data_9MQP
# 
_entry.id   9MQP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9MQP         pdb_00009mqp 10.2210/pdb9mqp/pdb 
WWPDB D_1000291533 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MQP 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-04 
_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              chris@sas.upenn.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Christianson 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0194-5212 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Goulart Stollmaier, J.' 1 0000-0002-5110-8818 
'Czarnecki, B.A.R.'      2 0009-0008-8279-476X 
'Christianson, D.W.'     3 0000-0002-0194-5212 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                6373 
_citation.page_last                 6377 
_citation.title                     
'Mechanism-Based Inhibition of Histone Deacetylase 6 by a Selenocyanate Is Subject to Redox Modulation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.5c00157 
_citation.pdbx_database_id_PubMed   39957581 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Goulart Stollmaier, J.' 1 ? 
primary 'Czarnecki, B.A.R.'      2 ? 
primary 'Christianson, D.W.'     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'              40285.484 2   ? ? 'catalytic domain 2' ? 
2 non-polymer syn N-phenyl-6-selanylhexanamide 270.229   2   ? ? ?                    ? 
3 non-polymer syn 1,2-ETHANEDIOL               62.068    2   ? ? ?                    ? 
4 non-polymer syn 'ZINC ION'                   65.409    2   ? ? ?                    ? 
5 non-polymer syn 'POTASSIUM ION'              39.098    4   ? ? ?                    ? 
6 water       nat water                        18.015    204 ? ? ?                    ? 
# 
_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       
;SNAGGSSPITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSS
EHMKPRDLNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTAR
YAQSITRESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMG
DPEYMAAFHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESM
SMCTSMLLGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAGGSSPITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSS
EHMKPRDLNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTAR
YAQSITRESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMG
DPEYMAAFHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESM
SMCTSMLLGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_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-phenyl-6-selanylhexanamide A1BNN 
3 1,2-ETHANEDIOL               EDO   
4 'ZINC ION'                   ZN    
5 'POTASSIUM ION'              K     
6 water                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   GLY n 
1 5   GLY n 
1 6   SER n 
1 7   SER n 
1 8   PRO n 
1 9   ILE n 
1 10  THR n 
1 11  GLY n 
1 12  LEU n 
1 13  VAL n 
1 14  TYR n 
1 15  ASP n 
1 16  GLN n 
1 17  ARG n 
1 18  MET n 
1 19  MET n 
1 20  LEU n 
1 21  HIS n 
1 22  HIS n 
1 23  ASN n 
1 24  MET n 
1 25  TRP n 
1 26  ASP n 
1 27  SER n 
1 28  HIS n 
1 29  HIS n 
1 30  PRO n 
1 31  GLU n 
1 32  LEU n 
1 33  PRO n 
1 34  GLN n 
1 35  ARG n 
1 36  ILE n 
1 37  SER n 
1 38  ARG n 
1 39  ILE n 
1 40  PHE n 
1 41  SER n 
1 42  ARG n 
1 43  HIS n 
1 44  GLU n 
1 45  GLU n 
1 46  LEU n 
1 47  ARG n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  ARG n 
1 52  CYS n 
1 53  HIS n 
1 54  ARG n 
1 55  ILE n 
1 56  PRO n 
1 57  ALA n 
1 58  ARG n 
1 59  LEU n 
1 60  ALA n 
1 61  THR n 
1 62  GLU n 
1 63  GLU n 
1 64  GLU n 
1 65  LEU n 
1 66  ALA n 
1 67  LEU n 
1 68  CYS n 
1 69  HIS n 
1 70  SER n 
1 71  SER n 
1 72  LYS n 
1 73  HIS n 
1 74  ILE n 
1 75  SER n 
1 76  ILE n 
1 77  ILE n 
1 78  LYS n 
1 79  SER n 
1 80  SER n 
1 81  GLU n 
1 82  HIS n 
1 83  MET n 
1 84  LYS n 
1 85  PRO n 
1 86  ARG n 
1 87  ASP n 
1 88  LEU n 
1 89  ASN n 
1 90  ARG n 
1 91  LEU n 
1 92  GLY n 
1 93  ASP n 
1 94  GLU n 
1 95  TYR n 
1 96  ASN n 
1 97  SER n 
1 98  ILE n 
1 99  PHE n 
1 100 ILE n 
1 101 SER n 
1 102 ASN n 
1 103 GLU n 
1 104 SER n 
1 105 TYR n 
1 106 THR n 
1 107 CYS n 
1 108 ALA n 
1 109 LEU n 
1 110 LEU n 
1 111 ALA n 
1 112 ALA n 
1 113 GLY n 
1 114 SER n 
1 115 CYS n 
1 116 PHE n 
1 117 ASN n 
1 118 SER n 
1 119 ALA n 
1 120 GLN n 
1 121 ALA n 
1 122 ILE n 
1 123 LEU n 
1 124 THR n 
1 125 GLY n 
1 126 GLN n 
1 127 VAL n 
1 128 ARG n 
1 129 ASN n 
1 130 ALA n 
1 131 VAL n 
1 132 ALA n 
1 133 ILE n 
1 134 VAL n 
1 135 ARG n 
1 136 PRO n 
1 137 PRO n 
1 138 GLY n 
1 139 HIS n 
1 140 HIS n 
1 141 ALA n 
1 142 GLU n 
1 143 LYS n 
1 144 ASP n 
1 145 THR n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 PHE n 
1 150 CYS n 
1 151 PHE n 
1 152 PHE n 
1 153 ASN n 
1 154 THR n 
1 155 ALA n 
1 156 ALA n 
1 157 LEU n 
1 158 THR n 
1 159 ALA n 
1 160 ARG n 
1 161 TYR n 
1 162 ALA n 
1 163 GLN n 
1 164 SER n 
1 165 ILE n 
1 166 THR n 
1 167 ARG n 
1 168 GLU n 
1 169 SER n 
1 170 LEU n 
1 171 ARG n 
1 172 VAL n 
1 173 LEU n 
1 174 ILE n 
1 175 VAL n 
1 176 ASP n 
1 177 TRP n 
1 178 ASP n 
1 179 VAL n 
1 180 HIS n 
1 181 HIS n 
1 182 GLY n 
1 183 ASN n 
1 184 GLY n 
1 185 THR n 
1 186 GLN n 
1 187 HIS n 
1 188 ILE n 
1 189 PHE n 
1 190 GLU n 
1 191 GLU n 
1 192 ASP n 
1 193 ASP n 
1 194 SER n 
1 195 VAL n 
1 196 LEU n 
1 197 TYR n 
1 198 ILE n 
1 199 SER n 
1 200 LEU n 
1 201 HIS n 
1 202 ARG n 
1 203 TYR n 
1 204 GLU n 
1 205 ASP n 
1 206 GLY n 
1 207 ALA n 
1 208 PHE n 
1 209 PHE n 
1 210 PRO n 
1 211 ASN n 
1 212 SER n 
1 213 GLU n 
1 214 ASP n 
1 215 ALA n 
1 216 ASN n 
1 217 TYR n 
1 218 ASP n 
1 219 LYS n 
1 220 VAL n 
1 221 GLY n 
1 222 LEU n 
1 223 GLY n 
1 224 LYS n 
1 225 GLY n 
1 226 ARG n 
1 227 GLY n 
1 228 TYR n 
1 229 ASN n 
1 230 VAL n 
1 231 ASN n 
1 232 ILE n 
1 233 PRO n 
1 234 TRP n 
1 235 ASN n 
1 236 GLY n 
1 237 GLY n 
1 238 LYS n 
1 239 MET n 
1 240 GLY n 
1 241 ASP n 
1 242 PRO n 
1 243 GLU n 
1 244 TYR n 
1 245 MET n 
1 246 ALA n 
1 247 ALA n 
1 248 PHE n 
1 249 HIS n 
1 250 HIS n 
1 251 LEU n 
1 252 VAL n 
1 253 MET n 
1 254 PRO n 
1 255 ILE n 
1 256 ALA n 
1 257 ARG n 
1 258 GLU n 
1 259 PHE n 
1 260 ALA n 
1 261 PRO n 
1 262 GLU n 
1 263 LEU n 
1 264 VAL n 
1 265 LEU n 
1 266 VAL n 
1 267 SER n 
1 268 ALA n 
1 269 GLY n 
1 270 PHE n 
1 271 ASP n 
1 272 ALA n 
1 273 ALA n 
1 274 ARG n 
1 275 GLY n 
1 276 ASP n 
1 277 PRO n 
1 278 LEU n 
1 279 GLY n 
1 280 GLY n 
1 281 PHE n 
1 282 GLN n 
1 283 VAL n 
1 284 THR n 
1 285 PRO n 
1 286 GLU n 
1 287 GLY n 
1 288 TYR n 
1 289 ALA n 
1 290 HIS n 
1 291 LEU n 
1 292 THR n 
1 293 HIS n 
1 294 GLN n 
1 295 LEU n 
1 296 MET n 
1 297 SER n 
1 298 LEU n 
1 299 ALA n 
1 300 ALA n 
1 301 GLY n 
1 302 ARG n 
1 303 VAL n 
1 304 LEU n 
1 305 ILE n 
1 306 ILE n 
1 307 LEU n 
1 308 GLU n 
1 309 GLY n 
1 310 GLY n 
1 311 TYR n 
1 312 ASN n 
1 313 LEU n 
1 314 THR n 
1 315 SER n 
1 316 ILE n 
1 317 SER n 
1 318 GLU n 
1 319 SER n 
1 320 MET n 
1 321 SER n 
1 322 MET n 
1 323 CYS n 
1 324 THR n 
1 325 SER n 
1 326 MET n 
1 327 LEU n 
1 328 LEU n 
1 329 GLY n 
1 330 ASP n 
1 331 SER n 
1 332 PRO n 
1 333 PRO n 
1 334 SER n 
1 335 LEU n 
1 336 ASP n 
1 337 HIS n 
1 338 LEU n 
1 339 THR n 
1 340 PRO n 
1 341 LEU n 
1 342 LYS n 
1 343 THR n 
1 344 SER n 
1 345 ALA n 
1 346 THR n 
1 347 VAL n 
1 348 SER n 
1 349 ILE n 
1 350 ASN n 
1 351 ASN n 
1 352 VAL n 
1 353 LEU n 
1 354 ARG n 
1 355 ALA n 
1 356 HIS n 
1 357 ALA n 
1 358 PRO n 
1 359 PHE n 
1 360 TRP n 
1 361 SER n 
1 362 SER n 
1 363 LEU n 
1 364 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                   364 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BNN non-polymer         . N-phenyl-6-selanylhexanamide ?                 'C12 H17 N O Se' 270.229 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL               'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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   SER 1   435 ?   ?   ?   A . n 
A 1 2   ASN 2   436 ?   ?   ?   A . n 
A 1 3   ALA 3   437 ?   ?   ?   A . n 
A 1 4   GLY 4   438 ?   ?   ?   A . n 
A 1 5   GLY 5   439 ?   ?   ?   A . n 
A 1 6   SER 6   440 ?   ?   ?   A . n 
A 1 7   SER 7   441 ?   ?   ?   A . n 
A 1 8   PRO 8   442 442 PRO PRO A . n 
A 1 9   ILE 9   443 443 ILE ILE A . n 
A 1 10  THR 10  444 444 THR THR A . n 
A 1 11  GLY 11  445 445 GLY GLY A . n 
A 1 12  LEU 12  446 446 LEU LEU A . n 
A 1 13  VAL 13  447 447 VAL VAL A . n 
A 1 14  TYR 14  448 448 TYR TYR A . n 
A 1 15  ASP 15  449 449 ASP ASP A . n 
A 1 16  GLN 16  450 450 GLN GLN A . n 
A 1 17  ARG 17  451 451 ARG ARG A . n 
A 1 18  MET 18  452 452 MET MET A . n 
A 1 19  MET 19  453 453 MET MET A . n 
A 1 20  LEU 20  454 454 LEU LEU A . n 
A 1 21  HIS 21  455 455 HIS HIS A . n 
A 1 22  HIS 22  456 456 HIS HIS A . n 
A 1 23  ASN 23  457 457 ASN ASN A . n 
A 1 24  MET 24  458 458 MET MET A . n 
A 1 25  TRP 25  459 459 TRP TRP A . n 
A 1 26  ASP 26  460 460 ASP ASP A . n 
A 1 27  SER 27  461 461 SER SER A . n 
A 1 28  HIS 28  462 462 HIS HIS A . n 
A 1 29  HIS 29  463 463 HIS HIS A . n 
A 1 30  PRO 30  464 464 PRO PRO A . n 
A 1 31  GLU 31  465 465 GLU GLU A . n 
A 1 32  LEU 32  466 466 LEU LEU A . n 
A 1 33  PRO 33  467 467 PRO PRO A . n 
A 1 34  GLN 34  468 468 GLN GLN A . n 
A 1 35  ARG 35  469 469 ARG ARG A . n 
A 1 36  ILE 36  470 470 ILE ILE A . n 
A 1 37  SER 37  471 471 SER SER A . n 
A 1 38  ARG 38  472 472 ARG ARG A . n 
A 1 39  ILE 39  473 473 ILE ILE A . n 
A 1 40  PHE 40  474 474 PHE PHE A . n 
A 1 41  SER 41  475 475 SER SER A . n 
A 1 42  ARG 42  476 476 ARG ARG A . n 
A 1 43  HIS 43  477 477 HIS HIS A . n 
A 1 44  GLU 44  478 478 GLU GLU A . n 
A 1 45  GLU 45  479 479 GLU GLU A . n 
A 1 46  LEU 46  480 480 LEU LEU A . n 
A 1 47  ARG 47  481 481 ARG ARG A . n 
A 1 48  LEU 48  482 482 LEU LEU A . n 
A 1 49  LEU 49  483 483 LEU LEU A . n 
A 1 50  SER 50  484 484 SER SER A . n 
A 1 51  ARG 51  485 485 ARG ARG A . n 
A 1 52  CYS 52  486 486 CYS CYS A . n 
A 1 53  HIS 53  487 487 HIS HIS A . n 
A 1 54  ARG 54  488 488 ARG ARG A . n 
A 1 55  ILE 55  489 489 ILE ILE A . n 
A 1 56  PRO 56  490 490 PRO PRO A . n 
A 1 57  ALA 57  491 491 ALA ALA A . n 
A 1 58  ARG 58  492 492 ARG ARG A . n 
A 1 59  LEU 59  493 493 LEU LEU A . n 
A 1 60  ALA 60  494 494 ALA ALA A . n 
A 1 61  THR 61  495 495 THR THR A . n 
A 1 62  GLU 62  496 496 GLU GLU A . n 
A 1 63  GLU 63  497 497 GLU GLU A . n 
A 1 64  GLU 64  498 498 GLU GLU A . n 
A 1 65  LEU 65  499 499 LEU LEU A . n 
A 1 66  ALA 66  500 500 ALA ALA A . n 
A 1 67  LEU 67  501 501 LEU LEU A . n 
A 1 68  CYS 68  502 502 CYS CYS A . n 
A 1 69  HIS 69  503 503 HIS HIS A . n 
A 1 70  SER 70  504 504 SER SER A . n 
A 1 71  SER 71  505 505 SER SER A . n 
A 1 72  LYS 72  506 506 LYS LYS A . n 
A 1 73  HIS 73  507 507 HIS HIS A . n 
A 1 74  ILE 74  508 508 ILE ILE A . n 
A 1 75  SER 75  509 509 SER SER A . n 
A 1 76  ILE 76  510 510 ILE ILE A . n 
A 1 77  ILE 77  511 511 ILE ILE A . n 
A 1 78  LYS 78  512 512 LYS LYS A . n 
A 1 79  SER 79  513 513 SER SER A . n 
A 1 80  SER 80  514 514 SER SER A . n 
A 1 81  GLU 81  515 515 GLU GLU A . n 
A 1 82  HIS 82  516 516 HIS HIS A . n 
A 1 83  MET 83  517 517 MET MET A . n 
A 1 84  LYS 84  518 518 LYS LYS A . n 
A 1 85  PRO 85  519 519 PRO PRO A . n 
A 1 86  ARG 86  520 520 ARG ARG A . n 
A 1 87  ASP 87  521 521 ASP ASP A . n 
A 1 88  LEU 88  522 522 LEU LEU A . n 
A 1 89  ASN 89  523 523 ASN ASN A . n 
A 1 90  ARG 90  524 524 ARG ARG A . n 
A 1 91  LEU 91  525 525 LEU LEU A . n 
A 1 92  GLY 92  526 526 GLY GLY A . n 
A 1 93  ASP 93  527 527 ASP ASP A . n 
A 1 94  GLU 94  528 528 GLU GLU A . n 
A 1 95  TYR 95  529 529 TYR TYR A . n 
A 1 96  ASN 96  530 530 ASN ASN A . n 
A 1 97  SER 97  531 531 SER SER A . n 
A 1 98  ILE 98  532 532 ILE ILE A . n 
A 1 99  PHE 99  533 533 PHE PHE A . n 
A 1 100 ILE 100 534 534 ILE ILE A . n 
A 1 101 SER 101 535 535 SER SER A . n 
A 1 102 ASN 102 536 536 ASN ASN A . n 
A 1 103 GLU 103 537 537 GLU GLU A . n 
A 1 104 SER 104 538 538 SER SER A . n 
A 1 105 TYR 105 539 539 TYR TYR A . n 
A 1 106 THR 106 540 540 THR THR A . n 
A 1 107 CYS 107 541 541 CYS CYS A . n 
A 1 108 ALA 108 542 542 ALA ALA A . n 
A 1 109 LEU 109 543 543 LEU LEU A . n 
A 1 110 LEU 110 544 544 LEU LEU A . n 
A 1 111 ALA 111 545 545 ALA ALA A . n 
A 1 112 ALA 112 546 546 ALA ALA A . n 
A 1 113 GLY 113 547 547 GLY GLY A . n 
A 1 114 SER 114 548 548 SER SER A . n 
A 1 115 CYS 115 549 549 CYS CYS A . n 
A 1 116 PHE 116 550 550 PHE PHE A . n 
A 1 117 ASN 117 551 551 ASN ASN A . n 
A 1 118 SER 118 552 552 SER SER A . n 
A 1 119 ALA 119 553 553 ALA ALA A . n 
A 1 120 GLN 120 554 554 GLN GLN A . n 
A 1 121 ALA 121 555 555 ALA ALA A . n 
A 1 122 ILE 122 556 556 ILE ILE A . n 
A 1 123 LEU 123 557 557 LEU LEU A . n 
A 1 124 THR 124 558 558 THR THR A . n 
A 1 125 GLY 125 559 559 GLY GLY A . n 
A 1 126 GLN 126 560 560 GLN GLN A . n 
A 1 127 VAL 127 561 561 VAL VAL A . n 
A 1 128 ARG 128 562 562 ARG ARG A . n 
A 1 129 ASN 129 563 563 ASN ASN A . n 
A 1 130 ALA 130 564 564 ALA ALA A . n 
A 1 131 VAL 131 565 565 VAL VAL A . n 
A 1 132 ALA 132 566 566 ALA ALA A . n 
A 1 133 ILE 133 567 567 ILE ILE A . n 
A 1 134 VAL 134 568 568 VAL VAL A . n 
A 1 135 ARG 135 569 569 ARG ARG A . n 
A 1 136 PRO 136 570 570 PRO PRO A . n 
A 1 137 PRO 137 571 571 PRO PRO A . n 
A 1 138 GLY 138 572 572 GLY GLY A . n 
A 1 139 HIS 139 573 573 HIS HIS A . n 
A 1 140 HIS 140 574 574 HIS HIS A . n 
A 1 141 ALA 141 575 575 ALA ALA A . n 
A 1 142 GLU 142 576 576 GLU GLU A . n 
A 1 143 LYS 143 577 577 LYS LYS A . n 
A 1 144 ASP 144 578 578 ASP ASP A . n 
A 1 145 THR 145 579 579 THR THR A . n 
A 1 146 ALA 146 580 580 ALA ALA A . n 
A 1 147 CYS 147 581 581 CYS CYS A . n 
A 1 148 GLY 148 582 582 GLY GLY A . n 
A 1 149 PHE 149 583 583 PHE PHE A . n 
A 1 150 CYS 150 584 584 CYS CYS A . n 
A 1 151 PHE 151 585 585 PHE PHE A . n 
A 1 152 PHE 152 586 586 PHE PHE A . n 
A 1 153 ASN 153 587 587 ASN ASN A . n 
A 1 154 THR 154 588 588 THR THR A . n 
A 1 155 ALA 155 589 589 ALA ALA A . n 
A 1 156 ALA 156 590 590 ALA ALA A . n 
A 1 157 LEU 157 591 591 LEU LEU A . n 
A 1 158 THR 158 592 592 THR THR A . n 
A 1 159 ALA 159 593 593 ALA ALA A . n 
A 1 160 ARG 160 594 594 ARG ARG A . n 
A 1 161 TYR 161 595 595 TYR TYR A . n 
A 1 162 ALA 162 596 596 ALA ALA A . n 
A 1 163 GLN 163 597 597 GLN GLN A . n 
A 1 164 SER 164 598 598 SER SER A . n 
A 1 165 ILE 165 599 599 ILE ILE A . n 
A 1 166 THR 166 600 600 THR THR A . n 
A 1 167 ARG 167 601 601 ARG ARG A . n 
A 1 168 GLU 168 602 602 GLU GLU A . n 
A 1 169 SER 169 603 603 SER SER A . n 
A 1 170 LEU 170 604 604 LEU LEU A . n 
A 1 171 ARG 171 605 605 ARG ARG A . n 
A 1 172 VAL 172 606 606 VAL VAL A . n 
A 1 173 LEU 173 607 607 LEU LEU A . n 
A 1 174 ILE 174 608 608 ILE ILE A . n 
A 1 175 VAL 175 609 609 VAL VAL A . n 
A 1 176 ASP 176 610 610 ASP ASP A . n 
A 1 177 TRP 177 611 611 TRP TRP A . n 
A 1 178 ASP 178 612 612 ASP ASP A . n 
A 1 179 VAL 179 613 613 VAL VAL A . n 
A 1 180 HIS 180 614 614 HIS HIS A . n 
A 1 181 HIS 181 615 615 HIS HIS A . n 
A 1 182 GLY 182 616 616 GLY GLY A . n 
A 1 183 ASN 183 617 617 ASN ASN A . n 
A 1 184 GLY 184 618 618 GLY GLY A . n 
A 1 185 THR 185 619 619 THR THR A . n 
A 1 186 GLN 186 620 620 GLN GLN A . n 
A 1 187 HIS 187 621 621 HIS HIS A . n 
A 1 188 ILE 188 622 622 ILE ILE A . n 
A 1 189 PHE 189 623 623 PHE PHE A . n 
A 1 190 GLU 190 624 624 GLU GLU A . n 
A 1 191 GLU 191 625 625 GLU GLU A . n 
A 1 192 ASP 192 626 626 ASP ASP A . n 
A 1 193 ASP 193 627 627 ASP ASP A . n 
A 1 194 SER 194 628 628 SER SER A . n 
A 1 195 VAL 195 629 629 VAL VAL A . n 
A 1 196 LEU 196 630 630 LEU LEU A . n 
A 1 197 TYR 197 631 631 TYR TYR A . n 
A 1 198 ILE 198 632 632 ILE ILE A . n 
A 1 199 SER 199 633 633 SER SER A . n 
A 1 200 LEU 200 634 634 LEU LEU A . n 
A 1 201 HIS 201 635 635 HIS HIS A . n 
A 1 202 ARG 202 636 636 ARG ARG A . n 
A 1 203 TYR 203 637 637 TYR TYR A . n 
A 1 204 GLU 204 638 638 GLU GLU A . n 
A 1 205 ASP 205 639 639 ASP ASP A . n 
A 1 206 GLY 206 640 640 GLY GLY A . n 
A 1 207 ALA 207 641 641 ALA ALA A . n 
A 1 208 PHE 208 642 642 PHE PHE A . n 
A 1 209 PHE 209 643 643 PHE PHE A . n 
A 1 210 PRO 210 644 644 PRO PRO A . n 
A 1 211 ASN 211 645 645 ASN ASN A . n 
A 1 212 SER 212 646 646 SER SER A . n 
A 1 213 GLU 213 647 647 GLU GLU A . n 
A 1 214 ASP 214 648 648 ASP ASP A . n 
A 1 215 ALA 215 649 649 ALA ALA A . n 
A 1 216 ASN 216 650 650 ASN ASN A . n 
A 1 217 TYR 217 651 651 TYR TYR A . n 
A 1 218 ASP 218 652 652 ASP ASP A . n 
A 1 219 LYS 219 653 653 LYS LYS A . n 
A 1 220 VAL 220 654 654 VAL VAL A . n 
A 1 221 GLY 221 655 655 GLY GLY A . n 
A 1 222 LEU 222 656 656 LEU LEU A . n 
A 1 223 GLY 223 657 657 GLY GLY A . n 
A 1 224 LYS 224 658 658 LYS LYS A . n 
A 1 225 GLY 225 659 659 GLY GLY A . n 
A 1 226 ARG 226 660 660 ARG ARG A . n 
A 1 227 GLY 227 661 661 GLY GLY A . n 
A 1 228 TYR 228 662 662 TYR TYR A . n 
A 1 229 ASN 229 663 663 ASN ASN A . n 
A 1 230 VAL 230 664 664 VAL VAL A . n 
A 1 231 ASN 231 665 665 ASN ASN A . n 
A 1 232 ILE 232 666 666 ILE ILE A . n 
A 1 233 PRO 233 667 667 PRO PRO A . n 
A 1 234 TRP 234 668 668 TRP TRP A . n 
A 1 235 ASN 235 669 669 ASN ASN A . n 
A 1 236 GLY 236 670 670 GLY GLY A . n 
A 1 237 GLY 237 671 671 GLY GLY A . n 
A 1 238 LYS 238 672 672 LYS LYS A . n 
A 1 239 MET 239 673 673 MET MET A . n 
A 1 240 GLY 240 674 674 GLY GLY A . n 
A 1 241 ASP 241 675 675 ASP ASP A . n 
A 1 242 PRO 242 676 676 PRO PRO A . n 
A 1 243 GLU 243 677 677 GLU GLU A . n 
A 1 244 TYR 244 678 678 TYR TYR A . n 
A 1 245 MET 245 679 679 MET MET A . n 
A 1 246 ALA 246 680 680 ALA ALA A . n 
A 1 247 ALA 247 681 681 ALA ALA A . n 
A 1 248 PHE 248 682 682 PHE PHE A . n 
A 1 249 HIS 249 683 683 HIS HIS A . n 
A 1 250 HIS 250 684 684 HIS HIS A . n 
A 1 251 LEU 251 685 685 LEU LEU A . n 
A 1 252 VAL 252 686 686 VAL VAL A . n 
A 1 253 MET 253 687 687 MET MET A . n 
A 1 254 PRO 254 688 688 PRO PRO A . n 
A 1 255 ILE 255 689 689 ILE ILE A . n 
A 1 256 ALA 256 690 690 ALA ALA A . n 
A 1 257 ARG 257 691 691 ARG ARG A . n 
A 1 258 GLU 258 692 692 GLU GLU A . n 
A 1 259 PHE 259 693 693 PHE PHE A . n 
A 1 260 ALA 260 694 694 ALA ALA A . n 
A 1 261 PRO 261 695 695 PRO PRO A . n 
A 1 262 GLU 262 696 696 GLU GLU A . n 
A 1 263 LEU 263 697 697 LEU LEU A . n 
A 1 264 VAL 264 698 698 VAL VAL A . n 
A 1 265 LEU 265 699 699 LEU LEU A . n 
A 1 266 VAL 266 700 700 VAL VAL A . n 
A 1 267 SER 267 701 701 SER SER A . n 
A 1 268 ALA 268 702 702 ALA ALA A . n 
A 1 269 GLY 269 703 703 GLY GLY A . n 
A 1 270 PHE 270 704 704 PHE PHE A . n 
A 1 271 ASP 271 705 705 ASP ASP A . n 
A 1 272 ALA 272 706 706 ALA ALA A . n 
A 1 273 ALA 273 707 707 ALA ALA A . n 
A 1 274 ARG 274 708 708 ARG ARG A . n 
A 1 275 GLY 275 709 709 GLY GLY A . n 
A 1 276 ASP 276 710 710 ASP ASP A . n 
A 1 277 PRO 277 711 711 PRO PRO A . n 
A 1 278 LEU 278 712 712 LEU LEU A . n 
A 1 279 GLY 279 713 713 GLY GLY A . n 
A 1 280 GLY 280 714 714 GLY GLY A . n 
A 1 281 PHE 281 715 715 PHE PHE A . n 
A 1 282 GLN 282 716 716 GLN GLN A . n 
A 1 283 VAL 283 717 717 VAL VAL A . n 
A 1 284 THR 284 718 718 THR THR A . n 
A 1 285 PRO 285 719 719 PRO PRO A . n 
A 1 286 GLU 286 720 720 GLU GLU A . n 
A 1 287 GLY 287 721 721 GLY GLY A . n 
A 1 288 TYR 288 722 722 TYR TYR A . n 
A 1 289 ALA 289 723 723 ALA ALA A . n 
A 1 290 HIS 290 724 724 HIS HIS A . n 
A 1 291 LEU 291 725 725 LEU LEU A . n 
A 1 292 THR 292 726 726 THR THR A . n 
A 1 293 HIS 293 727 727 HIS HIS A . n 
A 1 294 GLN 294 728 728 GLN GLN A . n 
A 1 295 LEU 295 729 729 LEU LEU A . n 
A 1 296 MET 296 730 730 MET MET A . n 
A 1 297 SER 297 731 731 SER SER A . n 
A 1 298 LEU 298 732 732 LEU LEU A . n 
A 1 299 ALA 299 733 733 ALA ALA A . n 
A 1 300 ALA 300 734 734 ALA ALA A . n 
A 1 301 GLY 301 735 735 GLY GLY A . n 
A 1 302 ARG 302 736 736 ARG ARG A . n 
A 1 303 VAL 303 737 737 VAL VAL A . n 
A 1 304 LEU 304 738 738 LEU LEU A . n 
A 1 305 ILE 305 739 739 ILE ILE A . n 
A 1 306 ILE 306 740 740 ILE ILE A . n 
A 1 307 LEU 307 741 741 LEU LEU A . n 
A 1 308 GLU 308 742 742 GLU GLU A . n 
A 1 309 GLY 309 743 743 GLY GLY A . n 
A 1 310 GLY 310 744 744 GLY GLY A . n 
A 1 311 TYR 311 745 745 TYR TYR A . n 
A 1 312 ASN 312 746 746 ASN ASN A . n 
A 1 313 LEU 313 747 747 LEU LEU A . n 
A 1 314 THR 314 748 748 THR THR A . n 
A 1 315 SER 315 749 749 SER SER A . n 
A 1 316 ILE 316 750 750 ILE ILE A . n 
A 1 317 SER 317 751 751 SER SER A . n 
A 1 318 GLU 318 752 752 GLU GLU A . n 
A 1 319 SER 319 753 753 SER SER A . n 
A 1 320 MET 320 754 754 MET MET A . n 
A 1 321 SER 321 755 755 SER SER A . n 
A 1 322 MET 322 756 756 MET MET A . n 
A 1 323 CYS 323 757 757 CYS CYS A . n 
A 1 324 THR 324 758 758 THR THR A . n 
A 1 325 SER 325 759 759 SER SER A . n 
A 1 326 MET 326 760 760 MET MET A . n 
A 1 327 LEU 327 761 761 LEU LEU A . n 
A 1 328 LEU 328 762 762 LEU LEU A . n 
A 1 329 GLY 329 763 763 GLY GLY A . n 
A 1 330 ASP 330 764 764 ASP ASP A . n 
A 1 331 SER 331 765 765 SER SER A . n 
A 1 332 PRO 332 766 766 PRO PRO A . n 
A 1 333 PRO 333 767 767 PRO PRO A . n 
A 1 334 SER 334 768 768 SER SER A . n 
A 1 335 LEU 335 769 769 LEU LEU A . n 
A 1 336 ASP 336 770 ?   ?   ?   A . n 
A 1 337 HIS 337 771 ?   ?   ?   A . n 
A 1 338 LEU 338 772 ?   ?   ?   A . n 
A 1 339 THR 339 773 773 THR THR A . n 
A 1 340 PRO 340 774 774 PRO PRO A . n 
A 1 341 LEU 341 775 775 LEU LEU A . n 
A 1 342 LYS 342 776 776 LYS LYS A . n 
A 1 343 THR 343 777 777 THR THR A . n 
A 1 344 SER 344 778 778 SER SER A . n 
A 1 345 ALA 345 779 779 ALA ALA A . n 
A 1 346 THR 346 780 780 THR THR A . n 
A 1 347 VAL 347 781 781 VAL VAL A . n 
A 1 348 SER 348 782 782 SER SER A . n 
A 1 349 ILE 349 783 783 ILE ILE A . n 
A 1 350 ASN 350 784 784 ASN ASN A . n 
A 1 351 ASN 351 785 785 ASN ASN A . n 
A 1 352 VAL 352 786 786 VAL VAL A . n 
A 1 353 LEU 353 787 787 LEU LEU A . n 
A 1 354 ARG 354 788 788 ARG ARG A . n 
A 1 355 ALA 355 789 789 ALA ALA A . n 
A 1 356 HIS 356 790 790 HIS HIS A . n 
A 1 357 ALA 357 791 791 ALA ALA A . n 
A 1 358 PRO 358 792 792 PRO PRO A . n 
A 1 359 PHE 359 793 793 PHE PHE A . n 
A 1 360 TRP 360 794 794 TRP TRP A . n 
A 1 361 SER 361 795 795 SER SER A . n 
A 1 362 SER 362 796 796 SER SER A . n 
A 1 363 LEU 363 797 797 LEU LEU A . n 
A 1 364 ARG 364 798 ?   ?   ?   A . n 
B 1 1   SER 1   435 ?   ?   ?   B . n 
B 1 2   ASN 2   436 ?   ?   ?   B . n 
B 1 3   ALA 3   437 ?   ?   ?   B . n 
B 1 4   GLY 4   438 ?   ?   ?   B . n 
B 1 5   GLY 5   439 ?   ?   ?   B . n 
B 1 6   SER 6   440 ?   ?   ?   B . n 
B 1 7   SER 7   441 ?   ?   ?   B . n 
B 1 8   PRO 8   442 442 PRO PRO B . n 
B 1 9   ILE 9   443 443 ILE ILE B . n 
B 1 10  THR 10  444 444 THR THR B . n 
B 1 11  GLY 11  445 445 GLY GLY B . n 
B 1 12  LEU 12  446 446 LEU LEU B . n 
B 1 13  VAL 13  447 447 VAL VAL B . n 
B 1 14  TYR 14  448 448 TYR TYR B . n 
B 1 15  ASP 15  449 449 ASP ASP B . n 
B 1 16  GLN 16  450 450 GLN GLN B . n 
B 1 17  ARG 17  451 451 ARG ARG B . n 
B 1 18  MET 18  452 452 MET MET B . n 
B 1 19  MET 19  453 453 MET MET B . n 
B 1 20  LEU 20  454 454 LEU LEU B . n 
B 1 21  HIS 21  455 455 HIS HIS B . n 
B 1 22  HIS 22  456 456 HIS HIS B . n 
B 1 23  ASN 23  457 457 ASN ASN B . n 
B 1 24  MET 24  458 458 MET MET B . n 
B 1 25  TRP 25  459 459 TRP TRP B . n 
B 1 26  ASP 26  460 460 ASP ASP B . n 
B 1 27  SER 27  461 461 SER SER B . n 
B 1 28  HIS 28  462 462 HIS HIS B . n 
B 1 29  HIS 29  463 463 HIS HIS B . n 
B 1 30  PRO 30  464 464 PRO PRO B . n 
B 1 31  GLU 31  465 465 GLU GLU B . n 
B 1 32  LEU 32  466 466 LEU LEU B . n 
B 1 33  PRO 33  467 467 PRO PRO B . n 
B 1 34  GLN 34  468 468 GLN GLN B . n 
B 1 35  ARG 35  469 469 ARG ARG B . n 
B 1 36  ILE 36  470 470 ILE ILE B . n 
B 1 37  SER 37  471 471 SER SER B . n 
B 1 38  ARG 38  472 472 ARG ARG B . n 
B 1 39  ILE 39  473 473 ILE ILE B . n 
B 1 40  PHE 40  474 474 PHE PHE B . n 
B 1 41  SER 41  475 475 SER SER B . n 
B 1 42  ARG 42  476 476 ARG ARG B . n 
B 1 43  HIS 43  477 477 HIS HIS B . n 
B 1 44  GLU 44  478 478 GLU GLU B . n 
B 1 45  GLU 45  479 479 GLU GLU B . n 
B 1 46  LEU 46  480 480 LEU LEU B . n 
B 1 47  ARG 47  481 481 ARG ARG B . n 
B 1 48  LEU 48  482 482 LEU LEU B . n 
B 1 49  LEU 49  483 483 LEU LEU B . n 
B 1 50  SER 50  484 484 SER SER B . n 
B 1 51  ARG 51  485 485 ARG ARG B . n 
B 1 52  CYS 52  486 486 CYS CYS B . n 
B 1 53  HIS 53  487 487 HIS HIS B . n 
B 1 54  ARG 54  488 488 ARG ARG B . n 
B 1 55  ILE 55  489 489 ILE ILE B . n 
B 1 56  PRO 56  490 490 PRO PRO B . n 
B 1 57  ALA 57  491 491 ALA ALA B . n 
B 1 58  ARG 58  492 492 ARG ARG B . n 
B 1 59  LEU 59  493 493 LEU LEU B . n 
B 1 60  ALA 60  494 494 ALA ALA B . n 
B 1 61  THR 61  495 495 THR THR B . n 
B 1 62  GLU 62  496 496 GLU GLU B . n 
B 1 63  GLU 63  497 497 GLU GLU B . n 
B 1 64  GLU 64  498 498 GLU GLU B . n 
B 1 65  LEU 65  499 499 LEU LEU B . n 
B 1 66  ALA 66  500 500 ALA ALA B . n 
B 1 67  LEU 67  501 501 LEU LEU B . n 
B 1 68  CYS 68  502 502 CYS CYS B . n 
B 1 69  HIS 69  503 503 HIS HIS B . n 
B 1 70  SER 70  504 504 SER SER B . n 
B 1 71  SER 71  505 505 SER SER B . n 
B 1 72  LYS 72  506 506 LYS LYS B . n 
B 1 73  HIS 73  507 507 HIS HIS B . n 
B 1 74  ILE 74  508 508 ILE ILE B . n 
B 1 75  SER 75  509 509 SER SER B . n 
B 1 76  ILE 76  510 510 ILE ILE B . n 
B 1 77  ILE 77  511 511 ILE ILE B . n 
B 1 78  LYS 78  512 512 LYS LYS B . n 
B 1 79  SER 79  513 513 SER SER B . n 
B 1 80  SER 80  514 514 SER SER B . n 
B 1 81  GLU 81  515 515 GLU GLU B . n 
B 1 82  HIS 82  516 516 HIS HIS B . n 
B 1 83  MET 83  517 517 MET MET B . n 
B 1 84  LYS 84  518 518 LYS LYS B . n 
B 1 85  PRO 85  519 519 PRO PRO B . n 
B 1 86  ARG 86  520 520 ARG ARG B . n 
B 1 87  ASP 87  521 521 ASP ASP B . n 
B 1 88  LEU 88  522 522 LEU LEU B . n 
B 1 89  ASN 89  523 523 ASN ASN B . n 
B 1 90  ARG 90  524 524 ARG ARG B . n 
B 1 91  LEU 91  525 525 LEU LEU B . n 
B 1 92  GLY 92  526 526 GLY GLY B . n 
B 1 93  ASP 93  527 527 ASP ASP B . n 
B 1 94  GLU 94  528 528 GLU GLU B . n 
B 1 95  TYR 95  529 529 TYR TYR B . n 
B 1 96  ASN 96  530 530 ASN ASN B . n 
B 1 97  SER 97  531 531 SER SER B . n 
B 1 98  ILE 98  532 532 ILE ILE B . n 
B 1 99  PHE 99  533 533 PHE PHE B . n 
B 1 100 ILE 100 534 534 ILE ILE B . n 
B 1 101 SER 101 535 535 SER SER B . n 
B 1 102 ASN 102 536 536 ASN ASN B . n 
B 1 103 GLU 103 537 537 GLU GLU B . n 
B 1 104 SER 104 538 538 SER SER B . n 
B 1 105 TYR 105 539 539 TYR TYR B . n 
B 1 106 THR 106 540 540 THR THR B . n 
B 1 107 CYS 107 541 541 CYS CYS B . n 
B 1 108 ALA 108 542 542 ALA ALA B . n 
B 1 109 LEU 109 543 543 LEU LEU B . n 
B 1 110 LEU 110 544 544 LEU LEU B . n 
B 1 111 ALA 111 545 545 ALA ALA B . n 
B 1 112 ALA 112 546 546 ALA ALA B . n 
B 1 113 GLY 113 547 547 GLY GLY B . n 
B 1 114 SER 114 548 548 SER SER B . n 
B 1 115 CYS 115 549 549 CYS CYS B . n 
B 1 116 PHE 116 550 550 PHE PHE B . n 
B 1 117 ASN 117 551 551 ASN ASN B . n 
B 1 118 SER 118 552 552 SER SER B . n 
B 1 119 ALA 119 553 553 ALA ALA B . n 
B 1 120 GLN 120 554 554 GLN GLN B . n 
B 1 121 ALA 121 555 555 ALA ALA B . n 
B 1 122 ILE 122 556 556 ILE ILE B . n 
B 1 123 LEU 123 557 557 LEU LEU B . n 
B 1 124 THR 124 558 558 THR THR B . n 
B 1 125 GLY 125 559 559 GLY GLY B . n 
B 1 126 GLN 126 560 560 GLN GLN B . n 
B 1 127 VAL 127 561 561 VAL VAL B . n 
B 1 128 ARG 128 562 562 ARG ARG B . n 
B 1 129 ASN 129 563 563 ASN ASN B . n 
B 1 130 ALA 130 564 564 ALA ALA B . n 
B 1 131 VAL 131 565 565 VAL VAL B . n 
B 1 132 ALA 132 566 566 ALA ALA B . n 
B 1 133 ILE 133 567 567 ILE ILE B . n 
B 1 134 VAL 134 568 568 VAL VAL B . n 
B 1 135 ARG 135 569 569 ARG ARG B . n 
B 1 136 PRO 136 570 570 PRO PRO B . n 
B 1 137 PRO 137 571 571 PRO PRO B . n 
B 1 138 GLY 138 572 572 GLY GLY B . n 
B 1 139 HIS 139 573 573 HIS HIS B . n 
B 1 140 HIS 140 574 574 HIS HIS B . n 
B 1 141 ALA 141 575 575 ALA ALA B . n 
B 1 142 GLU 142 576 576 GLU GLU B . n 
B 1 143 LYS 143 577 577 LYS LYS B . n 
B 1 144 ASP 144 578 578 ASP ASP B . n 
B 1 145 THR 145 579 579 THR THR B . n 
B 1 146 ALA 146 580 580 ALA ALA B . n 
B 1 147 CYS 147 581 581 CYS CYS B . n 
B 1 148 GLY 148 582 582 GLY GLY B . n 
B 1 149 PHE 149 583 583 PHE PHE B . n 
B 1 150 CYS 150 584 584 CYS CYS B . n 
B 1 151 PHE 151 585 585 PHE PHE B . n 
B 1 152 PHE 152 586 586 PHE PHE B . n 
B 1 153 ASN 153 587 587 ASN ASN B . n 
B 1 154 THR 154 588 588 THR THR B . n 
B 1 155 ALA 155 589 589 ALA ALA B . n 
B 1 156 ALA 156 590 590 ALA ALA B . n 
B 1 157 LEU 157 591 591 LEU LEU B . n 
B 1 158 THR 158 592 592 THR THR B . n 
B 1 159 ALA 159 593 593 ALA ALA B . n 
B 1 160 ARG 160 594 594 ARG ARG B . n 
B 1 161 TYR 161 595 595 TYR TYR B . n 
B 1 162 ALA 162 596 596 ALA ALA B . n 
B 1 163 GLN 163 597 597 GLN GLN B . n 
B 1 164 SER 164 598 598 SER SER B . n 
B 1 165 ILE 165 599 599 ILE ILE B . n 
B 1 166 THR 166 600 600 THR THR B . n 
B 1 167 ARG 167 601 601 ARG ARG B . n 
B 1 168 GLU 168 602 602 GLU GLU B . n 
B 1 169 SER 169 603 603 SER SER B . n 
B 1 170 LEU 170 604 604 LEU LEU B . n 
B 1 171 ARG 171 605 605 ARG ARG B . n 
B 1 172 VAL 172 606 606 VAL VAL B . n 
B 1 173 LEU 173 607 607 LEU LEU B . n 
B 1 174 ILE 174 608 608 ILE ILE B . n 
B 1 175 VAL 175 609 609 VAL VAL B . n 
B 1 176 ASP 176 610 610 ASP ASP B . n 
B 1 177 TRP 177 611 611 TRP TRP B . n 
B 1 178 ASP 178 612 612 ASP ASP B . n 
B 1 179 VAL 179 613 613 VAL VAL B . n 
B 1 180 HIS 180 614 614 HIS HIS B . n 
B 1 181 HIS 181 615 615 HIS HIS B . n 
B 1 182 GLY 182 616 616 GLY GLY B . n 
B 1 183 ASN 183 617 617 ASN ASN B . n 
B 1 184 GLY 184 618 618 GLY GLY B . n 
B 1 185 THR 185 619 619 THR THR B . n 
B 1 186 GLN 186 620 620 GLN GLN B . n 
B 1 187 HIS 187 621 621 HIS HIS B . n 
B 1 188 ILE 188 622 622 ILE ILE B . n 
B 1 189 PHE 189 623 623 PHE PHE B . n 
B 1 190 GLU 190 624 624 GLU GLU B . n 
B 1 191 GLU 191 625 625 GLU GLU B . n 
B 1 192 ASP 192 626 626 ASP ASP B . n 
B 1 193 ASP 193 627 627 ASP ASP B . n 
B 1 194 SER 194 628 628 SER SER B . n 
B 1 195 VAL 195 629 629 VAL VAL B . n 
B 1 196 LEU 196 630 630 LEU LEU B . n 
B 1 197 TYR 197 631 631 TYR TYR B . n 
B 1 198 ILE 198 632 632 ILE ILE B . n 
B 1 199 SER 199 633 633 SER SER B . n 
B 1 200 LEU 200 634 634 LEU LEU B . n 
B 1 201 HIS 201 635 635 HIS HIS B . n 
B 1 202 ARG 202 636 636 ARG ARG B . n 
B 1 203 TYR 203 637 637 TYR TYR B . n 
B 1 204 GLU 204 638 638 GLU GLU B . n 
B 1 205 ASP 205 639 639 ASP ASP B . n 
B 1 206 GLY 206 640 640 GLY GLY B . n 
B 1 207 ALA 207 641 641 ALA ALA B . n 
B 1 208 PHE 208 642 642 PHE PHE B . n 
B 1 209 PHE 209 643 643 PHE PHE B . n 
B 1 210 PRO 210 644 644 PRO PRO B . n 
B 1 211 ASN 211 645 645 ASN ASN B . n 
B 1 212 SER 212 646 646 SER SER B . n 
B 1 213 GLU 213 647 647 GLU GLU B . n 
B 1 214 ASP 214 648 648 ASP ASP B . n 
B 1 215 ALA 215 649 649 ALA ALA B . n 
B 1 216 ASN 216 650 650 ASN ASN B . n 
B 1 217 TYR 217 651 651 TYR TYR B . n 
B 1 218 ASP 218 652 652 ASP ASP B . n 
B 1 219 LYS 219 653 653 LYS LYS B . n 
B 1 220 VAL 220 654 654 VAL VAL B . n 
B 1 221 GLY 221 655 655 GLY GLY B . n 
B 1 222 LEU 222 656 656 LEU LEU B . n 
B 1 223 GLY 223 657 657 GLY GLY B . n 
B 1 224 LYS 224 658 658 LYS LYS B . n 
B 1 225 GLY 225 659 659 GLY GLY B . n 
B 1 226 ARG 226 660 660 ARG ARG B . n 
B 1 227 GLY 227 661 661 GLY GLY B . n 
B 1 228 TYR 228 662 662 TYR TYR B . n 
B 1 229 ASN 229 663 663 ASN ASN B . n 
B 1 230 VAL 230 664 664 VAL VAL B . n 
B 1 231 ASN 231 665 665 ASN ASN B . n 
B 1 232 ILE 232 666 666 ILE ILE B . n 
B 1 233 PRO 233 667 667 PRO PRO B . n 
B 1 234 TRP 234 668 668 TRP TRP B . n 
B 1 235 ASN 235 669 669 ASN ASN B . n 
B 1 236 GLY 236 670 670 GLY GLY B . n 
B 1 237 GLY 237 671 671 GLY GLY B . n 
B 1 238 LYS 238 672 672 LYS LYS B . n 
B 1 239 MET 239 673 673 MET MET B . n 
B 1 240 GLY 240 674 674 GLY GLY B . n 
B 1 241 ASP 241 675 675 ASP ASP B . n 
B 1 242 PRO 242 676 676 PRO PRO B . n 
B 1 243 GLU 243 677 677 GLU GLU B . n 
B 1 244 TYR 244 678 678 TYR TYR B . n 
B 1 245 MET 245 679 679 MET MET B . n 
B 1 246 ALA 246 680 680 ALA ALA B . n 
B 1 247 ALA 247 681 681 ALA ALA B . n 
B 1 248 PHE 248 682 682 PHE PHE B . n 
B 1 249 HIS 249 683 683 HIS HIS B . n 
B 1 250 HIS 250 684 684 HIS HIS B . n 
B 1 251 LEU 251 685 685 LEU LEU B . n 
B 1 252 VAL 252 686 686 VAL VAL B . n 
B 1 253 MET 253 687 687 MET MET B . n 
B 1 254 PRO 254 688 688 PRO PRO B . n 
B 1 255 ILE 255 689 689 ILE ILE B . n 
B 1 256 ALA 256 690 690 ALA ALA B . n 
B 1 257 ARG 257 691 691 ARG ARG B . n 
B 1 258 GLU 258 692 692 GLU GLU B . n 
B 1 259 PHE 259 693 693 PHE PHE B . n 
B 1 260 ALA 260 694 694 ALA ALA B . n 
B 1 261 PRO 261 695 695 PRO PRO B . n 
B 1 262 GLU 262 696 696 GLU GLU B . n 
B 1 263 LEU 263 697 697 LEU LEU B . n 
B 1 264 VAL 264 698 698 VAL VAL B . n 
B 1 265 LEU 265 699 699 LEU LEU B . n 
B 1 266 VAL 266 700 700 VAL VAL B . n 
B 1 267 SER 267 701 701 SER SER B . n 
B 1 268 ALA 268 702 702 ALA ALA B . n 
B 1 269 GLY 269 703 703 GLY GLY B . n 
B 1 270 PHE 270 704 704 PHE PHE B . n 
B 1 271 ASP 271 705 705 ASP ASP B . n 
B 1 272 ALA 272 706 706 ALA ALA B . n 
B 1 273 ALA 273 707 707 ALA ALA B . n 
B 1 274 ARG 274 708 708 ARG ARG B . n 
B 1 275 GLY 275 709 709 GLY GLY B . n 
B 1 276 ASP 276 710 710 ASP ASP B . n 
B 1 277 PRO 277 711 711 PRO PRO B . n 
B 1 278 LEU 278 712 712 LEU LEU B . n 
B 1 279 GLY 279 713 713 GLY GLY B . n 
B 1 280 GLY 280 714 714 GLY GLY B . n 
B 1 281 PHE 281 715 715 PHE PHE B . n 
B 1 282 GLN 282 716 716 GLN GLN B . n 
B 1 283 VAL 283 717 717 VAL VAL B . n 
B 1 284 THR 284 718 718 THR THR B . n 
B 1 285 PRO 285 719 719 PRO PRO B . n 
B 1 286 GLU 286 720 720 GLU GLU B . n 
B 1 287 GLY 287 721 721 GLY GLY B . n 
B 1 288 TYR 288 722 722 TYR TYR B . n 
B 1 289 ALA 289 723 723 ALA ALA B . n 
B 1 290 HIS 290 724 724 HIS HIS B . n 
B 1 291 LEU 291 725 725 LEU LEU B . n 
B 1 292 THR 292 726 726 THR THR B . n 
B 1 293 HIS 293 727 727 HIS HIS B . n 
B 1 294 GLN 294 728 728 GLN GLN B . n 
B 1 295 LEU 295 729 729 LEU LEU B . n 
B 1 296 MET 296 730 730 MET MET B . n 
B 1 297 SER 297 731 731 SER SER B . n 
B 1 298 LEU 298 732 732 LEU LEU B . n 
B 1 299 ALA 299 733 733 ALA ALA B . n 
B 1 300 ALA 300 734 734 ALA ALA B . n 
B 1 301 GLY 301 735 735 GLY GLY B . n 
B 1 302 ARG 302 736 736 ARG ARG B . n 
B 1 303 VAL 303 737 737 VAL VAL B . n 
B 1 304 LEU 304 738 738 LEU LEU B . n 
B 1 305 ILE 305 739 739 ILE ILE B . n 
B 1 306 ILE 306 740 740 ILE ILE B . n 
B 1 307 LEU 307 741 741 LEU LEU B . n 
B 1 308 GLU 308 742 742 GLU GLU B . n 
B 1 309 GLY 309 743 743 GLY GLY B . n 
B 1 310 GLY 310 744 744 GLY GLY B . n 
B 1 311 TYR 311 745 745 TYR TYR B . n 
B 1 312 ASN 312 746 746 ASN ASN B . n 
B 1 313 LEU 313 747 747 LEU LEU B . n 
B 1 314 THR 314 748 748 THR THR B . n 
B 1 315 SER 315 749 749 SER SER B . n 
B 1 316 ILE 316 750 750 ILE ILE B . n 
B 1 317 SER 317 751 751 SER SER B . n 
B 1 318 GLU 318 752 752 GLU GLU B . n 
B 1 319 SER 319 753 753 SER SER B . n 
B 1 320 MET 320 754 754 MET MET B . n 
B 1 321 SER 321 755 755 SER SER B . n 
B 1 322 MET 322 756 756 MET MET B . n 
B 1 323 CYS 323 757 757 CYS CYS B . n 
B 1 324 THR 324 758 758 THR THR B . n 
B 1 325 SER 325 759 759 SER SER B . n 
B 1 326 MET 326 760 760 MET MET B . n 
B 1 327 LEU 327 761 761 LEU LEU B . n 
B 1 328 LEU 328 762 762 LEU LEU B . n 
B 1 329 GLY 329 763 763 GLY GLY B . n 
B 1 330 ASP 330 764 764 ASP ASP B . n 
B 1 331 SER 331 765 765 SER SER B . n 
B 1 332 PRO 332 766 766 PRO PRO B . n 
B 1 333 PRO 333 767 767 PRO PRO B . n 
B 1 334 SER 334 768 ?   ?   ?   B . n 
B 1 335 LEU 335 769 ?   ?   ?   B . n 
B 1 336 ASP 336 770 ?   ?   ?   B . n 
B 1 337 HIS 337 771 ?   ?   ?   B . n 
B 1 338 LEU 338 772 ?   ?   ?   B . n 
B 1 339 THR 339 773 ?   ?   ?   B . n 
B 1 340 PRO 340 774 774 PRO PRO B . n 
B 1 341 LEU 341 775 775 LEU LEU B . n 
B 1 342 LYS 342 776 776 LYS LYS B . n 
B 1 343 THR 343 777 777 THR THR B . n 
B 1 344 SER 344 778 778 SER SER B . n 
B 1 345 ALA 345 779 779 ALA ALA B . n 
B 1 346 THR 346 780 780 THR THR B . n 
B 1 347 VAL 347 781 781 VAL VAL B . n 
B 1 348 SER 348 782 782 SER SER B . n 
B 1 349 ILE 349 783 783 ILE ILE B . n 
B 1 350 ASN 350 784 784 ASN ASN B . n 
B 1 351 ASN 351 785 785 ASN ASN B . n 
B 1 352 VAL 352 786 786 VAL VAL B . n 
B 1 353 LEU 353 787 787 LEU LEU B . n 
B 1 354 ARG 354 788 788 ARG ARG B . n 
B 1 355 ALA 355 789 789 ALA ALA B . n 
B 1 356 HIS 356 790 790 HIS HIS B . n 
B 1 357 ALA 357 791 791 ALA ALA B . n 
B 1 358 PRO 358 792 792 PRO PRO B . n 
B 1 359 PHE 359 793 793 PHE PHE B . n 
B 1 360 TRP 360 794 794 TRP TRP B . n 
B 1 361 SER 361 795 795 SER SER B . n 
B 1 362 SER 362 796 796 SER SER B . n 
B 1 363 LEU 363 797 797 LEU LEU B . n 
B 1 364 ARG 364 798 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BNN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BNN 
_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 A1BNN 1   801  801 A1BNN SEH A . 
D 3 EDO   1   802  802 EDO   EDO A . 
E 4 ZN    1   803  2   ZN    ZN  A . 
F 5 K     1   804  2   K     K   A . 
G 5 K     1   805  3   K     K   A . 
H 3 EDO   1   801  801 EDO   EDO B . 
I 2 A1BNN 1   802  802 A1BNN SEH B . 
J 4 ZN    1   803  1   ZN    ZN  B . 
K 5 K     1   804  1   K     K   B . 
L 5 K     1   805  4   K     K   B . 
M 6 HOH   1   901  73  HOH   HOH A . 
M 6 HOH   2   902  72  HOH   HOH A . 
M 6 HOH   3   903  16  HOH   HOH A . 
M 6 HOH   4   904  13  HOH   HOH A . 
M 6 HOH   5   905  216 HOH   HOH A . 
M 6 HOH   6   906  25  HOH   HOH A . 
M 6 HOH   7   907  38  HOH   HOH A . 
M 6 HOH   8   908  28  HOH   HOH A . 
M 6 HOH   9   909  12  HOH   HOH A . 
M 6 HOH   10  910  23  HOH   HOH A . 
M 6 HOH   11  911  58  HOH   HOH A . 
M 6 HOH   12  912  167 HOH   HOH A . 
M 6 HOH   13  913  6   HOH   HOH A . 
M 6 HOH   14  914  14  HOH   HOH A . 
M 6 HOH   15  915  149 HOH   HOH A . 
M 6 HOH   16  916  24  HOH   HOH A . 
M 6 HOH   17  917  181 HOH   HOH A . 
M 6 HOH   18  918  52  HOH   HOH A . 
M 6 HOH   19  919  87  HOH   HOH A . 
M 6 HOH   20  920  21  HOH   HOH A . 
M 6 HOH   21  921  97  HOH   HOH A . 
M 6 HOH   22  922  152 HOH   HOH A . 
M 6 HOH   23  923  109 HOH   HOH A . 
M 6 HOH   24  924  185 HOH   HOH A . 
M 6 HOH   25  925  170 HOH   HOH A . 
M 6 HOH   26  926  212 HOH   HOH A . 
M 6 HOH   27  927  9   HOH   HOH A . 
M 6 HOH   28  928  85  HOH   HOH A . 
M 6 HOH   29  929  213 HOH   HOH A . 
M 6 HOH   30  930  154 HOH   HOH A . 
M 6 HOH   31  931  32  HOH   HOH A . 
M 6 HOH   32  932  39  HOH   HOH A . 
M 6 HOH   33  933  75  HOH   HOH A . 
M 6 HOH   34  934  3   HOH   HOH A . 
M 6 HOH   35  935  132 HOH   HOH A . 
M 6 HOH   36  936  86  HOH   HOH A . 
M 6 HOH   37  937  93  HOH   HOH A . 
M 6 HOH   38  938  4   HOH   HOH A . 
M 6 HOH   39  939  1   HOH   HOH A . 
M 6 HOH   40  940  107 HOH   HOH A . 
M 6 HOH   41  941  183 HOH   HOH A . 
M 6 HOH   42  942  70  HOH   HOH A . 
M 6 HOH   43  943  182 HOH   HOH A . 
M 6 HOH   44  944  89  HOH   HOH A . 
M 6 HOH   45  945  175 HOH   HOH A . 
M 6 HOH   46  946  115 HOH   HOH A . 
M 6 HOH   47  947  71  HOH   HOH A . 
M 6 HOH   48  948  56  HOH   HOH A . 
M 6 HOH   49  949  169 HOH   HOH A . 
M 6 HOH   50  950  53  HOH   HOH A . 
M 6 HOH   51  951  218 HOH   HOH A . 
M 6 HOH   52  952  148 HOH   HOH A . 
M 6 HOH   53  953  84  HOH   HOH A . 
M 6 HOH   54  954  54  HOH   HOH A . 
M 6 HOH   55  955  178 HOH   HOH A . 
M 6 HOH   56  956  42  HOH   HOH A . 
M 6 HOH   57  957  134 HOH   HOH A . 
M 6 HOH   58  958  15  HOH   HOH A . 
M 6 HOH   59  959  158 HOH   HOH A . 
M 6 HOH   60  960  184 HOH   HOH A . 
M 6 HOH   61  961  99  HOH   HOH A . 
M 6 HOH   62  962  5   HOH   HOH A . 
M 6 HOH   63  963  26  HOH   HOH A . 
M 6 HOH   64  964  22  HOH   HOH A . 
M 6 HOH   65  965  176 HOH   HOH A . 
M 6 HOH   66  966  156 HOH   HOH A . 
M 6 HOH   67  967  198 HOH   HOH A . 
M 6 HOH   68  968  129 HOH   HOH A . 
M 6 HOH   69  969  135 HOH   HOH A . 
M 6 HOH   70  970  118 HOH   HOH A . 
M 6 HOH   71  971  57  HOH   HOH A . 
M 6 HOH   72  972  64  HOH   HOH A . 
M 6 HOH   73  973  186 HOH   HOH A . 
M 6 HOH   74  974  214 HOH   HOH A . 
M 6 HOH   75  975  128 HOH   HOH A . 
M 6 HOH   76  976  137 HOH   HOH A . 
M 6 HOH   77  977  136 HOH   HOH A . 
M 6 HOH   78  978  106 HOH   HOH A . 
M 6 HOH   79  979  180 HOH   HOH A . 
M 6 HOH   80  980  197 HOH   HOH A . 
M 6 HOH   81  981  177 HOH   HOH A . 
M 6 HOH   82  982  40  HOH   HOH A . 
