data_9EGF
# 
_entry.id   9EGF 
# 
_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   9EGF         pdb_00009egf 10.2210/pdb9egf/pdb 
WWPDB D_1000290368 ?            ?                   
# 
_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                        9EGF 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-21 
_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 '4-({(ethanesulfonyl)[(pyridin-3-yl)methyl]amino}methyl)-N-hydroxybenzamide' 349.405   2   ? ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                   65.409    2   ? ? ? ? 
4 non-polymer syn 'POTASSIUM ION'                                                              39.098    2   ? ? ? ? 
5 water       nat water                                                                        18.015    804 ? ? ? ? 
# 
_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 '4-({(ethanesulfonyl)[(pyridin-3-yl)methyl]amino}methyl)-N-hydroxybenzamide' A1BH8 
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 
A1BH8 non-polymer         . '4-({(ethanesulfonyl)[(pyridin-3-yl)methyl]amino}methyl)-N-hydroxybenzamide' ? 'C16 H19 N3 O4 S' 
349.405 
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 329 770 770 ASP ASP A . n 
A 1 330 HIS 330 771 771 HIS HIS A . n 
A 1 331 LEU 331 772 772 LEU LEU 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        A1BH8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BH8 
_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 A1BH8 1   801  1   A1BH8 TO5 A . 
D 3 ZN    1   802  3   ZN    ZN  A . 
E 4 K     1   803  1   K     K   A . 
F 2 A1BH8 1   801  2   A1BH8 TO5 B . 
G 3 ZN    1   802  4   ZN    ZN  B . 
H 4 K     1   803  501 K     K   B . 
I 5 HOH   1   901  639 HOH   HOH A . 
I 5 HOH   2   902  896 HOH   HOH A . 
I 5 HOH   3   903  678 HOH   HOH A . 
I 5 HOH   4   904  197 HOH   HOH A . 
I 5 HOH   5   905  842 HOH   HOH A . 
I 5 HOH   6   906  759 HOH   HOH A . 
I 5 HOH   7   907  806 HOH   HOH A . 
I 5 HOH   8   908  408 HOH   HOH A . 
I 5 HOH   9   909  886 HOH   HOH A . 
I 5 HOH   10  910  783 HOH   HOH A . 
I 5 HOH   11  911  879 HOH   HOH A . 
I 5 HOH   12  912  602 HOH   HOH A . 
I 5 HOH   13  913  717 HOH   HOH A . 
I 5 HOH   14  914  453 HOH   HOH A . 
I 5 HOH   15  915  758 HOH   HOH A . 
I 5 HOH   16  916  96  HOH   HOH A . 
I 5 HOH   17  917  505 HOH   HOH A . 
I 5 HOH   18  918  311 HOH   HOH A . 
I 5 HOH   19  919  744 HOH   HOH A . 
I 5 HOH   20  920  465 HOH   HOH A . 
I 5 HOH   21  921  184 HOH   HOH A . 
I 5 HOH   22  922  328 HOH   HOH A . 
I 5 HOH   23  923  600 HOH   HOH A . 
I 5 HOH   24  924  209 HOH   HOH A . 
I 5 HOH   25  925  255 HOH   HOH A . 
I 5 HOH   26  926  180 HOH   HOH A . 
I 5 HOH   27  927  787 HOH   HOH A . 
I 5 HOH   28  928  146 HOH   HOH A . 
I 5 HOH   29  929  141 HOH   HOH A . 
I 5 HOH   30  930  126 HOH   HOH A . 
I 5 HOH   31  931  474 HOH   HOH A . 
I 5 HOH   32  932  24  HOH   HOH A . 
I 5 HOH   33  933  702 HOH   HOH A . 
I 5 HOH   34  934  332 HOH   HOH A . 
I 5 HOH   35  935  391 HOH   HOH A . 
I 5 HOH   36  936  56  HOH   HOH A . 
I 5 HOH   37  937  230 HOH   HOH A . 
I 5 HOH   38  938  60  HOH   HOH A . 
I 5 HOH   39  939  442 HOH   HOH A . 
I 5 HOH   40  940  526 HOH   HOH A . 
I 5 HOH   41  941  18  HOH   HOH A . 
I 5 HOH   42  942  215 HOH   HOH A . 
I 5 HOH   43  943  413 HOH   HOH A . 
I 5 HOH   44  944  846 HOH   HOH A . 
I 5 HOH   45  945  253 HOH   HOH A . 
I 5 HOH   46  946  5   HOH   HOH A . 
I 5 HOH   47  947  853 HOH   HOH A . 
I 5 HOH   48  948  32  HOH   HOH A . 
I 5 HOH   49  949  226 HOH   HOH A . 
I 5 HOH   50  950  55  HOH   HOH A . 
I 5 HOH   51  951  294 HOH   HOH A . 
I 5 HOH   52  952  120 HOH   HOH A . 
I 5 HOH   53  953  162 HOH   HOH A . 
I 5 HOH   54  954  176 HOH   HOH A . 
I 5 HOH   55  955  112 HOH   HOH A . 
I 5 HOH   56  956  242 HOH   HOH A . 
I 5 HOH   57  957  11  HOH   HOH A . 
I 5 HOH   58  958  901 HOH   HOH A . 
I 5 HOH   59  959  576 HOH   HOH A . 
I 5 HOH   60  960  415 HOH   HOH A . 
I 5 HOH   61  961  625 HOH   HOH A . 
I 5 HOH   62  962  115 HOH   HOH A . 
I 5 HOH   63  963  62  HOH   HOH A . 
I 5 HOH   64  964  278 HOH   HOH A . 
I 5 HOH   65  965  274 HOH   HOH A . 
I 5 HOH   66  966  928 HOH   HOH A . 
I 5 HOH   67  967  68  HOH   HOH A . 
I 5 HOH   68  968  569 HOH   HOH A . 
I 5 HOH   69  969  86  HOH   HOH A . 
I 5 HOH   70  970  164 HOH   HOH A . 
I 5 HOH   71  971  562 HOH   HOH A . 
I 5 HOH   72  972  268 HOH   HOH A . 
I 5 HOH   73  973  200 HOH   HOH A . 
I 5 HOH   74  974  223 HOH   HOH A . 
I 5 HOH   75  975  367 HOH   HOH A . 
I 5 HOH   76  976  193 HOH   HOH A . 
I 5 HOH   77  977  348 HOH   HOH A . 
I 5 HOH   78  978  189 HOH   HOH A . 
I 5 HOH   79  979  364 HOH   HOH A . 
I 5 HOH   80  980  822 HOH   HOH A . 
I 5 HOH   81  981  252 HOH   HOH A . 
I 5 HOH   82  982  762 HOH   HOH A . 
I 5 HOH   83  983  333 HOH   HOH A . 
I 5 HOH   84  984  860 HOH   HOH A . 
I 5 HOH   85  985  59  HOH   HOH A . 
I 5 HOH   86  986  149 HOH   HOH A . 
I 5 HOH   87  987  448 HOH   HOH A . 
I 5 HOH   88  988  16  HOH   HOH A . 
I 5 HOH   89  989  454 HOH   HOH A . 
I 5 HOH   90  990  21  HOH   HOH A . 
I 5 HOH   91  991  815 HOH   HOH A . 
I 5 HOH   92  992  939 HOH   HOH A . 
I 5 HOH   93  993  109 HOH   HOH A . 
I 5 HOH   94  994  265 HOH   HOH A . 
I 5 HOH   95  995  8   HOH   HOH A . 
I 5 HOH   96  996  509 HOH   HOH A . 
I 5 HOH   97  997  285 HOH   HOH A . 
I 5 HOH   98  998  2   HOH   HOH A . 
I 5 HOH   99  999  579 HOH   HOH A . 
I 5 HOH   100 1000 37  HOH   HOH A . 
I 5 HOH   101 1001 9   HOH   HOH A . 
I 5 HOH   102 1002 286 HOH   HOH A . 
I 5 HOH   103 1003 401 HOH   HOH A . 
I 5 HOH   104 1004 104 HOH   HOH A . 
I 5 HOH   105 1005 42  HOH   HOH A . 
I 5 HOH   106 1006 422 HOH   HOH A . 
I 5 HOH   107 1007 130 HOH   HOH A . 
I 5 HOH   108 1008 13  HOH   HOH A . 
I 5 HOH   109 1009 19  HOH   HOH A . 
I 5 HOH   110 1010 635 HOH   HOH A . 
I 5 HOH   111 1011 734 HOH   HOH A . 
I 5 HOH   112 1012 29  HOH   HOH A . 
I 5 HOH   113 1013 121 HOH   HOH A . 
I 5 HOH   114 1014 46  HOH   HOH A . 
I 5 HOH   115 1015 273 HOH   HOH A . 
I 5 HOH   116 1016 20  HOH   HOH A . 
I 5 HOH   117 1017 65  HOH   HOH A . 
I 5 HOH   118 1018 195 HOH   HOH A . 
I 5 HOH   119 1019 12  HOH   HOH A . 
I 5 HOH   120 1020 321 HOH   HOH A . 
I 5 HOH   121 1021 260 HOH   HOH A . 
I 5 HOH   122 1022 287 HOH   HOH A . 
I 5 HOH   123 1023 309 HOH   HOH A . 
I 5 HOH   124 1024 228 HOH   HOH A . 
I 5 HOH   125 1025 528 HOH   HOH A . 
I 5 HOH   126 1026 77  HOH   HOH A . 
I 5 HOH   127 1027 412 HOH   HOH A . 
I 5 HOH   128 1028 618 HOH   HOH A . 
I 5 HOH   129 1029 158 HOH   HOH A . 
I 5 HOH   130 1030 26  HOH   HOH A . 
I 5 HOH   131 1031 202 HOH   HOH A . 
I 5 HOH   132 1032 49  HOH   HOH A . 
I 5 HOH   133 1033 67  HOH   HOH A . 
I 5 HOH   134 1034 91  HOH   HOH A . 
I 5 HOH   135 1035 824 HOH   HOH A . 
I 5 HOH   136 1036 288 HOH   HOH A . 
I 5 HOH   137 1037 833 HOH   HOH A . 
I 5 HOH   138 1038 320 HOH   HOH A . 
I 5 HOH   139 1039 206 HOH   HOH A . 
I 5 HOH   140 1040 638 HOH   HOH A . 
I 5 HOH   141 1041 865 HOH   HOH A . 
I 5 HOH   142 1042 108 HOH   HOH A . 
I 5 HOH   143 1043 229 HOH   HOH A . 
I 5 HOH   144 1044 258 HOH   HOH A . 
I 5 HOH   145 1045 306 HOH   HOH A . 
I 5 HOH   146 1046 107 HOH   HOH A . 
I 5 HOH   147 1047 231 HOH   HOH A . 
I 5 HOH   148 1048 190 HOH   HOH A . 
I 5 HOH   149 1049 39  HOH   HOH A . 
I 5 HOH   150 1050 564 HOH   HOH A . 
I 5 HOH   151 1051 897 HOH   HOH A . 
I 5 HOH   152 1052 205 HOH   HOH A . 
I 5 HOH   153 1053 435 HOH   HOH A . 
I 5 HOH   154 1054 324 HOH   HOH A . 
I 5 HOH   155 1055 41  HOH   HOH A . 
I 5 HOH   156 1056 507 HOH   HOH A . 
I 5 HOH   157 1057 293 HOH   HOH A . 
I 5 HOH   158 1058 125 HOH   HOH A . 
I 5 HOH   159 1059 598 HOH   HOH A . 
I 5 HOH   160 1060 142 HOH   HOH A . 
I 5 HOH   161 1061 361 HOH   HOH A . 
I 5 HOH   162 1062 151 HOH   HOH A . 
I 5 HOH   163 1063 852 HOH   HOH A . 
I 5 HOH   164 1064 262 HOH   HOH A . 
I 5 HOH   165 1065 338 HOH   HOH A . 
I 5 HOH   166 1066 396 HOH   HOH A . 
I 5 HOH   167 1067 53  HOH   HOH A . 
I 5 HOH   168 1068 78  HOH   HOH A . 
I 5 HOH   169 1069 698 HOH   HOH A . 
I 5 HOH   170 1070 43  HOH   HOH A . 
I 5 HOH   171 1071 446 HOH   HOH A . 
I 5 HOH   172 1072 404 HOH   HOH A . 
I 5 HOH   173 1073 627 HOH   HOH A . 
I 5 HOH   174 1074 179 HOH   HOH A . 
I 5 HOH   175 1075 578 HOH   HOH A . 
I 5 HOH   176 1076 443 HOH   HOH A . 
I 5 HOH   177 1077 350 HOH   HOH A . 
I 5 HOH   178 1078 153 HOH   HOH A . 
I 5 HOH   179 1079 792 HOH   HOH A . 
I 5 HOH   180 1080 106 HOH   HOH A . 
I 5 HOH   181 1081 385 HOH   HOH A . 
I 5 HOH   182 1082 399 HOH   HOH A . 
I 5 HOH   183 1083 838 HOH   HOH A . 
I 5 HOH   184 1084 628 HOH   HOH A . 
I 5 HOH   185 1085 129 HOH   HOH A . 
I 5 HOH   186 1086 346 HOH   HOH A . 
I 5 HOH   187 1087 118 HOH   HOH A . 
I 5 HOH   188 1088 820 HOH   HOH A . 
I 5 HOH   189 1089 248 HOH   HOH A . 
I 5 HOH   190 1090 145 HOH   HOH A . 
I 5 HOH   191 1091 888 HOH   HOH A . 
I 5 HOH   192 1092 203 HOH   HOH A . 
I 5 HOH   193 1093 684 HOH   HOH A . 
I 5 HOH   194 1094 303 HOH   HOH A . 
I 5 HOH   195 1095 224 HOH   HOH A . 
I 5 HOH   196 1096 52  HOH   HOH A . 
I 5 HOH   197 1097 220 HOH   HOH A . 
I 5 HOH   198 1098 864 HOH   HOH A . 
I 5 HOH   199 1099 267 HOH   HOH A . 
I 5 HOH   200 1100 143 HOH   HOH A . 
I 5 HOH   201 1101 289 HOH   HOH A . 
I 5 HOH   202 1102 166 HOH   HOH A . 
I 5 HOH   203 1103 33  HOH   HOH A . 
I 5 HOH   204 1104 931 HOH   HOH A . 
I 5 HOH   205 1105 814 HOH   HOH A . 
I 5 HOH   206 1106 64  HOH   HOH A . 
I 5 HOH   207 1107 733 HOH   HOH A . 
I 5 HOH   208 1108 246 HOH   HOH A . 
I 5 HOH   209 1109 119 HOH   HOH A . 
I 5 HOH   210 1110 817 HOH   HOH A . 
I 5 HOH   211 1111 218 HOH   HOH A . 
I 5 HOH   212 1112 244 HOH   HOH A . 
I 5 HOH   213 1113 238 HOH   HOH A . 
I 5 HOH   214 1114 464 HOH   HOH A . 
I 5 HOH   215 1115 467 HOH   HOH A . 
I 5 HOH   216 1116 418 HOH   HOH A . 
I 5 HOH   217 1117 174 HOH   HOH A . 
I 5 HOH   218 1118 98  HOH   HOH A . 
I 5 HOH   219 1119 171 HOH   HOH A . 
I 5 HOH   220 1120 591 HOH   HOH A . 
I 5 HOH   221 1121 307 HOH   HOH A . 
I 5 HOH   222 1122 745 HOH   HOH A . 
I 5 HOH   223 1123 183 HOH   HOH A . 
I 5 HOH   224 1124 471 HOH   HOH A . 
I 5 HOH   225 1125 432 HOH   HOH A . 
I 5 HOH   226 1126 270 HOH   HOH A . 
I 5 HOH   227 1127 593 HOH   HOH A . 
I 5 HOH   228 1128 712 HOH   HOH A . 
I 5 HOH   229 1129 450 HOH   HOH A . 
I 5 HOH   230 1130 144 HOH   HOH A . 
I 5 HOH   231 1131 552 HOH   HOH A . 
I 5 HOH   232 1132 210 HOH   HOH A . 
I 5 HOH   233 1133 780 HOH   HOH A . 
I 5 HOH   234 1134 877 HOH   HOH A . 
I 5 HOH   235 1135 907 HOH   HOH A . 
I 5 HOH   236 1136 584 HOH   HOH A . 
I 5 HOH   237 1137 495 HOH   HOH A . 
I 5 HOH   238 1138 277 HOH   HOH A . 
I 5 HOH   239 1139 58  HOH   HOH A . 
I 5 HOH   240 1140 726 HOH   HOH A . 
I 5 HOH   241 1141 577 HOH   HOH A . 
I 5 HOH   242 1142 88  HOH   HOH A . 
I 5 HOH   243 1143 275 HOH   HOH A . 
I 5 HOH   244 1144 155 HOH   HOH A . 
I 5 HOH   245 1145 72  HOH   HOH A . 
I 5 HOH   246 1146 586 HOH   HOH A . 
I 5 HOH   247 1147 947 HOH   HOH A . 
I 5 HOH   248 1148 873 HOH   HOH A . 
I 5 HOH   249 1149 656 HOH   HOH A . 
I 5 HOH   250 1150 929 HOH   HOH A . 
I 5 HOH   251 1151 761 HOH   HOH A . 
I 5 HOH   252 1152 478 HOH   HOH A . 
I 5 HOH   253 1153 148 HOH   HOH A . 
I 5 HOH   254 1154 867 HOH   HOH A . 
I 5 HOH   255 1155 74  HOH   HOH A . 
I 5 HOH   256 1156 132 HOH   HOH A . 
I 5 HOH   257 1157 356 HOH   HOH A . 
I 5 HOH   258 1158 383 HOH   HOH A . 
I 5 HOH   259 1159 379 HOH   HOH A . 
I 5 HOH   260 1160 298 HOH   HOH A . 
I 5 HOH   261 1161 549 HOH   HOH A . 
I 5 HOH   262 1162 803 HOH   HOH A . 
I 5 HOH   263 1163 604 HOH   HOH A . 
I 5 HOH   264 1164 652 HOH   HOH A . 
I 5 HOH   265 1165 160 HOH   HOH A . 
I 5 HOH   266 1166 159 HOH   HOH A . 
I 5 HOH   267 1167 264 HOH   HOH A . 
I 5 HOH   268 1168 725 HOH   HOH A . 
I 5 HOH   269 1169 861 HOH   HOH A . 
I 5 HOH   270 1170 609 HOH   HOH A . 
I 5 HOH   271 1171 629 HOH   HOH A . 
I 5 HOH   272 1172 373 HOH   HOH A . 
I 5 HOH   273 1173 349 HOH   HOH A . 
I 5 HOH   274 1174 839 HOH   HOH A . 
I 5 HOH   275 1175 529 HOH   HOH A . 
I 5 HOH   276 1176 491 HOH   HOH A . 
I 5 HOH   277 1177 945 HOH   HOH A . 
I 5 HOH   278 1178 531 HOH   HOH A . 
I 5 HOH   279 1179 894 HOH   HOH A . 
I 5 HOH   280 1180 477 HOH   HOH A . 
I 5 HOH   281 1181 553 HOH   HOH A . 
I 5 HOH   282 1182 426 HOH   HOH A . 
I 5 HOH   283 1183 483 HOH   HOH A . 
I 5 HOH   284 1184 551 HOH   HOH A . 
I 5 HOH   285 1185 386 HOH   HOH A . 
I 5 HOH   286 1186 508 HOH   HOH A . 
I 5 HOH   287 1187 854 HOH   HOH A . 
I 5 HOH   288 1188 616 HOH   HOH A . 
I 5 HOH   289 1189 791 HOH   HOH A . 
I 5 HOH   290 1190 181 HOH   HOH A . 
I 5 HOH   291 1191 534 HOH   HOH A . 
I 5 HOH   292 1192 859 HOH   HOH A . 
I 5 HOH   293 1193 654 HOH   HOH A . 
I 5 HOH   294 1194 473 HOH   HOH A . 
I 5 HOH   295 1195 871 HOH   HOH A . 
I 5 HOH   296 1196 472 HOH   HOH A . 
I 5 HOH   297 1197 587 HOH   HOH A . 
I 5 HOH   298 1198 889 HOH   HOH A . 
I 5 HOH   299 1199 646 HOH   HOH A . 
I 5 HOH   300 1200 921 HOH   HOH A . 
I 5 HOH   301 1201 801 HOH   HOH A . 
I 5 HOH   302 1202 133 HOH   HOH A . 
I 5 HOH   303 1203 676 HOH   HOH A . 
I 5 HOH   304 1204 574 HOH   HOH A . 
I 5 HOH   305 1205 764 HOH   HOH A . 
I 5 HOH   306 1206 862 HOH   HOH A . 
I 5 HOH   307 1207 256 HOH   HOH A . 
I 5 HOH   308 1208 468 HOH   HOH A . 
I 5 HOH   309 1209 335 HOH   HOH A . 
I 5 HOH   310 1210 485 HOH   HOH A . 
I 5 HOH   311 1211 445 HOH   HOH A . 
I 5 HOH   312 1212 706 HOH   HOH A . 
I 5 HOH   313 1213 697 HOH   HOH A . 
I 5 HOH   314 1214 537 HOH   HOH A . 
I 5 HOH   315 1215 245 HOH   HOH A . 
I 5 HOH   316 1216 235 HOH   HOH A . 
I 5 HOH   317 1217 536 HOH   HOH A . 
I 5 HOH   318 1218 703 HOH   HOH A . 
I 5 HOH   319 1219 503 HOH   HOH A . 
I 5 HOH   320 1220 540 HOH   HOH A . 
I 5 HOH   321 1221 369 HOH   HOH A . 
I 5 HOH   322 1222 284 HOH   HOH A . 
I 5 HOH   323 1223 263 HOH   HOH A . 
I 5 HOH   324 1224 918 HOH   HOH A . 
I 5 HOH   325 1225 941 HOH   HOH A . 
I 5 HOH   326 1226 872 HOH   HOH A . 
I 5 HOH   327 1227 140 HOH   HOH A . 
I 5 HOH   328 1228 884 HOH   HOH A . 
I 5 HOH   329 1229 431 HOH   HOH A . 
I 5 HOH   330 1230 329 HOH   HOH A . 
I 5 HOH   331 1231 751 HOH   HOH A . 
I 5 HOH   332 1232 707 HOH   HOH A . 
I 5 HOH   333 1233 186 HOH   HOH A . 
I 5 HOH   334 1234 855 HOH   HOH A . 
I 5 HOH   335 1235 685 HOH   HOH A . 
I 5 HOH   336 1236 624 HOH   HOH A . 
I 5 HOH   337 1237 870 HOH   HOH A . 
I 5 HOH   338 1238 812 HOH   HOH A . 
I 5 HOH   339 1239 281 HOH   HOH A . 
I 5 HOH   340 1240 302 HOH   HOH A . 
I 5 HOH   341 1241 856 HOH   HOH A . 
I 5 HOH   342 1242 384 HOH   HOH A . 
I 5 HOH   343 1243 633 HOH   HOH A . 
I 5 HOH   344 1244 523 HOH   HOH A . 
I 5 HOH   345 1245 506 HOH   HOH A . 
I 5 HOH   346 1246 779 HOH   HOH A . 
I 5 HOH   347 1247 672 HOH   HOH A . 
I 5 HOH   348 1248 400 HOH   HOH A . 
I 5 HOH   349 1249 885 HOH   HOH A . 
I 5 HOH   350 1250 101 HOH   HOH A . 
I 5 HOH   351 1251 571 HOH   HOH A . 
I 5 HOH   352 1252 251 HOH   HOH A . 
I 5 HOH   353 1253 731 HOH   HOH A . 
I 5 HOH   354 1254 935 HOH   HOH A . 
I 5 HOH   355 1255 425 HOH   HOH A . 
I 5 HOH   356 1256 686 HOH   HOH A . 
I 5 HOH   357 1257 461 HOH   HOH A . 
I 5 HOH   358 1258 809 HOH   HOH A . 
I 5 HOH   359 1259 608 HOH   HOH A . 
I 5 HOH   360 1260 325 HOH   HOH A . 
I 5 HOH   361 1261 496 HOH   HOH A . 
I 5 HOH   362 1262 757 HOH   HOH A . 
I 5 HOH   363 1263 800 HOH   HOH A . 
I 5 HOH   364 1264 388 HOH   HOH A . 
I 5 HOH   365 1265 795 HOH   HOH A . 
I 5 HOH   366 1266 178 HOH   HOH A . 
I 5 HOH   367 1267 405 HOH   HOH A . 
I 5 HOH   368 1268 623 HOH   HOH A . 
I 5 HOH   369 1269 642 HOH   HOH A . 
I 5 HOH   370 1270 671 HOH   HOH A . 
I 5 HOH   371 1271 173 HOH   HOH A . 
I 5 HOH   372 1272 344 HOH   HOH A . 
I 5 HOH   373 1273 919 HOH   HOH A . 
I 5 HOH   374 1274 705 HOH   HOH A . 
I 5 HOH   375 1275 647 HOH   HOH A . 
I 5 HOH   376 1276 811 HOH   HOH A . 
I 5 HOH   377 1277 550 HOH   HOH A . 
I 5 HOH   378 1278 799 HOH   HOH A . 
I 5 HOH   379 1279 798 HOH   HOH A . 
I 5 HOH   380 1280 420 HOH   HOH A . 
I 5 HOH   381 1281 701 HOH   HOH A . 
I 5 HOH   382 1282 542 HOH   HOH A . 
I 5 HOH   383 1283 915 HOH   HOH A . 
I 5 HOH   384 1284 458 HOH   HOH A . 
I 5 HOH   385 1285 358 HOH   HOH A . 
I 5 HOH   386 1286 299 HOH   HOH A . 
I 5 HOH   387 1287 488 HOH   HOH A . 
I 5 HOH   388 1288 323 HOH   HOH A . 
I 5 HOH   389 1289 269 HOH   HOH A . 
I 5 HOH   390 1290 890 HOH   HOH A . 
I 5 HOH   391 1291 775 HOH   HOH A . 
I 5 HOH   392 1292 765 HOH   HOH A . 
I 5 HOH   393 1293 911 HOH   HOH A . 
I 5 HOH   394 1294 596 HOH   HOH A . 
I 5 HOH   395 1295 796 HOH   HOH A . 
I 5 HOH   396 1296 527 HOH   HOH A . 
I 5 HOH   397 1297 723 HOH   HOH A . 
I 5 HOH   398 1298 845 HOH   HOH A . 
I 5 HOH   399 1299 570 HOH   HOH A . 
I 5 HOH   400 1300 881 HOH   HOH A . 
J 5 HOH   1   901  662 HOH   HOH B . 
J 5 HOH   2   902  651 HOH   HOH B . 
J 5 HOH   3   903  456 HOH   HOH B . 
J 5 HOH   4   904  753 HOH   HOH B . 
J 5 HOH   5   905  704 HOH   HOH B . 
J 5 HOH   6   906  768 HOH   HOH B . 
J 5 HOH   7   907  480 HOH   HOH B . 
J 5 HOH   8   908  621 HOH   HOH B . 
J 5 HOH   9   909  147 HOH   HOH B . 
J 5 HOH   10  910  331 HOH   HOH B . 
J 5 HOH   11  911  857 HOH   HOH B . 
J 5 HOH   12  912  607 HOH   HOH B . 
J 5 HOH   13  913  891 HOH   HOH B . 
J 5 HOH   14  914  925 HOH   HOH B . 
J 5 HOH   15  915  946 HOH   HOH B . 
J 5 HOH   16  916  592 HOH   HOH B . 
J 5 HOH   17  917  463 HOH   HOH B . 
J 5 HOH   18  918  843 HOH   HOH B . 
J 5 HOH   19  919  785 HOH   HOH B . 
J 5 HOH   20  920  777 HOH   HOH B . 
J 5 HOH   21  921  511 HOH   HOH B . 
J 5 HOH   22  922  381 HOH   HOH B . 
J 5 HOH   23  923  100 HOH   HOH B . 
J 5 HOH   24  924  417 HOH   HOH B . 
J 5 HOH   25  925  169 HOH   HOH B . 
J 5 HOH   26  926  87  HOH   HOH B . 
J 5 HOH   27  927  280 HOH   HOH B . 
J 5 HOH   28  928  545 HOH   HOH B . 
J 5 HOH   29  929  172 HOH   HOH B . 
J 5 HOH   30  930  342 HOH   HOH B . 
J 5 HOH   31  931  243 HOH   HOH B . 
J 5 HOH   32  932  493 HOH   HOH B . 
J 5 HOH   33  933  127 HOH   HOH B . 
J 5 HOH   34  934  729 HOH   HOH B . 
J 5 HOH   35  935  345 HOH   HOH B . 
J 5 HOH   36  936  643 HOH   HOH B . 
J 5 HOH   37  937  354 HOH   HOH B . 
J 5 HOH   38  938  122 HOH   HOH B . 
J 5 HOH   39  939  315 HOH   HOH B . 
J 5 HOH   40  940  207 HOH   HOH B . 
J 5 HOH   41  941  599 HOH   HOH B . 
J 5 HOH   42  942  219 HOH   HOH B . 
J 5 HOH   43  943  375 HOH   HOH B . 
J 5 HOH   44  944  124 HOH   HOH B . 
J 5 HOH   45  945  645 HOH   HOH B . 
J 5 HOH   46  946  588 HOH   HOH B . 
J 5 HOH   47  947  581 HOH   HOH B . 
J 5 HOH   48  948  7   HOH   HOH B . 
J 5 HOH   49  949  234 HOH   HOH B . 
J 5 HOH   50  950  720 HOH   HOH B . 
J 5 HOH   51  951  308 HOH   HOH B . 
J 5 HOH   52  952  441 HOH   HOH B . 
J 5 HOH   53  953  50  HOH   HOH B . 
J 5 HOH   54  954  357 HOH   HOH B . 
J 5 HOH   55  955  1   HOH   HOH B . 
J 5 HOH   56  956  25  HOH   HOH B . 
J 5 HOH   57  957  492 HOH   HOH B . 
J 5 HOH   58  958  73  HOH   HOH B . 
J 5 HOH   59  959  114 HOH   HOH B . 
J 5 HOH   60  960  71  HOH   HOH B . 
J 5 HOH   61  961  154 HOH   HOH B . 
J 5 HOH   62  962  519 HOH   HOH B . 
J 5 HOH   63  963  17  HOH   HOH B . 
J 5 HOH   64  964  318 HOH   HOH B . 
J 5 HOH   65  965  157 HOH   HOH B . 
J 5 HOH   66  966  353 HOH   HOH B . 
J 5 HOH   67  967  470 HOH   HOH B . 
J 5 HOH   68  968  337 HOH   HOH B . 
J 5 HOH   69  969  372 HOH   HOH B . 
J 5 HOH   70  970  136 HOH   HOH B . 
J 5 HOH   71  971  398 HOH   HOH B . 
J 5 HOH   72  972  3   HOH   HOH B . 
J 5 HOH   73  973  57  HOH   HOH B . 
J 5 HOH   74  974  152 HOH   HOH B . 
J 5 HOH   75  975  36  HOH   HOH B . 
J 5 HOH   76  976  44  HOH   HOH B . 
J 5 HOH   77  977  330 HOH   HOH B . 
J 5 HOH   78  978  589 HOH   HOH B . 
J 5 HOH   79  979  191 HOH   HOH B . 
J 5 HOH   80  980  222 HOH   HOH B . 
J 5 HOH   81  981  182 HOH   HOH B . 
J 5 HOH   82  982  30  HOH   HOH B . 
J 5 HOH   83  983  156 HOH   HOH B . 
J 5 HOH   84  984  38  HOH   HOH B . 
J 5 HOH   85  985  520 HOH   HOH B . 
J 5 HOH   86  986  459 HOH   HOH B . 
J 5 HOH   87  987  66  HOH   HOH B . 
J 5 HOH   88  988  117 HOH   HOH B . 
J 5 HOH   89  989  402 HOH   HOH B . 
J 5 HOH   90  990  6   HOH   HOH B . 
J 5 HOH   91  991  116 HOH   HOH B . 
J 5 HOH   92  992  649 HOH   HOH B . 
J 5 HOH   93  993  233 HOH   HOH B . 
J 5 HOH   94  994  371 HOH   HOH B . 
J 5 HOH   95  995  4   HOH   HOH B . 
J 5 HOH   96  996  583 HOH   HOH B . 
J 5 HOH   97  997  772 HOH   HOH B . 
J 5 HOH   98  998  214 HOH   HOH B . 
J 5 HOH   99  999  336 HOH   HOH B . 
J 5 HOH   100 1000 316 HOH   HOH B . 
J 5 HOH   101 1001 187 HOH   HOH B . 
J 5 HOH   102 1002 95  HOH   HOH B . 
J 5 HOH   103 1003 736 HOH   HOH B . 
J 5 HOH   104 1004 355 HOH   HOH B . 
J 5 HOH   105 1005 35  HOH   HOH B . 
J 5 HOH   106 1006 128 HOH   HOH B . 
J 5 HOH   107 1007 250 HOH   HOH B . 
J 5 HOH   108 1008 14  HOH   HOH B . 
J 5 HOH   109 1009 175 HOH   HOH B . 
J 5 HOH   110 1010 168 HOH   HOH B . 
J 5 HOH   111 1011 167 HOH   HOH B . 
J 5 HOH   112 1012 825 HOH   HOH B . 
J 5 HOH   113 1013 614 HOH   HOH B . 
J 5 HOH   114 1014 10  HOH   HOH B . 
J 5 HOH   115 1015 573 HOH   HOH B . 
J 5 HOH   116 1016 40  HOH   HOH B . 
J 5 HOH   117 1017 407 HOH   HOH B . 
J 5 HOH   118 1018 23  HOH   HOH B . 
J 5 HOH   119 1019 99  HOH   HOH B . 
J 5 HOH   120 1020 377 HOH   HOH B . 
J 5 HOH   121 1021 513 HOH   HOH B . 
J 5 HOH   122 1022 295 HOH   HOH B . 
J 5 HOH   123 1023 790 HOH   HOH B . 
J 5 HOH   124 1024 76  HOH   HOH B . 
J 5 HOH   125 1025 161 HOH   HOH B . 
J 5 HOH   126 1026 439 HOH   HOH B . 
J 5 HOH   127 1027 232 HOH   HOH B . 
J 5 HOH   128 1028 165 HOH   HOH B . 
J 5 HOH   129 1029 75  HOH   HOH B . 
J 5 HOH   130 1030 452 HOH   HOH B . 
J 5 HOH   131 1031 135 HOH   HOH B . 
J 5 HOH   132 1032 177 HOH   HOH B . 
J 5 HOH   133 1033 199 HOH   HOH B . 
J 5 HOH   134 1034 196 HOH   HOH B . 
J 5 HOH   135 1035 580 HOH   HOH B . 
J 5 HOH   136 1036 22  HOH   HOH B . 
J 5 HOH   137 1037 276 HOH   HOH B . 
J 5 HOH   138 1038 427 HOH   HOH B . 
J 5 HOH   139 1039 31  HOH   HOH B . 
J 5 HOH   140 1040 90  HOH   HOH B . 
J 5 HOH   141 1041 45  HOH   HOH B . 
J 5 HOH   142 1042 760 HOH   HOH B . 
J 5 HOH   143 1043 47  HOH   HOH B . 
J 5 HOH   144 1044 397 HOH   HOH B . 
J 5 HOH   145 1045 561 HOH   HOH B . 
J 5 HOH   146 1046 359 HOH   HOH B . 
J 5 HOH   147 1047 370 HOH   HOH B . 
J 5 HOH   148 1048 682 HOH   HOH B . 
J 5 HOH   149 1049 518 HOH   HOH B . 
J 5 HOH   150 1050 54  HOH   HOH B . 
J 5 HOH   151 1051 317 HOH   HOH B . 
J 5 HOH   152 1052 27  HOH   HOH B . 
J 5 HOH   153 1053 436 HOH   HOH B . 
J 5 HOH   154 1054 240 HOH   HOH B . 
J 5 HOH   155 1055 150 HOH   HOH B . 
J 5 HOH   156 1056 490 HOH   HOH B . 
J 5 HOH   157 1057 658 HOH   HOH B . 
J 5 HOH   158 1058 606 HOH   HOH B . 
J 5 HOH   159 1059 314 HOH   HOH B . 
J 5 HOH   160 1060 110 HOH   HOH B . 
J 5 HOH   161 1061 565 HOH   HOH B . 
J 5 HOH   162 1062 97  HOH   HOH B . 
J 5 HOH   163 1063 249 HOH   HOH B . 
J 5 HOH   164 1064 746 HOH   HOH B . 
J 5 HOH   165 1065 395 HOH   HOH B . 
J 5 HOH   166 1066 94  HOH   HOH B . 
J 5 HOH   167 1067 51  HOH   HOH B . 
J 5 HOH   168 1068 489 HOH   HOH B . 
J 5 HOH   169 1069 634 HOH   HOH B . 
J 5 HOH   170 1070 89  HOH   HOH B . 
J 5 HOH   171 1071 15  HOH   HOH B . 
J 5 HOH   172 1072 541 HOH   HOH B . 
J 5 HOH   173 1073 111 HOH   HOH B . 
J 5 HOH   174 1074 827 HOH   HOH B . 
J 5 HOH   175 1075 211 HOH   HOH B . 
J 5 HOH   176 1076 212 HOH   HOH B . 
J 5 HOH   177 1077 79  HOH   HOH B . 
J 5 HOH   178 1078 70  HOH   HOH B . 
J 5 HOH   179 1079 297 HOH   HOH B . 
J 5 HOH   180 1080 366 HOH   HOH B . 
J 5 HOH   181 1081 713 HOH   HOH B . 
J 5 HOH   182 1082 650 HOH   HOH B . 
J 5 HOH   183 1083 449 HOH   HOH B . 
J 5 HOH   184 1084 296 HOH   HOH B . 
J 5 HOH   185 1085 139 HOH   HOH B . 
J 5 HOH   186 1086 326 HOH   HOH B . 
J 5 HOH   187 1087 28  HOH   HOH B . 
J 5 HOH   188 1088 301 HOH   HOH B . 
J 5 HOH   189 1089 271 HOH   HOH B . 
J 5 HOH   190 1090 341 HOH   HOH B . 
J 5 HOH   191 1091 305 HOH   HOH B . 
J 5 HOH   192 1092 217 HOH   HOH B . 
J 5 HOH   193 1093 63  HOH   HOH B . 
J 5 HOH   194 1094 532 HOH   HOH B . 
J 5 HOH   195 1095 221 HOH   HOH B . 
J 5 HOH   196 1096 419 HOH   HOH B . 
J 5 HOH   197 1097 816 HOH   HOH B . 
J 5 HOH   198 1098 585 HOH   HOH B . 
J 5 HOH   199 1099 679 HOH   HOH B . 
J 5 HOH   200 1100 257 HOH   HOH B . 
J 5 HOH   201 1101 774 HOH   HOH B . 
J 5 HOH   202 1102 292 HOH   HOH B . 
J 5 HOH   203 1103 34  HOH   HOH B . 
J 5 HOH   204 1104 300 HOH   HOH B . 
J 5 HOH   205 1105 601 HOH   HOH B . 
J 5 HOH   206 1106 48  HOH   HOH B . 
J 5 HOH   207 1107 365 HOH   HOH B . 
J 5 HOH   208 1108 82  HOH   HOH B . 
J 5 HOH   209 1109 673 HOH   HOH B . 
J 5 HOH   210 1110 752 HOH   HOH B . 
J 5 HOH   211 1111 247 HOH   HOH B . 
J 5 HOH   212 1112 188 HOH   HOH B . 
J 5 HOH   213 1113 113 HOH   HOH B . 
J 5 HOH   214 1114 669 HOH   HOH B . 
J 5 HOH   215 1115 81  HOH   HOH B . 
J 5 HOH   216 1116 674 HOH   HOH B . 
J 5 HOH   217 1117 170 HOH   HOH B . 
J 5 HOH   218 1118 414 HOH   HOH B . 
J 5 HOH   219 1119 572 HOH   HOH B . 
J 5 HOH   220 1120 92  HOH   HOH B . 
J 5 HOH   221 1121 693 HOH   HOH B . 
J 5 HOH   222 1122 123 HOH   HOH B . 
J 5 HOH   223 1123 134 HOH   HOH B . 
J 5 HOH   224 1124 546 HOH   HOH B . 
J 5 HOH   225 1125 131 HOH   HOH B . 
J 5 HOH   226 1126 103 HOH   HOH B . 
J 5 HOH   227 1127 749 HOH   HOH B . 
J 5 HOH   228 1128 272 HOH   HOH B . 
J 5 HOH   229 1129 185 HOH   HOH B . 
J 5 HOH   230 1130 351 HOH   HOH B . 
J 5 HOH   231 1131 512 HOH   HOH B . 
J 5 HOH   232 1132 80  HOH   HOH B . 
J 5 HOH   233 1133 416 HOH   HOH B . 
J 5 HOH   234 1134 848 HOH   HOH B . 
J 5 HOH   235 1135 241 HOH   HOH B . 
J 5 HOH   236 1136 866 HOH   HOH B . 
J 5 HOH   237 1137 393 HOH   HOH B . 
J 5 HOH   238 1138 327 HOH   HOH B . 
J 5 HOH   239 1139 69  HOH   HOH B . 
J 5 HOH   240 1140 594 HOH   HOH B . 
J 5 HOH   241 1141 498 HOH   HOH B . 
J 5 HOH   242 1142 291 HOH   HOH B . 
J 5 HOH   243 1143 482 HOH   HOH B . 
J 5 HOH   244 1144 653 HOH   HOH B . 
J 5 HOH   245 1145 410 HOH   HOH B . 
J 5 HOH   246 1146 93  HOH   HOH B . 
J 5 HOH   247 1147 304 HOH   HOH B . 
J 5 HOH   248 1148 666 HOH   HOH B . 
J 5 HOH   249 1149 782 HOH   HOH B . 
J 5 HOH   250 1150 755 HOH   HOH B . 
J 5 HOH   251 1151 724 HOH   HOH B . 
J 5 HOH   252 1152 347 HOH   HOH B . 
J 5 HOH   253 1153 691 HOH   HOH B . 
J 5 HOH   254 1154 105 HOH   HOH B . 
J 5 HOH   255 1155 225 HOH   HOH B . 
J 5 HOH   256 1156 279 HOH   HOH B . 
J 5 HOH   257 1157 667 HOH   HOH B . 
J 5 HOH   258 1158 339 HOH   HOH B . 
J 5 HOH   259 1159 836 HOH   HOH B . 
J 5 HOH   260 1160 711 HOH   HOH B . 
J 5 HOH   261 1161 595 HOH   HOH B . 
J 5 HOH   262 1162 438 HOH   HOH B . 
J 5 HOH   263 1163 387 HOH   HOH B . 
J 5 HOH   264 1164 429 HOH   HOH B . 
J 5 HOH   265 1165 83  HOH   HOH B . 
J 5 HOH   266 1166 376 HOH   HOH B . 
J 5 HOH   267 1167 556 HOH   HOH B . 
J 5 HOH   268 1168 605 HOH   HOH B . 
J 5 HOH   269 1169 501 HOH   HOH B . 
J 5 HOH   270 1170 84  HOH   HOH B . 
J 5 HOH   271 1171 835 HOH   HOH B . 
J 5 HOH   272 1172 476 HOH   HOH B . 
J 5 HOH   273 1173 61  HOH   HOH B . 
J 5 HOH   274 1174 499 HOH   HOH B . 
J 5 HOH   275 1175 486 HOH   HOH B . 
J 5 HOH   276 1176 259 HOH   HOH B . 
J 5 HOH   277 1177 920 HOH   HOH B . 
J 5 HOH   278 1178 769 HOH   HOH B . 
J 5 HOH   279 1179 227 HOH   HOH B . 
J 5 HOH   280 1180 236 HOH   HOH B . 
J 5 HOH   281 1181 902 HOH   HOH B . 
J 5 HOH   282 1182 102 HOH   HOH B . 
J 5 HOH   283 1183 844 HOH   HOH B . 
J 5 HOH   284 1184 469 HOH   HOH B . 
J 5 HOH   285 1185 457 HOH   HOH B . 
J 5 HOH   286 1186 208 HOH   HOH B . 
J 5 HOH   287 1187 677 HOH   HOH B . 
J 5 HOH   288 1188 434 HOH   HOH B . 
J 5 HOH   289 1189 340 HOH   HOH B . 
J 5 HOH   290 1190 690 HOH   HOH B . 
J 5 HOH   291 1191 590 HOH   HOH B . 
J 5 HOH   292 1192 858 HOH   HOH B . 
J 5 HOH   293 1193 517 HOH   HOH B . 
J 5 HOH   294 1194 730 HOH   HOH B . 
J 5 HOH   295 1195 924 HOH   HOH B . 
J 5 HOH   296 1196 626 HOH   HOH B . 
J 5 HOH   297 1197 819 HOH   HOH B . 
J 5 HOH   298 1198 525 HOH   HOH B . 
J 5 HOH   299 1199 789 HOH   HOH B . 
J 5 HOH   300 1200 793 HOH   HOH B . 
J 5 HOH   301 1201 522 HOH   HOH B . 
J 5 HOH   302 1202 899 HOH   HOH B . 
J 5 HOH   303 1203 575 HOH   HOH B . 
J 5 HOH   304 1204 192 HOH   HOH B . 
J 5 HOH   305 1205 632 HOH   HOH B . 
J 5 HOH   306 1206 566 HOH   HOH B . 
J 5 HOH   307 1207 394 HOH   HOH B . 
J 5 HOH   308 1208 738 HOH   HOH B . 
J 5 HOH   309 1209 360 HOH   HOH B . 
J 5 HOH   310 1210 696 HOH   HOH B . 
J 5 HOH   311 1211 613 HOH   HOH B . 
J 5 HOH   312 1212 763 HOH   HOH B . 
J 5 HOH   313 1213 559 HOH   HOH B . 
J 5 HOH   314 1214 310 HOH   HOH B . 
J 5 HOH   315 1215 368 HOH   HOH B . 
J 5 HOH   316 1216 830 HOH   HOH B . 
J 5 HOH   317 1217 823 HOH   HOH B . 
J 5 HOH   318 1218 837 HOH   HOH B . 
J 5 HOH   319 1219 198 HOH   HOH B . 
J 5 HOH   320 1220 424 HOH   HOH B . 
J 5 HOH   321 1221 502 HOH   HOH B . 
J 5 HOH   322 1222 521 HOH   HOH B . 
J 5 HOH   323 1223 687 HOH   HOH B . 
J 5 HOH   324 1224 138 HOH   HOH B . 
J 5 HOH   325 1225 719 HOH   HOH B . 
J 5 HOH   326 1226 747 HOH   HOH B . 
J 5 HOH   327 1227 555 HOH   HOH B . 
J 5 HOH   328 1228 204 HOH   HOH B . 
J 5 HOH   329 1229 430 HOH   HOH B . 
J 5 HOH   330 1230 533 HOH   HOH B . 
J 5 HOH   331 1231 699 HOH   HOH B . 
J 5 HOH   332 1232 876 HOH   HOH B . 
J 5 HOH   333 1233 563 HOH   HOH B . 
J 5 HOH   334 1234 849 HOH   HOH B . 
J 5 HOH   335 1235 926 HOH   HOH B . 
J 5 HOH   336 1236 460 HOH   HOH B . 
J 5 HOH   337 1237 788 HOH   HOH B . 
J 5 HOH   338 1238 421 HOH   HOH B . 
J 5 HOH   339 1239 878 HOH   HOH B . 
J 5 HOH   340 1240 382 HOH   HOH B . 
J 5 HOH   341 1241 479 HOH   HOH B . 
J 5 HOH   342 1242 805 HOH   HOH B . 
J 5 HOH   343 1243 216 HOH   HOH B . 
J 5 HOH   344 1244 535 HOH   HOH B . 
J 5 HOH   345 1245 237 HOH   HOH B . 
J 5 HOH   346 1246 750 HOH   HOH B . 
J 5 HOH   347 1247 692 HOH   HOH B . 
J 5 HOH   348 1248 494 HOH   HOH B . 
J 5 HOH   349 1249 548 HOH   HOH B . 
J 5 HOH   350 1250 201 HOH   HOH B . 
J 5 HOH   351 1251 737 HOH   HOH B . 
J 5 HOH   352 1252 847 HOH   HOH B . 
J 5 HOH   353 1253 663 HOH   HOH B . 
J 5 HOH   354 1254 700 HOH   HOH B . 
J 5 HOH   355 1255 648 HOH   HOH B . 
J 5 HOH   356 1256 617 HOH   HOH B . 
J 5 HOH   357 1257 821 HOH   HOH B . 
J 5 HOH   358 1258 363 HOH   HOH B . 
J 5 HOH   359 1259 657 HOH   HOH B . 
J 5 HOH   360 1260 631 HOH   HOH B . 
J 5 HOH   361 1261 466 HOH   HOH B . 
J 5 HOH   362 1262 544 HOH   HOH B . 
J 5 HOH   363 1263 334 HOH   HOH B . 
J 5 HOH   364 1264 732 HOH   HOH B . 
J 5 HOH   365 1265 390 HOH   HOH B . 
J 5 HOH   366 1266 668 HOH   HOH B . 
J 5 HOH   367 1267 619 HOH   HOH B . 
J 5 HOH   368 1268 603 HOH   HOH B . 
J 5 HOH   369 1269 688 HOH   HOH B . 
J 5 HOH   370 1270 374 HOH   HOH B . 
J 5 HOH   371 1271 670 HOH   HOH B . 
J 5 HOH   372 1272 547 HOH   HOH B . 
J 5 HOH   373 1273 239 HOH   HOH B . 
J 5 HOH   374 1274 515 HOH   HOH B . 
J 5 HOH   375 1275 778 HOH   HOH B . 
J 5 HOH   376 1276 343 HOH   HOH B . 
J 5 HOH   377 1277 352 HOH   HOH B . 
J 5 HOH   378 1278 874 HOH   HOH B . 
J 5 HOH   379 1279 213 HOH   HOH B . 
J 5 HOH   380 1280 636 HOH   HOH B . 
J 5 HOH   381 1281 767 HOH   HOH B . 
J 5 HOH   382 1282 610 HOH   HOH B . 
J 5 HOH   383 1283 282 HOH   HOH B . 
J 5 HOH   384 1284 462 HOH   HOH B . 
J 5 HOH   385 1285 403 HOH   HOH B . 
J 5 HOH   386 1286 484 HOH   HOH B . 
J 5 HOH   387 1287 392 HOH   HOH B . 
J 5 HOH   388 1288 475 HOH   HOH B . 
J 5 HOH   389 1289 261 HOH   HOH B . 
J 5 HOH   390 1290 797 HOH   HOH B . 
J 5 HOH   391 1291 567 HOH   HOH B . 
J 5 HOH   392 1292 895 HOH   HOH B . 
J 5 HOH   393 1293 615 HOH   HOH B . 
J 5 HOH   394 1294 630 HOH   HOH B . 
J 5 HOH   395 1295 754 HOH   HOH B . 
J 5 HOH   396 1296 680 HOH   HOH B . 
J 5 HOH   397 1297 137 HOH   HOH B . 
J 5 HOH   398 1298 538 HOH   HOH B . 
J 5 HOH   399 1299 942 HOH   HOH B . 
J 5 HOH   400 1300 597 HOH   HOH B . 
J 5 HOH   401 1301 664 HOH   HOH B . 
J 5 HOH   402 1302 914 HOH   HOH B . 
J 5 HOH   403 1303 735 HOH   HOH B . 
J 5 HOH   404 1304 694 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 HIS 771 ? CG  ? A HIS 330 CG  
2 1 Y 1 A HIS 771 ? ND1 ? A HIS 330 ND1 
3 1 Y 1 A HIS 771 ? CD2 ? A HIS 330 CD2 
4 1 Y 1 A HIS 771 ? CE1 ? A HIS 330 CE1 
5 1 Y 1 A HIS 771 ? NE2 ? A HIS 330 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20_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                     9EGF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     75.370 
_cell.length_a_esd                 ? 
_cell.length_b                     91.820 
_cell.length_b_esd                 ? 
_cell.length_c                     96.630 
_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                         9EGF 
_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                   9EGF 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.55 
_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    '19% PEG 4K, 0.2M NH4 Acet., 0.1M Na Citrate 58' 
_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         2021-09-23 
_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                                       9EGF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.25 
_reflns.d_resolution_low                               91.82 
_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                                     169926 
_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                           91.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.158 
_reflns.pdbx_Rpim_I_all                                0.062 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1080979 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.144 
_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                                    1.25 
_reflns_shell.d_res_low                                     1.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           22955 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5124 
_reflns_shell.percent_possible_obs                          56.0 
_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                               4.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               2.003 
_reflns_shell.pdbx_Rpim_I_all                               0.924 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.304 
_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                                  1.764 
_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                                 9EGF 
_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                            1.250 
_refine.ls_d_res_low                             66.562 
_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                     169113 
_refine.ls_number_reflns_R_free                  8506 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.40 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2009 
_refine.ls_R_factor_R_free                       0.2206 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1998 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.79 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5575 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             804 
_refine_hist.number_atoms_total               6431 
_refine_hist.d_res_high                       1.250 
_refine_hist.d_res_low                        66.562 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? 5930 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.843 ? 8062 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.697 ? 3424 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.079 ? 866  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1060 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.2500 1.2642 . . 145 3213 55.00  . . . . 0.3778 . . . . . . . . . . . 0.3625 
'X-RAY DIFFRACTION' 1.2642 1.2791 . . 191 3402 59.00  . . . . 0.3612 . . . . . . . . . . . 0.3612 
'X-RAY DIFFRACTION' 1.2791 1.2947 . . 179 3298 57.00  . . . . 0.3791 . . . . . . . . . . . 0.3747 
'X-RAY DIFFRACTION' 1.2947 1.3111 . . 187 3727 64.00  . . . . 0.3747 . . . . . . . . . . . 0.4340 
'X-RAY DIFFRACTION' 1.3111 1.3283 . . 232 4455 77.00  . . . . 0.3166 . . . . . . . . . . . 0.3132 
'X-RAY DIFFRACTION' 1.3283 1.3465 . . 268 4979 85.00  . . . . 0.3114 . . . . . . . . . . . 0.3284 
'X-RAY DIFFRACTION' 1.3465 1.3658 . . 289 5405 94.00  . . . . 0.2896 . . . . . . . . . . . 0.2948 
'X-RAY DIFFRACTION' 1.3658 1.3862 . . 304 5548 96.00  . . . . 0.2865 . . . . . . . . . . . 0.3277 
'X-RAY DIFFRACTION' 1.3862 1.4078 . . 316 5664 98.00  . . . . 0.2672 . . . . . . . . . . . 0.2767 
'X-RAY DIFFRACTION' 1.4078 1.4309 . . 327 5677 98.00  . . . . 0.2503 . . . . . . . . . . . 0.2971 
'X-RAY DIFFRACTION' 1.4309 1.4556 . . 293 5662 97.00  . . . . 0.2534 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 1.4556 1.4820 . . 317 5658 97.00  . . . . 0.2837 . . . . . . . . . . . 0.3035 
'X-RAY DIFFRACTION' 1.4820 1.5106 . . 324 5648 98.00  . . . . 0.2195 . . . . . . . . . . . 0.2413 
'X-RAY DIFFRACTION' 1.5106 1.5414 . . 301 5736 98.00  . . . . 0.2239 . . . . . . . . . . . 0.2694 
'X-RAY DIFFRACTION' 1.5414 1.5749 . . 295 5794 99.00  . . . . 0.2055 . . . . . . . . . . . 0.2225 
'X-RAY DIFFRACTION' 1.5749 1.6115 . . 295 5763 99.00  . . . . 0.2013 . . . . . . . . . . . 0.2173 
'X-RAY DIFFRACTION' 1.6115 1.6518 . . 302 5670 98.00  . . . . 0.1950 . . . . . . . . . . . 0.2334 
'X-RAY DIFFRACTION' 1.6518 1.6965 . . 263 5825 99.00  . . . . 0.1899 . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 1.6965 1.7464 . . 306 5773 99.00  . . . . 0.1915 . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 1.7464 1.8028 . . 292 5834 99.00  . . . . 0.1885 . . . . . . . . . . . 0.2345 
'X-RAY DIFFRACTION' 1.8028 1.8673 . . 289 5806 99.00  . . . . 0.1929 . . . . . . . . . . . 0.2028 
'X-RAY DIFFRACTION' 1.8673 1.9420 . . 260 5270 89.00  . . . . 0.2462 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 1.9420 2.0304 . . 313 5820 99.00  . . . . 0.1856 . . . . . . . . . . . 0.1942 
'X-RAY DIFFRACTION' 2.0304 2.1375 . . 293 5853 99.00  . . . . 0.1772 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 2.1375 2.2714 . . 303 5433 92.00  . . . . 0.1874 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 2.2714 2.4468 . . 290 5853 99.00  . . . . 0.1750 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 2.4468 2.6930 . . 343 5904 100.00 . . . . 0.1786 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 2.6930 3.0827 . . 303 5914 100.00 . . . . 0.1859 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 3.0827 3.8838 . . 342 5889 99.00  . . . . 0.1714 . . . . . . . . . . . 0.1946 
# 
_struct.entry_id                     9EGF 
_struct.title                        
'Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 complexed with TO-589' 
_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        9EGF 
_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 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J 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 9EGF A 1 ? 357 ? A7YT55 290 ? 646 ? 442 798 
2 1 9EGF 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,I 
2 1 B,F,G,H,J 
# 
_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 ? THR A 159 ? ASN A 587 THR A 600 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 175 ? GLU A 183 ? GLY A 616 GLU A 624 1 ? 9  
HELX_P HELX_P11 AB2 GLU A 197 ? ALA A 200 ? GLU A 638 ALA A 641 5 ? 4  
HELX_P HELX_P12 AB3 SER A 205 ? ASN A 209 ? SER A 646 ASN A 650 5 ? 5  
HELX_P HELX_P13 AB4 LEU A 215 ? ARG A 219 ? LEU A 656 ARG A 660 5 ? 5  
HELX_P HELX_P14 AB5 GLY A 233 ? LEU A 244 ? GLY A 674 LEU A 685 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 244 ? ALA A 253 ? LEU A 685 ALA A 694 1 ? 10 
HELX_P HELX_P16 AB7 THR A 277 ? MET A 289 ? THR A 718 MET A 730 1 ? 13 
HELX_P HELX_P17 AB8 SER A 290 ? GLY A 294 ? SER A 731 GLY A 735 5 ? 5  
HELX_P HELX_P18 AB9 ASN A 305 ? LEU A 321 ? ASN A 746 LEU A 762 1 ? 17 
HELX_P HELX_P19 AC1 LYS A 335 ? ALA A 350 ? LYS A 776 ALA A 791 1 ? 16 
HELX_P HELX_P20 AC2 TRP A 353 ? ARG A 357 ? TRP A 794 ARG A 798 5 ? 5  
HELX_P HELX_P21 AC3 GLN B 9   ? HIS B 14  ? GLN B 450 HIS B 455 5 ? 6  
HELX_P HELX_P22 AC4 PRO B 26  ? LEU B 39  ? PRO B 467 LEU B 480 1 ? 14 
HELX_P HELX_P23 AC5 LEU B 41  ? CYS B 45  ? LEU B 482 CYS B 486 5 ? 5  
HELX_P HELX_P24 AC6 THR B 54  ? ALA B 59  ? THR B 495 ALA B 500 1 ? 6  
HELX_P HELX_P25 AC7 SER B 63  ? SER B 73  ? SER B 504 SER B 514 1 ? 11 
HELX_P HELX_P26 AC8 GLU B 74  ? MET B 76  ? GLU B 515 MET B 517 5 ? 3  
HELX_P HELX_P27 AC9 LYS B 77  ? ASP B 86  ? LYS B 518 ASP B 527 1 ? 10 
HELX_P HELX_P28 AD1 GLU B 96  ? THR B 117 ? GLU B 537 THR B 558 1 ? 22 
HELX_P HELX_P29 AD2 ASN B 146 ? ILE B 158 ? ASN B 587 ILE B 599 1 ? 13 
HELX_P HELX_P30 AD3 GLY B 175 ? GLU B 183 ? GLY B 616 GLU B 624 1 ? 9  
HELX_P HELX_P31 AD4 GLU B 197 ? ALA B 200 ? GLU B 638 ALA B 641 5 ? 4  
HELX_P HELX_P32 AD5 SER B 205 ? ASN B 209 ? SER B 646 ASN B 650 5 ? 5  
HELX_P HELX_P33 AD6 LEU B 215 ? ARG B 219 ? LEU B 656 ARG B 660 5 ? 5  
HELX_P HELX_P34 AD7 GLY B 233 ? LEU B 244 ? GLY B 674 LEU B 685 1 ? 12 
HELX_P HELX_P35 AD8 LEU B 244 ? ALA B 253 ? LEU B 685 ALA B 694 1 ? 10 
HELX_P HELX_P36 AD9 THR B 277 ? MET B 289 ? THR B 718 MET B 730 1 ? 13 
HELX_P HELX_P37 AE1 SER B 290 ? GLY B 294 ? SER B 731 GLY B 735 5 ? 5  
HELX_P HELX_P38 AE2 ASN B 305 ? LEU B 321 ? ASN B 746 LEU B 762 1 ? 17 
HELX_P HELX_P39 AE3 LYS B 335 ? ALA B 350 ? LYS B 776 ALA B 791 1 ? 16 
HELX_P HELX_P40 AE4 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   171 OD1 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   612 A ZN  802  1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc2  metalc ? ? A HIS   173 ND1 ? ? ? 1_555 D ZN  . ZN ? ? A HIS   614 A ZN  802  1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc3  metalc ? ? A PHE   182 O   ? ? ? 1_555 E K   . K  ? ? A PHE   623 A K   803  1_555 ? ? ? ? ? ? ? 2.709 ? ? 
metalc4  metalc ? ? A ASP   185 O   ? ? ? 1_555 E K   . K  ? ? A ASP   626 A K   803  1_555 ? ? ? ? ? ? ? 2.862 ? ? 
metalc5  metalc ? ? A VAL   188 O   ? ? ? 1_555 E K   . K  ? ? A VAL   629 A K   803  1_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc6  metalc ? ? A TYR   221 O   ? ? ? 1_555 E K   . K  ? ? A TYR   662 A K   803  1_555 ? ? ? ? ? ? ? 2.851 ? ? 
metalc7  metalc ? ? A ASP   264 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   705 A ZN  802  1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc8  metalc ? ? C A1BH8 .   N03 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH8 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.636 ? ? 
metalc9  metalc ? ? C A1BH8 .   O01 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH8 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc10 metalc ? ? C A1BH8 .   O04 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH8 801 A ZN  802  1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc11 metalc ? ? E K     .   K   ? ? ? 1_555 I HOH . O  ? ? A K     803 A HOH 948  1_555 ? ? ? ? ? ? ? 3.024 ? ? 
metalc12 metalc ? ? E K     .   K   ? ? ? 1_555 I HOH . O  ? ? A K     803 A HOH 998  1_555 ? ? ? ? ? ? ? 2.736 ? ? 
metalc13 metalc ? ? B ASP   171 OD1 ? ? ? 1_555 G ZN  . ZN ? ? B ASP   612 B ZN  802  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc14 metalc ? ? B HIS   173 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS   614 B ZN  802  1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc15 metalc ? ? B PHE   182 O   ? ? ? 1_555 H K   . K  ? ? B PHE   623 B K   803  1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc16 metalc ? ? B ASP   185 O   ? ? ? 1_555 H K   . K  ? ? B ASP   626 B K   803  1_555 ? ? ? ? ? ? ? 2.871 ? ? 
metalc17 metalc ? ? B VAL   188 O   ? ? ? 1_555 H K   . K  ? ? B VAL   629 B K   803  1_555 ? ? ? ? ? ? ? 2.665 ? ? 
metalc18 metalc ? ? B TYR   221 O   ? ? ? 1_555 H K   . K  ? ? B TYR   662 B K   803  1_555 ? ? ? ? ? ? ? 2.851 ? ? 
metalc19 metalc ? ? B ASP   264 OD2 ? ? ? 1_555 G ZN  . ZN ? ? B ASP   705 B ZN  802  1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc20 metalc ? ? F A1BH8 .   N03 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH8 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.669 ? ? 
metalc21 metalc ? ? F A1BH8 .   O01 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH8 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc22 metalc ? ? F A1BH8 .   O04 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH8 801 B ZN  802  1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc23 metalc ? ? H K     .   K   ? ? ? 1_555 J HOH . O  ? ? B K     803 B HOH 975  1_555 ? ? ? ? ? ? ? 2.707 ? ? 
metalc24 metalc ? ? H K     .   K   ? ? ? 1_555 J HOH . O  ? ? B K     803 B HOH 1039 1_555 ? ? ? ? ? ? ? 3.009 ? ? 
# 
_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  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_555 102.5 ? 
2  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_555 103.3 ? 
3  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 98.0  ? 
4  OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 119.8 ? 
5  ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 78.7  ? 
6  OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 136.6 ? 
7  OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 167.0 ? 
8  ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 87.3  ? 
9  OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 83.4  ? 
10 N03 ? C A1BH8 .   ? A A1BH8 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 53.3  ? 
11 OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 91.8  ? 
12 ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 100.0 ? 
13 OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 153.4 ? 
14 N03 ? C A1BH8 .   ? A A1BH8 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 32.1  ? 
15 O01 ? C A1BH8 .   ? A A1BH8 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH8 .   ? A A1BH8 801  ? 1_555 78.0  ? 
16 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A ASP   185 ? A ASP   626  ? 1_555 76.0  ? 
17 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A VAL   188 ? A VAL   629  ? 1_555 118.6 ? 
18 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A VAL   188 ? A VAL   629  ? 1_555 78.8  ? 
19 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 155.1 ? 
20 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 115.3 ? 
21 O   ? A VAL   188 ? A VAL   629 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? A TYR   221 ? A TYR   662  ? 1_555 86.0  ? 
22 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   948  ? 1_555 71.2  ? 
23 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   948  ? 1_555 146.1 ? 
24 O   ? A VAL   188 ? A VAL   629 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   948  ? 1_555 124.5 ? 
25 O   ? A TYR   221 ? A TYR   662 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   948  ? 1_555 92.4  ? 
26 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   998  ? 1_555 79.3  ? 
27 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   998  ? 1_555 85.3  ? 
28 O   ? A VAL   188 ? A VAL   629 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   998  ? 1_555 151.6 ? 
29 O   ? A TYR   221 ? A TYR   662 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   998  ? 1_555 79.7  ? 
30 O   ? I HOH   .   ? A HOH   948 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   998  ? 1_555 80.7  ? 
31 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 ND1 ? B HIS   173 ? B HIS   614  ? 1_555 102.2 ? 
32 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   264 ? B ASP   705  ? 1_555 104.5 ? 
33 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 OD2 ? B ASP   264 ? B ASP   705  ? 1_555 98.0  ? 
34 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 121.6 ? 
35 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 79.4  ? 
36 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 133.5 ? 
37 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 168.9 ? 
38 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 86.1  ? 
39 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 81.4  ? 
40 N03 ? F A1BH8 .   ? B A1BH8 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 52.1  ? 
41 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 95.0  ? 
42 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 101.7 ? 
43 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 148.6 ? 
44 N03 ? F A1BH8 .   ? B A1BH8 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 31.6  ? 
45 O01 ? F A1BH8 .   ? B A1BH8 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH8 .   ? B A1BH8 801  ? 1_555 75.9  ? 
46 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B ASP   185 ? B ASP   626  ? 1_555 74.8  ? 
47 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B VAL   188 ? B VAL   629  ? 1_555 117.8 ? 
48 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B VAL   188 ? B VAL   629  ? 1_555 82.5  ? 
49 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 155.0 ? 
50 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 116.6 ? 
51 O   ? B VAL   188 ? B VAL   629 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? B TYR   221 ? B TYR   662  ? 1_555 86.6  ? 
52 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   975  ? 1_555 81.0  ? 
53 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   975  ? 1_555 84.5  ? 
54 O   ? B VAL   188 ? B VAL   629 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   975  ? 1_555 153.0 ? 
55 O   ? B TYR   221 ? B TYR   662 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   975  ? 1_555 78.3  ? 
56 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   1039 ? 1_555 69.7  ? 
57 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   1039 ? 1_555 143.3 ? 
58 O   ? B VAL   188 ? B VAL   629 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   1039 ? 1_555 122.5 ? 
59 O   ? B TYR   221 ? B TYR   662 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   1039 ? 1_555 93.2  ? 
60 O   ? J HOH   .   ? B HOH   975 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   1039 ? 1_555 81.0  ? 
# 
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 -2.81 
2 PHE 202 A . ? PHE 643 A PRO 203 A ? PRO 644 A 1 10.60 
3 ARG 128 B . ? ARG 569 B PRO 129 B ? PRO 570 B 1 -4.18 
4 PHE 202 B . ? PHE 643 B PRO 203 B ? PRO 644 B 1 7.57  
# 
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   ? TYR B 7   ? THR B 444 TYR B 448 
AA2 3 ASN B 122 ? ILE B 126 ? ASN B 563 ILE B 567 
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 ILE A 299 ? O ILE A 740 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 ASP A 169 ? N ASP A 610 O ILE A 191 ? O ILE A 632 
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 ILE B 299 ? O ILE B 740 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                   9EGF 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    1223 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    1266 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OD2 A ASP 460  ? ? 1_555 NH2 B ARG 660  ? B 2_654 2.05 
2 1 O   A HOH 1151 ? ? 1_555 O   B HOH 1127 ? ? 4_455 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 531 ? ? 62.01   60.39   
2  1 CYS A 581 ? ? -170.14 145.58  
3  1 THR A 600 ? ? -125.86 -91.32  
4  1 TYR A 637 ? ? -121.38 -50.63  
5  1 ASN A 645 ? ? 72.71   33.99   
6  1 LEU A 685 ? ? -123.21 -60.95  
7  1 GLN A 716 ? ? -141.85 35.93   
8  1 GLU A 742 ? ? -111.13 -113.97 
9  1 SER B 531 ? ? 65.15   60.38   
10 1 CYS B 581 ? ? -171.89 142.30  
11 1 THR B 600 ? ? -124.64 -98.46  
12 1 TYR B 637 ? ? -120.20 -50.49  
13 1 ASN B 645 ? ? 70.63   35.21   
14 1 LEU B 685 ? ? -127.83 -61.42  
15 1 GLN B 716 ? ? -143.39 36.32   
16 1 GLU B 742 ? ? -110.47 -112.56 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1300 ? 6.01 . 
2 1 O ? B HOH 1302 ? 6.32 . 
3 1 O ? B HOH 1303 ? 6.54 . 
4 1 O ? B HOH 1304 ? 6.82 . 
# 
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 
A1BH8 C11  C  N N 1   
A1BH8 C12  C  Y N 2   
A1BH8 C13  C  Y N 3   
A1BH8 C14  C  Y N 4   
A1BH8 C02  C  N N 5   
A1BH8 C05  C  Y N 6   
A1BH8 C06  C  Y N 7   
A1BH8 C07  C  Y N 8   
A1BH8 C08  C  Y N 9   
A1BH8 C09  C  N N 10  
A1BH8 C15  C  Y N 11  
A1BH8 C17  C  Y N 12  
A1BH8 C20  C  N N 13  
A1BH8 C21  C  N N 14  
A1BH8 C23  C  Y N 15  
A1BH8 C24  C  Y N 16  
A1BH8 N03  N  N N 17  
A1BH8 N10  N  N N 18  
A1BH8 N16  N  Y N 19  
A1BH8 O01  O  N N 20  
A1BH8 O04  O  N N 21  
A1BH8 O19  O  N N 22  
A1BH8 O22  O  N N 23  
A1BH8 S18  S  N N 24  
A1BH8 H1   H  N N 25  
A1BH8 H2   H  N N 26  
A1BH8 H3   H  N N 27  
A1BH8 H4   H  N N 28  
A1BH8 H5   H  N N 29  
A1BH8 H6   H  N N 30  
A1BH8 H7   H  N N 31  
A1BH8 H8   H  N N 32  
A1BH8 H9   H  N N 33  
A1BH8 H10  H  N N 34  
A1BH8 H11  H  N N 35  
A1BH8 H12  H  N N 36  
A1BH8 H13  H  N N 37  
A1BH8 H14  H  N N 38  
A1BH8 H15  H  N N 39  
A1BH8 H16  H  N N 40  
A1BH8 H17  H  N N 41  
A1BH8 H18  H  N N 42  
A1BH8 H19  H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
GLN   N    N  N N 131 
GLN   CA   C  N S 132 
GLN   C    C  N N 133 
GLN   O    O  N N 134 
GLN   CB   C  N N 135 
GLN   CG   C  N N 136 
GLN   CD   C  N N 137 
GLN   OE1  O  N N 138 
GLN   NE2  N  N N 139 
GLN   OXT  O  N N 140 
GLN   H    H  N N 141 
GLN   H2   H  N N 142 
GLN   HA   H  N N 143 
GLN   HB2  H  N N 144 
GLN   HB3  H  N N 145 
GLN   HG2  H  N N 146 
GLN   HG3  H  N N 147 
GLN   HE21 H  N N 148 
GLN   HE22 H  N N 149 
GLN   HXT  H  N N 150 
GLU   N    N  N N 151 
GLU   CA   C  N S 152 
GLU   C    C  N N 153 
GLU   O    O  N N 154 
GLU   CB   C  N N 155 
GLU   CG   C  N N 156 
GLU   CD   C  N N 157 
GLU   OE1  O  N N 158 
GLU   OE2  O  N N 159 
GLU   OXT  O  N N 160 
GLU   H    H  N N 161 
GLU   H2   H  N N 162 
GLU   HA   H  N N 163 
GLU   HB2  H  N N 164 
GLU   HB3  H  N N 165 
GLU   HG2  H  N N 166 
GLU   HG3  H  N N 167 
GLU   HE2  H  N N 168 
GLU   HXT  H  N N 169 
GLY   N    N  N N 170 
GLY   CA   C  N N 171 
GLY   C    C  N N 172 
GLY   O    O  N N 173 
GLY   OXT  O  N N 174 
GLY   H    H  N N 175 
GLY   H2   H  N N 176 
GLY   HA2  H  N N 177 
GLY   HA3  H  N N 178 
GLY   HXT  H  N N 179 
HIS   N    N  N N 180 
HIS   CA   C  N S 181 
HIS   C    C  N N 182 
HIS   O    O  N N 183 
HIS   CB   C  N N 184 
HIS   CG   C  Y N 185 
HIS   ND1  N  Y N 186 
HIS   CD2  C  Y N 187 
HIS   CE1  C  Y N 188 
HIS   NE2  N  Y N 189 
HIS   OXT  O  N N 190 
HIS   H    H  N N 191 
HIS   H2   H  N N 192 
HIS   HA   H  N N 193 
HIS   HB2  H  N N 194 
HIS   HB3  H  N N 195 
HIS   HD1  H  N N 196 
HIS   HD2  H  N N 197 
HIS   HE1  H  N N 198 
HIS   HE2  H  N N 199 
HIS   HXT  H  N N 200 
HOH   O    O  N N 201 
HOH   H1   H  N N 202 
HOH   H2   H  N N 203 
ILE   N    N  N N 204 
ILE   CA   C  N S 205 
ILE   C    C  N N 206 
ILE   O    O  N N 207 
ILE   CB   C  N S 208 
ILE   CG1  C  N N 209 
ILE   CG2  C  N N 210 
ILE   CD1  C  N N 211 
ILE   OXT  O  N N 212 
ILE   H    H  N N 213 
ILE   H2   H  N N 214 
ILE   HA   H  N N 215 
ILE   HB   H  N N 216 
ILE   HG12 H  N N 217 
ILE   HG13 H  N N 218 
ILE   HG21 H  N N 219 
ILE   HG22 H  N N 220 
ILE   HG23 H  N N 221 
ILE   HD11 H  N N 222 
ILE   HD12 H  N N 223 
ILE   HD13 H  N N 224 
ILE   HXT  H  N N 225 
K     K    K  N N 226 
LEU   N    N  N N 227 
LEU   CA   C  N S 228 
LEU   C    C  N N 229 
LEU   O    O  N N 230 
LEU   CB   C  N N 231 
LEU   CG   C  N N 232 
LEU   CD1  C  N N 233 
LEU   CD2  C  N N 234 
LEU   OXT  O  N N 235 
LEU   H    H  N N 236 
LEU   H2   H  N N 237 
LEU   HA   H  N N 238 
LEU   HB2  H  N N 239 
LEU   HB3  H  N N 240 
LEU   HG   H  N N 241 
LEU   HD11 H  N N 242 
LEU   HD12 H  N N 243 
LEU   HD13 H  N N 244 
LEU   HD21 H  N N 245 
LEU   HD22 H  N N 246 
LEU   HD23 H  N N 247 
LEU   HXT  H  N N 248 
LYS   N    N  N N 249 
LYS   CA   C  N S 250 
LYS   C    C  N N 251 
LYS   O    O  N N 252 
LYS   CB   C  N N 253 
LYS   CG   C  N N 254 
LYS   CD   C  N N 255 
LYS   CE   C  N N 256 
LYS   NZ   N  N N 257 
LYS   OXT  O  N N 258 
LYS   H    H  N N 259 
LYS   H2   H  N N 260 
LYS   HA   H  N N 261 
LYS   HB2  H  N N 262 
LYS   HB3  H  N N 263 
LYS   HG2  H  N N 264 
LYS   HG3  H  N N 265 
LYS   HD2  H  N N 266 
LYS   HD3  H  N N 267 
LYS   HE2  H  N N 268 
LYS   HE3  H  N N 269 
LYS   HZ1  H  N N 270 
LYS   HZ2  H  N N 271 
LYS   HZ3  H  N N 272 
LYS   HXT  H  N N 273 
MET   N    N  N N 274 
MET   CA   C  N S 275 
MET   C    C  N N 276 
MET   O    O  N N 277 
MET   CB   C  N N 278 
MET   CG   C  N N 279 
MET   SD   S  N N 280 
MET   CE   C  N N 281 
MET   OXT  O  N N 282 
MET   H    H  N N 283 
MET   H2   H  N N 284 
MET   HA   H  N N 285 
MET   HB2  H  N N 286 
MET   HB3  H  N N 287 
MET   HG2  H  N N 288 
MET   HG3  H  N N 289 
MET   HE1  H  N N 290 
MET   HE2  H  N N 291 
MET   HE3  H  N N 292 
MET   HXT  H  N N 293 
PHE   N    N  N N 294 
PHE   CA   C  N S 295 
PHE   C    C  N N 296 
PHE   O    O  N N 297 
PHE   CB   C  N N 298 
PHE   CG   C  Y N 299 
PHE   CD1  C  Y N 300 
PHE   CD2  C  Y N 301 
PHE   CE1  C  Y N 302 
PHE   CE2  C  Y N 303 
PHE   CZ   C  Y N 304 
PHE   OXT  O  N N 305 
PHE   H    H  N N 306 
PHE   H2   H  N N 307 
PHE   HA   H  N N 308 
PHE   HB2  H  N N 309 
PHE   HB3  H  N N 310 
PHE   HD1  H  N N 311 
PHE   HD2  H  N N 312 
PHE   HE1  H  N N 313 
PHE   HE2  H  N N 314 
PHE   HZ   H  N N 315 
PHE   HXT  H  N N 316 
PRO   N    N  N N 317 
PRO   CA   C  N S 318 
PRO   C    C  N N 319 
PRO   O    O  N N 320 
PRO   CB   C  N N 321 
PRO   CG   C  N N 322 
PRO   CD   C  N N 323 
PRO   OXT  O  N N 324 
PRO   H    H  N N 325 
PRO   HA   H  N N 326 
PRO   HB2  H  N N 327 
PRO   HB3  H  N N 328 
PRO   HG2  H  N N 329 
PRO   HG3  H  N N 330 
PRO   HD2  H  N N 331 
PRO   HD3  H  N N 332 
PRO   HXT  H  N N 333 
SER   N    N  N N 334 
SER   CA   C  N S 335 
SER   C    C  N N 336 
SER   O    O  N N 337 
SER   CB   C  N N 338 
SER   OG   O  N N 339 
SER   OXT  O  N N 340 
SER   H    H  N N 341 
SER   H2   H  N N 342 
SER   HA   H  N N 343 
SER   HB2  H  N N 344 
SER   HB3  H  N N 345 
SER   HG   H  N N 346 
SER   HXT  H  N N 347 
THR   N    N  N N 348 
THR   CA   C  N S 349 
THR   C    C  N N 350 
THR   O    O  N N 351 
THR   CB   C  N R 352 
THR   OG1  O  N N 353 
THR   CG2  C  N N 354 
THR   OXT  O  N N 355 
THR   H    H  N N 356 
THR   H2   H  N N 357 
THR   HA   H  N N 358 
THR   HB   H  N N 359 
THR   HG1  H  N N 360 
THR   HG21 H  N N 361 
THR   HG22 H  N N 362 
THR   HG23 H  N N 363 
THR   HXT  H  N N 364 
TRP   N    N  N N 365 
TRP   CA   C  N S 366 
TRP   C    C  N N 367 
TRP   O    O  N N 368 
TRP   CB   C  N N 369 
TRP   CG   C  Y N 370 
TRP   CD1  C  Y N 371 
TRP   CD2  C  Y N 372 
TRP   NE1  N  Y N 373 
TRP   CE2  C  Y N 374 
TRP   CE3  C  Y N 375 
TRP   CZ2  C  Y N 376 
TRP   CZ3  C  Y N 377 
TRP   CH2  C  Y N 378 
TRP   OXT  O  N N 379 
TRP   H    H  N N 380 
TRP   H2   H  N N 381 
TRP   HA   H  N N 382 
TRP   HB2  H  N N 383 
TRP   HB3  H  N N 384 
TRP   HD1  H  N N 385 
TRP   HE1  H  N N 386 
TRP   HE3  H  N N 387 
TRP   HZ2  H  N N 388 
TRP   HZ3  H  N N 389 
TRP   HH2  H  N N 390 
TRP   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
ZN    ZN   ZN N N 435 
# 
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 
A1BH8 C13 C14  doub Y N 1   
A1BH8 C13 C12  sing Y N 2   
A1BH8 C11 C12  sing N N 3   
A1BH8 C11 N10  sing N N 4   
A1BH8 C14 C15  sing Y N 5   
A1BH8 C20 C21  sing N N 6   
A1BH8 C20 S18  sing N N 7   
A1BH8 C12 C17  doub Y N 8   
A1BH8 N10 S18  sing N N 9   
A1BH8 N10 C09  sing N N 10  
A1BH8 C15 N16  doub Y N 11  
A1BH8 C17 N16  sing Y N 12  
A1BH8 O19 S18  doub N N 13  
A1BH8 S18 O22  doub N N 14  
A1BH8 C09 C08  sing N N 15  
A1BH8 C23 C08  doub Y N 16  
A1BH8 C23 C24  sing Y N 17  
A1BH8 C08 C07  sing Y N 18  
A1BH8 C24 C05  doub Y N 19  
A1BH8 C07 C06  doub Y N 20  
A1BH8 C05 C06  sing Y N 21  
A1BH8 C05 C02  sing N N 22  
A1BH8 N03 C02  sing N N 23  
A1BH8 N03 O04  sing N N 24  
A1BH8 C02 O01  doub N N 25  
A1BH8 C11 H1   sing N N 26  
A1BH8 C11 H2   sing N N 27  
A1BH8 C13 H3   sing N N 28  
A1BH8 C14 H4   sing N N 29  
A1BH8 C06 H5   sing N N 30  
A1BH8 C07 H6   sing N N 31  
A1BH8 C09 H7   sing N N 32  
A1BH8 C09 H8   sing N N 33  
A1BH8 C15 H9   sing N N 34  
A1BH8 C17 H10  sing N N 35  
A1BH8 C20 H11  sing N N 36  
A1BH8 C20 H12  sing N N 37  
A1BH8 C21 H13  sing N N 38  
A1BH8 C21 H14  sing N N 39  
A1BH8 C21 H15  sing N N 40  
A1BH8 C23 H16  sing N N 41  
A1BH8 C24 H17  sing N N 42  
A1BH8 N03 H18  sing N N 43  
A1BH8 O04 H19  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
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                    9EGF 
_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]   0.013268 
_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]   0.010891 
_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]   0.010349 
_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   ? 10.533 5.196   21.016  1.00 36.88 ?  442  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 1   ? 10.699 4.432   19.775  1.00 35.53 ?  442  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 1   ? 11.833 3.413   19.867  1.00 33.79 ?  442  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 1   ? 12.847 3.663   20.518  1.00 34.52 ?  442  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 1   ? 11.034 5.514   18.743  1.00 36.07 ?  442  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 1   ? 11.663 6.599   19.531  1.00 37.69 ?  442  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 1   ? 10.977 6.593   20.870  1.00 37.76 ?  442  PRO   A CD  1 
ATOM   8    N  N   . ILE   A 1 2   ? 11.651 2.274   19.203  1.00 30.24 ?  443  ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 2   ? 12.594 1.163   19.234  1.00 25.62 ?  443  ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 2   ? 13.160 0.976   17.830  1.00 19.71 ?  443  ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 2   ? 12.415 1.007   16.844  1.00 18.51 ?  443  ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 2   ? 11.903 -0.126  19.717  1.00 26.07 ?  443  ILE   A CB  1 
ATOM   13   C  CG1 . ILE   A 1 2   ? 11.403 0.052   21.152  1.00 28.68 ?  443  ILE   A CG1 1 
ATOM   14   C  CG2 . ILE   A 1 2   ? 12.836 -1.320  19.600  1.00 24.82 ?  443  ILE   A CG2 1 
ATOM   15   C  CD1 . ILE   A 1 2   ? 10.594 -1.115  21.680  1.00 30.54 ?  443  ILE   A CD1 1 
ATOM   16   N  N   . THR   A 1 3   ? 14.477 0.807   17.738  1.00 15.42 ?  444  THR   A N   1 
ATOM   17   C  CA  . THR   A 1 3   ? 15.145 0.513   16.477  1.00 13.90 ?  444  THR   A CA  1 
ATOM   18   C  C   . THR   A 1 3   ? 15.603 -0.938  16.471  1.00 13.08 ?  444  THR   A C   1 
ATOM   19   O  O   . THR   A 1 3   ? 16.330 -1.371  17.371  1.00 15.01 ?  444  THR   A O   1 
ATOM   20   C  CB  . THR   A 1 3   ? 16.347 1.433   16.266  1.00 14.90 ?  444  THR   A CB  1 
ATOM   21   O  OG1 . THR   A 1 3   ? 15.897 2.787   16.165  1.00 14.82 ?  444  THR   A OG1 1 
ATOM   22   C  CG2 . THR   A 1 3   ? 17.110 1.054   14.987  1.00 14.25 ?  444  THR   A CG2 1 
ATOM   23   N  N   . GLY   A 1 4   ? 15.182 -1.685  15.446  1.00 11.96 ?  445  GLY   A N   1 
ATOM   24   C  CA  . GLY   A 1 4   ? 15.643 -3.045  15.299  1.00 14.04 ?  445  GLY   A CA  1 
ATOM   25   C  C   . GLY   A 1 4   ? 16.963 -3.117  14.551  1.00 11.37 ?  445  GLY   A C   1 
ATOM   26   O  O   . GLY   A 1 4   ? 17.307 -2.247  13.744  1.00 13.13 ?  445  GLY   A O   1 
ATOM   27   N  N   . LEU   A 1 5   ? 17.711 -4.181  14.822  1.00 11.39 ?  446  LEU   A N   1 
ATOM   28   C  CA  . LEU   A 1 5   ? 18.962 -4.434  14.121  1.00 11.13 ?  446  LEU   A CA  1 
ATOM   29   C  C   . LEU   A 1 5   ? 19.071 -5.927  13.870  1.00 11.43 ?  446  LEU   A C   1 
ATOM   30   O  O   . LEU   A 1 5   ? 18.919 -6.730  14.797  1.00 13.56 ?  446  LEU   A O   1 
ATOM   31   C  CB  . LEU   A 1 5   ? 20.170 -3.942  14.937  1.00 11.89 ?  446  LEU   A CB  1 
ATOM   32   C  CG  . LEU   A 1 5   ? 21.557 -4.098  14.292  1.00 12.58 ?  446  LEU   A CG  1 
ATOM   33   C  CD1 . LEU   A 1 5   ? 22.454 -2.938  14.707  1.00 12.26 ?  446  LEU   A CD1 1 
ATOM   34   C  CD2 . LEU   A 1 5   ? 22.205 -5.440  14.634  1.00 13.11 ?  446  LEU   A CD2 1 
ATOM   35   N  N   . VAL   A 1 6   ? 19.314 -6.300  12.615  1.00 10.34 ?  447  VAL   A N   1 
ATOM   36   C  CA  . VAL   A 1 6   ? 19.578 -7.689  12.267  1.00 12.27 ?  447  VAL   A CA  1 
ATOM   37   C  C   . VAL   A 1 6   ? 21.005 -7.839  11.736  1.00 12.13 ?  447  VAL   A C   1 
ATOM   38   O  O   . VAL   A 1 6   ? 21.441 -7.092  10.849  1.00 12.98 ?  447  VAL   A O   1 
ATOM   39   C  CB  . VAL   A 1 6   ? 18.505 -8.288  11.331  1.00 12.38 ?  447  VAL   A CB  1 
ATOM   40   C  CG1 . VAL   A 1 6   ? 18.356 -7.480  10.057  1.00 13.52 ?  447  VAL   A CG1 1 
ATOM   41   C  CG2 . VAL   A 1 6   ? 18.835 -9.739  11.011  1.00 14.99 ?  447  VAL   A CG2 1 
ATOM   42   N  N   . TYR   A 1 7   ? 21.736 -8.796  12.302  1.00 12.04 ?  448  TYR   A N   1 
ATOM   43   C  CA  . TYR   A 1 7   ? 23.061 -9.193  11.856  1.00 13.20 ?  448  TYR   A CA  1 
ATOM   44   C  C   . TYR   A 1 7   ? 23.243 -10.642 12.262  1.00 13.06 ?  448  TYR   A C   1 
ATOM   45   O  O   . TYR   A 1 7   ? 22.977 -11.009 13.411  1.00 13.67 ?  448  TYR   A O   1 
ATOM   46   C  CB  . TYR   A 1 7   ? 24.173 -8.346  12.495  1.00 12.49 ?  448  TYR   A CB  1 
ATOM   47   C  CG  . TYR   A 1 7   ? 25.558 -8.937  12.269  1.00 13.12 ?  448  TYR   A CG  1 
ATOM   48   C  CD1 . TYR   A 1 7   ? 26.194 -8.811  11.038  1.00 11.27 ?  448  TYR   A CD1 1 
ATOM   49   C  CD2 . TYR   A 1 7   ? 26.220 -9.637  13.273  1.00 12.62 ?  448  TYR   A CD2 1 
ATOM   50   C  CE1 . TYR   A 1 7   ? 27.434 -9.363  10.820  1.00 13.54 ?  448  TYR   A CE1 1 
ATOM   51   C  CE2 . TYR   A 1 7   ? 27.468 -10.185 13.062  1.00 12.86 ?  448  TYR   A CE2 1 
ATOM   52   C  CZ  . TYR   A 1 7   ? 28.076 -10.044 11.825  1.00 12.63 ?  448  TYR   A CZ  1 
ATOM   53   O  OH  . TYR   A 1 7   ? 29.319 -10.575 11.579  1.00 15.84 ?  448  TYR   A OH  1 
ATOM   54   N  N   . ASP   A 1 8   ? 23.698 -11.465 11.327  1.00 12.52 ?  449  ASP   A N   1 
ATOM   55   C  CA  . ASP   A 1 8   ? 24.001 -12.860 11.619  1.00 13.22 ?  449  ASP   A CA  1 
ATOM   56   C  C   . ASP   A 1 8   ? 25.299 -13.208 10.916  1.00 12.19 ?  449  ASP   A C   1 
ATOM   57   O  O   . ASP   A 1 8   ? 25.388 -13.080 9.688   1.00 13.24 ?  449  ASP   A O   1 
ATOM   58   C  CB  . ASP   A 1 8   ? 22.864 -13.769 11.145  1.00 13.73 ?  449  ASP   A CB  1 
ATOM   59   C  CG  . ASP   A 1 8   ? 22.971 -15.183 11.683  1.00 16.91 ?  449  ASP   A CG  1 
ATOM   60   O  OD1 . ASP   A 1 8   ? 24.044 -15.803 11.547  1.00 16.86 ?  449  ASP   A OD1 1 
ATOM   61   O  OD2 . ASP   A 1 8   ? 21.967 -15.680 12.250  1.00 19.78 -1 449  ASP   A OD2 1 
ATOM   62   N  N   A GLN   A 1 9   ? 26.304 -13.637 11.684  0.53 12.81 ?  450  GLN   A N   1 
ATOM   63   N  N   B GLN   A 1 9   ? 26.281 -13.676 11.696  0.47 12.91 ?  450  GLN   A N   1 
ATOM   64   C  CA  A GLN   A 1 9   ? 27.624 -13.906 11.124  0.53 14.54 ?  450  GLN   A CA  1 
ATOM   65   C  CA  B GLN   A 1 9   ? 27.595 -14.034 11.172  0.47 13.82 ?  450  GLN   A CA  1 
ATOM   66   C  C   A GLN   A 1 9   ? 27.626 -15.036 10.104  0.53 13.65 ?  450  GLN   A C   1 
ATOM   67   C  C   B GLN   A 1 9   ? 27.524 -15.075 10.063  0.47 13.90 ?  450  GLN   A C   1 
ATOM   68   O  O   A GLN   A 1 9   ? 28.613 -15.183 9.377   0.53 11.66 ?  450  GLN   A O   1 
ATOM   69   O  O   B GLN   A 1 9   ? 28.438 -15.140 9.237   0.47 12.78 ?  450  GLN   A O   1 
ATOM   70   C  CB  A GLN   A 1 9   ? 28.634 -14.200 12.239  0.53 18.03 ?  450  GLN   A CB  1 
ATOM   71   C  CB  B GLN   A 1 9   ? 28.484 -14.547 12.316  0.47 14.36 ?  450  GLN   A CB  1 
ATOM   72   C  CG  A GLN   A 1 9   ? 28.321 -15.436 13.054  0.53 21.84 ?  450  GLN   A CG  1 
ATOM   73   C  CG  B GLN   A 1 9   ? 29.949 -14.756 11.947  0.47 14.49 ?  450  GLN   A CG  1 
ATOM   74   C  CD  A GLN   A 1 9   ? 29.382 -15.724 14.101  0.53 27.20 ?  450  GLN   A CD  1 
ATOM   75   C  CD  B GLN   A 1 9   ? 30.225 -16.138 11.392  0.47 14.95 ?  450  GLN   A CD  1 
ATOM   76   O  OE1 A GLN   A 1 9   ? 29.963 -14.807 14.687  0.53 29.14 ?  450  GLN   A OE1 1 
ATOM   77   O  OE1 B GLN   A 1 9   ? 29.512 -17.093 11.700  0.47 16.05 ?  450  GLN   A OE1 1 
ATOM   78   N  NE2 A GLN   A 1 9   ? 29.642 -17.005 14.341  0.53 28.83 ?  450  GLN   A NE2 1 
ATOM   79   N  NE2 B GLN   A 1 9   ? 31.248 -16.247 10.550  0.47 14.77 ?  450  GLN   A NE2 1 
ATOM   80   N  N   A ARG   A 1 10  ? 26.560 -15.836 10.028  0.53 13.18 ?  451  ARG   A N   1 
ATOM   81   N  N   B ARG   A 1 10  ? 26.467 -15.889 10.020  0.47 13.58 ?  451  ARG   A N   1 
ATOM   82   C  CA  A ARG   A 1 10  ? 26.499 -16.876 9.004   0.53 13.13 ?  451  ARG   A CA  1 
ATOM   83   C  CA  B ARG   A 1 10  ? 26.371 -16.920 8.989   0.47 13.74 ?  451  ARG   A CA  1 
ATOM   84   C  C   A ARG   A 1 10  ? 26.561 -16.287 7.599   0.53 12.15 ?  451  ARG   A C   1 
ATOM   85   C  C   B ARG   A 1 10  ? 26.377 -16.344 7.577   0.47 12.97 ?  451  ARG   A C   1 
ATOM   86   O  O   A ARG   A 1 10  ? 27.050 -16.946 6.672   0.53 11.50 ?  451  ARG   A O   1 
ATOM   87   O  O   B ARG   A 1 10  ? 26.654 -17.081 6.623   0.47 13.22 ?  451  ARG   A O   1 
ATOM   88   C  CB  A ARG   A 1 10  ? 25.229 -17.708 9.179   0.53 14.03 ?  451  ARG   A CB  1 
ATOM   89   C  CB  B ARG   A 1 10  ? 25.124 -17.778 9.207   0.47 14.97 ?  451  ARG   A CB  1 
ATOM   90   C  CG  A ARG   A 1 10  ? 25.286 -18.701 10.333  0.53 15.09 ?  451  ARG   A CG  1 
ATOM   91   C  CG  B ARG   A 1 10  ? 25.259 -18.784 10.340  0.47 16.16 ?  451  ARG   A CG  1 
ATOM   92   C  CD  A ARG   A 1 10  ? 23.969 -19.455 10.459  0.53 16.70 ?  451  ARG   A CD  1 
ATOM   93   C  CD  B ARG   A 1 10  ? 23.893 -19.284 10.775  0.47 17.81 ?  451  ARG   A CD  1 
ATOM   94   N  NE  A ARG   A 1 10  ? 22.854 -18.558 10.753  0.53 18.90 ?  451  ARG   A NE  1 
ATOM   95   N  NE  B ARG   A 1 10  ? 23.106 -19.760 9.641   0.47 20.61 ?  451  ARG   A NE  1 
ATOM   96   C  CZ  A ARG   A 1 10  ? 21.571 -18.879 10.615  0.53 18.83 ?  451  ARG   A CZ  1 
ATOM   97   C  CZ  B ARG   A 1 10  ? 22.613 -20.988 9.528   0.47 22.99 ?  451  ARG   A CZ  1 
ATOM   98   N  NH1 A ARG   A 1 10  ? 21.226 -20.086 10.184  0.53 14.39 ?  451  ARG   A NH1 1 
ATOM   99   N  NH1 B ARG   A 1 10  ? 22.828 -21.882 10.485  0.47 26.12 ?  451  ARG   A NH1 1 
ATOM   100  N  NH2 A ARG   A 1 10  ? 20.633 -17.991 10.913  0.53 20.86 ?  451  ARG   A NH2 1 
ATOM   101  N  NH2 B ARG   A 1 10  ? 21.910 -21.328 8.453   0.47 22.29 ?  451  ARG   A NH2 1 
ATOM   102  N  N   . MET   A 1 11  ? 26.081 -15.051 7.417   1.00 10.96 ?  452  MET   A N   1 
ATOM   103  C  CA  . MET   A 1 11  ? 26.140 -14.426 6.098   1.00 12.59 ?  452  MET   A CA  1 
ATOM   104  C  C   . MET   A 1 11  ? 27.568 -14.145 5.653   1.00 13.24 ?  452  MET   A C   1 
ATOM   105  O  O   . MET   A 1 11  ? 27.775 -13.798 4.491   1.00 12.79 ?  452  MET   A O   1 
ATOM   106  C  CB  . MET   A 1 11  ? 25.282 -13.160 6.047   1.00 12.14 ?  452  MET   A CB  1 
ATOM   107  C  CG  . MET   A 1 11  ? 23.803 -13.425 5.829   1.00 11.93 ?  452  MET   A CG  1 
ATOM   108  S  SD  . MET   A 1 11  ? 22.748 -11.965 5.998   1.00 12.38 ?  452  MET   A SD  1 
ATOM   109  C  CE  . MET   A 1 11  ? 22.783 -11.659 7.767   1.00 15.86 ?  452  MET   A CE  1 
ATOM   110  N  N   . MET   A 1 12  ? 28.554 -14.299 6.542   1.00 13.03 ?  453  MET   A N   1 
ATOM   111  C  CA  . MET   A 1 12  ? 29.952 -14.216 6.145   1.00 12.39 ?  453  MET   A CA  1 
ATOM   112  C  C   . MET   A 1 12  ? 30.411 -15.427 5.351   1.00 11.91 ?  453  MET   A C   1 
ATOM   113  O  O   . MET   A 1 12  ? 31.477 -15.367 4.734   1.00 13.32 ?  453  MET   A O   1 
ATOM   114  C  CB  . MET   A 1 12  ? 30.845 -14.061 7.378   1.00 13.94 ?  453  MET   A CB  1 
ATOM   115  C  CG  . MET   A 1 12  ? 30.643 -12.763 8.146   1.00 13.45 ?  453  MET   A CG  1 
ATOM   116  S  SD  . MET   A 1 12  ? 31.811 -12.560 9.522   1.00 16.73 ?  453  MET   A SD  1 
ATOM   117  C  CE  . MET   A 1 12  ? 33.383 -12.490 8.659   1.00 16.01 ?  453  MET   A CE  1 
ATOM   118  N  N   . LEU   A 1 13  ? 29.639 -16.521 5.341   1.00 12.09 ?  454  LEU   A N   1 
ATOM   119  C  CA  . LEU   A 1 13  ? 30.143 -17.766 4.757   1.00 14.00 ?  454  LEU   A CA  1 
ATOM   120  C  C   . LEU   A 1 13  ? 30.235 -17.706 3.235   1.00 14.01 ?  454  LEU   A C   1 
ATOM   121  O  O   . LEU   A 1 13  ? 31.051 -18.417 2.643   1.00 14.81 ?  454  LEU   A O   1 
ATOM   122  C  CB  . LEU   A 1 13  ? 29.304 -18.962 5.211   1.00 15.32 ?  454  LEU   A CB  1 
ATOM   123  C  CG  . LEU   A 1 13  ? 29.396 -19.274 6.711   1.00 15.58 ?  454  LEU   A CG  1 
ATOM   124  C  CD1 . LEU   A 1 13  ? 28.484 -20.438 7.074   1.00 16.46 ?  454  LEU   A CD1 1 
ATOM   125  C  CD2 . LEU   A 1 13  ? 30.836 -19.548 7.137   1.00 18.41 ?  454  LEU   A CD2 1 
ATOM   126  N  N   . HIS   A 1 14  ? 29.411 -16.886 2.595   1.00 12.62 ?  455  HIS   A N   1 
ATOM   127  C  CA  . HIS   A 1 14  ? 29.533 -16.611 1.167   1.00 10.95 ?  455  HIS   A CA  1 
ATOM   128  C  C   . HIS   A 1 14  ? 30.868 -15.933 0.888   1.00 11.09 ?  455  HIS   A C   1 
ATOM   129  O  O   . HIS   A 1 14  ? 31.151 -14.863 1.428   1.00 12.38 ?  455  HIS   A O   1 
ATOM   130  C  CB  . HIS   A 1 14  ? 28.374 -15.688 0.790   1.00 10.82 ?  455  HIS   A CB  1 
ATOM   131  C  CG  . HIS   A 1 14  ? 28.501 -15.043 -0.559  1.00 11.24 ?  455  HIS   A CG  1 
ATOM   132  N  ND1 . HIS   A 1 14  ? 28.561 -15.763 -1.735  1.00 11.45 ?  455  HIS   A ND1 1 
ATOM   133  C  CD2 . HIS   A 1 14  ? 28.529 -13.738 -0.916  1.00 12.12 ?  455  HIS   A CD2 1 
ATOM   134  C  CE1 . HIS   A 1 14  ? 28.630 -14.927 -2.757  1.00 11.11 ?  455  HIS   A CE1 1 
ATOM   135  N  NE2 . HIS   A 1 14  ? 28.614 -13.691 -2.284  1.00 10.88 ?  455  HIS   A NE2 1 
ATOM   136  N  N   . HIS   A 1 15  ? 31.711 -16.557 0.067   1.00 13.22 ?  456  HIS   A N   1 
ATOM   137  C  CA  . HIS   A 1 15  ? 33.042 -16.003 -0.152  1.00 12.56 ?  456  HIS   A CA  1 
ATOM   138  C  C   . HIS   A 1 15  ? 33.556 -16.379 -1.537  1.00 13.46 ?  456  HIS   A C   1 
ATOM   139  O  O   . HIS   A 1 15  ? 33.035 -17.277 -2.190  1.00 13.67 ?  456  HIS   A O   1 
ATOM   140  C  CB  . HIS   A 1 15  ? 34.011 -16.466 0.939   1.00 13.02 ?  456  HIS   A CB  1 
ATOM   141  C  CG  . HIS   A 1 15  ? 34.357 -17.919 0.845   1.00 15.89 ?  456  HIS   A CG  1 
ATOM   142  N  ND1 . HIS   A 1 15  ? 33.464 -18.914 1.172   1.00 17.47 ?  456  HIS   A ND1 1 
ATOM   143  C  CD2 . HIS   A 1 15  ? 35.490 -18.545 0.437   1.00 16.94 ?  456  HIS   A CD2 1 
ATOM   144  C  CE1 . HIS   A 1 15  ? 34.032 -20.093 0.979   1.00 19.26 ?  456  HIS   A CE1 1 
ATOM   145  N  NE2 . HIS   A 1 15  ? 35.260 -19.896 0.534   1.00 18.83 ?  456  HIS   A NE2 1 
ATOM   146  N  N   . ASN   A 1 16  ? 34.618 -15.688 -1.954  1.00 13.08 ?  457  ASN   A N   1 
ATOM   147  C  CA  . ASN   A 1 16  ? 35.273 -15.913 -3.239  1.00 13.71 ?  457  ASN   A CA  1 
ATOM   148  C  C   . ASN   A 1 16  ? 36.483 -16.808 -2.986  1.00 14.73 ?  457  ASN   A C   1 
ATOM   149  O  O   . ASN   A 1 16  ? 37.493 -16.359 -2.430  1.00 15.97 ?  457  ASN   A O   1 
ATOM   150  C  CB  . ASN   A 1 16  ? 35.693 -14.572 -3.836  1.00 12.91 ?  457  ASN   A CB  1 
ATOM   151  C  CG  . ASN   A 1 16  ? 36.177 -14.698 -5.263  1.00 15.32 ?  457  ASN   A CG  1 
ATOM   152  O  OD1 . ASN   A 1 16  ? 36.952 -15.597 -5.570  1.00 15.61 ?  457  ASN   A OD1 1 
ATOM   153  N  ND2 . ASN   A 1 16  ? 35.714 -13.808 -6.141  1.00 13.57 ?  457  ASN   A ND2 1 
ATOM   154  N  N   . MET   A 1 17  ? 36.382 -18.075 -3.380  1.00 17.92 ?  458  MET   A N   1 
ATOM   155  C  CA  . MET   A 1 17  ? 37.439 -19.016 -3.028  1.00 21.61 ?  458  MET   A CA  1 
ATOM   156  C  C   . MET   A 1 17  ? 38.685 -18.878 -3.893  1.00 19.24 ?  458  MET   A C   1 
ATOM   157  O  O   . MET   A 1 17  ? 39.730 -19.425 -3.527  1.00 20.49 ?  458  MET   A O   1 
ATOM   158  C  CB  . MET   A 1 17  ? 36.930 -20.454 -3.086  1.00 29.72 ?  458  MET   A CB  1 
ATOM   159  C  CG  . MET   A 1 17  ? 36.441 -20.860 -4.451  1.00 37.41 ?  458  MET   A CG  1 
ATOM   160  S  SD  . MET   A 1 17  ? 35.798 -22.534 -4.439  1.00 40.01 ?  458  MET   A SD  1 
ATOM   161  C  CE  . MET   A 1 17  ? 34.624 -22.408 -3.094  1.00 41.08 ?  458  MET   A CE  1 
ATOM   162  N  N   . TRP   A 1 18  ? 38.606 -18.174 -5.021  1.00 17.61 ?  459  TRP   A N   1 
ATOM   163  C  CA  . TRP   A 1 18  ? 39.757 -18.000 -5.905  1.00 17.46 ?  459  TRP   A CA  1 
ATOM   164  C  C   . TRP   A 1 18  ? 40.460 -16.673 -5.699  1.00 19.20 ?  459  TRP   A C   1 
ATOM   165  O  O   . TRP   A 1 18  ? 41.682 -16.591 -5.872  1.00 17.99 ?  459  TRP   A O   1 
ATOM   166  C  CB  . TRP   A 1 18  ? 39.312 -18.111 -7.368  1.00 20.34 ?  459  TRP   A CB  1 
ATOM   167  C  CG  . TRP   A 1 18  ? 38.421 -19.282 -7.578  1.00 30.59 ?  459  TRP   A CG  1 
ATOM   168  C  CD1 . TRP   A 1 18  ? 38.802 -20.575 -7.775  1.00 33.16 ?  459  TRP   A CD1 1 
ATOM   169  C  CD2 . TRP   A 1 18  ? 36.989 -19.282 -7.560  1.00 37.54 ?  459  TRP   A CD2 1 
ATOM   170  N  NE1 . TRP   A 1 18  ? 37.695 -21.381 -7.901  1.00 37.10 ?  459  TRP   A NE1 1 
ATOM   171  C  CE2 . TRP   A 1 18  ? 36.569 -20.609 -7.777  1.00 39.84 ?  459  TRP   A CE2 1 
ATOM   172  C  CE3 . TRP   A 1 18  ? 36.021 -18.287 -7.400  1.00 38.59 ?  459  TRP   A CE3 1 
ATOM   173  C  CZ2 . TRP   A 1 18  ? 35.223 -20.967 -7.824  1.00 40.88 ?  459  TRP   A CZ2 1 
ATOM   174  C  CZ3 . TRP   A 1 18  ? 34.687 -18.644 -7.454  1.00 38.57 ?  459  TRP   A CZ3 1 
ATOM   175  C  CH2 . TRP   A 1 18  ? 34.300 -19.970 -7.670  1.00 39.50 ?  459  TRP   A CH2 1 
ATOM   176  N  N   . ASP   A 1 19  ? 39.714 -15.637 -5.324  1.00 21.35 ?  460  ASP   A N   1 
ATOM   177  C  CA  . ASP   A 1 19  ? 40.233 -14.285 -5.141  1.00 19.73 ?  460  ASP   A CA  1 
ATOM   178  C  C   . ASP   A 1 19  ? 39.786 -13.823 -3.756  1.00 20.64 ?  460  ASP   A C   1 
ATOM   179  O  O   . ASP   A 1 19  ? 38.734 -13.190 -3.607  1.00 20.29 ?  460  ASP   A O   1 
ATOM   180  C  CB  . ASP   A 1 19  ? 39.685 -13.404 -6.239  1.00 16.95 ?  460  ASP   A CB  1 
ATOM   181  C  CG  . ASP   A 1 19  ? 40.081 -11.956 -6.087  1.00 15.32 ?  460  ASP   A CG  1 
ATOM   182  O  OD1 . ASP   A 1 19  ? 40.999 -11.651 -5.293  1.00 17.13 ?  460  ASP   A OD1 1 
ATOM   183  O  OD2 . ASP   A 1 19  ? 39.449 -11.133 -6.767  1.00 16.79 -1 460  ASP   A OD2 1 
ATOM   184  N  N   . SER   A 1 20  ? 40.591 -14.141 -2.744  1.00 22.36 ?  461  SER   A N   1 
ATOM   185  C  CA  . SER   A 1 20  ? 40.261 -13.784 -1.369  1.00 22.13 ?  461  SER   A CA  1 
ATOM   186  C  C   . SER   A 1 20  ? 40.228 -12.276 -1.141  1.00 21.79 ?  461  SER   A C   1 
ATOM   187  O  O   . SER   A 1 20  ? 39.710 -11.833 -0.109  1.00 24.04 ?  461  SER   A O   1 
ATOM   188  C  CB  . SER   A 1 20  ? 41.267 -14.438 -0.421  1.00 23.94 ?  461  SER   A CB  1 
ATOM   189  O  OG  . SER   A 1 20  ? 42.480 -13.701 -0.407  1.00 24.69 ?  461  SER   A OG  1 
ATOM   190  N  N   . HIS   A 1 21  ? 40.762 -11.479 -2.067  1.00 17.41 ?  462  HIS   A N   1 
ATOM   191  C  CA  . HIS   A 1 21  ? 40.742 -10.029 -1.954  1.00 16.83 ?  462  HIS   A CA  1 
ATOM   192  C  C   . HIS   A 1 21  ? 39.627 -9.380  -2.767  1.00 16.13 ?  462  HIS   A C   1 
ATOM   193  O  O   . HIS   A 1 21  ? 39.620 -8.153  -2.915  1.00 18.14 ?  462  HIS   A O   1 
ATOM   194  C  CB  . HIS   A 1 21  ? 42.098 -9.440  -2.341  1.00 21.67 ?  462  HIS   A CB  1 
ATOM   195  C  CG  . HIS   A 1 21  ? 43.198 -9.813  -1.399  1.00 25.94 ?  462  HIS   A CG  1 
ATOM   196  N  ND1 . HIS   A 1 21  ? 44.135 -10.780 -1.693  1.00 30.16 ?  462  HIS   A ND1 1 
ATOM   197  C  CD2 . HIS   A 1 21  ? 43.500 -9.361  -0.159  1.00 28.96 ?  462  HIS   A CD2 1 
ATOM   198  C  CE1 . HIS   A 1 21  ? 44.976 -10.898 -0.682  1.00 30.58 ?  462  HIS   A CE1 1 
ATOM   199  N  NE2 . HIS   A 1 21  ? 44.612 -10.049 0.263   1.00 31.28 ?  462  HIS   A NE2 1 
ATOM   200  N  N   . HIS   A 1 22  ? 38.688 -10.163 -3.282  1.00 14.72 ?  463  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 22  ? 37.559 -9.587  -3.993  1.00 14.81 ?  463  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 22  ? 36.820 -8.618  -3.071  1.00 15.08 ?  463  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 22  ? 36.631 -8.914  -1.886  1.00 14.09 ?  463  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 22  ? 36.624 -10.697 -4.472  1.00 13.75 ?  463  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 22  ? 35.480 -10.209 -5.302  1.00 14.00 ?  463  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 22  ? 34.423 -9.505  -4.765  1.00 13.53 ?  463  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 22  ? 35.210 -10.346 -6.620  1.00 15.16 ?  463  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 22  ? 33.562 -9.210  -5.721  1.00 13.46 ?  463  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 22  ? 34.017 -9.708  -6.859  1.00 14.04 ?  463  HIS   A NE2 1 
ATOM   210  N  N   . PRO   A 1 23  ? 36.394 -7.457  -3.579  1.00 12.91 ?  464  PRO   A N   1 
ATOM   211  C  CA  . PRO   A 1 23  ? 35.885 -6.393  -2.686  1.00 13.43 ?  464  PRO   A CA  1 
ATOM   212  C  C   . PRO   A 1 23  ? 34.616 -6.739  -1.910  1.00 10.72 ?  464  PRO   A C   1 
ATOM   213  O  O   . PRO   A 1 23  ? 34.372 -6.136  -0.852  1.00 10.80 ?  464  PRO   A O   1 
ATOM   214  C  CB  . PRO   A 1 23  ? 35.663 -5.215  -3.645  1.00 12.79 ?  464  PRO   A CB  1 
ATOM   215  C  CG  . PRO   A 1 23  ? 35.528 -5.848  -5.005  1.00 14.27 ?  464  PRO   A CG  1 
ATOM   216  C  CD  . PRO   A 1 23  ? 36.489 -6.998  -4.977  1.00 13.70 ?  464  PRO   A CD  1 
ATOM   217  N  N   . GLU   A 1 24  ? 33.786 -7.670  -2.389  1.00 10.99 ?  465  GLU   A N   1 
ATOM   218  C  CA  . GLU   A 1 24  ? 32.551 -8.014  -1.681  1.00 11.10 ?  465  GLU   A CA  1 
ATOM   219  C  C   . GLU   A 1 24  ? 32.893 -9.040  -0.598  1.00 11.43 ?  465  GLU   A C   1 
ATOM   220  O  O   . GLU   A 1 24  ? 32.594 -10.233 -0.690  1.00 11.88 ?  465  GLU   A O   1 
ATOM   221  C  CB  . GLU   A 1 24  ? 31.479 -8.502  -2.657  1.00 11.10 ?  465  GLU   A CB  1 
ATOM   222  C  CG  . GLU   A 1 24  ? 30.034 -8.268  -2.179  1.00 11.87 ?  465  GLU   A CG  1 
ATOM   223  C  CD  . GLU   A 1 24  ? 29.647 -9.157  -0.999  1.00 12.16 ?  465  GLU   A CD  1 
ATOM   224  O  OE1 . GLU   A 1 24  ? 29.879 -8.739  0.150   1.00 12.26 ?  465  GLU   A OE1 1 
ATOM   225  O  OE2 . GLU   A 1 24  ? 29.080 -10.254 -1.216  1.00 11.72 -1 465  GLU   A OE2 1 
ATOM   226  N  N   . LEU   A 1 25  ? 33.553 -8.541  0.457   1.00 11.56 ?  466  LEU   A N   1 
ATOM   227  C  CA  . LEU   A 1 25  ? 34.212 -9.331  1.495   1.00 11.82 ?  466  LEU   A CA  1 
ATOM   228  C  C   . LEU   A 1 25  ? 33.230 -9.756  2.579   1.00 12.00 ?  466  LEU   A C   1 
ATOM   229  O  O   . LEU   A 1 25  ? 32.361 -8.971  2.972   1.00 11.24 ?  466  LEU   A O   1 
ATOM   230  C  CB  . LEU   A 1 25  ? 35.305 -8.524  2.180   1.00 12.00 ?  466  LEU   A CB  1 
ATOM   231  C  CG  . LEU   A 1 25  ? 36.570 -8.283  1.368   1.00 13.79 ?  466  LEU   A CG  1 
ATOM   232  C  CD1 . LEU   A 1 25  ? 37.422 -7.225  2.038   1.00 14.19 ?  466  LEU   A CD1 1 
ATOM   233  C  CD2 . LEU   A 1 25  ? 37.331 -9.597  1.176   1.00 16.27 ?  466  LEU   A CD2 1 
ATOM   234  N  N   . PRO   A 1 26  ? 33.410 -10.972 3.106   1.00 11.81 ?  467  PRO   A N   1 
ATOM   235  C  CA  . PRO   A 1 26  ? 32.671 -11.367 4.320   1.00 12.89 ?  467  PRO   A CA  1 
ATOM   236  C  C   . PRO   A 1 26  ? 32.743 -10.331 5.424   1.00 11.87 ?  467  PRO   A C   1 
ATOM   237  O  O   . PRO   A 1 26  ? 31.731 -10.070 6.099   1.00 13.44 ?  467  PRO   A O   1 
ATOM   238  C  CB  . PRO   A 1 26  ? 33.368 -12.672 4.737   1.00 14.45 ?  467  PRO   A CB  1 
ATOM   239  C  CG  . PRO   A 1 26  ? 33.837 -13.263 3.431   1.00 14.61 ?  467  PRO   A CG  1 
ATOM   240  C  CD  . PRO   A 1 26  ? 34.239 -12.071 2.573   1.00 12.27 ?  467  PRO   A CD  1 
ATOM   241  N  N   . GLN   A 1 27  ? 33.903 -9.703  5.598   1.00 11.87 ?  468  GLN   A N   1 
ATOM   242  C  CA  . GLN   A 1 27  ? 34.095 -8.769  6.694   1.00 12.08 ?  468  GLN   A CA  1 
ATOM   243  C  C   . GLN   A 1 27  ? 33.366 -7.451  6.487   1.00 11.71 ?  468  GLN   A C   1 
ATOM   244  O  O   . GLN   A 1 27  ? 33.380 -6.620  7.400   1.00 12.18 ?  468  GLN   A O   1 
ATOM   245  C  CB  . GLN   A 1 27  ? 35.586 -8.543  6.983   1.00 17.11 ?  468  GLN   A CB  1 
ATOM   246  C  CG  . GLN   A 1 27  ? 36.466 -8.232  5.785   1.00 20.74 ?  468  GLN   A CG  1 
ATOM   247  C  CD  . GLN   A 1 27  ? 37.161 -9.465  5.210   1.00 22.15 ?  468  GLN   A CD  1 
ATOM   248  O  OE1 . GLN   A 1 27  ? 36.519 -10.474 4.922   1.00 18.15 ?  468  GLN   A OE1 1 
ATOM   249  N  NE2 . GLN   A 1 27  ? 38.484 -9.376  5.027   1.00 23.24 ?  468  GLN   A NE2 1 
ATOM   250  N  N   . ARG   A 1 28  ? 32.708 -7.235  5.341   1.00 10.99 ?  469  ARG   A N   1 
ATOM   251  C  CA  . ARG   A 1 28  ? 31.884 -6.035  5.213   1.00 11.73 ?  469  ARG   A CA  1 
ATOM   252  C  C   . ARG   A 1 28  ? 30.843 -5.967  6.321   1.00 11.43 ?  469  ARG   A C   1 
ATOM   253  O  O   . ARG   A 1 28  ? 30.663 -4.919  6.955   1.00 12.23 ?  469  ARG   A O   1 
ATOM   254  C  CB  . ARG   A 1 28  ? 31.203 -5.987  3.842   1.00 10.77 ?  469  ARG   A CB  1 
ATOM   255  C  CG  . ARG   A 1 28  ? 32.185 -5.737  2.707   1.00 9.83  ?  469  ARG   A CG  1 
ATOM   256  C  CD  . ARG   A 1 28  ? 31.505 -5.909  1.339   1.00 10.92 ?  469  ARG   A CD  1 
