23.625 1.00 17.88 ? 497  GLU   A O   1 
ATOM   493  C  CB  . GLU   A 1 56  ? 31.493  -19.577 -25.300 1.00 26.49 ? 497  GLU   A CB  1 
ATOM   494  C  CG  . GLU   A 1 56  ? 32.830  -18.975 -24.906 1.00 47.81 ? 497  GLU   A CG  1 
ATOM   495  C  CD  . GLU   A 1 56  ? 33.903  -19.178 -25.961 1.00 62.73 ? 497  GLU   A CD  1 
ATOM   496  O  OE1 . GLU   A 1 56  ? 33.784  -20.123 -26.768 1.00 52.09 ? 497  GLU   A OE1 1 
ATOM   497  O  OE2 . GLU   A 1 56  ? 34.867  -18.385 -25.982 1.00 59.70 ? 497  GLU   A OE2 1 
ATOM   498  N  N   . GLU   A 1 57  ? 29.421  -17.121 -25.506 1.00 18.74 ? 498  GLU   A N   1 
ATOM   499  C  CA  . GLU   A 1 57  ? 29.107  -15.696 -25.585 1.00 17.52 ? 498  GLU   A CA  1 
ATOM   500  C  C   . GLU   A 1 57  ? 28.260  -15.233 -24.407 1.00 14.64 ? 498  GLU   A C   1 
ATOM   501  O  O   . GLU   A 1 57  ? 28.491  -14.143 -23.864 1.00 14.73 ? 498  GLU   A O   1 
ATOM   502  C  CB  . GLU   A 1 57  ? 28.437  -15.371 -26.924 1.00 16.99 ? 498  GLU   A CB  1 
ATOM   503  C  CG  . GLU   A 1 57  ? 29.461  -15.447 -28.065 1.00 18.56 ? 498  GLU   A CG  1 
ATOM   504  C  CD  . GLU   A 1 57  ? 28.856  -15.492 -29.456 1.00 18.77 ? 498  GLU   A CD  1 
ATOM   505  O  OE1 . GLU   A 1 57  ? 27.669  -15.852 -29.600 1.00 20.96 ? 498  GLU   A OE1 1 
ATOM   506  O  OE2 . GLU   A 1 57  ? 29.609  -15.189 -30.402 1.00 19.43 ? 498  GLU   A OE2 1 
ATOM   507  N  N   . LEU   A 1 58  ? 27.283  -16.039 -23.996 1.00 14.57 ? 499  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 58  ? 26.460  -15.635 -22.857 1.00 13.97 ? 499  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 58  ? 27.300  -15.437 -21.612 1.00 15.09 ? 499  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 58  ? 26.982  -14.575 -20.780 1.00 15.22 ? 499  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 58  ? 25.371  -16.673 -22.577 1.00 16.65 ? 499  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 58  ? 24.291  -16.855 -23.654 1.00 15.98 ? 499  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 58  ? 23.265  -17.852 -23.153 1.00 19.02 ? 499  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 58  ? 23.630  -15.512 -24.008 1.00 15.88 ? 499  LEU   A CD2 1 
ATOM   515  N  N   . ALA   A 1 59  ? 28.366  -16.228 -21.468 1.00 15.31 ? 500  ALA   A N   1 
ATOM   516  C  CA  . ALA   A 1 59  ? 29.219  -16.171 -20.293 1.00 20.03 ? 500  ALA   A CA  1 
ATOM   517  C  C   . ALA   A 1 59  ? 30.025  -14.884 -20.221 1.00 18.09 ? 500  ALA   A C   1 
ATOM   518  O  O   . ALA   A 1 59  ? 30.622  -14.601 -19.175 1.00 20.70 ? 500  ALA   A O   1 
ATOM   519  C  CB  . ALA   A 1 59  ? 30.157  -17.378 -20.286 1.00 20.22 ? 500  ALA   A CB  1 
ATOM   520  N  N   . LEU   A 1 60  ? 30.037  -14.089 -21.298 1.00 17.05 ? 501  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 60  ? 30.617  -12.755 -21.219 1.00 16.59 ? 501  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 60  ? 29.983  -11.925 -20.108 1.00 16.61 ? 501  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 60  ? 30.646  -11.055 -19.528 1.00 18.95 ? 501  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 60  ? 30.475  -12.033 -22.557 1.00 18.52 ? 501  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 60  ? 31.347  -12.575 -23.686 1.00 21.05 ? 501  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 60  ? 30.905  -11.976 -25.009 1.00 19.08 ? 501  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 60  ? 32.833  -12.315 -23.407 1.00 23.01 ? 501  LEU   A CD2 1 
ATOM   528  N  N   . CYS   A 1 61  ? 28.697  -12.157 -19.803 1.00 16.02 ? 502  CYS   A N   1 
ATOM   529  C  CA  . CYS   A 1 61  ? 28.007  -11.390 -18.784 1.00 15.04 ? 502  CYS   A CA  1 
ATOM   530  C  C   . CYS   A 1 61  ? 27.254  -12.235 -17.769 1.00 15.49 ? 502  CYS   A C   1 
ATOM   531  O  O   . CYS   A 1 61  ? 26.924  -11.704 -16.704 1.00 17.34 ? 502  CYS   A O   1 
ATOM   532  C  CB  . CYS   A 1 61  ? 26.980  -10.442 -19.426 1.00 15.42 ? 502  CYS   A CB  1 
ATOM   533  S  SG  . CYS   A 1 61  ? 27.680  -9.124  -20.454 1.00 16.45 ? 502  CYS   A SG  1 
ATOM   534  N  N   . HIS   A 1 62  ? 26.969  -13.510 -18.049 1.00 14.42 ? 503  HIS   A N   1 
ATOM   535  C  CA  . HIS   A 1 62  ? 26.062  -14.274 -17.205 1.00 15.75 ? 503  HIS   A CA  1 
ATOM   536  C  C   . HIS   A 1 62  ? 26.744  -15.486 -16.592 1.00 16.35 ? 503  HIS   A C   1 
ATOM   537  O  O   . HIS   A 1 62  ? 27.696  -16.033 -17.149 1.00 17.66 ? 503  HIS   A O   1 
ATOM   538  C  CB  . HIS   A 1 62  ? 24.808  -14.709 -17.988 1.00 15.99 ? 503  HIS   A CB  1 
ATOM   539  C  CG  . HIS   A 1 62  ? 23.972  -13.556 -18.445 1.00 15.31 ? 503  HIS   A CG  1 
ATOM   540  N  ND1 . HIS   A 1 62  ? 23.208  -12.812 -17.575 1.00 14.38 ? 503  HIS   A ND1 1 
ATOM   541  C  CD2 . HIS   A 1 62  ? 23.837  -12.980 -19.664 1.00 13.02 ? 503  HIS   A CD2 1 
ATOM   542  C  CE1 . HIS   A 1 62  ? 22.610  -11.838 -18.243 1.00 14.20 ? 503  HIS   A CE1 1 
ATOM   543  N  NE2 . HIS   A 1 62  ? 22.987  -11.912 -19.506 1.00 14.21 ? 503  HIS   A NE2 1 
ATOM   544  N  N   . SER   A 1 63  ? 26.233  -15.892 -15.434 1.00 14.94 ? 504  SER   A N   1 
ATOM   545  C  CA  . SER   A 1 63  ? 26.805  -17.002 -14.690 1.00 16.38 ? 504  SER   A CA  1 
ATOM   546  C  C   . SER   A 1 63  ? 26.408  -18.322 -15.327 1.00 18.99 ? 504  SER   A C   1 
ATOM   547  O  O   . SER   A 1 63  ? 25.413  -18.425 -16.049 1.00 16.35 ? 504  SER   A O   1 
ATOM   548  C  CB  . SER   A 1 63  ? 26.283  -16.986 -13.257 1.00 18.82 ? 504  SER   A CB  1 
ATOM   549  O  OG  . SER   A 1 63  ? 24.899  -17.328 -13.249 1.00 18.42 ? 504  SER   A OG  1 
ATOM   550  N  N   A SER   A 1 64  ? 27.204  -19.355 -15.045 0.55 20.11 ? 505  SER   A N   1 
ATOM   551  N  N   B SER   A 1 64  ? 27.203  -19.356 -15.046 0.45 19.93 ? 505  SER   A N   1 
ATOM   552  C  CA  A SER   A 1 64  ? 26.898  -20.676 -15.578 0.55 17.27 ? 505  SER   A CA  1 
ATOM   553  C  CA  B SER   A 1 64  ? 26.893  -20.671 -15.592 0.45 16.46 ? 505  SER   A CA  1 
ATOM   554  C  C   A SER   A 1 64  ? 25.550  -21.172 -15.065 0.55 16.75 ? 505  SER   A C   1 
ATOM   555  C  C   B SER   A 1 64  ? 25.567  -21.201 -15.055 0.45 16.36 ? 505  SER   A C   1 
ATOM   556  O  O   A SER   A 1 64  ? 24.781  -21.780 -15.812 0.55 17.96 ? 505  SER   A O   1 
ATOM   557  O  O   B SER   A 1 64  ? 24.829  -21.864 -15.785 0.45 19.02 ? 505  SER   A O   1 
ATOM   558  C  CB  A SER   A 1 64  ? 28.009  -21.656 -15.200 0.55 20.25 ? 505  SER   A CB  1 
ATOM   559  C  CB  B SER   A 1 64  ? 28.035  -21.647 -15.298 0.45 19.66 ? 505  SER   A CB  1 
ATOM   560  O  OG  A SER   A 1 64  ? 28.043  -21.852 -13.800 0.55 28.18 ? 505  SER   A OG  1 
ATOM   561  O  OG  B SER   A 1 64  ? 27.755  -22.927 -15.835 0.45 21.00 ? 505  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 65  ? 25.240  -20.896 -13.798 1.00 17.94 ? 506  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 65  ? 23.984  -21.360 -13.216 1.00 16.31 ? 506  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 65  ? 22.780  -20.744 -13.922 1.00 16.28 ? 506  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 65  ? 21.797  -21.431 -14.208 1.00 18.43 ? 506  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 65  ? 23.951  -20.995 -11.731 1.00 23.13 ? 506  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 65  ? 22.735  -21.491 -10.975 1.00 26.97 ? 506  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 65  ? 22.769  -20.992 -9.532  1.00 39.89 ? 506  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 65  ? 21.910  -21.852 -8.625  1.00 41.39 ? 506  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 65  ? 21.912  -23.277 -9.068  1.00 56.64 ? 506  LYS   A NZ  1 
ATOM   571  N  N   . HIS   A 1 66  ? 22.843  -19.445 -14.209 1.00 15.85 ? 507  HIS   A N   1 
ATOM   572  C  CA  . HIS   A 1 66  ? 21.737  -18.764 -14.867 1.00 16.42 ? 507  HIS   A CA  1 
ATOM   573  C  C   . HIS   A 1 66  ? 21.584  -19.258 -16.297 1.00 17.07 ? 507  HIS   A C   1 
ATOM   574  O  O   . HIS   A 1 66  ? 20.468  -19.538 -16.758 1.00 16.74 ? 507  HIS   A O   1 
ATOM   575  C  CB  . HIS   A 1 66  ? 21.992  -17.257 -14.847 1.00 15.93 ? 507  HIS   A CB  1 
ATOM   576  C  CG  . HIS   A 1 66  ? 20.934  -16.472 -15.546 1.00 14.28 ? 507  HIS   A CG  1 
ATOM   577  N  ND1 . HIS   A 1 66  ? 19.605  -16.524 -15.177 1.00 16.08 ? 507  HIS   A ND1 1 
ATOM   578  C  CD2 . HIS   A 1 66  ? 20.995  -15.659 -16.624 1.00 16.37 ? 507  HIS   A CD2 1 
ATOM   579  C  CE1 . HIS   A 1 66  ? 18.897  -15.763 -15.991 1.00 15.43 ? 507  HIS   A CE1 1 
ATOM   580  N  NE2 . HIS   A 1 66  ? 19.714  -15.228 -16.879 1.00 15.15 ? 507  HIS   A NE2 1 
ATOM   581  N  N   . ILE   A 1 67  ? 22.695  -19.364 -17.018 1.00 15.58 ? 508  ILE   A N   1 
ATOM   582  C  CA  . ILE   A 1 67  ? 22.648  -19.897 -18.371 1.00 14.40 ? 508  ILE   A CA  1 
ATOM   583  C  C   . ILE   A 1 67  ? 22.030  -21.287 -18.379 1.00 17.22 ? 508  ILE   A C   1 
ATOM   584  O  O   . ILE   A 1 67  ? 21.146  -21.584 -19.189 1.00 17.88 ? 508  ILE   A O   1 
ATOM   585  C  CB  . ILE   A 1 67  ? 24.053  -19.917 -18.992 1.00 17.38 ? 508  ILE   A CB  1 
ATOM   586  C  CG1 . ILE   A 1 67  ? 24.591  -18.500 -19.181 1.00 14.29 ? 508  ILE   A CG1 1 
ATOM   587  C  CG2 . ILE   A 1 67  ? 24.038  -20.715 -20.302 1.00 18.95 ? 508  ILE   A CG2 1 
ATOM   588  C  CD1 . ILE   A 1 67  ? 26.123  -18.453 -19.474 1.00 15.55 ? 508  ILE   A CD1 1 
ATOM   589  N  N   . SER   A 1 68  ? 22.486  -22.158 -17.469 1.00 17.38 ? 509  SER   A N   1 
ATOM   590  C  CA  . SER   A 1 68  ? 22.010  -23.538 -17.447 1.00 18.75 ? 509  SER   A CA  1 
ATOM   591  C  C   . SER   A 1 68  ? 20.505  -23.615 -17.185 1.00 16.76 ? 509  SER   A C   1 
ATOM   592  O  O   . SER   A 1 68  ? 19.795  -24.393 -17.843 1.00 17.80 ? 509  SER   A O   1 
ATOM   593  C  CB  . SER   A 1 68  ? 22.802  -24.325 -16.395 1.00 19.77 ? 509  SER   A CB  1 
ATOM   594  O  OG  . SER   A 1 68  ? 22.254  -25.616 -16.198 1.00 23.68 ? 509  SER   A OG  1 
ATOM   595  N  N   . ILE   A 1 69  ? 19.999  -22.837 -16.221 1.00 16.94 ? 510  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 69  ? 18.588  -22.977 -15.868 1.00 17.57 ? 510  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 69  ? 17.688  -22.466 -16.991 1.00 19.84 ? 510  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 69  ? 16.713  -23.127 -17.366 1.00 18.92 ? 510  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 69  ? 18.267  -22.392 -14.480 1.00 17.48 ? 510  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 69  ? 16.893  -22.896 -14.022 1.00 24.34 ? 510  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 69  ? 18.356  -20.867 -14.463 1.00 19.99 ? 510  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 69  ? 16.729  -22.958 -12.526 1.00 28.26 ? 510  ILE   A CD1 1 
ATOM   603  N  N   . ILE   A 1 70  ? 18.038  -21.331 -17.599 1.00 15.67 ? 511  ILE   A N   1 
ATOM   604  C  CA  . ILE   A 1 70  ? 17.245  -20.848 -18.731 1.00 18.15 ? 511  ILE   A CA  1 
ATOM   605  C  C   . ILE   A 1 70  ? 17.349  -21.811 -19.907 1.00 17.26 ? 511  ILE   A C   1 
ATOM   606  O  O   . ILE   A 1 70  ? 16.344  -22.126 -20.555 1.00 16.70 ? 511  ILE   A O   1 
ATOM   607  C  CB  . ILE   A 1 70  ? 17.608  -19.397 -19.098 1.00 14.98 ? 511  ILE   A CB  1 
ATOM   608  C  CG1 . ILE   A 1 70  ? 17.398  -18.473 -17.890 1.00 15.49 ? 511  ILE   A CG1 1 
ATOM   609  C  CG2 . ILE   A 1 70  ? 16.764  -18.904 -20.254 1.00 15.81 ? 511  ILE   A CG2 1 
ATOM   610  C  CD1 . ILE   A 1 70  ? 16.021  -18.547 -17.265 1.00 15.98 ? 511  ILE   A CD1 1 
ATOM   611  N  N   . LYS   A 1 71  ? 18.557  -22.331 -20.174 1.00 16.45 ? 512  LYS   A N   1 
ATOM   612  C  CA  . LYS   A 1 71  ? 18.734  -23.313 -21.238 1.00 16.45 ? 512  LYS   A CA  1 
ATOM   613  C  C   . LYS   A 1 71  ? 17.817  -24.516 -21.040 1.00 16.55 ? 512  LYS   A C   1 
ATOM   614  O  O   . LYS   A 1 71  ? 17.194  -25.001 -21.997 1.00 18.05 ? 512  LYS   A O   1 
ATOM   615  C  CB  . LYS   A 1 71  ? 20.206  -23.746 -21.295 1.00 16.10 ? 512  LYS   A CB  1 
ATOM   616  C  CG  . LYS   A 1 71  ? 20.513  -24.832 -22.312 1.00 20.53 ? 512  LYS   A CG  1 
ATOM   617  C  CD  . LYS   A 1 71  ? 21.986  -25.231 -22.245 1.00 20.02 ? 512  LYS   A CD  1 
ATOM   618  C  CE  . LYS   A 1 71  ? 22.246  -26.528 -23.013 1.00 28.02 ? 512  LYS   A CE  1 
ATOM   619  N  NZ  . LYS   A 1 71  ? 23.644  -27.024 -22.809 1.00 28.64 ? 512  LYS   A NZ  1 
ATOM   620  N  N   . SER   A 1 72  ? 17.685  -24.979 -19.794 1.00 16.50 ? 513  SER   A N   1 
ATOM   621  C  CA  . SER   A 1 72  ? 16.869  -26.160 -19.520 1.00 18.45 ? 513  SER   A CA  1 
ATOM   622  C  C   . SER   A 1 72  ? 15.390  -25.935 -19.790 1.00 19.74 ? 513  SER   A C   1 
ATOM   623  O  O   . SER   A 1 72  ? 14.648  -26.913 -19.963 1.00 20.98 ? 513  SER   A O   1 
ATOM   624  C  CB  . SER   A 1 72  ? 17.035  -26.614 -18.072 1.00 16.45 ? 513  SER   A CB  1 
ATOM   625  O  OG  . SER   A 1 72  ? 16.305  -25.808 -17.174 1.00 19.78 ? 513  SER   A OG  1 
ATOM   626  N  N   . SER   A 1 73  ? 14.928  -24.684 -19.828 1.00 16.57 ? 514  SER   A N   1 
ATOM   627  C  CA  . SER   A 1 73  ? 13.493  -24.471 -19.998 1.00 16.40 ? 514  SER   A CA  1 
ATOM   628  C  C   . SER   A 1 73  ? 13.005  -24.889 -21.382 1.00 18.60 ? 514  SER   A C   1 
ATOM   629  O  O   . SER   A 1 73  ? 11.795  -25.056 -21.564 1.00 19.49 ? 514  SER   A O   1 
ATOM   630  C  CB  . SER   A 1 73  ? 13.119  -23.018 -19.704 1.00 17.28 ? 514  SER   A CB  1 
ATOM   631  O  OG  . SER   A 1 73  ? 13.701  -22.139 -20.655 1.00 16.82 ? 514  SER   A OG  1 
ATOM   632  N  N   . GLU   A 1 74  ? 13.912  -25.089 -22.351 1.00 17.21 ? 515  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 74  ? 13.510  -25.537 -23.682 1.00 19.58 ? 515  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 74  ? 12.779  -26.874 -23.639 1.00 21.74 ? 515  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 74  ? 11.923  -27.137 -24.493 1.00 23.69 ? 515  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 74  ? 14.725  -25.618 -24.609 1.00 22.80 ? 515  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 74  ? 14.402  -26.221 -25.964 1.00 19.77 ? 515  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 74  ? 15.540  -26.085 -26.947 1.00 42.97 ? 515  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 74  ? 16.686  -25.897 -26.494 1.00 32.35 ? 515  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 74  ? 15.287  -26.168 -28.170 1.00 38.12 ? 515  GLU   A OE2 1 
ATOM   641  N  N   . HIS   A 1 75  ? 13.077  -27.723 -22.656 1.00 19.60 ? 516  HIS   A N   1 
ATOM   642  C  CA  . HIS   A 1 75  ? 12.492  -29.058 -22.585 1.00 21.86 ? 516  HIS   A CA  1 
ATOM   643  C  C   . HIS   A 1 75  ? 11.606  -29.247 -21.368 1.00 23.91 ? 516  HIS   A C   1 
ATOM   644  O  O   . HIS   A 1 75  ? 11.307  -30.385 -20.999 1.00 29.10 ? 516  HIS   A O   1 
ATOM   645  C  CB  . HIS   A 1 75  ? 13.589  -30.120 -22.606 1.00 27.12 ? 516  HIS   A CB  1 
ATOM   646  C  CG  . HIS   A 1 75  ? 14.498  -30.000 -23.781 1.00 25.21 ? 516  HIS   A CG  1 
ATOM   647  N  ND1 . HIS   A 1 75  ? 15.823  -29.646 -23.662 1.00 41.95 ? 516  HIS   A ND1 1 
ATOM   648  C  CD2 . HIS   A 1 75  ? 14.262  -30.149 -25.105 1.00 30.74 ? 516  HIS   A CD2 1 
ATOM   649  C  CE1 . HIS   A 1 75  ? 16.371  -29.599 -24.862 1.00 35.03 ? 516  HIS   A CE1 1 
ATOM   650  N  NE2 . HIS   A 1 75  ? 15.444  -29.900 -25.755 1.00 33.13 ? 516  HIS   A NE2 1 
ATOM   651  N  N   . MET   A 1 76  ? 11.184  -28.160 -20.732 1.00 20.93 ? 517  MET   A N   1 
ATOM   652  C  CA  . MET   A 1 76  ? 10.370  -28.230 -19.536 1.00 21.34 ? 517  MET   A CA  1 
ATOM   653  C  C   . MET   A 1 76  ? 8.903   -28.433 -19.894 1.00 20.06 ? 517  MET   A C   1 
ATOM   654  O  O   . MET   A 1 76  ? 8.443   -28.067 -20.982 1.00 21.04 ? 517  MET   A O   1 
ATOM   655  C  CB  . MET   A 1 76  ? 10.512  -26.941 -18.738 1.00 18.99 ? 517  MET   A CB  1 
ATOM   656  C  CG  . MET   A 1 76  ? 11.724  -26.927 -17.826 1.00 16.54 ? 517  MET   A CG  1 
ATOM   657  S  SD  . MET   A 1 76  ? 11.749  -25.415 -16.878 1.00 19.83 ? 517  MET   A SD  1 
ATOM   658  C  CE  . MET   A 1 76  ? 13.012  -25.839 -15.692 1.00 20.08 ? 517  MET   A CE  1 
ATOM   659  N  N   . LYS   A 1 77  ? 8.180   -29.023 -18.958 1.00 20.70 ? 518  LYS   A N   1 
ATOM   660  C  CA  . LYS   A 1 77  ? 6.745   -29.192 -19.050 1.00 21.25 ? 518  LYS   A CA  1 
ATOM   661  C  C   . LYS   A 1 77  ? 6.059   -27.899 -18.628 1.00 20.32 ? 518  LYS   A C   1 
ATOM   662  O  O   . LYS   A 1 77  ? 6.649   -27.078 -17.917 1.00 18.62 ? 518  LYS   A O   1 
ATOM   663  C  CB  . LYS   A 1 77  ? 6.326   -30.317 -18.108 1.00 25.31 ? 518  LYS   A CB  1 
ATOM   664  C  CG  . LYS   A 1 77  ? 6.680   -31.713 -18.609 1.00 30.38 ? 518  LYS   A CG  1 
ATOM   665  C  CD  . LYS   A 1 77  ? 6.398   -32.770 -17.541 1.00 45.79 ? 518  LYS   A CD  1 
ATOM   666  C  CE  . LYS   A 1 77  ? 5.081   -33.489 -17.812 1.00 48.34 ? 518  LYS   A CE  1 
ATOM   667  N  NZ  . LYS   A 1 77  ? 4.489   -34.107 -16.584 1.00 55.09 ? 518  LYS   A NZ  1 
ATOM   668  N  N   . PRO   A 1 78  ? 4.803   -27.687 -19.048 1.00 19.60 ? 519  PRO   A N   1 
ATOM   669  C  CA  . PRO   A 1 78  ? 4.113   -26.443 -18.666 1.00 22.43 ? 519  PRO   A CA  1 
ATOM   670  C  C   . PRO   A 1 78  ? 4.221   -26.100 -17.191 1.00 24.65 ? 519  PRO   A C   1 
ATOM   671  O  O   . PRO   A 1 78  ? 4.511   -24.941 -16.861 1.00 21.74 ? 519  PRO   A O   1 
ATOM   672  C  CB  . PRO   A 1 78  ? 2.663   -26.707 -19.100 1.00 18.56 ? 519  PRO   A CB  1 
ATOM   673  C  CG  . PRO   A 1 78  ? 2.819   -27.584 -20.264 1.00 22.68 ? 519  PRO   A CG  1 
ATOM   674  C  CD  . PRO   A 1 78  ? 3.974   -28.504 -19.950 1.00 29.32 ? 519  PRO   A CD  1 
ATOM   675  N  N   . ARG   A 1 79  ? 4.025   -27.069 -16.288 1.00 19.88 ? 520  ARG   A N   1 
ATOM   676  C  CA  . ARG   A 1 79  ? 4.119   -26.739 -14.871 1.00 18.72 ? 520  ARG   A CA  1 
ATOM   677  C  C   . ARG   A 1 79  ? 5.525   -26.306 -14.501 1.00 18.39 ? 520  ARG   A C   1 
ATOM   678  O  O   . ARG   A 1 79  ? 5.696   -25.420 -13.658 1.00 18.63 ? 520  ARG   A O   1 
ATOM   679  C  CB  . ARG   A 1 79  ? 3.663   -27.893 -13.968 1.00 20.42 ? 520  ARG   A CB  1 
ATOM   680  C  CG  . ARG   A 1 79  ? 3.464   -27.447 -12.513 1.00 23.87 ? 520  ARG   A CG  1 
ATOM   681  C  CD  . ARG   A 1 79  ? 3.289   -28.619 -11.532 1.00 26.01 ? 520  ARG   A CD  1 
ATOM   682  N  NE  . ARG   A 1 79  ? 4.478   -29.467 -11.499 0.76 23.73 ? 520  ARG   A NE  1 
ATOM   683  C  CZ  . ARG   A 1 79  ? 4.591   -30.597 -10.809 0.76 28.12 ? 520  ARG   A CZ  1 
ATOM   684  N  NH1 . ARG   A 1 79  ? 3.585   -31.041 -10.068 1.00 29.33 ? 520  ARG   A NH1 1 
ATOM   685  N  NH2 . ARG   A 1 79  ? 5.722   -31.286 -10.865 0.66 21.16 ? 520  ARG   A NH2 1 
ATOM   686  N  N   . ASP   A 1 80  ? 6.538   -26.942 -15.099 1.00 18.43 ? 521  ASP   A N   1 
ATOM   687  C  CA  . ASP   A 1 80  ? 7.922   -26.541 -14.837 1.00 18.57 ? 521  ASP   A CA  1 
ATOM   688  C  C   . ASP   A 1 80  ? 8.151   -25.105 -15.284 1.00 16.86 ? 521  ASP   A C   1 
ATOM   689  O  O   . ASP   A 1 80  ? 8.802   -24.320 -14.581 1.00 17.27 ? 521  ASP   A O   1 
ATOM   690  C  CB  . ASP   A 1 80  ? 8.883   -27.426 -15.623 1.00 19.55 ? 521  ASP   A CB  1 
ATOM   691  C  CG  . ASP   A 1 80  ? 8.896   -28.871 -15.167 1.00 24.65 ? 521  ASP   A CG  1 
ATOM   692  O  OD1 . ASP   A 1 80  ? 8.817   -29.129 -13.954 1.00 19.38 ? 521  ASP   A OD1 1 
ATOM   693  O  OD2 . ASP   A 1 80  ? 9.012   -29.749 -16.051 1.00 25.86 ? 521  ASP   A OD2 1 
ATOM   694  N  N   . LEU   A 1 81  ? 7.621   -24.749 -16.457 1.00 16.87 ? 522  LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 81  ? 7.791   -23.396 -16.980 1.00 16.49 ? 522  LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 81  ? 7.108   -22.368 -16.094 1.00 20.42 ? 522  LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 81  ? 7.670   -21.305 -15.814 1.00 17.58 ? 522  LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 81  ? 7.216   -23.313 -18.389 1.00 17.71 ? 522  LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 81  ? 7.996   -24.084 -19.450 1.00 17.24 ? 522  LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 81  ? 7.173   -24.227 -20.717 1.00 18.25 ? 522  LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 81  ? 9.329   -23.401 -19.752 1.00 20.95 ? 522  LEU   A CD2 1 
ATOM   702  N  N   . ASN   A 1 82  ? 5.890   -22.666 -15.643 1.00 16.38 ? 523  ASN   A N   1 
ATOM   703  C  CA  . ASN   A 1 82  ? 5.161   -21.728 -14.795 1.00 18.45 ? 523  ASN   A CA  1 
ATOM   704  C  C   . ASN   A 1 82  ? 5.878   -21.499 -13.471 1.00 17.16 ? 523  ASN   A C   1 
ATOM   705  O  O   . ASN   A 1 82  ? 6.005   -20.359 -13.016 1.00 17.08 ? 523  ASN   A O   1 
ATOM   706  C  CB  . ASN   A 1 82  ? 3.741   -22.242 -14.550 1.00 22.56 ? 523  ASN   A CB  1 
ATOM   707  C  CG  . ASN   A 1 82  ? 2.897   -21.258 -13.770 1.00 40.71 ? 523  ASN   A CG  1 
ATOM   708  O  OD1 . ASN   A 1 82  ? 2.377   -21.585 -12.705 1.00 45.87 ? 523  ASN   A OD1 1 
ATOM   709  N  ND2 . ASN   A 1 82  ? 2.756   -20.045 -14.294 1.00 53.22 ? 523  ASN   A ND2 1 
ATOM   710  N  N   . ARG   A 1 83  ? 6.341   -22.579 -12.824 1.00 17.63 ? 524  ARG   A N   1 
ATOM   711  C  CA  . ARG   A 1 83  ? 7.020   -22.431 -11.539 1.00 17.51 ? 524  ARG   A CA  1 
ATOM   712  C  C   . ARG   A 1 83  ? 8.360   -21.709 -11.694 1.00 12.72 ? 524  ARG   A C   1 
ATOM   713  O  O   . ARG   A 1 83  ? 8.703   -20.837 -10.886 1.00 17.39 ? 524  ARG   A O   1 
ATOM   714  C  CB  . ARG   A 1 83  ? 7.228   -23.802 -10.892 1.00 17.00 ? 524  ARG   A CB  1 
ATOM   715  C  CG  . ARG   A 1 83  ? 5.928   -24.476 -10.470 1.00 19.89 ? 524  ARG   A CG  1 
ATOM   716  C  CD  . ARG   A 1 83  ? 6.198   -25.888 -9.943  1.00 24.21 ? 524  ARG   A CD  1 
ATOM   717  N  NE  . ARG   A 1 83  ? 5.054   -26.420 -9.200  1.00 20.03 ? 524  ARG   A NE  1 
ATOM   718  C  CZ  . ARG   A 1 83  ? 5.063   -27.590 -8.564  1.00 24.74 ? 524  ARG   A CZ  1 
ATOM   719  N  NH1 . ARG   A 1 83  ? 6.160   -28.343 -8.575  1.00 19.00 ? 524  ARG   A NH1 1 
ATOM   720  N  NH2 . ARG   A 1 83  ? 3.984   -28.004 -7.909  1.00 23.94 ? 524  ARG   A NH2 1 
ATOM   721  N  N   . LEU   A 1 84  ? 9.125   -22.054 -12.733 1.00 16.92 ? 525  LEU   A N   1 
ATOM   722  C  CA  . LEU   A 1 84  ? 10.394  -21.370 -12.955 1.00 16.64 ? 525  LEU   A CA  1 
ATOM   723  C  C   . LEU   A 1 84  ? 10.179  -19.882 -13.206 1.00 15.18 ? 525  LEU   A C   1 
ATOM   724  O  O   . LEU   A 1 84  ? 10.845  -19.044 -12.589 1.00 16.14 ? 525  LEU   A O   1 
ATOM   725  C  CB  . LEU   A 1 84  ? 11.162  -22.012 -14.111 1.00 17.05 ? 525  LEU   A CB  1 
ATOM   726  C  CG  . LEU   A 1 84  ? 12.464  -21.290 -14.502 1.00 15.85 ? 525  LEU   A CG  1 
ATOM   727  C  CD1 . LEU   A 1 84  ? 13.414  -21.187 -13.292 1.00 14.98 ? 525  LEU   A CD1 1 
ATOM   728  C  CD2 . LEU   A 1 84  ? 13.144  -21.971 -15.701 1.00 18.06 ? 525  LEU   A CD2 1 
ATOM   729  N  N   . GLY   A 1 85  ? 9.228   -19.529 -14.083 1.00 15.87 ? 526  GLY   A N   1 
ATOM   730  C  CA  . GLY   A 1 85  ? 8.983   -18.118 -14.336 1.00 18.34 ? 526  GLY   A CA  1 
ATOM   731  C  C   . GLY   A 1 85  ? 8.616   -17.366 -13.072 1.00 18.71 ? 526  GLY   A C   1 
ATOM   732  O  O   . GLY   A 1 85  ? 9.036   -16.223 -12.865 1.00 18.17 ? 526  GLY   A O   1 
ATOM   733  N  N   . ASP   A 1 86  ? 7.864   -18.018 -12.183 1.00 17.54 ? 527  ASP   A N   1 
ATOM   734  C  CA  . ASP   A 1 86  ? 7.402   -17.366 -10.971 1.00 20.57 ? 527  ASP   A CA  1 
ATOM   735  C  C   . ASP   A 1 86  ? 8.501   -17.197 -9.931  1.00 24.32 ? 527  ASP   A C   1 
ATOM   736  O  O   . ASP   A 1 86  ? 8.274   -16.518 -8.922  1.00 21.75 ? 527  ASP   A O   1 
ATOM   737  C  CB  . ASP   A 1 86  ? 6.200   -18.122 -10.407 1.00 18.76 ? 527  ASP   A CB  1 
ATOM   738  C  CG  . ASP   A 1 86  ? 4.948   -17.919 -11.240 1.00 40.02 ? 527  ASP   A CG  1 
ATOM   739  O  OD1 . ASP   A 1 86  ? 4.995   -17.129 -12.213 1.00 32.33 ? 527  ASP   A OD1 1 
ATOM   740  O  OD2 . ASP   A 1 86  ? 3.917   -18.548 -10.926 1.00 44.56 ? 527  ASP   A OD2 1 
ATOM   741  N  N   . GLU   A 1 87  ? 9.682   -17.784 -10.152 1.00 18.04 ? 528  GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 87  ? 10.824  -17.497 -9.290  1.00 22.77 ? 528  GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 87  ? 11.384  -16.102 -9.521  1.00 24.20 ? 528  GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 87  ? 12.078  -15.576 -8.647  1.00 24.74 ? 528  GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 87  ? 11.949  -18.520 -9.499  1.00 19.66 ? 528  GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 87  ? 11.529  -19.970 -9.289  1.00 22.30 ? 528  GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 87  ? 11.242  -20.299 -7.833  1.00 39.94 ? 528  GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 87  ? 11.749  -19.578 -6.948  1.00 40.11 ? 528  GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 87  ? 10.515  -21.282 -7.573  1.00 39.69 ? 528  GLU   A OE2 1 
ATOM   750  N  N   . TYR   A 1 88  ? 11.115  -15.502 -10.676 1.00 16.64 ? 529  TYR   A N   1 
ATOM   751  C  CA  . TYR   A 1 88  ? 11.666  -14.205 -11.044 1.00 15.78 ? 529  TYR   A CA  1 
ATOM   752  C  C   . TYR   A 1 88  ? 10.618  -13.112 -10.893 1.00 14.34 ? 529  TYR   A C   1 
ATOM   753  O  O   . TYR   A 1 88  ? 9.424   -13.370 -10.777 1.00 16.01 ? 529  TYR   A O   1 
ATOM   754  C  CB  . TYR   A 1 88  ? 12.183  -14.223 -12.492 1.00 13.69 ? 529  TYR   A CB  1 
ATOM   755  C  CG  . TYR   A 1 88  ? 13.143  -15.335 -12.753 1.00 13.46 ? 529  TYR   A CG  1 
ATOM   756  C  CD1 . TYR   A 1 88  ? 14.434  -15.258 -12.281 1.00 14.71 ? 529  TYR   A CD1 1 
ATOM   757  C  CD2 . TYR   A 1 88  ? 12.764  -16.458 -13.481 1.00 14.89 ? 529  TYR   A CD2 1 
ATOM   758  C  CE1 . TYR   A 1 88  ? 15.344  -16.276 -12.512 1.00 16.32 ? 529  TYR   A CE1 1 
ATOM   759  C  CE2 . TYR   A 1 88  ? 13.670  -17.489 -13.716 1.00 15.92 ? 529  TYR   A CE2 1 
ATOM   760  C  CZ  . TYR   A 1 88  ? 14.964  -17.384 -13.244 1.00 15.21 ? 529  TYR   A CZ  1 
ATOM   761  O  OH  . TYR   A 1 88  ? 15.869  -18.408 -13.462 1.00 15.76 ? 529  TYR   A OH  1 
ATOM   762  N  N   . ASN   A 1 89  ? 11.095  -11.873 -10.912 1.00 16.25 ? 530  ASN   A N   1 
ATOM   763  C  CA  . ASN   A 1 89  ? 10.232  -10.700 -10.970 1.00 16.46 ? 530  ASN   A CA  1 
ATOM   764  C  C   . ASN   A 1 89  ? 9.786   -10.492 -12.419 1.00 15.25 ? 530  ASN   A C   1 
ATOM   765  O  O   . ASN   A 1 89  ? 10.596  -10.135 -13.276 1.00 14.48 ? 530  ASN   A O   1 
ATOM   766  C  CB  . ASN   A 1 89  ? 11.016  -9.496  -10.466 1.00 15.47 ? 530  ASN   A CB  1 
ATOM   767  C  CG  . ASN   A 1 89  ? 10.165  -8.241  -10.349 1.00 19.12 ? 530  ASN   A CG  1 
ATOM   768  O  OD1 . ASN   A 1 89  ? 9.076   -8.148  -10.913 1.00 22.76 ? 530  ASN   A OD1 1 
ATOM   769  N  ND2 . ASN   A 1 89  ? 10.700  -7.241  -9.657  1.00 25.14 ? 530  ASN   A ND2 1 
ATOM   770  N  N   . SER   A 1 90  ? 8.503   -10.698 -12.706 1.00 15.03 ? 531  SER   A N   1 
ATOM   771  C  CA  . SER   A 1 90  ? 7.898   -10.366 -14.005 1.00 15.64 ? 531  SER   A CA  1 
ATOM   772  C  C   . SER   A 1 90  ? 8.559   -11.085 -15.188 1.00 15.03 ? 531  SER   A C   1 
ATOM   773  O  O   . SER   A 1 90  ? 9.040   -10.463 -16.137 1.00 13.69 ? 531  SER   A O   1 
ATOM   774  C  CB  . SER   A 1 90  ? 7.818   -8.850  -14.232 1.00 17.43 ? 531  SER   A CB  1 
ATOM   775  O  OG  . SER   A 1 90  ? 7.100   -8.226  -13.162 1.00 21.28 ? 531  SER   A OG  1 
ATOM   776  N  N   . ILE   A 1 91  ? 8.484   -12.415 -15.166 1.00 15.20 ? 532  ILE   A N   1 
ATOM   777  C  CA  . ILE   A 1 91  ? 8.973   -13.261 -16.249 1.00 13.85 ? 532  ILE   A CA  1 
ATOM   778  C  C   . ILE   A 1 91  ? 7.912   -14.301 -16.581 1.00 15.95 ? 532  ILE   A C   1 
ATOM   779  O  O   . ILE   A 1 91  ? 7.332   -14.912 -15.665 1.00 14.96 ? 532  ILE   A O   1 
ATOM   780  C  CB  . ILE   A 1 91  ? 10.282  -13.967 -15.847 1.00 14.59 ? 532  ILE   A CB  1 
ATOM   781  C  CG1 . ILE   A 1 91  ? 11.454  -12.974 -15.813 1.00 13.91 ? 532  ILE   A CG1 1 
ATOM   782  C  CG2 . ILE   A 1 91  ? 10.569  -15.169 -16.745 1.00 15.77 ? 532  ILE   A CG2 1 
ATOM   783  C  CD1 . ILE   A 1 91  ? 11.960  -12.551 -17.223 1.00 13.60 ? 532  ILE   A CD1 1 
ATOM   784  N  N   . PHE   A 1 92  ? 7.671   -14.512 -17.879 1.00 13.44 ? 533  PHE   A N   1 
ATOM   785  C  CA  . PHE   A 1 92  ? 6.980   -15.691 -18.373 1.00 14.02 ? 533  PHE   A CA  1 
ATOM   786  C  C   . PHE   A 1 92  ? 7.910   -16.433 -19.324 1.00 15.62 ? 533  PHE   A C   1 
ATOM   787  O  O   . PHE   A 1 92  ? 8.753   -15.825 -20.000 1.00 13.53 ? 533  PHE   A O   1 
ATOM   788  C  CB  . PHE   A 1 92  ? 5.664   -15.332 -19.099 1.00 14.26 ? 533  PHE   A CB  1 
ATOM   789  C  CG  . PHE   A 1 92  ? 5.859   -14.472 -20.320 1.00 13.84 ? 533  PHE   A CG  1 
ATOM   790  C  CD1 . PHE   A 1 92  ? 6.101   -15.061 -21.562 1.00 12.84 ? 533  PHE   A CD1 1 
ATOM   791  C  CD2 . PHE   A 1 92  ? 5.782   -13.086 -20.239 1.00 14.11 ? 533  PHE   A CD2 1 
ATOM   792  C  CE1 . PHE   A 1 92  ? 6.273   -14.292 -22.703 1.00 14.45 ? 533  PHE   A CE1 1 
ATOM   793  C  CE2 . PHE   A 1 92  ? 5.973   -12.299 -21.373 1.00 14.04 ? 533  PHE   A CE2 1 
ATOM   794  C  CZ  . PHE   A 1 92  ? 6.216   -12.903 -22.609 1.00 13.24 ? 533  PHE   A CZ  1 
ATOM   795  N  N   . ILE   A 1 93  ? 7.759   -17.757 -19.373 1.00 15.20 ? 534  ILE   A N   1 
ATOM   796  C  CA  . ILE   A 1 93  ? 8.671   -18.625 -20.106 1.00 14.99 ? 534  ILE   A CA  1 
ATOM   797  C  C   . ILE   A 1 93  ? 7.858   -19.651 -20.884 1.00 15.00 ? 534  ILE   A C   1 
ATOM   798  O  O   . ILE   A 1 93  ? 6.933   -20.255 -20.333 1.00 15.39 ? 534  ILE   A O   1 
ATOM   799  C  CB  . ILE   A 1 93  ? 9.667   -19.348 -19.179 1.00 14.49 ? 534  ILE   A CB  1 
ATOM   800  C  CG1 . ILE   A 1 93  ? 10.212  -18.430 -18.081 1.00 15.60 ? 534  ILE   A CG1 1 
ATOM   801  C  CG2 . ILE   A 1 93  ? 10.814  -19.944 -20.008 1.00 17.59 ? 534  ILE   A CG2 1 
ATOM   802  C  CD1 . ILE   A 1 93  ? 11.264  -19.115 -17.202 1.00 17.36 ? 534  ILE   A CD1 1 
ATOM   803  N  N   . SER   A 1 94  ? 8.202   -19.846 -22.153 1.00 13.59 ? 535  SER   A N   1 
ATOM   804  C  CA  . SER   A 1 94  ? 7.717   -20.940 -22.987 1.00 14.62 ? 535  SER   A CA  1 
ATOM   805  C  C   . SER   A 1 94  ? 8.896   -21.801 -23.433 1.00 16.27 ? 535  SER   A C   1 
ATOM   806  O  O   . SER   A 1 94  ? 10.066  -21.454 -23.226 1.00 15.42 ? 535  SER   A O   1 
ATOM   807  C  CB  . SER   A 1 94  ? 6.930   -20.410 -24.205 1.00 16.09 ? 535  SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 94  ? 7.763   -19.705 -25.123 1.00 16.80 ? 535  SER   A OG  1 
ATOM   809  N  N   . ASN   A 1 95  ? 8.594   -22.932 -24.080 1.00 17.23 ? 536  ASN   A N   1 
ATOM   810  C  CA  . ASN   A 1 95  ? 9.685   -23.788 -24.536 1.00 16.21 ? 536  ASN   A CA  1 
ATOM   811  C  C   . ASN   A 1 95  ? 10.551  -23.119 -25.593 1.00 17.63 ? 536  ASN   A C   1 
ATOM   812  O  O   . ASN   A 1 95  ? 11.637  -23.632 -25.883 1.00 20.38 ? 536  ASN   A O   1 
ATOM   813  C  CB  . ASN   A 1 95  ? 9.186   -25.131 -25.098 1.00 17.61 ? 536  ASN   A CB  1 
ATOM   814  C  CG  . ASN   A 1 95  ? 8.599   -26.042 -24.032 1.00 24.91 ? 536  ASN   A CG  1 
ATOM   815  O  OD1 . ASN   A 1 95  ? 7.487   -26.529 -24.182 1.00 28.18 ? 536  ASN   A OD1 1 
ATOM   816  N  ND2 . ASN   A 1 95  ? 9.334   -26.272 -22.955 1.00 19.14 ? 536  ASN   A ND2 1 
ATOM   817  N  N   . GLU   A 1 96  ? 10.113  -21.994 -26.166 1.00 17.26 ? 537  GLU   A N   1 
ATOM   818  C  CA  . GLU   A 1 96  ? 10.842  -21.274 -27.207 1.00 16.92 ? 537  GLU   A CA  1 
ATOM   819  C  C   . GLU   A 1 96  ? 11.647  -20.084 -26.678 1.00 16.37 ? 537  GLU   A C   1 
ATOM   820  O  O   . GLU   A 1 96  ? 12.429  -19.491 -27.440 1.00 17.14 ? 537  GLU   A O   1 
ATOM   821  C  CB  . GLU   A 1 96  ? 9.866   -20.764 -28.280 1.00 18.94 ? 537  GLU   A CB  1 
ATOM   822  C  CG  . GLU   A 1 96  ? 9.017   -21.848 -28.966 1.00 20.63 ? 537  GLU   A CG  1 
ATOM   823  C  CD  . GLU   A 1 96  ? 7.710   -22.170 -28.226 1.00 30.40 ? 537  GLU   A CD  1 
ATOM   824  O  OE1 . GLU   A 1 96  ? 7.406   -21.538 -27.192 1.00 20.77 ? 537  GLU   A OE1 1 
ATOM   825  O  OE2 . GLU   A 1 96  ? 6.970   -23.055 -28.696 1.00 44.83 ? 537  GLU   A OE2 1 
ATOM   826  N  N   . SER   A 1 97  ? 11.494  -19.742 -25.401 1.00 15.08 ? 538  SER   A N   1 
ATOM   827  C  CA  . SER   A 1 97  ? 12.059  -18.504 -24.866 1.00 13.23 ? 538  SER   A CA  1 
ATOM   828  C  C   . SER   A 1 97  ? 13.575  -18.478 -24.940 1.00 13.22 ? 538  SER   A C   1 
ATOM   829  O  O   . SER   A 1 97  ? 14.163  -17.468 -25.334 1.00 13.34 ? 538  SER   A O   1 
ATOM   830  C  CB  . SER   A 1 97  ? 11.621  -18.299 -23.417 1.00 13.75 ? 538  SER   A CB  1 
ATOM   831  O  OG  . SER   A 1 97  ? 10.214  -18.290 -23.324 1.00 13.49 ? 538  SER   A OG  1 
ATOM   832  N  N   . TYR   A 1 98  ? 14.230  -19.548 -24.490 1.00 14.87 ? 539  TYR   A N   1 
ATOM   833  C  CA  . TYR   A 1 98  ? 15.687  -19.563 -24.496 1.00 14.95 ? 539  TYR   A CA  1 
ATOM   834  C  C   . TYR   A 1 98  ? 16.234  -19.320 -25.900 1.00 14.57 ? 539  TYR   A C   1 
ATOM   835  O  O   . TYR   A 1 98  ? 17.104  -18.461 -26.109 1.00 15.16 ? 539  TYR   A O   1 
ATOM   836  C  CB  . TYR   A 1 98  ? 16.176  -20.895 -23.927 1.00 17.57 ? 539  TYR   A CB  1 
ATOM   837  C  CG  . TYR   A 1 98  ? 17.660  -21.143 -24.045 1.00 17.18 ? 539  TYR   A CG  1 
ATOM   838  C  CD1 . TYR   A 1 98  ? 18.572  -20.406 -23.293 1.00 17.00 ? 539  TYR   A CD1 1 
ATOM   839  C  CD2 . TYR   A 1 98  ? 18.145  -22.145 -24.876 1.00 17.81 ? 539  TYR   A CD2 1 
ATOM   840  C  CE1 . TYR   A 1 98  ? 19.934  -20.654 -23.391 1.00 16.53 ? 539  TYR   A CE1 1 
ATOM   841  C  CE2 . TYR   A 1 98  ? 19.506  -22.391 -24.979 1.00 17.05 ? 539  TYR   A CE2 1 
ATOM   842  C  CZ  . TYR   A 1 98  ? 20.373  -21.641 -24.230 1.00 15.68 ? 539  TYR   A CZ  1 
ATOM   843  O  OH  . TYR   A 1 98  ? 21.725  -21.870 -24.291 1.00 21.14 ? 539  TYR   A OH  1 
ATOM   844  N  N   . THR   A 1 99  ? 15.725  -20.058 -26.884 1.00 15.18 ? 540  THR   A N   1 
ATOM   845  C  CA  . THR   A 1 99  ? 16.223  -19.881 -28.246 1.00 16.82 ? 540  THR   A CA  1 
ATOM   846  C  C   . THR   A 1 99  ? 15.962  -18.464 -28.744 1.00 14.22 ? 540  THR   A C   1 
ATOM   847  O  O   . THR   A 1 99  ? 16.804  -17.864 -29.422 1.00 15.35 ? 540  THR   A O   1 
ATOM   848  C  CB  . THR   A 1 99  ? 15.595  -20.922 -29.169 1.00 20.44 ? 540  THR   A CB  1 
ATOM   849  O  OG1 . THR   A 1 99  ? 15.906  -22.233 -28.681 1.00 27.60 ? 540  THR   A OG1 1 
ATOM   850  C  CG2 . THR   A 1 99  ? 16.132  -20.779 -30.578 1.00 21.82 ? 540  THR   A CG2 1 
ATOM   851  N  N   . CYS   A 1 100 ? 14.806  -17.894 -28.387 1.00 12.36 ? 541  CYS   A N   1 
ATOM   852  C  CA  . CYS   A 1 100 ? 14.516  -16.531 -28.829 1.00 16.07 ? 541  CYS   A CA  1 
ATOM   853  C  C   . CYS   A 1 100 ? 15.493  -15.539 -28.218 1.00 12.83 ? 541  CYS   A C   1 
ATOM   854  O  O   . CYS   A 1 100 ? 15.968  -14.627 -28.901 1.00 13.11 ? 541  CYS   A O   1 
ATOM   855  C  CB  . CYS   A 1 100 ? 13.084  -16.151 -28.461 1.00 13.43 ? 541  CYS   A CB  1 
ATOM   856  S  SG  . CYS   A 1 100 ? 11.899  -17.006 -29.534 1.00 17.67 ? 541  CYS   A SG  1 
ATOM   857  N  N   . ALA   A 1 101 ? 15.804  -15.709 -26.934 1.00 13.32 ? 542  ALA   A N   1 
ATOM   858  C  CA  . ALA   A 1 101 ? 16.782  -14.840 -26.294 1.00 12.09 ? 542  ALA   A CA  1 
ATOM   859  C  C   . ALA   A 1 101 ? 18.165  -14.986 -26.930 1.00 13.66 ? 542  ALA   A C   1 
ATOM   860  O  O   . ALA   A 1 101 ? 18.883  -13.991 -27.104 1.00 12.59 ? 542  ALA   A O   1 
ATOM   861  C  CB  . ALA   A 1 101 ? 16.858  -15.135 -24.805 1.00 14.64 ? 542  ALA   A CB  1 
ATOM   862  N  N   . LEU   A 1 102 ? 18.551  -16.215 -27.309 1.00 12.35 ? 543  LEU   A N   1 
ATOM   863  C  CA  . LEU   A 1 102 ? 19.820  -16.415 -28.011 1.00 14.85 ? 543  LEU   A CA  1 
ATOM   864  C  C   . LEU   A 1 102 ? 19.808  -15.698 -29.341 1.00 14.40 ? 543  LEU   A C   1 
ATOM   865  O  O   . LEU   A 1 102 ? 20.812  -15.108 -29.756 1.00 12.55 ? 543  LEU   A O   1 
ATOM   866  C  CB  . LEU   A 1 102 ? 20.055  -17.906 -28.264 1.00 15.59 ? 543  LEU   A CB  1 
ATOM   867  C  CG  . LEU   A 1 102 ? 20.340  -18.840 -27.091 1.00 15.81 ? 543  LEU   A CG  1 
ATOM   868  C  CD1 . LEU   A 1 102 ? 20.657  -20.229 -27.643 1.00 20.07 ? 543  LEU   A CD1 1 
ATOM   869  C  CD2 . LEU   A 1 102 ? 21.487  -18.310 -26.240 1.00 16.84 ? 543  LEU   A CD2 1 
ATOM   870  N  N   . LEU   A 1 103 ? 18.675  -15.757 -30.033 1.00 12.00 ? 544  LEU   A N   1 
ATOM   871  C  CA  . LEU   A 1 103 ? 18.555  -15.099 -31.324 1.00 14.97 ? 544  LEU   A CA  1 
ATOM   872  C  C   . LEU   A 1 103 ? 18.645  -13.586 -31.192 1.00 13.99 ? 544  LEU   A C   1 
ATOM   873  O  O   . LEU   A 1 103 ? 19.264  -12.921 -32.029 1.00 14.76 ? 544  LEU   A O   1 
ATOM   874  C  CB  . LEU   A 1 103 ? 17.237  -15.494 -31.970 1.00 17.21 ? 544  LEU   A CB  1 
ATOM   875  C  CG  . LEU   A 1 103 ? 17.254  -16.488 -33.108 1.00 33.98 ? 544  LEU   A CG  1 
ATOM   876  C  CD1 . LEU   A 1 103 ? 15.813  -16.765 -33.513 1.00 25.22 ? 544  LEU   A CD1 1 
ATOM   877  C  CD2 . LEU   A 1 103 ? 18.053  -15.926 -34.281 1.00 25.83 ? 544  LEU   A CD2 1 
ATOM   878  N  N   . ALA   A 1 104 ? 18.014  -13.017 -30.158 1.00 14.12 ? 545  ALA   A N   1 
ATOM   879  C  CA  . ALA   A 1 104 ? 18.105  -11.576 -29.940 1.00 13.57 ? 545  ALA   A CA  1 
ATOM   880  C  C   . ALA   A 1 104 ? 19.563  -11.164 -29.765 1.00 13.53 ? 545  ALA   A C   1 
ATOM   881  O  O   . ALA   A 1 104 ? 20.035  -10.210 -30.394 1.00 15.24 ? 545  ALA   A O   1 
ATOM   882  C  CB  . ALA   A 1 104 ? 17.239  -11.169 -28.735 1.00 12.94 ? 545  ALA   A CB  1 
ATOM   883  N  N   . ALA   A 1 105 ? 20.305  -11.904 -28.938 1.00 13.00 ? 546  ALA   A N   1 
ATOM   884  C  CA  . ALA   A 1 105 ? 21.697  -11.547 -28.687 1.00 11.92 ? 546  ALA   A CA  1 
ATOM   885  C  C   . ALA   A 1 105 ? 22.564  -11.750 -29.932 1.00 13.58 ? 546  ALA   A C   1 
ATOM   886  O  O   . ALA   A 1 105 ? 23.322  -10.850 -30.318 1.00 13.56 ? 546  ALA   A O   1 
ATOM   887  C  CB  . ALA   A 1 105 ? 22.234  -12.333 -27.487 1.00 13.97 ? 546  ALA   A CB  1 
ATOM   888  N  N   . GLY   A 1 106 ? 22.438  -12.903 -30.595 1.00 13.43 ? 547  GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 106 ? 23.284  -13.168 -31.753 1.00 13.51 ? 547  GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 106 ? 23.025  -12.193 -32.888 1.00 14.51 ? 547  GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 106 ? 23.944  -11.782 -33.592 1.00 15.53 ? 547  GLY   A O   1 
ATOM   892  N  N   . SER   A 1 107 ? 21.768  -11.794 -33.058 1.00 15.57 ? 548  SER   A N   1 
ATOM   893  C  CA  . SER   A 1 107 ? 21.429  -10.739 -34.009 1.00 14.72 ? 548  SER   A CA  1 
ATOM   894  C  C   . SER   A 1 107 ? 22.205  -9.466  -33.720 1.00 13.30 ? 548  SER   A C   1 
ATOM   895  O  O   . SER   A 1 107 ? 22.739  -8.826  -34.637 1.00 14.26 ? 548  SER   A O   1 
ATOM   896  C  CB  . SER   A 1 107 ? 19.937  -10.432 -33.918 1.00 16.03 ? 548  SER   A CB  1 
ATOM   897  O  OG  . SER   A 1 107 ? 19.218  -11.537 -34.415 1.00 17.93 ? 548  SER   A OG  1 
ATOM   898  N  N   . CYS   A 1 108 ? 22.290  -9.093  -32.451 1.00 13.05 ? 549  CYS   A N   1 
ATOM   899  C  CA  . CYS   A 1 108 ? 23.001  -7.887  -32.075 1.00 13.21 ? 549  CYS   A CA  1 
ATOM   900  C  C   . CYS   A 1 108 ? 24.508  -8.062  -32.226 1.00 14.64 ? 549  CYS   A C   1 
ATOM   901  O  O   . CYS   A 1 108 ? 25.201  -7.109  -32.604 1.00 14.66 ? 549  CYS   A O   1 
ATOM   902  C  CB  . CYS   A 1 108 ? 22.611  -7.466  -30.656 1.00 10.06 ? 549  CYS   A CB  1 
ATOM   903  S  SG  . CYS   A 1 108 ? 20.934  -6.838  -30.592 1.00 14.34 ? 549  CYS   A SG  1 
ATOM   904  N  N   . PHE   A 1 109 ? 25.032  -9.259  -31.953 1.00 15.46 ? 550  PHE   A N   1 
ATOM   905  C  CA  . PHE   A 1 109 ? 26.456  -9.503  -32.197 1.00 11.95 ? 550  PHE   A CA  1 
ATOM   906  C  C   . PHE   A 1 109 ? 26.788  -9.341  -33.673 1.00 14.67 ? 550  PHE   A C   1 
ATOM   907  O  O   . PHE   A 1 109 ? 27.774  -8.680  -34.027 1.00 14.51 ? 550  PHE   A O   1 
ATOM   908  C  CB  . PHE   A 1 109 ? 26.857  -10.908 -31.750 1.00 15.07 ? 550  PHE   A CB  1 
ATOM   909  C  CG  . PHE   A 1 109 ? 26.621  -11.194 -30.296 1.00 13.67 ? 550  PHE   A CG  1 
ATOM   910  C  CD1 . PHE   A 1 109 ? 26.404  -10.182 -29.390 1.00 13.53 ? 550  PHE   A CD1 1 
ATOM   911  C  CD2 . PHE   A 1 109 ? 26.611  -12.512 -29.843 1.00 13.71 ? 550  PHE   A CD2 1 
ATOM   912  C  CE1 . PHE   A 1 109 ? 26.151  -10.480 -28.039 1.00 16.57 ? 550  PHE   A CE1 1 
ATOM   913  C  CE2 . PHE   A 1 109 ? 26.384  -12.825 -28.504 1.00 14.87 ? 550  PHE   A CE2 1 
ATOM   914  C  CZ  . PHE   A 1 109 ? 26.151  -11.800 -27.606 1.00 16.45 ? 550  PHE   A CZ  1 
ATOM   915  N  N   . ASN   A 1 110 ? 25.988  -9.945  -34.556 1.00 14.38 ? 551  ASN   A N   1 
ATOM   916  C  CA  . ASN   A 1 110 ? 26.268  -9.804  -35.984 1.00 16.30 ? 551  ASN   A CA  1 
ATOM   917  C  C   . ASN   A 1 110 ? 26.196  -8.349  -36.413 1.00 18.02 ? 551  ASN   A C   1 
ATOM   918  O  O   . ASN   A 1 110 ? 26.960  -7.924  -37.288 1.00 15.41 ? 551  ASN   A O   1 
ATOM   919  C  CB  . ASN   A 1 110 ? 25.306  -10.643 -36.830 1.00 15.49 ? 551  ASN   A CB  1 
ATOM   920  C  CG  . ASN   A 1 110 ? 25.723  -12.108 -36.918 1.00 18.29 ? 551  ASN   A CG  1 
ATOM   921  O  OD1 . ASN   A 1 110 ? 26.809  -12.482 -36.458 1.00 17.17 ? 551  ASN   A OD1 1 
ATOM   922  N  ND2 . ASN   A 1 110 ? 24.891  -12.935 -37.535 1.00 17.63 ? 551  ASN   A ND2 1 
ATOM   923  N  N   . SER   A 1 111 ? 25.298  -7.568  -35.812 1.00 15.97 ? 552  SER   A N   1 
ATOM   924  C  CA  . SER   A 1 111 ? 25.204  -6.154  -36.160 1.00 16.42 ? 552  SER   A CA  1 
ATOM   925  C  C   . SER   A 1 111 ? 26.442  -5.395  -35.694 1.00 16.12 ? 552  SER   A C   1 
ATOM   926  O  O   . SER   A 1 111 ? 27.007  -4.586  -36.447 1.00 15.32 ? 552  SER   A O   1 
ATOM   927  C  CB  . SER   A 1 111 ? 23.937  -5.545  -35.547 1.00 16.36 ? 552  SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 111 ? 22.782  -6.179  -36.060 1.00 15.70 ? 552  SER   A OG  1 
ATOM   929  N  N   . ALA   A 1 112 ? 26.870  -5.639  -34.448 1.00 13.82 ? 553  ALA   A N   1 
ATOM   930  C  CA  . ALA   A 1 112 ? 28.074  -4.994  -33.941 1.00 15.29 ? 553  ALA   A CA  1 
ATOM   931  C  C   . ALA   A 1 112 ? 29.278  -5.369  -34.782 1.00 14.22 ? 553  ALA   A C   1 
ATOM   932  O  O   . ALA   A 1 112 ? 30.138  -4.524  -35.044 1.00 15.06 ? 553  ALA   A O   1 
ATOM   933  C  CB  . ALA   A 1 112 ? 28.318  -5.372  -32.481 1.00 16.37 ? 553  ALA   A CB  1 
ATOM   934  N  N   . GLN   A 1 113 ? 29.372  -6.637  -35.175 1.00 13.44 ? 554  GLN   A N   1 
ATOM   935  C  CA  . GLN   A 1 113 ? 30.492  -7.079  -35.994 1.00 15.60 ? 554  GLN   A CA  1 
ATOM   936  C  C   . GLN   A 1 113 ? 30.490  -6.369  -37.344 1.00 18.19 ? 554  GLN   A C   1 
ATOM   937  O  O   . GLN   A 1 113 ? 31.550  -5.978  -37.851 1.00 15.96 ? 554  GLN   A O   1 
ATOM   938  C  CB  . GLN   A 1 113 ? 30.386  -8.580  -36.196 1.00 16.33 ? 554  GLN   A CB  1 
ATOM   939  C  CG  . GLN   A 1 113 ? 31.476  -9.196  -37.050 1.00 19.40 ? 554  GLN   A CG  1 
ATOM   940  C  CD  . GLN   A 1 113 ? 31.244  -10.673 -37.208 1.00 22.14 ? 554  GLN   A CD  1 
ATOM   941  O  OE1 . GLN   A 1 113 ? 30.196  -11.099 -37.712 1.00 32.48 ? 554  GLN   A OE1 1 
ATOM   942  N  NE2 . GLN   A 1 113 ? 32.206  -11.472 -36.782 1.00 29.52 ? 554  GLN   A NE2 1 
ATOM   943  N  N   . ALA   A 1 114 ? 29.310  -6.183  -37.940 1.00 15.29 ? 555  ALA   A N   1 
ATOM   944  C  CA  . ALA   A 1 114 ? 29.234  -5.467  -39.205 1.00 15.99 ? 555  ALA   A CA  1 
ATOM   945  C  C   . ALA   A 1 114 ? 29.672  -4.013  -39.060 1.00 16.64 ? 555  ALA   A C   1 
ATOM   946  O  O   . ALA   A 1 114 ? 30.375  -3.484  -39.928 1.00 16.38 ? 555  ALA   A O   1 
ATOM   947  C  CB  . ALA   A 1 114 ? 27.828  -5.585  -39.778 1.00 16.73 ? 555  ALA   A CB  1 
ATOM   948  N  N   . ILE   A 1 115 ? 29.297  -3.352  -37.965 1.00 14.12 ? 556  ILE   A N   1 
ATOM   949  C  CA  . ILE   A 1 115 ? 29.751  -1.985  -37.714 1.00 15.46 ? 556  ILE   A CA  1 
ATOM   950  C  C   . ILE   A 1 115 ? 31.264  -1.952  -37.514 1.00 17.76 ? 556  ILE   A C   1 
ATOM   951  O  O   . ILE   A 1 115 ? 31.970  -1.119  -38.099 1.00 18.33 ? 556  ILE   A O   1 
ATOM   952  C  CB  . ILE   A 1 115 ? 29.007  -1.383  -36.507 1.00 14.99 ? 556  ILE   A CB  1 
ATOM   953  C  CG1 . ILE   A 1 115 ? 27.537  -1.199  -36.845 1.00 14.90 ? 556  ILE   A CG1 1 
ATOM   954  C  CG2 . ILE   A 1 115 ? 29.608  -0.068  -36.110 1.00 18.43 ? 556  ILE   A CG2 1 
ATOM   955  C  CD1 . ILE   A 1 115 ? 26.663  -0.851  -35.646 1.00 19.00 ? 556  ILE   A CD1 1 
ATOM   956  N  N   . LEU   A 1 116 ? 31.783  -2.844  -36.674 1.00 17.66 ? 557  LEU   A N   1 
ATOM   957  C  CA  . LEU   A 1 116 ? 33.178  -2.765  -36.260 1.00 17.40 ? 557  LEU   A CA  1 
ATOM   958  C  C   . LEU   A 1 116 ? 34.159  -3.240  -37.328 1.00 23.90 ? 557  LEU   A C   1 
ATOM   959  O  O   . LEU   A 1 116 ? 35.356  -2.937  -37.231 1.00 23.87 ? 557  LEU   A O   1 
ATOM   960  C  CB  . LEU   A 1 116 ? 33.384  -3.547  -34.973 1.00 17.54 ? 557  LEU   A CB  1 
ATOM   961  C  CG  . LEU   A 1 116 ? 32.636  -2.947  -33.786 1.00 19.56 ? 557  LEU   A CG  1 
ATOM   962  C  CD1 . LEU   A 1 116 ? 32.656  -3.960  -32.657 1.00 18.35 ? 557  LEU   A CD1 1 
ATOM   963  C  CD2 . LEU   A 1 116 ? 33.249  -1.639  -33.354 1.00 18.41 ? 557  LEU   A CD2 1 
ATOM   964  N  N   . THR   A 1 117 ? 33.699  -3.983  -38.322 1.00 15.38 ? 558  THR   A N   1 
ATOM   965  C  CA  . THR   A 1 117 ? 34.522  -4.335  -39.481 1.00 16.37 ? 558  THR   A CA  1 
ATOM   966  C  C   . THR   A 1 117 ? 34.291  -3.404  -40.657 1.00 18.87 ? 558  THR   A C   1 
ATOM   967  O  O   . THR   A 1 117 ? 34.864  -3.622  -41.733 1.00 20.76 ? 558  THR   A O   1 
ATOM   968  C  CB  . THR   A 1 117 ? 34.279  -5.784  -39.922 1.00 19.08 ? 558  THR   A CB  1 
ATOM   969  O  OG1 . THR   A 1 117 ? 32.903  -5.945  -40.320 1.00 19.45 ? 558  THR   A OG1 1 
ATOM   970  C  CG2 . THR   A 1 117 ? 34.615  -6.743  -38.799 1.00 20.73 ? 558  THR   A CG2 1 
ATOM   971  N  N   . GLY   A 1 118 ? 33.488  -2.366  -40.485 1.00 19.92 ? 559  GLY   A N   1 
ATOM   972  C  CA  . GLY   A 1 118 ? 33.276  -1.398  -41.537 1.00 24.36 ? 559  GLY   A CA  1 
ATOM   973  C  C   . GLY   A 1 118 ? 32.342  -1.830  -42.644 1.00 22.19 ? 559  GLY   A C   1 
ATOM   974  O  O   . GLY   A 1 118 ? 32.301  -1.163  -43.684 1.00 32.12 ? 559  GLY   A O   1 
ATOM   975  N  N   . GLN   A 1 119 ? 31.597  -2.923  -42.463 1.00 19.65 ? 560  GLN   A N   1 
ATOM   976  C  CA  . GLN   A 1 119 ? 30.631  -3.355  -43.464 1.00 18.19 ? 560  GLN   A CA  1 
ATOM   977  C  C   . GLN   A 1 119 ? 29.433  -2.415  -43.530 1.00 24.52 ? 560  GLN   A C   1 
ATOM   978  O  O   . GLN   A 1 119 ? 28.880  -2.187  -44.610 1.00 21.58 ? 560  GLN   A O   1 
ATOM   979  C  CB  . GLN   A 1 119 ? 30.158  -4.778  -43.173 1.00 22.88 ? 560  GLN   A CB  1 
ATOM   980  C  CG  . GLN   A 1 119 ? 31.147  -5.880  -43.549 0.90 42.03 ? 560  GLN   A CG  1 
ATOM   981  C  CD  . GLN   A 1 119 ? 31.172  -6.178  -45.041 0.64 41.33 ? 560  GLN   A CD  1 
ATOM   982  O  OE1 . GLN   A 1 119 ? 32.203  -6.062  -45.689 0.51 30.45 ? 560  GLN   A OE1 1 
ATOM   983  N  NE2 . GLN   A 1 119 ? 30.028  -6.567  -45.590 0.59 29.01 ? 560  GLN   A NE2 1 
ATOM   984  N  N   . VAL   A 1 120 ? 28.985  -1.903  -42.377 1.00 19.75 ? 561  VAL   A N   1 
ATOM   985  C  CA  . VAL   A 1 120 ? 27.945  -0.887  -42.305 1.00 17.80 ? 561  VAL   A CA  1 
ATOM   986  C  C   . VAL   A 1 120 ? 28.424  0.217   -41.371 1.00 16.46 ? 561  VAL   A C   1 
ATOM   987  O  O   . VAL   A 1 120 ? 29.320  0.023   -40.546 1.00 17.59 ? 561  VAL   A O   1 
ATOM   988  C  CB  . VAL   A 1 120 ? 26.581  -1.453  -41.827 1.00 17.59 ? 561  VAL   A CB  1 
ATOM   989  C  CG1 . VAL   A 1 120 ? 26.141  -2.604  -42.706 1.00 20.53 ? 561  VAL   A CG1 1 
ATOM   990  C  CG2 . VAL   A 1 120 ? 26.684  -1.922  -40.370 1.00 18.66 ? 561  VAL   A CG2 1 
ATOM   991  N  N   . ARG   A 1 121 ? 27.798  1.391   -41.504 1.00 19.17 ? 562  ARG   A N   1 
ATOM   992  C  CA  . ARG   A 1 121 ? 28.122  2.492   -40.613 1.00 15.94 ? 562  ARG   A CA  1 
ATOM   993  C  C   . ARG   A 1 121 ? 27.366  2.392   -39.295 1.00 13.65 ? 562  ARG   A C   1 
ATOM   994  O  O   . ARG   A 1 121 ? 27.923  2.674   -38.231 1.00 17.61 ? 562  ARG   A O   1 
ATOM   995  C  CB  . ARG   A 1 121 ? 27.792  3.836   -41.262 1.00 22.80 ? 562  ARG   A CB  1 
ATOM   996  C  CG  . ARG   A 1 121 ? 28.141  5.021   -40.354 1.00 25.41 ? 562  ARG   A CG  1 
ATOM   997  C  CD  . ARG   A 1 121 ? 27.320  6.262   -40.655 1.00 55.49 ? 562  ARG   A CD  1 
ATOM   998  N  NE  . ARG   A 1 121 ? 28.167  7.453   -40.721 1.00 63.32 ? 562  ARG   A NE  1 
ATOM   999  C  CZ  . ARG   A 1 121 ? 27.817  8.659   -40.276 1.00 69.51 ? 562  ARG   A CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 121 ? 26.622  8.858   -39.718 1.00 32.82 ? 562  ARG   A NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 121 ? 28.666  9.672   -40.391 1.00 63.49 ? 562  ARG   A NH2 1 
ATOM   1002 N  N   . ASN   A 1 122 ? 26.080  2.026   -39.368 1.00 15.34 ? 563  ASN   A N   1 
ATOM   1003 C  CA  . ASN   A 1 122 ? 25.176  1.967   -38.220 1.00 15.08 ? 563  ASN   A CA  1 
ATOM   1004 C  C   . ASN   A 1 122 ? 24.158  0.852   -38.465 1.00 12.58 ? 563  ASN   A C   1 
ATOM   1005 O  O   . ASN   A 1 122 ? 24.164  0.214   -39.517 1.00 13.75 ? 563  ASN   A O   1 
ATOM   1006 C  CB  . ASN   A 1 122 ? 24.583  3.344   -37.957 1.00 13.85 ? 563  ASN   A CB  1 
ATOM   1007 C  CG  . ASN   A 1 122 ? 23.820  3.874   -39.146 1.00 15.21 ? 563  ASN   A CG  1 
ATOM   1008 O  OD1 . ASN   A 1 122 ? 23.178  3.112   -39.855 1.00 15.31 ? 563  ASN   A OD1 1 
ATOM   1009 N  ND2 . ASN   A 1 122 ? 23.903  5.184   -39.383 1.00 16.70 ? 563  ASN   A ND2 1 
ATOM   1010 N  N   . ALA   A 1 123 ? 23.303  0.587   -37.465 1.00 13.50 ? 564  ALA   A N   1 
ATOM   1011 C  CA  . ALA   A 1 123 ? 22.406  -0.549  -37.592 1.00 12.35 ? 564  ALA   A CA  1 
ATOM   1012 C  C   . ALA   A 1 123 ? 21.276  -0.471  -36.587 1.00 11.83 ? 564  ALA   A C   1 
ATOM   1013 O  O   . ALA   A 1 123 ? 21.374  0.193   -35.559 1.00 12.69 ? 564  ALA   A O   1 
ATOM   1014 C  CB  . ALA   A 1 123 ? 23.133  -1.900  -37.486 1.00 15.33 ? 564  ALA   A CB  1 
ATOM   1015 N  N   A VAL   A 1 124 ? 20.186  -1.153  -36.925 0.82 13.40 ? 565  VAL   A N   1 
ATOM   1016 N  N   B VAL   A 1 124 ? 20.199  -1.178  -36.915 0.18 11.94 ? 565  VAL   A N   1 
ATOM   1017 C  CA  A VAL   A 1 124 ? 19.023  -1.284  -36.048 0.82 14.40 ? 565  VAL   A CA  1 
ATOM   1018 C  CA  B VAL   A 1 124 ? 19.032  -1.324  -36.056 0.18 12.26 ? 565  VAL   A CA  1 
ATOM   1019 C  C   A VAL   A 1 124 ? 18.695  -2.768  -35.872 0.82 15.26 ? 565  VAL   A C   1 
ATOM   1020 C  C   B VAL   A 1 124 ? 18.794  -2.809  -35.839 0.18 7.11  ? 565  VAL   A C   1 
ATOM   1021 O  O   A VAL   A 1 124 ? 18.721  -3.541  -36.841 0.82 15.19 ? 565  VAL   A O   1 
ATOM   1022 O  O   B VAL   A 1 124 ? 18.973  -3.617  -36.758 0.18 14.89 ? 565  VAL   A O   1 
ATOM   1023 C  CB  A VAL   A 1 124 ? 17.815  -0.462  -36.580 0.82 12.92 ? 565  VAL   A CB  1 
ATOM   1024 C  CB  B VAL   A 1 124 ? 17.793  -0.658  -36.689 0.18 13.92 ? 565  VAL   A CB  1 
ATOM   1025 C  CG1 A VAL   A 1 124 ? 17.223  -1.070  -37.879 0.82 13.49 ? 565  VAL   A CG1 1 
ATOM   1026 C  CG1 B VAL   A 1 124 ? 16.495  -1.188  -36.085 0.18 13.31 ? 565  VAL   A CG1 1 
ATOM   1027 C  CG2 A VAL   A 1 124 ? 16.738  -0.306  -35.528 0.82 16.97 ? 565  VAL   A CG2 1 
ATOM   1028 C  CG2 B VAL   A 1 124 ? 17.877  0.816   -36.507 0.18 4.93  ? 565  VAL   A CG2 1 
ATOM   1029 N  N   . ALA   A 1 125 ? 18.378  -3.168  -34.627 1.00 12.00 ? 566  ALA   A N   1 
ATOM   1030 C  CA  . ALA   A 1 125 ? 18.097  -4.557  -34.287 1.00 12.23 ? 566  ALA   A CA  1 
ATOM   1031 C  C   . ALA   A 1 125 ? 16.683  -4.631  -33.729 1.00 12.40 ? 566  ALA   A C   1 
ATOM   1032 O  O   . ALA   A 1 125 ? 16.422  -4.141  -32.620 1.00 11.08 ? 566  ALA   A O   1 
ATOM   1033 C  CB  . ALA   A 1 125 ? 19.102  -5.103  -33.268 1.00 12.18 ? 566  ALA   A CB  1 
ATOM   1034 N  N   . ILE   A 1 126 ? 15.797  -5.286  -34.478 1.00 10.52 ? 567  ILE   A N   1 
ATOM   1035 C  CA  . ILE   A 1 126 ? 14.385  -5.441  -34.099 1.00 10.19 ? 567  ILE   A CA  1 
ATOM   1036 C  C   . ILE   A 1 126 ? 14.261  -6.819  -33.452 1.00 12.97 ? 567  ILE   A C   1 
ATOM   1037 O  O   . ILE   A 1 126 ? 14.055  -7.836  -34.132 1.00 12.27 ? 567  ILE   A O   1 
ATOM   1038 C  CB  . ILE   A 1 126 ? 13.465  -5.285  -35.309 1.00 12.51 ? 567  ILE   A CB  1 
ATOM   1039 C  CG1 . ILE   A 1 126 ? 13.755  -3.984  -36.057 1.00 13.07 ? 567  ILE   A CG1 1 
ATOM   1040 C  CG2 . ILE   A 1 126 ? 11.991  -5.380  -34.908 1.00 13.40 ? 567  ILE   A CG2 1 
ATOM   1041 C  CD1 . ILE   A 1 126 ? 13.145  -3.952  -37.467 1.00 14.83 ? 567  ILE   A CD1 1 
ATOM   1042 N  N   . VAL   A 1 127 ? 14.410  -6.860  -32.119 1.00 11.56 ? 568  VAL   A N   1 
ATOM   1043 C  CA  . VAL   A 1 127 ? 14.622  -8.108  -31.385 1.00 10.20 ? 568  VAL   A CA  1 
ATOM   1044 C  C   . VAL   A 1 127 ? 13.718  -8.174  -30.161 1.00 10.90 ? 568  VAL   A C   1 
ATOM   1045 O  O   . VAL   A 1 127 ? 13.363  -7.150  -29.568 1.00 11.62 ? 568  VAL   A O   1 
ATOM   1046 C  CB  . VAL   A 1 127 ? 16.106  -8.306  -30.940 1.00 10.72 ? 568  VAL   A CB  1 
ATOM   1047 C  CG1 . VAL   A 1 127 ? 17.027  -8.445  -32.157 1.00 13.83 ? 568  VAL   A CG1 1 
ATOM   1048 C  CG2 . VAL   A 1 127 ? 16.592  -7.157  -30.052 1.00 12.79 ? 568  VAL   A CG2 1 
ATOM   1049 N  N   . ARG   A 1 128 ? 13.379  -9.393  -29.752 1.00 11.22 ? 569  ARG   A N   1 
ATOM   1050 C  CA  . ARG   A 1 128 ? 12.739  -9.674  -28.477 1.00 9.38  ? 569  ARG   A CA  1 
ATOM   1051 C  C   . ARG   A 1 128 ? 13.075  -11.114 -28.113 1.00 11.39 ? 569  ARG   A C   1 
ATOM   1052 O  O   . ARG   A 1 128 ? 13.480  -11.896 -28.990 1.00 11.27 ? 569  ARG   A O   1 
ATOM   1053 C  CB  . ARG   A 1 128 ? 11.214  -9.497  -28.564 1.00 11.12 ? 569  ARG   A CB  1 
ATOM   1054 C  CG  . ARG   A 1 128 ? 10.524  -10.588 -29.389 1.00 10.64 ? 569  ARG   A CG  1 
ATOM   1055 C  CD  . ARG   A 1 128 ? 9.015   -10.363 -29.425 1.00 11.13 ? 569  ARG   A CD  1 
ATOM   1056 N  NE  . ARG   A 1 128 ? 8.278   -10.759 -28.227 1.00 12.04 ? 569  ARG   A NE  1 
ATOM   1057 C  CZ  . ARG   A 1 128 ? 7.833   -11.989 -27.986 1.00 12.39 ? 569  ARG   A CZ  1 
ATOM   1058 N  NH1 . ARG   A 1 128 ? 8.123   -12.985 -28.826 1.00 12.71 ? 569  ARG   A NH1 1 
ATOM   1059 N  NH2 . ARG   A 1 128 ? 7.060   -12.223 -26.914 1.00 11.46 ? 569  ARG   A NH2 1 
ATOM   1060 N  N   . PRO   A 1 129 ? 12.962  -11.494 -26.827 1.00 12.04 ? 570  PRO   A N   1 
ATOM   1061 C  CA  . PRO   A 1 129 ? 12.639  -10.678 -25.653 1.00 11.11 ? 570  PRO   A CA  1 
ATOM   1062 C  C   . PRO   A 1 129 ? 13.689  -9.614  -25.383 1.00 11.55 ? 570  PRO   A C   1 
ATOM   1063 O  O   . PRO   A 1 129 ? 14.802  -9.710  -25.899 1.00 12.35 ? 570  PRO   A O   1 
ATOM   1064 C  CB  . PRO   A 1 129 ? 12.629  -11.698 -24.497 1.00 11.67 ? 570  PRO   A CB  1 
ATOM   1065 C  CG  . PRO   A 1 129 ? 13.484  -12.822 -24.975 1.00 13.74 ? 570  PRO   A CG  1 
ATOM   1066 C  CD  . PRO   A 1 129 ? 13.249  -12.891 -26.455 1.00 14.28 ? 570  PRO   A CD  1 
ATOM   1067 N  N   . PRO   A 1 130 ? 13.340  -8.612  -24.580 1.00 11.05 ? 571  PRO   A N   1 
ATOM   1068 C  CA  . PRO   A 1 130 ? 14.295  -7.534  -24.255 1.00 10.86 ? 571  PRO   A CA  1 
ATOM   1069 C  C   . PRO   A 1 130 ? 15.402  -7.990  -23.315 1.00 11.96 ? 571  PRO   A C   1 
ATOM   1070 O  O   . PRO   A 1 130 ? 15.416  -9.151  -22.885 1.00 11.52 ? 571  PRO   A O   1 
ATOM   1071 C  CB  . PRO   A 1 130 ? 13.404  -6.474  -23.587 1.00 11.25 ? 571  PRO   A CB  1 
ATOM   1072 C  CG  . PRO   A 1 130 ? 12.237  -7.270  -23.019 1.00 10.48 ? 571  PRO   A CG  1 
ATOM   1073 C  CD  . PRO   A 1 130 ? 11.991  -8.368  -24.019 1.00 13.34 ? 571  PRO   A CD  1 
ATOM   1074 N  N   . GLY   A 1 131 ? 16.313  -7.086  -22.945 1.00 11.41 ? 572  GLY   A N   1 
ATOM   1075 C  CA  . GLY   A 1 131 ? 17.462  -7.526  -22.184 1.00 11.46 ? 572  GLY   A CA  1 
ATOM   1076 C  C   . GLY   A 1 131 ? 17.849  -6.710  -20.965 1.00 12.86 ? 572  GLY   A C   1 
ATOM   1077 O  O   . GLY   A 1 131 ? 18.492  -7.260  -20.063 1.00 11.67 ? 572  GLY   A O   1 
ATOM   1078 N  N   . HIS   A 1 132 ? 17.484  -5.424  -20.873 1.00 11.23 ? 573  HIS   A N   1 
ATOM   1079 C  CA  . HIS   A 1 132 ? 18.248  -4.574  -19.956 1.00 12.45 ? 573  HIS   A CA  1 
ATOM   1080 C  C   . HIS   A 1 132 ? 17.958  -4.798  -18.477 1.00 10.56 ? 573  HIS   A C   1 
ATOM   1081 O  O   . HIS   A 1 132 ? 18.751  -4.326  -17.645 1.00 12.81 ? 573  HIS   A O   1 
ATOM   1082 C  CB  . HIS   A 1 132 ? 18.134  -3.093  -20.315 1.00 12.17 ? 573  HIS   A CB  1 
ATOM   1083 C  CG  . HIS   A 1 132 ? 16.780  -2.493  -20.109 1.00 12.96 ? 573  HIS   A CG  1 
ATOM   1084 N  ND1 . HIS   A 1 132 ? 16.623  -1.151  -19.850 1.00 11.98 ? 573  HIS   A ND1 1 
ATOM   1085 C  CD2 . HIS   A 1 132 ? 15.526  -3.016  -20.153 1.00 14.65 ? 573  HIS   A CD2 1 
ATOM   1086 C  CE1 . HIS   A 1 132 ? 15.338  -0.868  -19.738 1.00 13.70 ? 573  HIS   A CE1 1 
ATOM   1087 N  NE2 . HIS   A 1 132 ? 14.646  -1.979  -19.921 1.00 14.52 ? 573  HIS   A NE2 1 
ATOM   1088 N  N   . HIS   A 1 133 ? 16.903  -5.510  -18.116 1.00 10.69 ? 574  HIS   A N   1 
ATOM   1089 C  CA  . HIS   A 1 133 ? 16.687  -5.874  -16.719 1.00 12.49 ? 574  HIS   A CA  1 
ATOM   1090 C  C   . HIS   A 1 133 ? 17.414  -7.154  -16.312 1.00 12.60 ? 574  HIS   A C   1 
ATOM   1091 O  O   . HIS   A 1 133 ? 17.488  -7.453  -15.106 1.00 13.53 ? 574  HIS   A O   1 
ATOM   1092 C  CB  . HIS   A 1 133 ? 15.199  -6.054  -16.426 1.00 12.52 ? 574  HIS   A CB  1 
ATOM   1093 C  CG  . HIS   A 1 133 ? 14.385  -4.812  -16.590 1.00 13.98 ? 574  HIS   A CG  1 
ATOM   1094 N  ND1 . HIS   A 1 133 ? 14.630  -3.656  -15.876 1.00 13.48 ? 574  HIS   A ND1 1 
ATOM   1095 C  CD2 . HIS   A 1 133 ? 13.317  -4.547  -17.383 1.00 14.06 ? 574  HIS   A CD2 1 
ATOM   1096 C  CE1 . HIS   A 1 133 ? 13.761  -2.728  -16.240 1.00 15.70 ? 574  HIS   A CE1 1 
ATOM   1097 N  NE2 . HIS   A 1 133 ? 12.939  -3.251  -17.131 1.00 14.21 ? 574  HIS   A NE2 1 
ATOM   1098 N  N   . ALA   A 1 134 ? 17.947  -7.916  -17.269 1.00 12.31 ? 575  ALA   A N   1 
ATOM   1099 C  CA  . ALA   A 1 134 ? 18.614  -9.168  -16.907 1.00 11.24 ? 575  ALA   A CA  1 
ATOM   1100 C  C   . ALA   A 1 134 ? 19.956  -8.894  -16.226 1.00 14.33 ? 575  ALA   A C   1 
ATOM   1101 O  O   . ALA   A 1 134 ? 20.745  -8.056  -16.689 1.00 13.42 ? 575  ALA   A O   1 
ATOM   1102 C  CB  . ALA   A 1 134 ? 18.808  -10.063 -18.123 1.00 12.97 ? 575  ALA   A CB  1 
ATOM   1103 N  N   . GLU   A 1 135 ? 20.202  -9.600  -15.120 1.00 15.14 ? 576  GLU   A N   1 
ATOM   1104 C  CA  . GLU   A 1 135 ? 21.415  -9.476  -14.320 1.00 17.74 ? 576  GLU   A CA  1 
ATOM   1105 C  C   . GLU   A 1 135 ? 22.358  -10.635 -14.634 1.00 14.46 ? 576  GLU   A C   1 
ATOM   1106 O  O   . GLU   A 1 135 ? 22.000  -11.588 -15.328 1.00 14.63 ? 576  GLU   A O   1 
ATOM   1107 C  CB  . GLU   A 1 135 ? 21.047  -9.478  -12.832 1.00 16.78 ? 576  GLU   A CB  1 
ATOM   1108 C  CG  . GLU   A 1 135 ? 20.075  -8.368  -12.422 1.00 18.05 ? 576  GLU   A CG  1 
ATOM   1109 C  CD  . GLU   A 1 135 ? 20.800  -7.109  -11.963 1.00 17.44 ? 576  GLU   A CD  1 
ATOM   1110 O  OE1 . GLU   A 1 135 ? 22.035  -7.116  -11.967 1.00 21.63 ? 576  GLU   A OE1 1 
ATOM   1111 O  OE2 . GLU   A 1 135 ? 20.147  -6.129  -11.557 1.00 22.33 ? 576  GLU   A OE2 1 
ATOM   1112 N  N   . LYS   A 1 136 ? 23.591  -10.539 -14.128 1.00 17.34 ? 577  LYS   A N   1 
ATOM   1113 C  CA  . LYS   A 1 136 ? 24.542  -11.629 -14.325 1.00 17.02 ? 577  LYS   A CA  1 
ATOM   1114 C  C   . LYS   A 1 136 ? 23.922  -12.974 -13.958 1.00 13.05 ? 577  LYS   A C   1 
ATOM   1115 O  O   . LYS   A 1 136 ? 24.059  -13.961 -14.692 1.00 15.82 ? 577  LYS   A O   1 
ATOM   1116 C  CB  . LYS   A 1 136 ? 25.796  -11.375 -13.480 1.00 19.22 ? 577  LYS   A CB  1 
ATOM   1117 C  CG  . LYS   A 1 136 ? 26.765  -12.543 -13.492 1.00 20.03 ? 577  LYS   A CG  1 
ATOM   1118 C  CD  . LYS   A 1 136 ? 27.893  -12.342 -12.472 1.00 28.80 ? 577  LYS   A CD  1 
ATOM   1119 C  CE  . LYS   A 1 136 ? 29.186  -12.991 -12.932 1.00 46.72 ? 577  LYS   A CE  1 
ATOM   1120 N  NZ  . LYS   A 1 136 ? 29.027  -14.456 -13.154 1.00 49.61 ? 577  LYS   A NZ  1 
ATOM   1121 N  N   . ASP   A 1 137 ? 23.170  -13.004 -12.864 1.00 14.98 ? 578  ASP   A N   1 
ATOM   1122 C  CA  . ASP   A 1 137 ? 22.709  -14.247 -12.260 1.00 16.71 ? 578  ASP   A CA  1 
ATOM   1123 C  C   . ASP   A 1 137 ? 21.193  -14.441 -12.288 1.00 15.49 ? 578  ASP   A C   1 
ATOM   1124 O  O   . ASP   A 1 137 ? 20.707  -15.408 -11.693 1.00 17.63 ? 578  ASP   A O   1 
ATOM   1125 C  CB  . ASP   A 1 137 ? 23.230  -14.338 -10.816 1.00 18.13 ? 578  ASP   A CB  1 
ATOM   1126 C  CG  . ASP   A 1 137 ? 23.225  -15.750 -10.276 1.00 52.55 ? 578  ASP   A CG  1 
ATOM   1127 O  OD1 . ASP   A 1 137 ? 23.949  -16.617 -10.818 1.00 42.34 ? 578  ASP   A OD1 1 
ATOM   1128 O  OD2 . ASP   A 1 137 ? 22.499  -16.007 -9.291  1.00 43.94 ? 578  ASP   A OD2 1 
ATOM   1129 N  N   . THR   A 1 138 ? 20.423  -13.563 -12.937 1.00 15.87 ? 579  THR   A N   1 
ATOM   1130 C  CA  . THR   A 1 138 ? 18.975  -13.722 -12.852 1.00 16.07 ? 579  THR   A CA  1 
ATOM   1131 C  C   . THR   A 1 138 ? 18.262  -13.022 -14.002 1.00 14.43 ? 579  THR   A C   1 
ATOM   1132 O  O   . THR   A 1 138 ? 18.781  -12.083 -14.608 1.00 16.61 ? 579  THR   A O   1 
ATOM   1133 C  CB  . THR   A 1 138 ? 18.448  -13.272 -11.483 1.00 18.43 ? 579  THR   A CB  1 
ATOM   1134 O  OG1 . THR   A 1 138 ? 17.242  -13.966 -11.211 1.00 18.67 ? 579  THR   A OG1 1 
ATOM   1135 C  CG2 . THR   A 1 138 ? 18.209  -11.771 -11.413 1.00 18.72 ? 579  THR   A CG2 1 
ATOM   1136 N  N   . ALA   A 1 139 ? 17.058  -13.523 -14.295 1.00 14.51 ? 580  ALA   A N   1 
ATOM   1137 C  CA  . ALA   A 1 139 ? 16.134  -12.951 -15.263 1.00 15.52 ? 580  ALA   A CA  1 
ATOM   1138 C  C   . ALA   A 1 139 ? 15.183  -12.014 -14.531 1.00 17.23 ? 580  ALA   A C   1 
ATOM   1139 O  O   . ALA   A 1 139 ? 14.958  -12.157 -13.328 1.00 15.89 ? 580  ALA   A O   1 
ATOM   1140 C  CB  . ALA   A 1 139 ? 15.330  -14.059 -15.952 1.00 14.29 ? 580  ALA   A CB  1 
ATOM   1141 N  N   . CYS   A 1 140 ? 14.648  -11.034 -15.254 1.00 15.65 ? 581  CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 140 ? 13.819  -10.010 -14.621 1.00 13.41 ? 581  CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 140 ? 13.120  -9.184  -15.694 1.00 13.87 ? 581  CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 140 ? 13.699  -8.911  -16.752 1.00 12.00 ? 581  CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 140 ? 14.680  -9.066  -13.763 1.00 12.97 ? 581  CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 140 ? 13.712  -7.744  -12.993 1.00 18.10 ? 581  CYS   A SG  1 
ATOM   1147 N  N   . GLY   A 1 141 ? 11.882  -8.770  -15.418 1.00 13.77 ? 582  GLY   A N   1 
ATOM   1148 C  CA  . GLY   A 1 141 ? 11.248  -7.752  -16.239 1.00 13.60 ? 582  GLY   A CA  1 
ATOM   1149 C  C   . GLY   A 1 141 ? 11.204  -8.060  -17.722 1.00 12.76 ? 582  GLY   A C   1 
ATOM   1150 O  O   . GLY   A 1 141 ? 11.531  -7.206  -18.552 1.00 12.74 ? 582  GLY   A O   1 
ATOM   1151 N  N   . PHE   A 1 142 ? 10.774  -9.270  -18.068 1.00 12.56 ? 583  PHE   A N   1 
ATOM   1152 C  CA  . PHE   A 1 142 ? 10.622  -9.759  -19.432 1.00 13.33 ? 583  PHE   A CA  1 
ATOM   1153 C  C   . PHE   A 1 142 ? 11.960  -10.109 -20.087 1.00 13.07 ? 583  PHE   A C   1 
ATOM   1154 O  O   . PHE   A 1 142 ? 11.966  -10.464 -21.267 1.00 12.29 ? 583  PHE   A O   1 
ATOM   1155 C  CB  . PHE   A 1 142 ? 9.822   -8.823  -20.373 1.00 12.12 ? 583  PHE   A CB  1 
ATOM   1156 C  CG  . PHE   A 1 142 ? 8.552   -8.233  -19.784 1.00 14.15 ? 583  PHE   A CG  1 
ATOM   1157 C  CD1 . PHE   A 1 142 ? 7.908   -8.813  -18.703 1.00 15.90 ? 583  PHE   A CD1 1 
ATOM   1158 C  CD2 . PHE   A 1 142 ? 8.025   -7.062  -20.322 1.00 17.32 ? 583  PHE   A CD2 1 
ATOM   1159 C  CE1 . PHE   A 1 142 ? 6.740   -8.247  -18.177 1.00 15.91 ? 583  PHE   A CE1 1 
ATOM   1160 C  CE2 . PHE   A 1 142 ? 6.864   -6.496  -19.811 1.00 16.77 ? 583  PHE   A CE2 1 
ATOM   1161 C  CZ  . PHE   A 1 142 ? 6.224   -7.093  -18.724 1.00 15.93 ? 583  PHE   A CZ  1 
ATOM   1162 N  N   . CYS   A 1 143 ? 13.083  -10.006 -19.371 1.00 12.27 ? 584  CYS   A N   1 
ATOM   1163 C  CA  . CYS   A 1 143 ? 14.426  -10.119 -19.934 1.00 12.24 ? 584  CYS   A CA  1 
ATOM   1164 C  C   . CYS   A 1 143 ? 15.130  -11.359 -19.386 1.00 12.74 ? 584  CYS   A C   1 
ATOM   1165 O  O   . CYS   A 1 143 ? 15.162  -11.576 -18.163 1.00 13.95 ? 584  CYS   A O   1 
ATOM   1166 C  CB  . CYS   A 1 143 ? 15.248  -8.894  -19.526 1.00 13.31 ? 584  CYS   A CB  1 
ATOM   1167 S  SG  . CYS   A 1 143 ? 14.598  -7.300  -20.046 1.00 12.41 ? 584  CYS   A SG  1 
ATOM   1168 N  N   . PHE   A 1 144 ? 15.716  -12.156 -20.290 1.00 11.68 ? 585  PHE   A N   1 
ATOM   1169 C  CA  . PHE   A 1 144 ? 16.474  -13.342 -19.874 1.00 12.07 ? 585  PHE   A CA  1 
ATOM   1170 C  C   . PHE   A 1 144 ? 17.983  -13.131 -19.836 1.00 12.35 ? 585  PHE   A C   1 
ATOM   1171 O  O   . PHE   A 1 144 ? 18.638  -13.464 -18.827 1.00 13.54 ? 585  PHE   A O   1 
ATOM   1172 C  CB  . PHE   A 1 144 ? 16.157  -14.514 -20.801 1.00 13.97 ? 585  PHE   A CB  1 
ATOM   1173 C  CG  . PHE   A 1 144 ? 14.734  -14.947 -20.703 1.00 13.28 ? 585  PHE   A CG  1 
ATOM   1174 C  CD1 . PHE   A 1 144 ? 14.348  -15.850 -19.736 1.00 14.20 ? 585  PHE   A CD1 1 
ATOM   1175 C  CD2 . PHE   A 1 144 ? 13.772  -14.411 -21.542 1.00 15.09 ? 585  PHE   A CD2 1 
ATOM   1176 C  CE1 . PHE   A 1 144 ? 13.011  -16.229 -19.612 1.00 14.73 ? 585  PHE   A CE1 1 
ATOM   1177 C  CE2 . PHE   A 1 144 ? 12.434  -14.780 -21.428 1.00 13.35 ? 585  PHE   A CE2 1 
ATOM   1178 C  CZ  . PHE   A 1 144 ? 12.059  -15.687 -20.470 1.00 15.34 ? 585  PHE   A CZ  1 
ATOM   1179 N  N   . PHE   A 1 145 ? 18.538  -12.594 -20.911 1.00 11.84 ? 586  PHE   A N   1 
ATOM   1180 C  CA  . PHE   A 1 145 ? 19.953  -12.284 -21.006 1.00 13.03 ? 586  PHE   A CA  1 
ATOM   1181 C  C   . PHE   A 1 145 ? 20.080  -10.826 -21.405 1.00 14.11 ? 586  PHE   A C   1 
ATOM   1182 O  O   . PHE   A 1 145 ? 19.214  -10.277 -22.103 1.00 12.45 ? 586  PHE   A O   1 
ATOM   1183 C  CB  . PHE   A 1 145 ? 20.680  -13.196 -22.006 1.00 14.13 ? 586  PHE   A CB  1 
ATOM   1184 C  CG  . PHE   A 1 145 ? 20.483  -14.663 -21.742 1.00 13.91 ? 586  PHE   A CG  1 
ATOM   1185 C  CD1 . PHE   A 1 145 ? 20.859  -15.219 -20.540 1.00 13.72 ? 586  PHE   A CD1 1 
ATOM   1186 C  CD2 . PHE   A 1 145 ? 19.893  -15.482 -22.684 1.00 14.54 ? 586  PHE   A CD2 1 
ATOM   1187 C  CE1 . PHE   A 1 145 ? 20.665  -16.576 -20.283 1.00 14.70 ? 586  PHE   A CE1 1 
ATOM   1188 C  CE2 . PHE   A 1 145 ? 19.688  -16.843 -22.421 1.00 15.56 ? 586  PHE   A CE2 1 
ATOM   1189 C  CZ  . PHE   A 1 145 ? 20.104  -17.384 -21.222 1.00 16.51 ? 586  PHE   A CZ  1 
ATOM   1190 N  N   . ASN   A 1 146 ? 21.155  -10.181 -20.955 1.00 12.19 ? 587  ASN   A N   1 
ATOM   1191 C  CA  . ASN   A 1 146 ? 21.241  -8.742  -21.155 1.00 10.65 ? 587  ASN   A CA  1 
ATOM   1192 C  C   . ASN   A 1 146 ? 21.875  -8.489  -22.521 1.00 10.03 ? 587  ASN   A C   1 
ATOM   1193 O  O   . ASN   A 1 146 ? 23.099  -8.377  -22.659 1.00 13.10 ? 587  ASN   A O   1 
ATOM   1194 C  CB  . ASN   A 1 146 ? 21.988  -8.055  -20.023 1.00 13.09 ? 587  ASN   A CB  1 
ATOM   1195 C  CG  . ASN   A 1 146 ? 21.806  -6.556  -20.077 1.00 11.37 ? 587  ASN   A CG  1 
ATOM   1196 O  OD1 . ASN   A 1 146 ? 21.821  -5.953  -21.180 1.00 11.50 ? 587  ASN   A OD1 1 
ATOM   1197 N  ND2 . ASN   A 1 146 ? 21.579  -5.942  -18.909 1.00 11.22 ? 587  ASN   A ND2 1 
ATOM   1198 N  N   . THR   A 1 147 ? 21.025  -8.434  -23.552 1.00 11.25 ? 588  THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 147 ? 21.472  -8.306  -24.936 1.00 12.98 ? 588  THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 147 ? 22.453  -7.150  -25.142 1.00 12.44 ? 588  THR   A C   1 
ATOM   1201 O  O   . THR   A 1 147 ? 23.517  -7.324  -25.755 1.00 12.62 ? 588  THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 147 ? 20.233  -8.151  -25.801 1.00 13.36 ? 588  THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 147 ? 19.453  -9.340  -25.629 1.00 13.65 ? 588  THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 147 ? 20.603  -7.907  -27.278 1.00 14.58 ? 588  THR   A CG2 1 
ATOM   1205 N  N   . ALA   A 1 148 ? 22.125  -5.960  -24.643 1.00 12.87 ? 589  ALA   A N   1 
ATOM   1206 C  CA  . ALA   A 1 148 ? 23.003  -4.815  -24.879 1.00 13.60 ? 589  ALA   A CA  1 
ATOM   1207 C  C   . ALA   A 1 148 ? 24.337  -4.977  -24.150 1.00 12.47 ? 589  ALA   A C   1 
ATOM   1208 O  O   . ALA   A 1 148 ? 25.386  -4.635  -24.701 1.00 13.36 ? 589  ALA   A O   1 
ATOM   1209 C  CB  . ALA   A 1 148 ? 22.319  -3.505  -24.477 1.00 14.34 ? 589  ALA   A CB  1 
ATOM   1210 N  N   . ALA   A 1 149 ? 24.312  -5.447  -22.895 1.00 12.27 ? 590  ALA   A N   1 
ATOM   1211 C  CA  . ALA   A 1 149 ? 25.557  -5.640  -22.158 1.00 13.78 ? 590  ALA   A CA  1 
ATOM   1212 C  C   . ALA   A 1 149 ? 26.421  -6.692  -22.828 1.00 14.45 ? 590  ALA   A C   1 
ATOM   1213 O  O   . ALA   A 1 149 ? 27.651  -6.530  -22.927 1.00 13.17 ? 590  ALA   A O   1 
ATOM   1214 C  CB  . ALA   A 1 149 ? 25.224  -6.075  -20.736 1.00 14.64 ? 590  ALA   A CB  1 
ATOM   1215 N  N   . LEU   A 1 150 ? 25.794  -7.780  -23.286 1.00 12.19 ? 591  LEU   A N   1 
ATOM   1216 C  CA  . LEU   A 1 150 ? 26.509  -8.816  -24.011 1.00 11.72 ? 591  LEU   A CA  1 
ATOM   1217 C  C   . LEU   A 1 150 ? 27.116  -8.257  -25.289 1.00 15.84 ? 591  LEU   A C   1 
ATOM   1218 O  O   . LEU   A 1 150 ? 28.242  -8.610  -25.663 1.00 15.20 ? 591  LEU   A O   1 
ATOM   1219 C  CB  . LEU   A 1 150 ? 25.572  -9.971  -24.344 1.00 12.45 ? 591  LEU   A CB  1 
ATOM   1220 C  CG  . LEU   A 1 150 ? 25.187  -10.855 -23.165 1.00 12.83 ? 591  LEU   A CG  1 
ATOM   1221 C  CD1 . LEU   A 1 150 ? 23.953  -11.674 -23.546 1.00 13.97 ? 591  LEU   A CD1 1 
ATOM   1222 C  CD2 . LEU   A 1 150 ? 26.377  -11.762 -22.769 1.00 15.55 ? 591  LEU   A CD2 1 
ATOM   1223 N  N   . THR   A 1 151 ? 26.381  -7.396  -25.982 1.00 11.74 ? 592  THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 151 ? 26.885  -6.833  -27.227 1.00 15.18 ? 592  THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 151 ? 28.088  -5.943  -26.973 1.00 13.69 ? 592  THR   A C   1 
ATOM   1226 O  O   . THR   A 1 151 ? 29.051  -5.960  -27.760 1.00 12.76 ? 592  THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 151 ? 25.757  -6.084  -27.945 1.00 13.51 ? 592  THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 151 ? 24.693  -6.992  -28.277 1.00 14.55 ? 592  THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 151 ? 26.272  -5.467  -29.245 1.00 14.34 ? 592  THR   A CG2 1 
ATOM   1230 N  N   . ALA   A 1 152 ? 28.085  -5.206  -25.867 1.00 12.73 ? 593  ALA   A N   1 
ATOM   1231 C  CA  . ALA   A 1 152 ? 29.251  -4.394  -25.526 1.00 14.19 ? 593  ALA   A CA  1 
ATOM   1232 C  C   . ALA   A 1 152 ? 30.471  -5.276  -25.292 1.00 17.14 ? 593  ALA   A C   1 
ATOM   1233 O  O   . ALA   A 1 152 ? 31.552  -5.017  -25.840 1.00 15.90 ? 593  ALA   A O   1 
ATOM   1234 C  CB  . ALA   A 1 152 ? 28.940  -3.518  -24.313 1.00 14.45 ? 593  ALA   A CB  1 
ATOM   1235 N  N   . ARG   A 1 153 ? 30.310  -6.358  -24.520 1.00 14.06 ? 594  ARG   A N   1 
ATOM   1236 C  CA  . ARG   A 1 153 ? 31.445  -7.263  -24.281 1.00 14.92 ? 594  ARG   A CA  1 
ATOM   1237 C  C   . ARG   A 1 153 ? 31.839  -8.003  -25.546 1.00 16.10 ? 594  ARG   A C   1 
ATOM   1238 O  O   . ARG   A 1 153 ? 33.039  -8.207  -25.808 1.00 17.32 ? 594  ARG   A O   1 
ATOM   1239 C  CB  . ARG   A 1 153 ? 31.103  -8.282  -23.193 1.00 17.86 ? 594  ARG   A CB  1 
ATOM   1240 C  CG  . ARG   A 1 153 ? 30.928  -7.714  -21.806 1.00 19.11 ? 594  ARG   A CG  1 
ATOM   1241 C  CD  . ARG   A 1 153 ? 32.197  -7.035  -21.339 1.00 21.77 ? 594  ARG   A CD  1 
ATOM   1242 N  NE  . ARG   A 1 153 ? 32.119  -6.767  -19.910 1.00 18.00 ? 594  ARG   A NE  1 
