data_9EGU
# 
_entry.id   9EGU 
# 
_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   9EGU         pdb_00009egu 10.2210/pdb9egu/pdb 
WWPDB D_1000290395 ?            ?                   
# 
_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                        9EGU 
_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 'N-hydroxy-4-({[(pyridin-3-yl)methyl](thiophene-3-sulfonyl)amino}methyl)benzamide' 403.475   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    564 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Histone Deacetylase 6' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;PITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRD
LNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITR
ESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAA
FHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSML
LGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRD
LNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITR
ESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAA
FHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSML
LGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-hydroxy-4-({[(pyridin-3-yl)methyl](thiophene-3-sulfonyl)amino}methyl)benzamide' A1BH9 
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 
A1BH9 non-polymer         . 'N-hydroxy-4-({[(pyridin-3-yl)methyl](thiophene-3-sulfonyl)amino}methyl)benzamide' ? 
'C18 H17 N3 O4 S2' 403.475 
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        A1BH9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BH9 
_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 A1BH9 1   801  401 A1BH9 LIG A . 
D 3 ZN    1   802  1   ZN    ZN  A . 
E 4 K     1   803  1   K     K   A . 
F 2 A1BH9 1   801  402 A1BH9 LIG B . 
G 3 ZN    1   802  2   ZN    ZN  B . 
H 4 K     1   803  2   K     K   B . 
I 5 HOH   1   901  233 HOH   HOH A . 
I 5 HOH   2   902  599 HOH   HOH A . 
I 5 HOH   3   903  604 HOH   HOH A . 
I 5 HOH   4   904  139 HOH   HOH A . 
I 5 HOH   5   905  538 HOH   HOH A . 
I 5 HOH   6   906  437 HOH   HOH A . 
I 5 HOH   7   907  61  HOH   HOH A . 
I 5 HOH   8   908  520 HOH   HOH A . 
I 5 HOH   9   909  261 HOH   HOH A . 
I 5 HOH   10  910  513 HOH   HOH A . 
I 5 HOH   11  911  630 HOH   HOH A . 
I 5 HOH   12  912  479 HOH   HOH A . 
I 5 HOH   13  913  191 HOH   HOH A . 
I 5 HOH   14  914  288 HOH   HOH A . 
I 5 HOH   15  915  557 HOH   HOH A . 
I 5 HOH   16  916  2   HOH   HOH A . 
I 5 HOH   17  917  372 HOH   HOH A . 
I 5 HOH   18  918  290 HOH   HOH A . 
I 5 HOH   19  919  6   HOH   HOH A . 
I 5 HOH   20  920  324 HOH   HOH A . 
I 5 HOH   21  921  591 HOH   HOH A . 
I 5 HOH   22  922  84  HOH   HOH A . 
I 5 HOH   23  923  453 HOH   HOH A . 
I 5 HOH   24  924  16  HOH   HOH A . 
I 5 HOH   25  925  44  HOH   HOH A . 
I 5 HOH   26  926  26  HOH   HOH A . 
I 5 HOH   27  927  264 HOH   HOH A . 
I 5 HOH   28  928  378 HOH   HOH A . 
I 5 HOH   29  929  54  HOH   HOH A . 
I 5 HOH   30  930  37  HOH   HOH A . 
I 5 HOH   31  931  374 HOH   HOH A . 
I 5 HOH   32  932  55  HOH   HOH A . 
I 5 HOH   33  933  404 HOH   HOH A . 
I 5 HOH   34  934  149 HOH   HOH A . 
I 5 HOH   35  935  210 HOH   HOH A . 
I 5 HOH   36  936  385 HOH   HOH A . 
I 5 HOH   37  937  77  HOH   HOH A . 
I 5 HOH   38  938  99  HOH   HOH A . 
I 5 HOH   39  939  40  HOH   HOH A . 
I 5 HOH   40  940  514 HOH   HOH A . 
I 5 HOH   41  941  623 HOH   HOH A . 
I 5 HOH   42  942  262 HOH   HOH A . 
I 5 HOH   43  943  92  HOH   HOH A . 
I 5 HOH   44  944  3   HOH   HOH A . 
I 5 HOH   45  945  142 HOH   HOH A . 
I 5 HOH   46  946  21  HOH   HOH A . 
I 5 HOH   47  947  89  HOH   HOH A . 
I 5 HOH   48  948  141 HOH   HOH A . 
I 5 HOH   49  949  564 HOH   HOH A . 
I 5 HOH   50  950  380 HOH   HOH A . 
I 5 HOH   51  951  291 HOH   HOH A . 
I 5 HOH   52  952  10  HOH   HOH A . 
I 5 HOH   53  953  432 HOH   HOH A . 
I 5 HOH   54  954  449 HOH   HOH A . 
I 5 HOH   55  955  29  HOH   HOH A . 
I 5 HOH   56  956  417 HOH   HOH A . 
I 5 HOH   57  957  49  HOH   HOH A . 
I 5 HOH   58  958  183 HOH   HOH A . 
I 5 HOH   59  959  541 HOH   HOH A . 
I 5 HOH   60  960  287 HOH   HOH A . 
I 5 HOH   61  961  420 HOH   HOH A . 
I 5 HOH   62  962  5   HOH   HOH A . 
I 5 HOH   63  963  13  HOH   HOH A . 
I 5 HOH   64  964  371 HOH   HOH A . 
I 5 HOH   65  965  35  HOH   HOH A . 
I 5 HOH   66  966  31  HOH   HOH A . 
I 5 HOH   67  967  388 HOH   HOH A . 
I 5 HOH   68  968  409 HOH   HOH A . 
I 5 HOH   69  969  132 HOH   HOH A . 
I 5 HOH   70  970  325 HOH   HOH A . 
I 5 HOH   71  971  609 HOH   HOH A . 
I 5 HOH   72  972  209 HOH   HOH A . 
I 5 HOH   73  973  472 HOH   HOH A . 
I 5 HOH   74  974  75  HOH   HOH A . 
I 5 HOH   75  975  524 HOH   HOH A . 
I 5 HOH   76  976  46  HOH   HOH A . 
I 5 HOH   77  977  39  HOH   HOH A . 
I 5 HOH   78  978  365 HOH   HOH A . 
I 5 HOH   79  979  586 HOH   HOH A . 
I 5 HOH   80  980  153 HOH   HOH A . 
I 5 HOH   81  981  282 HOH   HOH A . 
I 5 HOH   82  982  567 HOH   HOH A . 
I 5 HOH   83  983  605 HOH   HOH A . 
I 5 HOH   84  984  445 HOH   HOH A . 
I 5 HOH   85  985  48  HOH   HOH A . 
I 5 HOH   86  986  357 HOH   HOH A . 
I 5 HOH   87  987  507 HOH   HOH A . 
I 5 HOH   88  988  94  HOH   HOH A . 
I 5 HOH   89  989  314 HOH   HOH A . 
I 5 HOH   90  990  582 HOH   HOH A . 
I 5 HOH   91  991  18  HOH   HOH A . 
I 5 HOH   92  992  134 HOH   HOH A . 
I 5 HOH   93  993  30  HOH   HOH A . 
I 5 HOH   94  994  51  HOH   HOH A . 
I 5 HOH   95  995  508 HOH   HOH A . 
I 5 HOH   96  996  95  HOH   HOH A . 
I 5 HOH   97  997  103 HOH   HOH A . 
I 5 HOH   98  998  580 HOH   HOH A . 
I 5 HOH   99  999  128 HOH   HOH A . 
I 5 HOH   100 1000 124 HOH   HOH A . 
I 5 HOH   101 1001 235 HOH   HOH A . 
I 5 HOH   102 1002 102 HOH   HOH A . 
I 5 HOH   103 1003 455 HOH   HOH A . 
I 5 HOH   104 1004 431 HOH   HOH A . 
I 5 HOH   105 1005 551 HOH   HOH A . 
I 5 HOH   106 1006 137 HOH   HOH A . 
I 5 HOH   107 1007 163 HOH   HOH A . 
I 5 HOH   108 1008 526 HOH   HOH A . 
I 5 HOH   109 1009 50  HOH   HOH A . 
I 5 HOH   110 1010 542 HOH   HOH A . 
I 5 HOH   111 1011 180 HOH   HOH A . 
I 5 HOH   112 1012 511 HOH   HOH A . 
I 5 HOH   113 1013 354 HOH   HOH A . 
I 5 HOH   114 1014 466 HOH   HOH A . 
I 5 HOH   115 1015 326 HOH   HOH A . 
I 5 HOH   116 1016 68  HOH   HOH A . 
I 5 HOH   117 1017 492 HOH   HOH A . 
I 5 HOH   118 1018 330 HOH   HOH A . 
I 5 HOH   119 1019 590 HOH   HOH A . 
I 5 HOH   120 1020 475 HOH   HOH A . 
I 5 HOH   121 1021 123 HOH   HOH A . 
I 5 HOH   122 1022 529 HOH   HOH A . 
I 5 HOH   123 1023 160 HOH   HOH A . 
I 5 HOH   124 1024 345 HOH   HOH A . 
I 5 HOH   125 1025 204 HOH   HOH A . 
I 5 HOH   126 1026 333 HOH   HOH A . 
I 5 HOH   127 1027 184 HOH   HOH A . 
I 5 HOH   128 1028 24  HOH   HOH A . 
I 5 HOH   129 1029 148 HOH   HOH A . 
I 5 HOH   130 1030 250 HOH   HOH A . 
I 5 HOH   131 1031 98  HOH   HOH A . 
I 5 HOH   132 1032 106 HOH   HOH A . 
I 5 HOH   133 1033 484 HOH   HOH A . 
I 5 HOH   134 1034 532 HOH   HOH A . 
I 5 HOH   135 1035 195 HOH   HOH A . 
I 5 HOH   136 1036 56  HOH   HOH A . 
I 5 HOH   137 1037 101 HOH   HOH A . 
I 5 HOH   138 1038 97  HOH   HOH A . 
I 5 HOH   139 1039 382 HOH   HOH A . 
I 5 HOH   140 1040 569 HOH   HOH A . 
I 5 HOH   141 1041 81  HOH   HOH A . 
I 5 HOH   142 1042 312 HOH   HOH A . 
I 5 HOH   143 1043 127 HOH   HOH A . 
I 5 HOH   144 1044 386 HOH   HOH A . 
I 5 HOH   145 1045 395 HOH   HOH A . 
I 5 HOH   146 1046 294 HOH   HOH A . 
I 5 HOH   147 1047 65  HOH   HOH A . 
I 5 HOH   148 1048 402 HOH   HOH A . 
I 5 HOH   149 1049 90  HOH   HOH A . 
I 5 HOH   150 1050 574 HOH   HOH A . 
I 5 HOH   151 1051 93  HOH   HOH A . 
I 5 HOH   152 1052 559 HOH   HOH A . 
I 5 HOH   153 1053 589 HOH   HOH A . 
I 5 HOH   154 1054 284 HOH   HOH A . 
I 5 HOH   155 1055 428 HOH   HOH A . 
I 5 HOH   156 1056 473 HOH   HOH A . 
I 5 HOH   157 1057 392 HOH   HOH A . 
I 5 HOH   158 1058 182 HOH   HOH A . 
I 5 HOH   159 1059 460 HOH   HOH A . 
I 5 HOH   160 1060 140 HOH   HOH A . 
I 5 HOH   161 1061 109 HOH   HOH A . 
I 5 HOH   162 1062 415 HOH   HOH A . 
I 5 HOH   163 1063 43  HOH   HOH A . 
I 5 HOH   164 1064 555 HOH   HOH A . 
I 5 HOH   165 1065 162 HOH   HOH A . 
I 5 HOH   166 1066 300 HOH   HOH A . 
I 5 HOH   167 1067 83  HOH   HOH A . 
I 5 HOH   168 1068 504 HOH   HOH A . 
I 5 HOH   169 1069 566 HOH   HOH A . 
I 5 HOH   170 1070 571 HOH   HOH A . 
I 5 HOH   171 1071 100 HOH   HOH A . 
I 5 HOH   172 1072 523 HOH   HOH A . 
I 5 HOH   173 1073 220 HOH   HOH A . 
I 5 HOH   174 1074 283 HOH   HOH A . 
I 5 HOH   175 1075 565 HOH   HOH A . 
I 5 HOH   176 1076 361 HOH   HOH A . 
I 5 HOH   177 1077 258 HOH   HOH A . 
I 5 HOH   178 1078 346 HOH   HOH A . 
I 5 HOH   179 1079 251 HOH   HOH A . 
I 5 HOH   180 1080 306 HOH   HOH A . 
I 5 HOH   181 1081 113 HOH   HOH A . 
I 5 HOH   182 1082 117 HOH   HOH A . 
I 5 HOH   183 1083 487 HOH   HOH A . 
I 5 HOH   184 1084 379 HOH   HOH A . 
I 5 HOH   185 1085 252 HOH   HOH A . 
I 5 HOH   186 1086 213 HOH   HOH A . 
I 5 HOH   187 1087 433 HOH   HOH A . 
I 5 HOH   188 1088 458 HOH   HOH A . 
I 5 HOH   189 1089 358 HOH   HOH A . 
I 5 HOH   190 1090 224 HOH   HOH A . 
I 5 HOH   191 1091 562 HOH   HOH A . 
I 5 HOH   192 1092 236 HOH   HOH A . 
I 5 HOH   193 1093 355 HOH   HOH A . 
I 5 HOH   194 1094 74  HOH   HOH A . 
I 5 HOH   195 1095 632 HOH   HOH A . 
I 5 HOH   196 1096 225 HOH   HOH A . 
I 5 HOH   197 1097 422 HOH   HOH A . 
I 5 HOH   198 1098 613 HOH   HOH A . 
I 5 HOH   199 1099 625 HOH   HOH A . 
I 5 HOH   200 1100 540 HOH   HOH A . 
I 5 HOH   201 1101 359 HOH   HOH A . 
I 5 HOH   202 1102 440 HOH   HOH A . 
I 5 HOH   203 1103 493 HOH   HOH A . 
I 5 HOH   204 1104 624 HOH   HOH A . 
I 5 HOH   205 1105 635 HOH   HOH A . 
I 5 HOH   206 1106 505 HOH   HOH A . 
I 5 HOH   207 1107 522 HOH   HOH A . 
I 5 HOH   208 1108 545 HOH   HOH A . 
I 5 HOH   209 1109 593 HOH   HOH A . 
I 5 HOH   210 1110 285 HOH   HOH A . 
I 5 HOH   211 1111 531 HOH   HOH A . 
I 5 HOH   212 1112 240 HOH   HOH A . 
I 5 HOH   213 1113 434 HOH   HOH A . 
I 5 HOH   214 1114 628 HOH   HOH A . 
I 5 HOH   215 1115 305 HOH   HOH A . 
I 5 HOH   216 1116 168 HOH   HOH A . 
I 5 HOH   217 1117 280 HOH   HOH A . 
I 5 HOH   218 1118 302 HOH   HOH A . 
I 5 HOH   219 1119 175 HOH   HOH A . 
I 5 HOH   220 1120 343 HOH   HOH A . 
I 5 HOH   221 1121 321 HOH   HOH A . 
I 5 HOH   222 1122 179 HOH   HOH A . 
I 5 HOH   223 1123 500 HOH   HOH A . 
I 5 HOH   224 1124 515 HOH   HOH A . 
I 5 HOH   225 1125 451 HOH   HOH A . 
I 5 HOH   226 1126 399 HOH   HOH A . 
I 5 HOH   227 1127 578 HOH   HOH A . 
I 5 HOH   228 1128 450 HOH   HOH A . 
I 5 HOH   229 1129 596 HOH   HOH A . 
I 5 HOH   230 1130 241 HOH   HOH A . 
I 5 HOH   231 1131 477 HOH   HOH A . 
I 5 HOH   232 1132 452 HOH   HOH A . 
I 5 HOH   233 1133 579 HOH   HOH A . 
I 5 HOH   234 1134 364 HOH   HOH A . 
I 5 HOH   235 1135 478 HOH   HOH A . 
I 5 HOH   236 1136 476 HOH   HOH A . 
I 5 HOH   237 1137 193 HOH   HOH A . 
I 5 HOH   238 1138 389 HOH   HOH A . 
I 5 HOH   239 1139 530 HOH   HOH A . 
I 5 HOH   240 1140 468 HOH   HOH A . 
I 5 HOH   241 1141 459 HOH   HOH A . 
I 5 HOH   242 1142 501 HOH   HOH A . 
I 5 HOH   243 1143 275 HOH   HOH A . 
I 5 HOH   244 1144 496 HOH   HOH A . 
I 5 HOH   245 1145 497 HOH   HOH A . 
I 5 HOH   246 1146 429 HOH   HOH A . 
I 5 HOH   247 1147 222 HOH   HOH A . 
I 5 HOH   248 1148 174 HOH   HOH A . 
I 5 HOH   249 1149 490 HOH   HOH A . 
I 5 HOH   250 1150 256 HOH   HOH A . 
I 5 HOH   251 1151 211 HOH   HOH A . 
I 5 HOH   252 1152 394 HOH   HOH A . 
I 5 HOH   253 1153 339 HOH   HOH A . 
I 5 HOH   254 1154 368 HOH   HOH A . 
I 5 HOH   255 1155 435 HOH   HOH A . 
I 5 HOH   256 1156 401 HOH   HOH A . 
I 5 HOH   257 1157 255 HOH   HOH A . 
I 5 HOH   258 1158 550 HOH   HOH A . 
J 5 HOH   1   901  178 HOH   HOH B . 
J 5 HOH   2   902  521 HOH   HOH B . 
J 5 HOH   3   903  607 HOH   HOH B . 
J 5 HOH   4   904  467 HOH   HOH B . 
J 5 HOH   5   905  259 HOH   HOH B . 
J 5 HOH   6   906  202 HOH   HOH B . 
J 5 HOH   7   907  588 HOH   HOH B . 
J 5 HOH   8   908  376 HOH   HOH B . 
J 5 HOH   9   909  633 HOH   HOH B . 
J 5 HOH   10  910  154 HOH   HOH B . 
J 5 HOH   11  911  561 HOH   HOH B . 
J 5 HOH   12  912  194 HOH   HOH B . 
J 5 HOH   13  913  214 HOH   HOH B . 
J 5 HOH   14  914  344 HOH   HOH B . 
J 5 HOH   15  915  369 HOH   HOH B . 
J 5 HOH   16  916  25  HOH   HOH B . 
J 5 HOH   17  917  406 HOH   HOH B . 
J 5 HOH   18  918  192 HOH   HOH B . 
J 5 HOH   19  919  597 HOH   HOH B . 
J 5 HOH   20  920  412 HOH   HOH B . 
J 5 HOH   21  921  187 HOH   HOH B . 
J 5 HOH   22  922  122 HOH   HOH B . 
J 5 HOH   23  923  489 HOH   HOH B . 
J 5 HOH   24  924  130 HOH   HOH B . 
J 5 HOH   25  925  1   HOH   HOH B . 
J 5 HOH   26  926  69  HOH   HOH B . 
J 5 HOH   27  927  47  HOH   HOH B . 
J 5 HOH   28  928  85  HOH   HOH B . 
J 5 HOH   29  929  366 HOH   HOH B . 
J 5 HOH   30  930  390 HOH   HOH B . 
J 5 HOH   31  931  602 HOH   HOH B . 
J 5 HOH   32  932  381 HOH   HOH B . 
J 5 HOH   33  933  199 HOH   HOH B . 
J 5 HOH   34  934  4   HOH   HOH B . 
J 5 HOH   35  935  9   HOH   HOH B . 
J 5 HOH   36  936  190 HOH   HOH B . 
J 5 HOH   37  937  34  HOH   HOH B . 
J 5 HOH   38  938  60  HOH   HOH B . 
J 5 HOH   39  939  411 HOH   HOH B . 
J 5 HOH   40  940  59  HOH   HOH B . 
J 5 HOH   41  941  383 HOH   HOH B . 
J 5 HOH   42  942  185 HOH   HOH B . 
J 5 HOH   43  943  543 HOH   HOH B . 
J 5 HOH   44  944  577 HOH   HOH B . 
J 5 HOH   45  945  176 HOH   HOH B . 
J 5 HOH   46  946  528 HOH   HOH B . 
J 5 HOH   47  947  329 HOH   HOH B . 
J 5 HOH   48  948  144 HOH   HOH B . 
J 5 HOH   49  949  114 HOH   HOH B . 
J 5 HOH   50  950  108 HOH   HOH B . 
J 5 HOH   51  951  426 HOH   HOH B . 
J 5 HOH   52  952  438 HOH   HOH B . 
J 5 HOH   53  953  474 HOH   HOH B . 
J 5 HOH   54  954  157 HOH   HOH B . 
J 5 HOH   55  955  172 HOH   HOH B . 
J 5 HOH   56  956  82  HOH   HOH B . 
J 5 HOH   57  957  138 HOH   HOH B . 
J 5 HOH   58  958  22  HOH   HOH B . 
J 5 HOH   59  959  481 HOH   HOH B . 
J 5 HOH   60  960  161 HOH   HOH B . 
J 5 HOH   61  961  8   HOH   HOH B . 
J 5 HOH   62  962  610 HOH   HOH B . 
J 5 HOH   63  963  408 HOH   HOH B . 
J 5 HOH   64  964  483 HOH   HOH B . 
J 5 HOH   65  965  87  HOH   HOH B . 
J 5 HOH   66  966  155 HOH   HOH B . 
J 5 HOH   67  967  72  HOH   HOH B . 
J 5 HOH   68  968  416 HOH   HOH B . 
J 5 HOH   69  969  328 HOH   HOH B . 
J 5 HOH   70  970  158 HOH   HOH B . 
J 5 HOH   71  971  201 HOH   HOH B . 
J 5 HOH   72  972  480 HOH   HOH B . 
J 5 HOH   73  973  23  HOH   HOH B . 
J 5 HOH   74  974  232 HOH   HOH B . 
J 5 HOH   75  975  181 HOH   HOH B . 
J 5 HOH   76  976  33  HOH   HOH B . 
J 5 HOH   77  977  53  HOH   HOH B . 
J 5 HOH   78  978  196 HOH   HOH B . 
J 5 HOH   79  979  171 HOH   HOH B . 
J 5 HOH   80  980  27  HOH   HOH B . 
J 5 HOH   81  981  219 HOH   HOH B . 
J 5 HOH   82  982  276 HOH   HOH B . 
J 5 HOH   83  983  289 HOH   HOH B . 
J 5 HOH   84  984  293 HOH   HOH B . 
J 5 HOH   85  985  121 HOH   HOH B . 
J 5 HOH   86  986  519 HOH   HOH B . 
J 5 HOH   87  987  11  HOH   HOH B . 
J 5 HOH   88  988  28  HOH   HOH B . 
J 5 HOH   89  989  568 HOH   HOH B . 
J 5 HOH   90  990  486 HOH   HOH B . 
J 5 HOH   91  991  20  HOH   HOH B . 
J 5 HOH   92  992  338 HOH   HOH B . 
J 5 HOH   93  993  207 HOH   HOH B . 
J 5 HOH   94  994  136 HOH   HOH B . 
J 5 HOH   95  995  518 HOH   HOH B . 
J 5 HOH   96  996  166 HOH   HOH B . 
J 5 HOH   97  997  465 HOH   HOH B . 
J 5 HOH   98  998  64  HOH   HOH B . 
J 5 HOH   99  999  239 HOH   HOH B . 
J 5 HOH   100 1000 145 HOH   HOH B . 
J 5 HOH   101 1001 36  HOH   HOH B . 
J 5 HOH   102 1002 552 HOH   HOH B . 
J 5 HOH   103 1003 427 HOH   HOH B . 
J 5 HOH   104 1004 86  HOH   HOH B . 
J 5 HOH   105 1005 15  HOH   HOH B . 
J 5 HOH   106 1006 527 HOH   HOH B . 
J 5 HOH   107 1007 242 HOH   HOH B . 
J 5 HOH   108 1008 405 HOH   HOH B . 
J 5 HOH   109 1009 243 HOH   HOH B . 
J 5 HOH   110 1010 485 HOH   HOH B . 
J 5 HOH   111 1011 66  HOH   HOH B . 
J 5 HOH   112 1012 337 HOH   HOH B . 
J 5 HOH   113 1013 512 HOH   HOH B . 
J 5 HOH   114 1014 269 HOH   HOH B . 
J 5 HOH   115 1015 32  HOH   HOH B . 
J 5 HOH   116 1016 41  HOH   HOH B . 
J 5 HOH   117 1017 253 HOH   HOH B . 
J 5 HOH   118 1018 58  HOH   HOH B . 
J 5 HOH   119 1019 173 HOH   HOH B . 
J 5 HOH   120 1020 553 HOH   HOH B . 
J 5 HOH   121 1021 471 HOH   HOH B . 
J 5 HOH   122 1022 62  HOH   HOH B . 
J 5 HOH   123 1023 212 HOH   HOH B . 
J 5 HOH   124 1024 254 HOH   HOH B . 
J 5 HOH   125 1025 295 HOH   HOH B . 
J 5 HOH   126 1026 407 HOH   HOH B . 
J 5 HOH   127 1027 150 HOH   HOH B . 
J 5 HOH   128 1028 356 HOH   HOH B . 
J 5 HOH   129 1029 63  HOH   HOH B . 
J 5 HOH   130 1030 7   HOH   HOH B . 
J 5 HOH   131 1031 14  HOH   HOH B . 
J 5 HOH   132 1032 278 HOH   HOH B . 
J 5 HOH   133 1033 188 HOH   HOH B . 
J 5 HOH   134 1034 165 HOH   HOH B . 
J 5 HOH   135 1035 12  HOH   HOH B . 
J 5 HOH   136 1036 398 HOH   HOH B . 
J 5 HOH   137 1037 42  HOH   HOH B . 
J 5 HOH   138 1038 156 HOH   HOH B . 
J 5 HOH   139 1039 164 HOH   HOH B . 
J 5 HOH   140 1040 462 HOH   HOH B . 
J 5 HOH   141 1041 454 HOH   HOH B . 
J 5 HOH   142 1042 19  HOH   HOH B . 
J 5 HOH   143 1043 375 HOH   HOH B . 
J 5 HOH   144 1044 147 HOH   HOH B . 
J 5 HOH   145 1045 470 HOH   HOH B . 
J 5 HOH   146 1046 396 HOH   HOH B . 
J 5 HOH   147 1047 498 HOH   HOH B . 
J 5 HOH   148 1048 80  HOH   HOH B . 
J 5 HOH   149 1049 208 HOH   HOH B . 
J 5 HOH   150 1050 266 HOH   HOH B . 
J 5 HOH   151 1051 189 HOH   HOH B . 
J 5 HOH   152 1052 419 HOH   HOH B . 
J 5 HOH   153 1053 502 HOH   HOH B . 
J 5 HOH   154 1054 336 HOH   HOH B . 
J 5 HOH   155 1055 400 HOH   HOH B . 
J 5 HOH   156 1056 70  HOH   HOH B . 
J 5 HOH   157 1057 443 HOH   HOH B . 
J 5 HOH   158 1058 17  HOH   HOH B . 
J 5 HOH   159 1059 410 HOH   HOH B . 
J 5 HOH   160 1060 594 HOH   HOH B . 
J 5 HOH   161 1061 353 HOH   HOH B . 
J 5 HOH   162 1062 413 HOH   HOH B . 
J 5 HOH   163 1063 360 HOH   HOH B . 
J 5 HOH   164 1064 304 HOH   HOH B . 
J 5 HOH   165 1065 38  HOH   HOH B . 
J 5 HOH   166 1066 57  HOH   HOH B . 
J 5 HOH   167 1067 277 HOH   HOH B . 
J 5 HOH   168 1068 79  HOH   HOH B . 
J 5 HOH   169 1069 297 HOH   HOH B . 
J 5 HOH   170 1070 228 HOH   HOH B . 
J 5 HOH   171 1071 197 HOH   HOH B . 
J 5 HOH   172 1072 350 HOH   HOH B . 
J 5 HOH   173 1073 341 HOH   HOH B . 
J 5 HOH   174 1074 335 HOH   HOH B . 
J 5 HOH   175 1075 603 HOH   HOH B . 
J 5 HOH   176 1076 384 HOH   HOH B . 
J 5 HOH   177 1077 119 HOH   HOH B . 
J 5 HOH   178 1078 52  HOH   HOH B . 
J 5 HOH   179 1079 76  HOH   HOH B . 
J 5 HOH   180 1080 576 HOH   HOH B . 
J 5 HOH   181 1081 296 HOH   HOH B . 
J 5 HOH   182 1082 227 HOH   HOH B . 
J 5 HOH   183 1083 169 HOH   HOH B . 
J 5 HOH   184 1084 206 HOH   HOH B . 
J 5 HOH   185 1085 146 HOH   HOH B . 
J 5 HOH   186 1086 573 HOH   HOH B . 
J 5 HOH   187 1087 391 HOH   HOH B . 
J 5 HOH   188 1088 307 HOH   HOH B . 
J 5 HOH   189 1089 205 HOH   HOH B . 
J 5 HOH   190 1090 143 HOH   HOH B . 
J 5 HOH   191 1091 316 HOH   HOH B . 
J 5 HOH   192 1092 221 HOH   HOH B . 
J 5 HOH   193 1093 447 HOH   HOH B . 
J 5 HOH   194 1094 619 HOH   HOH B . 
J 5 HOH   195 1095 78  HOH   HOH B . 
J 5 HOH   196 1096 238 HOH   HOH B . 
J 5 HOH   197 1097 88  HOH   HOH B . 
J 5 HOH   198 1098 403 HOH   HOH B . 
J 5 HOH   199 1099 547 HOH   HOH B . 
J 5 HOH   200 1100 217 HOH   HOH B . 
J 5 HOH   201 1101 387 HOH   HOH B . 
J 5 HOH   202 1102 323 HOH   HOH B . 
J 5 HOH   203 1103 425 HOH   HOH B . 
J 5 HOH   204 1104 110 HOH   HOH B . 
J 5 HOH   205 1105 584 HOH   HOH B . 
J 5 HOH   206 1106 482 HOH   HOH B . 
J 5 HOH   207 1107 441 HOH   HOH B . 
J 5 HOH   208 1108 263 HOH   HOH B . 
J 5 HOH   209 1109 544 HOH   HOH B . 
J 5 HOH   210 1110 317 HOH   HOH B . 
J 5 HOH   211 1111 260 HOH   HOH B . 
J 5 HOH   212 1112 352 HOH   HOH B . 
J 5 HOH   213 1113 281 HOH   HOH B . 
J 5 HOH   214 1114 583 HOH   HOH B . 
J 5 HOH   215 1115 231 HOH   HOH B . 
J 5 HOH   216 1116 71  HOH   HOH B . 
J 5 HOH   217 1117 373 HOH   HOH B . 
J 5 HOH   218 1118 554 HOH   HOH B . 
J 5 HOH   219 1119 244 HOH   HOH B . 
J 5 HOH   220 1120 626 HOH   HOH B . 
J 5 HOH   221 1121 537 HOH   HOH B . 
J 5 HOH   222 1122 347 HOH   HOH B . 
J 5 HOH   223 1123 311 HOH   HOH B . 
J 5 HOH   224 1124 525 HOH   HOH B . 
J 5 HOH   225 1125 509 HOH   HOH B . 
J 5 HOH   226 1126 73  HOH   HOH B . 
J 5 HOH   227 1127 320 HOH   HOH B . 
J 5 HOH   228 1128 560 HOH   HOH B . 
J 5 HOH   229 1129 313 HOH   HOH B . 
J 5 HOH   230 1130 510 HOH   HOH B . 
J 5 HOH   231 1131 249 HOH   HOH B . 
J 5 HOH   232 1132 348 HOH   HOH B . 
J 5 HOH   233 1133 516 HOH   HOH B . 
J 5 HOH   234 1134 461 HOH   HOH B . 
J 5 HOH   235 1135 495 HOH   HOH B . 
J 5 HOH   236 1136 423 HOH   HOH B . 
J 5 HOH   237 1137 448 HOH   HOH B . 
J 5 HOH   238 1138 464 HOH   HOH B . 
J 5 HOH   239 1139 129 HOH   HOH B . 
J 5 HOH   240 1140 257 HOH   HOH B . 
J 5 HOH   241 1141 309 HOH   HOH B . 
J 5 HOH   242 1142 621 HOH   HOH B . 
J 5 HOH   243 1143 271 HOH   HOH B . 
J 5 HOH   244 1144 533 HOH   HOH B . 
J 5 HOH   245 1145 606 HOH   HOH B . 
J 5 HOH   246 1146 248 HOH   HOH B . 
J 5 HOH   247 1147 96  HOH   HOH B . 
J 5 HOH   248 1148 614 HOH   HOH B . 
J 5 HOH   249 1149 418 HOH   HOH B . 
J 5 HOH   250 1150 223 HOH   HOH B . 
J 5 HOH   251 1151 301 HOH   HOH B . 
J 5 HOH   252 1152 393 HOH   HOH B . 
J 5 HOH   253 1153 612 HOH   HOH B . 
J 5 HOH   254 1154 351 HOH   HOH B . 
J 5 HOH   255 1155 499 HOH   HOH B . 
J 5 HOH   256 1156 135 HOH   HOH B . 
J 5 HOH   257 1157 237 HOH   HOH B . 
J 5 HOH   258 1158 216 HOH   HOH B . 
J 5 HOH   259 1159 299 HOH   HOH B . 
J 5 HOH   260 1160 506 HOH   HOH B . 
J 5 HOH   261 1161 203 HOH   HOH B . 
J 5 HOH   262 1162 442 HOH   HOH B . 
J 5 HOH   263 1163 563 HOH   HOH B . 
J 5 HOH   264 1164 598 HOH   HOH B . 
J 5 HOH   265 1165 469 HOH   HOH B . 
J 5 HOH   266 1166 570 HOH   HOH B . 
J 5 HOH   267 1167 315 HOH   HOH B . 
J 5 HOH   268 1168 436 HOH   HOH B . 
J 5 HOH   269 1169 556 HOH   HOH B . 
J 5 HOH   270 1170 548 HOH   HOH B . 
J 5 HOH   271 1171 105 HOH   HOH B . 
J 5 HOH   272 1172 620 HOH   HOH B . 
J 5 HOH   273 1173 267 HOH   HOH B . 
J 5 HOH   274 1174 286 HOH   HOH B . 
J 5 HOH   275 1175 615 HOH   HOH B . 
J 5 HOH   276 1176 308 HOH   HOH B . 
J 5 HOH   277 1177 549 HOH   HOH B . 
J 5 HOH   278 1178 535 HOH   HOH B . 
J 5 HOH   279 1179 575 HOH   HOH B . 
J 5 HOH   280 1180 234 HOH   HOH B . 
J 5 HOH   281 1181 414 HOH   HOH B . 
J 5 HOH   282 1182 634 HOH   HOH B . 
J 5 HOH   283 1183 245 HOH   HOH B . 
J 5 HOH   284 1184 45  HOH   HOH B . 
J 5 HOH   285 1185 167 HOH   HOH B . 
J 5 HOH   286 1186 622 HOH   HOH B . 
J 5 HOH   287 1187 611 HOH   HOH B . 
J 5 HOH   288 1188 595 HOH   HOH B . 
J 5 HOH   289 1189 215 HOH   HOH B . 
J 5 HOH   290 1190 177 HOH   HOH B . 
J 5 HOH   291 1191 397 HOH   HOH B . 
J 5 HOH   292 1192 629 HOH   HOH B . 
J 5 HOH   293 1193 517 HOH   HOH B . 
J 5 HOH   294 1194 618 HOH   HOH B . 
J 5 HOH   295 1195 319 HOH   HOH B . 
J 5 HOH   296 1196 494 HOH   HOH B . 
J 5 HOH   297 1197 592 HOH   HOH B . 
J 5 HOH   298 1198 362 HOH   HOH B . 
J 5 HOH   299 1199 539 HOH   HOH B . 
J 5 HOH   300 1200 322 HOH   HOH B . 
J 5 HOH   301 1201 310 HOH   HOH B . 
J 5 HOH   302 1202 558 HOH   HOH B . 
J 5 HOH   303 1203 444 HOH   HOH B . 
J 5 HOH   304 1204 200 HOH   HOH B . 
J 5 HOH   305 1205 327 HOH   HOH B . 
J 5 HOH   306 1206 636 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 ARG 788 ? CG  ? A ARG 347 CG  
2  1 Y 1 A ARG 788 ? CD  ? A ARG 347 CD  
3  1 Y 1 A ARG 788 ? NE  ? A ARG 347 NE  
4  1 Y 1 A ARG 788 ? CZ  ? A ARG 347 CZ  
5  1 Y 1 A ARG 788 ? NH1 ? A ARG 347 NH1 
6  1 Y 1 A ARG 788 ? NH2 ? A ARG 347 NH2 
7  1 Y 1 B ASP 770 ? CG  ? B ASP 329 CG  
8  1 Y 1 B ASP 770 ? OD1 ? B ASP 329 OD1 
9  1 Y 1 B ASP 770 ? OD2 ? B ASP 329 OD2 
10 1 Y 1 B HIS 771 ? CG  ? B HIS 330 CG  
11 1 Y 1 B HIS 771 ? ND1 ? B HIS 330 ND1 
12 1 Y 1 B HIS 771 ? CD2 ? B HIS 330 CD2 
13 1 Y 1 B HIS 771 ? CE1 ? B HIS 330 CE1 
14 1 Y 1 B HIS 771 ? NE2 ? B 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                     9EGU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.790 
_cell.length_a_esd                 ? 
_cell.length_b                     91.190 
_cell.length_b_esd                 ? 
_cell.length_c                     96.160 
_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                         9EGU 
_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                   9EGU 
_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             2.06 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.40 
_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    '30% PEG 4K, 0.2M NH4 Acet. 0.1M Na Citrate 5.6' 
_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         2021-06-10 
_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                                       9EGU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.27 
_reflns.d_resolution_low                               91.19 
_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                                     162298 
_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                           93.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.097 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1079785 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_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                                    1.27 
_reflns_shell.d_res_low                                     1.29 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           25511 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5163 
_reflns_shell.percent_possible_obs                          60.6 
_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                               4.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.6 
_reflns_shell.pdbx_Rrim_I_all                               2.377 
_reflns_shell.pdbx_Rpim_I_all                               1.027 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.313 
_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                                  2.127 
_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                                 9EGU 
_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                            1.270 
_refine.ls_d_res_low                             59.036 
_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                     161851 
_refine.ls_number_reflns_R_free                  8136 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.49 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2086 
_refine.ls_R_factor_R_free                       0.2212 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2080 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.77 
_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                            0.17 
_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        5566 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             564 
_refine_hist.number_atoms_total               6188 
_refine_hist.d_res_high                       1.270 
_refine_hist.d_res_low                        59.036 
# 
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 ? 5878 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.803 ? 7988 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 3.809 ? 3388 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076 ? 856  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 1050 ? 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' 1.2700 1.2844 . . 141 3193 58.00  . . . . 0.4049 . . . . . . . . . . . 0.4189 
'X-RAY DIFFRACTION' 1.2844 1.2995 . . 190 3430 63.00  . . . . 0.3815 . . . . . . . . . . . 0.4017 
'X-RAY DIFFRACTION' 1.2995 1.3154 . . 195 3731 69.00  . . . . 0.3761 . . . . . . . . . . . 0.4085 
'X-RAY DIFFRACTION' 1.3154 1.3321 . . 204 4158 77.00  . . . . 0.3674 . . . . . . . . . . . 0.3672 
'X-RAY DIFFRACTION' 1.3321 1.3496 . . 238 4665 85.00  . . . . 0.3632 . . . . . . . . . . . 0.3522 
'X-RAY DIFFRACTION' 1.3496 1.3681 . . 294 5054 93.00  . . . . 0.3452 . . . . . . . . . . . 0.3858 
'X-RAY DIFFRACTION' 1.3681 1.3876 . . 252 5160 95.00  . . . . 0.3250 . . . . . . . . . . . 0.3295 
'X-RAY DIFFRACTION' 1.3876 1.4083 . . 256 5263 97.00  . . . . 0.3156 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 1.4083 1.4303 . . 267 5288 98.00  . . . . 0.3049 . . . . . . . . . . . 0.2986 
'X-RAY DIFFRACTION' 1.4303 1.4538 . . 254 5345 97.00  . . . . 0.2864 . . . . . . . . . . . 0.3513 
'X-RAY DIFFRACTION' 1.4538 1.4789 . . 303 5274 97.00  . . . . 0.2790 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 1.4789 1.5058 . . 281 5339 98.00  . . . . 0.2671 . . . . . . . . . . . 0.2994 
'X-RAY DIFFRACTION' 1.5058 1.5347 . . 279 5302 98.00  . . . . 0.2524 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 1.5347 1.5660 . . 299 5350 98.00  . . . . 0.2419 . . . . . . . . . . . 0.2814 
'X-RAY DIFFRACTION' 1.5660 1.6001 . . 300 5354 98.00  . . . . 0.2395 . . . . . . . . . . . 0.2581 
'X-RAY DIFFRACTION' 1.6001 1.6373 . . 295 5359 98.00  . . . . 0.2358 . . . . . . . . . . . 0.2898 
'X-RAY DIFFRACTION' 1.6373 1.6783 . . 293 5212 97.00  . . . . 0.2301 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 1.6783 1.7237 . . 275 5388 98.00  . . . . 0.2212 . . . . . . . . . . . 0.2576 
'X-RAY DIFFRACTION' 1.7237 1.7744 . . 292 5362 98.00  . . . . 0.2118 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 1.7744 1.8317 . . 263 5440 99.00  . . . . 0.2159 . . . . . . . . . . . 0.2371 
'X-RAY DIFFRACTION' 1.8317 1.8971 . . 291 5422 99.00  . . . . 0.2042 . . . . . . . . . . . 0.2172 
'X-RAY DIFFRACTION' 1.8971 1.9731 . . 273 5450 99.00  . . . . 0.1925 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 1.9731 2.0629 . . 270 5452 99.00  . . . . 0.1922 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 2.0629 2.1716 . . 263 5513 99.00  . . . . 0.1867 . . . . . . . . . . . 0.2084 
'X-RAY DIFFRACTION' 2.1716 2.3077 . . 289 5390 98.00  . . . . 0.1876 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 2.3077 2.4859 . . 322 5442 99.00  . . . . 0.1864 . . . . . . . . . . . 0.2140 
'X-RAY DIFFRACTION' 2.4859 2.7361 . . 325 5485 99.00  . . . . 0.1897 . . . . . . . . . . . 0.2200 
'X-RAY DIFFRACTION' 2.7361 3.1320 . . 319 5540 100.00 . . . . 0.1952 . . . . . . . . . . . 0.2170 
'X-RAY DIFFRACTION' 3.1320 3.9458 . . 298 5590 100.00 . . . . 0.1733 . . . . . . . . . . . 0.1755 
# 
_struct.entry_id                     9EGU 
_struct.title                        
'Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 complexed with TO-599' 
_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        9EGU 
_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 9EGU A 1 ? 357 ? A7YT55 290 ? 646 ? 442 798 
2 1 9EGU 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 GLN A 9   ? HIS A 14  ? GLN A 450 HIS A 455 5 ? 6  
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  ? TYR A 88  ? LYS A 518 TYR A 529 1 ? 12 
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 ASP B 8   ? HIS B 14  ? ASP B 449 HIS B 455 5 ? 7  
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  ? GLU B 87  ? LYS B 518 GLU B 528 1 ? 11 
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 ? THR B 159 ? ASN B 587 THR B 600 1 ? 14 
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 ? ? ? ? ? ? ? 2.022 ? ? 
metalc2  metalc ? ? A HIS   173 ND1 ? ? ? 1_555 D ZN  . ZN ? ? A HIS   614 A ZN  802 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc3  metalc ? ? A PHE   182 O   ? ? ? 1_555 E K   . K  ? ? A PHE   623 A K   803 1_555 ? ? ? ? ? ? ? 2.735 ? ? 
metalc4  metalc ? ? A ASP   185 O   ? ? ? 1_555 E K   . K  ? ? A ASP   626 A K   803 1_555 ? ? ? ? ? ? ? 2.897 ? ? 
metalc5  metalc ? ? A VAL   188 O   ? ? ? 1_555 E K   . K  ? ? A VAL   629 A K   803 1_555 ? ? ? ? ? ? ? 2.701 ? ? 
metalc6  metalc ? ? A TYR   221 O   ? ? ? 1_555 E K   . K  ? ? A TYR   662 A K   803 1_555 ? ? ? ? ? ? ? 2.869 ? ? 
metalc7  metalc ? ? A ASP   264 OD2 ? ? ? 1_555 D ZN  . ZN ? ? A ASP   705 A ZN  802 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc8  metalc ? ? C A1BH9 .   N03 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH9 801 A ZN  802 1_555 ? ? ? ? ? ? ? 2.578 ? ? 
metalc9  metalc ? ? C A1BH9 .   O01 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH9 801 A ZN  802 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc10 metalc ? ? C A1BH9 .   O04 ? ? ? 1_555 D ZN  . ZN ? ? A A1BH9 801 A ZN  802 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc11 metalc ? ? E K     .   K   ? ? ? 1_555 I HOH . O  ? ? A K     803 A HOH 963 1_555 ? ? ? ? ? ? ? 2.732 ? ? 
metalc12 metalc ? ? E K     .   K   ? ? ? 1_555 I HOH . O  ? ? A K     803 A HOH 991 1_555 ? ? ? ? ? ? ? 2.989 ? ? 
metalc13 metalc ? ? B ASP   171 OD1 ? ? ? 1_555 G ZN  . ZN ? ? B ASP   612 B ZN  802 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc14 metalc ? ? B HIS   173 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS   614 B ZN  802 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc15 metalc ? ? B PHE   182 O   ? ? ? 1_555 H K   . K  ? ? B PHE   623 B K   803 1_555 ? ? ? ? ? ? ? 2.728 ? ? 
metalc16 metalc ? ? B ASP   185 O   ? ? ? 1_555 H K   . K  ? ? B ASP   626 B K   803 1_555 ? ? ? ? ? ? ? 2.925 ? ? 
metalc17 metalc ? ? B VAL   188 O   ? ? ? 1_555 H K   . K  ? ? B VAL   629 B K   803 1_555 ? ? ? ? ? ? ? 2.663 ? ? 
metalc18 metalc ? ? B TYR   221 O   ? ? ? 1_555 H K   . K  ? ? B TYR   662 B K   803 1_555 ? ? ? ? ? ? ? 2.854 ? ? 
metalc19 metalc ? ? B ASP   264 OD2 ? ? ? 1_555 G ZN  . ZN ? ? B ASP   705 B ZN  802 1_555 ? ? ? ? ? ? ? 1.956 ? ? 
metalc20 metalc ? ? F A1BH9 .   N03 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH9 801 B ZN  802 1_555 ? ? ? ? ? ? ? 2.673 ? ? 
metalc21 metalc ? ? F A1BH9 .   O01 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH9 801 B ZN  802 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc22 metalc ? ? F A1BH9 .   O04 ? ? ? 1_555 G ZN  . ZN ? ? B A1BH9 801 B ZN  802 1_555 ? ? ? ? ? ? ? 2.118 ? ? 
metalc23 metalc ? ? H K     .   K   ? ? ? 1_555 J HOH . O  ? ? B K     803 B HOH 958 1_555 ? ? ? ? ? ? ? 3.046 ? ? 
metalc24 metalc ? ? H K     .   K   ? ? ? 1_555 J HOH . O  ? ? B K     803 B HOH 976 1_555 ? ? ? ? ? ? ? 2.714 ? ? 
# 
_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_555 101.6 ? 
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_555 105.9 ? 
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 97.5  ? 
4  OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 118.7 ? 
5  ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 80.3  ? 
6  OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 N03 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 134.9 ? 
7  OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 165.6 ? 
8  ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 88.1  ? 
9  OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 83.0  ? 
10 N03 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O01 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 52.0  ? 
11 OD1 ? A ASP   171 ? A ASP   612 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 91.1  ? 
12 ND1 ? A HIS   173 ? A HIS   614 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 102.7 ? 
13 OD2 ? A ASP   264 ? A ASP   705 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 150.4 ? 
14 N03 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 32.6  ? 
15 O01 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 ZN ? D ZN . ? A ZN 802 ? 1_555 O04 ? C A1BH9 .   ? A A1BH9 801 ? 1_555 76.3  ? 
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 74.2  ? 
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_555 117.7 ? 
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 79.5  ? 
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_555 156.8 ? 
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_555 114.8 ? 
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 85.5  ? 
22 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   963 ? 1_555 79.9  ? 
23 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   963 ? 1_555 84.6  ? 
24 O   ? A VAL   188 ? A VAL   629 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   963 ? 1_555 151.4 ? 
25 O   ? A TYR   221 ? A TYR   662 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   963 ? 1_555 79.7  ? 
26 O   ? A PHE   182 ? A PHE   623 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   991 ? 1_555 70.0  ? 
27 O   ? A ASP   185 ? A ASP   626 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   991 ? 1_555 143.4 ? 
28 O   ? A VAL   188 ? A VAL   629 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   991 ? 1_555 123.9 ? 
29 O   ? A TYR   221 ? A TYR   662 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   991 ? 1_555 96.2  ? 
30 O   ? I HOH   .   ? A HOH   963 ? 1_555 K  ? E K  . ? A K  803 ? 1_555 O   ? I HOH   .   ? A HOH   991 ? 1_555 82.3  ? 
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_555 107.2 ? 
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 98.9  ? 
34 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 118.1 ? 
35 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 80.4  ? 
36 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 N03 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 133.9 ? 
37 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 163.8 ? 
38 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 89.1  ? 
39 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 82.2  ? 
40 N03 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O01 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 51.8  ? 
41 OD1 ? B ASP   171 ? B ASP   612 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 91.6  ? 
42 ND1 ? B HIS   173 ? B HIS   614 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 102.8 ? 
43 OD2 ? B ASP   264 ? B ASP   705 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 147.6 ? 
44 N03 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 31.6  ? 
45 O01 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 ZN ? G ZN . ? B ZN 802 ? 1_555 O04 ? F A1BH9 .   ? B A1BH9 801 ? 1_555 74.4  ? 
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 75.5  ? 
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_555 119.6 ? 
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 79.2  ? 
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_555 154.0 ? 
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_555 116.7 ? 
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 86.1  ? 
52 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   958 ? 1_555 69.9  ? 
53 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   958 ? 1_555 144.7 ? 
54 O   ? B VAL   188 ? B VAL   629 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   958 ? 1_555 124.6 ? 
55 O   ? B TYR   221 ? B TYR   662 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   958 ? 1_555 92.7  ? 
56 O   ? B PHE   182 ? B PHE   623 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   976 ? 1_555 79.8  ? 
57 O   ? B ASP   185 ? B ASP   626 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   976 ? 1_555 87.3  ? 
58 O   ? B VAL   188 ? B VAL   629 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   976 ? 1_555 151.9 ? 
59 O   ? B TYR   221 ? B TYR   662 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   976 ? 1_555 78.0  ? 
60 O   ? J HOH   .   ? B HOH   958 ? 1_555 K  ? H K  . ? B K  803 ? 1_555 O   ? J HOH   .   ? B HOH   976 ? 1_555 79.7  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ARG 128 A . ? ARG 569 A PRO 129 A ? PRO 570 A 1 -4.79 
2 PHE 202 A . ? PHE 643 A PRO 203 A ? PRO 644 A 1 8.18  
3 ARG 128 B . ? ARG 569 B PRO 129 B ? PRO 570 B 1 -1.90 
4 PHE 202 B . ? PHE 643 B PRO 203 B ? PRO 644 B 1 8.31  
# 
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   ? TYR A 7   ? THR A 444 TYR A 448 
AA1 3 ASN A 122 ? ILE A 126 ? ASN A 563 ILE A 567 
AA1 4 VAL A 296 ? LEU A 300 ? VAL A 737 LEU A 741 
AA1 5 LEU A 256 ? ALA A 261 ? LEU A 697 ALA A 702 
AA1 6 VAL A 165 ? ASP A 169 ? VAL A 606 ASP A 610 
AA1 7 VAL A 188 ? ARG A 195 ? VAL A 629 ARG A 636 
AA1 8 ASN A 222 ? TRP A 227 ? ASN A 663 TRP A 668 
AA2 1 HIS B 46  ? ARG B 47  ? HIS B 487 ARG B 488 
AA2 2 THR B 3   ? VAL B 6   ? THR B 444 VAL B 447 
AA2 3 ASN B 122 ? ALA B 125 ? ASN B 563 ALA B 566 
AA2 4 VAL B 296 ? LEU B 300 ? VAL B 737 LEU B 741 
AA2 5 LEU B 256 ? ALA B 261 ? LEU B 697 ALA B 702 
AA2 6 VAL B 165 ? ASP B 169 ? VAL B 606 ASP B 610 
AA2 7 VAL B 188 ? ARG B 195 ? VAL B 629 ARG B 636 
AA2 8 ASN B 222 ? TRP B 227 ? ASN B 663 TRP B 668 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O HIS A 46  ? O HIS A 487 N THR A 3   ? N THR A 444 
AA1 2 3 N GLY A 4   ? N GLY A 445 O ASN A 122 ? O ASN A 563 
AA1 3 4 N ALA A 125 ? N ALA A 566 O ILE A 298 ? O ILE A 739 
AA1 4 5 O LEU A 297 ? O LEU A 738 N VAL A 259 ? N VAL A 700 
AA1 5 6 O LEU A 258 ? O LEU A 699 N LEU A 166 ? N LEU A 607 
AA1 6 7 N 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 LEU B 297 ? O LEU B 738 N VAL B 259 ? N VAL B 700 
AA2 5 6 O LEU B 258 ? O LEU B 699 N LEU B 166 ? N LEU B 607 
AA2 6 7 N ASP B 169 ? N ASP B 610 O ILE B 191 ? O ILE B 632 
AA2 7 8 N TYR B 190 ? N TYR B 631 O VAL B 223 ? O VAL B 664 
# 
_pdbx_entry_details.entry_id                   9EGU 
_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   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    660 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    901 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.02 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              774 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              774 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              774 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                94.38 
_pdbx_validate_rmsd_angle.angle_target_value         103.30 
_pdbx_validate_rmsd_angle.angle_deviation            -8.92 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 531 ? ? 61.69   60.45   
2  1 CYS A 581 ? ? -171.48 142.96  
3  1 THR A 600 ? ? -124.85 -99.48  
4  1 LEU A 685 ? ? -126.49 -61.77  
5  1 GLN A 716 ? ? -141.46 36.40   
6  1 GLU A 742 ? ? -109.36 -112.46 
7  1 SER B 531 ? ? 63.58   60.32   
8  1 CYS B 581 ? ? -170.26 145.55  
9  1 THR B 600 ? ? -124.37 -99.54  
10 1 LEU B 685 ? ? -127.85 -62.47  
11 1 GLN B 716 ? ? -140.80 38.26   
12 1 GLU B 742 ? ? -110.58 -110.34 
# 
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 
A1BH9 C13  C  Y N 1   
A1BH9 C17  C  Y N 2   
A1BH9 C20  C  Y N 3   
A1BH9 C21  C  Y N 4   
A1BH9 C24  C  Y N 5   
A1BH9 C26  C  Y N 6   
A1BH9 C02  C  N N 7   
A1BH9 C05  C  Y N 8   
A1BH9 C06  C  Y N 9   
A1BH9 C07  C  Y N 10  
A1BH9 C08  C  Y N 11  
A1BH9 C09  C  N N 12  
A1BH9 C14  C  Y N 13  
A1BH9 C16  C  Y N 14  
A1BH9 C19  C  N N 15  
A1BH9 C23  C  Y N 16  
A1BH9 C25  C  Y N 17  
A1BH9 C27  C  Y N 18  
A1BH9 N03  N  N N 19  
A1BH9 N10  N  N N 20  
A1BH9 N22  N  Y N 21  
A1BH9 O01  O  N N 22  
A1BH9 O04  O  N N 23  
A1BH9 O12  O  N N 24  
A1BH9 O18  O  N N 25  
A1BH9 S11  S  N N 26  
A1BH9 S15  S  Y N 27  
A1BH9 H1   H  N N 28  
A1BH9 H2   H  N N 29  
A1BH9 H3   H  N N 30  
A1BH9 H4   H  N N 31  
A1BH9 H5   H  N N 32  
A1BH9 H6   H  N N 33  
A1BH9 H7   H  N N 34  
A1BH9 H8   H  N N 35  
A1BH9 H9   H  N N 36  
A1BH9 H10  H  N N 37  
A1BH9 H11  H  N N 38  
A1BH9 H12  H  N N 39  
A1BH9 H13  H  N N 40  
A1BH9 H14  H  N N 41  
A1BH9 H15  H  N N 42  
A1BH9 H16  H  N N 43  
A1BH9 H17  H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
HIS   N    N  N N 181 
HIS   CA   C  N S 182 
HIS   C    C  N N 183 
HIS   O    O  N N 184 
HIS   CB   C  N N 185 
HIS   CG   C  Y N 186 
HIS   ND1  N  Y N 187 
HIS   CD2  C  Y N 188 
HIS   CE1  C  Y N 189 
HIS   NE2  N  Y N 190 
HIS   OXT  O  N N 191 
HIS   H    H  N N 192 
HIS   H2   H  N N 193 
HIS   HA   H  N N 194 
HIS   HB2  H  N N 195 
HIS   HB3  H  N N 196 
HIS   HD1  H  N N 197 
HIS   HD2  H  N N 198 
HIS   HE1  H  N N 199 
HIS   HE2  H  N N 200 
HIS   HXT  H  N N 201 
HOH   O    O  N N 202 
HOH   H1   H  N N 203 
HOH   H2   H  N N 204 
ILE   N    N  N N 205 
ILE   CA   C  N S 206 
ILE   C    C  N N 207 
ILE   O    O  N N 208 
ILE   CB   C  N S 209 
ILE   CG1  C  N N 210 
ILE   CG2  C  N N 211 
ILE   CD1  C  N N 212 
ILE   OXT  O  N N 213 
ILE   H    H  N N 214 
ILE   H2   H  N N 215 
ILE   HA   H  N N 216 
ILE   HB   H  N N 217 
ILE   HG12 H  N N 218 
ILE   HG13 H  N N 219 
ILE   HG21 H  N N 220 
ILE   HG22 H  N N 221 
ILE   HG23 H  N N 222 
ILE   HD11 H  N N 223 
ILE   HD12 H  N N 224 
ILE   HD13 H  N N 225 
ILE   HXT  H  N N 226 
K     K    K  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
ZN    ZN   ZN N N 436 
# 
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 
A1BH9 O01 C02  doub N N 1   
A1BH9 O04 N03  sing N N 2   
A1BH9 C02 N03  sing N N 3   
A1BH9 C02 C05  sing N N 4   
A1BH9 C27 C05  doub Y N 5   
A1BH9 C27 C26  sing Y N 6   
A1BH9 C05 C06  sing Y N 7   
A1BH9 C26 C08  doub Y N 8   
A1BH9 C06 C07  doub Y N 9   
A1BH9 O12 S11  doub N N 10  
A1BH9 C08 C07  sing Y N 11  
A1BH9 C08 C09  sing N N 12  
A1BH9 O18 S11  doub N N 13  
A1BH9 S11 N10  sing N N 14  
A1BH9 S11 C13  sing N N 15  
A1BH9 C09 N10  sing N N 16  
A1BH9 N22 C21  doub Y N 17  
A1BH9 N22 C23  sing Y N 18  
A1BH9 C21 C20  sing Y N 19  
A1BH9 N10 C19  sing N N 20  
A1BH9 C23 C24  doub Y N 21  
A1BH9 C17 C13  sing Y N 22  
A1BH9 C17 C16  doub Y N 23  
A1BH9 C13 C14  doub Y N 24  
A1BH9 C20 C19  sing N N 25  
A1BH9 C20 C25  doub Y N 26  
A1BH9 C16 S15  sing Y N 27  
A1BH9 C24 C25  sing Y N 28  
A1BH9 C14 S15  sing Y N 29  
A1BH9 C17 H1   sing N N 30  
A1BH9 C21 H2   sing N N 31  
A1BH9 C24 H3   sing N N 32  
A1BH9 C26 H4   sing N N 33  
A1BH9 C06 H5   sing N N 34  
A1BH9 C07 H6   sing N N 35  
A1BH9 C09 H7   sing N N 36  
A1BH9 C09 H8   sing N N 37  
A1BH9 C14 H9   sing N N 38  
A1BH9 C16 H10  sing N N 39  
A1BH9 C19 H11  sing N N 40  
A1BH9 C19 H12  sing N N 41  
A1BH9 C23 H13  sing N N 42  
A1BH9 C25 H14  sing N N 43  
A1BH9 C27 H15  sing N N 44  
A1BH9 N03 H16  sing N N 45  
A1BH9 O04 H17  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
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                    9EGU 
_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]   0.013371 
_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]   0.010966 
_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]   0.010399 
_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   ? 9.573  40.322  1.304  1.00 41.48 ? 442  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 1   ? 10.145 40.432  2.652  1.00 38.83 ? 442  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 1   ? 11.365 41.349  2.677  1.00 33.49 ? 442  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 1   ? 12.454 40.949  2.264  1.00 30.00 ? 442  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 1   ? 10.545 38.990  2.984  1.00 40.47 ? 442  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 1   ? 10.734 38.336  1.652  1.00 44.07 ? 442  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 1   ? 9.727  38.970  0.741  1.00 43.06 ? 442  PRO   A CD  1 
ATOM   8    N  N   . ILE   A 1 2   ? 11.174 42.570  3.169  1.00 28.85 ? 443  ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 2   ? 12.200 43.605  3.159  1.00 24.10 ? 443  ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 2   ? 12.762 43.766  4.566  1.00 19.50 ? 443  ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 2   ? 12.020 43.737  5.556  1.00 20.78 ? 443  ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 2   ? 11.621 44.931  2.624  1.00 26.56 ? 443  ILE   A CB  1 
ATOM   13   C  CG1 . ILE   A 1 2   ? 11.145 44.749  1.181  1.00 29.21 ? 443  ILE   A CG1 1 
ATOM   14   C  CG2 . ILE   A 1 2   ? 12.652 46.051  2.711  1.00 25.75 ? 443  ILE   A CG2 1 
ATOM   15   C  CD1 . ILE   A 1 2   ? 10.446 45.958  0.593  1.00 34.69 ? 443  ILE   A CD1 1 
ATOM   16   N  N   . THR   A 1 3   ? 14.081 43.915  4.653  1.00 16.51 ? 444  THR   A N   1 
ATOM   17   C  CA  . THR   A 1 3   ? 14.758 44.230  5.905  1.00 17.35 ? 444  THR   A CA  1 
ATOM   18   C  C   . THR   A 1 3   ? 15.186 45.689  5.862  1.00 15.76 ? 444  THR   A C   1 
ATOM   19   O  O   . THR   A 1 3   ? 15.833 46.118  4.904  1.00 17.18 ? 444  THR   A O   1 
ATOM   20   C  CB  . THR   A 1 3   ? 15.992 43.341  6.076  1.00 15.34 ? 444  THR   A CB  1 
ATOM   21   O  OG1 . THR   A 1 3   ? 15.586 41.978  6.252  1.00 16.51 ? 444  THR   A OG1 1 
ATOM   22   C  CG2 . THR   A 1 3   ? 16.841 43.792  7.272  1.00 14.48 ? 444  THR   A CG2 1 
ATOM   23   N  N   . GLY   A 1 4   ? 14.828 46.446  6.896  1.00 13.77 ? 445  GLY   A N   1 
ATOM   24   C  CA  . GLY   A 1 4   ? 15.254 47.827  6.995  1.00 14.39 ? 445  GLY   A CA  1 
ATOM   25   C  C   . GLY   A 1 4   ? 16.565 47.973  7.759  1.00 15.20 ? 445  GLY   A C   1 
ATOM   26   O  O   . GLY   A 1 4   ? 16.930 47.139  8.584  1.00 14.14 ? 445  GLY   A O   1 
ATOM   27   N  N   . LEU   A 1 5   ? 17.272 49.061  7.481  1.00 13.22 ? 446  LEU   A N   1 
ATOM   28   C  CA  . LEU   A 1 5   ? 18.501 49.390  8.193  1.00 12.33 ? 446  LEU   A CA  1 
ATOM   29   C  C   . LEU   A 1 5   ? 18.527 50.886  8.421  1.00 13.30 ? 446  LEU   A C   1 
ATOM   30   O  O   . LEU   A 1 5   ? 18.316 51.663  7.482  1.00 14.24 ? 446  LEU   A O   1 
ATOM   31   C  CB  . LEU   A 1 5   ? 19.750 48.973  7.398  1.00 13.59 ? 446  LEU   A CB  1 
ATOM   32   C  CG  . LEU   A 1 5   ? 21.124 49.190  8.052  1.00 13.97 ? 446  LEU   A CG  1 
ATOM   33   C  CD1 . LEU   A 1 5   ? 22.092 48.096  7.603  1.00 15.48 ? 446  LEU   A CD1 1 
ATOM   34   C  CD2 . LEU   A 1 5   ? 21.691 50.573  7.711  1.00 14.23 ? 446  LEU   A CD2 1 
ATOM   35   N  N   . VAL   A 1 6   ? 18.834 51.291  9.652  1.00 12.23 ? 447  VAL   A N   1 
ATOM   36   C  CA  . VAL   A 1 6   ? 18.988 52.702  9.981  1.00 12.82 ? 447  VAL   A CA  1 
ATOM   37   C  C   . VAL   A 1 6   ? 20.387 52.930  10.544 1.00 14.10 ? 447  VAL   A C   1 
ATOM   38   O  O   . VAL   A 1 6   ? 20.884 52.139  11.359 1.00 14.83 ? 447  VAL   A O   1 
ATOM   39   C  CB  . VAL   A 1 6   ? 17.861 53.244  10.884 1.00 13.53 ? 447  VAL   A CB  1 
ATOM   40   C  CG1 . VAL   A 1 6   ? 17.886 52.599  12.264 1.00 13.55 ? 447  VAL   A CG1 1 
ATOM   41   C  CG2 . VAL   A 1 6   ? 17.937 54.752  10.960 1.00 15.46 ? 447  VAL   A CG2 1 
ATOM   42   N  N   . TYR   A 1 7   ? 21.030 53.987  10.065 1.00 14.65 ? 448  TYR   A N   1 
ATOM   43   C  CA  . TYR   A 1 7   ? 22.376 54.371  10.459 1.00 14.73 ? 448  TYR   A CA  1 
ATOM   44   C  C   . TYR   A 1 7   ? 22.558 55.835  10.089 1.00 16.84 ? 448  TYR   A C   1 
ATOM   45   O  O   . TYR   A 1 7   ? 22.120 56.269  9.024  1.00 16.98 ? 448  TYR   A O   1 
ATOM   46   C  CB  . TYR   A 1 7   ? 23.436 53.530  9.733  1.00 14.89 ? 448  TYR   A CB  1 
ATOM   47   C  CG  . TYR   A 1 7   ? 24.838 54.080  9.916  1.00 14.16 ? 448  TYR   A CG  1 
ATOM   48   C  CD1 . TYR   A 1 7   ? 25.522 53.906  11.109 1.00 15.83 ? 448  TYR   A CD1 1 
ATOM   49   C  CD2 . TYR   A 1 7   ? 25.478 54.770  8.892  1.00 14.20 ? 448  TYR   A CD2 1 
ATOM   50   C  CE1 . TYR   A 1 7   ? 26.795 54.397  11.280 1.00 15.37 ? 448  TYR   A CE1 1 
ATOM   51   C  CE2 . TYR   A 1 7   ? 26.758 55.272  9.058  1.00 15.95 ? 448  TYR   A CE2 1 
ATOM   52   C  CZ  . TYR   A 1 7   ? 27.415 55.083  10.257 1.00 18.50 ? 448  TYR   A CZ  1 
ATOM   53   O  OH  . TYR   A 1 7   ? 28.698 55.567  10.463 1.00 21.09 ? 448  TYR   A OH  1 
ATOM   54   N  N   . ASP   A 1 8   ? 23.197 56.597  10.966 1.00 16.73 ? 449  ASP   A N   1 
ATOM   55   C  CA  . ASP   A 1 8   ? 23.539 57.980  10.656 1.00 17.35 ? 449  ASP   A CA  1 
ATOM   56   C  C   . ASP   A 1 8   ? 24.894 58.264  11.275 1.00 15.27 ? 449  ASP   A C   1 
ATOM   57   O  O   . ASP   A 1 8   ? 25.057 58.130  12.494 1.00 13.96 ? 449  ASP   A O   1 
ATOM   58   C  CB  . ASP   A 1 8   ? 22.478 58.958  11.175 1.00 16.79 ? 449  ASP   A CB  1 
ATOM   59   C  CG  . ASP   A 1 8   ? 22.620 60.348  10.587 1.00 23.02 ? 449  ASP   A CG  1 
ATOM   60   O  OD1 . ASP   A 1 8   ? 23.753 60.882  10.563 1.00 22.08 ? 449  ASP   A OD1 1 
ATOM   61   O  OD2 . ASP   A 1 8   ? 21.600 60.917  10.151 1.00 23.46 ? 449  ASP   A OD2 1 
ATOM   62   N  N   A GLN   A 1 9   ? 25.853 58.687  10.445 0.48 14.62 ? 450  GLN   A N   1 
ATOM   63   N  N   B GLN   A 1 9   ? 25.860 58.645  10.430 0.52 15.04 ? 450  GLN   A N   1 
ATOM   64   C  CA  A GLN   A 1 9   ? 27.198 58.953  10.941 0.48 14.44 ? 450  GLN   A CA  1 
ATOM   65   C  CA  B GLN   A 1 9   ? 27.229 58.862  10.882 0.52 15.13 ? 450  GLN   A CA  1 
ATOM   66   C  C   A GLN   A 1 9   ? 27.226 60.093  11.952 0.48 14.46 ? 450  GLN   A C   1 
ATOM   67   C  C   B GLN   A 1 9   ? 27.313 59.925  11.966 0.52 15.80 ? 450  GLN   A C   1 
ATOM   68   O  O   A GLN   A 1 9   ? 28.210 60.228  12.685 0.48 14.29 ? 450  GLN   A O   1 
ATOM   69   O  O   B GLN   A 1 9   ? 28.253 59.910  12.764 0.52 16.60 ? 450  GLN   A O   1 
ATOM   70   C  CB  A GLN   A 1 9   ? 28.162 59.226  9.778  0.48 16.67 ? 450  GLN   A CB  1 
ATOM   71   C  CB  B GLN   A 1 9   ? 28.122 59.238  9.690  0.52 17.66 ? 450  GLN   A CB  1 
ATOM   72   C  CG  A GLN   A 1 9   ? 27.924 60.546  9.063  0.48 20.19 ? 450  GLN   A CG  1 
ATOM   73   C  CG  B GLN   A 1 9   ? 29.589 59.486  10.040 0.52 21.57 ? 450  GLN   A CG  1 
ATOM   74   C  CD  A GLN   A 1 9   ? 28.837 60.739  7.865  0.48 24.01 ? 450  GLN   A CD  1 
ATOM   75   C  CD  B GLN   A 1 9   ? 29.879 60.937  10.411 0.52 24.42 ? 450  GLN   A CD  1 
ATOM   76   O  OE1 A GLN   A 1 9   ? 29.534 59.815  7.446  0.48 25.77 ? 450  GLN   A OE1 1 
ATOM   77   O  OE1 B GLN   A 1 9   ? 29.247 61.862  9.897  0.52 27.52 ? 450  GLN   A OE1 1 
ATOM   78   N  NE2 A GLN   A 1 9   ? 28.834 61.944  7.306  0.48 27.52 ? 450  GLN   A NE2 1 
ATOM   79   N  NE2 B GLN   A 1 9   ? 30.838 61.139  11.312 0.52 26.44 ? 450  GLN   A NE2 1 
ATOM   80   N  N   A ARG   A 1 10  ? 26.171 60.909  12.017 0.48 15.28 ? 451  ARG   A N   1 
ATOM   81   N  N   B ARG   A 1 10  ? 26.351 60.839  12.023 0.52 14.61 ? 451  ARG   A N   1 
ATOM   82   C  CA  A ARG   A 1 10  ? 26.119 61.978  13.010 0.48 15.07 ? 451  ARG   A CA  1 
ATOM   83   C  CA  B ARG   A 1 10  ? 26.400 61.918  13.000 0.52 14.26 ? 451  ARG   A CA  1 
ATOM   84   C  C   A ARG   A 1 10  ? 26.222 61.434  14.427 0.48 15.41 ? 451  ARG   A C   1 
ATOM   85   C  C   B ARG   A 1 10  ? 26.230 61.435  14.439 0.52 15.67 ? 451  ARG   A C   1 
ATOM   86   O  O   A ARG   A 1 10  ? 26.721 62.125  15.323 0.48 16.20 ? 451  ARG   A O   1 
ATOM   87   O  O   B ARG   A 1 10  ? 26.550 62.189  15.365 0.52 17.09 ? 451  ARG   A O   1 
ATOM   88   C  CB  A ARG   A 1 10  ? 24.813 62.754  12.871 0.48 18.49 ? 451  ARG   A CB  1 
ATOM   89   C  CB  B ARG   A 1 10  ? 25.372 62.990  12.635 0.52 13.52 ? 451  ARG   A CB  1 
ATOM   90   C  CG  A ARG   A 1 10  ? 24.714 63.647  11.661 0.48 20.90 ? 451  ARG   A CG  1 
ATOM   91   C  CG  B ARG   A 1 10  ? 25.730 63.767  11.379 0.52 13.80 ? 451  ARG   A CG  1 
ATOM   92   C  CD  A ARG   A 1 10  ? 23.491 64.521  11.785 0.48 22.90 ? 451  ARG   A CD  1 
ATOM   93   C  CD  B ARG   A 1 10  ? 24.794 64.946  11.184 0.52 14.55 ? 451  ARG   A CD  1 
ATOM   94   N  NE  A ARG   A 1 10  ? 22.264 63.857  11.343 0.48 24.07 ? 451  ARG   A NE  1 
ATOM   95   N  NE  B ARG   A 1 10  ? 24.670 65.725  12.411 0.52 16.45 ? 451  ARG   A NE  1 
ATOM   96   C  CZ  A ARG   A 1 10  ? 21.032 64.242  11.680 0.48 20.33 ? 451  ARG   A CZ  1 
ATOM   97   C  CZ  B ARG   A 1 10  ? 25.527 66.671  12.789 0.52 18.42 ? 451  ARG   A CZ  1 
ATOM   98   N  NH1 A ARG   A 1 10  ? 20.852 65.292  12.471 0.48 20.99 ? 451  ARG   A NH1 1 
ATOM   99   N  NH1 B ARG   A 1 10  ? 26.565 66.970  12.027 0.52 15.96 ? 451  ARG   A NH1 1 
ATOM   100  N  NH2 A ARG   A 1 10  ? 19.976 63.583  11.222 0.48 20.06 ? 451  ARG   A NH2 1 
ATOM   101  N  NH2 B ARG   A 1 10  ? 25.343 67.318  13.933 0.52 16.55 ? 451  ARG   A NH2 1 
ATOM   102  N  N   . MET   A 1 11  ? 25.755 60.204  14.655 1.00 13.94 ? 452  MET   A N   1 
ATOM   103  C  CA  . MET   A 1 11  ? 25.815 59.631  15.997 1.00 13.54 ? 452  MET   A CA  1 
ATOM   104  C  C   . MET   A 1 11  ? 27.247 59.397  16.463 1.00 13.76 ? 452  MET   A C   1 
ATOM   105  O  O   . MET   A 1 11  ? 27.456 59.123  17.648 1.00 15.13 ? 452  MET   A O   1 
ATOM   106  C  CB  . MET   A 1 11  ? 25.008 58.338  16.075 1.00 13.01 ? 452  MET   A CB  1 
ATOM   107  C  CG  . MET   A 1 11  ? 23.517 58.581  16.244 1.00 13.51 ? 452  MET   A CG  1 
ATOM   108  S  SD  . MET   A 1 11  ? 22.500 57.102  16.183 1.00 23.53 ? 452  MET   A SD  1 
ATOM   109  C  CE  . MET   A 1 11  ? 22.571 56.677  14.444 1.00 15.06 ? 452  MET   A CE  1 
ATOM   110  N  N   . MET   A 1 12  ? 28.233 59.510  15.568 1.00 13.78 ? 453  MET   A N   1 
ATOM   111  C  CA  . MET   A 1 12  ? 29.630 59.440  15.984 1.00 14.60 ? 453  MET   A CA  1 
ATOM   112  C  C   . MET   A 1 12  ? 30.093 60.679  16.737 1.00 15.23 ? 453  MET   A C   1 
ATOM   113  O  O   . MET   A 1 12  ? 31.156 60.629  17.372 1.00 17.15 ? 453  MET   A O   1 
ATOM   114  C  CB  . MET   A 1 12  ? 30.541 59.243  14.771 1.00 15.82 ? 453  MET   A CB  1 
ATOM   115  C  CG  . MET   A 1 12  ? 30.299 57.962  13.997 1.00 19.24 ? 453  MET   A CG  1 
ATOM   116  S  SD  . MET   A 1 12  ? 31.416 57.825  12.574 1.00 22.83 ? 453  MET   A SD  1 
ATOM   117  C  CE  . MET   A 1 12  ? 33.012 57.683  13.369 1.00 22.60 ? 453  MET   A CE  1 
ATOM   118  N  N   . LEU   A 1 13  ? 29.334 61.779  16.698 1.00 14.78 ? 454  LEU   A N   1 
ATOM   119  C  CA  . LEU   A 1 13  ? 29.820 63.040  17.261 1.00 16.66 ? 454  LEU   A CA  1 
ATOM   120  C  C   . LEU   A 1 13  ? 29.885 63.035  18.788 1.00 17.35 ? 454  LEU   A C   1 
ATOM   121  O  O   . LEU   A 1 13  ? 30.682 63.787  19.363 1.00 19.66 ? 454  LEU   A O   1 
ATOM   122  C  CB  . LEU   A 1 13  ? 28.978 64.207  16.747 1.00 17.43 ? 454  LEU   A CB  1 
ATOM   123  C  CG  . LEU   A 1 13  ? 29.143 64.444  15.241 1.00 17.45 ? 454  LEU   A CG  1 
ATOM   124  C  CD1 . LEU   A 1 13  ? 28.146 65.498  14.772 1.00 19.54 ? 454  LEU   A CD1 1 
ATOM   125  C  CD2 . LEU   A 1 13  ? 30.577 64.837  14.903 1.00 18.18 ? 454  LEU   A CD2 1 
ATOM   126  N  N   . HIS   A 1 14  ? 29.060 62.229  19.452 1.00 14.81 ? 455  HIS   A N   1 
ATOM   127  C  CA  . HIS   A 1 14  ? 29.153 62.030  20.892 1.00 15.13 ? 455  HIS   A CA  1 
ATOM   128  C  C   . HIS   A 1 14  ? 30.512 61.423  21.232 1.00 14.73 ? 455  HIS   A C   1 
ATOM   129  O  O   . HIS   A 1 14  ? 30.883 60.379  20.687 1.00 14.94 ? 455  HIS   A O   1 
ATOM   130  C  CB  . HIS   A 1 14  ? 28.017 61.082  21.286 1.00 14.43 ? 455  HIS   A CB  1 
ATOM   131  C  CG  . HIS   A 1 14  ? 28.134 60.494  22.659 1.00 15.99 ? 455  HIS   A CG  1 
ATOM   132  N  ND1 . HIS   A 1 14  ? 28.135 61.263  23.802 1.00 15.96 ? 455  HIS   A ND1 1 
ATOM   133  C  CD2 . HIS   A 1 14  ? 28.186 59.206  23.073 1.00 13.99 ? 455  HIS   A CD2 1 
ATOM   134  C  CE1 . HIS   A 1 14  ? 28.210 60.475  24.860 1.00 16.27 ? 455  HIS   A CE1 1 
ATOM   135  N  NE2 . HIS   A 1 14  ? 28.247 59.221  24.444 1.00 14.61 ? 455  HIS   A NE2 1 
ATOM   136  N  N   . HIS   A 1 15  ? 31.269 62.082  22.113 1.00 14.84 ? 456  HIS   A N   1 
ATOM   137  C  CA  . HIS   A 1 15  ? 32.634 61.647  22.374 1.00 14.93 ? 456  HIS   A CA  1 
ATOM   138  C  C   . HIS   A 1 15  ? 33.071 62.026  23.784 1.00 16.50 ? 456  HIS   A C   1 
ATOM   139  O  O   . HIS   A 1 15  ? 32.463 62.867  24.452 1.00 17.03 ? 456  HIS   A O   1 
ATOM   140  C  CB  . HIS   A 1 15  ? 33.610 62.227  21.344 1.00 15.40 ? 456  HIS   A CB  1 
ATOM   141  C  CG  . HIS   A 1 15  ? 33.815 63.705  21.472 1.00 16.34 ? 456  HIS   A CG  1 
ATOM   142  N  ND1 . HIS   A 1 15  ? 32.898 64.621  21.003 1.00 19.81 ? 456  HIS   A ND1 1 
ATOM   143  C  CD2 . HIS   A 1 15  ? 34.831 64.427  22.006 1.00 19.21 ? 456  HIS   A CD2 1 
ATOM   144  C  CE1 . HIS   A 1 15  ? 33.336 65.844  21.247 1.00 22.96 ? 456  HIS   A CE1 1 
ATOM   145  N  NE2 . HIS   A 1 15  ? 34.503 65.754  21.860 1.00 21.00 ? 456  HIS   A NE2 1 
ATOM   146  N  N   . ASN   A 1 16  ? 34.163 61.396  24.214 1.00 18.02 ? 457  ASN   A N   1 
ATOM   147  C  CA  . ASN   A 1 16  ? 34.720 61.600  25.546 1.00 17.87 ? 457  ASN   A CA  1 
ATOM   148  C  C   . ASN   A 1 16  ? 35.861 62.605  25.421 1.00 16.94 ? 457  ASN   A C   1 
ATOM   149  O  O   . ASN   A 1 16  ? 36.894 62.311  24.806 1.00 18.88 ? 457  ASN   A O   1 
ATOM   150  C  CB  . ASN   A 1 16  ? 35.196 60.266  26.123 1.00 16.50 ? 457  ASN   A CB  1 
ATOM   151  C  CG  . ASN   A 1 16  ? 35.575 60.365  27.587 1.00 17.74 ? 457  ASN   A CG  1 
ATOM   152  O  OD1 . ASN   A 1 16  ? 36.200 61.336  28.009 1.00 22.10 ? 457  ASN   A OD1 1 
ATOM   153  N  ND2 . ASN   A 1 16  ? 35.205 59.358  28.368 1.00 16.03 ? 457  ASN   A ND2 1 
ATOM   154  N  N   . MET   A 1 17  ? 35.667 63.795  26.000 1.00 18.92 ? 458  MET   A N   1 
ATOM   155  C  CA  . MET   A 1 17  ? 36.646 64.863  25.822 1.00 23.99 ? 458  MET   A CA  1 
ATOM   156  C  C   . MET   A 1 17  ? 37.942 64.599  26.571 1.00 20.44 ? 458  MET   A C   1 
ATOM   157  O  O   . MET   A 1 17  ? 38.969 65.181  26.222 1.00 21.38 ? 458  MET   A O   1 
ATOM   158  C  CB  . MET   A 1 17  ? 36.095 66.213  26.284 1.00 33.74 ? 458  MET   A CB  1 
ATOM   159  C  CG  . MET   A 1 17  ? 34.913 66.718  25.480 1.00 44.52 ? 458  MET   A CG  1 
ATOM   160  S  SD  . MET   A 1 17  ? 34.113 68.131  26.268 1.00 46.77 ? 458  MET   A SD  1 
ATOM   161  C  CE  . MET   A 1 17  ? 35.532 68.945  26.973 1.00 44.90 ? 458  MET   A CE  1 
ATOM   162  N  N   . TRP   A 1 18  ? 37.912 63.756  27.595 1.00 22.78 ? 459  TRP   A N   1 
ATOM   163  C  CA  . TRP   A 1 18  ? 39.094 63.500  28.401 1.00 27.25 ? 459  TRP   A CA  1 
ATOM   164  C  C   . TRP   A 1 18  ? 39.837 62.240  27.987 1.00 27.58 ? 459  TRP   A C   1 
ATOM   165  O  O   . TRP   A 1 18  ? 41.047 62.148  28.216 1.00 27.92 ? 459  TRP   A O   1 
ATOM   166  C  CB  . TRP   A 1 18  ? 38.697 63.402  29.880 1.00 30.95 ? 459  TRP   A CB  1 
ATOM   167  C  CG  . TRP   A 1 18  ? 38.714 64.723  30.572 1.00 39.63 ? 459  TRP   A CG  1 
ATOM   168  C  CD1 . TRP   A 1 18  ? 37.695 65.627  30.641 1.00 44.27 ? 459  TRP   A CD1 1 
ATOM   169  C  CD2 . TRP   A 1 18  ? 39.813 65.300  31.287 1.00 46.22 ? 459  TRP   A CD2 1 
ATOM   170  N  NE1 . TRP   A 1 18  ? 38.092 66.732  31.357 1.00 46.83 ? 459  TRP   A NE1 1 
ATOM   171  C  CE2 . TRP   A 1 18  ? 39.388 66.555  31.764 1.00 45.31 ? 459  TRP   A CE2 1 
ATOM   172  C  CE3 . TRP   A 1 18  ? 41.115 64.878  31.567 1.00 43.73 ? 459  TRP   A CE3 1 
ATOM   173  C  CZ2 . TRP   A 1 18  ? 40.218 67.390  32.509 1.00 39.22 ? 459  TRP   A CZ2 1 
ATOM   174  C  CZ3 . TRP   A 1 18  ? 41.935 65.707  32.304 1.00 36.78 ? 459  TRP   A CZ3 1 
ATOM   175  C  CH2 . TRP   A 1 18  ? 41.485 66.950  32.763 1.00 39.85 ? 459  TRP   A CH2 1 
ATOM   176  N  N   . ASP   A 1 19  ? 39.151 61.284  27.362 1.00 29.91 ? 460  ASP   A N   1 
ATOM   177  C  CA  . ASP   A 1 19  ? 39.702 59.956  27.095 1.00 24.32 ? 460  ASP   A CA  1 
ATOM   178  C  C   . ASP   A 1 19  ? 39.199 59.545  25.714 1.00 23.59 ? 460  ASP   A C   1 
ATOM   179  O  O   . ASP   A 1 19  ? 38.135 58.932  25.592 1.00 24.04 ? 460  ASP   A O   1 
ATOM   180  C  CB  . ASP   A 1 19  ? 39.238 58.986  28.175 1.00 22.55 ? 460  ASP   A CB  1 
ATOM   181  C  CG  . ASP   A 1 19  ? 39.728 57.568  27.954 1.00 19.85 ? 460  ASP   A CG  1 
ATOM   182  O  OD1 . ASP   A 1 19  ? 40.626 57.351  27.113 1.00 21.27 ? 460  ASP   A OD1 1 
ATOM   183  O  OD2 . ASP   A 1 19  ? 39.187 56.664  28.627 1.00 21.80 ? 460  ASP   A OD2 1 
ATOM   184  N  N   . SER   A 1 20  ? 39.975 59.879  24.682 1.00 23.34 ? 461  SER   A N   1 
ATOM   185  C  CA  . SER   A 1 20  ? 39.608 59.519  23.320 1.00 23.71 ? 461  SER   A CA  1 
ATOM   186  C  C   . SER   A 1 20  ? 39.636 58.016  23.077 1.00 25.19 ? 461  SER   A C   1 
ATOM   187  O  O   . SER   A 1 20  ? 39.132 57.567  22.041 1.00 30.04 ? 461  SER   A O   1 
ATOM   188  C  CB  . SER   A 1 20  ? 40.535 60.223  22.331 1.00 26.58 ? 461  SER   A CB  1 
ATOM   189  O  OG  . SER   A 1 20  ? 41.844 59.681  22.399 1.00 29.60 ? 461  SER   A OG  1 
ATOM   190  N  N   . HIS   A 1 21  ? 40.205 57.235  23.996 1.00 22.53 ? 462  HIS   A N   1 
ATOM   191  C  CA  . HIS   A 1 21  ? 40.251 55.785  23.896 1.00 21.19 ? 462  HIS   A CA  1 
ATOM   192  C  C   . HIS   A 1 21  ? 39.208 55.101  24.772 1.00 18.32 ? 462  HIS   A C   1 
ATOM   193  O  O   . HIS   A 1 21  ? 39.258 53.880  24.941 1.00 20.02 ? 462  HIS   A O   1 
ATOM   194  C  CB  . HIS   A 1 21  ? 41.658 55.279  24.220 1.00 26.08 ? 462  HIS   A CB  1 
ATOM   195  C  CG  . HIS   A 1 21  ? 42.713 55.838  23.319 1.00 35.20 ? 462  HIS   A CG  1 
ATOM   196  N  ND1 . HIS   A 1 21  ? 43.188 55.160  22.218 1.00 40.72 ? 462  HIS   A ND1 1 
ATOM   197  C  CD2 . HIS   A 1 21  ? 43.378 57.018  23.349 1.00 37.20 ? 462  HIS   A CD2 1 
ATOM   198  C  CE1 . HIS   A 1 21  ? 44.103 55.895  21.610 1.00 40.23 ? 462  HIS   A CE1 1 
ATOM   199  N  NE2 . HIS   A 1 21  ? 44.236 57.028  22.277 1.00 40.24 ? 462  HIS   A NE2 1 
ATOM   200  N  N   . HIS   A 1 22  ? 38.268 55.859  25.323 1.00 16.80 ? 463  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 22  ? 37.181 55.255  26.069 1.00 15.71 ? 463  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 22  ? 36.461 54.237  25.182 1.00 17.34 ? 463  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 22  ? 36.229 54.504  23.999 1.00 17.09 ? 463  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 22  ? 36.206 56.344  26.510 1.00 16.88 ? 463  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 22  ? 35.102 55.842  27.376 1.00 18.14 ? 463  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 22  ? 34.082 55.051  26.894 1.00 20.22 ? 463  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 22  ? 34.853 56.019  28.694 1.00 20.03 ? 463  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 22  ? 33.255 54.757  27.881 1.00 19.50 ? 463  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 22  ? 33.702 55.330  28.986 1.00 20.13 ? 463  HIS   A NE2 1 
ATOM   210  N  N   . PRO   A 1 23  ? 36.083 53.072  25.722 1.00 15.00 ? 464  PRO   A N   1 
ATOM   211  C  CA  . PRO   A 1 23  ? 35.586 51.983  24.849 1.00 16.14 ? 464  PRO   A CA  1 
ATOM   212  C  C   . PRO   A 1 23  ? 34.294 52.282  24.095 1.00 14.96 ? 464  PRO   A C   1 
ATOM   213  O  O   . PRO   A 1 23  ? 34.055 51.659  23.053 1.00 15.23 ? 464  PRO   A O   1 
ATOM   214  C  CB  . PRO   A 1 23  ? 35.407 50.797  25.810 1.00 17.45 ? 464  PRO   A CB  1 
ATOM   215  C  CG  . PRO   A 1 23  ? 35.381 51.390  27.177 1.00 18.14 ? 464  PRO   A CG  1 
ATOM   216  C  CD  . PRO   A 1 23  ? 36.222 52.644  27.126 1.00 15.22 ? 464  PRO   A CD  1 
ATOM   217  N  N   . GLU   A 1 24  ? 33.432 53.168  24.600 1.00 13.23 ? 465  GLU   A N   1 
ATOM   218  C  CA  . GLU   A 1 24  ? 32.197 53.516  23.896 1.00 13.52 ? 465  GLU   A CA  1 
ATOM   219  C  C   . GLU   A 1 24  ? 32.555 54.526  22.806 1.00 13.31 ? 465  GLU   A C   1 
ATOM   220  O  O   . GLU   A 1 24  ? 32.280 55.726  22.897 1.00 14.50 ? 465  GLU   A O   1 
ATOM   221  C  CB  . GLU   A 1 24  ? 31.153 54.057  24.862 1.00 13.31 ? 465  GLU   A CB  1 
ATOM   222  C  CG  . GLU   A 1 24  ? 29.711 53.795  24.403 1.00 14.42 ? 465  GLU   A CG  1 
ATOM   223  C  CD  . GLU   A 1 24  ? 29.305 54.639  23.198 1.00 16.31 ? 465  GLU   A CD  1 
ATOM   224  O  OE1 . GLU   A 1 24  ? 28.782 55.761  23.386 1.00 16.19 ? 465  GLU   A OE1 1 
ATOM   225  O  OE2 . GLU   A 1 24  ? 29.547 54.192  22.055 1.00 16.22 ? 465  GLU   A OE2 1 
ATOM   226  N  N   . LEU   A 1 25  ? 33.204 54.004  21.754 1.00 14.30 ? 466  LEU   A N   1 
ATOM   227  C  CA  . LEU   A 1 25  ? 33.881 54.775  20.716 1.00 14.17 ? 466  LEU   A CA  1 
ATOM   228  C  C   . LEU   A 1 25  ? 32.905 55.204  19.623 1.00 16.46 ? 466  LEU   A C   1 
ATOM   229  O  O   . LEU   A 1 25  ? 32.026 54.431  19.227 1.00 15.22 ? 466  LEU   A O   1 
ATOM   230  C  CB  . LEU   A 1 25  ? 34.959 53.923  20.055 1.00 14.84 ? 466  LEU   A CB  1 
ATOM   231  C  CG  . LEU   A 1 25  ? 36.268 53.727  20.815 1.00 16.97 ? 466  LEU   A CG  1 
ATOM   232  C  CD1 . LEU   A 1 25  ? 37.086 52.653  20.130 1.00 17.99 ? 466  LEU   A CD1 1 
ATOM   233  C  CD2 . LEU   A 1 25  ? 37.047 55.034  20.856 1.00 18.27 ? 466  LEU   A CD2 1 
ATOM   234  N  N   . PRO   A 1 26  ? 33.085 56.407  19.083 1.00 15.43 ? 467  PRO   A N   1 
ATOM   235  C  CA  . PRO   A 1 26  ? 32.332 56.793  17.880 1.00 15.64 ? 467  PRO   A CA  1 
ATOM   236  C  C   . PRO   A 1 26  ? 32.383 55.743  16.785 1.00 14.46 ? 467  PRO   A C   1 
ATOM   237  O  O   . PRO   A 1 26  ? 31.361 55.471  16.135 1.00 15.43 ? 467  PRO   A O   1 
ATOM   238  C  CB  . PRO   A 1 26  ? 33.015 58.099  17.454 1.00 16.86 ? 467  PRO   A CB  1 
ATOM   239  C  CG  . PRO   A 1 26  ? 33.529 58.674  18.741 1.00 15.28 ? 467  PRO   A CG  1 
ATOM   240  C  CD  . PRO   A 1 26  ? 33.927 57.500  19.603 1.00 16.17 ? 467  PRO   A CD  1 
ATOM   241  N  N   . GLN   A 1 27  ? 33.532 55.107  16.588 1.00 14.96 ? 468  GLN   A N   1 
ATOM   242  C  CA  . GLN   A 1 27  ? 33.672 54.191  15.469 1.00 14.24 ? 468  GLN   A CA  1 
ATOM   243  C  C   . GLN   A 1 27  ? 32.988 52.848  15.689 1.00 14.11 ? 468  GLN   A C   1 
ATOM   244  O  O   . GLN   A 1 27  ? 33.015 52.020  14.780 1.00 15.76 ? 468  GLN   A O   1 
ATOM   245  C  CB  . GLN   A 1 27  ? 35.145 54.002  15.087 1.00 17.39 ? 468  GLN   A CB  1 
ATOM   246  C  CG  . GLN   A 1 27  ? 36.056 53.624  16.239 1.00 24.30 ? 468  GLN   A CG  1 
ATOM   247  C  CD  . GLN   A 1 27  ? 36.759 54.819  16.862 1.00 28.41 ? 468  GLN   A CD  1 
ATOM   248  O  OE1 . GLN   A 1 27  ? 36.152 55.862  17.096 1.00 26.97 ? 468  GLN   A OE1 1 
ATOM   249  N  NE2 . GLN   A 1 27  ? 38.059 54.669  17.126 1.00 30.20 ? 468  GLN   A NE2 1 
ATOM   250  N  N   . ARG   A 1 28  ? 32.384 52.599  16.862 1.00 12.61 ? 469  ARG   A N   1 
ATOM   251  C  CA  . ARG   A 1 28  ? 31.566 51.397  17.011 1.00 12.26 ? 469  ARG   A CA  1 
ATOM   252  C  C   . ARG   A 1 28  ? 30.530 51.302  15.895 1.00 13.16 ? 469  ARG   A C   1 
ATOM   253  O  O   . ARG   A 1 28  ? 30.376 50.250  15.263 1.00 14.39 ? 469  ARG   A O   1 
ATOM   254  C  CB  . ARG   A 1 28  ? 30.859 51.400  18.364 1.00 13.73 ? 469  ARG   A CB  1 
ATOM   255  C  CG  . ARG   A 1 28  ? 31.827 51.240  19.515 1.00 12.24 ? 469  ARG   A CG  1 
ATOM   256  C  CD  . ARG   A 1 28  ? 31.140 51.386  20.874 1.00 15.50 ? 469  ARG   A CD  1 
ATOM   257  N  NE  . ARG   A 1 28  ? 30.155 50.330  21.061 1.00 14.94 ? 469  ARG   A NE  1 
ATOM   258  C  CZ  . ARG   A 1 28  ? 28.842 50.513  21.162 1.00 15.18 ? 469  ARG   A CZ  1 
ATOM   259  N  NH1 . ARG   A 1 28  ? 28.322 51.734  21.141 1.00 14.92 ? 469  ARG   A NH1 1 
ATOM   260  N  NH2 . ARG   A 1 28  ? 28.054 49.452  21.271 1.00 16.54 ? 469  ARG   A NH2 1 
ATOM   261  N  N   . ILE   A 1 29  ? 29.828 52.404  15.620 1.00 11.55 ? 470  ILE   A N   1 
ATOM   262  C  CA  . ILE   A 1 29  ? 28.749 52.338  14.637 1.00 13.44 ? 470  ILE   A CA  1 
ATOM   263  C  C   . ILE   A 1 29  ? 29.281 52.362  13.210 1.00 15.01 ? 470  ILE   A C   1 
ATOM   264  O  O   . ILE   A 1 29  ? 28.754 51.666  12.339 1.00 14.88 ? 470  ILE   A O   1 
ATOM   265  C  CB  . ILE   A 1 29  ? 27.657 53.397  14.880 1.00 13.21 ? 470  ILE   A CB  1 
ATOM   266  C  CG1 . ILE   A 1 29  ? 28.225 54.821  14.840 1.00 14.51 ? 470  ILE   A CG1 1 
ATOM   267  C  CG2 . ILE   A 1 29  ? 26.920 53.107  16.200 1.00 12.46 ? 470  ILE   A CG2 1 
ATOM   268  C  CD1 . ILE   A 1 29  ? 27.160 55.899  14.729 1.00 14.42 ? 470  ILE   A CD1 1 
ATOM   269  N  N   . SER   A 1 30  ? 30.323 53.152  12.935 1.00 14.51 ? 471  SER   A N   1 
ATOM   270  C  CA  . SER   A 1 30  ? 30.856 53.158  11.572 1.00 13.43 ? 471  SER   A CA  1 
ATOM   271  C  C   . SER   A 1 30  ? 31.488 51.821  11.215 1.00 13.24 ? 471  SER   A C   1 
ATOM   272  O  O   . SER   A 1 30  ? 31.434 51.398  10.055 1.00 15.27 ? 471  SER   A O   1 
ATOM   273  C  CB  . SER   A 1 30  ? 31.842 54.311  11.368 1.00 15.36 ? 471  SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 30  ? 32.918 54.246  12.278 1.00 16.93 ? 471  SER   A OG  1 
ATOM   275  N  N   . ARG   A 1 31  ? 32.085 51.141  12.192 1.00 13.27 ? 472  ARG   A N   1 
ATOM   276  C  CA  . ARG   A 1 31  ? 32.666 49.832  11.920 1.00 12.40 ? 472  ARG   A CA  1 
ATOM   277  C  C   . ARG   A 1 31  ? 31.590 48.810  11.576 1.00 13.10 ? 472  ARG   A C   1 
ATOM   278  O  O   . ARG   A 1 31  ? 31.760 48.008  10.652 1.00 13.57 ? 472  ARG   A O   1 
ATOM   279  C  CB  . ARG   A 1 31  ? 33.514 49.371  13.108 1.00 13.68 ? 472  ARG   A CB  1 
ATOM   280  C  CG  . ARG   A 1 31  ? 34.898 50.036  13.176 1.00 13.17 ? 472  ARG   A CG  1 
ATOM   281  C  CD  . ARG   A 1 31  ? 35.817 49.556  12.048 1.00 14.18 ? 472  ARG   A CD  1 
ATOM   282  N  NE  . ARG   A 1 31  ? 36.072 48.124  12.135 1.00 14.16 ? 472  ARG   A NE  1 
ATOM   283  C  CZ  . ARG   A 1 31  ? 36.997 47.580  12.917 1.00 14.76 ? 472  ARG   A CZ  1 
ATOM   284  N  NH1 . ARG   A 1 31  ? 37.770 48.356  13.663 1.00 16.73 ? 472  ARG   A NH1 1 
ATOM   285  N  NH2 . ARG   A 1 31  ? 37.145 46.263  12.946 1.00 16.98 ? 472  ARG   A NH2 1 
ATOM   286  N  N   . ILE   A 1 32  ? 30.484 48.808  12.322 1.00 12.86 ? 473  ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 32  ? 29.406 47.882  12.002 1.00 11.53 ? 473  ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 32  ? 28.849 48.178  10.621 1.00 12.47 ? 473  ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 32  ? 28.641 47.266  9.817  1.00 13.00 ? 473  ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 32  ? 28.317 47.924  13.089 1.00 11.58 ? 473  ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 32  ? 28.865 47.417  14.428 1.00 12.40 ? 473  ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 32  ? 27.098 47.124  12.633 1.00 14.92 ? 473  ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 32  ? 27.997 47.833  15.614 1.00 13.86 ? 473  ILE   A CD1 1 
ATOM   294  N  N   . PHE   A 1 33  ? 28.613 49.457  10.321 1.00 12.89 ? 474  PHE   A N   1 
ATOM   295  C  CA  . PHE   A 1 33  ? 28.111 49.840  9.006  1.00 12.28 ? 474  PHE   A CA  1 
ATOM   296  C  C   . PHE   A 1 33  ? 29.072 49.400  7.909  1.00 14.88 ? 474  PHE   A C   1 
ATOM   297  O  O   . PHE   A 1 33  ? 28.656 48.813  6.906  1.00 15.37 ? 474  PHE   A O   1 
ATOM   298  C  CB  . PHE   A 1 33  ? 27.906 51.350  8.979  1.00 13.77 ? 474  PHE   A CB  1 
ATOM   299  C  CG  . PHE   A 1 33  ? 27.245 51.861  7.738  1.00 15.10 ? 474  PHE   A CG  1 
ATOM   300  C  CD1 . PHE   A 1 33  ? 25.874 51.743  7.572  1.00 15.40 ? 474  PHE   A CD1 1 
ATOM   301  C  CD2 . PHE   A 1 33  ? 27.988 52.496  6.758  1.00 15.55 ? 474  PHE   A CD2 1 
ATOM   302  C  CE1 . PHE   A 1 33  ? 25.258 52.232  6.436  1.00 17.56 ? 474  PHE   A CE1 1 
ATOM   303  C  CE2 . PHE   A 1 33  ? 27.381 52.993  5.634  1.00 17.04 ? 474  PHE   A CE2 1 
ATOM   304  C  CZ  . PHE   A 1 33  ? 26.019 52.862  5.477  1.00 17.68 ? 474  PHE   A CZ  1 
ATOM   305  N  N   . SER   A 1 34  ? 30.369 49.652  8.103  1.00 14.69 ? 475  SER   A N   1 
ATOM   306  C  CA  . SER   A 1 34  ? 31.367 49.272  7.108  1.00 14.15 ? 475  SER   A CA  1 
ATOM   307  C  C   . SER   A 1 34  ? 31.362 47.770  6.859  1.00 13.10 ? 475  SER   A C   1 
ATOM   308  O  O   . SER   A 1 34  ? 31.506 47.322  5.714  1.00 14.10 ? 475  SER   A O   1 
ATOM   309  C  CB  . SER   A 1 34  ? 32.745 49.721  7.591  1.00 14.90 ? 475  SER   A CB  1 
ATOM   310  O  OG  . SER   A 1 34  ? 33.765 49.212  6.739  1.00 17.55 ? 475  SER   A OG  1 
ATOM   311  N  N   . ARG   A 1 35  ? 31.220 46.968  7.919  1.00 12.42 ? 476  ARG   A N   1 
ATOM   312  C  CA  . ARG   A 1 35  ? 31.211 45.525  7.724  1.00 12.65 ? 476  ARG   A CA  1 
ATOM   313  C  C   . ARG   A 1 35  ? 29.987 45.079  6.936  1.00 13.25 ? 476  ARG   A C   1 
ATOM   314  O  O   . ARG   A 1 35  ? 30.073 44.139  6.140  1.00 13.82 ? 476  ARG   A O   1 
ATOM   315  C  CB  . ARG   A 1 35  ? 31.321 44.810  9.071  1.00 12.62 ? 476  ARG   A CB  1 
ATOM   316  C  CG  . ARG   A 1 35  ? 31.505 43.311  8.967  1.00 14.20 ? 476  ARG   A CG  1 
ATOM   317  C  CD  . ARG   A 1 35  ? 32.853 42.957  8.360  1.00 16.11 ? 476  ARG   A CD  1 
ATOM   318  N  NE  . ARG   A 1 35  ? 33.062 41.513  8.379  1.00 18.45 ? 476  ARG   A NE  1 
ATOM   319  C  CZ  . ARG   A 1 35  ? 33.663 40.823  7.415  1.00 19.54 ? 476  ARG   A CZ  1 
ATOM   320  N  NH1 . ARG   A 1 35  ? 34.133 41.435  6.330  1.00 18.98 ? 476  ARG   A NH1 1 
ATOM   321  N  NH2 . ARG   A 1 35  ? 33.781 39.510  7.534  1.00 19.45 ? 476  ARG   A NH2 1 
ATOM   322  N  N   . HIS   A 1 36  ? 28.852 45.758  7.128  1.00 13.99 ? 477  HIS   A N   1 
ATOM   323  C  CA  . HIS   A 1 36  ? 27.674 45.480  6.317  1.00 15.89 ? 477  HIS   A CA  1 
ATOM   324  C  C   . HIS   A 1 36  ? 27.953 45.752  4.839  1.00 17.58 ? 477  HIS   A C   1 
ATOM   325  O  O   . HIS   A 1 36  ? 27.530 44.985  3.964  1.00 16.68 ? 477  HIS   A O   1 
ATOM   326  C  CB  . HIS   A 1 36  ? 26.490 46.328  6.799  1.00 14.64 ? 477  HIS   A CB  1 
ATOM   327  C  CG  . HIS   A 1 36  ? 25.768 45.777  7.992  1.00 14.75 ? 477  HIS   A CG  1 
ATOM   328  N  ND1 . HIS   A 1 36  ? 26.299 45.794  9.264  1.00 14.03 ? 477  HIS   A ND1 1 
ATOM   329  C  CD2 . HIS   A 1 36  ? 24.541 45.214  8.107  1.00 14.83 ? 477  HIS   A CD2 1 
ATOM   330  C  CE1 . HIS   A 1 36  ? 25.433 45.261  10.108 1.00 15.15 ? 477  HIS   A CE1 1 
ATOM   331  N  NE2 . HIS   A 1 36  ? 24.357 44.900  9.430  1.00 14.52 ? 477  HIS   A NE2 1 
ATOM   332  N  N   . GLU   A 1 37  ? 28.661 46.841  4.541  1.00 17.59 ? 478  GLU   A N   1 
ATOM   333  C  CA  . GLU   A 1 37  ? 29.001 47.133  3.150  1.00 19.69 ? 478  GLU   A CA  1 
ATOM   334  C  C   . GLU   A 1 37  ? 29.977 46.102  2.593  1.00 19.69 ? 478  GLU   A C   1 
ATOM   335  O  O   . GLU   A 1 37  ? 29.808 45.616  1.467  1.00 18.85 ? 478  GLU   A O   1 
ATOM   336  C  CB  . GLU   A 1 37  ? 29.583 48.543  3.049  1.00 22.62 ? 478  GLU   A CB  1 
ATOM   337  C  CG  . GLU   A 1 37  ? 29.715 49.063  1.626  1.00 37.29 ? 478  GLU   A CG  1 
ATOM   338  C  CD  . GLU   A 1 37  ? 29.699 50.578  1.558  1.00 50.09 ? 478  GLU   A CD  1 
ATOM   339  O  OE1 . GLU   A 1 37  ? 30.303 51.218  2.446  1.00 54.22 ? 478  GLU   A OE1 1 
ATOM   340  O  OE2 . GLU   A 1 37  ? 29.084 51.129  0.617  1.00 55.90 ? 478  GLU   A OE2 1 
ATOM   341  N  N   . GLU   A 1 38  ? 30.994 45.750  3.384  1.00 20.37 ? 479  GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 38  ? 32.016 44.790  2.975  1.00 20.92 ? 479  GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 38  ? 31.412 43.442  2.615  1.00 18.94 ? 479  GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 38  ? 31.838 42.795  1.646  1.00 20.66 ? 479  GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 38  ? 32.944 44.581  4.162  1.00 23.46 ? 479  GLU   A CB  1 
ATOM   346  C  CG  . GLU   A 1 38  ? 34.388 44.720  3.896  1.00 25.22 ? 479  GLU   A CG  1 
ATOM   347  C  CD  . GLU   A 1 38  ? 35.171 44.862  5.188  1.00 26.29 ? 479  GLU   A CD  1 
ATOM   348  O  OE1 . GLU   A 1 38  ? 34.897 44.110  6.144  1.00 21.54 ? 479  GLU   A OE1 1 
ATOM   349  O  OE2 . GLU   A 1 38  ? 36.049 45.739  5.248  1.00 24.80 ? 479  GLU   A OE2 1 
ATOM   350  N  N   . LEU   A 1 39  ? 30.443 42.985  3.407  1.00 16.89 ? 480  LEU   A N   1 
ATOM   351  C  CA  . LEU   A 1 39  ? 29.754 41.726  3.180  1.00 17.17 ? 480  LEU   A CA  1 