ATOM   257  N  NE  . ARG   A 1 28  ? 30.496 -4.876  1.169   1.00 11.51 ?  469  ARG   A NE  1 
ATOM   258  C  CZ  . ARG   A 1 28  ? 29.185 -5.079  1.092   1.00 10.80 ?  469  ARG   A CZ  1 
ATOM   259  N  NH1 . ARG   A 1 28  ? 28.664 -6.308  1.100   1.00 11.05 ?  469  ARG   A NH1 1 
ATOM   260  N  NH2 . ARG   A 1 28  ? 28.381 -4.023  1.022   1.00 12.00 ?  469  ARG   A NH2 1 
ATOM   261  N  N   . ILE   A 1 29  ? 30.184 -7.086  6.603   1.00 10.17 ?  470  ILE   A N   1 
ATOM   262  C  CA  . ILE   A 1 29  ? 29.110 -7.051  7.591   1.00 9.87  ?  470  ILE   A CA  1 
ATOM   263  C  C   . ILE   A 1 29  ? 29.645 -7.107  9.018   1.00 9.42  ?  470  ILE   A C   1 
ATOM   264  O  O   . ILE   A 1 29  ? 29.104 -6.442  9.912   1.00 10.89 ?  470  ILE   A O   1 
ATOM   265  C  CB  . ILE   A 1 29  ? 28.023 -8.114  7.331   1.00 9.60  ?  470  ILE   A CB  1 
ATOM   266  C  CG1 . ILE   A 1 29  ? 28.610 -9.530  7.298   1.00 11.28 ?  470  ILE   A CG1 1 
ATOM   267  C  CG2 . ILE   A 1 29  ? 27.243 -7.774  6.058   1.00 11.17 ?  470  ILE   A CG2 1 
ATOM   268  C  CD1 . ILE   A 1 29  ? 27.573 -10.656 7.399   1.00 10.54 ?  470  ILE   A CD1 1 
ATOM   269  N  N   . SER   A 1 30  ? 30.681 -7.912  9.272   1.00 10.31 ?  471  SER   A N   1 
ATOM   270  C  CA  . SER   A 1 30  ? 31.257 -7.938  10.616  1.00 10.71 ?  471  SER   A CA  1 
ATOM   271  C  C   . SER   A 1 30  ? 31.871 -6.598  11.001  1.00 11.64 ?  471  SER   A C   1 
ATOM   272  O  O   . SER   A 1 30  ? 31.800 -6.203  12.173  1.00 12.02 ?  471  SER   A O   1 
ATOM   273  C  CB  . SER   A 1 30  ? 32.254 -9.091  10.734  1.00 13.04 ?  471  SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 30  ? 33.344 -8.902  9.861   1.00 14.00 ?  471  SER   A OG  1 
ATOM   275  N  N   . ARG   A 1 31  ? 32.460 -5.880  10.044  1.00 11.15 ?  472  ARG   A N   1 
ATOM   276  C  CA  . ARG   A 1 31  ? 33.011 -4.558  10.338  1.00 11.81 ?  472  ARG   A CA  1 
ATOM   277  C  C   . ARG   A 1 31  ? 31.916 -3.544  10.657  1.00 10.50 ?  472  ARG   A C   1 
ATOM   278  O  O   . ARG   A 1 31  ? 32.059 -2.742  11.593  1.00 10.34 ?  472  ARG   A O   1 
ATOM   279  C  CB  . ARG   A 1 31  ? 33.884 -4.065  9.184   1.00 11.14 ?  472  ARG   A CB  1 
ATOM   280  C  CG  . ARG   A 1 31  ? 35.272 -4.712  9.160   1.00 10.57 ?  472  ARG   A CG  1 
ATOM   281  C  CD  . ARG   A 1 31  ? 36.153 -4.220  10.311  1.00 11.18 ?  472  ARG   A CD  1 
ATOM   282  N  NE  . ARG   A 1 31  ? 36.419 -2.788  10.179  1.00 12.46 ?  472  ARG   A NE  1 
ATOM   283  C  CZ  . ARG   A 1 31  ? 37.361 -2.286  9.393   1.00 12.20 ?  472  ARG   A CZ  1 
ATOM   284  N  NH1 . ARG   A 1 31  ? 38.137 -3.104  8.682   1.00 11.78 ?  472  ARG   A NH1 1 
ATOM   285  N  NH2 . ARG   A 1 31  ? 37.532 -0.974  9.306   1.00 13.18 ?  472  ARG   A NH2 1 
ATOM   286  N  N   . ILE   A 1 32  ? 30.814 -3.555  9.904   1.00 9.41  ?  473  ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 32  ? 29.718 -2.655  10.236  1.00 10.05 ?  473  ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 32  ? 29.186 -2.965  11.629  1.00 8.95  ?  473  ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 32  ? 28.950 -2.058  12.440  1.00 10.19 ?  473  ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 32  ? 28.616 -2.733  9.171   1.00 9.86  ?  473  ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 32  ? 29.126 -2.170  7.829   1.00 9.71  ?  473  ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 32  ? 27.396 -1.996  9.659   1.00 11.00 ?  473  ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 32  ? 28.241 -2.540  6.623   1.00 11.36 ?  473  ILE   A CD1 1 
ATOM   294  N  N   . PHE   A 1 33  ? 28.978 -4.250  11.913  1.00 10.97 ?  474  PHE   A N   1 
ATOM   295  C  CA  . PHE   A 1 33  ? 28.496 -4.674  13.224  1.00 10.56 ?  474  PHE   A CA  1 
ATOM   296  C  C   . PHE   A 1 33  ? 29.428 -4.211  14.342  1.00 12.02 ?  474  PHE   A C   1 
ATOM   297  O  O   . PHE   A 1 33  ? 28.976 -3.625  15.342  1.00 11.97 ?  474  PHE   A O   1 
ATOM   298  C  CB  . PHE   A 1 33  ? 28.352 -6.191  13.229  1.00 12.53 ?  474  PHE   A CB  1 
ATOM   299  C  CG  . PHE   A 1 33  ? 27.751 -6.750  14.484  1.00 12.97 ?  474  PHE   A CG  1 
ATOM   300  C  CD1 . PHE   A 1 33  ? 26.395 -6.621  14.750  1.00 14.03 ?  474  PHE   A CD1 1 
ATOM   301  C  CD2 . PHE   A 1 33  ? 28.543 -7.442  15.381  1.00 14.72 ?  474  PHE   A CD2 1 
ATOM   302  C  CE1 . PHE   A 1 33  ? 25.852 -7.165  15.895  1.00 15.93 ?  474  PHE   A CE1 1 
ATOM   303  C  CE2 . PHE   A 1 33  ? 28.000 -7.982  16.528  1.00 15.38 ?  474  PHE   A CE2 1 
ATOM   304  C  CZ  . PHE   A 1 33  ? 26.659 -7.850  16.774  1.00 16.31 ?  474  PHE   A CZ  1 
ATOM   305  N  N   . SER   A 1 34  ? 30.734 -4.455  14.172  1.00 11.32 ?  475  SER   A N   1 
ATOM   306  C  CA  . SER   A 1 34  ? 31.738 -4.006  15.137  1.00 11.22 ?  475  SER   A CA  1 
ATOM   307  C  C   . SER   A 1 34  ? 31.652 -2.509  15.392  1.00 10.96 ?  475  SER   A C   1 
ATOM   308  O  O   . SER   A 1 34  ? 31.729 -2.066  16.543  1.00 12.85 ?  475  SER   A O   1 
ATOM   309  C  CB  . SER   A 1 34  ? 33.139 -4.360  14.650  1.00 11.48 ?  475  SER   A CB  1 
ATOM   310  O  OG  . SER   A 1 34  ? 34.116 -3.760  15.488  1.00 14.27 ?  475  SER   A OG  1 
ATOM   311  N  N   . ARG   A 1 35  ? 31.509 -1.698  14.335  1.00 11.05 ?  476  ARG   A N   1 
ATOM   312  C  CA  . ARG   A 1 35  ? 31.458 -0.256  14.552  1.00 9.99  ?  476  ARG   A CA  1 
ATOM   313  C  C   . ARG   A 1 35  ? 30.226 0.135   15.362  1.00 9.73  ?  476  ARG   A C   1 
ATOM   314  O  O   . ARG   A 1 35  ? 30.281 1.054   16.191  1.00 11.97 ?  476  ARG   A O   1 
ATOM   315  C  CB  . ARG   A 1 35  ? 31.514 0.480   13.209  1.00 9.23  ?  476  ARG   A CB  1 
ATOM   316  C  CG  . ARG   A 1 35  ? 31.710 1.984   13.328  1.00 10.82 ?  476  ARG   A CG  1 
ATOM   317  C  CD  . ARG   A 1 35  ? 33.051 2.346   13.945  1.00 12.86 ?  476  ARG   A CD  1 
ATOM   318  N  NE  . ARG   A 1 35  ? 33.251 3.798   13.956  1.00 13.51 ?  476  ARG   A NE  1 
ATOM   319  C  CZ  . ARG   A 1 35  ? 33.814 4.465   14.961  1.00 12.88 ?  476  ARG   A CZ  1 
ATOM   320  N  NH1 . ARG   A 1 35  ? 34.253 3.820   16.042  1.00 14.33 ?  476  ARG   A NH1 1 
ATOM   321  N  NH2 . ARG   A 1 35  ? 33.926 5.786   14.881  1.00 14.47 ?  476  ARG   A NH2 1 
ATOM   322  N  N   . HIS   A 1 36  ? 29.108 -0.565  15.155  1.00 9.55  ?  477  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 36  ? 27.921 -0.318  15.968  1.00 11.88 ?  477  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 36  ? 28.200 -0.591  17.440  1.00 11.55 ?  477  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 36  ? 27.752 0.158   18.319  1.00 12.47 ?  477  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 36  ? 26.760 -1.191  15.486  1.00 12.37 ?  477  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 36  ? 26.032 -0.636  14.302  1.00 10.91 ?  477  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 36  ? 26.528 -0.686  13.015  1.00 11.64 ?  477  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 36  ? 24.834 -0.011  14.221  1.00 10.94 ?  477  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 36  ? 25.661 -0.120  12.193  1.00 11.90 ?  477  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 36  ? 24.627 0.302   12.901  1.00 11.99 ?  477  HIS   A NE2 1 
ATOM   332  N  N   . GLU   A 1 37  ? 28.922 -1.674  17.731  1.00 12.36 ?  478  GLU   A N   1 
ATOM   333  C  CA  . GLU   A 1 37  ? 29.236 -1.983  19.125  1.00 13.48 ?  478  GLU   A CA  1 
ATOM   334  C  C   . GLU   A 1 37  ? 30.214 -0.966  19.703  1.00 13.57 ?  478  GLU   A C   1 
ATOM   335  O  O   . GLU   A 1 37  ? 30.036 -0.496  20.829  1.00 13.58 ?  478  GLU   A O   1 
ATOM   336  C  CB  . GLU   A 1 37  ? 29.799 -3.401  19.218  1.00 16.32 ?  478  GLU   A CB  1 
ATOM   337  C  CG  . GLU   A 1 37  ? 30.102 -3.849  20.637  1.00 26.03 ?  478  GLU   A CG  1 
ATOM   338  C  CD  . GLU   A 1 37  ? 30.540 -5.298  20.705  1.00 36.57 ?  478  GLU   A CD  1 
ATOM   339  O  OE1 . GLU   A 1 37  ? 31.651 -5.608  20.225  1.00 39.51 ?  478  GLU   A OE1 1 
ATOM   340  O  OE2 . GLU   A 1 37  ? 29.772 -6.128  21.243  1.00 41.62 -1 478  GLU   A OE2 1 
ATOM   341  N  N   . GLU   A 1 38  ? 31.228 -0.592  18.927  1.00 12.67 ?  479  GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 38  ? 32.256 0.341   19.369  1.00 13.62 ?  479  GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 38  ? 31.679 1.716   19.692  1.00 12.96 ?  479  GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 38  ? 32.169 2.403   20.602  1.00 14.92 ?  479  GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 38  ? 33.266 0.444   18.230  1.00 13.30 ?  479  GLU   A CB  1 
ATOM   346  C  CG  . GLU   A 1 38  ? 34.615 1.003   18.531  1.00 15.44 ?  479  GLU   A CG  1 
ATOM   347  C  CD  . GLU   A 1 38  ? 35.534 0.761   17.366  1.00 14.77 ?  479  GLU   A CD  1 
ATOM   348  O  OE1 . GLU   A 1 38  ? 35.159 1.160   16.236  1.00 13.40 ?  479  GLU   A OE1 1 
ATOM   349  O  OE2 . GLU   A 1 38  ? 36.601 0.148   17.561  1.00 14.59 -1 479  GLU   A OE2 1 
ATOM   350  N  N   . LEU   A 1 39  ? 30.643 2.134   18.971  1.00 11.40 ?  480  LEU   A N   1 
ATOM   351  C  CA  . LEU   A 1 39  ? 29.975 3.404   19.205  1.00 12.92 ?  480  LEU   A CA  1 
ATOM   352  C  C   . LEU   A 1 39  ? 28.822 3.282   20.197  1.00 12.09 ?  480  LEU   A C   1 
ATOM   353  O  O   . LEU   A 1 39  ? 28.087 4.258   20.396  1.00 15.73 ?  480  LEU   A O   1 
ATOM   354  C  CB  . LEU   A 1 39  ? 29.476 3.982   17.876  1.00 13.53 ?  480  LEU   A CB  1 
ATOM   355  C  CG  . LEU   A 1 39  ? 30.559 4.450   16.907  1.00 13.94 ?  480  LEU   A CG  1 
ATOM   356  C  CD1 . LEU   A 1 39  ? 29.944 4.839   15.552  1.00 13.11 ?  480  LEU   A CD1 1 
ATOM   357  C  CD2 . LEU   A 1 39  ? 31.360 5.605   17.513  1.00 15.73 ?  480  LEU   A CD2 1 
ATOM   358  N  N   . ARG   A 1 40  ? 28.631 2.097   20.784  1.00 12.06 ?  481  ARG   A N   1 
ATOM   359  C  CA  . ARG   A 1 40  ? 27.576 1.831   21.768  1.00 11.15 ?  481  ARG   A CA  1 
ATOM   360  C  C   . ARG   A 1 40  ? 26.182 1.963   21.180  1.00 13.44 ?  481  ARG   A C   1 
ATOM   361  O  O   . ARG   A 1 40  ? 25.205 2.165   21.908  1.00 15.30 ?  481  ARG   A O   1 
ATOM   362  C  CB  . ARG   A 1 40  ? 27.740 2.656   23.049  1.00 14.79 ?  481  ARG   A CB  1 
ATOM   363  C  CG  . ARG   A 1 40  ? 29.098 2.481   23.654  1.00 17.01 ?  481  ARG   A CG  1 
ATOM   364  C  CD  . ARG   A 1 40  ? 29.167 3.169   24.992  1.00 20.97 ?  481  ARG   A CD  1 
ATOM   365  N  NE  . ARG   A 1 40  ? 30.489 3.011   25.576  1.00 23.24 ?  481  ARG   A NE  1 
ATOM   366  C  CZ  . ARG   A 1 40  ? 30.834 3.504   26.759  1.00 26.32 ?  481  ARG   A CZ  1 
ATOM   367  N  NH1 . ARG   A 1 40  ? 29.946 4.185   27.471  1.00 26.72 ?  481  ARG   A NH1 1 
ATOM   368  N  NH2 . ARG   A 1 40  ? 32.058 3.313   27.221  1.00 26.04 ?  481  ARG   A NH2 1 
ATOM   369  N  N   . LEU   A 1 41  ? 26.078 1.838   19.862  1.00 11.63 ?  482  LEU   A N   1 
ATOM   370  C  CA  . LEU   A 1 41  ? 24.785 1.859   19.194  1.00 12.36 ?  482  LEU   A CA  1 
ATOM   371  C  C   . LEU   A 1 41  ? 24.082 0.511   19.273  1.00 12.31 ?  482  LEU   A C   1 
ATOM   372  O  O   . LEU   A 1 41  ? 22.841 0.465   19.318  1.00 13.43 ?  482  LEU   A O   1 
ATOM   373  C  CB  . LEU   A 1 41  ? 24.960 2.243   17.716  1.00 12.27 ?  482  LEU   A CB  1 
ATOM   374  C  CG  . LEU   A 1 41  ? 25.512 3.645   17.466  1.00 13.13 ?  482  LEU   A CG  1 
ATOM   375  C  CD1 . LEU   A 1 41  ? 25.968 3.800   16.038  1.00 13.99 ?  482  LEU   A CD1 1 
ATOM   376  C  CD2 . LEU   A 1 41  ? 24.498 4.712   17.775  1.00 15.71 ?  482  LEU   A CD2 1 
ATOM   377  N  N   . LEU   A 1 42  ? 24.849 -0.584  19.262  1.00 13.25 ?  483  LEU   A N   1 
ATOM   378  C  CA  . LEU   A 1 42  ? 24.255 -1.918  19.223  1.00 14.41 ?  483  LEU   A CA  1 
ATOM   379  C  C   . LEU   A 1 42  ? 23.355 -2.163  20.431  1.00 14.41 ?  483  LEU   A C   1 
ATOM   380  O  O   . LEU   A 1 42  ? 22.205 -2.600  20.286  1.00 14.83 ?  483  LEU   A O   1 
ATOM   381  C  CB  . LEU   A 1 42  ? 25.358 -2.972  19.152  1.00 15.24 ?  483  LEU   A CB  1 
ATOM   382  C  CG  . LEU   A 1 42  ? 24.867 -4.424  19.212  1.00 15.83 ?  483  LEU   A CG  1 
ATOM   383  C  CD1 . LEU   A 1 42  ? 24.016 -4.754  17.979  1.00 14.92 ?  483  LEU   A CD1 1 
ATOM   384  C  CD2 . LEU   A 1 42  ? 26.039 -5.390  19.320  1.00 17.30 ?  483  LEU   A CD2 1 
ATOM   385  N  N   . SER   A 1 43  ? 23.851 -1.860  21.636  1.00 14.64 ?  484  SER   A N   1 
ATOM   386  C  CA  . SER   A 1 43  ? 23.070 -2.123  22.844  1.00 16.31 ?  484  SER   A CA  1 
ATOM   387  C  C   . SER   A 1 43  ? 21.801 -1.283  22.915  1.00 15.63 ?  484  SER   A C   1 
ATOM   388  O  O   . SER   A 1 43  ? 20.896 -1.616  23.691  1.00 18.96 ?  484  SER   A O   1 
ATOM   389  C  CB  . SER   A 1 43  ? 23.925 -1.888  24.095  1.00 18.50 ?  484  SER   A CB  1 
ATOM   390  O  OG  . SER   A 1 43  ? 24.336 -0.535  24.193  1.00 22.42 ?  484  SER   A OG  1 
ATOM   391  N  N   . ARG   A 1 44  ? 21.722 -0.197  22.146  1.00 13.23 ?  485  ARG   A N   1 
ATOM   392  C  CA  . ARG   A 1 44  ? 20.537 0.648   22.100  1.00 12.52 ?  485  ARG   A CA  1 
ATOM   393  C  C   . ARG   A 1 44  ? 19.478 0.134   21.141  1.00 14.07 ?  485  ARG   A C   1 
ATOM   394  O  O   . ARG   A 1 44  ? 18.391 0.723   21.074  1.00 14.47 ?  485  ARG   A O   1 
ATOM   395  C  CB  . ARG   A 1 44  ? 20.915 2.070   21.684  1.00 12.64 ?  485  ARG   A CB  1 
ATOM   396  C  CG  . ARG   A 1 44  ? 21.957 2.712   22.595  1.00 13.02 ?  485  ARG   A CG  1 
ATOM   397  C  CD  . ARG   A 1 44  ? 22.435 4.039   22.039  1.00 15.57 ?  485  ARG   A CD  1 
ATOM   398  N  NE  . ARG   A 1 44  ? 21.351 5.001   21.856  1.00 14.16 ?  485  ARG   A NE  1 
ATOM   399  C  CZ  . ARG   A 1 44  ? 21.449 6.089   21.094  1.00 13.88 ?  485  ARG   A CZ  1 
ATOM   400  N  NH1 . ARG   A 1 44  ? 22.578 6.343   20.447  1.00 14.68 ?  485  ARG   A NH1 1 
ATOM   401  N  NH2 . ARG   A 1 44  ? 20.426 6.922   20.969  1.00 12.96 ?  485  ARG   A NH2 1 
ATOM   402  N  N   . CYS   A 1 45  ? 19.771 -0.924  20.393  1.00 13.08 ?  486  CYS   A N   1 
ATOM   403  C  CA  . CYS   A 1 45  ? 18.866 -1.467  19.394  1.00 13.31 ?  486  CYS   A CA  1 
ATOM   404  C  C   . CYS   A 1 45  ? 18.252 -2.745  19.944  1.00 15.03 ?  486  CYS   A C   1 
ATOM   405  O  O   . CYS   A 1 45  ? 18.802 -3.388  20.842  1.00 18.02 ?  486  CYS   A O   1 
ATOM   406  C  CB  . CYS   A 1 45  ? 19.655 -1.809  18.131  1.00 14.16 ?  486  CYS   A CB  1 
ATOM   407  S  SG  . CYS   A 1 45  ? 20.189 -0.388  17.186  1.00 13.81 ?  486  CYS   A SG  1 
ATOM   408  N  N   . HIS   A 1 46  ? 17.108 -3.121  19.382  1.00 15.81 ?  487  HIS   A N   1 
ATOM   409  C  CA  . HIS   A 1 46  ? 16.497 -4.406  19.675  1.00 15.65 ?  487  HIS   A CA  1 
ATOM   410  C  C   . HIS   A 1 46  ? 16.894 -5.399  18.590  1.00 14.14 ?  487  HIS   A C   1 
ATOM   411  O  O   . HIS   A 1 46  ? 16.635 -5.169  17.402  1.00 14.17 ?  487  HIS   A O   1 
ATOM   412  C  CB  . HIS   A 1 46  ? 14.978 -4.293  19.753  1.00 17.20 ?  487  HIS   A CB  1 
ATOM   413  C  CG  . HIS   A 1 46  ? 14.311 -5.603  20.024  1.00 20.58 ?  487  HIS   A CG  1 
ATOM   414  N  ND1 . HIS   A 1 46  ? 14.446 -6.265  21.226  1.00 21.53 ?  487  HIS   A ND1 1 
ATOM   415  C  CD2 . HIS   A 1 46  ? 13.546 -6.397  19.238  1.00 23.04 ?  487  HIS   A CD2 1 
ATOM   416  C  CE1 . HIS   A 1 46  ? 13.776 -7.402  21.175  1.00 25.01 ?  487  HIS   A CE1 1 
ATOM   417  N  NE2 . HIS   A 1 46  ? 13.222 -7.507  19.979  1.00 25.41 ?  487  HIS   A NE2 1 
ATOM   418  N  N   . ARG   A 1 47  ? 17.501 -6.505  18.995  1.00 13.68 ?  488  ARG   A N   1 
ATOM   419  C  CA  . ARG   A 1 47  ? 18.028 -7.473  18.041  1.00 15.76 ?  488  ARG   A CA  1 
ATOM   420  C  C   . ARG   A 1 47  ? 16.893 -8.276  17.410  1.00 15.96 ?  488  ARG   A C   1 
ATOM   421  O  O   . ARG   A 1 47  ? 16.026 -8.810  18.111  1.00 18.08 ?  488  ARG   A O   1 
ATOM   422  C  CB  . ARG   A 1 47  ? 19.008 -8.395  18.762  1.00 17.63 ?  488  ARG   A CB  1 
ATOM   423  C  CG  . ARG   A 1 47  ? 19.952 -9.130  17.873  1.00 20.16 ?  488  ARG   A CG  1 
ATOM   424  C  CD  . ARG   A 1 47  ? 20.969 -8.206  17.222  1.00 20.12 ?  488  ARG   A CD  1 
ATOM   425  N  NE  . ARG   A 1 47  ? 21.873 -9.035  16.457  1.00 19.39 ?  488  ARG   A NE  1 
ATOM   426  C  CZ  . ARG   A 1 47  ? 23.048 -9.469  16.881  1.00 16.30 ?  488  ARG   A CZ  1 
ATOM   427  N  NH1 . ARG   A 1 47  ? 23.508 -9.117  18.081  1.00 16.03 ?  488  ARG   A NH1 1 
ATOM   428  N  NH2 . ARG   A 1 47  ? 23.765 -10.256 16.092  1.00 18.15 ?  488  ARG   A NH2 1 
ATOM   429  N  N   . ILE   A 1 48  ? 16.881 -8.321  16.087  1.00 16.85 ?  489  ILE   A N   1 
ATOM   430  C  CA  . ILE   A 1 48  ? 15.919 -9.091  15.300  1.00 14.39 ?  489  ILE   A CA  1 
ATOM   431  C  C   . ILE   A 1 48  ? 16.676 -10.265 14.685  1.00 14.91 ?  489  ILE   A C   1 
ATOM   432  O  O   . ILE   A 1 48  ? 17.753 -10.055 14.121  1.00 13.85 ?  489  ILE   A O   1 
ATOM   433  C  CB  . ILE   A 1 48  ? 15.277 -8.225  14.196  1.00 14.45 ?  489  ILE   A CB  1 
ATOM   434  C  CG1 . ILE   A 1 48  ? 14.430 -7.118  14.833  1.00 15.52 ?  489  ILE   A CG1 1 
ATOM   435  C  CG2 . ILE   A 1 48  ? 14.488 -9.077  13.179  1.00 13.84 ?  489  ILE   A CG2 1 
ATOM   436  C  CD1 . ILE   A 1 48  ? 13.827 -6.166  13.847  1.00 15.75 ?  489  ILE   A CD1 1 
ATOM   437  N  N   . PRO   A 1 49  ? 16.162 -11.489 14.759  1.00 16.17 ?  490  PRO   A N   1 
ATOM   438  C  CA  . PRO   A 1 49  ? 16.920 -12.627 14.226  1.00 15.56 ?  490  PRO   A CA  1 
ATOM   439  C  C   . PRO   A 1 49  ? 16.851 -12.732 12.709  1.00 16.36 ?  490  PRO   A C   1 
ATOM   440  O  O   . PRO   A 1 49  ? 15.893 -12.300 12.066  1.00 17.07 ?  490  PRO   A O   1 
ATOM   441  C  CB  . PRO   A 1 49  ? 16.236 -13.833 14.881  1.00 17.56 ?  490  PRO   A CB  1 
ATOM   442  C  CG  . PRO   A 1 49  ? 14.815 -13.384 15.060  1.00 17.02 ?  490  PRO   A CG  1 
ATOM   443  C  CD  . PRO   A 1 49  ? 14.886 -11.908 15.371  1.00 15.43 ?  490  PRO   A CD  1 
ATOM   444  N  N   . ALA   A 1 50  ? 17.894 -13.331 12.138  1.00 15.55 ?  491  ALA   A N   1 
ATOM   445  C  CA  . ALA   A 1 50  ? 17.849 -13.747 10.747  1.00 16.56 ?  491  ALA   A CA  1 
ATOM   446  C  C   . ALA   A 1 50  ? 17.055 -15.041 10.626  1.00 16.82 ?  491  ALA   A C   1 
ATOM   447  O  O   . ALA   A 1 50  ? 16.910 -15.805 11.588  1.00 16.97 ?  491  ALA   A O   1 
ATOM   448  C  CB  . ALA   A 1 50  ? 19.265 -13.978 10.222  1.00 17.43 ?  491  ALA   A CB  1 
ATOM   449  N  N   . ARG   A 1 51  ? 16.523 -15.272 9.428   1.00 15.75 ?  492  ARG   A N   1 
ATOM   450  C  CA  . ARG   A 1 51  ? 15.906 -16.541 9.078   1.00 14.68 ?  492  ARG   A CA  1 
ATOM   451  C  C   . ARG   A 1 51  ? 16.082 -16.757 7.584   1.00 14.69 ?  492  ARG   A C   1 
ATOM   452  O  O   . ARG   A 1 51  ? 16.400 -15.824 6.837   1.00 16.07 ?  492  ARG   A O   1 
ATOM   453  C  CB  . ARG   A 1 51  ? 14.416 -16.567 9.451   1.00 13.99 ?  492  ARG   A CB  1 
ATOM   454  C  CG  . ARG   A 1 51  ? 13.530 -15.726 8.539   1.00 13.14 ?  492  ARG   A CG  1 
ATOM   455  C  CD  . ARG   A 1 51  ? 12.069 -16.089 8.731   1.00 13.70 ?  492  ARG   A CD  1 
ATOM   456  N  NE  . ARG   A 1 51  ? 11.096 -15.214 8.073   1.00 13.73 ?  492  ARG   A NE  1 
ATOM   457  C  CZ  . ARG   A 1 51  ? 10.645 -15.379 6.828   1.00 14.82 ?  492  ARG   A CZ  1 
ATOM   458  N  NH1 . ARG   A 1 51  ? 11.113 -16.358 6.066   1.00 14.35 ?  492  ARG   A NH1 1 
ATOM   459  N  NH2 . ARG   A 1 51  ? 9.720  -14.563 6.334   1.00 14.50 ?  492  ARG   A NH2 1 
ATOM   460  N  N   . LEU   A 1 52  ? 15.912 -18.002 7.152   1.00 14.10 ?  493  LEU   A N   1 
ATOM   461  C  CA  . LEU   A 1 52  ? 15.927 -18.293 5.725   1.00 14.86 ?  493  LEU   A CA  1 
ATOM   462  C  C   . LEU   A 1 52  ? 14.642 -17.797 5.076   1.00 13.24 ?  493  LEU   A C   1 
ATOM   463  O  O   . LEU   A 1 52  ? 13.543 -18.046 5.578   1.00 15.09 ?  493  LEU   A O   1 
ATOM   464  C  CB  . LEU   A 1 52  ? 16.017 -19.800 5.497   1.00 15.01 ?  493  LEU   A CB  1 
ATOM   465  C  CG  . LEU   A 1 52  ? 17.237 -20.579 5.969   1.00 17.06 ?  493  LEU   A CG  1 
ATOM   466  C  CD1 . LEU   A 1 52  ? 17.038 -22.052 5.638   1.00 18.34 ?  493  LEU   A CD1 1 
ATOM   467  C  CD2 . LEU   A 1 52  ? 18.496 -20.060 5.309   1.00 16.85 ?  493  LEU   A CD2 1 
ATOM   468  N  N   . ALA   A 1 53  ? 14.768 -17.103 3.949   1.00 13.29 ?  494  ALA   A N   1 
ATOM   469  C  CA  . ALA   A 1 53  ? 13.624 -16.977 3.065   1.00 14.50 ?  494  ALA   A CA  1 
ATOM   470  C  C   . ALA   A 1 53  ? 13.241 -18.360 2.550   1.00 13.98 ?  494  ALA   A C   1 
ATOM   471  O  O   . ALA   A 1 53  ? 14.092 -19.241 2.371   1.00 16.50 ?  494  ALA   A O   1 
ATOM   472  C  CB  . ALA   A 1 53  ? 13.964 -16.076 1.879   1.00 12.89 ?  494  ALA   A CB  1 
ATOM   473  N  N   . THR   A 1 54  ? 11.948 -18.563 2.342   1.00 15.59 ?  495  THR   A N   1 
ATOM   474  C  CA  . THR   A 1 54  ? 11.497 -19.789 1.703   1.00 14.62 ?  495  THR   A CA  1 
ATOM   475  C  C   . THR   A 1 54  ? 11.474 -19.604 0.195   1.00 16.11 ?  495  THR   A C   1 
ATOM   476  O  O   . THR   A 1 54  ? 11.461 -18.482 -0.318  1.00 15.42 ?  495  THR   A O   1 
ATOM   477  C  CB  . THR   A 1 54  ? 10.091 -20.154 2.162   1.00 15.67 ?  495  THR   A CB  1 
ATOM   478  O  OG1 . THR   A 1 54  ? 9.186  -19.150 1.698   1.00 14.85 ?  495  THR   A OG1 1 
ATOM   479  C  CG2 . THR   A 1 54  ? 10.030 -20.283 3.697   1.00 15.08 ?  495  THR   A CG2 1 
ATOM   480  N  N   . GLU   A 1 55  ? 11.467 -20.731 -0.523  1.00 17.38 ?  496  GLU   A N   1 
ATOM   481  C  CA  . GLU   A 1 55  ? 11.379 -20.667 -1.979  1.00 17.30 ?  496  GLU   A CA  1 
ATOM   482  C  C   . GLU   A 1 55  ? 10.083 -20.003 -2.429  1.00 16.54 ?  496  GLU   A C   1 
ATOM   483  O  O   . GLU   A 1 55  ? 10.067 -19.300 -3.446  1.00 16.60 ?  496  GLU   A O   1 
ATOM   484  C  CB  . GLU   A 1 55  ? 11.523 -22.069 -2.574  1.00 18.52 ?  496  GLU   A CB  1 
ATOM   485  C  CG  . GLU   A 1 55  ? 12.908 -22.669 -2.379  1.00 22.82 ?  496  GLU   A CG  1 
ATOM   486  C  CD  . GLU   A 1 55  ? 13.033 -24.052 -2.979  1.00 27.53 ?  496  GLU   A CD  1 
ATOM   487  O  OE1 . GLU   A 1 55  ? 12.437 -24.294 -4.045  1.00 29.05 ?  496  GLU   A OE1 1 
ATOM   488  O  OE2 . GLU   A 1 55  ? 13.719 -24.904 -2.376  1.00 29.91 -1 496  GLU   A OE2 1 
ATOM   489  N  N   . GLU   A 1 56  ? 8.994  -20.194 -1.684  1.00 18.66 ?  497  GLU   A N   1 
ATOM   490  C  CA  . GLU   A 1 56  ? 7.763  -19.489 -2.024  1.00 17.11 ?  497  GLU   A CA  1 
ATOM   491  C  C   . GLU   A 1 56  ? 7.948  -17.982 -1.904  1.00 16.04 ?  497  GLU   A C   1 
ATOM   492  O  O   . GLU   A 1 56  ? 7.460  -17.217 -2.744  1.00 16.28 ?  497  GLU   A O   1 
ATOM   493  C  CB  . GLU   A 1 56  ? 6.596  -19.975 -1.159  1.00 21.44 ?  497  GLU   A CB  1 
ATOM   494  C  CG  . GLU   A 1 56  ? 6.453  -21.494 -1.109  1.00 28.41 ?  497  GLU   A CG  1 
ATOM   495  C  CD  . GLU   A 1 56  ? 7.115  -22.101 0.117   1.00 33.60 ?  497  GLU   A CD  1 
ATOM   496  O  OE1 . GLU   A 1 56  ? 6.492  -22.069 1.210   1.00 32.83 ?  497  GLU   A OE1 1 
ATOM   497  O  OE2 . GLU   A 1 56  ? 8.256  -22.602 -0.009  1.00 36.19 -1 497  GLU   A OE2 1 
ATOM   498  N  N   . GLU   A 1 57  ? 8.682  -17.536 -0.884  1.00 15.11 ?  498  GLU   A N   1 
ATOM   499  C  CA  . GLU   A 1 57  ? 8.949  -16.107 -0.764  1.00 13.91 ?  498  GLU   A CA  1 
ATOM   500  C  C   . GLU   A 1 57  ? 9.809  -15.600 -1.918  1.00 10.92 ?  498  GLU   A C   1 
ATOM   501  O  O   . GLU   A 1 57  ? 9.522  -14.540 -2.480  1.00 13.15 ?  498  GLU   A O   1 
ATOM   502  C  CB  . GLU   A 1 57  ? 9.572  -15.796 0.598   1.00 14.02 ?  498  GLU   A CB  1 
ATOM   503  C  CG  . GLU   A 1 57  ? 8.540  -15.905 1.731   1.00 16.16 ?  498  GLU   A CG  1 
ATOM   504  C  CD  . GLU   A 1 57  ? 9.132  -15.952 3.123   1.00 16.29 ?  498  GLU   A CD  1 
ATOM   505  O  OE1 . GLU   A 1 57  ? 10.320 -16.312 3.283   1.00 13.36 ?  498  GLU   A OE1 1 
ATOM   506  O  OE2 . GLU   A 1 57  ? 8.374  -15.643 4.076   1.00 16.31 -1 498  GLU   A OE2 1 
ATOM   507  N  N   . LEU   A 1 58  ? 10.847 -16.346 -2.298  1.00 11.99 ?  499  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 58  ? 11.669 -15.948 -3.444  1.00 12.58 ?  499  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 58  ? 10.837 -15.793 -4.707  1.00 12.69 ?  499  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 58  ? 11.138 -14.943 -5.555  1.00 13.50 ?  499  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 58  ? 12.759 -16.982 -3.681  1.00 12.20 ?  499  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 58  ? 13.791 -17.148 -2.574  1.00 13.54 ?  499  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 58  ? 14.816 -18.148 -3.074  1.00 16.23 ?  499  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 58  ? 14.458 -15.827 -2.196  1.00 15.70 ?  499  LEU   A CD2 1 
ATOM   515  N  N   . ALA   A 1 59  ? 9.783  -16.598 -4.847  1.00 14.09 ?  500  ALA   A N   1 
ATOM   516  C  CA  . ALA   A 1 59  ? 8.935  -16.542 -6.030  1.00 15.18 ?  500  ALA   A CA  1 
ATOM   517  C  C   . ALA   A 1 59  ? 8.079  -15.287 -6.084  1.00 14.36 ?  500  ALA   A C   1 
ATOM   518  O  O   . ALA   A 1 59  ? 7.435  -15.041 -7.110  1.00 16.07 ?  500  ALA   A O   1 
ATOM   519  C  CB  . ALA   A 1 59  ? 8.060  -17.799 -6.118  1.00 18.59 ?  500  ALA   A CB  1 
ATOM   520  N  N   . LEU   A 1 60  ? 8.067  -14.476 -5.023  1.00 15.75 ?  501  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 60  ? 7.397  -13.187 -5.118  1.00 15.70 ?  501  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 60  ? 8.025  -12.307 -6.191  1.00 14.57 ?  501  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 60  ? 7.337  -11.477 -6.795  1.00 14.46 ?  501  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 60  ? 7.432  -12.476 -3.772  1.00 15.45 ?  501  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 60  ? 6.657  -13.128 -2.630  1.00 16.94 ?  501  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 60  ? 7.004  -12.464 -1.285  1.00 18.03 ?  501  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 60  ? 5.147  -13.119 -2.905  1.00 18.95 ?  501  LEU   A CD2 1 
ATOM   528  N  N   . CYS   A 1 61  ? 9.324  -12.464 -6.442  1.00 12.18 ?  502  CYS   A N   1 
ATOM   529  C  CA  . CYS   A 1 61  ? 10.001 -11.670 -7.457  1.00 13.43 ?  502  CYS   A CA  1 
ATOM   530  C  C   . CYS   A 1 61  ? 10.798 -12.464 -8.465  1.00 13.59 ?  502  CYS   A C   1 
ATOM   531  O  O   . CYS   A 1 61  ? 11.146 -11.897 -9.503  1.00 14.46 ?  502  CYS   A O   1 
ATOM   532  C  CB  . CYS   A 1 61  ? 10.950 -10.640 -6.826  1.00 11.40 ?  502  CYS   A CB  1 
ATOM   533  S  SG  . CYS   A 1 61  ? 10.163 -9.472  -5.699  1.00 12.52 ?  502  CYS   A SG  1 
ATOM   534  N  N   . HIS   A 1 62  ? 11.135 -13.721 -8.200  1.00 12.39 ?  503  HIS   A N   1 
ATOM   535  C  CA  . HIS   A 1 62  ? 12.074 -14.435 -9.053  1.00 11.58 ?  503  HIS   A CA  1 
ATOM   536  C  C   . HIS   A 1 62  ? 11.431 -15.635 -9.726  1.00 12.79 ?  503  HIS   A C   1 
ATOM   537  O  O   . HIS   A 1 62  ? 10.495 -16.251 -9.196  1.00 13.29 ?  503  HIS   A O   1 
ATOM   538  C  CB  . HIS   A 1 62  ? 13.287 -14.860 -8.242  1.00 12.40 ?  503  HIS   A CB  1 
ATOM   539  C  CG  . HIS   A 1 62  ? 14.091 -13.698 -7.753  1.00 10.74 ?  503  HIS   A CG  1 
ATOM   540  N  ND1 . HIS   A 1 62  ? 14.860 -12.927 -8.602  1.00 12.16 ?  503  HIS   A ND1 1 
ATOM   541  C  CD2 . HIS   A 1 62  ? 14.220 -13.151 -6.521  1.00 11.14 ?  503  HIS   A CD2 1 
ATOM   542  C  CE1 . HIS   A 1 62  ? 15.433 -11.958 -7.909  1.00 12.41 ?  503  HIS   A CE1 1 
ATOM   543  N  NE2 . HIS   A 1 62  ? 15.065 -12.072 -6.645  1.00 11.97 ?  503  HIS   A NE2 1 
ATOM   544  N  N   . SER   A 1 63  ? 11.958 -15.947 -10.908 1.00 14.04 ?  504  SER   A N   1 
ATOM   545  C  CA  . SER   A 1 63  ? 11.489 -17.086 -11.676 1.00 12.53 ?  504  SER   A CA  1 
ATOM   546  C  C   . SER   A 1 63  ? 11.885 -18.385 -10.984 1.00 12.15 ?  504  SER   A C   1 
ATOM   547  O  O   . SER   A 1 63  ? 12.893 -18.460 -10.275 1.00 14.10 ?  504  SER   A O   1 
ATOM   548  C  CB  . SER   A 1 63  ? 12.114 -17.060 -13.073 1.00 12.32 ?  504  SER   A CB  1 
ATOM   549  O  OG  . SER   A 1 63  ? 13.483 -17.430 -13.014 1.00 14.04 ?  504  SER   A OG  1 
ATOM   550  N  N   A SER   A 1 64  ? 11.073 -19.420 -11.211 0.83 13.77 ?  505  SER   A N   1 
ATOM   551  N  N   B SER   A 1 64  ? 11.084 -19.426 -11.217 0.17 13.28 ?  505  SER   A N   1 
ATOM   552  C  CA  A SER   A 1 64  ? 11.370 -20.728 -10.650 0.83 13.75 ?  505  SER   A CA  1 
ATOM   553  C  CA  B SER   A 1 64  ? 11.384 -20.728 -10.634 0.17 14.07 ?  505  SER   A CA  1 
ATOM   554  C  C   A SER   A 1 64  ? 12.685 -21.272 -11.184 0.83 10.45 ?  505  SER   A C   1 
ATOM   555  C  C   B SER   A 1 64  ? 12.668 -21.318 -11.202 0.17 12.97 ?  505  SER   A C   1 
ATOM   556  O  O   A SER   A 1 64  ? 13.429 -21.922 -10.441 0.83 13.17 ?  505  SER   A O   1 
ATOM   557  O  O   B SER   A 1 64  ? 13.360 -22.070 -10.505 0.17 13.53 ?  505  SER   A O   1 
ATOM   558  C  CB  A SER   A 1 64  ? 10.208 -21.693 -10.916 0.83 13.26 ?  505  SER   A CB  1 
ATOM   559  C  CB  B SER   A 1 64  ? 10.207 -21.682 -10.835 0.17 15.05 ?  505  SER   A CB  1 
ATOM   560  O  OG  A SER   A 1 64  ? 10.075 -21.964 -12.303 0.83 12.40 ?  505  SER   A OG  1 
ATOM   561  O  OG  B SER   A 1 64  ? 10.459 -22.930 -10.215 0.17 15.73 ?  505  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 65  ? 13.007 -20.992 -12.454 1.00 12.57 ?  506  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 65  ? 14.273 -21.455 -13.018 1.00 13.43 ?  506  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 65  ? 15.459 -20.838 -12.279 1.00 11.93 ?  506  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 65  ? 16.398 -21.540 -11.899 1.00 13.67 ?  506  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 65  ? 14.342 -21.143 -14.516 1.00 13.51 ?  506  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 65  ? 15.688 -21.493 -15.166 1.00 14.89 ?  506  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 65  ? 15.660 -21.221 -16.663 1.00 17.85 ?  506  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 65  ? 17.042 -21.389 -17.284 1.00 21.69 ?  506  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 65  ? 17.951 -20.239 -16.975 1.00 23.50 ?  506  LYS   A NZ  1 
ATOM   571  N  N   . HIS   A 1 66  ? 15.434 -19.516 -12.069 1.00 12.39 ?  507  HIS   A N   1 
ATOM   572  C  CA  . HIS   A 1 66  ? 16.550 -18.847 -11.396 1.00 12.08 ?  507  HIS   A CA  1 
ATOM   573  C  C   . HIS   A 1 66  ? 16.742 -19.362 -9.967  1.00 11.73 ?  507  HIS   A C   1 
ATOM   574  O  O   . HIS   A 1 66  ? 17.871 -19.641 -9.539  1.00 12.93 ?  507  HIS   A O   1 
ATOM   575  C  CB  . HIS   A 1 66  ? 16.323 -17.335 -11.426 1.00 13.16 ?  507  HIS   A CB  1 
ATOM   576  C  CG  . HIS   A 1 66  ? 17.344 -16.559 -10.660 1.00 13.50 ?  507  HIS   A CG  1 
ATOM   577  N  ND1 . HIS   A 1 66  ? 18.691 -16.604 -10.952 1.00 15.63 ?  507  HIS   A ND1 1 
ATOM   578  C  CD2 . HIS   A 1 66  ? 17.210 -15.712 -9.614  1.00 13.47 ?  507  HIS   A CD2 1 
ATOM   579  C  CE1 . HIS   A 1 66  ? 19.344 -15.827 -10.105 1.00 13.18 ?  507  HIS   A CE1 1 
ATOM   580  N  NE2 . HIS   A 1 66  ? 18.467 -15.274 -9.287  1.00 12.66 ?  507  HIS   A NE2 1 
ATOM   581  N  N   . ILE   A 1 67  ? 15.646 -19.514 -9.225  1.00 11.85 ?  508  ILE   A N   1 
ATOM   582  C  CA  . ILE   A 1 67  ? 15.722 -20.087 -7.879  1.00 12.61 ?  508  ILE   A CA  1 
ATOM   583  C  C   . ILE   A 1 67  ? 16.405 -21.451 -7.915  1.00 11.53 ?  508  ILE   A C   1 
ATOM   584  O  O   . ILE   A 1 67  ? 17.306 -21.738 -7.114  1.00 12.98 ?  508  ILE   A O   1 
ATOM   585  C  CB  . ILE   A 1 67  ? 14.315 -20.171 -7.264  1.00 12.01 ?  508  ILE   A CB  1 
ATOM   586  C  CG1 . ILE   A 1 67  ? 13.719 -18.767 -7.109  1.00 13.15 ?  508  ILE   A CG1 1 
ATOM   587  C  CG2 . ILE   A 1 67  ? 14.353 -20.936 -5.953  1.00 13.41 ?  508  ILE   A CG2 1 
ATOM   588  C  CD1 . ILE   A 1 67  ? 12.236 -18.763 -6.777  1.00 13.85 ?  508  ILE   A CD1 1 
ATOM   589  N  N   . SER   A 1 68  ? 16.009 -22.299 -8.880  1.00 13.05 ?  509  SER   A N   1 
ATOM   590  C  CA  . SER   A 1 68  ? 16.527 -23.664 -8.932  1.00 14.58 ?  509  SER   A CA  1 
ATOM   591  C  C   . SER   A 1 68  ? 18.018 -23.694 -9.259  1.00 12.75 ?  509  SER   A C   1 
ATOM   592  O  O   . SER   A 1 68  ? 18.760 -24.526 -8.719  1.00 13.56 ?  509  SER   A O   1 
ATOM   593  C  CB  . SER   A 1 68  ? 15.720 -24.489 -9.943  1.00 13.38 ?  509  SER   A CB  1 
ATOM   594  O  OG  . SER   A 1 68  ? 16.054 -24.164 -11.293 1.00 15.97 ?  509  SER   A OG  1 
ATOM   595  N  N   . ILE   A 1 69  ? 18.480 -22.798 -10.137 1.00 13.28 ?  510  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 69  ? 19.894 -22.781 -10.499 1.00 14.23 ?  510  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 69  ? 20.748 -22.357 -9.311  1.00 14.30 ?  510  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 69  ? 21.747 -23.008 -8.983  1.00 13.30 ?  510  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 69  ? 20.142 -21.895 -11.731 1.00 14.64 ?  510  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 69  ? 19.502 -22.510 -12.979 1.00 13.59 ?  510  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 69  ? 21.638 -21.704 -11.943 1.00 14.73 ?  510  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 69  ? 19.392 -21.522 -14.131 1.00 15.46 ?  510  ILE   A CD1 1 
ATOM   603  N  N   . ILE   A 1 70  ? 20.382 -21.251 -8.655  1.00 13.23 ?  511  ILE   A N   1 
ATOM   604  C  CA  . ILE   A 1 70  ? 21.180 -20.805 -7.513  1.00 13.20 ?  511  ILE   A CA  1 
ATOM   605  C  C   . ILE   A 1 70  ? 21.132 -21.843 -6.399  1.00 12.90 ?  511  ILE   A C   1 
ATOM   606  O  O   . ILE   A 1 70  ? 22.146 -22.127 -5.751  1.00 14.44 ?  511  ILE   A O   1 
ATOM   607  C  CB  . ILE   A 1 70  ? 20.732 -19.411 -7.034  1.00 13.46 ?  511  ILE   A CB  1 
ATOM   608  C  CG1 . ILE   A 1 70  ? 20.733 -18.414 -8.201  1.00 12.56 ?  511  ILE   A CG1 1 
ATOM   609  C  CG2 . ILE   A 1 70  ? 21.622 -18.949 -5.879  1.00 11.65 ?  511  ILE   A CG2 1 
ATOM   610  C  CD1 . ILE   A 1 70  ? 22.032 -18.334 -8.990  1.00 14.51 ?  511  ILE   A CD1 1 
ATOM   611  N  N   . LYS   A 1 71  ? 19.964 -22.453 -6.187  1.00 13.11 ?  512  LYS   A N   1 
ATOM   612  C  CA  . LYS   A 1 71  ? 19.860 -23.530 -5.207  1.00 13.60 ?  512  LYS   A CA  1 
ATOM   613  C  C   . LYS   A 1 71  ? 20.805 -24.683 -5.537  1.00 13.86 ?  512  LYS   A C   1 
ATOM   614  O  O   . LYS   A 1 71  ? 21.462 -25.235 -4.643  1.00 16.52 ?  512  LYS   A O   1 
ATOM   615  C  CB  . LYS   A 1 71  ? 18.413 -24.014 -5.141  1.00 15.75 ?  512  LYS   A CB  1 
ATOM   616  C  CG  . LYS   A 1 71  ? 18.195 -25.173 -4.179  1.00 19.44 ?  512  LYS   A CG  1 
ATOM   617  C  CD  . LYS   A 1 71  ? 16.728 -25.561 -4.144  1.00 23.15 ?  512  LYS   A CD  1 
ATOM   618  C  CE  . LYS   A 1 71  ? 16.455 -26.671 -3.134  1.00 29.11 ?  512  LYS   A CE  1 
ATOM   619  N  NZ  . LYS   A 1 71  ? 15.074 -27.213 -3.282  1.00 32.36 ?  512  LYS   A NZ  1 
ATOM   620  N  N   . SER   A 1 72  ? 20.900 -25.055 -6.821  1.00 14.80 ?  513  SER   A N   1 
ATOM   621  C  CA  . SER   A 1 72  ? 21.752 -26.171 -7.220  1.00 14.70 ?  513  SER   A CA  1 
ATOM   622  C  C   . SER   A 1 72  ? 23.230 -25.911 -6.950  1.00 17.11 ?  513  SER   A C   1 
ATOM   623  O  O   . SER   A 1 72  ? 24.001 -26.870 -6.823  1.00 18.98 ?  513  SER   A O   1 
ATOM   624  C  CB  . SER   A 1 72  ? 21.528 -26.506 -8.707  1.00 15.11 ?  513  SER   A CB  1 
ATOM   625  O  OG  . SER   A 1 72  ? 22.256 -25.635 -9.560  1.00 16.27 ?  513  SER   A OG  1 
ATOM   626  N  N   . SER   A 1 73  ? 23.645 -24.643 -6.841  1.00 14.44 ?  514  SER   A N   1 
ATOM   627  C  CA  . SER   A 1 73  ? 25.059 -24.352 -6.637  1.00 15.78 ?  514  SER   A CA  1 
ATOM   628  C  C   . SER   A 1 73  ? 25.562 -24.848 -5.289  1.00 17.19 ?  514  SER   A C   1 
ATOM   629  O  O   . SER   A 1 73  ? 26.772 -25.032 -5.132  1.00 18.42 ?  514  SER   A O   1 
ATOM   630  C  CB  . SER   A 1 73  ? 25.344 -22.850 -6.761  1.00 15.62 ?  514  SER   A CB  1 
ATOM   631  O  OG  . SER   A 1 73  ? 24.734 -22.109 -5.718  1.00 16.08 ?  514  SER   A OG  1 
ATOM   632  N  N   . GLU   A 1 74  ? 24.660 -25.067 -4.326  1.00 17.36 ?  515  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 74  ? 25.045 -25.531 -2.994  1.00 23.39 ?  515  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 74  ? 25.771 -26.871 -3.033  1.00 26.21 ?  515  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 74  ? 26.518 -27.184 -2.101  1.00 24.76 ?  515  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 74  ? 23.798 -25.615 -2.101  1.00 25.09 ?  515  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 74  ? 24.068 -26.010 -0.646  1.00 31.94 ?  515  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 74  ? 22.868 -25.790 0.270   1.00 36.88 ?  515  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 74  ? 22.837 -26.390 1.371   1.00 38.89 ?  515  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 74  ? 21.959 -25.019 -0.100  1.00 39.17 -1 515  GLU   A OE2 1 
ATOM   641  N  N   . HIS   A 1 75  ? 25.596 -27.654 -4.098  1.00 28.86 ?  516  HIS   A N   1 
ATOM   642  C  CA  . HIS   A 1 75  ? 26.146 -29.003 -4.179  1.00 30.49 ?  516  HIS   A CA  1 
ATOM   643  C  C   . HIS   A 1 75  ? 27.290 -29.132 -5.179  1.00 29.84 ?  516  HIS   A C   1 
ATOM   644  O  O   . HIS   A 1 75  ? 27.711 -30.254 -5.476  1.00 29.13 ?  516  HIS   A O   1 
ATOM   645  C  CB  . HIS   A 1 75  ? 25.040 -30.011 -4.509  1.00 33.32 ?  516  HIS   A CB  1 
ATOM   646  C  CG  . HIS   A 1 75  ? 23.825 -29.879 -3.644  1.00 37.07 ?  516  HIS   A CG  1 
ATOM   647  N  ND1 . HIS   A 1 75  ? 23.851 -30.104 -2.284  1.00 39.64 ?  516  HIS   A ND1 1 
ATOM   648  C  CD2 . HIS   A 1 75  ? 22.549 -29.542 -3.946  1.00 38.93 ?  516  HIS   A CD2 1 
ATOM   649  C  CE1 . HIS   A 1 75  ? 22.643 -29.910 -1.785  1.00 40.65 ?  516  HIS   A CE1 1 
ATOM   650  N  NE2 . HIS   A 1 75  ? 21.834 -29.570 -2.773  1.00 40.02 ?  516  HIS   A NE2 1 
ATOM   651  N  N   . MET   A 1 76  ? 27.818 -28.025 -5.689  1.00 27.93 ?  517  MET   A N   1 
ATOM   652  C  CA  . MET   A 1 76  ? 28.829 -28.068 -6.734  1.00 28.81 ?  517  MET   A CA  1 
ATOM   653  C  C   . MET   A 1 76  ? 30.239 -27.977 -6.159  1.00 31.63 ?  517  MET   A C   1 
ATOM   654  O  O   . MET   A 1 76  ? 30.462 -27.468 -5.056  1.00 29.00 ?  517  MET   A O   1 
ATOM   655  C  CB  . MET   A 1 76  ? 28.601 -26.940 -7.742  1.00 26.99 ?  517  MET   A CB  1 
ATOM   656  C  CG  . MET   A 1 76  ? 27.277 -27.049 -8.476  1.00 24.90 ?  517  MET   A CG  1 
ATOM   657  S  SD  . MET   A 1 76  ? 27.092 -25.746 -9.702  1.00 20.67 ?  517  MET   A SD  1 
ATOM   658  C  CE  . MET   A 1 76  ? 25.608 -26.281 -10.561 1.00 22.35 ?  517  MET   A CE  1 
ATOM   659  N  N   . LYS   A 1 77  ? 31.200 -28.486 -6.937  1.00 33.45 ?  518  LYS   A N   1 
ATOM   660  C  CA  . LYS   A 1 77  ? 32.614 -28.442 -6.608  1.00 35.99 ?  518  LYS   A CA  1 
ATOM   661  C  C   . LYS   A 1 77  ? 33.230 -27.146 -7.121  1.00 35.71 ?  518  LYS   A C   1 
ATOM   662  O  O   . LYS   A 1 77  ? 32.680 -26.502 -8.020  1.00 36.44 ?  518  LYS   A O   1 
ATOM   663  C  CB  . LYS   A 1 77  ? 33.322 -29.641 -7.238  1.00 36.74 ?  518  LYS   A CB  1 
ATOM   664  C  CG  . LYS   A 1 77  ? 32.873 -30.987 -6.675  1.00 37.32 ?  518  LYS   A CG  1 
ATOM   665  C  CD  . LYS   A 1 77  ? 33.679 -31.378 -5.443  1.00 37.35 ?  518  LYS   A CD  1 
ATOM   666  C  CE  . LYS   A 1 77  ? 34.031 -32.860 -5.451  1.00 36.13 ?  518  LYS   A CE  1 
ATOM   667  N  NZ  . LYS   A 1 77  ? 35.128 -33.181 -4.488  1.00 35.25 ?  518  LYS   A NZ  1 
ATOM   668  N  N   . PRO   A 1 78  ? 34.372 -26.730 -6.554  1.00 32.71 ?  519  PRO   A N   1 
ATOM   669  C  CA  . PRO   A 1 78  ? 34.965 -25.433 -6.945  1.00 33.60 ?  519  PRO   A CA  1 
ATOM   670  C  C   . PRO   A 1 78  ? 35.078 -25.184 -8.442  1.00 37.43 ?  519  PRO   A C   1 
ATOM   671  O  O   . PRO   A 1 78  ? 34.737 -24.091 -8.912  1.00 39.77 ?  519  PRO   A O   1 
ATOM   672  C  CB  . PRO   A 1 78  ? 36.337 -25.477 -6.259  1.00 31.41 ?  519  PRO   A CB  1 
ATOM   673  C  CG  . PRO   A 1 78  ? 36.077 -26.240 -5.014  1.00 30.11 ?  519  PRO   A CG  1 
ATOM   674  C  CD  . PRO   A 1 78  ? 35.068 -27.312 -5.390  1.00 30.17 ?  519  PRO   A CD  1 
ATOM   675  N  N   . ARG   A 1 79  ? 35.561 -26.168 -9.203  1.00 35.43 ?  520  ARG   A N   1 
ATOM   676  C  CA  . ARG   A 1 79  ? 35.709 -25.984 -10.644 1.00 34.75 ?  520  ARG   A CA  1 
ATOM   677  C  C   . ARG   A 1 79  ? 34.372 -25.665 -11.298 1.00 34.00 ?  520  ARG   A C   1 
ATOM   678  O  O   . ARG   A 1 79  ? 34.293 -24.803 -12.181 1.00 32.61 ?  520  ARG   A O   1 
ATOM   679  C  CB  . ARG   A 1 79  ? 36.319 -27.238 -11.267 1.00 35.41 ?  520  ARG   A CB  1 
ATOM   680  C  CG  . ARG   A 1 79  ? 36.595 -27.117 -12.754 1.00 37.55 ?  520  ARG   A CG  1 
ATOM   681  C  CD  . ARG   A 1 79  ? 38.016 -27.561 -13.075 1.00 38.65 ?  520  ARG   A CD  1 
ATOM   682  N  NE  . ARG   A 1 79  ? 38.493 -27.028 -14.349 0.37 37.53 ?  520  ARG   A NE  1 
ATOM   683  C  CZ  . ARG   A 1 79  ? 38.802 -25.751 -14.567 0.31 36.76 ?  520  ARG   A CZ  1 
ATOM   684  N  NH1 . ARG   A 1 79  ? 38.689 -24.854 -13.595 1.00 38.05 ?  520  ARG   A NH1 1 
ATOM   685  N  NH2 . ARG   A 1 79  ? 39.229 -25.370 -15.762 0.50 36.14 ?  520  ARG   A NH2 1 
ATOM   686  N  N   . ASP   A 1 80  ? 33.308 -26.345 -10.868 1.00 33.27 ?  521  ASP   A N   1 
ATOM   687  C  CA  . ASP   A 1 80  ? 31.990 -26.111 -11.448 1.00 35.39 ?  521  ASP   A CA  1 
ATOM   688  C  C   . ASP   A 1 80  ? 31.399 -24.785 -10.990 1.00 35.40 ?  521  ASP   A C   1 
ATOM   689  O  O   . ASP   A 1 80  ? 30.696 -24.121 -11.761 1.00 34.96 ?  521  ASP   A O   1 
ATOM   690  C  CB  . ASP   A 1 80  ? 31.061 -27.275 -11.107 1.00 37.86 ?  521  ASP   A CB  1 
ATOM   691  C  CG  . ASP   A 1 80  ? 31.618 -28.611 -11.569 1.00 41.07 ?  521  ASP   A CG  1 
ATOM   692  O  OD1 . ASP   A 1 80  ? 32.015 -28.712 -12.749 1.00 41.71 ?  521  ASP   A OD1 1 
ATOM   693  O  OD2 . ASP   A 1 80  ? 31.676 -29.553 -10.751 1.00 42.97 -1 521  ASP   A OD2 1 
ATOM   694  N  N   . LEU   A 1 81  ? 31.674 -24.382 -9.747  1.00 30.35 ?  522  LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 81  ? 31.197 -23.091 -9.266  1.00 25.59 ?  522  LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 81  ? 31.881 -21.945 -9.999  1.00 23.60 ?  522  LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 81  ? 31.245 -20.926 -10.294 1.00 22.30 ?  522  LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 81  ? 31.425 -22.976 -7.760  1.00 23.05 ?  522  LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 81  ? 30.554 -23.855 -6.858  1.00 22.66 ?  522  LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 81  ? 31.096 -23.903 -5.431  1.00 23.29 ?  522  LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 81  ? 29.100 -23.381 -6.859  1.00 23.86 ?  522  LEU   A CD2 1 
ATOM   702  N  N   . ASN   A 1 82  ? 33.178 -22.086 -10.294 1.00 22.01 ?  523  ASN   A N   1 
ATOM   703  C  CA  . ASN   A 1 82  ? 33.873 -21.046 -11.044 1.00 24.93 ?  523  ASN   A CA  1 
ATOM   704  C  C   . ASN   A 1 82  ? 33.227 -20.850 -12.405 1.00 22.84 ?  523  ASN   A C   1 
ATOM   705  O  O   . ASN   A 1 82  ? 32.970 -19.714 -12.822 1.00 18.09 ?  523  ASN   A O   1 
ATOM   706  C  CB  . ASN   A 1 82  ? 35.355 -21.401 -11.196 1.00 32.20 ?  523  ASN   A CB  1 
ATOM   707  C  CG  . ASN   A 1 82  ? 36.254 -20.177 -11.184 1.00 39.58 ?  523  ASN   A CG  1 
ATOM   708  O  OD1 . ASN   A 1 82  ? 35.782 -19.045 -11.292 1.00 41.94 ?  523  ASN   A OD1 1 
ATOM   709  N  ND2 . ASN   A 1 82  ? 37.557 -20.399 -11.045 1.00 40.84 ?  523  ASN   A ND2 1 
ATOM   710  N  N   . ARG   A 1 83  ? 32.926 -21.952 -13.096 1.00 21.36 ?  524  ARG   A N   1 
ATOM   711  C  CA  . ARG   A 1 83  ? 32.293 -21.858 -14.407 1.00 23.16 ?  524  ARG   A CA  1 
ATOM   712  C  C   . ARG   A 1 83  ? 30.885 -21.289 -14.301 1.00 20.44 ?  524  ARG   A C   1 
ATOM   713  O  O   . ARG   A 1 83  ? 30.487 -20.450 -15.115 1.00 19.98 ?  524  ARG   A O   1 
ATOM   714  C  CB  . ARG   A 1 83  ? 32.258 -23.235 -15.065 1.00 27.87 ?  524  ARG   A CB  1 
ATOM   715  C  CG  . ARG   A 1 83  ? 33.460 -23.526 -15.940 1.00 33.89 ?  524  ARG   A CG  1 
ATOM   716  C  CD  . ARG   A 1 83  ? 33.692 -25.019 -16.079 1.00 39.40 ?  524  ARG   A CD  1 
ATOM   717  N  NE  . ARG   A 1 83  ? 34.435 -25.333 -17.295 1.00 42.50 ?  524  ARG   A NE  1 
ATOM   718  C  CZ  . ARG   A 1 83  ? 35.753 -25.208 -17.413 1.00 44.00 ?  524  ARG   A CZ  1 
ATOM   719  N  NH1 . ARG   A 1 83  ? 36.468 -24.765 -16.389 1.00 43.41 ?  524  ARG   A NH1 1 
ATOM   720  N  NH2 . ARG   A 1 83  ? 36.355 -25.520 -18.554 1.00 43.96 ?  524  ARG   A NH2 1 
ATOM   721  N  N   . LEU   A 1 84  ? 30.119 -21.718 -13.296 1.00 17.57 ?  525  LEU   A N   1 
ATOM   722  C  CA  . LEU   A 1 84  ? 28.746 -21.234 -13.175 1.00 17.57 ?  525  LEU   A CA  1 
ATOM   723  C  C   . LEU   A 1 84  ? 28.711 -19.733 -12.894 1.00 16.63 ?  525  LEU   A C   1 
ATOM   724  O  O   . LEU   A 1 84  ? 27.965 -18.986 -13.541 1.00 15.84 ?  525  LEU   A O   1 
ATOM   725  C  CB  . LEU   A 1 84  ? 27.998 -22.011 -12.094 1.00 19.58 ?  525  LEU   A CB  1 
ATOM   726  C  CG  . LEU   A 1 84  ? 26.580 -21.500 -11.828 1.00 19.17 ?  525  LEU   A CG  1 
ATOM   727  C  CD1 . LEU   A 1 84  ? 25.689 -21.605 -13.065 1.00 20.17 ?  525  LEU   A CD1 1 
ATOM   728  C  CD2 . LEU   A 1 84  ? 25.974 -22.262 -10.660 1.00 22.19 ?  525  LEU   A CD2 1 
ATOM   729  N  N   . GLY   A 1 85  ? 29.530 -19.268 -11.946 1.00 16.25 ?  526  GLY   A N   1 
ATOM   730  C  CA  . GLY   A 1 85  ? 29.572 -17.842 -11.663 1.00 15.99 ?  526  GLY   A CA  1 
ATOM   731  C  C   . GLY   A 1 85  ? 29.955 -17.024 -12.881 1.00 14.78 ?  526  GLY   A C   1 
ATOM   732  O  O   . GLY   A 1 85  ? 29.416 -15.940 -13.109 1.00 15.00 ?  526  GLY   A O   1 
ATOM   733  N  N   . ASP   A 1 86  ? 30.870 -17.549 -13.701 1.00 14.76 ?  527  ASP   A N   1 
ATOM   734  C  CA  . ASP   A 1 86  ? 31.327 -16.836 -14.889 1.00 18.10 ?  527  ASP   A CA  1 
ATOM   735  C  C   . ASP   A 1 86  ? 30.232 -16.686 -15.944 1.00 18.30 ?  527  ASP   A C   1 
ATOM   736  O  O   . ASP   A 1 86  ? 30.403 -15.899 -16.883 1.00 19.80 ?  527  ASP   A O   1 
ATOM   737  C  CB  . ASP   A 1 86  ? 32.574 -17.512 -15.488 1.00 18.61 ?  527  ASP   A CB  1 
ATOM   738  C  CG  . ASP   A 1 86  ? 33.847 -17.206 -14.702 1.00 23.25 ?  527  ASP   A CG  1 
ATOM   739  O  OD1 . ASP   A 1 86  ? 33.769 -16.495 -13.680 1.00 24.76 ?  527  ASP   A OD1 1 
ATOM   740  O  OD2 . ASP   A 1 86  ? 34.930 -17.683 -15.104 1.00 22.67 -1 527  ASP   A OD2 1 
ATOM   741  N  N   . GLU   A 1 87  ? 29.119 -17.418 -15.817 1.00 18.37 ?  528  GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 87  ? 27.987 -17.258 -16.727 1.00 18.25 ?  528  GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 87  ? 27.234 -15.950 -16.504 1.00 17.38 ?  528  GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 87  ? 26.467 -15.530 -17.379 1.00 18.44 ?  528  GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 87  ? 27.016 -18.434 -16.578 1.00 20.91 ?  528  GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 87  ? 27.608 -19.786 -16.954 1.00 27.98 ?  528  GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 87  ? 26.581 -20.906 -16.910 1.00 37.82 ?  528  GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 87  ? 25.400 -20.619 -16.613 1.00 40.46 ?  528  GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 87  ? 26.950 -22.070 -17.184 1.00 41.07 -1 528  GLU   A OE2 1 
ATOM   750  N  N   . TYR   A 1 88  ? 27.437 -15.296 -15.366 1.00 15.03 ?  529  TYR   A N   1 
ATOM   751  C  CA  . TYR   A 1 88  ? 26.770 -14.050 -15.024 1.00 14.22 ?  529  TYR   A CA  1 
ATOM   752  C  C   . TYR   A 1 88  ? 27.733 -12.882 -15.159 1.00 11.65 ?  529  TYR   A C   1 
ATOM   753  O  O   . TYR   A 1 88  ? 28.953 -13.052 -15.229 1.00 13.91 ?  529  TYR   A O   1 
ATOM   754  C  CB  . TYR   A 1 88  ? 26.239 -14.102 -13.587 1.00 13.26 ?  529  TYR   A CB  1 
ATOM   755  C  CG  . TYR   A 1 88  ? 25.315 -15.261 -13.323 1.00 11.98 ?  529  TYR   A CG  1 
ATOM   756  C  CD1 . TYR   A 1 88  ? 23.959 -15.178 -13.617 1.00 12.21 ?  529  TYR   A CD1 1 
ATOM   757  C  CD2 . TYR   A 1 88  ? 25.795 -16.436 -12.769 1.00 16.15 ?  529  TYR   A CD2 1 
ATOM   758  C  CE1 . TYR   A 1 88  ? 23.109 -16.251 -13.377 1.00 14.44 ?  529  TYR   A CE1 1 
ATOM   759  C  CE2 . TYR   A 1 88  ? 24.961 -17.507 -12.523 1.00 16.79 ?  529  TYR   A CE2 1 
ATOM   760  C  CZ  . TYR   A 1 88  ? 23.621 -17.412 -12.818 1.00 14.93 ?  529  TYR   A CZ  1 
ATOM   761  O  OH  . TYR   A 1 88  ? 22.809 -18.498 -12.559 1.00 17.56 ?  529  TYR   A OH  1 
ATOM   762  N  N   . ASN   A 1 89  ? 27.162 -11.681 -15.188 1.00 12.33 ?  530  ASN   A N   1 
ATOM   763  C  CA  . ASN   A 1 89  ? 27.940 -10.456 -15.069 1.00 13.06 ?  530  ASN   A CA  1 
ATOM   764  C  C   . ASN   A 1 89  ? 28.304 -10.254 -13.598 1.00 11.61 ?  530  ASN   A C   1 
ATOM   765  O  O   . ASN   A 1 89  ? 27.426 -9.976  -12.767 1.00 13.13 ?  530  ASN   A O   1 
ATOM   766  C  CB  . ASN   A 1 89  ? 27.109 -9.285  -15.591 1.00 13.22 ?  530  ASN   A CB  1 
ATOM   767  C  CG  . ASN   A 1 89  ? 27.870 -7.983  -15.612 1.00 14.68 ?  530  ASN   A CG  1 
ATOM   768  O  OD1 . ASN   A 1 89  ? 28.971 -7.882  -15.093 1.00 15.88 ?  530  ASN   A OD1 1 
ATOM   769  N  ND2 . ASN   A 1 89  ? 27.271 -6.967  -16.221 1.00 18.92 ?  530  ASN   A ND2 1 
ATOM   770  N  N   . SER   A 1 90  ? 29.593 -10.412 -13.278 1.00 12.49 ?  531  SER   A N   1 
ATOM   771  C  CA  . SER   A 1 90  ? 30.160 -10.027 -11.982 1.00 11.62 ?  531  SER   A CA  1 
ATOM   772  C  C   . SER   A 1 90  ? 29.538 -10.803 -10.811 1.00 12.02 ?  531  SER   A C   1 
ATOM   773  O  O   . SER   A 1 90  ? 28.979 -10.225 -9.878  1.00 11.91 ?  531  SER   A O   1 
ATOM   774  C  CB  . SER   A 1 90  ? 30.076 -8.506  -11.775 1.00 12.20 ?  531  SER   A CB  1 
ATOM   775  O  OG  . SER   A 1 90  ? 30.615 -7.817  -12.906 1.00 17.07 ?  531  SER   A OG  1 
ATOM   776  N  N   . ILE   A 1 91  ? 29.684 -12.128 -10.846 1.00 12.63 ?  532  ILE   A N   1 
ATOM   777  C  CA  . ILE   A 1 91  ? 29.197 -13.011 -9.785  1.00 11.41 ?  532  ILE   A CA  1 
ATOM   778  C  C   . ILE   A 1 91  ? 30.286 -14.020 -9.429  1.00 13.42 ?  532  ILE   A C   1 
ATOM   779  O  O   . ILE   A 1 91  ? 30.850 -14.669 -10.316 1.00 14.91 ?  532  ILE   A O   1 
ATOM   780  C  CB  . ILE   A 1 91  ? 27.908 -13.752 -10.201 1.00 11.20 ?  532  ILE   A CB  1 
ATOM   781  C  CG1 . ILE   A 1 91  ? 26.714 -12.798 -10.249 1.00 10.30 ?  532  ILE   A CG1 1 
ATOM   782  C  CG2 . ILE   A 1 91  ? 27.630 -14.945 -9.297  1.00 11.50 ?  532  ILE   A CG2 1 
ATOM   783  C  CD1 . ILE   A 1 91  ? 26.145 -12.437 -8.869  1.00 12.01 ?  532  ILE   A CD1 1 
ATOM   784  N  N   . PHE   A 1 92  ? 30.558 -14.173 -8.132  1.00 11.53 ?  533  PHE   A N   1 
ATOM   785  C  CA  . PHE   A 1 92  ? 31.262 -15.340 -7.620  1.00 12.60 ?  533  PHE   A CA  1 
ATOM   786  C  C   . PHE   A 1 92  ? 30.314 -16.137 -6.731  1.00 12.95 ?  533  PHE   A C   1 
ATOM   787  O  O   . PHE   A 1 92  ? 29.398 -15.578 -6.108  1.00 12.77 ?  533  PHE   A O   1 
ATOM   788  C  CB  . PHE   A 1 92  ? 32.539 -14.972 -6.847  1.00 12.30 ?  533  PHE   A CB  1 
ATOM   789  C  CG  . PHE   A 1 92  ? 32.282 -14.176 -5.597  1.00 11.87 ?  533  PHE   A CG  1 
ATOM   790  C  CD1 . PHE   A 1 92  ? 32.040 -14.811 -4.380  1.00 11.78 ?  533  PHE   A CD1 1 
ATOM   791  C  CD2 . PHE   A 1 92  ? 32.299 -12.787 -5.639  1.00 14.22 ?  533  PHE   A CD2 1 
ATOM   792  C  CE1 . PHE   A 1 92  ? 31.793 -14.063 -3.221  1.00 12.83 ?  533  PHE   A CE1 1 
ATOM   793  C  CE2 . PHE   A 1 92  ? 32.069 -12.040 -4.495  1.00 14.89 ?  533  PHE   A CE2 1 
ATOM   794  C  CZ  . PHE   A 1 92  ? 31.810 -12.673 -3.288  1.00 14.02 ?  533  PHE   A CZ  1 
ATOM   795  N  N   . ILE   A 1 93  ? 30.524 -17.454 -6.682  1.00 13.12 ?  534  ILE   A N   1 
ATOM   796  C  CA  . ILE   A 1 93  ? 29.647 -18.363 -5.949  1.00 13.78 ?  534  ILE   A CA  1 
ATOM   797  C  C   . ILE   A 1 93  ? 30.503 -19.344 -5.162  1.00 12.49 ?  534  ILE   A C   1 
ATOM   798  O  O   . ILE   A 1 93  ? 31.474 -19.896 -5.691  1.00 13.50 ?  534  ILE   A O   1 
ATOM   799  C  CB  . ILE   A 1 93  ? 28.690 -19.143 -6.878  1.00 12.89 ?  534  ILE   A CB  1 
ATOM   800  C  CG1 . ILE   A 1 93  ? 28.154 -18.231 -7.985  1.00 11.04 ?  534  ILE   A CG1 1 
ATOM   801  C  CG2 . ILE   A 1 93  ? 27.567 -19.793 -6.055  1.00 13.76 ?  534  ILE   A CG2 1 
ATOM   802  C  CD1 . ILE   A 1 93  ? 27.205 -18.929 -8.953  1.00 12.52 ?  534  ILE   A CD1 1 
ATOM   803  N  N   . SER   A 1 94  ? 30.134 -19.570 -3.904  1.00 12.90 ?  535  SER   A N   1 
ATOM   804  C  CA  . SER   A 1 94  ? 30.646 -20.659 -3.080  1.00 14.06 ?  535  SER   A CA  1 
ATOM   805  C  C   . SER   A 1 94  ? 29.460 -21.523 -2.660  1.00 13.95 ?  535  SER   A C   1 
ATOM   806  O  O   . SER   A 1 94  ? 28.308 -21.196 -2.930  1.00 13.83 ?  535  SER   A O   1 
ATOM   807  C  CB  . SER   A 1 94  ? 31.441 -20.137 -1.874  1.00 15.37 ?  535  SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 94  ? 30.611 -19.511 -0.901  1.00 16.01 ?  535  SER   A OG  1 
ATOM   809  N  N   . ASN   A 1 95  ? 29.733 -22.642 -1.986  1.00 15.95 ?  536  ASN   A N   1 
ATOM   810  C  CA  . ASN   A 1 95  ? 28.635 -23.549 -1.662  1.00 16.84 ?  536  ASN   A CA  1 
ATOM   811  C  C   . ASN   A 1 95  ? 27.679 -22.971 -0.627  1.00 15.90 ?  536  ASN   A C   1 
ATOM   812  O  O   . ASN   A 1 95  ? 26.583 -23.508 -0.456  1.00 18.35 ?  536  ASN   A O   1 
ATOM   813  C  CB  . ASN   A 1 95  ? 29.142 -24.923 -1.219  1.00 24.88 ?  536  ASN   A CB  1 
ATOM   814  C  CG  . ASN   A 1 95  ? 29.905 -24.873 0.093   1.00 33.32 ?  536  ASN   A CG  1 
ATOM   815  O  OD1 . ASN   A 1 95  ? 30.278 -23.803 0.575   1.00 38.17 ?  536  ASN   A OD1 1 
ATOM   816  N  ND2 . ASN   A 1 95  ? 30.140 -26.045 0.681   1.00 35.41 ?  536  ASN   A ND2 1 
ATOM   817  N  N   . GLU   A 1 96  ? 28.060 -21.893 0.056   1.00 14.73 ?  537  GLU   A N   1 
ATOM   818  C  CA  . GLU   A 1 96  ? 27.183 -21.239 1.015   1.00 14.42 ?  537  GLU   A CA  1 
ATOM   819  C  C   . GLU   A 1 96  ? 26.459 -20.026 0.445   1.00 12.94 ?  537  GLU   A C   1 
ATOM   820  O  O   . GLU   A 1 96  ? 25.682 -19.396 1.171   1.00 14.52 ?  537  GLU   A O   1 
ATOM   821  C  CB  . GLU   A 1 96  ? 27.962 -20.820 2.264   1.00 16.64 ?  537  GLU   A CB  1 
ATOM   822  C  CG  . GLU   A 1 96  ? 28.470 -21.987 3.108   1.00 21.71 ?  537  GLU   A CG  1 
ATOM   823  C  CD  . GLU   A 1 96  ? 27.377 -22.659 3.935   1.00 31.02 ?  537  GLU   A CD  1 
ATOM   824  O  OE1 . GLU   A 1 96  ? 26.187 -22.314 3.767   1.00 32.60 ?  537  GLU   A OE1 1 
ATOM   825  O  OE2 . GLU   A 1 96  ? 27.714 -23.536 4.761   1.00 34.33 -1 537  GLU   A OE2 1 
ATOM   826  N  N   . SER   A 1 97  ? 26.698 -19.669 -0.821  1.00 12.07 ?  538  SER   A N   1 
ATOM   827  C  CA  . SER   A 1 97  ? 26.117 -18.441 -1.361  1.00 13.00 ?  538  SER   A CA  1 
ATOM   828  C  C   . SER   A 1 97  ? 24.597 -18.463 -1.319  1.00 13.41 ?  538  SER   A C   1 
ATOM   829  O  O   . SER   A 1 97  ? 23.964 -17.481 -0.921  1.00 12.78 ?  538  SER   A O   1 
ATOM   830  C  CB  . SER   A 1 97  ? 26.611 -18.190 -2.781  1.00 12.68 ?  538  SER   A CB  1 
ATOM   831  O  OG  . SER   A 1 97  ? 28.010 -18.138 -2.817  1.00 13.89 ?  538  SER   A OG  1 
ATOM   832  N  N   . TYR   A 1 98  ? 23.991 -19.568 -1.750  1.00 12.34 ?  539  TYR   A N   1 
ATOM   833  C  CA  . TYR   A 1 98  ? 22.535 -19.649 -1.769  1.00 13.32 ?  539  TYR   A CA  1 
ATOM   834  C  C   . TYR   A 1 98  ? 21.952 -19.420 -0.378  1.00 12.98 ?  539  TYR   A C   1 
ATOM   835  O  O   . TYR   A 1 98  ? 21.032 -18.613 -0.203  1.00 12.59 ?  539  TYR   A O   1 
ATOM   836  C  CB  . TYR   A 1 98  ? 22.114 -21.013 -2.322  1.00 13.39 ?  539  TYR   A CB  1 
ATOM   837  C  CG  . TYR   A 1 98  ? 20.644 -21.317 -2.246  1.00 12.82 ?  539  TYR   A CG  1 
ATOM   838  C  CD1 . TYR   A 1 98  ? 19.727 -20.600 -2.992  1.00 13.88 ?  539  TYR   A CD1 1 
ATOM   839  C  CD2 . TYR   A 1 98  ? 20.177 -22.352 -1.443  1.00 14.45 ?  539  TYR   A CD2 1 
ATOM   840  C  CE1 . TYR   A 1 98  ? 18.379 -20.888 -2.935  1.00 14.32 ?  539  TYR   A CE1 1 
ATOM   841  C  CE2 . TYR   A 1 98  ? 18.829 -22.651 -1.378  1.00 15.31 ?  539  TYR   A CE2 1 
ATOM   842  C  CZ  . TYR   A 1 98  ? 17.938 -21.917 -2.128  1.00 15.86 ?  539  TYR   A CZ  1 
ATOM   843  O  OH  . TYR   A 1 98  ? 16.595 -22.195 -2.089  1.00 17.97 ?  539  TYR   A OH  1 
ATOM   844  N  N   . THR   A 1 99  ? 22.483 -20.120 0.626   1.00 12.05 ?  540  THR   A N   1 
ATOM   845  C  CA  . THR   A 1 99  ? 21.944 -19.976 1.972   1.00 13.34 ?  540  THR   A CA  1 
ATOM   846  C  C   . THR   A 1 99  ? 22.131 -18.556 2.487   1.00 11.55 ?  540  THR   A C   1 
ATOM   847  O  O   . THR   A 1 99  ? 21.240 -18.008 3.145   1.00 11.86 ?  540  THR   A O   1 
ATOM   848  C  CB  . THR   A 1 99  ? 22.599 -21.005 2.894   1.00 14.26 ?  540  THR   A CB  1 
ATOM   849  O  OG1 . THR   A 1 99  ? 22.267 -22.319 2.422   1.00 16.85 ?  540  THR   A OG1 1 
ATOM   850  C  CG2 . THR   A 1 99  ? 22.125 -20.843 4.348   1.00 12.87 ?  540  THR   A CG2 1 
ATOM   851  N  N   . CYS   A 1 100 ? 23.270 -17.930 2.177   1.00 11.52 ?  541  CYS   A N   1 
ATOM   852  C  CA  . CYS   A 1 100 ? 23.519 -16.584 2.670   1.00 11.82 ?  541  CYS   A CA  1 
ATOM   853  C  C   . CYS   A 1 100 ? 22.538 -15.609 2.038   1.00 12.41 ?  541  CYS   A C   1 
ATOM   854  O  O   . CYS   A 1 100 ? 22.007 -14.719 2.714   1.00 12.57 ?  541  CYS   A O   1 
ATOM   855  C  CB  . CYS   A 1 100 ? 24.953 -16.191 2.331   1.00 12.28 ?  541  CYS   A CB  1 
ATOM   856  S  SG  . CYS   A 1 100 ? 26.157 -16.975 3.416   1.00 14.94 ?  541  CYS   A SG  1 
ATOM   857  N  N   . ALA   A 1 101 ? 22.262 -15.781 0.742   1.00 10.49 ?  542  ALA   A N   1 
ATOM   858  C  CA  . ALA   A 1 101 ? 21.255 -14.967 0.076   1.00 11.37 ?  542  ALA   A CA  1 
ATOM   859  C  C   . ALA   A 1 101 ? 19.885 -15.163 0.717   1.00 9.91  ?  542  ALA   A C   1 
ATOM   860  O  O   . ALA   A 1 101 ? 19.124 -14.202 0.873   1.00 12.21 ?  542  ALA   A O   1 
ATOM   861  C  CB  . ALA   A 1 101 ? 21.204 -15.314 -1.414  1.00 12.02 ?  542  ALA   A CB  1 
ATOM   862  N  N   . LEU   A 1 102 ? 19.548 -16.404 1.094   1.00 11.42 ?  543  LEU   A N   1 
ATOM   863  C  CA  . LEU   A 1 102 ? 18.271 -16.658 1.761   1.00 11.36 ?  543  LEU   A CA  1 
ATOM   864  C  C   . LEU   A 1 102 ? 18.217 -15.964 3.116   1.00 11.57 ?  543  LEU   A C   1 
ATOM   865  O  O   . LEU   A 1 102 ? 17.177 -15.415 3.505   1.00 12.62 ?  543  LEU   A O   1 
ATOM   866  C  CB  . LEU   A 1 102 ? 18.063 -18.168 1.957   1.00 11.12 ?  543  LEU   A CB  1 
ATOM   867  C  CG  . LEU   A 1 102 ? 17.853 -19.072 0.743   1.00 14.00 ?  543  LEU   A CG  1 
ATOM   868  C  CD1 . LEU   A 1 102 ? 17.635 -20.520 1.203   1.00 15.12 ?  543  LEU   A CD1 1 
ATOM   869  C  CD2 . LEU   A 1 102 ? 16.674 -18.610 -0.048  1.00 14.13 ?  543  LEU   A CD2 1 
ATOM   870  N  N   . LEU   A 1 103 ? 19.330 -15.982 3.847   1.00 11.50 ?  544  LEU   A N   1 
ATOM   871  C  CA  . LEU   A 1 103 ? 19.392 -15.322 5.147   1.00 11.13 ?  544  LEU   A CA  1 
ATOM   872  C  C   . LEU   A 1 103 ? 19.278 -13.811 5.010   1.00 11.45 ?  544  LEU   A C   1 
ATOM   873  O  O   . LEU   A 1 103 ? 18.664 -13.155 5.860   1.00 12.28 ?  544  LEU   A O   1 
ATOM   874  C  CB  . LEU   A 1 103 ? 20.683 -15.690 5.869   1.00 13.63 ?  544  LEU   A CB  1 
ATOM   875  C  CG  . LEU   A 1 103 ? 20.771 -17.120 6.404   1.00 13.63 ?  544  LEU   A CG  1 
ATOM   876  C  CD1 . LEU   A 1 103 ? 22.191 -17.436 6.833   1.00 14.11 ?  544  LEU   A CD1 1 
ATOM   877  C  CD2 . LEU   A 1 103 ? 19.813 -17.325 7.563   1.00 14.29 ?  544  LEU   A CD2 1 
ATOM   878  N  N   . ALA   A 1 104 ? 19.883 -13.240 3.962   1.00 10.98 ?  545  ALA   A N   1 
ATOM   879  C  CA  . ALA   A 1 104 ? 19.786 -11.799 3.757   1.00 11.72 ?  545  ALA   A CA  1 
ATOM   880  C  C   . ALA   A 1 104 ? 18.332 -11.384 3.559   1.00 11.49 ?  545  ALA   A C   1 
ATOM   881  O  O   . ALA   A 1 104 ? 17.849 -10.442 4.196   1.00 12.29 ?  545  ALA   A O   1 
ATOM   882  C  CB  . ALA   A 1 104 ? 20.689 -11.366 2.594   1.00 12.07 ?  545  ALA   A CB  1 
ATOM   883  N  N   . ALA   A 1 105 ? 17.608 -12.114 2.704   1.00 11.84 ?  546  ALA   A N   1 
ATOM   884  C  CA  . ALA   A 1 105 ? 16.202 -11.816 2.462   1.00 9.68  ?  546  ALA   A CA  1 
ATOM   885  C  C   . ALA   A 1 105 ? 15.359 -12.072 3.713   1.00 11.60 ?  546  ALA   A C   1 
ATOM   886  O  O   . ALA   A 1 105 ? 14.556 -11.223 4.106   1.00 13.26 ?  546  ALA   A O   1 
ATOM   887  C  CB  . ALA   A 1 105 ? 15.707 -12.632 1.266   1.00 11.49 ?  546  ALA   A CB  1 
ATOM   888  N  N   . GLY   A 1 106 ? 15.533 -13.228 4.355   1.00 10.82 ?  547  GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 106 ? 14.709 -13.540 5.521   1.00 11.93 ?  547  GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 106 ? 14.912 -12.572 6.674   1.00 13.50 ?  547  GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 106 ? 13.968 -12.248 7.408   1.00 13.05 ?  547  GLY   A O   1 
ATOM   892  N  N   . SER   A 1 107 ? 16.152 -12.110 6.850   1.00 12.94 ?  548  SER   A N   1 
ATOM   893  C  CA  . SER   A 1 107 ? 16.461 -11.064 7.821   1.00 12.66 ?  548  SER   A CA  1 
ATOM   894  C  C   . SER   A 1 107 ? 15.628 -9.821  7.559   1.00 12.98 ?  548  SER   A C   1 
ATOM   895  O  O   . SER   A 1 107 ? 15.098 -9.200  8.488   1.00 13.36 ?  548  SER   A O   1 
ATOM   896  C  CB  . SER   A 1 107 ? 17.940 -10.688 7.701   1.00 12.31 ?  548  SER   A CB  1 
ATOM   897  O  OG  . SER   A 1 107 ? 18.792 -11.705 8.163   1.00 14.14 ?  548  SER   A OG  1 
ATOM   898  N  N   . CYS   A 1 108 ? 15.538 -9.418  6.292   1.00 11.45 ?  549  CYS   A N   1 
ATOM   899  C  CA  . CYS   A 1 108 ? 14.766 -8.236  5.960   1.00 11.01 ?  549  CYS   A CA  1 
ATOM   900  C  C   . CYS   A 1 108 ? 13.271 -8.471  6.091   1.00 11.41 ?  549  CYS   A C   1 
ATOM   901  O  O   . CYS   A 1 108 ? 12.546 -7.536  6.437   1.00 11.41 ?  549  CYS   A O   1 
ATOM   902  C  CB  . CYS   A 1 108 ? 15.150 -7.689  4.579   1.00 12.23 ?  549  CYS   A CB  1 
ATOM   903  S  SG  . CYS   A 1 108 ? 16.848 -7.101  4.522   1.00 11.05 ?  549  CYS   A SG  1 
ATOM   904  N  N   . PHE   A 1 109 ? 12.786 -9.688  5.806   1.00 10.92 ?  550  PHE   A N   1 
ATOM   905  C  CA  . PHE   A 1 109 ? 11.375 -9.971  6.048   1.00 10.85 ?  550  PHE   A CA  1 
ATOM   906  C  C   . PHE   A 1 109 ? 11.055 -9.843  7.532   1.00 11.32 ?  550  PHE   A C   1 
ATOM   907  O  O   . PHE   A 1 109 ? 10.055 -9.225  7.903   1.00 12.68 ?  550  PHE   A O   1 
ATOM   908  C  CB  . PHE   A 1 109 ? 10.987 -11.371 5.569   1.00 10.41 ?  550  PHE   A CB  1 
ATOM   909  C  CG  . PHE   A 1 109 ? 11.297 -11.662 4.120   1.00 11.33 ?  550  PHE   A CG  1 
ATOM   910  C  CD1 . PHE   A 1 109 ? 11.493 -10.653 3.183   1.00 11.93 ?  550  PHE   A CD1 1 
ATOM   911  C  CD2 . PHE   A 1 109 ? 11.337 -12.980 3.698   1.00 11.30 ?  550  PHE   A CD2 1 
ATOM   912  C  CE1 . PHE   A 1 109 ? 11.777 -10.965 1.846   1.00 13.06 ?  550  PHE   A CE1 1 
ATOM   913  C  CE2 . PHE   A 1 109 ? 11.607 -13.295 2.367   1.00 12.26 ?  550  PHE   A CE2 1 
ATOM   914  C  CZ  . PHE   A 1 109 ? 11.834 -12.288 1.451   1.00 12.76 ?  550  PHE   A CZ  1 
ATOM   915  N  N   . ASN   A 1 110 ? 11.880 -10.450 8.391   1.00 12.23 ?  551  ASN   A N   1 
ATOM   916  C  CA  . ASN   A 1 110 ? 11.644 -10.340 9.828   1.00 12.34 ?  551  ASN   A CA  1 
ATOM   917  C  C   . ASN   A 1 110 ? 11.651 -8.880  10.267  1.00 14.72 ?  551  ASN   A C   1 
ATOM   918  O  O   . ASN   A 1 110 ? 10.847 -8.477  11.115  1.00 13.04 ?  551  ASN   A O   1 
ATOM   919  C  CB  . ASN   A 1 110 ? 12.677 -11.159 10.613  1.00 13.48 ?  551  ASN   A CB  1 
ATOM   920  C  CG  . ASN   A 1 110 ? 12.343 -12.652 10.670  1.00 11.54 ?  551  ASN   A CG  1 
ATOM   921  O  OD1 . ASN   A 1 110 ? 11.259 -13.080 10.251  1.00 14.40 ?  551  ASN   A OD1 1 
ATOM   922  N  ND2 . ASN   A 1 110 ? 13.277 -13.444 11.181  1.00 13.24 ?  551  ASN   A ND2 1 
ATOM   923  N  N   . SER   A 1 111 ? 12.539 -8.067  9.689   1.00 11.82 ?  552  SER   A N   1 
ATOM   924  C  CA  . SER   A 1 111 ? 12.612 -6.652  10.052  1.00 12.16 ?  552  SER   A CA  1 
ATOM   925  C  C   . SER   A 1 111 ? 11.378 -5.892  9.585   1.00 13.00 ?  552  SER   A C   1 
ATOM   926  O  O   . SER   A 1 111 ? 10.801 -5.102  10.340  1.00 13.16 ?  552  SER   A O   1 
ATOM   927  C  CB  . SER   A 1 111 ? 13.884 -6.020  9.472   1.00 11.96 ?  552  SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 111 ? 15.041 -6.641  9.986   1.00 13.57 ?  552  SER   A OG  1 
ATOM   929  N  N   . ALA   A 1 112 ? 10.954 -6.120  8.344   1.00 11.87 ?  553  ALA   A N   1 
ATOM   930  C  CA  . ALA   A 1 112 ? 9.753  -5.459  7.849   1.00 9.50  ?  553  ALA   A CA  1 
ATOM   931  C  C   . ALA   A 1 112 ? 8.530  -5.858  8.669   1.00 12.05 ?  553  ALA   A C   1 
ATOM   932  O  O   . ALA   A 1 112 ? 7.673  -5.016  8.957   1.00 13.69 ?  553  ALA   A O   1 
ATOM   933  C  CB  . ALA   A 1 112 ? 9.552  -5.771  6.364   1.00 11.35 ?  553  ALA   A CB  1 
ATOM   934  N  N   . GLN   A 1 113 ? 8.425  -7.141  9.029   1.00 11.04 ?  554  GLN   A N   1 
ATOM   935  C  CA  . GLN   A 1 113 ? 7.324  -7.597  9.868   1.00 12.12 ?  554  GLN   A CA  1 
ATOM   936  C  C   . GLN   A 1 113 ? 7.329  -6.873  11.207  1.00 13.52 ?  554  GLN   A C   1 
ATOM   937  O  O   . GLN   A 1 113 ? 6.275  -6.449  11.691  1.00 14.34 ?  554  GLN   A O   1 
ATOM   938  C  CB  . GLN   A 1 113 ? 7.452  -9.102  10.085  1.00 14.07 ?  554  GLN   A CB  1 
ATOM   939  C  CG  . GLN   A 1 113 ? 6.358  -9.708  10.945  1.00 15.34 ?  554  GLN   A CG  1 
ATOM   940  C  CD  . GLN   A 1 113 ? 6.542  -11.199 11.099  1.00 17.79 ?  554  GLN   A CD  1 
ATOM   941  O  OE1 . GLN   A 1 113 ? 7.619  -11.669 11.460  1.00 21.34 ?  554  GLN   A OE1 1 
ATOM   942  N  NE2 . GLN   A 1 113 ? 5.489  -11.956 10.826  1.00 20.37 ?  554  GLN   A NE2 1 
ATOM   943  N  N   . ALA   A 1 114 ? 8.509  -6.715  11.816  1.00 12.43 ?  555  ALA   A N   1 
ATOM   944  C  CA  . ALA   A 1 114 ? 8.594  -6.033  13.103  1.00 12.75 ?  555  ALA   A CA  1 
ATOM   945  C  C   . ALA   A 1 114 ? 8.169  -4.575  12.974  1.00 13.53 ?  555  ALA   A C   1 
ATOM   946  O  O   . ALA   A 1 114 ? 7.501  -4.029  13.862  1.00 15.11 ?  555  ALA   A O   1 
ATOM   947  C  CB  . ALA   A 1 114 ? 10.014 -6.147  13.659  1.00 14.47 ?  555  ALA   A CB  1 
ATOM   948  N  N   . ILE   A 1 115 ? 8.529  -3.934  11.863  1.00 12.16 ?  556  ILE   A N   1 
ATOM   949  C  CA  . ILE   A 1 115 ? 8.122  -2.555  11.629  1.00 13.84 ?  556  ILE   A CA  1 
ATOM   950  C  C   . ILE   A 1 115 ? 6.614  -2.462  11.426  1.00 14.97 ?  556  ILE   A C   1 
ATOM   951  O  O   . ILE   A 1 115 ? 5.946  -1.590  12.001  1.00 15.42 ?  556  ILE   A O   1 
ATOM   952  C  CB  . ILE   A 1 115 ? 8.890  -1.992  10.425  1.00 14.00 ?  556  ILE   A CB  1 
ATOM   953  C  CG1 . ILE   A 1 115 ? 10.360 -1.818  10.779  1.00 12.90 ?  556  ILE   A CG1 1 
ATOM   954  C  CG2 . ILE   A 1 115 ? 8.304  -0.674  9.996   1.00 13.21 ?  556  ILE   A CG2 1 
ATOM   955  C  CD1 . ILE   A 1 115 ? 11.219 -1.526  9.569   1.00 14.78 ?  556  ILE   A CD1 1 
ATOM   956  N  N   . LEU   A 1 116 ? 6.052  -3.361  10.621  1.00 13.54 ?  557  LEU   A N   1 
ATOM   957  C  CA  . LEU   A 1 116 ? 4.655  -3.271  10.235  1.00 14.22 ?  557  LEU   A CA  1 
ATOM   958  C  C   . LEU   A 1 116 ? 3.698  -3.677  11.343  1.00 16.46 ?  557  LEU   A C   1 
ATOM   959  O  O   . LEU   A 1 116 ? 2.511  -3.352  11.256  1.00 21.62 ?  557  LEU   A O   1 
ATOM   960  C  CB  . LEU   A 1 116 ? 4.409  -4.119  8.985   1.00 14.47 ?  557  LEU   A CB  1 
ATOM   961  C  CG  . LEU   A 1 116 ? 5.107  -3.559  7.739   1.00 15.03 ?  557  LEU   A CG  1 
ATOM   962  C  CD1 . LEU   A 1 116 ? 5.107  -4.567  6.586   1.00 15.44 ?  557  LEU   A CD1 1 
ATOM   963  C  CD2 . LEU   A 1 116 ? 4.456  -2.265  7.311   1.00 15.03 ?  557  LEU   A CD2 1 
ATOM   964  N  N   . THR   A 1 117 ? 4.179  -4.387  12.354  1.00 14.63 ?  558  THR   A N   1 
ATOM   965  C  CA  . THR   A 1 117 ? 3.378  -4.698  13.528  1.00 14.22 ?  558  THR   A CA  1 
ATOM   966  C  C   . THR   A 1 117 ? 3.662  -3.756  14.684  1.00 17.08 ?  558  THR   A C   1 
ATOM   967  O  O   . THR   A 1 117 ? 3.020  -3.866  15.734  1.00 17.23 ?  558  THR   A O   1 
ATOM   968  C  CB  . THR   A 1 117 ? 3.603  -6.154  13.955  1.00 17.05 ?  558  THR   A CB  1 
ATOM   969  O  OG1 . THR   A 1 117 ? 4.992  -6.362  14.233  1.00 18.68 ?  558  THR   A OG1 1 
ATOM   970  C  CG2 . THR   A 1 117 ? 3.138  -7.114  12.874  1.00 17.29 ?  558  THR   A CG2 1 
ATOM   971  N  N   . GLY   A 1 118 ? 4.617  -2.844  14.529  1.00 18.17 ?  559  GLY   A N   1 
ATOM   972  C  CA  . GLY   A 1 118 ? 4.960  -1.929  15.597  1.00 20.31 ?  559  GLY   A CA  1 
ATOM   973  C  C   . GLY   A 1 118 ? 5.864  -2.494  16.668  1.00 19.29 ?  559  GLY   A C   1 
ATOM   974  O  O   . GLY   A 1 118 ? 6.062  -1.834  17.695  1.00 21.64 ?  559  GLY   A O   1 
ATOM   975  N  N   . GLN   A 1 119 ? 6.406  -3.701  16.482  1.00 16.97 ?  560  GLN   A N   1 
ATOM   976  C  CA  . GLN   A 1 119 ? 7.378  -4.228  17.437  1.00 17.64 ?  560  GLN   A CA  1 
ATOM   977  C  C   . GLN   A 1 119 ? 8.601  -3.321  17.525  1.00 20.23 ?  560  GLN   A C   1 
ATOM   978  O  O   . GLN   A 1 119 ? 9.206  -3.173  18.596  1.00 21.84 ?  560  GLN   A O   1 
ATOM   979  C  CB  . GLN   A 1 119 ? 7.787  -5.651  17.050  1.00 18.82 ?  560  GLN   A CB  1 
ATOM   980  C  CG  . GLN   A 1 119 ? 6.723  -6.721  17.297  1.00 20.37 ?  560  GLN   A CG  1 
ATOM   981  C  CD  . GLN   A 1 119 ? 6.488  -6.982  18.779  0.78 21.66 ?  560  GLN   A CD  1 
ATOM   982  O  OE1 . GLN   A 1 119 ? 7.430  -7.177  19.544  0.85 21.55 ?  560  GLN   A OE1 1 
ATOM   983  N  NE2 . GLN   A 1 119 ? 5.225  -6.994  19.184  0.94 20.75 ?  560  GLN   A NE2 1 
ATOM   984  N  N   . VAL   A 1 120 ? 8.995  -2.724  16.397  1.00 17.39 ?  561  VAL   A N   1 
ATOM   985  C  CA  . VAL   A 1 120 ? 10.011 -1.682  16.345  1.00 17.15 ?  561  VAL   A CA  1 
ATOM   986  C  C   . VAL   A 1 120 ? 9.472  -0.545  15.488  1.00 15.49 ?  561  VAL   A C   1 
ATOM   987  O  O   . VAL   A 1 120 ? 8.557  -0.725  14.680  1.00 17.02 ?  561  VAL   A O   1 
ATOM   988  C  CB  . VAL   A 1 120 ? 11.356 -2.191  15.775  1.00 14.23 ?  561  VAL   A CB  1 
ATOM   989  C  CG1 . VAL   A 1 120 ? 11.823 -3.411  16.528  1.00 15.44 ?  561  VAL   A CG1 1 
ATOM   990  C  CG2 . VAL   A 1 120 ? 11.237 -2.510  14.277  1.00 13.97 ?  561  VAL   A CG2 1 
ATOM   991  N  N   . ARG   A 1 121 ? 10.051 0.648   15.673  1.00 15.75 ?  562  ARG   A N   1 
ATOM   992  C  CA  . ARG   A 1 121 ? 9.656  1.772   14.832  1.00 17.34 ?  562  ARG   A CA  1 
ATOM   993  C  C   . ARG   A 1 121 ? 10.351 1.727   13.478  1.00 15.17 ?  562  ARG   A C   1 
ATOM   994  O  O   . ARG   A 1 121 ? 9.726  2.010   12.450  1.00 17.81 ?  562  ARG   A O   1 
ATOM   995  C  CB  . ARG   A 1 121 ? 9.954  3.111   15.506  1.00 21.30 ?  562  ARG   A CB  1 
ATOM   996  C  CG  . ARG   A 1 121 ? 9.508  4.295   14.652  1.00 28.58 ?  562  ARG   A CG  1 
ATOM   997  C  CD  . ARG   A 1 121 ? 9.580  5.621   15.397  1.00 35.08 ?  562  ARG   A CD  1 
ATOM   998  N  NE  . ARG   A 1 121 ? 10.422 6.604   14.717  1.00 37.24 ?  562  ARG   A NE  1 
ATOM   999  C  CZ  . ARG   A 1 121 ? 9.960  7.702   14.123  1.00 36.29 ?  562  ARG   A CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 121 ? 8.656  7.958   14.121  1.00 38.26 ?  562  ARG   A NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 121 ? 10.799 8.542   13.531  1.00 33.20 ?  562  ARG   A NH2 1 
ATOM   1002 N  N   . ASN   A 1 122 ? 11.641 1.393   13.472  1.00 13.71 ?  563  ASN   A N   1 
ATOM   1003 C  CA  . ASN   A 1 122 ? 12.467 1.382   12.270  1.00 11.18 ?  563  ASN   A CA  1 
ATOM   1004 C  C   . ASN   A 1 122 ? 13.529 0.312   12.484  1.00 10.95 ?  563  ASN   A C   1 
ATOM   1005 O  O   . ASN   A 1 122 ? 13.584 -0.314  13.543  1.00 11.21 ?  563  ASN   A O   1 
ATOM   1006 C  CB  . ASN   A 1 122 ? 13.030 2.783   12.029  1.00 11.28 ?  563  ASN   A CB  1 
ATOM   1007 C  CG  . ASN   A 1 122 ? 13.768 3.327   13.235  1.00 11.63 ?  563  ASN   A CG  1 
ATOM   1008 O  OD1 . ASN   A 1 122 ? 14.445 2.593   13.919  1.00 12.60 ?  563  ASN   A OD1 1 
ATOM   1009 N  ND2 . ASN   A 1 122 ? 13.640 4.618   13.479  1.00 12.89 ?  563  ASN   A ND2 1 
ATOM   1010 N  N   . ALA   A 1 123 ? 14.378 0.087   11.478  1.00 11.88 ?  564  ALA   A N   1 
ATOM   1011 C  CA  . ALA   A 1 123 ? 15.325 -1.010  11.611  1.00 12.18 ?  564  ALA   A CA  1 
ATOM   1012 C  C   . ALA   A 1 123 ? 16.446 -0.888  10.593  1.00 11.83 ?  564  ALA   A C   1 
ATOM   1013 O  O   . ALA   A 1 123 ? 16.317 -0.219  9.569   1.00 12.51 ?  564  ALA   A O   1 
ATOM   1014 C  CB  . ALA   A 1 123 ? 14.652 -2.381  11.500  1.00 11.79 ?  564  ALA   A CB  1 
ATOM   1015 N  N   A VAL   A 1 124 ? 17.548 -1.559  10.900  0.80 10.02 ?  565  VAL   A N   1 
ATOM   1016 N  N   B VAL   A 1 124 ? 17.561 -1.539  10.916  0.20 11.00 ?  565  VAL   A N   1 
ATOM   1017 C  CA  A VAL   A 1 124 ? 18.715 -1.625  10.035  0.80 11.33 ?  565  VAL   A CA  1 
ATOM   1018 C  CA  B VAL   A 1 124 ? 18.730 -1.637  10.054  0.20 11.32 ?  565  VAL   A CA  1 
ATOM   1019 C  C   A VAL   A 1 124 ? 19.074 -3.093  9.852   0.80 11.82 ?  565  VAL   A C   1 
ATOM   1020 C  C   B VAL   A 1 124 ? 19.027 -3.113  9.842   0.20 11.23 ?  565  VAL   A C   1 
ATOM   1021 O  O   A VAL   A 1 124 ? 19.062 -3.874  10.812  0.80 12.35 ?  565  VAL   A O   1 
ATOM   1022 O  O   B VAL   A 1 124 ? 18.930 -3.916  10.777  0.20 11.80 ?  565  VAL   A O   1 
ATOM   1023 C  CB  A VAL   A 1 124 ? 19.889 -0.797  10.608  0.80 11.37 ?  565  VAL   A CB  1 
ATOM   1024 C  CB  B VAL   A 1 124 ? 19.947 -0.915  10.672  0.20 11.71 ?  565  VAL   A CB  1 
ATOM   1025 C  CG1 A VAL   A 1 124 ? 20.358 -1.345  11.965  0.80 11.95 ?  565  VAL   A CG1 1 
ATOM   1026 C  CG1 B VAL   A 1 124 ? 21.256 -1.502  10.162  0.20 13.53 ?  565  VAL   A CG1 1 
ATOM   1027 C  CG2 A VAL   A 1 124 ? 21.037 -0.695  9.612   0.80 13.36 ?  565  VAL   A CG2 1 
ATOM   1028 C  CG2 B VAL   A 1 124 ? 19.889 0.558   10.363  0.20 10.65 ?  565  VAL   A CG2 1 
ATOM   1029 N  N   . ALA   A 1 125 ? 19.382 -3.470  8.611   1.00 10.68 ?  566  ALA   A N   1 
ATOM   1030 C  CA  . ALA   A 1 125 ? 19.701 -4.848  8.250   1.00 12.62 ?  566  ALA   A CA  1 
ATOM   1031 C  C   . ALA   A 1 125 ? 21.120 -4.896  7.698   1.00 10.72 ?  566  ALA   A C   1 
ATOM   1032 O  O   . ALA   A 1 125 ? 21.380 -4.392  6.594   1.00 10.47 ?  566  ALA   A O   1 
ATOM   1033 C  CB  . ALA   A 1 125 ? 18.691 -5.387  7.240   1.00 10.74 ?  566  ALA   A CB  1 
ATOM   1034 N  N   . ILE   A 1 126 ? 22.024 -5.502  8.470   1.00 11.98 ?  567  ILE   A N   1 
ATOM   1035 C  CA  . ILE   A 1 126 ? 23.443 -5.608  8.113   1.00 10.85 ?  567  ILE   A CA  1 
ATOM   1036 C  C   . ILE   A 1 126 ? 23.615 -6.961  7.424   1.00 12.41 ?  567  ILE   A C   1 
ATOM   1037 O  O   . ILE   A 1 126 ? 23.975 -7.968  8.046   1.00 12.58 ?  567  ILE   A O   1 
ATOM   1038 C  CB  . ILE   A 1 126 ? 24.354 -5.437  9.333   1.00 8.98  ?  567  ILE   A CB  1 
ATOM   1039 C  CG1 . ILE   A 1 126 ? 24.003 -4.149  10.089  1.00 12.53 ?  567  ILE   A CG1 1 
ATOM   1040 C  CG2 . ILE   A 1 126 ? 25.806 -5.464  8.874   1.00 10.35 ?  567  ILE   A CG2 1 
ATOM   1041 C  CD1 . ILE   A 1 126 ? 24.643 -4.048  11.491  1.00 12.49 ?  567  ILE   A CD1 1 
ATOM   1042 N  N   . VAL   A 1 127 ? 23.359 -6.986  6.109   1.00 11.51 ?  568  VAL   A N   1 
ATOM   1043 C  CA  . VAL   A 1 127 ? 23.200 -8.220  5.340   1.00 10.56 ?  568  VAL   A CA  1 
ATOM   1044 C  C   . VAL   A 1 127 ? 24.087 -8.239  4.101   1.00 9.69  ?  568  VAL   A C   1 
ATOM   1045 O  O   . VAL   A 1 127 ? 24.436 -7.195  3.540   1.00 9.66  ?  568  VAL   A O   1 
ATOM   1046 C  CB  . VAL   A 1 127 ? 21.726 -8.483  4.959   1.00 11.31 ?  568  VAL   A CB  1 
ATOM   1047 C  CG1 . VAL   A 1 127 ? 20.891 -8.643  6.227   1.00 12.30 ?  568  VAL   A CG1 1 
ATOM   1048 C  CG2 . VAL   A 1 127 ? 21.179 -7.368  4.077   1.00 11.77 ?  568  VAL   A CG2 1 
ATOM   1049 N  N   . ARG   A 1 128 ? 24.473 -9.450  3.709   1.00 10.03 ?  569  ARG   A N   1 
ATOM   1050 C  CA  . ARG   A 1 128 ? 25.132 -9.709  2.435   1.00 10.56 ?  569  ARG   A CA  1 
ATOM   1051 C  C   . ARG   A 1 128 ? 24.818 -11.149 2.046   1.00 10.48 ?  569  ARG   A C   1 
ATOM   1052 O  O   . ARG   A 1 128 ? 24.475 -11.963 2.909   1.00 11.74 ?  569  ARG   A O   1 
ATOM   1053 C  CB  . ARG   A 1 128 ? 26.659 -9.489  2.520   1.00 10.92 ?  569  ARG   A CB  1 
ATOM   1054 C  CG  . ARG   A 1 128 ? 27.413 -10.548 3.334   1.00 10.44 ?  569  ARG   A CG  1 
ATOM   1055 C  CD  . ARG   A 1 128 ? 28.891 -10.241 3.403   1.00 10.24 ?  569  ARG   A CD  1 
ATOM   1056 N  NE  . ARG   A 1 128 ? 29.633 -10.613 2.193   1.00 10.40 ?  569  ARG   A NE  1 
ATOM   1057 C  CZ  . ARG   A 1 128 ? 30.121 -11.829 1.947   1.00 10.82 ?  569  ARG   A CZ  1 
ATOM   1058 N  NH1 . ARG   A 1 128 ? 29.874 -12.834 2.784   1.00 11.84 ?  569  ARG   A NH1 1 
ATOM   1059 N  NH2 . ARG   A 1 128 ? 30.836 -12.042 0.844   1.00 11.12 ?  569  ARG   A NH2 1 
ATOM   1060 N  N   . PRO   A 1 129 ? 24.922 -11.501 0.751   1.00 10.26 ?  570  PRO   A N   1 
ATOM   1061 C  CA  . PRO   A 1 129 ? 25.254 -10.668 -0.409  1.00 10.20 ?  570  PRO   A CA  1 
ATOM   1062 C  C   . PRO   A 1 129 ? 24.153 -9.645  -0.704  1.00 9.61  ?  570  PRO   A C   1 
ATOM   1063 O  O   . PRO   A 1 129 ? 23.020 -9.786  -0.212  1.00 10.16 ?  570  PRO   A O   1 
ATOM   1064 C  CB  . PRO   A 1 129 ? 25.359 -11.688 -1.550  1.00 10.41 ?  570  PRO   A CB  1 
ATOM   1065 C  CG  . PRO   A 1 129 ? 24.445 -12.784 -1.152  1.00 11.14 ?  570  PRO   A CG  1 
ATOM   1066 C  CD  . PRO   A 1 129 ? 24.610 -12.890 0.360   1.00 10.50 ?  570  PRO   A CD  1 
ATOM   1067 N  N   . PRO   A 1 130 ? 24.501 -8.611  -1.453  1.00 10.02 ?  571  PRO   A N   1 
ATOM   1068 C  CA  . PRO   A 1 130 ? 23.528 -7.561  -1.790  1.00 9.68  ?  571  PRO   A CA  1 
ATOM   1069 C  C   . PRO   A 1 130 ? 22.481 -8.035  -2.780  1.00 9.18  ?  571  PRO   A C   1 
ATOM   1070 O  O   . PRO   A 1 130 ? 22.519 -9.187  -3.226  1.00 10.42 ?  571  PRO   A O   1 
ATOM   1071 C  CB  . PRO   A 1 130 ? 24.403 -6.469  -2.421  1.00 10.68 ?  571  PRO   A CB  1 
ATOM   1072 C  CG  . PRO   A 1 130 ? 25.591 -7.216  -2.963  1.00 9.61  ?  571  PRO   A CG  1 
ATOM   1073 C  CD  . PRO   A 1 130 ? 25.843 -8.335  -2.003  1.00 10.20 ?  571  PRO   A CD  1 
ATOM   1074 N  N   . GLY   A 1 131 ? 21.543 -7.155  -3.120  1.00 9.40  ?  572  GLY   A N   1 
ATOM   1075 C  CA  . GLY   A 1 131 ? 20.372 -7.568  -3.870  1.00 9.88  ?  572  GLY   A CA  1 
ATOM   1076 C  C   . GLY   A 1 131 ? 19.971 -6.778  -5.100  1.00 9.22  ?  572  GLY   A C   1 
ATOM   1077 O  O   . GLY   A 1 131 ? 19.345 -7.359  -5.982  1.00 9.75  ?  572  GLY   A O   1 
ATOM   1078 N  N   . HIS   A 1 132 ? 20.284 -5.483  -5.202  1.00 9.17  ?  573  HIS   A N   1 
ATOM   1079 C  CA  . HIS   A 1 132 ? 19.512 -4.642  -6.120  1.00 9.43  ?  573  HIS   A CA  1 
ATOM   1080 C  C   . HIS   A 1 132 ? 19.814 -4.859  -7.607  1.00 9.49  ?  573  HIS   A C   1 
ATOM   1081 O  O   . HIS   A 1 132 ? 19.025 -4.407  -8.448  1.00 10.34 ?  573  HIS   A O   1 
ATOM   1082 C  CB  . HIS   A 1 132 ? 19.589 -3.162  -5.734  1.00 9.65  ?  573  HIS   A CB  1 
ATOM   1083 C  CG  . HIS   A 1 132 ? 20.932 -2.533  -5.941  1.00 11.01 ?  573  HIS   A CG  1 
ATOM   1084 N  ND1 . HIS   A 1 132 ? 21.077 -1.183  -6.175  1.00 12.03 ?  573  HIS   A ND1 1 
ATOM   1085 C  CD2 . HIS   A 1 132 ? 22.184 -3.053  -5.948  1.00 12.71 ?  573  HIS   A CD2 1 
ATOM   1086 C  CE1 . HIS   A 1 132 ? 22.357 -0.897  -6.312  1.00 11.84 ?  573  HIS   A CE1 1 
ATOM   1087 N  NE2 . HIS   A 1 132 ? 23.052 -2.012  -6.171  1.00 12.17 ?  573  HIS   A NE2 1 
ATOM   1088 N  N   . HIS   A 1 133 ? 20.915 -5.525  -7.952  1.00 9.66  ?  574  HIS   A N   1 
ATOM   1089 C  CA  . HIS   A 1 133 ? 21.163 -5.869  -9.349  1.00 10.32 ?  574  HIS   A CA  1 
ATOM   1090 C  C   . HIS   A 1 133 ? 20.500 -7.170  -9.777  1.00 10.65 ?  574  HIS   A C   1 
ATOM   1091 O  O   . HIS   A 1 133 ? 20.503 -7.486  -10.983 1.00 11.65 ?  574  HIS   A O   1 
ATOM   1092 C  CB  . HIS   A 1 133 ? 22.659 -6.008  -9.604  1.00 11.50 ?  574  HIS   A CB  1 
ATOM   1093 C  CG  . HIS   A 1 133 ? 23.419 -4.728  -9.460  1.00 10.20 ?  574  HIS   A CG  1 
ATOM   1094 N  ND1 . HIS   A 1 133 ? 23.104 -3.589  -10.175 1.00 12.04 ?  574  HIS   A ND1 1 
ATOM   1095 C  CD2 . HIS   A 1 133 ? 24.482 -4.408  -8.685  1.00 11.68 ?  574  HIS   A CD2 1 
ATOM   1096 C  CE1 . HIS   A 1 133 ? 23.938 -2.621  -9.840  1.00 12.14 ?  574  HIS   A CE1 1 
ATOM   1097 N  NE2 . HIS   A 1 133 ? 24.798 -3.099  -8.959  1.00 12.35 ?  574  HIS   A NE2 1 
ATOM   1098 N  N   . ALA   A 1 134 ? 19.974 -7.948  -8.833  1.00 11.30 ?  575  ALA   A N   1 
ATOM   1099 C  CA  . ALA   A 1 134 ? 19.359 -9.222  -9.185  1.00 11.24 ?  575  ALA   A CA  1 
ATOM   1100 C  C   . ALA   A 1 134 ? 18.037 -8.985  -9.896  1.00 11.38 ?  575  ALA   A C   1 
ATOM   1101 O  O   . ALA   A 1 134 ? 17.211 -8.185  -9.445  1.00 11.78 ?  575  ALA   A O   1 
ATOM   1102 C  CB  . ALA   A 1 134 ? 19.152 -10.074 -7.934  1.00 10.82 ?  575  ALA   A CB  1 
ATOM   1103 N  N   . GLU   A 1 135 ? 17.857 -9.674  -11.020 1.00 11.61 ?  576  GLU   A N   1 
ATOM   1104 C  CA  . GLU   A 1 135 ? 16.659 -9.572  -11.839 1.00 12.58 ?  576  GLU   A CA  1 
ATOM   1105 C  C   . GLU   A 1 135 ? 15.724 -10.723 -11.517 1.00 12.95 ?  576  GLU   A C   1 
ATOM   1106 O  O   . GLU   A 1 135 ? 16.087 -11.656 -10.809 1.00 13.06 ?  576  GLU   A O   1 
ATOM   1107 C  CB  . GLU   A 1 135 ? 17.043 -9.653  -13.319 1.00 13.25 ?  576  GLU   A CB  1 
ATOM   1108 C  CG  . GLU   A 1 135 ? 17.999 -8.561  -13.774 1.00 14.95 ?  576  GLU   A CG  1 
ATOM   1109 C  CD  . GLU   A 1 135 ? 17.288 -7.274  -14.136 1.00 16.25 ?  576  GLU   A CD  1 
ATOM   1110 O  OE1 . GLU   A 1 135 ? 16.048 -7.226  -14.071 1.00 17.39 ?  576  GLU   A OE1 1 
ATOM   1111 O  OE2 . GLU   A 1 135 ? 17.984 -6.313  -14.517 1.00 18.67 -1 576  GLU   A OE2 1 
ATOM   1112 N  N   . LYS   A 1 136 ? 14.518 -10.674 -12.091 1.00 12.50 ?  577  LYS   A N   1 
ATOM   1113 C  CA  . LYS   A 1 136 ? 13.595 -11.795 -11.928 1.00 13.34 ?  577  LYS   A CA  1 
ATOM   1114 C  C   . LYS   A 1 136 ? 14.264 -13.128 -12.252 1.00 11.66 ?  577  LYS   A C   1 
ATOM   1115 O  O   . LYS   A 1 136 ? 14.159 -14.093 -11.485 1.00 11.39 ?  577  LYS   A O   1 
ATOM   1116 C  CB  . LYS   A 1 136 ? 12.362 -11.592 -12.809 1.00 15.98 ?  577  LYS   A CB  1 
ATOM   1117 C  CG  . LYS   A 1 136 ? 11.339 -12.714 -12.700 1.00 20.19 ?  577  LYS   A CG  1 
ATOM   1118 C  CD  . LYS   A 1 136 ? 10.132 -12.452 -13.591 1.00 26.19 ?  577  LYS   A CD  1 
ATOM   1119 C  CE  . LYS   A 1 136 ? 9.201  -13.656 -13.621 1.00 32.77 ?  577  LYS   A CE  1 
ATOM   1120 N  NZ  . LYS   A 1 136 ? 8.139  -13.521 -14.653 1.00 37.34 ?  577  LYS   A NZ  1 
ATOM   1121 N  N   . ASP   A 1 137 ? 14.990 -13.190 -13.368 1.00 12.07 ?  578  ASP   A N   1 
ATOM   1122 C  CA  . ASP   A 1 137 ? 15.477 -14.455 -13.905 1.00 12.39 ?  578  ASP   A CA  1 
ATOM   1123 C  C   . ASP   A 1 137 ? 16.998 -14.597 -13.886 1.00 11.91 ?  578  ASP   A C   1 
ATOM   1124 O  O   . ASP   A 1 137 ? 17.516 -15.564 -14.455 1.00 15.01 ?  578  ASP   A O   1 
ATOM   1125 C  CB  . ASP   A 1 137 ? 14.934 -14.652 -15.330 1.00 14.47 ?  578  ASP   A CB  1 
ATOM   1126 C  CG  . ASP   A 1 137 ? 15.206 -16.053 -15.898 1.00 16.06 ?  578  ASP   A CG  1 
ATOM   1127 O  OD1 . ASP   A 1 137 ? 14.873 -17.060 -15.231 1.00 15.80 ?  578  ASP   A OD1 1 
ATOM   1128 O  OD2 . ASP   A 1 137 ? 15.736 -16.146 -17.036 1.00 19.01 -1 578  ASP   A OD2 1 
ATOM   1129 N  N   . THR   A 1 138 ? 17.741 -13.698 -13.231 1.00 11.66 ?  579  THR   A N   1 
ATOM   1130 C  CA  . THR   A 1 138 ? 19.194 -13.876 -13.240 1.00 12.24 ?  579  THR   A CA  1 
ATOM   1131 C  C   . THR   A 1 138 ? 19.855 -13.110 -12.095 1.00 10.95 ?  579  THR   A C   1 
ATOM   1132 O  O   . THR   A 1 138 ? 19.283 -12.173 -11.530 1.00 11.42 ?  579  THR   A O   1 
ATOM   1133 C  CB  . THR   A 1 138 ? 19.815 -13.498 -14.602 1.00 13.25 ?  579  THR   A CB  1 
ATOM   1134 O  OG1 . THR   A 1 138 ? 21.093 -14.136 -14.753 1.00 15.57 ?  579  THR   A OG1 1 
ATOM   1135 C  CG2 . THR   A 1 138 ? 19.966 -11.999 -14.729 1.00 13.77 ?  579  THR   A CG2 1 
ATOM   1136 N  N   . ALA   A 1 139 ? 21.079 -13.528 -11.781 1.00 11.80 ?  580  ALA   A N   1 
ATOM   1137 C  CA  . ALA   A 1 139 ? 21.981 -12.876 -10.838 1.00 13.02 ?  580  ALA   A CA  1 
ATOM   1138 C  C   . ALA   A 1 139 ? 22.917 -11.919 -11.578 1.00 12.52 ?  580  ALA   A C   1 
ATOM   1139 O  O   . ALA   A 1 139 ? 23.195 -12.085 -12.772 1.00 12.95 ?  580  ALA   A O   1 
ATOM   1140 C  CB  . ALA   A 1 139 ? 22.819 -13.938 -10.123 1.00 11.78 ?  580  ALA   A CB  1 
ATOM   1141 N  N   . CYS   A 1 140 ? 23.424 -10.924 -10.849 1.00 11.18 ?  581  CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 140 ? 24.284 -9.918  -11.453 1.00 10.35 ?  581  CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 140 ? 24.907 -9.061  -10.361 1.00 10.04 ?  581  CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 140 ? 24.269 -8.772  -9.347  1.00 11.49 ?  581  CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 140 ? 23.466 -9.028  -12.393 1.00 13.68 ?  581  CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 140 ? 24.387 -7.684  -13.165 1.00 16.20 ?  581  CYS   A SG  1 
ATOM   1147 N  N   . GLY   A 1 141 ? 26.148 -8.632  -10.595 1.00 11.12 ?  582  GLY   A N   1 
ATOM   1148 C  CA  . GLY   A 1 141 ? 26.742 -7.595  -9.771  1.00 11.20 ?  582  GLY   A CA  1 
ATOM   1149 C  C   . GLY   A 1 141 ? 26.739 -7.901  -8.293  1.00 9.37  ?  582  GLY   A C   1 
ATOM   1150 O  O   . GLY   A 1 141 ? 26.348 -7.061  -7.486  1.00 9.99  ?  582  GLY   A O   1 
ATOM   1151 N  N   . PHE   A 1 142 ? 27.135 -9.122  -7.941  1.00 10.22 ?  583  PHE   A N   1 
ATOM   1152 C  CA  . PHE   A 1 142 ? 27.307 -9.615  -6.577  1.00 8.26  ?  583  PHE   A CA  1 
ATOM   1153 C  C   . PHE   A 1 142 ? 25.972 -9.977  -5.937  1.00 10.09 ?  583  PHE   A C   1 