ATOM   1243 C  CZ  . ARG   A 1 153 ? 32.745  -5.770  -19.291 1.00 30.88 ? 594  ARG   A CZ  1 
ATOM   1244 N  NH1 . ARG   A 1 153 ? 33.510  -4.923  -19.984 1.00 18.37 ? 594  ARG   A NH1 1 
ATOM   1245 N  NH2 . ARG   A 1 153 ? 32.592  -5.618  -17.972 1.00 24.17 ? 594  ARG   A NH2 1 
ATOM   1246 N  N   . TYR   A 1 154 ? 30.860  -8.430  -26.340 1.00 15.23 ? 595  TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 154 ? 31.176  -9.037  -27.628 1.00 14.48 ? 595  TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 154 ? 32.023  -8.085  -28.485 1.00 18.09 ? 595  TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 154 ? 33.047  -8.481  -29.065 1.00 15.91 ? 595  TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 154 ? 29.879  -9.463  -28.351 1.00 13.76 ? 595  TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 154 ? 30.183  -9.894  -29.759 1.00 14.19 ? 595  TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 154 ? 30.681  -11.166 -30.015 1.00 16.60 ? 595  TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 154 ? 30.044  -9.018  -30.818 1.00 12.76 ? 595  TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 154 ? 31.022  -11.559 -31.301 1.00 15.92 ? 595  TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 154 ? 30.397  -9.394  -32.109 1.00 14.93 ? 595  TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 154 ? 30.862  -10.669 -32.341 1.00 17.13 ? 595  TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 154 ? 31.207  -11.039 -33.621 1.00 18.05 ? 595  TYR   A OH  1 
ATOM   1258 N  N   . ALA   A 1 155 ? 31.606  -6.821  -28.574 1.00 15.03 ? 596  ALA   A N   1 
ATOM   1259 C  CA  . ALA   A 1 155 ? 32.363  -5.811  -29.310 1.00 16.16 ? 596  ALA   A CA  1 
ATOM   1260 C  C   . ALA   A 1 155 ? 33.804  -5.742  -28.824 1.00 14.58 ? 596  ALA   A C   1 
ATOM   1261 O  O   . ALA   A 1 155 ? 34.737  -5.652  -29.635 1.00 15.86 ? 596  ALA   A O   1 
ATOM   1262 C  CB  . ALA   A 1 155 ? 31.712  -4.444  -29.131 1.00 16.77 ? 596  ALA   A CB  1 
ATOM   1263 N  N   . GLN   A 1 156 ? 34.000  -5.778  -27.514 1.00 15.32 ? 597  GLN   A N   1 
ATOM   1264 C  CA  . GLN   A 1 156 ? 35.344  -5.745  -26.960 1.00 19.64 ? 597  GLN   A CA  1 
ATOM   1265 C  C   . GLN   A 1 156 ? 36.120  -6.995  -27.343 1.00 21.95 ? 597  GLN   A C   1 
ATOM   1266 O  O   . GLN   A 1 156 ? 37.319  -6.918  -27.663 1.00 19.16 ? 597  GLN   A O   1 
ATOM   1267 C  CB  . GLN   A 1 156 ? 35.248  -5.548  -25.449 1.00 13.72 ? 597  GLN   A CB  1 
ATOM   1268 C  CG  . GLN   A 1 156 ? 34.908  -4.124  -25.113 1.00 15.51 ? 597  GLN   A CG  1 
ATOM   1269 C  CD  . GLN   A 1 156 ? 34.585  -3.869  -23.648 1.00 15.83 ? 597  GLN   A CD  1 
ATOM   1270 O  OE1 . GLN   A 1 156 ? 34.335  -4.797  -22.869 1.00 19.57 ? 597  GLN   A OE1 1 
ATOM   1271 N  NE2 . GLN   A 1 156 ? 34.610  -2.603  -23.254 1.00 16.16 ? 597  GLN   A NE2 1 
ATOM   1272 N  N   . SER   A 1 157 ? 35.441  -8.143  -27.378 1.00 17.28 ? 598  SER   A N   1 
ATOM   1273 C  CA  . SER   A 1 157 ? 36.096  -9.405  -27.675 1.00 18.58 ? 598  SER   A CA  1 
ATOM   1274 C  C   . SER   A 1 157 ? 36.621  -9.462  -29.103 1.00 21.44 ? 598  SER   A C   1 
ATOM   1275 O  O   . SER   A 1 157 ? 37.588  -10.180 -29.371 1.00 25.46 ? 598  SER   A O   1 
ATOM   1276 C  CB  . SER   A 1 157 ? 35.158  -10.576 -27.390 1.00 20.83 ? 598  SER   A CB  1 
ATOM   1277 O  OG  . SER   A 1 157 ? 34.252  -10.759 -28.457 1.00 20.19 ? 598  SER   A OG  1 
ATOM   1278 N  N   . ILE   A 1 158 ? 36.007  -8.737  -30.041 1.00 18.04 ? 599  ILE   A N   1 
ATOM   1279 C  CA  . ILE   A 1 158 ? 36.468  -8.760  -31.426 1.00 18.34 ? 599  ILE   A CA  1 
ATOM   1280 C  C   . ILE   A 1 158 ? 37.299  -7.537  -31.797 1.00 16.44 ? 599  ILE   A C   1 
ATOM   1281 O  O   . ILE   A 1 158 ? 37.679  -7.385  -32.973 1.00 19.01 ? 599  ILE   A O   1 
ATOM   1282 C  CB  . ILE   A 1 158 ? 35.326  -8.994  -32.440 1.00 19.84 ? 599  ILE   A CB  1 
ATOM   1283 C  CG1 . ILE   A 1 158 ? 34.287  -7.871  -32.367 1.00 15.24 ? 599  ILE   A CG1 1 
ATOM   1284 C  CG2 . ILE   A 1 158 ? 34.675  -10.355 -32.206 1.00 18.82 ? 599  ILE   A CG2 1 
ATOM   1285 C  CD1 . ILE   A 1 158 ? 33.353  -7.874  -33.546 1.00 19.43 ? 599  ILE   A CD1 1 
ATOM   1286 N  N   . THR   A 1 159 ? 37.576  -6.656  -30.840 1.00 17.89 ? 600  THR   A N   1 
ATOM   1287 C  CA  . THR   A 1 159 ? 38.458  -5.520  -31.074 1.00 16.74 ? 600  THR   A CA  1 
ATOM   1288 C  C   . THR   A 1 159 ? 39.567  -5.525  -30.033 1.00 24.42 ? 600  THR   A C   1 
ATOM   1289 O  O   . THR   A 1 159 ? 40.575  -6.227  -30.193 1.00 21.97 ? 600  THR   A O   1 
ATOM   1290 C  CB  . THR   A 1 159 ? 37.684  -4.187  -31.121 1.00 15.74 ? 600  THR   A CB  1 
ATOM   1291 O  OG1 . THR   A 1 159 ? 36.905  -4.007  -29.928 1.00 16.05 ? 600  THR   A OG1 1 
ATOM   1292 C  CG2 . THR   A 1 159 ? 36.752  -4.184  -32.324 1.00 17.50 ? 600  THR   A CG2 1 
ATOM   1293 N  N   . ARG   A 1 160 ? 39.387  -4.762  -28.964 1.00 18.57 ? 601  ARG   A N   1 
ATOM   1294 C  CA  . ARG   A 1 160 ? 40.277  -4.821  -27.819 1.00 18.63 ? 601  ARG   A CA  1 
ATOM   1295 C  C   . ARG   A 1 160 ? 39.451  -4.685  -26.552 1.00 19.77 ? 601  ARG   A C   1 
ATOM   1296 O  O   . ARG   A 1 160 ? 38.344  -4.133  -26.570 1.00 21.12 ? 601  ARG   A O   1 
ATOM   1297 C  CB  . ARG   A 1 160 ? 41.340  -3.721  -27.879 1.00 21.76 ? 601  ARG   A CB  1 
ATOM   1298 C  CG  . ARG   A 1 160 ? 40.775  -2.332  -27.815 1.00 22.56 ? 601  ARG   A CG  1 
ATOM   1299 C  CD  . ARG   A 1 160 ? 41.869  -1.297  -27.925 1.00 23.31 ? 601  ARG   A CD  1 
ATOM   1300 N  NE  . ARG   A 1 160 ? 41.499  -0.109  -27.189 1.00 31.89 ? 601  ARG   A NE  1 
ATOM   1301 C  CZ  . ARG   A 1 160 ? 40.708  0.839   -27.666 1.00 24.27 ? 601  ARG   A CZ  1 
ATOM   1302 N  NH1 . ARG   A 1 160 ? 40.225  0.732   -28.896 1.00 47.97 ? 601  ARG   A NH1 1 
ATOM   1303 N  NH2 . ARG   A 1 160 ? 40.408  1.894   -26.913 1.00 38.51 ? 601  ARG   A NH2 1 
ATOM   1304 N  N   . GLU   A 1 161 ? 40.002  -5.200  -25.446 1.00 21.04 ? 602  GLU   A N   1 
ATOM   1305 C  CA  . GLU   A 1 161 ? 39.260  -5.256  -24.183 1.00 23.41 ? 602  GLU   A CA  1 
ATOM   1306 C  C   . GLU   A 1 161 ? 38.776  -3.883  -23.732 1.00 24.86 ? 602  GLU   A C   1 
ATOM   1307 O  O   . GLU   A 1 161 ? 37.711  -3.771  -23.110 1.00 23.02 ? 602  GLU   A O   1 
ATOM   1308 C  CB  . GLU   A 1 161 ? 40.137  -5.867  -23.086 1.00 25.34 ? 602  GLU   A CB  1 
ATOM   1309 C  CG  . GLU   A 1 161 ? 40.446  -7.345  -23.276 1.00 44.51 ? 602  GLU   A CG  1 
ATOM   1310 C  CD  . GLU   A 1 161 ? 39.213  -8.229  -23.176 1.00 60.08 ? 602  GLU   A CD  1 
ATOM   1311 O  OE1 . GLU   A 1 161 ? 38.786  -8.529  -22.037 1.00 62.72 ? 602  GLU   A OE1 1 
ATOM   1312 O  OE2 . GLU   A 1 161 ? 38.677  -8.630  -24.235 1.00 57.51 ? 602  GLU   A OE2 1 
ATOM   1313 N  N   . SER   A 1 162 ? 39.534  -2.836  -24.019 1.00 21.62 ? 603  SER   A N   1 
ATOM   1314 C  CA  . SER   A 1 162 ? 39.253  -1.510  -23.503 1.00 22.29 ? 603  SER   A CA  1 
ATOM   1315 C  C   . SER   A 1 162 ? 38.474  -0.633  -24.478 1.00 16.11 ? 603  SER   A C   1 
ATOM   1316 O  O   . SER   A 1 162 ? 38.341  0.570   -24.231 1.00 20.38 ? 603  SER   A O   1 
ATOM   1317 C  CB  . SER   A 1 162 ? 40.549  -0.825  -23.071 1.00 30.82 ? 603  SER   A CB  1 
ATOM   1318 O  OG  . SER   A 1 162 ? 40.836  -1.152  -21.723 1.00 55.25 ? 603  SER   A OG  1 
ATOM   1319 N  N   . LEU   A 1 163 ? 37.973  -1.206  -25.567 1.00 19.12 ? 604  LEU   A N   1 
ATOM   1320 C  CA  . LEU   A 1 163 ? 37.147  -0.457  -26.511 1.00 18.36 ? 604  LEU   A CA  1 
ATOM   1321 C  C   . LEU   A 1 163 ? 36.075  0.310   -25.753 1.00 17.20 ? 604  LEU   A C   1 
ATOM   1322 O  O   . LEU   A 1 163 ? 35.374  -0.256  -24.912 1.00 16.91 ? 604  LEU   A O   1 
ATOM   1323 C  CB  . LEU   A 1 163 ? 36.487  -1.428  -27.482 1.00 21.13 ? 604  LEU   A CB  1 
ATOM   1324 C  CG  . LEU   A 1 163 ? 35.637  -0.747  -28.556 1.00 24.62 ? 604  LEU   A CG  1 
ATOM   1325 C  CD1 . LEU   A 1 163 ? 36.506  -0.334  -29.728 1.00 25.19 ? 604  LEU   A CD1 1 
ATOM   1326 C  CD2 . LEU   A 1 163 ? 34.497  -1.675  -29.008 1.00 22.03 ? 604  LEU   A CD2 1 
ATOM   1327 N  N   . ARG   A 1 164 ? 35.998  1.610   -25.991 1.00 16.62 ? 605  ARG   A N   1 
ATOM   1328 C  CA  . ARG   A 1 164 ? 35.075  2.447   -25.245 1.00 18.43 ? 605  ARG   A CA  1 
ATOM   1329 C  C   . ARG   A 1 164 ? 33.676  2.330   -25.839 1.00 19.65 ? 605  ARG   A C   1 
ATOM   1330 O  O   . ARG   A 1 164 ? 33.440  2.725   -26.989 1.00 18.60 ? 605  ARG   A O   1 
ATOM   1331 C  CB  . ARG   A 1 164 ? 35.548  3.896   -25.227 1.00 18.75 ? 605  ARG   A CB  1 
ATOM   1332 C  CG  . ARG   A 1 164 ? 36.825  4.096   -24.397 1.00 19.21 ? 605  ARG   A CG  1 
ATOM   1333 C  CD  . ARG   A 1 164 ? 37.128  5.574   -24.179 1.00 22.99 ? 605  ARG   A CD  1 
ATOM   1334 N  NE  . ARG   A 1 164 ? 37.254  6.312   -25.438 1.00 24.88 ? 605  ARG   A NE  1 
ATOM   1335 C  CZ  . ARG   A 1 164 ? 38.295  6.225   -26.266 1.00 33.55 ? 605  ARG   A CZ  1 
ATOM   1336 N  NH1 . ARG   A 1 164 ? 39.327  5.435   -25.982 1.00 30.79 ? 605  ARG   A NH1 1 
ATOM   1337 N  NH2 . ARG   A 1 164 ? 38.306  6.942   -27.382 1.00 28.25 ? 605  ARG   A NH2 1 
ATOM   1338 N  N   . VAL   A 1 165 ? 32.751  1.788   -25.054 1.00 16.28 ? 606  VAL   A N   1 
ATOM   1339 C  CA  . VAL   A 1 165 ? 31.369  1.589   -25.483 1.00 14.03 ? 606  VAL   A CA  1 
ATOM   1340 C  C   . VAL   A 1 165 ? 30.469  2.468   -24.633 1.00 15.60 ? 606  VAL   A C   1 
ATOM   1341 O  O   . VAL   A 1 165 ? 30.515  2.401   -23.397 1.00 16.66 ? 606  VAL   A O   1 
ATOM   1342 C  CB  . VAL   A 1 165 ? 30.964  0.112   -25.381 1.00 15.24 ? 606  VAL   A CB  1 
ATOM   1343 C  CG1 . VAL   A 1 165 ? 29.515  -0.072  -25.898 1.00 15.92 ? 606  VAL   A CG1 1 
ATOM   1344 C  CG2 . VAL   A 1 165 ? 31.912  -0.747  -26.180 1.00 17.89 ? 606  VAL   A CG2 1 
ATOM   1345 N  N   . LEU   A 1 166 ? 29.647  3.291   -25.291 1.00 15.13 ? 607  LEU   A N   1 
ATOM   1346 C  CA  . LEU   A 1 166 ? 28.589  4.045   -24.632 1.00 15.83 ? 607  LEU   A CA  1 
ATOM   1347 C  C   . LEU   A 1 166 ? 27.271  3.306   -24.822 1.00 14.63 ? 607  LEU   A C   1 
ATOM   1348 O  O   . LEU   A 1 166 ? 26.915  2.955   -25.952 1.00 15.55 ? 607  LEU   A O   1 
ATOM   1349 C  CB  . LEU   A 1 166 ? 28.457  5.462   -25.208 1.00 16.89 ? 607  LEU   A CB  1 
ATOM   1350 C  CG  . LEU   A 1 166 ? 27.193  6.254   -24.864 1.00 16.73 ? 607  LEU   A CG  1 
ATOM   1351 C  CD1 . LEU   A 1 166 ? 27.094  6.505   -23.360 1.00 19.21 ? 607  LEU   A CD1 1 
ATOM   1352 C  CD2 . LEU   A 1 166 ? 27.040  7.567   -25.637 1.00 16.99 ? 607  LEU   A CD2 1 
ATOM   1353 N  N   . ILE   A 1 167 ? 26.567  3.038   -23.719 1.00 12.61 ? 608  ILE   A N   1 
ATOM   1354 C  CA  . ILE   A 1 167 ? 25.198  2.527   -23.780 1.00 14.14 ? 608  ILE   A CA  1 
ATOM   1355 C  C   . ILE   A 1 167 ? 24.284  3.644   -23.312 1.00 13.54 ? 608  ILE   A C   1 
ATOM   1356 O  O   . ILE   A 1 167 ? 24.361  4.070   -22.161 1.00 13.94 ? 608  ILE   A O   1 
ATOM   1357 C  CB  . ILE   A 1 167 ? 24.980  1.271   -22.917 1.00 13.16 ? 608  ILE   A CB  1 
ATOM   1358 C  CG1 . ILE   A 1 167 ? 25.871  0.113   -23.375 1.00 14.34 ? 608  ILE   A CG1 1 
ATOM   1359 C  CG2 . ILE   A 1 167 ? 23.467  0.871   -22.925 1.00 15.77 ? 608  ILE   A CG2 1 
ATOM   1360 C  CD1 . ILE   A 1 167 ? 25.827  -1.098  -22.431 1.00 15.59 ? 608  ILE   A CD1 1 
ATOM   1361 N  N   . VAL   A 1 168 ? 23.428  4.136   -24.208 1.00 14.17 ? 609  VAL   A N   1 
ATOM   1362 C  CA  . VAL   A 1 168 ? 22.369  5.076   -23.842 1.00 13.38 ? 609  VAL   A CA  1 
ATOM   1363 C  C   . VAL   A 1 168 ? 21.074  4.294   -23.781 1.00 13.04 ? 609  VAL   A C   1 
ATOM   1364 O  O   . VAL   A 1 168 ? 20.685  3.683   -24.776 1.00 13.31 ? 609  VAL   A O   1 
ATOM   1365 C  CB  . VAL   A 1 168 ? 22.263  6.219   -24.861 1.00 14.09 ? 609  VAL   A CB  1 
ATOM   1366 C  CG1 . VAL   A 1 168 ? 21.090  7.136   -24.525 1.00 15.77 ? 609  VAL   A CG1 1 
ATOM   1367 C  CG2 . VAL   A 1 168 ? 23.558  6.998   -24.910 1.00 17.74 ? 609  VAL   A CG2 1 
ATOM   1368 N  N   . ASP   A 1 169 ? 20.419  4.304   -22.620 1.00 13.02 ? 610  ASP   A N   1 
ATOM   1369 C  CA  . ASP   A 1 169 ? 19.223  3.503   -22.365 1.00 14.79 ? 610  ASP   A CA  1 
ATOM   1370 C  C   . ASP   A 1 169 ? 18.050  4.473   -22.215 1.00 11.65 ? 610  ASP   A C   1 
ATOM   1371 O  O   . ASP   A 1 169 ? 17.874  5.095   -21.161 1.00 12.84 ? 610  ASP   A O   1 
ATOM   1372 C  CB  . ASP   A 1 169 ? 19.474  2.653   -21.110 1.00 12.91 ? 610  ASP   A CB  1 
ATOM   1373 C  CG  . ASP   A 1 169 ? 18.346  1.688   -20.797 1.00 13.88 ? 610  ASP   A CG  1 
ATOM   1374 O  OD1 . ASP   A 1 169 ? 17.182  1.958   -21.162 1.00 13.45 ? 610  ASP   A OD1 1 
ATOM   1375 O  OD2 . ASP   A 1 169 ? 18.653  0.667   -20.091 1.00 12.96 ? 610  ASP   A OD2 1 
ATOM   1376 N  N   . TRP   A 1 170 ? 17.253  4.623   -23.275 1.00 12.27 ? 611  TRP   A N   1 
ATOM   1377 C  CA  . TRP   A 1 170 ? 16.118  5.539   -23.221 1.00 13.59 ? 611  TRP   A CA  1 
ATOM   1378 C  C   . TRP   A 1 170 ? 14.787  4.830   -23.036 1.00 14.27 ? 611  TRP   A C   1 
ATOM   1379 O  O   . TRP   A 1 170 ? 13.747  5.481   -23.091 1.00 12.21 ? 611  TRP   A O   1 
ATOM   1380 C  CB  . TRP   A 1 170 ? 16.108  6.540   -24.384 1.00 14.48 ? 611  TRP   A CB  1 
ATOM   1381 C  CG  . TRP   A 1 170 ? 15.783  5.981   -25.768 1.00 12.89 ? 611  TRP   A CG  1 
ATOM   1382 C  CD1 . TRP   A 1 170 ? 14.837  5.054   -26.086 1.00 14.81 ? 611  TRP   A CD1 1 
ATOM   1383 C  CD2 . TRP   A 1 170 ? 16.407  6.358   -27.008 1.00 12.49 ? 611  TRP   A CD2 1 
ATOM   1384 N  NE1 . TRP   A 1 170 ? 14.823  4.828   -27.455 1.00 13.56 ? 611  TRP   A NE1 1 
ATOM   1385 C  CE2 . TRP   A 1 170 ? 15.764  5.631   -28.046 1.00 13.84 ? 611  TRP   A CE2 1 
ATOM   1386 C  CE3 . TRP   A 1 170 ? 17.432  7.253   -27.347 1.00 15.01 ? 611  TRP   A CE3 1 
ATOM   1387 C  CZ2 . TRP   A 1 170 ? 16.132  5.753   -29.396 1.00 14.94 ? 611  TRP   A CZ2 1 
ATOM   1388 C  CZ3 . TRP   A 1 170 ? 17.788  7.384   -28.690 1.00 17.07 ? 611  TRP   A CZ3 1 
ATOM   1389 C  CH2 . TRP   A 1 170 ? 17.140  6.628   -29.698 1.00 16.10 ? 611  TRP   A CH2 1 
ATOM   1390 N  N   . ASP   A 1 171 ? 14.804  3.522   -22.783 1.00 12.68 ? 612  ASP   A N   1 
ATOM   1391 C  CA  . ASP   A 1 171 ? 13.618  2.840   -22.283 1.00 13.48 ? 612  ASP   A CA  1 
ATOM   1392 C  C   . ASP   A 1 171 ? 13.137  3.602   -21.053 1.00 12.88 ? 612  ASP   A C   1 
ATOM   1393 O  O   . ASP   A 1 171 ? 13.945  4.195   -20.326 1.00 13.04 ? 612  ASP   A O   1 
ATOM   1394 C  CB  . ASP   A 1 171 ? 14.021  1.388   -21.952 1.00 13.73 ? 612  ASP   A CB  1 
ATOM   1395 C  CG  . ASP   A 1 171 ? 12.854  0.505   -21.538 1.00 13.02 ? 612  ASP   A CG  1 
ATOM   1396 O  OD1 . ASP   A 1 171 ? 12.350  0.677   -20.443 1.00 12.10 ? 612  ASP   A OD1 1 
ATOM   1397 O  OD2 . ASP   A 1 171 ? 12.411  -0.403  -22.272 1.00 14.14 ? 612  ASP   A OD2 1 
ATOM   1398 N  N   . VAL   A 1 172 ? 11.833  3.628   -20.832 1.00 11.86 ? 613  VAL   A N   1 
ATOM   1399 C  CA  . VAL   A 1 172 ? 11.279  4.424   -19.704 1.00 11.31 ? 613  VAL   A CA  1 
ATOM   1400 C  C   . VAL   A 1 172 ? 11.723  3.810   -18.360 1.00 13.48 ? 613  VAL   A C   1 
ATOM   1401 O  O   . VAL   A 1 172 ? 11.649  4.504   -17.345 1.00 14.15 ? 613  VAL   A O   1 
ATOM   1402 C  CB  . VAL   A 1 172 ? 9.744   4.499   -19.795 1.00 14.28 ? 613  VAL   A CB  1 
ATOM   1403 C  CG1 . VAL   A 1 172 ? 9.055   3.238   -19.289 1.00 13.70 ? 613  VAL   A CG1 1 
ATOM   1404 C  CG2 . VAL   A 1 172 ? 9.202   5.725   -19.066 1.00 17.15 ? 613  VAL   A CG2 1 
ATOM   1405 N  N   . HIS   A 1 173 ? 12.148  2.555   -18.382 1.00 13.66 ? 614  HIS   A N   1 
ATOM   1406 C  CA  . HIS   A 1 173 ? 12.584  1.849   -17.149 1.00 18.16 ? 614  HIS   A CA  1 
ATOM   1407 C  C   . HIS   A 1 173 ? 14.102  1.892   -17.000 1.00 13.02 ? 614  HIS   A C   1 
ATOM   1408 O  O   . HIS   A 1 173 ? 14.832  1.906   -17.966 1.00 14.00 ? 614  HIS   A O   1 
ATOM   1409 C  CB  . HIS   A 1 173 ? 12.110  0.389   -17.147 1.00 54.46 ? 614  HIS   A CB  1 
ATOM   1410 C  CG  . HIS   A 1 173 ? 10.637  0.269   -17.291 1.00 24.67 ? 614  HIS   A CG  1 
ATOM   1411 N  ND1 . HIS   A 1 173 ? 9.973   -0.077  -18.449 1.00 28.52 ? 614  HIS   A ND1 1 
ATOM   1412 C  CD2 . HIS   A 1 173 ? 9.695   0.470   -16.368 1.00 30.67 ? 614  HIS   A CD2 1 
ATOM   1413 C  CE1 . HIS   A 1 173 ? 8.672   -0.085  -18.207 1.00 17.92 ? 614  HIS   A CE1 1 
ATOM   1414 N  NE2 . HIS   A 1 173 ? 8.483   0.247   -16.955 1.00 18.24 ? 614  HIS   A NE2 1 
ATOM   1415 N  N   . HIS   A 1 174 ? 14.533  1.900   -15.746 1.00 12.58 ? 615  HIS   A N   1 
ATOM   1416 C  CA  . HIS   A 1 174 ? 15.977  1.827   -15.463 1.00 15.52 ? 615  HIS   A CA  1 
ATOM   1417 C  C   . HIS   A 1 174 ? 16.489  0.434   -15.846 1.00 12.50 ? 615  HIS   A C   1 
ATOM   1418 O  O   . HIS   A 1 174 ? 15.860  -0.569  -15.515 1.00 12.61 ? 615  HIS   A O   1 
ATOM   1419 C  CB  . HIS   A 1 174 ? 16.214  2.059   -13.973 1.00 14.36 ? 615  HIS   A CB  1 
ATOM   1420 C  CG  . HIS   A 1 174 ? 17.664  2.059   -13.621 1.00 12.47 ? 615  HIS   A CG  1 
ATOM   1421 N  ND1 . HIS   A 1 174 ? 18.210  1.199   -12.695 1.00 16.45 ? 615  HIS   A ND1 1 
ATOM   1422 C  CD2 . HIS   A 1 174 ? 18.671  2.815   -14.063 1.00 15.68 ? 615  HIS   A CD2 1 
ATOM   1423 C  CE1 . HIS   A 1 174 ? 19.503  1.434   -12.596 1.00 14.22 ? 615  HIS   A CE1 1 
ATOM   1424 N  NE2 . HIS   A 1 174 ? 19.806  2.416   -13.413 1.00 17.03 ? 615  HIS   A NE2 1 
ATOM   1425 N  N   . GLY   A 1 175 ? 17.578  0.419   -16.600 1.00 12.57 ? 616  GLY   A N   1 
ATOM   1426 C  CA  . GLY   A 1 175 ? 18.224  -0.835  -16.958 1.00 12.67 ? 616  GLY   A CA  1 
ATOM   1427 C  C   . GLY   A 1 175 ? 19.072  -1.336  -15.791 1.00 13.69 ? 616  GLY   A C   1 
ATOM   1428 O  O   . GLY   A 1 175 ? 20.303  -1.225  -15.827 1.00 14.40 ? 616  GLY   A O   1 
ATOM   1429 N  N   . ASN   A 1 176 ? 18.426  -1.877  -14.743 1.00 12.31 ? 617  ASN   A N   1 
ATOM   1430 C  CA  . ASN   A 1 176 ? 19.163  -2.305  -13.544 1.00 13.51 ? 617  ASN   A CA  1 
ATOM   1431 C  C   . ASN   A 1 176 ? 20.259  -3.314  -13.888 1.00 13.51 ? 617  ASN   A C   1 
ATOM   1432 O  O   . ASN   A 1 176 ? 21.356  -3.269  -13.316 1.00 13.95 ? 617  ASN   A O   1 
ATOM   1433 C  CB  . ASN   A 1 176 ? 18.217  -2.927  -12.508 1.00 16.03 ? 617  ASN   A CB  1 
ATOM   1434 C  CG  . ASN   A 1 176 ? 17.366  -4.046  -13.103 1.00 16.49 ? 617  ASN   A CG  1 
ATOM   1435 O  OD1 . ASN   A 1 176 ? 16.479  -3.775  -13.872 1.00 14.50 ? 617  ASN   A OD1 1 
ATOM   1436 N  ND2 . ASN   A 1 176 ? 17.675  -5.297  -12.796 1.00 17.19 ? 617  ASN   A ND2 1 
ATOM   1437 N  N   . GLY   A 1 177 ? 19.984  -4.223  -14.830 1.00 12.62 ? 618  GLY   A N   1 
ATOM   1438 C  CA  . GLY   A 1 177 ? 20.960  -5.235  -15.189 1.00 14.43 ? 618  GLY   A CA  1 
ATOM   1439 C  C   . GLY   A 1 177 ? 22.193  -4.631  -15.832 1.00 15.36 ? 618  GLY   A C   1 
ATOM   1440 O  O   . GLY   A 1 177 ? 23.335  -4.978  -15.478 1.00 13.41 ? 618  GLY   A O   1 
ATOM   1441 N  N   . THR   A 1 178 ? 21.990  -3.697  -16.769 1.00 12.13 ? 619  THR   A N   1 
ATOM   1442 C  CA  . THR   A 1 178 ? 23.117  -3.075  -17.429 1.00 14.30 ? 619  THR   A CA  1 
ATOM   1443 C  C   . THR   A 1 178 ? 23.942  -2.265  -16.451 1.00 13.69 ? 619  THR   A C   1 
ATOM   1444 O  O   . THR   A 1 178 ? 25.176  -2.354  -16.462 1.00 12.59 ? 619  THR   A O   1 
ATOM   1445 C  CB  . THR   A 1 178 ? 22.607  -2.201  -18.565 1.00 14.14 ? 619  THR   A CB  1 
ATOM   1446 O  OG1 . THR   A 1 178 ? 21.669  -2.987  -19.305 1.00 12.42 ? 619  THR   A OG1 1 
ATOM   1447 C  CG2 . THR   A 1 178 ? 23.747  -1.780  -19.465 1.00 14.03 ? 619  THR   A CG2 1 
ATOM   1448 N  N   . GLN   A 1 179 ? 23.289  -1.491  -15.582 1.00 14.05 ? 620  GLN   A N   1 
ATOM   1449 C  CA  . GLN   A 1 179 ? 24.036  -0.747  -14.571 1.00 16.33 ? 620  GLN   A CA  1 
ATOM   1450 C  C   . GLN   A 1 179 ? 24.896  -1.690  -13.741 1.00 15.24 ? 620  GLN   A C   1 
ATOM   1451 O  O   . GLN   A 1 179 ? 26.098  -1.452  -13.551 1.00 16.27 ? 620  GLN   A O   1 
ATOM   1452 C  CB  . GLN   A 1 179 ? 23.085  0.043   -13.674 1.00 15.42 ? 620  GLN   A CB  1 
ATOM   1453 C  CG  . GLN   A 1 179 ? 23.790  0.570   -12.418 1.00 14.99 ? 620  GLN   A CG  1 
ATOM   1454 C  CD  . GLN   A 1 179 ? 22.964  1.567   -11.653 1.00 18.87 ? 620  GLN   A CD  1 
ATOM   1455 O  OE1 . GLN   A 1 179 ? 22.331  2.443   -12.242 1.00 16.30 ? 620  GLN   A OE1 1 
ATOM   1456 N  NE2 . GLN   A 1 179 ? 22.956  1.446   -10.323 1.00 19.81 ? 620  GLN   A NE2 1 
ATOM   1457 N  N   . HIS   A 1 180 ? 24.300  -2.774  -13.245 1.00 13.47 ? 621  HIS   A N   1 
ATOM   1458 C  CA  . HIS   A 1 180 ? 25.031  -3.657  -12.335 1.00 13.90 ? 621  HIS   A CA  1 
ATOM   1459 C  C   . HIS   A 1 180 ? 26.176  -4.361  -13.045 1.00 16.83 ? 621  HIS   A C   1 
ATOM   1460 O  O   . HIS   A 1 180 ? 27.281  -4.458  -12.497 1.00 15.51 ? 621  HIS   A O   1 
ATOM   1461 C  CB  . HIS   A 1 180 ? 24.078  -4.638  -11.650 1.00 15.75 ? 621  HIS   A CB  1 
ATOM   1462 C  CG  . HIS   A 1 180 ? 23.132  -3.975  -10.695 1.00 15.02 ? 621  HIS   A CG  1 
ATOM   1463 N  ND1 . HIS   A 1 180 ? 21.846  -4.424  -10.485 1.00 17.31 ? 621  HIS   A ND1 1 
ATOM   1464 C  CD2 . HIS   A 1 180 ? 23.281  -2.884  -9.902  1.00 19.61 ? 621  HIS   A CD2 1 
ATOM   1465 C  CE1 . HIS   A 1 180 ? 21.247  -3.645  -9.602  1.00 24.22 ? 621  HIS   A CE1 1 
ATOM   1466 N  NE2 . HIS   A 1 180 ? 22.091  -2.694  -9.244  1.00 21.54 ? 621  HIS   A NE2 1 
ATOM   1467 N  N   . ILE   A 1 181 ? 25.954  -4.805  -14.275 1.00 13.56 ? 622  ILE   A N   1 
ATOM   1468 C  CA  . ILE   A 1 181 ? 26.990  -5.505  -15.027 1.00 13.94 ? 622  ILE   A CA  1 
ATOM   1469 C  C   . ILE   A 1 181 ? 28.230  -4.629  -15.208 1.00 17.39 ? 622  ILE   A C   1 
ATOM   1470 O  O   . ILE   A 1 181 ? 29.367  -5.108  -15.104 1.00 16.71 ? 622  ILE   A O   1 
ATOM   1471 C  CB  . ILE   A 1 181 ? 26.428  -6.036  -16.365 1.00 13.90 ? 622  ILE   A CB  1 
ATOM   1472 C  CG1 . ILE   A 1 181 ? 25.490  -7.227  -16.108 1.00 14.40 ? 622  ILE   A CG1 1 
ATOM   1473 C  CG2 . ILE   A 1 181 ? 27.581  -6.426  -17.308 1.00 15.00 ? 622  ILE   A CG2 1 
ATOM   1474 C  CD1 . ILE   A 1 181 ? 24.654  -7.606  -17.305 1.00 14.38 ? 622  ILE   A CD1 1 
ATOM   1475 N  N   . PHE   A 1 182 ? 28.040  -3.331  -15.456 1.00 13.91 ? 623  PHE   A N   1 
ATOM   1476 C  CA  . PHE   A 1 182 ? 29.149  -2.428  -15.727 1.00 13.75 ? 623  PHE   A CA  1 
ATOM   1477 C  C   . PHE   A 1 182 ? 29.439  -1.475  -14.579 1.00 13.15 ? 623  PHE   A C   1 
ATOM   1478 O  O   . PHE   A 1 182 ? 30.204  -0.524  -14.771 1.00 16.15 ? 623  PHE   A O   1 
ATOM   1479 C  CB  . PHE   A 1 182 ? 28.891  -1.656  -17.025 1.00 15.50 ? 623  PHE   A CB  1 
ATOM   1480 C  CG  . PHE   A 1 182 ? 28.696  -2.544  -18.212 1.00 14.78 ? 623  PHE   A CG  1 
ATOM   1481 C  CD1 . PHE   A 1 182 ? 29.738  -3.323  -18.688 1.00 13.45 ? 623  PHE   A CD1 1 
ATOM   1482 C  CD2 . PHE   A 1 182 ? 27.459  -2.619  -18.836 1.00 14.32 ? 623  PHE   A CD2 1 
ATOM   1483 C  CE1 . PHE   A 1 182 ? 29.579  -4.162  -19.790 1.00 13.27 ? 623  PHE   A CE1 1 
ATOM   1484 C  CE2 . PHE   A 1 182 ? 27.273  -3.444  -19.919 1.00 15.00 ? 623  PHE   A CE2 1 
ATOM   1485 C  CZ  . PHE   A 1 182 ? 28.317  -4.223  -20.415 1.00 14.40 ? 623  PHE   A CZ  1 
ATOM   1486 N  N   . GLU   A 1 183 ? 28.881  -1.717  -13.392 1.00 13.22 ? 624  GLU   A N   1 
ATOM   1487 C  CA  . GLU   A 1 183 ? 28.989  -0.728  -12.323 1.00 15.73 ? 624  GLU   A CA  1 
ATOM   1488 C  C   . GLU   A 1 183 ? 30.441  -0.431  -11.949 1.00 18.98 ? 624  GLU   A C   1 
ATOM   1489 O  O   . GLU   A 1 183 ? 30.749  0.698   -11.544 1.00 16.89 ? 624  GLU   A O   1 
ATOM   1490 C  CB  . GLU   A 1 183 ? 28.219  -1.185  -11.084 1.00 16.17 ? 624  GLU   A CB  1 
ATOM   1491 C  CG  . GLU   A 1 183 ? 27.760  -0.053  -10.190 1.00 23.66 ? 624  GLU   A CG  1 
ATOM   1492 C  CD  . GLU   A 1 183 ? 26.706  -0.489  -9.178  1.00 28.05 ? 624  GLU   A CD  1 
ATOM   1493 O  OE1 . GLU   A 1 183 ? 26.558  -1.717  -8.964  1.00 24.65 ? 624  GLU   A OE1 1 
ATOM   1494 O  OE2 . GLU   A 1 183 ? 26.033  0.396   -8.590  1.00 32.50 ? 624  GLU   A OE2 1 
ATOM   1495 N  N   . GLU   A 1 184 ? 31.340  -1.410  -12.091 1.00 16.56 ? 625  GLU   A N   1 
ATOM   1496 C  CA  . GLU   A 1 184 ? 32.748  -1.255  -11.734 1.00 18.43 ? 625  GLU   A CA  1 
ATOM   1497 C  C   . GLU   A 1 184 ? 33.621  -1.154  -12.977 1.00 21.27 ? 625  GLU   A C   1 
ATOM   1498 O  O   . GLU   A 1 184 ? 34.809  -1.509  -12.950 1.00 22.12 ? 625  GLU   A O   1 
ATOM   1499 C  CB  . GLU   A 1 184 ? 33.223  -2.401  -10.838 1.00 17.42 ? 625  GLU   A CB  1 
ATOM   1500 C  CG  . GLU   A 1 184 ? 32.598  -2.423  -9.469  1.00 25.73 ? 625  GLU   A CG  1 
ATOM   1501 C  CD  . GLU   A 1 184 ? 32.966  -3.674  -8.690  1.00 36.21 ? 625  GLU   A CD  1 
ATOM   1502 O  OE1 . GLU   A 1 184 ? 32.875  -4.784  -9.254  1.00 57.06 ? 625  GLU   A OE1 1 
ATOM   1503 O  OE2 . GLU   A 1 184 ? 33.358  -3.545  -7.518  1.00 41.43 ? 625  GLU   A OE2 1 
ATOM   1504 N  N   . ASP   A 1 185 ? 33.042  -0.678  -14.081 1.00 18.52 ? 626  ASP   A N   1 
ATOM   1505 C  CA  . ASP   A 1 185 ? 33.713  -0.701  -15.370 1.00 18.98 ? 626  ASP   A CA  1 
ATOM   1506 C  C   . ASP   A 1 185 ? 33.754  0.697   -15.960 1.00 22.71 ? 626  ASP   A C   1 
ATOM   1507 O  O   . ASP   A 1 185 ? 32.707  1.339   -16.138 1.00 21.58 ? 626  ASP   A O   1 
ATOM   1508 C  CB  . ASP   A 1 185 ? 33.027  -1.665  -16.341 1.00 25.89 ? 626  ASP   A CB  1 
ATOM   1509 C  CG  . ASP   A 1 185 ? 33.941  -2.095  -17.465 1.00 25.86 ? 626  ASP   A CG  1 
ATOM   1510 O  OD1 . ASP   A 1 185 ? 34.950  -1.394  -17.728 0.69 26.14 ? 626  ASP   A OD1 1 
ATOM   1511 O  OD2 . ASP   A 1 185 ? 33.656  -3.134  -18.081 0.78 28.58 ? 626  ASP   A OD2 1 
ATOM   1512 N  N   . ASP   A 1 186 ? 34.969  1.151   -16.283 1.00 22.01 ? 627  ASP   A N   1 
ATOM   1513 C  CA  . ASP   A 1 186 ? 35.177  2.427   -16.941 1.00 21.32 ? 627  ASP   A CA  1 
ATOM   1514 C  C   . ASP   A 1 186 ? 35.255  2.306   -18.458 1.00 20.35 ? 627  ASP   A C   1 
ATOM   1515 O  O   . ASP   A 1 186 ? 35.335  3.341   -19.138 1.00 25.30 ? 627  ASP   A O   1 
ATOM   1516 C  CB  . ASP   A 1 186 ? 36.454  3.091   -16.402 1.00 25.83 ? 627  ASP   A CB  1 
ATOM   1517 C  CG  . ASP   A 1 186 ? 37.700  2.263   -16.663 1.00 24.18 ? 627  ASP   A CG  1 
ATOM   1518 O  OD1 . ASP   A 1 186 ? 37.600  1.035   -16.890 1.00 37.19 ? 627  ASP   A OD1 1 
ATOM   1519 O  OD2 . ASP   A 1 186 ? 38.805  2.845   -16.644 1.00 55.93 ? 627  ASP   A OD2 1 
ATOM   1520 N  N   . SER   A 1 187 ? 35.252  1.085   -19.010 1.00 16.54 ? 628  SER   A N   1 
ATOM   1521 C  CA  . SER   A 1 187 ? 35.285  0.937   -20.463 1.00 16.67 ? 628  SER   A CA  1 
ATOM   1522 C  C   . SER   A 1 187 ? 33.903  1.009   -21.105 1.00 16.48 ? 628  SER   A C   1 
ATOM   1523 O  O   . SER   A 1 187 ? 33.822  1.187   -22.314 1.00 17.11 ? 628  SER   A O   1 
ATOM   1524 C  CB  . SER   A 1 187 ? 35.955  -0.380  -20.872 1.00 19.59 ? 628  SER   A CB  1 
ATOM   1525 O  OG  . SER   A 1 187 ? 35.130  -1.501  -20.575 1.00 20.60 ? 628  SER   A OG  1 
ATOM   1526 N  N   . VAL   A 1 188 ? 32.838  0.831   -20.324 1.00 17.30 ? 629  VAL   A N   1 
ATOM   1527 C  CA  . VAL   A 1 188 ? 31.466  0.963   -20.787 1.00 15.85 ? 629  VAL   A CA  1 
ATOM   1528 C  C   . VAL   A 1 188 ? 30.859  2.068   -19.945 1.00 18.29 ? 629  VAL   A C   1 
ATOM   1529 O  O   . VAL   A 1 188 ? 30.936  2.015   -18.717 1.00 37.76 ? 629  VAL   A O   1 
ATOM   1530 C  CB  . VAL   A 1 188 ? 30.706  -0.368  -20.630 1.00 15.36 ? 629  VAL   A CB  1 
ATOM   1531 C  CG1 . VAL   A 1 188 ? 29.286  -0.252  -21.211 1.00 17.98 ? 629  VAL   A CG1 1 
ATOM   1532 C  CG2 . VAL   A 1 188 ? 31.466  -1.485  -21.317 1.00 16.25 ? 629  VAL   A CG2 1 
ATOM   1533 N  N   . LEU   A 1 189 ? 30.417  3.136   -20.593 1.00 14.38 ? 630  LEU   A N   1 
ATOM   1534 C  CA  . LEU   A 1 189 ? 29.709  4.231   -19.952 1.00 16.26 ? 630  LEU   A CA  1 
ATOM   1535 C  C   . LEU   A 1 189 ? 28.224  3.935   -20.117 1.00 16.42 ? 630  LEU   A C   1 
ATOM   1536 O  O   . LEU   A 1 189 ? 27.755  3.732   -21.248 1.00 15.88 ? 630  LEU   A O   1 
ATOM   1537 C  CB  . LEU   A 1 189 ? 30.068  5.562   -20.610 1.00 19.09 ? 630  LEU   A CB  1 
ATOM   1538 C  CG  . LEU   A 1 189 ? 29.260  6.793   -20.260 1.00 16.98 ? 630  LEU   A CG  1 
ATOM   1539 C  CD1 . LEU   A 1 189 ? 29.340  7.055   -18.756 1.00 19.21 ? 630  LEU   A CD1 1 
ATOM   1540 C  CD2 . LEU   A 1 189 ? 29.762  7.982   -21.059 1.00 20.64 ? 630  LEU   A CD2 1 
ATOM   1541 N  N   . TYR   A 1 190 ? 27.497  3.876   -19.001 1.00 13.89 ? 631  TYR   A N   1 
ATOM   1542 C  CA  . TYR   A 1 190 ? 26.068  3.593   -19.016 1.00 13.79 ? 631  TYR   A CA  1 
ATOM   1543 C  C   . TYR   A 1 190 ? 25.326  4.879   -18.665 1.00 16.12 ? 631  TYR   A C   1 
ATOM   1544 O  O   . TYR   A 1 190 ? 25.544  5.450   -17.590 1.00 15.14 ? 631  TYR   A O   1 
ATOM   1545 C  CB  . TYR   A 1 190 ? 25.717  2.474   -18.025 1.00 13.56 ? 631  TYR   A CB  1 
ATOM   1546 C  CG  . TYR   A 1 190 ? 24.239  2.168   -17.979 1.00 13.18 ? 631  TYR   A CG  1 
ATOM   1547 C  CD1 . TYR   A 1 190 ? 23.576  1.666   -19.100 1.00 14.75 ? 631  TYR   A CD1 1 
ATOM   1548 C  CD2 . TYR   A 1 190 ? 23.510  2.409   -16.850 1.00 13.31 ? 631  TYR   A CD2 1 
ATOM   1549 C  CE1 . TYR   A 1 190 ? 22.209  1.411   -19.090 1.00 13.98 ? 631  TYR   A CE1 1 
ATOM   1550 C  CE2 . TYR   A 1 190 ? 22.129  2.161   -16.816 1.00 14.90 ? 631  TYR   A CE2 1 
ATOM   1551 C  CZ  . TYR   A 1 190 ? 21.489  1.657   -17.939 1.00 14.08 ? 631  TYR   A CZ  1 
ATOM   1552 O  OH  . TYR   A 1 190 ? 20.141  1.422   -17.860 1.00 13.50 ? 631  TYR   A OH  1 
ATOM   1553 N  N   . ILE   A 1 191 ? 24.465  5.343   -19.577 1.00 16.74 ? 632  ILE   A N   1 
ATOM   1554 C  CA  . ILE   A 1 191 ? 23.619  6.508   -19.324 1.00 14.92 ? 632  ILE   A CA  1 
ATOM   1555 C  C   . ILE   A 1 191 ? 22.174  6.070   -19.483 1.00 14.46 ? 632  ILE   A C   1 
ATOM   1556 O  O   . ILE   A 1 191 ? 21.773  5.669   -20.585 1.00 16.24 ? 632  ILE   A O   1 
ATOM   1557 C  CB  . ILE   A 1 191 ? 23.946  7.683   -20.266 1.00 16.93 ? 632  ILE   A CB  1 
ATOM   1558 C  CG1 . ILE   A 1 191 ? 25.454  8.031   -20.200 1.00 14.48 ? 632  ILE   A CG1 1 
ATOM   1559 C  CG2 . ILE   A 1 191 ? 23.092  8.880   -19.907 1.00 19.50 ? 632  ILE   A CG2 1 
ATOM   1560 C  CD1 . ILE   A 1 191 ? 25.837  9.271   -20.993 1.00 18.63 ? 632  ILE   A CD1 1 
ATOM   1561 N  N   . SER   A 1 192 ? 21.394  6.155   -18.410 1.00 13.83 ? 633  SER   A N   1 
ATOM   1562 C  CA  . SER   A 1 192 ? 19.985  5.799   -18.461 1.00 14.63 ? 633  SER   A CA  1 
ATOM   1563 C  C   . SER   A 1 192 ? 19.140  7.014   -18.117 1.00 14.50 ? 633  SER   A C   1 
ATOM   1564 O  O   . SER   A 1 192 ? 19.436  7.741   -17.172 1.00 16.52 ? 633  SER   A O   1 
ATOM   1565 C  CB  . SER   A 1 192 ? 19.663  4.646   -17.481 1.00 13.73 ? 633  SER   A CB  1 
ATOM   1566 O  OG  . SER   A 1 192 ? 18.280  4.357   -17.456 1.00 13.61 ? 633  SER   A OG  1 
ATOM   1567 N  N   . LEU   A 1 193 ? 18.085  7.229   -18.892 1.00 14.22 ? 634  LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 193 ? 17.006  8.124   -18.518 1.00 14.85 ? 634  LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 193 ? 15.803  7.254   -18.178 1.00 14.61 ? 634  LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 193 ? 15.526  6.282   -18.889 1.00 15.88 ? 634  LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 193 ? 16.659  9.069   -19.671 1.00 16.16 ? 634  LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 193 ? 17.819  9.784   -20.380 1.00 17.55 ? 634  LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 193 ? 18.300  9.013   -21.598 1.00 15.30 ? 634  LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 193 ? 17.366  11.186  -20.807 1.00 20.90 ? 634  LEU   A CD2 1 
ATOM   1575 N  N   . HIS   A 1 194 ? 15.076  7.584   -17.109 1.00 13.59 ? 635  HIS   A N   1 
ATOM   1576 C  CA  . HIS   A 1 194 ? 13.998  6.686   -16.705 1.00 14.71 ? 635  HIS   A CA  1 
ATOM   1577 C  C   . HIS   A 1 194 ? 13.031  7.360   -15.746 1.00 15.71 ? 635  HIS   A C   1 
ATOM   1578 O  O   . HIS   A 1 194 ? 13.415  8.212   -14.930 1.00 17.62 ? 635  HIS   A O   1 
ATOM   1579 C  CB  . HIS   A 1 194 ? 14.537  5.411   -16.025 1.00 16.65 ? 635  HIS   A CB  1 
ATOM   1580 C  CG  . HIS   A 1 194 ? 15.656  5.678   -15.070 1.00 13.54 ? 635  HIS   A CG  1 
ATOM   1581 N  ND1 . HIS   A 1 194 ? 16.962  5.782   -15.488 1.00 14.66 ? 635  HIS   A ND1 1 
ATOM   1582 C  CD2 . HIS   A 1 194 ? 15.656  5.907   -13.737 1.00 15.25 ? 635  HIS   A CD2 1 
ATOM   1583 C  CE1 . HIS   A 1 194 ? 17.732  6.051   -14.446 1.00 14.82 ? 635  HIS   A CE1 1 
ATOM   1584 N  NE2 . HIS   A 1 194 ? 16.965  6.129   -13.373 1.00 15.27 ? 635  HIS   A NE2 1 
ATOM   1585 N  N   . ARG   A 1 195 ? 11.783  6.913   -15.819 1.00 16.71 ? 636  ARG   A N   1 
ATOM   1586 C  CA  . ARG   A 1 195 ? 10.807  7.261   -14.808 1.00 14.07 ? 636  ARG   A CA  1 
ATOM   1587 C  C   . ARG   A 1 195 ? 11.195  6.585   -13.498 1.00 18.91 ? 636  ARG   A C   1 
ATOM   1588 O  O   . ARG   A 1 195 ? 11.446  5.375   -13.460 1.00 17.00 ? 636  ARG   A O   1 
ATOM   1589 C  CB  . ARG   A 1 195 ? 9.424   6.816   -15.263 1.00 15.25 ? 636  ARG   A CB  1 
ATOM   1590 C  CG  . ARG   A 1 195 ? 8.343   7.398   -14.377 1.00 16.59 ? 636  ARG   A CG  1 
ATOM   1591 C  CD  . ARG   A 1 195 ? 6.981   7.151   -14.959 1.00 16.04 ? 636  ARG   A CD  1 
ATOM   1592 N  NE  . ARG   A 1 195 ? 5.935   7.649   -14.066 1.00 18.73 ? 636  ARG   A NE  1 
ATOM   1593 C  CZ  . ARG   A 1 195 ? 4.640   7.403   -14.225 1.00 22.59 ? 636  ARG   A CZ  1 
ATOM   1594 N  NH1 . ARG   A 1 195 ? 4.221   6.672   -15.251 1.00 21.86 ? 636  ARG   A NH1 1 
ATOM   1595 N  NH2 . ARG   A 1 195 ? 3.762   7.891   -13.350 1.00 23.81 ? 636  ARG   A NH2 1 
ATOM   1596 N  N   . TYR   A 1 196 ? 11.274  7.377   -12.431 1.00 16.92 ? 637  TYR   A N   1 
ATOM   1597 C  CA  . TYR   A 1 196 ? 11.803  6.925   -11.149 1.00 18.09 ? 637  TYR   A CA  1 
ATOM   1598 C  C   . TYR   A 1 196 ? 10.775  7.048   -10.033 1.00 20.37 ? 637  TYR   A C   1 
ATOM   1599 O  O   . TYR   A 1 196 ? 10.520  6.070   -9.315  1.00 20.58 ? 637  TYR   A O   1 
ATOM   1600 C  CB  . TYR   A 1 196 ? 13.059  7.736   -10.811 1.00 17.65 ? 637  TYR   A CB  1 
ATOM   1601 C  CG  . TYR   A 1 196 ? 13.722  7.338   -9.503  1.00 23.83 ? 637  TYR   A CG  1 
ATOM   1602 C  CD1 . TYR   A 1 196 ? 14.177  6.038   -9.300  1.00 19.50 ? 637  TYR   A CD1 1 
ATOM   1603 C  CD2 . TYR   A 1 196 ? 13.901  8.265   -8.479  1.00 22.24 ? 637  TYR   A CD2 1 
ATOM   1604 C  CE1 . TYR   A 1 196 ? 14.797  5.663   -8.107  1.00 19.31 ? 637  TYR   A CE1 1 
ATOM   1605 C  CE2 . TYR   A 1 196 ? 14.506  7.906   -7.290  1.00 21.91 ? 637  TYR   A CE2 1 
ATOM   1606 C  CZ  . TYR   A 1 196 ? 14.944  6.605   -7.105  1.00 26.85 ? 637  TYR   A CZ  1 
ATOM   1607 O  OH  . TYR   A 1 196 ? 15.540  6.238   -5.914  1.00 23.22 ? 637  TYR   A OH  1 
ATOM   1608 N  N   . GLU   A 1 197 ? 10.136  8.214   -9.900  1.00 19.42 ? 638  GLU   A N   1 
ATOM   1609 C  CA  . GLU   A 1 197 ? 9.110   8.457   -8.888  1.00 19.37 ? 638  GLU   A CA  1 
ATOM   1610 C  C   . GLU   A 1 197 ? 9.618   8.103   -7.491  1.00 24.09 ? 638  GLU   A C   1 
ATOM   1611 O  O   . GLU   A 1 197 ? 8.980   7.368   -6.740  1.00 22.51 ? 638  GLU   A O   1 
ATOM   1612 C  CB  . GLU   A 1 197 ? 7.801   7.742   -9.217  1.00 22.14 ? 638  GLU   A CB  1 
ATOM   1613 C  CG  . GLU   A 1 197 ? 7.287   7.935   -10.660 1.00 22.21 ? 638  GLU   A CG  1 
ATOM   1614 C  CD  . GLU   A 1 197 ? 6.988   9.388   -11.032 1.00 35.38 ? 638  GLU   A CD  1 
ATOM   1615 O  OE1 . GLU   A 1 197 ? 7.068   10.293  -10.165 1.00 26.72 ? 638  GLU   A OE1 1 
ATOM   1616 O  OE2 . GLU   A 1 197 ? 6.633   9.617   -12.210 1.00 23.91 ? 638  GLU   A OE2 1 
ATOM   1617 N  N   . ASP   A 1 198 ? 10.806  8.614   -7.168  1.00 20.83 ? 639  ASP   A N   1 
ATOM   1618 C  CA  . ASP   A 1 198 ? 11.441  8.378   -5.866  1.00 26.86 ? 639  ASP   A CA  1 
ATOM   1619 C  C   . ASP   A 1 198 ? 11.459  6.895   -5.501  1.00 40.27 ? 639  ASP   A C   1 
ATOM   1620 O  O   . ASP   A 1 198 ? 11.194  6.506   -4.363  1.00 29.32 ? 639  ASP   A O   1 
ATOM   1621 C  CB  . ASP   A 1 198 ? 10.815  9.231   -4.763  1.00 26.46 ? 639  ASP   A CB  1 
ATOM   1622 C  CG  . ASP   A 1 198 ? 11.093  10.708  -4.954  1.00 43.28 ? 639  ASP   A CG  1 
ATOM   1623 O  OD1 . ASP   A 1 198 ? 12.275  11.068  -5.148  1.00 60.04 ? 639  ASP   A OD1 1 
ATOM   1624 O  OD2 . ASP   A 1 198 ? 10.130  11.504  -4.928  1.00 47.26 ? 639  ASP   A OD2 1 
ATOM   1625 N  N   . GLY   A 1 199 ? 11.752  6.053   -6.490  1.00 23.24 ? 640  GLY   A N   1 
ATOM   1626 C  CA  . GLY   A 1 199 ? 11.893  4.632   -6.264  1.00 24.95 ? 640  GLY   A CA  1 
ATOM   1627 C  C   . GLY   A 1 199 ? 10.622  3.820   -6.367  1.00 21.54 ? 640  GLY   A C   1 
ATOM   1628 O  O   . GLY   A 1 199 ? 10.678  2.595   -6.207  1.00 27.06 ? 640  GLY   A O   1 
ATOM   1629 N  N   . ALA   A 1 200 ? 9.484   4.447   -6.663  1.00 22.15 ? 641  ALA   A N   1 
ATOM   1630 C  CA  . ALA   A 1 200 ? 8.212   3.739   -6.699  1.00 23.81 ? 641  ALA   A CA  1 
ATOM   1631 C  C   . ALA   A 1 200 ? 7.918   3.071   -8.039  1.00 34.35 ? 641  ALA   A C   1 
ATOM   1632 O  O   . ALA   A 1 200 ? 7.058   2.186   -8.095  1.00 40.20 ? 641  ALA   A O   1 
ATOM   1633 C  CB  . ALA   A 1 200 ? 7.058   4.685   -6.343  1.00 29.54 ? 641  ALA   A CB  1 
ATOM   1634 N  N   . PHE   A 1 201 ? 8.607   3.462   -9.108  1.00 23.72 ? 642  PHE   A N   1 
ATOM   1635 C  CA  . PHE   A 1 201 ? 8.348   2.929   -10.442 1.00 21.14 ? 642  PHE   A CA  1 
ATOM   1636 C  C   . PHE   A 1 201 ? 9.254   1.737   -10.724 1.00 17.30 ? 642  PHE   A C   1 
ATOM   1637 O  O   . PHE   A 1 201 ? 10.414  1.724   -10.310 1.00 18.57 ? 642  PHE   A O   1 
ATOM   1638 C  CB  . PHE   A 1 201 ? 8.608   4.020   -11.477 1.00 17.09 ? 642  PHE   A CB  1 
ATOM   1639 C  CG  . PHE   A 1 201 ? 7.843   3.830   -12.765 1.00 17.52 ? 642  PHE   A CG  1 
ATOM   1640 C  CD1 . PHE   A 1 201 ? 6.474   4.042   -12.803 1.00 21.89 ? 642  PHE   A CD1 1 
ATOM   1641 C  CD2 . PHE   A 1 201 ? 8.488   3.433   -13.928 1.00 20.44 ? 642  PHE   A CD2 1 
ATOM   1642 C  CE1 . PHE   A 1 201 ? 5.767   3.867   -13.973 1.00 21.65 ? 642  PHE   A CE1 1 
ATOM   1643 C  CE2 . PHE   A 1 201 ? 7.776   3.260   -15.102 1.00 22.59 ? 642  PHE   A CE2 1 
ATOM   1644 C  CZ  . PHE   A 1 201 ? 6.425   3.476   -15.123 1.00 19.35 ? 642  PHE   A CZ  1 
ATOM   1645 N  N   . PHE   A 1 202 ? 8.712   0.738   -11.424 1.00 17.77 ? 643  PHE   A N   1 
ATOM   1646 C  CA  . PHE   A 1 202 ? 9.472   -0.469  -11.737 1.00 17.24 ? 643  PHE   A CA  1 
ATOM   1647 C  C   . PHE   A 1 202 ? 10.818  -0.088  -12.346 1.00 15.68 ? 643  PHE   A C   1 
ATOM   1648 O  O   . PHE   A 1 202 ? 10.872  0.788   -13.219 1.00 15.78 ? 643  PHE   A O   1 
ATOM   1649 C  CB  . PHE   A 1 202 ? 8.697   -1.331  -12.744 1.00 17.78 ? 643  PHE   A CB  1 
ATOM   1650 C  CG  . PHE   A 1 202 ? 9.345   -2.652  -13.007 1.00 16.72 ? 643  PHE   A CG  1 
ATOM   1651 C  CD1 . PHE   A 1 202 ? 10.300  -2.788  -14.007 1.00 15.71 ? 643  PHE   A CD1 1 
ATOM   1652 C  CD2 . PHE   A 1 202 ? 9.042   -3.760  -12.214 1.00 17.34 ? 643  PHE   A CD2 1 
ATOM   1653 C  CE1 . PHE   A 1 202 ? 10.926  -3.997  -14.228 1.00 18.70 ? 643  PHE   A CE1 1 
ATOM   1654 C  CE2 . PHE   A 1 202 ? 9.675   -4.980  -12.432 1.00 20.11 ? 643  PHE   A CE2 1 
ATOM   1655 C  CZ  . PHE   A 1 202 ? 10.611  -5.097  -13.440 1.00 17.79 ? 643  PHE   A CZ  1 
ATOM   1656 N  N   . PRO   A 1 203 ? 11.924  -0.747  -11.958 1.00 15.47 ? 644  PRO   A N   1 
ATOM   1657 C  CA  . PRO   A 1 203 ? 12.036  -1.933  -11.098 1.00 18.34 ? 644  PRO   A CA  1 
ATOM   1658 C  C   . PRO   A 1 203 ? 12.153  -1.664  -9.594  1.00 21.32 ? 644  PRO   A C   1 
ATOM   1659 O  O   . PRO   A 1 203 ? 12.642  -2.544  -8.885  1.00 19.55 ? 644  PRO   A O   1 
ATOM   1660 C  CB  . PRO   A 1 203 ? 13.326  -2.602  -11.597 1.00 20.65 ? 644  PRO   A CB  1 
ATOM   1661 C  CG  . PRO   A 1 203 ? 14.164  -1.481  -12.102 1.00 18.35 ? 644  PRO   A CG  1 
ATOM   1662 C  CD  . PRO   A 1 203 ? 13.211  -0.403  -12.585 1.00 15.51 ? 644  PRO   A CD  1 
ATOM   1663 N  N   . ASN   A 1 204 ? 11.745  -0.481  -9.135  1.00 17.14 ? 645  ASN   A N   1 
ATOM   1664 C  CA  . ASN   A 1 204 ? 11.415  -0.244  -7.725  1.00 21.00 ? 645  ASN   A CA  1 
ATOM   1665 C  C   . ASN   A 1 204 ? 12.644  -0.218  -6.817  1.00 21.30 ? 645  ASN   A C   1 
ATOM   1666 O  O   . ASN   A 1 204 ? 12.583  -0.658  -5.667  1.00 23.02 ? 645  ASN   A O   1 
ATOM   1667 C  CB  . ASN   A 1 204 ? 10.381  -1.248  -7.215  1.00 22.17 ? 645  ASN   A CB  1 
ATOM   1668 C  CG  . ASN   A 1 204 ? 9.112   -1.208  -8.004  1.00 26.87 ? 645  ASN   A CG  1 
ATOM   1669 O  OD1 . ASN   A 1 204 ? 8.861   -2.095  -8.808  1.00 29.45 ? 645  ASN   A OD1 1 
ATOM   1670 N  ND2 . ASN   A 1 204 ? 8.304   -0.168  -7.794  1.00 29.17 ? 645  ASN   A ND2 1 
ATOM   1671 N  N   . SER   A 1 205 ? 13.756  0.303   -7.319  1.00 18.63 ? 646  SER   A N   1 
ATOM   1672 C  CA  . SER   A 1 205 ? 15.002  0.299   -6.573  1.00 16.65 ? 646  SER   A CA  1 
ATOM   1673 C  C   . SER   A 1 205 ? 15.653  1.673   -6.601  1.00 21.46 ? 646  SER   A C   1 
ATOM   1674 O  O   . SER   A 1 205 ? 15.742  2.315   -7.657  1.00 19.58 ? 646  SER   A O   1 
ATOM   1675 C  CB  . SER   A 1 205 ? 15.965  -0.724  -7.168  1.00 16.57 ? 646  SER   A CB  1 
ATOM   1676 O  OG  . SER   A 1 205 ? 17.236  -0.630  -6.561  1.00 21.14 ? 646  SER   A OG  1 
ATOM   1677 N  N   . GLU   A 1 206 ? 16.135  2.113   -5.431  1.00 17.91 ? 647  GLU   A N   1 
ATOM   1678 C  CA  . GLU   A 1 206 ? 16.923  3.334   -5.390  1.00 16.64 ? 647  GLU   A CA  1 
ATOM   1679 C  C   . GLU   A 1 206 ? 18.262  3.213   -6.093  1.00 15.54 ? 647  GLU   A C   1 
ATOM   1680 O  O   . GLU   A 1 206 ? 18.978  4.214   -6.197  1.00 17.86 ? 647  GLU   A O   1 
ATOM   1681 C  CB  . GLU   A 1 206 ? 17.111  3.796   -3.940  1.00 18.33 ? 647  GLU   A CB  1 
ATOM   1682 C  CG  . GLU   A 1 206 ? 15.785  4.068   -3.265  1.00 17.58 ? 647  GLU   A CG  1 
ATOM   1683 C  CD  . GLU   A 1 206 ? 15.930  4.741   -1.905  1.00 31.73 ? 647  GLU   A CD  1 
ATOM   1684 O  OE1 . GLU   A 1 206 ? 16.918  5.467   -1.700  1.00 38.61 ? 647  GLU   A OE1 1 
ATOM   1685 O  OE2 . GLU   A 1 206 ? 15.034  4.561   -1.063  1.00 26.20 ? 647  GLU   A OE2 1 
ATOM   1686 N  N   . ASP   A 1 207 ? 18.621  2.031   -6.611  1.00 18.47 ? 648  ASP   A N   1 
ATOM   1687 C  CA  . ASP   A 1 207 ? 19.799  1.924   -7.474  1.00 19.21 ? 648  ASP   A CA  1 
ATOM   1688 C  C   . ASP   A 1 207 ? 19.700  2.850   -8.685  1.00 14.21 ? 648  ASP   A C   1 
ATOM   1689 O  O   . ASP   A 1 207 ? 20.725  3.208   -9.276  1.00 16.12 ? 648  ASP   A O   1 
ATOM   1690 C  CB  . ASP   A 1 207 ? 19.949  0.494   -8.000  1.00 19.60 ? 648  ASP   A CB  1 
ATOM   1691 C  CG  . ASP   A 1 207 ? 20.303  -0.509  -6.918  1.00 33.63 ? 648  ASP   A CG  1 
ATOM   1692 O  OD1 . ASP   A 1 207 ? 20.586  -0.103  -5.772  1.00 26.51 ? 648  ASP   A OD1 1 
ATOM   1693 O  OD2 . ASP   A 1 207 ? 20.296  -1.717  -7.228  1.00 28.31 ? 648  ASP   A OD2 1 
ATOM   1694 N  N   . ALA   A 1 208 ? 18.478  3.202   -9.091  1.00 16.48 ? 649  ALA   A N   1 
ATOM   1695 C  CA  . ALA   A 1 208 ? 18.248  4.052   -10.259 1.00 17.06 ? 649  ALA   A CA  1 
ATOM   1696 C  C   . ALA   A 1 208 ? 18.406  5.548   -9.968  1.00 24.29 ? 649  ALA   A C   1 
ATOM   1697 O  O   . ALA   A 1 208 ? 18.230  6.367   -10.883 1.00 18.45 ? 649  ALA   A O   1 
ATOM   1698 C  CB  . ALA   A 1 208 ? 16.860  3.767   -10.839 1.00 17.24 ? 649  ALA   A CB  1 
ATOM   1699 N  N   . ASN   A 1 209 ? 18.725  5.943   -8.731  1.00 18.49 ? 650  ASN   A N   1 
ATOM   1700 C  CA  . ASN   A 1 209 ? 18.781  7.365   -8.429  1.00 18.77 ? 650  ASN   A CA  1 
ATOM   1701 C  C   . ASN   A 1 209 ? 20.053  7.998   -8.992  1.00 16.53 ? 650  ASN   A C   1 
ATOM   1702 O  O   . ASN   A 1 209 ? 21.035  7.324   -9.336  1.00 17.00 ? 650  ASN   A O   1 
ATOM   1703 C  CB  . ASN   A 1 209 ? 18.661  7.611   -6.918  1.00 21.13 ? 650  ASN   A CB  1 
ATOM   1704 C  CG  . ASN   A 1 209 ? 17.947  8.909   -6.607  1.00 27.96 ? 650  ASN   A CG  1 
ATOM   1705 O  OD1 . ASN   A 1 209 ? 17.713  9.719   -7.498  1.00 23.27 ? 650  ASN   A OD1 1 
ATOM   1706 N  ND2 . ASN   A 1 209 ? 17.614  9.123   -5.340  1.00 24.14 ? 650  ASN   A ND2 1 
ATOM   1707 N  N   . TYR   A 1 210 ? 20.048  9.341   -9.024  1.00 19.99 ? 651  TYR   A N   1 
ATOM   1708 C  CA  . TYR   A 1 210 ? 21.141  10.079  -9.650  1.00 18.67 ? 651  TYR   A CA  1 
ATOM   1709 C  C   . TYR   A 1 210 ? 22.456  9.950   -8.893  1.00 19.22 ? 651  TYR   A C   1 
ATOM   1710 O  O   . TYR   A 1 210 ? 23.525  10.135  -9.490  1.00 20.70 ? 651  TYR   A O   1 
ATOM   1711 C  CB  . TYR   A 1 210 ? 20.789  11.564  -9.830  1.00 18.99 ? 651  TYR   A CB  1 
ATOM   1712 C  CG  . TYR   A 1 210 ? 20.474  12.256  -8.520  1.00 23.97 ? 651  TYR   A CG  1 
ATOM   1713 C  CD1 . TYR   A 1 210 ? 21.489  12.765  -7.719  1.00 29.58 ? 651  TYR   A CD1 1 
ATOM   1714 C  CD2 . TYR   A 1 210 ? 19.171  12.377  -8.078  1.00 21.32 ? 651  TYR   A CD2 1 
ATOM   1715 C  CE1 . TYR   A 1 210 ? 21.200  13.378  -6.505  1.00 24.69 ? 651  TYR   A CE1 1 
ATOM   1716 C  CE2 . TYR   A 1 210 ? 18.872  12.989  -6.877  1.00 25.76 ? 651  TYR   A CE2 1 
ATOM   1717 C  CZ  . TYR   A 1 210 ? 19.895  13.479  -6.098  1.00 23.37 ? 651  TYR   A CZ  1 
ATOM   1718 O  OH  . TYR   A 1 210 ? 19.584  14.089  -4.902  1.00 32.47 ? 651  TYR   A OH  1 
ATOM   1719 N  N   . ASP   A 1 211 ? 22.398  9.622   -7.604  1.00 21.33 ? 652  ASP   A N   1 
ATOM   1720 C  CA  . ASP   A 1 211 ? 23.613  9.539   -6.810  1.00 22.62 ? 652  ASP   A CA  1 
ATOM   1721 C  C   . ASP   A 1 211 ? 24.376  8.237   -7.005  1.00 27.79 ? 652  ASP   A C   1 
ATOM   1722 O  O   . ASP   A 1 211 ? 25.447  8.079   -6.414  1.00 25.80 ? 652  ASP   A O   1 
ATOM   1723 C  CB  . ASP   A 1 211 ? 23.318  9.776   -5.326  1.00 20.66 ? 652  ASP   A CB  1 
ATOM   1724 C  CG  . ASP   A 1 211 ? 22.416  8.708   -4.715  1.00 41.17 ? 652  ASP   A CG  1 
ATOM   1725 O  OD1 . ASP   A 1 211 ? 21.700  8.007   -5.458  1.00 27.79 ? 652  ASP   A OD1 1 
ATOM   1726 O  OD2 . ASP   A 1 211 ? 22.421  8.575   -3.472  1.00 41.70 ? 652  ASP   A OD2 1 
ATOM   1727 N  N   . LYS   A 1 212 ? 23.878  7.312   -7.823  1.00 20.25 ? 653  LYS   A N   1 
ATOM   1728 C  CA  . LYS   A 1 212 ? 24.608  6.084   -8.116  1.00 19.51 ? 653  LYS   A CA  1 
ATOM   1729 C  C   . LYS   A 1 212 ? 25.478  6.353   -9.334  1.00 21.76 ? 653  LYS   A C   1 
ATOM   1730 O  O   . LYS   A 1 212 ? 25.011  6.303   -10.474 1.00 21.37 ? 653  LYS   A O   1 
ATOM   1731 C  CB  . LYS   A 1 212 ? 23.644  4.913   -8.278  1.00 20.63 ? 653  LYS   A CB  1 
ATOM   1732 C  CG  . LYS   A 1 212 ? 22.547  4.861   -7.178  1.00 23.37 ? 653  LYS   A CG  1 
ATOM   1733 C  CD  . LYS   A 1 212 ? 23.132  4.790   -5.763  1.00 27.09 ? 653  LYS   A CD  1 
ATOM   1734 C  CE  . LYS   A 1 212 ? 22.064  4.468   -4.715  1.00 24.78 ? 653  LYS   A CE  1 
ATOM   1735 N  NZ  . LYS   A 1 212 ? 21.029  5.542   -4.504  1.00 20.17 ? 653  LYS   A NZ  1 
ATOM   1736 N  N   . VAL   A 1 213 ? 26.756  6.655   -9.090  1.00 18.93 ? 654  VAL   A N   1 
ATOM   1737 C  CA  . VAL   A 1 213 ? 27.674  7.128   -10.121 1.00 19.51 ? 654  VAL   A CA  1 
ATOM   1738 C  C   . VAL   A 1 213 ? 28.643  6.053   -10.596 1.00 15.47 ? 654  VAL   A C   1 
ATOM   1739 O  O   . VAL   A 1 213 ? 29.498  6.336   -11.442 1.00 19.85 ? 654  VAL   A O   1 
ATOM   1740 C  CB  . VAL   A 1 213 ? 28.453  8.391   -9.684  1.00 23.52 ? 654  VAL   A CB  1 
ATOM   1741 C  CG1 . VAL   A 1 213 ? 27.519  9.543   -9.384  1.00 21.89 ? 654  VAL   A CG1 1 
ATOM   1742 C  CG2 . VAL   A 1 213 ? 29.347  8.085   -8.477  1.00 20.13 ? 654  VAL   A CG2 1 
ATOM   1743 N  N   . GLY   A 1 214 ? 28.526  4.831   -10.085 1.00 19.92 ? 655  GLY   A N   1 
ATOM   1744 C  CA  . GLY   A 1 214 ? 29.488  3.778   -10.332 1.00 18.42 ? 655  GLY   A CA  1 
ATOM   1745 C  C   . GLY   A 1 214 ? 30.328  3.489   -9.096  1.00 18.03 ? 655  GLY   A C   1 
ATOM   1746 O  O   . GLY   A 1 214 ? 30.301  4.213   -8.102  1.00 22.24 ? 655  GLY   A O   1 
ATOM   1747 N  N   . LEU   A 1 215 ? 31.085  2.402   -9.200  1.00 16.20 ? 656  LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 215 ? 31.915  1.930   -8.067  1.00 16.76 ? 656  LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 215 ? 33.320  1.607   -8.557  1.00 17.87 ? 656  LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 215 ? 33.512  1.201   -9.696  1.00 18.02 ? 656  LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 215 ? 31.257  0.678   -7.486  1.00 18.21 ? 656  LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 215 ? 29.866  0.865   -6.876  1.00 23.45 ? 656  LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 215 ? 29.243  -0.470  -6.528  1.00 23.49 ? 656  LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 215 ? 29.939  1.752   -5.654  1.00 24.91 ? 656  LEU   A CD2 1 
ATOM   1755 N  N   . GLY   A 1 216 ? 34.277  1.745   -7.650  1.00 18.75 ? 657  GLY   A N   1 
ATOM   1756 C  CA  . GLY   A 1 216 ? 35.653  1.370   -7.995  1.00 17.25 ? 657  GLY   A CA  1 
ATOM   1757 C  C   . GLY   A 1 216 ? 36.179  2.149   -9.183  1.00 15.76 ? 657  GLY   A C   1 
ATOM   1758 O  O   . GLY   A 1 216 ? 35.961  3.352   -9.254  1.00 23.38 ? 657  GLY   A O   1 
ATOM   1759 N  N   . LYS   A 1 217 ? 36.792  1.446   -10.107 1.00 16.00 ? 658  LYS   A N   1 
ATOM   1760 C  CA  . LYS   A 1 217 ? 37.288  2.128   -11.331 1.00 17.54 ? 658  LYS   A CA  1 
ATOM   1761 C  C   . LYS   A 1 217 ? 36.132  2.648   -12.197 1.00 33.73 ? 658  LYS   A C   1 
ATOM   1762 O  O   . LYS   A 1 217 ? 36.403  3.475   -13.073 1.00 29.58 ? 658  LYS   A O   1 
ATOM   1763 C  CB  . LYS   A 1 217 ? 38.157  1.210   -12.173 1.00 24.20 ? 658  LYS   A CB  1 
ATOM   1764 C  CG  . LYS   A 1 217 ? 37.483  0.086   -12.930 1.00 59.58 ? 658  LYS   A CG  1 
ATOM   1765 C  CD  . LYS   A 1 217 ? 38.456  -0.662  -13.831 1.00 75.95 ? 658  LYS   A CD  1 
ATOM   1766 C  CE  . LYS   A 1 217 ? 37.828  -1.709  -14.699 1.00 49.92 ? 658  LYS   A CE  1 
ATOM   1767 N  NZ  . LYS   A 1 217 ? 37.125  -2.759  -13.956 1.00 61.91 ? 658  LYS   A NZ  1 
ATOM   1768 N  N   . GLY   A 1 218 ? 34.907  2.210   -11.937 1.00 18.31 ? 659  GLY   A N   1 
ATOM   1769 C  CA  . GLY   A 1 218 ? 33.763  2.761   -12.673 1.00 21.40 ? 659  GLY   A CA  1 
ATOM   1770 C  C   . GLY   A 1 218 ? 33.196  4.000   -12.033 1.00 20.39 ? 659  GLY   A C   1 
ATOM   1771 O  O   . GLY   A 1 218 ? 32.135  4.428   -12.498 1.00 23.44 ? 659  GLY   A O   1 
ATOM   1772 N  N   A ARG   A 1 219 ? 33.746  4.649   -11.100 0.85 19.54 ? 660  ARG   A N   1 
ATOM   1773 N  N   B ARG   A 1 219 ? 33.755  4.659   -11.116 0.15 19.65 ? 660  ARG   A N   1 
ATOM   1774 C  CA  A ARG   A 1 219 ? 33.125  5.844   -10.553 0.85 21.68 ? 660  ARG   A CA  1 
ATOM   1775 C  CA  B ARG   A 1 219 ? 33.143  5.853   -10.545 0.15 20.78 ? 660  ARG   A CA  1 
ATOM   1776 C  C   A ARG   A 1 219 ? 33.090  6.930   -11.618 0.85 25.03 ? 660  ARG   A C   1 
ATOM   1777 C  C   B ARG   A 1 219 ? 33.098  6.962   -11.591 0.15 22.29 ? 660  ARG   A C   1 
ATOM   1778 O  O   A ARG   A 1 219 ? 34.117  7.244   -12.225 0.85 27.18 ? 660  ARG   A O   1 
ATOM   1779 O  O   B ARG   A 1 219 ? 34.133  7.338   -12.152 0.15 22.35 ? 660  ARG   A O   1 
ATOM   1780 C  CB  A ARG   A 1 219 ? 33.902  6.325   -9.325  0.85 24.76 ? 660  ARG   A CB  1 
ATOM   1781 C  CB  B ARG   A 1 219 ? 33.930  6.301   -9.317  0.15 20.37 ? 660  ARG   A CB  1 
ATOM   1782 C  CG  A ARG   A 1 219 ? 33.863  5.365   -8.157  0.85 32.78 ? 660  ARG   A CG  1 
ATOM   1783 C  CG  B ARG   A 1 219 ? 33.584  5.527   -8.068  0.15 19.08 ? 660  ARG   A CG  1 
ATOM   1784 C  CD  A ARG   A 1 219 ? 34.564  5.961   -6.943  0.85 20.83 ? 660  ARG   A CD  1 
ATOM   1785 C  CD  B ARG   A 1 219 ? 32.510  6.243   -7.282  0.15 19.20 ? 660  ARG   A CD  1 
ATOM   1786 N  NE  A ARG   A 1 219 ? 33.816  7.085   -6.385  0.85 18.74 ? 660  ARG   A NE  1 
ATOM   1787 N  NE  B ARG   A 1 219 ? 32.950  6.564   -5.930  0.15 17.91 ? 660  ARG   A NE  1 
ATOM   1788 C  CZ  A ARG   A 1 219 ? 34.295  8.327   -6.284  0.85 20.48 ? 660  ARG   A CZ  1 
ATOM   1789 C  CZ  B ARG   A 1 219 ? 32.156  7.065   -4.990  0.15 20.99 ? 660  ARG   A CZ  1 
ATOM   1790 N  NH1 A ARG   A 1 219 ? 35.515  8.609   -6.714  0.85 18.30 ? 660  ARG   A NH1 1 
ATOM   1791 N  NH1 B ARG   A 1 219 ? 30.878  7.306   -5.258  0.15 13.62 ? 660  ARG   A NH1 1 
ATOM   1792 N  NH2 A ARG   A 1 219 ? 33.553  9.285   -5.744  0.85 23.35 ? 660  ARG   A NH2 1 
ATOM   1793 N  NH2 B ARG   A 1 219 ? 32.637  7.326   -3.783  0.15 18.12 ? 660  ARG   A NH2 1 
ATOM   1794 N  N   . GLY   A 1 220 ? 31.900  7.483   -11.855 1.00 26.40 ? 661  GLY   A N   1 
ATOM   1795 C  CA  . GLY   A 1 220 ? 31.676  8.456   -12.898 1.00 29.12 ? 661  GLY   A CA  1 
ATOM   1796 C  C   . GLY   A 1 220 ? 31.130  7.875   -14.188 1.00 33.88 ? 661  GLY   A C   1 
ATOM   1797 O  O   . GLY   A 1 220 ? 30.590  8.632   -15.006 1.00 24.31 ? 661  GLY   A O   1 
ATOM   1798 N  N   . TYR   A 1 221 ? 31.237  6.553   -14.380 1.00 21.33 ? 662  TYR   A N   1 
ATOM   1799 C  CA  . TYR   A 1 221 ? 30.875  5.891   -15.630 1.00 21.02 ? 662  TYR   A CA  1 
ATOM   1800 C  C   . TYR   A 1 221 ? 29.480  5.260   -15.597 1.00 18.02 ? 662  TYR   A C   1 
ATOM   1801 O  O   . TYR   A 1 221 ? 29.192  4.373   -16.424 1.00 17.07 ? 662  TYR   A O   1 
ATOM   1802 C  CB  . TYR   A 1 221 ? 31.945  4.882   -16.039 1.00 18.40 ? 662  TYR   A CB  1 
ATOM   1803 C  CG  . TYR   A 1 221 ? 33.263  5.547   -16.333 1.00 20.16 ? 662  TYR   A CG  1 
ATOM   1804 C  CD1 . TYR   A 1 221 ? 34.178  5.814   -15.316 1.00 23.84 ? 662  TYR   A CD1 1 
ATOM   1805 C  CD2 . TYR   A 1 221 ? 33.569  5.966   -17.616 1.00 19.49 ? 662  TYR   A CD2 1 
ATOM   1806 C  CE1 . TYR   A 1 221 ? 35.386  6.447   -15.589 1.00 33.92 ? 662  TYR   A CE1 1 
ATOM   1807 C  CE2 . TYR   A 1 221 ? 34.768  6.597   -17.902 1.00 17.97 ? 662  TYR   A CE2 1 
ATOM   1808 C  CZ  . TYR   A 1 221 ? 35.674  6.836   -16.885 1.00 26.57 ? 662  TYR   A CZ  1 
ATOM   1809 O  OH  . TYR   A 1 221 ? 36.866  7.466   -17.173 1.00 33.11 ? 662  TYR   A OH  1 
ATOM   1810 N  N   . ASN   A 1 222 ? 28.644  5.686   -14.647 1.00 17.09 ? 663  ASN   A N   1 
ATOM   1811 C  CA  . ASN   A 1 222 ? 27.237  5.321   -14.552 1.00 15.89 ? 663  ASN   A CA  1 
ATOM   1812 C  C   . ASN   A 1 222 ? 26.460  6.609   -14.317 1.00 17.79 ? 663  ASN   A C   1 
ATOM   1813 O  O   . ASN   A 1 222 ? 26.653  7.276   -13.292 1.00 19.78 ? 663  ASN   A O   1 
ATOM   1814 C  CB  . ASN   A 1 222 ? 26.982  4.347   -13.389 1.00 16.45 ? 663  ASN   A CB  1 
ATOM   1815 C  CG  . ASN   A 1 222 ? 25.609  3.715   -13.452 1.00 17.36 ? 663  ASN   A CG  1 
ATOM   1816 O  OD1 . ASN   A 1 222 ? 25.409  2.735   -14.171 1.00 16.86 ? 663  ASN   A OD1 1 
ATOM   1817 N  ND2 . ASN   A 1 222 ? 24.655  4.283   -12.743 1.00 17.22 ? 663  ASN   A ND2 1 
ATOM   1818 N  N   . VAL   A 1 223 ? 25.574  6.955   -15.250 1.00 18.40 ? 664  VAL   A N   1 
ATOM   1819 C  CA  . VAL   A 1 223 ? 24.829  8.207   -15.202 1.00 15.37 ? 664  VAL   A CA  1 
ATOM   1820 C  C   . VAL   A 1 223 ? 23.345  7.875   -15.218 1.00 18.43 ? 664  VAL   A C   1 
ATOM   1821 O  O   . VAL   A 1 223 ? 22.811  7.443   -16.251 1.00 17.34 ? 664  VAL   A O   1 
ATOM   1822 C  CB  . VAL   A 1 223 ? 25.192  9.122   -16.381 1.00 21.10 ? 664  VAL   A CB  1 
ATOM   1823 C  CG1 . VAL   A 1 223 ? 24.395  10.414  -16.319 1.00 16.60 ? 664  VAL   A CG1 1 
ATOM   1824 C  CG2 . VAL   A 1 223 ? 26.703  9.378   -16.424 1.00 19.81 ? 664  VAL   A CG2 1 
ATOM   1825 N  N   . ASN   A 1 224 ? 22.676  8.077   -14.090 1.00 17.82 ? 665  ASN   A N   1 
ATOM   1826 C  CA  . ASN   A 1 224 ? 21.239  7.888   -13.990 1.00 17.31 ? 665  ASN   A CA  1 
ATOM   1827 C  C   . ASN   A 1 224 ? 20.560  9.244   -14.027 1.00 21.21 ? 665  ASN   A C   1 
ATOM   1828 O  O   . ASN   A 1 224 ? 20.884  10.125  -13.221 1.00 20.52 ? 665  ASN   A O   1 
ATOM   1829 C  CB  . ASN   A 1 224 ? 20.857  7.206   -12.678 1.00 17.49 ? 665  ASN   A CB  1 
ATOM   1830 C  CG  . ASN   A 1 224 ? 21.134  5.717   -12.691 1.00 18.53 ? 665  ASN   A CG  1 
ATOM   1831 O  OD1 . ASN   A 1 224 ? 21.122  5.077   -13.743 1.00 14.79 ? 665  ASN   A OD1 1 
ATOM   1832 N  ND2 . ASN   A 1 224 ? 21.415  5.157   -11.513 1.00 17.28 ? 665  ASN   A ND2 1 
ATOM   1833 N  N   . ILE   A 1 225 ? 19.599  9.393   -14.937 1.00 16.89 ? 666  ILE   A N   1 
ATOM   1834 C  CA  . ILE   A 1 225 ? 18.796  10.605  -15.065 1.00 18.74 ? 666  ILE   A CA  1 
ATOM   1835 C  C   . ILE   A 1 225 ? 17.369  10.239  -14.680 1.00 18.27 ? 666  ILE   A C   1 
ATOM   1836 O  O   . ILE   A 1 225 ? 16.598  9.762   -15.525 1.00 16.61 ? 666  ILE   A O   1 
ATOM   1837 C  CB  . ILE   A 1 225 ? 18.886  11.177  -16.486 1.00 21.39 ? 666  ILE   A CB  1 
ATOM   1838 C  CG1 . ILE   A 1 225 ? 20.353  11.390  -16.852 1.00 18.62 ? 666  ILE   A CG1 1 
ATOM   1839 C  CG2 . ILE   A 1 225 ? 18.032  12.453  -16.598 1.00 17.03 ? 666  ILE   A CG2 1 
ATOM   1840 C  CD1 . ILE   A 1 225 ? 20.602  11.866  -18.291 1.00 18.21 ? 666  ILE   A CD1 1 
ATOM   1841 N  N   . PRO   A 1 226 ? 16.971  10.431  -13.424 1.00 16.40 ? 667  PRO   A N   1 
ATOM   1842 C  CA  . PRO   A 1 226 ? 15.679  9.916   -12.972 1.00 16.81 ? 667  PRO   A CA  1 
ATOM   1843 C  C   . PRO   A 1 226 ? 14.571  10.959  -12.965 1.00 20.94 ? 667  PRO   A C   1 
ATOM   1844 O  O   . PRO   A 1 226 ? 14.760  12.055  -12.430 1.00 23.33 ? 667  PRO   A O   1 
ATOM   1845 C  CB  . PRO   A 1 226 ? 15.978  9.436   -11.543 1.00 20.87 ? 667  PRO   A CB  1 
ATOM   1846 C  CG  . PRO   A 1 226 ? 17.177  10.223  -11.115 1.00 25.07 ? 667  PRO   A CG  1 
ATOM   1847 C  CD  . PRO   A 1 226 ? 17.827  10.870  -12.311 1.00 18.01 ? 667  PRO   A CD  1 
ATOM   1848 N  N   . TRP   A 1 227 ? 13.412  10.631  -13.537 1.00 19.23 ? 668  TRP   A N   1 
ATOM   1849 C  CA  . TRP   A 1 227 ? 12.296  11.566  -13.609 1.00 20.80 ? 668  TRP   A CA  1 
ATOM   1850 C  C   . TRP   A 1 227 ? 11.333  11.322  -12.458 1.00 20.78 ? 668  TRP   A C   1 
ATOM   1851 O  O   . TRP   A 1 227 ? 11.004  10.173  -12.142 1.00 19.36 ? 668  TRP   A O   1 
ATOM   1852 C  CB  . TRP   A 1 227 ? 11.527  11.397  -14.924 1.00 18.29 ? 668  TRP   A CB  1 
ATOM   1853 C  CG  . TRP   A 1 227 ? 12.343  11.534  -16.164 1.00 20.37 ? 668  TRP   A CG  1 
ATOM   1854 C  CD1 . TRP   A 1 227 ? 12.474  10.602  -17.152 1.00 18.08 ? 668  TRP   A CD1 1 
ATOM   1855 C  CD2 . TRP   A 1 227 ? 13.147  12.660  -16.565 1.00 19.17 ? 668  TRP   A CD2 1 
ATOM   1856 N  NE1 . TRP   A 1 227 ? 13.289  11.080  -18.153 1.00 19.37 ? 668  TRP   A NE1 1 
ATOM   1857 C  CE2 . TRP   A 1 227 ? 13.719  12.339  -17.818 1.00 20.67 ? 668  TRP   A CE2 1 
ATOM   1858 C  CE3 . TRP   A 1 227 ? 13.422  13.912  -15.999 1.00 20.54 ? 668  TRP   A CE3 1 
ATOM   1859 C  CZ2 . TRP   A 1 227 ? 14.553  13.223  -18.509 1.00 19.25 ? 668  TRP   A CZ2 1 
ATOM   1860 C  CZ3 . TRP   A 1 227 ? 14.258  14.784  -16.685 1.00 21.69 ? 668  TRP   A CZ3 1 
ATOM   1861 C  CH2 . TRP   A 1 227 ? 14.812  14.434  -17.926 1.00 21.71 ? 668  TRP   A CH2 1 
ATOM   1862 N  N   . ASN   A 1 228 ? 10.851  12.413  -11.859 1.00 25.83 ? 669  ASN   A N   1 
ATOM   1863 C  CA  . ASN   A 1 228 ? 9.858   12.370  -10.796 1.00 23.40 ? 669  ASN   A CA  1 
ATOM   1864 C  C   . ASN   A 1 228 ? 8.753   13.378  -11.088 1.00 23.66 ? 669  ASN   A C   1 
ATOM   1865 O  O   . ASN   A 1 228 ? 9.030   14.496  -11.525 1.00 27.84 ? 669  ASN   A O   1 
ATOM   1866 C  CB  . ASN   A 1 228 ? 10.498  12.732  -9.437  1.00 19.33 ? 669  ASN   A CB  1 
ATOM   1867 C  CG  . ASN   A 1 228 ? 11.640  11.800  -9.059  1.00 22.97 ? 669  ASN   A CG  1 
ATOM   1868 O  OD1 . ASN   A 1 228 ? 11.449  10.596  -8.963  1.00 25.05 ? 669  ASN   A OD1 1 
ATOM   1869 N  ND2 . ASN   A 1 228 ? 12.838  12.352  -8.890  1.00 23.62 ? 669  ASN   A ND2 1 
ATOM   1870 N  N   . GLY   A 1 229 ? 7.507   12.973  -10.863 1.00 21.21 ? 670  GLY   A N   1 
ATOM   1871 C  CA  . GLY   A 1 229 ? 6.388   13.898  -10.858 1.00 24.84 ? 670  GLY   A CA  1 
ATOM   1872 C  C   . GLY   A 1 229 ? 6.139   14.675  -12.136 1.00 36.24 ? 670  GLY   A C   1 
ATOM   1873 O  O   . GLY   A 1 229 ? 6.306   15.899  -12.177 1.00 33.03 ? 670  GLY   A O   1 
ATOM   1874 N  N   . GLY   A 1 230 ? 5.717   13.983  -13.186 1.00 33.95 ? 671  GLY   A N   1 
ATOM   1875 C  CA  . GLY   A 1 230 ? 5.436   14.658  -14.433 1.00 25.83 ? 671  GLY   A CA  1 
ATOM   1876 C  C   . GLY   A 1 230 ? 5.456   13.731  -15.627 1.00 28.12 ? 671  GLY   A C   1 
ATOM   1877 O  O   . GLY   A 1 230 ? 6.215   12.755  -15.659 1.00 23.32 ? 671  GLY   A O   1 
ATOM   1878 N  N   . LYS   A 1 231 ? 4.617   14.034  -16.616 1.00 26.18 ? 672  LYS   A N   1 
ATOM   1879 C  CA  . LYS   A 1 231 ? 4.487   13.224  -17.825 1.00 25.08 ? 672  LYS   A CA  1 
ATOM   1880 C  C   . LYS   A 1 231 ? 5.528   13.744  -18.800 1.00 23.03 ? 672  LYS   A C   1 
ATOM   1881 O  O   . LYS   A 1 231 ? 5.257   14.614  -19.626 0.81 21.37 ? 672  LYS   A O   1 
ATOM   1882 C  CB  . LYS   A 1 231 ? 3.078   13.336  -18.391 1.00 22.55 ? 672  LYS   A CB  1 
ATOM   1883 C  CG  . LYS   A 1 231 ? 2.097   12.382  -17.747 1.00 42.54 ? 672  LYS   A CG  1 
ATOM   1884 C  CD  . LYS   A 1 231 ? 0.720   12.436  -18.404 1.00 45.71 ? 672  LYS   A CD  1 
ATOM   1885 C  CE  . LYS   A 1 231 ? 0.836   12.540  -19.927 1.00 41.61 ? 672  LYS   A CE  1 
ATOM   1886 N  NZ  . LYS   A 1 231 ? 0.356   11.323  -20.666 1.00 40.56 ? 672  LYS   A NZ  1 
ATOM   1887 N  N   . MET   A 1 232 ? 6.738   13.202  -18.711 1.00 18.71 ? 673  MET   A N   1 
ATOM   1888 C  CA  . MET   A 1 232 ? 7.851   13.771  -19.446 1.00 20.20 ? 673  MET   A CA  1 
ATOM   1889 C  C   . MET   A 1 232 ? 7.739   13.446  -20.929 1.00 18.52 ? 673  MET   A C   1 
ATOM   1890 O  O   . MET   A 1 232 ? 7.121   12.455  -21.338 1.00 21.16 ? 673  MET   A O   1 
ATOM   1891 C  CB  . MET   A 1 232 ? 9.186   13.273  -18.896 1.00 21.43 ? 673  MET   A CB  1 
ATOM   1892 C  CG  . MET   A 1 232 ? 9.354   13.472  -17.391 1.00 22.39 ? 673  MET   A CG  1 
ATOM   1893 S  SD  . MET   A 1 232 ? 8.901   15.144  -16.870 1.00 23.36 ? 673  MET   A SD  1 
ATOM   1894 C  CE  . MET   A 1 232 ? 9.380   15.082  -15.135 1.00 23.29 ? 673  MET   A CE  1 
ATOM   1895 N  N   . GLY   A 1 233 ? 8.345   14.304  -21.734 1.00 17.65 ? 674  GLY   A N   1 
ATOM   1896 C  CA  . GLY   A 1 233 ? 8.197   14.219  -23.167 1.00 19.34 ? 674  GLY   A CA  1 
ATOM   1897 C  C   . GLY   A 1 233 ? 9.375   14.830  -23.877 1.00 18.75 ? 674  GLY   A C   1 
ATOM   1898 O  O   . GLY   A 1 233 ? 10.457  14.941  -23.300 1.00 18.77 ? 674  GLY   A O   1 
ATOM   1899 N  N   . ASP   A 1 234 ? 9.183   15.230  -25.131 1.00 19.57 ? 675  ASP   A N   1 
ATOM   1900 C  CA  . ASP   A 1 234 ? 10.289  15.743  -25.937 1.00 21.78 ? 675  ASP   A CA  1 
ATOM   1901 C  C   . ASP   A 1 234 ? 11.074  16.857  -25.259 1.00 19.05 ? 675  ASP   A C   1 
ATOM   1902 O  O   . ASP   A 1 234 ? 12.311  16.795  -25.272 1.00 20.47 ? 675  ASP   A O   1 
ATOM   1903 C  CB  . ASP   A 1 234 ? 9.797   16.180  -27.328 1.00 19.54 ? 675  ASP   A CB  1 
ATOM   1904 C  CG  . ASP   A 1 234 ? 9.208   15.042  -28.139 1.00 22.27 ? 675  ASP   A CG  1 
ATOM   1905 O  OD1 . ASP   A 1 234 ? 9.286   13.872  -27.716 1.00 19.47 ? 675  ASP   A OD1 1 
ATOM   1906 O  OD2 . ASP   A 1 234 ? 8.647   15.326  -29.227 1.00 24.20 ? 675  ASP   A OD2 1 
ATOM   1907 N  N   . PRO   A 1 235 ? 10.446  17.894  -24.680 1.00 20.74 ? 676  PRO   A N   1 
ATOM   1908 C  CA  . PRO   A 1 235 ? 11.256  18.972  -24.085 1.00 22.15 ? 676  PRO   A CA  1 
ATOM   1909 C  C   . PRO   A 1 235 ? 12.191  18.487  -22.997 1.00 21.43 ? 676  PRO   A C   1 
ATOM   1910 O  O   . PRO   A 1 235 ? 13.337  18.939  -22.922 1.00 21.99 ? 676  PRO   A O   1 
ATOM   1911 C  CB  . PRO   A 1 235 ? 10.207  19.953  -23.542 1.00 21.35 ? 676  PRO   A CB  1 
ATOM   1912 C  CG  . PRO   A 1 235 ? 8.982   19.660  -24.307 1.00 33.28 ? 676  PRO   A CG  1 
ATOM   1913 C  CD  . PRO   A 1 235 ? 9.005   18.191  -24.593 1.00 29.00 ? 676  PRO   A CD  1 
ATOM   1914 N  N   . GLU   A 1 236 ? 11.723  17.559  -22.161 1.00 20.59 ? 677  GLU   A N   1 
ATOM   1915 C  CA  . GLU   A 1 236 ? 12.537  17.062  -21.059 1.00 20.07 ? 677  GLU   A CA  1 
ATOM   1916 C  C   . GLU   A 1 236 ? 13.690  16.196  -21.560 1.00 20.46 ? 677  GLU   A C   1 
ATOM   1917 O  O   . GLU   A 1 236 ? 14.830  16.316  -21.078 1.00 19.51 ? 677  GLU   A O   1 
ATOM   1918 C  CB  . GLU   A 1 236 ? 11.631  16.309  -20.089 1.00 19.55 ? 677  GLU   A CB  1 
ATOM   1919 C  CG  . GLU   A 1 236 ? 10.609  17.189  -19.384 1.00 20.98 ? 677  GLU   A CG  1 
ATOM   1920 C  CD  . GLU   A 1 236 ? 9.461   17.661  -20.260 1.00 27.42 ? 677  GLU   A CD  1 
ATOM   1921 O  OE1 . GLU   A 1 236 ? 8.955   16.866  -21.077 1.00 24.65 ? 677  GLU   A OE1 1 
ATOM   1922 O  OE2 . GLU   A 1 236 ? 9.049   18.831  -20.117 1.00 30.13 ? 677  GLU   A OE2 1 
ATOM   1923 N  N   . TYR   A 1 237 ? 13.423  15.332  -22.542 1.00 19.45 ? 678  TYR   A N   1 
ATOM   1924 C  CA  . TYR   A 1 237 ? 14.482  14.496  -23.101 1.00 18.94 ? 678  TYR   A CA  1 
ATOM   1925 C  C   . TYR   A 1 237 ? 15.513  15.328  -23.857 1.00 17.71 ? 678  TYR   A C   1 
ATOM   1926 O  O   . TYR   A 1 237 ? 16.721  15.083  -23.751 1.00 18.59 ? 678  TYR   A O   1 
ATOM   1927 C  CB  . TYR   A 1 237 ? 13.895  13.354  -23.945 1.00 18.93 ? 678  TYR   A CB  1 
ATOM   1928 C  CG  . TYR   A 1 237 ? 13.423  12.218  -23.059 1.00 16.65 ? 678  TYR   A CG  1 
ATOM   1929 C  CD1 . TYR   A 1 237 ? 12.300  12.367  -22.259 1.00 16.62 ? 678  TYR   A CD1 1 
ATOM   1930 C  CD2 . TYR   A 1 237 ? 14.131  11.016  -22.990 1.00 17.36 ? 678  TYR   A CD2 1 
ATOM   1931 C  CE1 . TYR   A 1 237 ? 11.867  11.354  -21.411 1.00 15.82 ? 678  TYR   A CE1 1 
ATOM   1932 C  CE2 . TYR   A 1 237 ? 13.713  9.983   -22.134 1.00 17.03 ? 678  TYR   A CE2 1 
ATOM   1933 C  CZ  . TYR   A 1 237 ? 12.578  10.166  -21.352 1.00 15.86 ? 678  TYR   A CZ  1 
ATOM   1934 O  OH  . TYR   A 1 237 ? 12.131  9.189   -20.484 1.00 16.63 ? 678  TYR   A OH  1 
ATOM   1935 N  N   . MET   A 1 238 ? 15.065  16.329  -24.618 1.00 22.04 ? 679  MET   A N   1 
ATOM   1936 C  CA  . MET   A 1 238 ? 16.021  17.193  -25.301 1.00 18.48 ? 679  MET   A CA  1 
ATOM   1937 C  C   . MET   A 1 238 ? 16.890  17.955  -24.306 1.00 17.90 ? 679  MET   A C   1 
ATOM   1938 O  O   . MET   A 1 238 ? 18.094  18.111  -24.519 1.00 19.99 ? 679  MET   A O   1 
ATOM   1939 C  CB  . MET   A 1 238 ? 15.286  18.166  -26.222 1.00 20.26 ? 679  MET   A CB  1 
ATOM   1940 C  CG  . MET   A 1 238 ? 14.556  17.492  -27.364 1.00 21.85 ? 679  MET   A CG  1 
ATOM   1941 S  SD  . MET   A 1 238 ? 15.646  16.740  -28.587 1.00 27.67 ? 679  MET   A SD  1 
ATOM   1942 C  CE  . MET   A 1 238 ? 16.355  18.189  -29.380 1.00 33.32 ? 679  MET   A CE  1 
ATOM   1943 N  N   . ALA   A 1 239 ? 16.292  18.430  -23.212 1.00 19.62 ? 680  ALA   A N   1 
ATOM   1944 C  CA  . ALA   A 1 239 ? 17.061  19.149  -22.198 1.00 20.12 ? 680  ALA   A CA  1 
ATOM   1945 C  C   . ALA   A 1 239 ? 18.098  18.238  -21.546 1.00 20.12 ? 680  ALA   A C   1 
ATOM   1946 O  O   . ALA   A 1 239 ? 19.266  18.613  -21.396 1.00 21.73 ? 680  ALA   A O   1 
ATOM   1947 C  CB  . ALA   A 1 239 ? 16.110  19.750  -21.166 1.00 21.84 ? 680  ALA   A CB  1 
ATOM   1948 N  N   . ALA   A 1 240 ? 17.699  17.012  -21.195 1.00 22.38 ? 681  ALA   A N   1 
ATOM   1949 C  CA  . ALA   A 1 240 ? 18.665  16.063  -20.650 1.00 21.63 ? 681  ALA   A CA  1 
ATOM   1950 C  C   . ALA   A 1 240 ? 19.791  15.751  -21.640 1.00 23.35 ? 681  ALA   A C   1 
ATOM   1951 O  O   . ALA   A 1 240 ? 20.959  15.626  -21.245 1.00 19.31 ? 681  ALA   A O   1 
ATOM   1952 C  CB  . ALA   A 1 240 ? 17.945  14.804  -20.157 1.00 19.36 ? 681  ALA   A CB  1 
ATOM   1953 N  N   . PHE   A 1 241 ? 19.476  15.635  -22.937 1.00 18.04 ? 682  PHE   A N   1 
ATOM   1954 C  CA  . PHE   A 1 241 ? 20.535  15.398  -23.911 1.00 17.95 ? 682  PHE   A CA  1 
ATOM   1955 C  C   . PHE   A 1 241 ? 21.473  16.597  -24.029 1.00 23.70 ? 682  PHE   A C   1 
ATOM   1956 O  O   . PHE   A 1 241 ? 22.693  16.430  -24.147 1.00 20.90 ? 682  PHE   A O   1 
ATOM   1957 C  CB  . PHE   A 1 241 ? 19.947  15.044  -25.279 1.00 16.94 ? 682  PHE   A CB  1 
ATOM   1958 C  CG  . PHE   A 1 241 ? 19.846  13.560  -25.530 1.00 16.67 ? 682  PHE   A CG  1 
ATOM   1959 C  CD1 . PHE   A 1 241 ? 19.128  12.758  -24.654 1.00 16.43 ? 682  PHE   A CD1 1 
ATOM   1960 C  CD2 . PHE   A 1 241 ? 20.467  12.976  -26.628 1.00 19.63 ? 682  PHE   A CD2 1 
ATOM   1961 C  CE1 . PHE   A 1 241 ? 19.021  11.384  -24.869 1.00 17.72 ? 682  PHE   A CE1 1 
ATOM   1962 C  CE2 . PHE   A 1 241 ? 20.362  11.608  -26.850 1.00 19.03 ? 682  PHE   A CE2 1 
ATOM   1963 C  CZ  . PHE   A 1 241 ? 19.634  10.816  -25.953 1.00 18.45 ? 682  PHE   A CZ  1 
ATOM   1964 N  N   . HIS   A 1 242 ? 20.916  17.812  -24.007 1.00 23.06 ? 683  HIS   A N   1 
ATOM   1965 C  CA  . HIS   A 1 242 ? 21.746  19.007  -24.150 1.00 20.45 ? 683  HIS   A CA  1 
ATOM   1966 C  C   . HIS   A 1 242 ? 22.675  19.189  -22.952 1.00 21.10 ? 683  HIS   A C   1 
ATOM   1967 O  O   . HIS   A 1 242 ? 23.866  19.474  -23.118 1.00 23.84 ? 683  HIS   A O   1 
ATOM   1968 C  CB  . HIS   A 1 242 ? 20.844  20.233  -24.282 1.00 22.87 ? 683  HIS   A CB  1 
ATOM   1969 C  CG  . HIS   A 1 242 ? 21.603  21.520  -24.346 1.00 26.15 ? 683  HIS   A CG  1 
ATOM   1970 N  ND1 . HIS   A 1 242 ? 22.315  21.908  -25.460 1.00 34.07 ? 683  HIS   A ND1 1 
ATOM   1971 C  CD2 . HIS   A 1 242 ? 21.803  22.484  -23.416 1.00 35.62 ? 683  HIS   A CD2 1 
ATOM   1972 C  CE1 . HIS   A 1 242 ? 22.900  23.068  -25.223 1.00 42.51 ? 683  HIS   A CE1 1 
ATOM   1973 N  NE2 . HIS   A 1 242 ? 22.605  23.439  -23.990 1.00 44.92 ? 683  HIS   A NE2 1 
ATOM   1974 N  N   . HIS   A 1 243 ? 22.147  19.027  -21.739 1.00 19.48 ? 684  HIS   A N   1 
ATOM   1975 C  CA  . HIS   A 1 243 ? 22.905  19.349  -20.529 1.00 22.89 ? 684  HIS   A CA  1 
ATOM   1976 C  C   . HIS   A 1 243 ? 23.760  18.199  -20.014 1.00 34.62 ? 684  HIS   A C   1 
ATOM   1977 O  O   . HIS   A 1 243 ? 24.797  18.447  -19.383 1.00 26.13 ? 684  HIS   A O   1 
ATOM   1978 C  CB  . HIS   A 1 243 ? 21.958  19.780  -19.411 1.00 20.24 ? 684  HIS   A CB  1 
ATOM   1979 C  CG  . HIS   A 1 243 ? 21.372  21.143  -19.606 1.00 30.29 ? 684  HIS   A CG  1 
ATOM   1980 N  ND1 . HIS   A 1 243 ? 20.022  21.356  -19.789 1.00 44.21 ? 684  HIS   A ND1 1 
ATOM   1981 C  CD2 . HIS   A 1 243 ? 21.953  22.364  -19.636 1.00 28.69 ? 684  HIS   A CD2 1 
ATOM   1982 C  CE1 . HIS   A 1 243 ? 19.799  22.651  -19.934 1.00 31.01 ? 684  HIS   A CE1 1 
ATOM   1983 N  NE2 . HIS   A 1 243 ? 20.955  23.283  -19.849 1.00 35.63 ? 684  HIS   A NE2 1 
ATOM   1984 N  N   . LEU   A 1 244 ? 23.362  16.950  -20.262 1.00 31.05 ? 685  LEU   A N   1 
ATOM   1985 C  CA  . LEU   A 1 244 ? 24.006  15.796  -19.634 1.00 21.49 ? 685  LEU   A CA  1 
ATOM   1986 C  C   . LEU   A 1 244 ? 24.500  14.773  -20.644 1.00 18.57 ? 685  LEU   A C   1 
ATOM   1987 O  O   . LEU   A 1 244 ? 25.702  14.510  -20.717 1.00 20.85 ? 685  LEU   A O   1 
ATOM   1988 C  CB  . LEU   A 1 244 ? 23.046  15.132  -18.645 1.00 19.44 ? 685  LEU   A CB  1 
ATOM   1989 C  CG  . LEU   A 1 244 ? 22.670  15.927  -17.400 1.00 20.16 ? 685  LEU   A CG  1 
ATOM   1990 C  CD1 . LEU   A 1 244 ? 21.447  15.329  -16.721 1.00 20.61 ? 685  LEU   A CD1 1 
ATOM   1991 C  CD2 . LEU   A 1 244 ? 23.852  16.006  -16.435 1.00 21.92 ? 685  LEU   A CD2 1 
ATOM   1992 N  N   . VAL   A 1 245 ? 23.604  14.168  -21.423 1.00 18.68 ? 686  VAL   A N   1 
ATOM   1993 C  CA  . VAL   A 1 245 ? 24.002  13.016  -22.223 1.00 18.33 ? 686  VAL   A CA  1 
ATOM   1994 C  C   . VAL   A 1 245 ? 25.084  13.391  -23.221 1.00 17.79 ? 686  VAL   A C   1 
ATOM   1995 O  O   . VAL   A 1 245 ? 26.111  12.716  -23.333 1.00 20.42 ? 686  VAL   A O   1 
ATOM   1996 C  CB  . VAL   A 1 245 ? 22.785  12.398  -22.932 1.00 18.51 ? 686  VAL   A CB  1 
ATOM   1997 C  CG1 . VAL   A 1 245 ? 23.214  11.134  -23.653 1.00 19.38 ? 686  VAL   A CG1 1 