ATOM   352  C  C   . LEU   A 1 39  ? 28.617 41.842  2.173  1.00 16.62 ? 480  LEU   A C   1 
ATOM   353  O  O   . LEU   A 1 39  ? 27.938 40.837  1.922  1.00 19.13 ? 480  LEU   A O   1 
ATOM   354  C  CB  . LEU   A 1 39  ? 29.217 41.168  4.499  1.00 16.69 ? 480  LEU   A CB  1 
ATOM   355  C  CG  . LEU   A 1 39  ? 30.290 40.745  5.497  1.00 15.72 ? 480  LEU   A CG  1 
ATOM   356  C  CD1 . LEU   A 1 39  ? 29.670 40.513  6.877  1.00 17.06 ? 480  LEU   A CD1 1 
ATOM   357  C  CD2 . LEU   A 1 39  ? 31.012 39.496  4.973  1.00 18.77 ? 480  LEU   A CD2 1 
ATOM   358  N  N   . ARG   A 1 40  ? 28.382 43.036  1.622  1.00 16.59 ? 481  ARG   A N   1 
ATOM   359  C  CA  . ARG   A 1 40  ? 27.330 43.257  0.629  1.00 15.94 ? 481  ARG   A CA  1 
ATOM   360  C  C   . ARG   A 1 40  ? 25.934 43.023  1.201  1.00 17.91 ? 481  ARG   A C   1 
ATOM   361  O  O   . ARG   A 1 40  ? 25.000 42.650  0.478  1.00 21.54 ? 481  ARG   A O   1 
ATOM   362  C  CB  . ARG   A 1 40  ? 27.569 42.465  -0.661 1.00 20.35 ? 481  ARG   A CB  1 
ATOM   363  C  CG  . ARG   A 1 40  ? 28.836 42.880  -1.377 1.00 28.45 ? 481  ARG   A CG  1 
ATOM   364  C  CD  . ARG   A 1 40  ? 29.011 42.100  -2.672 1.00 34.59 ? 481  ARG   A CD  1 
ATOM   365  N  NE  . ARG   A 1 40  ? 30.318 42.347  -3.271 1.00 37.90 ? 481  ARG   A NE  1 
ATOM   366  C  CZ  . ARG   A 1 40  ? 30.728 41.816  -4.417 1.00 40.13 ? 481  ARG   A CZ  1 
ATOM   367  N  NH1 . ARG   A 1 40  ? 29.931 41.001  -5.098 1.00 39.83 ? 481  ARG   A NH1 1 
ATOM   368  N  NH2 . ARG   A 1 40  ? 31.933 42.102  -4.883 1.00 39.43 ? 481  ARG   A NH2 1 
ATOM   369  N  N   . LEU   A 1 41  ? 25.788 43.237  2.509  1.00 16.86 ? 482  LEU   A N   1 
ATOM   370  C  CA  . LEU   A 1 41  ? 24.496 43.194  3.176  1.00 15.53 ? 482  LEU   A CA  1 
ATOM   371  C  C   . LEU   A 1 41  ? 23.764 44.524  3.088  1.00 16.14 ? 482  LEU   A C   1 
ATOM   372  O  O   . LEU   A 1 41  ? 22.528 44.543  3.045  1.00 16.03 ? 482  LEU   A O   1 
ATOM   373  C  CB  . LEU   A 1 41  ? 24.673 42.807  4.649  1.00 16.78 ? 482  LEU   A CB  1 
ATOM   374  C  CG  . LEU   A 1 41  ? 25.318 41.450  4.941  1.00 16.95 ? 482  LEU   A CG  1 
ATOM   375  C  CD1 . LEU   A 1 41  ? 25.769 41.399  6.399  1.00 17.62 ? 482  LEU   A CD1 1 
ATOM   376  C  CD2 . LEU   A 1 41  ? 24.376 40.294  4.636  1.00 18.88 ? 482  LEU   A CD2 1 
ATOM   377  N  N   . LEU   A 1 42  ? 24.494 45.639  3.049  1.00 15.86 ? 483  LEU   A N   1 
ATOM   378  C  CA  . LEU   A 1 42  ? 23.847 46.946  3.077  1.00 16.17 ? 483  LEU   A CA  1 
ATOM   379  C  C   . LEU   A 1 42  ? 22.921 47.149  1.884  1.00 18.49 ? 483  LEU   A C   1 
ATOM   380  O  O   . LEU   A 1 42  ? 21.789 47.622  2.046  1.00 18.75 ? 483  LEU   A O   1 
ATOM   381  C  CB  . LEU   A 1 42  ? 24.893 48.055  3.160  1.00 16.70 ? 483  LEU   A CB  1 
ATOM   382  C  CG  . LEU   A 1 42  ? 24.406 49.504  3.100  1.00 18.15 ? 483  LEU   A CG  1 
ATOM   383  C  CD1 . LEU   A 1 42  ? 23.471 49.831  4.262  1.00 17.82 ? 483  LEU   A CD1 1 
ATOM   384  C  CD2 . LEU   A 1 42  ? 25.606 50.444  3.080  1.00 20.80 ? 483  LEU   A CD2 1 
ATOM   385  N  N   . SER   A 1 43  ? 23.373 46.795  0.678  1.00 18.48 ? 484  SER   A N   1 
ATOM   386  C  CA  . SER   A 1 43  ? 22.546 46.994  -0.512 1.00 19.83 ? 484  SER   A CA  1 
ATOM   387  C  C   . SER   A 1 43  ? 21.307 46.111  -0.514 1.00 21.54 ? 484  SER   A C   1 
ATOM   388  O  O   . SER   A 1 43  ? 20.354 46.406  -1.245 1.00 21.93 ? 484  SER   A O   1 
ATOM   389  C  CB  . SER   A 1 43  ? 23.351 46.766  -1.798 1.00 24.59 ? 484  SER   A CB  1 
ATOM   390  O  OG  . SER   A 1 43  ? 23.878 45.451  -1.868 1.00 29.05 ? 484  SER   A OG  1 
ATOM   391  N  N   . ARG   A 1 44  ? 21.301 45.035  0.273  1.00 18.16 ? 485  ARG   A N   1 
ATOM   392  C  CA  . ARG   A 1 44  ? 20.149 44.151  0.380  1.00 18.12 ? 485  ARG   A CA  1 
ATOM   393  C  C   . ARG   A 1 44  ? 19.071 44.701  1.303  1.00 16.94 ? 485  ARG   A C   1 
ATOM   394  O  O   . ARG   A 1 44  ? 17.967 44.145  1.347  1.00 17.78 ? 485  ARG   A O   1 
ATOM   395  C  CB  . ARG   A 1 44  ? 20.597 42.761  0.848  1.00 15.94 ? 485  ARG   A CB  1 
ATOM   396  C  CG  . ARG   A 1 44  ? 21.570 42.076  -0.126 1.00 16.36 ? 485  ARG   A CG  1 
ATOM   397  C  CD  . ARG   A 1 44  ? 22.093 40.777  0.453  1.00 17.11 ? 485  ARG   A CD  1 
ATOM   398  N  NE  . ARG   A 1 44  ? 21.026 39.810  0.695  1.00 18.36 ? 485  ARG   A NE  1 
ATOM   399  C  CZ  . ARG   A 1 44  ? 21.158 38.726  1.451  1.00 18.35 ? 485  ARG   A CZ  1 
ATOM   400  N  NH1 . ARG   A 1 44  ? 22.316 38.471  2.049  1.00 18.72 ? 485  ARG   A NH1 1 
ATOM   401  N  NH2 . ARG   A 1 44  ? 20.133 37.901  1.620  1.00 19.00 ? 485  ARG   A NH2 1 
ATOM   402  N  N   . CYS   A 1 45  ? 19.354 45.783  2.019  1.00 17.23 ? 486  CYS   A N   1 
ATOM   403  C  CA  . CYS   A 1 45  ? 18.449 46.329  3.015  1.00 16.41 ? 486  CYS   A CA  1 
ATOM   404  C  C   . CYS   A 1 45  ? 17.844 47.619  2.474  1.00 17.66 ? 486  CYS   A C   1 
ATOM   405  O  O   . CYS   A 1 45  ? 18.472 48.340  1.689  1.00 19.96 ? 486  CYS   A O   1 
ATOM   406  C  CB  . CYS   A 1 45  ? 19.241 46.684  4.277  1.00 15.28 ? 486  CYS   A CB  1 
ATOM   407  S  SG  . CYS   A 1 45  ? 19.848 45.275  5.229  1.00 16.77 ? 486  CYS   A SG  1 
ATOM   408  N  N   . HIS   A 1 46  ? 16.622 47.916  2.904  1.00 15.23 ? 487  HIS   A N   1 
ATOM   409  C  CA  . HIS   A 1 46  ? 16.038 49.222  2.638  1.00 16.38 ? 487  HIS   A CA  1 
ATOM   410  C  C   . HIS   A 1 46  ? 16.507 50.207  3.702  1.00 14.21 ? 487  HIS   A C   1 
ATOM   411  O  O   . HIS   A 1 46  ? 16.391 49.943  4.905  1.00 16.27 ? 487  HIS   A O   1 
ATOM   412  C  CB  . HIS   A 1 46  ? 14.512 49.133  2.628  1.00 17.04 ? 487  HIS   A CB  1 
ATOM   413  C  CG  . HIS   A 1 46  ? 13.830 50.460  2.512  1.00 23.80 ? 487  HIS   A CG  1 
ATOM   414  N  ND1 . HIS   A 1 46  ? 13.890 51.235  1.373  1.00 26.21 ? 487  HIS   A ND1 1 
ATOM   415  C  CD2 . HIS   A 1 46  ? 13.075 51.153  3.397  1.00 25.69 ? 487  HIS   A CD2 1 
ATOM   416  C  CE1 . HIS   A 1 46  ? 13.200 52.346  1.561  1.00 25.79 ? 487  HIS   A CE1 1 
ATOM   417  N  NE2 . HIS   A 1 46  ? 12.694 52.320  2.781  1.00 25.99 ? 487  HIS   A NE2 1 
ATOM   418  N  N   . ARG   A 1 47  ? 17.060 51.330  3.268  1.00 15.17 ? 488  ARG   A N   1 
ATOM   419  C  CA  . ARG   A 1 47  ? 17.577 52.331  4.192  1.00 15.72 ? 488  ARG   A CA  1 
ATOM   420  C  C   . ARG   A 1 47  ? 16.412 53.123  4.782  1.00 15.62 ? 488  ARG   A C   1 
ATOM   421  O  O   . ARG   A 1 47  ? 15.662 53.786  4.049  1.00 19.28 ? 488  ARG   A O   1 
ATOM   422  C  CB  . ARG   A 1 47  ? 18.556 53.240  3.449  1.00 16.57 ? 488  ARG   A CB  1 
ATOM   423  C  CG  . ARG   A 1 47  ? 19.391 54.134  4.321  1.00 18.85 ? 488  ARG   A CG  1 
ATOM   424  C  CD  . ARG   A 1 47  ? 20.373 53.349  5.194  1.00 20.71 ? 488  ARG   A CD  1 
ATOM   425  N  NE  . ARG   A 1 47  ? 21.165 54.284  5.983  1.00 19.86 ? 488  ARG   A NE  1 
ATOM   426  C  CZ  . ARG   A 1 47  ? 22.316 54.813  5.590  1.00 18.20 ? 488  ARG   A CZ  1 
ATOM   427  N  NH1 . ARG   A 1 47  ? 22.864 54.469  4.422  1.00 17.88 ? 488  ARG   A NH1 1 
ATOM   428  N  NH2 . ARG   A 1 47  ? 22.930 55.680  6.374  1.00 21.17 ? 488  ARG   A NH2 1 
ATOM   429  N  N   . ILE   A 1 48  ? 16.244 53.036  6.096  1.00 14.82 ? 489  ILE   A N   1 
ATOM   430  C  CA  . ILE   A 1 48  ? 15.207 53.778  6.806  1.00 16.73 ? 489  ILE   A CA  1 
ATOM   431  C  C   . ILE   A 1 48  ? 15.793 55.128  7.189  1.00 16.33 ? 489  ILE   A C   1 
ATOM   432  O  O   . ILE   A 1 48  ? 16.920 55.181  7.693  1.00 17.45 ? 489  ILE   A O   1 
ATOM   433  C  CB  . ILE   A 1 48  ? 14.713 52.987  8.025  1.00 18.07 ? 489  ILE   A CB  1 
ATOM   434  C  CG1 . ILE   A 1 48  ? 13.943 51.742  7.559  1.00 17.53 ? 489  ILE   A CG1 1 
ATOM   435  C  CG2 . ILE   A 1 48  ? 13.910 53.882  8.970  1.00 16.44 ? 489  ILE   A CG2 1 
ATOM   436  C  CD1 . ILE   A 1 48  ? 13.820 50.681  8.630  1.00 19.85 ? 489  ILE   A CD1 1 
ATOM   437  N  N   . PRO   A 1 49  ? 15.093 56.237  6.956  1.00 19.47 ? 490  PRO   A N   1 
ATOM   438  C  CA  . PRO   A 1 49  ? 15.684 57.541  7.272  1.00 23.44 ? 490  PRO   A CA  1 
ATOM   439  C  C   . PRO   A 1 49  ? 15.816 57.748  8.771  1.00 21.94 ? 490  PRO   A C   1 
ATOM   440  O  O   . PRO   A 1 49  ? 14.932 57.396  9.555  1.00 20.81 ? 490  PRO   A O   1 
ATOM   441  C  CB  . PRO   A 1 49  ? 14.701 58.540  6.651  1.00 26.99 ? 490  PRO   A CB  1 
ATOM   442  C  CG  . PRO   A 1 49  ? 13.418 57.807  6.568  1.00 26.57 ? 490  PRO   A CG  1 
ATOM   443  C  CD  . PRO   A 1 49  ? 13.763 56.364  6.333  1.00 23.87 ? 490  PRO   A CD  1 
ATOM   444  N  N   . ALA   A 1 50  ? 16.943 58.318  9.168  1.00 19.20 ? 491  ALA   A N   1 
ATOM   445  C  CA  . ALA   A 1 50  ? 17.140 58.691  10.555 1.00 19.89 ? 491  ALA   A CA  1 
ATOM   446  C  C   . ALA   A 1 50  ? 16.457 60.031  10.835 1.00 19.10 ? 491  ALA   A C   1 
ATOM   447  O  O   . ALA   A 1 50  ? 16.234 60.840  9.932  1.00 20.70 ? 491  ALA   A O   1 
ATOM   448  C  CB  . ALA   A 1 50  ? 18.636 58.797  10.853 1.00 22.91 ? 491  ALA   A CB  1 
ATOM   449  N  N   . ARG   A 1 51  ? 16.124 60.260  12.106 1.00 17.44 ? 492  ARG   A N   1 
ATOM   450  C  CA  . ARG   A 1 51  ? 15.555 61.532  12.541 1.00 16.78 ? 492  ARG   A CA  1 
ATOM   451  C  C   . ARG   A 1 51  ? 15.773 61.684  14.039 1.00 19.24 ? 492  ARG   A C   1 
ATOM   452  O  O   . ARG   A 1 51  ? 16.083 60.719  14.745 1.00 17.05 ? 492  ARG   A O   1 
ATOM   453  C  CB  . ARG   A 1 51  ? 14.054 61.650  12.227 1.00 16.22 ? 492  ARG   A CB  1 
ATOM   454  C  CG  . ARG   A 1 51  ? 13.151 60.840  13.153 1.00 14.81 ? 492  ARG   A CG  1 
ATOM   455  C  CD  . ARG   A 1 51  ? 11.685 61.292  13.024 1.00 15.21 ? 492  ARG   A CD  1 
ATOM   456  N  NE  . ARG   A 1 51  ? 10.726 60.419  13.705 1.00 15.60 ? 492  ARG   A NE  1 
ATOM   457  C  CZ  . ARG   A 1 51  ? 10.301 60.561  14.966 1.00 19.23 ? 492  ARG   A CZ  1 
ATOM   458  N  NH1 . ARG   A 1 51  ? 10.759 61.544  15.737 1.00 17.74 ? 492  ARG   A NH1 1 
ATOM   459  N  NH2 . ARG   A 1 51  ? 9.410  59.711  15.469 1.00 18.30 ? 492  ARG   A NH2 1 
ATOM   460  N  N   . LEU   A 1 52  ? 15.581 62.912  14.519 1.00 16.74 ? 493  LEU   A N   1 
ATOM   461  C  CA  . LEU   A 1 52  ? 15.669 63.214  15.940 1.00 16.29 ? 493  LEU   A CA  1 
ATOM   462  C  C   . LEU   A 1 52  ? 14.344 62.900  16.621 1.00 16.06 ? 493  LEU   A C   1 
ATOM   463  O  O   . LEU   A 1 52  ? 13.274 63.259  16.118 1.00 18.78 ? 493  LEU   A O   1 
ATOM   464  C  CB  . LEU   A 1 52  ? 16.009 64.693  16.156 1.00 18.16 ? 493  LEU   A CB  1 
ATOM   465  C  CG  . LEU   A 1 52  ? 17.359 65.218  15.639 1.00 24.04 ? 493  LEU   A CG  1 
ATOM   466  C  CD1 . LEU   A 1 52  ? 17.624 66.643  16.119 1.00 28.67 ? 493  LEU   A CD1 1 
ATOM   467  C  CD2 . LEU   A 1 52  ? 18.531 64.311  16.023 1.00 21.82 ? 493  LEU   A CD2 1 
ATOM   468  N  N   . ALA   A 1 53  ? 14.414 62.222  17.763 1.00 17.50 ? 494  ALA   A N   1 
ATOM   469  C  CA  . ALA   A 1 53  ? 13.258 62.140  18.641 1.00 17.06 ? 494  ALA   A CA  1 
ATOM   470  C  C   . ALA   A 1 53  ? 12.892 63.535  19.135 1.00 18.82 ? 494  ALA   A C   1 
ATOM   471  O  O   . ALA   A 1 53  ? 13.736 64.438  19.197 1.00 19.97 ? 494  ALA   A O   1 
ATOM   472  C  CB  . ALA   A 1 53  ? 13.580 61.258  19.851 1.00 17.62 ? 494  ALA   A CB  1 
ATOM   473  N  N   . THR   A 1 54  ? 11.622 63.708  19.496 1.00 16.66 ? 495  THR   A N   1 
ATOM   474  C  CA  . THR   A 1 54  ? 11.158 64.940  20.116 1.00 18.15 ? 495  THR   A CA  1 
ATOM   475  C  C   . THR   A 1 54  ? 11.148 64.810  21.634 1.00 18.56 ? 495  THR   A C   1 
ATOM   476  O  O   . THR   A 1 54  ? 11.149 63.708  22.194 1.00 17.41 ? 495  THR   A O   1 
ATOM   477  C  CB  . THR   A 1 54  ? 9.745  65.286  19.650 1.00 19.90 ? 495  THR   A CB  1 
ATOM   478  O  OG1 . THR   A 1 54  ? 8.815  64.355  20.216 1.00 20.15 ? 495  THR   A OG1 1 
ATOM   479  C  CG2 . THR   A 1 54  ? 9.652  65.236  18.135 1.00 20.68 ? 495  THR   A CG2 1 
ATOM   480  N  N   . GLU   A 1 55  ? 11.095 65.967  22.300 1.00 19.17 ? 496  GLU   A N   1 
ATOM   481  C  CA  . GLU   A 1 55  ? 10.977 65.975  23.757 1.00 19.06 ? 496  GLU   A CA  1 
ATOM   482  C  C   . GLU   A 1 55  ? 9.699  65.287  24.218 1.00 19.79 ? 496  GLU   A C   1 
ATOM   483  O  O   . GLU   A 1 55  ? 9.685  64.619  25.259 1.00 18.97 ? 496  GLU   A O   1 
ATOM   484  C  CB  . GLU   A 1 55  ? 11.044 67.407  24.296 1.00 20.56 ? 496  GLU   A CB  1 
ATOM   485  C  CG  . GLU   A 1 55  ? 12.421 68.047  24.182 1.00 23.93 ? 496  GLU   A CG  1 
ATOM   486  C  CD  . GLU   A 1 55  ? 12.456 69.472  24.704 1.00 29.71 ? 496  GLU   A CD  1 
ATOM   487  O  OE1 . GLU   A 1 55  ? 11.822 69.752  25.745 1.00 33.73 ? 496  GLU   A OE1 1 
ATOM   488  O  OE2 . GLU   A 1 55  ? 13.131 70.313  24.071 1.00 29.78 ? 496  GLU   A OE2 1 
ATOM   489  N  N   . GLU   A 1 56  ? 8.610  65.440  23.457 1.00 19.23 ? 497  GLU   A N   1 
ATOM   490  C  CA  . GLU   A 1 56  ? 7.370  64.755  23.805 1.00 22.16 ? 497  GLU   A CA  1 
ATOM   491  C  C   . GLU   A 1 56  ? 7.539  63.242  23.727 1.00 19.93 ? 497  GLU   A C   1 
ATOM   492  O  O   . GLU   A 1 56  ? 7.010  62.503  24.569 1.00 19.22 ? 497  GLU   A O   1 
ATOM   493  C  CB  . GLU   A 1 56  ? 6.238  65.223  22.888 1.00 31.49 ? 497  GLU   A CB  1 
ATOM   494  C  CG  . GLU   A 1 56  ? 5.653  66.580  23.256 1.00 44.01 ? 497  GLU   A CG  1 
ATOM   495  C  CD  . GLU   A 1 56  ? 6.653  67.717  23.093 1.00 56.60 ? 497  GLU   A CD  1 
ATOM   496  O  OE1 . GLU   A 1 56  ? 6.787  68.532  24.032 1.00 59.87 ? 497  GLU   A OE1 1 
ATOM   497  O  OE2 . GLU   A 1 56  ? 7.317  67.786  22.035 1.00 60.48 ? 497  GLU   A OE2 1 
ATOM   498  N  N   . GLU   A 1 57  ? 8.292  62.760  22.733 1.00 17.65 ? 498  GLU   A N   1 
ATOM   499  C  CA  . GLU   A 1 57  ? 8.574  61.332  22.653 1.00 16.61 ? 498  GLU   A CA  1 
ATOM   500  C  C   . GLU   A 1 57  ? 9.429  60.864  23.831 1.00 15.51 ? 498  GLU   A C   1 
ATOM   501  O  O   . GLU   A 1 57  ? 9.189  59.785  24.383 1.00 18.11 ? 498  GLU   A O   1 
ATOM   502  C  CB  . GLU   A 1 57  ? 9.212  61.001  21.306 1.00 16.51 ? 498  GLU   A CB  1 
ATOM   503  C  CG  . GLU   A 1 57  ? 8.178  61.034  20.181 1.00 17.40 ? 498  GLU   A CG  1 
ATOM   504  C  CD  . GLU   A 1 57  ? 8.777  61.076  18.798 1.00 18.75 ? 498  GLU   A CD  1 
ATOM   505  O  OE1 . GLU   A 1 57  ? 9.948  61.485  18.643 1.00 18.27 ? 498  GLU   A OE1 1 
ATOM   506  O  OE2 . GLU   A 1 57  ? 8.043  60.727  17.844 1.00 18.58 ? 498  GLU   A OE2 1 
ATOM   507  N  N   . LEU   A 1 58  ? 10.413 61.665  24.249 1.00 14.78 ? 499  LEU   A N   1 
ATOM   508  C  CA  . LEU   A 1 58  ? 11.225 61.270  25.401 1.00 15.41 ? 499  LEU   A CA  1 
ATOM   509  C  C   . LEU   A 1 58  ? 10.382 61.143  26.660 1.00 18.70 ? 499  LEU   A C   1 
ATOM   510  O  O   . LEU   A 1 58  ? 10.686 60.323  27.538 1.00 17.27 ? 499  LEU   A O   1 
ATOM   511  C  CB  . LEU   A 1 58  ? 12.349 62.280  25.638 1.00 15.61 ? 499  LEU   A CB  1 
ATOM   512  C  CG  . LEU   A 1 58  ? 13.440 62.456  24.582 1.00 15.98 ? 499  LEU   A CG  1 
ATOM   513  C  CD1 . LEU   A 1 58  ? 14.511 63.450  25.071 1.00 18.09 ? 499  LEU   A CD1 1 
ATOM   514  C  CD2 . LEU   A 1 58  ? 14.076 61.120  24.201 1.00 17.03 ? 499  LEU   A CD2 1 
ATOM   515  N  N   . ALA   A 1 59  ? 9.322  61.942  26.765 1.00 18.17 ? 500  ALA   A N   1 
ATOM   516  C  CA  . ALA   A 1 59  ? 8.457  61.919  27.937 1.00 16.66 ? 500  ALA   A CA  1 
ATOM   517  C  C   . ALA   A 1 59  ? 7.627  60.647  28.034 1.00 15.33 ? 500  ALA   A C   1 
ATOM   518  O  O   . ALA   A 1 59  ? 6.977  60.429  29.065 1.00 17.32 ? 500  ALA   A O   1 
ATOM   519  C  CB  . ALA   A 1 59  ? 7.550  63.155  27.949 1.00 17.83 ? 500  ALA   A CB  1 
ATOM   520  N  N   . LEU   A 1 60  ? 7.611  59.810  26.995 1.00 15.92 ? 501  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 60  ? 6.960  58.512  27.120 1.00 16.21 ? 501  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 60  ? 7.580  57.681  28.235 1.00 16.74 ? 501  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 60  ? 6.889  56.854  28.848 1.00 19.12 ? 501  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 60  ? 7.062  57.755  25.799 1.00 18.68 ? 501  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 60  ? 6.261  58.335  24.637 1.00 19.28 ? 501  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 60  ? 6.683  57.690  23.304 1.00 18.66 ? 501  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 60  ? 4.767  58.172  24.894 1.00 19.51 ? 501  LEU   A CD2 1 
ATOM   528  N  N   . CYS   A 1 61  ? 8.871  57.897  28.522 1.00 16.07 ? 502  CYS   A N   1 
ATOM   529  C  CA  . CYS   A 1 61  ? 9.588  57.095  29.505 1.00 15.50 ? 502  CYS   A CA  1 
ATOM   530  C  C   . CYS   A 1 61  ? 10.363 57.916  30.525 1.00 16.79 ? 502  CYS   A C   1 
ATOM   531  O  O   . CYS   A 1 61  ? 10.682 57.380  31.594 1.00 17.89 ? 502  CYS   A O   1 
ATOM   532  C  CB  . CYS   A 1 61  ? 10.606 56.198  28.792 1.00 15.65 ? 502  CYS   A CB  1 
ATOM   533  S  SG  . CYS   A 1 61  ? 9.855  54.858  27.901 1.00 15.45 ? 502  CYS   A SG  1 
ATOM   534  N  N   . HIS   A 1 62  ? 10.687 59.181  30.246 1.00 15.05 ? 503  HIS   A N   1 
ATOM   535  C  CA  . HIS   A 1 62  ? 11.603 59.939  31.086 1.00 15.71 ? 503  HIS   A CA  1 
ATOM   536  C  C   . HIS   A 1 62  ? 10.924 61.161  31.691 1.00 16.72 ? 503  HIS   A C   1 
ATOM   537  O  O   . HIS   A 1 62  ? 9.978  61.716  31.126 1.00 17.63 ? 503  HIS   A O   1 
ATOM   538  C  CB  . HIS   A 1 62  ? 12.846 60.350  30.297 1.00 15.21 ? 503  HIS   A CB  1 
ATOM   539  C  CG  . HIS   A 1 62  ? 13.660 59.186  29.822 1.00 15.63 ? 503  HIS   A CG  1 
ATOM   540  N  ND1 . HIS   A 1 62  ? 14.461 58.452  30.670 1.00 13.59 ? 503  HIS   A ND1 1 
ATOM   541  C  CD2 . HIS   A 1 62  ? 13.785 58.620  28.596 1.00 15.02 ? 503  HIS   A CD2 1 
ATOM   542  C  CE1 . HIS   A 1 62  ? 15.047 57.483  29.986 1.00 15.38 ? 503  HIS   A CE1 1 
ATOM   543  N  NE2 . HIS   A 1 62  ? 14.657 57.566  28.727 1.00 16.50 ? 503  HIS   A NE2 1 
ATOM   544  N  N   . SER   A 1 63  ? 11.419 61.558  32.859 1.00 17.23 ? 504  SER   A N   1 
ATOM   545  C  CA  . SER   A 1 63  ? 10.890 62.706  33.572 1.00 16.01 ? 504  SER   A CA  1 
ATOM   546  C  C   . SER   A 1 63  ? 11.297 64.001  32.882 1.00 17.74 ? 504  SER   A C   1 
ATOM   547  O  O   . SER   A 1 63  ? 12.286 64.066  32.148 1.00 16.46 ? 504  SER   A O   1 
ATOM   548  C  CB  . SER   A 1 63  ? 11.446 62.735  34.990 1.00 15.61 ? 504  SER   A CB  1 
ATOM   549  O  OG  . SER   A 1 63  ? 12.824 63.079  34.987 1.00 17.42 ? 504  SER   A OG  1 
ATOM   550  N  N   A SER   A 1 64  ? 10.514 65.049  33.135 0.66 18.32 ? 505  SER   A N   1 
ATOM   551  N  N   B SER   A 1 64  ? 10.517 65.051  33.141 0.34 17.85 ? 505  SER   A N   1 
ATOM   552  C  CA  A SER   A 1 64  ? 10.833 66.355  32.568 0.66 18.89 ? 505  SER   A CA  1 
ATOM   553  C  CA  B SER   A 1 64  ? 10.832 66.355  32.569 0.34 18.21 ? 505  SER   A CA  1 
ATOM   554  C  C   A SER   A 1 64  ? 12.165 66.882  33.090 0.66 15.72 ? 505  SER   A C   1 
ATOM   555  C  C   B SER   A 1 64  ? 12.157 66.893  33.094 0.34 16.22 ? 505  SER   A C   1 
ATOM   556  O  O   A SER   A 1 64  ? 12.910 67.533  32.349 0.66 18.31 ? 505  SER   A O   1 
ATOM   557  O  O   B SER   A 1 64  ? 12.886 67.567  32.358 0.34 18.22 ? 505  SER   A O   1 
ATOM   558  C  CB  A SER   A 1 64  ? 9.699  67.338  32.859 0.66 21.24 ? 505  SER   A CB  1 
ATOM   559  C  CB  B SER   A 1 64  ? 9.703  67.345  32.853 0.34 18.50 ? 505  SER   A CB  1 
ATOM   560  O  OG  A SER   A 1 64  ? 9.508  67.496  34.252 0.66 22.98 ? 505  SER   A OG  1 
ATOM   561  O  OG  B SER   A 1 64  ? 9.930  68.567  32.171 0.34 21.87 ? 505  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 65  ? 12.482 66.612  34.358 1.00 17.51 ? 506  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 65  ? 13.748 67.076  34.915 1.00 17.38 ? 506  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 65  ? 14.927 66.424  34.205 1.00 18.97 ? 506  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 65  ? 15.902 67.101  33.856 1.00 19.06 ? 506  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 65  ? 13.789 66.794  36.417 1.00 21.59 ? 506  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 65  ? 15.016 67.333  37.133 1.00 29.72 ? 506  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 65  ? 15.242 66.613  38.459 1.00 35.79 ? 506  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 65  ? 16.284 67.322  39.312 1.00 45.92 ? 506  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 65  ? 16.592 68.686  38.796 1.00 50.63 ? 506  LYS   A NZ  1 
ATOM   571  N  N   . HIS   A 1 66  ? 14.855 65.110  33.984 1.00 17.79 ? 507  HIS   A N   1 
ATOM   572  C  CA  . HIS   A 1 66  ? 15.939 64.413  33.303 1.00 16.49 ? 507  HIS   A CA  1 
ATOM   573  C  C   . HIS   A 1 66  ? 16.094 64.910  31.873 1.00 16.10 ? 507  HIS   A C   1 
ATOM   574  O  O   . HIS   A 1 66  ? 17.207 65.180  31.410 1.00 16.68 ? 507  HIS   A O   1 
ATOM   575  C  CB  . HIS   A 1 66  ? 15.684 62.906  33.327 1.00 16.35 ? 507  HIS   A CB  1 
ATOM   576  C  CG  . HIS   A 1 66  ? 16.743 62.111  32.630 1.00 16.81 ? 507  HIS   A CG  1 
ATOM   577  N  ND1 . HIS   A 1 66  ? 18.067 62.126  33.018 1.00 17.90 ? 507  HIS   A ND1 1 
ATOM   578  C  CD2 . HIS   A 1 66  ? 16.672 61.278  31.564 1.00 17.36 ? 507  HIS   A CD2 1 
ATOM   579  C  CE1 . HIS   A 1 66  ? 18.764 61.331  32.223 1.00 17.46 ? 507  HIS   A CE1 1 
ATOM   580  N  NE2 . HIS   A 1 66  ? 17.943 60.808  31.332 1.00 17.15 ? 507  HIS   A NE2 1 
ATOM   581  N  N   . ILE   A 1 67  ? 14.980 65.041  31.157 1.00 17.92 ? 508  ILE   A N   1 
ATOM   582  C  CA  . ILE   A 1 67  ? 15.051 65.554  29.794 1.00 19.16 ? 508  ILE   A CA  1 
ATOM   583  C  C   . ILE   A 1 67  ? 15.695 66.932  29.772 1.00 17.47 ? 508  ILE   A C   1 
ATOM   584  O  O   . ILE   A 1 67  ? 16.554 67.214  28.932 1.00 17.57 ? 508  ILE   A O   1 
ATOM   585  C  CB  . ILE   A 1 67  ? 13.654 65.569  29.152 1.00 18.46 ? 508  ILE   A CB  1 
ATOM   586  C  CG1 . ILE   A 1 67  ? 13.122 64.142  29.030 1.00 19.10 ? 508  ILE   A CG1 1 
ATOM   587  C  CG2 . ILE   A 1 67  ? 13.707 66.283  27.807 1.00 18.33 ? 508  ILE   A CG2 1 
ATOM   588  C  CD1 . ILE   A 1 67  ? 11.627 64.071  28.754 1.00 17.42 ? 508  ILE   A CD1 1 
ATOM   589  N  N   . SER   A 1 68  ? 15.299 67.809  30.700 1.00 17.86 ? 509  SER   A N   1 
ATOM   590  C  CA  . SER   A 1 68  ? 15.823 69.171  30.682 1.00 18.65 ? 509  SER   A CA  1 
ATOM   591  C  C   . SER   A 1 68  ? 17.316 69.215  31.005 1.00 17.33 ? 509  SER   A C   1 
ATOM   592  O  O   . SER   A 1 68  ? 18.065 69.977  30.381 1.00 18.91 ? 509  SER   A O   1 
ATOM   593  C  CB  . SER   A 1 68  ? 15.030 70.061  31.636 1.00 23.60 ? 509  SER   A CB  1 
ATOM   594  O  OG  . SER   A 1 68  ? 15.562 71.376  31.637 1.00 32.40 ? 509  SER   A OG  1 
ATOM   595  N  N   . ILE   A 1 69  ? 17.767 68.409  31.972 1.00 16.97 ? 510  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 69  ? 19.181 68.407  32.331 1.00 19.83 ? 510  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 69  ? 20.045 67.916  31.173 1.00 18.47 ? 510  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 69  ? 21.054 68.544  30.825 1.00 21.39 ? 510  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 69  ? 19.423 67.643  33.650 1.00 23.75 ? 510  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 69  ? 20.872 67.792  34.122 1.00 26.41 ? 510  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 69  ? 19.100 66.180  33.524 1.00 26.28 ? 510  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 69  ? 20.999 67.783  35.638 1.00 30.40 ? 510  ILE   A CD1 1 
ATOM   603  N  N   . ILE   A 1 70  ? 19.659 66.811  30.531 1.00 16.97 ? 511  ILE   A N   1 
ATOM   604  C  CA  . ILE   A 1 70  ? 20.458 66.324  29.408 1.00 16.15 ? 511  ILE   A CA  1 
ATOM   605  C  C   . ILE   A 1 70  ? 20.389 67.296  28.234 1.00 17.24 ? 511  ILE   A C   1 
ATOM   606  O  O   . ILE   A 1 70  ? 21.403 67.576  27.585 1.00 20.22 ? 511  ILE   A O   1 
ATOM   607  C  CB  . ILE   A 1 70  ? 20.058 64.893  29.005 1.00 16.01 ? 511  ILE   A CB  1 
ATOM   608  C  CG1 . ILE   A 1 70  ? 20.161 63.959  30.214 1.00 15.04 ? 511  ILE   A CG1 1 
ATOM   609  C  CG2 . ILE   A 1 70  ? 20.923 64.413  27.839 1.00 17.96 ? 511  ILE   A CG2 1 
ATOM   610  C  CD1 . ILE   A 1 70  ? 21.528 63.970  30.866 1.00 16.84 ? 511  ILE   A CD1 1 
ATOM   611  N  N   . LYS   A 1 71  ? 19.193 67.820  27.938 1.00 15.94 ? 512  LYS   A N   1 
ATOM   612  C  CA  . LYS   A 1 71  ? 19.055 68.820  26.880 1.00 17.58 ? 512  LYS   A CA  1 
ATOM   613  C  C   . LYS   A 1 71  ? 19.992 69.997  27.117 1.00 17.93 ? 512  LYS   A C   1 
ATOM   614  O  O   . LYS   A 1 71  ? 20.617 70.511  26.181 1.00 19.69 ? 512  LYS   A O   1 
ATOM   615  C  CB  . LYS   A 1 71  ? 17.604 69.301  26.841 1.00 17.63 ? 512  LYS   A CB  1 
ATOM   616  C  CG  . LYS   A 1 71  ? 17.337 70.448  25.881 1.00 20.25 ? 512  LYS   A CG  1 
ATOM   617  C  CD  . LYS   A 1 71  ? 15.880 70.857  25.979 1.00 22.93 ? 512  LYS   A CD  1 
ATOM   618  C  CE  . LYS   A 1 71  ? 15.577 72.114  25.179 1.00 26.52 ? 512  LYS   A CE  1 
ATOM   619  N  NZ  . LYS   A 1 71  ? 14.159 72.531  25.380 1.00 26.17 ? 512  LYS   A NZ  1 
ATOM   620  N  N   . SER   A 1 72  ? 20.122 70.415  28.371 1.00 18.72 ? 513  SER   A N   1 
ATOM   621  C  CA  . SER   A 1 72  ? 20.964 71.558  28.695 1.00 20.05 ? 513  SER   A CA  1 
ATOM   622  C  C   . SER   A 1 72  ? 22.429 71.330  28.350 1.00 22.12 ? 513  SER   A C   1 
ATOM   623  O  O   . SER   A 1 72  ? 23.160 72.304  28.135 1.00 22.92 ? 513  SER   A O   1 
ATOM   624  C  CB  . SER   A 1 72  ? 20.794 71.914  30.171 1.00 20.87 ? 513  SER   A CB  1 
ATOM   625  O  OG  . SER   A 1 72  ? 21.597 71.119  31.023 1.00 22.03 ? 513  SER   A OG  1 
ATOM   626  N  N   . SER   A 1 73  ? 22.876 70.074  28.260 1.00 21.16 ? 514  SER   A N   1 
ATOM   627  C  CA  . SER   A 1 73  ? 24.298 69.827  28.045 1.00 17.84 ? 514  SER   A CA  1 
ATOM   628  C  C   . SER   A 1 73  ? 24.760 70.260  26.663 1.00 19.08 ? 514  SER   A C   1 
ATOM   629  O  O   . SER   A 1 73  ? 25.965 70.411  26.445 1.00 22.71 ? 514  SER   A O   1 
ATOM   630  C  CB  . SER   A 1 73  ? 24.646 68.354  28.291 1.00 16.89 ? 514  SER   A CB  1 
ATOM   631  O  OG  . SER   A 1 73  ? 24.008 67.491  27.366 1.00 18.30 ? 514  SER   A OG  1 
ATOM   632  N  N   . GLU   A 1 74  ? 23.832 70.477  25.727 1.00 19.68 ? 515  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 74  ? 24.221 70.884  24.380 1.00 19.65 ? 515  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 74  ? 24.948 72.225  24.381 1.00 22.54 ? 515  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 74  ? 25.814 72.461  23.531 1.00 24.72 ? 515  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 74  ? 22.991 70.917  23.468 1.00 20.70 ? 515  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 74  ? 23.301 71.384  22.053 1.00 30.10 ? 515  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 74  ? 22.124 71.245  21.105 1.00 36.28 ? 515  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 74  ? 20.993 71.009  21.581 1.00 35.16 ? 515  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 74  ? 22.336 71.376  19.881 1.00 36.60 ? 515  GLU   A OE2 1 
ATOM   641  N  N   . HIS   A 1 75  ? 24.636 73.103  25.336 1.00 24.98 ? 516  HIS   A N   1 
ATOM   642  C  CA  . HIS   A 1 75  ? 25.250 74.426  25.395 1.00 26.48 ? 516  HIS   A CA  1 
ATOM   643  C  C   . HIS   A 1 75  ? 26.158 74.616  26.606 1.00 28.57 ? 516  HIS   A C   1 
ATOM   644  O  O   . HIS   A 1 75  ? 26.459 75.756  26.972 1.00 32.03 ? 516  HIS   A O   1 
ATOM   645  C  CB  . HIS   A 1 75  ? 24.182 75.516  25.339 1.00 27.74 ? 516  HIS   A CB  1 
ATOM   646  C  CG  . HIS   A 1 75  ? 23.251 75.372  24.179 1.00 34.55 ? 516  HIS   A CG  1 
ATOM   647  N  ND1 . HIS   A 1 75  ? 21.943 74.963  24.322 1.00 36.92 ? 516  HIS   A ND1 1 
ATOM   648  C  CD2 . HIS   A 1 75  ? 23.448 75.554  22.852 1.00 31.70 ? 516  HIS   A CD2 1 
ATOM   649  C  CE1 . HIS   A 1 75  ? 21.370 74.911  23.133 1.00 36.45 ? 516  HIS   A CE1 1 
ATOM   650  N  NE2 . HIS   A 1 75  ? 22.261 75.265  22.224 1.00 33.10 ? 516  HIS   A NE2 1 
ATOM   651  N  N   . MET   A 1 76  ? 26.614 73.533  27.225 1.00 24.98 ? 517  MET   A N   1 
ATOM   652  C  CA  . MET   A 1 76  ? 27.433 73.634  28.423 1.00 22.01 ? 517  MET   A CA  1 
ATOM   653  C  C   . MET   A 1 76  ? 28.906 73.812  28.085 1.00 23.22 ? 517  MET   A C   1 
ATOM   654  O  O   . MET   A 1 76  ? 29.397 73.329  27.061 1.00 23.06 ? 517  MET   A O   1 
ATOM   655  C  CB  . MET   A 1 76  ? 27.298 72.379  29.274 1.00 20.68 ? 517  MET   A CB  1 
ATOM   656  C  CG  . MET   A 1 76  ? 26.104 72.364  30.177 1.00 21.70 ? 517  MET   A CG  1 
ATOM   657  S  SD  . MET   A 1 76  ? 26.151 70.883  31.183 1.00 23.79 ? 517  MET   A SD  1 
ATOM   658  C  CE  . MET   A 1 76  ? 24.841 71.277  32.348 1.00 23.05 ? 517  MET   A CE  1 
ATOM   659  N  N   . LYS   A 1 77  ? 29.615 74.492  28.986 1.00 24.43 ? 518  LYS   A N   1 
ATOM   660  C  CA  . LYS   A 1 77  ? 31.060 74.586  28.904 1.00 25.64 ? 518  LYS   A CA  1 
ATOM   661  C  C   . LYS   A 1 77  ? 31.694 73.276  29.374 1.00 25.61 ? 518  LYS   A C   1 
ATOM   662  O  O   . LYS   A 1 77  ? 31.048 72.476  30.057 1.00 24.51 ? 518  LYS   A O   1 
ATOM   663  C  CB  . LYS   A 1 77  ? 31.550 75.749  29.767 1.00 29.47 ? 518  LYS   A CB  1 
ATOM   664  C  CG  . LYS   A 1 77  ? 31.313 77.118  29.134 1.00 38.41 ? 518  LYS   A CG  1 
ATOM   665  C  CD  . LYS   A 1 77  ? 31.966 77.216  27.755 1.00 42.11 ? 518  LYS   A CD  1 
ATOM   666  C  CE  . LYS   A 1 77  ? 33.021 78.317  27.704 1.00 49.34 ? 518  LYS   A CE  1 
ATOM   667  N  NZ  . LYS   A 1 77  ? 32.413 79.677  27.601 1.00 52.33 ? 518  LYS   A NZ  1 
ATOM   668  N  N   . PRO   A 1 78  ? 32.963 73.035  29.011 1.00 26.83 ? 519  PRO   A N   1 
ATOM   669  C  CA  . PRO   A 1 78  ? 33.622 71.779  29.413 1.00 24.56 ? 519  PRO   A CA  1 
ATOM   670  C  C   . PRO   A 1 78  ? 33.557 71.464  30.899 1.00 22.50 ? 519  PRO   A C   1 
ATOM   671  O  O   . PRO   A 1 78  ? 33.308 70.306  31.259 1.00 26.11 ? 519  PRO   A O   1 
ATOM   672  C  CB  . PRO   A 1 78  ? 35.070 71.991  28.952 1.00 25.24 ? 519  PRO   A CB  1 
ATOM   673  C  CG  . PRO   A 1 78  ? 34.937 72.870  27.765 1.00 25.02 ? 519  PRO   A CG  1 
ATOM   674  C  CD  . PRO   A 1 78  ? 33.815 73.821  28.099 1.00 24.96 ? 519  PRO   A CD  1 
ATOM   675  N  N   . ARG   A 1 79  ? 33.796 72.449  31.774 1.00 23.21 ? 520  ARG   A N   1 
ATOM   676  C  CA  . ARG   A 1 79  ? 33.702 72.188  33.208 1.00 23.35 ? 520  ARG   A CA  1 
ATOM   677  C  C   . ARG   A 1 79  ? 32.316 71.702  33.588 1.00 21.46 ? 520  ARG   A C   1 
ATOM   678  O  O   . ARG   A 1 79  ? 32.176 70.777  34.393 1.00 25.80 ? 520  ARG   A O   1 
ATOM   679  C  CB  . ARG   A 1 79  ? 34.046 73.443  34.010 1.00 25.46 ? 520  ARG   A CB  1 
ATOM   680  C  CG  . ARG   A 1 79  ? 34.243 73.176  35.494 1.00 25.34 ? 520  ARG   A CG  1 
ATOM   681  C  CD  . ARG   A 1 79  ? 35.196 74.188  36.110 1.00 26.05 ? 520  ARG   A CD  1 
ATOM   682  N  NE  . ARG   A 1 79  ? 36.415 74.328  35.313 0.53 29.26 ? 520  ARG   A NE  1 
ATOM   683  C  CZ  . ARG   A 1 79  ? 36.731 75.410  34.606 0.57 28.71 ? 520  ARG   A CZ  1 
ATOM   684  N  NH1 . ARG   A 1 79  ? 35.917 76.460  34.589 1.00 31.35 ? 520  ARG   A NH1 1 
ATOM   685  N  NH2 . ARG   A 1 79  ? 37.861 75.441  33.910 0.60 29.48 ? 520  ARG   A NH2 1 
ATOM   686  N  N   . ASP   A 1 80  ? 31.277 72.323  33.022 1.00 21.69 ? 521  ASP   A N   1 
ATOM   687  C  CA  . ASP   A 1 80  ? 29.909 71.902  33.309 1.00 21.48 ? 521  ASP   A CA  1 
ATOM   688  C  C   . ASP   A 1 80  ? 29.661 70.484  32.813 1.00 20.53 ? 521  ASP   A C   1 
ATOM   689  O  O   . ASP   A 1 80  ? 29.004 69.687  33.493 1.00 21.62 ? 521  ASP   A O   1 
ATOM   690  C  CB  . ASP   A 1 80  ? 28.928 72.866  32.643 1.00 24.47 ? 521  ASP   A CB  1 
ATOM   691  C  CG  . ASP   A 1 80  ? 28.916 74.240  33.293 1.00 27.87 ? 521  ASP   A CG  1 
ATOM   692  O  OD1 . ASP   A 1 80  ? 28.994 74.324  34.536 1.00 26.18 ? 521  ASP   A OD1 1 
ATOM   693  O  OD2 . ASP   A 1 80  ? 28.839 75.239  32.541 1.00 35.07 ? 521  ASP   A OD2 1 
ATOM   694  N  N   . LEU   A 1 81  ? 30.176 70.157  31.621 1.00 20.65 ? 522  LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 81  ? 30.001 68.816  31.069 1.00 20.19 ? 522  LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 81  ? 30.697 67.770  31.927 1.00 18.81 ? 522  LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 81  ? 30.142 66.694  32.181 1.00 18.84 ? 522  LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 81  ? 30.570 68.769  29.653 1.00 18.68 ? 522  LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 81  ? 29.740 69.466  28.581 1.00 19.61 ? 522  LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 81  ? 30.539 69.565  27.317 1.00 19.65 ? 522  LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 81  ? 28.445 68.701  28.333 1.00 19.93 ? 522  LEU   A CD2 1 
ATOM   702  N  N   . ASN   A 1 82  ? 31.923 68.060  32.365 1.00 20.04 ? 523  ASN   A N   1 
ATOM   703  C  CA  . ASN   A 1 82  ? 32.665 67.111  33.182 1.00 20.38 ? 523  ASN   A CA  1 
ATOM   704  C  C   . ASN   A 1 82  ? 31.975 66.891  34.516 1.00 19.31 ? 523  ASN   A C   1 
ATOM   705  O  O   . ASN   A 1 82  ? 31.871 65.756  34.997 1.00 20.99 ? 523  ASN   A O   1 
ATOM   706  C  CB  . ASN   A 1 82  ? 34.087 67.618  33.415 1.00 30.31 ? 523  ASN   A CB  1 
ATOM   707  C  CG  . ASN   A 1 82  ? 34.904 67.661  32.146 1.00 43.97 ? 523  ASN   A CG  1 
ATOM   708  O  OD1 . ASN   A 1 82  ? 34.730 66.835  31.248 1.00 47.03 ? 523  ASN   A OD1 1 
ATOM   709  N  ND2 . ASN   A 1 82  ? 35.811 68.626  32.066 1.00 47.59 ? 523  ASN   A ND2 1 
ATOM   710  N  N   . ARG   A 1 83  ? 31.525 67.977  35.152 1.00 19.69 ? 524  ARG   A N   1 
ATOM   711  C  CA  . ARG   A 1 83  ? 30.883 67.842  36.454 1.00 19.49 ? 524  ARG   A CA  1 
ATOM   712  C  C   . ARG   A 1 83  ? 29.557 67.116  36.335 1.00 19.37 ? 524  ARG   A C   1 
ATOM   713  O  O   . ARG   A 1 83  ? 29.241 66.256  37.163 1.00 22.79 ? 524  ARG   A O   1 
ATOM   714  C  CB  . ARG   A 1 83  ? 30.659 69.214  37.086 1.00 21.78 ? 524  ARG   A CB  1 
ATOM   715  C  CG  . ARG   A 1 83  ? 31.922 69.912  37.532 1.00 22.97 ? 524  ARG   A CG  1 
ATOM   716  C  CD  . ARG   A 1 83  ? 31.589 71.304  38.021 1.00 23.00 ? 524  ARG   A CD  1 
ATOM   717  N  NE  . ARG   A 1 83  ? 32.697 71.909  38.754 1.00 25.99 ? 524  ARG   A NE  1 
ATOM   718  C  CZ  . ARG   A 1 83  ? 32.592 73.027  39.468 1.00 24.85 ? 524  ARG   A CZ  1 
ATOM   719  N  NH1 . ARG   A 1 83  ? 31.423 73.661  39.550 1.00 24.40 ? 524  ARG   A NH1 1 
ATOM   720  N  NH2 . ARG   A 1 83  ? 33.653 73.509  40.100 1.00 28.61 ? 524  ARG   A NH2 1 
ATOM   721  N  N   . LEU   A 1 84  ? 28.761 67.460  35.319 1.00 19.44 ? 525  LEU   A N   1 
ATOM   722  C  CA  . LEU   A 1 84  ? 27.482 66.786  35.142 1.00 19.62 ? 525  LEU   A CA  1 
ATOM   723  C  C   . LEU   A 1 84  ? 27.691 65.301  34.884 1.00 19.62 ? 525  LEU   A C   1 
ATOM   724  O  O   . LEU   A 1 84  ? 27.029 64.452  35.488 1.00 20.70 ? 525  LEU   A O   1 
ATOM   725  C  CB  . LEU   A 1 84  ? 26.695 67.429  34.001 1.00 18.82 ? 525  LEU   A CB  1 
ATOM   726  C  CG  . LEU   A 1 84  ? 25.387 66.721  33.653 1.00 19.14 ? 525  LEU   A CG  1 
ATOM   727  C  CD1 . LEU   A 1 84  ? 24.467 66.697  34.867 1.00 18.38 ? 525  LEU   A CD1 1 
ATOM   728  C  CD2 . LEU   A 1 84  ? 24.727 67.413  32.487 1.00 19.84 ? 525  LEU   A CD2 1 
ATOM   729  N  N   . GLY   A 1 85  ? 28.628 64.968  33.998 1.00 19.47 ? 526  GLY   A N   1 
ATOM   730  C  CA  . GLY   A 1 85  ? 28.895 63.568  33.721 1.00 18.69 ? 526  GLY   A CA  1 
ATOM   731  C  C   . GLY   A 1 85  ? 29.308 62.799  34.959 1.00 18.87 ? 526  GLY   A C   1 
ATOM   732  O  O   . GLY   A 1 85  ? 28.855 61.673  35.183 1.00 18.46 ? 526  GLY   A O   1 
ATOM   733  N  N   . ASP   A 1 86  ? 30.144 63.413  35.806 1.00 21.88 ? 527  ASP   A N   1 
ATOM   734  C  CA  . ASP   A 1 86  ? 30.606 62.724  37.005 1.00 24.27 ? 527  ASP   A CA  1 
ATOM   735  C  C   . ASP   A 1 86  ? 29.527 62.574  38.071 1.00 21.75 ? 527  ASP   A C   1 
ATOM   736  O  O   . ASP   A 1 86  ? 29.729 61.810  39.019 1.00 24.77 ? 527  ASP   A O   1 
ATOM   737  C  CB  . ASP   A 1 86  ? 31.865 63.388  37.566 1.00 31.67 ? 527  ASP   A CB  1 
ATOM   738  C  CG  . ASP   A 1 86  ? 33.057 63.254  36.626 1.00 36.05 ? 527  ASP   A CG  1 
ATOM   739  O  OD1 . ASP   A 1 86  ? 33.020 62.375  35.733 1.00 37.44 ? 527  ASP   A OD1 1 
ATOM   740  O  OD2 . ASP   A 1 86  ? 34.034 64.018  36.782 1.00 40.42 ? 527  ASP   A OD2 1 
ATOM   741  N  N   . GLU   A 1 87  ? 28.388 63.262  37.940 1.00 21.72 ? 528  GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 87  ? 27.283 63.039  38.866 1.00 21.31 ? 528  GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 87  ? 26.600 61.694  38.636 1.00 22.10 ? 528  GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 87  ? 25.962 61.168  39.552 1.00 27.27 ? 528  GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 87  ? 26.265 64.180  38.759 1.00 26.45 ? 528  GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 87  ? 26.678 65.449  39.497 1.00 32.69 ? 528  GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 87  ? 27.239 65.175  40.888 1.00 37.68 ? 528  GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 87  ? 26.508 64.609  41.732 1.00 42.06 ? 528  GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 87  ? 28.412 65.530  41.138 1.00 43.47 ? 528  GLU   A OE2 1 
ATOM   750  N  N   . TYR   A 1 88  ? 26.723 61.125  37.440 1.00 19.90 ? 529  TYR   A N   1 
ATOM   751  C  CA  . TYR   A 1 88  ? 26.123 59.839  37.120 1.00 19.21 ? 529  TYR   A CA  1 
ATOM   752  C  C   . TYR   A 1 88  ? 27.144 58.716  37.287 1.00 18.48 ? 529  TYR   A C   1 
ATOM   753  O  O   . TYR   A 1 88  ? 28.347 58.943  37.396 1.00 17.50 ? 529  TYR   A O   1 
ATOM   754  C  CB  . TYR   A 1 88  ? 25.598 59.834  35.679 1.00 17.08 ? 529  TYR   A CB  1 
ATOM   755  C  CG  . TYR   A 1 88  ? 24.619 60.935  35.367 1.00 15.49 ? 529  TYR   A CG  1 
ATOM   756  C  CD1 . TYR   A 1 88  ? 23.319 60.894  35.847 1.00 15.94 ? 529  TYR   A CD1 1 
ATOM   757  C  CD2 . TYR   A 1 88  ? 24.981 61.990  34.544 1.00 16.28 ? 529  TYR   A CD2 1 
ATOM   758  C  CE1 . TYR   A 1 88  ? 22.408 61.905  35.543 1.00 15.95 ? 529  TYR   A CE1 1 
ATOM   759  C  CE2 . TYR   A 1 88  ? 24.086 63.000  34.235 1.00 18.22 ? 529  TYR   A CE2 1 
ATOM   760  C  CZ  . TYR   A 1 88  ? 22.808 62.957  34.744 1.00 16.55 ? 529  TYR   A CZ  1 
ATOM   761  O  OH  . TYR   A 1 88  ? 21.927 63.972  34.421 1.00 20.47 ? 529  TYR   A OH  1 
ATOM   762  N  N   . ASN   A 1 89  ? 26.636 57.489  37.319 1.00 17.67 ? 530  ASN   A N   1 
ATOM   763  C  CA  . ASN   A 1 89  ? 27.471 56.297  37.280 1.00 16.44 ? 530  ASN   A CA  1 
ATOM   764  C  C   . ASN   A 1 89  ? 27.866 56.039  35.824 1.00 16.46 ? 530  ASN   A C   1 
ATOM   765  O  O   . ASN   A 1 89  ? 27.016 55.695  34.997 1.00 16.55 ? 530  ASN   A O   1 
ATOM   766  C  CB  . ASN   A 1 89  ? 26.683 55.128  37.870 1.00 19.44 ? 530  ASN   A CB  1 
ATOM   767  C  CG  . ASN   A 1 89  ? 27.488 53.836  37.936 1.00 21.67 ? 530  ASN   A CG  1 
ATOM   768  O  OD1 . ASN   A 1 89  ? 28.554 53.715  37.338 1.00 22.29 ? 530  ASN   A OD1 1 
ATOM   769  N  ND2 . ASN   A 1 89  ? 26.952 52.850  38.646 1.00 23.55 ? 530  ASN   A ND2 1 
ATOM   770  N  N   . SER   A 1 90  ? 29.147 56.232  35.505 1.00 15.22 ? 531  SER   A N   1 
ATOM   771  C  CA  . SER   A 1 90  ? 29.751 55.854  34.227 1.00 16.59 ? 531  SER   A CA  1 
ATOM   772  C  C   . SER   A 1 90  ? 29.125 56.577  33.041 1.00 16.47 ? 531  SER   A C   1 
ATOM   773  O  O   . SER   A 1 90  ? 28.596 55.938  32.120 1.00 17.44 ? 531  SER   A O   1 
ATOM   774  C  CB  . SER   A 1 90  ? 29.685 54.339  34.015 1.00 17.73 ? 531  SER   A CB  1 
ATOM   775  O  OG  . SER   A 1 90  ? 30.342 53.659  35.069 1.00 22.97 ? 531  SER   A OG  1 
ATOM   776  N  N   . ILE   A 1 91  ? 29.205 57.905  33.038 1.00 14.51 ? 532  ILE   A N   1 
ATOM   777  C  CA  . ILE   A 1 91  ? 28.717 58.723  31.933 1.00 14.43 ? 532  ILE   A CA  1 
ATOM   778  C  C   . ILE   A 1 91  ? 29.789 59.741  31.578 1.00 16.58 ? 532  ILE   A C   1 
ATOM   779  O  O   . ILE   A 1 91  ? 30.361 60.372  32.475 1.00 18.08 ? 532  ILE   A O   1 
ATOM   780  C  CB  . ILE   A 1 91  ? 27.429 59.462  32.340 1.00 14.82 ? 532  ILE   A CB  1 
ATOM   781  C  CG1 . ILE   A 1 91  ? 26.236 58.507  32.396 1.00 15.14 ? 532  ILE   A CG1 1 
ATOM   782  C  CG2 . ILE   A 1 91  ? 27.145 60.638  31.409 1.00 15.57 ? 532  ILE   A CG2 1 
ATOM   783  C  CD1 . ILE   A 1 91  ? 25.713 58.101  31.015 1.00 13.77 ? 532  ILE   A CD1 1 
ATOM   784  N  N   . PHE   A 1 92  ? 30.054 59.906  30.276 1.00 16.21 ? 533  PHE   A N   1 
ATOM   785  C  CA  . PHE   A 1 92  ? 30.758 61.072  29.753 1.00 15.44 ? 533  PHE   A CA  1 
ATOM   786  C  C   . PHE   A 1 92  ? 29.829 61.831  28.811 1.00 16.04 ? 533  PHE   A C   1 
ATOM   787  O  O   . PHE   A 1 92  ? 28.983 61.236  28.139 1.00 17.03 ? 533  PHE   A O   1 
ATOM   788  C  CB  . PHE   A 1 92  ? 32.070 60.691  29.017 1.00 15.39 ? 533  PHE   A CB  1 
ATOM   789  C  CG  . PHE   A 1 92  ? 31.855 59.845  27.788 1.00 15.60 ? 533  PHE   A CG  1 
ATOM   790  C  CD1 . PHE   A 1 92  ? 31.584 60.426  26.553 1.00 15.71 ? 533  PHE   A CD1 1 
ATOM   791  C  CD2 . PHE   A 1 92  ? 31.917 58.468  27.871 1.00 15.87 ? 533  PHE   A CD2 1 
ATOM   792  C  CE1 . PHE   A 1 92  ? 31.365 59.639  25.423 1.00 15.61 ? 533  PHE   A CE1 1 
ATOM   793  C  CE2 . PHE   A 1 92  ? 31.709 57.681  26.758 1.00 17.78 ? 533  PHE   A CE2 1 
ATOM   794  C  CZ  . PHE   A 1 92  ? 31.428 58.265  25.535 1.00 15.72 ? 533  PHE   A CZ  1 
ATOM   795  N  N   . ILE   A 1 93  ? 29.978 63.155  28.766 1.00 15.11 ? 534  ILE   A N   1 
ATOM   796  C  CA  . ILE   A 1 93  ? 29.100 64.012  27.977 1.00 16.59 ? 534  ILE   A CA  1 
ATOM   797  C  C   . ILE   A 1 93  ? 29.937 64.969  27.140 1.00 16.96 ? 534  ILE   A C   1 
ATOM   798  O  O   . ILE   A 1 93  ? 30.948 65.505  27.610 1.00 17.89 ? 534  ILE   A O   1 
ATOM   799  C  CB  . ILE   A 1 93  ? 28.114 64.800  28.865 1.00 17.22 ? 534  ILE   A CB  1 
ATOM   800  C  CG1 . ILE   A 1 93  ? 27.569 63.913  29.984 1.00 19.84 ? 534  ILE   A CG1 1 
ATOM   801  C  CG2 . ILE   A 1 93  ? 26.951 65.340  28.026 1.00 17.08 ? 534  ILE   A CG2 1 
ATOM   802  C  CD1 . ILE   A 1 93  ? 26.611 64.625  30.921 1.00 18.60 ? 534  ILE   A CD1 1 
ATOM   803  N  N   . SER   A 1 94  ? 29.512 65.185  25.900 1.00 17.70 ? 535  SER   A N   1 
ATOM   804  C  CA  . SER   A 1 94  ? 30.048 66.235  25.046 1.00 16.31 ? 535  SER   A CA  1 
ATOM   805  C  C   . SER   A 1 94  ? 28.894 67.109  24.566 1.00 16.76 ? 535  SER   A C   1 
ATOM   806  O  O   . SER   A 1 94  ? 27.723 66.815  24.818 1.00 18.67 ? 535  SER   A O   1 
ATOM   807  C  CB  . SER   A 1 94  ? 30.876 65.666  23.881 1.00 16.36 ? 535  SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 94  ? 30.056 65.034  22.912 1.00 16.62 ? 535  SER   A OG  1 
ATOM   809  N  N   . ASN   A 1 95  ? 29.222 68.206  23.876 1.00 18.72 ? 536  ASN   A N   1 
ATOM   810  C  CA  . ASN   A 1 95  ? 28.156 69.095  23.418 1.00 19.66 ? 536  ASN   A CA  1 
ATOM   811  C  C   . ASN   A 1 95  ? 27.236 68.430  22.401 1.00 17.71 ? 536  ASN   A C   1 
ATOM   812  O  O   . ASN   A 1 95  ? 26.143 68.943  22.151 1.00 21.39 ? 536  ASN   A O   1 
ATOM   813  C  CB  . ASN   A 1 95  ? 28.725 70.393  22.839 1.00 21.06 ? 536  ASN   A CB  1 
ATOM   814  C  CG  . ASN   A 1 95  ? 29.255 71.330  23.909 1.00 23.39 ? 536  ASN   A CG  1 
ATOM   815  O  OD1 . ASN   A 1 95  ? 30.382 71.817  23.813 1.00 28.56 ? 536  ASN   A OD1 1 
ATOM   816  N  ND2 . ASN   A 1 95  ? 28.455 71.581  24.935 1.00 25.73 ? 536  ASN   A ND2 1 
ATOM   817  N  N   . GLU   A 1 96  ? 27.650 67.306  21.813 1.00 17.78 ? 537  GLU   A N   1 
ATOM   818  C  CA  . GLU   A 1 96  ? 26.856 66.596  20.819 1.00 17.29 ? 537  GLU   A CA  1 
ATOM   819  C  C   . GLU   A 1 96  ? 26.051 65.436  21.404 1.00 17.23 ? 537  GLU   A C   1 
ATOM   820  O  O   . GLU   A 1 96  ? 25.266 64.814  20.671 1.00 18.76 ? 537  GLU   A O   1 
ATOM   821  C  CB  . GLU   A 1 96  ? 27.775 66.076  19.704 1.00 19.57 ? 537  GLU   A CB  1 
ATOM   822  C  CG  . GLU   A 1 96  ? 28.641 67.152  19.043 1.00 23.76 ? 537  GLU   A CG  1 
ATOM   823  C  CD  . GLU   A 1 96  ? 29.980 67.376  19.743 1.00 31.09 ? 537  GLU   A CD  1 
ATOM   824  O  OE1 . GLU   A 1 96  ? 30.254 66.730  20.780 1.00 28.62 ? 537  GLU   A OE1 1 
ATOM   825  O  OE2 . GLU   A 1 96  ? 30.769 68.207  19.248 1.00 38.32 ? 537  GLU   A OE2 1 
ATOM   826  N  N   . SER   A 1 97  ? 26.210 65.149  22.702 1.00 18.20 ? 538  SER   A N   1 
ATOM   827  C  CA  . SER   A 1 97  ? 25.644 63.933  23.291 1.00 15.75 ? 538  SER   A CA  1 
ATOM   828  C  C   . SER   A 1 97  ? 24.122 63.933  23.249 1.00 15.91 ? 538  SER   A C   1 
ATOM   829  O  O   . SER   A 1 97  ? 23.506 62.929  22.880 1.00 15.98 ? 538  SER   A O   1 
ATOM   830  C  CB  . SER   A 1 97  ? 26.128 63.762  24.733 1.00 14.67 ? 538  SER   A CB  1 
ATOM   831  O  OG  . SER   A 1 97  ? 27.536 63.736  24.781 1.00 16.47 ? 538  SER   A OG  1 
ATOM   832  N  N   . TYR   A 1 98  ? 23.495 65.039  23.650 1.00 15.11 ? 539  TYR   A N   1 
ATOM   833  C  CA  . TYR   A 1 98  ? 22.039 65.095  23.657 1.00 16.30 ? 539  TYR   A CA  1 
ATOM   834  C  C   . TYR   A 1 98  ? 21.476 64.839  22.268 1.00 16.85 ? 539  TYR   A C   1 
ATOM   835  O  O   . TYR   A 1 98  ? 20.590 63.992  22.094 1.00 16.44 ? 539  TYR   A O   1 
ATOM   836  C  CB  . TYR   A 1 98  ? 21.581 66.455  24.170 1.00 15.77 ? 539  TYR   A CB  1 
ATOM   837  C  CG  . TYR   A 1 98  ? 20.090 66.698  24.072 1.00 16.37 ? 539  TYR   A CG  1 
ATOM   838  C  CD1 . TYR   A 1 98  ? 19.190 65.947  24.824 1.00 16.66 ? 539  TYR   A CD1 1 
ATOM   839  C  CD2 . TYR   A 1 98  ? 19.595 67.713  23.264 1.00 16.71 ? 539  TYR   A CD2 1 
ATOM   840  C  CE1 . TYR   A 1 98  ? 17.831 66.185  24.756 1.00 17.59 ? 539  TYR   A CE1 1 
ATOM   841  C  CE2 . TYR   A 1 98  ? 18.242 67.960  23.187 1.00 16.17 ? 539  TYR   A CE2 1 
ATOM   842  C  CZ  . TYR   A 1 98  ? 17.365 67.196  23.943 1.00 18.68 ? 539  TYR   A CZ  1 
ATOM   843  O  OH  . TYR   A 1 98  ? 16.014 67.431  23.877 1.00 19.80 ? 539  TYR   A OH  1 
ATOM   844  N  N   . THR   A 1 99  ? 22.000 65.544  21.261 1.00 17.77 ? 540  THR   A N   1 
ATOM   845  C  CA  . THR   A 1 99  ? 21.513 65.368  19.897 1.00 17.38 ? 540  THR   A CA  1 
ATOM   846  C  C   . THR   A 1 99  ? 21.743 63.939  19.414 1.00 16.56 ? 540  THR   A C   1 
ATOM   847  O  O   . THR   A 1 99  ? 20.899 63.370  18.710 1.00 15.14 ? 540  THR   A O   1 
ATOM   848  C  CB  . THR   A 1 99  ? 22.202 66.376  18.974 1.00 21.51 ? 540  THR   A CB  1 
ATOM   849  O  OG1 . THR   A 1 99  ? 21.830 67.702  19.365 1.00 25.45 ? 540  THR   A OG1 1 
ATOM   850  C  CG2 . THR   A 1 99  ? 21.781 66.160  17.533 1.00 23.56 ? 540  THR   A CG2 1 
ATOM   851  N  N   . CYS   A 1 100 ? 22.885 63.336  19.779 1.00 15.81 ? 541  CYS   A N   1 
ATOM   852  C  CA  . CYS   A 1 100 ? 23.138 61.963  19.355 1.00 14.61 ? 541  CYS   A CA  1 
ATOM   853  C  C   . CYS   A 1 100 ? 22.153 60.996  19.997 1.00 13.70 ? 541  CYS   A C   1 
ATOM   854  O  O   . CYS   A 1 100 ? 21.674 60.063  19.341 1.00 15.00 ? 541  CYS   A O   1 
ATOM   855  C  CB  . CYS   A 1 100 ? 24.577 61.564  19.669 1.00 14.92 ? 541  CYS   A CB  1 
ATOM   856  S  SG  . CYS   A 1 100 ? 25.780 62.327  18.573 1.00 20.65 ? 541  CYS   A SG  1 
ATOM   857  N  N   . ALA   A 1 101 ? 21.832 61.205  21.275 1.00 13.42 ? 542  ALA   A N   1 
ATOM   858  C  CA  . ALA   A 1 101 ? 20.852 60.350  21.925 1.00 14.07 ? 542  ALA   A CA  1 
ATOM   859  C  C   . ALA   A 1 101 ? 19.478 60.500  21.281 1.00 12.61 ? 542  ALA   A C   1 
ATOM   860  O  O   . ALA   A 1 101 ? 18.754 59.507  21.123 1.00 15.28 ? 542  ALA   A O   1 
ATOM   861  C  CB  . ALA   A 1 101 ? 20.803 60.649  23.421 1.00 14.83 ? 542  ALA   A CB  1 
ATOM   862  N  N   . LEU   A 1 102 ? 19.104 61.733  20.898 1.00 12.98 ? 543  LEU   A N   1 
ATOM   863  C  CA  . LEU   A 1 102 ? 17.837 61.953  20.200 1.00 15.01 ? 543  LEU   A CA  1 
ATOM   864  C  C   . LEU   A 1 102 ? 17.824 61.218  18.869 1.00 15.55 ? 543  LEU   A C   1 
ATOM   865  O  O   . LEU   A 1 102 ? 16.790 60.667  18.454 1.00 13.75 ? 543  LEU   A O   1 
ATOM   866  C  CB  . LEU   A 1 102 ? 17.645 63.446  19.916 1.00 16.02 ? 543  LEU   A CB  1 
ATOM   867  C  CG  . LEU   A 1 102 ? 17.337 64.392  21.073 1.00 18.26 ? 543  LEU   A CG  1 
ATOM   868  C  CD1 . LEU   A 1 102 ? 17.109 65.804  20.518 1.00 17.20 ? 543  LEU   A CD1 1 
ATOM   869  C  CD2 . LEU   A 1 102 ? 16.125 63.927  21.847 1.00 18.45 ? 543  LEU   A CD2 1 
ATOM   870  N  N   . LEU   A 1 103 ? 18.961 61.238  18.171 1.00 15.85 ? 544  LEU   A N   1 
ATOM   871  C  CA  . LEU   A 1 103 ? 19.062 60.599  16.866 1.00 15.16 ? 544  LEU   A CA  1 
ATOM   872  C  C   . LEU   A 1 103 ? 18.975 59.082  16.986 1.00 15.00 ? 544  LEU   A C   1 
ATOM   873  O  O   . LEU   A 1 103 ? 18.358 58.419  16.141 1.00 15.55 ? 544  LEU   A O   1 
ATOM   874  C  CB  . LEU   A 1 103 ? 20.367 61.033  16.190 1.00 19.31 ? 544  LEU   A CB  1 
ATOM   875  C  CG  . LEU   A 1 103 ? 20.591 60.659  14.720 1.00 27.06 ? 544  LEU   A CG  1 
ATOM   876  C  CD1 . LEU   A 1 103 ? 19.419 61.097  13.848 1.00 29.97 ? 544  LEU   A CD1 1 
ATOM   877  C  CD2 . LEU   A 1 103 ? 21.894 61.260  14.207 1.00 27.65 ? 544  LEU   A CD2 1 
ATOM   878  N  N   . ALA   A 1 104 ? 19.588 58.514  18.027 1.00 14.56 ? 545  ALA   A N   1 
ATOM   879  C  CA  . ALA   A 1 104 ? 19.487 57.077  18.252 1.00 14.05 ? 545  ALA   A CA  1 
ATOM   880  C  C   . ALA   A 1 104 ? 18.032 56.675  18.461 1.00 13.65 ? 545  ALA   A C   1 
ATOM   881  O  O   . ALA   A 1 104 ? 17.550 55.708  17.862 1.00 14.86 ? 545  ALA   A O   1 
ATOM   882  C  CB  . ALA   A 1 104 ? 20.342 56.674  19.459 1.00 13.62 ? 545  ALA   A CB  1 
ATOM   883  N  N   . ALA   A 1 105 ? 17.305 57.436  19.282 1.00 14.96 ? 546  ALA   A N   1 
ATOM   884  C  CA  . ALA   A 1 105 ? 15.909 57.113  19.566 1.00 12.94 ? 546  ALA   A CA  1 
ATOM   885  C  C   . ALA   A 1 105 ? 15.019 57.318  18.342 1.00 13.67 ? 546  ALA   A C   1 
ATOM   886  O  O   . ALA   A 1 105 ? 14.188 56.457  18.017 1.00 14.12 ? 546  ALA   A O   1 
ATOM   887  C  CB  . ALA   A 1 105 ? 15.412 57.941  20.754 1.00 15.17 ? 546  ALA   A CB  1 
ATOM   888  N  N   . GLY   A 1 106 ? 15.148 58.464  17.673 1.00 14.51 ? 547  GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 106 ? 14.288 58.737  16.527 1.00 14.38 ? 547  GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 106 ? 14.511 57.763  15.386 1.00 14.75 ? 547  GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 106 ? 13.571 57.397  14.670 1.00 15.87 ? 547  GLY   A O   1 
ATOM   892  N  N   . SER   A 1 107 ? 15.761 57.341  15.191 1.00 15.53 ? 548  SER   A N   1 
ATOM   893  C  CA  . SER   A 1 107 ? 16.063 56.306  14.207 1.00 14.46 ? 548  SER   A CA  1 
ATOM   894  C  C   . SER   A 1 107 ? 15.317 55.023  14.528 1.00 14.08 ? 548  SER   A C   1 
ATOM   895  O  O   . SER   A 1 107 ? 14.798 54.348  13.632 1.00 14.39 ? 548  SER   A O   1 
ATOM   896  C  CB  . SER   A 1 107 ? 17.571 56.044  14.177 1.00 15.12 ? 548  SER   A CB  1 
ATOM   897  O  OG  . SER   A 1 107 ? 18.267 57.178  13.683 1.00 18.62 ? 548  SER   A OG  1 
ATOM   898  N  N   . CYS   A 1 108 ? 15.249 54.679  15.810 1.00 13.59 ? 549  CYS   A N   1 
ATOM   899  C  CA  . CYS   A 1 108 ? 14.546 53.473  16.222 1.00 13.66 ? 549  CYS   A CA  1 
ATOM   900  C  C   . CYS   A 1 108 ? 13.032 53.637  16.085 1.00 13.91 ? 549  CYS   A C   1 
ATOM   901  O  O   . CYS   A 1 108 ? 12.346 52.679  15.708 1.00 14.64 ? 549  CYS   A O   1 
ATOM   902  C  CB  . CYS   A 1 108 ? 14.962 53.141  17.655 1.00 13.79 ? 549  CYS   A CB  1 
ATOM   903  S  SG  . CYS   A 1 108 ? 16.641 52.388  17.721 1.00 21.43 ? 549  CYS   A SG  1 
ATOM   904  N  N   . PHE   A 1 109 ? 12.499 54.837  16.350 1.00 13.65 ? 550  PHE   A N   1 
ATOM   905  C  CA  . PHE   A 1 109 ? 11.068 55.071  16.136 1.00 12.48 ? 550  PHE   A CA  1 
ATOM   906  C  C   . PHE   A 1 109 ? 10.716 54.885  14.667 1.00 13.15 ? 550  PHE   A C   1 
ATOM   907  O  O   . PHE   A 1 109 ? 9.730  54.219  14.328 1.00 13.91 ? 550  PHE   A O   1 
ATOM   908  C  CB  . PHE   A 1 109 ? 10.673 56.484  16.573 1.00 13.96 ? 550  PHE   A CB  1 
ATOM   909  C  CG  . PHE   A 1 109 ? 10.973 56.812  18.022 1.00 14.27 ? 550  PHE   A CG  1 
ATOM   910  C  CD1 . PHE   A 1 109 ? 11.245 55.826  18.962 1.00 13.68 ? 550  PHE   A CD1 1 
ATOM   911  C  CD2 . PHE   A 1 109 ? 10.977 58.139  18.431 1.00 15.45 ? 550  PHE   A CD2 1 
ATOM   912  C  CE1 . PHE   A 1 109 ? 11.533 56.168  20.281 1.00 13.10 ? 550  PHE   A CE1 1 
ATOM   913  C  CE2 . PHE   A 1 109 ? 11.238 58.484  19.746 1.00 14.86 ? 550  PHE   A CE2 1 
ATOM   914  C  CZ  . PHE   A 1 109 ? 11.522 57.503  20.664 1.00 14.11 ? 550  PHE   A CZ  1 
ATOM   915  N  N   . ASN   A 1 110 ? 11.510 55.479  13.772 1.00 14.16 ? 551  ASN   A N   1 
ATOM   916  C  CA  . ASN   A 1 110 ? 11.220 55.325  12.349 1.00 14.60 ? 551  ASN   A CA  1 
ATOM   917  C  C   . ASN   A 1 110 ? 11.285 53.861  11.938 1.00 15.65 ? 551  ASN   A C   1 
ATOM   918  O  O   . ASN   A 1 110 ? 10.512 53.412  11.085 1.00 15.98 ? 551  ASN   A O   1 
ATOM   919  C  CB  . ASN   A 1 110 ? 12.192 56.158  11.507 1.00 14.51 ? 551  ASN   A CB  1 
ATOM   920  C  CG  . ASN   A 1 110 ? 11.773 57.613  11.391 1.00 15.55 ? 551  ASN   A CG  1 
ATOM   921  O  OD1 . ASN   A 1 110 ? 10.733 58.009  11.903 1.00 16.14 ? 551  ASN   A OD1 1 
ATOM   922  N  ND2 . ASN   A 1 110 ? 12.594 58.417  10.722 1.00 16.35 ? 551  ASN   A ND2 1 
ATOM   923  N  N   . SER   A 1 111 ? 12.198 53.096  12.540 1.00 14.06 ? 552  SER   A N   1 
ATOM   924  C  CA  . SER   A 1 111 ? 12.326 51.683  12.196 1.00 13.29 ? 552  SER   A CA  1 
ATOM   925  C  C   . SER   A 1 111 ? 11.122 50.895  12.681 1.00 13.95 ? 552  SER   A C   1 
ATOM   926  O  O   . SER   A 1 111 ? 10.576 50.062  11.946 1.00 14.98 ? 552  SER   A O   1 
ATOM   927  C  CB  . SER   A 1 111 ? 13.608 51.110  12.796 1.00 15.23 ? 552  SER   A CB  1 
ATOM   928  O  OG  . SER   A 1 111 ? 14.739 51.757  12.239 1.00 16.00 ? 552  SER   A OG  1 
ATOM   929  N  N   . ALA   A 1 112 ? 10.685 51.154  13.920 1.00 12.79 ? 553  ALA   A N   1 
ATOM   930  C  CA  . ALA   A 1 112 ? 9.472  50.513  14.424 1.00 13.39 ? 553  ALA   A CA  1 
ATOM   931  C  C   . ALA   A 1 112 ? 8.265  50.874  13.566 1.00 13.63 ? 553  ALA   A C   1 
ATOM   932  O  O   . ALA   A 1 112 ? 7.428  50.016  13.266 1.00 14.27 ? 553  ALA   A O   1 
ATOM   933  C  CB  . ALA   A 1 112 ? 9.221  50.920  15.879 1.00 13.99 ? 553  ALA   A CB  1 
ATOM   934  N  N   . GLN   A 1 113 ? 8.155  52.145  13.174 1.00 14.32 ? 554  GLN   A N   1 
ATOM   935  C  CA  . GLN   A 1 113 ? 7.043  52.574  12.330 1.00 15.25 ? 554  GLN   A CA  1 
ATOM   936  C  C   . GLN   A 1 113 ? 7.069  51.858  10.987 1.00 17.69 ? 554  GLN   A C   1 
ATOM   937  O  O   . GLN   A 1 113 ? 6.019  51.453  10.474 1.00 16.02 ? 554  GLN   A O   1 
ATOM   938  C  CB  . GLN   A 1 113 ? 7.102  54.088  12.137 1.00 15.79 ? 554  GLN   A CB  1 
ATOM   939  C  CG  . GLN   A 1 113 ? 5.983  54.673  11.273 1.00 19.78 ? 554  GLN   A CG  1 
ATOM   940  C  CD  . GLN   A 1 113 ? 6.121  56.178  11.115 1.00 28.19 ? 554  GLN   A CD  1 
ATOM   941  O  OE1 . GLN   A 1 113 ? 7.123  56.667  10.592 1.00 31.39 ? 554  GLN   A OE1 1 
ATOM   942  N  NE2 . GLN   A 1 113 ? 5.104  56.915  11.534 1.00 30.11 ? 554  GLN   A NE2 1 
ATOM   943  N  N   . ALA   A 1 114 ? 8.258  51.679  10.406 1.00 15.82 ? 555  ALA   A N   1 
ATOM   944  C  CA  . ALA   A 1 114 ? 8.359  50.972  9.133  1.00 15.48 ? 555  ALA   A CA  1 
ATOM   945  C  C   . ALA   A 1 114 ? 7.902  49.521  9.274  1.00 16.29 ? 555  ALA   A C   1 
ATOM   946  O  O   . ALA   A 1 114 ? 7.207  48.993  8.395  1.00 15.69 ? 555  ALA   A O   1 
ATOM   947  C  CB  . ALA   A 1 114 ? 9.786  51.070  8.592  1.00 14.63 ? 555  ALA   A CB  1 
ATOM   948  N  N   . ILE   A 1 115 ? 8.241  48.879  10.398 1.00 14.17 ? 556  ILE   A N   1 
ATOM   949  C  CA  . ILE   A 1 115 ? 7.796  47.515  10.664 1.00 13.63 ? 556  ILE   A CA  1 
ATOM   950  C  C   . ILE   A 1 115 ? 6.287  47.476  10.883 1.00 15.47 ? 556  ILE   A C   1 
ATOM   951  O  O   . ILE   A 1 115 ? 5.577  46.650  10.297 1.00 16.77 ? 556  ILE   A O   1 
ATOM   952  C  CB  . ILE   A 1 115 ? 8.551  46.944  11.882 1.00 14.04 ? 556  ILE   A CB  1 
ATOM   953  C  CG1 . ILE   A 1 115 ? 10.031 46.740  11.544 1.00 12.93 ? 556  ILE   A CG1 1 
ATOM   954  C  CG2 . ILE   A 1 115 ? 7.929  45.622  12.334 1.00 14.79 ? 556  ILE   A CG2 1 
ATOM   955  C  CD1 . ILE   A 1 115 ? 10.909 46.398  12.765 1.00 15.02 ? 556  ILE   A CD1 1 
ATOM   956  N  N   . LEU   A 1 116 ? 5.772  48.373  11.725 1.00 15.03 ? 557  LEU   A N   1 
ATOM   957  C  CA  . LEU   A 1 116 ? 4.373  48.280  12.132 1.00 17.12 ? 557  LEU   A CA  1 
ATOM   958  C  C   . LEU   A 1 116 ? 3.408  48.700  11.035 1.00 19.65 ? 557  LEU   A C   1 
ATOM   959  O  O   . LEU   A 1 116 ? 2.235  48.307  11.082 1.00 21.12 ? 557  LEU   A O   1 
ATOM   960  C  CB  . LEU   A 1 116 ? 4.127  49.075  13.415 1.00 16.58 ? 557  LEU   A CB  1 
ATOM   961  C  CG  . LEU   A 1 116 ? 4.866  48.508  14.626 1.00 16.41 ? 557  LEU   A CG  1 
ATOM   962  C  CD1 . LEU   A 1 116 ? 4.921  49.543  15.735 1.00 16.69 ? 557  LEU   A CD1 1 
ATOM   963  C  CD2 . LEU   A 1 116 ? 4.204  47.217  15.090 1.00 17.93 ? 557  LEU   A CD2 1 
ATOM   964  N  N   . THR   A 1 117 ? 3.863  49.484  10.062 1.00 18.22 ? 558  THR   A N   1 
ATOM   965  C  CA  . THR   A 1 117 ? 3.042  49.842  8.913  1.00 16.88 ? 558  THR   A CA  1 
ATOM   966  C  C   . THR   A 1 117 ? 3.252  48.911  7.730  1.00 17.60 ? 558  THR   A C   1 
ATOM   967  O  O   . THR   A 1 117 ? 2.719  49.182  6.647  1.00 19.84 ? 558  THR   A O   1 
ATOM   968  C  CB  . THR   A 1 117 ? 3.300  51.290  8.492  1.00 18.14 ? 558  THR   A CB  1 
ATOM   969  O  OG1 . THR   A 1 117 ? 4.685  51.445  8.149  1.00 20.72 ? 558  THR   A OG1 1 
ATOM   970  C  CG2 . THR   A 1 117 ? 2.921  52.263  9.608  1.00 18.76 ? 558  THR   A CG2 1 
ATOM   971  N  N   . GLY   A 1 118 ? 4.006  47.830  7.902  1.00 17.19 ? 559  GLY   A N   1 
ATOM   972  C  CA  . GLY   A 1 118 ? 4.211  46.864  6.844  1.00 18.71 ? 559  GLY   A CA  1 
ATOM   973  C  C   . GLY   A 1 118 ? 5.135  47.295  5.725  1.00 23.49 ? 559  GLY   A C   1 
ATOM   974  O  O   . GLY   A 1 118 ? 5.135  46.653  4.667  1.00 25.02 ? 559  GLY   A O   1 
ATOM   975  N  N   . GLN   A 1 119 ? 5.917  48.362  5.910  1.00 19.98 ? 560  GLN   A N   1 
ATOM   976  C  CA  . GLN   A 1 119 ? 6.867  48.772  4.877  1.00 21.20 ? 560  GLN   A CA  1 
ATOM   977  C  C   . GLN   A 1 119 ? 8.066  47.833  4.825  1.00 17.75 ? 560  GLN   A C   1 
ATOM   978  O  O   . GLN   A 1 119 ? 8.618  47.578  3.748  1.00 18.28 ? 560  GLN   A O   1 
ATOM   979  C  CB  . GLN   A 1 119 ? 7.319  50.215  5.104  1.00 26.85 ? 560  GLN   A CB  1 
ATOM   980  C  CG  . GLN   A 1 119 ? 6.231  51.266  4.897  1.00 34.75 ? 560  GLN   A CG  1 
ATOM   981  C  CD  . GLN   A 1 119 ? 6.602  52.614  5.494  0.74 36.20 ? 560  GLN   A CD  1 
ATOM   982  O  OE1 . GLN   A 1 119 ? 7.744  53.061  5.385  0.50 38.21 ? 560  GLN   A OE1 1 
ATOM   983  N  NE2 . GLN   A 1 119 ? 5.642  53.256  6.149  0.67 35.85 ? 560  GLN   A NE2 1 
ATOM   984  N  N   . VAL   A 1 120 ? 8.498  47.331  5.984  1.00 17.58 ? 561  VAL   A N   1 
ATOM   985  C  CA  . VAL   A 1 120 ? 9.532  46.311  6.073  1.00 16.79 ? 561  VAL   A CA  1 
ATOM   986  C  C   . VAL   A 1 120 ? 9.042  45.232  7.028  1.00 16.43 ? 561  VAL   A C   1 
ATOM   987  O  O   . VAL   A 1 120 ? 8.172  45.462  7.874  1.00 17.42 ? 561  VAL   A O   1 
ATOM   988  C  CB  . VAL   A 1 120 ? 10.897 46.877  6.540  1.00 15.12 ? 561  VAL   A CB  1 
ATOM   989  C  CG1 . VAL   A 1 120 ? 11.324 48.044  5.672  1.00 16.87 ? 561  VAL   A CG1 1 
ATOM   990  C  CG2 . VAL   A 1 120 ? 10.811 47.320  7.994  1.00 16.62 ? 561  VAL   A CG2 1 
ATOM   991  N  N   . ARG   A 1 121 ? 9.593  44.032  6.869  1.00 15.65 ? 562  ARG   A N   1 
ATOM   992  C  CA  . ARG   A 1 121 ? 9.278  42.955  7.796  1.00 18.39 ? 562  ARG   A CA  1 
ATOM   993  C  C   . ARG   A 1 121 ? 10.032 43.109  9.112  1.00 15.99 ? 562  ARG   A C   1 
ATOM   994  O  O   . ARG   A 1 121 ? 9.454  42.900  10.186 1.00 16.56 ? 562  ARG   A O   1 
ATOM   995  C  CB  . ARG   A 1 121 ? 9.610  41.604  7.167  1.00 22.40 ? 562  ARG   A CB  1 
ATOM   996  C  CG  . ARG   A 1 121 ? 9.253  40.422  8.040  1.00 37.21 ? 562  ARG   A CG  1 
ATOM   997  C  CD  . ARG   A 1 121 ? 9.621  39.118  7.371  1.00 49.56 ? 562  ARG   A CD  1 
ATOM   998  N  NE  . ARG   A 1 121 ? 8.698  38.054  7.747  1.00 57.81 ? 562  ARG   A NE  1 
ATOM   999  C  CZ  . ARG   A 1 121 ? 9.055  36.948  8.389  1.00 61.89 ? 562  ARG   A CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 121 ? 10.323 36.757  8.734  1.00 52.76 ? 562  ARG   A NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 121 ? 8.140  36.035  8.691  1.00 64.96 ? 562  ARG   A NH2 1 
ATOM   1002 N  N   . ASN   A 1 122 ? 11.314 43.477  9.046  1.00 14.40 ? 563  ASN   A N   1 
ATOM   1003 C  CA  . ASN   A 1 122 ? 12.185 43.515  10.213 1.00 12.35 ? 563  ASN   A CA  1 
ATOM   1004 C  C   . ASN   A 1 122 ? 13.236 44.586  9.953  1.00 14.50 ? 563  ASN   A C   1 
ATOM   1005 O  O   . ASN   A 1 122 ? 13.287 45.176  8.869  1.00 14.41 ? 563  ASN   A O   1 
ATOM   1006 C  CB  . ASN   A 1 122 ? 12.772 42.127  10.483 1.00 13.69 ? 563  ASN   A CB  1 
ATOM   1007 C  CG  . ASN   A 1 122 ? 13.516 41.542  9.278  1.00 14.18 ? 563  ASN   A CG  1 
ATOM   1008 O  OD1 . ASN   A 1 122 ? 14.199 42.261  8.560  1.00 16.01 ? 563  ASN   A OD1 1 
ATOM   1009 N  ND2 . ASN   A 1 122 ? 13.414 40.228  9.091  1.00 14.51 ? 563  ASN   A ND2 1 
ATOM   1010 N  N   . ALA   A 1 123 ? 14.063 44.871  10.962 1.00 12.88 ? 564  ALA   A N   1 
ATOM   1011 C  CA  . ALA   A 1 123 ? 15.021 45.953  10.779 1.00 13.82 ? 564  ALA   A CA  1 
ATOM   1012 C  C   . ALA   A 1 123 ? 16.152 45.873  11.793 1.00 13.09 ? 564  ALA   A C   1 
ATOM   1013 O  O   . ALA   A 1 123 ? 16.042 45.226  12.836 1.00 12.78 ? 564  ALA   A O   1 
ATOM   1014 C  CB  . ALA   A 1 123 ? 14.362 47.334  10.847 1.00 13.64 ? 564  ALA   A CB  1 
ATOM   1015 N  N   A VAL   A 1 124 ? 17.242 46.564  11.468 0.79 13.30 ? 565  VAL   A N   1 
ATOM   1016 N  N   B VAL   A 1 124 ? 17.244 46.559  11.455 0.21 12.15 ? 565  VAL   A N   1 
ATOM   1017 C  CA  A VAL   A 1 124 ? 18.413 46.674  12.331 0.79 13.22 ? 565  VAL   A CA  1 
ATOM   1018 C  CA  B VAL   A 1 124 ? 18.417 46.709  12.308 0.21 10.87 ? 565  VAL   A CA  1 
ATOM   1019 C  C   A VAL   A 1 124 ? 18.755 48.153  12.492 0.79 11.59 ? 565  VAL   A C   1 
ATOM   1020 C  C   B VAL   A 1 124 ? 18.650 48.196  12.520 0.21 12.67 ? 565  VAL   A C   1 
ATOM   1021 O  O   A VAL   A 1 124 ? 18.712 48.917  11.521 0.79 14.33 ? 565  VAL   A O   1 
ATOM   1022 O  O   B VAL   A 1 124 ? 18.436 49.002  11.608 0.21 11.03 ? 565  VAL   A O   1 
ATOM   1023 C  CB  A VAL   A 1 124 ? 19.599 45.855  11.760 0.79 13.08 ? 565  VAL   A CB  1 
ATOM   1024 C  CB  B VAL   A 1 124 ? 19.657 46.055  11.660 0.21 8.61  ? 565  VAL   A CB  1 
ATOM   1025 C  CG1 A VAL   A 1 124 ? 20.061 46.390  10.401 0.79 12.95 ? 565  VAL   A CG1 1 
ATOM   1026 C  CG1 B VAL   A 1 124 ? 20.962 46.624  12.233 0.21 12.19 ? 565  VAL   A CG1 1 
ATOM   1027 C  CG2 A VAL   A 1 124 ? 20.766 45.801  12.731 0.79 14.93 ? 565  VAL   A CG2 1 
ATOM   1028 C  CG2 B VAL   A 1 124 ? 19.607 44.564  11.843 0.21 8.95  ? 565  VAL   A CG2 1 
ATOM   1029 N  N   . ALA   A 1 125 ? 19.096 48.559  13.721 1.00 12.28 ? 566  ALA   A N   1 
ATOM   1030 C  CA  . ALA   A 1 125 ? 19.382 49.954  14.051 1.00 11.47 ? 566  ALA   A CA  1 
ATOM   1031 C  C   . ALA   A 1 125 ? 20.801 50.057  14.589 1.00 11.49 ? 566  ALA   A C   1 
ATOM   1032 O  O   . ALA   A 1 125 ? 21.091 49.589  15.698 1.00 14.30 ? 566  ALA   A O   1 
ATOM   1033 C  CB  . ALA   A 1 125 ? 18.381 50.507  15.060 1.00 13.32 ? 566  ALA   A CB  1 
ATOM   1034 N  N   . ILE   A 1 126 ? 21.680 50.668  13.796 1.00 12.64 ? 567  ILE   A N   1 
ATOM   1035 C  CA  . ILE   A 1 126 ? 23.100 50.810  14.148 1.00 12.60 ? 567  ILE   A CA  1 
ATOM   1036 C  C   . ILE   A 1 126 ? 23.238 52.184  14.791 1.00 12.60 ? 567  ILE   A C   1 
ATOM   1037 O  O   . ILE   A 1 126 ? 23.466 53.190  14.108 1.00 13.83 ? 567  ILE   A O   1 
ATOM   1038 C  CB  . ILE   A 1 126 ? 24.009 50.641  12.927 1.00 11.98 ? 567  ILE   A CB  1 
ATOM   1039 C  CG1 . ILE   A 1 126 ? 23.718 49.327  12.201 1.00 15.07 ? 567  ILE   A CG1 1 
ATOM   1040 C  CG2 . ILE   A 1 126 ? 25.472 50.710  13.341 1.00 12.96 ? 567  ILE   A CG2 1 
ATOM   1041 C  CD1 . ILE   A 1 126 ? 24.396 49.225  10.832 1.00 15.19 ? 567  ILE   A CD1 1 
ATOM   1042 N  N   . VAL   A 1 127 ? 23.091 52.230  16.130 1.00 14.08 ? 568  VAL   A N   1 
ATOM   1043 C  CA  . VAL   A 1 127 ? 22.933 53.478  16.876 1.00 11.39 ? 568  VAL   A CA  1 
ATOM   1044 C  C   . VAL   A 1 127 ? 23.835 53.528  18.101 1.00 12.65 ? 568  VAL   A C   1 
ATOM   1045 O  O   . VAL   A 1 127 ? 24.166 52.502  18.703 1.00 13.51 ? 568  VAL   A O   1 
ATOM   1046 C  CB  . VAL   A 1 127 ? 21.465 53.723  17.307 1.00 12.49 ? 568  VAL   A CB  1 
ATOM   1047 C  CG1 . VAL   A 1 127 ? 20.560 53.881  16.078 1.00 13.54 ? 568  VAL   A CG1 1 
ATOM   1048 C  CG2 . VAL   A 1 127 ? 20.950 52.607  18.234 1.00 12.47 ? 568  VAL   A CG2 1 
ATOM   1049 N  N   . ARG   A 1 128 ? 24.176 54.751  18.488 1.00 11.67 ? 569  ARG   A N   1 
ATOM   1050 C  CA  . ARG   A 1 128 ? 24.839 55.059  19.750 1.00 11.79 ? 569  ARG   A CA  1 
ATOM   1051 C  C   . ARG   A 1 128 ? 24.508 56.502  20.096 1.00 12.48 ? 569  ARG   A C   1 
ATOM   1052 O  O   . ARG   A 1 128 ? 24.112 57.279  19.218 1.00 13.87 ? 569  ARG   A O   1 
ATOM   1053 C  CB  . ARG   A 1 128 ? 26.356 54.867  19.634 1.00 11.38 ? 569  ARG   A CB  1 
ATOM   1054 C  CG  . ARG   A 1 128 ? 27.066 55.960  18.831 1.00 12.53 ? 569  ARG   A CG  1 
ATOM   1055 C  CD  . ARG   A 1 128 ? 28.571 55.693  18.748 1.00 11.87 ? 569  ARG   A CD  1 
ATOM   1056 N  NE  . ARG   A 1 128 ? 29.322 56.042  19.956 1.00 13.37 ? 569  ARG   A NE  1 
ATOM   1057 C  CZ  . ARG   A 1 128 ? 29.781 57.261  20.239 1.00 14.25 ? 569  ARG   A CZ  1 
ATOM   1058 N  NH1 . ARG   A 1 128 ? 29.527 58.281  19.433 1.00 14.28 ? 569  ARG   A NH1 1 
ATOM   1059 N  NH2 . ARG   A 1 128 ? 30.506 57.461  21.344 1.00 13.22 ? 569  ARG   A NH2 1 
ATOM   1060 N  N   . PRO   A 1 129 ? 24.614 56.894  21.381 1.00 13.76 ? 570  PRO   A N   1 
ATOM   1061 C  CA  . PRO   A 1 129 ? 24.925 56.100  22.577 1.00 13.32 ? 570  PRO   A CA  1 
ATOM   1062 C  C   . PRO   A 1 129 ? 23.845 55.062  22.879 1.00 13.39 ? 570  PRO   A C   1 
ATOM   1063 O  O   . PRO   A 1 129 ? 22.716 55.183  22.388 1.00 14.41 ? 570  PRO   A O   1 
ATOM   1064 C  CB  . PRO   A 1 129 ? 24.979 57.153  23.696 1.00 13.62 ? 570  PRO   A CB  1 
ATOM   1065 C  CG  . PRO   A 1 129 ? 24.108 58.254  23.222 1.00 13.01 ? 570  PRO   A CG  1 
ATOM   1066 C  CD  . PRO   A 1 129 ? 24.321 58.297  21.726 1.00 14.13 ? 570  PRO   A CD  1 
ATOM   1067 N  N   . PRO   A 1 130 ? 24.200 54.047  23.655 1.00 12.46 ? 571  PRO   A N   1 
ATOM   1068 C  CA  . PRO   A 1 130 ? 23.235 53.006  24.034 1.00 12.12 ? 571  PRO   A CA  1 
ATOM   1069 C  C   . PRO   A 1 130 ? 22.147 53.521  24.960 1.00 12.98 ? 571  PRO   A C   1 
ATOM   1070 O  O   . PRO   A 1 130 ? 22.169 54.687  25.369 1.00 14.37 ? 571  PRO   A O   1 
ATOM   1071 C  CB  . PRO   A 1 130 ? 24.106 51.961  24.742 1.00 12.64 ? 571  PRO   A CB  1 
ATOM   1072 C  CG  . PRO   A 1 130 ? 25.249 52.748  25.279 1.00 13.01 ? 571  PRO   A CG  1 
ATOM   1073 C  CD  . PRO   A 1 130 ? 25.535 53.784  24.222 1.00 13.26 ? 571  PRO   A CD  1 
ATOM   1074 N  N   . GLY   A 1 131 ? 21.201 52.649  25.314 1.00 13.19 ? 572  GLY   A N   1 
ATOM   1075 C  CA  . GLY   A 1 131 ? 20.042 53.077  26.080 1.00 12.31 ? 572  GLY   A CA  1 
ATOM   1076 C  C   . GLY   A 1 131 ? 19.667 52.300  27.328 1.00 12.21 ? 572  GLY   A C   1 
ATOM   1077 O  O   . GLY   A 1 131 ? 19.017 52.881  28.202 1.00 12.38 ? 572  GLY   A O   1 
ATOM   1078 N  N   . HIS   A 1 132 ? 20.027 51.017  27.448 1.00 12.44 ? 573  HIS   A N   1 
ATOM   1079 C  CA  . HIS   A 1 132 ? 19.268 50.174  28.384 1.00 12.19 ? 573  HIS   A CA  1 
ATOM   1080 C  C   . HIS   A 1 132 ? 19.563 50.420  29.864 1.00 12.41 ? 573  HIS   A C   1 
ATOM   1081 O  O   . HIS   A 1 132 ? 18.778 49.971  30.710 1.00 13.97 ? 573  HIS   A O   1 
ATOM   1082 C  CB  . HIS   A 1 132 ? 19.356 48.681  28.043 1.00 12.23 ? 573  HIS   A CB  1 
ATOM   1083 C  CG  . HIS   A 1 132 ? 20.705 48.069  28.251 1.00 12.41 ? 573  HIS   A CG  1 
ATOM   1084 N  ND1 . HIS   A 1 132 ? 20.867 46.732  28.543 1.00 15.05 ? 573  HIS   A ND1 1 
ATOM   1085 C  CD2 . HIS   A 1 132 ? 21.952 48.596  28.179 1.00 14.96 ? 573  HIS   A CD2 1 
ATOM   1086 C  CE1 . HIS   A 1 132 ? 22.156 46.466  28.666 1.00 15.73 ? 573  HIS   A CE1 1 
ATOM   1087 N  NE2 . HIS   A 1 132 ? 22.838 47.573  28.432 1.00 17.38 ? 573  HIS   A NE2 1 
ATOM   1088 N  N   . HIS   A 1 133 ? 20.635 51.132  30.203 1.00 12.36 ? 574  HIS   A N   1 
ATOM   1089 C  CA  . HIS   A 1 133 ? 20.872 51.491  31.598 1.00 13.58 ? 574  HIS   A CA  1 
ATOM   1090 C  C   . HIS   A 1 133 ? 20.171 52.772  32.009 1.00 13.65 ? 574  HIS   A C   1 
ATOM   1091 O  O   . HIS   A 1 133 ? 20.118 53.067  33.208 1.00 14.16 ? 574  HIS   A O   1 
ATOM   1092 C  CB  . HIS   A 1 133 ? 22.368 51.674  31.856 1.00 13.84 ? 574  HIS   A CB  1 
ATOM   1093 C  CG  . HIS   A 1 133 ? 23.153 50.414  31.724 1.00 14.16 ? 574  HIS   A CG  1 
ATOM   1094 N  ND1 . HIS   A 1 133 ? 22.836 49.272  32.424 1.00 15.02 ? 574  HIS   A ND1 1 
ATOM   1095 C  CD2 . HIS   A 1 133 ? 24.227 50.106  30.965 1.00 14.94 ? 574  HIS   A CD2 1 
ATOM   1096 C  CE1 . HIS   A 1 133 ? 23.693 48.316  32.111 1.00 15.62 ? 574  HIS   A CE1 1 
ATOM   1097 N  NE2 . HIS   A 1 133 ? 24.550 48.798  31.235 1.00 15.70 ? 574  HIS   A NE2 1 
ATOM   1098 N  N   . ALA   A 1 134 ? 19.638 53.537  31.055 1.00 13.78 ? 575  ALA   A N   1 
ATOM   1099 C  CA  . ALA   A 1 134 ? 18.985 54.801  31.385 1.00 13.60 ? 575  ALA   A CA  1 
ATOM   1100 C  C   . ALA   A 1 134 ? 17.662 54.553  32.089 1.00 14.03 ? 575  ALA   A C   1 
ATOM   1101 O  O   . ALA   A 1 134 ? 16.848 53.734  31.655 1.00 14.29 ? 575  ALA   A O   1 
ATOM   1102 C  CB  . ALA   A 1 134 ? 18.759 55.639  30.128 1.00 15.23 ? 575  ALA   A CB  1 
ATOM   1103 N  N   . GLU   A 1 135 ? 17.457 55.270  33.178 1.00 14.49 ? 576  GLU   A N   1 
ATOM   1104 C  CA  . GLU   A 1 135 ? 16.249 55.177  33.978 1.00 15.19 ? 576  GLU   A CA  1 
ATOM   1105 C  C   . GLU   A 1 135 ? 15.311 56.329  33.638 1.00 15.16 ? 576  GLU   A C   1 
ATOM   1106 O  O   . GLU   A 1 135 ? 15.671 57.268  32.931 1.00 16.55 ? 576  GLU   A O   1 
ATOM   1107 C  CB  . GLU   A 1 135 ? 16.613 55.195  35.469 1.00 15.62 ? 576  GLU   A CB  1 
ATOM   1108 C  CG  . GLU   A 1 135 ? 17.580 54.090  35.885 1.00 17.71 ? 576  GLU   A CG  1 
ATOM   1109 C  CD  . GLU   A 1 135 ? 16.872 52.835  36.365 1.00 21.76 ? 576  GLU   A CD  1 
ATOM   1110 O  OE1 . GLU   A 1 135 ? 15.625 52.794  36.317 1.00 23.62 ? 576  GLU   A OE1 1 
ATOM   1111 O  OE2 . GLU   A 1 135 ? 17.564 51.881  36.792 1.00 22.90 ? 576  GLU   A OE2 1 
ATOM   1112 N  N   . LYS   A 1 136 ? 14.090 56.256  34.171 1.00 16.71 ? 577  LYS   A N   1 
ATOM   1113 C  CA  . LYS   A 1 136 ? 13.151 57.363  34.003 1.00 17.53 ? 577  LYS   A CA  1 
ATOM   1114 C  C   . LYS   A 1 136 ? 13.800 58.701  34.328 1.00 16.70 ? 577  LYS   A C   1 
ATOM   1115 O  O   . LYS   A 1 136 ? 13.649 59.674  33.578 1.00 16.88 ? 577  LYS   A O   1 
ATOM   1116 C  CB  . LYS   A 1 136 ? 11.916 57.143  34.880 1.00 18.20 ? 577  LYS   A CB  1 
ATOM   1117 C  CG  . LYS   A 1 136 ? 10.839 58.206  34.704 1.00 26.69 ? 577  LYS   A CG  1 
ATOM   1118 C  CD  . LYS   A 1 136 ? 9.632  57.939  35.589 1.00 32.50 ? 577  LYS   A CD  1 
ATOM   1119 C  CE  . LYS   A 1 136 ? 8.759  59.183  35.722 1.00 40.88 ? 577  LYS   A CE  1 
ATOM   1120 N  NZ  . LYS   A 1 136 ? 7.301  58.854  35.749 1.00 44.93 ? 577  LYS   A NZ  1 
ATOM   1121 N  N   . ASP   A 1 137 ? 14.564 58.757  35.421 1.00 15.93 ? 578  ASP   A N   1 
ATOM   1122 C  CA  . ASP   A 1 137 ? 15.020 60.022  35.985 1.00 18.20 ? 578  ASP   A CA  1 
ATOM   1123 C  C   . ASP   A 1 137 ? 16.538 60.194  35.993 1.00 19.00 ? 578  ASP   A C   1 
ATOM   1124 O  O   . ASP   A 1 137 ? 17.025 61.170  36.573 1.00 21.35 ? 578  ASP   A O   1 
ATOM   1125 C  CB  . ASP   A 1 137 ? 14.451 60.186  37.404 1.00 31.43 ? 578  ASP   A CB  1 
ATOM   1126 C  CG  . ASP   A 1 137 ? 14.484 61.626  37.900 1.00 44.71 ? 578  ASP   A CG  1 
ATOM   1127 O  OD1 . ASP   A 1 137 ? 13.773 62.479  37.330 1.00 45.83 ? 578  ASP   A OD1 1 
ATOM   1128 O  OD2 . ASP   A 1 137 ? 15.214 61.897  38.881 1.00 44.72 ? 578  ASP   A OD2 1 
ATOM   1129 N  N   . THR   A 1 138 ? 17.303 59.304  35.361 1.00 17.86 ? 579  THR   A N   1 
ATOM   1130 C  CA  . THR   A 1 138 ? 18.756 59.457  35.429 1.00 16.65 ? 579  THR   A CA  1 
ATOM   1131 C  C   . THR   A 1 138 ? 19.440 58.736  34.271 1.00 17.54 ? 579  THR   A C   1 
ATOM   1132 O  O   . THR   A 1 138 ? 18.898 57.795  33.685 1.00 16.77 ? 579  THR   A O   1 
ATOM   1133 C  CB  . THR   A 1 138 ? 19.317 59.014  36.794 1.00 17.46 ? 579  THR   A CB  1 
ATOM   1134 O  OG1 . THR   A 1 138 ? 20.583 59.640  37.016 1.00 21.91 ? 579  THR   A OG1 1 
ATOM   1135 C  CG2 . THR   A 1 138 ? 19.476 57.505  36.869 1.00 17.95 ? 579  THR   A CG2 1 
ATOM   1136 N  N   . ALA   A 1 139 ? 20.637 59.215  33.940 1.00 15.85 ? 580  ALA   A N   1 
ATOM   1137 C  CA  . ALA   A 1 139 ? 21.531 58.561  32.996 1.00 16.11 ? 580  ALA   A CA  1 
ATOM   1138 C  C   . ALA   A 1 139 ? 22.468 57.612  33.740 1.00 16.13 ? 580  ALA   A C   1 
ATOM   1139 O  O   . ALA   A 1 139 ? 22.723 57.767  34.939 1.00 17.57 ? 580  ALA   A O   1 
ATOM   1140 C  CB  . ALA   A 1 139 ? 22.358 59.603  32.249 1.00 17.03 ? 580  ALA   A CB  1 
ATOM   1141 N  N   . CYS   A 1 140 ? 22.991 56.629  33.012 1.00 15.27 ? 581  CYS   A N   1 
ATOM   1142 C  CA  . CYS   A 1 140 ? 23.839 55.634  33.654 1.00 14.77 ? 581  CYS   A CA  1 
ATOM   1143 C  C   . CYS   A 1 140 ? 24.473 54.758  32.586 1.00 14.48 ? 581  CYS   A C   1 
ATOM   1144 O  O   . CYS   A 1 140 ? 23.833 54.424  31.585 1.00 14.82 ? 581  CYS   A O   1 
ATOM   1145 C  CB  . CYS   A 1 140 ? 23.009 54.755  34.598 1.00 15.31 ? 581  CYS   A CB  1 
ATOM   1146 S  SG  . CYS   A 1 140 ? 23.865 53.331  35.306 1.00 19.03 ? 581  CYS   A SG  1 
ATOM   1147 N  N   . GLY   A 1 141 ? 25.727 54.375  32.817 1.00 14.69 ? 582  GLY   A N   1 
ATOM   1148 C  CA  . GLY   A 1 141 ? 26.333 53.323  32.028 1.00 14.01 ? 582  GLY   A CA  1 
ATOM   1149 C  C   . GLY   A 1 141 ? 26.369 53.590  30.540 1.00 12.37 ? 582  GLY   A C   1 
ATOM   1150 O  O   . GLY   A 1 141 ? 26.007 52.722  29.734 1.00 14.02 ? 582  GLY   A O   1 
ATOM   1151 N  N   . PHE   A 1 142 ? 26.794 54.795  30.169 1.00 15.00 ? 583  PHE   A N   1 
ATOM   1152 C  CA  . PHE   A 1 142 ? 26.961 55.243  28.789 1.00 14.23 ? 583  PHE   A CA  1 
ATOM   1153 C  C   . PHE   A 1 142 ? 25.620 55.572  28.143 1.00 14.21 ? 583  PHE   A C   1 
ATOM   1154 O  O   . PHE   A 1 142 ? 25.594 55.895  26.946 1.00 14.05 ? 583  PHE   A O   1 
ATOM   1155 C  CB  . PHE   A 1 142 ? 27.737 54.281  27.871 1.00 14.83 ? 583  PHE   A CB  1 
ATOM   1156 C  CG  . PHE   A 1 142 ? 29.006 53.710  28.467 1.00 16.59 ? 583  PHE   A CG  1 
ATOM   1157 C  CD1 . PHE   A 1 142 ? 29.693 54.345  29.488 1.00 15.02 ? 583  PHE   A CD1 1 
ATOM   1158 C  CD2 . PHE   A 1 142 ? 29.521 52.525  27.955 1.00 17.43 ? 583  PHE   A CD2 1 
ATOM   1159 C  CE1 . PHE   A 1 142 ? 30.870 53.792  30.006 1.00 15.32 ? 583  PHE   A CE1 1 
ATOM   1160 C  CE2 . PHE   A 1 142 ? 30.688 51.971  28.460 1.00 18.31 ? 583  PHE   A CE2 1 
ATOM   1161 C  CZ  . PHE   A 1 142 ? 31.360 52.608  29.485 1.00 16.83 ? 583  PHE   A CZ  1 
ATOM   1162 N  N   . CYS   A 1 143 ? 24.517 55.518  28.891 1.00 14.05 ? 584  CYS   A N   1 
ATOM   1163 C  CA  . CYS   A 1 143 ? 23.169 55.648  28.338 1.00 13.05 ? 584  CYS   A CA  1 
ATOM   1164 C  C   . CYS   A 1 143 ? 22.495 56.904  28.889 1.00 15.53 ? 584  CYS   A C   1 
ATOM   1165 O  O   . CYS   A 1 143 ? 22.496 57.138  30.108 1.00 14.57 ? 584  CYS   A O   1 
ATOM   1166 C  CB  . CYS   A 1 143 ? 22.298 54.442  28.726 1.00 13.25 ? 584  CYS   A CB  1 
ATOM   1167 S  SG  . CYS   A 1 143 ? 22.902 52.842  28.242 1.00 31.97 ? 584  CYS   A SG  1 
ATOM   1168 N  N   . PHE   A 1 144 ? 21.882 57.694  27.995 1.00 14.42 ? 585  PHE   A N   1 
ATOM   1169 C  CA  . PHE   A 1 144 ? 21.171 58.913  28.383 1.00 15.16 ? 585  PHE   A CA  1 
ATOM   1170 C  C   . PHE   A 1 144 ? 19.660 58.733  28.423 1.00 13.04 ? 585  PHE   A C   1 
ATOM   1171 O  O   . PHE   A 1 144 ? 19.014 59.128  29.400 1.00 15.30 ? 585  PHE   A O   1 
ATOM   1172 C  CB  . PHE   A 1 144 ? 21.538 60.050  27.425 1.00 15.93 ? 585  PHE   A CB  1 
ATOM   1173 C  CG  . PHE   A 1 144 ? 22.976 60.440  27.511 1.00 15.25 ? 585  PHE   A CG  1 
ATOM   1174 C  CD1 . PHE   A 1 144 ? 23.407 61.314  28.496 1.00 16.62 ? 585  PHE   A CD1 1 
ATOM   1175 C  CD2 . PHE   A 1 144 ? 23.902 59.904  26.643 1.00 15.84 ? 585  PHE   A CD2 1 
ATOM   1176 C  CE1 . PHE   A 1 144 ? 24.734 61.671  28.590 1.00 15.63 ? 585  PHE   A CE1 1 
ATOM   1177 C  CE2 . PHE   A 1 144 ? 25.236 60.249  26.730 1.00 16.52 ? 585  PHE   A CE2 1 
ATOM   1178 C  CZ  . PHE   A 1 144 ? 25.649 61.131  27.710 1.00 15.88 ? 585  PHE   A CZ  1 
ATOM   1179 N  N   . PHE   A 1 145 ? 19.088 58.180  27.358 1.00 13.54 ? 586  PHE   A N   1 
ATOM   1180 C  CA  . PHE   A 1 145 ? 17.673 57.877  27.256 1.00 13.79 ? 586  PHE   A CA  1 
ATOM   1181 C  C   . PHE   A 1 145 ? 17.533 56.415  26.859 1.00 13.56 ? 586  PHE   A C   1 
ATOM   1182 O  O   . PHE   A 1 145 ? 18.398 55.851  26.182 1.00 15.08 ? 586  PHE   A O   1 
ATOM   1183 C  CB  . PHE   A 1 145 ? 16.982 58.773  26.209 1.00 14.14 ? 586  PHE   A CB  1 
ATOM   1184 C  CG  . PHE   A 1 145 ? 17.207 60.246  26.426 1.00 13.85 ? 586  PHE   A CG  1 
ATOM   1185 C  CD1 . PHE   A 1 145 ? 16.827 60.846  27.617 1.00 13.51 ? 586  PHE   A CD1 1 
ATOM   1186 C  CD2 . PHE   A 1 145 ? 17.800 61.028  25.447 1.00 15.73 ? 586  PHE   A CD2 1 
ATOM   1187 C  CE1 . PHE   A 1 145 ? 17.036 62.212  27.826 1.00 15.46 ? 586  PHE   A CE1 1 
ATOM   1188 C  CE2 . PHE   A 1 145 ? 18.008 62.390  25.648 1.00 17.10 ? 586  PHE   A CE2 1 
ATOM   1189 C  CZ  . PHE   A 1 145 ? 17.626 62.981  26.836 1.00 15.76 ? 586  PHE   A CZ  1 
ATOM   1190 N  N   . ASN   A 1 146 ? 16.448 55.785  27.308 1.00 12.82 ? 587  ASN   A N   1 
ATOM   1191 C  CA  . ASN   A 1 146 ? 16.314 54.343  27.121 1.00 12.42 ? 587  ASN   A CA  1 
ATOM   1192 C  C   . ASN   A 1 146 ? 15.659 54.083  25.774 1.00 13.40 ? 587  ASN   A C   1 
ATOM   1193 O  O   . ASN   A 1 146 ? 14.443 53.937  25.655 1.00 13.59 ? 587  ASN   A O   1 
ATOM   1194 C  CB  . ASN   A 1 146 ? 15.583 53.683  28.284 1.00 13.39 ? 587  ASN   A CB  1 
ATOM   1195 C  CG  . ASN   A 1 146 ? 15.751 52.175  28.275 1.00 12.06 ? 587  ASN   A CG  1 
ATOM   1196 O  OD1 . ASN   A 1 146 ? 15.680 51.539  27.206 1.00 14.02 ? 587  ASN   A OD1 1 
ATOM   1197 N  ND2 . ASN   A 1 146 ? 16.020 51.598  29.443 1.00 13.21 ? 587  ASN   A ND2 1 
ATOM   1198 N  N   . THR   A 1 147 ? 16.513 53.998  24.754 1.00 12.14 ? 588  THR   A N   1 
ATOM   1199 C  CA  . THR   A 1 147 ? 16.072 53.863  23.370 1.00 12.65 ? 588  THR   A CA  1 
ATOM   1200 C  C   . THR   A 1 147 ? 15.092 52.712  23.189 1.00 11.81 ? 588  THR   A C   1 
ATOM   1201 O  O   . THR   A 1 147 ? 14.025 52.887  22.587 1.00 12.18 ? 588  THR   A O   1 