M 6 HOH   83  983  155 HOH   HOH A . 
M 6 HOH   84  984  2   HOH   HOH A . 
M 6 HOH   85  985  74  HOH   HOH A . 
M 6 HOH   86  986  166 HOH   HOH A . 
M 6 HOH   87  987  122 HOH   HOH A . 
M 6 HOH   88  988  173 HOH   HOH A . 
M 6 HOH   89  989  103 HOH   HOH A . 
M 6 HOH   90  990  119 HOH   HOH A . 
M 6 HOH   91  991  120 HOH   HOH A . 
M 6 HOH   92  992  142 HOH   HOH A . 
M 6 HOH   93  993  174 HOH   HOH A . 
M 6 HOH   94  994  104 HOH   HOH A . 
M 6 HOH   95  995  215 HOH   HOH A . 
M 6 HOH   96  996  127 HOH   HOH A . 
M 6 HOH   97  997  217 HOH   HOH A . 
M 6 HOH   98  998  210 HOH   HOH A . 
M 6 HOH   99  999  179 HOH   HOH A . 
M 6 HOH   100 1000 116 HOH   HOH A . 
N 6 HOH   1   901  11  HOH   HOH B . 
N 6 HOH   2   902  187 HOH   HOH B . 
N 6 HOH   3   903  36  HOH   HOH B . 
N 6 HOH   4   904  205 HOH   HOH B . 
N 6 HOH   5   905  51  HOH   HOH B . 
N 6 HOH   6   906  91  HOH   HOH B . 
N 6 HOH   7   907  139 HOH   HOH B . 
N 6 HOH   8   908  43  HOH   HOH B . 
N 6 HOH   9   909  190 HOH   HOH B . 
N 6 HOH   10  910  34  HOH   HOH B . 
N 6 HOH   11  911  81  HOH   HOH B . 
N 6 HOH   12  912  19  HOH   HOH B . 
N 6 HOH   13  913  171 HOH   HOH B . 
N 6 HOH   14  914  27  HOH   HOH B . 
N 6 HOH   15  915  111 HOH   HOH B . 
N 6 HOH   16  916  195 HOH   HOH B . 
N 6 HOH   17  917  29  HOH   HOH B . 
N 6 HOH   18  918  83  HOH   HOH B . 
N 6 HOH   19  919  157 HOH   HOH B . 
N 6 HOH   20  920  108 HOH   HOH B . 
N 6 HOH   21  921  46  HOH   HOH B . 
N 6 HOH   22  922  31  HOH   HOH B . 
N 6 HOH   23  923  45  HOH   HOH B . 
N 6 HOH   24  924  30  HOH   HOH B . 
N 6 HOH   25  925  33  HOH   HOH B . 
N 6 HOH   26  926  44  HOH   HOH B . 
N 6 HOH   27  927  101 HOH   HOH B . 
N 6 HOH   28  928  124 HOH   HOH B . 
N 6 HOH   29  929  20  HOH   HOH B . 
N 6 HOH   30  930  8   HOH   HOH B . 
N 6 HOH   31  931  35  HOH   HOH B . 
N 6 HOH   32  932  191 HOH   HOH B . 
N 6 HOH   33  933  95  HOH   HOH B . 
N 6 HOH   34  934  133 HOH   HOH B . 
N 6 HOH   35  935  144 HOH   HOH B . 
N 6 HOH   36  936  50  HOH   HOH B . 
N 6 HOH   37  937  203 HOH   HOH B . 
N 6 HOH   38  938  65  HOH   HOH B . 
N 6 HOH   39  939  113 HOH   HOH B . 
N 6 HOH   40  940  60  HOH   HOH B . 
N 6 HOH   41  941  102 HOH   HOH B . 
N 6 HOH   42  942  79  HOH   HOH B . 
N 6 HOH   43  943  192 HOH   HOH B . 
N 6 HOH   44  944  117 HOH   HOH B . 
N 6 HOH   45  945  41  HOH   HOH B . 
N 6 HOH   46  946  37  HOH   HOH B . 
N 6 HOH   47  947  146 HOH   HOH B . 
N 6 HOH   48  948  105 HOH   HOH B . 
N 6 HOH   49  949  17  HOH   HOH B . 
N 6 HOH   50  950  63  HOH   HOH B . 
N 6 HOH   51  951  96  HOH   HOH B . 
N 6 HOH   52  952  209 HOH   HOH B . 
N 6 HOH   53  953  141 HOH   HOH B . 
N 6 HOH   54  954  208 HOH   HOH B . 
N 6 HOH   55  955  194 HOH   HOH B . 
N 6 HOH   56  956  48  HOH   HOH B . 
N 6 HOH   57  957  59  HOH   HOH B . 
N 6 HOH   58  958  200 HOH   HOH B . 
N 6 HOH   59  959  131 HOH   HOH B . 
N 6 HOH   60  960  110 HOH   HOH B . 
N 6 HOH   61  961  69  HOH   HOH B . 
N 6 HOH   62  962  162 HOH   HOH B . 
N 6 HOH   63  963  199 HOH   HOH B . 
N 6 HOH   64  964  88  HOH   HOH B . 
N 6 HOH   65  965  98  HOH   HOH B . 
N 6 HOH   66  966  147 HOH   HOH B . 
N 6 HOH   67  967  189 HOH   HOH B . 
N 6 HOH   68  968  153 HOH   HOH B . 
N 6 HOH   69  969  172 HOH   HOH B . 
N 6 HOH   70  970  68  HOH   HOH B . 
N 6 HOH   71  971  18  HOH   HOH B . 
N 6 HOH   72  972  211 HOH   HOH B . 
N 6 HOH   73  973  47  HOH   HOH B . 
N 6 HOH   74  974  207 HOH   HOH B . 
N 6 HOH   75  975  67  HOH   HOH B . 
N 6 HOH   76  976  202 HOH   HOH B . 
N 6 HOH   77  977  145 HOH   HOH B . 
N 6 HOH   78  978  206 HOH   HOH B . 
N 6 HOH   79  979  196 HOH   HOH B . 
N 6 HOH   80  980  188 HOH   HOH B . 
N 6 HOH   81  981  150 HOH   HOH B . 
N 6 HOH   82  982  126 HOH   HOH B . 
N 6 HOH   83  983  164 HOH   HOH B . 
N 6 HOH   84  984  161 HOH   HOH B . 
N 6 HOH   85  985  193 HOH   HOH B . 
N 6 HOH   86  986  159 HOH   HOH B . 
N 6 HOH   87  987  130 HOH   HOH B . 
N 6 HOH   88  988  163 HOH   HOH B . 
N 6 HOH   89  989  114 HOH   HOH B . 
N 6 HOH   90  990  82  HOH   HOH B . 
N 6 HOH   91  991  151 HOH   HOH B . 
N 6 HOH   92  992  125 HOH   HOH B . 
N 6 HOH   93  993  140 HOH   HOH B . 
N 6 HOH   94  994  138 HOH   HOH B . 
N 6 HOH   95  995  121 HOH   HOH B . 
N 6 HOH   96  996  160 HOH   HOH B . 
N 6 HOH   97  997  165 HOH   HOH B . 
N 6 HOH   98  998  143 HOH   HOH B . 
N 6 HOH   99  999  77  HOH   HOH B . 
N 6 HOH   100 1000 49  HOH   HOH B . 
N 6 HOH   101 1001 61  HOH   HOH B . 
N 6 HOH   102 1002 168 HOH   HOH B . 
N 6 HOH   103 1003 66  HOH   HOH B . 
N 6 HOH   104 1004 201 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 GLN 450 ? CG  ? A GLN 16  CG  
2  1 Y 1 A GLN 450 ? CD  ? A GLN 16  CD  
3  1 Y 1 A GLN 450 ? OE1 ? A GLN 16  OE1 
4  1 Y 1 A GLN 450 ? NE2 ? A GLN 16  NE2 
5  1 Y 1 A ARG 481 ? CG  ? A ARG 47  CG  
6  1 Y 1 A ARG 481 ? CD  ? A ARG 47  CD  
7  1 Y 1 A ARG 481 ? NE  ? A ARG 47  NE  
8  1 Y 1 A ARG 481 ? CZ  ? A ARG 47  CZ  
9  1 Y 1 A ARG 481 ? NH1 ? A ARG 47  NH1 
10 1 Y 1 A ARG 481 ? NH2 ? A ARG 47  NH2 
11 1 Y 1 A LYS 518 ? CG  ? A LYS 84  CG  
12 1 Y 1 A LYS 518 ? CD  ? A LYS 84  CD  
13 1 Y 1 A LYS 518 ? CE  ? A LYS 84  CE  
14 1 Y 1 A LYS 518 ? NZ  ? A LYS 84  NZ  
15 1 Y 1 A ARG 520 ? CG  ? A ARG 86  CG  
16 1 Y 1 A ARG 520 ? CD  ? A ARG 86  CD  
17 1 Y 1 A ARG 520 ? NE  ? A ARG 86  NE  
18 1 Y 1 A ARG 520 ? CZ  ? A ARG 86  CZ  
19 1 Y 1 A ARG 520 ? NH1 ? A ARG 86  NH1 
20 1 Y 1 A ARG 520 ? NH2 ? A ARG 86  NH2 
21 1 Y 1 A ARG 524 ? CG  ? A ARG 90  CG  
22 1 Y 1 A ARG 524 ? CD  ? A ARG 90  CD  
23 1 Y 1 A ARG 524 ? NE  ? A ARG 90  NE  
24 1 Y 1 A ARG 524 ? CZ  ? A ARG 90  CZ  
25 1 Y 1 A ARG 524 ? NH1 ? A ARG 90  NH1 
26 1 Y 1 A ARG 524 ? NH2 ? A ARG 90  NH2 
27 1 Y 1 A LYS 577 ? CG  ? A LYS 143 CG  
28 1 Y 1 A LYS 577 ? CD  ? A LYS 143 CD  
29 1 Y 1 A LYS 577 ? CE  ? A LYS 143 CE  
30 1 Y 1 A LYS 577 ? NZ  ? A LYS 143 NZ  
31 1 Y 1 A LYS 672 ? CG  ? A LYS 238 CG  
32 1 Y 1 A LYS 672 ? CD  ? A LYS 238 CD  
33 1 Y 1 A LYS 672 ? CE  ? A LYS 238 CE  
34 1 Y 1 A LYS 672 ? NZ  ? A LYS 238 NZ  
35 1 Y 1 B GLU 497 ? CG  ? B GLU 63  CG  
36 1 Y 1 B GLU 497 ? CD  ? B GLU 63  CD  
37 1 Y 1 B GLU 497 ? OE1 ? B GLU 63  OE1 
38 1 Y 1 B GLU 497 ? OE2 ? B GLU 63  OE2 
39 1 Y 1 B LYS 506 ? CG  ? B LYS 72  CG  
40 1 Y 1 B LYS 506 ? CD  ? B LYS 72  CD  
41 1 Y 1 B LYS 506 ? CE  ? B LYS 72  CE  
42 1 Y 1 B LYS 506 ? NZ  ? B LYS 72  NZ  
43 1 Y 1 B ARG 524 ? CG  ? B ARG 90  CG  
44 1 Y 1 B ARG 524 ? CD  ? B ARG 90  CD  
45 1 Y 1 B ARG 524 ? NE  ? B ARG 90  NE  
46 1 Y 1 B ARG 524 ? CZ  ? B ARG 90  CZ  
47 1 Y 1 B ARG 524 ? NH1 ? B ARG 90  NH1 
48 1 Y 1 B ARG 524 ? NH2 ? B ARG 90  NH2 
49 1 Y 1 B ARG 562 ? CG  ? B ARG 128 CG  
50 1 Y 1 B ARG 562 ? CD  ? B ARG 128 CD  
51 1 Y 1 B ARG 562 ? NE  ? B ARG 128 NE  
52 1 Y 1 B ARG 562 ? CZ  ? B ARG 128 CZ  
53 1 Y 1 B ARG 562 ? NH1 ? B ARG 128 NH1 
54 1 Y 1 B ARG 562 ? NH2 ? B ARG 128 NH2 
55 1 Y 1 B ASP 578 ? CG  ? B ASP 144 CG  
56 1 Y 1 B ASP 578 ? OD1 ? B ASP 144 OD1 
57 1 Y 1 B ASP 578 ? OD2 ? B ASP 144 OD2 
# 
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 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '1.0.5 (20240123)'              1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? 'Jun 30, 2024 (BUILT 20241002)' 2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? 0.7.9                           3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419                     4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 2.8.3                           5 
# 
_cell.angle_alpha                  73.051 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   89.827 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  82.907 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MQP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.168 
_cell.length_a_esd                 ? 
_cell.length_b                     54.190 
_cell.length_b_esd                 ? 
_cell.length_c                     74.349 
_cell.length_c_esd                 ? 
_cell.volume                       184106.256 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9MQP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            'P 1' 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MQP 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.17 
_exptl_crystal.description                  'thin needles' 
_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    
;10 mg/mL HDAC6 zCD2 protein, 0.09 M Bis-Tris (pH 6.0), 0.18 M potassium thiocyanate, 0.01 M cadmium chloride hydrate, 18% (w/v) PEG 3350
;
_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                      'KB bimorph mirrors' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-10-28 
_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                    'Si(111) DCM' 
_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   0.920 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.920 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          12.89 
_reflns.entry_id                                       9MQP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               34.32 
_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                                     79465 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.194 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.765 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.224 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.15 
_reflns_shell.d_res_low                                     2.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6476 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.495 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.624 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.5 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.565 
_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                               14.82 
_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                                 9MQP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.15 
_refine.ls_d_res_low                             34.32 
_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                     38151 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  65876 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.55 
_refine.ls_percent_reflns_R_free                 5.22 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2263 
_refine.ls_R_factor_R_free                       0.2400 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2255 
_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                          1.96 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.9810 
_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                            0.2853 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        34.32 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               5674 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5426 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.0045  ? 5636 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8081  ? 7652 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0485  ? 836  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0055  ? 999  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.3221 ? 2015 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.18  . . 125 2494 85.37 . . . . 0.2861 . . . . . . . . . . . 0.3549 
'X-RAY DIFFRACTION' 2.18 2.21  . . 103 2311 82.05 . . . . 0.3043 . . . . . . . . . . . 0.2797 
'X-RAY DIFFRACTION' 2.21 2.24  . . 125 2284 82.05 . . . . 0.2711 . . . . . . . . . . . 0.3007 
'X-RAY DIFFRACTION' 2.24 2.27  . . 157 2533 87.97 . . . . 0.2772 . . . . . . . . . . . 0.2795 
'X-RAY DIFFRACTION' 2.27 2.31  . . 131 2538 90.78 . . . . 0.2703 . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 2.31 2.35  . . 162 2513 89.70 . . . . 0.2795 . . . . . . . . . . . 0.2768 
'X-RAY DIFFRACTION' 2.35 2.39  . . 132 2580 89.50 . . . . 0.2773 . . . . . . . . . . . 0.2885 
'X-RAY DIFFRACTION' 2.39 2.43  . . 136 2504 88.53 . . . . 0.2545 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 2.43 2.48  . . 162 2429 87.18 . . . . 0.2683 . . . . . . . . . . . 0.3036 
'X-RAY DIFFRACTION' 2.48 2.53  . . 128 2370 83.32 . . . . 0.2567 . . . . . . . . . . . 0.2992 
'X-RAY DIFFRACTION' 2.53 2.58  . . 141 2429 86.77 . . . . 0.2667 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 2.58 2.64  . . 140 2625 92.85 . . . . 0.2440 . . . . . . . . . . . 0.2732 
'X-RAY DIFFRACTION' 2.64 2.71  . . 118 2659 92.94 . . . . 0.2485 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 2.71 2.78  . . 155 2588 92.98 . . . . 0.2372 . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 2.78 2.86  . . 151 2666 93.03 . . . . 0.2393 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 2.86 2.96  . . 133 2631 92.26 . . . . 0.2328 . . . . . . . . . . . 0.2601 
'X-RAY DIFFRACTION' 2.96 3.06  . . 146 2601 92.62 . . . . 0.2263 . . . . . . . . . . . 0.2320 
'X-RAY DIFFRACTION' 3.06 3.18  . . 148 2628 92.53 . . . . 0.2273 . . . . . . . . . . . 0.2196 
'X-RAY DIFFRACTION' 3.18 3.33  . . 137 2533 91.38 . . . . 0.2105 . . . . . . . . . . . 0.2773 
'X-RAY DIFFRACTION' 3.33 3.50  . . 139 2570 90.42 . . . . 0.2078 . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 3.50 3.72  . . 149 2559 89.37 . . . . 0.1843 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 3.72 4.01  . . 120 2379 83.41 . . . . 0.1774 . . . . . . . . . . . 0.1603 
'X-RAY DIFFRACTION' 4.01 4.41  . . 138 2558 91.45 . . . . 0.1773 . . . . . . . . . . . 0.1867 
'X-RAY DIFFRACTION' 4.41 5.05  . . 143 2526 90.35 . . . . 0.1703 . . . . . . . . . . . 0.1798 
'X-RAY DIFFRACTION' 5.05 6.36  . . 151 2632 93.08 . . . . 0.1877 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 6.36 34.32 . . 156 2736 96.40 . . . . 0.1896 . . . . . . . . . . . 0.1702 
# 
_struct.entry_id                     9MQP 
_struct.title                        
'Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 complexed with SelSA' 
_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        9MQP 
_struct_keywords.text            'Hydrolase, histone deacetylase, selenol, inhibitor, metallohydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 3 ? 
I N N 2 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_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   
;SSPITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKP
RDLNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSI
TRESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYM
AAFHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTS
MLLGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLR
;
_struct_ref.pdbx_align_begin           288 
# 
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 9MQP A 6 ? 364 ? A7YT55 288 ? 646 ? 440 798 
2 1 9MQP B 6 ? 364 ? A7YT55 288 ? 646 ? 440 798 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9MQP SER A 1 ? UNP A7YT55 ? ? 'expression tag' 435 1  
1 9MQP ASN A 2 ? UNP A7YT55 ? ? 'expression tag' 436 2  
1 9MQP ALA A 3 ? UNP A7YT55 ? ? 'expression tag' 437 3  
1 9MQP GLY A 4 ? UNP A7YT55 ? ? 'expression tag' 438 4  
1 9MQP GLY A 5 ? UNP A7YT55 ? ? 'expression tag' 439 5  
2 9MQP SER B 1 ? UNP A7YT55 ? ? 'expression tag' 435 6  
2 9MQP ASN B 2 ? UNP A7YT55 ? ? 'expression tag' 436 7  
2 9MQP ALA B 3 ? UNP A7YT55 ? ? 'expression tag' 437 8  
2 9MQP GLY B 4 ? UNP A7YT55 ? ? 'expression tag' 438 9  
2 9MQP GLY B 5 ? UNP A7YT55 ? ? 'expression tag' 439 10 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,M 
2 1 B,H,I,J,K,L,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 15  ? HIS A 21  ? ASP A 449 HIS A 455 5 ? 7  
HELX_P HELX_P2  AA2 PRO A 33  ? LEU A 46  ? PRO A 467 LEU A 480 1 ? 14 
HELX_P HELX_P3  AA3 THR A 61  ? ALA A 66  ? THR A 495 ALA A 500 1 ? 6  
HELX_P HELX_P4  AA4 SER A 70  ? SER A 80  ? SER A 504 SER A 514 1 ? 11 
HELX_P HELX_P5  AA5 GLU A 81  ? MET A 83  ? GLU A 515 MET A 517 5 ? 3  
HELX_P HELX_P6  AA6 LYS A 84  ? GLU A 94  ? LYS A 518 GLU A 528 1 ? 11 
HELX_P HELX_P7  AA7 GLU A 103 ? THR A 124 ? GLU A 537 THR A 558 1 ? 22 
HELX_P HELX_P8  AA8 ASN A 153 ? ILE A 165 ? ASN A 587 ILE A 599 1 ? 13 
HELX_P HELX_P9  AA9 GLY A 182 ? PHE A 189 ? GLY A 616 PHE A 623 1 ? 8  
HELX_P HELX_P10 AB1 SER A 212 ? ASN A 216 ? SER A 646 ASN A 650 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 222 ? ARG A 226 ? LEU A 656 ARG A 660 5 ? 5  
HELX_P HELX_P12 AB3 GLY A 240 ? LEU A 251 ? GLY A 674 LEU A 685 1 ? 12 
HELX_P HELX_P13 AB4 LEU A 251 ? ALA A 260 ? LEU A 685 ALA A 694 1 ? 10 
HELX_P HELX_P14 AB5 THR A 284 ? MET A 296 ? THR A 718 MET A 730 1 ? 13 
HELX_P HELX_P15 AB6 SER A 297 ? GLY A 301 ? SER A 731 GLY A 735 5 ? 5  
HELX_P HELX_P16 AB7 ASN A 312 ? LEU A 328 ? ASN A 746 LEU A 762 1 ? 17 
HELX_P HELX_P17 AB8 LYS A 342 ? ALA A 357 ? LYS A 776 ALA A 791 1 ? 16 
HELX_P HELX_P18 AB9 ASP B 15  ? HIS B 21  ? ASP B 449 HIS B 455 5 ? 7  
HELX_P HELX_P19 AC1 PRO B 33  ? LEU B 46  ? PRO B 467 LEU B 480 1 ? 14 
HELX_P HELX_P20 AC2 LEU B 48  ? CYS B 52  ? LEU B 482 CYS B 486 5 ? 5  
HELX_P HELX_P21 AC3 THR B 61  ? ALA B 66  ? THR B 495 ALA B 500 1 ? 6  
HELX_P HELX_P22 AC4 SER B 70  ? SER B 80  ? SER B 504 SER B 514 1 ? 11 
HELX_P HELX_P23 AC5 GLU B 81  ? MET B 83  ? GLU B 515 MET B 517 5 ? 3  
HELX_P HELX_P24 AC6 LYS B 84  ? GLU B 94  ? LYS B 518 GLU B 528 1 ? 11 
HELX_P HELX_P25 AC7 GLU B 103 ? THR B 124 ? GLU B 537 THR B 558 1 ? 22 
HELX_P HELX_P26 AC8 ASN B 153 ? THR B 166 ? ASN B 587 THR B 600 1 ? 14 
HELX_P HELX_P27 AC9 GLY B 182 ? PHE B 189 ? GLY B 616 PHE B 623 1 ? 8  
HELX_P HELX_P28 AD1 GLU B 204 ? ALA B 207 ? GLU B 638 ALA B 641 5 ? 4  
HELX_P HELX_P29 AD2 SER B 212 ? ASN B 216 ? SER B 646 ASN B 650 5 ? 5  
HELX_P HELX_P30 AD3 LEU B 222 ? ARG B 226 ? LEU B 656 ARG B 660 5 ? 5  
HELX_P HELX_P31 AD4 GLY B 240 ? LEU B 251 ? GLY B 674 LEU B 685 1 ? 12 
HELX_P HELX_P32 AD5 LEU B 251 ? ALA B 260 ? LEU B 685 ALA B 694 1 ? 10 
HELX_P HELX_P33 AD6 THR B 284 ? MET B 296 ? THR B 718 MET B 730 1 ? 13 
HELX_P HELX_P34 AD7 SER B 297 ? GLY B 301 ? SER B 731 GLY B 735 5 ? 5  
HELX_P HELX_P35 AD8 ASN B 312 ? LEU B 328 ? ASN B 746 LEU B 762 1 ? 17 
HELX_P HELX_P36 AD9 LYS B 342 ? ALA B 357 ? LYS B 776 ALA B 791 1 ? 16 
# 
_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 176 O   ? ? ? 1_555 F K   . K  ? ? A ASP 610 A K   804 1_555 ? ? ? ? ? ? ? 2.671 ? ? 
metalc2  metalc ? ? A ASP 176 OD1 ? ? ? 1_555 F K   . K  ? ? A ASP 610 A K   804 1_555 ? ? ? ? ? ? ? 2.763 ? ? 
metalc3  metalc ? ? A ASP 178 OD1 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 612 A ZN  803 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc4  metalc ? ? A ASP 178 O   ? ? ? 1_555 F K   . K  ? ? A ASP 612 A K   804 1_555 ? ? ? ? ? ? ? 2.623 ? ? 
metalc5  metalc ? ? A HIS 180 ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 614 A ZN  803 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc6  metalc ? ? A HIS 180 O   ? ? ? 1_555 F K   . K  ? ? A HIS 614 A K   804 1_555 ? ? ? ? ? ? ? 2.733 ? ? 
metalc7  metalc ? ? A PHE 189 O   ? ? ? 1_555 G K   . K  ? ? A PHE 623 A K   805 1_555 ? ? ? ? ? ? ? 2.612 ? ? 
metalc8  metalc ? ? A ASP 192 O   ? ? ? 1_555 G K   . K  ? ? A ASP 626 A K   805 1_555 ? ? ? ? ? ? ? 2.925 ? ? 
metalc9  metalc ? ? A VAL 195 O   ? ? ? 1_555 G K   . K  ? ? A VAL 629 A K   805 1_555 ? ? ? ? ? ? ? 2.749 ? ? 
metalc10 metalc ? ? A SER 199 OG  ? ? ? 1_555 F K   . K  ? ? A SER 633 A K   804 1_555 ? ? ? ? ? ? ? 2.669 ? ? 
metalc11 metalc ? ? A LEU 200 O   ? ? ? 1_555 F K   . K  ? ? A LEU 634 A K   804 1_555 ? ? ? ? ? ? ? 2.703 ? ? 
metalc12 metalc ? ? A TYR 228 O   ? ? ? 1_555 G K   . K  ? ? A TYR 662 A K   805 1_555 ? ? ? ? ? ? ? 2.815 ? ? 
metalc13 metalc ? ? A ASP 271 OD2 ? ? ? 1_555 E ZN  . ZN ? ? A ASP 705 A ZN  803 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc14 metalc ? ? G K   .   K   ? ? ? 1_555 M HOH . O  ? ? A K   805 A HOH 914 1_555 ? ? ? ? ? ? ? 2.702 ? ? 
metalc15 metalc ? ? G K   .   K   ? ? ? 1_555 M HOH . O  ? ? A K   805 A HOH 958 1_555 ? ? ? ? ? ? ? 3.048 ? ? 
metalc16 metalc ? ? B ASP 176 O   ? ? ? 1_555 K K   . K  ? ? B ASP 610 B K   804 1_555 ? ? ? ? ? ? ? 2.547 ? ? 
metalc17 metalc ? ? B ASP 176 OD1 ? ? ? 1_555 K K   . K  ? ? B ASP 610 B K   804 1_555 ? ? ? ? ? ? ? 2.916 ? ? 
metalc18 metalc ? ? B ASP 178 OD1 ? ? ? 1_555 J ZN  . ZN ? ? B ASP 612 B ZN  803 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc19 metalc ? ? B ASP 178 O   ? ? ? 1_555 K K   . K  ? ? B ASP 612 B K   804 1_555 ? ? ? ? ? ? ? 2.486 ? ? 
metalc20 metalc ? ? B HIS 180 ND1 ? ? ? 1_555 J ZN  . ZN ? ? B HIS 614 B ZN  803 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc21 metalc ? ? B HIS 180 O   ? ? ? 1_555 K K   . K  ? ? B HIS 614 B K   804 1_555 ? ? ? ? ? ? ? 2.804 ? ? 
metalc22 metalc ? ? B PHE 189 O   ? ? ? 1_555 L K   . K  ? ? B PHE 623 B K   805 1_555 ? ? ? ? ? ? ? 2.553 ? ? 
metalc23 metalc ? ? B ASP 192 O   ? ? ? 1_555 L K   . K  ? ? B ASP 626 B K   805 1_555 ? ? ? ? ? ? ? 2.855 ? ? 
metalc24 metalc ? ? B VAL 195 O   ? ? ? 1_555 L K   . K  ? ? B VAL 629 B K   805 1_555 ? ? ? ? ? ? ? 2.720 ? ? 
metalc25 metalc ? ? B SER 199 OG  ? ? ? 1_555 K K   . K  ? ? B SER 633 B K   804 1_555 ? ? ? ? ? ? ? 2.650 ? ? 
metalc26 metalc ? ? B LEU 200 O   ? ? ? 1_555 K K   . K  ? ? B LEU 634 B K   804 1_555 ? ? ? ? ? ? ? 2.643 ? ? 
metalc27 metalc ? ? B TYR 228 O   ? ? ? 1_555 L K   . K  ? ? B TYR 662 B K   805 1_555 ? ? ? ? ? ? ? 2.715 ? ? 
metalc28 metalc ? ? B ASP 271 OD2 ? ? ? 1_555 J ZN  . ZN ? ? B ASP 705 B ZN  803 1_555 ? ? ? ? ? ? ? 1.853 ? ? 
metalc29 metalc ? ? L K   .   K   ? ? ? 1_555 N HOH . O  ? ? B K   805 B HOH 910 1_555 ? ? ? ? ? ? ? 2.682 ? ? 
metalc30 metalc ? ? L K   .   K   ? ? ? 1_555 N HOH . O  ? ? B K   805 B HOH 931 1_555 ? ? ? ? ? ? ? 2.952 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 OD1 ? A ASP 176 ? A ASP 610 ? 1_555 70.3  ? 
2  O   ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A ASP 178 ? A ASP 612 ? 1_555 97.6  ? 
3  OD1 ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A ASP 178 ? A ASP 612 ? 1_555 94.5  ? 
4  O   ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A HIS 180 ? A HIS 614 ? 1_555 161.2 ? 
5  OD1 ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A HIS 180 ? A HIS 614 ? 1_555 91.5  ? 
6  O   ? A ASP 178 ? A ASP 612 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A HIS 180 ? A HIS 614 ? 1_555 78.8  ? 
7  O   ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 OG  ? A SER 199 ? A SER 633 ? 1_555 85.7  ? 
8  OD1 ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 OG  ? A SER 199 ? A SER 633 ? 1_555 113.3 ? 
9  O   ? A ASP 178 ? A ASP 612 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 OG  ? A SER 199 ? A SER 633 ? 1_555 151.3 ? 
10 O   ? A HIS 180 ? A HIS 614 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 OG  ? A SER 199 ? A SER 633 ? 1_555 106.4 ? 
11 O   ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A LEU 200 ? A LEU 634 ? 1_555 77.5  ? 
12 OD1 ? A ASP 176 ? A ASP 610 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A LEU 200 ? A LEU 634 ? 1_555 138.6 ? 
13 O   ? A ASP 178 ? A ASP 612 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A LEU 200 ? A LEU 634 ? 1_555 64.3  ? 
14 O   ? A HIS 180 ? A HIS 614 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A LEU 200 ? A LEU 634 ? 1_555 116.2 ? 
15 OG  ? A SER 199 ? A SER 633 ? 1_555 K  ? F K  . ? A K  804 ? 1_555 O   ? A LEU 200 ? A LEU 634 ? 1_555 88.9  ? 
16 OD1 ? A ASP 178 ? A ASP 612 ? 1_555 ZN ? E ZN . ? A ZN 803 ? 1_555 ND1 ? A HIS 180 ? A HIS 614 ? 1_555 102.1 ? 
17 OD1 ? A ASP 178 ? A ASP 612 ? 1_555 ZN ? E ZN . ? A ZN 803 ? 1_555 OD2 ? A ASP 271 ? A ASP 705 ? 1_555 94.8  ? 
18 ND1 ? A HIS 180 ? A HIS 614 ? 1_555 ZN ? E ZN . ? A ZN 803 ? 1_555 OD2 ? A ASP 271 ? A ASP 705 ? 1_555 95.9  ? 
19 O   ? A PHE 189 ? A PHE 623 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A ASP 192 ? A ASP 626 ? 1_555 77.8  ? 
20 O   ? A PHE 189 ? A PHE 623 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A VAL 195 ? A VAL 629 ? 1_555 117.4 ? 
21 O   ? A ASP 192 ? A ASP 626 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A VAL 195 ? A VAL 629 ? 1_555 74.4  ? 
22 O   ? A PHE 189 ? A PHE 623 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A TYR 228 ? A TYR 662 ? 1_555 154.1 ? 
23 O   ? A ASP 192 ? A ASP 626 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A TYR 228 ? A TYR 662 ? 1_555 115.3 ? 
24 O   ? A VAL 195 ? A VAL 629 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? A TYR 228 ? A TYR 662 ? 1_555 88.3  ? 
25 O   ? A PHE 189 ? A PHE 623 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 914 ? 1_555 82.5  ? 
26 O   ? A ASP 192 ? A ASP 626 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 914 ? 1_555 93.0  ? 
27 O   ? A VAL 195 ? A VAL 629 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 914 ? 1_555 152.4 ? 
28 O   ? A TYR 228 ? A TYR 662 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 914 ? 1_555 74.9  ? 
29 O   ? A PHE 189 ? A PHE 623 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 958 ? 1_555 67.6  ? 
30 O   ? A ASP 192 ? A ASP 626 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 958 ? 1_555 144.8 ? 
31 O   ? A VAL 195 ? A VAL 629 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 958 ? 1_555 127.2 ? 
32 O   ? A TYR 228 ? A TYR 662 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 958 ? 1_555 94.5  ? 
33 O   ? M HOH .   ? A HOH 914 ? 1_555 K  ? G K  . ? A K  805 ? 1_555 O   ? M HOH .   ? A HOH 958 ? 1_555 76.7  ? 
34 O   ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 OD1 ? B ASP 176 ? B ASP 610 ? 1_555 69.8  ? 
35 O   ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B ASP 178 ? B ASP 612 ? 1_555 103.7 ? 
36 OD1 ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B ASP 178 ? B ASP 612 ? 1_555 94.1  ? 
37 O   ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B HIS 180 ? B HIS 614 ? 1_555 159.6 ? 
38 OD1 ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B HIS 180 ? B HIS 614 ? 1_555 90.5  ? 
39 O   ? B ASP 178 ? B ASP 612 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B HIS 180 ? B HIS 614 ? 1_555 71.8  ? 
40 O   ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 OG  ? B SER 199 ? B SER 633 ? 1_555 85.5  ? 
41 OD1 ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 OG  ? B SER 199 ? B SER 633 ? 1_555 112.7 ? 
42 O   ? B ASP 178 ? B ASP 612 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 OG  ? B SER 199 ? B SER 633 ? 1_555 153.2 ? 
43 O   ? B HIS 180 ? B HIS 614 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 OG  ? B SER 199 ? B SER 633 ? 1_555 107.6 ? 
44 O   ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B LEU 200 ? B LEU 634 ? 1_555 82.1  ? 
45 OD1 ? B ASP 176 ? B ASP 610 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B LEU 200 ? B LEU 634 ? 1_555 142.4 ? 
46 O   ? B ASP 178 ? B ASP 612 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B LEU 200 ? B LEU 634 ? 1_555 68.2  ? 
47 O   ? B HIS 180 ? B HIS 614 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B LEU 200 ? B LEU 634 ? 1_555 113.0 ? 
48 OG  ? B SER 199 ? B SER 633 ? 1_555 K  ? K K  . ? B K  804 ? 1_555 O   ? B LEU 200 ? B LEU 634 ? 1_555 88.7  ? 
49 OD1 ? B ASP 178 ? B ASP 612 ? 1_555 ZN ? J ZN . ? B ZN 803 ? 1_555 ND1 ? B HIS 180 ? B HIS 614 ? 1_555 102.1 ? 
50 OD1 ? B ASP 178 ? B ASP 612 ? 1_555 ZN ? J ZN . ? B ZN 803 ? 1_555 OD2 ? B ASP 271 ? B ASP 705 ? 1_555 93.6  ? 
51 ND1 ? B HIS 180 ? B HIS 614 ? 1_555 ZN ? J ZN . ? B ZN 803 ? 1_555 OD2 ? B ASP 271 ? B ASP 705 ? 1_555 93.2  ? 
52 O   ? B PHE 189 ? B PHE 623 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B ASP 192 ? B ASP 626 ? 1_555 73.9  ? 
53 O   ? B PHE 189 ? B PHE 623 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B VAL 195 ? B VAL 629 ? 1_555 120.1 ? 
54 O   ? B ASP 192 ? B ASP 626 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B VAL 195 ? B VAL 629 ? 1_555 75.8  ? 
55 O   ? B PHE 189 ? B PHE 623 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B TYR 228 ? B TYR 662 ? 1_555 150.0 ? 
56 O   ? B ASP 192 ? B ASP 626 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B TYR 228 ? B TYR 662 ? 1_555 119.6 ? 
57 O   ? B VAL 195 ? B VAL 629 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? B TYR 228 ? B TYR 662 ? 1_555 89.8  ? 
58 O   ? B PHE 189 ? B PHE 623 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 910 ? 1_555 81.3  ? 
59 O   ? B ASP 192 ? B ASP 626 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 910 ? 1_555 92.4  ? 
60 O   ? B VAL 195 ? B VAL 629 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 910 ? 1_555 150.0 ? 
61 O   ? B TYR 228 ? B TYR 662 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 910 ? 1_555 71.9  ? 
62 O   ? B PHE 189 ? B PHE 623 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 931 ? 1_555 65.7  ? 
63 O   ? B ASP 192 ? B ASP 626 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 931 ? 1_555 139.0 ? 
64 O   ? B VAL 195 ? B VAL 629 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 931 ? 1_555 130.8 ? 
65 O   ? B TYR 228 ? B TYR 662 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 931 ? 1_555 94.1  ? 
66 O   ? N HOH .   ? B HOH 910 ? 1_555 K  ? L K  . ? B K  805 ? 1_555 O   ? N HOH .   ? B HOH 931 ? 1_555 75.6  ? 
# 
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 135 A . ? ARG 569 A PRO 136 A ? PRO 570 A 1 -4.76 
2 PHE 209 A . ? PHE 643 A PRO 210 A ? PRO 644 A 1 3.42  
3 ARG 135 B . ? ARG 569 B PRO 136 B ? PRO 570 B 1 -3.91 
4 PHE 209 B . ? PHE 643 B PRO 210 B ? PRO 644 B 1 1.50  
# 
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 53  ? ARG A 54  ? HIS A 487 ARG A 488 
AA1 2 THR A 10  ? VAL A 13  ? THR A 444 VAL A 447 
AA1 3 ASN A 129 ? ALA A 132 ? ASN A 563 ALA A 566 
AA1 4 VAL A 303 ? LEU A 307 ? VAL A 737 LEU A 741 
AA1 5 LEU A 263 ? ALA A 268 ? LEU A 697 ALA A 702 
AA1 6 VAL A 172 ? ASP A 176 ? VAL A 606 ASP A 610 
AA1 7 VAL A 195 ? ARG A 202 ? VAL A 629 ARG A 636 
AA1 8 ASN A 229 ? TRP A 234 ? ASN A 663 TRP A 668 
AA2 1 HIS B 53  ? ARG B 54  ? HIS B 487 ARG B 488 
AA2 2 THR B 10  ? VAL B 13  ? THR B 444 VAL B 447 
AA2 3 ASN B 129 ? ALA B 132 ? ASN B 563 ALA B 566 
AA2 4 VAL B 303 ? LEU B 307 ? VAL B 737 LEU B 741 
AA2 5 LEU B 263 ? ALA B 268 ? LEU B 697 ALA B 702 
AA2 6 VAL B 172 ? ASP B 176 ? VAL B 606 ASP B 610 
AA2 7 VAL B 195 ? ARG B 202 ? VAL B 629 ARG B 636 
AA2 8 ASN B 229 ? TRP B 234 ? 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 53  ? O HIS A 487 N THR A 10  ? N THR A 444 
AA1 2 3 N GLY A 11  ? N GLY A 445 O ASN A 129 ? O ASN A 563 
AA1 3 4 N ALA A 132 ? N ALA A 566 O ILE A 305 ? O ILE A 739 
AA1 4 5 O LEU A 304 ? O LEU A 738 N VAL A 266 ? N VAL A 700 
AA1 5 6 O LEU A 265 ? O LEU A 699 N LEU A 173 ? N LEU A 607 
AA1 6 7 N ASP A 176 ? N ASP A 610 O ILE A 198 ? O ILE A 632 
AA1 7 8 N SER A 199 ? N SER A 633 O ILE A 232 ? O ILE A 666 
AA2 1 2 O HIS B 53  ? O HIS B 487 N THR B 10  ? N THR B 444 
AA2 2 3 N GLY B 11  ? N GLY B 445 O ASN B 129 ? O ASN B 563 
AA2 3 4 N ALA B 132 ? N ALA B 566 O ILE B 305 ? O ILE B 739 
AA2 4 5 O LEU B 304 ? O LEU B 738 N VAL B 266 ? N VAL B 700 
AA2 5 6 O LEU B 265 ? O LEU B 699 N LEU B 173 ? N LEU B 607 
AA2 6 7 N ASP B 176 ? N ASP B 610 O ILE B 198 ? O ILE B 632 
AA2 7 8 N TYR B 197 ? N TYR B 631 O VAL B 230 ? O VAL B 664 
# 
_pdbx_entry_details.entry_id                   9MQP 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 460 ? ? -157.62 88.35   
2  1 SER A 531 ? ? 61.64   62.83   
3  1 PHE A 583 ? ? 70.77   -1.03   
4  1 PHE A 585 ? ? -109.09 -60.45  
5  1 THR A 600 ? ? -125.20 -84.45  
6  1 LEU A 685 ? ? -126.48 -68.74  
7  1 GLU A 742 ? ? -118.91 -111.45 
8  1 ASP B 460 ? ? -161.28 94.15   
9  1 PRO B 571 ? ? -65.94  -177.75 
10 1 THR B 600 ? ? -118.70 -73.87  
11 1 TYR B 637 ? ? -126.46 -53.02  
12 1 LEU B 685 ? ? -127.68 -64.19  
13 1 ALA B 702 ? ? -107.16 67.16   
14 1 GLU B 742 ? ? -112.76 -107.09 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -19.8239137685 9.81983209205 25.2636907739 0.0742665767593 ? -0.0173113506459   ? -0.0156372300669 
? 0.08762339354   ? 0.00291183892861 ? 0.091389118281  ? 0.912652727532 ? -0.377530809217 ? -0.0979341691951  ? 0.611920206313 ? 
0.224167494236   ? 0.659198286191 ? 0.0283635367516   ? -0.0320587069019  ? -0.0779447889645 ? -0.0269128902725 ? -0.0474333089588 
? 0.0690570759024    ? 0.109992899021   ? -0.0558099453231 ? 0.0138327929751  ? 
2 'X-RAY DIFFRACTION' ? refined -4.68827318607 22.1490925512 28.2308127055 0.0739573762309 ? -0.000894190038767 ? 
0.000177434623443 ? 0.0820898830491 ? -0.0098898692915 ? 0.0892577845358 ? 1.03705998126  ? 0.294564955678  ? 0.125795830724    ? 
0.498667080522 ? -0.0515953326479 ? 0.949264243739 ? -0.00107936204056 ? -0.0236530472152  ? 0.0216016719755  ? 0.0215095899417  ? 
0.0122439364447  ? -0.0639311443956   ? -0.011515146926  ? 0.0391908719735  ? -0.0137077990659 ? 
3 'X-RAY DIFFRACTION' ? refined -49.2576242905 40.549434294  58.4256734511 0.092740434994  ? -0.0134204737023   ? 0.0202737801254 
? 0.180386585031  ? 0.0679328933357  ? 0.134985044835  ? 1.31945765858  ? -0.393963662902 ? 0.712037943221    ? 1.39754880479  ? 
-0.266000248854  ? 1.37360232972  ? 0.074675083782    ? -0.0381934908024  ? -0.0173040311046 ? 0.0404855173074  ? 0.0100056730378  
? 0.224025647702     ? -0.134861508     ? -0.0167938777349 ? -0.101776184823  ? 
4 'X-RAY DIFFRACTION' ? refined -43.8348927302 43.0917619955 63.905762587  0.0539549404666 ? -0.0182285555024   ? 
-0.00189902195059 ? 0.129789313307  ? 0.00877029990259 ? 0.0902100301614 ? 0.527016651372 ? 0.0545413244249 ? -0.00630507744891 ? 
0.663311202136 ? 0.0633786353122  ? 0.814049571515 ? 0.0559772266093   ? -0.134936856291   ? 0.0403811968434  ? 0.00778972824326 ? 
-0.172589389157  ? -0.000867126623758 ? -0.0295634775307 ? -0.086418127812  ? 0.103392350083   ? 
5 'X-RAY DIFFRACTION' ? refined -31.7540391764 39.8797990995 56.0531852747 0.0857152658237 ? -0.00722273475275  ? 0.00318841789313 
? 0.129940840118  ? 0.0051515222331  ? 0.0887775731539 ? 0.591034605272 ? -0.102943241932 ? 0.20723473329     ? 0.650613536709 ? 
0.393562727187   ? 1.19068556136  ? 0.0481695207252   ? 0.079178414132    ? 0.039486974138   ? -0.0400471977154 ? -0.033266057554  
? -0.0489379473179   ? -0.0216623798735 ? 0.12855085083    ? -0.0190992337283 ? 
6 'X-RAY DIFFRACTION' ? refined -30.7293225681 26.6933156451 60.2221115958 0.0841580096549 ? 0.000388845843161  ? 
-0.00831111125843 ? 0.175605363963  ? -0.0453346539726 ? 0.133101815306  ? 0.715444123562 ? -0.139566067836 ? -0.272462692758   ? 
0.418547654212 ? -0.2601996473    ? 0.454175766886 ? 0.041390655626    ? -0.00342069760903 ? -0.011051161512  ? 0.0904579369019  ? 
0.0210834927183  ? -0.0486734439473   ? 0.109533572162   ? 0.122682172382   ? -0.0460140748399 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 442 ? A 136 A 577 ? ? 
;chain 'A' and (resid 442 through 577 )
;
2 'X-RAY DIFFRACTION' 2 A 137 A 578 ? A 353 A 797 ? ? 
;chain 'A' and (resid 578 through 797 )
;
3 'X-RAY DIFFRACTION' 3 D 1   B 442 ? D 25  B 466 ? ? 
;chain 'B' and (resid 442 through 466 )
;
4 'X-RAY DIFFRACTION' 4 D 26  B 467 ? D 75  B 516 ? ? 
;chain 'B' and (resid 467 through 516 )
;
5 'X-RAY DIFFRACTION' 5 D 76  B 517 ? D 243 B 684 ? ? 
;chain 'B' and (resid 517 through 684 )
;
6 'X-RAY DIFFRACTION' 6 D 244 B 685 ? D 350 B 797 ? ? 