ATOM   1998 C  CG2 . VAL   A 1 245 ? 21.648  12.122  -21.954 1.00 19.45 ? 686  VAL   A CG2 1 
ATOM   1999 N  N   . MET   A 1 246 ? 24.863  14.453  -23.984 1.00 20.11 ? 687  MET   A N   1 
ATOM   2000 C  CA  . MET   A 1 246 ? 25.839  14.763  -25.022 1.00 16.79 ? 687  MET   A CA  1 
ATOM   2001 C  C   . MET   A 1 246 ? 27.161  15.319  -24.484 1.00 19.28 ? 687  MET   A C   1 
ATOM   2002 O  O   . MET   A 1 246 ? 28.218  14.920  -24.976 1.00 21.35 ? 687  MET   A O   1 
ATOM   2003 C  CB  . MET   A 1 246 ? 25.227  15.643  -26.128 1.00 19.80 ? 687  MET   A CB  1 
ATOM   2004 C  CG  . MET   A 1 246 ? 24.069  14.970  -26.935 1.00 18.90 ? 687  MET   A CG  1 
ATOM   2005 S  SD  . MET   A 1 246 ? 24.509  13.399  -27.663 1.00 19.98 ? 687  MET   A SD  1 
ATOM   2006 C  CE  . MET   A 1 246 ? 25.775  13.930  -28.806 1.00 23.96 ? 687  MET   A CE  1 
ATOM   2007 N  N   . PRO   A 1 247 ? 27.163  16.222  -23.497 1.00 20.39 ? 688  PRO   A N   1 
ATOM   2008 C  CA  . PRO   A 1 247 ? 28.463  16.656  -22.939 1.00 22.68 ? 688  PRO   A CA  1 
ATOM   2009 C  C   . PRO   A 1 247 ? 29.284  15.502  -22.380 1.00 24.20 ? 688  PRO   A C   1 
ATOM   2010 O  O   . PRO   A 1 247 ? 30.472  15.362  -22.707 1.00 23.71 ? 688  PRO   A O   1 
ATOM   2011 C  CB  . PRO   A 1 247 ? 28.067  17.681  -21.868 1.00 26.44 ? 688  PRO   A CB  1 
ATOM   2012 C  CG  . PRO   A 1 247 ? 26.719  18.155  -22.262 1.00 36.32 ? 688  PRO   A CG  1 
ATOM   2013 C  CD  . PRO   A 1 247 ? 26.046  17.010  -22.959 1.00 19.68 ? 688  PRO   A CD  1 
ATOM   2014 N  N   . ILE   A 1 248 ? 28.660  14.649  -21.566 1.00 20.24 ? 689  ILE   A N   1 
ATOM   2015 C  CA  . ILE   A 1 248 ? 29.363  13.502  -20.992 1.00 20.80 ? 689  ILE   A CA  1 
ATOM   2016 C  C   . ILE   A 1 248 ? 29.841  12.551  -22.089 1.00 18.77 ? 689  ILE   A C   1 
ATOM   2017 O  O   . ILE   A 1 248 ? 31.003  12.127  -22.102 1.00 21.91 ? 689  ILE   A O   1 
ATOM   2018 C  CB  . ILE   A 1 248 ? 28.477  12.797  -19.945 1.00 18.41 ? 689  ILE   A CB  1 
ATOM   2019 C  CG1 . ILE   A 1 248 ? 28.116  13.747  -18.797 1.00 22.42 ? 689  ILE   A CG1 1 
ATOM   2020 C  CG2 . ILE   A 1 248 ? 29.164  11.524  -19.437 1.00 21.62 ? 689  ILE   A CG2 1 
ATOM   2021 C  CD1 . ILE   A 1 248 ? 27.151  13.177  -17.754 1.00 19.45 ? 689  ILE   A CD1 1 
ATOM   2022 N  N   . ALA   A 1 249 ? 28.958  12.226  -23.051 1.00 19.50 ? 690  ALA   A N   1 
ATOM   2023 C  CA  . ALA   A 1 249 ? 29.333  11.288  -24.104 1.00 17.44 ? 690  ALA   A CA  1 
ATOM   2024 C  C   . ALA   A 1 249 ? 30.512  11.810  -24.912 1.00 19.39 ? 690  ALA   A C   1 
ATOM   2025 O  O   . ALA   A 1 249 ? 31.423  11.050  -25.261 1.00 21.28 ? 690  ALA   A O   1 
ATOM   2026 C  CB  . ALA   A 1 249 ? 28.141  11.000  -25.027 1.00 18.49 ? 690  ALA   A CB  1 
ATOM   2027 N  N   . ARG   A 1 250 ? 30.492  13.103  -25.242 1.00 22.22 ? 691  ARG   A N   1 
ATOM   2028 C  CA  . ARG   A 1 250 ? 31.570  13.678  -26.038 1.00 22.29 ? 691  ARG   A CA  1 
ATOM   2029 C  C   . ARG   A 1 250 ? 32.896  13.595  -25.299 1.00 26.90 ? 691  ARG   A C   1 
ATOM   2030 O  O   . ARG   A 1 250 ? 33.941  13.306  -25.901 1.00 26.00 ? 691  ARG   A O   1 
ATOM   2031 C  CB  . ARG   A 1 250 ? 31.239  15.130  -26.376 1.00 22.62 ? 691  ARG   A CB  1 
ATOM   2032 C  CG  . ARG   A 1 250 ? 30.380  15.247  -27.624 1.00 27.81 ? 691  ARG   A CG  1 
ATOM   2033 C  CD  . ARG   A 1 250 ? 30.243  16.681  -28.066 1.00 31.84 ? 691  ARG   A CD  1 
ATOM   2034 N  NE  . ARG   A 1 250 ? 29.506  17.474  -27.090 1.00 34.49 ? 691  ARG   A NE  1 
ATOM   2035 C  CZ  . ARG   A 1 250 ? 28.233  17.826  -27.231 1.00 33.35 ? 691  ARG   A CZ  1 
ATOM   2036 N  NH1 . ARG   A 1 250 ? 27.557  17.447  -28.310 1.00 33.87 ? 691  ARG   A NH1 1 
ATOM   2037 N  NH2 . ARG   A 1 250 ? 27.641  18.553  -26.292 1.00 29.28 ? 691  ARG   A NH2 1 
ATOM   2038 N  N   . GLU   A 1 251 ? 32.868  13.840  -23.992 1.00 23.66 ? 692  GLU   A N   1 
ATOM   2039 C  CA  . GLU   A 1 251 ? 34.088  13.733  -23.197 1.00 20.83 ? 692  GLU   A CA  1 
ATOM   2040 C  C   . GLU   A 1 251 ? 34.580  12.289  -23.124 1.00 26.11 ? 692  GLU   A C   1 
ATOM   2041 O  O   . GLU   A 1 251 ? 35.785  12.032  -23.203 1.00 28.20 ? 692  GLU   A O   1 
ATOM   2042 C  CB  . GLU   A 1 251 ? 33.838  14.313  -21.812 1.00 22.91 ? 692  GLU   A CB  1 
ATOM   2043 C  CG  . GLU   A 1 251 ? 35.126  14.607  -21.054 1.00 28.32 ? 692  GLU   A CG  1 
ATOM   2044 C  CD  . GLU   A 1 251 ? 34.917  15.375  -19.765 1.00 32.26 ? 692  GLU   A CD  1 
ATOM   2045 O  OE1 . GLU   A 1 251 ? 33.869  16.026  -19.591 1.00 27.33 ? 692  GLU   A OE1 1 
ATOM   2046 O  OE2 . GLU   A 1 251 ? 35.816  15.318  -18.902 1.00 34.67 ? 692  GLU   A OE2 1 
ATOM   2047 N  N   . PHE   A 1 252 ? 33.658  11.328  -22.986 1.00 21.33 ? 693  PHE   A N   1 
ATOM   2048 C  CA  . PHE   A 1 252 ? 34.028  9.916   -23.006 1.00 19.50 ? 693  PHE   A CA  1 
ATOM   2049 C  C   . PHE   A 1 252 ? 34.594  9.498   -24.361 1.00 23.07 ? 693  PHE   A C   1 
ATOM   2050 O  O   . PHE   A 1 252 ? 35.476  8.635   -24.420 1.00 23.12 ? 693  PHE   A O   1 
ATOM   2051 C  CB  . PHE   A 1 252 ? 32.796  9.085   -22.595 1.00 21.34 ? 693  PHE   A CB  1 
ATOM   2052 C  CG  . PHE   A 1 252 ? 33.002  7.589   -22.583 1.00 18.59 ? 693  PHE   A CG  1 
ATOM   2053 C  CD1 . PHE   A 1 252 ? 33.786  6.973   -21.610 1.00 21.06 ? 693  PHE   A CD1 1 
ATOM   2054 C  CD2 . PHE   A 1 252 ? 32.347  6.779   -23.502 1.00 18.28 ? 693  PHE   A CD2 1 
ATOM   2055 C  CE1 . PHE   A 1 252 ? 33.945  5.587   -21.599 1.00 20.31 ? 693  PHE   A CE1 1 
ATOM   2056 C  CE2 . PHE   A 1 252 ? 32.504  5.400   -23.493 1.00 19.87 ? 693  PHE   A CE2 1 
ATOM   2057 C  CZ  . PHE   A 1 252 ? 33.291  4.804   -22.546 1.00 17.29 ? 693  PHE   A CZ  1 
ATOM   2058 N  N   . ALA   A 1 253 ? 34.118  10.112  -25.462 1.00 19.41 ? 694  ALA   A N   1 
ATOM   2059 C  CA  . ALA   A 1 253 ? 34.559  9.775   -26.813 1.00 25.12 ? 694  ALA   A CA  1 
ATOM   2060 C  C   . ALA   A 1 253 ? 34.401  8.281   -27.084 1.00 22.57 ? 694  ALA   A C   1 
ATOM   2061 O  O   . ALA   A 1 253 ? 35.399  7.577   -27.292 1.00 22.43 ? 694  ALA   A O   1 
ATOM   2062 C  CB  . ALA   A 1 253 ? 36.006  10.234  -27.063 1.00 22.02 ? 694  ALA   A CB  1 
ATOM   2063 N  N   . PRO   A 1 254 ? 33.170  7.756   -27.098 1.00 18.16 ? 695  PRO   A N   1 
ATOM   2064 C  CA  . PRO   A 1 254 ? 32.997  6.323   -27.350 1.00 19.52 ? 695  PRO   A CA  1 
ATOM   2065 C  C   . PRO   A 1 254 ? 33.470  5.950   -28.742 1.00 19.71 ? 695  PRO   A C   1 
ATOM   2066 O  O   . PRO   A 1 254 ? 33.491  6.773   -29.661 1.00 19.36 ? 695  PRO   A O   1 
ATOM   2067 C  CB  . PRO   A 1 254 ? 31.479  6.123   -27.228 1.00 18.56 ? 695  PRO   A CB  1 
ATOM   2068 C  CG  . PRO   A 1 254 ? 30.894  7.479   -27.533 1.00 20.02 ? 695  PRO   A CG  1 
ATOM   2069 C  CD  . PRO   A 1 254 ? 31.884  8.455   -26.943 1.00 22.64 ? 695  PRO   A CD  1 
ATOM   2070 N  N   . GLU   A 1 255 ? 33.871  4.693   -28.884 1.00 19.35 ? 696  GLU   A N   1 
ATOM   2071 C  CA  . GLU   A 1 255 ? 34.205  4.126   -30.179 1.00 22.43 ? 696  GLU   A CA  1 
ATOM   2072 C  C   . GLU   A 1 255 ? 33.052  3.323   -30.765 1.00 19.74 ? 696  GLU   A C   1 
ATOM   2073 O  O   . GLU   A 1 255 ? 33.108  2.947   -31.937 1.00 18.03 ? 696  GLU   A O   1 
ATOM   2074 C  CB  . GLU   A 1 255 ? 35.481  3.276   -30.076 1.00 20.41 ? 696  GLU   A CB  1 
ATOM   2075 C  CG  . GLU   A 1 255 ? 36.667  4.103   -29.548 1.00 25.99 ? 696  GLU   A CG  1 
ATOM   2076 C  CD  . GLU   A 1 255 ? 37.850  3.260   -29.115 1.00 38.47 ? 696  GLU   A CD  1 
ATOM   2077 O  OE1 . GLU   A 1 255 ? 37.798  2.678   -28.013 1.00 23.74 ? 696  GLU   A OE1 1 
ATOM   2078 O  OE2 . GLU   A 1 255 ? 38.844  3.195   -29.869 1.00 44.72 ? 696  GLU   A OE2 1 
ATOM   2079 N  N   . LEU   A 1 256 ? 32.029  3.052   -29.959 1.00 15.65 ? 697  LEU   A N   1 
ATOM   2080 C  CA  . LEU   A 1 256 ? 30.808  2.383   -30.381 1.00 17.09 ? 697  LEU   A CA  1 
ATOM   2081 C  C   . LEU   A 1 256 ? 29.702  2.862   -29.455 1.00 13.76 ? 697  LEU   A C   1 
ATOM   2082 O  O   . LEU   A 1 256 ? 29.909  3.004   -28.243 1.00 15.58 ? 697  LEU   A O   1 
ATOM   2083 C  CB  . LEU   A 1 256 ? 30.944  0.853   -30.283 1.00 15.50 ? 697  LEU   A CB  1 
ATOM   2084 C  CG  . LEU   A 1 256 ? 29.710  -0.019  -30.575 1.00 15.29 ? 697  LEU   A CG  1 
ATOM   2085 C  CD1 . LEU   A 1 256 ? 29.238  0.167   -32.008 1.00 18.43 ? 697  LEU   A CD1 1 
ATOM   2086 C  CD2 . LEU   A 1 256 ? 29.994  -1.473  -30.323 1.00 16.39 ? 697  LEU   A CD2 1 
ATOM   2087 N  N   . VAL   A 1 257 ? 28.530  3.127   -30.028 1.00 15.40 ? 698  VAL   A N   1 
ATOM   2088 C  CA  . VAL   A 1 257 ? 27.355  3.532   -29.260 1.00 14.86 ? 698  VAL   A CA  1 
ATOM   2089 C  C   . VAL   A 1 257 ? 26.282  2.462   -29.419 1.00 13.25 ? 698  VAL   A C   1 
ATOM   2090 O  O   . VAL   A 1 257 ? 25.903  2.108   -30.549 1.00 14.31 ? 698  VAL   A O   1 
ATOM   2091 C  CB  . VAL   A 1 257 ? 26.804  4.899   -29.714 1.00 15.63 ? 698  VAL   A CB  1 
ATOM   2092 C  CG1 . VAL   A 1 257 ? 25.535  5.251   -28.957 1.00 17.26 ? 698  VAL   A CG1 1 
ATOM   2093 C  CG2 . VAL   A 1 257 ? 27.870  5.994   -29.536 1.00 17.01 ? 698  VAL   A CG2 1 
ATOM   2094 N  N   . LEU   A 1 258 ? 25.791  1.951   -28.291 1.00 13.16 ? 699  LEU   A N   1 
ATOM   2095 C  CA  . LEU   A 1 258 ? 24.634  1.077   -28.298 1.00 13.65 ? 699  LEU   A CA  1 
ATOM   2096 C  C   . LEU   A 1 258 ? 23.486  1.839   -27.668 1.00 14.29 ? 699  LEU   A C   1 
ATOM   2097 O  O   . LEU   A 1 258 ? 23.658  2.511   -26.643 1.00 13.53 ? 699  LEU   A O   1 
ATOM   2098 C  CB  . LEU   A 1 258 ? 24.916  -0.169  -27.467 1.00 15.06 ? 699  LEU   A CB  1 
ATOM   2099 C  CG  . LEU   A 1 258 ? 26.157  -0.986  -27.820 1.00 15.35 ? 699  LEU   A CG  1 
ATOM   2100 C  CD1 . LEU   A 1 258 ? 26.290  -2.207  -26.918 1.00 14.63 ? 699  LEU   A CD1 1 
ATOM   2101 C  CD2 . LEU   A 1 258 ? 26.134  -1.407  -29.299 1.00 15.31 ? 699  LEU   A CD2 1 
ATOM   2102 N  N   . VAL   A 1 259 ? 22.313  1.758   -28.284 1.00 11.90 ? 700  VAL   A N   1 
ATOM   2103 C  CA  . VAL   A 1 259 ? 21.119  2.344   -27.683 1.00 14.52 ? 700  VAL   A CA  1 
ATOM   2104 C  C   . VAL   A 1 259 ? 20.247  1.217   -27.158 1.00 13.47 ? 700  VAL   A C   1 
ATOM   2105 O  O   . VAL   A 1 259 ? 19.829  0.351   -27.935 1.00 12.07 ? 700  VAL   A O   1 
ATOM   2106 C  CB  . VAL   A 1 259 ? 20.335  3.249   -28.648 1.00 13.71 ? 700  VAL   A CB  1 
ATOM   2107 C  CG1 . VAL   A 1 259 ? 19.251  3.996   -27.871 1.00 14.56 ? 700  VAL   A CG1 1 
ATOM   2108 C  CG2 . VAL   A 1 259 ? 21.262  4.264   -29.313 1.00 16.19 ? 700  VAL   A CG2 1 
ATOM   2109 N  N   . SER   A 1 260 ? 20.013  1.200   -25.846 1.00 12.87 ? 701  SER   A N   1 
ATOM   2110 C  CA  . SER   A 1 260 ? 18.960  0.353   -25.294 1.00 12.45 ? 701  SER   A CA  1 
ATOM   2111 C  C   . SER   A 1 260 ? 17.673  1.116   -25.562 1.00 12.39 ? 701  SER   A C   1 
ATOM   2112 O  O   . SER   A 1 260 ? 17.236  1.959   -24.772 1.00 12.44 ? 701  SER   A O   1 
ATOM   2113 C  CB  . SER   A 1 260 ? 19.198  0.104   -23.810 1.00 13.81 ? 701  SER   A CB  1 
ATOM   2114 O  OG  . SER   A 1 260 ? 19.952  -1.091  -23.625 1.00 14.89 ? 701  SER   A OG  1 
ATOM   2115 N  N   . ALA   A 1 261 ? 17.088  0.819   -26.724 1.00 11.09 ? 702  ALA   A N   1 
ATOM   2116 C  CA  . ALA   A 1 261 ? 16.012  1.628   -27.286 1.00 12.01 ? 702  ALA   A CA  1 
ATOM   2117 C  C   . ALA   A 1 261 ? 14.673  0.953   -26.998 1.00 12.36 ? 702  ALA   A C   1 
ATOM   2118 O  O   . ALA   A 1 261 ? 14.061  0.313   -27.859 1.00 12.04 ? 702  ALA   A O   1 
ATOM   2119 C  CB  . ALA   A 1 261 ? 16.258  1.834   -28.787 1.00 13.59 ? 702  ALA   A CB  1 
ATOM   2120 N  N   . GLY   A 1 262 ? 14.230  1.078   -25.752 1.00 14.37 ? 703  GLY   A N   1 
ATOM   2121 C  CA  . GLY   A 1 262 ? 12.832  0.846   -25.479 1.00 13.22 ? 703  GLY   A CA  1 
ATOM   2122 C  C   . GLY   A 1 262 ? 12.004  2.016   -25.968 1.00 13.19 ? 703  GLY   A C   1 
ATOM   2123 O  O   . GLY   A 1 262 ? 12.479  3.153   -26.042 1.00 15.86 ? 703  GLY   A O   1 
ATOM   2124 N  N   . PHE   A 1 263 ? 10.759  1.729   -26.343 1.00 10.64 ? 704  PHE   A N   1 
ATOM   2125 C  CA  . PHE   A 1 263 ? 9.842   2.775   -26.764 1.00 12.50 ? 704  PHE   A CA  1 
ATOM   2126 C  C   . PHE   A 1 263 ? 8.645   2.847   -25.824 1.00 15.15 ? 704  PHE   A C   1 
ATOM   2127 O  O   . PHE   A 1 263 ? 7.560   3.270   -26.224 1.00 14.89 ? 704  PHE   A O   1 
ATOM   2128 C  CB  . PHE   A 1 263 ? 9.502   2.645   -28.250 1.00 14.49 ? 704  PHE   A CB  1 
ATOM   2129 C  CG  . PHE   A 1 263 ? 10.718  2.790   -29.124 1.00 10.88 ? 704  PHE   A CG  1 
ATOM   2130 C  CD1 . PHE   A 1 263 ? 11.191  4.052   -29.428 1.00 13.82 ? 704  PHE   A CD1 1 
ATOM   2131 C  CD2 . PHE   A 1 263 ? 11.414  1.677   -29.598 1.00 12.33 ? 704  PHE   A CD2 1 
ATOM   2132 C  CE1 . PHE   A 1 263 ? 12.359  4.213   -30.218 1.00 13.46 ? 704  PHE   A CE1 1 
ATOM   2133 C  CE2 . PHE   A 1 263 ? 12.577  1.828   -30.391 1.00 12.87 ? 704  PHE   A CE2 1 
ATOM   2134 C  CZ  . PHE   A 1 263 ? 13.054  3.090   -30.671 1.00 12.58 ? 704  PHE   A CZ  1 
ATOM   2135 N  N   . ASP   A 1 264 ? 8.862   2.569   -24.549 1.00 13.65 ? 705  ASP   A N   1 
ATOM   2136 C  CA  . ASP   A 1 264 ? 7.779   2.630   -23.533 1.00 15.11 ? 705  ASP   A CA  1 
ATOM   2137 C  C   . ASP   A 1 264 ? 7.634   4.047   -22.961 1.00 15.10 ? 705  ASP   A C   1 
ATOM   2138 O  O   . ASP   A 1 264 ? 6.703   4.238   -22.195 1.00 16.12 ? 705  ASP   A O   1 
ATOM   2139 C  CB  . ASP   A 1 264 ? 7.923   1.530   -22.498 1.00 18.47 ? 705  ASP   A CB  1 
ATOM   2140 C  CG  . ASP   A 1 264 ? 9.325   1.132   -22.085 1.00 12.88 ? 705  ASP   A CG  1 
ATOM   2141 O  OD1 . ASP   A 1 264 ? 10.247  1.910   -22.333 1.00 17.32 ? 705  ASP   A OD1 1 
ATOM   2142 O  OD2 . ASP   A 1 264 ? 9.448   0.057   -21.491 1.00 20.27 ? 705  ASP   A OD2 1 
ATOM   2143 N  N   . ALA   A 1 265 ? 8.535   4.963   -23.299 1.00 13.05 ? 706  ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 265 ? 8.336   6.378   -22.906 1.00 13.74 ? 706  ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 265 ? 7.509   7.085   -23.989 1.00 15.60 ? 706  ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 265 ? 7.295   8.285   -23.848 1.00 16.85 ? 706  ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 265 ? 9.659   7.076   -22.671 1.00 16.63 ? 706  ALA   A CB  1 
ATOM   2148 N  N   . ALA   A 1 266 ? 7.039   6.334   -24.992 1.00 16.13 ? 707  ALA   A N   1 
ATOM   2149 C  CA  . ALA   A 1 266 ? 6.366   6.970   -26.113 1.00 14.33 ? 707  ALA   A CA  1 
ATOM   2150 C  C   . ALA   A 1 266 ? 4.935   7.352   -25.754 1.00 15.15 ? 707  ALA   A C   1 
ATOM   2151 O  O   . ALA   A 1 266 ? 4.262   6.681   -24.957 1.00 15.75 ? 707  ALA   A O   1 
ATOM   2152 C  CB  . ALA   A 1 266 ? 6.295   6.005   -27.290 1.00 14.10 ? 707  ALA   A CB  1 
ATOM   2153 N  N   A ARG   A 1 267 ? 4.463   8.428   -26.381 0.33 15.79 ? 708  ARG   A N   1 
ATOM   2154 N  N   B ARG   A 1 267 ? 4.468   8.448   -26.359 0.67 16.89 ? 708  ARG   A N   1 
ATOM   2155 C  CA  A ARG   A 1 267 ? 3.050   8.775   -26.316 0.33 15.69 ? 708  ARG   A CA  1 
ATOM   2156 C  CA  B ARG   A 1 267 ? 3.044   8.766   -26.326 0.67 15.06 ? 708  ARG   A CA  1 
ATOM   2157 C  C   A ARG   A 1 267 ? 2.217   7.587   -26.780 0.33 15.16 ? 708  ARG   A C   1 
ATOM   2158 C  C   B ARG   A 1 267 ? 2.257   7.540   -26.747 0.67 16.63 ? 708  ARG   A C   1 
ATOM   2159 O  O   A ARG   A 1 267 ? 2.485   7.002   -27.832 0.33 17.68 ? 708  ARG   A O   1 
ATOM   2160 O  O   B ARG   A 1 267 ? 2.592   6.891   -27.738 0.67 15.09 ? 708  ARG   A O   1 
ATOM   2161 C  CB  A ARG   A 1 267 ? 2.805   9.991   -27.212 0.33 17.94 ? 708  ARG   A CB  1 
ATOM   2162 C  CB  B ARG   A 1 267 ? 2.765   9.911   -27.303 0.67 18.42 ? 708  ARG   A CB  1 
ATOM   2163 C  CG  A ARG   A 1 267 ? 1.414   10.100  -27.798 0.33 15.10 ? 708  ARG   A CG  1 
ATOM   2164 C  CG  B ARG   A 1 267 ? 1.471   10.659  -27.017 0.67 20.22 ? 708  ARG   A CG  1 
ATOM   2165 C  CD  A ARG   A 1 267 ? 1.367   11.153  -28.909 0.33 23.91 ? 708  ARG   A CD  1 
ATOM   2166 C  CD  B ARG   A 1 267 ? 0.957   11.429  -28.219 0.67 20.72 ? 708  ARG   A CD  1 
ATOM   2167 N  NE  A ARG   A 1 267 ? 1.840   10.642  -30.196 0.33 30.51 ? 708  ARG   A NE  1 
ATOM   2168 N  NE  B ARG   A 1 267 ? 2.001   12.041  -29.039 0.67 41.46 ? 708  ARG   A NE  1 
ATOM   2169 C  CZ  A ARG   A 1 267 ? 2.344   11.403  -31.165 0.33 14.89 ? 708  ARG   A CZ  1 
ATOM   2170 C  CZ  B ARG   A 1 267 ? 2.315   11.650  -30.274 0.67 45.52 ? 708  ARG   A CZ  1 
ATOM   2171 N  NH1 A ARG   A 1 267 ? 2.450   12.716  -30.993 0.33 18.59 ? 708  ARG   A NH1 1 
ATOM   2172 N  NH1 B ARG   A 1 267 ? 1.683   10.630  -30.843 0.67 39.36 ? 708  ARG   A NH1 1 
ATOM   2173 N  NH2 A ARG   A 1 267 ? 2.746   10.853  -32.301 0.33 23.77 ? 708  ARG   A NH2 1 
ATOM   2174 N  NH2 B ARG   A 1 267 ? 3.268   12.278  -30.946 0.67 39.07 ? 708  ARG   A NH2 1 
ATOM   2175 N  N   . GLY   A 1 268 ? 1.226   7.209   -25.970 1.00 14.62 ? 709  GLY   A N   1 
ATOM   2176 C  CA  . GLY   A 1 268 ? 0.377   6.071   -26.238 1.00 16.53 ? 709  GLY   A CA  1 
ATOM   2177 C  C   . GLY   A 1 268 ? 0.749   4.788   -25.516 1.00 13.23 ? 709  GLY   A C   1 
ATOM   2178 O  O   . GLY   A 1 268 ? -0.044  3.842   -25.540 1.00 15.64 ? 709  GLY   A O   1 
ATOM   2179 N  N   . ASP   A 1 269 ? 1.930   4.706   -24.906 1.00 14.14 ? 710  ASP   A N   1 
ATOM   2180 C  CA  . ASP   A 1 269 ? 2.306   3.446   -24.275 1.00 14.49 ? 710  ASP   A CA  1 
ATOM   2181 C  C   . ASP   A 1 269 ? 1.361   3.125   -23.121 1.00 15.48 ? 710  ASP   A C   1 
ATOM   2182 O  O   . ASP   A 1 269 ? 1.040   4.009   -22.323 1.00 17.50 ? 710  ASP   A O   1 
ATOM   2183 C  CB  . ASP   A 1 269 ? 3.721   3.519   -23.714 1.00 15.87 ? 710  ASP   A CB  1 
ATOM   2184 C  CG  . ASP   A 1 269 ? 4.259   2.147   -23.337 1.00 14.59 ? 710  ASP   A CG  1 
ATOM   2185 O  OD1 . ASP   A 1 269 ? 4.758   1.438   -24.244 1.00 14.27 ? 710  ASP   A OD1 1 
ATOM   2186 O  OD2 . ASP   A 1 269 ? 4.159   1.757   -22.152 1.00 14.46 ? 710  ASP   A OD2 1 
ATOM   2187 N  N   . PRO   A 1 270 ? 0.959   1.863   -22.953 1.00 12.99 ? 711  PRO   A N   1 
ATOM   2188 C  CA  . PRO   A 1 270 ? 0.008   1.540   -21.875 1.00 14.90 ? 711  PRO   A CA  1 
ATOM   2189 C  C   . PRO   A 1 270 ? 0.616   1.482   -20.490 1.00 14.37 ? 711  PRO   A C   1 
ATOM   2190 O  O   . PRO   A 1 270 ? -0.145  1.441   -19.504 1.00 17.84 ? 711  PRO   A O   1 
ATOM   2191 C  CB  . PRO   A 1 270 ? -0.545  0.168   -22.290 1.00 16.45 ? 711  PRO   A CB  1 
ATOM   2192 C  CG  . PRO   A 1 270 ? 0.586   -0.439  -23.118 1.00 18.90 ? 711  PRO   A CG  1 
ATOM   2193 C  CD  . PRO   A 1 270 ? 1.172   0.725   -23.867 1.00 14.28 ? 711  PRO   A CD  1 
ATOM   2194 N  N   . LEU   A 1 271 ? 1.945   1.481   -20.362 1.00 15.92 ? 712  LEU   A N   1 
ATOM   2195 C  CA  . LEU   A 1 271 ? 2.626   1.350   -19.076 1.00 16.10 ? 712  LEU   A CA  1 
ATOM   2196 C  C   . LEU   A 1 271 ? 3.474   2.556   -18.705 1.00 17.03 ? 712  LEU   A C   1 
ATOM   2197 O  O   . LEU   A 1 271 ? 3.554   2.913   -17.531 1.00 18.71 ? 712  LEU   A O   1 
ATOM   2198 C  CB  . LEU   A 1 271 ? 3.518   0.085   -19.092 1.00 17.59 ? 712  LEU   A CB  1 
ATOM   2199 C  CG  . LEU   A 1 271 ? 2.770   -1.245  -19.276 1.00 16.37 ? 712  LEU   A CG  1 
ATOM   2200 C  CD1 . LEU   A 1 271 ? 3.749   -2.410  -19.436 1.00 17.69 ? 712  LEU   A CD1 1 
ATOM   2201 C  CD2 . LEU   A 1 271 ? 1.849   -1.514  -18.091 1.00 19.04 ? 712  LEU   A CD2 1 
ATOM   2202 N  N   . GLY   A 1 272 ? 4.133   3.193   -19.674 1.00 15.83 ? 713  GLY   A N   1 
ATOM   2203 C  CA  . GLY   A 1 272 ? 5.132   4.187   -19.333 1.00 16.17 ? 713  GLY   A CA  1 
ATOM   2204 C  C   . GLY   A 1 272 ? 4.565   5.484   -18.787 1.00 20.46 ? 713  GLY   A C   1 
ATOM   2205 O  O   . GLY   A 1 272 ? 5.191   6.133   -17.948 1.00 17.76 ? 713  GLY   A O   1 
ATOM   2206 N  N   . GLY   A 1 273 ? 3.400   5.898   -19.276 1.00 18.54 ? 714  GLY   A N   1 
ATOM   2207 C  CA  . GLY   A 1 273 ? 2.812   7.154   -18.841 1.00 23.83 ? 714  GLY   A CA  1 
ATOM   2208 C  C   . GLY   A 1 273 ? 3.512   8.422   -19.290 1.00 22.12 ? 714  GLY   A C   1 
ATOM   2209 O  O   . GLY   A 1 273 ? 3.264   9.483   -18.714 1.00 22.37 ? 714  GLY   A O   1 
ATOM   2210 N  N   . PHE   A 1 274 ? 4.361   8.359   -20.318 1.00 17.11 ? 715  PHE   A N   1 
ATOM   2211 C  CA  . PHE   A 1 274 ? 5.129   9.494   -20.813 1.00 20.14 ? 715  PHE   A CA  1 
ATOM   2212 C  C   . PHE   A 1 274 ? 4.643   9.835   -22.225 1.00 17.26 ? 715  PHE   A C   1 
ATOM   2213 O  O   . PHE   A 1 274 ? 3.709   9.211   -22.748 1.00 19.03 ? 715  PHE   A O   1 
ATOM   2214 C  CB  . PHE   A 1 274 ? 6.635   9.181   -20.793 1.00 16.51 ? 715  PHE   A CB  1 
ATOM   2215 C  CG  . PHE   A 1 274 ? 7.335   9.437   -19.450 1.00 17.02 ? 715  PHE   A CG  1 
ATOM   2216 C  CD1 . PHE   A 1 274 ? 6.633   9.723   -18.285 1.00 19.56 ? 715  PHE   A CD1 1 
ATOM   2217 C  CD2 . PHE   A 1 274 ? 8.722   9.391   -19.375 1.00 18.67 ? 715  PHE   A CD2 1 
ATOM   2218 C  CE1 . PHE   A 1 274 ? 7.310   9.961   -17.072 1.00 18.44 ? 715  PHE   A CE1 1 
ATOM   2219 C  CE2 . PHE   A 1 274 ? 9.399   9.619   -18.173 1.00 17.88 ? 715  PHE   A CE2 1 
ATOM   2220 C  CZ  . PHE   A 1 274 ? 8.682   9.909   -17.021 1.00 20.28 ? 715  PHE   A CZ  1 
ATOM   2221 N  N   . GLN   A 1 275 ? 5.297   10.809  -22.864 1.00 16.75 ? 716  GLN   A N   1 
ATOM   2222 C  CA  . GLN   A 1 275 ? 4.766   11.338  -24.121 1.00 16.67 ? 716  GLN   A CA  1 
ATOM   2223 C  C   . GLN   A 1 275 ? 5.856   11.745  -25.105 1.00 21.66 ? 716  GLN   A C   1 
ATOM   2224 O  O   . GLN   A 1 275 ? 5.693   12.700  -25.876 1.00 19.93 ? 716  GLN   A O   1 
ATOM   2225 C  CB  . GLN   A 1 275 ? 3.758   12.462  -23.886 1.00 23.49 ? 716  GLN   A CB  1 
ATOM   2226 C  CG  . GLN   A 1 275 ? 4.279   13.665  -23.130 1.00 24.03 ? 716  GLN   A CG  1 
ATOM   2227 C  CD  . GLN   A 1 275 ? 3.139   14.618  -22.738 1.00 38.49 ? 716  GLN   A CD  1 
ATOM   2228 O  OE1 . GLN   A 1 275 ? 2.172   14.772  -23.481 1.00 36.88 ? 716  GLN   A OE1 1 
ATOM   2229 N  NE2 . GLN   A 1 275 ? 3.256   15.258  -21.578 1.00 31.39 ? 716  GLN   A NE2 1 
ATOM   2230 N  N   . VAL   A 1 276 ? 6.972   11.011  -25.131 1.00 15.29 ? 717  VAL   A N   1 
ATOM   2231 C  CA  . VAL   A 1 276 ? 7.968   11.236  -26.172 1.00 14.50 ? 717  VAL   A CA  1 
ATOM   2232 C  C   . VAL   A 1 276 ? 7.353   10.910  -27.532 1.00 15.27 ? 717  VAL   A C   1 
ATOM   2233 O  O   . VAL   A 1 276 ? 6.681   9.884   -27.704 1.00 14.23 ? 717  VAL   A O   1 
ATOM   2234 C  CB  . VAL   A 1 276 ? 9.234   10.400  -25.905 1.00 15.65 ? 717  VAL   A CB  1 
ATOM   2235 C  CG1 . VAL   A 1 276 ? 10.279  10.673  -26.964 1.00 17.80 ? 717  VAL   A CG1 1 
ATOM   2236 C  CG2 . VAL   A 1 276 ? 9.804   10.692  -24.519 1.00 14.90 ? 717  VAL   A CG2 1 
ATOM   2237 N  N   . THR   A 1 277 ? 7.594   11.787  -28.518 1.00 16.79 ? 718  THR   A N   1 
ATOM   2238 C  CA  . THR   A 1 277 ? 6.972   11.569  -29.818 1.00 17.94 ? 718  THR   A CA  1 
ATOM   2239 C  C   . THR   A 1 277 ? 7.947   10.856  -30.746 1.00 17.38 ? 718  THR   A C   1 
ATOM   2240 O  O   . THR   A 1 277 ? 9.147   10.780  -30.457 1.00 16.45 ? 718  THR   A O   1 
ATOM   2241 C  CB  . THR   A 1 277 ? 6.568   12.907  -30.446 1.00 18.39 ? 718  THR   A CB  1 
ATOM   2242 O  OG1 . THR   A 1 277 ? 7.740   13.617  -30.857 1.00 18.71 ? 718  THR   A OG1 1 
ATOM   2243 C  CG2 . THR   A 1 277 ? 5.740   13.753  -29.473 1.00 20.39 ? 718  THR   A CG2 1 
ATOM   2244 N  N   . PRO   A 1 278 ? 7.473   10.335  -31.890 1.00 15.22 ? 719  PRO   A N   1 
ATOM   2245 C  CA  . PRO   A 1 278 ? 8.420   9.756   -32.853 1.00 15.22 ? 719  PRO   A CA  1 
ATOM   2246 C  C   . PRO   A 1 278 ? 9.471   10.747  -33.311 1.00 17.49 ? 719  PRO   A C   1 
ATOM   2247 O  O   . PRO   A 1 278 ? 10.642  10.382  -33.515 1.00 16.96 ? 719  PRO   A O   1 
ATOM   2248 C  CB  . PRO   A 1 278 ? 7.507   9.295   -34.004 1.00 17.55 ? 719  PRO   A CB  1 
ATOM   2249 C  CG  . PRO   A 1 278 ? 6.200   9.036   -33.332 1.00 17.46 ? 719  PRO   A CG  1 
ATOM   2250 C  CD  . PRO   A 1 278 ? 6.067   10.088  -32.284 1.00 17.28 ? 719  PRO   A CD  1 
ATOM   2251 N  N   . GLU   A 1 279 ? 9.069   12.002  -33.502 1.00 15.24 ? 720  GLU   A N   1 
ATOM   2252 C  CA  . GLU   A 1 279 ? 10.022  13.029  -33.890 1.00 15.97 ? 720  GLU   A CA  1 
ATOM   2253 C  C   . GLU   A 1 279 ? 11.024  13.275  -32.778 1.00 17.47 ? 720  GLU   A C   1 
ATOM   2254 O  O   . GLU   A 1 279 ? 12.204  13.527  -33.046 1.00 17.95 ? 720  GLU   A O   1 
ATOM   2255 C  CB  . GLU   A 1 279 ? 9.264   14.314  -34.238 1.00 18.77 ? 720  GLU   A CB  1 
ATOM   2256 C  CG  . GLU   A 1 279 ? 8.346   14.175  -35.462 1.00 21.16 ? 720  GLU   A CG  1 
ATOM   2257 C  CD  . GLU   A 1 279 ? 7.007   13.515  -35.169 1.00 30.88 ? 720  GLU   A CD  1 
ATOM   2258 O  OE1 . GLU   A 1 279 ? 6.613   13.434  -33.987 1.00 21.46 ? 720  GLU   A OE1 1 
ATOM   2259 O  OE2 . GLU   A 1 279 ? 6.347   13.074  -36.135 1.00 30.68 ? 720  GLU   A OE2 1 
ATOM   2260 N  N   . GLY   A 1 280 ? 10.580  13.156  -31.528 1.00 17.48 ? 721  GLY   A N   1 
ATOM   2261 C  CA  . GLY   A 1 280 ? 11.511  13.249  -30.418 1.00 16.33 ? 721  GLY   A CA  1 
ATOM   2262 C  C   . GLY   A 1 280 ? 12.571  12.163  -30.463 1.00 16.95 ? 721  GLY   A C   1 
ATOM   2263 O  O   . GLY   A 1 280 ? 13.772  12.439  -30.354 1.00 17.62 ? 721  GLY   A O   1 
ATOM   2264 N  N   . TYR   A 1 281 ? 12.143  10.906  -30.640 1.00 16.11 ? 722  TYR   A N   1 
ATOM   2265 C  CA  . TYR   A 1 281 ? 13.117  9.824   -30.776 1.00 14.34 ? 722  TYR   A CA  1 
ATOM   2266 C  C   . TYR   A 1 281 ? 14.043  10.056  -31.965 1.00 16.01 ? 722  TYR   A C   1 
ATOM   2267 O  O   . TYR   A 1 281 ? 15.250  9.766   -31.890 1.00 15.93 ? 722  TYR   A O   1 
ATOM   2268 C  CB  . TYR   A 1 281 ? 12.412  8.474   -30.905 1.00 14.12 ? 722  TYR   A CB  1 
ATOM   2269 C  CG  . TYR   A 1 281 ? 11.752  7.979   -29.629 1.00 13.76 ? 722  TYR   A CG  1 
ATOM   2270 C  CD1 . TYR   A 1 281 ? 12.518  7.533   -28.550 1.00 14.63 ? 722  TYR   A CD1 1 
ATOM   2271 C  CD2 . TYR   A 1 281 ? 10.361  7.916   -29.519 1.00 13.38 ? 722  TYR   A CD2 1 
ATOM   2272 C  CE1 . TYR   A 1 281 ? 11.938  7.080   -27.395 1.00 14.39 ? 722  TYR   A CE1 1 
ATOM   2273 C  CE2 . TYR   A 1 281 ? 9.763   7.448   -28.354 1.00 14.17 ? 722  TYR   A CE2 1 
ATOM   2274 C  CZ  . TYR   A 1 281 ? 10.550  7.039   -27.300 1.00 13.19 ? 722  TYR   A CZ  1 
ATOM   2275 O  OH  . TYR   A 1 281 ? 9.944   6.562   -26.171 1.00 14.12 ? 722  TYR   A OH  1 
ATOM   2276 N  N   . ALA   A 1 282 ? 13.506  10.585  -33.072 1.00 14.68 ? 723  ALA   A N   1 
ATOM   2277 C  CA  . ALA   A 1 282 ? 14.358  10.896  -34.226 1.00 15.03 ? 723  ALA   A CA  1 
ATOM   2278 C  C   . ALA   A 1 282 ? 15.443  11.912  -33.861 1.00 13.01 ? 723  ALA   A C   1 
ATOM   2279 O  O   . ALA   A 1 282 ? 16.615  11.746  -34.224 1.00 15.14 ? 723  ALA   A O   1 
ATOM   2280 C  CB  . ALA   A 1 282 ? 13.510  11.402  -35.398 1.00 15.17 ? 723  ALA   A CB  1 
ATOM   2281 N  N   . HIS   A 1 283 ? 15.081  12.941  -33.094 1.00 17.01 ? 724  HIS   A N   1 
ATOM   2282 C  CA  . HIS   A 1 283 ? 16.092  13.915  -32.686 1.00 16.51 ? 724  HIS   A CA  1 
ATOM   2283 C  C   . HIS   A 1 283 ? 17.138  13.295  -31.763 1.00 23.66 ? 724  HIS   A C   1 
ATOM   2284 O  O   . HIS   A 1 283 ? 18.337  13.590  -31.889 1.00 19.55 ? 724  HIS   A O   1 
ATOM   2285 C  CB  . HIS   A 1 283 ? 15.437  15.132  -32.051 1.00 22.29 ? 724  HIS   A CB  1 
ATOM   2286 C  CG  . HIS   A 1 283 ? 14.986  16.137  -33.061 1.00 31.03 ? 724  HIS   A CG  1 
ATOM   2287 N  ND1 . HIS   A 1 283 ? 15.749  17.226  -33.419 1.00 34.83 ? 724  HIS   A ND1 1 
ATOM   2288 C  CD2 . HIS   A 1 283 ? 13.871  16.188  -33.829 1.00 33.06 ? 724  HIS   A CD2 1 
ATOM   2289 C  CE1 . HIS   A 1 283 ? 15.114  17.919  -34.348 1.00 35.19 ? 724  HIS   A CE1 1 
ATOM   2290 N  NE2 . HIS   A 1 283 ? 13.971  17.312  -34.613 1.00 25.20 ? 724  HIS   A NE2 1 
ATOM   2291 N  N   . LEU   A 1 284 ? 16.712  12.437  -30.830 1.00 18.00 ? 725  LEU   A N   1 
ATOM   2292 C  CA  . LEU   A 1 284 ? 17.686  11.785  -29.956 1.00 15.53 ? 725  LEU   A CA  1 
ATOM   2293 C  C   . LEU   A 1 284 ? 18.647  10.923  -30.759 1.00 16.56 ? 725  LEU   A C   1 
ATOM   2294 O  O   . LEU   A 1 284 ? 19.865  10.953  -30.524 1.00 16.85 ? 725  LEU   A O   1 
ATOM   2295 C  CB  . LEU   A 1 284 ? 16.984  10.961  -28.871 1.00 17.23 ? 725  LEU   A CB  1 
ATOM   2296 C  CG  . LEU   A 1 284 ? 15.938  11.659  -27.994 1.00 15.12 ? 725  LEU   A CG  1 
ATOM   2297 C  CD1 . LEU   A 1 284 ? 15.398  10.689  -26.940 1.00 16.35 ? 725  LEU   A CD1 1 
ATOM   2298 C  CD2 . LEU   A 1 284 ? 16.503  12.919  -27.304 1.00 18.05 ? 725  LEU   A CD2 1 
ATOM   2299 N  N   . THR   A 1 285 ? 18.130  10.172  -31.736 1.00 14.44 ? 726  THR   A N   1 
ATOM   2300 C  CA  . THR   A 1 285 ? 18.997  9.360   -32.586 1.00 15.30 ? 726  THR   A CA  1 
ATOM   2301 C  C   . THR   A 1 285 ? 19.996  10.229  -33.334 1.00 16.89 ? 726  THR   A C   1 
ATOM   2302 O  O   . THR   A 1 285 ? 21.196  9.938   -33.356 1.00 14.85 ? 726  THR   A O   1 
ATOM   2303 C  CB  . THR   A 1 285 ? 18.152  8.575   -33.594 1.00 13.86 ? 726  THR   A CB  1 
ATOM   2304 O  OG1 . THR   A 1 285 ? 17.222  7.733   -32.896 1.00 14.36 ? 726  THR   A OG1 1 
ATOM   2305 C  CG2 . THR   A 1 285 ? 18.999  7.735   -34.487 1.00 13.72 ? 726  THR   A CG2 1 
ATOM   2306 N  N   . HIS   A 1 286 ? 19.503  11.292  -33.976 1.00 17.68 ? 727  HIS   A N   1 
ATOM   2307 C  CA  . HIS   A 1 286 ? 20.372  12.172  -34.749 1.00 15.82 ? 727  HIS   A CA  1 
ATOM   2308 C  C   . HIS   A 1 286 ? 21.483  12.770  -33.883 1.00 19.64 ? 727  HIS   A C   1 
ATOM   2309 O  O   . HIS   A 1 286 ? 22.622  12.901  -34.334 1.00 18.33 ? 727  HIS   A O   1 
ATOM   2310 C  CB  . HIS   A 1 286 ? 19.520  13.265  -35.389 1.00 19.17 ? 727  HIS   A CB  1 
ATOM   2311 C  CG  . HIS   A 1 286 ? 20.283  14.187  -36.281 1.00 23.44 ? 727  HIS   A CG  1 
ATOM   2312 N  ND1 . HIS   A 1 286 ? 20.628  13.857  -37.575 1.00 33.75 ? 727  HIS   A ND1 1 
ATOM   2313 C  CD2 . HIS   A 1 286 ? 20.758  15.433  -36.066 1.00 20.03 ? 727  HIS   A CD2 1 
ATOM   2314 C  CE1 . HIS   A 1 286 ? 21.291  14.861  -38.118 1.00 24.92 ? 727  HIS   A CE1 1 
ATOM   2315 N  NE2 . HIS   A 1 286 ? 21.378  15.832  -37.226 1.00 34.63 ? 727  HIS   A NE2 1 
ATOM   2316 N  N   . GLN   A 1 287 ? 21.182  13.129  -32.637 1.00 17.11 ? 728  GLN   A N   1 
ATOM   2317 C  CA  . GLN   A 1 287 ? 22.243  13.599  -31.747 1.00 17.15 ? 728  GLN   A CA  1 
ATOM   2318 C  C   . GLN   A 1 287 ? 23.281  12.509  -31.488 1.00 18.13 ? 728  GLN   A C   1 
ATOM   2319 O  O   . GLN   A 1 287 ? 24.494  12.760  -31.558 1.00 19.25 ? 728  GLN   A O   1 
ATOM   2320 C  CB  . GLN   A 1 287 ? 21.634  14.099  -30.445 1.00 18.23 ? 728  GLN   A CB  1 
ATOM   2321 C  CG  . GLN   A 1 287 ? 20.859  15.396  -30.629 1.00 19.82 ? 728  GLN   A CG  1 
ATOM   2322 C  CD  . GLN   A 1 287 ? 20.359  15.962  -29.324 1.00 29.28 ? 728  GLN   A CD  1 
ATOM   2323 O  OE1 . GLN   A 1 287 ? 21.142  16.254  -28.428 1.00 29.10 ? 728  GLN   A OE1 1 
ATOM   2324 N  NE2 . GLN   A 1 287 ? 19.049  16.112  -29.203 1.00 34.63 ? 728  GLN   A NE2 1 
ATOM   2325 N  N   . LEU   A 1 288 ? 22.827  11.282  -31.204 1.00 17.03 ? 729  LEU   A N   1 
ATOM   2326 C  CA  . LEU   A 1 288 ? 23.775  10.210  -30.930 1.00 15.34 ? 729  LEU   A CA  1 
ATOM   2327 C  C   . LEU   A 1 288 ? 24.656  9.914   -32.138 1.00 15.92 ? 729  LEU   A C   1 
ATOM   2328 O  O   . LEU   A 1 288 ? 25.803  9.485   -31.977 1.00 17.59 ? 729  LEU   A O   1 
ATOM   2329 C  CB  . LEU   A 1 288 ? 23.069  8.937   -30.460 1.00 16.62 ? 729  LEU   A CB  1 
ATOM   2330 C  CG  . LEU   A 1 288 ? 22.335  9.077   -29.124 1.00 17.95 ? 729  LEU   A CG  1 
ATOM   2331 C  CD1 . LEU   A 1 288 ? 21.688  7.754   -28.694 1.00 17.11 ? 729  LEU   A CD1 1 
ATOM   2332 C  CD2 . LEU   A 1 288 ? 23.266  9.602   -28.038 1.00 17.21 ? 729  LEU   A CD2 1 
ATOM   2333 N  N   . MET   A 1 289 ? 24.147  10.134  -33.358 1.00 16.26 ? 730  MET   A N   1 
ATOM   2334 C  CA  . MET   A 1 289 ? 24.915  9.874   -34.574 1.00 14.59 ? 730  MET   A CA  1 
ATOM   2335 C  C   . MET   A 1 289 ? 26.156  10.765  -34.697 1.00 14.31 ? 730  MET   A C   1 
ATOM   2336 O  O   . MET   A 1 289 ? 27.052  10.454  -35.494 1.00 19.72 ? 730  MET   A O   1 
ATOM   2337 C  CB  . MET   A 1 289 ? 23.997  10.037  -35.799 1.00 19.96 ? 730  MET   A CB  1 
ATOM   2338 C  CG  . MET   A 1 289 ? 22.984  8.909   -35.968 1.00 14.97 ? 730  MET   A CG  1 
ATOM   2339 S  SD  . MET   A 1 289 ? 21.791  9.258   -37.288 1.00 17.89 ? 730  MET   A SD  1 
ATOM   2340 C  CE  . MET   A 1 289 ? 22.873  9.302   -38.722 1.00 15.66 ? 730  MET   A CE  1 
ATOM   2341 N  N   . SER   A 1 290 ? 26.211  11.873  -33.957 1.00 17.79 ? 731  SER   A N   1 
ATOM   2342 C  CA  . SER   A 1 290 ? 27.389  12.743  -33.935 1.00 19.93 ? 731  SER   A CA  1 
ATOM   2343 C  C   . SER   A 1 290 ? 28.544  12.166  -33.128 1.00 35.57 ? 731  SER   A C   1 
ATOM   2344 O  O   . SER   A 1 290 ? 29.628  12.763  -33.112 1.00 28.22 ? 731  SER   A O   1 
ATOM   2345 C  CB  . SER   A 1 290 ? 27.025  14.128  -33.380 1.00 22.08 ? 731  SER   A CB  1 
ATOM   2346 O  OG  . SER   A 1 290 ? 26.705  14.097  -31.997 1.00 23.26 ? 731  SER   A OG  1 
ATOM   2347 N  N   . LEU   A 1 291 ? 28.339  11.036  -32.461 1.00 19.63 ? 732  LEU   A N   1 
ATOM   2348 C  CA  . LEU   A 1 291 ? 29.325  10.401  -31.601 1.00 16.74 ? 732  LEU   A CA  1 
ATOM   2349 C  C   . LEU   A 1 291 ? 29.911  9.200   -32.316 1.00 19.11 ? 732  LEU   A C   1 
ATOM   2350 O  O   . LEU   A 1 291 ? 29.294  8.624   -33.220 1.00 20.79 ? 732  LEU   A O   1 
ATOM   2351 C  CB  . LEU   A 1 291 ? 28.661  9.909   -30.317 1.00 18.46 ? 732  LEU   A CB  1 
ATOM   2352 C  CG  . LEU   A 1 291 ? 27.895  10.874  -29.437 1.00 18.34 ? 732  LEU   A CG  1 
ATOM   2353 C  CD1 . LEU   A 1 291 ? 27.084  10.085  -28.416 1.00 18.10 ? 732  LEU   A CD1 1 
ATOM   2354 C  CD2 . LEU   A 1 291 ? 28.854  11.865  -28.750 1.00 24.89 ? 732  LEU   A CD2 1 
ATOM   2355 N  N   . ALA   A 1 292 ? 31.125  8.820   -31.905 1.00 22.34 ? 733  ALA   A N   1 
ATOM   2356 C  CA  . ALA   A 1 292 ? 31.735  7.573   -32.362 1.00 20.07 ? 733  ALA   A CA  1 
ATOM   2357 C  C   . ALA   A 1 292 ? 31.789  7.477   -33.885 1.00 18.52 ? 733  ALA   A C   1 
ATOM   2358 O  O   . ALA   A 1 292 ? 31.682  6.390   -34.450 1.00 17.88 ? 733  ALA   A O   1 
ATOM   2359 C  CB  . ALA   A 1 292 ? 31.033  6.347   -31.769 1.00 20.48 ? 733  ALA   A CB  1 
ATOM   2360 N  N   . ALA   A 1 293 ? 31.958  8.619   -34.562 1.00 21.82 ? 734  ALA   A N   1 
ATOM   2361 C  CA  . ALA   A 1 293 ? 31.990  8.664   -36.029 1.00 21.71 ? 734  ALA   A CA  1 
ATOM   2362 C  C   . ALA   A 1 293 ? 30.763  7.994   -36.647 1.00 22.83 ? 734  ALA   A C   1 
ATOM   2363 O  O   . ALA   A 1 293 ? 30.828  7.411   -37.733 1.00 22.71 ? 734  ALA   A O   1 
ATOM   2364 C  CB  . ALA   A 1 293 ? 33.290  8.081   -36.587 1.00 25.03 ? 734  ALA   A CB  1 
ATOM   2365 N  N   . GLY   A 1 294 ? 29.648  8.035   -35.921 1.00 19.18 ? 735  GLY   A N   1 
ATOM   2366 C  CA  . GLY   A 1 294 ? 28.394  7.494   -36.413 1.00 18.89 ? 735  GLY   A CA  1 
ATOM   2367 C  C   . GLY   A 1 294 ? 28.177  6.013   -36.182 1.00 19.19 ? 735  GLY   A C   1 
ATOM   2368 O  O   . GLY   A 1 294 ? 27.166  5.475   -36.652 1.00 17.41 ? 735  GLY   A O   1 
ATOM   2369 N  N   . ARG   A 1 295 ? 29.068  5.333   -35.455 1.00 17.67 ? 736  ARG   A N   1 
ATOM   2370 C  CA  . ARG   A 1 295 ? 28.938  3.893   -35.217 1.00 16.17 ? 736  ARG   A CA  1 
ATOM   2371 C  C   . ARG   A 1 295 ? 27.931  3.677   -34.090 1.00 14.63 ? 736  ARG   A C   1 
ATOM   2372 O  O   . ARG   A 1 295 ? 28.279  3.607   -32.906 1.00 15.90 ? 736  ARG   A O   1 
ATOM   2373 C  CB  . ARG   A 1 295 ? 30.290  3.276   -34.892 1.00 15.12 ? 736  ARG   A CB  1 
ATOM   2374 C  CG  . ARG   A 1 295 ? 31.260  3.484   -36.052 1.00 21.24 ? 736  ARG   A CG  1 
ATOM   2375 C  CD  . ARG   A 1 295 ? 32.533  2.667   -35.921 1.00 19.15 ? 736  ARG   A CD  1 
ATOM   2376 N  NE  . ARG   A 1 295 ? 33.362  2.804   -37.119 1.00 41.88 ? 736  ARG   A NE  1 
ATOM   2377 C  CZ  . ARG   A 1 295 ? 34.342  3.695   -37.264 1.00 35.22 ? 736  ARG   A CZ  1 
ATOM   2378 N  NH1 . ARG   A 1 295 ? 34.639  4.538   -36.286 1.00 24.21 ? 736  ARG   A NH1 1 
ATOM   2379 N  NH2 . ARG   A 1 295 ? 35.032  3.738   -38.395 1.00 37.16 ? 736  ARG   A NH2 1 
ATOM   2380 N  N   . VAL   A 1 296 ? 26.655  3.558   -34.485 1.00 14.76 ? 737  VAL   A N   1 
ATOM   2381 C  CA  . VAL   A 1 296 ? 25.517  3.483   -33.568 1.00 16.49 ? 737  VAL   A CA  1 
ATOM   2382 C  C   . VAL   A 1 296 ? 24.711  2.235   -33.890 1.00 12.63 ? 737  VAL   A C   1 
ATOM   2383 O  O   . VAL   A 1 296 ? 24.368  1.994   -35.056 1.00 13.00 ? 737  VAL   A O   1 
ATOM   2384 C  CB  . VAL   A 1 296 ? 24.597  4.713   -33.699 1.00 15.94 ? 737  VAL   A CB  1 
ATOM   2385 C  CG1 . VAL   A 1 296 ? 23.344  4.524   -32.863 1.00 15.40 ? 737  VAL   A CG1 1 
ATOM   2386 C  CG2 . VAL   A 1 296 ? 25.345  5.999   -33.325 1.00 19.07 ? 737  VAL   A CG2 1 
ATOM   2387 N  N   . LEU   A 1 297 ? 24.381  1.459   -32.858 1.00 13.85 ? 738  LEU   A N   1 
ATOM   2388 C  CA  . LEU   A 1 297 ? 23.525  0.286   -32.990 1.00 12.88 ? 738  LEU   A CA  1 
ATOM   2389 C  C   . LEU   A 1 297 ? 22.324  0.469   -32.080 1.00 13.23 ? 738  LEU   A C   1 
ATOM   2390 O  O   . LEU   A 1 297 ? 22.472  0.592   -30.860 1.00 13.18 ? 738  LEU   A O   1 
ATOM   2391 C  CB  . LEU   A 1 297 ? 24.289  -0.980  -32.609 1.00 15.11 ? 738  LEU   A CB  1 
ATOM   2392 C  CG  . LEU   A 1 297 ? 23.482  -2.257  -32.381 1.00 15.07 ? 738  LEU   A CG  1 
ATOM   2393 C  CD1 . LEU   A 1 297 ? 22.598  -2.561  -33.598 1.00 17.64 ? 738  LEU   A CD1 1 
ATOM   2394 C  CD2 . LEU   A 1 297 ? 24.424  -3.419  -32.062 1.00 16.26 ? 738  LEU   A CD2 1 
ATOM   2395 N  N   . ILE   A 1 298 ? 21.142  0.512   -32.681 1.00 11.78 ? 739  ILE   A N   1 
ATOM   2396 C  CA  . ILE   A 1 298 ? 19.897  0.718   -31.946 1.00 13.46 ? 739  ILE   A CA  1 
ATOM   2397 C  C   . ILE   A 1 298 ? 19.277  -0.646  -31.659 1.00 11.41 ? 739  ILE   A C   1 
ATOM   2398 O  O   . ILE   A 1 298 ? 18.931  -1.370  -32.589 1.00 13.10 ? 739  ILE   A O   1 
ATOM   2399 C  CB  . ILE   A 1 298 ? 18.948  1.629   -32.748 1.00 13.33 ? 739  ILE   A CB  1 
ATOM   2400 C  CG1 . ILE   A 1 298 ? 19.590  3.015   -32.924 1.00 15.34 ? 739  ILE   A CG1 1 
ATOM   2401 C  CG2 . ILE   A 1 298 ? 17.558  1.694   -32.088 1.00 13.93 ? 739  ILE   A CG2 1 
ATOM   2402 C  CD1 . ILE   A 1 298 ? 18.766  3.999   -33.738 1.00 17.49 ? 739  ILE   A CD1 1 
ATOM   2403 N  N   . ILE   A 1 299 ? 19.094  -1.000  -30.383 1.00 11.27 ? 740  ILE   A N   1 
ATOM   2404 C  CA  . ILE   A 1 299 ? 18.592  -2.316  -29.977 1.00 14.07 ? 740  ILE   A CA  1 
ATOM   2405 C  C   . ILE   A 1 299 ? 17.225  -2.158  -29.302 1.00 11.02 ? 740  ILE   A C   1 
ATOM   2406 O  O   . ILE   A 1 299 ? 17.108  -1.470  -28.282 1.00 12.23 ? 740  ILE   A O   1 
ATOM   2407 C  CB  . ILE   A 1 299 ? 19.566  -2.982  -28.993 1.00 11.88 ? 740  ILE   A CB  1 
ATOM   2408 C  CG1 . ILE   A 1 299 ? 20.979  -3.087  -29.605 1.00 11.60 ? 740  ILE   A CG1 1 
ATOM   2409 C  CG2 . ILE   A 1 299 ? 19.045  -4.334  -28.554 1.00 14.97 ? 740  ILE   A CG2 1 
ATOM   2410 C  CD1 . ILE   A 1 299 ? 22.025  -3.564  -28.625 1.00 13.60 ? 740  ILE   A CD1 1 
ATOM   2411 N  N   . LEU   A 1 300 ? 16.198  -2.821  -29.839 1.00 11.54 ? 741  LEU   A N   1 
ATOM   2412 C  CA  . LEU   A 1 300 ? 14.879  -2.734  -29.211 1.00 12.27 ? 741  LEU   A CA  1 
ATOM   2413 C  C   . LEU   A 1 300 ? 14.903  -3.299  -27.784 1.00 12.19 ? 741  LEU   A C   1 
ATOM   2414 O  O   . LEU   A 1 300 ? 15.409  -4.403  -27.548 1.00 12.19 ? 741  LEU   A O   1 
ATOM   2415 C  CB  . LEU   A 1 300 ? 13.866  -3.500  -30.065 1.00 13.86 ? 741  LEU   A CB  1 
ATOM   2416 C  CG  . LEU   A 1 300 ? 12.422  -3.485  -29.554 1.00 11.50 ? 741  LEU   A CG  1 
ATOM   2417 C  CD1 . LEU   A 1 300 ? 11.894  -2.060  -29.584 1.00 13.17 ? 741  LEU   A CD1 1 
ATOM   2418 C  CD2 . LEU   A 1 300 ? 11.545  -4.401  -30.384 1.00 13.96 ? 741  LEU   A CD2 1 
ATOM   2419 N  N   . GLU   A 1 301 ? 14.360  -2.533  -26.818 1.00 10.33 ? 742  GLU   A N   1 
ATOM   2420 C  CA  . GLU   A 1 301 ? 14.092  -3.047  -25.470 1.00 12.61 ? 742  GLU   A CA  1 
ATOM   2421 C  C   . GLU   A 1 301 ? 12.572  -3.192  -25.299 1.00 10.17 ? 742  GLU   A C   1 
ATOM   2422 O  O   . GLU   A 1 301 ? 11.966  -4.040  -25.957 1.00 12.53 ? 742  GLU   A O   1 
ATOM   2423 C  CB  . GLU   A 1 301 ? 14.753  -2.169  -24.382 1.00 11.81 ? 742  GLU   A CB  1 
ATOM   2424 C  CG  . GLU   A 1 301 ? 16.320  -2.113  -24.464 1.00 12.46 ? 742  GLU   A CG  1 
ATOM   2425 C  CD  . GLU   A 1 301 ? 17.062  -3.337  -23.885 1.00 13.62 ? 742  GLU   A CD  1 
ATOM   2426 O  OE1 . GLU   A 1 301 ? 16.435  -4.336  -23.496 1.00 14.74 ? 742  GLU   A OE1 1 
ATOM   2427 O  OE2 . GLU   A 1 301 ? 18.317  -3.301  -23.821 1.00 13.96 ? 742  GLU   A OE2 1 
ATOM   2428 N  N   . GLY   A 1 302 ? 11.963  -2.390  -24.424 1.00 13.29 ? 743  GLY   A N   1 
ATOM   2429 C  CA  . GLY   A 1 302 ? 10.524  -2.406  -24.224 1.00 13.71 ? 743  GLY   A CA  1 
ATOM   2430 C  C   . GLY   A 1 302 ? 9.764   -1.483  -25.152 1.00 14.77 ? 743  GLY   A C   1 
ATOM   2431 O  O   . GLY   A 1 302 ? 10.262  -1.039  -26.187 1.00 13.84 ? 743  GLY   A O   1 
ATOM   2432 N  N   . GLY   A 1 303 ? 8.526   -1.206  -24.774 1.00 13.85 ? 744  GLY   A N   1 
ATOM   2433 C  CA  . GLY   A 1 303 ? 7.599   -0.460  -25.613 1.00 14.31 ? 744  GLY   A CA  1 
ATOM   2434 C  C   . GLY   A 1 303 ? 6.426   -1.324  -26.029 1.00 13.47 ? 744  GLY   A C   1 
ATOM   2435 O  O   . GLY   A 1 303 ? 6.625   -2.349  -26.686 1.00 12.60 ? 744  GLY   A O   1 
ATOM   2436 N  N   . TYR   A 1 304 ? 5.195   -0.914  -25.687 1.00 12.05 ? 745  TYR   A N   1 
ATOM   2437 C  CA  . TYR   A 1 304 ? 4.078   -1.836  -25.699 1.00 11.93 ? 745  TYR   A CA  1 
ATOM   2438 C  C   . TYR   A 1 304 ? 2.840   -1.345  -26.434 1.00 14.54 ? 745  TYR   A C   1 
ATOM   2439 O  O   . TYR   A 1 304 ? 1.865   -2.095  -26.501 1.00 17.47 ? 745  TYR   A O   1 
ATOM   2440 C  CB  . TYR   A 1 304 ? 3.716   -2.243  -24.251 1.00 14.71 ? 745  TYR   A CB  1 
ATOM   2441 C  CG  . TYR   A 1 304 ? 4.951   -2.765  -23.585 1.00 14.16 ? 745  TYR   A CG  1 
ATOM   2442 C  CD1 . TYR   A 1 304 ? 5.440   -4.021  -23.917 1.00 15.15 ? 745  TYR   A CD1 1 
ATOM   2443 C  CD2 . TYR   A 1 304 ? 5.696   -1.968  -22.712 1.00 15.11 ? 745  TYR   A CD2 1 
ATOM   2444 C  CE1 . TYR   A 1 304 ? 6.617   -4.496  -23.379 1.00 15.66 ? 745  TYR   A CE1 1 
ATOM   2445 C  CE2 . TYR   A 1 304 ? 6.893   -2.429  -22.157 1.00 14.90 ? 745  TYR   A CE2 1 
ATOM   2446 C  CZ  . TYR   A 1 304 ? 7.327   -3.708  -22.484 1.00 15.76 ? 745  TYR   A CZ  1 
ATOM   2447 O  OH  . TYR   A 1 304 ? 8.506   -4.221  -21.997 1.00 19.91 ? 745  TYR   A OH  1 
ATOM   2448 N  N   . ASN   A 1 305 ? 2.844   -0.130  -26.979 1.00 11.83 ? 746  ASN   A N   1 
ATOM   2449 C  CA  . ASN   A 1 305 ? 1.819   0.289   -27.932 1.00 11.71 ? 746  ASN   A CA  1 
ATOM   2450 C  C   . ASN   A 1 305 ? 2.356   -0.034  -29.321 1.00 13.38 ? 746  ASN   A C   1 
ATOM   2451 O  O   . ASN   A 1 305 ? 3.323   0.594   -29.778 1.00 13.62 ? 746  ASN   A O   1 
ATOM   2452 C  CB  . ASN   A 1 305 ? 1.478   1.767   -27.742 1.00 12.11 ? 746  ASN   A CB  1 
ATOM   2453 C  CG  . ASN   A 1 305 ? 0.428   2.255   -28.744 1.00 15.25 ? 746  ASN   A CG  1 
ATOM   2454 O  OD1 . ASN   A 1 305 ? 0.520   2.004   -29.942 1.00 14.06 ? 746  ASN   A OD1 1 
ATOM   2455 N  ND2 . ASN   A 1 305 ? -0.602  2.933   -28.229 1.00 13.52 ? 746  ASN   A ND2 1 
ATOM   2456 N  N   . LEU   A 1 306 ? 1.743   -1.030  -29.968 1.00 11.39 ? 747  LEU   A N   1 
ATOM   2457 C  CA  . LEU   A 1 306 ? 2.276   -1.539  -31.228 1.00 12.19 ? 747  LEU   A CA  1 
ATOM   2458 C  C   . LEU   A 1 306 ? 2.408   -0.427  -32.258 1.00 14.18 ? 747  LEU   A C   1 
ATOM   2459 O  O   . LEU   A 1 306 ? 3.406   -0.363  -32.990 1.00 12.24 ? 747  LEU   A O   1 
ATOM   2460 C  CB  . LEU   A 1 306 ? 1.385   -2.666  -31.767 1.00 12.60 ? 747  LEU   A CB  1 
ATOM   2461 C  CG  . LEU   A 1 306 ? 1.287   -3.904  -30.866 1.00 12.56 ? 747  LEU   A CG  1 
ATOM   2462 C  CD1 . LEU   A 1 306 ? 0.258   -4.908  -31.389 1.00 14.99 ? 747  LEU   A CD1 1 
ATOM   2463 C  CD2 . LEU   A 1 306 ? 2.664   -4.567  -30.746 1.00 13.42 ? 747  LEU   A CD2 1 
ATOM   2464 N  N   . THR   A 1 307 ? 1.410   0.459   -32.340 1.00 12.44 ? 748  THR   A N   1 
ATOM   2465 C  CA  . THR   A 1 307 ? 1.497   1.575   -33.279 1.00 13.44 ? 748  THR   A CA  1 
ATOM   2466 C  C   . THR   A 1 307 ? 2.585   2.564   -32.881 1.00 14.11 ? 748  THR   A C   1 
ATOM   2467 O  O   . THR   A 1 307 ? 3.371   2.996   -33.735 1.00 13.77 ? 748  THR   A O   1 
ATOM   2468 C  CB  . THR   A 1 307 ? 0.127   2.246   -33.375 1.00 15.32 ? 748  THR   A CB  1 
ATOM   2469 O  OG1 . THR   A 1 307 ? -0.785  1.306   -33.942 1.00 14.80 ? 748  THR   A OG1 1 
ATOM   2470 C  CG2 . THR   A 1 307 ? 0.209   3.502   -34.227 1.00 21.52 ? 748  THR   A CG2 1 
ATOM   2471 N  N   . SER   A 1 308 ? 2.682   2.905   -31.594 1.00 14.86 ? 749  SER   A N   1 
ATOM   2472 C  CA  . SER   A 1 308 ? 3.684   3.879   -31.169 1.00 13.67 ? 749  SER   A CA  1 
ATOM   2473 C  C   . SER   A 1 308 ? 5.100   3.360   -31.398 1.00 14.03 ? 749  SER   A C   1 
ATOM   2474 O  O   . SER   A 1 308 ? 5.990   4.112   -31.818 1.00 14.74 ? 749  SER   A O   1 
ATOM   2475 C  CB  . SER   A 1 308 ? 3.542   4.201   -29.677 1.00 14.91 ? 749  SER   A CB  1 
ATOM   2476 O  OG  . SER   A 1 308 ? 2.265   4.751   -29.382 1.00 19.38 ? 749  SER   A OG  1 
ATOM   2477 N  N   . ILE   A 1 309 ? 5.355   2.097   -31.041 1.00 12.64 ? 750  ILE   A N   1 
ATOM   2478 C  CA  . ILE   A 1 309 ? 6.722   1.592   -31.192 1.00 11.25 ? 750  ILE   A CA  1 
ATOM   2479 C  C   . ILE   A 1 309 ? 7.110   1.465   -32.657 1.00 13.75 ? 750  ILE   A C   1 
ATOM   2480 O  O   . ILE   A 1 309 ? 8.283   1.671   -33.020 1.00 12.22 ? 750  ILE   A O   1 
ATOM   2481 C  CB  . ILE   A 1 309 ? 6.954   0.280   -30.425 1.00 10.99 ? 750  ILE   A CB  1 
ATOM   2482 C  CG1 . ILE   A 1 309 ? 6.233   -0.902  -31.090 1.00 14.13 ? 750  ILE   A CG1 1 
ATOM   2483 C  CG2 . ILE   A 1 309 ? 6.539   0.441   -28.975 1.00 12.06 ? 750  ILE   A CG2 1 
ATOM   2484 C  CD1 . ILE   A 1 309 ? 6.432   -2.239  -30.369 1.00 15.48 ? 750  ILE   A CD1 1 
ATOM   2485 N  N   . SER   A 1 310 ? 6.142   1.141   -33.519 1.00 10.57 ? 751  SER   A N   1 
ATOM   2486 C  CA  . SER   A 1 310 ? 6.452   0.960   -34.930 1.00 13.13 ? 751  SER   A CA  1 
ATOM   2487 C  C   . SER   A 1 310 ? 6.794   2.291   -35.554 1.00 12.88 ? 751  SER   A C   1 
ATOM   2488 O  O   . SER   A 1 310 ? 7.739   2.384   -36.342 1.00 13.45 ? 751  SER   A O   1 
ATOM   2489 C  CB  . SER   A 1 310 ? 5.267   0.297   -35.636 1.00 12.86 ? 751  SER   A CB  1 
ATOM   2490 O  OG  . SER   A 1 310 ? 5.053   -1.006  -35.119 1.00 13.22 ? 751  SER   A OG  1 
ATOM   2491 N  N   . GLU   A 1 311 ? 6.029   3.328   -35.230 1.00 12.56 ? 752  GLU   A N   1 
ATOM   2492 C  CA  . GLU   A 1 311 ? 6.321   4.655   -35.762 1.00 16.05 ? 752  GLU   A CA  1 
ATOM   2493 C  C   . GLU   A 1 311 ? 7.627   5.192   -35.196 1.00 14.30 ? 752  GLU   A C   1 
ATOM   2494 O  O   . GLU   A 1 311 ? 8.453   5.745   -35.932 1.00 14.12 ? 752  GLU   A O   1 
ATOM   2495 C  CB  . GLU   A 1 311 ? 5.164   5.605   -35.443 1.00 15.04 ? 752  GLU   A CB  1 
ATOM   2496 C  CG  . GLU   A 1 311 ? 5.308   6.950   -36.076 1.00 18.82 ? 752  GLU   A CG  1 
ATOM   2497 C  CD  . GLU   A 1 311 ? 5.246   6.904   -37.592 1.00 47.06 ? 752  GLU   A CD  1 
ATOM   2498 O  OE1 . GLU   A 1 311 ? 4.572   6.002   -38.133 1.00 23.36 ? 752  GLU   A OE1 1 
ATOM   2499 O  OE2 . GLU   A 1 311 ? 5.874   7.773   -38.237 1.00 34.60 ? 752  GLU   A OE2 1 
ATOM   2500 N  N   . SER   A 1 312 ? 7.851   4.986   -33.908 1.00 12.70 ? 753  SER   A N   1 
ATOM   2501 C  CA  . SER   A 1 312 ? 9.021   5.549   -33.238 1.00 16.20 ? 753  SER   A CA  1 
ATOM   2502 C  C   . SER   A 1 312 ? 10.313  4.899   -33.716 1.00 13.28 ? 753  SER   A C   1 
ATOM   2503 O  O   . SER   A 1 312 ? 11.281  5.596   -34.057 1.00 13.09 ? 753  SER   A O   1 
ATOM   2504 C  CB  . SER   A 1 312 ? 8.897   5.364   -31.725 1.00 15.79 ? 753  SER   A CB  1 
ATOM   2505 O  OG  . SER   A 1 312 ? 7.796   6.091   -31.198 1.00 15.58 ? 753  SER   A OG  1 
ATOM   2506 N  N   . MET   A 1 313 ? 10.365  3.568   -33.727 1.00 11.33 ? 754  MET   A N   1 
ATOM   2507 C  CA  . MET   A 1 313 ? 11.605  2.917   -34.148 1.00 13.38 ? 754  MET   A CA  1 
ATOM   2508 C  C   . MET   A 1 313 ? 11.885  3.165   -35.627 1.00 13.86 ? 754  MET   A C   1 
ATOM   2509 O  O   . MET   A 1 313 ? 13.048  3.348   -36.019 1.00 13.55 ? 754  MET   A O   1 
ATOM   2510 C  CB  . MET   A 1 313 ? 11.585  1.431   -33.859 1.00 12.09 ? 754  MET   A CB  1 
ATOM   2511 C  CG  . MET   A 1 313 ? 12.997  0.860   -33.861 1.00 14.57 ? 754  MET   A CG  1 
ATOM   2512 S  SD  . MET   A 1 313 ? 13.110  -0.832  -33.262 1.00 13.63 ? 754  MET   A SD  1 
ATOM   2513 C  CE  . MET   A 1 313 ? 14.822  -0.933  -32.783 1.00 16.32 ? 754  MET   A CE  1 
ATOM   2514 N  N   A SER   A 1 314 ? 10.834  3.266   -36.444 0.41 13.13 ? 755  SER   A N   1 
ATOM   2515 N  N   B SER   A 1 314 ? 10.857  3.083   -36.477 0.59 12.77 ? 755  SER   A N   1 
ATOM   2516 C  CA  A SER   A 1 314 ? 11.035  3.617   -37.848 0.41 9.49  ? 755  SER   A CA  1 
ATOM   2517 C  CA  B SER   A 1 314 ? 11.085  3.294   -37.906 0.59 15.15 ? 755  SER   A CA  1 
ATOM   2518 C  C   A SER   A 1 314 ? 11.617  5.017   -37.992 0.41 8.68  ? 755  SER   A C   1 
ATOM   2519 C  C   B SER   A 1 314 ? 11.636  4.685   -38.184 0.59 12.93 ? 755  SER   A C   1 
ATOM   2520 O  O   A SER   A 1 314 ? 12.480  5.253   -38.848 0.41 8.68  ? 755  SER   A O   1 
ATOM   2521 O  O   B SER   A 1 314 ? 12.442  4.859   -39.111 0.59 16.03 ? 755  SER   A O   1 
ATOM   2522 C  CB  A SER   A 1 314 ? 9.727   3.498   -38.631 0.41 12.14 ? 755  SER   A CB  1 
ATOM   2523 C  CB  B SER   A 1 314 ? 9.811   3.041   -38.724 0.59 14.72 ? 755  SER   A CB  1 
ATOM   2524 O  OG  A SER   A 1 314 ? 9.282   2.158   -38.658 0.41 11.32 ? 755  SER   A OG  1 
ATOM   2525 O  OG  B SER   A 1 314 ? 8.786   3.955   -38.385 0.59 14.08 ? 755  SER   A OG  1 
ATOM   2526 N  N   A MET   A 1 315 ? 11.166  5.961   -37.158 0.41 11.75 ? 756  MET   A N   1 
ATOM   2527 N  N   B MET   A 1 315 ? 11.230  5.683   -37.387 0.59 13.91 ? 756  MET   A N   1 
ATOM   2528 C  CA  A MET   A 1 315 ? 11.718  7.309   -37.222 0.41 15.53 ? 756  MET   A CA  1 
ATOM   2529 C  CA  B MET   A 1 315 ? 11.789  7.021   -37.553 0.59 13.87 ? 756  MET   A CA  1 
ATOM   2530 C  C   A MET   A 1 315 ? 13.195  7.315   -36.874 0.41 12.64 ? 756  MET   A C   1 
ATOM   2531 C  C   B MET   A 1 315 ? 13.254  7.074   -37.124 0.59 13.91 ? 756  MET   A C   1 
ATOM   2532 O  O   A MET   A 1 315 ? 13.953  8.159   -37.368 0.41 14.83 ? 756  MET   A O   1 
ATOM   2533 O  O   B MET   A 1 315 ? 14.061  7.752   -37.772 0.59 11.77 ? 756  MET   A O   1 
ATOM   2534 C  CB  A MET   A 1 315 ? 10.960  8.241   -36.285 0.41 9.35  ? 756  MET   A CB  1 
ATOM   2535 C  CB  B MET   A 1 315 ? 10.939  8.083   -36.842 0.59 20.33 ? 756  MET   A CB  1 
ATOM   2536 C  CG  A MET   A 1 315 ? 10.752  9.630   -36.860 0.41 32.32 ? 756  MET   A CG  1 
ATOM   2537 C  CG  B MET   A 1 315 ? 10.942  9.456   -37.550 0.59 26.43 ? 756  MET   A CG  1 
ATOM   2538 S  SD  A MET   A 1 315 ? 10.119  9.616   -38.551 0.41 30.11 ? 756  MET   A SD  1 
ATOM   2539 S  SD  B MET   A 1 315 ? 9.758   10.668  -36.915 0.59 22.41 ? 756  MET   A SD  1 
ATOM   2540 C  CE  A MET   A 1 315 ? 11.415  10.516  -39.396 0.41 32.56 ? 756  MET   A CE  1 
ATOM   2541 C  CE  B MET   A 1 315 ? 8.345   10.382  -37.978 0.59 28.57 ? 756  MET   A CE  1 
ATOM   2542 N  N   . CYS   A 1 316 ? 13.621  6.376   -36.037 1.00 12.28 ? 757  CYS   A N   1 
ATOM   2543 C  CA  . CYS   A 1 316 ? 15.040  6.275   -35.705 1.00 13.38 ? 757  CYS   A CA  1 
ATOM   2544 C  C   . CYS   A 1 316 ? 15.843  5.720   -36.871 1.00 15.13 ? 757  CYS   A C   1 
ATOM   2545 O  O   . CYS   A 1 316 ? 16.925  6.231   -37.196 1.00 14.18 ? 757  CYS   A O   1 
ATOM   2546 C  CB  . CYS   A 1 316 ? 15.284  5.410   -34.466 1.00 14.87 ? 757  CYS   A CB  1 
ATOM   2547 S  SG  . CYS   A 1 316 ? 14.533  6.000   -32.952 1.00 15.65 ? 757  CYS   A SG  1 
ATOM   2548 N  N   . THR   A 1 317 ? 15.338  4.671   -37.511 1.00 12.23 ? 758  THR   A N   1 
ATOM   2549 C  CA  . THR   A 1 317 ? 16.029  4.106   -38.654 1.00 14.36 ? 758  THR   A CA  1 
ATOM   2550 C  C   . THR   A 1 317 ? 16.144  5.132   -39.770 1.00 14.24 ? 758  THR   A C   1 
ATOM   2551 O  O   . THR   A 1 317 ? 17.179  5.206   -40.446 1.00 13.68 ? 758  THR   A O   1 
ATOM   2552 C  CB  . THR   A 1 317 ? 15.305  2.843   -39.133 1.00 13.91 ? 758  THR   A CB  1 
ATOM   2553 O  OG1 . THR   A 1 317 ? 15.247  1.881   -38.072 1.00 14.52 ? 758  THR   A OG1 1 
ATOM   2554 C  CG2 . THR   A 1 317 ? 16.051  2.226   -40.300 1.00 14.51 ? 758  THR   A CG2 1 
ATOM   2555 N  N   . SER   A 1 318 ? 15.079  5.917   -39.996 1.00 12.46 ? 759  SER   A N   1 
ATOM   2556 C  CA  . SER   A 1 318 ? 15.146  7.013   -40.961 1.00 15.83 ? 759  SER   A CA  1 
ATOM   2557 C  C   . SER   A 1 318 ? 16.314  7.943   -40.669 1.00 16.42 ? 759  SER   A C   1 
ATOM   2558 O  O   . SER   A 1 318 ? 17.022  8.380   -41.588 1.00 14.86 ? 759  SER   A O   1 
ATOM   2559 C  CB  . SER   A 1 318 ? 13.832  7.792   -40.944 1.00 15.73 ? 759  SER   A CB  1 
ATOM   2560 O  OG  . SER   A 1 318 ? 13.897  8.876   -41.864 1.00 24.56 ? 759  SER   A OG  1 
ATOM   2561 N  N   . MET   A 1 319 ? 16.563  8.228   -39.392 1.00 15.23 ? 760  MET   A N   1 
ATOM   2562 C  CA  . MET   A 1 319 ? 17.698  9.073   -39.041 1.00 15.85 ? 760  MET   A CA  1 
ATOM   2563 C  C   . MET   A 1 319 ? 19.023  8.376   -39.337 1.00 16.66 ? 760  MET   A C   1 
ATOM   2564 O  O   . MET   A 1 319 ? 19.925  8.970   -39.946 1.00 15.96 ? 760  MET   A O   1 
ATOM   2565 C  CB  . MET   A 1 319 ? 17.628  9.480   -37.574 1.00 14.42 ? 760  MET   A CB  1 
ATOM   2566 C  CG  . MET   A 1 319 ? 16.413  10.314  -37.244 1.00 16.60 ? 760  MET   A CG  1 
ATOM   2567 S  SD  . MET   A 1 319 ? 16.325  11.867  -38.177 1.00 18.35 ? 760  MET   A SD  1 
ATOM   2568 C  CE  . MET   A 1 319 ? 15.168  11.467  -39.490 1.00 18.43 ? 760  MET   A CE  1 
ATOM   2569 N  N   . LEU   A 1 320 ? 19.155  7.104   -38.940 1.00 13.89 ? 761  LEU   A N   1 
ATOM   2570 C  CA  . LEU   A 1 320 ? 20.371  6.356   -39.267 1.00 16.42 ? 761  LEU   A CA  1 
ATOM   2571 C  C   . LEU   A 1 320 ? 20.665  6.378   -40.762 1.00 19.99 ? 761  LEU   A C   1 
ATOM   2572 O  O   . LEU   A 1 320 ? 21.834  6.403   -41.163 1.00 15.35 ? 761  LEU   A O   1 
ATOM   2573 C  CB  . LEU   A 1 320 ? 20.265  4.908   -38.789 1.00 16.04 ? 761  LEU   A CB  1 
ATOM   2574 C  CG  . LEU   A 1 320 ? 20.139  4.686   -37.273 1.00 15.25 ? 761  LEU   A CG  1 
ATOM   2575 C  CD1 . LEU   A 1 320 ? 20.198  3.220   -37.010 1.00 17.31 ? 761  LEU   A CD1 1 
ATOM   2576 C  CD2 . LEU   A 1 320 ? 21.227  5.445   -36.509 1.00 16.50 ? 761  LEU   A CD2 1 
ATOM   2577 N  N   . LEU   A 1 321 ? 19.626  6.371   -41.595 1.00 15.34 ? 762  LEU   A N   1 
ATOM   2578 C  CA  . LEU   A 1 321 ? 19.764  6.365   -43.046 1.00 17.24 ? 762  LEU   A CA  1 
ATOM   2579 C  C   . LEU   A 1 321 ? 20.152  7.725   -43.601 1.00 15.46 ? 762  LEU   A C   1 
ATOM   2580 O  O   . LEU   A 1 321 ? 20.416  7.824   -44.810 1.00 19.41 ? 762  LEU   A O   1 
ATOM   2581 C  CB  . LEU   A 1 321 ? 18.458  5.874   -43.701 1.00 14.05 ? 762  LEU   A CB  1 
ATOM   2582 C  CG  . LEU   A 1 321 ? 18.247  4.354   -43.652 1.00 15.29 ? 762  LEU   A CG  1 
ATOM   2583 C  CD1 . LEU   A 1 321 ? 16.793  3.997   -43.913 1.00 17.50 ? 762  LEU   A CD1 1 
ATOM   2584 C  CD2 . LEU   A 1 321 ? 19.139  3.606   -44.631 1.00 16.45 ? 762  LEU   A CD2 1 
ATOM   2585 N  N   . GLY   A 1 322 ? 20.194  8.754   -42.765 1.00 17.05 ? 763  GLY   A N   1 
ATOM   2586 C  CA  . GLY   A 1 322 ? 20.647  10.071  -43.166 1.00 19.68 ? 763  GLY   A CA  1 
ATOM   2587 C  C   . GLY   A 1 322 ? 19.543  11.046  -43.491 1.00 21.19 ? 763  GLY   A C   1 
ATOM   2588 O  O   . GLY   A 1 322 ? 19.834  12.140  -43.991 1.00 25.36 ? 763  GLY   A O   1 
ATOM   2589 N  N   . ASP   A 1 323 ? 18.290  10.696  -43.216 1.00 18.04 ? 764  ASP   A N   1 
ATOM   2590 C  CA  . ASP   A 1 323 ? 17.191  11.610  -43.494 1.00 17.43 ? 764  ASP   A CA  1 
ATOM   2591 C  C   . ASP   A 1 323 ? 17.211  12.785  -42.522 1.00 21.91 ? 764  ASP   A C   1 
ATOM   2592 O  O   . ASP   A 1 323 ? 17.673  12.677  -41.386 1.00 22.03 ? 764  ASP   A O   1 
ATOM   2593 C  CB  . ASP   A 1 323 ? 15.851  10.875  -43.411 1.00 19.01 ? 764  ASP   A CB  1 
ATOM   2594 C  CG  . ASP   A 1 323 ? 15.692  9.816   -44.489 1.00 21.37 ? 764  ASP   A CG  1 
ATOM   2595 O  OD1 . ASP   A 1 323 ? 16.439  9.872   -45.496 1.00 23.48 ? 764  ASP   A OD1 1 
ATOM   2596 O  OD2 . ASP   A 1 323 ? 14.813  8.930   -44.337 1.00 20.72 ? 764  ASP   A OD2 1 
ATOM   2597 N  N   . SER   A 1 324 ? 16.697  13.922  -42.981 1.00 23.36 ? 765  SER   A N   1 
ATOM   2598 C  CA  . SER   A 1 324 ? 16.747  15.128  -42.169 1.00 26.11 ? 765  SER   A CA  1 
ATOM   2599 C  C   . SER   A 1 324 ? 15.784  15.006  -40.991 1.00 24.50 ? 765  SER   A C   1 
ATOM   2600 O  O   . SER   A 1 324 ? 14.678  14.484  -41.145 1.00 22.60 ? 765  SER   A O   1 
ATOM   2601 C  CB  . SER   A 1 324 ? 16.374  16.347  -43.013 1.00 26.10 ? 765  SER   A CB  1 
ATOM   2602 O  OG  . SER   A 1 324 ? 17.436  16.689  -43.887 0.47 30.05 ? 765  SER   A OG  1 
ATOM   2603 N  N   . PRO   A 1 325 ? 16.176  15.466  -39.807 1.00 23.73 ? 766  PRO   A N   1 
ATOM   2604 C  CA  . PRO   A 1 325 ? 15.308  15.355  -38.630 1.00 21.36 ? 766  PRO   A CA  1 
ATOM   2605 C  C   . PRO   A 1 325 ? 14.024  16.142  -38.817 1.00 24.46 ? 766  PRO   A C   1 
ATOM   2606 O  O   . PRO   A 1 325 ? 14.052  17.305  -39.245 1.00 27.49 ? 766  PRO   A O   1 
ATOM   2607 C  CB  . PRO   A 1 325 ? 16.164  15.972  -37.510 1.00 27.66 ? 766  PRO   A CB  1 
ATOM   2608 C  CG  . PRO   A 1 325 ? 17.570  15.820  -37.988 1.00 33.08 ? 766  PRO   A CG  1 
ATOM   2609 C  CD  . PRO   A 1 325 ? 17.497  16.019  -39.474 1.00 24.54 ? 766  PRO   A CD  1 
ATOM   2610 N  N   . PRO   A 1 326 ? 12.875  15.544  -38.524 1.00 22.63 ? 767  PRO   A N   1 
ATOM   2611 C  CA  . PRO   A 1 326 ? 11.618  16.298  -38.591 1.00 21.09 ? 767  PRO   A CA  1 
ATOM   2612 C  C   . PRO   A 1 326 ? 11.520  17.296  -37.449 1.00 31.78 ? 767  PRO   A C   1 
ATOM   2613 O  O   . PRO   A 1 326 ? 12.115  17.118  -36.385 1.00 35.71 ? 767  PRO   A O   1 
ATOM   2614 C  CB  . PRO   A 1 326 ? 10.551  15.207  -38.457 1.00 25.77 ? 767  PRO   A CB  1 
ATOM   2615 C  CG  . PRO   A 1 326 ? 11.237  14.140  -37.653 1.00 32.28 ? 767  PRO   A CG  1 
ATOM   2616 C  CD  . PRO   A 1 326 ? 12.660  14.138  -38.138 1.00 28.49 ? 767  PRO   A CD  1 
ATOM   2617 N  N   . SER   A 1 327 ? 10.727  18.327  -37.709 1.00 25.58 ? 768  SER   A N   1 
ATOM   2618 C  CA  . SER   A 1 327 ? 10.553  19.373  -36.692 1.00 29.79 ? 768  SER   A CA  1 
ATOM   2619 C  C   . SER   A 1 327 ? 9.760   18.870  -35.478 1.00 26.37 ? 768  SER   A C   1 
ATOM   2620 O  O   . SER   A 1 327 ? 8.824   18.097  -35.663 1.00 27.99 ? 768  SER   A O   1 
ATOM   2621 C  CB  . SER   A 1 327 ? 9.918   20.641  -37.280 1.00 41.43 ? 768  SER   A CB  1 
ATOM   2622 O  OG  . SER   A 1 327 ? 10.526  21.011  -38.506 1.00 57.29 ? 768  SER   A OG  1 
ATOM   2623 N  N   . LEU   A 1 328 ? 10.138  19.350  -34.298 1.00 35.29 ? 769  LEU   A N   1 
ATOM   2624 C  CA  . LEU   A 1 328 ? 9.429   19.011  -33.042 1.00 47.86 ? 769  LEU   A CA  1 
ATOM   2625 C  C   . LEU   A 1 328 ? 8.135   19.838  -32.894 1.00 53.43 ? 769  LEU   A C   1 
ATOM   2626 O  O   . LEU   A 1 328 ? 8.121   20.966  -33.396 1.00 60.85 ? 769  LEU   A O   1 
ATOM   2627 C  CB  . LEU   A 1 328 ? 10.395  19.318  -31.902 1.00 39.13 ? 769  LEU   A CB  1 
ATOM   2628 C  CG  . LEU   A 1 328 ? 11.282  18.185  -31.382 1.00 44.02 ? 769  LEU   A CG  1 
ATOM   2629 C  CD1 . LEU   A 1 328 ? 10.912  16.791  -31.842 1.00 28.94 ? 769  LEU   A CD1 1 
ATOM   2630 C  CD2 . LEU   A 1 328 ? 12.740  18.494  -31.637 1.00 41.38 ? 769  LEU   A CD2 1 
ATOM   2631 N  N   . THR   A 1 332 ? 5.125   21.745  -25.628 1.00 73.18 ? 773  THR   A N   1 
ATOM   2632 C  CA  . THR   A 1 332 ? 4.806   22.178  -24.257 1.00 63.67 ? 773  THR   A CA  1 
ATOM   2633 C  C   . THR   A 1 332 ? 6.008   22.855  -23.635 1.00 52.32 ? 773  THR   A C   1 
ATOM   2634 O  O   . THR   A 1 332 ? 7.127   22.725  -24.166 1.00 51.13 ? 773  THR   A O   1 
ATOM   2635 C  CB  . THR   A 1 332 ? 4.353   20.962  -23.447 1.00 57.79 ? 773  THR   A CB  1 
ATOM   2636 N  N   . PRO   A 1 333 ? 5.807   23.701  -22.613 1.00 62.95 ? 774  PRO   A N   1 
ATOM   2637 C  CA  . PRO   A 1 333 ? 6.921   24.287  -21.883 1.00 56.55 ? 774  PRO   A CA  1 
ATOM   2638 C  C   . PRO   A 1 333 ? 7.620   23.251  -21.023 1.00 46.35 ? 774  PRO   A C   1 
ATOM   2639 O  O   . PRO   A 1 333 ? 6.940   22.376  -20.492 1.00 43.78 ? 774  PRO   A O   1 
ATOM   2640 C  CB  . PRO   A 1 333 ? 6.195   25.348  -21.052 1.00 46.90 ? 774  PRO   A CB  1 
ATOM   2641 C  CG  . PRO   A 1 333 ? 4.829   24.763  -20.820 1.00 57.50 ? 774  PRO   A CG  1 
ATOM   2642 C  CD  . PRO   A 1 333 ? 4.510   24.217  -22.193 1.00 62.15 ? 774  PRO   A CD  1 
ATOM   2643 N  N   . LEU   A 1 334 ? 8.921   23.407  -20.862 1.00 33.63 ? 775  LEU   A N   1 
ATOM   2644 C  CA  . LEU   A 1 334 ? 9.725   22.422  -20.106 1.00 36.01 ? 775  LEU   A CA  1 
ATOM   2645 C  C   . LEU   A 1 334 ? 9.139   22.295  -18.702 1.00 41.81 ? 775  LEU   A C   1 
ATOM   2646 O  O   . LEU   A 1 334 ? 8.886   23.315  -18.061 1.00 32.94 ? 775  LEU   A O   1 
ATOM   2647 C  CB  . LEU   A 1 334 ? 11.170  22.900  -20.068 1.00 28.05 ? 775  LEU   A CB  1 
ATOM   2648 C  CG  . LEU   A 1 334 ? 12.171  22.030  -19.307 1.00 37.33 ? 775  LEU   A CG  1 
ATOM   2649 C  CD1 . LEU   A 1 334 ? 12.157  20.613  -19.844 1.00 27.26 ? 775  LEU   A CD1 1 
ATOM   2650 C  CD2 . LEU   A 1 334 ? 13.553  22.625  -19.471 1.00 28.42 ? 775  LEU   A CD2 1 
ATOM   2651 N  N   . LYS   A 1 335 ? 9.001   21.062  -18.239 1.00 27.36 ? 776  LYS   A N   1 
ATOM   2652 C  CA  . LYS   A 1 335 ? 8.457   20.842  -16.882 1.00 33.09 ? 776  LYS   A CA  1 
ATOM   2653 C  C   . LYS   A 1 335 ? 9.536   21.164  -15.837 1.00 36.54 ? 776  LYS   A C   1 
ATOM   2654 O  O   . LYS   A 1 335 ? 10.693  20.739  -15.992 1.00 29.82 ? 776  LYS   A O   1 
ATOM   2655 C  CB  . LYS   A 1 335 ? 7.844   19.447  -16.745 1.00 28.20 ? 776  LYS   A CB  1 
ATOM   2656 C  CG  . LYS   A 1 335 ? 6.660   19.214  -17.657 1.00 30.38 ? 776  LYS   A CG  1 
ATOM   2657 C  CD  . LYS   A 1 335 ? 6.111   17.796  -17.659 1.00 26.75 ? 776  LYS   A CD  1 
ATOM   2658 C  CE  . LYS   A 1 335 ? 4.763   17.729  -18.295 1.00 30.82 ? 776  LYS   A CE  1 
ATOM   2659 N  NZ  . LYS   A 1 335 ? 4.707   18.481  -19.551 1.00 27.05 ? 776  LYS   A NZ  1 
ATOM   2660 N  N   . THR   A 1 336 ? 9.123   21.875  -14.798 1.00 35.12 ? 777  THR   A N   1 
ATOM   2661 C  CA  . THR   A 1 336 ? 10.031  22.292  -13.732 1.00 36.67 ? 777  THR   A CA  1 
ATOM   2662 C  C   . THR   A 1 336 ? 10.700  21.101  -13.054 1.00 32.87 ? 777  THR   A C   1 
ATOM   2663 O  O   . THR   A 1 336 ? 11.907  21.137  -12.764 1.00 26.02 ? 777  THR   A O   1 
ATOM   2664 C  CB  . THR   A 1 336 ? 9.244   23.117  -12.713 1.00 31.23 ? 777  THR   A CB  1 
ATOM   2665 O  OG1 . THR   A 1 336 ? 9.124   24.467  -13.182 1.00 48.52 ? 777  THR   A OG1 1 
ATOM   2666 C  CG2 . THR   A 1 336 ? 9.932   23.104  -11.363 1.00 60.09 ? 777  THR   A CG2 1 
ATOM   2667 N  N   . SER   A 1 337 ? 9.925   20.049  -12.776 1.00 34.54 ? 778  SER   A N   1 
ATOM   2668 C  CA  . SER   A 1 337 ? 10.466  18.852  -12.140 1.00 36.23 ? 778  SER   A CA  1 
ATOM   2669 C  C   . SER   A 1 337 ? 11.615  18.254  -12.940 1.00 26.78 ? 778  SER   A C   1 
ATOM   2670 O  O   . SER   A 1 337 ? 12.570  17.727  -12.360 1.00 25.44 ? 778  SER   A O   1 
ATOM   2671 C  CB  . SER   A 1 337 ? 9.356   17.816  -11.967 1.00 31.76 ? 778  SER   A CB  1 
ATOM   2672 O  OG  . SER   A 1 337 ? 9.894   16.531  -11.739 1.00 52.85 ? 778  SER   A OG  1 
ATOM   2673 N  N   . ALA   A 1 338 ? 11.552  18.318  -14.271 1.00 24.14 ? 779  ALA   A N   1 
ATOM   2674 C  CA  . ALA   A 1 338 ? 12.646  17.769  -15.060 1.00 21.72 ? 779  ALA   A CA  1 
ATOM   2675 C  C   . ALA   A 1 338 ? 13.931  18.545  -14.834 1.00 20.57 ? 779  ALA   A C   1 
ATOM   2676 O  O   . ALA   A 1 338 ? 15.015  17.960  -14.780 1.00 21.41 ? 779  ALA   A O   1 
ATOM   2677 C  CB  . ALA   A 1 338 ? 12.283  17.758  -16.541 1.00 21.67 ? 779  ALA   A CB  1 
ATOM   2678 N  N   . THR   A 1 339 ? 13.835  19.864  -14.693 1.00 25.91 ? 780  THR   A N   1 
ATOM   2679 C  CA  . THR   A 1 339 ? 15.044  20.648  -14.484 1.00 19.82 ? 780  THR   A CA  1 
ATOM   2680 C  C   . THR   A 1 339 ? 15.677  20.326  -13.134 1.00 21.67 ? 780  THR   A C   1 
ATOM   2681 O  O   . THR   A 1 339 ? 16.906  20.273  -13.016 1.00 25.11 ? 780  THR   A O   1 
ATOM   2682 C  CB  . THR   A 1 339 ? 14.712  22.134  -14.633 1.00 34.87 ? 780  THR   A CB  1 
ATOM   2683 O  OG1 . THR   A 1 339 ? 14.406  22.405  -16.010 1.00 30.60 ? 780  THR   A OG1 1 
ATOM   2684 C  CG2 . THR   A 1 339 ? 15.875  23.003  -14.187 1.00 24.49 ? 780  THR   A CG2 1 
ATOM   2685 N  N   . VAL   A 1 340 ? 14.848  20.072  -12.124 1.00 22.57 ? 781  VAL   A N   1 
ATOM   2686 C  CA  . VAL   A 1 340 ? 15.355  19.637  -10.823 1.00 25.87 ? 781  VAL   A CA  1 
ATOM   2687 C  C   . VAL   A 1 340 ? 16.189  18.367  -10.975 1.00 24.76 ? 781  VAL   A C   1 
ATOM   2688 O  O   . VAL   A 1 340 ? 17.320  18.284  -10.485 1.00 25.34 ? 781  VAL   A O   1 
ATOM   2689 C  CB  . VAL   A 1 340 ? 14.189  19.446  -9.838  1.00 23.32 ? 781  VAL   A CB  1 
ATOM   2690 C  CG1 . VAL   A 1 340 ? 14.694  18.855  -8.528  1.00 31.82 ? 781  VAL   A CG1 1 
ATOM   2691 C  CG2 . VAL   A 1 340 ? 13.472  20.780  -9.583  1.00 26.18 ? 781  VAL   A CG2 1 
ATOM   2692 N  N   . SER   A 1 341 ? 15.651  17.366  -11.684 1.00 22.02 ? 782  SER   A N   1 
ATOM   2693 C  CA  . SER   A 1 341 ? 16.402  16.129  -11.902 1.00 21.76 ? 782  SER   A CA  1 
ATOM   2694 C  C   . SER   A 1 341 ? 17.710  16.397  -12.629 1.00 24.94 ? 782  SER   A C   1 
ATOM   2695 O  O   . SER   A 1 341 ? 18.754  15.841  -12.273 1.00 22.46 ? 782  SER   A O   1 
ATOM   2696 C  CB  . SER   A 1 341 ? 15.566  15.123  -12.695 1.00 23.77 ? 782  SER   A CB  1 
ATOM   2697 O  OG  . SER   A 1 341 ? 14.425  14.693  -11.978 1.00 22.88 ? 782  SER   A OG  1 
ATOM   2698 N  N   . ILE   A 1 342 ? 17.668  17.219  -13.682 1.00 20.88 ? 783  ILE   A N   1 
ATOM   2699 C  CA  . ILE   A 1 342 ? 18.875  17.488  -14.458 1.00 26.01 ? 783  ILE   A CA  1 
ATOM   2700 C  C   . ILE   A 1 342 ? 19.934  18.136  -13.576 1.00 19.77 ? 783  ILE   A C   1 
ATOM   2701 O  O   . ILE   A 1 342 ? 21.114  17.775  -13.622 1.00 21.57 ? 783  ILE   A O   1 
ATOM   2702 C  CB  . ILE   A 1 342 ? 18.542  18.339  -15.700 1.00 22.40 ? 783  ILE   A CB  1 
ATOM   2703 C  CG1 . ILE   A 1 342 ? 17.695  17.517  -16.684 1.00 21.66 ? 783  ILE   A CG1 1 
ATOM   2704 C  CG2 . ILE   A 1 342 ? 19.816  18.846  -16.360 1.00 26.69 ? 783  ILE   A CG2 1 
ATOM   2705 C  CD1 . ILE   A 1 342 ? 17.241  18.290  -17.916 1.00 22.80 ? 783  ILE   A CD1 1 
ATOM   2706 N  N   . ASN   A 1 343 ? 19.511  19.075  -12.727 1.00 26.80 ? 784  ASN   A N   1 
ATOM   2707 C  CA  . ASN   A 1 343 ? 20.456  19.763  -11.857 1.00 24.50 ? 784  ASN   A CA  1 
ATOM   2708 C  C   . ASN   A 1 343 ? 21.054  18.820  -10.815 1.00 23.75 ? 784  ASN   A C   1 
ATOM   2709 O  O   . ASN   A 1 343 ? 22.235  18.947  -10.483 1.00 25.58 ? 784  ASN   A O   1 
ATOM   2710 C  CB  . ASN   A 1 343 ? 19.777  20.976  -11.215 1.00 27.02 ? 784  ASN   A CB  1 
ATOM   2711 C  CG  . ASN   A 1 343 ? 19.579  22.118  -12.205 1.00 24.41 ? 784  ASN   A CG  1 
ATOM   2712 O  OD1 . ASN   A 1 343 ? 20.328  22.244  -13.174 1.00 28.60 ? 784  ASN   A OD1 1 
ATOM   2713 N  ND2 . ASN   A 1 343 ? 18.564  22.945  -11.966 1.00 30.91 ? 784  ASN   A ND2 1 
ATOM   2714 N  N   . ASN   A 1 344 ? 20.272  17.856  -10.316 1.00 25.30 ? 785  ASN   A N   1 
ATOM   2715 C  CA  . ASN   A 1 344 ? 20.829  16.865  -9.392  1.00 21.41 ? 785  ASN   A CA  1 
ATOM   2716 C  C   . ASN   A 1 344 ? 21.878  15.987  -10.069 1.00 25.63 ? 785  ASN   A C   1 
ATOM   2717 O  O   . ASN   A 1 344 ? 22.922  15.689  -9.476  1.00 24.78 ? 785  ASN   A O   1 
ATOM   2718 C  CB  . ASN   A 1 344 ? 19.716  16.030  -8.772  1.00 24.10 ? 785  ASN   A CB  1 
ATOM   2719 C  CG  . ASN   A 1 344 ? 18.974  16.778  -7.694  1.00 29.40 ? 785  ASN   A CG  1 
ATOM   2720 O  OD1 . ASN   A 1 344 ? 19.566  17.584  -6.975  1.00 38.31 ? 785  ASN   A OD1 1 
ATOM   2721 N  ND2 . ASN   A 1 344 ? 17.684  16.516  -7.565  1.00 32.29 ? 785  ASN   A ND2 1 
ATOM   2722 N  N   . VAL   A 1 345 ? 21.636  15.565  -11.311 1.00 20.75 ? 786  VAL   A N   1 
ATOM   2723 C  CA  . VAL   A 1 345 ? 22.629  14.757  -12.000 1.00 19.86 ? 786  VAL   A CA  1 
ATOM   2724 C  C   . VAL   A 1 345 ? 23.892  15.566  -12.251 1.00 25.42 ? 786  VAL   A C   1 
ATOM   2725 O  O   . VAL   A 1 345 ? 25.012  15.049  -12.138 1.00 24.45 ? 786  VAL   A O   1 
ATOM   2726 C  CB  . VAL   A 1 345 ? 22.055  14.190  -13.313 1.00 21.38 ? 786  VAL   A CB  1 
ATOM   2727 C  CG1 . VAL   A 1 345 ? 23.093  13.310  -13.981 1.00 21.85 ? 786  VAL   A CG1 1 
ATOM   2728 C  CG2 . VAL   A 1 345 ? 20.768  13.431  -13.054 1.00 21.59 ? 786  VAL   A CG2 1 
ATOM   2729 N  N   . LEU   A 1 346 ? 23.729  16.838  -12.638 1.00 22.70 ? 787  LEU   A N   1 
ATOM   2730 C  CA  . LEU   A 1 346 ? 24.882  17.699  -12.870 1.00 24.78 ? 787  LEU   A CA  1 
ATOM   2731 C  C   . LEU   A 1 346 ? 25.763  17.796  -11.630 1.00 22.87 ? 787  LEU   A C   1 
ATOM   2732 O  O   . LEU   A 1 346 ? 26.994  17.753  -11.737 1.00 25.98 ? 787  LEU   A O   1 
ATOM   2733 C  CB  . LEU   A 1 346 ? 24.409  19.089  -13.303 1.00 27.74 ? 787  LEU   A CB  1 
ATOM   2734 C  CG  . LEU   A 1 346 ? 23.992  19.255  -14.765 1.00 30.63 ? 787  LEU   A CG  1 
ATOM   2735 C  CD1 . LEU   A 1 346 ? 23.157  20.521  -14.936 1.00 30.07 ? 787  LEU   A CD1 1 
ATOM   2736 C  CD2 . LEU   A 1 346 ? 25.216  19.281  -15.656 1.00 31.04 ? 787  LEU   A CD2 1 
ATOM   2737 N  N   . ARG   A 1 347 ? 25.149  17.932  -10.454 1.00 23.77 ? 788  ARG   A N   1 
ATOM   2738 C  CA  . ARG   A 1 347 ? 25.927  17.996  -9.217  1.00 24.40 ? 788  ARG   A CA  1 
ATOM   2739 C  C   . ARG   A 1 347 ? 26.649  16.680  -8.950  1.00 34.72 ? 788  ARG   A C   1 
ATOM   2740 O  O   . ARG   A 1 347 ? 27.813  16.675  -8.531  1.00 28.19 ? 788  ARG   A O   1 
ATOM   2741 C  CB  . ARG   A 1 347 ? 25.025  18.365  -8.041  1.00 27.53 ? 788  ARG   A CB  1 
ATOM   2742 C  CG  . ARG   A 1 347 ? 24.833  19.862  -7.855  1.00 45.78 ? 788  ARG   A CG  1 
ATOM   2743 C  CD  . ARG   A 1 347 ? 24.065  20.188  -6.575  1.00 42.15 ? 788  ARG   A CD  1 
ATOM   2744 N  NE  . ARG   A 1 347 ? 22.623  19.985  -6.718  1.00 59.11 ? 788  ARG   A NE  1 
ATOM   2745 C  CZ  . ARG   A 1 347 ? 21.796  20.820  -7.347  1.00 52.53 ? 788  ARG   A CZ  1 
ATOM   2746 N  NH1 . ARG   A 1 347 ? 22.254  21.936  -7.911  1.00 45.86 ? 788  ARG   A NH1 1 
ATOM   2747 N  NH2 . ARG   A 1 347 ? 20.503  20.534  -7.413  1.00 36.16 ? 788  ARG   A NH2 1 
ATOM   2748 N  N   . ALA   A 1 348 ? 25.977  15.557  -9.205  1.00 36.65 ? 789  ALA   A N   1 
ATOM   2749 C  CA  . ALA   A 1 348 ? 26.567  14.247  -8.951  1.00 23.87 ? 789  ALA   A CA  1 
ATOM   2750 C  C   . ALA   A 1 348 ? 27.753  13.957  -9.860  1.00 23.74 ? 789  ALA   A C   1 
ATOM   2751 O  O   . ALA   A 1 348 ? 28.684  13.254  -9.454  1.00 25.87 ? 789  ALA   A O   1 
ATOM   2752 C  CB  . ALA   A 1 348 ? 25.501  13.165  -9.128  1.00 26.81 ? 789  ALA   A CB  1 
ATOM   2753 N  N   . HIS   A 1 349 ? 27.742  14.458  -11.097 1.00 20.02 ? 790  HIS   A N   1 