ATOM   1202 C  CB  . THR   A 1 147 ? 17.310 53.666  22.512 1.00 14.10 ? 588  THR   A CB  1 
ATOM   1203 O  OG1 . THR   A 1 147 ? 18.140 54.823  22.652 1.00 16.12 ? 588  THR   A OG1 1 
ATOM   1204 C  CG2 . THR   A 1 147 ? 16.935 53.466  21.049 1.00 14.58 ? 588  THR   A CG2 1 
ATOM   1205 N  N   . ALA   A 1 148 ? 15.419 51.529  23.713 1.00 12.37 ? 589  ALA   A N   1 
ATOM   1206 C  CA  . ALA   A 1 148 ? 14.539 50.380  23.502 1.00 13.52 ? 589  ALA   A CA  1 
ATOM   1207 C  C   . ALA   A 1 148 ? 13.203 50.567  24.208 1.00 12.96 ? 589  ALA   A C   1 
ATOM   1208 O  O   . ALA   A 1 148 ? 12.142 50.253  23.650 1.00 13.93 ? 589  ALA   A O   1 
ATOM   1209 C  CB  . ALA   A 1 148 ? 15.212 49.094  23.978 1.00 14.64 ? 589  ALA   A CB  1 
ATOM   1210 N  N   . ALA   A 1 149 ? 13.234 51.058  25.445 1.00 12.78 ? 590  ALA   A N   1 
ATOM   1211 C  CA  . ALA   A 1 149 ? 11.997 51.299  26.177 1.00 12.52 ? 590  ALA   A CA  1 
ATOM   1212 C  C   . ALA   A 1 149 ? 11.149 52.352  25.482 1.00 12.72 ? 590  ALA   A C   1 
ATOM   1213 O  O   . ALA   A 1 149 ? 9.924  52.206  25.378 1.00 12.12 ? 590  ALA   A O   1 
ATOM   1214 C  CB  . ALA   A 1 149 ? 12.325 51.744  27.604 1.00 12.56 ? 590  ALA   A CB  1 
ATOM   1215 N  N   . LEU   A 1 150 ? 11.778 53.434  25.020 1.00 12.13 ? 591  LEU   A N   1 
ATOM   1216 C  CA  . LEU   A 1 150 ? 11.058 54.475  24.296 1.00 12.61 ? 591  LEU   A CA  1 
ATOM   1217 C  C   . LEU   A 1 150 ? 10.452 53.932  23.010 1.00 14.18 ? 591  LEU   A C   1 
ATOM   1218 O  O   . LEU   A 1 150 ? 9.351  54.336  22.610 1.00 14.60 ? 591  LEU   A O   1 
ATOM   1219 C  CB  . LEU   A 1 150 ? 12.011 55.622  23.959 1.00 13.35 ? 591  LEU   A CB  1 
ATOM   1220 C  CG  . LEU   A 1 150 ? 12.432 56.505  25.134 1.00 13.23 ? 591  LEU   A CG  1 
ATOM   1221 C  CD1 . LEU   A 1 150 ? 13.608 57.372  24.734 1.00 14.99 ? 591  LEU   A CD1 1 
ATOM   1222 C  CD2 . LEU   A 1 150 ? 11.245 57.365  25.590 1.00 15.12 ? 591  LEU   A CD2 1 
ATOM   1223 N  N   . THR   A 1 151 ? 11.165 53.030  22.334 1.00 12.92 ? 592  THR   A N   1 
ATOM   1224 C  CA  . THR   A 1 151 ? 10.653 52.463  21.090 1.00 12.96 ? 592  THR   A CA  1 
ATOM   1225 C  C   . THR   A 1 151 ? 9.436  51.584  21.354 1.00 13.14 ? 592  THR   A C   1 
ATOM   1226 O  O   . THR   A 1 151 ? 8.477  51.591  20.571 1.00 13.59 ? 592  THR   A O   1 
ATOM   1227 C  CB  . THR   A 1 151 ? 11.773 51.703  20.376 1.00 11.13 ? 592  THR   A CB  1 
ATOM   1228 O  OG1 . THR   A 1 151 ? 12.832 52.617  20.052 1.00 14.15 ? 592  THR   A OG1 1 
ATOM   1229 C  CG2 . THR   A 1 151 ? 11.258 51.073  19.090 1.00 13.69 ? 592  THR   A CG2 1 
ATOM   1230 N  N   . ALA   A 1 152 ? 9.448  50.829  22.454 1.00 12.57 ? 593  ALA   A N   1 
ATOM   1231 C  CA  . ALA   A 1 152 ? 8.263  50.067  22.843 1.00 12.96 ? 593  ALA   A CA  1 
ATOM   1232 C  C   . ALA   A 1 152 ? 7.069  50.988  23.075 1.00 13.78 ? 593  ALA   A C   1 
ATOM   1233 O  O   . ALA   A 1 152 ? 5.964  50.724  22.583 1.00 14.44 ? 593  ALA   A O   1 
ATOM   1234 C  CB  . ALA   A 1 152 ? 8.569  49.218  24.082 1.00 13.86 ? 593  ALA   A CB  1 
ATOM   1235 N  N   . ARG   A 1 153 ? 7.276  52.091  23.801 1.00 14.83 ? 594  ARG   A N   1 
ATOM   1236 C  CA  . ARG   A 1 153 ? 6.177  53.023  24.056 1.00 15.35 ? 594  ARG   A CA  1 
ATOM   1237 C  C   . ARG   A 1 153 ? 5.766  53.759  22.790 1.00 14.77 ? 594  ARG   A C   1 
ATOM   1238 O  O   . ARG   A 1 153 ? 4.571  54.011  22.571 1.00 15.70 ? 594  ARG   A O   1 
ATOM   1239 C  CB  . ARG   A 1 153 ? 6.553  54.026  25.149 1.00 14.70 ? 594  ARG   A CB  1 
ATOM   1240 C  CG  . ARG   A 1 153 ? 6.674  53.454  26.544 1.00 16.92 ? 594  ARG   A CG  1 
ATOM   1241 C  CD  . ARG   A 1 153 ? 5.397  52.782  27.000 1.00 21.09 ? 594  ARG   A CD  1 
ATOM   1242 N  NE  . ARG   A 1 153 ? 5.447  52.532  28.441 1.00 21.94 ? 594  ARG   A NE  1 
ATOM   1243 C  CZ  . ARG   A 1 153 ? 4.818  51.537  29.047 1.00 23.39 ? 594  ARG   A CZ  1 
ATOM   1244 N  NH1 . ARG   A 1 153 ? 4.074  50.686  28.343 1.00 21.27 ? 594  ARG   A NH1 1 
ATOM   1245 N  NH2 . ARG   A 1 153 ? 4.934  51.397  30.363 1.00 21.66 ? 594  ARG   A NH2 1 
ATOM   1246 N  N   . TYR   A 1 154 ? 6.737  54.121  21.949 1.00 15.28 ? 595  TYR   A N   1 
ATOM   1247 C  CA  . TYR   A 1 154 ? 6.405  54.742  20.675 1.00 13.28 ? 595  TYR   A CA  1 
ATOM   1248 C  C   . TYR   A 1 154 ? 5.551  53.804  19.828 1.00 14.97 ? 595  TYR   A C   1 
ATOM   1249 O  O   . TYR   A 1 154 ? 4.538  54.223  19.249 1.00 15.28 ? 595  TYR   A O   1 
ATOM   1250 C  CB  . TYR   A 1 154 ? 7.683  55.156  19.930 1.00 15.30 ? 595  TYR   A CB  1 
ATOM   1251 C  CG  . TYR   A 1 154 ? 7.372  55.578  18.520 1.00 16.21 ? 595  TYR   A CG  1 
ATOM   1252 C  CD1 . TYR   A 1 154 ? 6.960  56.874  18.242 1.00 16.10 ? 595  TYR   A CD1 1 
ATOM   1253 C  CD2 . TYR   A 1 154 ? 7.449  54.670  17.472 1.00 15.96 ? 595  TYR   A CD2 1 
ATOM   1254 C  CE1 . TYR   A 1 154 ? 6.628  57.258  16.942 1.00 15.69 ? 595  TYR   A CE1 1 
ATOM   1255 C  CE2 . TYR   A 1 154 ? 7.121  55.034  16.180 1.00 14.67 ? 595  TYR   A CE2 1 
ATOM   1256 C  CZ  . TYR   A 1 154 ? 6.721  56.327  15.921 1.00 15.32 ? 595  TYR   A CZ  1 
ATOM   1257 O  OH  . TYR   A 1 154 ? 6.404  56.656  14.615 1.00 17.10 ? 595  TYR   A OH  1 
ATOM   1258 N  N   . ALA   A 1 155 ? 5.936  52.526  19.764 1.00 14.65 ? 596  ALA   A N   1 
ATOM   1259 C  CA  . ALA   A 1 155 ? 5.167  51.540  19.013 1.00 13.64 ? 596  ALA   A CA  1 
ATOM   1260 C  C   . ALA   A 1 155 ? 3.731  51.497  19.507 1.00 15.31 ? 596  ALA   A C   1 
ATOM   1261 O  O   . ALA   A 1 155 ? 2.790  51.477  18.706 1.00 15.39 ? 596  ALA   A O   1 
ATOM   1262 C  CB  . ALA   A 1 155 ? 5.819  50.167  19.169 1.00 13.96 ? 596  ALA   A CB  1 
ATOM   1263 N  N   . GLN   A 1 156 ? 3.544  51.500  20.830 1.00 13.74 ? 597  GLN   A N   1 
ATOM   1264 C  CA  . GLN   A 1 156 ? 2.206  51.512  21.408 1.00 15.01 ? 597  GLN   A CA  1 
ATOM   1265 C  C   . GLN   A 1 156 ? 1.442  52.784  21.048 1.00 16.96 ? 597  GLN   A C   1 
ATOM   1266 O  O   . GLN   A 1 156 ? 0.229  52.733  20.810 1.00 17.86 ? 597  GLN   A O   1 
ATOM   1267 C  CB  . GLN   A 1 156 ? 2.298  51.293  22.922 1.00 13.64 ? 597  GLN   A CB  1 
ATOM   1268 C  CG  . GLN   A 1 156 ? 2.684  49.864  23.273 1.00 15.28 ? 597  GLN   A CG  1 
ATOM   1269 C  CD  . GLN   A 1 156 ? 2.960  49.648  24.751 1.00 17.75 ? 597  GLN   A CD  1 
ATOM   1270 O  OE1 . GLN   A 1 156 ? 3.201  50.597  25.500 1.00 18.66 ? 597  GLN   A OE1 1 
ATOM   1271 N  NE2 . GLN   A 1 156 ? 2.903  48.391  25.182 1.00 16.95 ? 597  GLN   A NE2 1 
ATOM   1272 N  N   . SER   A 1 157 ? 2.127  53.927  20.974 1.00 15.53 ? 598  SER   A N   1 
ATOM   1273 C  CA  . SER   A 1 157 ? 1.467  55.192  20.676 1.00 17.02 ? 598  SER   A CA  1 
ATOM   1274 C  C   . SER   A 1 157 ? 0.966  55.277  19.240 1.00 18.98 ? 598  SER   A C   1 
ATOM   1275 O  O   . SER   A 1 157 ? 0.077  56.088  18.959 1.00 19.77 ? 598  SER   A O   1 
ATOM   1276 C  CB  . SER   A 1 157 ? 2.415  56.362  20.937 1.00 17.97 ? 598  SER   A CB  1 
ATOM   1277 O  OG  . SER   A 1 157 ? 3.355  56.490  19.885 1.00 18.04 ? 598  SER   A OG  1 
ATOM   1278 N  N   . ILE   A 1 158 ? 1.529  54.494  18.317 1.00 16.81 ? 599  ILE   A N   1 
ATOM   1279 C  CA  . ILE   A 1 158 ? 1.089  54.519  16.922 1.00 15.76 ? 599  ILE   A CA  1 
ATOM   1280 C  C   . ILE   A 1 158 ? 0.286  53.294  16.541 1.00 17.14 ? 599  ILE   A C   1 
ATOM   1281 O  O   . ILE   A 1 158 ? -0.093 53.154  15.367 1.00 17.40 ? 599  ILE   A O   1 
ATOM   1282 C  CB  . ILE   A 1 158 ? 2.241  54.740  15.918 1.00 17.07 ? 599  ILE   A CB  1 
ATOM   1283 C  CG1 . ILE   A 1 158 ? 3.240  53.578  15.967 1.00 15.28 ? 599  ILE   A CG1 1 
ATOM   1284 C  CG2 . ILE   A 1 158 ? 2.915  56.080  16.155 1.00 18.14 ? 599  ILE   A CG2 1 
ATOM   1285 C  CD1 . ILE   A 1 158 ? 4.178  53.556  14.773 1.00 17.29 ? 599  ILE   A CD1 1 
ATOM   1286 N  N   . THR   A 1 159 ? 0.018  52.395  17.494 1.00 16.88 ? 600  THR   A N   1 
ATOM   1287 C  CA  . THR   A 1 159 ? -0.818 51.233  17.253 1.00 18.38 ? 600  THR   A CA  1 
ATOM   1288 C  C   . THR   A 1 159 ? -1.933 51.265  18.290 1.00 19.53 ? 600  THR   A C   1 
ATOM   1289 O  O   . THR   A 1 159 ? -2.917 52.004  18.121 1.00 19.78 ? 600  THR   A O   1 
ATOM   1290 C  CB  . THR   A 1 159 ? 0.012  49.936  17.232 1.00 17.99 ? 600  THR   A CB  1 
ATOM   1291 O  OG1 . THR   A 1 159 ? 0.714  49.770  18.478 1.00 17.14 ? 600  THR   A OG1 1 
ATOM   1292 C  CG2 . THR   A 1 159 ? 1.012  49.961  16.090 1.00 16.10 ? 600  THR   A CG2 1 
ATOM   1293 N  N   . ARG   A 1 160 ? -1.819 50.498  19.369 1.00 19.13 ? 601  ARG   A N   1 
ATOM   1294 C  CA  . ARG   A 1 160 ? -2.741 50.596  20.485 1.00 19.56 ? 601  ARG   A CA  1 
ATOM   1295 C  C   . ARG   A 1 160 ? -1.934 50.495  21.767 1.00 18.98 ? 601  ARG   A C   1 
ATOM   1296 O  O   . ARG   A 1 160 ? -0.851 49.903  21.790 1.00 18.78 ? 601  ARG   A O   1 
ATOM   1297 C  CB  . ARG   A 1 160 ? -3.819 49.506  20.451 1.00 20.61 ? 601  ARG   A CB  1 
ATOM   1298 C  CG  . ARG   A 1 160 ? -3.292 48.106  20.602 1.00 22.03 ? 601  ARG   A CG  1 
ATOM   1299 C  CD  . ARG   A 1 160 ? -4.420 47.117  20.841 1.00 24.59 ? 601  ARG   A CD  1 
ATOM   1300 N  NE  . ARG   A 1 160 ? -3.923 45.931  21.521 1.00 27.50 ? 601  ARG   A NE  1 
ATOM   1301 C  CZ  . ARG   A 1 160 ? -3.223 44.971  20.926 1.00 38.85 ? 601  ARG   A CZ  1 
ATOM   1302 N  NH1 . ARG   A 1 160 ? -2.945 45.052  19.632 1.00 41.76 ? 601  ARG   A NH1 1 
ATOM   1303 N  NH2 . ARG   A 1 160 ? -2.800 43.927  21.626 1.00 34.27 ? 601  ARG   A NH2 1 
ATOM   1304 N  N   . GLU   A 1 161 ? -2.472 51.081  22.834 1.00 20.32 ? 602  GLU   A N   1 
ATOM   1305 C  CA  . GLU   A 1 161 ? -1.701 51.214  24.065 1.00 23.87 ? 602  GLU   A CA  1 
ATOM   1306 C  C   . GLU   A 1 161 ? -1.271 49.864  24.628 1.00 22.08 ? 602  GLU   A C   1 
ATOM   1307 O  O   . GLU   A 1 161 ? -0.205 49.764  25.248 1.00 24.76 ? 602  GLU   A O   1 
ATOM   1308 C  CB  . GLU   A 1 161 ? -2.496 52.027  25.091 1.00 34.27 ? 602  GLU   A CB  1 
ATOM   1309 C  CG  . GLU   A 1 161 ? -2.502 53.534  24.829 1.00 43.54 ? 602  GLU   A CG  1 
ATOM   1310 C  CD  . GLU   A 1 161 ? -1.107 54.129  24.706 1.00 54.59 ? 602  GLU   A CD  1 
ATOM   1311 O  OE1 . GLU   A 1 161 ? -0.172 53.612  25.354 1.00 61.51 ? 602  GLU   A OE1 1 
ATOM   1312 O  OE2 . GLU   A 1 161 ? -0.946 55.120  23.962 1.00 56.60 ? 602  GLU   A OE2 1 
ATOM   1313 N  N   . SER   A 1 162 ? -2.059 48.817  24.397 1.00 21.10 ? 603  SER   A N   1 
ATOM   1314 C  CA  . SER   A 1 162 ? -1.800 47.492  24.935 1.00 23.56 ? 603  SER   A CA  1 
ATOM   1315 C  C   . SER   A 1 162 ? -1.046 46.579  23.971 1.00 19.88 ? 603  SER   A C   1 
ATOM   1316 O  O   . SER   A 1 162 ? -0.983 45.369  24.210 1.00 19.99 ? 603  SER   A O   1 
ATOM   1317 C  CB  . SER   A 1 162 ? -3.114 46.835  25.359 1.00 35.85 ? 603  SER   A CB  1 
ATOM   1318 O  OG  . SER   A 1 162 ? -3.593 47.405  26.562 1.00 48.15 ? 603  SER   A OG  1 
ATOM   1319 N  N   . LEU   A 1 163 ? -0.482 47.121  22.891 1.00 18.47 ? 604  LEU   A N   1 
ATOM   1320 C  CA  . LEU   A 1 163 ? 0.303  46.308  21.966 1.00 17.23 ? 604  LEU   A CA  1 
ATOM   1321 C  C   . LEU   A 1 163 ? 1.373  45.534  22.730 1.00 17.23 ? 604  LEU   A C   1 
ATOM   1322 O  O   . LEU   A 1 163 ? 2.115  46.101  23.535 1.00 16.90 ? 604  LEU   A O   1 
ATOM   1323 C  CB  . LEU   A 1 163 ? 0.963  47.216  20.928 1.00 18.75 ? 604  LEU   A CB  1 
ATOM   1324 C  CG  . LEU   A 1 163 ? 1.705  46.507  19.787 1.00 19.10 ? 604  LEU   A CG  1 
ATOM   1325 C  CD1 . LEU   A 1 163 ? 0.728  46.134  18.688 1.00 18.93 ? 604  LEU   A CD1 1 
ATOM   1326 C  CD2 . LEU   A 1 163 ? 2.836  47.373  19.230 1.00 20.39 ? 604  LEU   A CD2 1 
ATOM   1327 N  N   . ARG   A 1 164 ? 1.428  44.226  22.496 1.00 15.09 ? 605  ARG   A N   1 
ATOM   1328 C  CA  . ARG   A 1 164 ? 2.341  43.354  23.228 1.00 15.66 ? 605  ARG   A CA  1 
ATOM   1329 C  C   . ARG   A 1 164 ? 3.727  43.454  22.603 1.00 15.99 ? 605  ARG   A C   1 
ATOM   1330 O  O   . ARG   A 1 164 ? 3.933  43.053  21.451 1.00 16.66 ? 605  ARG   A O   1 
ATOM   1331 C  CB  . ARG   A 1 164 ? 1.827  41.918  23.222 1.00 16.22 ? 605  ARG   A CB  1 
ATOM   1332 C  CG  . ARG   A 1 164 ? 0.512  41.745  23.996 1.00 18.66 ? 605  ARG   A CG  1 
ATOM   1333 C  CD  . ARG   A 1 164 ? 0.145  40.271  24.167 1.00 19.97 ? 605  ARG   A CD  1 
ATOM   1334 N  NE  . ARG   A 1 164 ? -0.014 39.610  22.870 1.00 23.67 ? 605  ARG   A NE  1 
ATOM   1335 C  CZ  . ARG   A 1 164 ? -1.073 39.740  22.075 1.00 27.78 ? 605  ARG   A CZ  1 
ATOM   1336 N  NH1 . ARG   A 1 164 ? -2.100 40.499  22.439 1.00 26.19 ? 605  ARG   A NH1 1 
ATOM   1337 N  NH2 . ARG   A 1 164 ? -1.109 39.108  20.907 1.00 27.29 ? 605  ARG   A NH2 1 
ATOM   1338 N  N   . VAL   A 1 165 ? 4.675  43.996  23.358 1.00 14.94 ? 606  VAL   A N   1 
ATOM   1339 C  CA  . VAL   A 1 165 ? 6.056  44.147  22.910 1.00 13.40 ? 606  VAL   A CA  1 
ATOM   1340 C  C   . VAL   A 1 165 ? 6.928  43.258  23.778 1.00 13.33 ? 606  VAL   A C   1 
ATOM   1341 O  O   . VAL   A 1 165 ? 6.868  43.331  25.013 1.00 14.00 ? 606  VAL   A O   1 
ATOM   1342 C  CB  . VAL   A 1 165 ? 6.523  45.611  22.991 1.00 14.43 ? 606  VAL   A CB  1 
ATOM   1343 C  CG1 . VAL   A 1 165 ? 7.959  45.749  22.475 1.00 15.29 ? 606  VAL   A CG1 1 
ATOM   1344 C  CG2 . VAL   A 1 165 ? 5.575  46.538  22.250 1.00 15.63 ? 606  VAL   A CG2 1 
ATOM   1345 N  N   . LEU   A 1 166 ? 7.727  42.412  23.139 1.00 14.25 ? 607  LEU   A N   1 
ATOM   1346 C  CA  . LEU   A 1 166 ? 8.764  41.653  23.820 1.00 14.60 ? 607  LEU   A CA  1 
ATOM   1347 C  C   . LEU   A 1 166 ? 10.085 42.370  23.610 1.00 14.62 ? 607  LEU   A C   1 
ATOM   1348 O  O   . LEU   A 1 166 ? 10.426 42.711  22.475 1.00 14.87 ? 607  LEU   A O   1 
ATOM   1349 C  CB  . LEU   A 1 166 ? 8.870  40.239  23.248 1.00 14.85 ? 607  LEU   A CB  1 
ATOM   1350 C  CG  . LEU   A 1 166 ? 10.146 39.472  23.604 1.00 14.52 ? 607  LEU   A CG  1 
ATOM   1351 C  CD1 . LEU   A 1 166 ? 10.188 39.165  25.082 1.00 15.40 ? 607  LEU   A CD1 1 
ATOM   1352 C  CD2 . LEU   A 1 166 ? 10.177 38.186  22.812 1.00 15.72 ? 607  LEU   A CD2 1 
ATOM   1353 N  N   . ILE   A 1 167 ? 10.808 42.628  24.699 1.00 13.34 ? 608  ILE   A N   1 
ATOM   1354 C  CA  . ILE   A 1 167 ? 12.177 43.122  24.621 1.00 14.60 ? 608  ILE   A CA  1 
ATOM   1355 C  C   . ILE   A 1 167 ? 13.080 42.004  25.111 1.00 16.16 ? 608  ILE   A C   1 
ATOM   1356 O  O   . ILE   A 1 167 ? 12.976 41.578  26.271 1.00 16.36 ? 608  ILE   A O   1 
ATOM   1357 C  CB  . ILE   A 1 167 ? 12.388 44.389  25.463 1.00 13.59 ? 608  ILE   A CB  1 
ATOM   1358 C  CG1 . ILE   A 1 167 ? 11.522 45.545  24.963 1.00 13.12 ? 608  ILE   A CG1 1 
ATOM   1359 C  CG2 . ILE   A 1 167 ? 13.863 44.784  25.463 1.00 13.79 ? 608  ILE   A CG2 1 
ATOM   1360 C  CD1 . ILE   A 1 167 ? 11.615 46.798  25.796 1.00 14.08 ? 608  ILE   A CD1 1 
ATOM   1361 N  N   . VAL   A 1 168 ? 13.952 41.519  24.235 1.00 14.18 ? 609  VAL   A N   1 
ATOM   1362 C  CA  . VAL   A 1 168 ? 14.977 40.548  24.604 1.00 13.50 ? 609  VAL   A CA  1 
ATOM   1363 C  C   . VAL   A 1 168 ? 16.299 41.293  24.668 1.00 12.36 ? 609  VAL   A C   1 
ATOM   1364 O  O   . VAL   A 1 168 ? 16.709 41.914  23.682 1.00 14.49 ? 609  VAL   A O   1 
ATOM   1365 C  CB  . VAL   A 1 168 ? 15.048 39.386  23.600 1.00 14.48 ? 609  VAL   A CB  1 
ATOM   1366 C  CG1 . VAL   A 1 168 ? 16.253 38.505  23.883 1.00 15.92 ? 609  VAL   A CG1 1 
ATOM   1367 C  CG2 . VAL   A 1 168 ? 13.754 38.565  23.635 1.00 16.42 ? 609  VAL   A CG2 1 
ATOM   1368 N  N   . ASP   A 1 169 ? 16.957 41.247  25.821 1.00 14.31 ? 610  ASP   A N   1 
ATOM   1369 C  CA  . ASP   A 1 169 ? 18.153 42.042  26.088 1.00 12.55 ? 610  ASP   A CA  1 
ATOM   1370 C  C   . ASP   A 1 169 ? 19.309 41.057  26.256 1.00 13.76 ? 610  ASP   A C   1 
ATOM   1371 O  O   . ASP   A 1 169 ? 19.480 40.454  27.327 1.00 12.74 ? 610  ASP   A O   1 
ATOM   1372 C  CB  . ASP   A 1 169 ? 17.919 42.876  27.348 1.00 13.44 ? 610  ASP   A CB  1 
ATOM   1373 C  CG  . ASP   A 1 169 ? 19.039 43.863  27.629 1.00 15.69 ? 610  ASP   A CG  1 
ATOM   1374 O  OD1 . ASP   A 1 169 ? 20.195 43.582  27.255 1.00 16.45 ? 610  ASP   A OD1 1 
ATOM   1375 O  OD2 . ASP   A 1 169 ? 18.757 44.912  28.268 1.00 15.54 ? 610  ASP   A OD2 1 
ATOM   1376 N  N   . TRP   A 1 170 ? 20.105 40.890  25.200 1.00 13.69 ? 611  TRP   A N   1 
ATOM   1377 C  CA  . TRP   A 1 170 ? 21.237 39.971  25.237 1.00 13.30 ? 611  TRP   A CA  1 
ATOM   1378 C  C   . TRP   A 1 170 ? 22.584 40.669  25.400 1.00 12.16 ? 611  TRP   A C   1 
ATOM   1379 O  O   . TRP   A 1 170 ? 23.623 40.007  25.331 1.00 13.94 ? 611  TRP   A O   1 
ATOM   1380 C  CB  . TRP   A 1 170 ? 21.206 38.979  24.062 1.00 14.35 ? 611  TRP   A CB  1 
ATOM   1381 C  CG  . TRP   A 1 170 ? 21.536 39.493  22.659 1.00 12.16 ? 611  TRP   A CG  1 
ATOM   1382 C  CD1 . TRP   A 1 170 ? 22.531 40.362  22.312 1.00 12.78 ? 611  TRP   A CD1 1 
ATOM   1383 C  CD2 . TRP   A 1 170 ? 20.903 39.104  21.435 1.00 12.20 ? 611  TRP   A CD2 1 
ATOM   1384 N  NE1 . TRP   A 1 170 ? 22.543 40.555  20.952 1.00 13.17 ? 611  TRP   A NE1 1 
ATOM   1385 C  CE2 . TRP   A 1 170 ? 21.548 39.799  20.391 1.00 13.49 ? 611  TRP   A CE2 1 
ATOM   1386 C  CE3 . TRP   A 1 170 ? 19.843 38.248  21.124 1.00 15.01 ? 611  TRP   A CE3 1 
ATOM   1387 C  CZ2 . TRP   A 1 170 ? 21.176 39.657  19.055 1.00 13.90 ? 611  TRP   A CZ2 1 
ATOM   1388 C  CZ3 . TRP   A 1 170 ? 19.463 38.114  19.803 1.00 14.49 ? 611  TRP   A CZ3 1 
ATOM   1389 C  CH2 . TRP   A 1 170 ? 20.129 38.812  18.778 1.00 14.75 ? 611  TRP   A CH2 1 
ATOM   1390 N  N   . ASP   A 1 171 ? 22.590 41.986  25.606 1.00 13.35 ? 612  ASP   A N   1 
ATOM   1391 C  CA  . ASP   A 1 171 ? 23.777 42.661  26.116 1.00 12.57 ? 612  ASP   A CA  1 
ATOM   1392 C  C   . ASP   A 1 171 ? 24.245 41.936  27.372 1.00 13.22 ? 612  ASP   A C   1 
ATOM   1393 O  O   . ASP   A 1 171 ? 23.434 41.387  28.119 1.00 14.39 ? 612  ASP   A O   1 
ATOM   1394 C  CB  . ASP   A 1 171 ? 23.381 44.108  26.438 1.00 14.46 ? 612  ASP   A CB  1 
ATOM   1395 C  CG  . ASP   A 1 171 ? 24.562 44.992  26.804 1.00 13.86 ? 612  ASP   A CG  1 
ATOM   1396 O  OD1 . ASP   A 1 171 ? 25.051 44.881  27.950 1.00 14.73 ? 612  ASP   A OD1 1 
ATOM   1397 O  OD2 . ASP   A 1 171 ? 24.965 45.837  25.968 1.00 17.82 ? 612  ASP   A OD2 1 
ATOM   1398 N  N   . VAL   A 1 172 ? 25.563 41.898  27.593 1.00 13.38 ? 613  VAL   A N   1 
ATOM   1399 C  CA  . VAL   A 1 172 ? 26.100 41.139  28.730 1.00 15.18 ? 613  VAL   A CA  1 
ATOM   1400 C  C   . VAL   A 1 172 ? 25.686 41.740  30.070 1.00 15.72 ? 613  VAL   A C   1 
ATOM   1401 O  O   . VAL   A 1 172 ? 25.779 41.066  31.115 1.00 15.54 ? 613  VAL   A O   1 
ATOM   1402 C  CB  . VAL   A 1 172 ? 27.632 40.992  28.644 1.00 13.88 ? 613  VAL   A CB  1 
ATOM   1403 C  CG1 . VAL   A 1 172 ? 28.313 42.257  29.137 1.00 13.69 ? 613  VAL   A CG1 1 
ATOM   1404 C  CG2 . VAL   A 1 172 ? 28.113 39.772  29.447 1.00 14.49 ? 613  VAL   A CG2 1 
ATOM   1405 N  N   . HIS   A 1 173 ? 25.255 42.992  30.076 1.00 14.75 ? 614  HIS   A N   1 
ATOM   1406 C  CA  . HIS   A 1 173 ? 24.852 43.666  31.303 1.00 24.83 ? 614  HIS   A CA  1 
ATOM   1407 C  C   . HIS   A 1 173 ? 23.335 43.660  31.437 1.00 16.78 ? 614  HIS   A C   1 
ATOM   1408 O  O   . HIS   A 1 173 ? 22.603 43.646  30.444 1.00 14.44 ? 614  HIS   A O   1 
ATOM   1409 C  CB  . HIS   A 1 173 ? 25.350 45.112  31.302 1.00 43.43 ? 614  HIS   A CB  1 
ATOM   1410 C  CG  . HIS   A 1 173 ? 26.835 45.238  31.169 1.00 33.80 ? 614  HIS   A CG  1 
ATOM   1411 N  ND1 . HIS   A 1 173 ? 27.452 45.545  29.974 1.00 19.07 ? 614  HIS   A ND1 1 
ATOM   1412 C  CD2 . HIS   A 1 173 ? 27.826 45.099  32.082 1.00 24.67 ? 614  HIS   A CD2 1 
ATOM   1413 C  CE1 . HIS   A 1 173 ? 28.762 45.595  30.162 1.00 19.73 ? 614  HIS   A CE1 1 
ATOM   1414 N  NE2 . HIS   A 1 173 ? 29.015 45.322  31.429 1.00 19.14 ? 614  HIS   A NE2 1 
ATOM   1415 N  N   . HIS   A 1 174 ? 22.867 43.673  32.682 1.00 13.69 ? 615  HIS   A N   1 
ATOM   1416 C  CA  . HIS   A 1 174 ? 21.442 43.799  32.943 1.00 13.65 ? 615  HIS   A CA  1 
ATOM   1417 C  C   . HIS   A 1 174 ? 20.951 45.184  32.535 1.00 13.48 ? 615  HIS   A C   1 
ATOM   1418 O  O   . HIS   A 1 174 ? 21.559 46.200  32.895 1.00 14.24 ? 615  HIS   A O   1 
ATOM   1419 C  CB  . HIS   A 1 174 ? 21.170 43.598  34.433 1.00 14.59 ? 615  HIS   A CB  1 
ATOM   1420 C  CG  . HIS   A 1 174 ? 19.714 43.597  34.781 1.00 13.72 ? 615  HIS   A CG  1 
ATOM   1421 N  ND1 . HIS   A 1 174 ? 19.169 44.450  35.720 1.00 15.39 ? 615  HIS   A ND1 1 
ATOM   1422 C  CD2 . HIS   A 1 174 ? 18.688 42.853  34.308 1.00 14.67 ? 615  HIS   A CD2 1 
ATOM   1423 C  CE1 . HIS   A 1 174 ? 17.873 44.221  35.820 1.00 13.41 ? 615  HIS   A CE1 1 
ATOM   1424 N  NE2 . HIS   A 1 174 ? 17.552 43.254  34.975 1.00 15.08 ? 615  HIS   A NE2 1 
ATOM   1425 N  N   . GLY   A 1 175 ? 19.833 45.224  31.804 1.00 12.88 ? 616  GLY   A N   1 
ATOM   1426 C  CA  . GLY   A 1 175 ? 19.215 46.485  31.442 1.00 14.05 ? 616  GLY   A CA  1 
ATOM   1427 C  C   . GLY   A 1 175 ? 18.362 47.022  32.570 1.00 14.25 ? 616  GLY   A C   1 
ATOM   1428 O  O   . GLY   A 1 175 ? 17.131 46.917  32.530 1.00 14.37 ? 616  GLY   A O   1 
ATOM   1429 N  N   . ASN   A 1 176 ? 19.016 47.599  33.581 1.00 14.45 ? 617  ASN   A N   1 
ATOM   1430 C  CA  . ASN   A 1 176 ? 18.302 48.016  34.787 1.00 14.99 ? 617  ASN   A CA  1 
ATOM   1431 C  C   . ASN   A 1 176 ? 17.213 49.027  34.463 1.00 15.90 ? 617  ASN   A C   1 
ATOM   1432 O  O   . ASN   A 1 176 ? 16.130 48.997  35.063 1.00 15.93 ? 617  ASN   A O   1 
ATOM   1433 C  CB  . ASN   A 1 176 ? 19.277 48.613  35.799 1.00 14.04 ? 617  ASN   A CB  1 
ATOM   1434 C  CG  . ASN   A 1 176 ? 20.126 49.700  35.197 1.00 15.36 ? 617  ASN   A CG  1 
ATOM   1435 O  OD1 . ASN   A 1 176 ? 21.048 49.412  34.446 1.00 15.68 ? 617  ASN   A OD1 1 
ATOM   1436 N  ND2 . ASN   A 1 176 ? 19.820 50.951  35.504 1.00 19.07 ? 617  ASN   A ND2 1 
ATOM   1437 N  N   . GLY   A 1 177 ? 17.485 49.942  33.536 1.00 12.71 ? 618  GLY   A N   1 
ATOM   1438 C  CA  . GLY   A 1 177 ? 16.491 50.949  33.220 1.00 14.27 ? 618  GLY   A CA  1 
ATOM   1439 C  C   . GLY   A 1 177 ? 15.281 50.347  32.544 1.00 13.82 ? 618  GLY   A C   1 
ATOM   1440 O  O   . GLY   A 1 177 ? 14.139 50.712  32.846 1.00 14.31 ? 618  GLY   A O   1 
ATOM   1441 N  N   . THR   A 1 178 ? 15.510 49.407  31.622 1.00 13.16 ? 619  THR   A N   1 
ATOM   1442 C  CA  . THR   A 1 178 ? 14.384 48.773  30.947 1.00 12.18 ? 619  THR   A CA  1 
ATOM   1443 C  C   . THR   A 1 178 ? 13.538 47.973  31.926 1.00 13.38 ? 619  THR   A C   1 
ATOM   1444 O  O   . THR   A 1 178 ? 12.300 48.056  31.903 1.00 13.67 ? 619  THR   A O   1 
ATOM   1445 C  CB  . THR   A 1 178 ? 14.876 47.878  29.814 1.00 11.82 ? 619  THR   A CB  1 
ATOM   1446 O  OG1 . THR   A 1 178 ? 15.828 48.607  29.034 1.00 14.47 ? 619  THR   A OG1 1 
ATOM   1447 C  CG2 . THR   A 1 178 ? 13.727 47.488  28.923 1.00 13.66 ? 619  THR   A CG2 1 
ATOM   1448 N  N   . GLN   A 1 179 ? 14.181 47.185  32.788 1.00 14.35 ? 620  GLN   A N   1 
ATOM   1449 C  CA  . GLN   A 1 179 ? 13.431 46.472  33.818 1.00 12.95 ? 620  GLN   A CA  1 
ATOM   1450 C  C   . GLN   A 1 179 ? 12.577 47.433  34.634 1.00 12.40 ? 620  GLN   A C   1 
ATOM   1451 O  O   . GLN   A 1 179 ? 11.375 47.205  34.827 1.00 12.91 ? 620  GLN   A O   1 
ATOM   1452 C  CB  . GLN   A 1 179 ? 14.376 45.687  34.728 1.00 13.76 ? 620  GLN   A CB  1 
ATOM   1453 C  CG  . GLN   A 1 179 ? 13.696 45.233  36.020 1.00 16.35 ? 620  GLN   A CG  1 
ATOM   1454 C  CD  . GLN   A 1 179 ? 14.491 44.196  36.776 1.00 17.37 ? 620  GLN   A CD  1 
ATOM   1455 O  OE1 . GLN   A 1 179 ? 15.048 43.276  36.181 1.00 17.39 ? 620  GLN   A OE1 1 
ATOM   1456 N  NE2 . GLN   A 1 179 ? 14.547 44.332  38.100 1.00 18.08 ? 620  GLN   A NE2 1 
ATOM   1457 N  N   . HIS   A 1 180 ? 13.174 48.525  35.108 1.00 13.11 ? 621  HIS   A N   1 
ATOM   1458 C  CA  . HIS   A 1 180 ? 12.449 49.413  36.014 1.00 14.39 ? 621  HIS   A CA  1 
ATOM   1459 C  C   . HIS   A 1 180 ? 11.309 50.126  35.301 1.00 14.86 ? 621  HIS   A C   1 
ATOM   1460 O  O   . HIS   A 1 180 ? 10.215 50.263  35.855 1.00 16.01 ? 621  HIS   A O   1 
ATOM   1461 C  CB  . HIS   A 1 180 ? 13.414 50.400  36.655 1.00 16.92 ? 621  HIS   A CB  1 
ATOM   1462 C  CG  . HIS   A 1 180 ? 14.345 49.760  37.630 1.00 20.29 ? 621  HIS   A CG  1 
ATOM   1463 N  ND1 . HIS   A 1 180 ? 15.643 50.185  37.815 1.00 18.65 ? 621  HIS   A ND1 1 
ATOM   1464 C  CD2 . HIS   A 1 180 ? 14.169 48.708  38.464 1.00 22.60 ? 621  HIS   A CD2 1 
ATOM   1465 C  CE1 . HIS   A 1 180 ? 16.225 49.424  38.725 1.00 19.73 ? 621  HIS   A CE1 1 
ATOM   1466 N  NE2 . HIS   A 1 180 ? 15.352 48.521  39.134 1.00 21.92 ? 621  HIS   A NE2 1 
ATOM   1467 N  N   . ILE   A 1 181 ? 11.536 50.557  34.061 1.00 12.23 ? 622  ILE   A N   1 
ATOM   1468 C  CA  . ILE   A 1 181 ? 10.497 51.266  33.317 1.00 13.28 ? 622  ILE   A CA  1 
ATOM   1469 C  C   . ILE   A 1 181 ? 9.262  50.390  33.144 1.00 14.02 ? 622  ILE   A C   1 
ATOM   1470 O  O   . ILE   A 1 181 ? 8.122  50.865  33.253 1.00 15.23 ? 622  ILE   A O   1 
ATOM   1471 C  CB  . ILE   A 1 181 ? 11.054 51.770  31.969 1.00 12.38 ? 622  ILE   A CB  1 
ATOM   1472 C  CG1 . ILE   A 1 181 ? 12.000 52.944  32.206 1.00 14.42 ? 622  ILE   A CG1 1 
ATOM   1473 C  CG2 . ILE   A 1 181 ? 9.907  52.164  31.032 1.00 14.69 ? 622  ILE   A CG2 1 
ATOM   1474 C  CD1 . ILE   A 1 181 ? 12.859 53.320  31.007 1.00 15.02 ? 622  ILE   A CD1 1 
ATOM   1475 N  N   . PHE   A 1 182 ? 9.452  49.100  32.904 1.00 15.24 ? 623  PHE   A N   1 
ATOM   1476 C  CA  . PHE   A 1 182 ? 8.325  48.217  32.634 1.00 14.35 ? 623  PHE   A CA  1 
ATOM   1477 C  C   . PHE   A 1 182 ? 7.984  47.283  33.791 1.00 13.66 ? 623  PHE   A C   1 
ATOM   1478 O  O   . PHE   A 1 182 ? 7.172  46.373  33.613 1.00 15.32 ? 623  PHE   A O   1 
ATOM   1479 C  CB  . PHE   A 1 182 ? 8.589  47.427  31.354 1.00 12.80 ? 623  PHE   A CB  1 
ATOM   1480 C  CG  . PHE   A 1 182 ? 8.761  48.297  30.137 1.00 13.18 ? 623  PHE   A CG  1 
ATOM   1481 C  CD1 . PHE   A 1 182 ? 7.712  49.073  29.665 1.00 14.22 ? 623  PHE   A CD1 1 
ATOM   1482 C  CD2 . PHE   A 1 182 ? 9.976  48.344  29.466 1.00 12.16 ? 623  PHE   A CD2 1 
ATOM   1483 C  CE1 . PHE   A 1 182 ? 7.870  49.875  28.550 1.00 13.81 ? 623  PHE   A CE1 1 
ATOM   1484 C  CE2 . PHE   A 1 182 ? 10.129 49.137  28.344 1.00 14.21 ? 623  PHE   A CE2 1 
ATOM   1485 C  CZ  . PHE   A 1 182 ? 9.086  49.908  27.893 1.00 14.47 ? 623  PHE   A CZ  1 
ATOM   1486 N  N   . GLU   A 1 183 ? 8.569  47.486  34.973 1.00 14.51 ? 624  GLU   A N   1 
ATOM   1487 C  CA  . GLU   A 1 183 ? 8.437  46.491  36.037 1.00 17.33 ? 624  GLU   A CA  1 
ATOM   1488 C  C   . GLU   A 1 183 ? 6.988  46.247  36.437 1.00 15.32 ? 624  GLU   A C   1 
ATOM   1489 O  O   . GLU   A 1 183 ? 6.629  45.116  36.780 1.00 15.61 ? 624  GLU   A O   1 
ATOM   1490 C  CB  . GLU   A 1 183 ? 9.268  46.889  37.257 1.00 20.92 ? 624  GLU   A CB  1 
ATOM   1491 C  CG  . GLU   A 1 183 ? 9.607  45.706  38.147 1.00 23.47 ? 624  GLU   A CG  1 
ATOM   1492 C  CD  . GLU   A 1 183 ? 10.766 45.989  39.086 1.00 25.55 ? 624  GLU   A CD  1 
ATOM   1493 O  OE1 . GLU   A 1 183 ? 11.145 47.170  39.225 1.00 27.76 ? 624  GLU   A OE1 1 
ATOM   1494 O  OE2 . GLU   A 1 183 ? 11.282 45.032  39.706 1.00 27.50 ? 624  GLU   A OE2 1 
ATOM   1495 N  N   . GLU   A 1 184 ? 6.141  47.270  36.364 1.00 16.18 ? 625  GLU   A N   1 
ATOM   1496 C  CA  . GLU   A 1 184 ? 4.728  47.145  36.701 1.00 17.40 ? 625  GLU   A CA  1 
ATOM   1497 C  C   . GLU   A 1 184 ? 3.842  47.062  35.467 1.00 17.55 ? 625  GLU   A C   1 
ATOM   1498 O  O   . GLU   A 1 184 ? 2.664  47.440  35.525 1.00 19.79 ? 625  GLU   A O   1 
ATOM   1499 C  CB  . GLU   A 1 184 ? 4.283  48.311  37.585 1.00 18.89 ? 625  GLU   A CB  1 
ATOM   1500 C  CG  . GLU   A 1 184 ? 4.887  48.331  38.975 1.00 26.59 ? 625  GLU   A CG  1 
ATOM   1501 C  CD  . GLU   A 1 184 ? 4.564  49.612  39.720 1.00 39.17 ? 625  GLU   A CD  1 
ATOM   1502 O  OE1 . GLU   A 1 184 ? 4.631  50.694  39.101 1.00 49.60 ? 625  GLU   A OE1 1 
ATOM   1503 O  OE2 . GLU   A 1 184 ? 4.229  49.537  40.920 1.00 36.32 ? 625  GLU   A OE2 1 
ATOM   1504 N  N   . ASP   A 1 185 ? 4.378  46.571  34.347 1.00 17.34 ? 626  ASP   A N   1 
ATOM   1505 C  CA  . ASP   A 1 185 ? 3.667  46.557  33.077 1.00 17.45 ? 626  ASP   A CA  1 
ATOM   1506 C  C   . ASP   A 1 185 ? 3.602  45.143  32.524 1.00 18.34 ? 626  ASP   A C   1 
ATOM   1507 O  O   . ASP   A 1 185 ? 4.629  44.469  32.408 1.00 22.85 ? 626  ASP   A O   1 
ATOM   1508 C  CB  . ASP   A 1 185 ? 4.360  47.474  32.065 1.00 20.49 ? 626  ASP   A CB  1 
ATOM   1509 C  CG  . ASP   A 1 185 ? 3.421  47.952  30.971 1.00 22.35 ? 626  ASP   A CG  1 
ATOM   1510 O  OD1 . ASP   A 1 185 ? 2.427  47.255  30.677 0.76 22.12 ? 626  ASP   A OD1 1 
ATOM   1511 O  OD2 . ASP   A 1 185 ? 3.674  49.038  30.420 0.70 24.99 ? 626  ASP   A OD2 1 
ATOM   1512 N  N   . ASP   A 1 186 ? 2.400  44.713  32.149 1.00 19.87 ? 627  ASP   A N   1 
ATOM   1513 C  CA  . ASP   A 1 186 ? 2.195  43.434  31.487 1.00 21.50 ? 627  ASP   A CA  1 
ATOM   1514 C  C   . ASP   A 1 186 ? 2.150  43.543  29.965 1.00 21.46 ? 627  ASP   A C   1 
ATOM   1515 O  O   . ASP   A 1 186 ? 2.093  42.510  29.292 1.00 25.09 ? 627  ASP   A O   1 
ATOM   1516 C  CB  . ASP   A 1 186 ? 0.923  42.741  32.009 1.00 26.27 ? 627  ASP   A CB  1 
ATOM   1517 C  CG  . ASP   A 1 186 ? -0.331 43.560  31.782 1.00 39.95 ? 627  ASP   A CG  1 
ATOM   1518 O  OD1 . ASP   A 1 186 ? -0.227 44.782  31.562 1.00 33.21 ? 627  ASP   A OD1 1 
ATOM   1519 O  OD2 . ASP   A 1 186 ? -1.434 42.980  31.832 1.00 49.51 ? 627  ASP   A OD2 1 
ATOM   1520 N  N   . SER   A 1 187 ? 2.162  44.759  29.406 1.00 17.66 ? 628  SER   A N   1 
ATOM   1521 C  CA  . SER   A 1 187 ? 2.136  44.917  27.951 1.00 16.80 ? 628  SER   A CA  1 
ATOM   1522 C  C   . SER   A 1 187 ? 3.515  44.786  27.317 1.00 18.30 ? 628  SER   A C   1 
ATOM   1523 O  O   . SER   A 1 187 ? 3.611  44.602  26.091 1.00 16.58 ? 628  SER   A O   1 
ATOM   1524 C  CB  . SER   A 1 187 ? 1.512  46.260  27.552 1.00 17.14 ? 628  SER   A CB  1 
ATOM   1525 O  OG  . SER   A 1 187 ? 2.367  47.348  27.871 1.00 17.93 ? 628  SER   A OG  1 
ATOM   1526 N  N   . VAL   A 1 188 ? 4.574  44.879  28.120 1.00 16.14 ? 629  VAL   A N   1 
ATOM   1527 C  CA  . VAL   A 1 188 ? 5.958  44.808  27.654 1.00 15.08 ? 629  VAL   A CA  1 
ATOM   1528 C  C   . VAL   A 1 188 ? 6.641  43.729  28.476 1.00 22.33 ? 629  VAL   A C   1 
ATOM   1529 O  O   . VAL   A 1 188 ? 6.879  43.916  29.675 1.00 27.96 ? 629  VAL   A O   1 
ATOM   1530 C  CB  . VAL   A 1 188 ? 6.691  46.146  27.807 1.00 14.45 ? 629  VAL   A CB  1 
ATOM   1531 C  CG1 . VAL   A 1 188 ? 8.132  46.029  27.300 1.00 15.69 ? 629  VAL   A CG1 1 
ATOM   1532 C  CG2 . VAL   A 1 188 ? 5.955  47.237  27.050 1.00 16.25 ? 629  VAL   A CG2 1 
ATOM   1533 N  N   . LEU   A 1 189 ? 6.937  42.599  27.849 1.00 17.22 ? 630  LEU   A N   1 
ATOM   1534 C  CA  . LEU   A 1 189 ? 7.658  41.513  28.496 1.00 14.95 ? 630  LEU   A CA  1 
ATOM   1535 C  C   . LEU   A 1 189 ? 9.150  41.767  28.323 1.00 15.28 ? 630  LEU   A C   1 
ATOM   1536 O  O   . LEU   A 1 189 ? 9.636  41.893  27.190 1.00 15.26 ? 630  LEU   A O   1 
ATOM   1537 C  CB  . LEU   A 1 189 ? 7.280  40.193  27.833 1.00 15.15 ? 630  LEU   A CB  1 
ATOM   1538 C  CG  . LEU   A 1 189 ? 8.071  38.936  28.165 1.00 17.55 ? 630  LEU   A CG  1 
ATOM   1539 C  CD1 . LEU   A 1 189 ? 7.925  38.598  29.645 1.00 18.83 ? 630  LEU   A CD1 1 
ATOM   1540 C  CD2 . LEU   A 1 189 ? 7.604  37.781  27.289 1.00 16.43 ? 630  LEU   A CD2 1 
ATOM   1541 N  N   . TYR   A 1 190 ? 9.868  41.859  29.435 1.00 13.61 ? 631  TYR   A N   1 
ATOM   1542 C  CA  . TYR   A 1 190 ? 11.303 42.111  29.429 1.00 14.34 ? 631  TYR   A CA  1 
ATOM   1543 C  C   . TYR   A 1 190 ? 12.018 40.822  29.798 1.00 14.64 ? 631  TYR   A C   1 
ATOM   1544 O  O   . TYR   A 1 190 ? 11.762 40.249  30.861 1.00 16.55 ? 631  TYR   A O   1 
ATOM   1545 C  CB  . TYR   A 1 190 ? 11.673 43.225  30.414 1.00 14.32 ? 631  TYR   A CB  1 
ATOM   1546 C  CG  . TYR   A 1 190 ? 13.150 43.510  30.441 1.00 14.04 ? 631  TYR   A CG  1 
ATOM   1547 C  CD1 . TYR   A 1 190 ? 13.805 43.970  29.309 1.00 13.17 ? 631  TYR   A CD1 1 
ATOM   1548 C  CD2 . TYR   A 1 190 ? 13.895 43.297  31.589 1.00 13.94 ? 631  TYR   A CD2 1 
ATOM   1549 C  CE1 . TYR   A 1 190 ? 15.181 44.213  29.322 1.00 12.76 ? 631  TYR   A CE1 1 
ATOM   1550 C  CE2 . TYR   A 1 190 ? 15.257 43.534  31.619 1.00 14.50 ? 631  TYR   A CE2 1 
ATOM   1551 C  CZ  . TYR   A 1 190 ? 15.899 43.997  30.481 1.00 14.76 ? 631  TYR   A CZ  1 
ATOM   1552 O  OH  . TYR   A 1 190 ? 17.256 44.230  30.539 1.00 15.44 ? 631  TYR   A OH  1 
ATOM   1553 N  N   . ILE   A 1 191 ? 12.899 40.361  28.915 1.00 14.43 ? 632  ILE   A N   1 
ATOM   1554 C  CA  . ILE   A 1 191 ? 13.729 39.182  29.148 1.00 13.89 ? 632  ILE   A CA  1 
ATOM   1555 C  C   . ILE   A 1 191 ? 15.179 39.597  28.959 1.00 15.20 ? 632  ILE   A C   1 
ATOM   1556 O  O   . ILE   A 1 191 ? 15.572 39.987  27.850 1.00 16.03 ? 632  ILE   A O   1 
ATOM   1557 C  CB  . ILE   A 1 191 ? 13.383 38.037  28.185 1.00 15.58 ? 632  ILE   A CB  1 
ATOM   1558 C  CG1 . ILE   A 1 191 ? 11.897 37.698  28.241 1.00 13.74 ? 632  ILE   A CG1 1 
ATOM   1559 C  CG2 . ILE   A 1 191 ? 14.229 36.805  28.503 1.00 16.53 ? 632  ILE   A CG2 1 
ATOM   1560 C  CD1 . ILE   A 1 191 ? 11.545 36.470  27.435 1.00 15.48 ? 632  ILE   A CD1 1 
ATOM   1561 N  N   . SER   A 1 192 ? 15.974 39.497  30.018 1.00 14.33 ? 633  SER   A N   1 
ATOM   1562 C  CA  . SER   A 1 192 ? 17.390 39.837  29.974 1.00 13.44 ? 633  SER   A CA  1 
ATOM   1563 C  C   . SER   A 1 192 ? 18.214 38.615  30.338 1.00 15.10 ? 633  SER   A C   1 
ATOM   1564 O  O   . SER   A 1 192 ? 17.906 37.925  31.318 1.00 15.37 ? 633  SER   A O   1 
ATOM   1565 C  CB  . SER   A 1 192 ? 17.710 40.969  30.948 1.00 14.10 ? 633  SER   A CB  1 
ATOM   1566 O  OG  . SER   A 1 192 ? 19.089 41.311  30.914 1.00 15.08 ? 633  SER   A OG  1 
ATOM   1567 N  N   . LEU   A 1 193 ? 19.271 38.366  29.567 1.00 14.39 ? 634  LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 193 ? 20.352 37.472  29.950 1.00 13.71 ? 634  LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 193 ? 21.549 38.348  30.264 1.00 16.19 ? 634  LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 193 ? 21.812 39.314  29.542 1.00 16.74 ? 634  LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 193 ? 20.691 36.507  28.803 1.00 15.44 ? 634  LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 193 ? 19.491 35.825  28.127 1.00 17.73 ? 634  LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 193 ? 19.054 36.537  26.851 1.00 18.17 ? 634  LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 193 ? 19.797 34.360  27.852 1.00 19.86 ? 634  LEU   A CD2 1 
ATOM   1575 N  N   . HIS   A 1 194 ? 22.258 38.044  31.351 1.00 13.94 ? 635  HIS   A N   1 
ATOM   1576 C  CA  . HIS   A 1 194 ? 23.344 38.938  31.734 1.00 16.67 ? 635  HIS   A CA  1 
ATOM   1577 C  C   . HIS   A 1 194 ? 24.293 38.260  32.705 1.00 17.54 ? 635  HIS   A C   1 
ATOM   1578 O  O   . HIS   A 1 194 ? 23.887 37.436  33.531 1.00 17.72 ? 635  HIS   A O   1 
ATOM   1579 C  CB  . HIS   A 1 194 ? 22.796 40.214  32.382 1.00 15.97 ? 635  HIS   A CB  1 
ATOM   1580 C  CG  . HIS   A 1 194 ? 21.677 39.951  33.334 1.00 14.01 ? 635  HIS   A CG  1 
ATOM   1581 N  ND1 . HIS   A 1 194 ? 20.364 39.876  32.925 1.00 15.32 ? 635  HIS   A ND1 1 
ATOM   1582 C  CD2 . HIS   A 1 194 ? 21.675 39.701  34.667 1.00 16.18 ? 635  HIS   A CD2 1 
ATOM   1583 C  CE1 . HIS   A 1 194 ? 19.595 39.612  33.967 1.00 16.27 ? 635  HIS   A CE1 1 
ATOM   1584 N  NE2 . HIS   A 1 194 ? 20.366 39.506  35.036 1.00 16.97 ? 635  HIS   A NE2 1 
ATOM   1585 N  N   . ARG   A 1 195 ? 25.559 38.650  32.618 1.00 16.36 ? 636  ARG   A N   1 
ATOM   1586 C  CA  . ARG   A 1 195 ? 26.511 38.278  33.646 1.00 16.36 ? 636  ARG   A CA  1 
ATOM   1587 C  C   . ARG   A 1 195 ? 26.106 38.973  34.937 1.00 16.79 ? 636  ARG   A C   1 
ATOM   1588 O  O   . ARG   A 1 195 ? 25.906 40.193  34.964 1.00 17.67 ? 636  ARG   A O   1 
ATOM   1589 C  CB  . ARG   A 1 195 ? 27.915 38.703  33.233 1.00 15.82 ? 636  ARG   A CB  1 
ATOM   1590 C  CG  . ARG   A 1 195 ? 28.974 38.122  34.142 1.00 15.51 ? 636  ARG   A CG  1 
ATOM   1591 C  CD  . ARG   A 1 195 ? 30.342 38.207  33.511 1.00 17.00 ? 636  ARG   A CD  1 
ATOM   1592 N  NE  . ARG   A 1 195 ? 31.356 37.678  34.412 1.00 18.76 ? 636  ARG   A NE  1 
ATOM   1593 C  CZ  . ARG   A 1 195 ? 32.659 37.853  34.243 1.00 19.95 ? 636  ARG   A CZ  1 
ATOM   1594 N  NH1 . ARG   A 1 195 ? 33.108 38.538  33.197 1.00 21.30 ? 636  ARG   A NH1 1 
ATOM   1595 N  NH2 . ARG   A 1 195 ? 33.518 37.338  35.118 1.00 21.60 ? 636  ARG   A NH2 1 
ATOM   1596 N  N   . TYR   A 1 196 ? 25.980 38.190  36.003 1.00 16.46 ? 637  TYR   A N   1 
ATOM   1597 C  CA  . TYR   A 1 196 ? 25.467 38.666  37.282 1.00 17.63 ? 637  TYR   A CA  1 
ATOM   1598 C  C   . TYR   A 1 196 ? 26.494 38.556  38.399 1.00 19.78 ? 637  TYR   A C   1 
ATOM   1599 O  O   . TYR   A 1 196 ? 26.734 39.540  39.110 1.00 21.38 ? 637  TYR   A O   1 
ATOM   1600 C  CB  . TYR   A 1 196 ? 24.199 37.879  37.631 1.00 19.79 ? 637  TYR   A CB  1 
ATOM   1601 C  CG  . TYR   A 1 196 ? 23.549 38.268  38.940 1.00 20.22 ? 637  TYR   A CG  1 
ATOM   1602 C  CD1 . TYR   A 1 196 ? 23.137 39.577  39.173 1.00 23.84 ? 637  TYR   A CD1 1 
ATOM   1603 C  CD2 . TYR   A 1 196 ? 23.320 37.320  39.925 1.00 20.02 ? 637  TYR   A CD2 1 
ATOM   1604 C  CE1 . TYR   A 1 196 ? 22.531 39.937  40.366 1.00 22.51 ? 637  TYR   A CE1 1 
ATOM   1605 C  CE2 . TYR   A 1 196 ? 22.710 37.670  41.122 1.00 21.30 ? 637  TYR   A CE2 1 
ATOM   1606 C  CZ  . TYR   A 1 196 ? 22.321 38.978  41.333 1.00 22.34 ? 637  TYR   A CZ  1 
ATOM   1607 O  OH  . TYR   A 1 196 ? 21.725 39.330  42.526 1.00 23.71 ? 637  TYR   A OH  1 
ATOM   1608 N  N   . GLU   A 1 197 ? 27.132 37.395  38.551 1.00 21.23 ? 638  GLU   A N   1 
ATOM   1609 C  CA  . GLU   A 1 197 ? 28.148 37.162  39.584 1.00 21.44 ? 638  GLU   A CA  1 
ATOM   1610 C  C   . GLU   A 1 197 ? 27.646 37.540  40.980 1.00 21.17 ? 638  GLU   A C   1 
ATOM   1611 O  O   . GLU   A 1 197 ? 28.289 38.287  41.716 1.00 22.65 ? 638  GLU   A O   1 
ATOM   1612 C  CB  . GLU   A 1 197 ? 29.471 37.857  39.258 1.00 21.35 ? 638  GLU   A CB  1 
ATOM   1613 C  CG  . GLU   A 1 197 ? 29.995 37.621  37.834 1.00 25.20 ? 638  GLU   A CG  1 
ATOM   1614 C  CD  . GLU   A 1 197 ? 30.360 36.169  37.543 1.00 29.94 ? 638  GLU   A CD  1 
ATOM   1615 O  OE1 . GLU   A 1 197 ? 30.310 35.320  38.459 1.00 29.78 ? 638  GLU   A OE1 1 
ATOM   1616 O  OE2 . GLU   A 1 197 ? 30.710 35.875  36.380 1.00 31.19 ? 638  GLU   A OE2 1 
ATOM   1617 N  N   . ASP   A 1 198 ? 26.462 37.031  41.321 1.00 25.24 ? 639  ASP   A N   1 
ATOM   1618 C  CA  . ASP   A 1 198 ? 25.862 37.246  42.639 1.00 30.09 ? 639  ASP   A CA  1 
ATOM   1619 C  C   . ASP   A 1 198 ? 25.736 38.729  42.980 1.00 32.98 ? 639  ASP   A C   1 
ATOM   1620 O  O   . ASP   A 1 198 ? 25.818 39.120  44.149 1.00 30.52 ? 639  ASP   A O   1 
ATOM   1621 C  CB  . ASP   A 1 198 ? 26.612 36.477  43.731 1.00 37.57 ? 639  ASP   A CB  1 
ATOM   1622 C  CG  . ASP   A 1 198 ? 26.495 34.971  43.565 1.00 46.12 ? 639  ASP   A CG  1 
ATOM   1623 O  OD1 . ASP   A 1 198 ? 25.447 34.507  43.066 1.00 46.95 ? 639  ASP   A OD1 1 
ATOM   1624 O  OD2 . ASP   A 1 198 ? 27.453 34.253  43.926 1.00 53.37 ? 639  ASP   A OD2 1 
ATOM   1625 N  N   . GLY   A 1 199 ? 25.546 39.568  41.962 1.00 28.43 ? 640  GLY   A N   1 
ATOM   1626 C  CA  . GLY   A 1 199 ? 25.380 40.992  42.156 1.00 23.56 ? 640  GLY   A CA  1 
ATOM   1627 C  C   . GLY   A 1 199 ? 26.639 41.823  42.049 1.00 23.87 ? 640  GLY   A C   1 
ATOM   1628 O  O   . GLY   A 1 199 ? 26.564 43.049  42.211 1.00 25.38 ? 640  GLY   A O   1 
ATOM   1629 N  N   . ALA   A 1 200 ? 27.790 41.211  41.773 1.00 26.89 ? 641  ALA   A N   1 
ATOM   1630 C  CA  . ALA   A 1 200 ? 29.057 41.930  41.732 1.00 28.87 ? 641  ALA   A CA  1 
ATOM   1631 C  C   . ALA   A 1 200 ? 29.401 42.504  40.359 1.00 29.63 ? 641  ALA   A C   1 
ATOM   1632 O  O   . ALA   A 1 200 ? 30.358 43.280  40.257 1.00 33.52 ? 641  ALA   A O   1 
ATOM   1633 C  CB  . ALA   A 1 200 ? 30.198 41.022  42.204 1.00 27.42 ? 641  ALA   A CB  1 
ATOM   1634 N  N   . PHE   A 1 201 ? 28.661 42.150  39.310 1.00 23.42 ? 642  PHE   A N   1 
ATOM   1635 C  CA  . PHE   A 1 201 ? 28.944 42.649  37.969 1.00 22.04 ? 642  PHE   A CA  1 
ATOM   1636 C  C   . PHE   A 1 201 ? 28.093 43.879  37.681 1.00 19.69 ? 642  PHE   A C   1 
ATOM   1637 O  O   . PHE   A 1 201 ? 26.924 43.938  38.078 1.00 19.80 ? 642  PHE   A O   1 
ATOM   1638 C  CB  . PHE   A 1 201 ? 28.650 41.565  36.928 1.00 19.41 ? 642  PHE   A CB  1 
ATOM   1639 C  CG  . PHE   A 1 201 ? 29.420 41.727  35.643 1.00 20.51 ? 642  PHE   A CG  1 
ATOM   1640 C  CD1 . PHE   A 1 201 ? 30.787 41.490  35.598 1.00 19.26 ? 642  PHE   A CD1 1 
ATOM   1641 C  CD2 . PHE   A 1 201 ? 28.772 42.112  34.481 1.00 19.06 ? 642  PHE   A CD2 1 
ATOM   1642 C  CE1 . PHE   A 1 201 ? 31.497 41.633  34.409 1.00 21.29 ? 642  PHE   A CE1 1 
ATOM   1643 C  CE2 . PHE   A 1 201 ? 29.472 42.256  33.295 1.00 21.18 ? 642  PHE   A CE2 1 
ATOM   1644 C  CZ  . PHE   A 1 201 ? 30.832 42.018  33.259 1.00 21.92 ? 642  PHE   A CZ  1 
ATOM   1645 N  N   . PHE   A 1 202 ? 28.690 44.861  37.000 1.00 18.56 ? 643  PHE   A N   1 
ATOM   1646 C  CA  . PHE   A 1 202 ? 27.957 46.067  36.629 1.00 18.55 ? 643  PHE   A CA  1 
ATOM   1647 C  C   . PHE   A 1 202 ? 26.616 45.687  36.005 1.00 16.85 ? 643  PHE   A C   1 
ATOM   1648 O  O   . PHE   A 1 202 ? 26.573 44.802  35.140 1.00 15.67 ? 643  PHE   A O   1 
ATOM   1649 C  CB  . PHE   A 1 202 ? 28.754 46.892  35.616 1.00 18.94 ? 643  PHE   A CB  1 
ATOM   1650 C  CG  . PHE   A 1 202 ? 28.150 48.234  35.347 1.00 18.72 ? 643  PHE   A CG  1 
ATOM   1651 C  CD1 . PHE   A 1 202 ? 27.195 48.405  34.352 1.00 18.21 ? 643  PHE   A CD1 1 
ATOM   1652 C  CD2 . PHE   A 1 202 ? 28.504 49.327  36.124 1.00 20.25 ? 643  PHE   A CD2 1 
ATOM   1653 C  CE1 . PHE   A 1 202 ? 26.625 49.639  34.143 1.00 15.99 ? 643  PHE   A CE1 1 
ATOM   1654 C  CE2 . PHE   A 1 202 ? 27.938 50.563  35.902 1.00 17.86 ? 643  PHE   A CE2 1 
ATOM   1655 C  CZ  . PHE   A 1 202 ? 26.999 50.720  34.915 1.00 17.61 ? 643  PHE   A CZ  1 
ATOM   1656 N  N   . PRO   A 1 203 ? 25.503 46.362  36.376 1.00 17.07 ? 644  PRO   A N   1 
ATOM   1657 C  CA  . PRO   A 1 203 ? 25.429 47.566  37.215 1.00 16.96 ? 644  PRO   A CA  1 
ATOM   1658 C  C   . PRO   A 1 203 ? 25.329 47.307  38.733 1.00 18.83 ? 644  PRO   A C   1 
ATOM   1659 O  O   . PRO   A 1 203 ? 24.879 48.200  39.458 1.00 20.38 ? 644  PRO   A O   1 
ATOM   1660 C  CB  . PRO   A 1 203 ? 24.167 48.270  36.696 1.00 18.03 ? 644  PRO   A CB  1 
ATOM   1661 C  CG  . PRO   A 1 203 ? 23.287 47.169  36.281 1.00 18.02 ? 644  PRO   A CG  1 
ATOM   1662 C  CD  . PRO   A 1 203 ? 24.191 46.057  35.771 1.00 17.46 ? 644  PRO   A CD  1 
ATOM   1663 N  N   . ASN   A 1 204 ? 25.730 46.119  39.200 1.00 16.98 ? 645  ASN   A N   1 
ATOM   1664 C  CA  . ASN   A 1 204 ? 26.024 45.883  40.622 1.00 19.98 ? 645  ASN   A CA  1 
ATOM   1665 C  C   . ASN   A 1 204 ? 24.784 45.955  41.512 1.00 20.87 ? 645  ASN   A C   1 
ATOM   1666 O  O   . ASN   A 1 204 ? 24.852 46.435  42.650 1.00 22.29 ? 645  ASN   A O   1 
ATOM   1667 C  CB  . ASN   A 1 204 ? 27.118 46.816  41.138 1.00 21.08 ? 645  ASN   A CB  1 
ATOM   1668 C  CG  . ASN   A 1 204 ? 28.360 46.766  40.296 1.00 26.40 ? 645  ASN   A CG  1 
ATOM   1669 O  OD1 . ASN   A 1 204 ? 28.648 47.699  39.553 1.00 30.20 ? 645  ASN   A OD1 1 
ATOM   1670 N  ND2 . ASN   A 1 204 ? 29.112 45.676  40.407 1.00 27.82 ? 645  ASN   A ND2 1 
ATOM   1671 N  N   . SER   A 1 205 ? 23.655 45.458  41.016 1.00 19.80 ? 646  SER   A N   1 
ATOM   1672 C  CA  . SER   A 1 205 ? 22.409 45.464  41.771 1.00 19.60 ? 646  SER   A CA  1 
ATOM   1673 C  C   . SER   A 1 205 ? 21.786 44.077  41.786 1.00 19.50 ? 646  SER   A C   1 
ATOM   1674 O  O   . SER   A 1 205 ? 21.746 43.392  40.760 1.00 18.73 ? 646  SER   A O   1 
ATOM   1675 C  CB  . SER   A 1 205 ? 21.398 46.452  41.175 1.00 19.93 ? 646  SER   A CB  1 
ATOM   1676 O  OG  . SER   A 1 205 ? 20.163 46.389  41.874 1.00 19.65 ? 646  SER   A OG  1 
ATOM   1677 N  N   . GLU   A 1 206 ? 21.257 43.680  42.949 1.00 17.52 ? 647  GLU   A N   1 
ATOM   1678 C  CA  . GLU   A 1 206 ? 20.490 42.445  43.005 1.00 15.25 ? 647  GLU   A CA  1 
ATOM   1679 C  C   . GLU   A 1 206 ? 19.157 42.541  42.269 1.00 15.35 ? 647  GLU   A C   1 
ATOM   1680 O  O   . GLU   A 1 206 ? 18.445 41.536  42.177 1.00 18.80 ? 647  GLU   A O   1 
ATOM   1681 C  CB  . GLU   A 1 206 ? 20.314 41.985  44.455 1.00 17.52 ? 647  GLU   A CB  1 
ATOM   1682 C  CG  . GLU   A 1 206 ? 21.650 41.686  45.107 1.00 22.73 ? 647  GLU   A CG  1 
ATOM   1683 C  CD  . GLU   A 1 206 ? 21.526 41.033  46.470 1.00 26.96 ? 647  GLU   A CD  1 
ATOM   1684 O  OE1 . GLU   A 1 206 ? 20.468 40.443  46.759 1.00 35.56 ? 647  GLU   A OE1 1 
ATOM   1685 O  OE2 . GLU   A 1 206 ? 22.503 41.102  47.234 1.00 28.11 ? 647  GLU   A OE2 1 
ATOM   1686 N  N   . ASP   A 1 207 ? 18.807 43.712  41.719 1.00 17.28 ? 648  ASP   A N   1 
ATOM   1687 C  CA  . ASP   A 1 207 ? 17.617 43.810  40.877 1.00 18.28 ? 648  ASP   A CA  1 
ATOM   1688 C  C   . ASP   A 1 207 ? 17.700 42.886  39.671 1.00 15.99 ? 648  ASP   A C   1 
ATOM   1689 O  O   . ASP   A 1 207 ? 16.668 42.569  39.071 1.00 17.64 ? 648  ASP   A O   1 
ATOM   1690 C  CB  . ASP   A 1 207 ? 17.457 45.239  40.357 1.00 23.68 ? 648  ASP   A CB  1 
ATOM   1691 C  CG  . ASP   A 1 207 ? 17.137 46.226  41.451 1.00 28.47 ? 648  ASP   A CG  1 
ATOM   1692 O  OD1 . ASP   A 1 207 ? 16.964 45.795  42.615 1.00 28.56 ? 648  ASP   A OD1 1 
ATOM   1693 O  OD2 . ASP   A 1 207 ? 17.065 47.434  41.138 1.00 29.85 ? 648  ASP   A OD2 1 
ATOM   1694 N  N   . ALA   A 1 208 ? 18.905 42.455  39.313 1.00 17.58 ? 649  ALA   A N   1 
ATOM   1695 C  CA  . ALA   A 1 208 ? 19.136 41.607  38.152 1.00 18.60 ? 649  ALA   A CA  1 
ATOM   1696 C  C   . ALA   A 1 208 ? 18.964 40.120  38.447 1.00 20.05 ? 649  ALA   A C   1 
ATOM   1697 O  O   . ALA   A 1 208 ? 19.132 39.302  37.534 1.00 19.44 ? 649  ALA   A O   1 
ATOM   1698 C  CB  . ALA   A 1 208 ? 20.534 41.865  37.581 1.00 15.78 ? 649  ALA   A CB  1 
ATOM   1699 N  N   . ASN   A 1 209 ? 18.619 39.740  39.681 1.00 19.13 ? 650  ASN   A N   1 
ATOM   1700 C  CA  . ASN   A 1 209 ? 18.531 38.318  39.977 1.00 17.33 ? 650  ASN   A CA  1 
ATOM   1701 C  C   . ASN   A 1 209 ? 17.229 37.724  39.438 1.00 16.72 ? 650  ASN   A C   1 
ATOM   1702 O  O   . ASN   A 1 209 ? 16.273 38.431  39.106 1.00 17.52 ? 650  ASN   A O   1 
ATOM   1703 C  CB  . ASN   A 1 209 ? 18.654 38.057  41.480 1.00 18.85 ? 650  ASN   A CB  1 
ATOM   1704 C  CG  . ASN   A 1 209 ? 19.360 36.748  41.785 1.00 23.53 ? 650  ASN   A CG  1 
ATOM   1705 O  OD1 . ASN   A 1 209 ? 19.677 35.970  40.883 1.00 23.14 ? 650  ASN   A OD1 1 
ATOM   1706 N  ND2 . ASN   A 1 209 ? 19.609 36.495  43.065 1.00 25.77 ? 650  ASN   A ND2 1 
ATOM   1707 N  N   . TYR   A 1 210 ? 17.192 36.388  39.383 1.00 16.86 ? 651  TYR   A N   1 
ATOM   1708 C  CA  . TYR   A 1 210 ? 16.083 35.676  38.764 1.00 18.54 ? 651  TYR   A CA  1 
ATOM   1709 C  C   . TYR   A 1 210 ? 14.788 35.818  39.551 1.00 17.28 ? 651  TYR   A C   1 
ATOM   1710 O  O   . TYR   A 1 210 ? 13.709 35.573  38.999 1.00 19.99 ? 651  TYR   A O   1 
ATOM   1711 C  CB  . TYR   A 1 210 ? 16.420 34.190  38.591 1.00 20.10 ? 651  TYR   A CB  1 
ATOM   1712 C  CG  . TYR   A 1 210 ? 16.730 33.487  39.902 1.00 24.05 ? 651  TYR   A CG  1 
ATOM   1713 C  CD1 . TYR   A 1 210 ? 15.712 32.954  40.694 1.00 25.11 ? 651  TYR   A CD1 1 
ATOM   1714 C  CD2 . TYR   A 1 210 ? 18.039 33.357  40.345 1.00 24.36 ? 651  TYR   A CD2 1 
ATOM   1715 C  CE1 . TYR   A 1 210 ? 15.998 32.320  41.898 1.00 26.95 ? 651  TYR   A CE1 1 
ATOM   1716 C  CE2 . TYR   A 1 210 ? 18.334 32.724  41.542 1.00 22.83 ? 651  TYR   A CE2 1 
ATOM   1717 C  CZ  . TYR   A 1 210 ? 17.308 32.212  42.314 1.00 27.01 ? 651  TYR   A CZ  1 
ATOM   1718 O  OH  . TYR   A 1 210 ? 17.606 31.584  43.505 1.00 29.85 ? 651  TYR   A OH  1 
ATOM   1719 N  N   . ASP   A 1 211 ? 14.878 36.175  40.829 1.00 20.17 ? 652  ASP   A N   1 
ATOM   1720 C  CA  . ASP   A 1 211 ? 13.685 36.277  41.659 1.00 23.48 ? 652  ASP   A CA  1 
ATOM   1721 C  C   . ASP   A 1 211 ? 12.913 37.566  41.433 1.00 22.68 ? 652  ASP   A C   1 
ATOM   1722 O  O   . ASP   A 1 211 ? 11.838 37.737  42.017 1.00 24.54 ? 652  ASP   A O   1 
ATOM   1723 C  CB  . ASP   A 1 211 ? 14.028 36.096  43.146 1.00 31.32 ? 652  ASP   A CB  1 
ATOM   1724 C  CG  . ASP   A 1 211 ? 14.932 37.188  43.681 1.00 34.34 ? 652  ASP   A CG  1 
ATOM   1725 O  OD1 . ASP   A 1 211 ? 15.613 37.855  42.878 1.00 31.31 ? 652  ASP   A OD1 1 
ATOM   1726 O  OD2 . ASP   A 1 211 ? 14.970 37.374  44.920 1.00 36.13 ? 652  ASP   A OD2 1 
ATOM   1727 N  N   . LYS   A 1 212 ? 13.420 38.473  40.601 1.00 19.54 ? 653  LYS   A N   1 
ATOM   1728 C  CA  . LYS   A 1 212 ? 12.700 39.698  40.270 1.00 18.58 ? 653  LYS   A CA  1 
ATOM   1729 C  C   . LYS   A 1 212 ? 11.836 39.385  39.056 1.00 18.51 ? 653  LYS   A C   1 
ATOM   1730 O  O   . LYS   A 1 212 ? 12.309 39.397  37.916 1.00 19.23 ? 653  LYS   A O   1 
ATOM   1731 C  CB  . LYS   A 1 212 ? 13.669 40.846  40.017 1.00 17.42 ? 653  LYS   A CB  1 
ATOM   1732 C  CG  . LYS   A 1 212 ? 14.724 41.030  41.107 1.00 21.42 ? 653  LYS   A CG  1 
ATOM   1733 C  CD  . LYS   A 1 212 ? 14.133 41.097  42.510 1.00 23.83 ? 653  LYS   A CD  1 
ATOM   1734 C  CE  . LYS   A 1 212 ? 15.203 41.502  43.520 1.00 23.64 ? 653  LYS   A CE  1 
ATOM   1735 N  NZ  . LYS   A 1 212 ? 16.219 40.436  43.775 1.00 22.74 ? 653  LYS   A NZ  1 
ATOM   1736 N  N   . VAL   A 1 213 ? 10.559 39.090  39.303 1.00 16.13 ? 654  VAL   A N   1 
ATOM   1737 C  CA  . VAL   A 1 213 ? 9.647  38.595  38.284 1.00 20.64 ? 654  VAL   A CA  1 
ATOM   1738 C  C   . VAL   A 1 213 ? 8.665  39.656  37.810 1.00 18.94 ? 654  VAL   A C   1 
ATOM   1739 O  O   . VAL   A 1 213 ? 7.824  39.371  36.945 1.00 19.64 ? 654  VAL   A O   1 
ATOM   1740 C  CB  . VAL   A 1 213 ? 8.917  37.327  38.777 1.00 18.42 ? 654  VAL   A CB  1 
ATOM   1741 C  CG1 . VAL   A 1 213 ? 9.931  36.266  39.162 1.00 17.61 ? 654  VAL   A CG1 1 
ATOM   1742 C  CG2 . VAL   A 1 213 ? 7.984  37.655  39.954 1.00 19.08 ? 654  VAL   A CG2 1 
ATOM   1743 N  N   . GLY   A 1 214 ? 8.758  40.869  38.338 1.00 17.31 ? 655  GLY   A N   1 
ATOM   1744 C  CA  . GLY   A 1 214 ? 7.817  41.932  38.062 1.00 17.32 ? 655  GLY   A CA  1 
ATOM   1745 C  C   . GLY   A 1 214 ? 6.942  42.237  39.269 1.00 20.51 ? 655  GLY   A C   1 
ATOM   1746 O  O   . GLY   A 1 214 ? 6.880  41.488  40.246 1.00 21.21 ? 655  GLY   A O   1 
ATOM   1747 N  N   . LEU   A 1 215 ? 6.261  43.373  39.178 1.00 19.49 ? 656  LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 215 ? 5.443  43.884  40.270 1.00 17.50 ? 656  LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 215 ? 4.053  44.232  39.764 1.00 18.43 ? 656  LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 215 ? 3.876  44.614  38.605 1.00 17.43 ? 656  LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 215 ? 6.061  45.152  40.840 1.00 18.12 ? 656  LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 215 ? 7.448  45.022  41.463 1.00 20.05 ? 656  LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 215 ? 8.042  46.402  41.645 1.00 20.24 ? 656  LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 215 ? 7.357  44.290  42.784 1.00 20.59 ? 656  LEU   A CD2 1 
ATOM   1755 N  N   . GLY   A 1 216 ? 3.066  44.117  40.661 1.00 16.34 ? 657  GLY   A N   1 
ATOM   1756 C  CA  . GLY   A 1 216 ? 1.706  44.504  40.314 1.00 16.63 ? 657  GLY   A CA  1 
ATOM   1757 C  C   . GLY   A 1 216 ? 1.199  43.708  39.131 1.00 17.07 ? 657  GLY   A C   1 
ATOM   1758 O  O   . GLY   A 1 216 ? 1.373  42.484  39.058 1.00 19.10 ? 657  GLY   A O   1 
ATOM   1759 N  N   . LYS   A 1 217 ? 0.589  44.404  38.170 1.00 18.87 ? 658  LYS   A N   1 
ATOM   1760 C  CA  . LYS   A 1 217 ? 0.110  43.713  36.978 1.00 26.40 ? 658  LYS   A CA  1 
ATOM   1761 C  C   . LYS   A 1 217 ? 1.247  43.147  36.138 1.00 26.85 ? 658  LYS   A C   1 
ATOM   1762 O  O   . LYS   A 1 217 ? 0.996  42.295  35.280 1.00 25.24 ? 658  LYS   A O   1 
ATOM   1763 C  CB  . LYS   A 1 217 ? -0.794 44.619  36.138 1.00 37.54 ? 658  LYS   A CB  1 
ATOM   1764 C  CG  . LYS   A 1 217 ? -0.070 45.695  35.352 1.00 53.78 ? 658  LYS   A CG  1 
ATOM   1765 C  CD  . LYS   A 1 217 ? -1.042 46.473  34.481 1.00 67.64 ? 658  LYS   A CD  1 
ATOM   1766 C  CE  . LYS   A 1 217 ? -0.321 47.496  33.624 1.00 65.95 ? 658  LYS   A CE  1 
ATOM   1767 N  NZ  . LYS   A 1 217 ? 0.281  48.575  34.451 1.00 57.97 ? 658  LYS   A NZ  1 
ATOM   1768 N  N   . GLY   A 1 218 ? 2.482  43.571  36.388 1.00 22.97 ? 659  GLY   A N   1 
ATOM   1769 C  CA  . GLY   A 1 218 ? 3.637  43.056  35.691 1.00 20.35 ? 659  GLY   A CA  1 
ATOM   1770 C  C   . GLY   A 1 218 ? 4.224  41.779  36.249 1.00 21.12 ? 659  GLY   A C   1 
ATOM   1771 O  O   . GLY   A 1 218 ? 5.271  41.343  35.768 1.00 20.31 ? 659  GLY   A O   1 
ATOM   1772 N  N   A ARG   A 1 219 ? 3.608  41.169  37.264 0.84 21.93 ? 660  ARG   A N   1 
ATOM   1773 N  N   B ARG   A 1 219 ? 3.581  41.158  37.234 0.16 20.73 ? 660  ARG   A N   1 
ATOM   1774 C  CA  A ARG   A 1 219 ? 4.165  39.947  37.830 0.84 22.98 ? 660  ARG   A CA  1 
ATOM   1775 C  CA  B ARG   A 1 219 ? 4.101  39.923  37.808 0.16 20.47 ? 660  ARG   A CA  1 
ATOM   1776 C  C   A ARG   A 1 219 ? 4.168  38.839  36.785 0.84 21.97 ? 660  ARG   A C   1 
ATOM   1777 C  C   B ARG   A 1 219 ? 4.160  38.834  36.747 0.16 21.98 ? 660  ARG   A C   1 
ATOM   1778 O  O   A ARG   A 1 219 ? 3.127  38.513  36.207 0.84 21.72 ? 660  ARG   A O   1 
ATOM   1779 O  O   B ARG   A 1 219 ? 3.146  38.508  36.121 0.16 21.02 ? 660  ARG   A O   1 
ATOM   1780 C  CB  A ARG   A 1 219 ? 3.361  39.521  39.055 0.84 26.11 ? 660  ARG   A CB  1 
ATOM   1781 C  CB  B ARG   A 1 219 ? 3.202  39.488  38.961 0.16 19.51 ? 660  ARG   A CB  1 
ATOM   1782 C  CG  A ARG   A 1 219 ? 3.517  40.449  40.235 0.84 27.26 ? 660  ARG   A CG  1 
ATOM   1783 C  CG  B ARG   A 1 219 ? 3.498  40.210  40.252 0.16 19.39 ? 660  ARG   A CG  1 
ATOM   1784 C  CD  A ARG   A 1 219 ? 2.880  39.849  41.481 0.84 26.06 ? 660  ARG   A CD  1 
ATOM   1785 C  CD  B ARG   A 1 219 ? 4.574  39.486  41.030 0.16 19.05 ? 660  ARG   A CD  1 
ATOM   1786 N  NE  A ARG   A 1 219 ? 3.656  38.732  42.012 0.84 22.22 ? 660  ARG   A NE  1 
ATOM   1787 N  NE  B ARG   A 1 219 ? 4.151  39.199  42.394 0.16 19.25 ? 660  ARG   A NE  1 
ATOM   1788 C  CZ  A ARG   A 1 219 ? 3.214  37.482  42.097 0.84 19.37 ? 660  ARG   A CZ  1 
ATOM   1789 C  CZ  B ARG   A 1 219 ? 4.930  38.642  43.314 0.16 16.96 ? 660  ARG   A CZ  1 
ATOM   1790 N  NH1 A ARG   A 1 219 ? 1.997  37.172  41.676 0.84 17.99 ? 660  ARG   A NH1 1 
ATOM   1791 N  NH1 B ARG   A 1 219 ? 6.179  38.306  43.015 0.16 16.25 ? 660  ARG   A NH1 1 
ATOM   1792 N  NH2 A ARG   A 1 219 ? 3.996  36.541  42.608 0.84 18.14 ? 660  ARG   A NH2 1 
ATOM   1793 N  NH2 B ARG   A 1 219 ? 4.458  38.419  44.531 0.16 19.08 ? 660  ARG   A NH2 1 
ATOM   1794 N  N   . GLY   A 1 220 ? 5.351  38.272  36.544 1.00 22.99 ? 661  GLY   A N   1 
ATOM   1795 C  CA  . GLY   A 1 220 ? 5.572  37.294  35.501 1.00 26.95 ? 661  GLY   A CA  1 
ATOM   1796 C  C   . GLY   A 1 220 ? 6.101  37.872  34.204 1.00 26.29 ? 661  GLY   A C   1 
ATOM   1797 O  O   . GLY   A 1 220 ? 6.544  37.109  33.338 1.00 21.61 ? 661  GLY   A O   1 
ATOM   1798 N  N   . TYR   A 1 221 ? 6.082  39.195  34.048 1.00 21.81 ? 662  TYR   A N   1 
ATOM   1799 C  CA  . TYR   A 1 221 ? 6.474  39.838  32.799 1.00 17.24 ? 662  TYR   A CA  1 
ATOM   1800 C  C   . TYR   A 1 221 ? 7.878  40.431  32.850 1.00 18.57 ? 662  TYR   A C   1 
ATOM   1801 O  O   . TYR   A 1 221 ? 8.233  41.241  31.980 1.00 15.79 ? 662  TYR   A O   1 
ATOM   1802 C  CB  . TYR   A 1 221 ? 5.427  40.870  32.391 1.00 18.09 ? 662  TYR   A CB  1 
ATOM   1803 C  CG  . TYR   A 1 221 ? 4.105  40.227  32.054 1.00 20.75 ? 662  TYR   A CG  1 
ATOM   1804 C  CD1 . TYR   A 1 221 ? 3.169  39.963  33.043 1.00 23.80 ? 662  TYR   A CD1 1 
ATOM   1805 C  CD2 . TYR   A 1 221 ? 3.805  39.855  30.751 1.00 20.72 ? 662  TYR   A CD2 1 
ATOM   1806 C  CE1 . TYR   A 1 221 ? 1.964  39.366  32.741 1.00 27.78 ? 662  TYR   A CE1 1 
ATOM   1807 C  CE2 . TYR   A 1 221 ? 2.595  39.257  30.436 1.00 23.91 ? 662  TYR   A CE2 1 
ATOM   1808 C  CZ  . TYR   A 1 221 ? 1.682  39.015  31.439 1.00 28.01 ? 662  TYR   A CZ  1 
ATOM   1809 O  OH  . TYR   A 1 221 ? 0.480  38.419  31.140 1.00 30.72 ? 662  TYR   A OH  1 
ATOM   1810 N  N   . ASN   A 1 222 ? 8.676  40.044  33.847 1.00 16.65 ? 663  ASN   A N   1 
ATOM   1811 C  CA  . ASN   A 1 222 ? 10.091 40.390  33.926 1.00 17.41 ? 663  ASN   A CA  1 
ATOM   1812 C  C   . ASN   A 1 222 ? 10.859 39.096  34.156 1.00 18.43 ? 663  ASN   A C   1 
ATOM   1813 O  O   . ASN   A 1 222 ? 10.668 38.433  35.183 1.00 18.19 ? 663  ASN   A O   1 
ATOM   1814 C  CB  . ASN   A 1 222 ? 10.359 41.382  35.057 1.00 16.96 ? 663  ASN   A CB  1 
ATOM   1815 C  CG  . ASN   A 1 222 ? 11.724 42.011  34.952 1.00 16.89 ? 663  ASN   A CG  1 
ATOM   1816 O  OD1 . ASN   A 1 222 ? 11.923 42.966  34.194 1.00 15.71 ? 663  ASN   A OD1 1 
ATOM   1817 N  ND2 . ASN   A 1 222 ? 12.680 41.483  35.704 1.00 16.25 ? 663  ASN   A ND2 1 
ATOM   1818 N  N   . VAL   A 1 223 ? 11.713 38.734  33.198 1.00 15.42 ? 664  VAL   A N   1 
ATOM   1819 C  CA  . VAL   A 1 223 ? 12.464 37.480  33.224 1.00 16.20 ? 664  VAL   A CA  1 
ATOM   1820 C  C   . VAL   A 1 223 ? 13.949 37.809  33.201 1.00 16.42 ? 664  VAL   A C   1 
ATOM   1821 O  O   . VAL   A 1 223 ? 14.488 38.189  32.152 1.00 16.06 ? 664  VAL   A O   1 
ATOM   1822 C  CB  . VAL   A 1 223 ? 12.096 36.566  32.046 1.00 16.04 ? 664  VAL   A CB  1 
ATOM   1823 C  CG1 . VAL   A 1 223 ? 12.889 35.269  32.112 1.00 16.35 ? 664  VAL   A CG1 1 
ATOM   1824 C  CG2 . VAL   A 1 223 ? 10.588 36.285  32.019 1.00 17.44 ? 664  VAL   A CG2 1 
ATOM   1825 N  N   . ASN   A 1 224 ? 14.621 37.639  34.335 1.00 16.36 ? 665  ASN   A N   1 
ATOM   1826 C  CA  . ASN   A 1 224 ? 16.065 37.816  34.437 1.00 17.14 ? 665  ASN   A CA  1 
ATOM   1827 C  C   . ASN   A 1 224 ? 16.735 36.450  34.416 1.00 16.88 ? 665  ASN   A C   1 
ATOM   1828 O  O   . ASN   A 1 224 ? 16.405 35.578  35.231 1.00 17.57 ? 665  ASN   A O   1 
ATOM   1829 C  CB  . ASN   A 1 224 ? 16.436 38.503  35.751 1.00 17.34 ? 665  ASN   A CB  1 
ATOM   1830 C  CG  . ASN   A 1 224 ? 16.187 39.995  35.728 1.00 16.31 ? 665  ASN   A CG  1 
ATOM   1831 O  OD1 . ASN   A 1 224 ? 16.256 40.630  34.683 1.00 16.65 ? 665  ASN   A OD1 1 
ATOM   1832 N  ND2 . ASN   A 1 224 ? 15.898 40.564  36.900 1.00 17.29 ? 665  ASN   A ND2 1 
ATOM   1833 N  N   . ILE   A 1 225 ? 17.700 36.285  33.517 1.00 16.96 ? 666  ILE   A N   1 
ATOM   1834 C  CA  . ILE   A 1 225 ? 18.490 35.063  33.417 1.00 16.82 ? 666  ILE   A CA  1 
ATOM   1835 C  C   . ILE   A 1 225 ? 19.922 35.425  33.788 1.00 18.50 ? 666  ILE   A C   1 
ATOM   1836 O  O   . ILE   A 1 225 ? 20.696 35.877  32.929 1.00 19.46 ? 666  ILE   A O   1 
ATOM   1837 C  CB  . ILE   A 1 225 ? 18.395 34.437  32.017 1.00 17.29 ? 666  ILE   A CB  1 
ATOM   1838 C  CG1 . ILE   A 1 225 ? 16.923 34.214  31.641 1.00 18.76 ? 666  ILE   A CG1 1 
ATOM   1839 C  CG2 . ILE   A 1 225 ? 19.225 33.155  31.973 1.00 17.16 ? 666  ILE   A CG2 1 
ATOM   1840 C  CD1 . ILE   A 1 225 ? 16.684 33.720  30.232 1.00 17.80 ? 666  ILE   A CD1 1 
ATOM   1841 N  N   . PRO   A 1 226 ? 20.303 35.271  35.056 1.00 19.37 ? 667  PRO   A N   1 
ATOM   1842 C  CA  . PRO   A 1 226 ? 21.612 35.729  35.525 1.00 18.36 ? 667  PRO   A CA  1 
ATOM   1843 C  C   . PRO   A 1 226 ? 22.635 34.607  35.523 1.00 18.12 ? 667  PRO   A C   1 
ATOM   1844 O  O   . PRO   A 1 226 ? 22.365 33.490  35.974 1.00 20.80 ? 667  PRO   A O   1 
ATOM   1845 C  CB  . PRO   A 1 226 ? 21.311 36.144  36.973 1.00 18.27 ? 667  PRO   A CB  1 
ATOM   1846 C  CG  . PRO   A 1 226 ? 20.115 35.340  37.374 1.00 20.73 ? 667  PRO   A CG  1 
ATOM   1847 C  CD  . PRO   A 1 226 ? 19.457 34.776  36.152 1.00 19.28 ? 667  PRO   A CD  1 
ATOM   1848 N  N   . TRP   A 1 227 ? 23.826 34.921  35.010 1.00 17.79 ? 668  TRP   A N   1 
ATOM   1849 C  CA  . TRP   A 1 227 ? 24.925 33.971  34.921 1.00 17.88 ? 668  TRP   A CA  1 
ATOM   1850 C  C   . TRP   A 1 227 ? 25.934 34.226  36.029 1.00 19.03 ? 668  TRP   A C   1 
ATOM   1851 O  O   . TRP   A 1 227 ? 26.350 35.369  36.259 1.00 18.96 ? 668  TRP   A O   1 
ATOM   1852 C  CB  . TRP   A 1 227 ? 25.656 34.088  33.579 1.00 18.28 ? 668  TRP   A CB  1 
ATOM   1853 C  CG  . TRP   A 1 227 ? 24.833 33.917  32.344 1.00 17.04 ? 668  TRP   A CG  1 
ATOM   1854 C  CD1 . TRP   A 1 227 ? 24.695 34.822  31.329 1.00 18.99 ? 668  TRP   A CD1 1 
ATOM   1855 C  CD2 . TRP   A 1 227 ? 24.048 32.774  31.973 1.00 16.84 ? 668  TRP   A CD2 1 
ATOM   1856 N  NE1 . TRP   A 1 227 ? 23.881 34.313  30.351 1.00 18.52 ? 668  TRP   A NE1 1 
ATOM   1857 C  CE2 . TRP   A 1 227 ? 23.464 33.060  30.719 1.00 17.99 ? 668  TRP   A CE2 1 
ATOM   1858 C  CE3 . TRP   A 1 227 ? 23.785 31.539  32.574 1.00 17.82 ? 668  TRP   A CE3 1 
ATOM   1859 C  CZ2 . TRP   A 1 227 ? 22.629 32.160  30.057 1.00 20.02 ? 668  TRP   A CZ2 1 
ATOM   1860 C  CZ3 . TRP   A 1 227 ? 22.953 30.640  31.912 1.00 19.98 ? 668  TRP   A CZ3 1 
ATOM   1861 C  CH2 . TRP   A 1 227 ? 22.387 30.957  30.665 1.00 19.48 ? 668  TRP   A CH2 1 
ATOM   1862 N  N   . ASN   A 1 228 ? 26.361 33.145  36.685 1.00 21.24 ? 669  ASN   A N   1 
ATOM   1863 C  CA  . ASN   A 1 228 ? 27.352 33.213  37.746 1.00 23.46 ? 669  ASN   A CA  1 
ATOM   1864 C  C   . ASN   A 1 228 ? 28.460 32.205  37.489 1.00 23.62 ? 669  ASN   A C   1 
ATOM   1865 O  O   . ASN   A 1 228 ? 28.201 31.089  37.029 1.00 26.02 ? 669  ASN   A O   1 
ATOM   1866 C  CB  . ASN   A 1 228 ? 26.722 32.883  39.097 1.00 23.31 ? 669  ASN   A CB  1 
ATOM   1867 C  CG  . ASN   A 1 228 ? 25.554 33.780  39.419 1.00 21.90 ? 669  ASN   A CG  1 
ATOM   1868 O  OD1 . ASN   A 1 228 ? 25.725 34.984  39.575 1.00 26.12 ? 669  ASN   A OD1 1 
ATOM   1869 N  ND2 . ASN   A 1 228 ? 24.359 33.202  39.517 1.00 19.97 ? 669  ASN   A ND2 1 
ATOM   1870 N  N   . GLY   A 1 229 ? 29.686 32.612  37.797 1.00 23.74 ? 670  GLY   A N   1 
ATOM   1871 C  CA  . GLY   A 1 229 ? 30.819 31.712  37.880 1.00 27.98 ? 670  GLY   A CA  1 
ATOM   1872 C  C   . GLY   A 1 229 ? 31.081 30.904  36.631 1.00 32.91 ? 670  GLY   A C   1 
ATOM   1873 O  O   . GLY   A 1 229 ? 30.974 29.674  36.651 1.00 40.87 ? 670  GLY   A O   1 
ATOM   1874 N  N   . GLY   A 1 230 ? 31.421 31.573  35.535 1.00 34.14 ? 671  GLY   A N   1 
ATOM   1875 C  CA  . GLY   A 1 230 ? 31.693 30.852  34.307 1.00 34.31 ? 671  GLY   A CA  1 
ATOM   1876 C  C   . GLY   A 1 230 ? 31.752 31.716  33.065 1.00 30.56 ? 671  GLY   A C   1 
ATOM   1877 O  O   . GLY   A 1 230 ? 31.017 32.703  32.938 1.00 31.49 ? 671  GLY   A O   1 
ATOM   1878 N  N   . LYS   A 1 231 ? 32.642 31.344  32.145 1.00 27.05 ? 672  LYS   A N   1 
ATOM   1879 C  CA  . LYS   A 1 231 ? 32.793 32.015  30.857 1.00 25.50 ? 672  LYS   A CA  1 
ATOM   1880 C  C   . LYS   A 1 231 ? 31.713 31.461  29.945 1.00 22.89 ? 672  LYS   A C   1 
ATOM   1881 O  O   . LYS   A 1 231 ? 31.926 30.497  29.204 0.72 25.48 ? 672  LYS   A O   1 
ATOM   1882 C  CB  . LYS   A 1 231 ? 34.171 31.730  30.273 1.00 32.78 ? 672  LYS   A CB  1 
ATOM   1883 C  CG  . LYS   A 1 231 ? 35.312 32.484  30.926 1.00 37.40 ? 672  LYS   A CG  1 
ATOM   1884 C  CD  . LYS   A 1 231 ? 36.628 31.705  30.816 1.00 42.46 ? 672  LYS   A CD  1 
ATOM   1885 C  CE  . LYS   A 1 231 ? 37.527 32.244  29.703 1.00 44.11 ? 672  LYS   A CE  1 
ATOM   1886 N  NZ  . LYS   A 1 231 ? 38.980 31.996  29.967 1.00 44.57 ? 672  LYS   A NZ  1 
ATOM   1887 N  N   . MET   A 1 232 ? 30.538 32.081  29.984 1.00 20.23 ? 673  MET   A N   1 
ATOM   1888 C  CA  . MET   A 1 232 ? 29.429 31.560  29.207 1.00 19.93 ? 673  MET   A CA  1 
ATOM   1889 C  C   . MET   A 1 232 ? 29.624 31.869  27.723 1.00 20.92 ? 673  MET   A C   1 
ATOM   1890 O  O   . MET   A 1 232 ? 30.339 32.802  27.336 1.00 20.58 ? 673  MET   A O   1 
ATOM   1891 C  CB  . MET   A 1 232 ? 28.108 32.145  29.700 1.00 20.11 ? 673  MET   A CB  1 
ATOM   1892 C  CG  . MET   A 1 232 ? 27.873 31.989  31.206 1.00 22.62 ? 673  MET   A CG  1 
ATOM   1893 S  SD  . MET   A 1 232 ? 28.293 30.352  31.870 1.00 22.12 ? 673  MET   A SD  1 
ATOM   1894 C  CE  . MET   A 1 232 ? 27.684 30.469  33.547 1.00 24.78 ? 673  MET   A CE  1 
ATOM   1895 N  N   . GLY   A 1 233 ? 28.983 31.066  26.897 1.00 18.90 ? 674  GLY   A N   1 
ATOM   1896 C  CA  . GLY   A 1 233 ? 29.079 31.212  25.457 1.00 16.66 ? 674  GLY   A CA  1 
ATOM   1897 C  C   . GLY   A 1 233 ? 27.875 30.596  24.800 1.00 17.32 ? 674  GLY   A C   1 
ATOM   1898 O  O   . GLY   A 1 233 ? 26.804 30.490  25.403 1.00 17.42 ? 674  GLY   A O   1 
ATOM   1899 N  N   . ASP   A 1 234 ? 28.055 30.178  23.547 1.00 18.84 ? 675  ASP   A N   1 
ATOM   1900 C  CA  . ASP   A 1 234 ? 26.949 29.641  22.755 1.00 19.01 ? 675  ASP   A CA  1 
ATOM   1901 C  C   . ASP   A 1 234 ? 26.166 28.530  23.445 1.00 21.35 ? 675  ASP   A C   1 
ATOM   1902 O  O   . ASP   A 1 234 ? 24.928 28.558  23.383 1.00 20.94 ? 675  ASP   A O   1 
ATOM   1903 C  CB  . ASP   A 1 234 ? 27.441 29.178  21.377 1.00 19.26 ? 675  ASP   A CB  1 
ATOM   1904 C  CG  . ASP   A 1 234 ? 27.931 30.321  20.494 1.00 21.51 ? 675  ASP   A CG  1 
ATOM   1905 O  OD1 . ASP   A 1 234 ? 27.880 31.500  20.899 1.00 21.97 ? 675  ASP   A OD1 1 
ATOM   1906 O  OD2 . ASP   A 1 234 ? 28.383 30.031  19.366 1.00 23.01 ? 675  ASP   A OD2 1 
ATOM   1907 N  N   . PRO   A 1 235 ? 26.792 27.529  24.083 1.00 22.88 ? 676  PRO   A N   1 
ATOM   1908 C  CA  . PRO   A 1 235 ? 25.978 26.467  24.701 1.00 21.63 ? 676  PRO   A CA  1 
ATOM   1909 C  C   . PRO   A 1 235 ? 24.991 26.996  25.727 1.00 18.65 ? 676  PRO   A C   1 
ATOM   1910 O  O   . PRO   A 1 235 ? 23.821 26.588  25.730 1.00 20.19 ? 676  PRO   A O   1 
ATOM   1911 C  CB  . PRO   A 1 235 ? 27.029 25.533  25.318 1.00 24.85 ? 676  PRO   A CB  1 
ATOM   1912 C  CG  . PRO   A 1 235 ? 28.264 25.777  24.491 1.00 26.90 ? 676  PRO   A CG  1 
ATOM   1913 C  CD  . PRO   A 1 235 ? 28.236 27.245  24.204 1.00 24.14 ? 676  PRO   A CD  1 
ATOM   1914 N  N   . GLU   A 1 236 ? 25.429 27.933  26.569 1.00 19.31 ? 677  GLU   A N   1 
ATOM   1915 C  CA  . GLU   A 1 236 ? 24.562 28.455  27.619 1.00 18.69 ? 677  GLU   A CA  1 
ATOM   1916 C  C   . GLU   A 1 236 ? 23.444 29.317  27.037 1.00 18.32 ? 677  GLU   A C   1 
ATOM   1917 O  O   . GLU   A 1 236 ? 22.283 29.207  27.454 1.00 18.86 ? 677  GLU   A O   1 
ATOM   1918 C  CB  . GLU   A 1 236 ? 25.408 29.240  28.623 1.00 20.33 ? 677  GLU   A CB  1 
ATOM   1919 C  CG  . GLU   A 1 236 ? 26.387 28.395  29.446 1.00 23.96 ? 677  GLU   A CG  1 
ATOM   1920 C  CD  . GLU   A 1 236 ? 27.555 27.838  28.652 1.00 27.46 ? 677  GLU   A CD  1 
ATOM   1921 O  OE1 . GLU   A 1 236 ? 28.062 28.539  27.751 1.00 27.15 ? 677  GLU   A OE1 1 
ATOM   1922 O  OE2 . GLU   A 1 236 ? 27.985 26.701  28.955 1.00 28.15 ? 677  GLU   A OE2 1 
ATOM   1923 N  N   . TYR   A 1 237 ? 23.765 30.160  26.053 1.00 17.64 ? 678  TYR   A N   1 
ATOM   1924 C  CA  . TYR   A 1 237 ? 22.742 31.021  25.470 1.00 17.20 ? 678  TYR   A CA  1 
ATOM   1925 C  C   . TYR   A 1 237 ? 21.725 30.213  24.671 1.00 20.08 ? 678  TYR   A C   1 
ATOM   1926 O  O   . TYR   A 1 237 ? 20.519 30.473  24.751 1.00 19.89 ? 678  TYR   A O   1 
ATOM   1927 C  CB  . TYR   A 1 237 ? 23.402 32.133  24.644 1.00 15.73 ? 678  TYR   A CB  1 
ATOM   1928 C  CG  . TYR   A 1 237 ? 23.892 33.264  25.525 1.00 16.40 ? 678  TYR   A CG  1 
ATOM   1929 C  CD1 . TYR   A 1 237 ? 24.993 33.095  26.362 1.00 16.04 ? 678  TYR   A CD1 1 
ATOM   1930 C  CD2 . TYR   A 1 237 ? 23.228 34.485  25.557 1.00 17.29 ? 678  TYR   A CD2 1 
ATOM   1931 C  CE1 . TYR   A 1 237 ? 25.434 34.117  27.196 1.00 17.57 ? 678  TYR   A CE1 1 
ATOM   1932 C  CE2 . TYR   A 1 237 ? 23.662 35.512  26.382 1.00 17.14 ? 678  TYR   A CE2 1 
ATOM   1933 C  CZ  . TYR   A 1 237 ? 24.760 35.323  27.199 1.00 18.33 ? 678  TYR   A CZ  1 
ATOM   1934 O  OH  . TYR   A 1 237 ? 25.189 36.336  28.023 1.00 18.34 ? 678  TYR   A OH  1 
ATOM   1935 N  N   . MET   A 1 238 ? 22.186 29.203  23.922 1.00 19.89 ? 679  MET   A N   1 
ATOM   1936 C  CA  . MET   A 1 238 ? 21.252 28.327  23.220 1.00 19.20 ? 679  MET   A CA  1 
ATOM   1937 C  C   . MET   A 1 238 ? 20.348 27.581  24.196 1.00 15.93 ? 679  MET   A C   1 
ATOM   1938 O  O   . MET   A 1 238 ? 19.146 27.444  23.952 1.00 18.75 ? 679  MET   A O   1 
ATOM   1939 C  CB  . MET   A 1 238 ? 22.007 27.355  22.312 1.00 20.81 ? 679  MET   A CB  1 
ATOM   1940 C  CG  . MET   A 1 238 ? 22.808 28.046  21.219 1.00 22.04 ? 679  MET   A CG  1 
ATOM   1941 S  SD  . MET   A 1 238 ? 21.767 28.796  19.947 1.00 23.28 ? 679  MET   A SD  1 
ATOM   1942 C  CE  . MET   A 1 238 ? 20.941 27.359  19.271 1.00 29.91 ? 679  MET   A CE  1 
ATOM   1943 N  N   . ALA   A 1 239 ? 20.906 27.105  25.312 1.00 18.01 ? 680  ALA   A N   1 
ATOM   1944 C  CA  . ALA   A 1 239 ? 20.084 26.407  26.297 1.00 20.15 ? 680  ALA   A CA  1 
ATOM   1945 C  C   . ALA   A 1 239 ? 19.067 27.342  26.940 1.00 21.02 ? 680  ALA   A C   1 
ATOM   1946 O  O   . ALA   A 1 239 ? 17.904 26.967  27.132 1.00 20.94 ? 680  ALA   A O   1 
ATOM   1947 C  CB  . ALA   A 1 239 ? 20.973 25.764  27.359 1.00 20.46 ? 680  ALA   A CB  1 
ATOM   1948 N  N   . ALA   A 1 240 ? 19.480 28.568  27.265 1.00 19.48 ? 681  ALA   A N   1 
ATOM   1949 C  CA  . ALA   A 1 240 ? 18.541 29.528  27.839 1.00 19.42 ? 681  ALA   A CA  1 
ATOM   1950 C  C   . ALA   A 1 240 ? 17.427 29.879  26.859 1.00 19.80 ? 681  ALA   A C   1 
ATOM   1951 O  O   . ALA   A 1 240 ? 16.270 30.048  27.260 1.00 18.47 ? 681  ALA   A O   1 
ATOM   1952 C  CB  . ALA   A 1 240 ? 19.286 30.782  28.293 1.00 18.29 ? 681  ALA   A CB  1 
ATOM   1953 N  N   . PHE   A 1 241 ? 17.748 29.994  25.566 1.00 20.06 ? 682  PHE   A N   1 
ATOM   1954 C  CA  . PHE   A 1 241 ? 16.696 30.261  24.593 1.00 18.08 ? 682  PHE   A CA  1 
ATOM   1955 C  C   . PHE   A 1 241 ? 15.742 29.081  24.475 1.00 19.21 ? 682  PHE   A C   1 
ATOM   1956 O  O   . PHE   A 1 241 ? 14.528 29.268  24.345 1.00 19.61 ? 682  PHE   A O   1 
ATOM   1957 C  CB  . PHE   A 1 241 ? 17.308 30.608  23.237 1.00 17.26 ? 682  PHE   A CB  1 
ATOM   1958 C  CG  . PHE   A 1 241 ? 17.435 32.082  23.002 1.00 17.95 ? 682  PHE   A CG  1 
ATOM   1959 C  CD1 . PHE   A 1 241 ? 18.171 32.871  23.878 1.00 18.44 ? 682  PHE   A CD1 1 
ATOM   1960 C  CD2 . PHE   A 1 241 ? 16.821 32.679  21.923 1.00 17.11 ? 682  PHE   A CD2 1 
ATOM   1961 C  CE1 . PHE   A 1 241 ? 18.284 34.234  23.679 1.00 18.56 ? 682  PHE   A CE1 1 
ATOM   1962 C  CE2 . PHE   A 1 241 ? 16.934 34.050  21.719 1.00 17.49 ? 682  PHE   A CE2 1 
ATOM   1963 C  CZ  . PHE   A 1 241 ? 17.668 34.820  22.602 1.00 15.64 ? 682  PHE   A CZ  1 
ATOM   1964 N  N   . HIS   A 1 242 ? 16.275 27.857  24.503 1.00 20.26 ? 683  HIS   A N   1 
ATOM   1965 C  CA  . HIS   A 1 242 ? 15.432 26.684  24.304 1.00 22.11 ? 683  HIS   A CA  1 
ATOM   1966 C  C   . HIS   A 1 242 ? 14.498 26.472  25.484 1.00 19.40 ? 683  HIS   A C   1 
ATOM   1967 O  O   . HIS   A 1 242 ? 13.306 26.201  25.298 1.00 21.50 ? 683  HIS   A O   1 
ATOM   1968 C  CB  . HIS   A 1 242 ? 16.302 25.447  24.098 1.00 24.74 ? 683  HIS   A CB  1 
ATOM   1969 C  CG  . HIS   A 1 242 ? 15.521 24.180  23.953 1.00 32.11 ? 683  HIS   A CG  1 
ATOM   1970 N  ND1 . HIS   A 1 242 ? 14.903 23.817  22.777 1.00 34.49 ? 683  HIS   A ND1 1 
ATOM   1971 C  CD2 . HIS   A 1 242 ? 15.254 23.191  24.840 1.00 36.43 ? 683  HIS   A CD2 1 
ATOM   1972 C  CE1 . HIS   A 1 242 ? 14.289 22.659  22.943 1.00 38.35 ? 683  HIS   A CE1 1 
ATOM   1973 N  NE2 . HIS   A 1 242 ? 14.486 22.258  24.186 1.00 38.98 ? 683  HIS   A NE2 1 
ATOM   1974 N  N   . HIS   A 1 243 ? 15.015 26.616  26.699 1.00 22.02 ? 684  HIS   A N   1 
ATOM   1975 C  CA  . HIS   A 1 243 ? 14.238 26.292  27.889 1.00 25.69 ? 684  HIS   A CA  1 
ATOM   1976 C  C   . HIS   A 1 243 ? 13.417 27.462  28.414 1.00 28.32 ? 684  HIS   A C   1 
ATOM   1977 O  O   . HIS   A 1 243 ? 12.393 27.237  29.070 1.00 28.04 ? 684  HIS   A O   1 
ATOM   1978 C  CB  . HIS   A 1 243 ? 15.167 25.804  29.000 1.00 30.31 ? 684  HIS   A CB  1 
ATOM   1979 C  CG  . HIS   A 1 243 ? 15.724 24.436  28.760 1.00 32.80 ? 684  HIS   A CG  1 
ATOM   1980 N  ND1 . HIS   A 1 243 ? 14.936 23.306  28.743 1.00 37.89 ? 684  HIS   A ND1 1 
ATOM   1981 C  CD2 . HIS   A 1 243 ? 16.991 24.016  28.528 1.00 31.97 ? 684  HIS   A CD2 1 
ATOM   1982 C  CE1 . HIS   A 1 243 ? 15.692 22.248  28.510 1.00 37.37 ? 684  HIS   A CE1 1 
ATOM   1983 N  NE2 . HIS   A 1 243 ? 16.943 22.650  28.378 1.00 31.77 ? 684  HIS   A NE2 1 
ATOM   1984 N  N   . LEU   A 1 244 ? 13.825 28.700  28.133 1.00 24.69 ? 685  LEU   A N   1 
ATOM   1985 C  CA  . LEU   A 1 244 ? 13.208 29.853  28.783 1.00 22.12 ? 685  LEU   A CA  1 
ATOM   1986 C  C   . LEU   A 1 244 ? 12.698 30.902  27.806 1.00 21.55 ? 685  LEU   A C   1 
ATOM   1987 O  O   . LEU   A 1 244 ? 11.500 31.190  27.771 1.00 22.81 ? 685  LEU   A O   1 
ATOM   1988 C  CB  . LEU   A 1 244 ? 14.198 30.501  29.749 1.00 20.42 ? 685  LEU   A CB  1 
ATOM   1989 C  CG  . LEU   A 1 244 ? 14.490 29.693  31.006 1.00 20.56 ? 685  LEU   A CG  1 
ATOM   1990 C  CD1 . LEU   A 1 244 ? 15.725 30.219  31.714 1.00 18.37 ? 685  LEU   A CD1 1 
ATOM   1991 C  CD2 . LEU   A 1 244 ? 13.275 29.734  31.922 1.00 21.10 ? 685  LEU   A CD2 1 
ATOM   1992 N  N   . VAL   A 1 245 ? 13.600 31.488  27.014 1.00 18.62 ? 686  VAL   A N   1 
ATOM   1993 C  CA  . VAL   A 1 245 ? 13.233 32.651  26.212 1.00 16.63 ? 686  VAL   A CA  1 
ATOM   1994 C  C   . VAL   A 1 245 ? 12.107 32.306  25.255 1.00 17.28 ? 686  VAL   A C   1 
ATOM   1995 O  O   . VAL   A 1 245 ? 11.075 32.980  25.217 1.00 19.08 ? 686  VAL   A O   1 
ATOM   1996 C  CB  . VAL   A 1 245 ? 14.456 33.207  25.462 1.00 16.64 ? 686  VAL   A CB  1 
ATOM   1997 C  CG1 . VAL   A 1 245 ? 14.056 34.431  24.662 1.00 16.83 ? 686  VAL   A CG1 1 
ATOM   1998 C  CG2 . VAL   A 1 245 ? 15.557 33.544  26.440 1.00 18.72 ? 686  VAL   A CG2 1 
ATOM   1999 N  N   . MET   A 1 246 ? 12.295 31.257  24.452 1.00 18.79 ? 687  MET   A N   1 
ATOM   2000 C  CA  . MET   A 1 246 ? 11.342 30.931  23.400 1.00 21.10 ? 687  MET   A CA  1 
ATOM   2001 C  C   . MET   A 1 246 ? 10.013 30.399  23.937 1.00 20.79 ? 687  MET   A C   1 
ATOM   2002 O  O   . MET   A 1 246 ? 8.959  30.816  23.444 1.00 21.45 ? 687  MET   A O   1 
ATOM   2003 C  CB  . MET   A 1 246 ? 11.973 30.015  22.345 1.00 19.39 ? 687  MET   A CB  1 
ATOM   2004 C  CG  . MET   A 1 246 ? 13.116 30.680  21.591 1.00 18.36 ? 687  MET   A CG  1 
ATOM   2005 S  SD  . MET   A 1 246 ? 12.675 32.249  20.830 1.00 21.03 ? 687  MET   A SD  1 
ATOM   2006 C  CE  . MET   A 1 246 ? 11.364 31.729  19.727 1.00 20.57 ? 687  MET   A CE  1 
ATOM   2007 N  N   . PRO   A 1 247 ? 10.002 29.487  24.919 1.00 22.66 ? 688  PRO   A N   1 
ATOM   2008 C  CA  . PRO   A 1 247 ? 8.703  29.068  25.477 1.00 23.28 ? 688  PRO   A CA  1 
ATOM   2009 C  C   . PRO   A 1 247 ? 7.905  30.218  26.061 1.00 21.64 ? 688  PRO   A C   1 
ATOM   2010 O  O   . PRO   A 1 247 ? 6.701  30.319  25.801 1.00 23.88 ? 688  PRO   A O   1 
ATOM   2011 C  CB  . PRO   A 1 247 ? 9.095  28.030  26.536 1.00 26.03 ? 688  PRO   A CB  1 
ATOM   2012 C  CG  . PRO   A 1 247 ? 10.390 27.486  26.053 1.00 30.13 ? 688  PRO   A CG  1 
ATOM   2013 C  CD  . PRO   A 1 247 ? 11.102 28.673  25.465 1.00 27.98 ? 688  PRO   A CD  1 
ATOM   2014 N  N   . ILE   A 1 248 ? 8.546  31.098  26.832 1.00 20.93 ? 689  ILE   A N   1 
ATOM   2015 C  CA  . ILE   A 1 248 ? 7.828  32.233  27.407 1.00 19.71 ? 689  ILE   A CA  1 
ATOM   2016 C  C   . ILE   A 1 248 ? 7.371  33.182  26.308 1.00 20.99 ? 689  ILE   A C   1 
ATOM   2017 O  O   . ILE   A 1 248 ? 6.214  33.622  26.277 1.00 23.80 ? 689  ILE   A O   1 
ATOM   2018 C  CB  . ILE   A 1 248 ? 8.702  32.949  28.450 1.00 19.83 ? 689  ILE   A CB  1 
ATOM   2019 C  CG1 . ILE   A 1 248 ? 8.996  32.032  29.642 1.00 19.64 ? 689  ILE   A CG1 1 
ATOM   2020 C  CG2 . ILE   A 1 248 ? 8.038  34.252  28.899 1.00 18.06 ? 689  ILE   A CG2 1 
ATOM   2021 C  CD1 . ILE   A 1 248 ? 10.029 32.599  30.578 1.00 19.08 ? 689  ILE   A CD1 1 
ATOM   2022 N  N   . ALA   A 1 249 ? 8.271  33.495  25.372 1.00 19.50 ? 690  ALA   A N   1 
ATOM   2023 C  CA  . ALA   A 1 249 ? 7.918  34.424  24.309 1.00 18.87 ? 690  ALA   A CA  1 
ATOM   2024 C  C   . ALA   A 1 249 ? 6.744  33.907  23.489 1.00 19.30 ? 690  ALA   A C   1 
ATOM   2025 O  O   . ALA   A 1 249 ? 5.861  34.680  23.107 1.00 20.27 ? 690  ALA   A O   1 
ATOM   2026 C  CB  . ALA   A 1 249 ? 9.133  34.697  23.425 1.00 16.46 ? 690  ALA   A CB  1 
ATOM   2027 N  N   . ARG   A 1 250 ? 6.717  32.602  23.203 1.00 20.29 ? 691  ARG   A N   1 
ATOM   2028 C  CA  . ARG   A 1 250 ? 5.620  32.051  22.414 1.00 21.67 ? 691  ARG   A CA  1 
ATOM   2029 C  C   . ARG   A 1 250 ? 4.295  32.178  23.150 1.00 23.10 ? 691  ARG   A C   1 
ATOM   2030 O  O   . ARG   A 1 250 ? 3.261  32.486  22.544 1.00 23.41 ? 691  ARG   A O   1 
ATOM   2031 C  CB  . ARG   A 1 250 ? 5.904  30.592  22.062 1.00 22.81 ? 691  ARG   A CB  1 
ATOM   2032 C  CG  . ARG   A 1 250 ? 6.726  30.430  20.793 1.00 26.81 ? 691  ARG   A CG  1 
ATOM   2033 C  CD  . ARG   A 1 250 ? 6.771  28.983  20.351 1.00 28.49 ? 691  ARG   A CD  1 
ATOM   2034 N  NE  . ARG   A 1 250 ? 7.516  28.166  21.301 1.00 29.02 ? 691  ARG   A NE  1 
ATOM   2035 C  CZ  . ARG   A 1 250 ? 8.807  27.874  21.185 1.00 30.95 ? 691  ARG   A CZ  1 
ATOM   2036 N  NH1 . ARG   A 1 250 ? 9.503  28.333  20.153 1.00 33.23 ? 691  ARG   A NH1 1 
ATOM   2037 N  NH2 . ARG   A 1 250 ? 9.403  27.123  22.101 1.00 29.65 ? 691  ARG   A NH2 1 
ATOM   2038 N  N   . GLU   A 1 251 ? 4.311  31.960  24.463 1.00 23.91 ? 692  GLU   A N   1 
ATOM   2039 C  CA  . GLU   A 1 251 ? 3.087  32.084  25.246 1.00 25.32 ? 692  GLU   A CA  1 
ATOM   2040 C  C   . GLU   A 1 251 ? 2.626  33.534  25.334 1.00 24.46 ? 692  GLU   A C   1 
ATOM   2041 O  O   . GLU   A 1 251 ? 1.424  33.816  25.259 1.00 24.34 ? 692  GLU   A O   1 
ATOM   2042 C  CB  . GLU   A 1 251 ? 3.305  31.491  26.634 1.00 25.75 ? 692  GLU   A CB  1 
ATOM   2043 C  CG  . GLU   A 1 251 ? 2.010  31.223  27.375 1.00 26.21 ? 692  GLU   A CG  1 
ATOM   2044 C  CD  . GLU   A 1 251 ? 2.223  30.479  28.675 1.00 30.48 ? 692  GLU   A CD  1 
ATOM   2045 O  OE1 . GLU   A 1 251 ? 3.269  29.815  28.826 1.00 30.02 ? 692  GLU   A OE1 1 
ATOM   2046 O  OE2 . GLU   A 1 251 ? 1.335  30.552  29.546 1.00 34.44 ? 692  GLU   A OE2 1 
ATOM   2047 N  N   . PHE   A 1 252 ? 3.569  34.467  25.491 1.00 21.91 ? 693  PHE   A N   1 
ATOM   2048 C  CA  . PHE   A 1 252 ? 3.241  35.889  25.491 1.00 20.13 ? 693  PHE   A CA  1 
ATOM   2049 C  C   . PHE   A 1 252 ? 2.656  36.335  24.154 1.00 19.60 ? 693  PHE   A C   1 
ATOM   2050 O  O   . PHE   A 1 252 ? 1.799  37.226  24.113 1.00 20.26 ? 693  PHE   A O   1 
ATOM   2051 C  CB  . PHE   A 1 252 ? 4.517  36.672  25.808 1.00 18.68 ? 693  PHE   A CB  1 
ATOM   2052 C  CG  . PHE   A 1 252 ? 4.337  38.160  25.848 1.00 18.75 ? 693  PHE   A CG  1 
ATOM   2053 C  CD1 . PHE   A 1 252 ? 3.503  38.745  26.789 1.00 17.74 ? 693  PHE   A CD1 1 
ATOM   2054 C  CD2 . PHE   A 1 252 ? 5.032  38.981  24.968 1.00 16.17 ? 693  PHE   A CD2 1 
ATOM   2055 C  CE1 . PHE   A 1 252 ? 3.346  40.120  26.838 1.00 19.26 ? 693  PHE   A CE1 1 
ATOM   2056 C  CE2 . PHE   A 1 252 ? 4.894  40.352  25.017 1.00 15.93 ? 693  PHE   A CE2 1 