ATOM   1154 O  O   . PHE   A 1 142 ? 25.960 -10.357 -4.767  1.00 10.94 ?  583  PHE   A O   1 
ATOM   1155 C  CB  . PHE   A 1 142 ? 28.062 -8.663  -5.628  1.00 10.68 ?  583  PHE   A CB  1 
ATOM   1156 C  CG  . PHE   A 1 142 ? 29.330 -8.057  -6.205  1.00 12.10 ?  583  PHE   A CG  1 
ATOM   1157 C  CD1 . PHE   A 1 142 ? 30.024 -8.653  -7.247  1.00 13.10 ?  583  PHE   A CD1 1 
ATOM   1158 C  CD2 . PHE   A 1 142 ? 29.817 -6.869  -5.680  1.00 13.75 ?  583  PHE   A CD2 1 
ATOM   1159 C  CE1 . PHE   A 1 142 ? 31.192 -8.065  -7.755  1.00 13.52 ?  583  PHE   A CE1 1 
ATOM   1160 C  CE2 . PHE   A 1 142 ? 30.974 -6.285  -6.170  1.00 12.91 ?  583  PHE   A CE2 1 
ATOM   1161 C  CZ  . PHE   A 1 142 ? 31.658 -6.891  -7.220  1.00 13.17 ?  583  PHE   A CZ  1 
ATOM   1162 N  N   . CYS   A 1 143 ? 24.863 -9.902  -6.668  1.00 10.99 ?  584  CYS   A N   1 
ATOM   1163 C  CA  . CYS   A 1 143 ? 23.521 -10.068 -6.123  1.00 10.61 ?  584  CYS   A CA  1 
ATOM   1164 C  C   . CYS   A 1 143 ? 22.863 -11.313 -6.701  1.00 9.74  ?  584  CYS   A C   1 
ATOM   1165 O  O   . CYS   A 1 143 ? 22.851 -11.507 -7.920  1.00 10.26 ?  584  CYS   A O   1 
ATOM   1166 C  CB  . CYS   A 1 143 ? 22.662 -8.870  -6.502  1.00 10.89 ?  584  CYS   A CB  1 
ATOM   1167 S  SG  . CYS   A 1 143 ? 23.279 -7.250  -5.984  1.00 22.14 ?  584  CYS   A SG  1 
ATOM   1168 N  N   . PHE   A 1 144 ? 22.277 -12.137 -5.828  1.00 10.11 ?  585  PHE   A N   1 
ATOM   1169 C  CA  . PHE   A 1 144 ? 21.578 -13.347 -6.256  1.00 11.08 ?  585  PHE   A CA  1 
ATOM   1170 C  C   . PHE   A 1 144 ? 20.067 -13.185 -6.296  1.00 10.91 ?  585  PHE   A C   1 
ATOM   1171 O  O   . PHE   A 1 144 ? 19.426 -13.562 -7.280  1.00 11.32 ?  585  PHE   A O   1 
ATOM   1172 C  CB  . PHE   A 1 144 ? 21.961 -14.515 -5.348  1.00 11.61 ?  585  PHE   A CB  1 
ATOM   1173 C  CG  . PHE   A 1 144 ? 23.397 -14.879 -5.449  1.00 11.47 ?  585  PHE   A CG  1 
ATOM   1174 C  CD1 . PHE   A 1 144 ? 23.838 -15.753 -6.426  1.00 12.31 ?  585  PHE   A CD1 1 
ATOM   1175 C  CD2 . PHE   A 1 144 ? 24.321 -14.328 -4.586  1.00 10.68 ?  585  PHE   A CD2 1 
ATOM   1176 C  CE1 . PHE   A 1 144 ? 25.180 -16.087 -6.520  1.00 13.06 ?  585  PHE   A CE1 1 
ATOM   1177 C  CE2 . PHE   A 1 144 ? 25.664 -14.650 -4.687  1.00 12.58 ?  585  PHE   A CE2 1 
ATOM   1178 C  CZ  . PHE   A 1 144 ? 26.086 -15.540 -5.650  1.00 12.15 ?  585  PHE   A CZ  1 
ATOM   1179 N  N   . PHE   A 1 145 ? 19.487 -12.654 -5.232  1.00 10.26 ?  586  PHE   A N   1 
ATOM   1180 C  CA  . PHE   A 1 145 ? 18.059 -12.415 -5.148  1.00 11.44 ?  586  PHE   A CA  1 
ATOM   1181 C  C   . PHE   A 1 145 ? 17.877 -10.978 -4.695  1.00 10.38 ?  586  PHE   A C   1 
ATOM   1182 O  O   . PHE   A 1 145 ? 18.720 -10.424 -3.976  1.00 11.35 ?  586  PHE   A O   1 
ATOM   1183 C  CB  . PHE   A 1 145 ? 17.387 -13.373 -4.134  1.00 10.51 ?  586  PHE   A CB  1 
ATOM   1184 C  CG  . PHE   A 1 145 ? 17.622 -14.837 -4.426  1.00 11.01 ?  586  PHE   A CG  1 
ATOM   1185 C  CD1 . PHE   A 1 145 ? 17.242 -15.391 -5.642  1.00 11.75 ?  586  PHE   A CD1 1 
ATOM   1186 C  CD2 . PHE   A 1 145 ? 18.195 -15.664 -3.478  1.00 13.18 ?  586  PHE   A CD2 1 
ATOM   1187 C  CE1 . PHE   A 1 145 ? 17.454 -16.739 -5.903  1.00 13.68 ?  586  PHE   A CE1 1 
ATOM   1188 C  CE2 . PHE   A 1 145 ? 18.401 -17.009 -3.741  1.00 14.06 ?  586  PHE   A CE2 1 
ATOM   1189 C  CZ  . PHE   A 1 145 ? 18.022 -17.546 -4.954  1.00 13.87 ?  586  PHE   A CZ  1 
ATOM   1190 N  N   . ASN   A 1 146 ? 16.789 -10.358 -5.138  1.00 9.28  ?  587  ASN   A N   1 
ATOM   1191 C  CA  . ASN   A 1 146 ? 16.643 -8.923  -4.918  1.00 9.54  ?  587  ASN   A CA  1 
ATOM   1192 C  C   . ASN   A 1 146 ? 15.974 -8.709  -3.567  1.00 11.14 ?  587  ASN   A C   1 
ATOM   1193 O  O   . ASN   A 1 146 ? 14.760 -8.558  -3.458  1.00 11.15 ?  587  ASN   A O   1 
ATOM   1194 C  CB  . ASN   A 1 146 ? 15.890 -8.244  -6.049  1.00 9.87  ?  587  ASN   A CB  1 
ATOM   1195 C  CG  . ASN   A 1 146 ? 16.033 -6.744  -6.001  1.00 10.90 ?  587  ASN   A CG  1 
ATOM   1196 O  OD1 . ASN   A 1 146 ? 15.937 -6.141  -4.936  1.00 11.58 ?  587  ASN   A OD1 1 
ATOM   1197 N  ND2 . ASN   A 1 146 ? 16.309 -6.133  -7.149  1.00 10.20 ?  587  ASN   A ND2 1 
ATOM   1198 N  N   . THR   A 1 147 ? 16.804 -8.656  -2.529  1.00 10.47 ?  588  THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 147 ? 16.338 -8.532  -1.148  1.00 10.12 ?  588  THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 147 ? 15.342 -7.393  -0.946  1.00 11.46 ?  588  THR   A C   1 
ATOM   1201 O  O   . THR   A 1 147 ? 14.276 -7.592  -0.355  1.00 11.72 ?  588  THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 147 ? 17.562 -8.337  -0.274  1.00 11.28 ?  588  THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 147 ? 18.396 -9.487  -0.418  1.00 11.87 ?  588  THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 147 ? 17.175 -8.135  1.188   1.00 12.80 ?  588  THR   A CG2 1 
ATOM   1205 N  N   . ALA   A 1 148 ? 15.659 -6.188  -1.430  1.00 11.07 ?  589  ALA   A N   1 
ATOM   1206 C  CA  . ALA   A 1 148 ? 14.740 -5.067  -1.212  1.00 11.32 ?  589  ALA   A CA  1 
ATOM   1207 C  C   . ALA   A 1 148 ? 13.417 -5.270  -1.940  1.00 10.81 ?  589  ALA   A C   1 
ATOM   1208 O  O   . ALA   A 1 148 ? 12.342 -5.015  -1.370  1.00 10.82 ?  589  ALA   A O   1 
ATOM   1209 C  CB  . ALA   A 1 148 ? 15.374 -3.734  -1.605  1.00 12.21 ?  589  ALA   A CB  1 
ATOM   1210 N  N   . ALA   A 1 149 ? 13.472 -5.743  -3.189  1.00 10.02 ?  590  ALA   A N   1 
ATOM   1211 C  CA  . ALA   A 1 149 ? 12.239 -5.988  -3.934  1.00 10.47 ?  590  ALA   A CA  1 
ATOM   1212 C  C   . ALA   A 1 149 ? 11.393 -7.058  -3.261  1.00 10.92 ?  590  ALA   A C   1 
ATOM   1213 O  O   . ALA   A 1 149 ? 10.172 -6.900  -3.122  1.00 12.01 ?  590  ALA   A O   1 
ATOM   1214 C  CB  . ALA   A 1 149 ? 12.564 -6.394  -5.376  1.00 10.62 ?  590  ALA   A CB  1 
ATOM   1215 N  N   . LEU   A 1 150 ? 12.037 -8.143  -2.812  1.00 11.22 ?  591  LEU   A N   1 
ATOM   1216 C  CA  . LEU   A 1 150 ? 11.337 -9.211  -2.106  1.00 9.13  ?  591  LEU   A CA  1 
ATOM   1217 C  C   . LEU   A 1 150 ? 10.717 -8.696  -0.812  1.00 12.20 ?  591  LEU   A C   1 
ATOM   1218 O  O   . LEU   A 1 150 ? 9.604  -9.099  -0.437  1.00 12.15 ?  591  LEU   A O   1 
ATOM   1219 C  CB  . LEU   A 1 150 ? 12.309 -10.354 -1.803  1.00 11.64 ?  591  LEU   A CB  1 
ATOM   1220 C  CG  . LEU   A 1 150 ? 12.769 -11.186 -2.996  1.00 10.22 ?  591  LEU   A CG  1 
ATOM   1221 C  CD1 . LEU   A 1 150 ? 13.963 -12.054 -2.636  1.00 13.88 ?  591  LEU   A CD1 1 
ATOM   1222 C  CD2 . LEU   A 1 150 ? 11.598 -12.024 -3.476  1.00 12.47 ?  591  LEU   A CD2 1 
ATOM   1223 N  N   . THR   A 1 151 ? 11.440 -7.829  -0.096  1.00 11.16 ?  592  THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 151 ? 10.910 -7.271  1.144   1.00 10.77 ?  592  THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 151 ? 9.662  -6.431  0.877   1.00 10.79 ?  592  THR   A C   1 
ATOM   1226 O  O   . THR   A 1 151 ? 8.699  -6.488  1.652   1.00 11.75 ?  592  THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 151 ? 12.001 -6.482  1.874   1.00 10.72 ?  592  THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 151 ? 13.063 -7.380  2.226   1.00 12.67 ?  592  THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 151 ? 11.437 -5.849  3.139   1.00 10.97 ?  592  THR   A CG2 1 
ATOM   1230 N  N   . ALA   A 1 152 ? 9.656  -5.642  -0.201  1.00 10.26 ?  593  ALA   A N   1 
ATOM   1231 C  CA  . ALA   A 1 152 ? 8.445  -4.909  -0.575  1.00 10.40 ?  593  ALA   A CA  1 
ATOM   1232 C  C   . ALA   A 1 152 ? 7.276  -5.865  -0.785  1.00 12.63 ?  593  ALA   A C   1 
ATOM   1233 O  O   . ALA   A 1 152 ? 6.181  -5.646  -0.255  1.00 12.81 ?  593  ALA   A O   1 
ATOM   1234 C  CB  . ALA   A 1 152 ? 8.686  -4.053  -1.825  1.00 12.47 ?  593  ALA   A CB  1 
ATOM   1235 N  N   . ARG   A 1 153 ? 7.489  -6.940  -1.547  1.00 13.74 ?  594  ARG   A N   1 
ATOM   1236 C  CA  . ARG   A 1 153 ? 6.401  -7.883  -1.799  1.00 15.32 ?  594  ARG   A CA  1 
ATOM   1237 C  C   . ARG   A 1 153 ? 6.007  -8.631  -0.528  1.00 12.90 ?  594  ARG   A C   1 
ATOM   1238 O  O   . ARG   A 1 153 ? 4.814  -8.877  -0.287  1.00 14.43 ?  594  ARG   A O   1 
ATOM   1239 C  CB  . ARG   A 1 153 ? 6.795  -8.870  -2.905  1.00 14.00 ?  594  ARG   A CB  1 
ATOM   1240 C  CG  . ARG   A 1 153 ? 6.950  -8.259  -4.289  1.00 16.85 ?  594  ARG   A CG  1 
ATOM   1241 C  CD  . ARG   A 1 153 ? 5.737  -7.441  -4.685  1.00 18.01 ?  594  ARG   A CD  1 
ATOM   1242 N  NE  . ARG   A 1 153 ? 5.728  -7.214  -6.129  1.00 16.58 ?  594  ARG   A NE  1 
ATOM   1243 C  CZ  . ARG   A 1 153 ? 4.988  -6.297  -6.733  1.00 17.79 ?  594  ARG   A CZ  1 
ATOM   1244 N  NH1 . ARG   A 1 153 ? 4.184  -5.514  -6.012  1.00 15.25 ?  594  ARG   A NH1 1 
ATOM   1245 N  NH2 . ARG   A 1 153 ? 5.061  -6.167  -8.056  1.00 19.54 ?  594  ARG   A NH2 1 
ATOM   1246 N  N   . TYR   A 1 154 ? 6.988  -8.996  0.305   1.00 11.76 ?  595  TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 154 ? 6.663  -9.645  1.575   1.00 13.90 ?  595  TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 154 ? 5.804  -8.735  2.447   1.00 13.44 ?  595  TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 154 ? 4.821  -9.183  3.060   1.00 13.29 ?  595  TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 154 ? 7.940  -10.050 2.316   1.00 12.90 ?  595  TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 154 ? 7.635  -10.520 3.721   1.00 13.88 ?  595  TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 154 ? 7.223  -11.826 3.970   1.00 15.33 ?  595  TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 154 ? 7.724  -9.642  4.796   1.00 13.80 ?  595  TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 154 ? 6.910  -12.246 5.272   1.00 15.24 ?  595  TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 154 ? 7.411  -10.045 6.083   1.00 15.33 ?  595  TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 154 ? 7.011  -11.346 6.315   1.00 15.99 ?  595  TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 154 ? 6.708  -11.738 7.607   1.00 16.03 ?  595  TYR   A OH  1 
ATOM   1258 N  N   . ALA   A 1 155 ? 6.159  -7.450  2.506   1.00 14.95 ?  596  ALA   A N   1 
ATOM   1259 C  CA  . ALA   A 1 155 ? 5.391  -6.482  3.282   1.00 12.79 ?  596  ALA   A CA  1 
ATOM   1260 C  C   . ALA   A 1 155 ? 3.949  -6.423  2.810   1.00 13.28 ?  596  ALA   A C   1 
ATOM   1261 O  O   . ALA   A 1 155 ? 3.015  -6.449  3.623   1.00 13.71 ?  596  ALA   A O   1 
ATOM   1262 C  CB  . ALA   A 1 155 ? 6.043  -5.105  3.175   1.00 12.57 ?  596  ALA   A CB  1 
ATOM   1263 N  N   . GLN   A 1 156 ? 3.750  -6.339  1.492   1.00 12.61 ?  597  GLN   A N   1 
ATOM   1264 C  CA  . GLN   A 1 156 ? 2.404  -6.358  0.932   1.00 13.64 ?  597  GLN   A CA  1 
ATOM   1265 C  C   . GLN   A 1 156 ? 1.661  -7.634  1.321   1.00 14.75 ?  597  GLN   A C   1 
ATOM   1266 O  O   . GLN   A 1 156 ? 0.464  -7.591  1.643   1.00 15.75 ?  597  GLN   A O   1 
ATOM   1267 C  CB  . GLN   A 1 156 ? 2.479  -6.162  -0.588  1.00 12.80 ?  597  GLN   A CB  1 
ATOM   1268 C  CG  . GLN   A 1 156 ? 2.753  -4.721  -0.955  1.00 12.12 ?  597  GLN   A CG  1 
ATOM   1269 C  CD  . GLN   A 1 156 ? 3.105  -4.503  -2.421  1.00 13.69 ?  597  GLN   A CD  1 
ATOM   1270 O  OE1 . GLN   A 1 156 ? 3.381  -5.446  -3.176  1.00 13.63 ?  597  GLN   A OE1 1 
ATOM   1271 N  NE2 . GLN   A 1 156 ? 3.078  -3.254  -2.833  1.00 15.14 ?  597  GLN   A NE2 1 
ATOM   1272 N  N   . SER   A 1 157 ? 2.362  -8.769  1.348   1.00 13.30 ?  598  SER   A N   1 
ATOM   1273 C  CA  . SER   A 1 157 ? 1.747  -10.058 1.650   1.00 14.82 ?  598  SER   A CA  1 
ATOM   1274 C  C   . SER   A 1 157 ? 1.226  -10.169 3.083   1.00 16.63 ?  598  SER   A C   1 
ATOM   1275 O  O   . SER   A 1 157 ? 0.342  -10.991 3.342   1.00 18.10 ?  598  SER   A O   1 
ATOM   1276 C  CB  . SER   A 1 157 ? 2.736  -11.186 1.319   1.00 14.85 ?  598  SER   A CB  1 
ATOM   1277 O  OG  . SER   A 1 157 ? 3.567  -11.497 2.423   1.00 15.65 ?  598  SER   A OG  1 
ATOM   1278 N  N   . ILE   A 1 158 ? 1.750  -9.381  4.021   1.00 15.16 ?  599  ILE   A N   1 
ATOM   1279 C  CA  . ILE   A 1 158 ? 1.310  -9.433  5.416   1.00 17.22 ?  599  ILE   A CA  1 
ATOM   1280 C  C   . ILE   A 1 158 ? 0.452  -8.250  5.816   1.00 16.56 ?  599  ILE   A C   1 
ATOM   1281 O  O   . ILE   A 1 158 ? 0.074  -8.141  6.997   1.00 17.79 ?  599  ILE   A O   1 
ATOM   1282 C  CB  . ILE   A 1 158 ? 2.475  -9.624  6.403   1.00 15.19 ?  599  ILE   A CB  1 
ATOM   1283 C  CG1 . ILE   A 1 158 ? 3.464  -8.451  6.339   1.00 17.09 ?  599  ILE   A CG1 1 
ATOM   1284 C  CG2 . ILE   A 1 158 ? 3.179  -10.947 6.152   1.00 17.83 ?  599  ILE   A CG2 1 
ATOM   1285 C  CD1 . ILE   A 1 158 ? 4.463  -8.444  7.504   1.00 17.53 ?  599  ILE   A CD1 1 
ATOM   1286 N  N   . THR   A 1 159 ? 0.148  -7.354  4.894   1.00 16.16 ?  600  THR   A N   1 
ATOM   1287 C  CA  . THR   A 1 159 ? -0.697 -6.207  5.177   1.00 17.24 ?  600  THR   A CA  1 
ATOM   1288 C  C   . THR   A 1 159 ? -1.839 -6.196  4.175   1.00 19.98 ?  600  THR   A C   1 
ATOM   1289 O  O   . THR   A 1 159 ? -2.885 -6.815  4.404   1.00 21.44 ?  600  THR   A O   1 
ATOM   1290 C  CB  . THR   A 1 159 ? 0.109  -4.898  5.146   1.00 16.21 ?  600  THR   A CB  1 
ATOM   1291 O  OG1 . THR   A 1 159 ? 0.816  -4.773  3.898   1.00 15.11 ?  600  THR   A OG1 1 
ATOM   1292 C  CG2 . THR   A 1 159 ? 1.104  -4.854  6.297   1.00 14.94 ?  600  THR   A CG2 1 
ATOM   1293 N  N   . ARG   A 1 160 ? -1.643 -5.507  3.059   1.00 18.21 ?  601  ARG   A N   1 
ATOM   1294 C  CA  . ARG   A 1 160 ? -2.556 -5.587  1.932   1.00 20.26 ?  601  ARG   A CA  1 
ATOM   1295 C  C   . ARG   A 1 160 ? -1.727 -5.464  0.664   1.00 19.51 ?  601  ARG   A C   1 
ATOM   1296 O  O   . ARG   A 1 160 ? -0.620 -4.915  0.677   1.00 19.28 ?  601  ARG   A O   1 
ATOM   1297 C  CB  . ARG   A 1 160 ? -3.653 -4.515  1.999   1.00 21.23 ?  601  ARG   A CB  1 
ATOM   1298 C  CG  . ARG   A 1 160 ? -3.138 -3.102  1.924   1.00 24.03 ?  601  ARG   A CG  1 
ATOM   1299 C  CD  . ARG   A 1 160 ? -4.256 -2.115  1.625   1.00 26.99 ?  601  ARG   A CD  1 
ATOM   1300 N  NE  . ARG   A 1 160 ? -3.756 -0.956  0.890   1.00 28.55 ?  601  ARG   A NE  1 
ATOM   1301 C  CZ  . ARG   A 1 160 ? -3.143 0.075   1.462   1.00 26.95 ?  601  ARG   A CZ  1 
ATOM   1302 N  NH1 . ARG   A 1 160 ? -2.970 0.091   2.771   1.00 25.10 ?  601  ARG   A NH1 1 
ATOM   1303 N  NH2 . ARG   A 1 160 ? -2.701 1.083   0.724   1.00 26.59 ?  601  ARG   A NH2 1 
ATOM   1304 N  N   . GLU   A 1 161 ? -2.263 -5.998  -0.437  1.00 19.51 ?  602  GLU   A N   1 
ATOM   1305 C  CA  . GLU   A 1 161 ? -1.475 -6.073  -1.666  1.00 22.63 ?  602  GLU   A CA  1 
ATOM   1306 C  C   . GLU   A 1 161 ? -1.079 -4.696  -2.187  1.00 19.87 ?  602  GLU   A C   1 
ATOM   1307 O  O   . GLU   A 1 161 ? -0.008 -4.549  -2.789  1.00 20.63 ?  602  GLU   A O   1 
ATOM   1308 C  CB  . GLU   A 1 161 ? -2.215 -6.875  -2.741  1.00 27.34 ?  602  GLU   A CB  1 
ATOM   1309 C  CG  . GLU   A 1 161 ? -2.342 -8.370  -2.444  1.00 33.77 ?  602  GLU   A CG  1 
ATOM   1310 C  CD  . GLU   A 1 161 ? -1.058 -8.990  -1.907  1.00 41.46 ?  602  GLU   A CD  1 
ATOM   1311 O  OE1 . GLU   A 1 161 ? -1.146 -9.821  -0.975  1.00 44.85 ?  602  GLU   A OE1 1 
ATOM   1312 O  OE2 . GLU   A 1 161 ? 0.037  -8.655  -2.413  1.00 43.96 -1 602  GLU   A OE2 1 
ATOM   1313 N  N   . SER   A 1 162 ? -1.908 -3.680  -1.963  1.00 17.83 ?  603  SER   A N   1 
ATOM   1314 C  CA  . SER   A 1 162 ? -1.639 -2.336  -2.459  1.00 18.72 ?  603  SER   A CA  1 
ATOM   1315 C  C   . SER   A 1 162 ? -0.885 -1.457  -1.461  1.00 17.87 ?  603  SER   A C   1 
ATOM   1316 O  O   . SER   A 1 162 ? -0.815 -0.238  -1.667  1.00 19.43 ?  603  SER   A O   1 
ATOM   1317 C  CB  . SER   A 1 162 ? -2.942 -1.657  -2.905  1.00 20.87 ?  603  SER   A CB  1 
ATOM   1318 O  OG  . SER   A 1 162 ? -3.828 -1.479  -1.819  1.00 23.96 ?  603  SER   A OG  1 
ATOM   1319 N  N   . LEU   A 1 163 ? -0.336 -2.035  -0.392  1.00 15.35 ?  604  LEU   A N   1 
ATOM   1320 C  CA  . LEU   A 1 163 ? 0.466  -1.255  0.546   1.00 16.55 ?  604  LEU   A CA  1 
ATOM   1321 C  C   . LEU   A 1 163 ? 1.529  -0.471  -0.212  1.00 16.71 ?  604  LEU   A C   1 
ATOM   1322 O  O   . LEU   A 1 163 ? 2.278  -1.034  -1.016  1.00 15.82 ?  604  LEU   A O   1 
ATOM   1323 C  CB  . LEU   A 1 163 ? 1.134  -2.185  1.558   1.00 16.61 ?  604  LEU   A CB  1 
ATOM   1324 C  CG  . LEU   A 1 163 ? 1.989  -1.480  2.624   1.00 16.94 ?  604  LEU   A CG  1 
ATOM   1325 C  CD1 . LEU   A 1 163 ? 1.114  -1.074  3.808   1.00 18.71 ?  604  LEU   A CD1 1 
ATOM   1326 C  CD2 . LEU   A 1 163 ? 3.145  -2.347  3.083   1.00 16.98 ?  604  LEU   A CD2 1 
ATOM   1327 N  N   . ARG   A 1 164 ? 1.575  0.840   0.025   1.00 14.47 ?  605  ARG   A N   1 
ATOM   1328 C  CA  . ARG   A 1 164 ? 2.492  1.706   -0.706  1.00 13.60 ?  605  ARG   A CA  1 
ATOM   1329 C  C   . ARG   A 1 164 ? 3.895  1.616   -0.106  1.00 13.79 ?  605  ARG   A C   1 
ATOM   1330 O  O   . ARG   A 1 164 ? 4.123  1.996   1.053   1.00 13.84 ?  605  ARG   A O   1 
ATOM   1331 C  CB  . ARG   A 1 164 ? 1.985  3.144   -0.722  1.00 16.62 ?  605  ARG   A CB  1 
ATOM   1332 C  CG  . ARG   A 1 164 ? 0.659  3.306   -1.458  1.00 18.41 ?  605  ARG   A CG  1 
ATOM   1333 C  CD  . ARG   A 1 164 ? 0.282  4.769   -1.597  1.00 20.00 ?  605  ARG   A CD  1 
ATOM   1334 N  NE  . ARG   A 1 164 ? 0.125  5.415   -0.297  1.00 18.77 ?  605  ARG   A NE  1 
ATOM   1335 C  CZ  . ARG   A 1 164 ? -0.946 5.306   0.482   1.00 21.60 ?  605  ARG   A CZ  1 
ATOM   1336 N  NH1 . ARG   A 1 164 ? -1.984 4.569   0.099   1.00 20.31 ?  605  ARG   A NH1 1 
ATOM   1337 N  NH2 . ARG   A 1 164 ? -0.973 5.936   1.648   1.00 23.71 ?  605  ARG   A NH2 1 
ATOM   1338 N  N   . VAL   A 1 165 ? 4.838  1.124   -0.899  1.00 12.95 ?  606  VAL   A N   1 
ATOM   1339 C  CA  . VAL   A 1 165 ? 6.219  0.957   -0.462  1.00 13.22 ?  606  VAL   A CA  1 
ATOM   1340 C  C   . VAL   A 1 165 ? 7.094  1.878   -1.291  1.00 11.28 ?  606  VAL   A C   1 
ATOM   1341 O  O   . VAL   A 1 165 ? 7.051  1.837   -2.526  1.00 12.85 ?  606  VAL   A O   1 
ATOM   1342 C  CB  . VAL   A 1 165 ? 6.696  -0.501  -0.599  1.00 13.81 ?  606  VAL   A CB  1 
ATOM   1343 C  CG1 . VAL   A 1 165 ? 8.144  -0.634  -0.120  1.00 11.96 ?  606  VAL   A CG1 1 
ATOM   1344 C  CG2 . VAL   A 1 165 ? 5.781  -1.452  0.171   1.00 14.49 ?  606  VAL   A CG2 1 
ATOM   1345 N  N   . LEU   A 1 166 ? 7.887  2.703   -0.615  1.00 12.13 ?  607  LEU   A N   1 
ATOM   1346 C  CA  . LEU   A 1 166 ? 8.909  3.498   -1.284  1.00 11.94 ?  607  LEU   A CA  1 
ATOM   1347 C  C   . LEU   A 1 166 ? 10.251 2.799   -1.115  1.00 11.07 ?  607  LEU   A C   1 
ATOM   1348 O  O   . LEU   A 1 166 ? 10.617 2.432   0.006   1.00 12.73 ?  607  LEU   A O   1 
ATOM   1349 C  CB  . LEU   A 1 166 ? 8.986  4.909   -0.698  1.00 13.12 ?  607  LEU   A CB  1 
ATOM   1350 C  CG  . LEU   A 1 166 ? 10.248 5.719   -1.044  1.00 13.20 ?  607  LEU   A CG  1 
ATOM   1351 C  CD1 . LEU   A 1 166 ? 10.314 6.012   -2.544  1.00 14.12 ?  607  LEU   A CD1 1 
ATOM   1352 C  CD2 . LEU   A 1 166 ? 10.306 7.004   -0.244  1.00 13.84 ?  607  LEU   A CD2 1 
ATOM   1353 N  N   . ILE   A 1 167 ? 10.968 2.599   -2.224  1.00 10.89 ?  608  ILE   A N   1 
ATOM   1354 C  CA  . ILE   A 1 167 ? 12.356 2.141   -2.191  1.00 10.98 ?  608  ILE   A CA  1 
ATOM   1355 C  C   . ILE   A 1 167 ? 13.236 3.290   -2.652  1.00 9.47  ?  608  ILE   A C   1 
ATOM   1356 O  O   . ILE   A 1 167 ? 13.141 3.733   -3.803  1.00 11.50 ?  608  ILE   A O   1 
ATOM   1357 C  CB  . ILE   A 1 167 ? 12.593 0.893   -3.056  1.00 10.62 ?  608  ILE   A CB  1 
ATOM   1358 C  CG1 . ILE   A 1 167 ? 11.671 -0.258  -2.634  1.00 12.95 ?  608  ILE   A CG1 1 
ATOM   1359 C  CG2 . ILE   A 1 167 ? 14.092 0.469   -2.993  1.00 10.36 ?  608  ILE   A CG2 1 
ATOM   1360 C  CD1 . ILE   A 1 167 ? 11.842 -1.526  -3.478  1.00 12.60 ?  608  ILE   A CD1 1 
ATOM   1361 N  N   . VAL   A 1 168 ? 14.094 3.772   -1.754  1.00 10.89 ?  609  VAL   A N   1 
ATOM   1362 C  CA  . VAL   A 1 168 ? 15.101 4.772   -2.082  1.00 11.16 ?  609  VAL   A CA  1 
ATOM   1363 C  C   . VAL   A 1 168 ? 16.426 4.042   -2.171  1.00 10.40 ?  609  VAL   A C   1 
ATOM   1364 O  O   . VAL   A 1 168 ? 16.848 3.398   -1.206  1.00 10.78 ?  609  VAL   A O   1 
ATOM   1365 C  CB  . VAL   A 1 168 ? 15.179 5.863   -1.007  1.00 12.34 ?  609  VAL   A CB  1 
ATOM   1366 C  CG1 . VAL   A 1 168 ? 16.322 6.809   -1.311  1.00 13.41 ?  609  VAL   A CG1 1 
ATOM   1367 C  CG2 . VAL   A 1 168 ? 13.879 6.621   -0.915  1.00 12.46 ?  609  VAL   A CG2 1 
ATOM   1368 N  N   . ASP   A 1 169 ? 17.079 4.136   -3.320  1.00 10.09 ?  610  ASP   A N   1 
ATOM   1369 C  CA  . ASP   A 1 169 ? 18.286 3.364   -3.610  1.00 10.50 ?  610  ASP   A CA  1 
ATOM   1370 C  C   . ASP   A 1 169 ? 19.431 4.356   -3.760  1.00 9.66  ?  610  ASP   A C   1 
ATOM   1371 O  O   . ASP   A 1 169 ? 19.559 5.025   -4.790  1.00 10.19 ?  610  ASP   A O   1 
ATOM   1372 C  CB  . ASP   A 1 169 ? 18.040 2.556   -4.887  1.00 10.22 ?  610  ASP   A CB  1 
ATOM   1373 C  CG  . ASP   A 1 169 ? 19.169 1.594   -5.223  1.00 10.64 ?  610  ASP   A CG  1 
ATOM   1374 O  OD1 . ASP   A 1 169 ? 20.326 1.849   -4.828  1.00 11.78 ?  610  ASP   A OD1 1 
ATOM   1375 O  OD2 . ASP   A 1 169 ? 18.908 0.564   -5.896  1.00 10.87 -1 610  ASP   A OD2 1 
ATOM   1376 N  N   . TRP   A 1 170 ? 20.245 4.499   -2.711  1.00 10.33 ?  611  TRP   A N   1 
ATOM   1377 C  CA  . TRP   A 1 170 ? 21.340 5.459   -2.742  1.00 10.02 ?  611  TRP   A CA  1 
ATOM   1378 C  C   . TRP   A 1 170 ? 22.700 4.803   -2.929  1.00 10.02 ?  611  TRP   A C   1 
ATOM   1379 O  O   . TRP   A 1 170 ? 23.729 5.481   -2.863  1.00 9.11  ?  611  TRP   A O   1 
ATOM   1380 C  CB  . TRP   A 1 170 ? 21.302 6.425   -1.555  1.00 10.44 ?  611  TRP   A CB  1 
ATOM   1381 C  CG  . TRP   A 1 170 ? 21.663 5.870   -0.184  1.00 10.50 ?  611  TRP   A CG  1 
ATOM   1382 C  CD1 . TRP   A 1 170 ? 22.676 5.001   0.119   1.00 10.38 ?  611  TRP   A CD1 1 
ATOM   1383 C  CD2 . TRP   A 1 170 ? 21.041 6.203   1.066   1.00 10.50 ?  611  TRP   A CD2 1 
ATOM   1384 N  NE1 . TRP   A 1 170 ? 22.724 4.772   1.477   1.00 9.82  ?  611  TRP   A NE1 1 
ATOM   1385 C  CE2 . TRP   A 1 170 ? 21.722 5.489   2.077   1.00 10.21 ?  611  TRP   A CE2 1 
ATOM   1386 C  CE3 . TRP   A 1 170 ? 19.967 7.029   1.432   1.00 11.28 ?  611  TRP   A CE3 1 
ATOM   1387 C  CZ2 . TRP   A 1 170 ? 21.368 5.577   3.415   1.00 11.58 ?  611  TRP   A CZ2 1 
ATOM   1388 C  CZ3 . TRP   A 1 170 ? 19.623 7.117   2.762   1.00 11.87 ?  611  TRP   A CZ3 1 
ATOM   1389 C  CH2 . TRP   A 1 170 ? 20.316 6.395   3.734   1.00 12.79 ?  611  TRP   A CH2 1 
ATOM   1390 N  N   . ASP   A 1 171 ? 22.723 3.501   -3.192  1.00 10.55 ?  612  ASP   A N   1 
ATOM   1391 C  CA  . ASP   A 1 171 ? 23.922 2.866   -3.718  1.00 9.28  ?  612  ASP   A CA  1 
ATOM   1392 C  C   . ASP   A 1 171 ? 24.348 3.624   -4.973  1.00 9.76  ?  612  ASP   A C   1 
ATOM   1393 O  O   . ASP   A 1 171 ? 23.505 4.154   -5.707  1.00 11.26 ?  612  ASP   A O   1 
ATOM   1394 C  CB  . ASP   A 1 171 ? 23.562 1.410   -4.016  1.00 9.40  ?  612  ASP   A CB  1 
ATOM   1395 C  CG  . ASP   A 1 171 ? 24.735 0.569   -4.402  1.00 12.02 ?  612  ASP   A CG  1 
ATOM   1396 O  OD1 . ASP   A 1 171 ? 25.249 0.718   -5.526  1.00 10.82 ?  612  ASP   A OD1 1 
ATOM   1397 O  OD2 . ASP   A 1 171 ? 25.138 -0.292  -3.579  1.00 12.32 -1 612  ASP   A OD2 1 
ATOM   1398 N  N   . VAL   A 1 172 ? 25.668 3.728   -5.190  1.00 9.85  ?  613  VAL   A N   1 
ATOM   1399 C  CA  . VAL   A 1 172 ? 26.196 4.521   -6.304  1.00 9.95  ?  613  VAL   A CA  1 
ATOM   1400 C  C   . VAL   A 1 172 ? 25.810 3.924   -7.651  1.00 9.78  ?  613  VAL   A C   1 
ATOM   1401 O  O   . VAL   A 1 172 ? 25.861 4.620   -8.671  1.00 10.39 ?  613  VAL   A O   1 
ATOM   1402 C  CB  . VAL   A 1 172 ? 27.731 4.670   -6.194  1.00 11.62 ?  613  VAL   A CB  1 
ATOM   1403 C  CG1 . VAL   A 1 172 ? 28.406 3.404   -6.680  1.00 9.81  ?  613  VAL   A CG1 1 
ATOM   1404 C  CG2 . VAL   A 1 172 ? 28.230 5.884   -6.961  1.00 11.44 ?  613  VAL   A CG2 1 
ATOM   1405 N  N   . HIS   A 1 173 ? 25.429 2.649   -7.684  1.00 11.17 ?  614  HIS   A N   1 
ATOM   1406 C  CA  . HIS   A 1 173 ? 25.021 1.975   -8.911  1.00 10.33 ?  614  HIS   A CA  1 
ATOM   1407 C  C   . HIS   A 1 173 ? 23.504 1.953   -9.041  1.00 10.48 ?  614  HIS   A C   1 
ATOM   1408 O  O   . HIS   A 1 173 ? 22.777 1.912   -8.051  1.00 9.66  ?  614  HIS   A O   1 
ATOM   1409 C  CB  . HIS   A 1 173 ? 25.526 0.531   -8.923  1.00 9.35  ?  614  HIS   A CB  1 
ATOM   1410 C  CG  . HIS   A 1 173 ? 27.001 0.411   -8.796  1.00 8.80  ?  614  HIS   A CG  1 
ATOM   1411 N  ND1 . HIS   A 1 173 ? 27.630 0.076   -7.605  1.00 9.05  ?  614  HIS   A ND1 1 
ATOM   1412 C  CD2 . HIS   A 1 173 ? 27.979 0.611   -9.713  1.00 10.95 ?  614  HIS   A CD2 1 
ATOM   1413 C  CE1 . HIS   A 1 173 ? 28.940 0.062   -7.818  1.00 11.65 ?  614  HIS   A CE1 1 
ATOM   1414 N  NE2 . HIS   A 1 173 ? 29.174 0.378   -9.083  1.00 10.89 ?  614  HIS   A NE2 1 
ATOM   1415 N  N   . HIS   A 1 174 ? 23.031 1.978   -10.281 1.00 11.70 ?  615  HIS   A N   1 
ATOM   1416 C  CA  . HIS   A 1 174 ? 21.610 1.811   -10.552 1.00 10.14 ?  615  HIS   A CA  1 
ATOM   1417 C  C   . HIS   A 1 174 ? 21.140 0.422   -10.131 1.00 9.26  ?  615  HIS   A C   1 
ATOM   1418 O  O   . HIS   A 1 174 ? 21.780 -0.584  -10.454 1.00 10.23 ?  615  HIS   A O   1 
ATOM   1419 C  CB  . HIS   A 1 174 ? 21.352 1.994   -12.043 1.00 9.66  ?  615  HIS   A CB  1 
ATOM   1420 C  CG  . HIS   A 1 174 ? 19.900 2.009   -12.391 1.00 10.14 ?  615  HIS   A CG  1 
ATOM   1421 N  ND1 . HIS   A 1 174 ? 19.354 1.184   -13.352 1.00 12.39 ?  615  HIS   A ND1 1 
ATOM   1422 C  CD2 . HIS   A 1 174 ? 18.874 2.731   -11.884 1.00 10.25 ?  615  HIS   A CD2 1 
ATOM   1423 C  CE1 . HIS   A 1 174 ? 18.054 1.410   -13.425 1.00 11.76 ?  615  HIS   A CE1 1 
ATOM   1424 N  NE2 . HIS   A 1 174 ? 17.738 2.351   -12.552 1.00 11.24 ?  615  HIS   A NE2 1 
ATOM   1425 N  N   . GLY   A 1 175 ? 20.016 0.361   -9.411  1.00 10.09 ?  616  GLY   A N   1 
ATOM   1426 C  CA  . GLY   A 1 175 ? 19.421 -0.919  -9.076  1.00 9.42  ?  616  GLY   A CA  1 
ATOM   1427 C  C   . GLY   A 1 175 ? 18.570 -1.422  -10.218 1.00 10.73 ?  616  GLY   A C   1 
ATOM   1428 O  O   . GLY   A 1 175 ? 17.336 -1.369  -10.170 1.00 12.07 ?  616  GLY   A O   1 
ATOM   1429 N  N   . ASN   A 1 176 ? 19.239 -1.897  -11.268 1.00 10.39 ?  617  ASN   A N   1 
ATOM   1430 C  CA  . ASN   A 1 176 ? 18.524 -2.328  -12.469 1.00 10.81 ?  617  ASN   A CA  1 
ATOM   1431 C  C   . ASN   A 1 176 ? 17.467 -3.376  -12.147 1.00 11.53 ?  617  ASN   A C   1 
ATOM   1432 O  O   . ASN   A 1 176 ? 16.372 -3.351  -12.714 1.00 11.71 ?  617  ASN   A O   1 
ATOM   1433 C  CB  . ASN   A 1 176 ? 19.518 -2.868  -13.497 1.00 12.83 ?  617  ASN   A CB  1 
ATOM   1434 C  CG  . ASN   A 1 176 ? 20.385 -3.957  -12.927 1.00 20.31 ?  617  ASN   A CG  1 
ATOM   1435 O  OD1 . ASN   A 1 176 ? 21.324 -3.675  -12.203 1.00 15.94 ?  617  ASN   A OD1 1 
ATOM   1436 N  ND2 . ASN   A 1 176 ? 20.061 -5.210  -13.225 1.00 24.01 ?  617  ASN   A ND2 1 
ATOM   1437 N  N   . GLY   A 1 177 ? 17.781 -4.314  -11.259 1.00 10.03 ?  618  GLY   A N   1 
ATOM   1438 C  CA  . GLY   A 1 177 ? 16.823 -5.357  -10.943 1.00 11.02 ?  618  GLY   A CA  1 
ATOM   1439 C  C   . GLY   A 1 177 ? 15.579 -4.805  -10.288 1.00 10.99 ?  618  GLY   A C   1 
ATOM   1440 O  O   . GLY   A 1 177 ? 14.458 -5.201  -10.621 1.00 10.26 ?  618  GLY   A O   1 
ATOM   1441 N  N   . THR   A 1 178 ? 15.757 -3.870  -9.354  1.00 11.01 ?  619  THR   A N   1 
ATOM   1442 C  CA  . THR   A 1 178 ? 14.608 -3.286  -8.675  1.00 10.08 ?  619  THR   A CA  1 
ATOM   1443 C  C   . THR   A 1 178 ? 13.747 -2.493  -9.643  1.00 8.89  ?  619  THR   A C   1 
ATOM   1444 O  O   . THR   A 1 178 ? 12.511 -2.624  -9.652  1.00 11.46 ?  619  THR   A O   1 
ATOM   1445 C  CB  . THR   A 1 178 ? 15.087 -2.406  -7.518  1.00 9.50  ?  619  THR   A CB  1 
ATOM   1446 O  OG1 . THR   A 1 178 ? 16.049 -3.144  -6.745  1.00 11.00 ?  619  THR   A OG1 1 
ATOM   1447 C  CG2 . THR   A 1 178 ? 13.924 -1.999  -6.641  1.00 11.98 ?  619  THR   A CG2 1 
ATOM   1448 N  N   . GLN   A 1 179 ? 14.377 -1.676  -10.475 1.00 10.27 ?  620  GLN   A N   1 
ATOM   1449 C  CA  . GLN   A 1 179 ? 13.625 -0.959  -11.496 1.00 11.37 ?  620  GLN   A CA  1 
ATOM   1450 C  C   . GLN   A 1 179 ? 12.802 -1.918  -12.346 1.00 11.49 ?  620  GLN   A C   1 
ATOM   1451 O  O   . GLN   A 1 179 ? 11.596 -1.717  -12.539 1.00 11.51 ?  620  GLN   A O   1 
ATOM   1452 C  CB  . GLN   A 1 179 ? 14.571 -0.164  -12.386 1.00 11.15 ?  620  GLN   A CB  1 
ATOM   1453 C  CG  . GLN   A 1 179 ? 13.875 0.321   -13.660 1.00 10.98 ?  620  GLN   A CG  1 
ATOM   1454 C  CD  . GLN   A 1 179 ? 14.674 1.383   -14.377 1.00 11.83 ?  620  GLN   A CD  1 
ATOM   1455 O  OE1 . GLN   A 1 179 ? 15.200 2.297   -13.750 1.00 12.80 ?  620  GLN   A OE1 1 
ATOM   1456 N  NE2 . GLN   A 1 179 ? 14.761 1.283   -15.697 1.00 14.84 ?  620  GLN   A NE2 1 
ATOM   1457 N  N   . HIS   A 1 180 ? 13.433 -2.983  -12.848 1.00 10.89 ?  621  HIS   A N   1 
ATOM   1458 C  CA  . HIS   A 1 180 ? 12.718 -3.863  -13.770 1.00 11.20 ?  621  HIS   A CA  1 
ATOM   1459 C  C   . HIS   A 1 180 ? 11.591 -4.619  -13.065 1.00 12.59 ?  621  HIS   A C   1 
ATOM   1460 O  O   . HIS   A 1 180 ? 10.496 -4.783  -13.621 1.00 13.25 ?  621  HIS   A O   1 
ATOM   1461 C  CB  . HIS   A 1 180 ? 13.699 -4.808  -14.463 1.00 12.98 ?  621  HIS   A CB  1 
ATOM   1462 C  CG  . HIS   A 1 180 ? 14.627 -4.112  -15.407 1.00 13.80 ?  621  HIS   A CG  1 
ATOM   1463 N  ND1 . HIS   A 1 180 ? 15.940 -4.494  -15.576 1.00 13.66 ?  621  HIS   A ND1 1 
ATOM   1464 C  CD2 . HIS   A 1 180 ? 14.432 -3.055  -16.233 1.00 15.19 ?  621  HIS   A CD2 1 
ATOM   1465 C  CE1 . HIS   A 1 180 ? 16.515 -3.703  -16.466 1.00 16.59 ?  621  HIS   A CE1 1 
ATOM   1466 N  NE2 . HIS   A 1 180 ? 15.623 -2.818  -16.875 1.00 17.63 ?  621  HIS   A NE2 1 
ATOM   1467 N  N   . ILE   A 1 181 ? 11.830 -5.078  -11.838 1.00 11.36 ?  622  ILE   A N   1 
ATOM   1468 C  CA  . ILE   A 1 181 ? 10.813 -5.837  -11.110 1.00 11.89 ?  622  ILE   A CA  1 
ATOM   1469 C  C   . ILE   A 1 181 ? 9.546  -5.013  -10.932 1.00 11.24 ?  622  ILE   A C   1 
ATOM   1470 O  O   . ILE   A 1 181 ? 8.425  -5.518  -11.089 1.00 13.17 ?  622  ILE   A O   1 
ATOM   1471 C  CB  . ILE   A 1 181 ? 11.368 -6.353  -9.764  1.00 11.42 ?  622  ILE   A CB  1 
ATOM   1472 C  CG1 . ILE   A 1 181 ? 12.322 -7.529  -10.024 1.00 12.18 ?  622  ILE   A CG1 1 
ATOM   1473 C  CG2 . ILE   A 1 181 ? 10.225 -6.738  -8.800  1.00 12.26 ?  622  ILE   A CG2 1 
ATOM   1474 C  CD1 . ILE   A 1 181 ? 13.200 -7.918  -8.843  1.00 12.01 ?  622  ILE   A CD1 1 
ATOM   1475 N  N   . PHE   A 1 182 ? 9.697  -3.730  -10.642 1.00 10.47 ?  623  PHE   A N   1 
ATOM   1476 C  CA  . PHE   A 1 182 ? 8.556  -2.878  -10.333 1.00 10.21 ?  623  PHE   A CA  1 
ATOM   1477 C  C   . PHE   A 1 182 ? 8.195  -1.920  -11.460 1.00 10.78 ?  623  PHE   A C   1 
ATOM   1478 O  O   . PHE   A 1 182 ? 7.386  -1.008  -11.235 1.00 11.79 ?  623  PHE   A O   1 
ATOM   1479 C  CB  . PHE   A 1 182 ? 8.824  -2.102  -9.040  1.00 11.54 ?  623  PHE   A CB  1 
ATOM   1480 C  CG  . PHE   A 1 182 ? 8.991  -2.980  -7.845  1.00 11.68 ?  623  PHE   A CG  1 
ATOM   1481 C  CD1 . PHE   A 1 182 ? 7.930  -3.738  -7.374  1.00 12.71 ?  623  PHE   A CD1 1 
ATOM   1482 C  CD2 . PHE   A 1 182 ? 10.211 -3.049  -7.188  1.00 10.80 ?  623  PHE   A CD2 1 
ATOM   1483 C  CE1 . PHE   A 1 182 ? 8.084  -4.567  -6.267  1.00 11.83 ?  623  PHE   A CE1 1 
ATOM   1484 C  CE2 . PHE   A 1 182 ? 10.371 -3.862  -6.095  1.00 10.68 ?  623  PHE   A CE2 1 
ATOM   1485 C  CZ  . PHE   A 1 182 ? 9.311  -4.614  -5.614  1.00 10.88 ?  623  PHE   A CZ  1 
ATOM   1486 N  N   . GLU   A 1 183 ? 8.736  -2.124  -12.668 1.00 12.14 ?  624  GLU   A N   1 
ATOM   1487 C  CA  . GLU   A 1 183 ? 8.610  -1.107  -13.711 1.00 12.57 ?  624  GLU   A CA  1 
ATOM   1488 C  C   . GLU   A 1 183 ? 7.155  -0.829  -14.079 1.00 11.91 ?  624  GLU   A C   1 
ATOM   1489 O  O   . GLU   A 1 183 ? 6.805  0.309   -14.410 1.00 13.17 ?  624  GLU   A O   1 
ATOM   1490 C  CB  . GLU   A 1 183 ? 9.399  -1.528  -14.946 1.00 14.40 ?  624  GLU   A CB  1 
ATOM   1491 C  CG  . GLU   A 1 183 ? 9.739  -0.361  -15.846 1.00 19.09 ?  624  GLU   A CG  1 
ATOM   1492 C  CD  . GLU   A 1 183 ? 10.829 -0.691  -16.843 1.00 23.29 ?  624  GLU   A CD  1 
ATOM   1493 O  OE1 . GLU   A 1 183 ? 11.107 -1.894  -17.061 1.00 23.65 ?  624  GLU   A OE1 1 
ATOM   1494 O  OE2 . GLU   A 1 183 ? 11.395 0.259   -17.423 1.00 26.09 -1 624  GLU   A OE2 1 
ATOM   1495 N  N   . GLU   A 1 184 ? 6.292  -1.835  -13.985 1.00 13.48 ?  625  GLU   A N   1 
ATOM   1496 C  CA  . GLU   A 1 184 ? 4.874  -1.687  -14.305 1.00 15.29 ?  625  GLU   A CA  1 
ATOM   1497 C  C   . GLU   A 1 184 ? 3.992  -1.621  -13.063 1.00 17.37 ?  625  GLU   A C   1 
ATOM   1498 O  O   . GLU   A 1 184 ? 2.796  -1.932  -13.135 1.00 18.51 ?  625  GLU   A O   1 
ATOM   1499 C  CB  . GLU   A 1 184 ? 4.408  -2.818  -15.219 1.00 15.70 ?  625  GLU   A CB  1 
ATOM   1500 C  CG  . GLU   A 1 184 ? 4.986  -2.741  -16.622 1.00 21.72 ?  625  GLU   A CG  1 
ATOM   1501 C  CD  . GLU   A 1 184 ? 4.597  -3.923  -17.482 1.00 30.43 ?  625  GLU   A CD  1 
ATOM   1502 O  OE1 . GLU   A 1 184 ? 4.926  -5.067  -17.109 1.00 34.09 ?  625  GLU   A OE1 1 
ATOM   1503 O  OE2 . GLU   A 1 184 ? 3.962  -3.706  -18.534 1.00 33.48 -1 625  GLU   A OE2 1 
ATOM   1504 N  N   . ASP   A 1 185 ? 4.550  -1.205  -11.929 1.00 14.42 ?  626  ASP   A N   1 
ATOM   1505 C  CA  . ASP   A 1 185 ? 3.873  -1.260  -10.641 1.00 16.02 ?  626  ASP   A CA  1 
ATOM   1506 C  C   . ASP   A 1 185 ? 3.784  0.145   -10.065 1.00 16.82 ?  626  ASP   A C   1 
ATOM   1507 O  O   . ASP   A 1 185 ? 4.801  0.842   -9.944  1.00 16.01 ?  626  ASP   A O   1 
ATOM   1508 C  CB  . ASP   A 1 185 ? 4.662  -2.164  -9.686  1.00 16.98 ?  626  ASP   A CB  1 
ATOM   1509 C  CG  . ASP   A 1 185 ? 3.832  -2.653  -8.515  1.00 20.57 ?  626  ASP   A CG  1 
ATOM   1510 O  OD1 . ASP   A 1 185 ? 2.810  -2.014  -8.204  0.61 22.35 ?  626  ASP   A OD1 1 
ATOM   1511 O  OD2 . ASP   A 1 185 ? 4.237  -3.660  -7.891  0.62 20.86 -1 626  ASP   A OD2 1 
ATOM   1512 N  N   . ASP   A 1 186 ? 2.573  0.557   -9.703  1.00 15.71 ?  627  ASP   A N   1 
ATOM   1513 C  CA  . ASP   A 1 186 ? 2.372  1.827   -9.020  1.00 16.42 ?  627  ASP   A CA  1 
ATOM   1514 C  C   . ASP   A 1 186 ? 2.250  1.684   -7.507  1.00 14.59 ?  627  ASP   A C   1 
ATOM   1515 O  O   . ASP   A 1 186 ? 2.074  2.697   -6.817  1.00 17.94 ?  627  ASP   A O   1 
ATOM   1516 C  CB  . ASP   A 1 186 ? 1.166  2.589   -9.593  1.00 20.44 ?  627  ASP   A CB  1 
ATOM   1517 C  CG  . ASP   A 1 186 ? -0.141 1.852   -9.407  1.00 26.24 ?  627  ASP   A CG  1 
ATOM   1518 O  OD1 . ASP   A 1 186 ? -0.130 0.666   -9.012  1.00 25.71 ?  627  ASP   A OD1 1 
ATOM   1519 O  OD2 . ASP   A 1 186 ? -1.197 2.477   -9.646  1.00 31.15 -1 627  ASP   A OD2 1 
ATOM   1520 N  N   . SER   A 1 187 ? 2.341  0.465   -6.972  1.00 13.96 ?  628  SER   A N   1 
ATOM   1521 C  CA  . SER   A 1 187 ? 2.334  0.282   -5.526  1.00 13.69 ?  628  SER   A CA  1 
ATOM   1522 C  C   . SER   A 1 187 ? 3.719  0.387   -4.898  1.00 13.32 ?  628  SER   A C   1 
ATOM   1523 O  O   . SER   A 1 187 ? 3.820  0.563   -3.674  1.00 14.69 ?  628  SER   A O   1 
ATOM   1524 C  CB  . SER   A 1 187 ? 1.687  -1.053  -5.125  1.00 14.61 ?  628  SER   A CB  1 
ATOM   1525 O  OG  . SER   A 1 187 ? 2.488  -2.168  -5.486  1.00 13.72 ?  628  SER   A OG  1 
ATOM   1526 N  N   . VAL   A 1 188 ? 4.774  0.279   -5.702  1.00 12.04 ?  629  VAL   A N   1 
ATOM   1527 C  CA  . VAL   A 1 188 ? 6.150  0.372   -5.238  1.00 11.75 ?  629  VAL   A CA  1 
ATOM   1528 C  C   . VAL   A 1 188 ? 6.800  1.482   -6.041  1.00 13.54 ?  629  VAL   A C   1 
ATOM   1529 O  O   . VAL   A 1 188 ? 7.020  1.339   -7.248  1.00 14.11 ?  629  VAL   A O   1 
ATOM   1530 C  CB  . VAL   A 1 188 ? 6.902  -0.949  -5.414  1.00 11.46 ?  629  VAL   A CB  1 
ATOM   1531 C  CG1 . VAL   A 1 188 ? 8.340  -0.807  -4.913  1.00 13.52 ?  629  VAL   A CG1 1 
ATOM   1532 C  CG2 . VAL   A 1 188 ? 6.191  -2.048  -4.668  1.00 14.00 ?  629  VAL   A CG2 1 
ATOM   1533 N  N   . LEU   A 1 189 ? 7.087  2.597   -5.380  1.00 13.62 ?  630  LEU   A N   1 
ATOM   1534 C  CA  . LEU   A 1 189 ? 7.774  3.717   -6.001  1.00 12.39 ?  630  LEU   A CA  1 
ATOM   1535 C  C   . LEU   A 1 189 ? 9.277  3.487   -5.842  1.00 13.01 ?  630  LEU   A C   1 
ATOM   1536 O  O   . LEU   A 1 189 ? 9.767  3.319   -4.718  1.00 12.16 ?  630  LEU   A O   1 
ATOM   1537 C  CB  . LEU   A 1 189 ? 7.349  5.003   -5.302  1.00 12.55 ?  630  LEU   A CB  1 
ATOM   1538 C  CG  . LEU   A 1 189 ? 8.146  6.254   -5.631  1.00 13.33 ?  630  LEU   A CG  1 
ATOM   1539 C  CD1 . LEU   A 1 189 ? 8.005  6.585   -7.102  1.00 14.17 ?  630  LEU   A CD1 1 
ATOM   1540 C  CD2 . LEU   A 1 189 ? 7.673  7.410   -4.773  1.00 14.98 ?  630  LEU   A CD2 1 
ATOM   1541 N  N   . TYR   A 1 190 ? 9.998  3.446   -6.959  1.00 11.40 ?  631  TYR   A N   1 
ATOM   1542 C  CA  . TYR   A 1 190 ? 11.442 3.220   -6.941  1.00 11.40 ?  631  TYR   A CA  1 
ATOM   1543 C  C   . TYR   A 1 190 ? 12.129 4.536   -7.264  1.00 11.43 ?  631  TYR   A C   1 
ATOM   1544 O  O   . TYR   A 1 190 ? 11.871 5.129   -8.316  1.00 13.02 ?  631  TYR   A O   1 
ATOM   1545 C  CB  . TYR   A 1 190 ? 11.857 2.148   -7.952  1.00 11.10 ?  631  TYR   A CB  1 
ATOM   1546 C  CG  . TYR   A 1 190 ? 13.355 1.894   -7.978  1.00 11.83 ?  631  TYR   A CG  1 
ATOM   1547 C  CD1 . TYR   A 1 190 ? 14.025 1.428   -6.849  1.00 10.56 ?  631  TYR   A CD1 1 
ATOM   1548 C  CD2 . TYR   A 1 190 ? 14.101 2.131   -9.120  1.00 12.35 ?  631  TYR   A CD2 1 
ATOM   1549 C  CE1 . TYR   A 1 190 ? 15.396 1.197   -6.868  1.00 11.08 ?  631  TYR   A CE1 1 
ATOM   1550 C  CE2 . TYR   A 1 190 ? 15.466 1.916   -9.152  1.00 12.65 ?  631  TYR   A CE2 1 
ATOM   1551 C  CZ  . TYR   A 1 190 ? 16.111 1.438   -8.030  1.00 10.78 ?  631  TYR   A CZ  1 
ATOM   1552 O  OH  . TYR   A 1 190 ? 17.470 1.238   -8.062  1.00 11.28 ?  631  TYR   A OH  1 
ATOM   1553 N  N   . ILE   A 1 191 ? 12.983 5.005   -6.352  1.00 10.94 ?  632  ILE   A N   1 
ATOM   1554 C  CA  . ILE   A 1 191 ? 13.790 6.201   -6.586  1.00 11.74 ?  632  ILE   A CA  1 
ATOM   1555 C  C   . ILE   A 1 191 ? 15.255 5.817   -6.419  1.00 12.52 ?  632  ILE   A C   1 
ATOM   1556 O  O   . ILE   A 1 191 ? 15.666 5.395   -5.330  1.00 13.98 ?  632  ILE   A O   1 
ATOM   1557 C  CB  . ILE   A 1 191 ? 13.419 7.348   -5.630  1.00 12.76 ?  632  ILE   A CB  1 
ATOM   1558 C  CG1 . ILE   A 1 191 ? 11.927 7.695   -5.722  1.00 11.76 ?  632  ILE   A CG1 1 
ATOM   1559 C  CG2 . ILE   A 1 191 ? 14.280 8.569   -5.907  1.00 13.55 ?  632  ILE   A CG2 1 
ATOM   1560 C  CD1 . ILE   A 1 191 ? 11.504 8.832   -4.789  1.00 16.15 ?  632  ILE   A CD1 1 
ATOM   1561 N  N   . SER   A 1 192 ? 16.045 5.972   -7.480  1.00 10.47 ?  633  SER   A N   1 
ATOM   1562 C  CA  . SER   A 1 192 ? 17.465 5.652   -7.435  1.00 10.91 ?  633  SER   A CA  1 
ATOM   1563 C  C   . SER   A 1 192 ? 18.294 6.885   -7.770  1.00 11.77 ?  633  SER   A C   1 
ATOM   1564 O  O   . SER   A 1 192 ? 17.988 7.606   -8.729  1.00 12.69 ?  633  SER   A O   1 
ATOM   1565 C  CB  . SER   A 1 192 ? 17.794 4.524   -8.415  1.00 11.45 ?  633  SER   A CB  1 
ATOM   1566 O  OG  . SER   A 1 192 ? 19.195 4.338   -8.501  1.00 13.22 ?  633  SER   A OG  1 
ATOM   1567 N  N   . LEU   A 1 193 ? 19.334 7.130   -6.979  1.00 11.05 ?  634  LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 193 ? 20.391 8.065   -7.345  1.00 10.70 ?  634  LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 193 ? 21.613 7.237   -7.709  1.00 10.93 ?  634  LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 193 ? 21.924 6.258   -7.023  1.00 11.72 ?  634  LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 193 ? 20.723 9.012   -6.176  1.00 11.66 ?  634  LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 193 ? 19.523 9.681   -5.504  1.00 12.22 ?  634  LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 193 ? 19.055 8.889   -4.295  1.00 13.54 ?  634  LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 193 ? 19.851 11.108  -5.078  1.00 12.95 ?  634  LEU   A CD2 1 
ATOM   1575 N  N   . HIS   A 1 194 ? 22.276 7.579   -8.808  1.00 10.98 ?  635  HIS   A N   1 
ATOM   1576 C  CA  . HIS   A 1 194 ? 23.366 6.702   -9.210  1.00 11.37 ?  635  HIS   A CA  1 
ATOM   1577 C  C   . HIS   A 1 194 ? 24.297 7.418   -10.164 1.00 11.07 ?  635  HIS   A C   1 
ATOM   1578 O  O   . HIS   A 1 194 ? 23.872 8.282   -10.941 1.00 12.71 ?  635  HIS   A O   1 
ATOM   1579 C  CB  . HIS   A 1 194 ? 22.845 5.428   -9.882  1.00 10.80 ?  635  HIS   A CB  1 
ATOM   1580 C  CG  . HIS   A 1 194 ? 21.734 5.677   -10.852 1.00 10.14 ?  635  HIS   A CG  1 
ATOM   1581 N  ND1 . HIS   A 1 194 ? 20.417 5.785   -10.461 1.00 12.01 ?  635  HIS   A ND1 1 
ATOM   1582 C  CD2 . HIS   A 1 194 ? 21.752 5.891   -12.189 1.00 12.36 ?  635  HIS   A CD2 1 
ATOM   1583 C  CE1 . HIS   A 1 194 ? 19.665 6.024   -11.521 1.00 12.99 ?  635  HIS   A CE1 1 
ATOM   1584 N  NE2 . HIS   A 1 194 ? 20.454 6.109   -12.578 1.00 13.76 ?  635  HIS   A NE2 1 
ATOM   1585 N  N   . ARG   A 1 195 ? 25.570 7.027   -10.112 1.00 11.48 ?  636  ARG   A N   1 
ATOM   1586 C  CA  . ARG   A 1 195 ? 26.522 7.434   -11.131 1.00 12.13 ?  636  ARG   A CA  1 
ATOM   1587 C  C   . ARG   A 1 195 ? 26.154 6.746   -12.438 1.00 12.70 ?  636  ARG   A C   1 
ATOM   1588 O  O   . ARG   A 1 195 ? 25.954 5.526   -12.478 1.00 13.11 ?  636  ARG   A O   1 
ATOM   1589 C  CB  . ARG   A 1 195 ? 27.942 7.058   -10.699 1.00 11.52 ?  636  ARG   A CB  1 
ATOM   1590 C  CG  . ARG   A 1 195 ? 29.018 7.707   -11.548 1.00 11.68 ?  636  ARG   A CG  1 
ATOM   1591 C  CD  . ARG   A 1 195 ? 30.400 7.501   -10.972 1.00 13.23 ?  636  ARG   A CD  1 
ATOM   1592 N  NE  . ARG   A 1 195 ? 31.406 8.035   -11.882 1.00 17.08 ?  636  ARG   A NE  1 
ATOM   1593 C  CZ  . ARG   A 1 195 ? 32.718 7.896   -11.722 1.00 19.06 ?  636  ARG   A CZ  1 
ATOM   1594 N  NH1 . ARG   A 1 195 ? 33.211 7.249   -10.669 1.00 18.28 ?  636  ARG   A NH1 1 
ATOM   1595 N  NH2 . ARG   A 1 195 ? 33.546 8.410   -12.621 1.00 21.46 ?  636  ARG   A NH2 1 
ATOM   1596 N  N   . TYR   A 1 196 ? 26.065 7.535   -13.506 1.00 12.60 ?  637  TYR   A N   1 
ATOM   1597 C  CA  . TYR   A 1 196 ? 25.570 7.093   -14.807 1.00 14.16 ?  637  TYR   A CA  1 
ATOM   1598 C  C   . TYR   A 1 196 ? 26.603 7.286   -15.906 1.00 14.04 ?  637  TYR   A C   1 
ATOM   1599 O  O   . TYR   A 1 196 ? 26.900 6.340   -16.648 1.00 13.73 ?  637  TYR   A O   1 
ATOM   1600 C  CB  . TYR   A 1 196 ? 24.292 7.882   -15.133 1.00 12.33 ?  637  TYR   A CB  1 
ATOM   1601 C  CG  . TYR   A 1 196 ? 23.606 7.493   -16.431 1.00 13.72 ?  637  TYR   A CG  1 
ATOM   1602 C  CD1 . TYR   A 1 196 ? 23.187 6.187   -16.660 1.00 14.28 ?  637  TYR   A CD1 1 
ATOM   1603 C  CD2 . TYR   A 1 196 ? 23.377 8.436   -17.423 1.00 13.87 ?  637  TYR   A CD2 1 
ATOM   1604 C  CE1 . TYR   A 1 196 ? 22.549 5.833   -17.858 1.00 15.03 ?  637  TYR   A CE1 1 
ATOM   1605 C  CE2 . TYR   A 1 196 ? 22.750 8.088   -18.613 1.00 13.81 ?  637  TYR   A CE2 1 
ATOM   1606 C  CZ  . TYR   A 1 196 ? 22.350 6.795   -18.823 1.00 16.51 ?  637  TYR   A CZ  1 
ATOM   1607 O  OH  . TYR   A 1 196 ? 21.725 6.467   -20.004 1.00 17.90 ?  637  TYR   A OH  1 
ATOM   1608 N  N   . GLU   A 1 197 ? 27.176 8.483   -16.013 1.00 15.50 ?  638  GLU   A N   1 
ATOM   1609 C  CA  . GLU   A 1 197 ? 28.167 8.805   -17.040 1.00 13.92 ?  638  GLU   A CA  1 
ATOM   1610 C  C   . GLU   A 1 197 ? 27.672 8.428   -18.434 1.00 14.46 ?  638  GLU   A C   1 
ATOM   1611 O  O   . GLU   A 1 197 ? 28.349 7.726   -19.188 1.00 15.89 ?  638  GLU   A O   1 
ATOM   1612 C  CB  . GLU   A 1 197 ? 29.529 8.180   -16.727 1.00 14.62 ?  638  GLU   A CB  1 
ATOM   1613 C  CG  . GLU   A 1 197 ? 29.996 8.371   -15.288 1.00 15.47 ?  638  GLU   A CG  1 
ATOM   1614 C  CD  . GLU   A 1 197 ? 30.259 9.823   -14.927 1.00 17.60 ?  638  GLU   A CD  1 
ATOM   1615 O  OE1 . GLU   A 1 197 ? 30.196 10.717  -15.795 1.00 18.31 ?  638  GLU   A OE1 1 
ATOM   1616 O  OE2 . GLU   A 1 197 ? 30.563 10.082  -13.750 1.00 18.56 -1 638  GLU   A OE2 1 
ATOM   1617 N  N   . ASP   A 1 198 ? 26.459 8.879   -18.747 1.00 13.96 ?  639  ASP   A N   1 
ATOM   1618 C  CA  . ASP   A 1 198 ? 25.827 8.650   -20.052 1.00 18.30 ?  639  ASP   A CA  1 
ATOM   1619 C  C   . ASP   A 1 198 ? 25.817 7.173   -20.444 1.00 19.74 ?  639  ASP   A C   1 
ATOM   1620 O  O   . ASP   A 1 198 ? 25.999 6.818   -21.611 1.00 21.88 ?  639  ASP   A O   1 
ATOM   1621 C  CB  . ASP   A 1 198 ? 26.428 9.534   -21.146 1.00 22.50 ?  639  ASP   A CB  1 
ATOM   1622 C  CG  . ASP   A 1 198 ? 26.319 11.012  -20.822 1.00 29.51 ?  639  ASP   A CG  1 
ATOM   1623 O  OD1 . ASP   A 1 198 ? 25.207 11.467  -20.478 1.00 33.52 -1 639  ASP   A OD1 1 
ATOM   1624 O  OD2 . ASP   A 1 198 ? 27.349 11.715  -20.895 1.00 31.42 ?  639  ASP   A OD2 1 
ATOM   1625 N  N   . GLY   A 1 199 ? 25.590 6.302   -19.454 1.00 16.28 ?  640  GLY   A N   1 
ATOM   1626 C  CA  . GLY   A 1 199 ? 25.524 4.874   -19.682 1.00 15.66 ?  640  GLY   A CA  1 
ATOM   1627 C  C   . GLY   A 1 199 ? 26.842 4.132   -19.623 1.00 15.03 ?  640  GLY   A C   1 
ATOM   1628 O  O   . GLY   A 1 199 ? 26.850 2.908   -19.827 1.00 18.79 ?  640  GLY   A O   1 
ATOM   1629 N  N   . ALA   A 1 200 ? 27.958 4.816   -19.354 1.00 16.56 ?  641  ALA   A N   1 
ATOM   1630 C  CA  . ALA   A 1 200 ? 29.268 4.178   -19.281 1.00 19.02 ?  641  ALA   A CA  1 
ATOM   1631 C  C   . ALA   A 1 200 ? 29.606 3.590   -17.912 1.00 20.95 ?  641  ALA   A C   1 
ATOM   1632 O  O   . ALA   A 1 200 ? 30.582 2.843   -17.808 1.00 23.02 ?  641  ALA   A O   1 
ATOM   1633 C  CB  . ALA   A 1 200 ? 30.373 5.170   -19.662 1.00 20.86 ?  641  ALA   A CB  1 
ATOM   1634 N  N   . PHE   A 1 201 ? 28.862 3.911   -16.859 1.00 17.67 ?  642  PHE   A N   1 
ATOM   1635 C  CA  . PHE   A 1 201 ? 29.155 3.370   -15.533 1.00 15.76 ?  642  PHE   A CA  1 
ATOM   1636 C  C   . PHE   A 1 201 ? 28.332 2.108   -15.291 1.00 14.03 ?  642  PHE   A C   1 
ATOM   1637 O  O   . PHE   A 1 201 ? 27.181 2.016   -15.732 1.00 14.39 ?  642  PHE   A O   1 
ATOM   1638 C  CB  . PHE   A 1 201 ? 28.855 4.422   -14.464 1.00 14.15 ?  642  PHE   A CB  1 
ATOM   1639 C  CG  . PHE   A 1 201 ? 29.612 4.212   -13.181 1.00 14.01 ?  642  PHE   A CG  1 
ATOM   1640 C  CD1 . PHE   A 1 201 ? 30.962 4.510   -13.091 1.00 15.45 ?  642  PHE   A CD1 1 
ATOM   1641 C  CD2 . PHE   A 1 201 ? 28.965 3.710   -12.064 1.00 13.78 ?  642  PHE   A CD2 1 
ATOM   1642 C  CE1 . PHE   A 1 201 ? 31.653 4.312   -11.914 1.00 16.36 ?  642  PHE   A CE1 1 
ATOM   1643 C  CE2 . PHE   A 1 201 ? 29.655 3.510   -10.880 1.00 15.03 ?  642  PHE   A CE2 1 
ATOM   1644 C  CZ  . PHE   A 1 201 ? 31.000 3.811   -10.812 1.00 14.75 ?  642  PHE   A CZ  1 
ATOM   1645 N  N   . PHE   A 1 202 ? 28.926 1.144   -14.573 1.00 13.29 ?  643  PHE   A N   1 
ATOM   1646 C  CA  . PHE   A 1 202 ? 28.244 -0.117  -14.298 1.00 12.60 ?  643  PHE   A CA  1 
ATOM   1647 C  C   . PHE   A 1 202 ? 26.872 0.174   -13.699 1.00 13.30 ?  643  PHE   A C   1 
ATOM   1648 O  O   . PHE   A 1 202 ? 26.763 1.013   -12.799 1.00 12.31 ?  643  PHE   A O   1 
ATOM   1649 C  CB  . PHE   A 1 202 ? 29.056 -0.953  -13.295 1.00 13.68 ?  643  PHE   A CB  1 
ATOM   1650 C  CG  . PHE   A 1 202 ? 28.487 -2.332  -13.038 1.00 13.65 ?  643  PHE   A CG  1 
ATOM   1651 C  CD1 . PHE   A 1 202 ? 27.544 -2.552  -12.033 1.00 13.93 ?  643  PHE   A CD1 1 
ATOM   1652 C  CD2 . PHE   A 1 202 ? 28.888 -3.407  -13.817 1.00 14.55 ?  643  PHE   A CD2 1 
ATOM   1653 C  CE1 . PHE   A 1 202 ? 27.017 -3.821  -11.829 1.00 13.60 ?  643  PHE   A CE1 1 
ATOM   1654 C  CE2 . PHE   A 1 202 ? 28.371 -4.672  -13.605 1.00 15.94 ?  643  PHE   A CE2 1 
ATOM   1655 C  CZ  . PHE   A 1 202 ? 27.433 -4.878  -12.611 1.00 15.98 ?  643  PHE   A CZ  1 
ATOM   1656 N  N   . PRO   A 1 203 ? 25.803 -0.521  -14.130 1.00 11.57 ?  644  PRO   A N   1 
ATOM   1657 C  CA  . PRO   A 1 203 ? 25.755 -1.709  -14.981 1.00 12.84 ?  644  PRO   A CA  1 
ATOM   1658 C  C   . PRO   A 1 203 ? 25.624 -1.449  -16.493 1.00 13.35 ?  644  PRO   A C   1 
ATOM   1659 O  O   . PRO   A 1 203 ? 25.205 -2.354  -17.206 1.00 16.71 ?  644  PRO   A O   1 
ATOM   1660 C  CB  . PRO   A 1 203 ? 24.527 -2.449  -14.445 1.00 15.30 ?  644  PRO   A CB  1 
ATOM   1661 C  CG  . PRO   A 1 203 ? 23.603 -1.365  -14.029 1.00 13.91 ?  644  PRO   A CG  1 
ATOM   1662 C  CD  . PRO   A 1 203 ? 24.493 -0.259  -13.500 1.00 12.81 ?  644  PRO   A CD  1 
ATOM   1663 N  N   . ASN   A 1 204 ? 25.967 -0.246  -16.960 1.00 14.22 ?  645  ASN   A N   1 
ATOM   1664 C  CA  . ASN   A 1 204 ? 26.262 0.011   -18.377 1.00 14.36 ?  645  ASN   A CA  1 
ATOM   1665 C  C   . ASN   A 1 204 ? 25.018 0.000   -19.269 1.00 15.26 ?  645  ASN   A C   1 
ATOM   1666 O  O   . ASN   A 1 204 ? 25.084 -0.392  -20.442 1.00 16.32 ?  645  ASN   A O   1 
ATOM   1667 C  CB  . ASN   A 1 204 ? 27.348 -0.931  -18.911 1.00 16.10 ?  645  ASN   A CB  1 
ATOM   1668 C  CG  . ASN   A 1 204 ? 28.580 -0.953  -18.030 1.00 20.40 ?  645  ASN   A CG  1 
ATOM   1669 O  OD1 . ASN   A 1 204 ? 28.763 -1.860  -17.221 1.00 21.31 ?  645  ASN   A OD1 1 
ATOM   1670 N  ND2 . ASN   A 1 204 ? 29.434 0.058   -18.179 1.00 23.50 ?  645  ASN   A ND2 1 
ATOM   1671 N  N   . SER   A 1 205 ? 23.886 0.452   -18.746 1.00 14.14 ?  646  SER   A N   1 
ATOM   1672 C  CA  . SER   A 1 205 ? 22.644 0.432   -19.499 1.00 13.33 ?  646  SER   A CA  1 
ATOM   1673 C  C   . SER   A 1 205 ? 21.950 1.788   -19.451 1.00 14.80 ?  646  SER   A C   1 
ATOM   1674 O  O   . SER   A 1 205 ? 21.924 2.452   -18.410 1.00 16.13 ?  646  SER   A O   1 
ATOM   1675 C  CB  . SER   A 1 205 ? 21.717 -0.668  -18.978 1.00 14.86 ?  646  SER   A CB  1 
ATOM   1676 O  OG  . SER   A 1 205 ? 20.409 -0.548  -19.517 1.00 14.67 ?  646  SER   A OG  1 
ATOM   1677 N  N   . GLU   A 1 206 ? 21.389 2.205   -20.595 1.00 14.42 ?  647  GLU   A N   1 
ATOM   1678 C  CA  . GLU   A 1 206 ? 20.564 3.409   -20.627 1.00 12.50 ?  647  GLU   A CA  1 
ATOM   1679 C  C   . GLU   A 1 206 ? 19.250 3.258   -19.875 1.00 12.34 ?  647  GLU   A C   1 
ATOM   1680 O  O   . GLU   A 1 206 ? 18.518 4.243   -19.742 1.00 14.23 ?  647  GLU   A O   1 
ATOM   1681 C  CB  . GLU   A 1 206 ? 20.286 3.840   -22.067 1.00 13.48 ?  647  GLU   A CB  1 
ATOM   1682 C  CG  . GLU   A 1 206 ? 21.548 4.156   -22.824 1.00 16.08 ?  647  GLU   A CG  1 
ATOM   1683 C  CD  . GLU   A 1 206 ? 21.283 4.843   -24.146 1.00 21.60 ?  647  GLU   A CD  1 
ATOM   1684 O  OE1 . GLU   A 1 206 ? 20.163 5.374   -24.338 1.00 22.74 ?  647  GLU   A OE1 1 
ATOM   1685 O  OE2 . GLU   A 1 206 ? 22.203 4.846   -24.990 1.00 23.57 -1 647  GLU   A OE2 1 
ATOM   1686 N  N   . ASP   A 1 207 ? 18.931 2.062   -19.367 1.00 11.91 ?  648  ASP   A N   1 
ATOM   1687 C  CA  . ASP   A 1 207 ? 17.762 1.906   -18.505 1.00 12.92 ?  648  ASP   A CA  1 
ATOM   1688 C  C   . ASP   A 1 207 ? 17.838 2.807   -17.280 1.00 12.11 ?  648  ASP   A C   1 
ATOM   1689 O  O   . ASP   A 1 207 ? 16.806 3.109   -16.675 1.00 13.87 ?  648  ASP   A O   1 
ATOM   1690 C  CB  . ASP   A 1 207 ? 17.679 0.474   -17.977 1.00 16.42 ?  648  ASP   A CB  1 
ATOM   1691 C  CG  . ASP   A 1 207 ? 17.359 -0.546  -19.047 1.00 19.76 ?  648  ASP   A CG  1 
ATOM   1692 O  OD1 . ASP   A 1 207 ? 17.142 -0.175  -20.218 1.00 20.56 ?  648  ASP   A OD1 1 
ATOM   1693 O  OD2 . ASP   A 1 207 ? 17.330 -1.739  -18.693 1.00 21.92 -1 648  ASP   A OD2 1 
ATOM   1694 N  N   . ALA   A 1 208 ? 19.045 3.222   -16.907 1.00 12.76 ?  649  ALA   A N   1 
ATOM   1695 C  CA  . ALA   A 1 208 ? 19.290 4.046   -15.729 1.00 11.79 ?  649  ALA   A CA  1 
ATOM   1696 C  C   . ALA   A 1 208 ? 19.092 5.541   -15.988 1.00 11.61 ?  649  ALA   A C   1 
ATOM   1697 O  O   . ALA   A 1 208 ? 19.264 6.342   -15.069 1.00 13.10 ?  649  ALA   A O   1 
ATOM   1698 C  CB  . ALA   A 1 208 ? 20.702 3.780   -15.201 1.00 11.87 ?  649  ALA   A CB  1 
ATOM   1699 N  N   . ASN   A 1 209 ? 18.716 5.946   -17.202 1.00 13.39 ?  650  ASN   A N   1 
ATOM   1700 C  CA  . ASN   A 1 209 ? 18.555 7.369   -17.488 1.00 13.48 ?  650  ASN   A CA  1 
ATOM   1701 C  C   . ASN   A 1 209 ? 17.248 7.930   -16.911 1.00 11.89 ?  650  ASN   A C   1 
ATOM   1702 O  O   . ASN   A 1 209 ? 16.301 7.203   -16.590 1.00 12.70 ?  650  ASN   A O   1 
ATOM   1703 C  CB  . ASN   A 1 209 ? 18.628 7.645   -18.991 1.00 12.87 ?  650  ASN   A CB  1 
ATOM   1704 C  CG  . ASN   A 1 209 ? 19.295 8.966   -19.292 1.00 15.39 ?  650  ASN   A CG  1 
ATOM   1705 O  OD1 . ASN   A 1 209 ? 19.628 9.733   -18.375 1.00 16.92 ?  650  ASN   A OD1 1 
ATOM   1706 N  ND2 . ASN   A 1 209 ? 19.520 9.239   -20.574 1.00 17.21 ?  650  ASN   A ND2 1 
ATOM   1707 N  N   . TYR   A 1 210 ? 17.205 9.266   -16.805 1.00 12.94 ?  651  TYR   A N   1 
ATOM   1708 C  CA  . TYR   A 1 210 ? 16.096 9.971   -16.173 1.00 12.81 ?  651  TYR   A CA  1 
ATOM   1709 C  C   . TYR   A 1 210 ? 14.790 9.835   -16.945 1.00 12.13 ?  651  TYR   A C   1 
ATOM   1710 O  O   . TYR   A 1 210 ? 13.724 10.068  -16.365 1.00 13.82 ?  651  TYR   A O   1 
ATOM   1711 C  CB  . TYR   A 1 210 ? 16.424 11.466  -16.010 1.00 12.62 ?  651  TYR   A CB  1 
ATOM   1712 C  CG  . TYR   A 1 210 ? 16.727 12.183  -17.322 1.00 14.40 ?  651  TYR   A CG  1 
ATOM   1713 C  CD1 . TYR   A 1 210 ? 15.704 12.639  -18.149 1.00 14.88 ?  651  TYR   A CD1 1 
ATOM   1714 C  CD2 . TYR   A 1 210 ? 18.035 12.401  -17.728 1.00 15.29 ?  651  TYR   A CD2 1 
ATOM   1715 C  CE1 . TYR   A 1 210 ? 15.981 13.281  -19.356 1.00 16.80 ?  651  TYR   A CE1 1 
ATOM   1716 C  CE2 . TYR   A 1 210 ? 18.324 13.040  -18.934 1.00 17.75 ?  651  TYR   A CE2 1 
ATOM   1717 C  CZ  . TYR   A 1 210 ? 17.291 13.478  -19.734 1.00 17.47 ?  651  TYR   A CZ  1 
ATOM   1718 O  OH  . TYR   A 1 210 ? 17.571 14.120  -20.923 1.00 21.57 ?  651  TYR   A OH  1 
ATOM   1719 N  N   . ASP   A 1 211 ? 14.850 9.478   -18.229 1.00 16.32 ?  652  ASP   A N   1 
ATOM   1720 C  CA  . ASP   A 1 211 ? 13.636 9.386   -19.032 1.00 16.45 ?  652  ASP   A CA  1 
ATOM   1721 C  C   . ASP   A 1 211 ? 12.902 8.061   -18.866 1.00 16.88 ?  652  ASP   A C   1 
ATOM   1722 O  O   . ASP   A 1 211 ? 11.795 7.913   -19.392 1.00 18.05 ?  652  ASP   A O   1 
ATOM   1723 C  CB  . ASP   A 1 211 ? 13.899 9.719   -20.509 1.00 16.99 ?  652  ASP   A CB  1 
ATOM   1724 C  CG  . ASP   A 1 211 ? 14.806 8.717   -21.196 1.00 20.41 ?  652  ASP   A CG  1 
ATOM   1725 O  OD1 . ASP   A 1 211 ? 15.550 7.992   -20.506 1.00 18.93 ?  652  ASP   A OD1 1 
ATOM   1726 O  OD2 . ASP   A 1 211 ? 14.801 8.667   -22.449 1.00 25.07 -1 652  ASP   A OD2 1 
ATOM   1727 N  N   . LYS   A 1 212 ? 13.458 7.113   -18.117 1.00 15.20 ?  653  LYS   A N   1 
ATOM   1728 C  CA  . LYS   A 1 212 ? 12.767 5.860   -17.828 1.00 15.51 ?  653  LYS   A CA  1 
ATOM   1729 C  C   . LYS   A 1 212 ? 11.907 6.101   -16.591 1.00 14.34 ?  653  LYS   A C   1 
ATOM   1730 O  O   . LYS   A 1 212 ? 12.386 6.037   -15.453 1.00 14.05 ?  653  LYS   A O   1 
ATOM   1731 C  CB  . LYS   A 1 212 ? 13.762 4.713   -17.676 1.00 17.39 ?  653  LYS   A CB  1 
ATOM   1732 C  CG  . LYS   A 1 212 ? 14.828 4.682   -18.784 1.00 19.98 ?  653  LYS   A CG  1 
ATOM   1733 C  CD  . LYS   A 1 212 ? 14.230 4.744   -20.195 1.00 20.82 ?  653  LYS   A CD  1 
ATOM   1734 C  CE  . LYS   A 1 212 ? 15.285 4.357   -21.238 1.00 19.68 ?  653  LYS   A CE  1 
ATOM   1735 N  NZ  . LYS   A 1 212 ? 16.386 5.374   -21.445 1.00 18.32 ?  653  LYS   A NZ  1 
ATOM   1736 N  N   . VAL   A 1 213 ? 10.627 6.410   -16.816 1.00 13.01 ?  654  VAL   A N   1 
ATOM   1737 C  CA  . VAL   A 1 213 ? 9.718  6.830   -15.750 1.00 14.71 ?  654  VAL   A CA  1 
ATOM   1738 C  C   . VAL   A 1 213 ? 8.770  5.730   -15.306 1.00 12.92 ?  654  VAL   A C   1 
ATOM   1739 O  O   . VAL   A 1 213 ? 7.914  5.982   -14.447 1.00 16.17 ?  654  VAL   A O   1 
ATOM   1740 C  CB  . VAL   A 1 213 ? 8.908  8.092   -16.121 1.00 15.51 ?  654  VAL   A CB  1 
ATOM   1741 C  CG1 . VAL   A 1 213 ? 9.827  9.261   -16.441 1.00 16.06 ?  654  VAL   A CG1 1 
ATOM   1742 C  CG2 . VAL   A 1 213 ? 7.946  7.802   -17.300 1.00 15.24 ?  654  VAL   A CG2 1 
ATOM   1743 N  N   . GLY   A 1 214 ? 8.897  4.524   -15.847 1.00 13.27 ?  655  GLY   A N   1 
ATOM   1744 C  CA  . GLY   A 1 214 ? 7.941  3.461   -15.613 1.00 12.89 ?  655  GLY   A CA  1 
ATOM   1745 C  C   . GLY   A 1 214 ? 7.099  3.183   -16.849 1.00 12.50 ?  655  GLY   A C   1 
ATOM   1746 O  O   . GLY   A 1 214 ? 7.106  3.931   -17.827 1.00 15.05 ?  655  GLY   A O   1 
ATOM   1747 N  N   . LEU   A 1 215 ? 6.357  2.072   -16.782 1.00 12.95 ?  656  LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 215 ? 5.560  1.597   -17.909 1.00 12.16 ?  656  LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 215 ? 4.175  1.197   -17.425 1.00 12.96 ?  656  LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 215 ? 3.999  0.763   -16.285 1.00 13.63 ?  656  LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 215 ? 6.229  0.391   -18.576 1.00 15.11 ?  656  LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 215 ? 7.585  0.645   -19.243 1.00 17.65 ?  656  LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 215 ? 8.228  -0.675  -19.676 1.00 20.65 ?  656  LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 215 ? 7.456  1.612   -20.411 1.00 19.75 ?  656  LEU   A CD2 1 
ATOM   1755 N  N   . GLY   A 1 216 ? 3.186  1.350   -18.309 1.00 13.78 ?  657  GLY   A N   1 
ATOM   1756 C  CA  . GLY   A 1 216 ? 1.839  0.940   -17.954 1.00 14.26 ?  657  GLY   A CA  1 
ATOM   1757 C  C   . GLY   A 1 216 ? 1.319  1.736   -16.777 1.00 15.19 ?  657  GLY   A C   1 
ATOM   1758 O  O   . GLY   A 1 216 ? 1.487  2.958   -16.700 1.00 14.68 ?  657  GLY   A O   1 
ATOM   1759 N  N   . LYS   A 1 217 ? 0.690  1.036   -15.835 1.00 15.45 ?  658  LYS   A N   1 
ATOM   1760 C  CA  . LYS   A 1 217 ? 0.209  1.729   -14.651 1.00 16.15 ?  658  LYS   A CA  1 
ATOM   1761 C  C   . LYS   A 1 217 ? 1.350  2.266   -13.799 1.00 16.99 ?  658  LYS   A C   1 
ATOM   1762 O  O   . LYS   A 1 217 ? 1.103  3.099   -12.919 1.00 18.56 ?  658  LYS   A O   1 
ATOM   1763 C  CB  . LYS   A 1 217 ? -0.706 0.830   -13.826 1.00 19.78 ?  658  LYS   A CB  1 
ATOM   1764 C  CG  . LYS   A 1 217 ? -0.016 -0.289  -13.080 1.00 22.09 ?  658  LYS   A CG  1 
ATOM   1765 C  CD  . LYS   A 1 217 ? -1.024 -1.057  -12.236 1.00 25.71 ?  658  LYS   A CD  1 
ATOM   1766 C  CE  . LYS   A 1 217 ? -0.353 -2.051  -11.304 1.00 27.17 ?  658  LYS   A CE  1 
ATOM   1767 N  NZ  . LYS   A 1 217 ? 0.396  -3.095  -12.043 1.00 27.72 ?  658  LYS   A NZ  1 
ATOM   1768 N  N   . GLY   A 1 218 ? 2.581  1.842   -14.059 1.00 13.66 ?  659  GLY   A N   1 
ATOM   1769 C  CA  . GLY   A 1 218 ? 3.729  2.323   -13.324 1.00 14.45 ?  659  GLY   A CA  1 
ATOM   1770 C  C   . GLY   A 1 218 ? 4.360  3.589   -13.852 1.00 14.07 ?  659  GLY   A C   1 
ATOM   1771 O  O   . GLY   A 1 218 ? 5.401  4.002   -13.330 1.00 14.96 ?  659  GLY   A O   1 
ATOM   1772 N  N   A ARG   A 1 219 ? 3.789  4.221   -14.879 0.74 16.54 ?  660  ARG   A N   1 
ATOM   1773 N  N   B ARG   A 1 219 ? 3.775  4.225   -14.866 0.26 15.56 ?  660  ARG   A N   1 
ATOM   1774 C  CA  A ARG   A 1 219 ? 4.366  5.460   -15.385 0.74 14.46 ?  660  ARG   A CA  1 
ATOM   1775 C  CA  B ARG   A 1 219 ? 4.327  5.472   -15.384 0.26 15.59 ?  660  ARG   A CA  1 
ATOM   1776 C  C   A ARG   A 1 219 ? 4.323  6.532   -14.304 0.74 15.19 ?  660  ARG   A C   1 
ATOM   1777 C  C   B ARG   A 1 219 ? 4.313  6.539   -14.297 0.26 16.05 ?  660  ARG   A C   1 
ATOM   1778 O  O   A ARG   A 1 219 ? 3.261  6.830   -13.749 0.74 15.90 ?  660  ARG   A O   1 
ATOM   1779 O  O   B ARG   A 1 219 ? 3.260  6.851   -13.732 0.26 16.46 ?  660  ARG   A O   1 
ATOM   1780 C  CB  A ARG   A 1 219 ? 3.615  5.930   -16.633 0.74 16.68 ?  660  ARG   A CB  1 
ATOM   1781 C  CB  B ARG   A 1 219 ? 3.516  5.937   -16.594 0.26 16.53 ?  660  ARG   A CB  1 
ATOM   1782 C  CG  A ARG   A 1 219 ? 3.782  5.030   -17.843 0.74 17.72 ?  660  ARG   A CG  1 
ATOM   1783 C  CG  B ARG   A 1 219 ? 3.864  5.234   -17.901 0.26 16.96 ?  660  ARG   A CG  1 
ATOM   1784 C  CD  A ARG   A 1 219 ? 3.105  5.635   -19.075 0.74 17.19 ?  660  ARG   A CD  1 
ATOM   1785 C  CD  B ARG   A 1 219 ? 3.615  6.154   -19.090 0.26 17.32 ?  660  ARG   A CD  1 
ATOM   1786 N  NE  A ARG   A 1 219 ? 3.798  6.832   -19.543 0.74 16.13 ?  660  ARG   A NE  1 
ATOM   1787 N  NE  B ARG   A 1 219 ? 2.373  6.901   -18.922 0.26 17.77 ?  660  ARG   A NE  1 
ATOM   1788 C  CZ  A ARG   A 1 219 ? 3.259  8.048   -19.582 0.74 16.40 ?  660  ARG   A CZ  1 
ATOM   1789 C  CZ  B ARG   A 1 219 ? 2.211  8.174   -19.264 0.26 17.23 ?  660  ARG   A CZ  1 
ATOM   1790 N  NH1 A ARG   A 1 219 ? 2.016  8.247   -19.172 0.74 18.02 ?  660  ARG   A NH1 1 
ATOM   1791 N  NH1 B ARG   A 1 219 ? 3.212  8.853   -19.804 0.26 16.86 ?  660  ARG   A NH1 1 
ATOM   1792 N  NH2 A ARG   A 1 219 ? 3.973  9.070   -20.025 0.74 16.02 ?  660  ARG   A NH2 1 
ATOM   1793 N  NH2 B ARG   A 1 219 ? 1.044  8.768   -19.060 0.26 16.57 ?  660  ARG   A NH2 1 
ATOM   1794 N  N   . GLY   A 1 220 ? 5.488  7.093   -14.000 1.00 15.97 ?  661  GLY   A N   1 
ATOM   1795 C  CA  . GLY   A 1 220 ? 5.647  8.038   -12.917 1.00 16.67 ?  661  GLY   A CA  1 
ATOM   1796 C  C   . GLY   A 1 220 ? 6.202  7.435   -11.645 1.00 16.71 ?  661  GLY   A C   1 
ATOM   1797 O  O   . GLY   A 1 220 ? 6.622  8.185   -10.749 1.00 17.04 ?  661  GLY   A O   1 
ATOM   1798 N  N   . TYR   A 1 221 ? 6.222  6.107   -11.537 1.00 14.48 ?  662  TYR   A N   1 
ATOM   1799 C  CA  . TYR   A 1 221 ? 6.608  5.436   -10.301 1.00 11.68 ?  662  TYR   A CA  1 
ATOM   1800 C  C   . TYR   A 1 221 ? 8.016  4.867   -10.359 1.00 11.34 ?  662  TYR   A C   1 
ATOM   1801 O  O   . TYR   A 1 221 ? 8.388  4.042   -9.511  1.00 12.28 ?  662  TYR   A O   1 
ATOM   1802 C  CB  . TYR   A 1 221 ? 5.564  4.394   -9.893  1.00 14.33 ?  662  TYR   A CB  1 
ATOM   1803 C  CG  . TYR   A 1 221 ? 4.241  5.044   -9.566  1.00 12.67 ?  662  TYR   A CG  1 
ATOM   1804 C  CD1 . TYR   A 1 221 ? 3.298  5.306   -10.561 1.00 16.64 ?  662  TYR   A CD1 1 
ATOM   1805 C  CD2 . TYR   A 1 221 ? 3.939  5.419   -8.264  1.00 14.15 ?  662  TYR   A CD2 1 
ATOM   1806 C  CE1 . TYR   A 1 221 ? 2.085  5.910   -10.259 1.00 20.27 ?  662  TYR   A CE1 1 
ATOM   1807 C  CE2 . TYR   A 1 221 ? 2.733  6.032   -7.951  1.00 17.41 ?  662  TYR   A CE2 1 
ATOM   1808 C  CZ  . TYR   A 1 221 ? 1.813  6.275   -8.954  1.00 20.99 ?  662  TYR   A CZ  1 
ATOM   1809 O  OH  . TYR   A 1 221 ? 0.613  6.884   -8.646  1.00 23.70 ?  662  TYR   A OH  1 
ATOM   1810 N  N   . ASN   A 1 222 ? 8.814  5.326   -11.320 1.00 11.37 ?  663  ASN   A N   1 
ATOM   1811 C  CA  . ASN   A 1 222 ? 10.221 4.968   -11.426 1.00 11.77 ?  663  ASN   A CA  1 
ATOM   1812 C  C   . ASN   A 1 222 ? 10.993 6.257   -11.658 1.00 11.80 ?  663  ASN   A C   1 
ATOM   1813 O  O   . ASN   A 1 222 ? 10.832 6.904   -12.701 1.00 13.70 ?  663  ASN   A O   1 
ATOM   1814 C  CB  . ASN   A 1 222 ? 10.465 3.987   -12.569 1.00 11.87 ?  663  ASN   A CB  1 
ATOM   1815 C  CG  . ASN   A 1 222 ? 11.847 3.384   -12.511 1.00 12.56 ?  663  ASN   A CG  1 
ATOM   1816 O  OD1 . ASN   A 1 222 ? 12.082 2.421   -11.761 1.00 11.78 ?  663  ASN   A OD1 1 
ATOM   1817 N  ND2 . ASN   A 1 222 ? 12.783 3.963   -13.262 1.00 12.12 ?  663  ASN   A ND2 1 
ATOM   1818 N  N   . VAL   A 1 223 ? 11.826 6.632   -10.686 1.00 11.57 ?  664  VAL   A N   1 
ATOM   1819 C  CA  . VAL   A 1 223 ? 12.525 7.910   -10.693 1.00 11.89 ?  664  VAL   A CA  1 
ATOM   1820 C  C   . VAL   A 1 223 ? 14.022 7.633   -10.661 1.00 12.44 ?  664  VAL   A C   1 
ATOM   1821 O  O   . VAL   A 1 223 ? 14.569 7.234   -9.623  1.00 12.52 ?  664  VAL   A O   1 
ATOM   1822 C  CB  . VAL   A 1 223 ? 12.110 8.780   -9.500  1.00 11.89 ?  664  VAL   A CB  1 
ATOM   1823 C  CG1 . VAL   A 1 223 ? 12.814 10.128  -9.549  1.00 14.76 ?  664  VAL   A CG1 1 
ATOM   1824 C  CG2 . VAL   A 1 223 ? 10.577 8.971   -9.465  1.00 13.72 ?  664  VAL   A CG2 1 
ATOM   1825 N  N   . ASN   A 1 224 ? 14.689 7.858   -11.781 1.00 11.49 ?  665  ASN   A N   1 
ATOM   1826 C  CA  . ASN   A 1 224 ? 16.136 7.725   -11.890 1.00 11.72 ?  665  ASN   A CA  1 
ATOM   1827 C  C   . ASN   A 1 224 ? 16.765 9.109   -11.845 1.00 11.57 ?  665  ASN   A C   1 
ATOM   1828 O  O   . ASN   A 1 224 ? 16.418 9.982   -12.652 1.00 14.02 ?  665  ASN   A O   1 
ATOM   1829 C  CB  . ASN   A 1 224 ? 16.527 7.065   -13.212 1.00 11.24 ?  665  ASN   A CB  1 
ATOM   1830 C  CG  . ASN   A 1 224 ? 16.274 5.570   -13.238 1.00 12.18 ?  665  ASN   A CG  1 
ATOM   1831 O  OD1 . ASN   A 1 224 ? 16.372 4.886   -12.224 1.00 12.33 ?  665  ASN   A OD1 1 
ATOM   1832 N  ND2 . ASN   A 1 224 ? 15.955 5.051   -14.422 1.00 13.21 ?  665  ASN   A ND2 1 
ATOM   1833 N  N   . ILE   A 1 225 ? 17.699 9.297   -10.916 1.00 12.07 ?  666  ILE   A N   1 
ATOM   1834 C  CA  . ILE   A 1 225 ? 18.475 10.525  -10.785 1.00 12.90 ?  666  ILE   A CA  1 
ATOM   1835 C  C   . ILE   A 1 225 ? 19.905 10.177  -11.173 1.00 13.40 ?  666  ILE   A C   1 
ATOM   1836 O  O   . ILE   A 1 225 ? 20.684 9.706   -10.326 1.00 12.71 ?  666  ILE   A O   1 
ATOM   1837 C  CB  . ILE   A 1 225 ? 18.381 11.108  -9.367  1.00 13.14 ?  666  ILE   A CB  1 
ATOM   1838 C  CG1 . ILE   A 1 225 ? 16.910 11.290  -8.974  1.00 12.78 ?  666  ILE   A CG1 1 
ATOM   1839 C  CG2 . ILE   A 1 225 ? 19.147 12.421  -9.293  1.00 13.64 ?  666  ILE   A CG2 1 
ATOM   1840 C  CD1 . ILE   A 1 225 ? 16.681 11.652  -7.517  1.00 13.63 ?  666  ILE   A CD1 1 
ATOM   1841 N  N   . PRO   A 1 226 ? 20.282 10.373  -12.440 1.00 12.83 ?  667  PRO   A N   1 
ATOM   1842 C  CA  . PRO   A 1 226 ? 21.593 9.929   -12.924 1.00 12.32 ?  667  PRO   A CA  1 
ATOM   1843 C  C   . PRO   A 1 226 ? 22.639 11.031  -12.899 1.00 14.31 ?  667  PRO   A C   1 
ATOM   1844 O  O   . PRO   A 1 226 ? 22.400 12.143  -13.391 1.00 14.00 ?  667  PRO   A O   1 
ATOM   1845 C  CB  . PRO   A 1 226 ? 21.293 9.472   -14.362 1.00 14.28 ?  667  PRO   A CB  1 
ATOM   1846 C  CG  . PRO   A 1 226 ? 19.918 10.055  -14.702 1.00 16.09 ?  667  PRO   A CG  1 
ATOM   1847 C  CD  . PRO   A 1 226 ? 19.418 10.843  -13.532 1.00 13.06 ?  667  PRO   A CD  1 
ATOM   1848 N  N   . TRP   A 1 227 ? 23.810 10.735  -12.341 1.00 12.51 ?  668  TRP   A N   1 
ATOM   1849 C  CA  . TRP   A 1 227 ? 24.886 11.711  -12.235 1.00 12.44 ?  668  TRP   A CA  1 
ATOM   1850 C  C   . TRP   A 1 227 ? 25.893 11.526  -13.362 1.00 14.47 ?  668  TRP   A C   1 
ATOM   1851 O  O   . TRP   A 1 227 ? 26.320 10.404  -13.662 1.00 13.88 ?  668  TRP   A O   1 
ATOM   1852 C  CB  . TRP   A 1 227 ? 25.630 11.555  -10.907 1.00 13.16 ?  668  TRP   A CB  1 
ATOM   1853 C  CG  . TRP   A 1 227 ? 24.800 11.727  -9.695  1.00 12.61 ?  668  TRP   A CG  1 
ATOM   1854 C  CD1 . TRP   A 1 227 ? 24.660 10.823  -8.682  1.00 14.05 ?  668  TRP   A CD1 1 
ATOM   1855 C  CD2 . TRP   A 1 227 ? 24.012 12.872  -9.319  1.00 12.68 ?  668  TRP   A CD2 1 
ATOM   1856 N  NE1 . TRP   A 1 227 ? 23.840 11.328  -7.709  1.00 11.94 ?  668  TRP   A NE1 1 
ATOM   1857 C  CE2 . TRP   A 1 227 ? 23.425 12.580  -8.074  1.00 12.95 ?  668  TRP   A CE2 1 
ATOM   1858 C  CE3 . TRP   A 1 227 ? 23.746 14.107  -9.914  1.00 14.29 ?  668  TRP   A CE3 1 
ATOM   1859 C  CZ2 . TRP   A 1 227 ? 22.588 13.475  -7.406  1.00 14.37 ?  668  TRP   A CZ2 1 
ATOM   1860 C  CZ3 . TRP   A 1 227 ? 22.911 14.997  -9.256  1.00 14.10 ?  668  TRP   A CZ3 1 
ATOM   1861 C  CH2 . TRP   A 1 227 ? 22.345 14.680  -8.012  1.00 15.72 ?  668  TRP   A CH2 1 
ATOM   1862 N  N   . ASN   A 1 228 ? 26.308 12.643  -13.953 1.00 15.45 ?  669  ASN   A N   1 
ATOM   1863 C  CA  . ASN   A 1 228 ? 27.274 12.645  -15.042 1.00 16.05 ?  669  ASN   A CA  1 
ATOM   1864 C  C   . ASN   A 1 228 ? 28.353 13.678  -14.757 1.00 17.54 ?  669  ASN   A C   1 
ATOM   1865 O  O   . ASN   A 1 228 ? 28.069 14.739  -14.191 1.00 20.11 ?  669  ASN   A O   1 
ATOM   1866 C  CB  . ASN   A 1 228 ? 26.612 13.014  -16.386 1.00 16.32 ?  669  ASN   A CB  1 
ATOM   1867 C  CG  . ASN   A 1 228 ? 25.465 12.086  -16.754 1.00 16.21 ?  669  ASN   A CG  1 
ATOM   1868 O  OD1 . ASN   A 1 228 ? 25.644 10.871  -16.849 1.00 17.41 ?  669  ASN   A OD1 1 
ATOM   1869 N  ND2 . ASN   A 1 228 ? 24.283 12.655  -16.965 1.00 16.88 ?  669  ASN   A ND2 1 
ATOM   1870 N  N   . GLY   A 1 229 ? 29.585 13.358  -15.145 0.89 16.70 ?  670  GLY   A N   1 
ATOM   1871 C  CA  . GLY   A 1 229 ? 30.655 14.335  -15.220 0.89 20.58 ?  670  GLY   A CA  1 
ATOM   1872 C  C   . GLY   A 1 229 ? 30.969 15.076  -13.939 0.89 25.01 ?  670  GLY   A C   1 
ATOM   1873 O  O   . GLY   A 1 229 ? 31.042 16.308  -13.933 0.89 28.68 ?  670  GLY   A O   1 
ATOM   1874 N  N   . GLY   A 1 230 ? 31.152 14.348  -12.844 1.00 24.91 ?  671  GLY   A N   1 
ATOM   1875 C  CA  . GLY   A 1 230 ? 31.489 14.999  -11.595 1.00 24.64 ?  671  GLY   A CA  1 
ATOM   1876 C  C   . GLY   A 1 230 ? 31.647 14.038  -10.438 1.00 23.40 ?  671  GLY   A C   1 
ATOM   1877 O  O   . GLY   A 1 230 ? 31.004 12.983  -10.405 1.00 22.23 ?  671  GLY   A O   1 
ATOM   1878 N  N   . LYS   A 1 231 ? 32.512 14.396  -9.491  1.00 20.30 ?  672  LYS   A N   1 
ATOM   1879 C  CA  . LYS   A 1 231 ? 32.705 13.636  -8.253  0.99 19.25 ?  672  LYS   A CA  1 
ATOM   1880 C  C   . LYS   A 1 231 ? 31.677 14.140  -7.246  1.00 18.16 ?  672  LYS   A C   1 
ATOM   1881 O  O   . LYS   A 1 231 ? 31.944 15.019  -6.423  0.73 19.07 ?  672  LYS   A O   1 
ATOM   1882 C  CB  . LYS   A 1 231 ? 34.139 13.802  -7.761  1.00 19.67 ?  672  LYS   A CB  1 
ATOM   1883 C  CG  . LYS   A 1 231 ? 34.438 13.145  -6.416  1.00 25.74 ?  672  LYS   A CG  1 
ATOM   1884 C  CD  . LYS   A 1 231 ? 35.785 13.603  -5.864  1.00 31.78 ?  672  LYS   A CD  1 
ATOM   1885 C  CE  . LYS   A 1 231 ? 36.447 12.520  -5.019  1.00 35.95 ?  672  LYS   A CE  1 
ATOM   1886 N  NZ  . LYS   A 1 231 ? 36.562 11.216  -5.739  1.00 38.23 ?  672  LYS   A NZ  1 
ATOM   1887 N  N   . MET   A 1 232 ? 30.481 13.567  -7.302  1.00 15.46 ?  673  MET   A N   1 
ATOM   1888 C  CA  . MET   A 1 232 ? 29.366 14.080  -6.529  1.00 14.06 ?  673  MET   A CA  1 
ATOM   1889 C  C   . MET   A 1 232 ? 29.541 13.755  -5.049  1.00 13.26 ?  673  MET   A C   1 
ATOM   1890 O  O   . MET   A 1 232 ? 30.232 12.805  -4.667  1.00 15.32 ?  673  MET   A O   1 
ATOM   1891 C  CB  . MET   A 1 232 ? 28.055 13.515  -7.065  1.00 12.44 ?  673  MET   A CB  1 
ATOM   1892 C  CG  . MET   A 1 232 ? 27.903 13.667  -8.580  1.00 14.02 ?  673  MET   A CG  1 
ATOM   1893 S  SD  . MET   A 1 232 ? 28.142 15.393  -9.074  1.00 17.24 ?  673  MET   A SD  1 
ATOM   1894 C  CE  . MET   A 1 232 ? 27.931 15.248  -10.854 1.00 14.38 ?  673  MET   A CE  1 
ATOM   1895 N  N   . GLY   A 1 233 ? 28.904 14.568  -4.210  1.00 12.41 ?  674  GLY   A N   1 
ATOM   1896 C  CA  . GLY   A 1 233 ? 29.027 14.421  -2.774  1.00 12.86 ?  674  GLY   A CA  1 
ATOM   1897 C  C   . GLY   A 1 233 ? 27.824 14.979  -2.047  1.00 12.83 ?  674  GLY   A C   1 
ATOM   1898 O  O   . GLY   A 1 233 ? 26.731 15.047  -2.624  1.00 13.59 ?  674  GLY   A O   1 
ATOM   1899 N  N   . ASP   A 1 234 ? 28.004 15.365  -0.774  1.00 12.22 ?  675  ASP   A N   1 
ATOM   1900 C  CA  . ASP   A 1 234 ? 26.898 15.869  0.040   1.00 13.67 ?  675  ASP   A CA  1 
ATOM   1901 C  C   . ASP   A 1 234 ? 26.084 16.980  -0.622  1.00 12.70 ?  675  ASP   A C   1 
ATOM   1902 O  O   . ASP   A 1 234 ? 24.847 16.909  -0.570  1.00 13.88 ?  675  ASP   A O   1 
ATOM   1903 C  CB  . ASP   A 1 234 ? 27.390 16.317  1.424   1.00 14.03 ?  675  ASP   A CB  1 
ATOM   1904 C  CG  . ASP   A 1 234 ? 27.958 15.183  2.259   1.00 14.58 ?  675  ASP   A CG  1 
ATOM   1905 O  OD1 . ASP   A 1 234 ? 27.944 14.001  1.846   1.00 13.80 ?  675  ASP   A OD1 1 
ATOM   1906 O  OD2 . ASP   A 1 234 ? 28.435 15.487  3.373   1.00 15.82 -1 675  ASP   A OD2 1 
ATOM   1907 N  N   . PRO   A 1 235 ? 26.683 18.027  -1.220  1.00 14.95 ?  676  PRO   A N   1 
ATOM   1908 C  CA  . PRO   A 1 235 ? 25.845 19.076  -1.834  1.00 16.27 ?  676  PRO   A CA  1 
ATOM   1909 C  C   . PRO   A 1 235 ? 24.882 18.543  -2.880  1.00 14.32 ?  676  PRO   A C   1 
ATOM   1910 O  O   . PRO   A 1 235 ? 23.700 18.913  -2.880  1.00 15.07 ?  676  PRO   A O   1 
ATOM   1911 C  CB  . PRO   A 1 235 ? 26.873 20.049  -2.439  1.00 16.26 ?  676  PRO   A CB  1 
ATOM   1912 C  CG  . PRO   A 1 235 ? 28.149 19.784  -1.693  1.00 15.02 ?  676  PRO   A CG  1 
ATOM   1913 C  CD  . PRO   A 1 235 ? 28.122 18.322  -1.366  1.00 15.90 ?  676  PRO   A CD  1 
ATOM   1914 N  N   . GLU   A 1 236 ? 25.355 17.660  -3.757  1.00 14.61 ?  677  GLU   A N   1 
ATOM   1915 C  CA  . GLU   A 1 236 ? 24.515 17.145  -4.831  1.00 14.65 ?  677  GLU   A CA  1 
ATOM   1916 C  C   . GLU   A 1 236 ? 23.427 16.227  -4.285  1.00 13.61 ?  677  GLU   A C   1 
ATOM   1917 O  O   . GLU   A 1 236 ? 22.276 16.291  -4.726  1.00 13.86 ?  677  GLU   A O   1 
ATOM   1918 C  CB  . GLU   A 1 236 ? 25.382 16.433  -5.868  1.00 15.45 ?  677  GLU   A CB  1 
ATOM   1919 C  CG  . GLU   A 1 236 ? 26.299 17.358  -6.669  1.00 15.33 ?  677  GLU   A CG  1 
ATOM   1920 C  CD  . GLU   A 1 236 ? 27.463 17.900  -5.865  1.00 17.44 ?  677  GLU   A CD  1 
ATOM   1921 O  OE1 . GLU   A 1 236 ? 27.947 17.201  -4.948  1.00 16.38 ?  677  GLU   A OE1 1 
ATOM   1922 O  OE2 . GLU   A 1 236 ? 27.898 19.032  -6.158  1.00 20.17 -1 677  GLU   A OE2 1 
ATOM   1923 N  N   . TYR   A 1 237 ? 23.760 15.386  -3.299  1.00 12.69 ?  678  TYR   A N   1 
ATOM   1924 C  CA  . TYR   A 1 237 ? 22.761 14.491  -2.726  1.00 14.75 ?  678  TYR   A CA  1 
ATOM   1925 C  C   . TYR   A 1 237 ? 21.704 15.248  -1.922  1.00 13.12 ?  678  TYR   A C   1 
ATOM   1926 O  O   . TYR   A 1 237 ? 20.508 14.933  -2.012  1.00 13.73 ?  678  TYR   A O   1 
ATOM   1927 C  CB  . TYR   A 1 237 ? 23.456 13.378  -1.937  1.00 12.55 ?  678  TYR   A CB  1 
ATOM   1928 C  CG  . TYR   A 1 237 ? 23.938 12.282  -2.854  1.00 11.94 ?  678  TYR   A CG  1 
ATOM   1929 C  CD1 . TYR   A 1 237 ? 25.043 12.461  -3.694  1.00 11.73 ?  678  TYR   A CD1 1 
ATOM   1930 C  CD2 . TYR   A 1 237 ? 23.265 11.085  -2.926  1.00 13.39 ?  678  TYR   A CD2 1 
ATOM   1931 C  CE1 . TYR   A 1 237 ? 25.464 11.465  -4.554  1.00 13.15 ?  678  TYR   A CE1 1 
ATOM   1932 C  CE2 . TYR   A 1 237 ? 23.676 10.081  -3.780  1.00 13.11 ?  678  TYR   A CE2 1 
ATOM   1933 C  CZ  . TYR   A 1 237 ? 24.777 10.274  -4.596  1.00 14.29 ?  678  TYR   A CZ  1 
ATOM   1934 O  OH  . TYR   A 1 237 ? 25.189 9.273   -5.454  1.00 14.12 ?  678  TYR   A OH  1 
ATOM   1935 N  N   . MET   A 1 238 ? 22.114 16.256  -1.138  1.00 12.93 ?  679  MET   A N   1 
ATOM   1936 C  CA  . MET   A 1 238 ? 21.140 17.076  -0.418  1.00 13.56 ?  679  MET   A CA  1 
ATOM   1937 C  C   . MET   A 1 238 ? 20.201 17.800  -1.380  1.00 14.41 ?  679  MET   A C   1 
ATOM   1938 O  O   . MET   A 1 238 ? 18.988 17.860  -1.145  1.00 15.57 ?  679  MET   A O   1 
ATOM   1939 C  CB  . MET   A 1 238 ? 21.867 18.078  0.478   1.00 14.60 ?  679  MET   A CB  1 
ATOM   1940 C  CG  . MET   A 1 238 ? 22.639 17.432  1.629   1.00 15.73 ?  679  MET   A CG  1 
ATOM   1941 S  SD  . MET   A 1 238 ? 21.625 16.524  2.792   1.00 19.23 ?  679  MET   A SD  1 
ATOM   1942 C  CE  . MET   A 1 238 ? 20.950 17.902  3.710   1.00 21.10 ?  679  MET   A CE  1 
ATOM   1943 N  N   . ALA   A 1 239 ? 20.745 18.358  -2.462  1.00 13.80 ?  680  ALA   A N   1 
ATOM   1944 C  CA  . ALA   A 1 239 ? 19.911 19.045  -3.445  1.00 14.17 ?  680  ALA   A CA  1 
ATOM   1945 C  C   . ALA   A 1 239 ? 18.929 18.091  -4.117  1.00 14.63 ?  680  ALA   A C   1 
ATOM   1946 O  O   . ALA   A 1 239 ? 17.758 18.438  -4.324  1.00 14.56 ?  680  ALA   A O   1 
ATOM   1947 C  CB  . ALA   A 1 239 ? 20.799 19.725  -4.482  1.00 13.76 ?  680  ALA   A CB  1 
ATOM   1948 N  N   . ALA   A 1 240 ? 19.385 16.889  -4.477  1.00 14.69 ?  681  ALA   A N   1 
ATOM   1949 C  CA  . ALA   A 1 240 ? 18.478 15.908  -5.065  1.00 13.53 ?  681  ALA   A CA  1 
ATOM   1950 C  C   . ALA   A 1 240 ? 17.367 15.531  -4.091  1.00 13.07 ?  681  ALA   A C   1 
ATOM   1951 O  O   . ALA   A 1 240 ? 16.213 15.351  -4.490  1.00 14.31 ?  681  ALA   A O   1 
ATOM   1952 C  CB  . ALA   A 1 240 ? 19.271 14.681  -5.498  1.00 14.73 ?  681  ALA   A CB  1 
ATOM   1953 N  N   . PHE   A 1 241 ? 17.688 15.416  -2.806  1.00 13.61 ?  682  PHE   A N   1 
ATOM   1954 C  CA  . PHE   A 1 241 ? 16.656 15.089  -1.833  1.00 13.17 ?  682  PHE   A CA  1 
ATOM   1955 C  C   . PHE   A 1 241 ? 15.656 16.229  -1.668  1.00 15.12 ?  682  PHE   A C   1 
ATOM   1956 O  O   . PHE   A 1 241 ? 14.449 15.990  -1.535  1.00 14.42 ?  682  PHE   A O   1 
ATOM   1957 C  CB  . PHE   A 1 241 ? 17.299 14.722  -0.493  1.00 15.11 ?  682  PHE   A CB  1 
ATOM   1958 C  CG  . PHE   A 1 241 ? 17.431 13.246  -0.278  1.00 14.49 ?  682  PHE   A CG  1 
ATOM   1959 C  CD1 . PHE   A 1 241 ? 18.158 12.467  -1.169  1.00 12.66 ?  682  PHE   A CD1 1 
ATOM   1960 C  CD2 . PHE   A 1 241 ? 16.810 12.634  0.793   1.00 14.11 ?  682  PHE   A CD2 1 
ATOM   1961 C  CE1 . PHE   A 1 241 ? 18.261 11.094  -0.972  1.00 15.33 ?  682  PHE   A CE1 1 
ATOM   1962 C  CE2 . PHE   A 1 241 ? 16.913 11.272  0.997   1.00 14.61 ?  682  PHE   A CE2 1 
ATOM   1963 C  CZ  . PHE   A 1 241 ? 17.647 10.503  0.111   1.00 15.08 ?  682  PHE   A CZ  1 
ATOM   1964 N  N   . HIS   A 1 242 ? 16.146 17.472  -1.665  1.00 15.80 ?  683  HIS   A N   1 
ATOM   1965 C  CA  . HIS   A 1 242 ? 15.270 18.616  -1.446  1.00 17.01 ?  683  HIS   A CA  1 
ATOM   1966 C  C   . HIS   A 1 242 ? 14.349 18.850  -2.641  1.00 17.89 ?  683  HIS   A C   1 
ATOM   1967 O  O   . HIS   A 1 242 ? 13.156 19.132  -2.467  1.00 17.99 ?  683  HIS   A O   1 
ATOM   1968 C  CB  . HIS   A 1 242 ? 16.116 19.860  -1.188  1.00 20.44 ?  683  HIS   A CB  1 
ATOM   1969 C  CG  . HIS   A 1 242 ? 15.309 21.066  -0.825  1.00 26.98 ?  683  HIS   A CG  1 
ATOM   1970 N  ND1 . HIS   A 1 242 ? 14.961 21.364  0.475   1.00 31.52 ?  683  HIS   A ND1 1 
ATOM   1971 C  CD2 . HIS   A 1 242 ? 14.756 22.034  -1.594  1.00 29.32 ?  683  HIS   A CD2 1 
ATOM   1972 C  CE1 . HIS   A 1 242 ? 14.241 22.472  0.492   1.00 32.20 ?  683  HIS   A CE1 1 
ATOM   1973 N  NE2 . HIS   A 1 242 ? 14.099 22.897  -0.751  1.00 31.34 ?  683  HIS   A NE2 1 
ATOM   1974 N  N   . HIS   A 1 243 ? 14.878 18.731  -3.854  1.00 16.94 ?  684  HIS   A N   1 
ATOM   1975 C  CA  . HIS   A 1 243 ? 14.104 19.060  -5.045  1.00 17.97 ?  684  HIS   A CA  1 
ATOM   1976 C  C   . HIS   A 1 243 ? 13.357 17.873  -5.645  1.00 19.78 ?  684  HIS   A C   1 
ATOM   1977 O  O   . HIS   A 1 243 ? 12.348 18.083  -6.329  1.00 20.75 ?  684  HIS   A O   1 
ATOM   1978 C  CB  . HIS   A 1 243 ? 15.015 19.679  -6.110  1.00 21.46 ?  684  HIS   A CB  1 
ATOM   1979 C  CG  . HIS   A 1 243 ? 15.660 20.961  -5.686  1.00 27.80 ?  684  HIS   A CG  1 
ATOM   1980 N  ND1 . HIS   A 1 243 ? 14.936 22.064  -5.287  1.00 31.21 ?  684  HIS   A ND1 1 
ATOM   1981 C  CD2 . HIS   A 1 243 ? 16.964 21.315  -5.594  1.00 30.63 ?  684  HIS   A CD2 1 
ATOM   1982 C  CE1 . HIS   A 1 243 ? 15.766 23.041  -4.968  1.00 32.80 ?  684  HIS   A CE1 1 
ATOM   1983 N  NE2 . HIS   A 1 243 ? 17.002 22.612  -5.145  1.00 32.57 ?  684  HIS   A NE2 1 
ATOM   1984 N  N   . LEU   A 1 244 ? 13.819 16.640  -5.427  1.00 17.48 ?  685  LEU   A N   1 
ATOM   1985 C  CA  . LEU   A 1 244 ? 13.231 15.477  -6.090  1.00 16.80 ?  685  LEU   A CA  1 
ATOM   1986 C  C   . LEU   A 1 244 ? 12.739 14.423  -5.108  1.00 16.52 ?  685  LEU   A C   1 
ATOM   1987 O  O   . LEU   A 1 244 ? 11.543 14.120  -5.091  1.00 16.67 ?  685  LEU   A O   1 
ATOM   1988 C  CB  . LEU   A 1 244 ? 14.238 14.868  -7.075  1.00 16.93 ?  685  LEU   A CB  1 
ATOM   1989 C  CG  . LEU   A 1 244 ? 14.594 15.700  -8.310  1.00 16.83 ?  685  LEU   A CG  1 
ATOM   1990 C  CD1 . LEU   A 1 244 ? 15.843 15.155  -8.961  1.00 14.73 ?  685  LEU   A CD1 1 
ATOM   1991 C  CD2 . LEU   A 1 244 ? 13.440 15.704  -9.303  1.00 18.39 ?  685  LEU   A CD2 1 
ATOM   1992 N  N   . VAL   A 1 245 ? 13.621 13.855  -4.286  1.00 15.20 ?  686  VAL   A N   1 
ATOM   1993 C  CA  . VAL   A 1 245 ? 13.250 12.665  -3.527  1.00 12.81 ?  686  VAL   A CA  1 
ATOM   1994 C  C   . VAL   A 1 245 ? 12.142 12.987  -2.537  1.00 14.05 ?  686  VAL   A C   1 
ATOM   1995 O  O   . VAL   A 1 245 ? 11.133 12.280  -2.452  1.00 15.06 ?  686  VAL   A O   1 
ATOM   1996 C  CB  . VAL   A 1 245 ? 14.481 12.056  -2.828  1.00 14.30 ?  686  VAL   A CB  1 
ATOM   1997 C  CG1 . VAL   A 1 245 ? 14.100 10.775  -2.078  1.00 15.32 ?  686  VAL   A CG1 1 
ATOM   1998 C  CG2 . VAL   A 1 245 ? 15.601 11.801  -3.827  1.00 13.24 ?  686  VAL   A CG2 1 
ATOM   1999 N  N   . MET   A 1 246 ? 12.327 14.040  -1.746  1.00 14.85 ?  687  MET   A N   1 
ATOM   2000 C  CA  . MET   A 1 246 ? 11.363 14.283  -0.679  1.00 14.36 ?  687  MET   A CA  1 
ATOM   2001 C  C   . MET   A 1 246 ? 10.014 14.776  -1.202  1.00 15.26 ?  687  MET   A C   1 
ATOM   2002 O  O   . MET   A 1 246 ? 8.981  14.290  -0.734  1.00 16.34 ?  687  MET   A O   1 
ATOM   2003 C  CB  . MET   A 1 246 ? 11.948 15.163  0.429   1.00 14.77 ?  687  MET   A CB  1 
ATOM   2004 C  CG  . MET   A 1 246 ? 13.146 14.505  1.132   1.00 14.69 ?  687  MET   A CG  1 
ATOM   2005 S  SD  . MET   A 1 246 ? 12.762 12.893  1.844   1.00 17.80 ?  687  MET   A SD  1 
ATOM   2006 C  CE  . MET   A 1 246 ? 11.499 13.378  3.020   1.00 17.63 ?  687  MET   A CE  1 
ATOM   2007 N  N   . PRO   A 1 247 ? 9.956  15.720  -2.147  1.00 15.73 ?  688  PRO   A N   1 
ATOM   2008 C  CA  . PRO   A 1 247 ? 8.628  16.097  -2.668  1.00 16.19 ?  688  PRO   A CA  1 
ATOM   2009 C  C   . PRO   A 1 247 ? 7.875  14.937  -3.305  1.00 15.45 ?  688  PRO   A C   1 
ATOM   2010 O  O   . PRO   A 1 247 ? 6.683  14.752  -3.025  1.00 16.31 ?  688  PRO   A O   1 
ATOM   2011 C  CB  . PRO   A 1 247 ? 8.939  17.212  -3.677  1.00 18.37 ?  688  PRO   A CB  1 
ATOM   2012 C  CG  . PRO   A 1 247 ? 10.251 17.779  -3.225  1.00 19.78 ?  688  PRO   A CG  1 
ATOM   2013 C  CD  . PRO   A 1 247 ? 11.017 16.607  -2.667  1.00 16.38 ?  688  PRO   A CD  1 
ATOM   2014 N  N   . ILE   A 1 248 ? 8.548  14.121  -4.117  1.00 15.58 ?  689  ILE   A N   1 
ATOM   2015 C  CA  . ILE   A 1 248 ? 7.877  12.968  -4.718  1.00 15.28 ?  689  ILE   A CA  1 
ATOM   2016 C  C   . ILE   A 1 248 ? 7.424  11.991  -3.643  1.00 16.61 ?  689  ILE   A C   1 
ATOM   2017 O  O   . ILE   A 1 248 ? 6.274  11.530  -3.637  1.00 15.86 ?  689  ILE   A O   1 
ATOM   2018 C  CB  . ILE   A 1 248 ? 8.791  12.297  -5.758  1.00 13.59 ?  689  ILE   A CB  1 
ATOM   2019 C  CG1 . ILE   A 1 248 ? 9.052  13.251  -6.917  1.00 14.09 ?  689  ILE   A CG1 1 
ATOM   2020 C  CG2 . ILE   A 1 248 ? 8.178  10.982  -6.233  1.00 17.08 ?  689  ILE   A CG2 1 
ATOM   2021 C  CD1 . ILE   A 1 248 ? 10.049 12.742  -7.937  1.00 15.43 ?  689  ILE   A CD1 1 
ATOM   2022 N  N   . ALA   A 1 249 ? 8.323  11.665  -2.708  1.00 14.76 ?  690  ALA   A N   1 
ATOM   2023 C  CA  . ALA   A 1 249 ? 7.990  10.717  -1.651  1.00 15.29 ?  690  ALA   A CA  1 
ATOM   2024 C  C   . ALA   A 1 249 ? 6.785  11.183  -0.837  1.00 15.11 ?  690  ALA   A C   1 
ATOM   2025 O  O   . ALA   A 1 249 ? 5.894  10.387  -0.521  1.00 15.10 ?  690  ALA   A O   1 
ATOM   2026 C  CB  . ALA   A 1 249 ? 9.207  10.489  -0.749  1.00 14.53 ?  690  ALA   A CB  1 
ATOM   2027 N  N   . ARG   A 1 250 ? 6.760  12.466  -0.455  1.00 15.83 ?  691  ARG   A N   1 
ATOM   2028 C  CA  . ARG   A 1 250 ? 5.654  12.971  0.357   1.00 15.46 ?  691  ARG   A CA  1 
ATOM   2029 C  C   . ARG   A 1 250 ? 4.333  12.884  -0.396  1.00 15.54 ?  691  ARG   A C   1 
ATOM   2030 O  O   . ARG   A 1 250 ? 3.285  12.600  0.199   1.00 18.61 ?  691  ARG   A O   1 
ATOM   2031 C  CB  . ARG   A 1 250 ? 5.924  14.414  0.771   1.00 17.02 ?  691  ARG   A CB  1 
ATOM   2032 C  CG  . ARG   A 1 250 ? 6.893  14.547  1.920   1.00 21.93 ?  691  ARG   A CG  1 
ATOM   2033 C  CD  . ARG   A 1 250 ? 6.927  15.980  2.405   1.00 25.66 ?  691  ARG   A CD  1 
ATOM   2034 N  NE  . ARG   A 1 250 ? 7.603  16.833  1.436   1.00 27.81 ?  691  ARG   A NE  1 
ATOM   2035 C  CZ  . ARG   A 1 250 ? 8.863  17.241  1.554   1.00 27.15 ?  691  ARG   A CZ  1 
ATOM   2036 N  NH1 . ARG   A 1 250 ? 9.577  16.871  2.608   1.00 26.22 ?  691  ARG   A NH1 1 
ATOM   2037 N  NH2 . ARG   A 1 250 ? 9.404  18.013  0.618   1.00 24.78 ?  691  ARG   A NH2 1 
ATOM   2038 N  N   . GLU   A 1 251 ? 4.364  13.138  -1.706  1.00 15.86 ?  692  GLU   A N   1 
ATOM   2039 C  CA  . GLU   A 1 251 ? 3.141  13.057  -2.500  1.00 17.99 ?  692  GLU   A CA  1 
ATOM   2040 C  C   . GLU   A 1 251 ? 2.673  11.613  -2.631  1.00 18.61 ?  692  GLU   A C   1 
ATOM   2041 O  O   . GLU   A 1 251 ? 1.470  11.334  -2.589  1.00 21.25 ?  692  GLU   A O   1 
ATOM   2042 C  CB  . GLU   A 1 251 ? 3.392  13.669  -3.880  1.00 18.46 ?  692  GLU   A CB  1 
ATOM   2043 C  CG  . GLU   A 1 251 ? 2.130  13.859  -4.720  1.00 21.79 ?  692  GLU   A CG  1 
ATOM   2044 C  CD  . GLU   A 1 251 ? 2.357  14.650  -6.002  1.00 23.90 ?  692  GLU   A CD  1 
ATOM   2045 O  OE1 . GLU   A 1 251 ? 3.394  15.340  -6.133  1.00 21.02 ?  692  GLU   A OE1 1 
ATOM   2046 O  OE2 . GLU   A 1 251 ? 1.480  14.579  -6.892  1.00 26.95 -1 692  GLU   A OE2 1 
ATOM   2047 N  N   . PHE   A 1 252 ? 3.617  10.684  -2.797  1.00 14.93 ?  693  PHE   A N   1 
ATOM   2048 C  CA  . PHE   A 1 252 ? 3.298  9.261   -2.808  1.00 15.04 ?  693  PHE   A CA  1 
ATOM   2049 C  C   . PHE   A 1 252 ? 2.743  8.792   -1.463  1.00 16.63 ?  693  PHE   A C   1 
ATOM   2050 O  O   . PHE   A 1 252 ? 1.899  7.890   -1.421  1.00 16.62 ?  693  PHE   A O   1 
ATOM   2051 C  CB  . PHE   A 1 252 ? 4.564  8.495   -3.205  1.00 14.49 ?  693  PHE   A CB  1 
ATOM   2052 C  CG  . PHE   A 1 252 ? 4.396  6.998   -3.276  1.00 14.05 ?  693  PHE   A CG  1 
ATOM   2053 C  CD1 . PHE   A 1 252 ? 3.575  6.415   -4.235  1.00 15.45 ?  693  PHE   A CD1 1 
ATOM   2054 C  CD2 . PHE   A 1 252 ? 5.097  6.172   -2.405  1.00 15.04 ?  693  PHE   A CD2 1 