;chain 'B' and (resid 685 through 797 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1004 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.31 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 435 ? A SER 1   
2  1 Y 1 A ASN 436 ? A ASN 2   
3  1 Y 1 A ALA 437 ? A ALA 3   
4  1 Y 1 A GLY 438 ? A GLY 4   
5  1 Y 1 A GLY 439 ? A GLY 5   
6  1 Y 1 A SER 440 ? A SER 6   
7  1 Y 1 A SER 441 ? A SER 7   
8  1 Y 1 A ASP 770 ? A ASP 336 
9  1 Y 1 A HIS 771 ? A HIS 337 
10 1 Y 1 A LEU 772 ? A LEU 338 
11 1 Y 1 A ARG 798 ? A ARG 364 
12 1 Y 1 B SER 435 ? B SER 1   
13 1 Y 1 B ASN 436 ? B ASN 2   
14 1 Y 1 B ALA 437 ? B ALA 3   
15 1 Y 1 B GLY 438 ? B GLY 4   
16 1 Y 1 B GLY 439 ? B GLY 5   
17 1 Y 1 B SER 440 ? B SER 6   
18 1 Y 1 B SER 441 ? B SER 7   
19 1 Y 1 B SER 768 ? B SER 334 
20 1 Y 1 B LEU 769 ? B LEU 335 
21 1 Y 1 B ASP 770 ? B ASP 336 
22 1 Y 1 B HIS 771 ? B HIS 337 
23 1 Y 1 B LEU 772 ? B LEU 338 
24 1 Y 1 B THR 773 ? B THR 339 
25 1 Y 1 B ARG 798 ? B ARG 364 
# 
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 
A1BNN C13  C  Y N 1   
A1BNN C02  C  N N 2   
A1BNN C03  C  N N 3   
A1BNN C04  C  N N 4   
A1BNN C05  C  N N 5   
A1BNN C06  C  N N 6   
A1BNN C07  C  N N 7   
A1BNN C09  C  Y N 8   
A1BNN C10  C  Y N 9   
A1BNN C11  C  Y N 10  
A1BNN C12  C  Y N 11  
A1BNN C14  C  Y N 12  
A1BNN N08  N  N N 13  
A1BNN O15  O  N N 14  
A1BNN SE01 SE N N 15  
A1BNN H131 H  N N 16  
A1BNN H021 H  N N 17  
A1BNN H022 H  N N 18  
A1BNN H032 H  N N 19  
A1BNN H031 H  N N 20  
A1BNN H042 H  N N 21  
A1BNN H041 H  N N 22  
A1BNN H051 H  N N 23  
A1BNN H052 H  N N 24  
A1BNN H061 H  N N 25  
A1BNN H062 H  N N 26  
A1BNN H101 H  N N 27  
A1BNN H111 H  N N 28  
A1BNN H121 H  N N 29  
A1BNN H141 H  N N 30  
A1BNN H081 H  N N 31  
A1BNN H011 H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
EDO   C1   C  N N 120 
EDO   O1   O  N N 121 
EDO   C2   C  N N 122 
EDO   O2   O  N N 123 
EDO   H11  H  N N 124 
EDO   H12  H  N N 125 
EDO   HO1  H  N N 126 
EDO   H21  H  N N 127 
EDO   H22  H  N N 128 
EDO   HO2  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
K     K    K  N N 225 
LEU   N    N  N N 226 
LEU   CA   C  N S 227 
LEU   C    C  N N 228 
LEU   O    O  N N 229 
LEU   CB   C  N N 230 
LEU   CG   C  N N 231 
LEU   CD1  C  N N 232 
LEU   CD2  C  N N 233 
LEU   OXT  O  N N 234 
LEU   H    H  N N 235 
LEU   H2   H  N N 236 
LEU   HA   H  N N 237 
LEU   HB2  H  N N 238 
LEU   HB3  H  N N 239 
LEU   HG   H  N N 240 
LEU   HD11 H  N N 241 
LEU   HD12 H  N N 242 
LEU   HD13 H  N N 243 
LEU   HD21 H  N N 244 
LEU   HD22 H  N N 245 
LEU   HD23 H  N N 246 
LEU   HXT  H  N N 247 
LYS   N    N  N N 248 
LYS   CA   C  N S 249 
LYS   C    C  N N 250 
LYS   O    O  N N 251 
LYS   CB   C  N N 252 
LYS   CG   C  N N 253 
LYS   CD   C  N N 254 
LYS   CE   C  N N 255 
LYS   NZ   N  N N 256 
LYS   OXT  O  N N 257 
LYS   H    H  N N 258 
LYS   H2   H  N N 259 
LYS   HA   H  N N 260 
LYS   HB2  H  N N 261 
LYS   HB3  H  N N 262 
LYS   HG2  H  N N 263 
LYS   HG3  H  N N 264 
LYS   HD2  H  N N 265 
LYS   HD3  H  N N 266 
LYS   HE2  H  N N 267 
LYS   HE3  H  N N 268 
LYS   HZ1  H  N N 269 
LYS   HZ2  H  N N 270 
LYS   HZ3  H  N N 271 
LYS   HXT  H  N N 272 
MET   N    N  N N 273 
MET   CA   C  N S 274 
MET   C    C  N N 275 
MET   O    O  N N 276 
MET   CB   C  N N 277 
MET   CG   C  N N 278 
MET   SD   S  N N 279 
MET   CE   C  N N 280 
MET   OXT  O  N N 281 
MET   H    H  N N 282 
MET   H2   H  N N 283 
MET   HA   H  N N 284 
MET   HB2  H  N N 285 
MET   HB3  H  N N 286 
MET   HG2  H  N N 287 
MET   HG3  H  N N 288 
MET   HE1  H  N N 289 
MET   HE2  H  N N 290 
MET   HE3  H  N N 291 
MET   HXT  H  N N 292 
PHE   N    N  N N 293 
PHE   CA   C  N S 294 
PHE   C    C  N N 295 
PHE   O    O  N N 296 
PHE   CB   C  N N 297 
PHE   CG   C  Y N 298 
PHE   CD1  C  Y N 299 
PHE   CD2  C  Y N 300 
PHE   CE1  C  Y N 301 
PHE   CE2  C  Y N 302 
PHE   CZ   C  Y N 303 
PHE   OXT  O  N N 304 
PHE   H    H  N N 305 
PHE   H2   H  N N 306 
PHE   HA   H  N N 307 
PHE   HB2  H  N N 308 
PHE   HB3  H  N N 309 
PHE   HD1  H  N N 310 
PHE   HD2  H  N N 311 
PHE   HE1  H  N N 312 
PHE   HE2  H  N N 313 
PHE   HZ   H  N N 314 
PHE   HXT  H  N N 315 
PRO   N    N  N N 316 
PRO   CA   C  N S 317 
PRO   C    C  N N 318 
PRO   O    O  N N 319 
PRO   CB   C  N N 320 
PRO   CG   C  N N 321 
PRO   CD   C  N N 322 
PRO   OXT  O  N N 323 
PRO   H    H  N N 324 
PRO   HA   H  N N 325 
PRO   HB2  H  N N 326 
PRO   HB3  H  N N 327 
PRO   HG2  H  N N 328 
PRO   HG3  H  N N 329 
PRO   HD2  H  N N 330 
PRO   HD3  H  N N 331 
PRO   HXT  H  N N 332 
SER   N    N  N N 333 
SER   CA   C  N S 334 
SER   C    C  N N 335 
SER   O    O  N N 336 
SER   CB   C  N N 337 
SER   OG   O  N N 338 
SER   OXT  O  N N 339 
SER   H    H  N N 340 
SER   H2   H  N N 341 
SER   HA   H  N N 342 
SER   HB2  H  N N 343 
SER   HB3  H  N N 344 
SER   HG   H  N N 345 
SER   HXT  H  N N 346 
THR   N    N  N N 347 
THR   CA   C  N S 348 
THR   C    C  N N 349 
THR   O    O  N N 350 
THR   CB   C  N R 351 
THR   OG1  O  N N 352 
THR   CG2  C  N N 353 
THR   OXT  O  N N 354 
THR   H    H  N N 355 
THR   H2   H  N N 356 
THR   HA   H  N N 357 
THR   HB   H  N N 358 
THR   HG1  H  N N 359 
THR   HG21 H  N N 360 
THR   HG22 H  N N 361 
THR   HG23 H  N N 362 
THR   HXT  H  N N 363 
TRP   N    N  N N 364 
TRP   CA   C  N S 365 
TRP   C    C  N N 366 
TRP   O    O  N N 367 
TRP   CB   C  N N 368 
TRP   CG   C  Y N 369 
TRP   CD1  C  Y N 370 
TRP   CD2  C  Y N 371 
TRP   NE1  N  Y N 372 
TRP   CE2  C  Y N 373 
TRP   CE3  C  Y N 374 
TRP   CZ2  C  Y N 375 
TRP   CZ3  C  Y N 376 
TRP   CH2  C  Y N 377 
TRP   OXT  O  N N 378 
TRP   H    H  N N 379 
TRP   H2   H  N N 380 
TRP   HA   H  N N 381 
TRP   HB2  H  N N 382 
TRP   HB3  H  N N 383 
TRP   HD1  H  N N 384 
TRP   HE1  H  N N 385 
TRP   HE3  H  N N 386 
TRP   HZ2  H  N N 387 
TRP   HZ3  H  N N 388 
TRP   HH2  H  N N 389 
TRP   HXT  H  N N 390 
TYR   N    N  N N 391 
TYR   CA   C  N S 392 
TYR   C    C  N N 393 
TYR   O    O  N N 394 
TYR   CB   C  N N 395 
TYR   CG   C  Y N 396 
TYR   CD1  C  Y N 397 
TYR   CD2  C  Y N 398 
TYR   CE1  C  Y N 399 
TYR   CE2  C  Y N 400 
TYR   CZ   C  Y N 401 
TYR   OH   O  N N 402 
TYR   OXT  O  N N 403 
TYR   H    H  N N 404 
TYR   H2   H  N N 405 
TYR   HA   H  N N 406 
TYR   HB2  H  N N 407 
TYR   HB3  H  N N 408 
TYR   HD1  H  N N 409 
TYR   HD2  H  N N 410 
TYR   HE1  H  N N 411 
TYR   HE2  H  N N 412 
TYR   HH   H  N N 413 
TYR   HXT  H  N N 414 
VAL   N    N  N N 415 
VAL   CA   C  N S 416 
VAL   C    C  N N 417 
VAL   O    O  N N 418 
VAL   CB   C  N N 419 
VAL   CG1  C  N N 420 
VAL   CG2  C  N N 421 
VAL   OXT  O  N N 422 
VAL   H    H  N N 423 
VAL   H2   H  N N 424 
VAL   HA   H  N N 425 
VAL   HB   H  N N 426 
VAL   HG11 H  N N 427 
VAL   HG12 H  N N 428 
VAL   HG13 H  N N 429 
VAL   HG21 H  N N 430 
VAL   HG22 H  N N 431 
VAL   HG23 H  N N 432 
VAL   HXT  H  N N 433 
ZN    ZN   ZN N N 434 
# 
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 
A1BNN C02  SE01 sing N N 1   
A1BNN C03  C02  sing N N 2   
A1BNN C04  C03  sing N N 3   
A1BNN C05  C04  sing N N 4   
A1BNN C06  C05  sing N N 5   
A1BNN C07  C06  sing N N 6   
A1BNN C09  N08  sing N N 7   
A1BNN C10  C09  doub Y N 8   
A1BNN C11  C10  sing Y N 9   
A1BNN C12  C11  doub Y N 10  
A1BNN C13  C12  sing Y N 11  
A1BNN C14  C13  doub Y N 12  
A1BNN N08  C07  sing N N 13  
A1BNN O15  C07  doub N N 14  
A1BNN C09  C14  sing Y N 15  
A1BNN C13  H131 sing N N 16  
A1BNN C02  H021 sing N N 17  
A1BNN C02  H022 sing N N 18  
A1BNN C03  H032 sing N N 19  
A1BNN C03  H031 sing N N 20  
A1BNN C04  H042 sing N N 21  
A1BNN C04  H041 sing N N 22  
A1BNN C05  H051 sing N N 23  
A1BNN C05  H052 sing N N 24  
A1BNN C06  H061 sing N N 25  
A1BNN C06  H062 sing N N 26  
A1BNN C10  H101 sing N N 27  
A1BNN C11  H111 sing N N 28  
A1BNN C12  H121 sing N N 29  
A1BNN C14  H141 sing N N 30  
A1BNN N08  H081 sing N N 31  
A1BNN SE01 H011 sing N N 32  
ALA   N    CA   sing N N 33  
ALA   N    H    sing N N 34  
ALA   N    H2   sing N N 35  
ALA   CA   C    sing N N 36  
ALA   CA   CB   sing N N 37  
ALA   CA   HA   sing N N 38  
ALA   C    O    doub N N 39  
ALA   C    OXT  sing N N 40  
ALA   CB   HB1  sing N N 41  
ALA   CB   HB2  sing N N 42  
ALA   CB   HB3  sing N N 43  
ALA   OXT  HXT  sing N N 44  
ARG   N    CA   sing N N 45  
ARG   N    H    sing N N 46  
ARG   N    H2   sing N N 47  
ARG   CA   C    sing N N 48  
ARG   CA   CB   sing N N 49  
ARG   CA   HA   sing N N 50  
ARG   C    O    doub N N 51  
ARG   C    OXT  sing N N 52  
ARG   CB   CG   sing N N 53  
ARG   CB   HB2  sing N N 54  
ARG   CB   HB3  sing N N 55  
ARG   CG   CD   sing N N 56  
ARG   CG   HG2  sing N N 57  
ARG   CG   HG3  sing N N 58  
ARG   CD   NE   sing N N 59  
ARG   CD   HD2  sing N N 60  
ARG   CD   HD3  sing N N 61  
ARG   NE   CZ   sing N N 62  
ARG   NE   HE   sing N N 63  
ARG   CZ   NH1  sing N N 64  
ARG   CZ   NH2  doub N N 65  
ARG   NH1  HH11 sing N N 66  
ARG   NH1  HH12 sing N N 67  
ARG   NH2  HH21 sing N N 68  
ARG   NH2  HH22 sing N N 69  
ARG   OXT  HXT  sing N N 70  
ASN   N    CA   sing N N 71  
ASN   N    H    sing N N 72  
ASN   N    H2   sing N N 73  
ASN   CA   C    sing N N 74  
ASN   CA   CB   sing N N 75  
ASN   CA   HA   sing N N 76  
ASN   C    O    doub N N 77  
ASN   C    OXT  sing N N 78  
ASN   CB   CG   sing N N 79  
ASN   CB   HB2  sing N N 80  
ASN   CB   HB3  sing N N 81  
ASN   CG   OD1  doub N N 82  
ASN   CG   ND2  sing N N 83  
ASN   ND2  HD21 sing N N 84  
ASN   ND2  HD22 sing N N 85  
ASN   OXT  HXT  sing N N 86  
ASP   N    CA   sing N N 87  
ASP   N    H    sing N N 88  
ASP   N    H2   sing N N 89  
ASP   CA   C    sing N N 90  
ASP   CA   CB   sing N N 91  
ASP   CA   HA   sing N N 92  
ASP   C    O    doub N N 93  
ASP   C    OXT  sing N N 94  
ASP   CB   CG   sing N N 95  
ASP   CB   HB2  sing N N 96  
ASP   CB   HB3  sing N N 97  
ASP   CG   OD1  doub N N 98  
ASP   CG   OD2  sing N N 99  
ASP   OD2  HD2  sing N N 100 
ASP   OXT  HXT  sing N N 101 
CYS   N    CA   sing N N 102 
CYS   N    H    sing N N 103 
CYS   N    H2   sing N N 104 
CYS   CA   C    sing N N 105 
CYS   CA   CB   sing N N 106 
CYS   CA   HA   sing N N 107 
CYS   C    O    doub N N 108 
CYS   C    OXT  sing N N 109 
CYS   CB   SG   sing N N 110 
CYS   CB   HB2  sing N N 111 
CYS   CB   HB3  sing N N 112 
CYS   SG   HG   sing N N 113 
CYS   OXT  HXT  sing N N 114 
EDO   C1   O1   sing N N 115 
EDO   C1   C2   sing N N 116 
EDO   C1   H11  sing N N 117 
EDO   C1   H12  sing N N 118 
EDO   O1   HO1  sing N N 119 
EDO   C2   O2   sing N N 120 
EDO   C2   H21  sing N N 121 
EDO   C2   H22  sing N N 122 
EDO   O2   HO2  sing N N 123 
GLN   N    CA   sing N N 124 
GLN   N    H    sing N N 125 
GLN   N    H2   sing N N 126 
GLN   CA   C    sing N N 127 
GLN   CA   CB   sing N N 128 
GLN   CA   HA   sing N N 129 
GLN   C    O    doub N N 130 
GLN   C    OXT  sing N N 131 
GLN   CB   CG   sing N N 132 
GLN   CB   HB2  sing N N 133 
GLN   CB   HB3  sing N N 134 
GLN   CG   CD   sing N N 135 
GLN   CG   HG2  sing N N 136 
GLN   CG   HG3  sing N N 137 
GLN   CD   OE1  doub N N 138 
GLN   CD   NE2  sing N N 139 
GLN   NE2  HE21 sing N N 140 
GLN   NE2  HE22 sing N N 141 
GLN   OXT  HXT  sing N N 142 
GLU   N    CA   sing N N 143 
GLU   N    H    sing N N 144 
GLU   N    H2   sing N N 145 
GLU   CA   C    sing N N 146 
GLU   CA   CB   sing N N 147 
GLU   CA   HA   sing N N 148 
GLU   C    O    doub N N 149 
GLU   C    OXT  sing N N 150 
GLU   CB   CG   sing N N 151 
GLU   CB   HB2  sing N N 152 
GLU   CB   HB3  sing N N 153 
GLU   CG   CD   sing N N 154 
GLU   CG   HG2  sing N N 155 
GLU   CG   HG3  sing N N 156 
GLU   CD   OE1  doub N N 157 
GLU   CD   OE2  sing N N 158 
GLU   OE2  HE2  sing N N 159 
GLU   OXT  HXT  sing N N 160 
GLY   N    CA   sing N N 161 
GLY   N    H    sing N N 162 
GLY   N    H2   sing N N 163 
GLY   CA   C    sing N N 164 
GLY   CA   HA2  sing N N 165 
GLY   CA   HA3  sing N N 166 
GLY   C    O    doub N N 167 
GLY   C    OXT  sing N N 168 
GLY   OXT  HXT  sing N N 169 
HIS   N    CA   sing N N 170 
HIS   N    H    sing N N 171 
HIS   N    H2   sing N N 172 
HIS   CA   C    sing N N 173 
HIS   CA   CB   sing N N 174 
HIS   CA   HA   sing N N 175 
HIS   C    O    doub N N 176 
HIS   C    OXT  sing N N 177 
HIS   CB   CG   sing N N 178 
HIS   CB   HB2  sing N N 179 
HIS   CB   HB3  sing N N 180 
HIS   CG   ND1  sing Y N 181 
HIS   CG   CD2  doub Y N 182 
HIS   ND1  CE1  doub Y N 183 
HIS   ND1  HD1  sing N N 184 
HIS   CD2  NE2  sing Y N 185 
HIS   CD2  HD2  sing N N 186 
HIS   CE1  NE2  sing Y N 187 
HIS   CE1  HE1  sing N N 188 
HIS   NE2  HE2  sing N N 189 
HIS   OXT  HXT  sing N N 190 
HOH   O    H1   sing N N 191 
HOH   O    H2   sing N N 192 
ILE   N    CA   sing N N 193 
ILE   N    H    sing N N 194 
ILE   N    H2   sing N N 195 
ILE   CA   C    sing N N 196 
ILE   CA   CB   sing N N 197 
ILE   CA   HA   sing N N 198 
ILE   C    O    doub N N 199 
ILE   C    OXT  sing N N 200 
ILE   CB   CG1  sing N N 201 
ILE   CB   CG2  sing N N 202 
ILE   CB   HB   sing N N 203 
ILE   CG1  CD1  sing N N 204 
ILE   CG1  HG12 sing N N 205 
ILE   CG1  HG13 sing N N 206 
ILE   CG2  HG21 sing N N 207 
ILE   CG2  HG22 sing N N 208 
ILE   CG2  HG23 sing N N 209 
ILE   CD1  HD11 sing N N 210 
ILE   CD1  HD12 sing N N 211 
ILE   CD1  HD13 sing N N 212 
ILE   OXT  HXT  sing N N 213 
LEU   N    CA   sing N N 214 
LEU   N    H    sing N N 215 
LEU   N    H2   sing N N 216 
LEU   CA   C    sing N N 217 
LEU   CA   CB   sing N N 218 
LEU   CA   HA   sing N N 219 
LEU   C    O    doub N N 220 
LEU   C    OXT  sing N N 221 
LEU   CB   CG   sing N N 222 
LEU   CB   HB2  sing N N 223 
LEU   CB   HB3  sing N N 224 
LEU   CG   CD1  sing N N 225 
LEU   CG   CD2  sing N N 226 
LEU   CG   HG   sing N N 227 
LEU   CD1  HD11 sing N N 228 
LEU   CD1  HD12 sing N N 229 
LEU   CD1  HD13 sing N N 230 
LEU   CD2  HD21 sing N N 231 
LEU   CD2  HD22 sing N N 232 
LEU   CD2  HD23 sing N N 233 
LEU   OXT  HXT  sing N N 234 
LYS   N    CA   sing N N 235 
LYS   N    H    sing N N 236 
LYS   N    H2   sing N N 237 
LYS   CA   C    sing N N 238 
LYS   CA   CB   sing N N 239 
LYS   CA   HA   sing N N 240 
LYS   C    O    doub N N 241 
LYS   C    OXT  sing N N 242 
LYS   CB   CG   sing N N 243 
LYS   CB   HB2  sing N N 244 
LYS   CB   HB3  sing N N 245 
LYS   CG   CD   sing N N 246 
LYS   CG   HG2  sing N N 247 
LYS   CG   HG3  sing N N 248 
LYS   CD   CE   sing N N 249 
LYS   CD   HD2  sing N N 250 
LYS   CD   HD3  sing N N 251 
LYS   CE   NZ   sing N N 252 
LYS   CE   HE2  sing N N 253 
LYS   CE   HE3  sing N N 254 
LYS   NZ   HZ1  sing N N 255 
LYS   NZ   HZ2  sing N N 256 
LYS   NZ   HZ3  sing N N 257 
LYS   OXT  HXT  sing N N 258 
MET   N    CA   sing N N 259 
MET   N    H    sing N N 260 
MET   N    H2   sing N N 261 
MET   CA   C    sing N N 262 
MET   CA   CB   sing N N 263 
MET   CA   HA   sing N N 264 
MET   C    O    doub N N 265 
MET   C    OXT  sing N N 266 
MET   CB   CG   sing N N 267 
MET   CB   HB2  sing N N 268 
MET   CB   HB3  sing N N 269 
MET   CG   SD   sing N N 270 
MET   CG   HG2  sing N N 271 
MET   CG   HG3  sing N N 272 
MET   SD   CE   sing N N 273 
MET   CE   HE1  sing N N 274 
MET   CE   HE2  sing N N 275 
MET   CE   HE3  sing N N 276 
MET   OXT  HXT  sing N N 277 
PHE   N    CA   sing N N 278 
PHE   N    H    sing N N 279 
PHE   N    H2   sing N N 280 
PHE   CA   C    sing N N 281 
PHE   CA   CB   sing N N 282 
PHE   CA   HA   sing N N 283 
PHE   C    O    doub N N 284 
PHE   C    OXT  sing N N 285 
PHE   CB   CG   sing N N 286 
PHE   CB   HB2  sing N N 287 
PHE   CB   HB3  sing N N 288 
PHE   CG   CD1  doub Y N 289 
PHE   CG   CD2  sing Y N 290 
PHE   CD1  CE1  sing Y N 291 
PHE   CD1  HD1  sing N N 292 
PHE   CD2  CE2  doub Y N 293 
PHE   CD2  HD2  sing N N 294 
PHE   CE1  CZ   doub Y N 295 
PHE   CE1  HE1  sing N N 296 
PHE   CE2  CZ   sing Y N 297 
PHE   CE2  HE2  sing N N 298 
PHE   CZ   HZ   sing N N 299 
PHE   OXT  HXT  sing N N 300 
PRO   N    CA   sing N N 301 
PRO   N    CD   sing N N 302 
PRO   N    H    sing N N 303 
PRO   CA   C    sing N N 304 
PRO   CA   CB   sing N N 305 
PRO   CA   HA   sing N N 306 
PRO   C    O    doub N N 307 
PRO   C    OXT  sing N N 308 
PRO   CB   CG   sing N N 309 
PRO   CB   HB2  sing N N 310 
PRO   CB   HB3  sing N N 311 
PRO   CG   CD   sing N N 312 
PRO   CG   HG2  sing N N 313 
PRO   CG   HG3  sing N N 314 
PRO   CD   HD2  sing N N 315 
PRO   CD   HD3  sing N N 316 
PRO   OXT  HXT  sing N N 317 
SER   N    CA   sing N N 318 
SER   N    H    sing N N 319 
SER   N    H2   sing N N 320 
SER   CA   C    sing N N 321 
SER   CA   CB   sing N N 322 
SER   CA   HA   sing N N 323 
SER   C    O    doub N N 324 
SER   C    OXT  sing N N 325 
SER   CB   OG   sing N N 326 
SER   CB   HB2  sing N N 327 
SER   CB   HB3  sing N N 328 
SER   OG   HG   sing N N 329 
SER   OXT  HXT  sing N N 330 
THR   N    CA   sing N N 331 
THR   N    H    sing N N 332 
THR   N    H2   sing N N 333 
THR   CA   C    sing N N 334 
THR   CA   CB   sing N N 335 
THR   CA   HA   sing N N 336 
THR   C    O    doub N N 337 
THR   C    OXT  sing N N 338 
THR   CB   OG1  sing N N 339 
THR   CB   CG2  sing N N 340 
THR   CB   HB   sing N N 341 
THR   OG1  HG1  sing N N 342 
THR   CG2  HG21 sing N N 343 
THR   CG2  HG22 sing N N 344 
THR   CG2  HG23 sing N N 345 
THR   OXT  HXT  sing N N 346 
TRP   N    CA   sing N N 347 
TRP   N    H    sing N N 348 
TRP   N    H2   sing N N 349 
TRP   CA   C    sing N N 350 
TRP   CA   CB   sing N N 351 
TRP   CA   HA   sing N N 352 
TRP   C    O    doub N N 353 
TRP   C    OXT  sing N N 354 
TRP   CB   CG   sing N N 355 
TRP   CB   HB2  sing N N 356 
TRP   CB   HB3  sing N N 357 
TRP   CG   CD1  doub Y N 358 
TRP   CG   CD2  sing Y N 359 
TRP   CD1  NE1  sing Y N 360 
TRP   CD1  HD1  sing N N 361 
TRP   CD2  CE2  doub Y N 362 
TRP   CD2  CE3  sing Y N 363 
TRP   NE1  CE2  sing Y N 364 
TRP   NE1  HE1  sing N N 365 
TRP   CE2  CZ2  sing Y N 366 
TRP   CE3  CZ3  doub Y N 367 
TRP   CE3  HE3  sing N N 368 
TRP   CZ2  CH2  doub Y N 369 
TRP   CZ2  HZ2  sing N N 370 
TRP   CZ3  CH2  sing Y N 371 
TRP   CZ3  HZ3  sing N N 372 
TRP   CH2  HH2  sing N N 373 
TRP   OXT  HXT  sing N N 374 
TYR   N    CA   sing N N 375 
TYR   N    H    sing N N 376 
TYR   N    H2   sing N N 377 
TYR   CA   C    sing N N 378 
TYR   CA   CB   sing N N 379 
TYR   CA   HA   sing N N 380 
TYR   C    O    doub N N 381 
TYR   C    OXT  sing N N 382 
TYR   CB   CG   sing N N 383 
TYR   CB   HB2  sing N N 384 
TYR   CB   HB3  sing N N 385 
TYR   CG   CD1  doub Y N 386 
TYR   CG   CD2  sing Y N 387 
TYR   CD1  CE1  sing Y N 388 
TYR   CD1  HD1  sing N N 389 
TYR   CD2  CE2  doub Y N 390 
TYR   CD2  HD2  sing N N 391 
TYR   CE1  CZ   doub Y N 392 
TYR   CE1  HE1  sing N N 393 
TYR   CE2  CZ   sing Y N 394 
TYR   CE2  HE2  sing N N 395 
TYR   CZ   OH   sing N N 396 
TYR   OH   HH   sing N N 397 
TYR   OXT  HXT  sing N N 398 
VAL   N    CA   sing N N 399 
VAL   N    H    sing N N 400 
VAL   N    H2   sing N N 401 
VAL   CA   C    sing N N 402 
VAL   CA   CB   sing N N 403 
VAL   CA   HA   sing N N 404 
VAL   C    O    doub N N 405 
VAL   C    OXT  sing N N 406 
VAL   CB   CG1  sing N N 407 
VAL   CB   CG2  sing N N 408 
VAL   CB   HB   sing N N 409 
VAL   CG1  HG11 sing N N 410 
VAL   CG1  HG12 sing N N 411 
VAL   CG1  HG13 sing N N 412 
VAL   CG2  HG21 sing N N 413 
VAL   CG2  HG22 sing N N 414 
VAL   CG2  HG23 sing N N 415 
VAL   OXT  HXT  sing N N 416 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM49758 
_pdbx_audit_support.ordinal                1 
# 
_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   5EEM 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1' 
_space_group.name_Hall        'P 1' 
_space_group.IT_number        1 
_space_group.crystal_system   triclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MQP 
_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]   0.020761 
_atom_sites.fract_transf_matrix[1][2]   -0.002583 
_atom_sites.fract_transf_matrix[1][3]   0.000727 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018596 
_atom_sites.fract_transf_matrix[2][3]   -0.005707 
_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]   0.014069 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
K  ? ? 16.37977 2.54835 ? ? 4.54127  84.28225 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
SE ? ? 26.02326 7.89457 ? ? 1.54240  29.12501 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 8   ? -11.73900 24.65200 2.95800  1.000 27.36408 ? 442  PRO   A N    1 
ATOM   2    C  CA   . PRO   A 1 8   ? -11.66800 24.20600 4.35400  1.000 30.72182 ? 442  PRO   A CA   1 
ATOM   3    C  C    . PRO   A 1 8   ? -13.02500 23.78000 4.90300  1.000 26.49650 ? 442  PRO   A C    1 
ATOM   4    O  O    . PRO   A 1 8   ? -13.98200 24.55000 4.83300  1.000 31.36473 ? 442  PRO   A O    1 
ATOM   5    C  CB   . PRO   A 1 8   ? -11.14900 25.44400 5.09800  1.000 22.19246 ? 442  PRO   A CB   1 
ATOM   6    C  CG   . PRO   A 1 8   ? -10.51600 26.29700 4.05300  1.000 21.77774 ? 442  PRO   A CG   1 
ATOM   7    C  CD   . PRO   A 1 8   ? -11.31400 26.05200 2.80500  1.000 23.75101 ? 442  PRO   A CD   1 
ATOM   8    N  N    . ILE   A 1 9   ? -13.10400 22.56900 5.44600  1.000 19.70778 ? 443  ILE   A N    1 
ATOM   9    C  CA   . ILE   A 1 9   ? -14.34100 22.02300 5.99200  1.000 21.56392 ? 443  ILE   A CA   1 
ATOM   10   C  C    . ILE   A 1 9   ? -14.13800 21.73400 7.47200  1.000 13.89256 ? 443  ILE   A C    1 
ATOM   11   O  O    . ILE   A 1 9   ? -13.14800 21.10300 7.85700  1.000 11.82391 ? 443  ILE   A O    1 
ATOM   12   C  CB   . ILE   A 1 9   ? -14.77900 20.74500 5.25100  1.000 26.21535 ? 443  ILE   A CB   1 
ATOM   13   C  CG1  . ILE   A 1 9   ? -15.02800 21.02800 3.77000  1.000 27.47417 ? 443  ILE   A CG1  1 
ATOM   14   C  CG2  . ILE   A 1 9   ? -16.02700 20.17400 5.88400  1.000 16.60129 ? 443  ILE   A CG2  1 
ATOM   15   C  CD1  . ILE   A 1 9   ? -15.50600 19.81300 2.99900  1.000 26.87156 ? 443  ILE   A CD1  1 
ATOM   16   N  N    . THR   A 1 10  ? -15.08100 22.18700 8.29400  1.000 15.75749 ? 444  THR   A N    1 
ATOM   17   C  CA   . THR   A 1 10  ? -15.12500 21.86200 9.71400  1.000 10.33915 ? 444  THR   A CA   1 
ATOM   18   C  C    . THR   A 1 10  ? -16.12400 20.73600 9.93700  1.000 9.55367  ? 444  THR   A C    1 
ATOM   19   O  O    . THR   A 1 10  ? -17.26600 20.81100 9.47400  1.000 19.30606 ? 444  THR   A O    1 
ATOM   20   C  CB   . THR   A 1 10  ? -15.51800 23.08100 10.54800 1.000 11.73476 ? 444  THR   A CB   1 
ATOM   21   O  OG1  . THR   A 1 10  ? -14.52300 24.10300 10.40800 1.000 10.17374 ? 444  THR   A OG1  1 
ATOM   22   C  CG2  . THR   A 1 10  ? -15.65800 22.70600 12.02200 1.000 10.54023 ? 444  THR   A CG2  1 
ATOM   23   N  N    . GLY   A 1 11  ? -15.69900 19.69700 10.63200 1.000 9.81580  ? 445  GLY   A N    1 
ATOM   24   C  CA   . GLY   A 1 11  ? -16.56900 18.58900 10.94500 1.000 14.22570 ? 445  GLY   A CA   1 
ATOM   25   C  C    . GLY   A 1 11  ? -17.20200 18.72900 12.31900 1.000 15.28601 ? 445  GLY   A C    1 
ATOM   26   O  O    . GLY   A 1 11  ? -16.68400 19.40800 13.19900 1.000 10.20385 ? 445  GLY   A O    1 
ATOM   27   N  N    . LEU   A 1 12  ? -18.34500 18.07100 12.49400 1.000 9.81032  ? 446  LEU   A N    1 
ATOM   28   C  CA   . LEU   A 1 12  ? -19.05600 18.08600 13.76600 1.000 8.03751  ? 446  LEU   A CA   1 
ATOM   29   C  C    . LEU   A 1 12  ? -19.72200 16.73600 13.96600 1.000 11.37497 ? 446  LEU   A C    1 
ATOM   30   O  O    . LEU   A 1 12  ? -20.40800 16.24400 13.06600 1.000 17.10142 ? 446  LEU   A O    1 
ATOM   31   C  CB   . LEU   A 1 12  ? -20.09900 19.21400 13.80800 1.000 8.78775  ? 446  LEU   A CB   1 
ATOM   32   C  CG   . LEU   A 1 12  ? -20.94600 19.44800 15.06600 1.000 7.84185  ? 446  LEU   A CG   1 
ATOM   33   C  CD1  . LEU   A 1 12  ? -21.45200 20.87100 15.06200 1.000 8.05711  ? 446  LEU   A CD1  1 
ATOM   34   C  CD2  . LEU   A 1 12  ? -22.12200 18.49000 15.15800 1.000 7.86515  ? 446  LEU   A CD2  1 
ATOM   35   N  N    . VAL   A 1 13  ? -19.53800 16.14800 15.14500 1.000 9.94443  ? 447  VAL   A N    1 
ATOM   36   C  CA   . VAL   A 1 13  ? -20.14000 14.86200 15.46800 1.000 11.57123 ? 447  VAL   A CA   1 
ATOM   37   C  C    . VAL   A 1 13  ? -20.94300 15.01100 16.75200 1.000 16.05024 ? 447  VAL   A C    1 
ATOM   38   O  O    . VAL   A 1 13  ? -20.47300 15.61700 17.72200 1.000 11.80370 ? 447  VAL   A O    1 
ATOM   39   C  CB   . VAL   A 1 13  ? -19.08600 13.74300 15.59500 1.000 8.78408  ? 447  VAL   A CB   1 
ATOM   40   C  CG1  . VAL   A 1 13  ? -18.05900 14.07200 16.66400 1.000 13.42100 ? 447  VAL   A CG1  1 
ATOM   41   C  CG2  . VAL   A 1 13  ? -19.75900 12.40400 15.86900 1.000 11.09671 ? 447  VAL   A CG2  1 
ATOM   42   N  N    . TYR   A 1 14  ? -22.16300 14.47800 16.74000 1.000 10.29599 ? 448  TYR   A N    1 
ATOM   43   C  CA   . TYR   A 1 14  ? -23.07000 14.51400 17.87800 1.000 11.92394 ? 448  TYR   A CA   1 
ATOM   44   C  C    . TYR   A 1 14  ? -24.09700 13.40900 17.69000 1.000 13.68746 ? 448  TYR   A C    1 
ATOM   45   O  O    . TYR   A 1 14  ? -24.61300 13.22400 16.58600 1.000 19.92825 ? 448  TYR   A O    1 
ATOM   46   C  CB   . TYR   A 1 14  ? -23.76900 15.87300 17.99900 1.000 11.94966 ? 448  TYR   A CB   1 
ATOM   47   C  CG   . TYR   A 1 14  ? -24.96700 15.85800 18.92200 1.000 11.38524 ? 448  TYR   A CG   1 
ATOM   48   C  CD1  . TYR   A 1 14  ? -24.81100 15.97500 20.29700 1.000 10.07239 ? 448  TYR   A CD1  1 
ATOM   49   C  CD2  . TYR   A 1 14  ? -26.25600 15.72200 18.41700 1.000 12.73803 ? 448  TYR   A CD2  1 
ATOM   50   C  CE1  . TYR   A 1 14  ? -25.90300 15.96000 21.14500 1.000 11.06442 ? 448  TYR   A CE1  1 
ATOM   51   C  CE2  . TYR   A 1 14  ? -27.35300 15.70500 19.25500 1.000 11.76875 ? 448  TYR   A CE2  1 
ATOM   52   C  CZ   . TYR   A 1 14  ? -27.17000 15.82700 20.62000 1.000 17.34339 ? 448  TYR   A CZ   1 
ATOM   53   O  OH   . TYR   A 1 14  ? -28.25600 15.81300 21.46500 1.000 13.52958 ? 448  TYR   A OH   1 
ATOM   54   N  N    . ASP   A 1 15  ? -24.39100 12.68100 18.76500 1.000 14.28139 ? 449  ASP   A N    1 
ATOM   55   C  CA   . ASP   A 1 15  ? -25.38500 11.61400 18.71900 1.000 11.14717 ? 449  ASP   A CA   1 
ATOM   56   C  C    . ASP   A 1 15  ? -26.24300 11.68500 19.97300 1.000 13.97996 ? 449  ASP   A C    1 
ATOM   57   O  O    . ASP   A 1 15  ? -25.72800 11.57500 21.08900 1.000 26.39603 ? 449  ASP   A O    1 
ATOM   58   C  CB   . ASP   A 1 15  ? -24.72100 10.24100 18.58900 1.000 11.20989 ? 449  ASP   A CB   1 
ATOM   59   C  CG   . ASP   A 1 15  ? -25.66900 9.18600  18.06100 1.000 14.63982 ? 449  ASP   A CG   1 
ATOM   60   O  OD1  . ASP   A 1 15  ? -26.73900 8.98900  18.67000 1.000 15.14356 ? 449  ASP   A OD1  1 
ATOM   61   O  OD2  . ASP   A 1 15  ? -25.35100 8.56100  17.02700 1.000 16.03934 ? 449  ASP   A OD2  1 
ATOM   62   N  N    . GLN   A 1 16  ? -27.55100 11.86500 19.77900 1.000 11.78651 ? 450  GLN   A N    1 
ATOM   63   C  CA   . GLN   A 1 16  ? -28.48800 11.95600 20.89500 1.000 11.51780 ? 450  GLN   A CA   1 
ATOM   64   C  C    . GLN   A 1 16  ? -28.39900 10.74800 21.81900 1.000 11.75095 ? 450  GLN   A C    1 
ATOM   65   O  O    . GLN   A 1 16  ? -28.67800 10.86400 23.01700 1.000 10.87372 ? 450  GLN   A O    1 
ATOM   66   C  CB   . GLN   A 1 16  ? -29.91300 12.12000 20.34900 1.000 14.82836 ? 450  GLN   A CB   1 
ATOM   67   N  N    . ARG   A 1 17  ? -27.99800 9.58900  21.29100 1.000 9.88719  ? 451  ARG   A N    1 
ATOM   68   C  CA   . ARG   A 1 17  ? -27.90300 8.38200  22.10400 1.000 8.73356  ? 451  ARG   A CA   1 
ATOM   69   C  C    . ARG   A 1 17  ? -26.94100 8.54100  23.27400 1.000 11.92250 ? 451  ARG   A C    1 
ATOM   70   O  O    . ARG   A 1 17  ? -27.08000 7.82700  24.27200 1.000 16.56378 ? 451  ARG   A O    1 
ATOM   71   C  CB   . ARG   A 1 17  ? -27.46700 7.19700  21.24000 1.000 11.43133 ? 451  ARG   A CB   1 
ATOM   72   C  CG   . ARG   A 1 17  ? -28.50600 6.73800  20.22800 1.000 18.42331 ? 451  ARG   A CG   1 
ATOM   73   C  CD   . ARG   A 1 17  ? -27.96500 5.59800  19.38400 1.000 25.07055 ? 451  ARG   A CD   1 
ATOM   74   N  NE   . ARG   A 1 17  ? -26.93500 6.04300  18.45200 1.000 20.30960 ? 451  ARG   A NE   1 
ATOM   75   C  CZ   . ARG   A 1 17  ? -26.09000 5.23300  17.82800 1.000 18.14587 ? 451  ARG   A CZ   1 
ATOM   76   N  NH1  . ARG   A 1 17  ? -26.10000 3.92800  18.04100 1.000 25.38261 ? 451  ARG   A NH1  1 
ATOM   77   N  NH2  . ARG   A 1 17  ? -25.21400 5.74600  16.96900 1.000 14.97587 ? 451  ARG   A NH2  1 
ATOM   78   N  N    . MET   A 1 18  ? -25.96600 9.45100  23.17600 1.000 12.68049 ? 452  MET   A N    1 
ATOM   79   C  CA   . MET   A 1 18  ? -25.06800 9.68100  24.30000 1.000 15.46447 ? 452  MET   A CA   1 
ATOM   80   C  C    . MET   A 1 18  ? -25.78800 10.29000 25.49300 1.000 11.39034 ? 452  MET   A C    1 
ATOM   81   O  O    . MET   A 1 18  ? -25.24400 10.26600 26.60100 1.000 13.44076 ? 452  MET   A O    1 
ATOM   82   C  CB   . MET   A 1 18  ? -23.89200 10.56800 23.88000 1.000 9.41790  ? 452  MET   A CB   1 
ATOM   83   C  CG   . MET   A 1 18  ? -22.77100 9.79500  23.18700 1.000 10.09988 ? 452  MET   A CG   1 
ATOM   84   S  SD   . MET   A 1 18  ? -21.37300 10.81700 22.67500 1.000 13.20801 ? 452  MET   A SD   1 
ATOM   85   C  CE   . MET   A 1 18  ? -22.14200 11.80900 21.39400 1.000 10.34691 ? 452  MET   A CE   1 
ATOM   86   N  N    . MET   A 1 19  ? -27.00100 10.82000 25.29400 1.000 11.78811 ? 453  MET   A N    1 
ATOM   87   C  CA   . MET   A 1 19  ? -27.81000 11.33600 26.39200 1.000 11.26233 ? 453  MET   A CA   1 
ATOM   88   C  C    . MET   A 1 19  ? -28.34900 10.24000 27.29500 1.000 8.32249  ? 453  MET   A C    1 
ATOM   89   O  O    . MET   A 1 19  ? -28.86400 10.55600 28.37100 1.000 9.42407  ? 453  MET   A O    1 
ATOM   90   C  CB   . MET   A 1 19  ? -28.99400 12.15100 25.86200 1.000 9.24824  ? 453  MET   A CB   1 
ATOM   91   C  CG   . MET   A 1 19  ? -28.62500 13.39200 25.07100 1.000 8.06531  ? 453  MET   A CG   1 
ATOM   92   S  SD   . MET   A 1 19  ? -30.09000 14.36200 24.66600 1.000 18.79031 ? 453  MET   A SD   1 
ATOM   93   C  CE   . MET   A 1 19  ? -30.53700 14.97100 26.29000 1.000 10.68949 ? 453  MET   A CE   1 
ATOM   94   N  N    . LEU   A 1 20  ? -28.25400 8.97000  26.88900 1.000 8.58003  ? 454  LEU   A N    1 
ATOM   95   C  CA   . LEU   A 1 20  ? -28.88200 7.90500  27.66700 1.000 9.08750  ? 454  LEU   A CA   1 
ATOM   96   C  C    . LEU   A 1 20  ? -28.16600 7.67600  28.99200 1.000 9.03602  ? 454  LEU   A C    1 
ATOM   97   O  O    . LEU   A 1 20  ? -28.79800 7.26500  29.97000 1.000 9.44833  ? 454  LEU   A O    1 
ATOM   98   C  CB   . LEU   A 1 20  ? -28.93400 6.61500  26.84800 1.000 9.82521  ? 454  LEU   A CB   1 
ATOM   99   C  CG   . LEU   A 1 20  ? -29.83400 6.66600  25.60700 1.000 9.69813  ? 454  LEU   A CG   1 
ATOM   100  C  CD1  . LEU   A 1 20  ? -29.91700 5.31100  24.92900 1.000 11.97131 ? 454  LEU   A CD1  1 
ATOM   101  C  CD2  . LEU   A 1 20  ? -31.22700 7.17400  25.96300 1.000 13.22342 ? 454  LEU   A CD2  1 
ATOM   102  N  N    . HIS   A 1 21  ? -26.85900 7.92500  29.03700 1.000 8.60650  ? 455  HIS   A N    1 
ATOM   103  C  CA   . HIS   A 1 21  ? -26.10500 7.92100  30.28700 1.000 9.19339  ? 455  HIS   A CA   1 
ATOM   104  C  C    . HIS   A 1 21  ? -26.74900 8.86100  31.30200 1.000 12.51677 ? 455  HIS   A C    1 
ATOM   105  O  O    . HIS   A 1 21  ? -26.86500 10.06500 31.05800 1.000 13.38692 ? 455  HIS   A O    1 
ATOM   106  C  CB   . HIS   A 1 21  ? -24.66100 8.33800  29.99000 1.000 8.07101  ? 455  HIS   A CB   1 
ATOM   107  C  CG   . HIS   A 1 21  ? -23.79400 8.47300  31.20300 1.000 8.59936  ? 455  HIS   A CG   1 
ATOM   108  N  ND1  . HIS   A 1 21  ? -23.74200 7.52100  32.19700 1.000 8.58610  ? 455  HIS   A ND1  1 
ATOM   109  C  CD2  . HIS   A 1 21  ? -22.92700 9.44600  31.57100 1.000 7.68736  ? 455  HIS   A CD2  1 
ATOM   110  C  CE1  . HIS   A 1 21  ? -22.88300 7.90100  33.12600 1.000 8.33484  ? 455  HIS   A CE1  1 
ATOM   111  N  NE2  . HIS   A 1 21  ? -22.37800 9.06800  32.77200 1.000 7.88888  ? 455  HIS   A NE2  1 
ATOM   112  N  N    . HIS   A 1 22  ? -27.18500 8.31700  32.44000 1.000 9.31465  ? 456  HIS   A N    1 
ATOM   113  C  CA   . HIS   A 1 22  ? -27.96800 9.11800  33.37100 1.000 9.38242  ? 456  HIS   A CA   1 
ATOM   114  C  C    . HIS   A 1 22  ? -27.74700 8.65300  34.80300 1.000 10.52407 ? 456  HIS   A C    1 
ATOM   115  O  O    . HIS   A 1 22  ? -27.42000 7.49000  35.05300 1.000 17.60763 ? 456  HIS   A O    1 
ATOM   116  C  CB   . HIS   A 1 22  ? -29.46700 9.06800  33.02900 1.000 16.11288 ? 456  HIS   A CB   1 
ATOM   117  C  CG   . HIS   A 1 22  ? -30.10800 7.73700  33.28200 1.000 11.31946 ? 456  HIS   A CG   1 
ATOM   118  N  ND1  . HIS   A 1 22  ? -30.03300 6.69000  32.38800 1.000 10.68763 ? 456  HIS   A ND1  1 
ATOM   119  C  CD2  . HIS   A 1 22  ? -30.84100 7.28500  34.32700 1.000 14.07833 ? 456  HIS   A CD2  1 
ATOM   120  C  CE1  . HIS   A 1 22  ? -30.68500 5.64900  32.87400 1.000 11.63934 ? 456  HIS   A CE1  1 
ATOM   121  N  NE2  . HIS   A 1 22  ? -31.18800 5.98400  34.04800 1.000 20.82386 ? 456  HIS   A NE2  1 
ATOM   122  N  N    . ASN   A 1 23  ? -27.94800 9.58400  35.74200 1.000 10.68565 ? 457  ASN   A N    1 
ATOM   123  C  CA   . ASN   A 1 23  ? -27.85200 9.32700  37.17700 1.000 10.01795 ? 457  ASN   A CA   1 
ATOM   124  C  C    . ASN   A 1 23  ? -29.26100 9.09900  37.71500 1.000 13.16227 ? 457  ASN   A C    1 
ATOM   125  O  O    . ASN   A 1 23  ? -30.04900 10.04300 37.83100 1.000 18.26932 ? 457  ASN   A O    1 
ATOM   126  C  CB   . ASN   A 1 23  ? -27.17200 10.49900 37.88300 1.000 9.74733  ? 457  ASN   A CB   1 
ATOM   127  C  CG   . ASN   A 1 23  ? -26.89500 10.23200 39.35600 1.000 13.68638 ? 457  ASN   A CG   1 
ATOM   128  O  OD1  . ASN   A 1 23  ? -27.63900 9.52000  40.03100 1.000 11.54328 ? 457  ASN   A OD1  1 
ATOM   129  N  ND2  . ASN   A 1 23  ? -25.81600 10.81900 39.86400 1.000 13.48302 ? 457  ASN   A ND2  1 
ATOM   130  N  N    . MET   A 1 24  ? -29.57200 7.85000  38.05900 1.000 14.95924 ? 458  MET   A N    1 
ATOM   131  C  CA   . MET   A 1 24  ? -30.92700 7.49500  38.45500 1.000 15.81213 ? 458  MET   A CA   1 
ATOM   132  C  C    . MET   A 1 24  ? -31.23800 7.81900  39.91000 1.000 22.57521 ? 458  MET   A C    1 
ATOM   133  O  O    . MET   A 1 24  ? -32.41100 7.77000  40.29200 1.000 17.52247 ? 458  MET   A O    1 
ATOM   134  C  CB   . MET   A 1 24  ? -31.17700 6.00600  38.20600 1.000 22.69939 ? 458  MET   A CB   1 
ATOM   135  C  CG   . MET   A 1 24  ? -30.32000 5.09700  39.05700 1.000 23.07086 ? 458  MET   A CG   1 
ATOM   136  S  SD   . MET   A 1 24  ? -30.77600 3.36400  38.90000 1.000 38.63029 ? 458  MET   A SD   1 
ATOM   137  C  CE   . MET   A 1 24  ? -30.35800 3.06800  37.18200 1.000 29.18681 ? 458  MET   A CE   1 
ATOM   138  N  N    . TRP   A 1 25  ? -30.23300 8.13500  40.73100 1.000 17.28827 ? 459  TRP   A N    1 
ATOM   139  C  CA   . TRP   A 1 25  ? -30.46700 8.48600  42.12600 1.000 19.33848 ? 459  TRP   A CA   1 
ATOM   140  C  C    . TRP   A 1 25  ? -30.47000 9.98700  42.37100 1.000 21.84707 ? 459  TRP   A C    1 
ATOM   141  O  O    . TRP   A 1 25  ? -30.81400 10.41600 43.47700 1.000 38.34737 ? 459  TRP   A O    1 
ATOM   142  C  CB   . TRP   A 1 25  ? -29.41500 7.83000  43.02600 1.000 19.22329 ? 459  TRP   A CB   1 
ATOM   143  C  CG   . TRP   A 1 25  ? -29.33400 6.35600  42.83200 1.000 25.49222 ? 459  TRP   A CG   1 
ATOM   144  C  CD1  . TRP   A 1 25  ? -30.05300 5.40200  43.48500 1.000 26.18543 ? 459  TRP   A CD1  1 
ATOM   145  C  CD2  . TRP   A 1 25  ? -28.49200 5.66200  41.90500 1.000 27.28295 ? 459  TRP   A CD2  1 
ATOM   146  N  NE1  . TRP   A 1 25  ? -29.70800 4.15400  43.02700 1.000 24.34477 ? 459  TRP   A NE1  1 
ATOM   147  C  CE2  . TRP   A 1 25  ? -28.75200 4.28700  42.05500 1.000 26.45098 ? 459  TRP   A CE2  1 
ATOM   148  C  CE3  . TRP   A 1 25  ? -27.54400 6.06900  40.96200 1.000 24.09475 ? 459  TRP   A CE3  1 
ATOM   149  C  CZ2  . TRP   A 1 25  ? -28.10000 3.31900  41.29600 1.000 22.70268 ? 459  TRP   A CZ2  1 
ATOM   150  C  CZ3  . TRP   A 1 25  ? -26.89400 5.10500  40.21500 1.000 21.94660 ? 459  TRP   A CZ3  1 
ATOM   151  C  CH2  . TRP   A 1 25  ? -27.17500 3.74800  40.38600 1.000 21.51384 ? 459  TRP   A CH2  1 
ATOM   152  N  N    . ASP   A 1 26  ? -30.12100 10.79000 41.36700 1.000 11.64094 ? 460  ASP   A N    1 
ATOM   153  C  CA   . ASP   A 1 26  ? -30.01400 12.23900 41.54300 1.000 12.97556 ? 460  ASP   A CA   1 
ATOM   154  C  C    . ASP   A 1 26  ? -30.16300 12.86200 40.15100 1.000 13.38668 ? 460  ASP   A C    1 
ATOM   155  O  O    . ASP   A 1 26  ? -29.17200 13.09100 39.45900 1.000 12.21273 ? 460  ASP   A O    1 
ATOM   156  C  CB   . ASP   A 1 26  ? -28.69800 12.61800 42.19600 1.000 12.26087 ? 460  ASP   A CB   1 
ATOM   157  C  CG   . ASP   A 1 26  ? -28.50300 14.11900 42.31200 1.000 17.98387 ? 460  ASP   A CG   1 
ATOM   158  O  OD1  . ASP   A 1 26  ? -29.46700 14.88000 42.08500 1.000 22.75632 ? 460  ASP   A OD1  1 
ATOM   159  O  OD2  . ASP   A 1 26  ? -27.37100 14.53800 42.63400 1.000 22.25710 ? 460  ASP   A OD2  1 
ATOM   160  N  N    . SER   A 1 27  ? -31.41000 13.13700 39.76300 1.000 12.51233 ? 461  SER   A N    1 
ATOM   161  C  CA   . SER   A 1 27  ? -31.66900 13.68100 38.43300 1.000 15.39323 ? 461  SER   A CA   1 
ATOM   162  C  C    . SER   A 1 27  ? -31.02200 15.04600 38.21600 1.000 16.19427 ? 461  SER   A C    1 
ATOM   163  O  O    . SER   A 1 27  ? -30.96600 15.51200 37.07200 1.000 9.87851  ? 461  SER   A O    1 
ATOM   164  C  CB   . SER   A 1 27  ? -33.17800 13.76800 38.18900 1.000 16.00464 ? 461  SER   A CB   1 
ATOM   165  O  OG   . SER   A 1 27  ? -33.80100 14.61000 39.14000 1.000 17.07878 ? 461  SER   A OG   1 
ATOM   166  N  N    . HIS   A 1 28  ? -30.51900 15.68900 39.27100 1.000 12.65918 ? 462  HIS   A N    1 
ATOM   167  C  CA   . HIS   A 1 28  ? -29.88100 16.99200 39.15100 1.000 10.53605 ? 462  HIS   A CA   1 
ATOM   168  C  C    . HIS   A 1 28  ? -28.36200 16.92500 39.25600 1.000 15.65623 ? 462  HIS   A C    1 
ATOM   169  O  O    . HIS   A 1 28  ? -27.72300 17.96800 39.43500 1.000 11.85531 ? 462  HIS   A O    1 
ATOM   170  C  CB   . HIS   A 1 28  ? -30.43400 17.95100 40.20500 1.000 14.26379 ? 462  HIS   A CB   1 
ATOM   171  C  CG   . HIS   A 1 28  ? -31.74900 18.56400 39.83800 1.000 16.12522 ? 462  HIS   A CG   1 
ATOM   172  N  ND1  . HIS   A 1 28  ? -31.86000 19.60700 38.94300 1.000 13.43081 ? 462  HIS   A ND1  1 
ATOM   173  C  CD2  . HIS   A 1 28  ? -33.00800 18.29100 40.25600 1.000 13.28709 ? 462  HIS   A CD2  1 
ATOM   174  C  CE1  . HIS   A 1 28  ? -33.13100 19.94400 38.81900 1.000 16.43606 ? 462  HIS   A CE1  1 
ATOM   175  N  NE2  . HIS   A 1 28  ? -33.84900 19.16300 39.60700 1.000 10.75806 ? 462  HIS   A NE2  1 
ATOM   176  N  N    . HIS   A 1 29  ? -27.77100 15.73600 39.17100 1.000 10.31634 ? 463  HIS   A N    1 
ATOM   177  C  CA   . HIS   A 1 29  ? -26.32000 15.64400 39.11000 1.000 9.01192  ? 463  HIS   A CA   1 
ATOM   178  C  C    . HIS   A 1 29  ? -25.81800 16.47100 37.92800 1.000 10.77290 ? 463  HIS   A C    1 
ATOM   179  O  O    . HIS   A 1 29  ? -26.41900 16.43400 36.85000 1.000 12.10848 ? 463  HIS   A O    1 
ATOM   180  C  CB   . HIS   A 1 29  ? -25.87600 14.18600 38.96500 1.000 12.79093 ? 463  HIS   A CB   1 
ATOM   181  C  CG   . HIS   A 1 29  ? -24.39300 13.99100 39.04800 1.000 13.85374 ? 463  HIS   A CG   1 
ATOM   182  N  ND1  . HIS   A 1 29  ? -23.53200 14.38900 38.04800 1.000 11.30661 ? 463  HIS   A ND1  1 
ATOM   183  C  CD2  . HIS   A 1 29  ? -23.62000 13.43700 40.01000 1.000 9.15365  ? 463  HIS   A CD2  1 
ATOM   184  C  CE1  . HIS   A 1 29  ? -22.29200 14.09000 38.39200 1.000 11.94372 ? 463  HIS   A CE1  1 
ATOM   185  N  NE2  . HIS   A 1 29  ? -22.31800 13.51300 39.57900 1.000 10.16967 ? 463  HIS   A NE2  1 
ATOM   186  N  N    . PRO   A 1 30  ? -24.73700 17.23800 38.09400 1.000 10.45816 ? 464  PRO   A N    1 
ATOM   187  C  CA   . PRO   A 1 30  ? -24.36700 18.21700 37.05700 1.000 8.08745  ? 464  PRO   A CA   1 
ATOM   188  C  C    . PRO   A 1 30  ? -23.93300 17.61300 35.72500 1.000 9.98131  ? 464  PRO   A C    1 
ATOM   189  O  O    . PRO   A 1 30  ? -24.01200 18.31500 34.70900 1.000 12.19350 ? 464  PRO   A O    1 
ATOM   190  C  CB   . PRO   A 1 30  ? -23.22200 19.00500 37.71100 1.000 7.93717  ? 464  PRO   A CB   1 
ATOM   191  C  CG   . PRO   A 1 30  ? -22.70700 18.11600 38.78300 1.000 11.05969 ? 464  PRO   A CG   1 
ATOM   192  C  CD   . PRO   A 1 30  ? -23.89600 17.36300 39.29300 1.000 8.53288  ? 464  PRO   A CD   1 
ATOM   193  N  N    . GLU   A 1 31  ? -23.48600 16.34500 35.66100 1.000 7.55500  ? 465  GLU   A N    1 
ATOM   194  C  CA   . GLU   A 1 31  ? -23.04800 15.67700 34.38500 1.000 8.54222  ? 465  GLU   A CA   1 
ATOM   195  C  C    . GLU   A 1 31  ? -24.34400 15.25200 33.66400 1.000 11.35659 ? 465  GLU   A C    1 
ATOM   196  O  O    . GLU   A 1 31  ? -24.59900 14.05300 33.55000 1.000 12.32444 ? 465  GLU   A O    1 
ATOM   197  C  CB   . GLU   A 1 31  ? -21.99000 14.58300 34.58500 1.000 10.20334 ? 465  GLU   A CB   1 
ATOM   198  C  CG   . GLU   A 1 31  ? -21.10900 14.32500 33.36500 1.000 13.83906 ? 465  GLU   A CG   1 
ATOM   199  C  CD   . GLU   A 1 31  ? -21.83600 13.75700 32.16000 1.000 6.90032  ? 465  GLU   A CD   1 
ATOM   200  O  OE1  . GLU   A 1 31  ? -22.32700 14.55000 31.34900 1.000 6.76470  ? 465  GLU   A OE1  1 
ATOM   201  O  OE2  . GLU   A 1 31  ? -21.93100 12.53000 32.05300 1.000 7.05004  ? 465  GLU   A OE2  1 
ATOM   202  N  N    . LEU   A 1 32  ? -25.09200 16.22200 33.18400 1.000 11.63919 ? 466  LEU   A N    1 
ATOM   203  C  CA   . LEU   A 1 32  ? -26.45500 16.03500 32.70100 1.000 12.91904 ? 466  LEU   A CA   1 
ATOM   204  C  C    . LEU   A 1 32  ? -26.47100 15.62500 31.23000 1.000 17.49900 ? 466  LEU   A C    1 
ATOM   205  O  O    . LEU   A 1 32  ? -25.64200 16.09400 30.44000 1.000 8.32117  ? 466  LEU   A O    1 
ATOM   206  C  CB   . LEU   A 1 32  ? -27.26400 17.31800 32.87100 1.000 9.04163  ? 466  LEU   A CB   1 
ATOM   207  C  CG   . LEU   A 1 32  ? -27.67200 17.72800 34.28700 1.000 7.91123  ? 466  LEU   A CG   1 
ATOM   208  C  CD1  . LEU   A 1 32  ? -28.08600 19.19200 34.31400 1.000 12.27807 ? 466  LEU   A CD1  1 
ATOM   209  C  CD2  . LEU   A 1 32  ? -28.79700 16.85400 34.80100 1.000 8.32429  ? 466  LEU   A CD2  1 
ATOM   210  N  N    . PRO   A 1 33  ? -27.41300 14.75400 30.85900 1.000 12.58842 ? 467  PRO   A N    1 
ATOM   211  C  CA   . PRO   A 1 33  ? -27.64400 14.49900 29.43100 1.000 7.54362  ? 467  PRO   A CA   1 
ATOM   212  C  C    . PRO   A 1 33  ? -27.84300 15.77400 28.63300 1.000 8.97233  ? 467  PRO   A C    1 
ATOM   213  O  O    . PRO   A 1 33  ? -27.38400 15.87100 27.48900 1.000 14.59680 ? 467  PRO   A O    1 
ATOM   214  C  CB   . PRO   A 1 33  ? -28.90700 13.62800 29.44200 1.000 7.98106  ? 467  PRO   A CB   1 