ATOM   2057 C  CZ  . PHE   A 1 252 ? 4.044  40.927  25.950 1.00 18.13 ? 693  PHE   A CZ  1 
ATOM   2058 N  N   . ALA   A 1 253 ? 3.108  35.732  23.051 1.00 22.58 ? 694  ALA   A N   1 
ATOM   2059 C  CA  . ALA   A 1 253 ? 2.623  36.040  21.711 1.00 21.16 ? 694  ALA   A CA  1 
ATOM   2060 C  C   . ALA   A 1 253 ? 2.821  37.517  21.381 1.00 21.70 ? 694  ALA   A C   1 
ATOM   2061 O  O   . ALA   A 1 253 ? 1.845  38.249  21.179 1.00 23.08 ? 694  ALA   A O   1 
ATOM   2062 C  CB  . ALA   A 1 253 ? 1.155  35.626  21.550 1.00 21.88 ? 694  ALA   A CB  1 
ATOM   2063 N  N   . PRO   A 1 254 ? 4.064  37.993  21.309 1.00 20.87 ? 695  PRO   A N   1 
ATOM   2064 C  CA  . PRO   A 1 254 ? 4.280  39.417  21.046 1.00 18.01 ? 695  PRO   A CA  1 
ATOM   2065 C  C   . PRO   A 1 254 ? 3.796  39.808  19.663 1.00 17.86 ? 695  PRO   A C   1 
ATOM   2066 O  O   . PRO   A 1 254 ? 3.739  38.993  18.735 1.00 19.55 ? 695  PRO   A O   1 
ATOM   2067 C  CB  . PRO   A 1 254 ? 5.803  39.574  21.150 1.00 16.79 ? 695  PRO   A CB  1 
ATOM   2068 C  CG  . PRO   A 1 254 ? 6.346  38.219  20.868 1.00 18.33 ? 695  PRO   A CG  1 
ATOM   2069 C  CD  . PRO   A 1 254 ? 5.328  37.249  21.417 1.00 19.55 ? 695  PRO   A CD  1 
ATOM   2070 N  N   . GLU   A 1 255 ? 3.440  41.079  19.538 1.00 18.47 ? 696  GLU   A N   1 
ATOM   2071 C  CA  . GLU   A 1 255 ? 3.126  41.687  18.258 1.00 19.22 ? 696  GLU   A CA  1 
ATOM   2072 C  C   . GLU   A 1 255 ? 4.310  42.447  17.680 1.00 17.73 ? 696  GLU   A C   1 
ATOM   2073 O  O   . GLU   A 1 255 ? 4.281  42.799  16.499 1.00 18.78 ? 696  GLU   A O   1 
ATOM   2074 C  CB  . GLU   A 1 255 ? 1.909  42.608  18.407 1.00 22.83 ? 696  GLU   A CB  1 
ATOM   2075 C  CG  . GLU   A 1 255 ? 0.633  41.838  18.778 1.00 27.23 ? 696  GLU   A CG  1 
ATOM   2076 C  CD  . GLU   A 1 255 ? -0.478 42.730  19.290 1.00 32.91 ? 696  GLU   A CD  1 
ATOM   2077 O  OE1 . GLU   A 1 255 ? -0.418 43.130  20.471 1.00 30.13 ? 696  GLU   A OE1 1 
ATOM   2078 O  OE2 . GLU   A 1 255 ? -1.415 43.025  18.519 1.00 37.64 ? 696  GLU   A OE2 1 
ATOM   2079 N  N   . LEU   A 1 256 ? 5.348  42.681  18.483 1.00 14.86 ? 697  LEU   A N   1 
ATOM   2080 C  CA  . LEU   A 1 256 ? 6.588  43.302  18.046 1.00 14.12 ? 697  LEU   A CA  1 
ATOM   2081 C  C   . LEU   A 1 256 ? 7.682  42.803  18.978 1.00 14.26 ? 697  LEU   A C   1 
ATOM   2082 O  O   . LEU   A 1 256 ? 7.462  42.690  20.185 1.00 14.80 ? 697  LEU   A O   1 
ATOM   2083 C  CB  . LEU   A 1 256 ? 6.503  44.826  18.145 1.00 14.37 ? 697  LEU   A CB  1 
ATOM   2084 C  CG  . LEU   A 1 256 ? 7.795  45.583  17.823 1.00 15.07 ? 697  LEU   A CG  1 
ATOM   2085 C  CD1 . LEU   A 1 256 ? 8.246  45.317  16.385 1.00 17.56 ? 697  LEU   A CD1 1 
ATOM   2086 C  CD2 . LEU   A 1 256 ? 7.579  47.064  18.071 1.00 17.41 ? 697  LEU   A CD2 1 
ATOM   2087 N  N   . VAL   A 1 257 ? 8.842  42.480  18.416 1.00 15.15 ? 698  VAL   A N   1 
ATOM   2088 C  CA  . VAL   A 1 257 ? 10.015 42.078  19.187 1.00 13.40 ? 698  VAL   A CA  1 
ATOM   2089 C  C   . VAL   A 1 257 ? 11.088 43.141  19.000 1.00 13.09 ? 698  VAL   A C   1 
ATOM   2090 O  O   . VAL   A 1 257 ? 11.451 43.469  17.861 1.00 15.33 ? 698  VAL   A O   1 
ATOM   2091 C  CB  . VAL   A 1 257 ? 10.537 40.703  18.737 1.00 16.52 ? 698  VAL   A CB  1 
ATOM   2092 C  CG1 . VAL   A 1 257 ? 11.811 40.315  19.493 1.00 16.92 ? 698  VAL   A CG1 1 
ATOM   2093 C  CG2 . VAL   A 1 257 ? 9.450  39.633  18.903 1.00 17.56 ? 698  VAL   A CG2 1 
ATOM   2094 N  N   . LEU   A 1 258 ? 11.601 43.669  20.104 1.00 13.32 ? 699  LEU   A N   1 
ATOM   2095 C  CA  . LEU   A 1 258 ? 12.773 44.530  20.094 1.00 13.09 ? 699  LEU   A CA  1 
ATOM   2096 C  C   . LEU   A 1 258 ? 13.907 43.748  20.734 1.00 14.90 ? 699  LEU   A C   1 
ATOM   2097 O  O   . LEU   A 1 258 ? 13.706 43.087  21.760 1.00 13.77 ? 699  LEU   A O   1 
ATOM   2098 C  CB  . LEU   A 1 258 ? 12.515 45.792  20.917 1.00 13.17 ? 699  LEU   A CB  1 
ATOM   2099 C  CG  . LEU   A 1 258 ? 11.270 46.612  20.573 1.00 13.94 ? 699  LEU   A CG  1 
ATOM   2100 C  CD1 . LEU   A 1 258 ? 11.164 47.826  21.474 1.00 16.04 ? 699  LEU   A CD1 1 
ATOM   2101 C  CD2 . LEU   A 1 258 ? 11.306 47.051  19.111 1.00 15.53 ? 699  LEU   A CD2 1 
ATOM   2102 N  N   . VAL   A 1 259 ? 15.093 43.810  20.138 1.00 14.47 ? 700  VAL   A N   1 
ATOM   2103 C  CA  . VAL   A 1 259 ? 16.276 43.195  20.724 1.00 13.28 ? 700  VAL   A CA  1 
ATOM   2104 C  C   . VAL   A 1 259 ? 17.165 44.317  21.236 1.00 12.66 ? 700  VAL   A C   1 
ATOM   2105 O  O   . VAL   A 1 259 ? 17.578 45.190  20.464 1.00 13.55 ? 700  VAL   A O   1 
ATOM   2106 C  CB  . VAL   A 1 259 ? 17.028 42.286  19.738 1.00 12.70 ? 700  VAL   A CB  1 
ATOM   2107 C  CG1 . VAL   A 1 259 ? 18.153 41.536  20.475 1.00 13.55 ? 700  VAL   A CG1 1 
ATOM   2108 C  CG2 . VAL   A 1 259 ? 16.079 41.299  19.071 1.00 13.78 ? 700  VAL   A CG2 1 
ATOM   2109 N  N   . SER   A 1 260 ? 17.406 44.336  22.544 1.00 13.18 ? 701  SER   A N   1 
ATOM   2110 C  CA  . SER   A 1 260 ? 18.464 45.180  23.090 1.00 12.61 ? 701  SER   A CA  1 
ATOM   2111 C  C   . SER   A 1 260 ? 19.749 44.407  22.832 1.00 11.43 ? 701  SER   A C   1 
ATOM   2112 O  O   . SER   A 1 260 ? 20.203 43.593  23.646 1.00 13.29 ? 701  SER   A O   1 
ATOM   2113 C  CB  . SER   A 1 260 ? 18.231 45.458  24.572 1.00 13.60 ? 701  SER   A CB  1 
ATOM   2114 O  OG  . SER   A 1 260 ? 17.485 46.651  24.723 1.00 14.30 ? 701  SER   A OG  1 
ATOM   2115 N  N   . ALA   A 1 261 ? 20.312 44.648  21.651 1.00 12.12 ? 702  ALA   A N   1 
ATOM   2116 C  CA  . ALA   A 1 261 ? 21.384 43.824  21.103 1.00 13.07 ? 702  ALA   A CA  1 
ATOM   2117 C  C   . ALA   A 1 261 ? 22.731 44.483  21.384 1.00 14.03 ? 702  ALA   A C   1 
ATOM   2118 O  O   . ALA   A 1 261 ? 23.359 45.100  20.518 1.00 14.29 ? 702  ALA   A O   1 
ATOM   2119 C  CB  . ALA   A 1 261 ? 21.167 43.605  19.614 1.00 13.91 ? 702  ALA   A CB  1 
ATOM   2120 N  N   . GLY   A 1 262 ? 23.165 44.372  22.635 1.00 14.68 ? 703  GLY   A N   1 
ATOM   2121 C  CA  . GLY   A 1 262 ? 24.561 44.595  22.936 1.00 16.13 ? 703  GLY   A CA  1 
ATOM   2122 C  C   . GLY   A 1 262 ? 25.385 43.404  22.497 1.00 13.44 ? 703  GLY   A C   1 
ATOM   2123 O  O   . GLY   A 1 262 ? 24.921 42.265  22.489 1.00 16.37 ? 703  GLY   A O   1 
ATOM   2124 N  N   . PHE   A 1 263 ? 26.617 43.669  22.080 1.00 12.41 ? 704  PHE   A N   1 
ATOM   2125 C  CA  . PHE   A 1 263 ? 27.490 42.592  21.630 1.00 12.55 ? 704  PHE   A CA  1 
ATOM   2126 C  C   . PHE   A 1 263 ? 28.706 42.469  22.535 1.00 13.83 ? 704  PHE   A C   1 
ATOM   2127 O  O   . PHE   A 1 263 ? 29.788 42.069  22.106 1.00 14.29 ? 704  PHE   A O   1 
ATOM   2128 C  CB  . PHE   A 1 263 ? 27.837 42.711  20.148 1.00 12.90 ? 704  PHE   A CB  1 
ATOM   2129 C  CG  . PHE   A 1 263 ? 26.638 42.581  19.266 1.00 12.85 ? 704  PHE   A CG  1 
ATOM   2130 C  CD1 . PHE   A 1 263 ? 26.131 41.326  18.953 1.00 13.03 ? 704  PHE   A CD1 1 
ATOM   2131 C  CD2 . PHE   A 1 263 ? 25.971 43.709  18.808 1.00 13.21 ? 704  PHE   A CD2 1 
ATOM   2132 C  CE1 . PHE   A 1 263 ? 24.992 41.189  18.156 1.00 14.25 ? 704  PHE   A CE1 1 
ATOM   2133 C  CE2 . PHE   A 1 263 ? 24.826 43.586  17.999 1.00 13.34 ? 704  PHE   A CE2 1 
ATOM   2134 C  CZ  . PHE   A 1 263 ? 24.339 42.322  17.683 1.00 14.41 ? 704  PHE   A CZ  1 
ATOM   2135 N  N   . ASP   A 1 264 ? 28.525 42.819  23.803 1.00 13.64 ? 705  ASP   A N   1 
ATOM   2136 C  CA  . ASP   A 1 264 ? 29.575 42.719  24.807 1.00 14.06 ? 705  ASP   A CA  1 
ATOM   2137 C  C   . ASP   A 1 264 ? 29.659 41.356  25.487 1.00 13.48 ? 705  ASP   A C   1 
ATOM   2138 O  O   . ASP   A 1 264 ? 30.609 41.126  26.250 1.00 14.93 ? 705  ASP   A O   1 
ATOM   2139 C  CB  . ASP   A 1 264 ? 29.548 43.900  25.796 1.00 13.35 ? 705  ASP   A CB  1 
ATOM   2140 C  CG  . ASP   A 1 264 ? 28.168 44.258  26.286 1.00 14.30 ? 705  ASP   A CG  1 
ATOM   2141 O  OD1 . ASP   A 1 264 ? 27.201 43.527  25.988 1.00 14.08 ? 705  ASP   A OD1 1 
ATOM   2142 O  OD2 . ASP   A 1 264 ? 28.060 45.323  26.952 1.00 14.27 ? 705  ASP   A OD2 1 
ATOM   2143 N  N   . ALA   A 1 265 ? 28.728 40.438  25.204 1.00 14.60 ? 706  ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 265 ? 28.928 39.035  25.545 1.00 15.70 ? 706  ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 265 ? 29.753 38.300  24.493 1.00 14.75 ? 706  ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 265 ? 29.949 37.085  24.609 1.00 16.14 ? 706  ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 265 ? 27.587 38.323  25.754 1.00 16.39 ? 706  ALA   A CB  1 
ATOM   2148 N  N   . ALA   A 1 266 ? 30.255 39.005  23.482 1.00 14.68 ? 707  ALA   A N   1 
ATOM   2149 C  CA  . ALA   A 1 266 ? 30.917 38.356  22.365 1.00 14.36 ? 707  ALA   A CA  1 
ATOM   2150 C  C   . ALA   A 1 266 ? 32.331 37.935  22.725 1.00 14.58 ? 707  ALA   A C   1 
ATOM   2151 O  O   . ALA   A 1 266 ? 33.020 38.579  23.529 1.00 16.14 ? 707  ALA   A O   1 
ATOM   2152 C  CB  . ALA   A 1 266 ? 31.023 39.319  21.184 1.00 13.40 ? 707  ALA   A CB  1 
ATOM   2153 N  N   A ARG   A 1 267 ? 32.770 36.844  22.104 0.50 14.13 ? 708  ARG   A N   1 
ATOM   2154 N  N   B ARG   A 1 267 ? 32.761 36.832  22.117 0.50 13.10 ? 708  ARG   A N   1 
ATOM   2155 C  CA  A ARG   A 1 267 ? 34.169 36.458  22.184 0.50 16.42 ? 708  ARG   A CA  1 
ATOM   2156 C  CA  B ARG   A 1 267 ? 34.169 36.473  22.141 0.50 17.57 ? 708  ARG   A CA  1 
ATOM   2157 C  C   A ARG   A 1 267 ? 35.043 37.615  21.717 0.50 16.95 ? 708  ARG   A C   1 
ATOM   2158 C  C   B ARG   A 1 267 ? 35.003 37.680  21.739 0.50 16.64 ? 708  ARG   A C   1 
ATOM   2159 O  O   A ARG   A 1 267 ? 34.829 38.176  20.638 0.50 16.70 ? 708  ARG   A O   1 
ATOM   2160 O  O   B ARG   A 1 267 ? 34.717 38.340  20.736 0.50 15.78 ? 708  ARG   A O   1 
ATOM   2161 C  CB  A ARG   A 1 267 ? 34.398 35.229  21.308 0.50 16.40 ? 708  ARG   A CB  1 
ATOM   2162 C  CB  B ARG   A 1 267 ? 34.406 35.328  21.158 0.50 18.25 ? 708  ARG   A CB  1 
ATOM   2163 C  CG  A ARG   A 1 267 ? 35.836 35.015  20.885 0.50 19.10 ? 708  ARG   A CG  1 
ATOM   2164 C  CG  B ARG   A 1 267 ? 35.657 34.522  21.456 0.50 21.96 ? 708  ARG   A CG  1 
ATOM   2165 C  CD  A ARG   A 1 267 ? 35.923 33.921  19.838 0.50 21.88 ? 708  ARG   A CD  1 
ATOM   2166 C  CD  B ARG   A 1 267 ? 36.175 33.796  20.228 0.50 30.69 ? 708  ARG   A CD  1 
ATOM   2167 N  NE  A ARG   A 1 267 ? 35.535 34.419  18.525 0.50 24.30 ? 708  ARG   A NE  1 
ATOM   2168 N  NE  B ARG   A 1 267 ? 35.104 33.272  19.386 0.50 36.04 ? 708  ARG   A NE  1 
ATOM   2169 C  CZ  A ARG   A 1 267 ? 35.011 33.667  17.563 0.50 24.89 ? 708  ARG   A CZ  1 
ATOM   2170 C  CZ  B ARG   A 1 267 ? 34.847 33.699  18.155 0.50 40.63 ? 708  ARG   A CZ  1 
ATOM   2171 N  NH1 A ARG   A 1 267 ? 34.807 32.372  17.768 0.50 19.56 ? 708  ARG   A NH1 1 
ATOM   2172 N  NH1 B ARG   A 1 267 ? 35.581 34.666  17.621 0.50 43.41 ? 708  ARG   A NH1 1 
ATOM   2173 N  NH2 A ARG   A 1 267 ? 34.685 34.214  16.402 0.50 19.71 ? 708  ARG   A NH2 1 
ATOM   2174 N  NH2 B ARG   A 1 267 ? 33.855 33.164  17.456 0.50 42.52 ? 708  ARG   A NH2 1 
ATOM   2175 N  N   . GLY   A 1 268 ? 36.015 37.990  22.553 1.00 16.87 ? 709  GLY   A N   1 
ATOM   2176 C  CA  . GLY   A 1 268 ? 36.913 39.096  22.280 1.00 15.72 ? 709  GLY   A CA  1 
ATOM   2177 C  C   . GLY   A 1 268 ? 36.577 40.411  22.957 1.00 15.24 ? 709  GLY   A C   1 
ATOM   2178 O  O   . GLY   A 1 268 ? 37.399 41.334  22.912 1.00 18.11 ? 709  GLY   A O   1 
ATOM   2179 N  N   . ASP   A 1 269 ? 35.395 40.535  23.555 1.00 15.10 ? 710  ASP   A N   1 
ATOM   2180 C  CA  . ASP   A 1 269 ? 35.029 41.795  24.188 1.00 13.63 ? 710  ASP   A CA  1 
ATOM   2181 C  C   . ASP   A 1 269 ? 35.980 42.116  25.339 1.00 15.06 ? 710  ASP   A C   1 
ATOM   2182 O  O   . ASP   A 1 269 ? 36.327 41.226  26.125 1.00 16.81 ? 710  ASP   A O   1 
ATOM   2183 C  CB  . ASP   A 1 269 ? 33.608 41.730  24.742 1.00 15.06 ? 710  ASP   A CB  1 
ATOM   2184 C  CG  . ASP   A 1 269 ? 33.077 43.102  25.109 1.00 15.56 ? 710  ASP   A CG  1 
ATOM   2185 O  OD1 . ASP   A 1 269 ? 32.625 43.821  24.193 1.00 14.56 ? 710  ASP   A OD1 1 
ATOM   2186 O  OD2 . ASP   A 1 269 ? 33.157 43.487  26.295 1.00 15.88 ? 710  ASP   A OD2 1 
ATOM   2187 N  N   . PRO   A 1 270 ? 36.389 43.378  25.496 1.00 15.47 ? 711  PRO   A N   1 
ATOM   2188 C  CA  . PRO   A 1 270 ? 37.325 43.722  26.579 1.00 16.05 ? 711  PRO   A CA  1 
ATOM   2189 C  C   . PRO   A 1 270 ? 36.685 43.785  27.954 1.00 17.50 ? 711  PRO   A C   1 
ATOM   2190 O  O   . PRO   A 1 270 ? 37.425 43.827  28.950 1.00 17.66 ? 711  PRO   A O   1 
ATOM   2191 C  CB  . PRO   A 1 270 ? 37.866 45.092  26.156 1.00 16.81 ? 711  PRO   A CB  1 
ATOM   2192 C  CG  . PRO   A 1 270 ? 36.776 45.673  25.285 1.00 17.65 ? 711  PRO   A CG  1 
ATOM   2193 C  CD  . PRO   A 1 270 ? 36.187 44.498  24.555 1.00 17.22 ? 711  PRO   A CD  1 
ATOM   2194 N  N   . LEU   A 1 271 ? 35.351 43.781  28.048 1.00 15.02 ? 712  LEU   A N   1 
ATOM   2195 C  CA  . LEU   A 1 271 ? 34.637 43.958  29.306 1.00 16.68 ? 712  LEU   A CA  1 
ATOM   2196 C  C   . LEU   A 1 271 ? 33.805 42.756  29.721 1.00 18.21 ? 712  LEU   A C   1 
ATOM   2197 O  O   . LEU   A 1 271 ? 33.724 42.454  30.916 1.00 18.13 ? 712  LEU   A O   1 
ATOM   2198 C  CB  . LEU   A 1 271 ? 33.710 45.180  29.224 1.00 16.64 ? 712  LEU   A CB  1 
ATOM   2199 C  CG  . LEU   A 1 271 ? 34.403 46.532  29.059 1.00 20.36 ? 712  LEU   A CG  1 
ATOM   2200 C  CD1 . LEU   A 1 271 ? 33.394 47.650  28.944 1.00 20.39 ? 712  LEU   A CD1 1 
ATOM   2201 C  CD2 . LEU   A 1 271 ? 35.362 46.802  30.220 1.00 22.02 ? 712  LEU   A CD2 1 
ATOM   2202 N  N   . GLY   A 1 272 ? 33.178 42.061  28.769 1.00 17.13 ? 713  GLY   A N   1 
ATOM   2203 C  CA  . GLY   A 1 272 ? 32.155 41.090  29.127 1.00 16.92 ? 713  GLY   A CA  1 
ATOM   2204 C  C   . GLY   A 1 272 ? 32.705 39.801  29.708 1.00 17.52 ? 713  GLY   A C   1 
ATOM   2205 O  O   . GLY   A 1 272 ? 32.088 39.202  30.594 1.00 17.94 ? 713  GLY   A O   1 
ATOM   2206 N  N   . GLY   A 1 273 ? 33.848 39.340  29.205 1.00 17.56 ? 714  GLY   A N   1 
ATOM   2207 C  CA  . GLY   A 1 273 ? 34.422 38.080  29.656 1.00 19.12 ? 714  GLY   A CA  1 
ATOM   2208 C  C   . GLY   A 1 273 ? 33.735 36.828  29.157 1.00 20.31 ? 714  GLY   A C   1 
ATOM   2209 O  O   . GLY   A 1 273 ? 34.007 35.744  29.685 1.00 23.09 ? 714  GLY   A O   1 
ATOM   2210 N  N   . PHE   A 1 274 ? 32.853 36.933  28.162 1.00 17.25 ? 715  PHE   A N   1 
ATOM   2211 C  CA  . PHE   A 1 274 ? 32.085 35.810  27.635 1.00 16.03 ? 715  PHE   A CA  1 
ATOM   2212 C  C   . PHE   A 1 274 ? 32.571 35.485  26.226 1.00 17.39 ? 715  PHE   A C   1 
ATOM   2213 O  O   . PHE   A 1 274 ? 33.463 36.143  25.683 1.00 18.36 ? 715  PHE   A O   1 
ATOM   2214 C  CB  . PHE   A 1 274 ? 30.585 36.118  27.639 1.00 18.18 ? 715  PHE   A CB  1 
ATOM   2215 C  CG  . PHE   A 1 274 ? 29.910 35.923  28.979 1.00 18.03 ? 715  PHE   A CG  1 
ATOM   2216 C  CD1 . PHE   A 1 274 ? 30.641 35.652  30.134 1.00 21.43 ? 715  PHE   A CD1 1 
ATOM   2217 C  CD2 . PHE   A 1 274 ? 28.527 36.022  29.071 1.00 19.52 ? 715  PHE   A CD2 1 
ATOM   2218 C  CE1 . PHE   A 1 274 ? 29.992 35.481  31.354 1.00 19.31 ? 715  PHE   A CE1 1 
ATOM   2219 C  CE2 . PHE   A 1 274 ? 27.879 35.854  30.278 1.00 19.25 ? 715  PHE   A CE2 1 
ATOM   2220 C  CZ  . PHE   A 1 274 ? 28.615 35.584  31.426 1.00 19.01 ? 715  PHE   A CZ  1 
ATOM   2221 N  N   . GLN   A 1 275 ? 31.962 34.468  25.615 1.00 17.03 ? 716  GLN   A N   1 
ATOM   2222 C  CA  . GLN   A 1 275 ? 32.484 33.971  24.346 1.00 17.06 ? 716  GLN   A CA  1 
ATOM   2223 C  C   . GLN   A 1 275 ? 31.375 33.590  23.382 1.00 18.55 ? 716  GLN   A C   1 
ATOM   2224 O  O   . GLN   A 1 275 ? 31.506 32.630  22.618 1.00 17.63 ? 716  GLN   A O   1 
ATOM   2225 C  CB  . GLN   A 1 275 ? 33.470 32.820  24.550 1.00 21.73 ? 716  GLN   A CB  1 
ATOM   2226 C  CG  . GLN   A 1 275 ? 32.927 31.644  25.335 1.00 30.20 ? 716  GLN   A CG  1 
ATOM   2227 C  CD  . GLN   A 1 275 ? 34.019 30.640  25.685 1.00 33.89 ? 716  GLN   A CD  1 
ATOM   2228 O  OE1 . GLN   A 1 275 ? 34.990 30.485  24.946 1.00 34.67 ? 716  GLN   A OE1 1 
ATOM   2229 N  NE2 . GLN   A 1 275 ? 33.867 29.965  26.822 1.00 38.04 ? 716  GLN   A NE2 1 
ATOM   2230 N  N   . VAL   A 1 276 ? 30.272 34.341  23.381 1.00 16.20 ? 717  VAL   A N   1 
ATOM   2231 C  CA  . VAL   A 1 276 ? 29.269 34.143  22.341 1.00 16.14 ? 717  VAL   A CA  1 
ATOM   2232 C  C   . VAL   A 1 276 ? 29.893 34.479  20.991 1.00 16.26 ? 717  VAL   A C   1 
ATOM   2233 O  O   . VAL   A 1 276 ? 30.573 35.501  20.838 1.00 15.64 ? 717  VAL   A O   1 
ATOM   2234 C  CB  . VAL   A 1 276 ? 28.014 34.984  22.633 1.00 15.24 ? 717  VAL   A CB  1 
ATOM   2235 C  CG1 . VAL   A 1 276 ? 26.924 34.719  21.595 1.00 15.98 ? 717  VAL   A CG1 1 
ATOM   2236 C  CG2 . VAL   A 1 276 ? 27.486 34.685  24.028 1.00 16.59 ? 717  VAL   A CG2 1 
ATOM   2237 N  N   . THR   A 1 277 ? 29.666 33.609  20.001 1.00 16.11 ? 718  THR   A N   1 
ATOM   2238 C  CA  . THR   A 1 277 ? 30.260 33.747  18.679 1.00 16.85 ? 718  THR   A CA  1 
ATOM   2239 C  C   . THR   A 1 277 ? 29.303 34.462  17.739 1.00 16.84 ? 718  THR   A C   1 
ATOM   2240 O  O   . THR   A 1 277 ? 28.102 34.562  18.012 1.00 16.88 ? 718  THR   A O   1 
ATOM   2241 C  CB  . THR   A 1 277 ? 30.585 32.369  18.103 1.00 17.27 ? 718  THR   A CB  1 
ATOM   2242 O  OG1 . THR   A 1 277 ? 29.369 31.671  17.795 1.00 17.54 ? 718  THR   A OG1 1 
ATOM   2243 C  CG2 . THR   A 1 277 ? 31.439 31.556  19.071 1.00 18.12 ? 718  THR   A CG2 1 
ATOM   2244 N  N   . PRO   A 1 278 ? 29.809 34.985  16.615 1.00 16.53 ? 719  PRO   A N   1 
ATOM   2245 C  CA  . PRO   A 1 278 ? 28.891 35.593  15.641 1.00 15.48 ? 719  PRO   A CA  1 
ATOM   2246 C  C   . PRO   A 1 278 ? 27.826 34.620  15.162 1.00 15.34 ? 719  PRO   A C   1 
ATOM   2247 O  O   . PRO   A 1 278 ? 26.659 35.001  14.985 1.00 16.55 ? 719  PRO   A O   1 
ATOM   2248 C  CB  . PRO   A 1 278 ? 29.827 36.057  14.509 1.00 16.84 ? 719  PRO   A CB  1 
ATOM   2249 C  CG  . PRO   A 1 278 ? 31.165 36.217  15.171 1.00 18.17 ? 719  PRO   A CG  1 
ATOM   2250 C  CD  . PRO   A 1 278 ? 31.224 35.164  16.232 1.00 16.73 ? 719  PRO   A CD  1 
ATOM   2251 N  N   . GLU   A 1 279 ? 28.198 33.356  14.964 1.00 16.16 ? 720  GLU   A N   1 
ATOM   2252 C  CA  . GLU   A 1 279 ? 27.216 32.350  14.585 1.00 17.86 ? 720  GLU   A CA  1 
ATOM   2253 C  C   . GLU   A 1 279 ? 26.199 32.125  15.698 1.00 16.18 ? 720  GLU   A C   1 
ATOM   2254 O  O   . GLU   A 1 279 ? 25.019 31.879  15.418 1.00 18.00 ? 720  GLU   A O   1 
ATOM   2255 C  CB  . GLU   A 1 279 ? 27.933 31.050  14.212 1.00 20.36 ? 720  GLU   A CB  1 
ATOM   2256 C  CG  . GLU   A 1 279 ? 28.830 31.158  12.968 1.00 23.93 ? 720  GLU   A CG  1 
ATOM   2257 C  CD  . GLU   A 1 279 ? 30.185 31.797  13.255 1.00 26.88 ? 720  GLU   A CD  1 
ATOM   2258 O  OE1 . GLU   A 1 279 ? 30.593 31.853  14.438 1.00 26.91 ? 720  GLU   A OE1 1 
ATOM   2259 O  OE2 . GLU   A 1 279 ? 30.847 32.245  12.293 1.00 28.34 ? 720  GLU   A OE2 1 
ATOM   2260 N  N   . GLY   A 1 280 ? 26.638 32.210  16.956 1.00 15.36 ? 721  GLY   A N   1 
ATOM   2261 C  CA  . GLY   A 1 280 ? 25.701 32.158  18.070 1.00 17.61 ? 721  GLY   A CA  1 
ATOM   2262 C  C   . GLY   A 1 280 ? 24.645 33.247  17.999 1.00 17.41 ? 721  GLY   A C   1 
ATOM   2263 O  O   . GLY   A 1 280 ? 23.446 32.970  18.071 1.00 15.41 ? 721  GLY   A O   1 
ATOM   2264 N  N   . TYR   A 1 281 ? 25.077 34.502  17.837 1.00 16.28 ? 722  TYR   A N   1 
ATOM   2265 C  CA  . TYR   A 1 281 ? 24.120 35.596  17.688 1.00 15.10 ? 722  TYR   A CA  1 
ATOM   2266 C  C   . TYR   A 1 281 ? 23.180 35.361  16.510 1.00 14.62 ? 722  TYR   A C   1 
ATOM   2267 O  O   . TYR   A 1 281 ? 21.994 35.701  16.584 1.00 15.39 ? 722  TYR   A O   1 
ATOM   2268 C  CB  . TYR   A 1 281 ? 24.848 36.932  17.534 1.00 16.51 ? 722  TYR   A CB  1 
ATOM   2269 C  CG  . TYR   A 1 281 ? 25.494 37.422  18.811 1.00 13.90 ? 722  TYR   A CG  1 
ATOM   2270 C  CD1 . TYR   A 1 281 ? 24.728 37.869  19.876 1.00 13.67 ? 722  TYR   A CD1 1 
ATOM   2271 C  CD2 . TYR   A 1 281 ? 26.871 37.442  18.941 1.00 14.18 ? 722  TYR   A CD2 1 
ATOM   2272 C  CE1 . TYR   A 1 281 ? 25.323 38.315  21.047 1.00 13.42 ? 722  TYR   A CE1 1 
ATOM   2273 C  CE2 . TYR   A 1 281 ? 27.476 37.893  20.095 1.00 14.78 ? 722  TYR   A CE2 1 
ATOM   2274 C  CZ  . TYR   A 1 281 ? 26.703 38.322  21.145 1.00 13.75 ? 722  TYR   A CZ  1 
ATOM   2275 O  OH  . TYR   A 1 281 ? 27.346 38.760  22.272 1.00 14.62 ? 722  TYR   A OH  1 
ATOM   2276 N  N   . ALA   A 1 282 ? 23.691 34.795  15.409 1.00 13.99 ? 723  ALA   A N   1 
ATOM   2277 C  CA  . ALA   A 1 282 ? 22.826 34.501  14.269 1.00 14.08 ? 723  ALA   A CA  1 
ATOM   2278 C  C   . ALA   A 1 282 ? 21.733 33.513  14.650 1.00 15.24 ? 723  ALA   A C   1 
ATOM   2279 O  O   . ALA   A 1 282 ? 20.573 33.677  14.252 1.00 15.89 ? 723  ALA   A O   1 
ATOM   2280 C  CB  . ALA   A 1 282 ? 23.650 33.969  13.096 1.00 15.06 ? 723  ALA   A CB  1 
ATOM   2281 N  N   . HIS   A 1 283 ? 22.084 32.475  15.418 1.00 16.17 ? 724  HIS   A N   1 
ATOM   2282 C  CA  . HIS   A 1 283 ? 21.073 31.504  15.823 1.00 19.61 ? 724  HIS   A CA  1 
ATOM   2283 C  C   . HIS   A 1 283 ? 20.052 32.132  16.760 1.00 16.91 ? 724  HIS   A C   1 
ATOM   2284 O  O   . HIS   A 1 283 ? 18.850 31.856  16.654 1.00 18.58 ? 724  HIS   A O   1 
ATOM   2285 C  CB  . HIS   A 1 283 ? 21.732 30.282  16.451 1.00 22.10 ? 724  HIS   A CB  1 
ATOM   2286 C  CG  . HIS   A 1 283 ? 22.226 29.294  15.443 1.00 25.84 ? 724  HIS   A CG  1 
ATOM   2287 N  ND1 . HIS   A 1 283 ? 21.582 28.105  15.185 1.00 28.04 ? 724  HIS   A ND1 1 
ATOM   2288 C  CD2 . HIS   A 1 283 ? 23.292 29.335  14.610 1.00 26.95 ? 724  HIS   A CD2 1 
ATOM   2289 C  CE1 . HIS   A 1 283 ? 22.236 27.448  14.242 1.00 29.31 ? 724  HIS   A CE1 1 
ATOM   2290 N  NE2 . HIS   A 1 283 ? 23.279 28.172  13.878 1.00 29.05 ? 724  HIS   A NE2 1 
ATOM   2291 N  N   . LEU   A 1 284 ? 20.502 33.004  17.663 1.00 15.97 ? 725  LEU   A N   1 
ATOM   2292 C  CA  . LEU   A 1 284 ? 19.549 33.694  18.528 1.00 15.72 ? 725  LEU   A CA  1 
ATOM   2293 C  C   . LEU   A 1 284 ? 18.602 34.560  17.710 1.00 15.72 ? 725  LEU   A C   1 
ATOM   2294 O  O   . LEU   A 1 284 ? 17.388 34.562  17.948 1.00 16.37 ? 725  LEU   A O   1 
ATOM   2295 C  CB  . LEU   A 1 284 ? 20.277 34.529  19.583 1.00 14.93 ? 725  LEU   A CB  1 
ATOM   2296 C  CG  . LEU   A 1 284 ? 21.276 33.817  20.498 1.00 14.86 ? 725  LEU   A CG  1 
ATOM   2297 C  CD1 . LEU   A 1 284 ? 21.813 34.784  21.554 1.00 15.33 ? 725  LEU   A CD1 1 
ATOM   2298 C  CD2 . LEU   A 1 284 ? 20.648 32.588  21.147 1.00 16.19 ? 725  LEU   A CD2 1 
ATOM   2299 N  N   . THR   A 1 285 ? 19.134 35.299  16.733 1.00 14.26 ? 726  THR   A N   1 
ATOM   2300 C  CA  . THR   A 1 285 ? 18.279 36.124  15.879 1.00 13.37 ? 726  THR   A CA  1 
ATOM   2301 C  C   . THR   A 1 285 ? 17.252 35.276  15.145 1.00 16.69 ? 726  THR   A C   1 
ATOM   2302 O  O   . THR   A 1 285 ? 16.063 35.617  15.098 1.00 16.44 ? 726  THR   A O   1 
ATOM   2303 C  CB  . THR   A 1 285 ? 19.136 36.888  14.865 1.00 14.48 ? 726  THR   A CB  1 
ATOM   2304 O  OG1 . THR   A 1 285 ? 20.066 37.725  15.565 1.00 14.49 ? 726  THR   A OG1 1 
ATOM   2305 C  CG2 . THR   A 1 285 ? 18.259 37.751  13.967 1.00 15.49 ? 726  THR   A CG2 1 
ATOM   2306 N  N   . HIS   A 1 286 ? 17.704 34.173  14.544 1.00 16.33 ? 727  HIS   A N   1 
ATOM   2307 C  CA  . HIS   A 1 286 ? 16.811 33.335  13.754 1.00 17.98 ? 727  HIS   A CA  1 
ATOM   2308 C  C   . HIS   A 1 286 ? 15.671 32.780  14.604 1.00 16.58 ? 727  HIS   A C   1 
ATOM   2309 O  O   . HIS   A 1 286 ? 14.534 32.664  14.130 1.00 18.35 ? 727  HIS   A O   1 
ATOM   2310 C  CB  . HIS   A 1 286 ? 17.618 32.209  13.107 1.00 19.53 ? 727  HIS   A CB  1 
ATOM   2311 C  CG  . HIS   A 1 286 ? 16.821 31.360  12.170 1.00 23.81 ? 727  HIS   A CG  1 
ATOM   2312 N  ND1 . HIS   A 1 286 ? 16.567 31.725  10.866 1.00 27.91 ? 727  HIS   A ND1 1 
ATOM   2313 C  CD2 . HIS   A 1 286 ? 16.225 30.159  12.348 1.00 25.27 ? 727  HIS   A CD2 1 
ATOM   2314 C  CE1 . HIS   A 1 286 ? 15.842 30.787  10.283 1.00 30.48 ? 727  HIS   A CE1 1 
ATOM   2315 N  NE2 . HIS   A 1 286 ? 15.623 29.824  11.159 1.00 29.42 ? 727  HIS   A NE2 1 
ATOM   2316 N  N   . GLN   A 1 287 ? 15.951 32.444  15.868 1.00 16.76 ? 728  GLN   A N   1 
ATOM   2317 C  CA  . GLN   A 1 287 ? 14.891 31.980  16.758 1.00 16.83 ? 728  GLN   A CA  1 
ATOM   2318 C  C   . GLN   A 1 287 ? 13.864 33.077  17.012 1.00 18.13 ? 728  GLN   A C   1 
ATOM   2319 O  O   . GLN   A 1 287 ? 12.655 32.832  16.926 1.00 18.60 ? 728  GLN   A O   1 
ATOM   2320 C  CB  . GLN   A 1 287 ? 15.494 31.488  18.068 1.00 17.56 ? 728  GLN   A CB  1 
ATOM   2321 C  CG  . GLN   A 1 287 ? 16.245 30.173  17.917 1.00 19.86 ? 728  GLN   A CG  1 
ATOM   2322 C  CD  . GLN   A 1 287 ? 16.775 29.649  19.228 1.00 26.09 ? 728  GLN   A CD  1 
ATOM   2323 O  OE1 . GLN   A 1 287 ? 16.026 29.484  20.186 1.00 27.63 ? 728  GLN   A OE1 1 
ATOM   2324 N  NE2 . GLN   A 1 287 ? 18.069 29.370  19.277 1.00 31.25 ? 728  GLN   A NE2 1 
ATOM   2325 N  N   . LEU   A 1 288 ? 14.323 34.302  17.285 1.00 16.47 ? 729  LEU   A N   1 
ATOM   2326 C  CA  . LEU   A 1 288 ? 13.390 35.397  17.533 1.00 16.97 ? 729  LEU   A CA  1 
ATOM   2327 C  C   . LEU   A 1 288 ? 12.537 35.715  16.306 1.00 17.56 ? 729  LEU   A C   1 
ATOM   2328 O  O   . LEU   A 1 288 ? 11.402 36.189  16.449 1.00 19.35 ? 729  LEU   A O   1 
ATOM   2329 C  CB  . LEU   A 1 288 ? 14.142 36.640  18.020 1.00 16.46 ? 729  LEU   A CB  1 
ATOM   2330 C  CG  . LEU   A 1 288 ? 14.865 36.485  19.369 1.00 16.60 ? 729  LEU   A CG  1 
ATOM   2331 C  CD1 . LEU   A 1 288 ? 15.501 37.797  19.774 1.00 17.28 ? 729  LEU   A CD1 1 
ATOM   2332 C  CD2 . LEU   A 1 288 ? 13.923 35.992  20.470 1.00 17.35 ? 729  LEU   A CD2 1 
ATOM   2333 N  N   . MET   A 1 289 ? 13.050 35.450  15.097 1.00 16.37 ? 730  MET   A N   1 
ATOM   2334 C  CA  . MET   A 1 289 ? 12.286 35.726  13.885 1.00 16.31 ? 730  MET   A CA  1 
ATOM   2335 C  C   . MET   A 1 289 ? 11.038 34.859  13.762 1.00 17.16 ? 730  MET   A C   1 
ATOM   2336 O  O   . MET   A 1 289 ? 10.165 35.170  12.944 1.00 18.55 ? 730  MET   A O   1 
ATOM   2337 C  CB  . MET   A 1 289 ? 13.172 35.539  12.654 1.00 17.11 ? 730  MET   A CB  1 
ATOM   2338 C  CG  . MET   A 1 289 ? 14.281 36.566  12.519 1.00 16.80 ? 730  MET   A CG  1 
ATOM   2339 S  SD  . MET   A 1 289 ? 15.431 36.172  11.193 1.00 19.63 ? 730  MET   A SD  1 
ATOM   2340 C  CE  . MET   A 1 289 ? 14.321 36.071  9.775  1.00 17.01 ? 730  MET   A CE  1 
ATOM   2341 N  N   . SER   A 1 290 ? 10.948 33.775  14.532 1.00 18.57 ? 731  SER   A N   1 
ATOM   2342 C  CA  . SER   A 1 290 ? 9.752  32.944  14.546 1.00 22.02 ? 731  SER   A CA  1 
ATOM   2343 C  C   . SER   A 1 290 ? 8.616  33.557  15.355 1.00 27.09 ? 731  SER   A C   1 
ATOM   2344 O  O   . SER   A 1 290 ? 7.518  32.989  15.376 1.00 24.71 ? 731  SER   A O   1 
ATOM   2345 C  CB  . SER   A 1 290 ? 10.084 31.534  15.051 1.00 20.93 ? 731  SER   A CB  1 
ATOM   2346 O  OG  . SER   A 1 290 ? 10.371 31.524  16.444 1.00 21.23 ? 731  SER   A OG  1 
ATOM   2347 N  N   . LEU   A 1 291 ? 8.845  34.701  15.993 1.00 21.90 ? 732  LEU   A N   1 
ATOM   2348 C  CA  . LEU   A 1 291 ? 7.851  35.388  16.802 1.00 16.68 ? 732  LEU   A CA  1 
ATOM   2349 C  C   . LEU   A 1 291 ? 7.304  36.601  16.066 1.00 19.31 ? 732  LEU   A C   1 
ATOM   2350 O  O   . LEU   A 1 291 ? 7.922  37.122  15.132 1.00 21.77 ? 732  LEU   A O   1 
ATOM   2351 C  CB  . LEU   A 1 291 ? 8.466  35.861  18.121 1.00 17.80 ? 732  LEU   A CB  1 
ATOM   2352 C  CG  . LEU   A 1 291 ? 9.187  34.813  18.957 1.00 18.17 ? 732  LEU   A CG  1 
ATOM   2353 C  CD1 . LEU   A 1 291 ? 10.097 35.481  19.989 1.00 18.37 ? 732  LEU   A CD1 1 
ATOM   2354 C  CD2 . LEU   A 1 291 ? 8.162  33.900  19.627 1.00 20.98 ? 732  LEU   A CD2 1 
ATOM   2355 N  N   . ALA   A 1 292 ? 6.111  37.032  16.494 1.00 18.84 ? 733  ALA   A N   1 
ATOM   2356 C  CA  . ALA   A 1 292 ? 5.499  38.287  16.049 1.00 18.09 ? 733  ALA   A CA  1 
ATOM   2357 C  C   . ALA   A 1 292 ? 5.394  38.381  14.528 1.00 17.39 ? 733  ALA   A C   1 
ATOM   2358 O  O   . ALA   A 1 292 ? 5.496  39.464  13.950 1.00 17.69 ? 733  ALA   A O   1 
ATOM   2359 C  CB  . ALA   A 1 292 ? 6.213  39.506  16.643 1.00 15.92 ? 733  ALA   A CB  1 
ATOM   2360 N  N   . ALA   A 1 293 ? 5.172  37.242  13.874 1.00 17.46 ? 734  ALA   A N   1 
ATOM   2361 C  CA  . ALA   A 1 293 ? 5.116  37.182  12.416 1.00 19.40 ? 734  ALA   A CA  1 
ATOM   2362 C  C   . ALA   A 1 293 ? 6.375  37.759  11.777 1.00 20.22 ? 734  ALA   A C   1 
ATOM   2363 O  O   . ALA   A 1 293 ? 6.327  38.317  10.676 1.00 21.29 ? 734  ALA   A O   1 
ATOM   2364 C  CB  . ALA   A 1 293 ? 3.856  37.850  11.856 1.00 19.94 ? 734  ALA   A CB  1 
ATOM   2365 N  N   . GLY   A 1 294 ? 7.498  37.651  12.487 1.00 20.10 ? 735  GLY   A N   1 
ATOM   2366 C  CA  . GLY   A 1 294 ? 8.778  38.129  12.007 1.00 18.59 ? 735  GLY   A CA  1 
ATOM   2367 C  C   . GLY   A 1 294 ? 9.079  39.589  12.266 1.00 16.68 ? 735  GLY   A C   1 
ATOM   2368 O  O   . GLY   A 1 294 ? 10.112 40.078  11.792 1.00 16.81 ? 735  GLY   A O   1 
ATOM   2369 N  N   . ARG   A 1 295 ? 8.228  40.299  13.003 1.00 15.52 ? 736  ARG   A N   1 
ATOM   2370 C  CA  . ARG   A 1 295 ? 8.414  41.728  13.253 1.00 15.87 ? 736  ARG   A CA  1 
ATOM   2371 C  C   . ARG   A 1 295 ? 9.438  41.919  14.364 1.00 16.22 ? 736  ARG   A C   1 
ATOM   2372 O  O   . ARG   A 1 295 ? 9.096  42.016  15.549 1.00 17.19 ? 736  ARG   A O   1 
ATOM   2373 C  CB  . ARG   A 1 295 ? 7.078  42.380  13.582 1.00 15.45 ? 736  ARG   A CB  1 
ATOM   2374 C  CG  . ARG   A 1 295 ? 6.123  42.365  12.400 1.00 20.75 ? 736  ARG   A CG  1 
ATOM   2375 C  CD  . ARG   A 1 295 ? 4.819  43.081  12.716 1.00 31.62 ? 736  ARG   A CD  1 
ATOM   2376 N  NE  . ARG   A 1 295 ? 4.216  43.641  11.508 1.00 36.44 ? 736  ARG   A NE  1 
ATOM   2377 C  CZ  . ARG   A 1 295 ? 3.072  44.320  11.478 1.00 39.04 ? 736  ARG   A CZ  1 
ATOM   2378 N  NH1 . ARG   A 1 295 ? 2.386  44.529  12.593 1.00 38.85 ? 736  ARG   A NH1 1 
ATOM   2379 N  NH2 . ARG   A 1 295 ? 2.613  44.788  10.325 1.00 40.32 ? 736  ARG   A NH2 1 
ATOM   2380 N  N   . VAL   A 1 296 ? 10.707 41.997  13.958 1.00 14.02 ? 737  VAL   A N   1 
ATOM   2381 C  CA  . VAL   A 1 296 ? 11.851 42.073  14.862 1.00 14.30 ? 737  VAL   A CA  1 
ATOM   2382 C  C   . VAL   A 1 296 ? 12.660 43.322  14.530 1.00 14.60 ? 737  VAL   A C   1 
ATOM   2383 O  O   . VAL   A 1 296 ? 13.012 43.546  13.364 1.00 14.41 ? 737  VAL   A O   1 
ATOM   2384 C  CB  . VAL   A 1 296 ? 12.747 40.828  14.722 1.00 14.70 ? 737  VAL   A CB  1 
ATOM   2385 C  CG1 . VAL   A 1 296 ? 13.993 40.978  15.579 1.00 14.91 ? 737  VAL   A CG1 1 
ATOM   2386 C  CG2 . VAL   A 1 296 ? 11.982 39.558  15.077 1.00 17.69 ? 737  VAL   A CG2 1 
ATOM   2387 N  N   . LEU   A 1 297 ? 12.987 44.115  15.554 1.00 12.71 ? 738  LEU   A N   1 
ATOM   2388 C  CA  . LEU   A 1 297 ? 13.893 45.255  15.414 1.00 13.21 ? 738  LEU   A CA  1 
ATOM   2389 C  C   . LEU   A 1 297 ? 15.106 45.035  16.310 1.00 12.29 ? 738  LEU   A C   1 
ATOM   2390 O  O   . LEU   A 1 297 ? 14.963 44.918  17.529 1.00 12.97 ? 738  LEU   A O   1 
ATOM   2391 C  CB  . LEU   A 1 297 ? 13.171 46.552  15.792 1.00 13.45 ? 738  LEU   A CB  1 
ATOM   2392 C  CG  . LEU   A 1 297 ? 14.011 47.834  15.884 1.00 14.08 ? 738  LEU   A CG  1 
ATOM   2393 C  CD1 . LEU   A 1 297 ? 14.849 48.034  14.635 1.00 16.35 ? 738  LEU   A CD1 1 
ATOM   2394 C  CD2 . LEU   A 1 297 ? 13.113 49.037  16.112 1.00 15.96 ? 738  LEU   A CD2 1 
ATOM   2395 N  N   . ILE   A 1 298 ? 16.294 44.970  15.711 1.00 11.41 ? 739  ILE   A N   1 
ATOM   2396 C  CA  . ILE   A 1 298 ? 17.538 44.749  16.447 1.00 12.60 ? 739  ILE   A CA  1 
ATOM   2397 C  C   . ILE   A 1 298 ? 18.189 46.104  16.699 1.00 12.39 ? 739  ILE   A C   1 
ATOM   2398 O  O   . ILE   A 1 298 ? 18.537 46.816  15.753 1.00 14.20 ? 739  ILE   A O   1 
ATOM   2399 C  CB  . ILE   A 1 298 ? 18.477 43.806  15.676 1.00 12.71 ? 739  ILE   A CB  1 
ATOM   2400 C  CG1 . ILE   A 1 298 ? 17.799 42.452  15.465 1.00 15.09 ? 739  ILE   A CG1 1 
ATOM   2401 C  CG2 . ILE   A 1 298 ? 19.810 43.638  16.396 1.00 13.66 ? 739  ILE   A CG2 1 
ATOM   2402 C  CD1 . ILE   A 1 298 ? 18.638 41.461  14.705 1.00 15.74 ? 739  ILE   A CD1 1 
ATOM   2403 N  N   . ILE   A 1 299 ? 18.373 46.457  17.972 1.00 11.75 ? 740  ILE   A N   1 
ATOM   2404 C  CA  . ILE   A 1 299 ? 18.870 47.776  18.382 1.00 12.40 ? 740  ILE   A CA  1 
ATOM   2405 C  C   . ILE   A 1 299 ? 20.236 47.608  19.053 1.00 12.12 ? 740  ILE   A C   1 
ATOM   2406 O  O   . ILE   A 1 299 ? 20.339 46.923  20.079 1.00 13.05 ? 740  ILE   A O   1 
ATOM   2407 C  CB  . ILE   A 1 299 ? 17.890 48.457  19.355 1.00 13.20 ? 740  ILE   A CB  1 
ATOM   2408 C  CG1 . ILE   A 1 299 ? 16.500 48.611  18.715 1.00 13.08 ? 740  ILE   A CG1 1 
ATOM   2409 C  CG2 . ILE   A 1 299 ? 18.421 49.821  19.804 1.00 14.97 ? 740  ILE   A CG2 1 
ATOM   2410 C  CD1 . ILE   A 1 299 ? 15.440 49.138  19.661 1.00 15.76 ? 740  ILE   A CD1 1 
ATOM   2411 N  N   . LEU   A 1 300 ? 21.266 48.271  18.519 1.00 11.93 ? 741  LEU   A N   1 
ATOM   2412 C  CA  . LEU   A 1 300 ? 22.590 48.177  19.130 1.00 12.22 ? 741  LEU   A CA  1 
ATOM   2413 C  C   . LEU   A 1 300 ? 22.573 48.771  20.535 1.00 13.56 ? 741  LEU   A C   1 
ATOM   2414 O  O   . LEU   A 1 300 ? 22.078 49.885  20.738 1.00 14.75 ? 741  LEU   A O   1 
ATOM   2415 C  CB  . LEU   A 1 300 ? 23.620 48.919  18.278 1.00 12.93 ? 741  LEU   A CB  1 
ATOM   2416 C  CG  . LEU   A 1 300 ? 25.072 48.855  18.786 1.00 13.02 ? 741  LEU   A CG  1 
ATOM   2417 C  CD1 . LEU   A 1 300 ? 25.579 47.430  18.781 1.00 13.68 ? 741  LEU   A CD1 1 
ATOM   2418 C  CD2 . LEU   A 1 300 ? 25.951 49.753  17.942 1.00 14.49 ? 741  LEU   A CD2 1 
ATOM   2419 N  N   . GLU   A 1 301 ? 23.098 48.012  21.509 1.00 13.19 ? 742  GLU   A N   1 
ATOM   2420 C  CA  . GLU   A 1 301 ? 23.366 48.523  22.850 1.00 12.67 ? 742  GLU   A CA  1 
ATOM   2421 C  C   . GLU   A 1 301 ? 24.878 48.625  23.024 1.00 13.60 ? 742  GLU   A C   1 
ATOM   2422 O  O   . GLU   A 1 301 ? 25.515 49.435  22.345 1.00 13.91 ? 742  GLU   A O   1 
ATOM   2423 C  CB  . GLU   A 1 301 ? 22.684 47.652  23.912 1.00 13.59 ? 742  GLU   A CB  1 
ATOM   2424 C  CG  . GLU   A 1 301 ? 21.129 47.631  23.801 1.00 13.35 ? 742  GLU   A CG  1 
ATOM   2425 C  CD  . GLU   A 1 301 ? 20.433 48.832  24.468 1.00 17.86 ? 742  GLU   A CD  1 
ATOM   2426 O  OE1 . GLU   A 1 301 ? 21.106 49.799  24.867 1.00 18.86 ? 742  GLU   A OE1 1 
ATOM   2427 O  OE2 . GLU   A 1 301 ? 19.193 48.816  24.594 1.00 15.45 ? 742  GLU   A OE2 1 
ATOM   2428 N  N   . GLY   A 1 302 ? 25.461 47.803  23.897 1.00 15.75 ? 743  GLY   A N   1 
ATOM   2429 C  CA  . GLY   A 1 302 ? 26.893 47.793  24.122 1.00 14.79 ? 743  GLY   A CA  1 
ATOM   2430 C  C   . GLY   A 1 302 ? 27.646 46.875  23.180 1.00 16.14 ? 743  GLY   A C   1 
ATOM   2431 O  O   . GLY   A 1 302 ? 27.145 46.470  22.129 1.00 16.43 ? 743  GLY   A O   1 
ATOM   2432 N  N   . GLY   A 1 303 ? 28.887 46.555  23.561 1.00 17.60 ? 744  GLY   A N   1 
ATOM   2433 C  CA  . GLY   A 1 303 ? 29.773 45.801  22.689 1.00 14.73 ? 744  GLY   A CA  1 
ATOM   2434 C  C   . GLY   A 1 303 ? 30.966 46.648  22.292 1.00 15.26 ? 744  GLY   A C   1 
ATOM   2435 O  O   . GLY   A 1 303 ? 30.808 47.693  21.651 1.00 16.27 ? 744  GLY   A O   1 
ATOM   2436 N  N   . TYR   A 1 304 ? 32.174 46.200  22.643 1.00 15.21 ? 745  TYR   A N   1 
ATOM   2437 C  CA  . TYR   A 1 304 ? 33.337 47.078  22.638 1.00 13.19 ? 745  TYR   A CA  1 
ATOM   2438 C  C   . TYR   A 1 304 ? 34.556 46.560  21.889 1.00 14.28 ? 745  TYR   A C   1 
ATOM   2439 O  O   . TYR   A 1 304 ? 35.531 47.310  21.755 1.00 17.87 ? 745  TYR   A O   1 
ATOM   2440 C  CB  . TYR   A 1 304 ? 33.696 47.484  24.076 1.00 13.77 ? 745  TYR   A CB  1 
ATOM   2441 C  CG  . TYR   A 1 304 ? 32.458 48.024  24.723 1.00 15.05 ? 745  TYR   A CG  1 
ATOM   2442 C  CD1 . TYR   A 1 304 ? 31.980 49.273  24.357 1.00 17.20 ? 745  TYR   A CD1 1 
ATOM   2443 C  CD2 . TYR   A 1 304 ? 31.718 47.263  25.637 1.00 14.52 ? 745  TYR   A CD2 1 
ATOM   2444 C  CE1 . TYR   A 1 304 ? 30.824 49.779  24.906 1.00 16.30 ? 745  TYR   A CE1 1 
ATOM   2445 C  CE2 . TYR   A 1 304 ? 30.548 47.765  26.191 1.00 15.33 ? 745  TYR   A CE2 1 
ATOM   2446 C  CZ  . TYR   A 1 304 ? 30.109 49.021  25.816 1.00 16.20 ? 745  TYR   A CZ  1 
ATOM   2447 O  OH  . TYR   A 1 304 ? 28.950 49.544  26.350 1.00 19.18 ? 745  TYR   A OH  1 
ATOM   2448 N  N   . ASN   A 1 305 ? 34.540 45.326  21.389 1.00 12.44 ? 746  ASN   A N   1 
ATOM   2449 C  CA  . ASN   A 1 305 ? 35.553 44.884  20.439 1.00 13.22 ? 746  ASN   A CA  1 
ATOM   2450 C  C   . ASN   A 1 305 ? 35.018 45.201  19.045 1.00 15.18 ? 746  ASN   A C   1 
ATOM   2451 O  O   . ASN   A 1 305 ? 34.042 44.591  18.594 1.00 15.02 ? 746  ASN   A O   1 
ATOM   2452 C  CB  . ASN   A 1 305 ? 35.873 43.403  20.628 1.00 13.19 ? 746  ASN   A CB  1 
ATOM   2453 C  CG  . ASN   A 1 305 ? 36.934 42.896  19.661 1.00 14.77 ? 746  ASN   A CG  1 
ATOM   2454 O  OD1 . ASN   A 1 305 ? 36.869 43.132  18.447 1.00 14.99 ? 746  ASN   A OD1 1 
ATOM   2455 N  ND2 . ASN   A 1 305 ? 37.926 42.189  20.202 1.00 14.61 ? 746  ASN   A ND2 1 
ATOM   2456 N  N   . LEU   A 1 306 ? 35.638 46.181  18.385 1.00 14.09 ? 747  LEU   A N   1 
ATOM   2457 C  CA  . LEU   A 1 306 ? 35.114 46.688  17.120 1.00 13.15 ? 747  LEU   A CA  1 
ATOM   2458 C  C   . LEU   A 1 306 ? 34.975 45.573  16.094 1.00 13.23 ? 747  LEU   A C   1 
ATOM   2459 O  O   . LEU   A 1 306 ? 33.975 45.509  15.372 1.00 13.30 ? 747  LEU   A O   1 
ATOM   2460 C  CB  . LEU   A 1 306 ? 36.019 47.801  16.599 1.00 15.22 ? 747  LEU   A CB  1 
ATOM   2461 C  CG  . LEU   A 1 306 ? 36.127 49.035  17.497 1.00 16.31 ? 747  LEU   A CG  1 
ATOM   2462 C  CD1 . LEU   A 1 306 ? 37.178 49.981  16.945 1.00 16.25 ? 747  LEU   A CD1 1 
ATOM   2463 C  CD2 . LEU   A 1 306 ? 34.773 49.729  17.601 1.00 17.40 ? 747  LEU   A CD2 1 
ATOM   2464 N  N   . THR   A 1 307 ? 35.949 44.662  16.034 1.00 13.17 ? 748  THR   A N   1 
ATOM   2465 C  CA  . THR   A 1 307 ? 35.837 43.545  15.099 1.00 14.05 ? 748  THR   A CA  1 
ATOM   2466 C  C   . THR   A 1 307 ? 34.709 42.596  15.497 1.00 13.75 ? 748  THR   A C   1 
ATOM   2467 O  O   . THR   A 1 307 ? 33.899 42.189  14.652 1.00 15.92 ? 748  THR   A O   1 
ATOM   2468 C  CB  . THR   A 1 307 ? 37.186 42.831  15.005 1.00 16.53 ? 748  THR   A CB  1 
ATOM   2469 O  OG1 . THR   A 1 307 ? 38.150 43.729  14.440 1.00 15.72 ? 748  THR   A OG1 1 
ATOM   2470 C  CG2 . THR   A 1 307 ? 37.103 41.575  14.139 1.00 17.29 ? 748  THR   A CG2 1 
ATOM   2471 N  N   . SER   A 1 308 ? 34.615 42.264  16.787 1.00 14.99 ? 749  SER   A N   1 
ATOM   2472 C  CA  . SER   A 1 308 ? 33.590 41.330  17.250 1.00 14.96 ? 749  SER   A CA  1 
ATOM   2473 C  C   . SER   A 1 308 ? 32.184 41.868  17.017 1.00 13.74 ? 749  SER   A C   1 
ATOM   2474 O  O   . SER   A 1 308 ? 31.297 41.130  16.567 1.00 15.62 ? 749  SER   A O   1 
ATOM   2475 C  CB  . SER   A 1 308 ? 33.779 41.027  18.733 1.00 16.59 ? 749  SER   A CB  1 
ATOM   2476 O  OG  . SER   A 1 308 ? 35.060 40.474  19.002 1.00 18.11 ? 749  SER   A OG  1 
ATOM   2477 N  N   . ILE   A 1 309 ? 31.940 43.134  17.370 1.00 12.65 ? 750  ILE   A N   1 
ATOM   2478 C  CA  . ILE   A 1 309 ? 30.589 43.676  17.210 1.00 12.30 ? 750  ILE   A CA  1 
ATOM   2479 C  C   . ILE   A 1 309 ? 30.217 43.784  15.738 1.00 12.91 ? 750  ILE   A C   1 
ATOM   2480 O  O   . ILE   A 1 309 ? 29.059 43.560  15.362 1.00 15.53 ? 750  ILE   A O   1 
ATOM   2481 C  CB  . ILE   A 1 309 ? 30.389 45.000  17.975 1.00 12.82 ? 750  ILE   A CB  1 
ATOM   2482 C  CG1 . ILE   A 1 309 ? 31.139 46.159  17.313 1.00 13.50 ? 750  ILE   A CG1 1 
ATOM   2483 C  CG2 . ILE   A 1 309 ? 30.809 44.851  19.439 1.00 13.97 ? 750  ILE   A CG2 1 
ATOM   2484 C  CD1 . ILE   A 1 309 ? 30.915 47.485  17.983 1.00 14.28 ? 750  ILE   A CD1 1 
ATOM   2485 N  N   . SER   A 1 310 ? 31.188 44.099  14.880 1.00 12.14 ? 751  SER   A N   1 
ATOM   2486 C  CA  . SER   A 1 310 ? 30.924 44.238  13.453 1.00 12.84 ? 751  SER   A CA  1 
ATOM   2487 C  C   . SER   A 1 310 ? 30.543 42.900  12.838 1.00 12.56 ? 751  SER   A C   1 
ATOM   2488 O  O   . SER   A 1 310 ? 29.589 42.810  12.053 1.00 14.03 ? 751  SER   A O   1 
ATOM   2489 C  CB  . SER   A 1 310 ? 32.159 44.815  12.767 1.00 14.41 ? 751  SER   A CB  1 
ATOM   2490 O  OG  . SER   A 1 310 ? 32.360 46.155  13.184 1.00 15.36 ? 751  SER   A OG  1 
ATOM   2491 N  N   . GLU   A 1 311 ? 31.291 41.847  13.167 1.00 12.89 ? 752  GLU   A N   1 
ATOM   2492 C  CA  . GLU   A 1 311 ? 30.955 40.519  12.674 1.00 14.55 ? 752  GLU   A CA  1 
ATOM   2493 C  C   . GLU   A 1 311 ? 29.636 40.034  13.263 1.00 13.11 ? 752  GLU   A C   1 
ATOM   2494 O  O   . GLU   A 1 311 ? 28.791 39.485  12.545 1.00 15.27 ? 752  GLU   A O   1 
ATOM   2495 C  CB  . GLU   A 1 311 ? 32.088 39.548  12.996 1.00 19.04 ? 752  GLU   A CB  1 
ATOM   2496 C  CG  . GLU   A 1 311 ? 32.021 38.222  12.244 1.00 31.49 ? 752  GLU   A CG  1 
ATOM   2497 C  CD  . GLU   A 1 311 ? 32.091 38.383  10.736 1.00 39.04 ? 752  GLU   A CD  1 
ATOM   2498 O  OE1 . GLU   A 1 311 ? 32.755 39.326  10.265 1.00 31.35 ? 752  GLU   A OE1 1 
ATOM   2499 O  OE2 . GLU   A 1 311 ? 31.493 37.553  10.024 1.00 41.97 ? 752  GLU   A OE2 1 
ATOM   2500 N  N   . SER   A 1 312 ? 29.424 40.260  14.560 1.00 13.12 ? 753  SER   A N   1 
ATOM   2501 C  CA  . SER   A 1 312 ? 28.238 39.724  15.220 1.00 14.23 ? 753  SER   A CA  1 
ATOM   2502 C  C   . SER   A 1 312 ? 26.966 40.396  14.712 1.00 12.00 ? 753  SER   A C   1 
ATOM   2503 O  O   . SER   A 1 312 ? 25.995 39.722  14.349 1.00 14.46 ? 753  SER   A O   1 
ATOM   2504 C  CB  . SER   A 1 312 ? 28.353 39.868  16.738 1.00 15.34 ? 753  SER   A CB  1 
ATOM   2505 O  OG  . SER   A 1 312 ? 29.458 39.129  17.227 1.00 16.39 ? 753  SER   A OG  1 
ATOM   2506 N  N   . MET   A 1 313 ? 26.944 41.728  14.672 1.00 12.75 ? 754  MET   A N   1 
ATOM   2507 C  CA  . MET   A 1 313 ? 25.726 42.387  14.212 1.00 13.65 ? 754  MET   A CA  1 
ATOM   2508 C  C   . MET   A 1 313 ? 25.451 42.113  12.739 1.00 13.26 ? 754  MET   A C   1 
ATOM   2509 O  O   . MET   A 1 313 ? 24.292 41.951  12.349 1.00 13.56 ? 754  MET   A O   1 
ATOM   2510 C  CB  . MET   A 1 313 ? 25.735 43.883  14.522 1.00 14.32 ? 754  MET   A CB  1 
ATOM   2511 C  CG  . MET   A 1 313 ? 24.349 44.503  14.420 1.00 15.07 ? 754  MET   A CG  1 
ATOM   2512 S  SD  . MET   A 1 313 ? 24.287 46.185  15.026 1.00 24.69 ? 754  MET   A SD  1 
ATOM   2513 C  CE  . MET   A 1 313 ? 22.592 46.340  15.585 1.00 16.16 ? 754  MET   A CE  1 
ATOM   2514 N  N   A SER   A 1 314 ? 26.499 41.992  11.914 0.45 11.08 ? 755  SER   A N   1 
ATOM   2515 N  N   B SER   A 1 314 ? 26.492 42.120  11.898 0.55 13.90 ? 755  SER   A N   1 
ATOM   2516 C  CA  A SER   A 1 314 ? 26.296 41.626  10.511 0.45 11.31 ? 755  SER   A CA  1 
ATOM   2517 C  CA  B SER   A 1 314 ? 26.272 41.902  10.470 0.55 13.80 ? 755  SER   A CA  1 
ATOM   2518 C  C   A SER   A 1 314 ? 25.672 40.241  10.389 0.45 10.82 ? 755  SER   A C   1 
ATOM   2519 C  C   B SER   A 1 314 ? 25.681 40.526  10.209 0.55 14.42 ? 755  SER   A C   1 
ATOM   2520 O  O   A SER   A 1 314 ? 24.778 40.023  9.562  0.45 10.90 ? 755  SER   A O   1 
ATOM   2521 O  O   B SER   A 1 314 ? 24.864 40.365  9.295  0.55 16.63 ? 755  SER   A O   1 
ATOM   2522 C  CB  A SER   A 1 314 ? 27.621 41.684  9.744  0.45 10.30 ? 755  SER   A CB  1 
ATOM   2523 C  CB  B SER   A 1 314 ? 27.562 42.125  9.667  0.55 14.29 ? 755  SER   A CB  1 
ATOM   2524 O  OG  A SER   A 1 314 ? 28.139 43.002  9.702  0.45 11.15 ? 755  SER   A OG  1 
ATOM   2525 O  OG  B SER   A 1 314 ? 28.587 41.236  10.074 0.55 19.41 ? 755  SER   A OG  1 
ATOM   2526 N  N   A MET   A 1 315 ? 26.111 39.296  11.223 0.45 10.35 ? 756  MET   A N   1 
ATOM   2527 N  N   B MET   A 1 315 ? 26.042 39.533  11.027 0.55 13.22 ? 756  MET   A N   1 
ATOM   2528 C  CA  A MET   A 1 315 ? 25.515 37.965  11.203 0.45 13.09 ? 756  MET   A CA  1 
ATOM   2529 C  CA  B MET   A 1 315 ? 25.430 38.216  10.891 0.55 15.99 ? 756  MET   A CA  1 
ATOM   2530 C  C   A MET   A 1 315 ? 24.035 38.007  11.567 0.45 14.40 ? 756  MET   A C   1 
ATOM   2531 C  C   B MET   A 1 315 ? 23.966 38.232  11.325 0.55 13.80 ? 756  MET   A C   1 
ATOM   2532 O  O   A MET   A 1 315 ? 23.253 37.171  11.097 0.45 13.80 ? 756  MET   A O   1 
ATOM   2533 O  O   B MET   A 1 315 ? 23.127 37.572  10.700 0.55 13.17 ? 756  MET   A O   1 
ATOM   2534 C  CB  A MET   A 1 315 ? 26.281 37.035  12.142 0.45 20.17 ? 756  MET   A CB  1 
ATOM   2535 C  CB  B MET   A 1 315 ? 26.232 37.160  11.656 0.55 18.59 ? 756  MET   A CB  1 
ATOM   2536 C  CG  A MET   A 1 315 ? 26.499 35.638  11.579 0.45 27.13 ? 756  MET   A CG  1 
ATOM   2537 C  CG  B MET   A 1 315 ? 26.301 35.809  10.929 0.55 23.69 ? 756  MET   A CG  1 
ATOM   2538 S  SD  A MET   A 1 315 ? 27.234 35.651  9.934  0.45 30.30 ? 756  MET   A SD  1 
ATOM   2539 S  SD  B MET   A 1 315 ? 27.538 34.666  11.573 0.55 28.41 ? 756  MET   A SD  1 
ATOM   2540 C  CE  A MET   A 1 315 ? 25.928 34.876  8.979  0.45 31.03 ? 756  MET   A CE  1 
ATOM   2541 C  CE  B MET   A 1 315 ? 28.930 34.979  10.485 0.55 27.15 ? 756  MET   A CE  1 
ATOM   2542 N  N   . CYS   A 1 316 ? 23.629 38.976  12.389 1.00 14.19 ? 757  CYS   A N   1 
ATOM   2543 C  CA  . CYS   A 1 316 ? 22.220 39.124  12.730 1.00 14.46 ? 757  CYS   A CA  1 
ATOM   2544 C  C   . CYS   A 1 316 ? 21.437 39.679  11.555 1.00 14.14 ? 757  CYS   A C   1 
ATOM   2545 O  O   . CYS   A 1 316 ? 20.338 39.196  11.260 1.00 13.95 ? 757  CYS   A O   1 
ATOM   2546 C  CB  . CYS   A 1 316 ? 22.027 40.014  13.960 1.00 14.76 ? 757  CYS   A CB  1 
ATOM   2547 S  SG  . CYS   A 1 316 ? 22.769 39.360  15.497 1.00 15.25 ? 757  CYS   A SG  1 
ATOM   2548 N  N   . THR   A 1 317 ? 21.977 40.697  10.883 1.00 12.46 ? 758  THR   A N   1 
ATOM   2549 C  CA  . THR   A 1 317 ? 21.299 41.249  9.715  1.00 13.09 ? 758  THR   A CA  1 
ATOM   2550 C  C   . THR   A 1 317 ? 21.151 40.202  8.620  1.00 14.48 ? 758  THR   A C   1 
ATOM   2551 O  O   . THR   A 1 317 ? 20.103 40.121  7.973  1.00 15.62 ? 758  THR   A O   1 
ATOM   2552 C  CB  . THR   A 1 317 ? 22.040 42.483  9.203  1.00 12.76 ? 758  THR   A CB  1 
ATOM   2553 O  OG1 . THR   A 1 317 ? 22.153 43.443  10.260 1.00 13.83 ? 758  THR   A OG1 1 
ATOM   2554 C  CG2 . THR   A 1 317 ? 21.287 43.119  8.036  1.00 12.27 ? 758  THR   A CG2 1 
ATOM   2555 N  N   . SER   A 1 318 ? 22.185 39.385  8.407  1.00 13.59 ? 759  SER   A N   1 
ATOM   2556 C  CA  . SER   A 1 318 ? 22.090 38.299  7.436  1.00 15.77 ? 759  SER   A CA  1 
ATOM   2557 C  C   . SER   A 1 318 ? 20.912 37.380  7.746  1.00 16.46 ? 759  SER   A C   1 
ATOM   2558 O  O   . SER   A 1 318 ? 20.198 36.943  6.834  1.00 16.82 ? 759  SER   A O   1 
ATOM   2559 C  CB  . SER   A 1 318 ? 23.407 37.526  7.421  1.00 17.38 ? 759  SER   A CB  1 
ATOM   2560 O  OG  . SER   A 1 318 ? 23.300 36.371  6.615  1.00 21.22 ? 759  SER   A OG  1 
ATOM   2561 N  N   . MET   A 1 319 ? 20.662 37.113  9.032  1.00 13.94 ? 760  MET   A N   1 
ATOM   2562 C  CA  . MET   A 1 319 ? 19.512 36.293  9.413  1.00 15.28 ? 760  MET   A CA  1 
ATOM   2563 C  C   . MET   A 1 319 ? 18.201 36.998  9.093  1.00 15.82 ? 760  MET   A C   1 
ATOM   2564 O  O   . MET   A 1 319 ? 17.292 36.393  8.518  1.00 16.31 ? 760  MET   A O   1 
ATOM   2565 C  CB  . MET   A 1 319 ? 19.587 35.921  10.897 1.00 15.21 ? 760  MET   A CB  1 
ATOM   2566 C  CG  . MET   A 1 319 ? 20.775 35.056  11.235 1.00 15.26 ? 760  MET   A CG  1 
ATOM   2567 S  SD  . MET   A 1 319 ? 20.844 33.483  10.357 1.00 18.79 ? 760  MET   A SD  1 
ATOM   2568 C  CE  . MET   A 1 319 ? 21.990 33.883  9.029  1.00 18.75 ? 760  MET   A CE  1 
ATOM   2569 N  N   . LEU   A 1 320 ? 18.098 38.288  9.435  1.00 14.45 ? 761  LEU   A N   1 
ATOM   2570 C  CA  . LEU   A 1 320 ? 16.886 39.041  9.132  1.00 14.62 ? 761  LEU   A CA  1 
ATOM   2571 C  C   . LEU   A 1 320 ? 16.583 39.045  7.640  1.00 14.48 ? 761  LEU   A C   1 
ATOM   2572 O  O   . LEU   A 1 320 ? 15.406 39.062  7.241  1.00 15.23 ? 761  LEU   A O   1 
ATOM   2573 C  CB  . LEU   A 1 320 ? 17.006 40.482  9.637  1.00 14.84 ? 761  LEU   A CB  1 
ATOM   2574 C  CG  . LEU   A 1 320 ? 17.170 40.751  11.130 1.00 14.14 ? 761  LEU   A CG  1 
ATOM   2575 C  CD1 . LEU   A 1 320 ? 17.141 42.258  11.320 1.00 14.01 ? 761  LEU   A CD1 1 
ATOM   2576 C  CD2 . LEU   A 1 320 ? 16.036 40.085  11.905 1.00 14.13 ? 761  LEU   A CD2 1 
ATOM   2577 N  N   . LEU   A 1 321 ? 17.629 39.036  6.803  1.00 13.92 ? 762  LEU   A N   1 
ATOM   2578 C  CA  . LEU   A 1 321 ? 17.479 39.033  5.353  1.00 15.73 ? 762  LEU   A CA  1 
ATOM   2579 C  C   . LEU   A 1 321 ? 17.070 37.672  4.810  1.00 16.65 ? 762  LEU   A C   1 
ATOM   2580 O  O   . LEU   A 1 321 ? 16.812 37.559  3.603  1.00 18.66 ? 762  LEU   A O   1 
ATOM   2581 C  CB  . LEU   A 1 321 ? 18.777 39.493  4.673  1.00 15.71 ? 762  LEU   A CB  1 
ATOM   2582 C  CG  . LEU   A 1 321 ? 19.087 40.990  4.771  1.00 16.34 ? 762  LEU   A CG  1 
ATOM   2583 C  CD1 . LEU   A 1 321 ? 20.582 41.265  4.577  1.00 17.05 ? 762  LEU   A CD1 1 
ATOM   2584 C  CD2 . LEU   A 1 321 ? 18.266 41.767  3.750  1.00 16.27 ? 762  LEU   A CD2 1 
ATOM   2585 N  N   . GLY   A 1 322 ? 17.004 36.648  5.657  1.00 16.63 ? 763  GLY   A N   1 
ATOM   2586 C  CA  . GLY   A 1 322 ? 16.537 35.338  5.256  1.00 16.49 ? 763  GLY   A CA  1 
ATOM   2587 C  C   . GLY   A 1 322 ? 17.620 34.312  5.006  1.00 19.77 ? 763  GLY   A C   1 
ATOM   2588 O  O   . GLY   A 1 322 ? 17.301 33.187  4.606  1.00 21.54 ? 763  GLY   A O   1 
ATOM   2589 N  N   . ASP   A 1 323 ? 18.887 34.644  5.252  1.00 17.75 ? 764  ASP   A N   1 
ATOM   2590 C  CA  . ASP   A 1 323 ? 19.956 33.688  4.996  1.00 19.81 ? 764  ASP   A CA  1 
ATOM   2591 C  C   . ASP   A 1 323 ? 19.903 32.535  6.001  1.00 21.77 ? 764  ASP   A C   1 
ATOM   2592 O  O   . ASP   A 1 323 ? 19.406 32.678  7.119  1.00 21.55 ? 764  ASP   A O   1 
ATOM   2593 C  CB  . ASP   A 1 323 ? 21.324 34.375  5.041  1.00 19.32 ? 764  ASP   A CB  1 
ATOM   2594 C  CG  . ASP   A 1 323 ? 21.497 35.437  3.953  1.00 20.29 ? 764  ASP   A CG  1 
ATOM   2595 O  OD1 . ASP   A 1 323 ? 20.813 35.366  2.906  1.00 22.59 ? 764  ASP   A OD1 1 
ATOM   2596 O  OD2 . ASP   A 1 323 ? 22.340 36.343  4.143  1.00 19.50 ? 764  ASP   A OD2 1 
ATOM   2597 N  N   . SER   A 1 324 ? 20.414 31.379  5.586  1.00 25.81 ? 765  SER   A N   1 
ATOM   2598 C  CA  . SER   A 1 324 ? 20.342 30.194  6.430  1.00 24.99 ? 765  SER   A CA  1 
ATOM   2599 C  C   . SER   A 1 324 ? 21.314 30.323  7.601  1.00 21.26 ? 765  SER   A C   1 
ATOM   2600 O  O   . SER   A 1 324 ? 22.438 30.799  7.421  1.00 20.78 ? 765  SER   A O   1 
ATOM   2601 C  CB  . SER   A 1 324 ? 20.694 28.951  5.617  1.00 28.30 ? 765  SER   A CB  1 
ATOM   2602 O  OG  . SER   A 1 324 ? 19.692 28.678  4.653  0.53 28.58 ? 765  SER   A OG  1 
ATOM   2603 N  N   . PRO   A 1 325 ? 20.922 29.893  8.823  1.00 23.47 ? 766  PRO   A N   1 
ATOM   2604 C  CA  . PRO   A 1 325 ? 21.799 29.973  9.970  1.00 24.54 ? 766  PRO   A CA  1 
ATOM   2605 C  C   . PRO   A 1 325 ? 23.083 29.250  9.744  1.00 25.82 ? 766  PRO   A C   1 
ATOM   2606 O  O   . PRO   A 1 325 ? 23.060 28.114  9.296  1.00 28.23 ? 766  PRO   A O   1 
ATOM   2607 C  CB  . PRO   A 1 325 ? 20.996 29.318  11.086 1.00 24.24 ? 766  PRO   A CB  1 
ATOM   2608 C  CG  . PRO   A 1 325 ? 19.576 29.631  10.734 1.00 27.68 ? 766  PRO   A CG  1 
ATOM   2609 C  CD  . PRO   A 1 325 ? 19.601 29.360  9.250  1.00 28.05 ? 766  PRO   A CD  1 
ATOM   2610 N  N   . PRO   A 1 326 ? 24.221 29.896  10.021 1.00 25.46 ? 767  PRO   A N   1 
ATOM   2611 C  CA  . PRO   A 1 326 ? 25.506 29.247  9.903  1.00 26.31 ? 767  PRO   A CA  1 
ATOM   2612 C  C   . PRO   A 1 326 ? 25.702 28.172  10.950 1.00 27.53 ? 767  PRO   A C   1 
ATOM   2613 O  O   . PRO   A 1 326 ? 25.071 28.170  11.997 1.00 29.52 ? 767  PRO   A O   1 
ATOM   2614 C  CB  . PRO   A 1 326 ? 26.446 30.441  10.088 1.00 25.80 ? 767  PRO   A CB  1 
ATOM   2615 C  CG  . PRO   A 1 326 ? 25.706 31.346  11.021 1.00 26.96 ? 767  PRO   A CG  1 
ATOM   2616 C  CD  . PRO   A 1 326 ? 24.310 31.277  10.451 1.00 25.51 ? 767  PRO   A CD  1 
ATOM   2617 N  N   . SER   A 1 327 ? 26.604 27.259  10.648 1.00 28.64 ? 768  SER   A N   1 
ATOM   2618 C  CA  . SER   A 1 327 ? 26.952 26.177  11.589 1.00 34.59 ? 768  SER   A CA  1 
ATOM   2619 C  C   . SER   A 1 327 ? 27.657 26.741  12.820 1.00 32.17 ? 768  SER   A C   1 
ATOM   2620 O  O   . SER   A 1 327 ? 28.496 27.611  12.685 1.00 27.30 ? 768  SER   A O   1 
ATOM   2621 C  CB  . SER   A 1 327 ? 27.845 25.165  10.875 1.00 44.39 ? 768  SER   A CB  1 
ATOM   2622 O  OG  . SER   A 1 327 ? 27.419 24.965  9.536  1.00 50.90 ? 768  SER   A OG  1 
ATOM   2623 N  N   . LEU   A 1 328 ? 27.297 26.217  13.969 1.00 35.88 ? 769  LEU   A N   1 
ATOM   2624 C  CA  . LEU   A 1 328 ? 27.953 26.637  15.217 1.00 42.22 ? 769  LEU   A CA  1 
ATOM   2625 C  C   . LEU   A 1 328 ? 29.222 25.822  15.441 1.00 50.15 ? 769  LEU   A C   1 
ATOM   2626 O  O   . LEU   A 1 328 ? 29.346 24.744  14.860 1.00 54.44 ? 769  LEU   A O   1 
ATOM   2627 C  CB  . LEU   A 1 328 ? 27.002 26.389  16.378 1.00 40.91 ? 769  LEU   A CB  1 
ATOM   2628 C  CG  . LEU   A 1 328 ? 25.781 27.306  16.484 1.00 38.21 ? 769  LEU   A CG  1 
ATOM   2629 C  CD1 . LEU   A 1 328 ? 24.855 26.812  17.576 1.00 34.23 ? 769  LEU   A CD1 1 
ATOM   2630 C  CD2 . LEU   A 1 328 ? 26.218 28.724  16.773 1.00 39.78 ? 769  LEU   A CD2 1 
ATOM   2631 N  N   . ASP   A 1 329 ? 30.126 26.344  16.261 1.00 30.00 ? 770  ASP   A N   1 
ATOM   2632 C  CA  . ASP   A 1 329 ? 31.295 25.541  16.685 1.00 30.00 ? 770  ASP   A CA  1 
ATOM   2633 C  C   . ASP   A 1 329 ? 30.796 24.455  17.627 1.00 30.00 ? 770  ASP   A C   1 
ATOM   2634 O  O   . ASP   A 1 329 ? 29.637 24.500  18.040 1.00 30.00 ? 770  ASP   A O   1 
ATOM   2635 C  CB  . ASP   A 1 329 ? 32.333 26.402  17.381 1.00 30.00 ? 770  ASP   A CB  1 
ATOM   2636 C  CG  . ASP   A 1 329 ? 33.716 25.793  17.545 1.00 30.00 ? 770  ASP   A CG  1 
ATOM   2637 O  OD1 . ASP   A 1 329 ? 33.965 24.730  16.940 1.00 30.00 ? 770  ASP   A OD1 1 
ATOM   2638 O  OD2 . ASP   A 1 329 ? 34.528 26.395  18.278 1.00 30.00 ? 770  ASP   A OD2 1 
ATOM   2639 N  N   . HIS   A 1 330 ? 31.674 23.510  17.937 1.00 30.00 ? 771  HIS   A N   1 
ATOM   2640 C  CA  . HIS   A 1 330 ? 31.342 22.423  18.877 1.00 30.00 ? 771  HIS   A CA  1 
ATOM   2641 C  C   . HIS   A 1 330 ? 30.858 23.076  20.154 1.00 30.00 ? 771  HIS   A C   1 
ATOM   2642 O  O   . HIS   A 1 330 ? 31.531 23.997  20.645 1.00 30.00 ? 771  HIS   A O   1 
ATOM   2643 C  CB  . HIS   A 1 330 ? 32.580 21.584  19.192 1.00 30.00 ? 771  HIS   A CB  1 
ATOM   2644 C  CG  . HIS   A 1 330 ? 32.302 20.472  20.137 1.00 30.00 ? 771  HIS   A CG  1 
ATOM   2645 N  ND1 . HIS   A 1 330 ? 31.469 19.420  19.829 1.00 30.00 ? 771  HIS   A ND1 1 
ATOM   2646 C  CD2 . HIS   A 1 330 ? 32.729 20.258  21.383 1.00 30.00 ? 771  HIS   A CD2 1 
ATOM   2647 C  CE1 . HIS   A 1 330 ? 31.407 18.605  20.864 1.00 30.00 ? 771  HIS   A CE1 1 
ATOM   2648 N  NE2 . HIS   A 1 330 ? 32.171 19.094  21.816 1.00 30.00 ? 771  HIS   A NE2 1 
ATOM   2649 N  N   . LEU   A 1 331 ? 29.734 22.611  20.646 1.00 30.00 ? 772  LEU   A N   1 
ATOM   2650 C  CA  . LEU   A 1 331 ? 29.181 23.138  21.904 1.00 30.00 ? 772  LEU   A CA  1 
ATOM   2651 C  C   . LEU   A 1 331 ? 29.644 22.275  23.087 1.00 30.00 ? 772  LEU   A C   1 
ATOM   2652 O  O   . LEU   A 1 331 ? 29.197 21.127  23.173 1.00 30.00 ? 772  LEU   A O   1 
ATOM   2653 C  CB  . LEU   A 1 331 ? 27.669 23.109  21.742 1.00 30.00 ? 772  LEU   A CB  1 
ATOM   2654 C  CG  . LEU   A 1 331 ? 27.071 24.007  20.656 1.00 30.00 ? 772  LEU   A CG  1 
ATOM   2655 C  CD1 . LEU   A 1 331 ? 25.563 23.847  20.657 1.00 30.00 ? 772  LEU   A CD1 1 
ATOM   2656 C  CD2 . LEU   A 1 331 ? 27.440 25.462  20.874 1.00 30.00 ? 772  LEU   A CD2 1 
ATOM   2657 N  N   . THR   A 1 332 ? 30.478 22.824  23.959 1.00 66.77 ? 773  THR   A N   1 
ATOM   2658 C  CA  . THR   A 1 332 ? 30.854 22.096  25.184 1.00 61.27 ? 773  THR   A CA  1 
ATOM   2659 C  C   . THR   A 1 332 ? 29.635 21.829  26.032 1.00 59.59 ? 773  THR   A C   1 
ATOM   2660 O  O   . THR   A 1 332 ? 28.602 22.498  25.858 1.00 54.36 ? 773  THR   A O   1 
ATOM   2661 C  CB  . THR   A 1 332 ? 31.867 22.930  25.961 1.00 30.00 ? 773  THR   A CB  1 
ATOM   2662 O  OG1 . THR   A 1 332 ? 31.354 24.257  25.991 1.00 30.00 ? 773  THR   A OG1 1 
ATOM   2663 C  CG2 . THR   A 1 332 ? 33.239 22.918  25.315 1.00 30.00 ? 773  THR   A CG2 1 
ATOM   2664 N  N   . PRO   A 1 333 ? 29.689 20.872  26.965 1.00 57.40 ? 774  PRO   A N   1 
ATOM   2665 C  CA  . PRO   A 1 333 ? 28.596 20.671  27.879 1.00 51.83 ? 774  PRO   A CA  1 
ATOM   2666 C  C   . PRO   A 1 333 ? 28.289 21.968  28.570 1.00 47.25 ? 774  PRO   A C   1 
ATOM   2667 O  O   . PRO   A 1 333 ? 29.187 22.733  28.897 1.00 48.48 ? 774  PRO   A O   1 
ATOM   2668 C  CB  . PRO   A 1 333 ? 29.102 19.623  28.881 1.00 54.89 ? 774  PRO   A CB  1 
ATOM   2669 C  CG  . PRO   A 1 333 ? 30.572 19.492  28.573 1.00 56.48 ? 774  PRO   A CG  1 
ATOM   2670 C  CD  . PRO   A 1 333 ? 30.752 19.906  27.126 1.00 58.98 ? 774  PRO   A CD  1 
ATOM   2671 N  N   . LEU   A 1 334 ? 27.008 22.125  28.854 1.00 44.20 ? 775  LEU   A N   1 
ATOM   2672 C  CA  . LEU   A 1 334 ? 26.553 23.340  29.541 1.00 35.65 ? 775  LEU   A CA  1 
ATOM   2673 C  C   . LEU   A 1 334 ? 27.355 23.437  30.823 1.00 37.13 ? 775  LEU   A C   1 
ATOM   2674 O  O   . LEU   A 1 334 ? 27.525 22.420  31.509 1.00 39.68 ? 775  LEU   A O   1 
ATOM   2675 C  CB  . LEU   A 1 334 ? 25.044 23.314  29.803 1.00 34.92 ? 775  LEU   A CB  1 
ATOM   2676 C  CG  . LEU   A 1 334 ? 24.354 24.671  29.849 1.00 32.68 ? 775  LEU   A CG  1 
ATOM   2677 C  CD1 . LEU   A 1 334 ? 24.391 25.066  28.411 1.00 32.27 ? 775  LEU   A CD1 1 
ATOM   2678 C  CD2 . LEU   A 1 334 ? 22.929 24.488  30.323 1.00 34.46 ? 775  LEU   A CD2 1 
ATOM   2679 N  N   . LYS   A 1 335 ? 27.863 24.612  31.103 1.00 38.70 ? 776  LYS   A N   1 
ATOM   2680 C  CA  . LYS   A 1 335 ? 28.560 24.831  32.371 1.00 31.91 ? 776  LYS   A CA  1 
ATOM   2681 C  C   . LYS   A 1 335 ? 27.553 24.569  33.496 1.00 36.81 ? 776  LYS   A C   1 
ATOM   2682 O  O   . LYS   A 1 335 ? 26.401 24.989  33.444 1.00 43.33 ? 776  LYS   A O   1 
ATOM   2683 C  CB  . LYS   A 1 335 ? 29.250 26.188  32.413 1.00 31.98 ? 776  LYS   A CB  1 
ATOM   2684 C  CG  . LYS   A 1 335 ? 30.336 26.336  31.362 1.00 30.76 ? 776  LYS   A CG  1 
ATOM   2685 C  CD  . LYS   A 1 335 ? 31.162 27.608  31.477 1.00 31.28 ? 776  LYS   A CD  1 
ATOM   2686 C  CE  . LYS   A 1 335 ? 32.411 27.538  30.657 1.00 30.10 ? 776  LYS   A CE  1 
ATOM   2687 N  NZ  . LYS   A 1 335 ? 32.230 26.783  29.417 1.00 30.21 ? 776  LYS   A NZ  1 
ATOM   2688 N  N   . THR   A 1 336 ? 27.998 23.779  34.430 1.00 37.97 ? 777  THR   A N   1 
ATOM   2689 C  CA  . THR   A 1 336 ? 27.157 23.356  35.542 1.00 39.38 ? 777  THR   A CA  1 
ATOM   2690 C  C   . THR   A 1 336 ? 26.425 24.529  36.194 1.00 37.21 ? 777  THR   A C   1 
ATOM   2691 O  O   . THR   A 1 336 ? 25.242 24.417  36.539 1.00 35.20 ? 777  THR   A O   1 
ATOM   2692 C  CB  . THR   A 1 336 ? 28.022 22.563  36.523 1.00 51.78 ? 777  THR   A CB  1 
ATOM   2693 O  OG1 . THR   A 1 336 ? 28.180 21.217  36.046 1.00 45.15 ? 777  THR   A OG1 1 
ATOM   2694 C  CG2 . THR   A 1 336 ? 27.464 22.586  37.917 1.00 54.67 ? 777  THR   A CG2 1 
ATOM   2695 N  N   . SER   A 1 337 ? 27.092 25.673  36.342 1.00 35.85 ? 778  SER   A N   1 
ATOM   2696 C  CA  . SER   A 1 337 ? 26.429 26.814  36.969 1.00 32.84 ? 778  SER   A CA  1 
ATOM   2697 C  C   . SER   A 1 337 ? 25.364 27.430  36.065 1.00 28.24 ? 778  SER   A C   1 
ATOM   2698 O  O   . SER   A 1 337 ? 24.412 28.045  36.565 1.00 27.93 ? 778  SER   A O   1 
ATOM   2699 C  CB  . SER   A 1 337 ? 27.457 27.855  37.416 1.00 40.81 ? 778  SER   A CB  1 
ATOM   2700 O  OG  . SER   A 1 337 ? 26.873 29.143  37.491 1.00 46.94 ? 778  SER   A OG  1 
ATOM   2701 N  N   . ALA   A 1 338 ? 25.499 27.276  34.746 1.00 25.02 ? 779  ALA   A N   1 
ATOM   2702 C  CA  . ALA   A 1 338 ? 24.439 27.719  33.849 1.00 24.87 ? 779  ALA   A CA  1 
ATOM   2703 C  C   . ALA   A 1 338 ? 23.193 26.857  33.995 1.00 26.39 ? 779  ALA   A C   1 
ATOM   2704 O  O   . ALA   A 1 338 ? 22.066 27.355  33.854 1.00 25.22 ? 779  ALA   A O   1 
ATOM   2705 C  CB  . ALA   A 1 338 ? 24.927 27.683  32.408 1.00 22.28 ? 779  ALA   A CB  1 
ATOM   2706 N  N   . THR   A 1 339 ? 23.379 25.560  34.263 1.00 26.78 ? 780  THR   A N   1 
ATOM   2707 C  CA  . THR   A 1 339 ? 22.247 24.689  34.549 1.00 30.33 ? 780  THR   A CA  1 
ATOM   2708 C  C   . THR   A 1 339 ? 21.492 25.180  35.775 1.00 25.90 ? 780  THR   A C   1 
ATOM   2709 O  O   . THR   A 1 339 ? 20.255 25.211  35.783 1.00 26.73 ? 780  THR   A O   1 
ATOM   2710 C  CB  . THR   A 1 339 ? 22.754 23.264  34.765 1.00 30.61 ? 780  THR   A CB  1 
ATOM   2711 O  OG1 . THR   A 1 339 ? 23.288 22.763  33.535 1.00 33.75 ? 780  THR   A OG1 1 
ATOM   2712 C  CG2 . THR   A 1 339 ? 21.629 22.351  35.240 1.00 32.40 ? 780  THR   A CG2 1 
ATOM   2713 N  N   . VAL   A 1 340 ? 22.227 25.589  36.811 1.00 23.90 ? 781  VAL   A N   1 
ATOM   2714 C  CA  . VAL   A 1 340 ? 21.601 26.096  38.028 1.00 25.21 ? 781  VAL   A CA  1 
ATOM   2715 C  C   . VAL   A 1 340 ? 20.795 27.356  37.735 1.00 27.19 ? 781  VAL   A C   1 
ATOM   2716 O  O   . VAL   A 1 340 ? 19.654 27.500  38.194 1.00 26.39 ? 781  VAL   A O   1 
ATOM   2717 C  CB  . VAL   A 1 340 ? 22.666 26.328  39.116 1.00 28.46 ? 781  VAL   A CB  1 
ATOM   2718 C  CG1 . VAL   A 1 340 ? 22.055 27.014  40.330 1.00 27.13 ? 781  VAL   A CG1 1 
ATOM   2719 C  CG2 . VAL   A 1 340 ? 23.329 25.006  39.504 1.00 27.34 ? 781  VAL   A CG2 1 
ATOM   2720 N  N   . SER   A 1 341 ? 21.367 28.278  36.950 1.00 24.93 ? 782  SER   A N   1 
ATOM   2721 C  CA  . SER   A 1 341 ? 20.665 29.513  36.604 1.00 22.11 ? 782  SER   A CA  1 
ATOM   2722 C  C   . SER   A 1 341 ? 19.354 29.228  35.885 1.00 22.24 ? 782  SER   A C   1 
ATOM   2723 O  O   . SER   A 1 341 ? 18.303 29.758  36.258 1.00 21.13 ? 782  SER   A O   1 
ATOM   2724 C  CB  . SER   A 1 341 ? 21.557 30.407  35.740 1.00 21.42 ? 782  SER   A CB  1 
ATOM   2725 O  OG  . SER   A 1 341 ? 22.647 30.896  36.496 1.00 22.11 ? 782  SER   A OG  1 
ATOM   2726 N  N   . ILE   A 1 342 ? 19.405 28.412  34.826 1.00 21.19 ? 783  ILE   A N   1 
ATOM   2727 C  CA  . ILE   A 1 342 ? 18.207 28.108  34.048 1.00 22.04 ? 783  ILE   A CA  1 
ATOM   2728 C  C   . ILE   A 1 342 ? 17.143 27.464  34.926 1.00 23.15 ? 783  ILE   A C   1 
ATOM   2729 O  O   . ILE   A 1 342 ? 15.952 27.788  34.820 1.00 22.82 ? 783  ILE   A O   1 
ATOM   2730 C  CB  . ILE   A 1 342 ? 18.577 27.240  32.829 1.00 21.95 ? 783  ILE   A CB  1 
ATOM   2731 C  CG1 . ILE   A 1 342 ? 19.440 28.060  31.860 1.00 20.06 ? 783  ILE   A CG1 1 
ATOM   2732 C  CG2 . ILE   A 1 342 ? 17.333 26.669  32.161 1.00 22.75 ? 783  ILE   A CG2 1 
ATOM   2733 C  CD1 . ILE   A 1 342 ? 19.906 27.291  30.635 1.00 23.98 ? 783  ILE   A CD1 1 
ATOM   2734 N  N   . ASN   A 1 343 ? 17.551 26.552  35.815 1.00 22.32 ? 784  ASN   A N   1 
ATOM   2735 C  CA  . ASN   A 1 343 ? 16.565 25.887  36.662 1.00 26.53 ? 784  ASN   A CA  1 
ATOM   2736 C  C   . ASN   A 1 343 ? 15.972 26.850  37.686 1.00 25.90 ? 784  ASN   A C   1 
ATOM   2737 O  O   . ASN   A 1 343 ? 14.785 26.753  38.016 1.00 24.68 ? 784  ASN   A O   1 
ATOM   2738 C  CB  . ASN   A 1 343 ? 17.168 24.654  37.341 1.00 27.68 ? 784  ASN   A CB  1 
ATOM   2739 C  CG  . ASN   A 1 343 ? 17.512 23.545  36.354 1.00 31.61 ? 784  ASN   A CG  1 
ATOM   2740 O  OD1 . ASN   A 1 343 ? 16.973 23.488  35.246 1.00 32.32 ? 784  ASN   A OD1 1 
ATOM   2741 N  ND2 . ASN   A 1 343 ? 18.408 22.650  36.764 1.00 29.24 ? 784  ASN   A ND2 1 
ATOM   2742 N  N   . ASN   A 1 344 ? 16.777 27.795  38.184 1.00 24.66 ? 785  ASN   A N   1 
ATOM   2743 C  CA  . ASN   A 1 344 ? 16.253 28.811  39.095 1.00 25.43 ? 785  ASN   A CA  1 
ATOM   2744 C  C   . ASN   A 1 344 ? 15.222 29.703  38.411 1.00 23.57 ? 785  ASN   A C   1 
ATOM   2745 O  O   . ASN   A 1 344 ? 14.185 30.026  39.003 1.00 24.31 ? 785  ASN   A O   1 
ATOM   2746 C  CB  . ASN   A 1 344 ? 17.385 29.652  39.681 1.00 25.06 ? 785  ASN   A CB  1 
ATOM   2747 C  CG  . ASN   A 1 344 ? 18.174 28.911  40.747 1.00 30.49 ? 785  ASN   A CG  1 
ATOM   2748 O  OD1 . ASN   A 1 344 ? 17.644 28.031  41.422 1.00 33.99 ? 785  ASN   A OD1 1 
ATOM   2749 N  ND2 . ASN   A 1 344 ? 19.432 29.290  40.929 1.00 27.33 ? 785  ASN   A ND2 1 
ATOM   2750 N  N   . VAL   A 1 345 ? 15.492 30.125  37.170 1.00 22.25 ? 786  VAL   A N   1 
ATOM   2751 C  CA  . VAL   A 1 345 ? 14.516 30.921  36.433 1.00 21.25 ? 786  VAL   A CA  1 
ATOM   2752 C  C   . VAL   A 1 345 ? 13.260 30.106  36.157 1.00 23.58 ? 786  VAL   A C   1 
ATOM   2753 O  O   . VAL   A 1 345 ? 12.136 30.618  36.244 1.00 23.61 ? 786  VAL   A O   1 
ATOM   2754 C  CB  . VAL   A 1 345 ? 15.136 31.481  35.138 1.00 18.18 ? 786  VAL   A CB  1 
ATOM   2755 C  CG1 . VAL   A 1 345 ? 14.132 32.373  34.413 1.00 18.39 ? 786  VAL   A CG1 1 
ATOM   2756 C  CG2 . VAL   A 1 345 ? 16.424 32.228  35.439 1.00 18.26 ? 786  VAL   A CG2 1 
ATOM   2757 N  N   . LEU   A 1 346 ? 13.432 28.827  35.803 1.00 25.69 ? 787  LEU   A N   1 
ATOM   2758 C  CA  . LEU   A 1 346 ? 12.283 27.964  35.543 1.00 26.01 ? 787  LEU   A CA  1 
ATOM   2759 C  C   . LEU   A 1 346 ? 11.397 27.846  36.777 1.00 22.86 ? 787  LEU   A C   1 
ATOM   2760 O  O   . LEU   A 1 346 ? 10.166 27.871  36.672 1.00 25.16 ? 787  LEU   A O   1 
ATOM   2761 C  CB  . LEU   A 1 346 ? 12.765 26.581  35.105 1.00 26.85 ? 787  LEU   A CB  1 
ATOM   2762 C  CG  . LEU   A 1 346 ? 13.219 26.417  33.652 1.00 27.16 ? 787  LEU   A CG  1 
ATOM   2763 C  CD1 . LEU   A 1 346 ? 14.077 25.164  33.511 1.00 29.76 ? 787  LEU   A CD1 1 
ATOM   2764 C  CD2 . LEU   A 1 346 ? 12.034 26.359  32.720 1.00 26.72 ? 787  LEU   A CD2 1 
ATOM   2765 N  N   . ARG   A 1 347 ? 12.010 27.713  37.953 1.00 24.36 ? 788  ARG   A N   1 
ATOM   2766 C  CA  . ARG   A 1 347 ? 11.236 27.620  39.186 1.00 29.38 ? 788  ARG   A CA  1 
ATOM   2767 C  C   . ARG   A 1 347 ? 10.530 28.935  39.481 1.00 29.74 ? 788  ARG   A C   1 
ATOM   2768 O  O   . ARG   A 1 347 ? 9.397  28.943  39.976 1.00 30.45 ? 788  ARG   A O   1 
ATOM   2769 C  CB  . ARG   A 1 347 ? 12.158 27.235  40.343 1.00 35.38 ? 788  ARG   A CB  1 
ATOM   2770 N  N   . ALA   A 1 348 ? 11.177 30.057  39.169 1.00 30.00 ? 789  ALA   A N   1 
ATOM   2771 C  CA  . ALA   A 1 348 ? 10.588 31.358  39.449 1.00 27.12 ? 789  ALA   A CA  1 
ATOM   2772 C  C   . ALA   A 1 348 ? 9.452  31.705  38.495 1.00 24.47 ? 789  ALA   A C   1 
ATOM   2773 O  O   . ALA   A 1 348 ? 8.532  32.434  38.881 1.00 24.41 ? 789  ALA   A O   1 
ATOM   2774 C  CB  . ALA   A 1 348 ? 11.671 32.438  39.426 1.00 23.42 ? 789  ALA   A CB  1 
ATOM   2775 N  N   . HIS   A 1 349 ? 9.475  31.197  37.261 1.00 20.79 ? 790  HIS   A N   1 
ATOM   2776 C  CA  . HIS   A 1 349 ? 8.485  31.606  36.276 1.00 22.67 ? 790  HIS   A CA  1 
ATOM   2777 C  C   . HIS   A 1 349 ? 7.459  30.545  35.908 1.00 26.86 ? 790  HIS   A C   1 
ATOM   2778 O  O   . HIS   A 1 349 ? 6.454  30.885  35.274 1.00 25.68 ? 790  HIS   A O   1 
ATOM   2779 C  CB  . HIS   A 1 349 ? 9.161  32.178  35.021 1.00 21.23 ? 790  HIS   A CB  1 
ATOM   2780 C  CG  . HIS   A 1 349 ? 9.556  33.606  35.186 1.00 20.15 ? 790  HIS   A CG  1 
ATOM   2781 N  ND1 . HIS   A 1 349 ? 8.668  34.643  35.004 1.00 18.84 ? 790  HIS   A ND1 1 
ATOM   2782 C  CD2 . HIS   A 1 349 ? 10.725 34.170  35.561 1.00 19.37 ? 790  HIS   A CD2 1 
ATOM   2783 C  CE1 . HIS   A 1 349 ? 9.277  35.787  35.252 1.00 19.65 ? 790  HIS   A CE1 1 
ATOM   2784 N  NE2 . HIS   A 1 349 ? 10.526 35.529  35.588 1.00 18.61 ? 790  HIS   A NE2 1 
ATOM   2785 N  N   . ALA   A 1 350 ? 7.673  29.287  36.288 1.00 30.50 ? 791  ALA   A N   1 
ATOM   2786 C  CA  . ALA   A 1 350 ? 6.642  28.267  36.108 1.00 33.57 ? 791  ALA   A CA  1 
ATOM   2787 C  C   . ALA   A 1 350 ? 5.271  28.667  36.654 1.00 31.24 ? 791  ALA   A C   1 
ATOM   2788 O  O   . ALA   A 1 350 ? 4.263  28.295  36.030 1.00 31.73 ? 791  ALA   A O   1 
ATOM   2789 C  CB  . ALA   A 1 350 ? 7.119  26.925  36.685 1.00 36.57 ? 791  ALA   A CB  1 
ATOM   2790 N  N   . PRO   A 1 351 ? 5.152  29.396  37.770 1.00 29.34 ? 792  PRO   A N   1 
ATOM   2791 C  CA  . PRO   A 1 351 ? 3.820  29.872  38.185 1.00 30.11 ? 792  PRO   A CA  1 
ATOM   2792 C  C   . PRO   A 1 351 ? 3.107  30.712  37.141 1.00 30.07 ? 792  PRO   A C   1 
ATOM   2793 O  O   . PRO   A 1 351 ? 1.871  30.664  37.061 1.00 32.93 ? 792  PRO   A O   1 
ATOM   2794 C  CB  . PRO   A 1 351 ? 4.115  30.707  39.437 1.00 28.19 ? 792  PRO   A CB  1 
ATOM   2795 C  CG  . PRO   A 1 351 ? 5.390  30.211  39.959 1.00 27.88 ? 792  PRO   A CG  1 
ATOM   2796 C  CD  . PRO   A 1 351 ? 6.158  29.586  38.830 1.00 26.84 ? 792  PRO   A CD  1 
ATOM   2797 N  N   . PHE   A 1 352 ? 3.841  31.493  36.344 1.00 26.19 ? 793  PHE   A N   1 
ATOM   2798 C  CA  . PHE   A 1 352 ? 3.214  32.455  35.450 1.00 23.99 ? 793  PHE   A CA  1 
ATOM   2799 C  C   . PHE   A 1 352 ? 3.082  31.975  34.015 1.00 27.53 ? 793  PHE   A C   1 
ATOM   2800 O  O   . PHE   A 1 352 ? 2.228  32.491  33.284 1.00 31.05 ? 793  PHE   A O   1 
ATOM   2801 C  CB  . PHE   A 1 352 ? 3.979  33.783  35.471 1.00 23.65 ? 793  PHE   A CB  1 
ATOM   2802 C  CG  . PHE   A 1 352 ? 4.326  34.248  36.849 1.00 24.17 ? 793  PHE   A CG  1 
ATOM   2803 C  CD1 . PHE   A 1 352 ? 3.347  34.778  37.671 1.00 23.86 ? 793  PHE   A CD1 1 
ATOM   2804 C  CD2 . PHE   A 1 352 ? 5.615  34.155  37.329 1.00 23.37 ? 793  PHE   A CD2 1 
ATOM   2805 C  CE1 . PHE   A 1 352 ? 3.651  35.210  38.944 1.00 24.27 ? 793  PHE   A CE1 1 
ATOM   2806 C  CE2 . PHE   A 1 352 ? 5.930  34.589  38.603 1.00 24.76 ? 793  PHE   A CE2 1 
ATOM   2807 C  CZ  . PHE   A 1 352 ? 4.936  35.115  39.417 1.00 24.49 ? 793  PHE   A CZ  1 
ATOM   2808 N  N   . TRP   A 1 353 ? 3.894  31.008  33.599 1.00 28.03 ? 794  TRP   A N   1 
ATOM   2809 C  CA  . TRP   A 1 353 ? 3.944  30.570  32.208 1.00 27.25 ? 794  TRP   A CA  1 
ATOM   2810 C  C   . TRP   A 1 353 ? 3.714  29.067  32.177 1.00 28.91 ? 794  TRP   A C   1 
ATOM   2811 O  O   . TRP   A 1 353 ? 4.594  28.297  32.574 1.00 27.46 ? 794  TRP   A O   1 
ATOM   2812 C  CB  . TRP   A 1 353 ? 5.290  30.943  31.580 1.00 23.42 ? 794  TRP   A CB  1 
ATOM   2813 C  CG  . TRP   A 1 353 ? 5.540  32.418  31.665 1.00 21.34 ? 794  TRP   A CG  1 
ATOM   2814 C  CD1 . TRP   A 1 353 ? 6.319  33.064  32.574 1.00 20.30 ? 794  TRP   A CD1 1 
ATOM   2815 C  CD2 . TRP   A 1 353 ? 4.964  33.432  30.833 1.00 20.84 ? 794  TRP   A CD2 1 
ATOM   2816 N  NE1 . TRP   A 1 353 ? 6.278  34.424  32.351 1.00 18.40 ? 794  TRP   A NE1 1 
ATOM   2817 C  CE2 . TRP   A 1 353 ? 5.455  34.675  31.290 1.00 20.02 ? 794  TRP   A CE2 1 
ATOM   2818 C  CE3 . TRP   A 1 353 ? 4.086  33.411  29.746 1.00 23.65 ? 794  TRP   A CE3 1 
ATOM   2819 C  CZ2 . TRP   A 1 353 ? 5.096  35.883  30.697 1.00 21.51 ? 794  TRP   A CZ2 1 
ATOM   2820 C  CZ3 . TRP   A 1 353 ? 3.735  34.614  29.150 1.00 24.44 ? 794  TRP   A CZ3 1 
ATOM   2821 C  CH2 . TRP   A 1 353 ? 4.243  35.834  29.629 1.00 24.04 ? 794  TRP   A CH2 1 
ATOM   2822 N  N   . SER   A 1 354 ? 2.529  28.658  31.708 1.00 29.55 ? 795  SER   A N   1 
ATOM   2823 C  CA  A SER   A 1 354 ? 2.191  27.240  31.651 0.31 32.98 ? 795  SER   A CA  1 
ATOM   2824 C  CA  B SER   A 1 354 ? 2.193  27.240  31.654 0.69 32.36 ? 795  SER   A CA  1 
ATOM   2825 C  C   . SER   A 1 354 ? 3.123  26.458  30.737 1.00 36.14 ? 795  SER   A C   1 
ATOM   2826 O  O   . SER   A 1 354 ? 3.285  25.248  30.925 1.00 41.71 ? 795  SER   A O   1 
ATOM   2827 C  CB  A SER   A 1 354 ? 0.742  27.063  31.195 0.31 31.87 ? 795  SER   A CB  1 
ATOM   2828 C  CB  B SER   A 1 354 ? 0.732  27.048  31.232 0.69 31.85 ? 795  SER   A CB  1 
ATOM   2829 O  OG  A SER   A 1 354 ? -0.168 27.517  32.182 0.31 31.13 ? 795  SER   A OG  1 
ATOM   2830 O  OG  B SER   A 1 354 ? 0.506  27.472  29.897 0.69 29.51 ? 795  SER   A OG  1 
ATOM   2831 N  N   . SER   A 1 355 ? 3.741  27.120  29.757 1.00 37.09 ? 796  SER   A N   1 
ATOM   2832 C  CA  . SER   A 1 355 ? 4.655  26.450  28.839 1.00 37.53 ? 796  SER   A CA  1 
ATOM   2833 C  C   . SER   A 1 355 ? 5.934  25.969  29.512 1.00 33.92 ? 796  SER   A C   1 
ATOM   2834 O  O   . SER   A 1 355 ? 6.700  25.228  28.884 1.00 35.48 ? 796  SER   A O   1 
ATOM   2835 C  CB  . SER   A 1 355 ? 5.001  27.389  27.684 1.00 36.76 ? 796  SER   A CB  1 
ATOM   2836 O  OG  . SER   A 1 355 ? 5.875  28.415  28.124 1.00 34.68 ? 796  SER   A OG  1 
ATOM   2837 N  N   . LEU   A 1 356 ? 6.191  26.382  30.753 1.00 34.51 ? 797  LEU   A N   1 
ATOM   2838 C  CA  . LEU   A 1 356 ? 7.378  25.981  31.496 1.00 38.36 ? 797  LEU   A CA  1 
ATOM   2839 C  C   . LEU   A 1 356 ? 7.113  24.848  32.475 1.00 40.53 ? 797  LEU   A C   1 
ATOM   2840 O  O   . LEU   A 1 356 ? 8.060  24.360  33.104 1.00 39.96 ? 797  LEU   A O   1 
ATOM   2841 C  CB  . LEU   A 1 356 ? 7.944  27.171  32.282 1.00 32.71 ? 797  LEU   A CB  1 
ATOM   2842 C  CG  . LEU   A 1 356 ? 8.207  28.455  31.497 1.00 33.25 ? 797  LEU   A CG  1 
ATOM   2843 C  CD1 . LEU   A 1 356 ? 8.720  29.546  32.426 1.00 32.70 ? 797  LEU   A CD1 1 
ATOM   2844 C  CD2 . LEU   A 1 356 ? 9.195  28.190  30.368 1.00 32.68 ? 797  LEU   A CD2 1 
ATOM   2845 N  N   . ARG   A 1 357 ? 5.863  24.433  32.631 1.00 46.75 ? 798  ARG   A N   1 
ATOM   2846 C  CA  . ARG   A 1 357 ? 5.522  23.393  33.590 1.00 49.82 ? 798  ARG   A CA  1 
ATOM   2847 C  C   . ARG   A 1 357 ? 5.758  22.003  33.003 1.00 55.82 ? 798  ARG   A C   1 
ATOM   2848 O  O   . ARG   A 1 357 ? 5.728  21.811  31.786 1.00 58.97 ? 798  ARG   A O   1 
ATOM   2849 C  CB  . ARG   A 1 357 ? 4.069  23.546  34.035 1.00 48.74 ? 798  ARG   A CB  1 
ATOM   2850 C  CG  . ARG   A 1 357 ? 3.832  24.723  34.969 1.00 45.84 ? 798  ARG   A CG  1 
ATOM   2851 C  CD  . ARG   A 1 357 ? 2.415  25.253  34.834 1.00 47.08 ? 798  ARG   A CD  1 
ATOM   2852 N  NE  . ARG   A 1 357 ? 2.059  26.154  35.926 1.00 50.22 ? 798  ARG   A NE  1 
ATOM   2853 C  CZ  . ARG   A 1 357 ? 1.060  27.028  35.873 1.00 57.62 ? 798  ARG   A CZ  1 
ATOM   2854 N  NH1 . ARG   A 1 357 ? 0.315  27.120  34.779 1.00 61.75 ? 798  ARG   A NH1 1 
ATOM   2855 N  NH2 . ARG   A 1 357 ? 0.804  27.808  36.913 1.00 56.72 ? 798  ARG   A NH2 1 
ATOM   2856 O  OXT . ARG   A 1 357 ? 5.987  21.040  33.736 1.00 56.55 ? 798  ARG   A OXT 1 
ATOM   2857 N  N   . PRO   B 1 1   ? 10.049 85.857  26.867 1.00 41.52 ? 442  PRO   B N   1 
ATOM   2858 C  CA  . PRO   B 1 1   ? 10.321 86.446  28.184 1.00 40.05 ? 442  PRO   B CA  1 
ATOM   2859 C  C   . PRO   B 1 1   ? 11.505 87.412  28.154 1.00 34.12 ? 442  PRO   B C   1 
ATOM   2860 O  O   . PRO   B 1 1   ? 12.567 87.070  27.639 1.00 31.20 ? 442  PRO   B O   1 
ATOM   2861 C  CB  . PRO   B 1 1   ? 10.658 85.226  29.051 1.00 42.51 ? 442  PRO   B CB  1 
ATOM   2862 C  CG  . PRO   B 1 1   ? 11.180 84.214  28.081 1.00 44.46 ? 442  PRO   B CG  1 
ATOM   2863 C  CD  . PRO   B 1 1   ? 10.390 84.424  26.818 1.00 42.73 ? 442  PRO   B CD  1 
ATOM   2864 N  N   . ILE   B 1 2   ? 11.320 88.602  28.719 1.00 29.31 ? 443  ILE   B N   1 
ATOM   2865 C  CA  . ILE   B 1 2   ? 12.333 89.651  28.724 1.00 24.52 ? 443  ILE   B CA  1 
ATOM   2866 C  C   . ILE   B 1 2   ? 12.876 89.822  30.139 1.00 21.16 ? 443  ILE   B C   1 
ATOM   2867 O  O   . ILE   B 1 2   ? 12.121 89.772  31.119 1.00 21.98 ? 443  ILE   B O   1 
ATOM   2868 C  CB  . ILE   B 1 2   ? 11.734 90.970  28.196 1.00 27.88 ? 443  ILE   B CB  1 
ATOM   2869 C  CG1 . ILE   B 1 2   ? 11.207 90.776  26.771 1.00 31.03 ? 443  ILE   B CG1 1 
ATOM   2870 C  CG2 . ILE   B 1 2   ? 12.758 92.100  28.277 1.00 25.43 ? 443  ILE   B CG2 1 
ATOM   2871 C  CD1 . ILE   B 1 2   ? 10.453 91.968  26.215 1.00 35.74 ? 443  ILE   B CD1 1 
ATOM   2872 N  N   . THR   B 1 3   ? 14.190 90.022  30.246 1.00 20.24 ? 444  THR   B N   1 
ATOM   2873 C  CA  . THR   B 1 3   ? 14.851 90.335  31.508 1.00 18.97 ? 444  THR   B CA  1 
ATOM   2874 C  C   . THR   B 1 3   ? 15.276 91.797  31.490 1.00 16.25 ? 444  THR   B C   1 
ATOM   2875 O  O   . THR   B 1 3   ? 15.928 92.246  30.541 1.00 18.09 ? 444  THR   B O   1 
ATOM   2876 C  CB  . THR   B 1 3   ? 16.081 89.442  31.709 1.00 16.24 ? 444  THR   B CB  1 
ATOM   2877 O  OG1 . THR   B 1 3   ? 15.670 88.076  31.833 1.00 17.51 ? 444  THR   B OG1 1 
ATOM   2878 C  CG2 . THR   B 1 3   ? 16.868 89.860  32.956 1.00 15.25 ? 444  THR   B CG2 1 
ATOM   2879 N  N   . GLY   B 1 4   ? 14.879 92.550  32.527 1.00 13.93 ? 445  GLY   B N   1 
ATOM   2880 C  CA  . GLY   B 1 4   ? 15.320 93.916  32.673 1.00 13.70 ? 445  GLY   B CA  1 
ATOM   2881 C  C   . GLY   B 1 4   ? 16.636 94.029  33.421 1.00 15.89 ? 445  GLY   B C   1 
ATOM   2882 O  O   . GLY   B 1 4   ? 17.007 93.158  34.207 1.00 14.92 ? 445  GLY   B O   1 
ATOM   2883 N  N   . LEU   B 1 5   ? 17.348 95.121  33.156 1.00 14.92 ? 446  LEU   B N   1 
ATOM   2884 C  CA  . LEU   B 1 5   ? 18.591 95.421  33.851 1.00 13.68 ? 446  LEU   B CA  1 
ATOM   2885 C  C   . LEU   B 1 5   ? 18.658 96.913  34.097 1.00 14.18 ? 446  LEU   B C   1 
ATOM   2886 O  O   . LEU   B 1 5   ? 18.467 97.710  33.172 1.00 16.48 ? 446  LEU   B O   1 
ATOM   2887 C  CB  . LEU   B 1 5   ? 19.820 94.969  33.046 1.00 14.30 ? 446  LEU   B CB  1 
ATOM   2888 C  CG  . LEU   B 1 5   ? 21.201 95.163  33.692 1.00 14.37 ? 446  LEU   B CG  1 
ATOM   2889 C  CD1 . LEU   B 1 5   ? 22.127 94.049  33.266 1.00 15.01 ? 446  LEU   B CD1 1 
ATOM   2890 C  CD2 . LEU   B 1 5   ? 21.823 96.518  33.365 1.00 14.50 ? 446  LEU   B CD2 1 
ATOM   2891 N  N   . VAL   B 1 6   ? 18.937 97.289  35.342 1.00 14.39 ? 447  VAL   B N   1 
ATOM   2892 C  CA  . VAL   B 1 6   ? 19.151 98.684  35.691 1.00 14.77 ? 447  VAL   B CA  1 
ATOM   2893 C  C   . VAL   B 1 6   ? 20.562 98.861  36.243 1.00 14.39 ? 447  VAL   B C   1 
ATOM   2894 O  O   . VAL   B 1 6   ? 21.019 98.081  37.091 1.00 15.70 ? 447  VAL   B O   1 
ATOM   2895 C  CB  . VAL   B 1 6   ? 18.050 99.258  36.606 1.00 14.46 ? 447  VAL   B CB  1 
ATOM   2896 C  CG1 . VAL   B 1 6   ? 17.940 98.483  37.910 1.00 14.83 ? 447  VAL   B CG1 1 
ATOM   2897 C  CG2 . VAL   B 1 6   ? 18.317 100.733 36.865 1.00 16.51 ? 447  VAL   B CG2 1 
ATOM   2898 N  N   . TYR   B 1 7   ? 21.262 99.864  35.723 1.00 16.03 ? 448  TYR   B N   1 
ATOM   2899 C  CA  . TYR   B 1 7   ? 22.593 100.245 36.165 1.00 15.57 ? 448  TYR   B CA  1 
ATOM   2900 C  C   . TYR   B 1 7   ? 22.762 101.708 35.802 1.00 16.04 ? 448  TYR   B C   1 
ATOM   2901 O  O   . TYR   B 1 7   ? 22.427 102.109 34.688 1.00 18.74 ? 448  TYR   B O   1 
ATOM   2902 C  CB  . TYR   B 1 7   ? 23.693 99.446  35.454 1.00 15.60 ? 448  TYR   B CB  1 
ATOM   2903 C  CG  . TYR   B 1 7   ? 25.078 100.038 35.655 1.00 15.63 ? 448  TYR   B CG  1 
ATOM   2904 C  CD1 . TYR   B 1 7   ? 25.750 99.883  36.859 1.00 17.11 ? 448  TYR   B CD1 1 
ATOM   2905 C  CD2 . TYR   B 1 7   ? 25.716 100.747 34.641 1.00 15.24 ? 448  TYR   B CD2 1 
ATOM   2906 C  CE1 . TYR   B 1 7   ? 27.008 100.422 37.052 1.00 16.29 ? 448  TYR   B CE1 1 
ATOM   2907 C  CE2 . TYR   B 1 7   ? 26.972 101.289 34.829 1.00 16.41 ? 448  TYR   B CE2 1 
ATOM   2908 C  CZ  . TYR   B 1 7   ? 27.615 101.117 36.042 1.00 17.76 ? 448  TYR   B CZ  1 
ATOM   2909 O  OH  . TYR   B 1 7   ? 28.877 101.639 36.280 1.00 20.46 ? 448  TYR   B OH  1 
ATOM   2910 N  N   . ASP   B 1 8   ? 23.281 102.505 36.730 1.00 15.78 ? 449  ASP   B N   1 
ATOM   2911 C  CA  . ASP   B 1 8   ? 23.567 103.906 36.439 1.00 17.00 ? 449  ASP   B CA  1 