ATOM   2754 C  CA  . HIS   A 1 349 ? 28.742  14.069  -12.072 1.00 20.36 ? 790  HIS   A CA  1 
ATOM   2755 C  C   . HIS   A 1 349 ? 29.764  15.145  -12.396 1.00 20.36 ? 790  HIS   A C   1 
ATOM   2756 O  O   . HIS   A 1 349 ? 30.733  14.852  -13.100 1.00 24.77 ? 790  HIS   A O   1 
ATOM   2757 C  CB  . HIS   A 1 349 ? 28.081  13.533  -13.350 1.00 20.96 ? 790  HIS   A CB  1 
ATOM   2758 C  CG  . HIS   A 1 349 ? 27.641  12.119  -13.201 1.00 19.32 ? 790  HIS   A CG  1 
ATOM   2759 N  ND1 . HIS   A 1 349 ? 28.500  11.061  -13.401 1.00 22.92 ? 790  HIS   A ND1 1 
ATOM   2760 C  CD2 . HIS   A 1 349 ? 26.467  11.588  -12.790 1.00 24.89 ? 790  HIS   A CD2 1 
ATOM   2761 C  CE1 . HIS   A 1 349 ? 27.860  9.935   -13.143 1.00 17.29 ? 790  HIS   A CE1 1 
ATOM   2762 N  NE2 . HIS   A 1 349 ? 26.626  10.225  -12.780 1.00 21.61 ? 790  HIS   A NE2 1 
ATOM   2763 N  N   . ALA   A 1 350 ? 29.560  16.368  -11.913 1.00 36.04 ? 791  ALA   A N   1 
ATOM   2764 C  CA  . ALA   A 1 350 ? 30.599  17.389  -11.999 1.00 36.24 ? 791  ALA   A CA  1 
ATOM   2765 C  C   . ALA   A 1 350 ? 31.964  16.916  -11.504 1.00 30.11 ? 791  ALA   A C   1 
ATOM   2766 O  O   . ALA   A 1 350 ? 32.968  17.255  -12.152 1.00 35.10 ? 791  ALA   A O   1 
ATOM   2767 C  CB  . ALA   A 1 350 ? 30.133  18.673  -11.296 1.00 40.25 ? 791  ALA   A CB  1 
ATOM   2768 N  N   . PRO   A 1 351 ? 32.081  16.145  -10.412 1.00 29.54 ? 792  PRO   A N   1 
ATOM   2769 C  CA  . PRO   A 1 351 ? 33.410  15.638  -10.023 1.00 24.94 ? 792  PRO   A CA  1 
ATOM   2770 C  C   . PRO   A 1 351 ? 34.131  14.855  -11.106 1.00 30.99 ? 792  PRO   A C   1 
ATOM   2771 O  O   . PRO   A 1 351 ? 35.367  14.864  -11.133 1.00 38.93 ? 792  PRO   A O   1 
ATOM   2772 C  CB  . PRO   A 1 351 ? 33.104  14.766  -8.798  1.00 29.77 ? 792  PRO   A CB  1 
ATOM   2773 C  CG  . PRO   A 1 351 ? 31.919  15.413  -8.180  1.00 29.56 ? 792  PRO   A CG  1 
ATOM   2774 C  CD  . PRO   A 1 351 ? 31.080  15.886  -9.360  1.00 28.71 ? 792  PRO   A CD  1 
ATOM   2775 N  N   . PHE   A 1 352 ? 33.406  14.189  -12.012 1.00 21.67 ? 793  PHE   A N   1 
ATOM   2776 C  CA  . PHE   A 1 352 ? 34.007  13.238  -12.931 1.00 22.67 ? 793  PHE   A CA  1 
ATOM   2777 C  C   . PHE   A 1 352 ? 34.111  13.719  -14.376 1.00 25.49 ? 793  PHE   A C   1 
ATOM   2778 O  O   . PHE   A 1 352 ? 34.881  13.134  -15.146 1.00 31.48 ? 793  PHE   A O   1 
ATOM   2779 C  CB  . PHE   A 1 352 ? 33.255  11.896  -12.867 1.00 23.11 ? 793  PHE   A CB  1 
ATOM   2780 C  CG  . PHE   A 1 352 ? 32.915  11.463  -11.466 1.00 21.91 ? 793  PHE   A CG  1 
ATOM   2781 C  CD1 . PHE   A 1 352 ? 33.888  10.893  -10.657 1.00 24.67 ? 793  PHE   A CD1 1 
ATOM   2782 C  CD2 . PHE   A 1 352 ? 31.648  11.640  -10.950 1.00 22.25 ? 793  PHE   A CD2 1 
ATOM   2783 C  CE1 . PHE   A 1 352 ? 33.590  10.504  -9.355  1.00 25.94 ? 793  PHE   A CE1 1 
ATOM   2784 C  CE2 . PHE   A 1 352 ? 31.339  11.252  -9.658  1.00 26.94 ? 793  PHE   A CE2 1 
ATOM   2785 C  CZ  . PHE   A 1 352 ? 32.318  10.685  -8.856  1.00 25.07 ? 793  PHE   A CZ  1 
ATOM   2786 N  N   . TRP   A 1 353 ? 33.364  14.757  -14.769 1.00 32.79 ? 794  TRP   A N   1 
ATOM   2787 C  CA  . TRP   A 1 353 ? 33.297  15.200  -16.162 1.00 29.91 ? 794  TRP   A CA  1 
ATOM   2788 C  C   . TRP   A 1 353 ? 33.544  16.704  -16.222 1.00 23.47 ? 794  TRP   A C   1 
ATOM   2789 O  O   . TRP   A 1 353 ? 32.691  17.492  -15.801 1.00 28.85 ? 794  TRP   A O   1 
ATOM   2790 C  CB  . TRP   A 1 353 ? 31.945  14.825  -16.784 1.00 26.59 ? 794  TRP   A CB  1 
ATOM   2791 C  CG  . TRP   A 1 353 ? 31.705  13.353  -16.690 1.00 21.20 ? 794  TRP   A CG  1 
ATOM   2792 C  CD1 . TRP   A 1 353 ? 30.916  12.709  -15.782 1.00 19.56 ? 794  TRP   A CD1 1 
ATOM   2793 C  CD2 . TRP   A 1 353 ? 32.285  12.344  -17.506 1.00 19.19 ? 794  TRP   A CD2 1 
ATOM   2794 N  NE1 . TRP   A 1 353 ? 30.969  11.352  -15.987 1.00 19.81 ? 794  TRP   A NE1 1 
ATOM   2795 C  CE2 . TRP   A 1 353 ? 31.797  11.099  -17.043 1.00 19.49 ? 794  TRP   A CE2 1 
ATOM   2796 C  CE3 . TRP   A 1 353 ? 33.168  12.362  -18.589 1.00 24.69 ? 794  TRP   A CE3 1 
ATOM   2797 C  CZ2 . TRP   A 1 353 ? 32.163  9.891   -17.629 1.00 20.93 ? 794  TRP   A CZ2 1 
ATOM   2798 C  CZ3 . TRP   A 1 353 ? 33.529  11.158  -19.177 1.00 26.76 ? 794  TRP   A CZ3 1 
ATOM   2799 C  CH2 . TRP   A 1 353 ? 33.031  9.937   -18.689 1.00 26.19 ? 794  TRP   A CH2 1 
ATOM   2800 N  N   . SER   A 1 354 ? 34.707  17.093  -16.750 1.00 29.44 ? 795  SER   A N   1 
ATOM   2801 C  CA  A SER   A 1 354 ? 35.054  18.509  -16.801 0.34 29.21 ? 795  SER   A CA  1 
ATOM   2802 C  CA  B SER   A 1 354 ? 35.060  18.509  -16.807 0.66 29.28 ? 795  SER   A CA  1 
ATOM   2803 C  C   . SER   A 1 354 ? 34.114  19.296  -17.707 1.00 41.24 ? 795  SER   A C   1 
ATOM   2804 O  O   . SER   A 1 354 ? 33.877  20.484  -17.463 1.00 45.21 ? 795  SER   A O   1 
ATOM   2805 C  CB  A SER   A 1 354 ? 36.508  18.682  -17.234 0.34 29.68 ? 795  SER   A CB  1 
ATOM   2806 C  CB  B SER   A 1 354 ? 36.516  18.687  -17.244 0.66 27.63 ? 795  SER   A CB  1 
ATOM   2807 O  OG  A SER   A 1 354 ? 37.390  18.225  -16.222 0.34 31.55 ? 795  SER   A OG  1 
ATOM   2808 O  OG  B SER   A 1 354 ? 36.737  18.232  -18.571 0.66 30.37 ? 795  SER   A OG  1 
ATOM   2809 N  N   . SER   A 1 355 ? 33.559  18.657  -18.740 1.00 40.87 ? 796  SER   A N   1 
ATOM   2810 C  CA  . SER   A 1 355 ? 32.631  19.347  -19.632 1.00 33.74 ? 796  SER   A CA  1 
ATOM   2811 C  C   . SER   A 1 355 ? 31.366  19.816  -18.925 1.00 36.00 ? 796  SER   A C   1 
ATOM   2812 O  O   . SER   A 1 355 ? 30.606  20.597  -19.510 1.00 40.53 ? 796  SER   A O   1 
ATOM   2813 C  CB  . SER   A 1 355 ? 32.263  18.450  -20.813 1.00 33.30 ? 796  SER   A CB  1 
ATOM   2814 O  OG  . SER   A 1 355 ? 31.404  17.407  -20.397 1.00 38.01 ? 796  SER   A OG  1 
ATOM   2815 N  N   . LEU   A 1 356 ? 31.116  19.362  -17.697 1.00 27.55 ? 797  LEU   A N   1 
ATOM   2816 C  CA  . LEU   A 1 356 ? 29.962  19.794  -16.926 1.00 24.85 ? 797  LEU   A CA  1 
ATOM   2817 C  C   . LEU   A 1 356 ? 30.274  20.923  -15.957 1.00 44.09 ? 797  LEU   A C   1 
ATOM   2818 O  O   . LEU   A 1 356 ? 29.350  21.439  -15.319 1.00 33.60 ? 797  LEU   A O   1 
ATOM   2819 C  CB  . LEU   A 1 356 ? 29.380  18.625  -16.118 1.00 36.35 ? 797  LEU   A CB  1 
ATOM   2820 C  CG  . LEU   A 1 356 ? 28.957  17.358  -16.860 1.00 39.47 ? 797  LEU   A CG  1 
ATOM   2821 C  CD1 . LEU   A 1 356 ? 28.530  16.289  -15.851 1.00 30.58 ? 797  LEU   A CD1 1 
ATOM   2822 C  CD2 . LEU   A 1 356 ? 27.841  17.649  -17.857 1.00 26.05 ? 797  LEU   A CD2 1 
ATOM   2823 N  N   . ARG   A 1 357 ? 31.539  21.300  -15.819 1.00 42.98 ? 798  ARG   A N   1 
ATOM   2824 C  CA  . ARG   A 1 357 ? 31.944  22.303  -14.843 1.00 54.40 ? 798  ARG   A CA  1 
ATOM   2825 C  C   . ARG   A 1 357 ? 31.857  23.714  -15.412 1.00 61.54 ? 798  ARG   A C   1 
ATOM   2826 O  O   . ARG   A 1 357 ? 32.045  23.925  -16.612 1.00 55.47 ? 798  ARG   A O   1 
ATOM   2827 C  CB  . ARG   A 1 357 ? 33.367  22.020  -14.364 1.00 43.81 ? 798  ARG   A CB  1 
ATOM   2828 C  CG  . ARG   A 1 357 ? 33.461  20.894  -13.354 1.00 40.30 ? 798  ARG   A CG  1 
ATOM   2829 C  CD  . ARG   A 1 357 ? 34.768  20.146  -13.514 1.00 38.77 ? 798  ARG   A CD  1 
ATOM   2830 N  NE  . ARG   A 1 357 ? 35.150  19.454  -12.291 1.00 51.03 ? 798  ARG   A NE  1 
ATOM   2831 C  CZ  . ARG   A 1 357 ? 36.050  18.480  -12.237 1.00 64.11 ? 798  ARG   A CZ  1 
ATOM   2832 N  NH1 . ARG   A 1 357 ? 36.667  18.082  -13.344 1.00 59.86 ? 798  ARG   A NH1 1 
ATOM   2833 N  NH2 . ARG   A 1 357 ? 36.333  17.909  -11.074 1.00 45.98 ? 798  ARG   A NH2 1 
ATOM   2834 O  OXT . ARG   A 1 357 ? 31.603  24.674  -14.679 1.00 51.93 ? 798  ARG   A OXT 1 
ATOM   2835 N  N   . PRO   B 1 1   ? -27.527 5.471   -27.589 1.00 45.24 ? 442  PRO   B N   1 
ATOM   2836 C  CA  . PRO   B 1 1   ? -27.372 4.691   -28.820 1.00 55.43 ? 442  PRO   B CA  1 
ATOM   2837 C  C   . PRO   B 1 1   ? -26.162 3.762   -28.768 1.00 55.44 ? 442  PRO   B C   1 
ATOM   2838 O  O   . PRO   B 1 1   ? -25.120 4.127   -28.231 1.00 34.05 ? 442  PRO   B O   1 
ATOM   2839 C  CB  . PRO   B 1 1   ? -27.168 5.768   -29.888 1.00 52.53 ? 442  PRO   B CB  1 
ATOM   2840 C  CG  . PRO   B 1 1   ? -26.516 6.890   -29.166 1.00 48.43 ? 442  PRO   B CG  1 
ATOM   2841 C  CD  . PRO   B 1 1   ? -26.978 6.832   -27.723 1.00 50.60 ? 442  PRO   B CD  1 
ATOM   2842 N  N   . ILE   B 1 2   ? -26.305 2.571   -29.338 1.00 41.84 ? 443  ILE   B N   1 
ATOM   2843 C  CA  . ILE   B 1 2   ? -25.275 1.539   -29.303 1.00 27.92 ? 443  ILE   B CA  1 
ATOM   2844 C  C   . ILE   B 1 2   ? -24.687 1.396   -30.702 1.00 21.62 ? 443  ILE   B C   1 
ATOM   2845 O  O   . ILE   B 1 2   ? -25.414 1.508   -31.696 1.00 22.75 ? 443  ILE   B O   1 
ATOM   2846 C  CB  . ILE   B 1 2   ? -25.910 0.214   -28.840 1.00 22.44 ? 443  ILE   B CB  1 
ATOM   2847 C  CG1 . ILE   B 1 2   ? -26.464 0.348   -27.421 1.00 40.47 ? 443  ILE   B CG1 1 
ATOM   2848 C  CG2 . ILE   B 1 2   ? -24.916 -0.924  -28.927 1.00 28.63 ? 443  ILE   B CG2 1 
ATOM   2849 C  CD1 . ILE   B 1 2   ? -27.417 -0.760  -27.044 1.00 50.36 ? 443  ILE   B CD1 1 
ATOM   2850 N  N   . THR   B 1 3   ? -23.370 1.164   -30.779 1.00 16.80 ? 444  THR   B N   1 
ATOM   2851 C  CA  . THR   B 1 3   ? -22.680 0.874   -32.041 1.00 16.12 ? 444  THR   B CA  1 
ATOM   2852 C  C   . THR   B 1 3   ? -22.263 -0.590  -32.038 1.00 16.58 ? 444  THR   B C   1 
ATOM   2853 O  O   . THR   B 1 3   ? -21.574 -1.037  -31.120 1.00 16.96 ? 444  THR   B O   1 
ATOM   2854 C  CB  . THR   B 1 3   ? -21.418 1.744   -32.203 1.00 13.90 ? 444  THR   B CB  1 
ATOM   2855 O  OG1 . THR   B 1 3   ? -21.800 3.121   -32.313 1.00 17.65 ? 444  THR   B OG1 1 
ATOM   2856 C  CG2 . THR   B 1 3   ? -20.627 1.353   -33.438 1.00 15.15 ? 444  THR   B CG2 1 
ATOM   2857 N  N   . GLY   B 1 4   ? -22.671 -1.338  -33.061 1.00 13.43 ? 445  GLY   B N   1 
ATOM   2858 C  CA  . GLY   B 1 4   ? -22.230 -2.716  -33.203 1.00 14.67 ? 445  GLY   B CA  1 
ATOM   2859 C  C   . GLY   B 1 4   ? -20.889 -2.828  -33.923 1.00 15.60 ? 445  GLY   B C   1 
ATOM   2860 O  O   . GLY   B 1 4   ? -20.522 -1.978  -34.727 1.00 14.12 ? 445  GLY   B O   1 
ATOM   2861 N  N   . LEU   B 1 5   ? -20.167 -3.901  -33.625 1.00 14.41 ? 446  LEU   B N   1 
ATOM   2862 C  CA  . LEU   B 1 5   ? -18.923 -4.208  -34.322 1.00 12.95 ? 446  LEU   B CA  1 
ATOM   2863 C  C   . LEU   B 1 5   ? -18.863 -5.707  -34.560 1.00 14.19 ? 446  LEU   B C   1 
ATOM   2864 O  O   . LEU   B 1 5   ? -19.066 -6.498  -33.630 1.00 13.73 ? 446  LEU   B O   1 
ATOM   2865 C  CB  . LEU   B 1 5   ? -17.706 -3.721  -33.515 1.00 14.00 ? 446  LEU   B CB  1 
ATOM   2866 C  CG  . LEU   B 1 5   ? -16.314 -3.953  -34.120 1.00 14.59 ? 446  LEU   B CG  1 
ATOM   2867 C  CD1 . LEU   B 1 5   ? -15.362 -2.874  -33.618 1.00 15.25 ? 446  LEU   B CD1 1 
ATOM   2868 C  CD2 . LEU   B 1 5   ? -15.784 -5.343  -33.785 1.00 14.60 ? 446  LEU   B CD2 1 
ATOM   2869 N  N   . VAL   B 1 6   ? -18.583 -6.106  -35.803 1.00 12.83 ? 447  VAL   B N   1 
ATOM   2870 C  CA  . VAL   B 1 6   ? -18.388 -7.512  -36.125 1.00 12.30 ? 447  VAL   B CA  1 
ATOM   2871 C  C   . VAL   B 1 6   ? -16.972 -7.711  -36.660 1.00 14.15 ? 447  VAL   B C   1 
ATOM   2872 O  O   . VAL   B 1 6   ? -16.504 -6.946  -37.518 1.00 12.63 ? 447  VAL   B O   1 
ATOM   2873 C  CB  . VAL   B 1 6   ? -19.481 -8.084  -37.059 1.00 15.68 ? 447  VAL   B CB  1 
ATOM   2874 C  CG1 . VAL   B 1 6   ? -19.615 -7.306  -38.350 1.00 15.46 ? 447  VAL   B CG1 1 
ATOM   2875 C  CG2 . VAL   B 1 6   ? -19.226 -9.557  -37.323 1.00 16.66 ? 447  VAL   B CG2 1 
ATOM   2876 N  N   . TYR   B 1 7   ? -16.273 -8.690  -36.097 1.00 13.94 ? 448  TYR   B N   1 
ATOM   2877 C  CA  . TYR   B 1 7   ? -14.946 -9.089  -36.537 1.00 15.67 ? 448  TYR   B CA  1 
ATOM   2878 C  C   . TYR   B 1 7   ? -14.769 -10.560 -36.185 1.00 17.06 ? 448  TYR   B C   1 
ATOM   2879 O  O   . TYR   B 1 7   ? -15.103 -10.968 -35.073 1.00 17.93 ? 448  TYR   B O   1 
ATOM   2880 C  CB  . TYR   B 1 7   ? -13.861 -8.282  -35.826 1.00 16.09 ? 448  TYR   B CB  1 
ATOM   2881 C  CG  . TYR   B 1 7   ? -12.496 -8.899  -36.042 1.00 16.60 ? 448  TYR   B CG  1 
ATOM   2882 C  CD1 . TYR   B 1 7   ? -11.861 -8.801  -37.273 1.00 14.11 ? 448  TYR   B CD1 1 
ATOM   2883 C  CD2 . TYR   B 1 7   ? -11.875 -9.639  -35.048 1.00 16.40 ? 448  TYR   B CD2 1 
ATOM   2884 C  CE1 . TYR   B 1 7   ? -10.627 -9.369  -37.500 1.00 15.62 ? 448  TYR   B CE1 1 
ATOM   2885 C  CE2 . TYR   B 1 7   ? -10.637 -10.217 -35.260 1.00 16.38 ? 448  TYR   B CE2 1 
ATOM   2886 C  CZ  . TYR   B 1 7   ? -10.018 -10.085 -36.503 1.00 14.51 ? 448  TYR   B CZ  1 
ATOM   2887 O  OH  . TYR   B 1 7   ? -8.779  -10.657 -36.729 1.00 19.74 ? 448  TYR   B OH  1 
ATOM   2888 N  N   . ASP   B 1 8   ? -14.279 -11.364 -37.128 1.00 16.20 ? 449  ASP   B N   1 
ATOM   2889 C  CA  . ASP   B 1 8   ? -14.051 -12.777 -36.848 1.00 16.78 ? 449  ASP   B CA  1 
ATOM   2890 C  C   . ASP   B 1 8   ? -12.744 -13.201 -37.498 1.00 16.74 ? 449  ASP   B C   1 
ATOM   2891 O  O   . ASP   B 1 8   ? -12.592 -13.071 -38.715 1.00 18.42 ? 449  ASP   B O   1 
ATOM   2892 C  CB  . ASP   B 1 8   ? -15.253 -13.621 -37.310 1.00 18.83 ? 449  ASP   B CB  1 
ATOM   2893 C  CG  . ASP   B 1 8   ? -15.220 -15.041 -36.772 1.00 27.49 ? 449  ASP   B CG  1 
ATOM   2894 O  OD1 . ASP   B 1 8   ? -14.196 -15.716 -36.937 1.00 20.08 ? 449  ASP   B OD1 1 
ATOM   2895 O  OD2 . ASP   B 1 8   ? -16.215 -15.488 -36.162 1.00 24.42 ? 449  ASP   B OD2 1 
ATOM   2896 N  N   A GLN   B 1 9   ? -11.792 -13.664 -36.682 0.66 15.88 ? 450  GLN   B N   1 
ATOM   2897 N  N   B GLN   B 1 9   ? -11.826 -13.738 -36.688 0.34 17.15 ? 450  GLN   B N   1 
ATOM   2898 C  CA  A GLN   B 1 9   ? -10.458 -13.978 -37.187 0.66 17.58 ? 450  GLN   B CA  1 
ATOM   2899 C  CA  B GLN   B 1 9   ? -10.510 -14.139 -37.183 0.34 16.90 ? 450  GLN   B CA  1 
ATOM   2900 C  C   A GLN   B 1 9   ? -10.461 -15.105 -38.217 0.66 16.59 ? 450  GLN   B C   1 
ATOM   2901 C  C   B GLN   B 1 9   ? -10.600 -15.177 -38.302 0.34 15.23 ? 450  GLN   B C   1 
ATOM   2902 O  O   A GLN   B 1 9   ? -9.472  -15.264 -38.936 0.66 19.77 ? 450  GLN   B O   1 
ATOM   2903 O  O   B GLN   B 1 9   ? -9.686  -15.274 -39.129 0.34 11.27 ? 450  GLN   B O   1 
ATOM   2904 C  CB  A GLN   B 1 9   ? -9.492  -14.275 -36.034 0.66 23.98 ? 450  GLN   B CB  1 
ATOM   2905 C  CB  B GLN   B 1 9   ? -9.654  -14.652 -36.020 0.34 21.00 ? 450  GLN   B CB  1 
ATOM   2906 C  CG  A GLN   B 1 9   ? -9.737  -15.605 -35.353 0.66 22.92 ? 450  GLN   B CG  1 
ATOM   2907 C  CG  B GLN   B 1 9   ? -8.172  -14.791 -36.329 0.34 17.78 ? 450  GLN   B CG  1 
ATOM   2908 C  CD  A GLN   B 1 9   ? -8.848  -15.812 -34.137 0.66 36.46 ? 450  GLN   B CD  1 
ATOM   2909 C  CD  B GLN   B 1 9   ? -7.811  -16.171 -36.843 0.34 26.81 ? 450  GLN   B CD  1 
ATOM   2910 O  OE1 A GLN   B 1 9   ? -8.206  -14.879 -33.658 0.66 34.03 ? 450  GLN   B OE1 1 
ATOM   2911 O  OE1 B GLN   B 1 9   ? -8.358  -17.176 -36.391 0.34 22.42 ? 450  GLN   B OE1 1 
ATOM   2912 N  NE2 A GLN   B 1 9   ? -8.817  -17.038 -33.627 0.66 47.58 ? 450  GLN   B NE2 1 
ATOM   2913 N  NE2 B GLN   B 1 9   ? -6.885  -16.227 -37.793 0.34 20.26 ? 450  GLN   B NE2 1 
ATOM   2914 N  N   A ARG   B 1 10  ? -11.540 -15.890 -38.305 0.66 17.18 ? 451  ARG   B N   1 
ATOM   2915 N  N   B ARG   B 1 10  ? -11.688 -15.952 -38.357 0.34 15.37 ? 451  ARG   B N   1 
ATOM   2916 C  CA  A ARG   B 1 10  ? -11.622 -16.925 -39.333 0.66 19.94 ? 451  ARG   B CA  1 
ATOM   2917 C  CA  B ARG   B 1 10  ? -11.818 -16.987 -39.380 0.34 17.64 ? 451  ARG   B CA  1 
ATOM   2918 C  C   A ARG   B 1 10  ? -11.509 -16.342 -40.742 0.66 15.37 ? 451  ARG   B C   1 
ATOM   2919 C  C   B ARG   B 1 10  ? -11.813 -16.421 -40.798 0.34 12.53 ? 451  ARG   B C   1 
ATOM   2920 O  O   A ARG   B 1 10  ? -10.979 -17.007 -41.644 0.66 16.60 ? 451  ARG   B O   1 
ATOM   2921 O  O   B ARG   B 1 10  ? -11.631 -17.180 -41.756 0.34 12.69 ? 451  ARG   B O   1 
ATOM   2922 C  CB  A ARG   B 1 10  ? -12.921 -17.720 -39.185 0.66 21.14 ? 451  ARG   B CB  1 
ATOM   2923 C  CB  B ARG   B 1 10  ? -13.081 -17.814 -39.138 0.34 19.90 ? 451  ARG   B CB  1 
ATOM   2924 C  CG  A ARG   B 1 10  ? -12.956 -18.648 -37.973 0.66 18.60 ? 451  ARG   B CG  1 
ATOM   2925 C  CG  B ARG   B 1 10  ? -13.066 -18.591 -37.831 0.34 18.28 ? 451  ARG   B CG  1 
ATOM   2926 C  CD  A ARG   B 1 10  ? -14.289 -19.357 -37.843 0.66 20.17 ? 451  ARG   B CD  1 
ATOM   2927 C  CD  B ARG   B 1 10  ? -13.919 -19.833 -37.935 0.34 23.57 ? 451  ARG   B CD  1 
ATOM   2928 N  NE  A ARG   B 1 10  ? -15.365 -18.466 -37.431 0.66 16.92 ? 451  ARG   B NE  1 
ATOM   2929 N  NE  B ARG   B 1 10  ? -13.807 -20.439 -39.257 0.34 32.47 ? 451  ARG   B NE  1 
ATOM   2930 C  CZ  A ARG   B 1 10  ? -16.654 -18.766 -37.552 0.66 17.61 ? 451  ARG   B CZ  1 
ATOM   2931 C  CZ  B ARG   B 1 10  ? -12.850 -21.289 -39.622 0.34 29.22 ? 451  ARG   B CZ  1 
ATOM   2932 N  NH1 A ARG   B 1 10  ? -17.001 -19.932 -38.073 0.66 20.23 ? 451  ARG   B NH1 1 
ATOM   2933 N  NH1 B ARG   B 1 10  ? -11.902 -21.655 -38.762 0.34 17.90 ? 451  ARG   B NH1 1 
ATOM   2934 N  NH2 A ARG   B 1 10  ? -17.588 -17.913 -37.152 0.66 15.58 ? 451  ARG   B NH2 1 
ATOM   2935 N  NH2 B ARG   B 1 10  ? -12.845 -21.773 -40.854 0.34 16.02 ? 451  ARG   B NH2 1 
ATOM   2936 N  N   . MET   B 1 11  ? -11.995 -15.109 -40.951 1.00 17.11 ? 452  MET   B N   1 
ATOM   2937 C  CA  . MET   B 1 11  ? -11.899 -14.475 -42.261 1.00 14.93 ? 452  MET   B CA  1 
ATOM   2938 C  C   . MET   B 1 11  ? -10.461 -14.218 -42.693 1.00 17.26 ? 452  MET   B C   1 
ATOM   2939 O  O   . MET   B 1 11  ? -10.231 -13.882 -43.864 1.00 18.52 ? 452  MET   B O   1 
ATOM   2940 C  CB  . MET   B 1 11  ? -12.720 -13.179 -42.303 1.00 15.89 ? 452  MET   B CB  1 
ATOM   2941 C  CG  . MET   B 1 11  ? -14.194 -13.395 -42.547 1.00 14.97 ? 452  MET   B CG  1 
ATOM   2942 S  SD  . MET   B 1 11  ? -15.206 -11.913 -42.399 1.00 16.71 ? 452  MET   B SD  1 
ATOM   2943 C  CE  . MET   B 1 11  ? -15.239 -11.678 -40.603 1.00 22.59 ? 452  MET   B CE  1 
ATOM   2944 N  N   . MET   B 1 12  ? -9.491  -14.371 -41.796 1.00 15.72 ? 453  MET   B N   1 
ATOM   2945 C  CA  . MET   B 1 12  ? -8.092  -14.296 -42.192 1.00 16.93 ? 453  MET   B CA  1 
ATOM   2946 C  C   . MET   B 1 12  ? -7.618  -15.509 -42.981 1.00 19.16 ? 453  MET   B C   1 
ATOM   2947 O  O   . MET   B 1 12  ? -6.515  -15.456 -43.549 1.00 20.26 ? 453  MET   B O   1 
ATOM   2948 C  CB  . MET   B 1 12  ? -7.200  -14.145 -40.962 1.00 17.64 ? 453  MET   B CB  1 
ATOM   2949 C  CG  . MET   B 1 12  ? -7.437  -12.861 -40.161 1.00 16.23 ? 453  MET   B CG  1 
ATOM   2950 S  SD  . MET   B 1 12  ? -6.361  -12.810 -38.698 1.00 21.55 ? 453  MET   B SD  1 
ATOM   2951 C  CE  . MET   B 1 12  ? -4.738  -12.737 -39.418 1.00 22.48 ? 453  MET   B CE  1 
ATOM   2952 N  N   . LEU   B 1 13  ? -8.408  -16.589 -43.038 1.00 18.39 ? 454  LEU   B N   1 
ATOM   2953 C  CA  . LEU   B 1 13  ? -7.892  -17.845 -43.587 1.00 20.14 ? 454  LEU   B CA  1 
ATOM   2954 C  C   . LEU   B 1 13  ? -7.797  -17.817 -45.108 1.00 17.94 ? 454  LEU   B C   1 
ATOM   2955 O  O   . LEU   B 1 13  ? -6.991  -18.554 -45.690 1.00 19.41 ? 454  LEU   B O   1 
ATOM   2956 C  CB  . LEU   B 1 13  ? -8.747  -19.024 -43.123 1.00 18.95 ? 454  LEU   B CB  1 
ATOM   2957 C  CG  . LEU   B 1 13  ? -8.619  -19.325 -41.624 1.00 22.96 ? 454  LEU   B CG  1 
ATOM   2958 C  CD1 . LEU   B 1 13  ? -9.587  -20.418 -41.199 1.00 27.91 ? 454  LEU   B CD1 1 
ATOM   2959 C  CD2 . LEU   B 1 13  ? -7.193  -19.683 -41.239 1.00 25.66 ? 454  LEU   B CD2 1 
ATOM   2960 N  N   . HIS   B 1 14  ? -8.597  -16.990 -45.761 1.00 15.46 ? 455  HIS   B N   1 
ATOM   2961 C  CA  . HIS   B 1 14  ? -8.463  -16.764 -47.201 1.00 16.44 ? 455  HIS   B CA  1 
ATOM   2962 C  C   . HIS   B 1 14  ? -7.089  -16.166 -47.505 1.00 18.35 ? 455  HIS   B C   1 
ATOM   2963 O  O   . HIS   B 1 14  ? -6.716  -15.136 -46.943 1.00 15.86 ? 455  HIS   B O   1 
ATOM   2964 C  CB  . HIS   B 1 14  ? -9.587  -15.814 -47.607 1.00 15.84 ? 455  HIS   B CB  1 
ATOM   2965 C  CG  . HIS   B 1 14  ? -9.424  -15.182 -48.952 1.00 15.08 ? 455  HIS   B CG  1 
ATOM   2966 N  ND1 . HIS   B 1 14  ? -9.424  -15.897 -50.137 1.00 17.57 ? 455  HIS   B ND1 1 
ATOM   2967 C  CD2 . HIS   B 1 14  ? -9.326  -13.876 -49.300 1.00 17.52 ? 455  HIS   B CD2 1 
ATOM   2968 C  CE1 . HIS   B 1 14  ? -9.315  -15.056 -51.151 1.00 16.45 ? 455  HIS   B CE1 1 
ATOM   2969 N  NE2 . HIS   B 1 14  ? -9.244  -13.826 -50.668 1.00 17.24 ? 455  HIS   B NE2 1 
ATOM   2970 N  N   . HIS   B 1 15  ? -6.309  -16.825 -48.366 1.00 17.04 ? 456  HIS   B N   1 
ATOM   2971 C  CA  . HIS   B 1 15  ? -4.939  -16.384 -48.580 1.00 18.70 ? 456  HIS   B CA  1 
ATOM   2972 C  C   . HIS   B 1 15  ? -4.473  -16.765 -49.981 1.00 15.99 ? 456  HIS   B C   1 
ATOM   2973 O  O   . HIS   B 1 15  ? -5.096  -17.573 -50.680 1.00 20.21 ? 456  HIS   B O   1 
ATOM   2974 C  CB  . HIS   B 1 15  ? -3.997  -16.959 -47.525 1.00 17.00 ? 456  HIS   B CB  1 
ATOM   2975 C  CG  . HIS   B 1 15  ? -3.812  -18.437 -47.639 1.00 20.10 ? 456  HIS   B CG  1 
ATOM   2976 N  ND1 . HIS   B 1 15  ? -4.785  -19.343 -47.280 1.00 26.95 ? 456  HIS   B ND1 1 
ATOM   2977 C  CD2 . HIS   B 1 15  ? -2.771  -19.167 -48.106 1.00 32.61 ? 456  HIS   B CD2 1 
ATOM   2978 C  CE1 . HIS   B 1 15  ? -4.344  -20.570 -47.501 1.00 33.02 ? 456  HIS   B CE1 1 
ATOM   2979 N  NE2 . HIS   B 1 15  ? -3.126  -20.490 -48.006 1.00 37.92 ? 456  HIS   B NE2 1 
ATOM   2980 N  N   . ASN   B 1 16  ? -3.389  -16.112 -50.397 1.00 18.78 ? 457  ASN   B N   1 
ATOM   2981 C  CA  . ASN   B 1 16  ? -2.803  -16.298 -51.722 1.00 21.51 ? 457  ASN   B CA  1 
ATOM   2982 C  C   . ASN   B 1 16  ? -1.648  -17.288 -51.604 1.00 20.72 ? 457  ASN   B C   1 
ATOM   2983 O  O   . ASN   B 1 16  ? -0.604  -16.960 -51.043 1.00 20.40 ? 457  ASN   B O   1 
ATOM   2984 C  CB  . ASN   B 1 16  ? -2.306  -14.959 -52.259 1.00 20.92 ? 457  ASN   B CB  1 
ATOM   2985 C  CG  . ASN   B 1 16  ? -1.912  -15.032 -53.726 1.00 22.43 ? 457  ASN   B CG  1 
ATOM   2986 O  OD1 . ASN   B 1 16  ? -1.389  -16.042 -54.179 1.00 24.07 ? 457  ASN   B OD1 1 
ATOM   2987 N  ND2 . ASN   B 1 16  ? -2.175  -13.963 -54.472 1.00 20.65 ? 457  ASN   B ND2 1 
ATOM   2988 N  N   . MET   B 1 17  ? -1.838  -18.494 -52.139 1.00 22.54 ? 458  MET   B N   1 
ATOM   2989 C  CA  . MET   B 1 17  ? -0.838  -19.539 -51.928 1.00 32.33 ? 458  MET   B CA  1 
ATOM   2990 C  C   . MET   B 1 17  ? 0.470   -19.235 -52.648 1.00 31.11 ? 458  MET   B C   1 
ATOM   2991 O  O   . MET   B 1 17  ? 1.543   -19.593 -52.154 1.00 29.40 ? 458  MET   B O   1 
ATOM   2992 C  CB  . MET   B 1 17  ? -1.381  -20.880 -52.410 1.00 30.44 ? 458  MET   B CB  1 
ATOM   2993 C  CG  . MET   B 1 17  ? -2.560  -21.390 -51.602 1.00 56.51 ? 458  MET   B CG  1 
ATOM   2994 S  SD  . MET   B 1 17  ? -3.250  -22.885 -52.317 1.00 59.89 ? 458  MET   B SD  1 
ATOM   2995 C  CE  . MET   B 1 17  ? -1.990  -23.260 -53.540 1.00 45.03 ? 458  MET   B CE  1 
ATOM   2996 N  N   . TRP   B 1 18  ? 0.405   -18.578 -53.804 1.00 23.46 ? 459  TRP   B N   1 
ATOM   2997 C  CA  . TRP   B 1 18  ? 1.583   -18.385 -54.640 1.00 23.31 ? 459  TRP   B CA  1 
ATOM   2998 C  C   . TRP   B 1 18  ? 2.289   -17.059 -54.400 1.00 34.35 ? 459  TRP   B C   1 
ATOM   2999 O  O   . TRP   B 1 18  ? 3.495   -16.960 -54.656 1.00 31.78 ? 459  TRP   B O   1 
ATOM   3000 C  CB  . TRP   B 1 18  ? 1.186   -18.540 -56.106 1.00 23.90 ? 459  TRP   B CB  1 
ATOM   3001 C  CG  . TRP   B 1 18  ? 0.326   -19.744 -56.295 1.00 50.15 ? 459  TRP   B CG  1 
ATOM   3002 C  CD1 . TRP   B 1 18  ? 0.742   -21.013 -56.577 1.00 48.09 ? 459  TRP   B CD1 1 
ATOM   3003 C  CD2 . TRP   B 1 18  ? -1.101  -19.807 -56.171 1.00 57.36 ? 459  TRP   B CD2 1 
ATOM   3004 N  NE1 . TRP   B 1 18  ? -0.338  -21.859 -56.655 1.00 51.18 ? 459  TRP   B NE1 1 
ATOM   3005 C  CE2 . TRP   B 1 18  ? -1.482  -21.144 -56.408 1.00 47.79 ? 459  TRP   B CE2 1 
ATOM   3006 C  CE3 . TRP   B 1 18  ? -2.094  -18.860 -55.896 1.00 41.96 ? 459  TRP   B CE3 1 
ATOM   3007 C  CZ2 . TRP   B 1 18  ? -2.813  -21.558 -56.378 1.00 51.58 ? 459  TRP   B CZ2 1 
ATOM   3008 C  CZ3 . TRP   B 1 18  ? -3.415  -19.273 -55.870 1.00 45.97 ? 459  TRP   B CZ3 1 
ATOM   3009 C  CH2 . TRP   B 1 18  ? -3.763  -20.612 -56.109 1.00 39.12 ? 459  TRP   B CH2 1 
ATOM   3010 N  N   . ASP   B 1 19  ? 1.578   -16.051 -53.884 1.00 31.86 ? 460  ASP   B N   1 
ATOM   3011 C  CA  . ASP   B 1 19  ? 2.136   -14.720 -53.624 1.00 22.73 ? 460  ASP   B CA  1 
ATOM   3012 C  C   . ASP   B 1 19  ? 1.636   -14.300 -52.241 1.00 27.72 ? 460  ASP   B C   1 
ATOM   3013 O  O   . ASP   B 1 19  ? 0.622   -13.614 -52.117 1.00 24.12 ? 460  ASP   B O   1 
ATOM   3014 C  CB  . ASP   B 1 19  ? 1.686   -13.735 -54.702 1.00 22.57 ? 460  ASP   B CB  1 
ATOM   3015 C  CG  . ASP   B 1 19  ? 2.115   -12.308 -54.415 1.00 18.61 ? 460  ASP   B CG  1 
ATOM   3016 O  OD1 . ASP   B 1 19  ? 2.979   -12.079 -53.559 1.00 22.28 ? 460  ASP   B OD1 1 
ATOM   3017 O  OD2 . ASP   B 1 19  ? 1.553   -11.419 -55.076 1.00 24.39 ? 460  ASP   B OD2 1 
ATOM   3018 N  N   . SER   B 1 20  ? 2.359   -14.718 -51.201 1.00 31.41 ? 461  SER   B N   1 
ATOM   3019 C  CA  . SER   B 1 20  ? 1.919   -14.459 -49.834 1.00 27.82 ? 461  SER   B CA  1 
ATOM   3020 C  C   . SER   B 1 20  ? 1.988   -12.982 -49.461 1.00 28.45 ? 461  SER   B C   1 
ATOM   3021 O  O   . SER   B 1 20  ? 1.398   -12.587 -48.450 1.00 36.84 ? 461  SER   B O   1 
ATOM   3022 C  CB  . SER   B 1 20  ? 2.736   -15.294 -48.850 1.00 28.69 ? 461  SER   B CB  1 
ATOM   3023 O  OG  . SER   B 1 20  ? 4.099   -14.892 -48.870 1.00 30.34 ? 461  SER   B OG  1 
ATOM   3024 N  N   . HIS   B 1 21  ? 2.681   -12.162 -50.248 1.00 24.76 ? 462  HIS   B N   1 
ATOM   3025 C  CA  . HIS   B 1 21  ? 2.756   -10.723 -50.030 1.00 23.27 ? 462  HIS   B CA  1 
ATOM   3026 C  C   . HIS   B 1 21  ? 1.709   -9.945  -50.818 1.00 16.01 ? 462  HIS   B C   1 
ATOM   3027 O  O   . HIS   B 1 21  ? 1.771   -8.707  -50.858 1.00 20.24 ? 462  HIS   B O   1 
ATOM   3028 C  CB  . HIS   B 1 21  ? 4.150   -10.209 -50.380 1.00 22.27 ? 462  HIS   B CB  1 
ATOM   3029 C  CG  . HIS   B 1 21  ? 5.218   -10.701 -49.458 1.00 42.86 ? 462  HIS   B CG  1 
ATOM   3030 N  ND1 . HIS   B 1 21  ? 5.769   -9.912  -48.472 1.00 37.74 ? 462  HIS   B ND1 1 
ATOM   3031 C  CD2 . HIS   B 1 21  ? 5.829   -11.906 -49.364 1.00 49.38 ? 462  HIS   B CD2 1 
ATOM   3032 C  CE1 . HIS   B 1 21  ? 6.678   -10.608 -47.813 1.00 55.69 ? 462  HIS   B CE1 1 
ATOM   3033 N  NE2 . HIS   B 1 21  ? 6.733   -11.821 -48.333 1.00 60.05 ? 462  HIS   B NE2 1 
ATOM   3034 N  N   . HIS   B 1 22  ? 0.787   -10.637 -51.468 1.00 17.46 ? 463  HIS   B N   1 
ATOM   3035 C  CA  . HIS   B 1 22  ? -0.272  -9.964  -52.202 1.00 15.89 ? 463  HIS   B CA  1 
ATOM   3036 C  C   . HIS   B 1 22  ? -0.986  -8.981  -51.275 1.00 17.88 ? 463  HIS   B C   1 
ATOM   3037 O  O   . HIS   B 1 22  ? -1.287  -9.326  -50.127 1.00 20.25 ? 463  HIS   B O   1 
ATOM   3038 C  CB  . HIS   B 1 22  ? -1.274  -11.000 -52.711 1.00 19.73 ? 463  HIS   B CB  1 
ATOM   3039 C  CG  . HIS   B 1 22  ? -2.344  -10.430 -53.578 1.00 17.43 ? 463  HIS   B CG  1 
ATOM   3040 N  ND1 . HIS   B 1 22  ? -3.392  -9.680  -53.081 1.00 17.27 ? 463  HIS   B ND1 1 
ATOM   3041 C  CD2 . HIS   B 1 22  ? -2.542  -10.519 -54.913 1.00 19.74 ? 463  HIS   B CD2 1 
ATOM   3042 C  CE1 . HIS   B 1 22  ? -4.180  -9.324  -54.077 1.00 18.77 ? 463  HIS   B CE1 1 
ATOM   3043 N  NE2 . HIS   B 1 22  ? -3.682  -9.812  -55.202 1.00 19.95 ? 463  HIS   B NE2 1 
ATOM   3044 N  N   . PRO   B 1 23  ? -1.276  -7.763  -51.743 1.00 14.56 ? 464  PRO   B N   1 
ATOM   3045 C  CA  . PRO   B 1 23  ? -1.769  -6.709  -50.834 1.00 16.80 ? 464  PRO   B CA  1 
ATOM   3046 C  C   . PRO   B 1 23  ? -3.085  -7.013  -50.113 1.00 14.28 ? 464  PRO   B C   1 
ATOM   3047 O  O   . PRO   B 1 23  ? -3.335  -6.392  -49.072 1.00 14.34 ? 464  PRO   B O   1 
ATOM   3048 C  CB  . PRO   B 1 23  ? -1.919  -5.490  -51.761 1.00 18.58 ? 464  PRO   B CB  1 
ATOM   3049 C  CG  . PRO   B 1 23  ? -1.993  -6.062  -53.141 1.00 18.38 ? 464  PRO   B CG  1 
ATOM   3050 C  CD  . PRO   B 1 23  ? -1.050  -7.248  -53.103 1.00 16.36 ? 464  PRO   B CD  1 
ATOM   3051 N  N   . GLU   B 1 24  ? -3.946  -7.896  -50.634 1.00 14.61 ? 465  GLU   B N   1 
ATOM   3052 C  CA  . GLU   B 1 24  ? -5.223  -8.207  -49.970 1.00 14.71 ? 465  GLU   B CA  1 
ATOM   3053 C  C   . GLU   B 1 24  ? -4.943  -9.247  -48.888 1.00 14.37 ? 465  GLU   B C   1 
ATOM   3054 O  O   . GLU   B 1 24  ? -5.286  -10.428 -49.007 1.00 15.95 ? 465  GLU   B O   1 
ATOM   3055 C  CB  . GLU   B 1 24  ? -6.264  -8.692  -50.969 1.00 13.26 ? 465  GLU   B CB  1 
ATOM   3056 C  CG  . GLU   B 1 24  ? -7.734  -8.466  -50.545 1.00 14.36 ? 465  GLU   B CG  1 
ATOM   3057 C  CD  . GLU   B 1 24  ? -8.160  -9.309  -49.344 1.00 16.10 ? 465  GLU   B CD  1 
ATOM   3058 O  OE1 . GLU   B 1 24  ? -8.641  -10.448 -49.561 1.00 16.84 ? 465  GLU   B OE1 1 
ATOM   3059 O  OE2 . GLU   B 1 24  ? -8.037  -8.829  -48.186 1.00 14.92 ? 465  GLU   B OE2 1 
ATOM   3060 N  N   . LEU   B 1 25  ? -4.280  -8.782  -47.830 1.00 13.11 ? 466  LEU   B N   1 
ATOM   3061 C  CA  . LEU   B 1 25  ? -3.678  -9.650  -46.821 1.00 14.57 ? 466  LEU   B CA  1 
ATOM   3062 C  C   . LEU   B 1 25  ? -4.668  -10.030 -45.720 1.00 15.35 ? 466  LEU   B C   1 
ATOM   3063 O  O   . LEU   B 1 25  ? -5.498  -9.210  -45.297 1.00 14.97 ? 466  LEU   B O   1 
ATOM   3064 C  CB  . LEU   B 1 25  ? -2.542  -8.928  -46.120 1.00 15.04 ? 466  LEU   B CB  1 
ATOM   3065 C  CG  . LEU   B 1 25  ? -1.253  -8.690  -46.899 1.00 18.62 ? 466  LEU   B CG  1 
ATOM   3066 C  CD1 . LEU   B 1 25  ? -0.400  -7.685  -46.162 1.00 19.46 ? 466  LEU   B CD1 1 
ATOM   3067 C  CD2 . LEU   B 1 25  ? -0.506  -10.007 -47.076 1.00 18.69 ? 466  LEU   B CD2 1 
ATOM   3068 N  N   . PRO   B 1 26  ? -4.516  -11.251 -45.188 1.00 14.58 ? 467  PRO   B N   1 
ATOM   3069 C  CA  . PRO   B 1 26  ? -5.230  -11.624 -43.959 1.00 16.64 ? 467  PRO   B CA  1 
ATOM   3070 C  C   . PRO   B 1 26  ? -5.139  -10.566 -42.875 1.00 17.28 ? 467  PRO   B C   1 
ATOM   3071 O  O   . PRO   B 1 26  ? -6.142  -10.278 -42.209 1.00 17.86 ? 467  PRO   B O   1 
ATOM   3072 C  CB  . PRO   B 1 26  ? -4.510  -12.915 -43.532 1.00 16.70 ? 467  PRO   B CB  1 
ATOM   3073 C  CG  . PRO   B 1 26  ? -4.063  -13.526 -44.829 1.00 17.71 ? 467  PRO   B CG  1 
ATOM   3074 C  CD  . PRO   B 1 26  ? -3.710  -12.367 -45.731 1.00 16.80 ? 467  PRO   B CD  1 
ATOM   3075 N  N   . GLN   B 1 27  ? -3.971  -9.955  -42.699 1.00 14.19 ? 468  GLN   B N   1 
ATOM   3076 C  CA  . GLN   B 1 27  ? -3.771  -9.011  -41.616 1.00 14.81 ? 468  GLN   B CA  1 
ATOM   3077 C  C   . GLN   B 1 27  ? -4.504  -7.688  -41.801 1.00 15.18 ? 468  GLN   B C   1 
ATOM   3078 O  O   . GLN   B 1 27  ? -4.469  -6.863  -40.876 1.00 12.87 ? 468  GLN   B O   1 
ATOM   3079 C  CB  . GLN   B 1 27  ? -2.283  -8.775  -41.320 1.00 18.59 ? 468  GLN   B CB  1 
ATOM   3080 C  CG  . GLN   B 1 27  ? -1.377  -8.516  -42.497 1.00 40.22 ? 468  GLN   B CG  1 
ATOM   3081 C  CD  . GLN   B 1 27  ? -0.689  -9.785  -42.984 1.00 30.50 ? 468  GLN   B CD  1 
ATOM   3082 O  OE1 . GLN   B 1 27  ? -1.347  -10.794 -43.225 1.00 18.03 ? 468  GLN   B OE1 1 
ATOM   3083 N  NE2 . GLN   B 1 27  ? 0.639   -9.734  -43.140 1.00 24.08 ? 468  GLN   B NE2 1 
ATOM   3084 N  N   . ARG   B 1 28  ? -5.123  -7.447  -42.958 1.00 12.51 ? 469  ARG   B N   1 
ATOM   3085 C  CA  . ARG   B 1 28  ? -5.920  -6.232  -43.100 1.00 11.90 ? 469  ARG   B CA  1 
ATOM   3086 C  C   . ARG   B 1 28  ? -6.955  -6.139  -41.975 1.00 12.00 ? 469  ARG   B C   1 
ATOM   3087 O  O   . ARG   B 1 28  ? -7.082  -5.103  -41.310 1.00 11.84 ? 469  ARG   B O   1 
ATOM   3088 C  CB  . ARG   B 1 28  ? -6.597  -6.185  -44.473 1.00 12.78 ? 469  ARG   B CB  1 
ATOM   3089 C  CG  . ARG   B 1 28  ? -5.610  -5.970  -45.626 1.00 13.54 ? 469  ARG   B CG  1 
ATOM   3090 C  CD  . ARG   B 1 28  ? -6.271  -6.132  -47.000 1.00 13.65 ? 469  ARG   B CD  1 
ATOM   3091 N  NE  . ARG   B 1 28  ? -7.222  -5.044  -47.183 1.00 13.78 ? 469  ARG   B NE  1 
ATOM   3092 C  CZ  . ARG   B 1 28  ? -8.534  -5.199  -47.236 1.00 12.89 ? 469  ARG   B CZ  1 
ATOM   3093 N  NH1 . ARG   B 1 28  ? -9.077  -6.418  -47.207 1.00 13.24 ? 469  ARG   B NH1 1 
ATOM   3094 N  NH2 . ARG   B 1 28  ? -9.303  -4.114  -47.301 1.00 13.16 ? 469  ARG   B NH2 1 
ATOM   3095 N  N   . ILE   B 1 29  ? -7.687  -7.229  -41.732 1.00 12.23 ? 470  ILE   B N   1 
ATOM   3096 C  CA  . ILE   B 1 29  ? -8.770  -7.172  -40.757 1.00 12.98 ? 470  ILE   B CA  1 
ATOM   3097 C  C   . ILE   B 1 29  ? -8.228  -7.234  -39.340 1.00 12.65 ? 470  ILE   B C   1 
ATOM   3098 O  O   . ILE   B 1 29  ? -8.737  -6.552  -38.448 1.00 11.67 ? 470  ILE   B O   1 
ATOM   3099 C  CB  . ILE   B 1 29  ? -9.876  -8.217  -41.016 1.00 13.40 ? 470  ILE   B CB  1 
ATOM   3100 C  CG1 . ILE   B 1 29  ? -9.317  -9.655  -41.033 1.00 14.67 ? 470  ILE   B CG1 1 
ATOM   3101 C  CG2 . ILE   B 1 29  ? -10.609 -7.861  -42.306 1.00 11.65 ? 470  ILE   B CG2 1 
ATOM   3102 C  CD1 . ILE   B 1 29  ? -10.376 -10.746 -40.986 1.00 15.48 ? 470  ILE   B CD1 1 
ATOM   3103 N  N   . SER   B 1 30  ? -7.197  -8.036  -39.096 1.00 13.61 ? 471  SER   B N   1 
ATOM   3104 C  CA  . SER   B 1 30  ? -6.684  -8.107  -37.730 1.00 14.30 ? 471  SER   B CA  1 
ATOM   3105 C  C   . SER   B 1 30  ? -6.034  -6.793  -37.316 1.00 13.76 ? 471  SER   B C   1 
ATOM   3106 O  O   . SER   B 1 30  ? -6.109  -6.403  -36.145 1.00 12.88 ? 471  SER   B O   1 
ATOM   3107 C  CB  . SER   B 1 30  ? -5.728  -9.291  -37.566 1.00 17.27 ? 471  SER   B CB  1 
ATOM   3108 O  OG  . SER   B 1 30  ? -4.624  -9.161  -38.426 1.00 18.77 ? 471  SER   B OG  1 
ATOM   3109 N  N   . ARG   B 1 31  ? -5.416  -6.087  -38.267 1.00 14.68 ? 472  ARG   B N   1 
ATOM   3110 C  CA  . ARG   B 1 31  ? -4.817  -4.798  -37.946 1.00 11.46 ? 472  ARG   B CA  1 
ATOM   3111 C  C   . ARG   B 1 31  ? -5.875  -3.756  -37.626 1.00 12.85 ? 472  ARG   B C   1 
ATOM   3112 O  O   . ARG   B 1 31  ? -5.716  -2.972  -36.690 1.00 11.68 ? 472  ARG   B O   1 
ATOM   3113 C  CB  . ARG   B 1 31  ? -3.942  -4.313  -39.101 1.00 13.32 ? 472  ARG   B CB  1 
ATOM   3114 C  CG  . ARG   B 1 31  ? -2.564  -5.024  -39.146 1.00 13.29 ? 472  ARG   B CG  1 
ATOM   3115 C  CD  . ARG   B 1 31  ? -1.642  -4.560  -37.986 1.00 13.79 ? 472  ARG   B CD  1 
ATOM   3116 N  NE  . ARG   B 1 31  ? -1.360  -3.138  -38.101 1.00 13.15 ? 472  ARG   B NE  1 
ATOM   3117 C  CZ  . ARG   B 1 31  ? -0.427  -2.623  -38.892 1.00 12.24 ? 472  ARG   B CZ  1 
ATOM   3118 N  NH1 . ARG   B 1 31  ? 0.339   -3.423  -39.625 1.00 14.26 ? 472  ARG   B NH1 1 
ATOM   3119 N  NH2 . ARG   B 1 31  ? -0.261  -1.316  -38.943 1.00 16.23 ? 472  ARG   B NH2 1 
ATOM   3120 N  N   . ILE   B 1 32  ? -6.957  -3.719  -38.402 1.00 12.16 ? 473  ILE   B N   1 
ATOM   3121 C  CA  . ILE   B 1 32  ? -8.030  -2.777  -38.097 1.00 12.63 ? 473  ILE   B CA  1 
ATOM   3122 C  C   . ILE   B 1 32  ? -8.615  -3.070  -36.719 1.00 11.71 ? 473  ILE   B C   1 
ATOM   3123 O  O   . ILE   B 1 32  ? -8.809  -2.160  -35.904 1.00 11.75 ? 473  ILE   B O   1 
ATOM   3124 C  CB  . ILE   B 1 32  ? -9.101  -2.803  -39.202 1.00 11.43 ? 473  ILE   B CB  1 
ATOM   3125 C  CG1 . ILE   B 1 32  ? -8.540  -2.266  -40.520 1.00 10.96 ? 473  ILE   B CG1 1 
ATOM   3126 C  CG2 . ILE   B 1 32  ? -10.332 -2.000  -38.751 1.00 12.47 ? 473  ILE   B CG2 1 
ATOM   3127 C  CD1 . ILE   B 1 32  ? -9.416  -2.618  -41.727 1.00 10.66 ? 473  ILE   B CD1 1 
ATOM   3128 N  N   . PHE   B 1 33  ? -8.848  -4.355  -36.426 1.00 11.81 ? 474  PHE   B N   1 
ATOM   3129 C  CA  . PHE   B 1 33  ? -9.384  -4.744  -35.124 1.00 13.57 ? 474  PHE   B CA  1 
ATOM   3130 C  C   . PHE   B 1 33  ? -8.438  -4.326  -33.995 1.00 11.88 ? 474  PHE   B C   1 
ATOM   3131 O  O   . PHE   B 1 33  ? -8.878  -3.771  -32.975 1.00 13.27 ? 474  PHE   B O   1 
ATOM   3132 C  CB  . PHE   B 1 33  ? -9.607  -6.253  -35.121 1.00 14.64 ? 474  PHE   B CB  1 
ATOM   3133 C  CG  . PHE   B 1 33  ? -10.248 -6.794  -33.857 1.00 16.00 ? 474  PHE   B CG  1 
ATOM   3134 C  CD1 . PHE   B 1 33  ? -11.596 -6.593  -33.596 1.00 14.59 ? 474  PHE   B CD1 1 
ATOM   3135 C  CD2 . PHE   B 1 33  ? -9.499  -7.518  -32.943 1.00 17.60 ? 474  PHE   B CD2 1 
ATOM   3136 C  CE1 . PHE   B 1 33  ? -12.192 -7.118  -32.444 1.00 18.18 ? 474  PHE   B CE1 1 
ATOM   3137 C  CE2 . PHE   B 1 33  ? -10.090 -8.031  -31.776 1.00 17.11 ? 474  PHE   B CE2 1 
ATOM   3138 C  CZ  . PHE   B 1 33  ? -11.435 -7.825  -31.539 1.00 21.16 ? 474  PHE   B CZ  1 
ATOM   3139 N  N   . SER   B 1 34  ? -7.131  -4.567  -34.179 1.00 13.73 ? 475  SER   B N   1 
ATOM   3140 C  CA  . SER   B 1 34  ? -6.130  -4.209  -33.173 1.00 17.30 ? 475  SER   B CA  1 
ATOM   3141 C  C   . SER   B 1 34  ? -6.136  -2.713  -32.902 1.00 12.73 ? 475  SER   B C   1 
ATOM   3142 O  O   . SER   B 1 34  ? -6.056  -2.270  -31.750 1.00 13.25 ? 475  SER   B O   1 
ATOM   3143 C  CB  . SER   B 1 34  ? -4.749  -4.639  -33.675 1.00 16.20 ? 475  SER   B CB  1 
ATOM   3144 O  OG  . SER   B 1 34  ? -3.739  -4.153  -32.810 1.00 17.37 ? 475  SER   B OG  1 
ATOM   3145 N  N   . ARG   B 1 35  ? -6.234  -1.905  -33.959 1.00 11.36 ? 476  ARG   B N   1 
ATOM   3146 C  CA  . ARG   B 1 35  ? -6.259  -0.467  -33.747 1.00 11.88 ? 476  ARG   B CA  1 
ATOM   3147 C  C   . ARG   B 1 35  ? -7.504  -0.038  -32.963 1.00 13.02 ? 476  ARG   B C   1 
ATOM   3148 O  O   . ARG   B 1 35  ? -7.433  0.882   -32.143 1.00 12.48 ? 476  ARG   B O   1 
ATOM   3149 C  CB  . ARG   B 1 35  ? -6.156  0.249   -35.093 1.00 12.35 ? 476  ARG   B CB  1 
ATOM   3150 C  CG  . ARG   B 1 35  ? -5.975  1.741   -34.991 1.00 12.96 ? 476  ARG   B CG  1 
ATOM   3151 C  CD  . ARG   B 1 35  ? -4.583  2.099   -34.486 1.00 17.91 ? 476  ARG   B CD  1 
ATOM   3152 N  NE  . ARG   B 1 35  ? -4.404  3.550   -34.450 1.00 15.55 ? 476  ARG   B NE  1 
ATOM   3153 C  CZ  . ARG   B 1 35  ? -3.879  4.212   -33.418 1.00 16.33 ? 476  ARG   B CZ  1 
ATOM   3154 N  NH1 . ARG   B 1 35  ? -3.458  3.546   -32.346 1.00 17.16 ? 476  ARG   B NH1 1 
ATOM   3155 N  NH2 . ARG   B 1 35  ? -3.742  5.533   -33.479 1.00 19.09 ? 476  ARG   B NH2 1 
ATOM   3156 N  N   . HIS   B 1 36  ? -8.651  -0.698  -33.182 1.00 12.41 ? 477  HIS   B N   1 
ATOM   3157 C  CA  . HIS   B 1 36  ? -9.830  -0.409  -32.373 1.00 12.39 ? 477  HIS   B CA  1 
ATOM   3158 C  C   . HIS   B 1 36  ? -9.570  -0.711  -30.897 1.00 13.97 ? 477  HIS   B C   1 
ATOM   3159 O  O   . HIS   B 1 36  ? -10.016 0.029   -30.009 1.00 13.86 ? 477  HIS   B O   1 
ATOM   3160 C  CB  . HIS   B 1 36  ? -11.009 -1.245  -32.873 1.00 14.29 ? 477  HIS   B CB  1 
ATOM   3161 C  CG  . HIS   B 1 36  ? -11.725 -0.664  -34.057 1.00 12.75 ? 477  HIS   B CG  1 
ATOM   3162 N  ND1 . HIS   B 1 36  ? -11.215 -0.721  -35.337 1.00 12.75 ? 477  HIS   B ND1 1 
ATOM   3163 C  CD2 . HIS   B 1 36  ? -12.917 -0.024  -34.150 1.00 14.50 ? 477  HIS   B CD2 1 
ATOM   3164 C  CE1 . HIS   B 1 36  ? -12.079 -0.165  -36.175 1.00 13.67 ? 477  HIS   B CE1 1 
ATOM   3165 N  NE2 . HIS   B 1 36  ? -13.113 0.281   -35.478 1.00 13.22 ? 477  HIS   B NE2 1 
ATOM   3166 N  N   . GLU   B 1 37  ? -8.874  -1.808  -30.604 1.00 13.56 ? 478  GLU   B N   1 
ATOM   3167 C  CA  . GLU   B 1 37  ? -8.539  -2.117  -29.213 1.00 16.97 ? 478  GLU   B CA  1 
ATOM   3168 C  C   . GLU   B 1 37  ? -7.552  -1.101  -28.641 1.00 17.19 ? 478  GLU   B C   1 
ATOM   3169 O  O   . GLU   B 1 37  ? -7.751  -0.575  -27.540 1.00 17.07 ? 478  GLU   B O   1 
ATOM   3170 C  CB  . GLU   B 1 37  ? -7.983  -3.536  -29.129 1.00 16.52 ? 478  GLU   B CB  1 
ATOM   3171 C  CG  . GLU   B 1 37  ? -7.813  -4.066  -27.717 1.00 25.03 ? 478  GLU   B CG  1 
ATOM   3172 C  CD  . GLU   B 1 37  ? -7.321  -5.499  -27.716 1.00 53.39 ? 478  GLU   B CD  1 
ATOM   3173 O  OE1 . GLU   B 1 37  ? -6.089  -5.703  -27.757 1.00 57.45 ? 478  GLU   B OE1 1 
ATOM   3174 O  OE2 . GLU   B 1 37  ? -8.168  -6.419  -27.695 1.00 56.63 ? 478  GLU   B OE2 1 
ATOM   3175 N  N   . GLU   B 1 38  ? -6.499  -0.795  -29.403 1.00 14.57 ? 479  GLU   B N   1 
ATOM   3176 C  CA  . GLU   B 1 38  ? -5.487  0.175   -29.000 1.00 15.88 ? 479  GLU   B CA  1 
ATOM   3177 C  C   . GLU   B 1 38  ? -6.089  1.520   -28.657 1.00 15.33 ? 479  GLU   B C   1 
ATOM   3178 O  O   . GLU   B 1 38  ? -5.639  2.187   -27.711 1.00 18.80 ? 479  GLU   B O   1 
ATOM   3179 C  CB  . GLU   B 1 38  ? -4.530  0.395   -30.166 1.00 18.96 ? 479  GLU   B CB  1 
ATOM   3180 C  CG  . GLU   B 1 38  ? -3.097  0.295   -29.859 1.00 22.54 ? 479  GLU   B CG  1 
ATOM   3181 C  CD  . GLU   B 1 38  ? -2.284  0.200   -31.127 1.00 17.58 ? 479  GLU   B CD  1 
ATOM   3182 O  OE1 . GLU   B 1 38  ? -2.632  0.874   -32.120 1.00 17.66 ? 479  GLU   B OE1 1 
ATOM   3183 O  OE2 . GLU   B 1 38  ? -1.311  -0.565  -31.138 1.00 20.72 ? 479  GLU   B OE2 1 
ATOM   3184 N  N   . LEU   B 1 39  ? -7.097  1.952   -29.410 1.00 14.40 ? 480  LEU   B N   1 
ATOM   3185 C  CA  . LEU   B 1 39  ? -7.742  3.235   -29.167 1.00 16.05 ? 480  LEU   B CA  1 
ATOM   3186 C  C   . LEU   B 1 39  ? -8.881  3.139   -28.151 1.00 18.23 ? 480  LEU   B C   1 
ATOM   3187 O  O   . LEU   B 1 39  ? -9.552  4.150   -27.886 1.00 18.43 ? 480  LEU   B O   1 
ATOM   3188 C  CB  . LEU   B 1 39  ? -8.257  3.828   -30.481 1.00 14.90 ? 480  LEU   B CB  1 
ATOM   3189 C  CG  . LEU   B 1 39  ? -7.158  4.271   -31.470 1.00 16.14 ? 480  LEU   B CG  1 
ATOM   3190 C  CD1 . LEU   B 1 39  ? -7.751  4.682   -32.813 1.00 16.11 ? 480  LEU   B CD1 1 
ATOM   3191 C  CD2 . LEU   B 1 39  ? -6.350  5.416   -30.888 1.00 20.87 ? 480  LEU   B CD2 1 
ATOM   3192 N  N   . ARG   B 1 40  ? -9.118  1.952   -27.586 1.00 15.43 ? 481  ARG   B N   1 
ATOM   3193 C  CA  . ARG   B 1 40  ? -10.184 1.745   -26.591 1.00 13.77 ? 481  ARG   B CA  1 
ATOM   3194 C  C   . ARG   B 1 40  ? -11.582 1.975   -27.171 1.00 17.94 ? 481  ARG   B C   1 
ATOM   3195 O  O   . ARG   B 1 40  ? -12.534 2.284   -26.451 1.00 19.39 ? 481  ARG   B O   1 
ATOM   3196 C  CB  . ARG   B 1 40  ? -9.941  2.542   -25.300 1.00 18.42 ? 481  ARG   B CB  1 
ATOM   3197 C  CG  . ARG   B 1 40  ? -8.556  2.296   -24.720 1.00 22.59 ? 481  ARG   B CG  1 
ATOM   3198 C  CD  . ARG   B 1 40  ? -8.438  2.869   -23.313 1.00 29.15 ? 481  ARG   B CD  1 
ATOM   3199 N  NE  . ARG   B 1 40  ? -7.076  2.723   -22.814 1.00 33.64 ? 481  ARG   B NE  1 
ATOM   3200 C  CZ  . ARG   B 1 40  ? -6.642  3.218   -21.662 1.00 37.71 ? 481  ARG   B CZ  1 
ATOM   3201 N  NH1 . ARG   B 1 40  ? -7.466  3.897   -20.875 1.00 36.55 ? 481  ARG   B NH1 1 
ATOM   3202 N  NH2 . ARG   B 1 40  ? -5.382  3.028   -21.300 1.00 39.49 ? 481  ARG   B NH2 1 
ATOM   3203 N  N   . LEU   B 1 41  ? -11.699 1.811   -28.480 1.00 15.72 ? 482  LEU   B N   1 
ATOM   3204 C  CA  . LEU   B 1 41  ? -12.981 1.868   -29.165 1.00 14.92 ? 482  LEU   B CA  1 
ATOM   3205 C  C   . LEU   B 1 41  ? -13.716 0.541   -29.091 1.00 16.17 ? 482  LEU   B C   1 
ATOM   3206 O  O   . LEU   B 1 41  ? -14.949 0.532   -29.025 1.00 15.42 ? 482  LEU   B O   1 
ATOM   3207 C  CB  . LEU   B 1 41  ? -12.755 2.230   -30.640 1.00 14.77 ? 482  LEU   B CB  1 
ATOM   3208 C  CG  . LEU   B 1 41  ? -12.139 3.604   -30.894 1.00 14.60 ? 482  LEU   B CG  1 
ATOM   3209 C  CD1 . LEU   B 1 41  ? -11.651 3.741   -32.330 1.00 16.70 ? 482  LEU   B CD1 1 
ATOM   3210 C  CD2 . LEU   B 1 41  ? -13.136 4.714   -30.553 1.00 17.02 ? 482  LEU   B CD2 1 
ATOM   3211 N  N   . LEU   B 1 42  ? -12.990 -0.580  -29.113 1.00 15.16 ? 483  LEU   B N   1 
ATOM   3212 C  CA  . LEU   B 1 42  ? -13.645 -1.882  -29.157 1.00 15.31 ? 483  LEU   B CA  1 
ATOM   3213 C  C   . LEU   B 1 42  ? -14.561 -2.086  -27.955 1.00 14.67 ? 483  LEU   B C   1 
ATOM   3214 O  O   . LEU   B 1 42  ? -15.702 -2.558  -28.099 1.00 18.75 ? 483  LEU   B O   1 
ATOM   3215 C  CB  . LEU   B 1 42  ? -12.597 -2.990  -29.237 1.00 19.04 ? 483  LEU   B CB  1 
ATOM   3216 C  CG  . LEU   B 1 42  ? -13.111 -4.429  -29.157 1.00 18.13 ? 483  LEU   B CG  1 
ATOM   3217 C  CD1 . LEU   B 1 42  ? -14.084 -4.729  -30.303 1.00 21.29 ? 483  LEU   B CD1 1 
ATOM   3218 C  CD2 . LEU   B 1 42  ? -11.927 -5.397  -29.193 1.00 20.39 ? 483  LEU   B CD2 1 
ATOM   3219 N  N   . SER   B 1 43  ? -14.073 -1.749  -26.754 1.00 15.90 ? 484  SER   B N   1 
ATOM   3220 C  CA  . SER   B 1 43  ? -14.876 -1.961  -25.553 1.00 18.88 ? 484  SER   B CA  1 
ATOM   3221 C  C   . SER   B 1 43  ? -16.122 -1.071  -25.505 1.00 16.80 ? 484  SER   B C   1 
ATOM   3222 O  O   . SER   B 1 43  ? -17.044 -1.349  -24.718 1.00 20.41 ? 484  SER   B O   1 
ATOM   3223 C  CB  . SER   B 1 43  ? -14.013 -1.787  -24.302 1.00 21.60 ? 484  SER   B CB  1 
ATOM   3224 O  OG  . SER   B 1 43  ? -13.517 -0.464  -24.213 1.00 26.02 ? 484  SER   B OG  1 
ATOM   3225 N  N   . ARG   B 1 44  ? -16.173 -0.012  -26.314 1.00 14.94 ? 485  ARG   B N   1 
ATOM   3226 C  CA  . ARG   B 1 44  ? -17.319 0.878   -26.402 1.00 15.63 ? 485  ARG   B CA  1 
ATOM   3227 C  C   . ARG   B 1 44  ? -18.409 0.373   -27.339 1.00 16.11 ? 485  ARG   B C   1 
ATOM   3228 O  O   . ARG   B 1 44  ? -19.487 0.980   -27.394 1.00 19.64 ? 485  ARG   B O   1 
ATOM   3229 C  CB  . ARG   B 1 44  ? -16.868 2.263   -26.852 1.00 17.32 ? 485  ARG   B CB  1 
ATOM   3230 C  CG  . ARG   B 1 44  ? -15.863 2.873   -25.877 1.00 15.80 ? 485  ARG   B CG  1 
ATOM   3231 C  CD  . ARG   B 1 44  ? -15.314 4.181   -26.403 1.00 16.51 ? 485  ARG   B CD  1 
ATOM   3232 N  NE  . ARG   B 1 44  ? -16.367 5.169   -26.618 1.00 16.23 ? 485  ARG   B NE  1 
ATOM   3233 C  CZ  . ARG   B 1 44  ? -16.220 6.266   -27.358 1.00 15.54 ? 485  ARG   B CZ  1 
ATOM   3234 N  NH1 . ARG   B 1 44  ? -15.065 6.505   -27.990 1.00 15.82 ? 485  ARG   B NH1 1 
ATOM   3235 N  NH2 . ARG   B 1 44  ? -17.224 7.123   -27.495 1.00 17.10 ? 485  ARG   B NH2 1 
ATOM   3236 N  N   . CYS   B 1 45  ? -18.156 -0.715  -28.057 1.00 16.61 ? 486  CYS   B N   1 
ATOM   3237 C  CA  . CYS   B 1 45  ? -19.053 -1.215  -29.081 1.00 15.74 ? 486  CYS   B CA  1 
ATOM   3238 C  C   . CYS   B 1 45  ? -19.697 -2.490  -28.553 1.00 17.63 ? 486  CYS   B C   1 
ATOM   3239 O  O   . CYS   B 1 45  ? -19.172 -3.152  -27.663 1.00 18.87 ? 486  CYS   B O   1 
ATOM   3240 C  CB  . CYS   B 1 45  ? -18.199 -1.586  -30.299 1.00 17.96 ? 486  CYS   B CB  1 
ATOM   3241 S  SG  . CYS   B 1 45  ? -17.613 -0.193  -31.293 1.00 16.79 ? 486  CYS   B SG  1 
ATOM   3242 N  N   . HIS   B 1 46  ? -20.849 -2.833  -29.105 1.00 18.31 ? 487  HIS   B N   1 
ATOM   3243 C  CA  . HIS   B 1 46  ? -21.467 -4.120  -28.816 1.00 16.90 ? 487  HIS   B CA  1 
ATOM   3244 C  C   . HIS   B 1 46  ? -21.049 -5.108  -29.899 1.00 16.90 ? 487  HIS   B C   1 
ATOM   3245 O  O   . HIS   B 1 46  ? -21.280 -4.863  -31.089 1.00 16.33 ? 487  HIS   B O   1 
ATOM   3246 C  CB  . HIS   B 1 46  ? -22.989 -4.008  -28.769 1.00 18.73 ? 487  HIS   B CB  1 
ATOM   3247 C  CG  . HIS   B 1 46  ? -23.660 -5.322  -28.535 1.00 19.09 ? 487  HIS   B CG  1 
ATOM   3248 N  ND1 . HIS   B 1 46  ? -23.549 -6.015  -27.347 1.00 21.70 ? 487  HIS   B ND1 1 
ATOM   3249 C  CD2 . HIS   B 1 46  ? -24.401 -6.102  -29.358 1.00 27.87 ? 487  HIS   B CD2 1 
ATOM   3250 C  CE1 . HIS   B 1 46  ? -24.221 -7.149  -27.438 1.00 31.23 ? 487  HIS   B CE1 1 
ATOM   3251 N  NE2 . HIS   B 1 46  ? -24.749 -7.226  -28.647 1.00 43.02 ? 487  HIS   B NE2 1 
ATOM   3252 N  N   . ARG   B 1 47  ? -20.464 -6.220  -29.494 1.00 15.20 ? 488  ARG   B N   1 
ATOM   3253 C  CA  . ARG   B 1 47  ? -19.960 -7.211  -30.444 1.00 17.23 ? 488  ARG   B CA  1 
ATOM   3254 C  C   . ARG   B 1 47  ? -21.111 -8.006  -31.062 1.00 21.77 ? 488  ARG   B C   1 
ATOM   3255 O  O   . ARG   B 1 47  ? -21.907 -8.625  -30.346 1.00 22.17 ? 488  ARG   B O   1 
ATOM   3256 C  CB  . ARG   B 1 47  ? -19.008 -8.146  -29.712 1.00 19.20 ? 488  ARG   B CB  1 
ATOM   3257 C  CG  . ARG   B 1 47  ? -18.079 -8.924  -30.596 1.00 29.52 ? 488  ARG   B CG  1 
ATOM   3258 C  CD  . ARG   B 1 47  ? -17.005 -8.063  -31.263 1.00 21.35 ? 488  ARG   B CD  1 
ATOM   3259 N  NE  . ARG   B 1 47  ? -16.162 -8.967  -32.012 1.00 24.51 ? 488  ARG   B NE  1 
ATOM   3260 C  CZ  . ARG   B 1 47  ? -15.011 -9.451  -31.566 1.00 17.22 ? 488  ARG   B CZ  1 
ATOM   3261 N  NH1 . ARG   B 1 47  ? -14.541 -9.092  -30.376 1.00 21.27 ? 488  ARG   B NH1 1 
ATOM   3262 N  NH2 . ARG   B 1 47  ? -14.338 -10.300 -32.324 1.00 22.97 ? 488  ARG   B NH2 1 
ATOM   3263 N  N   . ILE   B 1 48  ? -21.186 -7.990  -32.387 1.00 17.45 ? 489  ILE   B N   1 
ATOM   3264 C  CA  . ILE   B 1 48  ? -22.164 -8.755  -33.161 1.00 16.88 ? 489  ILE   B CA  1 
ATOM   3265 C  C   . ILE   B 1 48  ? -21.442 -9.973  -33.728 1.00 18.07 ? 489  ILE   B C   1 
ATOM   3266 O  O   . ILE   B 1 48  ? -20.341 -9.822  -34.278 1.00 18.88 ? 489  ILE   B O   1 
ATOM   3267 C  CB  . ILE   B 1 48  ? -22.738 -7.883  -34.290 1.00 16.46 ? 489  ILE   B CB  1 
ATOM   3268 C  CG1 . ILE   B 1 48  ? -23.556 -6.743  -33.683 1.00 18.30 ? 489  ILE   B CG1 1 
ATOM   3269 C  CG2 . ILE   B 1 48  ? -23.517 -8.731  -35.304 1.00 18.05 ? 489  ILE   B CG2 1 
ATOM   3270 C  CD1 . ILE   B 1 48  ? -24.022 -5.708  -34.676 1.00 20.35 ? 489  ILE   B CD1 1 
ATOM   3271 N  N   . PRO   B 1 49  ? -21.989 -11.176 -33.604 1.00 19.11 ? 490  PRO   B N   1 
ATOM   3272 C  CA  . PRO   B 1 49  ? -21.275 -12.358 -34.095 1.00 19.08 ? 490  PRO   B CA  1 
ATOM   3273 C  C   . PRO   B 1 49  ? -21.306 -12.458 -35.609 1.00 17.76 ? 490  PRO   B C   1 
ATOM   3274 O  O   . PRO   B 1 49  ? -22.252 -12.015 -36.259 1.00 18.87 ? 490  PRO   B O   1 
ATOM   3275 C  CB  . PRO   B 1 49  ? -22.058 -13.522 -33.470 1.00 22.96 ? 490  PRO   B CB  1 
ATOM   3276 C  CG  . PRO   B 1 49  ? -23.422 -12.977 -33.253 1.00 24.84 ? 490  PRO   B CG  1 
ATOM   3277 C  CD  . PRO   B 1 49  ? -23.221 -11.536 -32.879 1.00 22.24 ? 490  PRO   B CD  1 
ATOM   3278 N  N   . ALA   B 1 50  ? -20.253 -13.057 -36.163 1.00 18.81 ? 491  ALA   B N   1 
ATOM   3279 C  CA  . ALA   B 1 50  ? -20.281 -13.465 -37.559 1.00 18.11 ? 491  ALA   B CA  1 
ATOM   3280 C  C   . ALA   B 1 50  ? -21.149 -14.713 -37.724 1.00 19.68 ? 491  ALA   B C   1 
ATOM   3281 O  O   . ALA   B 1 50  ? -21.389 -15.460 -36.772 1.00 21.69 ? 491  ALA   B O   1 
ATOM   3282 C  CB  . ALA   B 1 50  ? -18.869 -13.782 -38.047 1.00 19.30 ? 491  ALA   B CB  1 
ATOM   3283 N  N   . ARG   B 1 51  ? -21.643 -14.924 -38.947 1.00 18.90 ? 492  ARG   B N   1 
ATOM   3284 C  CA  . ARG   B 1 51  ? -22.278 -16.187 -39.318 1.00 20.56 ? 492  ARG   B CA  1 
ATOM   3285 C  C   . ARG   B 1 51  ? -22.051 -16.404 -40.806 1.00 25.87 ? 492  ARG   B C   1 
ATOM   3286 O  O   . ARG   B 1 51  ? -21.671 -15.485 -41.534 1.00 21.13 ? 492  ARG   B O   1 
ATOM   3287 C  CB  . ARG   B 1 51  ? -23.789 -16.209 -39.019 1.00 20.88 ? 492  ARG   B CB  1 
ATOM   3288 C  CG  . ARG   B 1 51  ? -24.640 -15.285 -39.907 1.00 19.53 ? 492  ARG   B CG  1 
ATOM   3289 C  CD  . ARG   B 1 51  ? -26.122 -15.644 -39.811 1.00 20.05 ? 492  ARG   B CD  1 
ATOM   3290 N  NE  . ARG   B 1 51  ? -27.046 -14.713 -40.455 1.00 18.86 ? 492  ARG   B NE  1 
ATOM   3291 C  CZ  . ARG   B 1 51  ? -27.536 -14.867 -41.682 1.00 18.02 ? 492  ARG   B CZ  1 
ATOM   3292 N  NH1 . ARG   B 1 51  ? -27.137 -15.881 -42.434 1.00 21.27 ? 492  ARG   B NH1 1 
ATOM   3293 N  NH2 . ARG   B 1 51  ? -28.399 -14.000 -42.164 1.00 17.78 ? 492  ARG   B NH2 1 
ATOM   3294 N  N   . LEU   B 1 52  ? -22.283 -17.635 -41.257 1.00 21.79 ? 493  LEU   B N   1 
ATOM   3295 C  CA  . LEU   B 1 52  ? -22.258 -17.929 -42.684 1.00 20.93 ? 493  LEU   B CA  1 
ATOM   3296 C  C   . LEU   B 1 52  ? -23.529 -17.420 -43.334 1.00 24.28 ? 493  LEU   B C   1 
ATOM   3297 O  O   . LEU   B 1 52  ? -24.627 -17.646 -42.825 1.00 20.50 ? 493  LEU   B O   1 
ATOM   3298 C  CB  . LEU   B 1 52  ? -22.192 -19.434 -42.924 1.00 23.29 ? 493  LEU   B CB  1 
ATOM   3299 C  CG  . LEU   B 1 52  ? -21.001 -20.204 -42.398 1.00 22.36 ? 493  LEU   B CG  1 
ATOM   3300 C  CD1 . LEU   B 1 52  ? -21.246 -21.710 -42.542 1.00 27.76 ? 493  LEU   B CD1 1 
ATOM   3301 C  CD2 . LEU   B 1 52  ? -19.747 -19.781 -43.150 1.00 21.09 ? 493  LEU   B CD2 1 
ATOM   3302 N  N   . ALA   B 1 53  ? -23.385 -16.734 -44.459 1.00 17.76 ? 494  ALA   B N   1 
ATOM   3303 C  CA  . ALA   B 1 53  ? -24.502 -16.579 -45.370 1.00 18.38 ? 494  ALA   B CA  1 
ATOM   3304 C  C   . ALA   B 1 53  ? -24.930 -17.960 -45.849 1.00 18.85 ? 494  ALA   B C   1 
ATOM   3305 O  O   . ALA   B 1 53  ? -24.107 -18.872 -45.972 1.00 20.63 ? 494  ALA   B O   1 
ATOM   3306 C  CB  . ALA   B 1 53  ? -24.052 -15.736 -46.561 1.00 19.16 ? 494  ALA   B CB  1 
ATOM   3307 N  N   . THR   B 1 54  ? -26.231 -18.120 -46.072 1.00 20.42 ? 495  THR   B N   1 
ATOM   3308 C  CA  . THR   B 1 54  ? -26.748 -19.319 -46.710 1.00 25.53 ? 495  THR   B CA  1 
ATOM   3309 C  C   . THR   B 1 54  ? -26.660 -19.191 -48.226 1.00 33.72 ? 495  THR   B C   1 
ATOM   3310 O  O   . THR   B 1 54  ? -26.573 -18.092 -48.784 1.00 19.90 ? 495  THR   B O   1 
ATOM   3311 C  CB  . THR   B 1 54  ? -28.203 -19.572 -46.307 1.00 19.64 ? 495  THR   B CB  1 
ATOM   3312 O  OG1 . THR   B 1 54  ? -29.054 -18.563 -46.860 1.00 22.76 ? 495  THR   B OG1 1 
ATOM   3313 C  CG2 . THR   B 1 54  ? -28.340 -19.585 -44.782 1.00 28.24 ? 495  THR   B CG2 1 
ATOM   3314 N  N   . GLU   B 1 55  ? -26.696 -20.344 -48.898 1.00 33.29 ? 496  GLU   B N   1 
ATOM   3315 C  CA  . GLU   B 1 55  ? -26.748 -20.328 -50.356 1.00 21.53 ? 496  GLU   B CA  1 
ATOM   3316 C  C   . GLU   B 1 55  ? -28.004 -19.634 -50.859 1.00 21.14 ? 496  GLU   B C   1 
ATOM   3317 O  O   . GLU   B 1 55  ? -27.963 -18.965 -51.895 1.00 21.33 ? 496  GLU   B O   1 
ATOM   3318 C  CB  . GLU   B 1 55  ? -26.653 -21.752 -50.909 1.00 29.92 ? 496  GLU   B CB  1 
ATOM   3319 C  CG  . GLU   B 1 55  ? -25.375 -22.464 -50.526 1.00 32.60 ? 496  GLU   B CG  1 
ATOM   3320 C  CD  . GLU   B 1 55  ? -25.214 -23.808 -51.214 1.00 40.60 ? 496  GLU   B CD  1 
ATOM   3321 O  OE1 . GLU   B 1 55  ? -25.641 -23.942 -52.381 1.00 39.75 ? 496  GLU   B OE1 1 
ATOM   3322 O  OE2 . GLU   B 1 55  ? -24.662 -24.732 -50.583 1.00 43.01 ? 496  GLU   B OE2 1 
ATOM   3323 N  N   . GLU   B 1 56  ? -29.125 -19.765 -50.144 1.00 21.37 ? 497  GLU   B N   1 
ATOM   3324 C  CA  . GLU   B 1 56  ? -30.323 -19.040 -50.542 1.00 24.76 ? 497  GLU   B CA  1 
ATOM   3325 C  C   . GLU   B 1 56  ? -30.120 -17.535 -50.415 1.00 21.24 ? 497  GLU   B C   1 
ATOM   3326 O  O   . GLU   B 1 56  ? -30.601 -16.767 -51.249 1.00 22.45 ? 497  GLU   B O   1 
ATOM   3327 C  CB  . GLU   B 1 56  ? -31.528 -19.503 -49.726 1.00 30.13 ? 497  GLU   B CB  1 
ATOM   3328 C  CG  . GLU   B 1 56  ? -32.829 -18.809 -50.119 1.00 42.58 ? 497  GLU   B CG  1 
ATOM   3329 C  CD  . GLU   B 1 56  ? -33.984 -19.149 -49.189 1.00 64.54 ? 497  GLU   B CD  1 
ATOM   3330 O  OE1 . GLU   B 1 56  ? -33.764 -19.891 -48.207 1.00 65.17 ? 497  GLU   B OE1 1 
ATOM   3331 O  OE2 . GLU   B 1 56  ? -35.112 -18.679 -49.446 1.00 59.96 ? 497  GLU   B OE2 1 
ATOM   3332 N  N   . GLU   B 1 57  ? -29.408 -17.095 -49.373 1.00 21.51 ? 498  GLU   B N   1 
ATOM   3333 C  CA  . GLU   B 1 57  ? -29.098 -15.674 -49.259 1.00 18.97 ? 498  GLU   B CA  1 
ATOM   3334 C  C   . GLU   B 1 57  ? -28.209 -15.196 -50.401 1.00 18.58 ? 498  GLU   B C   1 
ATOM   3335 O  O   . GLU   B 1 57  ? -28.455 -14.124 -50.967 1.00 18.97 ? 498  GLU   B O   1 
ATOM   3336 C  CB  . GLU   B 1 57  ? -28.479 -15.358 -47.895 1.00 19.90 ? 498  GLU   B CB  1 
ATOM   3337 C  CG  . GLU   B 1 57  ? -29.544 -15.238 -46.803 1.00 18.36 ? 498  GLU   B CG  1 
ATOM   3338 C  CD  . GLU   B 1 57  ? -29.003 -15.465 -45.400 1.00 22.52 ? 498  GLU   B CD  1 
ATOM   3339 O  OE1 . GLU   B 1 57  ? -27.845 -15.893 -45.251 1.00 19.23 ? 498  GLU   B OE1 1 
ATOM   3340 O  OE2 . GLU   B 1 57  ? -29.751 -15.218 -44.431 1.00 22.04 ? 498  GLU   B OE2 1 
ATOM   3341 N  N   . LEU   B 1 58  ? -27.193 -15.982 -50.764 1.00 18.07 ? 499  LEU   B N   1 
ATOM   3342 C  CA  . LEU   B 1 58  ? -26.350 -15.595 -51.898 1.00 17.99 ? 499  LEU   B CA  1 
ATOM   3343 C  C   . LEU   B 1 58  ? -27.160 -15.432 -53.180 1.00 26.95 ? 499  LEU   B C   1 
ATOM   3344 O  O   . LEU   B 1 58  ? -26.846 -14.562 -54.006 1.00 19.19 ? 499  LEU   B O   1 
ATOM   3345 C  CB  . LEU   B 1 58  ? -25.221 -16.600 -52.121 1.00 21.25 ? 499  LEU   B CB  1 
ATOM   3346 C  CG  . LEU   B 1 58  ? -24.225 -16.874 -50.995 1.00 18.88 ? 499  LEU   B CG  1 
ATOM   3347 C  CD1 . LEU   B 1 58  ? -23.271 -17.961 -51.441 1.00 22.29 ? 499  LEU   B CD1 1 
ATOM   3348 C  CD2 . LEU   B 1 58  ? -23.467 -15.618 -50.632 1.00 21.16 ? 499  LEU   B CD2 1 
ATOM   3349 N  N   . ALA   B 1 59  ? -28.203 -16.253 -53.363 1.00 21.56 ? 500  ALA   B N   1 
ATOM   3350 C  CA  . ALA   B 1 59  ? -29.061 -16.164 -54.536 1.00 24.21 ? 500  ALA   B CA  1 
ATOM   3351 C  C   . ALA   B 1 59  ? -29.853 -14.866 -54.600 1.00 23.18 ? 500  ALA   B C   1 
ATOM   3352 O  O   . ALA   B 1 59  ? -30.479 -14.594 -55.633 1.00 23.30 ? 500  ALA   B O   1 
ATOM   3353 C  CB  . ALA   B 1 59  ? -30.015 -17.360 -54.576 1.00 27.86 ? 500  ALA   B CB  1 
ATOM   3354 N  N   . LEU   B 1 60  ? -29.847 -14.055 -53.533 1.00 21.48 ? 501  LEU   B N   1 
ATOM   3355 C  CA  . LEU   B 1 60  ? -30.472 -12.744 -53.629 1.00 22.80 ? 501  LEU   B CA  1 
ATOM   3356 C  C   . LEU   B 1 60  ? -29.817 -11.889 -54.709 1.00 17.99 ? 501  LEU   B C   1 
ATOM   3357 O  O   . LEU   B 1 60  ? -30.461 -10.995 -55.267 1.00 21.09 ? 501  LEU   B O   1 
ATOM   3358 C  CB  . LEU   B 1 60  ? -30.415 -12.025 -52.280 1.00 20.94 ? 501  LEU   B CB  1 
ATOM   3359 C  CG  . LEU   B 1 60  ? -31.301 -12.599 -51.179 1.00 19.77 ? 501  LEU   B CG  1 
ATOM   3360 C  CD1 . LEU   B 1 60  ? -30.884 -12.007 -49.833 1.00 24.22 ? 501  LEU   B CD1 1 
ATOM   3361 C  CD2 . LEU   B 1 60  ? -32.783 -12.328 -51.463 1.00 25.00 ? 501  LEU   B CD2 1 
ATOM   3362 N  N   . CYS   B 1 61  ? -28.527 -12.119 -54.988 1.00 17.64 ? 502  CYS   B N   1 
ATOM   3363 C  CA  . CYS   B 1 61  ? -27.799 -11.333 -55.969 1.00 18.55 ? 502  CYS   B CA  1 
ATOM   3364 C  C   . CYS   B 1 61  ? -27.018 -12.169 -56.973 1.00 17.58 ? 502  CYS   B C   1 
ATOM   3365 O  O   . CYS   B 1 61  ? -26.657 -11.635 -58.029 1.00 21.37 ? 502  CYS   B O   1 
ATOM   3366 C  CB  . CYS   B 1 61  ? -26.814 -10.380 -55.267 1.00 17.24 ? 502  CYS   B CB  1 
ATOM   3367 S  SG  . CYS   B 1 61  ? -27.593 -9.162  -54.196 1.00 18.15 ? 502  CYS   B SG  1 
ATOM   3368 N  N   . HIS   B 1 62  ? -26.740 -13.442 -56.696 1.00 17.09 ? 503  HIS   B N   1 
ATOM   3369 C  CA  . HIS   B 1 62  ? -25.806 -14.204 -57.511 1.00 20.26 ? 503  HIS   B CA  1 
ATOM   3370 C  C   . HIS   B 1 62  ? -26.483 -15.391 -58.181 1.00 22.70 ? 503  HIS   B C   1 
ATOM   3371 O  O   . HIS   B 1 62  ? -27.480 -15.928 -57.684 1.00 22.54 ? 503  HIS   B O   1 
ATOM   3372 C  CB  . HIS   B 1 62  ? -24.609 -14.653 -56.671 1.00 17.85 ? 503  HIS   B CB  1 
ATOM   3373 C  CG  . HIS   B 1 62  ? -23.776 -13.507 -56.186 1.00 16.93 ? 503  HIS   B CG  1 
ATOM   3374 N  ND1 . HIS   B 1 62  ? -22.941 -12.797 -57.018 1.00 17.59 ? 503  HIS   B ND1 1 
ATOM   3375 C  CD2 . HIS   B 1 62  ? -23.681 -12.925 -54.967 1.00 18.14 ? 503  HIS   B CD2 1 
ATOM   3376 C  CE1 . HIS   B 1 62  ? -22.358 -11.829 -56.332 1.00 17.07 ? 503  HIS   B CE1 1 
ATOM   3377 N  NE2 . HIS   B 1 62  ? -22.786 -11.889 -55.086 1.00 18.24 ? 503  HIS   B NE2 1 
ATOM   3378 N  N   . SER   B 1 63  ? -25.929 -15.763 -59.333 1.00 22.41 ? 504  SER   B N   1 
ATOM   3379 C  CA  . SER   B 1 63  ? -26.444 -16.873 -60.114 1.00 22.77 ? 504  SER   B CA  1 
ATOM   3380 C  C   . SER   B 1 63  ? -26.095 -18.188 -59.439 1.00 19.69 ? 504  SER   B C   1 
ATOM   3381 O  O   . SER   B 1 63  ? -25.107 -18.300 -58.709 1.00 21.23 ? 504  SER   B O   1 
ATOM   3382 C  CB  . SER   B 1 63  ? -25.807 -16.855 -61.502 1.00 21.55 ? 504  SER   B CB  1 
ATOM   3383 O  OG  . SER   B 1 63  ? -24.473 -17.326 -61.445 1.00 24.52 ? 504  SER   B OG  1 
ATOM   3384 N  N   A SER   B 1 64  ? -26.931 -19.202 -59.676 0.83 21.75 ? 505  SER   B N   1 
ATOM   3385 N  N   B SER   B 1 64  ? -26.922 -19.203 -59.702 0.17 16.46 ? 505  SER   B N   1 
ATOM   3386 C  CA  A SER   B 1 64  ? -26.636 -20.514 -59.114 0.83 20.69 ? 505  SER   B CA  1 
ATOM   3387 C  CA  B SER   B 1 64  ? -26.659 -20.522 -59.141 0.17 19.34 ? 505  SER   B CA  1 
ATOM   3388 C  C   A SER   B 1 64  ? -25.310 -21.061 -59.627 0.83 19.24 ? 505  SER   B C   1 
ATOM   3389 C  C   B SER   B 1 64  ? -25.343 -21.097 -59.647 0.17 18.67 ? 505  SER   B C   1 
ATOM   3390 O  O   A SER   B 1 64  ? -24.591 -21.732 -58.884 0.83 22.85 ? 505  SER   B O   1 
ATOM   3391 O  O   B SER   B 1 64  ? -24.666 -21.828 -58.916 0.17 20.42 ? 505  SER   B O   1 
ATOM   3392 C  CB  A SER   B 1 64  ? -27.766 -21.489 -59.428 0.83 25.38 ? 505  SER   B CB  1 
ATOM   3393 C  CB  B SER   B 1 64  ? -27.816 -21.472 -59.449 0.17 19.61 ? 505  SER   B CB  1 
ATOM   3394 O  OG  A SER   B 1 64  ? -27.730 -21.838 -60.791 0.83 26.49 ? 505  SER   B OG  1 
ATOM   3395 O  OG  B SER   B 1 64  ? -27.951 -22.434 -58.419 0.17 19.03 ? 505  SER   B OG  1 
ATOM   3396 N  N   . LYS   B 1 65  ? -24.957 -20.774 -60.885 1.00 20.84 ? 506  LYS   B N   1 
ATOM   3397 C  CA  . LYS   B 1 65  ? -23.702 -21.290 -61.422 1.00 23.22 ? 506  LYS   B CA  1 
ATOM   3398 C  C   . LYS   B 1 65  ? -22.497 -20.695 -60.702 1.00 20.57 ? 506  LYS   B C   1 
ATOM   3399 O  O   . LYS   B 1 65  ? -21.548 -21.407 -60.356 1.00 19.16 ? 506  LYS   B O   1 
ATOM   3400 C  CB  . LYS   B 1 65  ? -23.606 -20.999 -62.923 1.00 22.69 ? 506  LYS   B CB  1 
ATOM   3401 C  CG  . LYS   B 1 65  ? -22.238 -21.337 -63.512 1.00 30.39 ? 506  LYS   B CG  1 
ATOM   3402 C  CD  . LYS   B 1 65  ? -22.238 -21.260 -65.032 1.00 32.55 ? 506  LYS   B CD  1 
ATOM   3403 C  CE  . LYS   B 1 65  ? -20.831 -21.439 -65.595 1.00 39.09 ? 506  LYS   B CE  1 
ATOM   3404 N  NZ  . LYS   B 1 65  ? -19.946 -20.270 -65.309 1.00 38.42 ? 506  LYS   B NZ  1 
ATOM   3405 N  N   . HIS   B 1 66  ? -22.522 -19.385 -60.469 1.00 21.98 ? 507  HIS   B N   1 
ATOM   3406 C  CA  . HIS   B 1 66  ? -21.403 -18.733 -59.808 1.00 21.54 ? 507  HIS   B CA  1 
ATOM   3407 C  C   . HIS   B 1 66  ? -21.274 -19.212 -58.369 1.00 19.28 ? 507  HIS   B C   1 
ATOM   3408 O  O   . HIS   B 1 66  ? -20.170 -19.538 -57.912 1.00 20.56 ? 507  HIS   B O   1 
ATOM   3409 C  CB  . HIS   B 1 66  ? -21.592 -17.217 -59.882 1.00 23.54 ? 507  HIS   B CB  1 
ATOM   3410 C  CG  . HIS   B 1 66  ? -20.571 -16.450 -59.110 1.00 18.64 ? 507  HIS   B CG  1 
ATOM   3411 N  ND1 . HIS   B 1 66  ? -19.219 -16.535 -59.370 1.00 18.62 ? 507  HIS   B ND1 1 
ATOM   3412 C  CD2 . HIS   B 1 66  ? -20.699 -15.613 -58.052 1.00 21.94 ? 507  HIS   B CD2 1 
ATOM   3413 C  CE1 . HIS   B 1 66  ? -18.560 -15.768 -58.521 1.00 18.95 ? 507  HIS   B CE1 1 
ATOM   3414 N  NE2 . HIS   B 1 66  ? -19.437 -15.191 -57.718 1.00 19.93 ? 507  HIS   B NE2 1 
ATOM   3415 N  N   . ILE   B 1 67  ? -22.405 -19.273 -57.649 1.00 19.89 ? 508  ILE   B N   1 
ATOM   3416 C  CA  . ILE   B 1 67  ? -22.401 -19.833 -56.299 1.00 20.57 ? 508  ILE   B CA  1 
ATOM   3417 C  C   . ILE   B 1 67  ? -21.782 -21.222 -56.319 1.00 23.80 ? 508  ILE   B C   1 
ATOM   3418 O  O   . ILE   B 1 67  ? -20.900 -21.539 -55.524 1.00 21.27 ? 508  ILE   B O   1 
ATOM   3419 C  CB  . ILE   B 1 67  ? -23.820 -19.851 -55.706 1.00 20.37 ? 508  ILE   B CB  1 
ATOM   3420 C  CG1 . ILE   B 1 67  ? -24.364 -18.427 -55.539 1.00 18.36 ? 508  ILE   B CG1 1 
ATOM   3421 C  CG2 . ILE   B 1 67  ? -23.824 -20.599 -54.367 1.00 21.91 ? 508  ILE   B CG2 1 
ATOM   3422 C  CD1 . ILE   B 1 67  ? -25.847 -18.363 -55.312 1.00 22.13 ? 508  ILE   B CD1 1 
ATOM   3423 N  N   . SER   B 1 68  ? -22.191 -22.053 -57.285 1.00 22.63 ? 509  SER   B N   1 
ATOM   3424 C  CA  . SER   B 1 68  ? -21.724 -23.434 -57.289 1.00 27.47 ? 509  SER   B CA  1 
ATOM   3425 C  C   . SER   B 1 68  ? -20.235 -23.537 -57.588 1.00 21.73 ? 509  SER   B C   1 
ATOM   3426 O  O   . SER   B 1 68  ? -19.539 -24.359 -56.982 1.00 22.82 ? 509  SER   B O   1 
ATOM   3427 C  CB  . SER   B 1 68  ? -22.541 -24.240 -58.288 1.00 30.57 ? 509  SER   B CB  1 
ATOM   3428 O  OG  . SER   B 1 68  ? -23.823 -24.487 -57.739 1.00 56.62 ? 509  SER   B OG  1 
ATOM   3429 N  N   . ILE   B 1 69  ? -19.721 -22.703 -58.495 1.00 22.85 ? 510  ILE   B N   1 
ATOM   3430 C  CA  . ILE   B 1 69  ? -18.301 -22.762 -58.830 1.00 21.09 ? 510  ILE   B CA  1 
ATOM   3431 C  C   . ILE   B 1 69  ? -17.447 -22.357 -57.634 1.00 21.54 ? 510  ILE   B C   1 
ATOM   3432 O  O   . ILE   B 1 69  ? -16.497 -23.054 -57.267 1.00 24.61 ? 510  ILE   B O   1 
ATOM   3433 C  CB  . ILE   B 1 69  ? -17.994 -21.901 -60.070 1.00 22.00 ? 510  ILE   B CB  1 
ATOM   3434 C  CG1 . ILE   B 1 69  ? -18.569 -22.543 -61.333 1.00 27.76 ? 510  ILE   B CG1 1 
ATOM   3435 C  CG2 . ILE   B 1 69  ? -16.495 -21.736 -60.232 1.00 26.89 ? 510  ILE   B CG2 1 
ATOM   3436 C  CD1 . ILE   B 1 69  ? -18.527 -21.622 -62.549 1.00 29.65 ? 510  ILE   B CD1 1 
ATOM   3437 N  N   . ILE   B 1 70  ? -17.768 -21.221 -57.015 1.00 22.82 ? 511  ILE   B N   1 
ATOM   3438 C  CA  . ILE   B 1 70  ? -17.016 -20.775 -55.841 1.00 23.72 ? 511  ILE   B CA  1 
ATOM   3439 C  C   . ILE   B 1 70  ? -17.152 -21.778 -54.700 1.00 22.86 ? 511  ILE   B C   1 
ATOM   3440 O  O   . ILE   B 1 70  ? -16.166 -22.103 -54.026 1.00 22.93 ? 511  ILE   B O   1 
ATOM   3441 C  CB  . ILE   B 1 70  ? -17.446 -19.354 -55.428 1.00 20.13 ? 511  ILE   B CB  1 
ATOM   3442 C  CG1 . ILE   B 1 70  ? -17.266 -18.374 -56.594 1.00 18.47 ? 511  ILE   B CG1 1 
ATOM   3443 C  CG2 . ILE   B 1 70  ? -16.631 -18.868 -54.265 1.00 21.35 ? 511  ILE   B CG2 1 
ATOM   3444 C  CD1 . ILE   B 1 70  ? -15.882 -18.335 -57.174 1.00 19.99 ? 511  ILE   B CD1 1 
ATOM   3445 N  N   . LYS   B 1 71  ? -18.370 -22.290 -54.481 1.00 22.96 ? 512  LYS   B N   1 
ATOM   3446 C  CA  . LYS   B 1 71  ? -18.584 -23.336 -53.479 1.00 21.54 ? 512  LYS   B CA  1 
ATOM   3447 C  C   . LYS   B 1 71  ? -17.694 -24.541 -53.754 1.00 22.27 ? 512  LYS   B C   1 
ATOM   3448 O  O   . LYS   B 1 71  ? -17.033 -25.059 -52.845 1.00 25.89 ? 512  LYS   B O   1 
ATOM   3449 C  CB  . LYS   B 1 71  ? -20.068 -23.727 -53.442 1.00 21.83 ? 512  LYS   B CB  1 
ATOM   3450 C  CG  . LYS   B 1 71  ? -20.431 -24.849 -52.472 1.00 25.64 ? 512  LYS   B CG  1 
ATOM   3451 C  CD  . LYS   B 1 71  ? -21.875 -25.280 -52.649 1.00 28.00 ? 512  LYS   B CD  1 
ATOM   3452 C  CE  . LYS   B 1 71  ? -22.227 -26.422 -51.707 1.00 37.22 ? 512  LYS   B CE  1 
ATOM   3453 N  NZ  . LYS   B 1 71  ? -23.453 -27.112 -52.169 1.00 39.04 ? 512  LYS   B NZ  1 
ATOM   3454 N  N   . SER   B 1 72  ? -17.633 -24.979 -55.015 1.00 22.41 ? 513  SER   B N   1 
ATOM   3455 C  CA  . SER   B 1 72  ? -16.808 -26.127 -55.370 1.00 26.96 ? 513  SER   B CA  1 
ATOM   3456 C  C   . SER   B 1 72  ? -15.334 -25.904 -55.074 1.00 30.99 ? 513  SER   B C   1 
ATOM   3457 O  O   . SER   B 1 72  ? -14.581 -26.878 -54.964 1.00 32.79 ? 513  SER   B O   1 
ATOM   3458 C  CB  . SER   B 1 72  ? -16.988 -26.463 -56.852 1.00 28.40 ? 513  SER   B CB  1 
ATOM   3459 O  OG  . SER   B 1 72  ? -16.092 -25.717 -57.649 1.00 29.43 ? 513  SER   B OG  1 
ATOM   3460 N  N   . SER   B 1 73  ? -14.892 -24.649 -54.939 1.00 26.68 ? 514  SER   B N   1 
ATOM   3461 C  CA  . SER   B 1 73  ? -13.468 -24.432 -54.739 1.00 19.87 ? 514  SER   B CA  1 
ATOM   3462 C  C   . SER   B 1 73  ? -13.004 -24.890 -53.364 1.00 25.37 ? 514  SER   B C   1 
ATOM   3463 O  O   . SER   B 1 73  ? -11.807 -25.104 -53.178 1.00 23.45 ? 514  SER   B O   1 
ATOM   3464 C  CB  . SER   B 1 73  ? -13.089 -22.962 -54.950 1.00 29.21 ? 514  SER   B CB  1 
ATOM   3465 O  OG  . SER   B 1 73  ? -13.766 -22.119 -54.035 1.00 23.11 ? 514  SER   B OG  1 
ATOM   3466 N  N   . GLU   B 1 74  ? -13.925 -25.051 -52.407 1.00 25.79 ? 515  GLU   B N   1 
ATOM   3467 C  CA  . GLU   B 1 74  ? -13.543 -25.492 -51.065 1.00 29.27 ? 515  GLU   B CA  1 
ATOM   3468 C  C   . GLU   B 1 74  ? -12.804 -26.823 -51.101 1.00 33.50 ? 515  GLU   B C   1 
ATOM   3469 O  O   . GLU   B 1 74  ? -11.886 -27.048 -50.303 1.00 33.72 ? 515  GLU   B O   1 
ATOM   3470 C  CB  . GLU   B 1 74  ? -14.783 -25.595 -50.171 1.00 25.68 ? 515  GLU   B CB  1 
ATOM   3471 C  CG  . GLU   B 1 74  ? -14.470 -25.916 -48.703 1.00 27.11 ? 515  GLU   B CG  1 
ATOM   3472 C  CD  . GLU   B 1 74  ? -15.698 -25.900 -47.806 1.00 43.34 ? 515  GLU   B CD  1 
ATOM   3473 O  OE1 . GLU   B 1 74  ? -16.800 -25.568 -48.291 1.00 48.00 ? 515  GLU   B OE1 1 
ATOM   3474 O  OE2 . GLU   B 1 74  ? -15.556 -26.209 -46.603 1.00 51.54 ? 515  GLU   B OE2 1 
ATOM   3475 N  N   . HIS   B 1 75  ? -13.162 -27.699 -52.041 1.00 38.46 ? 516  HIS   B N   1 
ATOM   3476 C  CA  . HIS   B 1 75  ? -12.624 -29.052 -52.114 1.00 40.32 ? 516  HIS   B CA  1 
ATOM   3477 C  C   . HIS   B 1 75  ? -11.682 -29.243 -53.294 1.00 41.37 ? 516  HIS   B C   1 
ATOM   3478 O  O   . HIS   B 1 75  ? -11.409 -30.381 -53.683 1.00 43.18 ? 516  HIS   B O   1 
ATOM   3479 C  CB  . HIS   B 1 75  ? -13.766 -30.070 -52.153 1.00 30.96 ? 516  HIS   B CB  1 
ATOM   3480 C  CG  . HIS   B 1 75  ? -14.719 -29.933 -51.009 1.00 31.57 ? 516  HIS   B CG  1 
ATOM   3481 N  ND1 . HIS   B 1 75  ? -14.327 -30.079 -49.696 1.00 40.99 ? 516  HIS   B ND1 1 
ATOM   3482 C  CD2 . HIS   B 1 75  ? -16.039 -29.631 -50.977 1.00 38.69 ? 516  HIS   B CD2 1 
ATOM   3483 C  CE1 . HIS   B 1 75  ? -15.367 -29.889 -48.904 1.00 49.72 ? 516  HIS   B CE1 1 
ATOM   3484 N  NE2 . HIS   B 1 75  ? -16.419 -29.616 -49.656 1.00 51.11 ? 516  HIS   B NE2 1 
ATOM   3485 N  N   . MET   B 1 76  ? -11.172 -28.154 -53.865 1.00 34.42 ? 517  MET   B N   1 
ATOM   3486 C  CA  . MET   B 1 76  ? -10.278 -28.229 -55.009 1.00 35.10 ? 517  MET   B CA  1 
ATOM   3487 C  C   . MET   B 1 76  ? -8.833  -28.389 -54.558 1.00 35.86 ? 517  MET   B C   1 
ATOM   3488 O  O   . MET   B 1 76  ? -8.447  -27.956 -53.470 1.00 36.51 ? 517  MET   B O   1 
ATOM   3489 C  CB  . MET   B 1 76  ? -10.370 -26.953 -55.840 1.00 29.93 ? 517  MET   B CB  1 
ATOM   3490 C  CG  . MET   B 1 76  ? -11.520 -26.921 -56.804 1.00 22.92 ? 517  MET   B CG  1 
ATOM   3491 S  SD  . MET   B 1 76  ? -11.411 -25.429 -57.790 1.00 30.63 ? 517  MET   B SD  1 
ATOM   3492 C  CE  . MET   B 1 76  ? -12.898 -25.646 -58.772 1.00 33.24 ? 517  MET   B CE  1 
ATOM   3493 N  N   . LYS   B 1 77  ? -8.033  -29.013 -55.418 1.00 40.31 ? 518  LYS   B N   1 
ATOM   3494 C  CA  . LYS   B 1 77  ? -6.596  -29.063 -55.212 1.00 22.71 ? 518  LYS   B CA  1 
ATOM   3495 C  C   . LYS   B 1 77  ? -5.951  -27.794 -55.755 1.00 47.74 ? 518  LYS   B C   1 
ATOM   3496 O  O   . LYS   B 1 77  ? -6.552  -27.081 -56.564 1.00 29.92 ? 518  LYS   B O   1 
ATOM   3497 C  CB  . LYS   B 1 77  ? -6.009  -30.304 -55.880 1.00 41.98 ? 518  LYS   B CB  1 
ATOM   3498 C  CG  . LYS   B 1 77  ? -6.461  -31.598 -55.214 1.00 56.29 ? 518  LYS   B CG  1 
ATOM   3499 C  CD  . LYS   B 1 77  ? -6.873  -32.629 -56.240 1.00 50.76 ? 518  LYS   B CD  1 
ATOM   3500 C  CE  . LYS   B 1 77  ? -8.083  -32.141 -56.993 1.00 42.90 ? 518  LYS   B CE  1 
ATOM   3501 N  NZ  . LYS   B 1 77  ? -8.870  -33.247 -57.601 1.00 44.81 ? 518  LYS   B NZ  1 
ATOM   3502 N  N   . PRO   B 1 78  ? -4.735  -27.472 -55.294 1.00 25.16 ? 519  PRO   B N   1 
ATOM   3503 C  CA  . PRO   B 1 78  ? -4.088  -26.224 -55.729 1.00 41.27 ? 519  PRO   B CA  1 
ATOM   3504 C  C   . PRO   B 1 78  ? -4.081  -26.016 -57.226 1.00 51.82 ? 519  PRO   B C   1 
ATOM   3505 O  O   . PRO   B 1 78  ? -4.240  -24.878 -57.682 1.00 51.22 ? 519  PRO   B O   1 
ATOM   3506 C  CB  . PRO   B 1 78  ? -2.665  -26.367 -55.184 1.00 25.77 ? 519  PRO   B CB  1 
ATOM   3507 C  CG  . PRO   B 1 78  ? -2.824  -27.200 -53.972 1.00 37.88 ? 519  PRO   B CG  1 
ATOM   3508 C  CD  . PRO   B 1 78  ? -3.953  -28.155 -54.248 1.00 42.11 ? 519  PRO   B CD  1 
ATOM   3509 N  N   . ARG   B 1 79  ? -3.875  -27.077 -58.004 1.00 28.95 ? 520  ARG   B N   1 
ATOM   3510 C  CA  . ARG   B 1 79  ? -3.983  -26.937 -59.446 1.00 27.65 ? 520  ARG   B CA  1 
ATOM   3511 C  C   . ARG   B 1 79  ? -5.346  -26.400 -59.820 1.00 23.95 ? 520  ARG   B C   1 