ATOM   215  C  CG   . PRO   A 1 33  ? -28.86800 12.93000 30.75200 1.000 9.12901  ? 467  PRO   A CG   1 
ATOM   216  C  CD   . PRO   A 1 33  ? -28.24600 13.89900 31.72300 1.000 10.65099 ? 467  PRO   A CD   1 
ATOM   217  N  N    . GLN   A 1 34  ? -28.50400 16.77100 29.22300 1.000 7.53059  ? 468  GLN   A N    1 
ATOM   218  C  CA   . GLN   A 1 34  ? -28.80800 18.01900 28.53300 1.000 7.50850  ? 468  GLN   A CA   1 
ATOM   219  C  C    . GLN   A 1 34  ? -27.57600 18.87100 28.25700 1.000 7.20254  ? 468  GLN   A C    1 
ATOM   220  O  O    . GLN   A 1 34  ? -27.69500 19.90000 27.58100 1.000 7.22415  ? 468  GLN   A O    1 
ATOM   221  C  CB   . GLN   A 1 34  ? -29.83100 18.82300 29.33900 1.000 7.78256  ? 468  GLN   A CB   1 
ATOM   222  C  CG   . GLN   A 1 34  ? -31.25800 18.31300 29.21800 1.000 8.18295  ? 468  GLN   A CG   1 
ATOM   223  C  CD   . GLN   A 1 34  ? -31.43300 16.91600 29.76700 1.000 9.21021  ? 468  GLN   A CD   1 
ATOM   224  O  OE1  . GLN   A 1 34  ? -30.96000 16.60500 30.85700 1.000 13.92385 ? 468  GLN   A OE1  1 
ATOM   225  N  NE2  . GLN   A 1 34  ? -32.11700 16.06200 29.01200 1.000 10.34006 ? 468  GLN   A NE2  1 
ATOM   226  N  N    . ARG   A 1 35  ? -26.40100 18.47900 28.75000 1.000 10.63547 ? 469  ARG   A N    1 
ATOM   227  C  CA   . ARG   A 1 35  ? -25.18900 19.22600 28.43000 1.000 11.18558 ? 469  ARG   A CA   1 
ATOM   228  C  C    . ARG   A 1 35  ? -24.92600 19.21100 26.93000 1.000 6.68879  ? 469  ARG   A C    1 
ATOM   229  O  O    . ARG   A 1 35  ? -24.69800 20.25900 26.31900 1.000 7.35656  ? 469  ARG   A O    1 
ATOM   230  C  CB   . ARG   A 1 35  ? -24.00100 18.65400 29.20200 1.000 11.99939 ? 469  ARG   A CB   1 
ATOM   231  C  CG   . ARG   A 1 35  ? -24.12000 18.81400 30.70600 1.000 12.67141 ? 469  ARG   A CG   1 
ATOM   232  C  CD   . ARG   A 1 35  ? -22.98100 18.12000 31.44500 1.000 12.07434 ? 469  ARG   A CD   1 
ATOM   233  N  NE   . ARG   A 1 35  ? -21.68700 18.65500 31.04600 1.000 8.33421  ? 469  ARG   A NE   1 
ATOM   234  C  CZ   . ARG   A 1 35  ? -20.80800 18.01300 30.29200 1.000 6.34834  ? 469  ARG   A CZ   1 
ATOM   235  N  NH1  . ARG   A 1 35  ? -21.01700 16.76900 29.89400 1.000 8.52482  ? 469  ARG   A NH1  1 
ATOM   236  N  NH2  . ARG   A 1 35  ? -19.69600 18.63800 29.92000 1.000 6.25619  ? 469  ARG   A NH2  1 
ATOM   237  N  N    . ILE   A 1 36  ? -24.99600 18.03400 26.31100 1.000 8.92996  ? 470  ILE   A N    1 
ATOM   238  C  CA   . ILE   A 1 36  ? -24.69700 17.95100 24.88500 1.000 9.43391  ? 470  ILE   A CA   1 
ATOM   239  C  C    . ILE   A 1 36  ? -25.87100 18.41900 24.03100 1.000 12.92661 ? 470  ILE   A C    1 
ATOM   240  O  O    . ILE   A 1 36  ? -25.66100 18.98200 22.95000 1.000 13.33184 ? 470  ILE   A O    1 
ATOM   241  C  CB   . ILE   A 1 36  ? -24.26800 16.52500 24.50600 1.000 7.39842  ? 470  ILE   A CB   1 
ATOM   242  C  CG1  . ILE   A 1 36  ? -25.38800 15.52400 24.79500 1.000 6.86711  ? 470  ILE   A CG1  1 
ATOM   243  C  CG2  . ILE   A 1 36  ? -22.98800 16.14800 25.24500 1.000 6.42237  ? 470  ILE   A CG2  1 
ATOM   244  C  CD1  . ILE   A 1 36  ? -25.13300 14.14500 24.21000 1.000 8.44871  ? 470  ILE   A CD1  1 
ATOM   245  N  N    . SER   A 1 37  ? -27.11400 18.19700 24.47500 1.000 8.81378  ? 471  SER   A N    1 
ATOM   246  C  CA   . SER   A 1 37  ? -28.24900 18.63100 23.66400 1.000 12.33945 ? 471  SER   A CA   1 
ATOM   247  C  C    . SER   A 1 37  ? -28.40700 20.14400 23.69400 1.000 11.60341 ? 471  SER   A C    1 
ATOM   248  O  O    . SER   A 1 37  ? -28.86300 20.73300 22.70900 1.000 11.66277 ? 471  SER   A O    1 
ATOM   249  C  CB   . SER   A 1 37  ? -29.54000 17.94600 24.12100 1.000 7.75526  ? 471  SER   A CB   1 
ATOM   250  O  OG   . SER   A 1 37  ? -29.76600 18.12100 25.50500 1.000 10.79181 ? 471  SER   A OG   1 
ATOM   251  N  N    . ARG   A 1 38  ? -28.03000 20.79200 24.80100 1.000 12.00669 ? 472  ARG   A N    1 
ATOM   252  C  CA   . ARG   A 1 38  ? -28.04700 22.25200 24.83600 1.000 11.71386 ? 472  ARG   A CA   1 
ATOM   253  C  C    . ARG   A 1 38  ? -26.95600 22.83800 23.94700 1.000 11.39013 ? 472  ARG   A C    1 
ATOM   254  O  O    . ARG   A 1 38  ? -27.17200 23.85400 23.27900 1.000 12.29913 ? 472  ARG   A O    1 
ATOM   255  C  CB   . ARG   A 1 38  ? -27.89400 22.75800 26.27300 1.000 7.45662  ? 472  ARG   A CB   1 
ATOM   256  C  CG   . ARG   A 1 38  ? -29.17000 22.72300 27.09300 1.000 7.70652  ? 472  ARG   A CG   1 
ATOM   257  C  CD   . ARG   A 1 38  ? -30.13900 23.81000 26.66300 1.000 8.04864  ? 472  ARG   A CD   1 
ATOM   258  N  NE   . ARG   A 1 38  ? -29.61800 25.15100 26.90800 1.000 12.43159 ? 472  ARG   A NE   1 
ATOM   259  C  CZ   . ARG   A 1 38  ? -29.71800 25.80000 28.06200 1.000 13.81686 ? 472  ARG   A CZ   1 
ATOM   260  N  NH1  . ARG   A 1 38  ? -30.27200 25.24000 29.12600 1.000 8.25906  ? 472  ARG   A NH1  1 
ATOM   261  N  NH2  . ARG   A 1 38  ? -29.25300 27.04300 28.14800 1.000 13.09246 ? 472  ARG   A NH2  1 
ATOM   262  N  N    . ILE   A 1 39  ? -25.77400 22.22000 23.92700 1.000 7.14714  ? 473  ILE   A N    1 
ATOM   263  C  CA   . ILE   A 1 39  ? -24.71600 22.70100 23.04100 1.000 7.12651  ? 473  ILE   A CA   1 
ATOM   264  C  C    . ILE   A 1 39  ? -25.13500 22.53500 21.58500 1.000 8.66676  ? 473  ILE   A C    1 
ATOM   265  O  O    . ILE   A 1 39  ? -24.99100 23.45300 20.76600 1.000 7.57574  ? 473  ILE   A O    1 
ATOM   266  C  CB   . ILE   A 1 39  ? -23.39300 21.97500 23.34100 1.000 10.17158 ? 473  ILE   A CB   1 
ATOM   267  C  CG1  . ILE   A 1 39  ? -22.84100 22.42900 24.69700 1.000 7.50513  ? 473  ILE   A CG1  1 
ATOM   268  C  CG2  . ILE   A 1 39  ? -22.38200 22.22400 22.22700 1.000 6.87739  ? 473  ILE   A CG2  1 
ATOM   269  C  CD1  . ILE   A 1 39  ? -21.73000 21.56300 25.23000 1.000 11.41237 ? 473  ILE   A CD1  1 
ATOM   270  N  N    . PHE   A 1 40  ? -25.68500 21.36700 21.25000 1.000 7.34689  ? 474  PHE   A N    1 
ATOM   271  C  CA   . PHE   A 1 40  ? -26.10700 21.09900 19.87800 1.000 7.61650  ? 474  PHE   A CA   1 
ATOM   272  C  C    . PHE   A 1 40  ? -27.15300 22.10500 19.41400 1.000 9.69276  ? 474  PHE   A C    1 
ATOM   273  O  O    . PHE   A 1 40  ? -27.03500 22.68200 18.32600 1.000 12.57234 ? 474  PHE   A O    1 
ATOM   274  C  CB   . PHE   A 1 40  ? -26.64500 19.67100 19.77800 1.000 7.63293  ? 474  PHE   A CB   1 
ATOM   275  C  CG   . PHE   A 1 40  ? -26.95600 19.23400 18.37600 1.000 12.88449 ? 474  PHE   A CG   1 
ATOM   276  C  CD1  . PHE   A 1 40  ? -25.93500 18.91500 17.49500 1.000 7.91284  ? 474  PHE   A CD1  1 
ATOM   277  C  CD2  . PHE   A 1 40  ? -28.26900 19.11800 17.94600 1.000 8.33199  ? 474  PHE   A CD2  1 
ATOM   278  C  CE1  . PHE   A 1 40  ? -26.21700 18.49700 16.20600 1.000 11.60006 ? 474  PHE   A CE1  1 
ATOM   279  C  CE2  . PHE   A 1 40  ? -28.56000 18.70700 16.65500 1.000 12.69134 ? 474  PHE   A CE2  1 
ATOM   280  C  CZ   . PHE   A 1 40  ? -27.53400 18.39700 15.78300 1.000 11.20932 ? 474  PHE   A CZ   1 
ATOM   281  N  N    . SER   A 1 41  ? -28.18600 22.33000 20.23100 1.000 8.55684  ? 475  SER   A N    1 
ATOM   282  C  CA   A SER   A 1 41  ? -29.24700 23.25300 19.84200 0.141 9.93499  ? 475  SER   A CA   1 
ATOM   283  C  CA   B SER   A 1 41  ? -29.25000 23.25900 19.85600 0.859 9.96761  ? 475  SER   A CA   1 
ATOM   284  C  C    . SER   A 1 41  ? -28.69900 24.64800 19.56500 1.000 9.38450  ? 475  SER   A C    1 
ATOM   285  O  O    . SER   A 1 41  ? -29.11100 25.30100 18.60000 1.000 13.27213 ? 475  SER   A O    1 
ATOM   286  C  CB   A SER   A 1 41  ? -30.32300 23.30600 20.92600 0.141 9.13621  ? 475  SER   A CB   1 
ATOM   287  C  CB   B SER   A 1 41  ? -30.30100 23.33400 20.96300 0.859 9.48533  ? 475  SER   A CB   1 
ATOM   288  O  OG   A SER   A 1 41  ? -31.36500 24.19100 20.55800 0.141 11.38114 ? 475  SER   A OG   1 
ATOM   289  O  OG   B SER   A 1 41  ? -31.00300 22.11300 21.09700 0.859 11.66563 ? 475  SER   A OG   1 
ATOM   290  N  N    . ARG   A 1 42  ? -27.77200 25.12200 20.39800 1.000 11.48661 ? 476  ARG   A N    1 
ATOM   291  C  CA   . ARG   A 1 42  ? -27.21000 26.45000 20.18400 1.000 12.57287 ? 476  ARG   A CA   1 
ATOM   292  C  C    . ARG   A 1 42  ? -26.40100 26.50600 18.89400 1.000 11.66188 ? 476  ARG   A C    1 
ATOM   293  O  O    . ARG   A 1 42  ? -26.39800 27.53700 18.21200 1.000 12.37009 ? 476  ARG   A O    1 
ATOM   294  C  CB   . ARG   A 1 42  ? -26.35200 26.85600 21.38600 1.000 10.59616 ? 476  ARG   A CB   1 
ATOM   295  C  CG   . ARG   A 1 42  ? -25.90000 28.31300 21.38900 1.000 11.21274 ? 476  ARG   A CG   1 
ATOM   296  C  CD   . ARG   A 1 42  ? -27.07400 29.27400 21.51700 1.000 14.83057 ? 476  ARG   A CD   1 
ATOM   297  N  NE   . ARG   A 1 42  ? -26.63000 30.66400 21.51000 1.000 16.95533 ? 476  ARG   A NE   1 
ATOM   298  C  CZ   . ARG   A 1 42  ? -27.34700 31.68100 21.05200 1.000 14.23692 ? 476  ARG   A CZ   1 
ATOM   299  N  NH1  . ARG   A 1 42  ? -28.55700 31.50300 20.54500 1.000 14.73150 ? 476  ARG   A NH1  1 
ATOM   300  N  NH2  . ARG   A 1 42  ? -26.83200 32.90600 21.08900 1.000 13.72556 ? 476  ARG   A NH2  1 
ATOM   301  N  N    . HIS   A 1 43  ? -25.72000 25.41100 18.54200 1.000 11.06813 ? 477  HIS   A N    1 
ATOM   302  C  CA   . HIS   A 1 43  ? -25.07300 25.33600 17.23600 1.000 13.41658 ? 477  HIS   A CA   1 
ATOM   303  C  C    . HIS   A 1 43  ? -26.09800 25.45000 16.11300 1.000 11.46417 ? 477  HIS   A C    1 
ATOM   304  O  O    . HIS   A 1 43  ? -25.82100 26.05300 15.07000 1.000 11.50464 ? 477  HIS   A O    1 
ATOM   305  C  CB   . HIS   A 1 43  ? -24.27600 24.03400 17.10800 1.000 9.21373  ? 477  HIS   A CB   1 
ATOM   306  C  CG   . HIS   A 1 43  ? -22.89700 24.10100 17.69000 1.000 8.04424  ? 477  HIS   A CG   1 
ATOM   307  N  ND1  . HIS   A 1 43  ? -22.65900 24.08700 19.04700 1.000 9.84538  ? 477  HIS   A ND1  1 
ATOM   308  C  CD2  . HIS   A 1 43  ? -21.68100 24.17700 17.09600 1.000 8.77204  ? 477  HIS   A CD2  1 
ATOM   309  C  CE1  . HIS   A 1 43  ? -21.35700 24.15200 19.26600 1.000 12.39096 ? 477  HIS   A CE1  1 
ATOM   310  N  NE2  . HIS   A 1 43  ? -20.74100 24.20600 18.09900 1.000 7.79859  ? 477  HIS   A NE2  1 
ATOM   311  N  N    . GLU   A 1 44  ? -27.28700 24.87600 16.30800 1.000 12.44039 ? 478  GLU   A N    1 
ATOM   312  C  CA   . GLU   A 1 44  ? -28.36300 25.04200 15.33400 1.000 10.80151 ? 478  GLU   A CA   1 
ATOM   313  C  C    . GLU   A 1 44  ? -28.83300 26.49000 15.28600 1.000 10.78773 ? 478  GLU   A C    1 
ATOM   314  O  O    . GLU   A 1 44  ? -28.92100 27.09100 14.21000 1.000 14.67050 ? 478  GLU   A O    1 
ATOM   315  C  CB   . GLU   A 1 44  ? -29.53600 24.12400 15.67800 1.000 17.21552 ? 478  GLU   A CB   1 
ATOM   316  C  CG   . GLU   A 1 44  ? -29.29200 22.63700 15.52600 1.000 15.18469 ? 478  GLU   A CG   1 
ATOM   317  C  CD   . GLU   A 1 44  ? -30.47400 21.81500 16.03000 1.000 28.85706 ? 478  GLU   A CD   1 
ATOM   318  O  OE1  . GLU   A 1 44  ? -30.76700 21.86400 17.24500 1.000 17.28723 ? 478  GLU   A OE1  1 
ATOM   319  O  OE2  . GLU   A 1 44  ? -31.12400 21.13700 15.20900 1.000 33.88705 ? 478  GLU   A OE2  1 
ATOM   320  N  N    . GLU   A 1 45  ? -29.13300 27.06500 16.45200 1.000 9.99795  ? 479  GLU   A N    1 
ATOM   321  C  CA   . GLU   A 1 45  ? -29.66300 28.42200 16.52000 1.000 10.96725 ? 479  GLU   A CA   1 
ATOM   322  C  C    . GLU   A 1 45  ? -28.68800 29.44500 15.95400 1.000 21.54604 ? 479  GLU   A C    1 
ATOM   323  O  O    . GLU   A 1 45  ? -29.10900 30.49900 15.46400 1.000 25.32196 ? 479  GLU   A O    1 
ATOM   324  C  CB   . GLU   A 1 45  ? -30.00600 28.76200 17.96900 1.000 12.89321 ? 479  GLU   A CB   1 
ATOM   325  C  CG   . GLU   A 1 45  ? -31.13800 27.91900 18.52700 1.000 13.14774 ? 479  GLU   A CG   1 
ATOM   326  C  CD   . GLU   A 1 45  ? -31.12600 27.83600 20.04000 1.000 10.43119 ? 479  GLU   A CD   1 
ATOM   327  O  OE1  . GLU   A 1 45  ? -30.22000 28.42300 20.67400 1.000 9.69923  ? 479  GLU   A OE1  1 
ATOM   328  O  OE2  . GLU   A 1 45  ? -32.02600 27.16900 20.59200 1.000 14.99343 ? 479  GLU   A OE2  1 
ATOM   329  N  N    . LEU   A 1 46  ? -27.39300 29.16000 16.01300 1.000 22.66367 ? 480  LEU   A N    1 
ATOM   330  C  CA   . LEU   A 1 46  ? -26.37800 30.05900 15.49400 1.000 12.83898 ? 480  LEU   A CA   1 
ATOM   331  C  C    . LEU   A 1 46  ? -26.02200 29.75700 14.04900 1.000 16.31678 ? 480  LEU   A C    1 
ATOM   332  O  O    . LEU   A 1 46  ? -25.11100 30.38800 13.50600 1.000 24.41820 ? 480  LEU   A O    1 
ATOM   333  C  CB   . LEU   A 1 46  ? -25.12800 29.99900 16.37700 1.000 10.79784 ? 480  LEU   A CB   1 
ATOM   334  C  CG   . LEU   A 1 46  ? -25.33800 30.65100 17.74800 1.000 14.18299 ? 480  LEU   A CG   1 
ATOM   335  C  CD1  . LEU   A 1 46  ? -24.15800 30.42500 18.68300 1.000 9.63724  ? 480  LEU   A CD1  1 
ATOM   336  C  CD2  . LEU   A 1 46  ? -25.60500 32.13900 17.57100 1.000 13.26672 ? 480  LEU   A CD2  1 
ATOM   337  N  N    . ARG   A 1 47  ? -26.73400 28.81900 13.41700 1.000 17.44302 ? 481  ARG   A N    1 
ATOM   338  C  CA   . ARG   A 1 47  ? -26.47100 28.39500 12.04000 1.000 21.40648 ? 481  ARG   A CA   1 
ATOM   339  C  C    . ARG   A 1 47  ? -25.03300 27.91700 11.86300 1.000 15.16460 ? 481  ARG   A C    1 
ATOM   340  O  O    . ARG   A 1 47  ? -24.44200 28.07500 10.79500 1.000 15.28585 ? 481  ARG   A O    1 
ATOM   341  C  CB   . ARG   A 1 47  ? -26.79800 29.50700 11.03600 1.000 12.18537 ? 481  ARG   A CB   1 
ATOM   342  N  N    . LEU   A 1 48  ? -24.45500 27.33800 12.91300 1.000 15.46851 ? 482  LEU   A N    1 
ATOM   343  C  CA   . LEU   A 1 48  ? -23.12300 26.75300 12.82300 1.000 17.72235 ? 482  LEU   A CA   1 
ATOM   344  C  C    . LEU   A 1 48  ? -23.15800 25.29500 12.39100 1.000 16.76150 ? 482  LEU   A C    1 
ATOM   345  O  O    . LEU   A 1 48  ? -22.21100 24.82000 11.75100 1.000 14.63807 ? 482  LEU   A O    1 
ATOM   346  C  CB   . LEU   A 1 48  ? -22.40000 26.87400 14.16900 1.000 12.44689 ? 482  LEU   A CB   1 
ATOM   347  C  CG   . LEU   A 1 48  ? -22.14000 28.29400 14.67500 1.000 11.87861 ? 482  LEU   A CG   1 
ATOM   348  C  CD1  . LEU   A 1 48  ? -21.60800 28.26600 16.10400 1.000 9.82034  ? 482  LEU   A CD1  1 
ATOM   349  C  CD2  . LEU   A 1 48  ? -21.16900 29.02000 13.75400 1.000 15.91284 ? 482  LEU   A CD2  1 
ATOM   350  N  N    . LEU   A 1 49  ? -24.23400 24.57600 12.72400 1.000 19.47004 ? 483  LEU   A N    1 
ATOM   351  C  CA   . LEU   A 1 49  ? -24.34000 23.17500 12.33200 1.000 15.48302 ? 483  LEU   A CA   1 
ATOM   352  C  C    . LEU   A 1 49  ? -24.44400 23.03000 10.82200 1.000 14.03050 ? 483  LEU   A C    1 
ATOM   353  O  O    . LEU   A 1 49  ? -23.85100 22.11400 10.23900 1.000 20.40524 ? 483  LEU   A O    1 
ATOM   354  C  CB   . LEU   A 1 49  ? -25.54700 22.52900 13.01000 1.000 19.55925 ? 483  LEU   A CB   1 
ATOM   355  C  CG   . LEU   A 1 49  ? -25.82100 21.07500 12.61900 1.000 11.84420 ? 483  LEU   A CG   1 
ATOM   356  C  CD1  . LEU   A 1 49  ? -24.72100 20.16500 13.13900 1.000 10.82139 ? 483  LEU   A CD1  1 
ATOM   357  C  CD2  . LEU   A 1 49  ? -27.18700 20.63000 13.12600 1.000 14.25811 ? 483  LEU   A CD2  1 
ATOM   358  N  N    . SER   A 1 50  ? -25.19100 23.92100 10.16900 1.000 12.60664 ? 484  SER   A N    1 
ATOM   359  C  CA   . SER   A 1 50  ? -25.32200 23.85300 8.71900  1.000 12.39576 ? 484  SER   A CA   1 
ATOM   360  C  C    . SER   A 1 50  ? -24.02600 24.20600 8.00500  1.000 14.94696 ? 484  SER   A C    1 
ATOM   361  O  O    . SER   A 1 50  ? -23.83400 23.79100 6.85700  1.000 20.12761 ? 484  SER   A O    1 
ATOM   362  C  CB   . SER   A 1 50  ? -26.45000 24.77100 8.24800  1.000 19.30696 ? 484  SER   A CB   1 
ATOM   363  O  OG   . SER   A 1 50  ? -26.30800 26.08100 8.76800  1.000 16.05501 ? 484  SER   A OG   1 
ATOM   364  N  N    . ARG   A 1 51  ? -23.13400 24.95400 8.65500  1.000 16.06767 ? 485  ARG   A N    1 
ATOM   365  C  CA   . ARG   A 1 51  ? -21.84700 25.29300 8.06500  1.000 14.58361 ? 485  ARG   A CA   1 
ATOM   366  C  C    . ARG   A 1 51  ? -20.82900 24.16600 8.17700  1.000 13.39564 ? 485  ARG   A C    1 
ATOM   367  O  O    . ARG   A 1 51  ? -19.77200 24.24400 7.54300  1.000 17.94666 ? 485  ARG   A O    1 
ATOM   368  C  CB   . ARG   A 1 51  ? -21.28300 26.55600 8.72200  1.000 17.47770 ? 485  ARG   A CB   1 
ATOM   369  C  CG   . ARG   A 1 51  ? -22.15300 27.79500 8.55100  1.000 15.84438 ? 485  ARG   A CG   1 
ATOM   370  C  CD   . ARG   A 1 51  ? -21.56500 28.98600 9.29200  1.000 15.23761 ? 485  ARG   A CD   1 
ATOM   371  N  NE   . ARG   A 1 51  ? -20.17900 29.22600 8.90800  1.000 20.39673 ? 485  ARG   A NE   1 
ATOM   372  C  CZ   . ARG   A 1 51  ? -19.39900 30.14700 9.45600  1.000 17.27799 ? 485  ARG   A CZ   1 
ATOM   373  N  NH1  . ARG   A 1 51  ? -19.84100 30.94500 10.41300 1.000 16.09132 ? 485  ARG   A NH1  1 
ATOM   374  N  NH2  . ARG   A 1 51  ? -18.14300 30.26800 9.03400  1.000 25.24124 ? 485  ARG   A NH2  1 
ATOM   375  N  N    . CYS   A 1 52  ? -21.12000 23.12800 8.95200  1.000 16.43197 ? 486  CYS   A N    1 
ATOM   376  C  CA   . CYS   A 1 52  ? -20.18500 22.04000 9.18900  1.000 11.32735 ? 486  CYS   A CA   1 
ATOM   377  C  C    . CYS   A 1 52  ? -20.56900 20.81100 8.37600  1.000 15.74203 ? 486  CYS   A C    1 
ATOM   378  O  O    . CYS   A 1 52  ? -21.71000 20.65900 7.93400  1.000 17.18950 ? 486  CYS   A O    1 
ATOM   379  C  CB   . CYS   A 1 52  ? -20.13900 21.67500 10.67700 1.000 15.13565 ? 486  CYS   A CB   1 
ATOM   380  S  SG   . CYS   A 1 52  ? -19.57400 22.99000 11.77900 1.000 9.36176  ? 486  CYS   A SG   1 
ATOM   381  N  N    . HIS   A 1 53  ? -19.58800 19.93300 8.17700  1.000 14.13094 ? 487  HIS   A N    1 
ATOM   382  C  CA   . HIS   A 1 53  ? -19.83200 18.60100 7.64300  1.000 21.11861 ? 487  HIS   A CA   1 
ATOM   383  C  C    . HIS   A 1 53  ? -20.11500 17.65400 8.80000  1.000 18.36012 ? 487  HIS   A C    1 
ATOM   384  O  O    . HIS   A 1 53  ? -19.31400 17.55100 9.73500  1.000 10.07262 ? 487  HIS   A O    1 
ATOM   385  C  CB   . HIS   A 1 53  ? -18.63600 18.10100 6.83000  1.000 11.07855 ? 487  HIS   A CB   1 
ATOM   386  C  CG   . HIS   A 1 53  ? -18.72200 16.65500 6.45300  1.000 13.94506 ? 487  HIS   A CG   1 
ATOM   387  N  ND1  . HIS   A 1 53  ? -19.32700 16.22200 5.29300  1.000 20.16651 ? 487  HIS   A ND1  1 
ATOM   388  C  CD2  . HIS   A 1 53  ? -18.28800 15.54000 7.08900  1.000 16.82293 ? 487  HIS   A CD2  1 
ATOM   389  C  CE1  . HIS   A 1 53  ? -19.26100 14.90400 5.22900  1.000 18.24622 ? 487  HIS   A CE1  1 
ATOM   390  N  NE2  . HIS   A 1 53  ? -18.63500 14.46500 6.30600  1.000 20.77639 ? 487  HIS   A NE2  1 
ATOM   391  N  N    . ARG   A 1 54  ? -21.25300 16.96900 8.73700  1.000 15.49446 ? 488  ARG   A N    1 
ATOM   392  C  CA   . ARG   A 1 54  ? -21.68000 16.10300 9.82800  1.000 16.69439 ? 488  ARG   A CA   1 
ATOM   393  C  C    . ARG   A 1 54  ? -20.93600 14.77400 9.75600  1.000 18.26219 ? 488  ARG   A C    1 
ATOM   394  O  O    . ARG   A 1 54  ? -21.03000 14.05500 8.75600  1.000 16.97768 ? 488  ARG   A O    1 
ATOM   395  C  CB   . ARG   A 1 54  ? -23.18800 15.88600 9.76300  1.000 11.88257 ? 488  ARG   A CB   1 
ATOM   396  C  CG   . ARG   A 1 54  ? -23.76400 15.18300 10.96900 1.000 9.37889  ? 488  ARG   A CG   1 
ATOM   397  C  CD   . ARG   A 1 54  ? -23.71900 16.07100 12.21700 1.000 9.83545  ? 488  ARG   A CD   1 
ATOM   398  N  NE   . ARG   A 1 54  ? -24.36000 15.41600 13.35100 1.000 9.79827  ? 488  ARG   A NE   1 
ATOM   399  C  CZ   . ARG   A 1 54  ? -25.64500 15.53600 13.65600 1.000 8.83920  ? 488  ARG   A CZ   1 
ATOM   400  N  NH1  . ARG   A 1 54  ? -26.45100 16.32100 12.95900 1.000 9.98784  ? 488  ARG   A NH1  1 
ATOM   401  N  NH2  . ARG   A 1 54  ? -26.13600 14.85000 14.68500 1.000 14.85629 ? 488  ARG   A NH2  1 
ATOM   402  N  N    . ILE   A 1 55  ? -20.20700 14.44900 10.81300 1.000 18.92584 ? 489  ILE   A N    1 
ATOM   403  C  CA   . ILE   A 1 55  ? -19.42800 13.21600 10.89900 1.000 17.25822 ? 489  ILE   A CA   1 
ATOM   404  C  C    . ILE   A 1 55  ? -20.23400 12.19300 11.69000 1.000 15.95001 ? 489  ILE   A C    1 
ATOM   405  O  O    . ILE   A 1 55  ? -20.70300 12.51400 12.78900 1.000 14.13151 ? 489  ILE   A O    1 
ATOM   406  C  CB   . ILE   A 1 55  ? -18.05900 13.46300 11.56000 1.000 20.01865 ? 489  ILE   A CB   1 
ATOM   407  C  CG1  . ILE   A 1 55  ? -17.20700 14.38700 10.68600 1.000 14.03516 ? 489  ILE   A CG1  1 
ATOM   408  C  CG2  . ILE   A 1 55  ? -17.34100 12.14600 11.82400 1.000 16.21174 ? 489  ILE   A CG2  1 
ATOM   409  C  CD1  . ILE   A 1 55  ? -15.86400 14.73000 11.28600 1.000 8.48199  ? 489  ILE   A CD1  1 
ATOM   410  N  N    . PRO   A 1 56  ? -20.40700 10.97200 11.18900 1.000 16.69670 ? 490  PRO   A N    1 
ATOM   411  C  CA   . PRO   A 1 56  ? -21.21900 9.99100  11.91500 1.000 11.14941 ? 490  PRO   A CA   1 
ATOM   412  C  C    . PRO   A 1 56  ? -20.50400 9.46500  13.14800 1.000 15.29875 ? 490  PRO   A C    1 
ATOM   413  O  O    . PRO   A 1 56  ? -19.27700 9.35400  13.18700 1.000 27.24167 ? 490  PRO   A O    1 
ATOM   414  C  CB   . PRO   A 1 56  ? -21.43600 8.87800  10.88400 1.000 13.15683 ? 490  PRO   A CB   1 
ATOM   415  C  CG   . PRO   A 1 56  ? -20.26400 8.98700  9.97400  1.000 18.29781 ? 490  PRO   A CG   1 
ATOM   416  C  CD   . PRO   A 1 56  ? -19.91800 10.44700 9.90300  1.000 21.63927 ? 490  PRO   A CD   1 
ATOM   417  N  N    . ALA   A 1 57  ? -21.29700 9.14700  14.16300 1.000 14.94073 ? 491  ALA   A N    1 
ATOM   418  C  CA   . ALA   A 1 57  ? -20.80600 8.52800  15.38200 1.000 10.32455 ? 491  ALA   A CA   1 
ATOM   419  C  C    . ALA   A 1 57  ? -20.76800 7.01300  15.22300 1.000 11.05900 ? 491  ALA   A C    1 
ATOM   420  O  O    . ALA   A 1 57  ? -21.44300 6.43900  14.36600 1.000 14.97557 ? 491  ALA   A O    1 
ATOM   421  C  CB   . ALA   A 1 57  ? -21.69400 8.90100  16.56800 1.000 13.37564 ? 491  ALA   A CB   1 
ATOM   422  N  N    . ARG   A 1 58  ? -19.96600 6.36700  16.06600 1.000 10.58262 ? 492  ARG   A N    1 
ATOM   423  C  CA   . ARG   A 1 58  ? -19.92900 4.91100  16.09600 1.000 16.62540 ? 492  ARG   A CA   1 
ATOM   424  C  C    . ARG   A 1 58  ? -19.44400 4.46000  17.46400 1.000 10.57935 ? 492  ARG   A C    1 
ATOM   425  O  O    . ARG   A 1 58  ? -18.90100 5.24700  18.24000 1.000 14.29661 ? 492  ARG   A O    1 
ATOM   426  C  CB   . ARG   A 1 58  ? -19.03300 4.34000  14.99100 1.000 11.49303 ? 492  ARG   A CB   1 
ATOM   427  C  CG   . ARG   A 1 58  ? -17.53500 4.55100  15.19500 1.000 14.37918 ? 492  ARG   A CG   1 
ATOM   428  C  CD   . ARG   A 1 58  ? -16.73900 3.75900  14.15500 1.000 8.96540  ? 492  ARG   A CD   1 
ATOM   429  N  NE   . ARG   A 1 58  ? -15.30500 4.02600  14.20600 1.000 9.47857  ? 492  ARG   A NE   1 
ATOM   430  C  CZ   . ARG   A 1 58  ? -14.44400 3.38100  14.98100 1.000 10.40397 ? 492  ARG   A CZ   1 
ATOM   431  N  NH1  . ARG   A 1 58  ? -14.83900 2.44200  15.82500 1.000 8.80478  ? 492  ARG   A NH1  1 
ATOM   432  N  NH2  . ARG   A 1 58  ? -13.15000 3.68100  14.90100 1.000 16.38934 ? 492  ARG   A NH2  1 
ATOM   433  N  N    . LEU   A 1 59  ? -19.66200 3.17800  17.75100 1.000 9.24922  ? 493  LEU   A N    1 
ATOM   434  C  CA   . LEU   A 1 59  ? -19.14300 2.57300  18.96900 1.000 9.26473  ? 493  LEU   A CA   1 
ATOM   435  C  C    . LEU   A 1 59  ? -17.66600 2.25000  18.79200 1.000 16.28365 ? 493  LEU   A C    1 
ATOM   436  O  O    . LEU   A 1 59  ? -17.26700 1.66300  17.78100 1.000 17.47185 ? 493  LEU   A O    1 
ATOM   437  C  CB   . LEU   A 1 59  ? -19.90200 1.29000  19.31100 1.000 10.94198 ? 493  LEU   A CB   1 
ATOM   438  C  CG   . LEU   A 1 59  ? -21.39900 1.30100  19.62700 1.000 15.24558 ? 493  LEU   A CG   1 
ATOM   439  C  CD1  . LEU   A 1 59  ? -21.89800 -0.12800 19.76800 1.000 10.20202 ? 493  LEU   A CD1  1 
ATOM   440  C  CD2  . LEU   A 1 59  ? -21.68200 2.07800  20.89500 1.000 15.71253 ? 493  LEU   A CD2  1 
ATOM   441  N  N    . ALA   A 1 60  ? -16.85500 2.63200  19.77200 1.000 13.27050 ? 494  ALA   A N    1 
ATOM   442  C  CA   . ALA   A 1 60  ? -15.49500 2.12200  19.81900 1.000 13.41470 ? 494  ALA   A CA   1 
ATOM   443  C  C    . ALA   A 1 60  ? -15.52900 0.61800  20.05000 1.000 17.80949 ? 494  ALA   A C    1 
ATOM   444  O  O    . ALA   A 1 60  ? -16.43700 0.08600  20.69600 1.000 14.46784 ? 494  ALA   A O    1 
ATOM   445  C  CB   . ALA   A 1 60  ? -14.69700 2.80900  20.92600 1.000 8.02339  ? 494  ALA   A CB   1 
ATOM   446  N  N    . THR   A 1 61  ? -14.54300 -0.07300 19.49500 1.000 20.84516 ? 495  THR   A N    1 
ATOM   447  C  CA   . THR   A 1 61  ? -14.39900 -1.50200 19.72100 1.000 16.63942 ? 495  THR   A CA   1 
ATOM   448  C  C    . THR   A 1 61  ? -13.52900 -1.74500 20.94900 1.000 16.12030 ? 495  THR   A C    1 
ATOM   449  O  O    . THR   A 1 61  ? -12.74400 -0.88900 21.35900 1.000 18.79447 ? 495  THR   A O    1 
ATOM   450  C  CB   . THR   A 1 61  ? -13.77800 -2.18700 18.50400 1.000 14.93723 ? 495  THR   A CB   1 
ATOM   451  O  OG1  . THR   A 1 61  ? -12.38300 -1.87100 18.44500 1.000 10.63798 ? 495  THR   A OG1  1 
ATOM   452  C  CG2  . THR   A 1 61  ? -14.45100 -1.71500 17.21800 1.000 10.17427 ? 495  THR   A CG2  1 
ATOM   453  N  N    . GLU   A 1 62  ? -13.67900 -2.93800 21.53400 1.000 15.06251 ? 496  GLU   A N    1 
ATOM   454  C  CA   . GLU   A 1 62  ? -12.86000 -3.30100 22.68700 1.000 23.02251 ? 496  GLU   A CA   1 
ATOM   455  C  C    . GLU   A 1 62  ? -11.37800 -3.26800 22.34200 1.000 16.32128 ? 496  GLU   A C    1 
ATOM   456  O  O    . GLU   A 1 62  ? -10.54500 -2.88700 23.17200 1.000 18.53495 ? 496  GLU   A O    1 
ATOM   457  C  CB   . GLU   A 1 62  ? -13.24500 -4.68900 23.19200 1.000 18.73131 ? 496  GLU   A CB   1 
ATOM   458  C  CG   . GLU   A 1 62  ? -14.65300 -4.80000 23.71700 1.000 18.10825 ? 496  GLU   A CG   1 
ATOM   459  C  CD   . GLU   A 1 62  ? -15.00000 -6.22300 24.08000 1.000 25.51469 ? 496  GLU   A CD   1 
ATOM   460  O  OE1  . GLU   A 1 62  ? -14.15500 -7.11400 23.84600 1.000 31.32211 ? 496  GLU   A OE1  1 
ATOM   461  O  OE2  . GLU   A 1 62  ? -16.11000 -6.45300 24.59600 1.000 17.14866 ? 496  GLU   A OE2  1 
ATOM   462  N  N    . GLU   A 1 63  ? -11.03300 -3.67200 21.12100 1.000 13.49089 ? 497  GLU   A N    1 
ATOM   463  C  CA   . GLU   A 1 63  ? -9.64300  -3.63600 20.68800 1.000 17.26885 ? 497  GLU   A CA   1 
ATOM   464  C  C    . GLU   A 1 63  ? -9.12300  -2.20600 20.62800 1.000 16.88566 ? 497  GLU   A C    1 
ATOM   465  O  O    . GLU   A 1 63  ? -7.94100  -1.96200 20.89500 1.000 18.24498 ? 497  GLU   A O    1 
ATOM   466  C  CB   . GLU   A 1 63  ? -9.50300  -4.32200 19.32500 1.000 10.65100 ? 497  GLU   A CB   1 
ATOM   467  C  CG   . GLU   A 1 63  ? -9.90800  -5.80000 19.30800 1.000 18.65031 ? 497  GLU   A CG   1 
ATOM   468  C  CD   . GLU   A 1 63  ? -11.41900 -6.01100 19.33000 1.000 22.68033 ? 497  GLU   A CD   1 
ATOM   469  O  OE1  . GLU   A 1 63  ? -12.16400 -5.08300 18.94800 1.000 18.36664 ? 497  GLU   A OE1  1 
ATOM   470  O  OE2  . GLU   A 1 63  ? -11.86300 -7.10600 19.73700 1.000 28.73575 ? 497  GLU   A OE2  1 
ATOM   471  N  N    . GLU   A 1 64  ? -9.98800  -1.25100 20.28200 1.000 13.16447 ? 498  GLU   A N    1 
ATOM   472  C  CA   . GLU   A 1 64  ? -9.58400  0.15000  20.31400 1.000 9.32458  ? 498  GLU   A CA   1 
ATOM   473  C  C    . GLU   A 1 64  ? -9.49500  0.66200  21.74700 1.000 20.60291 ? 498  GLU   A C    1 
ATOM   474  O  O    . GLU   A 1 64  ? -8.62000  1.47500  22.06600 1.000 15.65585 ? 498  GLU   A O    1 
ATOM   475  C  CB   . GLU   A 1 64  ? -10.55600 0.99600  19.49200 1.000 10.47060 ? 498  GLU   A CB   1 
ATOM   476  C  CG   . GLU   A 1 64  ? -10.29800 0.95500  17.99100 1.000 8.77940  ? 498  GLU   A CG   1 
ATOM   477  C  CD   . GLU   A 1 64  ? -11.50500 1.38500  17.16900 1.000 10.64240 ? 498  GLU   A CD   1 
ATOM   478  O  OE1  . GLU   A 1 64  ? -12.60400 1.52800  17.74600 1.000 8.92791  ? 498  GLU   A OE1  1 
ATOM   479  O  OE2  . GLU   A 1 64  ? -11.35500 1.57700  15.94100 1.000 22.58678 ? 498  GLU   A OE2  1 
ATOM   480  N  N    . LEU   A 1 65  ? -10.39200 0.19900  22.62600 1.000 21.44086 ? 499  LEU   A N    1 
ATOM   481  C  CA   . LEU   A 1 65  ? -10.31200 0.58100  24.03200 1.000 14.26040 ? 499  LEU   A CA   1 
ATOM   482  C  C    . LEU   A 1 65  ? -9.03600  0.06600  24.67900 1.000 20.25043 ? 499  LEU   A C    1 
ATOM   483  O  O    . LEU   A 1 65  ? -8.47700  0.73100  25.56000 1.000 14.48468 ? 499  LEU   A O    1 
ATOM   484  C  CB   . LEU   A 1 65  ? -11.51800 0.05100  24.80700 1.000 17.48740 ? 499  LEU   A CB   1 
ATOM   485  C  CG   . LEU   A 1 65  ? -12.93200 0.55600  24.53300 1.000 15.97853 ? 499  LEU   A CG   1 
ATOM   486  C  CD1  . LEU   A 1 65  ? -13.89400 -0.22800 25.40100 1.000 13.02670 ? 499  LEU   A CD1  1 
ATOM   487  C  CD2  . LEU   A 1 65  ? -13.05300 2.04700  24.80000 1.000 14.63076 ? 499  LEU   A CD2  1 
ATOM   488  N  N    . ALA   A 1 66  ? -8.56000  -1.11000 24.26000 1.000 15.37201 ? 500  ALA   A N    1 
ATOM   489  C  CA   . ALA   A 1 66  ? -7.34400  -1.67800 24.82800 1.000 14.01396 ? 500  ALA   A CA   1 
ATOM   490  C  C    . ALA   A 1 66  ? -6.09900  -0.88600 24.46200 1.000 10.53714 ? 500  ALA   A C    1 
ATOM   491  O  O    . ALA   A 1 66  ? -5.04400  -1.12200 25.06100 1.000 12.61650 ? 500  ALA   A O    1 
ATOM   492  C  CB   . ALA   A 1 66  ? -7.17600  -3.12900 24.38100 1.000 10.75432 ? 500  ALA   A CB   1 
ATOM   493  N  N    . LEU   A 1 67  ? -6.19700  0.04300  23.50300 1.000 9.01141  ? 501  LEU   A N    1 
ATOM   494  C  CA   . LEU   A 1 67  ? -5.06400  0.90400  23.17900 1.000 11.58165 ? 501  LEU   A CA   1 
ATOM   495  C  C    . LEU   A 1 67  ? -4.56000  1.64400  24.41200 1.000 9.91388  ? 501  LEU   A C    1 
ATOM   496  O  O    . LEU   A 1 67  ? -3.35600  1.87300  24.55800 1.000 17.75914 ? 501  LEU   A O    1 
ATOM   497  C  CB   . LEU   A 1 67  ? -5.44500  1.90800  22.08900 1.000 8.53605  ? 501  LEU   A CB   1 
ATOM   498  C  CG   . LEU   A 1 67  ? -5.63300  1.43400  20.64600 1.000 8.70085  ? 501  LEU   A CG   1 
ATOM   499  C  CD1  . LEU   A 1 67  ? -5.96500  2.62400  19.75000 1.000 11.95254 ? 501  LEU   A CD1  1 
ATOM   500  C  CD2  . LEU   A 1 67  ? -4.40000  0.70800  20.13500 1.000 9.09494  ? 501  LEU   A CD2  1 
ATOM   501  N  N    . CYS   A 1 68  ? -5.46900  2.02500  25.31000 1.000 12.97080 ? 502  CYS   A N    1 
ATOM   502  C  CA   . CYS   A 1 68  ? -5.10200  2.71900  26.53600 1.000 18.66173 ? 502  CYS   A CA   1 
ATOM   503  C  C    . CYS   A 1 68  ? -5.52100  2.00400  27.81000 1.000 13.54799 ? 502  CYS   A C    1 
ATOM   504  O  O    . CYS   A 1 68  ? -4.91000  2.24400  28.85600 1.000 20.00345 ? 502  CYS   A O    1 
ATOM   505  C  CB   . CYS   A 1 68  ? -5.70900  4.13200  26.56300 1.000 9.76274  ? 502  CYS   A CB   1 
ATOM   506  S  SG   . CYS   A 1 68  ? -5.15100  5.22200  25.24500 1.000 9.03204  ? 502  CYS   A SG   1 
ATOM   507  N  N    . HIS   A 1 69  ? -6.53000  1.14200  27.76400 1.000 16.26420 ? 503  HIS   A N    1 
ATOM   508  C  CA   . HIS   A 1 69  ? -7.13300  0.61200  28.97600 1.000 19.21713 ? 503  HIS   A CA   1 
ATOM   509  C  C    . HIS   A 1 69  ? -6.89900  -0.88600 29.11000 1.000 10.53123 ? 503  HIS   A C    1 
ATOM   510  O  O    . HIS   A 1 69  ? -6.82000  -1.61600 28.11800 1.000 24.59797 ? 503  HIS   A O    1 
ATOM   511  C  CB   . HIS   A 1 69  ? -8.63100  0.92000  29.00600 1.000 15.27844 ? 503  HIS   A CB   1 
ATOM   512  C  CG   . HIS   A 1 69  ? -8.93400  2.38400  29.06300 1.000 13.83312 ? 503  HIS   A CG   1 
ATOM   513  N  ND1  . HIS   A 1 69  ? -8.86400  3.11100  30.23100 1.000 8.44373  ? 503  HIS   A ND1  1 
ATOM   514  C  CD2  . HIS   A 1 69  ? -9.28400  3.26200  28.09300 1.000 13.56066 ? 503  HIS   A CD2  1 
ATOM   515  C  CE1  . HIS   A 1 69  ? -9.16800  4.37200  29.98100 1.000 16.21229 ? 503  HIS   A CE1  1 
ATOM   516  N  NE2  . HIS   A 1 69  ? -9.42900  4.49000  28.69100 1.000 12.95247 ? 503  HIS   A NE2  1 
ATOM   517  N  N    . SER   A 1 70  ? -6.79400  -1.33400 30.35700 1.000 14.88005 ? 504  SER   A N    1 
ATOM   518  C  CA   . SER   A 1 70  ? -6.56500  -2.74000 30.64100 1.000 18.23963 ? 504  SER   A CA   1 
ATOM   519  C  C    . SER   A 1 70  ? -7.83300  -3.55000 30.40900 1.000 16.07765 ? 504  SER   A C    1 
ATOM   520  O  O    . SER   A 1 70  ? -8.95000  -3.03300 30.49300 1.000 18.12262 ? 504  SER   A O    1 
ATOM   521  C  CB   . SER   A 1 70  ? -6.09700  -2.92200 32.08600 1.000 20.23882 ? 504  SER   A CB   1 
ATOM   522  O  OG   . SER   A 1 70  ? -7.14500  -2.63500 32.99800 1.000 13.61817 ? 504  SER   A OG   1 
ATOM   523  N  N    . SER   A 1 71  ? -7.64500  -4.84000 30.11900 1.000 16.12314 ? 505  SER   A N    1 
ATOM   524  C  CA   . SER   A 1 71  ? -8.77700  -5.74400 29.94200 1.000 11.97403 ? 505  SER   A CA   1 
ATOM   525  C  C    . SER   A 1 71  ? -9.70100  -5.72700 31.15300 1.000 21.36575 ? 505  SER   A C    1 
ATOM   526  O  O    . SER   A 1 71  ? -10.92900 -5.74000 31.00700 1.000 14.32299 ? 505  SER   A O    1 
ATOM   527  C  CB   . SER   A 1 71  ? -8.27400  -7.16600 29.68200 1.000 12.69103 ? 505  SER   A CB   1 
ATOM   528  O  OG   . SER   A 1 71  ? -7.54300  -7.24000 28.47000 1.000 28.44452 ? 505  SER   A OG   1 
ATOM   529  N  N    . LYS   A 1 72  ? -9.12500  -5.69600 32.36000 1.000 14.22378 ? 506  LYS   A N    1 
ATOM   530  C  CA   . LYS   A 1 72  ? -9.93700  -5.72300 33.57300 1.000 14.06788 ? 506  LYS   A CA   1 
ATOM   531  C  C    . LYS   A 1 72  ? -10.87200 -4.52400 33.63800 1.000 15.70352 ? 506  LYS   A C    1 
ATOM   532  O  O    . LYS   A 1 72  ? -12.07000 -4.67200 33.90100 1.000 13.17885 ? 506  LYS   A O    1 
ATOM   533  C  CB   . LYS   A 1 72  ? -9.04600  -5.76500 34.81300 1.000 20.54674 ? 506  LYS   A CB   1 
ATOM   534  C  CG   . LYS   A 1 72  ? -9.81900  -5.48900 36.08700 1.000 21.74241 ? 506  LYS   A CG   1 
ATOM   535  C  CD   . LYS   A 1 72  ? -9.06400  -5.90400 37.33500 1.000 27.05436 ? 506  LYS   A CD   1 
ATOM   536  C  CE   . LYS   A 1 72  ? -10.03400 -6.06600 38.49800 1.000 28.62068 ? 506  LYS   A CE   1 
ATOM   537  N  NZ   . LYS   A 1 72  ? -9.39600  -6.60300 39.73200 1.000 41.75881 ? 506  LYS   A NZ   1 
ATOM   538  N  N    . HIS   A 1 73  ? -10.33800 -3.32400 33.40100 1.000 12.09928 ? 507  HIS   A N    1 
ATOM   539  C  CA   . HIS   A 1 73  ? -11.16100 -2.12300 33.48400 1.000 10.99979 ? 507  HIS   A CA   1 
ATOM   540  C  C    . HIS   A 1 73  ? -12.25100 -2.11000 32.42400 1.000 16.64346 ? 507  HIS   A C    1 
ATOM   541  O  O    . HIS   A 1 73  ? -13.35300 -1.60300 32.67200 1.000 16.44493 ? 507  HIS   A O    1 
ATOM   542  C  CB   . HIS   A 1 73  ? -10.29000 -0.87600 33.35000 1.000 13.98474 ? 507  HIS   A CB   1 
ATOM   543  C  CG   . HIS   A 1 73  ? -11.07300 0.38500  33.16500 1.000 19.12140 ? 507  HIS   A CG   1 
ATOM   544  N  ND1  . HIS   A 1 73  ? -11.91500 0.88600  34.13400 1.000 9.91553  ? 507  HIS   A ND1  1 
ATOM   545  C  CD2  . HIS   A 1 73  ? -11.15700 1.23700  32.11600 1.000 14.88139 ? 507  HIS   A CD2  1 
ATOM   546  C  CE1  . HIS   A 1 73  ? -12.47300 2.00100  33.69700 1.000 13.31899 ? 507  HIS   A CE1  1 
ATOM   547  N  NE2  . HIS   A 1 73  ? -12.03300 2.23400  32.47300 1.000 20.31889 ? 507  HIS   A NE2  1 
ATOM   548  N  N    . ILE   A 1 74  ? -11.96800 -2.65500 31.24100 1.000 13.58191 ? 508  ILE   A N    1 
ATOM   549  C  CA   . ILE   A 1 74  ? -12.97400 -2.66700 30.18600 1.000 12.94488 ? 508  ILE   A CA   1 
ATOM   550  C  C    . ILE   A 1 74  ? -14.12300 -3.59200 30.55900 1.000 18.04053 ? 508  ILE   A C    1 
ATOM   551  O  O    . ILE   A 1 74  ? -15.29500 -3.26200 30.34500 1.000 22.00852 ? 508  ILE   A O    1 
ATOM   552  C  CB   . ILE   A 1 74  ? -12.33000 -3.06100 28.84500 1.000 10.77317 ? 508  ILE   A CB   1 
ATOM   553  C  CG1  . ILE   A 1 74  ? -11.25300 -2.04500 28.45700 1.000 9.95742  ? 508  ILE   A CG1  1 
ATOM   554  C  CG2  . ILE   A 1 74  ? -13.38400 -3.16600 27.74700 1.000 15.28008 ? 508  ILE   A CG2  1 
ATOM   555  C  CD1  . ILE   A 1 74  ? -10.46500 -2.42600 27.21500 1.000 9.96580  ? 508  ILE   A CD1  1 
ATOM   556  N  N    . SER   A 1 75  ? -13.81100 -4.75000 31.14800 1.000 11.81996 ? 509  SER   A N    1 
ATOM   557  C  CA   . SER   A 1 75  ? -14.82100 -5.76900 31.40300 1.000 15.03454 ? 509  SER   A CA   1 
ATOM   558  C  C    . SER   A 1 75  ? -15.72000 -5.43900 32.58500 1.000 20.94267 ? 509  SER   A C    1 
ATOM   559  O  O    . SER   A 1 75  ? -16.84000 -5.95600 32.65200 1.000 22.61177 ? 509  SER   A O    1 
ATOM   560  C  CB   . SER   A 1 75  ? -14.15600 -7.12700 31.63500 1.000 14.40496 ? 509  SER   A CB   1 
ATOM   561  O  OG   . SER   A 1 75  ? -13.21500 -7.05700 32.68800 1.000 25.10826 ? 509  SER   A OG   1 
ATOM   562  N  N    . ILE   A 1 76  ? -15.26200 -4.60800 33.52000 1.000 17.62398 ? 510  ILE   A N    1 
ATOM   563  C  CA   . ILE   A 1 76  ? -16.12900 -4.23400 34.63100 1.000 16.73163 ? 510  ILE   A CA   1 
ATOM   564  C  C    . ILE   A 1 76  ? -17.10100 -3.13900 34.21300 1.000 20.10211 ? 510  ILE   A C    1 
ATOM   565  O  O    . ILE   A 1 76  ? -18.28800 -3.18500 34.55700 1.000 16.94790 ? 510  ILE   A O    1 
ATOM   566  C  CB   . ILE   A 1 76  ? -15.29900 -3.81900 35.85400 1.000 14.30728 ? 510  ILE   A CB   1 
ATOM   567  C  CG1  . ILE   A 1 76  ? -16.20800 -3.17800 36.89400 1.000 22.34037 ? 510  ILE   A CG1  1 
ATOM   568  C  CG2  . ILE   A 1 76  ? -14.19000 -2.86000 35.46300 1.000 18.91826 ? 510  ILE   A CG2  1 
ATOM   569  C  CD1  . ILE   A 1 76  ? -15.49100 -2.81300 38.12100 1.000 36.42759 ? 510  ILE   A CD1  1 
ATOM   570  N  N    . ILE   A 1 77  ? -16.61900 -2.13500 33.47600 1.000 15.94687 ? 511  ILE   A N    1 
ATOM   571  C  CA   . ILE   A 1 77  ? -17.52700 -1.15300 32.89600 1.000 13.18757 ? 511  ILE   A CA   1 
ATOM   572  C  C    . ILE   A 1 77  ? -18.46500 -1.83100 31.91000 1.000 18.80129 ? 511  ILE   A C    1 
ATOM   573  O  O    . ILE   A 1 77  ? -19.64000 -1.46100 31.79200 1.000 17.11987 ? 511  ILE   A O    1 
ATOM   574  C  CB   . ILE   A 1 77  ? -16.73000 -0.01400 32.23000 1.000 10.95094 ? 511  ILE   A CB   1 
ATOM   575  C  CG1  . ILE   A 1 77  ? -15.73100 0.59400  33.21900 1.000 11.69315 ? 511  ILE   A CG1  1 
ATOM   576  C  CG2  . ILE   A 1 77  ? -17.67500 1.05000  31.69300 1.000 13.58108 ? 511  ILE   A CG2  1 
ATOM   577  C  CD1  . ILE   A 1 77  ? -16.36800 1.12900  34.49200 1.000 13.48066 ? 511  ILE   A CD1  1 
ATOM   578  N  N    . LYS   A 1 78  ? -17.96700 -2.84400 31.19800 1.000 21.97872 ? 512  LYS   A N    1 
ATOM   579  C  CA   . LYS   A 1 78  ? -18.80600 -3.59300 30.27000 1.000 18.22157 ? 512  LYS   A CA   1 
ATOM   580  C  C    . LYS   A 1 78  ? -19.89900 -4.35100 31.01000 1.000 22.38094 ? 512  LYS   A C    1 
ATOM   581  O  O    . LYS   A 1 78  ? -21.05100 -4.38400 30.56200 1.000 15.26893 ? 512  LYS   A O    1 
ATOM   582  C  CB   . LYS   A 1 78  ? -17.93400 -4.54900 29.45900 1.000 13.92530 ? 512  LYS   A CB   1 
ATOM   583  C  CG   . LYS   A 1 78  ? -18.61200 -5.22500 28.28500 1.000 30.92500 ? 512  LYS   A CG   1 
ATOM   584  C  CD   . LYS   A 1 78  ? -17.55400 -5.83200 27.38200 1.000 21.72334 ? 512  LYS   A CD   1 
ATOM   585  C  CE   . LYS   A 1 78  ? -17.83900 -7.28900 27.06600 1.000 25.79688 ? 512  LYS   A CE   1 
ATOM   586  N  NZ   . LYS   A 1 78  ? -18.62500 -7.43200 25.81200 1.000 32.17726 ? 512  LYS   A NZ   1 
ATOM   587  N  N    . SER   A 1 79  ? -19.56100 -4.95000 32.15400 1.000 16.40204 ? 513  SER   A N    1 
ATOM   588  C  CA   . SER   A 1 79  ? -20.52300 -5.76300 32.88900 1.000 19.40104 ? 513  SER   A CA   1 
ATOM   589  C  C    . SER   A 1 79  ? -21.68300 -4.94400 33.44100 1.000 17.58565 ? 513  SER   A C    1 
ATOM   590  O  O    . SER   A 1 79  ? -22.75600 -5.50500 33.69100 1.000 16.80876 ? 513  SER   A O    1 
ATOM   591  C  CB   . SER   A 1 79  ? -19.82400 -6.50000 34.03200 1.000 19.21992 ? 513  SER   A CB   1 
ATOM   592  O  OG   . SER   A 1 79  ? -19.38800 -5.60600 35.04300 1.000 14.00353 ? 513  SER   A OG   1 
ATOM   593  N  N    . SER   A 1 80  ? -21.49800 -3.63800 33.64300 1.000 17.84846 ? 514  SER   A N    1 
ATOM   594  C  CA   . SER   A 1 80  ? -22.57600 -2.82100 34.18600 1.000 15.70188 ? 514  SER   A CA   1 
ATOM   595  C  C    . SER   A 1 80  ? -23.73800 -2.65700 33.21700 1.000 14.07037 ? 514  SER   A C    1 
ATOM   596  O  O    . SER   A 1 80  ? -24.79900 -2.18300 33.63000 1.000 13.85025 ? 514  SER   A O    1 
ATOM   597  C  CB   . SER   A 1 80  ? -22.05000 -1.44200 34.59200 1.000 14.46581 ? 514  SER   A CB   1 
ATOM   598  O  OG   . SER   A 1 80  ? -21.66800 -0.68700 33.45800 1.000 14.14371 ? 514  SER   A OG   1 
ATOM   599  N  N    . GLU   A 1 81  ? -23.56600 -3.02700 31.94600 1.000 17.25860 ? 515  GLU   A N    1 
ATOM   600  C  CA   . GLU   A 1 81  ? -24.65500 -2.90200 30.98500 1.000 18.21389 ? 515  GLU   A CA   1 
ATOM   601  C  C    . GLU   A 1 81  ? -25.84300 -3.78500 31.34500 1.000 22.16636 ? 515  GLU   A C    1 
ATOM   602  O  O    . GLU   A 1 81  ? -26.96500 -3.50900 30.90600 1.000 19.26972 ? 515  GLU   A O    1 
ATOM   603  C  CB   . GLU   A 1 81  ? -24.14600 -3.23900 29.58000 1.000 22.08504 ? 515  GLU   A CB   1 
ATOM   604  C  CG   . GLU   A 1 81  ? -25.11000 -2.88300 28.46100 1.000 23.85336 ? 515  GLU   A CG   1 
ATOM   605  C  CD   . GLU   A 1 81  ? -24.44100 -2.86600 27.09800 1.000 25.49400 ? 515  GLU   A CD   1 
ATOM   606  O  OE1  . GLU   A 1 81  ? -23.19700 -2.78800 27.04700 1.000 27.49112 ? 515  GLU   A OE1  1 
ATOM   607  O  OE2  . GLU   A 1 81  ? -25.15900 -2.93000 26.07800 1.000 47.66624 ? 515  GLU   A OE2  1 
ATOM   608  N  N    . HIS   A 1 82  ? -25.62900 -4.82500 32.15200 1.000 25.37023 ? 516  HIS   A N    1 
ATOM   609  C  CA   . HIS   A 1 82  ? -26.69000 -5.75400 32.52000 1.000 22.97748 ? 516  HIS   A CA   1 
ATOM   610  C  C    . HIS   A 1 82  ? -26.93000 -5.79500 34.02700 1.000 17.12011 ? 516  HIS   A C    1 
ATOM   611  O  O    . HIS   A 1 82  ? -27.52600 -6.75200 34.52900 1.000 22.83238 ? 516  HIS   A O    1 
ATOM   612  C  CB   . HIS   A 1 82  ? -26.36500 -7.15200 31.99100 1.000 19.10307 ? 516  HIS   A CB   1 
ATOM   613  C  CG   . HIS   A 1 82  ? -26.09800 -7.19200 30.51800 1.000 32.74097 ? 516  HIS   A CG   1 
ATOM   614  N  ND1  . HIS   A 1 82  ? -27.06700 -6.91400 29.57700 1.000 32.29385 ? 516  HIS   A ND1  1 
ATOM   615  C  CD2  . HIS   A 1 82  ? -24.97100 -7.47900 29.82300 1.000 24.69128 ? 516  HIS   A CD2  1 
ATOM   616  C  CE1  . HIS   A 1 82  ? -26.54800 -7.02500 28.36700 1.000 24.34420 ? 516  HIS   A CE1  1 
ATOM   617  N  NE2  . HIS   A 1 82  ? -25.27800 -7.36900 28.48800 1.000 30.70057 ? 516  HIS   A NE2  1 
ATOM   618  N  N    . MET   A 1 83  ? -26.50100 -4.77100 34.75800 1.000 21.31833 ? 517  MET   A N    1 
ATOM   619  C  CA   . MET   A 1 83  ? -26.57000 -4.79800 36.21300 1.000 22.16710 ? 517  MET   A CA   1 
ATOM   620  C  C    . MET   A 1 83  ? -27.92400 -4.32400 36.74100 1.000 18.60895 ? 517  MET   A C    1 
ATOM   621  O  O    . MET   A 1 83  ? -28.61600 -3.51400 36.11800 1.000 17.59328 ? 517  MET   A O    1 
ATOM   622  C  CB   . MET   A 1 83  ? -25.46000 -3.93400 36.81400 1.000 15.01826 ? 517  MET   A CB   1 
ATOM   623  C  CG   . MET   A 1 83  ? -24.13700 -4.65400 36.99600 1.000 15.13621 ? 517  MET   A CG   1 
ATOM   624  S  SD   . MET   A 1 83  ? -22.87700 -3.61200 37.75600 1.000 17.35073 ? 517  MET   A SD   1 
ATOM   625  C  CE   . MET   A 1 83  ? -21.52900 -4.78600 37.89900 1.000 22.10369 ? 517  MET   A CE   1 