ATOM   2055 C  CE1 . PHE   A 1 252 ? 3.442  5.042   -4.301  1.00 15.06 ?  693  PHE   A CE1 1 
ATOM   2056 C  CE2 . PHE   A 1 252 ? 4.975  4.799   -2.467  1.00 15.25 ?  693  PHE   A CE2 1 
ATOM   2057 C  CZ  . PHE   A 1 252 ? 4.150  4.231   -3.416  1.00 15.46 ?  693  PHE   A CZ  1 
ATOM   2058 N  N   . ALA   A 1 253 ? 3.200  9.392   -0.352  1.00 15.59 ?  694  ALA   A N   1 
ATOM   2059 C  CA  . ALA   A 1 253 ? 2.759  9.052   0.998   1.00 16.08 ?  694  ALA   A CA  1 
ATOM   2060 C  C   . ALA   A 1 253 ? 2.955  7.568   1.274   1.00 16.24 ?  694  ALA   A C   1 
ATOM   2061 O  O   . ALA   A 1 253 ? 1.983  6.834   1.493   1.00 17.62 ?  694  ALA   A O   1 
ATOM   2062 C  CB  . ALA   A 1 253 ? 1.307  9.481   1.240   1.00 17.43 ?  694  ALA   A CB  1 
ATOM   2063 N  N   . PRO   A 1 254 ? 4.199  7.089   1.292   1.00 14.79 ?  695  PRO   A N   1 
ATOM   2064 C  CA  . PRO   A 1 254 ? 4.429  5.662   1.526   1.00 13.22 ?  695  PRO   A CA  1 
ATOM   2065 C  C   . PRO   A 1 254 ? 3.971  5.237   2.911   1.00 13.55 ?  695  PRO   A C   1 
ATOM   2066 O  O   . PRO   A 1 254 ? 3.948  6.028   3.859   1.00 15.23 ?  695  PRO   A O   1 
ATOM   2067 C  CB  . PRO   A 1 254 ? 5.953  5.518   1.380   1.00 13.90 ?  695  PRO   A CB  1 
ATOM   2068 C  CG  . PRO   A 1 254 ? 6.490  6.877   1.733   1.00 16.37 ?  695  PRO   A CG  1 
ATOM   2069 C  CD  . PRO   A 1 254 ? 5.452  7.861   1.245   1.00 17.15 ?  695  PRO   A CD  1 
ATOM   2070 N  N   . GLU   A 1 255 ? 3.607  3.962   3.020   1.00 15.05 ?  696  GLU   A N   1 
ATOM   2071 C  CA  . GLU   A 1 255 ? 3.331  3.334   4.301   1.00 16.55 ?  696  GLU   A CA  1 
ATOM   2072 C  C   . GLU   A 1 255 ? 4.532  2.569   4.848   1.00 14.20 ?  696  GLU   A C   1 
ATOM   2073 O  O   . GLU   A 1 255 ? 4.534  2.199   6.025   1.00 18.32 ?  696  GLU   A O   1 
ATOM   2074 C  CB  . GLU   A 1 255 ? 2.112  2.410   4.161   1.00 18.12 ?  696  GLU   A CB  1 
ATOM   2075 C  CG  . GLU   A 1 255 ? 0.839  3.188   3.776   1.00 21.99 ?  696  GLU   A CG  1 
ATOM   2076 C  CD  . GLU   A 1 255 ? -0.283 2.310   3.252   1.00 28.71 ?  696  GLU   A CD  1 
ATOM   2077 O  OE1 . GLU   A 1 255 ? -0.220 1.912   2.074   1.00 21.92 ?  696  GLU   A OE1 1 
ATOM   2078 O  OE2 . GLU   A 1 255 ? -1.232 2.024   4.016   1.00 36.25 -1 696  GLU   A OE2 1 
ATOM   2079 N  N   . LEU   A 1 256 ? 5.550  2.342   4.021   1.00 12.55 ?  697  LEU   A N   1 
ATOM   2080 C  CA  . LEU   A 1 256 ? 6.796  1.717   4.431   1.00 12.51 ?  697  LEU   A CA  1 
ATOM   2081 C  C   . LEU   A 1 256 ? 7.886  2.261   3.521   1.00 13.11 ?  697  LEU   A C   1 
ATOM   2082 O  O   . LEU   A 1 256 ? 7.679  2.395   2.312   1.00 13.76 ?  697  LEU   A O   1 
ATOM   2083 C  CB  . LEU   A 1 256 ? 6.716  0.199   4.254   1.00 13.34 ?  697  LEU   A CB  1 
ATOM   2084 C  CG  . LEU   A 1 256 ? 7.984  -0.598  4.568   1.00 13.53 ?  697  LEU   A CG  1 
ATOM   2085 C  CD1 . LEU   A 1 256 ? 8.362  -0.444  6.046   1.00 14.04 ?  697  LEU   A CD1 1 
ATOM   2086 C  CD2 . LEU   A 1 256 ? 7.845  -2.067  4.184   1.00 16.31 ?  697  LEU   A CD2 1 
ATOM   2087 N  N   . VAL   A 1 257 ? 9.041  2.580   4.098   1.00 13.59 ?  698  VAL   A N   1 
ATOM   2088 C  CA  . VAL   A 1 257 ? 10.198 3.029   3.325   1.00 11.44 ?  698  VAL   A CA  1 
ATOM   2089 C  C   . VAL   A 1 257 ? 11.292 1.988   3.476   1.00 10.73 ?  698  VAL   A C   1 
ATOM   2090 O  O   . VAL   A 1 257 ? 11.690 1.648   4.600   1.00 12.53 ?  698  VAL   A O   1 
ATOM   2091 C  CB  . VAL   A 1 257 ? 10.717 4.398   3.794   1.00 14.32 ?  698  VAL   A CB  1 
ATOM   2092 C  CG1 . VAL   A 1 257 ? 11.975 4.781   3.018   1.00 14.86 ?  698  VAL   A CG1 1 
ATOM   2093 C  CG2 . VAL   A 1 257 ? 9.638  5.463   3.672   1.00 17.00 ?  698  VAL   A CG2 1 
ATOM   2094 N  N   . LEU   A 1 258 ? 11.778 1.484   2.346   1.00 11.42 ?  699  LEU   A N   1 
ATOM   2095 C  CA  . LEU   A 1 258 ? 12.959 0.636   2.302   1.00 10.95 ?  699  LEU   A CA  1 
ATOM   2096 C  C   . LEU   A 1 258 ? 14.082 1.442   1.675   1.00 11.50 ?  699  LEU   A C   1 
ATOM   2097 O  O   . LEU   A 1 258 ? 13.880 2.086   0.640   1.00 12.33 ?  699  LEU   A O   1 
ATOM   2098 C  CB  . LEU   A 1 258 ? 12.698 -0.603  1.445   1.00 9.80  ?  699  LEU   A CB  1 
ATOM   2099 C  CG  . LEU   A 1 258 ? 11.464 -1.444  1.800   1.00 12.06 ?  699  LEU   A CG  1 
ATOM   2100 C  CD1 . LEU   A 1 258 ? 11.337 -2.649  0.889   1.00 11.76 ?  699  LEU   A CD1 1 
ATOM   2101 C  CD2 . LEU   A 1 258 ? 11.534 -1.885  3.262   1.00 12.76 ?  699  LEU   A CD2 1 
ATOM   2102 N  N   . VAL   A 1 259 ? 15.260 1.406   2.284   1.00 10.56 ?  700  VAL   A N   1 
ATOM   2103 C  CA  . VAL   A 1 259 ? 16.438 2.028   1.700   1.00 10.60 ?  700  VAL   A CA  1 
ATOM   2104 C  C   . VAL   A 1 259 ? 17.358 0.935   1.198   1.00 9.60  ?  700  VAL   A C   1 
ATOM   2105 O  O   . VAL   A 1 259 ? 17.831 0.097   1.982   1.00 10.23 ?  700  VAL   A O   1 
ATOM   2106 C  CB  . VAL   A 1 259 ? 17.172 2.952   2.679   1.00 10.70 ?  700  VAL   A CB  1 
ATOM   2107 C  CG1 . VAL   A 1 259 ? 18.268 3.713   1.932   1.00 11.42 ?  700  VAL   A CG1 1 
ATOM   2108 C  CG2 . VAL   A 1 259 ? 16.203 3.924   3.342   1.00 12.04 ?  700  VAL   A CG2 1 
ATOM   2109 N  N   . SER   A 1 260 ? 17.588 0.933   -0.117  1.00 9.85  ?  701  SER   A N   1 
ATOM   2110 C  CA  . SER   A 1 260 ? 18.676 0.156   -0.712  1.00 10.49 ?  701  SER   A CA  1 
ATOM   2111 C  C   . SER   A 1 260 ? 19.952 0.933   -0.428  1.00 9.95  ?  701  SER   A C   1 
ATOM   2112 O  O   . SER   A 1 260 ? 20.391 1.786   -1.203  1.00 11.47 ?  701  SER   A O   1 
ATOM   2113 C  CB  . SER   A 1 260 ? 18.427 -0.095  -2.193  1.00 10.46 ?  701  SER   A CB  1 
ATOM   2114 O  OG  . SER   A 1 260 ? 17.739 -1.329  -2.343  1.00 12.31 ?  701  SER   A OG  1 
ATOM   2115 N  N   . ALA   A 1 261 ? 20.517 0.655   0.746   1.00 9.97  ?  702  ALA   A N   1 
ATOM   2116 C  CA  . ALA   A 1 261 ? 21.569 1.477   1.338   1.00 10.37 ?  702  ALA   A CA  1 
ATOM   2117 C  C   . ALA   A 1 261 ? 22.942 0.888   1.021   1.00 9.69  ?  702  ALA   A C   1 
ATOM   2118 O  O   . ALA   A 1 261 ? 23.603 0.258   1.855   1.00 11.00 ?  702  ALA   A O   1 
ATOM   2119 C  CB  . ALA   A 1 261 ? 21.324 1.622   2.834   1.00 9.70  ?  702  ALA   A CB  1 
ATOM   2120 N  N   . GLY   A 1 262 ? 23.364 1.076   -0.227  1.00 9.12  ?  703  GLY   A N   1 
ATOM   2121 C  CA  . GLY   A 1 262 ? 24.750 0.884   -0.549  1.00 9.49  ?  703  GLY   A CA  1 
ATOM   2122 C  C   . GLY   A 1 262 ? 25.552 2.071   -0.064  1.00 11.18 ?  703  GLY   A C   1 
ATOM   2123 O  O   . GLY   A 1 262 ? 25.057 3.198   -0.002  1.00 13.59 ?  703  GLY   A O   1 
ATOM   2124 N  N   . PHE   A 1 263 ? 26.800 1.810   0.308   1.00 10.34 ?  704  PHE   A N   1 
ATOM   2125 C  CA  . PHE   A 1 263 ? 27.699 2.861   0.778   1.00 9.28  ?  704  PHE   A CA  1 
ATOM   2126 C  C   . PHE   A 1 263 ? 28.912 3.012   -0.133  1.00 9.21  ?  704  PHE   A C   1 
ATOM   2127 O  O   . PHE   A 1 263 ? 29.994 3.420   0.299   1.00 11.26 ?  704  PHE   A O   1 
ATOM   2128 C  CB  . PHE   A 1 263 ? 28.039 2.710   2.265   1.00 9.55  ?  704  PHE   A CB  1 
ATOM   2129 C  CG  . PHE   A 1 263 ? 26.825 2.797   3.153   1.00 9.33  ?  704  PHE   A CG  1 
ATOM   2130 C  CD1 . PHE   A 1 263 ? 26.261 4.029   3.451   1.00 10.45 ?  704  PHE   A CD1 1 
ATOM   2131 C  CD2 . PHE   A 1 263 ? 26.210 1.646   3.619   1.00 9.51  ?  704  PHE   A CD2 1 
ATOM   2132 C  CE1 . PHE   A 1 263 ? 25.118 4.113   4.246   1.00 9.67  ?  704  PHE   A CE1 1 
ATOM   2133 C  CE2 . PHE   A 1 263 ? 25.061 1.721   4.392   1.00 10.85 ?  704  PHE   A CE2 1 
ATOM   2134 C  CZ  . PHE   A 1 263 ? 24.519 2.961   4.715   1.00 10.74 ?  704  PHE   A CZ  1 
ATOM   2135 N  N   . ASP   A 1 264 ? 28.722 2.710   -1.422  1.00 9.12  ?  705  ASP   A N   1 
ATOM   2136 C  CA  . ASP   A 1 264 ? 29.771 2.846   -2.424  1.00 9.92  ?  705  ASP   A CA  1 
ATOM   2137 C  C   . ASP   A 1 264 ? 29.827 4.232   -3.062  1.00 10.03 ?  705  ASP   A C   1 
ATOM   2138 O  O   . ASP   A 1 264 ? 30.765 4.505   -3.821  1.00 10.87 ?  705  ASP   A O   1 
ATOM   2139 C  CB  . ASP   A 1 264 ? 29.740 1.713   -3.471  1.00 9.98  ?  705  ASP   A CB  1 
ATOM   2140 C  CG  . ASP   A 1 264 ? 28.350 1.328   -3.912  1.00 8.75  ?  705  ASP   A CG  1 
ATOM   2141 O  OD1 . ASP   A 1 264 ? 27.377 2.063   -3.599  1.00 11.52 ?  705  ASP   A OD1 1 
ATOM   2142 O  OD2 . ASP   A 1 264 ? 28.245 0.284   -4.627  1.00 10.85 -1 705  ASP   A OD2 1 
ATOM   2143 N  N   . ALA   A 1 265 ? 28.887 5.127   -2.749  1.00 9.80  ?  706  ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 265 ? 29.070 6.540   -3.074  1.00 11.03 ?  706  ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 265 ? 29.886 7.266   -2.020  1.00 10.56 ?  706  ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 265 ? 30.067 8.485   -2.113  1.00 12.19 ?  706  ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 265 ? 27.729 7.252   -3.269  1.00 10.74 ?  706  ALA   A CB  1 
ATOM   2148 N  N   . ALA   A 1 266 ? 30.372 6.545   -1.019  1.00 10.32 ?  707  ALA   A N   1 
ATOM   2149 C  CA  . ALA   A 1 266 ? 31.028 7.183   0.104   1.00 9.92  ?  707  ALA   A CA  1 
ATOM   2150 C  C   . ALA   A 1 266 ? 32.435 7.624   -0.254  1.00 10.55 ?  707  ALA   A C   1 
ATOM   2151 O  O   . ALA   A 1 266 ? 33.127 6.997   -1.063  1.00 11.14 ?  707  ALA   A O   1 
ATOM   2152 C  CB  . ALA   A 1 266 ? 31.169 6.184   1.248   1.00 12.13 ?  707  ALA   A CB  1 
ATOM   2153 N  N   A ARG   A 1 267 ? 32.860 8.710   0.383   0.64 11.98 ?  708  ARG   A N   1 
ATOM   2154 N  N   B ARG   A 1 267 ? 32.875 8.698   0.397   0.36 11.79 ?  708  ARG   A N   1 
ATOM   2155 C  CA  A ARG   A 1 267 ? 34.268 9.079   0.375   0.64 12.54 ?  708  ARG   A CA  1 
ATOM   2156 C  CA  B ARG   A 1 267 ? 34.273 9.098   0.307   0.36 12.89 ?  708  ARG   A CA  1 
ATOM   2157 C  C   A ARG   A 1 267 ? 35.114 7.873   0.767   0.64 10.81 ?  708  ARG   A C   1 
ATOM   2158 C  C   B ARG   A 1 267 ? 35.166 7.962   0.793   0.36 11.82 ?  708  ARG   A C   1 
ATOM   2159 O  O   A ARG   A 1 267 ? 34.837 7.204   1.766   0.64 11.83 ?  708  ARG   A O   1 
ATOM   2160 O  O   B ARG   A 1 267 ? 34.985 7.441   1.897   0.36 12.95 ?  708  ARG   A O   1 
ATOM   2161 C  CB  A ARG   A 1 267 ? 34.480 10.210  1.380   0.64 15.04 ?  708  ARG   A CB  1 
ATOM   2162 C  CB  B ARG   A 1 267 ? 34.511 10.350  1.150   0.36 15.40 ?  708  ARG   A CB  1 
ATOM   2163 C  CG  A ARG   A 1 267 ? 35.887 10.774  1.425   0.64 15.30 ?  708  ARG   A CG  1 
ATOM   2164 C  CG  B ARG   A 1 267 ? 35.954 10.834  1.156   0.36 16.90 ?  708  ARG   A CG  1 
ATOM   2165 C  CD  A ARG   A 1 267 ? 36.036 11.736  2.601   0.64 17.44 ?  708  ARG   A CD  1 
ATOM   2166 C  CD  B ARG   A 1 267 ? 36.083 12.206  1.808   0.36 18.53 ?  708  ARG   A CD  1 
ATOM   2167 N  NE  A ARG   A 1 267 ? 35.747 11.063  3.860   0.64 18.31 ?  708  ARG   A NE  1 
ATOM   2168 N  NE  B ARG   A 1 267 ? 35.611 13.278  0.933   0.36 19.65 ?  708  ARG   A NE  1 
ATOM   2169 C  CZ  A ARG   A 1 267 ? 35.118 11.621  4.890   0.64 19.94 ?  708  ARG   A CZ  1 
ATOM   2170 C  CZ  B ARG   A 1 267 ? 35.173 14.457  1.361   0.36 18.75 ?  708  ARG   A CZ  1 
ATOM   2171 N  NH1 A ARG   A 1 267 ? 34.698 12.877  4.826   0.64 20.11 ?  708  ARG   A NH1 1 
ATOM   2172 N  NH1 B ARG   A 1 267 ? 35.136 14.728  2.661   0.36 17.35 ?  708  ARG   A NH1 1 
ATOM   2173 N  NH2 A ARG   A 1 267 ? 34.904 10.915  5.987   0.64 20.59 ?  708  ARG   A NH2 1 
ATOM   2174 N  NH2 B ARG   A 1 267 ? 34.764 15.365  0.487   0.36 18.12 ?  708  ARG   A NH2 1 
ATOM   2175 N  N   . GLY   A 1 268 ? 36.122 7.570   -0.045  1.00 13.09 ?  709  GLY   A N   1 
ATOM   2176 C  CA  . GLY   A 1 268 ? 37.002 6.457   0.225   1.00 11.83 ?  709  GLY   A CA  1 
ATOM   2177 C  C   . GLY   A 1 268 ? 36.669 5.177   -0.515  1.00 11.72 ?  709  GLY   A C   1 
ATOM   2178 O  O   . GLY   A 1 268 ? 37.493 4.258   -0.520  1.00 11.78 ?  709  GLY   A O   1 
ATOM   2179 N  N   . ASP   A 1 269 ? 35.500 5.079   -1.148  1.00 12.40 ?  710  ASP   A N   1 
ATOM   2180 C  CA  . ASP   A 1 269 ? 35.170 3.828   -1.819  1.00 12.03 ?  710  ASP   A CA  1 
ATOM   2181 C  C   . ASP   A 1 269 ? 36.144 3.552   -2.967  1.00 13.17 ?  710  ASP   A C   1 
ATOM   2182 O  O   . ASP   A 1 269 ? 36.491 4.465   -3.713  1.00 14.25 ?  710  ASP   A O   1 
ATOM   2183 C  CB  . ASP   A 1 269 ? 33.740 3.845   -2.358  1.00 11.17 ?  710  ASP   A CB  1 
ATOM   2184 C  CG  . ASP   A 1 269 ? 33.272 2.464   -2.744  1.00 11.76 ?  710  ASP   A CG  1 
ATOM   2185 O  OD1 . ASP   A 1 269 ? 32.866 1.689   -1.852  1.00 11.56 ?  710  ASP   A OD1 1 
ATOM   2186 O  OD2 . ASP   A 1 269 ? 33.375 2.115   -3.939  1.00 13.16 -1 710  ASP   A OD2 1 
ATOM   2187 N  N   . PRO   A 1 270 ? 36.574 2.300   -3.160  1.00 11.27 ?  711  PRO   A N   1 
ATOM   2188 C  CA  . PRO   A 1 270 ? 37.504 1.994   -4.259  1.00 11.81 ?  711  PRO   A CA  1 
ATOM   2189 C  C   . PRO   A 1 270 ? 36.869 1.943   -5.643  1.00 11.21 ?  711  PRO   A C   1 
ATOM   2190 O  O   . PRO   A 1 270 ? 37.614 1.905   -6.641  1.00 13.67 ?  711  PRO   A O   1 
ATOM   2191 C  CB  . PRO   A 1 270 ? 38.067 0.620   -3.860  1.00 13.72 ?  711  PRO   A CB  1 
ATOM   2192 C  CG  . PRO   A 1 270 ? 36.982 0.005   -3.049  1.00 12.03 ?  711  PRO   A CG  1 
ATOM   2193 C  CD  . PRO   A 1 270 ? 36.382 1.141   -2.270  1.00 11.01 ?  711  PRO   A CD  1 
ATOM   2194 N  N   . LEU   A 1 271 ? 35.539 1.981   -5.743  1.00 11.20 ?  712  LEU   A N   1 
ATOM   2195 C  CA  . LEU   A 1 271 ? 34.841 1.853   -7.011  1.00 12.00 ?  712  LEU   A CA  1 
ATOM   2196 C  C   . LEU   A 1 271 ? 33.936 3.027   -7.345  1.00 12.98 ?  712  LEU   A C   1 
ATOM   2197 O  O   . LEU   A 1 271 ? 33.799 3.364   -8.525  1.00 14.13 ?  712  LEU   A O   1 
ATOM   2198 C  CB  . LEU   A 1 271 ? 33.997 0.569   -7.018  1.00 14.48 ?  712  LEU   A CB  1 
ATOM   2199 C  CG  . LEU   A 1 271 ? 34.755 -0.751  -6.974  1.00 15.01 ?  712  LEU   A CG  1 
ATOM   2200 C  CD1 . LEU   A 1 271 ? 33.825 -1.903  -6.658  1.00 16.33 ?  712  LEU   A CD1 1 
ATOM   2201 C  CD2 . LEU   A 1 271 ? 35.472 -0.980  -8.296  1.00 15.29 ?  712  LEU   A CD2 1 
ATOM   2202 N  N   . GLY   A 1 272 ? 33.298 3.655   -6.359  1.00 12.00 ?  713  GLY   A N   1 
ATOM   2203 C  CA  . GLY   A 1 272 ? 32.255 4.613   -6.691  1.00 12.07 ?  713  GLY   A CA  1 
ATOM   2204 C  C   . GLY   A 1 272 ? 32.774 5.942   -7.214  1.00 11.86 ?  713  GLY   A C   1 
ATOM   2205 O  O   . GLY   A 1 272 ? 32.130 6.576   -8.054  1.00 12.73 ?  713  GLY   A O   1 
ATOM   2206 N  N   . GLY   A 1 273 ? 33.914 6.399   -6.706  1.00 13.51 ?  714  GLY   A N   1 
ATOM   2207 C  CA  . GLY   A 1 273 ? 34.465 7.666   -7.157  1.00 16.23 ?  714  GLY   A CA  1 
ATOM   2208 C  C   . GLY   A 1 273 ? 33.758 8.899   -6.641  1.00 15.96 ?  714  GLY   A C   1 
ATOM   2209 O  O   . GLY   A 1 273 ? 33.976 9.997   -7.172  1.00 16.88 ?  714  GLY   A O   1 
ATOM   2210 N  N   . PHE   A 1 274 ? 32.903 8.753   -5.634  1.00 13.00 ?  715  PHE   A N   1 
ATOM   2211 C  CA  . PHE   A 1 274 ? 32.118 9.852   -5.085  1.00 13.08 ?  715  PHE   A CA  1 
ATOM   2212 C  C   . PHE   A 1 274 ? 32.618 10.185  -3.679  1.00 13.76 ?  715  PHE   A C   1 
ATOM   2213 O  O   . PHE   A 1 274 ? 33.563 9.575   -3.165  1.00 14.91 ?  715  PHE   A O   1 
ATOM   2214 C  CB  . PHE   A 1 274 ? 30.626 9.505   -5.106  1.00 13.66 ?  715  PHE   A CB  1 
ATOM   2215 C  CG  . PHE   A 1 274 ? 29.951 9.742   -6.439  1.00 12.96 ?  715  PHE   A CG  1 
ATOM   2216 C  CD1 . PHE   A 1 274 ? 30.674 10.054  -7.583  1.00 14.33 ?  715  PHE   A CD1 1 
ATOM   2217 C  CD2 . PHE   A 1 274 ? 28.577 9.680   -6.527  1.00 12.40 ?  715  PHE   A CD2 1 
ATOM   2218 C  CE1 . PHE   A 1 274 ? 30.030 10.271  -8.802  1.00 15.40 ?  715  PHE   A CE1 1 
ATOM   2219 C  CE2 . PHE   A 1 274 ? 27.935 9.894   -7.736  1.00 15.04 ?  715  PHE   A CE2 1 
ATOM   2220 C  CZ  . PHE   A 1 274 ? 28.661 10.185  -8.873  1.00 15.45 ?  715  PHE   A CZ  1 
ATOM   2221 N  N   . GLN   A 1 275 ? 31.980 11.174  -3.050  1.00 11.01 ?  716  GLN   A N   1 
ATOM   2222 C  CA  . GLN   A 1 275 ? 32.486 11.684  -1.780  1.00 13.12 ?  716  GLN   A CA  1 
ATOM   2223 C  C   . GLN   A 1 275 ? 31.358 12.023  -0.817  1.00 12.13 ?  716  GLN   A C   1 
ATOM   2224 O  O   . GLN   A 1 275 ? 31.463 12.963  -0.021  1.00 13.94 ?  716  GLN   A O   1 
ATOM   2225 C  CB  . GLN   A 1 275 ? 33.425 12.874  -1.975  1.00 17.13 ?  716  GLN   A CB  1 
ATOM   2226 C  CG  . GLN   A 1 275 ? 32.851 14.021  -2.772  1.00 23.45 ?  716  GLN   A CG  1 
ATOM   2227 C  CD  . GLN   A 1 275 ? 33.895 15.089  -3.079  1.00 30.18 ?  716  GLN   A CD  1 
ATOM   2228 O  OE1 . GLN   A 1 275 ? 34.850 15.272  -2.318  1.00 34.46 ?  716  GLN   A OE1 1 
ATOM   2229 N  NE2 . GLN   A 1 275 ? 33.725 15.787  -4.203  1.00 29.50 ?  716  GLN   A NE2 1 
ATOM   2230 N  N   . VAL   A 1 276 ? 30.276 11.237  -0.830  1.00 11.50 ?  717  VAL   A N   1 
ATOM   2231 C  CA  . VAL   A 1 276 ? 29.270 11.377  0.222   1.00 11.78 ?  717  VAL   A CA  1 
ATOM   2232 C  C   . VAL   A 1 276 ? 29.890 11.005  1.570   1.00 12.04 ?  717  VAL   A C   1 
ATOM   2233 O  O   . VAL   A 1 276 ? 30.604 10.000  1.685   1.00 11.71 ?  717  VAL   A O   1 
ATOM   2234 C  CB  . VAL   A 1 276 ? 28.024 10.539  -0.111  1.00 11.09 ?  717  VAL   A CB  1 
ATOM   2235 C  CG1 . VAL   A 1 276 ? 26.949 10.740  0.962   1.00 11.55 ?  717  VAL   A CG1 1 
ATOM   2236 C  CG2 . VAL   A 1 276 ? 27.480 10.895  -1.506  1.00 10.79 ?  717  VAL   A CG2 1 
ATOM   2237 N  N   . THR   A 1 277 ? 29.664 11.837  2.587   1.00 9.99  ?  718  THR   A N   1 
ATOM   2238 C  CA  . THR   A 1 277 ? 30.292 11.658  3.892   1.00 11.77 ?  718  THR   A CA  1 
ATOM   2239 C  C   . THR   A 1 277 ? 29.373 10.895  4.838   1.00 10.80 ?  718  THR   A C   1 
ATOM   2240 O  O   . THR   A 1 277 ? 28.169 10.756  4.590   1.00 11.96 ?  718  THR   A O   1 
ATOM   2241 C  CB  . THR   A 1 277 ? 30.632 13.022  4.498   1.00 11.69 ?  718  THR   A CB  1 
ATOM   2242 O  OG1 . THR   A 1 277 ? 29.422 13.692  4.890   1.00 12.84 ?  718  THR   A OG1 1 
ATOM   2243 C  CG2 . THR   A 1 277 ? 31.431 13.886  3.531   1.00 11.54 ?  718  THR   A CG2 1 
ATOM   2244 N  N   . PRO   A 1 278 ? 29.904 10.396  5.961   1.00 11.28 ?  719  PRO   A N   1 
ATOM   2245 C  CA  . PRO   A 1 278 ? 29.011 9.755   6.935   1.00 10.51 ?  719  PRO   A CA  1 
ATOM   2246 C  C   . PRO   A 1 278 ? 27.922 10.694  7.420   1.00 11.50 ?  719  PRO   A C   1 
ATOM   2247 O  O   . PRO   A 1 278 ? 26.770 10.273  7.600   1.00 11.90 ?  719  PRO   A O   1 
ATOM   2248 C  CB  . PRO   A 1 278 ? 29.973 9.294   8.046   1.00 10.59 ?  719  PRO   A CB  1 
ATOM   2249 C  CG  . PRO   A 1 278 ? 31.269 9.064   7.350   1.00 11.60 ?  719  PRO   A CG  1 
ATOM   2250 C  CD  . PRO   A 1 278 ? 31.328 10.147  6.277   1.00 12.06 ?  719  PRO   A CD  1 
ATOM   2251 N  N   . GLU   A 1 279 ? 28.261 11.968  7.622   1.00 11.06 ?  720  GLU   A N   1 
ATOM   2252 C  CA  . GLU   A 1 279 ? 27.257 12.935  8.039   1.00 12.82 ?  720  GLU   A CA  1 
ATOM   2253 C  C   . GLU   A 1 279 ? 26.236 13.192  6.935   1.00 12.76 ?  720  GLU   A C   1 
ATOM   2254 O  O   . GLU   A 1 279 ? 25.063 13.435  7.228   1.00 12.92 ?  720  GLU   A O   1 
ATOM   2255 C  CB  . GLU   A 1 279 ? 27.923 14.216  8.563   1.00 14.51 ?  720  GLU   A CB  1 
ATOM   2256 C  CG  . GLU   A 1 279 ? 28.747 15.020  7.576   1.00 18.18 ?  720  GLU   A CG  1 
ATOM   2257 C  CD  . GLU   A 1 279 ? 30.244 14.658  7.534   1.00 17.60 ?  720  GLU   A CD  1 
ATOM   2258 O  OE1 . GLU   A 1 279 ? 30.639 13.540  7.960   1.00 17.13 ?  720  GLU   A OE1 1 
ATOM   2259 O  OE2 . GLU   A 1 279 ? 31.020 15.505  7.032   1.00 17.18 -1 720  GLU   A OE2 1 
ATOM   2260 N  N   . GLY   A 1 280 ? 26.655 13.119  5.668   1.00 11.77 ?  721  GLY   A N   1 
ATOM   2261 C  CA  . GLY   A 1 280 ? 25.689 13.187  4.575   1.00 10.81 ?  721  GLY   A CA  1 
ATOM   2262 C  C   . GLY   A 1 280 ? 24.661 12.069  4.620   1.00 11.95 ?  721  GLY   A C   1 
ATOM   2263 O  O   . GLY   A 1 280 ? 23.458 12.316  4.531   1.00 11.44 ?  721  GLY   A O   1 
ATOM   2264 N  N   . TYR   A 1 281 ? 25.121 10.823  4.764   1.00 11.08 ?  722  TYR   A N   1 
ATOM   2265 C  CA  . TYR   A 1 281 ? 24.189 9.703   4.885   1.00 10.95 ?  722  TYR   A CA  1 
ATOM   2266 C  C   . TYR   A 1 281 ? 23.276 9.863   6.099   1.00 11.06 ?  722  TYR   A C   1 
ATOM   2267 O  O   . TYR   A 1 281 ? 22.097 9.482   6.052   1.00 12.01 ?  722  TYR   A O   1 
ATOM   2268 C  CB  . TYR   A 1 281 ? 24.965 8.390   4.987   1.00 11.14 ?  722  TYR   A CB  1 
ATOM   2269 C  CG  . TYR   A 1 281 ? 25.616 7.930   3.696   1.00 9.54  ?  722  TYR   A CG  1 
ATOM   2270 C  CD1 . TYR   A 1 281 ? 24.853 7.497   2.612   1.00 9.38  ?  722  TYR   A CD1 1 
ATOM   2271 C  CD2 . TYR   A 1 281 ? 26.998 7.916   3.558   1.00 10.33 ?  722  TYR   A CD2 1 
ATOM   2272 C  CE1 . TYR   A 1 281 ? 25.458 7.070   1.429   1.00 10.78 ?  722  TYR   A CE1 1 
ATOM   2273 C  CE2 . TYR   A 1 281 ? 27.607 7.497   2.382   1.00 10.47 ?  722  TYR   A CE2 1 
ATOM   2274 C  CZ  . TYR   A 1 281 ? 26.829 7.071   1.329   1.00 9.86  ?  722  TYR   A CZ  1 
ATOM   2275 O  OH  . TYR   A 1 281 ? 27.452 6.647   0.199   1.00 10.80 ?  722  TYR   A OH  1 
ATOM   2276 N  N   . ALA   A 1 282 ? 23.802 10.403  7.204   1.00 11.61 ?  723  ALA   A N   1 
ATOM   2277 C  CA  . ALA   A 1 282 ? 22.954 10.650  8.367   1.00 9.60  ?  723  ALA   A CA  1 
ATOM   2278 C  C   . ALA   A 1 282 ? 21.831 11.617  8.011   1.00 11.02 ?  723  ALA   A C   1 
ATOM   2279 O  O   . ALA   A 1 282 ? 20.676 11.409  8.393   1.00 12.18 ?  723  ALA   A O   1 
ATOM   2280 C  CB  . ALA   A 1 282 ? 23.797 11.203  9.516   1.00 11.77 ?  723  ALA   A CB  1 
ATOM   2281 N  N   . HIS   A 1 283 ? 22.155 12.678  7.278   1.00 11.58 ?  724  HIS   A N   1 
ATOM   2282 C  CA  . HIS   A 1 283 ? 21.137 13.647  6.886   1.00 11.98 ?  724  HIS   A CA  1 
ATOM   2283 C  C   . HIS   A 1 283 ? 20.106 13.044  5.944   1.00 13.35 ?  724  HIS   A C   1 
ATOM   2284 O  O   . HIS   A 1 283 ? 18.915 13.348  6.062   1.00 14.62 ?  724  HIS   A O   1 
ATOM   2285 C  CB  . HIS   A 1 283 ? 21.785 14.890  6.287   1.00 13.07 ?  724  HIS   A CB  1 
ATOM   2286 C  CG  . HIS   A 1 283 ? 22.216 15.877  7.326   1.00 12.58 ?  724  HIS   A CG  1 
ATOM   2287 N  ND1 . HIS   A 1 283 ? 21.483 17.003  7.636   1.00 13.91 ?  724  HIS   A ND1 1 
ATOM   2288 C  CD2 . HIS   A 1 283 ? 23.284 15.879  8.157   1.00 14.47 ?  724  HIS   A CD2 1 
ATOM   2289 C  CE1 . HIS   A 1 283 ? 22.093 17.666  8.605   1.00 14.76 ?  724  HIS   A CE1 1 
ATOM   2290 N  NE2 . HIS   A 1 283 ? 23.186 17.003  8.941   1.00 14.54 ?  724  HIS   A NE2 1 
ATOM   2291 N  N   . LEU   A 1 284 ? 20.539 12.179  5.022   1.00 11.98 ?  725  LEU   A N   1 
ATOM   2292 C  CA  . LEU   A 1 284 ? 19.581 11.524  4.136   1.00 12.37 ?  725  LEU   A CA  1 
ATOM   2293 C  C   . LEU   A 1 284 ? 18.655 10.608  4.927   1.00 11.74 ?  725  LEU   A C   1 
ATOM   2294 O  O   . LEU   A 1 284 ? 17.433 10.599  4.717   1.00 12.02 ?  725  LEU   A O   1 
ATOM   2295 C  CB  . LEU   A 1 284 ? 20.317 10.750  3.039   1.00 11.70 ?  725  LEU   A CB  1 
ATOM   2296 C  CG  . LEU   A 1 284 ? 21.312 11.523  2.176   1.00 13.23 ?  725  LEU   A CG  1 
ATOM   2297 C  CD1 . LEU   A 1 284 ? 21.854 10.620  1.067   1.00 13.74 ?  725  LEU   A CD1 1 
ATOM   2298 C  CD2 . LEU   A 1 284 ? 20.661 12.766  1.586   1.00 13.78 ?  725  LEU   A CD2 1 
ATOM   2299 N  N   . THR   A 1 285 ? 19.212 9.872   5.890   1.00 11.19 ?  726  THR   A N   1 
ATOM   2300 C  CA  . THR   A 1 285 ? 18.397 9.011   6.736   1.00 11.70 ?  726  THR   A CA  1 
ATOM   2301 C  C   . THR   A 1 285 ? 17.383 9.832   7.512   1.00 13.03 ?  726  THR   A C   1 
ATOM   2302 O  O   . THR   A 1 285 ? 16.195 9.485   7.564   1.00 13.05 ?  726  THR   A O   1 
ATOM   2303 C  CB  . THR   A 1 285 ? 19.299 8.248   7.714   1.00 10.42 ?  726  THR   A CB  1 
ATOM   2304 O  OG1 . THR   A 1 285 ? 20.254 7.473   6.978   1.00 12.12 ?  726  THR   A OG1 1 
ATOM   2305 C  CG2 . THR   A 1 285 ? 18.475 7.315   8.610   1.00 11.47 ?  726  THR   A CG2 1 
ATOM   2306 N  N   . HIS   A 1 286 ? 17.844 10.924  8.133   1.00 12.67 ?  727  HIS   A N   1 
ATOM   2307 C  CA  . HIS   A 1 286 ? 16.957 11.753  8.937   1.00 13.06 ?  727  HIS   A CA  1 
ATOM   2308 C  C   . HIS   A 1 286 ? 15.788 12.282  8.114   1.00 13.48 ?  727  HIS   A C   1 
ATOM   2309 O  O   . HIS   A 1 286 ? 14.655 12.324  8.598   1.00 14.37 ?  727  HIS   A O   1 
ATOM   2310 C  CB  . HIS   A 1 286 ? 17.756 12.897  9.556   1.00 13.43 ?  727  HIS   A CB  1 
ATOM   2311 C  CG  . HIS   A 1 286 ? 16.987 13.701  10.558  1.00 17.32 ?  727  HIS   A CG  1 
ATOM   2312 N  ND1 . HIS   A 1 286 ? 16.881 13.349  11.886  1.00 20.38 ?  727  HIS   A ND1 1 
ATOM   2313 C  CD2 . HIS   A 1 286 ? 16.300 14.858  10.418  1.00 18.61 ?  727  HIS   A CD2 1 
ATOM   2314 C  CE1 . HIS   A 1 286 ? 16.154 14.252  12.521  1.00 19.88 ?  727  HIS   A CE1 1 
ATOM   2315 N  NE2 . HIS   A 1 286 ? 15.791 15.179  11.654  1.00 22.01 ?  727  HIS   A NE2 1 
ATOM   2316 N  N   . GLN   A 1 287 ? 16.032 12.659  6.860   1.00 14.15 ?  728  GLN   A N   1 
ATOM   2317 C  CA  . GLN   A 1 287 ? 14.939 13.130  6.013   1.00 15.31 ?  728  GLN   A CA  1 
ATOM   2318 C  C   . GLN   A 1 287 ? 13.937 12.021  5.721   1.00 15.15 ?  728  GLN   A C   1 
ATOM   2319 O  O   . GLN   A 1 287 ? 12.719 12.245  5.752   1.00 15.45 ?  728  GLN   A O   1 
ATOM   2320 C  CB  . GLN   A 1 287 ? 15.506 13.706  4.722   1.00 15.79 ?  728  GLN   A CB  1 
ATOM   2321 C  CG  . GLN   A 1 287 ? 16.285 14.994  4.940   1.00 16.01 ?  728  GLN   A CG  1 
ATOM   2322 C  CD  . GLN   A 1 287 ? 16.773 15.617  3.652   1.00 18.78 ?  728  GLN   A CD  1 
ATOM   2323 O  OE1 . GLN   A 1 287 ? 16.042 15.682  2.665   1.00 18.55 ?  728  GLN   A OE1 1 
ATOM   2324 N  NE2 . GLN   A 1 287 ? 18.018 16.083  3.653   1.00 21.59 ?  728  GLN   A NE2 1 
ATOM   2325 N  N   . LEU   A 1 288 ? 14.423 10.821  5.417   1.00 13.67 ?  729  LEU   A N   1 
ATOM   2326 C  CA  . LEU   A 1 288 ? 13.499 9.727   5.134   1.00 12.52 ?  729  LEU   A CA  1 
ATOM   2327 C  C   . LEU   A 1 288 ? 12.661 9.355   6.355   1.00 12.71 ?  729  LEU   A C   1 
ATOM   2328 O  O   . LEU   A 1 288 ? 11.541 8.851   6.212   1.00 14.03 ?  729  LEU   A O   1 
ATOM   2329 C  CB  . LEU   A 1 288 ? 14.275 8.531   4.584   1.00 12.45 ?  729  LEU   A CB  1 
ATOM   2330 C  CG  . LEU   A 1 288 ? 14.983 8.747   3.241   1.00 13.28 ?  729  LEU   A CG  1 
ATOM   2331 C  CD1 . LEU   A 1 288 ? 15.677 7.470   2.807   1.00 15.02 ?  729  LEU   A CD1 1 
ATOM   2332 C  CD2 . LEU   A 1 288 ? 14.008 9.222   2.161   1.00 14.68 ?  729  LEU   A CD2 1 
ATOM   2333 N  N   . MET   A 1 289 ? 13.179 9.592   7.564   1.00 12.06 ?  730  MET   A N   1 
ATOM   2334 C  CA  . MET   A 1 289 ? 12.434 9.276   8.775   1.00 14.15 ?  730  MET   A CA  1 
ATOM   2335 C  C   . MET   A 1 289 ? 11.166 10.105  8.924   1.00 12.53 ?  730  MET   A C   1 
ATOM   2336 O  O   . MET   A 1 289 ? 10.303 9.758   9.737   1.00 15.12 ?  730  MET   A O   1 
ATOM   2337 C  CB  . MET   A 1 289 ? 13.331 9.491   9.993   1.00 14.06 ?  730  MET   A CB  1 
ATOM   2338 C  CG  . MET   A 1 289 ? 14.394 8.434   10.140  1.00 13.18 ?  730  MET   A CG  1 
ATOM   2339 S  SD  . MET   A 1 289 ? 15.562 8.797   11.453  1.00 14.41 ?  730  MET   A SD  1 
ATOM   2340 C  CE  . MET   A 1 289 ? 14.443 8.872   12.855  1.00 15.16 ?  730  MET   A CE  1 
ATOM   2341 N  N   . SER   A 1 290 ? 11.043 11.192  8.177   1.00 12.44 ?  731  SER   A N   1 
ATOM   2342 C  CA  . SER   A 1 290 ? 9.834  11.999  8.189   1.00 15.38 ?  731  SER   A CA  1 
ATOM   2343 C  C   . SER   A 1 290 ? 8.708  11.398  7.355   1.00 18.09 ?  731  SER   A C   1 
ATOM   2344 O  O   . SER   A 1 290 ? 7.603  11.953  7.357   1.00 18.49 ?  731  SER   A O   1 
ATOM   2345 C  CB  . SER   A 1 290 ? 10.152 13.420  7.728   1.00 19.26 ?  731  SER   A CB  1 
ATOM   2346 O  OG  . SER   A 1 290 ? 10.362 13.468  6.326   1.00 21.54 ?  731  SER   A OG  1 
ATOM   2347 N  N   . LEU   A 1 291 ? 8.946  10.282  6.661   1.00 15.76 ?  732  LEU   A N   1 
ATOM   2348 C  CA  . LEU   A 1 291 ? 7.932  9.607   5.858   1.00 14.05 ?  732  LEU   A CA  1 
ATOM   2349 C  C   . LEU   A 1 291 ? 7.408  8.363   6.569   1.00 15.03 ?  732  LEU   A C   1 
ATOM   2350 O  O   . LEU   A 1 291 ? 8.076  7.783   7.431   1.00 16.16 ?  732  LEU   A O   1 
ATOM   2351 C  CB  . LEU   A 1 291 ? 8.513  9.179   4.505   1.00 15.52 ?  732  LEU   A CB  1 
ATOM   2352 C  CG  . LEU   A 1 291 ? 9.230  10.247  3.685   1.00 14.20 ?  732  LEU   A CG  1 
ATOM   2353 C  CD1 . LEU   A 1 291 ? 10.161 9.623   2.642   1.00 15.17 ?  732  LEU   A CD1 1 
ATOM   2354 C  CD2 . LEU   A 1 291 ? 8.195  11.156  3.018   1.00 14.82 ?  732  LEU   A CD2 1 
ATOM   2355 N  N   . ALA   A 1 292 ? 6.204  7.936   6.164   1.00 14.96 ?  733  ALA   A N   1 
ATOM   2356 C  CA  . ALA   A 1 292 ? 5.629  6.660   6.590   1.00 16.01 ?  733  ALA   A CA  1 
ATOM   2357 C  C   . ALA   A 1 292 ? 5.576  6.524   8.112   1.00 13.51 ?  733  ALA   A C   1 
ATOM   2358 O  O   . ALA   A 1 292 ? 5.725  5.432   8.664   1.00 14.73 ?  733  ALA   A O   1 
ATOM   2359 C  CB  . ALA   A 1 292 ? 6.360  5.481   5.938   1.00 14.33 ?  733  ALA   A CB  1 
ATOM   2360 N  N   . ALA   A 1 293 ? 5.334  7.645   8.804   1.00 14.63 ?  734  ALA   A N   1 
ATOM   2361 C  CA  . ALA   A 1 293 ? 5.313  7.671   10.267  1.00 18.52 ?  734  ALA   A CA  1 
ATOM   2362 C  C   . ALA   A 1 293 ? 6.578  7.047   10.850  1.00 17.32 ?  734  ALA   A C   1 
ATOM   2363 O  O   . ALA   A 1 293 ? 6.551  6.372   11.879  1.00 18.61 ?  734  ALA   A O   1 
ATOM   2364 C  CB  . ALA   A 1 293 ? 4.045  7.028   10.839  1.00 18.65 ?  734  ALA   A CB  1 
ATOM   2365 N  N   . GLY   A 1 294 ? 7.699  7.244   10.154  1.00 16.86 ?  735  GLY   A N   1 
ATOM   2366 C  CA  . GLY   A 1 294 ? 8.975  6.749   10.635  1.00 17.68 ?  735  GLY   A CA  1 
ATOM   2367 C  C   . GLY   A 1 294 ? 9.290  5.306   10.298  1.00 15.50 ?  735  GLY   A C   1 
ATOM   2368 O  O   . GLY   A 1 294 ? 10.336 4.802   10.720  1.00 14.99 ?  735  GLY   A O   1 
ATOM   2369 N  N   . ARG   A 1 295 ? 8.441  4.626   9.537   1.00 13.57 ?  736  ARG   A N   1 
ATOM   2370 C  CA  . ARG   A 1 295 ? 8.624  3.200   9.269   1.00 14.27 ?  736  ARG   A CA  1 
ATOM   2371 C  C   . ARG   A 1 295 ? 9.655  3.018   8.158   1.00 13.05 ?  736  ARG   A C   1 
ATOM   2372 O  O   . ARG   A 1 295 ? 9.320  2.944   6.967   1.00 13.18 ?  736  ARG   A O   1 
ATOM   2373 C  CB  . ARG   A 1 295 ? 7.288  2.555   8.928   1.00 16.64 ?  736  ARG   A CB  1 
ATOM   2374 C  CG  . ARG   A 1 295 ? 6.338  2.538   10.129  1.00 19.68 ?  736  ARG   A CG  1 
ATOM   2375 C  CD  . ARG   A 1 295 ? 5.045  1.810   9.826   1.00 26.18 ?  736  ARG   A CD  1 
ATOM   2376 N  NE  . ARG   A 1 295 ? 4.293  2.470   8.764   1.00 32.90 ?  736  ARG   A NE  1 
ATOM   2377 C  CZ  . ARG   A 1 295 ? 3.313  3.346   8.972   1.00 36.99 ?  736  ARG   A CZ  1 
ATOM   2378 N  NH1 . ARG   A 1 295 ? 2.959  3.675   10.211  1.00 37.63 ?  736  ARG   A NH1 1 
ATOM   2379 N  NH2 . ARG   A 1 295 ? 2.690  3.895   7.938   1.00 37.77 ?  736  ARG   A NH2 1 
ATOM   2380 N  N   . VAL   A 1 296 ? 10.928 2.933   8.562   1.00 12.50 ?  737  VAL   A N   1 
ATOM   2381 C  CA  . VAL   A 1 296 ? 12.070 2.920   7.648   1.00 11.62 ?  737  VAL   A CA  1 
ATOM   2382 C  C   . VAL   A 1 296 ? 12.915 1.699   7.954   1.00 11.58 ?  737  VAL   A C   1 
ATOM   2383 O  O   . VAL   A 1 296 ? 13.289 1.470   9.110   1.00 12.26 ?  737  VAL   A O   1 
ATOM   2384 C  CB  . VAL   A 1 296 ? 12.941 4.185   7.792   1.00 13.32 ?  737  VAL   A CB  1 
ATOM   2385 C  CG1 . VAL   A 1 296 ? 14.209 4.100   6.890   1.00 13.06 ?  737  VAL   A CG1 1 
ATOM   2386 C  CG2 . VAL   A 1 296 ? 12.135 5.432   7.486   1.00 14.14 ?  737  VAL   A CG2 1 
ATOM   2387 N  N   . LEU   A 1 297 ? 13.241 0.938   6.914   1.00 11.19 ?  738  LEU   A N   1 
ATOM   2388 C  CA  . LEU   A 1 297 ? 14.163 -0.186  7.002   1.00 11.53 ?  738  LEU   A CA  1 
ATOM   2389 C  C   . LEU   A 1 297 ? 15.358 0.109   6.101   1.00 10.63 ?  738  LEU   A C   1 
ATOM   2390 O  O   . LEU   A 1 297 ? 15.197 0.296   4.889   1.00 11.45 ?  738  LEU   A O   1 
ATOM   2391 C  CB  . LEU   A 1 297 ? 13.469 -1.482  6.577   1.00 11.83 ?  738  LEU   A CB  1 
ATOM   2392 C  CG  . LEU   A 1 297 ? 14.362 -2.719  6.447   1.00 13.47 ?  738  LEU   A CG  1 
ATOM   2393 C  CD1 . LEU   A 1 297 ? 15.170 -2.995  7.708   1.00 14.84 ?  738  LEU   A CD1 1 
ATOM   2394 C  CD2 . LEU   A 1 297 ? 13.567 -3.963  6.015   1.00 13.96 ?  738  LEU   A CD2 1 
ATOM   2395 N  N   . ILE   A 1 298 ? 16.548 0.145   6.681   1.00 10.57 ?  739  ILE   A N   1 
ATOM   2396 C  CA  . ILE   A 1 298 ? 17.777 0.423   5.941   1.00 10.53 ?  739  ILE   A CA  1 
ATOM   2397 C  C   . ILE   A 1 298 ? 18.464 -0.906  5.648   1.00 11.19 ?  739  ILE   A C   1 
ATOM   2398 O  O   . ILE   A 1 298 ? 18.866 -1.621  6.572   1.00 12.94 ?  739  ILE   A O   1 
ATOM   2399 C  CB  . ILE   A 1 298 ? 18.699 1.347   6.753   1.00 11.20 ?  739  ILE   A CB  1 
ATOM   2400 C  CG1 . ILE   A 1 298 ? 17.991 2.676   7.065   1.00 14.83 ?  739  ILE   A CG1 1 
ATOM   2401 C  CG2 . ILE   A 1 298 ? 20.051 1.543   6.048   1.00 12.17 ?  739  ILE   A CG2 1 
ATOM   2402 C  CD1 . ILE   A 1 298 ? 18.825 3.659   7.845   1.00 17.91 ?  739  ILE   A CD1 1 
ATOM   2403 N  N   . ILE   A 1 299 ? 18.601 -1.249  4.367   1.00 10.81 ?  740  ILE   A N   1 
ATOM   2404 C  CA  . ILE   A 1 299 ? 19.133 -2.544  3.932   1.00 9.91  ?  740  ILE   A CA  1 
ATOM   2405 C  C   . ILE   A 1 299 ? 20.493 -2.334  3.276   1.00 10.13 ?  740  ILE   A C   1 
ATOM   2406 O  O   . ILE   A 1 299 ? 20.590 -1.633  2.262   1.00 10.70 ?  740  ILE   A O   1 
ATOM   2407 C  CB  . ILE   A 1 299 ? 18.196 -3.236  2.931   1.00 10.63 ?  740  ILE   A CB  1 
ATOM   2408 C  CG1 . ILE   A 1 299 ? 16.813 -3.449  3.553   1.00 11.27 ?  740  ILE   A CG1 1 
ATOM   2409 C  CG2 . ILE   A 1 299 ? 18.805 -4.555  2.464   1.00 12.05 ?  740  ILE   A CG2 1 
ATOM   2410 C  CD1 . ILE   A 1 299 ? 15.764 -3.928  2.555   1.00 11.66 ?  740  ILE   A CD1 1 
ATOM   2411 N  N   . LEU   A 1 300 ? 21.531 -2.980  3.810   1.00 9.18  ?  741  LEU   A N   1 
ATOM   2412 C  CA  . LEU   A 1 300 ? 22.857 -2.866  3.196   1.00 9.61  ?  741  LEU   A CA  1 
ATOM   2413 C  C   . LEU   A 1 300 ? 22.842 -3.423  1.773   1.00 10.47 ?  741  LEU   A C   1 
ATOM   2414 O  O   . LEU   A 1 300 ? 22.356 -4.536  1.544   1.00 11.31 ?  741  LEU   A O   1 
ATOM   2415 C  CB  . LEU   A 1 300 ? 23.900 -3.632  4.020   1.00 11.39 ?  741  LEU   A CB  1 
ATOM   2416 C  CG  . LEU   A 1 300 ? 25.337 -3.524  3.484   1.00 10.41 ?  741  LEU   A CG  1 
ATOM   2417 C  CD1 . LEU   A 1 300 ? 25.799 -2.074  3.482   1.00 11.20 ?  741  LEU   A CD1 1 
ATOM   2418 C  CD2 . LEU   A 1 300 ? 26.303 -4.416  4.253   1.00 10.55 ?  741  LEU   A CD2 1 
ATOM   2419 N  N   . GLU   A 1 301 ? 23.378 -2.636  0.815   1.00 10.17 ?  742  GLU   A N   1 
ATOM   2420 C  CA  . GLU   A 1 301 ? 23.640 -3.107  -0.546  1.00 11.61 ?  742  GLU   A CA  1 
ATOM   2421 C  C   . GLU   A 1 301 ? 25.151 -3.182  -0.752  1.00 11.06 ?  742  GLU   A C   1 
ATOM   2422 O  O   . GLU   A 1 301 ? 25.803 -4.002  -0.102  1.00 11.73 ?  742  GLU   A O   1 
ATOM   2423 C  CB  . GLU   A 1 301 ? 22.937 -2.245  -1.602  1.00 10.58 ?  742  GLU   A CB  1 
ATOM   2424 C  CG  . GLU   A 1 301 ? 21.391 -2.246  -1.504  1.00 10.96 ?  742  GLU   A CG  1 
ATOM   2425 C  CD  . GLU   A 1 301 ? 20.707 -3.435  -2.155  1.00 12.11 ?  742  GLU   A CD  1 
ATOM   2426 O  OE1 . GLU   A 1 301 ? 21.373 -4.388  -2.602  1.00 13.66 ?  742  GLU   A OE1 1 
ATOM   2427 O  OE2 . GLU   A 1 301 ? 19.467 -3.430  -2.190  1.00 12.08 -1 742  GLU   A OE2 1 
ATOM   2428 N  N   . GLY   A 1 302 ? 25.726 -2.357  -1.633  1.00 11.10 ?  743  GLY   A N   1 
ATOM   2429 C  CA  . GLY   A 1 302 ? 27.168 -2.328  -1.832  1.00 10.89 ?  743  GLY   A CA  1 
ATOM   2430 C  C   . GLY   A 1 302 ? 27.900 -1.379  -0.897  1.00 11.22 ?  743  GLY   A C   1 
ATOM   2431 O  O   . GLY   A 1 302 ? 27.383 -0.957  0.141   1.00 10.81 ?  743  GLY   A O   1 
ATOM   2432 N  N   . GLY   A 1 303 ? 29.132 -1.044  -1.273  1.00 13.21 ?  744  GLY   A N   1 
ATOM   2433 C  CA  . GLY   A 1 303 ? 30.013 -0.288  -0.401  1.00 10.86 ?  744  GLY   A CA  1 
ATOM   2434 C  C   . GLY   A 1 303 ? 31.211 -1.126  -0.000  1.00 10.73 ?  744  GLY   A C   1 
ATOM   2435 O  O   . GLY   A 1 303 ? 31.054 -2.152  0.671   1.00 10.87 ?  744  GLY   A O   1 
ATOM   2436 N  N   . TYR   A 1 304 ? 32.419 -0.680  -0.358  1.00 10.12 ?  745  TYR   A N   1 
ATOM   2437 C  CA  . TYR   A 1 304 ? 33.590 -1.551  -0.344  1.00 10.78 ?  745  TYR   A CA  1 
ATOM   2438 C  C   . TYR   A 1 304 ? 34.795 -1.045  0.437   1.00 12.36 ?  745  TYR   A C   1 
ATOM   2439 O  O   . TYR   A 1 304 ? 35.789 -1.778  0.523   1.00 14.14 ?  745  TYR   A O   1 
ATOM   2440 C  CB  . TYR   A 1 304 ? 33.992 -1.934  -1.781  1.00 12.83 ?  745  TYR   A CB  1 
ATOM   2441 C  CG  . TYR   A 1 304 ? 32.768 -2.481  -2.441  1.00 12.04 ?  745  TYR   A CG  1 
ATOM   2442 C  CD1 . TYR   A 1 304 ? 32.322 -3.755  -2.119  1.00 12.43 ?  745  TYR   A CD1 1 
ATOM   2443 C  CD2 . TYR   A 1 304 ? 31.991 -1.691  -3.285  1.00 13.24 ?  745  TYR   A CD2 1 
ATOM   2444 C  CE1 . TYR   A 1 304 ? 31.166 -4.260  -2.646  1.00 12.46 ?  745  TYR   A CE1 1 
ATOM   2445 C  CE2 . TYR   A 1 304 ? 30.833 -2.184  -3.824  1.00 13.55 ?  745  TYR   A CE2 1 
ATOM   2446 C  CZ  . TYR   A 1 304 ? 30.425 -3.463  -3.497  1.00 12.86 ?  745  TYR   A CZ  1 
ATOM   2447 O  OH  . TYR   A 1 304 ? 29.268 -3.957  -4.029  1.00 14.53 ?  745  TYR   A OH  1 
ATOM   2448 N  N   . ASN   A 1 305 ? 34.770 0.176   0.968   1.00 9.65  ?  746  ASN   A N   1 
ATOM   2449 C  CA  . ASN   A 1 305 ? 35.812 0.619   1.896   1.00 8.78  ?  746  ASN   A CA  1 
ATOM   2450 C  C   . ASN   A 1 305 ? 35.276 0.291   3.284   1.00 9.29  ?  746  ASN   A C   1 
ATOM   2451 O  O   . ASN   A 1 305 ? 34.259 0.861   3.703   1.00 11.37 ?  746  ASN   A O   1 
ATOM   2452 C  CB  . ASN   A 1 305 ? 36.088 2.113   1.729   1.00 8.83  ?  746  ASN   A CB  1 
ATOM   2453 C  CG  . ASN   A 1 305 ? 37.132 2.627   2.701   1.00 11.42 ?  746  ASN   A CG  1 
ATOM   2454 O  OD1 . ASN   A 1 305 ? 37.040 2.405   3.909   1.00 10.95 ?  746  ASN   A OD1 1 
ATOM   2455 N  ND2 . ASN   A 1 305 ? 38.133 3.321   2.181   1.00 13.73 ?  746  ASN   A ND2 1 
ATOM   2456 N  N   . LEU   A 1 306 ? 35.909 -0.671  3.956   1.00 10.11 ?  747  LEU   A N   1 
ATOM   2457 C  CA  . LEU   A 1 306 ? 35.378 -1.180  5.218   1.00 10.37 ?  747  LEU   A CA  1 
ATOM   2458 C  C   . LEU   A 1 306 ? 35.197 -0.066  6.237   1.00 10.47 ?  747  LEU   A C   1 
ATOM   2459 O  O   . LEU   A 1 306 ? 34.193 -0.034  6.954   1.00 11.52 ?  747  LEU   A O   1 
ATOM   2460 C  CB  . LEU   A 1 306 ? 36.290 -2.278  5.771   1.00 11.06 ?  747  LEU   A CB  1 
ATOM   2461 C  CG  . LEU   A 1 306 ? 36.451 -3.500  4.864   1.00 10.73 ?  747  LEU   A CG  1 
ATOM   2462 C  CD1 . LEU   A 1 306 ? 37.490 -4.442  5.419   1.00 12.48 ?  747  LEU   A CD1 1 
ATOM   2463 C  CD2 . LEU   A 1 306 ? 35.132 -4.222  4.696   1.00 13.52 ?  747  LEU   A CD2 1 
ATOM   2464 N  N   . THR   A 1 307 ? 36.166 0.849   6.340   1.00 9.31  ?  748  THR   A N   1 
ATOM   2465 C  CA  . THR   A 1 307 ? 36.013 1.968   7.270   1.00 10.60 ?  748  THR   A CA  1 
ATOM   2466 C  C   . THR   A 1 307 ? 34.865 2.874   6.857   1.00 9.82  ?  748  THR   A C   1 
ATOM   2467 O  O   . THR   A 1 307 ? 34.032 3.253   7.691   1.00 12.77 ?  748  THR   A O   1 
ATOM   2468 C  CB  . THR   A 1 307 ? 37.317 2.752   7.374   1.00 13.01 ?  748  THR   A CB  1 
ATOM   2469 O  OG1 . THR   A 1 307 ? 38.288 1.919   8.007   1.00 11.93 ?  748  THR   A OG1 1 
ATOM   2470 C  CG2 . THR   A 1 307 ? 37.142 4.053   8.176   1.00 14.12 ?  748  THR   A CG2 1 
ATOM   2471 N  N   . SER   A 1 308 ? 34.796 3.220   5.569   1.00 11.15 ?  749  SER   A N   1 
ATOM   2472 C  CA  . SER   A 1 308 ? 33.747 4.115   5.094   1.00 12.70 ?  749  SER   A CA  1 
ATOM   2473 C  C   . SER   A 1 308 ? 32.360 3.544   5.355   1.00 10.58 ?  749  SER   A C   1 
ATOM   2474 O  O   . SER   A 1 308 ? 31.461 4.264   5.802   1.00 11.39 ?  749  SER   A O   1 
ATOM   2475 C  CB  . SER   A 1 308 ? 33.923 4.366   3.602   1.00 11.87 ?  749  SER   A CB  1 
ATOM   2476 O  OG  . SER   A 1 308 ? 35.177 4.977   3.328   1.00 13.63 ?  749  SER   A OG  1 
ATOM   2477 N  N   . ILE   A 1 309 ? 32.146 2.269   5.018   1.00 10.33 ?  750  ILE   A N   1 
ATOM   2478 C  CA  . ILE   A 1 309 ? 30.810 1.706   5.173   1.00 10.41 ?  750  ILE   A CA  1 
ATOM   2479 C  C   . ILE   A 1 309 ? 30.453 1.555   6.641   1.00 9.82  ?  750  ILE   A C   1 
ATOM   2480 O  O   . ILE   A 1 309 ? 29.287 1.707   7.021   1.00 10.09 ?  750  ILE   A O   1 
ATOM   2481 C  CB  . ILE   A 1 309 ? 30.623 0.394   4.386   1.00 9.55  ?  750  ILE   A CB  1 
ATOM   2482 C  CG1 . ILE   A 1 309 ? 31.430 -0.758  4.980   1.00 9.35  ?  750  ILE   A CG1 1 
ATOM   2483 C  CG2 . ILE   A 1 309 ? 31.009 0.600   2.936   1.00 9.91  ?  750  ILE   A CG2 1 
ATOM   2484 C  CD1 . ILE   A 1 309 ? 31.191 -2.070  4.238   1.00 11.29 ?  750  ILE   A CD1 1 
ATOM   2485 N  N   . SER   A 1 310 ? 31.433 1.231   7.482   1.00 9.77  ?  751  SER   A N   1 
ATOM   2486 C  CA  . SER   A 1 310 ? 31.155 1.064   8.904   1.00 10.67 ?  751  SER   A CA  1 
ATOM   2487 C  C   . SER   A 1 310 ? 30.753 2.380   9.538   1.00 10.02 ?  751  SER   A C   1 
ATOM   2488 O  O   . SER   A 1 310 ? 29.760 2.438   10.266  1.00 11.21 ?  751  SER   A O   1 
ATOM   2489 C  CB  . SER   A 1 310 ? 32.344 0.416   9.621   1.00 11.06 ?  751  SER   A CB  1 
ATOM   2490 O  OG  . SER   A 1 310 ? 32.641 -0.837  9.051   1.00 11.81 ?  751  SER   A OG  1 
ATOM   2491 N  N   . GLU   A 1 311 ? 31.493 3.454   9.253   1.00 10.57 ?  752  GLU   A N   1 
ATOM   2492 C  CA  . GLU   A 1 311 ? 31.123 4.758   9.791   1.00 10.29 ?  752  GLU   A CA  1 
ATOM   2493 C  C   . GLU   A 1 311 ? 29.795 5.231   9.218   1.00 10.83 ?  752  GLU   A C   1 
ATOM   2494 O  O   . GLU   A 1 311 ? 28.943 5.749   9.949   1.00 11.57 ?  752  GLU   A O   1 
ATOM   2495 C  CB  . GLU   A 1 311 ? 32.213 5.783   9.508   1.00 13.36 ?  752  GLU   A CB  1 
ATOM   2496 C  CG  . GLU   A 1 311 ? 31.995 7.114   10.217  1.00 16.29 ?  752  GLU   A CG  1 
ATOM   2497 C  CD  . GLU   A 1 311 ? 32.084 7.000   11.734  1.00 19.99 ?  752  GLU   A CD  1 
ATOM   2498 O  OE1 . GLU   A 1 311 ? 32.743 6.058   12.224  1.00 18.20 ?  752  GLU   A OE1 1 
ATOM   2499 O  OE2 . GLU   A 1 311 ? 31.501 7.858   12.437  1.00 22.91 -1 752  GLU   A OE2 1 
ATOM   2500 N  N   . SER   A 1 312 ? 29.597 5.039   7.914   1.00 11.00 ?  753  SER   A N   1 
ATOM   2501 C  CA  . SER   A 1 312 ? 28.417 5.576   7.248   1.00 10.98 ?  753  SER   A CA  1 
ATOM   2502 C  C   . SER   A 1 312 ? 27.153 4.878   7.739   1.00 8.32  ?  753  SER   A C   1 
ATOM   2503 O  O   . SER   A 1 312 ? 26.156 5.533   8.079   1.00 9.84  ?  753  SER   A O   1 
ATOM   2504 C  CB  . SER   A 1 312 ? 28.572 5.397   5.735   1.00 11.26 ?  753  SER   A CB  1 
ATOM   2505 O  OG  . SER   A 1 312 ? 29.581 6.256   5.246   1.00 11.20 ?  753  SER   A OG  1 
ATOM   2506 N  N   . MET   A 1 313 ? 27.165 3.543   7.769   1.00 8.73  ?  754  MET   A N   1 
ATOM   2507 C  CA  . MET   A 1 313 ? 25.956 2.845   8.178   1.00 10.69 ?  754  MET   A CA  1 
ATOM   2508 C  C   . MET   A 1 313 ? 25.674 3.054   9.660   1.00 9.57  ?  754  MET   A C   1 
ATOM   2509 O  O   . MET   A 1 313 ? 24.506 3.134   10.061  1.00 10.20 ?  754  MET   A O   1 
ATOM   2510 C  CB  . MET   A 1 313 ? 26.015 1.355   7.856   1.00 11.65 ?  754  MET   A CB  1 
ATOM   2511 C  CG  . MET   A 1 313 ? 24.621 0.720   7.897   1.00 12.00 ?  754  MET   A CG  1 
ATOM   2512 S  SD  . MET   A 1 313 ? 24.543 -0.971  7.295   1.00 12.78 ?  754  MET   A SD  1 
ATOM   2513 C  CE  . MET   A 1 313 ? 22.904 -1.047  6.587   1.00 13.12 ?  754  MET   A CE  1 
ATOM   2514 N  N   A SER   A 1 314 ? 26.725 3.154   10.492  0.73 9.86  ?  755  SER   A N   1 
ATOM   2515 N  N   B SER   A 1 314 ? 26.721 3.131   10.490  0.27 9.96  ?  755  SER   A N   1 
ATOM   2516 C  CA  A SER   A 1 314 ? 26.522 3.455   11.909  0.73 10.62 ?  755  SER   A CA  1 
ATOM   2517 C  CA  B SER   A 1 314 ? 26.502 3.363   11.914  0.27 10.55 ?  755  SER   A CA  1 
ATOM   2518 C  C   A SER   A 1 314 ? 25.848 4.808   12.094  0.73 10.17 ?  755  SER   A C   1 
ATOM   2519 C  C   B SER   A 1 314 ? 25.917 4.745   12.174  0.27 11.14 ?  755  SER   A C   1 
ATOM   2520 O  O   A SER   A 1 314 ? 24.944 4.947   12.927  0.73 10.84 ?  755  SER   A O   1 
ATOM   2521 O  O   B SER   A 1 314 ? 25.162 4.923   13.136  0.27 11.32 ?  755  SER   A O   1 
ATOM   2522 C  CB  A SER   A 1 314 ? 27.852 3.409   12.670  0.73 11.65 ?  755  SER   A CB  1 
ATOM   2523 C  CB  B SER   A 1 314 ? 27.796 3.153   12.707  0.27 10.34 ?  755  SER   A CB  1 
ATOM   2524 O  OG  A SER   A 1 314 ? 28.388 2.100   12.699  0.73 11.63 ?  755  SER   A OG  1 
ATOM   2525 O  OG  B SER   A 1 314 ? 28.761 4.140   12.392  0.27 9.67  ?  755  SER   A OG  1 
ATOM   2526 N  N   A MET   A 1 315 ? 26.270 5.816   11.329  0.73 11.66 ?  756  MET   A N   1 
ATOM   2527 N  N   B MET   A 1 315 ? 26.241 5.728   11.331  0.27 11.85 ?  756  MET   A N   1 
ATOM   2528 C  CA  A MET   A 1 315 ? 25.632 7.122   11.426  0.73 12.79 ?  756  MET   A CA  1 
ATOM   2529 C  CA  B MET   A 1 315 ? 25.628 7.042   11.481  0.27 12.70 ?  756  MET   A CA  1 
ATOM   2530 C  C   A MET   A 1 315 ? 24.163 7.061   11.038  0.73 11.21 ?  756  MET   A C   1 
ATOM   2531 C  C   B MET   A 1 315 ? 24.165 7.031   11.062  0.27 11.08 ?  756  MET   A C   1 
ATOM   2532 O  O   A MET   A 1 315 ? 23.341 7.781   11.623  0.73 12.76 ?  756  MET   A O   1 
ATOM   2533 O  O   B MET   A 1 315 ? 23.356 7.776   11.629  0.27 11.59 ?  756  MET   A O   1 
ATOM   2534 C  CB  A MET   A 1 315 ? 26.389 8.162   10.594  0.73 15.32 ?  756  MET   A CB  1 
ATOM   2535 C  CB  B MET   A 1 315 ? 26.419 8.105   10.716  0.27 15.57 ?  756  MET   A CB  1 
ATOM   2536 C  CG  A MET   A 1 315 ? 26.749 9.439   11.375  0.73 20.93 ?  756  MET   A CG  1 
ATOM   2537 C  CG  B MET   A 1 315 ? 27.099 9.111   11.636  0.27 18.65 ?  756  MET   A CG  1 
ATOM   2538 S  SD  A MET   A 1 315 ? 27.610 9.170   12.940  0.73 19.11 ?  756  MET   A SD  1 
ATOM   2539 S  SD  B MET   A 1 315 ? 27.915 10.468  10.783  0.27 20.66 ?  756  MET   A SD  1 
ATOM   2540 C  CE  A MET   A 1 315 ? 29.197 9.933   12.592  0.73 23.52 ?  756  MET   A CE  1 
ATOM   2541 C  CE  B MET   A 1 315 ? 28.829 11.218  12.128  0.27 20.99 ?  756  MET   A CE  1 
ATOM   2542 N  N   . CYS   A 1 316 ? 23.805 6.194   10.084  1.00 9.90  ?  757  CYS   A N   1 
ATOM   2543 C  CA  . CYS   A 1 316 ? 22.395 6.032   9.741   1.00 10.85 ?  757  CYS   A CA  1 
ATOM   2544 C  C   . CYS   A 1 316 ? 21.625 5.455   10.917  1.00 10.97 ?  757  CYS   A C   1 
ATOM   2545 O  O   . CYS   A 1 316 ? 20.531 5.934   11.250  1.00 11.72 ?  757  CYS   A O   1 
ATOM   2546 C  CB  . CYS   A 1 316 ? 22.255 5.114   8.529   1.00 9.39  ?  757  CYS   A CB  1 
ATOM   2547 S  SG  . CYS   A 1 316 ? 22.903 5.823   6.982   1.00 14.72 ?  757  CYS   A SG  1 
ATOM   2548 N  N   . THR   A 1 317 ? 22.181 4.432   11.565  1.00 10.35 ?  758  THR   A N   1 
ATOM   2549 C  CA  . THR   A 1 317 ? 21.498 3.843   12.715  1.00 10.32 ?  758  THR   A CA  1 
ATOM   2550 C  C   . THR   A 1 317 ? 21.369 4.847   13.849  1.00 12.15 ?  758  THR   A C   1 
ATOM   2551 O  O   . THR   A 1 317 ? 20.333 4.896   14.517  1.00 11.98 ?  758  THR   A O   1 
ATOM   2552 C  CB  . THR   A 1 317 ? 22.239 2.585   13.181  1.00 10.70 ?  758  THR   A CB  1 
ATOM   2553 O  OG1 . THR   A 1 317 ? 22.365 1.656   12.088  1.00 10.64 ?  758  THR   A OG1 1 
ATOM   2554 C  CG2 . THR   A 1 317 ? 21.510 1.906   14.349  1.00 11.47 ?  758  THR   A CG2 1 
ATOM   2555 N  N   . SER   A 1 318 ? 22.402 5.669   14.064  1.00 10.85 ?  759  SER   A N   1 
ATOM   2556 C  CA  . SER   A 1 318 ? 22.312 6.730   15.065  1.00 11.95 ?  759  SER   A CA  1 
ATOM   2557 C  C   . SER   A 1 318 ? 21.102 7.612   14.809  1.00 12.38 ?  759  SER   A C   1 
ATOM   2558 O  O   . SER   A 1 318 ? 20.403 8.011   15.747  1.00 12.65 ?  759  SER   A O   1 
ATOM   2559 C  CB  . SER   A 1 318 ? 23.603 7.554   15.042  1.00 13.51 ?  759  SER   A CB  1 
ATOM   2560 O  OG  . SER   A 1 318 ? 23.544 8.650   15.935  1.00 16.46 ?  759  SER   A OG  1 
ATOM   2561 N  N   . MET   A 1 319 ? 20.831 7.918   13.536  1.00 11.26 ?  760  MET   A N   1 
ATOM   2562 C  CA  . MET   A 1 319 ? 19.657 8.725   13.202  1.00 11.79 ?  760  MET   A CA  1 
ATOM   2563 C  C   . MET   A 1 319 ? 18.359 7.980   13.493  1.00 12.93 ?  760  MET   A C   1 
ATOM   2564 O  O   . MET   A 1 319 ? 17.412 8.557   14.047  1.00 12.34 ?  760  MET   A O   1 
ATOM   2565 C  CB  . MET   A 1 319 ? 19.693 9.137   11.733  1.00 10.73 ?  760  MET   A CB  1 
ATOM   2566 C  CG  . MET   A 1 319 ? 20.873 10.015  11.365  1.00 10.53 ?  760  MET   A CG  1 
ATOM   2567 S  SD  . MET   A 1 319 ? 20.997 11.569  12.279  1.00 12.77 ?  760  MET   A SD  1 
ATOM   2568 C  CE  . MET   A 1 319 ? 22.162 11.134  13.576  1.00 13.87 ?  760  MET   A CE  1 
ATOM   2569 N  N   . LEU   A 1 320 ? 18.279 6.706   13.091  1.00 11.63 ?  761  LEU   A N   1 
ATOM   2570 C  CA  . LEU   A 1 320 ? 17.104 5.898   13.407  1.00 13.14 ?  761  LEU   A CA  1 
ATOM   2571 C  C   . LEU   A 1 320 ? 16.836 5.857   14.905  1.00 14.23 ?  761  LEU   A C   1 
ATOM   2572 O  O   . LEU   A 1 320 ? 15.671 5.797   15.317  1.00 13.16 ?  761  LEU   A O   1 
ATOM   2573 C  CB  . LEU   A 1 320 ? 17.280 4.466   12.897  1.00 12.25 ?  761  LEU   A CB  1 
ATOM   2574 C  CG  . LEU   A 1 320 ? 17.426 4.249   11.392  1.00 14.32 ?  761  LEU   A CG  1 
ATOM   2575 C  CD1 . LEU   A 1 320 ? 17.431 2.768   11.137  1.00 15.63 ?  761  LEU   A CD1 1 
ATOM   2576 C  CD2 . LEU   A 1 320 ? 16.289 4.909   10.630  1.00 12.49 ?  761  LEU   A CD2 1 
ATOM   2577 N  N   . LEU   A 1 321 ? 17.893 5.862   15.724  1.00 11.62 ?  762  LEU   A N   1 
ATOM   2578 C  CA  . LEU   A 1 321 ? 17.758 5.833   17.173  1.00 11.96 ?  762  LEU   A CA  1 
ATOM   2579 C  C   . LEU   A 1 321 ? 17.320 7.166   17.756  1.00 12.75 ?  762  LEU   A C   1 
ATOM   2580 O  O   . LEU   A 1 321 ? 17.067 7.230   18.966  1.00 14.68 ?  762  LEU   A O   1 
ATOM   2581 C  CB  . LEU   A 1 321 ? 19.083 5.412   17.802  1.00 12.63 ?  762  LEU   A CB  1 
ATOM   2582 C  CG  . LEU   A 1 321 ? 19.386 3.917   17.684  1.00 13.01 ?  762  LEU   A CG  1 
ATOM   2583 C  CD1 . LEU   A 1 321 ? 20.869 3.617   17.910  1.00 13.48 ?  762  LEU   A CD1 1 
ATOM   2584 C  CD2 . LEU   A 1 321 ? 18.537 3.138   18.673  1.00 13.03 ?  762  LEU   A CD2 1 
ATOM   2585 N  N   . GLY   A 1 322 ? 17.232 8.210   16.947  1.00 12.94 ?  763  GLY   A N   1 
ATOM   2586 C  CA  . GLY   A 1 322 ? 16.732 9.491   17.388  1.00 13.89 ?  763  GLY   A CA  1 
ATOM   2587 C  C   . GLY   A 1 322 ? 17.778 10.530  17.702  1.00 13.50 ?  763  GLY   A C   1 
ATOM   2588 O  O   . GLY   A 1 322 ? 17.419 11.608  18.194  1.00 16.96 ?  763  GLY   A O   1 
ATOM   2589 N  N   . ASP   A 1 323 ? 19.055 10.250  17.443  1.00 12.68 ?  764  ASP   A N   1 
ATOM   2590 C  CA  . ASP   A 1 323 ? 20.103 11.230  17.690  1.00 13.26 ?  764  ASP   A CA  1 
ATOM   2591 C  C   . ASP   A 1 323 ? 20.009 12.367  16.675  1.00 12.34 ?  764  ASP   A C   1 
ATOM   2592 O  O   . ASP   A 1 323 ? 19.493 12.207  15.563  1.00 14.02 ?  764  ASP   A O   1 
ATOM   2593 C  CB  . ASP   A 1 323 ? 21.486 10.574  17.585  1.00 12.87 ?  764  ASP   A CB  1 
ATOM   2594 C  CG  . ASP   A 1 323 ? 21.709 9.482   18.629  1.00 15.05 ?  764  ASP   A CG  1 
ATOM   2595 O  OD1 . ASP   A 1 323 ? 21.052 9.539   19.688  1.00 18.68 ?  764  ASP   A OD1 1 
ATOM   2596 O  OD2 . ASP   A 1 323 ? 22.544 8.574   18.396  1.00 14.49 -1 764  ASP   A OD2 1 
ATOM   2597 N  N   . SER   A 1 324 ? 20.528 13.537  17.067  1.00 14.35 ?  765  SER   A N   1 
ATOM   2598 C  CA  . SER   A 1 324 ? 20.457 14.700  16.201  1.00 15.80 ?  765  SER   A CA  1 
ATOM   2599 C  C   . SER   A 1 324 ? 21.489 14.577  15.084  1.00 16.18 ?  765  SER   A C   1 
ATOM   2600 O  O   . SER   A 1 324 ? 22.571 14.021  15.287  1.00 17.45 ?  765  SER   A O   1 
ATOM   2601 C  CB  . SER   A 1 324 ? 20.737 15.968  17.001  1.00 17.23 ?  765  SER   A CB  1 
ATOM   2602 O  OG  . SER   A 1 324 ? 19.786 16.126  18.038  0.67 18.11 ?  765  SER   A OG  1 
ATOM   2603 N  N   . PRO   A 1 325 ? 21.175 15.080  13.894  1.00 16.36 ?  766  PRO   A N   1 
ATOM   2604 C  CA  . PRO   A 1 325 ? 22.097 14.941  12.764  1.00 16.17 ?  766  PRO   A CA  1 
ATOM   2605 C  C   . PRO   A 1 325 ? 23.421 15.630  13.043  1.00 17.18 ?  766  PRO   A C   1 
ATOM   2606 O  O   . PRO   A 1 325 ? 23.451 16.747  13.578  1.00 17.77 ?  766  PRO   A O   1 
ATOM   2607 C  CB  . PRO   A 1 325 ? 21.347 15.635  11.618  1.00 15.59 ?  766  PRO   A CB  1 
ATOM   2608 C  CG  . PRO   A 1 325 ? 19.901 15.525  11.991  1.00 17.13 ?  766  PRO   A CG  1 
ATOM   2609 C  CD  . PRO   A 1 325 ? 19.890 15.678  13.492  1.00 17.04 ?  766  PRO   A CD  1 
ATOM   2610 N  N   . PRO   A 1 326 ? 24.540 14.993  12.710  1.00 16.57 ?  767  PRO   A N   1 
ATOM   2611 C  CA  . PRO   A 1 326 ? 25.830 15.689  12.764  1.00 15.86 ?  767  PRO   A CA  1 
ATOM   2612 C  C   . PRO   A 1 326 ? 25.873 16.791  11.717  1.00 16.09 ?  767  PRO   A C   1 
ATOM   2613 O  O   . PRO   A 1 326 ? 25.142 16.775  10.722  1.00 16.47 ?  767  PRO   A O   1 
ATOM   2614 C  CB  . PRO   A 1 326 ? 26.846 14.583  12.456  1.00 14.82 ?  767  PRO   A CB  1 
ATOM   2615 C  CG  . PRO   A 1 326 ? 26.065 13.562  11.679  1.00 17.57 ?  767  PRO   A CG  1 
ATOM   2616 C  CD  . PRO   A 1 326 ? 24.655 13.621  12.182  1.00 18.09 ?  767  PRO   A CD  1 
ATOM   2617 N  N   . SER   A 1 327 ? 26.745 17.763  11.952  1.00 15.30 ?  768  SER   A N   1 
ATOM   2618 C  CA  . SER   A 1 327 ? 26.804 18.944  11.104  1.00 13.06 ?  768  SER   A CA  1 
ATOM   2619 C  C   . SER   A 1 327 ? 27.499 18.637  9.781   1.00 13.09 ?  768  SER   A C   1 
ATOM   2620 O  O   . SER   A 1 327 ? 28.600 18.079  9.763   1.00 13.27 ?  768  SER   A O   1 
ATOM   2621 C  CB  . SER   A 1 327 ? 27.579 20.053  11.805  1.00 13.73 ?  768  SER   A CB  1 
ATOM   2622 O  OG  . SER   A 1 327 ? 27.005 20.349  13.056  1.00 13.99 ?  768  SER   A OG  1 
ATOM   2623 N  N   . LEU   A 1 328 ? 26.870 19.033  8.675   1.00 13.85 ?  769  LEU   A N   1 
ATOM   2624 C  CA  . LEU   A 1 328 ? 27.520 18.932  7.376   1.00 13.06 ?  769  LEU   A CA  1 
ATOM   2625 C  C   . LEU   A 1 328 ? 28.607 19.987  7.258   1.00 16.79 ?  769  LEU   A C   1 
ATOM   2626 O  O   . LEU   A 1 328 ? 28.570 21.036  7.912   1.00 17.77 ?  769  LEU   A O   1 
ATOM   2627 C  CB  . LEU   A 1 328 ? 26.511 19.144  6.242   1.00 14.35 ?  769  LEU   A CB  1 
ATOM   2628 C  CG  . LEU   A 1 328 ? 25.404 18.094  6.151   1.00 14.52 ?  769  LEU   A CG  1 
ATOM   2629 C  CD1 . LEU   A 1 328 ? 24.371 18.469  5.086   1.00 15.59 ?  769  LEU   A CD1 1 
ATOM   2630 C  CD2 . LEU   A 1 328 ? 25.985 16.719  5.879   1.00 16.52 ?  769  LEU   A CD2 1 
ATOM   2631 N  N   . ASP   A 1 329 ? 29.595 19.688  6.426   1.00 18.32 ?  770  ASP   A N   1 
ATOM   2632 C  CA  . ASP   A 1 329 ? 30.563 20.693  6.038   1.00 21.54 ?  770  ASP   A CA  1 
ATOM   2633 C  C   . ASP   A 1 329 ? 29.849 21.800  5.262   1.00 23.79 ?  770  ASP   A C   1 
ATOM   2634 O  O   . ASP   A 1 329 ? 28.680 21.673  4.880   1.00 20.74 ?  770  ASP   A O   1 
ATOM   2635 C  CB  . ASP   A 1 329 ? 31.633 20.048  5.158   1.00 24.19 ?  770  ASP   A CB  1 
ATOM   2636 C  CG  . ASP   A 1 329 ? 32.968 20.767  5.223   1.00 29.59 ?  770  ASP   A CG  1 
ATOM   2637 O  OD1 . ASP   A 1 329 ? 33.034 21.890  5.776   1.00 29.13 ?  770  ASP   A OD1 1 
ATOM   2638 O  OD2 . ASP   A 1 329 ? 33.956 20.197  4.711   1.00 31.89 -1 770  ASP   A OD2 1 
ATOM   2639 N  N   . HIS   A 1 330 ? 30.558 22.904  5.043   1.00 28.44 ?  771  HIS   A N   1 
ATOM   2640 C  CA  . HIS   A 1 330 ? 30.050 23.941  4.154   1.00 34.28 ?  771  HIS   A CA  1 
ATOM   2641 C  C   . HIS   A 1 330 ? 29.805 23.345  2.774   1.00 33.09 ?  771  HIS   A C   1 
ATOM   2642 O  O   . HIS   A 1 330 ? 30.703 22.740  2.181   1.00 33.62 ?  771  HIS   A O   1 
ATOM   2643 C  CB  . HIS   A 1 330 ? 31.052 25.090  4.064   1.00 40.49 ?  771  HIS   A CB  1 
ATOM   2644 N  N   . LEU   A 1 331 ? 28.582 23.501  2.274   1.00 33.43 ?  772  LEU   A N   1 
ATOM   2645 C  CA  . LEU   A 1 331 ? 28.185 22.894  1.007   1.00 33.80 ?  772  LEU   A CA  1 
ATOM   2646 C  C   . LEU   A 1 331 ? 28.654 23.782  -0.140  1.00 37.31 ?  772  LEU   A C   1 
ATOM   2647 O  O   . LEU   A 1 331 ? 28.151 24.896  -0.320  1.00 40.09 ?  772  LEU   A O   1 
ATOM   2648 C  CB  . LEU   A 1 331 ? 26.671 22.701  0.973   1.00 30.83 ?  772  LEU   A CB  1 
ATOM   2649 C  CG  . LEU   A 1 331 ? 26.131 21.713  2.013   1.00 29.69 ?  772  LEU   A CG  1 
ATOM   2650 C  CD1 . LEU   A 1 331 ? 24.627 21.504  1.862   1.00 30.24 ?  772  LEU   A CD1 1 
ATOM   2651 C  CD2 . LEU   A 1 331 ? 26.874 20.381  1.932   1.00 28.77 ?  772  LEU   A CD2 1 
ATOM   2652 N  N   . THR   A 1 332 ? 29.623 23.288  -0.914  1.00 36.31 ?  773  THR   A N   1 
ATOM   2653 C  CA  . THR   A 1 332 ? 30.088 23.999  -2.091  1.00 35.32 ?  773  THR   A CA  1 
ATOM   2654 C  C   . THR   A 1 332 ? 28.944 24.128  -3.097  1.00 35.79 ?  773  THR   A C   1 
ATOM   2655 O  O   . THR   A 1 332 ? 27.955 23.394  -3.022  1.00 35.28 ?  773  THR   A O   1 
ATOM   2656 C  CB  . THR   A 1 332 ? 31.254 23.236  -2.720  1.00 35.23 ?  773  THR   A CB  1 
ATOM   2657 O  OG1 . THR   A 1 332 ? 30.880 21.867  -2.926  1.00 35.67 ?  773  THR   A OG1 1 
ATOM   2658 C  CG2 . THR   A 1 332 ? 32.477 23.290  -1.819  1.00 35.69 ?  773  THR   A CG2 1 
ATOM   2659 N  N   . PRO   A 1 333 ? 29.042 25.069  -4.037  1.00 35.55 ?  774  PRO   A N   1 
ATOM   2660 C  CA  . PRO   A 1 333 ? 28.020 25.150  -5.088  1.00 34.52 ?  774  PRO   A CA  1 
ATOM   2661 C  C   . PRO   A 1 333 ? 27.949 23.832  -5.839  1.00 29.70 ?  774  PRO   A C   1 
ATOM   2662 O  O   . PRO   A 1 333 ? 28.964 23.167  -6.049  1.00 30.34 ?  774  PRO   A O   1 
ATOM   2663 C  CB  . PRO   A 1 333 ? 28.528 26.278  -5.994  1.00 36.64 ?  774  PRO   A CB  1 
ATOM   2664 C  CG  . PRO   A 1 333 ? 29.439 27.084  -5.134  1.00 37.63 ?  774  PRO   A CG  1 
ATOM   2665 C  CD  . PRO   A 1 333 ? 30.071 26.116  -4.182  1.00 36.98 ?  774  PRO   A CD  1 
ATOM   2666 N  N   . LEU   A 1 334 ? 26.735 23.443  -6.214  1.00 27.79 ?  775  LEU   A N   1 
ATOM   2667 C  CA  . LEU   A 1 334 ? 26.557 22.194  -6.941  1.00 26.77 ?  775  LEU   A CA  1 
ATOM   2668 C  C   . LEU   A 1 334 ? 27.373 22.207  -8.223  1.00 27.01 ?  775  LEU   A C   1 
ATOM   2669 O  O   . LEU   A 1 334 ? 27.434 23.218  -8.931  1.00 26.98 ?  775  LEU   A O   1 
ATOM   2670 C  CB  . LEU   A 1 334 ? 25.087 21.989  -7.300  1.00 26.97 ?  775  LEU   A CB  1 
ATOM   2671 C  CG  . LEU   A 1 334 ? 24.059 22.161  -6.191  1.00 29.17 ?  775  LEU   A CG  1 
ATOM   2672 C  CD1 . LEU   A 1 334 ? 22.648 22.063  -6.764  1.00 30.73 ?  775  LEU   A CD1 1 
ATOM   2673 C  CD2 . LEU   A 1 334 ? 24.306 21.113  -5.130  1.00 29.73 ?  775  LEU   A CD2 1 
ATOM   2674 N  N   . LYS   A 1 335 ? 28.011 21.076  -8.515  1.00 26.30 ?  776  LYS   A N   1 
ATOM   2675 C  CA  . LYS   A 1 335 ? 28.623 20.895  -9.823  1.00 25.99 ?  776  LYS   A CA  1 
ATOM   2676 C  C   . LYS   A 1 335 ? 27.574 21.132  -10.901 1.00 25.44 ?  776  LYS   A C   1 
ATOM   2677 O  O   . LYS   A 1 335 ? 26.423 20.705  -10.771 1.00 24.16 ?  776  LYS   A O   1 
ATOM   2678 C  CB  . LYS   A 1 335 ? 29.198 19.482  -9.935  1.00 27.13 ?  776  LYS   A CB  1 
ATOM   2679 C  CG  . LYS   A 1 335 ? 30.392 19.228  -9.024  1.00 29.71 ?  776  LYS   A CG  1 
ATOM   2680 C  CD  . LYS   A 1 335 ? 29.999 18.430  -7.794  1.00 29.63 ?  776  LYS   A CD  1 
ATOM   2681 C  CE  . LYS   A 1 335 ? 31.215 17.756  -7.161  1.00 29.23 ?  776  LYS   A CE  1 
ATOM   2682 N  NZ  . LYS   A 1 335 ? 32.083 18.741  -6.457  1.00 29.41 ?  776  LYS   A NZ  1 
ATOM   2683 N  N   . THR   A 1 336 ? 27.963 21.853  -11.956 1.00 26.20 ?  777  THR   A N   1 
ATOM   2684 C  CA  . THR   A 1 336 ? 26.975 22.292  -12.938 1.00 26.51 ?  777  THR   A CA  1 
ATOM   2685 C  C   . THR   A 1 336 ? 26.251 21.110  -13.576 1.00 24.33 ?  777  THR   A C   1 
ATOM   2686 O  O   . THR   A 1 336 ? 25.040 21.175  -13.818 1.00 25.01 ?  777  THR   A O   1 
ATOM   2687 C  CB  . THR   A 1 336 ? 27.624 23.189  -13.991 1.00 30.14 ?  777  THR   A CB  1 
ATOM   2688 O  OG1 . THR   A 1 336 ? 28.639 22.454  -14.685 1.00 34.35 ?  777  THR   A OG1 1 
ATOM   2689 C  CG2 . THR   A 1 336 ? 28.246 24.413  -13.330 1.00 28.59 ?  777  THR   A CG2 1 
ATOM   2690 N  N   . SER   A 1 337 ? 26.964 20.009  -13.830 1.00 21.61 ?  778  SER   A N   1 
ATOM   2691 C  CA  . SER   A 1 337 ? 26.298 18.842  -14.401 1.00 21.92 ?  778  SER   A CA  1 
ATOM   2692 C  C   . SER   A 1 337 ? 25.264 18.253  -13.444 1.00 19.33 ?  778  SER   A C   1 
ATOM   2693 O  O   . SER   A 1 337 ? 24.297 17.627  -13.892 1.00 18.71 ?  778  SER   A O   1 
ATOM   2694 C  CB  . SER   A 1 337 ? 27.324 17.787  -14.812 1.00 23.65 ?  778  SER   A CB  1 
ATOM   2695 O  OG  . SER   A 1 337 ? 27.945 17.230  -13.669 1.00 23.76 ?  778  SER   A OG  1 
ATOM   2696 N  N   . ALA   A 1 338 ? 25.437 18.455  -12.133 1.00 18.82 ?  779  ALA   A N   1 
ATOM   2697 C  CA  . ALA   A 1 338 ? 24.446 17.970  -11.177 1.00 16.56 ?  779  ALA   A CA  1 
ATOM   2698 C  C   . ALA   A 1 338 ? 23.150 18.774  -11.267 1.00 16.93 ?  779  ALA   A C   1 
ATOM   2699 O  O   . ALA   A 1 338 ? 22.049 18.214  -11.143 1.00 15.08 ?  779  ALA   A O   1 
ATOM   2700 C  CB  . ALA   A 1 338 ? 25.034 18.009  -9.771  1.00 17.12 ?  779  ALA   A CB  1 
ATOM   2701 N  N   . THR   A 1 339 ? 23.258 20.085  -11.512 1.00 19.58 ?  780  THR   A N   1 
ATOM   2702 C  CA  . THR   A 1 339 ? 22.057 20.888  -11.717 1.00 20.59 ?  780  THR   A CA  1 
ATOM   2703 C  C   . THR   A 1 339 ? 21.322 20.449  -12.974 1.00 20.25 ?  780  THR   A C   1 
ATOM   2704 O  O   . THR   A 1 339 ? 20.088 20.378  -12.985 1.00 20.96 ?  780  THR   A O   1 
ATOM   2705 C  CB  . THR   A 1 339 ? 22.419 22.372  -11.787 1.00 23.27 ?  780  THR   A CB  1 
ATOM   2706 O  OG1 . THR   A 1 339 ? 23.002 22.775  -10.540 1.00 25.90 ?  780  THR   A OG1 1 
ATOM   2707 C  CG2 . THR   A 1 339 ? 21.173 23.212  -12.059 1.00 26.09 ?  780  THR   A CG2 1 
ATOM   2708 N  N   . VAL   A 1 340 ? 22.067 20.136  -14.037 1.00 20.11 ?  781  VAL   A N   1 
ATOM   2709 C  CA  . VAL   A 1 340 ? 21.453 19.641  -15.270 1.00 20.44 ?  781  VAL   A CA  1 
ATOM   2710 C  C   . VAL   A 1 340 ? 20.681 18.354  -14.997 1.00 18.68 ?  781  VAL   A C   1 
ATOM   2711 O  O   . VAL   A 1 340 ? 19.520 18.204  -15.404 1.00 16.86 ?  781  VAL   A O   1 
ATOM   2712 C  CB  . VAL   A 1 340 ? 22.518 19.451  -16.366 1.00 22.52 ?  781  VAL   A CB  1 
ATOM   2713 C  CG1 . VAL   A 1 340 ? 21.895 18.833  -17.615 1.00 22.41 ?  781  VAL   A CG1 1 
ATOM   2714 C  CG2 . VAL   A 1 340 ? 23.196 20.785  -16.692 1.00 24.79 ?  781  VAL   A CG2 1 
ATOM   2715 N  N   . SER   A 1 341 ? 21.311 17.410  -14.288 1.00 15.90 ?  782  SER   A N   1 
ATOM   2716 C  CA  . SER   A 1 341 ? 20.641 16.155  -13.958 1.00 14.81 ?  782  SER   A CA  1 
ATOM   2717 C  C   . SER   A 1 341 ? 19.340 16.400  -13.210 1.00 16.12 ?  782  SER   A C   1 
ATOM   2718 O  O   . SER   A 1 341 ? 18.298 15.831  -13.558 1.00 16.64 ?  782  SER   A O   1 
ATOM   2719 C  CB  . SER   A 1 341 ? 21.565 15.271  -13.118 1.00 15.23 ?  782  SER   A CB  1 
ATOM   2720 O  OG  . SER   A 1 341 ? 22.677 14.827  -13.874 1.00 16.64 ?  782  SER   A OG  1 
ATOM   2721 N  N   . ILE   A 1 342 ? 19.386 17.235  -12.164 1.00 13.79 ?  783  ILE   A N   1 
ATOM   2722 C  CA  . ILE   A 1 342 ? 18.192 17.495  -11.366 1.00 14.65 ?  783  ILE   A CA  1 
ATOM   2723 C  C   . ILE   A 1 342 ? 17.089 18.107  -12.223 1.00 14.45 ?  783  ILE   A C   1 
ATOM   2724 O  O   . ILE   A 1 342 ? 15.913 17.734  -12.104 1.00 14.88 ?  783  ILE   A O   1 
ATOM   2725 C  CB  . ILE   A 1 342 ? 18.542 18.370  -10.149 1.00 15.21 ?  783  ILE   A CB  1 
ATOM   2726 C  CG1 . ILE   A 1 342 ? 19.405 17.559  -9.185  1.00 16.20 ?  783  ILE   A CG1 1 
ATOM   2727 C  CG2 . ILE   A 1 342 ? 17.266 18.858  -9.457  1.00 16.38 ?  783  ILE   A CG2 1 
ATOM   2728 C  CD1 . ILE   A 1 342 ? 20.048 18.370  -8.076  1.00 17.23 ?  783  ILE   A CD1 1 
ATOM   2729 N  N   . ASN   A 1 343 ? 17.445 19.072  -13.074 1.00 15.44 ?  784  ASN   A N   1 
ATOM   2730 C  CA  . ASN   A 1 343 ? 16.453 19.702  -13.945 1.00 17.78 ?  784  ASN   A CA  1 
ATOM   2731 C  C   . ASN   A 1 343 ? 15.820 18.682  -14.882 1.00 17.53 ?  784  ASN   A C   1 
ATOM   2732 O  O   . ASN   A 1 343 ? 14.606 18.718  -15.130 1.00 18.61 ?  784  ASN   A O   1 
ATOM   2733 C  CB  . ASN   A 1 343 ? 17.105 20.808  -14.777 1.00 21.30 ?  784  ASN   A CB  1 
ATOM   2734 C  CG  . ASN   A 1 343 ? 17.394 22.059  -13.978 1.00 24.07 ?  784  ASN   A CG  1 
ATOM   2735 O  OD1 . ASN   A 1 343 ? 16.789 22.300  -12.940 1.00 24.63 ?  784  ASN   A OD1 1 
ATOM   2736 N  ND2 . ASN   A 1 343 ? 18.316 22.880  -14.481 1.00 25.92 ?  784  ASN   A ND2 1 
ATOM   2737 N  N   . ASN   A 1 344 ? 16.630 17.770  -15.418 1.00 16.22 ?  785  ASN   A N   1 
ATOM   2738 C  CA  . ASN   A 1 344 ? 16.107 16.746  -16.319 1.00 16.17 ?  785  ASN   A CA  1 
ATOM   2739 C  C   . ASN   A 1 344 ? 15.113 15.827  -15.618 1.00 16.21 ?  785  ASN   A C   1 
ATOM   2740 O  O   . ASN   A 1 344 ? 14.056 15.505  -16.174 1.00 15.86 ?  785  ASN   A O   1 
ATOM   2741 C  CB  . ASN   A 1 344 ? 17.253 15.957  -16.941 1.00 18.47 ?  785  ASN   A CB  1 
ATOM   2742 C  CG  . ASN   A 1 344 ? 17.937 16.724  -18.036 1.00 22.21 ?  785  ASN   A CG  1 
ATOM   2743 O  OD1 . ASN   A 1 344 ? 17.311 17.557  -18.697 1.00 24.67 ?  785  ASN   A OD1 1 
ATOM   2744 N  ND2 . ASN   A 1 344 ? 19.210 16.442  -18.257 1.00 21.96 ?  785  ASN   A ND2 1 
ATOM   2745 N  N   . VAL   A 1 345 ? 15.423 15.404  -14.386 1.00 15.08 ?  786  VAL   A N   1 
ATOM   2746 C  CA  . VAL   A 1 345 ? 14.477 14.576  -13.649 1.00 15.16 ?  786  VAL   A CA  1 
ATOM   2747 C  C   . VAL   A 1 345 ? 13.213 15.362  -13.324 1.00 16.04 ?  786  VAL   A C   1 
ATOM   2748 O  O   . VAL   A 1 345 ? 12.095 14.837  -13.430 1.00 14.63 ?  786  VAL   A O   1 
ATOM   2749 C  CB  . VAL   A 1 345 ? 15.123 13.990  -12.377 1.00 14.95 ?  786  VAL   A CB  1 
ATOM   2750 C  CG1 . VAL   A 1 345 ? 14.154 13.028  -11.692 1.00 17.01 ?  786  VAL   A CG1 1 
ATOM   2751 C  CG2 . VAL   A 1 345 ? 16.428 13.291  -12.706 1.00 16.18 ?  786  VAL   A CG2 1 
ATOM   2752 N  N   . LEU   A 1 346 ? 13.368 16.621  -12.899 1.00 16.13 ?  787  LEU   A N   1 
ATOM   2753 C  CA  . LEU   A 1 346 ? 12.212 17.448  -12.552 1.00 19.92 ?  787  LEU   A CA  1 
ATOM   2754 C  C   . LEU   A 1 346 ? 11.252 17.562  -13.724 1.00 20.73 ?  787  LEU   A C   1 
ATOM   2755 O  O   . LEU   A 1 346 ? 10.034 17.431  -13.560 1.00 21.90 ?  787  LEU   A O   1 
ATOM   2756 C  CB  . LEU   A 1 346 ? 12.680 18.844  -12.131 1.00 21.49 ?  787  LEU   A CB  1 
ATOM   2757 C  CG  . LEU   A 1 346 ? 13.197 19.053  -10.709 1.00 24.58 ?  787  LEU   A CG  1 
ATOM   2758 C  CD1 . LEU   A 1 346 ? 13.798 20.439  -10.581 1.00 26.91 ?  787  LEU   A CD1 1 
ATOM   2759 C  CD2 . LEU   A 1 346 ? 12.077 18.876  -9.687  1.00 25.98 ?  787  LEU   A CD2 1 
ATOM   2760 N  N   . ARG   A 1 347 ? 11.791 17.788  -14.919 1.00 18.14 ?  788  ARG   A N   1 
ATOM   2761 C  CA  . ARG   A 1 347 ? 10.958 17.961  -16.097 1.00 21.16 ?  788  ARG   A CA  1 
ATOM   2762 C  C   . ARG   A 1 347 ? 10.361 16.641  -16.565 1.00 22.38 ?  788  ARG   A C   1 
ATOM   2763 O  O   . ARG   A 1 347 ? 9.240  16.624  -17.085 1.00 24.88 ?  788  ARG   A O   1 
ATOM   2764 C  CB  . ARG   A 1 347 ? 11.766 18.651  -17.196 1.00 24.99 ?  788  ARG   A CB  1 
ATOM   2765 C  CG  . ARG   A 1 347 ? 11.743 20.173  -17.081 1.00 31.42 ?  788  ARG   A CG  1 
ATOM   2766 C  CD  . ARG   A 1 347 ? 13.130 20.793  -17.182 1.00 36.58 ?  788  ARG   A CD  1 
ATOM   2767 N  NE  . ARG   A 1 347 ? 13.228 22.027  -16.403 1.00 40.18 ?  788  ARG   A NE  1 
ATOM   2768 C  CZ  . ARG   A 1 347 ? 14.142 22.973  -16.605 1.00 41.16 ?  788  ARG   A CZ  1 
ATOM   2769 N  NH1 . ARG   A 1 347 ? 15.043 22.835  -17.570 1.00 39.99 ?  788  ARG   A NH1 1 
ATOM   2770 N  NH2 . ARG   A 1 347 ? 14.154 24.059  -15.843 1.00 41.64 ?  788  ARG   A NH2 1 
ATOM   2771 N  N   . ALA   A 1 348 ? 11.066 15.528  -16.357 1.00 19.61 ?  789  ALA   A N   1 
ATOM   2772 C  CA  . ALA   A 1 348 ? 10.511 14.230  -16.723 1.00 17.84 ?  789  ALA   A CA  1 
ATOM   2773 C  C   . ALA   A 1 348 ? 9.380  13.813  -15.794 1.00 18.66 ?  789  ALA   A C   1 
ATOM   2774 O  O   . ALA   A 1 348 ? 8.496  13.052  -16.201 1.00 20.20 ?  789  ALA   A O   1 
ATOM   2775 C  CB  . ALA   A 1 348 ? 11.611 13.172  -16.727 1.00 19.66 ?  789  ALA   A CB  1 
ATOM   2776 N  N   . HIS   A 1 349 ? 9.382  14.288  -14.549 1.00 15.38 ?  790  HIS   A N   1 
ATOM   2777 C  CA  . HIS   A 1 349 ? 8.439  13.800  -13.560 1.00 15.84 ?  790  HIS   A CA  1 
ATOM   2778 C  C   . HIS   A 1 349 ? 7.364  14.796  -13.138 1.00 14.94 ?  790  HIS   A C   1 
ATOM   2779 O  O   . HIS   A 1 349 ? 6.352  14.373  -12.571 1.00 16.56 ?  790  HIS   A O   1 
ATOM   2780 C  CB  . HIS   A 1 349 ? 9.187  13.227  -12.347 1.00 15.30 ?  790  HIS   A CB  1 
ATOM   2781 C  CG  . HIS   A 1 349 ? 9.638  11.820  -12.565 1.00 17.00 ?  790  HIS   A CG  1 
ATOM   2782 N  ND1 . HIS   A 1 349 ? 8.792  10.744  -12.405 1.00 15.99 ?  790  HIS   A ND1 1 
ATOM   2783 C  CD2 . HIS   A 1 349 ? 10.822 11.314  -12.986 1.00 16.47 ?  790  HIS   A CD2 1 
ATOM   2784 C  CE1 . HIS   A 1 349 ? 9.444  9.633   -12.701 1.00 15.17 ?  790  HIS   A CE1 1 
ATOM   2785 N  NE2 . HIS   A 1 349 ? 10.680 9.949   -13.045 1.00 14.81 ?  790  HIS   A NE2 1 
ATOM   2786 N  N   . ALA   A 1 350 ? 7.553  16.089  -13.399 1.00 16.35 ?  791  ALA   A N   1 
ATOM   2787 C  CA  . ALA   A 1 350 ? 6.489  17.067  -13.173 1.00 18.98 ?  791  ALA   A CA  1 
ATOM   2788 C  C   . ALA   A 1 350 ? 5.137  16.664  -13.759 1.00 20.47 ?  791  ALA   A C   1 
ATOM   2789 O  O   . ALA   A 1 350 ? 4.112  16.956  -13.119 1.00 19.95 ?  791  ALA   A O   1 
ATOM   2790 C  CB  . ALA   A 1 350 ? 6.934  18.451  -13.670 1.00 19.91 ?  791  ALA   A CB  1 
ATOM   2791 N  N   . PRO   A 1 351 ? 5.048  16.010  -14.922 1.00 19.59 ?  792  PRO   A N   1 
ATOM   2792 C  CA  . PRO   A 1 351 ? 3.731  15.530  -15.378 1.00 21.41 ?  792  PRO   A CA  1 
ATOM   2793 C  C   . PRO   A 1 351 ? 3.042  14.583  -14.415 1.00 22.63 ?  792  PRO   A C   1 
ATOM   2794 O  O   . PRO   A 1 351 ? 1.807  14.537  -14.397 1.00 24.18 ?  792  PRO   A O   1 
ATOM   2795 C  CB  . PRO   A 1 351 ? 4.052  14.835  -16.705 1.00 21.95 ?  792  PRO   A CB  1 
ATOM   2796 C  CG  . PRO   A 1 351 ? 5.263  15.511  -17.189 1.00 21.26 ?  792  PRO   A CG  1 
ATOM   2797 C  CD  . PRO   A 1 351 ? 6.067  15.860  -15.976 1.00 18.76 ?  792  PRO   A CD  1 
ATOM   2798 N  N   . PHE   A 1 352 ? 3.795  13.833  -13.605 1.00 18.33 ?  793  PHE   A N   1 
ATOM   2799 C  CA  . PHE   A 1 352 ? 3.218  12.826  -12.724 1.00 18.86 ?  793  PHE   A CA  1 
ATOM   2800 C  C   . PHE   A 1 352 ? 3.095  13.274  -11.274 1.00 17.64 ?  793  PHE   A C   1 
ATOM   2801 O  O   . PHE   A 1 352 ? 2.254  12.734  -10.539 1.00 21.69 ?  793  PHE   A O   1 
ATOM   2802 C  CB  . PHE   A 1 352 ? 4.042  11.538  -12.802 1.00 18.09 ?  793  PHE   A CB  1 
ATOM   2803 C  CG  . PHE   A 1 352 ? 4.290  11.090  -14.209 1.00 15.49 ?  793  PHE   A CG  1 
ATOM   2804 C  CD1 . PHE   A 1 352 ? 3.265  10.535  -14.956 1.00 18.24 ?  793  PHE   A CD1 1 
ATOM   2805 C  CD2 . PHE   A 1 352 ? 5.524  11.256  -14.801 1.00 17.04 ?  793  PHE   A CD2 1 
ATOM   2806 C  CE1 . PHE   A 1 352 ? 3.478  10.141  -16.260 1.00 17.17 ?  793  PHE   A CE1 1 
ATOM   2807 C  CE2 . PHE   A 1 352 ? 5.752  10.858  -16.095 1.00 18.41 ?  793  PHE   A CE2 1 
ATOM   2808 C  CZ  . PHE   A 1 352 ? 4.714  10.302  -16.839 1.00 16.74 ?  793  PHE   A CZ  1 
ATOM   2809 N  N   . TRP   A 1 353 ? 3.911  14.236  -10.841 1.00 18.16 ?  794  TRP   A N   1 
ATOM   2810 C  CA  . TRP   A 1 353 ? 3.964  14.672  -9.445  1.00 16.66 ?  794  TRP   A CA  1 
ATOM   2811 C  C   . TRP   A 1 353 ? 3.783  16.187  -9.413  1.00 19.49 ?  794  TRP   A C   1 
ATOM   2812 O  O   . TRP   A 1 353 ? 4.716  16.940  -9.713  1.00 19.93 ?  794  TRP   A O   1 
ATOM   2813 C  CB  . TRP   A 1 353 ? 5.285  14.243  -8.802  1.00 17.18 ?  794  TRP   A CB  1 
ATOM   2814 C  CG  . TRP   A 1 353 ? 5.520  12.775  -8.944  1.00 16.13 ?  794  TRP   A CG  1 
ATOM   2815 C  CD1 . TRP   A 1 353 ? 6.292  12.148  -9.881  1.00 16.38 ?  794  TRP   A CD1 1 
ATOM   2816 C  CD2 . TRP   A 1 353 ? 4.934  11.746  -8.149  1.00 16.61 ?  794  TRP   A CD2 1 
ATOM   2817 N  NE1 . TRP   A 1 353 ? 6.241  10.783  -9.692  1.00 14.41 ?  794  TRP   A NE1 1 
ATOM   2818 C  CE2 . TRP   A 1 353 ? 5.410  10.513  -8.642  1.00 16.03 ?  794  TRP   A CE2 1 
ATOM   2819 C  CE3 . TRP   A 1 353 ? 4.065  11.746  -7.055  1.00 18.88 ?  794  TRP   A CE3 1 
ATOM   2820 C  CZ2 . TRP   A 1 353 ? 5.047  9.292   -8.078  1.00 17.17 ?  794  TRP   A CZ2 1 
ATOM   2821 C  CZ3 . TRP   A 1 353 ? 3.704  10.531  -6.494  1.00 21.45 ?  794  TRP   A CZ3 1 
ATOM   2822 C  CH2 . TRP   A 1 353 ? 4.196  9.320   -7.008  1.00 19.76 ?  794  TRP   A CH2 1 
ATOM   2823 N  N   . SER   A 1 354 ? 2.583  16.633  -9.038  1.00 21.13 ?  795  SER   A N   1 
ATOM   2824 C  CA  A SER   A 1 354 ? 2.284  18.061  -9.036  0.36 22.25 ?  795  SER   A CA  1 
ATOM   2825 C  CA  B SER   A 1 354 ? 2.301  18.063  -9.053  0.64 22.16 ?  795  SER   A CA  1 
ATOM   2826 C  C   . SER   A 1 354 ? 3.169  18.841  -8.073  1.00 22.24 ?  795  SER   A C   1 
ATOM   2827 O  O   . SER   A 1 354 ? 3.341  20.050  -8.251  1.00 22.50 ?  795  SER   A O   1 
ATOM   2828 C  CB  A SER   A 1 354 ? 0.810  18.294  -8.699  0.36 23.42 ?  795  SER   A CB  1 
ATOM   2829 C  CB  B SER   A 1 354 ? 0.816  18.321  -8.794  0.64 23.48 ?  795  SER   A CB  1 
ATOM   2830 O  OG  A SER   A 1 354 ? -0.034 17.695  -9.666  0.36 23.84 ?  795  SER   A OG  1 
ATOM   2831 O  OG  B SER   A 1 354 ? 0.423  17.798  -7.541  0.64 23.75 ?  795  SER   A OG  1 
ATOM   2832 N  N   . SER   A 1 355 ? 3.732  18.176  -7.057  1.00 21.93 ?  796  SER   A N   1 
ATOM   2833 C  CA  . SER   A 1 355 ? 4.629  18.842  -6.116  1.00 24.02 ?  796  SER   A CA  1 
ATOM   2834 C  C   . SER   A 1 355 ? 5.898  19.361  -6.784  1.00 26.36 ?  796  SER   A C   1 
ATOM   2835 O  O   . SER   A 1 355 ? 6.581  20.213  -6.206  1.00 28.94 ?  796  SER   A O   1 
ATOM   2836 C  CB  . SER   A 1 355 ? 4.981  17.907  -4.950  1.00 24.21 ?  796  SER   A CB  1 
ATOM   2837 O  OG  . SER   A 1 355 ? 5.747  16.792  -5.388  1.00 23.92 ?  796  SER   A OG  1 
ATOM   2838 N  N   . LEU   A 1 356 ? 6.228  18.880  -7.981  1.00 25.35 ?  797  LEU   A N   1 
ATOM   2839 C  CA  . LEU   A 1 356 ? 7.423  19.313  -8.697  1.00 22.76 ?  797  LEU   A CA  1 
ATOM   2840 C  C   . LEU   A 1 356 ? 7.178  20.500  -9.615  1.00 25.42 ?  797  LEU   A C   1 
ATOM   2841 O  O   . LEU   A 1 356 ? 8.113  20.943  -10.294 1.00 26.08 ?  797  LEU   A O   1 
ATOM   2842 C  CB  . LEU   A 1 356 ? 7.988  18.164  -9.534  1.00 22.43 ?  797  LEU   A CB  1 
ATOM   2843 C  CG  . LEU   A 1 356 ? 8.378  16.894  -8.785  1.00 20.67 ?  797  LEU   A CG  1 
ATOM   2844 C  CD1 . LEU   A 1 356 ? 8.909  15.875  -9.777  1.00 19.95 ?  797  LEU   A CD1 1 
ATOM   2845 C  CD2 . LEU   A 1 356 ? 9.413  17.195  -7.699  1.00 19.77 ?  797  LEU   A CD2 1 
ATOM   2846 N  N   . ARG   A 1 357 ? 5.959  21.018  -9.663  1.00 26.73 ?  798  ARG   A N   1 
ATOM   2847 C  CA  . ARG   A 1 357 ? 5.616  22.064  -10.620 1.00 29.65 ?  798  ARG   A CA  1 
ATOM   2848 C  C   . ARG   A 1 357 ? 5.869  23.459  -10.062 1.00 32.59 ?  798  ARG   A C   1 
ATOM   2849 O  O   . ARG   A 1 357 ? 5.944  23.650  -8.846  1.00 34.33 ?  798  ARG   A O   1 
ATOM   2850 C  CB  . ARG   A 1 357 ? 4.156  21.918  -11.059 1.00 28.25 ?  798  ARG   A CB  1 
ATOM   2851 C  CG  . ARG   A 1 357 ? 3.894  20.611  -11.790 1.00 28.18 ?  798  ARG   A CG  1 
ATOM   2852 C  CD  . ARG   A 1 357 ? 2.414  20.343  -12.039 1.00 26.79 ?  798  ARG   A CD  1 
ATOM   2853 N  NE  . ARG   A 1 357 ? 2.248  19.085  -12.764 1.00 26.88 ?  798  ARG   A NE  1 
ATOM   2854 C  CZ  . ARG   A 1 357 ? 1.079  18.532  -13.073 1.00 28.60 ?  798  ARG   A CZ  1 
ATOM   2855 N  NH1 . ARG   A 1 357 ? -0.061 19.122  -12.730 1.00 29.99 ?  798  ARG   A NH1 1 
ATOM   2856 N  NH2 . ARG   A 1 357 ? 1.052  17.387  -13.740 1.00 29.29 ?  798  ARG   A NH2 1 
ATOM   2857 O  OXT . ARG   A 1 357 ? 6.006  24.420  -10.823 1.00 33.69 -1 798  ARG   A OXT 1 
ATOM   2858 N  N   . PRO   B 1 1   ? 64.867 5.968   1.288   1.00 31.24 ?  442  PRO   B N   1 
ATOM   2859 C  CA  . PRO   B 1 1   ? 64.725 5.061   2.433   1.00 28.85 ?  442  PRO   B CA  1 
ATOM   2860 C  C   . PRO   B 1 1   ? 63.567 4.082   2.275   1.00 26.81 ?  442  PRO   B C   1 
ATOM   2861 O  O   . PRO   B 1 1   ? 62.578 4.371   1.599   1.00 30.05 ?  442  PRO   B O   1 
ATOM   2862 C  CB  . PRO   B 1 1   ? 64.453 6.012   3.607   1.00 29.71 ?  442  PRO   B CB  1 
ATOM   2863 C  CG  . PRO   B 1 1   ? 63.926 7.255   2.983   1.00 30.89 ?  442  PRO   B CG  1 
ATOM   2864 C  CD  . PRO   B 1 1   ? 64.631 7.372   1.663   1.00 32.20 ?  442  PRO   B CD  1 
ATOM   2865 N  N   . ILE   B 1 2   ? 63.698 2.922   2.906   1.00 22.13 ?  443  ILE   B N   1 
ATOM   2866 C  CA  . ILE   B 1 2   ? 62.670 1.892   2.891   1.00 20.57 ?  443  ILE   B CA  1 
ATOM   2867 C  C   . ILE   B 1 2   ? 62.136 1.727   4.309   1.00 15.01 ?  443  ILE   B C   1 
ATOM   2868 O  O   . ILE   B 1 2   ? 62.904 1.724   5.279   1.00 16.78 ?  443  ILE   B O   1 
ATOM   2869 C  CB  . ILE   B 1 2   ? 63.237 0.562   2.359   1.00 22.74 ?  443  ILE   B CB  1 
ATOM   2870 C  CG1 . ILE   B 1 2   ? 63.702 0.720   0.905   1.00 26.44 ?  443  ILE   B CG1 1 
ATOM   2871 C  CG2 . ILE   B 1 2   ? 62.212 -0.548  2.482   1.00 21.07 ?  443  ILE   B CG2 1 
ATOM   2872 C  CD1 . ILE   B 1 2   ? 64.400 -0.513  0.341   1.00 27.91 ?  443  ILE   B CD1 1 
ATOM   2873 N  N   . THR   B 1 3   ? 60.817 1.592   4.423   1.00 13.95 ?  444  THR   B N   1 
ATOM   2874 C  CA  . THR   B 1 3   ? 60.149 1.301   5.685   1.00 13.90 ?  444  THR   B CA  1 
ATOM   2875 C  C   . THR   B 1 3   ? 59.697 -0.149  5.649   1.00 12.93 ?  444  THR   B C   1 
ATOM   2876 O  O   . THR   B 1 3   ? 58.984 -0.555  4.720   1.00 13.71 ?  444  THR   B O   1 
ATOM   2877 C  CB  . THR   B 1 3   ? 58.933 2.203   5.853   1.00 14.17 ?  444  THR   B CB  1 
ATOM   2878 O  OG1 . THR   B 1 3   ? 59.356 3.564   5.993   1.00 14.16 ?  444  THR   B OG1 1 
ATOM   2879 C  CG2 . THR   B 1 3   ? 58.103 1.774   7.081   1.00 14.16 ?  444  THR   B CG2 1 
ATOM   2880 N  N   . GLY   B 1 4   ? 60.122 -0.921  6.644   1.00 11.97 ?  445  GLY   B N   1 
ATOM   2881 C  CA  . GLY   B 1 4   ? 59.681 -2.294  6.767   1.00 13.37 ?  445  GLY   B CA  1 
ATOM   2882 C  C   . GLY   B 1 4   ? 58.385 -2.407  7.553   1.00 11.02 ?  445  GLY   B C   1 
ATOM   2883 O  O   . GLY   B 1 4   ? 58.064 -1.561  8.387   1.00 12.44 ?  445  GLY   B O   1 
ATOM   2884 N  N   . LEU   B 1 5   ? 57.637 -3.470  7.287   1.00 10.77 ?  446  LEU   B N   1 
ATOM   2885 C  CA  . LEU   B 1 5   ? 56.428 -3.778  8.042   1.00 10.46 ?  446  LEU   B CA  1 
ATOM   2886 C  C   . LEU   B 1 5   ? 56.395 -5.277  8.260   1.00 9.81  ?  446  LEU   B C   1 
ATOM   2887 O  O   . LEU   B 1 5   ? 56.577 -6.048  7.308   1.00 12.22 ?  446  LEU   B O   1 
ATOM   2888 C  CB  . LEU   B 1 5   ? 55.166 -3.349  7.277   1.00 12.02 ?  446  LEU   B CB  1 
ATOM   2889 C  CG  . LEU   B 1 5   ? 53.813 -3.597  7.963   1.00 11.45 ?  446  LEU   B CG  1 
ATOM   2890 C  CD1 . LEU   B 1 5   ? 52.817 -2.523  7.587   1.00 12.94 ?  446  LEU   B CD1 1 
ATOM   2891 C  CD2 . LEU   B 1 5   ? 53.256 -4.984  7.617   1.00 11.11 ?  446  LEU   B CD2 1 
ATOM   2892 N  N   . VAL   B 1 6   ? 56.158 -5.698  9.500   1.00 10.39 ?  447  VAL   B N   1 
ATOM   2893 C  CA  . VAL   B 1 6   ? 56.001 -7.110  9.803   1.00 10.07 ?  447  VAL   B CA  1 
ATOM   2894 C  C   . VAL   B 1 6   ? 54.617 -7.328  10.405  1.00 9.94  ?  447  VAL   B C   1 
ATOM   2895 O  O   . VAL   B 1 6   ? 54.162 -6.540  11.247  1.00 12.11 ?  447  VAL   B O   1 
ATOM   2896 C  CB  . VAL   B 1 6   ? 57.146 -7.666  10.677  1.00 10.04 ?  447  VAL   B CB  1 
ATOM   2897 C  CG1 . VAL   B 1 6   ? 57.193 -6.974  12.030  1.00 10.09 ?  447  VAL   B CG1 1 
ATOM   2898 C  CG2 . VAL   B 1 6   ? 57.025 -9.162  10.820  1.00 12.38 ?  447  VAL   B CG2 1 
ATOM   2899 N  N   . TYR   B 1 7   ? 53.937 -8.368  9.933   1.00 12.10 ?  448  TYR   B N   1 
ATOM   2900 C  CA  . TYR   B 1 7   ? 52.618 -8.770  10.398  1.00 12.20 ?  448  TYR   B CA  1 
ATOM   2901 C  C   . TYR   B 1 7   ? 52.422 -10.226 10.023  1.00 11.85 ?  448  TYR   B C   1 
ATOM   2902 O  O   . TYR   B 1 7   ? 52.806 -10.642 8.924   1.00 14.21 ?  448  TYR   B O   1 
ATOM   2903 C  CB  . TYR   B 1 7   ? 51.496 -7.935  9.758   1.00 13.05 ?  448  TYR   B CB  1 
ATOM   2904 C  CG  . TYR   B 1 7   ? 50.110 -8.508  9.982   1.00 12.11 ?  448  TYR   B CG  1 
ATOM   2905 C  CD1 . TYR   B 1 7   ? 49.482 -8.386  11.217  1.00 12.99 ?  448  TYR   B CD1 1 
ATOM   2906 C  CD2 . TYR   B 1 7   ? 49.435 -9.187  8.967   1.00 11.94 ?  448  TYR   B CD2 1 
ATOM   2907 C  CE1 . TYR   B 1 7   ? 48.226 -8.915  11.437  1.00 13.39 ?  448  TYR   B CE1 1 
ATOM   2908 C  CE2 . TYR   B 1 7   ? 48.179 -9.724  9.178   1.00 13.71 ?  448  TYR   B CE2 1 
ATOM   2909 C  CZ  . TYR   B 1 7   ? 47.572 -9.573  10.418  1.00 13.34 ?  448  TYR   B CZ  1 
ATOM   2910 O  OH  . TYR   B 1 7   ? 46.318 -10.091 10.655  1.00 13.48 ?  448  TYR   B OH  1 
ATOM   2911 N  N   . ASP   B 1 8   ? 51.808 -10.989 10.919  1.00 12.06 ?  449  ASP   B N   1 
ATOM   2912 C  CA  . ASP   B 1 8   ? 51.476 -12.382 10.647  1.00 11.73 ?  449  ASP   B CA  1 
ATOM   2913 C  C   . ASP   B 1 8   ? 50.137 -12.663 11.307  1.00 12.78 ?  449  ASP   B C   1 
ATOM   2914 O  O   . ASP   B 1 8   ? 50.002 -12.523 12.526  1.00 12.80 ?  449  ASP   B O   1 
ATOM   2915 C  CB  . ASP   B 1 8   ? 52.567 -13.314 11.189  1.00 14.04 ?  449  ASP   B CB  1 
ATOM   2916 C  CG  . ASP   B 1 8   ? 52.434 -14.737 10.682  1.00 16.14 ?  449  ASP   B CG  1 
ATOM   2917 O  OD1 . ASP   B 1 8   ? 51.300 -15.207 10.489  1.00 14.06 ?  449  ASP   B OD1 1 
ATOM   2918 O  OD2 . ASP   B 1 8   ? 53.475 -15.405 10.485  1.00 19.94 -1 449  ASP   B OD2 1 
ATOM   2919 N  N   A GLN   B 1 9   ? 49.146 -13.063 10.507  0.41 12.64 ?  450  GLN   B N   1 
ATOM   2920 N  N   B GLN   B 1 9   ? 49.154 -13.058 10.493  0.59 12.66 ?  450  GLN   B N   1 
ATOM   2921 C  CA  A GLN   B 1 9   ? 47.812 -13.312 11.043  0.41 13.01 ?  450  GLN   B CA  1 
ATOM   2922 C  CA  B GLN   B 1 9   ? 47.808 -13.332 10.987  0.59 13.12 ?  450  GLN   B CA  1 
ATOM   2923 C  C   A GLN   B 1 9   ? 47.780 -14.462 12.044  0.41 12.71 ?  450  GLN   B C   1 
ATOM   2924 C  C   B GLN   B 1 9   ? 47.796 -14.394 12.082  0.59 12.28 ?  450  GLN   B C   1 
ATOM   2925 O  O   A GLN   B 1 9   ? 46.798 -14.596 12.782  0.41 12.09 ?  450  GLN   B O   1 
ATOM   2926 O  O   B GLN   B 1 9   ? 46.887 -14.409 12.917  0.59 11.39 ?  450  GLN   B O   1 
ATOM   2927 C  CB  A GLN   B 1 9   ? 46.826 -13.575 9.904   0.41 13.85 ?  450  GLN   B CB  1 
ATOM   2928 C  CB  B GLN   B 1 9   ? 46.913 -13.750 9.812   0.59 14.38 ?  450  GLN   B CB  1 
ATOM   2929 C  CG  A GLN   B 1 9   ? 47.142 -14.819 9.097   0.41 14.66 ?  450  GLN   B CG  1 
ATOM   2930 C  CG  B GLN   B 1 9   ? 45.447 -13.983 10.162  0.59 16.09 ?  450  GLN   B CG  1 
ATOM   2931 C  CD  A GLN   B 1 9   ? 46.205 -14.995 7.919   0.41 16.76 ?  450  GLN   B CD  1 
ATOM   2932 C  CD  B GLN   B 1 9   ? 45.181 -15.388 10.682  0.59 18.01 ?  450  GLN   B CD  1 
ATOM   2933 O  OE1 A GLN   B 1 9   ? 45.007 -14.723 8.016   0.41 18.93 ?  450  GLN   B OE1 1 
ATOM   2934 O  OE1 B GLN   B 1 9   ? 45.888 -16.335 10.338  0.59 20.30 ?  450  GLN   B OE1 1 
ATOM   2935 N  NE2 A GLN   B 1 9   ? 46.748 -15.453 6.798   0.41 17.84 ?  450  GLN   B NE2 1 
ATOM   2936 N  NE2 B GLN   B 1 9   ? 44.175 -15.521 11.535  0.59 17.94 ?  450  GLN   B NE2 1 
ATOM   2937 N  N   A ARG   B 1 10  ? 48.821 -15.299 12.083  0.41 11.92 ?  451  ARG   B N   1 
ATOM   2938 N  N   B ARG   B 1 10  ? 48.786 -15.290 12.098  0.59 11.24 ?  451  ARG   B N   1 
ATOM   2939 C  CA  A ARG   B 1 10  ? 48.876 -16.366 13.075  0.41 12.13 ?  451  ARG   B CA  1 
ATOM   2940 C  CA  B ARG   B 1 10  ? 48.798 -16.362 13.087  0.59 11.64 ?  451  ARG   B CA  1 
ATOM   2941 C  C   A ARG   B 1 10  ? 48.902 -15.830 14.500  0.41 11.46 ?  451  ARG   B C   1 
ATOM   2942 C  C   B ARG   B 1 10  ? 49.003 -15.865 14.513  0.59 11.76 ?  451  ARG   B C   1 
ATOM   2943 O  O   A ARG   B 1 10  ? 48.471 -16.534 15.423  0.41 10.84 ?  451  ARG   B O   1 
ATOM   2944 O  O   B ARG   B 1 10  ? 48.809 -16.645 15.453  0.59 12.01 ?  451  ARG   B O   1 
ATOM   2945 C  CB  A ARG   B 1 10  ? 50.088 -17.264 12.837  0.41 12.39 ?  451  ARG   B CB  1 
ATOM   2946 C  CB  B ARG   B 1 10  ? 49.832 -17.422 12.721  0.59 10.03 ?  451  ARG   B CB  1 
ATOM   2947 C  CG  A ARG   B 1 10  ? 49.845 -18.386 11.840  0.41 16.17 ?  451  ARG   B CG  1 
ATOM   2948 C  CG  B ARG   B 1 10  ? 49.480 -18.175 11.433  0.59 9.29  ?  451  ARG   B CG  1 
ATOM   2949 C  CD  A ARG   B 1 10  ? 51.087 -19.249 11.705  0.41 17.47 ?  451  ARG   B CD  1 
ATOM   2950 C  CD  B ARG   B 1 10  ? 50.489 -19.298 11.131  0.59 10.10 ?  451  ARG   B CD  1 
ATOM   2951 N  NE  A ARG   B 1 10  ? 52.201 -18.484 11.152  0.41 18.91 ?  451  ARG   B NE  1 
ATOM   2952 N  NE  B ARG   B 1 10  ? 50.810 -20.059 12.336  0.59 10.38 ?  451  ARG   B NE  1 
ATOM   2953 C  CZ  A ARG   B 1 10  ? 53.463 -18.572 11.565  0.41 18.42 ?  451  ARG   B CZ  1 
ATOM   2954 C  CZ  B ARG   B 1 10  ? 50.059 -21.040 12.826  0.59 9.99  ?  451  ARG   B CZ  1 
ATOM   2955 N  NH1 A ARG   B 1 10  ? 53.807 -19.405 12.542  0.41 19.43 ?  451  ARG   B NH1 1 
ATOM   2956 N  NH1 B ARG   B 1 10  ? 48.941 -21.395 12.219  0.59 10.56 ?  451  ARG   B NH1 1 
ATOM   2957 N  NH2 A ARG   B 1 10  ? 54.389 -17.831 10.984  0.41 16.49 ?  451  ARG   B NH2 1 
ATOM   2958 N  NH2 B ARG   B 1 10  ? 50.414 -21.654 13.945  0.59 11.23 ?  451  ARG   B NH2 1 