ATOM   3512 O  O   . ARG   B 1 79  ? -5.465  -25.449 -60.602 1.00 51.91 ? 520  ARG   B O   1 
ATOM   3513 C  CB  . ARG   B 1 79  ? -3.740  -28.280 -60.129 1.00 42.10 ? 520  ARG   B CB  1 
ATOM   3514 C  CG  . ARG   B 1 79  ? -3.809  -28.210 -61.646 1.00 43.32 ? 520  ARG   B CG  1 
ATOM   3515 C  CD  . ARG   B 1 79  ? -3.852  -29.603 -62.266 1.00 50.28 ? 520  ARG   B CD  1 
ATOM   3516 N  NE  . ARG   B 1 79  ? -3.935  -29.561 -63.727 0.55 45.02 ? 520  ARG   B NE  1 
ATOM   3517 C  CZ  . ARG   B 1 79  ? -2.928  -29.243 -64.536 0.64 41.64 ? 520  ARG   B CZ  1 
ATOM   3518 N  NH1 . ARG   B 1 79  ? -1.732  -28.943 -64.043 1.00 43.45 ? 520  ARG   B NH1 1 
ATOM   3519 N  NH2 . ARG   B 1 79  ? -3.117  -29.234 -65.846 0.59 43.96 ? 520  ARG   B NH2 1 
ATOM   3520 N  N   . ASP   B 1 80  ? -6.390  -26.988 -59.247 1.00 29.40 ? 521  ASP   B N   1 
ATOM   3521 C  CA  . ASP   B 1 80  ? -7.731  -26.538 -59.575 1.00 33.33 ? 521  ASP   B CA  1 
ATOM   3522 C  C   . ASP   B 1 80  ? -7.940  -25.090 -59.159 1.00 52.87 ? 521  ASP   B C   1 
ATOM   3523 O  O   . ASP   B 1 80  ? -8.554  -24.308 -59.895 1.00 28.97 ? 521  ASP   B O   1 
ATOM   3524 C  CB  . ASP   B 1 80  ? -8.787  -27.442 -58.947 1.00 38.22 ? 521  ASP   B CB  1 
ATOM   3525 C  CG  . ASP   B 1 80  ? -8.757  -28.851 -59.491 1.00 56.28 ? 521  ASP   B CG  1 
ATOM   3526 O  OD1 . ASP   B 1 80  ? -8.169  -29.074 -60.573 1.00 36.83 ? 521  ASP   B OD1 1 
ATOM   3527 O  OD2 . ASP   B 1 80  ? -9.335  -29.737 -58.821 1.00 39.33 ? 521  ASP   B OD2 1 
ATOM   3528 N  N   . LEU   B 1 81  ? -7.391  -24.709 -58.005 1.00 38.94 ? 522  LEU   B N   1 
ATOM   3529 C  CA  . LEU   B 1 81  ? -7.608  -23.374 -57.453 1.00 32.43 ? 522  LEU   B CA  1 
ATOM   3530 C  C   . LEU   B 1 81  ? -6.905  -22.301 -58.277 1.00 31.46 ? 522  LEU   B C   1 
ATOM   3531 O  O   . LEU   B 1 81  ? -7.495  -21.261 -58.592 1.00 26.68 ? 522  LEU   B O   1 
ATOM   3532 C  CB  . LEU   B 1 81  ? -7.092  -23.339 -56.014 1.00 27.98 ? 522  LEU   B CB  1 
ATOM   3533 C  CG  . LEU   B 1 81  ? -7.958  -24.078 -54.996 1.00 23.35 ? 522  LEU   B CG  1 
ATOM   3534 C  CD1 . LEU   B 1 81  ? -7.182  -24.226 -53.702 1.00 28.12 ? 522  LEU   B CD1 1 
ATOM   3535 C  CD2 . LEU   B 1 81  ? -9.276  -23.356 -54.764 1.00 23.18 ? 522  LEU   B CD2 1 
ATOM   3536 N  N   . ASN   B 1 82  ? -5.654  -22.552 -58.657 1.00 25.10 ? 523  ASN   B N   1 
ATOM   3537 C  CA  . ASN   B 1 82  ? -4.872  -21.570 -59.461 1.00 33.89 ? 523  ASN   B CA  1 
ATOM   3538 C  C   . ASN   B 1 82  ? -5.564  -21.341 -60.813 1.00 51.08 ? 523  ASN   B C   1 
ATOM   3539 O  O   . ASN   B 1 82  ? -5.704  -20.190 -61.218 1.00 25.18 ? 523  ASN   B O   1 
ATOM   3540 C  CB  . ASN   B 1 82  ? -3.416  -21.980 -59.616 1.00 37.69 ? 523  ASN   B CB  1 
ATOM   3541 C  CG  . ASN   B 1 82  ? -2.509  -20.872 -60.105 1.00 62.42 ? 523  ASN   B CG  1 
ATOM   3542 O  OD1 . ASN   B 1 82  ? -2.751  -20.278 -61.158 1.00 77.71 ? 523  ASN   B OD1 1 
ATOM   3543 N  ND2 . ASN   B 1 82  ? -1.435  -20.594 -59.384 1.00 42.12 ? 523  ASN   B ND2 1 
ATOM   3544 N  N   . ARG   B 1 83  ? -5.966  -22.409 -61.494 1.00 37.22 ? 524  ARG   B N   1 
ATOM   3545 C  CA  . ARG   B 1 83  ? -6.573  -22.225 -62.835 1.00 36.20 ? 524  ARG   B CA  1 
ATOM   3546 C  C   . ARG   B 1 83  ? -7.951  -21.542 -62.716 1.00 33.75 ? 524  ARG   B C   1 
ATOM   3547 O  O   . ARG   B 1 83  ? -8.292  -20.774 -63.616 1.00 34.38 ? 524  ARG   B O   1 
ATOM   3548 C  CB  . ARG   B 1 83  ? -6.626  -23.571 -63.579 1.00 36.21 ? 524  ARG   B CB  1 
ATOM   3549 N  N   . LEU   B 1 84  ? -8.729  -21.872 -61.686 1.00 31.26 ? 525  LEU   B N   1 
ATOM   3550 C  CA  . LEU   B 1 84  ? -10.058 -21.248 -61.504 1.00 27.37 ? 525  LEU   B CA  1 
ATOM   3551 C  C   . LEU   B 1 84  ? -9.810  -19.749 -61.266 1.00 23.20 ? 525  LEU   B C   1 
ATOM   3552 O  O   . LEU   B 1 84  ? -10.491 -18.942 -61.889 1.00 23.12 ? 525  LEU   B O   1 
ATOM   3553 C  CB  . LEU   B 1 84  ? -10.868 -21.874 -60.370 1.00 18.87 ? 525  LEU   B CB  1 
ATOM   3554 C  CG  . LEU   B 1 84  ? -12.234 -21.244 -60.099 1.00 27.94 ? 525  LEU   B CG  1 
ATOM   3555 C  CD1 . LEU   B 1 84  ? -13.090 -21.284 -61.345 1.00 24.16 ? 525  LEU   B CD1 1 
ATOM   3556 C  CD2 . LEU   B 1 84  ? -12.917 -21.941 -58.938 1.00 29.77 ? 525  LEU   B CD2 1 
ATOM   3557 N  N   . GLY   B 1 85  ? -8.867  -19.446 -60.390 1.00 24.65 ? 526  GLY   B N   1 
ATOM   3558 C  CA  . GLY   B 1 85  ? -8.607  -18.041 -60.114 1.00 25.23 ? 526  GLY   B CA  1 
ATOM   3559 C  C   . GLY   B 1 85  ? -8.213  -17.271 -61.358 1.00 29.50 ? 526  GLY   B C   1 
ATOM   3560 O  O   . GLY   B 1 85  ? -8.672  -16.147 -61.579 1.00 22.97 ? 526  GLY   B O   1 
ATOM   3561 N  N   . ASP   B 1 86  ? -7.395  -17.883 -62.212 1.00 27.39 ? 527  ASP   B N   1 
ATOM   3562 C  CA  . ASP   B 1 86  ? -6.968  -17.200 -63.424 1.00 30.36 ? 527  ASP   B CA  1 
ATOM   3563 C  C   . ASP   B 1 86  ? -8.075  -17.060 -64.465 1.00 28.30 ? 527  ASP   B C   1 
ATOM   3564 O  O   . ASP   B 1 86  ? -7.867  -16.364 -65.464 1.00 29.35 ? 527  ASP   B O   1 
ATOM   3565 C  CB  . ASP   B 1 86  ? -5.704  -17.855 -63.985 1.00 32.49 ? 527  ASP   B CB  1 
ATOM   3566 C  CG  . ASP   B 1 86  ? -4.476  -17.589 -63.115 1.00 44.67 ? 527  ASP   B CG  1 
ATOM   3567 O  OD1 . ASP   B 1 86  ? -4.566  -16.755 -62.187 1.00 50.29 ? 527  ASP   B OD1 1 
ATOM   3568 O  OD2 . ASP   B 1 86  ? -3.418  -18.212 -63.349 1.00 42.65 ? 527  ASP   B OD2 1 
ATOM   3569 N  N   . GLU   B 1 87  ? -9.247  -17.672 -64.262 1.00 25.41 ? 528  GLU   B N   1 
ATOM   3570 C  CA  . GLU   B 1 87  ? -10.373 -17.399 -65.146 1.00 28.72 ? 528  GLU   B CA  1 
ATOM   3571 C  C   . GLU   B 1 87  ? -11.012 -16.051 -64.897 1.00 28.60 ? 528  GLU   B C   1 
ATOM   3572 O  O   . GLU   B 1 87  ? -11.839 -15.633 -65.712 1.00 31.19 ? 528  GLU   B O   1 
ATOM   3573 C  CB  . GLU   B 1 87  ? -11.468 -18.422 -64.937 1.00 25.88 ? 528  GLU   B CB  1 
ATOM   3574 C  CG  . GLU   B 1 87  ? -10.981 -19.774 -65.285 1.00 31.41 ? 528  GLU   B CG  1 
ATOM   3575 C  CD  . GLU   B 1 87  ? -10.950 -20.044 -66.788 1.00 55.59 ? 528  GLU   B CD  1 
ATOM   3576 O  OE1 . GLU   B 1 87  ? -11.946 -19.785 -67.498 1.00 57.40 ? 528  GLU   B OE1 1 
ATOM   3577 O  OE2 . GLU   B 1 87  ? -9.933  -20.597 -67.243 1.00 60.50 ? 528  GLU   B OE2 1 
ATOM   3578 N  N   . TYR   B 1 88  ? -10.708 -15.399 -63.781 1.00 23.45 ? 529  TYR   B N   1 
ATOM   3579 C  CA  . TYR   B 1 88  ? -11.324 -14.130 -63.434 1.00 17.92 ? 529  TYR   B CA  1 
ATOM   3580 C  C   . TYR   B 1 88  ? -10.294 -13.013 -63.530 1.00 21.18 ? 529  TYR   B C   1 
ATOM   3581 O  O   . TYR   B 1 88  ? -9.087  -13.238 -63.611 1.00 20.37 ? 529  TYR   B O   1 
ATOM   3582 C  CB  . TYR   B 1 88  ? -11.865 -14.171 -61.993 1.00 19.82 ? 529  TYR   B CB  1 
ATOM   3583 C  CG  . TYR   B 1 88  ? -12.800 -15.314 -61.709 1.00 17.16 ? 529  TYR   B CG  1 
ATOM   3584 C  CD1 . TYR   B 1 88  ? -14.112 -15.264 -62.113 1.00 18.70 ? 529  TYR   B CD1 1 
ATOM   3585 C  CD2 . TYR   B 1 88  ? -12.361 -16.440 -61.033 1.00 19.93 ? 529  TYR   B CD2 1 
ATOM   3586 C  CE1 . TYR   B 1 88  ? -14.982 -16.312 -61.863 1.00 18.49 ? 529  TYR   B CE1 1 
ATOM   3587 C  CE2 . TYR   B 1 88  ? -13.214 -17.496 -60.777 1.00 26.07 ? 529  TYR   B CE2 1 
ATOM   3588 C  CZ  . TYR   B 1 88  ? -14.509 -17.428 -61.185 1.00 19.99 ? 529  TYR   B CZ  1 
ATOM   3589 O  OH  . TYR   B 1 88  ? -15.357 -18.483 -60.922 1.00 23.72 ? 529  TYR   B OH  1 
ATOM   3590 N  N   . ASN   B 1 89  ? -10.796 -11.787 -63.487 1.00 20.80 ? 530  ASN   B N   1 
ATOM   3591 C  CA  . ASN   B 1 89  ? -9.943  -10.610 -63.409 1.00 19.99 ? 530  ASN   B CA  1 
ATOM   3592 C  C   . ASN   B 1 89  ? -9.536  -10.409 -61.952 1.00 21.15 ? 530  ASN   B C   1 
ATOM   3593 O  O   . ASN   B 1 89  ? -10.381 -10.086 -61.109 1.00 17.40 ? 530  ASN   B O   1 
ATOM   3594 C  CB  . ASN   B 1 89  ? -10.719 -9.406  -63.925 1.00 18.39 ? 530  ASN   B CB  1 
ATOM   3595 C  CG  . ASN   B 1 89  ? -9.855  -8.159  -64.054 1.00 19.40 ? 530  ASN   B CG  1 
ATOM   3596 O  OD1 . ASN   B 1 89  ? -8.820  -8.034  -63.418 1.00 24.24 ? 530  ASN   B OD1 1 
ATOM   3597 N  ND2 . ASN   B 1 89  ? -10.307 -7.217  -64.870 1.00 27.65 ? 530  ASN   B ND2 1 
ATOM   3598 N  N   . SER   B 1 90  ? -8.253  -10.622 -61.651 1.00 17.06 ? 531  SER   B N   1 
ATOM   3599 C  CA  . SER   B 1 90  ? -7.638  -10.257 -60.365 1.00 17.50 ? 531  SER   B CA  1 
ATOM   3600 C  C   . SER   B 1 90  ? -8.270  -10.996 -59.178 1.00 20.31 ? 531  SER   B C   1 
ATOM   3601 O  O   . SER   B 1 90  ? -8.833  -10.395 -58.248 1.00 16.59 ? 531  SER   B O   1 
ATOM   3602 C  CB  . SER   B 1 90  ? -7.623  -8.735  -60.153 1.00 17.11 ? 531  SER   B CB  1 
ATOM   3603 O  OG  . SER   B 1 90  ? -6.920  -8.096  -61.217 1.00 22.31 ? 531  SER   B OG  1 
ATOM   3604 N  N   . ILE   B 1 91  ? -8.139  -12.320 -59.198 1.00 19.41 ? 532  ILE   B N   1 
ATOM   3605 C  CA  . ILE   B 1 91  ? -8.683  -13.173 -58.145 1.00 16.54 ? 532  ILE   B CA  1 
ATOM   3606 C  C   . ILE   B 1 91  ? -7.647  -14.222 -57.797 1.00 18.51 ? 532  ILE   B C   1 
ATOM   3607 O  O   . ILE   B 1 91  ? -7.055  -14.833 -58.695 1.00 20.42 ? 532  ILE   B O   1 
ATOM   3608 C  CB  . ILE   B 1 91  ? -9.984  -13.869 -58.580 1.00 18.18 ? 532  ILE   B CB  1 
ATOM   3609 C  CG1 . ILE   B 1 91  ? -11.137 -12.872 -58.580 1.00 15.46 ? 532  ILE   B CG1 1 
ATOM   3610 C  CG2 . ILE   B 1 91  ? -10.279 -15.097 -57.687 1.00 19.19 ? 532  ILE   B CG2 1 
ATOM   3611 C  CD1 . ILE   B 1 91  ? -11.637 -12.505 -57.165 1.00 18.38 ? 532  ILE   B CD1 1 
ATOM   3612 N  N   . PHE   B 1 92  ? -7.436  -14.439 -56.503 1.00 17.52 ? 533  PHE   B N   1 
ATOM   3613 C  CA  . PHE   B 1 92  ? -6.746  -15.614 -56.000 1.00 21.61 ? 533  PHE   B CA  1 
ATOM   3614 C  C   . PHE   B 1 92  ? -7.704  -16.367 -55.088 1.00 22.33 ? 533  PHE   B C   1 
ATOM   3615 O  O   . PHE   B 1 92  ? -8.569  -15.767 -54.441 1.00 17.40 ? 533  PHE   B O   1 
ATOM   3616 C  CB  . PHE   B 1 92  ? -5.465  -15.263 -55.252 1.00 18.87 ? 533  PHE   B CB  1 
ATOM   3617 C  CG  . PHE   B 1 92  ? -5.679  -14.434 -54.013 1.00 18.00 ? 533  PHE   B CG  1 
ATOM   3618 C  CD1 . PHE   B 1 92  ? -5.921  -15.050 -52.794 1.00 16.49 ? 533  PHE   B CD1 1 
ATOM   3619 C  CD2 . PHE   B 1 92  ? -5.567  -13.044 -54.052 1.00 18.52 ? 533  PHE   B CD2 1 
ATOM   3620 C  CE1 . PHE   B 1 92  ? -6.072  -14.299 -51.621 1.00 17.27 ? 533  PHE   B CE1 1 
ATOM   3621 C  CE2 . PHE   B 1 92  ? -5.734  -12.283 -52.914 1.00 19.04 ? 533  PHE   B CE2 1 
ATOM   3622 C  CZ  . PHE   B 1 92  ? -5.991  -12.913 -51.681 1.00 17.95 ? 533  PHE   B CZ  1 
ATOM   3623 N  N   . ILE   B 1 93  ? -7.569  -17.693 -55.069 1.00 20.19 ? 534  ILE   B N   1 
ATOM   3624 C  CA  . ILE   B 1 93  ? -8.491  -18.570 -54.361 1.00 18.53 ? 534  ILE   B CA  1 
ATOM   3625 C  C   . ILE   B 1 93  ? -7.693  -19.588 -53.562 1.00 25.35 ? 534  ILE   B C   1 
ATOM   3626 O  O   . ILE   B 1 93  ? -6.734  -20.176 -54.076 1.00 23.71 ? 534  ILE   B O   1 
ATOM   3627 C  CB  . ILE   B 1 93  ? -9.451  -19.313 -55.314 1.00 18.20 ? 534  ILE   B CB  1 
ATOM   3628 C  CG1 . ILE   B 1 93  ? -9.964  -18.402 -56.433 1.00 21.07 ? 534  ILE   B CG1 1 
ATOM   3629 C  CG2 . ILE   B 1 93  ? -10.615 -19.919 -54.529 1.00 22.94 ? 534  ILE   B CG2 1 
ATOM   3630 C  CD1 . ILE   B 1 93  ? -10.964 -19.065 -57.374 1.00 19.04 ? 534  ILE   B CD1 1 
ATOM   3631 N  N   . SER   B 1 94  ? -8.103  -19.807 -52.310 1.00 20.50 ? 535  SER   B N   1 
ATOM   3632 C  CA  . SER   B 1 94  ? -7.642  -20.934 -51.512 1.00 19.34 ? 535  SER   B CA  1 
ATOM   3633 C  C   . SER   B 1 94  ? -8.845  -21.755 -51.074 1.00 17.81 ? 535  SER   B C   1 
ATOM   3634 O  O   . SER   B 1 94  ? -9.995  -21.402 -51.337 1.00 19.78 ? 535  SER   B O   1 
ATOM   3635 C  CB  . SER   B 1 94  ? -6.799  -20.477 -50.315 1.00 20.58 ? 535  SER   B CB  1 
ATOM   3636 O  OG  . SER   B 1 94  ? -7.574  -19.770 -49.350 1.00 22.38 ? 535  SER   B OG  1 
ATOM   3637 N  N   . ASN   B 1 95  ? -8.564  -22.888 -50.414 1.00 22.16 ? 536  ASN   B N   1 
ATOM   3638 C  CA  . ASN   B 1 95  ? -9.652  -23.775 -50.006 1.00 20.02 ? 536  ASN   B CA  1 
ATOM   3639 C  C   . ASN   B 1 95  ? -10.567 -23.130 -48.977 1.00 21.74 ? 536  ASN   B C   1 
ATOM   3640 O  O   . ASN   B 1 95  ? -11.678 -23.620 -48.763 1.00 22.95 ? 536  ASN   B O   1 
ATOM   3641 C  CB  . ASN   B 1 95  ? -9.097  -25.077 -49.424 1.00 38.47 ? 536  ASN   B CB  1 
ATOM   3642 C  CG  . ASN   B 1 95  ? -8.600  -26.030 -50.490 1.00 32.54 ? 536  ASN   B CG  1 
ATOM   3643 O  OD1 . ASN   B 1 95  ? -7.441  -26.421 -50.479 1.00 37.94 ? 536  ASN   B OD1 1 
ATOM   3644 N  ND2 . ASN   B 1 95  ? -9.483  -26.411 -51.418 1.00 27.59 ? 536  ASN   B ND2 1 
ATOM   3645 N  N   . GLU   B 1 96  ? -10.134 -22.032 -48.365 1.00 21.80 ? 537  GLU   B N   1 
ATOM   3646 C  CA  . GLU   B 1 96  ? -10.887 -21.329 -47.333 1.00 21.62 ? 537  GLU   B CA  1 
ATOM   3647 C  C   . GLU   B 1 96  ? -11.636 -20.117 -47.860 1.00 25.92 ? 537  GLU   B C   1 
ATOM   3648 O  O   . GLU   B 1 96  ? -12.409 -19.510 -47.110 1.00 20.63 ? 537  GLU   B O   1 
ATOM   3649 C  CB  . GLU   B 1 96  ? -9.934  -20.873 -46.224 1.00 23.06 ? 537  GLU   B CB  1 
ATOM   3650 C  CG  . GLU   B 1 96  ? -9.102  -21.988 -45.611 1.00 24.05 ? 537  GLU   B CG  1 
ATOM   3651 C  CD  . GLU   B 1 96  ? -7.688  -22.080 -46.187 1.00 51.58 ? 537  GLU   B CD  1 
ATOM   3652 O  OE1 . GLU   B 1 96  ? -7.451  -21.628 -47.336 1.00 28.46 ? 537  GLU   B OE1 1 
ATOM   3653 O  OE2 . GLU   B 1 96  ? -6.804  -22.610 -45.478 1.00 50.19 ? 537  GLU   B OE2 1 
ATOM   3654 N  N   . SER   B 1 97  ? -11.434 -19.760 -49.130 1.00 19.53 ? 538  SER   B N   1 
ATOM   3655 C  CA  . SER   B 1 97  ? -11.978 -18.518 -49.668 1.00 16.31 ? 538  SER   B CA  1 
ATOM   3656 C  C   . SER   B 1 97  ? -13.494 -18.490 -49.613 1.00 18.21 ? 538  SER   B C   1 
ATOM   3657 O  O   . SER   B 1 97  ? -14.091 -17.473 -49.243 1.00 17.36 ? 538  SER   B O   1 
ATOM   3658 C  CB  . SER   B 1 97  ? -11.527 -18.357 -51.116 1.00 20.05 ? 538  SER   B CB  1 
ATOM   3659 O  OG  . SER   B 1 97  ? -10.125 -18.308 -51.170 1.00 18.18 ? 538  SER   B OG  1 
ATOM   3660 N  N   . TYR   B 1 98  ? -14.141 -19.574 -50.047 1.00 17.98 ? 539  TYR   B N   1 
ATOM   3661 C  CA  . TYR   B 1 98  ? -15.593 -19.603 -50.084 1.00 16.65 ? 539  TYR   B CA  1 
ATOM   3662 C  C   . TYR   B 1 98  ? -16.173 -19.364 -48.696 1.00 16.26 ? 539  TYR   B C   1 
ATOM   3663 O  O   . TYR   B 1 98  ? -17.053 -18.513 -48.514 1.00 17.59 ? 539  TYR   B O   1 
ATOM   3664 C  CB  . TYR   B 1 98  ? -16.063 -20.943 -50.663 1.00 19.93 ? 539  TYR   B CB  1 
ATOM   3665 C  CG  . TYR   B 1 98  ? -17.544 -21.185 -50.596 1.00 19.37 ? 539  TYR   B CG  1 
ATOM   3666 C  CD1 . TYR   B 1 98  ? -18.430 -20.446 -51.373 1.00 22.97 ? 539  TYR   B CD1 1 
ATOM   3667 C  CD2 . TYR   B 1 98  ? -18.073 -22.172 -49.756 1.00 23.05 ? 539  TYR   B CD2 1 
ATOM   3668 C  CE1 . TYR   B 1 98  ? -19.805 -20.676 -51.321 1.00 22.33 ? 539  TYR   B CE1 1 
ATOM   3669 C  CE2 . TYR   B 1 98  ? -19.452 -22.411 -49.703 1.00 21.24 ? 539  TYR   B CE2 1 
ATOM   3670 C  CZ  . TYR   B 1 98  ? -20.309 -21.653 -50.483 1.00 20.55 ? 539  TYR   B CZ  1 
ATOM   3671 O  OH  . TYR   B 1 98  ? -21.668 -21.853 -50.463 1.00 26.66 ? 539  TYR   B OH  1 
ATOM   3672 N  N   . THR   B 1 99  ? -15.683 -20.114 -47.708 1.00 18.08 ? 540  THR   B N   1 
ATOM   3673 C  CA  . THR   B 1 99  ? -16.159 -19.940 -46.340 1.00 19.98 ? 540  THR   B CA  1 
ATOM   3674 C  C   . THR   B 1 99  ? -15.929 -18.516 -45.856 1.00 17.97 ? 540  THR   B C   1 
ATOM   3675 O  O   . THR   B 1 99  ? -16.805 -17.928 -45.213 1.00 18.49 ? 540  THR   B O   1 
ATOM   3676 C  CB  . THR   B 1 99  ? -15.452 -20.933 -45.417 1.00 19.67 ? 540  THR   B CB  1 
ATOM   3677 O  OG1 . THR   B 1 99  ? -15.857 -22.262 -45.755 1.00 27.05 ? 540  THR   B OG1 1 
ATOM   3678 C  CG2 . THR   B 1 99  ? -15.793 -20.661 -43.942 1.00 22.40 ? 540  THR   B CG2 1 
ATOM   3679 N  N   . CYS   B 1 100 ? -14.763 -17.937 -46.165 1.00 17.40 ? 541  CYS   B N   1 
ATOM   3680 C  CA  . CYS   B 1 100 ? -14.476 -16.580 -45.702 1.00 17.82 ? 541  CYS   B CA  1 
ATOM   3681 C  C   . CYS   B 1 100 ? -15.441 -15.588 -46.329 1.00 15.77 ? 541  CYS   B C   1 
ATOM   3682 O  O   . CYS   B 1 100 ? -15.953 -14.685 -45.655 1.00 15.46 ? 541  CYS   B O   1 
ATOM   3683 C  CB  . CYS   B 1 100 ? -13.046 -16.206 -46.064 1.00 16.34 ? 541  CYS   B CB  1 
ATOM   3684 S  SG  . CYS   B 1 100 ? -11.882 -17.019 -44.954 1.00 18.84 ? 541  CYS   B SG  1 
ATOM   3685 N  N   . ALA   B 1 101 ? -15.733 -15.758 -47.615 1.00 16.38 ? 542  ALA   B N   1 
ATOM   3686 C  CA  . ALA   B 1 101 ? -16.696 -14.885 -48.269 1.00 15.66 ? 542  ALA   B CA  1 
ATOM   3687 C  C   . ALA   B 1 101 ? -18.098 -15.042 -47.669 1.00 14.52 ? 542  ALA   B C   1 
ATOM   3688 O  O   . ALA   B 1 101 ? -18.827 -14.053 -47.511 1.00 14.86 ? 542  ALA   B O   1 
ATOM   3689 C  CB  . ALA   B 1 101 ? -16.691 -15.161 -49.774 1.00 17.34 ? 542  ALA   B CB  1 
ATOM   3690 N  N   . LEU   B 1 102 ? -18.490 -16.275 -47.321 1.00 15.05 ? 543  LEU   B N   1 
ATOM   3691 C  CA  . LEU   B 1 102 ? -19.765 -16.502 -46.633 1.00 15.93 ? 543  LEU   B CA  1 
ATOM   3692 C  C   . LEU   B 1 102 ? -19.801 -15.786 -45.289 1.00 17.50 ? 543  LEU   B C   1 
ATOM   3693 O  O   . LEU   B 1 102 ? -20.834 -15.222 -44.898 1.00 15.38 ? 543  LEU   B O   1 
ATOM   3694 C  CB  . LEU   B 1 102 ? -19.976 -18.000 -46.390 1.00 18.44 ? 543  LEU   B CB  1 
ATOM   3695 C  CG  . LEU   B 1 102 ? -20.280 -18.912 -47.584 1.00 23.03 ? 543  LEU   B CG  1 
ATOM   3696 C  CD1 . LEU   B 1 102 ? -20.611 -20.308 -47.079 1.00 25.13 ? 543  LEU   B CD1 1 
ATOM   3697 C  CD2 . LEU   B 1 102 ? -21.422 -18.364 -48.401 1.00 22.41 ? 543  LEU   B CD2 1 
ATOM   3698 N  N   . LEU   B 1 103 ? -18.689 -15.826 -44.557 1.00 14.59 ? 544  LEU   B N   1 
ATOM   3699 C  CA  . LEU   B 1 103 ? -18.642 -15.167 -43.255 1.00 16.74 ? 544  LEU   B CA  1 
ATOM   3700 C  C   . LEU   B 1 103 ? -18.702 -13.651 -43.397 1.00 14.14 ? 544  LEU   B C   1 
ATOM   3701 O  O   . LEU   B 1 103 ? -19.317 -12.964 -42.565 1.00 15.55 ? 544  LEU   B O   1 
ATOM   3702 C  CB  . LEU   B 1 103 ? -17.387 -15.575 -42.502 1.00 15.80 ? 544  LEU   B CB  1 
ATOM   3703 C  CG  . LEU   B 1 103 ? -17.351 -17.011 -42.001 1.00 16.84 ? 544  LEU   B CG  1 
ATOM   3704 C  CD1 . LEU   B 1 103 ? -15.987 -17.326 -41.404 1.00 21.71 ? 544  LEU   B CD1 1 
ATOM   3705 C  CD2 . LEU   B 1 103 ? -18.482 -17.252 -41.000 1.00 19.51 ? 544  LEU   B CD2 1 
ATOM   3706 N  N   . ALA   B 1 104 ? -18.040 -13.107 -44.421 1.00 14.82 ? 545  ALA   B N   1 
ATOM   3707 C  CA  . ALA   B 1 104 ? -18.090 -11.666 -44.630 1.00 15.25 ? 545  ALA   B CA  1 
ATOM   3708 C  C   . ALA   B 1 104 ? -19.532 -11.221 -44.831 1.00 15.34 ? 545  ALA   B C   1 
ATOM   3709 O  O   . ALA   B 1 104 ? -19.995 -10.250 -44.215 1.00 15.38 ? 545  ALA   B O   1 
ATOM   3710 C  CB  . ALA   B 1 104 ? -17.211 -11.275 -45.824 1.00 15.45 ? 545  ALA   B CB  1 
ATOM   3711 N  N   . ALA   B 1 105 ? -20.278 -11.958 -45.660 1.00 15.76 ? 546  ALA   B N   1 
ATOM   3712 C  CA  . ALA   B 1 105 ? -21.664 -11.589 -45.923 1.00 13.00 ? 546  ALA   B CA  1 
ATOM   3713 C  C   . ALA   B 1 105 ? -22.548 -11.823 -44.708 1.00 13.33 ? 546  ALA   B C   1 
ATOM   3714 O  O   . ALA   B 1 105 ? -23.338 -10.952 -44.337 1.00 15.94 ? 546  ALA   B O   1 
ATOM   3715 C  CB  . ALA   B 1 105 ? -22.191 -12.348 -47.138 1.00 15.22 ? 546  ALA   B CB  1 
ATOM   3716 N  N   . GLY   B 1 106 ? -22.414 -12.986 -44.067 1.00 15.37 ? 547  GLY   B N   1 
ATOM   3717 C  CA  . GLY   B 1 106 ? -23.241 -13.270 -42.901 1.00 15.36 ? 547  GLY   B CA  1 
ATOM   3718 C  C   . GLY   B 1 106 ? -23.018 -12.277 -41.779 1.00 18.01 ? 547  GLY   B C   1 
ATOM   3719 O  O   . GLY   B 1 106 ? -23.958 -11.879 -41.087 1.00 16.77 ? 547  GLY   B O   1 
ATOM   3720 N  N   . SER   B 1 107 ? -21.769 -11.868 -41.581 1.00 16.20 ? 548  SER   B N   1 
ATOM   3721 C  CA  . SER   B 1 107 ? -21.467 -10.827 -40.607 1.00 14.25 ? 548  SER   B CA  1 
ATOM   3722 C  C   . SER   B 1 107 ? -22.261 -9.567  -40.889 1.00 15.50 ? 548  SER   B C   1 
ATOM   3723 O  O   . SER   B 1 107 ? -22.812 -8.943  -39.969 1.00 13.80 ? 548  SER   B O   1 
ATOM   3724 C  CB  . SER   B 1 107 ? -19.980 -10.499 -40.671 1.00 15.66 ? 548  SER   B CB  1 
ATOM   3725 O  OG  . SER   B 1 107 ? -19.221 -11.585 -40.198 1.00 17.52 ? 548  SER   B OG  1 
ATOM   3726 N  N   . CYS   B 1 108 ? -22.336 -9.177  -42.153 1.00 13.51 ? 549  CYS   B N   1 
ATOM   3727 C  CA  . CYS   B 1 108 ? -23.059 -7.963  -42.481 1.00 13.56 ? 549  CYS   B CA  1 
ATOM   3728 C  C   . CYS   B 1 108 ? -24.558 -8.157  -42.375 1.00 14.55 ? 549  CYS   B C   1 
ATOM   3729 O  O   . CYS   B 1 108 ? -25.267 -7.213  -42.033 1.00 14.93 ? 549  CYS   B O   1 
ATOM   3730 C  CB  . CYS   B 1 108 ? -22.649 -7.446  -43.849 1.00 10.63 ? 549  CYS   B CB  1 
ATOM   3731 S  SG  . CYS   B 1 108 ? -20.935 -6.905  -43.898 1.00 14.57 ? 549  CYS   B SG  1 
ATOM   3732 N  N   . PHE   B 1 109 ? -25.060 -9.356  -42.675 1.00 15.80 ? 550  PHE   B N   1 
ATOM   3733 C  CA  . PHE   B 1 109 ? -26.479 -9.623  -42.448 1.00 14.82 ? 550  PHE   B CA  1 
ATOM   3734 C  C   . PHE   B 1 109 ? -26.828 -9.463  -40.976 1.00 15.69 ? 550  PHE   B C   1 
ATOM   3735 O  O   . PHE   B 1 109 ? -27.806 -8.791  -40.635 1.00 14.58 ? 550  PHE   B O   1 
ATOM   3736 C  CB  . PHE   B 1 109 ? -26.871 -11.029 -42.922 1.00 17.50 ? 550  PHE   B CB  1 
ATOM   3737 C  CG  . PHE   B 1 109 ? -26.603 -11.306 -44.384 1.00 17.17 ? 550  PHE   B CG  1 
ATOM   3738 C  CD1 . PHE   B 1 109 ? -26.403 -10.289 -45.303 1.00 15.28 ? 550  PHE   B CD1 1 
ATOM   3739 C  CD2 . PHE   B 1 109 ? -26.552 -12.622 -44.830 1.00 18.54 ? 550  PHE   B CD2 1 
ATOM   3740 C  CE1 . PHE   B 1 109 ? -26.129 -10.590 -46.648 1.00 18.31 ? 550  PHE   B CE1 1 
ATOM   3741 C  CE2 . PHE   B 1 109 ? -26.304 -12.932 -46.166 1.00 17.27 ? 550  PHE   B CE2 1 
ATOM   3742 C  CZ  . PHE   B 1 109 ? -26.097 -11.914 -47.078 1.00 16.18 ? 550  PHE   B CZ  1 
ATOM   3743 N  N   . ASN   B 1 110 ? -26.032 -10.060 -40.087 1.00 15.54 ? 551  ASN   B N   1 
ATOM   3744 C  CA  . ASN   B 1 110 ? -26.327 -9.923  -38.661 1.00 15.94 ? 551  ASN   B CA  1 
ATOM   3745 C  C   . ASN   B 1 110 ? -26.240 -8.470  -38.213 1.00 20.76 ? 551  ASN   B C   1 
ATOM   3746 O  O   . ASN   B 1 110 ? -26.987 -8.045  -37.323 1.00 17.51 ? 551  ASN   B O   1 
ATOM   3747 C  CB  . ASN   B 1 110 ? -25.368 -10.768 -37.822 1.00 16.44 ? 551  ASN   B CB  1 
ATOM   3748 C  CG  . ASN   B 1 110 ? -25.758 -12.240 -37.776 1.00 17.70 ? 551  ASN   B CG  1 
ATOM   3749 O  OD1 . ASN   B 1 110 ? -26.859 -12.610 -38.193 1.00 19.46 ? 551  ASN   B OD1 1 
ATOM   3750 N  ND2 . ASN   B 1 110 ? -24.863 -13.081 -37.274 1.00 18.44 ? 551  ASN   B ND2 1 
ATOM   3751 N  N   . SER   B 1 111 ? -25.329 -7.695  -38.799 1.00 16.70 ? 552  SER   B N   1 
ATOM   3752 C  CA  . SER   B 1 111 ? -25.229 -6.287  -38.421 1.00 15.78 ? 552  SER   B CA  1 
ATOM   3753 C  C   . SER   B 1 111 ? -26.447 -5.508  -38.890 1.00 15.89 ? 552  SER   B C   1 
ATOM   3754 O  O   . SER   B 1 111 ? -27.000 -4.698  -38.130 1.00 16.59 ? 552  SER   B O   1 
ATOM   3755 C  CB  . SER   B 1 111 ? -23.946 -5.675  -38.986 1.00 15.26 ? 552  SER   B CB  1 
ATOM   3756 O  OG  . SER   B 1 111 ? -22.815 -6.389  -38.516 1.00 16.75 ? 552  SER   B OG  1 
ATOM   3757 N  N   . ALA   B 1 112 ? -26.884 -5.742  -40.130 1.00 13.74 ? 553  ALA   B N   1 
ATOM   3758 C  CA  . ALA   B 1 112 ? -28.073 -5.068  -40.628 1.00 17.07 ? 553  ALA   B CA  1 
ATOM   3759 C  C   . ALA   B 1 112 ? -29.297 -5.450  -39.814 1.00 16.17 ? 553  ALA   B C   1 
ATOM   3760 O  O   . ALA   B 1 112 ? -30.141 -4.597  -39.525 1.00 15.93 ? 553  ALA   B O   1 
ATOM   3761 C  CB  . ALA   B 1 112 ? -28.273 -5.411  -42.105 1.00 16.59 ? 553  ALA   B CB  1 
ATOM   3762 N  N   . GLN   B 1 113 ? -29.390 -6.723  -39.430 1.00 14.01 ? 554  GLN   B N   1 
ATOM   3763 C  CA  . GLN   B 1 113 ? -30.518 -7.194  -38.626 1.00 15.59 ? 554  GLN   B CA  1 
ATOM   3764 C  C   . GLN   B 1 113 ? -30.533 -6.505  -37.271 1.00 19.89 ? 554  GLN   B C   1 
ATOM   3765 O  O   . GLN   B 1 113 ? -31.599 -6.117  -36.768 1.00 16.83 ? 554  GLN   B O   1 
ATOM   3766 C  CB  . GLN   B 1 113 ? -30.389 -8.697  -38.436 1.00 16.62 ? 554  GLN   B CB  1 
ATOM   3767 C  CG  . GLN   B 1 113 ? -31.466 -9.321  -37.550 1.00 16.99 ? 554  GLN   B CG  1 
ATOM   3768 C  CD  . GLN   B 1 113 ? -31.246 -10.789 -37.376 1.00 19.43 ? 554  GLN   B CD  1 
ATOM   3769 O  OE1 . GLN   B 1 113 ? -30.163 -11.229 -36.987 1.00 23.90 ? 554  GLN   B OE1 1 
ATOM   3770 N  NE2 . GLN   B 1 113 ? -32.274 -11.578 -37.676 1.00 26.90 ? 554  GLN   B NE2 1 
ATOM   3771 N  N   . ALA   B 1 114 ? -29.359 -6.335  -36.667 1.00 16.66 ? 555  ALA   B N   1 
ATOM   3772 C  CA  . ALA   B 1 114 ? -29.269 -5.630  -35.394 1.00 15.46 ? 555  ALA   B CA  1 
ATOM   3773 C  C   . ALA   B 1 114 ? -29.689 -4.171  -35.521 1.00 17.16 ? 555  ALA   B C   1 
ATOM   3774 O  O   . ALA   B 1 114 ? -30.359 -3.634  -34.634 1.00 16.89 ? 555  ALA   B O   1 
ATOM   3775 C  CB  . ALA   B 1 114 ? -27.853 -5.752  -34.835 1.00 15.85 ? 555  ALA   B CB  1 
ATOM   3776 N  N   . ILE   B 1 115 ? -29.310 -3.506  -36.605 1.00 14.78 ? 556  ILE   B N   1 
ATOM   3777 C  CA  . ILE   B 1 115 ? -29.732 -2.134  -36.851 1.00 13.52 ? 556  ILE   B CA  1 
ATOM   3778 C  C   . ILE   B 1 115 ? -31.238 -2.072  -37.059 1.00 16.61 ? 556  ILE   B C   1 
ATOM   3779 O  O   . ILE   B 1 115 ? -31.919 -1.190  -36.521 1.00 18.87 ? 556  ILE   B O   1 
ATOM   3780 C  CB  . ILE   B 1 115 ? -28.967 -1.556  -38.058 1.00 14.76 ? 556  ILE   B CB  1 
ATOM   3781 C  CG1 . ILE   B 1 115 ? -27.485 -1.377  -37.727 1.00 15.04 ? 556  ILE   B CG1 1 
ATOM   3782 C  CG2 . ILE   B 1 115 ? -29.538 -0.224  -38.462 1.00 17.37 ? 556  ILE   B CG2 1 
ATOM   3783 C  CD1 . ILE   B 1 115 ? -26.657 -1.016  -38.950 1.00 16.50 ? 556  ILE   B CD1 1 
ATOM   3784 N  N   . LEU   B 1 116 ? -31.781 -2.987  -37.856 1.00 17.41 ? 557  LEU   B N   1 
ATOM   3785 C  CA  . LEU   B 1 116 ? -33.176 -2.883  -38.260 1.00 18.86 ? 557  LEU   B CA  1 
ATOM   3786 C  C   . LEU   B 1 116 ? -34.146 -3.355  -37.189 1.00 21.10 ? 557  LEU   B C   1 
ATOM   3787 O  O   . LEU   B 1 116 ? -35.346 -3.079  -37.307 1.00 22.75 ? 557  LEU   B O   1 
ATOM   3788 C  CB  . LEU   B 1 116 ? -33.410 -3.637  -39.563 1.00 17.89 ? 557  LEU   B CB  1 
ATOM   3789 C  CG  . LEU   B 1 116 ? -32.689 -3.002  -40.762 1.00 18.48 ? 557  LEU   B CG  1 
ATOM   3790 C  CD1 . LEU   B 1 116 ? -32.698 -3.958  -41.937 1.00 18.54 ? 557  LEU   B CD1 1 
ATOM   3791 C  CD2 . LEU   B 1 116 ? -33.319 -1.686  -41.154 1.00 19.24 ? 557  LEU   B CD2 1 
ATOM   3792 N  N   . THR   B 1 117 ? -33.662 -4.046  -36.166 1.00 16.62 ? 558  THR   B N   1 
ATOM   3793 C  CA  . THR   B 1 117 ? -34.484 -4.419  -35.025 1.00 16.99 ? 558  THR   B CA  1 
ATOM   3794 C  C   . THR   B 1 117 ? -34.250 -3.514  -33.828 1.00 26.77 ? 558  THR   B C   1 
ATOM   3795 O  O   . THR   B 1 117 ? -34.847 -3.735  -32.768 1.00 23.33 ? 558  THR   B O   1 
ATOM   3796 C  CB  . THR   B 1 117 ? -34.244 -5.881  -34.652 1.00 18.31 ? 558  THR   B CB  1 
ATOM   3797 O  OG1 . THR   B 1 117 ? -32.854 -6.097  -34.372 1.00 20.19 ? 558  THR   B OG1 1 
ATOM   3798 C  CG2 . THR   B 1 117 ? -34.668 -6.786  -35.782 1.00 19.84 ? 558  THR   B CG2 1 
ATOM   3799 N  N   . GLY   B 1 118 ? -33.411 -2.496  -33.969 1.00 20.70 ? 559  GLY   B N   1 
ATOM   3800 C  CA  . GLY   B 1 118 ? -33.137 -1.589  -32.874 1.00 23.08 ? 559  GLY   B CA  1 
ATOM   3801 C  C   . GLY   B 1 118 ? -32.180 -2.098  -31.821 1.00 23.90 ? 559  GLY   B C   1 
ATOM   3802 O  O   . GLY   B 1 118 ? -32.031 -1.444  -30.784 1.00 30.59 ? 559  GLY   B O   1 
ATOM   3803 N  N   . GLN   B 1 119 ? -31.518 -3.239  -32.038 1.00 22.68 ? 560  GLN   B N   1 
ATOM   3804 C  CA  . GLN   B 1 119 ? -30.525 -3.702  -31.076 1.00 19.35 ? 560  GLN   B CA  1 
ATOM   3805 C  C   . GLN   B 1 119 ? -29.326 -2.764  -31.020 1.00 36.83 ? 560  GLN   B C   1 
ATOM   3806 O  O   . GLN   B 1 119 ? -28.719 -2.608  -29.957 1.00 25.64 ? 560  GLN   B O   1 
ATOM   3807 C  CB  . GLN   B 1 119 ? -30.049 -5.123  -31.388 1.00 22.90 ? 560  GLN   B CB  1 
ATOM   3808 C  CG  . GLN   B 1 119 ? -31.038 -6.239  -31.024 0.88 26.47 ? 560  GLN   B CG  1 
ATOM   3809 C  CD  . GLN   B 1 119 ? -31.061 -6.556  -29.531 0.73 29.26 ? 560  GLN   B CD  1 
ATOM   3810 O  OE1 . GLN   B 1 119 ? -32.121 -6.574  -28.913 0.74 26.57 ? 560  GLN   B OE1 1 
ATOM   3811 N  NE2 . GLN   B 1 119 ? -29.893 -6.824  -28.953 0.76 27.31 ? 560  GLN   B NE2 1 
ATOM   3812 N  N   . VAL   B 1 120 ? -28.951 -2.161  -32.155 1.00 21.37 ? 561  VAL   B N   1 
ATOM   3813 C  CA  . VAL   B 1 120 ? -27.902 -1.152  -32.210 1.00 19.50 ? 561  VAL   B CA  1 
ATOM   3814 C  C   . VAL   B 1 120 ? -28.391 -0.027  -33.107 1.00 19.65 ? 561  VAL   B C   1 
ATOM   3815 O  O   . VAL   B 1 120 ? -29.289 -0.204  -33.931 1.00 19.72 ? 561  VAL   B O   1 
ATOM   3816 C  CB  . VAL   B 1 120 ? -26.550 -1.705  -32.734 1.00 19.87 ? 561  VAL   B CB  1 
ATOM   3817 C  CG1 . VAL   B 1 120 ? -26.082 -2.875  -31.904 1.00 19.83 ? 561  VAL   B CG1 1 
ATOM   3818 C  CG2 . VAL   B 1 120 ? -26.670 -2.133  -34.210 1.00 18.87 ? 561  VAL   B CG2 1 
ATOM   3819 N  N   . ARG   B 1 121 ? -27.767 1.147   -32.959 1.00 20.16 ? 562  ARG   B N   1 
ATOM   3820 C  CA  . ARG   B 1 121 ? -28.135 2.250   -33.836 1.00 17.08 ? 562  ARG   B CA  1 
ATOM   3821 C  C   . ARG   B 1 121 ? -27.386 2.175   -35.153 1.00 13.27 ? 562  ARG   B C   1 
ATOM   3822 O  O   . ARG   B 1 121 ? -27.939 2.487   -36.217 1.00 18.95 ? 562  ARG   B O   1 
ATOM   3823 C  CB  . ARG   B 1 121 ? -27.851 3.600   -33.180 1.00 19.94 ? 562  ARG   B CB  1 
ATOM   3824 C  CG  . ARG   B 1 121 ? -28.152 4.787   -34.101 1.00 32.83 ? 562  ARG   B CG  1 
ATOM   3825 C  CD  . ARG   B 1 121 ? -27.968 6.135   -33.404 1.00 57.52 ? 562  ARG   B CD  1 
ATOM   3826 N  NE  . ARG   B 1 121 ? -27.716 7.207   -34.364 1.00 65.84 ? 562  ARG   B NE  1 
ATOM   3827 C  CZ  . ARG   B 1 121 ? -26.842 8.195   -34.183 1.00 52.33 ? 562  ARG   B CZ  1 
ATOM   3828 N  NH1 . ARG   B 1 121 ? -26.121 8.268   -33.067 1.00 48.15 ? 562  ARG   B NH1 1 
ATOM   3829 N  NH2 . ARG   B 1 121 ? -26.686 9.111   -35.128 1.00 27.15 ? 562  ARG   B NH2 1 
ATOM   3830 N  N   . ASN   B 1 122 ? -26.116 1.778   -35.090 1.00 15.75 ? 563  ASN   B N   1 
ATOM   3831 C  CA  . ASN   B 1 122 ? -25.251 1.754   -36.261 1.00 15.15 ? 563  ASN   B CA  1 
ATOM   3832 C  C   . ASN   B 1 122 ? -24.219 0.657   -36.042 1.00 13.98 ? 563  ASN   B C   1 
ATOM   3833 O  O   . ASN   B 1 122 ? -24.194 0.025   -34.986 1.00 13.38 ? 563  ASN   B O   1 
ATOM   3834 C  CB  . ASN   B 1 122 ? -24.665 3.138   -36.513 1.00 12.29 ? 563  ASN   B CB  1 
ATOM   3835 C  CG  . ASN   B 1 122 ? -23.905 3.681   -35.308 1.00 14.09 ? 563  ASN   B CG  1 
ATOM   3836 O  OD1 . ASN   B 1 122 ? -23.242 2.930   -34.613 1.00 14.17 ? 563  ASN   B OD1 1 
ATOM   3837 N  ND2 . ASN   B 1 122 ? -23.997 4.993   -35.072 1.00 14.37 ? 563  ASN   B ND2 1 
ATOM   3838 N  N   . ALA   B 1 123 ? -23.372 0.408   -37.052 1.00 13.73 ? 564  ALA   B N   1 
ATOM   3839 C  CA  . ALA   B 1 123 ? -22.455 -0.707  -36.888 1.00 12.30 ? 564  ALA   B CA  1 
ATOM   3840 C  C   . ALA   B 1 123 ? -21.311 -0.630  -37.888 1.00 10.63 ? 564  ALA   B C   1 
ATOM   3841 O  O   . ALA   B 1 123 ? -21.402 0.029   -38.930 1.00 12.59 ? 564  ALA   B O   1 
ATOM   3842 C  CB  . ALA   B 1 123 ? -23.143 -2.079  -36.975 1.00 15.42 ? 564  ALA   B CB  1 
ATOM   3843 N  N   A VAL   B 1 124 ? -20.221 -1.305  -37.534 0.72 11.48 ? 565  VAL   B N   1 
ATOM   3844 N  N   B VAL   B 1 124 ? -20.250 -1.376  -37.573 0.28 12.49 ? 565  VAL   B N   1 
ATOM   3845 C  CA  A VAL   B 1 124 ? -19.068 -1.448  -38.413 0.72 14.71 ? 565  VAL   B CA  1 
ATOM   3846 C  CA  B VAL   B 1 124 ? -19.041 -1.456  -38.387 0.28 12.65 ? 565  VAL   B CA  1 
ATOM   3847 C  C   A VAL   B 1 124 ? -18.779 -2.934  -38.602 0.72 10.79 ? 565  VAL   B C   1 
ATOM   3848 C  C   B VAL   B 1 124 ? -18.683 -2.922  -38.579 0.28 15.77 ? 565  VAL   B C   1 
ATOM   3849 O  O   A VAL   B 1 124 ? -18.878 -3.728  -37.656 0.72 14.67 ? 565  VAL   B O   1 
ATOM   3850 O  O   B VAL   B 1 124 ? -18.629 -3.684  -37.605 0.28 13.06 ? 565  VAL   B O   1 
ATOM   3851 C  CB  A VAL   B 1 124 ? -17.853 -0.649  -37.884 0.72 13.14 ? 565  VAL   B CB  1 
ATOM   3852 C  CB  B VAL   B 1 124 ? -17.878 -0.703  -37.719 0.28 15.03 ? 565  VAL   B CB  1 
ATOM   3853 C  CG1 A VAL   B 1 124 ? -17.337 -1.201  -36.559 0.72 12.31 ? 565  VAL   B CG1 1 
ATOM   3854 C  CG1 B VAL   B 1 124 ? -16.533 -1.181  -38.255 0.28 13.82 ? 565  VAL   B CG1 1 
ATOM   3855 C  CG2 A VAL   B 1 124 ? -16.746 -0.569  -38.912 0.72 14.90 ? 565  VAL   B CG2 1 
ATOM   3856 C  CG2 B VAL   B 1 124 ? -18.042 0.761   -37.949 0.28 8.50  ? 565  VAL   B CG2 1 
ATOM   3857 N  N   . ALA   B 1 125 ? -18.403 -3.306  -39.828 1.00 12.59 ? 566  ALA   B N   1 
ATOM   3858 C  CA  . ALA   B 1 125 ? -18.093 -4.694  -40.179 1.00 12.60 ? 566  ALA   B CA  1 
ATOM   3859 C  C   . ALA   B 1 125 ? -16.668 -4.754  -40.712 1.00 12.53 ? 566  ALA   B C   1 
ATOM   3860 O  O   . ALA   B 1 125 ? -16.399 -4.253  -41.812 1.00 11.07 ? 566  ALA   B O   1 
ATOM   3861 C  CB  . ALA   B 1 125 ? -19.087 -5.254  -41.203 1.00 12.23 ? 566  ALA   B CB  1 
ATOM   3862 N  N   . ILE   B 1 126 ? -15.780 -5.379  -39.947 1.00 10.47 ? 567  ILE   B N   1 
ATOM   3863 C  CA  . ILE   B 1 126 ? -14.367 -5.525  -40.315 1.00 11.31 ? 567  ILE   B CA  1 
ATOM   3864 C  C   . ILE   B 1 126 ? -14.230 -6.884  -41.000 1.00 16.98 ? 567  ILE   B C   1 
ATOM   3865 O  O   . ILE   B 1 126 ? -13.979 -7.902  -40.356 1.00 14.69 ? 567  ILE   B O   1 
ATOM   3866 C  CB  . ILE   B 1 126 ? -13.449 -5.378  -39.105 1.00 13.58 ? 567  ILE   B CB  1 
ATOM   3867 C  CG1 . ILE   B 1 126 ? -13.773 -4.083  -38.336 1.00 12.20 ? 567  ILE   B CG1 1 
ATOM   3868 C  CG2 . ILE   B 1 126 ? -11.982 -5.452  -39.520 1.00 13.03 ? 567  ILE   B CG2 1 
ATOM   3869 C  CD1 . ILE   B 1 126 ? -13.147 -4.060  -36.938 1.00 13.44 ? 567  ILE   B CD1 1 
ATOM   3870 N  N   . VAL   B 1 127 ? -14.421 -6.910  -42.323 1.00 11.96 ? 568  VAL   B N   1 
ATOM   3871 C  CA  . VAL   B 1 127 ? -14.582 -8.164  -43.042 1.00 11.72 ? 568  VAL   B CA  1 
ATOM   3872 C  C   . VAL   B 1 127 ? -13.672 -8.232  -44.259 1.00 11.88 ? 568  VAL   B C   1 
ATOM   3873 O  O   . VAL   B 1 127 ? -13.305 -7.209  -44.845 1.00 12.23 ? 568  VAL   B O   1 
ATOM   3874 C  CB  . VAL   B 1 127 ? -16.048 -8.418  -43.479 1.00 13.11 ? 568  VAL   B CB  1 
ATOM   3875 C  CG1 . VAL   B 1 127 ? -16.975 -8.583  -42.250 1.00 14.53 ? 568  VAL   B CG1 1 
ATOM   3876 C  CG2 . VAL   B 1 127 ? -16.570 -7.293  -44.394 1.00 14.57 ? 568  VAL   B CG2 1 
ATOM   3877 N  N   . ARG   B 1 128 ? -13.341 -9.465  -44.658 1.00 12.78 ? 569  ARG   B N   1 
ATOM   3878 C  CA  . ARG   B 1 128 ? -12.680 -9.754  -45.926 1.00 11.60 ? 569  ARG   B CA  1 
ATOM   3879 C  C   . ARG   B 1 128 ? -13.023 -11.185 -46.307 1.00 13.31 ? 569  ARG   B C   1 
ATOM   3880 O  O   . ARG   B 1 128 ? -13.448 -11.971 -45.444 1.00 12.86 ? 569  ARG   B O   1 
ATOM   3881 C  CB  . ARG   B 1 128 ? -11.158 -9.571  -45.836 1.00 12.81 ? 569  ARG   B CB  1 
ATOM   3882 C  CG  . ARG   B 1 128 ? -10.484 -10.611 -44.976 1.00 12.57 ? 569  ARG   B CG  1 
ATOM   3883 C  CD  . ARG   B 1 128 ? -8.984  -10.423 -44.940 1.00 13.15 ? 569  ARG   B CD  1 
ATOM   3884 N  NE  . ARG   B 1 128 ? -8.235  -10.807 -46.142 1.00 13.43 ? 569  ARG   B NE  1 
ATOM   3885 C  CZ  . ARG   B 1 128 ? -7.786  -12.037 -46.407 1.00 15.61 ? 569  ARG   B CZ  1 
ATOM   3886 N  NH1 . ARG   B 1 128 ? -8.055  -13.054 -45.579 1.00 15.39 ? 569  ARG   B NH1 1 
ATOM   3887 N  NH2 . ARG   B 1 128 ? -7.018  -12.244 -47.489 1.00 13.97 ? 569  ARG   B NH2 1 
ATOM   3888 N  N   . PRO   B 1 129 ? -12.911 -11.552 -47.602 1.00 14.23 ? 570  PRO   B N   1 
ATOM   3889 C  CA  . PRO   B 1 129 ? -12.562 -10.713 -48.751 1.00 12.04 ? 570  PRO   B CA  1 
ATOM   3890 C  C   . PRO   B 1 129 ? -13.611 -9.653  -49.040 1.00 12.43 ? 570  PRO   B C   1 
ATOM   3891 O  O   . PRO   B 1 129 ? -14.744 -9.774  -48.557 1.00 12.29 ? 570  PRO   B O   1 
ATOM   3892 C  CB  . PRO   B 1 129 ? -12.499 -11.714 -49.915 1.00 13.36 ? 570  PRO   B CB  1 
ATOM   3893 C  CG  . PRO   B 1 129 ? -13.440 -12.809 -49.508 1.00 14.80 ? 570  PRO   B CG  1 
ATOM   3894 C  CD  . PRO   B 1 129 ? -13.307 -12.917 -48.018 1.00 14.75 ? 570  PRO   B CD  1 
ATOM   3895 N  N   . PRO   B 1 130 ? -13.250 -8.635  -49.836 1.00 12.74 ? 571  PRO   B N   1 
ATOM   3896 C  CA  . PRO   B 1 130 ? -14.203 -7.558  -50.151 1.00 11.04 ? 571  PRO   B CA  1 
ATOM   3897 C  C   . PRO   B 1 130 ? -15.289 -8.026  -51.105 1.00 12.37 ? 571  PRO   B C   1 
ATOM   3898 O  O   . PRO   B 1 130 ? -15.295 -9.191  -51.529 1.00 12.19 ? 571  PRO   B O   1 
ATOM   3899 C  CB  . PRO   B 1 130 ? -13.322 -6.503  -50.837 1.00 13.11 ? 571  PRO   B CB  1 
ATOM   3900 C  CG  . PRO   B 1 130 ? -12.106 -7.283  -51.347 1.00 11.90 ? 571  PRO   B CG  1 
ATOM   3901 C  CD  . PRO   B 1 130 ? -11.878 -8.333  -50.302 1.00 11.65 ? 571  PRO   B CD  1 
ATOM   3902 N  N   . GLY   B 1 131 ? -16.190 -7.120  -51.490 1.00 12.39 ? 572  GLY   B N   1 
ATOM   3903 C  CA  . GLY   B 1 131 ? -17.342 -7.524  -52.280 1.00 12.57 ? 572  GLY   B CA  1 
ATOM   3904 C  C   . GLY   B 1 131 ? -17.737 -6.728  -53.507 1.00 13.34 ? 572  GLY   B C   1 
ATOM   3905 O  O   . GLY   B 1 131 ? -18.379 -7.295  -54.405 1.00 12.37 ? 572  GLY   B O   1 
ATOM   3906 N  N   . HIS   B 1 132 ? -17.377 -5.439  -53.601 1.00 10.86 ? 573  HIS   B N   1 
ATOM   3907 C  CA  . HIS   B 1 132 ? -18.106 -4.569  -54.525 1.00 13.40 ? 573  HIS   B CA  1 
ATOM   3908 C  C   . HIS   B 1 132 ? -17.805 -4.799  -56.000 1.00 9.77  ? 573  HIS   B C   1 
ATOM   3909 O  O   . HIS   B 1 132 ? -18.596 -4.358  -56.837 1.00 12.76 ? 573  HIS   B O   1 
ATOM   3910 C  CB  . HIS   B 1 132 ? -17.986 -3.101  -54.128 1.00 11.64 ? 573  HIS   B CB  1 
ATOM   3911 C  CG  . HIS   B 1 132 ? -16.634 -2.502  -54.320 1.00 11.63 ? 573  HIS   B CG  1 
ATOM   3912 N  ND1 . HIS   B 1 132 ? -16.474 -1.159  -54.577 1.00 12.42 ? 573  HIS   B ND1 1 
ATOM   3913 C  CD2 . HIS   B 1 132 ? -15.383 -3.029  -54.267 1.00 15.59 ? 573  HIS   B CD2 1 
ATOM   3914 C  CE1 . HIS   B 1 132 ? -15.186 -0.884  -54.691 1.00 12.39 ? 573  HIS   B CE1 1 
ATOM   3915 N  NE2 . HIS   B 1 132 ? -14.498 -1.999  -54.511 1.00 14.30 ? 573  HIS   B NE2 1 
ATOM   3916 N  N   . HIS   B 1 133 ? -16.700 -5.455  -56.339 1.00 10.53 ? 574  HIS   B N   1 
ATOM   3917 C  CA  . HIS   B 1 133 ? -16.457 -5.845  -57.725 1.00 13.73 ? 574  HIS   B CA  1 
ATOM   3918 C  C   . HIS   B 1 133 ? -17.183 -7.125  -58.137 1.00 14.23 ? 574  HIS   B C   1 
ATOM   3919 O  O   . HIS   B 1 133 ? -17.240 -7.413  -59.344 1.00 15.45 ? 574  HIS   B O   1 
ATOM   3920 C  CB  . HIS   B 1 133 ? -14.961 -6.016  -57.986 1.00 12.69 ? 574  HIS   B CB  1 
ATOM   3921 C  CG  . HIS   B 1 133 ? -14.163 -4.761  -57.815 1.00 15.05 ? 574  HIS   B CG  1 
ATOM   3922 N  ND1 . HIS   B 1 133 ? -14.433 -3.606  -58.522 1.00 13.68 ? 574  HIS   B ND1 1 
ATOM   3923 C  CD2 . HIS   B 1 133 ? -13.094 -4.490  -57.032 1.00 16.19 ? 574  HIS   B CD2 1 
ATOM   3924 C  CE1 . HIS   B 1 133 ? -13.566 -2.672  -58.173 1.00 16.66 ? 574  HIS   B CE1 1 
ATOM   3925 N  NE2 . HIS   B 1 133 ? -12.739 -3.186  -57.281 1.00 14.84 ? 574  HIS   B NE2 1 
ATOM   3926 N  N   . ALA   B 1 134 ? -17.711 -7.908  -57.190 1.00 14.07 ? 575  ALA   B N   1 
ATOM   3927 C  CA  . ALA   B 1 134 ? -18.369 -9.161  -57.564 1.00 15.31 ? 575  ALA   B CA  1 
ATOM   3928 C  C   . ALA   B 1 134 ? -19.668 -8.889  -58.303 1.00 15.67 ? 575  ALA   B C   1 
ATOM   3929 O  O   . ALA   B 1 134 ? -20.497 -8.077  -57.872 1.00 15.70 ? 575  ALA   B O   1 
ATOM   3930 C  CB  . ALA   B 1 134 ? -18.654 -10.030 -56.341 1.00 14.56 ? 575  ALA   B CB  1 
ATOM   3931 N  N   . GLU   B 1 135 ? -19.859 -9.605  -59.397 1.00 16.78 ? 576  GLU   B N   1 
ATOM   3932 C  CA  . GLU   B 1 135 ? -21.027 -9.474  -60.247 1.00 18.63 ? 576  GLU   B CA  1 
ATOM   3933 C  C   . GLU   B 1 135 ? -22.006 -10.611 -59.969 1.00 17.62 ? 576  GLU   B C   1 
ATOM   3934 O  O   . GLU   B 1 135 ? -21.686 -11.583 -59.285 1.00 16.65 ? 576  GLU   B O   1 
ATOM   3935 C  CB  . GLU   B 1 135 ? -20.593 -9.529  -61.718 1.00 20.99 ? 576  GLU   B CB  1 
ATOM   3936 C  CG  . GLU   B 1 135 ? -19.637 -8.405  -62.141 1.00 18.42 ? 576  GLU   B CG  1 
ATOM   3937 C  CD  . GLU   B 1 135 ? -20.367 -7.134  -62.549 1.00 19.03 ? 576  GLU   B CD  1 
ATOM   3938 O  OE1 . GLU   B 1 135 ? -21.610 -7.088  -62.472 1.00 22.69 ? 576  GLU   B OE1 1 
ATOM   3939 O  OE2 . GLU   B 1 135 ? -19.671 -6.182  -62.979 1.00 30.31 ? 576  GLU   B OE2 1 
ATOM   3940 N  N   . LYS   B 1 136 ? -23.218 -10.474 -60.515 1.00 18.19 ? 577  LYS   B N   1 
ATOM   3941 C  CA  . LYS   B 1 136 ? -24.203 -11.550 -60.437 1.00 22.49 ? 577  LYS   B CA  1 
ATOM   3942 C  C   . LYS   B 1 136 ? -23.571 -12.902 -60.753 1.00 20.09 ? 577  LYS   B C   1 
ATOM   3943 O  O   . LYS   B 1 136 ? -23.711 -13.867 -59.990 1.00 20.38 ? 577  LYS   B O   1 
ATOM   3944 C  CB  . LYS   B 1 136 ? -25.358 -11.260 -61.396 1.00 19.99 ? 577  LYS   B CB  1 
ATOM   3945 C  CG  . LYS   B 1 136 ? -26.506 -12.269 -61.352 1.00 32.21 ? 577  LYS   B CG  1 
ATOM   3946 C  CD  . LYS   B 1 136 ? -27.565 -11.898 -62.399 1.00 36.88 ? 577  LYS   B CD  1 
ATOM   3947 C  CE  . LYS   B 1 136 ? -28.734 -12.860 -62.394 1.00 48.08 ? 577  LYS   B CE  1 
ATOM   3948 N  NZ  . LYS   B 1 136 ? -28.319 -14.195 -61.898 1.00 46.56 ? 577  LYS   B NZ  1 
ATOM   3949 N  N   . ASP   B 1 137 ? -22.807 -12.972 -61.844 1.00 19.96 ? 578  ASP   B N   1 
ATOM   3950 C  CA  . ASP   B 1 137 ? -22.338 -14.246 -62.364 1.00 18.87 ? 578  ASP   B CA  1 
ATOM   3951 C  C   . ASP   B 1 137 ? -20.826 -14.421 -62.313 1.00 19.49 ? 578  ASP   B C   1 
ATOM   3952 O  O   . ASP   B 1 137 ? -20.318 -15.399 -62.868 1.00 20.37 ? 578  ASP   B O   1 
ATOM   3953 C  CB  . ASP   B 1 137 ? -22.853 -14.439 -63.801 1.00 23.75 ? 578  ASP   B CB  1 
ATOM   3954 C  CG  . ASP   B 1 137 ? -22.663 -15.866 -64.317 1.00 54.48 ? 578  ASP   B CG  1 
ATOM   3955 O  OD1 . ASP   B 1 137 ? -23.183 -16.816 -63.689 1.00 39.63 ? 578  ASP   B OD1 1 
ATOM   3956 O  OD2 . ASP   B 1 137 ? -22.004 -16.035 -65.367 1.00 30.52 ? 578  ASP   B OD2 1 
ATOM   3957 N  N   . THR   B 1 138 ? -20.077 -13.550 -61.633 1.00 17.27 ? 579  THR   B N   1 
ATOM   3958 C  CA  . THR   B 1 138 ? -18.636 -13.742 -61.655 1.00 17.81 ? 579  THR   B CA  1 
ATOM   3959 C  C   . THR   B 1 138 ? -17.946 -13.026 -60.498 1.00 19.13 ? 579  THR   B C   1 
ATOM   3960 O  O   . THR   B 1 138 ? -18.457 -12.053 -59.941 1.00 18.24 ? 579  THR   B O   1 
ATOM   3961 C  CB  . THR   B 1 138 ? -18.039 -13.322 -63.006 1.00 22.02 ? 579  THR   B CB  1 
ATOM   3962 O  OG1 . THR   B 1 138 ? -16.800 -13.998 -63.196 1.00 25.20 ? 579  THR   B OG1 1 
ATOM   3963 C  CG2 . THR   B 1 138 ? -17.820 -11.825 -63.077 1.00 22.79 ? 579  THR   B CG2 1 
ATOM   3964 N  N   . ALA   B 1 139 ? -16.768 -13.534 -60.156 1.00 17.18 ? 580  ALA   B N   1 
ATOM   3965 C  CA  . ALA   B 1 139 ? -15.847 -12.923 -59.206 1.00 16.79 ? 580  ALA   B CA  1 
ATOM   3966 C  C   . ALA   B 1 139 ? -14.900 -11.974 -59.946 1.00 22.01 ? 580  ALA   B C   1 
ATOM   3967 O  O   . ALA   B 1 139 ? -14.654 -12.122 -61.142 1.00 18.35 ? 580  ALA   B O   1 
ATOM   3968 C  CB  . ALA   B 1 139 ? -15.023 -14.004 -58.500 1.00 17.66 ? 580  ALA   B CB  1 
ATOM   3969 N  N   . CYS   B 1 140 ? -14.359 -11.000 -59.218 1.00 16.47 ? 581  CYS   B N   1 
ATOM   3970 C  CA  . CYS   B 1 140 ? -13.555 -9.944  -59.826 1.00 14.39 ? 581  CYS   B CA  1 
ATOM   3971 C  C   . CYS   B 1 140 ? -12.869 -9.126  -58.738 1.00 13.80 ? 581  CYS   B C   1 
ATOM   3972 O  O   . CYS   B 1 140 ? -13.464 -8.866  -57.690 1.00 13.01 ? 581  CYS   B O   1 
ATOM   3973 C  CB  . CYS   B 1 140 ? -14.433 -9.006  -60.653 1.00 15.48 ? 581  CYS   B CB  1 
ATOM   3974 S  SG  . CYS   B 1 140 ? -13.443 -7.704  -61.445 1.00 20.08 ? 581  CYS   B SG  1 
ATOM   3975 N  N   . GLY   B 1 141 ? -11.621 -8.719  -58.986 1.00 16.01 ? 582  GLY   B N   1 
ATOM   3976 C  CA  . GLY   B 1 141 ? -11.008 -7.693  -58.154 1.00 16.31 ? 582  GLY   B CA  1 
ATOM   3977 C  C   . GLY   B 1 141 ? -10.992 -7.996  -56.668 1.00 14.80 ? 582  GLY   B C   1 
ATOM   3978 O  O   . GLY   B 1 141 ? -11.331 -7.139  -55.839 1.00 13.95 ? 582  GLY   B O   1 
ATOM   3979 N  N   . PHE   B 1 142 ? -10.591 -9.221  -56.323 1.00 13.32 ? 583  PHE   B N   1 
ATOM   3980 C  CA  . PHE   B 1 142 ? -10.431 -9.729  -54.962 1.00 13.62 ? 583  PHE   B CA  1 
ATOM   3981 C  C   . PHE   B 1 142 ? -11.777 -10.061 -54.318 1.00 14.14 ? 583  PHE   B C   1 
ATOM   3982 O  O   . PHE   B 1 142 ? -11.791 -10.437 -53.142 1.00 14.56 ? 583  PHE   B O   1 
ATOM   3983 C  CB  . PHE   B 1 142 ? -9.635  -8.817  -54.001 1.00 14.19 ? 583  PHE   B CB  1 
ATOM   3984 C  CG  . PHE   B 1 142 ? -8.359  -8.229  -54.574 1.00 14.93 ? 583  PHE   B CG  1 
ATOM   3985 C  CD1 . PHE   B 1 142 ? -7.683  -8.820  -55.635 1.00 16.89 ? 583  PHE   B CD1 1 
ATOM   3986 C  CD2 . PHE   B 1 142 ? -7.849  -7.043  -54.038 1.00 16.10 ? 583  PHE   B CD2 1 
ATOM   3987 C  CE1 . PHE   B 1 142 ? -6.508  -8.232  -56.161 1.00 17.71 ? 583  PHE   B CE1 1 
ATOM   3988 C  CE2 . PHE   B 1 142 ? -6.671  -6.468  -54.542 1.00 21.07 ? 583  PHE   B CE2 1 
ATOM   3989 C  CZ  . PHE   B 1 142 ? -6.010  -7.060  -55.618 1.00 18.37 ? 583  PHE   B CZ  1 
ATOM   3990 N  N   . CYS   B 1 143 ? -12.888 -9.956  -55.040 1.00 13.58 ? 584  CYS   B N   1 
ATOM   3991 C  CA  . CYS   B 1 143 ? -14.238 -10.115 -54.494 1.00 14.42 ? 584  CYS   B CA  1 
ATOM   3992 C  C   . CYS   B 1 143 ? -14.923 -11.344 -55.068 1.00 15.41 ? 584  CYS   B C   1 
ATOM   3993 O  O   . CYS   B 1 143 ? -14.924 -11.542 -56.290 1.00 15.51 ? 584  CYS   B O   1 
ATOM   3994 C  CB  . CYS   B 1 143 ? -15.108 -8.905  -54.818 1.00 14.61 ? 584  CYS   B CB  1 
ATOM   3995 S  SG  . CYS   B 1 143 ? -14.406 -7.283  -54.393 1.00 13.68 ? 584  CYS   B SG  1 
ATOM   3996 N  N   . PHE   B 1 144 ? -15.541 -12.143 -54.188 1.00 13.96 ? 585  PHE   B N   1 
ATOM   3997 C  CA  . PHE   B 1 144 ? -16.269 -13.332 -54.628 1.00 15.76 ? 585  PHE   B CA  1 
ATOM   3998 C  C   . PHE   B 1 144 ? -17.777 -13.128 -54.682 1.00 13.22 ? 585  PHE   B C   1 
ATOM   3999 O  O   . PHE   B 1 144 ? -18.414 -13.438 -55.697 1.00 16.83 ? 585  PHE   B O   1 
ATOM   4000 C  CB  . PHE   B 1 144 ? -15.934 -14.506 -53.706 1.00 16.92 ? 585  PHE   B CB  1 
ATOM   4001 C  CG  . PHE   B 1 144 ? -14.509 -14.927 -53.801 1.00 16.16 ? 585  PHE   B CG  1 
ATOM   4002 C  CD1 . PHE   B 1 144 ? -14.108 -15.840 -54.767 1.00 19.13 ? 585  PHE   B CD1 1 
ATOM   4003 C  CD2 . PHE   B 1 144 ? -13.561 -14.378 -52.968 1.00 17.42 ? 585  PHE   B CD2 1 
ATOM   4004 C  CE1 . PHE   B 1 144 ? -12.798 -16.223 -54.883 1.00 18.26 ? 585  PHE   B CE1 1 
ATOM   4005 C  CE2 . PHE   B 1 144 ? -12.238 -14.751 -53.069 1.00 16.50 ? 585  PHE   B CE2 1 
ATOM   4006 C  CZ  . PHE   B 1 144 ? -11.848 -15.682 -54.035 1.00 19.77 ? 585  PHE   B CZ  1 
ATOM   4007 N  N   . PHE   B 1 145 ? -18.364 -12.610 -53.606 1.00 15.48 ? 586  PHE   B N   1 
ATOM   4008 C  CA  . PHE   B 1 145 ? -19.775 -12.288 -53.534 1.00 14.52 ? 586  PHE   B CA  1 
ATOM   4009 C  C   . PHE   B 1 145 ? -19.918 -10.842 -53.088 1.00 15.25 ? 586  PHE   B C   1 
ATOM   4010 O  O   . PHE   B 1 145 ? -19.090 -10.320 -52.328 1.00 13.72 ? 586  PHE   B O   1 
ATOM   4011 C  CB  . PHE   B 1 145 ? -20.526 -13.209 -52.553 1.00 16.04 ? 586  PHE   B CB  1 
ATOM   4012 C  CG  . PHE   B 1 145 ? -20.339 -14.673 -52.845 1.00 17.15 ? 586  PHE   B CG  1 
ATOM   4013 C  CD1 . PHE   B 1 145 ? -20.763 -15.212 -54.051 1.00 16.85 ? 586  PHE   B CD1 1 
ATOM   4014 C  CD2 . PHE   B 1 145 ? -19.752 -15.505 -51.920 1.00 17.77 ? 586  PHE   B CD2 1 
ATOM   4015 C  CE1 . PHE   B 1 145 ? -20.589 -16.564 -54.331 1.00 18.14 ? 586  PHE   B CE1 1 
ATOM   4016 C  CE2 . PHE   B 1 145 ? -19.571 -16.862 -52.183 1.00 23.26 ? 586  PHE   B CE2 1 
ATOM   4017 C  CZ  . PHE   B 1 145 ? -19.997 -17.388 -53.396 1.00 20.48 ? 586  PHE   B CZ  1 
ATOM   4018 N  N   . ASN   B 1 146 ? -20.974 -10.195 -53.566 1.00 14.59 ? 587  ASN   B N   1 
ATOM   4019 C  CA  . ASN   B 1 146 ? -21.114 -8.756  -53.354 1.00 11.90 ? 587  ASN   B CA  1 
ATOM   4020 C  C   . ASN   B 1 146 ? -21.762 -8.524  -51.988 1.00 11.31 ? 587  ASN   B C   1 
ATOM   4021 O  O   . ASN   B 1 146 ? -22.978 -8.370  -51.865 1.00 13.39 ? 587  ASN   B O   1 
ATOM   4022 C  CB  . ASN   B 1 146 ? -21.874 -8.080  -54.488 1.00 14.82 ? 587  ASN   B CB  1 
ATOM   4023 C  CG  . ASN   B 1 146 ? -21.700 -6.580  -54.453 1.00 14.31 ? 587  ASN   B CG  1 
ATOM   4024 O  OD1 . ASN   B 1 146 ? -21.746 -5.969  -53.371 1.00 13.86 ? 587  ASN   B OD1 1 
ATOM   4025 N  ND2 . ASN   B 1 146 ? -21.414 -5.982  -55.603 1.00 12.89 ? 587  ASN   B ND2 1 
ATOM   4026 N  N   . THR   B 1 147 ? -20.928 -8.498  -50.943 1.00 11.05 ? 588  THR   B N   1 
ATOM   4027 C  CA  . THR   B 1 147 ? -21.405 -8.359  -49.570 1.00 13.16 ? 588  THR   B CA  1 
ATOM   4028 C  C   . THR   B 1 147 ? -22.375 -7.188  -49.376 1.00 12.28 ? 588  THR   B C   1 
ATOM   4029 O  O   . THR   B 1 147 ? -23.457 -7.353  -48.792 1.00 13.98 ? 588  THR   B O   1 
ATOM   4030 C  CB  . THR   B 1 147 ? -20.190 -8.204  -48.675 1.00 14.83 ? 588  THR   B CB  1 
ATOM   4031 O  OG1 . THR   B 1 147 ? -19.374 -9.367  -48.825 1.00 14.12 ? 588  THR   B OG1 1 
ATOM   4032 C  CG2 . THR   B 1 147 ? -20.604 -8.031  -47.189 1.00 16.86 ? 588  THR   B CG2 1 
ATOM   4033 N  N   . ALA   B 1 148 ? -22.040 -5.998  -49.861 1.00 12.50 ? 589  ALA   B N   1 
ATOM   4034 C  CA  . ALA   B 1 148 ? -22.931 -4.851  -49.659 1.00 12.99 ? 589  ALA   B CA  1 
ATOM   4035 C  C   . ALA   B 1 148 ? -24.262 -5.031  -50.393 1.00 12.64 ? 589  ALA   B C   1 
ATOM   4036 O  O   . ALA   B 1 148 ? -25.330 -4.724  -49.841 1.00 13.54 ? 589  ALA   B O   1 
ATOM   4037 C  CB  . ALA   B 1 148 ? -22.259 -3.546  -50.083 1.00 16.01 ? 589  ALA   B CB  1 
ATOM   4038 N  N   . ALA   B 1 149 ? -24.220 -5.507  -51.642 1.00 13.12 ? 590  ALA   B N   1 
ATOM   4039 C  CA  . ALA   B 1 149 ? -25.451 -5.713  -52.394 1.00 14.56 ? 590  ALA   B CA  1 
ATOM   4040 C  C   . ALA   B 1 149 ? -26.325 -6.755  -51.718 1.00 13.75 ? 590  ALA   B C   1 
ATOM   4041 O  O   . ALA   B 1 149 ? -27.550 -6.577  -51.588 1.00 14.42 ? 590  ALA   B O   1 
ATOM   4042 C  CB  . ALA   B 1 149 ? -25.125 -6.138  -53.832 1.00 16.73 ? 590  ALA   B CB  1 
ATOM   4043 N  N   . LEU   B 1 150 ? -25.714 -7.865  -51.312 1.00 13.50 ? 591  LEU   B N   1 
ATOM   4044 C  CA  . LEU   B 1 150 ? -26.435 -8.899  -50.582 1.00 14.77 ? 591  LEU   B CA  1 
ATOM   4045 C  C   . LEU   B 1 150 ? -27.069 -8.322  -49.330 1.00 17.12 ? 591  LEU   B C   1 
ATOM   4046 O  O   . LEU   B 1 150 ? -28.225 -8.627  -49.001 1.00 15.79 ? 591  LEU   B O   1 
ATOM   4047 C  CB  . LEU   B 1 150 ? -25.498 -10.039 -50.215 1.00 15.04 ? 591  LEU   B CB  1 
ATOM   4048 C  CG  . LEU   B 1 150 ? -25.086 -10.899 -51.415 1.00 14.67 ? 591  LEU   B CG  1 
ATOM   4049 C  CD1 . LEU   B 1 150 ? -23.916 -11.764 -51.028 1.00 16.58 ? 591  LEU   B CD1 1 
ATOM   4050 C  CD2 . LEU   B 1 150 ? -26.272 -11.743 -51.891 1.00 19.25 ? 591  LEU   B CD2 1 
ATOM   4051 N  N   . THR   B 1 151 ? -26.338 -7.466  -48.622 1.00 15.16 ? 592  THR   B N   1 
ATOM   4052 C  CA  . THR   B 1 151 ? -26.851 -6.915  -47.377 1.00 15.95 ? 592  THR   B CA  1 
ATOM   4053 C  C   . THR   B 1 151 ? -28.076 -6.046  -47.620 1.00 15.38 ? 592  THR   B C   1 
ATOM   4054 O  O   . THR   B 1 151 ? -29.042 -6.094  -46.843 1.00 14.47 ? 592  THR   B O   1 
ATOM   4055 C  CB  . THR   B 1 151 ? -25.735 -6.132  -46.679 1.00 14.44 ? 592  THR   B CB  1 
ATOM   4056 O  OG1 . THR   B 1 151 ? -24.702 -7.035  -46.294 1.00 15.66 ? 592  THR   B OG1 1 
ATOM   4057 C  CG2 . THR   B 1 151 ? -26.289 -5.451  -45.442 1.00 14.90 ? 592  THR   B CG2 1 
ATOM   4058 N  N   . ALA   B 1 152 ? -28.058 -5.257  -48.689 1.00 13.69 ? 593  ALA   B N   1 
ATOM   4059 C  CA  . ALA   B 1 152 ? -29.221 -4.452  -49.053 1.00 15.88 ? 593  ALA   B CA  1 
ATOM   4060 C  C   . ALA   B 1 152 ? -30.437 -5.335  -49.306 1.00 19.37 ? 593  ALA   B C   1 
ATOM   4061 O  O   . ALA   B 1 152 ? -31.532 -5.057  -48.803 1.00 17.22 ? 593  ALA   B O   1 
ATOM   4062 C  CB  . ALA   B 1 152 ? -28.898 -3.612  -50.290 1.00 15.95 ? 593  ALA   B CB  1 
ATOM   4063 N  N   . ARG   B 1 153 ? -30.255 -6.425  -50.063 1.00 17.11 ? 594  ARG   B N   1 
ATOM   4064 C  CA  . ARG   B 1 153 ? -31.374 -7.322  -50.346 1.00 18.10 ? 594  ARG   B CA  1 
ATOM   4065 C  C   . ARG   B 1 153 ? -31.801 -8.074  -49.098 1.00 16.58 ? 594  ARG   B C   1 
ATOM   4066 O  O   . ARG   B 1 153 ? -33.005 -8.289  -48.885 1.00 19.43 ? 594  ARG   B O   1 
ATOM   4067 C  CB  . ARG   B 1 153 ? -31.004 -8.314  -51.455 1.00 18.94 ? 594  ARG   B CB  1 
ATOM   4068 C  CG  . ARG   B 1 153 ? -30.804 -7.718  -52.836 1.00 21.27 ? 594  ARG   B CG  1 
ATOM   4069 C  CD  . ARG   B 1 153 ? -32.066 -7.053  -53.329 1.00 28.00 ? 594  ARG   B CD  1 
ATOM   4070 N  NE  . ARG   B 1 153 ? -32.001 -6.736  -54.757 1.00 20.24 ? 594  ARG   B NE  1 
ATOM   4071 C  CZ  . ARG   B 1 153 ? -32.677 -5.740  -55.318 1.00 32.49 ? 594  ARG   B CZ  1 
ATOM   4072 N  NH1 . ARG   B 1 153 ? -33.455 -4.960  -54.565 1.00 21.46 ? 594  ARG   B NH1 1 
ATOM   4073 N  NH2 . ARG   B 1 153 ? -32.569 -5.515  -56.627 1.00 30.21 ? 594  ARG   B NH2 1 
ATOM   4074 N  N   . TYR   B 1 154 ? -30.842 -8.495  -48.270 1.00 18.62 ? 595  TYR   B N   1 
ATOM   4075 C  CA  . TYR   B 1 154 ? -31.181 -9.123  -47.000 1.00 17.72 ? 595  TYR   B CA  1 
ATOM   4076 C  C   . TYR   B 1 154 ? -32.024 -8.179  -46.150 1.00 19.28 ? 595  TYR   B C   1 
ATOM   4077 O  O   . TYR   B 1 154 ? -33.070 -8.567  -45.605 1.00 18.12 ? 595  TYR   B O   1 
ATOM   4078 C  CB  . TYR   B 1 154 ? -29.906 -9.552  -46.252 1.00 15.58 ? 595  TYR   B CB  1 
ATOM   4079 C  CG  . TYR   B 1 154 ? -30.252 -10.019 -44.867 1.00 17.77 ? 595  TYR   B CG  1 
ATOM   4080 C  CD1 . TYR   B 1 154 ? -30.711 -11.312 -44.643 1.00 22.10 ? 595  TYR   B CD1 1 
ATOM   4081 C  CD2 . TYR   B 1 154 ? -30.123 -9.172  -43.778 1.00 15.73 ? 595  TYR   B CD2 1 
ATOM   4082 C  CE1 . TYR   B 1 154 ? -31.046 -11.737 -43.364 1.00 17.55 ? 595  TYR   B CE1 1 
ATOM   4083 C  CE2 . TYR   B 1 154 ? -30.481 -9.578  -42.521 1.00 15.94 ? 595  TYR   B CE2 1 
ATOM   4084 C  CZ  . TYR   B 1 154 ? -30.930 -10.856 -42.314 1.00 22.32 ? 595  TYR   B CZ  1 
ATOM   4085 O  OH  . TYR   B 1 154 ? -31.272 -11.240 -41.033 1.00 18.72 ? 595  TYR   B OH  1 
ATOM   4086 N  N   . ALA   B 1 155 ? -31.605 -6.919  -46.056 1.00 16.91 ? 596  ALA   B N   1 
ATOM   4087 C  CA  . ALA   B 1 155 ? -32.351 -5.932  -45.281 1.00 15.70 ? 596  ALA   B CA  1 
ATOM   4088 C  C   . ALA   B 1 155 ? -33.789 -5.828  -45.773 1.00 16.71 ? 596  ALA   B C   1 
ATOM   4089 O  O   . ALA   B 1 155 ? -34.730 -5.777  -44.968 1.00 18.03 ? 596  ALA   B O   1 
ATOM   4090 C  CB  . ALA   B 1 155 ? -31.671 -4.572  -45.388 1.00 16.99 ? 596  ALA   B CB  1 
ATOM   4091 N  N   . GLN   B 1 156 ? -33.977 -5.789  -47.092 1.00 16.81 ? 597  GLN   B N   1 
ATOM   4092 C  CA  . GLN   B 1 156 ? -35.317 -5.757  -47.660 1.00 21.08 ? 597  GLN   B CA  1 
ATOM   4093 C  C   . GLN   B 1 156 ? -36.094 -7.010  -47.291 1.00 22.27 ? 597  GLN   B C   1 
ATOM   4094 O  O   . GLN   B 1 156 ? -37.296 -6.935  -47.000 1.00 21.72 ? 597  GLN   B O   1 
ATOM   4095 C  CB  . GLN   B 1 156 ? -35.219 -5.553  -49.173 1.00 15.44 ? 597  GLN   B CB  1 
ATOM   4096 C  CG  . GLN   B 1 156 ? -34.880 -4.113  -49.535 1.00 19.11 ? 597  GLN   B CG  1 
ATOM   4097 C  CD  . GLN   B 1 156 ? -34.500 -3.885  -50.992 1.00 17.89 ? 597  GLN   B CD  1 
ATOM   4098 O  OE1 . GLN   B 1 156 ? -34.228 -4.828  -51.748 1.00 21.30 ? 597  GLN   B OE1 1 
ATOM   4099 N  NE2 . GLN   B 1 156 ? -34.484 -2.620  -51.394 1.00 17.64 ? 597  GLN   B NE2 1 
ATOM   4100 N  N   . SER   B 1 157 ? -35.419 -8.155  -47.239 1.00 18.55 ? 598  SER   B N   1 
ATOM   4101 C  CA  . SER   B 1 157 ? -36.096 -9.413  -46.960 1.00 20.88 ? 598  SER   B CA  1 
ATOM   4102 C  C   . SER   B 1 157 ? -36.638 -9.487  -45.535 1.00 27.14 ? 598  SER   B C   1 
ATOM   4103 O  O   . SER   B 1 157 ? -37.605 -10.214 -45.294 1.00 26.03 ? 598  SER   B O   1 
ATOM   4104 C  CB  . SER   B 1 157 ? -35.181 -10.596 -47.256 1.00 20.98 ? 598  SER   B CB  1 
ATOM   4105 O  OG  . SER   B 1 157 ? -34.263 -10.812 -46.200 1.00 21.61 ? 598  SER   B OG  1 
ATOM   4106 N  N   . ILE   B 1 158 ? -36.052 -8.760  -44.581 1.00 20.54 ? 599  ILE   B N   1 
ATOM   4107 C  CA  . ILE   B 1 158 ? -36.538 -8.781  -43.198 1.00 21.56 ? 599  ILE   B CA  1 
ATOM   4108 C  C   . ILE   B 1 158 ? -37.347 -7.539  -42.835 1.00 18.54 ? 599  ILE   B C   1 
ATOM   4109 O  O   . ILE   B 1 158 ? -37.722 -7.364  -41.659 1.00 22.34 ? 599  ILE   B O   1 
ATOM   4110 C  CB  . ILE   B 1 158 ? -35.416 -9.030  -42.176 1.00 17.46 ? 599  ILE   B CB  1 
ATOM   4111 C  CG1 . ILE   B 1 158 ? -34.358 -7.920  -42.253 1.00 15.92 ? 599  ILE   B CG1 1 
ATOM   4112 C  CG2 . ILE   B 1 158 ? -34.782 -10.395 -42.419 1.00 21.47 ? 599  ILE   B CG2 1 
ATOM   4113 C  CD1 . ILE   B 1 158 ? -33.426 -7.915  -41.060 1.00 21.19 ? 599  ILE   B CD1 1 
ATOM   4114 N  N   . THR   B 1 159 ? -37.616 -6.665  -43.800 1.00 20.05 ? 600  THR   B N   1 
ATOM   4115 C  CA  . THR   B 1 159 ? -38.483 -5.526  -43.555 1.00 19.96 ? 600  THR   B CA  1 
ATOM   4116 C  C   . THR   B 1 159 ? -39.580 -5.511  -44.609 1.00 37.47 ? 600  THR   B C   1 
ATOM   4117 O  O   . THR   B 1 159 ? -40.601 -6.191  -44.452 1.00 26.91 ? 600  THR   B O   1 
ATOM   4118 C  CB  . THR   B 1 159 ? -37.678 -4.219  -43.494 1.00 18.41 ? 600  THR   B CB  1 
ATOM   4119 O  OG1 . THR   B 1 159 ? -36.938 -4.046  -44.716 1.00 17.60 ? 600  THR   B OG1 1 
ATOM   4120 C  CG2 . THR   B 1 159 ? -36.714 -4.257  -42.310 1.00 18.55 ? 600  THR   B CG2 1 
ATOM   4121 N  N   . ARG   B 1 160 ? -39.375 -4.766  -45.690 1.00 20.97 ? 601  ARG   B N   1 
ATOM   4122 C  CA  . ARG   B 1 160 ? -40.275 -4.796  -46.832 1.00 25.99 ? 601  ARG   B CA  1 
ATOM   4123 C  C   . ARG   B 1 160 ? -39.450 -4.636  -48.100 1.00 29.49 ? 601  ARG   B C   1 
ATOM   4124 O  O   . ARG   B 1 160 ? -38.358 -4.057  -48.076 1.00 24.06 ? 601  ARG   B O   1 
ATOM   4125 C  CB  . ARG   B 1 160 ? -41.347 -3.703  -46.744 1.00 23.92 ? 601  ARG   B CB  1 
ATOM   4126 C  CG  . ARG   B 1 160 ? -40.793 -2.318  -46.738 1.00 30.16 ? 601  ARG   B CG  1 
ATOM   4127 C  CD  . ARG   B 1 160 ? -41.891 -1.291  -46.821 1.00 27.11 ? 601  ARG   B CD  1 
ATOM   4128 N  NE  . ARG   B 1 160 ? -41.402 -0.112  -47.506 1.00 36.06 ? 601  ARG   B NE  1 
ATOM   4129 C  CZ  . ARG   B 1 160 ? -40.669 0.823   -46.921 1.00 28.47 ? 601  ARG   B CZ  1 
ATOM   4130 N  NH1 . ARG   B 1 160 ? -40.362 0.705   -45.637 1.00 36.90 ? 601  ARG   B NH1 1 
ATOM   4131 N  NH2 . ARG   B 1 160 ? -40.247 1.868   -47.619 1.00 35.70 ? 601  ARG   B NH2 1 
ATOM   4132 N  N   . GLU   B 1 161 ? -39.982 -5.152  -49.212 1.00 28.94 ? 602  GLU   B N   1 
ATOM   4133 C  CA  . GLU   B 1 161 ? -39.201 -5.199  -50.447 1.00 36.13 ? 602  GLU   B CA  1 
ATOM   4134 C  C   . GLU   B 1 161 ? -38.766 -3.816  -50.916 1.00 25.32 ? 602  GLU   B C   1 
ATOM   4135 O  O   . GLU   B 1 161 ? -37.689 -3.678  -51.513 1.00 23.87 ? 602  GLU   B O   1 
ATOM   4136 C  CB  . GLU   B 1 161 ? -39.966 -5.944  -51.545 1.00 34.66 ? 602  GLU   B CB  1 
ATOM   4137 C  CG  . GLU   B 1 161 ? -40.293 -7.385  -51.176 1.00 44.36 ? 602  GLU   B CG  1 
ATOM   4138 C  CD  . GLU   B 1 161 ? -39.046 -8.225  -50.971 1.00 62.40 ? 602  GLU   B CD  1 
ATOM   4139 O  OE1 . GLU   B 1 161 ? -38.167 -8.210  -51.859 1.00 60.02 ? 602  GLU   B OE1 1 
ATOM   4140 O  OE2 . GLU   B 1 161 ? -38.941 -8.896  -49.921 1.00 62.40 ? 602  GLU   B OE2 1 
ATOM   4141 N  N   . SER   B 1 162 ? -39.562 -2.787  -50.648 1.00 20.76 ? 603  SER   B N   1 
ATOM   4142 C  CA  . SER   B 1 162 ? -39.292 -1.432  -51.100 1.00 27.82 ? 603  SER   B CA  1 
ATOM   4143 C  C   . SER   B 1 162 ? -38.451 -0.613  -50.117 1.00 18.84 ? 603  SER   B C   1 
ATOM   4144 O  O   . SER   B 1 162 ? -38.310 0.599   -50.319 1.00 22.55 ? 603  SER   B O   1 
ATOM   4145 C  CB  . SER   B 1 162 ? -40.605 -0.697  -51.385 1.00 31.13 ? 603  SER   B CB  1 
ATOM   4146 O  OG  . SER   B 1 162 ? -41.331 -0.475  -50.183 1.00 40.85 ? 603  SER   B OG  1 
ATOM   4147 N  N   . LEU   B 1 163 ? -37.925 -1.231  -49.062 1.00 22.11 ? 604  LEU   B N   1 
ATOM   4148 C  CA  . LEU   B 1 163 ? -37.065 -0.512  -48.124 1.00 20.58 ? 604  LEU   B CA  1 
ATOM   4149 C  C   . LEU   B 1 163 ? -36.005 0.263   -48.894 1.00 18.54 ? 604  LEU   B C   1 
ATOM   4150 O  O   . LEU   B 1 163 ? -35.287 -0.306  -49.721 1.00 18.84 ? 604  LEU   B O   1 
ATOM   4151 C  CB  . LEU   B 1 163 ? -36.394 -1.528  -47.212 1.00 17.98 ? 604  LEU   B CB  1 
ATOM   4152 C  CG  . LEU   B 1 163 ? -35.562 -0.878  -46.089 1.00 23.91 ? 604  LEU   B CG  1 
ATOM   4153 C  CD1 . LEU   B 1 163 ? -36.451 -0.463  -44.927 1.00 23.21 ? 604  LEU   B CD1 1 
ATOM   4154 C  CD2 . LEU   B 1 163 ? -34.444 -1.791  -45.587 1.00 21.59 ? 604  LEU   B CD2 1 
ATOM   4155 N  N   . ARG   B 1 164 ? -35.928 1.569   -48.661 1.00 17.60 ? 605  ARG   B N   1 
ATOM   4156 C  CA  . ARG   B 1 164 ? -34.997 2.411   -49.402 1.00 19.86 ? 605  ARG   B CA  1 
ATOM   4157 C  C   . ARG   B 1 164 ? -33.607 2.269   -48.796 1.00 17.38 ? 605  ARG   B C   1 
ATOM   4158 O  O   . ARG   B 1 164 ? -33.363 2.711   -47.664 1.00 19.49 ? 605  ARG   B O   1 
ATOM   4159 C  CB  . ARG   B 1 164 ? -35.471 3.859   -49.375 1.00 20.83 ? 605  ARG   B CB  1 
ATOM   4160 C  CG  . ARG   B 1 164 ? -36.794 4.068   -50.156 1.00 19.63 ? 605  ARG   B CG  1 
ATOM   4161 C  CD  . ARG   B 1 164 ? -37.043 5.548   -50.393 1.00 22.45 ? 605  ARG   B CD  1 
ATOM   4162 N  NE  . ARG   B 1 164 ? -37.243 6.244   -49.126 1.00 26.28 ? 605  ARG   B NE  1 
ATOM   4163 C  CZ  . ARG   B 1 164 ? -38.316 6.108   -48.345 1.00 32.65 ? 605  ARG   B CZ  1 
ATOM   4164 N  NH1 . ARG   B 1 164 ? -39.328 5.313   -48.697 1.00 30.49 ? 605  ARG   B NH1 1 
ATOM   4165 N  NH2 . ARG   B 1 164 ? -38.385 6.783   -47.208 1.00 31.71 ? 605  ARG   B NH2 1 
ATOM   4166 N  N   . VAL   B 1 165 ? -32.684 1.666   -49.542 1.00 17.38 ? 606  VAL   B N   1 
ATOM   4167 C  CA  . VAL   B 1 165 ? -31.310 1.482   -49.080 1.00 13.64 ? 606  VAL   B CA  1 
ATOM   4168 C  C   . VAL   B 1 165 ? -30.386 2.364   -49.907 1.00 16.78 ? 606  VAL   B C   1 
ATOM   4169 O  O   . VAL   B 1 165 ? -30.426 2.331   -51.142 1.00 16.93 ? 606  VAL   B O   1 
ATOM   4170 C  CB  . VAL   B 1 165 ? -30.886 0.011   -49.141 1.00 17.06 ? 606  VAL   B CB  1 
ATOM   4171 C  CG1 . VAL   B 1 165 ? -29.456 -0.124  -48.596 1.00 15.88 ? 606  VAL   B CG1 1 
ATOM   4172 C  CG2 . VAL   B 1 165 ? -31.828 -0.853  -48.343 1.00 19.29 ? 606  VAL   B CG2 1 
ATOM   4173 N  N   . LEU   B 1 166 ? -29.582 3.185   -49.225 1.00 14.99 ? 607  LEU   B N   1 
ATOM   4174 C  CA  . LEU   B 1 166 ? -28.509 3.942   -49.855 1.00 17.26 ? 607  LEU   B CA  1 
ATOM   4175 C  C   . LEU   B 1 166 ? -27.204 3.183   -49.659 1.00 16.39 ? 607  LEU   B C   1 
ATOM   4176 O  O   . LEU   B 1 166 ? -26.850 2.838   -48.527 1.00 16.04 ? 607  LEU   B O   1 
ATOM   4177 C  CB  . LEU   B 1 166 ? -28.380 5.345   -49.251 1.00 15.42 ? 607  LEU   B CB  1 
ATOM   4178 C  CG  . LEU   B 1 166 ? -27.127 6.149   -49.617 1.00 16.47 ? 607  LEU   B CG  1 
ATOM   4179 C  CD1 . LEU   B 1 166 ? -27.091 6.414   -51.127 1.00 20.20 ? 607  LEU   B CD1 1 
ATOM   4180 C  CD2 . LEU   B 1 166 ? -27.035 7.451   -48.836 1.00 15.23 ? 607  LEU   B CD2 1 
ATOM   4181 N  N   . ILE   B 1 167 ? -26.503 2.917   -50.763 1.00 13.27 ? 608  ILE   B N   1 
ATOM   4182 C  CA  . ILE   B 1 167 ? -25.126 2.433   -50.705 1.00 13.16 ? 608  ILE   B CA  1 
ATOM   4183 C  C   . ILE   B 1 167 ? -24.220 3.571   -51.156 1.00 12.66 ? 608  ILE   B C   1 
ATOM   4184 O  O   . ILE   B 1 167 ? -24.288 4.018   -52.305 1.00 13.76 ? 608  ILE   B O   1 
ATOM   4185 C  CB  . ILE   B 1 167 ? -24.881 1.177   -51.555 1.00 13.99 ? 608  ILE   B CB  1 
ATOM   4186 C  CG1 . ILE   B 1 167 ? -25.747 0.000   -51.096 1.00 14.99 ? 608  ILE   B CG1 1 
ATOM   4187 C  CG2 . ILE   B 1 167 ? -23.381 0.805   -51.509 1.00 13.30 ? 608  ILE   B CG2 1 
ATOM   4188 C  CD1 . ILE   B 1 167 ? -25.738 -1.200  -52.040 1.00 14.63 ? 608  ILE   B CD1 1 
ATOM   4189 N  N   . VAL   B 1 168 ? -23.367 4.046   -50.241 1.00 13.53 ? 609  VAL   B N   1 
ATOM   4190 C  CA  . VAL   B 1 168 ? -22.316 5.001   -50.576 1.00 12.41 ? 609  VAL   B CA  1 
ATOM   4191 C  C   . VAL   B 1 168 ? -21.011 4.229   -50.649 1.00 13.17 ? 609  VAL   B C   1 
ATOM   4192 O  O   . VAL   B 1 168 ? -20.619 3.593   -49.664 1.00 12.22 ? 609  VAL   B O   1 
ATOM   4193 C  CB  . VAL   B 1 168 ? -22.221 6.128   -49.541 1.00 15.20 ? 609  VAL   B CB  1 
ATOM   4194 C  CG1 . VAL   B 1 168 ? -20.996 6.985   -49.822 1.00 14.45 ? 609  VAL   B CG1 1 
ATOM   4195 C  CG2 . VAL   B 1 168 ? -23.453 6.993   -49.611 1.00 17.83 ? 609  VAL   B CG2 1 
ATOM   4196 N  N   . ASP   B 1 169 ? -20.360 4.259   -51.800 1.00 12.64 ? 610  ASP   B N   1 
ATOM   4197 C  CA  . ASP   B 1 169 ? -19.147 3.480   -52.050 1.00 12.19 ? 610  ASP   B CA  1 
ATOM   4198 C  C   . ASP   B 1 169 ? -17.981 4.459   -52.194 1.00 10.29 ? 610  ASP   B C   1 
ATOM   4199 O  O   . ASP   B 1 169 ? -17.793 5.090   -53.238 1.00 12.91 ? 610  ASP   B O   1 
ATOM   4200 C  CB  . ASP   B 1 169 ? -19.384 2.628   -53.300 1.00 12.09 ? 610  ASP   B CB  1 
ATOM   4201 C  CG  . ASP   B 1 169 ? -18.250 1.680   -53.613 1.00 12.68 ? 610  ASP   B CG  1 
ATOM   4202 O  OD1 . ASP   B 1 169 ? -17.090 1.965   -53.240 1.00 12.01 ? 610  ASP   B OD1 1 
ATOM   4203 O  OD2 . ASP   B 1 169 ? -18.542 0.662   -54.320 1.00 12.51 ? 610  ASP   B OD2 1 
ATOM   4204 N  N   . TRP   B 1 170 ? -17.195 4.611   -51.118 1.00 10.76 ? 611  TRP   B N   1 
ATOM   4205 C  CA  . TRP   B 1 170 ? -16.054 5.524   -51.155 1.00 11.35 ? 611  TRP   B CA  1 
ATOM   4206 C  C   . TRP   B 1 170 ? -14.710 4.826   -51.312 1.00 12.24 ? 611  TRP   B C   1 
ATOM   4207 O  O   . TRP   B 1 170 ? -13.685 5.494   -51.258 1.00 10.64 ? 611  TRP   B O   1 
ATOM   4208 C  CB  . TRP   B 1 170 ? -16.076 6.498   -49.978 1.00 12.49 ? 611  TRP   B CB  1 
ATOM   4209 C  CG  . TRP   B 1 170 ? -15.761 5.932   -48.611 1.00 9.62  ? 611  TRP   B CG  1 
ATOM   4210 C  CD1 . TRP   B 1 170 ? -14.796 5.026   -48.287 1.00 13.51 ? 611  TRP   B CD1 1 
ATOM   4211 C  CD2 . TRP   B 1 170 ? -16.400 6.290   -47.361 1.00 10.65 ? 611  TRP   B CD2 1 
ATOM   4212 N  NE1 . TRP   B 1 170 ? -14.786 4.791   -46.915 1.00 11.92 ? 611  TRP   B NE1 1 
ATOM   4213 C  CE2 . TRP   B 1 170 ? -15.746 5.569   -46.320 1.00 10.90 ? 611  TRP   B CE2 1 
ATOM   4214 C  CE3 . TRP   B 1 170 ? -17.438 7.164   -47.015 1.00 12.36 ? 611  TRP   B CE3 1 
ATOM   4215 C  CZ2 . TRP   B 1 170 ? -16.126 5.684   -44.963 1.00 14.04 ? 611  TRP   B CZ2 1 
ATOM   4216 C  CZ3 . TRP   B 1 170 ? -17.809 7.283   -45.678 1.00 14.88 ? 611  TRP   B CZ3 1 
ATOM   4217 C  CH2 . TRP   B 1 170 ? -17.163 6.542   -44.666 1.00 13.49 ? 611  TRP   B CH2 1 
ATOM   4218 N  N   . ASP   B 1 171 ? -14.705 3.521   -51.594 1.00 12.34 ? 612  ASP   B N   1 
ATOM   4219 C  CA  . ASP   B 1 171 ? -13.505 2.851   -52.090 1.00 12.07 ? 612  ASP   B CA  1 
ATOM   4220 C  C   . ASP   B 1 171 ? -13.015 3.623   -53.309 1.00 12.44 ? 612  ASP   B C   1 
ATOM   4221 O  O   . ASP   B 1 171 ? -13.817 4.201   -54.049 1.00 12.22 ? 612  ASP   B O   1 
ATOM   4222 C  CB  . ASP   B 1 171 ? -13.900 1.404   -52.433 1.00 12.73 ? 612  ASP   B CB  1 
ATOM   4223 C  CG  . ASP   B 1 171 ? -12.739 0.526   -52.848 1.00 12.29 ? 612  ASP   B CG  1 
ATOM   4224 O  OD1 . ASP   B 1 171 ? -12.203 0.699   -53.935 1.00 11.44 ? 612  ASP   B OD1 1 
ATOM   4225 O  OD2 . ASP   B 1 171 ? -12.328 -0.391  -52.105 1.00 13.35 ? 612  ASP   B OD2 1 
ATOM   4226 N  N   . VAL   B 1 172 ? -11.693 3.688   -53.506 1.00 10.96 ? 613  VAL   B N   1 
ATOM   4227 C  CA  . VAL   B 1 172 ? -11.157 4.455   -54.629 1.00 9.93  ? 613  VAL   B CA  1 
ATOM   4228 C  C   . VAL   B 1 172 ? -11.567 3.862   -55.976 1.00 11.61 ? 613  VAL   B C   1 
ATOM   4229 O  O   . VAL   B 1 172 ? -11.511 4.542   -56.999 1.00 12.55 ? 613  VAL   B O   1 
ATOM   4230 C  CB  . VAL   B 1 172 ? -9.621  4.572   -54.514 1.00 11.63 ? 613  VAL   B CB  1 
ATOM   4231 C  CG1 . VAL   B 1 172 ? -8.963  3.291   -54.985 1.00 12.59 ? 613  VAL   B CG1 1 
ATOM   4232 C  CG2 . VAL   B 1 172 ? -9.115  5.777   -55.315 1.00 15.34 ? 613  VAL   B CG2 1 
ATOM   4233 N  N   . HIS   B 1 173 ? -12.022 2.612   -55.956 1.00 12.93 ? 614  HIS   B N   1 
ATOM   4234 C  CA  . HIS   B 1 173 ? -12.415 1.898   -57.193 1.00 18.44 ? 614  HIS   B CA  1 
ATOM   4235 C  C   . HIS   B 1 173 ? -13.931 1.920   -57.351 1.00 11.67 ? 614  HIS   B C   1 
ATOM   4236 O  O   . HIS   B 1 173 ? -14.709 1.921   -56.409 1.00 12.53 ? 614  HIS   B O   1 
ATOM   4237 C  CB  . HIS   B 1 173 ? -11.923 0.440   -57.194 1.00 51.61 ? 614  HIS   B CB  1 
ATOM   4238 C  CG  . HIS   B 1 173 ? -10.449 0.319   -57.050 1.00 27.24 ? 614  HIS   B CG  1 
ATOM   4239 N  ND1 . HIS   B 1 173 ? -9.791  -0.016  -55.886 1.00 32.47 ? 614  HIS   B ND1 1 
ATOM   4240 C  CD2 . HIS   B 1 173 ? -9.506  0.506   -57.972 1.00 35.09 ? 614  HIS   B CD2 1 
ATOM   4241 C  CE1 . HIS   B 1 173 ? -8.489  -0.022  -56.122 1.00 24.10 ? 614  HIS   B CE1 1 
ATOM   4242 N  NE2 . HIS   B 1 173 ? -8.298  0.295   -57.377 1.00 18.53 ? 614  HIS   B NE2 1 
ATOM   4243 N  N   . HIS   B 1 174 ? -14.301 1.889   -58.614 1.00 13.29 ? 615  HIS   B N   1 
ATOM   4244 C  CA  . HIS   B 1 174 ? -15.737 1.847   -58.912 1.00 14.87 ? 615  HIS   B CA  1 
ATOM   4245 C  C   . HIS   B 1 174 ? -16.294 0.472   -58.539 1.00 13.09 ? 615  HIS   B C   1 
ATOM   4246 O  O   . HIS   B 1 174 ? -15.695 -0.547  -58.883 1.00 13.92 ? 615  HIS   B O   1 
ATOM   4247 C  CB  . HIS   B 1 174 ? -15.987 2.080   -60.403 1.00 14.34 ? 615  HIS   B CB  1 
ATOM   4248 C  CG  . HIS   B 1 174 ? -17.438 2.071   -60.778 1.00 13.26 ? 615  HIS   B CG  1 
ATOM   4249 N  ND1 . HIS   B 1 174 ? -17.963 1.232   -61.745 1.00 15.91 ? 615  HIS   B ND1 1 
ATOM   4250 C  CD2 . HIS   B 1 174 ? -18.465 2.831   -60.341 1.00 15.66 ? 615  HIS   B CD2 1 
ATOM   4251 C  CE1 . HIS   B 1 174 ? -19.255 1.475   -61.875 1.00 14.07 ? 615  HIS   B CE1 1 
ATOM   4252 N  NE2 . HIS   B 1 174 ? -19.586 2.442   -61.036 1.00 14.78 ? 615  HIS   B NE2 1 
ATOM   4253 N  N   . GLY   B 1 175 ? -17.426 0.434   -57.830 1.00 11.70 ? 616  GLY   B N   1 
ATOM   4254 C  CA  . GLY   B 1 175 ? -18.055 -0.839  -57.497 1.00 13.12 ? 616  GLY   B CA  1 
ATOM   4255 C  C   . GLY   B 1 175 ? -18.904 -1.340  -58.657 1.00 14.81 ? 616  GLY   B C   1 
ATOM   4256 O  O   . GLY   B 1 175 ? -20.143 -1.260  -58.612 1.00 14.45 ? 616  GLY   B O   1 
ATOM   4257 N  N   . ASN   B 1 176 ? -18.243 -1.835  -59.715 1.00 13.43 ? 617  ASN   B N   1 
ATOM   4258 C  CA  . ASN   B 1 176 ? -18.963 -2.260  -60.920 1.00 14.35 ? 617  ASN   B CA  1 
ATOM   4259 C  C   . ASN   B 1 176 ? -20.034 -3.286  -60.589 1.00 14.45 ? 617  ASN   B C   1 
ATOM   4260 O  O   . ASN   B 1 176 ? -21.121 -3.255  -61.166 1.00 14.15 ? 617  ASN   B O   1 
ATOM   4261 C  CB  . ASN   B 1 176 ? -17.992 -2.848  -61.934 1.00 15.15 ? 617  ASN   B CB  1 
ATOM   4262 C  CG  . ASN   B 1 176 ? -17.174 -3.968  -61.353 1.00 16.05 ? 617  ASN   B CG  1 
ATOM   4263 O  OD1 . ASN   B 1 176 ? -16.293 -3.709  -60.569 1.00 15.10 ? 617  ASN   B OD1 1 
ATOM   4264 N  ND2 . ASN   B 1 176 ? -17.496 -5.222  -61.684 1.00 17.48 ? 617  ASN   B ND2 1 
ATOM   4265 N  N   . GLY   B 1 177 ? -19.754 -4.195  -59.659 1.00 12.74 ? 618  GLY   B N   1 
ATOM   4266 C  CA  . GLY   B 1 177 ? -20.723 -5.222  -59.334 1.00 14.66 ? 618  GLY   B CA  1 
ATOM   4267 C  C   . GLY   B 1 177 ? -21.973 -4.644  -58.705 1.00 15.45 ? 618  GLY   B C   1 
ATOM   4268 O  O   . GLY   B 1 177 ? -23.101 -4.999  -59.082 1.00 15.19 ? 618  GLY   B O   1 