ATOM   626  N  N    . LYS   A 1 84  ? -28.29000 -4.85100 37.91000 1.000 22.37518 ? 518  LYS   A N    1 
ATOM   627  C  CA   . LYS   A 1 84  ? -29.42900 -4.36100 38.67400 1.000 20.74306 ? 518  LYS   A CA   1 
ATOM   628  C  C    . LYS   A 1 84  ? -29.08300 -3.00200 39.28800 1.000 20.06461 ? 518  LYS   A C    1 
ATOM   629  O  O    . LYS   A 1 84  ? -27.91000 -2.70600 39.52000 1.000 23.21773 ? 518  LYS   A O    1 
ATOM   630  C  CB   . LYS   A 1 84  ? -29.78200 -5.37700 39.76500 1.000 18.47352 ? 518  LYS   A CB   1 
ATOM   631  N  N    . PRO   A 1 85  ? -30.08000 -2.14100 39.53100 1.000 27.61623 ? 519  PRO   A N    1 
ATOM   632  C  CA   . PRO   A 1 85  ? -29.77500 -0.82800 40.13200 1.000 29.38299 ? 519  PRO   A CA   1 
ATOM   633  C  C    . PRO   A 1 85  ? -28.95600 -0.88500 41.41700 1.000 22.83905 ? 519  PRO   A C    1 
ATOM   634  O  O    . PRO   A 1 85  ? -28.04200 -0.06900 41.58000 1.000 18.84068 ? 519  PRO   A O    1 
ATOM   635  C  CB   . PRO   A 1 85  ? -31.17000 -0.22300 40.36800 1.000 19.87406 ? 519  PRO   A CB   1 
ATOM   636  C  CG   . PRO   A 1 85  ? -32.16200 -1.31500 40.03000 1.000 26.81103 ? 519  PRO   A CG   1 
ATOM   637  C  CD   . PRO   A 1 85  ? -31.47100 -2.19500 39.05800 1.000 20.49180 ? 519  PRO   A CD   1 
ATOM   638  N  N    . ARG   A 1 86  ? -29.25600 -1.81000 42.33500 1.000 17.13478 ? 520  ARG   A N    1 
ATOM   639  C  CA   . ARG   A 1 86  ? -28.44200 -1.94200 43.54100 1.000 17.49430 ? 520  ARG   A CA   1 
ATOM   640  C  C    . ARG   A 1 86  ? -26.97900 -2.17700 43.19200 1.000 16.99846 ? 520  ARG   A C    1 
ATOM   641  O  O    . ARG   A 1 86  ? -26.08500 -1.56400 43.78600 1.000 21.74132 ? 520  ARG   A O    1 
ATOM   642  C  CB   . ARG   A 1 86  ? -28.96500 -3.07900 44.42200 1.000 18.79393 ? 520  ARG   A CB   1 
ATOM   643  N  N    . ASP   A 1 87  ? -26.71300 -3.05500 42.22200 1.000 20.13235 ? 521  ASP   A N    1 
ATOM   644  C  CA   . ASP   A 1 87  ? -25.33300 -3.30700 41.82000 1.000 19.54204 ? 521  ASP   A CA   1 
ATOM   645  C  C    . ASP   A 1 87  ? -24.72900 -2.11000 41.09900 1.000 17.37027 ? 521  ASP   A C    1 
ATOM   646  O  O    . ASP   A 1 87  ? -23.52300 -1.86500 41.21500 1.000 15.83950 ? 521  ASP   A O    1 
ATOM   647  C  CB   . ASP   A 1 87  ? -25.25300 -4.55700 40.93900 1.000 16.90264 ? 521  ASP   A CB   1 
ATOM   648  C  CG   . ASP   A 1 87  ? -25.35900 -5.84200 41.73700 1.000 21.30693 ? 521  ASP   A CG   1 
ATOM   649  O  OD1  . ASP   A 1 87  ? -25.02100 -5.82800 42.93800 1.000 30.27521 ? 521  ASP   A OD1  1 
ATOM   650  O  OD2  . ASP   A 1 87  ? -25.77400 -6.87000 41.16300 1.000 41.56731 ? 521  ASP   A OD2  1 
ATOM   651  N  N    . LEU   A 1 88  ? -25.54100 -1.35700 40.35400 1.000 15.54857 ? 522  LEU   A N    1 
ATOM   652  C  CA   . LEU   A 1 88  ? -25.03800 -0.15000 39.70600 1.000 16.02934 ? 522  LEU   A CA   1 
ATOM   653  C  C    . LEU   A 1 88  ? -24.66700 0.91100  40.73300 1.000 15.92066 ? 522  LEU   A C    1 
ATOM   654  O  O    . LEU   A 1 88  ? -23.67700 1.63100  40.56100 1.000 12.99960 ? 522  LEU   A O    1 
ATOM   655  C  CB   . LEU   A 1 88  ? -26.07800 0.39800  38.72900 1.000 21.24210 ? 522  LEU   A CB   1 
ATOM   656  C  CG   . LEU   A 1 88  ? -26.27700 -0.37100 37.42300 1.000 17.13513 ? 522  LEU   A CG   1 
ATOM   657  C  CD1  . LEU   A 1 88  ? -27.54000 0.09900  36.71800 1.000 19.30235 ? 522  LEU   A CD1  1 
ATOM   658  C  CD2  . LEU   A 1 88  ? -25.06700 -0.20100 36.52000 1.000 13.35294 ? 522  LEU   A CD2  1 
ATOM   659  N  N    . ASN   A 1 89  ? -25.45700 1.02900  41.80200 1.000 19.64968 ? 523  ASN   A N    1 
ATOM   660  C  CA   . ASN   A 1 89  ? -25.13300 1.98400  42.85400 1.000 24.11248 ? 523  ASN   A CA   1 
ATOM   661  C  C    . ASN   A 1 89  ? -23.86400 1.57000  43.58500 1.000 23.43865 ? 523  ASN   A C    1 
ATOM   662  O  O    . ASN   A 1 89  ? -22.95500 2.38400  43.78300 1.000 17.83387 ? 523  ASN   A O    1 
ATOM   663  C  CB   . ASN   A 1 89  ? -26.29900 2.10800  43.83200 1.000 16.88216 ? 523  ASN   A CB   1 
ATOM   664  C  CG   . ASN   A 1 89  ? -26.16400 3.30500  44.74400 1.000 23.47880 ? 523  ASN   A CG   1 
ATOM   665  O  OD1  . ASN   A 1 89  ? -26.12600 3.16900  45.96500 1.000 40.89975 ? 523  ASN   A OD1  1 
ATOM   666  N  ND2  . ASN   A 1 89  ? -26.07700 4.49100  44.15300 1.000 43.33169 ? 523  ASN   A ND2  1 
ATOM   667  N  N    . ARG   A 1 90  ? -23.78700 0.29900  43.98500 1.000 22.84017 ? 524  ARG   A N    1 
ATOM   668  C  CA   . ARG   A 1 90  ? -22.60200 -0.19900 44.67500 1.000 17.76280 ? 524  ARG   A CA   1 
ATOM   669  C  C    . ARG   A 1 90  ? -21.35200 -0.01600 43.82400 1.000 17.85539 ? 524  ARG   A C    1 
ATOM   670  O  O    . ARG   A 1 90  ? -20.32900 0.48600  44.30300 1.000 22.77041 ? 524  ARG   A O    1 
ATOM   671  C  CB   . ARG   A 1 90  ? -22.79600 -1.67000 45.04200 1.000 25.52595 ? 524  ARG   A CB   1 
ATOM   672  N  N    . LEU   A 1 91  ? -21.42000 -0.40900 42.55000 1.000 14.38496 ? 525  LEU   A N    1 
ATOM   673  C  CA   . LEU   A 1 91  ? -20.25900 -0.28900 41.67500 1.000 13.73239 ? 525  LEU   A CA   1 
ATOM   674  C  C    . LEU   A 1 91  ? -19.83600 1.16700  41.51100 1.000 15.50689 ? 525  LEU   A C    1 
ATOM   675  O  O    . LEU   A 1 91  ? -18.64100 1.48400  41.56700 1.000 17.51868 ? 525  LEU   A O    1 
ATOM   676  C  CB   . LEU   A 1 91  ? -20.56200 -0.92300 40.31600 1.000 13.51784 ? 525  LEU   A CB   1 
ATOM   677  C  CG   . LEU   A 1 91  ? -19.51900 -0.71800 39.21600 1.000 17.27432 ? 525  LEU   A CG   1 
ATOM   678  C  CD1  . LEU   A 1 91  ? -18.15100 -1.17800 39.68400 1.000 14.99356 ? 525  LEU   A CD1  1 
ATOM   679  C  CD2  . LEU   A 1 91  ? -19.92200 -1.42900 37.93300 1.000 12.75305 ? 525  LEU   A CD2  1 
ATOM   680  N  N    . GLY   A 1 92  ? -20.80000 2.06500  41.30900 1.000 13.26438 ? 526  GLY   A N    1 
ATOM   681  C  CA   . GLY   A 1 92  ? -20.46700 3.47100  41.15700 1.000 14.07986 ? 526  GLY   A CA   1 
ATOM   682  C  C    . GLY   A 1 92  ? -19.82500 4.06600  42.39400 1.000 18.13367 ? 526  GLY   A C    1 
ATOM   683  O  O    . GLY   A 1 92  ? -18.95200 4.93300  42.28900 1.000 13.74448 ? 526  GLY   A O    1 
ATOM   684  N  N    . ASP   A 1 93  ? -20.23800 3.60800  43.57900 1.000 12.87350 ? 527  ASP   A N    1 
ATOM   685  C  CA   . ASP   A 1 93  ? -19.66400 4.12200  44.81800 1.000 18.49123 ? 527  ASP   A CA   1 
ATOM   686  C  C    . ASP   A 1 93  ? -18.23900 3.63600  45.04200 1.000 24.73707 ? 527  ASP   A C    1 
ATOM   687  O  O    . ASP   A 1 93  ? -17.53200 4.20400  45.88200 1.000 20.87184 ? 527  ASP   A O    1 
ATOM   688  C  CB   . ASP   A 1 93  ? -20.53900 3.72700  46.00800 1.000 19.88840 ? 527  ASP   A CB   1 
ATOM   689  C  CG   . ASP   A 1 93  ? -21.89300 4.41800  45.99100 1.000 34.33119 ? 527  ASP   A CG   1 
ATOM   690  O  OD1  . ASP   A 1 93  ? -22.11700 5.27700  45.10900 1.000 32.88999 ? 527  ASP   A OD1  1 
ATOM   691  O  OD2  . ASP   A 1 93  ? -22.73300 4.10000  46.86200 1.000 53.17299 ? 527  ASP   A OD2  1 
ATOM   692  N  N    . GLU   A 1 94  ? -17.80400 2.60300  44.31600 1.000 17.63384 ? 528  GLU   A N    1 
ATOM   693  C  CA   . GLU   A 1 94  ? -16.44000 2.10900  44.46100 1.000 22.66851 ? 528  GLU   A CA   1 
ATOM   694  C  C    . GLU   A 1 94  ? -15.41500 3.04800  43.83900 1.000 18.14405 ? 528  GLU   A C    1 
ATOM   695  O  O    . GLU   A 1 94  ? -14.22900 2.95900  44.17600 1.000 12.98245 ? 528  GLU   A O    1 
ATOM   696  C  CB   . GLU   A 1 94  ? -16.32100 0.71400  43.84400 1.000 15.10881 ? 528  GLU   A CB   1 
ATOM   697  C  CG   . GLU   A 1 94  ? -17.21600 -0.32700 44.50000 1.000 15.70387 ? 528  GLU   A CG   1 
ATOM   698  C  CD   . GLU   A 1 94  ? -17.09000 -1.69500 43.86500 1.000 20.46380 ? 528  GLU   A CD   1 
ATOM   699  O  OE1  . GLU   A 1 94  ? -16.38800 -1.81700 42.84200 1.000 14.55594 ? 528  GLU   A OE1  1 
ATOM   700  O  OE2  . GLU   A 1 94  ? -17.69400 -2.65200 44.39100 1.000 33.84534 ? 528  GLU   A OE2  1 
ATOM   701  N  N    . TYR   A 1 95  ? -15.84200 3.94100  42.95100 1.000 16.50330 ? 529  TYR   A N    1 
ATOM   702  C  CA   . TYR   A 1 95  ? -14.95700 4.89900  42.30700 1.000 13.51613 ? 529  TYR   A CA   1 
ATOM   703  C  C    . TYR   A 1 95  ? -15.08100 6.26800  42.96300 1.000 18.06152 ? 529  TYR   A C    1 
ATOM   704  O  O    . TYR   A 1 95  ? -15.97400 6.52900  43.77100 1.000 14.79551 ? 529  TYR   A O    1 
ATOM   705  C  CB   . TYR   A 1 95  ? -15.27300 5.02800  40.81300 1.000 16.20570 ? 529  TYR   A CB   1 
ATOM   706  C  CG   . TYR   A 1 95  ? -15.17800 3.75500  40.00500 1.000 12.74913 ? 529  TYR   A CG   1 
ATOM   707  C  CD1  . TYR   A 1 95  ? -16.26500 2.90500  39.88700 1.000 16.74180 ? 529  TYR   A CD1  1 
ATOM   708  C  CD2  . TYR   A 1 95  ? -14.01100 3.42100  39.33300 1.000 18.19789 ? 529  TYR   A CD2  1 
ATOM   709  C  CE1  . TYR   A 1 95  ? -16.18800 1.75300  39.14100 1.000 17.71062 ? 529  TYR   A CE1  1 
ATOM   710  C  CE2  . TYR   A 1 95  ? -13.92500 2.27300  38.57800 1.000 22.39674 ? 529  TYR   A CE2  1 
ATOM   711  C  CZ   . TYR   A 1 95  ? -15.01600 1.44000  38.49100 1.000 21.05657 ? 529  TYR   A CZ   1 
ATOM   712  O  OH   . TYR   A 1 95  ? -14.94200 0.29100  37.74500 1.000 21.94834 ? 529  TYR   A OH   1 
ATOM   713  N  N    . ASN   A 1 96  ? -14.17200 7.15800  42.57500 1.000 18.41618 ? 530  ASN   A N    1 
ATOM   714  C  CA   . ASN   A 1 96  ? -14.20400 8.55000  43.00200 1.000 23.94803 ? 530  ASN   A CA   1 
ATOM   715  C  C    . ASN   A 1 96  ? -15.07000 9.33300  42.02000 1.000 14.83633 ? 530  ASN   A C    1 
ATOM   716  O  O    . ASN   A 1 96  ? -14.68700 9.52500  40.86100 1.000 13.38480 ? 530  ASN   A O    1 
ATOM   717  C  CB   . ASN   A 1 96  ? -12.78600 9.11500  43.07400 1.000 27.68221 ? 530  ASN   A CB   1 
ATOM   718  C  CG   . ASN   A 1 96  ? -12.71600 10.43600 43.81800 1.000 34.19434 ? 530  ASN   A CG   1 
ATOM   719  O  OD1  . ASN   A 1 96  ? -13.73200 10.95700 44.28700 1.000 48.18072 ? 530  ASN   A OD1  1 
ATOM   720  N  ND2  . ASN   A 1 96  ? -11.50900 10.97900 43.94200 1.000 25.63410 ? 530  ASN   A ND2  1 
ATOM   721  N  N    . SER   A 1 97  ? -16.24900 9.75700  42.48000 1.000 19.22718 ? 531  SER   A N    1 
ATOM   722  C  CA   . SER   A 1 97  ? -17.14600 10.64000 41.73100 1.000 12.19692 ? 531  SER   A CA   1 
ATOM   723  C  C    . SER   A 1 97  ? -17.61000 9.99700  40.41900 1.000 15.61464 ? 531  SER   A C    1 
ATOM   724  O  O    . SER   A 1 97  ? -17.34500 10.49600 39.32500 1.000 10.21013 ? 531  SER   A O    1 
ATOM   725  C  CB   . SER   A 1 97  ? -16.48100 11.99700 41.47300 1.000 9.67081  ? 531  SER   A CB   1 
ATOM   726  O  OG   . SER   A 1 97  ? -16.05200 12.59600 42.68400 1.000 14.42470 ? 531  SER   A OG   1 
ATOM   727  N  N    . ILE   A 1 98  ? -18.32900 8.88300  40.54800 1.000 14.26737 ? 532  ILE   A N    1 
ATOM   728  C  CA   . ILE   A 1 98  ? -18.86900 8.16200  39.39900 1.000 14.49585 ? 532  ILE   A CA   1 
ATOM   729  C  C    . ILE   A 1 98  ? -20.30100 7.73400  39.70400 1.000 16.29217 ? 532  ILE   A C    1 
ATOM   730  O  O    . ILE   A 1 98  ? -20.59800 7.27000  40.80900 1.000 14.48004 ? 532  ILE   A O    1 
ATOM   731  C  CB   . ILE   A 1 98  ? -18.00100 6.93400  39.03400 1.000 10.84439 ? 532  ILE   A CB   1 
ATOM   732  C  CG1  . ILE   A 1 98  ? -16.70800 7.36600  38.33800 1.000 11.33465 ? 532  ILE   A CG1  1 
ATOM   733  C  CG2  . ILE   A 1 98  ? -18.76600 5.96800  38.14000 1.000 9.67059  ? 532  ILE   A CG2  1 
ATOM   734  C  CD1  . ILE   A 1 98  ? -16.91000 7.85200  36.91900 1.000 10.58491 ? 532  ILE   A CD1  1 
ATOM   735  N  N    . PHE   A 1 99  ? -21.18900 7.91500  38.72600 1.000 11.98417 ? 533  PHE   A N    1 
ATOM   736  C  CA   . PHE   A 1 99  ? -22.50600 7.29400  38.70500 1.000 12.93337 ? 533  PHE   A CA   1 
ATOM   737  C  C    . PHE   A 1 99  ? -22.62500 6.45100  37.44100 1.000 14.03263 ? 533  PHE   A C    1 
ATOM   738  O  O    . PHE   A 1 99  ? -22.06500 6.79300  36.39400 1.000 15.35526 ? 533  PHE   A O    1 
ATOM   739  C  CB   . PHE   A 1 99  ? -23.63600 8.34300  38.76000 1.000 9.84912  ? 533  PHE   A CB   1 
ATOM   740  C  CG   . PHE   A 1 99  ? -23.71400 9.22700  37.54400 1.000 9.23982  ? 533  PHE   A CG   1 
ATOM   741  C  CD1  . PHE   A 1 99  ? -24.41500 8.82800  36.41500 1.000 9.73526  ? 533  PHE   A CD1  1 
ATOM   742  C  CD2  . PHE   A 1 99  ? -23.10500 10.46600 37.53400 1.000 9.54457  ? 533  PHE   A CD2  1 
ATOM   743  C  CE1  . PHE   A 1 99  ? -24.48900 9.64400  35.29700 1.000 12.88227 ? 533  PHE   A CE1  1 
ATOM   744  C  CE2  . PHE   A 1 99  ? -23.17700 11.28400 36.42000 1.000 8.94785  ? 533  PHE   A CE2  1 
ATOM   745  C  CZ   . PHE   A 1 99  ? -23.86700 10.86900 35.29900 1.000 9.12593  ? 533  PHE   A CZ   1 
ATOM   746  N  N    . ILE   A 1 100 ? -23.34600 5.33600  37.53800 1.000 10.38419 ? 534  ILE   A N    1 
ATOM   747  C  CA   . ILE   A 1 100 ? -23.43700 4.37500  36.44600 1.000 10.38307 ? 534  ILE   A CA   1 
ATOM   748  C  C    . ILE   A 1 100 ? -24.89200 3.99100  36.22100 1.000 10.78431 ? 534  ILE   A C    1 
ATOM   749  O  O    . ILE   A 1 100 ? -25.63400 3.74300  37.17700 1.000 12.74392 ? 534  ILE   A O    1 
ATOM   750  C  CB   . ILE   A 1 100 ? -22.59900 3.11200  36.73200 1.000 11.10887 ? 534  ILE   A CB   1 
ATOM   751  C  CG1  . ILE   A 1 100 ? -21.28400 3.48600  37.41500 1.000 11.82178 ? 534  ILE   A CG1  1 
ATOM   752  C  CG2  . ILE   A 1 100 ? -22.33100 2.35500  35.44400 1.000 10.67012 ? 534  ILE   A CG2  1 
ATOM   753  C  CD1  . ILE   A 1 100 ? -20.34700 2.31700  37.62100 1.000 13.65170 ? 534  ILE   A CD1  1 
ATOM   754  N  N    . SER   A 1 101 ? -25.28800 3.92500  34.95400 1.000 10.56361 ? 535  SER   A N    1 
ATOM   755  C  CA   . SER   A 1 101 ? -26.56400 3.36700  34.52800 1.000 12.76320 ? 535  SER   A CA   1 
ATOM   756  C  C    . SER   A 1 101 ? -26.31000 2.27200  33.49700 1.000 11.16336 ? 535  SER   A C    1 
ATOM   757  O  O    . SER   A 1 101 ? -25.18200 2.06200  33.04100 1.000 11.11373 ? 535  SER   A O    1 
ATOM   758  C  CB   . SER   A 1 101 ? -27.48100 4.45300  33.94700 1.000 12.51819 ? 535  SER   A CB   1 
ATOM   759  O  OG   . SER   A 1 101 ? -27.03100 4.88200  32.67100 1.000 12.63550 ? 535  SER   A OG   1 
ATOM   760  N  N    . ASN   A 1 102 ? -27.38200 1.57400  33.12000 1.000 16.63566 ? 536  ASN   A N    1 
ATOM   761  C  CA   . ASN   A 1 102 ? -27.25100 0.45400  32.19400 1.000 12.83963 ? 536  ASN   A CA   1 
ATOM   762  C  C    . ASN   A 1 102 ? -26.76700 0.88500  30.81700 1.000 15.99765 ? 536  ASN   A C    1 
ATOM   763  O  O    . ASN   A 1 102 ? -26.21700 0.05900  30.08300 1.000 15.94096 ? 536  ASN   A O    1 
ATOM   764  C  CB   . ASN   A 1 102 ? -28.58300 -0.28400 32.06600 1.000 12.77073 ? 536  ASN   A CB   1 
ATOM   765  C  CG   . ASN   A 1 102 ? -28.76500 -1.34300 33.13600 1.000 17.42990 ? 536  ASN   A CG   1 
ATOM   766  O  OD1  . ASN   A 1 102 ? -27.79100 -1.89400 33.65400 1.000 18.21047 ? 536  ASN   A OD1  1 
ATOM   767  N  ND2  . ASN   A 1 102 ? -30.01500 -1.63700 33.47100 1.000 21.60272 ? 536  ASN   A ND2  1 
ATOM   768  N  N    . GLU   A 1 103 ? -26.94900 2.15000  30.45300 1.000 14.79730 ? 537  GLU   A N    1 
ATOM   769  C  CA   . GLU   A 1 103 ? -26.53400 2.66000  29.15500 1.000 11.15812 ? 537  GLU   A CA   1 
ATOM   770  C  C    . GLU   A 1 103 ? -25.15300 3.31000  29.18100 1.000 11.99105 ? 537  GLU   A C    1 
ATOM   771  O  O    . GLU   A 1 103 ? -24.65500 3.70600  28.12100 1.000 9.31803  ? 537  GLU   A O    1 
ATOM   772  C  CB   . GLU   A 1 103 ? -27.56200 3.67400  28.63700 1.000 10.17757 ? 537  GLU   A CB   1 
ATOM   773  C  CG   . GLU   A 1 103 ? -29.01300 3.20800  28.71100 1.000 14.65343 ? 537  GLU   A CG   1 
ATOM   774  C  CD   . GLU   A 1 103 ? -29.66900 3.51400  30.05400 1.000 17.59459 ? 537  GLU   A CD   1 
ATOM   775  O  OE1  . GLU   A 1 103 ? -28.99500 4.08500  30.93500 1.000 13.46007 ? 537  GLU   A OE1  1 
ATOM   776  O  OE2  . GLU   A 1 103 ? -30.86100 3.18300  30.23100 1.000 22.20014 ? 537  GLU   A OE2  1 
ATOM   777  N  N    . SER   A 1 104 ? -24.53000 3.41700  30.36000 1.000 10.81298 ? 538  SER   A N    1 
ATOM   778  C  CA   . SER   A 1 104 ? -23.28600 4.17000  30.49900 1.000 9.11920  ? 538  SER   A CA   1 
ATOM   779  C  C    . SER   A 1 104 ? -22.20500 3.64400  29.56700 1.000 8.95915  ? 538  SER   A C    1 
ATOM   780  O  O    . SER   A 1 104 ? -21.58600 4.41400  28.82300 1.000 8.49018  ? 538  SER   A O    1 
ATOM   781  C  CB   . SER   A 1 104 ? -22.80400 4.12400  31.95000 1.000 9.27716  ? 538  SER   A CB   1 
ATOM   782  O  OG   . SER   A 1 104 ? -23.70300 4.81200  32.79800 1.000 10.06181 ? 538  SER   A OG   1 
ATOM   783  N  N    . TYR   A 1 105 ? -21.96600 2.32900  29.59800 1.000 12.90617 ? 539  TYR   A N    1 
ATOM   784  C  CA   . TYR   A 1 105 ? -20.91600 1.72600  28.78200 1.000 11.78971 ? 539  TYR   A CA   1 
ATOM   785  C  C    . TYR   A 1 105 ? -21.10600 2.06400  27.30900 1.000 11.45851 ? 539  TYR   A C    1 
ATOM   786  O  O    . TYR   A 1 105 ? -20.17100 2.52300  26.64100 1.000 12.42454 ? 539  TYR   A O    1 
ATOM   787  C  CB   . TYR   A 1 105 ? -20.90400 0.21200  29.00700 1.000 12.63761 ? 539  TYR   A CB   1 
ATOM   788  C  CG   . TYR   A 1 105 ? -19.90900 -0.55900 28.16500 1.000 16.22445 ? 539  TYR   A CG   1 
ATOM   789  C  CD1  . TYR   A 1 105 ? -18.54000 -0.37300 28.31800 1.000 9.77207  ? 539  TYR   A CD1  1 
ATOM   790  C  CD2  . TYR   A 1 105 ? -20.34300 -1.49800 27.23800 1.000 12.93234 ? 539  TYR   A CD2  1 
ATOM   791  C  CE1  . TYR   A 1 105 ? -17.63100 -1.08700 27.55200 1.000 14.06945 ? 539  TYR   A CE1  1 
ATOM   792  C  CE2  . TYR   A 1 105 ? -19.44600 -2.21300 26.47100 1.000 12.50731 ? 539  TYR   A CE2  1 
ATOM   793  C  CZ   . TYR   A 1 105 ? -18.09400 -2.00200 26.63000 1.000 13.77825 ? 539  TYR   A CZ   1 
ATOM   794  O  OH   . TYR   A 1 105 ? -17.20500 -2.71800 25.86800 1.000 13.64706 ? 539  TYR   A OH   1 
ATOM   795  N  N    . THR   A 1 106 ? -22.32700 1.87200  26.79700 1.000 9.50145  ? 540  THR   A N    1 
ATOM   796  C  CA   . THR   A 1 106 ? -22.63600 2.19000  25.40500 1.000 10.17848 ? 540  THR   A CA   1 
ATOM   797  C  C    . THR   A 1 106 ? -22.26500 3.63000  25.06800 1.000 13.60328 ? 540  THR   A C    1 
ATOM   798  O  O    . THR   A 1 106 ? -21.59100 3.89300  24.06500 1.000 12.06949 ? 540  THR   A O    1 
ATOM   799  C  CB   . THR   A 1 106 ? -24.12600 1.94900  25.13400 1.000 13.71844 ? 540  THR   A CB   1 
ATOM   800  O  OG1  . THR   A 1 106 ? -24.38900 0.54200  25.03700 1.000 22.78423 ? 540  THR   A OG1  1 
ATOM   801  C  CG2  . THR   A 1 106 ? -24.56200 2.63700  23.84900 1.000 15.21186 ? 540  THR   A CG2  1 
ATOM   802  N  N    . CYS   A 1 107 ? -22.69500 4.58000  25.90600 1.000 11.63537 ? 541  CYS   A N    1 
ATOM   803  C  CA   . CYS   A 1 107 ? -22.44200 5.98900  25.61800 1.000 13.60551 ? 541  CYS   A CA   1 
ATOM   804  C  C    . CYS   A 1 107 ? -20.94800 6.29600  25.61700 1.000 9.54486  ? 541  CYS   A C    1 
ATOM   805  O  O    . CYS   A 1 107 ? -20.46200 7.05300  24.76800 1.000 11.41500 ? 541  CYS   A O    1 
ATOM   806  C  CB   . CYS   A 1 107 ? -23.17700 6.87400  26.62600 1.000 12.14574 ? 541  CYS   A CB   1 
ATOM   807  S  SG   . CYS   A 1 107 ? -24.99100 6.71000  26.60000 1.000 12.18383 ? 541  CYS   A SG   1 
ATOM   808  N  N    . ALA   A 1 108 ? -20.20100 5.71700  26.55700 1.000 7.68558  ? 542  ALA   A N    1 
ATOM   809  C  CA   . ALA   A 1 108 ? -18.75800 5.92800  26.57000 1.000 11.17182 ? 542  ALA   A CA   1 
ATOM   810  C  C    . ALA   A 1 108 ? -18.10400 5.34600  25.32600 1.000 7.47857  ? 542  ALA   A C    1 
ATOM   811  O  O    . ALA   A 1 108 ? -17.10800 5.89400  24.84000 1.000 10.15234 ? 542  ALA   A O    1 
ATOM   812  C  CB   . ALA   A 1 108 ? -18.14400 5.32600  27.83200 1.000 12.89345 ? 542  ALA   A CB   1 
ATOM   813  N  N    . LEU   A 1 109 ? -18.65300 4.25200  24.79000 1.000 9.62738  ? 543  LEU   A N    1 
ATOM   814  C  CA   . LEU   A 1 109 ? -18.17600 3.73900  23.51100 1.000 8.01300  ? 543  LEU   A CA   1 
ATOM   815  C  C    . LEU   A 1 109 ? -18.47500 4.71200  22.38200 1.000 8.98116  ? 543  LEU   A C    1 
ATOM   816  O  O    . LEU   A 1 109 ? -17.63400 4.93300  21.50300 1.000 10.09996 ? 543  LEU   A O    1 
ATOM   817  C  CB   . LEU   A 1 109 ? -18.81000 2.38100  23.21500 1.000 11.61835 ? 543  LEU   A CB   1 
ATOM   818  C  CG   . LEU   A 1 109 ? -18.41700 1.22700  24.13400 1.000 9.34679  ? 543  LEU   A CG   1 
ATOM   819  C  CD1  . LEU   A 1 109 ? -18.97000 -0.08500 23.59700 1.000 9.43537  ? 543  LEU   A CD1  1 
ATOM   820  C  CD2  . LEU   A 1 109 ? -16.91400 1.17000  24.26400 1.000 9.21730  ? 543  LEU   A CD2  1 
ATOM   821  N  N    . LEU   A 1 110 ? -19.67500 5.29600  22.38300 1.000 11.04230 ? 544  LEU   A N    1 
ATOM   822  C  CA   . LEU   A 1 110 ? -20.03300 6.25700  21.34800 1.000 7.59022  ? 544  LEU   A CA   1 
ATOM   823  C  C    . LEU   A 1 110 ? -19.16800 7.50700  21.42400 1.000 7.17899  ? 544  LEU   A C    1 
ATOM   824  O  O    . LEU   A 1 110 ? -18.78200 8.06200  20.39300 1.000 12.89393 ? 544  LEU   A O    1 
ATOM   825  C  CB   . LEU   A 1 110 ? -21.50900 6.62500  21.46300 1.000 11.22988 ? 544  LEU   A CB   1 
ATOM   826  C  CG   . LEU   A 1 110 ? -22.47900 5.60000  20.88200 1.000 17.12811 ? 544  LEU   A CG   1 
ATOM   827  C  CD1  . LEU   A 1 110 ? -23.92400 6.03600  21.09400 1.000 24.87385 ? 544  LEU   A CD1  1 
ATOM   828  C  CD2  . LEU   A 1 110 ? -22.18900 5.40200  19.40900 1.000 10.12801 ? 544  LEU   A CD2  1 
ATOM   829  N  N    . ALA   A 1 111 ? -18.85400 7.96900  22.63400 1.000 6.96690  ? 545  ALA   A N    1 
ATOM   830  C  CA   . ALA   A 1 111 ? -18.01200 9.15100  22.77300 1.000 6.65648  ? 545  ALA   A CA   1 
ATOM   831  C  C    . ALA   A 1 111 ? -16.61400 8.91100  22.20900 1.000 10.46405 ? 545  ALA   A C    1 
ATOM   832  O  O    . ALA   A 1 111 ? -16.03000 9.80000  21.57500 1.000 9.09625  ? 545  ALA   A O    1 
ATOM   833  C  CB   . ALA   A 1 111 ? -17.93400 9.56300  24.24300 1.000 6.53189  ? 545  ALA   A CB   1 
ATOM   834  N  N    . ALA   A 1 112 ? -16.05700 7.71700  22.43500 1.000 6.79576  ? 546  ALA   A N    1 
ATOM   835  C  CA   . ALA   A 1 112 ? -14.73700 7.40900  21.89600 1.000 6.87677  ? 546  ALA   A CA   1 
ATOM   836  C  C    . ALA   A 1 112 ? -14.79300 7.19600  20.38700 1.000 9.55877  ? 546  ALA   A C    1 
ATOM   837  O  O    . ALA   A 1 112 ? -13.94900 7.72100  19.65300 1.000 7.36195  ? 546  ALA   A O    1 
ATOM   838  C  CB   . ALA   A 1 112 ? -14.15400 6.18200  22.59500 1.000 9.15481  ? 546  ALA   A CB   1 
ATOM   839  N  N    . GLY   A 1 113 ? -15.78000 6.43500  19.90600 1.000 8.89050  ? 547  GLY   A N    1 
ATOM   840  C  CA   . GLY   A 1 113 ? -15.88100 6.18800  18.47400 1.000 7.47954  ? 547  GLY   A CA   1 
ATOM   841  C  C    . GLY   A 1 113 ? -16.17400 7.44800  17.68100 1.000 11.06619 ? 547  GLY   A C    1 
ATOM   842  O  O    . GLY   A 1 113 ? -15.68800 7.61500  16.55900 1.000 12.69791 ? 547  GLY   A O    1 
ATOM   843  N  N    . SER   A 1 114 ? -16.97500 8.35100  18.25200 1.000 8.29374  ? 548  SER   A N    1 
ATOM   844  C  CA   . SER   A 1 114 ? -17.24400 9.62000  17.58500 1.000 10.67394 ? 548  SER   A CA   1 
ATOM   845  C  C    . SER   A 1 114 ? -15.95700 10.39300 17.35400 1.000 10.44821 ? 548  SER   A C    1 
ATOM   846  O  O    . SER   A 1 114 ? -15.78600 11.03700 16.31300 1.000 9.81852  ? 548  SER   A O    1 
ATOM   847  C  CB   . SER   A 1 114 ? -18.22400 10.45200 18.40800 1.000 8.90136  ? 548  SER   A CB   1 
ATOM   848  O  OG   . SER   A 1 114 ? -19.48000 9.80700  18.49500 1.000 12.07362 ? 548  SER   A OG   1 
ATOM   849  N  N    . CYS   A 1 115 ? -15.03400 10.32900 18.31500 1.000 11.58914 ? 549  CYS   A N    1 
ATOM   850  C  CA   . CYS   A 1 115 ? -13.77000 11.04400 18.18500 1.000 9.36137  ? 549  CYS   A CA   1 
ATOM   851  C  C    . CYS   A 1 115 ? -12.80200 10.31200 17.26500 1.000 9.79793  ? 549  CYS   A C    1 
ATOM   852  O  O    . CYS   A 1 115 ? -12.02400 10.95600 16.55400 1.000 8.54574  ? 549  CYS   A O    1 
ATOM   853  C  CB   . CYS   A 1 115 ? -13.14800 11.27000 19.56000 1.000 6.52980  ? 549  CYS   A CB   1 
ATOM   854  S  SG   . CYS   A 1 115 ? -14.08500 12.45300 20.54900 1.000 10.97273 ? 549  CYS   A SG   1 
ATOM   855  N  N    . PHE   A 1 116 ? -12.82200 8.97700  17.26900 1.000 7.11256  ? 550  PHE   A N    1 
ATOM   856  C  CA   . PHE   A 1 116 ? -12.03100 8.23200  16.29500 1.000 8.18358  ? 550  PHE   A CA   1 
ATOM   857  C  C    . PHE   A 1 116 ? -12.41800 8.64400  14.88200 1.000 13.39892 ? 550  PHE   A C    1 
ATOM   858  O  O    . PHE   A 1 116 ? -11.57100 9.07000  14.08600 1.000 12.36100 ? 550  PHE   A O    1 
ATOM   859  C  CB   . PHE   A 1 116 ? -12.22200 6.72100  16.47200 1.000 9.11966  ? 550  PHE   A CB   1 
ATOM   860  C  CG   . PHE   A 1 116 ? -11.85200 6.19800  17.83300 1.000 7.81001  ? 550  PHE   A CG   1 
ATOM   861  C  CD1  . PHE   A 1 116 ? -11.08800 6.94800  18.71200 1.000 7.43393  ? 550  PHE   A CD1  1 
ATOM   862  C  CD2  . PHE   A 1 116 ? -12.26500 4.93600  18.22400 1.000 9.12598  ? 550  PHE   A CD2  1 
ATOM   863  C  CE1  . PHE   A 1 116 ? -10.76000 6.45700  19.95500 1.000 7.18183  ? 550  PHE   A CE1  1 
ATOM   864  C  CE2  . PHE   A 1 116 ? -11.93500 4.44200  19.46500 1.000 7.63118  ? 550  PHE   A CE2  1 
ATOM   865  C  CZ   . PHE   A 1 116 ? -11.18400 5.20200  20.33000 1.000 7.38559  ? 550  PHE   A CZ   1 
ATOM   866  N  N    . ASN   A 1 117 ? -13.71300 8.53300  14.56300 1.000 10.26200 ? 551  ASN   A N    1 
ATOM   867  C  CA   . ASN   A 1 117 ? -14.22200 8.95500  13.26200 1.000 9.77893  ? 551  ASN   A CA   1 
ATOM   868  C  C    . ASN   A 1 117 ? -13.80300 10.38200 12.93400 1.000 12.67948 ? 551  ASN   A C    1 
ATOM   869  O  O    . ASN   A 1 117 ? -13.47200 10.69200 11.78400 1.000 12.85245 ? 551  ASN   A O    1 
ATOM   870  C  CB   . ASN   A 1 117 ? -15.74800 8.83100  13.23300 1.000 11.24451 ? 551  ASN   A CB   1 
ATOM   871  C  CG   . ASN   A 1 117 ? -16.21600 7.42000  12.93400 1.000 8.97544  ? 551  ASN   A CG   1 
ATOM   872  O  OD1  . ASN   A 1 117 ? -15.41400 6.50100  12.81100 1.000 13.32112 ? 551  ASN   A OD1  1 
ATOM   873  N  ND2  . ASN   A 1 117 ? -17.52100 7.24400  12.81700 1.000 10.64271 ? 551  ASN   A ND2  1 
ATOM   874  N  N    . SER   A 1 118 ? -13.80200 11.26600 13.93400 1.000 8.03979  ? 552  SER   A N    1 
ATOM   875  C  CA   . SER   A 1 118 ? -13.42700 12.65400 13.68700 1.000 8.78120  ? 552  SER   A CA   1 
ATOM   876  C  C    . SER   A 1 118 ? -11.93900 12.77300 13.37600 1.000 15.45889 ? 552  SER   A C    1 
ATOM   877  O  O    . SER   A 1 118 ? -11.55000 13.42700 12.40100 1.000 11.50812 ? 552  SER   A O    1 
ATOM   878  C  CB   . SER   A 1 118 ? -13.80400 13.52000 14.88900 1.000 14.09684 ? 552  SER   A CB   1 
ATOM   879  O  OG   . SER   A 1 118 ? -15.20800 13.70500 14.96100 1.000 11.79199 ? 552  SER   A OG   1 
ATOM   880  N  N    . ALA   A 1 119 ? -11.09100 12.14300 14.19500 1.000 13.94785 ? 553  ALA   A N    1 
ATOM   881  C  CA   . ALA   A 1 119 ? -9.65600  12.16500 13.92800 1.000 13.74418 ? 553  ALA   A CA   1 
ATOM   882  C  C    . ALA   A 1 119 ? -9.34400  11.55300 12.56900 1.000 10.12001 ? 553  ALA   A C    1 
ATOM   883  O  O    . ALA   A 1 119 ? -8.44000  12.01700 11.86400 1.000 8.51132  ? 553  ALA   A O    1 
ATOM   884  C  CB   . ALA   A 1 119 ? -8.89700  11.43100 15.03300 1.000 7.60515  ? 553  ALA   A CB   1 
ATOM   885  N  N    . GLN   A 1 120 ? -10.09200 10.52000 12.17800 1.000 9.76807  ? 554  GLN   A N    1 
ATOM   886  C  CA   . GLN   A 1 120 ? -9.88400  9.91100  10.86900 1.000 14.55360 ? 554  GLN   A CA   1 
ATOM   887  C  C    . GLN   A 1 120 ? -10.29300 10.85800 9.74700  1.000 13.22967 ? 554  GLN   A C    1 
ATOM   888  O  O    . GLN   A 1 120 ? -9.62400  10.92300 8.70700  1.000 13.95214 ? 554  GLN   A O    1 
ATOM   889  C  CB   . GLN   A 1 120 ? -10.65900 8.59700  10.77500 1.000 15.21380 ? 554  GLN   A CB   1 
ATOM   890  C  CG   . GLN   A 1 120 ? -10.52800 7.89900  9.43600  1.000 19.95751 ? 554  GLN   A CG   1 
ATOM   891  C  CD   . GLN   A 1 120 ? -11.19200 6.53600  9.42100  1.000 20.87709 ? 554  GLN   A CD   1 
ATOM   892  O  OE1  . GLN   A 1 120 ? -12.39100 6.41500  9.66300  1.000 22.98467 ? 554  GLN   A OE1  1 
ATOM   893  N  NE2  . GLN   A 1 120 ? -10.40900 5.50000  9.15000  1.000 36.03979 ? 554  GLN   A NE2  1 
ATOM   894  N  N    . ALA   A 1 121 ? -11.38700 11.60000 9.93700  1.000 15.30335 ? 555  ALA   A N    1 
ATOM   895  C  CA   . ALA   A 1 121 ? -11.78900 12.57800 8.93100  1.000 18.70147 ? 555  ALA   A CA   1 
ATOM   896  C  C    . ALA   A 1 121 ? -10.71700 13.64500 8.75100  1.000 12.89429 ? 555  ALA   A C    1 
ATOM   897  O  O    . ALA   A 1 121 ? -10.39500 14.02900 7.62100  1.000 20.15552 ? 555  ALA   A O    1 
ATOM   898  C  CB   . ALA   A 1 121 ? -13.12600 13.21400 9.31600  1.000 10.75298 ? 555  ALA   A CB   1 
ATOM   899  N  N    . ILE   A 1 122 ? -10.14700 14.12500 9.85800  1.000 13.92806 ? 556  ILE   A N    1 
ATOM   900  C  CA   . ILE   A 1 122 ? -9.08700  15.12800 9.78600  1.000 9.28208  ? 556  ILE   A CA   1 
ATOM   901  C  C    . ILE   A 1 122 ? -7.86200  14.55700 9.08400  1.000 9.65478  ? 556  ILE   A C    1 
ATOM   902  O  O    . ILE   A 1 122 ? -7.28700  15.18300 8.18800  1.000 13.16443 ? 556  ILE   A O    1 
ATOM   903  C  CB   . ILE   A 1 122 ? -8.73000  15.63300 11.19500 1.000 13.94052 ? 556  ILE   A CB   1 
ATOM   904  C  CG1  . ILE   A 1 122 ? -9.91500  16.35700 11.83700 1.000 11.75642 ? 556  ILE   A CG1  1 
ATOM   905  C  CG2  . ILE   A 1 122 ? -7.49600  16.53000 11.14400 1.000 10.05204 ? 556  ILE   A CG2  1 
ATOM   906  C  CD1  . ILE   A 1 122 ? -9.75200  16.57800 13.31900 1.000 8.15392  ? 556  ILE   A CD1  1 
ATOM   907  N  N    . LEU   A 1 123 ? -7.44900  13.35400 9.47900  1.000 9.48362  ? 557  LEU   A N    1 
ATOM   908  C  CA   . LEU   A 1 123 ? -6.15300  12.84100 9.05000  1.000 10.25230 ? 557  LEU   A CA   1 
ATOM   909  C  C    . LEU   A 1 123 ? -6.15600  12.41100 7.58400  1.000 17.29171 ? 557  LEU   A C    1 
ATOM   910  O  O    . LEU   A 1 123 ? -5.11400  12.48400 6.92500  1.000 13.28021 ? 557  LEU   A O    1 
ATOM   911  C  CB   . LEU   A 1 123 ? -5.72800  11.68200 9.95400  1.000 9.51111  ? 557  LEU   A CB   1 
ATOM   912  C  CG   . LEU   A 1 123 ? -5.28500  12.04500 11.37500 1.000 13.47031 ? 557  LEU   A CG   1 
ATOM   913  C  CD1  . LEU   A 1 123 ? -5.20800  10.80100 12.24300 1.000 8.85374  ? 557  LEU   A CD1  1 
ATOM   914  C  CD2  . LEU   A 1 123 ? -3.95300  12.77900 11.37500 1.000 9.38978  ? 557  LEU   A CD2  1 
ATOM   915  N  N    . THR   A 1 124 ? -7.29700  11.96600 7.05700  1.000 10.42639 ? 558  THR   A N    1 
ATOM   916  C  CA   . THR   A 1 124 ? -7.39600  11.59900 5.64800  1.000 11.03393 ? 558  THR   A CA   1 
ATOM   917  C  C    . THR   A 1 124 ? -7.80300  12.76700 4.75900  1.000 11.44700 ? 558  THR   A C    1 
ATOM   918  O  O    . THR   A 1 124 ? -8.00300  12.56900 3.55700  1.000 12.01947 ? 558  THR   A O    1 
ATOM   919  C  CB   . THR   A 1 124 ? -8.39200  10.45100 5.45200  1.000 11.01937 ? 558  THR   A CB   1 
ATOM   920  O  OG1  . THR   A 1 124 ? -9.68200  10.84000 5.94300  1.000 10.68495 ? 558  THR   A OG1  1 
ATOM   921  C  CG2  . THR   A 1 124 ? -7.92100  9.20000  6.17600  1.000 10.77542 ? 558  THR   A CG2  1 
ATOM   922  N  N    . GLY   A 1 125 ? -7.94800  13.96500 5.31500  1.000 11.23484 ? 559  GLY   A N    1 
ATOM   923  C  CA   . GLY   A 1 125 ? -8.23900  15.14200 4.52200  1.000 11.69600 ? 559  GLY   A CA   1 
ATOM   924  C  C    . GLY   A 1 125 ? -9.69800  15.39100 4.20900  1.000 12.65400 ? 559  GLY   A C    1 
ATOM   925  O  O    . GLY   A 1 125 ? -9.99600  16.30400 3.43000  1.000 12.21449 ? 559  GLY   A O    1 
ATOM   926  N  N    . GLN   A 1 126 ? -10.61700 14.61000 4.78000  1.000 11.29102 ? 560  GLN   A N    1 
ATOM   927  C  CA   . GLN   A 1 126 ? -12.03600 14.84600 4.52900  1.000 17.47324 ? 560  GLN   A CA   1 
ATOM   928  C  C    . GLN   A 1 126 ? -12.48800 16.16700 5.13900  1.000 11.14909 ? 560  GLN   A C    1 
ATOM   929  O  O    . GLN   A 1 126 ? -13.28000 16.89800 4.53700  1.000 11.50869 ? 560  GLN   A O    1 
ATOM   930  C  CB   . GLN   A 1 126 ? -12.86500 13.68600 5.07700  1.000 14.52611 ? 560  GLN   A CB   1 
ATOM   931  C  CG   . GLN   A 1 126 ? -12.54100 12.35000 4.43800  1.000 19.69995 ? 560  GLN   A CG   1 
ATOM   932  C  CD   . GLN   A 1 126 ? -13.23500 11.19100 5.12300  1.000 45.54479 ? 560  GLN   A CD   1 
ATOM   933  O  OE1  . GLN   A 1 126 ? -12.68300 10.09400 5.22000  1.000 38.03670 ? 560  GLN   A OE1  1 
ATOM   934  N  NE2  . GLN   A 1 126 ? -14.45500 11.42600 5.60100  1.000 33.59860 ? 560  GLN   A NE2  1 
ATOM   935  N  N    . VAL   A 1 127 ? -11.99800 16.48200 6.33600  1.000 17.18946 ? 561  VAL   A N    1 
ATOM   936  C  CA   . VAL   A 1 127 ? -12.21400 17.77000 6.97800  1.000 12.22041 ? 561  VAL   A CA   1 
ATOM   937  C  C    . VAL   A 1 127 ? -10.85300 18.27800 7.43600  1.000 13.20487 ? 561  VAL   A C    1 
ATOM   938  O  O    . VAL   A 1 127 ? -9.90200  17.51100 7.59300  1.000 10.65097 ? 561  VAL   A O    1 
ATOM   939  C  CB   . VAL   A 1 127 ? -13.19400 17.68600 8.17300  1.000 10.00474 ? 561  VAL   A CB   1 
ATOM   940  C  CG1  . VAL   A 1 127 ? -14.40200 16.83600 7.81900  1.000 9.91150  ? 561  VAL   A CG1  1 
ATOM   941  C  CG2  . VAL   A 1 127 ? -12.49700 17.13300 9.40100  1.000 13.75764 ? 561  VAL   A CG2  1 
ATOM   942  N  N    . ARG   A 1 128 ? -10.75700 19.59000 7.63500  1.000 14.05860 ? 562  ARG   A N    1 
ATOM   943  C  CA   . ARG   A 1 128 ? -9.50800  20.13700 8.15200  1.000 16.73554 ? 562  ARG   A CA   1 
ATOM   944  C  C    . ARG   A 1 128 ? -9.46500  20.08900 9.67200  1.000 14.80302 ? 562  ARG   A C    1 
ATOM   945  O  O    . ARG   A 1 128 ? -8.43900  19.72200 10.25400 1.000 15.82436 ? 562  ARG   A O    1 
ATOM   946  C  CB   . ARG   A 1 128 ? -9.30400  21.57700 7.67400  1.000 12.93110 ? 562  ARG   A CB   1 
ATOM   947  C  CG   . ARG   A 1 128 ? -10.06900 21.93100 6.41800  1.000 34.12511 ? 562  ARG   A CG   1 
ATOM   948  C  CD   . ARG   A 1 128 ? -9.62200  21.13100 5.20100  1.000 42.70667 ? 562  ARG   A CD   1 
ATOM   949  N  NE   . ARG   A 1 128 ? -10.66000 21.09200 4.17700  1.000 30.88782 ? 562  ARG   A NE   1 
ATOM   950  C  CZ   . ARG   A 1 128 ? -10.67800 20.23500 3.16600  1.000 35.03959 ? 562  ARG   A CZ   1 
ATOM   951  N  NH1  . ARG   A 1 128 ? -9.73700  19.31600 3.02600  1.000 30.84572 ? 562  ARG   A NH1  1 
ATOM   952  N  NH2  . ARG   A 1 128 ? -11.66600 20.29800 2.27800  1.000 42.91279 ? 562  ARG   A NH2  1 
ATOM   953  N  N    . ASN   A 1 129 ? -10.56800 20.44700 10.32100 1.000 9.67328  ? 563  ASN   A N    1 
ATOM   954  C  CA   . ASN   A 1 129 ? -10.68300 20.40800 11.76900 1.000 16.09686 ? 563  ASN   A CA   1 
ATOM   955  C  C    . ASN   A 1 129 ? -12.08300 19.92100 12.11100 1.000 16.18065 ? 563  ASN   A C    1 
ATOM   956  O  O    . ASN   A 1 129 ? -12.93700 19.76800 11.23400 1.000 16.10659 ? 563  ASN   A O    1 
ATOM   957  C  CB   . ASN   A 1 129 ? -10.37900 21.78000 12.39700 1.000 9.78272  ? 563  ASN   A CB   1 
ATOM   958  C  CG   . ASN   A 1 129 ? -11.17800 22.90700 11.76600 1.000 12.07877 ? 563  ASN   A CG   1 
ATOM   959  O  OD1  . ASN   A 1 129 ? -12.37200 22.76900 11.51000 1.000 10.18459 ? 563  ASN   A OD1  1 
ATOM   960  N  ND2  . ASN   A 1 129 ? -10.51700 24.02900 11.50500 1.000 10.12307 ? 563  ASN   A ND2  1 
ATOM   961  N  N    . ALA   A 1 130 ? -12.32200 19.66900 13.39600 1.000 12.12445 ? 564  ALA   A N    1 
ATOM   962  C  CA   . ALA   A 1 130 ? -13.58800 19.07000 13.79600 1.000 10.89777 ? 564  ALA   A CA   1 
ATOM   963  C  C    . ALA   A 1 130 ? -13.88200 19.37900 15.25900 1.000 14.32230 ? 564  ALA   A C    1 
ATOM   964  O  O    . ALA   A 1 130 ? -12.97800 19.64000 16.05900 1.000 8.51459  ? 564  ALA   A O    1 
ATOM   965  C  CB   . ALA   A 1 130 ? -13.58100 17.55500 13.56100 1.000 7.88719  ? 564  ALA   A CB   1 
ATOM   966  N  N    . VAL   A 1 131 ? -15.17200 19.33000 15.59200 1.000 11.85543 ? 565  VAL   A N    1 
ATOM   967  C  CA   . VAL   A 1 131 ? -15.67000 19.55700 16.94400 1.000 7.83938  ? 565  VAL   A CA   1 
ATOM   968  C  C    . VAL   A 1 131 ? -16.54900 18.37200 17.33000 1.000 9.33268  ? 565  VAL   A C    1 
ATOM   969  O  O    . VAL   A 1 131 ? -17.36100 17.90200 16.52500 1.000 9.76027  ? 565  VAL   A O    1 
ATOM   970  C  CB   . VAL   A 1 131 ? -16.44400 20.89000 17.04100 1.000 8.89916  ? 565  VAL   A CB   1 
ATOM   971  C  CG1  . VAL   A 1 131 ? -17.56000 20.94900 16.00200 1.000 13.96110 ? 565  VAL   A CG1  1 
ATOM   972  C  CG2  . VAL   A 1 131 ? -17.00500 21.07800 18.42300 1.000 9.83601  ? 565  VAL   A CG2  1 
ATOM   973  N  N    . ALA   A 1 132 ? -16.36500 17.86800 18.55000 1.000 7.78557  ? 566  ALA   A N    1 
ATOM   974  C  CA   . ALA   A 1 132 ? -17.02100 16.64700 19.00700 1.000 6.52398  ? 566  ALA   A CA   1 
ATOM   975  C  C    . ALA   A 1 132 ? -17.79600 16.94500 20.28300 1.000 6.77232  ? 566  ALA   A C    1 
ATOM   976  O  O    . ALA   A 1 132 ? -17.19800 17.20800 21.33100 1.000 6.22350  ? 566  ALA   A O    1 
ATOM   977  C  CB   . ALA   A 1 132 ? -16.00900 15.52400 19.23400 1.000 6.43707  ? 566  ALA   A CB   1 
ATOM   978  N  N    . ILE   A 1 133 ? -19.12000 16.88000 20.18800 1.000 7.74410  ? 567  ILE   A N    1 
ATOM   979  C  CA   . ILE   A 1 133 ? -20.01800 17.16200 21.30400 1.000 6.37041  ? 567  ILE   A CA   1 
ATOM   980  C  C    . ILE   A 1 133 ? -20.40000 15.80200 21.88100 1.000 6.62819  ? 567  ILE   A C    1 
ATOM   981  O  O    . ILE   A 1 133 ? -21.36400 15.16600 21.45000 1.000 10.28423 ? 567  ILE   A O    1 
ATOM   982  C  CB   . ILE   A 1 133 ? -21.23400 17.97100 20.85300 1.000 6.56440  ? 567  ILE   A CB   1 
ATOM   983  C  CG1  . ILE   A 1 133 ? -20.77500 19.23600 20.12300 1.000 6.70215  ? 567  ILE   A CG1  1 
ATOM   984  C  CG2  . ILE   A 1 133 ? -22.13000 18.32300 22.03600 1.000 7.54388  ? 567  ILE   A CG2  1 
ATOM   985  C  CD1  . ILE   A 1 133 ? -21.77400 19.77900 19.13400 1.000 7.00985  ? 567  ILE   A CD1  1 
ATOM   986  N  N    . VAL   A 1 134 ? -19.63000 15.34200 22.86600 1.000 6.76653  ? 568  VAL   A N    1 
ATOM   987  C  CA   . VAL   A 1 134 ? -19.75600 13.98700 23.38500 1.000 6.22162  ? 568  VAL   A CA   1 
ATOM   988  C  C    . VAL   A 1 134 ? -19.83700 13.99800 24.90500 1.000 9.59664  ? 568  VAL   A C    1 
ATOM   989  O  O    . VAL   A 1 134 ? -19.36400 14.92300 25.57400 1.000 8.03025  ? 568  VAL   A O    1 
ATOM   990  C  CB   . VAL   A 1 134 ? -18.58200 13.09000 22.92500 1.000 11.65148 ? 568  VAL   A CB   1 
ATOM   991  C  CG1  . VAL   A 1 134 ? -18.58800 12.92800 21.41000 1.000 6.34712  ? 568  VAL   A CG1  1 
ATOM   992  C  CG2  . VAL   A 1 134 ? -17.25200 13.66900 23.39700 1.000 6.07259  ? 568  VAL   A CG2  1 
ATOM   993  N  N    . ARG   A 1 135 ? -20.44800 12.95100 25.44500 1.000 8.60567  ? 569  ARG   A N    1 
ATOM   994  C  CA   . ARG   A 1 135 ? -20.46200 12.67400 26.87200 1.000 8.60360  ? 569  ARG   A CA   1 
ATOM   995  C  C    . ARG   A 1 135 ? -20.59000 11.17000 27.04800 1.000 8.20144  ? 569  ARG   A C    1 
ATOM   996  O  O    . ARG   A 1 135 ? -21.01200 10.47000 26.11900 1.000 11.03461 ? 569  ARG   A O    1 
ATOM   997  C  CB   . ARG   A 1 135 ? -21.61100 13.40500 27.58200 1.000 8.53109  ? 569  ARG   A CB   1 
ATOM   998  C  CG   . ARG   A 1 135 ? -22.99900 12.94200 27.17800 1.000 13.34284 ? 569  ARG   A CG   1 
ATOM   999  C  CD   . ARG   A 1 135 ? -24.07400 13.73000 27.92000 1.000 7.87969  ? 569  ARG   A CD   1 
ATOM   1000 N  NE   . ARG   A 1 135 ? -24.11100 13.41000 29.34300 1.000 10.98108 ? 569  ARG   A NE   1 
ATOM   1001 C  CZ   . ARG   A 1 135 ? -24.81400 12.41600 29.87000 1.000 9.51927  ? 569  ARG   A CZ   1 
ATOM   1002 N  NH1  . ARG   A 1 135 ? -25.52700 11.59700 29.11500 1.000 7.46382  ? 569  ARG   A NH1  1 
ATOM   1003 N  NH2  . ARG   A 1 135 ? -24.80900 12.24600 31.19000 1.000 7.43252  ? 569  ARG   A NH2  1 
ATOM   1004 N  N    . PRO   A 1 136 ? -20.19500 10.62800 28.21500 1.000 6.74810  ? 570  PRO   A N    1 
ATOM   1005 C  CA   . PRO   A 1 136 ? -19.54500 11.27700 29.36900 1.000 6.61824  ? 570  PRO   A CA   1 
ATOM   1006 C  C    . PRO   A 1 136 ? -18.12700 11.72300 29.02700 1.000 8.10451  ? 570  PRO   A C    1 
ATOM   1007 O  O    . PRO   A 1 136 ? -17.59000 11.32000 27.99000 1.000 9.29852  ? 570  PRO   A O    1 
ATOM   1008 C  CB   . PRO   A 1 136 ? -19.57100 10.17200 30.43900 1.000 6.92640  ? 570  PRO   A CB   1 
ATOM   1009 C  CG   . PRO   A 1 136 ? -19.51300 8.90200  29.64800 1.000 10.31251 ? 570  PRO   A CG   1 
ATOM   1010 C  CD   . PRO   A 1 136 ? -20.36800 9.18200  28.43700 1.000 6.99155  ? 570  PRO   A CD   1 
ATOM   1011 N  N    . PRO   A 1 137 ? -17.46700 12.56200 29.87200 1.000 10.97559 ? 571  PRO   A N    1 
ATOM   1012 C  CA   . PRO   A 1 137 ? -16.08500 12.95300 29.59300 1.000 6.25954  ? 571  PRO   A CA   1 
ATOM   1013 C  C    . PRO   A 1 137 ? -15.09600 11.82000 29.77700 1.000 10.24648 ? 571  PRO   A C    1 
ATOM   1014 O  O    . PRO   A 1 137 ? -15.50200 10.71800 30.10800 1.000 7.85831  ? 571  PRO   A O    1 
ATOM   1015 C  CB   . PRO   A 1 137 ? -15.82700 14.08300 30.57200 1.000 9.21726  ? 571  PRO   A CB   1 
ATOM   1016 C  CG   . PRO   A 1 137 ? -16.69800 13.75900 31.74900 1.000 10.64180 ? 571  PRO   A CG   1 
ATOM   1017 C  CD   . PRO   A 1 137 ? -17.93100 13.15300 31.13600 1.000 10.75498 ? 571  PRO   A CD   1 
ATOM   1018 N  N    . GLY   A 1 138 ? -13.80000 12.01800 29.51100 1.000 11.33167 ? 572  GLY   A N    1 
ATOM   1019 C  CA   . GLY   A 1 138 ? -12.84800 10.91900 29.77600 1.000 13.04998 ? 572  GLY   A CA   1 
ATOM   1020 C  C    . GLY   A 1 138 ? -11.49700 11.25200 30.39500 1.000 10.70909 ? 572  GLY   A C    1 
ATOM   1021 O  O    . GLY   A 1 138 ? -10.86500 10.31400 30.86800 1.000 9.99433  ? 572  GLY   A O    1 
ATOM   1022 N  N    . HIS   A 1 139 ? -11.09600 12.52000 30.42700 1.000 8.01853  ? 573  HIS   A N    1 
ATOM   1023 C  CA   . HIS   A 1 139 ? -9.71200  12.91400 30.83000 1.000 11.55124 ? 573  HIS   A CA   1 
ATOM   1024 C  C    . HIS   A 1 139 ? -9.27800  12.39000 32.21600 1.000 9.44119  ? 573  HIS   A C    1 
ATOM   1025 O  O    . HIS   A 1 139 ? -8.07400  12.31600 32.41200 1.000 10.46656 ? 573  HIS   A O    1 
ATOM   1026 C  CB   . HIS   A 1 139 ? -9.53700  14.43200 30.67000 1.000 9.62679  ? 573  HIS   A CB   1 
ATOM   1027 C  CG   . HIS   A 1 139 ? -10.19700 15.30600 31.67600 1.000 9.95718  ? 573  HIS   A CG   1 
ATOM   1028 N  ND1  . HIS   A 1 139 ? -9.67000  16.53700 31.99500 1.000 7.17899  ? 573  HIS   A ND1  1 
ATOM   1029 C  CD2  . HIS   A 1 139 ? -11.30400 15.18000 32.40400 1.000 6.89811  ? 573  HIS   A CD2  1 
ATOM   1030 C  CE1  . HIS   A 1 139 ? -10.44300 17.11700 32.89100 1.000 6.97171  ? 573  HIS   A CE1  1 
ATOM   1031 N  NE2  . HIS   A 1 139 ? -11.44600 16.32100 33.14000 1.000 9.55093  ? 573  HIS   A NE2  1 
ATOM   1032 N  N    . HIS   A 1 140 ? -10.21600 12.07900 33.11600 1.000 8.59673  ? 574  HIS   A N    1 
ATOM   1033 C  CA   . HIS   A 1 140 ? -9.89900  11.56500 34.47900 1.000 9.16414  ? 574  HIS   A CA   1 
ATOM   1034 C  C    . HIS   A 1 140 ? -9.74900  10.03900 34.47800 1.000 9.46271  ? 574  HIS   A C    1 
ATOM   1035 O  O    . HIS   A 1 140 ? -9.34100  9.47300  35.49800 1.000 8.13268  ? 574  HIS   A O    1 