ATOM   2959 N  N   . MET   B 1 11  ? 49.386 -14.601 14.703  1.00 11.61 ?  452  MET   B N   1 
ATOM   2960 C  CA  . MET   B 1 11  ? 49.366 -14.039 16.046  1.00 10.90 ?  452  MET   B CA  1 
ATOM   2961 C  C   . MET   B 1 11  ? 47.947 -13.807 16.556  1.00 11.48 ?  452  MET   B C   1 
ATOM   2962 O  O   . MET   B 1 11  ? 47.785 -13.508 17.746  1.00 11.58 ?  452  MET   B O   1 
ATOM   2963 C  CB  . MET   B 1 11  ? 50.170 -12.742 16.127  1.00 9.74  ?  452  MET   B CB  1 
ATOM   2964 C  CG  . MET   B 1 11  ? 51.676 -12.959 16.252  1.00 11.30 ?  452  MET   B CG  1 
ATOM   2965 S  SD  . MET   B 1 11  ? 52.662 -11.447 16.139  1.00 10.69 ?  452  MET   B SD  1 
ATOM   2966 C  CE  . MET   B 1 11  ? 52.543 -11.028 14.375  1.00 12.10 ?  452  MET   B CE  1 
ATOM   2967 N  N   . MET   B 1 12  ? 46.928 -13.936 15.697  1.00 10.08 ?  453  MET   B N   1 
ATOM   2968 C  CA  . MET   B 1 12  ? 45.544 -13.892 16.160  1.00 10.61 ?  453  MET   B CA  1 
ATOM   2969 C  C   . MET   B 1 12  ? 45.133 -15.144 16.921  1.00 11.99 ?  453  MET   B C   1 
ATOM   2970 O  O   . MET   B 1 12  ? 44.061 -15.144 17.534  1.00 12.57 ?  453  MET   B O   1 
ATOM   2971 C  CB  . MET   B 1 12  ? 44.594 -13.702 14.974  1.00 12.34 ?  453  MET   B CB  1 
ATOM   2972 C  CG  . MET   B 1 12  ? 44.780 -12.401 14.196  1.00 13.33 ?  453  MET   B CG  1 
ATOM   2973 S  SD  . MET   B 1 12  ? 43.650 -12.278 12.779  1.00 18.27 ?  453  MET   B SD  1 
ATOM   2974 C  CE  . MET   B 1 12  ? 42.076 -12.083 13.599  1.00 19.67 ?  453  MET   B CE  1 
ATOM   2975 N  N   . LEU   B 1 13  ? 45.948 -16.201 16.919  1.00 11.24 ?  454  LEU   B N   1 
ATOM   2976 C  CA  . LEU   B 1 13  ? 45.480 -17.474 17.465  1.00 12.13 ?  454  LEU   B CA  1 
ATOM   2977 C  C   . LEU   B 1 13  ? 45.359 -17.448 18.985  1.00 11.83 ?  454  LEU   B C   1 
ATOM   2978 O  O   . LEU   B 1 13  ? 44.524 -18.161 19.545  1.00 13.29 ?  454  LEU   B O   1 
ATOM   2979 C  CB  . LEU   B 1 13  ? 46.358 -18.626 16.983  1.00 13.01 ?  454  LEU   B CB  1 
ATOM   2980 C  CG  . LEU   B 1 13  ? 46.264 -18.941 15.490  1.00 13.84 ?  454  LEU   B CG  1 
ATOM   2981 C  CD1 . LEU   B 1 13  ? 47.318 -19.974 15.102  1.00 14.73 ?  454  LEU   B CD1 1 
ATOM   2982 C  CD2 . LEU   B 1 13  ? 44.867 -19.411 15.095  1.00 14.70 ?  454  LEU   B CD2 1 
ATOM   2983 N  N   . HIS   B 1 14  ? 46.190 -16.659 19.660  1.00 10.67 ?  455  HIS   B N   1 
ATOM   2984 C  CA  . HIS   B 1 14  ? 46.080 -16.438 21.100  1.00 11.86 ?  455  HIS   B CA  1 
ATOM   2985 C  C   . HIS   B 1 14  ? 44.720 -15.826 21.440  1.00 11.09 ?  455  HIS   B C   1 
ATOM   2986 O  O   . HIS   B 1 14  ? 44.353 -14.773 20.917  1.00 11.39 ?  455  HIS   B O   1 
ATOM   2987 C  CB  . HIS   B 1 14  ? 47.222 -15.491 21.470  1.00 10.70 ?  455  HIS   B CB  1 
ATOM   2988 C  CG  . HIS   B 1 14  ? 47.147 -14.904 22.851  1.00 9.33  ?  455  HIS   B CG  1 
ATOM   2989 N  ND1 . HIS   B 1 14  ? 47.132 -15.670 24.000  1.00 10.42 ?  455  HIS   B ND1 1 
ATOM   2990 C  CD2 . HIS   B 1 14  ? 47.123 -13.612 23.261  1.00 9.62  ?  455  HIS   B CD2 1 
ATOM   2991 C  CE1 . HIS   B 1 14  ? 47.100 -14.876 25.056  1.00 11.02 ?  455  HIS   B CE1 1 
ATOM   2992 N  NE2 . HIS   B 1 14  ? 47.101 -13.622 24.635  1.00 10.71 ?  455  HIS   B NE2 1 
ATOM   2993 N  N   . HIS   B 1 15  ? 43.965 -16.478 22.325  1.00 12.18 ?  456  HIS   B N   1 
ATOM   2994 C  CA  . HIS   B 1 15  ? 42.601 -16.025 22.597  1.00 12.08 ?  456  HIS   B CA  1 
ATOM   2995 C  C   . HIS   B 1 15  ? 42.188 -16.404 24.012  1.00 11.84 ?  456  HIS   B C   1 
ATOM   2996 O  O   . HIS   B 1 15  ? 42.808 -17.248 24.666  1.00 12.46 ?  456  HIS   B O   1 
ATOM   2997 C  CB  . HIS   B 1 15  ? 41.595 -16.596 21.591  1.00 12.87 ?  456  HIS   B CB  1 
ATOM   2998 C  CG  . HIS   B 1 15  ? 41.425 -18.077 21.703  1.00 14.92 ?  456  HIS   B CG  1 
ATOM   2999 N  ND1 . HIS   B 1 15  ? 42.384 -18.969 21.275  1.00 17.87 ?  456  HIS   B ND1 1 
ATOM   3000 C  CD2 . HIS   B 1 15  ? 40.413 -18.822 22.204  1.00 15.76 ?  456  HIS   B CD2 1 
ATOM   3001 C  CE1 . HIS   B 1 15  ? 41.969 -20.202 21.508  1.00 18.20 ?  456  HIS   B CE1 1 
ATOM   3002 N  NE2 . HIS   B 1 15  ? 40.779 -20.141 22.078  1.00 18.90 ?  456  HIS   B NE2 1 
ATOM   3003 N  N   . ASN   B 1 16  ? 41.131 -15.747 24.476  1.00 11.61 ?  457  ASN   B N   1 
ATOM   3004 C  CA  . ASN   B 1 16  ? 40.619 -15.912 25.833  1.00 12.06 ?  457  ASN   B CA  1 
ATOM   3005 C  C   . ASN   B 1 16  ? 39.452 -16.887 25.779  1.00 13.17 ?  457  ASN   B C   1 
ATOM   3006 O  O   . ASN   B 1 16  ? 38.378 -16.542 25.280  1.00 14.78 ?  457  ASN   B O   1 
ATOM   3007 C  CB  . ASN   B 1 16  ? 40.174 -14.563 26.395  1.00 12.79 ?  457  ASN   B CB  1 
ATOM   3008 C  CG  . ASN   B 1 16  ? 39.865 -14.626 27.871  1.00 13.98 ?  457  ASN   B CG  1 
ATOM   3009 O  OD1 . ASN   B 1 16  ? 39.320 -15.610 28.351  1.00 13.78 ?  457  ASN   B OD1 1 
ATOM   3010 N  ND2 . ASN   B 1 16  ? 40.202 -13.571 28.591  1.00 13.45 ?  457  ASN   B ND2 1 
ATOM   3011 N  N   . MET   B 1 17  ? 39.666 -18.086 26.332  1.00 14.66 ?  458  MET   B N   1 
ATOM   3012 C  CA  . MET   B 1 17  ? 38.670 -19.155 26.262  1.00 19.95 ?  458  MET   B CA  1 
ATOM   3013 C  C   . MET   B 1 17  ? 37.408 -18.811 27.050  1.00 17.51 ?  458  MET   B C   1 
ATOM   3014 O  O   . MET   B 1 17  ? 36.299 -19.145 26.620  1.00 19.80 ?  458  MET   B O   1 
ATOM   3015 C  CB  . MET   B 1 17  ? 39.271 -20.465 26.786  1.00 28.55 ?  458  MET   B CB  1 
ATOM   3016 C  CG  . MET   B 1 17  ? 40.524 -20.941 26.054  1.00 40.89 ?  458  MET   B CG  1 
ATOM   3017 S  SD  . MET   B 1 17  ? 41.129 -22.548 26.630  1.00 48.36 ?  458  MET   B SD  1 
ATOM   3018 C  CE  . MET   B 1 17  ? 39.802 -23.041 27.732  1.00 48.87 ?  458  MET   B CE  1 
ATOM   3019 N  N   . TRP   B 1 18  ? 37.551 -18.154 28.204  1.00 15.55 ?  459  TRP   B N   1 
ATOM   3020 C  CA  . TRP   B 1 18  ? 36.403 -17.876 29.060  1.00 18.34 ?  459  TRP   B CA  1 
ATOM   3021 C  C   . TRP   B 1 18  ? 35.682 -16.592 28.686  1.00 20.68 ?  459  TRP   B C   1 
ATOM   3022 O  O   . TRP   B 1 18  ? 34.474 -16.471 28.930  1.00 19.00 ?  459  TRP   B O   1 
ATOM   3023 C  CB  . TRP   B 1 18  ? 36.843 -17.777 30.521  1.00 21.06 ?  459  TRP   B CB  1 
ATOM   3024 C  CG  . TRP   B 1 18  ? 36.753 -19.059 31.260  1.00 24.80 ?  459  TRP   B CG  1 
ATOM   3025 C  CD1 . TRP   B 1 18  ? 37.789 -19.889 31.588  1.00 27.01 ?  459  TRP   B CD1 1 
ATOM   3026 C  CD2 . TRP   B 1 18  ? 35.565 -19.675 31.774  1.00 25.37 ?  459  TRP   B CD2 1 
ATOM   3027 N  NE1 . TRP   B 1 18  ? 37.318 -20.980 32.273  1.00 28.71 ?  459  TRP   B NE1 1 
ATOM   3028 C  CE2 . TRP   B 1 18  ? 35.958 -20.873 32.405  1.00 27.29 ?  459  TRP   B CE2 1 
ATOM   3029 C  CE3 . TRP   B 1 18  ? 34.209 -19.328 31.766  1.00 25.65 ?  459  TRP   B CE3 1 
ATOM   3030 C  CZ2 . TRP   B 1 18  ? 35.043 -21.732 33.018  1.00 27.59 ?  459  TRP   B CZ2 1 
ATOM   3031 C  CZ3 . TRP   B 1 18  ? 33.302 -20.181 32.378  1.00 27.34 ?  459  TRP   B CZ3 1 
ATOM   3032 C  CH2 . TRP   B 1 18  ? 33.725 -21.368 32.993  1.00 27.40 ?  459  TRP   B CH2 1 
ATOM   3033 N  N   . ASP   B 1 19  ? 36.388 -15.626 28.103  1.00 18.65 ?  460  ASP   B N   1 
ATOM   3034 C  CA  . ASP   B 1 19  ? 35.845 -14.292 27.854  1.00 17.37 ?  460  ASP   B CA  1 
ATOM   3035 C  C   . ASP   B 1 19  ? 36.259 -13.906 26.439  1.00 18.24 ?  460  ASP   B C   1 
ATOM   3036 O  O   . ASP   B 1 19  ? 37.286 -13.249 26.243  1.00 16.83 ?  460  ASP   B O   1 
ATOM   3037 C  CB  . ASP   B 1 19  ? 36.375 -13.310 28.885  1.00 16.95 ?  460  ASP   B CB  1 
ATOM   3038 C  CG  . ASP   B 1 19  ? 35.851 -11.904 28.672  1.00 17.54 ?  460  ASP   B CG  1 
ATOM   3039 O  OD1 . ASP   B 1 19  ? 34.881 -11.731 27.905  1.00 19.56 ?  460  ASP   B OD1 1 
ATOM   3040 O  OD2 . ASP   B 1 19  ? 36.435 -10.978 29.266  1.00 19.61 -1 460  ASP   B OD2 1 
ATOM   3041 N  N   . SER   B 1 20  ? 35.452 -14.308 25.455  1.00 20.52 ?  461  SER   B N   1 
ATOM   3042 C  CA  . SER   B 1 20  ? 35.796 -14.044 24.063  1.00 21.41 ?  461  SER   B CA  1 
ATOM   3043 C  C   . SER   B 1 20  ? 35.737 -12.564 23.704  1.00 19.59 ?  461  SER   B C   1 
ATOM   3044 O  O   . SER   B 1 20  ? 36.240 -12.183 22.643  1.00 20.94 ?  461  SER   B O   1 
ATOM   3045 C  CB  . SER   B 1 20  ? 34.885 -14.852 23.136  1.00 25.72 ?  461  SER   B CB  1 
ATOM   3046 O  OG  . SER   B 1 20  ? 33.541 -14.399 23.217  1.00 28.98 ?  461  SER   B OG  1 
ATOM   3047 N  N   . HIS   B 1 21  ? 35.150 -11.723 24.553  1.00 18.01 ?  462  HIS   B N   1 
ATOM   3048 C  CA  . HIS   B 1 21  ? 35.112 -10.285 24.325  1.00 17.71 ?  462  HIS   B CA  1 
ATOM   3049 C  C   . HIS   B 1 21  ? 36.148 -9.534  25.147  1.00 16.87 ?  462  HIS   B C   1 
ATOM   3050 O  O   . HIS   B 1 21  ? 36.086 -8.302  25.225  1.00 18.65 ?  462  HIS   B O   1 
ATOM   3051 C  CB  . HIS   B 1 21  ? 33.719 -9.732  24.611  1.00 21.78 ?  462  HIS   B CB  1 
ATOM   3052 C  CG  . HIS   B 1 21  ? 32.670 -10.240 23.674  1.00 26.01 ?  462  HIS   B CG  1 
ATOM   3053 N  ND1 . HIS   B 1 21  ? 31.923 -11.369 23.935  1.00 29.41 ?  462  HIS   B ND1 1 
ATOM   3054 C  CD2 . HIS   B 1 21  ? 32.254 -9.783  22.470  1.00 28.51 ?  462  HIS   B CD2 1 
ATOM   3055 C  CE1 . HIS   B 1 21  ? 31.083 -11.577 22.937  1.00 29.62 ?  462  HIS   B CE1 1 
ATOM   3056 N  NE2 . HIS   B 1 21  ? 31.266 -10.631 22.034  1.00 30.30 ?  462  HIS   B NE2 1 
ATOM   3057 N  N   . HIS   B 1 22  ? 37.090 -10.243 25.758  1.00 13.15 ?  463  HIS   B N   1 
ATOM   3058 C  CA  . HIS   B 1 22  ? 38.169 -9.589  26.473  1.00 12.98 ?  463  HIS   B CA  1 
ATOM   3059 C  C   . HIS   B 1 22  ? 38.878 -8.608  25.537  1.00 12.95 ?  463  HIS   B C   1 
ATOM   3060 O  O   . HIS   B 1 22  ? 39.104 -8.933  24.364  1.00 13.12 ?  463  HIS   B O   1 
ATOM   3061 C  CB  . HIS   B 1 22  ? 39.154 -10.659 26.935  1.00 12.65 ?  463  HIS   B CB  1 
ATOM   3062 C  CG  . HIS   B 1 22  ? 40.290 -10.123 27.732  1.00 13.85 ?  463  HIS   B CG  1 
ATOM   3063 N  ND1 . HIS   B 1 22  ? 41.304 -9.378  27.169  1.00 14.18 ?  463  HIS   B ND1 1 
ATOM   3064 C  CD2 . HIS   B 1 22  ? 40.576 -10.225 29.050  1.00 14.47 ?  463  HIS   B CD2 1 
ATOM   3065 C  CE1 . HIS   B 1 22  ? 42.161 -9.035  28.113  1.00 13.70 ?  463  HIS   B CE1 1 
ATOM   3066 N  NE2 . HIS   B 1 22  ? 41.742 -9.540  29.264  1.00 14.64 ?  463  HIS   B NE2 1 
ATOM   3067 N  N   . PRO   B 1 23  ? 39.273 -7.424  26.023  1.00 13.02 ?  464  PRO   B N   1 
ATOM   3068 C  CA  . PRO   B 1 23  ? 39.715 -6.358  25.099  1.00 13.13 ?  464  PRO   B CA  1 
ATOM   3069 C  C   . PRO   B 1 23  ? 40.998 -6.648  24.330  1.00 11.51 ?  464  PRO   B C   1 
ATOM   3070 O  O   . PRO   B 1 23  ? 41.209 -6.030  23.274  1.00 11.29 ?  464  PRO   B O   1 
ATOM   3071 C  CB  . PRO   B 1 23  ? 39.868 -5.136  26.015  1.00 15.56 ?  464  PRO   B CB  1 
ATOM   3072 C  CG  . PRO   B 1 23  ? 40.077 -5.727  27.395  1.00 16.47 ?  464  PRO   B CG  1 
ATOM   3073 C  CD  . PRO   B 1 23  ? 39.178 -6.939  27.410  1.00 15.68 ?  464  PRO   B CD  1 
ATOM   3074 N  N   . GLU   B 1 24  ? 41.865 -7.547  24.805  1.00 11.41 ?  465  GLU   B N   1 
ATOM   3075 C  CA  . GLU   B 1 24  ? 43.087 -7.896  24.072  1.00 10.43 ?  465  GLU   B CA  1 
ATOM   3076 C  C   . GLU   B 1 24  ? 42.730 -8.928  22.999  1.00 11.26 ?  465  GLU   B C   1 
ATOM   3077 O  O   . GLU   B 1 24  ? 43.019 -10.125 23.093  1.00 11.53 ?  465  GLU   B O   1 
ATOM   3078 C  CB  . GLU   B 1 24  ? 44.172 -8.392  25.023  1.00 11.03 ?  465  GLU   B CB  1 
ATOM   3079 C  CG  . GLU   B 1 24  ? 45.600 -8.128  24.522  1.00 11.25 ?  465  GLU   B CG  1 
ATOM   3080 C  CD  . GLU   B 1 24  ? 45.974 -9.003  23.345  1.00 12.51 ?  465  GLU   B CD  1 
ATOM   3081 O  OE1 . GLU   B 1 24  ? 45.709 -8.573  22.196  1.00 10.78 ?  465  GLU   B OE1 1 
ATOM   3082 O  OE2 . GLU   B 1 24  ? 46.521 -10.099 23.551  1.00 10.55 -1 465  GLU   B OE2 1 
ATOM   3083 N  N   . LEU   B 1 25  ? 42.042 -8.436  21.970  1.00 11.26 ?  466  LEU   B N   1 
ATOM   3084 C  CA  . LEU   B 1 25  ? 41.360 -9.227  20.952  1.00 11.40 ?  466  LEU   B CA  1 
ATOM   3085 C  C   . LEU   B 1 25  ? 42.308 -9.618  19.821  1.00 11.60 ?  466  LEU   B C   1 
ATOM   3086 O  O   . LEU   B 1 25  ? 43.159 -8.815  19.411  1.00 11.76 ?  466  LEU   B O   1 
ATOM   3087 C  CB  . LEU   B 1 25  ? 40.227 -8.419  20.343  1.00 12.86 ?  466  LEU   B CB  1 
ATOM   3088 C  CG  . LEU   B 1 25  ? 38.951 -8.226  21.141  1.00 13.67 ?  466  LEU   B CG  1 
ATOM   3089 C  CD1 . LEU   B 1 25  ? 38.084 -7.197  20.434  1.00 16.89 ?  466  LEU   B CD1 1 
ATOM   3090 C  CD2 . LEU   B 1 25  ? 38.242 -9.561  21.268  1.00 14.80 ?  466  LEU   B CD2 1 
ATOM   3091 N  N   . PRO   B 1 26  ? 42.114 -10.826 19.290  1.00 12.17 ?  467  PRO   B N   1 
ATOM   3092 C  CA  . PRO   B 1 26  ? 42.820 -11.209 18.060  1.00 12.11 ?  467  PRO   B CA  1 
ATOM   3093 C  C   . PRO   B 1 26  ? 42.737 -10.168 16.961  1.00 11.40 ?  467  PRO   B C   1 
ATOM   3094 O  O   . PRO   B 1 26  ? 43.736 -9.897  16.273  1.00 12.50 ?  467  PRO   B O   1 
ATOM   3095 C  CB  . PRO   B 1 26  ? 42.131 -12.521 17.672  1.00 13.70 ?  467  PRO   B CB  1 
ATOM   3096 C  CG  . PRO   B 1 26  ? 41.700 -13.107 18.971  1.00 12.10 ?  467  PRO   B CG  1 
ATOM   3097 C  CD  . PRO   B 1 26  ? 41.331 -11.942 19.852  1.00 11.60 ?  467  PRO   B CD  1 
ATOM   3098 N  N   . GLN   B 1 27  ? 41.571 -9.539  16.805  1.00 10.53 ?  468  GLN   B N   1 
ATOM   3099 C  CA  . GLN   B 1 27  ? 41.372 -8.608  15.708  1.00 13.26 ?  468  GLN   B CA  1 
ATOM   3100 C  C   . GLN   B 1 27  ? 42.080 -7.270  15.904  1.00 10.66 ?  468  GLN   B C   1 
ATOM   3101 O  O   . GLN   B 1 27  ? 42.045 -6.459  14.978  1.00 10.86 ?  468  GLN   B O   1 
ATOM   3102 C  CB  . GLN   B 1 27  ? 39.882 -8.428  15.382  1.00 17.86 ?  468  GLN   B CB  1 
ATOM   3103 C  CG  . GLN   B 1 27  ? 38.989 -8.070  16.560  1.00 20.97 ?  468  GLN   B CG  1 
ATOM   3104 C  CD  . GLN   B 1 27  ? 38.335 -9.283  17.232  1.00 23.00 ?  468  GLN   B CD  1 
ATOM   3105 O  OE1 . GLN   B 1 27  ? 39.007 -10.259 17.592  1.00 17.50 ?  468  GLN   B OE1 1 
ATOM   3106 N  NE2 . GLN   B 1 27  ? 37.008 -9.218  17.410  1.00 24.41 ?  468  GLN   B NE2 1 
ATOM   3107 N  N   . ARG   B 1 28  ? 42.755 -7.019  17.030  1.00 10.65 ?  469  ARG   B N   1 
ATOM   3108 C  CA  . ARG   B 1 28  ? 43.552 -5.803  17.134  1.00 10.22 ?  469  ARG   B CA  1 
ATOM   3109 C  C   . ARG   B 1 28  ? 44.566 -5.721  16.000  1.00 10.38 ?  469  ARG   B C   1 
ATOM   3110 O  O   . ARG   B 1 28  ? 44.721 -4.670  15.365  1.00 11.02 ?  469  ARG   B O   1 
ATOM   3111 C  CB  . ARG   B 1 28  ? 44.267 -5.764  18.483  1.00 9.92  ?  469  ARG   B CB  1 
ATOM   3112 C  CG  . ARG   B 1 28  ? 43.325 -5.624  19.668  1.00 10.33 ?  469  ARG   B CG  1 
ATOM   3113 C  CD  . ARG   B 1 28  ? 44.042 -5.755  21.012  1.00 11.10 ?  469  ARG   B CD  1 
ATOM   3114 N  NE  . ARG   B 1 28  ? 45.019 -4.690  21.173  1.00 10.68 ?  469  ARG   B NE  1 
ATOM   3115 C  CZ  . ARG   B 1 28  ? 46.339 -4.869  21.233  1.00 10.43 ?  469  ARG   B CZ  1 
ATOM   3116 N  NH1 . ARG   B 1 28  ? 46.884 -6.088  21.215  1.00 11.55 ?  469  ARG   B NH1 1 
ATOM   3117 N  NH2 . ARG   B 1 28  ? 47.118 -3.800  21.291  1.00 12.05 ?  469  ARG   B NH2 1 
ATOM   3118 N  N   . ILE   B 1 29  ? 45.269 -6.825  15.732  1.00 9.74  ?  470  ILE   B N   1 
ATOM   3119 C  CA  . ILE   B 1 29  ? 46.333 -6.767  14.734  1.00 9.47  ?  470  ILE   B CA  1 
ATOM   3120 C  C   . ILE   B 1 29  ? 45.775 -6.825  13.317  1.00 10.73 ?  470  ILE   B C   1 
ATOM   3121 O  O   . ILE   B 1 29  ? 46.296 -6.164  12.414  1.00 11.60 ?  470  ILE   B O   1 
ATOM   3122 C  CB  . ILE   B 1 29  ? 47.442 -7.812  14.973  1.00 9.92  ?  470  ILE   B CB  1 
ATOM   3123 C  CG1 . ILE   B 1 29  ? 46.885 -9.245  14.968  1.00 11.19 ?  470  ILE   B CG1 1 
ATOM   3124 C  CG2 . ILE   B 1 29  ? 48.243 -7.484  16.244  1.00 10.17 ?  470  ILE   B CG2 1 
ATOM   3125 C  CD1 . ILE   B 1 29  ? 47.966 -10.298 14.878  1.00 11.58 ?  470  ILE   B CD1 1 
ATOM   3126 N  N   . SER   B 1 30  ? 44.733 -7.626  13.078  1.00 10.41 ?  471  SER   B N   1 
ATOM   3127 C  CA  . SER   B 1 30  ? 44.174 -7.642  11.725  1.00 9.71  ?  471  SER   B CA  1 
ATOM   3128 C  C   . SER   B 1 30  ? 43.545 -6.305  11.366  1.00 10.88 ?  471  SER   B C   1 
ATOM   3129 O  O   . SER   B 1 30  ? 43.596 -5.898  10.197  1.00 12.05 ?  471  SER   B O   1 
ATOM   3130 C  CB  . SER   B 1 30  ? 43.159 -8.772  11.542  1.00 13.44 ?  471  SER   B CB  1 
ATOM   3131 O  OG  . SER   B 1 30  ? 42.142 -8.739  12.501  1.00 14.93 ?  471  SER   B OG  1 
ATOM   3132 N  N   . ARG   B 1 31  ? 42.939 -5.615  12.338  1.00 11.81 ?  472  ARG   B N   1 
ATOM   3133 C  CA  . ARG   B 1 31  ? 42.356 -4.309  12.042  1.00 10.97 ?  472  ARG   B CA  1 
ATOM   3134 C  C   . ARG   B 1 31  ? 43.431 -3.287  11.704  1.00 8.72  ?  472  ARG   B C   1 
ATOM   3135 O  O   . ARG   B 1 31  ? 43.276 -2.498  10.758  1.00 9.91  ?  472  ARG   B O   1 
ATOM   3136 C  CB  . ARG   B 1 31  ? 41.493 -3.825  13.201  1.00 11.44 ?  472  ARG   B CB  1 
ATOM   3137 C  CG  . ARG   B 1 31  ? 40.159 -4.553  13.301  1.00 10.87 ?  472  ARG   B CG  1 
ATOM   3138 C  CD  . ARG   B 1 31  ? 39.217 -4.113  12.170  1.00 11.98 ?  472  ARG   B CD  1 
ATOM   3139 N  NE  . ARG   B 1 31  ? 38.945 -2.680  12.261  1.00 10.33 ?  472  ARG   B NE  1 
ATOM   3140 C  CZ  . ARG   B 1 31  ? 37.995 -2.132  13.014  1.00 12.11 ?  472  ARG   B CZ  1 
ATOM   3141 N  NH1 . ARG   B 1 31  ? 37.203 -2.902  13.735  1.00 11.52 ?  472  ARG   B NH1 1 
ATOM   3142 N  NH2 . ARG   B 1 31  ? 37.839 -0.814  13.049  1.00 14.31 ?  472  ARG   B NH2 1 
ATOM   3143 N  N   . ILE   B 1 32  ? 44.538 -3.282  12.450  1.00 10.31 ?  473  ILE   B N   1 
ATOM   3144 C  CA  . ILE   B 1 32  ? 45.622 -2.376  12.102  1.00 10.02 ?  473  ILE   B CA  1 
ATOM   3145 C  C   . ILE   B 1 32  ? 46.154 -2.696  10.714  1.00 9.54  ?  473  ILE   B C   1 
ATOM   3146 O  O   . ILE   B 1 32  ? 46.387 -1.795  9.900   1.00 10.57 ?  473  ILE   B O   1 
ATOM   3147 C  CB  . ILE   B 1 32  ? 46.735 -2.419  13.162  1.00 10.48 ?  473  ILE   B CB  1 
ATOM   3148 C  CG1 . ILE   B 1 32  ? 46.236 -1.892  14.514  1.00 9.48  ?  473  ILE   B CG1 1 
ATOM   3149 C  CG2 . ILE   B 1 32  ? 47.924 -1.580  12.673  1.00 11.47 ?  473  ILE   B CG2 1 
ATOM   3150 C  CD1 . ILE   B 1 32  ? 47.131 -2.287  15.709  1.00 9.65  ?  473  ILE   B CD1 1 
ATOM   3151 N  N   . PHE   B 1 33  ? 46.391 -3.981  10.441  1.00 10.05 ?  474  PHE   B N   1 
ATOM   3152 C  CA  . PHE   B 1 33  ? 46.889 -4.384  9.128   1.00 10.24 ?  474  PHE   B CA  1 
ATOM   3153 C  C   . PHE   B 1 33  ? 45.926 -3.938  8.036   1.00 11.03 ?  474  PHE   B C   1 
ATOM   3154 O  O   . PHE   B 1 33  ? 46.348 -3.365  7.019   1.00 11.34 ?  474  PHE   B O   1 
ATOM   3155 C  CB  . PHE   B 1 33  ? 47.099 -5.895  9.092   1.00 11.06 ?  474  PHE   B CB  1 
ATOM   3156 C  CG  . PHE   B 1 33  ? 47.729 -6.408  7.812   1.00 13.07 ?  474  PHE   B CG  1 
ATOM   3157 C  CD1 . PHE   B 1 33  ? 49.079 -6.195  7.542   1.00 12.08 ?  474  PHE   B CD1 1 
ATOM   3158 C  CD2 . PHE   B 1 33  ? 46.975 -7.138  6.906   1.00 12.19 ?  474  PHE   B CD2 1 
ATOM   3159 C  CE1 . PHE   B 1 33  ? 49.665 -6.689  6.374   1.00 13.72 ?  474  PHE   B CE1 1 
ATOM   3160 C  CE2 . PHE   B 1 33  ? 47.555 -7.622  5.744   1.00 14.08 ?  474  PHE   B CE2 1 
ATOM   3161 C  CZ  . PHE   B 1 33  ? 48.895 -7.392  5.485   1.00 15.22 ?  474  PHE   B CZ  1 
ATOM   3162 N  N   . SER   B 1 34  ? 44.621 -4.144  8.261   1.00 11.49 ?  475  SER   B N   1 
ATOM   3163 C  CA  . SER   B 1 34  ? 43.627 -3.796  7.246   1.00 11.58 ?  475  SER   B CA  1 
ATOM   3164 C  C   . SER   B 1 34  ? 43.636 -2.296  6.970   1.00 11.36 ?  475  SER   B C   1 
ATOM   3165 O  O   . SER   B 1 34  ? 43.538 -1.876  5.810   1.00 12.87 ?  475  SER   B O   1 
ATOM   3166 C  CB  . SER   B 1 34  ? 42.228 -4.277  7.660   1.00 11.28 ?  475  SER   B CB  1 
ATOM   3167 O  OG  . SER   B 1 34  ? 41.211 -3.550  6.976   1.00 13.46 ?  475  SER   B OG  1 
ATOM   3168 N  N   . ARG   B 1 35  ? 43.793 -1.469  8.009   1.00 11.55 ?  476  ARG   B N   1 
ATOM   3169 C  CA  . ARG   B 1 35  ? 43.820 -0.027  7.788   1.00 9.93  ?  476  ARG   B CA  1 
ATOM   3170 C  C   . ARG   B 1 35  ? 45.028 0.380   6.949   1.00 9.75  ?  476  ARG   B C   1 
ATOM   3171 O  O   . ARG   B 1 35  ? 44.922 1.270   6.098   1.00 10.19 ?  476  ARG   B O   1 
ATOM   3172 C  CB  . ARG   B 1 35  ? 43.775 0.717   9.131   1.00 10.10 ?  476  ARG   B CB  1 
ATOM   3173 C  CG  . ARG   B 1 35  ? 43.567 2.219   9.012   1.00 11.65 ?  476  ARG   B CG  1 
ATOM   3174 C  CD  . ARG   B 1 35  ? 42.154 2.581   8.558   1.00 13.49 ?  476  ARG   B CD  1 
ATOM   3175 N  NE  . ARG   B 1 35  ? 41.975 4.034   8.550   1.00 14.71 ?  476  ARG   B NE  1 
ATOM   3176 C  CZ  . ARG   B 1 35  ? 41.421 4.716   7.554   1.00 15.32 ?  476  ARG   B CZ  1 
ATOM   3177 N  NH1 . ARG   B 1 35  ? 40.956 4.076   6.487   1.00 16.32 ?  476  ARG   B NH1 1 
ATOM   3178 N  NH2 . ARG   B 1 35  ? 41.328 6.039   7.626   1.00 13.86 ?  476  ARG   B NH2 1 
ATOM   3179 N  N   . HIS   B 1 36  ? 46.181 -0.263  7.174   1.00 10.31 ?  477  HIS   B N   1 
ATOM   3180 C  CA  . HIS   B 1 36  ? 47.357 0.011   6.353   1.00 12.21 ?  477  HIS   B CA  1 
ATOM   3181 C  C   . HIS   B 1 36  ? 47.085 -0.308  4.886   1.00 13.54 ?  477  HIS   B C   1 
ATOM   3182 O  O   . HIS   B 1 36  ? 47.508 0.440   3.992   1.00 14.10 ?  477  HIS   B O   1 
ATOM   3183 C  CB  . HIS   B 1 36  ? 48.554 -0.815  6.839   1.00 10.80 ?  477  HIS   B CB  1 
ATOM   3184 C  CG  . HIS   B 1 36  ? 49.263 -0.248  8.036   1.00 11.85 ?  477  HIS   B CG  1 
ATOM   3185 N  ND1 . HIS   B 1 36  ? 48.766 -0.324  9.321   1.00 12.22 ?  477  HIS   B ND1 1 
ATOM   3186 C  CD2 . HIS   B 1 36  ? 50.454 0.388   8.128   1.00 13.13 ?  477  HIS   B CD2 1 
ATOM   3187 C  CE1 . HIS   B 1 36  ? 49.623 0.250   10.153  1.00 11.72 ?  477  HIS   B CE1 1 
ATOM   3188 N  NE2 . HIS   B 1 36  ? 50.655 0.690   9.452   1.00 13.04 ?  477  HIS   B NE2 1 
ATOM   3189 N  N   . GLU   B 1 37  ? 46.420 -1.439  4.624   1.00 12.21 ?  478  GLU   B N   1 
ATOM   3190 C  CA  . GLU   B 1 37  ? 46.050 -1.815  3.258   1.00 13.01 ?  478  GLU   B CA  1 
ATOM   3191 C  C   . GLU   B 1 37  ? 45.096 -0.796  2.658   1.00 13.75 ?  478  GLU   B C   1 
ATOM   3192 O  O   . GLU   B 1 37  ? 45.276 -0.337  1.525   1.00 14.11 ?  478  GLU   B O   1 
ATOM   3193 C  CB  . GLU   B 1 37  ? 45.369 -3.183  3.292   1.00 16.99 ?  478  GLU   B CB  1 
ATOM   3194 C  CG  . GLU   B 1 37  ? 45.324 -3.907  1.954   1.00 25.15 ?  478  GLU   B CG  1 
ATOM   3195 C  CD  . GLU   B 1 37  ? 45.164 -5.405  2.136   1.00 35.82 ?  478  GLU   B CD  1 
ATOM   3196 O  OE1 . GLU   B 1 37  ? 44.724 -5.826  3.234   1.00 40.88 ?  478  GLU   B OE1 1 
ATOM   3197 O  OE2 . GLU   B 1 37  ? 45.476 -6.155  1.191   1.00 39.48 -1 478  GLU   B OE2 1 
ATOM   3198 N  N   . GLU   B 1 38  ? 44.069 -0.436  3.422   1.00 12.27 ?  479  GLU   B N   1 
ATOM   3199 C  CA  . GLU   B 1 38  ? 43.006 0.446   2.963   1.00 13.29 ?  479  GLU   B CA  1 
ATOM   3200 C  C   . GLU   B 1 38  ? 43.537 1.825   2.597   1.00 13.68 ?  479  GLU   B C   1 
ATOM   3201 O  O   . GLU   B 1 38  ? 43.067 2.446   1.634   1.00 14.56 ?  479  GLU   B O   1 
ATOM   3202 C  CB  . GLU   B 1 38  ? 42.037 0.556   4.131   1.00 14.29 ?  479  GLU   B CB  1 
ATOM   3203 C  CG  . GLU   B 1 38  ? 40.738 1.194   3.917   1.00 18.18 ?  479  GLU   B CG  1 
ATOM   3204 C  CD  . GLU   B 1 38  ? 39.871 0.952   5.126   1.00 15.76 ?  479  GLU   B CD  1 
ATOM   3205 O  OE1 . GLU   B 1 38  ? 40.206 1.464   6.221   1.00 15.50 ?  479  GLU   B OE1 1 
ATOM   3206 O  OE2 . GLU   B 1 38  ? 38.898 0.203   4.998   1.00 16.98 -1 479  GLU   B OE2 1 
ATOM   3207 N  N   . LEU   B 1 39  ? 44.518 2.316   3.347   1.00 13.11 ?  480  LEU   B N   1 
ATOM   3208 C  CA  . LEU   B 1 39  ? 45.150 3.609   3.115   1.00 12.40 ?  480  LEU   B CA  1 
ATOM   3209 C  C   . LEU   B 1 39  ? 46.289 3.545   2.108   1.00 15.07 ?  480  LEU   B C   1 
ATOM   3210 O  O   . LEU   B 1 39  ? 46.960 4.565   1.888   1.00 17.15 ?  480  LEU   B O   1 
ATOM   3211 C  CB  . LEU   B 1 39  ? 45.696 4.168   4.435   1.00 12.09 ?  480  LEU   B CB  1 
ATOM   3212 C  CG  . LEU   B 1 39  ? 44.641 4.627   5.433   1.00 13.16 ?  480  LEU   B CG  1 
ATOM   3213 C  CD1 . LEU   B 1 39  ? 45.290 4.920   6.783   1.00 13.07 ?  480  LEU   B CD1 1 
ATOM   3214 C  CD2 . LEU   B 1 39  ? 43.918 5.854   4.876   1.00 16.47 ?  480  LEU   B CD2 1 
ATOM   3215 N  N   . ARG   B 1 40  ? 46.537 2.374   1.524   1.00 14.08 ?  481  ARG   B N   1 
ATOM   3216 C  CA  . ARG   B 1 40  ? 47.611 2.144   0.555   1.00 15.44 ?  481  ARG   B CA  1 
ATOM   3217 C  C   . ARG   B 1 40  ? 49.001 2.337   1.144   1.00 16.79 ?  481  ARG   B C   1 
ATOM   3218 O  O   . ARG   B 1 40  ? 49.971 2.548   0.407   1.00 20.13 ?  481  ARG   B O   1 
ATOM   3219 C  CB  . ARG   B 1 40  ? 47.418 2.937   -0.742  1.00 18.34 ?  481  ARG   B CB  1 
ATOM   3220 C  CG  . ARG   B 1 40  ? 46.105 2.594   -1.420  1.00 21.57 ?  481  ARG   B CG  1 
ATOM   3221 C  CD  . ARG   B 1 40  ? 46.006 3.248   -2.779  1.00 26.29 ?  481  ARG   B CD  1 
ATOM   3222 N  NE  . ARG   B 1 40  ? 44.671 3.120   -3.349  1.00 30.54 ?  481  ARG   B NE  1 
ATOM   3223 C  CZ  . ARG   B 1 40  ? 44.356 3.508   -4.580  1.00 33.35 ?  481  ARG   B CZ  1 
ATOM   3224 N  NH1 . ARG   B 1 40  ? 45.282 4.049   -5.361  1.00 34.96 ?  481  ARG   B NH1 1 
ATOM   3225 N  NH2 . ARG   B 1 40  ? 43.118 3.358   -5.028  1.00 35.34 ?  481  ARG   B NH2 1 
ATOM   3226 N  N   . LEU   B 1 41  ? 49.107 2.239   2.470   1.00 13.06 ?  482  LEU   B N   1 
ATOM   3227 C  CA  . LEU   B 1 41  ? 50.395 2.293   3.150   1.00 13.33 ?  482  LEU   B CA  1 
ATOM   3228 C  C   . LEU   B 1 41  ? 51.152 0.971   3.050   1.00 13.21 ?  482  LEU   B C   1 
ATOM   3229 O  O   . LEU   B 1 41  ? 52.382 0.980   2.960   1.00 14.00 ?  482  LEU   B O   1 
ATOM   3230 C  CB  . LEU   B 1 41  ? 50.191 2.671   4.623   1.00 12.93 ?  482  LEU   B CB  1 
ATOM   3231 C  CG  . LEU   B 1 41  ? 49.586 4.057   4.862   1.00 13.69 ?  482  LEU   B CG  1 
ATOM   3232 C  CD1 . LEU   B 1 41  ? 49.227 4.240   6.323   1.00 15.14 ?  482  LEU   B CD1 1 
ATOM   3233 C  CD2 . LEU   B 1 41  ? 50.551 5.146   4.457   1.00 16.11 ?  482  LEU   B CD2 1 
ATOM   3234 N  N   . LEU   B 1 42  ? 50.446 -0.162  3.059   1.00 14.06 ?  483  LEU   B N   1 
ATOM   3235 C  CA  . LEU   B 1 42  ? 51.107 -1.464  3.057   1.00 15.41 ?  483  LEU   B CA  1 
ATOM   3236 C  C   . LEU   B 1 42  ? 51.977 -1.634  1.821   1.00 15.31 ?  483  LEU   B C   1 
ATOM   3237 O  O   . LEU   B 1 42  ? 53.116 -2.105  1.910   1.00 15.11 ?  483  LEU   B O   1 
ATOM   3238 C  CB  . LEU   B 1 42  ? 50.058 -2.574  3.111   1.00 15.71 ?  483  LEU   B CB  1 
ATOM   3239 C  CG  . LEU   B 1 42  ? 50.538 -4.026  3.011   1.00 16.06 ?  483  LEU   B CG  1 
ATOM   3240 C  CD1 . LEU   B 1 42  ? 51.511 -4.376  4.145   1.00 17.65 ?  483  LEU   B CD1 1 
ATOM   3241 C  CD2 . LEU   B 1 42  ? 49.335 -4.965  3.048   1.00 17.11 ?  483  LEU   B CD2 1 
ATOM   3242 N  N   . SER   B 1 43  ? 51.457 -1.251  0.653   1.00 19.01 ?  484  SER   B N   1 
ATOM   3243 C  CA  . SER   B 1 43  ? 52.200 -1.417  -0.591  1.00 19.67 ?  484  SER   B CA  1 
ATOM   3244 C  C   . SER   B 1 43  ? 53.384 -0.468  -0.710  1.00 18.22 ?  484  SER   B C   1 
ATOM   3245 O  O   . SER   B 1 43  ? 54.209 -0.653  -1.611  1.00 21.89 ?  484  SER   B O   1 
ATOM   3246 C  CB  . SER   B 1 43  ? 51.269 -1.252  -1.795  1.00 22.73 ?  484  SER   B CB  1 
ATOM   3247 O  OG  . SER   B 1 43  ? 50.653 0.025   -1.802  1.00 24.80 ?  484  SER   B OG  1 
ATOM   3248 N  N   . ARG   B 1 44  ? 53.484 0.541   0.157   1.00 13.90 ?  485  ARG   B N   1 
ATOM   3249 C  CA  . ARG   B 1 44  ? 54.640 1.422   0.194   1.00 15.31 ?  485  ARG   B CA  1 
ATOM   3250 C  C   . ARG   B 1 44  ? 55.729 0.899   1.119   1.00 15.17 ?  485  ARG   B C   1 
ATOM   3251 O  O   . ARG   B 1 44  ? 56.828 1.466   1.147   1.00 15.30 ?  485  ARG   B O   1 
ATOM   3252 C  CB  . ARG   B 1 44  ? 54.214 2.825   0.641   1.00 14.86 ?  485  ARG   B CB  1 
ATOM   3253 C  CG  . ARG   B 1 44  ? 53.178 3.473   -0.275  1.00 14.21 ?  485  ARG   B CG  1 
ATOM   3254 C  CD  . ARG   B 1 44  ? 52.666 4.795   0.293   1.00 17.05 ?  485  ARG   B CD  1 
ATOM   3255 N  NE  . ARG   B 1 44  ? 53.735 5.770   0.512   1.00 17.72 ?  485  ARG   B NE  1 
ATOM   3256 C  CZ  . ARG   B 1 44  ? 53.621 6.840   1.296   1.00 17.04 ?  485  ARG   B CZ  1 
ATOM   3257 N  NH1 . ARG   B 1 44  ? 52.485 7.068   1.949   1.00 16.66 ?  485  ARG   B NH1 1 
ATOM   3258 N  NH2 . ARG   B 1 44  ? 54.646 7.672   1.440   1.00 17.35 ?  485  ARG   B NH2 1 
ATOM   3259 N  N   . CYS   B 1 45  ? 55.450 -0.167  1.871   1.00 13.88 ?  486  CYS   B N   1 
ATOM   3260 C  CA  . CYS   B 1 45  ? 56.406 -0.741  2.800   1.00 14.32 ?  486  CYS   B CA  1 
ATOM   3261 C  C   . CYS   B 1 45  ? 57.004 -2.008  2.206   1.00 14.61 ?  486  CYS   B C   1 
ATOM   3262 O  O   . CYS   B 1 45  ? 56.417 -2.656  1.333   1.00 17.39 ?  486  CYS   B O   1 
ATOM   3263 C  CB  . CYS   B 1 45  ? 55.695 -1.107  4.109   1.00 13.67 ?  486  CYS   B CB  1 
ATOM   3264 S  SG  . CYS   B 1 45  ? 55.129 0.283   5.078   1.00 15.91 ?  486  CYS   B SG  1 
ATOM   3265 N  N   . HIS   B 1 46  ? 58.187 -2.359  2.687   1.00 13.74 ?  487  HIS   B N   1 
ATOM   3266 C  CA  . HIS   B 1 46  ? 58.754 -3.667  2.404   1.00 13.24 ?  487  HIS   B CA  1 
ATOM   3267 C  C   . HIS   B 1 46  ? 58.328 -4.653  3.487   1.00 11.45 ?  487  HIS   B C   1 
ATOM   3268 O  O   . HIS   B 1 46  ? 58.525 -4.403  4.683   1.00 14.33 ?  487  HIS   B O   1 
ATOM   3269 C  CB  . HIS   B 1 46  ? 60.275 -3.608  2.344   1.00 15.47 ?  487  HIS   B CB  1 
ATOM   3270 C  CG  . HIS   B 1 46  ? 60.904 -4.954  2.215   1.00 16.88 ?  487  HIS   B CG  1 
ATOM   3271 N  ND1 . HIS   B 1 46  ? 60.717 -5.754  1.105   1.00 17.39 ?  487  HIS   B ND1 1 
ATOM   3272 C  CD2 . HIS   B 1 46  ? 61.665 -5.670  3.075   1.00 18.86 ?  487  HIS   B CD2 1 
ATOM   3273 C  CE1 . HIS   B 1 46  ? 61.367 -6.891  1.275   1.00 19.92 ?  487  HIS   B CE1 1 
ATOM   3274 N  NE2 . HIS   B 1 46  ? 61.951 -6.865  2.459   1.00 21.05 ?  487  HIS   B NE2 1 
ATOM   3275 N  N   . ARG   B 1 47  ? 57.737 -5.772  3.073   1.00 11.82 ?  488  ARG   B N   1 
ATOM   3276 C  CA  . ARG   B 1 47  ? 57.237 -6.753  4.023   1.00 13.66 ?  488  ARG   B CA  1 
ATOM   3277 C  C   . ARG   B 1 47  ? 58.416 -7.542  4.581   1.00 12.94 ?  488  ARG   B C   1 
ATOM   3278 O  O   . ARG   B 1 47  ? 59.142 -8.203  3.827   1.00 15.87 ?  488  ARG   B O   1 
ATOM   3279 C  CB  . ARG   B 1 47  ? 56.237 -7.671  3.328   1.00 14.83 ?  488  ARG   B CB  1 
ATOM   3280 C  CG  . ARG   B 1 47  ? 55.411 -8.507  4.251   1.00 16.97 ?  488  ARG   B CG  1 
ATOM   3281 C  CD  . ARG   B 1 47  ? 54.435 -7.682  5.082   1.00 16.13 ?  488  ARG   B CD  1 
ATOM   3282 N  NE  . ARG   B 1 47  ? 53.637 -8.597  5.874   1.00 15.74 ?  488  ARG   B NE  1 
ATOM   3283 C  CZ  . ARG   B 1 47  ? 52.490 -9.128  5.481   1.00 12.94 ?  488  ARG   B CZ  1 
ATOM   3284 N  NH1 . ARG   B 1 47  ? 51.957 -8.805  4.306   1.00 14.48 ?  488  ARG   B NH1 1 
ATOM   3285 N  NH2 . ARG   B 1 47  ? 51.857 -9.972  6.271   1.00 17.18 ?  488  ARG   B NH2 1 
ATOM   3286 N  N   . ILE   B 1 48  ? 58.629 -7.447  5.891   1.00 12.10 ?  489  ILE   B N   1 
ATOM   3287 C  CA  . ILE   B 1 48  ? 59.672 -8.199  6.580   1.00 13.43 ?  489  ILE   B CA  1 
ATOM   3288 C  C   . ILE   B 1 48  ? 59.105 -9.542  7.028   1.00 13.42 ?  489  ILE   B C   1 
ATOM   3289 O  O   . ILE   B 1 48  ? 58.009 -9.586  7.612   1.00 13.24 ?  489  ILE   B O   1 
ATOM   3290 C  CB  . ILE   B 1 48  ? 60.240 -7.393  7.756   1.00 14.02 ?  489  ILE   B CB  1 
ATOM   3291 C  CG1 . ILE   B 1 48  ? 61.063 -6.213  7.230   1.00 16.92 ?  489  ILE   B CG1 1 
ATOM   3292 C  CG2 . ILE   B 1 48  ? 61.055 -8.293  8.669   1.00 14.70 ?  489  ILE   B CG2 1 
ATOM   3293 C  CD1 . ILE   B 1 48  ? 61.501 -5.246  8.315   1.00 18.65 ?  489  ILE   B CD1 1 
ATOM   3294 N  N   . PRO   B 1 49  ? 59.788 -10.657 6.759   1.00 16.06 ?  490  PRO   B N   1 
ATOM   3295 C  CA  . PRO   B 1 49  ? 59.247 -11.964 7.146   1.00 17.75 ?  490  PRO   B CA  1 
ATOM   3296 C  C   . PRO   B 1 49  ? 59.125 -12.101 8.655   1.00 16.63 ?  490  PRO   B C   1 
ATOM   3297 O  O   . PRO   B 1 49  ? 60.024 -11.722 9.410   1.00 15.47 ?  490  PRO   B O   1 
ATOM   3298 C  CB  . PRO   B 1 49  ? 60.276 -12.954 6.588   1.00 19.17 ?  490  PRO   B CB  1 
ATOM   3299 C  CG  . PRO   B 1 49  ? 61.502 -12.151 6.346   1.00 22.09 ?  490  PRO   B CG  1 
ATOM   3300 C  CD  . PRO   B 1 49  ? 61.026 -10.786 5.974   1.00 19.70 ?  490  PRO   B CD  1 
ATOM   3301 N  N   . ALA   B 1 50  ? 58.003 -12.667 9.087   1.00 15.68 ?  491  ALA   B N   1 
ATOM   3302 C  CA  . ALA   B 1 50  ? 57.789 -12.991 10.489  1.00 14.31 ?  491  ALA   B CA  1 
ATOM   3303 C  C   . ALA   B 1 50  ? 58.332 -14.389 10.773  1.00 17.57 ?  491  ALA   B C   1 
ATOM   3304 O  O   . ALA   B 1 50  ? 58.253 -15.284 9.926   1.00 19.74 ?  491  ALA   B O   1 
ATOM   3305 C  CB  . ALA   B 1 50  ? 56.295 -12.940 10.824  1.00 15.25 ?  491  ALA   B CB  1 
ATOM   3306 N  N   . ARG   B 1 51  ? 58.876 -14.577 11.973  1.00 15.52 ?  492  ARG   B N   1 
ATOM   3307 C  CA  . ARG   B 1 51  ? 59.391 -15.875 12.386  1.00 15.45 ?  492  ARG   B CA  1 
ATOM   3308 C  C   . ARG   B 1 51  ? 59.241 -16.019 13.893  1.00 12.65 ?  492  ARG   B C   1 
ATOM   3309 O  O   . ARG   B 1 51  ? 59.004 -15.044 14.613  1.00 14.36 ?  492  ARG   B O   1 
ATOM   3310 C  CB  . ARG   B 1 51  ? 60.874 -16.029 12.040  1.00 16.49 ?  492  ARG   B CB  1 
ATOM   3311 C  CG  . ARG   B 1 51  ? 61.771 -15.234 12.970  1.00 14.99 ?  492  ARG   B CG  1 
ATOM   3312 C  CD  . ARG   B 1 51  ? 63.213 -15.667 12.864  1.00 15.08 ?  492  ARG   B CD  1 
ATOM   3313 N  NE  . ARG   B 1 51  ? 64.150 -14.729 13.485  1.00 15.35 ?  492  ARG   B NE  1 
ATOM   3314 C  CZ  . ARG   B 1 51  ? 64.622 -14.829 14.724  1.00 14.69 ?  492  ARG   B CZ  1 
ATOM   3315 N  NH1 . ARG   B 1 51  ? 64.236 -15.810 15.534  1.00 14.23 ?  492  ARG   B NH1 1 
ATOM   3316 N  NH2 . ARG   B 1 51  ? 65.496 -13.932 15.165  1.00 14.63 ?  492  ARG   B NH2 1 
ATOM   3317 N  N   . LEU   B 1 52  ? 59.427 -17.250 14.367  1.00 13.43 ?  493  LEU   B N   1 
ATOM   3318 C  CA  . LEU   B 1 52  ? 59.404 -17.538 15.794  1.00 12.71 ?  493  LEU   B CA  1 
ATOM   3319 C  C   . LEU   B 1 52  ? 60.741 -17.185 16.427  1.00 13.12 ?  493  LEU   B C   1 
ATOM   3320 O  O   . LEU   B 1 52  ? 61.807 -17.535 15.904  1.00 14.70 ?  493  LEU   B O   1 
ATOM   3321 C  CB  . LEU   B 1 52  ? 59.163 -19.029 16.033  1.00 12.29 ?  493  LEU   B CB  1 
ATOM   3322 C  CG  . LEU   B 1 52  ? 57.814 -19.582 15.556  1.00 13.33 ?  493  LEU   B CG  1 
ATOM   3323 C  CD1 . LEU   B 1 52  ? 57.615 -21.029 16.012  1.00 14.80 ?  493  LEU   B CD1 1 
ATOM   3324 C  CD2 . LEU   B 1 52  ? 56.658 -18.699 16.036  1.00 15.35 ?  493  LEU   B CD2 1 
ATOM   3325 N  N   . ALA   B 1 53  ? 60.680 -16.504 17.566  1.00 12.90 ?  494  ALA   B N   1 
ATOM   3326 C  CA  . ALA   B 1 53  ? 61.844 -16.415 18.432  1.00 12.00 ?  494  ALA   B CA  1 
ATOM   3327 C  C   . ALA   B 1 53  ? 62.241 -17.811 18.907  1.00 13.73 ?  494  ALA   B C   1 
ATOM   3328 O  O   . ALA   B 1 53  ? 61.410 -18.721 18.997  1.00 14.01 ?  494  ALA   B O   1 
ATOM   3329 C  CB  . ALA   B 1 53  ? 61.525 -15.539 19.645  1.00 12.69 ?  494  ALA   B CB  1 
ATOM   3330 N  N   . THR   B 1 54  ? 63.525 -17.982 19.213  1.00 13.59 ?  495  THR   B N   1 
ATOM   3331 C  CA  . THR   B 1 54  ? 64.019 -19.231 19.774  1.00 14.33 ?  495  THR   B CA  1 
ATOM   3332 C  C   . THR   B 1 54  ? 64.123 -19.124 21.291  1.00 15.93 ?  495  THR   B C   1 
ATOM   3333 O  O   . THR   B 1 54  ? 64.157 -18.029 21.863  1.00 15.49 ?  495  THR   B O   1 
ATOM   3334 C  CB  . THR   B 1 54  ? 65.394 -19.579 19.198  1.00 15.84 ?  495  THR   B CB  1 
ATOM   3335 O  OG1 . THR   B 1 54  ? 66.373 -18.684 19.746  1.00 16.30 ?  495  THR   B OG1 1 
ATOM   3336 C  CG2 . THR   B 1 54  ? 65.390 -19.477 17.688  1.00 17.69 ?  495  THR   B CG2 1 
ATOM   3337 N  N   . GLU   B 1 55  ? 64.176 -20.289 21.946  1.00 16.67 ?  496  GLU   B N   1 
ATOM   3338 C  CA  . GLU   B 1 55  ? 64.339 -20.298 23.397  1.00 18.87 ?  496  GLU   B CA  1 
ATOM   3339 C  C   . GLU   B 1 55  ? 65.639 -19.626 23.809  1.00 18.03 ?  496  GLU   B C   1 
ATOM   3340 O  O   . GLU   B 1 55  ? 65.696 -18.976 24.859  1.00 17.47 ?  496  GLU   B O   1 
ATOM   3341 C  CB  . GLU   B 1 55  ? 64.286 -21.725 23.957  1.00 20.99 ?  496  GLU   B CB  1 
ATOM   3342 C  CG  . GLU   B 1 55  ? 62.927 -22.389 23.840  1.00 24.57 ?  496  GLU   B CG  1 
ATOM   3343 C  CD  . GLU   B 1 55  ? 62.875 -23.773 24.482  1.00 27.03 ?  496  GLU   B CD  1 
ATOM   3344 O  OE1 . GLU   B 1 55  ? 63.343 -23.926 25.631  1.00 27.75 ?  496  GLU   B OE1 1 
ATOM   3345 O  OE2 . GLU   B 1 55  ? 62.356 -24.706 23.832  1.00 28.75 -1 496  GLU   B OE2 1 
ATOM   3346 N  N   . GLU   B 1 56  ? 66.686 -19.751 22.991  1.00 19.76 ?  497  GLU   B N   1 
ATOM   3347 C  CA  . GLU   B 1 56  ? 67.950 -19.107 23.327  1.00 19.66 ?  497  GLU   B CA  1 
ATOM   3348 C  C   . GLU   B 1 56  ? 67.818 -17.593 23.260  1.00 18.44 ?  497  GLU   B C   1 
ATOM   3349 O  O   . GLU   B 1 56  ? 68.401 -16.872 24.077  1.00 18.50 ?  497  GLU   B O   1 
ATOM   3350 C  CB  . GLU   B 1 56  ? 69.059 -19.622 22.409  1.00 23.30 ?  497  GLU   B CB  1 
ATOM   3351 C  CG  . GLU   B 1 56  ? 69.101 -21.145 22.305  1.00 30.59 ?  497  GLU   B CG  1 
ATOM   3352 C  CD  . GLU   B 1 56  ? 68.167 -21.698 21.229  1.00 35.25 ?  497  GLU   B CD  1 
ATOM   3353 O  OE1 . GLU   B 1 56  ? 66.993 -22.002 21.532  1.00 34.28 ?  497  GLU   B OE1 1 
ATOM   3354 O  OE2 . GLU   B 1 56  ? 68.614 -21.827 20.067  1.00 39.24 -1 497  GLU   B OE2 1 
ATOM   3355 N  N   . GLU   B 1 57  ? 67.033 -17.095 22.305  1.00 15.50 ?  498  GLU   B N   1 
ATOM   3356 C  CA  . GLU   B 1 57  ? 66.745 -15.666 22.258  1.00 14.39 ?  498  GLU   B CA  1 
ATOM   3357 C  C   . GLU   B 1 57  ? 65.922 -15.224 23.468  1.00 13.67 ?  498  GLU   B C   1 
ATOM   3358 O  O   . GLU   B 1 57  ? 66.170 -14.153 24.034  1.00 14.46 ?  498  GLU   B O   1 
ATOM   3359 C  CB  . GLU   B 1 57  ? 66.051 -15.326 20.936  1.00 13.16 ?  498  GLU   B CB  1 
ATOM   3360 C  CG  . GLU   B 1 57  ? 67.029 -15.342 19.750  1.00 13.42 ?  498  GLU   B CG  1 
ATOM   3361 C  CD  . GLU   B 1 57  ? 66.365 -15.379 18.387  1.00 15.42 ?  498  GLU   B CD  1 
ATOM   3362 O  OE1 . GLU   B 1 57  ? 65.172 -15.736 18.282  1.00 14.59 ?  498  GLU   B OE1 1 
ATOM   3363 O  OE2 . GLU   B 1 57  ? 67.062 -15.049 17.404  1.00 16.80 -1 498  GLU   B OE2 1 
ATOM   3364 N  N   . LEU   B 1 58  ? 64.950 -16.032 23.895  1.00 12.80 ?  499  LEU   B N   1 
ATOM   3365 C  CA  . LEU   B 1 58  ? 64.150 -15.641 25.056  1.00 11.97 ?  499  LEU   B CA  1 
ATOM   3366 C  C   . LEU   B 1 58  ? 65.007 -15.502 26.305  1.00 12.64 ?  499  LEU   B C   1 
ATOM   3367 O  O   . LEU   B 1 58  ? 64.709 -14.677 27.183  1.00 14.09 ?  499  LEU   B O   1 
ATOM   3368 C  CB  . LEU   B 1 58  ? 63.053 -16.669 25.332  1.00 12.42 ?  499  LEU   B CB  1 
ATOM   3369 C  CG  . LEU   B 1 58  ? 61.949 -16.791 24.285  1.00 12.81 ?  499  LEU   B CG  1 
ATOM   3370 C  CD1 . LEU   B 1 58  ? 60.873 -17.727 24.811  1.00 15.49 ?  499  LEU   B CD1 1 
ATOM   3371 C  CD2 . LEU   B 1 58  ? 61.361 -15.430 23.957  1.00 14.20 ?  499  LEU   B CD2 1 
ATOM   3372 N  N   . ALA   B 1 59  ? 66.076 -16.299 26.400  1.00 12.72 ?  500  ALA   B N   1 
ATOM   3373 C  CA  . ALA   B 1 59  ? 66.954 -16.253 27.560  1.00 13.94 ?  500  ALA   B CA  1 
ATOM   3374 C  C   . ALA   B 1 59  ? 67.775 -14.969 27.622  1.00 13.83 ?  500  ALA   B C   1 
ATOM   3375 O  O   . ALA   B 1 59  ? 68.398 -14.704 28.659  1.00 16.25 ?  500  ALA   B O   1 
ATOM   3376 C  CB  . ALA   B 1 59  ? 67.858 -17.488 27.592  1.00 15.97 ?  500  ALA   B CB  1 
ATOM   3377 N  N   . LEU   B 1 60  ? 67.778 -14.166 26.555  1.00 14.31 ?  501  LEU   B N   1 
ATOM   3378 C  CA  . LEU   B 1 60  ? 68.390 -12.843 26.626  1.00 14.62 ?  501  LEU   B CA  1 
ATOM   3379 C  C   . LEU   B 1 60  ? 67.784 -12.006 27.743  1.00 14.14 ?  501  LEU   B C   1 
ATOM   3380 O  O   . LEU   B 1 60  ? 68.465 -11.145 28.308  1.00 15.29 ?  501  LEU   B O   1 
ATOM   3381 C  CB  . LEU   B 1 60  ? 68.213 -12.114 25.299  1.00 15.69 ?  501  LEU   B CB  1 
ATOM   3382 C  CG  . LEU   B 1 60  ? 68.984 -12.656 24.099  1.00 17.20 ?  501  LEU   B CG  1 
ATOM   3383 C  CD1 . LEU   B 1 60  ? 68.574 -11.894 22.848  1.00 18.90 ?  501  LEU   B CD1 1 
ATOM   3384 C  CD2 . LEU   B 1 60  ? 70.491 -12.557 24.344  1.00 18.45 ?  501  LEU   B CD2 1 
ATOM   3385 N  N   . CYS   B 1 61  ? 66.509 -12.230 28.078  1.00 13.17 ?  502  CYS   B N   1 
ATOM   3386 C  CA  . CYS   B 1 61  ? 65.851 -11.444 29.110  1.00 14.55 ?  502  CYS   B CA  1 
ATOM   3387 C  C   . CYS   B 1 61  ? 65.116 -12.275 30.156  1.00 13.60 ?  502  CYS   B C   1 
ATOM   3388 O  O   . CYS   B 1 61  ? 64.827 -11.745 31.235  1.00 16.53 ?  502  CYS   B O   1 
ATOM   3389 C  CB  . CYS   B 1 61  ? 64.817 -10.502 28.479  1.00 15.16 ?  502  CYS   B CB  1 
ATOM   3390 S  SG  . CYS   B 1 61  ? 65.500 -9.152  27.480  1.00 13.95 ?  502  CYS   B SG  1 
ATOM   3391 N  N   . HIS   B 1 62  ? 64.782 -13.535 29.882  1.00 12.49 ?  503  HIS   B N   1 
ATOM   3392 C  CA  . HIS   B 1 62  ? 63.872 -14.280 30.738  1.00 12.78 ?  503  HIS   B CA  1 
ATOM   3393 C  C   . HIS   B 1 62  ? 64.548 -15.494 31.355  1.00 14.83 ?  503  HIS   B C   1 
ATOM   3394 O  O   . HIS   B 1 62  ? 65.461 -16.089 30.781  1.00 15.82 ?  503  HIS   B O   1 
ATOM   3395 C  CB  . HIS   B 1 62  ? 62.597 -14.697 29.990  1.00 12.25 ?  503  HIS   B CB  1 
ATOM   3396 C  CG  . HIS   B 1 62  ? 61.764 -13.536 29.552  1.00 11.53 ?  503  HIS   B CG  1 
ATOM   3397 N  ND1 . HIS   B 1 62  ? 61.001 -12.793 30.426  1.00 11.79 ?  503  HIS   B ND1 1 
ATOM   3398 C  CD2 . HIS   B 1 62  ? 61.598 -12.975 28.329  1.00 11.43 ?  503  HIS   B CD2 1 
ATOM   3399 C  CE1 . HIS   B 1 62  ? 60.395 -11.824 29.755  1.00 11.44 ?  503  HIS   B CE1 1 
ATOM   3400 N  NE2 . HIS   B 1 62  ? 60.748 -11.910 28.485  1.00 12.90 ?  503  HIS   B NE2 1 
ATOM   3401 N  N   . SER   B 1 63  ? 64.072 -15.841 32.544  1.00 13.53 ?  504  SER   B N   1 
ATOM   3402 C  CA  . SER   B 1 63  ? 64.578 -16.981 33.286  1.00 14.23 ?  504  SER   B CA  1 
ATOM   3403 C  C   . SER   B 1 63  ? 64.136 -18.299 32.647  1.00 16.08 ?  504  SER   B C   1 
ATOM   3404 O  O   . SER   B 1 63  ? 63.112 -18.380 31.958  1.00 14.65 ?  504  SER   B O   1 
ATOM   3405 C  CB  . SER   B 1 63  ? 64.080 -16.883 34.722  1.00 14.84 ?  504  SER   B CB  1 
ATOM   3406 O  OG  . SER   B 1 63  ? 62.753 -17.380 34.792  1.00 16.11 ?  504  SER   B OG  1 
ATOM   3407 N  N   A SER   B 1 64  ? 64.941 -19.342 32.872  0.58 17.17 ?  505  SER   B N   1 
ATOM   3408 N  N   B SER   B 1 64  ? 64.938 -19.343 32.873  0.42 17.02 ?  505  SER   B N   1 
ATOM   3409 C  CA  A SER   B 1 64  ? 64.603 -20.662 32.347  0.58 17.17 ?  505  SER   B CA  1 
ATOM   3410 C  CA  B SER   B 1 64  ? 64.596 -20.657 32.338  0.42 16.90 ?  505  SER   B CA  1 
ATOM   3411 C  C   A SER   B 1 64  ? 63.287 -21.170 32.925  0.58 15.43 ?  505  SER   B C   1 
ATOM   3412 C  C   B SER   B 1 64  ? 63.297 -21.187 32.930  0.42 15.74 ?  505  SER   B C   1 
ATOM   3413 O  O   A SER   B 1 64  ? 62.501 -21.811 32.218  0.58 16.60 ?  505  SER   B O   1 
ATOM   3414 O  O   B SER   B 1 64  ? 62.532 -21.865 32.234  0.42 16.53 ?  505  SER   B O   1 
ATOM   3415 C  CB  A SER   B 1 64  ? 65.729 -21.652 32.642  0.58 19.34 ?  505  SER   B CB  1 
ATOM   3416 C  CB  B SER   B 1 64  ? 65.730 -21.648 32.595  0.42 18.07 ?  505  SER   B CB  1 
ATOM   3417 O  OG  A SER   B 1 64  ? 65.955 -21.762 34.035  0.58 21.48 ?  505  SER   B OG  1 
ATOM   3418 O  OG  B SER   B 1 64  ? 65.367 -22.945 32.159  0.42 19.56 ?  505  SER   B OG  1 
ATOM   3419 N  N   . LYS   B 1 65  ? 63.033 -20.903 34.207  1.00 15.57 ?  506  LYS   B N   1 
ATOM   3420 C  CA  . LYS   B 1 65  ? 61.785 -21.352 34.812  1.00 15.80 ?  506  LYS   B CA  1 
ATOM   3421 C  C   . LYS   B 1 65  ? 60.584 -20.702 34.132  1.00 14.24 ?  506  LYS   B C   1 
ATOM   3422 O  O   . LYS   B 1 65  ? 59.585 -21.371 33.848  1.00 14.43 ?  506  LYS   B O   1 
ATOM   3423 C  CB  . LYS   B 1 65  ? 61.795 -21.040 36.307  1.00 20.41 ?  506  LYS   B CB  1 
ATOM   3424 C  CG  . LYS   B 1 65  ? 60.499 -21.359 37.026  1.00 24.76 ?  506  LYS   B CG  1 
ATOM   3425 C  CD  . LYS   B 1 65  ? 60.683 -21.282 38.541  1.00 30.60 ?  506  LYS   B CD  1 
ATOM   3426 C  CE  . LYS   B 1 65  ? 59.577 -20.493 39.219  1.00 37.01 ?  506  LYS   B CE  1 
ATOM   3427 N  NZ  . LYS   B 1 65  ? 59.924 -20.159 40.638  1.00 41.01 ?  506  LYS   B NZ  1 
ATOM   3428 N  N   . HIS   B 1 66  ? 60.674 -19.403 33.843  1.00 13.14 ?  507  HIS   B N   1 
ATOM   3429 C  CA  . HIS   B 1 66  ? 59.567 -18.709 33.192  1.00 12.98 ?  507  HIS   B CA  1 
ATOM   3430 C  C   . HIS   B 1 66  ? 59.375 -19.188 31.752  1.00 11.91 ?  507  HIS   B C   1 
ATOM   3431 O  O   . HIS   B 1 66  ? 58.243 -19.436 31.317  1.00 13.44 ?  507  HIS   B O   1 
ATOM   3432 C  CB  . HIS   B 1 66  ? 59.785 -17.196 33.259  1.00 14.16 ?  507  HIS   B CB  1 
ATOM   3433 C  CG  . HIS   B 1 66  ? 58.739 -16.402 32.534  1.00 12.64 ?  507  HIS   B CG  1 
ATOM   3434 N  ND1 . HIS   B 1 66  ? 57.426 -16.351 32.947  1.00 14.35 ?  507  HIS   B ND1 1 
ATOM   3435 C  CD2 . HIS   B 1 66  ? 58.810 -15.637 31.416  1.00 11.84 ?  507  HIS   B CD2 1 
ATOM   3436 C  CE1 . HIS   B 1 66  ? 56.734 -15.582 32.123  1.00 13.10 ?  507  HIS   B CE1 1 
ATOM   3437 N  NE2 . HIS   B 1 66  ? 57.551 -15.132 31.188  1.00 12.56 ?  507  HIS   B NE2 1 
ATOM   3438 N  N   . ILE   B 1 67  ? 60.469 -19.312 30.994  1.00 12.34 ?  508  ILE   B N   1 
ATOM   3439 C  CA  . ILE   B 1 67  ? 60.378 -19.855 29.642  1.00 13.34 ?  508  ILE   B CA  1 
ATOM   3440 C  C   . ILE   B 1 67  ? 59.724 -21.225 29.659  1.00 13.40 ?  508  ILE   B C   1 
ATOM   3441 O  O   . ILE   B 1 67  ? 58.837 -21.515 28.849  1.00 13.51 ?  508  ILE   B O   1 
ATOM   3442 C  CB  . ILE   B 1 67  ? 61.765 -19.895 28.970  1.00 12.82 ?  508  ILE   B CB  1 
ATOM   3443 C  CG1 . ILE   B 1 67  ? 62.290 -18.474 28.746  1.00 13.28 ?  508  ILE   B CG1 1 
ATOM   3444 C  CG2 . ILE   B 1 67  ? 61.705 -20.702 27.652  1.00 15.18 ?  508  ILE   B CG2 1 
ATOM   3445 C  CD1 . ILE   B 1 67  ? 63.785 -18.400 28.453  1.00 14.95 ?  508  ILE   B CD1 1 
ATOM   3446 N  N   . SER   B 1 68  ? 60.136 -22.086 30.592  1.00 14.84 ?  509  SER   B N   1 
ATOM   3447 C  CA  . SER   B 1 68  ? 59.664 -23.468 30.581  1.00 14.50 ?  509  SER   B CA  1 
ATOM   3448 C  C   . SER   B 1 68  ? 58.168 -23.559 30.874  1.00 14.76 ?  509  SER   B C   1 
ATOM   3449 O  O   . SER   B 1 68  ? 57.449 -24.325 30.220  1.00 13.27 ?  509  SER   B O   1 
ATOM   3450 C  CB  . SER   B 1 68  ? 60.474 -24.293 31.582  1.00 20.61 ?  509  SER   B CB  1 
ATOM   3451 O  OG  . SER   B 1 68  ? 59.858 -25.542 31.830  1.00 25.87 ?  509  SER   B OG  1 
ATOM   3452 N  N   . ILE   B 1 69  ? 57.674 -22.786 31.843  1.00 13.50 ?  510  ILE   B N   1 
ATOM   3453 C  CA  . ILE   B 1 69  ? 56.267 -22.901 32.220  1.00 14.10 ?  510  ILE   B CA  1 
ATOM   3454 C  C   . ILE   B 1 69  ? 55.355 -22.357 31.121  1.00 14.03 ?  510  ILE   B C   1 
ATOM   3455 O  O   . ILE   B 1 69  ? 54.352 -22.987 30.768  1.00 13.39 ?  510  ILE   B O   1 
ATOM   3456 C  CB  . ILE   B 1 69  ? 55.981 -22.309 33.616  1.00 17.67 ?  510  ILE   B CB  1 
ATOM   3457 C  CG1 . ILE   B 1 69  ? 54.620 -22.808 34.123  1.00 24.34 ?  510  ILE   B CG1 1 
ATOM   3458 C  CG2 . ILE   B 1 69  ? 56.070 -20.782 33.622  1.00 17.25 ?  510  ILE   B CG2 1 
ATOM   3459 C  CD1 . ILE   B 1 69  ? 54.495 -22.832 35.641  1.00 29.18 ?  510  ILE   B CD1 1 
ATOM   3460 N  N   . ILE   B 1 70  ? 55.708 -21.216 30.524  1.00 12.06 ?  511  ILE   B N   1 
ATOM   3461 C  CA  . ILE   B 1 70  ? 54.902 -20.715 29.413  1.00 13.69 ?  511  ILE   B CA  1 
ATOM   3462 C  C   . ILE   B 1 70  ? 54.999 -21.652 28.211  1.00 14.23 ?  511  ILE   B C   1 
ATOM   3463 O  O   . ILE   B 1 70  ? 53.999 -21.933 27.543  1.00 13.41 ?  511  ILE   B O   1 
ATOM   3464 C  CB  . ILE   B 1 70  ? 55.269 -19.258 29.067  1.00 12.55 ?  511  ILE   B CB  1 
ATOM   3465 C  CG1 . ILE   B 1 70  ? 55.172 -18.351 30.300  1.00 12.19 ?  511  ILE   B CG1 1 
ATOM   3466 C  CG2 . ILE   B 1 70  ? 54.383 -18.728 27.909  1.00 12.52 ?  511  ILE   B CG2 1 
ATOM   3467 C  CD1 . ILE   B 1 70  ? 53.805 -18.370 30.965  1.00 13.28 ?  511  ILE   B CD1 1 
ATOM   3468 N  N   . LYS   B 1 71  ? 56.196 -22.172 27.931  1.00 13.36 ?  512  LYS   B N   1 
ATOM   3469 C  CA  . LYS   B 1 71  ? 56.346 -23.152 26.857  1.00 13.48 ?  512  LYS   B CA  1 
ATOM   3470 C  C   . LYS   B 1 71  ? 55.418 -24.349 27.054  1.00 13.72 ?  512  LYS   B C   1 
ATOM   3471 O  O   . LYS   B 1 71  ? 54.792 -24.820 26.097  1.00 14.30 ?  512  LYS   B O   1 
ATOM   3472 C  CB  . LYS   B 1 71  ? 57.805 -23.606 26.781  1.00 14.46 ?  512  LYS   B CB  1 
ATOM   3473 C  CG  . LYS   B 1 71  ? 58.078 -24.718 25.776  1.00 15.83 ?  512  LYS   B CG  1 
ATOM   3474 C  CD  . LYS   B 1 71  ? 59.542 -25.154 25.844  1.00 19.62 ?  512  LYS   B CD  1 
ATOM   3475 C  CE  . LYS   B 1 71  ? 59.802 -26.445 25.077  1.00 22.66 ?  512  LYS   B CE  1 
ATOM   3476 N  NZ  . LYS   B 1 71  ? 61.169 -26.987 25.341  1.00 25.23 ?  512  LYS   B NZ  1 
ATOM   3477 N  N   . SER   B 1 72  ? 55.294 -24.835 28.298  1.00 14.04 ?  513  SER   B N   1 
ATOM   3478 C  CA  . SER   B 1 72  ? 54.481 -26.015 28.585  1.00 13.52 ?  513  SER   B CA  1 
ATOM   3479 C  C   . SER   B 1 72  ? 52.997 -25.775 28.350  1.00 13.97 ?  513  SER   B C   1 
ATOM   3480 O  O   . SER   B 1 72  ? 52.241 -26.742 28.191  1.00 15.48 ?  513  SER   B O   1 
ATOM   3481 C  CB  . SER   B 1 72  ? 54.701 -26.476 30.034  1.00 13.84 ?  513  SER   B CB  1 
ATOM   3482 O  OG  . SER   B 1 72  ? 54.059 -25.618 30.962  1.00 15.66 ?  513  SER   B OG  1 
ATOM   3483 N  N   . SER   B 1 73  ? 52.571 -24.515 28.304  1.00 13.58 ?  514  SER   B N   1 
ATOM   3484 C  CA  . SER   B 1 73  ? 51.164 -24.213 28.105  1.00 13.30 ?  514  SER   B CA  1 
ATOM   3485 C  C   . SER   B 1 73  ? 50.656 -24.651 26.745  1.00 11.89 ?  514  SER   B C   1 
ATOM   3486 O  O   . SER   B 1 73  ? 49.443 -24.821 26.590  1.00 12.34 ?  514  SER   B O   1 
ATOM   3487 C  CB  . SER   B 1 73  ? 50.893 -22.729 28.371  1.00 12.16 ?  514  SER   B CB  1 
ATOM   3488 O  OG  . SER   B 1 73  ? 51.375 -21.894 27.331  1.00 11.94 ?  514  SER   B OG  1 
ATOM   3489 N  N   . GLU   B 1 74  ? 51.547 -24.855 25.774  1.00 13.27 ?  515  GLU   B N   1 
ATOM   3490 C  CA  . GLU   B 1 74  ? 51.107 -25.322 24.462  1.00 13.08 ?  515  GLU   B CA  1 
ATOM   3491 C  C   . GLU   B 1 74  ? 50.391 -26.664 24.547  1.00 13.87 ?  515  GLU   B C   1 
ATOM   3492 O  O   . GLU   B 1 74  ? 49.517 -26.954 23.719  1.00 14.72 ?  515  GLU   B O   1 
ATOM   3493 C  CB  . GLU   B 1 74  ? 52.296 -25.403 23.501  1.00 13.88 ?  515  GLU   B CB  1 
ATOM   3494 C  CG  . GLU   B 1 74  ? 51.935 -25.920 22.113  1.00 15.24 ?  515  GLU   B CG  1 
ATOM   3495 C  CD  . GLU   B 1 74  ? 53.110 -25.939 21.158  1.00 18.98 ?  515  GLU   B CD  1 
ATOM   3496 O  OE1 . GLU   B 1 74  ? 54.266 -25.867 21.632  1.00 19.47 ?  515  GLU   B OE1 1 
ATOM   3497 O  OE2 . GLU   B 1 74  ? 52.865 -26.031 19.933  1.00 22.87 -1 515  GLU   B OE2 1 
ATOM   3498 N  N   . HIS   B 1 75  ? 50.737 -27.493 25.533  1.00 16.20 ?  516  HIS   B N   1 
ATOM   3499 C  CA  . HIS   B 1 75  ? 50.197 -28.845 25.636  1.00 18.75 ?  516  HIS   B CA  1 
ATOM   3500 C  C   . HIS   B 1 75  ? 49.303 -29.043 26.856  1.00 17.56 ?  516  HIS   B C   1 
ATOM   3501 O  O   . HIS   B 1 75  ? 49.011 -30.182 27.227  1.00 20.49 ?  516  HIS   B O   1 
ATOM   3502 C  CB  . HIS   B 1 75  ? 51.328 -29.874 25.606  1.00 20.24 ?  516  HIS   B CB  1 
ATOM   3503 C  CG  . HIS   B 1 75  ? 52.206 -29.750 24.402  1.00 22.63 ?  516  HIS   B CG  1 
ATOM   3504 N  ND1 . HIS   B 1 75  ? 51.775 -30.087 23.138  1.00 24.44 ?  516  HIS   B ND1 1 
ATOM   3505 C  CD2 . HIS   B 1 75  ? 53.476 -29.303 24.261  1.00 24.48 ?  516  HIS   B CD2 1 
ATOM   3506 C  CE1 . HIS   B 1 75  ? 52.745 -29.858 22.269  1.00 24.18 ?  516  HIS   B CE1 1 
ATOM   3507 N  NE2 . HIS   B 1 75  ? 53.788 -29.382 22.925  1.00 27.38 ?  516  HIS   B NE2 1 
ATOM   3508 N  N   . MET   B 1 76  ? 48.846 -27.958 27.473  1.00 15.68 ?  517  MET   B N   1 
ATOM   3509 C  CA  . MET   B 1 76  ? 48.034 -28.039 28.675  1.00 15.44 ?  517  MET   B CA  1 
ATOM   3510 C  C   . MET   B 1 76  ? 46.565 -28.267 28.338  1.00 16.79 ?  517  MET   B C   1 
ATOM   3511 O  O   . MET   B 1 76  ? 46.074 -27.916 27.262  1.00 17.92 ?  517  MET   B O   1 
ATOM   3512 C  CB  . MET   B 1 76  ? 48.166 -26.753 29.483  1.00 14.72 ?  517  MET   B CB  1 
ATOM   3513 C  CG  . MET   B 1 76  ? 49.395 -26.730 30.373  1.00 14.51 ?  517  MET   B CG  1 
ATOM   3514 S  SD  . MET   B 1 76  ? 49.472 -25.208 31.320  1.00 16.67 ?  517  MET   B SD  1 
ATOM   3515 C  CE  . MET   B 1 76  ? 50.857 -25.571 32.407  1.00 17.66 ?  517  MET   B CE  1 
ATOM   3516 N  N   . LYS   B 1 77  ? 45.862 -28.863 29.293  1.00 16.14 ?  518  LYS   B N   1 
ATOM   3517 C  CA  . LYS   B 1 77  ? 44.419 -28.990 29.242  1.00 16.35 ?  518  LYS   B CA  1 
ATOM   3518 C  C   . LYS   B 1 77  ? 43.763 -27.680 29.658  1.00 15.88 ?  518  LYS   B C   1 
ATOM   3519 O  O   . LYS   B 1 77  ? 44.384 -26.844 30.313  1.00 15.72 ?  518  LYS   B O   1 
ATOM   3520 C  CB  . LYS   B 1 77  ? 43.977 -30.091 30.203  1.00 19.24 ?  518  LYS   B CB  1 
ATOM   3521 C  CG  . LYS   B 1 77  ? 44.616 -31.434 29.926  1.00 25.94 ?  518  LYS   B CG  1 
ATOM   3522 C  CD  . LYS   B 1 77  ? 44.278 -32.427 31.020  1.00 32.15 ?  518  LYS   B CD  1 
ATOM   3523 C  CE  . LYS   B 1 77  ? 45.420 -33.393 31.235  1.00 36.57 ?  518  LYS   B CE  1 
ATOM   3524 N  NZ  . LYS   B 1 77  ? 46.465 -32.795 32.123  1.00 38.88 ?  518  LYS   B NZ  1 
ATOM   3525 N  N   . PRO   B 1 78  ? 42.493 -27.482 29.297  1.00 16.38 ?  519  PRO   B N   1 
ATOM   3526 C  CA  . PRO   B 1 78  ? 41.806 -26.234 29.683  1.00 16.45 ?  519  PRO   B CA  1 
ATOM   3527 C  C   . PRO   B 1 78  ? 41.936 -25.840 31.151  1.00 14.54 ?  519  PRO   B C   1 
ATOM   3528 O  O   . PRO   B 1 78  ? 42.207 -24.666 31.444  1.00 15.32 ?  519  PRO   B O   1 
ATOM   3529 C  CB  . PRO   B 1 78  ? 40.356 -26.503 29.258  1.00 17.77 ?  519  PRO   B CB  1 
ATOM   3530 C  CG  . PRO   B 1 78  ? 40.500 -27.437 28.086  1.00 18.58 ?  519  PRO   B CG  1 
ATOM   3531 C  CD  . PRO   B 1 78  ? 41.646 -28.343 28.448  1.00 19.11 ?  519  PRO   B CD  1 
ATOM   3532 N  N   . ARG   B 1 79  ? 41.726 -26.772 32.088  1.00 12.70 ?  520  ARG   B N   1 
ATOM   3533 C  CA  . ARG   B 1 79  ? 41.861 -26.429 33.504  1.00 15.61 ?  520  ARG   B CA  1 
ATOM   3534 C  C   . ARG   B 1 79  ? 43.280 -25.998 33.835  1.00 13.27 ?  520  ARG   B C   1 
ATOM   3535 O  O   . ARG   B 1 79  ? 43.480 -25.079 34.638  1.00 14.42 ?  520  ARG   B O   1 
ATOM   3536 C  CB  . ARG   B 1 79  ? 41.430 -27.595 34.405  1.00 18.04 ?  520  ARG   B CB  1 
ATOM   3537 C  CG  . ARG   B 1 79  ? 41.335 -27.213 35.882  1.00 18.00 ?  520  ARG   B CG  1 
ATOM   3538 C  CD  . ARG   B 1 79  ? 41.141 -28.431 36.802  1.00 18.35 ?  520  ARG   B CD  1 
ATOM   3539 N  NE  . ARG   B 1 79  ? 42.335 -29.271 36.837  0.68 18.30 ?  520  ARG   B NE  1 
ATOM   3540 C  CZ  . ARG   B 1 79  ? 42.486 -30.343 37.612  0.78 19.51 ?  520  ARG   B CZ  1 
ATOM   3541 N  NH1 . ARG   B 1 79  ? 41.511 -30.727 38.431  1.00 22.90 ?  520  ARG   B NH1 1 
ATOM   3542 N  NH2 . ARG   B 1 79  ? 43.621 -31.032 37.565  0.67 19.95 ?  520  ARG   B NH2 1 
ATOM   3543 N  N   . ASP   B 1 80  ? 44.279 -26.666 33.239  1.00 13.33 ?  521  ASP   B N   1 
ATOM   3544 C  CA  . ASP   B 1 80  ? 45.672 -26.287 33.462  1.00 13.47 ?  521  ASP   B CA  1 
ATOM   3545 C  C   . ASP   B 1 80  ? 45.916 -24.853 33.018  1.00 12.27 ?  521  ASP   B C   1 
ATOM   3546 O  O   . ASP   B 1 80  ? 46.600 -24.089 33.705  1.00 12.72 ?  521  ASP   B O   1 
ATOM   3547 C  CB  . ASP   B 1 80  ? 46.607 -27.189 32.657  1.00 13.57 ?  521  ASP   B CB  1 
ATOM   3548 C  CG  . ASP   B 1 80  ? 46.591 -28.635 33.108  1.00 16.57 ?  521  ASP   B CG  1 
ATOM   3549 O  OD1 . ASP   B 1 80  ? 46.648 -28.907 34.328  1.00 15.17 ?  521  ASP   B OD1 1 
ATOM   3550 O  OD2 . ASP   B 1 80  ? 46.562 -29.509 32.213  1.00 20.33 -1 521  ASP   B OD2 1 
ATOM   3551 N  N   . LEU   B 1 81  ? 45.369 -24.484 31.853  1.00 12.87 ?  522  LEU   B N   1 
ATOM   3552 C  CA  . LEU   B 1 81  ? 45.538 -23.139 31.313  1.00 14.84 ?  522  LEU   B CA  1 
ATOM   3553 C  C   . LEU   B 1 81  ? 44.839 -22.101 32.172  1.00 14.80 ?  522  LEU   B C   1 
ATOM   3554 O  O   . LEU   B 1 81  ? 45.387 -21.018 32.408  1.00 13.30 ?  522  LEU   B O   1 
ATOM   3555 C  CB  . LEU   B 1 81  ? 44.971 -23.077 29.895  1.00 14.22 ?  522  LEU   B CB  1 
ATOM   3556 C  CG  . LEU   B 1 81  ? 45.712 -23.859 28.811  1.00 14.45 ?  522  LEU   B CG  1 
ATOM   3557 C  CD1 . LEU   B 1 81  ? 44.867 -23.957 27.561  1.00 13.32 ?  522  LEU   B CD1 1 
ATOM   3558 C  CD2 . LEU   B 1 81  ? 47.041 -23.213 28.470  1.00 14.41 ?  522  LEU   B CD2 1 
ATOM   3559 N  N   . ASN   B 1 82  ? 43.621 -22.403 32.639  1.00 14.25 ?  523  ASN   B N   1 
ATOM   3560 C  CA  . ASN   B 1 82  ? 42.915 -21.454 33.490  1.00 16.21 ?  523  ASN   B CA  1 
ATOM   3561 C  C   . ASN   B 1 82  ? 43.674 -21.231 34.786  1.00 14.46 ?  523  ASN   B C   1 
ATOM   3562 O  O   . ASN   B 1 82  ? 43.839 -20.090 35.233  1.00 14.55 ?  523  ASN   B O   1 
ATOM   3563 C  CB  . ASN   B 1 82  ? 41.503 -21.957 33.795  1.00 21.18 ?  523  ASN   B CB  1 
ATOM   3564 C  CG  . ASN   B 1 82  ? 40.625 -22.018 32.562  1.00 29.50 ?  523  ASN   B CG  1 
ATOM   3565 O  OD1 . ASN   B 1 82  ? 40.766 -21.207 31.647  1.00 33.03 ?  523  ASN   B OD1 1 
ATOM   3566 N  ND2 . ASN   B 1 82  ? 39.701 -22.978 32.538  1.00 31.34 ?  523  ASN   B ND2 1 
ATOM   3567 N  N   . ARG   B 1 83  ? 44.153 -22.317 35.400  1.00 13.87 ?  524  ARG   B N   1 
ATOM   3568 C  CA  . ARG   B 1 83  ? 44.855 -22.211 36.673  1.00 13.53 ?  524  ARG   B CA  1 
ATOM   3569 C  C   . ARG   B 1 83  ? 46.184 -21.489 36.512  1.00 12.63 ?  524  ARG   B C   1 
ATOM   3570 O  O   . ARG   B 1 83  ? 46.535 -20.637 37.331  1.00 13.19 ?  524  ARG   B O   1 
ATOM   3571 C  CB  . ARG   B 1 83  ? 45.063 -23.605 37.265  1.00 14.46 ?  524  ARG   B CB  1 
ATOM   3572 C  CG  . ARG   B 1 83  ? 43.801 -24.206 37.850  1.00 15.10 ?  524  ARG   B CG  1 
ATOM   3573 C  CD  . ARG   B 1 83  ? 44.036 -25.640 38.268  1.00 16.43 ?  524  ARG   B CD  1 
ATOM   3574 N  NE  . ARG   B 1 83  ? 42.906 -26.162 39.030  1.00 15.62 ?  524  ARG   B NE  1 
ATOM   3575 C  CZ  . ARG   B 1 83  ? 42.944 -27.302 39.710  1.00 16.43 ?  524  ARG   B CZ  1 
ATOM   3576 N  NH1 . ARG   B 1 83  ? 44.052 -28.028 39.703  1.00 15.03 ?  524  ARG   B NH1 1 
ATOM   3577 N  NH2 . ARG   B 1 83  ? 41.874 -27.718 40.380  1.00 16.76 ?  524  ARG   B NH2 1 
ATOM   3578 N  N   . LEU   B 1 84  ? 46.935 -21.808 35.458  1.00 12.14 ?  525  LEU   B N   1 
ATOM   3579 C  CA  . LEU   B 1 84  ? 48.207 -21.129 35.249  1.00 13.48 ?  525  LEU   B CA  1 
ATOM   3580 C  C   . LEU   B 1 84  ? 47.994 -19.639 35.005  1.00 12.14 ?  525  LEU   B C   1 
ATOM   3581 O  O   . LEU   B 1 84  ? 48.655 -18.804 35.620  1.00 13.16 ?  525  LEU   B O   1 
ATOM   3582 C  CB  . LEU   B 1 84  ? 48.980 -21.776 34.101  1.00 12.18 ?  525  LEU   B CB  1 
ATOM   3583 C  CG  . LEU   B 1 84  ? 50.289 -21.070 33.731  1.00 11.69 ?  525  LEU   B CG  1 
ATOM   3584 C  CD1 . LEU   B 1 84  ? 51.271 -21.039 34.932  1.00 13.05 ?  525  LEU   B CD1 1 
ATOM   3585 C  CD2 . LEU   B 1 84  ? 50.968 -21.704 32.516  1.00 13.11 ?  525  LEU   B CD2 1 
ATOM   3586 N  N   . GLY   B 1 85  ? 47.047 -19.284 34.135  1.00 12.64 ?  526  GLY   B N   1 
ATOM   3587 C  CA  . GLY   B 1 85  ? 46.808 -17.878 33.861  1.00 15.19 ?  526  GLY   B CA  1 
ATOM   3588 C  C   . GLY   B 1 85  ? 46.426 -17.110 35.110  1.00 15.00 ?  526  GLY   B C   1 
ATOM   3589 O  O   . GLY   B 1 85  ? 46.875 -15.979 35.319  1.00 13.96 ?  526  GLY   B O   1 
ATOM   3590 N  N   . ASP   B 1 86  ? 45.653 -17.745 35.996  1.00 15.90 ?  527  ASP   B N   1 
ATOM   3591 C  CA  . ASP   B 1 86  ? 45.194 -17.085 37.209  1.00 15.93 ?  527  ASP   B CA  1 
ATOM   3592 C  C   . ASP   B 1 86  ? 46.288 -16.930 38.259  1.00 17.49 ?  527  ASP   B C   1 
ATOM   3593 O  O   . ASP   B 1 86  ? 46.048 -16.274 39.280  1.00 18.53 ?  527  ASP   B O   1 
ATOM   3594 C  CB  . ASP   B 1 86  ? 43.988 -17.826 37.796  1.00 18.73 ?  527  ASP   B CB  1 
ATOM   3595 C  CG  . ASP   B 1 86  ? 42.706 -17.592 36.997  1.00 23.65 ?  527  ASP   B CG  1 
ATOM   3596 O  OD1 . ASP   B 1 86  ? 42.715 -16.793 36.034  1.00 23.51 ?  527  ASP   B OD1 1 
ATOM   3597 O  OD2 . ASP   B 1 86  ? 41.677 -18.213 37.335  1.00 26.97 -1 527  ASP   B OD2 1 
ATOM   3598 N  N   . GLU   B 1 87  ? 47.474 -17.512 38.041  1.00 16.33 ?  528  GLU   B N   1 
ATOM   3599 C  CA  . GLU   B 1 87  ? 48.603 -17.274 38.933  1.00 16.19 ?  528  GLU   B CA  1 
ATOM   3600 C  C   . GLU   B 1 87  ? 49.209 -15.897 38.717  1.00 14.45 ?  528  GLU   B C   1 
ATOM   3601 O  O   . GLU   B 1 87  ? 49.925 -15.397 39.596  1.00 18.00 ?  528  GLU   B O   1 
ATOM   3602 C  CB  . GLU   B 1 87  ? 49.696 -18.322 38.701  1.00 17.12 ?  528  GLU   B CB  1 
ATOM   3603 C  CG  . GLU   B 1 87  ? 49.311 -19.752 39.032  1.00 23.70 ?  528  GLU   B CG  1 
ATOM   3604 C  CD  . GLU   B 1 87  ? 48.995 -19.957 40.505  1.00 30.91 ?  528  GLU   B CD  1 
ATOM   3605 O  OE1 . GLU   B 1 87  ? 48.250 -20.906 40.819  1.00 32.75 ?  528  GLU   B OE1 1 
ATOM   3606 O  OE2 . GLU   B 1 87  ? 49.490 -19.177 41.348  1.00 35.17 -1 528  GLU   B OE2 1 
ATOM   3607 N  N   . TYR   B 1 88  ? 48.957 -15.282 37.568  1.00 12.56 ?  529  TYR   B N   1 
ATOM   3608 C  CA  . TYR   B 1 88  ? 49.536 -14.004 37.204  1.00 13.60 ?  529  TYR   B CA  1 
ATOM   3609 C  C   . TYR   B 1 88  ? 48.502 -12.899 37.369  1.00 11.25 ?  529  TYR   B C   1 
ATOM   3610 O  O   . TYR   B 1 88  ? 47.298 -13.146 37.486  1.00 12.36 ?  529  TYR   B O   1 
ATOM   3611 C  CB  . TYR   B 1 88  ? 50.031 -14.030 35.752  1.00 12.12 ?  529  TYR   B CB  1 
ATOM   3612 C  CG  . TYR   B 1 88  ? 51.001 -15.143 35.475  1.00 10.87 ?  529  TYR   B CG  1 
ATOM   3613 C  CD1 . TYR   B 1 88  ? 52.321 -15.063 35.909  1.00 11.86 ?  529  TYR   B CD1 1 
ATOM   3614 C  CD2 . TYR   B 1 88  ? 50.607 -16.269 34.767  1.00 12.67 ?  529  TYR   B CD2 1 
ATOM   3615 C  CE1 . TYR   B 1 88  ? 53.217 -16.084 35.656  1.00 13.57 ?  529  TYR   B CE1 1 
ATOM   3616 C  CE2 . TYR   B 1 88  ? 51.503 -17.286 34.495  1.00 12.19 ?  529  TYR   B CE2 1 
ATOM   3617 C  CZ  . TYR   B 1 88  ? 52.803 -17.199 34.960  1.00 12.92 ?  529  TYR   B CZ  1 
ATOM   3618 O  OH  . TYR   B 1 88  ? 53.686 -18.221 34.686  1.00 14.30 ?  529  TYR   B OH  1 
ATOM   3619 N  N   . ASN   B 1 89  ? 48.999 -11.666 37.376  1.00 12.07 ?  530  ASN   B N   1 
ATOM   3620 C  CA  . ASN   B 1 89  ? 48.146 -10.486 37.337  1.00 13.89 ?  530  ASN   B CA  1 
ATOM   3621 C  C   . ASN   B 1 89  ? 47.709 -10.258 35.891  1.00 12.84 ?  530  ASN   B C   1 
ATOM   3622 O  O   . ASN   B 1 89  ? 48.517 -9.852  35.047  1.00 12.52 ?  530  ASN   B O   1 
ATOM   3623 C  CB  . ASN   B 1 89  ? 48.918 -9.276  37.862  1.00 15.10 ?  530  ASN   B CB  1 
ATOM   3624 C  CG  . ASN   B 1 89  ? 48.058 -8.015  37.963  1.00 16.39 ?  530  ASN   B CG  1 
ATOM   3625 O  OD1 . ASN   B 1 89  ? 46.926 -7.952  37.458  1.00 16.28 ?  530  ASN   B OD1 1 
ATOM   3626 N  ND2 . ASN   B 1 89  ? 48.600 -6.998  38.626  1.00 18.44 ?  530  ASN   B ND2 1 
ATOM   3627 N  N   . SER   B 1 90  ? 46.434 -10.523 35.609  1.00 11.51 ?  531  SER   B N   1 
ATOM   3628 C  CA  . SER   B 1 90  ? 45.793 -10.131 34.352  1.00 12.25 ?  531  SER   B CA  1 
ATOM   3629 C  C   . SER   B 1 90  ? 46.401 -10.852 33.139  1.00 11.81 ?  531  SER   B C   1 
ATOM   3630 O  O   . SER   B 1 90  ? 46.906 -10.224 32.205  1.00 12.35 ?  531  SER   B O   1 
ATOM   3631 C  CB  . SER   B 1 90  ? 45.816 -8.603  34.170  1.00 14.43 ?  531  SER   B CB  1 
ATOM   3632 O  OG  . SER   B 1 90  ? 45.215 -7.934  35.276  1.00 16.44 ?  531  SER   B OG  1 
ATOM   3633 N  N   . ILE   B 1 91  ? 46.317 -12.188 33.147  1.00 10.66 ?  532  ILE   B N   1 
ATOM   3634 C  CA  . ILE   B 1 91  ? 46.762 -13.035 32.047  1.00 10.54 ?  532  ILE   B CA  1 
ATOM   3635 C  C   . ILE   B 1 91  ? 45.683 -14.069 31.734  1.00 12.50 ?  532  ILE   B C   1 
ATOM   3636 O  O   . ILE   B 1 91  ? 45.136 -14.709 32.642  1.00 12.86 ?  532  ILE   B O   1 
ATOM   3637 C  CB  . ILE   B 1 91  ? 48.075 -13.752 32.427  1.00 10.41 ?  532  ILE   B CB  1 
ATOM   3638 C  CG1 . ILE   B 1 91  ? 49.248 -12.772 32.453  1.00 11.48 ?  532  ILE   B CG1 1 
ATOM   3639 C  CG2 . ILE   B 1 91  ? 48.347 -14.938 31.502  1.00 11.07 ?  532  ILE   B CG2 1 
ATOM   3640 C  CD1 . ILE   B 1 91  ? 49.720 -12.363 31.070  1.00 10.78 ?  532  ILE   B CD1 1 
ATOM   3641 N  N   . PHE   B 1 92  ? 45.399 -14.251 30.442  1.00 12.33 ?  533  PHE   B N   1 
ATOM   3642 C  CA  . PHE   B 1 92  ? 44.715 -15.430 29.934  1.00 11.76 ?  533  PHE   B CA  1 
ATOM   3643 C  C   . PHE   B 1 92  ? 45.647 -16.193 29.000  1.00 11.18 ?  533  PHE   B C   1 
ATOM   3644 O  O   . PHE   B 1 92  ? 46.508 -15.604 28.333  1.00 11.28 ?  533  PHE   B O   1 
ATOM   3645 C  CB  . PHE   B 1 92  ? 43.389 -15.086 29.217  1.00 11.83 ?  533  PHE   B CB  1 
ATOM   3646 C  CG  . PHE   B 1 92  ? 43.566 -14.215 27.994  1.00 10.59 ?  533  PHE   B CG  1 
ATOM   3647 C  CD1 . PHE   B 1 92  ? 43.809 -14.776 26.740  1.00 12.70 ?  533  PHE   B CD1 1 
ATOM   3648 C  CD2 . PHE   B 1 92  ? 43.504 -12.838 28.106  1.00 11.99 ?  533  PHE   B CD2 1 
ATOM   3649 C  CE1 . PHE   B 1 92  ? 43.989 -13.974 25.617  1.00 12.25 ?  533  PHE   B CE1 1 
ATOM   3650 C  CE2 . PHE   B 1 92  ? 43.678 -12.027 26.985  1.00 13.79 ?  533  PHE   B CE2 1 
ATOM   3651 C  CZ  . PHE   B 1 92  ? 43.926 -12.597 25.740  1.00 14.32 ?  533  PHE   B CZ  1 
ATOM   3652 N  N   . ILE   B 1 93  ? 45.472 -17.515 28.952  1.00 11.90 ?  534  ILE   B N   1 
ATOM   3653 C  CA  . ILE   B 1 93  ? 46.350 -18.384 28.171  1.00 10.90 ?  534  ILE   B CA  1 
ATOM   3654 C  C   . ILE   B 1 93  ? 45.500 -19.380 27.394  1.00 11.54 ?  534  ILE   B C   1 
ATOM   3655 O  O   . ILE   B 1 93  ? 44.555 -19.964 27.937  1.00 12.50 ?  534  ILE   B O   1 
ATOM   3656 C  CB  . ILE   B 1 93  ? 47.374 -19.136 29.053  1.00 11.48 ?  534  ILE   B CB  1 
ATOM   3657 C  CG1 . ILE   B 1 93  ? 47.928 -18.224 30.145  1.00 11.91 ?  534  ILE   B CG1 1 
ATOM   3658 C  CG2 . ILE   B 1 93  ? 48.489 -19.727 28.177  1.00 12.20 ?  534  ILE   B CG2 1 
ATOM   3659 C  CD1 . ILE   B 1 93  ? 48.950 -18.899 31.065  1.00 12.93 ?  534  ILE   B CD1 1 
ATOM   3660 N  N   . SER   B 1 94  ? 45.840 -19.586 26.123  1.00 11.21 ?  535  SER   B N   1 
ATOM   3661 C  CA  . SER   B 1 94  ? 45.302 -20.688 25.340  1.00 12.55 ?  535  SER   B CA  1 
ATOM   3662 C  C   . SER   B 1 94  ? 46.469 -21.554 24.886  1.00 11.00 ?  535  SER   B C   1 
ATOM   3663 O  O   . SER   B 1 94  ? 47.638 -21.214 25.094  1.00 12.47 ?  535  SER   B O   1 
ATOM   3664 C  CB  . SER   B 1 94  ? 44.504 -20.190 24.126  1.00 12.84 ?  535  SER   B CB  1 
ATOM   3665 O  OG  . SER   B 1 94  ? 45.306 -19.453 23.210  1.00 13.23 ?  535  SER   B OG  1 
ATOM   3666 N  N   . ASN   B 1 95  ? 46.153 -22.670 24.222  1.00 12.79 ?  536  ASN   B N   1 
ATOM   3667 C  CA  . ASN   B 1 95  ? 47.223 -23.531 23.728  1.00 14.44 ?  536  ASN   B CA  1 
ATOM   3668 C  C   . ASN   B 1 95  ? 48.059 -22.876 22.640  1.00 13.64 ?  536  ASN   B C   1 
ATOM   3669 O  O   . ASN   B 1 95  ? 49.117 -23.412 22.300  1.00 15.57 ?  536  ASN   B O   1 
ATOM   3670 C  CB  . ASN   B 1 95  ? 46.683 -24.853 23.176  1.00 15.78 ?  536  ASN   B CB  1 
ATOM   3671 C  CG  . ASN   B 1 95  ? 46.160 -25.782 24.263  1.00 19.83 ?  536  ASN   B CG  1 
ATOM   3672 O  OD1 . ASN   B 1 95  ? 45.086 -26.358 24.119  1.00 23.80 ?  536  ASN   B OD1 1 
ATOM   3673 N  ND2 . ASN   B 1 95  ? 46.916 -25.938 25.347  1.00 19.64 ?  536  ASN   B ND2 1 
ATOM   3674 N  N   . GLU   B 1 96  ? 47.613 -21.758 22.079  1.00 12.24 ?  537  GLU   B N   1 
ATOM   3675 C  CA  . GLU   B 1 96  ? 48.347 -21.053 21.035  1.00 11.76 ?  537  GLU   B CA  1 
ATOM   3676 C  C   . GLU   B 1 96  ? 49.185 -19.885 21.559  1.00 12.45 ?  537  GLU   B C   1 
ATOM   3677 O  O   . GLU   B 1 96  ? 49.952 -19.296 20.796  1.00 13.31 ?  537  GLU   B O   1 
ATOM   3678 C  CB  . GLU   B 1 96  ? 47.370 -20.525 19.971  1.00 14.34 ?  537  GLU   B CB  1 
ATOM   3679 C  CG  . GLU   B 1 96  ? 46.477 -21.603 19.348  1.00 16.84 ?  537  GLU   B CG  1 
ATOM   3680 C  CD  . GLU   B 1 96  ? 45.124 -21.774 20.038  1.00 22.12 ?  537  GLU   B CD  1 
ATOM   3681 O  OE1 . GLU   B 1 96  ? 44.919 -21.261 21.159  1.00 18.82 ?  537  GLU   B OE1 1 
ATOM   3682 O  OE2 . GLU   B 1 96  ? 44.247 -22.433 19.442  1.00 28.70 -1 537  GLU   B OE2 1 
ATOM   3683 N  N   . SER   B 1 97  ? 49.069 -19.540 22.838  1.00 11.71 ?  538  SER   B N   1 
ATOM   3684 C  CA  . SER   B 1 97  ? 49.637 -18.288 23.338  1.00 10.65 ?  538  SER   B CA  1 
ATOM   3685 C  C   . SER   B 1 97  ? 51.159 -18.266 23.267  1.00 10.97 ?  538  SER   B C   1 
ATOM   3686 O  O   . SER   B 1 97  ? 51.746 -17.252 22.876  1.00 11.66 ?  538  SER   B O   1 
ATOM   3687 C  CB  . SER   B 1 97  ? 49.223 -18.063 24.791  1.00 10.71 ?  538  SER   B CB  1 
ATOM   3688 O  OG  . SER   B 1 97  ? 47.821 -18.076 24.946  1.00 11.25 ?  538  SER   B OG  1 
ATOM   3689 N  N   . TYR   B 1 98  ? 51.818 -19.335 23.732  1.00 11.67 ?  539  TYR   B N   1 
ATOM   3690 C  CA  . TYR   B 1 98  ? 53.276 -19.375 23.714  1.00 11.66 ?  539  TYR   B CA  1 
ATOM   3691 C  C   . TYR   B 1 98  ? 53.815 -19.099 22.322  1.00 11.51 ?  539  TYR   B C   1 
ATOM   3692 O  O   . TYR   B 1 98  ? 54.666 -18.226 22.129  1.00 12.04 ?  539  TYR   B O   1 
ATOM   3693 C  CB  . TYR   B 1 98  ? 53.746 -20.747 24.196  1.00 12.25 ?  539  TYR   B CB  1 
ATOM   3694 C  CG  . TYR   B 1 98  ? 55.223 -21.004 24.057  1.00 12.78 ?  539  TYR   B CG  1 
ATOM   3695 C  CD1 . TYR   B 1 98  ? 56.139 -20.270 24.784  1.00 12.08 ?  539  TYR   B CD1 1 
ATOM   3696 C  CD2 . TYR   B 1 98  ? 55.693 -22.009 23.226  1.00 12.26 ?  539  TYR   B CD2 1 
ATOM   3697 C  CE1 . TYR   B 1 98  ? 57.489 -20.514 24.682  1.00 12.23 ?  539  TYR   B CE1 1 
ATOM   3698 C  CE2 . TYR   B 1 98  ? 57.048 -22.261 23.111  1.00 12.75 ?  539  TYR   B CE2 1 
ATOM   3699 C  CZ  . TYR   B 1 98  ? 57.938 -21.508 23.847  1.00 12.55 ?  539  TYR   B CZ  1 
ATOM   3700 O  OH  . TYR   B 1 98  ? 59.296 -21.733 23.775  1.00 15.31 ?  539  TYR   B OH  1 
ATOM   3701 N  N   . THR   B 1 99  ? 53.317 -19.829 21.333  1.00 11.53 ?  540  THR   B N   1 
ATOM   3702 C  CA  . THR   B 1 99  ? 53.845 -19.660 19.986  1.00 11.92 ?  540  THR   B CA  1 
ATOM   3703 C  C   . THR   B 1 99  ? 53.549 -18.259 19.456  1.00 11.27 ?  540  THR   B C   1 
ATOM   3704 O  O   . THR   B 1 99  ? 54.370 -17.666 18.748  1.00 11.39 ?  540  THR   B O   1 
ATOM   3705 C  CB  . THR   B 1 99  ? 53.284 -20.760 19.083  1.00 14.10 ?  540  THR   B CB  1 
ATOM   3706 O  OG1 . THR   B 1 99  ? 53.690 -22.034 19.614  1.00 17.62 ?  540  THR   B OG1 1 
ATOM   3707 C  CG2 . THR   B 1 99  ? 53.782 -20.612 17.654  1.00 12.64 ?  540  THR   B CG2 1 
ATOM   3708 N  N   . CYS   B 1 100 ? 52.378 -17.702 19.793  1.00 10.32 ?  541  CYS   B N   1 
ATOM   3709 C  CA  . CYS   B 1 100 ? 52.083 -16.338 19.366  1.00 12.30 ?  541  CYS   B CA  1 
ATOM   3710 C  C   . CYS   B 1 100 ? 53.078 -15.356 19.967  1.00 10.90 ?  541  CYS   B C   1 
ATOM   3711 O  O   . CYS   B 1 100 ? 53.548 -14.436 19.285  1.00 10.57 ?  541  CYS   B O   1 
ATOM   3712 C  CB  . CYS   B 1 100 ? 50.662 -15.951 19.761  1.00 12.07 ?  541  CYS   B CB  1 
ATOM   3713 S  SG  . CYS   B 1 100 ? 49.389 -16.694 18.724  1.00 15.46 ?  541  CYS   B SG  1 
ATOM   3714 N  N   . ALA   B 1 101 ? 53.427 -15.554 21.241  1.00 10.28 ?  542  ALA   B N   1 
ATOM   3715 C  CA  . ALA   B 1 101 ? 54.413 -14.693 21.881  1.00 9.96  ?  542  ALA   B CA  1 
ATOM   3716 C  C   . ALA   B 1 101 ? 55.783 -14.834 21.227  1.00 9.86  ?  542  ALA   B C   1 
ATOM   3717 O  O   . ALA   B 1 101 ? 56.488 -13.835 21.044  1.00 11.14 ?  542  ALA   B O   1 
ATOM   3718 C  CB  . ALA   B 1 101 ? 54.479 -14.985 23.380  1.00 10.26 ?  542  ALA   B CB  1 
ATOM   3719 N  N   . LEU   B 1 102 ? 56.160 -16.058 20.844  1.00 9.98  ?  543  LEU   B N   1 
ATOM   3720 C  CA  . LEU   B 1 102 ? 57.396 -16.256 20.084  1.00 10.54 ?  543  LEU   B CA  1 
ATOM   3721 C  C   . LEU   B 1 102 ? 57.346 -15.528 18.745  1.00 9.98  ?  543  LEU   B C   1 
ATOM   3722 O  O   . LEU   B 1 102 ? 58.353 -14.960 18.297  1.00 10.65 ?  543  LEU   B O   1 
ATOM   3723 C  CB  . LEU   B 1 102 ? 57.628 -17.746 19.824  1.00 11.20 ?  543  LEU   B CB  1 
ATOM   3724 C  CG  . LEU   B 1 102 ? 57.911 -18.689 20.978  1.00 13.09 ?  543  LEU   B CG  1 
ATOM   3725 C  CD1 . LEU   B 1 102 ? 58.194 -20.079 20.437  1.00 13.84 ?  543  LEU   B CD1 1 
ATOM   3726 C  CD2 . LEU   B 1 102 ? 59.082 -18.177 21.781  1.00 14.51 ?  543  LEU   B CD2 1 
ATOM   3727 N  N   . LEU   B 1 103 ? 56.189 -15.558 18.077  1.00 9.36  ?  544  LEU   B N   1 
ATOM   3728 C  CA  . LEU   B 1 103 ? 56.069 -14.935 16.763  1.00 8.94  ?  544  LEU   B CA  1 
ATOM   3729 C  C   . LEU   B 1 103 ? 56.144 -13.415 16.861  1.00 9.63  ?  544  LEU   B C   1 
ATOM   3730 O  O   . LEU   B 1 103 ? 56.729 -12.754 15.989  1.00 11.51 ?  544  LEU   B O   1 
ATOM   3731 C  CB  . LEU   B 1 103 ? 54.760 -15.388 16.111  1.00 10.80 ?  544  LEU   B CB  1 
ATOM   3732 C  CG  . LEU   B 1 103 ? 54.419 -15.039 14.666  1.00 12.43 ?  544  LEU   B CG  1 
ATOM   3733 C  CD1 . LEU   B 1 103 ? 55.566 -15.431 13.747  1.00 12.52 ?  544  LEU   B CD1 1 
ATOM   3734 C  CD2 . LEU   B 1 103 ? 53.149 -15.800 14.276  1.00 13.59 ?  544  LEU   B CD2 1 
ATOM   3735 N  N   . ALA   B 1 104 ? 55.564 -12.841 17.922  1.00 10.12 ?  545  ALA   B N   1 
ATOM   3736 C  CA  . ALA   B 1 104 ? 55.673 -11.402 18.134  1.00 10.91 ?  545  ALA   B CA  1 
ATOM   3737 C  C   . ALA   B 1 104 ? 57.132 -10.996 18.302  1.00 10.58 ?  545  ALA   B C   1 
ATOM   3738 O  O   . ALA   B 1 104 ? 57.605 -10.057 17.650  1.00 11.61 ?  545  ALA   B O   1 
ATOM   3739 C  CB  . ALA   B 1 104 ? 54.848 -10.991 19.356  1.00 11.86 ?  545  ALA   B CB  1 
ATOM   3740 N  N   . ALA   B 1 105 ? 57.877 -11.742 19.125  1.00 10.79 ?  546  ALA   B N   1 
ATOM   3741 C  CA  . ALA   B 1 105 ? 59.282 -11.418 19.372  1.00 10.64 ?  546  ALA   B CA  1 
ATOM   3742 C  C   . ALA   B 1 105 ? 60.137 -11.632 18.124  1.00 11.31 ?  546  ALA   B C   1 
ATOM   3743 O  O   . ALA   B 1 105 ? 60.927 -10.759 17.752  1.00 11.37 ?  546  ALA   B O   1 
ATOM   3744 C  CB  . ALA   B 1 105 ? 59.817 -12.247 20.541  1.00 11.83 ?  546  ALA   B CB  1 
ATOM   3745 N  N   . GLY   B 1 106 ? 60.005 -12.795 17.473  1.00 11.28 ?  547  GLY   B N   1 
ATOM   3746 C  CA  . GLY   B 1 106 ? 60.834 -13.077 16.305  1.00 11.12 ?  547  GLY   B CA  1 
ATOM   3747 C  C   . GLY   B 1 106 ? 60.588 -12.101 15.169  1.00 10.84 ?  547  GLY   B C   1 
ATOM   3748 O  O   . GLY   B 1 106 ? 61.508 -11.749 14.422  1.00 13.54 ?  547  GLY   B O   1 
ATOM   3749 N  N   . SER   B 1 107 ? 59.338 -11.675 15.001  1.00 10.89 ?  548  SER   B N   1 
ATOM   3750 C  CA  . SER   B 1 107 ? 59.023 -10.648 14.010  1.00 11.22 ?  548  SER   B CA  1 
ATOM   3751 C  C   . SER   B 1 107 ? 59.789 -9.368  14.300  1.00 9.40  ?  548  SER   B C   1 
ATOM   3752 O  O   . SER   B 1 107 ? 60.329 -8.716  13.390  1.00 12.09 ?  548  SER   B O   1 
ATOM   3753 C  CB  . SER   B 1 107 ? 57.521 -10.352 14.007  1.00 13.98 ?  548  SER   B CB  1 
ATOM   3754 O  OG  . SER   B 1 107 ? 56.741 -11.495 13.679  1.00 15.22 ?  548  SER   B OG  1 
ATOM   3755 N  N   . CYS   B 1 108 ? 59.865 -9.006  15.575  1.00 9.84  ?  549  CYS   B N   1 
ATOM   3756 C  CA  . CYS   B 1 108 ? 60.564 -7.791  15.950  1.00 10.12 ?  549  CYS   B CA  1 
ATOM   3757 C  C   . CYS   B 1 108 ? 62.070 -7.960  15.782  1.00 11.91 ?  549  CYS   B C   1 
ATOM   3758 O  O   . CYS   B 1 108 ? 62.757 -7.023  15.364  1.00 12.30 ?  549  CYS   B O   1 
ATOM   3759 C  CB  . CYS   B 1 108 ? 60.207 -7.456  17.395  1.00 11.31 ?  549  CYS   B CB  1 
ATOM   3760 S  SG  . CYS   B 1 108 ? 58.554 -6.706  17.496  1.00 12.47 ?  549  CYS   B SG  1 
ATOM   3761 N  N   . PHE   B 1 109 ? 62.594 -9.160  16.054  1.00 10.80 ?  550  PHE   B N   1 
ATOM   3762 C  CA  . PHE   B 1 109 ? 64.022 -9.401  15.842  1.00 11.32 ?  550  PHE   B CA  1 
ATOM   3763 C  C   . PHE   B 1 109 ? 64.377 -9.235  14.370  1.00 11.82 ?  550  PHE   B C   1 
ATOM   3764 O  O   . PHE   B 1 109 ? 65.373 -8.586  14.020  1.00 12.99 ?  550  PHE   B O   1 
ATOM   3765 C  CB  . PHE   B 1 109 ? 64.416 -10.815 16.284  1.00 11.81 ?  550  PHE   B CB  1 
ATOM   3766 C  CG  . PHE   B 1 109 ? 64.158 -11.124 17.723  1.00 10.94 ?  550  PHE   B CG  1 
ATOM   3767 C  CD1 . PHE   B 1 109 ? 63.924 -10.128 18.655  1.00 11.18 ?  550  PHE   B CD1 1 
ATOM   3768 C  CD2 . PHE   B 1 109 ? 64.161 -12.443 18.147  1.00 12.91 ?  550  PHE   B CD2 1 
ATOM   3769 C  CE1 . PHE   B 1 109 ? 63.673 -10.446 19.983  1.00 12.46 ?  550  PHE   B CE1 1 
ATOM   3770 C  CE2 . PHE   B 1 109 ? 63.931 -12.767 19.462  1.00 13.09 ?  550  PHE   B CE2 1 
ATOM   3771 C  CZ  . PHE   B 1 109 ? 63.681 -11.770 20.384  1.00 11.74 ?  550  PHE   B CZ  1 
ATOM   3772 N  N   . ASN   B 1 110 ? 63.565 -9.818  13.485  1.00 10.30 ?  551  ASN   B N   1 
ATOM   3773 C  CA  . ASN   B 1 110 ? 63.849 -9.698  12.058  1.00 12.15 ?  551  ASN   B CA  1 
ATOM   3774 C  C   . ASN   B 1 110 ? 63.796 -8.245  11.618  1.00 14.31 ?  551  ASN   B C   1 
ATOM   3775 O  O   . ASN   B 1 110 ? 64.563 -7.820  10.748  1.00 14.55 ?  551  ASN   B O   1 
ATOM   3776 C  CB  . ASN   B 1 110 ? 62.856 -10.513 11.228  1.00 11.84 ?  551  ASN   B CB  1 
ATOM   3777 C  CG  . ASN   B 1 110 ? 63.265 -11.955 11.080  1.00 12.81 ?  551  ASN   B CG  1 
ATOM   3778 O  OD1 . ASN   B 1 110 ? 64.291 -12.383 11.614  1.00 13.65 ?  551  ASN   B OD1 1 
ATOM   3779 N  ND2 . ASN   B 1 110 ? 62.458 -12.725 10.349  1.00 13.21 ?  551  ASN   B ND2 1 
ATOM   3780 N  N   . SER   B 1 111 ? 62.882 -7.468  12.201  1.00 11.79 ?  552  SER   B N   1 
ATOM   3781 C  CA  . SER   B 1 111 ? 62.765 -6.063  11.846  1.00 11.79 ?  552  SER   B CA  1 
ATOM   3782 C  C   . SER   B 1 111 ? 63.999 -5.298  12.314  1.00 13.06 ?  552  SER   B C   1 
ATOM   3783 O  O   . SER   B 1 111 ? 64.559 -4.490  11.564  1.00 13.07 ?  552  SER   B O   1 
ATOM   3784 C  CB  . SER   B 1 111 ? 61.507 -5.500  12.515  1.00 13.61 ?  552  SER   B CB  1 
ATOM   3785 O  OG  . SER   B 1 111 ? 60.338 -6.078  11.960  1.00 13.09 ?  552  SER   B OG  1 
ATOM   3786 N  N   . ALA   B 1 112 ? 64.452 -5.563  13.539  1.00 12.58 ?  553  ALA   B N   1 
ATOM   3787 C  CA  . ALA   B 1 112 ? 65.662 -4.915  14.039  1.00 12.70 ?  553  ALA   B CA  1 
ATOM   3788 C  C   . ALA   B 1 112 ? 66.873 -5.289  13.197  1.00 12.48 ?  553  ALA   B C   1 
ATOM   3789 O  O   . ALA   B 1 112 ? 67.723 -4.435  12.915  1.00 13.74 ?  553  ALA   B O   1 
ATOM   3790 C  CB  . ALA   B 1 112 ? 65.901 -5.305  15.495  1.00 12.90 ?  553  ALA   B CB  1 
ATOM   3791 N  N   . GLN   B 1 113 ? 66.994 -6.571  12.830  1.00 12.87 ?  554  GLN   B N   1 
ATOM   3792 C  CA  . GLN   B 1 113 ? 68.098 -7.008  11.977  1.00 14.51 ?  554  GLN   B CA  1 
ATOM   3793 C  C   . GLN   B 1 113 ? 68.089 -6.267  10.642  1.00 14.67 ?  554  GLN   B C   1 
ATOM   3794 O  O   . GLN   B 1 113 ? 69.142 -5.833  10.151  1.00 14.86 ?  554  GLN   B O   1 
ATOM   3795 C  CB  . GLN   B 1 113 ? 68.005 -8.520  11.774  1.00 15.17 ?  554  GLN   B CB  1 
ATOM   3796 C  CG  . GLN   B 1 113 ? 69.136 -9.161  10.969  1.00 18.12 ?  554  GLN   B CG  1 
ATOM   3797 C  CD  . GLN   B 1 113 ? 68.895 -10.647 10.775  1.00 23.92 ?  554  GLN   B CD  1 
ATOM   3798 O  OE1 . GLN   B 1 113 ? 67.800 -11.064 10.383  1.00 26.76 ?  554  GLN   B OE1 1 
ATOM   3799 N  NE2 . GLN   B 1 113 ? 69.903 -11.455 11.068  1.00 25.80 ?  554  GLN   B NE2 1 
ATOM   3800 N  N   . ALA   B 1 114 ? 66.904 -6.086  10.052  1.00 11.47 ?  555  ALA   B N   1 
ATOM   3801 C  CA  . ALA   B 1 114 ? 66.799 -5.361  8.790   1.00 12.91 ?  555  ALA   B CA  1 
ATOM   3802 C  C   . ALA   B 1 114 ? 67.251 -3.913  8.947   1.00 13.24 ?  555  ALA   B C   1 
ATOM   3803 O  O   . ALA   B 1 114 ? 67.872 -3.344  8.039   1.00 15.21 ?  555  ALA   B O   1 
ATOM   3804 C  CB  . ALA   B 1 114 ? 65.374 -5.456  8.240   1.00 13.57 ?  555  ALA   B CB  1 
ATOM   3805 N  N   . ILE   B 1 115 ? 66.971 -3.307  10.105  1.00 13.90 ?  556  ILE   B N   1 
ATOM   3806 C  CA  . ILE   B 1 115 ? 67.400 -1.933  10.344  1.00 15.24 ?  556  ILE   B CA  1 
ATOM   3807 C  C   . ILE   B 1 115 ? 68.907 -1.871  10.547  1.00 14.67 ?  556  ILE   B C   1 
ATOM   3808 O  O   . ILE   B 1 115 ? 69.591 -1.016  9.968   1.00 17.13 ?  556  ILE   B O   1 
ATOM   3809 C  CB  . ILE   B 1 115 ? 66.638 -1.345  11.545  1.00 13.06 ?  556  ILE   B CB  1 
ATOM   3810 C  CG1 . ILE   B 1 115 ? 65.173 -1.137  11.208  1.00 12.97 ?  556  ILE   B CG1 1 
ATOM   3811 C  CG2 . ILE   B 1 115 ? 67.256 -0.022  11.985  1.00 16.26 ?  556  ILE   B CG2 1 
ATOM   3812 C  CD1 . ILE   B 1 115 ? 64.310 -0.831  12.439  1.00 14.57 ?  556  ILE   B CD1 1 
ATOM   3813 N  N   . LEU   B 1 116 ? 69.448 -2.791  11.345  1.00 13.91 ?  557  LEU   B N   1 
ATOM   3814 C  CA  . LEU   B 1 116 ? 70.852 -2.739  11.751  1.00 14.95 ?  557  LEU   B CA  1 
ATOM   3815 C  C   . LEU   B 1 116 ? 71.815 -3.174  10.654  1.00 21.54 ?  557  LEU   B C   1 
ATOM   3816 O  O   . LEU   B 1 116 ? 72.989 -2.783  10.693  1.00 24.66 ?  557  LEU   B O   1 
ATOM   3817 C  CB  . LEU   B 1 116 ? 71.081 -3.586  13.002  1.00 14.89 ?  557  LEU   B CB  1 
ATOM   3818 C  CG  . LEU   B 1 116 ? 70.389 -3.003  14.235  1.00 13.82 ?  557  LEU   B CG  1 
ATOM   3819 C  CD1 . LEU   B 1 116 ? 70.401 -4.023  15.331  1.00 14.75 ?  557  LEU   B CD1 1 
ATOM   3820 C  CD2 . LEU   B 1 116 ? 71.034 -1.691  14.680  1.00 16.09 ?  557  LEU   B CD2 1 
ATOM   3821 N  N   . THR   B 1 117 ? 71.364 -3.976  9.696   1.00 19.88 ?  558  THR   B N   1 
ATOM   3822 C  CA  . THR   B 1 117 ? 72.182 -4.328  8.544   1.00 20.69 ?  558  THR   B CA  1 
ATOM   3823 C  C   . THR   B 1 117 ? 71.932 -3.411  7.358   1.00 20.40 ?  558  THR   B C   1 
ATOM   3824 O  O   . THR   B 1 117 ? 72.507 -3.635  6.282   1.00 21.58 ?  558  THR   B O   1 
ATOM   3825 C  CB  . THR   B 1 117 ? 71.917 -5.774  8.130   1.00 20.94 ?  558  THR   B CB  1 
ATOM   3826 O  OG1 . THR   B 1 117 ? 70.548 -5.897  7.718   1.00 21.72 ?  558  THR   B OG1 1 
ATOM   3827 C  CG2 . THR   B 1 117 ? 72.230 -6.747  9.267   1.00 22.50 ?  558  THR   B CG2 1 
ATOM   3828 N  N   . GLY   B 1 118 ? 71.068 -2.411  7.512   1.00 20.99 ?  559  GLY   B N   1 
ATOM   3829 C  CA  . GLY   B 1 118 ? 70.845 -1.415  6.486   1.00 22.96 ?  559  GLY   B CA  1 
ATOM   3830 C  C   . GLY   B 1 118 ? 69.898 -1.796  5.369   1.00 23.88 ?  559  GLY   B C   1 
ATOM   3831 O  O   . GLY   B 1 118 ? 69.899 -1.129  4.330   1.00 27.94 ?  559  GLY   B O   1 
ATOM   3832 N  N   . GLN   B 1 119 ? 69.081 -2.840  5.538   1.00 18.70 ?  560  GLN   B N   1 
ATOM   3833 C  CA  . GLN   B 1 119 ? 68.126 -3.212  4.495   1.00 17.43 ?  560  GLN   B CA  1 
ATOM   3834 C  C   . GLN   B 1 119 ? 66.901 -2.308  4.486   1.00 18.50 ?  560  GLN   B C   1 
ATOM   3835 O  O   . GLN   B 1 119 ? 66.273 -2.124  3.433   1.00 20.23 ?  560  GLN   B O   1 
ATOM   3836 C  CB  . GLN   B 1 119 ? 67.695 -4.668  4.658   1.00 17.99 ?  560  GLN   B CB  1 
ATOM   3837 C  CG  . GLN   B 1 119 ? 68.844 -5.670  4.589   0.99 20.22 ?  560  GLN   B CG  1 
ATOM   3838 C  CD  . GLN   B 1 119 ? 68.448 -7.040  5.104   0.95 22.79 ?  560  GLN   B CD  1 
ATOM   3839 O  OE1 . GLN   B 1 119 ? 69.151 -7.635  5.923   0.34 23.52 ?  560  GLN   B OE1 1 
ATOM   3840 N  NE2 . GLN   B 1 119 ? 67.315 -7.546  4.631   0.69 21.98 ?  560  GLN   B NE2 1 
ATOM   3841 N  N   . VAL   B 1 120 ? 66.532 -1.766  5.649   1.00 18.26 ?  561  VAL   B N   1 
ATOM   3842 C  CA  . VAL   B 1 120 ? 65.479 -0.769  5.765   1.00 16.74 ?  561  VAL   B CA  1 
ATOM   3843 C  C   . VAL   B 1 120 ? 65.976 0.343   6.681   1.00 12.75 ?  561  VAL   B C   1 
ATOM   3844 O  O   . VAL   B 1 120 ? 66.891 0.156   7.482   1.00 15.86 ?  561  VAL   B O   1 
ATOM   3845 C  CB  . VAL   B 1 120 ? 64.150 -1.355  6.310   1.00 15.44 ?  561  VAL   B CB  1 
ATOM   3846 C  CG1 . VAL   B 1 120 ? 63.668 -2.545  5.479   1.00 17.30 ?  561  VAL   B CG1 1 
ATOM   3847 C  CG2 . VAL   B 1 120 ? 64.288 -1.734  7.795   1.00 15.42 ?  561  VAL   B CG2 1 
ATOM   3848 N  N   . ARG   B 1 121 ? 65.353 1.513   6.544   1.00 14.39 ?  562  ARG   B N   1 
ATOM   3849 C  CA  . ARG   B 1 121 ? 65.662 2.630   7.433   1.00 15.53 ?  562  ARG   B CA  1 
ATOM   3850 C  C   . ARG   B 1 121 ? 64.950 2.489   8.777   1.00 13.93 ?  562  ARG   B C   1 
ATOM   3851 O  O   . ARG   B 1 121 ? 65.560 2.675   9.837   1.00 15.38 ?  562  ARG   B O   1 
ATOM   3852 C  CB  . ARG   B 1 121 ? 65.261 3.945   6.766   1.00 17.34 ?  562  ARG   B CB  1 
ATOM   3853 C  CG  . ARG   B 1 121 ? 65.571 5.206   7.583   1.00 24.61 ?  562  ARG   B CG  1 
ATOM   3854 C  CD  . ARG   B 1 121 ? 66.957 5.158   8.218   1.00 29.59 ?  562  ARG   B CD  1 
ATOM   3855 N  NE  . ARG   B 1 121 ? 68.009 5.477   7.254   1.00 34.16 ?  562  ARG   B NE  1 
ATOM   3856 C  CZ  . ARG   B 1 121 ? 69.176 4.840   7.189   1.00 35.85 ?  562  ARG   B CZ  1 
ATOM   3857 N  NH1 . ARG   B 1 121 ? 69.439 3.846   8.031   1.00 37.30 ?  562  ARG   B NH1 1 
ATOM   3858 N  NH2 . ARG   B 1 121 ? 70.082 5.195   6.284   1.00 33.73 ?  562  ARG   B NH2 1 
ATOM   3859 N  N   . ASN   B 1 122 ? 63.661 2.158   8.741   1.00 11.81 ?  563  ASN   B N   1 
ATOM   3860 C  CA  . ASN   B 1 122 ? 62.808 2.096   9.918   1.00 11.20 ?  563  ASN   B CA  1 
ATOM   3861 C  C   . ASN   B 1 122 ? 61.775 1.001   9.664   1.00 12.12 ?  563  ASN   B C   1 
ATOM   3862 O  O   . ASN   B 1 122 ? 61.732 0.406   8.579   1.00 12.23 ?  563  ASN   B O   1 
ATOM   3863 C  CB  . ASN   B 1 122 ? 62.205 3.479   10.194  1.00 13.08 ?  563  ASN   B CB  1 