ATOM   2912 C  C   . ASP   B 1 8   ? 24.890 104.263 37.091 1.00 17.36 ? 449  ASP   B C   1 
ATOM   2913 O  O   . ASP   B 1 8   ? 25.030 104.146 38.314 1.00 16.90 ? 449  ASP   B O   1 
ATOM   2914 C  CB  . ASP   B 1 8   ? 22.448 104.823 36.935 1.00 17.14 ? 449  ASP   B CB  1 
ATOM   2915 C  CG  . ASP   B 1 8   ? 22.537 106.224 36.349 1.00 25.08 ? 449  ASP   B CG  1 
ATOM   2916 O  OD1 . ASP   B 1 8   ? 23.630 106.832 36.399 1.00 25.93 ? 449  ASP   B OD1 1 
ATOM   2917 O  OD2 . ASP   B 1 8   ? 21.518 106.720 35.822 1.00 25.74 ? 449  ASP   B OD2 1 
ATOM   2918 N  N   A GLN   B 1 9   ? 25.859 104.696 36.280 0.67 16.12 ? 450  GLN   B N   1 
ATOM   2919 N  N   B GLN   B 1 9   ? 25.845 104.719 36.274 0.33 16.02 ? 450  GLN   B N   1 
ATOM   2920 C  CA  A GLN   B 1 9   ? 27.181 105.001 36.816 0.67 15.56 ? 450  GLN   B CA  1 
ATOM   2921 C  CA  B GLN   B 1 9   ? 27.182 105.045 36.758 0.33 16.34 ? 450  GLN   B CA  1 
ATOM   2922 C  C   A GLN   B 1 9   ? 27.171 106.141 37.828 0.67 14.75 ? 450  GLN   B C   1 
ATOM   2923 C  C   B GLN   B 1 9   ? 27.166 106.098 37.861 0.33 16.87 ? 450  GLN   B C   1 
ATOM   2924 O  O   A GLN   B 1 9   ? 28.150 106.292 38.562 0.67 14.54 ? 450  GLN   B O   1 
ATOM   2925 O  O   B GLN   B 1 9   ? 28.095 106.135 38.675 0.33 20.32 ? 450  GLN   B O   1 
ATOM   2926 C  CB  A GLN   B 1 9   ? 28.201 105.241 35.694 0.67 18.54 ? 450  GLN   B CB  1 
ATOM   2927 C  CB  B GLN   B 1 9   ? 28.060 105.491 35.582 0.33 18.78 ? 450  GLN   B CB  1 
ATOM   2928 C  CG  A GLN   B 1 9   ? 27.959 106.481 34.858 0.67 20.92 ? 450  GLN   B CG  1 
ATOM   2929 C  CG  B GLN   B 1 9   ? 29.522 105.733 35.924 0.33 22.18 ? 450  GLN   B CG  1 
ATOM   2930 C  CD  A GLN   B 1 9   ? 28.978 106.629 33.733 0.67 24.39 ? 450  GLN   B CD  1 
ATOM   2931 C  CD  B GLN   B 1 9   ? 29.791 107.162 36.352 0.33 24.54 ? 450  GLN   B CD  1 
ATOM   2932 O  OE1 A GLN   B 1 9   ? 29.772 105.719 33.471 0.67 26.16 ? 450  GLN   B OE1 1 
ATOM   2933 O  OE1 B GLN   B 1 9   ? 29.080 108.086 35.951 0.33 28.04 ? 450  GLN   B OE1 1 
ATOM   2934 N  NE2 A GLN   B 1 9   ? 28.971 107.785 33.075 0.67 27.68 ? 450  GLN   B NE2 1 
ATOM   2935 N  NE2 B GLN   B 1 9   ? 30.819 107.352 37.171 0.33 26.92 ? 450  GLN   B NE2 1 
ATOM   2936 N  N   A ARG   B 1 10  ? 26.092 106.923 37.921 0.67 15.59 ? 451  ARG   B N   1 
ATOM   2937 N  N   B ARG   B 1 10  ? 26.128 106.938 37.925 0.33 16.15 ? 451  ARG   B N   1 
ATOM   2938 C  CA  A ARG   B 1 10  ? 26.051 107.973 38.933 0.67 15.71 ? 451  ARG   B CA  1 
ATOM   2939 C  CA  B ARG   B 1 10  ? 26.077 107.985 38.942 0.33 17.50 ? 451  ARG   B CA  1 
ATOM   2940 C  C   A ARG   B 1 10  ? 26.143 107.389 40.336 0.67 15.89 ? 451  ARG   B C   1 
ATOM   2941 C  C   B ARG   B 1 10  ? 26.055 107.420 40.358 0.33 16.08 ? 451  ARG   B C   1 
ATOM   2942 O  O   A ARG   B 1 10  ? 26.665 108.042 41.251 0.67 16.70 ? 451  ARG   B O   1 
ATOM   2943 O  O   B ARG   B 1 10  ? 26.395 108.136 41.309 0.33 14.54 ? 451  ARG   B O   1 
ATOM   2944 C  CB  A ARG   B 1 10  ? 24.777 108.802 38.780 0.67 18.93 ? 451  ARG   B CB  1 
ATOM   2945 C  CB  B ARG   B 1 10  ? 24.863 108.888 38.706 0.33 19.40 ? 451  ARG   B CB  1 
ATOM   2946 C  CG  A ARG   B 1 10  ? 24.733 109.631 37.516 0.67 21.56 ? 451  ARG   B CG  1 
ATOM   2947 C  CG  B ARG   B 1 10  ? 25.066 109.934 37.622 0.33 21.19 ? 451  ARG   B CG  1 
ATOM   2948 C  CD  A ARG   B 1 10  ? 23.481 110.484 37.478 0.67 23.00 ? 451  ARG   B CD  1 
ATOM   2949 C  CD  B ARG   B 1 10  ? 23.851 110.844 37.497 0.33 22.21 ? 451  ARG   B CD  1 
ATOM   2950 N  NE  A ARG   B 1 10  ? 22.350 109.747 36.932 0.67 22.97 ? 451  ARG   B NE  1 
ATOM   2951 N  NE  B ARG   B 1 10  ? 23.351 111.288 38.796 0.33 22.34 ? 451  ARG   B NE  1 
ATOM   2952 C  CZ  A ARG   B 1 10  ? 21.078 110.022 37.200 0.67 21.02 ? 451  ARG   B CZ  1 
ATOM   2953 C  CZ  B ARG   B 1 10  ? 23.975 112.158 39.585 0.33 23.54 ? 451  ARG   B CZ  1 
ATOM   2954 N  NH1 A ARG   B 1 10  ? 20.768 111.023 38.015 0.67 22.24 ? 451  ARG   B NH1 1 
ATOM   2955 N  NH1 B ARG   B 1 10  ? 25.127 112.682 39.219 0.33 25.12 ? 451  ARG   B NH1 1 
ATOM   2956 N  NH2 A ARG   B 1 10  ? 20.117 109.295 36.651 0.67 20.45 ? 451  ARG   B NH2 1 
ATOM   2957 N  NH2 B ARG   B 1 10  ? 23.453 112.507 40.747 0.33 20.48 ? 451  ARG   B NH2 1 
ATOM   2958 N  N   . MET   B 1 11  ? 25.662 106.157 40.526 1.00 14.12 ? 452  MET   B N   1 
ATOM   2959 C  CA  . MET   B 1 11  ? 25.740 105.533 41.841 1.00 14.46 ? 452  MET   B CA  1 
ATOM   2960 C  C   . MET   B 1 11  ? 27.177 105.275 42.278 1.00 16.74 ? 452  MET   B C   1 
ATOM   2961 O  O   . MET   B 1 11  ? 27.395 104.937 43.442 1.00 16.32 ? 452  MET   B O   1 
ATOM   2962 C  CB  . MET   B 1 11  ? 24.905 104.253 41.882 1.00 14.74 ? 452  MET   B CB  1 
ATOM   2963 C  CG  . MET   B 1 11  ? 23.429 104.528 42.082 1.00 15.83 ? 452  MET   B CG  1 
ATOM   2964 S  SD  . MET   B 1 11  ? 22.394 103.054 41.985 1.00 13.69 ? 452  MET   B SD  1 
ATOM   2965 C  CE  . MET   B 1 11  ? 22.420 102.702 40.225 1.00 17.68 ? 452  MET   B CE  1 
ATOM   2966 N  N   . MET   B 1 12  ? 28.158 105.450 41.384 1.00 15.24 ? 453  MET   B N   1 
ATOM   2967 C  CA  . MET   B 1 12  ? 29.566 105.375 41.781 1.00 14.11 ? 453  MET   B CA  1 
ATOM   2968 C  C   . MET   B 1 12  ? 30.039 106.600 42.551 1.00 17.13 ? 453  MET   B C   1 
ATOM   2969 O  O   . MET   B 1 12  ? 31.134 106.558 43.127 1.00 17.34 ? 453  MET   B O   1 
ATOM   2970 C  CB  . MET   B 1 12  ? 30.468 105.192 40.555 1.00 17.33 ? 453  MET   B CB  1 
ATOM   2971 C  CG  . MET   B 1 12  ? 30.268 103.881 39.807 1.00 19.27 ? 453  MET   B CG  1 
ATOM   2972 S  SD  . MET   B 1 12  ? 31.369 103.739 38.373 1.00 22.35 ? 453  MET   B SD  1 
ATOM   2973 C  CE  . MET   B 1 12  ? 32.964 103.463 39.130 1.00 22.26 ? 453  MET   B CE  1 
ATOM   2974 N  N   . LEU   B 1 13  ? 29.254 107.682 42.589 1.00 17.14 ? 454  LEU   B N   1 
ATOM   2975 C  CA  . LEU   B 1 13  ? 29.745 108.933 43.169 1.00 17.27 ? 454  LEU   B CA  1 
ATOM   2976 C  C   . LEU   B 1 13  ? 29.808 108.895 44.693 1.00 17.62 ? 454  LEU   B C   1 
ATOM   2977 O  O   . LEU   B 1 13  ? 30.588 109.644 45.291 1.00 20.63 ? 454  LEU   B O   1 
ATOM   2978 C  CB  . LEU   B 1 13  ? 28.888 110.105 42.693 1.00 17.42 ? 454  LEU   B CB  1 
ATOM   2979 C  CG  . LEU   B 1 13  ? 28.964 110.336 41.184 1.00 20.47 ? 454  LEU   B CG  1 
ATOM   2980 C  CD1 . LEU   B 1 13  ? 27.922 111.366 40.754 1.00 20.57 ? 454  LEU   B CD1 1 
ATOM   2981 C  CD2 . LEU   B 1 13  ? 30.373 110.775 40.796 1.00 21.59 ? 454  LEU   B CD2 1 
ATOM   2982 N  N   . HIS   B 1 14  ? 28.983 108.067 45.332 1.00 14.19 ? 455  HIS   B N   1 
ATOM   2983 C  CA  . HIS   B 1 14  ? 29.084 107.819 46.761 1.00 15.02 ? 455  HIS   B CA  1 
ATOM   2984 C  C   . HIS   B 1 14  ? 30.443 107.201 47.051 1.00 14.53 ? 455  HIS   B C   1 
ATOM   2985 O  O   . HIS   B 1 14  ? 30.793 106.160 46.486 1.00 15.54 ? 455  HIS   B O   1 
ATOM   2986 C  CB  . HIS   B 1 14  ? 27.965 106.844 47.137 1.00 13.43 ? 455  HIS   B CB  1 
ATOM   2987 C  CG  . HIS   B 1 14  ? 28.101 106.226 48.495 1.00 14.39 ? 455  HIS   B CG  1 
ATOM   2988 N  ND1 . HIS   B 1 14  ? 28.090 106.965 49.657 1.00 15.48 ? 455  HIS   B ND1 1 
ATOM   2989 C  CD2 . HIS   B 1 14  ? 28.165 104.927 48.875 1.00 14.28 ? 455  HIS   B CD2 1 
ATOM   2990 C  CE1 . HIS   B 1 14  ? 28.165 106.149 50.695 1.00 15.56 ? 455  HIS   B CE1 1 
ATOM   2991 N  NE2 . HIS   B 1 14  ? 28.213 104.907 50.244 1.00 15.37 ? 455  HIS   B NE2 1 
ATOM   2992 N  N   . HIS   B 1 15  ? 31.219 107.841 47.925 1.00 17.49 ? 456  HIS   B N   1 
ATOM   2993 C  CA  . HIS   B 1 15  ? 32.588 107.398 48.151 1.00 16.82 ? 456  HIS   B CA  1 
ATOM   2994 C  C   . HIS   B 1 15  ? 33.043 107.764 49.556 1.00 15.44 ? 456  HIS   B C   1 
ATOM   2995 O  O   . HIS   B 1 15  ? 32.457 108.615 50.230 1.00 17.19 ? 456  HIS   B O   1 
ATOM   2996 C  CB  . HIS   B 1 15  ? 33.543 107.991 47.109 1.00 17.32 ? 456  HIS   B CB  1 
ATOM   2997 C  CG  . HIS   B 1 15  ? 33.742 109.467 47.250 1.00 20.58 ? 456  HIS   B CG  1 
ATOM   2998 N  ND1 . HIS   B 1 15  ? 32.825 110.387 46.791 1.00 21.81 ? 456  HIS   B ND1 1 
ATOM   2999 C  CD2 . HIS   B 1 15  ? 34.752 110.185 47.801 1.00 21.46 ? 456  HIS   B CD2 1 
ATOM   3000 C  CE1 . HIS   B 1 15  ? 33.259 111.608 47.052 1.00 25.18 ? 456  HIS   B CE1 1 
ATOM   3001 N  NE2 . HIS   B 1 15  ? 34.426 111.513 47.663 1.00 23.29 ? 456  HIS   B NE2 1 
ATOM   3002 N  N   . ASN   B 1 16  ? 34.114 107.100 49.986 1.00 16.74 ? 457  ASN   B N   1 
ATOM   3003 C  CA  . ASN   B 1 16  ? 34.688 107.295 51.312 1.00 16.36 ? 457  ASN   B CA  1 
ATOM   3004 C  C   . ASN   B 1 16  ? 35.847 108.277 51.179 1.00 18.63 ? 457  ASN   B C   1 
ATOM   3005 O  O   . ASN   B 1 16  ? 36.890 107.945 50.607 1.00 18.73 ? 457  ASN   B O   1 
ATOM   3006 C  CB  . ASN   B 1 16  ? 35.146 105.953 51.877 1.00 16.06 ? 457  ASN   B CB  1 
ATOM   3007 C  CG  . ASN   B 1 16  ? 35.547 106.038 53.332 1.00 17.85 ? 457  ASN   B CG  1 
ATOM   3008 O  OD1 . ASN   B 1 16  ? 36.167 107.010 53.756 1.00 21.80 ? 457  ASN   B OD1 1 
ATOM   3009 N  ND2 . ASN   B 1 16  ? 35.205 105.016 54.101 1.00 18.48 ? 457  ASN   B ND2 1 
ATOM   3010 N  N   . MET   B 1 17  ? 35.653 109.489 51.699 1.00 20.60 ? 458  MET   B N   1 
ATOM   3011 C  CA  . MET   B 1 17  ? 36.641 110.542 51.499 1.00 24.62 ? 458  MET   B CA  1 
ATOM   3012 C  C   . MET   B 1 17  ? 37.943 110.249 52.230 1.00 20.95 ? 458  MET   B C   1 
ATOM   3013 O  O   . MET   B 1 17  ? 38.998 110.727 51.814 1.00 20.96 ? 458  MET   B O   1 
ATOM   3014 C  CB  . MET   B 1 17  ? 36.081 111.884 51.963 1.00 35.00 ? 458  MET   B CB  1 
ATOM   3015 C  CG  . MET   B 1 17  ? 34.893 112.378 51.161 1.00 45.04 ? 458  MET   B CG  1 
ATOM   3016 S  SD  . MET   B 1 17  ? 34.073 113.749 51.990 1.00 47.85 ? 458  MET   B SD  1 
ATOM   3017 C  CE  . MET   B 1 17  ? 35.389 114.299 53.072 1.00 41.01 ? 458  MET   B CE  1 
ATOM   3018 N  N   . TRP   B 1 18  ? 37.892 109.484 53.314 1.00 22.58 ? 459  TRP   B N   1 
ATOM   3019 C  CA  . TRP   B 1 18  ? 39.067 109.253 54.142 1.00 26.47 ? 459  TRP   B CA  1 
ATOM   3020 C  C   . TRP   B 1 18  ? 39.786 107.952 53.820 1.00 26.78 ? 459  TRP   B C   1 
ATOM   3021 O  O   . TRP   B 1 18  ? 41.010 107.876 53.976 1.00 27.04 ? 459  TRP   B O   1 
ATOM   3022 C  CB  . TRP   B 1 18  ? 38.667 109.289 55.621 1.00 31.50 ? 459  TRP   B CB  1 
ATOM   3023 C  CG  . TRP   B 1 18  ? 37.858 110.506 55.931 1.00 39.58 ? 459  TRP   B CG  1 
ATOM   3024 C  CD1 . TRP   B 1 18  ? 38.323 111.704 56.385 1.00 43.58 ? 459  TRP   B CD1 1 
ATOM   3025 C  CD2 . TRP   B 1 18  ? 36.440 110.663 55.765 1.00 45.45 ? 459  TRP   B CD2 1 
ATOM   3026 N  NE1 . TRP   B 1 18  ? 37.285 112.592 56.529 1.00 44.47 ? 459  TRP   B NE1 1 
ATOM   3027 C  CE2 . TRP   B 1 18  ? 36.118 111.978 56.154 1.00 43.90 ? 459  TRP   B CE2 1 
ATOM   3028 C  CE3 . TRP   B 1 18  ? 35.412 109.816 55.334 1.00 40.46 ? 459  TRP   B CE3 1 
ATOM   3029 C  CZ2 . TRP   B 1 18  ? 34.812 112.469 56.123 1.00 38.63 ? 459  TRP   B CZ2 1 
ATOM   3030 C  CZ3 . TRP   B 1 18  ? 34.113 110.304 55.314 1.00 33.82 ? 459  TRP   B CZ3 1 
ATOM   3031 C  CH2 . TRP   B 1 18  ? 33.825 111.617 55.706 1.00 37.86 ? 459  TRP   B CH2 1 
ATOM   3032 N  N   . ASP   B 1 19  ? 39.060 106.936 53.358 1.00 27.05 ? 460  ASP   B N   1 
ATOM   3033 C  CA  . ASP   B 1 19  ? 39.612 105.617 53.051 1.00 22.60 ? 460  ASP   B CA  1 
ATOM   3034 C  C   . ASP   B 1 19  ? 39.143 105.269 51.642 1.00 22.32 ? 460  ASP   B C   1 
ATOM   3035 O  O   . ASP   B 1 19  ? 38.091 104.646 51.466 1.00 21.83 ? 460  ASP   B O   1 
ATOM   3036 C  CB  . ASP   B 1 19  ? 39.103 104.603 54.066 1.00 22.02 ? 460  ASP   B CB  1 
ATOM   3037 C  CG  . ASP   B 1 19  ? 39.614 103.201 53.803 1.00 20.04 ? 460  ASP   B CG  1 
ATOM   3038 O  OD1 . ASP   B 1 19  ? 40.509 103.031 52.949 1.00 19.38 ? 460  ASP   B OD1 1 
ATOM   3039 O  OD2 . ASP   B 1 19  ? 39.100 102.271 54.455 1.00 22.49 ? 460  ASP   B OD2 1 
ATOM   3040 N  N   . SER   B 1 20  ? 39.927 105.657 50.637 1.00 22.84 ? 461  SER   B N   1 
ATOM   3041 C  CA  . SER   B 1 20  ? 39.550 105.378 49.255 1.00 22.49 ? 461  SER   B CA  1 
ATOM   3042 C  C   . SER   B 1 20  ? 39.581 103.891 48.918 1.00 23.81 ? 461  SER   B C   1 
ATOM   3043 O  O   . SER   B 1 20  ? 39.068 103.502 47.862 1.00 27.37 ? 461  SER   B O   1 
ATOM   3044 C  CB  . SER   B 1 20  ? 40.465 106.141 48.299 1.00 24.61 ? 461  SER   B CB  1 
ATOM   3045 O  OG  . SER   B 1 20  ? 41.799 105.689 48.431 1.00 25.75 ? 461  SER   B OG  1 
ATOM   3046 N  N   . HIS   B 1 21  ? 40.165 103.058 49.779 1.00 21.08 ? 462  HIS   B N   1 
ATOM   3047 C  CA  . HIS   B 1 21  ? 40.220 101.618 49.580 1.00 20.18 ? 462  HIS   B CA  1 
ATOM   3048 C  C   . HIS   B 1 21  ? 39.183 100.875 50.410 1.00 18.58 ? 462  HIS   B C   1 
ATOM   3049 O  O   . HIS   B 1 21  ? 39.234 99.646  50.487 1.00 18.73 ? 462  HIS   B O   1 
ATOM   3050 C  CB  . HIS   B 1 21  ? 41.623 101.085 49.885 1.00 26.72 ? 462  HIS   B CB  1 
ATOM   3051 C  CG  . HIS   B 1 21  ? 42.682 101.623 48.975 1.00 35.60 ? 462  HIS   B CG  1 
ATOM   3052 N  ND1 . HIS   B 1 21  ? 43.086 100.966 47.832 1.00 41.03 ? 462  HIS   B ND1 1 
ATOM   3053 C  CD2 . HIS   B 1 21  ? 43.422 102.755 49.040 1.00 36.05 ? 462  HIS   B CD2 1 
ATOM   3054 C  CE1 . HIS   B 1 21  ? 44.028 101.672 47.231 1.00 40.36 ? 462  HIS   B CE1 1 
ATOM   3055 N  NE2 . HIS   B 1 21  ? 44.251 102.761 47.944 1.00 39.76 ? 462  HIS   B NE2 1 
ATOM   3056 N  N   . HIS   B 1 22  ? 38.250 101.593 51.022 1.00 15.62 ? 463  HIS   B N   1 
ATOM   3057 C  CA  . HIS   B 1 22  ? 37.177 100.951 51.762 1.00 15.89 ? 463  HIS   B CA  1 
ATOM   3058 C  C   . HIS   B 1 22  ? 36.451 99.952  50.856 1.00 16.61 ? 463  HIS   B C   1 
ATOM   3059 O  O   . HIS   B 1 22  ? 36.172 100.264 49.692 1.00 17.13 ? 463  HIS   B O   1 
ATOM   3060 C  CB  . HIS   B 1 22  ? 36.196 102.014 52.263 1.00 16.30 ? 463  HIS   B CB  1 
ATOM   3061 C  CG  . HIS   B 1 22  ? 35.106 101.470 53.124 1.00 17.36 ? 463  HIS   B CG  1 
ATOM   3062 N  ND1 . HIS   B 1 22  ? 34.063 100.723 52.616 1.00 17.07 ? 463  HIS   B ND1 1 
ATOM   3063 C  CD2 . HIS   B 1 22  ? 34.890 101.564 54.455 1.00 20.23 ? 463  HIS   B CD2 1 
ATOM   3064 C  CE1 . HIS   B 1 22  ? 33.252 100.382 53.600 1.00 19.07 ? 463  HIS   B CE1 1 
ATOM   3065 N  NE2 . HIS   B 1 22  ? 33.733 100.875 54.728 1.00 21.61 ? 463  HIS   B NE2 1 
ATOM   3066 N  N   . PRO   B 1 23  ? 36.119 98.762  51.360 1.00 17.11 ? 464  PRO   B N   1 
ATOM   3067 C  CA  . PRO   B 1 23  ? 35.601 97.693  50.480 1.00 16.53 ? 464  PRO   B CA  1 
ATOM   3068 C  C   . PRO   B 1 23  ? 34.294 98.004  49.766 1.00 15.25 ? 464  PRO   B C   1 
ATOM   3069 O  O   . PRO   B 1 23  ? 34.035 97.404  48.716 1.00 14.83 ? 464  PRO   B O   1 
ATOM   3070 C  CB  . PRO   B 1 23  ? 35.430 96.500  51.434 1.00 16.79 ? 464  PRO   B CB  1 
ATOM   3071 C  CG  . PRO   B 1 23  ? 35.371 97.099  52.801 1.00 17.91 ? 464  PRO   B CG  1 
ATOM   3072 C  CD  . PRO   B 1 23  ? 36.276 98.303  52.749 1.00 16.63 ? 464  PRO   B CD  1 
ATOM   3073 N  N   . GLU   B 1 24  ? 33.445 98.885  50.298 1.00 14.85 ? 465  GLU   B N   1 
ATOM   3074 C  CA  . GLU   B 1 24  ? 32.202 99.243  49.605 1.00 13.98 ? 465  GLU   B CA  1 
ATOM   3075 C  C   . GLU   B 1 24  ? 32.532 100.277 48.531 1.00 12.68 ? 465  GLU   B C   1 
ATOM   3076 O  O   . GLU   B 1 24  ? 32.257 101.472 48.654 1.00 15.27 ? 465  GLU   B O   1 
ATOM   3077 C  CB  . GLU   B 1 24  ? 31.149 99.748  50.577 1.00 15.89 ? 465  GLU   B CB  1 
ATOM   3078 C  CG  . GLU   B 1 24  ? 29.714 99.522  50.083 1.00 15.85 ? 465  GLU   B CG  1 
ATOM   3079 C  CD  . GLU   B 1 24  ? 29.290 100.488 48.988 1.00 18.27 ? 465  GLU   B CD  1 
ATOM   3080 O  OE1 . GLU   B 1 24  ? 28.727 101.562 49.315 1.00 17.61 ? 465  GLU   B OE1 1 
ATOM   3081 O  OE2 . GLU   B 1 24  ? 29.513 100.168 47.801 1.00 17.96 ? 465  GLU   B OE2 1 
ATOM   3082 N  N   . LEU   B 1 25  ? 33.137 99.780  47.459 1.00 13.93 ? 466  LEU   B N   1 
ATOM   3083 C  CA  . LEU   B 1 25  ? 33.826 100.557 46.434 1.00 14.53 ? 466  LEU   B CA  1 
ATOM   3084 C  C   . LEU   B 1 25  ? 32.863 100.999 45.337 1.00 15.32 ? 466  LEU   B C   1 
ATOM   3085 O  O   . LEU   B 1 25  ? 31.980 100.229 44.929 1.00 14.34 ? 466  LEU   B O   1 
ATOM   3086 C  CB  . LEU   B 1 25  ? 34.897 99.707  45.776 1.00 15.13 ? 466  LEU   B CB  1 
ATOM   3087 C  CG  . LEU   B 1 25  ? 36.204 99.540  46.522 1.00 16.35 ? 466  LEU   B CG  1 
ATOM   3088 C  CD1 . LEU   B 1 25  ? 37.044 98.491  45.819 1.00 17.26 ? 466  LEU   B CD1 1 
ATOM   3089 C  CD2 . LEU   B 1 25  ? 36.952 100.869 46.565 1.00 18.50 ? 466  LEU   B CD2 1 
ATOM   3090 N  N   . PRO   B 1 26  ? 33.047 102.217 44.811 1.00 15.82 ? 467  PRO   B N   1 
ATOM   3091 C  CA  . PRO   B 1 26  ? 32.300 102.618 43.608 1.00 16.58 ? 467  PRO   B CA  1 
ATOM   3092 C  C   . PRO   B 1 26  ? 32.350 101.583 42.501 1.00 15.65 ? 467  PRO   B C   1 
ATOM   3093 O  O   . PRO   B 1 26  ? 31.331 101.319 41.844 1.00 16.17 ? 467  PRO   B O   1 
ATOM   3094 C  CB  . PRO   B 1 26  ? 32.983 103.933 43.198 1.00 16.30 ? 467  PRO   B CB  1 
ATOM   3095 C  CG  . PRO   B 1 26  ? 33.505 104.491 44.490 1.00 15.96 ? 467  PRO   B CG  1 
ATOM   3096 C  CD  . PRO   B 1 26  ? 33.927 103.292 45.308 1.00 17.21 ? 467  PRO   B CD  1 
ATOM   3097 N  N   . GLN   B 1 27  ? 33.504 100.954 42.302 1.00 14.43 ? 468  GLN   B N   1 
ATOM   3098 C  CA  . GLN   B 1 27  ? 33.650 100.020 41.196 1.00 14.18 ? 468  GLN   B CA  1 
ATOM   3099 C  C   . GLN   B 1 27  ? 32.971 98.677  41.430 1.00 15.13 ? 468  GLN   B C   1 
ATOM   3100 O  O   . GLN   B 1 27  ? 32.981 97.842  40.527 1.00 15.16 ? 468  GLN   B O   1 
ATOM   3101 C  CB  . GLN   B 1 27  ? 35.125 99.822  40.816 1.00 18.77 ? 468  GLN   B CB  1 
ATOM   3102 C  CG  . GLN   B 1 27  ? 36.035 99.447  41.972 1.00 24.01 ? 468  GLN   B CG  1 
ATOM   3103 C  CD  . GLN   B 1 27  ? 36.741 100.647 42.580 1.00 28.19 ? 468  GLN   B CD  1 
ATOM   3104 O  OE1 . GLN   B 1 27  ? 36.109 101.646 42.923 1.00 25.76 ? 468  GLN   B OE1 1 
ATOM   3105 N  NE2 . GLN   B 1 27  ? 38.063 100.553 42.710 1.00 28.25 ? 468  GLN   B NE2 1 
ATOM   3106 N  N   . ARG   B 1 28  ? 32.375 98.429  42.598 1.00 14.19 ? 469  ARG   B N   1 
ATOM   3107 C  CA  . ARG   B 1 28  ? 31.556 97.224  42.724 1.00 12.95 ? 469  ARG   B CA  1 
ATOM   3108 C  C   . ARG   B 1 28  ? 30.513 97.152  41.607 1.00 13.75 ? 469  ARG   B C   1 
ATOM   3109 O  O   . ARG   B 1 28  ? 30.360 96.115  40.945 1.00 14.29 ? 469  ARG   B O   1 
ATOM   3110 C  CB  . ARG   B 1 28  ? 30.870 97.201  44.088 1.00 12.24 ? 469  ARG   B CB  1 
ATOM   3111 C  CG  . ARG   B 1 28  ? 31.848 96.986  45.233 1.00 12.46 ? 469  ARG   B CG  1 
ATOM   3112 C  CD  . ARG   B 1 28  ? 31.161 97.050  46.605 1.00 15.66 ? 469  ARG   B CD  1 
ATOM   3113 N  NE  . ARG   B 1 28  ? 30.167 95.998  46.752 1.00 17.17 ? 469  ARG   B NE  1 
ATOM   3114 C  CZ  . ARG   B 1 28  ? 28.858 96.192  46.851 1.00 15.19 ? 469  ARG   B CZ  1 
ATOM   3115 N  NH1 . ARG   B 1 28  ? 28.348 97.421  46.843 1.00 14.92 ? 469  ARG   B NH1 1 
ATOM   3116 N  NH2 . ARG   B 1 28  ? 28.065 95.142  46.946 1.00 15.59 ? 469  ARG   B NH2 1 
ATOM   3117 N  N   . ILE   B 1 29  ? 29.824 98.264  41.346 1.00 11.59 ? 470  ILE   B N   1 
ATOM   3118 C  CA  . ILE   B 1 29  ? 28.755 98.223  40.345 1.00 11.81 ? 470  ILE   B CA  1 
ATOM   3119 C  C   . ILE   B 1 29  ? 29.301 98.245  38.922 1.00 14.06 ? 470  ILE   B C   1 
ATOM   3120 O  O   . ILE   B 1 29  ? 28.777 97.548  38.050 1.00 14.55 ? 470  ILE   B O   1 
ATOM   3121 C  CB  . ILE   B 1 29  ? 27.657 99.275  40.578 1.00 13.38 ? 470  ILE   B CB  1 
ATOM   3122 C  CG1 . ILE   B 1 29  ? 28.214 100.701 40.558 1.00 15.29 ? 470  ILE   B CG1 1 
ATOM   3123 C  CG2 . ILE   B 1 29  ? 26.911 98.963  41.879 1.00 14.02 ? 470  ILE   B CG2 1 
ATOM   3124 C  CD1 . ILE   B 1 29  ? 27.130 101.769 40.578 1.00 14.34 ? 470  ILE   B CD1 1 
ATOM   3125 N  N   . SER   B 1 30  ? 30.339 99.046  38.648 1.00 14.13 ? 471  SER   B N   1 
ATOM   3126 C  CA  . SER   B 1 30  ? 30.893 99.039  37.295 1.00 14.36 ? 471  SER   B CA  1 
ATOM   3127 C  C   . SER   B 1 30  ? 31.523 97.698  36.948 1.00 13.39 ? 471  SER   B C   1 
ATOM   3128 O  O   . SER   B 1 30  ? 31.446 97.266  35.799 1.00 15.07 ? 471  SER   B O   1 
ATOM   3129 C  CB  . SER   B 1 30  ? 31.881 100.189 37.093 1.00 15.79 ? 471  SER   B CB  1 
ATOM   3130 O  OG  . SER   B 1 30  ? 32.960 100.088 37.998 1.00 17.04 ? 471  SER   B OG  1 
ATOM   3131 N  N   . ARG   B 1 31  ? 32.123 97.012  37.926 1.00 13.83 ? 472  ARG   B N   1 
ATOM   3132 C  CA  . ARG   B 1 31  ? 32.687 95.690  37.647 1.00 13.13 ? 472  ARG   B CA  1 
ATOM   3133 C  C   . ARG   B 1 31  ? 31.608 94.672  37.304 1.00 14.27 ? 472  ARG   B C   1 
ATOM   3134 O  O   . ARG   B 1 31  ? 31.778 93.864  36.383 1.00 14.15 ? 472  ARG   B O   1 
ATOM   3135 C  CB  . ARG   B 1 31  ? 33.530 95.211  38.822 1.00 14.02 ? 472  ARG   B CB  1 
ATOM   3136 C  CG  . ARG   B 1 31  ? 34.885 95.902  38.890 1.00 12.61 ? 472  ARG   B CG  1 
ATOM   3137 C  CD  . ARG   B 1 31  ? 35.804 95.444  37.751 1.00 14.67 ? 472  ARG   B CD  1 
ATOM   3138 N  NE  . ARG   B 1 31  ? 36.070 94.014  37.840 1.00 14.27 ? 472  ARG   B NE  1 
ATOM   3139 C  CZ  . ARG   B 1 31  ? 37.009 93.476  38.614 1.00 15.30 ? 472  ARG   B CZ  1 
ATOM   3140 N  NH1 . ARG   B 1 31  ? 37.797 94.250  39.347 1.00 16.03 ? 472  ARG   B NH1 1 
ATOM   3141 N  NH2 . ARG   B 1 31  ? 37.159 92.164  38.645 1.00 16.16 ? 472  ARG   B NH2 1 
ATOM   3142 N  N   . ILE   B 1 32  ? 30.500 94.681  38.039 1.00 12.68 ? 473  ILE   B N   1 
ATOM   3143 C  CA  . ILE   B 1 32  ? 29.418 93.759  37.725 1.00 11.88 ? 473  ILE   B CA  1 
ATOM   3144 C  C   . ILE   B 1 32  ? 28.874 94.044  36.333 1.00 12.80 ? 473  ILE   B C   1 
ATOM   3145 O  O   . ILE   B 1 32  ? 28.669 93.130  35.527 1.00 13.42 ? 473  ILE   B O   1 
ATOM   3146 C  CB  . ILE   B 1 32  ? 28.328 93.852  38.803 1.00 12.10 ? 473  ILE   B CB  1 
ATOM   3147 C  CG1 . ILE   B 1 32  ? 28.850 93.324  40.137 1.00 12.75 ? 473  ILE   B CG1 1 
ATOM   3148 C  CG2 . ILE   B 1 32  ? 27.081 93.086  38.363 1.00 14.84 ? 473  ILE   B CG2 1 
ATOM   3149 C  CD1 . ILE   B 1 32  ? 27.979 93.762  41.324 1.00 12.65 ? 473  ILE   B CD1 1 
ATOM   3150 N  N   . PHE   B 1 33  ? 28.656 95.325  36.032 1.00 13.39 ? 474  PHE   B N   1 
ATOM   3151 C  CA  . PHE   B 1 33  ? 28.163 95.730  34.722 1.00 13.31 ? 474  PHE   B CA  1 
ATOM   3152 C  C   . PHE   B 1 33  ? 29.127 95.302  33.627 1.00 14.50 ? 474  PHE   B C   1 
ATOM   3153 O  O   . PHE   B 1 33  ? 28.708 94.746  32.607 1.00 14.83 ? 474  PHE   B O   1 
ATOM   3154 C  CB  . PHE   B 1 33  ? 27.967 97.246  34.726 1.00 13.69 ? 474  PHE   B CB  1 
ATOM   3155 C  CG  . PHE   B 1 33  ? 27.336 97.791  33.479 1.00 14.35 ? 474  PHE   B CG  1 
ATOM   3156 C  CD1 . PHE   B 1 33  ? 25.981 97.650  33.250 1.00 15.96 ? 474  PHE   B CD1 1 
ATOM   3157 C  CD2 . PHE   B 1 33  ? 28.099 98.472  32.551 1.00 16.96 ? 474  PHE   B CD2 1 
ATOM   3158 C  CE1 . PHE   B 1 33  ? 25.404 98.167  32.099 1.00 18.68 ? 474  PHE   B CE1 1 
ATOM   3159 C  CE2 . PHE   B 1 33  ? 27.530 98.983  31.405 1.00 16.86 ? 474  PHE   B CE2 1 
ATOM   3160 C  CZ  . PHE   B 1 33  ? 26.190 98.833  31.184 1.00 17.11 ? 474  PHE   B CZ  1 
ATOM   3161 N  N   . SER   B 1 34  ? 30.429 95.497  33.852 1.00 14.79 ? 475  SER   B N   1 
ATOM   3162 C  CA  . SER   B 1 34  ? 31.421 95.123  32.851 1.00 14.86 ? 475  SER   B CA  1 
ATOM   3163 C  C   . SER   B 1 34  ? 31.397 93.626  32.575 1.00 14.24 ? 475  SER   B C   1 
ATOM   3164 O  O   . SER   B 1 34  ? 31.541 93.198  31.423 1.00 15.44 ? 475  SER   B O   1 
ATOM   3165 C  CB  . SER   B 1 34  ? 32.814 95.550  33.319 1.00 14.09 ? 475  SER   B CB  1 
ATOM   3166 O  OG  . SER   B 1 34  ? 33.822 94.959  32.494 1.00 17.28 ? 475  SER   B OG  1 
ATOM   3167 N  N   . ARG   B 1 35  ? 31.251 92.808  33.620 1.00 14.65 ? 476  ARG   B N   1 
ATOM   3168 C  CA  . ARG   B 1 35  ? 31.202 91.369  33.405 1.00 13.61 ? 476  ARG   B CA  1 
ATOM   3169 C  C   . ARG   B 1 35  ? 29.965 90.978  32.601 1.00 13.59 ? 476  ARG   B C   1 
ATOM   3170 O  O   . ARG   B 1 35  ? 30.025 90.057  31.781 1.00 14.48 ? 476  ARG   B O   1 
ATOM   3171 C  CB  . ARG   B 1 35  ? 31.271 90.619  34.735 1.00 15.17 ? 476  ARG   B CB  1 
ATOM   3172 C  CG  . ARG   B 1 35  ? 31.429 89.108  34.613 1.00 15.86 ? 476  ARG   B CG  1 
ATOM   3173 C  CD  . ARG   B 1 35  ? 32.792 88.715  34.051 1.00 18.03 ? 476  ARG   B CD  1 
ATOM   3174 N  NE  . ARG   B 1 35  ? 32.970 87.265  34.054 1.00 19.13 ? 476  ARG   B NE  1 
ATOM   3175 C  CZ  . ARG   B 1 35  ? 33.574 86.579  33.087 1.00 18.81 ? 476  ARG   B CZ  1 
ATOM   3176 N  NH1 . ARG   B 1 35  ? 34.058 87.203  32.021 1.00 21.24 ? 476  ARG   B NH1 1 
ATOM   3177 N  NH2 . ARG   B 1 35  ? 33.674 85.264  33.179 1.00 18.82 ? 476  ARG   B NH2 1 
ATOM   3178 N  N   . HIS   B 1 36  ? 28.840 91.671  32.818 1.00 13.24 ? 477  HIS   B N   1 
ATOM   3179 C  CA  . HIS   B 1 36  ? 27.664 91.446  31.981 1.00 14.61 ? 477  HIS   B CA  1 
ATOM   3180 C  C   . HIS   B 1 36  ? 27.964 91.733  30.511 1.00 18.99 ? 477  HIS   B C   1 
ATOM   3181 O  O   . HIS   B 1 36  ? 27.511 90.996  29.627 1.00 17.14 ? 477  HIS   B O   1 
ATOM   3182 C  CB  . HIS   B 1 36  ? 26.482 92.288  32.476 1.00 14.82 ? 477  HIS   B CB  1 
ATOM   3183 C  CG  . HIS   B 1 36  ? 25.756 91.710  33.660 1.00 13.96 ? 477  HIS   B CG  1 
ATOM   3184 N  ND1 . HIS   B 1 36  ? 26.261 91.750  34.944 1.00 15.20 ? 477  HIS   B ND1 1 
ATOM   3185 C  CD2 . HIS   B 1 36  ? 24.550 91.101  33.752 1.00 15.19 ? 477  HIS   B CD2 1 
ATOM   3186 C  CE1 . HIS   B 1 36  ? 25.399 91.185  35.772 1.00 16.29 ? 477  HIS   B CE1 1 
ATOM   3187 N  NE2 . HIS   B 1 36  ? 24.350 90.786  35.074 1.00 15.73 ? 477  HIS   B NE2 1 
ATOM   3188 N  N   . GLU   B 1 37  ? 28.715 92.805  30.230 1.00 16.40 ? 478  GLU   B N   1 
ATOM   3189 C  CA  . GLU   B 1 37  ? 29.115 93.105  28.855 1.00 17.80 ? 478  GLU   B CA  1 
ATOM   3190 C  C   . GLU   B 1 37  ? 30.027 92.014  28.309 1.00 17.62 ? 478  GLU   B C   1 
ATOM   3191 O  O   . GLU   B 1 37  ? 29.847 91.535  27.180 1.00 18.53 ? 478  GLU   B O   1 
ATOM   3192 C  CB  . GLU   B 1 37  ? 29.850 94.445  28.824 1.00 22.67 ? 478  GLU   B CB  1 
ATOM   3193 C  CG  . GLU   B 1 37  ? 29.003 95.652  29.153 1.00 37.19 ? 478  GLU   B CG  1 
ATOM   3194 C  CD  . GLU   B 1 37  ? 29.808 96.944  29.178 1.00 50.62 ? 478  GLU   B CD  1 
ATOM   3195 O  OE1 . GLU   B 1 37  ? 29.305 97.966  28.662 1.00 54.96 ? 478  GLU   B OE1 1 
ATOM   3196 O  OE2 . GLU   B 1 37  ? 30.935 96.940  29.721 1.00 57.53 ? 478  GLU   B OE2 1 
ATOM   3197 N  N   . GLU   B 1 38  ? 31.026 91.624  29.103 1.00 17.42 ? 479  GLU   B N   1 
ATOM   3198 C  CA  . GLU   B 1 38  ? 32.026 90.648  28.676 1.00 17.88 ? 479  GLU   B CA  1 
ATOM   3199 C  C   . GLU   B 1 38  ? 31.402 89.313  28.310 1.00 17.91 ? 479  GLU   B C   1 
ATOM   3200 O  O   . GLU   B 1 38  ? 31.852 88.644  27.369 1.00 19.12 ? 479  GLU   B O   1 
ATOM   3201 C  CB  . GLU   B 1 38  ? 32.965 90.413  29.850 1.00 20.85 ? 479  GLU   B CB  1 
ATOM   3202 C  CG  . GLU   B 1 38  ? 34.401 90.321  29.541 1.00 24.90 ? 479  GLU   B CG  1 
ATOM   3203 C  CD  . GLU   B 1 38  ? 35.222 90.429  30.808 1.00 25.65 ? 479  GLU   B CD  1 
ATOM   3204 O  OE1 . GLU   B 1 38  ? 34.859 89.793  31.821 1.00 22.13 ? 479  GLU   B OE1 1 
ATOM   3205 O  OE2 . GLU   B 1 38  ? 36.210 91.180  30.804 1.00 25.71 ? 479  GLU   B OE2 1 
ATOM   3206 N  N   . LEU   B 1 39  ? 30.411 88.878  29.083 1.00 16.75 ? 480  LEU   B N   1 
ATOM   3207 C  CA  . LEU   B 1 39  ? 29.738 87.616  28.825 1.00 16.47 ? 480  LEU   B CA  1 
ATOM   3208 C  C   . LEU   B 1 39  ? 28.604 87.746  27.816 1.00 19.18 ? 480  LEU   B C   1 
ATOM   3209 O  O   . LEU   B 1 39  ? 27.923 86.747  27.554 1.00 18.40 ? 480  LEU   B O   1 
ATOM   3210 C  CB  . LEU   B 1 39  ? 29.203 87.012  30.124 1.00 15.63 ? 480  LEU   B CB  1 
ATOM   3211 C  CG  . LEU   B 1 39  ? 30.274 86.575  31.125 1.00 17.37 ? 480  LEU   B CG  1 
ATOM   3212 C  CD1 . LEU   B 1 39  ? 29.627 86.331  32.482 1.00 18.55 ? 480  LEU   B CD1 1 
ATOM   3213 C  CD2 . LEU   B 1 39  ? 31.014 85.330  30.637 1.00 19.65 ? 480  LEU   B CD2 1 
ATOM   3214 N  N   . ARG   B 1 40  ? 28.380 88.946  27.273 1.00 15.03 ? 481  ARG   B N   1 
ATOM   3215 C  CA  . ARG   B 1 40  ? 27.338 89.198  26.270 1.00 16.49 ? 481  ARG   B CA  1 
ATOM   3216 C  C   . ARG   B 1 40  ? 25.929 89.044  26.836 1.00 19.22 ? 481  ARG   B C   1 
ATOM   3217 O  O   . ARG   B 1 40  ? 24.975 88.782  26.096 1.00 22.42 ? 481  ARG   B O   1 
ATOM   3218 C  CB  . ARG   B 1 40  ? 27.527 88.376  24.991 1.00 21.18 ? 481  ARG   B CB  1 
ATOM   3219 C  CG  . ARG   B 1 40  ? 28.814 88.712  24.266 1.00 28.27 ? 481  ARG   B CG  1 
ATOM   3220 C  CD  . ARG   B 1 40  ? 28.890 87.997  22.926 1.00 34.82 ? 481  ARG   B CD  1 
ATOM   3221 N  NE  . ARG   B 1 40  ? 30.199 88.162  22.304 1.00 38.92 ? 481  ARG   B NE  1 
ATOM   3222 C  CZ  . ARG   B 1 40  ? 30.556 87.592  21.159 1.00 40.72 ? 481  ARG   B CZ  1 
ATOM   3223 N  NH1 . ARG   B 1 40  ? 29.701 86.813  20.507 1.00 39.68 ? 481  ARG   B NH1 1 
ATOM   3224 N  NH2 . ARG   B 1 40  ? 31.769 87.802  20.669 1.00 39.25 ? 481  ARG   B NH2 1 
ATOM   3225 N  N   . LEU   B 1 41  ? 25.790 89.212  28.148 1.00 15.82 ? 482  LEU   B N   1 
ATOM   3226 C  CA  . LEU   B 1 41  ? 24.492 89.208  28.804 1.00 15.30 ? 482  LEU   B CA  1 
ATOM   3227 C  C   . LEU   B 1 41  ? 23.796 90.554  28.711 1.00 16.02 ? 482  LEU   B C   1 
ATOM   3228 O  O   . LEU   B 1 41  ? 22.560 90.606  28.665 1.00 17.34 ? 482  LEU   B O   1 
ATOM   3229 C  CB  . LEU   B 1 41  ? 24.654 88.828  30.279 1.00 16.25 ? 482  LEU   B CB  1 
ATOM   3230 C  CG  . LEU   B 1 41  ? 25.246 87.443  30.544 1.00 15.99 ? 482  LEU   B CG  1 
ATOM   3231 C  CD1 . LEU   B 1 41  ? 25.658 87.311  32.007 1.00 17.33 ? 482  LEU   B CD1 1 
ATOM   3232 C  CD2 . LEU   B 1 41  ? 24.275 86.342  30.174 1.00 17.74 ? 482  LEU   B CD2 1 
ATOM   3233 N  N   . LEU   B 1 42  ? 24.557 91.645  28.673 1.00 16.02 ? 483  LEU   B N   1 
ATOM   3234 C  CA  . LEU   B 1 42  ? 23.957 92.973  28.713 1.00 17.46 ? 483  LEU   B CA  1 
ATOM   3235 C  C   . LEU   B 1 42  ? 23.030 93.196  27.527 1.00 20.42 ? 483  LEU   B C   1 
ATOM   3236 O  O   . LEU   B 1 42  ? 21.900 93.670  27.691 1.00 21.36 ? 483  LEU   B O   1 
ATOM   3237 C  CB  . LEU   B 1 42  ? 25.044 94.041  28.763 1.00 17.18 ? 483  LEU   B CB  1 
ATOM   3238 C  CG  . LEU   B 1 42  ? 24.518 95.477  28.754 1.00 18.42 ? 483  LEU   B CG  1 
ATOM   3239 C  CD1 . LEU   B 1 42  ? 23.608 95.729  29.951 1.00 19.99 ? 483  LEU   B CD1 1 
ATOM   3240 C  CD2 . LEU   B 1 42  ? 25.674 96.457  28.747 1.00 18.38 ? 483  LEU   B CD2 1 
ATOM   3241 N  N   . SER   B 1 43  ? 23.484 92.832  26.326 1.00 19.75 ? 484  SER   B N   1 
ATOM   3242 C  CA  . SER   B 1 43  ? 22.691 93.040  25.117 1.00 19.82 ? 484  SER   B CA  1 
ATOM   3243 C  C   . SER   B 1 43  ? 21.428 92.190  25.085 1.00 20.80 ? 484  SER   B C   1 
ATOM   3244 O  O   . SER   B 1 43  ? 20.498 92.514  24.339 1.00 21.29 ? 484  SER   B O   1 
ATOM   3245 C  CB  . SER   B 1 43  ? 23.544 92.751  23.877 1.00 25.39 ? 484  SER   B CB  1 
ATOM   3246 O  OG  . SER   B 1 43  ? 24.457 93.809  23.648 1.00 31.70 ? 484  SER   B OG  1 
ATOM   3247 N  N   . ARG   B 1 44  ? 21.375 91.113  25.865 1.00 16.81 ? 485  ARG   B N   1 
ATOM   3248 C  CA  . ARG   B 1 44  ? 20.194 90.270  25.947 1.00 18.58 ? 485  ARG   B CA  1 
ATOM   3249 C  C   . ARG   B 1 44  ? 19.138 90.818  26.895 1.00 16.82 ? 485  ARG   B C   1 
ATOM   3250 O  O   . ARG   B 1 44  ? 18.029 90.278  26.929 1.00 19.04 ? 485  ARG   B O   1 
ATOM   3251 C  CB  . ARG   B 1 44  ? 20.596 88.861  26.386 1.00 18.76 ? 485  ARG   B CB  1 
ATOM   3252 C  CG  . ARG   B 1 44  ? 21.613 88.212  25.459 1.00 17.29 ? 485  ARG   B CG  1 
ATOM   3253 C  CD  . ARG   B 1 44  ? 22.137 86.903  26.025 1.00 17.89 ? 485  ARG   B CD  1 
ATOM   3254 N  NE  . ARG   B 1 44  ? 21.077 85.919  26.226 1.00 19.35 ? 485  ARG   B NE  1 
ATOM   3255 C  CZ  . ARG   B 1 44  ? 21.214 84.825  26.975 1.00 19.35 ? 485  ARG   B CZ  1 
ATOM   3256 N  NH1 . ARG   B 1 44  ? 22.367 84.576  27.593 1.00 18.60 ? 485  ARG   B NH1 1 
ATOM   3257 N  NH2 . ARG   B 1 44  ? 20.206 83.984  27.104 1.00 18.83 ? 485  ARG   B NH2 1 
ATOM   3258 N  N   . CYS   B 1 45  ? 19.446 91.878  27.637 1.00 15.77 ? 486  CYS   B N   1 
ATOM   3259 C  CA  . CYS   B 1 45  ? 18.552 92.438  28.636 1.00 16.23 ? 486  CYS   B CA  1 
ATOM   3260 C  C   . CYS   B 1 45  ? 17.947 93.726  28.097 1.00 16.71 ? 486  CYS   B C   1 
ATOM   3261 O  O   . CYS   B 1 45  ? 18.556 94.436  27.294 1.00 19.19 ? 486  CYS   B O   1 
ATOM   3262 C  CB  . CYS   B 1 45  ? 19.367 92.786  29.881 1.00 16.31 ? 486  CYS   B CB  1 
ATOM   3263 S  SG  . CYS   B 1 45  ? 19.905 91.355  30.836 1.00 22.31 ? 486  CYS   B SG  1 
ATOM   3264 N  N   . HIS   B 1 46  ? 16.751 94.047  28.578 1.00 15.94 ? 487  HIS   B N   1 
ATOM   3265 C  CA  . HIS   B 1 46  ? 16.161 95.347  28.308 1.00 17.04 ? 487  HIS   B CA  1 
ATOM   3266 C  C   . HIS   B 1 46  ? 16.591 96.335  29.389 1.00 16.51 ? 487  HIS   B C   1 
ATOM   3267 O  O   . HIS   B 1 46  ? 16.391 96.087  30.583 1.00 17.71 ? 487  HIS   B O   1 
ATOM   3268 C  CB  . HIS   B 1 46  ? 14.641 95.220  28.277 1.00 16.51 ? 487  HIS   B CB  1 
ATOM   3269 C  CG  . HIS   B 1 46  ? 13.931 96.523  28.101 1.00 21.43 ? 487  HIS   B CG  1 
ATOM   3270 N  ND1 . HIS   B 1 46  ? 13.922 97.209  26.906 1.00 23.89 ? 487  HIS   B ND1 1 
ATOM   3271 C  CD2 . HIS   B 1 46  ? 13.206 97.269  28.968 1.00 24.78 ? 487  HIS   B CD2 1 
ATOM   3272 C  CE1 . HIS   B 1 46  ? 13.220 98.320  27.042 1.00 25.82 ? 487  HIS   B CE1 1 
ATOM   3273 N  NE2 . HIS   B 1 46  ? 12.772 98.379  28.284 1.00 25.62 ? 487  HIS   B NE2 1 
ATOM   3274 N  N   . ARG   B 1 47  ? 17.157 97.462  28.978 1.00 16.01 ? 488  ARG   B N   1 
ATOM   3275 C  CA  . ARG   B 1 47  ? 17.678 98.429  29.935 1.00 17.49 ? 488  ARG   B CA  1 
ATOM   3276 C  C   . ARG   B 1 47  ? 16.527 99.212  30.560 1.00 19.97 ? 488  ARG   B C   1 
ATOM   3277 O  O   . ARG   B 1 47  ? 15.709 99.807  29.849 1.00 21.33 ? 488  ARG   B O   1 
ATOM   3278 C  CB  . ARG   B 1 47  ? 18.656 99.363  29.230 1.00 16.92 ? 488  ARG   B CB  1 
ATOM   3279 C  CG  . ARG   B 1 47  ? 19.523 100.153 30.136 1.00 19.68 ? 488  ARG   B CG  1 
ATOM   3280 C  CD  . ARG   B 1 47  ? 20.531 99.277  30.851 1.00 20.53 ? 488  ARG   B CD  1 
ATOM   3281 N  NE  . ARG   B 1 47  ? 21.370 100.139 31.654 1.00 20.84 ? 488  ARG   B NE  1 
ATOM   3282 C  CZ  . ARG   B 1 47  ? 22.523 100.653 31.246 1.00 19.93 ? 488  ARG   B CZ  1 
ATOM   3283 N  NH1 . ARG   B 1 47  ? 23.013 100.362 30.038 1.00 18.47 ? 488  ARG   B NH1 1 
ATOM   3284 N  NH2 . ARG   B 1 47  ? 23.189 101.454 32.061 1.00 25.05 ? 488  ARG   B NH2 1 
ATOM   3285 N  N   . ILE   B 1 48  ? 16.452 99.197  31.881 1.00 18.98 ? 489  ILE   B N   1 
ATOM   3286 C  CA  . ILE   B 1 48  ? 15.456 99.960  32.631 1.00 17.32 ? 489  ILE   B CA  1 
ATOM   3287 C  C   . ILE   B 1 48  ? 16.142 101.208 33.175 1.00 18.60 ? 489  ILE   B C   1 
ATOM   3288 O  O   . ILE   B 1 48  ? 17.220 101.094 33.774 1.00 19.27 ? 489  ILE   B O   1 
ATOM   3289 C  CB  . ILE   B 1 48  ? 14.844 99.123  33.771 1.00 16.45 ? 489  ILE   B CB  1 
ATOM   3290 C  CG1 . ILE   B 1 48  ? 14.049 97.951  33.194 1.00 17.18 ? 489  ILE   B CG1 1 
ATOM   3291 C  CG2 . ILE   B 1 48  ? 13.976 99.987  34.689 1.00 17.27 ? 489  ILE   B CG2 1 
ATOM   3292 C  CD1 . ILE   B 1 48  ? 13.702 96.872  34.203 1.00 20.60 ? 489  ILE   B CD1 1 
ATOM   3293 N  N   . PRO   B 1 49  ? 15.578 102.395 32.981 1.00 22.21 ? 490  PRO   B N   1 
ATOM   3294 C  CA  . PRO   B 1 49  ? 16.254 103.606 33.451 1.00 21.82 ? 490  PRO   B CA  1 
ATOM   3295 C  C   . PRO   B 1 49  ? 16.232 103.706 34.968 1.00 21.08 ? 490  PRO   B C   1 
ATOM   3296 O  O   . PRO   B 1 49  ? 15.280 103.284 35.630 1.00 23.74 ? 490  PRO   B O   1 
ATOM   3297 C  CB  . PRO   B 1 49  ? 15.431 104.735 32.822 1.00 25.71 ? 490  PRO   B CB  1 
ATOM   3298 C  CG  . PRO   B 1 49  ? 14.083 104.134 32.618 1.00 26.29 ? 490  PRO   B CG  1 
ATOM   3299 C  CD  . PRO   B 1 49  ? 14.336 102.701 32.255 1.00 23.46 ? 490  PRO   B CD  1 
ATOM   3300 N  N   . ALA   B 1 50  ? 17.305 104.265 35.515 1.00 20.96 ? 491  ALA   B N   1 
ATOM   3301 C  CA  . ALA   B 1 50  ? 17.327 104.652 36.913 1.00 21.62 ? 491  ALA   B CA  1 
ATOM   3302 C  C   . ALA   B 1 50  ? 16.519 105.931 37.109 1.00 22.49 ? 491  ALA   B C   1 
ATOM   3303 O  O   . ALA   B 1 50  ? 16.284 106.700 36.172 1.00 26.07 ? 491  ALA   B O   1 
ATOM   3304 C  CB  . ALA   B 1 50  ? 18.766 104.889 37.376 1.00 21.07 ? 491  ALA   B CB  1 
ATOM   3305 N  N   . ARG   B 1 51  ? 16.066 106.139 38.342 1.00 19.39 ? 492  ARG   B N   1 
ATOM   3306 C  CA  . ARG   B 1 51  ? 15.457 107.401 38.728 1.00 18.22 ? 492  ARG   B CA  1 
ATOM   3307 C  C   . ARG   B 1 51  ? 15.680 107.603 40.215 1.00 20.87 ? 492  ARG   B C   1 
ATOM   3308 O  O   . ARG   B 1 51  ? 16.053 106.675 40.938 1.00 19.35 ? 492  ARG   B O   1 
ATOM   3309 C  CB  . ARG   B 1 51  ? 13.957 107.458 38.405 1.00 17.79 ? 492  ARG   B CB  1 
ATOM   3310 C  CG  . ARG   B 1 51  ? 13.069 106.707 39.394 1.00 17.81 ? 492  ARG   B CG  1 
ATOM   3311 C  CD  . ARG   B 1 51  ? 11.613 107.097 39.172 1.00 18.17 ? 492  ARG   B CD  1 
ATOM   3312 N  NE  . ARG   B 1 51  ? 10.641 106.189 39.780 1.00 19.04 ? 492  ARG   B NE  1 
ATOM   3313 C  CZ  . ARG   B 1 51  ? 10.176 106.324 41.019 1.00 18.55 ? 492  ARG   B CZ  1 
ATOM   3314 N  NH1 . ARG   B 1 51  ? 10.626 107.310 41.782 1.00 18.85 ? 492  ARG   B NH1 1 
ATOM   3315 N  NH2 . ARG   B 1 51  ? 9.266  105.481 41.500 1.00 17.02 ? 492  ARG   B NH2 1 
ATOM   3316 N  N   . LEU   B 1 52  ? 15.461 108.835 40.658 1.00 18.59 ? 493  LEU   B N   1 
ATOM   3317 C  CA  . LEU   B 1 52  ? 15.521 109.168 42.071 1.00 19.13 ? 493  LEU   B CA  1 
ATOM   3318 C  C   . LEU   B 1 52  ? 14.217 108.762 42.745 1.00 18.12 ? 493  LEU   B C   1 
ATOM   3319 O  O   . LEU   B 1 52  ? 13.128 109.073 42.245 1.00 19.89 ? 493  LEU   B O   1 
ATOM   3320 C  CB  . LEU   B 1 52  ? 15.687 110.679 42.223 1.00 20.58 ? 493  LEU   B CB  1 
ATOM   3321 C  CG  . LEU   B 1 52  ? 16.986 111.338 41.755 1.00 26.24 ? 493  LEU   B CG  1 
ATOM   3322 C  CD1 . LEU   B 1 52  ? 16.832 112.850 41.792 1.00 29.85 ? 493  LEU   B CD1 1 
ATOM   3323 C  CD2 . LEU   B 1 52  ? 18.150 110.917 42.625 1.00 25.97 ? 493  LEU   B CD2 1 
ATOM   3324 N  N   . ALA   B 1 53  ? 14.321 108.073 43.879 1.00 16.44 ? 494  ALA   B N   1 
ATOM   3325 C  CA  . ALA   B 1 53  ? 13.167 107.920 44.753 1.00 17.41 ? 494  ALA   B CA  1 
ATOM   3326 C  C   . ALA   B 1 53  ? 12.754 109.292 45.286 1.00 19.25 ? 494  ALA   B C   1 
ATOM   3327 O  O   . ALA   B 1 53  ? 13.586 110.185 45.478 1.00 19.86 ? 494  ALA   B O   1 
ATOM   3328 C  CB  . ALA   B 1 53  ? 13.516 106.998 45.925 1.00 17.79 ? 494  ALA   B CB  1 
ATOM   3329 N  N   . THR   B 1 54  ? 11.456 109.470 45.513 1.00 18.03 ? 495  THR   B N   1 
ATOM   3330 C  CA  . THR   B 1 54  ? 10.994 110.694 46.147 1.00 18.74 ? 495  THR   B CA  1 
ATOM   3331 C  C   . THR   B 1 54  ? 11.010 110.540 47.663 1.00 17.05 ? 495  THR   B C   1 
ATOM   3332 O  O   . THR   B 1 54  ? 11.055 109.429 48.199 1.00 17.65 ? 495  THR   B O   1 
ATOM   3333 C  CB  . THR   B 1 54  ? 9.573  111.031 45.705 1.00 22.70 ? 495  THR   B CB  1 
ATOM   3334 O  OG1 . THR   B 1 54  ? 8.669  110.083 46.285 1.00 21.02 ? 495  THR   B OG1 1 
ATOM   3335 C  CG2 . THR   B 1 54  ? 9.455  111.001 44.186 1.00 23.18 ? 495  THR   B CG2 1 
ATOM   3336 N  N   . GLU   B 1 55  ? 10.942 111.677 48.362 1.00 18.94 ? 496  GLU   B N   1 
ATOM   3337 C  CA  . GLU   B 1 55  ? 10.867 111.623 49.820 1.00 20.85 ? 496  GLU   B CA  1 
ATOM   3338 C  C   . GLU   B 1 55  ? 9.594  110.926 50.284 1.00 19.84 ? 496  GLU   B C   1 
ATOM   3339 O  O   . GLU   B 1 55  ? 9.600  110.238 51.312 1.00 17.90 ? 496  GLU   B O   1 
ATOM   3340 C  CB  . GLU   B 1 55  ? 10.980 113.030 50.419 1.00 21.98 ? 496  GLU   B CB  1 
ATOM   3341 C  CG  . GLU   B 1 55  ? 12.335 113.699 50.192 1.00 26.78 ? 496  GLU   B CG  1 
ATOM   3342 C  CD  . GLU   B 1 55  ? 12.416 115.101 50.784 1.00 30.13 ? 496  GLU   B CD  1 
ATOM   3343 O  OE1 . GLU   B 1 55  ? 11.877 115.319 51.890 1.00 32.35 ? 496  GLU   B OE1 1 
ATOM   3344 O  OE2 . GLU   B 1 55  ? 13.020 115.987 50.138 1.00 29.07 ? 496  GLU   B OE2 1 
ATOM   3345 N  N   . GLU   B 1 56  ? 8.494  111.090 49.542 1.00 19.98 ? 497  GLU   B N   1 
ATOM   3346 C  CA  . GLU   B 1 56  ? 7.261  110.390 49.886 1.00 24.77 ? 497  GLU   B CA  1 
ATOM   3347 C  C   . GLU   B 1 56  ? 7.448  108.884 49.786 1.00 20.95 ? 497  GLU   B C   1 
ATOM   3348 O  O   . GLU   B 1 56  ? 6.975  108.133 50.648 1.00 19.99 ? 497  GLU   B O   1 
ATOM   3349 C  CB  . GLU   B 1 56  ? 6.126  110.838 48.966 1.00 32.17 ? 497  GLU   B CB  1 
ATOM   3350 C  CG  . GLU   B 1 56  ? 5.687  112.259 49.188 1.00 44.01 ? 497  GLU   B CG  1 
ATOM   3351 C  CD  . GLU   B 1 56  ? 6.678  113.243 48.607 1.00 56.27 ? 497  GLU   B CD  1 
ATOM   3352 O  OE1 . GLU   B 1 56  ? 7.049  113.089 47.432 1.00 59.14 ? 497  GLU   B OE1 1 
ATOM   3353 O  OE2 . GLU   B 1 56  ? 7.115  114.152 49.333 1.00 59.40 ? 497  GLU   B OE2 1 
ATOM   3354 N  N   . GLU   B 1 57  ? 8.138  108.425 48.737 1.00 18.11 ? 498  GLU   B N   1 
ATOM   3355 C  CA  . GLU   B 1 57  ? 8.442  107.005 48.623 1.00 16.91 ? 498  GLU   B CA  1 
ATOM   3356 C  C   . GLU   B 1 57  ? 9.320  106.533 49.778 1.00 15.36 ? 498  GLU   B C   1 
ATOM   3357 O  O   . GLU   B 1 57  ? 9.062  105.475 50.367 1.00 16.08 ? 498  GLU   B O   1 
ATOM   3358 C  CB  . GLU   B 1 57  ? 9.079  106.717 47.265 1.00 17.87 ? 498  GLU   B CB  1 
ATOM   3359 C  CG  . GLU   B 1 57  ? 8.046  106.766 46.136 1.00 19.18 ? 498  GLU   B CG  1 
ATOM   3360 C  CD  . GLU   B 1 57  ? 8.643  106.885 44.736 1.00 18.25 ? 498  GLU   B CD  1 
ATOM   3361 O  OE1 . GLU   B 1 57  ? 9.813  107.319 44.579 1.00 16.81 ? 498  GLU   B OE1 1 
ATOM   3362 O  OE2 . GLU   B 1 57  ? 7.910  106.576 43.765 1.00 18.64 ? 498  GLU   B OE2 1 
ATOM   3363 N  N   . LEU   B 1 58  ? 10.347 107.306 50.140 1.00 15.77 ? 499  LEU   B N   1 
ATOM   3364 C  CA  . LEU   B 1 58  ? 11.164 106.914 51.286 1.00 18.31 ? 499  LEU   B CA  1 
ATOM   3365 C  C   . LEU   B 1 58  ? 10.321 106.759 52.544 1.00 19.95 ? 499  LEU   B C   1 
ATOM   3366 O  O   . LEU   B 1 58  ? 10.615 105.901 53.382 1.00 18.38 ? 499  LEU   B O   1 
ATOM   3367 C  CB  . LEU   B 1 58  ? 12.275 107.928 51.534 1.00 16.97 ? 499  LEU   B CB  1 
ATOM   3368 C  CG  . LEU   B 1 58  ? 13.329 108.125 50.457 1.00 15.03 ? 499  LEU   B CG  1 
ATOM   3369 C  CD1 . LEU   B 1 58  ? 14.338 109.112 50.995 1.00 19.57 ? 499  LEU   B CD1 1 
ATOM   3370 C  CD2 . LEU   B 1 58  ? 13.997 106.805 50.091 1.00 14.94 ? 499  LEU   B CD2 1 
ATOM   3371 N  N   . ALA   B 1 59  ? 9.254  107.555 52.678 1.00 17.70 ? 500  ALA   B N   1 
ATOM   3372 C  CA  . ALA   B 1 59  ? 8.407  107.500 53.862 1.00 16.97 ? 500  ALA   B CA  1 
ATOM   3373 C  C   . ALA   B 1 59  ? 7.583  106.224 53.941 1.00 15.86 ? 500  ALA   B C   1 
ATOM   3374 O  O   . ALA   B 1 59  ? 6.956  105.980 54.981 1.00 18.64 ? 500  ALA   B O   1 
ATOM   3375 C  CB  . ALA   B 1 59  ? 7.484  108.720 53.904 1.00 18.82 ? 500  ALA   B CB  1 
ATOM   3376 N  N   . LEU   B 1 60  ? 7.561  105.415 52.878 1.00 16.79 ? 501  LEU   B N   1 
ATOM   3377 C  CA  . LEU   B 1 60  ? 6.925  104.108 52.966 1.00 17.55 ? 501  LEU   B CA  1 
ATOM   3378 C  C   . LEU   B 1 60  ? 7.553  103.251 54.058 1.00 17.40 ? 501  LEU   B C   1 
ATOM   3379 O  O   . LEU   B 1 60  ? 6.864  102.422 54.670 1.00 19.37 ? 501  LEU   B O   1 
ATOM   3380 C  CB  . LEU   B 1 60  ? 7.036  103.391 51.627 1.00 18.67 ? 501  LEU   B CB  1 
ATOM   3381 C  CG  . LEU   B 1 60  ? 6.213  103.982 50.485 1.00 17.52 ? 501  LEU   B CG  1 
ATOM   3382 C  CD1 . LEU   B 1 60  ? 6.625  103.354 49.163 1.00 19.15 ? 501  LEU   B CD1 1 
ATOM   3383 C  CD2 . LEU   B 1 60  ? 4.702  103.823 50.747 1.00 19.88 ? 501  LEU   B CD2 1 
ATOM   3384 N  N   . CYS   B 1 61  ? 8.853  103.438 54.323 1.00 15.92 ? 502  CYS   B N   1 
ATOM   3385 C  CA  . CYS   B 1 61  ? 9.560  102.613 55.290 1.00 16.29 ? 502  CYS   B CA  1 
ATOM   3386 C  C   . CYS   B 1 61  ? 10.333 103.398 56.339 1.00 16.09 ? 502  CYS   B C   1 
ATOM   3387 O  O   . CYS   B 1 61  ? 10.641 102.829 57.396 1.00 17.51 ? 502  CYS   B O   1 
ATOM   3388 C  CB  . CYS   B 1 61  ? 10.568 101.720 54.561 1.00 15.45 ? 502  CYS   B CB  1 
ATOM   3389 S  SG  . CYS   B 1 61  ? 9.798  100.437 53.573 1.00 18.29 ? 502  CYS   B SG  1 
ATOM   3390 N  N   . HIS   B 1 62  ? 10.664 104.665 56.096 1.00 15.36 ? 503  HIS   B N   1 
ATOM   3391 C  CA  . HIS   B 1 62  ? 11.595 105.389 56.950 1.00 16.52 ? 503  HIS   B CA  1 
ATOM   3392 C  C   . HIS   B 1 62  ? 10.932 106.581 57.625 1.00 17.17 ? 503  HIS   B C   1 
ATOM   3393 O  O   . HIS   B 1 62  ? 9.993  107.181 57.093 1.00 17.57 ? 503  HIS   B O   1 
ATOM   3394 C  CB  . HIS   B 1 62  ? 12.817 105.835 56.153 1.00 15.44 ? 503  HIS   B CB  1 
ATOM   3395 C  CG  . HIS   B 1 62  ? 13.647 104.692 55.666 1.00 13.95 ? 503  HIS   B CG  1 
ATOM   3396 N  ND1 . HIS   B 1 62  ? 14.445 103.953 56.513 1.00 14.85 ? 503  HIS   B ND1 1 
ATOM   3397 C  CD2 . HIS   B 1 62  ? 13.781 104.138 54.437 1.00 13.89 ? 503  HIS   B CD2 1 
ATOM   3398 C  CE1 . HIS   B 1 62  ? 15.034 102.991 55.825 1.00 14.70 ? 503  HIS   B CE1 1 
ATOM   3399 N  NE2 . HIS   B 1 62  ? 14.660 103.089 54.563 1.00 14.89 ? 503  HIS   B NE2 1 
ATOM   3400 N  N   . SER   B 1 63  ? 11.430 106.903 58.816 1.00 16.77 ? 504  SER   B N   1 
ATOM   3401 C  CA  . SER   B 1 63  ? 10.917 108.032 59.572 1.00 17.29 ? 504  SER   B CA  1 
ATOM   3402 C  C   . SER   B 1 63  ? 11.309 109.342 58.902 1.00 16.88 ? 504  SER   B C   1 
ATOM   3403 O  O   . SER   B 1 63  ? 12.324 109.433 58.207 1.00 15.74 ? 504  SER   B O   1 
ATOM   3404 C  CB  . SER   B 1 63  ? 11.524 108.037 60.969 1.00 17.91 ? 504  SER   B CB  1 
ATOM   3405 O  OG  . SER   B 1 63  ? 12.914 108.340 60.900 1.00 18.28 ? 504  SER   B OG  1 
ATOM   3406 N  N   A SER   B 1 64  ? 10.493 110.369 59.133 0.87 17.40 ? 505  SER   B N   1 
ATOM   3407 N  N   B SER   B 1 64  ? 10.494 110.375 59.128 0.13 16.89 ? 505  SER   B N   1 
ATOM   3408 C  CA  A SER   B 1 64  ? 10.798 111.678 58.566 0.87 18.84 ? 505  SER   B CA  1 
ATOM   3409 C  CA  B SER   B 1 64  ? 10.798 111.683 58.554 0.13 18.43 ? 505  SER   B CA  1 
ATOM   3410 C  C   A SER   B 1 64  ? 12.118 112.217 59.097 0.87 16.07 ? 505  SER   B C   1 
ATOM   3411 C  C   B SER   B 1 64  ? 12.099 112.252 59.107 0.13 17.20 ? 505  SER   B C   1 
ATOM   3412 O  O   A SER   B 1 64  ? 12.860 112.874 58.362 0.87 18.13 ? 505  SER   B O   1 
ATOM   3413 O  O   B SER   B 1 64  ? 12.806 112.979 58.400 0.13 19.01 ? 505  SER   B O   1 
ATOM   3414 C  CB  A SER   B 1 64  ? 9.654  112.656 58.850 0.87 19.87 ? 505  SER   B CB  1 
ATOM   3415 C  CB  B SER   B 1 64  ? 9.636  112.650 58.792 0.13 18.09 ? 505  SER   B CB  1 
ATOM   3416 O  OG  A SER   B 1 64  ? 9.512  112.888 60.239 0.87 20.75 ? 505  SER   B OG  1 
ATOM   3417 O  OG  B SER   B 1 64  ? 9.959  113.957 58.348 0.13 21.47 ? 505  SER   B OG  1 
ATOM   3418 N  N   . LYS   B 1 65  ? 12.434 111.930 60.359 1.00 16.25 ? 506  LYS   B N   1 
ATOM   3419 C  CA  . LYS   B 1 65  ? 13.693 112.396 60.936 1.00 18.72 ? 506  LYS   B CA  1 
ATOM   3420 C  C   . LYS   B 1 65  ? 14.891 111.795 60.211 1.00 17.99 ? 506  LYS   B C   1 
ATOM   3421 O  O   . LYS   B 1 65  ? 15.831 112.510 59.841 1.00 16.55 ? 506  LYS   B O   1 
ATOM   3422 C  CB  . LYS   B 1 65  ? 13.745 112.028 62.419 1.00 19.37 ? 506  LYS   B CB  1 
ATOM   3423 C  CG  . LYS   B 1 65  ? 15.031 112.474 63.121 1.00 27.08 ? 506  LYS   B CG  1 
ATOM   3424 C  CD  . LYS   B 1 65  ? 15.064 111.994 64.563 1.00 35.05 ? 506  LYS   B CD  1 
ATOM   3425 C  CE  . LYS   B 1 65  ? 16.266 111.099 64.819 1.00 46.11 ? 506  LYS   B CE  1 
ATOM   3426 N  NZ  . LYS   B 1 65  ? 16.852 111.317 66.170 1.00 50.82 ? 506  LYS   B NZ  1 
ATOM   3427 N  N   . HIS   B 1 66  ? 14.882 110.474 60.020 1.00 17.01 ? 507  HIS   B N   1 
ATOM   3428 C  CA  . HIS   B 1 66  ? 15.984 109.809 59.333 1.00 16.08 ? 507  HIS   B CA  1 
ATOM   3429 C  C   . HIS   B 1 66  ? 16.134 110.310 57.902 1.00 16.36 ? 507  HIS   B C   1 
ATOM   3430 O  O   . HIS   B 1 66  ? 17.251 110.570 57.438 1.00 17.49 ? 507  HIS   B O   1 
ATOM   3431 C  CB  . HIS   B 1 66  ? 15.765 108.300 59.340 1.00 14.76 ? 507  HIS   B CB  1 
ATOM   3432 C  CG  . HIS   B 1 66  ? 16.809 107.542 58.584 1.00 17.04 ? 507  HIS   B CG  1 
ATOM   3433 N  ND1 . HIS   B 1 66  ? 18.151 107.621 58.891 1.00 17.15 ? 507  HIS   B ND1 1 
ATOM   3434 C  CD2 . HIS   B 1 66  ? 16.710 106.712 57.519 1.00 17.94 ? 507  HIS   B CD2 1 
ATOM   3435 C  CE1 . HIS   B 1 66  ? 18.834 106.862 58.050 1.00 17.94 ? 507  HIS   B CE1 1 
ATOM   3436 N  NE2 . HIS   B 1 66  ? 17.985 106.299 57.209 1.00 19.00 ? 507  HIS   B NE2 1 
ATOM   3437 N  N   . ILE   B 1 67  ? 15.024 110.423 57.173 1.00 14.62 ? 508  ILE   B N   1 
ATOM   3438 C  CA  . ILE   B 1 67  ? 15.084 110.984 55.827 1.00 16.06 ? 508  ILE   B CA  1 
ATOM   3439 C  C   . ILE   B 1 67  ? 15.723 112.362 55.855 1.00 18.46 ? 508  ILE   B C   1 
ATOM   3440 O  O   . ILE   B 1 67  ? 16.587 112.679 55.034 1.00 16.93 ? 508  ILE   B O   1 
ATOM   3441 C  CB  . ILE   B 1 67  ? 13.681 111.025 55.197 1.00 16.40 ? 508  ILE   B CB  1 
ATOM   3442 C  CG1 . ILE   B 1 67  ? 13.131 109.605 55.040 1.00 15.09 ? 508  ILE   B CG1 1 
ATOM   3443 C  CG2 . ILE   B 1 67  ? 13.738 111.770 53.870 1.00 18.60 ? 508  ILE   B CG2 1 
ATOM   3444 C  CD1 . ILE   B 1 67  ? 11.629 109.539 54.808 1.00 16.38 ? 508  ILE   B CD1 1 
ATOM   3445 N  N   . SER   B 1 68  ? 15.329 113.200 56.816 1.00 19.68 ? 509  SER   B N   1 
ATOM   3446 C  CA  . SER   B 1 68  ? 15.812 114.572 56.780 1.00 18.79 ? 509  SER   B CA  1 
ATOM   3447 C  C   . SER   B 1 68  ? 17.289 114.671 57.141 1.00 20.46 ? 509  SER   B C   1 
ATOM   3448 O  O   . SER   B 1 68  ? 17.983 115.559 56.644 1.00 18.88 ? 509  SER   B O   1 
ATOM   3449 C  CB  . SER   B 1 68  ? 14.980 115.455 57.689 1.00 24.10 ? 509  SER   B CB  1 
ATOM   3450 O  OG  . SER   B 1 68  ? 15.309 116.805 57.436 1.00 35.12 ? 509  SER   B OG  1 
ATOM   3451 N  N   . ILE   B 1 69  ? 17.786 113.785 58.000 1.00 17.56 ? 510  ILE   B N   1 
ATOM   3452 C  CA  . ILE   B 1 69  ? 19.198 113.849 58.365 1.00 18.17 ? 510  ILE   B CA  1 
ATOM   3453 C  C   . ILE   B 1 69  ? 20.080 113.406 57.205 1.00 17.67 ? 510  ILE   B C   1 
ATOM   3454 O  O   . ILE   B 1 69  ? 21.063 114.078 56.864 1.00 18.32 ? 510  ILE   B O   1 
ATOM   3455 C  CB  . ILE   B 1 69  ? 19.466 113.080 59.671 1.00 25.37 ? 510  ILE   B CB  1 
ATOM   3456 C  CG1 . ILE   B 1 69  ? 20.940 113.131 60.046 1.00 27.80 ? 510  ILE   B CG1 1 
ATOM   3457 C  CG2 . ILE   B 1 69  ? 19.032 111.658 59.573 1.00 26.54 ? 510  ILE   B CG2 1 
ATOM   3458 C  CD1 . ILE   B 1 69  ? 21.137 112.946 61.521 1.00 32.49 ? 510  ILE   B CD1 1 
ATOM   3459 N  N   . ILE   B 1 70  ? 19.734 112.293 56.552 1.00 16.15 ? 511  ILE   B N   1 
ATOM   3460 C  CA  . ILE   B 1 70  ? 20.519 111.874 55.392 1.00 15.35 ? 511  ILE   B CA  1 
ATOM   3461 C  C   . ILE   B 1 70  ? 20.433 112.919 54.292 1.00 15.79 ? 511  ILE   B C   1 
ATOM   3462 O  O   . ILE   B 1 70  ? 21.434 113.245 53.643 1.00 17.67 ? 511  ILE   B O   1 
ATOM   3463 C  CB  . ILE   B 1 70  ? 20.100 110.476 54.902 1.00 14.75 ? 511  ILE   B CB  1 
ATOM   3464 C  CG1 . ILE   B 1 70  ? 20.176 109.475 56.059 1.00 15.84 ? 511  ILE   B CG1 1 
ATOM   3465 C  CG2 . ILE   B 1 70  ? 20.981 110.030 53.730 1.00 15.92 ? 511  ILE   B CG2 1 
ATOM   3466 C  CD1 . ILE   B 1 70  ? 21.530 109.452 56.753 1.00 17.54 ? 511  ILE   B CD1 1 
ATOM   3467 N  N   . LYS   B 1 71  ? 19.237 113.473 54.075 1.00 16.02 ? 512  LYS   B N   1 
ATOM   3468 C  CA  . LYS   B 1 71  ? 19.081 114.551 53.109 1.00 16.78 ? 512  LYS   B CA  1 
ATOM   3469 C  C   . LYS   B 1 71  ? 19.999 115.725 53.438 1.00 16.18 ? 512  LYS   B C   1 
ATOM   3470 O  O   . LYS   B 1 71  ? 20.632 116.291 52.537 1.00 19.11 ? 512  LYS   B O   1 
ATOM   3471 C  CB  . LYS   B 1 71  ? 17.611 114.980 53.053 1.00 16.38 ? 512  LYS   B CB  1 
ATOM   3472 C  CG  . LYS   B 1 71  ? 17.332 116.167 52.152 1.00 19.39 ? 512  LYS   B CG  1 
ATOM   3473 C  CD  . LYS   B 1 71  ? 15.855 116.541 52.196 1.00 24.74 ? 512  LYS   B CD  1 
ATOM   3474 C  CE  . LYS   B 1 71  ? 15.603 117.905 51.574 1.00 28.71 ? 512  LYS   B CE  1 
ATOM   3475 N  NZ  . LYS   B 1 71  ? 14.200 118.341 51.809 1.00 31.10 ? 512  LYS   B NZ  1 
ATOM   3476 N  N   . SER   B 1 72  ? 20.104 116.085 54.726 1.00 19.51 ? 513  SER   B N   1 
ATOM   3477 C  CA  . SER   B 1 72  ? 20.922 117.227 55.129 1.00 18.54 ? 513  SER   B CA  1 
ATOM   3478 C  C   . SER   B 1 72  ? 22.397 117.008 54.824 1.00 23.00 ? 513  SER   B C   1 
ATOM   3479 O  O   . SER   B 1 72  ? 23.141 117.987 54.695 1.00 25.61 ? 513  SER   B O   1 
ATOM   3480 C  CB  . SER   B 1 72  ? 20.732 117.554 56.620 1.00 19.31 ? 513  SER   B CB  1 
ATOM   3481 O  OG  . SER   B 1 72  ? 21.458 116.678 57.475 1.00 20.40 ? 513  SER   B OG  1 
ATOM   3482 N  N   . SER   B 1 73  ? 22.840 115.751 54.695 1.00 21.19 ? 514  SER   B N   1 
ATOM   3483 C  CA  . SER   B 1 73  ? 24.260 115.508 54.470 1.00 18.27 ? 514  SER   B CA  1 
ATOM   3484 C  C   . SER   B 1 73  ? 24.717 115.996 53.103 1.00 18.13 ? 514  SER   B C   1 
ATOM   3485 O  O   . SER   B 1 73  ? 25.916 116.231 52.922 1.00 20.76 ? 514  SER   B O   1 
ATOM   3486 C  CB  . SER   B 1 73  ? 24.603 114.024 54.650 1.00 19.04 ? 514  SER   B CB  1 
ATOM   3487 O  OG  . SER   B 1 73  ? 24.051 113.240 53.603 1.00 20.58 ? 514  SER   B OG  1 
ATOM   3488 N  N   . GLU   B 1 74  ? 23.796 116.168 52.146 1.00 19.88 ? 515  GLU   B N   1 
ATOM   3489 C  CA  . GLU   B 1 74  ? 24.192 116.614 50.810 1.00 20.73 ? 515  GLU   B CA  1 
ATOM   3490 C  C   . GLU   B 1 74  ? 24.866 117.983 50.840 1.00 23.44 ? 515  GLU   B C   1 
ATOM   3491 O  O   . GLU   B 1 74  ? 25.683 118.289 49.964 1.00 25.10 ? 515  GLU   B O   1 
ATOM   3492 C  CB  . GLU   B 1 74  ? 22.978 116.629 49.874 1.00 22.92 ? 515  GLU   B CB  1 
ATOM   3493 C  CG  . GLU   B 1 74  ? 23.275 117.070 48.435 1.00 33.47 ? 515  GLU   B CG  1 
ATOM   3494 C  CD  . GLU   B 1 74  ? 22.150 116.747 47.455 1.00 38.25 ? 515  GLU   B CD  1 
ATOM   3495 O  OE1 . GLU   B 1 74  ? 21.122 116.174 47.874 1.00 38.46 ? 515  GLU   B OE1 1 
ATOM   3496 O  OE2 . GLU   B 1 74  ? 22.299 117.067 46.256 1.00 42.16 ? 515  GLU   B OE2 1 
ATOM   3497 N  N   . HIS   B 1 75  ? 24.551 118.815 51.838 1.00 27.59 ? 516  HIS   B N   1 
ATOM   3498 C  CA  . HIS   B 1 75  ? 25.106 120.162 51.937 1.00 27.97 ? 516  HIS   B CA  1 
ATOM   3499 C  C   . HIS   B 1 75  ? 26.127 120.301 53.060 1.00 28.12 ? 516  HIS   B C   1 
ATOM   3500 O  O   . HIS   B 1 75  ? 26.485 121.422 53.435 1.00 29.24 ? 516  HIS   B O   1 
ATOM   3501 C  CB  . HIS   B 1 75  ? 23.989 121.196 52.081 1.00 31.37 ? 516  HIS   B CB  1 
ATOM   3502 C  CG  . HIS   B 1 75  ? 22.946 121.099 51.014 1.00 37.90 ? 516  HIS   B CG  1 
ATOM   3503 N  ND1 . HIS   B 1 75  ? 21.646 120.720 51.274 1.00 37.89 ? 516  HIS   B ND1 1 
ATOM   3504 C  CD2 . HIS   B 1 75  ? 23.020 121.303 49.677 1.00 35.63 ? 516  HIS   B CD2 1 
ATOM   3505 C  CE1 . HIS   B 1 75  ? 20.960 120.712 50.145 1.00 38.11 ? 516  HIS   B CE1 1 
ATOM   3506 N  NE2 . HIS   B 1 75  ? 21.772 121.059 49.161 1.00 37.03 ? 516  HIS   B NE2 1 
ATOM   3507 N  N   . MET   B 1 76  ? 26.612 119.188 53.596 1.00 24.20 ? 517  MET   B N   1 
ATOM   3508 C  CA  . MET   B 1 76  ? 27.529 119.215 54.720 1.00 21.80 ? 517  MET   B CA  1 
ATOM   3509 C  C   . MET   B 1 76  ? 28.971 119.343 54.252 1.00 24.46 ? 517  MET   B C   1 
ATOM   3510 O  O   . MET   B 1 76  ? 29.370 118.797 53.218 1.00 24.30 ? 517  MET   B O   1 
ATOM   3511 C  CB  . MET   B 1 76  ? 27.385 117.940 55.540 1.00 19.88 ? 517  MET   B CB  1 
ATOM   3512 C  CG  . MET   B 1 76  ? 26.186 117.947 56.455 1.00 18.68 ? 517  MET   B CG  1 
ATOM   3513 S  SD  . MET   B 1 76  ? 26.243 116.555 57.577 1.00 22.94 ? 517  MET   B SD  1 
ATOM   3514 C  CE  . MET   B 1 76  ? 24.747 116.870 58.513 1.00 23.37 ? 517  MET   B CE  1 
ATOM   3515 N  N   . LYS   B 1 77  ? 29.751 120.078 55.036 1.00 28.20 ? 518  LYS   B N   1 
ATOM   3516 C  CA  . LYS   B 1 77  ? 31.181 120.144 54.826 1.00 25.91 ? 518  LYS   B CA  1 
ATOM   3517 C  C   . LYS   B 1 77  ? 31.829 118.850 55.316 1.00 24.50 ? 518  LYS   B C   1 
ATOM   3518 O  O   . LYS   B 1 77  ? 31.230 118.102 56.092 1.00 24.16 ? 518  LYS   B O   1 
ATOM   3519 C  CB  . LYS   B 1 77  ? 31.752 121.340 55.586 1.00 29.93 ? 518  LYS   B CB  1 
ATOM   3520 C  CG  . LYS   B 1 77  ? 31.898 122.595 54.736 1.00 37.52 ? 518  LYS   B CG  1 
ATOM   3521 C  CD  . LYS   B 1 77  ? 32.080 123.838 55.601 1.00 41.52 ? 518  LYS   B CD  1 
ATOM   3522 C  CE  . LYS   B 1 77  ? 33.556 124.121 55.866 1.00 49.54 ? 518  LYS   B CE  1 
ATOM   3523 N  NZ  . LYS   B 1 77  ? 34.195 123.088 56.735 1.00 52.85 ? 518  LYS   B NZ  1 
ATOM   3524 N  N   . PRO   B 1 78  ? 33.055 118.558 54.863 1.00 25.18 ? 519  PRO   B N   1 
ATOM   3525 C  CA  . PRO   B 1 78  ? 33.705 117.292 55.252 1.00 24.42 ? 519  PRO   B CA  1 
ATOM   3526 C  C   . PRO   B 1 78  ? 33.710 116.992 56.744 1.00 26.46 ? 519  PRO   B C   1 
ATOM   3527 O  O   . PRO   B 1 78  ? 33.465 115.841 57.132 1.00 31.34 ? 519  PRO   B O   1 
ATOM   3528 C  CB  . PRO   B 1 78  ? 35.123 117.456 54.698 1.00 24.79 ? 519  PRO   B CB  1 
ATOM   3529 C  CG  . PRO   B 1 78  ? 34.944 118.330 53.515 1.00 26.21 ? 519  PRO   B CG  1 
ATOM   3530 C  CD  . PRO   B 1 78  ? 33.865 119.307 53.886 1.00 25.29 ? 519  PRO   B CD  1 
ATOM   3531 N  N   . ARG   B 1 79  ? 34.004 117.985 57.592 1.00 26.65 ? 520  ARG   B N   1 
ATOM   3532 C  CA  . ARG   B 1 79  ? 33.979 117.755 59.033 1.00 25.17 ? 520  ARG   B CA  1 
ATOM   3533 C  C   . ARG   B 1 79  ? 32.608 117.276 59.488 1.00 23.34 ? 520  ARG   B C   1 
ATOM   3534 O  O   . ARG   B 1 79  ? 32.502 116.372 60.326 1.00 30.66 ? 520  ARG   B O   1 
ATOM   3535 C  CB  . ARG   B 1 79  ? 34.352 119.043 59.766 1.00 26.67 ? 520  ARG   B CB  1 
ATOM   3536 C  CG  . ARG   B 1 79  ? 34.438 118.919 61.271 1.00 29.31 ? 520  ARG   B CG  1 
ATOM   3537 C  CD  . ARG   B 1 79  ? 35.011 120.200 61.881 1.00 30.05 ? 520  ARG   B CD  1 
ATOM   3538 N  NE  . ARG   B 1 79  ? 35.732 121.009 60.897 0.54 32.23 ? 520  ARG   B NE  1 
ATOM   3539 C  CZ  . ARG   B 1 79  ? 35.316 122.188 60.437 0.58 30.19 ? 520  ARG   B CZ  1 
ATOM   3540 N  NH1 . ARG   B 1 79  ? 34.173 122.712 60.865 1.00 33.39 ? 520  ARG   B NH1 1 
ATOM   3541 N  NH2 . ARG   B 1 79  ? 36.044 122.845 59.545 0.64 30.20 ? 520  ARG   B NH2 1 
ATOM   3542 N  N   . ASP   B 1 80  ? 31.544 117.872 58.946 1.00 23.27 ? 521  ASP   B N   1 
ATOM   3543 C  CA  . ASP   B 1 80  ? 30.198 117.467 59.333 1.00 23.98 ? 521  ASP   B CA  1 
ATOM   3544 C  C   . ASP   B 1 80  ? 29.875 116.072 58.821 1.00 23.45 ? 521  ASP   B C   1 
ATOM   3545 O  O   . ASP   B 1 80  ? 29.206 115.294 59.512 1.00 23.29 ? 521  ASP   B O   1 
ATOM   3546 C  CB  . ASP   B 1 80  ? 29.182 118.488 58.826 1.00 25.69 ? 521  ASP   B CB  1 
ATOM   3547 C  CG  . ASP   B 1 80  ? 29.370 119.855 59.456 1.00 30.92 ? 521  ASP   B CG  1 
ATOM   3548 O  OD1 . ASP   B 1 80  ? 29.707 119.918 60.658 1.00 30.84 ? 521  ASP   B OD1 1 
ATOM   3549 O  OD2 . ASP   B 1 80  ? 29.186 120.864 58.746 1.00 36.98 ? 521  ASP   B OD2 1 
ATOM   3550 N  N   . LEU   B 1 81  ? 30.353 115.737 57.616 1.00 24.42 ? 522  LEU   B N   1 
ATOM   3551 C  CA  . LEU   B 1 81  ? 30.118 114.409 57.057 1.00 21.30 ? 522  LEU   B CA  1 
ATOM   3552 C  C   . LEU   B 1 81  ? 30.808 113.332 57.880 1.00 21.92 ? 522  LEU   B C   1 
ATOM   3553 O  O   . LEU   B 1 81  ? 30.226 112.273 58.138 1.00 25.61 ? 522  LEU   B O   1 
ATOM   3554 C  CB  . LEU   B 1 81  ? 30.629 114.359 55.623 1.00 17.73 ? 522  LEU   B CB  1 
ATOM   3555 C  CG  . LEU   B 1 81  ? 29.808 115.109 54.586 1.00 20.10 ? 522  LEU   B CG  1 
ATOM   3556 C  CD1 . LEU   B 1 81  ? 30.568 115.171 53.276 1.00 19.10 ? 522  LEU   B CD1 1 
ATOM   3557 C  CD2 . LEU   B 1 81  ? 28.446 114.447 54.386 1.00 20.28 ? 522  LEU   B CD2 1 
ATOM   3558 N  N   . ASN   B 1 82  ? 32.058 113.571 58.283 1.00 22.31 ? 523  ASN   B N   1 
ATOM   3559 C  CA  . ASN   B 1 82  ? 32.766 112.593 59.103 1.00 24.41 ? 523  ASN   B CA  1 
ATOM   3560 C  C   . ASN   B 1 82  ? 32.082 112.420 60.449 1.00 22.29 ? 523  ASN   B C   1 
ATOM   3561 O  O   . ASN   B 1 82  ? 31.898 111.293 60.926 1.00 22.73 ? 523  ASN   B O   1 
ATOM   3562 C  CB  . ASN   B 1 82  ? 34.218 113.025 59.305 1.00 35.46 ? 523  ASN   B CB  1 
ATOM   3563 C  CG  . ASN   B 1 82  ? 35.138 111.851 59.600 1.00 44.23 ? 523  ASN   B CG  1 
ATOM   3564 O  OD1 . ASN   B 1 82  ? 34.724 110.689 59.544 1.00 46.70 ? 523  ASN   B OD1 1 
ATOM   3565 N  ND2 . ASN   B 1 82  ? 36.395 112.149 59.903 1.00 47.53 ? 523  ASN   B ND2 1 
ATOM   3566 N  N   . ARG   B 1 83  ? 31.696 113.534 61.078 1.00 21.12 ? 524  ARG   B N   1 
ATOM   3567 C  CA  . ARG   B 1 83  ? 31.046 113.456 62.380 1.00 22.65 ? 524  ARG   B CA  1 
ATOM   3568 C  C   . ARG   B 1 83  ? 29.711 112.729 62.290 1.00 24.42 ? 524  ARG   B C   1 
ATOM   3569 O  O   . ARG   B 1 83  ? 29.402 111.884 63.138 1.00 25.80 ? 524  ARG   B O   1 
ATOM   3570 C  CB  . ARG   B 1 83  ? 30.857 114.858 62.959 1.00 23.53 ? 524  ARG   B CB  1 
ATOM   3571 C  CG  . ARG   B 1 83  ? 31.954 115.273 63.929 1.00 26.84 ? 524  ARG   B CG  1 
ATOM   3572 C  CD  . ARG   B 1 83  ? 32.153 116.781 63.952 1.00 28.69 ? 524  ARG   B CD  1 
ATOM   3573 N  NE  . ARG   B 1 83  ? 30.896 117.512 64.112 1.00 34.91 ? 524  ARG   B NE  1 
ATOM   3574 C  CZ  . ARG   B 1 83  ? 30.818 118.771 64.535 1.00 34.21 ? 524  ARG   B CZ  1 
ATOM   3575 N  NH1 . ARG   B 1 83  ? 31.925 119.432 64.855 1.00 35.80 ? 524  ARG   B NH1 1 
ATOM   3576 N  NH2 . ARG   B 1 83  ? 29.639 119.363 64.647 1.00 37.99 ? 524  ARG   B NH2 1 
ATOM   3577 N  N   . LEU   B 1 84  ? 28.908 113.044 61.272 1.00 22.35 ? 525  LEU   B N   1 
ATOM   3578 C  CA  . LEU   B 1 84  ? 27.615 112.384 61.129 1.00 19.50 ? 525  LEU   B CA  1 
ATOM   3579 C  C   . LEU   B 1 84  ? 27.797 110.898 60.856 1.00 22.37 ? 525  LEU   B C   1 
ATOM   3580 O  O   . LEU   B 1 84  ? 27.134 110.055 61.472 1.00 22.05 ? 525  LEU   B O   1 
ATOM   3581 C  CB  . LEU   B 1 84  ? 26.810 113.034 60.004 1.00 18.73 ? 525  LEU   B CB  1 
ATOM   3582 C  CG  . LEU   B 1 84  ? 25.480 112.355 59.666 1.00 19.10 ? 525  LEU   B CG  1 
ATOM   3583 C  CD1 . LEU   B 1 84  ? 24.570 112.381 60.882 1.00 19.27 ? 525  LEU   B CD1 1 
ATOM   3584 C  CD2 . LEU   B 1 84  ? 24.797 113.017 58.484 1.00 19.80 ? 525  LEU   B CD2 1 
ATOM   3585 N  N   . GLY   B 1 85  ? 28.711 110.560 59.945 1.00 21.72 ? 526  GLY   B N   1 
ATOM   3586 C  CA  . GLY   B 1 85  ? 28.946 109.160 59.638 1.00 20.37 ? 526  GLY   B CA  1 
ATOM   3587 C  C   . GLY   B 1 85  ? 29.360 108.363 60.858 1.00 21.70 ? 526  GLY   B C   1 
ATOM   3588 O  O   . GLY   B 1 85  ? 28.906 107.232 61.058 1.00 22.03 ? 526  GLY   B O   1 
ATOM   3589 N  N   . ASP   B 1 86  ? 30.210 108.951 61.707 1.00 22.45 ? 527  ASP   B N   1 
ATOM   3590 C  CA  . ASP   B 1 86  ? 30.668 108.251 62.899 1.00 24.21 ? 527  ASP   B CA  1 
ATOM   3591 C  C   . ASP   B 1 86  ? 29.574 108.053 63.939 1.00 23.08 ? 527  ASP   B C   1 
ATOM   3592 O  O   . ASP   B 1 86  ? 29.764 107.249 64.859 1.00 26.91 ? 527  ASP   B O   1 
ATOM   3593 C  CB  . ASP   B 1 86  ? 31.883 108.961 63.497 1.00 29.66 ? 527  ASP   B CB  1 
ATOM   3594 C  CG  . ASP   B 1 86  ? 33.113 108.856 62.606 1.00 35.59 ? 527  ASP   B CG  1 
ATOM   3595 O  OD1 . ASP   B 1 86  ? 33.081 108.085 61.618 1.00 37.11 ? 527  ASP   B OD1 1 
ATOM   3596 O  OD2 . ASP   B 1 86  ? 34.115 109.544 62.889 1.00 41.05 ? 527  ASP   B OD2 1 
ATOM   3597 N  N   . GLU   B 1 87  ? 28.435 108.743 63.815 1.00 22.76 ? 528  GLU   B N   1 
ATOM   3598 C  CA  . GLU   B 1 87  ? 27.315 108.508 64.720 1.00 22.12 ? 528  GLU   B CA  1 
ATOM   3599 C  C   . GLU   B 1 87  ? 26.627 107.175 64.464 1.00 21.07 ? 528  GLU   B C   1 
ATOM   3600 O  O   . GLU   B 1 87  ? 25.930 106.671 65.348 1.00 24.11 ? 528  GLU   B O   1 
ATOM   3601 C  CB  . GLU   B 1 87  ? 26.288 109.636 64.609 1.00 25.82 ? 528  GLU   B CB  1 
ATOM   3602 C  CG  . GLU   B 1 87  ? 26.550 110.782 65.565 1.00 32.39 ? 528  GLU   B CG  1 
ATOM   3603 C  CD  . GLU   B 1 87  ? 26.157 112.123 64.992 1.00 38.51 ? 528  GLU   B CD  1 
ATOM   3604 O  OE1 . GLU   B 1 87  ? 25.219 112.175 64.163 1.00 42.07 ? 528  GLU   B OE1 1 
ATOM   3605 O  OE2 . GLU   B 1 87  ? 26.789 113.135 65.369 1.00 45.67 ? 528  GLU   B OE2 1 
ATOM   3606 N  N   . TYR   B 1 88  ? 26.783 106.609 63.274 1.00 21.54 ? 529  TYR   B N   1 
ATOM   3607 C  CA  . TYR   B 1 88  ? 26.170 105.336 62.936 1.00 18.95 ? 529  TYR   B CA  1 
ATOM   3608 C  C   . TYR   B 1 88  ? 27.184 104.209 63.073 1.00 20.02 ? 529  TYR   B C   1 
ATOM   3609 O  O   . TYR   B 1 88  ? 28.395 104.423 63.149 1.00 22.10 ? 529  TYR   B O   1 
ATOM   3610 C  CB  . TYR   B 1 88  ? 25.628 105.356 61.502 1.00 18.27 ? 529  TYR   B CB  1 
ATOM   3611 C  CG  . TYR   B 1 88  ? 24.666 106.476 61.197 1.00 17.25 ? 529  TYR   B CG  1 
ATOM   3612 C  CD1 . TYR   B 1 88  ? 23.341 106.410 61.603 1.00 16.48 ? 529  TYR   B CD1 1 
ATOM   3613 C  CD2 . TYR   B 1 88  ? 25.076 107.583 60.473 1.00 16.43 ? 529  TYR   B CD2 1 
ATOM   3614 C  CE1 . TYR   B 1 88  ? 22.448 107.439 61.318 1.00 15.79 ? 529  TYR   B CE1 1 
ATOM   3615 C  CE2 . TYR   B 1 88  ? 24.200 108.606 60.176 1.00 18.27 ? 529  TYR   B CE2 1 
ATOM   3616 C  CZ  . TYR   B 1 88  ? 22.895 108.534 60.597 1.00 16.94 ? 529  TYR   B CZ  1 
ATOM   3617 O  OH  . TYR   B 1 88  ? 22.041 109.567 60.286 1.00 20.33 ? 529  TYR   B OH  1 
ATOM   3618 N  N   . ASN   B 1 89  ? 26.662 102.988 63.107 1.00 17.63 ? 530  ASN   B N   1 
ATOM   3619 C  CA  . ASN   B 1 89  ? 27.482 101.785 63.019 1.00 16.70 ? 530  ASN   B CA  1 
ATOM   3620 C  C   . ASN   B 1 89  ? 27.855 101.567 61.554 1.00 17.53 ? 530  ASN   B C   1 
ATOM   3621 O  O   . ASN   B 1 89  ? 26.990 101.275 60.723 1.00 16.56 ? 530  ASN   B O   1 
ATOM   3622 C  CB  . ASN   B 1 89  ? 26.690 100.608 63.585 1.00 19.36 ? 530  ASN   B CB  1 
ATOM   3623 C  CG  . ASN   B 1 89  ? 27.493 99.325  63.653 1.00 23.56 ? 530  ASN   B CG  1 
ATOM   3624 O  OD1 . ASN   B 1 89  ? 28.504 99.168  62.975 1.00 21.66 ? 530  ASN   B OD1 1 
ATOM   3625 N  ND2 . ASN   B 1 89  ? 27.032 98.390  64.478 1.00 26.63 ? 530  ASN   B ND2 1 
ATOM   3626 N  N   . SER   B 1 90  ? 29.138 101.758 61.232 1.00 16.36 ? 531  SER   B N   1 
ATOM   3627 C  CA  . SER   B 1 90  ? 29.728 101.364 59.949 1.00 16.94 ? 531  SER   B CA  1 
ATOM   3628 C  C   . SER   B 1 90  ? 29.117 102.119 58.760 1.00 17.15 ? 531  SER   B C   1 
ATOM   3629 O  O   . SER   B 1 90  ? 28.568 101.530 57.826 1.00 15.66 ? 531  SER   B O   1 
ATOM   3630 C  CB  . SER   B 1 90  ? 29.652 99.845  59.763 1.00 19.01 ? 531  SER   B CB  1 
ATOM   3631 O  OG  . SER   B 1 90  ? 30.428 99.181  60.754 1.00 22.93 ? 531  SER   B OG  1 
ATOM   3632 N  N   . ILE   B 1 91  ? 29.250 103.443 58.786 1.00 16.63 ? 532  ILE   B N   1 
ATOM   3633 C  CA  . ILE   B 1 91  ? 28.749 104.295 57.712 1.00 14.67 ? 532  ILE   B CA  1 
ATOM   3634 C  C   . ILE   B 1 91  ? 29.818 105.323 57.363 1.00 15.15 ? 532  ILE   B C   1 
ATOM   3635 O  O   . ILE   B 1 91  ? 30.399 105.948 58.260 1.00 16.37 ? 532  ILE   B O   1 
ATOM   3636 C  CB  . ILE   B 1 91  ? 27.458 105.027 58.130 1.00 13.67 ? 532  ILE   B CB  1 
ATOM   3637 C  CG1 . ILE   B 1 91  ? 26.275 104.053 58.197 1.00 14.26 ? 532  ILE   B CG1 1 
ATOM   3638 C  CG2 . ILE   B 1 91  ? 27.156 106.179 57.168 1.00 14.99 ? 532  ILE   B CG2 1 
ATOM   3639 C  CD1 . ILE   B 1 91  ? 25.731 103.670 56.817 1.00 14.35 ? 532  ILE   B CD1 1 
ATOM   3640 N  N   . PHE   B 1 92  ? 30.060 105.513 56.065 1.00 15.28 ? 533  PHE   B N   1 
ATOM   3641 C  CA  . PHE   B 1 92  ? 30.768 106.676 55.557 1.00 15.82 ? 533  PHE   B CA  1 
ATOM   3642 C  C   . PHE   B 1 92  ? 29.822 107.444 54.642 1.00 18.59 ? 533  PHE   B C   1 
ATOM   3643 O  O   . PHE   B 1 92  ? 28.953 106.850 53.991 1.00 16.20 ? 533  PHE   B O   1 
ATOM   3644 C  CB  . PHE   B 1 92  ? 32.074 106.302 54.799 1.00 14.14 ? 533  PHE   B CB  1 
ATOM   3645 C  CG  . PHE   B 1 92  ? 31.848 105.487 53.555 1.00 14.30 ? 533  PHE   B CG  1 
ATOM   3646 C  CD1 . PHE   B 1 92  ? 31.585 106.106 52.340 1.00 15.30 ? 533  PHE   B CD1 1 
ATOM   3647 C  CD2 . PHE   B 1 92  ? 31.920 104.098 53.599 1.00 15.66 ? 533  PHE   B CD2 1 
ATOM   3648 C  CE1 . PHE   B 1 92  ? 31.367 105.352 51.189 1.00 15.04 ? 533  PHE   B CE1 1 
ATOM   3649 C  CE2 . PHE   B 1 92  ? 31.711 103.339 52.463 1.00 16.58 ? 533  PHE   B CE2 1 
ATOM   3650 C  CZ  . PHE   B 1 92  ? 31.426 103.961 51.250 1.00 16.62 ? 533  PHE   B CZ  1 
ATOM   3651 N  N   . ILE   B 1 93  ? 29.971 108.771 54.613 1.00 16.60 ? 534  ILE   B N   1 
ATOM   3652 C  CA  . ILE   B 1 93  ? 29.075 109.648 53.864 1.00 16.04 ? 534  ILE   B CA  1 
ATOM   3653 C  C   . ILE   B 1 93  ? 29.894 110.648 53.058 1.00 15.86 ? 534  ILE   B C   1 
ATOM   3654 O  O   . ILE   B 1 93  ? 30.882 111.204 53.553 1.00 17.52 ? 534  ILE   B O   1 
ATOM   3655 C  CB  . ILE   B 1 93  ? 28.097 110.402 54.790 1.00 15.45 ? 534  ILE   B CB  1 
ATOM   3656 C  CG1 . ILE   B 1 93  ? 27.560 109.488 55.884 1.00 15.54 ? 534  ILE   B CG1 1 
ATOM   3657 C  CG2 . ILE   B 1 93  ? 26.933 110.960 53.982 1.00 15.57 ? 534  ILE   B CG2 1 
ATOM   3658 C  CD1 . ILE   B 1 93  ? 26.640 110.189 56.875 1.00 17.23 ? 534  ILE   B CD1 1 
ATOM   3659 N  N   . SER   B 1 94  ? 29.472 110.888 51.822 1.00 15.68 ? 535  SER   B N   1 
ATOM   3660 C  CA  . SER   B 1 94  ? 29.966 111.988 51.007 1.00 17.56 ? 535  SER   B CA  1 
ATOM   3661 C  C   . SER   B 1 94  ? 28.783 112.847 50.578 1.00 19.60 ? 535  SER   B C   1 
ATOM   3662 O  O   . SER   B 1 94  ? 27.626 112.523 50.853 1.00 18.69 ? 535  SER   B O   1 
ATOM   3663 C  CB  . SER   B 1 94  ? 30.781 111.483 49.804 1.00 17.65 ? 535  SER   B CB  1 
ATOM   3664 O  OG  . SER   B 1 94  ? 29.958 110.867 48.819 1.00 17.82 ? 535  SER   B OG  1 
ATOM   3665 N  N   . ASN   B 1 95  ? 29.074 113.964 49.906 1.00 18.72 ? 536  ASN   B N   1 
ATOM   3666 C  CA  . ASN   B 1 95  ? 28.002 114.863 49.486 1.00 20.19 ? 536  ASN   B CA  1 
ATOM   3667 C  C   . ASN   B 1 95  ? 27.059 114.211 48.482 1.00 17.66 ? 536  ASN   B C   1 
ATOM   3668 O  O   . ASN   B 1 95  ? 25.922 114.671 48.330 1.00 20.20 ? 536  ASN   B O   1 
ATOM   3669 C  CB  . ASN   B 1 95  ? 28.579 116.159 48.905 1.00 23.53 ? 536  ASN   B CB  1 
ATOM   3670 C  CG  . ASN   B 1 95  ? 29.140 117.074 49.974 1.00 26.49 ? 536  ASN   B CG  1 
ATOM   3671 O  OD1 . ASN   B 1 95  ? 30.223 117.641 49.814 1.00 32.31 ? 536  ASN   B OD1 1 
ATOM   3672 N  ND2 . ASN   B 1 95  ? 28.413 117.214 51.080 1.00 29.29 ? 536  ASN   B ND2 1 
ATOM   3673 N  N   . GLU   B 1 96  ? 27.500 113.147 47.814 1.00 17.67 ? 537  GLU   B N   1 
ATOM   3674 C  CA  . GLU   B 1 96  ? 26.706 112.436 46.823 1.00 18.34 ? 537  GLU   B CA  1 
ATOM   3675 C  C   . GLU   B 1 96  ? 25.956 111.233 47.395 1.00 18.60 ? 537  GLU   B C   1 
ATOM   3676 O  O   . GLU   B 1 96  ? 25.170 110.611 46.667 1.00 19.29 ? 537  GLU   B O   1 
ATOM   3677 C  CB  . GLU   B 1 96  ? 27.620 111.957 45.689 1.00 18.77 ? 537  GLU   B CB  1 
ATOM   3678 C  CG  . GLU   B 1 96  ? 28.482 113.046 45.039 1.00 25.89 ? 537  GLU   B CG  1 
ATOM   3679 C  CD  . GLU   B 1 96  ? 29.849 113.245 45.701 1.00 31.70 ? 537  GLU   B CD  1 
ATOM   3680 O  OE1 . GLU   B 1 96  ? 30.125 112.650 46.768 1.00 28.29 ? 537  GLU   B OE1 1 
ATOM   3681 O  OE2 . GLU   B 1 96  ? 30.667 114.002 45.132 1.00 38.27 ? 537  GLU   B OE2 1 
ATOM   3682 N  N   . SER   B 1 97  ? 26.178 110.887 48.666 1.00 16.54 ? 538  SER   B N   1 
ATOM   3683 C  CA  . SER   B 1 97  ? 25.608 109.660 49.220 1.00 15.71 ? 538  SER   B CA  1 
ATOM   3684 C  C   . SER   B 1 97  ? 24.086 109.663 49.159 1.00 16.55 ? 538  SER   B C   1 
ATOM   3685 O  O   . SER   B 1 97  ? 23.468 108.659 48.786 1.00 16.86 ? 538  SER   B O   1 
ATOM   3686 C  CB  . SER   B 1 97  ? 26.066 109.469 50.661 1.00 16.21 ? 538  SER   B CB  1 
ATOM   3687 O  OG  . SER   B 1 97  ? 27.471 109.334 50.729 1.00 17.18 ? 538  SER   B OG  1 
ATOM   3688 N  N   . TYR   B 1 98  ? 23.459 110.767 49.572 1.00 17.22 ? 539  TYR   B N   1 
ATOM   3689 C  CA  . TYR   B 1 98  ? 21.999 110.823 49.577 1.00 17.93 ? 539  TYR   B CA  1 
ATOM   3690 C  C   . TYR   B 1 98  ? 21.432 110.585 48.184 1.00 18.79 ? 539  TYR   B C   1 
ATOM   3691 O  O   . TYR   B 1 98  ? 20.534 109.754 48.000 1.00 17.42 ? 539  TYR   B O   1 
ATOM   3692 C  CB  . TYR   B 1 98  ? 21.540 112.168 50.142 1.00 16.14 ? 539  TYR   B CB  1 
ATOM   3693 C  CG  . TYR   B 1 98  ? 20.045 112.411 50.114 1.00 17.45 ? 539  TYR   B CG  1 
ATOM   3694 C  CD1 . TYR   B 1 98  ? 19.177 111.627 50.866 1.00 17.89 ? 539  TYR   B CD1 1 
ATOM   3695 C  CD2 . TYR   B 1 98  ? 19.510 113.457 49.367 1.00 17.35 ? 539  TYR   B CD2 1 
ATOM   3696 C  CE1 . TYR   B 1 98  ? 17.805 111.866 50.849 1.00 17.64 ? 539  TYR   B CE1 1 
ATOM   3697 C  CE2 . TYR   B 1 98  ? 18.146 113.703 49.345 1.00 16.85 ? 539  TYR   B CE2 1 
ATOM   3698 C  CZ  . TYR   B 1 98  ? 17.300 112.909 50.091 1.00 17.69 ? 539  TYR   B CZ  1 
ATOM   3699 O  OH  . TYR   B 1 98  ? 15.939 113.160 50.064 1.00 21.35 ? 539  TYR   B OH  1 
ATOM   3700 N  N   . THR   B 1 99  ? 21.949 111.307 47.185 1.00 17.78 ? 540  THR   B N   1 
ATOM   3701 C  CA  . THR   B 1 99  ? 21.498 111.106 45.809 1.00 19.46 ? 540  THR   B CA  1 
ATOM   3702 C  C   . THR   B 1 99  ? 21.670 109.657 45.370 1.00 16.98 ? 540  THR   B C   1 
ATOM   3703 O  O   . THR   B 1 99  ? 20.804 109.097 44.685 1.00 15.75 ? 540  THR   B O   1 
ATOM   3704 C  CB  . THR   B 1 99  ? 22.281 112.026 44.872 1.00 20.24 ? 540  THR   B CB  1 
ATOM   3705 O  OG1 . THR   B 1 99  ? 22.078 113.387 45.262 1.00 23.98 ? 540  THR   B OG1 1 
ATOM   3706 C  CG2 . THR   B 1 99  ? 21.839 111.828 43.430 1.00 18.24 ? 540  THR   B CG2 1 
ATOM   3707 N  N   . CYS   B 1 100 ? 22.798 109.040 45.732 1.00 17.13 ? 541  CYS   B N   1 
ATOM   3708 C  CA  . CYS   B 1 100 ? 23.066 107.682 45.278 1.00 16.20 ? 541  CYS   B CA  1 
ATOM   3709 C  C   . CYS   B 1 100 ? 22.105 106.696 45.924 1.00 14.74 ? 541  CYS   B C   1 
ATOM   3710 O  O   . CYS   B 1 100 ? 21.606 105.783 45.255 1.00 14.69 ? 541  CYS   B O   1 
ATOM   3711 C  CB  . CYS   B 1 100 ? 24.512 107.319 45.602 1.00 16.56 ? 541  CYS   B CB  1 
ATOM   3712 S  SG  . CYS   B 1 100 ? 25.679 108.133 44.484 1.00 22.86 ? 541  CYS   B SG  1 
ATOM   3713 N  N   . ALA   B 1 101 ? 21.812 106.884 47.215 1.00 14.65 ? 542  ALA   B N   1 
ATOM   3714 C  CA  . ALA   B 1 101 ? 20.809 106.062 47.885 1.00 13.65 ? 542  ALA   B CA  1 
ATOM   3715 C  C   . ALA   B 1 101 ? 19.436 106.230 47.237 1.00 14.34 ? 542  ALA   B C   1 
ATOM   3716 O  O   . ALA   B 1 101 ? 18.702 105.248 47.062 1.00 14.88 ? 542  ALA   B O   1 
ATOM   3717 C  CB  . ALA   B 1 101 ? 20.750 106.416 49.372 1.00 13.79 ? 542  ALA   B CB  1 
ATOM   3718 N  N   . LEU   B 1 102 ? 19.083 107.467 46.855 1.00 14.60 ? 543  LEU   B N   1 
ATOM   3719 C  CA  . LEU   B 1 102 ? 17.817 107.704 46.164 1.00 14.72 ? 543  LEU   B CA  1 
ATOM   3720 C  C   . LEU   B 1 102 ? 17.786 106.994 44.818 1.00 14.84 ? 543  LEU   B C   1 
ATOM   3721 O  O   . LEU   B 1 102 ? 16.742 106.473 44.405 1.00 15.12 ? 543  LEU   B O   1 
ATOM   3722 C  CB  . LEU   B 1 102 ? 17.621 109.207 45.940 1.00 16.35 ? 543  LEU   B CB  1 
ATOM   3723 C  CG  . LEU   B 1 102 ? 17.333 110.131 47.120 1.00 18.60 ? 543  LEU   B CG  1 
ATOM   3724 C  CD1 . LEU   B 1 102 ? 17.047 111.535 46.598 1.00 18.79 ? 543  LEU   B CD1 1 
ATOM   3725 C  CD2 . LEU   B 1 102 ? 16.166 109.640 47.959 1.00 17.58 ? 543  LEU   B CD2 1 
ATOM   3726 N  N   . LEU   B 1 103 ? 18.913 106.995 44.105 1.00 14.45 ? 544  LEU   B N   1 
ATOM   3727 C  CA  . LEU   B 1 103 ? 18.978 106.349 42.798 1.00 14.86 ? 544  LEU   B CA  1 
ATOM   3728 C  C   . LEU   B 1 103 ? 18.897 104.835 42.921 1.00 13.12 ? 544  LEU   B C   1 
ATOM   3729 O  O   . LEU   B 1 103 ? 18.304 104.168 42.064 1.00 14.11 ? 544  LEU   B O   1 
ATOM   3730 C  CB  . LEU   B 1 103 ? 20.272 106.743 42.090 1.00 19.64 ? 544  LEU   B CB  1 
ATOM   3731 C  CG  . LEU   B 1 103 ? 20.371 108.142 41.494 1.00 27.10 ? 544  LEU   B CG  1 
ATOM   3732 C  CD1 . LEU   B 1 103 ? 21.754 108.345 40.895 1.00 27.54 ? 544  LEU   B CD1 1 
ATOM   3733 C  CD2 . LEU   B 1 103 ? 19.301 108.332 40.422 1.00 30.66 ? 544  LEU   B CD2 1 
ATOM   3734 N  N   . ALA   B 1 104 ? 19.530 104.265 43.946 1.00 15.60 ? 545  ALA   B N   1 
ATOM   3735 C  CA  . ALA   B 1 104 ? 19.427 102.827 44.145 1.00 15.19 ? 545  ALA   B CA  1 
ATOM   3736 C  C   . ALA   B 1 104 ? 17.975 102.423 44.346 1.00 13.80 ? 545  ALA   B C   1 
ATOM   3737 O  O   . ALA   B 1 104 ? 17.494 101.461 43.736 1.00 15.77 ? 545  ALA   B O   1 
ATOM   3738 C  CB  . ALA   B 1 104 ? 20.282 102.401 45.335 1.00 13.95 ? 545  ALA   B CB  1 
ATOM   3739 N  N   . ALA   B 1 105 ? 17.248 103.173 45.180 1.00 13.74 ? 546  ALA   B N   1 
ATOM   3740 C  CA  . ALA   B 1 105 ? 15.848 102.851 45.442 1.00 13.66 ? 546  ALA   B CA  1 
ATOM   3741 C  C   . ALA   B 1 105 ? 14.991 103.072 44.202 1.00 15.16 ? 546  ALA   B C   1 
ATOM   3742 O  O   . ALA   B 1 105 ? 14.178 102.215 43.838 1.00 14.88 ? 546  ALA   B O   1 
ATOM   3743 C  CB  . ALA   B 1 105 ? 15.333 103.687 46.613 1.00 14.09 ? 546  ALA   B CB  1 
ATOM   3744 N  N   . GLY   B 1 106 ? 15.160 104.220 43.541 1.00 14.17 ? 547  GLY   B N   1 
ATOM   3745 C  CA  . GLY   B 1 106 ? 14.321 104.527 42.391 1.00 14.62 ? 547  GLY   B CA  1 
ATOM   3746 C  C   . GLY   B 1 106 ? 14.532 103.573 41.233 1.00 15.60 ? 547  GLY   B C   1 
ATOM   3747 O  O   . GLY   B 1 106 ? 13.594 103.270 40.489 1.00 15.43 ? 547  GLY   B O   1 
ATOM   3748 N  N   . SER   B 1 107 ? 15.772 103.110 41.050 1.00 15.97 ? 548  SER   B N   1 
ATOM   3749 C  CA  . SER   B 1 107 ? 16.062 102.088 40.048 1.00 16.57 ? 548  SER   B CA  1 
ATOM   3750 C  C   . SER   B 1 107 ? 15.273 100.824 40.325 1.00 15.31 ? 548  SER   B C   1 
ATOM   3751 O  O   . SER   B 1 107 ? 14.743 100.195 39.400 1.00 15.65 ? 548  SER   B O   1 
ATOM   3752 C  CB  . SER   B 1 107 ? 17.550 101.732 40.057 1.00 17.02 ? 548  SER   B CB  1 
ATOM   3753 O  OG  . SER   B 1 107 ? 18.369 102.835 39.738 1.00 17.90 ? 548  SER   B OG  1 
ATOM   3754 N  N   . CYS   B 1 108 ? 15.204 100.423 41.597 1.00 13.12 ? 549  CYS   B N   1 
ATOM   3755 C  CA  . CYS   B 1 108 ? 14.455 99.227  41.953 1.00 11.68 ? 549  CYS   B CA  1 
ATOM   3756 C  C   . CYS   B 1 108 ? 12.953 99.435  41.817 1.00 13.40 ? 549  CYS   B C   1 
ATOM   3757 O  O   . CYS   B 1 108 ? 12.243 98.502  41.430 1.00 13.21 ? 549  CYS   B O   1 
ATOM   3758 C  CB  . CYS   B 1 108 ? 14.843 98.741  43.352 1.00 11.36 ? 549  CYS   B CB  1 
ATOM   3759 S  SG  . CYS   B 1 108 ? 16.542 98.120  43.412 1.00 21.31 ? 549  CYS   B SG  1 
ATOM   3760 N  N   . PHE   B 1 109 ? 12.453 100.642 42.107 1.00 14.59 ? 550  PHE   B N   1 
ATOM   3761 C  CA  . PHE   B 1 109 ? 11.037 100.918 41.872 1.00 13.32 ? 550  PHE   B CA  1 
ATOM   3762 C  C   . PHE   B 1 109 ? 10.704 100.775 40.395 1.00 14.02 ? 550  PHE   B C   1 
ATOM   3763 O  O   . PHE   B 1 109 ? 9.700  100.153 40.036 1.00 15.39 ? 550  PHE   B O   1 
ATOM   3764 C  CB  . PHE   B 1 109 ? 10.662 102.329 42.325 1.00 14.50 ? 550  PHE   B CB  1 
ATOM   3765 C  CG  . PHE   B 1 109 ? 10.927 102.617 43.780 1.00 13.09 ? 550  PHE   B CG  1 
ATOM   3766 C  CD1 . PHE   B 1 109 ? 11.162 101.605 44.702 1.00 12.38 ? 550  PHE   B CD1 1 
ATOM   3767 C  CD2 . PHE   B 1 109 ? 10.918 103.932 44.228 1.00 14.49 ? 550  PHE   B CD2 1 