ATOM   1036 C  CB   . HIS   A 1 140 ? -10.95800 11.99800 35.49900 1.000 8.64307  ? 574  HIS   A CB   1 
ATOM   1037 C  CG   . HIS   A 1 140 ? -11.08500 13.46100 35.74100 1.000 12.33922 ? 574  HIS   A CG   1 
ATOM   1038 N  ND1  . HIS   A 1 140 ? -10.04800 14.24000 36.19600 1.000 13.11266 ? 574  HIS   A ND1  1 
ATOM   1039 C  CD2  . HIS   A 1 140 ? -12.13600 14.27900 35.62500 1.000 10.22699 ? 574  HIS   A CD2  1 
ATOM   1040 C  CE1  . HIS   A 1 140 ? -10.46800 15.48500 36.32800 1.000 10.70463 ? 574  HIS   A CE1  1 
ATOM   1041 N  NE2  . HIS   A 1 140 ? -11.73100 15.52900 35.99200 1.000 12.39489 ? 574  HIS   A NE2  1 
ATOM   1042 N  N    . ALA   A 1 141 ? -10.13700 9.39400  33.37600 1.000 8.77839  ? 575  ALA   A N    1 
ATOM   1043 C  CA   . ALA   A 1 141 ? -10.10300 7.92100  33.33500 1.000 8.87461  ? 575  ALA   A CA   1 
ATOM   1044 C  C    . ALA   A 1 141 ? -8.65900  7.43700  33.22000 1.000 8.13494  ? 575  ALA   A C    1 
ATOM   1045 O  O    . ALA   A 1 141 ? -7.95300  7.92600  32.35800 1.000 7.80575  ? 575  ALA   A O    1 
ATOM   1046 C  CB   . ALA   A 1 141 ? -10.94900 7.35700  32.23700 1.000 11.51135 ? 575  ALA   A CB   1 
ATOM   1047 N  N    . GLU   A 1 142 ? -8.29200  6.50900  34.08600 1.000 8.43491  ? 576  GLU   A N    1 
ATOM   1048 C  CA   . GLU   A 1 142 ? -6.96400  5.91900  34.03800 1.000 13.64104 ? 576  GLU   A CA   1 
ATOM   1049 C  C    . GLU   A 1 142 ? -6.99300  4.66200  33.17400 1.000 15.55611 ? 576  GLU   A C    1 
ATOM   1050 O  O    . GLU   A 1 142 ? -8.04700  4.22100  32.71100 1.000 15.43724 ? 576  GLU   A O    1 
ATOM   1051 C  CB   . GLU   A 1 142 ? -6.46800  5.60000  35.44600 1.000 12.01279 ? 576  GLU   A CB   1 
ATOM   1052 C  CG   . GLU   A 1 142 ? -6.52900  6.76900  36.42000 1.000 14.18797 ? 576  GLU   A CG   1 
ATOM   1053 C  CD   . GLU   A 1 142 ? -5.26600  7.60300  36.42500 1.000 14.90769 ? 576  GLU   A CD   1 
ATOM   1054 O  OE1  . GLU   A 1 142 ? -4.46300  7.47600  35.48400 1.000 11.76614 ? 576  GLU   A OE1  1 
ATOM   1055 O  OE2  . GLU   A 1 142 ? -5.07700  8.38800  37.37400 1.000 19.82630 ? 576  GLU   A OE2  1 
ATOM   1056 N  N    . LYS   A 1 143 ? -5.81600  4.06700  32.96400 1.000 17.04667 ? 577  LYS   A N    1 
ATOM   1057 C  CA   . LYS   A 1 143 ? -5.74400  2.82100  32.20900 1.000 13.46900 ? 577  LYS   A CA   1 
ATOM   1058 C  C    . LYS   A 1 143 ? -6.56500  1.72000  32.86900 1.000 16.41782 ? 577  LYS   A C    1 
ATOM   1059 O  O    . LYS   A 1 143 ? -7.03200  0.80200  32.18700 1.000 14.93542 ? 577  LYS   A O    1 
ATOM   1060 C  CB   . LYS   A 1 143 ? -4.28800  2.37900  32.06000 1.000 9.57054  ? 577  LYS   A CB   1 
ATOM   1061 N  N    . ASP   A 1 144 ? -6.77000  1.80400  34.18700 1.000 15.16727 ? 578  ASP   A N    1 
ATOM   1062 C  CA   . ASP   A 1 144 ? -7.42800  0.73400  34.92700 1.000 14.12838 ? 578  ASP   A CA   1 
ATOM   1063 C  C    . ASP   A 1 144 ? -8.51300  1.24600  35.86900 1.000 17.80524 ? 578  ASP   A C    1 
ATOM   1064 O  O    . ASP   A 1 144 ? -8.92100  0.51200  36.77600 1.000 19.14392 ? 578  ASP   A O    1 
ATOM   1065 C  CB   . ASP   A 1 144 ? -6.40200  -0.08700 35.71500 1.000 14.96471 ? 578  ASP   A CB   1 
ATOM   1066 C  CG   . ASP   A 1 144 ? -5.72100  0.71700  36.81000 1.000 25.84892 ? 578  ASP   A CG   1 
ATOM   1067 O  OD1  . ASP   A 1 144 ? -5.70300  1.96500  36.73200 1.000 27.31843 ? 578  ASP   A OD1  1 
ATOM   1068 O  OD2  . ASP   A 1 144 ? -5.19100  0.09500  37.75300 1.000 37.08092 ? 578  ASP   A OD2  1 
ATOM   1069 N  N    . THR   A 1 145 ? -9.00700  2.46000  35.63000 1.000 12.36137 ? 579  THR   A N    1 
ATOM   1070 C  CA   . THR   A 1 145 ? -10.00700 3.00400  36.57200 1.000 22.22219 ? 579  THR   A CA   1 
ATOM   1071 C  C    . THR   A 1 145 ? -10.87200 4.09400  35.97800 1.000 17.47933 ? 579  THR   A C    1 
ATOM   1072 O  O    . THR   A 1 145 ? -10.38800 4.84500  35.10500 1.000 16.61584 ? 579  THR   A O    1 
ATOM   1073 C  CB   . THR   A 1 145 ? -9.36600  3.52400  37.86900 1.000 19.99988 ? 579  THR   A CB   1 
ATOM   1074 O  OG1  . THR   A 1 145 ? -10.42200 3.82100  38.77100 1.000 33.75216 ? 579  THR   A OG1  1 
ATOM   1075 C  CG2  . THR   A 1 145 ? -8.56700  4.80100  37.67900 1.000 23.57790 ? 579  THR   A CG2  1 
ATOM   1076 N  N    . ALA   A 1 146 ? -12.12800 4.10000  36.36500 1.000 14.40496 ? 580  ALA   A N    1 
ATOM   1077 C  CA   . ALA   A 1 146 ? -13.00600 5.21200  36.03900 1.000 14.27860 ? 580  ALA   A CA   1 
ATOM   1078 C  C    . ALA   A 1 146 ? -12.98400 6.22100  37.18100 1.000 10.79014 ? 580  ALA   A C    1 
ATOM   1079 O  O    . ALA   A 1 146 ? -12.80200 5.86300  38.34600 1.000 11.26469 ? 580  ALA   A O    1 
ATOM   1080 C  CB   . ALA   A 1 146 ? -14.43600 4.72800  35.78900 1.000 11.19337 ? 580  ALA   A CB   1 
ATOM   1081 N  N    . CYS   A 1 147 ? -13.15600 7.49300  36.83600 1.000 10.18635 ? 581  CYS   A N    1 
ATOM   1082 C  CA   . CYS   A 1 147 ? -12.98100 8.55100  37.82000 1.000 10.39837 ? 581  CYS   A CA   1 
ATOM   1083 C  C    . CYS   A 1 147 ? -13.61700 9.83000  37.30200 1.000 11.86527 ? 581  CYS   A C    1 
ATOM   1084 O  O    . CYS   A 1 147 ? -13.65400 10.07200 36.09400 1.000 9.38909  ? 581  CYS   A O    1 
ATOM   1085 C  CB   . CYS   A 1 147 ? -11.49200 8.77800  38.12800 1.000 10.00269 ? 581  CYS   A CB   1 
ATOM   1086 S  SG   . CYS   A 1 147 ? -11.11200 10.23200 39.14600 1.000 17.60302 ? 581  CYS   A SG   1 
ATOM   1087 N  N    . GLY   A 1 148 ? -14.11600 10.64300 38.23400 1.000 11.80619 ? 582  GLY   A N    1 
ATOM   1088 C  CA   . GLY   A 1 148 ? -14.59500 11.97900 37.93200 1.000 11.19970 ? 582  GLY   A CA   1 
ATOM   1089 C  C    . GLY   A 1 148 ? -15.50100 12.08500 36.72400 1.000 8.93689  ? 582  GLY   A C    1 
ATOM   1090 O  O    . GLY   A 1 148 ? -15.22800 12.86400 35.80400 1.000 8.78769  ? 582  GLY   A O    1 
ATOM   1091 N  N    . PHE   A 1 149 ? -16.57200 11.29300 36.71200 1.000 10.82682 ? 583  PHE   A N    1 
ATOM   1092 C  CA   . PHE   A 1 149 ? -17.60000 11.23900 35.67400 1.000 10.05395 ? 583  PHE   A CA   1 
ATOM   1093 C  C    . PHE   A 1 149 ? -17.08000 10.61400 34.38700 1.000 8.97481  ? 583  PHE   A C    1 
ATOM   1094 O  O    . PHE   A 1 149 ? -17.84600 10.48300 33.42700 1.000 11.86890 ? 583  PHE   A O    1 
ATOM   1095 C  CB   . PHE   A 1 149 ? -18.19900 12.61700 35.33100 1.000 11.67964 ? 583  PHE   A CB   1 
ATOM   1096 C  CG   . PHE   A 1 149 ? -18.49600 13.49500 36.52500 1.000 9.08903  ? 583  PHE   A CG   1 
ATOM   1097 C  CD1  . PHE   A 1 149 ? -18.68400 12.96500 37.79100 1.000 9.58007  ? 583  PHE   A CD1  1 
ATOM   1098 C  CD2  . PHE   A 1 149 ? -18.60600 14.86800 36.36400 1.000 14.06271 ? 583  PHE   A CD2  1 
ATOM   1099 C  CE1  . PHE   A 1 149 ? -18.95400 13.79000 38.87000 1.000 10.49719 ? 583  PHE   A CE1  1 
ATOM   1100 C  CE2  . PHE   A 1 149 ? -18.88000 15.69400 37.43500 1.000 9.12348  ? 583  PHE   A CE2  1 
ATOM   1101 C  CZ   . PHE   A 1 149 ? -19.05500 15.15600 38.69000 1.000 9.60609  ? 583  PHE   A CZ   1 
ATOM   1102 N  N    . CYS   A 1 150 ? -15.80900 10.22300 34.33400 1.000 14.58634 ? 584  CYS   A N    1 
ATOM   1103 C  CA   . CYS   A 1 150 ? -15.18100 9.69800  33.13000 1.000 9.65940  ? 584  CYS   A CA   1 
ATOM   1104 C  C    . CYS   A 1 150 ? -15.03400 8.18800  33.23700 1.000 17.19166 ? 584  CYS   A C    1 
ATOM   1105 O  O    . CYS   A 1 150 ? -14.70500 7.66100  34.30400 1.000 12.02334 ? 584  CYS   A O    1 
ATOM   1106 C  CB   . CYS   A 1 150 ? -13.80600 10.33200 32.90500 1.000 8.41605  ? 584  CYS   A CB   1 
ATOM   1107 S  SG   . CYS   A 1 150 ? -13.79200 12.14000 32.89500 1.000 7.92472  ? 584  CYS   A SG   1 
ATOM   1108 N  N    . PHE   A 1 151 ? -15.27000 7.49700  32.12100 1.000 11.64961 ? 585  PHE   A N    1 
ATOM   1109 C  CA   . PHE   A 1 151 ? -15.18200 6.04200  32.06600 1.000 12.40927 ? 585  PHE   A CA   1 
ATOM   1110 C  C    . PHE   A 1 151 ? -13.97300 5.57500  31.26900 1.000 13.04722 ? 585  PHE   A C    1 
ATOM   1111 O  O    . PHE   A 1 151 ? -13.11000 4.87400  31.80500 1.000 11.29524 ? 585  PHE   A O    1 
ATOM   1112 C  CB   . PHE   A 1 151 ? -16.47700 5.45900  31.48300 1.000 11.38762 ? 585  PHE   A CB   1 
ATOM   1113 C  CG   . PHE   A 1 151 ? -17.62300 5.46900  32.44700 1.000 11.99008 ? 585  PHE   A CG   1 
ATOM   1114 C  CD1  . PHE   A 1 151 ? -18.42500 6.59300  32.58500 1.000 14.44137 ? 585  PHE   A CD1  1 
ATOM   1115 C  CD2  . PHE   A 1 151 ? -17.88700 4.36300  33.23300 1.000 11.19107 ? 585  PHE   A CD2  1 
ATOM   1116 C  CE1  . PHE   A 1 151 ? -19.47600 6.60400  33.48400 1.000 10.91914 ? 585  PHE   A CE1  1 
ATOM   1117 C  CE2  . PHE   A 1 151 ? -18.93600 4.36700  34.12800 1.000 12.16271 ? 585  PHE   A CE2  1 
ATOM   1118 C  CZ   . PHE   A 1 151 ? -19.73200 5.49000  34.25600 1.000 11.18390 ? 585  PHE   A CZ   1 
ATOM   1119 N  N    . PHE   A 1 152 ? -13.89500 5.93400  29.99300 1.000 11.24119 ? 586  PHE   A N    1 
ATOM   1120 C  CA   . PHE   A 1 152 ? -12.71000 5.71500  29.18400 1.000 9.67475  ? 586  PHE   A CA   1 
ATOM   1121 C  C    . PHE   A 1 152 ? -12.16600 7.07100  28.76100 1.000 15.68343 ? 586  PHE   A C    1 
ATOM   1122 O  O    . PHE   A 1 152 ? -12.92700 8.02600  28.57700 1.000 9.56896  ? 586  PHE   A O    1 
ATOM   1123 C  CB   . PHE   A 1 152 ? -13.02000 4.84300  27.96200 1.000 11.30609 ? 586  PHE   A CB   1 
ATOM   1124 C  CG   . PHE   A 1 152 ? -13.72600 3.56500  28.30200 1.000 10.69263 ? 586  PHE   A CG   1 
ATOM   1125 C  CD1  . PHE   A 1 152 ? -13.10300 2.60100  29.07700 1.000 11.43644 ? 586  PHE   A CD1  1 
ATOM   1126 C  CD2  . PHE   A 1 152 ? -15.01600 3.33300  27.85700 1.000 10.84801 ? 586  PHE   A CD2  1 
ATOM   1127 C  CE1  . PHE   A 1 152 ? -13.75100 1.42400  29.39600 1.000 11.93994 ? 586  PHE   A CE1  1 
ATOM   1128 C  CE2  . PHE   A 1 152 ? -15.67000 2.16000  28.17100 1.000 14.70992 ? 586  PHE   A CE2  1 
ATOM   1129 C  CZ   . PHE   A 1 152 ? -15.03900 1.20200  28.94300 1.000 12.08376 ? 586  PHE   A CZ   1 
ATOM   1130 N  N    . ASN   A 1 153 ? -10.84300 7.15900  28.63500 1.000 13.82026 ? 587  ASN   A N    1 
ATOM   1131 C  CA   . ASN   A 1 153 ? -10.18300 8.43000  28.34200 1.000 10.32436 ? 587  ASN   A CA   1 
ATOM   1132 C  C    . ASN   A 1 153 ? -10.26300 8.67000  26.84000 1.000 17.53199 ? 587  ASN   A C    1 
ATOM   1133 O  O    . ASN   A 1 153 ? -9.42100  8.21600  26.06100 1.000 17.12706 ? 587  ASN   A O    1 
ATOM   1134 C  CB   . ASN   A 1 153 ? -8.74800  8.42800  28.85000 1.000 8.60898  ? 587  ASN   A CB   1 
ATOM   1135 C  CG   . ASN   A 1 153 ? -8.16300  9.81900  28.93200 1.000 9.15962  ? 587  ASN   A CG   1 
ATOM   1136 O  OD1  . ASN   A 1 153 ? -8.39800  10.65300 28.06100 1.000 7.81163  ? 587  ASN   A OD1  1 
ATOM   1137 N  ND2  . ASN   A 1 153 ? -7.39600  10.08000 29.98800 1.000 9.00077  ? 587  ASN   A ND2  1 
ATOM   1138 N  N    . THR   A 1 154 ? -11.29700 9.41400  26.44000 1.000 20.48312 ? 588  THR   A N    1 
ATOM   1139 C  CA   . THR   A 1 154 ? -11.60400 9.59200  25.02500 1.000 14.83170 ? 588  THR   A CA   1 
ATOM   1140 C  C    . THR   A 1 154 ? -10.46700 10.28900 24.28600 1.000 7.87253  ? 588  THR   A C    1 
ATOM   1141 O  O    . THR   A 1 154 ? -10.14500 9.92600  23.14800 1.000 8.07990  ? 588  THR   A O    1 
ATOM   1142 C  CB   . THR   A 1 154 ? -12.90500 10.38000 24.88300 1.000 10.12107 ? 588  THR   A CB   1 
ATOM   1143 O  OG1  . THR   A 1 154 ? -13.98200 9.62300  25.45200 1.000 12.64562 ? 588  THR   A OG1  1 
ATOM   1144 C  CG2  . THR   A 1 154 ? -13.20100 10.67100 23.42100 1.000 7.82666  ? 588  THR   A CG2  1 
ATOM   1145 N  N    . ALA   A 1 155 ? -9.84000  11.28400 24.91800 1.000 7.55428  ? 589  ALA   A N    1 
ATOM   1146 C  CA   . ALA   A 1 155 ? -8.74700  11.99800 24.26500 1.000 13.49403 ? 589  ALA   A CA   1 
ATOM   1147 C  C    . ALA   A 1 155 ? -7.51700  11.11300 24.11400 1.000 12.59466 ? 589  ALA   A C    1 
ATOM   1148 O  O    . ALA   A 1 155 ? -6.86800  11.11900 23.06100 1.000 7.93222  ? 589  ALA   A O    1 
ATOM   1149 C  CB   . ALA   A 1 155 ? -8.40400  13.26600 25.04600 1.000 13.50266 ? 589  ALA   A CB   1 
ATOM   1150 N  N    . ALA   A 1 156 ? -7.18200  10.34600 25.15500 1.000 10.42823 ? 590  ALA   A N    1 
ATOM   1151 C  CA   . ALA   A 1 156 ? -6.02300  9.46400  25.08500 1.000 11.03455 ? 590  ALA   A CA   1 
ATOM   1152 C  C    . ALA   A 1 156 ? -6.22100  8.37800  24.03700 1.000 9.36757  ? 590  ALA   A C    1 
ATOM   1153 O  O    . ALA   A 1 156 ? -5.28900  8.04000  23.29700 1.000 10.60579 ? 590  ALA   A O    1 
ATOM   1154 C  CB   . ALA   A 1 156 ? -5.75200  8.84200  26.45500 1.000 8.69771  ? 590  ALA   A CB   1 
ATOM   1155 N  N    . LEU   A 1 157 ? -7.43100  7.82200  23.96200 1.000 9.00527  ? 591  LEU   A N    1 
ATOM   1156 C  CA   . LEU   A 1 157 ? -7.71800  6.79800  22.96500 1.000 9.49943  ? 591  LEU   A CA   1 
ATOM   1157 C  C    . LEU   A 1 157 ? -7.63600  7.36000  21.55500 1.000 9.41873  ? 591  LEU   A C    1 
ATOM   1158 O  O    . LEU   A 1 157 ? -7.18400  6.67100  20.63600 1.000 9.90795  ? 591  LEU   A O    1 
ATOM   1159 C  CB   . LEU   A 1 157 ? -9.09800  6.19600  23.22000 1.000 13.52623 ? 591  LEU   A CB   1 
ATOM   1160 C  CG   . LEU   A 1 157 ? -9.21200  5.32900  24.47100 1.000 13.74488 ? 591  LEU   A CG   1 
ATOM   1161 C  CD1  . LEU   A 1 157 ? -10.65300 5.26100  24.94700 1.000 9.85933  ? 591  LEU   A CD1  1 
ATOM   1162 C  CD2  . LEU   A 1 157 ? -8.67100  3.93500  24.19000 1.000 10.71118 ? 591  LEU   A CD2  1 
ATOM   1163 N  N    . THR   A 1 158 ? -8.07300  8.60600  21.36100 1.000 13.14507 ? 592  THR   A N    1 
ATOM   1164 C  CA   . THR   A 1 158 ? -8.04100  9.19700  20.02700 1.000 13.88620 ? 592  THR   A CA   1 
ATOM   1165 C  C    . THR   A 1 158 ? -6.60800  9.46900  19.57700 1.000 9.02749  ? 592  THR   A C    1 
ATOM   1166 O  O    . THR   A 1 158 ? -6.28800  9.33000  18.39100 1.000 9.32086  ? 592  THR   A O    1 
ATOM   1167 C  CB   . THR   A 1 158 ? -8.87500  10.47800 20.00100 1.000 8.34879  ? 592  THR   A CB   1 
ATOM   1168 O  OG1  . THR   A 1 158 ? -10.24100 10.15800 20.29300 1.000 9.06777  ? 592  THR   A OG1  1 
ATOM   1169 C  CG2  . THR   A 1 158 ? -8.81200  11.13800 18.63800 1.000 8.38686  ? 592  THR   A CG2  1 
ATOM   1170 N  N    . ALA   A 1 159 ? -5.73600  9.86600  20.50400 1.000 9.67102  ? 593  ALA   A N    1 
ATOM   1171 C  CA   . ALA   A 1 159 ? -4.32300  10.01300 20.16500 1.000 11.76489 ? 593  ALA   A CA   1 
ATOM   1172 C  C    . ALA   A 1 159 ? -3.74600  8.69100  19.67800 1.000 9.74783  ? 593  ALA   A C    1 
ATOM   1173 O  O    . ALA   A 1 159 ? -3.09900  8.62900  18.62600 1.000 10.30149 ? 593  ALA   A O    1 
ATOM   1174 C  CB   . ALA   A 1 159 ? -3.54400  10.53700 21.37400 1.000 8.81270  ? 593  ALA   A CB   1 
ATOM   1175 N  N    . ARG   A 1 160 ? -4.01100  7.61000  20.41500 1.000 10.02868 ? 594  ARG   A N    1 
ATOM   1176 C  CA   . ARG   A 1 160 ? -3.50400  6.29600  20.02600 1.000 10.80893 ? 594  ARG   A CA   1 
ATOM   1177 C  C    . ARG   A 1 160 ? -4.16800  5.79600  18.75000 1.000 11.16153 ? 594  ARG   A C    1 
ATOM   1178 O  O    . ARG   A 1 160 ? -3.49400  5.24100  17.87300 1.000 11.78053 ? 594  ARG   A O    1 
ATOM   1179 C  CB   . ARG   A 1 160 ? -3.71800  5.29800  21.15900 1.000 11.08038 ? 594  ARG   A CB   1 
ATOM   1180 C  CG   . ARG   A 1 160 ? -2.91700  5.60500  22.40300 1.000 17.47996 ? 594  ARG   A CG   1 
ATOM   1181 C  CD   . ARG   A 1 160 ? -1.44000  5.72800  22.07400 1.000 11.26819 ? 594  ARG   A CD   1 
ATOM   1182 N  NE   . ARG   A 1 160 ? -0.61600  5.63500  23.27100 1.000 18.63223 ? 594  ARG   A NE   1 
ATOM   1183 C  CZ   . ARG   A 1 160 ? 0.65900   5.99200  23.32700 1.000 12.57692 ? 594  ARG   A CZ   1 
ATOM   1184 N  NH1  . ARG   A 1 160 ? 1.27800   6.50500  22.27700 1.000 13.08313 ? 594  ARG   A NH1  1 
ATOM   1185 N  NH2  . ARG   A 1 160 ? 1.32500   5.83900  24.46900 1.000 22.18161 ? 594  ARG   A NH2  1 
ATOM   1186 N  N    . TYR   A 1 161 ? -5.48900  5.95900  18.63800 1.000 12.98159 ? 595  TYR   A N    1 
ATOM   1187 C  CA   . TYR   A 1 161 ? -6.17400  5.58700  17.40500 1.000 14.84308 ? 595  TYR   A CA   1 
ATOM   1188 C  C    . TYR   A 1 161 ? -5.56900  6.31500  16.21300 1.000 13.14086 ? 595  TYR   A C    1 
ATOM   1189 O  O    . TYR   A 1 161 ? -5.33800  5.71700  15.15600 1.000 14.52282 ? 595  TYR   A O    1 
ATOM   1190 C  CB   . TYR   A 1 161 ? -7.67400  5.89000  17.49800 1.000 12.07996 ? 595  TYR   A CB   1 
ATOM   1191 C  CG   . TYR   A 1 161 ? -8.34800  5.80900  16.14400 1.000 11.10870 ? 595  TYR   A CG   1 
ATOM   1192 C  CD1  . TYR   A 1 161 ? -8.77200  4.58800  15.63200 1.000 11.81186 ? 595  TYR   A CD1  1 
ATOM   1193 C  CD2  . TYR   A 1 161 ? -8.52900  6.94700  15.36300 1.000 10.77252 ? 595  TYR   A CD2  1 
ATOM   1194 C  CE1  . TYR   A 1 161 ? -9.36900  4.50100  14.38500 1.000 12.15718 ? 595  TYR   A CE1  1 
ATOM   1195 C  CE2  . TYR   A 1 161 ? -9.12100  6.86900  14.11300 1.000 11.38543 ? 595  TYR   A CE2  1 
ATOM   1196 C  CZ   . TYR   A 1 161 ? -9.53800  5.64400  13.63100 1.000 11.80297 ? 595  TYR   A CZ   1 
ATOM   1197 O  OH   . TYR   A 1 161 ? -10.12900 5.57100  12.39100 1.000 12.45118 ? 595  TYR   A OH   1 
ATOM   1198 N  N    . ALA   A 1 162 ? -5.32600  7.61900  16.36500 1.000 10.64539 ? 596  ALA   A N    1 
ATOM   1199 C  CA   . ALA   A 1 162 ? -4.74900  8.39900  15.27800 1.000 10.71310 ? 596  ALA   A CA   1 
ATOM   1200 C  C    . ALA   A 1 162 ? -3.41900  7.81000  14.82600 1.000 16.72103 ? 596  ALA   A C    1 
ATOM   1201 O  O    . ALA   A 1 162 ? -3.16200  7.69400  13.62200 1.000 14.65742 ? 596  ALA   A O    1 
ATOM   1202 C  CB   . ALA   A 1 162 ? -4.57800  9.85400  15.71400 1.000 10.04624 ? 596  ALA   A CB   1 
ATOM   1203 N  N    . GLN   A 1 163 ? -2.57400  7.40400  15.77800 1.000 13.39133 ? 597  GLN   A N    1 
ATOM   1204 C  CA   . GLN   A 1 163 ? -1.29400  6.80000  15.42300 1.000 12.18105 ? 597  GLN   A CA   1 
ATOM   1205 C  C    . GLN   A 1 163 ? -1.48000  5.41800  14.80700 1.000 13.01635 ? 597  GLN   A C    1 
ATOM   1206 O  O    . GLN   A 1 163 ? -0.70800  5.02800  13.92200 1.000 13.73097 ? 597  GLN   A O    1 
ATOM   1207 C  CB   . GLN   A 1 163 ? -0.38800  6.72600  16.65400 1.000 12.12830 ? 597  GLN   A CB   1 
ATOM   1208 C  CG   . GLN   A 1 163 ? -0.15700  8.07300  17.33200 1.000 15.10916 ? 597  GLN   A CG   1 
ATOM   1209 C  CD   . GLN   A 1 163 ? 0.69200   7.97100  18.59100 1.000 11.91422 ? 597  GLN   A CD   1 
ATOM   1210 O  OE1  . GLN   A 1 163 ? 0.55400   7.03800  19.38400 1.000 12.96640 ? 597  GLN   A OE1  1 
ATOM   1211 N  NE2  . GLN   A 1 163 ? 1.58500   8.92900  18.76900 1.000 11.21298 ? 597  GLN   A NE2  1 
ATOM   1212 N  N    . SER   A 1 164 ? -2.50000  4.67200  15.24600 1.000 13.01447 ? 598  SER   A N    1 
ATOM   1213 C  CA   . SER   A 1 164 ? -2.74700  3.35100  14.68100 1.000 13.87373 ? 598  SER   A CA   1 
ATOM   1214 C  C    . SER   A 1 164 ? -3.09400  3.42900  13.19900 1.000 14.87541 ? 598  SER   A C    1 
ATOM   1215 O  O    . SER   A 1 164 ? -2.73600  2.52800  12.43100 1.000 17.33815 ? 598  SER   A O    1 
ATOM   1216 C  CB   . SER   A 1 164 ? -3.86200  2.64000  15.45100 1.000 16.38207 ? 598  SER   A CB   1 
ATOM   1217 O  OG   . SER   A 1 164 ? -5.14600  3.10800  15.06900 1.000 13.35055 ? 598  SER   A OG   1 
ATOM   1218 N  N    . ILE   A 1 165 ? -3.77600  4.49700  12.77400 1.000 15.87293 ? 599  ILE   A N    1 
ATOM   1219 C  CA   . ILE   A 1 165 ? -4.16300  4.65500  11.37500 1.000 15.68923 ? 599  ILE   A CA   1 
ATOM   1220 C  C    . ILE   A 1 165 ? -3.19900  5.53800  10.60200 1.000 14.05197 ? 599  ILE   A C    1 
ATOM   1221 O  O    . ILE   A 1 165 ? -3.45300  5.83400  9.42700  1.000 17.54147 ? 599  ILE   A O    1 
ATOM   1222 C  CB   . ILE   A 1 165 ? -5.59600  5.20800  11.24400 1.000 15.37404 ? 599  ILE   A CB   1 
ATOM   1223 C  CG1  . ILE   A 1 165 ? -5.67200  6.63200  11.79800 1.000 18.53509 ? 599  ILE   A CG1  1 
ATOM   1224 C  CG2  . ILE   A 1 165 ? -6.59200  4.29300  11.94700 1.000 13.45873 ? 599  ILE   A CG2  1 
ATOM   1225 C  CD1  . ILE   A 1 165 ? -6.92300  7.37800  11.39300 1.000 12.09365 ? 599  ILE   A CD1  1 
ATOM   1226 N  N    . THR   A 1 166 ? -2.11000  5.98400  11.22500 1.000 17.05859 ? 600  THR   A N    1 
ATOM   1227 C  CA   . THR   A 1 166 ? -1.08400  6.72200  10.49800 1.000 19.84384 ? 600  THR   A CA   1 
ATOM   1228 C  C    . THR   A 1 166 ? 0.27400   6.05600  10.68900 1.000 15.24002 ? 600  THR   A C    1 
ATOM   1229 O  O    . THR   A 1 166 ? 0.69600   5.24500  9.86100  1.000 15.69927 ? 600  THR   A O    1 
ATOM   1230 C  CB   . THR   A 1 166 ? -1.04700  8.19100  10.94100 1.000 14.32071 ? 600  THR   A CB   1 
ATOM   1231 O  OG1  . THR   A 1 166 ? -0.91800  8.27600  12.36800 1.000 12.61099 ? 600  THR   A OG1  1 
ATOM   1232 C  CG2  . THR   A 1 166 ? -2.31800  8.91000  10.50100 1.000 12.69627 ? 600  THR   A CG2  1 
ATOM   1233 N  N    . ARG   A 1 167 ? 0.95900   6.37900  11.78200 1.000 14.65450 ? 601  ARG   A N    1 
ATOM   1234 C  CA   . ARG   A 1 167 ? 2.22000   5.73500  12.10600 1.000 17.26664 ? 601  ARG   A CA   1 
ATOM   1235 C  C    . ARG   A 1 167 ? 2.46800   5.89400  13.59600 1.000 18.32243 ? 601  ARG   A C    1 
ATOM   1236 O  O    . ARG   A 1 167 ? 1.89600   6.77000  14.25100 1.000 16.44269 ? 601  ARG   A O    1 
ATOM   1237 C  CB   . ARG   A 1 167 ? 3.37900   6.31500  11.29000 1.000 19.26494 ? 601  ARG   A CB   1 
ATOM   1238 C  CG   . ARG   A 1 167 ? 3.53300   7.81000  11.44900 1.000 18.60461 ? 601  ARG   A CG   1 
ATOM   1239 C  CD   . ARG   A 1 167 ? 4.72100   8.33100  10.67500 1.000 18.86794 ? 601  ARG   A CD   1 
ATOM   1240 N  NE   . ARG   A 1 167 ? 5.29700   9.48700  11.34700 1.000 21.06376 ? 601  ARG   A NE   1 
ATOM   1241 C  CZ   . ARG   A 1 167 ? 4.85900   10.72900 11.20600 1.000 14.01422 ? 601  ARG   A CZ   1 
ATOM   1242 N  NH1  . ARG   A 1 167 ? 3.86900   11.02200 10.37800 1.000 18.26038 ? 601  ARG   A NH1  1 
ATOM   1243 N  NH2  . ARG   A 1 167 ? 5.43000   11.70100 11.91000 1.000 13.59973 ? 601  ARG   A NH2  1 
ATOM   1244 N  N    . GLU   A 1 168 ? 3.33000   5.02200  14.12300 1.000 19.73600 ? 602  GLU   A N    1 
ATOM   1245 C  CA   . GLU   A 1 168 ? 3.58000   4.99800  15.56000 1.000 24.71074 ? 602  GLU   A CA   1 
ATOM   1246 C  C    . GLU   A 1 168 ? 4.09900   6.34200  16.05600 1.000 19.02846 ? 602  GLU   A C    1 
ATOM   1247 O  O    . GLU   A 1 168 ? 3.74400   6.78600  17.15500 1.000 17.59921 ? 602  GLU   A O    1 
ATOM   1248 C  CB   . GLU   A 1 168 ? 4.56700   3.87700  15.89300 1.000 30.40262 ? 602  GLU   A CB   1 
ATOM   1249 C  CG   . GLU   A 1 168 ? 4.69000   3.57300  17.37600 1.000 33.78027 ? 602  GLU   A CG   1 
ATOM   1250 C  CD   . GLU   A 1 168 ? 4.54500   2.09300  17.68200 1.000 44.17755 ? 602  GLU   A CD   1 
ATOM   1251 O  OE1  . GLU   A 1 168 ? 4.46000   1.29300  16.72500 1.000 40.59819 ? 602  GLU   A OE1  1 
ATOM   1252 O  OE2  . GLU   A 1 168 ? 4.51000   1.73200  18.87900 1.000 43.15516 ? 602  GLU   A OE2  1 
ATOM   1253 N  N    . SER   A 1 169 ? 4.91500   7.01700  15.25000 1.000 17.63825 ? 603  SER   A N    1 
ATOM   1254 C  CA   . SER   A 1 169 ? 5.59900   8.23200  15.67000 1.000 13.82318 ? 603  SER   A CA   1 
ATOM   1255 C  C    . SER   A 1 169 ? 4.82900   9.50500  15.34400 1.000 13.03119 ? 603  SER   A C    1 
ATOM   1256 O  O    . SER   A 1 169 ? 5.41400   10.59200 15.39400 1.000 15.11002 ? 603  SER   A O    1 
ATOM   1257 C  CB   . SER   A 1 169 ? 6.98600   8.30200  15.02800 1.000 14.60057 ? 603  SER   A CB   1 
ATOM   1258 O  OG   . SER   A 1 169 ? 6.88300   8.58500  13.64500 1.000 19.07161 ? 603  SER   A OG   1 
ATOM   1259 N  N    . LEU   A 1 170 ? 3.54500   9.40800  15.00700 1.000 12.67949 ? 604  LEU   A N    1 
ATOM   1260 C  CA   . LEU   A 1 170 ? 2.76000   10.61600 14.79100 1.000 11.97537 ? 604  LEU   A CA   1 
ATOM   1261 C  C    . LEU   A 1 170 ? 2.80900   11.48400 16.04300 1.000 12.89292 ? 604  LEU   A C    1 
ATOM   1262 O  O    . LEU   A 1 170 ? 2.60100   10.99900 17.15700 1.000 17.58572 ? 604  LEU   A O    1 
ATOM   1263 C  CB   . LEU   A 1 170 ? 1.31400   10.26500 14.44000 1.000 11.73952 ? 604  LEU   A CB   1 
ATOM   1264 C  CG   . LEU   A 1 170 ? 0.45700   11.46100 14.01100 1.000 13.22670 ? 604  LEU   A CG   1 
ATOM   1265 C  CD1  . LEU   A 1 170 ? 0.79600   11.88800 12.58600 1.000 12.66676 ? 604  LEU   A CD1  1 
ATOM   1266 C  CD2  . LEU   A 1 170 ? -1.03000  11.17400 14.15200 1.000 10.82011 ? 604  LEU   A CD2  1 
ATOM   1267 N  N    . ARG   A 1 171 ? 3.12200   12.76400 15.86200 1.000 11.02894 ? 605  ARG   A N    1 
ATOM   1268 C  CA   . ARG   A 1 171 ? 3.24400   13.69700 16.97400 1.000 10.48721 ? 605  ARG   A CA   1 
ATOM   1269 C  C    . ARG   A 1 171 ? 1.87600   14.30600 17.26500 1.000 14.06214 ? 605  ARG   A C    1 
ATOM   1270 O  O    . ARG   A 1 171 ? 1.28600   14.95800 16.39700 1.000 12.20027 ? 605  ARG   A O    1 
ATOM   1271 C  CB   . ARG   A 1 171 ? 4.27100   14.78400 16.65800 1.000 10.63670 ? 605  ARG   A CB   1 
ATOM   1272 C  CG   . ARG   A 1 171 ? 5.69400   14.26800 16.48600 1.000 11.36052 ? 605  ARG   A CG   1 
ATOM   1273 C  CD   . ARG   A 1 171 ? 6.69900   15.40800 16.36200 1.000 16.99458 ? 605  ARG   A CD   1 
ATOM   1274 N  NE   . ARG   A 1 171 ? 6.39300   16.28700 15.24000 1.000 18.82593 ? 605  ARG   A NE   1 
ATOM   1275 C  CZ   . ARG   A 1 171 ? 6.84400   16.11900 14.00400 1.000 15.54922 ? 605  ARG   A CZ   1 
ATOM   1276 N  NH1  . ARG   A 1 171 ? 7.64900   15.11600 13.69200 1.000 14.03248 ? 605  ARG   A NH1  1 
ATOM   1277 N  NH2  . ARG   A 1 171 ? 6.47600   16.97800 13.05700 1.000 16.20038 ? 605  ARG   A NH2  1 
ATOM   1278 N  N    . VAL   A 1 172 ? 1.37300   14.08900 18.47900 1.000 11.68437 ? 606  VAL   A N    1 
ATOM   1279 C  CA   . VAL   A 1 172 ? 0.03600   14.52100 18.86900 1.000 11.49834 ? 606  VAL   A CA   1 
ATOM   1280 C  C    . VAL   A 1 172 ? 0.13800   15.40300 20.10600 1.000 14.70558 ? 606  VAL   A C    1 
ATOM   1281 O  O    . VAL   A 1 172 ? 0.71500   14.99700 21.12200 1.000 12.91402 ? 606  VAL   A O    1 
ATOM   1282 C  CB   . VAL   A 1 172 ? -0.89600  13.32400 19.13000 1.000 15.64707 ? 606  VAL   A CB   1 
ATOM   1283 C  CG1  . VAL   A 1 172 ? -2.25300  13.80900 19.62300 1.000 10.12115 ? 606  VAL   A CG1  1 
ATOM   1284 C  CG2  . VAL   A 1 172 ? -1.05300  12.48500 17.86400 1.000 12.65323 ? 606  VAL   A CG2  1 
ATOM   1285 N  N    . LEU   A 1 173 ? -0.42600  16.60400 20.01900 1.000 17.82091 ? 607  LEU   A N    1 
ATOM   1286 C  CA   . LEU   A 1 173 ? -0.51100  17.52600 21.14400 1.000 9.70254  ? 607  LEU   A CA   1 
ATOM   1287 C  C    . LEU   A 1 173 ? -1.91600  17.46800 21.73200 1.000 12.58633 ? 607  LEU   A C    1 
ATOM   1288 O  O    . LEU   A 1 173 ? -2.89800  17.72500 21.02800 1.000 14.02599 ? 607  LEU   A O    1 
ATOM   1289 C  CB   . LEU   A 1 173 ? -0.18300  18.95000 20.70300 1.000 9.13582  ? 607  LEU   A CB   1 
ATOM   1290 C  CG   . LEU   A 1 173 ? -0.57000  20.05600 21.68600 1.000 10.43275 ? 607  LEU   A CG   1 
ATOM   1291 C  CD1  . LEU   A 1 173 ? 0.31100   20.01500 22.92900 1.000 10.88389 ? 607  LEU   A CD1  1 
ATOM   1292 C  CD2  . LEU   A 1 173 ? -0.51300  21.43000 21.02200 1.000 7.65542  ? 607  LEU   A CD2  1 
ATOM   1293 N  N    . ILE   A 1 174 ? -2.01000  17.13400 23.01600 1.000 12.22368 ? 608  ILE   A N    1 
ATOM   1294 C  CA   . ILE   A 1 174 ? -3.27000  17.15400 23.74900 1.000 6.98549  ? 608  ILE   A CA   1 
ATOM   1295 C  C    . ILE   A 1 174 ? -3.23000  18.36200 24.67100 1.000 6.78830  ? 608  ILE   A C    1 
ATOM   1296 O  O    . ILE   A 1 174 ? -2.44800  18.39600 25.62700 1.000 6.87188  ? 608  ILE   A O    1 
ATOM   1297 C  CB   . ILE   A 1 174 ? -3.49600  15.85900 24.54000 1.000 7.10249  ? 608  ILE   A CB   1 
ATOM   1298 C  CG1  . ILE   A 1 174 ? -3.53000  14.65200 23.60000 1.000 7.40098  ? 608  ILE   A CG1  1 
ATOM   1299 C  CG2  . ILE   A 1 174 ? -4.78300  15.94900 25.34200 1.000 7.32661  ? 608  ILE   A CG2  1 
ATOM   1300 C  CD1  . ILE   A 1 174 ? -3.83000  13.34400 24.29500 1.000 7.61146  ? 608  ILE   A CD1  1 
ATOM   1301 N  N    . VAL   A 1 175 ? -4.04900  19.36700 24.38000 1.000 6.60520  ? 609  VAL   A N    1 
ATOM   1302 C  CA   . VAL   A 1 175 ? -4.18800  20.53900 25.24000 1.000 6.88751  ? 609  VAL   A CA   1 
ATOM   1303 C  C    . VAL   A 1 175 ? -5.46500  20.37400 26.04900 1.000 6.34720  ? 609  VAL   A C    1 
ATOM   1304 O  O    . VAL   A 1 175 ? -6.55300  20.21100 25.48300 1.000 7.68227  ? 609  VAL   A O    1 
ATOM   1305 C  CB   . VAL   A 1 175 ? -4.21000  21.84400 24.43100 1.000 6.52184  ? 609  VAL   A CB   1 
ATOM   1306 C  CG1  . VAL   A 1 175 ? -4.62700  23.00100 25.32500 1.000 12.31136 ? 609  VAL   A CG1  1 
ATOM   1307 C  CG2  . VAL   A 1 175 ? -2.84600  22.11400 23.83400 1.000 6.74150  ? 609  VAL   A CG2  1 
ATOM   1308 N  N    . ASP   A 1 176 ? -5.33400  20.41100 27.37000 1.000 6.36336  ? 610  ASP   A N    1 
ATOM   1309 C  CA   . ASP   A 1 176 ? -6.43200  20.15100 28.29800 1.000 12.22971 ? 610  ASP   A CA   1 
ATOM   1310 C  C    . ASP   A 1 176 ? -6.73000  21.44500 29.05800 1.000 8.98169  ? 610  ASP   A C    1 
ATOM   1311 O  O    . ASP   A 1 176 ? -6.12700  21.72100 30.09700 1.000 7.39475  ? 610  ASP   A O    1 
ATOM   1312 C  CB   . ASP   A 1 176 ? -6.06100  19.00800 29.24700 1.000 6.44431  ? 610  ASP   A CB   1 
ATOM   1313 C  CG   . ASP   A 1 176 ? -7.21700  18.56300 30.11600 1.000 6.93153  ? 610  ASP   A CG   1 
ATOM   1314 O  OD1  . ASP   A 1 176 ? -8.15500  19.35300 30.35100 1.000 8.40918  ? 610  ASP   A OD1  1 
ATOM   1315 O  OD2  . ASP   A 1 176 ? -7.18500  17.40500 30.57100 1.000 10.31491 ? 610  ASP   A OD2  1 
ATOM   1316 N  N    . TRP   A 1 177 ? -7.67400  22.23300 28.53900 1.000 8.39056  ? 611  TRP   A N    1 
ATOM   1317 C  CA   . TRP   A 1 177 ? -8.06900  23.47800 29.18600 1.000 6.41684  ? 611  TRP   A CA   1 
ATOM   1318 C  C    . TRP   A 1 177 ? -9.33000  23.32700 30.02900 1.000 6.48337  ? 611  TRP   A C    1 
ATOM   1319 O  O    . TRP   A 1 177 ? -9.89700  24.33300 30.46300 1.000 15.06260 ? 611  TRP   A O    1 
ATOM   1320 C  CB   . TRP   A 1 177 ? -8.21900  24.60500 28.15100 1.000 6.47422  ? 611  TRP   A CB   1 
ATOM   1321 C  CG   . TRP   A 1 177 ? -9.42000  24.58200 27.21700 1.000 10.74544 ? 611  TRP   A CG   1 
ATOM   1322 C  CD1  . TRP   A 1 177 ? -10.71400 24.24200 27.51900 1.000 6.46669  ? 611  TRP   A CD1  1 
ATOM   1323 C  CD2  . TRP   A 1 177 ? -9.42200  24.95700 25.83300 1.000 9.42877  ? 611  TRP   A CD2  1 
ATOM   1324 N  NE1  . TRP   A 1 177 ? -11.51000 24.36900 26.40600 1.000 10.44487 ? 611  TRP   A NE1  1 
ATOM   1325 C  CE2  . TRP   A 1 177 ? -10.74200 24.80600 25.35800 1.000 15.70077 ? 611  TRP   A CE2  1 
ATOM   1326 C  CE3  . TRP   A 1 177 ? -8.43300  25.40000 24.94700 1.000 7.99496  ? 611  TRP   A CE3  1 
ATOM   1327 C  CZ2  . TRP   A 1 177 ? -11.09800 25.08500 24.04100 1.000 8.32328  ? 611  TRP   A CZ2  1 
ATOM   1328 C  CZ3  . TRP   A 1 177 ? -8.78800  25.67200 23.63500 1.000 14.76185 ? 611  TRP   A CZ3  1 
ATOM   1329 C  CH2  . TRP   A 1 177 ? -10.10900 25.51400 23.19700 1.000 11.66921 ? 611  TRP   A CH2  1 
ATOM   1330 N  N    . ASP   A 1 178 ? -9.78400  22.09500 30.25500 1.000 6.42716  ? 612  ASP   A N    1 
ATOM   1331 C  CA   . ASP   A 1 178 ? -10.71900 21.80800 31.33100 1.000 6.57266  ? 612  ASP   A CA   1 
ATOM   1332 C  C    . ASP   A 1 178 ? -10.14600 22.32000 32.65000 1.000 10.41224 ? 612  ASP   A C    1 
ATOM   1333 O  O    . ASP   A 1 178 ? -8.93000  22.30900 32.86500 1.000 6.76868  ? 612  ASP   A O    1 
ATOM   1334 C  CB   . ASP   A 1 178 ? -10.96700 20.29700 31.39100 1.000 6.55165  ? 612  ASP   A CB   1 
ATOM   1335 C  CG   . ASP   A 1 178 ? -12.13300 19.91300 32.27400 1.000 6.74956  ? 612  ASP   A CG   1 
ATOM   1336 O  OD1  . ASP   A 1 178 ? -12.10200 20.18600 33.49300 1.000 9.66933  ? 612  ASP   A OD1  1 
ATOM   1337 O  OD2  . ASP   A 1 178 ? -13.08600 19.31100 31.74000 1.000 7.36702  ? 612  ASP   A OD2  1 
ATOM   1338 N  N    . VAL   A 1 179 ? -11.02600 22.79000 33.54000 1.000 8.47676  ? 613  VAL   A N    1 
ATOM   1339 C  CA   . VAL   A 1 179 ? -10.54800 23.38200 34.78400 1.000 9.29406  ? 613  VAL   A CA   1 
ATOM   1340 C  C    . VAL   A 1 179 ? -9.89100  22.34400 35.68500 1.000 16.21006 ? 613  VAL   A C    1 
ATOM   1341 O  O    . VAL   A 1 179 ? -9.13600  22.70700 36.59400 1.000 16.30481 ? 613  VAL   A O    1 
ATOM   1342 C  CB   . VAL   A 1 179 ? -11.69700 24.10200 35.51800 1.000 12.62159 ? 613  VAL   A CB   1 
ATOM   1343 C  CG1  . VAL   A 1 179 ? -12.56600 23.10700 36.26900 1.000 15.60136 ? 613  VAL   A CG1  1 
ATOM   1344 C  CG2  . VAL   A 1 179 ? -11.15200 25.16000 36.46700 1.000 11.28275 ? 613  VAL   A CG2  1 
ATOM   1345 N  N    . HIS   A 1 180 ? -10.14200 21.06000 35.45100 1.000 11.49720 ? 614  HIS   A N    1 
ATOM   1346 C  CA   . HIS   A 1 180 ? -9.55400  19.99200 36.24300 1.000 9.53366  ? 614  HIS   A CA   1 
ATOM   1347 C  C    . HIS   A 1 180 ? -8.36900  19.36600 35.51500 1.000 7.66110  ? 614  HIS   A C    1 
ATOM   1348 O  O    . HIS   A 1 180 ? -8.34400  19.27400 34.28400 1.000 11.36121 ? 614  HIS   A O    1 
ATOM   1349 C  CB   . HIS   A 1 180 ? -10.59300 18.91500 36.56200 1.000 8.45905  ? 614  HIS   A CB   1 
ATOM   1350 C  CG   . HIS   A 1 180 ? -11.76500 19.41800 37.34800 1.000 18.55876 ? 614  HIS   A CG   1 
ATOM   1351 N  ND1  . HIS   A 1 180 ? -12.92300 19.86900 36.75300 1.000 9.78423  ? 614  HIS   A ND1  1 
ATOM   1352 C  CD2  . HIS   A 1 180 ? -11.95300 19.55100 38.68300 1.000 9.95614  ? 614  HIS   A CD2  1 
ATOM   1353 C  CE1  . HIS   A 1 180 ? -13.77700 20.25100 37.68600 1.000 9.89009  ? 614  HIS   A CE1  1 
ATOM   1354 N  NE2  . HIS   A 1 180 ? -13.21300 20.06500 38.86600 1.000 9.17568  ? 614  HIS   A NE2  1 
ATOM   1355 N  N    . HIS   A 1 181 ? -7.38600  18.93500 36.29600 1.000 7.46887  ? 615  HIS   A N    1 
ATOM   1356 C  CA   . HIS   A 1 181 ? -6.24200  18.22900 35.73800 1.000 9.44793  ? 615  HIS   A CA   1 
ATOM   1357 C  C    . HIS   A 1 181 ? -6.69400  16.90400 35.14500 1.000 7.41521  ? 615  HIS   A C    1 
ATOM   1358 O  O    . HIS   A 1 181 ? -7.44200  16.15000 35.77700 1.000 7.94029  ? 615  HIS   A O    1 
ATOM   1359 C  CB   . HIS   A 1 181 ? -5.19200  17.99200 36.82400 1.000 7.79520  ? 615  HIS   A CB   1 
ATOM   1360 C  CG   . HIS   A 1 181 ? -3.92000  17.38400 36.32000 1.000 7.86665  ? 615  HIS   A CG   1 
ATOM   1361 N  ND1  . HIS   A 1 181 ? -3.45600  16.16200 36.75500 1.000 8.84732  ? 615  HIS   A ND1  1 
ATOM   1362 C  CD2  . HIS   A 1 181 ? -3.00800  17.83600 35.42500 1.000 7.73314  ? 615  HIS   A CD2  1 
ATOM   1363 C  CE1  . HIS   A 1 181 ? -2.31300  15.88600 36.15200 1.000 8.27335  ? 615  HIS   A CE1  1 
ATOM   1364 N  NE2  . HIS   A 1 181 ? -2.01900  16.88500 35.33900 1.000 8.87277  ? 615  HIS   A NE2  1 
ATOM   1365 N  N    . GLY   A 1 182 ? -6.24800  16.62400 33.92600 1.000 7.24159  ? 616  GLY   A N    1 
ATOM   1366 C  CA   . GLY   A 1 182 ? -6.50800  15.33000 33.32600 1.000 11.87747 ? 616  GLY   A CA   1 
ATOM   1367 C  C    . GLY   A 1 182 ? -5.52100  14.29200 33.81300 1.000 10.94053 ? 616  GLY   A C    1 
ATOM   1368 O  O    . GLY   A 1 182 ? -4.53400  13.99800 33.13200 1.000 16.00510 ? 616  GLY   A O    1 
ATOM   1369 N  N    . ASN   A 1 183 ? -5.77300  13.74400 35.00500 1.000 13.88885 ? 617  ASN   A N    1 
ATOM   1370 C  CA   . ASN   A 1 183 ? -4.82500  12.81800 35.62000 1.000 14.81567 ? 617  ASN   A CA   1 
ATOM   1371 C  C    . ASN   A 1 183 ? -4.61100  11.58500 34.75500 1.000 11.77332 ? 617  ASN   A C    1 
ATOM   1372 O  O    . ASN   A 1 183 ? -3.48500  11.09200 34.63000 1.000 11.96680 ? 617  ASN   A O    1 
ATOM   1373 C  CB   . ASN   A 1 183 ? -5.31400  12.41900 37.01300 1.000 11.27806 ? 617  ASN   A CB   1 
ATOM   1374 C  CG   . ASN   A 1 183 ? -6.74800  11.90600 37.00600 1.000 10.48831 ? 617  ASN   A CG   1 
ATOM   1375 O  OD1  . ASN   A 1 183 ? -7.68500  12.67400 36.83400 1.000 10.11529 ? 617  ASN   A OD1  1 
ATOM   1376 N  ND2  . ASN   A 1 183 ? -6.91800  10.60500 37.20600 1.000 11.84934 ? 617  ASN   A ND2  1 
ATOM   1377 N  N    . GLY   A 1 184 ? -5.67800  11.07700 34.13900 1.000 11.89967 ? 618  GLY   A N    1 
ATOM   1378 C  CA   . GLY   A 1 184 ? -5.53900  9.88900  33.31400 1.000 13.53609 ? 618  GLY   A CA   1 
ATOM   1379 C  C    . GLY   A 1 184 ? -4.72700  10.13400 32.05700 1.000 11.19349 ? 618  GLY   A C    1 
ATOM   1380 O  O    . GLY   A 1 184 ? -3.91500  9.29600  31.66200 1.000 11.24079 ? 618  GLY   A O    1 
ATOM   1381 N  N    . THR   A 1 185 ? -4.94100  11.27800 31.40200 1.000 14.37839 ? 619  THR   A N    1 
ATOM   1382 C  CA   . THR   A 1 185 ? -4.18000  11.58600 30.19600 1.000 10.60056 ? 619  THR   A CA   1 
ATOM   1383 C  C    . THR   A 1 185 ? -2.69700  11.75000 30.51700 1.000 10.37280 ? 619  THR   A C    1 
ATOM   1384 O  O    . THR   A 1 185 ? -1.83400  11.22500 29.80500 1.000 8.60907  ? 619  THR   A O    1 
ATOM   1385 C  CB   . THR   A 1 185 ? -4.73500  12.84200 29.52900 1.000 7.73454  ? 619  THR   A CB   1 
ATOM   1386 O  OG1  . THR   A 1 185 ? -6.16800  12.78500 29.52300 1.000 15.91928 ? 619  THR   A OG1  1 
ATOM   1387 C  CG2  . THR   A 1 185 ? -4.24500  12.93500 28.09800 1.000 7.58732  ? 619  THR   A CG2  1 
ATOM   1388 N  N    . GLN   A 1 186 ? -2.38200  12.47000 31.59800 1.000 13.56230 ? 620  GLN   A N    1 
ATOM   1389 C  CA   . GLN   A 1 186 ? -0.99100  12.58800 32.02800 1.000 8.57376  ? 620  GLN   A CA   1 
ATOM   1390 C  C    . GLN   A 1 186 ? -0.37400  11.21800 32.28200 1.000 10.14595 ? 620  GLN   A C    1 
ATOM   1391 O  O    . GLN   A 1 186 ? 0.74400   10.93700 31.83700 1.000 14.57172 ? 620  GLN   A O    1 
ATOM   1392 C  CB   . GLN   A 1 186 ? -0.89100  13.45000 33.28400 1.000 10.23393 ? 620  GLN   A CB   1 
ATOM   1393 C  CG   . GLN   A 1 186 ? 0.44700   13.30000 34.00300 1.000 10.48862 ? 620  GLN   A CG   1 
ATOM   1394 C  CD   . GLN   A 1 186 ? 0.60000   14.22500 35.19500 1.000 9.13935  ? 620  GLN   A CD   1 
ATOM   1395 O  OE1  . GLN   A 1 186 ? 0.48400   15.44300 35.07200 1.000 10.59366 ? 620  GLN   A OE1  1 
ATOM   1396 N  NE2  . GLN   A 1 186 ? 0.88000   13.64800 36.35500 1.000 9.46084  ? 620  GLN   A NE2  1 
ATOM   1397 N  N    . HIS   A 1 187 ? -1.09200  10.34600 32.99200 1.000 9.40262  ? 621  HIS   A N    1 
ATOM   1398 C  CA   . HIS   A 1 187 ? -0.51300  9.06100  33.37100 1.000 10.08160 ? 621  HIS   A CA   1 
ATOM   1399 C  C    . HIS   A 1 187 ? -0.35500  8.14000  32.17000 1.000 15.26526 ? 621  HIS   A C    1 
ATOM   1400 O  O    . HIS   A 1 187 ? 0.61600   7.37800  32.08900 1.000 15.63796 ? 621  HIS   A O    1 
ATOM   1401 C  CB   . HIS   A 1 187 ? -1.36900  8.39900  34.44800 1.000 10.32817 ? 621  HIS   A CB   1 
ATOM   1402 C  CG   . HIS   A 1 187 ? -1.31500  9.09500  35.77200 1.000 10.31280 ? 621  HIS   A CG   1 
ATOM   1403 N  ND1  . HIS   A 1 187 ? -2.37200  9.10200  36.65500 1.000 15.25430 ? 621  HIS   A ND1  1 
ATOM   1404 C  CD2  . HIS   A 1 187 ? -0.32500  9.80300  36.36500 1.000 10.39425 ? 621  HIS   A CD2  1 
ATOM   1405 C  CE1  . HIS   A 1 187 ? -2.03800  9.78800  37.73300 1.000 11.16037 ? 621  HIS   A CE1  1 
ATOM   1406 N  NE2  . HIS   A 1 187 ? -0.80000  10.22300 37.58300 1.000 14.80281 ? 621  HIS   A NE2  1 
ATOM   1407 N  N    . ILE   A 1 188 ? -1.29700  8.19100  31.22800 1.000 9.99239  ? 622  ILE   A N    1 
ATOM   1408 C  CA   . ILE   A 1 188 ? -1.23700  7.29700  30.07800 1.000 10.30758 ? 622  ILE   A CA   1 
ATOM   1409 C  C    . ILE   A 1 188 ? -0.02900  7.62300  29.20800 1.000 14.07011 ? 622  ILE   A C    1 
ATOM   1410 O  O    . ILE   A 1 188 ? 0.62300   6.72200  28.66600 1.000 11.00473 ? 622  ILE   A O    1 
ATOM   1411 C  CB   . ILE   A 1 188 ? -2.56100  7.35500  29.29100 1.000 12.62318 ? 622  ILE   A CB   1 
ATOM   1412 C  CG1  . ILE   A 1 188 ? -3.65700  6.61700  30.06600 1.000 13.99644 ? 622  ILE   A CG1  1 
ATOM   1413 C  CG2  . ILE   A 1 188 ? -2.40300  6.74600  27.90000 1.000 10.20260 ? 622  ILE   A CG2  1 
ATOM   1414 C  CD1  . ILE   A 1 188 ? -5.07100  6.92000  29.59800 1.000 15.19528 ? 622  ILE   A CD1  1 
ATOM   1415 N  N    . PHE   A 1 189 ? 0.31800   8.90500  29.09100 1.000 9.95168  ? 623  PHE   A N    1 
ATOM   1416 C  CA   . PHE   A 1 189 ? 1.41800   9.32800  28.23200 1.000 12.84313 ? 623  PHE   A CA   1 
ATOM   1417 C  C    . PHE   A 1 189 ? 2.64000   9.82100  29.00300 1.000 19.28741 ? 623  PHE   A C    1 
ATOM   1418 O  O    . PHE   A 1 189 ? 3.52100   10.44500 28.40100 1.000 19.05054 ? 623  PHE   A O    1 
ATOM   1419 C  CB   . PHE   A 1 189 ? 0.94500   10.42500 27.27500 1.000 10.01065 ? 623  PHE   A CB   1 
ATOM   1420 C  CG   . PHE   A 1 189 ? -0.19100  10.01200 26.39400 1.000 9.35194  ? 623  PHE   A CG   1 
ATOM   1421 C  CD1  . PHE   A 1 189 ? 0.01600   9.13500  25.34300 1.000 9.79051  ? 623  PHE   A CD1  1 
ATOM   1422 C  CD2  . PHE   A 1 189 ? -1.46500  10.50800 26.60900 1.000 9.01866  ? 623  PHE   A CD2  1 
ATOM   1423 C  CE1  . PHE   A 1 189 ? -1.02700  8.75300  24.52100 1.000 10.76827 ? 623  PHE   A CE1  1 
ATOM   1424 C  CE2  . PHE   A 1 189 ? -2.51400  10.13500 25.79300 1.000 16.96392 ? 623  PHE   A CE2  1 
ATOM   1425 C  CZ   . PHE   A 1 189 ? -2.29500  9.25500  24.74400 1.000 9.87779  ? 623  PHE   A CZ   1 
ATOM   1426 N  N    . GLU   A 1 190 ? 2.73000   9.54500  30.30900 1.000 12.89281 ? 624  GLU   A N    1 
ATOM   1427 C  CA   . GLU   A 1 190 ? 3.78600   10.15200 31.11600 1.000 15.40162 ? 624  GLU   A CA   1 
ATOM   1428 C  C    . GLU   A 1 190 ? 5.17800   9.75400  30.63600 1.000 16.05908 ? 624  GLU   A C    1 
ATOM   1429 O  O    . GLU   A 1 190 ? 6.11500   10.55500 30.72400 1.000 13.43041 ? 624  GLU   A O    1 
ATOM   1430 C  CB   . GLU   A 1 190 ? 3.60600   9.78800  32.59100 1.000 11.37808 ? 624  GLU   A CB   1 
ATOM   1431 C  CG   . GLU   A 1 190 ? 4.18600   10.82900 33.54200 1.000 21.29051 ? 624  GLU   A CG   1 
ATOM   1432 C  CD   . GLU   A 1 190 ? 3.67200   10.68800 34.96500 1.000 17.36214 ? 624  GLU   A CD   1 
ATOM   1433 O  OE1  . GLU   A 1 190 ? 3.07300   9.63900  35.28300 1.000 20.28285 ? 624  GLU   A OE1  1 
ATOM   1434 O  OE2  . GLU   A 1 190 ? 3.86500   11.63000 35.76100 1.000 22.40592 ? 624  GLU   A OE2  1 
ATOM   1435 N  N    . GLU   A 1 191 ? 5.33500   8.53600  30.11700 1.000 16.38679 ? 625  GLU   A N    1 
ATOM   1436 C  CA   . GLU   A 1 191 ? 6.61600   8.05200  29.61600 1.000 12.53243 ? 625  GLU   A CA   1 
ATOM   1437 C  C    . GLU   A 1 191 ? 6.70000   8.09500  28.09400 1.000 15.75360 ? 625  GLU   A C    1 
ATOM   1438 O  O    . GLU   A 1 191 ? 7.44100   7.31200  27.49200 1.000 21.51240 ? 625  GLU   A O    1 
ATOM   1439 C  CB   . GLU   A 1 191 ? 6.87500   6.63100  30.11400 1.000 14.27707 ? 625  GLU   A CB   1 
ATOM   1440 C  CG   . GLU   A 1 191 ? 7.79200   6.55000  31.31700 1.000 23.78414 ? 625  GLU   A CG   1 
ATOM   1441 C  CD   . GLU   A 1 191 ? 8.16600   5.12300  31.66100 1.000 33.96932 ? 625  GLU   A CD   1 
ATOM   1442 O  OE1  . GLU   A 1 191 ? 7.26000   4.26300  31.70600 1.000 33.70979 ? 625  GLU   A OE1  1 
ATOM   1443 O  OE2  . GLU   A 1 191 ? 9.36900   4.86000  31.87200 1.000 43.64997 ? 625  GLU   A OE2  1 
ATOM   1444 N  N    . ASP   A 1 192 ? 5.97200   9.00800  27.46000 1.000 15.14415 ? 626  ASP   A N    1 
ATOM   1445 C  CA   . ASP   A 1 192 ? 5.79300   9.00000  26.01300 1.000 16.47094 ? 626  ASP   A CA   1 
ATOM   1446 C  C    . ASP   A 1 192 ? 6.22200   10.34400 25.44500 1.000 20.58597 ? 626  ASP   A C    1 