ATOM   3864 C  CG  . ASN   B 1 122 ? 61.473 4.049   8.997   1.00 11.75 ?  563  ASN   B CG  1 
ATOM   3865 O  OD1 . ASN   B 1 122 ? 60.820 3.318   8.260   1.00 13.13 ?  563  ASN   B OD1 1 
ATOM   3866 N  ND2 . ASN   B 1 122 ? 61.558 5.368   8.814   1.00 13.83 ?  563  ASN   B ND2 1 
ATOM   3867 N  N   . ALA   B 1 123 ? 60.935 0.722   10.664  1.00 11.30 ?  564  ALA   B N   1 
ATOM   3868 C  CA  . ALA   B 1 123 ? 59.997 -0.376  10.498  1.00 10.75 ?  564  ALA   B CA  1 
ATOM   3869 C  C   . ALA   B 1 123 ? 58.890 -0.289  11.530  1.00 10.03 ?  564  ALA   B C   1 
ATOM   3870 O  O   . ALA   B 1 123 ? 59.032 0.348   12.584  1.00 10.91 ?  564  ALA   B O   1 
ATOM   3871 C  CB  . ALA   B 1 123 ? 60.686 -1.741  10.595  1.00 12.20 ?  564  ALA   B CB  1 
ATOM   3872 N  N   A VAL   B 1 124 ? 57.795 -0.979  11.231  0.89 10.61 ?  565  VAL   B N   1 
ATOM   3873 N  N   B VAL   B 1 124 ? 57.775 -0.939  11.201  0.11 10.28 ?  565  VAL   B N   1 
ATOM   3874 C  CA  A VAL   B 1 124 ? 56.651 -1.086  12.128  0.89 10.60 ?  565  VAL   B CA  1 
ATOM   3875 C  CA  B VAL   B 1 124 ? 56.638 -1.128  12.090  0.11 10.59 ?  565  VAL   B CA  1 
ATOM   3876 C  C   A VAL   B 1 124 ? 56.300 -2.563  12.301  0.89 9.72  ?  565  VAL   B C   1 
ATOM   3877 C  C   B VAL   B 1 124 ? 56.504 -2.618  12.358  0.11 10.26 ?  565  VAL   B C   1 
ATOM   3878 O  O   A VAL   B 1 124 ? 56.321 -3.341  11.337  0.89 11.14 ?  565  VAL   B O   1 
ATOM   3879 O  O   B VAL   B 1 124 ? 56.853 -3.454  11.517  0.11 10.02 ?  565  VAL   B O   1 
ATOM   3880 C  CB  A VAL   B 1 124 ? 55.460 -0.242  11.623  0.89 10.64 ?  565  VAL   B CB  1 
ATOM   3881 C  CB  B VAL   B 1 124 ? 55.333 -0.583  11.468  0.11 11.35 ?  565  VAL   B CB  1 
ATOM   3882 C  CG1 A VAL   B 1 124 ? 54.934 -0.784  10.278  0.89 12.20 ?  565  VAL   B CG1 1 
ATOM   3883 C  CG1 B VAL   B 1 124 ? 54.221 -0.509  12.502  0.11 11.46 ?  565  VAL   B CG1 1 
ATOM   3884 C  CG2 A VAL   B 1 124 ? 54.344 -0.166  12.648  0.89 11.68 ?  565  VAL   B CG2 1 
ATOM   3885 C  CG2 B VAL   B 1 124 ? 55.570 0.765   10.845  0.11 11.48 ?  565  VAL   B CG2 1 
ATOM   3886 N  N   . ALA   B 1 125 ? 55.992 -2.951  13.538  1.00 11.06 ?  566  ALA   B N   1 
ATOM   3887 C  CA  . ALA   B 1 125 ? 55.707 -4.336  13.895  1.00 10.25 ?  566  ALA   B CA  1 
ATOM   3888 C  C   . ALA   B 1 125 ? 54.305 -4.418  14.479  1.00 10.28 ?  566  ALA   B C   1 
ATOM   3889 O  O   . ALA   B 1 125 ? 54.049 -3.921  15.582  1.00 10.77 ?  566  ALA   B O   1 
ATOM   3890 C  CB  . ALA   B 1 125 ? 56.742 -4.900  14.867  1.00 9.90  ?  566  ALA   B CB  1 
ATOM   3891 N  N   . ILE   B 1 126 ? 53.399 -5.035  13.725  1.00 10.44 ?  567  ILE   B N   1 
ATOM   3892 C  CA  . ILE   B 1 126 ? 51.996 -5.202  14.132  1.00 10.19 ?  567  ILE   B CA  1 
ATOM   3893 C  C   . ILE   B 1 126 ? 51.905 -6.580  14.784  1.00 10.13 ?  567  ILE   B C   1 
ATOM   3894 O  O   . ILE   B 1 126 ? 51.668 -7.587  14.115  1.00 10.28 ?  567  ILE   B O   1 
ATOM   3895 C  CB  . ILE   B 1 126 ? 51.046 -5.050  12.944  1.00 10.21 ?  567  ILE   B CB  1 
ATOM   3896 C  CG1 . ILE   B 1 126 ? 51.298 -3.721  12.220  1.00 11.80 ?  567  ILE   B CG1 1 
ATOM   3897 C  CG2 . ILE   B 1 126 ? 49.612 -5.190  13.416  1.00 9.08  ?  567  ILE   B CG2 1 
ATOM   3898 C  CD1 . ILE   B 1 126 ? 50.631 -3.660  10.814  1.00 11.17 ?  567  ILE   B CD1 1 
ATOM   3899 N  N   . VAL   B 1 127 ? 52.076 -6.623  16.119  1.00 9.95  ?  568  VAL   B N   1 
ATOM   3900 C  CA  . VAL   B 1 127 ? 52.255 -7.865  16.868  1.00 9.63  ?  568  VAL   B CA  1 
ATOM   3901 C  C   . VAL   B 1 127 ? 51.366 -7.917  18.111  1.00 9.32  ?  568  VAL   B C   1 
ATOM   3902 O  O   . VAL   B 1 127 ? 51.021 -6.888  18.702  1.00 9.85  ?  568  VAL   B O   1 
ATOM   3903 C  CB  . VAL   B 1 127 ? 53.732 -8.078  17.275  1.00 10.25 ?  568  VAL   B CB  1 
ATOM   3904 C  CG1 . VAL   B 1 127 ? 54.614 -8.158  16.035  1.00 10.64 ?  568  VAL   B CG1 1 
ATOM   3905 C  CG2 . VAL   B 1 127 ? 54.218 -6.953  18.220  1.00 10.76 ?  568  VAL   B CG2 1 
ATOM   3906 N  N   . ARG   B 1 128 ? 51.000 -9.137  18.497  1.00 9.53  ?  569  ARG   B N   1 
ATOM   3907 C  CA  . ARG   B 1 128 ? 50.359 -9.435  19.772  1.00 9.12  ?  569  ARG   B CA  1 
ATOM   3908 C  C   . ARG   B 1 128 ? 50.713 -10.870 20.128  1.00 8.87  ?  569  ARG   B C   1 
ATOM   3909 O  O   . ARG   B 1 128 ? 51.098 -11.653 19.252  1.00 10.61 ?  569  ARG   B O   1 
ATOM   3910 C  CB  . ARG   B 1 128 ? 48.835 -9.250  19.704  1.00 9.23  ?  569  ARG   B CB  1 
ATOM   3911 C  CG  . ARG   B 1 128 ? 48.118 -10.339 18.918  1.00 9.86  ?  569  ARG   B CG  1 
ATOM   3912 C  CD  . ARG   B 1 128 ? 46.622 -10.067 18.909  1.00 9.90  ?  569  ARG   B CD  1 
ATOM   3913 N  NE  . ARG   B 1 128 ? 45.915 -10.439 20.144  1.00 10.55 ?  569  ARG   B NE  1 
ATOM   3914 C  CZ  . ARG   B 1 128 ? 45.459 -11.664 20.404  1.00 9.29  ?  569  ARG   B CZ  1 
ATOM   3915 N  NH1 . ARG   B 1 128 ? 45.701 -12.656 19.552  1.00 9.96  ?  569  ARG   B NH1 1 
ATOM   3916 N  NH2 . ARG   B 1 128 ? 44.759 -11.900 21.520  1.00 10.40 ?  569  ARG   B NH2 1 
ATOM   3917 N  N   . PRO   B 1 129 ? 50.629 -11.249 21.411  1.00 8.98  ?  570  PRO   B N   1 
ATOM   3918 C  CA  . PRO   B 1 129 ? 50.311 -10.447 22.599  1.00 9.78  ?  570  PRO   B CA  1 
ATOM   3919 C  C   . PRO   B 1 129 ? 51.394 -9.405  22.881  1.00 10.47 ?  570  PRO   B C   1 
ATOM   3920 O  O   . PRO   B 1 129 ? 52.514 -9.499  22.339  1.00 10.64 ?  570  PRO   B O   1 
ATOM   3921 C  CB  . PRO   B 1 129 ? 50.284 -11.489 23.732  1.00 9.92  ?  570  PRO   B CB  1 
ATOM   3922 C  CG  . PRO   B 1 129 ? 51.162 -12.587 23.247  1.00 11.29 ?  570  PRO   B CG  1 
ATOM   3923 C  CD  . PRO   B 1 129 ? 50.921 -12.651 21.764  1.00 9.60  ?  570  PRO   B CD  1 
ATOM   3924 N  N   . PRO   B 1 130 ? 51.054 -8.397  23.684  1.00 10.28 ?  571  PRO   B N   1 
ATOM   3925 C  CA  . PRO   B 1 130 ? 52.026 -7.343  23.999  1.00 9.65  ?  571  PRO   B CA  1 
ATOM   3926 C  C   . PRO   B 1 130 ? 53.123 -7.824  24.937  1.00 8.74  ?  571  PRO   B C   1 
ATOM   3927 O  O   . PRO   B 1 130 ? 53.142 -8.993  25.343  1.00 11.03 ?  571  PRO   B O   1 
ATOM   3928 C  CB  . PRO   B 1 130 ? 51.169 -6.256  24.655  1.00 9.96  ?  571  PRO   B CB  1 
ATOM   3929 C  CG  . PRO   B 1 130 ? 49.999 -7.009  25.227  1.00 9.83  ?  571  PRO   B CG  1 
ATOM   3930 C  CD  . PRO   B 1 130 ? 49.718 -8.110  24.240  1.00 11.43 ?  571  PRO   B CD  1 
ATOM   3931 N  N   . GLY   B 1 131 ? 54.055 -6.936  25.269  1.00 9.37  ?  572  GLY   B N   1 
ATOM   3932 C  CA  . GLY   B 1 131 ? 55.245 -7.373  25.971  1.00 10.01 ?  572  GLY   B CA  1 
ATOM   3933 C  C   . GLY   B 1 131 ? 55.685 -6.596  27.203  1.00 10.30 ?  572  GLY   B C   1 
ATOM   3934 O  O   . GLY   B 1 131 ? 56.344 -7.181  28.070  1.00 10.15 ?  572  GLY   B O   1 
ATOM   3935 N  N   . HIS   B 1 132 ? 55.362 -5.303  27.321  1.00 9.93  ?  573  HIS   B N   1 
ATOM   3936 C  CA  . HIS   B 1 132 ? 56.149 -4.451  28.228  1.00 8.82  ?  573  HIS   B CA  1 
ATOM   3937 C  C   . HIS   B 1 132 ? 55.893 -4.682  29.727  1.00 11.07 ?  573  HIS   B C   1 
ATOM   3938 O  O   . HIS   B 1 132 ? 56.699 -4.217  30.557  1.00 10.48 ?  573  HIS   B O   1 
ATOM   3939 C  CB  . HIS   B 1 132 ? 56.053 -2.973  27.844  1.00 10.62 ?  573  HIS   B CB  1 
ATOM   3940 C  CG  . HIS   B 1 132 ? 54.716 -2.347  28.094  1.00 12.12 ?  573  HIS   B CG  1 
ATOM   3941 N  ND1 . HIS   B 1 132 ? 54.579 -1.007  28.392  1.00 12.25 ?  573  HIS   B ND1 1 
ATOM   3942 C  CD2 . HIS   B 1 132 ? 53.463 -2.865  28.100  1.00 14.07 ?  573  HIS   B CD2 1 
ATOM   3943 C  CE1 . HIS   B 1 132 ? 53.297 -0.724  28.554  1.00 11.66 ?  573  HIS   B CE1 1 
ATOM   3944 N  NE2 . HIS   B 1 132 ? 52.596 -1.832  28.383  1.00 13.78 ?  573  HIS   B NE2 1 
ATOM   3945 N  N   . HIS   B 1 133 ? 54.826 -5.389  30.095  1.00 9.34  ?  574  HIS   B N   1 
ATOM   3946 C  CA  . HIS   B 1 133 ? 54.607 -5.750  31.494  1.00 9.98  ?  574  HIS   B CA  1 
ATOM   3947 C  C   . HIS   B 1 133 ? 55.295 -7.042  31.877  1.00 11.45 ?  574  HIS   B C   1 
ATOM   3948 O  O   . HIS   B 1 133 ? 55.316 -7.381  33.068  1.00 11.33 ?  574  HIS   B O   1 
ATOM   3949 C  CB  . HIS   B 1 133 ? 53.118 -5.937  31.790  1.00 10.86 ?  574  HIS   B CB  1 
ATOM   3950 C  CG  . HIS   B 1 133 ? 52.314 -4.692  31.658  1.00 11.14 ?  574  HIS   B CG  1 
ATOM   3951 N  ND1 . HIS   B 1 133 ? 52.602 -3.542  32.360  1.00 14.29 ?  574  HIS   B ND1 1 
ATOM   3952 C  CD2 . HIS   B 1 133 ? 51.232 -4.416  30.897  1.00 11.63 ?  574  HIS   B CD2 1 
ATOM   3953 C  CE1 . HIS   B 1 133 ? 51.721 -2.608  32.041  1.00 13.93 ?  574  HIS   B CE1 1 
ATOM   3954 N  NE2 . HIS   B 1 133 ? 50.879 -3.115  31.159  1.00 13.20 ?  574  HIS   B NE2 1 
ATOM   3955 N  N   . ALA   B 1 134 ? 55.835 -7.789  30.914  1.00 10.30 ?  575  ALA   B N   1 
ATOM   3956 C  CA  . ALA   B 1 134 ? 56.476 -9.055  31.243  1.00 11.24 ?  575  ALA   B CA  1 
ATOM   3957 C  C   . ALA   B 1 134 ? 57.836 -8.804  31.881  1.00 10.31 ?  575  ALA   B C   1 
ATOM   3958 O  O   . ALA   B 1 134 ? 58.609 -7.951  31.432  1.00 11.52 ?  575  ALA   B O   1 
ATOM   3959 C  CB  . ALA   B 1 134 ? 56.621 -9.946  30.008  1.00 11.23 ?  575  ALA   B CB  1 
ATOM   3960 N  N   . GLU   B 1 135 ? 58.106 -9.541  32.953  1.00 12.22 ?  576  GLU   B N   1 
ATOM   3961 C  CA  . GLU   B 1 135 ? 59.333 -9.427  33.725  1.00 12.88 ?  576  GLU   B CA  1 
ATOM   3962 C  C   . GLU   B 1 135 ? 60.256 -10.589 33.389  1.00 12.50 ?  576  GLU   B C   1 
ATOM   3963 O  O   . GLU   B 1 135 ? 59.876 -11.531 32.696  1.00 13.43 ?  576  GLU   B O   1 
ATOM   3964 C  CB  . GLU   B 1 135 ? 59.002 -9.449  35.222  1.00 12.74 ?  576  GLU   B CB  1 
ATOM   3965 C  CG  . GLU   B 1 135 ? 58.076 -8.329  35.686  1.00 13.75 ?  576  GLU   B CG  1 
ATOM   3966 C  CD  . GLU   B 1 135 ? 58.837 -7.107  36.165  1.00 15.38 ?  576  GLU   B CD  1 
ATOM   3967 O  OE1 . GLU   B 1 135 ? 60.078 -7.132  36.156  1.00 18.66 ?  576  GLU   B OE1 1 
ATOM   3968 O  OE2 . GLU   B 1 135 ? 58.197 -6.105  36.542  1.00 17.58 -1 576  GLU   B OE2 1 
ATOM   3969 N  N   . LYS   B 1 136 ? 61.497 -10.505 33.880  1.00 13.14 ?  577  LYS   B N   1 
ATOM   3970 C  CA  . LYS   B 1 136 ? 62.434 -11.611 33.724  1.00 14.74 ?  577  LYS   B CA  1 
ATOM   3971 C  C   . LYS   B 1 136 ? 61.781 -12.939 34.071  1.00 13.29 ?  577  LYS   B C   1 
ATOM   3972 O  O   . LYS   B 1 136 ? 61.933 -13.931 33.345  1.00 12.92 ?  577  LYS   B O   1 
ATOM   3973 C  CB  . LYS   B 1 136 ? 63.613 -11.388 34.674  1.00 16.64 ?  577  LYS   B CB  1 
ATOM   3974 C  CG  . LYS   B 1 136 ? 64.809 -12.289 34.430  1.00 21.44 ?  577  LYS   B CG  1 
ATOM   3975 C  CD  . LYS   B 1 136 ? 66.111 -11.537 34.718  1.00 28.06 ?  577  LYS   B CD  1 
ATOM   3976 C  CE  . LYS   B 1 136 ? 66.119 -10.155 34.055  1.00 33.98 ?  577  LYS   B CE  1 
ATOM   3977 N  NZ  . LYS   B 1 136 ? 66.399 -10.185 32.579  1.00 36.06 ?  577  LYS   B NZ  1 
ATOM   3978 N  N   . ASP   B 1 137 ? 61.024 -12.966 35.165  1.00 12.92 ?  578  ASP   B N   1 
ATOM   3979 C  CA  . ASP   B 1 137 ? 60.576 -14.212 35.770  1.00 15.08 ?  578  ASP   B CA  1 
ATOM   3980 C  C   . ASP   B 1 137 ? 59.061 -14.367 35.801  1.00 14.84 ?  578  ASP   B C   1 
ATOM   3981 O  O   . ASP   B 1 137 ? 58.572 -15.334 36.397  1.00 15.56 ?  578  ASP   B O   1 
ATOM   3982 C  CB  . ASP   B 1 137 ? 61.168 -14.354 37.182  1.00 20.75 ?  578  ASP   B CB  1 
ATOM   3983 C  CG  . ASP   B 1 137 ? 61.054 -15.769 37.738  1.00 31.63 ?  578  ASP   B CG  1 
ATOM   3984 O  OD1 . ASP   B 1 137 ? 61.548 -16.715 37.088  1.00 35.11 -1 578  ASP   B OD1 1 
ATOM   3985 O  OD2 . ASP   B 1 137 ? 60.460 -15.944 38.826  1.00 34.56 ?  578  ASP   B OD2 1 
ATOM   3986 N  N   . THR   B 1 138 ? 58.294 -13.487 35.149  1.00 12.93 ?  579  THR   B N   1 
ATOM   3987 C  CA  . THR   B 1 138 ? 56.847 -13.617 35.277  1.00 11.93 ?  579  THR   B CA  1 
ATOM   3988 C  C   . THR   B 1 138 ? 56.115 -12.919 34.136  1.00 12.61 ?  579  THR   B C   1 
ATOM   3989 O  O   . THR   B 1 138 ? 56.624 -11.981 33.519  1.00 12.78 ?  579  THR   B O   1 
ATOM   3990 C  CB  . THR   B 1 138 ? 56.364 -13.109 36.643  1.00 15.53 ?  579  THR   B CB  1 
ATOM   3991 O  OG1 . THR   B 1 138 ? 55.154 -13.777 36.981  1.00 15.84 ?  579  THR   B OG1 1 
ATOM   3992 C  CG2 . THR   B 1 138 ? 56.103 -11.608 36.642  1.00 16.58 ?  579  THR   B CG2 1 
ATOM   3993 N  N   . ALA   B 1 139 ? 54.894 -13.391 33.889  1.00 12.47 ?  580  ALA   B N   1 
ATOM   3994 C  CA  . ALA   B 1 139 ? 53.956 -12.779 32.958  1.00 12.77 ?  580  ALA   B CA  1 
ATOM   3995 C  C   . ALA   B 1 139 ? 53.049 -11.820 33.717  1.00 13.62 ?  580  ALA   B C   1 
ATOM   3996 O  O   . ALA   B 1 139 ? 52.838 -11.961 34.923  1.00 14.06 ?  580  ALA   B O   1 
ATOM   3997 C  CB  . ALA   B 1 139 ? 53.087 -13.859 32.319  1.00 13.82 ?  580  ALA   B CB  1 
ATOM   3998 N  N   . CYS   B 1 140 ? 52.483 -10.858 32.991  1.00 11.95 ?  581  CYS   B N   1 
ATOM   3999 C  CA  . CYS   B 1 140 ? 51.676 -9.831  33.633  1.00 10.93 ?  581  CYS   B CA  1 
ATOM   4000 C  C   . CYS   B 1 140 ? 50.993 -8.988  32.572  1.00 10.90 ?  581  CYS   B C   1 
ATOM   4001 O  O   . CYS   B 1 140 ? 51.589 -8.678  31.535  1.00 10.88 ?  581  CYS   B O   1 
ATOM   4002 C  CB  . CYS   B 1 140 ? 52.561 -8.905  34.479  1.00 12.08 ?  581  CYS   B CB  1 
ATOM   4003 S  SG  . CYS   B 1 140 ? 51.618 -7.607  35.321  1.00 14.17 ?  581  CYS   B SG  1 
ATOM   4004 N  N   . GLY   B 1 141 ? 49.750 -8.600  32.857  1.00 11.37 ?  582  GLY   B N   1 
ATOM   4005 C  CA  . GLY   B 1 141 ? 49.073 -7.583  32.077  1.00 9.80  ?  582  GLY   B CA  1 
ATOM   4006 C  C   . GLY   B 1 141 ? 49.040 -7.857  30.588  1.00 10.43 ?  582  GLY   B C   1 
ATOM   4007 O  O   . GLY   B 1 141 ? 49.428 -7.006  29.782  1.00 11.08 ?  582  GLY   B O   1 
ATOM   4008 N  N   . PHE   B 1 142 ? 48.633 -9.067  30.217  1.00 10.83 ?  583  PHE   B N   1 
ATOM   4009 C  CA  . PHE   B 1 142 ? 48.442 -9.534  28.844  1.00 9.74  ?  583  PHE   B CA  1 
ATOM   4010 C  C   . PHE   B 1 142 ? 49.766 -9.893  28.161  1.00 10.29 ?  583  PHE   B C   1 
ATOM   4011 O  O   . PHE   B 1 142 ? 49.741 -10.278 26.996  1.00 10.97 ?  583  PHE   B O   1 
ATOM   4012 C  CB  . PHE   B 1 142 ? 47.668 -8.556  27.933  1.00 10.34 ?  583  PHE   B CB  1 
ATOM   4013 C  CG  . PHE   B 1 142 ? 46.421 -7.944  28.551  1.00 12.15 ?  583  PHE   B CG  1 
ATOM   4014 C  CD1 . PHE   B 1 142 ? 45.743 -8.555  29.598  1.00 12.18 ?  583  PHE   B CD1 1 
ATOM   4015 C  CD2 . PHE   B 1 142 ? 45.928 -6.753  28.048  1.00 14.19 ?  583  PHE   B CD2 1 
ATOM   4016 C  CE1 . PHE   B 1 142 ? 44.598 -7.970  30.143  1.00 14.07 ?  583  PHE   B CE1 1 
ATOM   4017 C  CE2 . PHE   B 1 142 ? 44.779 -6.167  28.575  1.00 13.96 ?  583  PHE   B CE2 1 
ATOM   4018 C  CZ  . PHE   B 1 142 ? 44.117 -6.780  29.622  1.00 13.27 ?  583  PHE   B CZ  1 
ATOM   4019 N  N   . CYS   B 1 143 ? 50.900 -9.838  28.867  1.00 10.65 ?  584  CYS   B N   1 
ATOM   4020 C  CA  . CYS   B 1 143 ? 52.235 -9.948  28.290  1.00 9.60  ?  584  CYS   B CA  1 
ATOM   4021 C  C   . CYS   B 1 143 ? 52.938 -11.184 28.834  1.00 10.06 ?  584  CYS   B C   1 
ATOM   4022 O  O   . CYS   B 1 143 ? 52.985 -11.392 30.051  1.00 10.46 ?  584  CYS   B O   1 
ATOM   4023 C  CB  . CYS   B 1 143 ? 53.074 -8.742  28.705  1.00 10.42 ?  584  CYS   B CB  1 
ATOM   4024 S  SG  . CYS   B 1 143 ? 52.423 -7.145  28.177  1.00 15.23 ?  584  CYS   B SG  1 
ATOM   4025 N  N   . PHE   B 1 144 ? 53.502 -11.996 27.939  1.00 10.58 ?  585  PHE   B N   1 
ATOM   4026 C  CA  . PHE   B 1 144 ? 54.229 -13.206 28.328  1.00 9.52  ?  585  PHE   B CA  1 
ATOM   4027 C  C   . PHE   B 1 144 ? 55.739 -13.030 28.334  1.00 10.86 ?  585  PHE   B C   1 
ATOM   4028 O  O   . PHE   B 1 144 ? 56.393 -13.408 29.316  1.00 11.49 ?  585  PHE   B O   1 
ATOM   4029 C  CB  . PHE   B 1 144 ? 53.852 -14.361 27.403  1.00 10.90 ?  585  PHE   B CB  1 
ATOM   4030 C  CG  . PHE   B 1 144 ? 52.420 -14.750 27.527  1.00 10.78 ?  585  PHE   B CG  1 
ATOM   4031 C  CD1 . PHE   B 1 144 ? 52.016 -15.632 28.512  1.00 11.66 ?  585  PHE   B CD1 1 
ATOM   4032 C  CD2 . PHE   B 1 144 ? 51.469 -14.192 26.689  1.00 11.90 ?  585  PHE   B CD2 1 
ATOM   4033 C  CE1 . PHE   B 1 144 ? 50.679 -15.977 28.654  1.00 12.42 ?  585  PHE   B CE1 1 
ATOM   4034 C  CE2 . PHE   B 1 144 ? 50.128 -14.532 26.818  1.00 13.32 ?  585  PHE   B CE2 1 
ATOM   4035 C  CZ  . PHE   B 1 144 ? 49.729 -15.423 27.803  1.00 11.22 ?  585  PHE   B CZ  1 
ATOM   4036 N  N   . PHE   B 1 145 ? 56.295 -12.492 27.256  1.00 9.25  ?  586  PHE   B N   1 
ATOM   4037 C  CA  . PHE   B 1 145 ? 57.710 -12.179 27.158  1.00 9.67  ?  586  PHE   B CA  1 
ATOM   4038 C  C   . PHE   B 1 145 ? 57.837 -10.720 26.756  1.00 10.08 ?  586  PHE   B C   1 
ATOM   4039 O  O   . PHE   B 1 145 ? 56.960 -10.164 26.085  1.00 11.17 ?  586  PHE   B O   1 
ATOM   4040 C  CB  . PHE   B 1 145 ? 58.411 -13.089 26.131  1.00 11.00 ?  586  PHE   B CB  1 
ATOM   4041 C  CG  . PHE   B 1 145 ? 58.193 -14.567 26.377  1.00 9.94  ?  586  PHE   B CG  1 
ATOM   4042 C  CD1 . PHE   B 1 145 ? 58.580 -15.163 27.578  1.00 10.57 ?  586  PHE   B CD1 1 
ATOM   4043 C  CD2 . PHE   B 1 145 ? 57.588 -15.360 25.406  1.00 11.43 ?  586  PHE   B CD2 1 
ATOM   4044 C  CE1 . PHE   B 1 145 ? 58.362 -16.530 27.794  1.00 11.53 ?  586  PHE   B CE1 1 
ATOM   4045 C  CE2 . PHE   B 1 145 ? 57.378 -16.717 25.619  1.00 12.16 ?  586  PHE   B CE2 1 
ATOM   4046 C  CZ  . PHE   B 1 145 ? 57.769 -17.305 26.801  1.00 12.19 ?  586  PHE   B CZ  1 
ATOM   4047 N  N   . ASN   B 1 146 ? 58.912 -10.084 27.197  1.00 10.51 ?  587  ASN   B N   1 
ATOM   4048 C  CA  . ASN   B 1 146 ? 59.041 -8.655  26.945  1.00 9.67  ?  587  ASN   B CA  1 
ATOM   4049 C  C   . ASN   B 1 146 ? 59.659 -8.417  25.570  1.00 10.92 ?  587  ASN   B C   1 
ATOM   4050 O  O   . ASN   B 1 146 ? 60.875 -8.294  25.412  1.00 11.31 ?  587  ASN   B O   1 
ATOM   4051 C  CB  . ASN   B 1 146 ? 59.823 -7.964  28.044  1.00 9.84  ?  587  ASN   B CB  1 
ATOM   4052 C  CG  . ASN   B 1 146 ? 59.617 -6.477  28.009  1.00 8.14  ?  587  ASN   B CG  1 
ATOM   4053 O  OD1 . ASN   B 1 146 ? 59.644 -5.865  26.925  1.00 10.28 ?  587  ASN   B OD1 1 
ATOM   4054 N  ND2 . ASN   B 1 146 ? 59.380 -5.877  29.179  1.00 9.98  ?  587  ASN   B ND2 1 
ATOM   4055 N  N   . THR   B 1 147 ? 58.789 -8.286  24.575  1.00 11.02 ?  588  THR   B N   1 
ATOM   4056 C  CA  . THR   B 1 147 ? 59.214 -8.198  23.183  1.00 10.70 ?  588  THR   B CA  1 
ATOM   4057 C  C   . THR   B 1 147 ? 60.187 -7.047  22.951  1.00 10.88 ?  588  THR   B C   1 
ATOM   4058 O  O   . THR   B 1 147 ? 61.227 -7.227  22.300  1.00 11.41 ?  588  THR   B O   1 
ATOM   4059 C  CB  . THR   B 1 147 ? 57.971 -8.050  22.320  1.00 10.20 ?  588  THR   B CB  1 
ATOM   4060 O  OG1 . THR   B 1 147 ? 57.163 -9.220  22.500  1.00 12.33 ?  588  THR   B OG1 1 
ATOM   4061 C  CG2 . THR   B 1 147 ? 58.339 -7.871  20.847  1.00 11.23 ?  588  THR   B CG2 1 
ATOM   4062 N  N   . ALA   B 1 148 ? 59.865 -5.852  23.460  1.00 10.33 ?  589  ALA   B N   1 
ATOM   4063 C  CA  . ALA   B 1 148 ? 60.749 -4.709  23.253  1.00 10.88 ?  589  ALA   B CA  1 
ATOM   4064 C  C   . ALA   B 1 148 ? 62.090 -4.909  23.941  1.00 9.55  ?  589  ALA   B C   1 
ATOM   4065 O  O   . ALA   B 1 148 ? 63.142 -4.630  23.351  1.00 10.89 ?  589  ALA   B O   1 
ATOM   4066 C  CB  . ALA   B 1 148 ? 60.086 -3.415  23.722  1.00 11.01 ?  589  ALA   B CB  1 
ATOM   4067 N  N   . ALA   B 1 149 ? 62.078 -5.392  25.185  1.00 9.93  ?  590  ALA   B N   1 
ATOM   4068 C  CA  . ALA   B 1 149 ? 63.336 -5.617  25.892  1.00 10.78 ?  590  ALA   B CA  1 
ATOM   4069 C  C   . ALA   B 1 149 ? 64.181 -6.667  25.177  1.00 11.08 ?  590  ALA   B C   1 
ATOM   4070 O  O   . ALA   B 1 149 ? 65.399 -6.493  25.015  1.00 11.81 ?  590  ALA   B O   1 
ATOM   4071 C  CB  . ALA   B 1 149 ? 63.056 -6.020  27.353  1.00 10.42 ?  590  ALA   B CB  1 
ATOM   4072 N  N   . LEU   B 1 150 ? 63.553 -7.773  24.766  1.00 9.84  ?  591  LEU   B N   1 
ATOM   4073 C  CA  . LEU   B 1 150 ? 64.254 -8.800  23.999  1.00 9.70  ?  591  LEU   B CA  1 
ATOM   4074 C  C   . LEU   B 1 150 ? 64.840 -8.238  22.714  1.00 11.56 ?  591  LEU   B C   1 
ATOM   4075 O  O   . LEU   B 1 150 ? 65.950 -8.615  22.308  1.00 10.73 ?  591  LEU   B O   1 
ATOM   4076 C  CB  . LEU   B 1 150 ? 63.288 -9.935  23.665  1.00 12.77 ?  591  LEU   B CB  1 
ATOM   4077 C  CG  . LEU   B 1 150 ? 62.890 -10.821 24.838  1.00 11.09 ?  591  LEU   B CG  1 
ATOM   4078 C  CD1 . LEU   B 1 150 ? 61.675 -11.674 24.494  1.00 12.74 ?  591  LEU   B CD1 1 
ATOM   4079 C  CD2 . LEU   B 1 150 ? 64.073 -11.697 25.281  1.00 12.61 ?  591  LEU   B CD2 1 
ATOM   4080 N  N   . THR   B 1 151 ? 64.097 -7.360  22.037  1.00 10.54 ?  592  THR   B N   1 
ATOM   4081 C  CA  . THR   B 1 151 ? 64.588 -6.785  20.788  1.00 10.19 ?  592  THR   B CA  1 
ATOM   4082 C  C   . THR   B 1 151 ? 65.818 -5.917  21.039  1.00 10.40 ?  592  THR   B C   1 
ATOM   4083 O  O   . THR   B 1 151 ? 66.767 -5.924  20.240  1.00 12.05 ?  592  THR   B O   1 
ATOM   4084 C  CB  . THR   B 1 151 ? 63.473 -6.004  20.088  1.00 11.65 ?  592  THR   B CB  1 
ATOM   4085 O  OG1 . THR   B 1 151 ? 62.368 -6.880  19.780  1.00 12.23 ?  592  THR   B OG1 1 
ATOM   4086 C  CG2 . THR   B 1 151 ? 63.988 -5.427  18.774  1.00 10.02 ?  592  THR   B CG2 1 
ATOM   4087 N  N   . ALA   B 1 152 ? 65.835 -5.176  22.146  1.00 11.35 ?  593  ALA   B N   1 
ATOM   4088 C  CA  . ALA   B 1 152 ? 67.028 -4.407  22.480  1.00 10.60 ?  593  ALA   B CA  1 
ATOM   4089 C  C   . ALA   B 1 152 ? 68.232 -5.324  22.683  1.00 11.68 ?  593  ALA   B C   1 
ATOM   4090 O  O   . ALA   B 1 152 ? 69.319 -5.059  22.159  1.00 12.41 ?  593  ALA   B O   1 
ATOM   4091 C  CB  . ALA   B 1 152 ? 66.772 -3.527  23.707  1.00 11.96 ?  593  ALA   B CB  1 
ATOM   4092 N  N   . ARG   B 1 153 ? 68.057 -6.416  23.435  1.00 11.30 ?  594  ARG   B N   1 
ATOM   4093 C  CA  . ARG   B 1 153 ? 69.158 -7.352  23.655  1.00 11.64 ?  594  ARG   B CA  1 
ATOM   4094 C  C   . ARG   B 1 153 ? 69.520 -8.100  22.381  1.00 13.80 ?  594  ARG   B C   1 
ATOM   4095 O  O   . ARG   B 1 153 ? 70.704 -8.373  22.139  1.00 12.75 ?  594  ARG   B O   1 
ATOM   4096 C  CB  . ARG   B 1 153 ? 68.796 -8.343  24.759  1.00 12.99 ?  594  ARG   B CB  1 
ATOM   4097 C  CG  . ARG   B 1 153 ? 68.683 -7.716  26.128  1.00 14.46 ?  594  ARG   B CG  1 
ATOM   4098 C  CD  . ARG   B 1 153 ? 69.975 -7.038  26.558  1.00 15.60 ?  594  ARG   B CD  1 
ATOM   4099 N  NE  . ARG   B 1 153 ? 69.952 -6.839  28.009  1.00 14.95 ?  594  ARG   B NE  1 
ATOM   4100 C  CZ  . ARG   B 1 153 ? 70.623 -5.896  28.656  1.00 15.08 ?  594  ARG   B CZ  1 
ATOM   4101 N  NH1 . ARG   B 1 153 ? 71.376 -5.037  27.983  1.00 14.82 ?  594  ARG   B NH1 1 
ATOM   4102 N  NH2 . ARG   B 1 153 ? 70.526 -5.817  29.980  1.00 16.35 ?  594  ARG   B NH2 1 
ATOM   4103 N  N   . TYR   B 1 154 ? 68.524 -8.472  21.571  1.00 12.52 ?  595  TYR   B N   1 
ATOM   4104 C  CA  . TYR   B 1 154 ? 68.826 -9.086  20.280  1.00 12.71 ?  595  TYR   B CA  1 
ATOM   4105 C  C   . TYR   B 1 154 ? 69.685 -8.158  19.425  1.00 11.93 ?  595  TYR   B C   1 
ATOM   4106 O  O   . TYR   B 1 154 ? 70.663 -8.595  18.798  1.00 13.13 ?  595  TYR   B O   1 
ATOM   4107 C  CB  . TYR   B 1 154 ? 67.528 -9.457  19.550  1.00 11.40 ?  595  TYR   B CB  1 
ATOM   4108 C  CG  . TYR   B 1 154 ? 67.807 -9.880  18.133  1.00 10.28 ?  595  TYR   B CG  1 
ATOM   4109 C  CD1 . TYR   B 1 154 ? 68.210 -11.181 17.851  1.00 13.22 ?  595  TYR   B CD1 1 
ATOM   4110 C  CD2 . TYR   B 1 154 ? 67.710 -8.977  17.091  1.00 12.41 ?  595  TYR   B CD2 1 
ATOM   4111 C  CE1 . TYR   B 1 154 ? 68.499 -11.574 16.555  1.00 14.58 ?  595  TYR   B CE1 1 
ATOM   4112 C  CE2 . TYR   B 1 154 ? 68.005 -9.356  15.793  1.00 12.20 ?  595  TYR   B CE2 1 
ATOM   4113 C  CZ  . TYR   B 1 154 ? 68.397 -10.656 15.542  1.00 14.51 ?  595  TYR   B CZ  1 
ATOM   4114 O  OH  . TYR   B 1 154 ? 68.687 -11.031 14.252  1.00 16.28 ?  595  TYR   B OH  1 
ATOM   4115 N  N   . ALA   B 1 155 ? 69.328 -6.872  19.392  1.00 12.97 ?  596  ALA   B N   1 
ATOM   4116 C  CA  . ALA   B 1 155 ? 70.085 -5.885  18.631  1.00 12.09 ?  596  ALA   B CA  1 
ATOM   4117 C  C   . ALA   B 1 155 ? 71.531 -5.847  19.094  1.00 11.46 ?  596  ALA   B C   1 
ATOM   4118 O  O   . ALA   B 1 155 ? 72.457 -5.826  18.271  1.00 12.24 ?  596  ALA   B O   1 
ATOM   4119 C  CB  . ALA   B 1 155 ? 69.447 -4.506  18.800  1.00 14.32 ?  596  ALA   B CB  1 
ATOM   4120 N  N   . GLN   B 1 156 ? 71.735 -5.830  20.413  1.00 11.63 ?  597  GLN   B N   1 
ATOM   4121 C  CA  . GLN   B 1 156 ? 73.082 -5.864  20.961  1.00 12.73 ?  597  GLN   B CA  1 
ATOM   4122 C  C   . GLN   B 1 156 ? 73.807 -7.152  20.581  1.00 13.88 ?  597  GLN   B C   1 
ATOM   4123 O  O   . GLN   B 1 156 ? 75.005 -7.125  20.275  1.00 15.58 ?  597  GLN   B O   1 
ATOM   4124 C  CB  . GLN   B 1 156 ? 73.022 -5.641  22.479  1.00 11.19 ?  597  GLN   B CB  1 
ATOM   4125 C  CG  . GLN   B 1 156 ? 72.645 -4.218  22.825  1.00 12.80 ?  597  GLN   B CG  1 
ATOM   4126 C  CD  . GLN   B 1 156 ? 72.356 -3.979  24.290  1.00 11.93 ?  597  GLN   B CD  1 
ATOM   4127 O  OE1 . GLN   B 1 156 ? 72.074 -4.906  25.056  1.00 13.48 ?  597  GLN   B OE1 1 
ATOM   4128 N  NE2 . GLN   B 1 156 ? 72.416 -2.718  24.684  1.00 14.19 ?  597  GLN   B NE2 1 
ATOM   4129 N  N   . SER   B 1 157 ? 73.085 -8.284  20.531  1.00 14.78 ?  598  SER   B N   1 
ATOM   4130 C  CA  . SER   B 1 157 ? 73.732 -9.565  20.255  1.00 13.85 ?  598  SER   B CA  1 
ATOM   4131 C  C   . SER   B 1 157 ? 74.278 -9.639  18.835  1.00 15.59 ?  598  SER   B C   1 
ATOM   4132 O  O   . SER   B 1 157 ? 75.204 -10.413 18.569  1.00 16.30 ?  598  SER   B O   1 
ATOM   4133 C  CB  . SER   B 1 157 ? 72.765 -10.726 20.497  1.00 15.28 ?  598  SER   B CB  1 
ATOM   4134 O  OG  . SER   B 1 157 ? 71.854 -10.890 19.424  1.00 15.61 ?  598  SER   B OG  1 
ATOM   4135 N  N   . ILE   B 1 158 ? 73.718 -8.870  17.903  1.00 13.39 ?  599  ILE   B N   1 
ATOM   4136 C  CA  . ILE   B 1 158 ? 74.164 -8.894  16.508  1.00 14.79 ?  599  ILE   B CA  1 
ATOM   4137 C  C   . ILE   B 1 158 ? 74.994 -7.682  16.138  1.00 14.27 ?  599  ILE   B C   1 
ATOM   4138 O  O   . ILE   B 1 158 ? 75.398 -7.548  14.969  1.00 15.78 ?  599  ILE   B O   1 
ATOM   4139 C  CB  . ILE   B 1 158 ? 73.003 -9.099  15.518  1.00 16.63 ?  599  ILE   B CB  1 
ATOM   4140 C  CG1 . ILE   B 1 158 ? 72.037 -7.905  15.552  1.00 15.45 ?  599  ILE   B CG1 1 
ATOM   4141 C  CG2 . ILE   B 1 158 ? 72.273 -10.390 15.835  1.00 15.17 ?  599  ILE   B CG2 1 
ATOM   4142 C  CD1 . ILE   B 1 158 ? 71.004 -7.915  14.419  1.00 15.64 ?  599  ILE   B CD1 1 
ATOM   4143 N  N   . THR   B 1 159 ? 75.261 -6.793  17.089  1.00 14.57 ?  600  THR   B N   1 
ATOM   4144 C  CA  . THR   B 1 159 ? 76.155 -5.671  16.872  1.00 16.48 ?  600  THR   B CA  1 
ATOM   4145 C  C   . THR   B 1 159 ? 77.246 -5.708  17.930  1.00 16.37 ?  600  THR   B C   1 
ATOM   4146 O  O   . THR   B 1 159 ? 78.219 -6.461  17.797  1.00 15.97 ?  600  THR   B O   1 
ATOM   4147 C  CB  . THR   B 1 159 ? 75.379 -4.344  16.857  1.00 15.82 ?  600  THR   B CB  1 
ATOM   4148 O  OG1 . THR   B 1 159 ? 74.646 -4.178  18.081  1.00 14.80 ?  600  THR   B OG1 1 
ATOM   4149 C  CG2 . THR   B 1 159 ? 74.427 -4.328  15.683  1.00 17.80 ?  600  THR   B CG2 1 
ATOM   4150 N  N   . ARG   B 1 160 ? 77.089 -4.918  18.983  1.00 13.93 ?  601  ARG   B N   1 
ATOM   4151 C  CA  . ARG   B 1 160 ? 77.982 -4.965  20.127  1.00 14.29 ?  601  ARG   B CA  1 
ATOM   4152 C  C   . ARG   B 1 160 ? 77.148 -4.838  21.390  1.00 16.04 ?  601  ARG   B C   1 
ATOM   4153 O  O   . ARG   B 1 160 ? 76.044 -4.281  21.373  1.00 16.11 ?  601  ARG   B O   1 
ATOM   4154 C  CB  . ARG   B 1 160 ? 79.039 -3.857  20.066  1.00 16.23 ?  601  ARG   B CB  1 
ATOM   4155 C  CG  . ARG   B 1 160 ? 78.476 -2.464  20.218  1.00 18.31 ?  601  ARG   B CG  1 
ATOM   4156 C  CD  . ARG   B 1 160 ? 79.572 -1.414  20.184  1.00 21.22 ?  601  ARG   B CD  1 
ATOM   4157 N  NE  . ARG   B 1 160 ? 79.148 -0.189  20.855  1.00 23.99 ?  601  ARG   B NE  1 
ATOM   4158 C  CZ  . ARG   B 1 160 ? 78.398 0.744   20.283  1.00 24.10 ?  601  ARG   B CZ  1 
ATOM   4159 N  NH1 . ARG   B 1 160 ? 77.989 0.590   19.030  1.00 24.73 ?  601  ARG   B NH1 1 
ATOM   4160 N  NH2 . ARG   B 1 160 ? 78.049 1.828   20.961  1.00 23.00 ?  601  ARG   B NH2 1 
ATOM   4161 N  N   . GLU   B 1 161 ? 77.690 -5.380  22.483  1.00 17.77 ?  602  GLU   B N   1 
ATOM   4162 C  CA  . GLU   B 1 161 ? 76.955 -5.436  23.742  1.00 20.56 ?  602  GLU   B CA  1 
ATOM   4163 C  C   . GLU   B 1 161 ? 76.514 -4.054  24.215  1.00 18.53 ?  602  GLU   B C   1 
ATOM   4164 O  O   . GLU   B 1 161 ? 75.429 -3.913  24.796  1.00 19.24 ?  602  GLU   B O   1 
ATOM   4165 C  CB  . GLU   B 1 161 ? 77.824 -6.115  24.806  1.00 27.29 ?  602  GLU   B CB  1 
ATOM   4166 C  CG  . GLU   B 1 161 ? 77.083 -6.489  26.074  1.00 36.70 ?  602  GLU   B CG  1 
ATOM   4167 C  CD  . GLU   B 1 161 ? 76.824 -7.983  26.181  1.00 46.11 ?  602  GLU   B CD  1 
ATOM   4168 O  OE1 . GLU   B 1 161 ? 75.726 -8.366  26.638  1.00 48.92 ?  602  GLU   B OE1 1 
ATOM   4169 O  OE2 . GLU   B 1 161 ? 77.718 -8.774  25.805  1.00 49.21 -1 602  GLU   B OE2 1 
ATOM   4170 N  N   . SER   B 1 162 ? 77.326 -3.029  23.987  1.00 16.30 ?  603  SER   B N   1 
ATOM   4171 C  CA  . SER   B 1 162 ? 77.039 -1.695  24.489  1.00 18.09 ?  603  SER   B CA  1 
ATOM   4172 C  C   . SER   B 1 162 ? 76.311 -0.817  23.478  1.00 15.11 ?  603  SER   B C   1 
ATOM   4173 O  O   . SER   B 1 162 ? 76.243 0.403   23.672  1.00 16.89 ?  603  SER   B O   1 
ATOM   4174 C  CB  . SER   B 1 162 ? 78.329 -1.018  24.963  1.00 21.48 ?  603  SER   B CB  1 
ATOM   4175 O  OG  . SER   B 1 162 ? 79.221 -0.828  23.876  1.00 24.81 ?  603  SER   B OG  1 
ATOM   4176 N  N   . LEU   B 1 163 ? 75.764 -1.405  22.411  1.00 14.18 ?  604  LEU   B N   1 
ATOM   4177 C  CA  . LEU   B 1 163 ? 74.962 -0.640  21.460  1.00 14.38 ?  604  LEU   B CA  1 
ATOM   4178 C  C   . LEU   B 1 163 ? 73.892 0.150   22.207  1.00 14.59 ?  604  LEU   B C   1 
ATOM   4179 O  O   . LEU   B 1 163 ? 73.146 -0.403  23.019  1.00 13.80 ?  604  LEU   B O   1 
ATOM   4180 C  CB  . LEU   B 1 163 ? 74.297 -1.582  20.458  1.00 15.01 ?  604  LEU   B CB  1 
ATOM   4181 C  CG  . LEU   B 1 163 ? 73.480 -0.835  19.410  1.00 15.13 ?  604  LEU   B CG  1 
ATOM   4182 C  CD1 . LEU   B 1 163 ? 74.383 -0.411  18.262  1.00 15.62 ?  604  LEU   B CD1 1 
ATOM   4183 C  CD2 . LEU   B 1 163 ? 72.308 -1.694  18.929  1.00 15.19 ?  604  LEU   B CD2 1 
ATOM   4184 N  N   . ARG   B 1 164 ? 73.839 1.453   21.959  1.00 13.68 ?  605  ARG   B N   1 
ATOM   4185 C  CA  . ARG   B 1 164 ? 72.947 2.330   22.715  1.00 13.31 ?  605  ARG   B CA  1 
ATOM   4186 C  C   . ARG   B 1 164 ? 71.543 2.222   22.139  1.00 13.33 ?  605  ARG   B C   1 
ATOM   4187 O  O   . ARG   B 1 164 ? 71.296 2.644   21.004  1.00 13.29 ?  605  ARG   B O   1 
ATOM   4188 C  CB  . ARG   B 1 164 ? 73.440 3.773   22.673  1.00 14.88 ?  605  ARG   B CB  1 
ATOM   4189 C  CG  . ARG   B 1 164 ? 74.690 4.000   23.511  1.00 15.45 ?  605  ARG   B CG  1 
ATOM   4190 C  CD  . ARG   B 1 164 ? 75.057 5.478   23.643  1.00 16.28 ?  605  ARG   B CD  1 
ATOM   4191 N  NE  . ARG   B 1 164 ? 75.189 6.154   22.357  1.00 19.92 ?  605  ARG   B NE  1 
ATOM   4192 C  CZ  . ARG   B 1 164 ? 76.254 6.083   21.563  1.00 22.04 ?  605  ARG   B CZ  1 
ATOM   4193 N  NH1 . ARG   B 1 164 ? 77.306 5.349   21.914  1.00 21.87 ?  605  ARG   B NH1 1 
ATOM   4194 N  NH2 . ARG   B 1 164 ? 76.261 6.741   20.411  1.00 22.85 ?  605  ARG   B NH2 1 
ATOM   4195 N  N   . VAL   B 1 165 ? 70.617 1.681   22.925  1.00 12.53 ?  606  VAL   B N   1 
ATOM   4196 C  CA  . VAL   B 1 165 ? 69.231 1.512   22.498  1.00 11.91 ?  606  VAL   B CA  1 
ATOM   4197 C  C   . VAL   B 1 165 ? 68.350 2.383   23.377  1.00 10.89 ?  606  VAL   B C   1 
ATOM   4198 O  O   . VAL   B 1 165 ? 68.425 2.313   24.613  1.00 11.64 ?  606  VAL   B O   1 
ATOM   4199 C  CB  . VAL   B 1 165 ? 68.779 0.043   22.559  1.00 11.47 ?  606  VAL   B CB  1 
ATOM   4200 C  CG1 . VAL   B 1 165 ? 67.333 -0.094  22.051  1.00 11.97 ?  606  VAL   B CG1 1 
ATOM   4201 C  CG2 . VAL   B 1 165 ? 69.709 -0.844  21.759  1.00 14.17 ?  606  VAL   B CG2 1 
ATOM   4202 N  N   . LEU   B 1 166 ? 67.542 3.223   22.739  1.00 12.39 ?  607  LEU   B N   1 
ATOM   4203 C  CA  . LEU   B 1 166 ? 66.521 3.998   23.430  1.00 11.64 ?  607  LEU   B CA  1 
ATOM   4204 C  C   . LEU   B 1 166 ? 65.188 3.303   23.229  1.00 10.42 ?  607  LEU   B C   1 
ATOM   4205 O  O   . LEU   B 1 166 ? 64.824 2.979   22.090  1.00 12.39 ?  607  LEU   B O   1 
ATOM   4206 C  CB  . LEU   B 1 166 ? 66.431 5.420   22.873  1.00 12.56 ?  607  LEU   B CB  1 
ATOM   4207 C  CG  . LEU   B 1 166 ? 65.148 6.198   23.213  1.00 11.21 ?  607  LEU   B CG  1 
ATOM   4208 C  CD1 . LEU   B 1 166 ? 65.062 6.522   24.714  1.00 12.24 ?  607  LEU   B CD1 1 
ATOM   4209 C  CD2 . LEU   B 1 166 ? 65.057 7.467   22.374  1.00 13.21 ?  607  LEU   B CD2 1 
ATOM   4210 N  N   . ILE   B 1 167 ? 64.474 3.062   24.330  1.00 10.21 ?  608  ILE   B N   1 
ATOM   4211 C  CA  . ILE   B 1 167 ? 63.104 2.553   24.295  1.00 10.77 ?  608  ILE   B CA  1 
ATOM   4212 C  C   . ILE   B 1 167 ? 62.202 3.672   24.801  1.00 9.99  ?  608  ILE   B C   1 
ATOM   4213 O  O   . ILE   B 1 167 ? 62.292 4.075   25.962  1.00 11.87 ?  608  ILE   B O   1 
ATOM   4214 C  CB  . ILE   B 1 167 ? 62.928 1.294   25.155  1.00 10.90 ?  608  ILE   B CB  1 
ATOM   4215 C  CG1 . ILE   B 1 167 ? 63.836 0.151   24.684  1.00 12.91 ?  608  ILE   B CG1 1 
ATOM   4216 C  CG2 . ILE   B 1 167 ? 61.456 0.847   25.153  1.00 12.22 ?  608  ILE   B CG2 1 
ATOM   4217 C  CD1 . ILE   B 1 167 ? 63.760 -1.083  25.585  1.00 12.52 ?  608  ILE   B CD1 1 
ATOM   4218 N  N   . VAL   B 1 168 ? 61.341 4.197   23.929  1.00 9.40  ?  609  VAL   B N   1 
ATOM   4219 C  CA  . VAL   B 1 168 ? 60.323 5.171   24.313  1.00 10.85 ?  609  VAL   B CA  1 
ATOM   4220 C  C   . VAL   B 1 168 ? 59.012 4.415   24.424  1.00 10.26 ?  609  VAL   B C   1 
ATOM   4221 O  O   . VAL   B 1 168 ? 58.577 3.780   23.458  1.00 9.90  ?  609  VAL   B O   1 
ATOM   4222 C  CB  . VAL   B 1 168 ? 60.209 6.315   23.290  1.00 11.73 ?  609  VAL   B CB  1 
ATOM   4223 C  CG1 . VAL   B 1 168 ? 59.029 7.222   23.625  1.00 14.32 ?  609  VAL   B CG1 1 
ATOM   4224 C  CG2 . VAL   B 1 168 ? 61.517 7.111   23.205  1.00 12.97 ?  609  VAL   B CG2 1 
ATOM   4225 N  N   . ASP   B 1 169 ? 58.392 4.469   25.592  1.00 10.65 ?  610  ASP   B N   1 
ATOM   4226 C  CA  . ASP   B 1 169 ? 57.200 3.682   25.890  1.00 9.55  ?  610  ASP   B CA  1 
ATOM   4227 C  C   . ASP   B 1 169 ? 56.032 4.654   26.072  1.00 9.70  ?  610  ASP   B C   1 
ATOM   4228 O  O   . ASP   B 1 169 ? 55.884 5.274   27.133  1.00 10.51 ?  610  ASP   B O   1 
ATOM   4229 C  CB  . ASP   B 1 169 ? 57.465 2.839   27.139  1.00 11.38 ?  610  ASP   B CB  1 
ATOM   4230 C  CG  . ASP   B 1 169 ? 56.357 1.853   27.457  1.00 10.30 ?  610  ASP   B CG  1 
ATOM   4231 O  OD1 . ASP   B 1 169 ? 55.182 2.114   27.138  1.00 11.04 ?  610  ASP   B OD1 1 
ATOM   4232 O  OD2 . ASP   B 1 169 ? 56.669 0.803   28.077  1.00 11.97 -1 610  ASP   B OD2 1 
ATOM   4233 N  N   . TRP   B 1 170 ? 55.214 4.811   25.027  1.00 9.86  ?  611  TRP   B N   1 
ATOM   4234 C  CA  . TRP   B 1 170 ? 54.085 5.734   25.080  1.00 10.18 ?  611  TRP   B CA  1 
ATOM   4235 C  C   . TRP   B 1 170 ? 52.747 5.031   25.290  1.00 8.43  ?  611  TRP   B C   1 
ATOM   4236 O  O   . TRP   B 1 170 ? 51.693 5.679   25.246  1.00 9.43  ?  611  TRP   B O   1 
ATOM   4237 C  CB  . TRP   B 1 170 ? 54.087 6.727   23.910  1.00 9.36  ?  611  TRP   B CB  1 
ATOM   4238 C  CG  . TRP   B 1 170 ? 53.714 6.196   22.534  1.00 9.67  ?  611  TRP   B CG  1 
ATOM   4239 C  CD1 . TRP   B 1 170 ? 52.715 5.318   22.223  1.00 8.91  ?  611  TRP   B CD1 1 
ATOM   4240 C  CD2 . TRP   B 1 170 ? 54.321 6.572   21.295  1.00 9.67  ?  611  TRP   B CD2 1 
ATOM   4241 N  NE1 . TRP   B 1 170 ? 52.671 5.107   20.859  1.00 9.81  ?  611  TRP   B NE1 1 
ATOM   4242 C  CE2 . TRP   B 1 170 ? 53.644 5.872   20.267  1.00 10.36 ?  611  TRP   B CE2 1 
ATOM   4243 C  CE3 . TRP   B 1 170 ? 55.371 7.431   20.949  1.00 9.59  ?  611  TRP   B CE3 1 
ATOM   4244 C  CZ2 . TRP   B 1 170 ? 53.997 5.995   18.919  1.00 10.54 ?  611  TRP   B CZ2 1 
ATOM   4245 C  CZ3 . TRP   B 1 170 ? 55.710 7.559   19.598  1.00 12.72 ?  611  TRP   B CZ3 1 
ATOM   4246 C  CH2 . TRP   B 1 170 ? 55.026 6.847   18.611  1.00 11.92 ?  611  TRP   B CH2 1 
ATOM   4247 N  N   . ASP   B 1 171 ? 52.765 3.722   25.530  1.00 10.31 ?  612  ASP   B N   1 
ATOM   4248 C  CA  . ASP   B 1 171 ? 51.588 3.050   26.059  1.00 10.57 ?  612  ASP   B CA  1 
ATOM   4249 C  C   . ASP   B 1 171 ? 51.155 3.785   27.322  1.00 10.37 ?  612  ASP   B C   1 
ATOM   4250 O  O   . ASP   B 1 171 ? 51.988 4.336   28.049  1.00 11.67 ?  612  ASP   B O   1 
ATOM   4251 C  CB  . ASP   B 1 171 ? 51.978 1.593   26.350  1.00 10.34 ?  612  ASP   B CB  1 
ATOM   4252 C  CG  . ASP   B 1 171 ? 50.811 0.724   26.727  1.00 10.88 ?  612  ASP   B CG  1 
ATOM   4253 O  OD1 . ASP   B 1 171 ? 50.322 0.853   27.871  1.00 10.45 ?  612  ASP   B OD1 1 
ATOM   4254 O  OD2 . ASP   B 1 171 ? 50.383 -0.111  25.907  1.00 12.11 -1 612  ASP   B OD2 1 
ATOM   4255 N  N   . VAL   B 1 172 ? 49.836 3.832   27.556  1.00 9.57  ?  613  VAL   B N   1 
ATOM   4256 C  CA  . VAL   B 1 172 ? 49.317 4.574   28.703  1.00 10.10 ?  613  VAL   B CA  1 
ATOM   4257 C  C   . VAL   B 1 172 ? 49.757 3.972   30.032  1.00 10.49 ?  613  VAL   B C   1 
ATOM   4258 O  O   . VAL   B 1 172 ? 49.718 4.663   31.065  1.00 11.60 ?  613  VAL   B O   1 
ATOM   4259 C  CB  . VAL   B 1 172 ? 47.779 4.696   28.628  1.00 10.60 ?  613  VAL   B CB  1 
ATOM   4260 C  CG1 . VAL   B 1 172 ? 47.102 3.413   29.113  1.00 10.81 ?  613  VAL   B CG1 1 
ATOM   4261 C  CG2 . VAL   B 1 172 ? 47.292 5.894   29.422  1.00 12.04 ?  613  VAL   B CG2 1 
ATOM   4262 N  N   . HIS   B 1 173 ? 50.179 2.712   30.039  1.00 9.99  ?  614  HIS   B N   1 
ATOM   4263 C  CA  . HIS   B 1 173 ? 50.627 2.037   31.251  1.00 11.04 ?  614  HIS   B CA  1 
ATOM   4264 C  C   . HIS   B 1 173 ? 52.148 2.035   31.344  1.00 10.28 ?  614  HIS   B C   1 
ATOM   4265 O  O   . HIS   B 1 173 ? 52.854 2.012   30.333  1.00 10.43 ?  614  HIS   B O   1 
ATOM   4266 C  CB  . HIS   B 1 173 ? 50.129 0.585   31.247  1.00 9.93  ?  614  HIS   B CB  1 
ATOM   4267 C  CG  . HIS   B 1 173 ? 48.649 0.461   31.151  1.00 8.83  ?  614  HIS   B CG  1 
ATOM   4268 N  ND1 . HIS   B 1 173 ? 48.006 0.125   29.969  1.00 9.41  ?  614  HIS   B ND1 1 
ATOM   4269 C  CD2 . HIS   B 1 173 ? 47.684 0.666   32.081  1.00 11.72 ?  614  HIS   B CD2 1 
ATOM   4270 C  CE1 . HIS   B 1 173 ? 46.696 0.113   30.202  1.00 10.03 ?  614  HIS   B CE1 1 
ATOM   4271 N  NE2 . HIS   B 1 173 ? 46.478 0.457   31.463  1.00 11.75 ?  614  HIS   B NE2 1 
ATOM   4272 N  N   . HIS   B 1 174 ? 52.647 2.031   32.575  1.00 10.40 ?  615  HIS   B N   1 
ATOM   4273 C  CA  . HIS   B 1 174 ? 54.077 1.903   32.794  1.00 9.15  ?  615  HIS   B CA  1 
ATOM   4274 C  C   . HIS   B 1 174 ? 54.540 0.517   32.362  1.00 9.00  ?  615  HIS   B C   1 
ATOM   4275 O  O   . HIS   B 1 174 ? 53.917 -0.487  32.706  1.00 10.63 ?  615  HIS   B O   1 
ATOM   4276 C  CB  . HIS   B 1 174 ? 54.378 2.102   34.279  1.00 10.10 ?  615  HIS   B CB  1 
ATOM   4277 C  CG  . HIS   B 1 174 ? 55.837 2.138   34.586  1.00 10.32 ?  615  HIS   B CG  1 
ATOM   4278 N  ND1 . HIS   B 1 174 ? 56.424 1.273   35.485  1.00 11.14 ?  615  HIS   B ND1 1 
ATOM   4279 C  CD2 . HIS   B 1 174 ? 56.821 2.957   34.146  1.00 11.05 ?  615  HIS   B CD2 1 
ATOM   4280 C  CE1 . HIS   B 1 174 ? 57.716 1.539   35.562  1.00 10.10 ?  615  HIS   B CE1 1 
ATOM   4281 N  NE2 . HIS   B 1 174 ? 57.988 2.548   34.751  1.00 10.56 ?  615  HIS   B NE2 1 
ATOM   4282 N  N   . GLY   B 1 175 ? 55.638 0.458   31.611  1.00 9.25  ?  616  GLY   B N   1 
ATOM   4283 C  CA  . GLY   B 1 175 ? 56.223 -0.826  31.271  1.00 10.05 ?  616  GLY   B CA  1 
ATOM   4284 C  C   . GLY   B 1 175 ? 57.135 -1.305  32.379  1.00 11.33 ?  616  GLY   B C   1 
ATOM   4285 O  O   . GLY   B 1 175 ? 58.362 -1.183  32.304  1.00 12.43 ?  616  GLY   B O   1 
ATOM   4286 N  N   . ASN   B 1 176 ? 56.515 -1.827  33.438  1.00 10.95 ?  617  ASN   B N   1 
ATOM   4287 C  CA  . ASN   B 1 176 ? 57.269 -2.257  34.620  1.00 11.14 ?  617  ASN   B CA  1 
ATOM   4288 C  C   . ASN   B 1 176 ? 58.351 -3.272  34.256  1.00 11.88 ?  617  ASN   B C   1 
ATOM   4289 O  O   . ASN   B 1 176 ? 59.469 -3.232  34.792  1.00 11.04 ?  617  ASN   B O   1 
ATOM   4290 C  CB  . ASN   B 1 176 ? 56.298 -2.863  35.639  1.00 12.21 ?  617  ASN   B CB  1 
ATOM   4291 C  CG  . ASN   B 1 176 ? 55.448 -3.966  35.028  1.00 13.27 ?  617  ASN   B CG  1 
ATOM   4292 O  OD1 . ASN   B 1 176 ? 54.469 -3.695  34.338  1.00 12.40 ?  617  ASN   B OD1 1 
ATOM   4293 N  ND2 . ASN   B 1 176 ? 55.833 -5.220  35.264  1.00 14.89 ?  617  ASN   B ND2 1 
ATOM   4294 N  N   . GLY   B 1 177 ? 58.043 -4.187  33.341  1.00 11.87 ?  618  GLY   B N   1 
ATOM   4295 C  CA  . GLY   B 1 177 ? 59.022 -5.188  32.964  1.00 12.94 ?  618  GLY   B CA  1 
ATOM   4296 C  C   . GLY   B 1 177 ? 60.233 -4.583  32.286  1.00 11.75 ?  618  GLY   B C   1 
ATOM   4297 O  O   . GLY   B 1 177 ? 61.368 -4.972  32.567  1.00 12.11 ?  618  GLY   B O   1 
ATOM   4298 N  N   . THR   B 1 178 ? 60.011 -3.650  31.351  1.00 10.03 ?  619  THR   B N   1 
ATOM   4299 C  CA  . THR   B 1 178 ? 61.126 -3.010  30.667  1.00 11.16 ?  619  THR   B CA  1 
ATOM   4300 C  C   . THR   B 1 178 ? 61.990 -2.232  31.648  1.00 10.48 ?  619  THR   B C   1 
ATOM   4301 O  O   . THR   B 1 178 ? 63.225 -2.346  31.625  1.00 10.75 ?  619  THR   B O   1 
ATOM   4302 C  CB  . THR   B 1 178 ? 60.612 -2.116  29.536  1.00 9.77  ?  619  THR   B CB  1 
ATOM   4303 O  OG1 . THR   B 1 178 ? 59.637 -2.850  28.782  1.00 11.29 ?  619  THR   B OG1 1 
ATOM   4304 C  CG2 . THR   B 1 178 ? 61.752 -1.732  28.614  1.00 13.03 ?  619  THR   B CG2 1 
ATOM   4305 N  N   . GLN   B 1 179 ? 61.358 -1.440  32.520  1.00 11.28 ?  620  GLN   B N   1 
ATOM   4306 C  CA  . GLN   B 1 179 ? 62.125 -0.725  33.543  1.00 10.12 ?  620  GLN   B CA  1 
ATOM   4307 C  C   . GLN   B 1 179 ? 62.993 -1.681  34.349  1.00 12.14 ?  620  GLN   B C   1 
ATOM   4308 O  O   . GLN   B 1 179 ? 64.196 -1.453  34.522  1.00 12.09 ?  620  GLN   B O   1 
ATOM   4309 C  CB  . GLN   B 1 179 ? 61.197 0.030   34.482  1.00 10.43 ?  620  GLN   B CB  1 
ATOM   4310 C  CG  . GLN   B 1 179 ? 61.955 0.536   35.698  1.00 11.58 ?  620  GLN   B CG  1 
ATOM   4311 C  CD  . GLN   B 1 179 ? 61.156 1.534   36.489  1.00 12.21 ?  620  GLN   B CD  1 
ATOM   4312 O  OE1 . GLN   B 1 179 ? 60.538 2.422   35.916  1.00 11.96 ?  620  GLN   B OE1 1 
ATOM   4313 N  NE2 . GLN   B 1 179 ? 61.155 1.396   37.812  1.00 12.81 ?  620  GLN   B NE2 1 
ATOM   4314 N  N   . HIS   B 1 180 ? 62.400 -2.768  34.831  1.00 11.49 ?  621  HIS   B N   1 
ATOM   4315 C  CA  . HIS   B 1 180 ? 63.136 -3.678  35.700  1.00 13.03 ?  621  HIS   B CA  1 
ATOM   4316 C  C   . HIS   B 1 180 ? 64.229 -4.411  34.951  1.00 12.72 ?  621  HIS   B C   1 
ATOM   4317 O  O   . HIS   B 1 180 ? 65.340 -4.553  35.466  1.00 13.73 ?  621  HIS   B O   1 
ATOM   4318 C  CB  . HIS   B 1 180 ? 62.188 -4.655  36.370  1.00 12.16 ?  621  HIS   B CB  1 
ATOM   4319 C  CG  . HIS   B 1 180 ? 61.314 -3.996  37.382  1.00 13.11 ?  621  HIS   B CG  1 
ATOM   4320 N  ND1 . HIS   B 1 180 ? 59.991 -4.334  37.572  1.00 14.15 ?  621  HIS   B ND1 1 
ATOM   4321 C  CD2 . HIS   B 1 180 ? 61.573 -2.981  38.242  1.00 15.66 ?  621  HIS   B CD2 1 
ATOM   4322 C  CE1 . HIS   B 1 180 ? 59.475 -3.561  38.514  1.00 16.65 ?  621  HIS   B CE1 1 
ATOM   4323 N  NE2 . HIS   B 1 180 ? 60.415 -2.733  38.936  1.00 17.20 ?  621  HIS   B NE2 1 
ATOM   4324 N  N   . ILE   B 1 181 ? 63.954 -4.862  33.729  1.00 12.16 ?  622  ILE   B N   1 
ATOM   4325 C  CA  . ILE   B 1 181 ? 64.975 -5.585  32.974  1.00 12.09 ?  622  ILE   B CA  1 
ATOM   4326 C  C   . ILE   B 1 181 ? 66.217 -4.722  32.780  1.00 13.40 ?  622  ILE   B C   1 
ATOM   4327 O  O   . ILE   B 1 181 ? 67.351 -5.215  32.850  1.00 13.82 ?  622  ILE   B O   1 
ATOM   4328 C  CB  . ILE   B 1 181 ? 64.397 -6.097  31.639  1.00 12.11 ?  622  ILE   B CB  1 
ATOM   4329 C  CG1 . ILE   B 1 181 ? 63.429 -7.250  31.913  1.00 12.15 ?  622  ILE   B CG1 1 
ATOM   4330 C  CG2 . ILE   B 1 181 ? 65.525 -6.522  30.666  1.00 11.91 ?  622  ILE   B CG2 1 
ATOM   4331 C  CD1 . ILE   B 1 181 ? 62.606 -7.678  30.711  1.00 11.98 ?  622  ILE   B CD1 1 
ATOM   4332 N  N   . PHE   B 1 182 ? 66.032 -3.423  32.540  1.00 12.21 ?  623  PHE   B N   1 
ATOM   4333 C  CA  . PHE   B 1 182 ? 67.146 -2.536  32.223  1.00 12.38 ?  623  PHE   B CA  1 
ATOM   4334 C  C   . PHE   B 1 182 ? 67.525 -1.605  33.370  1.00 11.85 ?  623  PHE   B C   1 
ATOM   4335 O  O   . PHE   B 1 182 ? 68.331 -0.692  33.169  1.00 13.64 ?  623  PHE   B O   1 
ATOM   4336 C  CB  . PHE   B 1 182 ? 66.854 -1.746  30.943  1.00 12.84 ?  623  PHE   B CB  1 
ATOM   4337 C  CG  . PHE   B 1 182 ? 66.652 -2.614  29.737  1.00 10.78 ?  623  PHE   B CG  1 
ATOM   4338 C  CD1 . PHE   B 1 182 ? 67.698 -3.369  29.238  1.00 11.70 ?  623  PHE   B CD1 1 
ATOM   4339 C  CD2 . PHE   B 1 182 ? 65.408 -2.685  29.118  1.00 11.24 ?  623  PHE   B CD2 1 
ATOM   4340 C  CE1 . PHE   B 1 182 ? 67.527 -4.172  28.133  1.00 11.63 ?  623  PHE   B CE1 1 
ATOM   4341 C  CE2 . PHE   B 1 182 ? 65.229 -3.488  28.017  1.00 11.70 ?  623  PHE   B CE2 1 
ATOM   4342 C  CZ  . PHE   B 1 182 ? 66.286 -4.235  27.508  1.00 11.31 ?  623  PHE   B CZ  1 
ATOM   4343 N  N   . GLU   B 1 183 ? 66.998 -1.836  34.572  1.00 11.83 ?  624  GLU   B N   1 
ATOM   4344 C  CA  . GLU   B 1 183 ? 67.158 -0.864  35.653  1.00 14.46 ?  624  GLU   B CA  1 
ATOM   4345 C  C   . GLU   B 1 183 ? 68.621 -0.611  36.000  1.00 15.28 ?  624  GLU   B C   1 
ATOM   4346 O  O   . GLU   B 1 183 ? 68.987 0.520   36.352  1.00 14.97 ?  624  GLU   B O   1 
ATOM   4347 C  CB  . GLU   B 1 183 ? 66.395 -1.325  36.895  1.00 16.32 ?  624  GLU   B CB  1 
ATOM   4348 C  CG  . GLU   B 1 183 ? 65.913 -0.178  37.768  1.00 19.66 ?  624  GLU   B CG  1 
ATOM   4349 C  CD  . GLU   B 1 183 ? 64.900 -0.612  38.806  1.00 22.92 ?  624  GLU   B CD  1 
ATOM   4350 O  OE1 . GLU   B 1 183 ? 64.747 -1.836  39.019  1.00 23.00 ?  624  GLU   B OE1 1 
ATOM   4351 O  OE2 . GLU   B 1 183 ? 64.255 0.277   39.405  1.00 26.04 -1 624  GLU   B OE2 1 
ATOM   4352 N  N   . GLU   B 1 184 ? 69.472 -1.627  35.884  1.00 15.12 ?  625  GLU   B N   1 
ATOM   4353 C  CA  . GLU   B 1 184 ? 70.894 -1.483  36.178  1.00 15.20 ?  625  GLU   B CA  1 
ATOM   4354 C  C   . GLU   B 1 184 ? 71.748 -1.399  34.919  1.00 15.68 ?  625  GLU   B C   1 
ATOM   4355 O  O   . GLU   B 1 184 ? 72.939 -1.735  34.944  1.00 18.28 ?  625  GLU   B O   1 
ATOM   4356 C  CB  . GLU   B 1 184 ? 71.379 -2.593  37.114  1.00 18.49 ?  625  GLU   B CB  1 
ATOM   4357 C  CG  . GLU   B 1 184 ? 70.693 -2.570  38.474  1.00 25.12 ?  625  GLU   B CG  1 
ATOM   4358 C  CD  . GLU   B 1 184 ? 70.947 -3.820  39.303  1.00 31.88 ?  625  GLU   B CD  1 
ATOM   4359 O  OE1 . GLU   B 1 184 ? 71.175 -4.897  38.711  1.00 35.15 ?  625  GLU   B OE1 1 
ATOM   4360 O  OE2 . GLU   B 1 184 ? 70.910 -3.726  40.548  1.00 33.76 -1 625  GLU   B OE2 1 
ATOM   4361 N  N   . ASP   B 1 185 ? 71.173 -0.930  33.818  1.00 15.80 ?  626  ASP   B N   1 
ATOM   4362 C  CA  . ASP   B 1 185 ? 71.843 -0.931  32.530  1.00 18.05 ?  626  ASP   B CA  1 
ATOM   4363 C  C   . ASP   B 1 185 ? 71.905 0.494   32.000  1.00 17.60 ?  626  ASP   B C   1 
ATOM   4364 O  O   . ASP   B 1 185 ? 70.893 1.202   32.000  1.00 17.57 ?  626  ASP   B O   1 
ATOM   4365 C  CB  . ASP   B 1 185 ? 71.052 -1.823  31.563  1.00 20.47 ?  626  ASP   B CB  1 
ATOM   4366 C  CG  . ASP   B 1 185 ? 71.851 -2.230  30.362  1.00 24.43 ?  626  ASP   B CG  1 
ATOM   4367 O  OD1 . ASP   B 1 185 ? 72.055 -1.377  29.478  0.55 26.48 ?  626  ASP   B OD1 1 
ATOM   4368 O  OD2 . ASP   B 1 185 ? 72.290 -3.397  30.302  0.59 23.87 -1 626  ASP   B OD2 1 
ATOM   4369 N  N   . ASP   B 1 186 ? 73.088 0.919   31.560  1.00 17.34 ?  627  ASP   B N   1 
ATOM   4370 C  CA  . ASP   B 1 186 ? 73.259 2.222   30.938  1.00 17.17 ?  627  ASP   B CA  1 
ATOM   4371 C  C   . ASP   B 1 186 ? 73.334 2.147   29.417  1.00 16.35 ?  627  ASP   B C   1 
ATOM   4372 O  O   . ASP   B 1 186 ? 73.448 3.189   28.763  1.00 16.92 ?  627  ASP   B O   1 
ATOM   4373 C  CB  . ASP   B 1 186 ? 74.481 2.951   31.528  1.00 20.85 ?  627  ASP   B CB  1 
ATOM   4374 C  CG  . ASP   B 1 186 ? 75.806 2.384   31.047  1.00 26.44 ?  627  ASP   B CG  1 
ATOM   4375 O  OD1 . ASP   B 1 186 ? 75.863 1.209   30.621  1.00 27.93 ?  627  ASP   B OD1 1 
ATOM   4376 O  OD2 . ASP   B 1 186 ? 76.809 3.126   31.114  1.00 29.82 -1 627  ASP   B OD2 1 
ATOM   4377 N  N   . SER   B 1 187 ? 73.237 0.949   28.833  1.00 13.70 ?  628  SER   B N   1 
ATOM   4378 C  CA  . SER   B 1 187 ? 73.218 0.821   27.380  1.00 13.52 ?  628  SER   B CA  1 
ATOM   4379 C  C   . SER   B 1 187 ? 71.820 0.946   26.793  1.00 12.30 ?  628  SER   B C   1 
ATOM   4380 O  O   . SER   B 1 187 ? 71.689 1.172   25.587  1.00 13.02 ?  628  SER   B O   1 
ATOM   4381 C  CB  . SER   B 1 187 ? 73.829 -0.519  26.951  1.00 14.82 ?  628  SER   B CB  1 
ATOM   4382 O  OG  . SER   B 1 187 ? 73.051 -1.625  27.393  1.00 14.98 ?  628  SER   B OG  1 
ATOM   4383 N  N   . VAL   B 1 188 ? 70.794 0.792   27.628  1.00 12.99 ?  629  VAL   B N   1 
ATOM   4384 C  CA  . VAL   B 1 188 ? 69.404 0.847   27.208  1.00 12.31 ?  629  VAL   B CA  1 
ATOM   4385 C  C   . VAL   B 1 188 ? 68.738 1.920   28.054  1.00 11.69 ?  629  VAL   B C   1 
ATOM   4386 O  O   . VAL   B 1 188 ? 68.531 1.737   29.265  1.00 13.18 ?  629  VAL   B O   1 
ATOM   4387 C  CB  . VAL   B 1 188 ? 68.698 -0.505  27.373  1.00 12.39 ?  629  VAL   B CB  1 
ATOM   4388 C  CG1 . VAL   B 1 188 ? 67.223 -0.393  26.944  1.00 14.53 ?  629  VAL   B CG1 1 
ATOM   4389 C  CG2 . VAL   B 1 188 ? 69.423 -1.579  26.569  1.00 11.66 ?  629  VAL   B CG2 1 
ATOM   4390 N  N   . LEU   B 1 189 ? 68.440 3.053   27.429  1.00 12.34 ?  630  LEU   B N   1 
ATOM   4391 C  CA  . LEU   B 1 189 ? 67.733 4.144   28.079  1.00 13.81 ?  630  LEU   B CA  1 
ATOM   4392 C  C   . LEU   B 1 189 ? 66.238 3.889   27.943  1.00 12.66 ?  630  LEU   B C   1 
ATOM   4393 O  O   . LEU   B 1 189 ? 65.727 3.753   26.824  1.00 12.26 ?  630  LEU   B O   1 
ATOM   4394 C  CB  . LEU   B 1 189 ? 68.106 5.466   27.408  1.00 14.57 ?  630  LEU   B CB  1 
ATOM   4395 C  CG  . LEU   B 1 189 ? 67.346 6.737   27.800  1.00 13.69 ?  630  LEU   B CG  1 
ATOM   4396 C  CD1 . LEU   B 1 189 ? 67.473 7.023   29.299  1.00 13.36 ?  630  LEU   B CD1 1 
ATOM   4397 C  CD2 . LEU   B 1 189 ? 67.841 7.922   26.999  1.00 14.92 ?  630  LEU   B CD2 1 
ATOM   4398 N  N   . TYR   B 1 190 ? 65.542 3.814   29.069  1.00 11.22 ?  631  TYR   B N   1 
ATOM   4399 C  CA  . TYR   B 1 190 ? 64.106 3.573   29.079  1.00 11.56 ?  631  TYR   B CA  1 
ATOM   4400 C  C   . TYR   B 1 190 ? 63.397 4.875   29.429  1.00 12.01 ?  631  TYR   B C   1 
ATOM   4401 O  O   . TYR   B 1 190 ? 63.679 5.479   30.469  1.00 12.10 ?  631  TYR   B O   1 
ATOM   4402 C  CB  . TYR   B 1 190 ? 63.753 2.462   30.072  1.00 11.56 ?  631  TYR   B CB  1 
ATOM   4403 C  CG  . TYR   B 1 190 ? 62.272 2.175   30.130  1.00 11.69 ?  631  TYR   B CG  1 
ATOM   4404 C  CD1 . TYR   B 1 190 ? 61.604 1.713   29.009  1.00 10.36 ?  631  TYR   B CD1 1 
ATOM   4405 C  CD2 . TYR   B 1 190 ? 61.539 2.415   31.278  1.00 11.51 ?  631  TYR   B CD2 1 
ATOM   4406 C  CE1 . TYR   B 1 190 ? 60.246 1.465   29.038  1.00 10.31 ?  631  TYR   B CE1 1 
ATOM   4407 C  CE2 . TYR   B 1 190 ? 60.183 2.176   31.318  1.00 11.88 ?  631  TYR   B CE2 1 
ATOM   4408 C  CZ  . TYR   B 1 190 ? 59.541 1.704   30.182  1.00 11.45 ?  631  TYR   B CZ  1 
ATOM   4409 O  OH  . TYR   B 1 190 ? 58.183 1.459   30.213  1.00 11.06 ?  631  TYR   B OH  1 
ATOM   4410 N  N   . ILE   B 1 191 ? 62.510 5.331   28.546  1.00 11.16 ?  632  ILE   B N   1 
ATOM   4411 C  CA  . ILE   B 1 191 ? 61.709 6.528   28.792  1.00 11.60 ?  632  ILE   B CA  1 
ATOM   4412 C  C   . ILE   B 1 191 ? 60.249 6.133   28.655  1.00 11.37 ?  632  ILE   B C   1 
ATOM   4413 O  O   . ILE   B 1 191 ? 59.815 5.738   27.571  1.00 12.77 ?  632  ILE   B O   1 
ATOM   4414 C  CB  . ILE   B 1 191 ? 62.051 7.675   27.826  1.00 11.91 ?  632  ILE   B CB  1 
ATOM   4415 C  CG1 . ILE   B 1 191 ? 63.543 8.008   27.876  1.00 12.37 ?  632  ILE   B CG1 1 
ATOM   4416 C  CG2 . ILE   B 1 191 ? 61.192 8.914   28.142  1.00 12.17 ?  632  ILE   B CG2 1 
ATOM   4417 C  CD1 . ILE   B 1 191 ? 63.911 9.280   27.113  1.00 13.90 ?  632  ILE   B CD1 1 
ATOM   4418 N  N   . SER   B 1 192 ? 59.497 6.221   29.747  1.00 10.14 ?  633  SER   B N   1 
ATOM   4419 C  CA  . SER   B 1 192 ? 58.086 5.866   29.749  1.00 10.62 ?  633  SER   B CA  1 
ATOM   4420 C  C   . SER   B 1 192 ? 57.259 7.094   30.088  1.00 9.88  ?  633  SER   B C   1 
ATOM   4421 O  O   . SER   B 1 192 ? 57.581 7.817   31.039  1.00 11.44 ?  633  SER   B O   1 
ATOM   4422 C  CB  . SER   B 1 192 ? 57.792 4.782   30.781  1.00 10.20 ?  633  SER   B CB  1 
ATOM   4423 O  OG  . SER   B 1 192 ? 56.405 4.470   30.773  1.00 11.84 ?  633  SER   B OG  1 
ATOM   4424 N  N   . LEU   B 1 193 ? 56.187 7.315   29.327  1.00 11.63 ?  634  LEU   B N   1 
ATOM   4425 C  CA  . LEU   B 1 193 ? 55.122 8.239   29.714  1.00 10.87 ?  634  LEU   B CA  1 
ATOM   4426 C  C   . LEU   B 1 193 ? 53.918 7.387   30.079  1.00 9.78  ?  634  LEU   B C   1 
ATOM   4427 O  O   . LEU   B 1 193 ? 53.604 6.423   29.363  1.00 10.74 ?  634  LEU   B O   1 
ATOM   4428 C  CB  . LEU   B 1 193 ? 54.738 9.188   28.572  1.00 12.18 ?  634  LEU   B CB  1 
ATOM   4429 C  CG  . LEU   B 1 193 ? 55.889 9.909   27.872  1.00 12.52 ?  634  LEU   B CG  1 
ATOM   4430 C  CD1 . LEU   B 1 193 ? 56.342 9.131   26.663  1.00 11.98 ?  634  LEU   B CD1 1 
ATOM   4431 C  CD2 . LEU   B 1 193 ? 55.455 11.322  27.478  1.00 13.20 ?  634  LEU   B CD2 1 
ATOM   4432 N  N   . HIS   B 1 194 ? 53.266 7.703   31.200  1.00 10.30 ?  635  HIS   B N   1 
ATOM   4433 C  CA  . HIS   B 1 194 ? 52.191 6.814   31.603  1.00 11.13 ?  635  HIS   B CA  1 
ATOM   4434 C  C   . HIS   B 1 194 ? 51.267 7.489   32.600  1.00 11.22 ?  635  HIS   B C   1 
ATOM   4435 O  O   . HIS   B 1 194 ? 51.692 8.317   33.417  1.00 12.17 ?  635  HIS   B O   1 
ATOM   4436 C  CB  . HIS   B 1 194 ? 52.756 5.547   32.247  1.00 11.61 ?  635  HIS   B CB  1 
ATOM   4437 C  CG  . HIS   B 1 194 ? 53.882 5.819   33.199  1.00 10.02 ?  635  HIS   B CG  1 
ATOM   4438 N  ND1 . HIS   B 1 194 ? 55.182 5.951   32.774  1.00 11.36 ?  635  HIS   B ND1 1 
ATOM   4439 C  CD2 . HIS   B 1 194 ? 53.907 6.019   34.539  1.00 10.49 ?  635  HIS   B CD2 1 
ATOM   4440 C  CE1 . HIS   B 1 194 ? 55.967 6.211   33.801  1.00 11.82 ?  635  HIS   B CE1 1 
ATOM   4441 N  NE2 . HIS   B 1 194 ? 55.218 6.255   34.888  1.00 11.94 ?  635  HIS   B NE2 1 
ATOM   4442 N  N   . ARG   B 1 195 ? 50.003 7.079   32.551  1.00 10.37 ?  636  ARG   B N   1 
ATOM   4443 C  CA  . ARG   B 1 195 ? 49.061 7.461   33.589  1.00 11.67 ?  636  ARG   B CA  1 
ATOM   4444 C  C   . ARG   B 1 195 ? 49.459 6.779   34.892  1.00 12.10 ?  636  ARG   B C   1 
ATOM   4445 O  O   . ARG   B 1 195 ? 49.669 5.565   34.932  1.00 12.83 ?  636  ARG   B O   1 
ATOM   4446 C  CB  . ARG   B 1 195 ? 47.647 7.053   33.175  1.00 12.09 ?  636  ARG   B CB  1 
ATOM   4447 C  CG  . ARG   B 1 195 ? 46.590 7.550   34.145  1.00 12.10 ?  636  ARG   B CG  1 
ATOM   4448 C  CD  . ARG   B 1 195 ? 45.212 7.399   33.552  1.00 13.31 ?  636  ARG   B CD  1 
ATOM   4449 N  NE  . ARG   B 1 195 ? 44.188 7.859   34.480  1.00 15.47 ?  636  ARG   B NE  1 
ATOM   4450 C  CZ  . ARG   B 1 195 ? 42.883 7.670   34.314  1.00 14.93 ?  636  ARG   B CZ  1 
ATOM   4451 N  NH1 . ARG   B 1 195 ? 42.419 7.027   33.248  1.00 16.30 ?  636  ARG   B NH1 1 
ATOM   4452 N  NH2 . ARG   B 1 195 ? 42.039 8.117   35.237  1.00 18.31 ?  636  ARG   B NH2 1 
ATOM   4453 N  N   . TYR   B 1 196 ? 49.584 7.565   35.955  1.00 10.45 ?  637  TYR   B N   1 
ATOM   4454 C  CA  . TYR   B 1 196 ? 50.118 7.073   37.217  1.00 10.78 ?  637  TYR   B CA  1 
ATOM   4455 C  C   . TYR   B 1 196 ? 49.124 7.217   38.358  1.00 11.86 ?  637  TYR   B C   1 
ATOM   4456 O  O   . TYR   B 1 196 ? 48.875 6.248   39.090  1.00 13.14 ?  637  TYR   B O   1 
ATOM   4457 C  CB  . TYR   B 1 196 ? 51.425 7.830   37.504  1.00 11.74 ?  637  TYR   B CB  1 
ATOM   4458 C  CG  . TYR   B 1 196 ? 52.133 7.431   38.783  1.00 12.30 ?  637  TYR   B CG  1 
ATOM   4459 C  CD1 . TYR   B 1 196 ? 52.616 6.133   38.974  1.00 12.37 ?  637  TYR   B CD1 1 
ATOM   4460 C  CD2 . TYR   B 1 196 ? 52.336 8.361   39.790  1.00 12.33 ?  637  TYR   B CD2 1 
ATOM   4461 C  CE1 . TYR   B 1 196 ? 53.278 5.771   40.162  1.00 12.57 ?  637  TYR   B CE1 1 
ATOM   4462 C  CE2 . TYR   B 1 196 ? 52.984 8.007   40.972  1.00 12.61 ?  637  TYR   B CE2 1 
ATOM   4463 C  CZ  . TYR   B 1 196 ? 53.445 6.717   41.145  1.00 14.02 ?  637  TYR   B CZ  1 
ATOM   4464 O  OH  . TYR   B 1 196 ? 54.076 6.364   42.324  1.00 14.49 ?  637  TYR   B OH  1 
ATOM   4465 N  N   . GLU   B 1 197 ? 48.552 8.403   38.534  1.00 13.02 ?  638  GLU   B N   1 
ATOM   4466 C  CA  . GLU   B 1 197 ? 47.566 8.662   39.584  1.00 13.71 ?  638  GLU   B CA  1 
ATOM   4467 C  C   . GLU   B 1 197 ? 48.095 8.271   40.964  1.00 13.37 ?  638  GLU   B C   1 
ATOM   4468 O  O   . GLU   B 1 197 ? 47.447 7.545   41.721  1.00 15.13 ?  638  GLU   B O   1 
ATOM   4469 C  CB  . GLU   B 1 197 ? 46.229 7.981   39.278  1.00 14.24 ?  638  GLU   B CB  1 
ATOM   4470 C  CG  . GLU   B 1 197 ? 45.710 8.173   37.847  1.00 15.85 ?  638  GLU   B CG  1 
ATOM   4471 C  CD  . GLU   B 1 197 ? 45.362 9.616   37.506  1.00 15.66 ?  638  GLU   B CD  1 
ATOM   4472 O  OE1 . GLU   B 1 197 ? 45.460 10.494  38.391  1.00 17.82 ?  638  GLU   B OE1 1 
ATOM   4473 O  OE2 . GLU   B 1 197 ? 44.992 9.878   36.340  1.00 16.40 -1 638  GLU   B OE2 1 
ATOM   4474 N  N   . ASP   B 1 198 ? 49.309 8.729   41.267  1.00 14.00 ?  639  ASP   B N   1 
ATOM   4475 C  CA  . ASP   B 1 198 ? 49.945 8.469   42.565  1.00 17.77 ?  639  ASP   B CA  1 
ATOM   4476 C  C   . ASP   B 1 198 ? 49.994 6.976   42.896  1.00 19.19 ?  639  ASP   B C   1 
ATOM   4477 O  O   . ASP   B 1 198 ? 49.835 6.567   44.052  1.00 20.71 ?  639  ASP   B O   1 
ATOM   4478 C  CB  . ASP   B 1 198 ? 49.296 9.280   43.690  1.00 23.08 ?  639  ASP   B CB  1 
ATOM   4479 C  CG  . ASP   B 1 198 ? 49.337 10.774  43.425  1.00 30.01 ?  639  ASP   B CG  1 
ATOM   4480 O  OD1 . ASP   B 1 198 ? 50.392 11.272  42.973  1.00 30.99 ?  639  ASP   B OD1 1 
ATOM   4481 O  OD2 . ASP   B 1 198 ? 48.313 11.451  43.662  1.00 35.42 -1 639  ASP   B OD2 1 
ATOM   4482 N  N   . GLY   B 1 199 ? 50.203 6.148   41.862  1.00 15.84 ?  640  GLY   B N   1 
ATOM   4483 C  CA  . GLY   B 1 199 ? 50.335 4.718   42.035  1.00 15.85 ?  640  GLY   B CA  1 
ATOM   4484 C  C   . GLY   B 1 199 ? 49.050 3.924   41.977  1.00 14.21 ?  640  GLY   B C   1 
ATOM   4485 O  O   . GLY   B 1 199 ? 49.099 2.693   42.133  1.00 16.36 ?  640  GLY   B O   1 
ATOM   4486 N  N   . ALA   B 1 200 ? 47.913 4.568   41.743  1.00 14.48 ?  641  ALA   B N   1 
ATOM   4487 C  CA  . ALA   B 1 200 ? 46.632 3.869   41.764  1.00 16.71 ?  641  ALA   B CA  1 
ATOM   4488 C  C   . ALA   B 1 200 ? 46.248 3.233   40.433  1.00 19.96 ?  641  ALA   B C   1 
ATOM   4489 O  O   . ALA   B 1 200 ? 45.364 2.368   40.412  1.00 23.35 ?  641  ALA   B O   1 
ATOM   4490 C  CB  . ALA   B 1 200 ? 45.507 4.803   42.238  1.00 19.11 ?  641  ALA   B CB  1 
ATOM   4491 N  N   . PHE   B 1 201 ? 46.889 3.622   39.336  1.00 14.63 ?  642  PHE   B N   1 
ATOM   4492 C  CA  . PHE   B 1 201 ? 46.572 3.103   38.009  1.00 14.13 ?  642  PHE   B CA  1 
ATOM   4493 C  C   . PHE   B 1 201 ? 47.434 1.884   37.687  1.00 11.28 ?  642  PHE   B C   1 
ATOM   4494 O  O   . PHE   B 1 201 ? 48.603 1.813   38.080  1.00 14.36 ?  642  PHE   B O   1 
ATOM   4495 C  CB  . PHE   B 1 201 ? 46.834 4.199   36.972  1.00 14.36 ?  642  PHE   B CB  1 
ATOM   4496 C  CG  . PHE   B 1 201 ? 46.095 4.000   35.667  1.00 14.21 ?  642  PHE   B CG  1 
ATOM   4497 C  CD1 . PHE   B 1 201 ? 44.713 4.139   35.598  1.00 16.11 ?  642  PHE   B CD1 1 
ATOM   4498 C  CD2 . PHE   B 1 201 ? 46.783 3.666   34.502  1.00 14.55 ?  642  PHE   B CD2 1 
ATOM   4499 C  CE1 . PHE   B 1 201 ? 44.034 3.950   34.394  1.00 17.93 ?  642  PHE   B CE1 1 
ATOM   4500 C  CE2 . PHE   B 1 201 ? 46.100 3.478   33.304  1.00 15.67 ?  642  PHE   B CE2 1 
ATOM   4501 C  CZ  . PHE   B 1 201 ? 44.736 3.619   33.254  1.00 17.53 ?  642  PHE   B CZ  1 
ATOM   4502 N  N   . PHE   B 1 202 ? 46.853 0.928   36.941  1.00 13.70 ?  643  PHE   B N   1 
ATOM   4503 C  CA  . PHE   B 1 202 ? 47.579 -0.291  36.593  1.00 12.72 ?  643  PHE   B CA  1 
ATOM   4504 C  C   . PHE   B 1 202 ? 48.930 0.067   35.973  1.00 13.22 ?  643  PHE   B C   1 
ATOM   4505 O  O   . PHE   B 1 202 ? 48.992 0.948   35.106  1.00 12.92 ?  643  PHE   B O   1 
ATOM   4506 C  CB  . PHE   B 1 202 ? 46.785 -1.117  35.574  1.00 13.52 ?  643  PHE   B CB  1 
ATOM   4507 C  CG  . PHE   B 1 202 ? 47.388 -2.475  35.300  1.00 13.63 ?  643  PHE   B CG  1 
ATOM   4508 C  CD1 . PHE   B 1 202 ? 48.344 -2.646  34.298  1.00 14.07 ?  643  PHE   B CD1 1 
ATOM   4509 C  CD2 . PHE   B 1 202 ? 47.017 -3.580  36.062  1.00 14.37 ?  643  PHE   B CD2 1 
ATOM   4510 C  CE1 . PHE   B 1 202 ? 48.922 -3.886  34.070  1.00 15.40 ?  643  PHE   B CE1 1 
ATOM   4511 C  CE2 . PHE   B 1 202 ? 47.591 -4.823  35.830  1.00 15.43 ?  643  PHE   B CE2 1 
ATOM   4512 C  CZ  . PHE   B 1 202 ? 48.543 -4.974  34.831  1.00 16.60 ?  643  PHE   B CZ  1 
ATOM   4513 N  N   . PRO   B 1 203 ? 50.029 -0.622  36.346  1.00 12.61 ?  644  PRO   B N   1 
ATOM   4514 C  CA  . PRO   B 1 203 ? 50.119 -1.819  37.192  1.00 11.66 ?  644  PRO   B CA  1 
ATOM   4515 C  C   . PRO   B 1 203 ? 50.250 -1.569  38.706  1.00 14.14 ?  644  PRO   B C   1 
ATOM   4516 O  O   . PRO   B 1 203 ? 50.693 -2.470  39.419  1.00 15.78 ?  644  PRO   B O   1 
ATOM   4517 C  CB  . PRO   B 1 203 ? 51.369 -2.519  36.647  1.00 13.61 ?  644  PRO   B CB  1 
ATOM   4518 C  CG  . PRO   B 1 203 ? 52.245 -1.407  36.249  1.00 15.11 ?  644  PRO   B CG  1 
ATOM   4519 C  CD  . PRO   B 1 203 ? 51.337 -0.311  35.734  1.00 12.55 ?  644  PRO   B CD  1 
ATOM   4520 N  N   . ASN   B 1 204 ? 49.884 -0.373  39.176  1.00 13.71 ?  645  ASN   B N   1 
ATOM   4521 C  CA  . ASN   B 1 204 ? 49.611 -0.147  40.601  1.00 15.02 ?  645  ASN   B CA  1 
ATOM   4522 C  C   . ASN   B 1 204 ? 50.870 -0.188  41.471  1.00 14.76 ?  645  ASN   B C   1 
ATOM   4523 O  O   . ASN   B 1 204 ? 50.814 -0.629  42.622  1.00 17.35 ?  645  ASN   B O   1 
ATOM   4524 C  CB  . ASN   B 1 204 ? 48.557 -1.122  41.139  1.00 15.63 ?  645  ASN   B CB  1 
ATOM   4525 C  CG  . ASN   B 1 204 ? 47.282 -1.097  40.333  1.00 18.87 ?  645  ASN   B CG  1 
ATOM   4526 O  OD1 . ASN   B 1 204 ? 47.063 -1.953  39.481  1.00 21.52 ?  645  ASN   B OD1 1 
ATOM   4527 N  ND2 . ASN   B 1 204 ? 46.430 -0.112  40.596  1.00 21.94 ?  645  ASN   B ND2 1 
ATOM   4528 N  N   . SER   B 1 205 ? 51.997 0.292   40.949  1.00 14.40 ?  646  SER   B N   1 
ATOM   4529 C  CA  . SER   B 1 205 ? 53.263 0.281   41.668  1.00 15.14 ?  646  SER   B CA  1 
ATOM   4530 C  C   . SER   B 1 205 ? 53.907 1.660   41.667  1.00 15.13 ?  646  SER   B C   1 
ATOM   4531 O  O   . SER   B 1 205 ? 53.927 2.353   40.640  1.00 14.37 ?  646  SER   B O   1 
ATOM   4532 C  CB  . SER   B 1 205 ? 54.238 -0.731  41.049  1.00 16.16 ?  646  SER   B CB  1 
ATOM   4533 O  OG  . SER   B 1 205 ? 55.507 -0.678  41.688  1.00 16.49 ?  646  SER   B OG  1 
ATOM   4534 N  N   . GLU   B 1 206 ? 54.490 2.035   42.814  1.00 13.62 ?  647  GLU   B N   1 
ATOM   4535 C  CA  . GLU   B 1 206 ? 55.234 3.284   42.867  1.00 13.28 ?  647  GLU   B CA  1 
ATOM   4536 C  C   . GLU   B 1 206 ? 56.571 3.214   42.145  1.00 12.31 ?  647  GLU   B C   1 
ATOM   4537 O  O   . GLU   B 1 206 ? 57.273 4.229   42.071  1.00 13.02 ?  647  GLU   B O   1 
ATOM   4538 C  CB  . GLU   B 1 206 ? 55.390 3.739   44.316  1.00 12.86 ?  647  GLU   B CB  1 
ATOM   4539 C  CG  . GLU   B 1 206 ? 54.045 4.018   44.961  1.00 15.03 ?  647  GLU   B CG  1 
ATOM   4540 C  CD  . GLU   B 1 206 ? 54.176 4.737   46.284  1.00 21.41 ?  647  GLU   B CD  1 
ATOM   4541 O  OE1 . GLU   B 1 206 ? 55.022 5.647   46.392  1.00 26.00 ?  647  GLU   B OE1 1 
ATOM   4542 O  OE2 . GLU   B 1 206 ? 53.427 4.388   47.212  1.00 20.88 -1 647  GLU   B OE2 1 
ATOM   4543 N  N   . ASP   B 1 207 ? 56.938 2.042   41.608  1.00 12.95 ?  648  ASP   B N   1 
ATOM   4544 C  CA  . ASP   B 1 207 ? 58.108 1.941   40.742  1.00 13.19 ?  648  ASP   B CA  1 
ATOM   4545 C  C   . ASP   B 1 207 ? 57.999 2.855   39.527  1.00 10.36 ?  648  ASP   B C   1 
ATOM   4546 O  O   . ASP   B 1 207 ? 59.023 3.191   38.919  1.00 13.91 ?  648  ASP   B O   1 
ATOM   4547 C  CB  . ASP   B 1 207 ? 58.237 0.515   40.220  1.00 14.92 ?  648  ASP   B CB  1 
ATOM   4548 C  CG  . ASP   B 1 207 ? 58.498 -0.499  41.305  1.00 20.68 ?  648  ASP   B CG  1 
ATOM   4549 O  OD1 . ASP   B 1 207 ? 58.697 -0.112  42.481  1.00 22.80 ?  648  ASP   B OD1 1 
ATOM   4550 O  OD2 . ASP   B 1 207 ? 58.505 -1.701  40.964  1.00 19.22 -1 648  ASP   B OD2 1 
ATOM   4551 N  N   . ALA   B 1 208 ? 56.790 3.264   39.176  1.00 10.31 ?  649  ALA   B N   1 
ATOM   4552 C  CA  . ALA   B 1 208 ? 56.538 4.087   38.005  1.00 10.74 ?  649  ALA   B CA  1 
ATOM   4553 C  C   . ALA   B 1 208 ? 56.688 5.579   38.278  1.00 10.54 ?  649  ALA   B C   1 
ATOM   4554 O  O   . ALA   B 1 208 ? 56.488 6.383   37.359  1.00 11.78 ?  649  ALA   B O   1 
ATOM   4555 C  CB  . ALA   B 1 208 ? 55.135 3.790   37.487  1.00 12.93 ?  649  ALA   B CB  1 
ATOM   4556 N  N   . ASN   B 1 209 ? 57.022 5.978   39.506  1.00 13.10 ?  650  ASN   B N   1 
ATOM   4557 C  CA  . ASN   B 1 209 ? 57.118 7.402   39.801  1.00 12.32 ?  650  ASN   B CA  1 
ATOM   4558 C  C   . ASN   B 1 209 ? 58.404 8.004   39.232  1.00 11.75 ?  650  ASN   B C   1 
ATOM   4559 O  O   . ASN   B 1 209 ? 59.358 7.298   38.894  1.00 10.90 ?  650  ASN   B O   1 
ATOM   4560 C  CB  . ASN   B 1 209 ? 57.020 7.664   41.307  1.00 12.36 ?  650  ASN   B CB  1 
ATOM   4561 C  CG  . ASN   B 1 209 ? 56.332 8.979   41.613  1.00 13.05 ?  650  ASN   B CG  1 
ATOM   4562 O  OD1 . ASN   B 1 209 ? 56.042 9.767   40.713  1.00 13.68 ?  650  ASN   B OD1 1 
ATOM   4563 N  ND2 . ASN   B 1 209 ? 56.054 9.218   42.896  1.00 15.51 ?  650  ASN   B ND2 1 
ATOM   4564 N  N   . TYR   B 1 210 ? 58.423 9.344   39.164  1.00 11.83 ?  651  TYR   B N   1 
ATOM   4565 C  CA  . TYR   B 1 210 ? 59.507 10.071  38.511  1.00 13.24 ?  651  TYR   B CA  1 
ATOM   4566 C  C   . TYR   B 1 210 ? 60.834 9.937   39.235  1.00 12.37 ?  651  TYR   B C   1 
ATOM   4567 O  O   . TYR   B 1 210 ? 61.874 10.187  38.621  1.00 12.83 ?  651  TYR   B O   1 
ATOM   4568 C  CB  . TYR   B 1 210 ? 59.162 11.557  38.384  1.00 11.27 ?  651  TYR   B CB  1 
ATOM   4569 C  CG  . TYR   B 1 210 ? 58.912 12.243  39.714  1.00 14.05 ?  651  TYR   B CG  1 
ATOM   4570 C  CD1 . TYR   B 1 210 ? 59.957 12.743  40.472  1.00 16.66 ?  651  TYR   B CD1 1 
ATOM   4571 C  CD2 . TYR   B 1 210 ? 57.625 12.385  40.197  1.00 15.31 ?  651  TYR   B CD2 1 
ATOM   4572 C  CE1 . TYR   B 1 210 ? 59.722 13.357  41.693  1.00 19.89 ?  651  TYR   B CE1 1 
ATOM   4573 C  CE2 . TYR   B 1 210 ? 57.377 12.997  41.411  1.00 18.33 ?  651  TYR   B CE2 1 
ATOM   4574 C  CZ  . TYR   B 1 210 ? 58.433 13.481  42.152  1.00 21.40 ?  651  TYR   B CZ  1 
ATOM   4575 O  OH  . TYR   B 1 210 ? 58.191 14.100  43.358  1.00 24.93 ?  651  TYR   B OH  1 
ATOM   4576 N  N   . ASP   B 1 211 ? 60.821 9.578   40.523  1.00 13.97 ?  652  ASP   B N   1 
ATOM   4577 C  CA  . ASP   B 1 211 ? 62.056 9.496   41.294  1.00 14.31 ?  652  ASP   B CA  1 
ATOM   4578 C  C   . ASP   B 1 211 ? 62.793 8.179   41.097  1.00 15.51 ?  652  ASP   B C   1 
ATOM   4579 O  O   . ASP   B 1 211 ? 63.867 7.984   41.682  1.00 16.03 ?  652  ASP   B O   1 
ATOM   4580 C  CB  . ASP   B 1 211 ? 61.818 9.801   42.792  1.00 16.02 ?  652  ASP   B CB  1 
ATOM   4581 C  CG  . ASP   B 1 211 ? 60.853 8.832   43.469  1.00 19.22 ?  652  ASP   B CG  1 
ATOM   4582 O  OD1 . ASP   B 1 211 ? 60.069 8.145   42.789  1.00 16.77 ?  652  ASP   B OD1 1 
ATOM   4583 O  OD2 . ASP   B 1 211 ? 60.850 8.787   44.722  1.00 23.82 -1 652  ASP   B OD2 1 
ATOM   4584 N  N   . LYS   B 1 212 ? 62.251 7.275   40.287  1.00 12.50 ?  653  LYS   B N   1 
ATOM   4585 C  CA  . LYS   B 1 212 ? 62.939 6.028   39.974  1.00 13.15 ?  653  LYS   B CA  1 
ATOM   4586 C  C   . LYS   B 1 212 ? 63.793 6.294   38.739  1.00 11.88 ?  653  LYS   B C   1 
ATOM   4587 O  O   . LYS   B 1 212 ? 63.303 6.268   37.602  1.00 13.11 ?  653  LYS   B O   1 
ATOM   4588 C  CB  . LYS   B 1 212 ? 61.941 4.887   39.813  1.00 16.28 ?  653  LYS   B CB  1 
ATOM   4589 C  CG  . LYS   B 1 212 ? 60.851 4.847   40.921  1.00 20.43 ?  653  LYS   B CG  1 
ATOM   4590 C  CD  . LYS   B 1 212 ? 61.409 4.854   42.337  1.00 23.73 ?  653  LYS   B CD  1 
ATOM   4591 C  CE  . LYS   B 1 212 ? 60.320 4.455   43.340  1.00 19.83 ?  653  LYS   B CE  1 
ATOM   4592 N  NZ  . LYS   B 1 212 ? 59.280 5.509   43.613  1.00 17.31 ?  653  LYS   B NZ  1 
ATOM   4593 N  N   . VAL   B 1 213 ? 65.074 6.601   38.968  1.00 12.01 ?  654  VAL   B N   1 
ATOM   4594 C  CA  . VAL   B 1 213 ? 65.985 7.022   37.909  1.00 12.60 ?  654  VAL   B CA  1 
ATOM   4595 C  C   . VAL   B 1 213 ? 66.915 5.914   37.455  1.00 9.18  ?  654  VAL   B C   1 
ATOM   4596 O  O   . VAL   B 1 213 ? 67.781 6.155   36.600  1.00 13.49 ?  654  VAL   B O   1 
ATOM   4597 C  CB  . VAL   B 1 213 ? 66.807 8.255   38.328  1.00 13.52 ?  654  VAL   B CB  1 
ATOM   4598 C  CG1 . VAL   B 1 213 ? 65.885 9.424   38.659  1.00 14.85 ?  654  VAL   B CG1 1 
ATOM   4599 C  CG2 . VAL   B 1 213 ? 67.705 7.913   39.529  1.00 15.06 ?  654  VAL   B CG2 1 
ATOM   4600 N  N   . GLY   B 1 214 ? 66.773 4.715   37.999  1.00 12.95 ?  655  GLY   B N   1 
ATOM   4601 C  CA  . GLY   B 1 214 ? 67.680 3.617   37.737  1.00 13.38 ?  655  GLY   B CA  1 
ATOM   4602 C  C   . GLY   B 1 214 ? 68.542 3.307   38.951  1.00 12.88 ?  655  GLY   B C   1 
ATOM   4603 O  O   . GLY   B 1 214 ? 68.580 4.045   39.936  1.00 14.44 ?  655  GLY   B O   1 
ATOM   4604 N  N   . LEU   B 1 215 ? 69.271 2.194   38.847  1.00 12.52 ?  656  LEU   B N   1 
ATOM   4605 C  CA  . LEU   B 1 215 ? 70.057 1.680   39.964  1.00 13.25 ?  656  LEU   B CA  1 
ATOM   4606 C  C   . LEU   B 1 215 ? 71.445 1.290   39.482  1.00 13.87 ?  656  LEU   B C   1 
ATOM   4607 O  O   . LEU   B 1 215 ? 71.620 0.861   38.346  1.00 13.61 ?  656  LEU   B O   1 
ATOM   4608 C  CB  . LEU   B 1 215 ? 69.395 0.440   40.569  1.00 14.96 ?  656  LEU   B CB  1 
ATOM   4609 C  CG  . LEU   B 1 215 ? 68.017 0.619   41.219  1.00 17.27 ?  656  LEU   B CG  1 
ATOM   4610 C  CD1 . LEU   B 1 215 ? 67.413 -0.724  41.607  1.00 19.26 ?  656  LEU   B CD1 1 
ATOM   4611 C  CD2 . LEU   B 1 215 ? 68.084 1.532   42.433  1.00 17.77 ?  656  LEU   B CD2 1 
ATOM   4612 N  N   . GLY   B 1 216 ? 72.437 1.431   40.371  1.00 13.28 ?  657  GLY   B N   1 
ATOM   4613 C  CA  . GLY   B 1 216 ? 73.794 1.027   40.032  1.00 15.33 ?  657  GLY   B CA  1 
ATOM   4614 C  C   . GLY   B 1 216 ? 74.310 1.740   38.797  1.00 13.87 ?  657  GLY   B C   1 
ATOM   4615 O  O   . GLY   B 1 216 ? 74.208 2.964   38.665  1.00 15.04 ?  657  GLY   B O   1 
ATOM   4616 N  N   . LYS   B 1 217 ? 74.864 0.957   37.875  1.00 15.90 ?  658  LYS   B N   1 
ATOM   4617 C  CA  . LYS   B 1 217 ? 75.358 1.438   36.592  1.00 18.48 ?  658  LYS   B CA  1 
ATOM   4618 C  C   . LYS   B 1 217 ? 74.282 2.209   35.833  1.00 17.47 ?  658  LYS   B C   1 
ATOM   4619 O  O   . LYS   B 1 217 ? 74.587 3.044   34.973  1.00 18.49 ?  658  LYS   B O   1 
ATOM   4620 C  CB  . LYS   B 1 217 ? 75.752 0.232   35.749  1.00 24.94 ?  658  LYS   B CB  1 
ATOM   4621 C  CG  . LYS   B 1 217 ? 76.357 0.550   34.393  1.00 29.76 ?  658  LYS   B CG  1 
ATOM   4622 C  CD  . LYS   B 1 217 ? 76.969 -0.694  33.790  1.00 32.35 ?  658  LYS   B CD  1 
ATOM   4623 C  CE  . LYS   B 1 217 ? 75.891 -1.541  33.124  1.00 34.16 ?  658  LYS   B CE  1 
ATOM   4624 N  NZ  . LYS   B 1 217 ? 75.389 -2.615  34.019  1.00 35.99 ?  658  LYS   B NZ  1 
ATOM   4625 N  N   . GLY   B 1 218 ? 73.019 1.922   36.133  1.00 15.08 ?  659  GLY   B N   1 
ATOM   4626 C  CA  . GLY   B 1 218 ? 71.907 2.462   35.382  1.00 14.43 ?  659  GLY   B CA  1 
ATOM   4627 C  C   . GLY   B 1 218 ? 71.339 3.764   35.891  1.00 13.82 ?  659  GLY   B C   1 
ATOM   4628 O  O   . GLY   B 1 218 ? 70.325 4.223   35.352  1.00 14.13 ?  659  GLY   B O   1 
ATOM   4629 N  N   A ARG   B 1 219 ? 71.949 4.380   36.906  0.86 14.74 ?  660  ARG   B N   1 
ATOM   4630 N  N   B ARG   B 1 219 ? 71.950 4.382   36.901  0.14 14.27 ?  660  ARG   B N   1 
ATOM   4631 C  CA  A ARG   B 1 219 ? 71.384 5.600   37.460  0.86 13.39 ?  660  ARG   B CA  1 
ATOM   4632 C  CA  B ARG   B 1 219 ? 71.408 5.613   37.465  0.14 14.53 ?  660  ARG   B CA  1 
ATOM   4633 C  C   A ARG   B 1 219 ? 71.390 6.701   36.408  0.86 13.66 ?  660  ARG   B C   1 
ATOM   4634 C  C   B ARG   B 1 219 ? 71.397 6.720   36.417  0.14 14.60 ?  660  ARG   B C   1 
ATOM   4635 O  O   A ARG   B 1 219 ? 72.427 6.991   35.805  0.86 15.10 ?  660  ARG   B O   1 
ATOM   4636 O  O   B ARG   B 1 219 ? 72.437 7.056   35.843  0.14 15.35 ?  660  ARG   B O   1 
ATOM   4637 C  CB  A ARG   B 1 219 ? 72.158 6.018   38.710  0.86 15.44 ?  660  ARG   B CB  1 
ATOM   4638 C  CB  B ARG   B 1 219 ? 72.237 6.029   38.678  0.14 15.16 ?  660  ARG   B CB  1 
ATOM   4639 C  CG  A ARG   B 1 219 ? 71.941 5.076   39.882  0.86 15.71 ?  660  ARG   B CG  1 
ATOM   4640 C  CG  B ARG   B 1 219 ? 71.956 5.211   39.931  0.14 15.78 ?  660  ARG   B CG  1 
ATOM   4641 C  CD  A ARG   B 1 219 ? 72.487 5.663   41.176  0.86 15.51 ?  660  ARG   B CD  1 
ATOM   4642 C  CD  B ARG   B 1 219 ? 71.967 6.097   41.163  0.14 16.30 ?  660  ARG   B CD  1 
ATOM   4643 N  NE  A ARG   B 1 219 ? 71.638 6.732   41.695  0.86 14.37 ?  660  ARG   B NE  1 
ATOM   4644 N  NE  B ARG   B 1 219 ? 73.045 7.077   41.086  0.14 16.76 ?  660  ARG   B NE  1 
ATOM   4645 C  CZ  A ARG   B 1 219 ? 72.019 8.002   41.846  0.86 14.37 ?  660  ARG   B CZ  1 
ATOM   4646 C  CZ  B ARG   B 1 219 ? 72.981 8.306   41.584  0.14 16.41 ?  660  ARG   B CZ  1 
ATOM   4647 N  NH1 A ARG   B 1 219 ? 73.244 8.381   41.502  0.86 15.23 ?  660  ARG   B NH1 1 
ATOM   4648 N  NH1 B ARG   B 1 219 ? 71.886 8.720   42.208  0.14 16.63 ?  660  ARG   B NH1 1 
ATOM   4649 N  NH2 A ARG   B 1 219 ? 71.169 8.895   42.347  0.86 13.19 ?  660  ARG   B NH2 1 
ATOM   4650 N  NH2 B ARG   B 1 219 ? 74.016 9.123   41.453  0.14 15.65 ?  660  ARG   B NH2 1 
ATOM   4651 N  N   . GLY   B 1 220 ? 70.213 7.286   36.171  1.00 14.12 ?  661  GLY   B N   1 
ATOM   4652 C  CA  . GLY   B 1 220 ? 70.020 8.267   35.127  1.00 15.30 ?  661  GLY   B CA  1 
ATOM   4653 C  C   . GLY   B 1 220 ? 69.464 7.701   33.835  1.00 14.42 ?  661  GLY   B C   1 
ATOM   4654 O  O   . GLY   B 1 220 ? 69.034 8.477   32.973  1.00 14.68 ?  661  GLY   B O   1 
ATOM   4655 N  N   . TYR   B 1 221 ? 69.440 6.378   33.685  1.00 12.22 ?  662  TYR   B N   1 
ATOM   4656 C  CA  . TYR   B 1 221 ? 69.036 5.750   32.435  1.00 11.62 ?  662  TYR   B CA  1 
ATOM   4657 C  C   . TYR   B 1 221 ? 67.626 5.192   32.490  1.00 12.36 ?  662  TYR   B C   1 
ATOM   4658 O  O   . TYR   B 1 221 ? 67.243 4.399   31.625  1.00 12.12 ?  662  TYR   B O   1 
ATOM   4659 C  CB  . TYR   B 1 221 ? 70.075 4.713   32.005  1.00 13.25 ?  662  TYR   B CB  1 
ATOM   4660 C  CG  . TYR   B 1 221 ? 71.382 5.388   31.679  1.00 14.82 ?  662  TYR   B CG  1 
ATOM   4661 C  CD1 . TYR   B 1 221 ? 72.314 5.663   32.677  1.00 17.32 ?  662  TYR   B CD1 1 
ATOM   4662 C  CD2 . TYR   B 1 221 ? 71.665 5.795   30.388  1.00 16.99 ?  662  TYR   B CD2 1 
ATOM   4663 C  CE1 . TYR   B 1 221 ? 73.503 6.305   32.380  1.00 19.98 ?  662  TYR   B CE1 1 
ATOM   4664 C  CE2 . TYR   B 1 221 ? 72.834 6.435   30.089  1.00 18.45 ?  662  TYR   B CE2 1 
ATOM   4665 C  CZ  . TYR   B 1 221 ? 73.754 6.689   31.086  1.00 20.38 ?  662  TYR   B CZ  1 
ATOM   4666 O  OH  . TYR   B 1 221 ? 74.931 7.321   30.769  1.00 24.80 ?  662  TYR   B OH  1 
ATOM   4667 N  N   . ASN   B 1 222 ? 66.831 5.621   33.464  1.00 11.25 ?  663  ASN   B N   1 
ATOM   4668 C  CA  . ASN   B 1 222 ? 65.420 5.276   33.547  1.00 11.17 ?  663  ASN   B CA  1 
ATOM   4669 C  C   . ASN   B 1 222 ? 64.663 6.566   33.792  1.00 11.12 ?  663  ASN   B C   1 
ATOM   4670 O  O   . ASN   B 1 222 ? 64.895 7.224   34.810  1.00 11.61 ?  663  ASN   B O   1 
ATOM   4671 C  CB  . ASN   B 1 222 ? 65.174 4.305   34.701  1.00 11.47 ?  663  ASN   B CB  1 
ATOM   4672 C  CG  . ASN   B 1 222 ? 63.808 3.679   34.641  1.00 10.57 ?  663  ASN   B CG  1 
ATOM   4673 O  OD1 . ASN   B 1 222 ? 63.589 2.726   33.889  1.00 11.68 ?  663  ASN   B OD1 1 
ATOM   4674 N  ND2 . ASN   B 1 222 ? 62.869 4.216   35.407  1.00 12.26 ?  663  ASN   B ND2 1 
ATOM   4675 N  N   . VAL   B 1 223 ? 63.782 6.933   32.862  1.00 11.23 ?  664  VAL   B N   1 
ATOM   4676 C  CA  . VAL   B 1 223 ? 63.053 8.194   32.912  1.00 10.93 ?  664  VAL   B CA  1 
ATOM   4677 C  C   . VAL   B 1 223 ? 61.568 7.869   32.924  1.00 12.54 ?  664  VAL   B C   1 
ATOM   4678 O  O   . VAL   B 1 223 ? 61.013 7.435   31.905  1.00 11.48 ?  664  VAL   B O   1 
ATOM   4679 C  CB  . VAL   B 1 223 ? 63.398 9.111   31.730  1.00 10.89 ?  664  VAL   B CB  1 
ATOM   4680 C  CG1 . VAL   B 1 223 ? 62.654 10.441  31.855  1.00 12.43 ?  664  VAL   B CG1 1 
ATOM   4681 C  CG2 . VAL   B 1 223 ? 64.898 9.348   31.638  1.00 12.55 ?  664  VAL   B CG2 1 
ATOM   4682 N  N   . ASN   B 1 224 ? 60.921 8.099   34.058  1.00 10.83 ?  665  ASN   B N   1 
ATOM   4683 C  CA  . ASN   B 1 224 ? 59.482 7.919   34.200  1.00 10.32 ?  665  ASN   B CA  1 
ATOM   4684 C  C   . ASN   B 1 224 ? 58.814 9.284   34.194  1.00 11.28 ?  665  ASN   B C   1 
ATOM   4685 O  O   . ASN   B 1 224 ? 59.176 10.157  34.990  1.00 12.99 ?  665  ASN   B O   1 
ATOM   4686 C  CB  . ASN   B 1 224 ? 59.163 7.234   35.531  1.00 10.60 ?  665  ASN   B CB  1 
ATOM   4687 C  CG  . ASN   B 1 224 ? 59.400 5.751   35.499  1.00 10.51 ?  665  ASN   B CG  1 
ATOM   4688 O  OD1 . ASN   B 1 224 ? 59.302 5.114   34.450  1.00 11.79 ?  665  ASN   B OD1 1 
ATOM   4689 N  ND2 . ASN   B 1 224 ? 59.708 5.176   36.659  1.00 11.48 ?  665  ASN   B ND2 1 
ATOM   4690 N  N   . ILE   B 1 225 ? 57.835 9.461   33.311  1.00 11.18 ?  666  ILE   B N   1 
ATOM   4691 C  CA  . ILE   B 1 225 ? 57.056 10.693  33.218  1.00 10.59 ?  666  ILE   B CA  1 
ATOM   4692 C  C   . ILE   B 1 225 ? 55.632 10.329  33.617  1.00 10.33 ?  666  ILE   B C   1 
ATOM   4693 O  O   . ILE   B 1 225 ? 54.836 9.877   32.774  1.00 11.41 ?  666  ILE   B O   1 
ATOM   4694 C  CB  . ILE   B 1 225 ? 57.120 11.292  31.804  1.00 12.10 ?  666  ILE   B CB  1 
ATOM   4695 C  CG1 . ILE   B 1 225 ? 58.585 11.457  31.373  1.00 11.72 ?  666  ILE   B CG1 1 
ATOM   4696 C  CG2 . ILE   B 1 225 ? 56.327 12.592  31.758  1.00 11.92 ?  666  ILE   B CG2 1 
ATOM   4697 C  CD1 . ILE   B 1 225 ? 58.766 11.894  29.899  1.00 12.82 ?  666  ILE   B CD1 1 
ATOM   4698 N  N   . PRO   B 1 226 ? 55.272 10.509  34.888  1.00 11.00 ?  667  PRO   B N   1 
ATOM   4699 C  CA  . PRO   B 1 226 ? 53.983 10.021  35.391  1.00 10.60 ?  667  PRO   B CA  1 
ATOM   4700 C  C   . PRO   B 1 226 ? 52.921 11.104  35.412  1.00 12.21 ?  667  PRO   B C   1 
ATOM   4701 O  O   . PRO   B 1 226 ? 53.161 12.204  35.923  1.00 14.71 ?  667  PRO   B O   1 
ATOM   4702 C  CB  . PRO   B 1 226 ? 54.323 9.572   36.827  1.00 12.07 ?  667  PRO   B CB  1 
ATOM   4703 C  CG  . PRO   B 1 226 ? 55.724 10.104  37.122  1.00 14.22 ?  667  PRO   B CG  1 
ATOM   4704 C  CD  . PRO   B 1 226 ? 56.141 10.986  35.968  1.00 10.54 ?  667  PRO   B CD  1 
ATOM   4705 N  N   . TRP   B 1 227 ? 51.748 10.804  34.867  1.00 12.83 ?  668  TRP   B N   1 
ATOM   4706 C  CA  . TRP   B 1 227 ? 50.651 11.758  34.808  1.00 13.26 ?  668  TRP   B CA  1 
ATOM   4707 C  C   . TRP   B 1 227 ? 49.689 11.522  35.960  1.00 12.80 ?  668  TRP   B C   1 
ATOM   4708 O  O   . TRP   B 1 227 ? 49.339 10.377  36.267  1.00 13.90 ?  668  TRP   B O   1 
ATOM   4709 C  CB  . TRP   B 1 227 ? 49.870 11.605  33.505  1.00 13.07 ?  668  TRP   B CB  1 
ATOM   4710 C  CG  . TRP   B 1 227 ? 50.654 11.805  32.246  1.00 12.36 ?  668  TRP   B CG  1 
ATOM   4711 C  CD1 . TRP   B 1 227 ? 50.761 10.923  31.214  1.00 13.62 ?  668  TRP   B CD1 1 
ATOM   4712 C  CD2 . TRP   B 1 227 ? 51.428 12.960  31.864  1.00 13.12 ?  668  TRP   B CD2 1 
ATOM   4713 N  NE1 . TRP   B 1 227 ? 51.551 11.443  30.221  1.00 13.18 ?  668  TRP   B NE1 1 
ATOM   4714 C  CE2 . TRP   B 1 227 ? 51.976 12.689  30.588  1.00 12.62 ?  668  TRP   B CE2 1 
ATOM   4715 C  CE3 . TRP   B 1 227 ? 51.725 14.182  32.474  1.00 13.20 ?  668  TRP   B CE3 1 
ATOM   4716 C  CZ2 . TRP   B 1 227 ? 52.780 13.603  29.903  1.00 12.52 ?  668  TRP   B CZ2 1 
ATOM   4717 C  CZ3 . TRP   B 1 227 ? 52.531 15.087  31.795  1.00 14.25 ?  668  TRP   B CZ3 1 
ATOM   4718 C  CH2 . TRP   B 1 227 ? 53.048 14.792  30.523  1.00 13.85 ?  668  TRP   B CH2 1 
ATOM   4719 N  N   . ASN   B 1 228 ? 49.276 12.616  36.604  1.00 13.16 ?  669  ASN   B N   1 
ATOM   4720 C  CA  . ASN   B 1 228 ? 48.284 12.573  37.668  1.00 16.46 ?  669  ASN   B CA  1 
ATOM   4721 C  C   . ASN   B 1 228 ? 47.190 13.597  37.412  1.00 17.10 ?  669  ASN   B C   1 
ATOM   4722 O  O   . ASN   B 1 228 ? 47.465 14.721  36.982  1.00 19.13 ?  669  ASN   B O   1 
ATOM   4723 C  CB  . ASN   B 1 228 ? 48.916 12.907  39.008  1.00 15.05 ?  669  ASN   B CB  1 
ATOM   4724 C  CG  . ASN   B 1 228 ? 50.086 12.012  39.341  1.00 14.36 ?  669  ASN   B CG  1 
ATOM   4725 O  OD1 . ASN   B 1 228 ? 49.937 10.796  39.476  1.00 16.78 ?  669  ASN   B OD1 1 
ATOM   4726 N  ND2 . ASN   B 1 228 ? 51.257 12.610  39.491  1.00 15.88 ?  669  ASN   B ND2 1 
ATOM   4727 N  N   . GLY   B 1 229 ? 45.953 13.204  37.692  0.96 16.88 ?  670  GLY   B N   1 
ATOM   4728 C  CA  . GLY   B 1 229 ? 44.845 14.139  37.780  0.96 18.38 ?  670  GLY   B CA  1 
ATOM   4729 C  C   . GLY   B 1 229 ? 44.603 14.949  36.523  0.96 22.76 ?  670  GLY   B C   1 
ATOM   4730 O  O   . GLY   B 1 229 ? 44.736 16.177  36.523  0.96 25.22 ?  670  GLY   B O   1 
ATOM   4731 N  N   . GLY   B 1 230 ? 44.247 14.271  35.443  1.00 20.74 ?  671  GLY   B N   1 
ATOM   4732 C  CA  . GLY   B 1 230 ? 43.958 14.960  34.202  1.00 17.78 ?  671  GLY   B CA  1 
ATOM   4733 C  C   . GLY   B 1 230 ? 43.783 14.016  33.032  1.00 17.35 ?  671  GLY   B C   1 
ATOM   4734 O  O   . GLY   B 1 230 ? 44.464 12.989  32.944  1.00 17.68 ?  671  GLY   B O   1 
ATOM   4735 N  N   . LYS   B 1 231 ? 42.874 14.353  32.119  1.00 17.07 ?  672  LYS   B N   1 
ATOM   4736 C  CA  . LYS   B 1 231 ? 42.684 13.576  30.898  1.00 17.08 ?  672  LYS   B CA  1 
ATOM   4737 C  C   . LYS   B 1 231 ? 43.721 14.094  29.906  1.00 15.20 ?  672  LYS   B C   1 
ATOM   4738 O  O   . LYS   B 1 231 ? 43.474 15.016  29.125  0.89 14.87 ?  672  LYS   B O   1 
ATOM   4739 C  CB  . LYS   B 1 231 ? 41.257 13.735  30.383  1.00 20.06 ?  672  LYS   B CB  1 
ATOM   4740 C  CG  . LYS   B 1 231 ? 40.993 13.045  29.060  1.00 25.29 ?  672  LYS   B CG  1 
ATOM   4741 C  CD  . LYS   B 1 231 ? 39.504 12.876  28.807  1.00 29.38 ?  672  LYS   B CD  1 
ATOM   4742 C  CE  . LYS   B 1 231 ? 39.208 11.520  28.180  1.00 32.56 ?  672  LYS   B CE  1 
ATOM   4743 N  NZ  . LYS   B 1 231 ? 37.831 11.041  28.495  1.00 35.17 ?  672  LYS   B NZ  1 
ATOM   4744 N  N   . MET   B 1 232 ? 44.919 13.524  29.973  1.00 14.27 ?  673  MET   B N   1 
ATOM   4745 C  CA  . MET   B 1 232 ? 46.031 14.049  29.199  1.00 13.07 ?  673  MET   B CA  1 
ATOM   4746 C  C   . MET   B 1 232 ? 45.833 13.758  27.716  1.00 14.22 ?  673  MET   B C   1 
ATOM   4747 O  O   . MET   B 1 232 ? 45.199 12.775  27.334  1.00 15.00 ?  673  MET   B O   1 
ATOM   4748 C  CB  . MET   B 1 232 ? 47.342 13.444  29.695  1.00 13.68 ?  673  MET   B CB  1 
ATOM   4749 C  CG  . MET   B 1 232 ? 47.546 13.636  31.196  1.00 13.78 ?  673  MET   B CG  1 
ATOM   4750 S  SD  . MET   B 1 232 ? 47.164 15.319  31.765  1.00 16.36 ?  673  MET   B SD  1 
ATOM   4751 C  CE  . MET   B 1 232 ? 47.604 15.191  33.501  1.00 17.13 ?  673  MET   B CE  1 
ATOM   4752 N  N   . GLY   B 1 233 ? 46.379 14.622  26.880  1.00 14.74 ?  674  GLY   B N   1 
ATOM   4753 C  CA  . GLY   B 1 233 ? 46.237 14.496  25.441  1.00 13.42 ?  674  GLY   B CA  1 
ATOM   4754 C  C   . GLY   B 1 233 ? 47.413 15.109  24.734  1.00 13.01 ?  674  GLY   B C   1 
ATOM   4755 O  O   . GLY   B 1 233 ? 48.521 15.181  25.281  1.00 13.38 ?  674  GLY   B O   1 
ATOM   4756 N  N   . ASP   B 1 234 ? 47.170 15.573  23.511  1.00 12.51 ?  675  ASP   B N   1 
ATOM   4757 C  CA  . ASP   B 1 234 ? 48.249 16.096  22.677  1.00 13.43 ?  675  ASP   B CA  1 
ATOM   4758 C  C   . ASP   B 1 234 ? 49.076 17.190  23.343  1.00 12.66 ?  675  ASP   B C   1 
ATOM   4759 O  O   . ASP   B 1 234 ? 50.309 17.125  23.253  1.00 14.60 ?  675  ASP   B O   1 
ATOM   4760 C  CB  . ASP   B 1 234 ? 47.722 16.579  21.316  1.00 14.44 ?  675  ASP   B CB  1 
ATOM   4761 C  CG  . ASP   B 1 234 ? 47.192 15.456  20.442  1.00 16.05 ?  675  ASP   B CG  1 
ATOM   4762 O  OD1 . ASP   B 1 234 ? 47.255 14.270  20.813  1.00 15.78 ?  675  ASP   B OD1 1 
ATOM   4763 O  OD2 . ASP   B 1 234 ? 46.695 15.767  19.341  1.00 18.64 -1 675  ASP   B OD2 1 
ATOM   4764 N  N   . PRO   B 1 235 ? 48.494 18.220  23.978  1.00 14.62 ?  676  PRO   B N   1 
ATOM   4765 C  CA  . PRO   B 1 235 ? 49.351 19.265  24.560  1.00 16.30 ?  676  PRO   B CA  1 
ATOM   4766 C  C   . PRO   B 1 235 ? 50.335 18.731  25.582  1.00 13.70 ?  676  PRO   B C   1 
ATOM   4767 O  O   . PRO   B 1 235 ? 51.493 19.166  25.602  1.00 14.85 ?  676  PRO   B O   1 
ATOM   4768 C  CB  . PRO   B 1 235 ? 48.348 20.259  25.165  1.00 17.00 ?  676  PRO   B CB  1 