ATOM   3768 C  CE1 . PHE   B 1 109 ? 11.417 101.904 46.038 1.00 12.57 ? 550  PHE   B CE1 1 
ATOM   3769 C  CE2 . PHE   B 1 109 ? 11.162 104.237 45.555 1.00 16.09 ? 550  PHE   B CE2 1 
ATOM   3770 C  CZ  . PHE   B 1 109 ? 11.405 103.229 46.464 1.00 13.47 ? 550  PHE   B CZ  1 
ATOM   3771 N  N   . ASN   B 1 110 ? 11.523 101.369 39.523 1.00 13.94 ? 551  ASN   B N   1 
ATOM   3772 C  CA  . ASN   B 1 110 ? 11.256 101.255 38.091 1.00 14.88 ? 551  ASN   B CA  1 
ATOM   3773 C  C   . ASN   B 1 110 ? 11.302 99.802  37.643 1.00 15.57 ? 551  ASN   B C   1 
ATOM   3774 O  O   . ASN   B 1 110 ? 10.513 99.378  36.787 1.00 15.63 ? 551  ASN   B O   1 
ATOM   3775 C  CB  . ASN   B 1 110 ? 12.250 102.087 37.280 1.00 16.67 ? 551  ASN   B CB  1 
ATOM   3776 C  CG  . ASN   B 1 110 ? 11.880 103.553 37.231 1.00 17.17 ? 551  ASN   B CG  1 
ATOM   3777 O  OD1 . ASN   B 1 110 ? 10.777 103.943 37.628 1.00 17.74 ? 551  ASN   B OD1 1 
ATOM   3778 N  ND2 . ASN   B 1 110 ? 12.798 104.377 36.733 1.00 17.57 ? 551  ASN   B ND2 1 
ATOM   3779 N  N   . SER   B 1 111 ? 12.209 99.017  38.227 1.00 14.85 ? 552  SER   B N   1 
ATOM   3780 C  CA  . SER   B 1 111 ? 12.323 97.612  37.854 1.00 14.19 ? 552  SER   B CA  1 
ATOM   3781 C  C   . SER   B 1 111 ? 11.112 96.825  38.326 1.00 14.41 ? 552  SER   B C   1 
ATOM   3782 O  O   . SER   B 1 111 ? 10.577 95.997  37.581 1.00 14.25 ? 552  SER   B O   1 
ATOM   3783 C  CB  . SER   B 1 111 ? 13.594 97.011  38.454 1.00 15.44 ? 552  SER   B CB  1 
ATOM   3784 O  OG  . SER   B 1 111 ? 14.744 97.648  37.942 1.00 15.07 ? 552  SER   B OG  1 
ATOM   3785 N  N   . ALA   B 1 112 ? 10.671 97.063  39.569 1.00 13.84 ? 553  ALA   B N   1 
ATOM   3786 C  CA  . ALA   B 1 112 ? 9.480  96.386  40.069 1.00 14.15 ? 553  ALA   B CA  1 
ATOM   3787 C  C   . ALA   B 1 112 ? 8.261  96.747  39.232 1.00 15.31 ? 553  ALA   B C   1 
ATOM   3788 O  O   . ALA   B 1 112 ? 7.416  95.887  38.944 1.00 15.34 ? 553  ALA   B O   1 
ATOM   3789 C  CB  . ALA   B 1 112 ? 9.240  96.743  41.539 1.00 14.82 ? 553  ALA   B CB  1 
ATOM   3790 N  N   . GLN   B 1 113 ? 8.152  98.017  38.843 1.00 14.33 ? 554  GLN   B N   1 
ATOM   3791 C  CA  . GLN   B 1 113 ? 7.039  98.454  38.006 1.00 15.78 ? 554  GLN   B CA  1 
ATOM   3792 C  C   . GLN   B 1 113 ? 7.062  97.758  36.654 1.00 15.34 ? 554  GLN   B C   1 
ATOM   3793 O  O   . GLN   B 1 113 ? 6.011  97.348  36.143 1.00 15.40 ? 554  GLN   B O   1 
ATOM   3794 C  CB  . GLN   B 1 113 ? 7.100  99.971  37.841 1.00 17.26 ? 554  GLN   B CB  1 
ATOM   3795 C  CG  . GLN   B 1 113 ? 5.990  100.569 36.983 1.00 18.90 ? 554  GLN   B CG  1 
ATOM   3796 C  CD  . GLN   B 1 113 ? 6.139  102.074 36.851 1.00 24.75 ? 554  GLN   B CD  1 
ATOM   3797 O  OE1 . GLN   B 1 113 ? 7.206  102.575 36.505 1.00 28.43 ? 554  GLN   B OE1 1 
ATOM   3798 N  NE2 . GLN   B 1 113 ? 5.064  102.798 37.120 1.00 26.83 ? 554  GLN   B NE2 1 
ATOM   3799 N  N   . ALA   B 1 114 ? 8.251  97.601  36.061 1.00 14.96 ? 555  ALA   B N   1 
ATOM   3800 C  CA  . ALA   B 1 114 ? 8.366  96.903  34.783 1.00 15.50 ? 555  ALA   B CA  1 
ATOM   3801 C  C   . ALA   B 1 114 ? 7.947  95.439  34.907 1.00 17.43 ? 555  ALA   B C   1 
ATOM   3802 O  O   . ALA   B 1 114 ? 7.311  94.886  33.999 1.00 17.25 ? 555  ALA   B O   1 
ATOM   3803 C  CB  . ALA   B 1 114 ? 9.794  97.027  34.242 1.00 15.23 ? 555  ALA   B CB  1 
ATOM   3804 N  N   . ILE   B 1 115 ? 8.270  94.801  36.033 1.00 14.84 ? 556  ILE   B N   1 
ATOM   3805 C  CA  . ILE   B 1 115 ? 7.853  93.421  36.264 1.00 13.53 ? 556  ILE   B CA  1 
ATOM   3806 C  C   . ILE   B 1 115 ? 6.347  93.343  36.476 1.00 15.81 ? 556  ILE   B C   1 
ATOM   3807 O  O   . ILE   B 1 115 ? 5.665  92.482  35.907 1.00 17.31 ? 556  ILE   B O   1 
ATOM   3808 C  CB  . ILE   B 1 115 ? 8.608  92.838  37.468 1.00 13.28 ? 556  ILE   B CB  1 
ATOM   3809 C  CG1 . ILE   B 1 115 ? 10.079 92.629  37.113 1.00 13.89 ? 556  ILE   B CG1 1 
ATOM   3810 C  CG2 . ILE   B 1 115 ? 7.999  91.515  37.896 1.00 15.37 ? 556  ILE   B CG2 1 
ATOM   3811 C  CD1 . ILE   B 1 115 ? 10.943 92.320  38.359 1.00 14.45 ? 556  ILE   B CD1 1 
ATOM   3812 N  N   . LEU   B 1 116 ? 5.808  94.227  37.312 1.00 15.53 ? 557  LEU   B N   1 
ATOM   3813 C  CA  . LEU   B 1 116 ? 4.404  94.121  37.700 1.00 16.96 ? 557  LEU   B CA  1 
ATOM   3814 C  C   . LEU   B 1 116 ? 3.448  94.528  36.592 1.00 18.93 ? 557  LEU   B C   1 
ATOM   3815 O  O   . LEU   B 1 116 ? 2.281  94.118  36.618 1.00 23.23 ? 557  LEU   B O   1 
ATOM   3816 C  CB  . LEU   B 1 116 ? 4.141  94.910  38.983 1.00 16.52 ? 557  LEU   B CB  1 
ATOM   3817 C  CG  . LEU   B 1 116 ? 4.845  94.318  40.202 1.00 16.37 ? 557  LEU   B CG  1 
ATOM   3818 C  CD1 . LEU   B 1 116 ? 4.853  95.327  41.324 1.00 16.85 ? 557  LEU   B CD1 1 
ATOM   3819 C  CD2 . LEU   B 1 116 ? 4.154  93.029  40.620 1.00 17.91 ? 557  LEU   B CD2 1 
ATOM   3820 N  N   . THR   B 1 117 ? 3.910  95.310  35.627 1.00 17.31 ? 558  THR   B N   1 
ATOM   3821 C  CA  . THR   B 1 117 ? 3.109  95.642  34.458 1.00 17.97 ? 558  THR   B CA  1 
ATOM   3822 C  C   . THR   B 1 117 ? 3.345  94.689  33.299 1.00 18.23 ? 558  THR   B C   1 
ATOM   3823 O  O   . THR   B 1 117 ? 2.737  94.865  32.238 1.00 19.75 ? 558  THR   B O   1 
ATOM   3824 C  CB  . THR   B 1 117 ? 3.375  97.081  34.012 1.00 18.88 ? 558  THR   B CB  1 
ATOM   3825 O  OG1 . THR   B 1 117 ? 4.770  97.243  33.707 1.00 22.63 ? 558  THR   B OG1 1 
ATOM   3826 C  CG2 . THR   B 1 117 ? 2.932  98.072  35.090 1.00 20.13 ? 558  THR   B CG2 1 
ATOM   3827 N  N   . GLY   B 1 118 ? 4.201  93.690  33.470 1.00 20.19 ? 559  GLY   B N   1 
ATOM   3828 C  CA  . GLY   B 1 118 ? 4.434  92.724  32.421 1.00 20.59 ? 559  GLY   B CA  1 
ATOM   3829 C  C   . GLY   B 1 118 ? 5.355  93.179  31.312 1.00 22.59 ? 559  GLY   B C   1 
ATOM   3830 O  O   . GLY   B 1 118 ? 5.454  92.487  30.290 1.00 25.98 ? 559  GLY   B O   1 
ATOM   3831 N  N   . GLN   B 1 119 ? 6.023  94.325  31.462 1.00 19.08 ? 560  GLN   B N   1 
ATOM   3832 C  CA  . GLN   B 1 119 ? 6.971  94.760  30.437 1.00 21.78 ? 560  GLN   B CA  1 
ATOM   3833 C  C   . GLN   B 1 119 ? 8.184  93.841  30.376 1.00 20.63 ? 560  GLN   B C   1 
ATOM   3834 O  O   . GLN   B 1 119 ? 8.731  93.593  29.296 1.00 24.07 ? 560  GLN   B O   1 
ATOM   3835 C  CB  . GLN   B 1 119 ? 7.398  96.208  30.677 1.00 28.79 ? 560  GLN   B CB  1 
ATOM   3836 C  CG  . GLN   B 1 119 ? 6.285  97.223  30.470 1.00 35.02 ? 560  GLN   B CG  1 
ATOM   3837 C  CD  . GLN   B 1 119 ? 6.704  98.628  30.845 0.67 35.83 ? 560  GLN   B CD  1 
ATOM   3838 O  OE1 . GLN   B 1 119 ? 7.745  99.118  30.403 0.56 35.17 ? 560  GLN   B OE1 1 
ATOM   3839 N  NE2 . GLN   B 1 119 ? 5.900  99.284  31.676 0.59 35.05 ? 560  GLN   B NE2 1 
ATOM   3840 N  N   . VAL   B 1 120 ? 8.636  93.354  31.532 1.00 16.69 ? 561  VAL   B N   1 
ATOM   3841 C  CA  . VAL   B 1 120 ? 9.677  92.340  31.617 1.00 18.07 ? 561  VAL   B CA  1 
ATOM   3842 C  C   . VAL   B 1 120 ? 9.154  91.236  32.526 1.00 16.73 ? 561  VAL   B C   1 
ATOM   3843 O  O   . VAL   B 1 120 ? 8.265  91.452  33.352 1.00 18.33 ? 561  VAL   B O   1 
ATOM   3844 C  CB  . VAL   B 1 120 ? 11.010 92.914  32.153 1.00 17.10 ? 561  VAL   B CB  1 
ATOM   3845 C  CG1 . VAL   B 1 120 ? 11.457 94.119  31.322 1.00 18.17 ? 561  VAL   B CG1 1 
ATOM   3846 C  CG2 . VAL   B 1 120 ? 10.863 93.307  33.633 1.00 18.14 ? 561  VAL   B CG2 1 
ATOM   3847 N  N   . ARG   B 1 121 ? 9.700  90.029  32.352 1.00 17.78 ? 562  ARG   B N   1 
ATOM   3848 C  CA  . ARG   B 1 121 ? 9.349  88.944  33.261 1.00 18.60 ? 562  ARG   B CA  1 
ATOM   3849 C  C   . ARG   B 1 121 ? 10.075 89.080  34.595 1.00 16.50 ? 562  ARG   B C   1 
ATOM   3850 O  O   . ARG   B 1 121 ? 9.502  88.784  35.652 1.00 17.10 ? 562  ARG   B O   1 
ATOM   3851 C  CB  . ARG   B 1 121 ? 9.677  87.586  32.641 1.00 24.01 ? 562  ARG   B CB  1 
ATOM   3852 C  CG  . ARG   B 1 121 ? 9.048  86.423  33.406 1.00 38.74 ? 562  ARG   B CG  1 
ATOM   3853 C  CD  . ARG   B 1 121 ? 9.391  85.066  32.802 1.00 49.89 ? 562  ARG   B CD  1 
ATOM   3854 N  NE  . ARG   B 1 121 ? 8.565  83.997  33.366 1.00 57.77 ? 562  ARG   B NE  1 
ATOM   3855 C  CZ  . ARG   B 1 121 ? 9.046  82.869  33.882 1.00 61.83 ? 562  ARG   B CZ  1 
ATOM   3856 N  NH1 . ARG   B 1 121 ? 10.356 82.654  33.912 1.00 52.70 ? 562  ARG   B NH1 1 
ATOM   3857 N  NH2 . ARG   B 1 121 ? 8.216  81.956  34.371 1.00 64.57 ? 562  ARG   B NH2 1 
ATOM   3858 N  N   . ASN   B 1 122 ? 11.330 89.524  34.561 1.00 15.15 ? 563  ASN   B N   1 
ATOM   3859 C  CA  . ASN   B 1 122 ? 12.200 89.531  35.735 1.00 14.61 ? 563  ASN   B CA  1 
ATOM   3860 C  C   . ASN   B 1 122 ? 13.274 90.592  35.495 1.00 14.45 ? 563  ASN   B C   1 
ATOM   3861 O  O   . ASN   B 1 122 ? 13.333 91.197  34.419 1.00 14.46 ? 563  ASN   B O   1 
ATOM   3862 C  CB  . ASN   B 1 122 ? 12.743 88.118  35.989 1.00 13.32 ? 563  ASN   B CB  1 
ATOM   3863 C  CG  . ASN   B 1 122 ? 13.518 87.545  34.801 1.00 13.96 ? 563  ASN   B CG  1 
ATOM   3864 O  OD1 . ASN   B 1 122 ? 14.215 88.265  34.104 1.00 15.25 ? 563  ASN   B OD1 1 
ATOM   3865 N  ND2 . ASN   B 1 122 ? 13.445 86.233  34.622 1.00 14.06 ? 563  ASN   B ND2 1 
ATOM   3866 N  N   . ALA   B 1 123 ? 14.131 90.830  36.496 1.00 13.94 ? 564  ALA   B N   1 
ATOM   3867 C  CA  . ALA   B 1 123 ? 15.060 91.947  36.368 1.00 14.77 ? 564  ALA   B CA  1 
ATOM   3868 C  C   . ALA   B 1 123 ? 16.182 91.847  37.390 1.00 14.29 ? 564  ALA   B C   1 
ATOM   3869 O  O   . ALA   B 1 123 ? 16.058 91.180  38.422 1.00 13.33 ? 564  ALA   B O   1 
ATOM   3870 C  CB  . ALA   B 1 123 ? 14.346 93.298  36.504 1.00 14.98 ? 564  ALA   B CB  1 
ATOM   3871 N  N   A VAL   B 1 124 ? 17.280 92.537  37.086 0.75 13.87 ? 565  VAL   B N   1 
ATOM   3872 N  N   B VAL   B 1 124 ? 17.282 92.537  37.081 0.25 12.40 ? 565  VAL   B N   1 
ATOM   3873 C  CA  A VAL   B 1 124 ? 18.444 92.631  37.962 0.75 13.83 ? 565  VAL   B CA  1 
ATOM   3874 C  CA  B VAL   B 1 124 ? 18.457 92.646  37.939 0.25 11.09 ? 565  VAL   B CA  1 
ATOM   3875 C  C   A VAL   B 1 124 ? 18.781 94.105  38.151 0.75 12.51 ? 565  VAL   B C   1 
ATOM   3876 C  C   B VAL   B 1 124 ? 18.737 94.125  38.160 0.25 13.60 ? 565  VAL   B C   1 
ATOM   3877 O  O   A VAL   B 1 124 ? 18.721 94.896  37.200 0.75 14.23 ? 565  VAL   B O   1 
ATOM   3878 O  O   B VAL   B 1 124 ? 18.598 94.935  37.236 0.25 11.36 ? 565  VAL   B O   1 
ATOM   3879 C  CB  A VAL   B 1 124 ? 19.637 91.826  37.390 0.75 14.31 ? 565  VAL   B CB  1 
ATOM   3880 C  CB  B VAL   B 1 124 ? 19.675 91.948  37.294 0.25 8.77  ? 565  VAL   B CB  1 
ATOM   3881 C  CG1 A VAL   B 1 124 ? 20.091 92.381  36.043 0.75 14.07 ? 565  VAL   B CG1 1 
ATOM   3882 C  CG1 B VAL   B 1 124 ? 20.998 92.407  37.925 0.25 11.38 ? 565  VAL   B CG1 1 
ATOM   3883 C  CG2 A VAL   B 1 124 ? 20.810 91.787  38.356 0.75 15.09 ? 565  VAL   B CG2 1 
ATOM   3884 C  CG2 B VAL   B 1 124 ? 19.529 90.452  37.386 0.25 8.25  ? 565  VAL   B CG2 1 
ATOM   3885 N  N   . ALA   B 1 125 ? 19.125 94.480  39.384 1.00 12.58 ? 566  ALA   B N   1 
ATOM   3886 C  CA  . ALA   B 1 125 ? 19.407 95.865  39.749 1.00 13.65 ? 566  ALA   B CA  1 
ATOM   3887 C  C   . ALA   B 1 125 ? 20.826 95.945  40.297 1.00 12.71 ? 566  ALA   B C   1 
ATOM   3888 O  O   . ALA   B 1 125 ? 21.100 95.461  41.402 1.00 14.08 ? 566  ALA   B O   1 
ATOM   3889 C  CB  . ALA   B 1 125 ? 18.390 96.385  40.763 1.00 13.97 ? 566  ALA   B CB  1 
ATOM   3890 N  N   . ILE   B 1 126 ? 21.715 96.562  39.522 1.00 12.43 ? 567  ILE   B N   1 
ATOM   3891 C  CA  . ILE   B 1 126 ? 23.136 96.681  39.875 1.00 11.27 ? 567  ILE   B CA  1 
ATOM   3892 C  C   . ILE   B 1 126 ? 23.302 98.040  40.550 1.00 14.83 ? 567  ILE   B C   1 
ATOM   3893 O  O   . ILE   B 1 126 ? 23.609 99.049  39.904 1.00 16.33 ? 567  ILE   B O   1 
ATOM   3894 C  CB  . ILE   B 1 126 ? 24.036 96.511  38.650 1.00 12.00 ? 567  ILE   B CB  1 
ATOM   3895 C  CG1 . ILE   B 1 126 ? 23.665 95.243  37.871 1.00 14.54 ? 567  ILE   B CG1 1 
ATOM   3896 C  CG2 . ILE   B 1 126 ? 25.499 96.505  39.073 1.00 13.68 ? 567  ILE   B CG2 1 
ATOM   3897 C  CD1 . ILE   B 1 126 ? 24.299 95.178  36.462 1.00 14.66 ? 567  ILE   B CD1 1 
ATOM   3898 N  N   . VAL   B 1 127 ? 23.082 98.076  41.870 1.00 12.93 ? 568  VAL   B N   1 
ATOM   3899 C  CA  . VAL   B 1 127 ? 22.905 99.331  42.588 1.00 13.07 ? 568  VAL   B CA  1 
ATOM   3900 C  C   . VAL   B 1 127 ? 23.800 99.361  43.820 1.00 12.31 ? 568  VAL   B C   1 
ATOM   3901 O  O   . VAL   B 1 127 ? 24.146 98.320  44.392 1.00 13.21 ? 568  VAL   B O   1 
ATOM   3902 C  CB  . VAL   B 1 127 ? 21.430 99.557  43.004 1.00 13.10 ? 568  VAL   B CB  1 
ATOM   3903 C  CG1 . VAL   B 1 127 ? 20.532 99.669  41.768 1.00 15.53 ? 568  VAL   B CG1 1 
ATOM   3904 C  CG2 . VAL   B 1 127 ? 20.952 98.445  43.950 1.00 14.40 ? 568  VAL   B CG2 1 
ATOM   3905 N  N   . ARG   B 1 128 ? 24.150 100.574 44.236 1.00 12.71 ? 569  ARG   B N   1 
ATOM   3906 C  CA  . ARG   B 1 128 ? 24.811 100.845 45.506 1.00 12.19 ? 569  ARG   B CA  1 
ATOM   3907 C  C   . ARG   B 1 128 ? 24.493 102.286 45.879 1.00 13.15 ? 569  ARG   B C   1 
ATOM   3908 O  O   . ARG   B 1 128 ? 24.117 103.087 45.008 1.00 14.50 ? 569  ARG   B O   1 
ATOM   3909 C  CB  . ARG   B 1 128 ? 26.330 100.628 45.397 1.00 12.32 ? 569  ARG   B CB  1 
ATOM   3910 C  CG  . ARG   B 1 128 ? 27.044 101.723 44.620 1.00 13.17 ? 569  ARG   B CG  1 
ATOM   3911 C  CD  . ARG   B 1 128 ? 28.534 101.483 44.519 1.00 11.47 ? 569  ARG   B CD  1 
ATOM   3912 N  NE  . ARG   B 1 128 ? 29.274 101.844 45.724 1.00 13.79 ? 569  ARG   B NE  1 
ATOM   3913 C  CZ  . ARG   B 1 128 ? 29.735 103.062 45.992 1.00 14.71 ? 569  ARG   B CZ  1 
ATOM   3914 N  NH1 . ARG   B 1 128 ? 29.489 104.074 45.167 1.00 14.73 ? 569  ARG   B NH1 1 
ATOM   3915 N  NH2 . ARG   B 1 128 ? 30.448 103.264 47.095 1.00 14.13 ? 569  ARG   B NH2 1 
ATOM   3916 N  N   . PRO   B 1 129 ? 24.577 102.644 47.167 1.00 14.04 ? 570  PRO   B N   1 
ATOM   3917 C  CA  . PRO   B 1 129 ? 24.906 101.835 48.346 1.00 14.15 ? 570  PRO   B CA  1 
ATOM   3918 C  C   . PRO   B 1 129 ? 23.839 100.776 48.619 1.00 14.39 ? 570  PRO   B C   1 
ATOM   3919 O  O   . PRO   B 1 129 ? 22.717 100.902 48.133 1.00 14.16 ? 570  PRO   B O   1 
ATOM   3920 C  CB  . PRO   B 1 129 ? 24.944 102.870 49.486 1.00 13.34 ? 570  PRO   B CB  1 
ATOM   3921 C  CG  . PRO   B 1 129 ? 24.046 103.951 49.030 1.00 14.27 ? 570  PRO   B CG  1 
ATOM   3922 C  CD  . PRO   B 1 129 ? 24.197 104.019 47.539 1.00 13.84 ? 570  PRO   B CD  1 
ATOM   3923 N  N   . PRO   B 1 130 ? 24.199 99.746  49.368 1.00 12.95 ? 571  PRO   B N   1 
ATOM   3924 C  CA  . PRO   B 1 130 ? 23.236 98.691  49.727 1.00 12.95 ? 571  PRO   B CA  1 
ATOM   3925 C  C   . PRO   B 1 130 ? 22.138 99.169  50.671 1.00 13.28 ? 571  PRO   B C   1 
ATOM   3926 O  O   . PRO   B 1 130 ? 22.164 100.317 51.131 1.00 13.97 ? 571  PRO   B O   1 
ATOM   3927 C  CB  . PRO   B 1 130 ? 24.115 97.639  50.411 1.00 12.55 ? 571  PRO   B CB  1 
ATOM   3928 C  CG  . PRO   B 1 130 ? 25.293 98.423  50.938 1.00 12.66 ? 571  PRO   B CG  1 
ATOM   3929 C  CD  . PRO   B 1 130 ? 25.550 99.476  49.899 1.00 11.82 ? 571  PRO   B CD  1 
ATOM   3930 N  N   . GLY   B 1 131 ? 21.184 98.290  51.002 1.00 13.59 ? 572  GLY   B N   1 
ATOM   3931 C  CA  . GLY   B 1 131 ? 20.025 98.702  51.775 1.00 13.17 ? 572  GLY   B CA  1 
ATOM   3932 C  C   . GLY   B 1 131 ? 19.649 97.902  53.010 1.00 12.48 ? 572  GLY   B C   1 
ATOM   3933 O  O   . GLY   B 1 131 ? 19.023 98.467  53.914 1.00 12.19 ? 572  GLY   B O   1 
ATOM   3934 N  N   . HIS   B 1 132 ? 19.993 96.612  53.095 1.00 11.32 ? 573  HIS   B N   1 
ATOM   3935 C  CA  . HIS   B 1 132 ? 19.247 95.756  54.027 1.00 12.59 ? 573  HIS   B CA  1 
ATOM   3936 C  C   . HIS   B 1 132 ? 19.555 95.997  55.507 1.00 12.32 ? 573  HIS   B C   1 
ATOM   3937 O  O   . HIS   B 1 132 ? 18.779 95.546  56.359 1.00 13.20 ? 573  HIS   B O   1 
ATOM   3938 C  CB  . HIS   B 1 132 ? 19.327 94.263  53.659 1.00 12.81 ? 573  HIS   B CB  1 
ATOM   3939 C  CG  . HIS   B 1 132 ? 20.670 93.636  53.874 1.00 11.93 ? 573  HIS   B CG  1 
ATOM   3940 N  ND1 . HIS   B 1 132 ? 20.822 92.288  54.117 1.00 13.01 ? 573  HIS   B ND1 1 
ATOM   3941 C  CD2 . HIS   B 1 132 ? 21.919 94.162  53.872 1.00 16.37 ? 573  HIS   B CD2 1 
ATOM   3942 C  CE1 . HIS   B 1 132 ? 22.104 92.010  54.258 1.00 14.19 ? 573  HIS   B CE1 1 
ATOM   3943 N  NE2 . HIS   B 1 132 ? 22.794 93.128  54.113 1.00 16.72 ? 573  HIS   B NE2 1 
ATOM   3944 N  N   . HIS   B 1 133 ? 20.645 96.690  55.846 1.00 12.51 ? 574  HIS   B N   1 
ATOM   3945 C  CA  . HIS   B 1 133 ? 20.894 97.029  57.247 1.00 12.77 ? 574  HIS   B CA  1 
ATOM   3946 C  C   . HIS   B 1 133 ? 20.177 98.295  57.687 1.00 14.00 ? 574  HIS   B C   1 
ATOM   3947 O  O   . HIS   B 1 133 ? 20.117 98.563  58.886 1.00 14.23 ? 574  HIS   B O   1 
ATOM   3948 C  CB  . HIS   B 1 133 ? 22.396 97.202  57.519 1.00 14.11 ? 574  HIS   B CB  1 
ATOM   3949 C  CG  . HIS   B 1 133 ? 23.171 95.933  57.387 1.00 13.65 ? 574  HIS   B CG  1 
ATOM   3950 N  ND1 . HIS   B 1 133 ? 22.865 94.809  58.121 1.00 16.06 ? 574  HIS   B ND1 1 
ATOM   3951 C  CD2 . HIS   B 1 133 ? 24.224 95.602  56.605 1.00 15.39 ? 574  HIS   B CD2 1 
ATOM   3952 C  CE1 . HIS   B 1 133 ? 23.698 93.836  57.796 1.00 15.20 ? 574  HIS   B CE1 1 
ATOM   3953 N  NE2 . HIS   B 1 133 ? 24.538 94.295  56.889 1.00 16.95 ? 574  HIS   B NE2 1 
ATOM   3954 N  N   . ALA   B 1 134 ? 19.654 99.088  56.753 1.00 14.08 ? 575  ALA   B N   1 
ATOM   3955 C  CA  . ALA   B 1 134 ? 19.008 100.347 57.115 1.00 13.45 ? 575  ALA   B CA  1 
ATOM   3956 C  C   . ALA   B 1 134 ? 17.693 100.085 57.836 1.00 14.66 ? 575  ALA   B C   1 
ATOM   3957 O  O   . ALA   B 1 134 ? 16.878 99.273  57.390 1.00 13.51 ? 575  ALA   B O   1 
ATOM   3958 C  CB  . ALA   B 1 134 ? 18.778 101.206 55.872 1.00 14.98 ? 575  ALA   B CB  1 
ATOM   3959 N  N   . GLU   B 1 135 ? 17.489 100.778 58.949 1.00 14.14 ? 576  GLU   B N   1 
ATOM   3960 C  CA  . GLU   B 1 135 ? 16.285 100.657 59.755 1.00 15.00 ? 576  GLU   B CA  1 
ATOM   3961 C  C   . GLU   B 1 135 ? 15.319 101.793 59.436 1.00 16.87 ? 576  GLU   B C   1 
ATOM   3962 O  O   . GLU   B 1 135 ? 15.654 102.745 58.734 1.00 16.98 ? 576  GLU   B O   1 
ATOM   3963 C  CB  . GLU   B 1 135 ? 16.656 100.669 61.242 1.00 17.79 ? 576  GLU   B CB  1 
ATOM   3964 C  CG  . GLU   B 1 135 ? 17.645 99.587  61.647 1.00 18.17 ? 576  GLU   B CG  1 
ATOM   3965 C  CD  . GLU   B 1 135 ? 16.947 98.310  62.059 1.00 22.22 ? 576  GLU   B CD  1 
ATOM   3966 O  OE1 . GLU   B 1 135 ? 15.705 98.273  61.971 1.00 21.13 ? 576  GLU   B OE1 1 
ATOM   3967 O  OE2 . GLU   B 1 135 ? 17.633 97.349  62.466 1.00 23.94 ? 576  GLU   B OE2 1 
ATOM   3968 N  N   . LYS   B 1 136 ? 14.105 101.694 59.985 1.00 16.84 ? 577  LYS   B N   1 
ATOM   3969 C  CA  . LYS   B 1 136 ? 13.154 102.793 59.834 1.00 17.85 ? 577  LYS   B CA  1 
ATOM   3970 C  C   . LYS   B 1 136 ? 13.800 104.132 60.170 1.00 16.95 ? 577  LYS   B C   1 
ATOM   3971 O  O   . LYS   B 1 136 ? 13.658 105.109 59.424 1.00 15.99 ? 577  LYS   B O   1 
ATOM   3972 C  CB  . LYS   B 1 136 ? 11.928 102.561 60.719 1.00 18.33 ? 577  LYS   B CB  1 
ATOM   3973 C  CG  . LYS   B 1 136 ? 10.879 103.661 60.611 1.00 22.26 ? 577  LYS   B CG  1 
ATOM   3974 C  CD  . LYS   B 1 136 ? 9.706  103.396 61.541 1.00 30.90 ? 577  LYS   B CD  1 
ATOM   3975 C  CE  . LYS   B 1 136 ? 8.747  104.575 61.588 1.00 40.72 ? 577  LYS   B CE  1 
ATOM   3976 N  NZ  . LYS   B 1 136 ? 7.630  104.413 60.614 1.00 46.72 ? 577  LYS   B NZ  1 
ATOM   3977 N  N   . ASP   B 1 137 ? 14.546 104.185 61.273 1.00 15.15 ? 578  ASP   B N   1 
ATOM   3978 C  CA  . ASP   B 1 137 ? 15.001 105.446 61.848 1.00 16.39 ? 578  ASP   B CA  1 
ATOM   3979 C  C   . ASP   B 1 137 ? 16.517 105.624 61.840 1.00 19.06 ? 578  ASP   B C   1 
ATOM   3980 O  O   . ASP   B 1 137 ? 17.006 106.598 62.421 1.00 22.41 ? 578  ASP   B O   1 
ATOM   3981 C  CB  . ASP   B 1 137 ? 14.445 105.599 63.274 1.00 30.83 ? 578  ASP   B CB  1 
ATOM   3982 C  CG  . ASP   B 1 137 ? 14.554 107.023 63.812 1.00 43.77 ? 578  ASP   B CG  1 
ATOM   3983 O  OD1 . ASP   B 1 137 ? 14.006 107.953 63.188 1.00 43.19 ? 578  ASP   B OD1 1 
ATOM   3984 O  OD2 . ASP   B 1 137 ? 15.186 107.206 64.878 1.00 42.70 ? 578  ASP   B OD2 1 
ATOM   3985 N  N   . THR   B 1 138 ? 17.283 104.742 61.196 1.00 15.62 ? 579  THR   B N   1 
ATOM   3986 C  CA  . THR   B 1 138 ? 18.730 104.942 61.224 1.00 15.36 ? 579  THR   B CA  1 
ATOM   3987 C  C   . THR   B 1 138 ? 19.420 104.214 60.073 1.00 16.53 ? 579  THR   B C   1 
ATOM   3988 O  O   . THR   B 1 138 ? 18.879 103.274 59.484 1.00 16.76 ? 579  THR   B O   1 
ATOM   3989 C  CB  . THR   B 1 138 ? 19.336 104.544 62.579 1.00 17.47 ? 579  THR   B CB  1 
ATOM   3990 O  OG1 . THR   B 1 138 ? 20.591 105.211 62.744 1.00 20.41 ? 579  THR   B OG1 1 
ATOM   3991 C  CG2 . THR   B 1 138 ? 19.541 103.039 62.678 1.00 16.80 ? 579  THR   B CG2 1 
ATOM   3992 N  N   . ALA   B 1 139 ? 20.621 104.689 59.747 1.00 15.19 ? 580  ALA   B N   1 
ATOM   3993 C  CA  . ALA   B 1 139 ? 21.518 104.053 58.789 1.00 16.38 ? 580  ALA   B CA  1 
ATOM   3994 C  C   . ALA   B 1 139 ? 22.469 103.103 59.518 1.00 18.09 ? 580  ALA   B C   1 
ATOM   3995 O  O   . ALA   B 1 139 ? 22.728 103.254 60.713 1.00 17.78 ? 580  ALA   B O   1 
ATOM   3996 C  CB  . ALA   B 1 139 ? 22.343 105.118 58.067 1.00 14.59 ? 580  ALA   B CB  1 
ATOM   3997 N  N   . CYS   B 1 140 ? 22.999 102.125 58.783 1.00 15.79 ? 581  CYS   B N   1 
ATOM   3998 C  CA  . CYS   B 1 140 ? 23.850 101.110 59.395 1.00 14.30 ? 581  CYS   B CA  1 
ATOM   3999 C  C   . CYS   B 1 140 ? 24.505 100.273 58.310 1.00 13.46 ? 581  CYS   B C   1 
ATOM   4000 O  O   . CYS   B 1 140 ? 23.886 99.998  57.283 1.00 14.50 ? 581  CYS   B O   1 
ATOM   4001 C  CB  . CYS   B 1 140 ? 23.018 100.176 60.284 1.00 17.31 ? 581  CYS   B CB  1 
ATOM   4002 S  SG  . CYS   B 1 140 ? 23.988 98.859  61.048 1.00 20.73 ? 581  CYS   B SG  1 
ATOM   4003 N  N   . GLY   B 1 141 ? 25.745 99.841  58.564 1.00 14.61 ? 582  GLY   B N   1 
ATOM   4004 C  CA  . GLY   B 1 141 ? 26.370 98.806  57.761 1.00 13.23 ? 582  GLY   B CA  1 
ATOM   4005 C  C   . GLY   B 1 141 ? 26.398 99.117  56.275 1.00 12.17 ? 582  GLY   B C   1 
ATOM   4006 O  O   . GLY   B 1 141 ? 26.048 98.265  55.445 1.00 13.50 ? 582  GLY   B O   1 
ATOM   4007 N  N   . PHE   B 1 142 ? 26.802 100.339 55.932 1.00 13.36 ? 583  PHE   B N   1 
ATOM   4008 C  CA  . PHE   B 1 142 ? 26.946 100.840 54.563 1.00 13.65 ? 583  PHE   B CA  1 
ATOM   4009 C  C   . PHE   B 1 142 ? 25.612 101.175 53.902 1.00 14.20 ? 583  PHE   B C   1 
ATOM   4010 O  O   . PHE   B 1 142 ? 25.598 101.550 52.711 1.00 14.27 ? 583  PHE   B O   1 
ATOM   4011 C  CB  . PHE   B 1 142 ? 27.762 99.934  53.612 1.00 14.82 ? 583  PHE   B CB  1 
ATOM   4012 C  CG  . PHE   B 1 142 ? 29.017 99.326  54.216 1.00 14.93 ? 583  PHE   B CG  1 
ATOM   4013 C  CD1 . PHE   B 1 142 ? 29.726 99.944  55.241 1.00 14.33 ? 583  PHE   B CD1 1 
ATOM   4014 C  CD2 . PHE   B 1 142 ? 29.507 98.131  53.699 1.00 18.18 ? 583  PHE   B CD2 1 
ATOM   4015 C  CE1 . PHE   B 1 142 ? 30.883 99.361  55.766 1.00 15.75 ? 583  PHE   B CE1 1 
ATOM   4016 C  CE2 . PHE   B 1 142 ? 30.665 97.547  54.211 1.00 19.92 ? 583  PHE   B CE2 1 
ATOM   4017 C  CZ  . PHE   B 1 142 ? 31.341 98.159  55.250 1.00 16.75 ? 583  PHE   B CZ  1 
ATOM   4018 N  N   . CYS   B 1 143 ? 24.494 101.069 54.628 1.00 13.63 ? 584  CYS   B N   1 
ATOM   4019 C  CA  . CYS   B 1 143 ? 23.154 101.220 54.066 1.00 13.92 ? 584  CYS   B CA  1 
ATOM   4020 C  C   . CYS   B 1 143 ? 22.481 102.467 54.637 1.00 13.97 ? 584  CYS   B C   1 
ATOM   4021 O  O   . CYS   B 1 143 ? 22.461 102.672 55.860 1.00 13.54 ? 584  CYS   B O   1 
ATOM   4022 C  CB  . CYS   B 1 143 ? 22.280 100.004 54.408 1.00 15.42 ? 584  CYS   B CB  1 
ATOM   4023 S  SG  . CYS   B 1 143 ? 22.946 98.397  53.951 1.00 39.30 ? 584  CYS   B SG  1 
ATOM   4024 N  N   . PHE   B 1 144 ? 21.904 103.289 53.756 1.00 14.83 ? 585  PHE   B N   1 
ATOM   4025 C  CA  . PHE   B 1 144 ? 21.182 104.493 54.166 1.00 14.33 ? 585  PHE   B CA  1 
ATOM   4026 C  C   . PHE   B 1 144 ? 19.673 104.302 54.195 1.00 14.75 ? 585  PHE   B C   1 
ATOM   4027 O  O   . PHE   B 1 144 ? 19.024 104.652 55.187 1.00 15.07 ? 585  PHE   B O   1 
ATOM   4028 C  CB  . PHE   B 1 144 ? 21.532 105.669 53.254 1.00 15.30 ? 585  PHE   B CB  1 
ATOM   4029 C  CG  . PHE   B 1 144 ? 22.962 106.075 53.347 1.00 14.81 ? 585  PHE   B CG  1 
ATOM   4030 C  CD1 . PHE   B 1 144 ? 23.379 106.978 54.316 1.00 16.79 ? 585  PHE   B CD1 1 
ATOM   4031 C  CD2 . PHE   B 1 144 ? 23.895 105.514 52.511 1.00 15.05 ? 585  PHE   B CD2 1 
ATOM   4032 C  CE1 . PHE   B 1 144 ? 24.710 107.338 54.417 1.00 16.47 ? 585  PHE   B CE1 1 
ATOM   4033 C  CE2 . PHE   B 1 144 ? 25.229 105.871 52.601 1.00 15.30 ? 585  PHE   B CE2 1 
ATOM   4034 C  CZ  . PHE   B 1 144 ? 25.634 106.785 53.551 1.00 15.32 ? 585  PHE   B CZ  1 
ATOM   4035 N  N   . PHE   B 1 145 ? 19.101 103.791 53.109 1.00 13.25 ? 586  PHE   B N   1 
ATOM   4036 C  CA  . PHE   B 1 145 ? 17.685 103.488 53.015 1.00 13.70 ? 586  PHE   B CA  1 
ATOM   4037 C  C   . PHE   B 1 145 ? 17.526 102.041 52.580 1.00 13.19 ? 586  PHE   B C   1 
ATOM   4038 O  O   . PHE   B 1 145 ? 18.373 101.495 51.867 1.00 13.99 ? 586  PHE   B O   1 
ATOM   4039 C  CB  . PHE   B 1 145 ? 16.961 104.413 52.019 1.00 14.28 ? 586  PHE   B CB  1 
ATOM   4040 C  CG  . PHE   B 1 145 ? 17.174 105.880 52.286 1.00 13.04 ? 586  PHE   B CG  1 
ATOM   4041 C  CD1 . PHE   B 1 145 ? 16.807 106.432 53.502 1.00 15.86 ? 586  PHE   B CD1 1 
ATOM   4042 C  CD2 . PHE   B 1 145 ? 17.729 106.704 51.320 1.00 15.82 ? 586  PHE   B CD2 1 
ATOM   4043 C  CE1 . PHE   B 1 145 ? 17.008 107.785 53.749 1.00 16.74 ? 586  PHE   B CE1 1 
ATOM   4044 C  CE2 . PHE   B 1 145 ? 17.920 108.055 51.567 1.00 16.53 ? 586  PHE   B CE2 1 
ATOM   4045 C  CZ  . PHE   B 1 145 ? 17.564 108.589 52.772 1.00 16.42 ? 586  PHE   B CZ  1 
ATOM   4046 N  N   . ASN   B 1 146 ? 16.436 101.413 53.017 1.00 12.92 ? 587  ASN   B N   1 
ATOM   4047 C  CA  . ASN   B 1 146 ? 16.288 99.977  52.810 1.00 12.11 ? 587  ASN   B CA  1 
ATOM   4048 C  C   . ASN   B 1 146 ? 15.635 99.746  51.455 1.00 12.76 ? 587  ASN   B C   1 
ATOM   4049 O  O   . ASN   B 1 146 ? 14.412 99.623  51.325 1.00 13.63 ? 587  ASN   B O   1 
ATOM   4050 C  CB  . ASN   B 1 146 ? 15.523 99.312  53.944 1.00 11.96 ? 587  ASN   B CB  1 
ATOM   4051 C  CG  . ASN   B 1 146 ? 15.708 97.815  53.930 1.00 11.95 ? 587  ASN   B CG  1 
ATOM   4052 O  OD1 . ASN   B 1 146 ? 15.639 97.182  52.859 1.00 13.79 ? 587  ASN   B OD1 1 
ATOM   4053 N  ND2 . ASN   B 1 146 ? 15.990 97.243  55.091 1.00 13.35 ? 587  ASN   B ND2 1 
ATOM   4054 N  N   . THR   B 1 147 ? 16.489 99.661  50.442 1.00 12.22 ? 588  THR   B N   1 
ATOM   4055 C  CA  . THR   B 1 147 ? 16.049 99.556  49.055 1.00 13.14 ? 588  THR   B CA  1 
ATOM   4056 C  C   . THR   B 1 147 ? 15.055 98.414  48.854 1.00 13.04 ? 588  THR   B C   1 
ATOM   4057 O  O   . THR   B 1 147 ? 13.974 98.616  48.282 1.00 12.61 ? 588  THR   B O   1 
ATOM   4058 C  CB  . THR   B 1 147 ? 17.291 99.375  48.197 1.00 13.33 ? 588  THR   B CB  1 
ATOM   4059 O  OG1 . THR   B 1 147 ? 18.112 100.537 48.346 1.00 15.78 ? 588  THR   B OG1 1 
ATOM   4060 C  CG2 . THR   B 1 147 ? 16.929 99.195  46.728 1.00 15.17 ? 588  THR   B CG2 1 
ATOM   4061 N  N   . ALA   B 1 148 ? 15.378 97.213  49.338 1.00 13.85 ? 589  ALA   B N   1 
ATOM   4062 C  CA  . ALA   B 1 148 ? 14.475 96.079  49.136 1.00 14.17 ? 589  ALA   B CA  1 
ATOM   4063 C  C   . ALA   B 1 148 ? 13.145 96.267  49.864 1.00 12.31 ? 589  ALA   B C   1 
ATOM   4064 O  O   . ALA   B 1 148 ? 12.078 95.974  49.305 1.00 12.66 ? 589  ALA   B O   1 
ATOM   4065 C  CB  . ALA   B 1 148 ? 15.150 94.769  49.540 1.00 15.30 ? 589  ALA   B CB  1 
ATOM   4066 N  N   . ALA   B 1 149 ? 13.190 96.744  51.110 1.00 11.76 ? 590  ALA   B N   1 
ATOM   4067 C  CA  . ALA   B 1 149 ? 11.960 96.989  51.851 1.00 11.70 ? 590  ALA   B CA  1 
ATOM   4068 C  C   . ALA   B 1 149 ? 11.109 98.045  51.161 1.00 13.12 ? 590  ALA   B C   1 
ATOM   4069 O  O   . ALA   B 1 149 ? 9.891  97.876  51.014 1.00 20.48 ? 590  ALA   B O   1 
ATOM   4070 C  CB  . ALA   B 1 149 ? 12.300 97.420  53.278 1.00 11.03 ? 590  ALA   B CB  1 
ATOM   4071 N  N   . LEU   B 1 150 ? 11.728 99.142  50.738 1.00 11.55 ? 591  LEU   B N   1 
ATOM   4072 C  CA  . LEU   B 1 150 ? 11.015 100.188 50.019 1.00 13.58 ? 591  LEU   B CA  1 
ATOM   4073 C  C   . LEU   B 1 150 ? 10.395 99.652  48.736 1.00 14.46 ? 591  LEU   B C   1 
ATOM   4074 O  O   . LEU   B 1 150 ? 9.274  100.030 48.381 1.00 14.34 ? 591  LEU   B O   1 
ATOM   4075 C  CB  . LEU   B 1 150 ? 11.971 101.331 49.687 1.00 12.48 ? 591  LEU   B CB  1 
ATOM   4076 C  CG  . LEU   B 1 150 ? 12.428 102.180 50.870 1.00 12.06 ? 591  LEU   B CG  1 
ATOM   4077 C  CD1 . LEU   B 1 150 ? 13.629 103.018 50.466 1.00 14.59 ? 591  LEU   B CD1 1 
ATOM   4078 C  CD2 . LEU   B 1 150 ? 11.284 103.052 51.346 1.00 15.64 ? 591  LEU   B CD2 1 
ATOM   4079 N  N   . THR   B 1 151 ? 11.115 98.780  48.020 1.00 12.14 ? 592  THR   B N   1 
ATOM   4080 C  CA  . THR   B 1 151 ? 10.598 98.226  46.771 1.00 12.73 ? 592  THR   B CA  1 
ATOM   4081 C  C   . THR   B 1 151 ? 9.370  97.354  47.019 1.00 13.47 ? 592  THR   B C   1 
ATOM   4082 O  O   . THR   B 1 151 ? 8.416  97.375  46.236 1.00 12.73 ? 592  THR   B O   1 
ATOM   4083 C  CB  . THR   B 1 151 ? 11.712 97.468  46.036 1.00 12.50 ? 592  THR   B CB  1 
ATOM   4084 O  OG1 . THR   B 1 151 ? 12.802 98.359  45.755 1.00 14.10 ? 592  THR   B OG1 1 
ATOM   4085 C  CG2 . THR   B 1 151 ? 11.203 96.914  44.714 1.00 13.60 ? 592  THR   B CG2 1 
ATOM   4086 N  N   . ALA   B 1 152 ? 9.364  96.588  48.106 1.00 11.81 ? 593  ALA   B N   1 
ATOM   4087 C  CA  . ALA   B 1 152 ? 8.174  95.822  48.464 1.00 13.43 ? 593  ALA   B CA  1 
ATOM   4088 C  C   . ALA   B 1 152 ? 6.970  96.738  48.690 1.00 14.13 ? 593  ALA   B C   1 
ATOM   4089 O  O   . ALA   B 1 152 ? 5.875  96.490  48.164 1.00 14.80 ? 593  ALA   B O   1 
ATOM   4090 C  CB  . ALA   B 1 152 ? 8.472  94.976  49.706 1.00 12.98 ? 593  ALA   B CB  1 
ATOM   4091 N  N   . ARG   B 1 153 ? 7.155  97.820  49.453 1.00 13.18 ? 594  ARG   B N   1 
ATOM   4092 C  CA  . ARG   B 1 153 ? 6.053  98.753  49.699 1.00 15.74 ? 594  ARG   B CA  1 
ATOM   4093 C  C   . ARG   B 1 153 ? 5.676  99.526  48.440 1.00 14.79 ? 594  ARG   B C   1 
ATOM   4094 O  O   . ARG   B 1 153 ? 4.491  99.812  48.215 1.00 15.01 ? 594  ARG   B O   1 
ATOM   4095 C  CB  . ARG   B 1 153 ? 6.419  99.717  50.832 1.00 15.05 ? 594  ARG   B CB  1 
ATOM   4096 C  CG  . ARG   B 1 153 ? 6.606  99.085  52.184 1.00 19.55 ? 594  ARG   B CG  1 
ATOM   4097 C  CD  . ARG   B 1 153 ? 5.336  98.487  52.663 1.00 21.29 ? 594  ARG   B CD  1 
ATOM   4098 N  NE  . ARG   B 1 153 ? 5.403  98.199  54.091 1.00 22.08 ? 594  ARG   B NE  1 
ATOM   4099 C  CZ  . ARG   B 1 153 ? 4.711  97.231  54.668 1.00 24.74 ? 594  ARG   B CZ  1 
ATOM   4100 N  NH1 . ARG   B 1 153 ? 3.898  96.474  53.929 1.00 18.91 ? 594  ARG   B NH1 1 
ATOM   4101 N  NH2 . ARG   B 1 153 ? 4.821  97.022  55.980 1.00 25.04 ? 594  ARG   B NH2 1 
ATOM   4102 N  N   . TYR   B 1 154 ? 6.661  99.882  47.610 1.00 14.08 ? 595  TYR   B N   1 
ATOM   4103 C  CA  . TYR   B 1 154 ? 6.336  100.545 46.352 1.00 15.63 ? 595  TYR   B CA  1 
ATOM   4104 C  C   . TYR   B 1 154 ? 5.491  99.633  45.468 1.00 14.95 ? 595  TYR   B C   1 
ATOM   4105 O  O   . TYR   B 1 154 ? 4.488  100.069 44.877 1.00 14.01 ? 595  TYR   B O   1 
ATOM   4106 C  CB  . TYR   B 1 154 ? 7.613  100.975 45.619 1.00 15.94 ? 595  TYR   B CB  1 
ATOM   4107 C  CG  . TYR   B 1 154 ? 7.306  101.412 44.202 1.00 16.04 ? 595  TYR   B CG  1 
ATOM   4108 C  CD1 . TYR   B 1 154 ? 6.856  102.701 43.936 1.00 16.41 ? 595  TYR   B CD1 1 
ATOM   4109 C  CD2 . TYR   B 1 154 ? 7.404  100.518 43.146 1.00 15.98 ? 595  TYR   B CD2 1 
ATOM   4110 C  CE1 . TYR   B 1 154 ? 6.541  103.093 42.639 1.00 14.52 ? 595  TYR   B CE1 1 
ATOM   4111 C  CE2 . TYR   B 1 154 ? 7.089  100.898 41.849 1.00 15.46 ? 595  TYR   B CE2 1 
ATOM   4112 C  CZ  . TYR   B 1 154 ? 6.660  102.186 41.608 1.00 15.89 ? 595  TYR   B CZ  1 
ATOM   4113 O  OH  . TYR   B 1 154 ? 6.341  102.574 40.319 1.00 18.51 ? 595  TYR   B OH  1 
ATOM   4114 N  N   . ALA   B 1 155 ? 5.897  98.365  45.354 1.00 13.75 ? 596  ALA   B N   1 
ATOM   4115 C  CA  . ALA   B 1 155 ? 5.133  97.377  44.603 1.00 13.15 ? 596  ALA   B CA  1 
ATOM   4116 C  C   . ALA   B 1 155 ? 3.689  97.316  45.087 1.00 14.21 ? 596  ALA   B C   1 
ATOM   4117 O  O   . ALA   B 1 155 ? 2.751  97.321  44.278 1.00 14.63 ? 596  ALA   B O   1 
ATOM   4118 C  CB  . ALA   B 1 155 ? 5.795  96.006  44.737 1.00 14.40 ? 596  ALA   B CB  1 
ATOM   4119 N  N   . GLN   B 1 156 ? 3.489  97.264  46.409 1.00 12.41 ? 597  GLN   B N   1 
ATOM   4120 C  CA  . GLN   B 1 156 ? 2.135  97.268  46.949 1.00 15.09 ? 597  GLN   B CA  1 
ATOM   4121 C  C   . GLN   B 1 156 ? 1.378  98.539  46.572 1.00 17.42 ? 597  GLN   B C   1 
ATOM   4122 O  O   . GLN   B 1 156 ? 0.170  98.486  46.296 1.00 17.24 ? 597  GLN   B O   1 
ATOM   4123 C  CB  . GLN   B 1 156 ? 2.202  97.063  48.466 1.00 13.60 ? 597  GLN   B CB  1 
ATOM   4124 C  CG  . GLN   B 1 156 ? 2.530  95.624  48.844 1.00 14.76 ? 597  GLN   B CG  1 
ATOM   4125 C  CD  . GLN   B 1 156 ? 2.888  95.431  50.311 1.00 15.56 ? 597  GLN   B CD  1 
ATOM   4126 O  OE1 . GLN   B 1 156 ? 3.130  96.390  51.046 1.00 16.94 ? 597  GLN   B OE1 1 
ATOM   4127 N  NE2 . GLN   B 1 156 ? 2.874  94.180  50.749 1.00 14.54 ? 597  GLN   B NE2 1 
ATOM   4128 N  N   . SER   B 1 157 ? 2.063  99.682  46.524 1.00 15.39 ? 598  SER   B N   1 
ATOM   4129 C  CA  . SER   B 1 157 ? 1.408  100.958 46.263 1.00 16.49 ? 598  SER   B CA  1 
ATOM   4130 C  C   . SER   B 1 157 ? 0.891  101.062 44.832 1.00 19.23 ? 598  SER   B C   1 
ATOM   4131 O  O   . SER   B 1 157 ? -0.019 101.857 44.566 1.00 18.85 ? 598  SER   B O   1 
ATOM   4132 C  CB  . SER   B 1 157 ? 2.347  102.125 46.580 1.00 16.80 ? 598  SER   B CB  1 
ATOM   4133 O  OG  . SER   B 1 157 ? 3.308  102.336 45.555 1.00 17.29 ? 598  SER   B OG  1 
ATOM   4134 N  N   . ILE   B 1 158 ? 1.457  100.297 43.902 1.00 16.29 ? 599  ILE   B N   1 
ATOM   4135 C  CA  . ILE   B 1 158 ? 1.028  100.324 42.506 1.00 16.71 ? 599  ILE   B CA  1 
ATOM   4136 C  C   . ILE   B 1 158 ? 0.237  99.095  42.110 1.00 16.48 ? 599  ILE   B C   1 
ATOM   4137 O  O   . ILE   B 1 158 ? -0.128 98.962  40.930 1.00 18.15 ? 599  ILE   B O   1 
ATOM   4138 C  CB  . ILE   B 1 158 ? 2.197  100.568 41.528 1.00 16.37 ? 599  ILE   B CB  1 
ATOM   4139 C  CG1 . ILE   B 1 158 ? 3.209  99.414  41.574 1.00 15.01 ? 599  ILE   B CG1 1 
ATOM   4140 C  CG2 . ILE   B 1 158 ? 2.837  101.919 41.812 1.00 17.35 ? 599  ILE   B CG2 1 
ATOM   4141 C  CD1 . ILE   B 1 158 ? 4.135  99.389  40.376 1.00 16.02 ? 599  ILE   B CD1 1 
ATOM   4142 N  N   . THR   B 1 159 ? -0.037 98.189  43.047 1.00 18.86 ? 600  THR   B N   1 
ATOM   4143 C  CA  . THR   B 1 159 ? -0.874 97.027  42.778 1.00 16.57 ? 600  THR   B CA  1 
ATOM   4144 C  C   . THR   B 1 159 ? -2.029 96.998  43.769 1.00 19.36 ? 600  THR   B C   1 
ATOM   4145 O  O   . THR   B 1 159 ? -3.023 97.705  43.580 1.00 21.00 ? 600  THR   B O   1 
ATOM   4146 C  CB  . THR   B 1 159 ? -0.055 95.727  42.789 1.00 17.81 ? 600  THR   B CB  1 
ATOM   4147 O  OG1 . THR   B 1 159 ? 0.641  95.582  44.042 1.00 17.28 ? 600  THR   B OG1 1 
ATOM   4148 C  CG2 . THR   B 1 159 ? 0.948  95.730  41.648 1.00 16.36 ? 600  THR   B CG2 1 
ATOM   4149 N  N   . ARG   B 1 160 ? -1.921 96.191  44.818 1.00 19.73 ? 601  ARG   B N   1 
ATOM   4150 C  CA  . ARG   B 1 160 ? -2.837 96.297  45.938 1.00 22.88 ? 601  ARG   B CA  1 
ATOM   4151 C  C   . ARG   B 1 160 ? -2.030 96.266  47.223 1.00 21.94 ? 601  ARG   B C   1 
ATOM   4152 O  O   . ARG   B 1 160 ? -0.925 95.715  47.273 1.00 21.55 ? 601  ARG   B O   1 
ATOM   4153 C  CB  . ARG   B 1 160 ? -3.918 95.211  45.964 1.00 23.16 ? 601  ARG   B CB  1 
ATOM   4154 C  CG  . ARG   B 1 160 ? -3.409 93.803  46.042 1.00 24.61 ? 601  ARG   B CG  1 
ATOM   4155 C  CD  . ARG   B 1 160 ? -4.528 92.852  46.504 1.00 26.69 ? 601  ARG   B CD  1 
ATOM   4156 N  NE  . ARG   B 1 160 ? -3.954 91.722  47.223 1.00 27.54 ? 601  ARG   B NE  1 
ATOM   4157 C  CZ  . ARG   B 1 160 ? -3.273 90.740  46.639 1.00 38.83 ? 601  ARG   B CZ  1 
ATOM   4158 N  NH1 . ARG   B 1 160 ? -3.100 90.741  45.323 1.00 41.46 ? 601  ARG   B NH1 1 
ATOM   4159 N  NH2 . ARG   B 1 160 ? -2.763 89.758  47.367 1.00 33.13 ? 601  ARG   B NH2 1 
ATOM   4160 N  N   . GLU   B 1 161 ? -2.599 96.873  48.265 1.00 21.47 ? 602  GLU   B N   1 
ATOM   4161 C  CA  . GLU   B 1 161 ? -1.848 97.058  49.502 1.00 23.57 ? 602  GLU   B CA  1 
ATOM   4162 C  C   . GLU   B 1 161 ? -1.361 95.743  50.086 1.00 20.68 ? 602  GLU   B C   1 
ATOM   4163 O  O   . GLU   B 1 161 ? -0.281 95.703  50.687 1.00 21.01 ? 602  GLU   B O   1 
ATOM   4164 C  CB  . GLU   B 1 161 ? -2.669 97.836  50.530 1.00 33.12 ? 602  GLU   B CB  1 
ATOM   4165 C  CG  . GLU   B 1 161 ? -2.699 99.345  50.314 1.00 42.35 ? 602  GLU   B CG  1 
ATOM   4166 C  CD  . GLU   B 1 161 ? -1.394 99.921  49.776 1.00 54.04 ? 602  GLU   B CD  1 
ATOM   4167 O  OE1 . GLU   B 1 161 ? -0.298 99.532  50.244 1.00 60.25 ? 602  GLU   B OE1 1 
ATOM   4168 O  OE2 . GLU   B 1 161 ? -1.468 100.774 48.867 1.00 55.86 ? 602  GLU   B OE2 1 
ATOM   4169 N  N   . SER   B 1 162 ? -2.115 94.661  49.900 1.00 19.80 ? 603  SER   B N   1 
ATOM   4170 C  CA  . SER   B 1 162 ? -1.805 93.365  50.484 1.00 22.70 ? 603  SER   B CA  1 
ATOM   4171 C  C   . SER   B 1 162 ? -1.058 92.437  49.529 1.00 19.09 ? 603  SER   B C   1 
ATOM   4172 O  O   . SER   B 1 162 ? -1.003 91.230  49.779 1.00 19.26 ? 603  SER   B O   1 
ATOM   4173 C  CB  . SER   B 1 162 ? -3.087 92.683  50.964 1.00 35.96 ? 603  SER   B CB  1 
ATOM   4174 O  OG  . SER   B 1 162 ? -3.411 93.074  52.285 1.00 48.04 ? 603  SER   B OG  1 
ATOM   4175 N  N   . LEU   B 1 163 ? -0.500 92.963  48.438 1.00 15.67 ? 604  LEU   B N   1 
ATOM   4176 C  CA  . LEU   B 1 163 ? 0.249  92.124  47.507 1.00 16.95 ? 604  LEU   B CA  1 
ATOM   4177 C  C   . LEU   B 1 163 ? 1.314  91.332  48.258 1.00 15.43 ? 604  LEU   B C   1 
ATOM   4178 O  O   . LEU   B 1 163 ? 2.060  91.883  49.069 1.00 16.01 ? 604  LEU   B O   1 
ATOM   4179 C  CB  . LEU   B 1 163 ? 0.914  93.001  46.445 1.00 17.71 ? 604  LEU   B CB  1 
ATOM   4180 C  CG  . LEU   B 1 163 ? 1.624  92.261  45.310 1.00 18.38 ? 604  LEU   B CG  1 
ATOM   4181 C  CD1 . LEU   B 1 163 ? 0.604  91.943  44.224 1.00 19.24 ? 604  LEU   B CD1 1 
ATOM   4182 C  CD2 . LEU   B 1 163 ? 2.786  93.078  44.735 1.00 19.05 ? 604  LEU   B CD2 1 
ATOM   4183 N  N   . ARG   B 1 164 ? 1.362  90.029  48.012 1.00 16.70 ? 605  ARG   B N   1 
ATOM   4184 C  CA  . ARG   B 1 164 ? 2.272  89.160  48.749 1.00 16.32 ? 605  ARG   B CA  1 
ATOM   4185 C  C   . ARG   B 1 164 ? 3.662  89.260  48.131 1.00 15.50 ? 605  ARG   B C   1 
ATOM   4186 O  O   . ARG   B 1 164 ? 3.875  88.868  46.974 1.00 16.29 ? 605  ARG   B O   1 
ATOM   4187 C  CB  . ARG   B 1 164 ? 1.757  87.726  48.737 1.00 16.45 ? 605  ARG   B CB  1 
ATOM   4188 C  CG  . ARG   B 1 164 ? 0.471  87.550  49.553 1.00 17.77 ? 605  ARG   B CG  1 
ATOM   4189 C  CD  . ARG   B 1 164 ? 0.076  86.084  49.677 1.00 19.12 ? 605  ARG   B CD  1 
ATOM   4190 N  NE  . ARG   B 1 164 ? -0.074 85.440  48.377 1.00 21.43 ? 605  ARG   B NE  1 
ATOM   4191 C  CZ  . ARG   B 1 164 ? -1.131 85.591  47.587 1.00 26.79 ? 605  ARG   B CZ  1 
ATOM   4192 N  NH1 . ARG   B 1 164 ? -2.141 86.361  47.970 1.00 24.42 ? 605  ARG   B NH1 1 
ATOM   4193 N  NH2 . ARG   B 1 164 ? -1.182 84.974  46.413 1.00 25.97 ? 605  ARG   B NH2 1 
ATOM   4194 N  N   . VAL   B 1 165 ? 4.608  89.801  48.891 1.00 13.67 ? 606  VAL   B N   1 
ATOM   4195 C  CA  . VAL   B 1 165 ? 5.987  89.960  48.435 1.00 13.57 ? 606  VAL   B CA  1 
ATOM   4196 C  C   . VAL   B 1 165 ? 6.877  89.063  49.280 1.00 12.61 ? 606  VAL   B C   1 
ATOM   4197 O  O   . VAL   B 1 165 ? 6.825  89.109  50.518 1.00 13.47 ? 606  VAL   B O   1 
ATOM   4198 C  CB  . VAL   B 1 165 ? 6.449  91.425  48.509 1.00 13.69 ? 606  VAL   B CB  1 
ATOM   4199 C  CG1 . VAL   B 1 165 ? 7.865  91.582  47.938 1.00 13.84 ? 606  VAL   B CG1 1 
ATOM   4200 C  CG2 . VAL   B 1 165 ? 5.458  92.347  47.813 1.00 15.03 ? 606  VAL   B CG2 1 
ATOM   4201 N  N   . LEU   B 1 166 ? 7.658  88.217  48.621 1.00 13.37 ? 607  LEU   B N   1 
ATOM   4202 C  CA  . LEU   B 1 166 ? 8.690  87.444  49.293 1.00 13.18 ? 607  LEU   B CA  1 
ATOM   4203 C  C   . LEU   B 1 166 ? 10.018 88.162  49.111 1.00 13.55 ? 607  LEU   B C   1 
ATOM   4204 O  O   . LEU   B 1 166 ? 10.363 88.543  47.987 1.00 14.59 ? 607  LEU   B O   1 
ATOM   4205 C  CB  . LEU   B 1 166 ? 8.792  86.039  48.701 1.00 13.72 ? 607  LEU   B CB  1 
ATOM   4206 C  CG  . LEU   B 1 166 ? 10.065 85.250  49.030 1.00 14.90 ? 607  LEU   B CG  1 
ATOM   4207 C  CD1 . LEU   B 1 166 ? 10.141 84.943  50.514 1.00 14.45 ? 607  LEU   B CD1 1 
ATOM   4208 C  CD2 . LEU   B 1 166 ? 10.088 83.964  48.232 1.00 15.56 ? 607  LEU   B CD2 1 
ATOM   4209 N  N   . ILE   B 1 167 ? 10.756 88.354  50.208 1.00 13.04 ? 608  ILE   B N   1 
ATOM   4210 C  CA  . ILE   B 1 167 ? 12.129 88.856  50.144 1.00 13.03 ? 608  ILE   B CA  1 
ATOM   4211 C  C   . ILE   B 1 167 ? 13.034 87.736  50.625 1.00 12.38 ? 608  ILE   B C   1 
ATOM   4212 O  O   . ILE   B 1 167 ? 12.953 87.326  51.791 1.00 13.83 ? 608  ILE   B O   1 
ATOM   4213 C  CB  . ILE   B 1 167 ? 12.348 90.108  51.003 1.00 12.37 ? 608  ILE   B CB  1 
ATOM   4214 C  CG1 . ILE   B 1 167 ? 11.401 91.238  50.574 1.00 13.51 ? 608  ILE   B CG1 1 
ATOM   4215 C  CG2 . ILE   B 1 167 ? 13.838 90.531  50.970 1.00 13.25 ? 608  ILE   B CG2 1 
ATOM   4216 C  CD1 . ILE   B 1 167 ? 11.521 92.497  51.420 1.00 13.94 ? 608  ILE   B CD1 1 
ATOM   4217 N  N   . VAL   B 1 168 ? 13.887 87.234  49.731 1.00 11.62 ? 609  VAL   B N   1 
ATOM   4218 C  CA  . VAL   B 1 168 ? 14.921 86.268  50.086 1.00 13.27 ? 609  VAL   B CA  1 
ATOM   4219 C  C   . VAL   B 1 168 ? 16.234 87.030  50.176 1.00 12.75 ? 609  VAL   B C   1 
ATOM   4220 O  O   . VAL   B 1 168 ? 16.643 87.690  49.217 1.00 12.48 ? 609  VAL   B O   1 
ATOM   4221 C  CB  . VAL   B 1 168 ? 15.020 85.135  49.054 1.00 13.27 ? 609  VAL   B CB  1 
ATOM   4222 C  CG1 . VAL   B 1 168 ? 16.164 84.206  49.410 1.00 14.55 ? 609  VAL   B CG1 1 
ATOM   4223 C  CG2 . VAL   B 1 168 ? 13.695 84.375  48.950 1.00 15.06 ? 609  VAL   B CG2 1 
ATOM   4224 N  N   . ASP   B 1 169 ? 16.878 86.964  51.325 1.00 13.36 ? 610  ASP   B N   1 
ATOM   4225 C  CA  . ASP   B 1 169 ? 18.096 87.729  51.596 1.00 12.44 ? 610  ASP   B CA  1 
ATOM   4226 C  C   . ASP   B 1 169 ? 19.234 86.727  51.750 1.00 14.08 ? 610  ASP   B C   1 
ATOM   4227 O  O   . ASP   B 1 169 ? 19.370 86.085  52.796 1.00 17.11 ? 610  ASP   B O   1 
ATOM   4228 C  CB  . ASP   B 1 169 ? 17.865 88.538  52.872 1.00 13.27 ? 610  ASP   B CB  1 
ATOM   4229 C  CG  . ASP   B 1 169 ? 18.986 89.494  53.199 1.00 14.66 ? 610  ASP   B CG  1 
ATOM   4230 O  OD1 . ASP   B 1 169 ? 20.139 89.203  52.857 1.00 13.65 ? 610  ASP   B OD1 1 
ATOM   4231 O  OD2 . ASP   B 1 169 ? 18.701 90.527  53.857 1.00 14.65 ? 610  ASP   B OD2 1 
ATOM   4232 N  N   . TRP   B 1 170 ? 20.054 86.590  50.709 1.00 11.95 ? 611  TRP   B N   1 
ATOM   4233 C  CA  . TRP   B 1 170 ? 21.161 85.651  50.745 1.00 13.22 ? 611  TRP   B CA  1 
ATOM   4234 C  C   . TRP   B 1 170 ? 22.514 86.318  50.937 1.00 13.01 ? 611  TRP   B C   1 
ATOM   4235 O  O   . TRP   B 1 170 ? 23.538 85.636  50.890 1.00 14.09 ? 611  TRP   B O   1 
ATOM   4236 C  CB  . TRP   B 1 170 ? 21.139 84.694  49.551 1.00 13.64 ? 611  TRP   B CB  1 
ATOM   4237 C  CG  . TRP   B 1 170 ? 21.512 85.224  48.170 1.00 12.74 ? 611  TRP   B CG  1 
ATOM   4238 C  CD1 . TRP   B 1 170 ? 22.522 86.085  47.851 1.00 12.75 ? 611  TRP   B CD1 1 
ATOM   4239 C  CD2 . TRP   B 1 170 ? 20.880 84.876  46.934 1.00 13.42 ? 611  TRP   B CD2 1 
ATOM   4240 N  NE1 . TRP   B 1 170 ? 22.559 86.295  46.485 1.00 13.27 ? 611  TRP   B NE1 1 
ATOM   4241 C  CE2 . TRP   B 1 170 ? 21.560 85.559  45.905 1.00 14.17 ? 611  TRP   B CE2 1 
ATOM   4242 C  CE3 . TRP   B 1 170 ? 19.807 84.043  46.599 1.00 13.93 ? 611  TRP   B CE3 1 
ATOM   4243 C  CZ2 . TRP   B 1 170 ? 21.188 85.447  44.555 1.00 13.49 ? 611  TRP   B CZ2 1 
ATOM   4244 C  CZ3 . TRP   B 1 170 ? 19.441 83.931  45.271 1.00 14.55 ? 611  TRP   B CZ3 1 
ATOM   4245 C  CH2 . TRP   B 1 170 ? 20.132 84.627  44.263 1.00 14.60 ? 611  TRP   B CH2 1 
ATOM   4246 N  N   . ASP   B 1 171 ? 22.535 87.631  51.150 1.00 12.91 ? 612  ASP   B N   1 
ATOM   4247 C  CA  . ASP   B 1 171 ? 23.725 88.281  51.677 1.00 11.00 ? 612  ASP   B CA  1 
ATOM   4248 C  C   . ASP   B 1 171 ? 24.176 87.520  52.920 1.00 12.25 ? 612  ASP   B C   1 
ATOM   4249 O  O   . ASP   B 1 171 ? 23.348 86.971  53.647 1.00 12.78 ? 612  ASP   B O   1 
ATOM   4250 C  CB  . ASP   B 1 171 ? 23.332 89.725  52.012 1.00 14.78 ? 612  ASP   B CB  1 
ATOM   4251 C  CG  . ASP   B 1 171 ? 24.503 90.602  52.398 1.00 14.27 ? 612  ASP   B CG  1 
ATOM   4252 O  OD1 . ASP   B 1 171 ? 24.979 90.500  53.549 1.00 14.36 ? 612  ASP   B OD1 1 
ATOM   4253 O  OD2 . ASP   B 1 171 ? 24.918 91.449  51.573 1.00 16.43 ? 612  ASP   B OD2 1 
ATOM   4254 N  N   . VAL   B 1 172 ? 25.493 87.450  53.151 1.00 13.70 ? 613  VAL   B N   1 
ATOM   4255 C  CA  . VAL   B 1 172 ? 26.002 86.681  54.292 1.00 12.51 ? 613  VAL   B CA  1 
ATOM   4256 C  C   . VAL   B 1 172 ? 25.571 87.273  55.631 1.00 12.34 ? 613  VAL   B C   1 
ATOM   4257 O  O   . VAL   B 1 172 ? 25.641 86.586  56.662 1.00 13.94 ? 613  VAL   B O   1 
ATOM   4258 C  CB  . VAL   B 1 172 ? 27.536 86.541  54.212 1.00 13.37 ? 613  VAL   B CB  1 
ATOM   4259 C  CG1 . VAL   B 1 172 ? 28.200 87.822  54.691 1.00 14.97 ? 613  VAL   B CG1 1 
ATOM   4260 C  CG2 . VAL   B 1 172 ? 28.017 85.341  55.025 1.00 14.63 ? 613  VAL   B CG2 1 
ATOM   4261 N  N   . HIS   B 1 173 ? 25.167 88.534  55.651 1.00 15.14 ? 614  HIS   B N   1 
ATOM   4262 C  CA  . HIS   B 1 173 ? 24.762 89.205  56.876 1.00 24.87 ? 614  HIS   B CA  1 
ATOM   4263 C  C   . HIS   B 1 173 ? 23.243 89.199  57.003 1.00 15.57 ? 614  HIS   B C   1 
ATOM   4264 O  O   . HIS   B 1 173 ? 22.515 89.211  56.007 1.00 14.06 ? 614  HIS   B O   1 
ATOM   4265 C  CB  . HIS   B 1 173 ? 25.267 90.648  56.880 1.00 43.37 ? 614  HIS   B CB  1 
ATOM   4266 C  CG  . HIS   B 1 173 ? 26.757 90.764  56.776 1.00 33.36 ? 614  HIS   B CG  1 
ATOM   4267 N  ND1 . HIS   B 1 173 ? 27.401 91.120  55.607 1.00 18.89 ? 614  HIS   B ND1 1 
ATOM   4268 C  CD2 . HIS   B 1 173 ? 27.728 90.563  57.698 1.00 23.86 ? 614  HIS   B CD2 1 
ATOM   4269 C  CE1 . HIS   B 1 173 ? 28.707 91.138  55.821 1.00 18.62 ? 614  HIS   B CE1 1 
ATOM   4270 N  NE2 . HIS   B 1 173 ? 28.931 90.796  57.077 1.00 17.00 ? 614  HIS   B NE2 1 
ATOM   4271 N  N   . HIS   B 1 174 ? 22.771 89.167  58.244 1.00 12.75 ? 615  HIS   B N   1 
ATOM   4272 C  CA  . HIS   B 1 174 ? 21.347 89.319  58.508 1.00 13.20 ? 615  HIS   B CA  1 
ATOM   4273 C  C   . HIS   B 1 174 ? 20.892 90.713  58.110 1.00 12.49 ? 615  HIS   B C   1 
ATOM   4274 O  O   . HIS   B 1 174 ? 21.523 91.710  58.478 1.00 14.23 ? 615  HIS   B O   1 
ATOM   4275 C  CB  . HIS   B 1 174 ? 21.087 89.120  59.999 1.00 14.27 ? 615  HIS   B CB  1 
ATOM   4276 C  CG  . HIS   B 1 174 ? 19.638 89.120  60.357 1.00 13.47 ? 615  HIS   B CG  1 
ATOM   4277 N  ND1 . HIS   B 1 174 ? 19.102 89.991  61.281 1.00 14.97 ? 615  HIS   B ND1 1 
ATOM   4278 C  CD2 . HIS   B 1 174 ? 18.611 88.373  59.897 1.00 13.58 ? 615  HIS   B CD2 1 
ATOM   4279 C  CE1 . HIS   B 1 174 ? 17.804 89.764  61.386 1.00 12.70 ? 615  HIS   B CE1 1 
ATOM   4280 N  NE2 . HIS   B 1 174 ? 17.484 88.781  60.566 1.00 13.56 ? 615  HIS   B NE2 1 
ATOM   4281 N  N   . GLY   B 1 175 ? 19.801 90.782  57.348 1.00 12.19 ? 616  GLY   B N   1 
ATOM   4282 C  CA  . GLY   B 1 175 ? 19.199 92.065  57.045 1.00 12.82 ? 616  GLY   B CA  1 
ATOM   4283 C  C   . GLY   B 1 175 ? 18.339 92.550  58.194 1.00 13.85 ? 616  GLY   B C   1 
ATOM   4284 O  O   . GLY   B 1 175 ? 17.111 92.474  58.132 1.00 16.50 ? 616  GLY   B O   1 
ATOM   4285 N  N   . ASN   B 1 176 ? 18.983 93.063  59.241 1.00 13.68 ? 617  ASN   B N   1 
ATOM   4286 C  CA  . ASN   B 1 176 ? 18.263 93.471  60.447 1.00 13.17 ? 617  ASN   B CA  1 
ATOM   4287 C  C   . ASN   B 1 176 ? 17.204 94.514  60.132 1.00 12.68 ? 617  ASN   B C   1 
ATOM   4288 O  O   . ASN   B 1 176 ? 16.117 94.510  60.722 1.00 14.43 ? 617  ASN   B O   1 
ATOM   4289 C  CB  . ASN   B 1 176 ? 19.265 94.028  61.457 1.00 13.47 ? 617  ASN   B CB  1 
ATOM   4290 C  CG  . ASN   B 1 176 ? 20.105 95.140  60.865 1.00 15.05 ? 617  ASN   B CG  1 
ATOM   4291 O  OD1 . ASN   B 1 176 ? 21.029 94.877  60.106 1.00 16.61 ? 617  ASN   B OD1 1 
ATOM   4292 N  ND2 . ASN   B 1 176 ? 19.773 96.385  61.182 1.00 17.87 ? 617  ASN   B ND2 1 
ATOM   4293 N  N   . GLY   B 1 177 ? 17.501 95.419  59.205 1.00 12.91 ? 618  GLY   B N   1 
ATOM   4294 C  CA  . GLY   B 1 177 ? 16.546 96.463  58.887 1.00 13.47 ? 618  GLY   B CA  1 
ATOM   4295 C  C   . GLY   B 1 177 ? 15.313 95.915  58.204 1.00 14.20 ? 618  GLY   B C   1 
ATOM   4296 O  O   . GLY   B 1 177 ? 14.186 96.318  58.512 1.00 13.80 ? 618  GLY   B O   1 
ATOM   4297 N  N   . THR   B 1 178 ? 15.506 94.972  57.285 1.00 13.08 ? 619  THR   B N   1 
ATOM   4298 C  CA  . THR   B 1 178 ? 14.370 94.372  56.596 1.00 11.29 ? 619  THR   B CA  1 
ATOM   4299 C  C   . THR   B 1 178 ? 13.501 93.579  57.560 1.00 12.50 ? 619  THR   B C   1 
ATOM   4300 O  O   . THR   B 1 178 ? 12.266 93.684  57.523 1.00 13.46 ? 619  THR   B O   1 
ATOM   4301 C  CB  . THR   B 1 178 ? 14.850 93.493  55.438 1.00 11.51 ? 619  THR   B CB  1 
ATOM   4302 O  OG1 . THR   B 1 178 ? 15.826 94.217  54.684 1.00 13.70 ? 619  THR   B OG1 1 
ATOM   4303 C  CG2 . THR   B 1 178 ? 13.719 93.158  54.499 1.00 13.44 ? 619  THR   B CG2 1 
ATOM   4304 N  N   . GLN   B 1 179 ? 14.125 92.781  58.429 1.00 14.42 ? 620  GLN   B N   1 
ATOM   4305 C  CA  . GLN   B 1 179 ? 13.358 92.050  59.433 1.00 13.64 ? 620  GLN   B CA  1 
ATOM   4306 C  C   . GLN   B 1 179 ? 12.512 93.005  60.257 1.00 13.19 ? 620  GLN   B C   1 
ATOM   4307 O  O   . GLN   B 1 179 ? 11.303 92.793  60.439 1.00 14.13 ? 620  GLN   B O   1 
ATOM   4308 C  CB  . GLN   B 1 179 ? 14.297 91.263  60.348 1.00 13.11 ? 620  GLN   B CB  1 
ATOM   4309 C  CG  . GLN   B 1 179 ? 13.594 90.744  61.609 1.00 13.77 ? 620  GLN   B CG  1 
ATOM   4310 C  CD  . GLN   B 1 179 ? 14.419 89.712  62.339 1.00 16.27 ? 620  GLN   B CD  1 
ATOM   4311 O  OE1 . GLN   B 1 179 ? 14.952 88.796  61.720 1.00 15.52 ? 620  GLN   B OE1 1 
ATOM   4312 N  NE2 . GLN   B 1 179 ? 14.521 89.843  63.665 1.00 17.56 ? 620  GLN   B NE2 1 
ATOM   4313 N  N   . HIS   B 1 180 ? 13.133 94.071  60.763 1.00 13.21 ? 621  HIS   B N   1 
ATOM   4314 C  CA  . HIS   B 1 180 ? 12.428 94.957  61.686 1.00 13.47 ? 621  HIS   B CA  1 
ATOM   4315 C  C   . HIS   B 1 180 ? 11.306 95.718  60.987 1.00 13.81 ? 621  HIS   B C   1 
ATOM   4316 O  O   . HIS   B 1 180 ? 10.208 95.863  61.542 1.00 14.74 ? 621  HIS   B O   1 
ATOM   4317 C  CB  . HIS   B 1 180 ? 13.423 95.910  62.339 1.00 14.60 ? 621  HIS   B CB  1 
ATOM   4318 C  CG  . HIS   B 1 180 ? 14.347 95.237  63.307 1.00 16.61 ? 621  HIS   B CG  1 
ATOM   4319 N  ND1 . HIS   B 1 180 ? 15.651 95.641  63.495 1.00 16.33 ? 621  HIS   B ND1 1 
ATOM   4320 C  CD2 . HIS   B 1 180 ? 14.155 94.184  64.137 1.00 19.80 ? 621  HIS   B CD2 1 
ATOM   4321 C  CE1 . HIS   B 1 180 ? 16.223 94.865  64.402 1.00 19.12 ? 621  HIS   B CE1 1 
ATOM   4322 N  NE2 . HIS   B 1 180 ? 15.337 93.972  64.806 1.00 20.81 ? 621  HIS   B NE2 1 
ATOM   4323 N  N   . ILE   B 1 181 ? 11.545 96.179  59.756 1.00 13.67 ? 622  ILE   B N   1 
ATOM   4324 C  CA  . ILE   B 1 181 ? 10.526 96.912  59.011 1.00 13.17 ? 622  ILE   B CA  1 
ATOM   4325 C  C   . ILE   B 1 181 ? 9.283  96.058  58.830 1.00 13.50 ? 622  ILE   B C   1 
ATOM   4326 O  O   . ILE   B 1 181 ? 8.151  96.545  58.964 1.00 14.97 ? 622  ILE   B O   1 
ATOM   4327 C  CB  . ILE   B 1 181 ? 11.100 97.406  57.668 1.00 13.63 ? 622  ILE   B CB  1 
ATOM   4328 C  CG1 . ILE   B 1 181 ? 12.034 98.591  57.912 1.00 14.33 ? 622  ILE   B CG1 1 
ATOM   4329 C  CG2 . ILE   B 1 181 ? 9.995  97.812  56.705 1.00 14.10 ? 622  ILE   B CG2 1 
ATOM   4330 C  CD1 . ILE   B 1 181 ? 12.869 98.989  56.692 1.00 13.96 ? 622  ILE   B CD1 1 
ATOM   4331 N  N   . PHE   B 1 182 ? 9.458  94.763  58.580 1.00 13.43 ? 623  PHE   B N   1 
ATOM   4332 C  CA  . PHE   B 1 182 ? 8.324  93.898  58.278 1.00 13.94 ? 623  PHE   B CA  1 
ATOM   4333 C  C   . PHE   B 1 182 ? 7.956  92.950  59.415 1.00 12.77 ? 623  PHE   B C   1 
ATOM   4334 O  O   . PHE   B 1 182 ? 7.151  92.039  59.204 1.00 13.22 ? 623  PHE   B O   1 
ATOM   4335 C  CB  . PHE   B 1 182 ? 8.578  93.121  56.984 1.00 13.37 ? 623  PHE   B CB  1 
ATOM   4336 C  CG  . PHE   B 1 182 ? 8.758  93.998  55.781 1.00 13.00 ? 623  PHE   B CG  1 
ATOM   4337 C  CD1 . PHE   B 1 182 ? 7.708  94.767  55.307 1.00 13.70 ? 623  PHE   B CD1 1 
ATOM   4338 C  CD2 . PHE   B 1 182 ? 9.969  94.050  55.129 1.00 12.34 ? 623  PHE   B CD2 1 
ATOM   4339 C  CE1 . PHE   B 1 182 ? 7.861  95.577  54.190 1.00 13.51 ? 623  PHE   B CE1 1 
ATOM   4340 C  CE2 . PHE   B 1 182 ? 10.139 94.849  54.015 1.00 13.74 ? 623  PHE   B CE2 1 
ATOM   4341 C  CZ  . PHE   B 1 182 ? 9.089  95.611  53.535 1.00 12.43 ? 623  PHE   B CZ  1 
ATOM   4342 N  N   . GLU   B 1 183 ? 8.512  93.143  60.615 1.00 13.57 ? 624  GLU   B N   1 
ATOM   4343 C  CA  . GLU   B 1 183 ? 8.369  92.122  61.648 1.00 14.80 ? 624  GLU   B CA  1 
ATOM   4344 C  C   . GLU   B 1 183 ? 6.917  91.881  62.034 1.00 14.19 ? 624  GLU   B C   1 
ATOM   4345 O  O   . GLU   B 1 183 ? 6.561  90.753  62.384 1.00 15.34 ? 624  GLU   B O   1 
ATOM   4346 C  CB  . GLU   B 1 183 ? 9.188  92.492  62.875 1.00 17.98 ? 624  GLU   B CB  1 
ATOM   4347 C  CG  . GLU   B 1 183 ? 9.566  91.288  63.698 1.00 22.52 ? 624  GLU   B CG  1 
ATOM   4348 C  CD  . GLU   B 1 183 ? 10.719 91.574  64.632 1.00 24.96 ? 624  GLU   B CD  1 
ATOM   4349 O  OE1 . GLU   B 1 183 ? 11.033 92.767  64.831 1.00 25.85 ? 624  GLU   B OE1 1 
ATOM   4350 O  OE2 . GLU   B 1 183 ? 11.286 90.606  65.186 1.00 27.54 ? 624  GLU   B OE2 1 
ATOM   4351 N  N   . GLU   B 1 184 ? 6.065  92.903  61.933 1.00 14.38 ? 625  GLU   B N   1 
ATOM   4352 C  CA  . GLU   B 1 184 ? 4.646  92.786  62.262 1.00 16.37 ? 625  GLU   B CA  1 
ATOM   4353 C  C   . GLU   B 1 184 ? 3.764  92.735  61.025 1.00 17.17 ? 625  GLU   B C   1 
ATOM   4354 O  O   . GLU   B 1 184 ? 2.582  93.090  61.093 1.00 19.80 ? 625  GLU   B O   1 
ATOM   4355 C  CB  . GLU   B 1 184 ? 4.202  93.930  63.172 1.00 21.39 ? 625  GLU   B CB  1 
ATOM   4356 C  CG  . GLU   B 1 184 ? 4.875  93.945  64.534 1.00 27.32 ? 625  GLU   B CG  1 
ATOM   4357 C  CD  . GLU   B 1 184 ? 4.610  95.225  65.306 1.00 39.94 ? 625  GLU   B CD  1 
ATOM   4358 O  OE1 . GLU   B 1 184 ? 4.743  96.319  64.721 1.00 49.95 ? 625  GLU   B OE1 1 
ATOM   4359 O  OE2 . GLU   B 1 184 ? 4.267  95.136  66.501 1.00 38.42 ? 625  GLU   B OE2 1 
ATOM   4360 N  N   . ASP   B 1 185 ? 4.310  92.292  59.898 1.00 16.15 ? 626  ASP   B N   1 
ATOM   4361 C  CA  . ASP   B 1 185 ? 3.626  92.360  58.614 1.00 18.71 ? 626  ASP   B CA  1 
ATOM   4362 C  C   . ASP   B 1 185 ? 3.501  90.964  58.019 1.00 19.53 ? 626  ASP   B C   1 
ATOM   4363 O  O   . ASP   B 1 185 ? 4.500  90.255  57.869 1.00 21.84 ? 626  ASP   B O   1 
ATOM   4364 C  CB  . ASP   B 1 185 ? 4.394  93.278  57.660 1.00 20.65 ? 626  ASP   B CB  1 
ATOM   4365 C  CG  . ASP   B 1 185 ? 3.566  93.717  56.471 1.00 23.85 ? 626  ASP   B CG  1 
ATOM   4366 O  OD1 . ASP   B 1 185 ? 2.565  93.049  56.148 0.81 24.58 ? 626  ASP   B OD1 1 
ATOM   4367 O  OD2 . ASP   B 1 185 ? 3.937  94.734  55.863 0.71 23.94 ? 626  ASP   B OD2 1 
ATOM   4368 N  N   . ASP   B 1 186 ? 2.276  90.583  57.659 1.00 19.96 ? 627  ASP   B N   1 
ATOM   4369 C  CA  . ASP   B 1 186 ? 2.018  89.293  57.033 1.00 20.43 ? 627  ASP   B CA  1 
ATOM   4370 C  C   . ASP   B 1 186 ? 1.989  89.369  55.512 1.00 19.48 ? 627  ASP   B C   1 
ATOM   4371 O  O   . ASP   B 1 186 ? 1.871  88.327  54.855 1.00 20.86 ? 627  ASP   B O   1 
ATOM   4372 C  CB  . ASP   B 1 186 ? 0.699  88.698  57.553 1.00 25.49 ? 627  ASP   B CB  1 
ATOM   4373 C  CG  . ASP   B 1 186 ? -0.501 89.565  57.231 1.00 41.50 ? 627  ASP   B CG  1 
ATOM   4374 O  OD1 . ASP   B 1 186 ? -0.317 90.766  56.951 1.00 32.96 ? 627  ASP   B OD1 1 
ATOM   4375 O  OD2 . ASP   B 1 186 ? -1.637 89.048  57.274 1.00 49.93 ? 627  ASP   B OD2 1 
ATOM   4376 N  N   . SER   B 1 187 ? 2.088  90.568  54.943 1.00 16.85 ? 628  SER   B N   1 
ATOM   4377 C  CA  . SER   B 1 187 ? 2.079  90.726  53.495 1.00 17.22 ? 628  SER   B CA  1 
ATOM   4378 C  C   . SER   B 1 187 ? 3.464  90.604  52.880 1.00 16.60 ? 628  SER   B C   1 
ATOM   4379 O  O   . SER   B 1 187 ? 3.573  90.424  51.659 1.00 14.77 ? 628  SER   B O   1 
ATOM   4380 C  CB  . SER   B 1 187 ? 1.454  92.066  53.094 1.00 17.12 ? 628  SER   B CB  1 
ATOM   4381 O  OG  . SER   B 1 187 ? 2.283  93.165  53.447 1.00 18.39 ? 628  SER   B OG  1 
ATOM   4382 N  N   . VAL   B 1 188 ? 4.518  90.701  53.684 1.00 14.73 ? 629  VAL   B N   1 
ATOM   4383 C  CA  . VAL   B 1 188 ? 5.896  90.590  53.212 1.00 14.37 ? 629  VAL   B CA  1 
ATOM   4384 C  C   . VAL   B 1 188 ? 6.561  89.488  54.019 1.00 21.27 ? 629  VAL   B C   1 
ATOM   4385 O  O   . VAL   B 1 188 ? 6.809  89.650  55.218 1.00 27.42 ? 629  VAL   B O   1 
ATOM   4386 C  CB  . VAL   B 1 188 ? 6.656  91.912  53.348 1.00 13.83 ? 629  VAL   B CB  1 
ATOM   4387 C  CG1 . VAL   B 1 188 ? 8.078  91.743  52.814 1.00 14.51 ? 629  VAL   B CG1 1 
ATOM   4388 C  CG2 . VAL   B 1 188 ? 5.938  93.018  52.596 1.00 12.82 ? 629  VAL   B CG2 1 
ATOM   4389 N  N   . LEU   B 1 189 ? 6.840  88.365  53.370 1.00 15.11 ? 630  LEU   B N   1 
ATOM   4390 C  CA  . LEU   B 1 189 ? 7.555  87.261  53.989 1.00 13.52 ? 630  LEU   B CA  1 
ATOM   4391 C  C   . LEU   B 1 189 ? 9.048  87.504  53.813 1.00 13.96 ? 630  LEU   B C   1 
ATOM   4392 O  O   . LEU   B 1 189 ? 9.526  87.664  52.681 1.00 13.64 ? 630  LEU   B O   1 
ATOM   4393 C  CB  . LEU   B 1 189 ? 7.160  85.963  53.293 1.00 15.85 ? 630  LEU   B CB  1 
ATOM   4394 C  CG  . LEU   B 1 189 ? 7.982  84.714  53.610 1.00 15.84 ? 630  LEU   B CG  1 
ATOM   4395 C  CD1 . LEU   B 1 189 ? 7.904  84.390  55.102 1.00 16.65 ? 630  LEU   B CD1 1 
ATOM   4396 C  CD2 . LEU   B 1 189 ? 7.478  83.547  52.771 1.00 16.63 ? 630  LEU   B CD2 1 
ATOM   4397 N  N   . TYR   B 1 190 ? 9.779  87.538  54.924 1.00 13.47 ? 631  TYR   B N   1 
ATOM   4398 C  CA  . TYR   B 1 190 ? 11.218 87.776  54.917 1.00 14.11 ? 631  TYR   B CA  1 
ATOM   4399 C  C   . TYR   B 1 190 ? 11.922 86.478  55.277 1.00 14.65 ? 631  TYR   B C   1 
ATOM   4400 O  O   . TYR   B 1 190 ? 11.680 85.915  56.349 1.00 15.33 ? 631  TYR   B O   1 
ATOM   4401 C  CB  . TYR   B 1 190 ? 11.610 88.873  55.909 1.00 13.31 ? 631  TYR   B CB  1 
ATOM   4402 C  CG  . TYR   B 1 190 ? 13.097 89.149  55.936 1.00 12.64 ? 631  TYR   B CG  1 
ATOM   4403 C  CD1 . TYR   B 1 190 ? 13.758 89.618  54.811 1.00 13.05 ? 631  TYR   B CD1 1 
ATOM   4404 C  CD2 . TYR   B 1 190 ? 13.840 88.920  57.085 1.00 13.67 ? 631  TYR   B CD2 1 
ATOM   4405 C  CE1 . TYR   B 1 190 ? 15.131 89.855  54.833 1.00 12.59 ? 631  TYR   B CE1 1 
ATOM   4406 C  CE2 . TYR   B 1 190 ? 15.214 89.152  57.118 1.00 13.03 ? 631  TYR   B CE2 1 
ATOM   4407 C  CZ  . TYR   B 1 190 ? 15.848 89.619  55.980 1.00 13.33 ? 631  TYR   B CZ  1 
ATOM   4408 O  OH  . TYR   B 1 190 ? 17.200 89.847  56.025 1.00 14.73 ? 631  TYR   B OH  1 
ATOM   4409 N  N   . ILE   B 1 191 ? 12.774 85.997  54.375 1.00 13.60 ? 632  ILE   B N   1 
ATOM   4410 C  CA  . ILE   B 1 191 ? 13.605 84.816  54.605 1.00 12.40 ? 632  ILE   B CA  1 
ATOM   4411 C  C   . ILE   B 1 191 ? 15.056 85.232  54.426 1.00 13.08 ? 632  ILE   B C   1 
ATOM   4412 O  O   . ILE   B 1 191 ? 15.453 85.640  53.326 1.00 15.20 ? 632  ILE   B O   1 
ATOM   4413 C  CB  . ILE   B 1 191 ? 13.250 83.667  53.646 1.00 14.29 ? 632  ILE   B CB  1 
ATOM   4414 C  CG1 . ILE   B 1 191 ? 11.752 83.341  53.719 1.00 13.87 ? 632  ILE   B CG1 1 
ATOM   4415 C  CG2 . ILE   B 1 191 ? 14.102 82.437  53.976 1.00 14.39 ? 632  ILE   B CG2 1 
ATOM   4416 C  CD1 . ILE   B 1 191 ? 11.341 82.122  52.906 1.00 16.04 ? 632  ILE   B CD1 1 
ATOM   4417 N  N   . SER   B 1 192 ? 15.836 85.134  55.497 1.00 13.17 ? 633  SER   B N   1 
ATOM   4418 C  CA  . SER   B 1 192 ? 17.262 85.423  55.470 1.00 12.32 ? 633  SER   B CA  1 
ATOM   4419 C  C   . SER   B 1 192 ? 18.067 84.173  55.775 1.00 13.27 ? 633  SER   B C   1 
ATOM   4420 O  O   . SER   B 1 192 ? 17.749 83.432  56.710 1.00 14.24 ? 633  SER   B O   1 
ATOM   4421 C  CB  . SER   B 1 192 ? 17.626 86.484  56.507 1.00 13.29 ? 633  SER   B CB  1 
ATOM   4422 O  OG  . SER   B 1 192 ? 18.996 86.859  56.423 1.00 14.15 ? 633  SER   B OG  1 
ATOM   4423 N  N   . LEU   B 1 193 ? 19.140 83.973  55.018 1.00 13.24 ? 634  LEU   B N   1 
ATOM   4424 C  CA  . LEU   B 1 193 ? 20.211 83.054  55.372 1.00 13.63 ? 634  LEU   B CA  1 
ATOM   4425 C  C   . LEU   B 1 193 ? 21.427 83.899  55.710 1.00 13.29 ? 634  LEU   B C   1 
ATOM   4426 O  O   . LEU   B 1 193 ? 21.714 84.877  55.010 1.00 14.69 ? 634  LEU   B O   1 
ATOM   4427 C  CB  . LEU   B 1 193 ? 20.551 82.108  54.207 1.00 14.54 ? 634  LEU   B CB  1 
ATOM   4428 C  CG  . LEU   B 1 193 ? 19.328 81.459  53.543 1.00 15.05 ? 634  LEU   B CG  1 
ATOM   4429 C  CD1 . LEU   B 1 193 ? 18.850 82.254  52.342 1.00 16.46 ? 634  LEU   B CD1 1 
ATOM   4430 C  CD2 . LEU   B 1 193 ? 19.614 80.014  53.147 1.00 16.19 ? 634  LEU   B CD2 1 
ATOM   4431 N  N   . HIS   B 1 194 ? 22.134 83.550  56.784 1.00 13.52 ? 635  HIS   B N   1 
ATOM   4432 C  CA  . HIS   B 1 194 ? 23.209 84.437  57.202 1.00 13.10 ? 635  HIS   B CA  1 
ATOM   4433 C  C   . HIS   B 1 194 ? 24.145 83.743  58.175 1.00 13.16 ? 635  HIS   B C   1 
ATOM   4434 O  O   . HIS   B 1 194 ? 23.736 82.887  58.968 1.00 15.56 ? 635  HIS   B O   1 
ATOM   4435 C  CB  . HIS   B 1 194 ? 22.647 85.712  57.841 1.00 13.35 ? 635  HIS   B CB  1 
ATOM   4436 C  CG  . HIS   B 1 194 ? 21.538 85.442  58.805 1.00 12.84 ? 635  HIS   B CG  1 
ATOM   4437 N  ND1 . HIS   B 1 194 ? 20.216 85.392  58.415 1.00 13.65 ? 635  HIS   B ND1 1 
ATOM   4438 C  CD2 . HIS   B 1 194 ? 21.551 85.179  60.135 1.00 14.24 ? 635  HIS   B CD2 1 
ATOM   4439 C  CE1 . HIS   B 1 194 ? 19.461 85.116  59.465 1.00 14.50 ? 635  HIS   B CE1 1 
ATOM   4440 N  NE2 . HIS   B 1 194 ? 20.245 84.980  60.519 1.00 14.32 ? 635  HIS   B NE2 1 
ATOM   4441 N  N   . ARG   B 1 195 ? 25.414 84.133  58.099 1.00 14.49 ? 636  ARG   B N   1 
ATOM   4442 C  CA  . ARG   B 1 195 ? 26.367 83.753  59.126 1.00 14.37 ? 636  ARG   B CA  1 
ATOM   4443 C  C   . ARG   B 1 195 ? 25.986 84.435  60.431 1.00 14.59 ? 636  ARG   B C   1 
ATOM   4444 O  O   . ARG   B 1 195 ? 25.765 85.653  60.478 1.00 15.04 ? 636  ARG   B O   1 
ATOM   4445 C  CB  . ARG   B 1 195 ? 27.774 84.156  58.708 1.00 14.03 ? 636  ARG   B CB  1 
ATOM   4446 C  CG  . ARG   B 1 195 ? 28.823 83.579  59.633 1.00 14.22 ? 636  ARG   B CG  1 
ATOM   4447 C  CD  . ARG   B 1 195 ? 30.211 83.732  59.049 1.00 14.90 ? 636  ARG   B CD  1 
ATOM   4448 N  NE  . ARG   B 1 195 ? 31.216 83.182  59.957 1.00 17.24 ? 636  ARG   B NE  1 
ATOM   4449 C  CZ  . ARG   B 1 195 ? 32.527 83.324  59.804 1.00 18.88 ? 636  ARG   B CZ  1 
ATOM   4450 N  NH1 . ARG   B 1 195 ? 33.022 83.993  58.772 1.00 19.86 ? 636  ARG   B NH1 1 
ATOM   4451 N  NH2 . ARG   B 1 195 ? 33.352 82.785  60.696 1.00 20.10 ? 636  ARG   B NH2 1 
ATOM   4452 N  N   . TYR   B 1 196 ? 25.912 83.647  61.492 1.00 13.15 ? 637  TYR   B N   1 
ATOM   4453 C  CA  . TYR   B 1 196 ? 25.383 84.110  62.768 1.00 14.09 ? 637  TYR   B CA  1 
ATOM   4454 C  C   . TYR   B 1 196 ? 26.381 83.936  63.901 1.00 15.84 ? 637  TYR   B C   1 
ATOM   4455 O  O   . TYR   B 1 196 ? 26.636 84.888  64.651 1.00 16.57 ? 637  TYR   B O   1 
ATOM   4456 C  CB  . TYR   B 1 196 ? 24.075 83.358  63.070 1.00 16.68 ? 637  TYR   B CB  1 
ATOM   4457 C  CG  . TYR   B 1 196 ? 23.412 83.711  64.386 1.00 18.30 ? 637  TYR   B CG  1 
ATOM   4458 C  CD1 . TYR   B 1 196 ? 23.025 85.012  64.672 1.00 19.33 ? 637  TYR   B CD1 1 
ATOM   4459 C  CD2 . TYR   B 1 196 ? 23.164 82.728  65.335 1.00 18.08 ? 637  TYR   B CD2 1 
ATOM   4460 C  CE1 . TYR   B 1 196 ? 22.414 85.327  65.886 1.00 22.84 ? 637  TYR   B CE1 1 
ATOM   4461 C  CE2 . TYR   B 1 196 ? 22.563 83.035  66.551 1.00 19.07 ? 637  TYR   B CE2 1 
ATOM   4462 C  CZ  . TYR   B 1 196 ? 22.192 84.333  66.818 1.00 20.88 ? 637  TYR   B CZ  1 
ATOM   4463 O  OH  . TYR   B 1 196 ? 21.592 84.640  68.024 1.00 19.04 ? 637  TYR   B OH  1 
ATOM   4464 N  N   . GLU   B 1 197 ? 26.971 82.746  64.032 1.00 19.23 ? 638  GLU   B N   1 
ATOM   4465 C  CA  . GLU   B 1 197 ? 27.984 82.462  65.055 1.00 19.12 ? 638  GLU   B CA  1 
ATOM   4466 C  C   . GLU   B 1 197 ? 27.489 82.809  66.459 1.00 20.23 ? 638  GLU   B C   1 
ATOM   4467 O  O   . GLU   B 1 197 ? 28.164 83.491  67.231 1.00 19.04 ? 638  GLU   B O   1 
ATOM   4468 C  CB  . GLU   B 1 197 ? 29.324 83.138  64.744 1.00 19.45 ? 638  GLU   B CB  1 
ATOM   4469 C  CG  . GLU   B 1 197 ? 29.844 82.924  63.320 1.00 22.77 ? 638  GLU   B CG  1 
ATOM   4470 C  CD  . GLU   B 1 197 ? 30.194 81.476  63.006 1.00 27.98 ? 638  GLU   B CD  1 
ATOM   4471 O  OE1 . GLU   B 1 197 ? 30.119 80.608  63.902 1.00 25.97 ? 638  GLU   B OE1 1 
ATOM   4472 O  OE2 . GLU   B 1 197 ? 30.563 81.201  61.847 1.00 25.76 ? 638  GLU   B OE2 1 
ATOM   4473 N  N   . ASP   B 1 198 ? 26.283 82.342  66.779 1.00 21.74 ? 639  ASP   B N   1 
ATOM   4474 C  CA  . ASP   B 1 198 ? 25.684 82.537  68.102 1.00 27.19 ? 639  ASP   B CA  1 
ATOM   4475 C  C   . ASP   B 1 198 ? 25.550 84.016  68.461 1.00 31.73 ? 639  ASP   B C   1 
ATOM   4476 O  O   . ASP   B 1 198 ? 25.604 84.391  69.636 1.00 27.94 ? 639  ASP   B O   1 
ATOM   4477 C  CB  . ASP   B 1 198 ? 26.436 81.760  69.186 1.00 34.30 ? 639  ASP   B CB  1 
ATOM   4478 C  CG  . ASP   B 1 198 ? 26.334 80.261  68.994 1.00 43.88 ? 639  ASP   B CG  1 
ATOM   4479 O  OD1 . ASP   B 1 198 ? 25.286 79.793  68.501 1.00 52.87 ? 639  ASP   B OD1 1 
ATOM   4480 O  OD2 . ASP   B 1 198 ? 27.310 79.553  69.315 1.00 43.95 ? 639  ASP   B OD2 1 
ATOM   4481 N  N   . GLY   B 1 199 ? 25.374 84.862  67.446 1.00 26.62 ? 640  GLY   B N   1 
ATOM   4482 C  CA  . GLY   B 1 199 ? 25.233 86.286  67.638 1.00 19.84 ? 640  GLY   B CA  1 
ATOM   4483 C  C   . GLY   B 1 199 ? 26.521 87.080  67.611 1.00 21.63 ? 640  GLY   B C   1 
ATOM   4484 O  O   . GLY   B 1 199 ? 26.477 88.296  67.831 1.00 23.61 ? 640  GLY   B O   1 
ATOM   4485 N  N   . ALA   B 1 200 ? 27.659 86.445  67.336 1.00 24.70 ? 641  ALA   B N   1 
ATOM   4486 C  CA  . ALA   B 1 200 ? 28.941 87.134  67.321 1.00 27.51 ? 641  ALA   B CA  1 
ATOM   4487 C  C   . ALA   B 1 200 ? 29.281 87.759  65.972 1.00 29.24 ? 641  ALA   B C   1 
ATOM   4488 O  O   . ALA   B 1 200 ? 30.183 88.600  65.910 1.00 34.13 ? 641  ALA   B O   1 
ATOM   4489 C  CB  . ALA   B 1 200 ? 30.068 86.187  67.754 1.00 25.02 ? 641  ALA   B CB  1 
ATOM   4490 N  N   . PHE   B 1 201 ? 28.595 87.378  64.898 1.00 23.43 ? 642  PHE   B N   1 
ATOM   4491 C  CA  . PHE   B 1 201 ? 28.889 87.921  63.576 1.00 20.21 ? 642  PHE   B CA  1 
ATOM   4492 C  C   . PHE   B 1 201 ? 28.040 89.160  63.316 1.00 17.45 ? 642  PHE   B C   1 
ATOM   4493 O  O   . PHE   B 1 201 ? 26.879 89.221  63.733 1.00 18.14 ? 642  PHE   B O   1 
ATOM   4494 C  CB  . PHE   B 1 201 ? 28.606 86.862  62.510 1.00 19.30 ? 642  PHE   B CB  1 
ATOM   4495 C  CG  . PHE   B 1 201 ? 29.346 87.087  61.224 1.00 20.28 ? 642  PHE   B CG  1 
ATOM   4496 C  CD1 . PHE   B 1 201 ? 30.722 86.912  61.158 1.00 19.36 ? 642  PHE   B CD1 1 
ATOM   4497 C  CD2 . PHE   B 1 201 ? 28.668 87.476  60.081 1.00 18.81 ? 642  PHE   B CD2 1 
ATOM   4498 C  CE1 . PHE   B 1 201 ? 31.407 87.122  59.971 1.00 19.92 ? 642  PHE   B CE1 1 
ATOM   4499 C  CE2 . PHE   B 1 201 ? 29.349 87.688  58.894 1.00 20.06 ? 642  PHE   B CE2 1 
ATOM   4500 C  CZ  . PHE   B 1 201 ? 30.720 87.508  58.842 1.00 21.08 ? 642  PHE   B CZ  1 
ATOM   4501 N  N   . PHE   B 1 202 ? 28.627 90.146  62.631 1.00 17.02 ? 643  PHE   B N   1 
ATOM   4502 C  CA  . PHE   B 1 202 ? 27.903 91.371  62.300 1.00 16.44 ? 643  PHE   B CA  1 
ATOM   4503 C  C   . PHE   B 1 202 ? 26.557 91.030  61.658 1.00 15.37 ? 643  PHE   B C   1 
ATOM   4504 O  O   . PHE   B 1 202 ? 26.496 90.169  60.775 1.00 13.91 ? 643  PHE   B O   1 
ATOM   4505 C  CB  . PHE   B 1 202 ? 28.719 92.229  61.324 1.00 16.49 ? 643  PHE   B CB  1 
ATOM   4506 C  CG  . PHE   B 1 202 ? 28.118 93.585  61.074 1.00 17.12 ? 643  PHE   B CG  1 
ATOM   4507 C  CD1 . PHE   B 1 202 ? 27.178 93.772  60.067 1.00 16.98 ? 643  PHE   B CD1 1 
ATOM   4508 C  CD2 . PHE   B 1 202 ? 28.481 94.672  61.850 1.00 18.53 ? 643  PHE   B CD2 1 
ATOM   4509 C  CE1 . PHE   B 1 202 ? 26.606 95.018  59.853 1.00 16.51 ? 643  PHE   B CE1 1 
ATOM   4510 C  CE2 . PHE   B 1 202 ? 27.928 95.917  61.629 1.00 18.20 ? 643  PHE   B CE2 1 
ATOM   4511 C  CZ  . PHE   B 1 202 ? 26.988 96.089  60.634 1.00 17.34 ? 643  PHE   B CZ  1 
ATOM   4512 N  N   . PRO   B 1 203 ? 25.457 91.708  62.044 1.00 14.74 ? 644  PRO   B N   1 
ATOM   4513 C  CA  . PRO   B 1 203 ? 25.386 92.887  62.915 1.00 17.78 ? 644  PRO   B CA  1 
ATOM   4514 C  C   . PRO   B 1 203 ? 25.311 92.637  64.438 1.00 17.77 ? 644  PRO   B C   1 
ATOM   4515 O  O   . PRO   B 1 203 ? 24.900 93.548  65.162 1.00 19.00 ? 644  PRO   B O   1 
ATOM   4516 C  CB  . PRO   B 1 203 ? 24.140 93.633  62.402 1.00 17.51 ? 644  PRO   B CB  1 
ATOM   4517 C  CG  . PRO   B 1 203 ? 23.277 92.572  61.835 1.00 17.19 ? 644  PRO   B CG  1 
ATOM   4518 C  CD  . PRO   B 1 203 ? 24.179 91.463  61.342 1.00 13.89 ? 644  PRO   B CD  1 
ATOM   4519 N  N   . ASN   B 1 204 ? 25.694 91.442  64.901 1.00 16.41 ? 645  ASN   B N   1 
ATOM   4520 C  CA  . ASN   B 1 204 ? 25.984 91.193  66.324 1.00 18.41 ? 645  ASN   B CA  1 
ATOM   4521 C  C   . ASN   B 1 204 ? 24.733 91.236  67.201 1.00 20.66 ? 645  ASN   B C   1 
ATOM   4522 O  O   . ASN   B 1 204 ? 24.790 91.684  68.350 1.00 20.02 ? 645  ASN   B O   1 
ATOM   4523 C  CB  . ASN   B 1 204 ? 27.056 92.146  66.863 1.00 21.92 ? 645  ASN   B CB  1 
ATOM   4524 C  CG  . ASN   B 1 204 ? 28.308 92.151  66.018 1.00 27.15 ? 645  ASN   B CG  1 
ATOM   4525 O  OD1 . ASN   B 1 204 ? 29.104 91.213  66.060 1.00 31.49 ? 645  ASN   B OD1 1 
ATOM   4526 N  ND2 . ASN   B 1 204 ? 28.483 93.203  65.231 1.00 27.29 ? 645  ASN   B ND2 1 
ATOM   4527 N  N   . SER   B 1 205 ? 23.607 90.753  66.684 1.00 18.57 ? 646  SER   B N   1 
ATOM   4528 C  CA  . SER   B 1 205 ? 22.360 90.751  67.438 1.00 17.85 ? 646  SER   B CA  1 
ATOM   4529 C  C   . SER   B 1 205 ? 21.692 89.384  67.401 1.00 16.95 ? 646  SER   B C   1 
ATOM   4530 O  O   . SER   B 1 205 ? 21.632 88.732  66.352 1.00 16.70 ? 646  SER   B O   1 
ATOM   4531 C  CB  . SER   B 1 205 ? 21.378 91.798  66.907 1.00 16.34 ? 646  SER   B CB  1 
ATOM   4532 O  OG  . SER   B 1 205 ? 20.114 91.660  67.540 1.00 17.62 ? 646  SER   B OG  1 
ATOM   4533 N  N   . GLU   B 1 206 ? 21.151 88.966  68.548 1.00 15.94 ? 647  GLU   B N   1 
ATOM   4534 C  CA  . GLU   B 1 206 ? 20.370 87.740  68.588 1.00 14.67 ? 647  GLU   B CA  1 
ATOM   4535 C  C   . GLU   B 1 206 ? 19.042 87.860  67.842 1.00 13.69 ? 647  GLU   B C   1 
ATOM   4536 O  O   . GLU   B 1 206 ? 18.318 86.862  67.715 1.00 17.71 ? 647  GLU   B O   1 
ATOM   4537 C  CB  . GLU   B 1 206 ? 20.182 87.290  70.041 1.00 15.84 ? 647  GLU   B CB  1 
ATOM   4538 C  CG  . GLU   B 1 206 ? 21.514 86.988  70.702 1.00 21.24 ? 647  GLU   B CG  1 
ATOM   4539 C  CD  . GLU   B 1 206 ? 21.378 86.285  72.037 1.00 27.26 ? 647  GLU   B CD  1 
ATOM   4540 O  OE1 . GLU   B 1 206 ? 20.315 85.684  72.291 1.00 31.73 ? 647  GLU   B OE1 1 
ATOM   4541 O  OE2 . GLU   B 1 206 ? 22.352 86.325  72.817 1.00 28.66 ? 647  GLU   B OE2 1 
ATOM   4542 N  N   . ASP   B 1 207 ? 18.704 89.053  67.330 1.00 14.80 ? 648  ASP   B N   1 
ATOM   4543 C  CA  . ASP   B 1 207 ? 17.536 89.198  66.465 1.00 16.17 ? 648  ASP   B CA  1 
ATOM   4544 C  C   . ASP   B 1 207 ? 17.625 88.312  65.232 1.00 14.01 ? 648  ASP   B C   1 
ATOM   4545 O  O   . ASP   B 1 207 ? 16.593 88.004  64.634 1.00 15.47 ? 648  ASP   B O   1 
ATOM   4546 C  CB  . ASP   B 1 207 ? 17.417 90.636  65.962 1.00 21.24 ? 648  ASP   B CB  1 
ATOM   4547 C  CG  . ASP   B 1 207 ? 17.101 91.621  67.056 1.00 27.60 ? 648  ASP   B CG  1 
ATOM   4548 O  OD1 . ASP   B 1 207 ? 16.890 91.194  68.212 1.00 25.91 ? 648  ASP   B OD1 1 
ATOM   4549 O  OD2 . ASP   B 1 207 ? 17.071 92.831  66.745 1.00 27.66 ? 648  ASP   B OD2 1 
ATOM   4550 N  N   . ALA   B 1 208 ? 18.836 87.893  64.852 1.00 15.19 ? 649  ALA   B N   1 
ATOM   4551 C  CA  . ALA   B 1 208 ? 19.059 87.064  63.671 1.00 14.55 ? 649  ALA   B CA  1 
ATOM   4552 C  C   . ALA   B 1 208 ? 18.858 85.575  63.941 1.00 16.41 ? 649  ALA   B C   1 
ATOM   4553 O  O   . ALA   B 1 208 ? 19.025 84.768  63.019 1.00 13.88 ? 649  ALA   B O   1 
ATOM   4554 C  CB  . ALA   B 1 208 ? 20.472 87.316  63.129 1.00 13.17 ? 649  ALA   B CB  1 
ATOM   4555 N  N   . ASN   B 1 209 ? 18.491 85.182  65.163 1.00 17.39 ? 650  ASN   B N   1 
ATOM   4556 C  CA  . ASN   B 1 209 ? 18.376 83.761  65.462 1.00 15.53 ? 650  ASN   B CA  1 
ATOM   4557 C  C   . ASN   B 1 209 ? 17.070 83.181  64.913 1.00 15.90 ? 650  ASN   B C   1 
ATOM   4558 O  O   . ASN   B 1 209 ? 16.125 83.898  64.568 1.00 14.54 ? 650  ASN   B O   1 
ATOM   4559 C  CB  . ASN   B 1 209 ? 18.502 83.504  66.973 1.00 17.38 ? 650  ASN   B CB  1 
ATOM   4560 C  CG  . ASN   B 1 209 ? 19.140 82.166  67.275 1.00 21.40 ? 650  ASN   B CG  1 
ATOM   4561 O  OD1 . ASN   B 1 209 ? 19.450 81.391  66.367 1.00 21.10 ? 650  ASN   B OD1 1 
ATOM   4562 N  ND2 . ASN   B 1 209 ? 19.345 81.885  68.560 1.00 24.28 ? 650  ASN   B ND2 1 
ATOM   4563 N  N   . TYR   B 1 210 ? 17.032 81.848  64.846 1.00 14.28 ? 651  TYR   B N   1 
ATOM   4564 C  CA  . TYR   B 1 210 ? 15.931 81.129  64.215 1.00 16.18 ? 651  TYR   B CA  1 
ATOM   4565 C  C   . TYR   B 1 210 ? 14.626 81.277  64.981 1.00 16.07 ? 651  TYR   B C   1 
ATOM   4566 O  O   . TYR   B 1 210 ? 13.556 81.052  64.402 1.00 16.69 ? 651  TYR   B O   1 
ATOM   4567 C  CB  . TYR   B 1 210 ? 16.268 79.637  64.066 1.00 17.88 ? 651  TYR   B CB  1 
ATOM   4568 C  CG  . TYR   B 1 210 ? 16.575 78.941  65.383 1.00 20.81 ? 651  TYR   B CG  1 
ATOM   4569 C  CD1 . TYR   B 1 210 ? 15.555 78.435  66.190 1.00 23.04 ? 651  TYR   B CD1 1 
ATOM   4570 C  CD2 . TYR   B 1 210 ? 17.884 78.790  65.811 1.00 22.02 ? 651  TYR   B CD2 1 
ATOM   4571 C  CE1 . TYR   B 1 210 ? 15.842 77.810  67.397 1.00 24.77 ? 651  TYR   B CE1 1 
ATOM   4572 C  CE2 . TYR   B 1 210 ? 18.178 78.172  67.010 1.00 22.13 ? 651  TYR   B CE2 1 
ATOM   4573 C  CZ  . TYR   B 1 210 ? 17.158 77.684  67.795 1.00 24.85 ? 651  TYR   B CZ  1 
ATOM   4574 O  OH  . TYR   B 1 210 ? 17.470 77.065  68.983 1.00 27.50 ? 651  TYR   B OH  1 
ATOM   4575 N  N   . ASP   B 1 211 ? 14.695 81.633  66.263 1.00 17.01 ? 652  ASP   B N   1 
ATOM   4576 C  CA  . ASP   B 1 211 ? 13.487 81.748  67.070 1.00 20.96 ? 652  ASP   B CA  1 
ATOM   4577 C  C   . ASP   B 1 211 ? 12.750 83.064  66.867 1.00 21.13 ? 652  ASP   B C   1 
ATOM   4578 O  O   . ASP   B 1 211 ? 11.662 83.239  67.427 1.00 22.04 ? 652  ASP   B O   1 
ATOM   4579 C  CB  . ASP   B 1 211 ? 13.792 81.496  68.555 1.00 29.08 ? 652  ASP   B CB  1 
ATOM   4580 C  CG  . ASP   B 1 211 ? 14.725 82.534  69.157 1.00 34.20 ? 652  ASP   B CG  1 
ATOM   4581 O  OD1 . ASP   B 1 211 ? 15.428 83.228  68.401 1.00 30.48 ? 652  ASP   B OD1 1 
ATOM   4582 O  OD2 . ASP   B 1 211 ? 14.765 82.643  70.403 1.00 35.59 ? 652  ASP   B OD2 1 
ATOM   4583 N  N   . LYS   B 1 212 ? 13.287 83.985  66.073 1.00 17.99 ? 653  LYS   B N   1 
ATOM   4584 C  CA  . LYS   B 1 212 ? 12.593 85.231  65.758 1.00 15.67 ? 653  LYS   B CA  1 
ATOM   4585 C  C   . LYS   B 1 212 ? 11.718 84.964  64.538 1.00 15.77 ? 653  LYS   B C   1 
ATOM   4586 O  O   . LYS   B 1 212 ? 12.178 85.026  63.396 1.00 14.79 ? 653  LYS   B O   1 
ATOM   4587 C  CB  . LYS   B 1 212 ? 13.587 86.367  65.548 1.00 16.51 ? 653  LYS   B CB  1 
ATOM   4588 C  CG  . LYS   B 1 212 ? 14.643 86.463  66.668 1.00 20.55 ? 653  LYS   B CG  1 
ATOM   4589 C  CD  . LYS   B 1 212 ? 14.043 86.461  68.074 1.00 22.74 ? 653  LYS   B CD  1 
ATOM   4590 C  CE  . LYS   B 1 212 ? 15.105 86.824  69.125 1.00 21.93 ? 653  LYS   B CE  1 
ATOM   4591 N  NZ  . LYS   B 1 212 ? 16.163 85.788  69.331 1.00 22.30 ? 653  LYS   B NZ  1 
ATOM   4592 N  N   . VAL   B 1 213 ? 10.449 84.636  64.791 1.00 14.71 ? 654  VAL   B N   1 
ATOM   4593 C  CA  . VAL   B 1 213 ? 9.524  84.195  63.754 1.00 18.01 ? 654  VAL   B CA  1 
ATOM   4594 C  C   . VAL   B 1 213 ? 8.582  85.293  63.297 1.00 15.19 ? 654  VAL   B C   1 
ATOM   4595 O  O   . VAL   B 1 213 ? 7.726  85.039  62.441 1.00 15.72 ? 654  VAL   B O   1 
ATOM   4596 C  CB  . VAL   B 1 213 ? 8.718  82.950  64.191 1.00 16.63 ? 654  VAL   B CB  1 
ATOM   4597 C  CG1 . VAL   B 1 213 ? 9.648  81.783  64.483 1.00 16.97 ? 654  VAL   B CG1 1 
ATOM   4598 C  CG2 . VAL   B 1 213 ? 7.833  83.275  65.415 1.00 16.03 ? 654  VAL   B CG2 1 
ATOM   4599 N  N   . GLY   B 1 214 ? 8.721  86.501  63.826 1.00 14.33 ? 655  GLY   B N   1 
ATOM   4600 C  CA  . GLY   B 1 214 ? 7.787  87.579  63.579 1.00 15.15 ? 655  GLY   B CA  1 
ATOM   4601 C  C   . GLY   B 1 214 ? 6.918  87.851  64.796 1.00 18.95 ? 655  GLY   B C   1 
ATOM   4602 O  O   . GLY   B 1 214 ? 6.860  87.072  65.748 1.00 19.01 ? 655  GLY   B O   1 
ATOM   4603 N  N   . LEU   B 1 215 ? 6.235  88.995  64.742 1.00 17.87 ? 656  LEU   B N   1 
ATOM   4604 C  CA  . LEU   B 1 215 ? 5.449  89.501  65.862 1.00 17.21 ? 656  LEU   B CA  1 
ATOM   4605 C  C   . LEU   B 1 215 ? 4.043  89.857  65.413 1.00 16.80 ? 656  LEU   B C   1 
ATOM   4606 O  O   . LEU   B 1 215 ? 3.845  90.359  64.307 1.00 15.84 ? 656  LEU   B O   1 
ATOM   4607 C  CB  . LEU   B 1 215 ? 6.092  90.763  66.444 1.00 18.52 ? 656  LEU   B CB  1 
ATOM   4608 C  CG  . LEU   B 1 215 ? 7.490  90.615  67.051 1.00 20.01 ? 656  LEU   B CG  1 
ATOM   4609 C  CD1 . LEU   B 1 215 ? 8.095  91.988  67.313 1.00 19.99 ? 656  LEU   B CD1 1 
ATOM   4610 C  CD2 . LEU   B 1 215 ? 7.412  89.804  68.323 1.00 20.88 ? 656  LEU   B CD2 1 
ATOM   4611 N  N   . GLY   B 1 216 ? 3.070  89.627  66.300 1.00 15.22 ? 657  GLY   B N   1 
ATOM   4612 C  CA  . GLY   B 1 216 ? 1.708  90.068  66.037 1.00 15.90 ? 657  GLY   B CA  1 
ATOM   4613 C  C   . GLY   B 1 216 ? 1.147  89.424  64.785 1.00 17.37 ? 657  GLY   B C   1 
ATOM   4614 O  O   . GLY   B 1 216 ? 1.188  88.200  64.614 1.00 17.53 ? 657  GLY   B O   1 
ATOM   4615 N  N   . LYS   B 1 217 ? 0.633  90.263  63.884 1.00 19.55 ? 658  LYS   B N   1 
ATOM   4616 C  CA  . LYS   B 1 217 ? 0.099  89.765  62.626 1.00 27.51 ? 658  LYS   B CA  1 
ATOM   4617 C  C   . LYS   B 1 217 ? 1.169  89.064  61.792 1.00 26.93 ? 658  LYS   B C   1 
ATOM   4618 O  O   . LYS   B 1 217 ? 0.838  88.255  60.914 1.00 25.13 ? 658  LYS   B O   1 
ATOM   4619 C  CB  . LYS   B 1 217 ? -0.477 90.931  61.833 1.00 37.06 ? 658  LYS   B CB  1 
ATOM   4620 C  CG  . LYS   B 1 217 ? -1.249 90.495  60.614 1.00 54.04 ? 658  LYS   B CG  1 
ATOM   4621 C  CD  . LYS   B 1 217 ? -1.861 91.673  59.936 1.00 67.86 ? 658  LYS   B CD  1 
ATOM   4622 C  CE  . LYS   B 1 217 ? -0.732 92.635  59.405 1.00 65.99 ? 658  LYS   B CE  1 
ATOM   4623 N  NZ  . LYS   B 1 217 ? -1.269 93.655  58.607 1.00 57.85 ? 658  LYS   B NZ  1 