ATOM   1447 O  O    . ASP   A 1 192 ? 5.66000   11.38100 25.81200 1.000 13.96233 ? 626  ASP   A O    1 
ATOM   1448 C  CB   . ASP   A 1 192 ? 4.33300   8.70400  25.65900 1.000 11.97603 ? 626  ASP   A CB   1 
ATOM   1449 C  CG   . ASP   A 1 192 ? 4.13400   8.39700  24.18800 1.000 12.89853 ? 626  ASP   A CG   1 
ATOM   1450 O  OD1  . ASP   A 1 192 ? 5.10200   8.48300  23.40800 1.000 19.14256 ? 626  ASP   A OD1  1 
ATOM   1451 O  OD2  . ASP   A 1 192 ? 2.99900   8.05900  23.81000 1.000 12.68007 ? 626  ASP   A OD2  1 
ATOM   1452 N  N    . ASP   A 1 193 ? 7.20600   10.32400 24.54600 1.000 12.71379 ? 627  ASP   A N    1 
ATOM   1453 C  CA   . ASP   A 1 193 ? 7.64900   11.52800 23.85600 1.000 11.68559 ? 627  ASP   A CA   1 
ATOM   1454 C  C    . ASP   A 1 193 ? 6.95000   11.73900 22.51700 1.000 16.43273 ? 627  ASP   A C    1 
ATOM   1455 O  O    . ASP   A 1 193 ? 7.29800   12.68000 21.79500 1.000 21.19710 ? 627  ASP   A O    1 
ATOM   1456 C  CB   . ASP   A 1 193 ? 9.17200   11.49800 23.65300 1.000 21.92652 ? 627  ASP   A CB   1 
ATOM   1457 C  CG   . ASP   A 1 193 ? 9.65700   10.24600 22.91800 1.000 20.12353 ? 627  ASP   A CG   1 
ATOM   1458 O  OD1  . ASP   A 1 193 ? 8.84100   9.53000  22.30300 1.000 16.19794 ? 627  ASP   A OD1  1 
ATOM   1459 O  OD2  . ASP   A 1 193 ? 10.87300  9.97300  22.96600 1.000 18.41487 ? 627  ASP   A OD2  1 
ATOM   1460 N  N    . SER   A 1 194 ? 5.98200   10.89200 22.16600 1.000 12.95218 ? 628  SER   A N    1 
ATOM   1461 C  CA   . SER   A 1 194 ? 5.21700   11.07100 20.93900 1.000 13.80520 ? 628  SER   A CA   1 
ATOM   1462 C  C    . SER   A 1 194 ? 3.91600   11.82600 21.15500 1.000 16.13804 ? 628  SER   A C    1 
ATOM   1463 O  O    . SER   A 1 194 ? 3.33900   12.32300 20.18200 1.000 11.29835 ? 628  SER   A O    1 
ATOM   1464 C  CB   . SER   A 1 194 ? 4.89600   9.71700  20.29600 1.000 11.75737 ? 628  SER   A CB   1 
ATOM   1465 O  OG   . SER   A 1 194 ? 3.82200   9.07400  20.95900 1.000 11.50629 ? 628  SER   A OG   1 
ATOM   1466 N  N    . VAL   A 1 195 ? 3.44000   11.92100 22.39300 1.000 14.73226 ? 629  VAL   A N    1 
ATOM   1467 C  CA   . VAL   A 1 195 ? 2.22700   12.66200 22.71600 1.000 13.48701 ? 629  VAL   A CA   1 
ATOM   1468 C  C    . VAL   A 1 195 ? 2.57300   13.69400 23.78000 1.000 10.42402 ? 629  VAL   A C    1 
ATOM   1469 O  O    . VAL   A 1 195 ? 2.99300   13.33800 24.88800 1.000 10.22568 ? 629  VAL   A O    1 
ATOM   1470 C  CB   . VAL   A 1 195 ? 1.09400   11.73700 23.19000 1.000 14.45457 ? 629  VAL   A CB   1 
ATOM   1471 C  CG1  . VAL   A 1 195 ? -0.12500  12.56000 23.59900 1.000 8.66086  ? 629  VAL   A CG1  1 
ATOM   1472 C  CG2  . VAL   A 1 195 ? 0.72800   10.75200 22.09200 1.000 9.80834  ? 629  VAL   A CG2  1 
ATOM   1473 N  N    . LEU   A 1 196 ? 2.40600   14.96700 23.43700 1.000 8.73729  ? 630  LEU   A N    1 
ATOM   1474 C  CA   . LEU   A 1 196 ? 2.68100   16.07300 24.34500 1.000 8.50134  ? 630  LEU   A CA   1 
ATOM   1475 C  C    . LEU   A 1 196 ? 1.39600   16.43900 25.08200 1.000 14.59236 ? 630  LEU   A C    1 
ATOM   1476 O  O    . LEU   A 1 196 ? 0.37900   16.74100 24.44900 1.000 7.91351  ? 630  LEU   A O    1 
ATOM   1477 C  CB   . LEU   A 1 196 ? 3.22600   17.27000 23.56600 1.000 8.51384  ? 630  LEU   A CB   1 
ATOM   1478 C  CG   . LEU   A 1 196 ? 3.53700   18.56100 24.32800 1.000 12.91131 ? 630  LEU   A CG   1 
ATOM   1479 C  CD1  . LEU   A 1 196 ? 4.65700   18.34200 25.33300 1.000 8.68535  ? 630  LEU   A CD1  1 
ATOM   1480 C  CD2  . LEU   A 1 196 ? 3.89600   19.67000 23.36000 1.000 8.43223  ? 630  LEU   A CD2  1 
ATOM   1481 N  N    . TYR   A 1 197 ? 1.43600   16.39300 26.41300 1.000 7.98722  ? 631  TYR   A N    1 
ATOM   1482 C  CA   . TYR   A 1 197 ? 0.28300   16.71000 27.24200 1.000 11.48709 ? 631  TYR   A CA   1 
ATOM   1483 C  C    . TYR   A 1 197 ? 0.49200   18.06000 27.90700 1.000 9.68172  ? 631  TYR   A C    1 
ATOM   1484 O  O    . TYR   A 1 197 ? 1.52400   18.29100 28.54700 1.000 11.72775 ? 631  TYR   A O    1 
ATOM   1485 C  CB   . TYR   A 1 197 ? 0.04200   15.63700 28.30400 1.000 12.13629 ? 631  TYR   A CB   1 
ATOM   1486 C  CG   . TYR   A 1 197 ? -1.20100  15.91200 29.10700 1.000 7.49539  ? 631  TYR   A CG   1 
ATOM   1487 C  CD1  . TYR   A 1 197 ? -2.43200  16.01300 28.48500 1.000 10.55197 ? 631  TYR   A CD1  1 
ATOM   1488 C  CD2  . TYR   A 1 197 ? -1.14500  16.08400 30.48000 1.000 12.97434 ? 631  TYR   A CD2  1 
ATOM   1489 C  CE1  . TYR   A 1 197 ? -3.57800  16.26900 29.20600 1.000 9.78800  ? 631  TYR   A CE1  1 
ATOM   1490 C  CE2  . TYR   A 1 197 ? -2.28800  16.34700 31.21200 1.000 11.48822 ? 631  TYR   A CE2  1 
ATOM   1491 C  CZ   . TYR   A 1 197 ? -3.50000  16.43500 30.56700 1.000 10.15139 ? 631  TYR   A CZ   1 
ATOM   1492 O  OH   . TYR   A 1 197 ? -4.64400  16.69000 31.28100 1.000 16.55392 ? 631  TYR   A OH   1 
ATOM   1493 N  N    . ILE   A 1 198 ? -0.48200  18.95100 27.74900 1.000 7.17747  ? 632  ILE   A N    1 
ATOM   1494 C  CA   . ILE   A 1 198 ? -0.41700  20.29500 28.30700 1.000 7.20706  ? 632  ILE   A CA   1 
ATOM   1495 C  C    . ILE   A 1 198 ? -1.75300  20.58100 28.96800 1.000 12.01534 ? 632  ILE   A C    1 
ATOM   1496 O  O    . ILE   A 1 198 ? -2.79300  20.57700 28.29800 1.000 6.83921  ? 632  ILE   A O    1 
ATOM   1497 C  CB   . ILE   A 1 198 ? -0.09800  21.35100 27.23600 1.000 7.11966  ? 632  ILE   A CB   1 
ATOM   1498 C  CG1  . ILE   A 1 198 ? 1.25200   21.04800 26.58200 1.000 7.63159  ? 632  ILE   A CG1  1 
ATOM   1499 C  CG2  . ILE   A 1 198 ? -0.10300  22.74200 27.84600 1.000 12.16559 ? 632  ILE   A CG2  1 
ATOM   1500 C  CD1  . ILE   A 1 198 ? 1.72300   22.10400 25.61400 1.000 13.94130 ? 632  ILE   A CD1  1 
ATOM   1501 N  N    . SER   A 1 199 ? -1.73200  20.81900 30.27700 1.000 13.95079 ? 633  SER   A N    1 
ATOM   1502 C  CA   . SER   A 1 199 ? -2.95100  20.99600 31.05200 1.000 7.44086  ? 633  SER   A CA   1 
ATOM   1503 C  C    . SER   A 1 199 ? -2.87200  22.27000 31.87900 1.000 8.00382  ? 633  SER   A C    1 
ATOM   1504 O  O    . SER   A 1 199 ? -1.91000  22.47600 32.62700 1.000 8.94321  ? 633  SER   A O    1 
ATOM   1505 C  CB   . SER   A 1 199 ? -3.19900  19.79200 31.96700 1.000 8.14316  ? 633  SER   A CB   1 
ATOM   1506 O  OG   . SER   A 1 199 ? -4.36000  19.98900 32.75400 1.000 7.34890  ? 633  SER   A OG   1 
ATOM   1507 N  N    . LEU   A 1 200 ? -3.87900  23.12300 31.73200 1.000 7.62394  ? 634  LEU   A N    1 
ATOM   1508 C  CA   . LEU   A 1 200 ? -4.12800  24.22200 32.65200 1.000 7.59325  ? 634  LEU   A CA   1 
ATOM   1509 C  C    . LEU   A 1 200 ? -5.27300  23.81000 33.56500 1.000 11.41381 ? 634  LEU   A C    1 
ATOM   1510 O  O    . LEU   A 1 200 ? -6.25600  23.21900 33.10600 1.000 13.42381 ? 634  LEU   A O    1 
ATOM   1511 C  CB   . LEU   A 1 200 ? -4.48000  25.51100 31.90400 1.000 7.16520  ? 634  LEU   A CB   1 
ATOM   1512 C  CG   . LEU   A 1 200 ? -3.68800  25.86000 30.64000 1.000 7.05125  ? 634  LEU   A CG   1 
ATOM   1513 C  CD1  . LEU   A 1 200 ? -4.34400  25.26400 29.39100 1.000 7.47605  ? 634  LEU   A CD1  1 
ATOM   1514 C  CD2  . LEU   A 1 200 ? -3.54900  27.36600 30.49200 1.000 7.30464  ? 634  LEU   A CD2  1 
ATOM   1515 N  N    . HIS   A 1 201 ? -5.14300  24.10100 34.85900 1.000 7.37253  ? 635  HIS   A N    1 
ATOM   1516 C  CA   . HIS   A 1 201 ? -6.10800  23.54100 35.79700 1.000 7.65969  ? 635  HIS   A CA   1 
ATOM   1517 C  C    . HIS   A 1 201 ? -5.99400  24.22600 37.15000 1.000 11.90250 ? 635  HIS   A C    1 
ATOM   1518 O  O    . HIS   A 1 201 ? -4.88900  24.53400 37.60400 1.000 8.09600  ? 635  HIS   A O    1 
ATOM   1519 C  CB   . HIS   A 1 201 ? -5.89700  22.02800 35.96600 1.000 7.43026  ? 635  HIS   A CB   1 
ATOM   1520 C  CG   . HIS   A 1 201 ? -4.46300  21.63800 36.13400 1.000 13.02218 ? 635  HIS   A CG   1 
ATOM   1521 N  ND1  . HIS   A 1 201 ? -3.64200  21.35000 35.06500 1.000 7.64660  ? 635  HIS   A ND1  1 
ATOM   1522 C  CD2  . HIS   A 1 201 ? -3.69500  21.50800 37.24200 1.000 14.44663 ? 635  HIS   A CD2  1 
ATOM   1523 C  CE1  . HIS   A 1 201 ? -2.43200  21.05600 35.50600 1.000 7.64035  ? 635  HIS   A CE1  1 
ATOM   1524 N  NE2  . HIS   A 1 201 ? -2.43900  21.14100 36.82400 1.000 9.08317  ? 635  HIS   A NE2  1 
ATOM   1525 N  N    . ARG   A 1 202 ? -7.14200  24.43700 37.78900 1.000 8.05997  ? 636  ARG   A N    1 
ATOM   1526 C  CA   . ARG   A 1 202 ? -7.16100  24.86500 39.18000 1.000 11.91629 ? 636  ARG   A CA   1 
ATOM   1527 C  C    . ARG   A 1 202 ? -6.58400  23.77000 40.07000 1.000 11.63174 ? 636  ARG   A C    1 
ATOM   1528 O  O    . ARG   A 1 202 ? -6.97800  22.60400 39.97700 1.000 11.81452 ? 636  ARG   A O    1 
ATOM   1529 C  CB   . ARG   A 1 202 ? -8.58900  25.20300 39.60400 1.000 18.99121 ? 636  ARG   A CB   1 
ATOM   1530 C  CG   . ARG   A 1 202 ? -8.70300  25.76100 41.00700 1.000 11.38137 ? 636  ARG   A CG   1 
ATOM   1531 C  CD   . ARG   A 1 202 ? -10.06600 26.39200 41.24300 1.000 12.64379 ? 636  ARG   A CD   1 
ATOM   1532 N  NE   . ARG   A 1 202 ? -10.11800 27.05800 42.53800 1.000 15.31997 ? 636  ARG   A NE   1 
ATOM   1533 C  CZ   . ARG   A 1 202 ? -11.19800 27.63700 43.04400 1.000 10.72482 ? 636  ARG   A CZ   1 
ATOM   1534 N  NH1  . ARG   A 1 202 ? -12.34900 27.64100 42.39200 1.000 10.59766 ? 636  ARG   A NH1  1 
ATOM   1535 N  NH2  . ARG   A 1 202 ? -11.12200 28.22200 44.23700 1.000 11.39047 ? 636  ARG   A NH2  1 
ATOM   1536 N  N    . TYR   A 1 203 ? -5.65200  24.15100 40.94000 1.000 14.36406 ? 637  TYR   A N    1 
ATOM   1537 C  CA   . TYR   A 1 203 ? -4.88500  23.19500 41.73100 1.000 13.13506 ? 637  TYR   A CA   1 
ATOM   1538 C  C    . TYR   A 1 203 ? -5.09400  23.38300 43.22700 1.000 10.27569 ? 637  TYR   A C    1 
ATOM   1539 O  O    . TYR   A 1 203 ? -5.53800  22.44800 43.90300 1.000 12.46862 ? 637  TYR   A O    1 
ATOM   1540 C  CB   . TYR   A 1 203 ? -3.40200  23.32200 41.36400 1.000 9.29499  ? 637  TYR   A CB   1 
ATOM   1541 C  CG   . TYR   A 1 203 ? -2.46700  22.38600 42.09500 1.000 9.61203  ? 637  TYR   A CG   1 
ATOM   1542 C  CD1  . TYR   A 1 203 ? -2.65300  21.01000 42.05300 1.000 9.55013  ? 637  TYR   A CD1  1 
ATOM   1543 C  CD2  . TYR   A 1 203 ? -1.38000  22.88200 42.80800 1.000 15.56060 ? 637  TYR   A CD2  1 
ATOM   1544 C  CE1  . TYR   A 1 203 ? -1.79200  20.15500 42.71800 1.000 9.93458  ? 637  TYR   A CE1  1 
ATOM   1545 C  CE2  . TYR   A 1 203 ? -0.51400  22.03700 43.47600 1.000 14.18749 ? 637  TYR   A CE2  1 
ATOM   1546 C  CZ   . TYR   A 1 203 ? -0.72300  20.67700 43.42700 1.000 14.39684 ? 637  TYR   A CZ   1 
ATOM   1547 O  OH   . TYR   A 1 203 ? 0.14300   19.83700 44.08800 1.000 12.69915 ? 637  TYR   A OH   1 
ATOM   1548 N  N    . GLU   A 1 204 ? -4.76700  24.55900 43.76500 1.000 10.26461 ? 638  GLU   A N    1 
ATOM   1549 C  CA   . GLU   A 1 204 ? -4.98000  24.88800 45.17500 1.000 10.92248 ? 638  GLU   A CA   1 
ATOM   1550 C  C    . GLU   A 1 204 ? -4.22700  23.92800 46.09600 1.000 16.90005 ? 638  GLU   A C    1 
ATOM   1551 O  O    . GLU   A 1 204 ? -4.78700  23.38100 47.04800 1.000 17.58763 ? 638  GLU   A O    1 
ATOM   1552 C  CB   . GLU   A 1 204 ? -6.47500  24.91200 45.51300 1.000 18.83784 ? 638  GLU   A CB   1 
ATOM   1553 C  CG   . GLU   A 1 204 ? -7.33700  25.74100 44.56400 1.000 15.33649 ? 638  GLU   A CG   1 
ATOM   1554 C  CD   . GLU   A 1 204 ? -7.14600  27.23800 44.72900 1.000 14.51077 ? 638  GLU   A CD   1 
ATOM   1555 O  OE1  . GLU   A 1 204 ? -6.26600  27.65500 45.50300 1.000 15.89817 ? 638  GLU   A OE1  1 
ATOM   1556 O  OE2  . GLU   A 1 204 ? -7.88400  28.00700 44.08300 1.000 16.21675 ? 638  GLU   A OE2  1 
ATOM   1557 N  N    . ASP   A 1 205 ? -2.93600  23.73200 45.80800 1.000 11.28413 ? 639  ASP   A N    1 
ATOM   1558 C  CA   . ASP   A 1 205 ? -2.07000  22.85000 46.59900 1.000 14.58541 ? 639  ASP   A CA   1 
ATOM   1559 C  C    . ASP   A 1 205 ? -2.67500  21.45300 46.73700 1.000 12.11982 ? 639  ASP   A C    1 
ATOM   1560 O  O    . ASP   A 1 205 ? -2.50600  20.77600 47.75300 1.000 22.00794 ? 639  ASP   A O    1 
ATOM   1561 C  CB   . ASP   A 1 205 ? -1.77800  23.45600 47.97800 1.000 23.00561 ? 639  ASP   A CB   1 
ATOM   1562 C  CG   . ASP   A 1 205 ? -0.73300  22.67200 48.75700 1.000 24.80324 ? 639  ASP   A CG   1 
ATOM   1563 O  OD1  . ASP   A 1 205 ? 0.15400   22.06300 48.12200 1.000 30.95510 ? 639  ASP   A OD1  1 
ATOM   1564 O  OD2  . ASP   A 1 205 ? -0.82100  22.63800 50.00300 1.000 20.98789 ? 639  ASP   A OD2  1 
ATOM   1565 N  N    . GLY   A 1 206 ? -3.39900  21.00800 45.71500 1.000 18.48895 ? 640  GLY   A N    1 
ATOM   1566 C  CA   . GLY   A 1 206 ? -4.03000  19.70800 45.78100 1.000 16.21494 ? 640  GLY   A CA   1 
ATOM   1567 C  C    . GLY   A 1 206 ? -5.38500  19.67800 46.45100 1.000 16.84436 ? 640  GLY   A C    1 
ATOM   1568 O  O    . GLY   A 1 206 ? -5.93200  18.58800 46.64900 1.000 27.11812 ? 640  GLY   A O    1 
ATOM   1569 N  N    . ALA   A 1 207 ? -5.94900  20.83100 46.80900 1.000 12.57212 ? 641  ALA   A N    1 
ATOM   1570 C  CA   . ALA   A 1 207 ? -7.26800  20.86700 47.42700 1.000 11.67363 ? 641  ALA   A CA   1 
ATOM   1571 C  C    . ALA   A 1 207 ? -8.40300  20.78600 46.41500 1.000 15.22346 ? 641  ALA   A C    1 
ATOM   1572 O  O    . ALA   A 1 207 ? -9.56200  20.63500 46.81800 1.000 26.70798 ? 641  ALA   A O    1 
ATOM   1573 C  CB   . ALA   A 1 207 ? -7.42500  22.13800 48.26400 1.000 15.19841 ? 641  ALA   A CB   1 
ATOM   1574 N  N    . PHE   A 1 208 ? -8.10800  20.89000 45.12500 1.000 18.19004 ? 642  PHE   A N    1 
ATOM   1575 C  CA   . PHE   A 1 208 ? -9.11800  20.81700 44.08100 1.000 13.37298 ? 642  PHE   A CA   1 
ATOM   1576 C  C    . PHE   A 1 208 ? -9.09100  19.43900 43.43100 1.000 12.25089 ? 642  PHE   A C    1 
ATOM   1577 O  O    . PHE   A 1 208 ? -8.02600  18.84100 43.26900 1.000 20.66243 ? 642  PHE   A O    1 
ATOM   1578 C  CB   . PHE   A 1 208 ? -8.88400  21.89800 43.02500 1.000 12.28244 ? 642  PHE   A CB   1 
ATOM   1579 C  CG   . PHE   A 1 208 ? -10.13700 22.34500 42.33900 1.000 10.86748 ? 642  PHE   A CG   1 
ATOM   1580 C  CD1  . PHE   A 1 208 ? -11.07900 23.09700 43.02400 1.000 19.79289 ? 642  PHE   A CD1  1 
ATOM   1581 C  CD2  . PHE   A 1 208 ? -10.38200 22.01000 41.02100 1.000 8.97574  ? 642  PHE   A CD2  1 
ATOM   1582 C  CE1  . PHE   A 1 208 ? -12.24200 23.51200 42.40600 1.000 17.33549 ? 642  PHE   A CE1  1 
ATOM   1583 C  CE2  . PHE   A 1 208 ? -11.54200 22.42500 40.39400 1.000 15.11368 ? 642  PHE   A CE2  1 
ATOM   1584 C  CZ   . PHE   A 1 208 ? -12.47400 23.17600 41.09000 1.000 17.01383 ? 642  PHE   A CZ   1 
ATOM   1585 N  N    . PHE   A 1 209 ? -10.26500 18.94200 43.06500 1.000 13.76471 ? 643  PHE   A N    1 
ATOM   1586 C  CA   . PHE   A 1 209 ? -10.35700 17.66700 42.36800 1.000 14.19211 ? 643  PHE   A CA   1 
ATOM   1587 C  C    . PHE   A 1 209 ? -9.45300  17.68000 41.13300 1.000 21.10574 ? 643  PHE   A C    1 
ATOM   1588 O  O    . PHE   A 1 209 ? -9.37200  18.70100 40.43700 1.000 11.70799 ? 643  PHE   A O    1 
ATOM   1589 C  CB   . PHE   A 1 209 ? -11.81300 17.39500 41.97000 1.000 10.33814 ? 643  PHE   A CB   1 
ATOM   1590 C  CG   . PHE   A 1 209 ? -12.04000 16.03000 41.39300 1.000 9.39247  ? 643  PHE   A CG   1 
ATOM   1591 C  CD1  . PHE   A 1 209 ? -12.30600 14.95300 42.22200 1.000 9.87734  ? 643  PHE   A CD1  1 
ATOM   1592 C  CD2  . PHE   A 1 209 ? -11.97800 15.82100 40.02200 1.000 8.92247  ? 643  PHE   A CD2  1 
ATOM   1593 C  CE1  . PHE   A 1 209 ? -12.50400 13.69200 41.70100 1.000 9.90539  ? 643  PHE   A CE1  1 
ATOM   1594 C  CE2  . PHE   A 1 209 ? -12.17100 14.55800 39.49200 1.000 8.94358  ? 643  PHE   A CE2  1 
ATOM   1595 C  CZ   . PHE   A 1 209 ? -12.43600 13.49200 40.33500 1.000 14.73782 ? 643  PHE   A CZ   1 
ATOM   1596 N  N    . PRO   A 1 210 ? -8.76500  16.56900 40.81600 1.000 12.25716 ? 644  PRO   A N    1 
ATOM   1597 C  CA   . PRO   A 1 210 ? -8.78700  15.24200 41.46200 1.000 9.41703  ? 644  PRO   A CA   1 
ATOM   1598 C  C    . PRO   A 1 210 ? -7.86800  15.08500 42.67600 1.000 17.76695 ? 644  PRO   A C    1 
ATOM   1599 O  O    . PRO   A 1 210 ? -7.53900  13.96100 43.06000 1.000 14.02511 ? 644  PRO   A O    1 
ATOM   1600 C  CB   . PRO   A 1 210 ? -8.36100  14.31300 40.31700 1.000 13.64021 ? 644  PRO   A CB   1 
ATOM   1601 C  CG   . PRO   A 1 210 ? -7.41700  15.15000 39.51300 1.000 8.79321  ? 644  PRO   A CG   1 
ATOM   1602 C  CD   . PRO   A 1 210 ? -7.98000  16.55000 39.56900 1.000 10.19184 ? 644  PRO   A CD   1 
ATOM   1603 N  N    . ASN   A 1 211 ? -7.42900  16.19400 43.27500 1.000 17.15409 ? 645  ASN   A N    1 
ATOM   1604 C  CA   . ASN   A 1 211 ? -6.84500  16.20800 44.62200 1.000 14.00159 ? 645  ASN   A CA   1 
ATOM   1605 C  C    . ASN   A 1 211 ? -5.54800  15.40300 44.70800 1.000 14.50203 ? 645  ASN   A C    1 
ATOM   1606 O  O    . ASN   A 1 211 ? -5.36500  14.57100 45.59700 1.000 18.73082 ? 645  ASN   A O    1 
ATOM   1607 C  CB   . ASN   A 1 211 ? -7.86100  15.70900 45.65000 1.000 15.04954 ? 645  ASN   A CB   1 
ATOM   1608 C  CG   . ASN   A 1 211 ? -9.12300  16.54000 45.66200 1.000 15.58711 ? 645  ASN   A CG   1 
ATOM   1609 O  OD1  . ASN   A 1 211 ? -10.15000 16.14000 45.11200 1.000 16.33198 ? 645  ASN   A OD1  1 
ATOM   1610 N  ND2  . ASN   A 1 211 ? -9.05100  17.71000 46.28100 1.000 25.69459 ? 645  ASN   A ND2  1 
ATOM   1611 N  N    . SER   A 1 212 ? -4.62900  15.67600 43.78800 1.000 18.02472 ? 646  SER   A N    1 
ATOM   1612 C  CA   . SER   A 1 212 ? -3.34500  14.99500 43.77700 1.000 10.73380 ? 646  SER   A CA   1 
ATOM   1613 C  C    . SER   A 1 212 ? -2.25600  15.96900 43.36500 1.000 10.54290 ? 646  SER   A C    1 
ATOM   1614 O  O    . SER   A 1 212 ? -2.46600  16.82200 42.49700 1.000 10.04080 ? 646  SER   A O    1 
ATOM   1615 C  CB   . SER   A 1 212 ? -3.35300  13.79100 42.82700 1.000 11.98723 ? 646  SER   A CB   1 
ATOM   1616 O  OG   . SER   A 1 212 ? -2.09300  13.14300 42.83200 1.000 11.30567 ? 646  SER   A OG   1 
ATOM   1617 N  N    . GLU   A 1 213 ? -1.09000  15.83700 43.99200 1.000 11.28154 ? 647  GLU   A N    1 
ATOM   1618 C  CA   . GLU   A 1 213 ? 0.05300   16.64300 43.59400 1.000 11.96450 ? 647  GLU   A CA   1 
ATOM   1619 C  C    . GLU   A 1 213 ? 0.65900   16.19600 42.27000 1.000 15.65496 ? 647  GLU   A C    1 
ATOM   1620 O  O    . GLU   A 1 213 ? 1.62700   16.81700 41.81700 1.000 16.29916 ? 647  GLU   A O    1 
ATOM   1621 C  CB   . GLU   A 1 213 ? 1.11400   16.61800 44.69300 1.000 12.67669 ? 647  GLU   A CB   1 
ATOM   1622 C  CG   . GLU   A 1 213 ? 0.57400   17.00900 46.05200 1.000 12.05314 ? 647  GLU   A CG   1 
ATOM   1623 C  CD   . GLU   A 1 213 ? 1.64400   17.03600 47.11300 1.000 24.79782 ? 647  GLU   A CD   1 
ATOM   1624 O  OE1  . GLU   A 1 213 ? 2.48300   17.96000 47.08600 1.000 33.00464 ? 647  GLU   A OE1  1 
ATOM   1625 O  OE2  . GLU   A 1 213 ? 1.64900   16.12500 47.96700 1.000 22.30055 ? 647  GLU   A OE2  1 
ATOM   1626 N  N    . ASP   A 1 214 ? 0.12400   15.14100 41.64400 1.000 10.47288 ? 648  ASP   A N    1 
ATOM   1627 C  CA   . ASP   A 1 214 ? 0.51900   14.80700 40.28000 1.000 12.96002 ? 648  ASP   A CA   1 
ATOM   1628 C  C    . ASP   A 1 214 ? 0.25900   15.95900 39.31700 1.000 10.26599 ? 648  ASP   A C    1 
ATOM   1629 O  O    . ASP   A 1 214 ? 0.85400   15.99600 38.23500 1.000 18.54251 ? 648  ASP   A O    1 
ATOM   1630 C  CB   . ASP   A 1 214 ? -0.23100  13.56200 39.79300 1.000 11.42424 ? 648  ASP   A CB   1 
ATOM   1631 C  CG   . ASP   A 1 214 ? 0.12700   12.31400 40.57800 1.000 16.29774 ? 648  ASP   A CG   1 
ATOM   1632 O  OD1  . ASP   A 1 214 ? 1.06300   12.36800 41.40200 1.000 11.29976 ? 648  ASP   A OD1  1 
ATOM   1633 O  OD2  . ASP   A 1 214 ? -0.53800  11.27400 40.37000 1.000 21.46490 ? 648  ASP   A OD2  1 
ATOM   1634 N  N    . ALA   A 1 215 ? -0.61000  16.89400 39.68800 1.000 11.10231 ? 649  ALA   A N    1 
ATOM   1635 C  CA   . ALA   A 1 215 ? -0.99500  18.01400 38.84400 1.000 10.47648 ? 649  ALA   A CA   1 
ATOM   1636 C  C    . ALA   A 1 215 ? -0.07500  19.22200 38.97600 1.000 12.17649 ? 649  ALA   A C    1 
ATOM   1637 O  O    . ALA   A 1 215 ? -0.33000  20.24600 38.33600 1.000 12.17237 ? 649  ALA   A O    1 
ATOM   1638 C  CB   . ALA   A 1 215 ? -2.43100  18.43100 39.17000 1.000 9.90933  ? 649  ALA   A CB   1 
ATOM   1639 N  N    . ASN   A 1 216 ? 0.97700   19.14600 39.78100 1.000 9.45924  ? 650  ASN   A N    1 
ATOM   1640 C  CA   . ASN   A 1 216 ? 1.77300   20.34200 39.99500 1.000 9.89730  ? 650  ASN   A CA   1 
ATOM   1641 C  C    . ASN   A 1 216 ? 2.76900   20.54300 38.85400 1.000 11.33566 ? 650  ASN   A C    1 
ATOM   1642 O  O    . ASN   A 1 216 ? 3.05100   19.63500 38.06800 1.000 12.77708 ? 650  ASN   A O    1 
ATOM   1643 C  CB   . ASN   A 1 216 ? 2.49800   20.27800 41.33800 1.000 10.84134 ? 650  ASN   A CB   1 
ATOM   1644 C  CG   . ASN   A 1 216 ? 2.73100   21.64700 41.92700 1.000 10.47168 ? 650  ASN   A CG   1 
ATOM   1645 O  OD1  . ASN   A 1 216 ? 2.37300   22.66000 41.32700 1.000 14.29298 ? 650  ASN   A OD1  1 
ATOM   1646 N  ND2  . ASN   A 1 216 ? 3.32000   21.68900 43.11200 1.000 16.50393 ? 650  ASN   A ND2  1 
ATOM   1647 N  N    . TYR   A 1 217 ? 3.30200   21.76500 38.77300 1.000 12.23812 ? 651  TYR   A N    1 
ATOM   1648 C  CA   . TYR   A 1 217 ? 4.17200   22.14000 37.66400 1.000 9.75322  ? 651  TYR   A CA   1 
ATOM   1649 C  C    . TYR   A 1 217 ? 5.43700   21.29100 37.59000 1.000 14.52930 ? 651  TYR   A C    1 
ATOM   1650 O  O    . TYR   A 1 217 ? 6.03500   21.18500 36.51300 1.000 12.69626 ? 651  TYR   A O    1 
ATOM   1651 C  CB   . TYR   A 1 217 ? 4.54800   23.62100 37.77300 1.000 9.74991  ? 651  TYR   A CB   1 
ATOM   1652 C  CG   . TYR   A 1 217 ? 5.35700   23.96600 39.00900 1.000 13.52884 ? 651  TYR   A CG   1 
ATOM   1653 C  CD1  . TYR   A 1 217 ? 6.74000   23.84200 39.01600 1.000 12.01947 ? 651  TYR   A CD1  1 
ATOM   1654 C  CD2  . TYR   A 1 217 ? 4.73900   24.42600 40.16400 1.000 11.99001 ? 651  TYR   A CD2  1 
ATOM   1655 C  CE1  . TYR   A 1 217 ? 7.48000   24.15300 40.14000 1.000 18.71743 ? 651  TYR   A CE1  1 
ATOM   1656 C  CE2  . TYR   A 1 217 ? 5.47400   24.74000 41.29200 1.000 15.00998 ? 651  TYR   A CE2  1 
ATOM   1657 C  CZ   . TYR   A 1 217 ? 6.84400   24.60000 41.27300 1.000 11.48786 ? 651  TYR   A CZ   1 
ATOM   1658 O  OH   . TYR   A 1 217 ? 7.58800   24.91100 42.39200 1.000 18.09623 ? 651  TYR   A OH   1 
ATOM   1659 N  N    . ASP   A 1 218 ? 5.86300   20.68700 38.69600 1.000 10.35790 ? 652  ASP   A N    1 
ATOM   1660 C  CA   . ASP   A 1 218 ? 7.11100   19.93700 38.70000 1.000 10.95938 ? 652  ASP   A CA   1 
ATOM   1661 C  C    . ASP   A 1 218 ? 6.96200   18.52100 38.14900 1.000 15.32302 ? 652  ASP   A C    1 
ATOM   1662 O  O    . ASP   A 1 218 ? 7.92900   17.75600 38.19400 1.000 18.98859 ? 652  ASP   A O    1 
ATOM   1663 C  CB   . ASP   A 1 218 ? 7.70700   19.89800 40.11500 1.000 11.47084 ? 652  ASP   A CB   1 
ATOM   1664 C  CG   . ASP   A 1 218 ? 6.87400   19.08600 41.09200 1.000 20.74352 ? 652  ASP   A CG   1 
ATOM   1665 O  OD1  . ASP   A 1 218 ? 5.62500   19.09300 40.99100 1.000 14.46894 ? 652  ASP   A OD1  1 
ATOM   1666 O  OD2  . ASP   A 1 218 ? 7.47900   18.44400 41.97800 1.000 28.99658 ? 652  ASP   A OD2  1 
ATOM   1667 N  N    . LYS   A 1 219 ? 5.79200   18.16000 37.62000 1.000 10.99239 ? 653  LYS   A N    1 
ATOM   1668 C  CA   . LYS   A 1 219 ? 5.57800   16.85400 36.99100 1.000 13.45260 ? 653  LYS   A CA   1 
ATOM   1669 C  C    . LYS   A 1 219 ? 5.77200   17.02500 35.48700 1.000 9.99826  ? 653  LYS   A C    1 
ATOM   1670 O  O    . LYS   A 1 219 ? 4.83700   17.34600 34.75200 1.000 9.49219  ? 653  LYS   A O    1 
ATOM   1671 C  CB   . LYS   A 1 219 ? 4.19300   16.30600 37.31800 1.000 15.72249 ? 653  LYS   A CB   1 
ATOM   1672 C  CG   . LYS   A 1 219 ? 4.15700   15.35100 38.50000 1.000 15.77162 ? 653  LYS   A CG   1 
ATOM   1673 C  CD   . LYS   A 1 219 ? 4.78000   15.97700 39.72600 1.000 10.91446 ? 653  LYS   A CD   1 
ATOM   1674 C  CE   . LYS   A 1 219 ? 4.57800   15.11700 40.95000 1.000 11.42002 ? 653  LYS   A CE   1 
ATOM   1675 N  NZ   . LYS   A 1 219 ? 4.72300   15.92600 42.19600 1.000 17.78253 ? 653  LYS   A NZ   1 
ATOM   1676 N  N    . VAL   A 1 220 ? 7.00300   16.79600 35.02300 1.000 10.39920 ? 654  VAL   A N    1 
ATOM   1677 C  CA   . VAL   A 1 220 ? 7.36700   17.07800 33.64000 1.000 10.25982 ? 654  VAL   A CA   1 
ATOM   1678 C  C    . VAL   A 1 220 ? 7.45300   15.82300 32.78600 1.000 12.92429 ? 654  VAL   A C    1 
ATOM   1679 O  O    . VAL   A 1 220 ? 7.83200   15.91000 31.61000 1.000 10.43914 ? 654  VAL   A O    1 
ATOM   1680 C  CB   . VAL   A 1 220 ? 8.69300   17.86100 33.57900 1.000 12.03646 ? 654  VAL   A CB   1 
ATOM   1681 C  CG1  . VAL   A 1 220 ? 8.59400   19.12300 34.43100 1.000 19.06779 ? 654  VAL   A CG1  1 
ATOM   1682 C  CG2  . VAL   A 1 220 ? 9.85200   16.99100 34.03800 1.000 13.40722 ? 654  VAL   A CG2  1 
ATOM   1683 N  N    . GLY   A 1 221 ? 7.11300   14.66500 33.32900 1.000 10.65104 ? 655  GLY   A N    1 
ATOM   1684 C  CA   . GLY   A 1 221 ? 7.19200   13.41700 32.60000 1.000 17.82828 ? 655  GLY   A CA   1 
ATOM   1685 C  C    . GLY   A 1 221 ? 8.20800   12.47300 33.21100 1.000 17.28782 ? 655  GLY   A C    1 
ATOM   1686 O  O    . GLY   A 1 221 ? 8.89600   12.79200 34.17900 1.000 21.10865 ? 655  GLY   A O    1 
ATOM   1687 N  N    . LEU   A 1 222 ? 8.28500   11.28200 32.61600 1.000 14.03085 ? 656  LEU   A N    1 
ATOM   1688 C  CA   . LEU   A 1 222 ? 9.16900   10.22500 33.08700 1.000 20.08524 ? 656  LEU   A CA   1 
ATOM   1689 C  C    . LEU   A 1 222 ? 9.87800   9.57900  31.90400 1.000 13.47026 ? 656  LEU   A C    1 
ATOM   1690 O  O    . LEU   A 1 222 ? 9.28500   9.41600  30.83500 1.000 17.39260 ? 656  LEU   A O    1 
ATOM   1691 C  CB   . LEU   A 1 222 ? 8.39200   9.15500  33.87100 1.000 13.63672 ? 656  LEU   A CB   1 
ATOM   1692 C  CG   . LEU   A 1 222 ? 7.61900   9.60500  35.11700 1.000 16.98883 ? 656  LEU   A CG   1 
ATOM   1693 C  CD1  . LEU   A 1 222 ? 6.90800   8.42500  35.75600 1.000 17.58608 ? 656  LEU   A CD1  1 
ATOM   1694 C  CD2  . LEU   A 1 222 ? 8.54800   10.27100 36.12100 1.000 13.17770 ? 656  LEU   A CD2  1 
ATOM   1695 N  N    . GLY   A 1 223 ? 11.14300  9.21000  32.10600 1.000 14.28590 ? 657  GLY   A N    1 
ATOM   1696 C  CA   . GLY   A 1 223 ? 11.88400  8.48900  31.08000 1.000 14.93029 ? 657  GLY   A CA   1 
ATOM   1697 C  C    . GLY   A 1 223 ? 11.98500  9.28400  29.79200 1.000 23.59477 ? 657  GLY   A C    1 
ATOM   1698 O  O    . GLY   A 1 223 ? 12.30100  10.48000 29.79300 1.000 19.66243 ? 657  GLY   A O    1 
ATOM   1699 N  N    . LYS   A 1 224 ? 11.69700  8.61300  28.67200 1.000 18.81390 ? 658  LYS   A N    1 
ATOM   1700 C  CA   . LYS   A 1 224 ? 11.70400  9.28200  27.37400 1.000 17.45931 ? 658  LYS   A CA   1 
ATOM   1701 C  C    . LYS   A 1 224 ? 10.75400  10.47400 27.34500 1.000 18.29286 ? 658  LYS   A C    1 
ATOM   1702 O  O    . LYS   A 1 224 ? 10.96800  11.41800 26.57600 1.000 17.27060 ? 658  LYS   A O    1 
ATOM   1703 C  CB   . LYS   A 1 224 ? 11.33300  8.28800  26.27200 1.000 19.56698 ? 658  LYS   A CB   1 
ATOM   1704 C  CG   . LYS   A 1 224 ? 12.28200  7.10800  26.14500 1.000 18.55068 ? 658  LYS   A CG   1 
ATOM   1705 C  CD   . LYS   A 1 224 ? 11.64300  5.97400  25.34600 1.000 22.13363 ? 658  LYS   A CD   1 
ATOM   1706 C  CE   . LYS   A 1 224 ? 12.61400  4.81900  25.14000 1.000 22.98945 ? 658  LYS   A CE   1 
ATOM   1707 N  NZ   . LYS   A 1 224 ? 13.73300  5.20000  24.23300 1.000 38.13558 ? 658  LYS   A NZ   1 
ATOM   1708 N  N    . GLY   A 1 225 ? 9.71400   10.45800 28.17900 1.000 12.84467 ? 659  GLY   A N    1 
ATOM   1709 C  CA   . GLY   A 1 225 ? 8.71100   11.49900 28.20400 1.000 11.96596 ? 659  GLY   A CA   1 
ATOM   1710 C  C    . GLY   A 1 225 ? 9.03200   12.72400 29.02300 1.000 11.69247 ? 659  GLY   A C    1 
ATOM   1711 O  O    . GLY   A 1 225 ? 8.17500   13.59900 29.14900 1.000 12.54358 ? 659  GLY   A O    1 
ATOM   1712 N  N    . ARG   A 1 226 ? 10.23300  12.83200 29.58500 1.000 15.30702 ? 660  ARG   A N    1 
ATOM   1713 C  CA   . ARG   A 1 226 ? 10.56400  14.00200 30.38900 1.000 12.80517 ? 660  ARG   A CA   1 
ATOM   1714 C  C    . ARG   A 1 226 ? 10.62700  15.24300 29.50700 1.000 14.61287 ? 660  ARG   A C    1 
ATOM   1715 O  O    . ARG   A 1 226 ? 11.25200  15.23600 28.44200 1.000 19.08671 ? 660  ARG   A O    1 
ATOM   1716 C  CB   . ARG   A 1 226 ? 11.88300  13.78500 31.13100 1.000 17.97638 ? 660  ARG   A CB   1 
ATOM   1717 C  CG   . ARG   A 1 226 ? 11.84400  12.56500 32.04100 1.000 21.41506 ? 660  ARG   A CG   1 
ATOM   1718 C  CD   . ARG   A 1 226 ? 12.97300  12.53300 33.04600 1.000 19.16222 ? 660  ARG   A CD   1 
ATOM   1719 N  NE   . ARG   A 1 226 ? 14.05000  13.44800 32.69400 1.000 23.47550 ? 660  ARG   A NE   1 
ATOM   1720 C  CZ   . ARG   A 1 226 ? 14.40000  14.50000 33.42000 1.000 23.29669 ? 660  ARG   A CZ   1 
ATOM   1721 N  NH1  . ARG   A 1 226 ? 13.78400  14.79000 34.55600 1.000 17.38377 ? 660  ARG   A NH1  1 
ATOM   1722 N  NH2  . ARG   A 1 226 ? 15.39500  15.27600 33.00000 1.000 17.14840 ? 660  ARG   A NH2  1 
ATOM   1723 N  N    . GLY   A 1 227 ? 9.97600   16.31100 29.95900 1.000 11.60663 ? 661  GLY   A N    1 
ATOM   1724 C  CA   . GLY   A 1 227 ? 9.74300   17.48500 29.15800 1.000 10.80163 ? 661  GLY   A CA   1 
ATOM   1725 C  C    . GLY   A 1 227 ? 8.42600   17.48100 28.41300 1.000 16.77105 ? 661  GLY   A C    1 
ATOM   1726 O  O    . GLY   A 1 227 ? 7.95600   18.54900 28.00400 1.000 10.70367 ? 661  GLY   A O    1 
ATOM   1727 N  N    . TYR   A 1 228 ? 7.80500   16.31200 28.24900 1.000 14.06165 ? 662  TYR   A N    1 
ATOM   1728 C  CA   . TYR   A 1 228 ? 6.62600   16.15500 27.41000 1.000 15.43975 ? 662  TYR   A CA   1 
ATOM   1729 C  C    . TYR   A 1 228 ? 5.33200   16.11600 28.21800 1.000 11.39212 ? 662  TYR   A C    1 
ATOM   1730 O  O    . TYR   A 1 228 ? 4.30900   15.63000 27.72100 1.000 16.27727 ? 662  TYR   A O    1 
ATOM   1731 C  CB   . TYR   A 1 228 ? 6.77100   14.90500 26.54100 1.000 15.13419 ? 662  TYR   A CB   1 
ATOM   1732 C  CG   . TYR   A 1 228 ? 7.87500   15.04000 25.51400 1.000 17.03287 ? 662  TYR   A CG   1 
ATOM   1733 C  CD1  . TYR   A 1 228 ? 9.20800   14.91500 25.87700 1.000 14.13890 ? 662  TYR   A CD1  1 
ATOM   1734 C  CD2  . TYR   A 1 228 ? 7.58400   15.31100 24.18500 1.000 15.51480 ? 662  TYR   A CD2  1 
ATOM   1735 C  CE1  . TYR   A 1 228 ? 10.21500  15.04600 24.94600 1.000 23.24422 ? 662  TYR   A CE1  1 
ATOM   1736 C  CE2  . TYR   A 1 228 ? 8.58400   15.44400 23.25000 1.000 15.23044 ? 662  TYR   A CE2  1 
ATOM   1737 C  CZ   . TYR   A 1 228 ? 9.89500   15.30900 23.63400 1.000 17.21594 ? 662  TYR   A CZ   1 
ATOM   1738 O  OH   . TYR   A 1 228 ? 10.89100  15.44200 22.69900 1.000 39.31971 ? 662  TYR   A OH   1 
ATOM   1739 N  N    . ASN   A 1 229 ? 5.35900   16.63200 29.44500 1.000 10.62266 ? 663  ASN   A N    1 
ATOM   1740 C  CA   . ASN   A 1 229 ? 4.16000   16.82700 30.25500 1.000 8.80432  ? 663  ASN   A CA   1 
ATOM   1741 C  C    . ASN   A 1 229 ? 4.28000   18.20300 30.88900 1.000 11.39091 ? 663  ASN   A C    1 
ATOM   1742 O  O    . ASN   A 1 229 ? 5.18200   18.43500 31.69700 1.000 10.29382 ? 663  ASN   A O    1 
ATOM   1743 C  CB   . ASN   A 1 229 ? 4.01700   15.74400 31.32300 1.000 9.05782  ? 663  ASN   A CB   1 
ATOM   1744 C  CG   . ASN   A 1 229 ? 2.68400   15.80500 32.04700 1.000 12.14723 ? 663  ASN   A CG   1 
ATOM   1745 O  OD1  . ASN   A 1 229 ? 1.73600   15.11700 31.67600 1.000 19.22940 ? 663  ASN   A OD1  1 
ATOM   1746 N  ND2  . ASN   A 1 229 ? 2.60900   16.62400 33.09300 1.000 8.67321  ? 663  ASN   A ND2  1 
ATOM   1747 N  N    . VAL   A 1 230 ? 3.38700   19.11600 30.52000 1.000 9.63950  ? 664  VAL   A N    1 
ATOM   1748 C  CA   . VAL   A 1 230 ? 3.43000   20.49800 30.98600 1.000 13.35244 ? 664  VAL   A CA   1 
ATOM   1749 C  C    . VAL   A 1 230 ? 2.17100   20.75100 31.80300 1.000 7.93791  ? 664  VAL   A C    1 
ATOM   1750 O  O    . VAL   A 1 230 ? 1.06300   20.79700 31.25200 1.000 7.60910  ? 664  VAL   A O    1 
ATOM   1751 C  CB   . VAL   A 1 230 ? 3.54600   21.49500 29.82500 1.000 8.10588  ? 664  VAL   A CB   1 
ATOM   1752 C  CG1  . VAL   A 1 230 ? 3.55300   22.92000 30.34700 1.000 8.13746  ? 664  VAL   A CG1  1 
ATOM   1753 C  CG2  . VAL   A 1 230 ? 4.79900   21.21900 29.00800 1.000 16.32069 ? 664  VAL   A CG2  1 
ATOM   1754 N  N    . ASN   A 1 231 ? 2.33700   20.90900 33.11300 1.000 8.16765  ? 665  ASN   A N    1 
ATOM   1755 C  CA   . ASN   A 1 231 ? 1.24000   21.23200 34.01400 1.000 15.62345 ? 665  ASN   A CA   1 
ATOM   1756 C  C    . ASN   A 1 231 ? 1.27200   22.71400 34.35200 1.000 11.24656 ? 665  ASN   A C    1 
ATOM   1757 O  O    . ASN   A 1 231 ? 2.31200   23.24300 34.75800 1.000 8.41359  ? 665  ASN   A O    1 
ATOM   1758 C  CB   . ASN   A 1 231 ? 1.31500   20.40900 35.30000 1.000 10.22211 ? 665  ASN   A CB   1 
ATOM   1759 C  CG   . ASN   A 1 231 ? 0.64700   19.06300 35.16800 1.000 8.21567  ? 665  ASN   A CG   1 
ATOM   1760 O  OD1  . ASN   A 1 231 ? -0.18700  18.85600 34.29100 1.000 7.89250  ? 665  ASN   A OD1  1 
ATOM   1761 N  ND2  . ASN   A 1 231 ? 1.00600   18.13800 36.04900 1.000 9.30464  ? 665  ASN   A ND2  1 
ATOM   1762 N  N    . ILE   A 1 232 ? 0.13200   23.37300 34.20000 1.000 8.85086  ? 666  ILE   A N    1 
ATOM   1763 C  CA   . ILE   A 1 232 ? -0.00200  24.78400 34.53900 1.000 7.99336  ? 666  ILE   A CA   1 
ATOM   1764 C  C    . ILE   A 1 232 ? -1.05600  24.88800 35.63500 1.000 10.55753 ? 666  ILE   A C    1 
ATOM   1765 O  O    . ILE   A 1 232 ? -2.25100  25.02600 35.33600 1.000 9.04894  ? 666  ILE   A O    1 
ATOM   1766 C  CB   . ILE   A 1 232 ? -0.35300  25.61600 33.29900 1.000 10.43288 ? 666  ILE   A CB   1 
ATOM   1767 C  CG1  . ILE   A 1 232 ? 0.70600   25.38300 32.21200 1.000 7.81528  ? 666  ILE   A CG1  1 
ATOM   1768 C  CG2  . ILE   A 1 232 ? -0.44600  27.08900 33.64100 1.000 8.06766  ? 666  ILE   A CG2  1 
ATOM   1769 C  CD1  . ILE   A 1 232 ? 0.44000   26.08700 30.90300 1.000 7.69861  ? 666  ILE   A CD1  1 
ATOM   1770 N  N    . PRO   A 1 233 ? -0.66500  24.79700 36.91100 1.000 8.49109  ? 667  PRO   A N    1 
ATOM   1771 C  CA   . PRO   A 1 233 ? -1.65800  24.75700 37.99300 1.000 10.00727 ? 667  PRO   A CA   1 
ATOM   1772 C  C    . PRO   A 1 233 ? -1.92400  26.13100 38.59200 1.000 8.85652  ? 667  PRO   A C    1 
ATOM   1773 O  O    . PRO   A 1 233 ? -0.99200  26.90200 38.82100 1.000 9.16933  ? 667  PRO   A O    1 
ATOM   1774 C  CB   . PRO   A 1 233 ? -0.99700  23.82400 39.01000 1.000 8.84305  ? 667  PRO   A CB   1 
ATOM   1775 C  CG   . PRO   A 1 233 ? 0.47400   24.13300 38.85900 1.000 10.30696 ? 667  PRO   A CG   1 
ATOM   1776 C  CD   . PRO   A 1 233 ? 0.69400   24.50400 37.39800 1.000 11.45868 ? 667  PRO   A CD   1 
ATOM   1777 N  N    . TRP   A 1 234 ? -3.19300  26.44800 38.85000 1.000 8.85335  ? 668  TRP   A N    1 
ATOM   1778 C  CA   . TRP   A 1 234 ? -3.57100  27.73800 39.40700 1.000 11.08347 ? 668  TRP   A CA   1 
ATOM   1779 C  C    . TRP   A 1 234 ? -3.81100  27.62100 40.90800 1.000 12.77249 ? 668  TRP   A C    1 
ATOM   1780 O  O    . TRP   A 1 234 ? -4.36500  26.62800 41.39000 1.000 9.65519  ? 668  TRP   A O    1 
ATOM   1781 C  CB   . TRP   A 1 234 ? -4.83800  28.29200 38.74200 1.000 12.22797 ? 668  TRP   A CB   1 
ATOM   1782 C  CG   . TRP   A 1 234 ? -4.81400  28.37200 37.23500 1.000 12.87247 ? 668  TRP   A CG   1 
ATOM   1783 C  CD1  . TRP   A 1 234 ? -5.62200  27.69200 36.36900 1.000 8.26602  ? 668  TRP   A CD1  1 
ATOM   1784 C  CD2  . TRP   A 1 234 ? -3.95500  29.19000 36.42400 1.000 8.94251  ? 668  TRP   A CD2  1 
ATOM   1785 N  NE1  . TRP   A 1 234 ? -5.31800  28.03200 35.07100 1.000 8.74474  ? 668  TRP   A NE1  1 
ATOM   1786 C  CE2  . TRP   A 1 234 ? -4.29700  28.94700 35.07700 1.000 9.88253  ? 668  TRP   A CE2  1 
ATOM   1787 C  CE3  . TRP   A 1 234 ? -2.92500  30.09300 36.70600 1.000 9.10144  ? 668  TRP   A CE3  1 
ATOM   1788 C  CZ2  . TRP   A 1 234 ? -3.64700  29.57600 34.01500 1.000 8.31062  ? 668  TRP   A CZ2  1 
ATOM   1789 C  CZ3  . TRP   A 1 234 ? -2.28400  30.72000 35.65100 1.000 11.32968 ? 668  TRP   A CZ3  1 
ATOM   1790 C  CH2  . TRP   A 1 234 ? -2.64600  30.45700 34.32200 1.000 8.69624  ? 668  TRP   A CH2  1 
ATOM   1791 N  N    . ASN   A 1 235 ? -3.41000  28.65200 41.64100 1.000 16.86567 ? 669  ASN   A N    1 
ATOM   1792 C  CA   . ASN   A 1 235 ? -3.64500  28.72500 43.07300 1.000 14.07770 ? 669  ASN   A CA   1 
ATOM   1793 C  C    . ASN   A 1 235 ? -4.30000  30.05800 43.40400 1.000 13.94365 ? 669  ASN   A C    1 
ATOM   1794 O  O    . ASN   A 1 235 ? -4.02900  31.07200 42.75800 1.000 16.98130 ? 669  ASN   A O    1 
ATOM   1795 C  CB   . ASN   A 1 235 ? -2.33800  28.56400 43.86000 1.000 11.18717 ? 669  ASN   A CB   1 
ATOM   1796 C  CG   . ASN   A 1 235 ? -1.62800  27.25400 43.54800 1.000 11.14426 ? 669  ASN   A CG   1 
ATOM   1797 O  OD1  . ASN   A 1 235 ? -2.21200  26.17400 43.65400 1.000 10.63841 ? 669  ASN   A OD1  1 
ATOM   1798 N  ND2  . ASN   A 1 235 ? -0.36100  27.34700 43.15300 1.000 10.86039 ? 669  ASN   A ND2  1 
ATOM   1799 N  N    . GLY   A 1 236 ? -5.19000  30.04400 44.39000 1.000 15.86318 ? 670  GLY   A N    1 
ATOM   1800 C  CA   . GLY   A 1 236 ? -5.74100  31.27800 44.91600 1.000 30.44946 ? 670  GLY   A CA   1 
ATOM   1801 C  C    . GLY   A 1 236 ? -6.87600  31.91900 44.13700 1.000 21.78719 ? 670  GLY   A C    1 
ATOM   1802 O  O    . GLY   A 1 236 ? -6.77500  33.08300 43.74300 1.000 19.06027 ? 670  GLY   A O    1 
ATOM   1803 N  N    . GLY   A 1 237 ? -7.95900  31.18500 43.91400 1.000 16.43092 ? 671  GLY   A N    1 
ATOM   1804 C  CA   . GLY   A 1 237 ? -9.20000  31.80100 43.48300 1.000 21.75609 ? 671  GLY   A CA   1 
ATOM   1805 C  C    . GLY   A 1 237 ? -9.35000  31.97400 41.98200 1.000 21.63715 ? 671  GLY   A C    1 
ATOM   1806 O  O    . GLY   A 1 237 ? -8.66300  31.35800 41.16400 1.000 13.79219 ? 671  GLY   A O    1 
ATOM   1807 N  N    . LYS   A 1 238 ? -10.27300 32.87300 41.62900 1.000 24.22452 ? 672  LYS   A N    1 
ATOM   1808 C  CA   . LYS   A 1 238 ? -10.81200 32.94300 40.27600 1.000 27.64039 ? 672  LYS   A CA   1 
ATOM   1809 C  C    . LYS   A 1 238 ? -9.75800  33.39100 39.26700 1.000 22.08478 ? 672  LYS   A C    1 
ATOM   1810 O  O    . LYS   A 1 238 ? -9.05100  34.37900 39.48000 1.000 27.17205 ? 672  LYS   A O    1 
ATOM   1811 C  CB   . LYS   A 1 238 ? -12.01700 33.89000 40.24300 1.000 16.74088 ? 672  LYS   A CB   1 
ATOM   1812 N  N    . MET   A 1 239 ? -9.65600  32.64900 38.17000 1.000 21.37481 ? 673  MET   A N    1 
ATOM   1813 C  CA   . MET   A 1 239 ? -8.84900  33.01200 37.01700 1.000 17.27101 ? 673  MET   A CA   1 
ATOM   1814 C  C    . MET   A 1 239 ? -9.76600  33.27700 35.83200 1.000 15.74644 ? 673  MET   A C    1 
ATOM   1815 O  O    . MET   A 1 239 ? -10.93000 32.87100 35.82400 1.000 15.28585 ? 673  MET   A O    1 
ATOM   1816 C  CB   . MET   A 1 239 ? -7.84500  31.90300 36.67500 1.000 14.49384 ? 673  MET   A CB   1 
ATOM   1817 C  CG   . MET   A 1 239 ? -6.91500  31.53000 37.82100 1.000 10.39286 ? 673  MET   A CG   1 
ATOM   1818 S  SD   . MET   A 1 239 ? -5.80100  32.87600 38.26200 1.000 13.46464 ? 673  MET   A SD   1 
ATOM   1819 C  CE   . MET   A 1 239 ? -5.07600  32.23700 39.77300 1.000 10.59177 ? 673  MET   A CE   1 
ATOM   1820 N  N    . GLY   A 1 240 ? -9.23000  33.95700 34.82100 1.000 19.90511 ? 674  GLY   A N    1 
ATOM   1821 C  CA   . GLY   A 1 240 ? -10.02500 34.30600 33.65800 1.000 10.55973 ? 674  GLY   A CA   1 
ATOM   1822 C  C    . GLY   A 1 240 ? -9.23700  34.43800 32.37000 1.000 12.96072 ? 674  GLY   A C    1 
ATOM   1823 O  O    . GLY   A 1 240 ? -8.13700  33.89000 32.25400 1.000 17.87217 ? 674  GLY   A O    1 
ATOM   1824 N  N    . ASP   A 1 241 ? -9.79800  35.16000 31.39700 1.000 10.28249 ? 675  ASP   A N    1 
ATOM   1825 C  CA   . ASP   A 1 241 ? -9.14800  35.32600 30.09800 1.000 11.26661 ? 675  ASP   A CA   1 
ATOM   1826 C  C    . ASP   A 1 241 ? -7.71400  35.83700 30.16600 1.000 15.69648 ? 675  ASP   A C    1 
ATOM   1827 O  O    . ASP   A 1 241 ? -6.87500  35.31700 29.41200 1.000 10.81307 ? 675  ASP   A O    1 
ATOM   1828 C  CB   . ASP   A 1 241 ? -9.95700  36.27900 29.21000 1.000 15.11535 ? 675  ASP   A CB   1 
ATOM   1829 C  CG   . ASP   A 1 241 ? -11.29800 35.72400 28.80300 1.000 15.20353 ? 675  ASP   A CG   1 
ATOM   1830 O  OD1  . ASP   A 1 241 ? -11.53500 34.50200 28.92800 1.000 11.39806 ? 675  ASP   A OD1  1 
ATOM   1831 O  OD2  . ASP   A 1 241 ? -12.11000 36.53800 28.33400 1.000 20.09747 ? 675  ASP   A OD2  1 
ATOM   1832 N  N    . PRO   A 1 242 ? -7.36700  36.85000 30.97200 1.000 14.70879 ? 676  PRO   A N    1 
ATOM   1833 C  CA   . PRO   A 1 242 ? -5.96700  37.30600 30.96800 1.000 14.78910 ? 676  PRO   A CA   1 
ATOM   1834 C  C    . PRO   A 1 242 ? -4.99500  36.23700 31.42000 1.000 10.33458 ? 676  PRO   A C    1 
ATOM   1835 O  O    . PRO   A 1 242 ? -3.91700  36.10100 30.83000 1.000 13.06837 ? 676  PRO   A O    1 
ATOM   1836 C  CB   . PRO   A 1 242 ? -5.97900  38.51300 31.91900 1.000 14.59905 ? 676  PRO   A CB   1 
ATOM   1837 C  CG   . PRO   A 1 242 ? -7.24700  38.40400 32.68700 1.000 17.87966 ? 676  PRO   A CG   1 
ATOM   1838 C  CD   . PRO   A 1 242 ? -8.22000  37.74600 31.77100 1.000 11.24716 ? 676  PRO   A CD   1 
ATOM   1839 N  N    . GLU   A 1 243 ? -5.35500  35.45900 32.44100 1.000 10.69193 ? 677  GLU   A N    1 
ATOM   1840 C  CA   . GLU   A 1 243 ? -4.47300  34.40100 32.91800 1.000 14.32570 ? 677  GLU   A CA   1 
ATOM   1841 C  C    . GLU   A 1 243 ? -4.28600  33.31600 31.86400 1.000 9.55633  ? 677  GLU   A C    1 
ATOM   1842 O  O    . GLU   A 1 243 ? -3.16900  32.83200 31.64600 1.000 14.98060 ? 677  GLU   A O    1 
ATOM   1843 C  CB   . GLU   A 1 243 ? -5.03300  33.80400 34.20900 1.000 11.22018 ? 677  GLU   A CB   1 
ATOM   1844 C  CG   . GLU   A 1 243 ? -4.88200  34.70600 35.43000 1.000 10.35724 ? 677  GLU   A CG   1 
ATOM   1845 C  CD   . GLU   A 1 243 ? -5.89200  35.83100 35.48800 1.000 17.83336 ? 677  GLU   A CD   1 
ATOM   1846 O  OE1  . GLU   A 1 243 ? -6.93700  35.73300 34.80800 1.000 18.05620 ? 677  GLU   A OE1  1 
ATOM   1847 O  OE2  . GLU   A 1 243 ? -5.63700  36.81400 36.22100 1.000 13.58380 ? 677  GLU   A OE2  1 
ATOM   1848 N  N    . TYR   A 1 244 ? -5.37000  32.91600 31.20400 1.000 19.01037 ? 678  TYR   A N    1 
ATOM   1849 C  CA   . TYR   A 1 244 ? -5.27000  31.85200 30.21300 1.000 10.73615 ? 678  TYR   A CA   1 
ATOM   1850 C  C    . TYR   A 1 244 ? -4.55000  32.32900 28.95800 1.000 10.23726 ? 678  TYR   A C    1 
ATOM   1851 O  O    . TYR   A 1 244 ? -3.77700  31.57400 28.35900 1.000 8.21927  ? 678  TYR   A O    1 
ATOM   1852 C  CB   . TYR   A 1 244 ? -6.66600  31.31000 29.89100 1.000 8.80382  ? 678  TYR   A CB   1 
ATOM   1853 C  CG   . TYR   A 1 244 ? -7.11600  30.27700 30.90000 1.000 7.91668  ? 678  TYR   A CG   1 
ATOM   1854 C  CD1  . TYR   A 1 244 ? -7.46600  30.64900 32.19000 1.000 11.36136 ? 678  TYR   A CD1  1 
ATOM   1855 C  CD2  . TYR   A 1 244 ? -7.16000  28.92900 30.57300 1.000 7.49998  ? 678  TYR   A CD2  1 
ATOM   1856 C  CE1  . TYR   A 1 244 ? -7.85700  29.71200 33.12200 1.000 9.30176  ? 678  TYR   A CE1  1 
ATOM   1857 C  CE2  . TYR   A 1 244 ? -7.55100  27.98400 31.49900 1.000 7.38052  ? 678  TYR   A CE2  1 