ATOM   4269 N  N   . THR   B 1 178 ? -21.797 -3.721  -57.751 1.00 12.85 ? 619  THR   B N   1 
ATOM   4270 C  CA  . THR   B 1 178 ? -22.950 -3.126  -57.098 1.00 14.06 ? 619  THR   B CA  1 
ATOM   4271 C  C   . THR   B 1 178 ? -23.754 -2.295  -58.080 1.00 13.97 ? 619  THR   B C   1 
ATOM   4272 O  O   . THR   B 1 178 ? -24.995 -2.354  -58.086 1.00 14.19 ? 619  THR   B O   1 
ATOM   4273 C  CB  . THR   B 1 178 ? -22.463 -2.249  -55.954 1.00 14.68 ? 619  THR   B CB  1 
ATOM   4274 O  OG1 . THR   B 1 178 ? -21.505 -2.989  -55.198 1.00 12.97 ? 619  THR   B OG1 1 
ATOM   4275 C  CG2 . THR   B 1 178 ? -23.615 -1.851  -55.060 1.00 12.76 ? 619  THR   B CG2 1 
ATOM   4276 N  N   . GLN   B 1 179 ? -23.078 -1.527  -58.938 1.00 13.86 ? 620  GLN   B N   1 
ATOM   4277 C  CA  . GLN   B 1 179 ? -23.796 -0.765  -59.957 1.00 17.53 ? 620  GLN   B CA  1 
ATOM   4278 C  C   . GLN   B 1 179 ? -24.672 -1.689  -60.792 1.00 16.25 ? 620  GLN   B C   1 
ATOM   4279 O  O   . GLN   B 1 179 ? -25.872 -1.435  -60.982 1.00 16.82 ? 620  GLN   B O   1 
ATOM   4280 C  CB  . GLN   B 1 179 ? -22.811 -0.003  -60.851 1.00 15.08 ? 620  GLN   B CB  1 
ATOM   4281 C  CG  . GLN   B 1 179 ? -23.502 0.533   -62.108 1.00 16.36 ? 620  GLN   B CG  1 
ATOM   4282 C  CD  . GLN   B 1 179 ? -22.674 1.574   -62.844 1.00 22.87 ? 620  GLN   B CD  1 
ATOM   4283 O  OE1 . GLN   B 1 179 ? -22.129 2.499   -62.229 1.00 16.83 ? 620  GLN   B OE1 1 
ATOM   4284 N  NE2 . GLN   B 1 179 ? -22.588 1.441   -64.172 1.00 20.30 ? 620  GLN   B NE2 1 
ATOM   4285 N  N   . HIS   B 1 180 ? -24.086 -2.771  -61.302 1.00 14.81 ? 621  HIS   B N   1 
ATOM   4286 C  CA  . HIS   B 1 180 ? -24.818 -3.641  -62.222 1.00 15.10 ? 621  HIS   B CA  1 
ATOM   4287 C  C   . HIS   B 1 180 ? -25.965 -4.347  -61.518 1.00 21.02 ? 621  HIS   B C   1 
ATOM   4288 O  O   . HIS   B 1 180 ? -27.063 -4.463  -62.078 1.00 16.41 ? 621  HIS   B O   1 
ATOM   4289 C  CB  . HIS   B 1 180 ? -23.857 -4.634  -62.871 1.00 15.86 ? 621  HIS   B CB  1 
ATOM   4290 C  CG  . HIS   B 1 180 ? -22.863 -3.994  -63.796 1.00 18.21 ? 621  HIS   B CG  1 
ATOM   4291 N  ND1 . HIS   B 1 180 ? -21.581 -4.476  -63.955 1.00 18.78 ? 621  HIS   B ND1 1 
ATOM   4292 C  CD2 . HIS   B 1 180 ? -22.960 -2.913  -64.610 1.00 17.07 ? 621  HIS   B CD2 1 
ATOM   4293 C  CE1 . HIS   B 1 180 ? -20.932 -3.725  -64.828 1.00 22.66 ? 621  HIS   B CE1 1 
ATOM   4294 N  NE2 . HIS   B 1 180 ? -21.744 -2.765  -65.237 1.00 19.93 ? 621  HIS   B NE2 1 
ATOM   4295 N  N   . ILE   B 1 181 ? -25.746 -4.797  -60.279 1.00 15.08 ? 622  ILE   B N   1 
ATOM   4296 C  CA  . ILE   B 1 181 ? -26.794 -5.499  -59.545 1.00 15.18 ? 622  ILE   B CA  1 
ATOM   4297 C  C   . ILE   B 1 181 ? -28.023 -4.617  -59.374 1.00 18.28 ? 622  ILE   B C   1 
ATOM   4298 O  O   . ILE   B 1 181 ? -29.163 -5.080  -59.514 1.00 17.29 ? 622  ILE   B O   1 
ATOM   4299 C  CB  . ILE   B 1 181 ? -26.238 -6.012  -58.198 1.00 13.48 ? 622  ILE   B CB  1 
ATOM   4300 C  CG1 . ILE   B 1 181 ? -25.327 -7.219  -58.437 1.00 15.52 ? 622  ILE   B CG1 1 
ATOM   4301 C  CG2 . ILE   B 1 181 ? -27.385 -6.369  -57.231 1.00 15.61 ? 622  ILE   B CG2 1 
ATOM   4302 C  CD1 . ILE   B 1 181 ? -24.467 -7.616  -57.222 1.00 16.00 ? 622  ILE   B CD1 1 
ATOM   4303 N  N   . PHE   B 1 182 ? -27.827 -3.332  -59.099 1.00 16.71 ? 623  PHE   B N   1 
ATOM   4304 C  CA  . PHE   B 1 182 ? -28.952 -2.444  -58.830 1.00 15.79 ? 623  PHE   B CA  1 
ATOM   4305 C  C   . PHE   B 1 182 ? -29.268 -1.500  -59.977 1.00 15.97 ? 623  PHE   B C   1 
ATOM   4306 O  O   . PHE   B 1 182 ? -30.071 -0.578  -59.789 1.00 16.25 ? 623  PHE   B O   1 
ATOM   4307 C  CB  . PHE   B 1 182 ? -28.735 -1.674  -57.522 1.00 14.79 ? 623  PHE   B CB  1 
ATOM   4308 C  CG  . PHE   B 1 182 ? -28.554 -2.567  -56.343 1.00 15.22 ? 623  PHE   B CG  1 
ATOM   4309 C  CD1 . PHE   B 1 182 ? -29.609 -3.329  -55.868 1.00 15.30 ? 623  PHE   B CD1 1 
ATOM   4310 C  CD2 . PHE   B 1 182 ? -27.326 -2.664  -55.721 1.00 15.86 ? 623  PHE   B CD2 1 
ATOM   4311 C  CE1 . PHE   B 1 182 ? -29.449 -4.165  -54.769 1.00 16.09 ? 623  PHE   B CE1 1 
ATOM   4312 C  CE2 . PHE   B 1 182 ? -27.152 -3.487  -54.643 1.00 14.82 ? 623  PHE   B CE2 1 
ATOM   4313 C  CZ  . PHE   B 1 182 ? -28.190 -4.239  -54.150 1.00 13.92 ? 623  PHE   B CZ  1 
ATOM   4314 N  N   . GLU   B 1 183 ? -28.680 -1.717  -61.162 1.00 13.67 ? 624  GLU   B N   1 
ATOM   4315 C  CA  . GLU   B 1 183 ? -28.777 -0.717  -62.223 1.00 16.77 ? 624  GLU   B CA  1 
ATOM   4316 C  C   . GLU   B 1 183 ? -30.221 -0.427  -62.616 1.00 15.29 ? 624  GLU   B C   1 
ATOM   4317 O  O   . GLU   B 1 183 ? -30.531 0.705   -63.000 1.00 16.18 ? 624  GLU   B O   1 
ATOM   4318 C  CB  . GLU   B 1 183 ? -27.980 -1.161  -63.444 1.00 17.40 ? 624  GLU   B CB  1 
ATOM   4319 C  CG  . GLU   B 1 183 ? -27.659 -0.064  -64.415 1.00 23.39 ? 624  GLU   B CG  1 
ATOM   4320 C  CD  . GLU   B 1 183 ? -26.520 -0.461  -65.335 1.00 32.62 ? 624  GLU   B CD  1 
ATOM   4321 O  OE1 . GLU   B 1 183 ? -26.364 -1.684  -65.572 1.00 23.55 ? 624  GLU   B OE1 1 
ATOM   4322 O  OE2 . GLU   B 1 183 ? -25.790 0.434   -65.814 1.00 38.22 ? 624  GLU   B OE2 1 
ATOM   4323 N  N   . GLU   B 1 184 ? -31.106 -1.422  -62.520 1.00 17.35 ? 625  GLU   B N   1 
ATOM   4324 C  CA  . GLU   B 1 184 ? -32.517 -1.254  -62.867 1.00 17.86 ? 625  GLU   B CA  1 
ATOM   4325 C  C   . GLU   B 1 184 ? -33.406 -1.154  -61.639 1.00 18.76 ? 625  GLU   B C   1 
ATOM   4326 O  O   . GLU   B 1 184 ? -34.605 -1.461  -61.712 1.00 22.66 ? 625  GLU   B O   1 
ATOM   4327 C  CB  . GLU   B 1 184 ? -32.991 -2.399  -63.762 1.00 22.37 ? 625  GLU   B CB  1 
ATOM   4328 C  CG  . GLU   B 1 184 ? -32.391 -2.398  -65.164 1.00 23.40 ? 625  GLU   B CG  1 
ATOM   4329 C  CD  . GLU   B 1 184 ? -32.796 -3.630  -65.954 1.00 30.59 ? 625  GLU   B CD  1 
ATOM   4330 O  OE1 . GLU   B 1 184 ? -32.575 -4.759  -65.471 1.00 47.04 ? 625  GLU   B OE1 1 
ATOM   4331 O  OE2 . GLU   B 1 184 ? -33.365 -3.465  -67.046 1.00 35.63 ? 625  GLU   B OE2 1 
ATOM   4332 N  N   . ASP   B 1 185 ? -32.848 -0.719  -60.509 1.00 17.90 ? 626  ASP   B N   1 
ATOM   4333 C  CA  . ASP   B 1 185 ? -33.541 -0.764  -59.232 1.00 18.96 ? 626  ASP   B CA  1 
ATOM   4334 C  C   . ASP   B 1 185 ? -33.575 0.633   -58.630 1.00 22.42 ? 626  ASP   B C   1 
ATOM   4335 O  O   . ASP   B 1 185 ? -32.531 1.269   -58.454 1.00 23.59 ? 626  ASP   B O   1 
ATOM   4336 C  CB  . ASP   B 1 185 ? -32.855 -1.756  -58.276 1.00 21.00 ? 626  ASP   B CB  1 
ATOM   4337 C  CG  . ASP   B 1 185 ? -33.728 -2.126  -57.069 1.00 23.75 ? 626  ASP   B CG  1 
ATOM   4338 O  OD1 . ASP   B 1 185 ? -34.753 -1.456  -56.813 0.72 24.51 ? 626  ASP   B OD1 1 
ATOM   4339 O  OD2 . ASP   B 1 185 ? -33.380 -3.107  -56.389 0.57 26.06 ? 626  ASP   B OD2 1 
ATOM   4340 N  N   . ASP   B 1 186 ? -34.777 1.111   -58.323 1.00 22.12 ? 627  ASP   B N   1 
ATOM   4341 C  CA  . ASP   B 1 186 ? -34.953 2.394   -57.664 1.00 19.80 ? 627  ASP   B CA  1 
ATOM   4342 C  C   . ASP   B 1 186 ? -35.046 2.281   -56.145 1.00 17.07 ? 627  ASP   B C   1 
ATOM   4343 O  O   . ASP   B 1 186 ? -35.116 3.321   -55.472 1.00 22.12 ? 627  ASP   B O   1 
ATOM   4344 C  CB  . ASP   B 1 186 ? -36.210 3.102   -58.198 1.00 29.19 ? 627  ASP   B CB  1 
ATOM   4345 C  CG  . ASP   B 1 186 ? -37.487 2.292   -57.980 1.00 20.20 ? 627  ASP   B CG  1 
ATOM   4346 O  OD1 . ASP   B 1 186 ? -37.438 1.069   -57.716 1.00 27.70 ? 627  ASP   B OD1 1 
ATOM   4347 O  OD2 . ASP   B 1 186 ? -38.573 2.895   -58.095 1.00 44.57 ? 627  ASP   B OD2 1 
ATOM   4348 N  N   . SER   B 1 187 ? -35.091 1.063   -55.596 1.00 16.07 ? 628  SER   B N   1 
ATOM   4349 C  CA  . SER   B 1 187 ? -35.141 0.895   -54.145 1.00 19.22 ? 628  SER   B CA  1 
ATOM   4350 C  C   . SER   B 1 187 ? -33.760 0.944   -53.492 1.00 19.58 ? 628  SER   B C   1 
ATOM   4351 O  O   . SER   B 1 187 ? -33.676 1.060   -52.263 1.00 19.17 ? 628  SER   B O   1 
ATOM   4352 C  CB  . SER   B 1 187 ? -35.810 -0.427  -53.764 1.00 20.99 ? 628  SER   B CB  1 
ATOM   4353 O  OG  . SER   B 1 187 ? -34.998 -1.553  -54.086 1.00 21.08 ? 628  SER   B OG  1 
ATOM   4354 N  N   . VAL   B 1 188 ? -32.694 0.843   -54.287 1.00 16.33 ? 629  VAL   B N   1 
ATOM   4355 C  CA  . VAL   B 1 188 ? -31.307 0.900   -53.827 1.00 15.68 ? 629  VAL   B CA  1 
ATOM   4356 C  C   . VAL   B 1 188 ? -30.613 1.980   -54.640 1.00 18.94 ? 629  VAL   B C   1 
ATOM   4357 O  O   . VAL   B 1 188 ? -30.346 1.794   -55.837 1.00 19.01 ? 629  VAL   B O   1 
ATOM   4358 C  CB  . VAL   B 1 188 ? -30.607 -0.449  -54.000 1.00 14.52 ? 629  VAL   B CB  1 
ATOM   4359 C  CG1 . VAL   B 1 188 ? -29.147 -0.362  -53.468 1.00 16.22 ? 629  VAL   B CG1 1 
ATOM   4360 C  CG2 . VAL   B 1 188 ? -31.396 -1.549  -53.294 1.00 17.33 ? 629  VAL   B CG2 1 
ATOM   4361 N  N   . LEU   B 1 189 ? -30.310 3.106   -53.998 1.00 15.48 ? 630  LEU   B N   1 
ATOM   4362 C  CA  . LEU   B 1 189 ? -29.575 4.195   -54.608 1.00 14.86 ? 630  LEU   B CA  1 
ATOM   4363 C  C   . LEU   B 1 189 ? -28.089 3.898   -54.424 1.00 17.29 ? 630  LEU   B C   1 
ATOM   4364 O  O   . LEU   B 1 189 ? -27.626 3.724   -53.285 1.00 17.33 ? 630  LEU   B O   1 
ATOM   4365 C  CB  . LEU   B 1 189 ? -29.922 5.500   -53.903 1.00 15.74 ? 630  LEU   B CB  1 
ATOM   4366 C  CG  . LEU   B 1 189 ? -29.121 6.753   -54.212 1.00 17.46 ? 630  LEU   B CG  1 
ATOM   4367 C  CD1 . LEU   B 1 189 ? -29.149 7.035   -55.705 1.00 18.27 ? 630  LEU   B CD1 1 
ATOM   4368 C  CD2 . LEU   B 1 189 ? -29.635 7.958   -53.425 1.00 18.84 ? 630  LEU   B CD2 1 
ATOM   4369 N  N   . TYR   B 1 190 ? -27.351 3.806   -55.530 1.00 13.84 ? 631  TYR   B N   1 
ATOM   4370 C  CA  . TYR   B 1 190 ? -25.917 3.538   -55.481 1.00 14.02 ? 631  TYR   B CA  1 
ATOM   4371 C  C   . TYR   B 1 190 ? -25.189 4.827   -55.817 1.00 15.83 ? 631  TYR   B C   1 
ATOM   4372 O  O   . TYR   B 1 190 ? -25.414 5.410   -56.884 1.00 16.16 ? 631  TYR   B O   1 
ATOM   4373 C  CB  . TYR   B 1 190 ? -25.542 2.440   -56.480 1.00 13.74 ? 631  TYR   B CB  1 
ATOM   4374 C  CG  . TYR   B 1 190 ? -24.063 2.140   -56.492 1.00 14.48 ? 631  TYR   B CG  1 
ATOM   4375 C  CD1 . TYR   B 1 190 ? -23.433 1.622   -55.365 1.00 12.94 ? 631  TYR   B CD1 1 
ATOM   4376 C  CD2 . TYR   B 1 190 ? -23.294 2.391   -57.615 1.00 13.26 ? 631  TYR   B CD2 1 
ATOM   4377 C  CE1 . TYR   B 1 190 ? -22.076 1.359   -55.345 1.00 14.10 ? 631  TYR   B CE1 1 
ATOM   4378 C  CE2 . TYR   B 1 190 ? -21.928 2.134   -57.626 1.00 14.16 ? 631  TYR   B CE2 1 
ATOM   4379 C  CZ  . TYR   B 1 190 ? -21.329 1.617   -56.476 1.00 14.06 ? 631  TYR   B CZ  1 
ATOM   4380 O  OH  . TYR   B 1 190 ? -19.984 1.378   -56.531 1.00 13.50 ? 631  TYR   B OH  1 
ATOM   4381 N  N   . ILE   B 1 191 ? -24.326 5.279   -54.909 1.00 16.67 ? 632  ILE   B N   1 
ATOM   4382 C  CA  . ILE   B 1 191 ? -23.507 6.466   -55.135 1.00 14.74 ? 632  ILE   B CA  1 
ATOM   4383 C  C   . ILE   B 1 191 ? -22.053 6.044   -54.949 1.00 13.88 ? 632  ILE   B C   1 
ATOM   4384 O  O   . ILE   B 1 191 ? -21.662 5.664   -53.837 1.00 14.71 ? 632  ILE   B O   1 
ATOM   4385 C  CB  . ILE   B 1 191 ? -23.872 7.613   -54.170 1.00 17.41 ? 632  ILE   B CB  1 
ATOM   4386 C  CG1 . ILE   B 1 191 ? -25.378 7.940   -54.233 1.00 15.27 ? 632  ILE   B CG1 1 
ATOM   4387 C  CG2 . ILE   B 1 191 ? -23.050 8.843   -54.496 1.00 18.39 ? 632  ILE   B CG2 1 
ATOM   4388 C  CD1 . ILE   B 1 191 ? -25.778 9.173   -53.424 1.00 17.02 ? 632  ILE   B CD1 1 
ATOM   4389 N  N   . SER   B 1 192 ? -21.259 6.122   -56.017 1.00 12.78 ? 633  SER   B N   1 
ATOM   4390 C  CA  . SER   B 1 192 ? -19.842 5.780   -55.960 1.00 12.87 ? 633  SER   B CA  1 
ATOM   4391 C  C   . SER   B 1 192 ? -18.998 7.004   -56.275 1.00 14.85 ? 633  SER   B C   1 
ATOM   4392 O  O   . SER   B 1 192 ? -19.272 7.725   -57.237 1.00 15.11 ? 633  SER   B O   1 
ATOM   4393 C  CB  . SER   B 1 192 ? -19.511 4.694   -56.988 1.00 13.69 ? 633  SER   B CB  1 
ATOM   4394 O  OG  . SER   B 1 192 ? -18.145 4.349   -56.928 1.00 13.70 ? 633  SER   B OG  1 
ATOM   4395 N  N   . LEU   B 1 193 ? -17.958 7.226   -55.485 1.00 13.08 ? 634  LEU   B N   1 
ATOM   4396 C  CA  . LEU   B 1 193 ? -16.881 8.131   -55.840 1.00 13.31 ? 634  LEU   B CA  1 
ATOM   4397 C  C   . LEU   B 1 193 ? -15.670 7.269   -56.163 1.00 13.28 ? 634  LEU   B C   1 
ATOM   4398 O  O   . LEU   B 1 193 ? -15.396 6.291   -55.459 1.00 14.27 ? 634  LEU   B O   1 
ATOM   4399 C  CB  . LEU   B 1 193 ? -16.540 9.076   -54.673 1.00 15.50 ? 634  LEU   B CB  1 
ATOM   4400 C  CG  . LEU   B 1 193 ? -17.744 9.777   -54.026 1.00 15.36 ? 634  LEU   B CG  1 
ATOM   4401 C  CD1 . LEU   B 1 193 ? -18.260 9.022   -52.830 1.00 15.56 ? 634  LEU   B CD1 1 
ATOM   4402 C  CD2 . LEU   B 1 193 ? -17.364 11.210  -53.637 1.00 18.19 ? 634  LEU   B CD2 1 
ATOM   4403 N  N   . HIS   B 1 194 ? -14.942 7.603   -57.220 1.00 14.12 ? 635  HIS   B N   1 
ATOM   4404 C  CA  . HIS   B 1 194 ? -13.881 6.693   -57.633 1.00 13.67 ? 635  HIS   B CA  1 
ATOM   4405 C  C   . HIS   B 1 194 ? -12.913 7.372   -58.583 1.00 15.33 ? 635  HIS   B C   1 
ATOM   4406 O  O   . HIS   B 1 194 ? -13.287 8.233   -59.392 1.00 17.32 ? 635  HIS   B O   1 
ATOM   4407 C  CB  . HIS   B 1 194 ? -14.439 5.425   -58.307 1.00 14.39 ? 635  HIS   B CB  1 
ATOM   4408 C  CG  . HIS   B 1 194 ? -15.533 5.712   -59.279 1.00 14.22 ? 635  HIS   B CG  1 
ATOM   4409 N  ND1 . HIS   B 1 194 ? -16.850 5.800   -58.886 1.00 13.10 ? 635  HIS   B ND1 1 
ATOM   4410 C  CD2 . HIS   B 1 194 ? -15.507 5.958   -60.611 1.00 14.54 ? 635  HIS   B CD2 1 
ATOM   4411 C  CE1 . HIS   B 1 194 ? -17.596 6.074   -59.948 1.00 14.43 ? 635  HIS   B CE1 1 
ATOM   4412 N  NE2 . HIS   B 1 194 ? -16.804 6.178   -61.003 1.00 14.95 ? 635  HIS   B NE2 1 
ATOM   4413 N  N   . ARG   B 1 195 ? -11.661 6.947   -58.491 1.00 14.26 ? 636  ARG   B N   1 
ATOM   4414 C  CA  . ARG   B 1 195 ? -10.682 7.321   -59.494 1.00 14.81 ? 636  ARG   B CA  1 
ATOM   4415 C  C   . ARG   B 1 195 ? -11.053 6.643   -60.802 1.00 15.13 ? 636  ARG   B C   1 
ATOM   4416 O  O   . ARG   B 1 195 ? -11.308 5.433   -60.842 1.00 15.07 ? 636  ARG   B O   1 
ATOM   4417 C  CB  . ARG   B 1 195 ? -9.285  6.889   -59.051 1.00 14.39 ? 636  ARG   B CB  1 
ATOM   4418 C  CG  . ARG   B 1 195 ? -8.205  7.521   -59.890 1.00 14.72 ? 636  ARG   B CG  1 
ATOM   4419 C  CD  . ARG   B 1 195 ? -6.838  7.243   -59.336 1.00 16.47 ? 636  ARG   B CD  1 
ATOM   4420 N  NE  . ARG   B 1 195 ? -5.798  7.782   -60.211 1.00 18.90 ? 636  ARG   B NE  1 
ATOM   4421 C  CZ  . ARG   B 1 195 ? -4.494  7.609   -60.014 1.00 23.65 ? 636  ARG   B CZ  1 
ATOM   4422 N  NH1 . ARG   B 1 195 ? -4.064  6.897   -58.978 1.00 21.29 ? 636  ARG   B NH1 1 
ATOM   4423 N  NH2 . ARG   B 1 195 ? -3.610  8.135   -60.863 1.00 24.87 ? 636  ARG   B NH2 1 
ATOM   4424 N  N   . TYR   B 1 196 ? -11.099 7.434   -61.871 1.00 15.47 ? 637  TYR   B N   1 
ATOM   4425 C  CA  . TYR   B 1 196 ? -11.584 6.986   -63.167 1.00 17.96 ? 637  TYR   B CA  1 
ATOM   4426 C  C   . TYR   B 1 196 ? -10.548 7.161   -64.265 1.00 17.83 ? 637  TYR   B C   1 
ATOM   4427 O  O   . TYR   B 1 196 ? -10.290 6.215   -65.022 1.00 18.80 ? 637  TYR   B O   1 
ATOM   4428 C  CB  . TYR   B 1 196 ? -12.867 7.749   -63.517 1.00 17.61 ? 637  TYR   B CB  1 
ATOM   4429 C  CG  . TYR   B 1 196 ? -13.488 7.373   -64.848 1.00 18.14 ? 637  TYR   B CG  1 
ATOM   4430 C  CD1 . TYR   B 1 196 ? -13.896 6.068   -65.104 1.00 18.91 ? 637  TYR   B CD1 1 
ATOM   4431 C  CD2 . TYR   B 1 196 ? -13.690 8.333   -65.844 1.00 19.65 ? 637  TYR   B CD2 1 
ATOM   4432 C  CE1 . TYR   B 1 196 ? -14.473 5.716   -66.331 1.00 18.29 ? 637  TYR   B CE1 1 
ATOM   4433 C  CE2 . TYR   B 1 196 ? -14.270 7.990   -67.060 1.00 17.78 ? 637  TYR   B CE2 1 
ATOM   4434 C  CZ  . TYR   B 1 196 ? -14.652 6.679   -67.299 1.00 19.64 ? 637  TYR   B CZ  1 
ATOM   4435 O  OH  . TYR   B 1 196 ? -15.216 6.330   -68.518 1.00 21.69 ? 637  TYR   B OH  1 
ATOM   4436 N  N   . GLU   B 1 197 ? -9.931  8.342   -64.362 1.00 18.00 ? 638  GLU   B N   1 
ATOM   4437 C  CA  . GLU   B 1 197 ? -8.885  8.618   -65.354 1.00 20.06 ? 638  GLU   B CA  1 
ATOM   4438 C  C   . GLU   B 1 197 ? -9.337  8.266   -66.769 1.00 23.34 ? 638  GLU   B C   1 
ATOM   4439 O  O   . GLU   B 1 197 ? -8.634  7.592   -67.519 1.00 22.11 ? 638  GLU   B O   1 
ATOM   4440 C  CB  . GLU   B 1 197 ? -7.566  7.926   -65.011 1.00 23.06 ? 638  GLU   B CB  1 
ATOM   4441 C  CG  . GLU   B 1 197 ? -7.082  8.133   -63.573 1.00 17.55 ? 638  GLU   B CG  1 
ATOM   4442 C  CD  . GLU   B 1 197 ? -6.721  9.579   -63.251 1.00 40.89 ? 638  GLU   B CD  1 
ATOM   4443 O  OE1 . GLU   B 1 197 ? -6.776  10.452  -64.145 1.00 26.81 ? 638  GLU   B OE1 1 
ATOM   4444 O  OE2 . GLU   B 1 197 ? -6.382  9.847   -62.082 1.00 24.29 ? 638  GLU   B OE2 1 
ATOM   4445 N  N   . ASP   B 1 198 ? -10.540 8.710   -67.123 1.00 19.40 ? 639  ASP   B N   1 
ATOM   4446 C  CA  . ASP   B 1 198 ? -11.070 8.510   -68.475 1.00 20.75 ? 639  ASP   B CA  1 
ATOM   4447 C  C   . ASP   B 1 198 ? -11.105 7.029   -68.849 1.00 24.50 ? 639  ASP   B C   1 
ATOM   4448 O  O   . ASP   B 1 198 ? -10.892 6.649   -70.001 1.00 26.66 ? 639  ASP   B O   1 
ATOM   4449 C  CB  . ASP   B 1 198 ? -10.311 9.355   -69.499 1.00 23.89 ? 639  ASP   B CB  1 
ATOM   4450 C  CG  . ASP   B 1 198 ? -10.467 10.841  -69.240 1.00 42.56 ? 639  ASP   B CG  1 
ATOM   4451 O  OD1 . ASP   B 1 198 ? -11.592 11.263  -68.893 1.00 45.64 ? 639  ASP   B OD1 1 
ATOM   4452 O  OD2 . ASP   B 1 198 ? -9.471  11.584  -69.368 1.00 56.54 ? 639  ASP   B OD2 1 
ATOM   4453 N  N   . GLY   B 1 199 ? -11.385 6.182   -67.858 1.00 19.17 ? 640  GLY   B N   1 
ATOM   4454 C  CA  . GLY   B 1 199 ? -11.493 4.754   -68.077 1.00 22.83 ? 640  GLY   B CA  1 
ATOM   4455 C  C   . GLY   B 1 199 ? -10.210 3.967   -67.932 1.00 20.22 ? 640  GLY   B C   1 
ATOM   4456 O  O   . GLY   B 1 199 ? -10.235 2.740   -68.118 1.00 26.67 ? 640  GLY   B O   1 
ATOM   4457 N  N   . ALA   B 1 200 ? -9.098  4.617   -67.611 1.00 22.00 ? 641  ALA   B N   1 
ATOM   4458 C  CA  . ALA   B 1 200 ? -7.805  3.951   -67.553 1.00 24.46 ? 641  ALA   B CA  1 
ATOM   4459 C  C   . ALA   B 1 200 ? -7.539  3.274   -66.217 1.00 34.05 ? 641  ALA   B C   1 
ATOM   4460 O  O   . ALA   B 1 200 ? -6.623  2.451   -66.125 1.00 52.44 ? 641  ALA   B O   1 
ATOM   4461 C  CB  . ALA   B 1 200 ? -6.674  4.949   -67.817 1.00 22.81 ? 641  ALA   B CB  1 
ATOM   4462 N  N   . PHE   B 1 201 ? -8.307  3.605   -65.190 1.00 19.92 ? 642  PHE   B N   1 
ATOM   4463 C  CA  . PHE   B 1 201 ? -8.100  3.081   -63.849 1.00 25.25 ? 642  PHE   B CA  1 
ATOM   4464 C  C   . PHE   B 1 201 ? -9.019  1.889   -63.607 1.00 17.44 ? 642  PHE   B C   1 
ATOM   4465 O  O   . PHE   B 1 201 ? -10.179 1.887   -64.031 1.00 18.27 ? 642  PHE   B O   1 
ATOM   4466 C  CB  . PHE   B 1 201 ? -8.372  4.175   -62.813 1.00 16.71 ? 642  PHE   B CB  1 
ATOM   4467 C  CG  . PHE   B 1 201 ? -7.643  3.976   -61.508 1.00 14.98 ? 642  PHE   B CG  1 
ATOM   4468 C  CD1 . PHE   B 1 201 ? -6.267  4.205   -61.434 1.00 18.38 ? 642  PHE   B CD1 1 
ATOM   4469 C  CD2 . PHE   B 1 201 ? -8.321  3.566   -60.353 1.00 15.64 ? 642  PHE   B CD2 1 
ATOM   4470 C  CE1 . PHE   B 1 201 ? -5.589  4.029   -60.248 1.00 21.27 ? 642  PHE   B CE1 1 
ATOM   4471 C  CE2 . PHE   B 1 201 ? -7.629  3.391   -59.162 1.00 17.50 ? 642  PHE   B CE2 1 
ATOM   4472 C  CZ  . PHE   B 1 201 ? -6.273  3.633   -59.111 1.00 19.21 ? 642  PHE   B CZ  1 
ATOM   4473 N  N   . PHE   B 1 202 ? -8.477  0.870   -62.940 1.00 15.42 ? 643  PHE   B N   1 
ATOM   4474 C  CA  . PHE   B 1 202 ? -9.245  -0.331  -62.639 1.00 16.29 ? 643  PHE   B CA  1 
ATOM   4475 C  C   . PHE   B 1 202 ? -10.600 0.049   -62.039 1.00 16.25 ? 643  PHE   B C   1 
ATOM   4476 O  O   . PHE   B 1 202 ? -10.661 0.915   -61.156 1.00 14.75 ? 643  PHE   B O   1 
ATOM   4477 C  CB  . PHE   B 1 202 ? -8.482  -1.186  -61.620 1.00 16.53 ? 643  PHE   B CB  1 
ATOM   4478 C  CG  . PHE   B 1 202 ? -9.113  -2.514  -61.369 1.00 17.57 ? 643  PHE   B CG  1 
ATOM   4479 C  CD1 . PHE   B 1 202 ? -10.080 -2.671  -60.377 1.00 17.42 ? 643  PHE   B CD1 1 
ATOM   4480 C  CD2 . PHE   B 1 202 ? -8.781  -3.607  -62.154 1.00 17.49 ? 643  PHE   B CD2 1 
ATOM   4481 C  CE1 . PHE   B 1 202 ? -10.695 -3.893  -60.171 1.00 17.43 ? 643  PHE   B CE1 1 
ATOM   4482 C  CE2 . PHE   B 1 202 ? -9.382  -4.832  -61.945 1.00 22.37 ? 643  PHE   B CE2 1 
ATOM   4483 C  CZ  . PHE   B 1 202 ? -10.341 -4.978  -60.956 1.00 17.88 ? 643  PHE   B CZ  1 
ATOM   4484 N  N   . PRO   B 1 203 ? -11.704 -0.607  -62.443 1.00 13.74 ? 644  PRO   B N   1 
ATOM   4485 C  CA  . PRO   B 1 203 ? -11.732 -1.786  -63.317 1.00 17.23 ? 644  PRO   B CA  1 
ATOM   4486 C  C   . PRO   B 1 203 ? -11.805 -1.532  -64.832 1.00 19.91 ? 644  PRO   B C   1 
ATOM   4487 O  O   . PRO   B 1 203 ? -12.249 -2.433  -65.553 1.00 20.68 ? 644  PRO   B O   1 
ATOM   4488 C  CB  . PRO   B 1 203 ? -12.980 -2.537  -62.840 1.00 21.89 ? 644  PRO   B CB  1 
ATOM   4489 C  CG  . PRO   B 1 203 ? -13.893 -1.460  -62.345 1.00 19.67 ? 644  PRO   B CG  1 
ATOM   4490 C  CD  . PRO   B 1 203 ? -13.006 -0.381  -61.786 1.00 13.88 ? 644  PRO   B CD  1 
ATOM   4491 N  N   . ASN   B 1 204 ? -11.419 -0.339  -65.283 1.00 17.64 ? 645  ASN   B N   1 
ATOM   4492 C  CA  . ASN   B 1 204 ? -11.087 -0.090  -66.696 1.00 19.43 ? 645  ASN   B CA  1 
ATOM   4493 C  C   . ASN   B 1 204 ? -12.317 -0.094  -67.602 1.00 23.41 ? 645  ASN   B C   1 
ATOM   4494 O  O   . ASN   B 1 204 ? -12.244 -0.520  -68.756 1.00 23.98 ? 645  ASN   B O   1 
ATOM   4495 C  CB  . ASN   B 1 204 ? -10.021 -1.061  -67.212 1.00 22.58 ? 645  ASN   B CB  1 
ATOM   4496 C  CG  . ASN   B 1 204 ? -8.761  -1.011  -66.398 1.00 24.23 ? 645  ASN   B CG  1 
ATOM   4497 O  OD1 . ASN   B 1 204 ? -7.996  -0.051  -66.475 1.00 33.66 ? 645  ASN   B OD1 1 
ATOM   4498 N  ND2 . ASN   B 1 204 ? -8.549  -2.031  -65.588 1.00 22.99 ? 645  ASN   B ND2 1 
ATOM   4499 N  N   . SER   B 1 205 ? -13.446 0.391   -67.095 1.00 19.07 ? 646  SER   B N   1 
ATOM   4500 C  CA  . SER   B 1 205 ? -14.686 0.377   -67.854 1.00 17.99 ? 646  SER   B CA  1 
ATOM   4501 C  C   . SER   B 1 205 ? -15.343 1.745   -67.830 1.00 18.98 ? 646  SER   B C   1 
ATOM   4502 O  O   . SER   B 1 205 ? -15.411 2.396   -66.781 1.00 19.77 ? 646  SER   B O   1 
ATOM   4503 C  CB  . SER   B 1 205 ? -15.660 -0.660  -67.275 1.00 17.03 ? 646  SER   B CB  1 
ATOM   4504 O  OG  . SER   B 1 205 ? -16.913 -0.586  -67.926 1.00 19.69 ? 646  SER   B OG  1 
ATOM   4505 N  N   . GLU   B 1 206 ? -15.852 2.173   -68.986 1.00 17.65 ? 647  GLU   B N   1 
ATOM   4506 C  CA  . GLU   B 1 206 ? -16.639 3.396   -69.027 1.00 15.85 ? 647  GLU   B CA  1 
ATOM   4507 C  C   . GLU   B 1 206 ? -17.975 3.273   -68.322 1.00 14.09 ? 647  GLU   B C   1 
ATOM   4508 O  O   . GLU   B 1 206 ? -18.701 4.270   -68.212 1.00 17.15 ? 647  GLU   B O   1 
ATOM   4509 C  CB  . GLU   B 1 206 ? -16.851 3.832   -70.482 1.00 18.77 ? 647  GLU   B CB  1 
ATOM   4510 C  CG  . GLU   B 1 206 ? -15.552 4.115   -71.218 1.00 19.21 ? 647  GLU   B CG  1 
ATOM   4511 C  CD  . GLU   B 1 206 ? -15.756 4.743   -72.585 1.00 24.09 ? 647  GLU   B CD  1 
ATOM   4512 O  OE1 . GLU   B 1 206 ? -16.868 5.224   -72.857 1.00 28.87 ? 647  GLU   B OE1 1 
ATOM   4513 O  OE2 . GLU   B 1 206 ? -14.791 4.749   -73.369 1.00 29.47 ? 647  GLU   B OE2 1 
ATOM   4514 N  N   . ASP   B 1 207 ? -18.331 2.082   -67.833 1.00 16.05 ? 648  ASP   B N   1 
ATOM   4515 C  CA  . ASP   B 1 207 ? -19.503 1.959   -66.967 1.00 17.68 ? 648  ASP   B CA  1 
ATOM   4516 C  C   . ASP   B 1 207 ? -19.417 2.868   -65.748 1.00 17.43 ? 648  ASP   B C   1 
ATOM   4517 O  O   . ASP   B 1 207 ? -20.445 3.172   -65.143 1.00 16.86 ? 648  ASP   B O   1 
ATOM   4518 C  CB  . ASP   B 1 207 ? -19.649 0.529   -66.444 1.00 17.77 ? 648  ASP   B CB  1 
ATOM   4519 C  CG  . ASP   B 1 207 ? -19.963 -0.475  -67.534 1.00 27.71 ? 648  ASP   B CG  1 
ATOM   4520 O  OD1 . ASP   B 1 207 ? -20.153 -0.085  -68.704 1.00 27.20 ? 648  ASP   B OD1 1 
ATOM   4521 O  OD2 . ASP   B 1 207 ? -20.035 -1.671  -67.209 1.00 25.72 ? 648  ASP   B OD2 1 
ATOM   4522 N  N   . ALA   B 1 208 ? -18.215 3.284   -65.368 1.00 15.94 ? 649  ALA   B N   1 
ATOM   4523 C  CA  . ALA   B 1 208 ? -17.989 4.115   -64.184 1.00 17.07 ? 649  ALA   B CA  1 
ATOM   4524 C  C   . ALA   B 1 208 ? -18.118 5.607   -64.474 1.00 17.88 ? 649  ALA   B C   1 
ATOM   4525 O  O   . ALA   B 1 208 ? -17.976 6.419   -63.552 1.00 15.84 ? 649  ALA   B O   1 
ATOM   4526 C  CB  . ALA   B 1 208 ? -16.617 3.798   -63.578 1.00 16.17 ? 649  ALA   B CB  1 
ATOM   4527 N  N   . ASN   B 1 209 ? -18.413 5.997   -65.722 1.00 16.93 ? 650  ASN   B N   1 
ATOM   4528 C  CA  . ASN   B 1 209 ? -18.471 7.419   -66.033 1.00 20.62 ? 650  ASN   B CA  1 
ATOM   4529 C  C   . ASN   B 1 209 ? -19.749 8.051   -65.476 1.00 16.60 ? 650  ASN   B C   1 
ATOM   4530 O  O   . ASN   B 1 209 ? -20.721 7.371   -65.136 1.00 16.25 ? 650  ASN   B O   1 
ATOM   4531 C  CB  . ASN   B 1 209 ? -18.348 7.669   -67.543 1.00 19.53 ? 650  ASN   B CB  1 
ATOM   4532 C  CG  . ASN   B 1 209 ? -17.651 8.978   -67.847 1.00 23.60 ? 650  ASN   B CG  1 
ATOM   4533 O  OD1 . ASN   B 1 209 ? -17.346 9.740   -66.939 1.00 22.75 ? 650  ASN   B OD1 1 
ATOM   4534 N  ND2 . ASN   B 1 209 ? -17.372 9.233   -69.123 1.00 24.52 ? 650  ASN   B ND2 1 
ATOM   4535 N  N   . TYR   B 1 210 ? -19.735 9.388   -65.394 1.00 17.95 ? 651  TYR   B N   1 
ATOM   4536 C  CA  . TYR   B 1 210 ? -20.845 10.112  -64.782 1.00 19.40 ? 651  TYR   B CA  1 
ATOM   4537 C  C   . TYR   B 1 210 ? -22.145 9.983   -65.571 1.00 20.61 ? 651  TYR   B C   1 
ATOM   4538 O  O   . TYR   B 1 210 ? -23.226 10.206  -65.009 1.00 20.36 ? 651  TYR   B O   1 
ATOM   4539 C  CB  . TYR   B 1 210 ? -20.490 11.595  -64.612 1.00 20.08 ? 651  TYR   B CB  1 
ATOM   4540 C  CG  . TYR   B 1 210 ? -20.159 12.284  -65.927 1.00 20.00 ? 651  TYR   B CG  1 
ATOM   4541 C  CD1 . TYR   B 1 210 ? -21.170 12.755  -66.762 1.00 28.69 ? 651  TYR   B CD1 1 
ATOM   4542 C  CD2 . TYR   B 1 210 ? -18.847 12.444  -66.341 1.00 22.36 ? 651  TYR   B CD2 1 
ATOM   4543 C  CE1 . TYR   B 1 210 ? -20.869 13.363  -67.970 1.00 23.62 ? 651  TYR   B CE1 1 
ATOM   4544 C  CE2 . TYR   B 1 210 ? -18.539 13.062  -67.547 1.00 24.99 ? 651  TYR   B CE2 1 
ATOM   4545 C  CZ  . TYR   B 1 210 ? -19.561 13.516  -68.348 1.00 27.25 ? 651  TYR   B CZ  1 
ATOM   4546 O  OH  . TYR   B 1 210 ? -19.270 14.130  -69.551 1.00 36.26 ? 651  TYR   B OH  1 
ATOM   4547 N  N   . ASP   B 1 211 ? -22.073 9.636   -66.852 1.00 22.30 ? 652  ASP   B N   1 
ATOM   4548 C  CA  . ASP   B 1 211 ? -23.302 9.585   -67.630 1.00 22.66 ? 652  ASP   B CA  1 
ATOM   4549 C  C   . ASP   B 1 211 ? -24.061 8.278   -67.466 1.00 24.08 ? 652  ASP   B C   1 
ATOM   4550 O  O   . ASP   B 1 211 ? -25.109 8.110   -68.093 1.00 23.47 ? 652  ASP   B O   1 
ATOM   4551 C  CB  . ASP   B 1 211 ? -23.023 9.868   -69.109 1.00 21.99 ? 652  ASP   B CB  1 
ATOM   4552 C  CG  . ASP   B 1 211 ? -22.158 8.805   -69.764 1.00 34.93 ? 652  ASP   B CG  1 
ATOM   4553 O  OD1 . ASP   B 1 211 ? -21.450 8.061   -69.048 1.00 25.25 ? 652  ASP   B OD1 1 
ATOM   4554 O  OD2 . ASP   B 1 211 ? -22.186 8.714   -71.011 1.00 39.36 ? 652  ASP   B OD2 1 
ATOM   4555 N  N   . LYS   B 1 212 ? -23.579 7.350   -66.642 1.00 19.90 ? 653  LYS   B N   1 
ATOM   4556 C  CA  . LYS   B 1 212 ? -24.316 6.121   -66.372 1.00 17.65 ? 653  LYS   B CA  1 
ATOM   4557 C  C   . LYS   B 1 212 ? -25.196 6.375   -65.156 1.00 21.74 ? 653  LYS   B C   1 
ATOM   4558 O  O   . LYS   B 1 212 ? -24.726 6.340   -64.010 1.00 20.63 ? 653  LYS   B O   1 
ATOM   4559 C  CB  . LYS   B 1 212 ? -23.373 4.939   -66.184 1.00 19.15 ? 653  LYS   B CB  1 
ATOM   4560 C  CG  . LYS   B 1 212 ? -22.312 4.794   -67.294 1.00 21.84 ? 653  LYS   B CG  1 
ATOM   4561 C  CD  . LYS   B 1 212 ? -22.909 4.894   -68.697 1.00 30.60 ? 653  LYS   B CD  1 
ATOM   4562 C  CE  . LYS   B 1 212 ? -21.883 4.510   -69.765 1.00 23.68 ? 653  LYS   B CE  1 
ATOM   4563 N  NZ  . LYS   B 1 212 ? -20.769 5.511   -69.948 1.00 20.39 ? 653  LYS   B NZ  1 
ATOM   4564 N  N   . VAL   B 1 213 ? -26.484 6.635   -65.410 1.00 20.06 ? 654  VAL   B N   1 
ATOM   4565 C  CA  . VAL   B 1 213 ? -27.415 7.103   -64.397 1.00 17.96 ? 654  VAL   B CA  1 
ATOM   4566 C  C   . VAL   B 1 213 ? -28.390 6.027   -63.948 1.00 18.94 ? 654  VAL   B C   1 
ATOM   4567 O  O   . VAL   B 1 213 ? -29.256 6.306   -63.113 1.00 17.73 ? 654  VAL   B O   1 
ATOM   4568 C  CB  . VAL   B 1 213 ? -28.182 8.369   -64.849 1.00 20.13 ? 654  VAL   B CB  1 
ATOM   4569 C  CG1 . VAL   B 1 213 ? -27.225 9.487   -65.224 1.00 22.72 ? 654  VAL   B CG1 1 
ATOM   4570 C  CG2 . VAL   B 1 213 ? -29.143 8.047   -66.009 1.00 17.31 ? 654  VAL   B CG2 1 
ATOM   4571 N  N   . GLY   B 1 214 ? -28.275 4.813   -64.466 1.00 17.12 ? 655  GLY   B N   1 
ATOM   4572 C  CA  . GLY   B 1 214 ? -29.233 3.758   -64.218 1.00 19.27 ? 655  GLY   B CA  1 
ATOM   4573 C  C   . GLY   B 1 214 ? -30.115 3.519   -65.432 1.00 19.33 ? 655  GLY   B C   1 
ATOM   4574 O  O   . GLY   B 1 214 ? -30.078 4.247   -66.422 1.00 22.47 ? 655  GLY   B O   1 
ATOM   4575 N  N   . LEU   B 1 215 ? -30.920 2.466   -65.333 1.00 17.79 ? 656  LEU   B N   1 
ATOM   4576 C  CA  . LEU   B 1 215 ? -31.716 1.995   -66.458 1.00 16.40 ? 656  LEU   B CA  1 
ATOM   4577 C  C   . LEU   B 1 215 ? -33.121 1.681   -65.981 1.00 19.60 ? 656  LEU   B C   1 
ATOM   4578 O  O   . LEU   B 1 215 ? -33.338 1.281   -64.837 1.00 18.20 ? 656  LEU   B O   1 
ATOM   4579 C  CB  . LEU   B 1 215 ? -31.104 0.716   -67.052 1.00 18.28 ? 656  LEU   B CB  1 
ATOM   4580 C  CG  . LEU   B 1 215 ? -29.699 0.864   -67.649 1.00 21.84 ? 656  LEU   B CG  1 
ATOM   4581 C  CD1 . LEU   B 1 215 ? -29.127 -0.508  -67.972 1.00 25.03 ? 656  LEU   B CD1 1 
ATOM   4582 C  CD2 . LEU   B 1 215 ? -29.757 1.738   -68.884 1.00 21.85 ? 656  LEU   B CD2 1 
ATOM   4583 N  N   . GLY   B 1 216 ? -34.078 1.824   -66.892 1.00 19.87 ? 657  GLY   B N   1 
ATOM   4584 C  CA  . GLY   B 1 216 ? -35.447 1.472   -66.558 1.00 18.97 ? 657  GLY   B CA  1 
ATOM   4585 C  C   . GLY   B 1 216 ? -35.948 2.298   -65.392 1.00 15.89 ? 657  GLY   B C   1 
ATOM   4586 O  O   . GLY   B 1 216 ? -35.715 3.511   -65.314 1.00 20.04 ? 657  GLY   B O   1 
ATOM   4587 N  N   . LYS   B 1 217 ? -36.611 1.634   -64.450 1.00 16.82 ? 658  LYS   B N   1 
ATOM   4588 C  CA  . LYS   B 1 217 ? -37.093 2.348   -63.273 1.00 17.54 ? 658  LYS   B CA  1 
ATOM   4589 C  C   . LYS   B 1 217 ? -35.938 2.892   -62.429 1.00 31.88 ? 658  LYS   B C   1 
ATOM   4590 O  O   . LYS   B 1 217 ? -36.145 3.801   -61.616 1.00 22.45 ? 658  LYS   B O   1 
ATOM   4591 C  CB  . LYS   B 1 217 ? -37.998 1.458   -62.427 1.00 21.84 ? 658  LYS   B CB  1 
ATOM   4592 C  CG  . LYS   B 1 217 ? -37.281 0.316   -61.754 1.00 27.43 ? 658  LYS   B CG  1 
ATOM   4593 C  CD  . LYS   B 1 217 ? -38.203 -0.403  -60.794 1.00 29.59 ? 658  LYS   B CD  1 
ATOM   4594 C  CE  . LYS   B 1 217 ? -37.507 -1.608  -60.174 1.00 33.40 ? 658  LYS   B CE  1 
ATOM   4595 N  NZ  . LYS   B 1 217 ? -38.448 -2.462  -59.410 1.00 43.50 ? 658  LYS   B NZ  1 
ATOM   4596 N  N   . GLY   B 1 218 ? -34.727 2.379   -62.616 1.00 19.76 ? 659  GLY   B N   1 
ATOM   4597 C  CA  . GLY   B 1 218 ? -33.556 2.872   -61.920 1.00 17.90 ? 659  GLY   B CA  1 
ATOM   4598 C  C   . GLY   B 1 218 ? -32.863 4.085   -62.503 1.00 21.99 ? 659  GLY   B C   1 
ATOM   4599 O  O   . GLY   B 1 218 ? -31.773 4.429   -62.036 1.00 21.77 ? 659  GLY   B O   1 
ATOM   4600 N  N   A ARG   B 1 219 ? -33.437 4.745   -63.508 0.59 20.33 ? 660  ARG   B N   1 
ATOM   4601 N  N   B ARG   B 1 219 ? -33.439 4.752   -63.504 0.41 20.06 ? 660  ARG   B N   1 
ATOM   4602 C  CA  A ARG   B 1 219 ? -32.825 5.956   -64.040 0.59 21.77 ? 660  ARG   B CA  1 
ATOM   4603 C  CA  B ARG   B 1 219 ? -32.806 5.947   -64.051 0.41 21.04 ? 660  ARG   B CA  1 
ATOM   4604 C  C   A ARG   B 1 219 ? -32.777 7.026   -62.958 0.59 24.96 ? 660  ARG   B C   1 
ATOM   4605 C  C   B ARG   B 1 219 ? -32.779 7.050   -62.998 0.41 24.24 ? 660  ARG   B C   1 
ATOM   4606 O  O   A ARG   B 1 219 ? -33.802 7.359   -62.355 0.59 25.89 ? 660  ARG   B O   1 
ATOM   4607 O  O   B ARG   B 1 219 ? -33.821 7.429   -62.452 0.41 25.42 ? 660  ARG   B O   1 
ATOM   4608 C  CB  A ARG   B 1 219 ? -33.619 6.459   -65.246 0.59 22.42 ? 660  ARG   B CB  1 
ATOM   4609 C  CB  B ARG   B 1 219 ? -33.545 6.415   -65.308 0.41 20.96 ? 660  ARG   B CB  1 
ATOM   4610 C  CG  A ARG   B 1 219 ? -33.548 5.542   -66.450 0.59 28.15 ? 660  ARG   B CG  1 
ATOM   4611 C  CG  B ARG   B 1 219 ? -32.950 5.877   -66.606 0.41 22.20 ? 660  ARG   B CG  1 
ATOM   4612 C  CD  A ARG   B 1 219 ? -34.316 6.127   -67.632 0.59 22.67 ? 660  ARG   B CD  1 
ATOM   4613 C  CD  B ARG   B 1 219 ? -33.657 6.435   -67.842 0.41 18.98 ? 660  ARG   B CD  1 
ATOM   4614 N  NE  A ARG   B 1 219 ? -33.678 7.325   -68.173 0.59 22.65 ? 660  ARG   B NE  1 
ATOM   4615 N  NE  B ARG   B 1 219 ? -34.939 7.045   -67.501 0.41 21.58 ? 660  ARG   B NE  1 
ATOM   4616 C  CZ  A ARG   B 1 219 ? -34.233 8.534   -68.178 0.59 19.99 ? 660  ARG   B CZ  1 
ATOM   4617 C  CZ  B ARG   B 1 219 ? -35.218 8.336   -67.651 0.41 17.24 ? 660  ARG   B CZ  1 
ATOM   4618 N  NH1 A ARG   B 1 219 ? -35.445 8.721   -67.672 0.59 19.22 ? 660  ARG   B NH1 1 
ATOM   4619 N  NH1 B ARG   B 1 219 ? -34.311 9.166   -68.147 0.41 17.58 ? 660  ARG   B NH1 1 
ATOM   4620 N  NH2 A ARG   B 1 219 ? -33.579 9.562   -68.702 0.59 17.43 ? 660  ARG   B NH2 1 
ATOM   4621 N  NH2 B ARG   B 1 219 ? -36.405 8.803   -67.301 0.41 14.06 ? 660  ARG   B NH2 1 
ATOM   4622 N  N   . GLY   B 1 220 ? -31.580 7.558   -62.710 1.00 22.04 ? 661  GLY   B N   1 
ATOM   4623 C  CA  . GLY   B 1 220 ? -31.365 8.511   -61.644 1.00 22.46 ? 661  GLY   B CA  1 
ATOM   4624 C  C   . GLY   B 1 220 ? -30.869 7.894   -60.351 1.00 21.49 ? 661  GLY   B C   1 
ATOM   4625 O  O   . GLY   B 1 220 ? -30.392 8.630   -59.476 1.00 21.05 ? 661  GLY   B O   1 
ATOM   4626 N  N   . TYR   B 1 221 ? -30.964 6.573   -60.201 1.00 18.95 ? 662  TYR   B N   1 
ATOM   4627 C  CA  . TYR   B 1 221 ? -30.624 5.905   -58.950 1.00 19.95 ? 662  TYR   B CA  1 
ATOM   4628 C  C   . TYR   B 1 221 ? -29.244 5.256   -58.983 1.00 16.02 ? 662  TYR   B C   1 
ATOM   4629 O  O   . TYR   B 1 221 ? -28.953 4.377   -58.154 1.00 17.64 ? 662  TYR   B O   1 
ATOM   4630 C  CB  . TYR   B 1 221 ? -31.711 4.914   -58.536 1.00 22.35 ? 662  TYR   B CB  1 
ATOM   4631 C  CG  . TYR   B 1 221 ? -33.014 5.605   -58.207 1.00 19.59 ? 662  TYR   B CG  1 
ATOM   4632 C  CD1 . TYR   B 1 221 ? -33.905 5.972   -59.220 1.00 23.67 ? 662  TYR   B CD1 1 
ATOM   4633 C  CD2 . TYR   B 1 221 ? -33.339 5.931   -56.902 1.00 21.18 ? 662  TYR   B CD2 1 
ATOM   4634 C  CE1 . TYR   B 1 221 ? -35.090 6.622   -58.924 1.00 26.96 ? 662  TYR   B CE1 1 
ATOM   4635 C  CE2 . TYR   B 1 221 ? -34.527 6.573   -56.594 1.00 21.34 ? 662  TYR   B CE2 1 
ATOM   4636 C  CZ  . TYR   B 1 221 ? -35.397 6.918   -57.613 1.00 29.97 ? 662  TYR   B CZ  1 
ATOM   4637 O  OH  . TYR   B 1 221 ? -36.577 7.562   -57.321 1.00 38.38 ? 662  TYR   B OH  1 
ATOM   4638 N  N   . ASN   B 1 222 ? -28.410 5.660   -59.935 1.00 18.73 ? 663  ASN   B N   1 
ATOM   4639 C  CA  . ASN   B 1 222 ? -27.000 5.288   -59.982 1.00 16.41 ? 663  ASN   B CA  1 
ATOM   4640 C  C   . ASN   B 1 222 ? -26.212 6.566   -60.182 1.00 18.81 ? 663  ASN   B C   1 
ATOM   4641 O  O   . ASN   B 1 222 ? -26.365 7.233   -61.209 1.00 19.32 ? 663  ASN   B O   1 
ATOM   4642 C  CB  . ASN   B 1 222 ? -26.733 4.332   -61.143 1.00 14.17 ? 663  ASN   B CB  1 
ATOM   4643 C  CG  . ASN   B 1 222 ? -25.394 3.682   -61.043 1.00 16.11 ? 663  ASN   B CG  1 
ATOM   4644 O  OD1 . ASN   B 1 222 ? -25.231 2.711   -60.300 1.00 16.77 ? 663  ASN   B OD1 1 
ATOM   4645 N  ND2 . ASN   B 1 222 ? -24.421 4.218   -61.770 1.00 17.79 ? 663  ASN   B ND2 1 
ATOM   4646 N  N   . VAL   B 1 223 ? -25.382 6.923   -59.204 1.00 18.33 ? 664  VAL   B N   1 
ATOM   4647 C  CA  . VAL   B 1 223 ? -24.658 8.191   -59.220 1.00 15.16 ? 664  VAL   B CA  1 
ATOM   4648 C  C   . VAL   B 1 223 ? -23.159 7.894   -59.212 1.00 15.03 ? 664  VAL   B C   1 
ATOM   4649 O  O   . VAL   B 1 223 ? -22.602 7.510   -58.172 1.00 15.70 ? 664  VAL   B O   1 
ATOM   4650 C  CB  . VAL   B 1 223 ? -25.049 9.098   -58.043 1.00 18.74 ? 664  VAL   B CB  1 
ATOM   4651 C  CG1 . VAL   B 1 223 ? -24.335 10.421  -58.156 1.00 17.25 ? 664  VAL   B CG1 1 
ATOM   4652 C  CG2 . VAL   B 1 223 ? -26.566 9.295   -58.003 1.00 17.37 ? 664  VAL   B CG2 1 
ATOM   4653 N  N   . ASN   B 1 224 ? -22.492 8.097   -60.342 1.00 15.88 ? 665  ASN   B N   1 
ATOM   4654 C  CA  . ASN   B 1 224 ? -21.051 7.911   -60.444 1.00 16.37 ? 665  ASN   B CA  1 
ATOM   4655 C  C   . ASN   B 1 224 ? -20.375 9.273   -60.397 1.00 23.33 ? 665  ASN   B C   1 
ATOM   4656 O  O   . ASN   B 1 224 ? -20.667 10.149  -61.223 1.00 18.91 ? 665  ASN   B O   1 
ATOM   4657 C  CB  . ASN   B 1 224 ? -20.673 7.225   -61.756 1.00 17.21 ? 665  ASN   B CB  1 
ATOM   4658 C  CG  . ASN   B 1 224 ? -20.942 5.729   -61.747 1.00 17.18 ? 665  ASN   B CG  1 
ATOM   4659 O  OD1 . ASN   B 1 224 ? -20.932 5.076   -60.693 1.00 15.77 ? 665  ASN   B OD1 1 
ATOM   4660 N  ND2 . ASN   B 1 224 ? -21.182 5.173   -62.939 1.00 16.30 ? 665  ASN   B ND2 1 
ATOM   4661 N  N   . ILE   B 1 225 ? -19.447 9.429   -59.460 1.00 17.11 ? 666  ILE   B N   1 
ATOM   4662 C  CA  . ILE   B 1 225 ? -18.624 10.622  -59.315 1.00 16.53 ? 666  ILE   B CA  1 
ATOM   4663 C  C   . ILE   B 1 225 ? -17.200 10.243  -59.692 1.00 17.56 ? 666  ILE   B C   1 
ATOM   4664 O  O   . ILE   B 1 225 ? -16.445 9.748   -58.842 1.00 17.25 ? 666  ILE   B O   1 
ATOM   4665 C  CB  . ILE   B 1 225 ? -18.736 11.179  -57.889 1.00 18.09 ? 666  ILE   B CB  1 
ATOM   4666 C  CG1 . ILE   B 1 225 ? -20.222 11.355  -57.570 1.00 16.30 ? 666  ILE   B CG1 1 
ATOM   4667 C  CG2 . ILE   B 1 225 ? -17.961 12.472  -57.782 1.00 16.93 ? 666  ILE   B CG2 1 
ATOM   4668 C  CD1 . ILE   B 1 225 ? -20.548 11.864  -56.206 1.00 17.90 ? 666  ILE   B CD1 1 
ATOM   4669 N  N   . PRO   B 1 226 ? -16.791 10.436  -60.939 1.00 15.47 ? 667  PRO   B N   1 
ATOM   4670 C  CA  . PRO   B 1 226 ? -15.487 9.936   -61.377 1.00 18.99 ? 667  PRO   B CA  1 
ATOM   4671 C  C   . PRO   B 1 226 ? -14.411 11.009  -61.362 1.00 18.70 ? 667  PRO   B C   1 
ATOM   4672 O  O   . PRO   B 1 226 ? -14.614 12.109  -61.895 1.00 20.98 ? 667  PRO   B O   1 
ATOM   4673 C  CB  . PRO   B 1 226 ? -15.767 9.468   -62.810 1.00 18.56 ? 667  PRO   B CB  1 
ATOM   4674 C  CG  . PRO   B 1 226 ? -16.919 10.320  -63.266 1.00 21.61 ? 667  PRO   B CG  1 
ATOM   4675 C  CD  . PRO   B 1 226 ? -17.635 10.875  -62.067 1.00 19.32 ? 667  PRO   B CD  1 
ATOM   4676 N  N   . TRP   B 1 227 ? -13.257 10.700  -60.778 1.00 18.10 ? 668  TRP   B N   1 
ATOM   4677 C  CA  . TRP   B 1 227 ? -12.155 11.646  -60.696 1.00 17.71 ? 668  TRP   B CA  1 
ATOM   4678 C  C   . TRP   B 1 227 ? -11.154 11.390  -61.812 1.00 20.09 ? 668  TRP   B C   1 
ATOM   4679 O  O   . TRP   B 1 227 ? -10.809 10.243  -62.105 1.00 18.63 ? 668  TRP   B O   1 
ATOM   4680 C  CB  . TRP   B 1 227 ? -11.428 11.506  -59.361 1.00 17.35 ? 668  TRP   B CB  1 
ATOM   4681 C  CG  . TRP   B 1 227 ? -12.273 11.661  -58.155 1.00 14.39 ? 668  TRP   B CG  1 
ATOM   4682 C  CD1 . TRP   B 1 227 ? -12.450 10.731  -57.170 1.00 16.19 ? 668  TRP   B CD1 1 
ATOM   4683 C  CD2 . TRP   B 1 227 ? -13.033 12.809  -57.768 1.00 17.20 ? 668  TRP   B CD2 1 
ATOM   4684 N  NE1 . TRP   B 1 227 ? -13.273 11.226  -56.195 1.00 17.40 ? 668  TRP   B NE1 1 
ATOM   4685 C  CE2 . TRP   B 1 227 ? -13.650 12.502  -56.534 1.00 17.76 ? 668  TRP   B CE2 1 
ATOM   4686 C  CE3 . TRP   B 1 227 ? -13.266 14.065  -58.349 1.00 19.72 ? 668  TRP   B CE3 1 
ATOM   4687 C  CZ2 . TRP   B 1 227 ? -14.469 13.402  -55.869 1.00 19.76 ? 668  TRP   B CZ2 1 
ATOM   4688 C  CZ3 . TRP   B 1 227 ? -14.085 14.957  -57.688 1.00 22.11 ? 668  TRP   B CZ3 1 
ATOM   4689 C  CH2 . TRP   B 1 227 ? -14.681 14.624  -56.465 1.00 20.56 ? 668  TRP   B CH2 1 
ATOM   4690 N  N   . ASN   B 1 228 ? -10.671 12.473  -62.418 1.00 20.34 ? 669  ASN   B N   1 
ATOM   4691 C  CA  . ASN   B 1 228 ? -9.680  12.425  -63.481 1.00 23.98 ? 669  ASN   B CA  1 
ATOM   4692 C  C   . ASN   B 1 228 ? -8.597  13.448  -63.183 1.00 21.00 ? 669  ASN   B C   1 
ATOM   4693 O  O   . ASN   B 1 228 ? -8.888  14.530  -62.667 1.00 26.93 ? 669  ASN   B O   1 
ATOM   4694 C  CB  . ASN   B 1 228 ? -10.316 12.807  -64.826 1.00 20.08 ? 669  ASN   B CB  1 
ATOM   4695 C  CG  . ASN   B 1 228 ? -11.478 11.933  -65.175 1.00 22.53 ? 669  ASN   B CG  1 
ATOM   4696 O  OD1 . ASN   B 1 228 ? -11.335 10.718  -65.273 1.00 24.40 ? 669  ASN   B OD1 1 
ATOM   4697 N  ND2 . ASN   B 1 228 ? -12.643 12.535  -65.346 1.00 20.40 ? 669  ASN   B ND2 1 
ATOM   4698 N  N   . GLY   B 1 229 ? -7.357  13.096  -63.511 0.85 19.72 ? 670  GLY   B N   1 
ATOM   4699 C  CA  . GLY   B 1 229 ? -6.244  14.025  -63.492 0.85 22.49 ? 670  GLY   B CA  1 
ATOM   4700 C  C   . GLY   B 1 229 ? -6.065  14.811  -62.211 0.85 28.56 ? 670  GLY   B C   1 
ATOM   4701 O  O   . GLY   B 1 229 ? -6.225  16.034  -62.197 0.85 36.18 ? 670  GLY   B O   1 
ATOM   4702 N  N   . GLY   B 1 230 ? -5.733  14.124  -61.127 1.00 38.89 ? 671  GLY   B N   1 
ATOM   4703 C  CA  . GLY   B 1 230 ? -5.512  14.808  -59.871 1.00 29.35 ? 671  GLY   B CA  1 
ATOM   4704 C  C   . GLY   B 1 230 ? -5.454  13.859  -58.698 1.00 36.41 ? 671  GLY   B C   1 
ATOM   4705 O  O   . GLY   B 1 230 ? -6.160  12.846  -58.670 1.00 22.42 ? 671  GLY   B O   1 
ATOM   4706 N  N   . LYS   B 1 231 ? -4.600  14.183  -57.730 1.00 23.87 ? 672  LYS   B N   1 
ATOM   4707 C  CA  . LYS   B 1 231 ? -4.455  13.395  -56.509 0.88 24.63 ? 672  LYS   B CA  1 
ATOM   4708 C  C   . LYS   B 1 231 ? -5.485  13.929  -55.523 1.00 20.94 ? 672  LYS   B C   1 
ATOM   4709 O  O   . LYS   B 1 231 ? -5.210  14.812  -54.709 0.79 20.83 ? 672  LYS   B O   1 
ATOM   4710 C  CB  . LYS   B 1 231 ? -3.035  13.512  -55.974 1.00 22.01 ? 672  LYS   B CB  1 
ATOM   4711 C  CG  . LYS   B 1 231 ? -2.785  12.725  -54.706 1.00 36.10 ? 672  LYS   B CG  1 
ATOM   4712 C  CD  . LYS   B 1 231 ? -1.345  12.833  -54.235 1.00 43.48 ? 672  LYS   B CD  1 
ATOM   4713 C  CE  . LYS   B 1 231 ? -1.051  11.790  -53.169 1.00 45.96 ? 672  LYS   B CE  1 
ATOM   4714 N  NZ  . LYS   B 1 231 ? 0.390   11.764  -52.800 1.00 57.99 ? 672  LYS   B NZ  1 
ATOM   4715 N  N   . MET   B 1 232 ? -6.690  13.375  -55.586 1.00 19.13 ? 673  MET   B N   1 
ATOM   4716 C  CA  . MET   B 1 232 ? -7.807  13.909  -54.826 1.00 18.45 ? 673  MET   B CA  1 
ATOM   4717 C  C   . MET   B 1 232 ? -7.656  13.598  -53.335 1.00 18.14 ? 673  MET   B C   1 
ATOM   4718 O  O   . MET   B 1 232 ? -7.012  12.621  -52.934 1.00 19.17 ? 673  MET   B O   1 
ATOM   4719 C  CB  . MET   B 1 232 ? -9.114  13.329  -55.363 1.00 19.08 ? 673  MET   B CB  1 
ATOM   4720 C  CG  . MET   B 1 232 ? -9.328  13.584  -56.875 1.00 21.78 ? 673  MET   B CG  1 
ATOM   4721 S  SD  . MET   B 1 232 ? -8.867  15.257  -57.416 1.00 21.21 ? 673  MET   B SD  1 
ATOM   4722 C  CE  . MET   B 1 232 ? -9.230  15.142  -59.176 1.00 24.52 ? 673  MET   B CE  1 
ATOM   4723 N  N   . GLY   B 1 233 ? -8.253  14.451  -52.512 1.00 18.03 ? 674  GLY   B N   1 
ATOM   4724 C  CA  . GLY   B 1 233 ? -8.168  14.309  -51.073 1.00 17.62 ? 674  GLY   B CA  1 
ATOM   4725 C  C   . GLY   B 1 233 ? -9.367  14.895  -50.363 1.00 15.97 ? 674  GLY   B C   1 
ATOM   4726 O  O   . GLY   B 1 233 ? -10.440 15.025  -50.963 1.00 16.76 ? 674  GLY   B O   1 
ATOM   4727 N  N   . ASP   B 1 234 ? -9.196  15.275  -49.092 1.00 16.32 ? 675  ASP   B N   1 
ATOM   4728 C  CA  . ASP   B 1 234 ? -10.312 15.802  -48.307 1.00 16.16 ? 675  ASP   B CA  1 
ATOM   4729 C  C   . ASP   B 1 234 ? -11.073 16.932  -48.997 1.00 17.83 ? 675  ASP   B C   1 
ATOM   4730 O  O   . ASP   B 1 234 ? -12.313 16.895  -48.993 1.00 18.89 ? 675  ASP   B O   1 
ATOM   4731 C  CB  . ASP   B 1 234 ? -9.824  16.273  -46.926 1.00 18.02 ? 675  ASP   B CB  1 
ATOM   4732 C  CG  . ASP   B 1 234 ? -9.277  15.150  -46.074 1.00 17.76 ? 675  ASP   B CG  1 
ATOM   4733 O  OD1 . ASP   B 1 234 ? -9.333  13.981  -46.488 1.00 17.06 ? 675  ASP   B OD1 1 
ATOM   4734 O  OD2 . ASP   B 1 234 ? -8.761  15.450  -44.974 1.00 19.68 ? 675  ASP   B OD2 1 
ATOM   4735 N  N   . PRO   B 1 235 ? -10.425 17.952  -49.587 1.00 18.40 ? 676  PRO   B N   1 
ATOM   4736 C  CA  . PRO   B 1 235 ? -11.234 19.024  -50.201 1.00 19.24 ? 676  PRO   B CA  1 
ATOM   4737 C  C   . PRO   B 1 235 ? -12.174 18.521  -51.283 1.00 18.00 ? 676  PRO   B C   1 
ATOM   4738 O  O   . PRO   B 1 235 ? -13.336 18.934  -51.322 1.00 17.58 ? 676  PRO   B O   1 
ATOM   4739 C  CB  . PRO   B 1 235 ? -10.193 20.006  -50.752 1.00 22.18 ? 676  PRO   B CB  1 
ATOM   4740 C  CG  . PRO   B 1 235 ? -8.923  19.684  -50.040 1.00 20.63 ? 676  PRO   B CG  1 
ATOM   4741 C  CD  . PRO   B 1 235 ? -8.984  18.198  -49.777 1.00 21.94 ? 676  PRO   B CD  1 
ATOM   4742 N  N   . GLU   B 1 236 ? -11.691 17.640  -52.168 1.00 18.06 ? 677  GLU   B N   1 
ATOM   4743 C  CA  . GLU   B 1 236 ? -12.529 17.122  -53.250 1.00 19.39 ? 677  GLU   B CA  1 
ATOM   4744 C  C   . GLU   B 1 236 ? -13.670 16.255  -52.723 1.00 18.57 ? 677  GLU   B C   1 
ATOM   4745 O  O   . GLU   B 1 236 ? -14.812 16.355  -53.203 1.00 18.38 ? 677  GLU   B O   1 
ATOM   4746 C  CB  . GLU   B 1 236 ? -11.661 16.357  -54.257 1.00 17.40 ? 677  GLU   B CB  1 
ATOM   4747 C  CG  . GLU   B 1 236 ? -10.726 17.247  -55.042 1.00 19.90 ? 677  GLU   B CG  1 
ATOM   4748 C  CD  . GLU   B 1 236 ? -9.584  17.810  -54.205 1.00 26.23 ? 677  GLU   B CD  1 
ATOM   4749 O  OE1 . GLU   B 1 236 ? -9.080  17.114  -53.290 1.00 22.71 ? 677  GLU   B OE1 1 
ATOM   4750 O  OE2 . GLU   B 1 236 ? -9.183  18.957  -54.466 1.00 27.25 ? 677  GLU   B OE2 1 
ATOM   4751 N  N   . TYR   B 1 237 ? -13.382 15.392  -51.743 1.00 17.45 ? 678  TYR   B N   1 
ATOM   4752 C  CA  . TYR   B 1 237 ? -14.419 14.532  -51.177 1.00 17.10 ? 678  TYR   B CA  1 
ATOM   4753 C  C   . TYR   B 1 237 ? -15.461 15.338  -50.397 1.00 16.34 ? 678  TYR   B C   1 
ATOM   4754 O  O   . TYR   B 1 237 ? -16.671 15.076  -50.504 1.00 16.11 ? 678  TYR   B O   1 
ATOM   4755 C  CB  . TYR   B 1 237 ? -13.793 13.391  -50.345 1.00 14.47 ? 678  TYR   B CB  1 
ATOM   4756 C  CG  . TYR   B 1 237 ? -13.330 12.262  -51.229 1.00 15.04 ? 678  TYR   B CG  1 
ATOM   4757 C  CD1 . TYR   B 1 237 ? -12.233 12.425  -52.055 1.00 14.68 ? 678  TYR   B CD1 1 
ATOM   4758 C  CD2 . TYR   B 1 237 ? -14.045 11.067  -51.315 1.00 16.05 ? 678  TYR   B CD2 1 
ATOM   4759 C  CE1 . TYR   B 1 237 ? -11.809 11.430  -52.924 1.00 15.43 ? 678  TYR   B CE1 1 
ATOM   4760 C  CE2 . TYR   B 1 237 ? -13.640 10.057  -52.193 1.00 16.94 ? 678  TYR   B CE2 1 
ATOM   4761 C  CZ  . TYR   B 1 237 ? -12.512 10.236  -52.987 1.00 14.73 ? 678  TYR   B CZ  1 
ATOM   4762 O  OH  . TYR   B 1 237 ? -12.122 9.240   -53.855 1.00 14.63 ? 678  TYR   B OH  1 
ATOM   4763 N  N   . MET   B 1 238 ? -15.029 16.346  -49.637 1.00 18.98 ? 679  MET   B N   1 
ATOM   4764 C  CA  . MET   B 1 238 ? -15.992 17.212  -48.966 1.00 18.88 ? 679  MET   B CA  1 
ATOM   4765 C  C   . MET   B 1 238 ? -16.864 17.962  -49.972 1.00 18.80 ? 679  MET   B C   1 
ATOM   4766 O  O   . MET   B 1 238 ? -18.080 18.068  -49.784 1.00 20.26 ? 679  MET   B O   1 
ATOM   4767 C  CB  . MET   B 1 238 ? -15.269 18.193  -48.045 1.00 18.22 ? 679  MET   B CB  1 
ATOM   4768 C  CG  . MET   B 1 238 ? -14.544 17.539  -46.870 1.00 18.05 ? 679  MET   B CG  1 
ATOM   4769 S  SD  . MET   B 1 238 ? -15.616 16.662  -45.713 1.00 21.87 ? 679  MET   B SD  1 
ATOM   4770 C  CE  . MET   B 1 238 ? -16.457 18.034  -44.921 1.00 31.88 ? 679  MET   B CE  1 
ATOM   4771 N  N   . ALA   B 1 239 ? -16.268 18.477  -51.052 1.00 18.65 ? 680  ALA   B N   1 
ATOM   4772 C  CA  . ALA   B 1 239 ? -17.064 19.185  -52.058 1.00 20.79 ? 680  ALA   B CA  1 
ATOM   4773 C  C   . ALA   B 1 239 ? -18.087 18.259  -52.715 1.00 23.15 ? 680  ALA   B C   1 
ATOM   4774 O  O   . ALA   B 1 239 ? -19.252 18.636  -52.895 1.00 22.33 ? 680  ALA   B O   1 
ATOM   4775 C  CB  . ALA   B 1 239 ? -16.152 19.804  -53.111 1.00 20.55 ? 680  ALA   B CB  1 
ATOM   4776 N  N   . ALA   B 1 240 ? -17.663 17.049  -53.093 1.00 18.95 ? 681  ALA   B N   1 
ATOM   4777 C  CA  . ALA   B 1 240 ? -18.590 16.083  -53.677 1.00 17.68 ? 681  ALA   B CA  1 
ATOM   4778 C  C   . ALA   B 1 240 ? -19.729 15.749  -52.720 1.00 19.78 ? 681  ALA   B C   1 
ATOM   4779 O  O   . ALA   B 1 240 ? -20.883 15.591  -53.140 1.00 18.93 ? 681  ALA   B O   1 
ATOM   4780 C  CB  . ALA   B 1 240 ? -17.837 14.819  -54.081 1.00 18.85 ? 681  ALA   B CB  1 
ATOM   4781 N  N   . PHE   B 1 241 ? -19.434 15.618  -51.427 1.00 19.20 ? 682  PHE   B N   1 
ATOM   4782 C  CA  . PHE   B 1 241 ? -20.499 15.353  -50.468 1.00 16.64 ? 682  PHE   B CA  1 
ATOM   4783 C  C   . PHE   B 1 241 ? -21.450 16.539  -50.349 1.00 19.72 ? 682  PHE   B C   1 
ATOM   4784 O  O   . PHE   B 1 241 ? -22.673 16.355  -50.246 1.00 19.05 ? 682  PHE   B O   1 
ATOM   4785 C  CB  . PHE   B 1 241 ? -19.908 14.993  -49.101 1.00 16.09 ? 682  PHE   B CB  1 
ATOM   4786 C  CG  . PHE   B 1 241 ? -19.827 13.514  -48.858 1.00 17.39 ? 682  PHE   B CG  1 
ATOM   4787 C  CD1 . PHE   B 1 241 ? -19.087 12.697  -49.716 1.00 13.69 ? 682  PHE   B CD1 1 
ATOM   4788 C  CD2 . PHE   B 1 241 ? -20.482 12.942  -47.781 1.00 16.86 ? 682  PHE   B CD2 1 
ATOM   4789 C  CE1 . PHE   B 1 241 ? -19.021 11.323  -49.495 1.00 16.24 ? 682  PHE   B CE1 1 
ATOM   4790 C  CE2 . PHE   B 1 241 ? -20.404 11.580  -47.543 1.00 18.07 ? 682  PHE   B CE2 1 
ATOM   4791 C  CZ  . PHE   B 1 241 ? -19.671 10.770  -48.412 1.00 17.96 ? 682  PHE   B CZ  1 
ATOM   4792 N  N   . HIS   B 1 242 ? -20.901 17.756  -50.382 1.00 20.85 ? 683  HIS   B N   1 
ATOM   4793 C  CA  . HIS   B 1 242 ? -21.729 18.948  -50.224 1.00 20.59 ? 683  HIS   B CA  1 
ATOM   4794 C  C   . HIS   B 1 242 ? -22.620 19.191  -51.441 1.00 19.13 ? 683  HIS   B C   1 
ATOM   4795 O  O   . HIS   B 1 242 ? -23.796 19.527  -51.284 1.00 23.23 ? 683  HIS   B O   1 
ATOM   4796 C  CB  . HIS   B 1 242 ? -20.854 20.165  -49.937 1.00 23.01 ? 683  HIS   B CB  1 
ATOM   4797 C  CG  . HIS   B 1 242 ? -21.626 21.443  -49.862 1.00 38.01 ? 683  HIS   B CG  1 
ATOM   4798 N  ND1 . HIS   B 1 242 ? -22.508 21.715  -48.839 1.00 42.50 ? 683  HIS   B ND1 1 
ATOM   4799 C  CD2 . HIS   B 1 242 ? -21.665 22.512  -50.689 1.00 44.05 ? 683  HIS   B CD2 1 
ATOM   4800 C  CE1 . HIS   B 1 242 ? -23.051 22.903  -49.036 1.00 38.56 ? 683  HIS   B CE1 1 
ATOM   4801 N  NE2 . HIS   B 1 242 ? -22.553 23.409  -50.150 1.00 45.71 ? 683  HIS   B NE2 1 
ATOM   4802 N  N   . HIS   B 1 243 ? -22.090 19.018  -52.648 1.00 19.05 ? 684  HIS   B N   1 
ATOM   4803 C  CA  . HIS   B 1 243 ? -22.843 19.338  -53.860 1.00 20.49 ? 684  HIS   B CA  1 
ATOM   4804 C  C   . HIS   B 1 243 ? -23.643 18.166  -54.413 1.00 34.90 ? 684  HIS   B C   1 
ATOM   4805 O  O   . HIS   B 1 243 ? -24.667 18.389  -55.073 1.00 25.61 ? 684  HIS   B O   1 
ATOM   4806 C  CB  . HIS   B 1 243 ? -21.899 19.815  -54.966 1.00 21.13 ? 684  HIS   B CB  1 
ATOM   4807 C  CG  . HIS   B 1 243 ? -21.173 21.086  -54.647 1.00 34.89 ? 684  HIS   B CG  1 
ATOM   4808 N  ND1 . HIS   B 1 243 ? -21.818 22.295  -54.499 1.00 41.80 ? 684  HIS   B ND1 1 
ATOM   4809 C  CD2 . HIS   B 1 243 ? -19.853 21.338  -54.469 1.00 33.29 ? 684  HIS   B CD2 1 
ATOM   4810 C  CE1 . HIS   B 1 243 ? -20.928 23.235  -54.234 1.00 35.64 ? 684  HIS   B CE1 1 
ATOM   4811 N  NE2 . HIS   B 1 243 ? -19.728 22.682  -54.210 1.00 32.73 ? 684  HIS   B NE2 1 
ATOM   4812 N  N   . LEU   B 1 244 ? -23.204 16.924  -54.178 1.00 24.68 ? 685  LEU   B N   1 
ATOM   4813 C  CA  . LEU   B 1 244 ? -23.812 15.757  -54.817 1.00 20.42 ? 685  LEU   B CA  1 
ATOM   4814 C  C   . LEU   B 1 244 ? -24.336 14.747  -53.807 1.00 21.39 ? 685  LEU   B C   1 
ATOM   4815 O  O   . LEU   B 1 244 ? -25.542 14.506  -53.765 1.00 20.15 ? 685  LEU   B O   1 
ATOM   4816 C  CB  . LEU   B 1 244 ? -22.850 15.102  -55.806 1.00 20.15 ? 685  LEU   B CB  1 
ATOM   4817 C  CG  . LEU   B 1 244 ? -22.522 15.952  -57.022 1.00 21.47 ? 685  LEU   B CG  1 
ATOM   4818 C  CD1 . LEU   B 1 244 ? -21.271 15.446  -57.718 1.00 21.45 ? 685  LEU   B CD1 1 
ATOM   4819 C  CD2 . LEU   B 1 244 ? -23.731 15.947  -57.962 1.00 22.83 ? 685  LEU   B CD2 1 
ATOM   4820 N  N   . VAL   B 1 245 ? -23.462 14.121  -53.006 1.00 17.84 ? 686  VAL   B N   1 
ATOM   4821 C  CA  . VAL   B 1 245 ? -23.883 12.965  -52.221 1.00 19.56 ? 686  VAL   B CA  1 
ATOM   4822 C  C   . VAL   B 1 245 ? -24.978 13.352  -51.242 1.00 17.10 ? 686  VAL   B C   1 
ATOM   4823 O  O   . VAL   B 1 245 ? -26.019 12.692  -51.151 1.00 17.51 ? 686  VAL   B O   1 
ATOM   4824 C  CB  . VAL   B 1 245 ? -22.685 12.335  -51.488 1.00 17.23 ? 686  VAL   B CB  1 
ATOM   4825 C  CG1 . VAL   B 1 245 ? -23.137 11.093  -50.740 1.00 16.38 ? 686  VAL   B CG1 1 
ATOM   4826 C  CG2 . VAL   B 1 245 ? -21.595 12.009  -52.445 1.00 18.37 ? 686  VAL   B CG2 1 
ATOM   4827 N  N   . MET   B 1 246 ? -24.756 14.412  -50.489 1.00 18.41 ? 687  MET   B N   1 
ATOM   4828 C  CA  . MET   B 1 246 ? -25.718 14.712  -49.433 1.00 17.23 ? 687  MET   B CA  1 
ATOM   4829 C  C   . MET   B 1 246 ? -27.042 15.260  -49.968 1.00 20.80 ? 687  MET   B C   1 
ATOM   4830 O  O   . MET   B 1 246 ? -28.095 14.827  -49.491 1.00 20.67 ? 687  MET   B O   1 
ATOM   4831 C  CB  . MET   B 1 246 ? -25.129 15.574  -48.307 1.00 20.42 ? 687  MET   B CB  1 
ATOM   4832 C  CG  . MET   B 1 246 ? -23.982 14.884  -47.537 1.00 19.55 ? 687  MET   B CG  1 
ATOM   4833 S  SD  . MET   B 1 246 ? -24.471 13.311  -46.823 1.00 19.43 ? 687  MET   B SD  1 
ATOM   4834 C  CE  . MET   B 1 246 ? -25.708 13.863  -45.657 1.00 19.93 ? 687  MET   B CE  1 
ATOM   4835 N  N   . PRO   B 1 247 ? -27.045 16.184  -50.942 1.00 21.20 ? 688  PRO   B N   1 
ATOM   4836 C  CA  . PRO   B 1 247 ? -28.346 16.607  -51.508 1.00 22.55 ? 688  PRO   B CA  1 
ATOM   4837 C  C   . PRO   B 1 247 ? -29.153 15.460  -52.100 1.00 25.00 ? 688  PRO   B C   1 
ATOM   4838 O  O   . PRO   B 1 247 ? -30.355 15.354  -51.829 1.00 22.71 ? 688  PRO   B O   1 
ATOM   4839 C  CB  . PRO   B 1 247 ? -27.958 17.678  -52.537 1.00 25.07 ? 688  PRO   B CB  1 
ATOM   4840 C  CG  . PRO   B 1 247 ? -26.641 18.183  -52.084 1.00 28.58 ? 688  PRO   B CG  1 
ATOM   4841 C  CD  . PRO   B 1 247 ? -25.936 16.994  -51.474 1.00 21.41 ? 688  PRO   B CD  1 
ATOM   4842 N  N   . ILE   B 1 248 ? -28.521 14.582  -52.887 1.00 22.16 ? 689  ILE   B N   1 
ATOM   4843 C  CA  . ILE   B 1 248 ? -29.242 13.459  -53.488 1.00 20.10 ? 689  ILE   B CA  1 
ATOM   4844 C  C   . ILE   B 1 248 ? -29.749 12.502  -52.414 1.00 20.27 ? 689  ILE   B C   1 
ATOM   4845 O  O   . ILE   B 1 248 ? -30.916 12.094  -52.416 1.00 21.96 ? 689  ILE   B O   1 
ATOM   4846 C  CB  . ILE   B 1 248 ? -28.362 12.746  -54.532 1.00 18.67 ? 689  ILE   B CB  1 
ATOM   4847 C  CG1 . ILE   B 1 248 ? -28.031 13.683  -55.697 1.00 19.72 ? 689  ILE   B CG1 1 
ATOM   4848 C  CG2 . ILE   B 1 248 ? -29.027 11.454  -54.994 1.00 18.91 ? 689  ILE   B CG2 1 
ATOM   4849 C  CD1 . ILE   B 1 248 ? -26.995 13.142  -56.664 1.00 22.77 ? 689  ILE   B CD1 1 
ATOM   4850 N  N   . ALA   B 1 249 ? -28.876 12.133  -51.469 1.00 20.29 ? 690  ALA   B N   1 
ATOM   4851 C  CA  . ALA   B 1 249 ? -29.249 11.197  -50.413 1.00 18.21 ? 690  ALA   B CA  1 
ATOM   4852 C  C   . ALA   B 1 249 ? -30.427 11.710  -49.584 1.00 20.49 ? 690  ALA   B C   1 
ATOM   4853 O  O   . ALA   B 1 249 ? -31.332 10.941  -49.231 1.00 19.66 ? 690  ALA   B O   1 
ATOM   4854 C  CB  . ALA   B 1 249 ? -28.035 10.911  -49.515 1.00 16.97 ? 690  ALA   B CB  1 
ATOM   4855 N  N   . ARG   B 1 250 ? -30.423 13.000  -49.243 1.00 20.95 ? 691  ARG   B N   1 
ATOM   4856 C  CA  . ARG   B 1 250 ? -31.508 13.542  -48.429 1.00 23.52 ? 691  ARG   B CA  1 
ATOM   4857 C  C   . ARG   B 1 250 ? -32.830 13.477  -49.177 1.00 26.89 ? 691  ARG   B C   1 
ATOM   4858 O  O   . ARG   B 1 250 ? -33.874 13.180  -48.585 1.00 28.01 ? 691  ARG   B O   1 
ATOM   4859 C  CB  . ARG   B 1 250 ? -31.195 14.985  -48.046 1.00 20.97 ? 691  ARG   B CB  1 
ATOM   4860 C  CG  . ARG   B 1 250 ? -30.269 15.108  -46.846 1.00 25.41 ? 691  ARG   B CG  1 
ATOM   4861 C  CD  . ARG   B 1 250 ? -30.159 16.557  -46.381 1.00 34.76 ? 691  ARG   B CD  1 
ATOM   4862 N  NE  . ARG   B 1 250 ? -29.467 17.392  -47.357 1.00 36.93 ? 691  ARG   B NE  1 
ATOM   4863 C  CZ  . ARG   B 1 250 ? -28.202 17.787  -47.251 1.00 38.55 ? 691  ARG   B CZ  1 
ATOM   4864 N  NH1 . ARG   B 1 250 ? -27.477 17.429  -46.195 1.00 36.71 ? 691  ARG   B NH1 1 
ATOM   4865 N  NH2 . ARG   B 1 250 ? -27.665 18.544  -48.202 1.00 30.36 ? 691  ARG   B NH2 1 
ATOM   4866 N  N   . GLU   B 1 251 ? -32.799 13.748  -50.480 1.00 22.94 ? 692  GLU   B N   1 
ATOM   4867 C  CA  . GLU   B 1 251 ? -34.017 13.668  -51.279 1.00 19.92 ? 692  GLU   B CA  1 
ATOM   4868 C  C   . GLU   B 1 251 ? -34.496 12.231  -51.395 1.00 24.52 ? 692  GLU   B C   1 
ATOM   4869 O  O   . GLU   B 1 251 ? -35.700 11.963  -51.331 1.00 29.31 ? 692  GLU   B O   1 
ATOM   4870 C  CB  . GLU   B 1 251 ? -33.758 14.271  -52.655 1.00 22.90 ? 692  GLU   B CB  1 
ATOM   4871 C  CG  . GLU   B 1 251 ? -35.017 14.410  -53.493 1.00 24.48 ? 692  GLU   B CG  1 
ATOM   4872 C  CD  . GLU   B 1 251 ? -34.813 15.217  -54.769 1.00 32.90 ? 692  GLU   B CD  1 
ATOM   4873 O  OE1 . GLU   B 1 251 ? -33.740 15.835  -54.953 1.00 30.98 ? 692  GLU   B OE1 1 
ATOM   4874 O  OE2 . GLU   B 1 251 ? -35.749 15.238  -55.597 1.00 39.08 ? 692  GLU   B OE2 1 
ATOM   4875 N  N   . PHE   B 1 252 ? -33.559 11.288  -51.558 1.00 21.03 ? 693  PHE   B N   1 
ATOM   4876 C  CA  . PHE   B 1 252 ? -33.903 9.872   -51.554 1.00 19.47 ? 693  PHE   B CA  1 
ATOM   4877 C  C   . PHE   B 1 252 ? -34.494 9.448   -50.214 1.00 23.21 ? 693  PHE   B C   1 
ATOM   4878 O  O   . PHE   B 1 252 ? -35.364 8.571   -50.173 1.00 22.91 ? 693  PHE   B O   1 
ATOM   4879 C  CB  . PHE   B 1 252 ? -32.648 9.056   -51.914 1.00 18.82 ? 693  PHE   B CB  1 
ATOM   4880 C  CG  . PHE   B 1 252 ? -32.848 7.557   -51.943 1.00 16.28 ? 693  PHE   B CG  1 
ATOM   4881 C  CD1 . PHE   B 1 252 ? -33.597 6.935   -52.940 1.00 19.05 ? 693  PHE   B CD1 1 
ATOM   4882 C  CD2 . PHE   B 1 252 ? -32.225 6.752   -51.004 1.00 18.19 ? 693  PHE   B CD2 1 
ATOM   4883 C  CE1 . PHE   B 1 252 ? -33.739 5.538   -52.946 1.00 19.33 ? 693  PHE   B CE1 1 
ATOM   4884 C  CE2 . PHE   B 1 252 ? -32.378 5.379   -50.999 1.00 16.48 ? 693  PHE   B CE2 1 
ATOM   4885 C  CZ  . PHE   B 1 252 ? -33.122 4.763   -51.975 1.00 18.89 ? 693  PHE   B CZ  1 
ATOM   4886 N  N   . ALA   B 1 253 ? -34.027 10.049  -49.101 1.00 18.69 ? 694  ALA   B N   1 
ATOM   4887 C  CA  . ALA   B 1 253 ? -34.503 9.731   -47.756 1.00 19.13 ? 694  ALA   B CA  1 
ATOM   4888 C  C   . ALA   B 1 253 ? -34.382 8.237   -47.471 1.00 19.42 ? 694  ALA   B C   1 
ATOM   4889 O  O   . ALA   B 1 253 ? -35.391 7.539   -47.323 1.00 21.36 ? 694  ALA   B O   1 
ATOM   4890 C  CB  . ALA   B 1 253 ? -35.955 10.190  -47.580 1.00 23.95 ? 694  ALA   B CB  1 
ATOM   4891 N  N   . PRO   B 1 254 ? -33.163 7.699   -47.396 1.00 16.67 ? 695  PRO   B N   1 
ATOM   4892 C  CA  . PRO   B 1 254 ? -33.017 6.256   -47.184 1.00 15.76 ? 695  PRO   B CA  1 
ATOM   4893 C  C   . PRO   B 1 254 ? -33.494 5.857   -45.806 1.00 20.34 ? 695  PRO   B C   1 
ATOM   4894 O  O   . PRO   B 1 254 ? -33.496 6.652   -44.863 1.00 19.78 ? 695  PRO   B O   1 
ATOM   4895 C  CB  . PRO   B 1 254 ? -31.500 6.030   -47.294 1.00 15.96 ? 695  PRO   B CB  1 
ATOM   4896 C  CG  . PRO   B 1 254 ? -30.895 7.365   -46.943 1.00 19.78 ? 695  PRO   B CG  1 
ATOM   4897 C  CD  . PRO   B 1 254 ? -31.868 8.397   -47.460 1.00 24.11 ? 695  PRO   B CD  1 
ATOM   4898 N  N   . GLU   B 1 255 ? -33.885 4.594   -45.694 1.00 19.72 ? 696  GLU   B N   1 
ATOM   4899 C  CA  . GLU   B 1 255 ? -34.211 3.996   -44.414 1.00 22.22 ? 696  GLU   B CA  1 
ATOM   4900 C  C   . GLU   B 1 255 ? -33.049 3.206   -43.828 1.00 19.16 ? 696  GLU   B C   1 
ATOM   4901 O  O   . GLU   B 1 255 ? -33.098 2.835   -42.652 1.00 19.32 ? 696  GLU   B O   1 
ATOM   4902 C  CB  . GLU   B 1 255 ? -35.461 3.109   -44.546 1.00 18.93 ? 696  GLU   B CB  1 
ATOM   4903 C  CG  . GLU   B 1 255 ? -36.722 3.920   -44.938 1.00 22.28 ? 696  GLU   B CG  1 
ATOM   4904 C  CD  . GLU   B 1 255 ? -37.847 3.054   -45.475 1.00 48.39 ? 696  GLU   B CD  1 
ATOM   4905 O  OE1 . GLU   B 1 255 ? -37.755 2.614   -46.636 1.00 23.43 ? 696  GLU   B OE1 1 
ATOM   4906 O  OE2 . GLU   B 1 255 ? -38.829 2.816   -44.741 1.00 38.65 ? 696  GLU   B OE2 1 
ATOM   4907 N  N   . LEU   B 1 256 ? -32.022 2.935   -44.631 1.00 15.35 ? 697  LEU   B N   1 
ATOM   4908 C  CA  . LEU   B 1 256 ? -30.806 2.273   -44.181 1.00 15.49 ? 697  LEU   B CA  1 
ATOM   4909 C  C   . LEU   B 1 256 ? -29.682 2.756   -45.077 1.00 14.80 ? 697  LEU   B C   1 
ATOM   4910 O  O   . LEU   B 1 256 ? -29.870 2.893   -46.291 1.00 14.88 ? 697  LEU   B O   1 
ATOM   4911 C  CB  . LEU   B 1 256 ? -30.935 0.754   -44.307 1.00 15.67 ? 697  LEU   B CB  1 
ATOM   4912 C  CG  . LEU   B 1 256 ? -29.709 -0.099  -43.966 1.00 15.66 ? 697  LEU   B CG  1 
ATOM   4913 C  CD1 . LEU   B 1 256 ? -29.340 0.067   -42.505 1.00 18.83 ? 697  LEU   B CD1 1 
ATOM   4914 C  CD2 . LEU   B 1 256 ? -29.940 -1.553  -44.268 1.00 16.18 ? 697  LEU   B CD2 1 
ATOM   4915 N  N   . VAL   B 1 257 ? -28.521 3.035   -44.480 1.00 14.52 ? 698  VAL   B N   1 
ATOM   4916 C  CA  . VAL   B 1 257 ? -27.331 3.419   -45.234 1.00 13.85 ? 698  VAL   B CA  1 
ATOM   4917 C  C   . VAL   B 1 257 ? -26.273 2.337   -45.068 1.00 12.75 ? 698  VAL   B C   1 
ATOM   4918 O  O   . VAL   B 1 257 ? -25.906 1.980   -43.935 1.00 14.52 ? 698  VAL   B O   1 
ATOM   4919 C  CB  . VAL   B 1 257 ? -26.749 4.766   -44.776 1.00 14.41 ? 698  VAL   B CB  1 
ATOM   4920 C  CG1 . VAL   B 1 257 ? -25.482 5.099   -45.592 1.00 17.22 ? 698  VAL   B CG1 1 
ATOM   4921 C  CG2 . VAL   B 1 257 ? -27.789 5.872   -44.895 1.00 16.60 ? 698  VAL   B CG2 1 
ATOM   4922 N  N   . LEU   B 1 258 ? -25.757 1.849   -46.197 1.00 12.15 ? 699  LEU   B N   1 
ATOM   4923 C  CA  . LEU   B 1 258 ? -24.596 0.968   -46.205 1.00 11.81 ? 699  LEU   B CA  1 
ATOM   4924 C  C   . LEU   B 1 258 ? -23.446 1.738   -46.808 1.00 14.44 ? 699  LEU   B C   1 
ATOM   4925 O  O   . LEU   B 1 258 ? -23.607 2.408   -47.834 1.00 13.11 ? 699  LEU   B O   1 
ATOM   4926 C  CB  . LEU   B 1 258 ? -24.869 -0.259  -47.072 1.00 16.11 ? 699  LEU   B CB  1 
ATOM   4927 C  CG  . LEU   B 1 258 ? -26.131 -1.063  -46.756 1.00 13.88 ? 699  LEU   B CG  1 
ATOM   4928 C  CD1 . LEU   B 1 258 ? -26.233 -2.288  -47.640 1.00 16.10 ? 699  LEU   B CD1 1 
ATOM   4929 C  CD2 . LEU   B 1 258 ? -26.102 -1.460  -45.274 1.00 15.96 ? 699  LEU   B CD2 1 
ATOM   4930 N  N   . VAL   B 1 259 ? -22.287 1.659   -46.165 1.00 12.13 ? 700  VAL   B N   1 
ATOM   4931 C  CA  . VAL   B 1 259 ? -21.079 2.229   -46.753 1.00 14.34 ? 700  VAL   B CA  1 
ATOM   4932 C  C   . VAL   B 1 259 ? -20.189 1.109   -47.274 1.00 12.38 ? 700  VAL   B C   1 
ATOM   4933 O  O   . VAL   B 1 259 ? -19.774 0.243   -46.497 1.00 11.82 ? 700  VAL   B O   1 
ATOM   4934 C  CB  . VAL   B 1 259 ? -20.315 3.128   -45.773 1.00 13.27 ? 700  VAL   B CB  1 
ATOM   4935 C  CG1 . VAL   B 1 259 ? -19.210 3.874   -46.540 1.00 11.94 ? 700  VAL   B CG1 1 
ATOM   4936 C  CG2 . VAL   B 1 259 ? -21.282 4.102   -45.068 1.00 15.25 ? 700  VAL   B CG2 1 
ATOM   4937 N  N   . SER   B 1 260 ? -19.933 1.111   -48.579 1.00 13.07 ? 701  SER   B N   1 
ATOM   4938 C  CA  . SER   B 1 260 ? -18.862 0.280   -49.126 1.00 12.63 ? 701  SER   B CA  1 
ATOM   4939 C  C   . SER   B 1 260 ? -17.581 1.052   -48.854 1.00 10.80 ? 701  SER   B C   1 
ATOM   4940 O  O   . SER   B 1 260 ? -17.132 1.896   -49.644 1.00 12.31 ? 701  SER   B O   1 
ATOM   4941 C  CB  . SER   B 1 260 ? -19.091 0.016   -50.608 1.00 12.87 ? 701  SER   B CB  1 
ATOM   4942 O  OG  . SER   B 1 260 ? -19.832 -1.180  -50.814 1.00 14.01 ? 701  SER   B OG  1 
ATOM   4943 N  N   . ALA   B 1 261 ? -17.032 0.781   -47.670 1.00 11.33 ? 702  ALA   B N   1 
ATOM   4944 C  CA  . ALA   B 1 261 ? -15.959 1.585   -47.090 1.00 11.10 ? 702  ALA   B CA  1 
ATOM   4945 C  C   . ALA   B 1 261 ? -14.618 0.924   -47.388 1.00 13.19 ? 702  ALA   B C   1 
ATOM   4946 O  O   . ALA   B 1 261 ? -13.991 0.285   -46.533 1.00 11.33 ? 702  ALA   B O   1 
ATOM   4947 C  CB  . ALA   B 1 261 ? -16.212 1.765   -45.600 1.00 12.99 ? 702  ALA   B CB  1 
ATOM   4948 N  N   . GLY   B 1 262 ? -14.154 1.187   -48.600 1.00 12.73 ? 703  GLY   B N   1 
ATOM   4949 C  CA  . GLY   B 1 262 ? -12.762 0.841   -48.882 1.00 12.38 ? 703  GLY   B CA  1 
ATOM   4950 C  C   . GLY   B 1 262 ? -11.931 1.996   -48.352 1.00 13.33 ? 703  GLY   B C   1 
ATOM   4951 O  O   . GLY   B 1 262 ? -12.436 3.113   -48.293 1.00 14.52 ? 703  GLY   B O   1 
ATOM   4952 N  N   . PHE   B 1 263 ? -10.688 1.734   -47.984 1.00 10.50 ? 704  PHE   B N   1 
ATOM   4953 C  CA  . PHE   B 1 263 ? -9.781  2.834   -47.533 1.00 12.27 ? 704  PHE   B CA  1 
ATOM   4954 C  C   . PHE   B 1 263 ? -8.556  2.902   -48.442 1.00 13.72 ? 704  PHE   B C   1 
ATOM   4955 O  O   . PHE   B 1 263 ? -7.482  3.264   -48.006 1.00 13.24 ? 704  PHE   B O   1 
ATOM   4956 C  CB  . PHE   B 1 263 ? -9.451  2.653   -46.054 1.00 13.30 ? 704  PHE   B CB  1 
ATOM   4957 C  CG  . PHE   B 1 263 ? -10.704 2.772   -45.199 1.00 9.60  ? 704  PHE   B CG  1 
ATOM   4958 C  CD1 . PHE   B 1 263 ? -11.217 4.020   -44.872 1.00 12.49 ? 704  PHE   B CD1 1 
ATOM   4959 C  CD2 . PHE   B 1 263 ? -11.381 1.643   -44.753 1.00 10.66 ? 704  PHE   B CD2 1 
ATOM   4960 C  CE1 . PHE   B 1 263 ? -12.367 4.137   -44.109 1.00 13.84 ? 704  PHE   B CE1 1 
ATOM   4961 C  CE2 . PHE   B 1 263 ? -12.534 1.766   -43.993 1.00 12.30 ? 704  PHE   B CE2 1 
ATOM   4962 C  CZ  . PHE   B 1 263 ? -13.025 3.009   -43.677 1.00 12.79 ? 704  PHE   B CZ  1 
ATOM   4963 N  N   . ASP   B 1 264 ? -8.774  2.599   -49.711 1.00 11.50 ? 705  ASP   B N   1 
ATOM   4964 C  CA  . ASP   B 1 264 ? -7.691  2.706   -50.728 1.00 11.92 ? 705  ASP   B CA  1 
ATOM   4965 C  C   . ASP   B 1 264 ? -7.589  4.127   -51.307 1.00 13.56 ? 705  ASP   B C   1 
ATOM   4966 O  O   . ASP   B 1 264 ? -6.673  4.342   -52.085 1.00 13.47 ? 705  ASP   B O   1 
ATOM   4967 C  CB  . ASP   B 1 264 ? -7.783  1.611   -51.784 1.00 13.19 ? 705  ASP   B CB  1 
ATOM   4968 C  CG  . ASP   B 1 264 ? -9.177  1.192   -52.227 1.00 13.03 ? 705  ASP   B CG  1 
ATOM   4969 O  OD1 . ASP   B 1 264 ? -10.125 1.931   -51.948 1.00 14.54 ? 705  ASP   B OD1 1 
ATOM   4970 O  OD2 . ASP   B 1 264 ? -9.294  0.127   -52.857 1.00 14.23 ? 705  ASP   B OD2 1 
ATOM   4971 N  N   . ALA   B 1 265 ? -8.507  5.031   -50.987 1.00 12.53 ? 706  ALA   B N   1 
ATOM   4972 C  CA  . ALA   B 1 265 ? -8.321  6.443   -51.399 1.00 12.40 ? 706  ALA   B CA  1 
ATOM   4973 C  C   . ALA   B 1 265 ? -7.501  7.152   -50.317 1.00 11.94 ? 706  ALA   B C   1 
ATOM   4974 O  O   . ALA   B 1 265 ? -7.290  8.351   -50.425 1.00 15.32 ? 706  ALA   B O   1 
ATOM   4975 C  CB  . ALA   B 1 265 ? -9.653  7.123   -51.609 1.00 15.16 ? 706  ALA   B CB  1 
ATOM   4976 N  N   . ALA   B 1 266 ? -7.040  6.406   -49.316 1.00 12.70 ? 707  ALA   B N   1 
ATOM   4977 C  CA  . ALA   B 1 266 ? -6.384  7.037   -48.184 1.00 14.21 ? 707  ALA   B CA  1 
ATOM   4978 C  C   . ALA   B 1 266 ? -4.957  7.435   -48.508 1.00 14.32 ? 707  ALA   B C   1 
ATOM   4979 O  O   . ALA   B 1 266 ? -4.262  6.778   -49.288 1.00 13.94 ? 707  ALA   B O   1 
ATOM   4980 C  CB  . ALA   B 1 266 ? -6.304  6.048   -47.028 1.00 12.79 ? 707  ALA   B CB  1 
ATOM   4981 N  N   A ARG   B 1 267 ? -4.522  8.523   -47.879 0.52 14.29 ? 708  ARG   B N   1 
ATOM   4982 N  N   B ARG   B 1 267 ? -4.512  8.517   -47.874 0.48 14.76 ? 708  ARG   B N   1 
ATOM   4983 C  CA  A ARG   B 1 267 ? -3.104  8.844   -47.814 0.52 15.63 ? 708  ARG   B CA  1 
ATOM   4984 C  CA  B ARG   B 1 267 ? -3.098  8.861   -47.903 0.48 15.36 ? 708  ARG   B CA  1 
ATOM   4985 C  C   A ARG   B 1 267 ? -2.305  7.599   -47.452 0.52 14.37 ? 708  ARG   B C   1 
ATOM   4986 C  C   B ARG   B 1 267 ? -2.268  7.671   -47.440 0.48 14.82 ? 708  ARG   B C   1 
ATOM   4987 O  O   A ARG   B 1 267 ? -2.609  6.913   -46.475 0.52 11.09 ? 708  ARG   B O   1 
ATOM   4988 O  O   B ARG   B 1 267 ? -2.513  7.100   -46.375 0.48 22.09 ? 708  ARG   B O   1 
ATOM   4989 C  CB  A ARG   B 1 267 ? -2.916  9.914   -46.741 0.52 17.03 ? 708  ARG   B CB  1 
ATOM   4990 C  CB  B ARG   B 1 267 ? -2.854  10.065  -46.996 0.48 15.81 ? 708  ARG   B CB  1 
ATOM   4991 C  CG  A ARG   B 1 267 ? -1.503  10.468  -46.622 0.52 18.59 ? 708  ARG   B CG  1 
ATOM   4992 C  CG  B ARG   B 1 267 ? -1.441  10.644  -47.073 0.48 16.48 ? 708  ARG   B CG  1 
ATOM   4993 C  CD  A ARG   B 1 267 ? -1.412  11.420  -45.427 0.52 16.69 ? 708  ARG   B CD  1 
ATOM   4994 C  CD  B ARG   B 1 267 ? -1.307  11.919  -46.229 0.48 18.22 ? 708  ARG   B CD  1 
ATOM   4995 N  NE  A ARG   B 1 267 ? -1.729  10.709  -44.194 0.52 22.97 ? 708  ARG   B NE  1 
ATOM   4996 N  NE  B ARG   B 1 267 ? -1.767  13.106  -46.949 0.48 26.65 ? 708  ARG   B NE  1 
ATOM   4997 C  CZ  A ARG   B 1 267 ? -2.309  11.248  -43.130 0.52 18.56 ? 708  ARG   B CZ  1 
ATOM   4998 C  CZ  B ARG   B 1 267 ? -2.242  14.207  -46.368 0.48 26.23 ? 708  ARG   B CZ  1 
ATOM   4999 N  NH1 A ARG   B 1 267 ? -2.667  12.525  -43.127 0.52 19.08 ? 708  ARG   B NH1 1 
ATOM   5000 N  NH1 B ARG   B 1 267 ? -2.324  14.295  -45.045 0.48 18.78 ? 708  ARG   B NH1 1 
ATOM   5001 N  NH2 A ARG   B 1 267 ? -2.546  10.495  -42.067 0.52 25.20 ? 708  ARG   B NH2 1 
ATOM   5002 N  NH2 B ARG   B 1 267 ? -2.636  15.225  -47.121 0.48 30.60 ? 708  ARG   B NH2 1 
ATOM   5003 N  N   . GLY   B 1 268 ? -1.300  7.286   -48.273 1.00 14.68 ? 709  GLY   B N   1 
ATOM   5004 C  CA  . GLY   B 1 268 ? -0.424  6.165   -48.018 1.00 13.91 ? 709  GLY   B CA  1 
ATOM   5005 C  C   . GLY   B 1 268 ? -0.757  4.879   -48.751 1.00 14.83 ? 709  GLY   B C   1 
ATOM   5006 O  O   . GLY   B 1 268 ? 0.060   3.949   -48.730 1.00 14.57 ? 709  GLY   B O   1 
ATOM   5007 N  N   . ASP   B 1 269 ? -1.939  4.770   -49.355 1.00 12.95 ? 710  ASP   B N   1 
ATOM   5008 C  CA  . ASP   B 1 269 ? -2.273  3.520   -50.016 1.00 13.70 ? 710  ASP   B CA  1 
ATOM   5009 C  C   . ASP   B 1 269 ? -1.328  3.240   -51.186 1.00 13.73 ? 710  ASP   B C   1 
ATOM   5010 O  O   . ASP   B 1 269 ? -1.027  4.142   -51.972 1.00 17.53 ? 710  ASP   B O   1 
ATOM   5011 C  CB  . ASP   B 1 269 ? -3.700  3.578   -50.540 1.00 13.99 ? 710  ASP   B CB  1 
ATOM   5012 C  CG  . ASP   B 1 269 ? -4.207  2.219   -50.977 1.00 13.91 ? 710  ASP   B CG  1 
ATOM   5013 O  OD1 . ASP   B 1 269 ? -4.691  1.482   -50.092 1.00 12.85 ? 710  ASP   B OD1 1 
ATOM   5014 O  OD2 . ASP   B 1 269 ? -4.115  1.874   -52.184 1.00 14.17 ? 710  ASP   B OD2 1 
ATOM   5015 N  N   . PRO   B 1 270 ? -0.905  1.987   -51.376 1.00 12.34 ? 711  PRO   B N   1 
ATOM   5016 C  CA  . PRO   B 1 270 ? 0.040   1.681   -52.467 1.00 14.20 ? 711  PRO   B CA  1 
ATOM   5017 C  C   . PRO   B 1 270 ? -0.583  1.634   -53.849 1.00 15.06 ? 711  PRO   B C   1 
ATOM   5018 O  O   . PRO   B 1 270 ? 0.164   1.630   -54.848 1.00 15.58 ? 711  PRO   B O   1 
ATOM   5019 C  CB  . PRO   B 1 270 ? 0.586   0.299   -52.081 1.00 15.31 ? 711  PRO   B CB  1 
ATOM   5020 C  CG  . PRO   B 1 270 ? -0.494  -0.312  -51.256 1.00 16.45 ? 711  PRO   B CG  1 
ATOM   5021 C  CD  . PRO   B 1 270 ? -1.071  0.837   -50.467 1.00 12.99 ? 711  PRO   B CD  1 
ATOM   5022 N  N   . LEU   B 1 271 ? -1.908  1.632   -53.953 1.00 15.46 ? 712  LEU   B N   1 
ATOM   5023 C  CA  . LEU   B 1 271 ? -2.602  1.522   -55.235 1.00 14.82 ? 712  LEU   B CA  1 
ATOM   5024 C  C   . LEU   B 1 271 ? -3.451  2.732   -55.594 1.00 17.54 ? 712  LEU   B C   1 
ATOM   5025 O  O   . LEU   B 1 271 ? -3.544  3.080   -56.776 1.00 18.33 ? 712  LEU   B O   1 