ATOM   4769 C  CG  . PRO   B 1 235 ? 47.073 20.001  24.446  1.00 14.61 ?  676  PRO   B CG  1 
ATOM   4770 C  CD  . PRO   B 1 235 ? 47.065 18.530  24.171  1.00 14.73 ?  676  PRO   B CD  1 
ATOM   4771 N  N   . GLU   B 1 236 ? 49.911 17.782  26.419  1.00 13.53 ?  677  GLU   B N   1 
ATOM   4772 C  CA  . GLU   B 1 236 ? 50.787 17.275  27.467  1.00 13.75 ?  677  GLU   B CA  1 
ATOM   4773 C  C   . GLU   B 1 236 ? 51.879 16.394  26.879  1.00 12.92 ?  677  GLU   B C   1 
ATOM   4774 O  O   . GLU   B 1 236 ? 53.045 16.482  27.286  1.00 13.90 ?  677  GLU   B O   1 
ATOM   4775 C  CB  . GLU   B 1 236 ? 49.954 16.503  28.486  1.00 14.84 ?  677  GLU   B CB  1 
ATOM   4776 C  CG  . GLU   B 1 236 ? 49.030 17.383  29.322  1.00 15.58 ?  677  GLU   B CG  1 
ATOM   4777 C  CD  . GLU   B 1 236 ? 47.839 17.969  28.559  1.00 16.94 ?  677  GLU   B CD  1 
ATOM   4778 O  OE1 . GLU   B 1 236 ? 47.261 17.285  27.684  1.00 14.34 ?  677  GLU   B OE1 1 
ATOM   4779 O  OE2 . GLU   B 1 236 ? 47.465 19.130  28.851  1.00 18.08 -1 677  GLU   B OE2 1 
ATOM   4780 N  N   . TYR   B 1 237 ? 51.523 15.559  25.899  1.00 13.04 ?  678  TYR   B N   1 
ATOM   4781 C  CA  . TYR   B 1 237 ? 52.517 14.691  25.285  1.00 13.29 ?  678  TYR   B CA  1 
ATOM   4782 C  C   . TYR   B 1 237 ? 53.520 15.493  24.466  1.00 12.86 ?  678  TYR   B C   1 
ATOM   4783 O  O   . TYR   B 1 237 ? 54.725 15.214  24.504  1.00 13.20 ?  678  TYR   B O   1 
ATOM   4784 C  CB  . TYR   B 1 237 ? 51.845 13.571  24.481  1.00 12.82 ?  678  TYR   B CB  1 
ATOM   4785 C  CG  . TYR   B 1 237 ? 51.414 12.436  25.375  1.00 11.24 ?  678  TYR   B CG  1 
ATOM   4786 C  CD1 . TYR   B 1 237 ? 50.326 12.578  26.229  1.00 12.67 ?  678  TYR   B CD1 1 
ATOM   4787 C  CD2 . TYR   B 1 237 ? 52.117 11.236  25.397  1.00 13.30 ?  678  TYR   B CD2 1 
ATOM   4788 C  CE1 . TYR   B 1 237 ? 49.950 11.561  27.077  1.00 13.39 ?  678  TYR   B CE1 1 
ATOM   4789 C  CE2 . TYR   B 1 237 ? 51.741 10.210  26.238  1.00 12.76 ?  678  TYR   B CE2 1 
ATOM   4790 C  CZ  . TYR   B 1 237 ? 50.651 10.379  27.076  1.00 12.64 ?  678  TYR   B CZ  1 
ATOM   4791 O  OH  . TYR   B 1 237 ? 50.254 9.379   27.934  1.00 15.07 ?  678  TYR   B OH  1 
ATOM   4792 N  N   . MET   B 1 238 ? 53.052 16.510  23.737  1.00 14.91 ?  679  MET   B N   1 
ATOM   4793 C  CA  . MET   B 1 238 ? 53.984 17.382  23.031  1.00 13.16 ?  679  MET   B CA  1 
ATOM   4794 C  C   . MET   B 1 238 ? 54.906 18.111  24.004  1.00 11.81 ?  679  MET   B C   1 
ATOM   4795 O  O   . MET   B 1 238 ? 56.105 18.235  23.750  1.00 12.21 ?  679  MET   B O   1 
ATOM   4796 C  CB  . MET   B 1 238 ? 53.219 18.379  22.171  1.00 12.84 ?  679  MET   B CB  1 
ATOM   4797 C  CG  . MET   B 1 238 ? 52.431 17.738  21.029  1.00 15.21 ?  679  MET   B CG  1 
ATOM   4798 S  SD  . MET   B 1 238 ? 53.420 16.865  19.801  1.00 18.87 ?  679  MET   B SD  1 
ATOM   4799 C  CE  . MET   B 1 238 ? 53.954 18.248  18.795  1.00 18.88 ?  679  MET   B CE  1 
ATOM   4800 N  N   . ALA   B 1 239 ? 54.373 18.582  25.131  1.00 13.33 ?  680  ALA   B N   1 
ATOM   4801 C  CA  . ALA   B 1 239 ? 55.218 19.293  26.083  1.00 13.15 ?  680  ALA   B CA  1 
ATOM   4802 C  C   . ALA   B 1 239 ? 56.248 18.363  26.709  1.00 12.97 ?  680  ALA   B C   1 
ATOM   4803 O  O   . ALA   B 1 239 ? 57.413 18.744  26.865  1.00 13.15 ?  680  ALA   B O   1 
ATOM   4804 C  CB  . ALA   B 1 239 ? 54.363 19.989  27.140  1.00 14.28 ?  680  ALA   B CB  1 
ATOM   4805 N  N   . ALA   B 1 240 ? 55.845 17.140  27.064  1.00 12.90 ?  681  ALA   B N   1 
ATOM   4806 C  CA  . ALA   B 1 240 ? 56.804 16.187  27.621  1.00 11.97 ?  681  ALA   B CA  1 
ATOM   4807 C  C   . ALA   B 1 240 ? 57.895 15.844  26.616  1.00 12.85 ?  681  ALA   B C   1 
ATOM   4808 O  O   . ALA   B 1 240 ? 59.065 15.684  26.986  1.00 12.89 ?  681  ALA   B O   1 
ATOM   4809 C  CB  . ALA   B 1 240 ? 56.085 14.923  28.090  1.00 13.45 ?  681  ALA   B CB  1 
ATOM   4810 N  N   . PHE   B 1 241 ? 57.538 15.723  25.337  1.00 10.84 ?  682  PHE   B N   1 
ATOM   4811 C  CA  . PHE   B 1 241 ? 58.564 15.454  24.338  1.00 11.87 ?  682  PHE   B CA  1 
ATOM   4812 C  C   . PHE   B 1 241 ? 59.525 16.630  24.193  1.00 12.95 ?  682  PHE   B C   1 
ATOM   4813 O  O   . PHE   B 1 241 ? 60.739 16.435  24.083  1.00 13.18 ?  682  PHE   B O   1 
ATOM   4814 C  CB  . PHE   B 1 241 ? 57.914 15.115  22.999  1.00 12.03 ?  682  PHE   B CB  1 
ATOM   4815 C  CG  . PHE   B 1 241 ? 57.792 13.636  22.746  1.00 11.84 ?  682  PHE   B CG  1 
ATOM   4816 C  CD1 . PHE   B 1 241 ? 57.124 12.828  23.645  1.00 12.91 ?  682  PHE   B CD1 1 
ATOM   4817 C  CD2 . PHE   B 1 241 ? 58.361 13.058  21.618  1.00 15.95 ?  682  PHE   B CD2 1 
ATOM   4818 C  CE1 . PHE   B 1 241 ? 57.013 11.467  23.419  1.00 13.84 ?  682  PHE   B CE1 1 
ATOM   4819 C  CE2 . PHE   B 1 241 ? 58.242 11.691  21.379  1.00 14.60 ?  682  PHE   B CE2 1 
ATOM   4820 C  CZ  . PHE   B 1 241 ? 57.572 10.896  22.290  1.00 14.45 ?  682  PHE   B CZ  1 
ATOM   4821 N  N   . HIS   B 1 242 ? 59.002 17.858  24.190  1.00 12.97 ?  683  HIS   B N   1 
ATOM   4822 C  CA  . HIS   B 1 242 ? 59.856 19.026  23.995  1.00 14.23 ?  683  HIS   B CA  1 
ATOM   4823 C  C   . HIS   B 1 242 ? 60.805 19.229  25.175  1.00 14.49 ?  683  HIS   B C   1 
ATOM   4824 O  O   . HIS   B 1 242 ? 61.992 19.537  24.985  1.00 15.92 ?  683  HIS   B O   1 
ATOM   4825 C  CB  . HIS   B 1 242 ? 58.978 20.262  23.801  1.00 17.65 ?  683  HIS   B CB  1 
ATOM   4826 C  CG  . HIS   B 1 242 ? 59.747 21.539  23.672  1.00 23.52 ?  683  HIS   B CG  1 
ATOM   4827 N  ND1 . HIS   B 1 242 ? 60.422 21.884  22.522  1.00 27.04 ?  683  HIS   B ND1 1 
ATOM   4828 C  CD2 . HIS   B 1 242 ? 59.944 22.556  24.544  1.00 27.47 ?  683  HIS   B CD2 1 
ATOM   4829 C  CE1 . HIS   B 1 242 ? 61.004 23.059  22.692  1.00 28.45 ?  683  HIS   B CE1 1 
ATOM   4830 N  NE2 . HIS   B 1 242 ? 60.725 23.490  23.908  1.00 28.29 ?  683  HIS   B NE2 1 
ATOM   4831 N  N   . HIS   B 1 243 ? 60.305 19.062  26.395  1.00 15.48 ?  684  HIS   B N   1 
ATOM   4832 C  CA  . HIS   B 1 243 ? 61.078 19.404  27.582  1.00 14.00 ?  684  HIS   B CA  1 
ATOM   4833 C  C   . HIS   B 1 243 ? 61.904 18.251  28.121  1.00 15.33 ?  684  HIS   B C   1 
ATOM   4834 O  O   . HIS   B 1 243 ? 62.899 18.496  28.820  1.00 16.58 ?  684  HIS   B O   1 
ATOM   4835 C  CB  . HIS   B 1 243 ? 60.153 19.899  28.699  1.00 18.51 ?  684  HIS   B CB  1 
ATOM   4836 C  CG  . HIS   B 1 243 ? 59.470 21.190  28.382  1.00 25.73 ?  684  HIS   B CG  1 
ATOM   4837 N  ND1 . HIS   B 1 243 ? 60.156 22.378  28.254  1.00 30.46 ?  684  HIS   B ND1 1 
ATOM   4838 C  CD2 . HIS   B 1 243 ? 58.165 21.483  28.170  1.00 27.34 ?  684  HIS   B CD2 1 
ATOM   4839 C  CE1 . HIS   B 1 243 ? 59.306 23.347  27.967  1.00 32.27 ?  684  HIS   B CE1 1 
ATOM   4840 N  NE2 . HIS   B 1 243 ? 58.090 22.831  27.913  1.00 30.77 ?  684  HIS   B NE2 1 
ATOM   4841 N  N   . LEU   B 1 244 ? 61.510 17.008  27.851  1.00 13.91 ?  685  LEU   B N   1 
ATOM   4842 C  CA  . LEU   B 1 244 ? 62.148 15.863  28.492  1.00 12.66 ?  685  LEU   B CA  1 
ATOM   4843 C  C   . LEU   B 1 244 ? 62.621 14.811  27.495  1.00 11.64 ?  685  LEU   B C   1 
ATOM   4844 O  O   . LEU   B 1 244 ? 63.819 14.517  27.425  1.00 13.47 ?  685  LEU   B O   1 
ATOM   4845 C  CB  . LEU   B 1 244 ? 61.178 15.221  29.480  1.00 11.61 ?  685  LEU   B CB  1 
ATOM   4846 C  CG  . LEU   B 1 244 ? 60.853 15.993  30.754  1.00 14.51 ?  685  LEU   B CG  1 
ATOM   4847 C  CD1 . LEU   B 1 244 ? 59.661 15.342  31.407  1.00 14.23 ?  685  LEU   B CD1 1 
ATOM   4848 C  CD2 . LEU   B 1 244 ? 62.053 16.003  31.675  1.00 16.94 ?  685  LEU   B CD2 1 
ATOM   4849 N  N   . VAL   B 1 245 ? 61.699 14.221  26.726  1.00 12.96 ?  686  VAL   B N   1 
ATOM   4850 C  CA  . VAL   B 1 245 ? 62.065 13.064  25.910  1.00 11.74 ?  686  VAL   B CA  1 
ATOM   4851 C  C   . VAL   B 1 245 ? 63.142 13.434  24.898  1.00 12.45 ?  686  VAL   B C   1 
ATOM   4852 O  O   . VAL   B 1 245 ? 64.163 12.750  24.770  1.00 13.84 ?  686  VAL   B O   1 
ATOM   4853 C  CB  . VAL   B 1 245 ? 60.830 12.471  25.212  1.00 13.03 ?  686  VAL   B CB  1 
ATOM   4854 C  CG1 . VAL   B 1 245 ? 61.250 11.268  24.382  1.00 13.48 ?  686  VAL   B CG1 1 
ATOM   4855 C  CG2 . VAL   B 1 245 ? 59.769 12.082  26.231  1.00 13.68 ?  686  VAL   B CG2 1 
ATOM   4856 N  N   . MET   B 1 246 ? 62.912 14.488  24.133  1.00 13.52 ?  687  MET   B N   1 
ATOM   4857 C  CA  . MET   B 1 246 ? 63.841 14.800  23.054  1.00 13.56 ?  687  MET   B CA  1 
ATOM   4858 C  C   . MET   B 1 246 ? 65.191 15.319  23.555  1.00 14.28 ?  687  MET   B C   1 
ATOM   4859 O  O   . MET   B 1 246 ? 66.231 14.883  23.042  1.00 13.57 ?  687  MET   B O   1 
ATOM   4860 C  CB  . MET   B 1 246 ? 63.188 15.711  22.011  1.00 14.14 ?  687  MET   B CB  1 
ATOM   4861 C  CG  . MET   B 1 246 ? 62.015 15.022  21.292  1.00 13.66 ?  687  MET   B CG  1 
ATOM   4862 S  SD  . MET   B 1 246 ? 62.482 13.450  20.516  1.00 14.37 ?  687  MET   B SD  1 
ATOM   4863 C  CE  . MET   B 1 246 ? 63.676 14.003  19.290  1.00 15.59 ?  687  MET   B CE  1 
ATOM   4864 N  N   . PRO   B 1 247 ? 65.244 16.230  24.540  1.00 14.08 ?  688  PRO   B N   1 
ATOM   4865 C  CA  . PRO   B 1 247 ? 66.566 16.640  25.050  1.00 14.94 ?  688  PRO   B CA  1 
ATOM   4866 C  C   . PRO   B 1 247 ? 67.374 15.490  25.629  1.00 14.57 ?  688  PRO   B C   1 
ATOM   4867 O  O   . PRO   B 1 247 ? 68.575 15.385  25.349  1.00 15.29 ?  688  PRO   B O   1 
ATOM   4868 C  CB  . PRO   B 1 247 ? 66.229 17.707  26.097  1.00 17.12 ?  688  PRO   B CB  1 
ATOM   4869 C  CG  . PRO   B 1 247 ? 64.921 18.270  25.634  1.00 17.05 ?  688  PRO   B CG  1 
ATOM   4870 C  CD  . PRO   B 1 247 ? 64.167 17.094  25.070  1.00 14.41 ?  688  PRO   B CD  1 
ATOM   4871 N  N   . ILE   B 1 248 ? 66.746 14.613  26.413  1.00 13.40 ?  689  ILE   B N   1 
ATOM   4872 C  CA  . ILE   B 1 248 ? 67.457 13.457  26.962  1.00 14.33 ?  689  ILE   B CA  1 
ATOM   4873 C  C   . ILE   B 1 248 ? 67.892 12.516  25.847  1.00 13.49 ?  689  ILE   B C   1 
ATOM   4874 O  O   . ILE   B 1 248 ? 69.049 12.084  25.794  1.00 13.38 ?  689  ILE   B O   1 
ATOM   4875 C  CB  . ILE   B 1 248 ? 66.583 12.732  27.995  1.00 14.02 ?  689  ILE   B CB  1 
ATOM   4876 C  CG1 . ILE   B 1 248 ? 66.326 13.631  29.203  1.00 13.59 ?  689  ILE   B CG1 1 
ATOM   4877 C  CG2 . ILE   B 1 248 ? 67.220 11.401  28.400  1.00 14.89 ?  689  ILE   B CG2 1 
ATOM   4878 C  CD1 . ILE   B 1 248 ? 65.393 13.007  30.250  1.00 13.35 ?  689  ILE   B CD1 1 
ATOM   4879 N  N   . ALA   B 1 249 ? 66.972 12.191  24.933  1.00 13.14 ?  690  ALA   B N   1 
ATOM   4880 C  CA  . ALA   B 1 249 ? 67.300 11.261  23.857  1.00 13.83 ?  690  ALA   B CA  1 
ATOM   4881 C  C   . ALA   B 1 249 ? 68.466 11.763  23.014  1.00 13.65 ?  690  ALA   B C   1 
ATOM   4882 O  O   . ALA   B 1 249 ? 69.376 10.993  22.678  1.00 14.35 ?  690  ALA   B O   1 
ATOM   4883 C  CB  . ALA   B 1 249 ? 66.070 11.005  22.991  1.00 13.76 ?  690  ALA   B CB  1 
ATOM   4884 N  N   . ARG   B 1 250 ? 68.469 13.050  22.666  1.00 14.02 ?  691  ARG   B N   1 
ATOM   4885 C  CA  . ARG   B 1 250 ? 69.560 13.565  21.844  1.00 15.17 ?  691  ARG   B CA  1 
ATOM   4886 C  C   . ARG   B 1 250 ? 70.888 13.475  22.580  1.00 15.96 ?  691  ARG   B C   1 
ATOM   4887 O  O   . ARG   B 1 250 ? 71.922 13.175  21.976  1.00 16.29 ?  691  ARG   B O   1 
ATOM   4888 C  CB  . ARG   B 1 250 ? 69.285 15.010  21.446  1.00 14.68 ?  691  ARG   B CB  1 
ATOM   4889 C  CG  . ARG   B 1 250 ? 68.229 15.144  20.379  1.00 19.99 ?  691  ARG   B CG  1 
ATOM   4890 C  CD  . ARG   B 1 250 ? 68.101 16.583  19.933  1.00 24.20 ?  691  ARG   B CD  1 
ATOM   4891 N  NE  . ARG   B 1 250 ? 67.500 17.415  20.967  1.00 26.83 ?  691  ARG   B NE  1 
ATOM   4892 C  CZ  . ARG   B 1 250 ? 66.237 17.832  20.943  1.00 27.05 ?  691  ARG   B CZ  1 
ATOM   4893 N  NH1 . ARG   B 1 250 ? 65.443 17.486  19.941  1.00 26.96 ?  691  ARG   B NH1 1 
ATOM   4894 N  NH2 . ARG   B 1 250 ? 65.765 18.587  21.923  1.00 25.29 ?  691  ARG   B NH2 1 
ATOM   4895 N  N   . GLU   B 1 251 ? 70.882 13.729  23.888  1.00 15.31 ?  692  GLU   B N   1 
ATOM   4896 C  CA  . GLU   B 1 251 ? 72.121 13.644  24.656  1.00 14.97 ?  692  GLU   B CA  1 
ATOM   4897 C  C   . GLU   B 1 251 ? 72.616 12.204  24.750  1.00 16.58 ?  692  GLU   B C   1 
ATOM   4898 O  O   . GLU   B 1 251 ? 73.824 11.946  24.660  1.00 17.36 ?  692  GLU   B O   1 
ATOM   4899 C  CB  . GLU   B 1 251 ? 71.915 14.243  26.045  1.00 15.72 ?  692  GLU   B CB  1 
ATOM   4900 C  CG  . GLU   B 1 251 ? 73.220 14.410  26.800  1.00 17.43 ?  692  GLU   B CG  1 
ATOM   4901 C  CD  . GLU   B 1 251 ? 73.063 15.200  28.093  1.00 19.60 ?  692  GLU   B CD  1 
ATOM   4902 O  OE1 . GLU   B 1 251 ? 71.980 15.768  28.332  1.00 17.82 ?  692  GLU   B OE1 1 
ATOM   4903 O  OE2 . GLU   B 1 251 ? 74.026 15.240  28.888  1.00 25.12 -1 692  GLU   B OE2 1 
ATOM   4904 N  N   . PHE   B 1 252 ? 71.692 11.254  24.918  1.00 14.28 ?  693  PHE   B N   1 
ATOM   4905 C  CA  . PHE   B 1 252 ? 72.042 9.837   24.928  1.00 14.23 ?  693  PHE   B CA  1 
ATOM   4906 C  C   . PHE   B 1 252 ? 72.585 9.380   23.573  1.00 14.63 ?  693  PHE   B C   1 
ATOM   4907 O  O   . PHE   B 1 252 ? 73.435 8.482   23.516  1.00 14.80 ?  693  PHE   B O   1 
ATOM   4908 C  CB  . PHE   B 1 252 ? 70.794 9.037   25.321  1.00 14.22 ?  693  PHE   B CB  1 
ATOM   4909 C  CG  . PHE   B 1 252 ? 70.991 7.536   25.371  1.00 13.84 ?  693  PHE   B CG  1 
ATOM   4910 C  CD1 . PHE   B 1 252 ? 71.814 6.943   26.319  1.00 15.48 ?  693  PHE   B CD1 1 
ATOM   4911 C  CD2 . PHE   B 1 252 ? 70.289 6.716   24.493  1.00 12.89 ?  693  PHE   B CD2 1 
ATOM   4912 C  CE1 . PHE   B 1 252 ? 71.965 5.558   26.376  1.00 16.04 ?  693  PHE   B CE1 1 
ATOM   4913 C  CE2 . PHE   B 1 252 ? 70.435 5.330   24.540  1.00 15.05 ?  693  PHE   B CE2 1 
ATOM   4914 C  CZ  . PHE   B 1 252 ? 71.270 4.753   25.481  1.00 14.48 ?  693  PHE   B CZ  1 
ATOM   4915 N  N   . ALA   B 1 253 ? 72.107 9.984   22.469  1.00 14.28 ?  694  ALA   B N   1 
ATOM   4916 C  CA  . ALA   B 1 253 ? 72.577 9.665   21.125  1.00 16.05 ?  694  ALA   B CA  1 
ATOM   4917 C  C   . ALA   B 1 253 ? 72.372 8.185   20.817  1.00 14.53 ?  694  ALA   B C   1 
ATOM   4918 O  O   . ALA   B 1 253 ? 73.342 7.451   20.592  1.00 15.48 ?  694  ALA   B O   1 
ATOM   4919 C  CB  . ALA   B 1 253 ? 74.045 10.072  20.965  1.00 16.01 ?  694  ALA   B CB  1 
ATOM   4920 N  N   . PRO   B 1 254 ? 71.128 7.709   20.783  1.00 12.80 ?  695  PRO   B N   1 
ATOM   4921 C  CA  . PRO   B 1 254 ? 70.902 6.280   20.562  1.00 12.88 ?  695  PRO   B CA  1 
ATOM   4922 C  C   . PRO   B 1 254 ? 71.349 5.859   19.174  1.00 14.29 ?  695  PRO   B C   1 
ATOM   4923 O  O   . PRO   B 1 254 ? 71.341 6.642   18.223  1.00 14.77 ?  695  PRO   B O   1 
ATOM   4924 C  CB  . PRO   B 1 254 ? 69.380 6.140   20.709  1.00 13.55 ?  695  PRO   B CB  1 
ATOM   4925 C  CG  . PRO   B 1 254 ? 68.859 7.484   20.295  1.00 14.20 ?  695  PRO   B CG  1 
ATOM   4926 C  CD  . PRO   B 1 254 ? 69.865 8.458   20.859  1.00 14.69 ?  695  PRO   B CD  1 
ATOM   4927 N  N   . GLU   B 1 255 ? 71.743 4.599   19.072  1.00 14.35 ?  696  GLU   B N   1 
ATOM   4928 C  CA  . GLU   B 1 255 ? 72.031 4.004   17.780  1.00 13.88 ?  696  GLU   B CA  1 
ATOM   4929 C  C   . GLU   B 1 255 ? 70.842 3.249   17.206  1.00 13.61 ?  696  GLU   B C   1 
ATOM   4930 O  O   . GLU   B 1 255 ? 70.825 2.975   16.003  1.00 16.23 ?  696  GLU   B O   1 
ATOM   4931 C  CB  . GLU   B 1 255 ? 73.261 3.098   17.886  1.00 13.71 ?  696  GLU   B CB  1 
ATOM   4932 C  CG  . GLU   B 1 255 ? 74.525 3.892   18.189  1.00 17.05 ?  696  GLU   B CG  1 
ATOM   4933 C  CD  . GLU   B 1 255 ? 75.656 3.028   18.679  1.00 21.56 ?  696  GLU   B CD  1 
ATOM   4934 O  OE1 . GLU   B 1 255 ? 75.663 2.649   19.867  1.00 17.91 ?  696  GLU   B OE1 1 
ATOM   4935 O  OE2 . GLU   B 1 255 ? 76.554 2.734   17.868  1.00 27.88 -1 696  GLU   B OE2 1 
ATOM   4936 N  N   . LEU   B 1 256 ? 69.843 2.935   18.030  1.00 12.62 ?  697  LEU   B N   1 
ATOM   4937 C  CA  . LEU   B 1 256 ? 68.597 2.331   17.584  1.00 10.94 ?  697  LEU   B CA  1 
ATOM   4938 C  C   . LEU   B 1 256 ? 67.515 2.820   18.536  1.00 12.24 ?  697  LEU   B C   1 
ATOM   4939 O  O   . LEU   B 1 256 ? 67.744 2.914   19.745  1.00 13.55 ?  697  LEU   B O   1 
ATOM   4940 C  CB  . LEU   B 1 256 ? 68.694 0.810   17.688  1.00 11.00 ?  697  LEU   B CB  1 
ATOM   4941 C  CG  . LEU   B 1 256 ? 67.428 0.012   17.371  1.00 12.14 ?  697  LEU   B CG  1 
ATOM   4942 C  CD1 . LEU   B 1 256 ? 67.033 0.127   15.896  1.00 14.34 ?  697  LEU   B CD1 1 
ATOM   4943 C  CD2 . LEU   B 1 256 ? 67.629 -1.446  17.775  1.00 13.47 ?  697  LEU   B CD2 1 
ATOM   4944 N  N   . VAL   B 1 257 ? 66.356 3.171   17.991  1.00 11.09 ?  698  VAL   B N   1 
ATOM   4945 C  CA  . VAL   B 1 257 ? 65.200 3.583   18.788  1.00 11.41 ?  698  VAL   B CA  1 
ATOM   4946 C  C   . VAL   B 1 257 ? 64.123 2.517   18.643  1.00 11.95 ?  698  VAL   B C   1 
ATOM   4947 O  O   . VAL   B 1 257 ? 63.763 2.130   17.522  1.00 11.88 ?  698  VAL   B O   1 
ATOM   4948 C  CB  . VAL   B 1 257 ? 64.670 4.965   18.360  1.00 11.69 ?  698  VAL   B CB  1 
ATOM   4949 C  CG1 . VAL   B 1 257 ? 63.420 5.338   19.161  1.00 13.81 ?  698  VAL   B CG1 1 
ATOM   4950 C  CG2 . VAL   B 1 257 ? 65.769 6.023   18.494  1.00 12.76 ?  698  VAL   B CG2 1 
ATOM   4951 N  N   . LEU   B 1 258 ? 63.626 2.028   19.774  1.00 11.73 ?  699  LEU   B N   1 
ATOM   4952 C  CA  . LEU   B 1 258 ? 62.457 1.162   19.802  1.00 10.64 ?  699  LEU   B CA  1 
ATOM   4953 C  C   . LEU   B 1 258 ? 61.314 1.928   20.450  1.00 10.97 ?  699  LEU   B C   1 
ATOM   4954 O  O   . LEU   B 1 258 ? 61.500 2.576   21.489  1.00 10.97 ?  699  LEU   B O   1 
ATOM   4955 C  CB  . LEU   B 1 258 ? 62.736 -0.116  20.599  1.00 10.64 ?  699  LEU   B CB  1 
ATOM   4956 C  CG  . LEU   B 1 258 ? 63.955 -0.977  20.229  1.00 11.39 ?  699  LEU   B CG  1 
ATOM   4957 C  CD1 . LEU   B 1 258 ? 64.063 -2.190  21.160  1.00 12.00 ?  699  LEU   B CD1 1 
ATOM   4958 C  CD2 . LEU   B 1 258 ? 63.858 -1.410  18.759  1.00 11.35 ?  699  LEU   B CD2 1 
ATOM   4959 N  N   . VAL   B 1 259 ? 60.129 1.856   19.859  1.00 11.25 ?  700  VAL   B N   1 
ATOM   4960 C  CA  . VAL   B 1 259 ? 58.950 2.452   20.468  1.00 11.19 ?  700  VAL   B CA  1 
ATOM   4961 C  C   . VAL   B 1 259 ? 58.073 1.324   20.995  1.00 10.40 ?  700  VAL   B C   1 
ATOM   4962 O  O   . VAL   B 1 259 ? 57.606 0.478   20.219  1.00 10.94 ?  700  VAL   B O   1 
ATOM   4963 C  CB  . VAL   B 1 259 ? 58.173 3.365   19.507  1.00 10.44 ?  700  VAL   B CB  1 
ATOM   4964 C  CG1 . VAL   B 1 259 ? 57.087 4.122   20.266  1.00 11.40 ?  700  VAL   B CG1 1 
ATOM   4965 C  CG2 . VAL   B 1 259 ? 59.114 4.325   18.761  1.00 12.26 ?  700  VAL   B CG2 1 
ATOM   4966 N  N   . SER   B 1 260 ? 57.855 1.304   22.310  1.00 10.66 ?  701  SER   B N   1 
ATOM   4967 C  CA  . SER   B 1 260 ? 56.812 0.467   22.887  1.00 9.76  ?  701  SER   B CA  1 
ATOM   4968 C  C   . SER   B 1 260 ? 55.525 1.247   22.652  1.00 9.69  ?  701  SER   B C   1 
ATOM   4969 O  O   . SER   B 1 260 ? 55.104 2.074   23.471  1.00 9.85  ?  701  SER   B O   1 
ATOM   4970 C  CB  . SER   B 1 260 ? 57.087 0.196   24.362  1.00 10.67 ?  701  SER   B CB  1 
ATOM   4971 O  OG  . SER   B 1 260 ? 57.834 -1.001  24.494  1.00 11.32 ?  701  SER   B OG  1 
ATOM   4972 N  N   . ALA   B 1 261 ? 54.925 0.995   21.486  1.00 8.84  ?  702  ALA   B N   1 
ATOM   4973 C  CA  . ALA   B 1 261 ? 53.851 1.818   20.934  1.00 10.18 ?  702  ALA   B CA  1 
ATOM   4974 C  C   . ALA   B 1 261 ? 52.510 1.176   21.272  1.00 10.91 ?  702  ALA   B C   1 
ATOM   4975 O  O   . ALA   B 1 261 ? 51.868 0.531   20.452  1.00 11.69 ?  702  ALA   B O   1 
ATOM   4976 C  CB  . ALA   B 1 261 ? 54.051 1.970   19.426  1.00 10.79 ?  702  ALA   B CB  1 
ATOM   4977 N  N   . GLY   B 1 262 ? 52.101 1.327   22.528  1.00 10.19 ?  703  GLY   B N   1 
ATOM   4978 C  CA  . GLY   B 1 262 ? 50.723 1.091   22.860  1.00 10.19 ?  703  GLY   B CA  1 
ATOM   4979 C  C   . GLY   B 1 262 ? 49.886 2.263   22.405  1.00 10.48 ?  703  GLY   B C   1 
ATOM   4980 O  O   . GLY   B 1 262 ? 50.348 3.403   22.358  1.00 12.30 ?  703  GLY   B O   1 
ATOM   4981 N  N   . PHE   B 1 263 ? 48.646 1.978   22.032  1.00 9.96  ?  704  PHE   B N   1 
ATOM   4982 C  CA  . PHE   B 1 263 ? 47.739 3.037   21.616  1.00 10.68 ?  704  PHE   B CA  1 
ATOM   4983 C  C   . PHE   B 1 263 ? 46.546 3.166   22.551  1.00 10.35 ?  704  PHE   B C   1 
ATOM   4984 O  O   . PHE   B 1 263 ? 45.466 3.597   22.135  1.00 11.55 ?  704  PHE   B O   1 
ATOM   4985 C  CB  . PHE   B 1 263 ? 47.355 2.927   20.140  1.00 10.05 ?  704  PHE   B CB  1 
ATOM   4986 C  CG  . PHE   B 1 263 ? 48.537 3.090   19.225  1.00 9.78  ?  704  PHE   B CG  1 
ATOM   4987 C  CD1 . PHE   B 1 263 ? 49.031 4.352   18.926  1.00 11.24 ?  704  PHE   B CD1 1 
ATOM   4988 C  CD2 . PHE   B 1 263 ? 49.197 1.978   18.730  1.00 11.54 ?  704  PHE   B CD2 1 
ATOM   4989 C  CE1 . PHE   B 1 263 ? 50.151 4.497   18.118  1.00 11.80 ?  704  PHE   B CE1 1 
ATOM   4990 C  CE2 . PHE   B 1 263 ? 50.322 2.116   17.920  1.00 11.16 ?  704  PHE   B CE2 1 
ATOM   4991 C  CZ  . PHE   B 1 263 ? 50.798 3.379   17.613  1.00 10.98 ?  704  PHE   B CZ  1 
ATOM   4992 N  N   . ASP   B 1 264 ? 46.758 2.838   23.829  1.00 10.04 ?  705  ASP   B N   1 
ATOM   4993 C  CA  . ASP   B 1 264 ? 45.714 2.937   24.846  1.00 8.28  ?  705  ASP   B CA  1 
ATOM   4994 C  C   . ASP   B 1 264 ? 45.628 4.311   25.511  1.00 9.98  ?  705  ASP   B C   1 
ATOM   4995 O  O   . ASP   B 1 264 ? 44.697 4.538   26.299  1.00 11.62 ?  705  ASP   B O   1 
ATOM   4996 C  CB  . ASP   B 1 264 ? 45.758 1.765   25.838  1.00 9.32  ?  705  ASP   B CB  1 
ATOM   4997 C  CG  . ASP   B 1 264 ? 47.164 1.416   26.310  1.00 10.51 ?  705  ASP   B CG  1 
ATOM   4998 O  OD1 . ASP   B 1 264 ? 48.125 2.180   26.027  1.00 11.44 ?  705  ASP   B OD1 1 
ATOM   4999 O  OD2 . ASP   B 1 264 ? 47.289 0.372   27.016  1.00 10.93 -1 705  ASP   B OD2 1 
ATOM   5000 N  N   . ALA   B 1 265 ? 46.544 5.240   25.196  1.00 10.57 ?  706  ALA   B N   1 
ATOM   5001 C  CA  . ALA   B 1 265 ? 46.354 6.649   25.535  1.00 11.51 ?  706  ALA   B CA  1 
ATOM   5002 C  C   . ALA   B 1 265 ? 45.493 7.385   24.512  1.00 11.71 ?  706  ALA   B C   1 
ATOM   5003 O  O   . ALA   B 1 265 ? 45.262 8.593   24.659  1.00 12.43 ?  706  ALA   B O   1 
ATOM   5004 C  CB  . ALA   B 1 265 ? 47.695 7.361   25.724  1.00 11.46 ?  706  ALA   B CB  1 
ATOM   5005 N  N   . ALA   B 1 266 ? 44.992 6.683   23.496  1.00 11.54 ?  707  ALA   B N   1 
ATOM   5006 C  CA  . ALA   B 1 266 ? 44.286 7.323   22.401  1.00 10.69 ?  707  ALA   B CA  1 
ATOM   5007 C  C   . ALA   B 1 266 ? 42.870 7.709   22.796  1.00 11.62 ?  707  ALA   B C   1 
ATOM   5008 O  O   . ALA   B 1 266 ? 42.206 7.025   23.583  1.00 12.86 ?  707  ALA   B O   1 
ATOM   5009 C  CB  . ALA   B 1 266 ? 44.192 6.359   21.223  1.00 10.71 ?  707  ALA   B CB  1 
ATOM   5010 N  N   A ARG   B 1 267 ? 42.413 8.824   22.234  0.57 11.60 ?  708  ARG   B N   1 
ATOM   5011 N  N   B ARG   B 1 267 ? 42.396 8.806   22.210  0.43 12.67 ?  708  ARG   B N   1 
ATOM   5012 C  CA  A ARG   B 1 267 ? 40.994 9.153   22.255  0.57 12.94 ?  708  ARG   B CA  1 
ATOM   5013 C  CA  B ARG   B 1 267 ? 40.991 9.169   22.337  0.43 14.36 ?  708  ARG   B CA  1 
ATOM   5014 C  C   A ARG   B 1 267 ? 40.184 7.929   21.844  0.57 12.10 ?  708  ARG   B C   1 
ATOM   5015 C  C   B ARG   B 1 267 ? 40.114 8.037   21.813  0.43 14.30 ?  708  ARG   B C   1 
ATOM   5016 O  O   A ARG   B 1 267 ? 40.495 7.266   20.852  0.57 11.30 ?  708  ARG   B O   1 
ATOM   5017 O  O   B ARG   B 1 267 ? 40.293 7.561   20.688  0.43 16.68 ?  708  ARG   B O   1 
ATOM   5018 C  CB  A ARG   B 1 267 ? 40.742 10.306  21.280  0.57 15.81 ?  708  ARG   B CB  1 
ATOM   5019 C  CB  B ARG   B 1 267 ? 40.712 10.458  21.563  0.43 16.22 ?  708  ARG   B CB  1 
ATOM   5020 C  CG  A ARG   B 1 267 ? 39.296 10.734  21.146  0.57 18.56 ?  708  ARG   B CG  1 
ATOM   5021 C  CG  B ARG   B 1 267 ? 39.253 10.881  21.561  0.43 17.26 ?  708  ARG   B CG  1 
ATOM   5022 C  CD  A ARG   B 1 267 ? 39.135 11.681  19.961  0.57 21.38 ?  708  ARG   B CD  1 
ATOM   5023 C  CD  B ARG   B 1 267 ? 39.072 12.269  20.953  0.43 16.75 ?  708  ARG   B CD  1 
ATOM   5024 N  NE  A ARG   B 1 267 ? 39.496 11.024  18.707  0.57 21.79 ?  708  ARG   B NE  1 
ATOM   5025 N  NE  B ARG   B 1 267 ? 39.554 13.325  21.843  0.43 17.32 ?  708  ARG   B NE  1 
ATOM   5026 C  CZ  A ARG   B 1 267 ? 40.082 11.630  17.679  0.57 22.40 ?  708  ARG   B CZ  1 
ATOM   5027 C  CZ  B ARG   B 1 267 ? 40.025 14.497  21.427  0.43 16.61 ?  708  ARG   B CZ  1 
ATOM   5028 N  NH1 A ARG   B 1 267 ? 40.382 12.923  17.742  0.57 21.66 ?  708  ARG   B NH1 1 
ATOM   5029 N  NH1 B ARG   B 1 267 ? 40.082 14.769  20.133  0.43 14.84 ?  708  ARG   B NH1 1 
ATOM   5030 N  NH2 A ARG   B 1 267 ? 40.371 10.940  16.586  0.57 24.77 ?  708  ARG   B NH2 1 
ATOM   5031 N  NH2 B ARG   B 1 267 ? 40.437 15.402  22.303  0.43 15.59 ?  708  ARG   B NH2 1 
ATOM   5032 N  N   . GLY   B 1 268 ? 39.175 7.594   22.645  1.00 13.36 ?  709  GLY   B N   1 
ATOM   5033 C  CA  . GLY   B 1 268 ? 38.317 6.469   22.348  1.00 13.10 ?  709  GLY   B CA  1 
ATOM   5034 C  C   . GLY   B 1 268 ? 38.694 5.164   23.023  1.00 11.00 ?  709  GLY   B C   1 
ATOM   5035 O  O   . GLY   B 1 268 ? 37.900 4.213   22.985  1.00 12.44 ?  709  GLY   B O   1 
ATOM   5036 N  N   . ASP   B 1 269 ? 39.877 5.064   23.617  1.00 10.85 ?  710  ASP   B N   1 
ATOM   5037 C  CA  . ASP   B 1 269 ? 40.233 3.807   24.268  1.00 12.26 ?  710  ASP   B CA  1 
ATOM   5038 C  C   . ASP   B 1 269 ? 39.255 3.494   25.400  1.00 11.93 ?  710  ASP   B C   1 
ATOM   5039 O  O   . ASP   B 1 269 ? 38.875 4.398   26.154  1.00 14.16 ?  710  ASP   B O   1 
ATOM   5040 C  CB  . ASP   B 1 269 ? 41.657 3.853   24.824  1.00 12.67 ?  710  ASP   B CB  1 
ATOM   5041 C  CG  . ASP   B 1 269 ? 42.164 2.482   25.194  1.00 12.87 ?  710  ASP   B CG  1 
ATOM   5042 O  OD1 . ASP   B 1 269 ? 42.627 1.754   24.288  1.00 10.93 ?  710  ASP   B OD1 1 
ATOM   5043 O  OD2 . ASP   B 1 269 ? 42.063 2.108   26.376  1.00 13.50 -1 710  ASP   B OD2 1 
ATOM   5044 N  N   . PRO   B 1 270 ? 38.854 2.225   25.570  1.00 12.21 ?  711  PRO   B N   1 
ATOM   5045 C  CA  . PRO   B 1 270 ? 37.922 1.885   26.659  1.00 13.21 ?  711  PRO   B CA  1 
ATOM   5046 C  C   . PRO   B 1 270 ? 38.556 1.825   28.042  1.00 11.69 ?  711  PRO   B C   1 
ATOM   5047 O  O   . PRO   B 1 270 ? 37.814 1.762   29.038  1.00 13.59 ?  711  PRO   B O   1 
ATOM   5048 C  CB  . PRO   B 1 270 ? 37.394 0.507   26.239  1.00 14.76 ?  711  PRO   B CB  1 
ATOM   5049 C  CG  . PRO   B 1 270 ? 38.506 -0.084  25.427  1.00 14.44 ?  711  PRO   B CG  1 
ATOM   5050 C  CD  . PRO   B 1 270 ? 39.071 1.085   24.663  1.00 13.24 ?  711  PRO   B CD  1 
ATOM   5051 N  N   . LEU   B 1 271 ? 39.882 1.884   28.149  1.00 12.21 ?  712  LEU   B N   1 
ATOM   5052 C  CA  . LEU   B 1 271 ? 40.587 1.704   29.411  1.00 13.17 ?  712  LEU   B CA  1 
ATOM   5053 C  C   . LEU   B 1 271 ? 41.498 2.863   29.799  1.00 13.52 ?  712  LEU   B C   1 
ATOM   5054 O  O   . LEU   B 1 271 ? 41.637 3.155   30.989  1.00 13.23 ?  712  LEU   B O   1 
ATOM   5055 C  CB  . LEU   B 1 271 ? 41.433 0.413   29.359  1.00 13.64 ?  712  LEU   B CB  1 
ATOM   5056 C  CG  . LEU   B 1 271 ? 40.632 -0.889  29.246  1.00 14.10 ?  712  LEU   B CG  1 
ATOM   5057 C  CD1 . LEU   B 1 271 ? 41.545 -2.082  29.017  1.00 16.70 ?  712  LEU   B CD1 1 
ATOM   5058 C  CD2 . LEU   B 1 271 ? 39.801 -1.104  30.504  1.00 15.97 ?  712  LEU   B CD2 1 
ATOM   5059 N  N   . GLY   B 1 272 ? 42.138 3.525   28.837  1.00 13.11 ?  713  GLY   B N   1 
ATOM   5060 C  CA  . GLY   B 1 272 ? 43.222 4.428   29.182  1.00 12.93 ?  713  GLY   B CA  1 
ATOM   5061 C  C   . GLY   B 1 272 ? 42.753 5.716   29.831  1.00 10.85 ?  713  GLY   B C   1 
ATOM   5062 O  O   . GLY   B 1 272 ? 43.435 6.262   30.699  1.00 14.23 ?  713  GLY   B O   1 
ATOM   5063 N  N   . GLY   B 1 273 ? 41.611 6.240   29.390  1.00 13.79 ?  714  GLY   B N   1 
ATOM   5064 C  CA  . GLY   B 1 273 ? 41.107 7.497   29.913  1.00 15.92 ?  714  GLY   B CA  1 
ATOM   5065 C  C   . GLY   B 1 273 ? 41.774 8.750   29.389  1.00 14.10 ?  714  GLY   B C   1 
ATOM   5066 O  O   . GLY   B 1 273 ? 41.561 9.823   29.966  1.00 16.91 ?  714  GLY   B O   1 
ATOM   5067 N  N   . PHE   B 1 274 ? 42.566 8.663   28.320  1.00 13.20 ?  715  PHE   B N   1 
ATOM   5068 C  CA  . PHE   B 1 274 ? 43.300 9.794   27.764  1.00 12.60 ?  715  PHE   B CA  1 
ATOM   5069 C  C   . PHE   B 1 274 ? 42.753 10.132  26.374  1.00 13.61 ?  715  PHE   B C   1 
ATOM   5070 O  O   . PHE   B 1 274 ? 41.818 9.502   25.870  1.00 14.48 ?  715  PHE   B O   1 
ATOM   5071 C  CB  . PHE   B 1 274 ? 44.803 9.488   27.724  1.00 11.72 ?  715  PHE   B CB  1 
ATOM   5072 C  CG  . PHE   B 1 274 ? 45.526 9.717   29.041  1.00 13.46 ?  715  PHE   B CG  1 
ATOM   5073 C  CD1 . PHE   B 1 274 ? 44.840 10.069  30.198  1.00 14.97 ?  715  PHE   B CD1 1 
ATOM   5074 C  CD2 . PHE   B 1 274 ? 46.903 9.590   29.099  1.00 13.00 ?  715  PHE   B CD2 1 
ATOM   5075 C  CE1 . PHE   B 1 274 ? 45.531 10.278  31.394  1.00 15.55 ?  715  PHE   B CE1 1 
ATOM   5076 C  CE2 . PHE   B 1 274 ? 47.592 9.796   30.282  1.00 14.86 ?  715  PHE   B CE2 1 
ATOM   5077 C  CZ  . PHE   B 1 274 ? 46.901 10.144  31.424  1.00 15.67 ?  715  PHE   B CZ  1 
ATOM   5078 N  N   . GLN   B 1 275 ? 43.347 11.138  25.733  1.00 12.41 ?  716  GLN   B N   1 
ATOM   5079 C  CA  . GLN   B 1 275 ? 42.784 11.641  24.482  1.00 13.38 ?  716  GLN   B CA  1 
ATOM   5080 C  C   . GLN   B 1 275 ? 43.865 12.053  23.482  1.00 13.43 ?  716  GLN   B C   1 
ATOM   5081 O  O   . GLN   B 1 275 ? 43.696 13.018  22.731  1.00 14.27 ?  716  GLN   B O   1 
ATOM   5082 C  CB  . GLN   B 1 275 ? 41.787 12.777  24.723  1.00 16.26 ?  716  GLN   B CB  1 
ATOM   5083 C  CG  . GLN   B 1 275 ? 42.346 13.990  25.444  1.00 20.30 ?  716  GLN   B CG  1 
ATOM   5084 C  CD  . GLN   B 1 275 ? 41.250 14.981  25.864  1.00 22.89 ?  716  GLN   B CD  1 
ATOM   5085 O  OE1 . GLN   B 1 275 ? 40.290 15.209  25.123  1.00 23.11 ?  716  GLN   B OE1 1 
ATOM   5086 N  NE2 . GLN   B 1 275 ? 41.390 15.563  27.057  1.00 22.45 ?  716  GLN   B NE2 1 
ATOM   5087 N  N   . VAL   B 1 276 ? 44.985 11.322  23.437  1.00 12.26 ?  717  VAL   B N   1 
ATOM   5088 C  CA  . VAL   B 1 276 ? 45.955 11.539  22.362  1.00 12.82 ?  717  VAL   B CA  1 
ATOM   5089 C  C   . VAL   B 1 276 ? 45.300 11.205  21.023  1.00 12.18 ?  717  VAL   B C   1 
ATOM   5090 O  O   . VAL   B 1 276 ? 44.588 10.201  20.886  1.00 11.64 ?  717  VAL   B O   1 
ATOM   5091 C  CB  . VAL   B 1 276 ? 47.234 10.711  22.596  1.00 10.98 ?  717  VAL   B CB  1 
ATOM   5092 C  CG1 . VAL   B 1 276 ? 48.283 10.986  21.509  1.00 13.23 ?  717  VAL   B CG1 1 
ATOM   5093 C  CG2 . VAL   B 1 276 ? 47.827 11.004  23.974  1.00 12.46 ?  717  VAL   B CG2 1 
ATOM   5094 N  N   . THR   B 1 277 ? 45.512 12.068  20.034  1.00 12.22 ?  718  THR   B N   1 
ATOM   5095 C  CA  . THR   B 1 277 ? 44.876 11.917  18.731  1.00 13.55 ?  718  THR   B CA  1 
ATOM   5096 C  C   . THR   B 1 277 ? 45.808 11.199  17.768  1.00 13.12 ?  718  THR   B C   1 
ATOM   5097 O  O   . THR   B 1 277 ? 47.008 11.065  18.027  1.00 13.43 ?  718  THR   B O   1 
ATOM   5098 C  CB  . THR   B 1 277 ? 44.534 13.295  18.148  1.00 14.02 ?  718  THR   B CB  1 
ATOM   5099 O  OG1 . THR   B 1 277 ? 45.737 13.962  17.777  1.00 14.28 ?  718  THR   B OG1 1 
ATOM   5100 C  CG2 . THR   B 1 277 ? 43.769 14.150  19.139  1.00 14.87 ?  718  THR   B CG2 1 
ATOM   5101 N  N   . PRO   B 1 278 ? 45.291 10.704  16.635  1.00 11.97 ?  719  PRO   B N   1 
ATOM   5102 C  CA  . PRO   B 1 278 ? 46.195 10.082  15.647  1.00 11.93 ?  719  PRO   B CA  1 
ATOM   5103 C  C   . PRO   B 1 278 ? 47.265 11.035  15.142  1.00 12.49 ?  719  PRO   B C   1 
ATOM   5104 O  O   . PRO   B 1 278 ? 48.428 10.637  14.987  1.00 12.85 ?  719  PRO   B O   1 
ATOM   5105 C  CB  . PRO   B 1 278 ? 45.243 9.621   14.531  1.00 13.86 ?  719  PRO   B CB  1 
ATOM   5106 C  CG  . PRO   B 1 278 ? 43.943 9.396   15.256  1.00 13.82 ?  719  PRO   B CG  1 
ATOM   5107 C  CD  . PRO   B 1 278 ? 43.874 10.484  16.284  1.00 14.10 ?  719  PRO   B CD  1 
ATOM   5108 N  N   . GLU   B 1 279 ? 46.901 12.297  14.915  1.00 12.18 ?  720  GLU   B N   1 
ATOM   5109 C  CA  . GLU   B 1 279 ? 47.869 13.309  14.524  1.00 13.24 ?  720  GLU   B CA  1 
ATOM   5110 C  C   . GLU   B 1 279 ? 48.892 13.545  15.631  1.00 11.95 ?  720  GLU   B C   1 
ATOM   5111 O  O   . GLU   B 1 279 ? 50.053 13.851  15.338  1.00 13.42 ?  720  GLU   B O   1 
ATOM   5112 C  CB  . GLU   B 1 279 ? 47.129 14.605  14.175  1.00 13.56 ?  720  GLU   B CB  1 
ATOM   5113 C  CG  . GLU   B 1 279 ? 46.152 14.491  12.985  1.00 17.26 ?  720  GLU   B CG  1 
ATOM   5114 C  CD  . GLU   B 1 279 ? 44.844 13.777  13.324  1.00 22.35 ?  720  GLU   B CD  1 
ATOM   5115 O  OE1 . GLU   B 1 279 ? 44.511 13.631  14.520  1.00 18.55 ?  720  GLU   B OE1 1 
ATOM   5116 O  OE2 . GLU   B 1 279 ? 44.136 13.362  12.382  1.00 24.92 -1 720  GLU   B OE2 1 
ATOM   5117 N  N   . GLY   B 1 280 ? 48.480 13.422  16.900  1.00 11.91 ?  721  GLY   B N   1 
ATOM   5118 C  CA  . GLY   B 1 280 ? 49.436 13.506  18.001  1.00 13.02 ?  721  GLY   B CA  1 
ATOM   5119 C  C   . GLY   B 1 280 ? 50.500 12.430  17.925  1.00 11.58 ?  721  GLY   B C   1 
ATOM   5120 O  O   . GLY   B 1 280 ? 51.701 12.716  17.965  1.00 11.92 ?  721  GLY   B O   1 
ATOM   5121 N  N   . TYR   B 1 281 ? 50.070 11.175  17.766  1.00 10.59 ?  722  TYR   B N   1 
ATOM   5122 C  CA  . TYR   B 1 281 ? 51.023 10.079  17.600  1.00 11.10 ?  722  TYR   B CA  1 
ATOM   5123 C  C   . TYR   B 1 281 ? 51.910 10.294  16.382  1.00 12.35 ?  722  TYR   B C   1 
ATOM   5124 O  O   . TYR   B 1 281 ? 53.101 9.967   16.415  1.00 12.83 ?  722  TYR   B O   1 
ATOM   5125 C  CB  . TYR   B 1 281 ? 50.290 8.748   17.480  1.00 9.96  ?  722  TYR   B CB  1 
ATOM   5126 C  CG  . TYR   B 1 281 ? 49.650 8.257   18.754  1.00 11.76 ?  722  TYR   B CG  1 
ATOM   5127 C  CD1 . TYR   B 1 281 ? 50.429 7.807   19.802  1.00 10.98 ?  722  TYR   B CD1 1 
ATOM   5128 C  CD2 . TYR   B 1 281 ? 48.268 8.224   18.900  1.00 11.44 ?  722  TYR   B CD2 1 
ATOM   5129 C  CE1 . TYR   B 1 281 ? 49.858 7.345   20.968  1.00 10.92 ?  722  TYR   B CE1 1 
ATOM   5130 C  CE2 . TYR   B 1 281 ? 47.674 7.757   20.071  1.00 12.69 ?  722  TYR   B CE2 1 
ATOM   5131 C  CZ  . TYR   B 1 281 ? 48.478 7.332   21.101  1.00 11.39 ?  722  TYR   B CZ  1 
ATOM   5132 O  OH  . TYR   B 1 281 ? 47.902 6.862   22.235  1.00 11.36 ?  722  TYR   B OH  1 
ATOM   5133 N  N   . ALA   B 1 282 ? 51.361 10.868  15.304  1.00 11.46 ?  723  ALA   B N   1 
ATOM   5134 C  CA  . ALA   B 1 282 ? 52.191 11.165  14.137  1.00 11.62 ?  723  ALA   B CA  1 
ATOM   5135 C  C   . ALA   B 1 282 ? 53.298 12.156  14.482  1.00 11.47 ?  723  ALA   B C   1 
ATOM   5136 O  O   . ALA   B 1 282 ? 54.454 11.967  14.090  1.00 12.22 ?  723  ALA   B O   1 
ATOM   5137 C  CB  . ALA   B 1 282 ? 51.321 11.703  13.002  1.00 11.68 ?  723  ALA   B CB  1 
ATOM   5138 N  N   . HIS   B 1 283 ? 52.971 13.212  15.228  1.00 12.96 ?  724  HIS   B N   1 
ATOM   5139 C  CA  . HIS   B 1 283 ? 54.006 14.166  15.613  1.00 13.36 ?  724  HIS   B CA  1 
ATOM   5140 C  C   . HIS   B 1 283 ? 55.061 13.530  16.510  1.00 12.47 ?  724  HIS   B C   1 
ATOM   5141 O  O   . HIS   B 1 283 ? 56.259 13.797  16.346  1.00 13.90 ?  724  HIS   B O   1 
ATOM   5142 C  CB  . HIS   B 1 283 ? 53.385 15.386  16.277  1.00 14.54 ?  724  HIS   B CB  1 
ATOM   5143 C  CG  . HIS   B 1 283 ? 52.830 16.363  15.297  1.00 16.05 ?  724  HIS   B CG  1 
ATOM   5144 N  ND1 . HIS   B 1 283 ? 53.449 17.561  15.015  1.00 18.47 ?  724  HIS   B ND1 1 
ATOM   5145 C  CD2 . HIS   B 1 283 ? 51.732 16.309  14.509  1.00 15.53 ?  724  HIS   B CD2 1 
ATOM   5146 C  CE1 . HIS   B 1 283 ? 52.745 18.212  14.106  1.00 18.90 ?  724  HIS   B CE1 1 
ATOM   5147 N  NE2 . HIS   B 1 283 ? 51.703 17.471  13.773  1.00 17.83 ?  724  HIS   B NE2 1 
ATOM   5148 N  N   . LEU   B 1 284 ? 54.640 12.677  17.451  1.00 12.91 ?  725  LEU   B N   1 
ATOM   5149 C  CA  . LEU   B 1 284 ? 55.605 11.980  18.301  1.00 11.78 ?  725  LEU   B CA  1 
ATOM   5150 C  C   . LEU   B 1 284 ? 56.545 11.110  17.469  1.00 10.68 ?  725  LEU   B C   1 
ATOM   5151 O  O   . LEU   B 1 284 ? 57.770 11.126  17.658  1.00 12.61 ?  725  LEU   B O   1 
ATOM   5152 C  CB  . LEU   B 1 284 ? 54.877 11.152  19.362  1.00 12.78 ?  725  LEU   B CB  1 
ATOM   5153 C  CG  . LEU   B 1 284 ? 53.907 11.905  20.291  1.00 12.46 ?  725  LEU   B CG  1 
ATOM   5154 C  CD1 . LEU   B 1 284 ? 53.402 10.982  21.412  1.00 13.02 ?  725  LEU   B CD1 1 
ATOM   5155 C  CD2 . LEU   B 1 284 ? 54.571 13.138  20.899  1.00 13.80 ?  725  LEU   B CD2 1 
ATOM   5156 N  N   . THR   B 1 285 ? 55.983 10.359  16.514  1.00 9.85  ?  726  THR   B N   1 
ATOM   5157 C  CA  . THR   B 1 285 ? 56.802 9.519   15.646  1.00 11.52 ?  726  THR   B CA  1 
ATOM   5158 C  C   . THR   B 1 285 ? 57.796 10.357  14.859  1.00 11.29 ?  726  THR   B C   1 
ATOM   5159 O  O   . THR   B 1 285 ? 58.989 10.025  14.793  1.00 12.52 ?  726  THR   B O   1 
ATOM   5160 C  CB  . THR   B 1 285 ? 55.908 8.751   14.676  1.00 10.71 ?  726  THR   B CB  1 
ATOM   5161 O  OG1 . THR   B 1 285 ? 54.979 7.950   15.412  1.00 12.08 ?  726  THR   B OG1 1 
ATOM   5162 C  CG2 . THR   B 1 285 ? 56.756 7.836   13.812  1.00 11.38 ?  726  THR   B CG2 1 
ATOM   5163 N  N   . HIS   B 1 286 ? 57.312 11.448  14.255  1.00 10.62 ?  727  HIS   B N   1 
ATOM   5164 C  CA  . HIS   B 1 286 ? 58.182 12.313  13.470  1.00 11.98 ?  727  HIS   B CA  1 
ATOM   5165 C  C   . HIS   B 1 286 ? 59.351 12.841  14.299  1.00 11.60 ?  727  HIS   B C   1 
ATOM   5166 O  O   . HIS   B 1 286 ? 60.480 12.938  13.799  1.00 14.75 ?  727  HIS   B O   1 
ATOM   5167 C  CB  . HIS   B 1 286 ? 57.360 13.451  12.869  1.00 13.54 ?  727  HIS   B CB  1 
ATOM   5168 C  CG  . HIS   B 1 286 ? 58.100 14.238  11.840  1.00 18.00 ?  727  HIS   B CG  1 
ATOM   5169 N  ND1 . HIS   B 1 286 ? 58.664 15.463  12.109  1.00 17.72 ?  727  HIS   B ND1 1 
ATOM   5170 C  CD2 . HIS   B 1 286 ? 58.367 13.974  10.539  1.00 18.78 ?  727  HIS   B CD2 1 
ATOM   5171 C  CE1 . HIS   B 1 286 ? 59.251 15.925  11.017  1.00 20.03 ?  727  HIS   B CE1 1 
ATOM   5172 N  NE2 . HIS   B 1 286 ? 59.084 15.040  10.050  1.00 19.97 ?  727  HIS   B NE2 1 
ATOM   5173 N  N   . GLN   B 1 287 ? 59.109 13.172  15.571  1.00 12.68 ?  728  GLN   B N   1 
ATOM   5174 C  CA  . GLN   B 1 287 ? 60.202 13.639  16.425  1.00 11.30 ?  728  GLN   B CA  1 
ATOM   5175 C  C   . GLN   B 1 287 ? 61.229 12.537  16.674  1.00 12.71 ?  728  GLN   B C   1 
ATOM   5176 O  O   . GLN   B 1 287 ? 62.439 12.784  16.609  1.00 12.02 ?  728  GLN   B O   1 
ATOM   5177 C  CB  . GLN   B 1 287 ? 59.638 14.168  17.737  1.00 13.49 ?  728  GLN   B CB  1 
ATOM   5178 C  CG  . GLN   B 1 287 ? 58.832 15.444  17.577  1.00 15.16 ?  728  GLN   B CG  1 
ATOM   5179 C  CD  . GLN   B 1 287 ? 58.416 16.039  18.901  1.00 19.30 ?  728  GLN   B CD  1 
ATOM   5180 O  OE1 . GLN   B 1 287 ? 59.193 16.064  19.857  1.00 19.98 ?  728  GLN   B OE1 1 
ATOM   5181 N  NE2 . GLN   B 1 287 ? 57.188 16.532  18.961  1.00 21.24 ?  728  GLN   B NE2 1 
ATOM   5182 N  N   . LEU   B 1 288 ? 60.772 11.313  16.941  1.00 11.55 ?  729  LEU   B N   1 
ATOM   5183 C  CA  . LEU   B 1 288 ? 61.710 10.222  17.185  1.00 11.63 ?  729  LEU   B CA  1 
ATOM   5184 C  C   . LEU   B 1 288 ? 62.528 9.888   15.941  1.00 12.43 ?  729  LEU   B C   1 
ATOM   5185 O  O   . LEU   B 1 288 ? 63.659 9.409   16.062  1.00 13.19 ?  729  LEU   B O   1 
ATOM   5186 C  CB  . LEU   B 1 288 ? 60.979 8.992   17.741  1.00 11.56 ?  729  LEU   B CB  1 
ATOM   5187 C  CG  . LEU   B 1 288 ? 60.264 9.155   19.094  1.00 13.11 ?  729  LEU   B CG  1 
ATOM   5188 C  CD1 . LEU   B 1 288 ? 59.665 7.817   19.500  1.00 14.52 ?  729  LEU   B CD1 1 
ATOM   5189 C  CD2 . LEU   B 1 288 ? 61.213 9.666   20.172  1.00 13.64 ?  729  LEU   B CD2 1 
ATOM   5190 N  N   . MET   B 1 289 ? 61.990 10.149  14.748  1.00 12.79 ?  730  MET   B N   1 
ATOM   5191 C  CA  . MET   B 1 289 ? 62.722 9.876   13.515  1.00 12.84 ?  730  MET   B CA  1 
ATOM   5192 C  C   . MET   B 1 289 ? 63.965 10.734  13.382  1.00 13.47 ?  730  MET   B C   1 
ATOM   5193 O  O   . MET   B 1 289 ? 64.852 10.393  12.591  1.00 14.09 ?  730  MET   B O   1 
ATOM   5194 C  CB  . MET   B 1 289 ? 61.806 10.104  12.316  1.00 13.54 ?  730  MET   B CB  1 
ATOM   5195 C  CG  . MET   B 1 289 ? 60.729 9.055   12.171  1.00 12.69 ?  730  MET   B CG  1 
ATOM   5196 S  SD  . MET   B 1 289 ? 59.521 9.424   10.879  1.00 14.95 ?  730  MET   B SD  1 
ATOM   5197 C  CE  . MET   B 1 289 ? 60.573 9.524   9.417   1.00 13.02 ?  730  MET   B CE  1 
ATOM   5198 N  N   . SER   B 1 290 ? 64.051 11.834  14.136  1.00 12.58 ?  731  SER   B N   1 
ATOM   5199 C  CA  . SER   B 1 290 ? 65.227 12.688  14.112  1.00 12.80 ?  731  SER   B CA  1 
ATOM   5200 C  C   . SER   B 1 290 ? 66.381 12.118  14.918  1.00 14.00 ?  731  SER   B C   1 
ATOM   5201 O  O   . SER   B 1 290 ? 67.473 12.693  14.890  1.00 17.25 ?  731  SER   B O   1 
ATOM   5202 C  CB  . SER   B 1 290 ? 64.869 14.099  14.584  1.00 13.75 ?  731  SER   B CB  1 
ATOM   5203 O  OG  . SER   B 1 290 ? 64.693 14.140  15.988  1.00 16.59 ?  731  SER   B OG  1 
ATOM   5204 N  N   . LEU   B 1 291 ? 66.169 11.002  15.609  1.00 12.90 ?  732  LEU   B N   1 
ATOM   5205 C  CA  . LEU   B 1 291 ? 67.183 10.336  16.410  1.00 13.29 ?  732  LEU   B CA  1 
ATOM   5206 C  C   . LEU   B 1 291 ? 67.737 9.131   15.661  1.00 15.02 ?  732  LEU   B C   1 
ATOM   5207 O  O   . LEU   B 1 291 ? 67.094 8.579   14.766  1.00 14.92 ?  732  LEU   B O   1 
ATOM   5208 C  CB  . LEU   B 1 291 ? 66.557 9.847   17.715  1.00 14.15 ?  732  LEU   B CB  1 
ATOM   5209 C  CG  . LEU   B 1 291 ? 65.866 10.862  18.611  1.00 13.91 ?  732  LEU   B CG  1 
ATOM   5210 C  CD1 . LEU   B 1 291 ? 65.026 10.120  19.645  1.00 13.56 ?  732  LEU   B CD1 1 
ATOM   5211 C  CD2 . LEU   B 1 291 ? 66.916 11.737  19.290  1.00 16.44 ?  732  LEU   B CD2 1 
ATOM   5212 N  N   . ALA   B 1 292 ? 68.951 8.728   16.038  1.00 14.72 ?  733  ALA   B N   1 
ATOM   5213 C  CA  . ALA   B 1 292 ? 69.543 7.460   15.598  1.00 14.09 ?  733  ALA   B CA  1 
ATOM   5214 C  C   . ALA   B 1 292 ? 69.634 7.346   14.078  1.00 14.14 ?  733  ALA   B C   1 
ATOM   5215 O  O   . ALA   B 1 292 ? 69.553 6.248   13.520  1.00 14.31 ?  733  ALA   B O   1 
ATOM   5216 C  CB  . ALA   B 1 292 ? 68.820 6.245   16.194  1.00 13.39 ?  733  ALA   B CB  1 
ATOM   5217 N  N   . ALA   B 1 293 ? 69.817 8.479   13.402  1.00 13.09 ?  734  ALA   B N   1 
ATOM   5218 C  CA  . ALA   B 1 293 ? 69.849 8.518   11.940  1.00 15.29 ?  734  ALA   B CA  1 
ATOM   5219 C  C   . ALA   B 1 293 ? 68.600 7.876   11.343  1.00 16.19 ?  734  ALA   B C   1 
ATOM   5220 O  O   . ALA   B 1 293 ? 68.647 7.245   10.283  1.00 16.62 ?  734  ALA   B O   1 
ATOM   5221 C  CB  . ALA   B 1 293 ? 71.137 7.906   11.377  1.00 16.08 ?  734  ALA   B CB  1 
ATOM   5222 N  N   . GLY   B 1 294 ? 67.477 8.019   12.050  1.00 14.08 ?  735  GLY   B N   1 
ATOM   5223 C  CA  . GLY   B 1 294 ? 66.200 7.519   11.600  1.00 14.40 ?  735  GLY   B CA  1 
ATOM   5224 C  C   . GLY   B 1 294 ? 65.949 6.054   11.867  1.00 13.06 ?  735  GLY   B C   1 
ATOM   5225 O  O   . GLY   B 1 294 ? 64.913 5.532   11.435  1.00 12.85 ?  735  GLY   B O   1 
ATOM   5226 N  N   . ARG   B 1 295 ? 66.841 5.373   12.581  1.00 12.90 ?  736  ARG   B N   1 
ATOM   5227 C  CA  . ARG   B 1 295 ? 66.682 3.939   12.812  1.00 11.60 ?  736  ARG   B CA  1 
ATOM   5228 C  C   . ARG   B 1 295 ? 65.687 3.720   13.950  1.00 11.20 ?  736  ARG   B C   1 
ATOM   5229 O  O   . ARG   B 1 295 ? 66.055 3.615   15.123  1.00 12.24 ?  736  ARG   B O   1 
ATOM   5230 C  CB  . ARG   B 1 295 ? 68.029 3.286   13.068  1.00 14.54 ?  736  ARG   B CB  1 
ATOM   5231 C  CG  . ARG   B 1 295 ? 68.929 3.373   11.834  1.00 16.95 ?  736  ARG   B CG  1 
ATOM   5232 C  CD  . ARG   B 1 295 ? 70.160 2.493   11.954  1.00 18.84 ?  736  ARG   B CD  1 
ATOM   5233 N  NE  . ARG   B 1 295 ? 71.013 2.613   10.770  1.00 23.12 ?  736  ARG   B NE  1 
ATOM   5234 C  CZ  . ARG   B 1 295 ? 72.062 3.430   10.679  1.00 30.81 ?  736  ARG   B CZ  1 
ATOM   5235 N  NH1 . ARG   B 1 295 ? 72.399 4.207   11.702  1.00 32.60 ?  736  ARG   B NH1 1 
ATOM   5236 N  NH2 . ARG   B 1 295 ? 72.775 3.473   9.561   1.00 32.96 ?  736  ARG   B NH2 1 
ATOM   5237 N  N   . VAL   B 1 296 ? 64.402 3.641   13.582  1.00 10.24 ?  737  VAL   B N   1 
ATOM   5238 C  CA  . VAL   B 1 296 ? 63.288 3.543   14.523  1.00 10.65 ?  737  VAL   B CA  1 
ATOM   5239 C  C   . VAL   B 1 296 ? 62.464 2.300   14.204  1.00 9.77  ?  737  VAL   B C   1 
ATOM   5240 O  O   . VAL   B 1 296 ? 62.092 2.081   13.043  1.00 11.74 ?  737  VAL   B O   1 
ATOM   5241 C  CB  . VAL   B 1 296 ? 62.386 4.789   14.445  1.00 12.00 ?  737  VAL   B CB  1 
ATOM   5242 C  CG1 . VAL   B 1 296 ? 61.141 4.636   15.337  1.00 12.82 ?  737  VAL   B CG1 1 
ATOM   5243 C  CG2 . VAL   B 1 296 ? 63.154 6.073   14.734  1.00 11.36 ?  737  VAL   B CG2 1 
ATOM   5244 N  N   . LEU   B 1 297 ? 62.142 1.512   15.234  1.00 10.32 ?  738  LEU   B N   1 
ATOM   5245 C  CA  . LEU   B 1 297 ? 61.236 0.373   15.100  1.00 11.45 ?  738  LEU   B CA  1 
ATOM   5246 C  C   . LEU   B 1 297 ? 60.055 0.569   16.045  1.00 10.97 ?  738  LEU   B C   1 
ATOM   5247 O  O   . LEU   B 1 297 ? 60.239 0.689   17.256  1.00 10.92 ?  738  LEU   B O   1 
ATOM   5248 C  CB  . LEU   B 1 297 ? 61.970 -0.931  15.393  1.00 11.07 ?  738  LEU   B CB  1 
ATOM   5249 C  CG  . LEU   B 1 297 ? 61.110 -2.176  15.611  1.00 12.78 ?  738  LEU   B CG  1 
ATOM   5250 C  CD1 . LEU   B 1 297 ? 60.211 -2.505  14.407  1.00 13.21 ?  738  LEU   B CD1 1 
ATOM   5251 C  CD2 . LEU   B 1 297 ? 62.018 -3.344  15.979  1.00 15.44 ?  738  LEU   B CD2 1 
ATOM   5252 N  N   . ILE   B 1 298 ? 58.853 0.651   15.487  1.00 9.95  ?  739  ILE   B N   1 
ATOM   5253 C  CA  . ILE   B 1 298 ? 57.626 0.868   16.253  1.00 9.96  ?  739  ILE   B CA  1 
ATOM   5254 C  C   . ILE   B 1 298 ? 56.987 -0.489  16.529  1.00 11.45 ?  739  ILE   B C   1 
ATOM   5255 O  O   . ILE   B 1 298 ? 56.642 -1.216  15.593  1.00 11.86 ?  739  ILE   B O   1 
ATOM   5256 C  CB  . ILE   B 1 298 ? 56.660 1.788   15.491  1.00 11.24 ?  739  ILE   B CB  1 
ATOM   5257 C  CG1 . ILE   B 1 298 ? 57.317 3.160   15.258  1.00 12.65 ?  739  ILE   B CG1 1 
ATOM   5258 C  CG2 . ILE   B 1 298 ? 55.342 1.894   16.223  1.00 10.72 ?  739  ILE   B CG2 1 
ATOM   5259 C  CD1 . ILE   B 1 298 ? 56.501 4.123   14.454  1.00 14.33 ?  739  ILE   B CD1 1 
ATOM   5260 N  N   . ILE   B 1 299 ? 56.811 -0.833  17.805  1.00 9.85  ?  740  ILE   B N   1 
ATOM   5261 C  CA  . ILE   B 1 299 ? 56.309 -2.141  18.226  1.00 8.76  ?  740  ILE   B CA  1 
ATOM   5262 C  C   . ILE   B 1 299 ? 54.963 -1.955  18.930  1.00 9.04  ?  740  ILE   B C   1 
ATOM   5263 O  O   . ILE   B 1 299 ? 54.888 -1.281  19.963  1.00 10.66 ?  740  ILE   B O   1 
ATOM   5264 C  CB  . ILE   B 1 299 ? 57.294 -2.827  19.187  1.00 9.80  ?  740  ILE   B CB  1 
ATOM   5265 C  CG1 . ILE   B 1 299 ? 58.657 -2.967  18.518  1.00 10.86 ?  740  ILE   B CG1 1 
ATOM   5266 C  CG2 . ILE   B 1 299 ? 56.766 -4.181  19.626  1.00 10.83 ?  740  ILE   B CG2 1 
ATOM   5267 C  CD1 . ILE   B 1 299 ? 59.731 -3.543  19.424  1.00 13.60 ?  740  ILE   B CD1 1 
ATOM   5268 N  N   . LEU   B 1 300 ? 53.907 -2.576  18.403  1.00 9.52  ?  741  LEU   B N   1 
ATOM   5269 C  CA  . LEU   B 1 300 ? 52.604 -2.500  19.067  1.00 10.05 ?  741  LEU   B CA  1 
ATOM   5270 C  C   . LEU   B 1 300 ? 52.657 -3.095  20.475  1.00 10.89 ?  741  LEU   B C   1 
ATOM   5271 O  O   . LEU   B 1 300 ? 53.143 -4.214  20.667  1.00 11.41 ?  741  LEU   B O   1 
ATOM   5272 C  CB  . LEU   B 1 300 ? 51.569 -3.261  18.236  1.00 10.77 ?  741  LEU   B CB  1 
ATOM   5273 C  CG  . LEU   B 1 300 ? 50.146 -3.229  18.792  1.00 9.90  ?  741  LEU   B CG  1 
ATOM   5274 C  CD1 . LEU   B 1 300 ? 49.612 -1.810  18.795  1.00 11.15 ?  741  LEU   B CD1 1 
ATOM   5275 C  CD2 . LEU   B 1 300 ? 49.249 -4.179  18.001  1.00 11.64 ?  741  LEU   B CD2 1 
ATOM   5276 N  N   . GLU   B 1 301 ? 52.120 -2.353  21.453  1.00 10.33 ?  742  GLU   B N   1 
ATOM   5277 C  CA  . GLU   B 1 301 ? 51.895 -2.862  22.806  1.00 10.06 ?  742  GLU   B CA  1 
ATOM   5278 C  C   . GLU   B 1 301 ? 50.391 -2.998  23.023  1.00 10.70 ?  742  GLU   B C   1 
ATOM   5279 O  O   . GLU   B 1 301 ? 49.757 -3.832  22.371  1.00 10.95 ?  742  GLU   B O   1 
ATOM   5280 C  CB  . GLU   B 1 301 ? 52.590 -2.000  23.880  1.00 10.75 ?  742  GLU   B CB  1 
ATOM   5281 C  CG  . GLU   B 1 301 ? 54.137 -1.951  23.778  1.00 11.90 ?  742  GLU   B CG  1 
ATOM   5282 C  CD  . GLU   B 1 301 ? 54.878 -3.165  24.374  1.00 13.22 ?  742  GLU   B CD  1 
ATOM   5283 O  OE1 . GLU   B 1 301 ? 54.246 -4.152  24.793  1.00 12.81 ?  742  GLU   B OE1 1 
ATOM   5284 O  OE2 . GLU   B 1 301 ? 56.128 -3.135  24.421  1.00 12.13 -1 742  GLU   B OE2 1 
ATOM   5285 N  N   . GLY   B 1 302 ? 49.801 -2.189  23.908  1.00 11.28 ?  743  GLY   B N   1 
ATOM   5286 C  CA  . GLY   B 1 302 ? 48.361 -2.180  24.117  1.00 10.55 ?  743  GLY   B CA  1 
ATOM   5287 C  C   . GLY   B 1 302 ? 47.619 -1.222  23.203  1.00 11.90 ?  743  GLY   B C   1 
ATOM   5288 O  O   . GLY   B 1 302 ? 48.137 -0.771  22.175  1.00 12.12 ?  743  GLY   B O   1 
ATOM   5289 N  N   . GLY   B 1 303 ? 46.382 -0.905  23.597  1.00 13.95 ?  744  GLY   B N   1 
ATOM   5290 C  CA  . GLY   B 1 303 ? 45.455 -0.158  22.763  1.00 11.47 ?  744  GLY   B CA  1 
ATOM   5291 C  C   . GLY   B 1 303 ? 44.259 -0.997  22.375  1.00 11.21 ?  744  GLY   B C   1 
ATOM   5292 O  O   . GLY   B 1 303 ? 44.414 -2.043  21.735  1.00 11.90 ?  744  GLY   B O   1 
ATOM   5293 N  N   . TYR   B 1 304 ? 43.054 -0.558  22.761  1.00 10.19 ?  745  TYR   B N   1 
ATOM   5294 C  CA  . TYR   B 1 304 ? 41.898 -1.445  22.791  1.00 11.53 ?  745  TYR   B CA  1 
ATOM   5295 C  C   . TYR   B 1 304 ? 40.672 -0.949  22.042  1.00 14.06 ?  745  TYR   B C   1 
ATOM   5296 O  O   . TYR   B 1 304 ? 39.704 -1.705  21.937  1.00 14.86 ?  745  TYR   B O   1 
ATOM   5297 C  CB  . TYR   B 1 304 ? 41.549 -1.826  24.247  1.00 11.96 ?  745  TYR   B CB  1 
ATOM   5298 C  CG  . TYR   B 1 304 ? 42.785 -2.397  24.870  1.00 12.34 ?  745  TYR   B CG  1 
ATOM   5299 C  CD1 . TYR   B 1 304 ? 43.214 -3.670  24.520  1.00 12.49 ?  745  TYR   B CD1 1 
ATOM   5300 C  CD2 . TYR   B 1 304 ? 43.597 -1.624  25.692  1.00 12.24 ?  745  TYR   B CD2 1 
ATOM   5301 C  CE1 . TYR   B 1 304 ? 44.381 -4.186  25.023  1.00 12.02 ?  745  TYR   B CE1 1 
ATOM   5302 C  CE2 . TYR   B 1 304 ? 44.772 -2.128  26.200  1.00 12.69 ?  745  TYR   B CE2 1 
ATOM   5303 C  CZ  . TYR   B 1 304 ? 45.154 -3.405  25.867  1.00 13.37 ?  745  TYR   B CZ  1 
ATOM   5304 O  OH  . TYR   B 1 304 ? 46.330 -3.917  26.364  1.00 15.19 ?  745  TYR   B OH  1 
ATOM   5305 N  N   . ASN   B 1 305 ? 40.679 0.266   21.506  1.00 9.89  ?  746  ASN   B N   1 
ATOM   5306 C  CA  . ASN   B 1 305 ? 39.634 0.697   20.584  1.00 10.20 ?  746  ASN   B CA  1 
ATOM   5307 C  C   . ASN   B 1 305 ? 40.146 0.377   19.185  1.00 9.95  ?  746  ASN   B C   1 
ATOM   5308 O  O   . ASN   B 1 305 ? 41.131 0.969   18.732  1.00 11.26 ?  746  ASN   B O   1 
ATOM   5309 C  CB  . ASN   B 1 305 ? 39.326 2.184   20.737  1.00 9.44  ?  746  ASN   B CB  1 
ATOM   5310 C  CG  . ASN   B 1 305 ? 38.243 2.660   19.770  1.00 11.51 ?  746  ASN   B CG  1 
ATOM   5311 O  OD1 . ASN   B 1 305 ? 38.338 2.462   18.561  1.00 11.09 ?  746  ASN   B OD1 1 
ATOM   5312 N  ND2 . ASN   B 1 305 ? 37.216 3.288   20.302  1.00 11.93 ?  746  ASN   B ND2 1 
ATOM   5313 N  N   . LEU   B 1 306 ? 39.510 -0.597  18.531  1.00 11.35 ?  747  LEU   B N   1 
ATOM   5314 C  CA  . LEU   B 1 306 ? 40.004 -1.098  17.250  1.00 11.54 ?  747  LEU   B CA  1 
ATOM   5315 C  C   . LEU   B 1 306 ? 40.168 0.019   16.227  1.00 10.66 ?  747  LEU   B C   1 
ATOM   5316 O  O   . LEU   B 1 306 ? 41.170 0.071   15.506  1.00 11.54 ?  747  LEU   B O   1 
ATOM   5317 C  CB  . LEU   B 1 306 ? 39.071 -2.185  16.706  1.00 12.13 ?  747  LEU   B CB  1 
ATOM   5318 C  CG  . LEU   B 1 306 ? 38.969 -3.441  17.574  1.00 12.17 ?  747  LEU   B CG  1 
ATOM   5319 C  CD1 . LEU   B 1 306 ? 37.900 -4.407  17.113  1.00 12.65 ?  747  LEU   B CD1 1 
ATOM   5320 C  CD2 . LEU   B 1 306 ? 40.312 -4.149  17.659  1.00 12.33 ?  747  LEU   B CD2 1 
ATOM   5321 N  N   . THR   B 1 307 ? 39.187 0.917   16.137  1.00 10.24 ?  748  THR   B N   1 
ATOM   5322 C  CA  . THR   B 1 307 ? 39.301 2.043   15.220  1.00 11.52 ?  748  THR   B CA  1 
ATOM   5323 C  C   . THR   B 1 307 ? 40.426 2.987   15.632  1.00 11.28 ?  748  THR   B C   1 
ATOM   5324 O  O   . THR   B 1 307 ? 41.232 3.404   14.797  1.00 12.68 ?  748  THR   B O   1 
ATOM   5325 C  CB  . THR   B 1 307 ? 37.962 2.775   15.142  1.00 13.72 ?  748  THR   B CB  1 
ATOM   5326 O  OG1 . THR   B 1 307 ? 36.997 1.905   14.537  1.00 12.96 ?  748  THR   B OG1 1 
ATOM   5327 C  CG2 . THR   B 1 307 ? 38.101 4.054   14.328  1.00 15.14 ?  748  THR   B CG2 1 
ATOM   5328 N  N   . SER   B 1 308 ? 40.508 3.326   16.917  1.00 11.57 ?  749  SER   B N   1 
ATOM   5329 C  CA  . SER   B 1 308 ? 41.546 4.250   17.367  1.00 11.87 ?  749  SER   B CA  1 
ATOM   5330 C  C   . SER   B 1 308 ? 42.942 3.711   17.096  1.00 10.38 ?  749  SER   B C   1 
ATOM   5331 O  O   . SER   B 1 308 ? 43.820 4.452   16.646  1.00 12.48 ?  749  SER   B O   1 
ATOM   5332 C  CB  . SER   B 1 308 ? 41.410 4.530   18.864  1.00 14.18 ?  749  SER   B CB  1 
ATOM   5333 O  OG  . SER   B 1 308 ? 40.146 5.075   19.195  1.00 13.99 ?  749  SER   B OG  1 
ATOM   5334 N  N   . ILE   B 1 309 ? 43.180 2.435   17.405  1.00 10.42 ?  750  ILE   B N   1 
ATOM   5335 C  CA  . ILE   B 1 309 ? 44.533 1.916   17.244  1.00 9.98  ?  750  ILE   B CA  1 
ATOM   5336 C  C   . ILE   B 1 309 ? 44.877 1.761   15.776  1.00 10.50 ?  750  ILE   B C   1 
ATOM   5337 O  O   . ILE   B 1 309 ? 46.037 1.942   15.380  1.00 10.59 ?  750  ILE   B O   1 
ATOM   5338 C  CB  . ILE   B 1 309 ? 44.766 0.612   18.031  1.00 9.79  ?  750  ILE   B CB  1 
ATOM   5339 C  CG1 . ILE   B 1 309 ? 44.033 -0.562  17.384  1.00 8.42  ?  750  ILE   B CG1 1 
ATOM   5340 C  CG2 . ILE   B 1 309 ? 44.361 0.785   19.501  1.00 10.69 ?  750  ILE   B CG2 1 
ATOM   5341 C  CD1 . ILE   B 1 309 ? 44.255 -1.891  18.080  1.00 10.33 ?  750  ILE   B CD1 1 
ATOM   5342 N  N   . SER   B 1 310 ? 43.887 1.441   14.942  1.00 9.68  ?  751  SER   B N   1 
ATOM   5343 C  CA  . SER   B 1 310 ? 44.148 1.331   13.519  1.00 10.70 ?  751  SER   B CA  1 
ATOM   5344 C  C   . SER   B 1 310 ? 44.511 2.682   12.921  1.00 10.69 ?  751  SER   B C   1 
ATOM   5345 O  O   . SER   B 1 310 ? 45.470 2.786   12.146  1.00 12.13 ?  751  SER   B O   1 
ATOM   5346 C  CB  . SER   B 1 310 ? 42.953 0.694   12.816  1.00 10.92 ?  751  SER   B CB  1 
ATOM   5347 O  OG  . SER   B 1 310 ? 42.713 -0.595  13.341  1.00 13.23 ?  751  SER   B OG  1 
ATOM   5348 N  N   . GLU   B 1 311 ? 43.753 3.730   13.254  1.00 11.83 ?  752  GLU   B N   1 
ATOM   5349 C  CA  . GLU   B 1 311 ? 44.073 5.050   12.724  1.00 12.44 ?  752  GLU   B CA  1 
ATOM   5350 C  C   . GLU   B 1 311 ? 45.392 5.550   13.290  1.00 11.64 ?  752  GLU   B C   1 
ATOM   5351 O  O   . GLU   B 1 311 ? 46.206 6.135   12.564  1.00 11.88 ?  752  GLU   B O   1 
ATOM   5352 C  CB  . GLU   B 1 311 ? 42.947 6.030   13.040  1.00 15.79 ?  752  GLU   B CB  1 
ATOM   5353 C  CG  . GLU   B 1 311 ? 43.040 7.348   12.291  1.00 20.80 ?  752  GLU   B CG  1 
ATOM   5354 C  CD  . GLU   B 1 311 ? 42.901 7.186   10.782  1.00 26.33 ?  752  GLU   B CD  1 
ATOM   5355 O  OE1 . GLU   B 1 311 ? 42.327 6.170   10.332  1.00 24.99 ?  752  GLU   B OE1 1 
ATOM   5356 O  OE2 . GLU   B 1 311 ? 43.368 8.083   10.051  1.00 29.72 -1 752  GLU   B OE2 1 
ATOM   5357 N  N   . SER   B 1 312 ? 45.632 5.303   14.577  1.00 11.80 ?  753  SER   B N   1 
ATOM   5358 C  CA  . SER   B 1 312 ? 46.815 5.862   15.217  1.00 10.29 ?  753  SER   B CA  1 
ATOM   5359 C  C   . SER   B 1 312 ? 48.082 5.205   14.687  1.00 9.51  ?  753  SER   B C   1 
ATOM   5360 O  O   . SER   B 1 312 ? 49.038 5.896   14.317  1.00 11.35 ?  753  SER   B O   1 
ATOM   5361 C  CB  . SER   B 1 312 ? 46.709 5.697   16.737  1.00 11.83 ?  753  SER   B CB  1 
ATOM   5362 O  OG  . SER   B 1 312 ? 45.659 6.515   17.233  1.00 12.77 ?  753  SER   B OG  1 
ATOM   5363 N  N   . MET   B 1 313 ? 48.108 3.868   14.629  1.00 10.61 ?  754  MET   B N   1 
ATOM   5364 C  CA  . MET   B 1 313 ? 49.326 3.200   14.192  1.00 10.87 ?  754  MET   B CA  1 
ATOM   5365 C  C   . MET   B 1 313 ? 49.589 3.448   12.711  1.00 9.61  ?  754  MET   B C   1 
ATOM   5366 O  O   . MET   B 1 313 ? 50.751 3.610   12.304  1.00 10.85 ?  754  MET   B O   1 
ATOM   5367 C  CB  . MET   B 1 313 ? 49.293 1.704   14.487  1.00 12.46 ?  754  MET   B CB  1 
ATOM   5368 C  CG  . MET   B 1 313 ? 50.703 1.112   14.487  1.00 11.44 ?  754  MET   B CG  1 
ATOM   5369 S  SD  . MET   B 1 313 ? 50.784 -0.595  15.042  1.00 17.48 ?  754  MET   B SD  1 
ATOM   5370 C  CE  . MET   B 1 313 ? 52.471 -0.679  15.650  1.00 12.87 ?  754  MET   B CE  1 
ATOM   5371 N  N   A SER   B 1 314 ? 48.531 3.532   11.893  0.45 9.96  ?  755  SER   B N   1 
ATOM   5372 N  N   B SER   B 1 314 ? 48.536 3.415   11.885  0.55 9.71  ?  755  SER   B N   1 
ATOM   5373 C  CA  A SER   B 1 314 ? 48.715 3.892   10.486  0.45 9.01  ?  755  SER   B CA  1 
ATOM   5374 C  CA  B SER   B 1 314 ? 48.726 3.657   10.456  0.55 9.23  ?  755  SER   B CA  1 
ATOM   5375 C  C   A SER   B 1 314 ? 49.297 5.294   10.336  0.45 9.46  ?  755  SER   B C   1 
ATOM   5376 C  C   B SER   B 1 314 ? 49.307 5.043   10.200  0.55 10.10 ?  755  SER   B C   1 
ATOM   5377 O  O   A SER   B 1 314 ? 50.130 5.538   9.454   0.45 10.49 ?  755  SER   B O   1 
ATOM   5378 O  O   B SER   B 1 314 ? 50.144 5.214   9.303   0.55 11.98 ?  755  SER   B O   1 
ATOM   5379 C  CB  A SER   B 1 314 ? 47.391 3.796   9.726   0.45 10.38 ?  755  SER   B CB  1 
ATOM   5380 C  CB  B SER   B 1 314 ? 47.423 3.428   9.677   0.55 10.22 ?  755  SER   B CB  1 
ATOM   5381 O  OG  A SER   B 1 314 ? 46.893 2.474   9.698   0.45 11.31 ?  755  SER   B OG  1 
ATOM   5382 O  OG  B SER   B 1 314 ? 46.412 4.368   10.019  0.55 11.53 ?  755  SER   B OG  1 
ATOM   5383 N  N   A MET   B 1 315 ? 48.863 6.236   11.182  0.45 10.43 ?  756  MET   B N   1 
ATOM   5384 N  N   B MET   B 1 315 ? 48.901 6.042   10.996  0.55 12.41 ?  756  MET   B N   1 
ATOM   5385 C  CA  A MET   B 1 315 ? 49.420 7.581   11.096  0.45 12.61 ?  756  MET   B CA  1 
ATOM   5386 C  CA  B MET   B 1 315 ? 49.482 7.372   10.829  0.55 13.10 ?  756  MET   B CA  1 
ATOM   5387 C  C   A MET   B 1 315 ? 50.904 7.585   11.432  0.45 12.01 ?  756  MET   B C   1 
ATOM   5388 C  C   B MET   B 1 315 ? 50.959 7.387   11.221  0.55 12.50 ?  756  MET   B C   1 
ATOM   5389 O  O   A MET   B 1 315 ? 51.659 8.418   10.919  0.45 12.45 ?  756  MET   B O   1 
ATOM   5390 O  O   B MET   B 1 315 ? 51.768 8.052   10.564  0.55 12.18 ?  756  MET   B O   1 
ATOM   5391 C  CB  A MET   B 1 315 ? 48.645 8.548   11.991  0.45 17.25 ?  756  MET   B CB  1 
ATOM   5392 C  CB  B MET   B 1 315 ? 48.664 8.444   11.564  0.55 15.02 ?  756  MET   B CB  1 
ATOM   5393 C  CG  A MET   B 1 315 ? 48.319 9.876   11.314  0.45 25.29 ?  756  MET   B CG  1 
ATOM   5394 C  CG  B MET   B 1 315 ? 48.584 9.804   10.818  0.55 15.29 ?  756  MET   B CG  1 
ATOM   5395 S  SD  A MET   B 1 315 ? 47.601 9.689   9.669   0.45 31.30 ?  756  MET   B SD  1 
ATOM   5396 S  SD  B MET   B 1 315 ? 47.414 10.991  11.538  0.55 16.33 ?  756  MET   B SD  1 
ATOM   5397 C  CE  A MET   B 1 315 ? 46.756 11.255  9.498   0.45 30.94 ?  756  MET   B CE  1 
ATOM   5398 C  CE  B MET   B 1 315 ? 45.899 10.575  10.670  0.55 17.48 ?  756  MET   B CE  1 
ATOM   5399 N  N   . CYS   B 1 316 ? 51.341 6.647   12.269  1.00 10.22 ?  757  CYS   B N   1 
ATOM   5400 C  CA  . CYS   B 1 316 ? 52.756 6.536   12.603  1.00 11.23 ?  757  CYS   B CA  1 
ATOM   5401 C  C   . CYS   B 1 316 ? 53.537 5.944   11.439  1.00 10.93 ?  757  CYS   B C   1 
ATOM   5402 O  O   . CYS   B 1 316 ? 54.637 6.402   11.131  1.00 11.15 ?  757  CYS   B O   1 
ATOM   5403 C  CB  . CYS   B 1 316 ? 52.943 5.638   13.822  1.00 10.84 ?  757  CYS   B CB  1 
ATOM   5404 S  SG  . CYS   B 1 316 ? 52.297 6.271   15.382  1.00 11.63 ?  757  CYS   B SG  1 
ATOM   5405 N  N   . THR   B 1 317 ? 52.992 4.918   10.780  1.00 10.87 ?  758  THR   B N   1 
ATOM   5406 C  CA  . THR   B 1 317 ? 53.686 4.361   9.617   1.00 10.87 ?  758  THR   B CA  1 
ATOM   5407 C  C   . THR   B 1 317 ? 53.802 5.387   8.493   1.00 11.27 ?  758  THR   B C   1 
ATOM   5408 O  O   . THR   B 1 317 ? 54.824 5.454   7.798   1.00 11.88 ?  758  THR   B O   1 
ATOM   5409 C  CB  . THR   B 1 317 ? 52.980 3.095   9.131   1.00 11.33 ?  758  THR   B CB  1 
ATOM   5410 O  OG1 . THR   B 1 317 ? 52.885 2.169   10.220  1.00 11.89 ?  758  THR   B OG1 1 
ATOM   5411 C  CG2 . THR   B 1 317 ? 53.758 2.454   7.975   1.00 10.96 ?  758  THR   B CG2 1 
ATOM   5412 N  N   . SER   B 1 318 ? 52.754 6.184   8.287   1.00 10.40 ?  759  SER   B N   1 
ATOM   5413 C  CA  . SER   B 1 318 ? 52.811 7.250   7.295   1.00 11.64 ?  759  SER   B CA  1 
ATOM   5414 C  C   . SER   B 1 318 ? 53.974 8.192   7.577   1.00 13.19 ?  759  SER   B C   1 
ATOM   5415 O  O   . SER   B 1 318 ? 54.634 8.665   6.643   1.00 14.08 ?  759  SER   B O   1 
ATOM   5416 C  CB  . SER   B 1 318 ? 51.479 7.995   7.279   1.00 15.25 ?  759  SER   B CB  1 
ATOM   5417 O  OG  . SER   B 1 318 ? 51.556 9.186   6.521   1.00 19.37 ?  759  SER   B OG  1 
ATOM   5418 N  N   . MET   B 1 319 ? 54.263 8.443   8.864   1.00 12.19 ?  760  MET   B N   1 
ATOM   5419 C  CA  . MET   B 1 319 ? 55.412 9.267   9.217   1.00 12.73 ?  760  MET   B CA  1 
ATOM   5420 C  C   . MET   B 1 319 ? 56.717 8.550   8.905   1.00 12.92 ?  760  MET   B C   1 
ATOM   5421 O  O   . MET   B 1 319 ? 57.642 9.154   8.351   1.00 14.50 ?  760  MET   B O   1 
ATOM   5422 C  CB  . MET   B 1 319 ? 55.363 9.654   10.698  1.00 12.90 ?  760  MET   B CB  1 
ATOM   5423 C  CG  . MET   B 1 319 ? 54.162 10.504  11.068  1.00 13.15 ?  760  MET   B CG  1 
ATOM   5424 S  SD  . MET   B 1 319 ? 54.060 12.085  10.198  1.00 15.16 ?  760  MET   B SD  1 
ATOM   5425 C  CE  . MET   B 1 319 ? 52.848 11.717  8.927   1.00 15.70 ?  760  MET   B CE  1 
ATOM   5426 N  N   . LEU   B 1 320 ? 56.807 7.256   9.241   1.00 11.41 ?  761  LEU   B N   1 
ATOM   5427 C  CA  . LEU   B 1 320 ? 58.005 6.489   8.906   1.00 13.02 ?  761  LEU   B CA  1 
ATOM   5428 C  C   . LEU   B 1 320 ? 58.271 6.507   7.404   1.00 13.85 ?  761  LEU   B C   1 
ATOM   5429 O  O   . LEU   B 1 320 ? 59.435 6.518   6.973   1.00 12.95 ?  761  LEU   B O   1 
ATOM   5430 C  CB  . LEU   B 1 320 ? 57.868 5.045   9.393   1.00 13.41 ?  761  LEU   B CB  1 
ATOM   5431 C  CG  . LEU   B 1 320 ? 57.798 4.821   10.905  1.00 12.89 ?  761  LEU   B CG  1 
ATOM   5432 C  CD1 . LEU   B 1 320 ? 57.826 3.328   11.155  1.00 13.88 ?  761  LEU   B CD1 1 
ATOM   5433 C  CD2 . LEU   B 1 320 ? 58.949 5.508   11.612  1.00 14.76 ?  761  LEU   B CD2 1 
ATOM   5434 N  N   . LEU   B 1 321 ? 57.210 6.519   6.598   1.00 11.34 ?  762  LEU   B N   1 
ATOM   5435 C  CA  . LEU   B 1 321 ? 57.346 6.549   5.145   1.00 11.56 ?  762  LEU   B CA  1 
ATOM   5436 C  C   . LEU   B 1 321 ? 57.755 7.918   4.615   1.00 14.33 ?  762  LEU   B C   1 
ATOM   5437 O  O   . LEU   B 1 321 ? 58.005 8.046   3.407   1.00 16.51 ?  762  LEU   B O   1 
ATOM   5438 C  CB  . LEU   B 1 321 ? 56.031 6.085   4.507   1.00 11.57 ?  762  LEU   B CB  1 
ATOM   5439 C  CG  . LEU   B 1 321 ? 55.759 4.587   4.600   1.00 12.42 ?  762  LEU   B CG  1 
ATOM   5440 C  CD1 . LEU   B 1 321 ? 54.281 4.284   4.376   1.00 14.13 ?  762  LEU   B CD1 1 
ATOM   5441 C  CD2 . LEU   B 1 321 ? 56.632 3.842   3.593   1.00 13.69 ?  762  LEU   B CD2 1 
ATOM   5442 N  N   . GLY   B 1 322 ? 57.844 8.928   5.474   1.00 14.76 ?  763  GLY   B N   1 
ATOM   5443 C  CA  . GLY   B 1 322 ? 58.302 10.245  5.091   1.00 15.47 ?  763  GLY   B CA  1 
ATOM   5444 C  C   . GLY   B 1 322 ? 57.219 11.262  4.807   1.00 17.45 ?  763  GLY   B C   1 
ATOM   5445 O  O   . GLY   B 1 322 ? 57.538 12.360  4.339   1.00 19.48 ?  763  GLY   B O   1 
ATOM   5446 N  N   . ASP   B 1 323 ? 55.952 10.942  5.067   1.00 15.98 ?  764  ASP   B N   1 
ATOM   5447 C  CA  . ASP   B 1 323 ? 54.889 11.908  4.822   1.00 16.26 ?  764  ASP   B CA  1 
ATOM   5448 C  C   . ASP   B 1 323 ? 54.955 13.054  5.829   1.00 18.95 ?  764  ASP   B C   1 
ATOM   5449 O  O   . ASP   B 1 323 ? 55.474 12.911  6.939   1.00 17.46 ?  764  ASP   B O   1 
ATOM   5450 C  CB  . ASP   B 1 323 ? 53.518 11.229  4.870   1.00 18.39 ?  764  ASP   B CB  1 
ATOM   5451 C  CG  . ASP   B 1 323 ? 53.360 10.158  3.806   1.00 19.20 ?  764  ASP   B CG  1 
ATOM   5452 O  OD1 . ASP   B 1 323 ? 54.137 10.185  2.827   1.00 19.27 ?  764  ASP   B OD1 1 
ATOM   5453 O  OD2 . ASP   B 1 323 ? 52.471 9.291   3.938   1.00 20.57 -1 764  ASP   B OD2 1 
ATOM   5454 N  N   . SER   B 1 324 ? 54.436 14.207  5.420   1.00 21.18 ?  765  SER   B N   1 
ATOM   5455 C  CA  . SER   B 1 324 ? 54.482 15.381  6.279   1.00 22.64 ?  765  SER   B CA  1 
ATOM   5456 C  C   . SER   B 1 324 ? 53.519 15.202  7.451   1.00 20.85 ?  765  SER   B C   1 
ATOM   5457 O  O   . SER   B 1 324 ? 52.419 14.673  7.273   1.00 21.72 ?  765  SER   B O   1 
ATOM   5458 C  CB  . SER   B 1 324 ? 54.091 16.623  5.483   1.00 22.58 ?  765  SER   B CB  1 
ATOM   5459 O  OG  . SER   B 1 324 ? 52.719 16.602  5.129   0.34 22.31 ?  765  SER   B OG  1 
ATOM   5460 N  N   . PRO   B 1 325 ? 53.905 15.618  8.656   1.00 20.65 ?  766  PRO   B N   1 
ATOM   5461 C  CA  . PRO   B 1 325 ? 53.007 15.492  9.810   1.00 20.85 ?  766  PRO   B CA  1 
ATOM   5462 C  C   . PRO   B 1 325 ? 51.721 16.268  9.590   1.00 21.26 ?  766  PRO   B C   1 
ATOM   5463 O  O   . PRO   B 1 325 ? 51.753 17.442  9.187   1.00 22.21 ?  766  PRO   B O   1 
ATOM   5464 C  CB  . PRO   B 1 325 ? 53.826 16.101  10.959  1.00 21.53 ?  766  PRO   B CB  1 
ATOM   5465 C  CG  . PRO   B 1 325 ? 55.248 15.947  10.532  1.00 21.93 ?  766  PRO   B CG  1 
ATOM   5466 C  CD  . PRO   B 1 325 ? 55.235 16.120  9.041   1.00 22.71 ?  766  PRO   B CD  1 
ATOM   5467 N  N   . PRO   B 1 326 ? 50.570 15.650  9.838   1.00 19.42 ?  767  PRO   B N   1 
ATOM   5468 C  CA  . PRO   B 1 326 ? 49.309 16.388  9.739   1.00 18.37 ?  767  PRO   B CA  1 
ATOM   5469 C  C   . PRO   B 1 326 ? 49.194 17.411  10.853  1.00 20.55 ?  767  PRO   B C   1 
ATOM   5470 O  O   . PRO   B 1 326 ? 49.780 17.264  11.930  1.00 20.44 ?  767  PRO   B O   1 
ATOM   5471 C  CB  . PRO   B 1 326 ? 48.248 15.294  9.895   1.00 20.46 ?  767  PRO   B CB  1 
ATOM   5472 C  CG  . PRO   B 1 326 ? 48.939 14.230  10.695  1.00 23.00 ?  767  PRO   B CG  1 
ATOM   5473 C  CD  . PRO   B 1 326 ? 50.354 14.239  10.201  1.00 22.01 ?  767  PRO   B CD  1 
ATOM   5474 N  N   . SER   B 1 327 ? 48.422 18.457  10.580  1.00 18.87 ?  768  SER   B N   1 
ATOM   5475 C  CA  . SER   B 1 327 ? 48.190 19.503  11.559  1.00 23.16 ?  768  SER   B CA  1 
ATOM   5476 C  C   . SER   B 1 327 ? 47.470 18.929  12.768  1.00 20.96 ?  768  SER   B C   1 
ATOM   5477 O  O   . SER   B 1 327 ? 46.594 18.070  12.640  1.00 21.05 ?  768  SER   B O   1 
ATOM   5478 C  CB  . SER   B 1 327 ? 47.311 20.591  10.936  1.00 28.36 ?  768  SER   B CB  1 
ATOM   5479 O  OG  . SER   B 1 327 ? 48.032 21.367  9.995   1.00 32.85 ?  768  SER   B OG  1 
ATOM   5480 N  N   . LEU   B 1 328 ? 47.847 19.404  13.947  1.00 21.05 ?  769  LEU   B N   1 
ATOM   5481 C  CA  . LEU   B 1 328 ? 47.156 19.010  15.159  1.00 21.32 ?  769  LEU   B CA  1 
ATOM   5482 C  C   . LEU   B 1 328 ? 45.861 19.803  15.297  1.00 24.01 ?  769  LEU   B C   1 
ATOM   5483 O  O   . LEU   B 1 328 ? 45.716 20.899  14.749  1.00 22.91 ?  769  LEU   B O   1 
ATOM   5484 C  CB  . LEU   B 1 328 ? 48.044 19.270  16.377  1.00 19.91 ?  769  LEU   B CB  1 
ATOM   5485 C  CG  . LEU   B 1 328 ? 49.310 18.416  16.475  1.00 19.35 ?  769  LEU   B CG  1 
ATOM   5486 C  CD1 . LEU   B 1 328 ? 50.195 18.875  17.628  1.00 22.73 ?  769  LEU   B CD1 1 
ATOM   5487 C  CD2 . LEU   B 1 328 ? 48.949 16.942  16.608  1.00 17.06 ?  769  LEU   B CD2 1 
ATOM   5488 N  N   . ASP   B 1 329 ? 44.906 19.228  16.030  1.00 25.04 ?  770  ASP   B N   1 
ATOM   5489 C  CA  . ASP   B 1 329 ? 43.718 19.974  16.415  1.00 28.73 ?  770  ASP   B CA  1 
ATOM   5490 C  C   . ASP   B 1 329 ? 44.119 21.112  17.353  1.00 28.26 ?  770  ASP   B C   1 
ATOM   5491 O  O   . ASP   B 1 329 ? 45.274 21.225  17.784  1.00 27.89 ?  770  ASP   B O   1 
ATOM   5492 C  CB  . ASP   B 1 329 ? 42.705 19.060  17.111  1.00 33.92 ?  770  ASP   B CB  1 
ATOM   5493 C  CG  . ASP   B 1 329 ? 42.102 18.014  16.173  1.00 39.40 ?  770  ASP   B CG  1 
ATOM   5494 O  OD1 . ASP   B 1 329 ? 42.112 18.227  14.938  1.00 40.65 -1 770  ASP   B OD1 1 
ATOM   5495 O  OD2 . ASP   B 1 329 ? 41.611 16.977  16.680  1.00 40.55 ?  770  ASP   B OD2 1 
ATOM   5496 N  N   . HIS   B 1 330 ? 43.152 21.972  17.665  1.00 26.88 ?  771  HIS   B N   1 
ATOM   5497 C  CA  . HIS   B 1 330 ? 43.417 23.048  18.610  1.00 27.23 ?  771  HIS   B CA  1 
ATOM   5498 C  C   . HIS   B 1 330 ? 43.937 22.467  19.918  1.00 26.83 ?  771  HIS   B C   1 
ATOM   5499 O  O   . HIS   B 1 330 ? 43.366 21.516  20.462  1.00 25.49 ?  771  HIS   B O   1 
ATOM   5500 C  CB  . HIS   B 1 330 ? 42.144 23.851  18.878  1.00 29.24 ?  771  HIS   B CB  1 
ATOM   5501 C  CG  . HIS   B 1 330 ? 42.333 24.958  19.869  1.00 32.35 ?  771  HIS   B CG  1 
ATOM   5502 N  ND1 . HIS   B 1 330 ? 41.975 24.841  21.196  1.00 35.28 ?  771  HIS   B ND1 1 
ATOM   5503 C  CD2 . HIS   B 1 330 ? 42.857 26.199  19.730  1.00 34.08 ?  771  HIS   B CD2 1 
ATOM   5504 C  CE1 . HIS   B 1 330 ? 42.265 25.964  21.830  1.00 34.94 ?  771  HIS   B CE1 1 
ATOM   5505 N  NE2 . HIS   B 1 330 ? 42.799 26.806  20.963  1.00 35.25 ?  771  HIS   B NE2 1 
ATOM   5506 N  N   . LEU   B 1 331 ? 45.038 23.022  20.406  1.00 26.71 ?  772  LEU   B N   1 
ATOM   5507 C  CA  . LEU   B 1 331 ? 45.647 22.555  21.644  1.00 28.29 ?  772  LEU   B CA  1 
ATOM   5508 C  C   . LEU   B 1 331 ? 45.010 23.284  22.821  1.00 30.31 ?  772  LEU   B C   1 
ATOM   5509 O  O   . LEU   B 1 331 ? 45.094 24.514  22.918  1.00 32.37 ?  772  LEU   B O   1 
ATOM   5510 C  CB  . LEU   B 1 331 ? 47.157 22.790  21.622  1.00 27.52 ?  772  LEU   B CB  1 
ATOM   5511 C  CG  . LEU   B 1 331 ? 47.977 22.000  20.598  1.00 28.72 ?  772  LEU   B CG  1 
ATOM   5512 C  CD1 . LEU   B 1 331 ? 49.433 22.447  20.625  1.00 30.19 ?  772  LEU   B CD1 1 
ATOM   5513 C  CD2 . LEU   B 1 331 ? 47.875 20.503  20.855  1.00 26.00 ?  772  LEU   B CD2 1 
ATOM   5514 N  N   . THR   B 1 332 ? 44.361 22.531  23.705  1.00 28.97 ?  773  THR   B N   1 
ATOM   5515 C  CA  . THR   B 1 332 ? 43.911 23.115  24.954  1.00 29.06 ?  773  THR   B CA  1 
ATOM   5516 C  C   . THR   B 1 332 ? 45.133 23.528  25.774  1.00 28.57 ?  773  THR   B C   1 
ATOM   5517 O  O   . THR   B 1 332 ? 46.212 22.945  25.628  1.00 26.13 ?  773  THR   B O   1 
ATOM   5518 C  CB  . THR   B 1 332 ? 43.067 22.107  25.734  1.00 30.37 ?  773  THR   B CB  1 
ATOM   5519 O  OG1 . THR   B 1 332 ? 43.724 20.834  25.752  1.00 32.22 ?  773  THR   B OG1 1 
ATOM   5520 C  CG2 . THR   B 1 332 ? 41.705 21.947  25.079  1.00 28.53 ?  773  THR   B CG2 1 
ATOM   5521 N  N   . PRO   B 1 333 ? 45.004 24.553  26.614  1.00 29.32 ?  774  PRO   B N   1 
ATOM   5522 C  CA  . PRO   B 1 333 ? 46.153 24.995  27.413  1.00 28.89 ?  774  PRO   B CA  1 
ATOM   5523 C  C   . PRO   B 1 333 ? 46.735 23.842  28.220  1.00 26.43 ?  774  PRO   B C   1 
ATOM   5524 O  O   . PRO   B 1 333 ? 46.004 23.025  28.787  1.00 25.95 ?  774  PRO   B O   1 
ATOM   5525 C  CB  . PRO   B 1 333 ? 45.553 26.071  28.324  1.00 31.42 ?  774  PRO   B CB  1 
ATOM   5526 C  CG  . PRO   B 1 333 ? 44.383 26.590  27.552  1.00 31.20 ?  774  PRO   B CG  1 
ATOM   5527 C  CD  . PRO   B 1 333 ? 43.817 25.397  26.837  1.00 29.51 ?  774  PRO   B CD  1 
ATOM   5528 N  N   . LEU   B 1 334 ? 48.065 23.777  28.251  1.00 25.31 ?  775  LEU   B N   1 
ATOM   5529 C  CA  . LEU   B 1 334 ? 48.766 22.721  28.974  1.00 24.33 ?  775  LEU   B CA  1 
ATOM   5530 C  C   . LEU   B 1 334 ? 48.239 22.609  30.399  1.00 23.40 ?  775  LEU   B C   1 
ATOM   5531 O  O   . LEU   B 1 334 ? 48.199 23.597  31.139  1.00 23.95 ?  775  LEU   B O   1 
ATOM   5532 C  CB  . LEU   B 1 334 ? 50.257 23.048  28.995  1.00 25.18 ?  775  LEU   B CB  1 
ATOM   5533 C  CG  . LEU   B 1 334 ? 51.180 21.995  29.597  1.00 26.12 ?  775  LEU   B CG  1 
ATOM   5534 C  CD1 . LEU   B 1 334 ? 50.978 20.660  28.893  1.00 27.51 ?  775  LEU   B CD1 1 
ATOM   5535 C  CD2 . LEU   B 1 334 ? 52.634 22.459  29.520  1.00 25.75 ?  775  LEU   B CD2 1 
ATOM   5536 N  N   . LYS   B 1 335 ? 47.810 21.404  30.773  1.00 21.86 ?  776  LYS   B N   1 
ATOM   5537 C  CA  . LYS   B 1 335 ? 47.225 21.196  32.093  1.00 18.96 ?  776  LYS   B CA  1 
ATOM   5538 C  C   . LYS   B 1 335 ? 48.264 21.396  33.192  1.00 20.13 ?  776  LYS   B C   1 
ATOM   5539 O  O   . LYS   B 1 335 ? 49.411 20.954  33.077  1.00 18.77 ?  776  LYS   B O   1 
ATOM   5540 C  CB  . LYS   B 1 335 ? 46.611 19.798  32.182  1.00 18.46 ?  776  LYS   B CB  1 
ATOM   5541 C  CG  . LYS   B 1 335 ? 45.217 19.693  31.543  1.00 19.04 ?  776  LYS   B CG  1 
ATOM   5542 C  CD  . LYS   B 1 335 ? 44.831 18.245  31.287  1.00 21.06 ?  776  LYS   B CD  1 
ATOM   5543 C  CE  . LYS   B 1 335 ? 43.413 18.115  30.746  1.00 21.89 ?  776  LYS   B CE  1 
ATOM   5544 N  NZ  . LYS   B 1 335 ? 43.156 18.992  29.567  1.00 19.68 ?  776  LYS   B NZ  1 
ATOM   5545 N  N   . THR   B 1 336 ? 47.844 22.056  34.279  1.00 20.24 ?  777  THR   B N   1 
ATOM   5546 C  CA  . THR   B 1 336 ? 48.782 22.430  35.335  1.00 21.63 ?  777  THR   B CA  1 
ATOM   5547 C  C   . THR   B 1 336 ? 49.435 21.205  35.968  1.00 19.00 ?  777  THR   B C   1 
ATOM   5548 O  O   . THR   B 1 336 ? 50.647 21.201  36.224  1.00 18.70 ?  777  THR   B O   1 
ATOM   5549 C  CB  . THR   B 1 336 ? 48.068 23.286  36.388  1.00 23.31 ?  777  THR   B CB  1 
ATOM   5550 O  OG1 . THR   B 1 336 ? 47.761 24.572  35.832  1.00 22.45 ?  777  THR   B OG1 1 
ATOM   5551 C  CG2 . THR   B 1 336 ? 48.938 23.472  37.634  1.00 25.74 ?  777  THR   B CG2 1 
ATOM   5552 N  N   . SER   B 1 337 ? 48.656 20.150  36.224  1.00 17.73 ?  778  SER   B N   1 
ATOM   5553 C  CA  . SER   B 1 337 ? 49.255 18.954  36.810  1.00 17.48 ?  778  SER   B CA  1 
ATOM   5554 C  C   . SER   B 1 337 ? 50.284 18.328  35.877  1.00 15.55 ?  778  SER   B C   1 
ATOM   5555 O  O   . SER   B 1 337 ? 51.246 17.711  36.349  1.00 15.59 ?  778  SER   B O   1 
ATOM   5556 C  CB  . SER   B 1 337 ? 48.187 17.942  37.224  1.00 20.97 ?  778  SER   B CB  1 
ATOM   5557 O  OG  . SER   B 1 337 ? 47.612 17.326  36.090  1.00 23.48 ?  778  SER   B OG  1 
ATOM   5558 N  N   . ALA   B 1 338 ? 50.120 18.505  34.561  1.00 15.52 ?  779  ALA   B N   1 
ATOM   5559 C  CA  . ALA   B 1 338 ? 51.125 18.015  33.622  1.00 15.42 ?  779  ALA   B CA  1 
ATOM   5560 C  C   . ALA   B 1 338 ? 52.412 18.821  33.720  1.00 14.86 ?  779  ALA   B C   1 
ATOM   5561 O  O   . ALA   B 1 338 ? 53.511 18.258  33.655  1.00 14.61 ?  779  ALA   B O   1 
ATOM   5562 C  CB  . ALA   B 1 338 ? 50.578 18.062  32.199  1.00 15.76 ?  779  ALA   B CB  1 
ATOM   5563 N  N   . THR   B 1 339 ? 52.299 20.144  33.866  1.00 14.03 ?  780  THR   B N   1 
ATOM   5564 C  CA  . THR   B 1 339 ? 53.485 20.955  34.119  1.00 16.04 ?  780  THR   B CA  1 
ATOM   5565 C  C   . THR   B 1 339 ? 54.170 20.523  35.415  1.00 15.45 ?  780  THR   B C   1 
ATOM   5566 O  O   . THR   B 1 339 ? 55.403 20.441  35.478  1.00 14.93 ?  780  THR   B O   1 
ATOM   5567 C  CB  . THR   B 1 339 ? 53.093 22.435  34.140  1.00 18.24 ?  780  THR   B CB  1 
ATOM   5568 O  OG1 . THR   B 1 339 ? 52.844 22.874  32.796  1.00 20.85 ?  780  THR   B OG1 1 
ATOM   5569 C  CG2 . THR   B 1 339 ? 54.182 23.300  34.752  1.00 21.25 ?  780  THR   B CG2 1 
ATOM   5570 N  N   . VAL   B 1 340 ? 53.388 20.221  36.456  1.00 15.51 ?  781  VAL   B N   1 
ATOM   5571 C  CA  . VAL   B 1 340 ? 53.969 19.751  37.715  1.00 14.85 ?  781  VAL   B CA  1 
ATOM   5572 C  C   . VAL   B 1 340 ? 54.745 18.453  37.501  1.00 13.74 ?  781  VAL   B C   1 
ATOM   5573 O  O   . VAL   B 1 340 ? 55.886 18.310  37.953  1.00 14.44 ?  781  VAL   B O   1 
ATOM   5574 C  CB  . VAL   B 1 340 ? 52.880 19.609  38.792  1.00 15.59 ?  781  VAL   B CB  1 
ATOM   5575 C  CG1 . VAL   B 1 340 ? 53.441 18.930  40.038  1.00 15.87 ?  781  VAL   B CG1 1 
ATOM   5576 C  CG2 . VAL   B 1 340 ? 52.302 20.990  39.126  1.00 17.24 ?  781  VAL   B CG2 1 
ATOM   5577 N  N   . SER   B 1 341 ? 54.139 17.490  36.793  1.00 13.10 ?  782  SER   B N   1 
ATOM   5578 C  CA  . SER   B 1 341 ? 54.832 16.239  36.485  1.00 13.34 ?  782  SER   B CA  1 
ATOM   5579 C  C   . SER   B 1 341 ? 56.124 16.497  35.726  1.00 12.00 ?  782  SER   B C   1 
ATOM   5580 O  O   . SER   B 1 341 ? 57.177 15.957  36.081  1.00 13.10 ?  782  SER   B O   1 
ATOM   5581 C  CB  . SER   B 1 341 ? 53.929 15.316  35.668  1.00 14.07 ?  782  SER   B CB  1 
ATOM   5582 O  OG  . SER   B 1 341 ? 52.838 14.822  36.434  1.00 16.25 ?  782  SER   B OG  1 
ATOM   5583 N  N   . ILE   B 1 342 ? 56.060 17.322  34.673  1.00 13.36 ?  783  ILE   B N   1 
ATOM   5584 C  CA  . ILE   B 1 342 ? 57.245 17.596  33.865  1.00 11.66 ?  783  ILE   B CA  1 
ATOM   5585 C  C   . ILE   B 1 342 ? 58.346 18.219  34.709  1.00 10.86 ?  783  ILE   B C   1 
ATOM   5586 O  O   . ILE   B 1 342 ? 59.516 17.839  34.599  1.00 12.90 ?  783  ILE   B O   1 
ATOM   5587 C  CB  . ILE   B 1 342 ? 56.894 18.464  32.644  1.00 12.58 ?  783  ILE   B CB  1 
ATOM   5588 C  CG1 . ILE   B 1 342 ? 56.032 17.651  31.675  1.00 12.30 ?  783  ILE   B CG1 1 
ATOM   5589 C  CG2 . ILE   B 1 342 ? 58.183 18.985  31.974  1.00 13.22 ?  783  ILE   B CG2 1 
ATOM   5590 C  CD1 . ILE   B 1 342 ? 55.406 18.448  30.549  1.00 13.59 ?  783  ILE   B CD1 1 
ATOM   5591 N  N   . ASN   B 1 343 ? 57.998 19.193  35.555  1.00 13.55 ?  784  ASN   B N   1 
ATOM   5592 C  CA  . ASN   B 1 343 ? 59.010 19.816  36.403  1.00 13.63 ?  784  ASN   B CA  1 
ATOM   5593 C  C   . ASN   B 1 343 ? 59.597 18.832  37.415  1.00 13.19 ?  784  ASN   B C   1 
ATOM   5594 O  O   . ASN   B 1 343 ? 60.787 18.925  37.738  1.00 14.22 ?  784  ASN   B O   1 
ATOM   5595 C  CB  . ASN   B 1 343 ? 58.434 21.041  37.112  1.00 18.67 ?  784  ASN   B CB  1 
ATOM   5596 C  CG  . ASN   B 1 343 ? 58.135 22.177  36.153  1.00 21.47 ?  784  ASN   B CG  1 
ATOM   5597 O  OD1 . ASN   B 1 343 ? 58.703 22.249  35.063  1.00 24.27 ?  784  ASN   B OD1 1 
ATOM   5598 N  ND2 . ASN   B 1 343 ? 57.241 23.074  36.556  1.00 23.89 ?  784  ASN   B ND2 1 
ATOM   5599 N  N   . ASN   B 1 344 ? 58.792 17.893  37.923  1.00 13.86 ?  785  ASN   B N   1 
ATOM   5600 C  CA  . ASN   B 1 344 ? 59.320 16.866  38.824  1.00 14.40 ?  785  ASN   B CA  1 
ATOM   5601 C  C   . ASN   B 1 344 ? 60.348 15.981  38.122  1.00 14.97 ?  785  ASN   B C   1 
ATOM   5602 O  O   . ASN   B 1 344 ? 61.409 15.681  38.683  1.00 16.04 ?  785  ASN   B O   1 
ATOM   5603 C  CB  . ASN   B 1 344 ? 58.180 16.026  39.411  1.00 14.16 ?  785  ASN   B CB  1 
ATOM   5604 C  CG  . ASN   B 1 344 ? 57.426 16.750  40.518  1.00 17.63 ?  785  ASN   B CG  1 
ATOM   5605 O  OD1 . ASN   B 1 344 ? 58.013 17.528  41.266  1.00 18.66 ?  785  ASN   B OD1 1 
ATOM   5606 N  ND2 . ASN   B 1 344 ? 56.130 16.482  40.635  1.00 18.72 ?  785  ASN   B ND2 1 
ATOM   5607 N  N   . VAL   B 1 345 ? 60.064 15.562  36.886  1.00 12.55 ?  786  VAL   B N   1 
ATOM   5608 C  CA  . VAL   B 1 345 ? 61.031 14.751  36.147  1.00 12.38 ?  786  VAL   B CA  1 
ATOM   5609 C  C   . VAL   B 1 345 ? 62.291 15.554  35.867  1.00 13.43 ?  786  VAL   B C   1 
ATOM   5610 O  O   . VAL   B 1 345 ? 63.411 15.026  35.944  1.00 13.07 ?  786  VAL   B O   1 
ATOM   5611 C  CB  . VAL   B 1 345 ? 60.417 14.201  34.846  1.00 12.83 ?  786  VAL   B CB  1 
ATOM   5612 C  CG1 . VAL   B 1 345 ? 61.411 13.277  34.145  1.00 15.11 ?  786  VAL   B CG1 1 
ATOM   5613 C  CG2 . VAL   B 1 345 ? 59.110 13.489  35.107  1.00 13.20 ?  786  VAL   B CG2 1 
ATOM   5614 N  N   . LEU   B 1 346 ? 62.127 16.833  35.503  1.00 13.01 ?  787  LEU   B N   1 
ATOM   5615 C  CA  . LEU   B 1 346 ? 63.278 17.687  35.234  1.00 16.12 ?  787  LEU   B CA  1 
ATOM   5616 C  C   . LEU   B 1 346 ? 64.181 17.780  36.454  1.00 16.01 ?  787  LEU   B C   1 
ATOM   5617 O  O   . LEU   B 1 346 ? 65.410 17.696  36.337  1.00 17.45 ?  787  LEU   B O   1 
ATOM   5618 C  CB  . LEU   B 1 346 ? 62.803 19.082  34.819  1.00 16.57 ?  787  LEU   B CB  1 
ATOM   5619 C  CG  . LEU   B 1 346 ? 62.469 19.273  33.339  1.00 19.40 ?  787  LEU   B CG  1 
ATOM   5620 C  CD1 . LEU   B 1 346 ? 61.674 20.551  33.130  1.00 22.34 ?  787  LEU   B CD1 1 
ATOM   5621 C  CD2 . LEU   B 1 346 ? 63.745 19.309  32.535  1.00 19.81 ?  787  LEU   B CD2 1 
ATOM   5622 N  N   . ARG   B 1 347 ? 63.584 17.956  37.631  1.00 15.61 ?  788  ARG   B N   1 
ATOM   5623 C  CA  . ARG   B 1 347 ? 64.369 18.026  38.858  1.00 16.55 ?  788  ARG   B CA  1 
ATOM   5624 C  C   . ARG   B 1 347 ? 65.097 16.710  39.110  1.00 16.42 ?  788  ARG   B C   1 
ATOM   5625 O  O   . ARG   B 1 347 ? 66.270 16.700  39.511  1.00 17.33 ?  788  ARG   B O   1 
ATOM   5626 C  CB  . ARG   B 1 347 ? 63.437 18.367  40.026  1.00 20.45 ?  788  ARG   B CB  1 
ATOM   5627 C  CG  . ARG   B 1 347 ? 64.126 18.607  41.351  1.00 27.57 ?  788  ARG   B CG  1 
ATOM   5628 C  CD  . ARG   B 1 347 ? 63.194 19.297  42.348  1.00 33.15 ?  788  ARG   B CD  1 
ATOM   5629 N  NE  . ARG   B 1 347 ? 61.800 18.876  42.212  1.00 36.53 ?  788  ARG   B NE  1 
ATOM   5630 C  CZ  . ARG   B 1 347 ? 61.285 17.793  42.790  1.00 38.33 ?  788  ARG   B CZ  1 
ATOM   5631 N  NH1 . ARG   B 1 347 ? 62.051 17.004  43.534  1.00 40.48 ?  788  ARG   B NH1 1 
ATOM   5632 N  NH2 . ARG   B 1 347 ? 60.007 17.488  42.613  1.00 37.32 ?  788  ARG   B NH2 1 
ATOM   5633 N  N   . ALA   B 1 348 ? 64.427 15.589  38.846  1.00 14.99 ?  789  ALA   B N   1 
ATOM   5634 C  CA  . ALA   B 1 348 ? 65.021 14.280  39.095  1.00 12.94 ?  789  ALA   B CA  1 
ATOM   5635 C  C   . ALA   B 1 348 ? 66.154 13.961  38.132  1.00 14.10 ?  789  ALA   B C   1 
ATOM   5636 O  O   . ALA   B 1 348 ? 67.091 13.242  38.498  1.00 15.32 ?  789  ALA   B O   1 
ATOM   5637 C  CB  . ALA   B 1 348 ? 63.949 13.196  39.027  1.00 13.78 ?  789  ALA   B CB  1 
ATOM   5638 N  N   . HIS   B 1 349 ? 66.086 14.455  36.896  1.00 13.28 ?  790  HIS   B N   1 
ATOM   5639 C  CA  . HIS   B 1 349 ? 67.021 14.033  35.865  1.00 13.69 ?  790  HIS   B CA  1 
ATOM   5640 C  C   . HIS   B 1 349 ? 68.053 15.076  35.461  1.00 12.99 ?  790  HIS   B C   1 
ATOM   5641 O  O   . HIS   B 1 349 ? 69.039 14.714  34.809  1.00 14.87 ?  790  HIS   B O   1 
ATOM   5642 C  CB  . HIS   B 1 349 ? 66.264 13.491  34.645  1.00 12.58 ?  790  HIS   B CB  1 
ATOM   5643 C  CG  . HIS   B 1 349 ? 65.903 12.052  34.796  1.00 11.72 ?  790  HIS   B CG  1 
ATOM   5644 N  ND1 . HIS   B 1 349 ? 66.811 11.040  34.574  1.00 13.45 ?  790  HIS   B ND1 1 
ATOM   5645 C  CD2 . HIS   B 1 349 ? 64.768 11.455  35.229  1.00 11.89 ?  790  HIS   B CD2 1 
ATOM   5646 C  CE1 . HIS   B 1 349 ? 66.240 9.878   34.836  1.00 13.17 ?  790  HIS   B CE1 1 
ATOM   5647 N  NE2 . HIS   B 1 349 ? 64.998 10.102  35.227  1.00 13.40 ?  790  HIS   B NE2 1 
ATOM   5648 N  N   . ALA   B 1 350 ? 67.861 16.343  35.820  1.00 15.17 ?  791  ALA   B N   1 
ATOM   5649 C  CA  . ALA   B 1 350 ? 68.906 17.342  35.601  1.00 16.25 ?  791  ALA   B CA  1 
ATOM   5650 C  C   . ALA   B 1 350 ? 70.273 16.928  36.148  1.00 16.54 ?  791  ALA   B C   1 
ATOM   5651 O  O   . ALA   B 1 350 ? 71.283 17.240  35.495  1.00 16.85 ?  791  ALA   B O   1 
ATOM   5652 C  CB  . ALA   B 1 350 ? 68.458 18.705  36.148  1.00 16.42 ?  791  ALA   B CB  1 
ATOM   5653 N  N   . PRO   B 1 351 ? 70.389 16.237  37.288  1.00 15.46 ?  792  PRO   B N   1 
ATOM   5654 C  CA  . PRO   B 1 351 ? 71.721 15.771  37.711  1.00 17.58 ?  792  PRO   B CA  1 
ATOM   5655 C  C   . PRO   B 1 351 ? 72.400 14.845  36.716  1.00 16.65 ?  792  PRO   B C   1 
ATOM   5656 O  O   . PRO   B 1 351 ? 73.635 14.780  36.696  1.00 17.91 ?  792  PRO   B O   1 
ATOM   5657 C  CB  . PRO   B 1 351 ? 71.439 15.064  39.045  1.00 17.04 ?  792  PRO   B CB  1 
ATOM   5658 C  CG  . PRO   B 1 351 ? 70.201 15.687  39.551  1.00 16.83 ?  792  PRO   B CG  1 
ATOM   5659 C  CD  . PRO   B 1 351 ? 69.377 15.993  38.335  1.00 14.00 ?  792  PRO   B CD  1 
ATOM   5660 N  N   . PHE   B 1 352 ? 71.632 14.132  35.881  1.00 14.26 ?  793  PHE   B N   1 
ATOM   5661 C  CA  . PHE   B 1 352 ? 72.175 13.127  34.979  1.00 14.59 ?  793  PHE   B CA  1 
ATOM   5662 C  C   . PHE   B 1 352 ? 72.296 13.593  33.533  1.00 15.10 ?  793  PHE   B C   1 
ATOM   5663 O  O   . PHE   B 1 352 ? 73.095 13.029  32.779  1.00 18.89 ?  793  PHE   B O   1 
ATOM   5664 C  CB  . PHE   B 1 352 ? 71.331 11.849  35.053  1.00 15.33 ?  793  PHE   B CB  1 
ATOM   5665 C  CG  . PHE   B 1 352 ? 71.195 11.319  36.450  1.00 15.09 ?  793  PHE   B CG  1 
ATOM   5666 C  CD1 . PHE   B 1 352 ? 72.259 10.701  37.076  1.00 16.30 ?  793  PHE   B CD1 1 
ATOM   5667 C  CD2 . PHE   B 1 352 ? 70.017 11.481  37.155  1.00 15.54 ?  793  PHE   B CD2 1 
ATOM   5668 C  CE1 . PHE   B 1 352 ? 72.143 10.232  38.362  1.00 17.89 ?  793  PHE   B CE1 1 
ATOM   5669 C  CE2 . PHE   B 1 352 ? 69.884 11.009  38.432  1.00 17.49 ?  793  PHE   B CE2 1 
ATOM   5670 C  CZ  . PHE   B 1 352 ? 70.958 10.387  39.052  1.00 16.58 ?  793  PHE   B CZ  1 
ATOM   5671 N  N   . TRP   B 1 353 ? 71.547 14.612  33.126  1.00 15.94 ?  794  TRP   B N   1 
ATOM   5672 C  CA  . TRP   B 1 353 ? 71.488 15.015  31.725  1.00 15.96 ?  794  TRP   B CA  1 