ATOM   4624 N  N   . GLY   B 1 218 ? 2.440  89.357  62.041 1.00 20.20 ? 659  GLY   B N   1 
ATOM   4625 C  CA  . GLY   B 1 218 ? 3.526  88.797  61.268 1.00 18.35 ? 659  GLY   B CA  1 
ATOM   4626 C  C   . GLY   B 1 218 ? 4.126  87.519  61.804 1.00 19.19 ? 659  GLY   B C   1 
ATOM   4627 O  O   . GLY   B 1 218 ? 5.160  87.081  61.282 1.00 17.19 ? 659  GLY   B O   1 
ATOM   4628 N  N   A ARG   B 1 219 ? 3.541  86.907  62.835 0.85 19.91 ? 660  ARG   B N   1 
ATOM   4629 N  N   B ARG   B 1 219 ? 3.519  86.896  62.814 0.15 20.10 ? 660  ARG   B N   1 
ATOM   4630 C  CA  A ARG   B 1 219 ? 4.113  85.675  63.362 0.85 21.33 ? 660  ARG   B CA  1 
ATOM   4631 C  CA  B ARG   B 1 219 ? 4.047  85.650  63.358 0.15 19.96 ? 660  ARG   B CA  1 
ATOM   4632 C  C   A ARG   B 1 219 ? 4.087  84.591  62.292 0.85 21.99 ? 660  ARG   B C   1 
ATOM   4633 C  C   B ARG   B 1 219 ? 4.072  84.579  62.276 0.15 21.53 ? 660  ARG   B C   1 
ATOM   4634 O  O   A ARG   B 1 219 ? 3.048  84.320  61.679 0.85 20.03 ? 660  ARG   B O   1 
ATOM   4635 O  O   B ARG   B 1 219 ? 3.046  84.287  61.654 0.15 20.37 ? 660  ARG   B O   1 
ATOM   4636 C  CB  A ARG   B 1 219 ? 3.362  85.217  64.613 0.85 24.79 ? 660  ARG   B CB  1 
ATOM   4637 C  CB  B ARG   B 1 219 ? 3.175  85.193  64.525 0.15 19.35 ? 660  ARG   B CB  1 
ATOM   4638 C  CG  A ARG   B 1 219 ? 3.562  86.123  65.805 0.85 27.61 ? 660  ARG   B CG  1 
ATOM   4639 C  CG  B ARG   B 1 219 ? 3.465  85.905  65.824 0.15 19.70 ? 660  ARG   B CG  1 
ATOM   4640 C  CD  A ARG   B 1 219 ? 3.018  85.485  67.083 0.85 28.06 ? 660  ARG   B CD  1 
ATOM   4641 C  CD  B ARG   B 1 219 ? 4.562  85.200  66.590 0.15 18.47 ? 660  ARG   B CD  1 
ATOM   4642 N  NE  A ARG   B 1 219 ? 3.850  84.386  67.571 0.85 23.69 ? 660  ARG   B NE  1 
ATOM   4643 N  NE  B ARG   B 1 219 ? 4.167  84.882  67.957 0.15 18.73 ? 660  ARG   B NE  1 
ATOM   4644 C  CZ  A ARG   B 1 219 ? 3.440  83.126  67.690 0.85 20.41 ? 660  ARG   B CZ  1 
ATOM   4645 C  CZ  B ARG   B 1 219 ? 5.015  84.474  68.894 0.15 16.97 ? 660  ARG   B CZ  1 
ATOM   4646 N  NH1 A ARG   B 1 219 ? 2.203  82.790  67.355 0.85 20.73 ? 660  ARG   B NH1 1 
ATOM   4647 N  NH1 B ARG   B 1 219 ? 6.304  84.345  68.607 0.15 15.62 ? 660  ARG   B NH1 1 
ATOM   4648 N  NH2 A ARG   B 1 219 ? 4.265  82.204  68.160 0.85 18.44 ? 660  ARG   B NH2 1 
ATOM   4649 N  NH2 B ARG   B 1 219 ? 4.578  84.203  70.116 0.15 19.71 ? 660  ARG   B NH2 1 
ATOM   4650 N  N   . GLY   B 1 220 ? 5.247  83.998  62.051 1.00 20.98 ? 661  GLY   B N   1 
ATOM   4651 C  CA  . GLY   B 1 220 ? 5.434  83.029  60.999 1.00 24.02 ? 661  GLY   B CA  1 
ATOM   4652 C  C   . GLY   B 1 220 ? 5.972  83.607  59.709 1.00 24.22 ? 661  GLY   B C   1 
ATOM   4653 O  O   . GLY   B 1 220 ? 6.410  82.841  58.848 1.00 19.73 ? 661  GLY   B O   1 
ATOM   4654 N  N   . TYR   B 1 221 ? 5.960  84.931  59.552 1.00 16.30 ? 662  TYR   B N   1 
ATOM   4655 C  CA  . TYR   B 1 221 ? 6.368  85.573  58.306 1.00 15.33 ? 662  TYR   B CA  1 
ATOM   4656 C  C   . TYR   B 1 221 ? 7.780  86.147  58.360 1.00 15.86 ? 662  TYR   B C   1 
ATOM   4657 O  O   . TYR   B 1 221 ? 8.143  86.969  57.506 1.00 14.23 ? 662  TYR   B O   1 
ATOM   4658 C  CB  . TYR   B 1 221 ? 5.345  86.631  57.887 1.00 17.53 ? 662  TYR   B CB  1 
ATOM   4659 C  CG  . TYR   B 1 221 ? 3.999  86.049  57.528 1.00 19.06 ? 662  TYR   B CG  1 
ATOM   4660 C  CD1 . TYR   B 1 221 ? 3.724  85.638  56.231 1.00 19.40 ? 662  TYR   B CD1 1 
ATOM   4661 C  CD2 . TYR   B 1 221 ? 3.011  85.888  58.492 1.00 22.88 ? 662  TYR   B CD2 1 
ATOM   4662 C  CE1 . TYR   B 1 221 ? 2.488  85.099  55.895 1.00 23.04 ? 662  TYR   B CE1 1 
ATOM   4663 C  CE2 . TYR   B 1 221 ? 1.774  85.352  58.168 1.00 27.32 ? 662  TYR   B CE2 1 
ATOM   4664 C  CZ  . TYR   B 1 221 ? 1.523  84.953  56.870 1.00 26.47 ? 662  TYR   B CZ  1 
ATOM   4665 O  OH  . TYR   B 1 221 ? 0.296  84.421  56.541 1.00 27.50 ? 662  TYR   B OH  1 
ATOM   4666 N  N   . ASN   B 1 222 ? 8.581  85.736  59.341 1.00 14.55 ? 663  ASN   B N   1 
ATOM   4667 C  CA  . ASN   B 1 222 ? 9.999  86.071  59.397 1.00 15.14 ? 663  ASN   B CA  1 
ATOM   4668 C  C   . ASN   B 1 222 ? 10.750 84.773  59.627 1.00 14.80 ? 663  ASN   B C   1 
ATOM   4669 O  O   . ASN   B 1 222 ? 10.537 84.111  60.647 1.00 15.38 ? 663  ASN   B O   1 
ATOM   4670 C  CB  . ASN   B 1 222 ? 10.277 87.045  60.539 1.00 15.81 ? 663  ASN   B CB  1 
ATOM   4671 C  CG  . ASN   B 1 222 ? 11.658 87.650  60.456 1.00 15.08 ? 663  ASN   B CG  1 
ATOM   4672 O  OD1 . ASN   B 1 222 ? 11.873 88.622  59.723 1.00 14.11 ? 663  ASN   B OD1 1 
ATOM   4673 N  ND2 . ASN   B 1 222 ? 12.611 87.084  61.209 1.00 14.31 ? 663  ASN   B ND2 1 
ATOM   4674 N  N   . VAL   B 1 223 ? 11.613 84.403  58.678 1.00 14.31 ? 664  VAL   B N   1 
ATOM   4675 C  CA  . VAL   B 1 223 ? 12.314 83.120  58.696 1.00 15.04 ? 664  VAL   B CA  1 
ATOM   4676 C  C   . VAL   B 1 223 ? 13.806 83.411  58.681 1.00 14.17 ? 664  VAL   B C   1 
ATOM   4677 O  O   . VAL   B 1 223 ? 14.343 83.813  57.643 1.00 13.97 ? 664  VAL   B O   1 
ATOM   4678 C  CB  . VAL   B 1 223 ? 11.939 82.244  57.490 1.00 14.42 ? 664  VAL   B CB  1 
ATOM   4679 C  CG1 . VAL   B 1 223 ? 12.683 80.925  57.549 1.00 16.40 ? 664  VAL   B CG1 1 
ATOM   4680 C  CG2 . VAL   B 1 223 ? 10.422 82.000  57.420 1.00 15.70 ? 664  VAL   B CG2 1 
ATOM   4681 N  N   . ASN   B 1 224 ? 14.481 83.195  59.807 1.00 13.63 ? 665  ASN   B N   1 
ATOM   4682 C  CA  . ASN   B 1 224 ? 15.927 83.356  59.902 1.00 14.84 ? 665  ASN   B CA  1 
ATOM   4683 C  C   . ASN   B 1 224 ? 16.581 81.985  59.846 1.00 14.39 ? 665  ASN   B C   1 
ATOM   4684 O  O   . ASN   B 1 224 ? 16.235 81.095  60.633 1.00 15.76 ? 665  ASN   B O   1 
ATOM   4685 C  CB  . ASN   B 1 224 ? 16.322 84.015  61.226 1.00 14.60 ? 665  ASN   B CB  1 
ATOM   4686 C  CG  . ASN   B 1 224 ? 16.089 85.514  61.233 1.00 15.10 ? 665  ASN   B CG  1 
ATOM   4687 O  OD1 . ASN   B 1 224 ? 16.146 86.168  60.187 1.00 14.46 ? 665  ASN   B OD1 1 
ATOM   4688 N  ND2 . ASN   B 1 224 ? 15.816 86.065  62.413 1.00 14.60 ? 665  ASN   B ND2 1 
ATOM   4689 N  N   . ILE   B 1 225 ? 17.542 81.833  58.941 1.00 13.58 ? 666  ILE   B N   1 
ATOM   4690 C  CA  . ILE   B 1 225 ? 18.321 80.607  58.803 1.00 15.14 ? 666  ILE   B CA  1 
ATOM   4691 C  C   . ILE   B 1 225 ? 19.753 80.958  59.178 1.00 16.12 ? 666  ILE   B C   1 
ATOM   4692 O  O   . ILE   B 1 225 ? 20.529 81.422  58.326 1.00 14.42 ? 666  ILE   B O   1 
ATOM   4693 C  CB  . ILE   B 1 225 ? 18.212 80.031  57.384 1.00 15.90 ? 666  ILE   B CB  1 
ATOM   4694 C  CG1 . ILE   B 1 225 ? 16.737 79.841  57.010 1.00 14.99 ? 666  ILE   B CG1 1 
ATOM   4695 C  CG2 . ILE   B 1 225 ? 18.964 78.720  57.311 1.00 16.09 ? 666  ILE   B CG2 1 
ATOM   4696 C  CD1 . ILE   B 1 225 ? 16.492 79.406  55.563 1.00 15.24 ? 666  ILE   B CD1 1 
ATOM   4697 N  N   . PRO   B 1 226 ? 20.132 80.770  60.434 1.00 17.03 ? 667  PRO   B N   1 
ATOM   4698 C  CA  . PRO   B 1 226 ? 21.438 81.230  60.916 1.00 17.56 ? 667  PRO   B CA  1 
ATOM   4699 C  C   . PRO   B 1 226 ? 22.490 80.136  60.891 1.00 16.18 ? 667  PRO   B C   1 
ATOM   4700 O  O   . PRO   B 1 226 ? 22.238 79.019  61.361 1.00 17.37 ? 667  PRO   B O   1 
ATOM   4701 C  CB  . PRO   B 1 226 ? 21.136 81.645  62.361 1.00 16.95 ? 667  PRO   B CB  1 
ATOM   4702 C  CG  . PRO   B 1 226 ? 19.913 80.824  62.755 1.00 18.76 ? 667  PRO   B CG  1 
ATOM   4703 C  CD  . PRO   B 1 226 ? 19.293 80.237  61.516 1.00 17.06 ? 667  PRO   B CD  1 
ATOM   4704 N  N   . TRP   B 1 227 ? 23.675 80.452  60.381 1.00 15.46 ? 668  TRP   B N   1 
ATOM   4705 C  CA  . TRP   B 1 227 ? 24.764 79.491  60.280 1.00 16.70 ? 668  TRP   B CA  1 
ATOM   4706 C  C   . TRP   B 1 227 ? 25.760 79.697  61.411 1.00 17.95 ? 668  TRP   B C   1 
ATOM   4707 O  O   . TRP   B 1 227 ? 26.149 80.833  61.710 1.00 16.51 ? 668  TRP   B O   1 
ATOM   4708 C  CB  . TRP   B 1 227 ? 25.485 79.617  58.939 1.00 14.04 ? 668  TRP   B CB  1 
ATOM   4709 C  CG  . TRP   B 1 227 ? 24.646 79.435  57.716 1.00 14.16 ? 668  TRP   B CG  1 
ATOM   4710 C  CD1 . TRP   B 1 227 ? 24.468 80.346  56.713 1.00 16.98 ? 668  TRP   B CD1 1 
ATOM   4711 C  CD2 . TRP   B 1 227 ? 23.878 78.278  57.348 1.00 14.45 ? 668  TRP   B CD2 1 
ATOM   4712 N  NE1 . TRP   B 1 227 ? 23.648 79.826  55.741 1.00 16.31 ? 668  TRP   B NE1 1 
ATOM   4713 C  CE2 . TRP   B 1 227 ? 23.272 78.560  56.100 1.00 15.15 ? 668  TRP   B CE2 1 
ATOM   4714 C  CE3 . TRP   B 1 227 ? 23.652 77.028  57.937 1.00 16.02 ? 668  TRP   B CE3 1 
ATOM   4715 C  CZ2 . TRP   B 1 227 ? 22.451 77.644  55.437 1.00 16.87 ? 668  TRP   B CZ2 1 
ATOM   4716 C  CZ3 . TRP   B 1 227 ? 22.828 76.117  57.271 1.00 17.77 ? 668  TRP   B CZ3 1 
ATOM   4717 C  CH2 . TRP   B 1 227 ? 22.237 76.435  56.040 1.00 17.19 ? 668  TRP   B CH2 1 
ATOM   4718 N  N   . ASN   B 1 228 ? 26.178 78.592  62.025 1.00 19.84 ? 669  ASN   B N   1 
ATOM   4719 C  CA  . ASN   B 1 228 ? 27.136 78.608  63.117 1.00 21.26 ? 669  ASN   B CA  1 
ATOM   4720 C  C   . ASN   B 1 228 ? 28.233 77.597  62.843 1.00 22.89 ? 669  ASN   B C   1 
ATOM   4721 O  O   . ASN   B 1 228 ? 27.970 76.510  62.322 1.00 24.69 ? 669  ASN   B O   1 
ATOM   4722 C  CB  . ASN   B 1 228 ? 26.470 78.237  64.440 1.00 20.03 ? 669  ASN   B CB  1 
ATOM   4723 C  CG  . ASN   B 1 228 ? 25.311 79.144  64.771 1.00 17.79 ? 669  ASN   B CG  1 
ATOM   4724 O  OD1 . ASN   B 1 228 ? 25.493 80.348  64.912 1.00 20.08 ? 669  ASN   B OD1 1 
ATOM   4725 N  ND2 . ASN   B 1 228 ? 24.114 78.572  64.912 1.00 19.06 ? 669  ASN   B ND2 1 
ATOM   4726 N  N   . GLY   B 1 229 ? 29.456 77.962  63.203 1.00 21.97 ? 670  GLY   B N   1 
ATOM   4727 C  CA  . GLY   B 1 229 ? 30.584 77.065  63.082 1.00 28.54 ? 670  GLY   B CA  1 
ATOM   4728 C  C   . GLY   B 1 229 ? 31.250 77.072  61.720 1.00 31.81 ? 670  GLY   B C   1 
ATOM   4729 O  O   . GLY   B 1 229 ? 32.254 77.761  61.515 1.00 38.97 ? 670  GLY   B O   1 
ATOM   4730 N  N   . GLY   B 1 230 ? 30.676 76.340  60.770 1.00 32.68 ? 671  GLY   B N   1 
ATOM   4731 C  CA  . GLY   B 1 230 ? 31.417 75.930  59.597 1.00 34.49 ? 671  GLY   B CA  1 
ATOM   4732 C  C   . GLY   B 1 230 ? 31.507 76.974  58.495 1.00 29.83 ? 671  GLY   B C   1 
ATOM   4733 O  O   . GLY   B 1 230 ? 30.788 77.977  58.452 1.00 27.94 ? 671  GLY   B O   1 
ATOM   4734 N  N   . LYS   B 1 231 ? 32.443 76.709  57.583 1.00 28.34 ? 672  LYS   B N   1 
ATOM   4735 C  CA  . LYS   B 1 231 ? 32.609 77.473  56.349 1.00 26.68 ? 672  LYS   B CA  1 
ATOM   4736 C  C   . LYS   B 1 231 ? 31.561 76.966  55.372 1.00 23.53 ? 672  LYS   B C   1 
ATOM   4737 O  O   . LYS   B 1 231 ? 31.794 76.046  54.587 0.87 24.38 ? 672  LYS   B O   1 
ATOM   4738 C  CB  . LYS   B 1 231 ? 34.017 77.281  55.796 1.00 32.17 ? 672  LYS   B CB  1 
ATOM   4739 C  CG  . LYS   B 1 231 ? 34.315 78.103  54.550 1.00 37.08 ? 672  LYS   B CG  1 
ATOM   4740 C  CD  . LYS   B 1 231 ? 35.712 77.821  54.009 1.00 41.17 ? 672  LYS   B CD  1 
ATOM   4741 C  CE  . LYS   B 1 231 ? 36.104 78.832  52.935 1.00 43.03 ? 672  LYS   B CE  1 
ATOM   4742 N  NZ  . LYS   B 1 231 ? 36.778 78.201  51.759 1.00 43.11 ? 672  LYS   B NZ  1 
ATOM   4743 N  N   . MET   B 1 232 ? 30.390 77.580  55.414 1.00 19.80 ? 673  MET   B N   1 
ATOM   4744 C  CA  . MET   B 1 232 ? 29.264 77.085  54.642 1.00 17.36 ? 673  MET   B CA  1 
ATOM   4745 C  C   . MET   B 1 232 ? 29.443 77.404  53.163 1.00 16.98 ? 673  MET   B C   1 
ATOM   4746 O  O   . MET   B 1 232 ? 30.130 78.358  52.789 1.00 17.22 ? 673  MET   B O   1 
ATOM   4747 C  CB  . MET   B 1 232 ? 27.962 77.694  55.165 1.00 18.12 ? 673  MET   B CB  1 
ATOM   4748 C  CG  . MET   B 1 232 ? 27.767 77.519  56.672 1.00 19.49 ? 673  MET   B CG  1 
ATOM   4749 S  SD  . MET   B 1 232 ? 28.059 75.815  57.207 1.00 20.63 ? 673  MET   B SD  1 
ATOM   4750 C  CE  . MET   B 1 232 ? 27.725 75.952  58.956 1.00 19.27 ? 673  MET   B CE  1 
ATOM   4751 N  N   . GLY   B 1 233 ? 28.807 76.607  52.326 1.00 16.04 ? 674  GLY   B N   1 
ATOM   4752 C  CA  . GLY   B 1 233 ? 28.914 76.764  50.885 1.00 16.38 ? 674  GLY   B CA  1 
ATOM   4753 C  C   . GLY   B 1 233 ? 27.714 76.190  50.174 1.00 17.03 ? 674  GLY   B C   1 
ATOM   4754 O  O   . GLY   B 1 233 ? 26.619 76.099  50.737 1.00 16.93 ? 674  GLY   B O   1 
ATOM   4755 N  N   . ASP   B 1 234 ? 27.916 75.800  48.916 1.00 17.20 ? 675  ASP   B N   1 
ATOM   4756 C  CA  . ASP   B 1 234 ? 26.814 75.292  48.099 1.00 17.86 ? 675  ASP   B CA  1 
ATOM   4757 C  C   . ASP   B 1 234 ? 26.017 74.172  48.755 1.00 19.41 ? 675  ASP   B C   1 
ATOM   4758 O  O   . ASP   B 1 234 ? 24.781 74.201  48.660 1.00 16.25 ? 675  ASP   B O   1 
ATOM   4759 C  CB  . ASP   B 1 234 ? 27.315 74.843  46.719 1.00 19.52 ? 675  ASP   B CB  1 
ATOM   4760 C  CG  . ASP   B 1 234 ? 27.822 75.986  45.875 1.00 19.84 ? 675  ASP   B CG  1 
ATOM   4761 O  OD1 . ASP   B 1 234 ? 27.783 77.152  46.322 1.00 19.23 ? 675  ASP   B OD1 1 
ATOM   4762 O  OD2 . ASP   B 1 234 ? 28.268 75.707  44.737 1.00 21.61 ? 675  ASP   B OD2 1 
ATOM   4763 N  N   . PRO   B 1 235 ? 26.629 73.152  49.377 1.00 20.77 ? 676  PRO   B N   1 
ATOM   4764 C  CA  . PRO   B 1 235 ? 25.805 72.082  49.966 1.00 19.86 ? 676  PRO   B CA  1 
ATOM   4765 C  C   . PRO   B 1 235 ? 24.814 72.590  50.995 1.00 17.49 ? 676  PRO   B C   1 
ATOM   4766 O  O   . PRO   B 1 235 ? 23.639 72.194  50.974 1.00 18.22 ? 676  PRO   B O   1 
ATOM   4767 C  CB  . PRO   B 1 235 ? 26.843 71.121  50.567 1.00 25.84 ? 676  PRO   B CB  1 
ATOM   4768 C  CG  . PRO   B 1 235 ? 28.104 71.387  49.793 1.00 26.02 ? 676  PRO   B CG  1 
ATOM   4769 C  CD  . PRO   B 1 235 ? 28.073 72.853  49.493 1.00 23.63 ? 676  PRO   B CD  1 
ATOM   4770 N  N   . GLU   B 1 236 ? 25.255 73.483  51.881 1.00 19.09 ? 677  GLU   B N   1 
ATOM   4771 C  CA  . GLU   B 1 236 ? 24.385 73.981  52.943 1.00 18.02 ? 677  GLU   B CA  1 
ATOM   4772 C  C   . GLU   B 1 236 ? 23.279 74.866  52.382 1.00 16.22 ? 677  GLU   B C   1 
ATOM   4773 O  O   . GLU   B 1 236 ? 22.119 74.767  52.804 1.00 16.53 ? 677  GLU   B O   1 
ATOM   4774 C  CB  . GLU   B 1 236 ? 25.226 74.750  53.960 1.00 18.67 ? 677  GLU   B CB  1 
ATOM   4775 C  CG  . GLU   B 1 236 ? 26.205 73.899  54.769 1.00 20.81 ? 677  GLU   B CG  1 
ATOM   4776 C  CD  . GLU   B 1 236 ? 27.350 73.307  53.967 1.00 23.89 ? 677  GLU   B CD  1 
ATOM   4777 O  OE1 . GLU   B 1 236 ? 27.853 73.984  53.047 1.00 21.77 ? 677  GLU   B OE1 1 
ATOM   4778 O  OE2 . GLU   B 1 236 ? 27.770 72.171  54.286 1.00 26.97 ? 677  GLU   B OE2 1 
ATOM   4779 N  N   . TYR   B 1 237 ? 23.618 75.738  51.433 1.00 17.36 ? 678  TYR   B N   1 
ATOM   4780 C  CA  . TYR   B 1 237 ? 22.616 76.620  50.844 1.00 16.89 ? 678  TYR   B CA  1 
ATOM   4781 C  C   . TYR   B 1 237 ? 21.590 75.842  50.025 1.00 18.31 ? 678  TYR   B C   1 
ATOM   4782 O  O   . TYR   B 1 237 ? 20.388 76.137  50.085 1.00 17.07 ? 678  TYR   B O   1 
ATOM   4783 C  CB  . TYR   B 1 237 ? 23.301 77.727  50.041 1.00 14.84 ? 678  TYR   B CB  1 
ATOM   4784 C  CG  . TYR   B 1 237 ? 23.780 78.845  50.931 1.00 15.88 ? 678  TYR   B CG  1 
ATOM   4785 C  CD1 . TYR   B 1 237 ? 24.875 78.670  51.778 1.00 16.07 ? 678  TYR   B CD1 1 
ATOM   4786 C  CD2 . TYR   B 1 237 ? 23.110 80.059  50.974 1.00 16.43 ? 678  TYR   B CD2 1 
ATOM   4787 C  CE1 . TYR   B 1 237 ? 25.299 79.675  52.628 1.00 17.49 ? 678  TYR   B CE1 1 
ATOM   4788 C  CE2 . TYR   B 1 237 ? 23.526 81.071  51.823 1.00 14.32 ? 678  TYR   B CE2 1 
ATOM   4789 C  CZ  . TYR   B 1 237 ? 24.622 80.874  52.646 1.00 16.78 ? 678  TYR   B CZ  1 
ATOM   4790 O  OH  . TYR   B 1 237 ? 25.045 81.869  53.498 1.00 17.42 ? 678  TYR   B OH  1 
ATOM   4791 N  N   . MET   B 1 238 ? 22.034 74.832  49.272 1.00 17.06 ? 679  MET   B N   1 
ATOM   4792 C  CA  . MET   B 1 238 ? 21.075 74.010  48.541 1.00 17.36 ? 679  MET   B CA  1 
ATOM   4793 C  C   . MET   B 1 238 ? 20.151 73.258  49.492 1.00 16.97 ? 679  MET   B C   1 
ATOM   4794 O  O   . MET   B 1 238 ? 18.942 73.174  49.248 1.00 18.01 ? 679  MET   B O   1 
ATOM   4795 C  CB  . MET   B 1 238 ? 21.785 73.049  47.590 1.00 20.25 ? 679  MET   B CB  1 
ATOM   4796 C  CG  . MET   B 1 238 ? 22.609 73.767  46.531 1.00 22.20 ? 679  MET   B CG  1 
ATOM   4797 S  SD  . MET   B 1 238 ? 21.604 74.581  45.280 1.00 22.05 ? 679  MET   B SD  1 
ATOM   4798 C  CE  . MET   B 1 238 ? 20.677 73.185  44.642 1.00 28.75 ? 679  MET   B CE  1 
ATOM   4799 N  N   . ALA   B 1 239 ? 20.698 72.713  50.580 1.00 17.86 ? 680  ALA   B N   1 
ATOM   4800 C  CA  . ALA   B 1 239 ? 19.857 72.030  51.561 1.00 19.70 ? 680  ALA   B CA  1 
ATOM   4801 C  C   . ALA   B 1 239 ? 18.846 72.986  52.191 1.00 18.43 ? 680  ALA   B C   1 
ATOM   4802 O  O   . ALA   B 1 239 ? 17.666 72.641  52.354 1.00 18.09 ? 680  ALA   B O   1 
ATOM   4803 C  CB  . ALA   B 1 239 ? 20.731 71.371  52.629 1.00 17.91 ? 680  ALA   B CB  1 
ATOM   4804 N  N   . ALA   B 1 240 ? 19.284 74.194  52.549 1.00 17.23 ? 681  ALA   B N   1 
ATOM   4805 C  CA  . ALA   B 1 240 ? 18.364 75.159  53.149 1.00 17.63 ? 681  ALA   B CA  1 
ATOM   4806 C  C   . ALA   B 1 240 ? 17.237 75.538  52.189 1.00 17.27 ? 681  ALA   B C   1 
ATOM   4807 O  O   . ALA   B 1 240 ? 16.082 75.704  52.607 1.00 17.93 ? 681  ALA   B O   1 
ATOM   4808 C  CB  . ALA   B 1 240 ? 19.133 76.399  53.609 1.00 19.40 ? 681  ALA   B CB  1 
ATOM   4809 N  N   . PHE   B 1 241 ? 17.546 75.667  50.897 1.00 17.18 ? 682  PHE   B N   1 
ATOM   4810 C  CA  . PHE   B 1 241 ? 16.504 75.979  49.926 1.00 16.37 ? 682  PHE   B CA  1 
ATOM   4811 C  C   . PHE   B 1 241 ? 15.533 74.817  49.771 1.00 17.82 ? 682  PHE   B C   1 
ATOM   4812 O  O   . PHE   B 1 241 ? 14.318 75.024  49.686 1.00 18.26 ? 682  PHE   B O   1 
ATOM   4813 C  CB  . PHE   B 1 241 ? 17.133 76.346  48.581 1.00 16.19 ? 682  PHE   B CB  1 
ATOM   4814 C  CG  . PHE   B 1 241 ? 17.293 77.824  48.380 1.00 16.23 ? 682  PHE   B CG  1 
ATOM   4815 C  CD1 . PHE   B 1 241 ? 18.029 78.580  49.294 1.00 16.85 ? 682  PHE   B CD1 1 
ATOM   4816 C  CD2 . PHE   B 1 241 ? 16.694 78.467  47.309 1.00 17.97 ? 682  PHE   B CD2 1 
ATOM   4817 C  CE1 . PHE   B 1 241 ? 18.167 79.949  49.125 1.00 17.53 ? 682  PHE   B CE1 1 
ATOM   4818 C  CE2 . PHE   B 1 241 ? 16.834 79.838  47.144 1.00 18.64 ? 682  PHE   B CE2 1 
ATOM   4819 C  CZ  . PHE   B 1 241 ? 17.573 80.573  48.055 1.00 17.33 ? 682  PHE   B CZ  1 
ATOM   4820 N  N   . HIS   B 1 242 ? 16.053 73.587  49.729 1.00 19.02 ? 683  HIS   B N   1 
ATOM   4821 C  CA  . HIS   B 1 242 ? 15.201 72.418  49.525 1.00 21.32 ? 683  HIS   B CA  1 
ATOM   4822 C  C   . HIS   B 1 242 ? 14.281 72.172  50.719 1.00 20.74 ? 683  HIS   B C   1 
ATOM   4823 O  O   . HIS   B 1 242 ? 13.095 71.873  50.542 1.00 21.32 ? 683  HIS   B O   1 
ATOM   4824 C  CB  . HIS   B 1 242 ? 16.066 71.190  49.239 1.00 23.86 ? 683  HIS   B CB  1 
ATOM   4825 C  CG  . HIS   B 1 242 ? 15.299 69.907  49.171 1.00 31.73 ? 683  HIS   B CG  1 
ATOM   4826 N  ND1 . HIS   B 1 242 ? 14.534 69.556  48.078 1.00 34.87 ? 683  HIS   B ND1 1 
ATOM   4827 C  CD2 . HIS   B 1 242 ? 15.189 68.884  50.051 1.00 36.20 ? 683  HIS   B CD2 1 
ATOM   4828 C  CE1 . HIS   B 1 242 ? 13.979 68.377  48.293 1.00 37.17 ? 683  HIS   B CE1 1 
ATOM   4829 N  NE2 . HIS   B 1 242 ? 14.361 67.946  49.481 1.00 38.39 ? 683  HIS   B NE2 1 
ATOM   4830 N  N   . HIS   B 1 243 ? 14.798 72.319  51.935 1.00 22.49 ? 684  HIS   B N   1 
ATOM   4831 C  CA  . HIS   B 1 243 ? 14.043 71.968  53.132 1.00 25.01 ? 684  HIS   B CA  1 
ATOM   4832 C  C   . HIS   B 1 243 ? 13.230 73.123  53.699 1.00 26.95 ? 684  HIS   B C   1 
ATOM   4833 O  O   . HIS   B 1 243 ? 12.235 72.880  54.393 1.00 22.75 ? 684  HIS   B O   1 
ATOM   4834 C  CB  . HIS   B 1 243 ? 14.994 71.455  54.216 1.00 27.70 ? 684  HIS   B CB  1 
ATOM   4835 C  CG  . HIS   B 1 243 ? 15.498 70.067  53.972 1.00 32.49 ? 684  HIS   B CG  1 
ATOM   4836 N  ND1 . HIS   B 1 243 ? 16.819 69.793  53.687 1.00 38.17 ? 684  HIS   B ND1 1 
ATOM   4837 C  CD2 . HIS   B 1 243 ? 14.859 68.873  53.981 1.00 32.73 ? 684  HIS   B CD2 1 
ATOM   4838 C  CE1 . HIS   B 1 243 ? 16.971 68.491  53.526 1.00 39.08 ? 684  HIS   B CE1 1 
ATOM   4839 N  NE2 . HIS   B 1 243 ? 15.798 67.910  53.699 1.00 34.81 ? 684  HIS   B NE2 1 
ATOM   4840 N  N   . LEU   B 1 244 ? 13.627 74.368  53.431 1.00 23.80 ? 685  LEU   B N   1 
ATOM   4841 C  CA  . LEU   B 1 244 ? 13.036 75.520  54.104 1.00 20.97 ? 685  LEU   B CA  1 
ATOM   4842 C  C   . LEU   B 1 244 ? 12.544 76.588  53.136 1.00 19.33 ? 685  LEU   B C   1 
ATOM   4843 O  O   . LEU   B 1 244 ? 11.346 76.886  53.092 1.00 18.35 ? 685  LEU   B O   1 
ATOM   4844 C  CB  . LEU   B 1 244 ? 14.044 76.146  55.070 1.00 19.57 ? 685  LEU   B CB  1 
ATOM   4845 C  CG  . LEU   B 1 244 ? 14.355 75.357  56.337 1.00 19.34 ? 685  LEU   B CG  1 
ATOM   4846 C  CD1 . LEU   B 1 244 ? 15.617 75.866  57.019 1.00 16.59 ? 685  LEU   B CD1 1 
ATOM   4847 C  CD2 . LEU   B 1 244 ? 13.164 75.447  57.279 1.00 19.09 ? 685  LEU   B CD2 1 
ATOM   4848 N  N   . VAL   B 1 245 ? 13.456 77.175  52.357 1.00 15.99 ? 686  VAL   B N   1 
ATOM   4849 C  CA  . VAL   B 1 245 ? 13.094 78.356  51.578 1.00 15.68 ? 686  VAL   B CA  1 
ATOM   4850 C  C   . VAL   B 1 245 ? 11.987 78.026  50.587 1.00 16.97 ? 686  VAL   B C   1 
ATOM   4851 O  O   . VAL   B 1 245 ? 10.965 78.716  50.519 1.00 18.03 ? 686  VAL   B O   1 
ATOM   4852 C  CB  . VAL   B 1 245 ? 14.323 78.966  50.881 1.00 15.91 ? 686  VAL   B CB  1 
ATOM   4853 C  CG1 . VAL   B 1 245 ? 13.899 80.167  50.053 1.00 18.20 ? 686  VAL   B CG1 1 
ATOM   4854 C  CG2 . VAL   B 1 245 ? 15.373 79.380  51.906 1.00 15.49 ? 686  VAL   B CG2 1 
ATOM   4855 N  N   . MET   B 1 246 ? 12.171 76.965  49.805 1.00 17.52 ? 687  MET   B N   1 
ATOM   4856 C  CA  . MET   B 1 246 ? 11.214 76.694  48.734 1.00 18.27 ? 687  MET   B CA  1 
ATOM   4857 C  C   . MET   B 1 246 ? 9.869  76.184  49.252 1.00 18.96 ? 687  MET   B C   1 
ATOM   4858 O  O   . MET   B 1 246 ? 8.827  76.628  48.753 1.00 18.80 ? 687  MET   B O   1 
ATOM   4859 C  CB  . MET   B 1 246 ? 11.821 75.796  47.646 1.00 17.00 ? 687  MET   B CB  1 
ATOM   4860 C  CG  . MET   B 1 246 ? 13.023 76.443  46.962 1.00 18.88 ? 687  MET   B CG  1 
ATOM   4861 S  SD  . MET   B 1 246 ? 12.629 78.028  46.182 1.00 19.34 ? 687  MET   B SD  1 
ATOM   4862 C  CE  . MET   B 1 246 ? 11.326 77.534  45.040 1.00 18.44 ? 687  MET   B CE  1 
ATOM   4863 N  N   . PRO   B 1 247 ? 9.828  75.273  50.234 1.00 20.36 ? 688  PRO   B N   1 
ATOM   4864 C  CA  . PRO   B 1 247 ? 8.509  74.865  50.761 1.00 19.65 ? 688  PRO   B CA  1 
ATOM   4865 C  C   . PRO   B 1 247 ? 7.715  76.022  51.338 1.00 19.99 ? 688  PRO   B C   1 
ATOM   4866 O  O   . PRO   B 1 247 ? 6.531  76.178  51.016 1.00 19.98 ? 688  PRO   B O   1 
ATOM   4867 C  CB  . PRO   B 1 247 ? 8.861  73.803  51.811 1.00 25.86 ? 688  PRO   B CB  1 
ATOM   4868 C  CG  . PRO   B 1 247 ? 10.165 73.253  51.361 1.00 30.13 ? 688  PRO   B CG  1 
ATOM   4869 C  CD  . PRO   B 1 247 ? 10.906 74.406  50.746 1.00 26.66 ? 688  PRO   B CD  1 
ATOM   4870 N  N   . ILE   B 1 248 ? 8.349  76.852  52.170 1.00 19.12 ? 689  ILE   B N   1 
ATOM   4871 C  CA  . ILE   B 1 248 ? 7.670  78.013  52.743 1.00 18.37 ? 689  ILE   B CA  1 
ATOM   4872 C  C   . ILE   B 1 248 ? 7.231  78.972  51.646 1.00 20.44 ? 689  ILE   B C   1 
ATOM   4873 O  O   . ILE   B 1 248 ? 6.081  79.427  51.614 1.00 18.79 ? 689  ILE   B O   1 
ATOM   4874 C  CB  . ILE   B 1 248 ? 8.578  78.709  53.772 1.00 16.87 ? 689  ILE   B CB  1 
ATOM   4875 C  CG1 . ILE   B 1 248 ? 8.902  77.762  54.926 1.00 17.56 ? 689  ILE   B CG1 1 
ATOM   4876 C  CG2 . ILE   B 1 248 ? 7.934  79.992  54.280 1.00 17.05 ? 689  ILE   B CG2 1 
ATOM   4877 C  CD1 . ILE   B 1 248 ? 9.907  78.326  55.906 1.00 18.29 ? 689  ILE   B CD1 1 
ATOM   4878 N  N   . ALA   B 1 249 ? 8.146  79.297  50.728 1.00 16.89 ? 690  ALA   B N   1 
ATOM   4879 C  CA  . ALA   B 1 249 ? 7.814  80.229  49.654 1.00 17.39 ? 690  ALA   B CA  1 
ATOM   4880 C  C   . ALA   B 1 249 ? 6.626  79.734  48.835 1.00 18.07 ? 690  ALA   B C   1 
ATOM   4881 O  O   . ALA   B 1 249 ? 5.724  80.513  48.508 1.00 18.74 ? 690  ALA   B O   1 
ATOM   4882 C  CB  . ALA   B 1 249 ? 9.030  80.457  48.757 1.00 15.93 ? 690  ALA   B CB  1 
ATOM   4883 N  N   . ARG   B 1 250 ? 6.604  78.441  48.503 1.00 18.56 ? 691  ARG   B N   1 
ATOM   4884 C  CA  . ARG   B 1 250 ? 5.495  77.906  47.720 1.00 20.53 ? 691  ARG   B CA  1 
ATOM   4885 C  C   . ARG   B 1 250 ? 4.178  78.013  48.480 1.00 21.42 ? 691  ARG   B C   1 
ATOM   4886 O  O   . ARG   B 1 250 ? 3.133  78.307  47.889 1.00 21.06 ? 691  ARG   B O   1 
ATOM   4887 C  CB  . ARG   B 1 250 ? 5.779  76.459  47.323 1.00 21.97 ? 691  ARG   B CB  1 
ATOM   4888 C  CG  . ARG   B 1 250 ? 6.676  76.303  46.100 1.00 24.53 ? 691  ARG   B CG  1 
ATOM   4889 C  CD  . ARG   B 1 250 ? 6.768  74.842  45.685 1.00 29.86 ? 691  ARG   B CD  1 
ATOM   4890 N  NE  . ARG   B 1 250 ? 7.513  74.042  46.654 1.00 33.69 ? 691  ARG   B NE  1 
ATOM   4891 C  CZ  . ARG   B 1 250 ? 8.791  73.694  46.517 1.00 33.83 ? 691  ARG   B CZ  1 
ATOM   4892 N  NH1 . ARG   B 1 250 ? 9.475  74.077  45.443 1.00 32.81 ? 691  ARG   B NH1 1 
ATOM   4893 N  NH2 . ARG   B 1 250 ? 9.385  72.965  47.456 1.00 29.97 ? 691  ARG   B NH2 1 
ATOM   4894 N  N   . GLU   B 1 251 ? 4.208  77.785  49.792 1.00 22.49 ? 692  GLU   B N   1 
ATOM   4895 C  CA  . GLU   B 1 251 ? 2.988  77.888  50.586 1.00 22.66 ? 692  GLU   B CA  1 
ATOM   4896 C  C   . GLU   B 1 251 ? 2.510  79.335  50.682 1.00 21.69 ? 692  GLU   B C   1 
ATOM   4897 O  O   . GLU   B 1 251 ? 1.303  79.605  50.636 1.00 21.67 ? 692  GLU   B O   1 
ATOM   4898 C  CB  . GLU   B 1 251 ? 3.228  77.292  51.974 1.00 22.85 ? 692  GLU   B CB  1 
ATOM   4899 C  CG  . GLU   B 1 251 ? 1.958  77.098  52.788 1.00 23.95 ? 692  GLU   B CG  1 
ATOM   4900 C  CD  . GLU   B 1 251 ? 2.194  76.283  54.043 1.00 27.81 ? 692  GLU   B CD  1 
ATOM   4901 O  OE1 . GLU   B 1 251 ? 3.273  75.659  54.164 1.00 26.92 ? 692  GLU   B OE1 1 
ATOM   4902 O  OE2 . GLU   B 1 251 ? 1.299  76.271  54.915 1.00 31.97 ? 692  GLU   B OE2 1 
ATOM   4903 N  N   . PHE   B 1 252 ? 3.447  80.276  50.815 1.00 18.61 ? 693  PHE   B N   1 
ATOM   4904 C  CA  . PHE   B 1 252 ? 3.110  81.696  50.853 1.00 18.84 ? 693  PHE   B CA  1 
ATOM   4905 C  C   . PHE   B 1 252 ? 2.534  82.173  49.526 1.00 20.57 ? 693  PHE   B C   1 
ATOM   4906 O  O   . PHE   B 1 252 ? 1.675  83.067  49.509 1.00 18.23 ? 693  PHE   B O   1 
ATOM   4907 C  CB  . PHE   B 1 252 ? 4.377  82.479  51.217 1.00 20.12 ? 693  PHE   B CB  1 
ATOM   4908 C  CG  . PHE   B 1 252 ? 4.198  83.974  51.291 1.00 18.70 ? 693  PHE   B CG  1 
ATOM   4909 C  CD1 . PHE   B 1 252 ? 3.373  84.547  52.245 1.00 16.67 ? 693  PHE   B CD1 1 
ATOM   4910 C  CD2 . PHE   B 1 252 ? 4.904  84.811  50.434 1.00 15.95 ? 693  PHE   B CD2 1 
ATOM   4911 C  CE1 . PHE   B 1 252 ? 3.228  85.932  52.321 1.00 17.59 ? 693  PHE   B CE1 1 
ATOM   4912 C  CE2 . PHE   B 1 252 ? 4.776  86.189  50.512 1.00 15.04 ? 693  PHE   B CE2 1 
ATOM   4913 C  CZ  . PHE   B 1 252 ? 3.938  86.750  51.451 1.00 17.45 ? 693  PHE   B CZ  1 
ATOM   4914 N  N   . ALA   B 1 253 ? 3.004  81.599  48.409 1.00 20.37 ? 694  ALA   B N   1 
ATOM   4915 C  CA  . ALA   B 1 253 ? 2.533  81.916  47.063 1.00 20.58 ? 694  ALA   B CA  1 
ATOM   4916 C  C   . ALA   B 1 253 ? 2.732  83.398  46.774 1.00 20.48 ? 694  ALA   B C   1 
ATOM   4917 O  O   . ALA   B 1 253 ? 1.757  84.131  46.566 1.00 21.49 ? 694  ALA   B O   1 
ATOM   4918 C  CB  . ALA   B 1 253 ? 1.062  81.524  46.890 1.00 20.81 ? 694  ALA   B CB  1 
ATOM   4919 N  N   . PRO   B 1 254 ? 3.972  83.879  46.755 1.00 17.52 ? 695  PRO   B N   1 
ATOM   4920 C  CA  . PRO   B 1 254 ? 4.197  85.305  46.521 1.00 16.68 ? 695  PRO   B CA  1 
ATOM   4921 C  C   . PRO   B 1 254 ? 3.721  85.723  45.141 1.00 17.41 ? 695  PRO   B C   1 
ATOM   4922 O  O   . PRO   B 1 254 ? 3.686  84.933  44.192 1.00 16.46 ? 695  PRO   B O   1 
ATOM   4923 C  CB  . PRO   B 1 254 ? 5.722  85.442  46.635 1.00 15.14 ? 695  PRO   B CB  1 
ATOM   4924 C  CG  . PRO   B 1 254 ? 6.241  84.102  46.245 1.00 16.79 ? 695  PRO   B CG  1 
ATOM   4925 C  CD  . PRO   B 1 254 ? 5.234  83.125  46.800 1.00 17.26 ? 695  PRO   B CD  1 
ATOM   4926 N  N   . GLU   B 1 255 ? 3.350  86.991  45.042 1.00 16.39 ? 696  GLU   B N   1 
ATOM   4927 C  CA  . GLU   B 1 255 ? 3.062  87.610  43.760 1.00 18.75 ? 696  GLU   B CA  1 
ATOM   4928 C  C   . GLU   B 1 255 ? 4.257  88.369  43.208 1.00 16.85 ? 696  GLU   B C   1 
ATOM   4929 O  O   . GLU   B 1 255 ? 4.240  88.767  42.042 1.00 18.14 ? 696  GLU   B O   1 
ATOM   4930 C  CB  . GLU   B 1 255 ? 1.837  88.520  43.901 1.00 22.02 ? 696  GLU   B CB  1 
ATOM   4931 C  CG  . GLU   B 1 255 ? 0.591  87.705  44.256 1.00 25.29 ? 696  GLU   B CG  1 
ATOM   4932 C  CD  . GLU   B 1 255 ? -0.537 88.533  44.829 1.00 31.81 ? 696  GLU   B CD  1 
ATOM   4933 O  OE1 . GLU   B 1 255 ? -0.415 88.986  45.984 1.00 26.38 ? 696  GLU   B OE1 1 
ATOM   4934 O  OE2 . GLU   B 1 255 ? -1.555 88.718  44.128 1.00 37.18 ? 696  GLU   B OE2 1 
ATOM   4935 N  N   . LEU   B 1 256 ? 5.297  88.552  44.015 1.00 14.09 ? 697  LEU   B N   1 
ATOM   4936 C  CA  . LEU   B 1 256 ? 6.544  89.166  43.586 1.00 14.02 ? 697  LEU   B CA  1 
ATOM   4937 C  C   . LEU   B 1 256 ? 7.647  88.643  44.494 1.00 14.70 ? 697  LEU   B C   1 
ATOM   4938 O  O   . LEU   B 1 256 ? 7.446  88.512  45.706 1.00 15.65 ? 697  LEU   B O   1 
ATOM   4939 C  CB  . LEU   B 1 256 ? 6.471  90.693  43.690 1.00 13.18 ? 697  LEU   B CB  1 
ATOM   4940 C  CG  . LEU   B 1 256 ? 7.754  91.473  43.373 1.00 14.94 ? 697  LEU   B CG  1 
ATOM   4941 C  CD1 . LEU   B 1 256 ? 8.167  91.316  41.917 1.00 17.40 ? 697  LEU   B CD1 1 
ATOM   4942 C  CD2 . LEU   B 1 256 ? 7.528  92.931  43.701 1.00 17.87 ? 697  LEU   B CD2 1 
ATOM   4943 N  N   . VAL   B 1 257 ? 8.797  88.324  43.906 1.00 14.27 ? 698  VAL   B N   1 
ATOM   4944 C  CA  . VAL   B 1 257 ? 9.968  87.895  44.673 1.00 14.31 ? 698  VAL   B CA  1 
ATOM   4945 C  C   . VAL   B 1 257 ? 11.056 88.954  44.530 1.00 11.62 ? 698  VAL   B C   1 
ATOM   4946 O  O   . VAL   B 1 257 ? 11.450 89.300  43.408 1.00 13.25 ? 698  VAL   B O   1 
ATOM   4947 C  CB  . VAL   B 1 257 ? 10.486 86.524  44.209 1.00 15.18 ? 698  VAL   B CB  1 
ATOM   4948 C  CG1 . VAL   B 1 257 ? 11.733 86.138  44.991 1.00 17.96 ? 698  VAL   B CG1 1 
ATOM   4949 C  CG2 . VAL   B 1 257 ? 9.388  85.469  44.339 1.00 16.07 ? 698  VAL   B CG2 1 
ATOM   4950 N  N   . LEU   B 1 258 ? 11.562 89.445  45.653 1.00 12.79 ? 699  LEU   B N   1 
ATOM   4951 C  CA  . LEU   B 1 258 ? 12.734 90.309  45.662 1.00 12.16 ? 699  LEU   B CA  1 
ATOM   4952 C  C   . LEU   B 1 258 ? 13.872 89.531  46.293 1.00 12.97 ? 699  LEU   B C   1 
ATOM   4953 O  O   . LEU   B 1 258 ? 13.686 88.888  47.334 1.00 14.14 ? 699  LEU   B O   1 
ATOM   4954 C  CB  . LEU   B 1 258 ? 12.482 91.577  46.477 1.00 12.78 ? 699  LEU   B CB  1 
ATOM   4955 C  CG  . LEU   B 1 258 ? 11.249 92.409  46.138 1.00 12.53 ? 699  LEU   B CG  1 
ATOM   4956 C  CD1 . LEU   B 1 258 ? 11.181 93.619  47.052 1.00 15.18 ? 699  LEU   B CD1 1 
ATOM   4957 C  CD2 . LEU   B 1 258 ? 11.266 92.869  44.690 1.00 13.41 ? 699  LEU   B CD2 1 
ATOM   4958 N  N   . VAL   B 1 259 ? 15.050 89.597  45.687 1.00 14.26 ? 700  VAL   B N   1 
ATOM   4959 C  CA  . VAL   B 1 259 ? 16.244 88.999  46.269 1.00 12.09 ? 700  VAL   B CA  1 
ATOM   4960 C  C   . VAL   B 1 259 ? 17.137 90.117  46.780 1.00 12.83 ? 700  VAL   B C   1 
ATOM   4961 O  O   . VAL   B 1 259 ? 17.579 90.974  46.004 1.00 13.60 ? 700  VAL   B O   1 
ATOM   4962 C  CB  . VAL   B 1 259 ? 16.987 88.066  45.299 1.00 13.46 ? 700  VAL   B CB  1 
ATOM   4963 C  CG1 . VAL   B 1 259 ? 18.067 87.299  46.050 1.00 15.21 ? 700  VAL   B CG1 1 
ATOM   4964 C  CG2 . VAL   B 1 259 ? 16.006 87.105  44.638 1.00 14.29 ? 700  VAL   B CG2 1 
ATOM   4965 N  N   . SER   B 1 260 ? 17.341 90.148  48.096 1.00 13.50 ? 701  SER   B N   1 
ATOM   4966 C  CA  . SER   B 1 260 ? 18.432 90.930  48.656 1.00 11.43 ? 701  SER   B CA  1 
ATOM   4967 C  C   . SER   B 1 260 ? 19.706 90.142  48.385 1.00 11.30 ? 701  SER   B C   1 
ATOM   4968 O  O   . SER   B 1 260 ? 20.151 89.333  49.211 1.00 12.74 ? 701  SER   B O   1 
ATOM   4969 C  CB  . SER   B 1 260 ? 18.220 91.207  50.147 1.00 13.88 ? 701  SER   B CB  1 
ATOM   4970 O  OG  . SER   B 1 260 ? 17.481 92.409  50.304 1.00 15.12 ? 701  SER   B OG  1 
ATOM   4971 N  N   . ALA   B 1 261 ? 20.282 90.371  47.206 1.00 12.45 ? 702  ALA   B N   1 
ATOM   4972 C  CA  . ALA   B 1 261 ? 21.365 89.554  46.661 1.00 13.81 ? 702  ALA   B CA  1 
ATOM   4973 C  C   . ALA   B 1 261 ? 22.716 90.193  46.981 1.00 13.55 ? 702  ALA   B C   1 
ATOM   4974 O  O   . ALA   B 1 261 ? 23.359 90.827  46.141 1.00 14.84 ? 702  ALA   B O   1 
ATOM   4975 C  CB  . ALA   B 1 261 ? 21.177 89.383  45.157 1.00 14.49 ? 702  ALA   B CB  1 
ATOM   4976 N  N   . GLY   B 1 262 ? 23.145 90.030  48.225 1.00 13.05 ? 703  GLY   B N   1 
ATOM   4977 C  CA  . GLY   B 1 262 ? 24.536 90.266  48.538 1.00 14.07 ? 703  GLY   B CA  1 
ATOM   4978 C  C   . GLY   B 1 262 ? 25.358 89.078  48.091 1.00 12.69 ? 703  GLY   B C   1 
ATOM   4979 O  O   . GLY   B 1 262 ? 24.880 87.946  48.066 1.00 16.37 ? 703  GLY   B O   1 
ATOM   4980 N  N   . PHE   B 1 263 ? 26.595 89.342  47.685 1.00 12.21 ? 704  PHE   B N   1 
ATOM   4981 C  CA  . PHE   B 1 263 ? 27.481 88.273  47.240 1.00 13.01 ? 704  PHE   B CA  1 
ATOM   4982 C  C   . PHE   B 1 263 ? 28.696 88.147  48.144 1.00 13.91 ? 704  PHE   B C   1 
ATOM   4983 O  O   . PHE   B 1 263 ? 29.777 87.728  47.707 1.00 12.83 ? 704  PHE   B O   1 
ATOM   4984 C  CB  . PHE   B 1 263 ? 27.832 88.402  45.759 1.00 12.36 ? 704  PHE   B CB  1 
ATOM   4985 C  CG  . PHE   B 1 263 ? 26.638 88.305  44.882 1.00 12.15 ? 704  PHE   B CG  1 
ATOM   4986 C  CD1 . PHE   B 1 263 ? 26.093 87.067  44.583 1.00 14.03 ? 704  PHE   B CD1 1 
ATOM   4987 C  CD2 . PHE   B 1 263 ? 26.001 89.447  44.411 1.00 12.61 ? 704  PHE   B CD2 1 
ATOM   4988 C  CE1 . PHE   B 1 263 ? 24.947 86.959  43.783 1.00 13.20 ? 704  PHE   B CE1 1 
ATOM   4989 C  CE2 . PHE   B 1 263 ? 24.850 89.350  43.621 1.00 13.92 ? 704  PHE   B CE2 1 
ATOM   4990 C  CZ  . PHE   B 1 263 ? 24.334 88.106  43.303 1.00 12.76 ? 704  PHE   B CZ  1 
ATOM   4991 N  N   . ASP   B 1 264 ? 28.516 88.494  49.417 1.00 13.23 ? 705  ASP   B N   1 
ATOM   4992 C  CA  . ASP   B 1 264 ? 29.575 88.370  50.404 1.00 15.06 ? 705  ASP   B CA  1 
ATOM   4993 C  C   . ASP   B 1 264 ? 29.630 86.998  51.057 1.00 13.07 ? 705  ASP   B C   1 
ATOM   4994 O  O   . ASP   B 1 264 ? 30.533 86.762  51.869 1.00 14.46 ? 705  ASP   B O   1 
ATOM   4995 C  CB  . ASP   B 1 264 ? 29.549 89.504  51.455 1.00 13.88 ? 705  ASP   B CB  1 
ATOM   4996 C  CG  . ASP   B 1 264 ? 28.153 89.895  51.898 1.00 13.29 ? 705  ASP   B CG  1 
ATOM   4997 O  OD1 . ASP   B 1 264 ? 27.207 89.134  51.612 1.00 13.59 ? 705  ASP   B OD1 1 
ATOM   4998 O  OD2 . ASP   B 1 264 ? 28.008 90.960  52.571 1.00 14.34 ? 705  ASP   B OD2 1 
ATOM   4999 N  N   . ALA   B 1 265 ? 28.715 86.086  50.725 1.00 13.09 ? 706  ALA   B N   1 
ATOM   5000 C  CA  . ALA   B 1 265 ? 28.888 84.687  51.097 1.00 14.72 ? 706  ALA   B CA  1 
ATOM   5001 C  C   . ALA   B 1 265 ? 29.703 83.929  50.065 1.00 13.91 ? 706  ALA   B C   1 
ATOM   5002 O  O   . ALA   B 1 265 ? 29.892 82.718  50.194 1.00 15.13 ? 706  ALA   B O   1 
ATOM   5003 C  CB  . ALA   B 1 265 ? 27.538 83.997  51.308 1.00 14.22 ? 706  ALA   B CB  1 
ATOM   5004 N  N   . ALA   B 1 266 ? 30.190 84.621  49.046 1.00 13.32 ? 707  ALA   B N   1 
ATOM   5005 C  CA  . ALA   B 1 266 ? 30.850 83.961  47.936 1.00 13.44 ? 707  ALA   B CA  1 
ATOM   5006 C  C   . ALA   B 1 266 ? 32.267 83.558  48.298 1.00 13.56 ? 707  ALA   B C   1 
ATOM   5007 O  O   . ALA   B 1 266 ? 32.941 84.206  49.108 1.00 13.66 ? 707  ALA   B O   1 
ATOM   5008 C  CB  . ALA   B 1 266 ? 30.954 84.908  46.745 1.00 15.62 ? 707  ALA   B CB  1 
ATOM   5009 N  N   A ARG   B 1 267 ? 32.729 82.488  47.659 0.39 14.81 ? 708  ARG   B N   1 
ATOM   5010 N  N   B ARG   B 1 267 ? 32.717 82.470  47.680 0.61 14.46 ? 708  ARG   B N   1 
ATOM   5011 C  CA  A ARG   B 1 267 ? 34.129 82.103  47.755 0.39 15.40 ? 708  ARG   B CA  1 
ATOM   5012 C  CA  B ARG   B 1 267 ? 34.129 82.123  47.722 0.61 16.03 ? 708  ARG   B CA  1 
ATOM   5013 C  C   A ARG   B 1 267 ? 35.015 83.259  47.302 0.39 15.95 ? 708  ARG   B C   1 
ATOM   5014 C  C   B ARG   B 1 267 ? 34.967 83.332  47.332 0.61 14.78 ? 708  ARG   B C   1 
ATOM   5015 O  O   A ARG   B 1 267 ? 34.839 83.802  46.207 0.39 16.23 ? 708  ARG   B O   1 
ATOM   5016 O  O   B ARG   B 1 267 ? 34.714 83.976  46.308 0.61 14.76 ? 708  ARG   B O   1 
ATOM   5017 C  CB  A ARG   B 1 267 ? 34.364 80.876  46.873 0.39 16.26 ? 708  ARG   B CB  1 
ATOM   5018 C  CB  B ARG   B 1 267 ? 34.402 80.981  46.743 0.61 17.30 ? 708  ARG   B CB  1 
ATOM   5019 C  CG  A ARG   B 1 267 ? 35.805 80.658  46.437 0.39 19.03 ? 708  ARG   B CG  1 
ATOM   5020 C  CG  B ARG   B 1 267 ? 35.669 80.196  47.073 0.61 20.34 ? 708  ARG   B CG  1 
ATOM   5021 C  CD  A ARG   B 1 267 ? 35.880 79.590  45.349 0.39 21.77 ? 708  ARG   B CD  1 
ATOM   5022 C  CD  B ARG   B 1 267 ? 36.220 79.437  45.882 0.61 29.97 ? 708  ARG   B CD  1 
ATOM   5023 N  NE  A ARG   B 1 267 ? 35.449 80.113  44.055 0.39 24.64 ? 708  ARG   B NE  1 
ATOM   5024 N  NE  B ARG   B 1 267 ? 35.176 78.860  45.041 0.61 35.75 ? 708  ARG   B NE  1 
ATOM   5025 C  CZ  A ARG   B 1 267 ? 34.953 79.372  43.066 0.39 24.47 ? 708  ARG   B CZ  1 
ATOM   5026 C  CZ  B ARG   B 1 267 ? 34.893 79.280  43.812 0.61 40.75 ? 708  ARG   B CZ  1 
ATOM   5027 N  NH1 A ARG   B 1 267 ? 34.821 78.060  43.210 0.39 18.32 ? 708  ARG   B NH1 1 
ATOM   5028 N  NH1 B ARG   B 1 267 ? 35.574 80.285  43.279 0.61 44.08 ? 708  ARG   B NH1 1 
ATOM   5029 N  NH2 A ARG   B 1 267 ? 34.585 79.947  41.930 0.39 19.77 ? 708  ARG   B NH2 1 
ATOM   5030 N  NH2 B ARG   B 1 267 ? 33.930 78.696  43.112 0.61 42.52 ? 708  ARG   B NH2 1 
ATOM   5031 N  N   . GLY   B 1 268 ? 35.959 83.645  48.160 1.00 14.59 ? 709  GLY   B N   1 
ATOM   5032 C  CA  . GLY   B 1 268 ? 36.852 84.756  47.907 1.00 15.06 ? 709  GLY   B CA  1 
ATOM   5033 C  C   . GLY   B 1 268 ? 36.496 86.061  48.594 1.00 14.46 ? 709  GLY   B C   1 
ATOM   5034 O  O   . GLY   B 1 268 ? 37.310 86.995  48.569 1.00 14.41 ? 709  GLY   B O   1 
ATOM   5035 N  N   . ASP   B 1 269 ? 35.316 86.166  49.209 1.00 14.08 ? 710  ASP   B N   1 
ATOM   5036 C  CA  . ASP   B 1 269 ? 34.963 87.430  49.836 1.00 14.78 ? 710  ASP   B CA  1 
ATOM   5037 C  C   . ASP   B 1 269 ? 35.902 87.728  51.005 1.00 14.31 ? 710  ASP   B C   1 
ATOM   5038 O  O   . ASP   B 1 269 ? 36.248 86.822  51.771 1.00 16.38 ? 710  ASP   B O   1 
ATOM   5039 C  CB  . ASP   B 1 269 ? 33.534 87.400  50.349 1.00 15.97 ? 710  ASP   B CB  1 
ATOM   5040 C  CG  . ASP   B 1 269 ? 33.046 88.773  50.736 1.00 15.70 ? 710  ASP   B CG  1 
ATOM   5041 O  OD1 . ASP   B 1 269 ? 32.615 89.521  49.827 1.00 14.24 ? 710  ASP   B OD1 1 
ATOM   5042 O  OD2 . ASP   B 1 269 ? 33.128 89.120  51.932 1.00 14.69 ? 710  ASP   B OD2 1 
ATOM   5043 N  N   . PRO   B 1 270 ? 36.307 88.987  51.191 1.00 14.09 ? 711  PRO   B N   1 
ATOM   5044 C  CA  . PRO   B 1 270 ? 37.238 89.302  52.287 1.00 15.99 ? 711  PRO   B CA  1 
ATOM   5045 C  C   . PRO   B 1 270 ? 36.598 89.329  53.664 1.00 17.21 ? 711  PRO   B C   1 
ATOM   5046 O  O   . PRO   B 1 270 ? 37.336 89.320  54.662 1.00 17.76 ? 711  PRO   B O   1 
ATOM   5047 C  CB  . PRO   B 1 270 ? 37.776 90.686  51.905 1.00 15.04 ? 711  PRO   B CB  1 
ATOM   5048 C  CG  . PRO   B 1 270 ? 36.708 91.285  51.037 1.00 17.14 ? 711  PRO   B CG  1 
ATOM   5049 C  CD  . PRO   B 1 270 ? 36.095 90.138  50.291 1.00 15.65 ? 711  PRO   B CD  1 
ATOM   5050 N  N   . LEU   B 1 271 ? 35.267 89.332  53.757 1.00 14.99 ? 712  LEU   B N   1 
ATOM   5051 C  CA  . LEU   B 1 271 ? 34.564 89.469  55.027 1.00 16.84 ? 712  LEU   B CA  1 
ATOM   5052 C  C   . LEU   B 1 271 ? 33.715 88.264  55.389 1.00 17.96 ? 712  LEU   B C   1 
ATOM   5053 O  O   . LEU   B 1 271 ? 33.613 87.924  56.574 1.00 18.86 ? 712  LEU   B O   1 
ATOM   5054 C  CB  . LEU   B 1 271 ? 33.663 90.717  54.998 1.00 17.15 ? 712  LEU   B CB  1 
ATOM   5055 C  CG  . LEU   B 1 271 ? 34.373 92.060  54.807 1.00 19.49 ? 712  LEU   B CG  1 
ATOM   5056 C  CD1 . LEU   B 1 271 ? 33.371 93.194  54.684 1.00 21.35 ? 712  LEU   B CD1 1 
ATOM   5057 C  CD2 . LEU   B 1 271 ? 35.309 92.333  55.957 1.00 20.32 ? 712  LEU   B CD2 1 
ATOM   5058 N  N   . GLY   B 1 272 ? 33.100 87.605  54.404 1.00 15.94 ? 713  GLY   B N   1 
ATOM   5059 C  CA  . GLY   B 1 272 ? 32.074 86.621  54.718 1.00 15.17 ? 713  GLY   B CA  1 
ATOM   5060 C  C   . GLY   B 1 272 ? 32.624 85.321  55.278 1.00 15.90 ? 713  GLY   B C   1 
ATOM   5061 O  O   . GLY   B 1 272 ? 32.010 84.704  56.150 1.00 16.90 ? 713  GLY   B O   1 
ATOM   5062 N  N   . GLY   B 1 273 ? 33.777 84.879  54.781 1.00 15.75 ? 714  GLY   B N   1 
ATOM   5063 C  CA  . GLY   B 1 273 ? 34.329 83.609  55.214 1.00 18.94 ? 714  GLY   B CA  1 
ATOM   5064 C  C   . GLY   B 1 273 ? 33.623 82.371  54.704 1.00 19.71 ? 714  GLY   B C   1 
ATOM   5065 O  O   . GLY   B 1 273 ? 33.901 81.276  55.207 1.00 21.22 ? 714  GLY   B O   1 
ATOM   5066 N  N   . PHE   B 1 274 ? 32.732 82.492  53.719 1.00 16.31 ? 715  PHE   B N   1 
ATOM   5067 C  CA  . PHE   B 1 274 ? 31.987 81.359  53.186 1.00 16.40 ? 715  PHE   B CA  1 
ATOM   5068 C  C   . PHE   B 1 274 ? 32.472 81.041  51.771 1.00 18.53 ? 715  PHE   B C   1 
ATOM   5069 O  O   . PHE   B 1 274 ? 33.366 81.699  51.230 1.00 18.49 ? 715  PHE   B O   1 
ATOM   5070 C  CB  . PHE   B 1 274 ? 30.482 81.644  53.193 1.00 16.13 ? 715  PHE   B CB  1 
ATOM   5071 C  CG  . PHE   B 1 274 ? 29.809 81.429  54.534 1.00 18.83 ? 715  PHE   B CG  1 
ATOM   5072 C  CD1 . PHE   B 1 274 ? 30.541 81.169  55.688 1.00 20.35 ? 715  PHE   B CD1 1 
ATOM   5073 C  CD2 . PHE   B 1 274 ? 28.428 81.507  54.631 1.00 17.41 ? 715  PHE   B CD2 1 
ATOM   5074 C  CE1 . PHE   B 1 274 ? 29.890 80.982  56.919 1.00 17.32 ? 715  PHE   B CE1 1 
ATOM   5075 C  CE2 . PHE   B 1 274 ? 27.781 81.319  55.839 1.00 17.19 ? 715  PHE   B CE2 1 
ATOM   5076 C  CZ  . PHE   B 1 274 ? 28.509 81.058  56.984 1.00 17.52 ? 715  PHE   B CZ  1 
ATOM   5077 N  N   . GLN   B 1 275 ? 31.869 80.024  51.157 1.00 16.59 ? 716  GLN   B N   1 
ATOM   5078 C  CA  . GLN   B 1 275 ? 32.372 79.543  49.871 1.00 16.84 ? 716  GLN   B CA  1 
ATOM   5079 C  C   . GLN   B 1 275 ? 31.243 79.172  48.918 1.00 17.49 ? 716  GLN   B C   1 
ATOM   5080 O  O   . GLN   B 1 275 ? 31.351 78.208  48.155 1.00 18.21 ? 716  GLN   B O   1 
ATOM   5081 C  CB  . GLN   B 1 275 ? 33.370 78.395  50.039 1.00 20.61 ? 716  GLN   B CB  1 
ATOM   5082 C  CG  . GLN   B 1 275 ? 32.853 77.218  50.846 1.00 28.95 ? 716  GLN   B CG  1 
ATOM   5083 C  CD  . GLN   B 1 275 ? 33.960 76.232  51.198 1.00 33.95 ? 716  GLN   B CD  1 
ATOM   5084 O  OE1 . GLN   B 1 275 ? 34.957 76.121  50.483 1.00 38.28 ? 716  GLN   B OE1 1 
ATOM   5085 N  NE2 . GLN   B 1 275 ? 33.789 75.518  52.307 1.00 34.91 ? 716  GLN   B NE2 1 
ATOM   5086 N  N   . VAL   B 1 276 ? 30.151 79.943  48.915 1.00 16.21 ? 717  VAL   B N   1 
ATOM   5087 C  CA  . VAL   B 1 276 ? 29.160 79.781  47.857 1.00 14.93 ? 717  VAL   B CA  1 
ATOM   5088 C  C   . VAL   B 1 276 ? 29.793 80.123  46.512 1.00 14.66 ? 717  VAL   B C   1 
ATOM   5089 O  O   . VAL   B 1 276 ? 30.522 81.114  46.381 1.00 15.75 ? 717  VAL   B O   1 
ATOM   5090 C  CB  . VAL   B 1 276 ? 27.927 80.655  48.141 1.00 13.51 ? 717  VAL   B CB  1 
ATOM   5091 C  CG1 . VAL   B 1 276 ? 26.861 80.473  47.060 1.00 15.28 ? 717  VAL   B CG1 1 
ATOM   5092 C  CG2 . VAL   B 1 276 ? 27.343 80.304  49.507 1.00 13.87 ? 717  VAL   B CG2 1 
ATOM   5093 N  N   . THR   B 1 277 ? 29.525 79.291  45.506 1.00 15.39 ? 718  THR   B N   1 
ATOM   5094 C  CA  . THR   B 1 277 ? 30.140 79.487  44.200 1.00 15.73 ? 718  THR   B CA  1 
ATOM   5095 C  C   . THR   B 1 277 ? 29.203 80.238  43.262 1.00 16.72 ? 718  THR   B C   1 
ATOM   5096 O  O   . THR   B 1 277 ? 28.001 80.355  43.524 1.00 16.93 ? 718  THR   B O   1 
ATOM   5097 C  CB  . THR   B 1 277 ? 30.500 78.132  43.578 1.00 16.48 ? 718  THR   B CB  1 
ATOM   5098 O  OG1 . THR   B 1 277 ? 29.301 77.458  43.178 1.00 17.45 ? 718  THR   B OG1 1 
ATOM   5099 C  CG2 . THR   B 1 277 ? 31.317 77.269  44.558 1.00 18.11 ? 718  THR   B CG2 1 
ATOM   5100 N  N   . PRO   B 1 278 ? 29.724 80.782  42.155 1.00 16.72 ? 719  PRO   B N   1 
ATOM   5101 C  CA  . PRO   B 1 278 ? 28.819 81.406  41.177 1.00 15.92 ? 719  PRO   B CA  1 
ATOM   5102 C  C   . PRO   B 1 278 ? 27.765 80.439  40.658 1.00 16.90 ? 719  PRO   B C   1 
ATOM   5103 O  O   . PRO   B 1 278 ? 26.607 80.833  40.443 1.00 16.66 ? 719  PRO   B O   1 
ATOM   5104 C  CB  . PRO   B 1 278 ? 29.775 81.909  40.080 1.00 15.96 ? 719  PRO   B CB  1 
ATOM   5105 C  CG  . PRO   B 1 278 ? 31.083 82.085  40.781 1.00 16.46 ? 719  PRO   B CG  1 
ATOM   5106 C  CD  . PRO   B 1 278 ? 31.142 80.979  41.799 1.00 17.83 ? 719  PRO   B CD  1 
ATOM   5107 N  N   . GLU   B 1 279 ? 28.133 79.167  40.470 1.00 15.54 ? 720  GLU   B N   1 
ATOM   5108 C  CA  . GLU   B 1 279 ? 27.155 78.162  40.073 1.00 15.94 ? 720  GLU   B CA  1 
ATOM   5109 C  C   . GLU   B 1 279 ? 26.121 77.947  41.170 1.00 15.71 ? 720  GLU   B C   1 
ATOM   5110 O  O   . GLU   B 1 279 ? 24.949 77.669  40.886 1.00 16.58 ? 720  GLU   B O   1 
ATOM   5111 C  CB  . GLU   B 1 279 ? 27.859 76.841  39.757 1.00 19.01 ? 720  GLU   B CB  1 
ATOM   5112 C  CG  . GLU   B 1 279 ? 28.817 76.875  38.574 1.00 24.65 ? 720  GLU   B CG  1 
ATOM   5113 C  CD  . GLU   B 1 279 ? 30.146 77.544  38.890 1.00 27.14 ? 720  GLU   B CD  1 
ATOM   5114 O  OE1 . GLU   B 1 279 ? 30.523 77.615  40.085 1.00 24.80 ? 720  GLU   B OE1 1 
ATOM   5115 O  OE2 . GLU   B 1 279 ? 30.822 77.986  37.937 1.00 32.18 ? 720  GLU   B OE2 1 
ATOM   5116 N  N   . GLY   B 1 280 ? 26.543 78.039  42.431 1.00 15.56 ? 721  GLY   B N   1 
ATOM   5117 C  CA  . GLY   B 1 280 ? 25.585 77.957  43.526 1.00 15.12 ? 721  GLY   B CA  1 
ATOM   5118 C  C   . GLY   B 1 280 ? 24.536 79.048  43.459 1.00 14.76 ? 721  GLY   B C   1 
ATOM   5119 O  O   . GLY   B 1 280 ? 23.330 78.779  43.512 1.00 15.20 ? 721  GLY   B O   1 
ATOM   5120 N  N   . TYR   B 1 281 ? 24.978 80.294  43.303 1.00 15.00 ? 722  TYR   B N   1 
ATOM   5121 C  CA  . TYR   B 1 281 ? 24.031 81.395  43.157 1.00 13.94 ? 722  TYR   B CA  1 
ATOM   5122 C  C   . TYR   B 1 281 ? 23.117 81.200  41.949 1.00 15.02 ? 722  TYR   B C   1 
ATOM   5123 O  O   . TYR   B 1 281 ? 21.940 81.567  41.995 1.00 14.24 ? 722  TYR   B O   1 
ATOM   5124 C  CB  . TYR   B 1 281 ? 24.771 82.728  43.050 1.00 15.07 ? 722  TYR   B CB  1 
ATOM   5125 C  CG  . TYR   B 1 281 ? 25.426 83.184  44.338 1.00 13.54 ? 722  TYR   B CG  1 
ATOM   5126 C  CD1 . TYR   B 1 281 ? 24.667 83.623  45.419 1.00 13.94 ? 722  TYR   B CD1 1 
ATOM   5127 C  CD2 . TYR   B 1 281 ? 26.809 83.206  44.462 1.00 13.71 ? 722  TYR   B CD2 1 
ATOM   5128 C  CE1 . TYR   B 1 281 ? 25.276 84.055  46.596 1.00 13.52 ? 722  TYR   B CE1 1 
ATOM   5129 C  CE2 . TYR   B 1 281 ? 27.422 83.649  45.617 1.00 13.54 ? 722  TYR   B CE2 1 
ATOM   5130 C  CZ  . TYR   B 1 281 ? 26.657 84.065  46.679 1.00 13.60 ? 722  TYR   B CZ  1 
ATOM   5131 O  OH  . TYR   B 1 281 ? 27.311 84.489  47.809 1.00 13.42 ? 722  TYR   B OH  1 
ATOM   5132 N  N   . ALA   B 1 282 ? 23.648 80.661  40.845 1.00 15.25 ? 723  ALA   B N   1 
ATOM   5133 C  CA  . ALA   B 1 282 ? 22.802 80.380  39.692 1.00 13.89 ? 723  ALA   B CA  1 
ATOM   5134 C  C   . ALA   B 1 282 ? 21.698 79.399  40.048 1.00 14.01 ? 723  ALA   B C   1 
ATOM   5135 O  O   . ALA   B 1 282 ? 20.536 79.587  39.658 1.00 13.87 ? 723  ALA   B O   1 
ATOM   5136 C  CB  . ALA   B 1 282 ? 23.648 79.828  38.547 1.00 13.94 ? 723  ALA   B CB  1 
ATOM   5137 N  N   . HIS   B 1 283 ? 22.037 78.339  40.784 1.00 15.71 ? 724  HIS   B N   1 
ATOM   5138 C  CA  . HIS   B 1 283 ? 21.014 77.370  41.171 1.00 15.91 ? 724  HIS   B CA  1 
ATOM   5139 C  C   . HIS   B 1 283 ? 19.967 77.993  42.092 1.00 17.14 ? 724  HIS   B C   1 
ATOM   5140 O  O   . HIS   B 1 283 ? 18.771 77.705  41.958 1.00 18.00 ? 724  HIS   B O   1 
ATOM   5141 C  CB  . HIS   B 1 283 ? 21.653 76.132  41.804 1.00 20.26 ? 724  HIS   B CB  1 
ATOM   5142 C  CG  . HIS   B 1 283 ? 22.116 75.119  40.800 1.00 24.89 ? 724  HIS   B CG  1 
ATOM   5143 N  ND1 . HIS   B 1 283 ? 21.427 73.953  40.545 1.00 28.28 ? 724  HIS   B ND1 1 
ATOM   5144 C  CD2 . HIS   B 1 283 ? 23.195 75.105  39.982 1.00 26.66 ? 724  HIS   B CD2 1 
ATOM   5145 C  CE1 . HIS   B 1 283 ? 22.062 73.263  39.613 1.00 29.54 ? 724  HIS   B CE1 1 
ATOM   5146 N  NE2 . HIS   B 1 283 ? 23.138 73.941  39.254 1.00 28.03 ? 724  HIS   B NE2 1 
ATOM   5147 N  N   . LEU   B 1 284 ? 20.393 78.844  43.036 1.00 15.61 ? 725  LEU   B N   1 
ATOM   5148 C  CA  . LEU   B 1 284 ? 19.425 79.501  43.918 1.00 15.62 ? 725  LEU   B CA  1 
ATOM   5149 C  C   . LEU   B 1 284 ? 18.485 80.393  43.123 1.00 15.84 ? 725  LEU   B C   1 
ATOM   5150 O  O   . LEU   B 1 284 ? 17.272 80.407  43.370 1.00 15.51 ? 725  LEU   B O   1 
ATOM   5151 C  CB  . LEU   B 1 284 ? 20.146 80.308  45.002 1.00 14.67 ? 725  LEU   B CB  1 
ATOM   5152 C  CG  . LEU   B 1 284 ? 21.111 79.569  45.932 1.00 14.67 ? 725  LEU   B CG  1 
ATOM   5153 C  CD1 . LEU   B 1 284 ? 21.675 80.512  46.990 1.00 14.92 ? 725  LEU   B CD1 1 
ATOM   5154 C  CD2 . LEU   B 1 284 ? 20.456 78.339  46.555 1.00 16.39 ? 725  LEU   B CD2 1 
ATOM   5155 N  N   . THR   B 1 285 ? 19.029 81.149  42.164 1.00 14.44 ? 726  THR   B N   1 
ATOM   5156 C  CA  . THR   B 1 285 ? 18.197 81.990  41.310 1.00 13.32 ? 726  THR   B CA  1 
ATOM   5157 C  C   . THR   B 1 285 ? 17.202 81.147  40.532 1.00 15.78 ? 726  THR   B C   1 
ATOM   5158 O  O   . THR   B 1 285 ? 16.017 81.483  40.449 1.00 14.74 ? 726  THR   B O   1 
ATOM   5159 C  CB  . THR   B 1 285 ? 19.077 82.757  40.321 1.00 14.10 ? 726  THR   B CB  1 
ATOM   5160 O  OG1 . THR   B 1 285 ? 20.016 83.574  41.034 1.00 15.30 ? 726  THR   B OG1 1 
ATOM   5161 C  CG2 . THR   B 1 285 ? 18.228 83.640  39.446 1.00 14.68 ? 726  THR   B CG2 1 
ATOM   5162 N  N   . HIS   B 1 286 ? 17.678 80.050  39.945 1.00 14.99 ? 727  HIS   B N   1 
ATOM   5163 C  CA  . HIS   B 1 286 ? 16.811 79.213  39.121 1.00 15.56 ? 727  HIS   B CA  1 
ATOM   5164 C  C   . HIS   B 1 286 ? 15.655 78.653  39.940 1.00 15.50 ? 727  HIS   B C   1 
ATOM   5165 O  O   . HIS   B 1 286 ? 14.518 78.570  39.452 1.00 17.31 ? 727  HIS   B O   1 
ATOM   5166 C  CB  . HIS   B 1 286 ? 17.636 78.092  38.472 1.00 19.38 ? 727  HIS   B CB  1 
ATOM   5167 C  CG  . HIS   B 1 286 ? 16.858 77.238  37.509 1.00 22.31 ? 727  HIS   B CG  1 
ATOM   5168 N  ND1 . HIS   B 1 286 ? 16.588 77.624  36.213 1.00 28.51 ? 727  HIS   B ND1 1 
ATOM   5169 C  CD2 . HIS   B 1 286 ? 16.309 76.010  37.656 1.00 26.02 ? 727  HIS   B CD2 1 
ATOM   5170 C  CE1 . HIS   B 1 286 ? 15.894 76.674  35.609 1.00 31.22 ? 727  HIS   B CE1 1 
ATOM   5171 N  NE2 . HIS   B 1 286 ? 15.708 75.685  36.465 1.00 29.36 ? 727  HIS   B NE2 1 
ATOM   5172 N  N   . GLN   B 1 287 ? 15.915 78.283  41.195 1.00 16.72 ? 728  GLN   B N   1 
ATOM   5173 C  CA  . GLN   B 1 287 ? 14.836 77.810  42.053 1.00 17.80 ? 728  GLN   B CA  1 
ATOM   5174 C  C   . GLN   B 1 287 ? 13.811 78.911  42.309 1.00 18.64 ? 728  GLN   B C   1 
ATOM   5175 O  O   . GLN   B 1 287 ? 12.602 78.676  42.212 1.00 18.58 ? 728  GLN   B O   1 
ATOM   5176 C  CB  . GLN   B 1 287 ? 15.418 77.281  43.362 1.00 16.38 ? 728  GLN   B CB  1 
ATOM   5177 C  CG  . GLN   B 1 287 ? 16.137 75.945  43.206 1.00 21.35 ? 728  GLN   B CG  1 
ATOM   5178 C  CD  . GLN   B 1 287 ? 16.691 75.428  44.511 1.00 24.75 ? 728  GLN   B CD  1 
ATOM   5179 O  OE1 . GLN   B 1 287 ? 15.953 75.227  45.470 1.00 25.01 ? 728  GLN   B OE1 1 
ATOM   5180 N  NE2 . GLN   B 1 287 ? 17.996 75.198  44.551 1.00 29.52 ? 728  GLN   B NE2 1 
ATOM   5181 N  N   . LEU   B 1 288 ? 14.268 80.129  42.609 1.00 16.71 ? 729  LEU   B N   1 
ATOM   5182 C  CA  . LEU   B 1 288 ? 13.327 81.209  42.901 1.00 15.59 ? 729  LEU   B CA  1 
ATOM   5183 C  C   . LEU   B 1 288 ? 12.485 81.579  41.684 1.00 14.88 ? 729  LEU   B C   1 
ATOM   5184 O  O   . LEU   B 1 288 ? 11.357 82.065  41.836 1.00 15.80 ? 729  LEU   B O   1 
ATOM   5185 C  CB  . LEU   B 1 288 ? 14.075 82.431  43.429 1.00 14.61 ? 729  LEU   B CB  1 
ATOM   5186 C  CG  . LEU   B 1 288 ? 14.771 82.252  44.779 1.00 15.40 ? 729  LEU   B CG  1 
ATOM   5187 C  CD1 . LEU   B 1 288 ? 15.442 83.557  45.159 1.00 15.67 ? 729  LEU   B CD1 1 
ATOM   5188 C  CD2 . LEU   B 1 288 ? 13.797 81.811  45.862 1.00 14.98 ? 729  LEU   B CD2 1 
ATOM   5189 N  N   . MET   B 1 289 ? 13.005 81.350  40.478 1.00 15.46 ? 730  MET   B N   1 
ATOM   5190 C  CA  . MET   B 1 289 ? 12.250 81.635  39.264 1.00 15.34 ? 730  MET   B CA  1 
ATOM   5191 C  C   . MET   B 1 289 ? 10.998 80.774  39.133 1.00 16.46 ? 730  MET   B C   1 
ATOM   5192 O  O   . MET   B 1 289 ? 10.132 81.091  38.311 1.00 18.37 ? 730  MET   B O   1 
ATOM   5193 C  CB  . MET   B 1 289 ? 13.155 81.425  38.047 1.00 15.27 ? 730  MET   B CB  1 
ATOM   5194 C  CG  . MET   B 1 289 ? 14.254 82.463  37.941 1.00 16.83 ? 730  MET   B CG  1 
ATOM   5195 S  SD  . MET   B 1 289 ? 15.387 82.148  36.582 1.00 18.65 ? 730  MET   B SD  1 
ATOM   5196 C  CE  . MET   B 1 289 ? 14.251 82.100  35.187 1.00 16.85 ? 730  MET   B CE  1 
ATOM   5197 N  N   . SER   B 1 290 ? 10.888 79.692  39.897 1.00 16.61 ? 731  SER   B N   1 
ATOM   5198 C  CA  . SER   B 1 290 ? 9.677  78.878  39.894 1.00 18.51 ? 731  SER   B CA  1 
ATOM   5199 C  C   . SER   B 1 290 ? 8.545  79.485  40.712 1.00 26.88 ? 731  SER   B C   1 
ATOM   5200 O  O   . SER   B 1 290 ? 7.458  78.900  40.756 1.00 26.90 ? 731  SER   B O   1 
ATOM   5201 C  CB  . SER   B 1 290 ? 9.975  77.466  40.396 1.00 19.26 ? 731  SER   B CB  1 
ATOM   5202 O  OG  . SER   B 1 290 ? 10.267 77.460  41.783 1.00 20.07 ? 731  SER   B OG  1 
ATOM   5203 N  N   . LEU   B 1 291 ? 8.762  80.636  41.340 1.00 19.73 ? 732  LEU   B N   1 
ATOM   5204 C  CA  . LEU   B 1 291 ? 7.770  81.294  42.178 1.00 16.11 ? 732  LEU   B CA  1 
ATOM   5205 C  C   . LEU   B 1 291 ? 7.218  82.524  41.473 1.00 18.33 ? 732  LEU   B C   1 
ATOM   5206 O  O   . LEU   B 1 291 ? 7.860  83.107  40.595 1.00 18.94 ? 732  LEU   B O   1 
ATOM   5207 C  CB  . LEU   B 1 291 ? 8.402  81.740  43.498 1.00 17.19 ? 732  LEU   B CB  1 
ATOM   5208 C  CG  . LEU   B 1 291 ? 9.098  80.665  44.326 1.00 18.53 ? 732  LEU   B CG  1 
ATOM   5209 C  CD1 . LEU   B 1 291 ? 10.016 81.297  45.377 1.00 18.13 ? 732  LEU   B CD1 1 
ATOM   5210 C  CD2 . LEU   B 1 291 ? 8.085  79.729  44.986 1.00 19.78 ? 732  LEU   B CD2 1 
ATOM   5211 N  N   . ALA   B 1 292 ? 6.009  82.924  41.881 1.00 19.31 ? 733  ALA   B N   1 
ATOM   5212 C  CA  . ALA   B 1 292 ? 5.424  84.202  41.475 1.00 18.38 ? 733  ALA   B CA  1 
ATOM   5213 C  C   . ALA   B 1 292 ? 5.336  84.337  39.959 1.00 17.73 ? 733  ALA   B C   1 
ATOM   5214 O  O   . ALA   B 1 292 ? 5.458  85.437  39.419 1.00 16.09 ? 733  ALA   B O   1 
ATOM   5215 C  CB  . ALA   B 1 292 ? 6.163  85.396  42.091 1.00 15.02 ? 733  ALA   B CB  1 
ATOM   5216 N  N   . ALA   B 1 293 ? 5.136  83.208  39.278 1.00 17.12 ? 734  ALA   B N   1 
ATOM   5217 C  CA  . ALA   B 1 293 ? 5.093  83.158  37.819 1.00 18.91 ? 734  ALA   B CA  1 
ATOM   5218 C  C   . ALA   B 1 293 ? 6.343  83.766  37.200 1.00 20.65 ? 734  ALA   B C   1 
ATOM   5219 O  O   . ALA   B 1 293 ? 6.289  84.376  36.129 1.00 21.31 ? 734  ALA   B O   1 
ATOM   5220 C  CB  . ALA   B 1 293 ? 3.822  83.798  37.256 1.00 20.78 ? 734  ALA   B CB  1 
ATOM   5221 N  N   . GLY   B 1 294 ? 7.472  83.624  37.892 1.00 19.10 ? 735  GLY   B N   1 
ATOM   5222 C  CA  . GLY   B 1 294 ? 8.748  84.091  37.402 1.00 18.12 ? 735  GLY   B CA  1 
ATOM   5223 C  C   . GLY   B 1 294 ? 9.076  85.536  37.705 1.00 16.57 ? 735  GLY   B C   1 
ATOM   5224 O  O   . GLY   B 1 294 ? 10.117 86.023  37.244 1.00 17.35 ? 735  GLY   B O   1 
ATOM   5225 N  N   . ARG   B 1 295 ? 8.246  86.230  38.480 1.00 14.67 ? 736  ARG   B N   1 
ATOM   5226 C  CA  . ARG   B 1 295 ? 8.431  87.658  38.740 1.00 15.38 ? 736  ARG   B CA  1 
ATOM   5227 C  C   . ARG   B 1 295 ? 9.456  87.832  39.856 1.00 15.10 ? 736  ARG   B C   1 
ATOM   5228 O  O   . ARG   B 1 295 ? 9.119  87.903  41.042 1.00 17.36 ? 736  ARG   B O   1 
ATOM   5229 C  CB  . ARG   B 1 295 ? 7.101  88.301  39.098 1.00 18.03 ? 736  ARG   B CB  1 
ATOM   5230 C  CG  . ARG   B 1 295 ? 6.133  88.304  37.917 1.00 22.04 ? 736  ARG   B CG  1 
ATOM   5231 C  CD  . ARG   B 1 295 ? 4.832  89.017  38.232 1.00 31.80 ? 736  ARG   B CD  1 
ATOM   5232 N  NE  . ARG   B 1 295 ? 4.161  89.423  36.999 1.00 36.34 ? 736  ARG   B NE  1 
ATOM   5233 C  CZ  . ARG   B 1 295 ? 3.018  90.099  36.944 1.00 39.33 ? 736  ARG   B CZ  1 
ATOM   5234 N  NH1 . ARG   B 1 295 ? 2.392  90.455  38.058 1.00 40.45 ? 736  ARG   B NH1 1 
ATOM   5235 N  NH2 . ARG   B 1 295 ? 2.504  90.424  35.764 1.00 40.22 ? 736  ARG   B NH2 1 
ATOM   5236 N  N   . VAL   B 1 296 ? 10.724 87.928  39.457 1.00 14.25 ? 737  VAL   B N   1 
ATOM   5237 C  CA  . VAL   B 1 296 ? 11.853 87.967  40.376 1.00 14.29 ? 737  VAL   B CA  1 
ATOM   5238 C  C   . VAL   B 1 296 ? 12.680 89.205  40.065 1.00 14.56 ? 737  VAL   B C   1 
ATOM   5239 O  O   . VAL   B 1 296 ? 13.056 89.430  38.908 1.00 15.63 ? 737  VAL   B O   1 
ATOM   5240 C  CB  . VAL   B 1 296 ? 12.726 86.707  40.228 1.00 14.60 ? 737  VAL   B CB  1 
ATOM   5241 C  CG1 . VAL   B 1 296 ? 13.982 86.836  41.076 1.00 14.04 ? 737  VAL   B CG1 1 
ATOM   5242 C  CG2 . VAL   B 1 296 ? 11.946 85.453  40.576 1.00 17.03 ? 737  VAL   B CG2 1 
ATOM   5243 N  N   . LEU   B 1 297 ? 12.998 89.990  41.094 1.00 14.09 ? 738  LEU   B N   1 
ATOM   5244 C  CA  . LEU   B 1 297 ? 13.903 91.132  40.974 1.00 12.76 ? 738  LEU   B CA  1 
ATOM   5245 C  C   . LEU   B 1 297 ? 15.114 90.886  41.869 1.00 11.64 ? 738  LEU   B C   1 
ATOM   5246 O  O   . LEU   B 1 297 ? 14.969 90.738  43.087 1.00 13.13 ? 738  LEU   B O   1 
ATOM   5247 C  CB  . LEU   B 1 297 ? 13.193 92.435  41.363 1.00 12.66 ? 738  LEU   B CB  1 
ATOM   5248 C  CG  . LEU   B 1 297 ? 14.033 93.704  41.534 1.00 13.21 ? 738  LEU   B CG  1 
ATOM   5249 C  CD1 . LEU   B 1 297 ? 14.860 93.965  40.308 1.00 15.67 ? 738  LEU   B CD1 1 
ATOM   5250 C  CD2 . LEU   B 1 297 ? 13.164 94.916  41.858 1.00 16.69 ? 738  LEU   B CD2 1 
ATOM   5251 N  N   . ILE   B 1 298 ? 16.301 90.836  41.273 1.00 12.47 ? 739  ILE   B N   1 
ATOM   5252 C  CA  . ILE   B 1 298 ? 17.532 90.580  42.015 1.00 13.18 ? 739  ILE   B CA  1 
ATOM   5253 C  C   . ILE   B 1 298 ? 18.204 91.918  42.299 1.00 11.84 ? 739  ILE   B C   1 
ATOM   5254 O  O   . ILE   B 1 298 ? 18.602 92.625  41.365 1.00 15.54 ? 739  ILE   B O   1 
ATOM   5255 C  CB  . ILE   B 1 298 ? 18.463 89.650  41.221 1.00 12.10 ? 739  ILE   B CB  1 
ATOM   5256 C  CG1 . ILE   B 1 298 ? 17.770 88.308  40.991 1.00 14.99 ? 739  ILE   B CG1 1 
ATOM   5257 C  CG2 . ILE   B 1 298 ? 19.803 89.462  41.943 1.00 14.01 ? 739  ILE   B CG2 1 
ATOM   5258 C  CD1 . ILE   B 1 298 ? 18.599 87.309  40.246 1.00 16.90 ? 739  ILE   B CD1 1 
ATOM   5259 N  N   . ILE   B 1 299 ? 18.373 92.249  43.581 1.00 12.29 ? 740  ILE   B N   1 
ATOM   5260 C  CA  . ILE   B 1 299 ? 18.874 93.554  44.021 1.00 13.11 ? 740  ILE   B CA  1 
ATOM   5261 C  C   . ILE   B 1 299 ? 20.237 93.374  44.688 1.00 12.67 ? 740  ILE   B C   1 
ATOM   5262 O  O   . ILE   B 1 299 ? 20.344 92.680  45.706 1.00 13.81 ? 740  ILE   B O   1 
ATOM   5263 C  CB  . ILE   B 1 299 ? 17.899 94.220  45.005 1.00 11.52 ? 740  ILE   B CB  1 
ATOM   5264 C  CG1 . ILE   B 1 299 ? 16.518 94.381  44.368 1.00 14.23 ? 740  ILE   B CG1 1 
ATOM   5265 C  CG2 . ILE   B 1 299 ? 18.429 95.578  45.470 1.00 15.71 ? 740  ILE   B CG2 1 
ATOM   5266 C  CD1 . ILE   B 1 299 ? 15.482 94.905  45.322 1.00 14.47 ? 740  ILE   B CD1 1 
ATOM   5267 N  N   . LEU   B 1 300 ? 21.263 94.043  44.163 1.00 12.56 ? 741  LEU   B N   1 
ATOM   5268 C  CA  . LEU   B 1 300 ? 22.583 93.929  44.784 1.00 13.15 ? 741  LEU   B CA  1 
ATOM   5269 C  C   . LEU   B 1 300 ? 22.577 94.498  46.201 1.00 12.81 ? 741  LEU   B C   1 
ATOM   5270 O  O   . LEU   B 1 300 ? 22.105 95.615  46.427 1.00 14.80 ? 741  LEU   B O   1 
ATOM   5271 C  CB  . LEU   B 1 300 ? 23.621 94.675  43.950 1.00 13.83 ? 741  LEU   B CB  1 
ATOM   5272 C  CG  . LEU   B 1 300 ? 25.065 94.582  44.451 1.00 13.42 ? 741  LEU   B CG  1 
ATOM   5273 C  CD1 . LEU   B 1 300 ? 25.585 93.151  44.421 1.00 13.45 ? 741  LEU   B CD1 1 
ATOM   5274 C  CD2 . LEU   B 1 300 ? 25.939 95.525  43.647 1.00 15.00 ? 741  LEU   B CD2 1 
ATOM   5275 N  N   . GLU   B 1 301 ? 23.104 93.720  47.162 1.00 12.13 ? 742  GLU   B N   1 
ATOM   5276 C  CA  . GLU   B 1 301 ? 23.352 94.224  48.512 1.00 12.54 ? 742  GLU   B CA  1 
ATOM   5277 C  C   . GLU   B 1 301 ? 24.863 94.313  48.706 1.00 15.97 ? 742  GLU   B C   1 
ATOM   5278 O  O   . GLU   B 1 301 ? 25.516 95.124  48.046 1.00 17.06 ? 742  GLU   B O   1 
ATOM   5279 C  CB  . GLU   B 1 301 ? 22.661 93.373  49.593 1.00 14.01 ? 742  GLU   B CB  1 
ATOM   5280 C  CG  . GLU   B 1 301 ? 21.118 93.322  49.452 1.00 13.25 ? 742  GLU   B CG  1 
ATOM   5281 C  CD  . GLU   B 1 301 ? 20.405 94.506  50.097 1.00 16.80 ? 742  GLU   B CD  1 
ATOM   5282 O  OE1 . GLU   B 1 301 ? 21.069 95.479  50.513 1.00 17.88 ? 742  GLU   B OE1 1 
ATOM   5283 O  OE2 . GLU   B 1 301 ? 19.164 94.463  50.190 1.00 14.36 ? 742  GLU   B OE2 1 
ATOM   5284 N  N   . GLY   B 1 302 ? 25.428 93.453  49.550 1.00 15.26 ? 743  GLY   B N   1 
ATOM   5285 C  CA  . GLY   B 1 302 ? 26.854 93.435  49.816 1.00 15.04 ? 743  GLY   B CA  1 
ATOM   5286 C  C   . GLY   B 1 302 ? 27.629 92.542  48.867 1.00 14.53 ? 743  GLY   B C   1 
ATOM   5287 O  O   . GLY   B 1 302 ? 27.150 92.152  47.798 1.00 15.67 ? 743  GLY   B O   1 
ATOM   5288 N  N   . GLY   B 1 303 ? 28.868 92.232  49.259 1.00 16.51 ? 744  GLY   B N   1 
ATOM   5289 C  CA  . GLY   B 1 303 ? 29.758 91.486  48.388 1.00 14.15 ? 744  GLY   B CA  1 
ATOM   5290 C  C   . GLY   B 1 303 ? 30.947 92.339  47.982 1.00 13.17 ? 744  GLY   B C   1 
ATOM   5291 O  O   . GLY   B 1 303 ? 30.770 93.373  47.328 1.00 14.08 ? 744  GLY   B O   1 
ATOM   5292 N  N   . TYR   B 1 304 ? 32.168 91.900  48.312 1.00 13.25 ? 745  TYR   B N   1 
ATOM   5293 C  CA  . TYR   B 1 304 ? 33.329 92.784  48.305 1.00 12.61 ? 745  TYR   B CA  1 
ATOM   5294 C  C   . TYR   B 1 304 ? 34.541 92.268  47.556 1.00 15.42 ? 745  TYR   B C   1 
ATOM   5295 O  O   . TYR   B 1 304 ? 35.503 93.029  47.400 1.00 18.18 ? 745  TYR   B O   1 
ATOM   5296 C  CB  . TYR   B 1 304 ? 33.710 93.186  49.742 1.00 15.54 ? 745  TYR   B CB  1 
ATOM   5297 C  CG  . TYR   B 1 304 ? 32.490 93.728  50.401 1.00 15.20 ? 745  TYR   B CG  1 
ATOM   5298 C  CD1 . TYR   B 1 304 ? 32.029 94.990  50.065 1.00 15.46 ? 745  TYR   B CD1 1 
ATOM   5299 C  CD2 . TYR   B 1 304 ? 31.727 92.944  51.269 1.00 15.46 ? 745  TYR   B CD2 1 
ATOM   5300 C  CE1 . TYR   B 1 304 ? 30.865 95.492  50.602 1.00 16.54 ? 745  TYR   B CE1 1 
ATOM   5301 C  CE2 . TYR   B 1 304 ? 30.550 93.435  51.817 1.00 14.54 ? 745  TYR   B CE2 1 
ATOM   5302 C  CZ  . TYR   B 1 304 ? 30.128 94.715  51.478 1.00 16.41 ? 745  TYR   B CZ  1 
ATOM   5303 O  OH  . TYR   B 1 304 ? 28.963 95.236  51.998 1.00 19.79 ? 745  TYR   B OH  1 
ATOM   5304 N  N   . ASN   B 1 305 ? 34.538 91.034  47.072 1.00 12.24 ? 746  ASN   B N   1 
ATOM   5305 C  CA  . ASN   B 1 305 ? 35.559 90.603  46.123 1.00 12.24 ? 746  ASN   B CA  1 
ATOM   5306 C  C   . ASN   B 1 305 ? 35.025 90.944  44.741 1.00 13.98 ? 746  ASN   B C   1 
ATOM   5307 O  O   . ASN   B 1 305 ? 34.042 90.353  44.291 1.00 13.28 ? 746  ASN   B O   1 
ATOM   5308 C  CB  . ASN   B 1 305 ? 35.853 89.113  46.275 1.00 13.58 ? 746  ASN   B CB  1 
ATOM   5309 C  CG  . ASN   B 1 305 ? 36.901 88.612  45.281 1.00 13.78 ? 746  ASN   B CG  1 
ATOM   5310 O  OD1 . ASN   B 1 305 ? 36.840 88.898  44.075 1.00 14.13 ? 746  ASN   B OD1 1 
ATOM   5311 N  ND2 . ASN   B 1 305 ? 37.877 87.865  45.794 1.00 15.49 ? 746  ASN   B ND2 1 
ATOM   5312 N  N   . LEU   B 1 306 ? 35.661 91.910  44.077 1.00 13.12 ? 747  LEU   B N   1 
ATOM   5313 C  CA  . LEU   B 1 306 ? 35.125 92.419  42.817 1.00 13.00 ? 747  LEU   B CA  1 
ATOM   5314 C  C   . LEU   B 1 306 ? 34.973 91.312  41.785 1.00 13.45 ? 747  LEU   B C   1 
ATOM   5315 O  O   . LEU   B 1 306 ? 33.975 91.269  41.059 1.00 12.82 ? 747  LEU   B O   1 
ATOM   5316 C  CB  . LEU   B 1 306 ? 36.024 93.537  42.286 1.00 13.84 ? 747  LEU   B CB  1 
ATOM   5317 C  CG  . LEU   B 1 306 ? 36.154 94.770  43.185 1.00 14.11 ? 747  LEU   B CG  1 
ATOM   5318 C  CD1 . LEU   B 1 306 ? 37.228 95.690  42.616 1.00 15.99 ? 747  LEU   B CD1 1 
ATOM   5319 C  CD2 . LEU   B 1 306 ? 34.828 95.516  43.305 1.00 14.07 ? 747  LEU   B CD2 1 
ATOM   5320 N  N   . THR   B 1 307 ? 35.939 90.397  41.705 1.00 13.17 ? 748  THR   B N   1 
ATOM   5321 C  CA  . THR   B 1 307 ? 35.803 89.294  40.753 1.00 14.35 ? 748  THR   B CA  1 
ATOM   5322 C  C   . THR   B 1 307 ? 34.666 88.356  41.153 1.00 13.41 ? 748  THR   B C   1 
ATOM   5323 O  O   . THR   B 1 307 ? 33.849 87.968  40.309 1.00 15.37 ? 748  THR   B O   1 
ATOM   5324 C  CB  . THR   B 1 307 ? 37.142 88.565  40.631 1.00 16.69 ? 748  THR   B CB  1 
ATOM   5325 O  OG1 . THR   B 1 307 ? 38.099 89.469  40.071 1.00 15.56 ? 748  THR   B OG1 1 
ATOM   5326 C  CG2 . THR   B 1 307 ? 37.046 87.327  39.737 1.00 18.04 ? 748  THR   B CG2 1 
ATOM   5327 N  N   . SER   B 1 308 ? 34.577 88.013  42.439 1.00 12.69 ? 749  SER   B N   1 
ATOM   5328 C  CA  . SER   B 1 308 ? 33.543 87.090  42.898 1.00 14.06 ? 749  SER   B CA  1 
ATOM   5329 C  C   . SER   B 1 308 ? 32.149 87.642  42.657 1.00 13.90 ? 749  SER   B C   1 
ATOM   5330 O  O   . SER   B 1 308 ? 31.270 86.923  42.178 1.00 14.74 ? 749  SER   B O   1 
ATOM   5331 C  CB  . SER   B 1 308 ? 33.713 86.779  44.380 1.00 15.12 ? 749  SER   B CB  1 
ATOM   5332 O  OG  . SER   B 1 308 ? 35.001 86.232  44.642 1.00 16.95 ? 749  SER   B OG  1 
ATOM   5333 N  N   . ILE   B 1 309 ? 31.913 88.905  43.017 1.00 13.37 ? 750  ILE   B N   1 
ATOM   5334 C  CA  . ILE   B 1 309 ? 30.568 89.456  42.864 1.00 12.78 ? 750  ILE   B CA  1 
ATOM   5335 C  C   . ILE   B 1 309 ? 30.211 89.588  41.396 1.00 13.71 ? 750  ILE   B C   1 
ATOM   5336 O  O   . ILE   B 1 309 ? 29.057 89.368  41.008 1.00 13.29 ? 750  ILE   B O   1 
ATOM   5337 C  CB  . ILE   B 1 309 ? 30.393 90.772  43.642 1.00 12.99 ? 750  ILE   B CB  1 
ATOM   5338 C  CG1 . ILE   B 1 309 ? 31.163 91.935  43.003 1.00 13.08 ? 750  ILE   B CG1 1 
ATOM   5339 C  CG2 . ILE   B 1 309 ? 30.802 90.573  45.099 1.00 13.72 ? 750  ILE   B CG2 1 
ATOM   5340 C  CD1 . ILE   B 1 309 ? 30.911 93.295  43.662 1.00 15.22 ? 750  ILE   B CD1 1 
ATOM   5341 N  N   . SER   B 1 310 ? 31.193 89.920  40.555 1.00 12.66 ? 751  SER   B N   1 
ATOM   5342 C  CA  . SER   B 1 310 ? 30.929 90.078  39.131 1.00 13.74 ? 751  SER   B CA  1 
ATOM   5343 C  C   . SER   B 1 310 ? 30.541 88.753  38.495 1.00 13.74 ? 751  SER   B C   1 
ATOM   5344 O  O   . SER   B 1 310 ? 29.574 88.690  37.725 1.00 13.74 ? 751  SER   B O   1 
ATOM   5345 C  CB  . SER   B 1 310 ? 32.159 90.689  38.457 1.00 13.84 ? 751  SER   B CB  1 
ATOM   5346 O  OG  . SER   B 1 310 ? 32.347 92.016  38.919 1.00 15.14 ? 751  SER   B OG  1 
ATOM   5347 N  N   . GLU   B 1 311 ? 31.280 87.682  38.800 1.00 12.88 ? 752  GLU   B N   1 
ATOM   5348 C  CA  . GLU   B 1 311 ? 30.919 86.370  38.269 1.00 14.68 ? 752  GLU   B CA  1 
ATOM   5349 C  C   . GLU   B 1 311 ? 29.601 85.879  38.859 1.00 12.92 ? 752  GLU   B C   1 
ATOM   5350 O  O   . GLU   B 1 311 ? 28.743 85.357  38.134 1.00 14.75 ? 752  GLU   B O   1 
ATOM   5351 C  CB  . GLU   B 1 311 ? 32.044 85.377  38.557 1.00 18.64 ? 752  GLU   B CB  1 
ATOM   5352 C  CG  . GLU   B 1 311 ? 31.939 84.043  37.834 1.00 30.59 ? 752  GLU   B CG  1 
ATOM   5353 C  CD  . GLU   B 1 311 ? 32.069 84.172  36.324 1.00 39.69 ? 752  GLU   B CD  1 
ATOM   5354 O  OE1 . GLU   B 1 311 ? 32.782 85.086  35.861 1.00 36.81 ? 752  GLU   B OE1 1 
ATOM   5355 O  OE2 . GLU   B 1 311 ? 31.460 83.356  35.600 1.00 40.88 ? 752  GLU   B OE2 1 
ATOM   5356 N  N   . SER   B 1 312 ? 29.404 86.072  40.165 1.00 13.83 ? 753  SER   B N   1 
ATOM   5357 C  CA  . SER   B 1 312 ? 28.213 85.549  40.828 1.00 14.46 ? 753  SER   B CA  1 
ATOM   5358 C  C   . SER   B 1 312 ? 26.944 86.221  40.317 1.00 12.55 ? 753  SER   B C   1 
ATOM   5359 O  O   . SER   B 1 312 ? 25.962 85.545  39.970 1.00 14.98 ? 753  SER   B O   1 
ATOM   5360 C  CB  . SER   B 1 312 ? 28.333 85.746  42.339 1.00 12.49 ? 753  SER   B CB  1 
ATOM   5361 O  OG  . SER   B 1 312 ? 29.428 85.002  42.833 1.00 15.41 ? 753  SER   B OG  1 
ATOM   5362 N  N   . MET   B 1 313 ? 26.925 87.555  40.287 1.00 12.20 ? 754  MET   B N   1 
ATOM   5363 C  CA  . MET   B 1 313 ? 25.707 88.236  39.845 1.00 11.84 ? 754  MET   B CA  1 
ATOM   5364 C  C   . MET   B 1 313 ? 25.432 87.987  38.367 1.00 13.24 ? 754  MET   B C   1 
ATOM   5365 O  O   . MET   B 1 313 ? 24.272 87.825  37.970 1.00 13.53 ? 754  MET   B O   1 
ATOM   5366 C  CB  . MET   B 1 313 ? 25.739 89.728  40.173 1.00 13.81 ? 754  MET   B CB  1 
ATOM   5367 C  CG  . MET   B 1 313 ? 24.337 90.364  40.144 1.00 15.66 ? 754  MET   B CG  1 
ATOM   5368 S  SD  . MET   B 1 313 ? 24.291 92.067  40.722 1.00 14.62 ? 754  MET   B SD  1 
ATOM   5369 C  CE  . MET   B 1 313 ? 22.612 92.180  41.331 1.00 15.21 ? 754  MET   B CE  1 
ATOM   5370 N  N   A SER   B 1 314 ? 26.480 87.900  37.541 0.53 11.93 ? 755  SER   B N   1 
ATOM   5371 N  N   B SER   B 1 314 ? 26.475 87.995  37.530 0.47 13.10 ? 755  SER   B N   1 
ATOM   5372 C  CA  A SER   B 1 314 ? 26.278 87.581  36.129 0.53 12.08 ? 755  SER   B CA  1 
ATOM   5373 C  CA  B SER   B 1 314 ? 26.267 87.776  36.102 0.47 13.51 ? 755  SER   B CA  1 
ATOM   5374 C  C   A SER   B 1 314 ? 25.646 86.201  35.960 0.53 11.33 ? 755  SER   B C   1 
ATOM   5375 C  C   B SER   B 1 314 ? 25.658 86.408  35.831 0.47 15.43 ? 755  SER   B C   1 
ATOM   5376 O  O   A SER   B 1 314 ? 24.754 86.012  35.117 0.53 12.51 ? 755  SER   B O   1 
ATOM   5377 O  O   B SER   B 1 314 ? 24.845 86.260  34.908 0.47 16.87 ? 755  SER   B O   1 
ATOM   5378 C  CB  A SER   B 1 314 ? 27.603 87.677  35.366 0.53 11.11 ? 755  SER   B CB  1 
ATOM   5379 C  CB  B SER   B 1 314 ? 27.578 87.952  35.331 0.47 14.43 ? 755  SER   B CB  1 
ATOM   5380 O  OG  A SER   B 1 314 ? 28.105 89.009  35.344 0.53 11.10 ? 755  SER   B OG  1 
ATOM   5381 O  OG  B SER   B 1 314 ? 28.524 86.964  35.692 0.47 18.81 ? 755  SER   B OG  1 
ATOM   5382 N  N   A MET   B 1 315 ? 26.076 85.228  36.767 0.53 11.11 ? 756  MET   B N   1 
ATOM   5383 N  N   B MET   B 1 315 ? 26.015 85.401  36.632 0.47 13.10 ? 756  MET   B N   1 
ATOM   5384 C  CA  A MET   B 1 315 ? 25.474 83.897  36.707 0.53 13.52 ? 756  MET   B CA  1 
ATOM   5385 C  CA  B MET   B 1 315 ? 25.396 84.090  36.467 0.47 16.01 ? 756  MET   B CA  1 
ATOM   5386 C  C   A MET   B 1 315 ? 23.992 83.919  37.084 0.53 14.31 ? 756  MET   B C   1 
ATOM   5387 C  C   B MET   B 1 315 ? 23.929 84.103  36.892 0.47 14.00 ? 756  MET   B C   1 
ATOM   5388 O  O   A MET   B 1 315 ? 23.211 83.095  36.588 0.53 15.14 ? 756  MET   B O   1 
ATOM   5389 O  O   B MET   B 1 315 ? 23.095 83.439  36.263 0.47 13.23 ? 756  MET   B O   1 
ATOM   5390 C  CB  A MET   B 1 315 ? 26.260 82.934  37.599 0.53 20.40 ? 756  MET   B CB  1 
ATOM   5391 C  CB  B MET   B 1 315 ? 26.188 83.011  37.208 0.47 19.22 ? 756  MET   B CB  1 
ATOM   5392 C  CG  A MET   B 1 315 ? 26.613 81.613  36.924 0.53 26.90 ? 756  MET   B CG  1 
ATOM   5393 C  CG  B MET   B 1 315 ? 26.217 81.669  36.469 0.47 24.50 ? 756  MET   B CG  1 
ATOM   5394 S  SD  A MET   B 1 315 ? 27.356 81.794  35.285 0.53 26.29 ? 756  MET   B SD  1 
ATOM   5395 S  SD  B MET   B 1 315 ? 27.453 80.518  37.111 0.47 33.49 ? 756  MET   B SD  1 
ATOM   5396 C  CE  A MET   B 1 315 ? 26.183 80.858  34.306 0.53 31.01 ? 756  MET   B CE  1 
ATOM   5397 C  CE  B MET   B 1 315 ? 28.836 80.836  36.018 0.47 29.51 ? 756  MET   B CE  1 
ATOM   5398 N  N   . CYS   B 1 316 ? 23.584 84.853  37.948 1.00 14.03 ? 757  CYS   B N   1 
ATOM   5399 C  CA  . CYS   B 1 316 ? 22.168 85.006  38.280 1.00 14.49 ? 757  CYS   B CA  1 
ATOM   5400 C  C   . CYS   B 1 316 ? 21.394 85.592  37.112 1.00 15.24 ? 757  CYS   B C   1 
ATOM   5401 O  O   . CYS   B 1 316 ? 20.279 85.143  36.815 1.00 15.67 ? 757  CYS   B O   1 
ATOM   5402 C  CB  . CYS   B 1 316 ? 21.966 85.888  39.510 1.00 13.14 ? 757  CYS   B CB  1 
ATOM   5403 S  SG  . CYS   B 1 316 ? 22.686 85.269  41.043 1.00 19.38 ? 757  CYS   B SG  1 
ATOM   5404 N  N   . THR   B 1 317 ? 21.958 86.609  36.449 1.00 12.72 ? 758  THR   B N   1 
ATOM   5405 C  CA  . THR   B 1 317 ? 21.287 87.201  35.297 1.00 13.57 ? 758  THR   B CA  1 
ATOM   5406 C  C   . THR   B 1 317 ? 21.146 86.195  34.165 1.00 15.78 ? 758  THR   B C   1 
ATOM   5407 O  O   . THR   B 1 317 ? 20.111 86.152  33.491 1.00 15.09 ? 758  THR   B O   1 
ATOM   5408 C  CB  . THR   B 1 317 ? 22.033 88.450  34.828 1.00 12.89 ? 758  THR   B CB  1 
ATOM   5409 O  OG1 . THR   B 1 317 ? 22.148 89.365  35.926 1.00 14.27 ? 758  THR   B OG1 1 
ATOM   5410 C  CG2 . THR   B 1 317 ? 21.265 89.142  33.690 1.00 14.97 ? 758  THR   B CG2 1 
ATOM   5411 N  N   . SER   B 1 318 ? 22.180 85.378  33.942 1.00 15.31 ? 759  SER   B N   1 
ATOM   5412 C  CA  . SER   B 1 318 ? 22.089 84.313  32.954 1.00 15.67 ? 759  SER   B CA  1 
ATOM   5413 C  C   . SER   B 1 318 ? 20.909 83.391  33.239 1.00 16.89 ? 759  SER   B C   1 
ATOM   5414 O  O   . SER   B 1 318 ? 20.182 83.004  32.317 1.00 16.07 ? 759  SER   B O   1 
ATOM   5415 C  CB  . SER   B 1 318 ? 23.410 83.545  32.929 1.00 15.85 ? 759  SER   B CB  1 
ATOM   5416 O  OG  . SER   B 1 318 ? 23.315 82.402  32.107 1.00 20.18 ? 759  SER   B OG  1 
ATOM   5417 N  N   . MET   B 1 319 ? 20.667 83.069  34.514 1.00 13.89 ? 760  MET   B N   1 
ATOM   5418 C  CA  . MET   B 1 319 ? 19.506 82.251  34.858 1.00 16.02 ? 760  MET   B CA  1 
ATOM   5419 C  C   . MET   B 1 319 ? 18.206 82.973  34.537 1.00 17.16 ? 760  MET   B C   1 
ATOM   5420 O  O   . MET   B 1 319 ? 17.280 82.371  33.980 1.00 17.95 ? 760  MET   B O   1 
ATOM   5421 C  CB  . MET   B 1 319 ? 19.550 81.856  36.335 1.00 16.62 ? 760  MET   B CB  1 
ATOM   5422 C  CG  . MET   B 1 319 ? 20.746 80.990  36.705 1.00 17.14 ? 760  MET   B CG  1 
ATOM   5423 S  SD  . MET   B 1 319 ? 20.840 79.457  35.770 1.00 20.01 ? 760  MET   B SD  1 
ATOM   5424 C  CE  . MET   B 1 319 ? 22.028 79.866  34.484 1.00 17.76 ? 760  MET   B CE  1 
ATOM   5425 N  N   . LEU   B 1 320 ? 18.112 84.260  34.882 1.00 14.71 ? 761  LEU   B N   1 
ATOM   5426 C  CA  . LEU   B 1 320 ? 16.891 85.011  34.599 1.00 14.70 ? 761  LEU   B CA  1 
ATOM   5427 C  C   . LEU   B 1 320 ? 16.606 85.068  33.105 1.00 16.09 ? 761  LEU   B C   1 
ATOM   5428 O  O   . LEU   B 1 320 ? 15.434 85.094  32.695 1.00 15.31 ? 761  LEU   B O   1 
ATOM   5429 C  CB  . LEU   B 1 320 ? 16.990 86.433  35.153 1.00 14.41 ? 761  LEU   B CB  1 
ATOM   5430 C  CG  . LEU   B 1 320 ? 17.162 86.612  36.665 1.00 14.76 ? 761  LEU   B CG  1 
ATOM   5431 C  CD1 . LEU   B 1 320 ? 17.143 88.081  36.950 1.00 16.76 ? 761  LEU   B CD1 1 
ATOM   5432 C  CD2 . LEU   B 1 320 ? 16.052 85.932  37.435 1.00 15.63 ? 761  LEU   B CD2 1 
ATOM   5433 N  N   . LEU   B 1 321 ? 17.660 85.093  32.282 1.00 14.50 ? 762  LEU   B N   1 
ATOM   5434 C  CA  . LEU   B 1 321 ? 17.521 85.110  30.834 1.00 15.20 ? 762  LEU   B CA  1 
ATOM   5435 C  C   . LEU   B 1 321 ? 17.094 83.765  30.269 1.00 16.91 ? 762  LEU   B C   1 
ATOM   5436 O  O   . LEU   B 1 321 ? 16.834 83.677  29.061 1.00 19.76 ? 762  LEU   B O   1 
ATOM   5437 C  CB  . LEU   B 1 321 ? 18.837 85.561  30.202 1.00 13.87 ? 762  LEU   B CB  1 
ATOM   5438 C  CG  . LEU   B 1 321 ? 19.105 87.067  30.305 1.00 15.77 ? 762  LEU   B CG  1 
ATOM   5439 C  CD1 . LEU   B 1 321 ? 20.583 87.360  30.110 1.00 15.80 ? 762  LEU   B CD1 1 
ATOM   5440 C  CD2 . LEU   B 1 321 ? 18.264 87.841  29.292 1.00 15.60 ? 762  LEU   B CD2 1 
ATOM   5441 N  N   . GLY   B 1 322 ? 17.028 82.724  31.092 1.00 17.49 ? 763  GLY   B N   1 
ATOM   5442 C  CA  . GLY   B 1 322 ? 16.562 81.426  30.657 1.00 19.10 ? 763  GLY   B CA  1 
ATOM   5443 C  C   . GLY   B 1 322 ? 17.653 80.431  30.345 1.00 22.50 ? 763  GLY   B C   1 
ATOM   5444 O  O   . GLY   B 1 322 ? 17.347 79.338  29.853 1.00 25.70 ? 763  GLY   B O   1 
ATOM   5445 N  N   . ASP   B 1 323 ? 18.912 80.767  30.606 1.00 19.42 ? 764  ASP   B N   1 
ATOM   5446 C  CA  . ASP   B 1 323 ? 19.992 79.818  30.391 1.00 20.45 ? 764  ASP   B CA  1 
ATOM   5447 C  C   . ASP   B 1 323 ? 19.905 78.678  31.399 1.00 22.33 ? 764  ASP   B C   1 
ATOM   5448 O  O   . ASP   B 1 323 ? 19.388 78.829  32.509 1.00 22.61 ? 764  ASP   B O   1 
ATOM   5449 C  CB  . ASP   B 1 323 ? 21.350 80.510  30.513 1.00 20.92 ? 764  ASP   B CB  1 
ATOM   5450 C  CG  . ASP   B 1 323 ? 21.562 81.581  29.460 1.00 20.34 ? 764  ASP   B CG  1 
ATOM   5451 O  OD1 . ASP   B 1 323 ? 20.876 81.531  28.409 1.00 23.00 ? 764  ASP   B OD1 1 
ATOM   5452 O  OD2 . ASP   B 1 323 ? 22.418 82.468  29.671 1.00 19.30 ? 764  ASP   B OD2 1 
ATOM   5453 N  N   . SER   B 1 324 ? 20.424 77.541  31.010 1.00 27.10 ? 765  SER   B N   1 
ATOM   5454 C  CA  . SER   B 1 324 ? 20.326 76.372  31.865 1.00 26.65 ? 765  SER   B CA  1 
ATOM   5455 C  C   . SER   B 1 324 ? 21.318 76.478  33.022 1.00 21.80 ? 765  SER   B C   1 
ATOM   5456 O  O   . SER   B 1 324 ? 22.409 77.026  32.859 1.00 23.24 ? 765  SER   B O   1 
ATOM   5457 C  CB  . SER   B 1 324 ? 20.652 75.133  31.056 1.00 29.03 ? 765  SER   B CB  1 
ATOM   5458 O  OG  . SER   B 1 324 ? 19.662 74.906  30.069 0.49 27.25 ? 765  SER   B OG  1 
ATOM   5459 N  N   . PRO   B 1 325 ? 20.962 75.956  34.195 1.00 24.16 ? 766  PRO   B N   1 
ATOM   5460 C  CA  . PRO   B 1 325 ? 21.865 76.033  35.353 1.00 24.17 ? 766  PRO   B CA  1 
ATOM   5461 C  C   . PRO   B 1 325 ? 23.166 75.302  35.086 1.00 27.07 ? 766  PRO   B C   1 
ATOM   5462 O  O   . PRO   B 1 325 ? 23.166 74.197  34.521 1.00 32.46 ? 766  PRO   B O   1 
ATOM   5463 C  CB  . PRO   B 1 325 ? 21.068 75.334  36.466 1.00 25.06 ? 766  PRO   B CB  1 
ATOM   5464 C  CG  . PRO   B 1 325 ? 19.644 75.422  36.035 1.00 27.67 ? 766  PRO   B CG  1 
ATOM   5465 C  CD  . PRO   B 1 325 ? 19.682 75.315  34.538 1.00 29.15 ? 766  PRO   B CD  1 
ATOM   5466 N  N   . PRO   B 1 326 ? 24.296 75.887  35.472 1.00 25.93 ? 767  PRO   B N   1 
ATOM   5467 C  CA  . PRO   B 1 326 ? 25.575 75.170  35.383 1.00 29.23 ? 767  PRO   B CA  1 
ATOM   5468 C  C   . PRO   B 1 326 ? 25.648 74.068  36.431 1.00 29.24 ? 767  PRO   B C   1 
ATOM   5469 O  O   . PRO   B 1 326 ? 24.841 73.988  37.359 1.00 31.11 ? 767  PRO   B O   1 
ATOM   5470 C  CB  . PRO   B 1 326 ? 26.612 76.263  35.656 1.00 27.72 ? 767  PRO   B CB  1 
ATOM   5471 C  CG  . PRO   B 1 326 ? 25.883 77.289  36.457 1.00 27.14 ? 767  PRO   B CG  1 
ATOM   5472 C  CD  . PRO   B 1 326 ? 24.457 77.262  35.973 1.00 25.19 ? 767  PRO   B CD  1 
ATOM   5473 N  N   . SER   B 1 327 ? 26.675 73.255  36.268 1.00 29.98 ? 768  SER   B N   1 
ATOM   5474 C  CA  . SER   B 1 327 ? 26.814 72.103  37.161 1.00 34.00 ? 768  SER   B CA  1 
ATOM   5475 C  C   . SER   B 1 327 ? 27.532 72.532  38.436 1.00 33.95 ? 768  SER   B C   1 
ATOM   5476 O  O   . SER   B 1 327 ? 28.535 73.241  38.362 1.00 29.91 ? 768  SER   B O   1 
ATOM   5477 C  CB  . SER   B 1 327 ? 27.561 70.998  36.442 1.00 43.50 ? 768  SER   B CB  1 
ATOM   5478 O  OG  . SER   B 1 327 ? 27.103 70.878  35.106 1.00 50.41 ? 768  SER   B OG  1 