ATOM   5026 C  CB  . LEU   B 1 271 ? -3.489  0.264   -55.262 1.00 17.82 ? 712  LEU   B CB  1 
ATOM   5027 C  CG  . LEU   B 1 271 ? -2.803  -1.073  -54.985 1.00 18.14 ? 712  LEU   B CG  1 
ATOM   5028 C  CD1 . LEU   B 1 271 ? -3.813  -2.210  -55.053 1.00 19.94 ? 712  LEU   B CD1 1 
ATOM   5029 C  CD2 . LEU   B 1 271 ? -1.681  -1.298  -55.980 1.00 30.67 ? 712  LEU   B CD2 1 
ATOM   5030 N  N   . GLY   B 1 272 ? -4.104  3.370   -54.619 1.00 15.01 ? 713  GLY   B N   1 
ATOM   5031 C  CA  . GLY   B 1 272 ? -5.095  4.381   -54.959 1.00 16.41 ? 713  GLY   B CA  1 
ATOM   5032 C  C   . GLY   B 1 272 ? -4.504  5.681   -55.483 1.00 16.29 ? 713  GLY   B C   1 
ATOM   5033 O  O   . GLY   B 1 272 ? -5.112  6.344   -56.334 1.00 17.07 ? 713  GLY   B O   1 
ATOM   5034 N  N   . GLY   B 1 273 ? -3.343  6.081   -54.959 1.00 16.56 ? 714  GLY   B N   1 
ATOM   5035 C  CA  . GLY   B 1 273 ? -2.728  7.339   -55.351 1.00 20.81 ? 714  GLY   B CA  1 
ATOM   5036 C  C   . GLY   B 1 273 ? -3.415  8.600   -54.862 1.00 21.91 ? 714  GLY   B C   1 
ATOM   5037 O  O   . GLY   B 1 273 ? -3.127  9.684   -55.384 1.00 20.83 ? 714  GLY   B O   1 
ATOM   5038 N  N   . PHE   B 1 274 ? -4.318  8.503   -53.878 1.00 14.23 ? 715  PHE   B N   1 
ATOM   5039 C  CA  . PHE   B 1 274 ? -5.094  9.629   -53.370 1.00 16.42 ? 715  PHE   B CA  1 
ATOM   5040 C  C   . PHE   B 1 274 ? -4.642  9.961   -51.947 1.00 15.84 ? 715  PHE   B C   1 
ATOM   5041 O  O   . PHE   B 1 274 ? -3.741  9.324   -51.387 1.00 16.89 ? 715  PHE   B O   1 
ATOM   5042 C  CB  . PHE   B 1 274 ? -6.591  9.308   -53.417 1.00 15.24 ? 715  PHE   B CB  1 
ATOM   5043 C  CG  . PHE   B 1 274 ? -7.245  9.550   -54.763 1.00 16.60 ? 715  PHE   B CG  1 
ATOM   5044 C  CD1 . PHE   B 1 274 ? -6.503  9.814   -55.918 1.00 17.81 ? 715  PHE   B CD1 1 
ATOM   5045 C  CD2 . PHE   B 1 274 ? -8.624  9.516   -54.863 1.00 15.51 ? 715  PHE   B CD2 1 
ATOM   5046 C  CE1 . PHE   B 1 274 ? -7.143  10.050  -57.131 1.00 19.31 ? 715  PHE   B CE1 1 
ATOM   5047 C  CE2 . PHE   B 1 274 ? -9.266  9.721   -56.092 1.00 17.09 ? 715  PHE   B CE2 1 
ATOM   5048 C  CZ  . PHE   B 1 274 ? -8.509  10.004  -57.221 1.00 19.79 ? 715  PHE   B CZ  1 
ATOM   5049 N  N   . GLN   B 1 275 ? -5.281  10.963  -51.343 1.00 14.44 ? 716  GLN   B N   1 
ATOM   5050 C  CA  . GLN   B 1 275 ? -4.791  11.464  -50.061 1.00 17.84 ? 716  GLN   B CA  1 
ATOM   5051 C  C   . GLN   B 1 275 ? -5.914  11.838  -49.099 1.00 19.09 ? 716  GLN   B C   1 
ATOM   5052 O  O   . GLN   B 1 275 ? -5.786  12.787  -48.318 1.00 17.72 ? 716  GLN   B O   1 
ATOM   5053 C  CB  . GLN   B 1 275 ? -3.795  12.612  -50.233 1.00 21.07 ? 716  GLN   B CB  1 
ATOM   5054 C  CG  . GLN   B 1 275 ? -4.296  13.802  -51.018 1.00 30.36 ? 716  GLN   B CG  1 
ATOM   5055 C  CD  . GLN   B 1 275 ? -3.151  14.718  -51.442 1.00 54.47 ? 716  GLN   B CD  1 
ATOM   5056 O  OE1 . GLN   B 1 275 ? -2.188  14.902  -50.698 1.00 54.60 ? 716  GLN   B OE1 1 
ATOM   5057 N  NE2 . GLN   B 1 275 ? -3.256  15.299  -52.638 1.00 30.76 ? 716  GLN   B NE2 1 
ATOM   5058 N  N   . VAL   B 1 276 ? -7.020  11.087  -49.104 1.00 14.81 ? 717  VAL   B N   1 
ATOM   5059 C  CA  . VAL   B 1 276 ? -8.033  11.292  -48.075 1.00 14.42 ? 717  VAL   B CA  1 
ATOM   5060 C  C   . VAL   B 1 276 ? -7.428  10.948  -46.720 1.00 12.68 ? 717  VAL   B C   1 
ATOM   5061 O  O   . VAL   B 1 276 ? -6.748  9.923   -46.571 1.00 13.75 ? 717  VAL   B O   1 
ATOM   5062 C  CB  . VAL   B 1 276 ? -9.284  10.454  -48.379 1.00 13.35 ? 717  VAL   B CB  1 
ATOM   5063 C  CG1 . VAL   B 1 276 ? -10.346 10.712  -47.309 1.00 16.04 ? 717  VAL   B CG1 1 
ATOM   5064 C  CG2 . VAL   B 1 276 ? -9.838  10.782  -49.770 1.00 14.95 ? 717  VAL   B CG2 1 
ATOM   5065 N  N   . THR   B 1 277 ? -7.655  11.804  -45.723 1.00 12.89 ? 718  THR   B N   1 
ATOM   5066 C  CA  . THR   B 1 277 ? -7.036  11.605  -44.412 1.00 15.22 ? 718  THR   B CA  1 
ATOM   5067 C  C   . THR   B 1 277 ? -7.988  10.848  -43.497 1.00 13.58 ? 718  THR   B C   1 
ATOM   5068 O  O   . THR   B 1 277 ? -9.187  10.754  -43.770 1.00 14.74 ? 718  THR   B O   1 
ATOM   5069 C  CB  . THR   B 1 277 ? -6.705  12.957  -43.769 1.00 14.82 ? 718  THR   B CB  1 
ATOM   5070 O  OG1 . THR   B 1 277 ? -7.920  13.626  -43.397 1.00 15.56 ? 718  THR   B OG1 1 
ATOM   5071 C  CG2 . THR   B 1 277 ? -5.861  13.831  -44.693 1.00 18.30 ? 718  THR   B CG2 1 
ATOM   5072 N  N   . PRO   B 1 278 ? -7.509  10.350  -42.345 1.00 13.11 ? 719  PRO   B N   1 
ATOM   5073 C  CA  . PRO   B 1 278 ? -8.450  9.739   -41.393 1.00 14.14 ? 719  PRO   B CA  1 
ATOM   5074 C  C   . PRO   B 1 278 ? -9.528  10.704  -40.935 1.00 14.48 ? 719  PRO   B C   1 
ATOM   5075 O  O   . PRO   B 1 278 ? -10.699 10.317  -40.763 1.00 13.05 ? 719  PRO   B O   1 
ATOM   5076 C  CB  . PRO   B 1 278 ? -7.548  9.289   -40.232 1.00 14.34 ? 719  PRO   B CB  1 
ATOM   5077 C  CG  . PRO   B 1 278 ? -6.222  9.037   -40.904 1.00 14.35 ? 719  PRO   B CG  1 
ATOM   5078 C  CD  . PRO   B 1 278 ? -6.110  10.151  -41.925 1.00 15.28 ? 719  PRO   B CD  1 
ATOM   5079 N  N   . GLU   B 1 279 ? -9.164  11.971  -40.731 1.00 13.08 ? 720  GLU   B N   1 
ATOM   5080 C  CA  . GLU   B 1 279 ? -10.170 12.951  -40.341 1.00 14.04 ? 720  GLU   B CA  1 
ATOM   5081 C  C   . GLU   B 1 279 ? -11.141 13.245  -41.482 1.00 13.61 ? 720  GLU   B C   1 
ATOM   5082 O  O   . GLU   B 1 279 ? -12.325 13.501  -41.226 1.00 14.91 ? 720  GLU   B O   1 
ATOM   5083 C  CB  . GLU   B 1 279 ? -9.506  14.213  -39.777 1.00 17.02 ? 720  GLU   B CB  1 
ATOM   5084 C  CG  . GLU   B 1 279 ? -8.649  15.002  -40.751 1.00 24.72 ? 720  GLU   B CG  1 
ATOM   5085 C  CD  . GLU   B 1 279 ? -7.155  14.610  -40.759 1.00 30.33 ? 720  GLU   B CD  1 
ATOM   5086 O  OE1 . GLU   B 1 279 ? -6.775  13.491  -40.305 1.00 19.61 ? 720  GLU   B OE1 1 
ATOM   5087 O  OE2 . GLU   B 1 279 ? -6.360  15.445  -41.260 1.00 21.93 ? 720  GLU   B OE2 1 
ATOM   5088 N  N   . GLY   B 1 280 ? -10.673 13.176  -42.730 1.00 14.85 ? 721  GLY   B N   1 
ATOM   5089 C  CA  . GLY   B 1 280 ? -11.600 13.207  -43.855 1.00 14.82 ? 721  GLY   B CA  1 
ATOM   5090 C  C   . GLY   B 1 280 ? -12.651 12.109  -43.785 1.00 15.49 ? 721  GLY   B C   1 
ATOM   5091 O  O   . GLY   B 1 280 ? -13.857 12.373  -43.861 1.00 13.94 ? 721  GLY   B O   1 
ATOM   5092 N  N   . TYR   B 1 281 ? -12.214 10.854  -43.615 1.00 13.76 ? 722  TYR   B N   1 
ATOM   5093 C  CA  . TYR   B 1 281 ? -13.180 9.762   -43.518 1.00 12.43 ? 722  TYR   B CA  1 
ATOM   5094 C  C   . TYR   B 1 281 ? -14.120 9.952   -42.331 1.00 14.19 ? 722  TYR   B C   1 
ATOM   5095 O  O   . TYR   B 1 281 ? -15.312 9.619   -42.412 1.00 13.99 ? 722  TYR   B O   1 
ATOM   5096 C  CB  . TYR   B 1 281 ? -12.456 8.425   -43.400 1.00 13.30 ? 722  TYR   B CB  1 
ATOM   5097 C  CG  . TYR   B 1 281 ? -11.798 7.943   -44.678 1.00 13.40 ? 722  TYR   B CG  1 
ATOM   5098 C  CD1 . TYR   B 1 281 ? -12.569 7.505   -45.769 1.00 12.43 ? 722  TYR   B CD1 1 
ATOM   5099 C  CD2 . TYR   B 1 281 ? -10.401 7.909   -44.803 1.00 11.49 ? 722  TYR   B CD2 1 
ATOM   5100 C  CE1 . TYR   B 1 281 ? -11.962 7.066   -46.951 1.00 12.49 ? 722  TYR   B CE1 1 
ATOM   5101 C  CE2 . TYR   B 1 281 ? -9.802  7.458   -45.965 1.00 11.46 ? 722  TYR   B CE2 1 
ATOM   5102 C  CZ  . TYR   B 1 281 ? -10.574 7.037   -47.029 1.00 11.68 ? 722  TYR   B CZ  1 
ATOM   5103 O  OH  . TYR   B 1 281 ? -9.936  6.582   -48.145 1.00 13.23 ? 722  TYR   B OH  1 
ATOM   5104 N  N   . ALA   B 1 282 ? -13.601 10.471  -41.217 1.00 13.10 ? 723  ALA   B N   1 
ATOM   5105 C  CA  . ALA   B 1 282 ? -14.465 10.781  -40.069 1.00 12.33 ? 723  ALA   B CA  1 
ATOM   5106 C  C   . ALA   B 1 282 ? -15.568 11.776  -40.452 1.00 13.14 ? 723  ALA   B C   1 
ATOM   5107 O  O   . ALA   B 1 282 ? -16.745 11.573  -40.126 1.00 13.52 ? 723  ALA   B O   1 
ATOM   5108 C  CB  . ALA   B 1 282 ? -13.639 11.295  -38.885 1.00 13.04 ? 723  ALA   B CB  1 
ATOM   5109 N  N   . HIS   B 1 283 ? -15.212 12.833  -41.187 1.00 15.87 ? 724  HIS   B N   1 
ATOM   5110 C  CA  . HIS   B 1 283 ? -16.218 13.800  -41.621 1.00 15.71 ? 724  HIS   B CA  1 
ATOM   5111 C  C   . HIS   B 1 283 ? -17.225 13.181  -42.586 1.00 17.21 ? 724  HIS   B C   1 
ATOM   5112 O  O   . HIS   B 1 283 ? -18.421 13.492  -42.517 1.00 17.13 ? 724  HIS   B O   1 
ATOM   5113 C  CB  . HIS   B 1 283 ? -15.556 15.038  -42.209 1.00 19.84 ? 724  HIS   B CB  1 
ATOM   5114 C  CG  . HIS   B 1 283 ? -15.153 16.034  -41.168 1.00 16.92 ? 724  HIS   B CG  1 
ATOM   5115 N  ND1 . HIS   B 1 283 ? -15.954 17.099  -40.824 1.00 19.98 ? 724  HIS   B ND1 1 
ATOM   5116 C  CD2 . HIS   B 1 283 ? -14.066 16.104  -40.361 1.00 17.08 ? 724  HIS   B CD2 1 
ATOM   5117 C  CE1 . HIS   B 1 283 ? -15.369 17.792  -39.861 1.00 19.93 ? 724  HIS   B CE1 1 
ATOM   5118 N  NE2 . HIS   B 1 283 ? -14.221 17.212  -39.564 1.00 16.78 ? 724  HIS   B NE2 1 
ATOM   5119 N  N   . LEU   B 1 284 ? -16.771 12.316  -43.500 1.00 16.40 ? 725  LEU   B N   1 
ATOM   5120 C  CA  . LEU   B 1 284 ? -17.721 11.667  -44.403 1.00 15.27 ? 725  LEU   B CA  1 
ATOM   5121 C  C   . LEU   B 1 284 ? -18.687 10.785  -43.622 1.00 13.20 ? 725  LEU   B C   1 
ATOM   5122 O  O   . LEU   B 1 284 ? -19.901 10.818  -43.865 1.00 14.32 ? 725  LEU   B O   1 
ATOM   5123 C  CB  . LEU   B 1 284 ? -17.009 10.861  -45.494 1.00 14.81 ? 725  LEU   B CB  1 
ATOM   5124 C  CG  . LEU   B 1 284 ? -15.986 11.583  -46.356 1.00 15.16 ? 725  LEU   B CG  1 
ATOM   5125 C  CD1 . LEU   B 1 284 ? -15.445 10.593  -47.392 1.00 14.84 ? 725  LEU   B CD1 1 
ATOM   5126 C  CD2 . LEU   B 1 284 ? -16.589 12.828  -47.044 1.00 16.38 ? 725  LEU   B CD2 1 
ATOM   5127 N  N   . THR   B 1 285 ? -18.187 10.034  -42.632 1.00 14.85 ? 726  THR   B N   1 
ATOM   5128 C  CA  . THR   B 1 285 ? -19.058 9.219   -41.785 1.00 14.49 ? 726  THR   B CA  1 
ATOM   5129 C  C   . THR   B 1 285 ? -20.062 10.080  -41.033 1.00 14.90 ? 726  THR   B C   1 
ATOM   5130 O  O   . THR   B 1 285 ? -21.265 9.776   -41.010 1.00 14.51 ? 726  THR   B O   1 
ATOM   5131 C  CB  . THR   B 1 285 ? -18.218 8.426   -40.774 1.00 12.22 ? 726  THR   B CB  1 
ATOM   5132 O  OG1 . THR   B 1 285 ? -17.276 7.609   -41.484 1.00 12.99 ? 726  THR   B OG1 1 
ATOM   5133 C  CG2 . THR   B 1 285 ? -19.093 7.553   -39.869 1.00 13.96 ? 726  THR   B CG2 1 
ATOM   5134 N  N   . HIS   B 1 286 ? -19.577 11.146  -40.382 1.00 15.38 ? 727  HIS   B N   1 
ATOM   5135 C  CA  . HIS   B 1 286 ? -20.458 12.008  -39.604 1.00 14.85 ? 727  HIS   B CA  1 
ATOM   5136 C  C   . HIS   B 1 286 ? -21.574 12.575  -40.472 1.00 18.71 ? 727  HIS   B C   1 
ATOM   5137 O  O   . HIS   B 1 286 ? -22.721 12.682  -40.026 1.00 16.82 ? 727  HIS   B O   1 
ATOM   5138 C  CB  . HIS   B 1 286 ? -19.646 13.133  -38.975 1.00 16.77 ? 727  HIS   B CB  1 
ATOM   5139 C  CG  . HIS   B 1 286 ? -20.403 13.904  -37.944 1.00 18.75 ? 727  HIS   B CG  1 
ATOM   5140 N  ND1 . HIS   B 1 286 ? -20.966 15.133  -38.206 1.00 22.33 ? 727  HIS   B ND1 1 
ATOM   5141 C  CD2 . HIS   B 1 286 ? -20.690 13.618  -36.655 1.00 20.85 ? 727  HIS   B CD2 1 
ATOM   5142 C  CE1 . HIS   B 1 286 ? -21.567 15.576  -37.113 1.00 22.39 ? 727  HIS   B CE1 1 
ATOM   5143 N  NE2 . HIS   B 1 286 ? -21.423 14.672  -36.161 1.00 22.40 ? 727  HIS   B NE2 1 
ATOM   5144 N  N   . GLN   B 1 287 ? -21.262 12.947  -41.709 1.00 15.98 ? 728  GLN   B N   1 
ATOM   5145 C  CA  . GLN   B 1 287 ? -22.307 13.433  -42.604 1.00 16.10 ? 728  GLN   B CA  1 
ATOM   5146 C  C   . GLN   B 1 287 ? -23.336 12.349  -42.894 1.00 17.04 ? 728  GLN   B C   1 
ATOM   5147 O  O   . GLN   B 1 287 ? -24.548 12.610  -42.866 1.00 18.71 ? 728  GLN   B O   1 
ATOM   5148 C  CB  . GLN   B 1 287 ? -21.691 13.964  -43.886 1.00 16.41 ? 728  GLN   B CB  1 
ATOM   5149 C  CG  . GLN   B 1 287 ? -20.981 15.270  -43.679 1.00 16.75 ? 728  GLN   B CG  1 
ATOM   5150 C  CD  . GLN   B 1 287 ? -20.479 15.872  -44.965 1.00 26.26 ? 728  GLN   B CD  1 
ATOM   5151 O  OE1 . GLN   B 1 287 ? -21.224 16.013  -45.932 1.00 25.03 ? 728  GLN   B OE1 1 
ATOM   5152 N  NE2 . GLN   B 1 287 ? -19.207 16.235  -44.988 1.00 38.62 ? 728  GLN   B NE2 1 
ATOM   5153 N  N   . LEU   B 1 288 ? -22.882 11.126  -43.185 1.00 15.04 ? 729  LEU   B N   1 
ATOM   5154 C  CA  . LEU   B 1 288 ? -23.817 10.056  -43.490 1.00 17.05 ? 729  LEU   B CA  1 
ATOM   5155 C  C   . LEU   B 1 288 ? -24.697 9.726   -42.291 1.00 13.25 ? 729  LEU   B C   1 
ATOM   5156 O  O   . LEU   B 1 288 ? -25.845 9.304   -42.466 1.00 16.40 ? 729  LEU   B O   1 
ATOM   5157 C  CB  . LEU   B 1 288 ? -23.089 8.822   -44.033 1.00 14.53 ? 729  LEU   B CB  1 
ATOM   5158 C  CG  . LEU   B 1 288 ? -22.341 8.993   -45.351 1.00 15.75 ? 729  LEU   B CG  1 
ATOM   5159 C  CD1 . LEU   B 1 288 ? -21.679 7.675   -45.752 1.00 16.49 ? 729  LEU   B CD1 1 
ATOM   5160 C  CD2 . LEU   B 1 288 ? -23.301 9.479   -46.432 1.00 15.12 ? 729  LEU   B CD2 1 
ATOM   5161 N  N   . MET   B 1 289 ? -24.198 9.931   -41.067 1.00 14.48 ? 730  MET   B N   1 
ATOM   5162 C  CA  . MET   B 1 289 ? -24.969 9.672   -39.856 1.00 13.21 ? 730  MET   B CA  1 
ATOM   5163 C  C   . MET   B 1 289 ? -26.214 10.557  -39.735 1.00 14.94 ? 730  MET   B C   1 
ATOM   5164 O  O   . MET   B 1 289 ? -27.099 10.240  -38.933 1.00 18.92 ? 730  MET   B O   1 
ATOM   5165 C  CB  . MET   B 1 289 ? -24.068 9.829   -38.620 1.00 15.71 ? 730  MET   B CB  1 
ATOM   5166 C  CG  . MET   B 1 289 ? -23.075 8.698   -38.445 1.00 14.82 ? 730  MET   B CG  1 
ATOM   5167 S  SD  . MET   B 1 289 ? -21.895 9.051   -37.123 1.00 17.14 ? 730  MET   B SD  1 
ATOM   5168 C  CE  . MET   B 1 289 ? -22.998 9.095   -35.692 1.00 15.20 ? 730  MET   B CE  1 
ATOM   5169 N  N   . SER   B 1 290 ? -26.280 11.669  -40.466 1.00 19.28 ? 731  SER   B N   1 
ATOM   5170 C  CA  . SER   B 1 290 ? -27.476 12.514  -40.485 1.00 16.22 ? 731  SER   B CA  1 
ATOM   5171 C  C   . SER   B 1 290 ? -28.629 11.930  -41.303 1.00 25.53 ? 731  SER   B C   1 
ATOM   5172 O  O   . SER   B 1 290 ? -29.719 12.515  -41.299 1.00 22.69 ? 731  SER   B O   1 
ATOM   5173 C  CB  . SER   B 1 290 ? -27.124 13.915  -40.997 1.00 23.54 ? 731  SER   B CB  1 
ATOM   5174 O  OG  . SER   B 1 290 ? -26.872 13.952  -42.396 1.00 22.79 ? 731  SER   B OG  1 
ATOM   5175 N  N   . LEU   B 1 291 ? -28.429 10.805  -41.989 1.00 20.68 ? 732  LEU   B N   1 
ATOM   5176 C  CA  . LEU   B 1 291 ? -29.430 10.158  -42.829 1.00 16.88 ? 732  LEU   B CA  1 
ATOM   5177 C  C   . LEU   B 1 291 ? -30.000 8.940   -42.121 1.00 18.21 ? 732  LEU   B C   1 
ATOM   5178 O  O   . LEU   B 1 291 ? -29.394 8.385   -41.194 1.00 20.49 ? 732  LEU   B O   1 
ATOM   5179 C  CB  . LEU   B 1 291 ? -28.782 9.672   -44.128 1.00 21.25 ? 732  LEU   B CB  1 
ATOM   5180 C  CG  . LEU   B 1 291 ? -28.050 10.691  -44.974 1.00 17.87 ? 732  LEU   B CG  1 
ATOM   5181 C  CD1 . LEU   B 1 291 ? -27.169 10.022  -46.031 1.00 19.29 ? 732  LEU   B CD1 1 
ATOM   5182 C  CD2 . LEU   B 1 291 ? -29.085 11.600  -45.624 1.00 23.99 ? 732  LEU   B CD2 1 
ATOM   5183 N  N   . ALA   B 1 292 ? -31.190 8.516   -42.564 1.00 19.79 ? 733  ALA   B N   1 
ATOM   5184 C  CA  . ALA   B 1 292 ? -31.796 7.264   -42.094 1.00 19.74 ? 733  ALA   B CA  1 
ATOM   5185 C  C   . ALA   B 1 292 ? -31.853 7.162   -40.566 1.00 16.30 ? 733  ALA   B C   1 
ATOM   5186 O  O   . ALA   B 1 292 ? -31.744 6.071   -39.999 1.00 18.80 ? 733  ALA   B O   1 
ATOM   5187 C  CB  . ALA   B 1 292 ? -31.114 6.031   -42.703 1.00 17.37 ? 733  ALA   B CB  1 
ATOM   5188 N  N   . ALA   B 1 293 ? -32.077 8.293   -39.891 1.00 22.19 ? 734  ALA   B N   1 
ATOM   5189 C  CA  . ALA   B 1 293 ? -32.108 8.339   -38.425 1.00 23.00 ? 734  ALA   B CA  1 
ATOM   5190 C  C   . ALA   B 1 293 ? -30.866 7.702   -37.806 1.00 22.55 ? 734  ALA   B C   1 
ATOM   5191 O  O   . ALA   B 1 293 ? -30.920 7.098   -36.731 1.00 22.60 ? 734  ALA   B O   1 
ATOM   5192 C  CB  . ALA   B 1 293 ? -33.394 7.733   -37.862 1.00 24.88 ? 734  ALA   B CB  1 
ATOM   5193 N  N   . GLY   B 1 294 ? -29.745 7.806   -38.516 1.00 18.07 ? 735  GLY   B N   1 
ATOM   5194 C  CA  . GLY   B 1 294 ? -28.471 7.293   -38.050 1.00 20.19 ? 735  GLY   B CA  1 
ATOM   5195 C  C   . GLY   B 1 294 ? -28.223 5.821   -38.299 1.00 18.61 ? 735  GLY   B C   1 
ATOM   5196 O  O   . GLY   B 1 294 ? -27.202 5.296   -37.836 1.00 17.89 ? 735  GLY   B O   1 
ATOM   5197 N  N   . ARG   B 1 295 ? -29.108 5.135   -39.025 1.00 16.44 ? 736  ARG   B N   1 
ATOM   5198 C  CA  . ARG   B 1 295 ? -28.962 3.703   -39.284 1.00 15.19 ? 736  ARG   B CA  1 
ATOM   5199 C  C   . ARG   B 1 295 ? -27.948 3.499   -40.407 1.00 15.01 ? 736  ARG   B C   1 
ATOM   5200 O  O   . ARG   B 1 295 ? -28.295 3.441   -41.598 1.00 15.74 ? 736  ARG   B O   1 
ATOM   5201 C  CB  . ARG   B 1 295 ? -30.314 3.079   -39.616 1.00 14.56 ? 736  ARG   B CB  1 
ATOM   5202 C  CG  . ARG   B 1 295 ? -31.268 3.204   -38.426 1.00 19.24 ? 736  ARG   B CG  1 
ATOM   5203 C  CD  . ARG   B 1 295 ? -32.607 2.533   -38.690 1.00 21.50 ? 736  ARG   B CD  1 
ATOM   5204 N  NE  . ARG   B 1 295 ? -33.501 2.740   -37.554 1.00 64.01 ? 736  ARG   B NE  1 
ATOM   5205 C  CZ  . ARG   B 1 295 ? -34.461 3.660   -37.512 1.00 44.57 ? 736  ARG   B CZ  1 
ATOM   5206 N  NH1 . ARG   B 1 295 ? -34.666 4.459   -38.551 1.00 36.59 ? 736  ARG   B NH1 1 
ATOM   5207 N  NH2 . ARG   B 1 295 ? -35.216 3.779   -36.425 1.00 41.25 ? 736  ARG   B NH2 1 
ATOM   5208 N  N   . VAL   B 1 296 ? -26.670 3.373   -40.004 1.00 14.53 ? 737  VAL   B N   1 
ATOM   5209 C  CA  . VAL   B 1 296 ? -25.526 3.308   -40.909 1.00 15.43 ? 737  VAL   B CA  1 
ATOM   5210 C  C   . VAL   B 1 296 ? -24.716 2.061   -40.587 1.00 13.65 ? 737  VAL   B C   1 
ATOM   5211 O  O   . VAL   B 1 296 ? -24.365 1.822   -39.424 1.00 13.11 ? 737  VAL   B O   1 
ATOM   5212 C  CB  . VAL   B 1 296 ? -24.631 4.549   -40.749 1.00 16.59 ? 737  VAL   B CB  1 
ATOM   5213 C  CG1 . VAL   B 1 296 ? -23.368 4.373   -41.599 1.00 15.34 ? 737  VAL   B CG1 1 
ATOM   5214 C  CG2 . VAL   B 1 296 ? -25.403 5.826   -41.109 1.00 16.91 ? 737  VAL   B CG2 1 
ATOM   5215 N  N   . LEU   B 1 297 ? -24.374 1.291   -41.622 1.00 12.99 ? 738  LEU   B N   1 
ATOM   5216 C  CA  . LEU   B 1 297 ? -23.511 0.120   -41.484 1.00 12.27 ? 738  LEU   B CA  1 
ATOM   5217 C  C   . LEU   B 1 297 ? -22.298 0.319   -42.372 1.00 14.85 ? 738  LEU   B C   1 
ATOM   5218 O  O   . LEU   B 1 297 ? -22.431 0.470   -43.584 1.00 13.54 ? 738  LEU   B O   1 
ATOM   5219 C  CB  . LEU   B 1 297 ? -24.255 -1.173  -41.855 1.00 13.94 ? 738  LEU   B CB  1 
ATOM   5220 C  CG  . LEU   B 1 297 ? -23.455 -2.456  -42.078 1.00 15.23 ? 738  LEU   B CG  1 
ATOM   5221 C  CD1 . LEU   B 1 297 ? -22.542 -2.769  -40.908 1.00 15.87 ? 738  LEU   B CD1 1 
ATOM   5222 C  CD2 . LEU   B 1 297 ? -24.398 -3.646  -42.365 1.00 18.16 ? 738  LEU   B CD2 1 
ATOM   5223 N  N   . ILE   B 1 298 ? -21.122 0.342   -41.756 1.00 11.38 ? 739  ILE   B N   1 
ATOM   5224 C  CA  . ILE   B 1 298 ? -19.875 0.585   -42.482 1.00 11.33 ? 739  ILE   B CA  1 
ATOM   5225 C  C   . ILE   B 1 298 ? -19.217 -0.760  -42.781 1.00 11.18 ? 739  ILE   B C   1 
ATOM   5226 O  O   . ILE   B 1 298 ? -18.887 -1.510  -41.860 1.00 12.75 ? 739  ILE   B O   1 
ATOM   5227 C  CB  . ILE   B 1 298 ? -18.953 1.514   -41.674 1.00 10.81 ? 739  ILE   B CB  1 
ATOM   5228 C  CG1 . ILE   B 1 298 ? -19.633 2.875   -41.475 1.00 14.96 ? 739  ILE   B CG1 1 
ATOM   5229 C  CG2 . ILE   B 1 298 ? -17.611 1.668   -42.379 1.00 12.23 ? 739  ILE   B CG2 1 
ATOM   5230 C  CD1 . ILE   B 1 298 ? -18.819 3.885   -40.668 1.00 16.93 ? 739  ILE   B CD1 1 
ATOM   5231 N  N   . ILE   B 1 299 ? -19.052 -1.086  -44.067 1.00 11.79 ? 740  ILE   B N   1 
ATOM   5232 C  CA  . ILE   B 1 299 ? -18.558 -2.392  -44.501 1.00 12.98 ? 740  ILE   B CA  1 
ATOM   5233 C  C   . ILE   B 1 299 ? -17.178 -2.218  -45.141 1.00 10.80 ? 740  ILE   B C   1 
ATOM   5234 O  O   . ILE   B 1 299 ? -17.043 -1.536  -46.159 1.00 11.48 ? 740  ILE   B O   1 
ATOM   5235 C  CB  . ILE   B 1 299 ? -19.521 -3.031  -45.515 1.00 12.19 ? 740  ILE   B CB  1 
ATOM   5236 C  CG1 . ILE   B 1 299 ? -20.955 -3.108  -44.945 1.00 12.34 ? 740  ILE   B CG1 1 
ATOM   5237 C  CG2 . ILE   B 1 299 ? -18.999 -4.419  -45.944 1.00 14.52 ? 740  ILE   B CG2 1 
ATOM   5238 C  CD1 . ILE   B 1 299 ? -21.990 -3.658  -45.907 1.00 11.92 ? 740  ILE   B CD1 1 
ATOM   5239 N  N   . LEU   B 1 300 ? -16.154 -2.861  -44.578 1.00 11.08 ? 741  LEU   B N   1 
ATOM   5240 C  CA  . LEU   B 1 300 ? -14.823 -2.806  -45.195 1.00 12.64 ? 741  LEU   B CA  1 
ATOM   5241 C  C   . LEU   B 1 300 ? -14.827 -3.378  -46.620 1.00 11.06 ? 741  LEU   B C   1 
ATOM   5242 O  O   . LEU   B 1 300 ? -15.329 -4.487  -46.857 1.00 13.36 ? 741  LEU   B O   1 
ATOM   5243 C  CB  . LEU   B 1 300 ? -13.821 -3.564  -44.319 1.00 13.61 ? 741  LEU   B CB  1 
ATOM   5244 C  CG  . LEU   B 1 300 ? -12.374 -3.539  -44.822 1.00 11.25 ? 741  LEU   B CG  1 
ATOM   5245 C  CD1 . LEU   B 1 300 ? -11.836 -2.120  -44.821 1.00 13.10 ? 741  LEU   B CD1 1 
ATOM   5246 C  CD2 . LEU   B 1 300 ? -11.483 -4.481  -44.035 1.00 13.93 ? 741  LEU   B CD2 1 
ATOM   5247 N  N   . GLU   B 1 301 ? -14.288 -2.605  -47.583 1.00 9.69  ? 742  GLU   B N   1 
ATOM   5248 C  CA  . GLU   B 1 301 ? -14.005 -3.091  -48.941 1.00 12.52 ? 742  GLU   B CA  1 
ATOM   5249 C  C   . GLU   B 1 301 ? -12.489 -3.199  -49.106 1.00 12.14 ? 742  GLU   B C   1 
ATOM   5250 O  O   . GLU   B 1 301 ? -11.870 -4.031  -48.440 1.00 12.94 ? 742  GLU   B O   1 
ATOM   5251 C  CB  . GLU   B 1 301 ? -14.667 -2.223  -50.026 1.00 11.90 ? 742  GLU   B CB  1 
ATOM   5252 C  CG  . GLU   B 1 301 ? -16.235 -2.167  -49.917 1.00 13.02 ? 742  GLU   B CG  1 
ATOM   5253 C  CD  . GLU   B 1 301 ? -16.972 -3.364  -50.533 1.00 14.64 ? 742  GLU   B CD  1 
ATOM   5254 O  OE1 . GLU   B 1 301 ? -16.338 -4.354  -50.932 1.00 15.24 ? 742  GLU   B OE1 1 
ATOM   5255 O  OE2 . GLU   B 1 301 ? -18.214 -3.329  -50.606 1.00 14.97 ? 742  GLU   B OE2 1 
ATOM   5256 N  N   . GLY   B 1 302 ? -11.893 -2.386  -49.982 1.00 13.34 ? 743  GLY   B N   1 
ATOM   5257 C  CA  . GLY   B 1 302 ? -10.453 -2.380  -50.192 1.00 12.52 ? 743  GLY   B CA  1 
ATOM   5258 C  C   . GLY   B 1 302 ? -9.694  -1.486  -49.234 1.00 12.81 ? 743  GLY   B C   1 
ATOM   5259 O  O   . GLY   B 1 302 ? -10.193 -1.066  -48.187 1.00 13.15 ? 743  GLY   B O   1 
ATOM   5260 N  N   . GLY   B 1 303 ? -8.450  -1.204  -49.598 1.00 14.55 ? 744  GLY   B N   1 
ATOM   5261 C  CA  . GLY   B 1 303 ? -7.557  -0.462  -48.727 1.00 13.19 ? 744  GLY   B CA  1 
ATOM   5262 C  C   . GLY   B 1 303 ? -6.379  -1.330  -48.317 1.00 13.46 ? 744  GLY   B C   1 
ATOM   5263 O  O   . GLY   B 1 303 ? -6.569  -2.377  -47.679 1.00 13.43 ? 744  GLY   B O   1 
ATOM   5264 N  N   . TYR   B 1 304 ? -5.161  -0.903  -48.661 1.00 11.77 ? 745  TYR   B N   1 
ATOM   5265 C  CA  . TYR   B 1 304 ? -4.028  -1.806  -48.638 1.00 11.50 ? 745  TYR   B CA  1 
ATOM   5266 C  C   . TYR   B 1 304 ? -2.813  -1.321  -47.868 1.00 15.01 ? 745  TYR   B C   1 
ATOM   5267 O  O   . TYR   B 1 304 ? -1.827  -2.069  -47.806 1.00 17.83 ? 745  TYR   B O   1 
ATOM   5268 C  CB  . TYR   B 1 304 ? -3.647  -2.197  -50.085 1.00 14.66 ? 745  TYR   B CB  1 
ATOM   5269 C  CG  . TYR   B 1 304 ? -4.867  -2.726  -50.753 1.00 13.35 ? 745  TYR   B CG  1 
ATOM   5270 C  CD1 . TYR   B 1 304 ? -5.347  -3.989  -50.417 1.00 14.60 ? 745  TYR   B CD1 1 
ATOM   5271 C  CD2 . TYR   B 1 304 ? -5.621  -1.936  -51.628 1.00 14.60 ? 745  TYR   B CD2 1 
ATOM   5272 C  CE1 . TYR   B 1 304 ? -6.529  -4.477  -50.965 1.00 16.28 ? 745  TYR   B CE1 1 
ATOM   5273 C  CE2 . TYR   B 1 304 ? -6.809  -2.410  -52.183 1.00 15.26 ? 745  TYR   B CE2 1 
ATOM   5274 C  CZ  . TYR   B 1 304 ? -7.247  -3.682  -51.860 1.00 14.68 ? 745  TYR   B CZ  1 
ATOM   5275 O  OH  . TYR   B 1 304 ? -8.406  -4.181  -52.376 1.00 19.25 ? 745  TYR   B OH  1 
ATOM   5276 N  N   . ASN   B 1 305 ? -2.819  -0.103  -47.321 1.00 10.51 ? 746  ASN   B N   1 
ATOM   5277 C  CA  . ASN   B 1 305 ? -1.791  0.319   -46.368 1.00 11.10 ? 746  ASN   B CA  1 
ATOM   5278 C  C   . ASN   B 1 305 ? -2.326  -0.001  -44.981 1.00 11.88 ? 746  ASN   B C   1 
ATOM   5279 O  O   . ASN   B 1 305 ? -3.308  0.602   -44.538 1.00 12.20 ? 746  ASN   B O   1 
ATOM   5280 C  CB  . ASN   B 1 305 ? -1.449  1.797   -46.555 1.00 12.38 ? 746  ASN   B CB  1 
ATOM   5281 C  CG  . ASN   B 1 305 ? -0.421  2.290   -45.552 1.00 13.53 ? 746  ASN   B CG  1 
ATOM   5282 O  OD1 . ASN   B 1 305 ? -0.532  2.040   -44.359 1.00 13.80 ? 746  ASN   B OD1 1 
ATOM   5283 N  ND2 . ASN   B 1 305 ? 0.594   3.003   -46.053 1.00 13.57 ? 746  ASN   B ND2 1 
ATOM   5284 N  N   . LEU   B 1 306 ? -1.729  -1.007  -44.338 1.00 11.76 ? 747  LEU   B N   1 
ATOM   5285 C  CA  . LEU   B 1 306 ? -2.265  -1.515  -43.085 1.00 12.54 ? 747  LEU   B CA  1 
ATOM   5286 C  C   . LEU   B 1 306 ? -2.403  -0.409  -42.049 1.00 13.82 ? 747  LEU   B C   1 
ATOM   5287 O  O   . LEU   B 1 306 ? -3.402  -0.358  -41.319 1.00 13.31 ? 747  LEU   B O   1 
ATOM   5288 C  CB  . LEU   B 1 306 ? -1.402  -2.657  -42.558 1.00 12.71 ? 747  LEU   B CB  1 
ATOM   5289 C  CG  . LEU   B 1 306 ? -1.294  -3.878  -43.475 1.00 13.58 ? 747  LEU   B CG  1 
ATOM   5290 C  CD1 . LEU   B 1 306 ? -0.275  -4.884  -42.907 1.00 15.31 ? 747  LEU   B CD1 1 
ATOM   5291 C  CD2 . LEU   B 1 306 ? -2.642  -4.528  -43.617 1.00 13.36 ? 747  LEU   B CD2 1 
ATOM   5292 N  N   . THR   B 1 307 ? -1.410  0.475   -41.948 1.00 12.75 ? 748  THR   B N   1 
ATOM   5293 C  CA  . THR   B 1 307 ? -1.519  1.584   -41.007 1.00 13.23 ? 748  THR   B CA  1 
ATOM   5294 C  C   . THR   B 1 307 ? -2.635  2.549   -41.399 1.00 13.64 ? 748  THR   B C   1 
ATOM   5295 O  O   . THR   B 1 307 ? -3.436  2.957   -40.541 1.00 12.85 ? 748  THR   B O   1 
ATOM   5296 C  CB  . THR   B 1 307 ? -0.170  2.295   -40.907 1.00 16.95 ? 748  THR   B CB  1 
ATOM   5297 O  OG1 . THR   B 1 307 ? 0.767   1.374   -40.349 1.00 16.90 ? 748  THR   B OG1 1 
ATOM   5298 C  CG2 . THR   B 1 307 ? -0.274  3.561   -40.042 1.00 21.58 ? 748  THR   B CG2 1 
ATOM   5299 N  N   . SER   B 1 308 ? -2.719  2.912   -42.685 1.00 14.59 ? 749  SER   B N   1 
ATOM   5300 C  CA  . SER   B 1 308 ? -3.727  3.874   -43.120 1.00 12.96 ? 749  SER   B CA  1 
ATOM   5301 C  C   . SER   B 1 308 ? -5.133  3.335   -42.918 1.00 13.19 ? 749  SER   B C   1 
ATOM   5302 O  O   . SER   B 1 308 ? -6.033  4.077   -42.500 1.00 13.28 ? 749  SER   B O   1 
ATOM   5303 C  CB  . SER   B 1 308 ? -3.584  4.189   -44.611 1.00 14.16 ? 749  SER   B CB  1 
ATOM   5304 O  OG  . SER   B 1 308 ? -2.295  4.716   -44.879 1.00 16.37 ? 749  SER   B OG  1 
ATOM   5305 N  N   . ILE   B 1 309 ? -5.370  2.071   -43.270 1.00 11.22 ? 750  ILE   B N   1 
ATOM   5306 C  CA  . ILE   B 1 309 ? -6.737  1.546   -43.137 1.00 9.58  ? 750  ILE   B CA  1 
ATOM   5307 C  C   . ILE   B 1 309 ? -7.140  1.398   -41.680 1.00 12.33 ? 750  ILE   B C   1 
ATOM   5308 O  O   . ILE   B 1 309 ? -8.318  1.602   -41.333 1.00 11.52 ? 750  ILE   B O   1 
ATOM   5309 C  CB  . ILE   B 1 309 ? -6.967  0.238   -43.915 1.00 11.90 ? 750  ILE   B CB  1 
ATOM   5310 C  CG1 . ILE   B 1 309 ? -6.270  -0.947  -43.249 1.00 13.30 ? 750  ILE   B CG1 1 
ATOM   5311 C  CG2 . ILE   B 1 309 ? -6.480  0.361   -45.352 1.00 12.23 ? 750  ILE   B CG2 1 
ATOM   5312 C  CD1 . ILE   B 1 309 ? -6.434  -2.231  -44.016 1.00 15.42 ? 750  ILE   B CD1 1 
ATOM   5313 N  N   . SER   B 1 310 ? -6.182  1.067   -40.812 1.00 10.77 ? 751  SER   B N   1 
ATOM   5314 C  CA  . SER   B 1 310 ? -6.481  0.883   -39.406 1.00 12.29 ? 751  SER   B CA  1 
ATOM   5315 C  C   . SER   B 1 310 ? -6.864  2.205   -38.778 1.00 12.12 ? 751  SER   B C   1 
ATOM   5316 O  O   . SER   B 1 310 ? -7.841  2.282   -38.032 1.00 11.74 ? 751  SER   B O   1 
ATOM   5317 C  CB  . SER   B 1 310 ? -5.267  0.252   -38.712 1.00 11.66 ? 751  SER   B CB  1 
ATOM   5318 O  OG  . SER   B 1 310 ? -5.074  -1.076  -39.196 1.00 12.77 ? 751  SER   B OG  1 
ATOM   5319 N  N   . GLU   B 1 311 ? -6.098  3.261   -39.049 1.00 11.56 ? 752  GLU   B N   1 
ATOM   5320 C  CA  . GLU   B 1 311 ? -6.435  4.571   -38.507 1.00 13.67 ? 752  GLU   B CA  1 
ATOM   5321 C  C   . GLU   B 1 311 ? -7.730  5.111   -39.112 1.00 13.34 ? 752  GLU   B C   1 
ATOM   5322 O  O   . GLU   B 1 311 ? -8.586  5.648   -38.396 1.00 12.27 ? 752  GLU   B O   1 
ATOM   5323 C  CB  . GLU   B 1 311 ? -5.286  5.538   -38.774 1.00 14.81 ? 752  GLU   B CB  1 
ATOM   5324 C  CG  . GLU   B 1 311 ? -5.456  6.897   -38.148 1.00 17.14 ? 752  GLU   B CG  1 
ATOM   5325 C  CD  . GLU   B 1 311 ? -5.432  6.875   -36.620 1.00 28.73 ? 752  GLU   B CD  1 
ATOM   5326 O  OE1 . GLU   B 1 311 ? -4.810  5.960   -36.051 1.00 21.43 ? 752  GLU   B OE1 1 
ATOM   5327 O  OE2 . GLU   B 1 311 ? -6.043  7.768   -35.983 1.00 26.36 ? 752  GLU   B OE2 1 
ATOM   5328 N  N   . SER   B 1 312 ? -7.915  4.934   -40.413 1.00 11.67 ? 753  SER   B N   1 
ATOM   5329 C  CA  . SER   B 1 312 ? -9.083  5.495   -41.081 1.00 14.38 ? 753  SER   B CA  1 
ATOM   5330 C  C   . SER   B 1 312 ? -10.371 4.827   -40.612 1.00 11.82 ? 753  SER   B C   1 
ATOM   5331 O  O   . SER   B 1 312 ? -11.361 5.507   -40.303 1.00 11.40 ? 753  SER   B O   1 
ATOM   5332 C  CB  . SER   B 1 312 ? -8.929  5.355   -42.590 1.00 14.43 ? 753  SER   B CB  1 
ATOM   5333 O  OG  . SER   B 1 312 ? -7.829  6.106   -43.049 1.00 14.38 ? 753  SER   B OG  1 
ATOM   5334 N  N   . MET   B 1 313 ? -10.399 3.498   -40.587 1.00 11.14 ? 754  MET   B N   1 
ATOM   5335 C  CA  . MET   B 1 313 ? -11.628 2.831   -40.195 1.00 12.85 ? 754  MET   B CA  1 
ATOM   5336 C  C   . MET   B 1 313 ? -11.913 3.078   -38.719 1.00 12.87 ? 754  MET   B C   1 
ATOM   5337 O  O   . MET   B 1 313 ? -13.068 3.235   -38.326 1.00 12.15 ? 754  MET   B O   1 
ATOM   5338 C  CB  . MET   B 1 313 ? -11.596 1.338   -40.511 1.00 9.98  ? 754  MET   B CB  1 
ATOM   5339 C  CG  . MET   B 1 313 ? -13.000 0.741   -40.500 1.00 12.83 ? 754  MET   B CG  1 
ATOM   5340 S  SD  . MET   B 1 313 ? -13.105 -0.940  -41.112 1.00 13.11 ? 754  MET   B SD  1 
ATOM   5341 C  CE  . MET   B 1 313 ? -14.782 -1.042  -41.697 1.00 14.91 ? 754  MET   B CE  1 
ATOM   5342 N  N   A SER   B 1 314 ? -10.873 3.131   -37.886 0.71 13.41 ? 755  SER   B N   1 
ATOM   5343 N  N   B SER   B 1 314 ? -10.880 3.112   -37.876 0.29 11.61 ? 755  SER   B N   1 
ATOM   5344 C  CA  A SER   B 1 314 ? -11.080 3.441   -36.475 0.71 12.88 ? 755  SER   B CA  1 
ATOM   5345 C  CA  B SER   B 1 314 ? -11.122 3.322   -36.451 0.29 11.78 ? 755  SER   B CA  1 
ATOM   5346 C  C   A SER   B 1 314 ? -11.700 4.820   -36.294 0.71 10.23 ? 755  SER   B C   1 
ATOM   5347 C  C   B SER   B 1 314 ? -11.717 4.699   -36.172 0.29 11.53 ? 755  SER   B C   1 
ATOM   5348 O  O   A SER   B 1 314 ? -12.596 5.005   -35.454 0.71 12.51 ? 755  SER   B O   1 
ATOM   5349 O  O   B SER   B 1 314 ? -12.501 4.856   -35.225 0.29 11.33 ? 755  SER   B O   1 
ATOM   5350 C  CB  A SER   B 1 314 ? -9.760  3.341   -35.700 0.71 14.83 ? 755  SER   B CB  1 
ATOM   5351 C  CB  B SER   B 1 314 ? -9.837  3.110   -35.648 0.29 11.87 ? 755  SER   B CB  1 
ATOM   5352 O  OG  A SER   B 1 314 ? -9.337  2.003   -35.627 0.71 12.63 ? 755  SER   B OG  1 
ATOM   5353 O  OG  B SER   B 1 314 ? -8.861  4.062   -36.018 0.29 12.86 ? 755  SER   B OG  1 
ATOM   5354 N  N   A MET   B 1 315 ? -11.268 5.794   -37.095 0.71 13.87 ? 756  MET   B N   1 
ATOM   5355 N  N   B MET   B 1 315 ? -11.374 5.699   -36.988 0.29 10.51 ? 756  MET   B N   1 
ATOM   5356 C  CA  A MET   B 1 315 ? -11.873 7.116   -37.008 0.71 14.77 ? 756  MET   B CA  1 
ATOM   5357 C  CA  B MET   B 1 315 ? -11.948 7.034   -36.849 0.29 10.34 ? 756  MET   B CA  1 
ATOM   5358 C  C   A MET   B 1 315 ? -13.354 7.055   -37.344 0.71 15.52 ? 756  MET   B C   1 
ATOM   5359 C  C   B MET   B 1 315 ? -13.358 7.128   -37.417 0.29 11.18 ? 756  MET   B C   1 
ATOM   5360 O  O   A MET   B 1 315 ? -14.167 7.694   -36.667 0.71 11.13 ? 756  MET   B O   1 
ATOM   5361 O  O   B MET   B 1 315 ? -14.113 8.024   -37.022 0.29 16.40 ? 756  MET   B O   1 
ATOM   5362 C  CB  A MET   B 1 315 ? -11.142 8.118   -37.905 0.71 12.24 ? 756  MET   B CB  1 
ATOM   5363 C  CB  B MET   B 1 315 ? -11.051 8.079   -37.514 0.29 22.61 ? 756  MET   B CB  1 
ATOM   5364 C  CG  A MET   B 1 315 ? -10.803 9.429   -37.174 0.71 43.56 ? 756  MET   B CG  1 
ATOM   5365 C  CG  B MET   B 1 315 ? -10.704 9.258   -36.613 0.29 25.11 ? 756  MET   B CG  1 
ATOM   5366 S  SD  A MET   B 1 315 ? -10.001 9.255   -35.551 0.71 21.05 ? 756  MET   B SD  1 
ATOM   5367 S  SD  B MET   B 1 315 ? -9.712  10.504  -37.451 0.29 23.41 ? 756  MET   B SD  1 
ATOM   5368 C  CE  A MET   B 1 315 ? -8.807  10.593  -35.648 0.71 49.38 ? 756  MET   B CE  1 
ATOM   5369 C  CE  B MET   B 1 315 ? -8.134  10.280  -36.634 0.29 20.28 ? 756  MET   B CE  1 
ATOM   5370 N  N   . CYS   B 1 316 ? -13.728 6.244   -38.342 1.00 12.42 ? 757  CYS   B N   1 
ATOM   5371 C  CA  . CYS   B 1 316 ? -15.139 6.098   -38.684 1.00 12.00 ? 757  CYS   B CA  1 
ATOM   5372 C  C   . CYS   B 1 316 ? -15.936 5.545   -37.507 1.00 14.11 ? 757  CYS   B C   1 
ATOM   5373 O  O   . CYS   B 1 316 ? -17.014 6.056   -37.180 1.00 12.81 ? 757  CYS   B O   1 
ATOM   5374 C  CB  . CYS   B 1 316 ? -15.332 5.228   -39.919 1.00 12.72 ? 757  CYS   B CB  1 
ATOM   5375 S  SG  . CYS   B 1 316 ? -14.590 5.899   -41.431 1.00 13.02 ? 757  CYS   B SG  1 
ATOM   5376 N  N   . THR   B 1 317 ? -15.426 4.503   -36.861 1.00 11.66 ? 758  THR   B N   1 
ATOM   5377 C  CA  . THR   B 1 317 ? -16.118 3.938   -35.708 1.00 11.82 ? 758  THR   B CA  1 
ATOM   5378 C  C   . THR   B 1 317 ? -16.238 4.959   -34.589 1.00 13.08 ? 758  THR   B C   1 
ATOM   5379 O  O   . THR   B 1 317 ? -17.273 5.016   -33.904 1.00 11.69 ? 758  THR   B O   1 
ATOM   5380 C  CB  . THR   B 1 317 ? -15.384 2.682   -35.235 1.00 12.91 ? 758  THR   B CB  1 
ATOM   5381 O  OG1 . THR   B 1 317 ? -15.290 1.768   -36.327 1.00 13.30 ? 758  THR   B OG1 1 
ATOM   5382 C  CG2 . THR   B 1 317 ? -16.118 1.999   -34.064 1.00 13.59 ? 758  THR   B CG2 1 
ATOM   5383 N  N   . SER   B 1 318 ? -15.173 5.736   -34.338 1.00 11.54 ? 759  SER   B N   1 
ATOM   5384 C  CA  . SER   B 1 318 ? -15.272 6.829   -33.374 1.00 13.90 ? 759  SER   B CA  1 
ATOM   5385 C  C   . SER   B 1 318 ? -16.458 7.735   -33.668 1.00 14.97 ? 759  SER   B C   1 
ATOM   5386 O  O   . SER   B 1 318 ? -17.187 8.127   -32.746 1.00 13.18 ? 759  SER   B O   1 
ATOM   5387 C  CB  . SER   B 1 318 ? -13.960 7.624   -33.366 1.00 12.91 ? 759  SER   B CB  1 
ATOM   5388 O  OG  . SER   B 1 318 ? -14.053 8.703   -32.453 1.00 19.78 ? 759  SER   B OG  1 
ATOM   5389 N  N   . MET   B 1 319 ? -16.700 8.042   -34.938 1.00 13.01 ? 760  MET   B N   1 
ATOM   5390 C  CA  . MET   B 1 319 ? -17.847 8.879   -35.280 1.00 13.64 ? 760  MET   B CA  1 
ATOM   5391 C  C   . MET   B 1 319 ? -19.160 8.157   -34.999 1.00 15.40 ? 760  MET   B C   1 
ATOM   5392 O  O   . MET   B 1 319 ? -20.084 8.739   -34.418 1.00 14.16 ? 760  MET   B O   1 
ATOM   5393 C  CB  . MET   B 1 319 ? -17.779 9.294   -36.746 1.00 13.87 ? 760  MET   B CB  1 
ATOM   5394 C  CG  . MET   B 1 319 ? -16.607 10.165  -37.117 1.00 14.51 ? 760  MET   B CG  1 
ATOM   5395 S  SD  . MET   B 1 319 ? -16.495 11.695  -36.168 1.00 16.55 ? 760  MET   B SD  1 
ATOM   5396 C  CE  . MET   B 1 319 ? -15.335 11.256  -34.850 1.00 16.51 ? 760  MET   B CE  1 
ATOM   5397 N  N   . LEU   B 1 320 ? -19.266 6.880   -35.392 1.00 11.11 ? 761  LEU   B N   1 
ATOM   5398 C  CA  . LEU   B 1 320 ? -20.485 6.123   -35.101 1.00 13.81 ? 761  LEU   B CA  1 
ATOM   5399 C  C   . LEU   B 1 320 ? -20.789 6.106   -33.603 1.00 16.81 ? 761  LEU   B C   1 
ATOM   5400 O  O   . LEU   B 1 320 ? -21.956 6.111   -33.211 1.00 14.29 ? 761  LEU   B O   1 
ATOM   5401 C  CB  . LEU   B 1 320 ? -20.352 4.689   -35.613 1.00 15.23 ? 761  LEU   B CB  1 
ATOM   5402 C  CG  . LEU   B 1 320 ? -20.234 4.537   -37.130 1.00 14.19 ? 761  LEU   B CG  1 
ATOM   5403 C  CD1 . LEU   B 1 320 ? -20.323 3.086   -37.422 1.00 16.93 ? 761  LEU   B CD1 1 
ATOM   5404 C  CD2 . LEU   B 1 320 ? -21.318 5.328   -37.863 1.00 14.63 ? 761  LEU   B CD2 1 
ATOM   5405 N  N   . LEU   B 1 321 ? -19.754 6.061   -32.759 1.00 14.03 ? 762  LEU   B N   1 
ATOM   5406 C  CA  . LEU   B 1 321 ? -19.911 6.078   -31.310 1.00 15.20 ? 762  LEU   B CA  1 
ATOM   5407 C  C   . LEU   B 1 321 ? -20.321 7.440   -30.768 1.00 16.70 ? 762  LEU   B C   1 
ATOM   5408 O  O   . LEU   B 1 321 ? -20.578 7.548   -29.563 1.00 19.22 ? 762  LEU   B O   1 
ATOM   5409 C  CB  . LEU   B 1 321 ? -18.604 5.613   -30.655 1.00 12.79 ? 762  LEU   B CB  1 
ATOM   5410 C  CG  . LEU   B 1 321 ? -18.345 4.118   -30.767 1.00 12.26 ? 762  LEU   B CG  1 
ATOM   5411 C  CD1 . LEU   B 1 321 ? -16.878 3.805   -30.526 1.00 16.11 ? 762  LEU   B CD1 1 
ATOM   5412 C  CD2 . LEU   B 1 321 ? -19.199 3.376   -29.769 1.00 14.87 ? 762  LEU   B CD2 1 
ATOM   5413 N  N   . GLY   B 1 322 ? -20.395 8.467   -31.604 1.00 15.59 ? 763  GLY   B N   1 
ATOM   5414 C  CA  . GLY   B 1 322 ? -20.824 9.781   -31.161 1.00 19.43 ? 763  GLY   B CA  1 
ATOM   5415 C  C   . GLY   B 1 322 ? -19.722 10.772  -30.843 1.00 17.51 ? 763  GLY   B C   1 
ATOM   5416 O  O   . GLY   B 1 322 ? -20.029 11.879  -30.384 1.00 21.21 ? 763  GLY   B O   1 
ATOM   5417 N  N   . ASP   B 1 323 ? -18.460 10.440  -31.101 1.00 16.20 ? 764  ASP   B N   1 
ATOM   5418 C  CA  . ASP   B 1 323 ? -17.388 11.385  -30.822 1.00 16.30 ? 764  ASP   B CA  1 
ATOM   5419 C  C   . ASP   B 1 323 ? -17.439 12.543  -31.810 1.00 17.07 ? 764  ASP   B C   1 
ATOM   5420 O  O   . ASP   B 1 323 ? -17.905 12.405  -32.938 1.00 17.96 ? 764  ASP   B O   1 
ATOM   5421 C  CB  . ASP   B 1 323 ? -16.042 10.681  -30.912 1.00 16.38 ? 764  ASP   B CB  1 
ATOM   5422 C  CG  . ASP   B 1 323 ? -15.865 9.629   -29.841 1.00 18.40 ? 764  ASP   B CG  1 
ATOM   5423 O  OD1 . ASP   B 1 323 ? -16.605 9.685   -28.836 1.00 20.20 ? 764  ASP   B OD1 1 
ATOM   5424 O  OD2 . ASP   B 1 323 ? -14.994 8.751   -29.993 1.00 20.48 ? 764  ASP   B OD2 1 
ATOM   5425 N  N   . SER   B 1 324 ? -16.965 13.703  -31.379 1.00 18.87 ? 765  SER   B N   1 
ATOM   5426 C  CA  . SER   B 1 324 ? -17.035 14.871  -32.238 1.00 20.41 ? 765  SER   B CA  1 
ATOM   5427 C  C   . SER   B 1 324 ? -16.001 14.741  -33.352 1.00 18.84 ? 765  SER   B C   1 
ATOM   5428 O  O   . SER   B 1 324 ? -14.917 14.191  -33.130 1.00 20.75 ? 765  SER   B O   1 
ATOM   5429 C  CB  . SER   B 1 324 ? -16.751 16.129  -31.416 1.00 23.12 ? 765  SER   B CB  1 
ATOM   5430 O  OG  . SER   B 1 324 ? -17.776 16.339  -30.463 0.57 20.89 ? 765  SER   B OG  1 
ATOM   5431 N  N   . PRO   B 1 325 ? -16.302 15.224  -34.554 1.00 18.83 ? 766  PRO   B N   1 
ATOM   5432 C  CA  . PRO   B 1 325 ? -15.373 15.058  -35.671 1.00 19.46 ? 766  PRO   B CA  1 
ATOM   5433 C  C   . PRO   B 1 325 ? -14.063 15.776  -35.403 1.00 20.98 ? 766  PRO   B C   1 
ATOM   5434 O  O   . PRO   B 1 325 ? -14.052 16.909  -34.901 1.00 23.31 ? 766  PRO   B O   1 
ATOM   5435 C  CB  . PRO   B 1 325 ? -16.121 15.699  -36.852 1.00 20.52 ? 766  PRO   B CB  1 
ATOM   5436 C  CG  . PRO   B 1 325 ? -17.559 15.635  -36.469 1.00 23.69 ? 766  PRO   B CG  1 
ATOM   5437 C  CD  . PRO   B 1 325 ? -17.544 15.889  -34.977 1.00 20.60 ? 766  PRO   B CD  1 
ATOM   5438 N  N   . PRO   B 1 326 ? -12.936 15.143  -35.699 1.00 18.51 ? 767  PRO   B N   1 
ATOM   5439 C  CA  . PRO   B 1 326 ? -11.655 15.846  -35.597 1.00 16.58 ? 767  PRO   B CA  1 
ATOM   5440 C  C   . PRO   B 1 326 ? -11.559 16.928  -36.660 1.00 19.59 ? 767  PRO   B C   1 
ATOM   5441 O  O   . PRO   B 1 326 ? -12.180 16.849  -37.723 1.00 21.90 ? 767  PRO   B O   1 
ATOM   5442 C  CB  . PRO   B 1 326 ? -10.620 14.738  -35.838 1.00 18.66 ? 767  PRO   B CB  1 
ATOM   5443 C  CG  . PRO   B 1 326 ? -11.382 13.667  -36.586 1.00 32.01 ? 767  PRO   B CG  1 
ATOM   5444 C  CD  . PRO   B 1 326 ? -12.793 13.735  -36.096 1.00 21.73 ? 767  PRO   B CD  1 
ATOM   5445 N  N   . SER   B 1 327 ? -10.758 17.952  -36.381 1.00 17.20 ? 768  SER   B N   1 
ATOM   5446 C  CA  . SER   B 1 327 ? -10.719 19.106  -37.265 1.00 17.82 ? 768  SER   B CA  1 
ATOM   5447 C  C   . SER   B 1 327 ? -10.011 18.778  -38.572 1.00 17.29 ? 768  SER   B C   1 
ATOM   5448 O  O   . SER   B 1 327 ? -8.918  18.200  -38.580 1.00 17.63 ? 768  SER   B O   1 
ATOM   5449 C  CB  . SER   B 1 327 ? -10.006 20.267  -36.568 1.00 21.93 ? 768  SER   B CB  1 
ATOM   5450 O  OG  . SER   B 1 327 ? -10.645 20.566  -35.344 1.00 19.66 ? 768  SER   B OG  1 
ATOM   5451 N  N   . LEU   B 1 328 ? -10.634 19.166  -39.681 1.00 17.26 ? 769  LEU   B N   1 
ATOM   5452 C  CA  . LEU   B 1 328 ? -9.976  19.043  -40.970 1.00 19.13 ? 769  LEU   B CA  1 
ATOM   5453 C  C   . LEU   B 1 328 ? -8.857  20.071  -41.087 1.00 25.12 ? 769  LEU   B C   1 
ATOM   5454 O  O   . LEU   B 1 328 ? -8.857  21.113  -40.421 1.00 22.18 ? 769  LEU   B O   1 
ATOM   5455 C  CB  . LEU   B 1 328 ? -10.972 19.278  -42.097 1.00 17.57 ? 769  LEU   B CB  1 
ATOM   5456 C  CG  . LEU   B 1 328 ? -12.031 18.181  -42.226 1.00 21.23 ? 769  LEU   B CG  1 
ATOM   5457 C  CD1 . LEU   B 1 328 ? -13.059 18.552  -43.298 1.00 22.59 ? 769  LEU   B CD1 1 
ATOM   5458 C  CD2 . LEU   B 1 328 ? -11.363 16.824  -42.517 1.00 19.86 ? 769  LEU   B CD2 1 
ATOM   5459 N  N   . ASP   B 1 329 ? -7.953  19.819  -42.005 1.00 22.92 ? 770  ASP   B N   1 
ATOM   5460 C  CA  . ASP   B 1 329 ? -6.948  20.840  -42.349 1.00 28.26 ? 770  ASP   B CA  1 
ATOM   5461 C  C   . ASP   B 1 329 ? -7.686  21.912  -43.156 1.00 39.64 ? 770  ASP   B C   1 
ATOM   5462 O  O   . ASP   B 1 329 ? -8.779  21.645  -43.633 1.00 29.09 ? 770  ASP   B O   1 
ATOM   5463 C  CB  . ASP   B 1 329 ? -5.872  20.167  -43.182 1.00 26.89 ? 770  ASP   B CB  1 
ATOM   5464 C  CG  . ASP   B 1 329 ? -4.481  20.783  -43.153 1.00 44.53 ? 770  ASP   B CG  1 
ATOM   5465 O  OD1 . ASP   B 1 329 ? -4.339  21.886  -42.600 1.00 45.78 ? 770  ASP   B OD1 1 
ATOM   5466 O  OD2 . ASP   B 1 329 ? -3.555  20.141  -43.685 1.00 68.91 ? 770  ASP   B OD2 1 
ATOM   5467 N  N   . HIS   B 1 330 ? -7.098  23.093  -43.311 1.00 47.49 ? 771  HIS   B N   1 
ATOM   5468 C  CA  . HIS   B 1 330 ? -7.728  24.097  -44.203 1.00 54.59 ? 771  HIS   B CA  1 
ATOM   5469 C  C   . HIS   B 1 330 ? -7.876  23.459  -45.573 1.00 50.08 ? 771  HIS   B C   1 
ATOM   5470 O  O   . HIS   B 1 330 ? -6.916  22.851  -46.057 1.00 67.50 ? 771  HIS   B O   1 
ATOM   5471 C  CB  . HIS   B 1 330 ? -6.833  25.310  -44.449 1.00 65.32 ? 771  HIS   B CB  1 
ATOM   5472 C  CG  . HIS   B 1 330 ? -6.927  26.375  -43.413 1.00 68.28 ? 771  HIS   B CG  1 
ATOM   5473 N  ND1 . HIS   B 1 330 ? -5.838  26.802  -42.686 1.00 62.75 ? 771  HIS   B ND1 1 
ATOM   5474 C  CD2 . HIS   B 1 330 ? -7.963  27.110  -42.996 1.00 68.42 ? 771  HIS   B CD2 1 
ATOM   5475 C  CE1 . HIS   B 1 330 ? -6.218  27.757  -41.852 1.00 69.21 ? 771  HIS   B CE1 1 
ATOM   5476 N  NE2 . HIS   B 1 330 ? -7.502  27.967  -42.031 1.00 79.04 ? 771  HIS   B NE2 1 
ATOM   5477 N  N   . LEU   B 1 331 ? -9.062  23.538  -46.137 1.00 45.46 ? 772  LEU   B N   1 
ATOM   5478 C  CA  . LEU   B 1 331 ? -9.296  22.893  -47.442 1.00 52.61 ? 772  LEU   B CA  1 
ATOM   5479 C  C   . LEU   B 1 331 ? -8.690  23.758  -48.559 1.00 58.97 ? 772  LEU   B C   1 
ATOM   5480 O  O   . LEU   B 1 331 ? -9.127  24.905  -48.736 1.00 50.00 ? 772  LEU   B O   1 
ATOM   5481 C  CB  . LEU   B 1 331 ? -10.780 22.588  -47.594 1.00 47.40 ? 772  LEU   B CB  1 
ATOM   5482 C  CG  . LEU   B 1 331 ? -11.350 21.654  -46.521 1.00 52.14 ? 772  LEU   B CG  1 
ATOM   5483 C  CD1 . LEU   B 1 331 ? -12.851 21.506  -46.638 1.00 49.54 ? 772  LEU   B CD1 1 
ATOM   5484 C  CD2 . LEU   B 1 331 ? -10.671 20.292  -46.527 1.00 55.26 ? 772  LEU   B CD2 1 
ATOM   5485 N  N   . THR   B 1 332 ? -7.647  23.246  -49.207 1.00 57.78 ? 773  THR   B N   1 
ATOM   5486 C  CA  . THR   B 1 332 ? -7.021  23.948  -50.329 1.00 46.23 ? 773  THR   B CA  1 
ATOM   5487 C  C   . THR   B 1 332 ? -8.066  24.131  -51.389 1.00 60.87 ? 773  THR   B C   1 
ATOM   5488 O  O   . THR   B 1 332 ? -9.038  23.348  -51.418 1.00 52.09 ? 773  THR   B O   1 
ATOM   5489 C  CB  . THR   B 1 332 ? -5.867  23.099  -50.841 1.00 51.17 ? 773  THR   B CB  1 
ATOM   5490 O  OG1 . THR   B 1 332 ? -6.421  21.823  -51.135 1.00 46.30 ? 773  THR   B OG1 1 
ATOM   5491 C  CG2 . THR   B 1 332 ? -4.757  22.943  -49.819 1.00 54.14 ? 773  THR   B CG2 1 
ATOM   5492 N  N   . PRO   B 1 333 ? -7.923  25.089  -52.339 1.00 65.10 ? 774  PRO   B N   1 
ATOM   5493 C  CA  . PRO   B 1 333 ? -8.864  25.166  -53.429 1.00 58.90 ? 774  PRO   B CA  1 
ATOM   5494 C  C   . PRO   B 1 333 ? -8.996  23.812  -54.079 1.00 47.37 ? 774  PRO   B C   1 
ATOM   5495 O  O   . PRO   B 1 333 ? -8.010  23.113  -54.256 1.00 43.70 ? 774  PRO   B O   1 
ATOM   5496 C  CB  . PRO   B 1 333 ? -8.287  26.194  -54.403 1.00 51.09 ? 774  PRO   B CB  1 
ATOM   5497 C  CG  . PRO   B 1 333 ? -7.453  27.082  -53.513 1.00 45.67 ? 774  PRO   B CG  1 
ATOM   5498 C  CD  . PRO   B 1 333 ? -6.915  26.165  -52.435 1.00 45.47 ? 774  PRO   B CD  1 
ATOM   5499 N  N   . LEU   B 1 334 ? -10.206 23.521  -54.515 1.00 39.08 ? 775  LEU   B N   1 
ATOM   5500 C  CA  . LEU   B 1 334 ? -10.474 22.255  -55.213 1.00 37.25 ? 775  LEU   B CA  1 
ATOM   5501 C  C   . LEU   B 1 334 ? -9.622  22.138  -56.463 1.00 45.08 ? 775  LEU   B C   1 
ATOM   5502 O  O   . LEU   B 1 334 ? -9.504  23.119  -57.206 1.00 38.52 ? 775  LEU   B O   1 
ATOM   5503 C  CB  . LEU   B 1 334 ? -11.943 22.240  -55.634 1.00 47.09 ? 775  LEU   B CB  1 
ATOM   5504 C  CG  . LEU   B 1 334 ? -12.932 21.468  -54.771 1.00 41.09 ? 775  LEU   B CG  1 
ATOM   5505 C  CD1 . LEU   B 1 334 ? -13.743 20.606  -55.722 1.00 32.68 ? 775  LEU   B CD1 1 
ATOM   5506 C  CD2 . LEU   B 1 334 ? -12.110 20.634  -53.838 1.00 41.43 ? 775  LEU   B CD2 1 
ATOM   5507 N  N   . LYS   B 1 335 ? -9.069  20.961  -56.688 1.00 35.62 ? 776  LYS   B N   1 
ATOM   5508 C  CA  . LYS   B 1 335 ? -8.382  20.735  -57.968 1.00 35.26 ? 776  LYS   B CA  1 
ATOM   5509 C  C   . LYS   B 1 335 ? -9.398  21.051  -59.081 1.00 46.98 ? 776  LYS   B C   1 
ATOM   5510 O  O   . LYS   B 1 335 ? -10.573 20.681  -58.940 1.00 43.47 ? 776  LYS   B O   1 
ATOM   5511 C  CB  . LYS   B 1 335 ? -7.782  19.331  -57.895 1.00 33.17 ? 776  LYS   B CB  1 
ATOM   5512 C  CG  . LYS   B 1 335 ? -6.745  19.208  -56.795 1.00 42.99 ? 776  LYS   B CG  1 
ATOM   5513 C  CD  . LYS   B 1 335 ? -6.024  17.871  -56.724 1.00 38.98 ? 776  LYS   B CD  1 
ATOM   5514 C  CE  . LYS   B 1 335 ? -4.746  17.965  -55.953 1.00 29.87 ? 776  LYS   B CE  1 
ATOM   5515 N  NZ  . LYS   B 1 335 ? -4.896  18.764  -54.737 1.00 27.34 ? 776  LYS   B NZ  1 
ATOM   5516 N  N   . THR   B 1 336 ? -8.946  21.703  -60.145 1.00 37.25 ? 777  THR   B N   1 
ATOM   5517 C  CA  . THR   B 1 336 ? -9.872  22.183  -61.178 1.00 30.40 ? 777  THR   B CA  1 
ATOM   5518 C  C   . THR   B 1 336 ? -10.649 21.034  -61.777 1.00 29.82 ? 777  THR   B C   1 
ATOM   5519 O  O   . THR   B 1 336 ? -11.855 21.175  -61.979 1.00 33.77 ? 777  THR   B O   1 
ATOM   5520 C  CB  . THR   B 1 336 ? -9.064  22.968  -62.209 1.00 42.99 ? 777  THR   B CB  1 
ATOM   5521 O  OG1 . THR   B 1 336 ? -8.137  22.049  -62.773 1.00 51.36 ? 777  THR   B OG1 1 
ATOM   5522 C  CG2 . THR   B 1 336 ? -8.328  24.138  -61.584 1.00 42.18 ? 777  THR   B CG2 1 
ATOM   5523 N  N   . SER   B 1 337 ? -9.964  19.929  -62.030 1.00 36.52 ? 778  SER   B N   1 
ATOM   5524 C  CA  . SER   B 1 337 ? -10.626 18.791  -62.656 1.00 34.13 ? 778  SER   B CA  1 
ATOM   5525 C  C   . SER   B 1 337 ? -11.682 18.189  -61.741 1.00 21.32 ? 778  SER   B C   1 
ATOM   5526 O  O   . SER   B 1 337 ? -12.646 17.588  -62.224 1.00 25.09 ? 778  SER   B O   1 
ATOM   5527 C  CB  . SER   B 1 337 ? -9.604  17.723  -63.048 1.00 30.44 ? 778  SER   B CB  1 
ATOM   5528 O  OG  . SER   B 1 337 ? -9.130  17.044  -61.899 1.00 34.18 ? 778  SER   B OG  1 
ATOM   5529 N  N   . ALA   B 1 338 ? -11.516 18.325  -60.421 1.00 22.91 ? 779  ALA   B N   1 
ATOM   5530 C  CA  . ALA   B 1 338 ? -12.575 17.899  -59.507 1.00 23.35 ? 779  ALA   B CA  1 
ATOM   5531 C  C   . ALA   B 1 338 ? -13.837 18.728  -59.697 1.00 23.89 ? 779  ALA   B C   1 
ATOM   5532 O  O   . ALA   B 1 338 ? -14.947 18.189  -59.676 1.00 20.98 ? 779  ALA   B O   1 
ATOM   5533 C  CB  . ALA   B 1 338 ? -12.090 17.974  -58.059 1.00 25.54 ? 779  ALA   B CB  1 
ATOM   5534 N  N   . THR   B 1 339 ? -13.691 20.043  -59.884 1.00 27.63 ? 780  THR   B N   1 
ATOM   5535 C  CA  . THR   B 1 339 ? -14.857 20.870  -60.171 1.00 26.48 ? 780  THR   B CA  1 
ATOM   5536 C  C   . THR   B 1 339 ? -15.511 20.449  -61.479 1.00 20.42 ? 780  THR   B C   1 
ATOM   5537 O  O   . THR   B 1 339 ? -16.740 20.401  -61.573 1.00 25.54 ? 780  THR   B O   1 
ATOM   5538 C  CB  . THR   B 1 339 ? -14.461 22.348  -60.214 1.00 31.47 ? 780  THR   B CB  1 
ATOM   5539 O  OG1 . THR   B 1 339 ? -13.989 22.743  -58.923 1.00 37.53 ? 780  THR   B OG1 1 
ATOM   5540 C  CG2 . THR   B 1 339 ? -15.652 23.218  -60.596 1.00 27.95 ? 780  THR   B CG2 1 
ATOM   5541 N  N   . VAL   B 1 340 ? -14.699 20.127  -62.489 1.00 24.59 ? 781  VAL   B N   1 
ATOM   5542 C  CA  . VAL   B 1 340 ? -15.229 19.636  -63.756 1.00 35.98 ? 781  VAL   B CA  1 
ATOM   5543 C  C   . VAL   B 1 340 ? -16.027 18.355  -63.541 1.00 41.38 ? 781  VAL   B C   1 
ATOM   5544 O  O   . VAL   B 1 340 ? -17.144 18.213  -64.043 1.00 26.92 ? 781  VAL   B O   1 
ATOM   5545 C  CB  . VAL   B 1 340 ? -14.094 19.452  -64.779 1.00 26.40 ? 781  VAL   B CB  1 
ATOM   5546 C  CG1 . VAL   B 1 340 ? -14.573 18.652  -65.988 1.00 25.87 ? 781  VAL   B CG1 1 
ATOM   5547 C  CG2 . VAL   B 1 340 ? -13.552 20.813  -65.207 1.00 27.25 ? 781  VAL   B CG2 1 
ATOM   5548 N  N   . SER   B 1 341 ? -15.475 17.410  -62.775 1.00 21.37 ? 782  SER   B N   1 
ATOM   5549 C  CA  . SER   B 1 341 ? -16.200 16.169  -62.505 1.00 21.55 ? 782  SER   B CA  1 
ATOM   5550 C  C   . SER   B 1 341 ? -17.511 16.447  -61.790 1.00 21.86 ? 782  SER   B C   1 
ATOM   5551 O  O   . SER   B 1 341 ? -18.553 15.892  -62.148 1.00 21.41 ? 782  SER   B O   1 
ATOM   5552 C  CB  . SER   B 1 341 ? -15.339 15.207  -61.677 1.00 20.82 ? 782  SER   B CB  1 
ATOM   5553 O  OG  . SER   B 1 341 ? -14.205 14.760  -62.385 1.00 22.71 ? 782  SER   B OG  1 
ATOM   5554 N  N   . ILE   B 1 342 ? -17.472 17.278  -60.748 1.00 21.60 ? 783  ILE   B N   1 
ATOM   5555 C  CA  . ILE   B 1 342 ? -18.687 17.570  -59.996 1.00 22.07 ? 783  ILE   B CA  1 
ATOM   5556 C  C   . ILE   B 1 342 ? -19.743 18.199  -60.898 1.00 25.33 ? 783  ILE   B C   1 
ATOM   5557 O  O   . ILE   B 1 342 ? -20.928 17.847  -60.832 1.00 22.83 ? 783  ILE   B O   1 
ATOM   5558 C  CB  . ILE   B 1 342 ? -18.362 18.448  -58.773 1.00 24.67 ? 783  ILE   B CB  1 
ATOM   5559 C  CG1 . ILE   B 1 342 ? -17.495 17.653  -57.793 1.00 22.91 ? 783  ILE   B CG1 1 
ATOM   5560 C  CG2 . ILE   B 1 342 ? -19.633 18.952  -58.122 1.00 22.73 ? 783  ILE   B CG2 1 
ATOM   5561 C  CD1 . ILE   B 1 342 ? -17.085 18.414  -56.551 1.00 23.41 ? 783  ILE   B CD1 1 
ATOM   5562 N  N   . ASN   B 1 343 ? -19.326 19.126  -61.765 1.00 24.93 ? 784  ASN   B N   1 
ATOM   5563 C  CA  . ASN   B 1 343 ? -20.282 19.782  -62.652 1.00 32.09 ? 784  ASN   B CA  1 
ATOM   5564 C  C   . ASN   B 1 343 ? -20.876 18.799  -63.655 1.00 24.44 ? 784  ASN   B C   1 
ATOM   5565 O  O   . ASN   B 1 343 ? -22.067 18.883  -63.982 1.00 26.75 ? 784  ASN   B O   1 
ATOM   5566 C  CB  . ASN   B 1 343 ? -19.620 20.964  -63.359 1.00 26.98 ? 784  ASN   B CB  1 
ATOM   5567 C  CG  . ASN   B 1 343 ? -19.350 22.124  -62.424 1.00 45.31 ? 784  ASN   B CG  1 
ATOM   5568 O  OD1 . ASN   B 1 343 ? -20.023 22.283  -61.406 1.00 31.78 ? 784  ASN   B OD1 1 
ATOM   5569 N  ND2 . ASN   B 1 343 ? -18.369 22.951  -62.772 1.00 39.33 ? 784  ASN   B ND2 1 
ATOM   5570 N  N   . ASN   B 1 344 ? -20.066 17.863  -64.154 1.00 22.43 ? 785  ASN   B N   1 
ATOM   5571 C  CA  . ASN   B 1 344 ? -20.588 16.851  -65.070 1.00 20.56 ? 785  ASN   B CA  1 
ATOM   5572 C  C   . ASN   B 1 344 ? -21.628 15.974  -64.388 1.00 22.42 ? 785  ASN   B C   1 
ATOM   5573 O  O   . ASN   B 1 344 ? -22.652 15.633  -64.992 1.00 23.71 ? 785  ASN   B O   1 
ATOM   5574 C  CB  . ASN   B 1 344 ? -19.444 16.014  -65.639 1.00 22.88 ? 785  ASN   B CB  1 
ATOM   5575 C  CG  . ASN   B 1 344 ? -18.642 16.762  -66.684 1.00 24.15 ? 785  ASN   B CG  1 
ATOM   5576 O  OD1 . ASN   B 1 344 ? -19.185 17.605  -67.400 1.00 39.37 ? 785  ASN   B OD1 1 
ATOM   5577 N  ND2 . ASN   B 1 344 ? -17.357 16.454  -66.795 1.00 29.83 ? 785  ASN   B ND2 1 
ATOM   5578 N  N   . VAL   B 1 345 ? -21.391 15.594  -63.129 1.00 21.45 ? 786  VAL   B N   1 
ATOM   5579 C  CA  . VAL   B 1 345 ? -22.374 14.790  -62.418 1.00 18.74 ? 786  VAL   B CA  1 
ATOM   5580 C  C   . VAL   B 1 345 ? -23.637 15.597  -62.164 1.00 21.27 ? 786  VAL   B C   1 
ATOM   5581 O  O   . VAL   B 1 345 ? -24.756 15.078  -62.260 1.00 22.59 ? 786  VAL   B O   1 
ATOM   5582 C  CB  . VAL   B 1 345 ? -21.780 14.250  -61.100 1.00 20.69 ? 786  VAL   B CB  1 
ATOM   5583 C  CG1 . VAL   B 1 345 ? -22.807 13.408  -60.380 1.00 22.20 ? 786  VAL   B CG1 1 
ATOM   5584 C  CG2 . VAL   B 1 345 ? -20.510 13.462  -61.351 1.00 19.51 ? 786  VAL   B CG2 1 
ATOM   5585 N  N   . LEU   B 1 346 ? -23.479 16.877  -61.819 1.00 23.74 ? 787  LEU   B N   1 
ATOM   5586 C  CA  . LEU   B 1 346 ? -24.637 17.736  -61.590 1.00 26.56 ? 787  LEU   B CA  1 
ATOM   5587 C  C   . LEU   B 1 346 ? -25.509 17.838  -62.838 1.00 24.75 ? 787  LEU   B C   1 
ATOM   5588 O  O   . LEU   B 1 346 ? -26.740 17.783  -62.748 1.00 25.71 ? 787  LEU   B O   1 
ATOM   5589 C  CB  . LEU   B 1 346 ? -24.164 19.121  -61.161 1.00 27.69 ? 787  LEU   B CB  1 
ATOM   5590 C  CG  . LEU   B 1 346 ? -23.725 19.243  -59.707 1.00 32.71 ? 787  LEU   B CG  1 
ATOM   5591 C  CD1 . LEU   B 1 346 ? -22.939 20.528  -59.496 1.00 33.96 ? 787  LEU   B CD1 1 
ATOM   5592 C  CD2 . LEU   B 1 346 ? -24.936 19.210  -58.821 1.00 28.76 ? 787  LEU   B CD2 1 
ATOM   5593 N  N   . ARG   B 1 347 ? -24.887 18.003  -64.006 1.00 28.33 ? 788  ARG   B N   1 
ATOM   5594 C  CA  . ARG   B 1 347 ? -25.644 18.071  -65.253 1.00 26.42 ? 788  ARG   B CA  1 
ATOM   5595 C  C   . ARG   B 1 347 ? -26.326 16.740  -65.549 1.00 38.73 ? 788  ARG   B C   1 
ATOM   5596 O  O   . ARG   B 1 347 ? -27.486 16.707  -65.980 1.00 29.81 ? 788  ARG   B O   1 
ATOM   5597 C  CB  . ARG   B 1 347 ? -24.712 18.501  -66.392 1.00 29.23 ? 788  ARG   B CB  1 
ATOM   5598 C  CG  . ARG   B 1 347 ? -24.578 20.024  -66.584 1.00 57.63 ? 788  ARG   B CG  1 
ATOM   5599 C  CD  . ARG   B 1 347 ? -23.227 20.446  -67.132 1.00 63.33 ? 788  ARG   B CD  1 
ATOM   5600 N  NE  . ARG   B 1 347 ? -22.876 21.805  -66.706 1.00 65.55 ? 788  ARG   B NE  1 
ATOM   5601 C  CZ  . ARG   B 1 347 ? -21.647 22.191  -66.368 1.00 64.70 ? 788  ARG   B CZ  1 
ATOM   5602 N  NH1 . ARG   B 1 347 ? -20.645 21.330  -66.420 1.00 64.85 ? 788  ARG   B NH1 1 
ATOM   5603 N  NH2 . ARG   B 1 347 ? -21.398 23.439  -65.993 1.00 59.28 ? 788  ARG   B NH2 1 
ATOM   5604 N  N   . ALA   B 1 348 ? -25.628 15.631  -65.288 1.00 35.97 ? 789  ALA   B N   1 
ATOM   5605 C  CA  . ALA   B 1 348 ? -26.177 14.311  -65.571 1.00 26.91 ? 789  ALA   B CA  1 
ATOM   5606 C  C   . ALA   B 1 348 ? -27.375 13.980  -64.685 1.00 21.35 ? 789  ALA   B C   1 
ATOM   5607 O  O   . ALA   B 1 348 ? -28.275 13.240  -65.105 1.00 23.00 ? 789  ALA   B O   1 
ATOM   5608 C  CB  . ALA   B 1 348 ? -25.087 13.251  -65.409 1.00 25.12 ? 789  ALA   B CB  1 
ATOM   5609 N  N   . HIS   B 1 349 ? -27.414 14.498  -63.459 1.00 22.19 ? 790  HIS   B N   1 
ATOM   5610 C  CA  . HIS   B 1 349 ? -28.419 14.071  -62.502 1.00 17.66 ? 790  HIS   B CA  1 
ATOM   5611 C  C   . HIS   B 1 349 ? -29.470 15.120  -62.168 1.00 24.12 ? 790  HIS   B C   1 
ATOM   5612 O  O   . HIS   B 1 349 ? -30.442 14.797  -61.480 1.00 23.88 ? 790  HIS   B O   1 
ATOM   5613 C  CB  . HIS   B 1 349 ? -27.761 13.534  -61.216 1.00 23.33 ? 790  HIS   B CB  1 
ATOM   5614 C  CG  . HIS   B 1 349 ? -27.368 12.095  -61.324 1.00 21.03 ? 790  HIS   B CG  1 
ATOM   5615 N  ND1 . HIS   B 1 349 ? -28.262 11.070  -61.111 1.00 24.95 ? 790  HIS   B ND1 1 
ATOM   5616 C  CD2 . HIS   B 1 349 ? -26.202 11.513  -61.691 1.00 20.14 ? 790  HIS   B CD2 1 
ATOM   5617 C  CE1 . HIS   B 1 349 ? -27.657 9.915   -61.320 1.00 18.02 ? 790  HIS   B CE1 1 
ATOM   5618 N  NE2 . HIS   B 1 349 ? -26.408 10.155  -61.674 1.00 17.79 ? 790  HIS   B NE2 1 
ATOM   5619 N  N   . ALA   B 1 350 ? -29.298 16.356  -62.621 1.00 30.98 ? 791  ALA   B N   1 
ATOM   5620 C  CA  . ALA   B 1 350 ? -30.387 17.329  -62.569 1.00 28.50 ? 791  ALA   B CA  1 
ATOM   5621 C  C   . ALA   B 1 350 ? -31.719 16.814  -63.098 1.00 33.70 ? 791  ALA   B C   1 
ATOM   5622 O  O   . ALA   B 1 350 ? -32.754 17.151  -62.498 1.00 31.60 ? 791  ALA   B O   1 
ATOM   5623 C  CB  . ALA   B 1 350 ? -30.005 18.561  -63.380 1.00 36.55 ? 791  ALA   B CB  1 
ATOM   5624 N  N   . PRO   B 1 351 ? -31.788 16.053  -64.197 1.00 23.52 ? 792  PRO   B N   1 
ATOM   5625 C  CA  . PRO   B 1 351 ? -33.103 15.557  -64.636 1.00 27.89 ? 792  PRO   B CA  1 
ATOM   5626 C  C   . PRO   B 1 351 ? -33.850 14.791  -63.567 1.00 33.76 ? 792  PRO   B C   1 
ATOM   5627 O  O   . PRO   B 1 351 ? -35.083 14.744  -63.617 1.00 34.39 ? 792  PRO   B O   1 
ATOM   5628 C  CB  . PRO   B 1 351 ? -32.772 14.668  -65.844 1.00 25.91 ? 792  PRO   B CB  1 
ATOM   5629 C  CG  . PRO   B 1 351 ? -31.519 15.253  -66.400 1.00 28.37 ? 792  PRO   B CG  1 
ATOM   5630 C  CD  . PRO   B 1 351 ? -30.739 15.733  -65.188 1.00 27.57 ? 792  PRO   B CD  1 
ATOM   5631 N  N   . PHE   B 1 352 ? -33.151 14.221  -62.575 1.00 24.15 ? 793  PHE   B N   1 
ATOM   5632 C  CA  . PHE   B 1 352 ? -33.759 13.275  -61.657 1.00 20.84 ? 793  PHE   B CA  1 
ATOM   5633 C  C   . PHE   B 1 352 ? -33.874 13.754  -60.221 1.00 23.74 ? 793  PHE   B C   1 
ATOM   5634 O  O   . PHE   B 1 352 ? -34.682 13.197  -59.478 1.00 26.97 ? 793  PHE   B O   1 
ATOM   5635 C  CB  . PHE   B 1 352 ? -32.993 11.941  -61.673 1.00 22.56 ? 793  PHE   B CB  1 
ATOM   5636 C  CG  . PHE   B 1 352 ? -32.665 11.470  -63.045 1.00 18.17 ? 793  PHE   B CG  1 
ATOM   5637 C  CD1 . PHE   B 1 352 ? -33.670 10.973  -63.862 1.00 24.21 ? 793  PHE   B CD1 1 
ATOM   5638 C  CD2 . PHE   B 1 352 ? -31.385 11.566  -63.548 1.00 22.91 ? 793  PHE   B CD2 1 
ATOM   5639 C  CE1 . PHE   B 1 352 ? -33.390 10.553  -65.149 1.00 22.29 ? 793  PHE   B CE1 1 
ATOM   5640 C  CE2 . PHE   B 1 352 ? -31.094 11.142  -64.831 1.00 24.82 ? 793  PHE   B CE2 1 
ATOM   5641 C  CZ  . PHE   B 1 352 ? -32.107 10.635  -65.635 1.00 27.58 ? 793  PHE   B CZ  1 
ATOM   5642 N  N   . TRP   B 1 353 ? -33.080 14.736  -59.800 1.00 31.26 ? 794  TRP   B N   1 
ATOM   5643 C  CA  . TRP   B 1 353 ? -33.023 15.150  -58.400 1.00 30.00 ? 794  TRP   B CA  1 
ATOM   5644 C  C   . TRP   B 1 353 ? -33.242 16.652  -58.332 1.00 25.95 ? 794  TRP   B C   1 
ATOM   5645 O  O   . TRP   B 1 353 ? -32.369 17.427  -58.735 1.00 27.84 ? 794  TRP   B O   1 
ATOM   5646 C  CB  . TRP   B 1 353 ? -31.684 14.756  -57.775 1.00 22.09 ? 794  TRP   B CB  1 
ATOM   5647 C  CG  . TRP   B 1 353 ? -31.482 13.288  -57.851 1.00 19.89 ? 794  TRP   B CG  1 
ATOM   5648 C  CD1 . TRP   B 1 353 ? -30.703 12.616  -58.743 1.00 20.73 ? 794  TRP   B CD1 1 
ATOM   5649 C  CD2 . TRP   B 1 353 ? -32.086 12.304  -57.019 1.00 18.29 ? 794  TRP   B CD2 1 
ATOM   5650 N  NE1 . TRP   B 1 353 ? -30.784 11.261  -58.518 1.00 20.18 ? 794  TRP   B NE1 1 
ATOM   5651 C  CE2 . TRP   B 1 353 ? -31.628 11.045  -57.464 1.00 16.89 ? 794  TRP   B CE2 1 
ATOM   5652 C  CE3 . TRP   B 1 353 ? -32.976 12.357  -55.942 1.00 23.04 ? 794  TRP   B CE3 1 
ATOM   5653 C  CZ2 . TRP   B 1 353 ? -32.029 9.853   -56.870 1.00 20.00 ? 794  TRP   B CZ2 1 
ATOM   5654 C  CZ3 . TRP   B 1 353 ? -33.370 11.174  -55.348 1.00 24.92 ? 794  TRP   B CZ3 1 
ATOM   5655 C  CH2 . TRP   B 1 353 ? -32.895 9.932   -55.816 1.00 22.61 ? 794  TRP   B CH2 1 
ATOM   5656 N  N   . SER   B 1 354 ? -34.406 17.055  -57.815 1.00 28.71 ? 795  SER   B N   1 
ATOM   5657 C  CA  A SER   B 1 354 ? -34.740 18.471  -57.756 0.30 30.75 ? 795  SER   B CA  1 
ATOM   5658 C  CA  B SER   B 1 354 ? -34.746 18.471  -57.750 0.70 31.60 ? 795  SER   B CA  1 
ATOM   5659 C  C   . SER   B 1 354 ? -33.826 19.252  -56.822 1.00 31.91 ? 795  SER   B C   1 
ATOM   5660 O  O   . SER   B 1 354 ? -33.717 20.475  -56.965 1.00 37.05 ? 795  SER   B O   1 
ATOM   5661 C  CB  A SER   B 1 354 ? -36.205 18.649  -57.361 0.30 27.34 ? 795  SER   B CB  1 
ATOM   5662 C  CB  B SER   B 1 354 ? -36.204 18.647  -57.319 0.70 26.14 ? 795  SER   B CB  1 
ATOM   5663 O  OG  A SER   B 1 354 ? -37.052 18.106  -58.359 0.30 32.11 ? 795  SER   B OG  1 
ATOM   5664 O  OG  B SER   B 1 354 ? -36.387 18.272  -55.966 0.70 37.16 ? 795  SER   B OG  1 
ATOM   5665 N  N   . SER   B 1 355 ? -33.158 18.580  -55.880 1.00 31.33 ? 796  SER   B N   1 
ATOM   5666 C  CA  . SER   B 1 355 ? -32.254 19.262  -54.964 1.00 30.94 ? 796  SER   B CA  1 
ATOM   5667 C  C   . SER   B 1 355 ? -30.997 19.785  -55.648 1.00 38.19 ? 796  SER   B C   1 
ATOM   5668 O  O   . SER   B 1 355 ? -30.286 20.604  -55.058 1.00 38.38 ? 796  SER   B O   1 
ATOM   5669 C  CB  . SER   B 1 355 ? -31.892 18.336  -53.797 1.00 27.45 ? 796  SER   B CB  1 
ATOM   5670 O  OG  . SER   B 1 355 ? -31.245 17.161  -54.247 1.00 32.29 ? 796  SER   B OG  1 
ATOM   5671 N  N   . LEU   B 1 356 ? -30.718 19.349  -56.872 1.00 29.94 ? 797  LEU   B N   1 
ATOM   5672 C  CA  . LEU   B 1 356 ? -29.528 19.758  -57.599 1.00 33.75 ? 797  LEU   B CA  1 
ATOM   5673 C  C   . LEU   B 1 356 ? -29.778 20.941  -58.519 1.00 40.12 ? 797  LEU   B C   1 
ATOM   5674 O  O   . LEU   B 1 356 ? -28.818 21.530  -59.022 1.00 41.32 ? 797  LEU   B O   1 
ATOM   5675 C  CB  . LEU   B 1 356 ? -29.024 18.589  -58.448 1.00 31.32 ? 797  LEU   B CB  1 
ATOM   5676 C  CG  . LEU   B 1 356 ? -28.684 17.292  -57.721 1.00 34.31 ? 797  LEU   B CG  1 
ATOM   5677 C  CD1 . LEU   B 1 356 ? -28.104 16.297  -58.726 1.00 27.06 ? 797  LEU   B CD1 1 
ATOM   5678 C  CD2 . LEU   B 1 356 ? -27.708 17.553  -56.579 1.00 29.55 ? 797  LEU   B CD2 1 
ATOM   5679 N  N   . ARG   B 1 357 ? -31.035 21.291  -58.759 1.00 40.21 ? 798  ARG   B N   1 
ATOM   5680 C  CA  . ARG   B 1 357 ? -31.353 22.387  -59.659 1.00 52.18 ? 798  ARG   B CA  1 
ATOM   5681 C  C   . ARG   B 1 357 ? -31.165 23.742  -58.980 1.00 56.28 ? 798  ARG   B C   1 
ATOM   5682 O  O   . ARG   B 1 357 ? -31.080 23.830  -57.753 1.00 56.43 ? 798  ARG   B O   1 
ATOM   5683 C  CB  . ARG   B 1 357 ? -32.779 22.237  -60.185 1.00 36.05 ? 798  ARG   B CB  1 
ATOM   5684 C  CG  . ARG   B 1 357 ? -32.994 20.969  -60.990 1.00 36.64 ? 798  ARG   B CG  1 
ATOM   5685 C  CD  . ARG   B 1 357 ? -34.448 20.533  -60.946 1.00 34.96 ? 798  ARG   B CD  1 
ATOM   5686 N  NE  . ARG   B 1 357 ? -34.671 19.286  -61.668 1.00 44.21 ? 798  ARG   B NE  1 
ATOM   5687 C  CZ  . ARG   B 1 357 ? -35.870 18.760  -61.894 1.00 48.03 ? 798  ARG   B CZ  1 
ATOM   5688 N  NH1 . ARG   B 1 357 ? -36.960 19.374  -61.453 1.00 55.92 ? 798  ARG   B NH1 1 
ATOM   5689 N  NH2 . ARG   B 1 357 ? -35.978 17.618  -62.561 1.00 41.62 ? 798  ARG   B NH2 1 
ATOM   5690 O  OXT . ARG   B 1 357 ? -31.084 24.778  -59.644 1.00 63.60 ? 798  ARG   B OXT 1 
HETATM 5691 C  C13 . A1BHX C 2 .   ? 4.101   -1.411  -14.042 1.00 22.56 ? 801  A1BHX A C13 1 
HETATM 5692 C  C15 . A1BHX C 2 .   ? 4.999   0.381   -15.363 1.00 18.50 ? 801  A1BHX A C15 1 
HETATM 5693 C  C17 . A1BHX C 2 .   ? 6.236   -1.577  -15.124 1.00 20.50 ? 801  A1BHX A C17 1 
HETATM 5694 C  C20 . A1BHX C 2 .   ? 3.215   -6.504  -14.090 1.00 41.65 ? 801  A1BHX A C20 1 
HETATM 5695 C  C21 . A1BHX C 2 .   ? 3.701   -6.333  -12.650 1.00 35.69 ? 801  A1BHX A C21 1 
HETATM 5696 C  C22 . A1BHX C 2 .   ? 1.729   -6.822  -14.216 1.00 44.70 ? 801  A1BHX A C22 1 
HETATM 5697 C  C24 . A1BHX C 2 .   ? 6.616   -4.025  -17.285 1.00 20.94 ? 801  A1BHX A C24 1 
HETATM 5698 C  C02 . A1BHX C 2 .   ? 9.735   -3.048  -19.234 1.00 26.41 ? 801  A1BHX A C02 1 
HETATM 5699 C  C05 . A1BHX C 2 .   ? 8.809   -3.735  -18.229 1.00 17.76 ? 801  A1BHX A C05 1 
HETATM 5700 C  C06 . A1BHX C 2 .   ? 9.340   -4.555  -17.242 1.00 20.86 ? 801  A1BHX A C06 1 
HETATM 5701 C  C07 . A1BHX C 2 .   ? 8.508   -5.119  -16.282 1.00 17.99 ? 801  A1BHX A C07 1 
HETATM 5702 C  C08 . A1BHX C 2 .   ? 7.154   -4.856  -16.316 1.00 16.22 ? 801  A1BHX A C08 1 
HETATM 5703 C  C09 . A1BHX C 2 .   ? 6.277   -5.495  -15.245 1.00 22.11 ? 801  A1BHX A C09 1 
HETATM 5704 C  C11 . A1BHX C 2 .   ? 5.427   -3.573  -13.775 1.00 21.44 ? 801  A1BHX A C11 1 
HETATM 5705 C  C12 . A1BHX C 2 .   ? 5.249   -2.147  -14.325 1.00 21.71 ? 801  A1BHX A C12 1 
HETATM 5706 C  C14 . A1BHX C 2 .   ? 3.982   -0.129  -14.568 1.00 24.06 ? 801  A1BHX A C14 1 
HETATM 5707 C  C25 . A1BHX C 2 .   ? 7.448   -3.454  -18.244 1.00 19.47 ? 801  A1BHX A C25 1 
HETATM 5708 N  N03 . A1BHX C 2 .   ? 11.128  -2.829  -18.897 1.00 55.80 ? 801  A1BHX A N03 1 
HETATM 5709 N  N10 . A1BHX C 2 .   ? 5.209   -4.584  -14.825 1.00 21.59 ? 801  A1BHX A N10 1 
HETATM 5710 N  N16 . A1BHX C 2 .   ? 6.078   -0.355  -15.608 1.00 19.87 ? 801  A1BHX A N16 1 
HETATM 5711 O  O01 . A1BHX C 2 .   ? 9.349   -2.571  -20.224 1.00 18.46 ? 801  A1BHX A O01 1 
HETATM 5712 O  O04 . A1BHX C 2 .   ? 12.073  -2.156  -19.713 1.00 18.18 ? 801  A1BHX A O04 1 
HETATM 5713 O  O19 . A1BHX C 2 .   ? 3.485   -5.593  -16.521 1.00 29.49 ? 801  A1BHX A O19 1 
HETATM 5714 O  O23 . A1BHX C 2 .   ? 2.709   -3.960  -15.153 1.00 27.47 ? 801  A1BHX A O23 1 
HETATM 5715 S  S18 . A1BHX C 2 .   ? 3.625   -5.094  -15.160 1.00 25.41 ? 801  A1BHX A S18 1 
HETATM 5716 ZN ZN  . ZN    D 3 .   ? 10.777  -0.620  -20.280 1.00 14.54 ? 802  ZN    A ZN  1 
HETATM 5717 K  K   . K     E 4 .   ? 16.260  3.750   -19.275 1.00 13.81 1 803  K     A K   1 
HETATM 5718 K  K   . K     F 4 .   ? 29.939  1.775   -16.101 1.00 18.47 1 804  K     A K   1 
HETATM 5719 C  C13 . A1BHX G 2 .   ? -4.680  -1.231  -60.926 1.00 43.88 ? 801  A1BHX B C13 1 
HETATM 5720 C  C15 . A1BHX G 2 .   ? -5.222  0.501   -59.353 1.00 21.91 ? 801  A1BHX B C15 1 
HETATM 5721 C  C17 . A1BHX G 2 .   ? -6.068  -1.632  -59.057 1.00 25.25 ? 801  A1BHX B C17 1 
HETATM 5722 C  C20 . A1BHX G 2 .   ? -2.885  -6.271  -60.519 1.00 38.64 ? 801  A1BHX B C20 1 
HETATM 5723 C  C21 . A1BHX G 2 .   ? -3.629  -7.577  -60.349 1.00 39.24 ? 801  A1BHX B C21 1 
HETATM 5724 C  C22 . A1BHX G 2 .   ? -1.386  -6.619  -60.547 1.00 43.26 ? 801  A1BHX B C22 1 
HETATM 5725 C  C24 . A1BHX G 2 .   ? -6.475  -4.046  -56.996 1.00 16.40 ? 801  A1BHX B C24 1 
HETATM 5726 C  C02 . A1BHX G 2 .   ? -9.607  -2.995  -55.093 1.00 29.07 ? 801  A1BHX B C02 1 
HETATM 5727 C  C05 . A1BHX G 2 .   ? -8.685  -3.705  -56.099 1.00 20.21 ? 801  A1BHX B C05 1 
HETATM 5728 C  C06 . A1BHX G 2 .   ? -9.203  -4.513  -57.099 1.00 25.16 ? 801  A1BHX B C06 1 
HETATM 5729 C  C07 . A1BHX G 2 .   ? -8.356  -5.089  -58.039 1.00 20.58 ? 801  A1BHX B C07 1 
HETATM 5730 C  C08 . A1BHX G 2 .   ? -6.996  -4.853  -57.979 1.00 19.27 ? 801  A1BHX B C08 1 
HETATM 5731 C  C09 . A1BHX G 2 .   ? -6.094  -5.489  -59.015 1.00 27.55 ? 801  A1BHX B C09 1 
HETATM 5732 C  C11 . A1BHX G 2 .   ? -5.502  -3.604  -60.615 1.00 22.67 ? 801  A1BHX B C11 1 
HETATM 5733 C  C12 . A1BHX G 2 .   ? -5.412  -2.130  -60.172 1.00 26.00 ? 801  A1BHX B C12 1 
HETATM 5734 C  C14 . A1BHX G 2 .   ? -4.555  0.085   -60.492 1.00 32.07 ? 801  A1BHX B C14 1 
HETATM 5735 C  C25 . A1BHX G 2 .   ? -7.324  -3.462  -56.063 1.00 19.38 ? 801  A1BHX B C25 1 
HETATM 5736 N  N03 . A1BHX G 2 .   ? -11.006 -2.817  -55.426 1.00 65.70 ? 801  A1BHX B N03 1 
HETATM 5737 N  N10 . A1BHX G 2 .   ? -5.117  -4.529  -59.521 1.00 24.46 ? 801  A1BHX B N10 1 
HETATM 5738 N  N16 . A1BHX G 2 .   ? -5.959  -0.364  -58.697 1.00 17.66 ? 801  A1BHX B N16 1 
HETATM 5739 O  O01 . A1BHX G 2 .   ? -9.222  -2.475  -54.110 1.00 18.58 ? 801  A1BHX B O01 1 
HETATM 5740 O  O04 . A1BHX G 2 .   ? -11.957 -2.134  -54.634 1.00 20.16 ? 801  A1BHX B O04 1 
HETATM 5741 O  O19 . A1BHX G 2 .   ? -3.746  -6.108  -58.072 1.00 32.52 ? 801  A1BHX B O19 1 
HETATM 5742 O  O23 . A1BHX G 2 .   ? -2.772  -4.612  -58.223 1.00 31.90 ? 801  A1BHX B O23 1 
HETATM 5743 S  S18 . A1BHX G 2 .   ? -3.563  -5.163  -59.220 1.00 28.45 ? 801  A1BHX B S18 1 
HETATM 5744 ZN ZN  . ZN    H 3 .   ? -10.642 -0.604  -54.080 1.00 13.94 ? 802  ZN    B ZN  1 
HETATM 5745 K  K   . K     I 4 .   ? -29.735 1.750   -58.445 1.00 18.77 1 803  K     B K   1 
HETATM 5746 K  K   . K     J 4 .   ? -16.148 3.747   -55.118 0.90 12.27 1 804  K     B K   1 
HETATM 5747 K  K   . K     K 4 .   ? -11.280 5.010   -49.855 0.72 23.19 1 805  K     B K   1 
HETATM 5748 O  O   . HOH   L 5 .   ? 17.506  14.363  -4.177  1.00 40.53 ? 901  HOH   A O   1 
HETATM 5749 O  O   . HOH   L 5 .   ? 5.423   -24.054 -27.238 1.00 34.11 ? 902  HOH   A O   1 
HETATM 5750 O  O   . HOH   L 5 .   ? 5.401   -35.084 -14.645 1.00 41.90 ? 903  HOH   A O   1 
HETATM 5751 O  O   . HOH   L 5 .   ? 27.413  -25.137 -16.679 1.00 48.55 ? 904  HOH   A O   1 
HETATM 5752 O  O   . HOH   L 5 .   ? 28.550  21.059  -20.648 1.00 40.47 ? 905  HOH   A O   1 
HETATM 5753 O  O   . HOH   L 5 .   ? 22.288  18.171  -27.507 1.00 42.26 ? 906  HOH   A O   1 
HETATM 5754 O  O   . HOH   L 5 .   ? 27.687  -3.859  -9.025  1.00 36.83 ? 907  HOH   A O   1 
HETATM 5755 O  O   . HOH   L 5 .   ? 38.769  7.078   -15.673 1.00 39.23 ? 908  HOH   A O   1 
HETATM 5756 O  O   . HOH   L 5 .   ? 14.604  -20.395 -33.811 1.00 39.19 ? 909  HOH   A O   1 
HETATM 5757 O  O   . HOH   L 5 .   ? 17.226  -1.918  -52.001 1.00 29.13 ? 910  HOH   A O   1 
HETATM 5758 O  O   . HOH   L 5 .   ? 34.480  -5.239  -6.084  1.00 42.76 ? 911  HOH   A O   1 
HETATM 5759 O  O   . HOH   L 5 .   ? 25.738  8.706   -42.052 1.00 44.83 ? 912  HOH   A O   1 
HETATM 5760 O  O   . HOH   L 5 .   ? 6.736   20.048  -21.388 1.00 34.45 ? 913  HOH   A O   1 
HETATM 5761 O  O   . HOH   L 5 .   ? 12.770  13.736  -42.590 1.00 35.01 ? 914  HOH   A O   1 
HETATM 5762 O  O   . HOH   L 5 .   ? 18.269  -25.993 -24.527 1.00 26.11 ? 915  HOH   A O   1 
HETATM 5763 O  O   . HOH   L 5 .   ? 23.686  -0.349  -7.991  1.00 26.79 ? 916  HOH   A O   1 
HETATM 5764 O  O   . HOH   L 5 .   ? 17.402  6.856   0.377   1.00 25.10 ? 917  HOH   A O   1 
HETATM 5765 O  O   . HOH   L 5 .   ? 18.828  -25.808 -27.871 1.00 44.88 ? 918  HOH   A O   1 
HETATM 5766 O  O   . HOH   L 5 .   ? 14.618  -15.425 -8.264  1.00 26.96 ? 919  HOH   A O   1 
HETATM 5767 O  O   . HOH   L 5 .   ? 24.113  -27.400 -16.183 1.00 44.94 ? 920  HOH   A O   1 
HETATM 5768 O  O   . HOH   L 5 .   ? 11.819  3.707   -9.446  1.00 24.31 ? 921  HOH   A O   1 
HETATM 5769 O  O   . HOH   L 5 .   ? 10.346  -31.943 -16.319 1.00 34.69 ? 922  HOH   A O   1 
HETATM 5770 O  O   . HOH   L 5 .   ? 30.724  -16.856 -32.036 1.00 36.52 ? 923  HOH   A O   1 
HETATM 5771 O  O   . HOH   L 5 .   ? 10.437  -23.344 -9.135  1.00 34.61 ? 924  HOH   A O   1 
HETATM 5772 O  O   . HOH   L 5 .   ? 19.721  -19.832 -36.335 1.00 33.74 ? 925  HOH   A O   1 
HETATM 5773 O  O   . HOH   L 5 .   ? 33.778  5.106   -33.606 1.00 28.38 ? 926  HOH   A O   1 
HETATM 5774 O  O   . HOH   L 5 .   ? 12.932  24.539  -16.216 1.00 35.72 ? 927  HOH   A O   1 
HETATM 5775 O  O   . HOH   L 5 .   ? 14.532  10.492  -3.987  1.00 46.68 ? 928  HOH   A O   1 
HETATM 5776 O  O   . HOH   L 5 .   ? 4.801   11.445  -12.518 1.00 30.44 ? 929  HOH   A O   1 
HETATM 5777 O  O   . HOH   L 5 .   ? 20.149  9.549   -46.752 1.00 41.66 ? 930  HOH   A O   1 
HETATM 5778 O  O   . HOH   L 5 .   ? 11.006  -18.586 -40.236 1.00 43.03 ? 931  HOH   A O   1 
HETATM 5779 O  O   . HOH   L 5 .   ? 13.622  7.064   -20.777 1.00 15.95 ? 932  HOH   A O   1 
HETATM 5780 O  O   . HOH   L 5 .   ? 0.234   -11.975 -17.034 1.00 29.85 ? 933  HOH   A O   1 
HETATM 5781 O  O   . HOH   L 5 .   ? 6.783   14.043  -38.525 1.00 40.45 ? 934  HOH   A O   1 
HETATM 5782 O  O   . HOH   L 5 .   ? 2.063   2.518   -15.409 1.00 29.05 ? 935  HOH   A O   1 