ATOM   5673 C  C   . TRP   B 1 353 ? 71.736 16.511  31.653  1.00 16.52 ?  794  TRP   B C   1 
ATOM   5674 O  O   . TRP   B 1 353 ? 70.862 17.304  32.019  1.00 17.38 ?  794  TRP   B O   1 
ATOM   5675 C  CB  . TRP   B 1 353 ? 70.137 14.639  31.120  1.00 14.38 ?  794  TRP   B CB  1 
ATOM   5676 C  CG  . TRP   B 1 353 ? 69.906 13.171  31.233  1.00 13.37 ?  794  TRP   B CG  1 
ATOM   5677 C  CD1 . TRP   B 1 353 ? 69.160 12.530  32.177  1.00 13.01 ?  794  TRP   B CD1 1 
ATOM   5678 C  CD2 . TRP   B 1 353 ? 70.457 12.160  30.397  1.00 14.10 ?  794  TRP   B CD2 1 
ATOM   5679 N  NE1 . TRP   B 1 353 ? 69.197 11.173  31.964  1.00 14.49 ?  794  TRP   B NE1 1 
ATOM   5680 C  CE2 . TRP   B 1 353 ? 69.992 10.921  30.877  1.00 15.39 ?  794  TRP   B CE2 1 
ATOM   5681 C  CE3 . TRP   B 1 353 ? 71.304 12.178  29.287  1.00 16.41 ?  794  TRP   B CE3 1 
ATOM   5682 C  CZ2 . TRP   B 1 353 ? 70.343 9.712   30.279  1.00 16.09 ?  794  TRP   B CZ2 1 
ATOM   5683 C  CZ3 . TRP   B 1 353 ? 71.648 10.980  28.695  1.00 19.31 ?  794  TRP   B CZ3 1 
ATOM   5684 C  CH2 . TRP   B 1 353 ? 71.174 9.765   29.192  1.00 18.44 ?  794  TRP   B CH2 1 
ATOM   5685 N  N   . SER   B 1 354 ? 72.925 16.888  31.179  1.00 16.99 ?  795  SER   B N   1 
ATOM   5686 C  CA  A SER   B 1 354 ? 73.291 18.298  31.130  0.22 19.29 ?  795  SER   B CA  1 
ATOM   5687 C  CA  B SER   B 1 354 ? 73.291 18.299  31.131  0.78 17.71 ?  795  SER   B CA  1 
ATOM   5688 C  C   . SER   B 1 354 ? 72.349 19.108  30.251  1.00 17.71 ?  795  SER   B C   1 
ATOM   5689 O  O   . SER   B 1 354 ? 72.214 20.319  30.460  1.00 18.60 ?  795  SER   B O   1 
ATOM   5690 C  CB  A SER   B 1 354 ? 74.736 18.451  30.650  0.22 22.53 ?  795  SER   B CB  1 
ATOM   5691 C  CB  B SER   B 1 354 ? 74.735 18.466  30.650  0.78 20.05 ?  795  SER   B CB  1 
ATOM   5692 O  OG  A SER   B 1 354 ? 75.620 17.689  31.455  0.22 24.28 ?  795  SER   B OG  1 
ATOM   5693 O  OG  B SER   B 1 354 ? 74.844 18.157  29.274  0.78 20.69 ?  795  SER   B OG  1 
ATOM   5694 N  N   . SER   B 1 355 ? 71.687 18.466  29.282  1.00 16.19 ?  796  SER   B N   1 
ATOM   5695 C  CA  . SER   B 1 355 ? 70.771 19.180  28.396  1.00 17.80 ?  796  SER   B CA  1 
ATOM   5696 C  C   . SER   B 1 355 ? 69.549 19.736  29.124  1.00 19.84 ?  796  SER   B C   1 
ATOM   5697 O  O   . SER   B 1 355 ? 68.865 20.612  28.581  1.00 21.70 ?  796  SER   B O   1 
ATOM   5698 C  CB  . SER   B 1 355 ? 70.339 18.273  27.236  1.00 19.34 ?  796  SER   B CB  1 
ATOM   5699 O  OG  . SER   B 1 355 ? 69.583 17.171  27.712  1.00 21.53 ?  796  SER   B OG  1 
ATOM   5700 N  N   . LEU   B 1 356 ? 69.263 19.262  30.333  1.00 19.02 ?  797  LEU   B N   1 
ATOM   5701 C  CA  . LEU   B 1 356 ? 68.109 19.710  31.100  1.00 19.53 ?  797  LEU   B CA  1 
ATOM   5702 C  C   . LEU   B 1 356 ? 68.432 20.857  32.046  1.00 24.07 ?  797  LEU   B C   1 
ATOM   5703 O  O   . LEU   B 1 356 ? 67.549 21.287  32.795  1.00 24.77 ?  797  LEU   B O   1 
ATOM   5704 C  CB  . LEU   B 1 356 ? 67.557 18.552  31.928  1.00 18.18 ?  797  LEU   B CB  1 
ATOM   5705 C  CG  . LEU   B 1 356 ? 67.123 17.288  31.193  1.00 18.10 ?  797  LEU   B CG  1 
ATOM   5706 C  CD1 . LEU   B 1 356 ? 66.585 16.261  32.189  1.00 17.57 ?  797  LEU   B CD1 1 
ATOM   5707 C  CD2 . LEU   B 1 356 ? 66.073 17.628  30.154  1.00 19.53 ?  797  LEU   B CD2 1 
ATOM   5708 N  N   . ARG   B 1 357 ? 69.663 21.353  32.041  1.00 27.19 ?  798  ARG   B N   1 
ATOM   5709 C  CA  . ARG   B 1 357 ? 70.079 22.351  33.016  1.00 30.81 ?  798  ARG   B CA  1 
ATOM   5710 C  C   . ARG   B 1 357 ? 69.902 23.766  32.489  1.00 37.12 ?  798  ARG   B C   1 
ATOM   5711 O  O   . ARG   B 1 357 ? 69.843 23.985  31.280  1.00 37.72 ?  798  ARG   B O   1 
ATOM   5712 C  CB  . ARG   B 1 357 ? 71.533 22.113  33.424  1.00 27.93 ?  798  ARG   B CB  1 
ATOM   5713 C  CG  . ARG   B 1 357 ? 71.742 20.771  34.092  1.00 26.88 ?  798  ARG   B CG  1 
ATOM   5714 C  CD  . ARG   B 1 357 ? 73.207 20.427  34.276  1.00 26.01 ?  798  ARG   B CD  1 
ATOM   5715 N  NE  . ARG   B 1 357 ? 73.342 19.018  34.621  1.00 24.25 ?  798  ARG   B NE  1 
ATOM   5716 C  CZ  . ARG   B 1 357 ? 74.453 18.306  34.485  1.00 23.42 ?  798  ARG   B CZ  1 
ATOM   5717 N  NH1 . ARG   B 1 357 ? 75.557 18.866  34.005  1.00 20.76 ?  798  ARG   B NH1 1 
ATOM   5718 N  NH2 . ARG   B 1 357 ? 74.454 17.025  34.821  1.00 23.60 ?  798  ARG   B NH2 1 
ATOM   5719 O  OXT . ARG   B 1 357 ? 69.816 24.715  33.270  1.00 40.91 -1 798  ARG   B OXT 1 
HETATM 5720 C  C11 . A1BH8 C 2 .   ? 32.424 -3.452  -12.117 1.00 18.45 ?  801  A1BH8 A C11 1 
HETATM 5721 C  C12 . A1BH8 C 2 .   ? 32.469 -1.971  -11.727 1.00 18.83 ?  801  A1BH8 A C12 1 
HETATM 5722 C  C13 . A1BH8 C 2 .   ? 33.497 -1.160  -12.190 1.00 22.60 ?  801  A1BH8 A C13 1 
HETATM 5723 C  C14 . A1BH8 C 2 .   ? 33.499 0.173   -11.800 1.00 20.92 ?  801  A1BH8 A C14 1 
HETATM 5724 C  C02 . A1BH8 C 2 .   ? 28.024 -2.841  -6.834  1.00 20.84 ?  801  A1BH8 A C02 1 
HETATM 5725 C  C05 . A1BH8 C 2 .   ? 29.007 -3.528  -7.786  1.00 18.46 ?  801  A1BH8 A C05 1 
HETATM 5726 C  C06 . A1BH8 C 2 .   ? 30.349 -3.207  -7.724  1.00 18.45 ?  801  A1BH8 A C06 1 
HETATM 5727 C  C07 . A1BH8 C 2 .   ? 31.253 -3.790  -8.588  1.00 17.80 ?  801  A1BH8 A C07 1 
HETATM 5728 C  C08 . A1BH8 C 2 .   ? 30.814 -4.689  -9.546  1.00 16.67 ?  801  A1BH8 A C08 1 
HETATM 5729 C  C09 . A1BH8 C 2 .   ? 31.824 -5.322  -10.501 1.00 16.78 ?  801  A1BH8 A C09 1 
HETATM 5730 C  C15 . A1BH8 C 2 .   ? 32.493 0.648   -10.972 1.00 17.87 ?  801  A1BH8 A C15 1 
HETATM 5731 C  C17 . A1BH8 C 2 .   ? 31.490 -1.433  -10.903 1.00 16.64 ?  801  A1BH8 A C17 1 
HETATM 5732 C  C20 . A1BH8 C 2 .   ? 35.088 -5.813  -11.752 1.00 22.86 ?  801  A1BH8 A C20 1 
HETATM 5733 C  C21 . A1BH8 C 2 .   ? 36.573 -5.990  -11.441 1.00 25.92 ?  801  A1BH8 A C21 1 
HETATM 5734 C  C23 . A1BH8 C 2 .   ? 29.468 -5.012  -9.631  1.00 15.83 ?  801  A1BH8 A C23 1 
HETATM 5735 C  C24 . A1BH8 C 2 .   ? 28.563 -4.430  -8.750  1.00 17.16 ?  801  A1BH8 A C24 1 
HETATM 5736 N  N03 . A1BH8 C 2 .   ? 26.622 -2.739  -7.189  1.00 23.20 ?  801  A1BH8 A N03 1 
HETATM 5737 N  N10 . A1BH8 C 2 .   ? 32.767 -4.314  -10.988 1.00 16.62 ?  801  A1BH8 A N10 1 
HETATM 5738 N  N16 . A1BH8 C 2 .   ? 31.543 -0.161  -10.557 1.00 13.94 ?  801  A1BH8 A N16 1 
HETATM 5739 O  O01 . A1BH8 C 2 .   ? 28.375 -2.302  -5.858  1.00 16.10 ?  801  A1BH8 A O01 1 
HETATM 5740 O  O04 . A1BH8 C 2 .   ? 25.659 -2.095  -6.383  1.00 16.88 ?  801  A1BH8 A O04 1 
HETATM 5741 O  O19 . A1BH8 C 2 .   ? 35.144 -3.318  -10.723 1.00 22.91 ?  801  A1BH8 A O19 1 
HETATM 5742 O  O22 . A1BH8 C 2 .   ? 34.579 -4.982  -9.244  1.00 24.71 ?  801  A1BH8 A O22 1 
HETATM 5743 S  S18 . A1BH8 C 2 .   ? 34.397 -4.570  -10.632 1.00 19.26 ?  801  A1BH8 A S18 1 
HETATM 5744 ZN ZN  . ZN    D 3 .   ? 26.872 -0.530  -5.772  1.00 15.33 ?  802  ZN    A ZN  1 
HETATM 5745 K  K   . K     E 4 .   ? 7.622  1.319   -9.869  1.00 14.09 1  803  K     A K   1 
HETATM 5746 C  C11 . A1BH8 F 2 .   ? 43.227 -3.303  34.606  1.00 17.23 ?  801  A1BH8 B C11 1 
HETATM 5747 C  C12 . A1BH8 F 2 .   ? 43.130 -1.867  34.080  1.00 15.97 ?  801  A1BH8 B C12 1 
HETATM 5748 C  C13 . A1BH8 F 2 .   ? 42.013 -1.087  34.347  1.00 17.83 ?  801  A1BH8 B C13 1 
HETATM 5749 C  C14 . A1BH8 F 2 .   ? 41.976 0.197   33.830  1.00 17.08 ?  801  A1BH8 B C14 1 
HETATM 5750 C  C02 . A1BH8 F 2 .   ? 47.546 -2.804  29.167  1.00 22.33 ?  801  A1BH8 B C02 1 
HETATM 5751 C  C05 . A1BH8 F 2 .   ? 46.610 -3.482  30.172  1.00 16.81 ?  801  A1BH8 B C05 1 
HETATM 5752 C  C06 . A1BH8 F 2 .   ? 45.265 -3.139  30.189  1.00 17.59 ?  801  A1BH8 B C06 1 
HETATM 5753 C  C07 . A1BH8 F 2 .   ? 44.412 -3.713  31.121  1.00 17.57 ?  801  A1BH8 B C07 1 
HETATM 5754 C  C08 . A1BH8 F 2 .   ? 44.901 -4.617  32.050  1.00 15.98 ?  801  A1BH8 B C08 1 
HETATM 5755 C  C09 . A1BH8 F 2 .   ? 43.965 -5.248  33.084  1.00 17.94 ?  801  A1BH8 B C09 1 
HETATM 5756 C  C15 . A1BH8 F 2 .   ? 43.034 0.655   33.060  1.00 17.33 ?  801  A1BH8 B C15 1 
HETATM 5757 C  C17 . A1BH8 F 2 .   ? 44.154 -1.351  33.303  1.00 13.82 ?  801  A1BH8 B C17 1 
HETATM 5758 C  C20 . A1BH8 F 2 .   ? 40.750 -6.112  34.200  1.00 28.04 ?  801  A1BH8 B C20 1 
HETATM 5759 C  C21 . A1BH8 F 2 .   ? 41.465 -6.180  35.548  1.00 31.09 ?  801  A1BH8 B C21 1 
HETATM 5760 C  C23 . A1BH8 F 2 .   ? 46.241 -4.957  32.048  1.00 16.05 ?  801  A1BH8 B C23 1 
HETATM 5761 C  C24 . A1BH8 F 2 .   ? 47.092 -4.383  31.111  1.00 16.19 ?  801  A1BH8 B C24 1 
HETATM 5762 N  N03 . A1BH8 F 2 .   ? 48.966 -2.731  29.431  1.00 25.94 ?  801  A1BH8 B N03 1 
HETATM 5763 N  N10 . A1BH8 F 2 .   ? 42.951 -4.295  33.554  1.00 19.21 ?  801  A1BH8 B N10 1 
HETATM 5764 N  N16 . A1BH8 F 2 .   ? 44.069 -0.124  32.834  1.00 13.84 ?  801  A1BH8 B N16 1 
HETATM 5765 O  O01 . A1BH8 F 2 .   ? 47.138 -2.246  28.220  1.00 19.18 ?  801  A1BH8 B O01 1 
HETATM 5766 O  O04 . A1BH8 F 2 .   ? 49.888 -2.082  28.581  1.00 17.46 ?  801  A1BH8 B O04 1 
HETATM 5767 O  O19 . A1BH8 F 2 .   ? 40.442 -3.558  33.286  1.00 24.99 ?  801  A1BH8 B O19 1 
HETATM 5768 O  O22 . A1BH8 F 2 .   ? 41.237 -5.062  31.787  1.00 24.80 ?  801  A1BH8 B O22 1 
HETATM 5769 S  S18 . A1BH8 F 2 .   ? 41.337 -4.713  33.197  1.00 22.96 ?  801  A1BH8 B S18 1 
HETATM 5770 ZN ZN  . ZN    G 3 .   ? 48.725 -0.423  28.112  1.00 15.33 ?  802  ZN    B ZN  1 
HETATM 5771 K  K   . K     H 4 .   ? 68.065 1.682   31.888  0.80 11.72 1  803  K     B K   1 
HETATM 5772 O  O   . HOH   I 5 .   ? 30.320 -30.070 -9.020  1.00 39.36 ?  901  HOH   A O   1 
HETATM 5773 O  O   . HOH   I 5 .   ? 8.404  20.599  -4.876  1.00 44.35 ?  902  HOH   A O   1 
HETATM 5774 O  O   . HOH   I 5 .   ? 18.728 -18.473 12.093  1.00 43.11 ?  903  HOH   A O   1 
HETATM 5775 O  O   . HOH   I 5 .   ? 10.456 -25.128 -9.439  1.00 21.87 ?  904  HOH   A O   1 
HETATM 5776 O  O   . HOH   I 5 .   ? 10.022 10.180  12.040  1.00 47.19 ?  905  HOH   A O   1 
HETATM 5777 O  O   . HOH   I 5 .   ? 36.523 -23.923 -13.620 1.00 41.21 ?  906  HOH   A O   1 
HETATM 5778 O  O   . HOH   I 5 .   ? -4.230 1.677   -0.993  1.00 41.86 ?  907  HOH   A O   1 
HETATM 5779 O  O   . HOH   I 5 .   ? 38.458 9.876   -6.433  1.00 36.93 ?  908  HOH   A O   1 
HETATM 5780 O  O   . HOH   I 5 .   ? -3.529 2.671   4.520   1.00 45.21 ?  909  HOH   A O   1 
HETATM 5781 O  O   . HOH   I 5 .   ? 10.181 -4.135  -16.778 1.00 38.71 ?  910  HOH   A O   1 
HETATM 5782 O  O   . HOH   I 5 .   ? 30.403 11.411  -18.167 1.00 46.81 ?  911  HOH   A O   1 
HETATM 5783 O  O   . HOH   I 5 .   ? 23.848 -24.124 3.075   1.00 30.17 ?  912  HOH   A O   1 
HETATM 5784 O  O   . HOH   I 5 .   ? 33.152 23.008  1.776   1.00 41.61 ?  913  HOH   A O   1 
HETATM 5785 O  O   . HOH   I 5 .   ? 0.832  6.425   -14.275 1.00 28.51 ?  914  HOH   A O   1 
HETATM 5786 O  O   . HOH   I 5 .   ? 29.070 -23.147 -16.330 1.00 34.19 ?  915  HOH   A O   1 
HETATM 5787 O  O   . HOH   I 5 .   ? 2.714  -1.855  -19.743 1.00 21.15 ?  916  HOH   A O   1 
HETATM 5788 O  O   . HOH   I 5 .   ? 36.626 5.367   -6.085  1.00 38.56 ?  917  HOH   A O   1 
HETATM 5789 O  O   . HOH   I 5 .   ? -1.848 -9.072  1.351   1.00 24.08 ?  918  HOH   A O   1 
HETATM 5790 O  O   . HOH   I 5 .   ? 30.930 -21.391 1.056   1.00 20.71 ?  919  HOH   A O   1 
HETATM 5791 O  O   . HOH   I 5 .   ? 39.856 -5.737  -3.684  1.00 26.82 ?  920  HOH   A O   1 
HETATM 5792 O  O   . HOH   I 5 .   ? 5.196  -13.787 7.777   1.00 19.55 ?  921  HOH   A O   1 
HETATM 5793 O  O   . HOH   I 5 .   ? 32.215 11.989  -13.310 1.00 32.83 ?  922  HOH   A O   1 
HETATM 5794 O  O   . HOH   I 5 .   ? -0.042 12.760  -14.432 1.00 35.49 ?  923  HOH   A O   1 
HETATM 5795 O  O   . HOH   I 5 .   ? 20.032 -14.781 13.690  1.00 17.69 ?  924  HOH   A O   1 
HETATM 5796 O  O   . HOH   I 5 .   ? 1.852  -7.635  -3.936  1.00 24.54 ?  925  HOH   A O   1 
HETATM 5797 O  O   . HOH   I 5 .   ? 20.281 -18.057 -12.854 1.00 19.94 ?  926  HOH   A O   1 
HETATM 5798 O  O   . HOH   I 5 .   ? -0.953 4.414   -12.059 1.00 48.11 ?  927  HOH   A O   1 
HETATM 5799 O  O   . HOH   I 5 .   ? 20.080 -1.750  26.143  1.00 24.16 ?  928  HOH   A O   1 
HETATM 5800 O  O   . HOH   I 5 .   ? 34.418 -5.145  17.654  1.00 22.40 ?  929  HOH   A O   1 
HETATM 5801 O  O   . HOH   I 5 .   ? 20.313 -10.215 14.472  1.00 15.08 ?  930  HOH   A O   1 
HETATM 5802 O  O   . HOH   I 5 .   ? 38.207 -16.406 0.063   1.00 33.99 ?  931  HOH   A O   1 
HETATM 5803 O  O   . HOH   I 5 .   ? 23.814 7.082   -5.183  1.00 12.03 ?  932  HOH   A O   1 
HETATM 5804 O  O   . HOH   I 5 .   ? 34.440 -35.408 -3.310  1.00 42.46 ?  933  HOH   A O   1 
HETATM 5805 O  O   . HOH   I 5 .   ? 7.971  12.571  -18.714 1.00 31.17 ?  934  HOH   A O   1 
HETATM 5806 O  O   . HOH   I 5 .   ? 17.268 5.797   21.147  1.00 29.56 ?  935  HOH   A O   1 
HETATM 5807 O  O   . HOH   I 5 .   ? 36.908 -1.296  19.731  1.00 15.43 ?  936  HOH   A O   1 
HETATM 5808 O  O   . HOH   I 5 .   ? 15.773 -23.879 -0.248  1.00 28.62 ?  937  HOH   A O   1 
HETATM 5809 O  O   . HOH   I 5 .   ? 13.894 -8.734  -14.031 1.00 21.77 ?  938  HOH   A O   1 
HETATM 5810 O  O   . HOH   I 5 .   ? -1.080 -9.929  8.545   1.00 30.28 ?  939  HOH   A O   1 
HETATM 5811 O  O   . HOH   I 5 .   ? 23.873 -15.424 -17.831 1.00 29.40 ?  940  HOH   A O   1 
HETATM 5812 O  O   . HOH   I 5 .   ? 20.706 -8.570  0.468   1.00 12.18 ?  941  HOH   A O   1 
HETATM 5813 O  O   . HOH   I 5 .   ? 22.473 8.007   -22.014 1.00 23.09 ?  942  HOH   A O   1 
HETATM 5814 O  O   . HOH   I 5 .   ? 31.767 8.600   14.960  1.00 24.81 ?  943  HOH   A O   1 
HETATM 5815 O  O   . HOH   I 5 .   ? -4.835 -3.845  -1.198  1.00 43.63 ?  944  HOH   A O   1 
HETATM 5816 O  O   . HOH   I 5 .   ? 28.556 -4.495  -17.341 1.00 26.62 ?  945  HOH   A O   1 
HETATM 5817 O  O   . HOH   I 5 .   ? 26.117 5.086   -1.530  1.00 11.41 ?  946  HOH   A O   1 
HETATM 5818 O  O   . HOH   I 5 .   ? 8.680  -13.962 12.286  1.00 46.64 ?  947  HOH   A O   1 
HETATM 5819 O  O   . HOH   I 5 .   ? 10.325 0.574   -11.002 1.00 12.93 ?  948  HOH   A O   1 
HETATM 5820 O  O   . HOH   I 5 .   ? 2.822  12.732  2.815   1.00 29.47 ?  949  HOH   A O   1 
HETATM 5821 O  O   . HOH   I 5 .   ? 30.684 -13.488 -13.253 1.00 13.99 ?  950  HOH   A O   1 
HETATM 5822 O  O   . HOH   I 5 .   ? 25.526 3.929   -16.569 1.00 17.84 ?  951  HOH   A O   1 
HETATM 5823 O  O   . HOH   I 5 .   ? 29.737 20.706  -5.178  1.00 25.43 ?  952  HOH   A O   1 
HETATM 5824 O  O   . HOH   I 5 .   ? 22.786 -13.288 -16.646 1.00 19.88 ?  953  HOH   A O   1 
HETATM 5825 O  O   . HOH   I 5 .   ? 0.818  -4.269  -5.321  1.00 26.25 ?  954  HOH   A O   1 
HETATM 5826 O  O   . HOH   I 5 .   ? 19.718 6.935   -26.470 1.00 21.60 ?  955  HOH   A O   1 
HETATM 5827 O  O   . HOH   I 5 .   ? 30.872 -10.935 13.745  1.00 23.45 ?  956  HOH   A O   1 
HETATM 5828 O  O   . HOH   I 5 .   ? 17.944 -5.530  -2.900  1.00 12.60 ?  957  HOH   A O   1 
HETATM 5829 O  O   . HOH   I 5 .   ? 20.124 14.507  -21.676 1.00 45.40 ?  958  HOH   A O   1 
HETATM 5830 O  O   . HOH   I 5 .   ? 13.158 10.200  -23.932 1.00 34.41 ?  959  HOH   A O   1 
HETATM 5831 O  O   . HOH   I 5 .   ? 25.409 10.585  15.747  1.00 30.86 ?  960  HOH   A O   1 
HETATM 5832 O  O   . HOH   I 5 .   ? 34.818 -19.963 -16.537 1.00 33.18 ?  961  HOH   A O   1 
HETATM 5833 O  O   . HOH   I 5 .   ? 9.048  -12.687 8.553   1.00 17.05 ?  962  HOH   A O   1 
HETATM 5834 O  O   . HOH   I 5 .   ? 12.082 6.440   11.963  1.00 18.67 ?  963  HOH   A O   1 
HETATM 5835 O  O   . HOH   I 5 .   ? 11.722 19.646  -0.240  1.00 23.37 ?  964  HOH   A O   1 
HETATM 5836 O  O   . HOH   I 5 .   ? 12.431 -23.481 -8.398  1.00 20.11 ?  965  HOH   A O   1 
HETATM 5837 O  O   . HOH   I 5 .   ? 19.933 -25.572 1.598   1.00 46.15 ?  966  HOH   A O   1 
HETATM 5838 O  O   . HOH   I 5 .   ? 24.292 -11.424 -15.151 1.00 15.69 ?  967  HOH   A O   1 
HETATM 5839 O  O   . HOH   I 5 .   ? 26.057 -23.703 6.890   1.00 40.71 ?  968  HOH   A O   1 
HETATM 5840 O  O   . HOH   I 5 .   ? 35.643 0.525   10.529  1.00 16.32 ?  969  HOH   A O   1 
HETATM 5841 O  O   . HOH   I 5 .   ? 33.561 15.927  6.205   1.00 18.68 ?  970  HOH   A O   1 
HETATM 5842 O  O   . HOH   I 5 .   ? 10.074 -7.745  19.432  1.00 34.27 ?  971  HOH   A O   1 
HETATM 5843 O  O   . HOH   I 5 .   ? 22.672 1.097   25.570  1.00 30.19 ?  972  HOH   A O   1 
HETATM 5844 O  O   . HOH   I 5 .   ? 33.728 -18.720 -4.374  1.00 18.39 ?  973  HOH   A O   1 
HETATM 5845 O  O   . HOH   I 5 .   ? 6.287  0.715   13.382  1.00 22.39 ?  974  HOH   A O   1 
HETATM 5846 O  O   . HOH   I 5 .   ? 33.818 -16.730 4.664   1.00 25.08 ?  975  HOH   A O   1 
HETATM 5847 O  O   . HOH   I 5 .   ? 29.670 17.247  5.023   1.00 23.47 ?  976  HOH   A O   1 
HETATM 5848 O  O   . HOH   I 5 .   ? 8.339  -17.777 -9.808  1.00 27.60 ?  977  HOH   A O   1 
HETATM 5849 O  O   . HOH   I 5 .   ? 5.737  -15.470 3.456   1.00 21.38 ?  978  HOH   A O   1 
HETATM 5850 O  O   . HOH   I 5 .   ? 23.724 -4.535  -17.855 1.00 30.51 ?  979  HOH   A O   1 
HETATM 5851 O  O   . HOH   I 5 .   ? 37.511 -12.884 4.160   1.00 38.15 ?  980  HOH   A O   1 
HETATM 5852 O  O   . HOH   I 5 .   ? 7.828  -17.448 6.030   1.00 21.75 ?  981  HOH   A O   1 
HETATM 5853 O  O   . HOH   I 5 .   ? 10.981 -4.769  19.892  1.00 42.45 ?  982  HOH   A O   1 
HETATM 5854 O  O   . HOH   I 5 .   ? 22.287 19.151  13.071  1.00 22.32 ?  983  HOH   A O   1 
HETATM 5855 O  O   . HOH   I 5 .   ? 0.153  10.649  -4.867  1.00 48.18 ?  984  HOH   A O   1 
HETATM 5856 O  O   . HOH   I 5 .   ? 17.170 11.244  14.386  1.00 16.29 ?  985  HOH   A O   1 
HETATM 5857 O  O   . HOH   I 5 .   ? 35.345 5.682   11.522  1.00 20.88 ?  986  HOH   A O   1 
HETATM 5858 O  O   . HOH   I 5 .   ? 12.972 13.287  10.513  1.00 31.13 ?  987  HOH   A O   1 
HETATM 5859 O  O   . HOH   I 5 .   ? 25.672 -6.451  1.091   1.00 11.37 ?  988  HOH   A O   1 
HETATM 5860 O  O   . HOH   I 5 .   ? 18.983 10.427  21.229  1.00 31.24 ?  989  HOH   A O   1 
HETATM 5861 O  O   . HOH   I 5 .   ? 28.405 -11.288 -3.649  1.00 12.06 ?  990  HOH   A O   1 
HETATM 5862 O  O   . HOH   I 5 .   ? 31.379 -20.445 -17.694 1.00 42.91 ?  991  HOH   A O   1 
HETATM 5863 O  O   . HOH   I 5 .   ? 17.572 2.460   23.013  1.00 41.55 ?  992  HOH   A O   1 
HETATM 5864 O  O   . HOH   I 5 .   ? 37.636 -11.527 -8.776  1.00 20.05 ?  993  HOH   A O   1 
HETATM 5865 O  O   . HOH   I 5 .   ? 30.665 17.379  -4.555  1.00 22.15 ?  994  HOH   A O   1 
HETATM 5866 O  O   . HOH   I 5 .   ? 24.962 2.991   -12.197 1.00 11.46 ?  995  HOH   A O   1 
HETATM 5867 O  O   . HOH   I 5 .   ? 4.989  -16.962 -3.893  1.00 32.15 ?  996  HOH   A O   1 
HETATM 5868 O  O   . HOH   I 5 .   ? 5.764  23.817  -13.482 1.00 30.24 ?  997  HOH   A O   1 
HETATM 5869 O  O   . HOH   I 5 .   ? 7.304  2.258   -12.419 1.00 13.84 ?  998  HOH   A O   1 
HETATM 5870 O  O   . HOH   I 5 .   ? 29.442 -25.055 -14.013 1.00 20.92 ?  999  HOH   A O   1 
HETATM 5871 O  O   . HOH   I 5 .   ? 22.922 1.233   -16.166 1.00 12.85 ?  1000 HOH   A O   1 
HETATM 5872 O  O   . HOH   I 5 .   ? 16.925 -1.234  -4.960  1.00 11.50 ?  1001 HOH   A O   1 
HETATM 5873 O  O   . HOH   I 5 .   ? 12.272 -19.891 7.161   1.00 21.49 ?  1002 HOH   A O   1 
HETATM 5874 O  O   . HOH   I 5 .   ? 12.235 24.596  -13.955 1.00 31.28 ?  1003 HOH   A O   1 
HETATM 5875 O  O   . HOH   I 5 .   ? 7.256  -8.953  -7.872  1.00 18.14 ?  1004 HOH   A O   1 
HETATM 5876 O  O   . HOH   I 5 .   ? 25.459 -21.761 -3.093  1.00 15.36 ?  1005 HOH   A O   1 
HETATM 5877 O  O   . HOH   I 5 .   ? -0.882 -12.821 1.698   1.00 30.91 ?  1006 HOH   A O   1 
HETATM 5878 O  O   . HOH   I 5 .   ? 9.552  -10.286 12.840  1.00 14.78 ?  1007 HOH   A O   1 
HETATM 5879 O  O   . HOH   I 5 .   ? 32.807 2.576   0.749   1.00 12.05 ?  1008 HOH   A O   1 
HETATM 5880 O  O   . HOH   I 5 .   ? 34.485 -1.497  11.962  1.00 11.57 ?  1009 HOH   A O   1 
HETATM 5881 O  O   . HOH   I 5 .   ? 13.090 -9.425  18.006  1.00 35.34 ?  1010 HOH   A O   1 
HETATM 5882 O  O   . HOH   I 5 .   ? 0.152  4.391   -18.639 1.00 33.13 ?  1011 HOH   A O   1 
HETATM 5883 O  O   . HOH   I 5 .   ? 32.511 6.639   -3.849  1.00 12.25 ?  1012 HOH   A O   1 
HETATM 5884 O  O   . HOH   I 5 .   ? 10.621 2.893   -17.696 1.00 19.00 ?  1013 HOH   A O   1 
HETATM 5885 O  O   . HOH   I 5 .   ? 30.740 15.620  0.178   1.00 16.21 ?  1014 HOH   A O   1 
HETATM 5886 O  O   . HOH   I 5 .   ? 6.569  -19.391 2.546   1.00 25.03 ?  1015 HOH   A O   1 
HETATM 5887 O  O   . HOH   I 5 .   ? 30.925 8.312   3.851   1.00 13.42 ?  1016 HOH   A O   1 
HETATM 5888 O  O   . HOH   I 5 .   ? 33.615 7.882   4.260   1.00 14.96 ?  1017 HOH   A O   1 
HETATM 5889 O  O   . HOH   I 5 .   ? 5.296  16.857  -1.884  1.00 23.65 ?  1018 HOH   A O   1 
HETATM 5890 O  O   . HOH   I 5 .   ? 20.695 -5.975  -0.139  1.00 13.89 ?  1019 HOH   A O   1 
HETATM 5891 O  O   . HOH   I 5 .   ? 7.602  -3.425  20.839  1.00 33.73 ?  1020 HOH   A O   1 
HETATM 5892 O  O   . HOH   I 5 .   ? 32.196 -23.897 -1.811  1.00 24.60 ?  1021 HOH   A O   1 
HETATM 5893 O  O   . HOH   I 5 .   ? 6.801  -7.565  -10.169 1.00 21.70 ?  1022 HOH   A O   1 
HETATM 5894 O  O   . HOH   I 5 .   ? 8.479  15.920  -19.654 1.00 32.35 ?  1023 HOH   A O   1 
HETATM 5895 O  O   . HOH   I 5 .   ? 15.727 0.902   20.333  1.00 23.39 ?  1024 HOH   A O   1 
HETATM 5896 O  O   . HOH   I 5 .   ? 29.192 6.771   20.789  1.00 36.38 ?  1025 HOH   A O   1 
HETATM 5897 O  O   . HOH   I 5 .   ? 24.082 -22.482 0.163   1.00 17.64 ?  1026 HOH   A O   1 
HETATM 5898 O  O   . HOH   I 5 .   ? 11.064 -22.949 -6.047  1.00 27.62 ?  1027 HOH   A O   1 
HETATM 5899 O  O   . HOH   I 5 .   ? 28.791 -19.558 10.635  1.00 34.85 ?  1028 HOH   A O   1 
HETATM 5900 O  O   . HOH   I 5 .   ? 34.188 1.865   22.441  1.00 17.57 ?  1029 HOH   A O   1 
HETATM 5901 O  O   . HOH   I 5 .   ? 13.013 8.595   -14.112 1.00 12.57 ?  1030 HOH   A O   1 
HETATM 5902 O  O   . HOH   I 5 .   ? 13.990 6.896   17.247  1.00 29.97 ?  1031 HOH   A O   1 
HETATM 5903 O  O   . HOH   I 5 .   ? 35.189 -11.256 -1.441  1.00 15.40 ?  1032 HOH   A O   1 
HETATM 5904 O  O   . HOH   I 5 .   ? 28.990 11.644  -12.061 1.00 17.02 ?  1033 HOH   A O   1 
HETATM 5905 O  O   . HOH   I 5 .   ? 25.333 15.043  -12.923 1.00 17.70 ?  1034 HOH   A O   1 
HETATM 5906 O  O   . HOH   I 5 .   ? -0.427 7.779   -2.954  1.00 41.05 ?  1035 HOH   A O   1 
HETATM 5907 O  O   . HOH   I 5 .   ? 30.930 -0.759  23.458  1.00 19.54 ?  1036 HOH   A O   1 
HETATM 5908 O  O   . HOH   I 5 .   ? 1.687  8.514   -12.132 1.00 40.90 ?  1037 HOH   A O   1 
HETATM 5909 O  O   . HOH   I 5 .   ? 9.311  -10.107 -10.612 1.00 22.40 ?  1038 HOH   A O   1 
HETATM 5910 O  O   . HOH   I 5 .   ? 23.049 21.372  -1.725  1.00 22.82 ?  1039 HOH   A O   1 
HETATM 5911 O  O   . HOH   I 5 .   ? 26.064 -11.806 16.463  1.00 38.70 ?  1040 HOH   A O   1 
HETATM 5912 O  O   . HOH   I 5 .   ? 36.265 -15.595 -12.789 1.00 39.71 ?  1041 HOH   A O   1 
HETATM 5913 O  O   . HOH   I 5 .   ? 6.415  -4.483  -12.741 1.00 17.26 ?  1042 HOH   A O   1 
HETATM 5914 O  O   . HOH   I 5 .   ? 27.045 22.889  9.357   1.00 22.57 ?  1043 HOH   A O   1 
HETATM 5915 O  O   . HOH   I 5 .   ? 0.070  3.594   -5.076  1.00 26.25 ?  1044 HOH   A O   1 
HETATM 5916 O  O   . HOH   I 5 .   ? 23.790 -29.416 -7.978  1.00 21.03 ?  1045 HOH   A O   1 
HETATM 5917 O  O   . HOH   I 5 .   ? 35.959 -4.559  0.842   1.00 21.19 ?  1046 HOH   A O   1 
HETATM 5918 O  O   . HOH   I 5 .   ? 10.955 20.523  -6.331  1.00 27.07 ?  1047 HOH   A O   1 
HETATM 5919 O  O   . HOH   I 5 .   ? 31.737 -8.177  14.172  1.00 20.24 ?  1048 HOH   A O   1 
HETATM 5920 O  O   . HOH   I 5 .   ? 20.528 -0.128  -15.543 1.00 16.55 ?  1049 HOH   A O   1 
HETATM 5921 O  O   . HOH   I 5 .   ? 17.413 -18.574 -14.775 1.00 23.87 ?  1050 HOH   A O   1 
HETATM 5922 O  O   . HOH   I 5 .   ? 16.045 13.232  -23.111 1.00 43.48 ?  1051 HOH   A O   1 
HETATM 5923 O  O   . HOH   I 5 .   ? 13.204 15.655  -18.851 1.00 21.77 ?  1052 HOH   A O   1 
HETATM 5924 O  O   . HOH   I 5 .   ? 24.785 -17.431 13.721  1.00 25.01 ?  1053 HOH   A O   1 
HETATM 5925 O  O   . HOH   I 5 .   ? 24.320 21.150  12.779  1.00 17.49 ?  1054 HOH   A O   1 
HETATM 5926 O  O   . HOH   I 5 .   ? 34.917 -1.182  14.687  1.00 13.01 ?  1055 HOH   A O   1 
HETATM 5927 O  O   . HOH   I 5 .   ? 19.770 -23.420 3.126   1.00 36.81 ?  1056 HOH   A O   1 
HETATM 5928 O  O   . HOH   I 5 .   ? 5.382  10.548  8.377   1.00 24.26 ?  1057 HOH   A O   1 
HETATM 5929 O  O   . HOH   I 5 .   ? 18.082 18.118  1.513   1.00 22.10 ?  1058 HOH   A O   1 
HETATM 5930 O  O   . HOH   I 5 .   ? 34.236 7.971   16.639  1.00 32.42 ?  1059 HOH   A O   1 
HETATM 5931 O  O   . HOH   I 5 .   ? 18.942 17.338  6.456   1.00 21.25 ?  1060 HOH   A O   1 
HETATM 5932 O  O   . HOH   I 5 .   ? 38.987 2.821   10.589  1.00 20.51 ?  1061 HOH   A O   1 
HETATM 5933 O  O   . HOH   I 5 .   ? 32.957 -16.467 -10.861 1.00 25.87 ?  1062 HOH   A O   1 
HETATM 5934 O  O   . HOH   I 5 .   ? -3.235 -8.897  6.280   1.00 38.85 ?  1063 HOH   A O   1 
HETATM 5935 O  O   . HOH   I 5 .   ? 17.898 -27.017 -7.702  1.00 23.39 ?  1064 HOH   A O   1 
HETATM 5936 O  O   . HOH   I 5 .   ? 14.560 4.299   18.147  1.00 25.61 ?  1065 HOH   A O   1 
HETATM 5937 O  O   . HOH   I 5 .   ? 14.910 -17.224 13.001  1.00 22.28 ?  1066 HOH   A O   1 
HETATM 5938 O  O   . HOH   I 5 .   ? 21.558 0.614   -22.931 1.00 23.39 ?  1067 HOH   A O   1 
HETATM 5939 O  O   . HOH   I 5 .   ? 14.055 -0.424  -18.113 1.00 19.63 ?  1068 HOH   A O   1 
HETATM 5940 O  O   . HOH   I 5 .   ? 19.743 23.295  -4.936  1.00 40.10 ?  1069 HOH   A O   1 
HETATM 5941 O  O   . HOH   I 5 .   ? 28.876 -12.791 -6.110  1.00 12.23 ?  1070 HOH   A O   1 
HETATM 5942 O  O   . HOH   I 5 .   ? 17.231 4.600   -24.041 1.00 24.53 ?  1071 HOH   A O   1 
HETATM 5943 O  O   . HOH   I 5 .   ? 14.477 -22.052 2.301   1.00 26.45 ?  1072 HOH   A O   1 
HETATM 5944 O  O   . HOH   I 5 .   ? 32.445 -26.228 -3.448  1.00 37.23 ?  1073 HOH   A O   1 
HETATM 5945 O  O   . HOH   I 5 .   ? 37.258 5.977   4.979   1.00 17.76 ?  1074 HOH   A O   1 
HETATM 5946 O  O   . HOH   I 5 .   ? 21.426 -11.803 -2.999  1.00 11.41 ?  1075 HOH   A O   1 
HETATM 5947 O  O   . HOH   I 5 .   ? 23.126 -19.872 -15.076 1.00 26.92 ?  1076 HOH   A O   1 
HETATM 5948 O  O   . HOH   I 5 .   ? 9.226  5.233   -19.207 1.00 20.74 ?  1077 HOH   A O   1 
HETATM 5949 O  O   . HOH   I 5 .   ? 12.626 -18.289 -16.471 1.00 20.43 ?  1078 HOH   A O   1 
HETATM 5950 O  O   . HOH   I 5 .   ? 25.756 -10.831 18.418  1.00 40.89 ?  1079 HOH   A O   1 
HETATM 5951 O  O   . HOH   I 5 .   ? 35.546 -13.641 -0.198  1.00 15.51 ?  1080 HOH   A O   1 
HETATM 5952 O  O   . HOH   I 5 .   ? 17.653 -4.271  -19.978 1.00 36.10 ?  1081 HOH   A O   1 
HETATM 5953 O  O   . HOH   I 5 .   ? 2.484  -13.659 3.948   1.00 21.32 ?  1082 HOH   A O   1 
HETATM 5954 O  O   . HOH   I 5 .   ? 21.878 13.941  19.556  1.00 42.90 ?  1083 HOH   A O   1 
HETATM 5955 O  O   . HOH   I 5 .   ? 31.218 -13.135 -16.983 1.00 38.11 ?  1084 HOH   A O   1 
HETATM 5956 O  O   . HOH   I 5 .   ? -0.999 1.580   -3.877  1.00 21.72 ?  1085 HOH   A O   1 
HETATM 5957 O  O   . HOH   I 5 .   ? 39.890 3.363   -1.816  1.00 26.15 ?  1086 HOH   A O   1 
HETATM 5958 O  O   . HOH   I 5 .   ? 7.649  18.981  -17.474 1.00 22.84 ?  1087 HOH   A O   1 
HETATM 5959 O  O   . HOH   I 5 .   ? 29.850 19.929  -14.044 1.00 45.75 ?  1088 HOH   A O   1 
HETATM 5960 O  O   . HOH   I 5 .   ? 18.733 7.266   -22.509 1.00 21.41 ?  1089 HOH   A O   1 
HETATM 5961 O  O   . HOH   I 5 .   ? 39.669 -7.020  6.174   1.00 18.27 ?  1090 HOH   A O   1 
HETATM 5962 O  O   . HOH   I 5 .   ? 26.396 -30.498 -0.998  1.00 41.97 ?  1091 HOH   A O   1 
HETATM 5963 O  O   . HOH   I 5 .   ? 21.904 -26.448 -12.300 1.00 18.11 ?  1092 HOH   A O   1 
HETATM 5964 O  O   . HOH   I 5 .   ? 40.099 -6.855  -0.389  1.00 39.69 ?  1093 HOH   A O   1 
HETATM 5965 O  O   . HOH   I 5 .   ? -1.215 7.467   -10.794 1.00 33.48 ?  1094 HOH   A O   1 
HETATM 5966 O  O   . HOH   I 5 .   ? 9.424  -21.060 -5.634  1.00 21.25 ?  1095 HOH   A O   1 
HETATM 5967 O  O   . HOH   I 5 .   ? 21.765 11.653  -18.105 1.00 17.35 ?  1096 HOH   A O   1 
HETATM 5968 O  O   . HOH   I 5 .   ? 33.465 12.956  7.930   1.00 24.67 ?  1097 HOH   A O   1 
HETATM 5969 O  O   . HOH   I 5 .   ? 30.718 20.183  0.837   1.00 42.91 ?  1098 HOH   A O   1 
HETATM 5970 O  O   . HOH   I 5 .   ? 24.201 20.101  8.975   1.00 17.55 ?  1099 HOH   A O   1 
HETATM 5971 O  O   . HOH   I 5 .   ? 35.871 -13.941 -9.026  1.00 28.50 ?  1100 HOH   A O   1 
HETATM 5972 O  O   . HOH   I 5 .   ? 12.060 -23.148 0.951   1.00 30.28 ?  1101 HOH   A O   1 
HETATM 5973 O  O   . HOH   I 5 .   ? 31.772 -18.319 -9.157  1.00 12.65 ?  1102 HOH   A O   1 
HETATM 5974 O  O   . HOH   I 5 .   ? 19.207 -12.177 -1.195  1.00 12.29 ?  1103 HOH   A O   1 
HETATM 5975 O  O   . HOH   I 5 .   ? 9.577  9.186   -20.760 1.00 40.80 ?  1104 HOH   A O   1 
HETATM 5976 O  O   . HOH   I 5 .   ? 4.532  -10.900 -6.327  1.00 40.78 ?  1105 HOH   A O   1 
HETATM 5977 O  O   . HOH   I 5 .   ? 3.614  2.490   -20.950 1.00 18.58 ?  1106 HOH   A O   1 
HETATM 5978 O  O   . HOH   I 5 .   ? 18.435 -20.538 9.497   1.00 44.43 ?  1107 HOH   A O   1 
HETATM 5979 O  O   . HOH   I 5 .   ? 2.925  -9.862  -2.270  1.00 21.16 ?  1108 HOH   A O   1 
HETATM 5980 O  O   . HOH   I 5 .   ? 25.859 -13.576 14.577  1.00 18.47 ?  1109 HOH   A O   1 
HETATM 5981 O  O   . HOH   I 5 .   ? 29.711 -8.699  19.871  1.00 36.75 ?  1110 HOH   A O   1 
HETATM 5982 O  O   . HOH   I 5 .   ? 5.171  -13.740 1.475   1.00 17.30 ?  1111 HOH   A O   1 
HETATM 5983 O  O   . HOH   I 5 .   ? 24.756 -23.821 -16.394 1.00 22.95 ?  1112 HOH   A O   1 
HETATM 5984 O  O   . HOH   I 5 .   ? -2.683 3.094   -2.322  1.00 27.20 ?  1113 HOH   A O   1 
HETATM 5985 O  O   . HOH   I 5 .   ? 43.817 -12.401 -5.452  1.00 28.85 ?  1114 HOH   A O   1 
HETATM 5986 O  O   . HOH   I 5 .   ? 38.425 -24.098 -8.686  1.00 25.11 ?  1115 HOH   A O   1 
HETATM 5987 O  O   . HOH   I 5 .   ? 37.762 -32.510 -5.561  1.00 28.82 ?  1116 HOH   A O   1 
HETATM 5988 O  O   . HOH   I 5 .   ? 31.679 -10.823 -15.286 1.00 18.93 ?  1117 HOH   A O   1 
HETATM 5989 O  O   . HOH   I 5 .   ? 35.461 5.032   18.417  1.00 17.66 ?  1118 HOH   A O   1 
HETATM 5990 O  O   . HOH   I 5 .   ? 12.662 -16.001 12.478  1.00 20.07 ?  1119 HOH   A O   1 
HETATM 5991 O  O   . HOH   I 5 .   ? 6.991  18.649  -0.925  1.00 32.49 ?  1120 HOH   A O   1 
HETATM 5992 O  O   . HOH   I 5 .   ? 25.524 5.610   20.859  1.00 22.26 ?  1121 HOH   A O   1 
HETATM 5993 O  O   . HOH   I 5 .   ? 24.632 -21.472 7.348   1.00 29.21 ?  1122 HOH   A O   1 
HETATM 5994 O  O   . HOH   I 5 .   ? 22.713 -7.441  20.364  1.00 23.25 ?  1123 HOH   A O   1 
HETATM 5995 O  O   . HOH   I 5 .   ? 25.302 -19.470 5.565   1.00 21.91 ?  1124 HOH   A O   1 
HETATM 5996 O  O   . HOH   I 5 .   ? 6.712  14.261  8.953   1.00 38.86 ?  1125 HOH   A O   1 
HETATM 5997 O  O   . HOH   I 5 .   ? 21.474 14.893  -17.184 1.00 26.03 ?  1126 HOH   A O   1 
HETATM 5998 O  O   . HOH   I 5 .   ? 24.598 -7.266  -17.426 1.00 24.45 ?  1127 HOH   A O   1 
HETATM 5999 O  O   . HOH   I 5 .   ? 2.347  9.839   -9.921  1.00 42.69 ?  1128 HOH   A O   1 
HETATM 6000 O  O   . HOH   I 5 .   ? 37.310 8.546   3.961   1.00 24.38 ?  1129 HOH   A O   1 
HETATM 6001 O  O   . HOH   I 5 .   ? 37.878 1.933   -9.596  1.00 25.64 ?  1130 HOH   A O   1 
HETATM 6002 O  O   . HOH   I 5 .   ? 20.727 17.488  -20.584 1.00 33.97 ?  1131 HOH   A O   1 
HETATM 6003 O  O   . HOH   I 5 .   ? 8.895  -18.852 -13.146 1.00 26.11 ?  1132 HOH   A O   1 
HETATM 6004 O  O   . HOH   I 5 .   ? 7.989  -23.750 -8.786  1.00 35.84 ?  1133 HOH   A O   1 
HETATM 6005 O  O   . HOH   I 5 .   ? 17.884 -2.064  23.337  1.00 40.55 ?  1134 HOH   A O   1 
HETATM 6006 O  O   . HOH   I 5 .   ? 5.402  -14.673 12.053  1.00 44.45 ?  1135 HOH   A O   1 
HETATM 6007 O  O   . HOH   I 5 .   ? 14.434 1.060   -20.454 1.00 28.65 ?  1136 HOH   A O   1 
HETATM 6008 O  O   . HOH   I 5 .   ? 6.625  6.289   -20.337 1.00 30.12 ?  1137 HOH   A O   1 
HETATM 6009 O  O   . HOH   I 5 .   ? 32.462 1.067   24.433  1.00 21.52 ?  1138 HOH   A O   1 
HETATM 6010 O  O   . HOH   I 5 .   ? 14.757 -11.158 -15.558 1.00 14.68 ?  1139 HOH   A O   1 
HETATM 6011 O  O   . HOH   I 5 .   ? 36.766 -28.797 -8.386  1.00 34.08 ?  1140 HOH   A O   1 
HETATM 6012 O  O   . HOH   I 5 .   ? 7.801  -13.970 -9.894  1.00 36.76 ?  1141 HOH   A O   1 
HETATM 6013 O  O   . HOH   I 5 .   ? 11.224 -20.066 -14.695 1.00 14.44 ?  1142 HOH   A O   1 
HETATM 6014 O  O   . HOH   I 5 .   ? 35.065 -7.270  11.714  1.00 18.78 ?  1143 HOH   A O   1 
HETATM 6015 O  O   . HOH   I 5 .   ? 23.877 15.635  -16.515 1.00 20.52 ?  1144 HOH   A O   1 
HETATM 6016 O  O   . HOH   I 5 .   ? 26.820 -1.574  22.058  1.00 15.41 ?  1145 HOH   A O   1 
HETATM 6017 O  O   . HOH   I 5 .   ? 19.283 22.399  -17.294 1.00 34.48 ?  1146 HOH   A O   1 
HETATM 6018 O  O   . HOH   I 5 .   ? 31.926 5.042   22.049  1.00 42.25 ?  1147 HOH   A O   1 
HETATM 6019 O  O   . HOH   I 5 .   ? 5.840  -9.186  14.944  1.00 39.39 ?  1148 HOH   A O   1 
HETATM 6020 O  O   . HOH   I 5 .   ? 21.052 12.841  -16.028 1.00 41.85 ?  1149 HOH   A O   1 
HETATM 6021 O  O   . HOH   I 5 .   ? 23.829 7.168   -23.717 1.00 45.86 ?  1150 HOH   A O   1 
HETATM 6022 O  O   . HOH   I 5 .   ? 17.514 24.613  -17.668 1.00 38.63 ?  1151 HOH   A O   1 
HETATM 6023 O  O   . HOH   I 5 .   ? 0.830  7.978   -5.802  1.00 31.58 ?  1152 HOH   A O   1 
HETATM 6024 O  O   . HOH   I 5 .   ? 4.625  9.414   4.000   1.00 22.10 ?  1153 HOH   A O   1 
HETATM 6025 O  O   . HOH   I 5 .   ? 14.481 6.071   -24.038 1.00 44.30 ?  1154 HOH   A O   1 
HETATM 6026 O  O   . HOH   I 5 .   ? 19.685 -2.453  -16.864 1.00 16.36 ?  1155 HOH   A O   1 
HETATM 6027 O  O   . HOH   I 5 .   ? 38.550 -6.147  8.606   1.00 16.42 ?  1156 HOH   A O   1 
HETATM 6028 O  O   . HOH   I 5 .   ? 24.686 16.502  16.399  1.00 22.77 ?  1157 HOH   A O   1 
HETATM 6029 O  O   . HOH   I 5 .   ? 20.926 11.683  -21.839 1.00 34.74 ?  1158 HOH   A O   1 
HETATM 6030 O  O   . HOH   I 5 .   ? 15.597 -20.274 9.230   1.00 21.81 ?  1159 HOH   A O   1 
HETATM 6031 O  O   . HOH   I 5 .   ? 20.101 -17.020 -15.343 1.00 25.57 ?  1160 HOH   A O   1 
HETATM 6032 O  O   . HOH   I 5 .   ? 2.846  -10.370 10.504  1.00 33.22 ?  1161 HOH   A O   1 
HETATM 6033 O  O   . HOH   I 5 .   ? 22.816 -6.132  -14.311 1.00 45.46 ?  1162 HOH   A O   1 
HETATM 6034 O  O   . HOH   I 5 .   ? 20.905 -21.046 -17.553 1.00 39.14 ?  1163 HOH   A O   1 
HETATM 6035 O  O   . HOH   I 5 .   ? 32.670 21.792  -6.902  1.00 39.50 ?  1164 HOH   A O   1 
HETATM 6036 O  O   . HOH   I 5 .   ? 37.653 -13.589 1.494   1.00 25.04 ?  1165 HOH   A O   1 
HETATM 6037 O  O   . HOH   I 5 .   ? 35.984 5.905   -9.995  1.00 32.33 ?  1166 HOH   A O   1 
HETATM 6038 O  O   . HOH   I 5 .   ? 33.651 -9.602  -10.004 1.00 21.89 ?  1167 HOH   A O   1 
HETATM 6039 O  O   . HOH   I 5 .   ? 10.999 -9.714  20.467  1.00 42.39 ?  1168 HOH   A O   1 
HETATM 6040 O  O   . HOH   I 5 .   ? 24.865 23.796  -2.432  1.00 44.92 ?  1169 HOH   A O   1 
HETATM 6041 O  O   . HOH   I 5 .   ? 33.276 -2.909  20.602  1.00 37.50 ?  1170 HOH   A O   1 
HETATM 6042 O  O   . HOH   I 5 .   ? 31.990 -21.314 3.584   1.00 33.81 ?  1171 HOH   A O   1 
HETATM 6043 O  O   . HOH   I 5 .   ? 19.270 -23.114 8.690   1.00 20.97 ?  1172 HOH   A O   1 
HETATM 6044 O  O   . HOH   I 5 .   ? 33.282 17.234  3.663   1.00 24.95 ?  1173 HOH   A O   1 
HETATM 6045 O  O   . HOH   I 5 .   ? 17.027 17.827  13.000  1.00 39.51 ?  1174 HOH   A O   1 
HETATM 6046 O  O   . HOH   I 5 .   ? 20.925 -12.766 15.208  1.00 29.12 ?  1175 HOH   A O   1 
HETATM 6047 O  O   . HOH   I 5 .   ? 26.621 0.624   26.191  1.00 23.66 ?  1176 HOH   A O   1 
HETATM 6048 O  O   . HOH   I 5 .   ? 29.392 1.270   -21.195 1.00 42.60 ?  1177 HOH   A O   1 
HETATM 6049 O  O   . HOH   I 5 .   ? 22.925 -22.450 -15.514 1.00 28.56 ?  1178 HOH   A O   1 
HETATM 6050 O  O   . HOH   I 5 .   ? 21.432 -32.820 -2.831  1.00 47.09 ?  1179 HOH   A O   1 
HETATM 6051 O  O   . HOH   I 5 .   ? 14.279 -3.028  -19.860 1.00 36.15 ?  1180 HOH   A O   1 
HETATM 6052 O  O   . HOH   I 5 .   ? 11.654 1.332   -20.514 1.00 36.06 ?  1181 HOH   A O   1 
HETATM 6053 O  O   . HOH   I 5 .   ? 6.643  14.441  5.433   1.00 35.12 ?  1182 HOH   A O   1 
HETATM 6054 O  O   . HOH   I 5 .   ? 14.156 -24.940 -6.797  1.00 23.44 ?  1183 HOH   A O   1 
HETATM 6055 O  O   . HOH   I 5 .   ? 31.634 -1.607  -15.566 1.00 35.81 ?  1184 HOH   A O   1 
HETATM 6056 O  O   . HOH   I 5 .   ? 31.613 17.074  -1.979  1.00 25.17 ?  1185 HOH   A O   1 
HETATM 6057 O  O   . HOH   I 5 .   ? 19.943 -31.595 -4.622  1.00 44.24 ?  1186 HOH   A O   1 
HETATM 6058 O  O   . HOH   I 5 .   ? 36.442 -20.471 3.608   1.00 46.40 ?  1187 HOH   A O   1 
HETATM 6059 O  O   . HOH   I 5 .   ? 19.963 19.674  6.239   1.00 34.29 ?  1188 HOH   A O   1 
HETATM 6060 O  O   . HOH   I 5 .   ? 24.333 -33.446 -2.478  1.00 44.49 ?  1189 HOH   A O   1 
HETATM 6061 O  O   . HOH   I 5 .   ? 31.074 17.355  2.340   1.00 19.83 ?  1190 HOH   A O   1 
HETATM 6062 O  O   . HOH   I 5 .   ? 36.617 7.370   13.544  1.00 38.10 ?  1191 HOH   A O   1 
HETATM 6063 O  O   . HOH   I 5 .   ? 3.102  -10.969 13.040  1.00 40.10 ?  1192 HOH   A O   1 
HETATM 6064 O  O   . HOH   I 5 .   ? -5.135 3.641   0.992   1.00 41.05 ?  1193 HOH   A O   1 
HETATM 6065 O  O   . HOH   I 5 .   ? 9.658  -19.125 7.455   1.00 28.07 ?  1194 HOH   A O   1 
HETATM 6066 O  O   . HOH   I 5 .   ? 8.828  -20.847 -8.020  1.00 38.95 ?  1195 HOH   A O   1 
HETATM 6067 O  O   . HOH   I 5 .   ? -1.981 0.100   -6.143  1.00 27.00 ?  1196 HOH   A O   1 
HETATM 6068 O  O   . HOH   I 5 .   ? 30.898 -26.856 -15.454 1.00 25.12 ?  1197 HOH   A O   1 
HETATM 6069 O  O   . HOH   I 5 .   ? 22.608 1.508   -25.913 1.00 44.14 ?  1198 HOH   A O   1 
HETATM 6070 O  O   . HOH   I 5 .   ? 31.939 -7.402  17.185  1.00 38.63 ?  1199 HOH   A O   1 
HETATM 6071 O  O   . HOH   I 5 .   ? 23.680 8.657   22.912  1.00 51.47 ?  1200 HOH   A O   1 
HETATM 6072 O  O   . HOH   I 5 .   ? 33.746 -19.731 4.648   1.00 37.59 ?  1201 HOH   A O   1 
HETATM 6073 O  O   . HOH   I 5 .   ? 38.919 -0.009  0.411   1.00 16.93 ?  1202 HOH   A O   1 
HETATM 6074 O  O   . HOH   I 5 .   ? 7.271  -24.176 -11.864 1.00 37.02 ?  1203 HOH   A O   1 
HETATM 6075 O  O   . HOH   I 5 .   ? 36.813 -8.066  10.348  1.00 44.27 ?  1204 HOH   A O   1 
HETATM 6076 O  O   . HOH   I 5 .   ? 28.078 -29.374 -10.730 1.00 40.91 ?  1205 HOH   A O   1 
HETATM 6077 O  O   . HOH   I 5 .   ? 25.966 -4.522  22.880  1.00 43.72 ?  1206 HOH   A O   1 
HETATM 6078 O  O   . HOH   I 5 .   ? 29.478 -11.484 16.045  1.00 29.36 ?  1207 HOH   A O   1 
HETATM 6079 O  O   . HOH   I 5 .   ? 18.638 22.032  -1.957  1.00 30.97 ?  1208 HOH   A O   1 
HETATM 6080 O  O   . HOH   I 5 .   ? 9.253  -25.003 -5.639  1.00 36.79 ?  1209 HOH   A O   1 
HETATM 6081 O  O   . HOH   I 5 .   ? 39.095 8.728   1.707   1.00 26.34 ?  1210 HOH   A O   1 
HETATM 6082 O  O   . HOH   I 5 .   ? 28.452 15.840  -17.646 1.00 33.00 ?  1211 HOH   A O   1 
HETATM 6083 O  O   . HOH   I 5 .   ? 13.902 8.956   19.591  1.00 43.01 ?  1212 HOH   A O   1 
HETATM 6084 O  O   . HOH   I 5 .   ? 44.862 -10.208 3.911   1.00 37.14 ?  1213 HOH   A O   1 
HETATM 6085 O  O   . HOH   I 5 .   ? 26.954 20.302  -17.482 1.00 36.12 ?  1214 HOH   A O   1 
HETATM 6086 O  O   . HOH   I 5 .   ? 12.483 19.129  2.481   1.00 32.85 ?  1215 HOH   A O   1 
HETATM 6087 O  O   . HOH   I 5 .   ? 23.811 3.432   -14.647 1.00 18.43 ?  1216 HOH   A O   1 
HETATM 6088 O  O   . HOH   I 5 .   ? 33.959 -8.206  14.425  1.00 34.79 ?  1217 HOH   A O   1 
HETATM 6089 O  O   . HOH   I 5 .   ? -5.593 -4.318  -3.443  1.00 39.50 ?  1218 HOH   A O   1 
HETATM 6090 O  O   . HOH   I 5 .   ? 11.095 -14.335 14.073  1.00 26.03 ?  1219 HOH   A O   1 
HETATM 6091 O  O   . HOH   I 5 .   ? 32.279 24.730  8.077   1.00 30.65 ?  1220 HOH   A O   1 
HETATM 6092 O  O   . HOH   I 5 .   ? 3.888  -5.378  -12.193 1.00 29.13 ?  1221 HOH   A O   1 
HETATM 6093 O  O   . HOH   I 5 .   ? 18.120 17.626  21.040  1.00 25.16 ?  1222 HOH   A O   1 
HETATM 6094 O  O   . HOH   I 5 .   ? 0.502  2.803   -20.486 1.00 34.94 ?  1223 HOH   A O   1 
HETATM 6095 O  O   . HOH   I 5 .   ? 14.298 -5.781  -18.777 1.00 43.25 ?  1224 HOH   A O   1 
HETATM 6096 O  O   . HOH   I 5 .   ? 7.528  -15.741 -11.668 1.00 49.25 ?  1225 HOH   A O   1 
HETATM 6097 O  O   . HOH   I 5 .   ? 34.735 -15.105 6.663   1.00 45.66 ?  1226 HOH   A O   1 
HETATM 6098 O  O   . HOH   I 5 .   ? 33.852 0.072   26.370  1.00 26.77 ?  1227 HOH   A O   1 
HETATM 6099 O  O   . HOH   I 5 .   ? 7.046  -11.789 -10.573 1.00 45.95 ?  1228 HOH   A O   1 
HETATM 6100 O  O   . HOH   I 5 .   ? 11.548 -11.563 14.028  1.00 19.76 ?  1229 HOH   A O   1 
HETATM 6101 O  O   . HOH   I 5 .   ? 1.640  -12.295 -1.865  1.00 27.67 ?  1230 HOH   A O   1 
HETATM 6102 O  O   . HOH   I 5 .   ? 22.256 20.741  7.162   1.00 34.91 ?  1231 HOH   A O   1 
HETATM 6103 O  O   . HOH   I 5 .   ? 34.410 -8.303  20.311  1.00 31.90 ?  1232 HOH   A O   1 
HETATM 6104 O  O   . HOH   I 5 .   ? -1.278 9.139   -15.999 1.00 29.98 ?  1233 HOH   A O   1 
HETATM 6105 O  O   . HOH   I 5 .   ? 18.646 20.650  1.505   1.00 47.13 ?  1234 HOH   A O   1 
HETATM 6106 O  O   . HOH   I 5 .   ? 23.418 -14.096 15.808  1.00 38.03 ?  1235 HOH   A O   1 
HETATM 6107 O  O   . HOH   I 5 .   ? 9.349  -8.678  -13.136 1.00 35.09 ?  1236 HOH   A O   1 
HETATM 6108 O  O   . HOH   I 5 .   ? 33.027 11.136  9.849   1.00 41.14 ?  1237 HOH   A O   1 
HETATM 6109 O  O   . HOH   I 5 .   ? 11.467 -4.309  22.793  1.00 44.17 ?  1238 HOH   A O   1 
HETATM 6110 O  O   . HOH   I 5 .   ? 14.615 12.070  14.853  1.00 24.81 ?  1239 HOH   A O   1 
HETATM 6111 O  O   . HOH   I 5 .   ? 10.316 21.840  -1.291  1.00 38.78 ?  1240 HOH   A O   1 
HETATM 6112 O  O   . HOH   I 5 .   ? 23.294 -16.780 15.833  1.00 42.13 ?  1241 HOH   A O   1 
HETATM 6113 O  O   . HOH   I 5 .   ? 20.828 19.630  10.786  1.00 22.63 ?  1242 HOH   A O   1 
HETATM 6114 O  O   . HOH   I 5 .   ? -1.751 -2.889  -5.976  1.00 36.06 ?  1243 HOH   A O   1 
HETATM 6115 O  O   . HOH   I 5 .   ? 28.296 -1.044  24.447  1.00 35.87 ?  1244 HOH   A O   1 
HETATM 6116 O  O   . HOH   I 5 .   ? 3.134  -14.489 -0.219  1.00 32.58 ?  1245 HOH   A O   1 
HETATM 6117 O  O   . HOH   I 5 .   ? 19.042 -28.525 -5.983  1.00 42.02 ?  1246 HOH   A O   1 
HETATM 6118 O  O   . HOH   I 5 .   ? 6.463  -15.971 8.246   1.00 31.44 ?  1247 HOH   A O   1 
HETATM 6119 O  O   . HOH   I 5 .   ? 1.423  -14.890 1.775   1.00 28.48 ?  1248 HOH   A O   1 
HETATM 6120 O  O   . HOH   I 5 .   ? 16.997 16.825  8.132   1.00 43.77 ?  1249 HOH   A O   1 
HETATM 6121 O  O   . HOH   I 5 .   ? 38.671 -4.651  0.351   1.00 22.02 ?  1250 HOH   A O   1 
HETATM 6122 O  O   . HOH   I 5 .   ? 21.407 -9.982  21.484  1.00 36.90 ?  1251 HOH   A O   1 
HETATM 6123 O  O   . HOH   I 5 .   ? 39.506 -2.058  -1.200  1.00 24.97 ?  1252 HOH   A O   1 
HETATM 6124 O  O   . HOH   I 5 .   ? 3.586  11.877  6.484   1.00 40.29 ?  1253 HOH   A O   1 
HETATM 6125 O  O   . HOH   I 5 .   ? 10.744 -7.493  16.698  1.00 46.18 ?  1254 HOH   A O   1 
HETATM 6126 O  O   . HOH   I 5 .   ? 22.242 -17.985 -16.632 1.00 32.68 ?  1255 HOH   A O   1 
HETATM 6127 O  O   . HOH   I 5 .   ? 17.341 26.065  -11.368 1.00 34.29 ?  1256 HOH   A O   1 
HETATM 6128 O  O   . HOH   I 5 .   ? 5.635  4.159   -22.083 1.00 33.45 ?  1257 HOH   A O   1 
HETATM 6129 O  O   . HOH   I 5 .   ? 24.516 -4.537  -20.659 1.00 38.81 ?  1258 HOH   A O   1 
HETATM 6130 O  O   . HOH   I 5 .   ? 19.947 -18.761 14.943  1.00 35.13 ?  1259 HOH   A O   1 
HETATM 6131 O  O   . HOH   I 5 .   ? 41.208 -8.267  1.893   1.00 28.39 ?  1260 HOH   A O   1 
HETATM 6132 O  O   . HOH   I 5 .   ? 24.630 22.503  10.379  1.00 19.36 ?  1261 HOH   A O   1 
HETATM 6133 O  O   . HOH   I 5 .   ? 23.060 -25.013 5.526   1.00 36.88 ?  1262 HOH   A O   1 
HETATM 6134 O  O   . HOH   I 5 .   ? 25.567 6.213   23.392  1.00 41.15 ?  1263 HOH   A O   1 
HETATM 6135 O  O   . HOH   I 5 .   ? 17.180 -11.316 -16.665 1.00 34.49 ?  1264 HOH   A O   1 
HETATM 6136 O  O   . HOH   I 5 .   ? 11.740 -6.373  -17.329 1.00 40.72 ?  1265 HOH   A O   1 
HETATM 6137 O  O   . HOH   I 5 .   ? 1.539  4.010   -21.894 1.00 35.83 ?  1266 HOH   A O   1 
HETATM 6138 O  O   . HOH   I 5 .   ? 23.181 -24.572 -13.556 1.00 19.79 ?  1267 HOH   A O   1 
HETATM 6139 O  O   . HOH   I 5 .   ? 20.557 -24.396 5.713   1.00 31.92 ?  1268 HOH   A O   1 
HETATM 6140 O  O   . HOH   I 5 .   ? 37.668 -33.240 -7.900  1.00 30.32 ?  1269 HOH   A O   1 
HETATM 6141 O  O   . HOH   I 5 .   ? 12.915 12.361  13.124  1.00 44.47 ?  1270 HOH   A O   1 
HETATM 6142 O  O   . HOH   I 5 .   ? 35.557 -3.926  19.796  1.00 27.28 ?  1271 HOH   A O   1 
HETATM 6143 O  O   . HOH   I 5 .   ? 25.619 17.150  -17.936 1.00 33.97 ?  1272 HOH   A O   1 
HETATM 6144 O  O   . HOH   I 5 .   ? 27.513 7.923   17.411  1.00 46.90 ?  1273 HOH   A O   1 
HETATM 6145 O  O   . HOH   I 5 .   ? 28.408 7.257   23.459  1.00 41.40 ?  1274 HOH   A O   1 
HETATM 6146 O  O   . HOH   I 5 .   ? 33.201 -2.596  22.893  1.00 38.24 ?  1275 HOH   A O   1 
HETATM 6147 O  O   . HOH   I 5 .   ? 13.733 13.033  -22.643 1.00 38.97 ?  1276 HOH   A O   1 
HETATM 6148 O  O   . HOH   I 5 .   ? 35.667 7.462   9.282   1.00 32.64 ?  1277 HOH   A O   1 
HETATM 6149 O  O   . HOH   I 5 .   ? 18.586 -12.994 -18.166 1.00 36.77 ?  1278 HOH   A O   1 
HETATM 6150 O  O   . HOH   I 5 .   ? 18.990 -16.582 15.389  1.00 38.62 ?  1279 HOH   A O   1 
HETATM 6151 O  O   . HOH   I 5 .   ? 38.077 7.296   15.413  1.00 30.88 ?  1280 HOH   A O   1 
HETATM 6152 O  O   . HOH   I 5 .   ? 16.116 -17.234 15.733  1.00 37.92 ?  1281 HOH   A O   1 
HETATM 6153 O  O   . HOH   I 5 .   ? 6.227  -19.426 5.263   1.00 29.27 ?  1282 HOH   A O   1 
HETATM 6154 O  O   . HOH   I 5 .   ? 11.169 -24.371 2.945   1.00 41.42 ?  1283 HOH   A O   1 
HETATM 6155 O  O   . HOH   I 5 .   ? 4.899  -17.680 1.882   1.00 30.16 ?  1284 HOH   A O   1 
HETATM 6156 O  O   . HOH   I 5 .   ? 23.266 -9.108  -16.320 1.00 29.88 ?  1285 HOH   A O   1 
HETATM 6157 O  O   . HOH   I 5 .   ? 12.619 -11.795 -16.999 1.00 27.59 ?  1286 HOH   A O   1 
HETATM 6158 O  O   . HOH   I 5 .   ? 10.655 3.718   -20.819 1.00 27.83 ?  1287 HOH   A O   1 
HETATM 6159 O  O   . HOH   I 5 .   ? 4.084  -14.920 5.517   1.00 24.49 ?  1288 HOH   A O   1 
HETATM 6160 O  O   . HOH   I 5 .   ? 12.476 12.896  -20.164 1.00 26.99 ?  1289 HOH   A O   1 
HETATM 6161 O  O   . HOH   I 5 .   ? 36.484 -16.369 3.519   1.00 44.13 ?  1290 HOH   A O   1 
HETATM 6162 O  O   . HOH   I 5 .   ? 9.076  -10.764 17.192  1.00 36.23 ?  1291 HOH   A O   1 
HETATM 6163 O  O   . HOH   I 5 .   ? 7.428  4.456   17.594  1.00 42.07 ?  1292 HOH   A O   1 
HETATM 6164 O  O   . HOH   I 5 .   ? 5.044  -8.823  -11.906 1.00 41.70 ?  1293 HOH   A O   1 
HETATM 6165 O  O   . HOH   I 5 .   ? 17.162 -23.701 2.316   1.00 37.37 ?  1294 HOH   A O   1 
HETATM 6166 O  O   . HOH   I 5 .   ? 21.249 -22.722 -19.287 1.00 38.12 ?  1295 HOH   A O   1 
HETATM 6167 O  O   . HOH   I 5 .   ? 28.939 -3.318  25.069  1.00 36.15 ?  1296 HOH   A O   1 
HETATM 6168 O  O   . HOH   I 5 .   ? 12.376 -19.839 10.141  1.00 40.88 ?  1297 HOH   A O   1 
HETATM 6169 O  O   . HOH   I 5 .   ? 21.881 23.708  -4.125  1.00 44.76 ?  1298 HOH   A O   1 
HETATM 6170 O  O   . HOH   I 5 .   ? 20.904 22.053  9.412   1.00 32.92 ?  1299 HOH   A O   1 
HETATM 6171 O  O   . HOH   I 5 .   ? 11.850 -15.699 16.561  1.00 44.95 ?  1300 HOH   A O   1 
HETATM 6172 O  O   . HOH   J 5 .   ? 47.941 -33.843 33.410  1.00 38.14 ?  901  HOH   B O   1 
HETATM 6173 O  O   . HOH   J 5 .   ? 56.455 -17.550 10.101  1.00 34.69 ?  902  HOH   B O   1 
HETATM 6174 O  O   . HOH   J 5 .   ? 65.069 -25.095 31.465  1.00 36.43 ?  903  HOH   B O   1 
HETATM 6175 O  O   . HOH   J 5 .   ? 41.904 -20.086 30.008  1.00 39.22 ?  904  HOH   B O   1 
HETATM 6176 O  O   . HOH   J 5 .   ? 46.337 -18.000 8.831   1.00 43.12 ?  905  HOH   B O   1 
HETATM 6177 O  O   . HOH   J 5 .   ? 32.877 -12.561 27.012  1.00 42.74 ?  906  HOH   B O   1 
HETATM 6178 O  O   . HOH   J 5 .   ? 48.465 -31.557 32.117  1.00 29.56 ?  907  HOH   B O   1 
HETATM 6179 O  O   . HOH   J 5 .   ? 65.744 -3.949  38.729  1.00 35.67 ?  908  HOH   B O   1 
HETATM 6180 O  O   . HOH   J 5 .   ? 43.849 17.562  13.485  1.00 31.13 ?  909  HOH   B O   1 
HETATM 6181 O  O   . HOH   J 5 .   ? 52.539 -19.717 14.509  1.00 22.79 ?  910  HOH   B O   1 
HETATM 6182 O  O   . HOH   J 5 .   ? 48.261 25.959  30.909  1.00 44.67 ?  911  HOH   B O   1 
HETATM 6183 O  O   . HOH   J 5 .   ? 39.154 5.764   28.102  1.00 31.33 ?  912  HOH   B O   1 
HETATM 6184 O  O   . HOH   J 5 .   ? 47.666 -6.229  0.174   1.00 41.71 ?  913  HOH   B O   1 
HETATM 6185 O  O   . HOH   J 5 .   ? 62.526 -8.657  3.988   1.00 45.85 ?  914  HOH   B O   1 
HETATM 6186 O  O   . HOH   J 5 .   ? 59.096 8.012   46.221  1.00 40.87 ?  915  HOH   B O   1 
HETATM 6187 O  O   . HOH   J 5 .   ? 71.711 4.721   14.007  1.00 24.25 ?  916  HOH   B O   1 
HETATM 6188 O  O   . HOH   J 5 .   ? 59.573 18.275  20.886  1.00 28.17 ?  917  HOH   B O   1 
HETATM 6189 O  O   . HOH   J 5 .   ? 66.687 21.076  27.513  1.00 43.30 ?  918  HOH   B O   1 
HETATM 6190 O  O   . HOH   J 5 .   ? 70.618 -16.636 25.176  1.00 38.14 ?  919  HOH   B O   1 
HETATM 6191 O  O   . HOH   J 5 .   ? 45.892 -18.502 11.564  1.00 35.86 ?  920  HOH   B O   1 
HETATM 6192 O  O   . HOH   J 5 .   ? 66.793 -13.367 10.425  1.00 37.36 ?  921  HOH   B O   1 
HETATM 6193 O  O   . HOH   J 5 .   ? 35.413 -5.897  25.559  1.00 31.32 ?  922  HOH   B O   1 
HETATM 6194 O  O   . HOH   J 5 .   ? 55.587 6.684   48.623  1.00 19.11 ?  923  HOH   B O   1 
HETATM 6195 O  O   . HOH   J 5 .   ? 78.383 -8.836  16.941  1.00 35.90 ?  924  HOH   B O   1 
HETATM 6196 O  O   . HOH   J 5 .   ? 39.667 0.604   12.019  1.00 20.74 ?  925  HOH   B O   1 
HETATM 6197 O  O   . HOH   J 5 .   ? 55.750 -25.891 23.691  1.00 18.30 ?  926  HOH   B O   1 
HETATM 6198 O  O   . HOH   J 5 .   ? 75.411 7.223   40.178  1.00 19.02 ?  927  HOH   B O   1 
HETATM 6199 O  O   . HOH   J 5 .   ? 73.430 7.771   17.318  1.00 37.95 ?  928  HOH   B O   1 
HETATM 6200 O  O   . HOH   J 5 .   ? 73.652 -7.235  25.689  1.00 18.77 ?  929  HOH   B O   1 
HETATM 6201 O  O   . HOH   J 5 .   ? 43.149 11.632  36.151  1.00 23.97 ?  930  HOH   B O   1 
HETATM 6202 O  O   . HOH   J 5 .   ? 55.362 -2.524  43.451  1.00 23.95 ?  931  HOH   B O   1 
HETATM 6203 O  O   . HOH   J 5 .   ? 44.524 10.953  40.736  1.00 33.54 ?  932  HOH   B O   1 
HETATM 6204 O  O   . HOH   J 5 .   ? 66.556 -12.149 13.360  1.00 19.89 ?  933  HOH   B O   1 
HETATM 6205 O  O   . HOH   J 5 .   ? 49.526 10.681  7.026   1.00 40.22 ?  934  HOH   B O   1 
HETATM 6206 O  O   . HOH   J 5 .   ? 45.831 -20.687 39.940  1.00 23.61 ?  935  HOH   B O   1 
HETATM 6207 O  O   . HOH   J 5 .   ? 44.625 18.137  34.842  1.00 30.93 ?  936  HOH   B O   1 
HETATM 6208 O  O   . HOH   J 5 .   ? 57.965 6.663   1.221   1.00 31.79 ?  937  HOH   B O   1 
HETATM 6209 O  O   . HOH   J 5 .   ? 39.079 -4.126  22.632  1.00 22.79 ?  938  HOH   B O   1 
HETATM 6210 O  O   . HOH   J 5 .   ? 51.594 -23.565 19.492  1.00 24.24 ?  939  HOH   B O   1 
HETATM 6211 O  O   . HOH   J 5 .   ? 39.988 2.608   32.935  1.00 22.57 ?  940  HOH   B O   1 
HETATM 6212 O  O   . HOH   J 5 .   ? 54.314 -27.738 18.592  1.00 28.26 ?  941  HOH   B O   1 
HETATM 6213 O  O   . HOH   J 5 .   ? 53.357 7.710   44.462  1.00 19.58 ?  942  HOH   B O   1 
HETATM 6214 O  O   . HOH   J 5 .   ? 47.651 -4.512  39.571  1.00 25.27 ?  943  HOH   B O   1 
HETATM 6215 O  O   . HOH   J 5 .   ? 69.081 1.293   8.552   1.00 24.44 ?  944  HOH   B O   1 
HETATM 6216 O  O   . HOH   J 5 .   ? 39.666 8.337   26.848  1.00 34.87 ?  945  HOH   B O   1 
HETATM 6217 O  O   . HOH   J 5 .   ? 56.360 -25.793 20.025  1.00 34.35 ?  946  HOH   B O   1 
HETATM 6218 O  O   . HOH   J 5 .   ? 70.446 -12.975 13.933  1.00 22.12 ?  947  HOH   B O   1 
HETATM 6219 O  O   . HOH   J 5 .   ? 49.260 5.225   23.938  1.00 11.52 ?  948  HOH   B O   1 
HETATM 6220 O  O   . HOH   J 5 .   ? 74.689 -3.772  27.333  1.00 21.79 ?  949  HOH   B O   1 
HETATM 6221 O  O   . HOH   J 5 .   ? 74.399 -4.972  29.999  1.00 41.45 ?  950  HOH   B O   1 
HETATM 6222 O  O   . HOH   J 5 .   ? 66.332 15.741  17.321  1.00 25.09 ?  951  HOH   B O   1 
HETATM 6223 O  O   . HOH   J 5 .   ? 56.622 -6.392  38.655  1.00 28.74 ?  952  HOH   B O   1 
HETATM 6224 O  O   . HOH   J 5 .   ? 38.533 -1.296  2.840   1.00 14.95 ?  953  HOH   B O   1 
HETATM 6225 O  O   . HOH   J 5 .   ? 40.079 10.305  32.116  1.00 30.72 ?  954  HOH   B O   1 
HETATM 6226 O  O   . HOH   J 5 .   ? 51.659 7.153   27.584  1.00 11.57 ?  955  HOH   B O   1 
HETATM 6227 O  O   . HOH   J 5 .   ? 54.791 -8.345  21.598  1.00 12.65 ?  956  HOH   B O   1 
HETATM 6228 O  O   . HOH   J 5 .   ? 74.618 -1.457  30.179  1.00 28.13 ?  957  HOH   B O   1 
HETATM 6229 O  O   . HOH   J 5 .   ? 51.835 -11.251 37.281  1.00 15.27 ?  958  HOH   B O   1 
HETATM 6230 O  O   . HOH   J 5 .   ? 61.775 -0.259  40.237  1.00 19.83 ?  959  HOH   B O   1 
HETATM 6231 O  O   . HOH   J 5 .   ? 62.386 -8.395  35.700  1.00 20.65 ?  960  HOH   B O   1 
HETATM 6232 O  O   . HOH   J 5 .   ? 44.810 -10.510 8.490   1.00 15.88 ?  961  HOH   B O   1 
HETATM 6233 O  O   . HOH   J 5 .   ? 62.064 13.992  11.921  1.00 33.03 ?  962  HOH   B O   1 
HETATM 6234 O  O   . HOH   J 5 .   ? 50.633 2.985   34.546  1.00 12.79 ?  963  HOH   B O   1 
HETATM 6235 O  O   . HOH   J 5 .   ? 44.593 17.259  27.479  1.00 19.16 ?  964  HOH   B O   1 
HETATM 6236 O  O   . HOH   J 5 .   ? 69.729 -14.892 17.558  1.00 19.53 ?  965  HOH   B O   1 
HETATM 6237 O  O   . HOH   J 5 .   ? 37.462 -17.700 23.046  1.00 25.30 ?  966  HOH   B O   1 
HETATM 6238 O  O   . HOH   J 5 .   ? 50.533 -27.150 19.210  1.00 25.81 ?  967  HOH   B O   1 
HETATM 6239 O  O   . HOH   J 5 .   ? 63.443 19.981  22.769  1.00 22.11 ?  968  HOH   B O   1 
HETATM 6240 O  O   . HOH   J 5 .   ? 47.244 22.957  17.205  1.00 37.53 ?  969  HOH   B O   1 
HETATM 6241 O  O   . HOH   J 5 .   ? 43.394 -16.656 33.276  1.00 20.98 ?  970  HOH   B O   1 
HETATM 6242 O  O   . HOH   J 5 .   ? 42.725 11.074  12.224  1.00 27.89 ?  971  HOH   B O   1 
HETATM 6243 O  O   . HOH   J 5 .   ? 47.243 -11.155 25.922  1.00 11.15 ?  972  HOH   B O   1 
HETATM 6244 O  O   . HOH   J 5 .   ? 55.330 -9.796  7.812   1.00 12.89 ?  973  HOH   B O   1 
HETATM 6245 O  O   . HOH   J 5 .   ? 45.345 20.516  27.923  1.00 22.83 ?  974  HOH   B O   1 
HETATM 6246 O  O   . HOH   J 5 .   ? 68.385 2.600   34.414  1.00 12.84 ?  975  HOH   B O   1 
HETATM 6247 O  O   . HOH   J 5 .   ? 63.110 7.196   10.311  1.00 17.31 ?  976  HOH   B O   1 
HETATM 6248 O  O   . HOH   J 5 .   ? 39.490 -22.315 23.037  1.00 35.10 ?  977  HOH   B O   1 
HETATM 6249 O  O   . HOH   J 5 .   ? 50.681 24.440  32.357  1.00 23.82 ?  978  HOH   B O   1 
HETATM 6250 O  O   . HOH   J 5 .   ? 53.424 -12.966 38.899  1.00 19.82 ?  979  HOH   B O   1 
HETATM 6251 O  O   . HOH   J 5 .   ? 45.071 -28.337 36.456  1.00 19.13 ?  980  HOH   B O   1 
HETATM 6252 O  O   . HOH   J 5 .   ? 61.314 -21.410 18.671  1.00 18.59 ?  981  HOH   B O   1 
HETATM 6253 O  O   . HOH   J 5 .   ? 50.439 -21.675 24.796  1.00 13.15 ?  982  HOH   B O   1 
HETATM 6254 O  O   . HOH   J 5 .   ? 54.560 -1.955  -3.963  1.00 22.27 ?  983  HOH   B O   1 
HETATM 6255 O  O   . HOH   J 5 .   ? 53.013 1.170   38.374  1.00 13.34 ?  984  HOH   B O   1 
HETATM 6256 O  O   . HOH   J 5 .   ? 55.619 14.332  44.198  1.00 35.24 ?  985  HOH   B O   1 
HETATM 6257 O  O   . HOH   J 5 .   ? 55.032 -26.731 33.241  1.00 20.51 ?  986  HOH   B O   1 
HETATM 6258 O  O   . HOH   J 5 .   ? 40.319 -1.083  7.683   1.00 13.79 ?  987  HOH   B O   1 
HETATM 6259 O  O   . HOH   J 5 .   ? 59.408 1.766   1.949   1.00 18.56 ?  988  HOH   B O   1 
HETATM 6260 O  O   . HOH   J 5 .   ? 62.265 15.497  41.258  1.00 28.21 ?  989  HOH   B O   1 
HETATM 6261 O  O   . HOH   J 5 .   ? 58.675 -0.954  27.083  1.00 10.28 ?  990  HOH   B O   1 
HETATM 6262 O  O   . HOH   J 5 .   ? 38.091 -11.549 31.354  1.00 26.52 ?  991  HOH   B O   1 
HETATM 6263 O  O   . HOH   J 5 .   ? 44.237 23.483  30.811  1.00 32.85 ?  992  HOH   B O   1 
HETATM 6264 O  O   . HOH   J 5 .   ? 69.985 17.365  24.114  1.00 19.54 ?  993  HOH   B O   1 
HETATM 6265 O  O   . HOH   J 5 .   ? 67.792 18.835  40.261  1.00 22.05 ?  994  HOH   B O   1 
HETATM 6266 O  O   . HOH   J 5 .   ? 49.820 -6.275  21.158  1.00 11.87 ?  995  HOH   B O   1 
HETATM 6267 O  O   . HOH   J 5 .   ? 68.719 -18.984 18.385  1.00 22.43 ?  996  HOH   B O   1 
HETATM 6268 O  O   . HOH   J 5 .   ? 57.524 3.223   -0.824  1.00 40.13 ?  997  HOH   B O   1 
HETATM 6269 O  O   . HOH   J 5 .   ? 63.839 -23.134 29.900  1.00 23.81 ?  998  HOH   B O   1 
HETATM 6270 O  O   . HOH   J 5 .   ? 70.469 -13.209 19.851  1.00 25.41 ?  999  HOH   B O   1 
HETATM 6271 O  O   . HOH   J 5 .   ? 41.396 17.136  19.744  1.00 31.23 ?  1000 HOH   B O   1 
HETATM 6272 O  O   . HOH   J 5 .   ? 50.259 3.818   38.929  1.00 16.02 ?  1001 HOH   B O   1 
HETATM 6273 O  O   . HOH   J 5 .   ? 57.748 11.873  8.065   1.00 17.81 ?  1002 HOH   B O   1 
HETATM 6274 O  O   . HOH   J 5 .   ? 61.239 7.462   5.144   1.00 36.63 ?  1003 HOH   B O   1 
HETATM 6275 O  O   . HOH   J 5 .   ? 51.482 2.484   47.500  1.00 30.44 ?  1004 HOH   B O   1 
HETATM 6276 O  O   . HOH   J 5 .   ? 45.419 -13.581 35.541  1.00 13.53 ?  1005 HOH   B O   1 
HETATM 6277 O  O   . HOH   J 5 .   ? 50.898 -16.872 8.351   1.00 17.90 ?  1006 HOH   B O   1 
HETATM 6278 O  O   . HOH   J 5 .   ? 64.347 20.818  28.669  1.00 21.34 ?  1007 HOH   B O   1 
HETATM 6279 O  O   . HOH   J 5 .   ? 57.644 -5.339  25.019  1.00 12.56 ?  1008 HOH   B O   1 
HETATM 6280 O  O   . HOH   J 5 .   ? 41.012 -5.051  4.691   1.00 23.17 ?  1009 HOH   B O   1 
HETATM 6281 O  O   . HOH   J 5 .   ? 38.092 6.096   17.694  1.00 19.77 ?  1010 HOH   B O   1 
HETATM 6282 O  O   . HOH   J 5 .   ? 42.418 -18.317 27.447  1.00 26.91 ?  1011 HOH   B O   1 
HETATM 6283 O  O   . HOH   J 5 .   ? 74.752 8.523   35.720  1.00 42.63 ?  1012 HOH   B O   1 
HETATM 6284 O  O   . HOH   J 5 .   ? 67.315 12.682  41.175  1.00 29.80 ?  1013 HOH   B O   1 
HETATM 6285 O  O   . HOH   J 5 .   ? 42.582 2.673   21.701  1.00 11.03 ?  1014 HOH   B O   1 
HETATM 6286 O  O   . HOH   J 5 .   ? 63.912 -2.779  41.460  1.00 33.60 ?  1015 HOH   B O   1 
HETATM 6287 O  O   . HOH   J 5 .   ? 42.916 6.628   26.402  1.00 13.17 ?  1016 HOH   B O   1 
HETATM 6288 O  O   . HOH   J 5 .   ? 72.355 13.638  19.302  1.00 22.74 ?  1017 HOH   B O   1 
HETATM 6289 O  O   . HOH   J 5 .   ? 40.805 -1.342  10.424  1.00 12.81 ?  1018 HOH   B O   1 
HETATM 6290 O  O   . HOH   J 5 .   ? 56.306 -17.573 35.208  1.00 15.73 ?  1019 HOH   B O   1 
HETATM 6291 O  O   . HOH   J 5 .   ? 76.831 4.192   33.866  1.00 24.61 ?  1020 HOH   B O   1 
HETATM 6292 O  O   . HOH   J 5 .   ? 80.205 -3.360  23.427  1.00 27.22 ?  1021 HOH   B O   1 
HETATM 6293 O  O   . HOH   J 5 .   ? 60.689 5.035   4.083   1.00 21.93 ?  1022 HOH   B O   1 
HETATM 6294 O  O   . HOH   J 5 .   ? 48.026 23.757  8.624   1.00 43.28 ?  1023 HOH   B O   1 
HETATM 6295 O  O   . HOH   J 5 .   ? 53.943 11.548  40.577  1.00 16.04 ?  1024 HOH   B O   1 
HETATM 6296 O  O   . HOH   J 5 .   ? 68.934 -7.304  31.994  1.00 18.46 ?  1025 HOH   B O   1 
HETATM 6297 O  O   . HOH   J 5 .   ? 44.468 14.493  9.889   1.00 25.51 ?  1026 HOH   B O   1 
HETATM 6298 O  O   . HOH   J 5 .   ? 56.781 7.160   44.899  1.00 20.21 ?  1027 HOH   B O   1 
HETATM 6299 O  O   . HOH   J 5 .   ? 76.550 1.960   25.929  1.00 19.83 ?  1028 HOH   B O   1 
HETATM 6300 O  O   . HOH   J 5 .   ? 60.045 -23.875 22.203  1.00 20.72 ?  1029 HOH   B O   1 
HETATM 6301 O  O   . HOH   J 5 .   ? 57.766 -25.766 33.624  1.00 19.86 ?  1030 HOH   B O   1 
HETATM 6302 O  O   . HOH   J 5 .   ? 72.650 -2.150  42.009  1.00 20.76 ?  1031 HOH   B O   1 
HETATM 6303 O  O   . HOH   J 5 .   ? 65.907 -9.588  9.010   1.00 18.64 ?  1032 HOH   B O   1 
HETATM 6304 O  O   . HOH   J 5 .   ? 74.269 -6.893  12.531  1.00 26.02 ?  1033 HOH   B O   1 
HETATM 6305 O  O   . HOH   J 5 .   ? 58.604 -26.611 29.171  1.00 20.06 ?  1034 HOH   B O   1 
HETATM 6306 O  O   . HOH   J 5 .   ? 75.901 4.425   40.296  1.00 18.67 ?  1035 HOH   B O   1 
HETATM 6307 O  O   . HOH   J 5 .   ? 54.845 -5.680  22.292  1.00 12.79 ?  1036 HOH   B O   1 
HETATM 6308 O  O   . HOH   J 5 .   ? 58.801 -16.014 7.305   1.00 23.08 ?  1037 HOH   B O   1 
HETATM 6309 O  O   . HOH   J 5 .   ? 68.340 19.073  23.029  1.00 30.18 ?  1038 HOH   B O   1 
HETATM 6310 O  O   . HOH   J 5 .   ? 65.423 0.819   33.042  1.00 12.57 ?  1039 HOH   B O   1 
HETATM 6311 O  O   . HOH   J 5 .   ? 50.188 15.055  35.623  1.00 14.99 ?  1040 HOH   B O   1 
HETATM 6312 O  O   . HOH   J 5 .   ? 44.322 8.539   18.672  1.00 14.51 ?  1041 HOH   B O   1 
HETATM 6313 O  O   . HOH   J 5 .   ? 44.247 -0.903  -1.000  1.00 35.77 ?  1042 HOH   B O   1 
HETATM 6314 O  O   . HOH   J 5 .   ? 44.495 15.686  22.696  1.00 15.75 ?  1043 HOH   B O   1 
HETATM 6315 O  O   . HOH   J 5 .   ? 52.698 -15.198 39.766  1.00 24.79 ?  1044 HOH   B O   1 
HETATM 6316 O  O   . HOH   J 5 .   ? 76.296 21.389  33.084  1.00 27.30 ?  1045 HOH   B O   1 
HETATM 6317 O  O   . HOH   J 5 .   ? 75.357 4.355   27.096  1.00 24.85 ?  1046 HOH   B O   1 
HETATM 6318 O  O   . HOH   J 5 .   ? 42.665 -23.780 21.304  1.00 27.99 ?  1047 HOH   B O   1 
HETATM 6319 O  O   . HOH   J 5 .   ? 46.445 -13.266 40.142  1.00 35.61 ?  1048 HOH   B O   1 
HETATM 6320 O  O   . HOH   J 5 .   ? 55.526 -29.288 20.740  1.00 36.42 ?  1049 HOH   B O   1 
HETATM 6321 O  O   . HOH   J 5 .   ? 55.347 -0.126  37.650  1.00 14.54 ?  1050 HOH   B O   1 
HETATM 6322 O  O   . HOH   J 5 .   ? 45.912 7.054   9.430   1.00 25.58 ?  1051 HOH   B O   1 
HETATM 6323 O  O   . HOH   J 5 .   ? 62.625 8.760   36.338  1.00 13.45 ?  1052 HOH   B O   1 
HETATM 6324 O  O   . HOH   J 5 .   ? 67.484 -18.015 30.908  1.00 27.62 ?  1053 HOH   B O   1 
HETATM 6325 O  O   . HOH   J 5 .   ? 39.668 5.618   11.000  1.00 24.49 ?  1054 HOH   B O   1 
HETATM 6326 O  O   . HOH   J 5 .   ? 56.967 18.611  21.116  1.00 17.85 ?  1055 HOH   B O   1 
HETATM 6327 O  O   . HOH   J 5 .   ? 57.840 -15.444 39.672  1.00 24.28 ?  1056 HOH   B O   1 
HETATM 6328 O  O   . HOH   J 5 .   ? 55.187 11.581  44.134  1.00 39.62 ?  1057 HOH   B O   1 
HETATM 6329 O  O   . HOH   J 5 .   ? 67.563 -16.522 15.070  1.00 26.14 ?  1058 HOH   B O   1 
HETATM 6330 O  O   . HOH   J 5 .   ? 38.422 9.027   24.936  1.00 28.57 ?  1059 HOH   B O   1 
HETATM 6331 O  O   . HOH   J 5 .   ? 44.243 -18.672 31.379  1.00 16.23 ?  1060 HOH   B O   1 
HETATM 6332 O  O   . HOH   J 5 .   ? 41.186 8.133   5.764   1.00 36.61 ?  1061 HOH   B O   1 
HETATM 6333 O  O   . HOH   J 5 .   ? 68.418 -8.652  29.601  1.00 16.81 ?  1062 HOH   B O   1 
HETATM 6334 O  O   . HOH   J 5 .   ? 51.794 -29.304 29.254  1.00 27.62 ?  1063 HOH   B O   1 
HETATM 6335 O  O   . HOH   J 5 .   ? 58.994 -23.848 35.037  1.00 30.95 ?  1064 HOH   B O   1 
HETATM 6336 O  O   . HOH   J 5 .   ? 48.808 -26.859 21.001  1.00 27.13 ?  1065 HOH   B O   1 
HETATM 6337 O  O   . HOH   J 5 .   ? 41.678 8.179   18.321  1.00 14.89 ?  1066 HOH   B O   1 
HETATM 6338 O  O   . HOH   J 5 .   ? 40.566 -11.290 23.829  1.00 15.38 ?  1067 HOH   B O   1 
HETATM 6339 O  O   . HOH   J 5 .   ? 52.810 10.436  44.153  1.00 35.33 ?  1068 HOH   B O   1 
HETATM 6340 O  O   . HOH   J 5 .   ? 45.540 23.570  33.676  1.00 34.70 ?  1069 HOH   B O   1 
HETATM 6341 O  O   . HOH   J 5 .   ? 40.005 -13.630 31.407  1.00 22.90 ?  1070 HOH   B O   1 
HETATM 6342 O  O   . HOH   J 5 .   ? 54.209 -11.593 25.064  1.00 10.87 ?  1071 HOH   B O   1 
HETATM 6343 O  O   . HOH   J 5 .   ? 52.393 -4.702  39.752  1.00 35.95 ?  1072 HOH   B O   1 
HETATM 6344 O  O   . HOH   J 5 .   ? 40.990 1.671   -0.118  1.00 17.44 ?  1073 HOH   B O   1 
HETATM 6345 O  O   . HOH   J 5 .   ? 73.911 -4.208  38.499  1.00 41.96 ?  1074 HOH   B O   1 
HETATM 6346 O  O   . HOH   J 5 .   ? 43.465 -23.540 24.050  1.00 19.17 ?  1075 HOH   B O   1 
HETATM 6347 O  O   . HOH   J 5 .   ? 54.111 14.736  39.692  1.00 38.67 ?  1076 HOH   B O   1 
HETATM 6348 O  O   . HOH   J 5 .   ? 69.311 -4.165  34.609  1.00 23.47 ?  1077 HOH   B O   1 
HETATM 6349 O  O   . HOH   J 5 .   ? 40.162 -13.730 22.735  1.00 15.50 ?  1078 HOH   B O   1 
HETATM 6350 O  O   . HOH   J 5 .   ? 66.562 -20.714 26.926  1.00 22.90 ?  1079 HOH   B O   1 
HETATM 6351 O  O   . HOH   J 5 .   ? 53.795 -19.568 37.180  1.00 18.34 ?  1080 HOH   B O   1 
HETATM 6352 O  O   . HOH   J 5 .   ? 55.347 22.757  31.459  1.00 33.72 ?  1081 HOH   B O   1 
HETATM 6353 O  O   . HOH   J 5 .   ? 44.745 17.733  38.901  1.00 37.00 ?  1082 HOH   B O   1 
HETATM 6354 O  O   . HOH   J 5 .   ? 40.271 -17.909 29.725  1.00 24.90 ?  1083 HOH   B O   1 
HETATM 6355 O  O   . HOH   J 5 .   ? 67.484 -19.005 34.115  1.00 28.21 ?  1084 HOH   B O   1 
HETATM 6356 O  O   . HOH   J 5 .   ? 37.566 1.742   31.880  1.00 18.11 ?  1085 HOH   B O   1 
HETATM 6357 O  O   . HOH   J 5 .   ? 62.720 -19.906 14.601  1.00 23.35 ?  1086 HOH   B O   1 
HETATM 6358 O  O   . HOH   J 5 .   ? 56.443 -11.888 23.219  1.00 12.23 ?  1087 HOH   B O   1 
HETATM 6359 O  O   . HOH   J 5 .   ? 66.501 5.379   41.371  1.00 20.26 ?  1088 HOH   B O   1 
HETATM 6360 O  O   . HOH   J 5 .   ? 77.367 -8.630  20.876  1.00 27.19 ?  1089 HOH   B O   1 
HETATM 6361 O  O   . HOH   J 5 .   ? 52.295 21.581  24.285  1.00 23.45 ?  1090 HOH   B O   1 
HETATM 6362 O  O   . HOH   J 5 .   ? 72.706 1.607   14.328  1.00 28.42 ?  1091 HOH   B O   1 
HETATM 6363 O  O   . HOH   J 5 .   ? 38.127 -12.870 18.389  1.00 21.29 ?  1092 HOH   B O   1 
HETATM 6364 O  O   . HOH   J 5 .   ? 54.186 0.406   45.156  1.00 23.03 ?  1093 HOH   B O   1 
HETATM 6365 O  O   . HOH   J 5 .   ? 41.564 -21.066 37.636  1.00 33.50 ?  1094 HOH   B O   1 
HETATM 6366 O  O   . HOH   J 5 .   ? 69.803 11.310  13.881  1.00 22.01 ?  1095 HOH   B O   1 
HETATM 6367 O  O   . HOH   J 5 .   ? 53.560 14.363  2.690   1.00 33.30 ?  1096 HOH   B O   1 
HETATM 6368 O  O   . HOH   J 5 .   ? 65.919 9.846   42.466  1.00 37.63 ?  1097 HOH   B O   1 
HETATM 6369 O  O   . HOH   J 5 .   ? 75.929 13.300  35.779  1.00 29.83 ?  1098 HOH   B O   1 
HETATM 6370 O  O   . HOH   J 5 .   ? 35.414 3.411   24.212  1.00 36.75 ?  1099 HOH   B O   1 
HETATM 6371 O  O   . HOH   J 5 .   ? 56.118 -16.364 37.830  1.00 20.18 ?  1100 HOH   B O   1 
HETATM 6372 O  O   . HOH   J 5 .   ? 80.124 -6.913  22.213  1.00 37.57 ?  1101 HOH   B O   1 
HETATM 6373 O  O   . HOH   J 5 .   ? 59.436 -1.793  44.712  1.00 29.95 ?  1102 HOH   B O   1 
HETATM 6374 O  O   . HOH   J 5 .   ? 46.974 -12.753 28.403  1.00 12.77 ?  1103 HOH   B O   1 
HETATM 6375 O  O   . HOH   J 5 .   ? 41.056 16.490  32.813  1.00 22.92 ?  1104 HOH   B O   1 
HETATM 6376 O  O   . HOH   J 5 .   ? 50.019 -20.047 18.005  1.00 26.86 ?  1105 HOH   B O   1 
HETATM 6377 O  O   . HOH   J 5 .   ? 51.730 -22.231 21.917  1.00 14.83 ?  1106 HOH   B O   1 
HETATM 6378 O  O   . HOH   J 5 .   ? 37.809 8.672   18.645  1.00 27.75 ?  1107 HOH   B O   1 
HETATM 6379 O  O   . HOH   J 5 .   ? 71.878 2.297   43.079  1.00 17.92 ?  1108 HOH   B O   1 
HETATM 6380 O  O   . HOH   J 5 .   ? 71.246 -10.404 27.966  1.00 36.58 ?  1109 HOH   B O   1 
HETATM 6381 O  O   . HOH   J 5 .   ? 40.279 -24.973 38.693  1.00 34.60 ?  1110 HOH   B O   1 
HETATM 6382 O  O   . HOH   J 5 .   ? 51.688 15.453  39.083  1.00 22.66 ?  1111 HOH   B O   1 
HETATM 6383 O  O   . HOH   J 5 .   ? 72.620 -9.329  24.102  1.00 21.93 ?  1112 HOH   B O   1 
HETATM 6384 O  O   . HOH   J 5 .   ? 44.673 16.123  16.145  1.00 26.52 ?  1113 HOH   B O   1 
HETATM 6385 O  O   . HOH   J 5 .   ? 50.195 25.667  34.666  1.00 33.84 ?  1114 HOH   B O   1 
HETATM 6386 O  O   . HOH   J 5 .   ? 46.493 11.690  34.618  1.00 16.18 ?  1115 HOH   B O   1 
HETATM 6387 O  O   . HOH   J 5 .   ? 42.414 21.663  30.474  1.00 39.04 ?  1116 HOH   B O   1 
HETATM 6388 O  O   . HOH   J 5 .   ? 49.284 -11.152 5.566   1.00 28.81 ?  1117 HOH   B O   1 
HETATM 6389 O  O   . HOH   J 5 .   ? 45.078 17.303  10.268  1.00 29.27 ?  1118 HOH   B O   1 
HETATM 6390 O  O   . HOH   J 5 .   ? 49.500 -10.169 3.507   1.00 41.83 ?  1119 HOH   B O   1 
HETATM 6391 O  O   . HOH   J 5 .   ? 56.470 -2.330  38.964  1.00 17.83 ?  1120 HOH   B O   1 
HETATM 6392 O  O   . HOH   J 5 .   ? 43.133 4.828   -0.075  1.00 38.23 ?  1121 HOH   B O   1 
HETATM 6393 O  O   . HOH   J 5 .   ? 38.029 -13.853 21.026  1.00 17.93 ?  1122 HOH   B O   1 
HETATM 6394 O  O   . HOH   J 5 .   ? 43.776 -7.941  8.099   1.00 17.66 ?  1123 HOH   B O   1 
HETATM 6395 O  O   . HOH   J 5 .   ? 44.851 -31.164 34.866  1.00 25.84 ?  1124 HOH   B O   1 
HETATM 6396 O  O   . HOH   J 5 .   ? 65.178 3.073   39.838  1.00 17.27 ?  1125 HOH   B O   1 
HETATM 6397 O  O   . HOH   J 5 .   ? 49.674 -13.026 7.603   1.00 17.09 ?  1126 HOH   B O   1 
HETATM 6398 O  O   . HOH   J 5 .   ? 54.480 20.152  15.939  1.00 34.55 ?  1127 HOH   B O   1 
HETATM 6399 O  O   . HOH   J 5 .   ? 48.516 -23.327 15.442  1.00 16.36 ?  1128 HOH   B O   1 
HETATM 6400 O  O   . HOH   J 5 .   ? 44.413 -11.028 37.694  1.00 18.90 ?  1129 HOH   B O   1 
HETATM 6401 O  O   . HOH   J 5 .   ? 56.438 -23.107 19.641  1.00 29.22 ?  1130 HOH   B O   1 
HETATM 6402 O  O   . HOH   J 5 .   ? 51.019 -18.428 16.272  1.00 22.95 ?  1131 HOH   B O   1 
HETATM 6403 O  O   . HOH   J 5 .   ? 39.796 5.206   4.014   1.00 16.07 ?  1132 HOH   B O   1 
HETATM 6404 O  O   . HOH   J 5 .   ? 43.912 0.907   36.636  1.00 24.04 ?  1133 HOH   B O   1 
HETATM 6405 O  O   . HOH   J 5 .   ? 75.219 10.692  26.946  1.00 43.24 ?  1134 HOH   B O   1 
HETATM 6406 O  O   . HOH   J 5 .   ? 70.545 10.219  18.034  1.00 18.78 ?  1135 HOH   B O   1 
HETATM 6407 O  O   . HOH   J 5 .   ? 64.136 6.503   44.231  1.00 47.03 ?  1136 HOH   B O   1 
HETATM 6408 O  O   . HOH   J 5 .   ? 76.137 -9.982  13.454  1.00 25.79 ?  1137 HOH   B O   1 
HETATM 6409 O  O   . HOH   J 5 .   ? 40.624 3.584   11.905  1.00 27.15 ?  1138 HOH   B O   1 
HETATM 6410 O  O   . HOH   J 5 .   ? 63.494 -15.220 9.137   1.00 17.29 ?  1139 HOH   B O   1 
HETATM 6411 O  O   . HOH   J 5 .   ? 41.722 -16.935 17.846  1.00 31.32 ?  1140 HOH   B O   1 
HETATM 6412 O  O   . HOH   J 5 .   ? 45.713 20.427  35.995  1.00 23.02 ?  1141 HOH   B O   1 
HETATM 6413 O  O   . HOH   J 5 .   ? 68.954 5.738   42.469  1.00 28.86 ?  1142 HOH   B O   1 
HETATM 6414 O  O   . HOH   J 5 .   ? 40.479 18.023  28.727  1.00 36.90 ?  1143 HOH   B O   1 
HETATM 6415 O  O   . HOH   J 5 .   ? 56.895 10.320  1.737   1.00 32.46 ?  1144 HOH   B O   1 
HETATM 6416 O  O   . HOH   J 5 .   ? 57.447 -1.246  -1.068  1.00 32.04 ?  1145 HOH   B O   1 
HETATM 6417 O  O   . HOH   J 5 .   ? 35.710 -6.855  16.166  1.00 18.49 ?  1146 HOH   B O   1 
HETATM 6418 O  O   . HOH   J 5 .   ? 78.080 3.819   24.343  1.00 25.72 ?  1147 HOH   B O   1 
HETATM 6419 O  O   . HOH   J 5 .   ? 69.382 9.288   8.251   1.00 38.94 ?  1148 HOH   B O   1 
HETATM 6420 O  O   . HOH   J 5 .   ? 49.720 -15.323 6.745   1.00 43.13 ?  1149 HOH   B O   1 
HETATM 6421 O  O   . HOH   J 5 .   ? 46.699 24.938  18.842  1.00 36.84 ?  1150 HOH   B O   1 
HETATM 6422 O  O   . HOH   J 5 .   ? 43.342 -7.274  5.448   1.00 34.87 ?  1151 HOH   B O   1 
HETATM 6423 O  O   . HOH   J 5 .   ? 62.157 -24.370 28.335  1.00 30.47 ?  1152 HOH   B O   1 
HETATM 6424 O  O   . HOH   J 5 .   ? 38.189 13.047  24.491  1.00 42.56 ?  1153 HOH   B O   1 
HETATM 6425 O  O   . HOH   J 5 .   ? 52.714 -7.024  1.999   1.00 18.69 ?  1154 HOH   B O   1 
HETATM 6426 O  O   . HOH   J 5 .   ? 56.301 17.702  15.971  1.00 20.73 ?  1155 HOH   B O   1 
HETATM 6427 O  O   . HOH   J 5 .   ? 66.562 2.309   3.626   1.00 24.98 ?  1156 HOH   B O   1 
HETATM 6428 O  O   . HOH   J 5 .   ? 54.540 12.819  38.539  1.00 38.65 ?  1157 HOH   B O   1 
HETATM 6429 O  O   . HOH   J 5 .   ? 63.673 -22.688 20.175  1.00 30.90 ?  1158 HOH   B O   1 
HETATM 6430 O  O   . HOH   J 5 .   ? 39.393 7.166   33.205  1.00 40.75 ?  1159 HOH   B O   1 
HETATM 6431 O  O   . HOH   J 5 .   ? 66.732 15.621  42.313  1.00 39.53 ?  1160 HOH   B O   1 
HETATM 6432 O  O   . HOH   J 5 .   ? 74.482 22.300  30.948  1.00 29.68 ?  1161 HOH   B O   1 
HETATM 6433 O  O   . HOH   J 5 .   ? 61.169 -26.900 28.394  1.00 34.69 ?  1162 HOH   B O   1 
HETATM 6434 O  O   . HOH   J 5 .   ? 49.055 23.614  24.707  1.00 36.24 ?  1163 HOH   B O   1 
HETATM 6435 O  O   . HOH   J 5 .   ? 42.048 -19.164 18.042  1.00 32.19 ?  1164 HOH   B O   1 
HETATM 6436 O  O   . HOH   J 5 .   ? 64.854 -19.997 36.503  1.00 24.72 ?  1165 HOH   B O   1 
HETATM 6437 O  O   . HOH   J 5 .   ? 35.383 -6.880  22.598  1.00 30.73 ?  1166 HOH   B O   1 
HETATM 6438 O  O   . HOH   J 5 .   ? 68.495 -5.507  37.345  1.00 37.26 ?  1167 HOH   B O   1 
HETATM 6439 O  O   . HOH   J 5 .   ? 48.150 -0.057  -3.584  1.00 41.34 ?  1168 HOH   B O   1 
HETATM 6440 O  O   . HOH   J 5 .   ? 42.190 8.784   38.237  1.00 30.11 ?  1169 HOH   B O   1 
HETATM 6441 O  O   . HOH   J 5 .   ? 36.874 -5.964  13.833  1.00 17.42 ?  1170 HOH   B O   1 
HETATM 6442 O  O   . HOH   J 5 .   ? 38.782 -29.381 38.924  1.00 43.56 ?  1171 HOH   B O   1 
HETATM 6443 O  O   . HOH   J 5 .   ? 68.605 14.867  16.760  1.00 31.58 ?  1172 HOH   B O   1 
HETATM 6444 O  O   . HOH   J 5 .   ? 61.420 -10.846 37.374  1.00 20.98 ?  1173 HOH   B O   1 
HETATM 6445 O  O   . HOH   J 5 .   ? 49.616 6.124   1.291   1.00 31.24 ?  1174 HOH   B O   1 
HETATM 6446 O  O   . HOH   J 5 .   ? 48.234 -24.956 19.760  1.00 31.02 ?  1175 HOH   B O   1 
HETATM 6447 O  O   . HOH   J 5 .   ? 40.734 -29.711 31.845  1.00 20.94 ?  1176 HOH   B O   1 
HETATM 6448 O  O   . HOH   J 5 .   ? 60.698 2.722   -0.262  1.00 44.78 ?  1177 HOH   B O   1 
HETATM 6449 O  O   . HOH   J 5 .   ? 56.320 19.563  42.921  1.00 35.02 ?  1178 HOH   B O   1 
HETATM 6450 O  O   . HOH   J 5 .   ? 40.340 -6.901  10.714  1.00 19.00 ?  1179 HOH   B O   1 
HETATM 6451 O  O   . HOH   J 5 .   ? 42.630 1.091   -2.106  1.00 25.09 ?  1180 HOH   B O   1 
HETATM 6452 O  O   . HOH   J 5 .   ? 79.773 2.250   23.647  1.00 44.56 ?  1181 HOH   B O   1 
HETATM 6453 O  O   . HOH   J 5 .   ? 48.334 -1.259  0.341   1.00 19.50 ?  1182 HOH   B O   1 
HETATM 6454 O  O   . HOH   J 5 .   ? 72.679 -9.985  11.253  1.00 48.82 ?  1183 HOH   B O   1 
HETATM 6455 O  O   . HOH   J 5 .   ? 77.322 0.296   27.965  1.00 28.29 ?  1184 HOH   B O   1 
HETATM 6456 O  O   . HOH   J 5 .   ? 44.020 19.497  22.817  1.00 30.01 ?  1185 HOH   B O   1 
HETATM 6457 O  O   . HOH   J 5 .   ? 42.319 -9.615  32.383  1.00 20.72 ?  1186 HOH   B O   1 
HETATM 6458 O  O   . HOH   J 5 .   ? 64.526 -4.466  2.177   1.00 40.42 ?  1187 HOH   B O   1 
HETATM 6459 O  O   . HOH   J 5 .   ? 59.529 20.558  40.678  1.00 32.53 ?  1188 HOH   B O   1 
HETATM 6460 O  O   . HOH   J 5 .   ? 74.595 8.662   27.858  1.00 26.34 ?  1189 HOH   B O   1 
HETATM 6461 O  O   . HOH   J 5 .   ? 44.262 -13.598 38.950  1.00 39.47 ?  1190 HOH   B O   1 
HETATM 6462 O  O   . HOH   J 5 .   ? 57.029 -19.387 12.030  1.00 25.75 ?  1191 HOH   B O   1 
HETATM 6463 O  O   . HOH   J 5 .   ? 65.136 22.373  30.925  1.00 43.07 ?  1192 HOH   B O   1 
HETATM 6464 O  O   . HOH   J 5 .   ? 54.237 17.246  43.192  1.00 33.86 ?  1193 HOH   B O   1 
HETATM 6465 O  O   . HOH   J 5 .   ? 63.609 -28.565 23.837  1.00 40.32 ?  1194 HOH   B O   1 
HETATM 6466 O  O   . HOH   J 5 .   ? 60.993 9.305   2.903   1.00 41.73 ?  1195 HOH   B O   1 
HETATM 6467 O  O   . HOH   J 5 .   ? 72.829 6.655   8.674   1.00 36.00 ?  1196 HOH   B O   1 
HETATM 6468 O  O   . HOH   J 5 .   ? 64.934 -7.707  36.372  1.00 44.21 ?  1197 HOH   B O   1 
HETATM 6469 O  O   . HOH   J 5 .   ? 62.754 19.365  20.365  1.00 37.96 ?  1198 HOH   B O   1 
HETATM 6470 O  O   . HOH   J 5 .   ? 72.598 -12.711 12.561  1.00 40.00 ?  1199 HOH   B O   1 
HETATM 6471 O  O   . HOH   J 5 .   ? 66.162 -17.317 12.792  1.00 40.25 ?  1200 HOH   B O   1 
HETATM 6472 O  O   . HOH   J 5 .   ? 42.157 -2.724  1.846   1.00 32.73 ?  1201 HOH   B O   1 
HETATM 6473 O  O   . HOH   J 5 .   ? 69.987 19.727  21.208  1.00 42.91 ?  1202 HOH   B O   1 
HETATM 6474 O  O   . HOH   J 5 .   ? 73.495 -5.440  36.278  1.00 34.97 ?  1203 HOH   B O   1 
HETATM 6475 O  O   . HOH   J 5 .   ? 41.698 0.287   -4.490  1.00 22.14 ?  1204 HOH   B O   1 
HETATM 6476 O  O   . HOH   J 5 .   ? 45.908 -25.414 19.051  1.00 34.02 ?  1205 HOH   B O   1 
HETATM 6477 O  O   . HOH   J 5 .   ? 43.945 -1.827  38.020  1.00 37.27 ?  1206 HOH   B O   1 
HETATM 6478 O  O   . HOH   J 5 .   ? 40.491 7.612   15.689  1.00 29.87 ?  1207 HOH   B O   1 
HETATM 6479 O  O   . HOH   J 5 .   ? 68.676 2.053   4.933   1.00 40.93 ?  1208 HOH   B O   1 
HETATM 6480 O  O   . HOH   J 5 .   ? 41.044 21.242  13.609  1.00 35.47 ?  1209 HOH   B O   1 
HETATM 6481 O  O   . HOH   J 5 .   ? 78.155 8.458   23.194  1.00 38.02 ?  1210 HOH   B O   1 
HETATM 6482 O  O   . HOH   J 5 .   ? 52.596 -20.715 41.235  1.00 32.56 ?  1211 HOH   B O   1 
HETATM 6483 O  O   . HOH   J 5 .   ? 43.487 17.160  24.798  1.00 36.90 ?  1212 HOH   B O   1 
HETATM 6484 O  O   . HOH   J 5 .   ? 59.250 20.723  43.710  1.00 41.13 ?  1213 HOH   B O   1 
HETATM 6485 O  O   . HOH   J 5 .   ? 73.930 9.714   34.039  1.00 33.48 ?  1214 HOH   B O   1 
HETATM 6486 O  O   . HOH   J 5 .   ? 42.406 -12.428 32.119  1.00 32.48 ?  1215 HOH   B O   1 
HETATM 6487 O  O   . HOH   J 5 .   ? 42.336 -31.177 33.773  1.00 45.28 ?  1216 HOH   B O   1 
HETATM 6488 O  O   . HOH   J 5 .   ? 66.599 -20.769 29.545  1.00 43.39 ?  1217 HOH   B O   1 
HETATM 6489 O  O   . HOH   J 5 .   ? 69.454 -20.835 33.899  1.00 45.37 ?  1218 HOH   B O   1 
HETATM 6490 O  O   . HOH   J 5 .   ? 43.864 17.539  20.746  1.00 25.51 ?  1219 HOH   B O   1 
HETATM 6491 O  O   . HOH   J 5 .   ? 40.441 -15.930 31.788  1.00 36.22 ?  1220 HOH   B O   1 
HETATM 6492 O  O   . HOH   J 5 .   ? 48.593 20.197  39.862  1.00 30.76 ?  1221 HOH   B O   1 
HETATM 6493 O  O   . HOH   J 5 .   ? 56.793 -28.245 24.669  1.00 32.54 ?  1222 HOH   B O   1 
HETATM 6494 O  O   . HOH   J 5 .   ? 41.193 -13.624 10.572  1.00 39.85 ?  1223 HOH   B O   1 
HETATM 6495 O  O   . HOH   J 5 .   ? 36.428 0.019   22.065  1.00 15.95 ?  1224 HOH   B O   1 
HETATM 6496 O  O   . HOH   J 5 .   ? 55.998 22.373  24.890  1.00 44.09 ?  1225 HOH   B O   1 
HETATM 6497 O  O   . HOH   J 5 .   ? 70.371 4.307   44.227  1.00 36.17 ?  1226 HOH   B O   1 
HETATM 6498 O  O   . HOH   J 5 .   ? 40.727 11.490  34.326  1.00 34.41 ?  1227 HOH   B O   1 
HETATM 6499 O  O   . HOH   J 5 .   ? 57.947 -25.799 22.261  1.00 29.63 ?  1228 HOH   B O   1 
HETATM 6500 O  O   . HOH   J 5 .   ? 48.670 -18.453 7.935   1.00 28.17 ?  1229 HOH   B O   1 
HETATM 6501 O  O   . HOH   J 5 .   ? 38.630 -32.650 36.998  1.00 35.31 ?  1230 HOH   B O   1 
HETATM 6502 O  O   . HOH   J 5 .   ? 46.149 20.652  38.971  1.00 42.95 ?  1231 HOH   B O   1 
HETATM 6503 O  O   . HOH   J 5 .   ? 64.737 21.526  37.738  1.00 42.11 ?  1232 HOH   B O   1 
HETATM 6504 O  O   . HOH   J 5 .   ? 46.195 -11.531 6.424   1.00 30.11 ?  1233 HOH   B O   1 
HETATM 6505 O  O   . HOH   J 5 .   ? 48.961 -3.828  -0.538  1.00 39.55 ?  1234 HOH   B O   1 
HETATM 6506 O  O   . HOH   J 5 .   ? 46.397 13.962  41.579  1.00 44.40 ?  1235 HOH   B O   1 
HETATM 6507 O  O   . HOH   J 5 .   ? 36.025 8.649   20.819  1.00 29.19 ?  1236 HOH   B O   1 
HETATM 6508 O  O   . HOH   J 5 .   ? 44.369 22.873  35.858  1.00 38.43 ?  1237 HOH   B O   1 
HETATM 6509 O  O   . HOH   J 5 .   ? 44.608 24.223  37.924  1.00 27.13 ?  1238 HOH   B O   1 
HETATM 6510 O  O   . HOH   J 5 .   ? 37.857 11.518  13.795  1.00 39.83 ?  1239 HOH   B O   1 
HETATM 6511 O  O   . HOH   J 5 .   ? 60.279 12.571  7.414   1.00 31.54 ?  1240 HOH   B O   1 
HETATM 6512 O  O   . HOH   J 5 .   ? 59.977 -0.338  -0.002  1.00 36.81 ?  1241 HOH   B O   1 
HETATM 6513 O  O   . HOH   J 5 .   ? 42.801 -12.538 34.756  1.00 38.16 ?  1242 HOH   B O   1 
HETATM 6514 O  O   . HOH   J 5 .   ? 52.083 3.373   36.941  1.00 15.44 ?  1243 HOH   B O   1 
HETATM 6515 O  O   . HOH   J 5 .   ? 49.194 -1.578  -4.975  1.00 36.35 ?  1244 HOH   B O   1 
HETATM 6516 O  O   . HOH   J 5 .   ? 76.259 9.166   38.319  1.00 21.91 ?  1245 HOH   B O   1 
HETATM 6517 O  O   . HOH   J 5 .   ? 51.371 -4.648  -1.198  1.00 40.72 ?  1246 HOH   B O   1 
HETATM 6518 O  O   . HOH   J 5 .   ? 70.631 -15.254 21.337  1.00 41.17 ?  1247 HOH   B O   1 
HETATM 6519 O  O   . HOH   J 5 .   ? 75.485 2.529   42.522  1.00 20.77 ?  1248 HOH   B O   1 
HETATM 6520 O  O   . HOH   J 5 .   ? 61.931 13.341  44.849  1.00 28.52 ?  1249 HOH   B O   1 
HETATM 6521 O  O   . HOH   J 5 .   ? 52.850 -18.785 7.323   1.00 28.04 ?  1250 HOH   B O   1 
HETATM 6522 O  O   . HOH   J 5 .   ? 39.865 -32.014 35.134  1.00 39.95 ?  1251 HOH   B O   1 
HETATM 6523 O  O   . HOH   J 5 .   ? 77.072 -2.572  28.084  1.00 41.72 ?  1252 HOH   B O   1 
HETATM 6524 O  O   . HOH   J 5 .   ? 46.558 -0.767  -2.174  1.00 43.77 ?  1253 HOH   B O   1 
HETATM 6525 O  O   . HOH   J 5 .   ? 38.273 -7.833  12.439  1.00 45.02 ?  1254 HOH   B O   1 
HETATM 6526 O  O   . HOH   J 5 .   ? 38.070 5.730   31.126  1.00 39.35 ?  1255 HOH   B O   1 
HETATM 6527 O  O   . HOH   J 5 .   ? 40.293 -15.214 12.387  1.00 34.79 ?  1256 HOH   B O   1 
HETATM 6528 O  O   . HOH   J 5 .   ? 39.779 -10.129 9.569   1.00 49.46 ?  1257 HOH   B O   1 
HETATM 6529 O  O   . HOH   J 5 .   ? 47.528 -7.457  -2.026  1.00 33.46 ?  1258 HOH   B O   1 
HETATM 6530 O  O   . HOH   J 5 .   ? 41.060 -8.295  8.086   1.00 34.33 ?  1259 HOH   B O   1 
HETATM 6531 O  O   . HOH   J 5 .   ? 70.295 13.482  17.748  1.00 43.04 ?  1260 HOH   B O   1 
HETATM 6532 O  O   . HOH   J 5 .   ? 64.926 -22.367 37.971  1.00 37.14 ?  1261 HOH   B O   1 
HETATM 6533 O  O   . HOH   J 5 .   ? 42.300 -11.882 9.316   1.00 36.93 ?  1262 HOH   B O   1 
HETATM 6534 O  O   . HOH   J 5 .   ? 49.317 6.239   -1.342  1.00 32.32 ?  1263 HOH   B O   1 
HETATM 6535 O  O   . HOH   J 5 .   ? 45.820 -10.451 40.621  1.00 44.40 ?  1264 HOH   B O   1 
HETATM 6536 O  O   . HOH   J 5 .   ? 50.021 17.320  40.331  1.00 30.77 ?  1265 HOH   B O   1 
HETATM 6537 O  O   . HOH   J 5 .   ? 71.096 -19.094 26.485  1.00 39.49 ?  1266 HOH   B O   1 
HETATM 6538 O  O   . HOH   J 5 .   ? 49.558 -22.749 17.959  1.00 35.30 ?  1267 HOH   B O   1 
HETATM 6539 O  O   . HOH   J 5 .   ? 48.275 -4.835  42.384  1.00 32.27 ?  1268 HOH   B O   1 
HETATM 6540 O  O   . HOH   J 5 .   ? 45.386 -36.898 31.541  1.00 40.25 ?  1269 HOH   B O   1 
HETATM 6541 O  O   . HOH   J 5 .   ? 55.035 -4.499  39.428  1.00 27.09 ?  1270 HOH   B O   1 
HETATM 6542 O  O   . HOH   J 5 .   ? 60.599 22.646  39.888  1.00 42.99 ?  1271 HOH   B O   1 
HETATM 6543 O  O   . HOH   J 5 .   ? 47.745 7.834   5.046   1.00 38.26 ?  1272 HOH   B O   1 
HETATM 6544 O  O   . HOH   J 5 .   ? 62.910 9.029   6.425   1.00 32.01 ?  1273 HOH   B O   1 
HETATM 6545 O  O   . HOH   J 5 .   ? 62.936 12.858  42.550  1.00 29.69 ?  1274 HOH   B O   1 
HETATM 6546 O  O   . HOH   J 5 .   ? 41.837 18.477  34.177  1.00 41.00 ?  1275 HOH   B O   1 
HETATM 6547 O  O   . HOH   J 5 .   ? 54.006 -17.456 39.067  1.00 21.17 ?  1276 HOH   B O   1 
HETATM 6548 O  O   . HOH   J 5 .   ? 50.539 -7.409  0.397   1.00 33.66 ?  1277 HOH   B O   1 
HETATM 6549 O  O   . HOH   J 5 .   ? 56.989 -22.958 38.826  1.00 41.41 ?  1278 HOH   B O   1 
HETATM 6550 O  O   . HOH   J 5 .   ? 39.916 -3.680  2.721   1.00 23.12 ?  1279 HOH   B O   1 
HETATM 6551 O  O   . HOH   J 5 .   ? 56.029 21.014  20.264  1.00 33.28 ?  1280 HOH   B O   1 
HETATM 6552 O  O   . HOH   J 5 .   ? 64.331 8.896   8.415   1.00 35.24 ?  1281 HOH   B O   1 
HETATM 6553 O  O   . HOH   J 5 .   ? 40.818 18.338  36.536  1.00 36.51 ?  1282 HOH   B O   1 
HETATM 6554 O  O   . HOH   J 5 .   ? 35.645 -1.931  23.828  1.00 23.45 ?  1283 HOH   B O   1 
HETATM 6555 O  O   . HOH   J 5 .   ? 58.751 -10.610 38.658  1.00 25.89 ?  1284 HOH   B O   1 
HETATM 6556 O  O   . HOH   J 5 .   ? 74.080 -11.573 23.966  1.00 30.16 ?  1285 HOH   B O   1 
HETATM 6557 O  O   . HOH   J 5 .   ? 66.804 21.156  39.531  1.00 38.04 ?  1286 HOH   B O   1 
HETATM 6558 O  O   . HOH   J 5 .   ? 71.065 -8.515  33.540  1.00 39.25 ?  1287 HOH   B O   1 
HETATM 6559 O  O   . HOH   J 5 .   ? 47.179 8.358   7.325   1.00 35.94 ?  1288 HOH   B O   1 
HETATM 6560 O  O   . HOH   J 5 .   ? 42.036 -2.747  -0.562  1.00 27.78 ?  1289 HOH   B O   1 
HETATM 6561 O  O   . HOH   J 5 .   ? 52.875 -8.286  37.676  1.00 45.89 ?  1290 HOH   B O   1 
HETATM 6562 O  O   . HOH   J 5 .   ? 39.193 17.047  30.787  1.00 34.63 ?  1291 HOH   B O   1 
HETATM 6563 O  O   . HOH   J 5 .   ? 62.603 23.357  41.444  1.00 42.41 ?  1292 HOH   B O   1 
HETATM 6564 O  O   . HOH   J 5 .   ? 64.916 3.683   43.053  1.00 37.03 ?  1293 HOH   B O   1 
HETATM 6565 O  O   . HOH   J 5 .   ? 51.746 -23.297 42.701  1.00 31.10 ?  1294 HOH   B O   1 
HETATM 6566 O  O   . HOH   J 5 .   ? 37.539 -16.377 20.714  1.00 33.77 ?  1295 HOH   B O   1 
HETATM 6567 O  O   . HOH   J 5 .   ? 53.423 23.433  26.155  1.00 40.70 ?  1296 HOH   B O   1 
HETATM 6568 O  O   . HOH   J 5 .   ? 73.988 3.243   44.467  1.00 27.45 ?  1297 HOH   B O   1 
HETATM 6569 O  O   . HOH   J 5 .   ? 45.631 13.568  7.662   1.00 37.62 ?  1298 HOH   B O   1 
HETATM 6570 O  O   . HOH   J 5 .   ? 47.267 -3.823  44.069  1.00 41.61 ?  1299 HOH   B O   1 
HETATM 6571 O  O   . HOH   J 5 .   ? 52.689 -21.699 38.493  1.00 26.87 ?  1300 HOH   B O   1 
HETATM 6572 O  O   . HOH   J 5 .   ? 46.374 -3.321  -2.818  1.00 32.82 ?  1301 HOH   B O   1 
HETATM 6573 O  O   . HOH   J 5 .   ? 75.553 11.389  16.175  1.00 47.85 ?  1302 HOH   B O   1 
HETATM 6574 O  O   . HOH   J 5 .   ? 76.245 18.071  22.293  1.00 44.76 ?  1303 HOH   B O   1 
HETATM 6575 O  O   . HOH   J 5 .   ? 40.389 21.296  37.693  1.00 39.65 ?  1304 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 
5745 K K . K E . ? 0.1939 0.1676 0.1739 0.0030 -0.0309 -0.0175 803 K A K 
5771 K K . K H . ? 0.1630 0.1546 0.1277 0.0190 -0.0312 -0.0192 803 K B K 
# 