ATOM   5479 N  N   . LEU   B 1 328 ? 27.007 72.072  39.552 1.00 36.15 ? 769  LEU   B N   1 
ATOM   5480 C  CA  . LEU   B 1 328 ? 27.699 72.339  40.814 1.00 41.81 ? 769  LEU   B CA  1 
ATOM   5481 C  C   . LEU   B 1 328 ? 28.805 71.325  40.954 1.00 48.98 ? 769  LEU   B C   1 
ATOM   5482 O  O   . LEU   B 1 328 ? 28.753 70.280  40.313 1.00 54.35 ? 769  LEU   B O   1 
ATOM   5483 C  CB  . LEU   B 1 328 ? 26.756 72.183  42.005 1.00 40.11 ? 769  LEU   B CB  1 
ATOM   5484 C  CG  . LEU   B 1 328 ? 25.537 73.109  42.029 1.00 37.92 ? 769  LEU   B CG  1 
ATOM   5485 C  CD1 . LEU   B 1 328 ? 24.527 72.629  43.047 1.00 34.14 ? 769  LEU   B CD1 1 
ATOM   5486 C  CD2 . LEU   B 1 328 ? 25.998 74.510  42.358 1.00 39.65 ? 769  LEU   B CD2 1 
ATOM   5487 N  N   . ASP   B 1 329 ? 29.747 71.661  41.810 1.00 30.00 ? 770  ASP   B N   1 
ATOM   5488 C  CA  . ASP   B 1 329 ? 30.768 70.666  42.167 1.00 30.00 ? 770  ASP   B CA  1 
ATOM   5489 C  C   . ASP   B 1 329 ? 30.071 69.580  42.976 1.00 30.00 ? 770  ASP   B C   1 
ATOM   5490 O  O   . ASP   B 1 329 ? 28.974 69.798  43.474 1.00 30.00 ? 770  ASP   B O   1 
ATOM   5491 C  CB  . ASP   B 1 329 ? 31.788 71.303  43.084 1.00 30.00 ? 770  ASP   B CB  1 
ATOM   5492 N  N   . HIS   B 1 330 ? 30.715 68.430  43.103 1.00 30.00 ? 771  HIS   B N   1 
ATOM   5493 C  CA  . HIS   B 1 330 ? 30.156 67.396  43.995 1.00 30.00 ? 771  HIS   B CA  1 
ATOM   5494 C  C   . HIS   B 1 330 ? 29.873 68.033  45.358 1.00 30.00 ? 771  HIS   B C   1 
ATOM   5495 O  O   . HIS   B 1 330 ? 30.748 68.659  45.961 1.00 30.00 ? 771  HIS   B O   1 
ATOM   5496 C  CB  . HIS   B 1 330 ? 31.129 66.222  44.126 1.00 30.00 ? 771  HIS   B CB  1 
ATOM   5497 N  N   . LEU   B 1 331 ? 28.637 67.914  45.800 1.00 30.00 ? 772  LEU   B N   1 
ATOM   5498 C  CA  . LEU   B 1 331 ? 28.252 68.499  47.103 1.00 30.00 ? 772  LEU   B CA  1 
ATOM   5499 C  C   . LEU   B 1 331 ? 28.690 67.552  48.226 1.00 30.00 ? 772  LEU   B C   1 
ATOM   5500 O  O   . LEU   B 1 331 ? 28.276 66.390  48.237 1.00 30.00 ? 772  LEU   B O   1 
ATOM   5501 C  CB  . LEU   B 1 331 ? 26.759 68.808  47.179 1.00 30.00 ? 772  LEU   B CB  1 
ATOM   5502 C  CG  . LEU   B 1 331 ? 26.217 69.723  46.077 1.00 30.00 ? 772  LEU   B CG  1 
ATOM   5503 C  CD1 . LEU   B 1 331 ? 24.725 69.906  46.252 1.00 30.00 ? 772  LEU   B CD1 1 
ATOM   5504 C  CD2 . LEU   B 1 331 ? 26.923 71.068  46.079 1.00 30.00 ? 772  LEU   B CD2 1 
ATOM   5505 N  N   . THR   B 1 332 ? 29.549 68.044  49.100 1.00 67.05 ? 773  THR   B N   1 
ATOM   5506 C  CA  . THR   B 1 332 ? 29.950 67.247  50.252 1.00 61.31 ? 773  THR   B CA  1 
ATOM   5507 C  C   . THR   B 1 332 ? 28.815 67.075  51.227 1.00 59.12 ? 773  THR   B C   1 
ATOM   5508 O  O   . THR   B 1 332 ? 27.808 67.811  51.172 1.00 53.81 ? 773  THR   B O   1 
ATOM   5509 C  CB  . THR   B 1 332 ? 31.096 67.989  50.924 1.00 30.00 ? 773  THR   B CB  1 
ATOM   5510 O  OG1 . THR   B 1 332 ? 30.671 69.333  51.140 1.00 30.00 ? 773  THR   B OG1 1 
ATOM   5511 C  CG2 . THR   B 1 332 ? 32.362 67.980  50.087 1.00 30.00 ? 773  THR   B CG2 1 
ATOM   5512 N  N   . PRO   B 1 333 ? 28.948 66.130  52.167 1.00 57.57 ? 774  PRO   B N   1 
ATOM   5513 C  CA  . PRO   B 1 333 ? 27.970 66.013  53.218 1.00 52.17 ? 774  PRO   B CA  1 
ATOM   5514 C  C   . PRO   B 1 333 ? 27.880 67.346  53.919 1.00 47.84 ? 774  PRO   B C   1 
ATOM   5515 O  O   . PRO   B 1 333 ? 28.883 68.021  54.121 1.00 51.41 ? 774  PRO   B O   1 
ATOM   5516 C  CB  . PRO   B 1 333 ? 28.787 65.024  54.027 1.00 56.11 ? 774  PRO   B CB  1 
ATOM   5517 C  CG  . PRO   B 1 333 ? 29.299 64.062  53.004 1.00 56.83 ? 774  PRO   B CG  1 
ATOM   5518 C  CD  . PRO   B 1 333 ? 29.970 65.097  52.151 1.00 59.43 ? 774  PRO   B CD  1 
ATOM   5519 N  N   . LEU   B 1 334 ? 26.683 67.686  54.356 1.00 41.51 ? 775  LEU   B N   1 
ATOM   5520 C  CA  . LEU   B 1 334 ? 26.516 68.995  55.008 1.00 35.36 ? 775  LEU   B CA  1 
ATOM   5521 C  C   . LEU   B 1 334 ? 27.329 69.025  56.297 1.00 37.17 ? 775  LEU   B C   1 
ATOM   5522 O  O   . LEU   B 1 334 ? 27.416 68.010  57.007 1.00 40.41 ? 775  LEU   B O   1 
ATOM   5523 C  CB  . LEU   B 1 334 ? 25.055 69.339  55.309 1.00 36.05 ? 775  LEU   B CB  1 
ATOM   5524 C  CG  . LEU   B 1 334 ? 24.446 70.454  54.467 1.00 33.24 ? 775  LEU   B CG  1 
ATOM   5525 C  CD1 . LEU   B 1 334 ? 24.168 69.863  53.111 1.00 33.21 ? 775  LEU   B CD1 1 
ATOM   5526 C  CD2 . LEU   B 1 334 ? 23.173 70.861  55.171 1.00 35.92 ? 775  LEU   B CD2 1 
ATOM   5527 N  N   . LYS   B 1 335 ? 27.860 70.185  56.611 1.00 37.15 ? 776  LYS   B N   1 
ATOM   5528 C  CA  . LYS   B 1 335 ? 28.521 70.360  57.910 1.00 30.55 ? 776  LYS   B CA  1 
ATOM   5529 C  C   . LYS   B 1 335 ? 27.489 70.065  59.003 1.00 35.00 ? 776  LYS   B C   1 
ATOM   5530 O  O   . LYS   B 1 335 ? 26.340 70.471  58.893 1.00 43.78 ? 776  LYS   B O   1 
ATOM   5531 C  CB  . LYS   B 1 335 ? 29.110 71.768  57.968 1.00 30.71 ? 776  LYS   B CB  1 
ATOM   5532 C  CG  . LYS   B 1 335 ? 30.155 71.894  56.870 1.00 30.55 ? 776  LYS   B CG  1 
ATOM   5533 C  CD  . LYS   B 1 335 ? 30.922 73.198  56.746 1.00 31.33 ? 776  LYS   B CD  1 
ATOM   5534 C  CE  . LYS   B 1 335 ? 32.205 72.963  56.006 1.00 28.71 ? 776  LYS   B CE  1 
ATOM   5535 N  NZ  . LYS   B 1 335 ? 32.006 72.354  54.692 1.00 28.38 ? 776  LYS   B NZ  1 
ATOM   5536 N  N   . THR   B 1 336 ? 27.910 69.277  59.977 1.00 34.48 ? 777  THR   B N   1 
ATOM   5537 C  CA  . THR   B 1 336 ? 27.031 68.896  61.078 1.00 37.37 ? 777  THR   B CA  1 
ATOM   5538 C  C   . THR   B 1 336 ? 26.282 70.102  61.635 1.00 34.72 ? 777  THR   B C   1 
ATOM   5539 O  O   . THR   B 1 336 ? 25.078 70.027  61.909 1.00 32.76 ? 777  THR   B O   1 
ATOM   5540 C  CB  . THR   B 1 336 ? 27.858 68.209  62.168 1.00 50.92 ? 777  THR   B CB  1 
ATOM   5541 O  OG1 . THR   B 1 336 ? 28.113 66.849  61.790 1.00 44.80 ? 777  THR   B OG1 1 
ATOM   5542 C  CG2 . THR   B 1 336 ? 27.132 68.233  63.506 1.00 54.41 ? 777  THR   B CG2 1 
ATOM   5543 N  N   . SER   B 1 337 ? 26.975 71.230  61.785 1.00 33.69 ? 778  SER   B N   1 
ATOM   5544 C  CA  . SER   B 1 337 ? 26.342 72.421  62.340 1.00 32.02 ? 778  SER   B CA  1 
ATOM   5545 C  C   . SER   B 1 337 ? 25.224 72.944  61.444 1.00 26.15 ? 778  SER   B C   1 
ATOM   5546 O  O   . SER   B 1 337 ? 24.255 73.534  61.943 1.00 21.69 ? 778  SER   B O   1 
ATOM   5547 C  CB  . SER   B 1 337 ? 27.399 73.501  62.557 1.00 41.31 ? 778  SER   B CB  1 
ATOM   5548 O  OG  . SER   B 1 337 ? 26.925 74.497  63.440 1.00 47.01 ? 778  SER   B OG  1 
ATOM   5549 N  N   . ALA   B 1 338 ? 25.339 72.742  60.129 1.00 22.18 ? 779  ALA   B N   1 
ATOM   5550 C  CA  . ALA   B 1 338 ? 24.305 73.211  59.210 1.00 22.78 ? 779  ALA   B CA  1 
ATOM   5551 C  C   . ALA   B 1 338 ? 23.025 72.397  59.350 1.00 24.24 ? 779  ALA   B C   1 
ATOM   5552 O  O   . ALA   B 1 338 ? 21.919 72.937  59.210 1.00 22.05 ? 779  ALA   B O   1 
ATOM   5553 C  CB  . ALA   B 1 338 ? 24.823 73.153  57.775 1.00 19.92 ? 779  ALA   B CB  1 
ATOM   5554 N  N   . THR   B 1 339 ? 23.157 71.091  59.605 1.00 21.65 ? 780  THR   B N   1 
ATOM   5555 C  CA  . THR   B 1 339 ? 21.989 70.255  59.853 1.00 26.36 ? 780  THR   B CA  1 
ATOM   5556 C  C   . THR   B 1 339 ? 21.264 70.703  61.114 1.00 22.81 ? 780  THR   B C   1 
ATOM   5557 O  O   . THR   B 1 339 ? 20.029 70.759  61.144 1.00 21.36 ? 780  THR   B O   1 
ATOM   5558 C  CB  . THR   B 1 339 ? 22.426 68.793  59.966 1.00 30.32 ? 780  THR   B CB  1 
ATOM   5559 O  OG1 . THR   B 1 339 ? 22.953 68.354  58.707 1.00 34.05 ? 780  THR   B OG1 1 
ATOM   5560 C  CG2 . THR   B 1 339 ? 21.250 67.904  60.359 1.00 31.49 ? 780  THR   B CG2 1 
ATOM   5561 N  N   . VAL   B 1 340 ? 22.018 71.044  62.162 1.00 20.94 ? 781  VAL   B N   1 
ATOM   5562 C  CA  . VAL   B 1 340 ? 21.410 71.566  63.386 1.00 21.70 ? 781  VAL   B CA  1 
ATOM   5563 C  C   . VAL   B 1 340 ? 20.618 72.836  63.093 1.00 22.78 ? 781  VAL   B C   1 
ATOM   5564 O  O   . VAL   B 1 340 ? 19.462 72.973  63.513 1.00 21.26 ? 781  VAL   B O   1 
ATOM   5565 C  CB  . VAL   B 1 340 ? 22.488 71.787  64.464 1.00 24.84 ? 781  VAL   B CB  1 
ATOM   5566 C  CG1 . VAL   B 1 340 ? 21.887 72.445  65.699 1.00 26.01 ? 781  VAL   B CG1 1 
ATOM   5567 C  CG2 . VAL   B 1 340 ? 23.168 70.463  64.826 1.00 23.17 ? 781  VAL   B CG2 1 
ATOM   5568 N  N   . SER   B 1 341 ? 21.223 73.779  62.358 1.00 21.00 ? 782  SER   B N   1 
ATOM   5569 C  CA  . SER   B 1 341 ? 20.533 75.021  62.018 1.00 21.65 ? 782  SER   B CA  1 
ATOM   5570 C  C   . SER   B 1 341 ? 19.233 74.744  61.275 1.00 18.88 ? 782  SER   B C   1 
ATOM   5571 O  O   . SER   B 1 341 ? 18.177 75.277  61.634 1.00 18.60 ? 782  SER   B O   1 
ATOM   5572 C  CB  . SER   B 1 341 ? 21.438 75.913  61.167 1.00 20.52 ? 782  SER   B CB  1 
ATOM   5573 O  OG  . SER   B 1 341 ? 22.542 76.398  61.913 1.00 18.85 ? 782  SER   B OG  1 
ATOM   5574 N  N   . ILE   B 1 342 ? 19.295 73.917  60.230 1.00 16.73 ? 783  ILE   B N   1 
ATOM   5575 C  CA  . ILE   B 1 342 ? 18.109 73.639  59.423 1.00 18.87 ? 783  ILE   B CA  1 
ATOM   5576 C  C   . ILE   B 1 342 ? 17.012 73.026  60.278 1.00 22.19 ? 783  ILE   B C   1 
ATOM   5577 O  O   . ILE   B 1 342 ? 15.838 73.399  60.163 1.00 16.98 ? 783  ILE   B O   1 
ATOM   5578 C  CB  . ILE   B 1 342 ? 18.468 72.755  58.215 1.00 18.56 ? 783  ILE   B CB  1 
ATOM   5579 C  CG1 . ILE   B 1 342 ? 19.348 73.542  57.241 1.00 17.90 ? 783  ILE   B CG1 1 
ATOM   5580 C  CG2 . ILE   B 1 342 ? 17.206 72.235  57.533 1.00 20.37 ? 783  ILE   B CG2 1 
ATOM   5581 C  CD1 . ILE   B 1 342 ? 19.844 72.728  56.051 1.00 20.38 ? 783  ILE   B CD1 1 
ATOM   5582 N  N   . ASN   B 1 343 ? 17.375 72.077  61.148 1.00 22.19 ? 784  ASN   B N   1 
ATOM   5583 C  CA  . ASN   B 1 343 ? 16.379 71.452  62.015 1.00 24.87 ? 784  ASN   B CA  1 
ATOM   5584 C  C   . ASN   B 1 343 ? 15.760 72.463  62.972 1.00 23.76 ? 784  ASN   B C   1 
ATOM   5585 O  O   . ASN   B 1 343 ? 14.550 72.416  63.236 1.00 19.20 ? 784  ASN   B O   1 
ATOM   5586 C  CB  . ASN   B 1 343 ? 16.997 70.287  62.791 1.00 24.75 ? 784  ASN   B CB  1 
ATOM   5587 C  CG  . ASN   B 1 343 ? 17.148 69.042  61.946 1.00 29.64 ? 784  ASN   B CG  1 
ATOM   5588 O  OD1 . ASN   B 1 343 ? 16.455 68.877  60.941 1.00 31.99 ? 784  ASN   B OD1 1 
ATOM   5589 N  ND2 . ASN   B 1 343 ? 18.043 68.148  62.357 1.00 27.07 ? 784  ASN   B ND2 1 
ATOM   5590 N  N   . ASN   B 1 344 ? 16.571 73.388  63.496 1.00 21.48 ? 785  ASN   B N   1 
ATOM   5591 C  CA  . ASN   B 1 344 ? 16.042 74.404  64.403 1.00 22.56 ? 785  ASN   B CA  1 
ATOM   5592 C  C   . ASN   B 1 344 ? 15.032 75.302  63.700 1.00 20.00 ? 785  ASN   B C   1 
ATOM   5593 O  O   . ASN   B 1 344 ? 13.982 75.625  64.269 1.00 19.05 ? 785  ASN   B O   1 
ATOM   5594 C  CB  . ASN   B 1 344 ? 17.175 75.231  65.009 1.00 23.89 ? 785  ASN   B CB  1 
ATOM   5595 C  CG  . ASN   B 1 344 ? 17.929 74.480  66.093 1.00 29.10 ? 785  ASN   B CG  1 
ATOM   5596 O  OD1 . ASN   B 1 344 ? 17.372 73.603  66.752 1.00 31.93 ? 785  ASN   B OD1 1 
ATOM   5597 N  ND2 . ASN   B 1 344 ? 19.191 74.840  66.302 1.00 26.46 ? 785  ASN   B ND2 1 
ATOM   5598 N  N   . VAL   B 1 345 ? 15.329 75.717  62.464 1.00 18.46 ? 786  VAL   B N   1 
ATOM   5599 C  CA  . VAL   B 1 345 ? 14.371 76.521  61.715 1.00 18.30 ? 786  VAL   B CA  1 
ATOM   5600 C  C   . VAL   B 1 345 ? 13.118 75.710  61.409 1.00 19.92 ? 786  VAL   B C   1 
ATOM   5601 O  O   . VAL   B 1 345 ? 11.991 76.216  61.517 1.00 17.29 ? 786  VAL   B O   1 
ATOM   5602 C  CB  . VAL   B 1 345 ? 15.013 77.092  60.438 1.00 18.04 ? 786  VAL   B CB  1 
ATOM   5603 C  CG1 . VAL   B 1 345 ? 14.029 78.027  59.741 1.00 19.01 ? 786  VAL   B CG1 1 
ATOM   5604 C  CG2 . VAL   B 1 345 ? 16.321 77.808  60.752 1.00 17.68 ? 786  VAL   B CG2 1 
ATOM   5605 N  N   . LEU   B 1 346 ? 13.293 74.447  61.007 1.00 22.14 ? 787  LEU   B N   1 
ATOM   5606 C  CA  . LEU   B 1 346 ? 12.145 73.593  60.706 1.00 23.45 ? 787  LEU   B CA  1 
ATOM   5607 C  C   . LEU   B 1 346 ? 11.217 73.482  61.906 1.00 22.79 ? 787  LEU   B C   1 
ATOM   5608 O  O   . LEU   B 1 346 ? 9.994  73.607  61.771 1.00 22.87 ? 787  LEU   B O   1 
ATOM   5609 C  CB  . LEU   B 1 346 ? 12.622 72.207  60.273 1.00 25.07 ? 787  LEU   B CB  1 
ATOM   5610 C  CG  . LEU   B 1 346 ? 13.067 72.056  58.816 1.00 26.99 ? 787  LEU   B CG  1 
ATOM   5611 C  CD1 . LEU   B 1 346 ? 13.720 70.701  58.581 1.00 29.25 ? 787  LEU   B CD1 1 
ATOM   5612 C  CD2 . LEU   B 1 346 ? 11.880 72.233  57.880 1.00 29.36 ? 787  LEU   B CD2 1 
ATOM   5613 N  N   . ARG   B 1 347 ? 11.789 73.259  63.090 1.00 21.83 ? 788  ARG   B N   1 
ATOM   5614 C  CA  . ARG   B 1 347 ? 10.985 73.103  64.297 1.00 26.89 ? 788  ARG   B CA  1 
ATOM   5615 C  C   . ARG   B 1 347 ? 10.344 74.421  64.713 1.00 29.19 ? 788  ARG   B C   1 
ATOM   5616 O  O   . ARG   B 1 347 ? 9.230  74.425  65.254 1.00 26.91 ? 788  ARG   B O   1 
ATOM   5617 C  CB  . ARG   B 1 347 ? 11.853 72.540  65.424 1.00 33.79 ? 788  ARG   B CB  1 
ATOM   5618 C  CG  . ARG   B 1 347 ? 11.781 71.022  65.575 1.00 41.45 ? 788  ARG   B CG  1 
ATOM   5619 C  CD  . ARG   B 1 347 ? 13.131 70.411  65.934 1.00 51.56 ? 788  ARG   B CD  1 
ATOM   5620 N  NE  . ARG   B 1 347 ? 13.363 69.145  65.240 1.00 52.97 ? 788  ARG   B NE  1 
ATOM   5621 C  CZ  . ARG   B 1 347 ? 14.366 68.314  65.511 1.00 49.02 ? 788  ARG   B CZ  1 
ATOM   5622 N  NH1 . ARG   B 1 347 ? 15.243 68.613  66.460 1.00 48.61 ? 788  ARG   B NH1 1 
ATOM   5623 N  NH2 . ARG   B 1 347 ? 14.498 67.187  64.828 1.00 49.63 ? 788  ARG   B NH2 1 
ATOM   5624 N  N   . ALA   B 1 348 ? 11.022 75.543  64.458 1.00 28.40 ? 789  ALA   B N   1 
ATOM   5625 C  CA  . ALA   B 1 348 ? 10.461 76.852  64.776 1.00 25.00 ? 789  ALA   B CA  1 
ATOM   5626 C  C   . ALA   B 1 348 ? 9.286  77.212  63.872 1.00 20.81 ? 789  ALA   B C   1 
ATOM   5627 O  O   . ALA   B 1 348 ? 8.346  77.877  64.318 1.00 19.20 ? 789  ALA   B O   1 
ATOM   5628 C  CB  . ALA   B 1 348 ? 11.545 77.924  64.663 1.00 21.93 ? 789  ALA   B CB  1 
ATOM   5629 N  N   . HIS   B 1 349 ? 9.312  76.790  62.608 1.00 17.45 ? 790  HIS   B N   1 
ATOM   5630 C  CA  . HIS   B 1 349 ? 8.339  77.263  61.638 1.00 19.47 ? 790  HIS   B CA  1 
ATOM   5631 C  C   . HIS   B 1 349 ? 7.290  76.245  61.223 1.00 24.25 ? 790  HIS   B C   1 
ATOM   5632 O  O   . HIS   B 1 349 ? 6.280  76.643  60.629 1.00 18.53 ? 790  HIS   B O   1 
ATOM   5633 C  CB  . HIS   B 1 349 ? 9.036  77.853  60.407 1.00 16.76 ? 790  HIS   B CB  1 
ATOM   5634 C  CG  . HIS   B 1 349 ? 9.449  79.270  60.613 1.00 18.38 ? 790  HIS   B CG  1 
ATOM   5635 N  ND1 . HIS   B 1 349 ? 8.570  80.320  60.466 1.00 17.79 ? 790  HIS   B ND1 1 
ATOM   5636 C  CD2 . HIS   B 1 349 ? 10.627 79.810  61.004 1.00 17.67 ? 790  HIS   B CD2 1 
ATOM   5637 C  CE1 . HIS   B 1 349 ? 9.194  81.451  60.744 1.00 17.84 ? 790  HIS   B CE1 1 
ATOM   5638 N  NE2 . HIS   B 1 349 ? 10.443 81.170  61.070 1.00 16.28 ? 790  HIS   B NE2 1 
ATOM   5639 N  N   . ALA   B 1 350 ? 7.491  74.965  61.515 1.00 28.67 ? 791  ALA   B N   1 
ATOM   5640 C  CA  . ALA   B 1 350 ? 6.437  73.976  61.306 1.00 31.28 ? 791  ALA   B CA  1 
ATOM   5641 C  C   . ALA   B 1 350 ? 5.087  74.371  61.902 1.00 29.53 ? 791  ALA   B C   1 
ATOM   5642 O  O   . ALA   B 1 350 ? 4.059  74.057  61.279 1.00 27.32 ? 791  ALA   B O   1 
ATOM   5643 C  CB  . ALA   B 1 350 ? 6.902  72.596  61.794 1.00 35.01 ? 791  ALA   B CB  1 
ATOM   5644 N  N   . PRO   B 1 351 ? 5.002  75.035  63.061 1.00 25.84 ? 792  PRO   B N   1 
ATOM   5645 C  CA  . PRO   B 1 351 ? 3.683  75.502  63.523 1.00 27.99 ? 792  PRO   B CA  1 
ATOM   5646 C  C   . PRO   B 1 351 ? 2.972  76.411  62.538 1.00 26.12 ? 792  PRO   B C   1 
ATOM   5647 O  O   . PRO   B 1 351 ? 1.734  76.426  62.511 1.00 30.34 ? 792  PRO   B O   1 
ATOM   5648 C  CB  . PRO   B 1 351 ? 4.001  76.241  64.829 1.00 25.85 ? 792  PRO   B CB  1 
ATOM   5649 C  CG  . PRO   B 1 351 ? 5.262  75.649  65.314 1.00 26.27 ? 792  PRO   B CG  1 
ATOM   5650 C  CD  . PRO   B 1 351 ? 6.030  75.168  64.113 1.00 25.18 ? 792  PRO   B CD  1 
ATOM   5651 N  N   . PHE   B 1 352 ? 3.710  77.171  61.722 1.00 21.41 ? 793  PHE   B N   1 
ATOM   5652 C  CA  . PHE   B 1 352 ? 3.089  78.161  60.852 1.00 21.05 ? 793  PHE   B CA  1 
ATOM   5653 C  C   . PHE   B 1 352 ? 2.977  77.734  59.397 1.00 25.88 ? 793  PHE   B C   1 
ATOM   5654 O  O   . PHE   B 1 352 ? 2.177  78.324  58.661 1.00 25.76 ? 793  PHE   B O   1 
ATOM   5655 C  CB  . PHE   B 1 352 ? 3.845  79.491  60.920 1.00 20.40 ? 793  PHE   B CB  1 
ATOM   5656 C  CG  . PHE   B 1 352 ? 4.174  79.920  62.315 1.00 20.15 ? 793  PHE   B CG  1 
ATOM   5657 C  CD1 . PHE   B 1 352 ? 3.181  80.414  63.142 1.00 21.87 ? 793  PHE   B CD1 1 
ATOM   5658 C  CD2 . PHE   B 1 352 ? 5.462  79.825  62.809 1.00 21.46 ? 793  PHE   B CD2 1 
ATOM   5659 C  CE1 . PHE   B 1 352 ? 3.468  80.807  64.441 1.00 22.27 ? 793  PHE   B CE1 1 
ATOM   5660 C  CE2 . PHE   B 1 352 ? 5.758  80.223  64.102 1.00 23.00 ? 793  PHE   B CE2 1 
ATOM   5661 C  CZ  . PHE   B 1 352 ? 4.754  80.711  64.924 1.00 23.08 ? 793  PHE   B CZ  1 
ATOM   5662 N  N   . TRP   B 1 353 ? 3.741  76.732  58.969 1.00 26.12 ? 794  TRP   B N   1 
ATOM   5663 C  CA  . TRP   B 1 353 ? 3.818  76.335  57.566 1.00 25.11 ? 794  TRP   B CA  1 
ATOM   5664 C  C   . TRP   B 1 353 ? 3.602  74.830  57.495 1.00 26.40 ? 794  TRP   B C   1 
ATOM   5665 O  O   . TRP   B 1 353 ? 4.487  74.057  57.867 1.00 23.83 ? 794  TRP   B O   1 
ATOM   5666 C  CB  . TRP   B 1 353 ? 5.176  76.733  56.980 1.00 20.42 ? 794  TRP   B CB  1 
ATOM   5667 C  CG  . TRP   B 1 353 ? 5.414  78.207  57.095 1.00 17.47 ? 794  TRP   B CG  1 
ATOM   5668 C  CD1 . TRP   B 1 353 ? 6.159  78.848  58.040 1.00 16.44 ? 794  TRP   B CD1 1 
ATOM   5669 C  CD2 . TRP   B 1 353 ? 4.860  79.224  56.256 1.00 18.78 ? 794  TRP   B CD2 1 
ATOM   5670 N  NE1 . TRP   B 1 353 ? 6.113  80.210  57.829 1.00 16.21 ? 794  TRP   B NE1 1 
ATOM   5671 C  CE2 . TRP   B 1 353 ? 5.327  80.464  56.738 1.00 19.23 ? 794  TRP   B CE2 1 
ATOM   5672 C  CE3 . TRP   B 1 353 ? 4.023  79.203  55.134 1.00 21.07 ? 794  TRP   B CE3 1 
ATOM   5673 C  CZ2 . TRP   B 1 353 ? 4.981  81.675  56.140 1.00 21.71 ? 794  TRP   B CZ2 1 
ATOM   5674 C  CZ3 . TRP   B 1 353 ? 3.684  80.404  54.535 1.00 23.03 ? 794  TRP   B CZ3 1 
ATOM   5675 C  CH2 . TRP   B 1 353 ? 4.164  81.627  55.042 1.00 23.04 ? 794  TRP   B CH2 1 
ATOM   5676 N  N   . SER   B 1 354 ? 2.427  74.416  57.013 1.00 26.57 ? 795  SER   B N   1 
ATOM   5677 C  CA  A SER   B 1 354 ? 2.097  72.995  56.969 0.22 31.89 ? 795  SER   B CA  1 
ATOM   5678 C  CA  B SER   B 1 354 ? 2.103  72.993  56.976 0.78 30.61 ? 795  SER   B CA  1 
ATOM   5679 C  C   . SER   B 1 354 ? 3.023  72.210  56.051 1.00 35.23 ? 795  SER   B C   1 
ATOM   5680 O  O   . SER   B 1 354 ? 3.178  70.998  56.233 1.00 39.82 ? 795  SER   B O   1 
ATOM   5681 C  CB  A SER   B 1 354 ? 0.641  72.805  56.539 0.22 31.39 ? 795  SER   B CB  1 
ATOM   5682 C  CB  B SER   B 1 354 ? 0.639  72.782  56.583 0.78 30.27 ? 795  SER   B CB  1 
ATOM   5683 O  OG  A SER   B 1 354 ? -0.250 73.281  57.534 0.22 31.19 ? 795  SER   B OG  1 
ATOM   5684 O  OG  B SER   B 1 354 ? 0.378  73.268  55.280 0.78 27.82 ? 795  SER   B OG  1 
ATOM   5685 N  N   . SER   B 1 355 ? 3.642  72.871  55.070 1.00 34.98 ? 796  SER   B N   1 
ATOM   5686 C  CA  . SER   B 1 355 ? 4.559  72.192  54.163 1.00 35.16 ? 796  SER   B CA  1 
ATOM   5687 C  C   . SER   B 1 355 ? 5.816  71.679  54.858 1.00 34.61 ? 796  SER   B C   1 
ATOM   5688 O  O   . SER   B 1 355 ? 6.542  70.872  54.267 1.00 35.91 ? 796  SER   B O   1 
ATOM   5689 C  CB  . SER   B 1 355 ? 4.950  73.130  53.018 1.00 34.46 ? 796  SER   B CB  1 
ATOM   5690 O  OG  . SER   B 1 355 ? 5.764  74.192  53.493 1.00 32.45 ? 796  SER   B OG  1 
ATOM   5691 N  N   . LEU   B 1 356 ? 6.099  72.128  56.079 1.00 34.20 ? 797  LEU   B N   1 
ATOM   5692 C  CA  . LEU   B 1 356 ? 7.289  71.709  56.807 1.00 37.34 ? 797  LEU   B CA  1 
ATOM   5693 C  C   . LEU   B 1 356 ? 7.036  70.532  57.737 1.00 39.90 ? 797  LEU   B C   1 
ATOM   5694 O  O   . LEU   B 1 356 ? 7.976  70.057  58.382 1.00 38.08 ? 797  LEU   B O   1 
ATOM   5695 C  CB  . LEU   B 1 356 ? 7.850  72.874  57.626 1.00 32.20 ? 797  LEU   B CB  1 
ATOM   5696 C  CG  . LEU   B 1 356 ? 8.171  74.159  56.868 1.00 32.34 ? 797  LEU   B CG  1 
ATOM   5697 C  CD1 . LEU   B 1 356 ? 8.714  75.201  57.830 1.00 30.18 ? 797  LEU   B CD1 1 
ATOM   5698 C  CD2 . LEU   B 1 356 ? 9.159  73.883  55.742 1.00 32.31 ? 797  LEU   B CD2 1 
ATOM   5699 N  N   . ARG   B 1 357 ? 5.800  70.056  57.821 1.00 46.23 ? 798  ARG   B N   1 
ATOM   5700 C  CA  . ARG   B 1 357 ? 5.450  69.005  58.764 1.00 49.14 ? 798  ARG   B CA  1 
ATOM   5701 C  C   . ARG   B 1 357 ? 5.667  67.618  58.166 1.00 55.74 ? 798  ARG   B C   1 
ATOM   5702 O  O   . ARG   B 1 357 ? 5.872  66.641  58.890 1.00 57.48 ? 798  ARG   B O   1 
ATOM   5703 C  CB  . ARG   B 1 357 ? 3.998  69.169  59.204 1.00 45.07 ? 798  ARG   B CB  1 
ATOM   5704 C  CG  . ARG   B 1 357 ? 3.778  70.357  60.117 1.00 42.12 ? 798  ARG   B CG  1 
ATOM   5705 C  CD  . ARG   B 1 357 ? 2.368  70.902  60.009 1.00 43.44 ? 798  ARG   B CD  1 
ATOM   5706 N  NE  . ARG   B 1 357 ? 1.985  71.654  61.199 1.00 49.90 ? 798  ARG   B NE  1 
ATOM   5707 C  CZ  . ARG   B 1 357 ? 0.982  72.524  61.244 1.00 57.67 ? 798  ARG   B CZ  1 
ATOM   5708 N  NH1 . ARG   B 1 357 ? 0.259  72.758  60.158 1.00 60.90 ? 798  ARG   B NH1 1 
ATOM   5709 N  NH2 . ARG   B 1 357 ? 0.699  73.159  62.374 1.00 57.69 ? 798  ARG   B NH2 1 
ATOM   5710 O  OXT . ARG   B 1 357 ? 5.644  67.442  56.946 1.00 57.90 ? 798  ARG   B OXT 1 
HETATM 5711 C  C13 . A1BH9 C 2 .   ? 35.184 51.307  33.760 1.00 34.28 ? 801  A1BH9 A C13 1 
HETATM 5712 C  C17 . A1BH9 C 2 .   ? 36.689 51.054  33.684 1.00 32.49 ? 801  A1BH9 A C17 1 
HETATM 5713 C  C20 . A1BH9 C 2 .   ? 32.132 47.791  34.195 1.00 25.67 ? 801  A1BH9 A C20 1 
HETATM 5714 C  C21 . A1BH9 C 2 .   ? 31.268 47.265  33.250 1.00 26.30 ? 801  A1BH9 A C21 1 
HETATM 5715 C  C24 . A1BH9 C 2 .   ? 32.880 45.582  34.617 1.00 25.81 ? 801  A1BH9 A C24 1 
HETATM 5716 C  C26 . A1BH9 C 2 .   ? 30.915 49.545  30.933 1.00 21.96 ? 801  A1BH9 A C26 1 
HETATM 5717 C  C02 . A1BH9 C 2 .   ? 27.760 48.516  29.085 1.00 26.07 ? 801  A1BH9 A C02 1 
HETATM 5718 C  C05 . A1BH9 C 2 .   ? 28.695 49.235  30.069 1.00 21.17 ? 801  A1BH9 A C05 1 
HETATM 5719 C  C06 . A1BH9 C 2 .   ? 28.226 50.101  31.032 1.00 21.80 ? 801  A1BH9 A C06 1 
HETATM 5720 C  C07 . A1BH9 C 2 .   ? 29.097 50.693  31.934 1.00 22.60 ? 801  A1BH9 A C07 1 
HETATM 5721 C  C08 . A1BH9 C 2 .   ? 30.446 50.411  31.893 1.00 21.42 ? 801  A1BH9 A C08 1 
HETATM 5722 C  C09 . A1BH9 C 2 .   ? 31.406 51.071  32.881 1.00 23.55 ? 801  A1BH9 A C09 1 
HETATM 5723 C  C14 . A1BH9 C 2 .   ? 34.849 52.333  34.673 1.00 39.56 ? 801  A1BH9 A C14 1 
HETATM 5724 C  C16 . A1BH9 C 2 .   ? 37.358 51.924  34.584 1.00 33.20 ? 801  A1BH9 A C16 1 
HETATM 5725 C  C19 . A1BH9 C 2 .   ? 32.196 49.292  34.500 1.00 24.63 ? 801  A1BH9 A C19 1 
HETATM 5726 C  C23 . A1BH9 C 2 .   ? 31.999 45.147  33.653 1.00 26.33 ? 801  A1BH9 A C23 1 
HETATM 5727 C  C25 . A1BH9 C 2 .   ? 32.947 46.927  34.900 1.00 25.70 ? 801  A1BH9 A C25 1 
HETATM 5728 C  C27 . A1BH9 C 2 .   ? 30.043 48.954  30.041 1.00 20.14 ? 801  A1BH9 A C27 1 
HETATM 5729 N  N03 . A1BH9 C 2 .   ? 26.373 48.335  29.387 1.00 29.20 ? 801  A1BH9 A N03 1 
HETATM 5730 N  N10 . A1BH9 C 2 .   ? 32.439 50.164  33.350 1.00 25.34 ? 801  A1BH9 A N10 1 
HETATM 5731 N  N22 . A1BH9 C 2 .   ? 31.232 45.988  33.003 1.00 26.18 ? 801  A1BH9 A N22 1 
HETATM 5732 O  O01 . A1BH9 C 2 .   ? 28.118 47.989  28.125 1.00 24.25 ? 801  A1BH9 A O01 1 
HETATM 5733 O  O04 . A1BH9 C 2 .   ? 25.460 47.646  28.582 1.00 28.27 ? 801  A1BH9 A O04 1 
HETATM 5734 O  O12 . A1BH9 C 2 .   ? 34.045 50.963  31.432 1.00 30.17 ? 801  A1BH9 A O12 1 
HETATM 5735 O  O18 . A1BH9 C 2 .   ? 34.639 49.117  32.517 1.00 33.62 ? 801  A1BH9 A O18 1 
HETATM 5736 S  S11 . A1BH9 C 2 .   ? 34.020 50.401  32.758 1.00 30.86 ? 801  A1BH9 A S11 1 
HETATM 5737 S  S15 . A1BH9 C 2 .   ? 36.238 52.824  35.301 1.00 38.32 ? 801  A1BH9 A S15 1 
HETATM 5738 ZN ZN  . ZN    D 3 .   ? 26.643 46.118  28.100 1.00 18.08 ? 802  ZN    A ZN  1 
HETATM 5739 K  K   . K     E 4 .   ? 7.484  43.991  32.306 1.00 20.26 1 803  K     A K   1 
HETATM 5740 C  C13 . A1BH9 F 2 .   ? 34.570 96.640  60.472 1.00 38.93 ? 801  A1BH9 B C13 1 
HETATM 5741 C  C17 . A1BH9 F 2 .   ? 35.770 96.095  61.230 1.00 40.74 ? 801  A1BH9 B C17 1 
HETATM 5742 C  C20 . A1BH9 F 2 .   ? 32.035 93.227  59.843 1.00 19.38 ? 801  A1BH9 B C20 1 
HETATM 5743 C  C21 . A1BH9 F 2 .   ? 31.184 92.663  58.900 1.00 19.24 ? 801  A1BH9 B C21 1 
HETATM 5744 C  C24 . A1BH9 F 2 .   ? 33.099 91.105  60.048 1.00 22.45 ? 801  A1BH9 B C24 1 
HETATM 5745 C  C26 . A1BH9 F 2 .   ? 30.880 95.122  56.656 1.00 20.42 ? 801  A1BH9 B C26 1 
HETATM 5746 C  C02 . A1BH9 F 2 .   ? 27.745 94.130  54.730 1.00 25.40 ? 801  A1BH9 B C02 1 
HETATM 5747 C  C05 . A1BH9 F 2 .   ? 28.677 94.812  55.744 1.00 21.01 ? 801  A1BH9 B C05 1 
HETATM 5748 C  C06 . A1BH9 F 2 .   ? 28.167 95.655  56.727 1.00 21.35 ? 801  A1BH9 B C06 1 
HETATM 5749 C  C07 . A1BH9 F 2 .   ? 29.014 96.236  57.674 1.00 21.37 ? 801  A1BH9 B C07 1 
HETATM 5750 C  C08 . A1BH9 F 2 .   ? 30.376 95.967  57.632 1.00 21.41 ? 801  A1BH9 B C08 1 
HETATM 5751 C  C09 . A1BH9 F 2 .   ? 31.324 96.594  58.650 1.00 23.30 ? 801  A1BH9 B C09 1 
HETATM 5752 C  C14 . A1BH9 F 2 .   ? 34.028 97.784  61.140 1.00 45.19 ? 801  A1BH9 B C14 1 
HETATM 5753 C  C16 . A1BH9 F 2 .   ? 36.012 96.905  62.386 1.00 45.37 ? 801  A1BH9 B C16 1 
HETATM 5754 C  C19 . A1BH9 F 2 .   ? 31.886 94.697  60.231 1.00 21.19 ? 801  A1BH9 B C19 1 
HETATM 5755 C  C23 . A1BH9 F 2 .   ? 32.219 90.612  59.095 1.00 20.24 ? 801  A1BH9 B C23 1 
HETATM 5756 C  C25 . A1BH9 F 2 .   ? 33.007 92.436  60.438 1.00 22.03 ? 801  A1BH9 B C25 1 
HETATM 5757 C  C27 . A1BH9 F 2 .   ? 30.035 94.539  55.723 1.00 19.53 ? 801  A1BH9 B C27 1 
HETATM 5758 N  N03 . A1BH9 F 2 .   ? 26.345 94.007  55.056 1.00 28.97 ? 801  A1BH9 B N03 1 
HETATM 5759 N  N10 . A1BH9 F 2 .   ? 32.257 95.576  59.127 1.00 22.61 ? 801  A1BH9 B N10 1 
HETATM 5760 N  N22 . A1BH9 F 2 .   ? 31.298 91.398  58.561 1.00 17.91 ? 801  A1BH9 B N22 1 
HETATM 5761 O  O01 . A1BH9 F 2 .   ? 28.118 93.625  53.737 1.00 24.68 ? 801  A1BH9 B O01 1 
HETATM 5762 O  O04 . A1BH9 F 2 .   ? 25.406 93.372  54.221 1.00 28.75 ? 801  A1BH9 B O04 1 
HETATM 5763 O  O12 . A1BH9 F 2 .   ? 34.146 96.706  57.743 1.00 33.40 ? 801  A1BH9 B O12 1 
HETATM 5764 O  O18 . A1BH9 F 2 .   ? 34.656 94.670  58.646 1.00 31.53 ? 801  A1BH9 B O18 1 
HETATM 5765 S  S11 . A1BH9 F 2 .   ? 33.919 95.905  58.948 1.00 30.20 ? 801  A1BH9 B S11 1 
HETATM 5766 S  S15 . A1BH9 F 2 .   ? 34.918 98.094  62.466 1.00 49.61 ? 801  A1BH9 B S15 1 
HETATM 5767 ZN ZN  . ZN    G 3 .   ? 26.615 91.705  53.725 1.00 17.10 ? 802  ZN    B ZN  1 
HETATM 5768 K  K   . K     H 4 .   ? 7.371  89.698  57.821 0.94 18.06 1 803  K     B K   1 
HETATM 5769 O  O   . HOH   I 5 .   ? 37.708 62.835  22.678 1.00 35.83 ? 901  HOH   A O   1 
HETATM 5770 O  O   . HOH   I 5 .   ? 29.533 63.907  11.133 1.00 40.02 ? 902  HOH   A O   1 
HETATM 5771 O  O   . HOH   I 5 .   ? 29.293 38.434  9.543  1.00 42.20 ? 903  HOH   A O   1 
HETATM 5772 O  O   . HOH   I 5 .   ? 19.607 71.431  23.528 1.00 23.86 ? 904  HOH   A O   1 
HETATM 5773 O  O   . HOH   I 5 .   ? 30.358 66.207  39.823 1.00 39.52 ? 905  HOH   A O   1 
HETATM 5774 O  O   . HOH   I 5 .   ? 12.138 63.906  38.525 1.00 39.40 ? 906  HOH   A O   1 
HETATM 5775 O  O   . HOH   I 5 .   ? 20.362 38.866  48.674 1.00 22.04 ? 907  HOH   A O   1 
HETATM 5776 O  O   . HOH   I 5 .   ? 32.420 33.826  36.114 1.00 39.30 ? 908  HOH   A O   1 
HETATM 5777 O  O   . HOH   I 5 .   ? 0.500  49.581  27.688 1.00 27.42 ? 909  HOH   A O   1 
HETATM 5778 O  O   . HOH   I 5 .   ? 20.725 60.454  7.803  1.00 34.35 ? 910  HOH   A O   1 
HETATM 5779 O  O   . HOH   I 5 .   ? 4.350  56.609  28.766 1.00 44.20 ? 911  HOH   A O   1 
HETATM 5780 O  O   . HOH   I 5 .   ? 39.557 51.474  25.743 1.00 43.68 ? 912  HOH   A O   1 
HETATM 5781 O  O   . HOH   I 5 .   ? 17.550 49.596  42.440 1.00 36.15 ? 913  HOH   A O   1 
HETATM 5782 O  O   . HOH   I 5 .   ? 23.480 60.685  40.057 1.00 37.67 ? 914  HOH   A O   1 
HETATM 5783 O  O   . HOH   I 5 .   ? 4.848  62.473  25.977 1.00 37.87 ? 915  HOH   A O   1 
HETATM 5784 O  O   . HOH   I 5 .   ? 21.100 41.839  29.142 1.00 5.44  ? 916  HOH   A O   1 
HETATM 5785 O  O   . HOH   I 5 .   ? 33.996 50.699  4.628  1.00 33.32 ? 917  HOH   A O   1 
HETATM 5786 O  O   . HOH   I 5 .   ? 25.378 41.747  38.984 1.00 26.96 ? 918  HOH   A O   1 
HETATM 5787 O  O   . HOH   I 5 .   ? 25.978 40.403  23.965 1.00 16.03 ? 919  HOH   A O   1 
HETATM 5788 O  O   . HOH   I 5 .   ? 15.756 24.910  20.574 1.00 37.18 ? 920  HOH   A O   1 
HETATM 5789 O  O   . HOH   I 5 .   ? 2.902  31.816  20.054 1.00 41.68 ? 921  HOH   A O   1 
HETATM 5790 O  O   . HOH   I 5 .   ? 15.464 43.919  2.061  1.00 21.66 ? 922  HOH   A O   1 
HETATM 5791 O  O   . HOH   I 5 .   ? 35.227 39.884  10.921 1.00 39.98 ? 923  HOH   A O   1 
HETATM 5792 O  O   . HOH   I 5 .   ? 23.731 38.490  27.693 1.00 16.82 ? 924  HOH   A O   1 
HETATM 5793 O  O   . HOH   I 5 .   ? 34.862 46.947  7.491  1.00 18.11 ? 925  HOH   A O   1 
HETATM 5794 O  O   . HOH   I 5 .   ? 20.438 53.974  21.693 1.00 16.21 ? 926  HOH   A O   1 
HETATM 5795 O  O   . HOH   I 5 .   ? -0.031 41.178  40.862 1.00 30.64 ? 927  HOH   A O   1 
HETATM 5796 O  O   . HOH   I 5 .   ? 22.369 58.962  38.833 1.00 26.69 ? 928  HOH   A O   1 
HETATM 5797 O  O   . HOH   I 5 .   ? 13.403 54.209  36.174 1.00 23.32 ? 929  HOH   A O   1 
HETATM 5798 O  O   . HOH   I 5 .   ? 11.804 38.389  10.649 1.00 19.70 ? 930  HOH   A O   1 
HETATM 5799 O  O   . HOH   I 5 .   ? -1.218 43.919  26.418 1.00 29.86 ? 931  HOH   A O   1 
HETATM 5800 O  O   . HOH   I 5 .   ? 19.546 55.440  7.966  1.00 18.95 ? 932  HOH   A O   1 
HETATM 5801 O  O   . HOH   I 5 .   ? 20.016 47.475  -3.660 1.00 32.18 ? 933  HOH   A O   1 
HETATM 5802 O  O   . HOH   I 5 .   ? 30.073 56.028  8.229  1.00 22.44 ? 934  HOH   A O   1 
HETATM 5803 O  O   . HOH   I 5 .   ? 30.694 28.285  27.427 1.00 27.93 ? 935  HOH   A O   1 
HETATM 5804 O  O   . HOH   I 5 .   ? 36.144 49.842  22.324 1.00 35.46 ? 936  HOH   A O   1 
HETATM 5805 O  O   . HOH   I 5 .   ? 15.130 69.471  22.403 1.00 22.94 ? 937  HOH   A O   1 
HETATM 5806 O  O   . HOH   I 5 .   ? 23.765 57.091  37.301 1.00 19.64 ? 938  HOH   A O   1 
HETATM 5807 O  O   . HOH   I 5 .   ? 24.836 42.832  34.667 1.00 17.28 ? 939  HOH   A O   1 
HETATM 5808 O  O   . HOH   I 5 .   ? 33.609 75.436  41.948 1.00 40.37 ? 940  HOH   A O   1 
HETATM 5809 O  O   . HOH   I 5 .   ? 33.470 61.968  17.321 1.00 38.04 ? 941  HOH   A O   1 
HETATM 5810 O  O   . HOH   I 5 .   ? 32.474 34.369  12.254 1.00 32.43 ? 942  HOH   A O   1 
HETATM 5811 O  O   . HOH   I 5 .   ? 17.086 33.735  8.283  1.00 22.07 ? 943  HOH   A O   1 
HETATM 5812 O  O   . HOH   I 5 .   ? 16.695 46.622  27.287 1.00 16.01 ? 944  HOH   A O   1 
HETATM 5813 O  O   . HOH   I 5 .   ? 6.336  64.633  19.220 1.00 25.58 ? 945  HOH   A O   1 
HETATM 5814 O  O   . HOH   I 5 .   ? 32.636 42.974  21.640 1.00 15.14 ? 946  HOH   A O   1 
HETATM 5815 O  O   . HOH   I 5 .   ? 23.665 67.930  21.856 1.00 20.36 ? 947  HOH   A O   1 
HETATM 5816 O  O   . HOH   I 5 .   ? 8.605  57.855  13.553 1.00 21.21 ? 948  HOH   A O   1 
HETATM 5817 O  O   . HOH   I 5 .   ? 19.240 52.322  38.868 1.00 40.74 ? 949  HOH   A O   1 
HETATM 5818 O  O   . HOH   I 5 .   ? 5.368  60.557  18.205 1.00 26.69 ? 950  HOH   A O   1 
HETATM 5819 O  O   . HOH   I 5 .   ? 22.325 37.727  44.629 1.00 36.93 ? 951  HOH   A O   1 
HETATM 5820 O  O   . HOH   I 5 .   ? 28.069 56.812  25.782 1.00 14.57 ? 952  HOH   A O   1 
HETATM 5821 O  O   . HOH   I 5 .   ? 8.826  29.800  17.866 1.00 34.00 ? 953  HOH   A O   1 
HETATM 5822 O  O   . HOH   I 5 .   ? 37.119 58.294  17.826 1.00 33.94 ? 954  HOH   A O   1 
HETATM 5823 O  O   . HOH   I 5 .   ? 22.741 44.626  38.553 1.00 18.22 ? 955  HOH   A O   1 
HETATM 5824 O  O   . HOH   I 5 .   ? 24.678 41.640  -2.026 1.00 36.13 ? 956  HOH   A O   1 
HETATM 5825 O  O   . HOH   I 5 .   ? 36.498 47.094  2.933  1.00 18.72 ? 957  HOH   A O   1 
HETATM 5826 O  O   . HOH   I 5 .   ? 27.756 22.703  17.235 1.00 25.84 ? 958  HOH   A O   1 
HETATM 5827 O  O   . HOH   I 5 .   ? 17.231 42.173  -0.383 1.00 39.09 ? 959  HOH   A O   1 
HETATM 5828 O  O   . HOH   I 5 .   ? 28.189 50.376  39.794 1.00 34.20 ? 960  HOH   A O   1 
HETATM 5829 O  O   . HOH   I 5 .   ? 32.631 69.229  20.961 1.00 38.04 ? 961  HOH   A O   1 
HETATM 5830 O  O   . HOH   I 5 .   ? 25.371 51.875  21.124 1.00 14.79 ? 962  HOH   A O   1 
HETATM 5831 O  O   . HOH   I 5 .   ? 7.166  43.093  34.867 1.00 17.14 ? 963  HOH   A O   1 
HETATM 5832 O  O   . HOH   I 5 .   ? 11.609 68.868  30.034 1.00 32.52 ? 964  HOH   A O   1 
HETATM 5833 O  O   . HOH   I 5 .   ? 17.679 51.012  25.202 1.00 15.43 ? 965  HOH   A O   1 
HETATM 5834 O  O   . HOH   I 5 .   ? 34.215 46.875  10.234 1.00 14.87 ? 966  HOH   A O   1 
HETATM 5835 O  O   . HOH   I 5 .   ? 8.213  48.901  1.384  1.00 30.59 ? 967  HOH   A O   1 
HETATM 5836 O  O   . HOH   I 5 .   ? 20.371 48.294  43.832 1.00 37.92 ? 968  HOH   A O   1 
HETATM 5837 O  O   . HOH   I 5 .   ? 6.490  52.915  32.450 1.00 26.04 ? 969  HOH   A O   1 
HETATM 5838 O  O   . HOH   I 5 .   ? 26.838 63.707  7.953  1.00 32.76 ? 970  HOH   A O   1 
HETATM 5839 O  O   . HOH   I 5 .   ? 3.174  54.444  5.981  1.00 42.05 ? 971  HOH   A O   1 
HETATM 5840 O  O   . HOH   I 5 .   ? 19.329 63.460  35.160 1.00 25.00 ? 972  HOH   A O   1 
HETATM 5841 O  O   . HOH   I 5 .   ? 7.886  63.459  31.505 1.00 37.72 ? 973  HOH   A O   1 
HETATM 5842 O  O   . HOH   I 5 .   ? 30.818 37.111  18.622 1.00 17.66 ? 974  HOH   A O   1 
HETATM 5843 O  O   . HOH   I 5 .   ? 0.087  37.541  26.242 1.00 37.88 ? 975  HOH   A O   1 
HETATM 5844 O  O   . HOH   I 5 .   ? 30.774 29.978  22.667 1.00 20.22 ? 976  HOH   A O   1 
HETATM 5845 O  O   . HOH   I 5 .   ? 20.399 51.362  22.343 1.00 16.96 ? 977  HOH   A O   1 
HETATM 5846 O  O   . HOH   I 5 .   ? 8.929  55.610  32.768 1.00 33.16 ? 978  HOH   A O   1 
HETATM 5847 O  O   . HOH   I 5 .   ? 23.128 74.976  28.805 1.00 41.83 ? 979  HOH   A O   1 
HETATM 5848 O  O   . HOH   I 5 .   ? 2.755  47.395  41.843 1.00 20.43 ? 980  HOH   A O   1 
HETATM 5849 O  O   . HOH   I 5 .   ? 32.333 62.319  33.059 1.00 31.87 ? 981  HOH   A O   1 
HETATM 5850 O  O   . HOH   I 5 .   ? 8.385  33.139  41.547 1.00 38.16 ? 982  HOH   A O   1 
HETATM 5851 O  O   . HOH   I 5 .   ? 21.513 26.298  7.899  1.00 40.73 ? 983  HOH   A O   1 
HETATM 5852 O  O   . HOH   I 5 .   ? 14.311 40.514  4.266  1.00 32.08 ? 984  HOH   A O   1 
HETATM 5853 O  O   . HOH   I 5 .   ? 32.351 38.977  26.352 1.00 16.30 ? 985  HOH   A O   1 
HETATM 5854 O  O   . HOH   I 5 .   ? 6.925  54.325  29.975 1.00 21.02 ? 986  HOH   A O   1 
HETATM 5855 O  O   . HOH   I 5 .   ? 0.458  39.247  36.281 1.00 39.24 ? 987  HOH   A O   1 
HETATM 5856 O  O   . HOH   I 5 .   ? 24.524 62.262  8.287  1.00 21.45 ? 988  HOH   A O   1 
HETATM 5857 O  O   . HOH   I 5 .   ? 37.151 39.482  17.477 1.00 26.79 ? 989  HOH   A O   1 
HETATM 5858 O  O   . HOH   I 5 .   ? 38.092 68.086  28.932 1.00 41.54 ? 990  HOH   A O   1 
HETATM 5859 O  O   . HOH   I 5 .   ? 10.113 44.916  33.386 1.00 16.04 ? 991  HOH   A O   1 
HETATM 5860 O  O   . HOH   I 5 .   ? 21.744 34.113  40.769 1.00 22.23 ? 992  HOH   A O   1 
HETATM 5861 O  O   . HOH   I 5 .   ? 24.920 67.306  24.745 1.00 17.64 ? 993  HOH   A O   1 
HETATM 5862 O  O   . HOH   I 5 .   ? 30.244 59.267  35.355 1.00 18.00 ? 994  HOH   A O   1 
HETATM 5863 O  O   . HOH   I 5 .   ? 31.079 26.014  22.511 1.00 38.92 ? 995  HOH   A O   1 
HETATM 5864 O  O   . HOH   I 5 .   ? 34.790 56.831  23.467 1.00 18.09 ? 996  HOH   A O   1 
HETATM 5865 O  O   . HOH   I 5 .   ? 20.242 45.858  37.876 1.00 19.55 ? 997  HOH   A O   1 
HETATM 5866 O  O   . HOH   I 5 .   ? 31.770 36.616  7.411  1.00 44.01 ? 998  HOH   A O   1 
HETATM 5867 O  O   . HOH   I 5 .   ? 0.001  41.580  27.682 1.00 35.85 ? 999  HOH   A O   1 
HETATM 5868 O  O   . HOH   I 5 .   ? 13.722 46.204  40.427 1.00 25.37 ? 1000 HOH   A O   1 
HETATM 5869 O  O   . HOH   I 5 .   ? 18.287 27.099  21.305 1.00 25.36 ? 1001 HOH   A O   1 
HETATM 5870 O  O   . HOH   I 5 .   ? 10.317 42.310  40.174 1.00 22.51 ? 1002 HOH   A O   1 
HETATM 5871 O  O   . HOH   I 5 .   ? 7.554  26.867  40.392 1.00 35.34 ? 1003 HOH   A O   1 
HETATM 5872 O  O   . HOH   I 5 .   ? 5.000  28.354  24.740 1.00 38.95 ? 1004 HOH   A O   1 
HETATM 5873 O  O   . HOH   I 5 .   ? 13.155 30.247  13.748 1.00 35.94 ? 1005 HOH   A O   1 
HETATM 5874 O  O   . HOH   I 5 .   ? 25.422 30.702  35.658 1.00 23.80 ? 1006 HOH   A O   1 
HETATM 5875 O  O   . HOH   I 5 .   ? 40.211 43.884  28.576 1.00 21.12 ? 1007 HOH   A O   1 
HETATM 5876 O  O   . HOH   I 5 .   ? 30.292 31.104  9.783  1.00 37.53 ? 1008 HOH   A O   1 
HETATM 5877 O  O   . HOH   I 5 .   ? 12.930 36.906  36.647 1.00 18.34 ? 1009 HOH   A O   1 
HETATM 5878 O  O   . HOH   I 5 .   ? 16.973 72.380  29.403 1.00 40.51 ? 1010 HOH   A O   1 
HETATM 5879 O  O   . HOH   I 5 .   ? 37.675 43.730  31.753 1.00 23.50 ? 1011 HOH   A O   1 
HETATM 5880 O  O   . HOH   I 5 .   ? 30.437 46.280  -1.201 1.00 40.32 ? 1012 HOH   A O   1 
HETATM 5881 O  O   . HOH   I 5 .   ? 33.492 37.557  18.230 1.00 19.91 ? 1013 HOH   A O   1 
HETATM 5882 O  O   . HOH   I 5 .   ? 1.148  57.011  24.102 1.00 39.34 ? 1014 HOH   A O   1 
HETATM 5883 O  O   . HOH   I 5 .   ? 23.450 23.948  24.792 1.00 35.05 ? 1015 HOH   A O   1 
HETATM 5884 O  O   . HOH   I 5 .   ? 6.144  49.819  34.981 1.00 19.66 ? 1016 HOH   A O   1 
HETATM 5885 O  O   . HOH   I 5 .   ? 12.953 70.033  28.321 1.00 39.84 ? 1017 HOH   A O   1 
HETATM 5886 O  O   . HOH   I 5 .   ? 18.860 40.118  -1.097 1.00 28.44 ? 1018 HOH   A O   1 
HETATM 5887 O  O   . HOH   I 5 .   ? 33.689 28.725  19.652 1.00 38.03 ? 1019 HOH   A O   1 
HETATM 5888 O  O   . HOH   I 5 .   ? 8.753  66.483  27.187 1.00 35.91 ? 1020 HOH   A O   1 
HETATM 5889 O  O   . HOH   I 5 .   ? 21.290 45.289  45.288 1.00 23.59 ? 1021 HOH   A O   1 
HETATM 5890 O  O   . HOH   I 5 .   ? 11.964 26.046  22.696 1.00 39.70 ? 1022 HOH   A O   1 
HETATM 5891 O  O   . HOH   I 5 .   ? 31.866 69.131  23.385 1.00 33.75 ? 1023 HOH   A O   1 
HETATM 5892 O  O   . HOH   I 5 .   ? 22.875 65.046  14.510 1.00 33.13 ? 1024 HOH   A O   1 
HETATM 5893 O  O   . HOH   I 5 .   ? 27.641 22.658  13.943 1.00 35.86 ? 1025 HOH   A O   1 
HETATM 5894 O  O   . HOH   I 5 .   ? 14.130 67.148  18.419 1.00 30.26 ? 1026 HOH   A O   1 
HETATM 5895 O  O   . HOH   I 5 .   ? 35.290 55.647  11.560 1.00 35.21 ? 1027 HOH   A O   1 
HETATM 5896 O  O   . HOH   I 5 .   ? 21.057 57.297  25.102 1.00 14.73 ? 1028 HOH   A O   1 
HETATM 5897 O  O   . HOH   I 5 .   ? 2.793  55.012  24.561 1.00 22.73 ? 1029 HOH   A O   1 
HETATM 5898 O  O   . HOH   I 5 .   ? 32.039 44.338  -2.150 1.00 33.85 ? 1030 HOH   A O   1 
HETATM 5899 O  O   . HOH   I 5 .   ? 0.157  47.196  38.630 1.00 20.64 ? 1031 HOH   A O   1 
HETATM 5900 O  O   . HOH   I 5 .   ? 5.834  44.149  8.880  1.00 21.20 ? 1032 HOH   A O   1 
HETATM 5901 O  O   . HOH   I 5 .   ? 4.748  58.920  20.485 1.00 35.79 ? 1033 HOH   A O   1 
HETATM 5902 O  O   . HOH   I 5 .   ? 13.633 37.956  5.281  1.00 38.42 ? 1034 HOH   A O   1 
HETATM 5903 O  O   . HOH   I 5 .   ? 28.145 20.786  19.112 1.00 25.90 ? 1035 HOH   A O   1 
HETATM 5904 O  O   . HOH   I 5 .   ? 28.456 58.423  28.288 1.00 15.81 ? 1036 HOH   A O   1 
HETATM 5905 O  O   . HOH   I 5 .   ? 29.073 34.152  34.776 1.00 21.52 ? 1037 HOH   A O   1 
HETATM 5906 O  O   . HOH   I 5 .   ? 35.101 59.337  22.451 1.00 20.24 ? 1038 HOH   A O   1 
HETATM 5907 O  O   . HOH   I 5 .   ? 4.400  35.835  18.466 1.00 29.93 ? 1039 HOH   A O   1 
HETATM 5908 O  O   . HOH   I 5 .   ? 6.167  51.766  36.917 1.00 40.88 ? 1040 HOH   A O   1 
HETATM 5909 O  O   . HOH   I 5 .   ? 35.252 40.368  3.902  1.00 21.96 ? 1041 HOH   A O   1 
HETATM 5910 O  O   . HOH   I 5 .   ? 17.116 61.266  7.222  1.00 25.51 ? 1042 HOH   A O   1 
HETATM 5911 O  O   . HOH   I 5 .   ? 39.477 52.450  15.956 1.00 20.91 ? 1043 HOH   A O   1 
HETATM 5912 O  O   . HOH   I 5 .   ? 27.215 68.942  15.407 1.00 30.37 ? 1044 HOH   A O   1 
HETATM 5913 O  O   . HOH   I 5 .   ? 15.811 47.369  44.750 1.00 34.44 ? 1045 HOH   A O   1 
HETATM 5914 O  O   . HOH   I 5 .   ? 10.950 24.731  29.200 1.00 36.82 ? 1046 HOH   A O   1 
HETATM 5915 O  O   . HOH   I 5 .   ? 3.619  43.140  43.333 1.00 19.13 ? 1047 HOH   A O   1 
HETATM 5916 O  O   . HOH   I 5 .   ? 31.290 56.774  37.380 1.00 25.96 ? 1048 HOH   A O   1 
HETATM 5917 O  O   . HOH   I 5 .   ? 31.343 64.155  31.120 1.00 18.79 ? 1049 HOH   A O   1 
HETATM 5918 O  O   . HOH   I 5 .   ? 23.204 50.467  40.150 1.00 42.95 ? 1050 HOH   A O   1 
HETATM 5919 O  O   . HOH   I 5 .   ? 34.395 41.979  11.799 1.00 20.71 ? 1051 HOH   A O   1 
HETATM 5920 O  O   . HOH   I 5 .   ? 0.867  37.060  28.603 1.00 39.45 ? 1052 HOH   A O   1 
HETATM 5921 O  O   . HOH   I 5 .   ? 18.065 25.199  40.934 1.00 44.37 ? 1053 HOH   A O   1 
HETATM 5922 O  O   . HOH   I 5 .   ? 35.779 35.422  31.968 1.00 38.71 ? 1054 HOH   A O   1 
HETATM 5923 O  O   . HOH   I 5 .   ? 36.320 36.821  25.201 1.00 38.06 ? 1055 HOH   A O   1 
HETATM 5924 O  O   . HOH   I 5 .   ? 31.150 28.453  13.533 1.00 35.97 ? 1056 HOH   A O   1 
HETATM 5925 O  O   . HOH   I 5 .   ? 5.017  34.377  14.374 1.00 31.83 ? 1057 HOH   A O   1 
HETATM 5926 O  O   . HOH   I 5 .   ? 30.786 29.423  16.035 1.00 34.50 ? 1058 HOH   A O   1 
HETATM 5927 O  O   . HOH   I 5 .   ? 12.450 65.008  13.936 1.00 36.36 ? 1059 HOH   A O   1 
HETATM 5928 O  O   . HOH   I 5 .   ? 31.223 53.391  7.932  1.00 25.75 ? 1060 HOH   A O   1 
HETATM 5929 O  O   . HOH   I 5 .   ? 38.232 51.246  13.683 1.00 22.47 ? 1061 HOH   A O   1 
HETATM 5930 O  O   . HOH   I 5 .   ? 34.827 52.689  10.697 1.00 28.67 ? 1062 HOH   A O   1 
HETATM 5931 O  O   . HOH   I 5 .   ? 18.834 57.610  23.351 1.00 16.30 ? 1063 HOH   A O   1 
HETATM 5932 O  O   . HOH   I 5 .   ? -0.154 38.227  39.989 1.00 37.74 ? 1064 HOH   A O   1 
HETATM 5933 O  O   . HOH   I 5 .   ? 13.993 61.963  8.407  1.00 24.83 ? 1065 HOH   A O   1 
HETATM 5934 O  O   . HOH   I 5 .   ? 23.921 30.318  39.172 1.00 28.31 ? 1066 HOH   A O   1 
HETATM 5935 O  O   . HOH   I 5 .   ? 25.238 58.644  7.554  1.00 20.54 ? 1067 HOH   A O   1 
HETATM 5936 O  O   . HOH   I 5 .   ? -2.289 54.218  21.148 1.00 38.92 ? 1068 HOH   A O   1 
HETATM 5937 O  O   . HOH   I 5 .   ? 31.374 59.380  38.736 1.00 42.92 ? 1069 HOH   A O   1 
HETATM 5938 O  O   . HOH   I 5 .   ? 14.353 72.342  29.119 1.00 43.42 ? 1070 HOH   A O   1 
HETATM 5939 O  O   . HOH   I 5 .   ? 11.790 60.974  9.470  1.00 19.97 ? 1071 HOH   A O   1 
HETATM 5940 O  O   . HOH   I 5 .   ? 25.805 22.306  24.912 1.00 41.97 ? 1072 HOH   A O   1 
HETATM 5941 O  O   . HOH   I 5 .   ? 33.926 43.901  -0.141 1.00 25.30 ? 1073 HOH   A O   1 
HETATM 5942 O  O   . HOH   I 5 .   ? 18.868 38.720  44.956 1.00 27.87 ? 1074 HOH   A O   1 
HETATM 5943 O  O   . HOH   I 5 .   ? 24.494 68.975  19.085 1.00 38.63 ? 1075 HOH   A O   1 
HETATM 5944 O  O   . HOH   I 5 .   ? 22.101 52.637  2.218  1.00 23.75 ? 1076 HOH   A O   1 
HETATM 5945 O  O   . HOH   I 5 .   ? 34.244 29.029  33.093 1.00 35.03 ? 1077 HOH   A O   1 
HETATM 5946 O  O   . HOH   I 5 .   ? 19.442 62.404  37.786 1.00 31.64 ? 1078 HOH   A O   1 
HETATM 5947 O  O   . HOH   I 5 .   ? 21.784 31.359  2.942  1.00 32.30 ? 1079 HOH   A O   1 
HETATM 5948 O  O   . HOH   I 5 .   ? 1.750  36.541  34.362 1.00 35.61 ? 1080 HOH   A O   1 
HETATM 5949 O  O   . HOH   I 5 .   ? 8.354  52.576  36.289 1.00 40.25 ? 1081 HOH   A O   1 
HETATM 5950 O  O   . HOH   I 5 .   ? 26.320 46.422  0.199  1.00 22.16 ? 1082 HOH   A O   1 
HETATM 5951 O  O   . HOH   I 5 .   ? 25.147 39.216  1.346  1.00 39.16 ? 1083 HOH   A O   1 
HETATM 5952 O  O   . HOH   I 5 .   ? 37.032 59.196  20.603 1.00 24.94 ? 1084 HOH   A O   1 
HETATM 5953 O  O   . HOH   I 5 .   ? -0.375 42.836  15.685 1.00 36.89 ? 1085 HOH   A O   1 
HETATM 5954 O  O   . HOH   I 5 .   ? -0.738 55.403  13.445 1.00 31.43 ? 1086 HOH   A O   1 
HETATM 5955 O  O   . HOH   I 5 .   ? 30.070 26.146  36.661 1.00 37.38 ? 1087 HOH   A O   1 
HETATM 5956 O  O   . HOH   I 5 .   ? 25.146 24.080  14.094 1.00 41.27 ? 1088 HOH   A O   1 
HETATM 5957 O  O   . HOH   I 5 .   ? 10.533 65.759  36.548 1.00 26.29 ? 1089 HOH   A O   1 
HETATM 5958 O  O   . HOH   I 5 .   ? 37.307 37.030  18.505 1.00 28.06 ? 1090 HOH   A O   1 
HETATM 5959 O  O   . HOH   I 5 .   ? 6.615  30.832  13.402 1.00 41.76 ? 1091 HOH   A O   1 
HETATM 5960 O  O   . HOH   I 5 .   ? 35.358 74.969  31.013 1.00 34.47 ? 1092 HOH   A O   1 
HETATM 5961 O  O   . HOH   I 5 .   ? 14.276 56.753  37.725 1.00 22.21 ? 1093 HOH   A O   1 
HETATM 5962 O  O   . HOH   I 5 .   ? 19.305 48.066  39.126 1.00 22.09 ? 1094 HOH   A O   1 
HETATM 5963 O  O   . HOH   I 5 .   ? 30.881 63.452  41.381 1.00 45.64 ? 1095 HOH   A O   1 
HETATM 5964 O  O   . HOH   I 5 .   ? 21.205 31.395  39.488 1.00 26.61 ? 1096 HOH   A O   1 
HETATM 5965 O  O   . HOH   I 5 .   ? 7.980  64.388  34.831 1.00 38.25 ? 1097 HOH   A O   1 
HETATM 5966 O  O   . HOH   I 5 .   ? 20.514 31.667  44.662 1.00 42.21 ? 1098 HOH   A O   1 
HETATM 5967 O  O   . HOH   I 5 .   ? 7.394  34.178  11.865 1.00 40.54 ? 1099 HOH   A O   1 
HETATM 5968 O  O   . HOH   I 5 .   ? 22.342 34.486  43.507 1.00 42.19 ? 1100 HOH   A O   1 
HETATM 5969 O  O   . HOH   I 5 .   ? 19.406 58.039  7.238  1.00 21.32 ? 1101 HOH   A O   1 
HETATM 5970 O  O   . HOH   I 5 .   ? 13.137 45.045  42.244 1.00 41.18 ? 1102 HOH   A O   1 
HETATM 5971 O  O   . HOH   I 5 .   ? 31.782 28.538  24.946 1.00 35.09 ? 1103 HOH   A O   1 
HETATM 5972 O  O   . HOH   I 5 .   ? 6.228  66.944  19.203 1.00 46.22 ? 1104 HOH   A O   1 
HETATM 5973 O  O   . HOH   I 5 .   ? 19.351 23.069  39.767 1.00 45.03 ? 1105 HOH   A O   1 
HETATM 5974 O  O   . HOH   I 5 .   ? -5.190 49.446  24.518 1.00 40.27 ? 1106 HOH   A O   1 
HETATM 5975 O  O   . HOH   I 5 .   ? 6.840  26.207  23.777 1.00 40.00 ? 1107 HOH   A O   1 
HETATM 5976 O  O   . HOH   I 5 .   ? 4.133  40.382  9.553  1.00 39.70 ? 1108 HOH   A O   1 
HETATM 5977 O  O   . HOH   I 5 .   ? 33.831 29.486  16.731 1.00 38.39 ? 1109 HOH   A O   1 
HETATM 5978 O  O   . HOH   I 5 .   ? 16.794 64.378  36.828 1.00 36.02 ? 1110 HOH   A O   1 
HETATM 5979 O  O   . HOH   I 5 .   ? 7.432  44.810  2.583  1.00 43.09 ? 1111 HOH   A O   1 
HETATM 5980 O  O   . HOH   I 5 .   ? 9.494  40.603  41.988 1.00 26.54 ? 1112 HOH   A O   1 
HETATM 5981 O  O   . HOH   I 5 .   ? 25.589 28.702  40.483 1.00 35.22 ? 1113 HOH   A O   1 
HETATM 5982 O  O   . HOH   I 5 .   ? -2.079 45.319  28.610 1.00 39.24 ? 1114 HOH   A O   1 
HETATM 5983 O  O   . HOH   I 5 .   ? -0.587 34.583  27.782 1.00 40.93 ? 1115 HOH   A O   1 
HETATM 5984 O  O   . HOH   I 5 .   ? 6.287  66.678  34.172 1.00 39.71 ? 1116 HOH   A O   1 
HETATM 5985 O  O   . HOH   I 5 .   ? 24.632 65.028  16.291 1.00 35.51 ? 1117 HOH   A O   1 
HETATM 5986 O  O   . HOH   I 5 .   ? 11.670 22.263  26.092 1.00 34.49 ? 1118 HOH   A O   1 
HETATM 5987 O  O   . HOH   I 5 .   ? 10.952 49.808  0.278  1.00 39.93 ? 1119 HOH   A O   1 
HETATM 5988 O  O   . HOH   I 5 .   ? 10.982 53.519  36.854 1.00 32.69 ? 1120 HOH   A O   1 
HETATM 5989 O  O   . HOH   I 5 .   ? 7.047  34.893  43.159 1.00 35.52 ? 1121 HOH   A O   1 
HETATM 5990 O  O   . HOH   I 5 .   ? 23.884 42.412  37.200 1.00 26.41 ? 1122 HOH   A O   1 
HETATM 5991 O  O   . HOH   I 5 .   ? 6.467  57.083  32.789 1.00 40.23 ? 1123 HOH   A O   1 
HETATM 5992 O  O   . HOH   I 5 .   ? 40.649 39.877  20.481 1.00 43.25 ? 1124 HOH   A O   1 
HETATM 5993 O  O   . HOH   I 5 .   ? 31.190 28.160  20.670 1.00 34.49 ? 1125 HOH   A O   1 
HETATM 5994 O  O   . HOH   I 5 .   ? 38.710 45.572  21.996 1.00 22.55 ? 1126 HOH   A O   1 
HETATM 5995 O  O   . HOH   I 5 .   ? 15.394 30.070  7.543  1.00 43.29 ? 1127 HOH   A O   1 
HETATM 5996 O  O   . HOH   I 5 .   ? 1.913  55.012  11.699 1.00 38.78 ? 1128 HOH   A O   1 
HETATM 5997 O  O   . HOH   I 5 .   ? 15.060 46.005  -0.065 1.00 36.70 ? 1129 HOH   A O   1 
HETATM 5998 O  O   . HOH   I 5 .   ? 33.531 45.400  -4.174 1.00 31.74 ? 1130 HOH   A O   1 
HETATM 5999 O  O   . HOH   I 5 .   ? 17.332 71.475  22.232 1.00 39.69 ? 1131 HOH   A O   1 
HETATM 6000 O  O   . HOH   I 5 .   ? 12.303 31.872  11.219 1.00 41.38 ? 1132 HOH   A O   1 
HETATM 6001 O  O   . HOH   I 5 .   ? 10.079 67.898  37.970 1.00 42.46 ? 1133 HOH   A O   1 
HETATM 6002 O  O   . HOH   I 5 .   ? 16.180 28.741  14.837 1.00 37.01 ? 1134 HOH   A O   1 
HETATM 6003 O  O   . HOH   I 5 .   ? 26.908 25.989  40.177 1.00 35.43 ? 1135 HOH   A O   1 
HETATM 6004 O  O   . HOH   I 5 .   ? 14.531 32.694  7.710  1.00 37.14 ? 1136 HOH   A O   1 
HETATM 6005 O  O   . HOH   I 5 .   ? 38.354 49.966  22.117 1.00 28.22 ? 1137 HOH   A O   1 
HETATM 6006 O  O   . HOH   I 5 .   ? 14.330 66.601  13.610 1.00 37.26 ? 1138 HOH   A O   1 
HETATM 6007 O  O   . HOH   I 5 .   ? 4.234  64.487  26.696 1.00 40.82 ? 1139 HOH   A O   1 
HETATM 6008 O  O   . HOH   I 5 .   ? 3.701  51.098  34.214 1.00 40.62 ? 1140 HOH   A O   1 
HETATM 6009 O  O   . HOH   I 5 .   ? 34.834 61.870  31.781 1.00 38.86 ? 1141 HOH   A O   1 
HETATM 6010 O  O   . HOH   I 5 .   ? 8.974  54.373  35.140 1.00 39.44 ? 1142 HOH   A O   1 
HETATM 6011 O  O   . HOH   I 5 .   ? 18.038 48.800  45.191 1.00 35.53 ? 1143 HOH   A O   1 
HETATM 6012 O  O   . HOH   I 5 .   ? 2.935  60.009  21.958 1.00 41.64 ? 1144 HOH   A O   1 
HETATM 6013 O  O   . HOH   I 5 .   ? 21.079 50.549  39.407 1.00 41.75 ? 1145 HOH   A O   1 
HETATM 6014 O  O   . HOH   I 5 .   ? 26.253 19.498  20.782 1.00 35.99 ? 1146 HOH   A O   1 
HETATM 6015 O  O   . HOH   I 5 .   ? 39.312 47.651  23.432 1.00 32.92 ? 1147 HOH   A O   1 
HETATM 6016 O  O   . HOH   I 5 .   ? 36.703 55.146  32.104 1.00 23.23 ? 1148 HOH   A O   1 
HETATM 6017 O  O   . HOH   I 5 .   ? -0.298 34.937  35.948 1.00 40.92 ? 1149 HOH   A O   1 
HETATM 6018 O  O   . HOH   I 5 .   ? -1.651 34.581  32.884 1.00 37.17 ? 1150 HOH   A O   1 
HETATM 6019 O  O   . HOH   I 5 .   ? 37.487 62.025  20.424 1.00 35.66 ? 1151 HOH   A O   1 
HETATM 6020 O  O   . HOH   I 5 .   ? 35.070 49.381  2.500  1.00 34.43 ? 1152 HOH   A O   1 
HETATM 6021 O  O   . HOH   I 5 .   ? 12.565 33.085  43.092 1.00 39.74 ? 1153 HOH   A O   1 
HETATM 6022 O  O   . HOH   I 5 .   ? 1.371  42.083  44.473 1.00 35.13 ? 1154 HOH   A O   1 
HETATM 6023 O  O   . HOH   I 5 .   ? 22.611 53.916  37.878 1.00 44.13 ? 1155 HOH   A O   1 
HETATM 6024 O  O   . HOH   I 5 .   ? 16.890 56.442  39.103 1.00 42.38 ? 1156 HOH   A O   1 
HETATM 6025 O  O   . HOH   I 5 .   ? 23.837 68.593  42.741 1.00 40.49 ? 1157 HOH   A O   1 
HETATM 6026 O  O   . HOH   I 5 .   ? 8.505  24.142  39.487 1.00 45.64 ? 1158 HOH   A O   1 
HETATM 6027 O  O   . HOH   J 5 .   ? 7.230  82.756  69.431 1.00 38.76 ? 901  HOH   B O   1 
HETATM 6028 O  O   . HOH   J 5 .   ? 34.942 76.660  44.949 1.00 42.26 ? 902  HOH   B O   1 
HETATM 6029 O  O   . HOH   J 5 .   ? 19.228 116.211 46.626 1.00 43.36 ? 903  HOH   B O   1 
HETATM 6030 O  O   . HOH   J 5 .   ? 29.510 84.576  35.373 1.00 38.78 ? 904  HOH   B O   1 
HETATM 6031 O  O   . HOH   J 5 .   ? -2.282 99.921  46.847 1.00 36.38 ? 905  HOH   B O   1 
HETATM 6032 O  O   . HOH   J 5 .   ? 30.862 75.625  41.351 1.00 26.19 ? 906  HOH   B O   1 
HETATM 6033 O  O   . HOH   J 5 .   ? 39.614 97.278  50.753 1.00 45.08 ? 907  HOH   B O   1 
HETATM 6034 O  O   . HOH   J 5 .   ? 32.494 123.668 62.314 1.00 30.33 ? 908  HOH   B O   1 
HETATM 6035 O  O   . HOH   J 5 .   ? 17.945 110.402 36.685 1.00 45.79 ? 909  HOH   B O   1 
HETATM 6036 O  O   . HOH   J 5 .   ? 16.834 117.853 55.841 1.00 24.03 ? 910  HOH   B O   1 
HETATM 6037 O  O   . HOH   J 5 .   ? 23.504 106.822 65.693 1.00 42.45 ? 911  HOH   B O   1 
HETATM 6038 O  O   . HOH   J 5 .   ? 8.929  75.485  43.493 1.00 37.79 ? 912  HOH   B O   1 
HETATM 6039 O  O   . HOH   J 5 .   ? 28.061 95.643  65.259 1.00 34.32 ? 913  HOH   B O   1 
HETATM 6040 O  O   . HOH   J 5 .   ? 42.641 103.912 52.032 1.00 36.13 ? 914  HOH   B O   1 
HETATM 6041 O  O   . HOH   J 5 .   ? 35.155 85.538  36.526 1.00 27.04 ? 915  HOH   B O   1 
HETATM 6042 O  O   . HOH   J 5 .   ? 28.062 102.487 51.555 1.00 15.05 ? 916  HOH   B O   1 
HETATM 6043 O  O   . HOH   J 5 .   ? 10.040 116.251 57.323 1.00 33.09 ? 917  HOH   B O   1 
HETATM 6044 O  O   . HOH   J 5 .   ? 11.867 82.326  31.923 1.00 38.69 ? 918  HOH   B O   1 
HETATM 6045 O  O   . HOH   J 5 .   ? 31.794 82.364  33.306 1.00 39.55 ? 919  HOH   B O   1 
HETATM 6046 O  O   . HOH   J 5 .   ? 20.188 93.289  21.945 1.00 37.24 ? 920  HOH   B O   1 
HETATM 6047 O  O   . HOH   J 5 .   ? 23.705 114.222 64.170 1.00 28.47 ? 921  HOH   B O   1 
HETATM 6048 O  O   . HOH   J 5 .   ? 4.856  104.638 40.051 1.00 24.32 ? 922  HOH   B O   1 
HETATM 6049 O  O   . HOH   J 5 .   ? 37.966 108.895 48.491 1.00 33.90 ? 923  HOH   B O   1 
HETATM 6050 O  O   . HOH   J 5 .   ? 19.762 101.374 33.611 1.00 21.96 ? 924  HOH   B O   1 
HETATM 6051 O  O   . HOH   J 5 .   ? 21.037 87.425  54.684 1.00 6.56  ? 925  HOH   B O   1 
HETATM 6052 O  O   . HOH   J 5 .   ? 20.081 84.056  74.278 1.00 23.04 ? 926  HOH   B O   1 
HETATM 6053 O  O   . HOH   J 5 .   ? 36.498 92.568  28.644 1.00 19.66 ? 927  HOH   B O   1 
HETATM 6054 O  O   . HOH   J 5 .   ? 15.094 115.141 48.619 1.00 26.91 ? 928  HOH   B O   1 
HETATM 6055 O  O   . HOH   J 5 .   ? 7.526  100.188 33.488 1.00 36.10 ? 929  HOH   B O   1 
HETATM 6056 O  O   . HOH   J 5 .   ? 37.476 102.988 56.354 1.00 34.64 ? 930  HOH   B O   1 
HETATM 6057 O  O   . HOH   J 5 .   ? -1.342 103.584 46.004 1.00 42.11 ? 931  HOH   B O   1 
HETATM 6058 O  O   . HOH   J 5 .   ? 4.701  108.010 51.939 1.00 37.24 ? 932  HOH   B O   1 
HETATM 6059 O  O   . HOH   J 5 .   ? 33.958 96.350  30.277 1.00 25.64 ? 933  HOH   B O   1 
HETATM 6060 O  O   . HOH   J 5 .   ? 25.956 86.084  49.564 1.00 15.02 ? 934  HOH   B O   1 
HETATM 6061 O  O   . HOH   J 5 .   ? 23.716 84.111  53.203 1.00 15.10 ? 935  HOH   B O   1 
HETATM 6062 O  O   . HOH   J 5 .   ? 1.441  98.434  51.879 1.00 28.46 ? 936  HOH   B O   1 
HETATM 6063 O  O   . HOH   J 5 .   ? 20.424 99.647  47.449 1.00 15.91 ? 937  HOH   B O   1 
HETATM 6064 O  O   . HOH   J 5 .   ? 11.747 84.388  35.968 1.00 19.28 ? 938  HOH   B O   1 
HETATM 6065 O  O   . HOH   J 5 .   ? 11.824 110.747 40.677 1.00 34.51 ? 939  HOH   B O   1 
HETATM 6066 O  O   . HOH   J 5 .   ? 13.474 99.683  61.974 1.00 21.69 ? 940  HOH   B O   1 
HETATM 6067 O  O   . HOH   J 5 .   ? 30.191 102.399 34.120 1.00 30.46 ? 941  HOH   B O   1 
HETATM 6068 O  O   . HOH   J 5 .   ? -0.062 86.663  66.365 1.00 27.78 ? 942  HOH   B O   1 
HETATM 6069 O  O   . HOH   J 5 .   ? 33.294 108.085 43.229 1.00 40.14 ? 943  HOH   B O   1 
HETATM 6070 O  O   . HOH   J 5 .   ? 28.794 84.240  27.614 1.00 43.87 ? 944  HOH   B O   1 
HETATM 6071 O  O   . HOH   J 5 .   ? 0.408  95.347  53.234 1.00 22.89 ? 945  HOH   B O   1 
HETATM 6072 O  O   . HOH   J 5 .   ? 6.359  102.898 58.827 1.00 42.99 ? 946  HOH   B O   1 
HETATM 6073 O  O   . HOH   J 5 .   ? 25.301 87.195  64.586 1.00 22.84 ? 947  HOH   B O   1 
HETATM 6074 O  O   . HOH   J 5 .   ? 33.065 109.976 52.446 1.00 25.74 ? 948  HOH   B O   1 
HETATM 6075 O  O   . HOH   J 5 .   ? 19.478 109.081 60.863 1.00 22.88 ? 949  HOH   B O   1 
HETATM 6076 O  O   . HOH   J 5 .   ? 17.024 79.732  33.643 1.00 23.99 ? 950  HOH   B O   1 
HETATM 6077 O  O   . HOH   J 5 .   ? 14.567 108.361 34.967 1.00 31.71 ? 951  HOH   B O   1 
HETATM 6078 O  O   . HOH   J 5 .   ? 8.109  78.563  66.895 1.00 34.33 ? 952  HOH   B O   1 
HETATM 6079 O  O   . HOH   J 5 .   ? 29.818 74.157  43.198 1.00 39.78 ? 953  HOH   B O   1 
HETATM 6080 O  O   . HOH   J 5 .   ? 15.537 89.710  27.736 1.00 22.24 ? 954  HOH   B O   1 
HETATM 6081 O  O   . HOH   J 5 .   ? 7.647  72.321  65.771 1.00 24.62 ? 955  HOH   B O   1 
HETATM 6082 O  O   . HOH   J 5 .   ? 23.481 113.825 47.596 1.00 21.54 ? 956  HOH   B O   1 
HETATM 6083 O  O   . HOH   J 5 .   ? 13.660 91.643  65.898 1.00 25.18 ? 957  HOH   B O   1 
HETATM 6084 O  O   . HOH   J 5 .   ? 10.073 90.478  58.991 1.00 15.70 ? 958  HOH   B O   1 
HETATM 6085 O  O   . HOH   J 5 .   ? 21.453 72.365  33.549 1.00 38.17 ? 959  HOH   B O   1 
HETATM 6086 O  O   . HOH   J 5 .   ? 11.673 114.209 56.290 1.00 23.47 ? 960  HOH   B O   1 
HETATM 6087 O  O   . HOH   J 5 .   ? 24.735 88.220  60.186 1.00 14.52 ? 961  HOH   B O   1 
HETATM 6088 O  O   . HOH   J 5 .   ? 23.343 95.554  66.072 1.00 43.28 ? 962  HOH   B O   1 
HETATM 6089 O  O   . HOH   J 5 .   ? 22.344 104.432 64.644 1.00 29.93 ? 963  HOH   B O   1 
HETATM 6090 O  O   . HOH   J 5 .   ? 32.408 115.111 46.875 1.00 40.12 ? 964  HOH   B O   1 
HETATM 6091 O  O   . HOH   J 5 .   ? 8.679  103.580 39.410 1.00 19.78 ? 965  HOH   B O   1 
HETATM 6092 O  O   . HOH   J 5 .   ? 12.125 109.426 64.453 1.00 22.37 ? 966  HOH   B O   1 
HETATM 6093 O  O   . HOH   J 5 .   ? 23.797 102.588 63.106 1.00 20.76 ? 967  HOH   B O   1 
HETATM 6094 O  O   . HOH   J 5 .   ? 8.887  101.149 58.586 1.00 28.49 ? 968  HOH   B O   1 
HETATM 6095 O  O   . HOH   J 5 .   ? 10.802 70.581  54.458 1.00 33.09 ? 969  HOH   B O   1 
HETATM 6096 O  O   . HOH   J 5 .   ? 11.552 71.555  48.270 1.00 24.23 ? 970  HOH   B O   1 
HETATM 6097 O  O   . HOH   J 5 .   ? 0.088  91.661  35.684 1.00 29.11 ? 971  HOH   B O   1 
HETATM 6098 O  O   . HOH   J 5 .   ? 2.610  77.968  45.246 1.00 32.36 ? 972  HOH   B O   1 
HETATM 6099 O  O   . HOH   J 5 .   ? 34.184 92.660  35.998 1.00 15.12 ? 973  HOH   B O   1 
HETATM 6100 O  O   . HOH   J 5 .   ? 5.226  106.350 44.130 1.00 24.73 ? 974  HOH   B O   1 
HETATM 6101 O  O   . HOH   J 5 .   ? 35.914 82.580  50.881 1.00 27.75 ? 975  HOH   B O   1 
HETATM 6102 O  O   . HOH   J 5 .   ? 7.099  88.742  60.346 1.00 15.70 ? 976  HOH   B O   1 
HETATM 6103 O  O   . HOH   J 5 .   ? -1.353 89.717  52.015 1.00 21.89 ? 977  HOH   B O   1 
HETATM 6104 O  O   . HOH   J 5 .   ? 22.302 82.917  70.012 1.00 28.91 ? 978  HOH   B O   1 
HETATM 6105 O  O   . HOH   J 5 .   ? 6.165  110.201 45.209 1.00 28.04 ? 979  HOH   B O   1 
HETATM 6106 O  O   . HOH   J 5 .   ? 32.613 88.598  47.251 1.00 14.23 ? 980  HOH   B O   1 
HETATM 6107 O  O   . HOH   J 5 .   ? 4.646  104.625 46.248 1.00 23.23 ? 981  HOH   B O   1 
HETATM 6108 O  O   . HOH   J 5 .   ? 17.117 85.014  26.684 1.00 36.04 ? 982  HOH   B O   1 
HETATM 6109 O  O   . HOH   J 5 .   ? 17.418 95.219  68.049 1.00 34.20 ? 983  HOH   B O   1 
HETATM 6110 O  O   . HOH   J 5 .   ? 6.446  98.547  58.182 1.00 30.37 ? 984  HOH   B O   1 
HETATM 6111 O  O   . HOH   J 5 .   ? 35.720 95.753  47.152 1.00 22.23 ? 985  HOH   B O   1 
HETATM 6112 O  O   . HOH   J 5 .   ? 32.362 107.756 58.906 1.00 40.64 ? 986  HOH   B O   1 
HETATM 6113 O  O   . HOH   J 5 .   ? 16.667 92.283  52.924 1.00 20.06 ? 987  HOH   B O   1 
HETATM 6114 O  O   . HOH   J 5 .   ? 17.625 96.664  50.819 1.00 14.79 ? 988  HOH   B O   1 
HETATM 6115 O  O   . HOH   J 5 .   ? 4.120  102.295 54.558 1.00 40.54 ? 989  HOH   B O   1 
HETATM 6116 O  O   . HOH   J 5 .   ? 10.410 98.563  30.789 1.00 40.52 ? 990  HOH   B O   1 
HETATM 6117 O  O   . HOH   J 5 .   ? 20.382 96.984  48.079 1.00 17.22 ? 991  HOH   B O   1 
HETATM 6118 O  O   . HOH   J 5 .   ? -0.022 87.413  53.079 1.00 34.40 ? 992  HOH   B O   1 
HETATM 6119 O  O   . HOH   J 5 .   ? 7.435  105.030 57.938 1.00 34.07 ? 993  HOH   B O   1 
HETATM 6120 O  O   . HOH   J 5 .   ? 35.323 90.538  37.394 1.00 24.47 ? 994  HOH   B O   1 
HETATM 6121 O  O   . HOH   J 5 .   ? 37.071 82.464  44.059 1.00 32.82 ? 995  HOH   B O   1 
HETATM 6122 O  O   . HOH   J 5 .   ? 30.596 73.808  52.763 1.00 24.06 ? 996  HOH   B O   1 
HETATM 6123 O  O   . HOH   J 5 .   ? 30.531 92.084  24.557 1.00 35.04 ? 997  HOH   B O   1 
HETATM 6124 O  O   . HOH   J 5 .   ? 30.271 104.774 61.143 1.00 18.33 ? 998  HOH   B O   1 
HETATM 6125 O  O   . HOH   J 5 .   ? 5.101  74.115  49.846 1.00 27.46 ? 999  HOH   B O   1 
HETATM 6126 O  O   . HOH   J 5 .   ? 4.353  81.892  43.847 1.00 23.23 ? 1000 HOH   B O   1 
HETATM 6127 O  O   . HOH   J 5 .   ? 22.680 89.946  64.093 1.00 17.76 ? 1001 HOH   B O   1 
HETATM 6128 O  O   . HOH   J 5 .   ? 23.981 96.270  24.828 1.00 41.82 ? 1002 HOH   B O   1 
HETATM 6129 O  O   . HOH   J 5 .   ? 14.457 86.611  29.817 1.00 28.20 ? 1003 HOH   B O   1 
HETATM 6130 O  O   . HOH   J 5 .   ? 6.835  99.835  55.813 1.00 21.03 ? 1004 HOH   B O   1 
HETATM 6131 O  O   . HOH   J 5 .   ? 32.319 84.568  51.926 1.00 15.16 ? 1005 HOH   B O   1 
HETATM 6132 O  O   . HOH   J 5 .   ? -5.134 97.990  48.109 1.00 36.71 ? 1006 HOH   B O   1 
HETATM 6133 O  O   . HOH   J 5 .   ? -2.658 87.291  55.384 1.00 38.24 ? 1007 HOH   B O   1 
HETATM 6134 O  O   . HOH   J 5 .   ? 8.352  75.330  67.728 1.00 36.69 ? 1008 HOH   B O   1 
HETATM 6135 O  O   . HOH   J 5 .   ? 14.146 117.968 55.198 1.00 27.02 ? 1009 HOH   B O   1 
HETATM 6136 O  O   . HOH   J 5 .   ? 27.130 68.568  38.841 1.00 40.75 ? 1010 HOH   B O   1 
HETATM 6137 O  O   . HOH   J 5 .   ? 25.173 76.119  61.056 1.00 18.78 ? 1011 HOH   B O   1 
HETATM 6138 O  O   . HOH   J 5 .   ? 20.050 76.513  69.867 1.00 36.28 ? 1012 HOH   B O   1 
HETATM 6139 O  O   . HOH   J 5 .   ? 7.886  94.890  26.981 1.00 38.84 ? 1013 HOH   B O   1 
HETATM 6140 O  O   . HOH   J 5 .   ? 39.585 87.753  49.991 1.00 29.21 ? 1014 HOH   B O   1 
HETATM 6141 O  O   . HOH   J 5 .   ? 30.614 75.529  47.913 1.00 19.77 ? 1015 HOH   B O   1 
HETATM 6142 O  O   . HOH   J 5 .   ? 28.426 104.110 54.047 1.00 16.17 ? 1016 HOH   B O   1 
HETATM 6143 O  O   . HOH   J 5 .   ? 35.145 88.483  58.839 1.00 29.18 ? 1017 HOH   B O   1 
HETATM 6144 O  O   . HOH   J 5 .   ? 34.745 102.624 49.239 1.00 18.72 ? 1018 HOH   B O   1 
HETATM 6145 O  O   . HOH   J 5 .   ? 33.907 89.394  25.626 1.00 22.60 ? 1019 HOH   B O   1 
HETATM 6146 O  O   . HOH   J 5 .   ? 15.343 100.595 27.190 1.00 40.85 ? 1020 HOH   B O   1 
HETATM 6147 O  O   . HOH   J 5 .   ? 30.703 71.060  47.397 1.00 40.66 ? 1021 HOH   B O   1 
HETATM 6148 O  O   . HOH   J 5 .   ? 20.280 91.337  63.439 1.00 17.85 ? 1022 HOH   B O   1 
HETATM 6149 O  O   . HOH   J 5 .   ? -3.029 87.892  50.145 1.00 31.60 ? 1023 HOH   B O   1 
HETATM 6150 O  O   . HOH   J 5 .   ? 33.380 78.109  40.187 1.00 35.15 ? 1024 HOH   B O   1 
HETATM 6151 O  O   . HOH   J 5 .   ? 10.059 68.955  56.859 1.00 40.18 ? 1025 HOH   B O   1 
HETATM 6152 O  O   . HOH   J 5 .   ? 29.741 71.306  62.255 1.00 38.38 ? 1026 HOH   B O   1 
HETATM 6153 O  O   . HOH   J 5 .   ? 37.134 104.965 46.446 1.00 22.74 ? 1027 HOH   B O   1 
HETATM 6154 O  O   . HOH   J 5 .   ? 9.233  101.295 35.039 1.00 26.05 ? 1028 HOH   B O   1 
HETATM 6155 O  O   . HOH   J 5 .   ? 6.257  95.509  60.764 1.00 19.74 ? 1029 HOH   B O   1 
HETATM 6156 O  O   . HOH   J 5 .   ? 12.835 82.511  62.110 1.00 14.93 ? 1030 HOH   B O   1 
HETATM 6157 O  O   . HOH   J 5 .   ? 21.089 102.911 50.967 1.00 14.65 ? 1031 HOH   B O   1 
HETATM 6158 O  O   . HOH   J 5 .   ? 2.723  100.678 50.224 1.00 22.40 ? 1032 HOH   B O   1 
HETATM 6159 O  O   . HOH   J 5 .   ? 18.521 83.752  70.498 1.00 26.95 ? 1033 HOH   B O   1 
HETATM 6160 O  O   . HOH   J 5 .   ? 18.037 72.990  46.589 1.00 23.45 ? 1034 HOH   B O   1 
HETATM 6161 O  O   . HOH   J 5 .   ? 25.366 97.680  46.847 1.00 15.21 ? 1035 HOH   B O   1 
HETATM 6162 O  O   . HOH   J 5 .   ? -0.833 100.958 39.072 1.00 37.20 ? 1036 HOH   B O   1 
HETATM 6163 O  O   . HOH   J 5 .   ? 34.688 92.396  33.280 1.00 16.69 ? 1037 HOH   B O   1 
HETATM 6164 O  O   . HOH   J 5 .   ? 13.260 75.483  66.990 1.00 22.70 ? 1038 HOH   B O   1 
HETATM 6165 O  O   . HOH   J 5 .   ? 7.299  108.698 42.013 1.00 27.67 ? 1039 HOH   B O   1 
HETATM 6166 O  O   . HOH   J 5 .   ? 31.447 90.105  62.632 1.00 31.29 ? 1040 HOH   B O   1 
HETATM 6167 O  O   . HOH   J 5 .   ? -1.718 87.572  59.676 1.00 32.81 ? 1041 HOH   B O   1 
HETATM 6168 O  O   . HOH   J 5 .   ? 30.784 82.863  44.181 1.00 15.01 ? 1042 HOH   B O   1 
HETATM 6169 O  O   . HOH   J 5 .   ? 6.034  90.054  34.512 1.00 30.42 ? 1043 HOH   B O   1 
HETATM 6170 O  O   . HOH   J 5 .   ? 18.813 73.772  41.602 1.00 27.72 ? 1044 HOH   B O   1 
HETATM 6171 O  O   . HOH   J 5 .   ? 15.633 92.454  70.411 1.00 39.94 ? 1045 HOH   B O   1 
HETATM 6172 O  O   . HOH   J 5 .   ? 37.111 104.197 43.631 1.00 32.47 ? 1046 HOH   B O   1 
HETATM 6173 O  O   . HOH   J 5 .   ? -0.550 79.987  52.743 1.00 41.46 ? 1047 HOH   B O   1 
HETATM 6174 O  O   . HOH   J 5 .   ? 21.338 90.579  70.868 1.00 21.82 ? 1048 HOH   B O   1 
HETATM 6175 O  O   . HOH   J 5 .   ? 38.331 97.032  39.409 1.00 26.29 ? 1049 HOH   B O   1 
HETATM 6176 O  O   . HOH   J 5 .   ? 23.101 69.672  49.798 1.00 27.72 ? 1050 HOH   B O   1 
HETATM 6177 O  O   . HOH   J 5 .   ? -0.029 91.930  38.046 1.00 37.23 ? 1051 HOH   B O   1 
HETATM 6178 O  O   . HOH   J 5 .   ? 5.061  80.406  39.712 1.00 35.25 ? 1052 HOH   B O   1 
HETATM 6179 O  O   . HOH   J 5 .   ? 9.915  81.661  69.010 1.00 37.18 ? 1053 HOH   B O   1 
HETATM 6180 O  O   . HOH   J 5 .   ? 32.159 80.438  37.432 1.00 37.05 ? 1054 HOH   B O   1 
HETATM 6181 O  O   . HOH   J 5 .   ? 13.782 112.958 44.906 1.00 34.83 ? 1055 HOH   B O   1 
HETATM 6182 O  O   . HOH   J 5 .   ? 33.420 83.318  43.794 1.00 18.54 ? 1056 HOH   B O   1 
HETATM 6183 O  O   . HOH   J 5 .   ? 13.094 76.139  39.045 1.00 34.05 ? 1057 HOH   B O   1 
HETATM 6184 O  O   . HOH   J 5 .   ? 24.791 112.940 50.870 1.00 18.62 ? 1058 HOH   B O   1 
HETATM 6185 O  O   . HOH   J 5 .   ? 13.419 84.010  30.995 1.00 40.50 ? 1059 HOH   B O   1 
HETATM 6186 O  O   . HOH   J 5 .   ? -0.219 83.379  51.618 1.00 38.55 ? 1060 HOH   B O   1 
HETATM 6187 O  O   . HOH   J 5 .   ? 10.352 87.956  65.690 1.00 20.34 ? 1061 HOH   B O   1 
HETATM 6188 O  O   . HOH   J 5 .   ? 35.356 120.379 56.804 1.00 35.56 ? 1062 HOH   B O   1 
HETATM 6189 O  O   . HOH   J 5 .   ? 28.931 79.498  60.227 1.00 22.35 ? 1063 HOH   B O   1 
HETATM 6190 O  O   . HOH   J 5 .   ? 18.863 86.220  24.434 1.00 33.72 ? 1064 HOH   B O   1 
HETATM 6191 O  O   . HOH   J 5 .   ? 21.588 79.491  66.146 1.00 18.93 ? 1065 HOH   B O   1 
HETATM 6192 O  O   . HOH   J 5 .   ? 3.683  88.642  68.927 1.00 19.35 ? 1066 HOH   B O   1 
HETATM 6193 O  O   . HOH   J 5 .   ? 25.597 74.234  65.974 1.00 30.64 ? 1067 HOH   B O   1 
HETATM 6194 O  O   . HOH   J 5 .   ? 35.106 105.105 48.169 1.00 18.81 ? 1068 HOH   B O   1 
HETATM 6195 O  O   . HOH   J 5 .   ? 1.732  82.350  59.978 1.00 34.22 ? 1069 HOH   B O   1 
HETATM 6196 O  O   . HOH   J 5 .   ? 0.088  83.902  65.746 1.00 31.29 ? 1070 HOH   B O   1 
HETATM 6197 O  O   . HOH   J 5 .   ? 7.785  108.969 57.579 1.00 27.49 ? 1071 HOH   B O   1 
HETATM 6198 O  O   . HOH   J 5 .   ? 25.253 104.782 33.444 1.00 22.74 ? 1072 HOH   B O   1 
HETATM 6199 O  O   . HOH   J 5 .   ? 35.491 105.017 56.984 1.00 29.60 ? 1073 HOH   B O   1 
HETATM 6200 O  O   . HOH   J 5 .   ? 5.132  105.583 36.322 1.00 40.48 ? 1074 HOH   B O   1 
HETATM 6201 O  O   . HOH   J 5 .   ? 19.121 97.846  64.904 1.00 43.93 ? 1075 HOH   B O   1 
HETATM 6202 O  O   . HOH   J 5 .   ? 25.443 102.585 30.626 1.00 39.42 ? 1076 HOH   B O   1 
HETATM 6203 O  O   . HOH   J 5 .   ? 35.169 86.076  29.589 1.00 23.69 ? 1077 HOH   B O   1 
HETATM 6204 O  O   . HOH   J 5 .   ? 18.822 103.272 49.186 1.00 15.56 ? 1078 HOH   B O   1 
HETATM 6205 O  O   . HOH   J 5 .   ? 31.294 109.751 57.007 1.00 20.12 ? 1079 HOH   B O   1 
HETATM 6206 O  O   . HOH   J 5 .   ? 9.741  95.370  64.844 1.00 44.04 ? 1080 HOH   B O   1 
HETATM 6207 O  O   . HOH   J 5 .   ? 6.533  76.856  42.618 1.00 32.33 ? 1081 HOH   B O   1 
HETATM 6208 O  O   . HOH   J 5 .   ? 19.344 108.004 63.450 1.00 30.11 ? 1082 HOH   B O   1 
HETATM 6209 O  O   . HOH   J 5 .   ? 31.177 102.228 63.270 1.00 25.08 ? 1083 HOH   B O   1 
HETATM 6210 O  O   . HOH   J 5 .   ? 37.159 85.094  43.031 1.00 27.48 ? 1084 HOH   B O   1 
HETATM 6211 O  O   . HOH   J 5 .   ? 39.937 98.147  48.072 1.00 35.64 ? 1085 HOH   B O   1 
HETATM 6212 O  O   . HOH   J 5 .   ? 18.520 71.007  66.033 1.00 41.27 ? 1086 HOH   B O   1 
HETATM 6213 O  O   . HOH   J 5 .   ? 23.699 75.693  64.548 1.00 27.21 ? 1087 HOH   B O   1 
HETATM 6214 O  O   . HOH   J 5 .   ? 22.016 77.399  28.552 1.00 39.00 ? 1088 HOH   B O   1 
HETATM 6215 O  O   . HOH   J 5 .   ? 13.157 115.566 54.522 1.00 33.06 ? 1089 HOH   B O   1 
HETATM 6216 O  O   . HOH   J 5 .   ? 31.743 114.932 49.149 1.00 27.26 ? 1090 HOH   B O   1 
HETATM 6217 O  O   . HOH   J 5 .   ? 35.451 101.250 36.959 1.00 40.81 ? 1091 HOH   B O   1 
HETATM 6218 O  O   . HOH   J 5 .   ? 21.190 76.694  65.199 1.00 31.30 ? 1092 HOH   B O   1 
HETATM 6219 O  O   . HOH   J 5 .   ? 32.021 90.109  23.548 1.00 32.98 ? 1093 HOH   B O   1 
HETATM 6220 O  O   . HOH   J 5 .   ? 17.138 88.011  25.277 1.00 41.08 ? 1094 HOH   B O   1 
HETATM 6221 O  O   . HOH   J 5 .   ? 26.377 92.449  25.916 1.00 22.84 ? 1095 HOH   B O   1 
HETATM 6222 O  O   . HOH   J 5 .   ? 1.215  98.237  38.407 1.00 29.62 ? 1096 HOH   B O   1 
HETATM 6223 O  O   . HOH   J 5 .   ? 21.589 117.213 60.373 1.00 23.15 ? 1097 HOH   B O   1 
HETATM 6224 O  O   . HOH   J 5 .   ? 31.484 99.266  33.625 1.00 34.31 ? 1098 HOH   B O   1 
HETATM 6225 O  O   . HOH   J 5 .   ? 34.788 98.487  36.313 1.00 34.32 ? 1099 HOH   B O   1 
HETATM 6226 O  O   . HOH   J 5 .   ? 39.111 89.821  37.305 1.00 27.93 ? 1100 HOH   B O   1 
HETATM 6227 O  O   . HOH   J 5 .   ? 22.244 98.531  27.832 1.00 30.25 ? 1101 HOH   B O   1 
HETATM 6228 O  O   . HOH   J 5 .   ? 0.023  96.040  36.764 1.00 31.02 ? 1102 HOH   B O   1 
HETATM 6229 O  O   . HOH   J 5 .   ? 15.152 111.121 38.774 1.00 34.75 ? 1103 HOH   B O   1 
HETATM 6230 O  O   . HOH   J 5 .   ? 11.158 114.151 46.717 1.00 29.02 ? 1104 HOH   B O   1 
HETATM 6231 O  O   . HOH   J 5 .   ? 15.201 74.374  68.642 1.00 41.69 ? 1105 HOH   B O   1 
HETATM 6232 O  O   . HOH   J 5 .   ? 19.504 117.552 49.983 1.00 36.57 ? 1106 HOH   B O   1 
HETATM 6233 O  O   . HOH   J 5 .   ? 25.256 85.504  27.000 1.00 33.68 ? 1107 HOH   B O   1 
HETATM 6234 O  O   . HOH   J 5 .   ? 11.950 106.915 35.380 1.00 27.43 ? 1108 HOH   B O   1 
HETATM 6235 O  O   . HOH   J 5 .   ? 24.193 74.822  31.770 1.00 41.50 ? 1109 HOH   B O   1 
HETATM 6236 O  O   . HOH   J 5 .   ? -2.086 85.427  58.078 1.00 38.74 ? 1110 HOH   B O   1 
HETATM 6237 O  O   . HOH   J 5 .   ? 34.243 74.377  58.193 1.00 36.37 ? 1111 HOH   B O   1 
HETATM 6238 O  O   . HOH   J 5 .   ? 14.412 102.184 63.532 1.00 20.21 ? 1112 HOH   B O   1 
HETATM 6239 O  O   . HOH   J 5 .   ? 17.487 92.604  24.613 1.00 39.92 ? 1113 HOH   B O   1 
HETATM 6240 O  O   . HOH   J 5 .   ? 4.328  86.371  34.969 1.00 41.50 ? 1114 HOH   B O   1 
HETATM 6241 O  O   . HOH   J 5 .   ? 9.269  85.802  67.340 1.00 24.19 ? 1115 HOH   B O   1 
HETATM 6242 O  O   . HOH   J 5 .   ? 19.254 93.585  64.762 1.00 23.29 ? 1116 HOH   B O   1 
HETATM 6243 O  O   . HOH   J 5 .   ? 39.522 98.012  41.838 1.00 27.30 ? 1117 HOH   B O   1 
HETATM 6244 O  O   . HOH   J 5 .   ? 26.580 68.133  42.547 1.00 42.67 ? 1118 HOH   B O   1 
HETATM 6245 O  O   . HOH   J 5 .   ? 14.724 97.885  65.361 1.00 38.68 ? 1119 HOH   B O   1 
HETATM 6246 O  O   . HOH   J 5 .   ? -2.019 91.304  54.366 1.00 38.50 ? 1120 HOH   B O   1 
HETATM 6247 O  O   . HOH   J 5 .   ? 26.448 66.360  44.318 1.00 40.13 ? 1121 HOH   B O   1 
HETATM 6248 O  O   . HOH   J 5 .   ? 11.445 93.707  67.721 1.00 39.83 ? 1122 HOH   B O   1 
HETATM 6249 O  O   . HOH   J 5 .   ? 33.344 100.913 57.771 1.00 36.21 ? 1123 HOH   B O   1 
HETATM 6250 O  O   . HOH   J 5 .   ? 20.849 79.480  69.766 1.00 42.75 ? 1124 HOH   B O   1 
HETATM 6251 O  O   . HOH   J 5 .   ? 6.460  76.479  39.129 1.00 38.48 ? 1125 HOH   B O   1 
HETATM 6252 O  O   . HOH   J 5 .   ? 10.616 110.967 62.661 1.00 18.45 ? 1126 HOH   B O   1 
HETATM 6253 O  O   . HOH   J 5 .   ? 22.469 115.494 43.033 1.00 35.87 ? 1127 HOH   B O   1 
HETATM 6254 O  O   . HOH   J 5 .   ? 31.271 93.212  63.879 1.00 41.88 ? 1128 HOH   B O   1 
HETATM 6255 O  O   . HOH   J 5 .   ? 16.161 104.708 66.435 1.00 34.53 ? 1129 HOH   B O   1 
HETATM 6256 O  O   . HOH   J 5 .   ? 17.137 86.667  72.160 1.00 39.56 ? 1130 HOH   B O   1 
HETATM 6257 O  O   . HOH   J 5 .   ? 27.303 123.220 55.849 1.00 36.00 ? 1131 HOH   B O   1 
HETATM 6258 O  O   . HOH   J 5 .   ? 8.400  89.664  29.017 1.00 29.70 ? 1132 HOH   B O   1 
HETATM 6259 O  O   . HOH   J 5 .   ? 19.236 68.852  65.167 1.00 42.33 ? 1133 HOH   B O   1 
HETATM 6260 O  O   . HOH   J 5 .   ? 6.538  72.149  49.040 1.00 36.74 ? 1134 HOH   B O   1 
HETATM 6261 O  O   . HOH   J 5 .   ? 31.047 68.642  60.060 1.00 41.89 ? 1135 HOH   B O   1 
HETATM 6262 O  O   . HOH   J 5 .   ? 18.178 74.006  27.375 1.00 40.20 ? 1136 HOH   B O   1 
HETATM 6263 O  O   . HOH   J 5 .   ? 42.195 111.281 51.852 1.00 45.27 ? 1137 HOH   B O   1 
HETATM 6264 O  O   . HOH   J 5 .   ? 27.413 116.344 62.094 1.00 39.47 ? 1138 HOH   B O   1 
HETATM 6265 O  O   . HOH   J 5 .   ? 32.781 119.803 68.067 1.00 39.09 ? 1139 HOH   B O   1 
HETATM 6266 O  O   . HOH   J 5 .   ? 36.596 83.734  60.873 1.00 39.35 ? 1140 HOH   B O   1 
HETATM 6267 O  O   . HOH   J 5 .   ? 22.115 110.981 63.509 1.00 37.30 ? 1141 HOH   B O   1 
HETATM 6268 O  O   . HOH   J 5 .   ? 11.642 68.481  51.444 1.00 42.83 ? 1142 HOH   B O   1 
HETATM 6269 O  O   . HOH   J 5 .   ? 18.430 119.827 51.915 1.00 31.60 ? 1143 HOH   B O   1 
HETATM 6270 O  O   . HOH   J 5 .   ? 40.848 99.405  45.772 1.00 37.75 ? 1144 HOH   B O   1 
HETATM 6271 O  O   . HOH   J 5 .   ? 40.145 102.336 44.799 1.00 43.54 ? 1145 HOH   B O   1 
HETATM 6272 O  O   . HOH   J 5 .   ? 31.482 74.042  50.208 1.00 23.15 ? 1146 HOH   B O   1 
HETATM 6273 O  O   . HOH   J 5 .   ? 23.863 87.884  62.698 1.00 23.72 ? 1147 HOH   B O   1 
HETATM 6274 O  O   . HOH   J 5 .   ? 5.335  108.325 57.007 1.00 41.61 ? 1148 HOH   B O   1 
HETATM 6275 O  O   . HOH   J 5 .   ? 9.089  110.227 40.535 1.00 35.88 ? 1149 HOH   B O   1 
HETATM 6276 O  O   . HOH   J 5 .   ? 2.046  100.999 37.417 1.00 35.39 ? 1150 HOH   B O   1 
HETATM 6277 O  O   . HOH   J 5 .   ? 0.306  91.532  33.222 1.00 33.69 ? 1151 HOH   B O   1 
HETATM 6278 O  O   . HOH   J 5 .   ? 31.041 73.841  45.949 1.00 32.45 ? 1152 HOH   B O   1 
HETATM 6279 O  O   . HOH   J 5 .   ? 10.890 99.129  62.850 1.00 39.97 ? 1153 HOH   B O   1 
HETATM 6280 O  O   . HOH   J 5 .   ? 38.652 91.308  47.592 1.00 19.90 ? 1154 HOH   B O   1 
HETATM 6281 O  O   . HOH   J 5 .   ? 33.348 103.861 57.994 1.00 44.90 ? 1155 HOH   B O   1 
HETATM 6282 O  O   . HOH   J 5 .   ? 19.696 123.078 53.236 1.00 32.20 ? 1156 HOH   B O   1 
HETATM 6283 O  O   . HOH   J 5 .   ? 15.208 92.207  25.662 1.00 31.56 ? 1157 HOH   B O   1 
HETATM 6284 O  O   . HOH   J 5 .   ? -0.260 91.269  40.425 1.00 35.87 ? 1158 HOH   B O   1 
HETATM 6285 O  O   . HOH   J 5 .   ? 1.235  103.079 49.823 1.00 29.93 ? 1159 HOH   B O   1 
HETATM 6286 O  O   . HOH   J 5 .   ? 14.700 78.556  33.083 1.00 37.89 ? 1160 HOH   B O   1 
HETATM 6287 O  O   . HOH   J 5 .   ? 3.955  91.215  69.649 1.00 23.63 ? 1161 HOH   B O   1 
HETATM 6288 O  O   . HOH   J 5 .   ? 3.873  96.823  59.667 1.00 37.92 ? 1162 HOH   B O   1 
HETATM 6289 O  O   . HOH   J 5 .   ? 29.322 70.765  64.764 1.00 40.61 ? 1163 HOH   B O   1 
HETATM 6290 O  O   . HOH   J 5 .   ? -0.004 88.464  68.258 1.00 39.43 ? 1164 HOH   B O   1 
HETATM 6291 O  O   . HOH   J 5 .   ? 39.017 93.349  49.082 1.00 41.84 ? 1165 HOH   B O   1 
HETATM 6292 O  O   . HOH   J 5 .   ? 9.087  99.805  60.932 1.00 41.92 ? 1166 HOH   B O   1 
HETATM 6293 O  O   . HOH   J 5 .   ? 22.852 109.099 64.729 1.00 42.30 ? 1167 HOH   B O   1 
HETATM 6294 O  O   . HOH   J 5 .   ? 10.340 105.113 33.708 1.00 37.69 ? 1168 HOH   B O   1 
HETATM 6295 O  O   . HOH   J 5 .   ? 28.769 62.911  61.680 1.00 42.34 ? 1169 HOH   B O   1 
HETATM 6296 O  O   . HOH   J 5 .   ? -7.308 90.250  48.837 1.00 42.57 ? 1170 HOH   B O   1 
HETATM 6297 O  O   . HOH   J 5 .   ? 10.880 102.352 33.843 1.00 38.46 ? 1171 HOH   B O   1 
HETATM 6298 O  O   . HOH   J 5 .   ? 17.839 94.241  70.660 1.00 38.88 ? 1172 HOH   B O   1 
HETATM 6299 O  O   . HOH   J 5 .   ? 38.361 95.901  47.565 1.00 30.51 ? 1173 HOH   B O   1 
HETATM 6300 O  O   . HOH   J 5 .   ? 21.026 95.602  64.979 1.00 41.41 ? 1174 HOH   B O   1 
HETATM 6301 O  O   . HOH   J 5 .   ? 32.630 66.350  40.103 1.00 41.29 ? 1175 HOH   B O   1 
HETATM 6302 O  O   . HOH   J 5 .   ? 18.045 119.650 54.417 1.00 33.29 ? 1176 HOH   B O   1 
HETATM 6303 O  O   . HOH   J 5 .   ? 33.049 93.795  25.812 1.00 43.15 ? 1177 HOH   B O   1 
HETATM 6304 O  O   . HOH   J 5 .   ? 2.962  105.847 47.771 1.00 40.80 ? 1178 HOH   B O   1 
HETATM 6305 O  O   . HOH   J 5 .   ? 18.124 69.872  45.946 1.00 43.71 ? 1179 HOH   B O   1 
HETATM 6306 O  O   . HOH   J 5 .   ? 3.356  79.542  41.510 1.00 41.82 ? 1180 HOH   B O   1 
HETATM 6307 O  O   . HOH   J 5 .   ? 36.658 100.718 57.781 1.00 37.09 ? 1181 HOH   B O   1 
HETATM 6308 O  O   . HOH   J 5 .   ? 18.430 66.759  68.537 1.00 41.88 ? 1182 HOH   B O   1 
HETATM 6309 O  O   . HOH   J 5 .   ? 1.506  87.533  69.957 1.00 38.71 ? 1183 HOH   B O   1 
HETATM 6310 O  O   . HOH   J 5 .   ? 16.547 102.493 64.767 1.00 35.15 ? 1184 HOH   B O   1 
HETATM 6311 O  O   . HOH   J 5 .   ? -0.126 80.572  61.515 1.00 29.84 ? 1185 HOH   B O   1 
HETATM 6312 O  O   . HOH   J 5 .   ? 12.312 113.300 42.319 1.00 41.31 ? 1186 HOH   B O   1 
HETATM 6313 O  O   . HOH   J 5 .   ? 41.745 113.096 54.152 1.00 42.14 ? 1187 HOH   B O   1 
HETATM 6314 O  O   . HOH   J 5 .   ? 35.829 105.815 41.819 1.00 43.55 ? 1188 HOH   B O   1 
HETATM 6315 O  O   . HOH   J 5 .   ? 6.914  87.175  30.569 1.00 37.94 ? 1189 HOH   B O   1 
HETATM 6316 O  O   . HOH   J 5 .   ? 10.244 79.148  68.201 1.00 34.75 ? 1190 HOH   B O   1 
HETATM 6317 O  O   . HOH   J 5 .   ? -7.532 93.614  48.977 1.00 38.10 ? 1191 HOH   B O   1 
HETATM 6318 O  O   . HOH   J 5 .   ? 24.689 98.873  26.238 1.00 37.62 ? 1192 HOH   B O   1 
HETATM 6319 O  O   . HOH   J 5 .   ? 36.769 83.888  40.988 1.00 42.71 ? 1193 HOH   B O   1 
HETATM 6320 O  O   . HOH   J 5 .   ? 33.700 74.062  44.854 1.00 38.98 ? 1194 HOH   B O   1 
HETATM 6321 O  O   . HOH   J 5 .   ? 34.984 94.839  28.158 1.00 31.30 ? 1195 HOH   B O   1 
HETATM 6322 O  O   . HOH   J 5 .   ? 4.456  108.535 46.005 1.00 40.47 ? 1196 HOH   B O   1 
HETATM 6323 O  O   . HOH   J 5 .   ? 5.531  110.256 42.568 1.00 41.38 ? 1197 HOH   B O   1 
HETATM 6324 O  O   . HOH   J 5 .   ? 12.263 102.918 65.019 1.00 36.10 ? 1198 HOH   B O   1 
HETATM 6325 O  O   . HOH   J 5 .   ? 18.636 104.007 29.960 1.00 43.29 ? 1199 HOH   B O   1 
HETATM 6326 O  O   . HOH   J 5 .   ? 3.541  105.876 42.288 1.00 34.23 ? 1200 HOH   B O   1 
HETATM 6327 O  O   . HOH   J 5 .   ? 37.724 107.645 46.008 1.00 30.02 ? 1201 HOH   B O   1 
HETATM 6328 O  O   . HOH   J 5 .   ? 22.585 86.843  21.871 1.00 41.46 ? 1202 HOH   B O   1 
HETATM 6329 O  O   . HOH   J 5 .   ? 17.557 115.409 44.907 1.00 44.39 ? 1203 HOH   B O   1 
HETATM 6330 O  O   . HOH   J 5 .   ? 15.960 73.041  40.875 1.00 35.51 ? 1204 HOH   B O   1 
HETATM 6331 O  O   . HOH   J 5 .   ? 12.378 78.055  68.346 1.00 34.95 ? 1205 HOH   B O   1 
HETATM 6332 O  O   . HOH   J 5 .   ? 23.802 68.889  37.943 1.00 45.28 ? 1206 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 
5739 K K . K E . ? 0.2701 0.2669 0.2330 -0.0280 0.0607 0.0038  803 K A K 
5768 K K . K H . ? 0.2436 0.2299 0.2125 -0.0153 0.0241 -0.0027 803 K B K 
# 