HETATM 5783 O  O   . HOH   L 5 .   ? 8.042   -20.696 -8.226  1.00 28.20 ? 936  HOH   A O   1 
HETATM 5784 O  O   . HOH   L 5 .   ? 37.431  13.659  -24.455 1.00 37.44 ? 937  HOH   A O   1 
HETATM 5785 O  O   . HOH   L 5 .   ? 17.126  -8.516  -26.543 1.00 13.78 ? 938  HOH   A O   1 
HETATM 5786 O  O   . HOH   L 5 .   ? 6.011   17.842  -13.935 1.00 38.44 ? 939  HOH   A O   1 
HETATM 5787 O  O   . HOH   L 5 .   ? 36.853  -3.802  -20.612 1.00 26.95 ? 940  HOH   A O   1 
HETATM 5788 O  O   . HOH   L 5 .   ? 17.836  -10.027 -40.404 1.00 16.53 ? 941  HOH   A O   1 
HETATM 5789 O  O   . HOH   L 5 .   ? 25.718  -18.219 -9.678  1.00 48.53 ? 942  HOH   A O   1 
HETATM 5790 O  O   . HOH   L 5 .   ? 23.486  15.669  -6.892  1.00 39.04 ? 943  HOH   A O   1 
HETATM 5791 O  O   . HOH   L 5 .   ? 17.056  -2.378  -4.583  1.00 31.84 ? 944  HOH   A O   1 
HETATM 5792 O  O   . HOH   L 5 .   ? -5.049  -12.992 -21.620 1.00 26.46 ? 945  HOH   A O   1 
HETATM 5793 O  O   . HOH   L 5 .   ? 6.572   10.961  -7.652  1.00 36.21 ? 946  HOH   A O   1 
HETATM 5794 O  O   . HOH   L 5 .   ? 22.610  25.589  -22.441 1.00 40.57 ? 947  HOH   A O   1 
HETATM 5795 O  O   . HOH   L 5 .   ? 22.990  0.996   -5.542  1.00 39.38 ? 948  HOH   A O   1 
HETATM 5796 O  O   . HOH   L 5 .   ? 3.225   -5.794  -43.566 1.00 23.61 ? 949  HOH   A O   1 
HETATM 5797 O  O   . HOH   L 5 .   ? 34.417  13.796  -28.475 1.00 37.69 ? 950  HOH   A O   1 
HETATM 5798 O  O   . HOH   L 5 .   ? 31.841  17.424  -23.707 1.00 39.04 ? 951  HOH   A O   1 
HETATM 5799 O  O   . HOH   L 5 .   ? 22.636  17.593  -5.530  1.00 36.59 ? 952  HOH   A O   1 
HETATM 5800 O  O   . HOH   L 5 .   ? 1.965   9.789   -16.397 1.00 37.20 ? 953  HOH   A O   1 
HETATM 5801 O  O   . HOH   L 5 .   ? 38.476  1.954   -21.946 1.00 24.32 ? 954  HOH   A O   1 
HETATM 5802 O  O   . HOH   L 5 .   ? 17.839  22.708  -9.400  1.00 40.66 ? 955  HOH   A O   1 
HETATM 5803 O  O   . HOH   L 5 .   ? 37.344  4.223   -20.673 1.00 28.71 ? 956  HOH   A O   1 
HETATM 5804 O  O   . HOH   L 5 .   ? 11.352  4.995   -24.458 1.00 11.38 ? 957  HOH   A O   1 
HETATM 5805 O  O   . HOH   L 5 .   ? 24.322  -8.459  -12.343 1.00 26.39 ? 958  HOH   A O   1 
HETATM 5806 O  O   . HOH   L 5 .   ? 2.065   5.326   -37.471 1.00 23.73 ? 959  HOH   A O   1 
HETATM 5807 O  O   . HOH   L 5 .   ? 14.748  1.156   -9.860  1.00 17.33 ? 960  HOH   A O   1 
HETATM 5808 O  O   . HOH   L 5 .   ? 32.699  -13.266 -33.725 1.00 24.45 ? 961  HOH   A O   1 
HETATM 5809 O  O   . HOH   L 5 .   ? 13.947  -11.397 -10.960 1.00 17.67 ? 962  HOH   A O   1 
HETATM 5810 O  O   . HOH   L 5 .   ? 5.403   -17.086 -14.867 1.00 33.80 ? 963  HOH   A O   1 
HETATM 5811 O  O   . HOH   L 5 .   ? 0.846   -1.830  -45.431 1.00 16.62 ? 964  HOH   A O   1 
HETATM 5812 O  O   . HOH   L 5 .   ? 7.288   -10.925 -39.832 1.00 19.94 ? 965  HOH   A O   1 
HETATM 5813 O  O   . HOH   L 5 .   ? 15.528  -13.136 -9.313  1.00 22.54 ? 966  HOH   A O   1 
HETATM 5814 O  O   . HOH   L 5 .   ? 16.682  -28.031 -29.518 1.00 47.06 ? 967  HOH   A O   1 
HETATM 5815 O  O   . HOH   L 5 .   ? 1.893   -22.780 -25.639 1.00 41.91 ? 968  HOH   A O   1 
HETATM 5816 O  O   . HOH   L 5 .   ? 17.029  -5.849  -25.959 1.00 15.09 ? 969  HOH   A O   1 
HETATM 5817 O  O   . HOH   L 5 .   ? 21.924  1.651   -46.318 1.00 24.01 ? 970  HOH   A O   1 
HETATM 5818 O  O   . HOH   L 5 .   ? 19.834  -5.419  -23.134 1.00 13.34 ? 971  HOH   A O   1 
HETATM 5819 O  O   . HOH   L 5 .   ? 31.035  -7.080  -15.879 1.00 24.40 ? 972  HOH   A O   1 
HETATM 5820 O  O   . HOH   L 5 .   ? 37.368  7.490   -8.324  1.00 36.99 ? 973  HOH   A O   1 
HETATM 5821 O  O   . HOH   L 5 .   ? 11.758  14.982  -12.924 1.00 22.06 ? 974  HOH   A O   1 
HETATM 5822 O  O   . HOH   L 5 .   ? 2.552   -1.820  -40.765 1.00 17.19 ? 975  HOH   A O   1 
HETATM 5823 O  O   . HOH   L 5 .   ? 6.451   15.720  -32.558 1.00 38.51 ? 976  HOH   A O   1 
HETATM 5824 O  O   . HOH   L 5 .   ? 29.630  -3.105  -47.039 1.00 28.64 ? 977  HOH   A O   1 
HETATM 5825 O  O   . HOH   L 5 .   ? 24.251  13.973  -36.213 1.00 29.48 ? 978  HOH   A O   1 
HETATM 5826 O  O   . HOH   L 5 .   ? 12.559  2.817   -13.833 1.00 15.78 ? 979  HOH   A O   1 
HETATM 5827 O  O   . HOH   L 5 .   ? 21.333  -23.830 -13.037 1.00 25.54 ? 980  HOH   A O   1 
HETATM 5828 O  O   . HOH   L 5 .   ? 7.222   -28.551 -11.841 1.00 22.87 ? 981  HOH   A O   1 
HETATM 5829 O  O   . HOH   L 5 .   ? 0.201   5.705   -30.859 1.00 24.08 ? 982  HOH   A O   1 
HETATM 5830 O  O   . HOH   L 5 .   ? 3.928   13.065  -33.849 1.00 36.55 ? 983  HOH   A O   1 
HETATM 5831 O  O   . HOH   L 5 .   ? 17.217  -0.181  -10.578 1.00 17.43 ? 984  HOH   A O   1 
HETATM 5832 O  O   . HOH   L 5 .   ? 28.490  15.609  -30.618 1.00 43.13 ? 985  HOH   A O   1 
HETATM 5833 O  O   . HOH   L 5 .   ? 20.052  3.003   -49.010 1.00 32.88 ? 986  HOH   A O   1 
HETATM 5834 O  O   . HOH   L 5 .   ? 10.775  -32.494 -19.369 1.00 43.29 ? 987  HOH   A O   1 
HETATM 5835 O  O   . HOH   L 5 .   ? 4.720   2.353   -26.804 1.00 20.00 ? 988  HOH   A O   1 
HETATM 5836 O  O   . HOH   L 5 .   ? 28.931  -12.145 -34.627 1.00 19.04 ? 989  HOH   A O   1 
HETATM 5837 O  O   . HOH   L 5 .   ? -2.438  -6.243  -22.672 1.00 32.12 ? 990  HOH   A O   1 
HETATM 5838 O  O   . HOH   L 5 .   ? 24.069  23.937  -8.270  1.00 48.57 ? 991  HOH   A O   1 
HETATM 5839 O  O   . HOH   L 5 .   ? 4.225   -16.467 -31.759 1.00 29.91 ? 992  HOH   A O   1 
HETATM 5840 O  O   . HOH   L 5 .   ? 25.378  7.160   -37.844 1.00 20.93 ? 993  HOH   A O   1 
HETATM 5841 O  O   . HOH   L 5 .   ? 34.684  -1.504  -6.278  1.00 23.53 ? 994  HOH   A O   1 
HETATM 5842 O  O   . HOH   L 5 .   ? 2.827   -11.619 -24.592 1.00 16.57 ? 995  HOH   A O   1 
HETATM 5843 O  O   . HOH   L 5 .   ? 18.457  -17.677 -12.964 1.00 17.56 ? 996  HOH   A O   1 
HETATM 5844 O  O   . HOH   L 5 .   ? 8.329   6.842   -39.005 1.00 23.56 ? 997  HOH   A O   1 
HETATM 5845 O  O   . HOH   L 5 .   ? 6.230   16.777  -21.303 1.00 25.86 ? 998  HOH   A O   1 
HETATM 5846 O  O   . HOH   L 5 .   ? 28.236  -9.623  -39.013 1.00 19.78 ? 999  HOH   A O   1 
HETATM 5847 O  O   . HOH   L 5 .   ? 18.994  18.382  -27.090 1.00 23.66 ? 1000 HOH   A O   1 
HETATM 5848 O  O   . HOH   L 5 .   ? 29.800  -17.763 -16.870 1.00 29.40 ? 1001 HOH   A O   1 
HETATM 5849 O  O   . HOH   L 5 .   ? 25.343  19.874  -25.390 1.00 30.16 ? 1002 HOH   A O   1 
HETATM 5850 O  O   . HOH   L 5 .   ? 14.187  21.310  -24.000 1.00 27.78 ? 1003 HOH   A O   1 
HETATM 5851 O  O   . HOH   L 5 .   ? 31.587  1.208   -39.494 1.00 23.61 ? 1004 HOH   A O   1 
HETATM 5852 O  O   . HOH   L 5 .   ? 32.794  9.861   -29.997 1.00 31.06 ? 1005 HOH   A O   1 
HETATM 5853 O  O   . HOH   L 5 .   ? 22.347  13.016  -44.649 1.00 46.27 ? 1006 HOH   A O   1 
HETATM 5854 O  O   . HOH   L 5 .   ? 22.389  -24.026 -25.850 1.00 24.69 ? 1007 HOH   A O   1 
HETATM 5855 O  O   . HOH   L 5 .   ? 14.857  7.776   -3.746  1.00 29.53 ? 1008 HOH   A O   1 
HETATM 5856 O  O   . HOH   L 5 .   ? 4.889   6.300   -22.234 1.00 16.13 ? 1009 HOH   A O   1 
HETATM 5857 O  O   . HOH   L 5 .   ? 4.738   -19.039 -21.453 1.00 23.09 ? 1010 HOH   A O   1 
HETATM 5858 O  O   . HOH   L 5 .   ? 6.069   -22.448 -31.221 1.00 47.31 ? 1011 HOH   A O   1 
HETATM 5859 O  O   . HOH   L 5 .   ? 37.586  -2.135  -17.973 1.00 40.29 ? 1012 HOH   A O   1 
HETATM 5860 O  O   . HOH   L 5 .   ? 9.560   -11.418 -22.410 1.00 44.60 ? 1013 HOH   A O   1 
HETATM 5861 O  O   . HOH   L 5 .   ? 35.021  10.493  -15.906 1.00 32.97 ? 1014 HOH   A O   1 
HETATM 5862 O  O   . HOH   L 5 .   ? 6.452   15.346  -26.023 1.00 22.28 ? 1015 HOH   A O   1 
HETATM 5863 O  O   . HOH   L 5 .   ? 19.932  6.304   -47.060 1.00 38.08 ? 1016 HOH   A O   1 
HETATM 5864 O  O   . HOH   L 5 .   ? 8.875   22.134  -40.409 1.00 42.97 ? 1017 HOH   A O   1 
HETATM 5865 O  O   . HOH   L 5 .   ? 23.848  -21.562 -29.372 1.00 24.65 ? 1018 HOH   A O   1 
HETATM 5866 O  O   . HOH   L 5 .   ? 2.001   0.373   -36.810 1.00 28.09 ? 1019 HOH   A O   1 
HETATM 5867 O  O   . HOH   L 5 .   ? 31.271  -18.877 -29.342 1.00 46.52 ? 1020 HOH   A O   1 
HETATM 5868 O  O   . HOH   L 5 .   ? 1.660   -4.844  -26.703 1.00 20.74 ? 1021 HOH   A O   1 
HETATM 5869 O  O   . HOH   L 5 .   ? -0.144  -17.859 -25.609 1.00 29.53 ? 1022 HOH   A O   1 
HETATM 5870 O  O   . HOH   L 5 .   ? 7.230   20.314  -13.339 1.00 33.06 ? 1023 HOH   A O   1 
HETATM 5871 O  O   . HOH   L 5 .   ? 12.109  -6.558  -27.174 1.00 11.43 ? 1024 HOH   A O   1 
HETATM 5872 O  O   . HOH   L 5 .   ? 12.597  3.450   -50.505 1.00 29.14 ? 1025 HOH   A O   1 
HETATM 5873 O  O   . HOH   L 5 .   ? 27.390  0.969   -14.960 1.00 15.40 ? 1026 HOH   A O   1 
HETATM 5874 O  O   . HOH   L 5 .   ? 5.393   8.873   -40.739 1.00 35.71 ? 1027 HOH   A O   1 
HETATM 5875 O  O   . HOH   L 5 .   ? 7.531   -13.843 -12.751 1.00 15.40 ? 1028 HOH   A O   1 
HETATM 5876 O  O   . HOH   L 5 .   ? 9.229   -4.838  -8.597  1.00 33.85 ? 1029 HOH   A O   1 
HETATM 5877 O  O   . HOH   L 5 .   ? 23.668  7.368   -43.012 1.00 27.01 ? 1030 HOH   A O   1 
HETATM 5878 O  O   . HOH   L 5 .   ? 25.993  -23.278 -17.953 1.00 27.22 ? 1031 HOH   A O   1 
HETATM 5879 O  O   . HOH   L 5 .   ? 17.177  -27.032 -14.837 1.00 32.22 ? 1032 HOH   A O   1 
HETATM 5880 O  O   . HOH   L 5 .   ? 5.202   -7.679  -44.971 1.00 45.73 ? 1033 HOH   A O   1 
HETATM 5881 O  O   . HOH   L 5 .   ? 6.107   17.612  -9.997  1.00 40.92 ? 1034 HOH   A O   1 
HETATM 5882 O  O   . HOH   L 5 .   ? 14.260  -4.721  -8.275  1.00 40.61 ? 1035 HOH   A O   1 
HETATM 5883 O  O   . HOH   L 5 .   ? 19.890  -16.421 -40.195 1.00 42.67 ? 1036 HOH   A O   1 
HETATM 5884 O  O   . HOH   L 5 .   ? 14.138  -22.471 -26.253 1.00 19.20 ? 1037 HOH   A O   1 
HETATM 5885 O  O   . HOH   L 5 .   ? 6.221   17.569  -34.835 1.00 38.39 ? 1038 HOH   A O   1 
HETATM 5886 O  O   . HOH   L 5 .   ? 2.178   -13.928 -17.036 1.00 25.04 ? 1039 HOH   A O   1 
HETATM 5887 O  O   . HOH   L 5 .   ? 32.345  -14.793 -30.066 1.00 27.40 ? 1040 HOH   A O   1 
HETATM 5888 O  O   . HOH   L 5 .   ? 5.955   0.631   -11.810 1.00 27.76 ? 1041 HOH   A O   1 
HETATM 5889 O  O   . HOH   L 5 .   ? 26.582  -26.792 -21.949 1.00 45.20 ? 1042 HOH   A O   1 
HETATM 5890 O  O   . HOH   L 5 .   ? 20.006  11.750  -40.161 1.00 23.61 ? 1043 HOH   A O   1 
HETATM 5891 O  O   . HOH   L 5 .   ? 28.730  -9.842  -15.668 1.00 29.22 ? 1044 HOH   A O   1 
HETATM 5892 O  O   . HOH   L 5 .   ? 6.455   8.169   -29.899 1.00 16.83 ? 1045 HOH   A O   1 
HETATM 5893 O  O   . HOH   L 5 .   ? 24.431  8.792   -11.814 1.00 20.34 ? 1046 HOH   A O   1 
HETATM 5894 O  O   . HOH   L 5 .   ? 37.936  4.744   -7.841  1.00 32.55 ? 1047 HOH   A O   1 
HETATM 5895 O  O   . HOH   L 5 .   ? 34.796  -9.287  -23.915 1.00 24.91 ? 1048 HOH   A O   1 
HETATM 5896 O  O   . HOH   L 5 .   ? 18.423  5.051   -49.455 1.00 52.19 ? 1049 HOH   A O   1 
HETATM 5897 O  O   . HOH   L 5 .   ? 12.882  -21.898 -23.326 1.00 16.69 ? 1050 HOH   A O   1 
HETATM 5898 O  O   . HOH   L 5 .   ? 13.402  15.407  -9.466  1.00 30.40 ? 1051 HOH   A O   1 
HETATM 5899 O  O   . HOH   L 5 .   ? 34.852  -10.556 -36.619 1.00 34.45 ? 1052 HOH   A O   1 
HETATM 5900 O  O   . HOH   L 5 .   ? 36.543  -6.518  -35.387 1.00 24.91 ? 1053 HOH   A O   1 
HETATM 5901 O  O   . HOH   L 5 .   ? 0.557   -13.303 -30.281 1.00 24.56 ? 1054 HOH   A O   1 
HETATM 5902 O  O   . HOH   L 5 .   ? 22.936  4.824   -44.255 1.00 23.65 ? 1055 HOH   A O   1 
HETATM 5903 O  O   . HOH   L 5 .   ? 26.307  20.815  -19.341 1.00 29.46 ? 1056 HOH   A O   1 
HETATM 5904 O  O   . HOH   L 5 .   ? 6.644   -1.075  -49.383 1.00 27.82 ? 1057 HOH   A O   1 
HETATM 5905 O  O   . HOH   L 5 .   ? 20.074  -25.826 -14.434 1.00 28.28 ? 1058 HOH   A O   1 
HETATM 5906 O  O   . HOH   L 5 .   ? 20.793  -26.774 -18.959 1.00 26.33 ? 1059 HOH   A O   1 
HETATM 5907 O  O   . HOH   L 5 .   ? 3.175   -1.682  -38.100 1.00 15.20 ? 1060 HOH   A O   1 
HETATM 5908 O  O   . HOH   L 5 .   ? 5.094   0.888   -50.472 1.00 28.34 ? 1061 HOH   A O   1 
HETATM 5909 O  O   . HOH   L 5 .   ? 3.771   7.742   -30.226 1.00 19.80 ? 1062 HOH   A O   1 
HETATM 5910 O  O   . HOH   L 5 .   ? 16.509  -11.737 -23.121 1.00 13.50 ? 1063 HOH   A O   1 
HETATM 5911 O  O   . HOH   L 5 .   ? 40.633  -3.727  -20.596 1.00 46.55 ? 1064 HOH   A O   1 
HETATM 5912 O  O   . HOH   L 5 .   ? 4.167   21.196  -19.015 1.00 39.02 ? 1065 HOH   A O   1 
HETATM 5913 O  O   . HOH   L 5 .   ? 2.586   -14.128 -25.709 1.00 18.48 ? 1066 HOH   A O   1 
HETATM 5914 O  O   . HOH   L 5 .   ? 4.895   10.661  -36.341 1.00 33.43 ? 1067 HOH   A O   1 
HETATM 5915 O  O   . HOH   L 5 .   ? 5.944   -23.824 -24.501 1.00 22.67 ? 1068 HOH   A O   1 
HETATM 5916 O  O   . HOH   L 5 .   ? 30.237  2.630   -13.581 1.00 17.00 ? 1069 HOH   A O   1 
HETATM 5917 O  O   . HOH   L 5 .   ? 16.833  -4.938  -45.993 1.00 38.20 ? 1070 HOH   A O   1 
HETATM 5918 O  O   . HOH   L 5 .   ? 20.369  4.515   -1.948  1.00 29.85 ? 1071 HOH   A O   1 
HETATM 5919 O  O   . HOH   L 5 .   ? 32.071  11.375  -33.917 1.00 28.68 ? 1072 HOH   A O   1 
HETATM 5920 O  O   . HOH   L 5 .   ? 31.314  -4.029  -13.351 1.00 21.11 ? 1073 HOH   A O   1 
HETATM 5921 O  O   . HOH   L 5 .   ? 30.096  -13.742 -16.525 1.00 32.25 ? 1074 HOH   A O   1 
HETATM 5922 O  O   . HOH   L 5 .   ? 39.493  0.614   -19.958 1.00 37.55 ? 1075 HOH   A O   1 
HETATM 5923 O  O   . HOH   L 5 .   ? 18.436  17.216  -32.514 1.00 33.47 ? 1076 HOH   A O   1 
HETATM 5924 O  O   . HOH   L 5 .   ? 30.586  -8.456  -18.223 1.00 21.83 ? 1077 HOH   A O   1 
HETATM 5925 O  O   . HOH   L 5 .   ? 13.304  -17.151 -39.902 1.00 27.10 ? 1078 HOH   A O   1 
HETATM 5926 O  O   . HOH   L 5 .   ? 16.053  0.453   -3.127  1.00 25.39 ? 1079 HOH   A O   1 
HETATM 5927 O  O   . HOH   L 5 .   ? 0.442   -14.147 -27.492 1.00 20.89 ? 1080 HOH   A O   1 
HETATM 5928 O  O   . HOH   L 5 .   ? 2.537   -25.142 -9.549  1.00 33.07 ? 1081 HOH   A O   1 
HETATM 5929 O  O   . HOH   L 5 .   ? 39.017  -12.139 -27.884 1.00 40.32 ? 1082 HOH   A O   1 
HETATM 5930 O  O   . HOH   L 5 .   ? 10.632  25.448  -17.357 1.00 30.38 ? 1083 HOH   A O   1 
HETATM 5931 O  O   . HOH   L 5 .   ? 18.138  -16.533 -10.365 1.00 22.71 ? 1084 HOH   A O   1 
HETATM 5932 O  O   . HOH   L 5 .   ? 25.557  -2.753  -6.506  1.00 39.26 ? 1085 HOH   A O   1 
HETATM 5933 O  O   . HOH   L 5 .   ? 2.283   4.866   -44.279 1.00 20.41 ? 1086 HOH   A O   1 
HETATM 5934 O  O   . HOH   L 5 .   ? 38.799  -11.286 -25.264 1.00 43.66 ? 1087 HOH   A O   1 
HETATM 5935 O  O   . HOH   L 5 .   ? 33.070  -16.281 -22.266 1.00 28.22 ? 1088 HOH   A O   1 
HETATM 5936 O  O   . HOH   L 5 .   ? 32.847  -13.141 -27.750 1.00 32.98 ? 1089 HOH   A O   1 
HETATM 5937 O  O   . HOH   L 5 .   ? 0.824   8.672   -23.551 1.00 30.75 ? 1090 HOH   A O   1 
HETATM 5938 O  O   . HOH   L 5 .   ? 13.192  -19.019 -32.072 1.00 30.27 ? 1091 HOH   A O   1 
HETATM 5939 O  O   . HOH   L 5 .   ? 19.800  -15.668 -8.414  1.00 35.71 ? 1092 HOH   A O   1 
HETATM 5940 O  O   . HOH   L 5 .   ? 9.214   -13.005 -19.899 1.00 13.09 ? 1093 HOH   A O   1 
HETATM 5941 O  O   . HOH   L 5 .   ? 18.780  -12.031 -24.919 1.00 21.39 ? 1094 HOH   A O   1 
HETATM 5942 O  O   . HOH   L 5 .   ? 17.819  20.153  -8.338  1.00 40.80 ? 1095 HOH   A O   1 
HETATM 5943 O  O   . HOH   L 5 .   ? 18.600  7.145   -3.300  1.00 26.02 ? 1096 HOH   A O   1 
HETATM 5944 O  O   . HOH   L 5 .   ? 30.342  19.224  -24.981 1.00 36.11 ? 1097 HOH   A O   1 
HETATM 5945 O  O   . HOH   L 5 .   ? 28.852  -20.783 -20.878 1.00 26.06 ? 1098 HOH   A O   1 
HETATM 5946 O  O   . HOH   L 5 .   ? 25.256  -19.746 -33.816 1.00 38.42 ? 1099 HOH   A O   1 
HETATM 5947 O  O   . HOH   L 5 .   ? 37.138  -1.338  -9.494  1.00 24.88 ? 1100 HOH   A O   1 
HETATM 5948 O  O   . HOH   L 5 .   ? 8.146   11.372  -13.907 1.00 21.78 ? 1101 HOH   A O   1 
HETATM 5949 O  O   . HOH   L 5 .   ? 27.233  -20.079 -11.688 1.00 22.12 ? 1102 HOH   A O   1 
HETATM 5950 O  O   . HOH   L 5 .   ? -4.369  -14.360 -28.038 1.00 44.41 ? 1103 HOH   A O   1 
HETATM 5951 O  O   . HOH   L 5 .   ? 3.421   1.326   -48.461 1.00 20.91 ? 1104 HOH   A O   1 
HETATM 5952 O  O   . HOH   L 5 .   ? -2.647  3.309   -24.423 1.00 38.79 ? 1105 HOH   A O   1 
HETATM 5953 O  O   . HOH   L 5 .   ? -0.356  1.299   -16.631 1.00 22.30 ? 1106 HOH   A O   1 
HETATM 5954 O  O   . HOH   L 5 .   ? 7.114   -31.403 -13.438 1.00 28.78 ? 1107 HOH   A O   1 
HETATM 5955 O  O   . HOH   L 5 .   ? 26.886  3.137   -8.261  1.00 22.66 ? 1108 HOH   A O   1 
HETATM 5956 O  O   . HOH   L 5 .   ? 23.494  -16.625 -39.460 1.00 26.74 ? 1109 HOH   A O   1 
HETATM 5957 O  O   . HOH   L 5 .   ? 35.802  -7.181  -22.150 1.00 27.05 ? 1110 HOH   A O   1 
HETATM 5958 O  O   . HOH   L 5 .   ? 27.423  -22.813 -20.332 1.00 32.20 ? 1111 HOH   A O   1 
HETATM 5959 O  O   . HOH   L 5 .   ? 6.152   -8.283  -40.286 1.00 18.41 ? 1112 HOH   A O   1 
HETATM 5960 O  O   . HOH   L 5 .   ? 6.614   -11.349 -10.614 1.00 24.44 ? 1113 HOH   A O   1 
HETATM 5961 O  O   . HOH   L 5 .   ? 28.121  5.524   -6.723  1.00 30.34 ? 1114 HOH   A O   1 
HETATM 5962 O  O   . HOH   L 5 .   ? 18.744  -6.578  -9.065  1.00 29.34 ? 1115 HOH   A O   1 
HETATM 5963 O  O   . HOH   L 5 .   ? 15.564  13.906  -45.646 1.00 31.67 ? 1116 HOH   A O   1 
HETATM 5964 O  O   . HOH   L 5 .   ? 6.306   22.536  -14.668 1.00 39.33 ? 1117 HOH   A O   1 
HETATM 5965 O  O   . HOH   L 5 .   ? 15.283  1.215   -51.682 1.00 43.50 ? 1118 HOH   A O   1 
HETATM 5966 O  O   . HOH   L 5 .   ? 2.039   17.597  -20.280 1.00 39.43 ? 1119 HOH   A O   1 
HETATM 5967 O  O   . HOH   L 5 .   ? 15.893  -19.735 -10.878 1.00 22.05 ? 1120 HOH   A O   1 
HETATM 5968 O  O   . HOH   L 5 .   ? -2.415  -7.469  -25.886 1.00 25.19 ? 1121 HOH   A O   1 
HETATM 5969 O  O   . HOH   L 5 .   ? 29.504  -18.829 -13.336 1.00 29.49 ? 1122 HOH   A O   1 
HETATM 5970 O  O   . HOH   L 5 .   ? 35.697  -4.404  -9.871  1.00 40.78 ? 1123 HOH   A O   1 
HETATM 5971 O  O   . HOH   L 5 .   ? 34.560  1.660   -40.386 1.00 40.71 ? 1124 HOH   A O   1 
HETATM 5972 O  O   . HOH   L 5 .   ? 13.338  -23.474 -29.349 1.00 34.41 ? 1125 HOH   A O   1 
HETATM 5973 O  O   . HOH   L 5 .   ? 4.868   -16.939 -34.779 1.00 31.84 ? 1126 HOH   A O   1 
HETATM 5974 O  O   . HOH   L 5 .   ? 14.718  10.355  -47.819 1.00 44.20 ? 1127 HOH   A O   1 
HETATM 5975 O  O   . HOH   L 5 .   ? 6.619   -18.772 -16.849 1.00 19.12 ? 1128 HOH   A O   1 
HETATM 5976 O  O   . HOH   L 5 .   ? 15.438  11.546  -7.782  1.00 22.94 ? 1129 HOH   A O   1 
HETATM 5977 O  O   . HOH   L 5 .   ? 33.744  2.670   -4.908  1.00 21.67 ? 1130 HOH   A O   1 
HETATM 5978 O  O   . HOH   L 5 .   ? 11.084  -1.604  -48.076 1.00 20.94 ? 1131 HOH   A O   1 
HETATM 5979 O  O   . HOH   L 5 .   ? 2.693   16.188  -16.036 1.00 27.28 ? 1132 HOH   A O   1 
HETATM 5980 O  O   . HOH   L 5 .   ? 40.039  3.698   -23.711 1.00 37.51 ? 1133 HOH   A O   1 
HETATM 5981 O  O   . HOH   L 5 .   ? 0.964   -29.827 -9.485  1.00 39.79 ? 1134 HOH   A O   1 
HETATM 5982 O  O   . HOH   L 5 .   ? 42.621  -6.520  -25.733 1.00 32.57 ? 1135 HOH   A O   1 
HETATM 5983 O  O   . HOH   L 5 .   ? 10.792  -0.201  -51.616 1.00 33.63 ? 1136 HOH   A O   1 
HETATM 5984 O  O   . HOH   L 5 .   ? 3.617   7.959   -42.653 1.00 33.05 ? 1137 HOH   A O   1 
HETATM 5985 O  O   . HOH   L 5 .   ? -1.958  -7.385  -32.340 1.00 18.96 ? 1138 HOH   A O   1 
HETATM 5986 O  O   . HOH   L 5 .   ? 29.596  18.889  -7.725  1.00 46.72 ? 1139 HOH   A O   1 
HETATM 5987 O  O   . HOH   L 5 .   ? 12.324  -13.502 -40.683 1.00 20.89 ? 1140 HOH   A O   1 
HETATM 5988 O  O   . HOH   L 5 .   ? 16.792  11.662  -4.063  1.00 37.13 ? 1141 HOH   A O   1 
HETATM 5989 O  O   . HOH   L 5 .   ? 10.561  -23.676 -32.574 1.00 28.68 ? 1142 HOH   A O   1 
HETATM 5990 O  O   . HOH   L 5 .   ? 11.173  16.817  -9.073  1.00 46.41 ? 1143 HOH   A O   1 
HETATM 5991 O  O   . HOH   L 5 .   ? 24.508  -24.438 -19.756 1.00 28.45 ? 1144 HOH   A O   1 
HETATM 5992 O  O   . HOH   L 5 .   ? 2.780   3.041   -36.648 1.00 22.36 ? 1145 HOH   A O   1 
HETATM 5993 O  O   . HOH   L 5 .   ? 26.162  -22.711 -27.711 1.00 30.46 ? 1146 HOH   A O   1 
HETATM 5994 O  O   . HOH   L 5 .   ? 30.416  11.351  -38.659 1.00 44.01 ? 1147 HOH   A O   1 
HETATM 5995 O  O   . HOH   L 5 .   ? 3.746   8.241   -10.390 1.00 38.39 ? 1148 HOH   A O   1 
HETATM 5996 O  O   . HOH   L 5 .   ? 22.167  -19.601 -35.667 1.00 28.10 ? 1149 HOH   A O   1 
HETATM 5997 O  O   . HOH   L 5 .   ? 2.794   -7.556  -37.731 1.00 22.36 ? 1150 HOH   A O   1 
HETATM 5998 O  O   . HOH   L 5 .   ? -4.360  -16.659 -22.219 1.00 45.79 ? 1151 HOH   A O   1 
HETATM 5999 O  O   . HOH   L 5 .   ? 27.838  -6.819  -43.571 1.00 46.45 ? 1152 HOH   A O   1 
HETATM 6000 O  O   . HOH   L 5 .   ? 11.956  5.769   -46.891 1.00 28.74 ? 1153 HOH   A O   1 
HETATM 6001 O  O   . HOH   L 5 .   ? 23.389  -11.088 -10.575 1.00 23.11 ? 1154 HOH   A O   1 
HETATM 6002 O  O   . HOH   L 5 .   ? 2.999   -29.859 -16.638 1.00 27.28 ? 1155 HOH   A O   1 
HETATM 6003 O  O   . HOH   L 5 .   ? 29.466  -22.280 -26.429 1.00 27.04 ? 1156 HOH   A O   1 
HETATM 6004 O  O   . HOH   L 5 .   ? 18.269  25.371  -13.739 1.00 31.57 ? 1157 HOH   A O   1 
HETATM 6005 O  O   . HOH   L 5 .   ? 23.724  21.576  -10.652 1.00 37.22 ? 1158 HOH   A O   1 
HETATM 6006 O  O   . HOH   L 5 .   ? 15.362  -7.145  -46.189 1.00 22.85 ? 1159 HOH   A O   1 
HETATM 6007 O  O   . HOH   L 5 .   ? 9.779   7.114   -45.643 1.00 44.75 ? 1160 HOH   A O   1 
HETATM 6008 O  O   . HOH   L 5 .   ? 26.090  -24.180 -13.630 1.00 44.49 ? 1161 HOH   A O   1 
HETATM 6009 O  O   . HOH   L 5 .   ? 18.128  -2.443  -9.224  1.00 21.36 ? 1162 HOH   A O   1 
HETATM 6010 O  O   . HOH   L 5 .   ? 6.736   -26.952 -27.093 1.00 52.39 ? 1163 HOH   A O   1 
HETATM 6011 O  O   . HOH   L 5 .   ? -0.699  -6.351  -34.591 1.00 18.62 ? 1164 HOH   A O   1 
HETATM 6012 O  O   . HOH   L 5 .   ? 28.456  12.452  -6.530  1.00 31.39 ? 1165 HOH   A O   1 
HETATM 6013 O  O   . HOH   L 5 .   ? 20.539  -11.246 -44.761 1.00 42.14 ? 1166 HOH   A O   1 
HETATM 6014 O  O   . HOH   L 5 .   ? 4.064   -10.004 -16.074 1.00 30.10 ? 1167 HOH   A O   1 
HETATM 6015 O  O   . HOH   L 5 .   ? 42.547  -3.205  -24.453 1.00 32.52 ? 1168 HOH   A O   1 
HETATM 6016 O  O   . HOH   L 5 .   ? 11.620  -11.510 -42.620 1.00 31.03 ? 1169 HOH   A O   1 
HETATM 6017 O  O   . HOH   L 5 .   ? 20.126  -1.446  -49.247 1.00 36.15 ? 1170 HOH   A O   1 
HETATM 6018 O  O   . HOH   L 5 .   ? 39.349  -4.229  -12.420 1.00 32.84 ? 1171 HOH   A O   1 
HETATM 6019 O  O   . HOH   L 5 .   ? 38.525  -10.083 -34.201 1.00 35.78 ? 1172 HOH   A O   1 
HETATM 6020 O  O   . HOH   L 5 .   ? 1.139   6.649   -15.338 1.00 38.63 ? 1173 HOH   A O   1 
HETATM 6021 O  O   . HOH   L 5 .   ? 12.778  2.081   -4.008  1.00 39.89 ? 1174 HOH   A O   1 
HETATM 6022 O  O   . HOH   L 5 .   ? 18.002  -12.915 -40.735 1.00 30.03 ? 1175 HOH   A O   1 
HETATM 6023 O  O   . HOH   L 5 .   ? 36.327  -4.678  -17.970 1.00 42.28 ? 1176 HOH   A O   1 
HETATM 6024 O  O   . HOH   L 5 .   ? 16.944  21.913  -17.712 1.00 28.52 ? 1177 HOH   A O   1 
HETATM 6025 O  O   . HOH   L 5 .   ? 26.492  10.844  -5.447  1.00 37.26 ? 1178 HOH   A O   1 
HETATM 6026 O  O   . HOH   L 5 .   ? 18.735  -23.581 -28.450 1.00 36.98 ? 1179 HOH   A O   1 
HETATM 6027 O  O   . HOH   L 5 .   ? 30.732  14.956  -31.138 1.00 42.98 ? 1180 HOH   A O   1 
HETATM 6028 O  O   . HOH   L 5 .   ? -0.052  8.144   -29.733 1.00 36.20 ? 1181 HOH   A O   1 
HETATM 6029 O  O   . HOH   L 5 .   ? 4.468   -31.562 -14.653 1.00 39.52 ? 1182 HOH   A O   1 
HETATM 6030 O  O   . HOH   L 5 .   ? 6.241   17.285  -28.249 1.00 34.49 ? 1183 HOH   A O   1 
HETATM 6031 O  O   . HOH   L 5 .   ? 4.119   -18.749 -30.218 1.00 38.29 ? 1184 HOH   A O   1 
HETATM 6032 O  O   . HOH   L 5 .   ? 8.820   -11.788 -42.011 1.00 31.38 ? 1185 HOH   A O   1 
HETATM 6033 O  O   . HOH   L 5 .   ? 34.876  -15.646 -24.161 1.00 35.40 ? 1186 HOH   A O   1 
HETATM 6034 O  O   . HOH   L 5 .   ? 23.574  -26.932 -19.514 1.00 37.26 ? 1187 HOH   A O   1 
HETATM 6035 O  O   . HOH   L 5 .   ? 3.716   15.111  -36.175 1.00 47.77 ? 1188 HOH   A O   1 
HETATM 6036 O  O   . HOH   L 5 .   ? 4.626   -12.977 -16.097 1.00 40.31 ? 1189 HOH   A O   1 
HETATM 6037 O  O   . HOH   L 5 .   ? -3.276  -8.806  -28.131 1.00 35.03 ? 1190 HOH   A O   1 
HETATM 6038 O  O   . HOH   L 5 .   ? 4.016   -0.149  -52.540 1.00 27.77 ? 1191 HOH   A O   1 
HETATM 6039 O  O   . HOH   L 5 .   ? 23.170  -7.017  -8.791  1.00 40.42 ? 1192 HOH   A O   1 
HETATM 6040 O  O   . HOH   L 5 .   ? 25.787  1.551   -5.427  1.00 39.34 ? 1193 HOH   A O   1 
HETATM 6041 O  O   . HOH   L 5 .   ? 16.075  18.274  -5.157  1.00 44.37 ? 1194 HOH   A O   1 
HETATM 6042 O  O   . HOH   L 5 .   ? -0.881  8.945   -32.357 1.00 39.32 ? 1195 HOH   A O   1 
HETATM 6043 O  O   . HOH   L 5 .   ? 2.529   7.421   -32.564 1.00 31.28 ? 1196 HOH   A O   1 
HETATM 6044 O  O   . HOH   L 5 .   ? 19.030  -28.385 -23.278 1.00 38.80 ? 1197 HOH   A O   1 
HETATM 6045 O  O   . HOH   L 5 .   ? 5.241   16.793  -23.987 1.00 32.79 ? 1198 HOH   A O   1 
HETATM 6046 O  O   . HOH   L 5 .   ? 26.242  -4.213  -48.548 1.00 39.86 ? 1199 HOH   A O   1 
HETATM 6047 O  O   . HOH   L 5 .   ? 14.866  -21.191 -7.036  1.00 32.78 ? 1200 HOH   A O   1 
HETATM 6048 O  O   . HOH   L 5 .   ? 35.036  -13.136 -35.510 1.00 32.48 ? 1201 HOH   A O   1 
HETATM 6049 O  O   . HOH   L 5 .   ? 32.630  -9.452  -40.497 1.00 43.22 ? 1202 HOH   A O   1 
HETATM 6050 O  O   . HOH   L 5 .   ? 35.717  -5.478  -12.213 1.00 36.40 ? 1203 HOH   A O   1 
HETATM 6051 O  O   . HOH   L 5 .   ? 36.848  -8.928  -36.039 1.00 29.96 ? 1204 HOH   A O   1 
HETATM 6052 O  O   . HOH   L 5 .   ? 17.169  23.422  -20.084 1.00 42.54 ? 1205 HOH   A O   1 
HETATM 6053 O  O   . HOH   L 5 .   ? 0.834   7.147   -39.485 1.00 42.83 ? 1206 HOH   A O   1 
HETATM 6054 O  O   . HOH   L 5 .   ? -1.323  -0.501  -26.396 1.00 17.08 ? 1207 HOH   A O   1 
HETATM 6055 O  O   . HOH   L 5 .   ? 28.570  15.086  -5.412  1.00 44.16 ? 1208 HOH   A O   1 
HETATM 6056 O  O   . HOH   L 5 .   ? 30.110  -8.531  -40.611 1.00 32.11 ? 1209 HOH   A O   1 
HETATM 6057 O  O   . HOH   L 5 .   ? 33.967  -14.880 -20.620 1.00 43.94 ? 1210 HOH   A O   1 
HETATM 6058 O  O   . HOH   L 5 .   ? 16.017  -33.256 -24.199 1.00 44.07 ? 1211 HOH   A O   1 
HETATM 6059 O  O   . HOH   L 5 .   ? 30.431  11.170  -5.098  1.00 36.61 ? 1212 HOH   A O   1 
HETATM 6060 O  O   . HOH   L 5 .   ? 29.165  -20.565 -18.318 1.00 40.06 ? 1213 HOH   A O   1 
HETATM 6061 O  O   . HOH   L 5 .   ? 9.112   -1.321  -50.170 1.00 43.74 ? 1214 HOH   A O   1 
HETATM 6062 O  O   . HOH   L 5 .   ? 26.965  -27.786 -24.408 1.00 44.85 ? 1215 HOH   A O   1 
HETATM 6063 O  O   . HOH   L 5 .   ? 13.700  3.259   -11.268 1.00 23.78 ? 1216 HOH   A O   1 
HETATM 6064 O  O   . HOH   L 5 .   ? 31.653  -20.776 -13.580 1.00 44.56 ? 1217 HOH   A O   1 
HETATM 6065 O  O   . HOH   L 5 .   ? 2.669   11.686  -14.360 1.00 39.80 ? 1218 HOH   A O   1 
HETATM 6066 O  O   . HOH   L 5 .   ? 14.120  -5.082  -49.136 1.00 46.53 ? 1219 HOH   A O   1 
HETATM 6067 O  O   . HOH   L 5 .   ? -0.234  5.697   -18.064 1.00 45.61 ? 1220 HOH   A O   1 
HETATM 6068 O  O   . HOH   L 5 .   ? 22.518  12.633  -40.690 1.00 28.83 ? 1221 HOH   A O   1 
HETATM 6069 O  O   . HOH   L 5 .   ? 28.665  -25.702 -20.262 1.00 48.19 ? 1222 HOH   A O   1 
HETATM 6070 O  O   . HOH   L 5 .   ? 11.603  -4.340  -48.836 1.00 44.44 ? 1223 HOH   A O   1 
HETATM 6071 O  O   . HOH   L 5 .   ? 24.835  16.643  -35.739 1.00 45.21 ? 1224 HOH   A O   1 
HETATM 6072 O  O   . HOH   L 5 .   ? 1.717   14.256  -14.090 1.00 40.33 ? 1225 HOH   A O   1 
HETATM 6073 O  O   . HOH   L 5 .   ? 16.462  -10.226 -47.130 1.00 38.18 ? 1226 HOH   A O   1 
HETATM 6074 O  O   . HOH   L 5 .   ? 38.749  -4.700  -16.892 1.00 46.86 ? 1227 HOH   A O   1 
HETATM 6075 O  O   . HOH   L 5 .   ? 30.873  -21.916 -28.818 1.00 31.41 ? 1228 HOH   A O   1 
HETATM 6076 O  O   . HOH   L 5 .   ? 20.548  -25.956 -25.946 1.00 36.19 ? 1229 HOH   A O   1 
HETATM 6077 O  O   . HOH   L 5 .   ? 26.590  -8.010  -11.005 1.00 38.84 ? 1230 HOH   A O   1 
HETATM 6078 O  O   . HOH   L 5 .   ? 33.948  -5.094  -14.315 1.00 43.37 ? 1231 HOH   A O   1 
HETATM 6079 O  O   . HOH   L 5 .   ? 30.865  -11.401 -15.616 1.00 32.12 ? 1232 HOH   A O   1 
HETATM 6080 O  O   . HOH   L 5 .   ? 26.207  -8.950  -42.737 1.00 44.82 ? 1233 HOH   A O   1 
HETATM 6081 O  O   . HOH   L 5 .   ? -2.405  -19.505 -25.550 1.00 47.83 ? 1234 HOH   A O   1 
HETATM 6082 O  O   . HOH   L 5 .   ? 6.688   20.041  -10.491 1.00 44.34 ? 1235 HOH   A O   1 
HETATM 6083 O  O   . HOH   L 5 .   ? 13.252  25.471  -13.726 1.00 31.30 ? 1236 HOH   A O   1 
HETATM 6084 O  O   . HOH   L 5 .   ? -3.407  5.794   -28.114 1.00 41.01 ? 1237 HOH   A O   1 
HETATM 6085 O  O   . HOH   L 5 .   ? 7.227   13.919  -6.973  1.00 40.11 ? 1238 HOH   A O   1 
HETATM 6086 O  O   . HOH   L 5 .   ? 36.347  -14.205 -28.378 1.00 36.42 ? 1239 HOH   A O   1 
HETATM 6087 O  O   . HOH   L 5 .   ? 23.793  -25.221 -12.487 1.00 43.20 ? 1240 HOH   A O   1 
HETATM 6088 O  O   . HOH   L 5 .   ? 28.749  -8.608  -13.145 1.00 44.61 ? 1241 HOH   A O   1 
HETATM 6089 O  O   . HOH   L 5 .   ? -0.924  -5.057  -26.253 1.00 21.95 ? 1242 HOH   A O   1 
HETATM 6090 O  O   . HOH   L 5 .   ? 36.114  6.503   -33.015 1.00 36.04 ? 1243 HOH   A O   1 
HETATM 6091 O  O   . HOH   L 5 .   ? 11.010  2.463   -52.659 1.00 31.46 ? 1244 HOH   A O   1 
HETATM 6092 O  O   . HOH   L 5 .   ? -6.193  -15.381 -21.844 1.00 49.03 ? 1245 HOH   A O   1 
HETATM 6093 O  O   . HOH   L 5 .   ? 7.873   -10.786 -7.962  1.00 44.95 ? 1246 HOH   A O   1 
HETATM 6094 O  O   . HOH   L 5 .   ? 30.262  -23.734 -24.265 1.00 39.81 ? 1247 HOH   A O   1 
HETATM 6095 O  O   . HOH   L 5 .   ? 36.147  -11.922 -24.401 1.00 41.71 ? 1248 HOH   A O   1 
HETATM 6096 O  O   . HOH   L 5 .   ? 35.057  -14.225 -26.051 1.00 36.31 ? 1249 HOH   A O   1 
HETATM 6097 O  O   . HOH   L 5 .   ? 25.036  12.580  -38.725 1.00 43.40 ? 1250 HOH   A O   1 
HETATM 6098 O  O   . HOH   L 5 .   ? 24.907  23.974  -5.406  1.00 38.62 ? 1251 HOH   A O   1 
HETATM 6099 O  O   . HOH   L 5 .   ? 10.208  7.529   -43.371 1.00 44.30 ? 1252 HOH   A O   1 
HETATM 6100 O  O   . HOH   L 5 .   ? 29.022  21.440  -23.353 1.00 43.85 ? 1253 HOH   A O   1 
HETATM 6101 O  O   . HOH   L 5 .   ? 2.195   -4.169  -45.666 1.00 24.04 ? 1254 HOH   A O   1 
HETATM 6102 O  O   . HOH   L 5 .   ? 44.844  -2.064  -25.408 1.00 34.02 ? 1255 HOH   A O   1 
HETATM 6103 O  O   . HOH   L 5 .   ? 0.954   16.917  -18.242 1.00 39.67 ? 1256 HOH   A O   1 
HETATM 6104 O  O   . HOH   L 5 .   ? 1.844   -14.847 -32.191 1.00 31.66 ? 1257 HOH   A O   1 
HETATM 6105 O  O   . HOH   L 5 .   ? 33.514  -18.873 -21.197 1.00 39.03 ? 1258 HOH   A O   1 
HETATM 6106 O  O   . HOH   L 5 .   ? 16.109  -17.760 -9.211  1.00 26.86 ? 1259 HOH   A O   1 
HETATM 6107 O  O   . HOH   L 5 .   ? 13.011  13.375  -45.163 1.00 45.80 ? 1260 HOH   A O   1 
HETATM 6108 O  O   . HOH   L 5 .   ? 5.142   -12.401 -39.292 1.00 31.82 ? 1261 HOH   A O   1 
HETATM 6109 O  O   . HOH   L 5 .   ? 31.685  -21.020 -21.511 1.00 43.43 ? 1262 HOH   A O   1 
HETATM 6110 O  O   . HOH   L 5 .   ? 25.428  -11.861 -9.360  1.00 43.88 ? 1263 HOH   A O   1 
HETATM 6111 O  O   . HOH   L 5 .   ? 20.792  -10.419 -9.467  1.00 30.89 ? 1264 HOH   A O   1 
HETATM 6112 O  O   . HOH   L 5 .   ? 42.085  2.609   -19.465 1.00 42.86 ? 1265 HOH   A O   1 
HETATM 6113 O  O   . HOH   L 5 .   ? 23.616  -21.431 -34.502 1.00 27.14 ? 1266 HOH   A O   1 
HETATM 6114 O  O   . HOH   L 5 .   ? 1.509   -18.109 -29.621 1.00 37.66 ? 1267 HOH   A O   1 
HETATM 6115 O  O   . HOH   L 5 .   ? 11.840  6.548   -49.525 1.00 35.28 ? 1268 HOH   A O   1 
HETATM 6116 O  O   . HOH   L 5 .   ? 24.584  12.880  -5.583  1.00 42.22 ? 1269 HOH   A O   1 
HETATM 6117 O  O   . HOH   L 5 .   ? 4.523   21.985  -16.789 1.00 40.84 ? 1270 HOH   A O   1 
HETATM 6118 O  O   . HOH   L 5 .   ? 15.132  4.094   -51.911 1.00 40.32 ? 1271 HOH   A O   1 
HETATM 6119 O  O   . HOH   L 5 .   ? 13.036  -7.476  -47.882 1.00 30.60 ? 1272 HOH   A O   1 
HETATM 6120 O  O   . HOH   L 5 .   ? 9.607   8.051   -41.012 1.00 40.24 ? 1273 HOH   A O   1 
HETATM 6121 O  O   . HOH   L 5 .   ? 3.589   18.408  -14.675 1.00 40.76 ? 1274 HOH   A O   1 
HETATM 6122 O  O   . HOH   L 5 .   ? 18.613  -20.557 -10.398 1.00 33.58 ? 1275 HOH   A O   1 
HETATM 6123 O  O   . HOH   L 5 .   ? 15.088  -8.887  -10.218 1.00 35.54 ? 1276 HOH   A O   1 
HETATM 6124 O  O   . HOH   L 5 .   ? 28.839  4.016   -2.869  1.00 35.70 ? 1277 HOH   A O   1 
HETATM 6125 O  O   . HOH   L 5 .   ? 26.825  3.760   -5.191  1.00 42.62 ? 1278 HOH   A O   1 
HETATM 6126 O  O   . HOH   L 5 .   ? 7.937   -37.085 -16.426 1.00 43.76 ? 1279 HOH   A O   1 
HETATM 6127 O  O   . HOH   L 5 .   ? 1.846   21.953  -20.325 1.00 42.73 ? 1280 HOH   A O   1 
HETATM 6128 O  O   . HOH   L 5 .   ? 18.549  -12.548 -43.674 1.00 40.08 ? 1281 HOH   A O   1 
HETATM 6129 O  O   . HOH   L 5 .   ? 16.052  22.967  -22.628 1.00 44.03 ? 1282 HOH   A O   1 
HETATM 6130 O  O   . HOH   L 5 .   ? -2.517  -16.747 -29.292 1.00 41.30 ? 1283 HOH   A O   1 
HETATM 6131 O  O   . HOH   L 5 .   ? 32.684  -8.301  -14.211 1.00 44.82 ? 1284 HOH   A O   1 
HETATM 6132 O  O   . HOH   L 5 .   ? 0.045   -16.730 -27.777 1.00 33.17 ? 1285 HOH   A O   1 
HETATM 6133 O  O   . HOH   L 5 .   ? 12.230  23.456  -24.218 1.00 44.17 ? 1286 HOH   A O   1 
HETATM 6134 O  O   . HOH   L 5 .   ? 24.378  -22.555 -31.854 1.00 26.16 ? 1287 HOH   A O   1 
HETATM 6135 O  O   . HOH   L 5 .   ? 14.861  -21.981 -9.693  1.00 25.57 ? 1288 HOH   A O   1 
HETATM 6136 O  O   . HOH   L 5 .   ? 8.292   12.944  -40.601 1.00 37.42 ? 1289 HOH   A O   1 
HETATM 6137 O  O   . HOH   L 5 .   ? 21.591  -23.223 -29.217 1.00 41.39 ? 1290 HOH   A O   1 
HETATM 6138 O  O   . HOH   L 5 .   ? 16.622  -24.099 -9.189  1.00 36.61 ? 1291 HOH   A O   1 
HETATM 6139 O  O   . HOH   L 5 .   ? 33.494  -19.106 -18.596 1.00 36.28 ? 1292 HOH   A O   1 
HETATM 6140 O  O   . HOH   L 5 .   ? 3.598   20.803  -10.018 1.00 45.04 ? 1293 HOH   A O   1 
HETATM 6141 O  O   . HOH   M 5 .   ? -28.580 21.190  -53.695 1.00 44.89 ? 901  HOH   B O   1 
HETATM 6142 O  O   . HOH   M 5 .   ? -14.173 -20.227 -67.393 1.00 44.98 ? 902  HOH   B O   1 
HETATM 6143 O  O   . HOH   M 5 .   ? -7.894  -20.716 -66.237 1.00 41.64 ? 903  HOH   B O   1 
HETATM 6144 O  O   . HOH   M 5 .   ? -17.074 14.457  -70.199 1.00 44.80 ? 904  HOH   B O   1 
HETATM 6145 O  O   . HOH   M 5 .   ? -38.734 -11.102 -49.196 1.00 50.77 ? 905  HOH   B O   1 
HETATM 6146 O  O   . HOH   M 5 .   ? -27.347 -3.834  -65.220 1.00 31.04 ? 906  HOH   B O   1 
HETATM 6147 O  O   . HOH   M 5 .   ? 4.948   -13.135 -52.708 1.00 32.84 ? 907  HOH   B O   1 
HETATM 6148 O  O   . HOH   M 5 .   ? -8.429  -28.050 -62.737 1.00 42.13 ? 908  HOH   B O   1 
HETATM 6149 O  O   . HOH   M 5 .   ? -11.622 3.664   -64.829 1.00 26.99 ? 909  HOH   B O   1 
HETATM 6150 O  O   . HOH   M 5 .   ? -37.499 7.492   -65.566 1.00 30.99 ? 910  HOH   B O   1 
HETATM 6151 O  O   . HOH   M 5 .   ? -27.678 -7.624  -29.573 1.00 42.17 ? 911  HOH   B O   1 
HETATM 6152 O  O   . HOH   M 5 .   ? -14.186 -15.303 -66.280 1.00 38.77 ? 912  HOH   B O   1 
HETATM 6153 O  O   . HOH   M 5 .   ? -38.410 7.414   -58.927 1.00 36.81 ? 913  HOH   B O   1 
HETATM 6154 O  O   . HOH   M 5 .   ? -4.581  23.592  -46.246 1.00 46.47 ? 914  HOH   B O   1 
HETATM 6155 O  O   . HOH   M 5 .   ? -9.883  -18.841 -32.341 1.00 40.59 ? 915  HOH   B O   1 
HETATM 6156 O  O   . HOH   M 5 .   ? -9.916  4.140   -20.636 1.00 39.58 ? 916  HOH   B O   1 
HETATM 6157 O  O   . HOH   M 5 .   ? -0.006  -11.884 -56.943 1.00 29.69 ? 917  HOH   B O   1 
HETATM 6158 O  O   . HOH   M 5 .   ? -34.597 -5.149  -68.387 1.00 41.91 ? 918  HOH   B O   1 
HETATM 6159 O  O   . HOH   M 5 .   ? -25.700 -23.168 -56.663 1.00 32.19 ? 919  HOH   B O   1 
HETATM 6160 O  O   . HOH   M 5 .   ? -10.592 -32.650 -55.808 1.00 33.85 ? 920  HOH   B O   1 
HETATM 6161 O  O   . HOH   M 5 .   ? -24.117 -21.410 -45.646 1.00 34.23 ? 921  HOH   B O   1 
HETATM 6162 O  O   . HOH   M 5 .   ? -0.510  5.178   -54.256 1.00 33.75 ? 922  HOH   B O   1 
HETATM 6163 O  O   . HOH   M 5 .   ? -23.801 -8.400  -62.259 1.00 26.52 ? 923  HOH   B O   1 
HETATM 6164 O  O   . HOH   M 5 .   ? 0.295   11.078  -50.326 1.00 47.32 ? 924  HOH   B O   1 
HETATM 6165 O  O   . HOH   M 5 .   ? -18.324 -25.923 -50.329 1.00 39.28 ? 925  HOH   B O   1 
HETATM 6166 O  O   . HOH   M 5 .   ? -6.226  10.959  -66.604 1.00 40.49 ? 926  HOH   B O   1 
HETATM 6167 O  O   . HOH   M 5 .   ? -19.662 -3.913  -68.412 1.00 35.69 ? 927  HOH   B O   1 
HETATM 6168 O  O   . HOH   M 5 .   ? -17.097 -8.577  -47.924 1.00 15.36 ? 928  HOH   B O   1 
HETATM 6169 O  O   . HOH   M 5 .   ? -13.497 7.083   -53.564 1.00 15.19 ? 929  HOH   B O   1 
HETATM 6170 O  O   . HOH   M 5 .   ? -13.198 13.199  -31.486 1.00 31.54 ? 930  HOH   B O   1 
HETATM 6171 O  O   . HOH   M 5 .   ? -4.598  11.672  -61.685 1.00 44.86 ? 931  HOH   B O   1 
HETATM 6172 O  O   . HOH   M 5 .   ? -39.703 -8.228  -47.544 1.00 30.58 ? 932  HOH   B O   1 
HETATM 6173 O  O   . HOH   M 5 .   ? -36.233 6.620   -62.911 1.00 26.85 ? 933  HOH   B O   1 
HETATM 6174 O  O   . HOH   M 5 .   ? -14.579 7.891   -70.488 1.00 26.81 ? 934  HOH   B O   1 
HETATM 6175 O  O   . HOH   M 5 .   ? -12.696 -19.423 -42.506 1.00 37.32 ? 935  HOH   B O   1 
HETATM 6176 O  O   . HOH   M 5 .   ? -25.872 -19.479 -41.470 1.00 39.06 ? 936  HOH   B O   1 
HETATM 6177 O  O   . HOH   M 5 .   ? -36.803 -3.917  -53.963 1.00 26.46 ? 937  HOH   B O   1 
HETATM 6178 O  O   . HOH   M 5 .   ? -25.451 19.768  -48.880 1.00 33.52 ? 938  HOH   B O   1 
HETATM 6179 O  O   . HOH   M 5 .   ? -17.252 6.872   -74.859 1.00 26.31 ? 939  HOH   B O   1 
HETATM 6180 O  O   . HOH   M 5 .   ? -32.853 -13.325 -40.869 1.00 24.44 ? 940  HOH   B O   1 
HETATM 6181 O  O   . HOH   M 5 .   ? -32.879 -16.243 -52.437 1.00 40.22 ? 941  HOH   B O   1 
HETATM 6182 O  O   . HOH   M 5 .   ? -34.679 -1.448  -68.101 1.00 22.98 ? 942  HOH   B O   1 
HETATM 6183 O  O   . HOH   M 5 .   ? -6.525  12.493  -37.885 1.00 41.65 ? 943  HOH   B O   1 
HETATM 6184 O  O   . HOH   M 5 .   ? -7.672  17.059  -43.201 1.00 24.88 ? 944  HOH   B O   1 
HETATM 6185 O  O   . HOH   M 5 .   ? -7.262  -11.048 -34.610 1.00 23.33 ? 945  HOH   B O   1 
HETATM 6186 O  O   . HOH   M 5 .   ? 0.597   -18.003 -48.941 1.00 44.01 ? 946  HOH   B O   1 
HETATM 6187 O  O   . HOH   M 5 .   ? -25.587 7.135   -70.496 1.00 38.06 ? 947  HOH   B O   1 
HETATM 6188 O  O   . HOH   M 5 .   ? -9.694  27.403  -49.377 1.00 53.91 ? 948  HOH   B O   1 
HETATM 6189 O  O   . HOH   M 5 .   ? -38.491 1.931   -52.596 1.00 25.66 ? 949  HOH   B O   1 
HETATM 6190 O  O   . HOH   M 5 .   ? -25.502 6.901   -36.591 1.00 21.66 ? 950  HOH   B O   1 
HETATM 6191 O  O   . HOH   M 5 .   ? -24.336 14.045  -38.428 1.00 30.38 ? 951  HOH   B O   1 
HETATM 6192 O  O   . HOH   M 5 .   ? -21.983 1.326   -28.232 1.00 28.20 ? 952  HOH   B O   1 
HETATM 6193 O  O   . HOH   M 5 .   ? -23.336 -0.320  -66.511 1.00 28.96 ? 953  HOH   B O   1 
HETATM 6194 O  O   . HOH   M 5 .   ? -8.428  6.868   -35.222 1.00 31.35 ? 954  HOH   B O   1 
HETATM 6195 O  O   . HOH   M 5 .   ? -17.703 -10.079 -34.008 1.00 19.06 ? 955  HOH   B O   1 
HETATM 6196 O  O   . HOH   M 5 .   ? -7.129  20.659  -53.426 1.00 37.03 ? 956  HOH   B O   1 
HETATM 6197 O  O   . HOH   M 5 .   ? -23.231 15.747  -67.592 1.00 36.98 ? 957  HOH   B O   1 
HETATM 6198 O  O   . HOH   M 5 .   ? -14.055 -22.565 -48.161 1.00 22.30 ? 958  HOH   B O   1 
HETATM 6199 O  O   . HOH   M 5 .   ? -18.035 -14.317 -34.598 1.00 26.05 ? 959  HOH   B O   1 
HETATM 6200 O  O   . HOH   M 5 .   ? -22.157 18.254  -47.046 1.00 43.39 ? 960  HOH   B O   1 
HETATM 6201 O  O   . HOH   M 5 .   ? -3.846  15.987  -41.983 1.00 24.44 ? 961  HOH   B O   1 
HETATM 6202 O  O   . HOH   M 5 .   ? -34.443 13.497  -45.992 1.00 39.10 ? 962  HOH   B O   1 
HETATM 6203 O  O   . HOH   M 5 .   ? -15.251 19.249  -35.395 1.00 25.09 ? 963  HOH   B O   1 
HETATM 6204 O  O   . HOH   M 5 .   ? -40.514 2.861   -42.662 1.00 46.05 ? 964  HOH   B O   1 
HETATM 6205 O  O   . HOH   M 5 .   ? -15.857 24.088  -57.553 1.00 45.27 ? 965  HOH   B O   1 
HETATM 6206 O  O   . HOH   M 5 .   ? -4.137  13.023  -40.243 1.00 25.11 ? 966  HOH   B O   1 
HETATM 6207 O  O   . HOH   M 5 .   ? -2.110  2.411   -58.942 1.00 26.27 ? 967  HOH   B O   1 
HETATM 6208 O  O   . HOH   M 5 .   ? -4.622  -18.890 -53.028 1.00 28.61 ? 968  HOH   B O   1 
HETATM 6209 O  O   . HOH   M 5 .   ? -13.554 -11.365 -63.473 1.00 20.31 ? 969  HOH   B O   1 
HETATM 6210 O  O   . HOH   M 5 .   ? -30.023 2.690   -60.963 1.00 18.45 ? 970  HOH   B O   1 
HETATM 6211 O  O   . HOH   M 5 .   ? -29.697 -3.198  -27.521 1.00 32.40 ? 971  HOH   B O   1 
HETATM 6212 O  O   . HOH   M 5 .   ? -16.690 -2.424  -69.883 1.00 31.86 ? 972  HOH   B O   1 
HETATM 6213 O  O   . HOH   M 5 .   ? -34.884 10.664  -58.580 1.00 40.36 ? 973  HOH   B O   1 
HETATM 6214 O  O   . HOH   M 5 .   ? -5.805  8.566   -33.419 1.00 26.76 ? 974  HOH   B O   1 
HETATM 6215 O  O   . HOH   M 5 .   ? -13.238 21.249  -35.628 1.00 22.33 ? 975  HOH   B O   1 
HETATM 6216 O  O   . HOH   M 5 .   ? -4.132  -16.356 -42.661 1.00 33.22 ? 976  HOH   B O   1 
HETATM 6217 O  O   . HOH   M 5 .   ? -1.745  9.942   -57.687 1.00 41.06 ? 977  HOH   B O   1 
HETATM 6218 O  O   . HOH   M 5 .   ? -20.085 2.037   -70.370 1.00 31.13 ? 978  HOH   B O   1 
HETATM 6219 O  O   . HOH   M 5 .   ? -5.185  -7.265  -25.750 1.00 44.72 ? 979  HOH   B O   1 
HETATM 6220 O  O   . HOH   M 5 .   ? -6.417  17.169  -52.853 1.00 28.70 ? 980  HOH   B O   1 
HETATM 6221 O  O   . HOH   M 5 .   ? -4.663  2.358   -47.538 1.00 11.72 ? 981  HOH   B O   1 
HETATM 6222 O  O   . HOH   M 5 .   ? -9.415  -11.421 -51.961 1.00 15.23 ? 982  HOH   B O   1 
HETATM 6223 O  O   . HOH   M 5 .   ? -14.023 21.314  -50.234 1.00 26.09 ? 983  HOH   B O   1 
HETATM 6224 O  O   . HOH   M 5 .   ? -2.594  -1.830  -33.600 1.00 16.64 ? 984  HOH   B O   1 
HETATM 6225 O  O   . HOH   M 5 .   ? -20.606 -1.002  -53.405 1.00 27.22 ? 985  HOH   B O   1 
HETATM 6226 O  O   . HOH   M 5 .   ? -12.347 2.942   -60.521 1.00 15.62 ? 986  HOH   B O   1 
HETATM 6227 O  O   . HOH   M 5 .   ? -2.712  -11.604 -49.728 1.00 18.31 ? 987  HOH   B O   1 
HETATM 6228 O  O   . HOH   M 5 .   ? -14.438 1.223   -64.530 1.00 17.13 ? 988  HOH   B O   1 
HETATM 6229 O  O   . HOH   M 5 .   ? -6.068  -23.846 -49.921 1.00 27.44 ? 989  HOH   B O   1 
HETATM 6230 O  O   . HOH   M 5 .   ? -32.385 -14.956 -45.058 1.00 24.43 ? 990  HOH   B O   1 
HETATM 6231 O  O   . HOH   M 5 .   ? -37.589 -4.621  -37.266 1.00 23.79 ? 991  HOH   B O   1 
HETATM 6232 O  O   . HOH   M 5 .   ? -18.531 -6.494  -65.432 1.00 32.02 ? 992  HOH   B O   1 
HETATM 6233 O  O   . HOH   M 5 .   ? -31.620 -18.940 -46.030 1.00 29.63 ? 993  HOH   B O   1 
HETATM 6234 O  O   . HOH   M 5 .   ? 2.425   -6.189  -51.694 1.00 31.32 ? 994  HOH   B O   1 
HETATM 6235 O  O   . HOH   M 5 .   ? -30.383 -16.982 -42.442 1.00 26.70 ? 995  HOH   B O   1 
HETATM 6236 O  O   . HOH   M 5 .   ? -0.828  -1.827  -28.762 1.00 15.90 ? 996  HOH   B O   1 
HETATM 6237 O  O   . HOH   M 5 .   ? -38.580 4.517   -60.296 1.00 44.31 ? 997  HOH   B O   1 
HETATM 6238 O  O   . HOH   M 5 .   ? -19.748 -5.467  -51.354 1.00 15.64 ? 998  HOH   B O   1 
HETATM 6239 O  O   . HOH   M 5 .   ? -28.988 -12.251 -39.913 1.00 21.41 ? 999  HOH   B O   1 
HETATM 6240 O  O   . HOH   M 5 .   ? -27.121 0.903   -59.488 1.00 31.55 ? 1000 HOH   B O   1 
HETATM 6241 O  O   . HOH   M 5 .   ? -12.068 -6.621  -47.218 1.00 13.64 ? 1001 HOH   B O   1 
HETATM 6242 O  O   . HOH   M 5 .   ? -6.443  15.442  -48.149 1.00 19.99 ? 1002 HOH   B O   1 
HETATM 6243 O  O   . HOH   M 5 .   ? -37.650 8.741   -51.676 1.00 42.63 ? 1003 HOH   B O   1 
HETATM 6244 O  O   . HOH   M 5 .   ? -37.250 13.630  -49.803 1.00 43.14 ? 1004 HOH   B O   1 
HETATM 6245 O  O   . HOH   M 5 .   ? -36.671 -6.351  -39.337 1.00 30.94 ? 1005 HOH   B O   1 
HETATM 6246 O  O   . HOH   M 5 .   ? -31.545 1.045   -34.965 1.00 24.66 ? 1006 HOH   B O   1 
HETATM 6247 O  O   . HOH   M 5 .   ? -28.254 -9.786  -35.614 1.00 18.88 ? 1007 HOH   B O   1 
HETATM 6248 O  O   . HOH   M 5 .   ? -16.884 -0.118  -63.891 1.00 17.10 ? 1008 HOH   B O   1 
HETATM 6249 O  O   . HOH   M 5 .   ? -30.538 -8.362  -56.434 1.00 24.32 ? 1009 HOH   B O   1 
HETATM 6250 O  O   . HOH   M 5 .   ? -3.274  -5.846  -30.683 1.00 23.50 ? 1010 HOH   B O   1 
HETATM 6251 O  O   . HOH   M 5 .   ? -28.524 12.383  -67.715 1.00 29.27 ? 1011 HOH   B O   1 
HETATM 6252 O  O   . HOH   M 5 .   ? -15.712 -17.135 -34.005 1.00 43.51 ? 1012 HOH   B O   1 
HETATM 6253 O  O   . HOH   M 5 .   ? -32.860 9.504   -44.529 1.00 24.86 ? 1013 HOH   B O   1 
HETATM 6254 O  O   . HOH   M 5 .   ? -16.989 -5.931  -48.526 1.00 15.87 ? 1014 HOH   B O   1 
HETATM 6255 O  O   . HOH   M 5 .   ? -1.633  -4.817  -47.569 1.00 20.18 ? 1015 HOH   B O   1 
HETATM 6256 O  O   . HOH   M 5 .   ? -36.463 8.793   -54.849 1.00 40.66 ? 1016 HOH   B O   1 
HETATM 6257 O  O   . HOH   M 5 .   ? -18.004 -17.794 -61.510 1.00 30.67 ? 1017 HOH   B O   1 
HETATM 6258 O  O   . HOH   M 5 .   ? -4.859  6.428   -52.049 1.00 13.79 ? 1018 HOH   B O   1 
HETATM 6259 O  O   . HOH   M 5 .   ? -37.083 4.833   -67.323 1.00 28.73 ? 1019 HOH   B O   1 
HETATM 6260 O  O   . HOH   M 5 .   ? -3.841  7.731   -44.029 1.00 17.16 ? 1020 HOH   B O   1 
HETATM 6261 O  O   . HOH   M 5 .   ? -20.248 11.493  -34.167 1.00 20.33 ? 1021 HOH   B O   1 
HETATM 6262 O  O   . HOH   M 5 .   ? -35.778 -6.928  -52.683 1.00 31.02 ? 1022 HOH   B O   1 
HETATM 6263 O  O   . HOH   M 5 .   ? -24.075 8.804   -62.772 1.00 20.13 ? 1023 HOH   B O   1 
HETATM 6264 O  O   . HOH   M 5 .   ? -9.460  -4.647  -65.724 1.00 34.15 ? 1024 HOH   B O   1 
HETATM 6265 O  O   . HOH   M 5 .   ? -22.233 -23.932 -48.716 1.00 29.30 ? 1025 HOH   B O   1 
HETATM 6266 O  O   . HOH   M 5 .   ? -12.735 -21.845 -51.344 1.00 20.87 ? 1026 HOH   B O   1 
HETATM 6267 O  O   . HOH   M 5 .   ? -20.376 3.051   -25.771 1.00 35.10 ? 1027 HOH   B O   1 
HETATM 6268 O  O   . HOH   M 5 .   ? -20.640 -26.764 -56.129 1.00 33.38 ? 1028 HOH   B O   1 
HETATM 6269 O  O   . HOH   M 5 .   ? -18.494 17.457  -41.898 1.00 24.71 ? 1029 HOH   B O   1 
HETATM 6270 O  O   . HOH   M 5 .   ? -15.385 0.999   -22.761 1.00 35.64 ? 1030 HOH   B O   1 
HETATM 6271 O  O   . HOH   M 5 .   ? -31.979 17.313  -50.704 1.00 28.54 ? 1031 HOH   B O   1 
HETATM 6272 O  O   . HOH   M 5 .   ? -1.936  -14.032 -57.246 1.00 31.18 ? 1032 HOH   B O   1 
HETATM 6273 O  O   . HOH   M 5 .   ? -26.239 20.688  -54.986 1.00 33.35 ? 1033 HOH   B O   1 
HETATM 6274 O  O   . HOH   M 5 .   ? -26.737 22.298  -57.333 1.00 44.62 ? 1034 HOH   B O   1 
HETATM 6275 O  O   . HOH   M 5 .   ? -6.557  8.197   -44.385 1.00 14.40 ? 1035 HOH   B O   1 
HETATM 6276 O  O   . HOH   M 5 .   ? -29.644 -17.640 -58.093 1.00 39.67 ? 1036 HOH   B O   1 
HETATM 6277 O  O   . HOH   M 5 .   ? -25.141 -18.317 -64.991 1.00 28.70 ? 1037 HOH   B O   1 
HETATM 6278 O  O   . HOH   M 5 .   ? -19.127 18.434  -47.224 1.00 23.72 ? 1038 HOH   B O   1 
HETATM 6279 O  O   . HOH   M 5 .   ? -23.032 4.485   -30.214 1.00 27.41 ? 1039 HOH   B O   1 
HETATM 6280 O  O   . HOH   M 5 .   ? -5.014  -17.031 -39.701 1.00 39.15 ? 1040 HOH   B O   1 
HETATM 6281 O  O   . HOH   M 5 .   ? -0.224  5.703   -43.289 1.00 25.15 ? 1041 HOH   B O   1 
HETATM 6282 O  O   . HOH   M 5 .   ? -5.428  -24.119 -47.381 1.00 31.88 ? 1042 HOH   B O   1 
HETATM 6283 O  O   . HOH   M 5 .   ? -30.815 -7.203  -58.764 1.00 29.19 ? 1043 HOH   B O   1 
HETATM 6284 O  O   . HOH   M 5 .   ? -16.061 -21.822 -40.155 1.00 47.87 ? 1044 HOH   B O   1 
HETATM 6285 O  O   . HOH   M 5 .   ? 1.925   -7.510  -42.043 1.00 19.84 ? 1045 HOH   B O   1 
HETATM 6286 O  O   . HOH   M 5 .   ? -15.268 11.566  -66.528 1.00 22.20 ? 1046 HOH   B O   1 
HETATM 6287 O  O   . HOH   M 5 .   ? -3.238  -1.744  -36.264 1.00 26.67 ? 1047 HOH   B O   1 
HETATM 6288 O  O   . HOH   M 5 .   ? -27.965 5.606   -67.657 1.00 29.08 ? 1048 HOH   B O   1 
HETATM 6289 O  O   . HOH   M 5 .   ? 2.466   3.313   -50.014 1.00 26.38 ? 1049 HOH   B O   1 
HETATM 6290 O  O   . HOH   M 5 .   ? -12.913 3.340   -23.885 1.00 26.00 ? 1050 HOH   B O   1 
HETATM 6291 O  O   . HOH   M 5 .   ? -13.180 -22.701 -36.500 1.00 26.66 ? 1051 HOH   B O   1 
HETATM 6292 O  O   . HOH   M 5 .   ? -32.848 -13.096 -46.996 1.00 23.65 ? 1052 HOH   B O   1 
HETATM 6293 O  O   . HOH   M 5 .   ? -23.430 -16.669 -35.277 1.00 27.78 ? 1053 HOH   B O   1 
HETATM 6294 O  O   . HOH   M 5 .   ? -37.252 4.337   -53.966 1.00 29.57 ? 1054 HOH   B O   1 
HETATM 6295 O  O   . HOH   M 5 .   ? -15.839 0.589   -71.300 1.00 25.11 ? 1055 HOH   B O   1 
HETATM 6296 O  O   . HOH   M 5 .   ? -23.784 7.260   -31.421 1.00 26.59 ? 1056 HOH   B O   1 
HETATM 6297 O  O   . HOH   M 5 .   ? -2.183  5.378   -36.846 1.00 21.01 ? 1057 HOH   B O   1 
HETATM 6298 O  O   . HOH   M 5 .   ? -12.065 10.667  -32.725 1.00 29.12 ? 1058 HOH   B O   1 
HETATM 6299 O  O   . HOH   M 5 .   ? -34.582 -16.093 -50.413 1.00 51.34 ? 1059 HOH   B O   1 
HETATM 6300 O  O   . HOH   M 5 .   ? -28.678 -20.730 -56.303 1.00 43.68 ? 1060 HOH   B O   1 
HETATM 6301 O  O   . HOH   M 5 .   ? -28.437 15.635  -44.019 1.00 37.69 ? 1061 HOH   B O   1 
HETATM 6302 O  O   . HOH   M 5 .   ? -33.638 2.793   -69.497 1.00 22.14 ? 1062 HOH   B O   1 
HETATM 6303 O  O   . HOH   M 5 .   ? -20.166 5.998   -27.248 1.00 37.17 ? 1063 HOH   B O   1 
HETATM 6304 O  O   . HOH   M 5 .   ? -20.192 9.305   -27.394 1.00 36.77 ? 1064 HOH   B O   1 
HETATM 6305 O  O   . HOH   M 5 .   ? -17.089 16.546  -27.737 1.00 43.35 ? 1065 HOH   B O   1 
HETATM 6306 O  O   . HOH   M 5 .   ? -2.301  4.729   -30.063 1.00 21.26 ? 1066 HOH   B O   1 
HETATM 6307 O  O   . HOH   M 5 .   ? -16.416 -11.779 -51.409 1.00 14.79 ? 1067 HOH   B O   1 
HETATM 6308 O  O   . HOH   M 5 .   ? -16.752 -5.177  -27.992 1.00 32.98 ? 1068 HOH   B O   1 
HETATM 6309 O  O   . HOH   M 5 .   ? -37.375 -2.467  -56.537 1.00 46.67 ? 1069 HOH   B O   1 
HETATM 6310 O  O   . HOH   M 5 .   ? -6.145  -8.363  -34.109 1.00 20.91 ? 1070 HOH   B O   1 
HETATM 6311 O  O   . HOH   M 5 .   ? -13.196 20.352  -39.529 1.00 22.76 ? 1071 HOH   B O   1 
HETATM 6312 O  O   . HOH   M 5 .   ? -11.564 15.009  -61.402 1.00 21.00 ? 1072 HOH   B O   1 
HETATM 6313 O  O   . HOH   M 5 .   ? -14.985 -13.131 -65.186 1.00 31.48 ? 1073 HOH   B O   1 
HETATM 6314 O  O   . HOH   M 5 .   ? -18.225 7.354   -71.060 1.00 29.47 ? 1074 HOH   B O   1 
HETATM 6315 O  O   . HOH   M 5 .   ? -35.258 9.575   -61.285 1.00 42.07 ? 1075 HOH   B O   1 
HETATM 6316 O  O   . HOH   M 5 .   ? 2.415   -7.393  -48.426 1.00 25.24 ? 1076 HOH   B O   1 
HETATM 6317 O  O   . HOH   M 5 .   ? -2.455  -14.142 -48.578 1.00 21.68 ? 1077 HOH   B O   1 
HETATM 6318 O  O   . HOH   M 5 .   ? -15.697 13.863  -28.842 1.00 34.98 ? 1078 HOH   B O   1 
HETATM 6319 O  O   . HOH   M 5 .   ? -4.509  -3.343  -27.850 1.00 28.39 ? 1079 HOH   B O   1 
HETATM 6320 O  O   . HOH   M 5 .   ? -9.026  -12.962 -54.439 1.00 15.58 ? 1080 HOH   B O   1 
HETATM 6321 O  O   . HOH   M 5 .   ? -6.103  -18.645 -57.311 1.00 22.57 ? 1081 HOH   B O   1 
HETATM 6322 O  O   . HOH   M 5 .   ? -11.694 -27.155 -47.468 1.00 42.31 ? 1082 HOH   B O   1 
HETATM 6323 O  O   . HOH   M 5 .   ? -28.345 -9.692  -59.243 1.00 34.28 ? 1083 HOH   B O   1 
HETATM 6324 O  O   . HOH   M 5 .   ? -26.610 3.129   -66.239 1.00 22.51 ? 1084 HOH   B O   1 
HETATM 6325 O  O   . HOH   M 5 .   ? -31.159 -4.049  -61.267 1.00 21.03 ? 1085 HOH   B O   1 
HETATM 6326 O  O   . HOH   M 5 .   ? -30.950 -6.095  -63.540 1.00 42.08 ? 1086 HOH   B O   1 
HETATM 6327 O  O   . HOH   M 5 .   ? -18.787 4.829   -25.131 1.00 33.10 ? 1087 HOH   B O   1 
HETATM 6328 O  O   . HOH   M 5 .   ? -26.439 -22.581 -47.133 1.00 35.69 ? 1088 HOH   B O   1 
HETATM 6329 O  O   . HOH   M 5 .   ? -7.117  -13.741 -61.588 1.00 19.56 ? 1089 HOH   B O   1 
HETATM 6330 O  O   . HOH   M 5 .   ? -8.011  11.510  -60.406 1.00 20.13 ? 1090 HOH   B O   1 
HETATM 6331 O  O   . HOH   M 5 .   ? -2.864  9.415   -39.428 1.00 40.05 ? 1091 HOH   B O   1 
HETATM 6332 O  O   . HOH   M 5 .   ? -1.996  0.324   -37.350 1.00 25.70 ? 1092 HOH   B O   1 
HETATM 6333 O  O   . HOH   M 5 .   ? -6.112  8.240   -68.727 1.00 42.96 ? 1093 HOH   B O   1 
HETATM 6334 O  O   . HOH   M 5 .   ? -28.785 -20.660 -54.065 1.00 33.51 ? 1094 HOH   B O   1 
HETATM 6335 O  O   . HOH   M 5 .   ? -11.963 -11.806 -31.705 1.00 34.01 ? 1095 HOH   B O   1 
HETATM 6336 O  O   . HOH   M 5 .   ? -0.540  -13.416 -44.101 1.00 25.30 ? 1096 HOH   B O   1 
HETATM 6337 O  O   . HOH   M 5 .   ? -20.190 17.074  -40.187 1.00 35.12 ? 1097 HOH   B O   1 
HETATM 6338 O  O   . HOH   M 5 .   ? -27.039 -22.680 -54.560 1.00 41.95 ? 1098 HOH   B O   1 
HETATM 6339 O  O   . HOH   M 5 .   ? -21.753 -9.783  -27.713 1.00 45.28 ? 1099 HOH   B O   1 
HETATM 6340 O  O   . HOH   M 5 .   ? -20.000 4.530   -72.547 1.00 30.59 ? 1100 HOH   B O   1 
HETATM 6341 O  O   . HOH   M 5 .   ? -18.639 -12.075 -49.607 1.00 15.27 ? 1101 HOH   B O   1 
HETATM 6342 O  O   . HOH   M 5 .   ? -19.925 -1.847  -70.985 1.00 42.04 ? 1102 HOH   B O   1 
HETATM 6343 O  O   . HOH   M 5 .   ? -0.981  8.675   -50.815 1.00 28.63 ? 1103 HOH   B O   1 
HETATM 6344 O  O   . HOH   M 5 .   ? -34.881 -9.061  -50.950 1.00 28.72 ? 1104 HOH   B O   1 
HETATM 6345 O  O   . HOH   M 5 .   ? -11.749 -30.862 -57.676 1.00 19.17 ? 1105 HOH   B O   1 
HETATM 6346 O  O   . HOH   M 5 .   ? -5.206  0.813   -23.938 1.00 29.42 ? 1106 HOH   B O   1 
HETATM 6347 O  O   . HOH   M 5 .   ? -18.644 -29.012 -47.897 1.00 44.37 ? 1107 HOH   B O   1 
HETATM 6348 O  O   . HOH   M 5 .   ? -32.176 11.147  -40.417 1.00 28.82 ? 1108 HOH   B O   1 
HETATM 6349 O  O   . HOH   M 5 .   ? -25.549 -2.704  -68.168 1.00 43.42 ? 1109 HOH   B O   1 
HETATM 6350 O  O   . HOH   M 5 .   ? -6.253  -11.166 -63.692 1.00 25.62 ? 1110 HOH   B O   1 
HETATM 6351 O  O   . HOH   M 5 .   ? -20.443 -18.448 -63.094 1.00 35.67 ? 1111 HOH   B O   1 
HETATM 6352 O  O   . HOH   M 5 .   ? -3.760  7.823   -31.681 1.00 45.27 ? 1112 HOH   B O   1 
HETATM 6353 O  O   . HOH   M 5 .   ? -12.999 15.545  -64.918 1.00 27.06 ? 1113 HOH   B O   1 
HETATM 6354 O  O   . HOH   M 5 .   ? -34.955 -10.449 -37.933 1.00 26.44 ? 1114 HOH   B O   1 
HETATM 6355 O  O   . HOH   M 5 .   ? -5.747  4.665   -26.162 1.00 45.00 ? 1115 HOH   B O   1 
HETATM 6356 O  O   . HOH   M 5 .   ? -22.984 -11.034 -64.029 1.00 23.46 ? 1116 HOH   B O   1 
HETATM 6357 O  O   . HOH   M 5 .   ? -15.195 14.718  -65.857 1.00 31.77 ? 1117 HOH   B O   1 
HETATM 6358 O  O   . HOH   M 5 .   ? -3.407  1.387   -25.993 1.00 22.21 ? 1118 HOH   B O   1 
HETATM 6359 O  O   . HOH   M 5 .   ? -0.040  8.317   -44.258 1.00 31.40 ? 1119 HOH   B O   1 
HETATM 6360 O  O   . HOH   M 5 .   ? -42.552 -6.533  -48.920 1.00 32.77 ? 1120 HOH   B O   1 
HETATM 6361 O  O   . HOH   M 5 .   ? -22.864 1.036   -68.755 1.00 35.93 ? 1121 HOH   B O   1 
HETATM 6362 O  O   . HOH   M 5 .   ? -17.832 -16.549 -64.220 1.00 38.69 ? 1122 HOH   B O   1 
HETATM 6363 O  O   . HOH   M 5 .   ? -29.224 -18.581 -61.416 1.00 37.35 ? 1123 HOH   B O   1 
HETATM 6364 O  O   . HOH   M 5 .   ? -25.679 -15.591 -35.985 1.00 21.85 ? 1124 HOH   B O   1 
HETATM 6365 O  O   . HOH   M 5 .   ? -19.953 -1.637  -25.046 1.00 33.78 ? 1125 HOH   B O   1 
HETATM 6366 O  O   . HOH   M 5 .   ? -20.295 17.678  -31.207 1.00 46.93 ? 1126 HOH   B O   1 
HETATM 6367 O  O   . HOH   M 5 .   ? -42.536 -3.166  -50.355 1.00 35.41 ? 1127 HOH   B O   1 
HETATM 6368 O  O   . HOH   M 5 .   ? -12.147 5.522   -27.544 1.00 25.33 ? 1128 HOH   B O   1 
HETATM 6369 O  O   . HOH   M 5 .   ? -13.160 -7.340  -65.657 1.00 42.33 ? 1129 HOH   B O   1 
HETATM 6370 O  O   . HOH   M 5 .   ? -14.823 10.093  -26.505 1.00 41.95 ? 1130 HOH   B O   1 
HETATM 6371 O  O   . HOH   M 5 .   ? -2.798  -7.630  -36.661 1.00 22.51 ? 1131 HOH   B O   1 
HETATM 6372 O  O   . HOH   M 5 .   ? -35.768 -12.873 -44.686 1.00 29.80 ? 1132 HOH   B O   1 
HETATM 6373 O  O   . HOH   M 5 .   ? -40.159 -10.760 -43.885 1.00 48.75 ? 1133 HOH   B O   1 
HETATM 6374 O  O   . HOH   M 5 .   ? -30.080 19.437  -49.680 1.00 31.96 ? 1134 HOH   B O   1 
HETATM 6375 O  O   . HOH   M 5 .   ? -11.061 24.997  -44.497 1.00 45.69 ? 1135 HOH   B O   1 
HETATM 6376 O  O   . HOH   M 5 .   ? -16.175 11.630  -70.406 1.00 35.92 ? 1136 HOH   B O   1 
HETATM 6377 O  O   . HOH   M 5 .   ? -2.543  16.287  -58.159 1.00 32.76 ? 1137 HOH   B O   1 
HETATM 6378 O  O   . HOH   M 5 .   ? -37.308 10.905  -53.598 1.00 40.52 ? 1138 HOH   B O   1 
HETATM 6379 O  O   . HOH   M 5 .   ? -13.940 -4.787  -66.227 1.00 41.46 ? 1139 HOH   B O   1 
HETATM 6380 O  O   . HOH   M 5 .   ? -11.125 -1.679  -26.335 1.00 18.04 ? 1140 HOH   B O   1 
HETATM 6381 O  O   . HOH   M 5 .   ? -3.568  -32.294 -64.864 1.00 37.34 ? 1141 HOH   B O   1 
HETATM 6382 O  O   . HOH   M 5 .   ? 0.650   -6.393  -39.751 1.00 19.77 ? 1142 HOH   B O   1 
HETATM 6383 O  O   . HOH   M 5 .   ? -17.619 22.592  -65.647 1.00 37.79 ? 1143 HOH   B O   1 
HETATM 6384 O  O   . HOH   M 5 .   ? -26.680 -19.902 -63.173 1.00 27.10 ? 1144 HOH   B O   1 
HETATM 6385 O  O   . HOH   M 5 .   ? -1.865  7.015   -52.128 1.00 40.94 ? 1145 HOH   B O   1 
HETATM 6386 O  O   . HOH   M 5 .   ? -12.450 -13.806 -33.755 1.00 23.17 ? 1146 HOH   B O   1 
HETATM 6387 O  O   . HOH   M 5 .   ? -29.651 -5.360  -65.828 1.00 41.82 ? 1147 HOH   B O   1 
HETATM 6388 O  O   . HOH   M 5 .   ? -16.098 17.608  -69.275 1.00 43.61 ? 1148 HOH   B O   1 
HETATM 6389 O  O   . HOH   M 5 .   ? -3.869  -10.104 -58.197 1.00 27.09 ? 1149 HOH   B O   1 
HETATM 6390 O  O   . HOH   M 5 .   ? -0.722  7.337   -61.226 1.00 40.78 ? 1150 HOH   B O   1 
HETATM 6391 O  O   . HOH   M 5 .   ? -22.501 -19.732 -39.094 1.00 28.12 ? 1151 HOH   B O   1 
HETATM 6392 O  O   . HOH   M 5 .   ? -17.807 20.153  -66.496 1.00 48.08 ? 1152 HOH   B O   1 
HETATM 6393 O  O   . HOH   M 5 .   ? -0.498  -14.221 -46.727 1.00 25.03 ? 1153 HOH   B O   1 
HETATM 6394 O  O   . HOH   M 5 .   ? -3.514  8.219   -63.906 1.00 40.65 ? 1154 HOH   B O   1 
HETATM 6395 O  O   . HOH   M 5 .   ? -15.458 -7.291  -28.097 1.00 26.31 ? 1155 HOH   B O   1 
HETATM 6396 O  O   . HOH   M 5 .   ? -13.032 16.665  -32.037 1.00 31.29 ? 1156 HOH   B O   1 
HETATM 6397 O  O   . HOH   M 5 .   ? -2.560  7.468   -41.678 1.00 31.29 ? 1157 HOH   B O   1 
HETATM 6398 O  O   . HOH   M 5 .   ? -30.761 14.705  -43.155 1.00 43.10 ? 1158 HOH   B O   1 
HETATM 6399 O  O   . HOH   M 5 .   ? -27.378 -25.318 -57.593 1.00 38.36 ? 1159 HOH   B O   1 
HETATM 6400 O  O   . HOH   M 5 .   ? -13.187 -17.068 -34.391 1.00 36.04 ? 1160 HOH   B O   1 
HETATM 6401 O  O   . HOH   M 5 .   ? 1.108   -22.815 -59.180 1.00 47.29 ? 1161 HOH   B O   1 
HETATM 6402 O  O   . HOH   M 5 .   ? -29.855 5.760   -25.615 1.00 46.78 ? 1162 HOH   B O   1 
HETATM 6403 O  O   . HOH   M 5 .   ? -32.437 -9.027  -33.543 1.00 43.26 ? 1163 HOH   B O   1 
HETATM 6404 O  O   . HOH   M 5 .   ? -29.868 -22.177 -48.388 1.00 28.05 ? 1164 HOH   B O   1 
HETATM 6405 O  O   . HOH   M 5 .   ? -29.799 -13.503 -58.430 1.00 39.30 ? 1165 HOH   B O   1 
HETATM 6406 O  O   . HOH   M 5 .   ? -38.660 -4.904  -57.510 1.00 42.11 ? 1166 HOH   B O   1 
HETATM 6407 O  O   . HOH   M 5 .   ? -17.765 -2.387  -65.220 1.00 22.96 ? 1167 HOH   B O   1 
HETATM 6408 O  O   . HOH   M 5 .   ? -40.079 3.626   -51.201 1.00 35.73 ? 1168 HOH   B O   1 
HETATM 6409 O  O   . HOH   M 5 .   ? -15.546 -22.751 -38.098 1.00 34.51 ? 1169 HOH   B O   1 
HETATM 6410 O  O   . HOH   M 5 .   ? -5.932  22.412  -59.729 1.00 38.36 ? 1170 HOH   B O   1 
HETATM 6411 O  O   . HOH   M 5 .   ? -26.344 10.920  -68.733 1.00 39.37 ? 1171 HOH   B O   1 
HETATM 6412 O  O   . HOH   M 5 .   ? -11.725 -22.053 -43.777 1.00 43.90 ? 1172 HOH   B O   1 
HETATM 6413 O  O   . HOH   M 5 .   ? -15.981 13.038  -64.572 1.00 40.79 ? 1173 HOH   B O   1 
HETATM 6414 O  O   . HOH   M 5 .   ? -11.337 -18.569 -34.741 1.00 29.47 ? 1174 HOH   B O   1 
HETATM 6415 O  O   . HOH   M 5 .   ? -12.099 23.657  -50.690 1.00 45.15 ? 1175 HOH   B O   1 
HETATM 6416 O  O   . HOH   M 5 .   ? -3.845  17.070  -44.603 1.00 30.92 ? 1176 HOH   B O   1 
HETATM 6417 O  O   . HOH   M 5 .   ? -41.594 -1.841  -59.434 1.00 41.39 ? 1177 HOH   B O   1 
HETATM 6418 O  O   . HOH   M 5 .   ? -38.724 -9.911  -39.981 1.00 33.20 ? 1178 HOH   B O   1 
HETATM 6419 O  O   . HOH   M 5 .   ? -13.045 -23.545 -44.884 1.00 40.00 ? 1179 HOH   B O   1 
HETATM 6420 O  O   . HOH   M 5 .   ? -23.291 -26.899 -55.673 1.00 33.74 ? 1180 HOH   B O   1 
HETATM 6421 O  O   . HOH   M 5 .   ? -40.647 -8.707  -42.003 1.00 45.71 ? 1181 HOH   B O   1 
HETATM 6422 O  O   . HOH   M 5 .   ? -6.312  17.330  -46.059 1.00 26.51 ? 1182 HOH   B O   1 
HETATM 6423 O  O   . HOH   M 5 .   ? -18.916 -23.434 -45.622 1.00 45.14 ? 1183 HOH   B O   1 
HETATM 6424 O  O   . HOH   M 5 .   ? -38.079 -12.747 -43.262 1.00 33.65 ? 1184 HOH   B O   1 
HETATM 6425 O  O   . HOH   M 5 .   ? -33.089 -17.076 -46.650 1.00 33.18 ? 1185 HOH   B O   1 
HETATM 6426 O  O   . HOH   M 5 .   ? -5.036  24.985  -40.043 1.00 46.89 ? 1186 HOH   B O   1 
HETATM 6427 O  O   . HOH   M 5 .   ? -36.144 -4.944  -56.651 1.00 40.18 ? 1187 HOH   B O   1 
HETATM 6428 O  O   . HOH   M 5 .   ? -22.336 -7.129  -65.842 1.00 50.81 ? 1188 HOH   B O   1 
HETATM 6429 O  O   . HOH   M 5 .   ? -12.518 2.377   -70.533 1.00 37.76 ? 1189 HOH   B O   1 
HETATM 6430 O  O   . HOH   M 5 .   ? -20.693 -11.754 -30.195 1.00 45.36 ? 1190 HOH   B O   1 
HETATM 6431 O  O   . HOH   M 5 .   ? -17.242 -12.637 -33.038 1.00 31.88 ? 1191 HOH   B O   1 
HETATM 6432 O  O   . HOH   M 5 .   ? -33.634 -14.966 -54.395 1.00 44.30 ? 1192 HOH   B O   1 
HETATM 6433 O  O   . HOH   M 5 .   ? -6.592  19.722  -47.376 1.00 44.92 ? 1193 HOH   B O   1 
HETATM 6434 O  O   . HOH   M 5 .   ? -15.777 -19.797 -34.316 1.00 38.98 ? 1194 HOH   B O   1 
HETATM 6435 O  O   . HOH   M 5 .   ? -29.786 -22.800 -63.346 1.00 41.90 ? 1195 HOH   B O   1 
HETATM 6436 O  O   . HOH   M 5 .   ? -13.143 3.308   -63.087 1.00 24.71 ? 1196 HOH   B O   1 
HETATM 6437 O  O   . HOH   M 5 .   ? -22.169 17.440  -69.084 1.00 45.37 ? 1197 HOH   B O   1 
HETATM 6438 O  O   . HOH   M 5 .   ? -41.326 -9.174  -46.017 1.00 45.39 ? 1198 HOH   B O   1 
HETATM 6439 O  O   . HOH   M 5 .   ? -28.663 -18.692 -41.082 1.00 30.07 ? 1199 HOH   B O   1 
HETATM 6440 O  O   . HOH   M 5 .   ? -19.339 24.679  -49.778 1.00 46.24 ? 1200 HOH   B O   1 
HETATM 6441 O  O   . HOH   M 5 .   ? -37.034 -8.760  -38.541 1.00 30.74 ? 1201 HOH   B O   1 
HETATM 6442 O  O   . HOH   M 5 .   ? -8.562  -11.683 -32.293 1.00 37.16 ? 1202 HOH   B O   1 
HETATM 6443 O  O   . HOH   M 5 .   ? 1.302   -0.495  -47.900 1.00 19.48 ? 1203 HOH   B O   1 
HETATM 6444 O  O   . HOH   M 5 .   ? -10.994 -35.524 -55.820 1.00 32.53 ? 1204 HOH   B O   1 
HETATM 6445 O  O   . HOH   M 5 .   ? -4.636  -3.181  -25.625 1.00 35.62 ? 1205 HOH   B O   1 
HETATM 6446 O  O   . HOH   M 5 .   ? -18.497 22.383  -50.828 1.00 41.21 ? 1206 HOH   B O   1 
HETATM 6447 O  O   . HOH   M 5 .   ? -32.006 19.958  -47.168 1.00 44.62 ? 1207 HOH   B O   1 
HETATM 6448 O  O   . HOH   M 5 .   ? -25.447 1.748   -69.165 1.00 33.07 ? 1208 HOH   B O   1 
HETATM 6449 O  O   . HOH   M 5 .   ? -30.465 11.282  -69.356 1.00 34.13 ? 1209 HOH   B O   1 
HETATM 6450 O  O   . HOH   M 5 .   ? -3.981  -0.245  -22.015 1.00 27.36 ? 1210 HOH   B O   1 
HETATM 6451 O  O   . HOH   M 5 .   ? -4.241  -19.699 -43.612 1.00 41.69 ? 1211 HOH   B O   1 
HETATM 6452 O  O   . HOH   M 5 .   ? 1.815   9.128   -48.615 1.00 42.08 ? 1212 HOH   B O   1 
HETATM 6453 O  O   . HOH   M 5 .   ? -20.382 -25.970 -48.804 1.00 44.93 ? 1213 HOH   B O   1 
HETATM 6454 O  O   . HOH   M 5 .   ? -35.282 -12.854 -39.283 1.00 31.16 ? 1214 HOH   B O   1 
HETATM 6455 O  O   . HOH   M 5 .   ? 1.581   8.482   -46.323 1.00 35.63 ? 1215 HOH   B O   1 
HETATM 6456 O  O   . HOH   M 5 .   ? -20.542 18.157  -35.368 1.00 43.45 ? 1216 HOH   B O   1 
HETATM 6457 O  O   . HOH   M 5 .   ? -28.473 14.945  -69.071 1.00 50.29 ? 1217 HOH   B O   1 
HETATM 6458 O  O   . HOH   M 5 .   ? 6.109   -15.352 -52.602 1.00 43.29 ? 1218 HOH   B O   1 
HETATM 6459 O  O   . HOH   M 5 .   ? -20.830 -11.553 -64.652 1.00 46.50 ? 1219 HOH   B O   1 
HETATM 6460 O  O   . HOH   M 5 .   ? -5.402  17.025  -50.115 1.00 33.48 ? 1220 HOH   B O   1 
HETATM 6461 O  O   . HOH   M 5 .   ? -37.949 -6.186  -54.995 1.00 43.38 ? 1221 HOH   B O   1 
HETATM 6462 O  O   . HOH   M 5 .   ? -17.678 -31.615 -52.554 1.00 47.15 ? 1222 HOH   B O   1 
HETATM 6463 O  O   . HOH   M 5 .   ? -31.102 -21.422 -52.894 1.00 40.62 ? 1223 HOH   B O   1 
HETATM 6464 O  O   . HOH   M 5 .   ? -27.067 -15.954 -64.996 1.00 51.61 ? 1224 HOH   B O   1 
HETATM 6465 O  O   . HOH   M 5 .   ? -22.802 12.199  -33.652 1.00 29.75 ? 1225 HOH   B O   1 
HETATM 6466 O  O   . HOH   M 5 .   ? -30.794 -11.280 -59.026 1.00 36.99 ? 1226 HOH   B O   1 
HETATM 6467 O  O   . HOH   M 5 .   ? -26.890 -13.970 -34.201 1.00 29.09 ? 1227 HOH   B O   1 
HETATM 6468 O  O   . HOH   M 5 .   ? -29.841 -8.647  -33.671 1.00 32.97 ? 1228 HOH   B O   1 
HETATM 6469 O  O   . HOH   M 5 .   ? -19.487 17.872  -27.408 1.00 30.06 ? 1229 HOH   B O   1 
HETATM 6470 O  O   . HOH   M 5 .   ? -39.610 0.457   -54.531 1.00 41.21 ? 1230 HOH   B O   1 
HETATM 6471 O  O   . HOH   M 5 .   ? -26.048 -7.786  -63.889 1.00 43.94 ? 1231 HOH   B O   1 
HETATM 6472 O  O   . HOH   M 5 .   ? -11.477 -4.478  -25.668 1.00 32.20 ? 1232 HOH   B O   1 
HETATM 6473 O  O   . HOH   M 5 .   ? -38.654 9.656   -64.205 1.00 33.46 ? 1233 HOH   B O   1 
HETATM 6474 O  O   . HOH   M 5 .   ? -12.798 22.591  -37.924 1.00 23.85 ? 1234 HOH   B O   1 
HETATM 6475 O  O   . HOH   M 5 .   ? -4.369  -12.995 -61.082 1.00 47.59 ? 1235 HOH   B O   1 
HETATM 6476 O  O   . HOH   M 5 .   ? -26.413 -11.116 -34.251 1.00 27.30 ? 1236 HOH   B O   1 
HETATM 6477 O  O   . HOH   M 5 .   ? -27.185 -7.305  -31.758 1.00 42.14 ? 1237 HOH   B O   1 
HETATM 6478 O  O   . HOH   M 5 .   ? -16.653 19.664  -37.667 1.00 26.46 ? 1238 HOH   B O   1 
HETATM 6479 O  O   . HOH   M 5 .   ? -7.679  -10.813 -66.389 1.00 43.07 ? 1239 HOH   B O   1 
HETATM 6480 O  O   . HOH   M 5 .   ? -28.436 -8.360  -61.646 1.00 33.51 ? 1240 HOH   B O   1 
HETATM 6481 O  O   . HOH   M 5 .   ? -31.137 -21.968 -46.049 1.00 44.47 ? 1241 HOH   B O   1 
HETATM 6482 O  O   . HOH   M 5 .   ? 0.931   -4.964  -47.962 1.00 21.32 ? 1242 HOH   B O   1 
HETATM 6483 O  O   . HOH   M 5 .   ? -31.634 -15.679 -40.379 1.00 39.06 ? 1243 HOH   B O   1 
HETATM 6484 O  O   . HOH   M 5 .   ? -3.535  -8.864  -34.172 1.00 27.67 ? 1244 HOH   B O   1 
HETATM 6485 O  O   . HOH   M 5 .   ? -28.557 -18.003 -38.559 1.00 43.94 ? 1245 HOH   B O   1 
HETATM 6486 O  O   . HOH   M 5 .   ? -22.560 12.883  -71.658 1.00 39.24 ? 1246 HOH   B O   1 
HETATM 6487 O  O   . HOH   M 5 .   ? -16.354 21.771  -48.579 1.00 43.31 ? 1247 HOH   B O   1 
HETATM 6488 O  O   . HOH   M 5 .   ? -4.525  21.846  -57.467 1.00 48.88 ? 1248 HOH   B O   1 
HETATM 6489 O  O   . HOH   M 5 .   ? 3.435   -8.796  -40.214 1.00 26.84 ? 1249 HOH   B O   1 
HETATM 6490 O  O   . HOH   M 5 .   ? -18.862 19.700  -42.706 1.00 37.55 ? 1250 HOH   B O   1 
HETATM 6491 O  O   . HOH   M 5 .   ? -0.825  -9.629  -58.225 1.00 28.79 ? 1251 HOH   B O   1 
HETATM 6492 O  O   . HOH   M 5 .   ? -14.789 -25.082 -42.477 1.00 42.44 ? 1252 HOH   B O   1 
HETATM 6493 O  O   . HOH   M 5 .   ? -14.913 21.103  -41.424 1.00 41.91 ? 1253 HOH   B O   1 
HETATM 6494 O  O   . HOH   M 5 .   ? -23.147 18.483  -36.167 1.00 45.52 ? 1254 HOH   B O   1 
HETATM 6495 O  O   . HOH   M 5 .   ? -37.160 -0.547  -34.194 1.00 33.47 ? 1255 HOH   B O   1 
HETATM 6496 O  O   . HOH   M 5 .   ? -35.970 -11.803 -50.522 1.00 35.92 ? 1256 HOH   B O   1 
HETATM 6497 O  O   . HOH   M 5 .   ? -19.143 18.894  -37.781 1.00 37.76 ? 1257 HOH   B O   1 
HETATM 6498 O  O   . HOH   M 5 .   ? -30.325 -23.801 -50.116 1.00 41.78 ? 1258 HOH   B O   1 
HETATM 6499 O  O   . HOH   M 5 .   ? -36.690 -14.228 -46.649 1.00 39.55 ? 1259 HOH   B O   1 
HETATM 6500 O  O   . HOH   M 5 .   ? -24.990 -12.006 -65.319 1.00 42.80 ? 1260 HOH   B O   1 
HETATM 6501 O  O   . HOH   M 5 .   ? -45.136 -2.062  -49.194 1.00 37.60 ? 1261 HOH   B O   1 
HETATM 6502 O  O   . HOH   M 5 .   ? -2.181  -4.312  -28.635 1.00 25.62 ? 1262 HOH   B O   1 
HETATM 6503 O  O   . HOH   M 5 .   ? -12.086 6.416   -24.959 1.00 40.79 ? 1263 HOH   B O   1 
HETATM 6504 O  O   . HOH   M 5 .   ? -5.036  -12.551 -35.275 1.00 43.93 ? 1264 HOH   B O   1 
HETATM 6505 O  O   . HOH   M 5 .   ? -1.188  17.120  -56.084 1.00 43.17 ? 1265 HOH   B O   1 
HETATM 6506 O  O   . HOH   M 5 .   ? -10.203 7.579   -30.974 1.00 52.71 ? 1266 HOH   B O   1 
HETATM 6507 O  O   . HOH   M 5 .   ? -34.830 -14.438 -48.692 1.00 38.96 ? 1267 HOH   B O   1 
HETATM 6508 O  O   . HOH   M 5 .   ? -25.690 -6.155  -65.841 1.00 38.82 ? 1268 HOH   B O   1 
HETATM 6509 O  O   . HOH   M 5 .   ? -21.591 19.824  -43.854 1.00 42.14 ? 1269 HOH   B O   1 
HETATM 6510 O  O   . HOH   M 5 .   ? -2.336  -10.795 -35.095 1.00 48.51 ? 1270 HOH   B O   1 
HETATM 6511 O  O   . HOH   M 5 .   ? -1.818  -14.962 -42.030 1.00 36.61 ? 1271 HOH   B O   1 
HETATM 6512 O  O   . HOH   M 5 .   ? -21.911 -23.057 -46.258 1.00 40.86 ? 1272 HOH   B O   1 
HETATM 6513 O  O   . HOH   M 5 .   ? -32.007 -18.851 -43.470 1.00 41.88 ? 1273 HOH   B O   1 
HETATM 6514 O  O   . HOH   M 5 .   ? -44.013 -5.977  -50.817 1.00 38.35 ? 1274 HOH   B O   1 
HETATM 6515 O  O   . HOH   M 5 .   ? -0.075  -16.841 -46.628 1.00 41.86 ? 1275 HOH   B O   1 
HETATM 6516 O  O   . HOH   M 5 .   ? -1.795  7.130   -39.220 1.00 41.34 ? 1276 HOH   B O   1 
HETATM 6517 O  O   . HOH   M 5 .   ? -24.644 7.642   -74.623 1.00 32.68 ? 1277 HOH   B O   1 
HETATM 6518 O  O   . HOH   M 5 .   ? -1.019  -18.490 -44.556 1.00 44.37 ? 1278 HOH   B O   1 
HETATM 6519 O  O   . HOH   M 5 .   ? -18.498 -12.587 -30.637 1.00 33.51 ? 1279 HOH   B O   1 
HETATM 6520 O  O   . HOH   M 5 .   ? -22.960 -13.419 -29.752 1.00 45.75 ? 1280 HOH   B O   1 
HETATM 6521 O  O   . HOH   M 5 .   ? -24.393 12.900  -69.065 1.00 37.80 ? 1281 HOH   B O   1 
HETATM 6522 O  O   . HOH   M 5 .   ? -26.574 3.819   -69.343 1.00 43.20 ? 1282 HOH   B O   1 
HETATM 6523 O  O   . HOH   M 5 .   ? -12.053 -26.023 -42.406 1.00 44.45 ? 1283 HOH   B O   1 
HETATM 6524 O  O   . HOH   M 5 .   ? -34.150 -14.226 -43.109 1.00 29.00 ? 1284 HOH   B O   1 
HETATM 6525 O  O   . HOH   M 5 .   ? -25.642 -19.470 -38.597 1.00 45.56 ? 1285 HOH   B O   1 
HETATM 6526 O  O   . HOH   M 5 .   ? -17.720 21.299  -46.409 1.00 46.88 ? 1286 HOH   B O   1 
HETATM 6527 O  O   . HOH   M 5 .   ? -2.984  18.445  -59.798 1.00 47.03 ? 1287 HOH   B O   1 
HETATM 6528 O  O   . HOH   M 5 .   ? -28.397 -23.605 -45.878 1.00 45.42 ? 1288 HOH   B O   1 
HETATM 6529 O  O   . HOH   M 5 .   ? -26.385 -10.669 -31.703 1.00 42.29 ? 1289 HOH   B O   1 
HETATM 6530 O  O   . HOH   M 5 .   ? -26.844 -17.991 -36.894 1.00 42.21 ? 1290 HOH   B O   1 
HETATM 6531 O  O   . HOH   M 5 .   ? -8.850  -4.056  -23.352 1.00 49.47 ? 1291 HOH   B O   1 
HETATM 6532 O  O   . HOH   M 5 .   ? -37.547 -13.088 -40.732 1.00 38.60 ? 1292 HOH   B O   1 
HETATM 6533 O  O   . HOH   M 5 .   ? -35.985 -13.204 -52.914 1.00 43.78 ? 1293 HOH   B O   1 
HETATM 6534 O  O   . HOH   M 5 .   ? -34.838 -17.223 -43.058 1.00 42.06 ? 1294 HOH   B O   1 
HETATM 6535 O  O   . HOH   M 5 .   ? -21.872 -15.936 -30.582 1.00 42.94 ? 1295 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
5717 K K . K E . ? 0.1783 0.1681 0.1783 0.0033  -0.0096 0.0019  803 K A K 
5718 K K . K F . ? 0.2252 0.2162 0.2605 -0.0633 -0.0633 0.0655  804 K A K 
5745 K K . K I . ? 0.2274 0.2444 0.2413 0.0409  -0.0633 -0.0566 803 K B K 
5746 K K . K J . ? 0.1468 0.1576 0.1619 0.0080  -0.0142 0.0052  804 K B K 
5747 K K . K K . ? 0.2405 0.3073 0.3333 -0.0197 -0.0271 0.0223  805 K B K 
# 