ATOM   1858 C  CZ   . TYR   A 1 244 ? -7.89600  28.38300 32.77400 1.000 12.81584 ? 678  TYR   A CZ   1 
ATOM   1859 O  OH   . TYR   A 1 244 ? -8.28800  27.45400 33.70700 1.000 9.53713  ? 678  TYR   A OH   1 
ATOM   1860 N  N    . MET   A 1 245 ? -4.77700  33.58100 28.55200 1.000 9.35272  ? 679  MET   A N    1 
ATOM   1861 C  CA   . MET   A 1 245 ? -4.07900  34.11500 27.38700 1.000 9.09450  ? 679  MET   A CA   1 
ATOM   1862 C  C    . MET   A 1 245 ? -2.58600  34.25300 27.65600 1.000 10.28911 ? 679  MET   A C    1 
ATOM   1863 O  O    . MET   A 1 245 ? -1.76500  33.96900 26.77800 1.000 13.60568 ? 679  MET   A O    1 
ATOM   1864 C  CB   . MET   A 1 245 ? -4.67600  35.46300 26.97900 1.000 9.68369  ? 679  MET   A CB   1 
ATOM   1865 C  CG   . MET   A 1 245 ? -6.08100  35.38100 26.39700 1.000 17.75405 ? 679  MET   A CG   1 
ATOM   1866 S  SD   . MET   A 1 245 ? -6.12800  34.68000 24.73500 1.000 27.69908 ? 679  MET   A SD   1 
ATOM   1867 C  CE   . MET   A 1 245 ? -5.37000  35.99600 23.78700 1.000 21.23083 ? 679  MET   A CE   1 
ATOM   1868 N  N    . ALA   A 1 246 ? -2.21100  34.68400 28.86500 1.000 9.53372  ? 680  ALA   A N    1 
ATOM   1869 C  CA   . ALA   A 1 246 ? -0.79500  34.81900 29.18600 1.000 11.73530 ? 680  ALA   A CA   1 
ATOM   1870 C  C    . ALA   A 1 246 ? -0.11900  33.45600 29.27500 1.000 12.29419 ? 680  ALA   A C    1 
ATOM   1871 O  O    . ALA   A 1 246 ? 1.04200   33.30300 28.87400 1.000 14.69187 ? 680  ALA   A O    1 
ATOM   1872 C  CB   . ALA   A 1 246 ? -0.61900  35.59900 30.49000 1.000 10.22866 ? 680  ALA   A CB   1 
ATOM   1873 N  N    . ALA   A 1 247 ? -0.83100  32.45100 29.78900 1.000 9.75372  ? 681  ALA   A N    1 
ATOM   1874 C  CA   . ALA   A 1 247 ? -0.27600  31.10300 29.81900 1.000 9.82221  ? 681  ALA   A CA   1 
ATOM   1875 C  C    . ALA   A 1 247 ? -0.06600  30.56700 28.40900 1.000 12.41239 ? 681  ALA   A C    1 
ATOM   1876 O  O    . ALA   A 1 247 ? 0.92300   29.87500 28.14100 1.000 16.49829 ? 681  ALA   A O    1 
ATOM   1877 C  CB   . ALA   A 1 247 ? -1.18600  30.17600 30.62000 1.000 8.23632  ? 681  ALA   A CB   1 
ATOM   1878 N  N    . PHE   A 1 248 ? -0.98300  30.87900 27.49100 1.000 8.90721  ? 682  PHE   A N    1 
ATOM   1879 C  CA   . PHE   A 1 248 ? -0.78700  30.48000 26.10300 1.000 11.20019 ? 682  PHE   A CA   1 
ATOM   1880 C  C    . PHE   A 1 248 ? 0.38900   31.22200 25.47900 1.000 10.25929 ? 682  PHE   A C    1 
ATOM   1881 O  O    . PHE   A 1 248 ? 1.15100   30.64400 24.69900 1.000 14.83283 ? 682  PHE   A O    1 
ATOM   1882 C  CB   . PHE   A 1 248 ? -2.06600  30.72000 25.29900 1.000 14.16851 ? 682  PHE   A CB   1 
ATOM   1883 C  CG   . PHE   A 1 248 ? -2.92600  29.49500 25.13800 1.000 11.21944 ? 682  PHE   A CG   1 
ATOM   1884 C  CD1  . PHE   A 1 248 ? -3.53500  28.90700 26.23700 1.000 12.15187 ? 682  PHE   A CD1  1 
ATOM   1885 C  CD2  . PHE   A 1 248 ? -3.14000  28.94200 23.88100 1.000 19.78909 ? 682  PHE   A CD2  1 
ATOM   1886 C  CE1  . PHE   A 1 248 ? -4.32900  27.78400 26.09200 1.000 12.89622 ? 682  PHE   A CE1  1 
ATOM   1887 C  CE2  . PHE   A 1 248 ? -3.93800  27.81500 23.72500 1.000 16.40356 ? 682  PHE   A CE2  1 
ATOM   1888 C  CZ   . PHE   A 1 248 ? -4.53000  27.23500 24.83400 1.000 12.76400 ? 682  PHE   A CZ   1 
ATOM   1889 N  N    . HIS   A 1 249 ? 0.56700   32.49700 25.83100 1.000 15.59465 ? 683  HIS   A N    1 
ATOM   1890 C  CA   . HIS   A 1 249 ? 1.60000   33.30800 25.19300 1.000 15.71903 ? 683  HIS   A CA   1 
ATOM   1891 C  C    . HIS   A 1 249 ? 2.99900   32.88300 25.62300 1.000 15.99482 ? 683  HIS   A C    1 
ATOM   1892 O  O    . HIS   A 1 249 ? 3.91100   32.80500 24.79000 1.000 14.72659 ? 683  HIS   A O    1 
ATOM   1893 C  CB   . HIS   A 1 249 ? 1.36700   34.78500 25.51100 1.000 10.00427 ? 683  HIS   A CB   1 
ATOM   1894 C  CG   . HIS   A 1 249 ? 2.42200   35.69800 24.96700 1.000 17.99215 ? 683  HIS   A CG   1 
ATOM   1895 N  ND1  . HIS   A 1 249 ? 2.56600   35.95200 23.62000 1.000 16.91763 ? 683  HIS   A ND1  1 
ATOM   1896 C  CD2  . HIS   A 1 249 ? 3.37600   36.43000 25.59100 1.000 16.77620 ? 683  HIS   A CD2  1 
ATOM   1897 C  CE1  . HIS   A 1 249 ? 3.56500   36.79700 23.43700 1.000 14.74015 ? 683  HIS   A CE1  1 
ATOM   1898 N  NE2  . HIS   A 1 249 ? 4.07400   37.10200 24.61700 1.000 17.03183 ? 683  HIS   A NE2  1 
ATOM   1899 N  N    . HIS   A 1 250 ? 3.19400   32.61300 26.91600 1.000 10.11473 ? 684  HIS   A N    1 
ATOM   1900 C  CA   . HIS   A 1 250 ? 4.51900   32.30000 27.43600 1.000 10.51611 ? 684  HIS   A CA   1 
ATOM   1901 C  C    . HIS   A 1 250 ? 4.83000   30.81100 27.46200 1.000 9.46326  ? 684  HIS   A C    1 
ATOM   1902 O  O    . HIS   A 1 250 ? 6.01100   30.44300 27.49200 1.000 9.71434  ? 684  HIS   A O    1 
ATOM   1903 C  CB   . HIS   A 1 250 ? 4.68000   32.85500 28.85700 1.000 14.08327 ? 684  HIS   A CB   1 
ATOM   1904 C  CG   . HIS   A 1 250 ? 4.64500   34.34900 28.93300 1.000 14.71296 ? 684  HIS   A CG   1 
ATOM   1905 N  ND1  . HIS   A 1 250 ? 5.77300   35.12800 28.79600 1.000 19.28360 ? 684  HIS   A ND1  1 
ATOM   1906 C  CD2  . HIS   A 1 250 ? 3.61700   35.20700 29.13500 1.000 12.54014 ? 684  HIS   A CD2  1 
ATOM   1907 C  CE1  . HIS   A 1 250 ? 5.44300   36.40200 28.91300 1.000 13.27947 ? 684  HIS   A CE1  1 
ATOM   1908 N  NE2  . HIS   A 1 250 ? 4.14000   36.47700 29.11500 1.000 11.34608 ? 684  HIS   A NE2  1 
ATOM   1909 N  N    . LEU   A 1 251 ? 3.81400   29.95000 27.45200 1.000 8.98545  ? 685  LEU   A N    1 
ATOM   1910 C  CA   . LEU   A 1 251 ? 4.03500   28.52900 27.68900 1.000 8.73327  ? 685  LEU   A CA   1 
ATOM   1911 C  C    . LEU   A 1 251 ? 3.45600   27.64700 26.59100 1.000 9.65763  ? 685  LEU   A C    1 
ATOM   1912 O  O    . LEU   A 1 251 ? 4.20900   27.02300 25.83800 1.000 14.48106 ? 685  LEU   A O    1 
ATOM   1913 C  CB   . LEU   A 1 251 ? 3.43800   28.12300 29.03600 1.000 8.54565  ? 685  LEU   A CB   1 
ATOM   1914 C  CG   . LEU   A 1 251 ? 4.06800   28.75600 30.27700 1.000 10.68115 ? 685  LEU   A CG   1 
ATOM   1915 C  CD1  . LEU   A 1 251 ? 3.07900   28.74200 31.43400 1.000 12.10602 ? 685  LEU   A CD1  1 
ATOM   1916 C  CD2  . LEU   A 1 251 ? 5.33400   28.01700 30.65500 1.000 11.23654 ? 685  LEU   A CD2  1 
ATOM   1917 N  N    . VAL   A 1 252 ? 2.12300   27.58800 26.49600 1.000 12.31904 ? 686  VAL   A N    1 
ATOM   1918 C  CA   . VAL   A 1 252 ? 1.47400   26.57300 25.66600 1.000 13.69294 ? 686  VAL   A CA   1 
ATOM   1919 C  C    . VAL   A 1 252 ? 1.89300   26.70600 24.20500 1.000 13.20064 ? 686  VAL   A C    1 
ATOM   1920 O  O    . VAL   A 1 252 ? 2.23400   25.71300 23.55100 1.000 10.60164 ? 686  VAL   A O    1 
ATOM   1921 C  CB   . VAL   A 1 252 ? -0.05500  26.64900 25.83000 1.000 12.06949 ? 686  VAL   A CB   1 
ATOM   1922 C  CG1  . VAL   A 1 252 ? -0.73600  25.65600 24.91000 1.000 7.26392  ? 686  VAL   A CG1  1 
ATOM   1923 C  CG2  . VAL   A 1 252 ? -0.44300  26.38600 27.27700 1.000 18.71953 ? 686  VAL   A CG2  1 
ATOM   1924 N  N    . MET   A 1 253 ? 1.89500   27.92500 23.67600 1.000 11.33456 ? 687  MET   A N    1 
ATOM   1925 C  CA   . MET   A 1 253 ? 2.17800   28.12900 22.26000 1.000 13.82081 ? 687  MET   A CA   1 
ATOM   1926 C  C    . MET   A 1 253 ? 3.66900   28.06900 21.92800 1.000 19.54502 ? 687  MET   A C    1 
ATOM   1927 O  O    . MET   A 1 253 ? 4.02700   27.57900 20.84800 1.000 12.82561 ? 687  MET   A O    1 
ATOM   1928 C  CB   . MET   A 1 253 ? 1.58300   29.45800 21.78700 1.000 13.26011 ? 687  MET   A CB   1 
ATOM   1929 C  CG   . MET   A 1 253 ? 0.06200   29.45100 21.71500 1.000 16.14755 ? 687  MET   A CG   1 
ATOM   1930 S  SD   . MET   A 1 253 ? -0.57300  27.99200 20.86400 1.000 19.61618 ? 687  MET   A SD   1 
ATOM   1931 C  CE   . MET   A 1 253 ? 0.04800   28.27100 19.21000 1.000 9.00273  ? 687  MET   A CE   1 
ATOM   1932 N  N    . PRO   A 1 254 ? 4.57100   28.57300 22.78200 1.000 15.08438 ? 688  PRO   A N    1 
ATOM   1933 C  CA   . PRO   A 1 254 ? 5.99800   28.32000 22.51900 1.000 12.95983 ? 688  PRO   A CA   1 
ATOM   1934 C  C    . PRO   A 1 254 ? 6.35900   26.84500 22.54500 1.000 12.55885 ? 688  PRO   A C    1 
ATOM   1935 O  O    . PRO   A 1 254 ? 7.12800   26.38400 21.69300 1.000 12.34624 ? 688  PRO   A O    1 
ATOM   1936 C  CB   . PRO   A 1 254 ? 6.70000   29.10200 23.63800 1.000 11.61653 ? 688  PRO   A CB   1 
ATOM   1937 C  CG   . PRO   A 1 254 ? 5.76500   30.19300 23.96400 1.000 11.70391 ? 688  PRO   A CG   1 
ATOM   1938 C  CD   . PRO   A 1 254 ? 4.39600   29.59700 23.83000 1.000 11.53558 ? 688  PRO   A CD   1 
ATOM   1939 N  N    . ILE   A 1 255 ? 5.81800   26.08400 23.49900 1.000 10.18657 ? 689  ILE   A N    1 
ATOM   1940 C  CA   . ILE   A 1 255 ? 6.15000   24.66600 23.59900 1.000 9.05886  ? 689  ILE   A CA   1 
ATOM   1941 C  C    . ILE   A 1 255 ? 5.54600   23.88400 22.43700 1.000 15.55878 ? 689  ILE   A C    1 
ATOM   1942 O  O    . ILE   A 1 255 ? 6.18300   22.98100 21.87900 1.000 10.70271 ? 689  ILE   A O    1 
ATOM   1943 C  CB   . ILE   A 1 255 ? 5.68700   24.10900 24.95600 1.000 11.38655 ? 689  ILE   A CB   1 
ATOM   1944 C  CG1  . ILE   A 1 255 ? 6.42000   24.81700 26.10000 1.000 21.58674 ? 689  ILE   A CG1  1 
ATOM   1945 C  CG2  . ILE   A 1 255 ? 5.91600   22.60700 25.02000 1.000 9.42154  ? 689  ILE   A CG2  1 
ATOM   1946 C  CD1  . ILE   A 1 255 ? 5.92500   24.42900 27.47200 1.000 10.15437 ? 689  ILE   A CD1  1 
ATOM   1947 N  N    . ALA   A 1 256 ? 4.30800   24.20400 22.05900 1.000 14.45790 ? 690  ALA   A N    1 
ATOM   1948 C  CA   . ALA   A 1 256 ? 3.66300   23.47300 20.97600 1.000 8.53429  ? 690  ALA   A CA   1 
ATOM   1949 C  C    . ALA   A 1 256 ? 4.37500   23.70500 19.64900 1.000 9.24353  ? 690  ALA   A C    1 
ATOM   1950 O  O    . ALA   A 1 256 ? 4.50700   22.78100 18.84300 1.000 9.44241  ? 690  ALA   A O    1 
ATOM   1951 C  CB   . ALA   A 1 256 ? 2.19000   23.87000 20.87800 1.000 8.15281  ? 690  ALA   A CB   1 
ATOM   1952 N  N    . ARG   A 1 257 ? 4.84900   24.92700 19.40600 1.000 10.05744 ? 691  ARG   A N    1 
ATOM   1953 C  CA   . ARG   A 1 257 ? 5.57800   25.19100 18.17000 1.000 9.75657  ? 691  ARG   A CA   1 
ATOM   1954 C  C    . ARG   A 1 257 ? 6.89300   24.42100 18.12100 1.000 14.63439 ? 691  ARG   A C    1 
ATOM   1955 O  O    . ARG   A 1 257 ? 7.25200   23.86800 17.07400 1.000 16.26100 ? 691  ARG   A O    1 
ATOM   1956 C  CB   . ARG   A 1 257 ? 5.82700   26.68900 18.01100 1.000 13.89763 ? 691  ARG   A CB   1 
ATOM   1957 C  CG   . ARG   A 1 257 ? 4.64500   27.45000 17.44600 1.000 15.13406 ? 691  ARG   A CG   1 
ATOM   1958 C  CD   . ARG   A 1 257 ? 5.02100   28.87500 17.08600 1.000 10.64145 ? 691  ARG   A CD   1 
ATOM   1959 N  NE   . ARG   A 1 257 ? 5.21300   29.70200 18.27000 1.000 15.02889 ? 691  ARG   A NE   1 
ATOM   1960 C  CZ   . ARG   A 1 257 ? 4.26400   30.43700 18.83300 1.000 26.65971 ? 691  ARG   A CZ   1 
ATOM   1961 N  NH1  . ARG   A 1 257 ? 3.03700   30.47700 18.34100 1.000 22.02906 ? 691  ARG   A NH1  1 
ATOM   1962 N  NH2  . ARG   A 1 257 ? 4.55400   31.15300 19.91400 1.000 23.31061 ? 691  ARG   A NH2  1 
ATOM   1963 N  N    . GLU   A 1 258 ? 7.63200   24.37600 19.23500 1.000 12.17764 ? 692  GLU   A N    1 
ATOM   1964 C  CA   . GLU   A 1 258 ? 8.87000   23.60000 19.25200 1.000 10.71426 ? 692  GLU   A CA   1 
ATOM   1965 C  C    . GLU   A 1 258 ? 8.59000   22.10900 19.11300 1.000 11.99084 ? 692  GLU   A C    1 
ATOM   1966 O  O    . GLU   A 1 258 ? 9.41200   21.37100 18.55600 1.000 15.45471 ? 692  GLU   A O    1 
ATOM   1967 C  CB   . GLU   A 1 258 ? 9.66100   23.88000 20.53500 1.000 11.19610 ? 692  GLU   A CB   1 
ATOM   1968 C  CG   . GLU   A 1 258 ? 11.09300  23.33400 20.51600 1.000 12.22488 ? 692  GLU   A CG   1 
ATOM   1969 C  CD   . GLU   A 1 258 ? 11.92600  23.78700 21.70500 1.000 13.77979 ? 692  GLU   A CD   1 
ATOM   1970 O  OE1  . GLU   A 1 258 ? 11.50300  24.72100 22.42000 1.000 15.78004 ? 692  GLU   A OE1  1 
ATOM   1971 O  OE2  . GLU   A 1 258 ? 13.01100  23.20800 21.92500 1.000 16.04790 ? 692  GLU   A OE2  1 
ATOM   1972 N  N    . PHE   A 1 259 ? 7.43400   21.65400 19.59800 1.000 15.91086 ? 693  PHE   A N    1 
ATOM   1973 C  CA   . PHE   A 1 259 ? 7.07300   20.24600 19.48500 1.000 13.10471 ? 693  PHE   A CA   1 
ATOM   1974 C  C    . PHE   A 1 259 ? 6.63400   19.89100 18.06900 1.000 10.25111 ? 693  PHE   A C    1 
ATOM   1975 O  O    . PHE   A 1 259 ? 6.76900   18.73600 17.65100 1.000 10.54543 ? 693  PHE   A O    1 
ATOM   1976 C  CB   . PHE   A 1 259 ? 5.97400   19.92600 20.49800 1.000 9.50500  ? 693  PHE   A CB   1 
ATOM   1977 C  CG   . PHE   A 1 259 ? 5.49500   18.50600 20.46000 1.000 9.50461  ? 693  PHE   A CG   1 
ATOM   1978 C  CD1  . PHE   A 1 259 ? 6.31800   17.47200 20.87300 1.000 9.90746  ? 693  PHE   A CD1  1 
ATOM   1979 C  CD2  . PHE   A 1 259 ? 4.21100   18.20600 20.03100 1.000 11.34126 ? 693  PHE   A CD2  1 
ATOM   1980 C  CE1  . PHE   A 1 259 ? 5.87800   16.16200 20.84200 1.000 10.00047 ? 693  PHE   A CE1  1 
ATOM   1981 C  CE2  . PHE   A 1 259 ? 3.76300   16.89500 19.99900 1.000 9.24438  ? 693  PHE   A CE2  1 
ATOM   1982 C  CZ   . PHE   A 1 259 ? 4.59700   15.87400 20.40600 1.000 9.66447  ? 693  PHE   A CZ   1 
ATOM   1983 N  N    . ALA   A 1 260 ? 6.12300   20.86800 17.32600 1.000 10.15091 ? 694  ALA   A N    1 
ATOM   1984 C  CA   . ALA   A 1 260 ? 5.63400   20.67500 15.96600 1.000 11.34102 ? 694  ALA   A CA   1 
ATOM   1985 C  C    . ALA   A 1 260 ? 4.60500   19.54500 15.87700 1.000 10.10697 ? 694  ALA   A C    1 
ATOM   1986 O  O    . ALA   A 1 260 ? 4.82100   18.55500 15.16900 1.000 16.48101 ? 694  ALA   A O    1 
ATOM   1987 C  CB   . ALA   A 1 260 ? 6.78900   20.43000 15.00600 1.000 11.09030 ? 694  ALA   A CB   1 
ATOM   1988 N  N    . PRO   A 1 261 ? 3.47500   19.66200 16.56800 1.000 9.52879  ? 695  PRO   A N    1 
ATOM   1989 C  CA   . PRO   A 1 261 ? 2.48100   18.58900 16.51100 1.000 16.65914 ? 695  PRO   A CA   1 
ATOM   1990 C  C    . PRO   A 1 261 ? 1.95700   18.43100 15.09400 1.000 15.22154 ? 695  PRO   A C    1 
ATOM   1991 O  O    . PRO   A 1 261 ? 1.84600   19.40100 14.34300 1.000 10.85146 ? 695  PRO   A O    1 
ATOM   1992 C  CB   . PRO   A 1 261 ? 1.38700   19.07000 17.46700 1.000 10.90010 ? 695  PRO   A CB   1 
ATOM   1993 C  CG   . PRO   A 1 261 ? 1.46000   20.54700 17.37100 1.000 8.66673  ? 695  PRO   A CG   1 
ATOM   1994 C  CD   . PRO   A 1 261 ? 2.92700   20.87200 17.20000 1.000 9.10551  ? 695  PRO   A CD   1 
ATOM   1995 N  N    . GLU   A 1 262 ? 1.66900   17.19000 14.72100 1.000 15.88852 ? 696  GLU   A N    1 
ATOM   1996 C  CA   . GLU   A 1 262 ? 0.98100   16.92000 13.46800 1.000 18.40564 ? 696  GLU   A CA   1 
ATOM   1997 C  C    . GLU   A 1 262 ? -0.52900  16.88900 13.63200 1.000 15.99557 ? 696  GLU   A C    1 
ATOM   1998 O  O    . GLU   A 1 262 ? -1.25400  16.98800 12.63400 1.000 19.33107 ? 696  GLU   A O    1 
ATOM   1999 C  CB   . GLU   A 1 262 ? 1.45100   15.58800 12.88400 1.000 20.97748 ? 696  GLU   A CB   1 
ATOM   2000 C  CG   . GLU   A 1 262 ? 2.90600   15.57000 12.46500 1.000 11.30384 ? 696  GLU   A CG   1 
ATOM   2001 C  CD   . GLU   A 1 262 ? 3.39200   14.16600 12.20400 1.000 18.36887 ? 696  GLU   A CD   1 
ATOM   2002 O  OE1  . GLU   A 1 262 ? 3.64600   13.44400 13.18900 1.000 11.85953 ? 696  GLU   A OE1  1 
ATOM   2003 O  OE2  . GLU   A 1 262 ? 3.49200   13.77500 11.01900 1.000 18.95042 ? 696  GLU   A OE2  1 
ATOM   2004 N  N    . LEU   A 1 263 ? -1.01200  16.75800 14.86400 1.000 15.04887 ? 697  LEU   A N    1 
ATOM   2005 C  CA   . LEU   A 1 263 ? -2.43600  16.72400 15.15800 1.000 9.81729  ? 697  LEU   A CA   1 
ATOM   2006 C  C    . LEU   A 1 263 ? -2.64600  17.26700 16.56100 1.000 14.31281 ? 697  LEU   A C    1 
ATOM   2007 O  O    . LEU   A 1 263 ? -1.91100  16.90800 17.48600 1.000 13.45401 ? 697  LEU   A O    1 
ATOM   2008 C  CB   . LEU   A 1 263 ? -2.99900  15.30400 15.05500 1.000 10.11033 ? 697  LEU   A CB   1 
ATOM   2009 C  CG   . LEU   A 1 263 ? -4.46500  15.16200 15.46700 1.000 12.75026 ? 697  LEU   A CG   1 
ATOM   2010 C  CD1  . LEU   A 1 263 ? -5.37600  15.77000 14.39800 1.000 14.79223 ? 697  LEU   A CD1  1 
ATOM   2011 C  CD2  . LEU   A 1 263 ? -4.82400  13.71400 15.73400 1.000 8.80271  ? 697  LEU   A CD2  1 
ATOM   2012 N  N    . VAL   A 1 264 ? -3.65100  18.12500 16.71300 1.000 17.04011 ? 698  VAL   A N    1 
ATOM   2013 C  CA   . VAL   A 1 264 ? -3.96400  18.77400 17.98100 1.000 12.62141 ? 698  VAL   A CA   1 
ATOM   2014 C  C    . VAL   A 1 264 ? -5.32200  18.27500 18.45200 1.000 11.16633 ? 698  VAL   A C    1 
ATOM   2015 O  O    . VAL   A 1 264 ? -6.32300  18.40700 17.73600 1.000 7.33118  ? 698  VAL   A O    1 
ATOM   2016 C  CB   . VAL   A 1 264 ? -3.96400  20.30500 17.85100 1.000 11.43285 ? 698  VAL   A CB   1 
ATOM   2017 C  CG1  . VAL   A 1 264 ? -4.23700  20.95000 19.20500 1.000 10.38965 ? 698  VAL   A CG1  1 
ATOM   2018 C  CG2  . VAL   A 1 264 ? -2.64500  20.79100 17.27800 1.000 8.23451  ? 698  VAL   A CG2  1 
ATOM   2019 N  N    . LEU   A 1 265 ? -5.35500  17.69800 19.64900 1.000 15.30527 ? 699  LEU   A N    1 
ATOM   2020 C  CA   . LEU   A 1 265 ? -6.58900  17.32000 20.32300 1.000 7.33775  ? 699  LEU   A CA   1 
ATOM   2021 C  C    . LEU   A 1 265 ? -6.78700  18.23800 21.51800 1.000 11.05527 ? 699  LEU   A C    1 
ATOM   2022 O  O    . LEU   A 1 265 ? -5.85200  18.46100 22.29400 1.000 11.08904 ? 699  LEU   A O    1 
ATOM   2023 C  CB   . LEU   A 1 265 ? -6.54800  15.86200 20.78700 1.000 7.08734  ? 699  LEU   A CB   1 
ATOM   2024 C  CG   . LEU   A 1 265 ? -6.15800  14.78900 19.76600 1.000 7.54116  ? 699  LEU   A CG   1 
ATOM   2025 C  CD1  . LEU   A 1 265 ? -6.35500  13.40000 20.36300 1.000 7.68073  ? 699  LEU   A CD1  1 
ATOM   2026 C  CD2  . LEU   A 1 265 ? -6.95600  14.94100 18.47800 1.000 7.61199  ? 699  LEU   A CD2  1 
ATOM   2027 N  N    . VAL   A 1 266 ? -7.99300  18.77400 21.66500 1.000 10.82532 ? 700  VAL   A N    1 
ATOM   2028 C  CA   . VAL   A 1 266 ? -8.31300  19.67300 22.76600 1.000 6.35747  ? 700  VAL   A CA   1 
ATOM   2029 C  C    . VAL   A 1 266 ? -9.25800  18.94000 23.70600 1.000 10.78827 ? 700  VAL   A C    1 
ATOM   2030 O  O    . VAL   A 1 266 ? -10.42200 18.69800 23.36500 1.000 7.74097  ? 700  VAL   A O    1 
ATOM   2031 C  CB   . VAL   A 1 266 ? -8.93100  20.99000 22.28100 1.000 9.26664  ? 700  VAL   A CB   1 
ATOM   2032 C  CG1  . VAL   A 1 266 ? -9.09500  21.95600 23.45900 1.000 7.17295  ? 700  VAL   A CG1  1 
ATOM   2033 C  CG2  . VAL   A 1 266 ? -8.07200  21.61300 21.18700 1.000 9.31610  ? 700  VAL   A CG2  1 
ATOM   2034 N  N    . SER   A 1 267 ? -8.76000  18.57800 24.88900 1.000 7.26107  ? 701  SER   A N    1 
ATOM   2035 C  CA   . SER   A 1 267 ? -9.63100  18.14100 25.97700 1.000 8.03230  ? 701  SER   A CA   1 
ATOM   2036 C  C    . SER   A 1 267 ? -10.34500 19.38800 26.48400 1.000 9.49087  ? 701  SER   A C    1 
ATOM   2037 O  O    . SER   A 1 267 ? -9.94300  20.03900 27.45200 1.000 6.81543  ? 701  SER   A O    1 
ATOM   2038 C  CB   . SER   A 1 267 ? -8.84400  17.43300 27.07000 1.000 12.79290 ? 701  SER   A CB   1 
ATOM   2039 O  OG   . SER   A 1 267 ? -8.62300  16.07800 26.71400 1.000 13.55016 ? 701  SER   A OG   1 
ATOM   2040 N  N    . ALA   A 1 268 ? -11.42600 19.72800 25.78700 1.000 7.60268  ? 702  ALA   A N    1 
ATOM   2041 C  CA   . ALA   A 1 268 ? -12.08500 21.02100 25.92700 1.000 8.31339  ? 702  ALA   A CA   1 
ATOM   2042 C  C    . ALA   A 1 268 ? -13.24300 20.88400 26.90900 1.000 8.62562  ? 702  ALA   A C    1 
ATOM   2043 O  O    . ALA   A 1 268 ? -14.41200 20.78300 26.53400 1.000 6.49172  ? 702  ALA   A O    1 
ATOM   2044 C  CB   . ALA   A 1 268 ? -12.56200 21.52800 24.57000 1.000 6.35370  ? 702  ALA   A CB   1 
ATOM   2045 N  N    . GLY   A 1 269 ? -12.89700 20.86600 28.19300 1.000 6.39607  ? 703  GLY   A N    1 
ATOM   2046 C  CA   . GLY   A 1 269 ? -13.87700 21.15000 29.20800 1.000 9.36607  ? 703  GLY   A CA   1 
ATOM   2047 C  C    . GLY   A 1 269 ? -14.17100 22.63700 29.24900 1.000 10.12689 ? 703  GLY   A C    1 
ATOM   2048 O  O    . GLY   A 1 269 ? -13.32400 23.47000 28.93900 1.000 9.73243  ? 703  GLY   A O    1 
ATOM   2049 N  N    . PHE   A 1 270 ? -15.40300 22.97500 29.60300 1.000 12.76960 ? 704  PHE   A N    1 
ATOM   2050 C  CA   . PHE   A 1 270 ? -15.79600 24.37300 29.70200 1.000 9.22191  ? 704  PHE   A CA   1 
ATOM   2051 C  C    . PHE   A 1 270 ? -16.23300 24.71400 31.11900 1.000 11.17408 ? 704  PHE   A C    1 
ATOM   2052 O  O    . PHE   A 1 270 ? -17.04600 25.61700 31.33100 1.000 15.97956 ? 704  PHE   A O    1 
ATOM   2053 C  CB   . PHE   A 1 270 ? -16.88300 24.70300 28.68100 1.000 8.57563  ? 704  PHE   A CB   1 
ATOM   2054 C  CG   . PHE   A 1 270 ? -16.41400 24.59100 27.25800 1.000 10.57762 ? 704  PHE   A CG   1 
ATOM   2055 C  CD1  . PHE   A 1 270 ? -15.58500 25.55600 26.71400 1.000 9.45632  ? 704  PHE   A CD1  1 
ATOM   2056 C  CD2  . PHE   A 1 270 ? -16.77400 23.51100 26.47600 1.000 7.07590  ? 704  PHE   A CD2  1 
ATOM   2057 C  CE1  . PHE   A 1 270 ? -15.13500 25.45700 25.40900 1.000 7.70029  ? 704  PHE   A CE1  1 
ATOM   2058 C  CE2  . PHE   A 1 270 ? -16.33000 23.41000 25.17000 1.000 6.97291  ? 704  PHE   A CE2  1 
ATOM   2059 C  CZ   . PHE   A 1 270 ? -15.51000 24.38600 24.63800 1.000 6.97733  ? 704  PHE   A CZ   1 
ATOM   2060 N  N    . ASP   A 1 271 ? -15.69500 23.99100 32.09600 1.000 13.37846 ? 705  ASP   A N    1 
ATOM   2061 C  CA   . ASP   A 1 271 ? -15.94800 24.26300 33.50300 1.000 11.65273 ? 705  ASP   A CA   1 
ATOM   2062 C  C    . ASP   A 1 271 ? -14.97700 25.27600 34.09600 1.000 20.02738 ? 705  ASP   A C    1 
ATOM   2063 O  O    . ASP   A 1 271 ? -14.92000 25.41300 35.32100 1.000 14.86090 ? 705  ASP   A O    1 
ATOM   2064 C  CB   . ASP   A 1 271 ? -15.93500 22.96400 34.32500 1.000 8.65161  ? 705  ASP   A CB   1 
ATOM   2065 C  CG   . ASP   A 1 271 ? -14.82400 22.00000 33.92600 1.000 9.92791  ? 705  ASP   A CG   1 
ATOM   2066 O  OD1  . ASP   A 1 271 ? -13.91300 22.37400 33.15800 1.000 7.56503  ? 705  ASP   A OD1  1 
ATOM   2067 O  OD2  . ASP   A 1 271 ? -14.86600 20.84700 34.40400 1.000 10.47317 ? 705  ASP   A OD2  1 
ATOM   2068 N  N    . ALA   A 1 272 ? -14.21300 25.98000 33.26200 1.000 11.71461 ? 706  ALA   A N    1 
ATOM   2069 C  CA   . ALA   A 1 272 ? -13.51500 27.18900 33.67900 1.000 10.81332 ? 706  ALA   A CA   1 
ATOM   2070 C  C    . ALA   A 1 272 ? -14.24700 28.44200 33.22800 1.000 15.91101 ? 706  ALA   A C    1 
ATOM   2071 O  O    . ALA   A 1 272 ? -13.72200 29.55000 33.38300 1.000 14.14025 ? 706  ALA   A O    1 
ATOM   2072 C  CB   . ALA   A 1 272 ? -12.07800 27.20200 33.15200 1.000 9.42622  ? 706  ALA   A CB   1 
ATOM   2073 N  N    . ALA   A 1 273 ? -15.44600 28.29000 32.67600 1.000 16.57626 ? 707  ALA   A N    1 
ATOM   2074 C  CA   . ALA   A 1 273 ? -16.25000 29.42500 32.26000 1.000 11.37362 ? 707  ALA   A CA   1 
ATOM   2075 C  C    . ALA   A 1 273 ? -17.02600 30.00000 33.44400 1.000 13.34129 ? 707  ALA   A C    1 
ATOM   2076 O  O    . ALA   A 1 273 ? -17.29400 29.32000 34.43800 1.000 9.49720  ? 707  ALA   A O    1 
ATOM   2077 C  CB   . ALA   A 1 273 ? -17.21400 29.01900 31.14200 1.000 8.97658  ? 707  ALA   A CB   1 
ATOM   2078 N  N    . ARG   A 1 274 ? -17.38800 31.27400 33.31800 1.000 12.87887 ? 708  ARG   A N    1 
ATOM   2079 C  CA   . ARG   A 1 274 ? -18.19900 31.93100 34.32900 1.000 11.99509 ? 708  ARG   A CA   1 
ATOM   2080 C  C    . ARG   A 1 274 ? -19.51800 31.18800 34.52000 1.000 18.54698 ? 708  ARG   A C    1 
ATOM   2081 O  O    . ARG   A 1 274 ? -20.08800 30.63300 33.57600 1.000 15.26638 ? 708  ARG   A O    1 
ATOM   2082 C  CB   . ARG   A 1 274 ? -18.44700 33.38600 33.93100 1.000 13.19298 ? 708  ARG   A CB   1 
ATOM   2083 C  CG   . ARG   A 1 274 ? -18.85200 33.54600 32.47800 1.000 33.29203 ? 708  ARG   A CG   1 
ATOM   2084 C  CD   . ARG   A 1 274 ? -18.75100 34.98600 31.99100 1.000 38.78442 ? 708  ARG   A CD   1 
ATOM   2085 N  NE   . ARG   A 1 274 ? -19.61000 35.19600 30.83100 1.000 50.62068 ? 708  ARG   A NE   1 
ATOM   2086 C  CZ   . ARG   A 1 274 ? -19.42500 36.13100 29.90900 1.000 34.81464 ? 708  ARG   A CZ   1 
ATOM   2087 N  NH1  . ARG   A 1 274 ? -18.39400 36.95900 29.96000 1.000 34.05552 ? 708  ARG   A NH1  1 
ATOM   2088 N  NH2  . ARG   A 1 274 ? -20.29300 36.23400 28.90700 1.000 47.59694 ? 708  ARG   A NH2  1 
ATOM   2089 N  N    . GLY   A 1 275 ? -19.98600 31.15500 35.76500 1.000 21.40176 ? 709  GLY   A N    1 
ATOM   2090 C  CA   . GLY   A 1 275 ? -21.21600 30.47500 36.10100 1.000 14.69513 ? 709  GLY   A CA   1 
ATOM   2091 C  C    . GLY   A 1 275 ? -21.08000 29.00700 36.44400 1.000 12.29402 ? 709  GLY   A C    1 
ATOM   2092 O  O    . GLY   A 1 275 ? -22.08400 28.37800 36.79900 1.000 13.51800 ? 709  GLY   A O    1 
ATOM   2093 N  N    . ASP   A 1 276 ? -19.85800 28.49900 36.28200 1.000 19.19538 ? 710  ASP   A N    1 
ATOM   2094 C  CA   . ASP   A 1 276 ? -19.61500 27.05700 36.53800 1.000 13.39755 ? 710  ASP   A CA   1 
ATOM   2095 C  C    . ASP   A 1 276 ? -19.36300 26.84100 38.03200 1.000 15.88493 ? 710  ASP   A C    1 
ATOM   2096 O  O    . ASP   A 1 276 ? -18.39900 27.40100 38.58100 1.000 15.30798 ? 710  ASP   A O    1 
ATOM   2097 C  CB   . ASP   A 1 276 ? -18.59700 26.42200 35.61200 1.000 10.79997 ? 710  ASP   A CB   1 
ATOM   2098 C  CG   . ASP   A 1 276 ? -18.64600 24.90200 35.57300 1.000 11.71895 ? 710  ASP   A CG   1 
ATOM   2099 O  OD1  . ASP   A 1 276 ? -18.37500 24.28300 36.61200 1.000 13.60385 ? 710  ASP   A OD1  1 
ATOM   2100 O  OD2  . ASP   A 1 276 ? -18.95300 24.35400 34.50600 1.000 13.51825 ? 710  ASP   A OD2  1 
ATOM   2101 N  N    . PRO   A 1 277 ? -20.18600 25.99900 38.67000 1.000 15.12932 ? 711  PRO   A N    1 
ATOM   2102 C  CA   . PRO   A 1 277 ? -20.07800 25.72300 40.12200 1.000 11.91151 ? 711  PRO   A CA   1 
ATOM   2103 C  C    . PRO   A 1 277 ? -18.89600 24.80000 40.44600 1.000 24.65000 ? 711  PRO   A C    1 
ATOM   2104 O  O    . PRO   A 1 277 ? -18.42100 24.76800 41.60200 1.000 14.26310 ? 711  PRO   A O    1 
ATOM   2105 C  CB   . PRO   A 1 277 ? -21.46800 25.15900 40.39900 1.000 15.64625 ? 711  PRO   A CB   1 
ATOM   2106 C  CG   . PRO   A 1 277 ? -22.31700 25.31700 39.16600 1.000 12.24237 ? 711  PRO   A CG   1 
ATOM   2107 C  CD   . PRO   A 1 277 ? -21.32600 25.24700 38.07200 1.000 17.64348 ? 711  PRO   A CD   1 
ATOM   2108 N  N    . LEU   A 1 278 ? -18.39900 24.06800 39.44400 1.000 15.29262 ? 712  LEU   A N    1 
ATOM   2109 C  CA   . LEU   A 1 278 ? -17.30000 23.10700 39.68400 1.000 15.90145 ? 712  LEU   A CA   1 
ATOM   2110 C  C    . LEU   A 1 278 ? -15.97100 23.70300 39.19200 1.000 25.10798 ? 712  LEU   A C    1 
ATOM   2111 O  O    . LEU   A 1 278 ? -15.04100 22.91900 38.94100 1.000 27.61988 ? 712  LEU   A O    1 
ATOM   2112 C  CB   . LEU   A 1 278 ? -17.60300 21.76400 39.03400 1.000 18.29085 ? 712  LEU   A CB   1 
ATOM   2113 C  CG   . LEU   A 1 278 ? -18.57600 20.86000 39.79500 1.000 16.54929 ? 712  LEU   A CG   1 
ATOM   2114 C  CD1  . LEU   A 1 278 ? -19.67600 20.34000 38.89600 1.000 14.81638 ? 712  LEU   A CD1  1 
ATOM   2115 C  CD2  . LEU   A 1 278 ? -17.83900 19.71600 40.44800 1.000 12.98656 ? 712  LEU   A CD2  1 
ATOM   2116 N  N    . GLY   A 1 279 ? -15.91200 25.01800 39.01400 1.000 13.70439 ? 713  GLY   A N    1 
ATOM   2117 C  CA   . GLY   A 1 279 ? -14.69900 25.63900 38.46400 1.000 14.00258 ? 713  GLY   A CA   1 
ATOM   2118 C  C    . GLY   A 1 279 ? -14.35300 26.91200 39.18700 1.000 17.48677 ? 713  GLY   A C    1 
ATOM   2119 O  O    . GLY   A 1 279 ? -13.20100 27.05800 39.61100 1.000 17.05809 ? 713  GLY   A O    1 
ATOM   2120 N  N    . GLY   A 1 280 ? -15.33600 27.78100 39.33100 1.000 16.07339 ? 714  GLY   A N    1 
ATOM   2121 C  CA   . GLY   A 1 280 ? -15.12800 29.04700 40.04800 1.000 13.34349 ? 714  GLY   A CA   1 
ATOM   2122 C  C    . GLY   A 1 280 ? -14.29100 30.03700 39.27900 1.000 16.58999 ? 714  GLY   A C    1 
ATOM   2123 O  O    . GLY   A 1 280 ? -13.82900 31.01000 39.88900 1.000 20.60914 ? 714  GLY   A O    1 
ATOM   2124 N  N    . PHE   A 1 281 ? -14.12900 29.81400 37.98100 1.000 14.08497 ? 715  PHE   A N    1 
ATOM   2125 C  CA   . PHE   A 1 281 ? -13.37100 30.75500 37.11800 1.000 14.21831 ? 715  PHE   A CA   1 
ATOM   2126 C  C    . PHE   A 1 281 ? -14.31100 31.59800 36.26000 1.000 11.46007 ? 715  PHE   A C    1 
ATOM   2127 O  O    . PHE   A 1 281 ? -15.52200 31.39400 36.31400 1.000 11.47451 ? 715  PHE   A O    1 
ATOM   2128 C  CB   . PHE   A 1 281 ? -12.36100 29.96000 36.28800 1.000 16.89458 ? 715  PHE   A CB   1 
ATOM   2129 C  CG   . PHE   A 1 281 ? -11.12500 29.50400 37.05100 1.000 18.84426 ? 715  PHE   A CG   1 
ATOM   2130 C  CD1  . PHE   A 1 281 ? -11.01100 29.70400 38.42200 1.000 13.86214 ? 715  PHE   A CD1  1 
ATOM   2131 C  CD2  . PHE   A 1 281 ? -10.08500 28.85900 36.39700 1.000 11.98923 ? 715  PHE   A CD2  1 
ATOM   2132 C  CE1  . PHE   A 1 281 ? -9.88600  29.28600 39.10800 1.000 10.80668 ? 715  PHE   A CE1  1 
ATOM   2133 C  CE2  . PHE   A 1 281 ? -8.96300  28.44700 37.09200 1.000 15.98394 ? 715  PHE   A CE2  1 
ATOM   2134 C  CZ   . PHE   A 1 281 ? -8.86600  28.66400 38.44300 1.000 9.11458  ? 715  PHE   A CZ   1 
ATOM   2135 N  N    . GLN   A 1 282 ? -13.73400 32.48000 35.45100 1.000 10.22515 ? 716  GLN   A N    1 
ATOM   2136 C  CA   . GLN   A 1 282 ? -14.53800 33.40200 34.62200 1.000 16.55543 ? 716  GLN   A CA   1 
ATOM   2137 C  C    . GLN   A 1 282 ? -13.98100 33.51500 33.19700 1.000 11.84776 ? 716  GLN   A C    1 
ATOM   2138 O  O    . GLN   A 1 282 ? -13.99700 34.61100 32.63800 1.000 14.96825 ? 716  GLN   A O    1 
ATOM   2139 C  CB   . GLN   A 1 282 ? -14.59900 34.75300 35.32700 1.000 11.29104 ? 716  GLN   A CB   1 
ATOM   2140 C  CG   . GLN   A 1 282 ? -13.24600 35.30500 35.75500 1.000 20.69747 ? 716  GLN   A CG   1 
ATOM   2141 C  CD   . GLN   A 1 282 ? -13.34500 36.66800 36.39900 1.000 22.57808 ? 716  GLN   A CD   1 
ATOM   2142 O  OE1  . GLN   A 1 282 ? -14.39900 37.30900 36.39800 1.000 16.50193 ? 716  GLN   A OE1  1 
ATOM   2143 N  NE2  . GLN   A 1 282 ? -12.23800 37.12500 36.96200 1.000 40.46933 ? 716  GLN   A NE2  1 
ATOM   2144 N  N    . VAL   A 1 283 ? -13.51900 32.40300 32.64700 1.000 11.31625 ? 717  VAL   A N    1 
ATOM   2145 C  CA   . VAL   A 1 283 ? -13.10000 32.43800 31.25000 1.000 16.69516 ? 717  VAL   A CA   1 
ATOM   2146 C  C    . VAL   A 1 283 ? -14.32600 32.65000 30.37600 1.000 11.38748 ? 717  VAL   A C    1 
ATOM   2147 O  O    . VAL   A 1 283 ? -15.32800 31.93500 30.50400 1.000 12.03615 ? 717  VAL   A O    1 
ATOM   2148 C  CB   . VAL   A 1 283 ? -12.35900 31.14900 30.87000 1.000 14.70371 ? 717  VAL   A CB   1 
ATOM   2149 C  CG1  . VAL   A 1 283 ? -11.95500 31.19100 29.40100 1.000 13.76322 ? 717  VAL   A CG1  1 
ATOM   2150 C  CG2  . VAL   A 1 283 ? -11.14100 30.95700 31.75800 1.000 14.47056 ? 717  VAL   A CG2  1 
ATOM   2151 N  N    . THR   A 1 284 ? -14.26200 33.64800 29.49500 1.000 9.69726  ? 718  THR   A N    1 
ATOM   2152 C  CA   . THR   A 1 284 ? -15.41800 34.04500 28.70700 1.000 16.12404 ? 718  THR   A CA   1 
ATOM   2153 C  C    . THR   A 1 284 ? -15.47500 33.26700 27.40100 1.000 12.70417 ? 718  THR   A C    1 
ATOM   2154 O  O    . THR   A 1 284 ? -14.47100 32.70200 26.95600 1.000 16.28595 ? 718  THR   A O    1 
ATOM   2155 C  CB   . THR   A 1 284 ? -15.36700 35.54400 28.41500 1.000 12.11065 ? 718  THR   A CB   1 
ATOM   2156 O  OG1  . THR   A 1 284 ? -14.42600 35.79000 27.36500 1.000 13.71694 ? 718  THR   A OG1  1 
ATOM   2157 C  CG2  . THR   A 1 284 ? -14.95200 36.31900 29.65500 1.000 14.58323 ? 718  THR   A CG2  1 
ATOM   2158 N  N    . PRO   A 1 285 ? -16.65300 33.19700 26.76900 1.000 18.08736 ? 719  PRO   A N    1 
ATOM   2159 C  CA   . PRO   A 1 285 ? -16.73200 32.56800 25.43800 1.000 13.54388 ? 719  PRO   A CA   1 
ATOM   2160 C  C    . PRO   A 1 285 ? -15.75400 33.16000 24.44000 1.000 13.19067 ? 719  PRO   A C    1 
ATOM   2161 O  O    . PRO   A 1 285 ? -15.20500 32.43500 23.60100 1.000 9.77426  ? 719  PRO   A O    1 
ATOM   2162 C  CB   . PRO   A 1 285 ? -18.18700 32.82400 25.02400 1.000 10.22484 ? 719  PRO   A CB   1 
ATOM   2163 C  CG   . PRO   A 1 285 ? -18.92700 32.94200 26.31400 1.000 10.99647 ? 719  PRO   A CG   1 
ATOM   2164 C  CD   . PRO   A 1 285 ? -17.97900 33.59300 27.27800 1.000 14.68361 ? 719  PRO   A CD   1 
ATOM   2165 N  N    . GLU   A 1 286 ? -15.52600 34.47300 24.51300 1.000 10.88966 ? 720  GLU   A N    1 
ATOM   2166 C  CA   . GLU   A 1 286 ? -14.57200 35.12500 23.62400 1.000 10.26460 ? 720  GLU   A CA   1 
ATOM   2167 C  C    . GLU   A 1 286 ? -13.15100 34.64300 23.88100 1.000 16.49976 ? 720  GLU   A C    1 
ATOM   2168 O  O    . GLU   A 1 286 ? -12.34100 34.58100 22.94900 1.000 15.97259 ? 720  GLU   A O    1 
ATOM   2169 C  CB   . GLU   A 1 286 ? -14.65900 36.64400 23.78900 1.000 11.05116 ? 720  GLU   A CB   1 
ATOM   2170 C  CG   . GLU   A 1 286 ? -15.95900 37.27500 23.27500 1.000 23.08905 ? 720  GLU   A CG   1 
ATOM   2171 C  CD   . GLU   A 1 286 ? -17.16900 37.00100 24.16000 1.000 16.05182 ? 720  GLU   A CD   1 
ATOM   2172 O  OE1  . GLU   A 1 286 ? -16.99100 36.66400 25.34700 1.000 22.67942 ? 720  GLU   A OE1  1 
ATOM   2173 O  OE2  . GLU   A 1 286 ? -18.30900 37.12600 23.66400 1.000 27.11676 ? 720  GLU   A OE2  1 
ATOM   2174 N  N    . GLY   A 1 287 ? -12.83100 34.30000 25.13000 1.000 17.25660 ? 721  GLY   A N    1 
ATOM   2175 C  CA   . GLY   A 1 287 ? -11.50200 33.79200 25.42900 1.000 12.92580 ? 721  GLY   A CA   1 
ATOM   2176 C  C    . GLY   A 1 287 ? -11.26800 32.40600 24.86100 1.000 11.18430 ? 721  GLY   A C    1 
ATOM   2177 O  O    . GLY   A 1 287 ? -10.20300 32.12900 24.30200 1.000 17.65889 ? 721  GLY   A O    1 
ATOM   2178 N  N    . TYR   A 1 288 ? -12.25500 31.51300 25.00300 1.000 9.13986  ? 722  TYR   A N    1 
ATOM   2179 C  CA   . TYR   A 1 288 ? -12.15600 30.19900 24.37800 1.000 8.91440  ? 722  TYR   A CA   1 
ATOM   2180 C  C    . TYR   A 1 288 ? -12.01200 30.31200 22.86900 1.000 11.84007 ? 722  TYR   A C    1 
ATOM   2181 O  O    . TYR   A 1 288 ? -11.38900 29.45200 22.23900 1.000 18.85761 ? 722  TYR   A O    1 
ATOM   2182 C  CB   . TYR   A 1 288 ? -13.37700 29.34800 24.72100 1.000 10.45654 ? 722  TYR   A CB   1 
ATOM   2183 C  CG   . TYR   A 1 288 ? -13.38900 28.83800 26.13700 1.000 14.66044 ? 722  TYR   A CG   1 
ATOM   2184 C  CD1  . TYR   A 1 288 ? -12.43900 27.92500 26.57300 1.000 13.53992 ? 722  TYR   A CD1  1 
ATOM   2185 C  CD2  . TYR   A 1 288 ? -14.35900 29.25900 27.03800 1.000 8.49473  ? 722  TYR   A CD2  1 
ATOM   2186 C  CE1  . TYR   A 1 288 ? -12.44700 27.45500 27.87200 1.000 15.04256 ? 722  TYR   A CE1  1 
ATOM   2187 C  CE2  . TYR   A 1 288 ? -14.37500 28.79300 28.33700 1.000 10.08075 ? 722  TYR   A CE2  1 
ATOM   2188 C  CZ   . TYR   A 1 288 ? -13.41800 27.89200 28.74700 1.000 9.44674  ? 722  TYR   A CZ   1 
ATOM   2189 O  OH   . TYR   A 1 288 ? -13.43200 27.42800 30.04100 1.000 14.15945 ? 722  TYR   A OH   1 
ATOM   2190 N  N    . ALA   A 1 289 ? -12.57600 31.36300 22.27200 1.000 11.61150 ? 723  ALA   A N    1 
ATOM   2191 C  CA   . ALA   A 1 289 ? -12.40900 31.56900 20.83900 1.000 10.76729 ? 723  ALA   A CA   1 
ATOM   2192 C  C    . ALA   A 1 289 ? -10.95600 31.87200 20.49300 1.000 13.87711 ? 723  ALA   A C    1 
ATOM   2193 O  O    . ALA   A 1 289 ? -10.45100 31.41500 19.46100 1.000 10.30743 ? 723  ALA   A O    1 
ATOM   2194 C  CB   . ALA   A 1 289 ? -13.32400 32.69600 20.36000 1.000 9.25671  ? 723  ALA   A CB   1 
ATOM   2195 N  N    A HIS   A 1 290 ? -10.26800 32.63400 21.34500 0.580 11.32563 ? 724  HIS   A N    1 
ATOM   2196 N  N    B HIS   A 1 290 ? -10.26400 32.63800 21.34400 0.420 11.46066 ? 724  HIS   A N    1 
ATOM   2197 C  CA   A HIS   A 1 290 ? -8.87700  32.97300 21.06900 0.580 11.98966 ? 724  HIS   A CA   1 
ATOM   2198 C  CA   B HIS   A 1 290 ? -8.87400  32.97300 21.05000 0.420 12.06043 ? 724  HIS   A CA   1 
ATOM   2199 C  C    A HIS   A 1 290 ? -7.94700  31.79700 21.33100 0.580 11.79005 ? 724  HIS   A C    1 
ATOM   2200 C  C    B HIS   A 1 290 ? -7.94600  31.79500 21.32500 0.420 11.79199 ? 724  HIS   A C    1 
ATOM   2201 O  O    A HIS   A 1 290 ? -6.96700  31.60900 20.60300 0.580 13.90835 ? 724  HIS   A O    1 
ATOM   2202 O  O    B HIS   A 1 290 ? -6.96300  31.60100 20.60100 0.420 13.95755 ? 724  HIS   A O    1 
ATOM   2203 C  CB   A HIS   A 1 290 ? -8.46100  34.18800 21.89200 0.580 13.88876 ? 724  HIS   A CB   1 
ATOM   2204 C  CB   B HIS   A 1 290 ? -8.43600  34.20200 21.84800 0.420 13.91431 ? 724  HIS   A CB   1 
ATOM   2205 C  CG   A HIS   A 1 290 ? -8.81800  35.48900 21.24800 0.580 14.65554 ? 724  HIS   A CG   1 
ATOM   2206 C  CG   B HIS   A 1 290 ? -7.43200  35.05800 21.13600 0.420 16.35271 ? 724  HIS   A CG   1 
ATOM   2207 N  ND1  A HIS   A 1 290 ? -7.93900  36.18600 20.44900 0.580 14.91832 ? 724  HIS   A ND1  1 
ATOM   2208 N  ND1  B HIS   A 1 290 ? -6.22300  34.57100 20.68500 0.420 15.78441 ? 724  HIS   A ND1  1 
ATOM   2209 C  CD2  A HIS   A 1 290 ? -9.96800  36.20200 21.25500 0.580 11.61916 ? 724  HIS   A CD2  1 
ATOM   2210 C  CD2  B HIS   A 1 290 ? -7.45700  36.36900 20.79900 0.420 15.58618 ? 724  HIS   A CD2  1 
ATOM   2211 C  CE1  A HIS   A 1 290 ? -8.52500  37.28400 20.00700 0.580 12.73300 ? 724  HIS   A CE1  1 
ATOM   2212 C  CE1  B HIS   A 1 290 ? -5.54800  35.54500 20.10100 0.420 10.07530 ? 724  HIS   A CE1  1 
ATOM   2213 N  NE2  A HIS   A 1 290 ? -9.75500  37.31800 20.48400 0.580 11.41150 ? 724  HIS   A NE2  1 
ATOM   2214 N  NE2  B HIS   A 1 290 ? -6.27300  36.64700 20.15900 0.420 10.57676 ? 724  HIS   A NE2  1 
ATOM   2215 N  N    . LEU   A 1 291 ? -8.23800  30.99800 22.36000 1.000 14.36040 ? 725  LEU   A N    1 
ATOM   2216 C  CA   . LEU   A 1 291 ? -7.45900  29.78400 22.59300 1.000 12.91029 ? 725  LEU   A CA   1 
ATOM   2217 C  C    . LEU   A 1 291 ? -7.59000  28.82400 21.41700 1.000 11.73794 ? 725  LEU   A C    1 
ATOM   2218 O  O    . LEU   A 1 291 ? -6.60900  28.19600 21.00400 1.000 15.80403 ? 725  LEU   A O    1 
ATOM   2219 C  CB   . LEU   A 1 291 ? -7.90600  29.10000 23.88500 1.000 12.54750 ? 725  LEU   A CB   1 
ATOM   2220 C  CG   . LEU   A 1 291 ? -7.84300  29.87700 25.20000 1.000 12.47065 ? 725  LEU   A CG   1 
ATOM   2221 C  CD1  . LEU   A 1 291 ? -8.06200  28.93200 26.37800 1.000 7.76944  ? 725  LEU   A CD1  1 
ATOM   2222 C  CD2  . LEU   A 1 291 ? -6.51500  30.61700 25.34000 1.000 12.97306 ? 725  LEU   A CD2  1 
ATOM   2223 N  N    . THR   A 1 292 ? -8.79800  28.70600 20.86300 1.000 12.10838 ? 726  THR   A N    1 
ATOM   2224 C  CA   . THR   A 1 292 ? -9.00400  27.88600 19.67400 1.000 10.04688 ? 726  THR   A CA   1 
ATOM   2225 C  C    . THR   A 1 292 ? -8.22900  28.44000 18.48400 1.000 8.63683  ? 726  THR   A C    1 
ATOM   2226 O  O    . THR   A 1 292 ? -7.55900  27.69400 17.76300 1.000 12.36118 ? 726  THR   A O    1 
ATOM   2227 C  CB   . THR   A 1 292 ? -10.49600 27.81600 19.34800 1.000 15.69081 ? 726  THR   A CB   1 
ATOM   2228 O  OG1  . THR   A 1 292 ? -11.20200 27.22200 20.44400 1.000 11.07823 ? 726  THR   A OG1  1 
ATOM   2229 C  CG2  . THR   A 1 292 ? -10.73300 27.00700 18.07800 1.000 8.15432  ? 726  THR   A CG2  1 
ATOM   2230 N  N    . HIS   A 1 293 ? -8.31400  29.75400 18.27200 1.000 8.22038  ? 727  HIS   A N    1 
ATOM   2231 C  CA   . HIS   A 1 293 ? -7.64800  30.39400 17.14200 1.000 8.63820  ? 727  HIS   A CA   1 
ATOM   2232 C  C    . HIS   A 1 293 ? -6.13900  30.16900 17.18000 1.000 15.97747 ? 727  HIS   A C    1 
ATOM   2233 O  O    . HIS   A 1 293 ? -5.51900  29.88100 16.14900 1.000 12.08595 ? 727  HIS   A O    1 
ATOM   2234 C  CB   . HIS   A 1 293 ? -7.97500  31.88800 17.15500 1.000 10.20997 ? 727  HIS   A CB   1 
ATOM   2235 C  CG   . HIS   A 1 293 ? -7.54300  32.62400 15.92700 1.000 10.96767 ? 727  HIS   A CG   1 
ATOM   2236 N  ND1  . HIS   A 1 293 ? -8.26000  32.59400 14.75000 1.000 18.46875 ? 727  HIS   A ND1  1 
ATOM   2237 C  CD2  . HIS   A 1 293 ? -6.48000  33.43000 15.70000 1.000 10.04016 ? 727  HIS   A CD2  1 
ATOM   2238 C  CE1  . HIS   A 1 293 ? -7.64800  33.33900 13.84600 1.000 17.90773 ? 727  HIS   A CE1  1 
ATOM   2239 N  NE2  . HIS   A 1 293 ? -6.56600  33.85800 14.39800 1.000 15.68885 ? 727  HIS   A NE2  1 
ATOM   2240 N  N    . GLN   A 1 294 ? -5.52900  30.30000 18.36400 1.000 13.82867 ? 728  GLN   A N    1 
ATOM   2241 C  CA   . GLN   A 1 294 ? -4.08900  30.10300 18.48500 1.000 8.45686  ? 728  GLN   A CA   1 
ATOM   2242 C  C    . GLN   A 1 294 ? -3.70400  28.65400 18.20900 1.000 18.05980 ? 728  GLN   A C    1 
ATOM   2243 O  O    . GLN   A 1 294 ? -2.69900  28.39000 17.54000 1.000 17.73599 ? 728  GLN   A O    1 
ATOM   2244 C  CB   . GLN   A 1 294 ? -3.61600  30.53500 19.87100 1.000 8.37742  ? 728  GLN   A CB   1 
ATOM   2245 C  CG   . GLN   A 1 294 ? -3.84100  32.01000 20.15400 1.000 14.15534 ? 728  GLN   A CG   1 
ATOM   2246 C  CD   . GLN   A 1 294 ? -3.26700  32.44500 21.48800 1.000 24.08008 ? 728  GLN   A CD   1 
ATOM   2247 O  OE1  . GLN   A 1 294 ? -2.14500  32.08100 21.83900 1.000 34.58591 ? 728  GLN   A OE1  1 
ATOM   2248 N  NE2  . GLN   A 1 294 ? -4.03500  33.23100 22.24000 1.000 26.43809 ? 728  GLN   A NE2  1 
ATOM   2249 N  N    . LEU   A 1 295 ? -4.49200  27.70000 18.71000 1.000 13.45059 ? 729  LEU   A N    1 
ATOM   2250 C  CA   . LEU   A 1 295 ? -4.19700  26.29900 18.43200 1.000 9.62077  ? 729  LEU   A CA   1 
ATOM   2251 C  C    . LEU   A 1 295 ? -4.33000  25.98700 16.94800 1.000 12.92345 ? 729  LEU   A C    1 
ATOM   2252 O  O    . LEU   A 1 295 ? -3.59300  25.14800 16.42100 1.000 11.65110 ? 729  LEU   A O    1 
ATOM   2253 C  CB   . LEU   A 1 295 ? -5.11100  25.39700 19.25800 1.000 12.03212 ? 729  LEU   A CB   1 
ATOM   2254 C  CG   . LEU   A 1 295 ? -4.84700  25.43300 20.76300 1.000 11.66693 ? 729  LEU   A CG   1 
ATOM   2255 C  CD1  . LEU   A 1 295 ? -5.88700  24.61500 21.50900 1.000 7.13813  ? 729  LEU   A CD1  1 
ATOM   2256 C  CD2  . LEU   A 1 295 ? -3.43500  24.92500 21.06300 1.000 9.21989  ? 729  LEU   A CD2  1 
ATOM   2257 N  N    . MET   A 1 296 ? -5.24300  26.67000 16.25500 1.000 16.19956 ? 730  MET   A N    1 
ATOM   2258 C  CA   . MET   A 1 296 ? -5.40800  26.47800 14.81900 1.000 13.18263 ? 730  MET   A CA   1 
ATOM   2259 C  C    . MET   A 1 296 ? -4.17800  26.88400 14.02100 1.000 11.59663 ? 730  MET   A C    1 
ATOM   2260 O  O    . MET   A 1 296 ? -4.09100  26.54300 12.83700 1.000 10.84286 ? 730  MET   A O    1 
ATOM   2261 C  CB   . MET   A 1 296 ? -6.61900  27.26800 14.31500 1.000 12.69437 ? 730  MET   A CB   1 
ATOM   2262 C  CG   . MET   A 1 296 ? -7.95600  26.75100 14.80600 1.000 8.34128  ? 730  MET   A CG   1 
ATOM   2263 S  SD   . MET   A 1 296 ? -9.29800  27.78700 14.21200 1.000 9.57590  ? 730  MET   A SD   1 
ATOM   2264 C  CE   . MET   A 1 296 ? -8.95800  27.79200 12.45600 1.000 13.00792 ? 730  MET   A CE   1 
ATOM   2265 N  N    . SER   A 1 297 ? -3.24000  27.61500 14.61800 1.000 9.97469  ? 731  SER   A N    1 
ATOM   2266 C  CA   . SER   A 1 297 ? -2.00900  27.95100 13.91400 1.000 14.62090 ? 731  SER   A CA   1 
ATOM   2267 C  C    . SER   A 1 297 ? -1.01700  26.79400 13.88400 1.000 14.55076 ? 731  SER   A C    1 
ATOM   2268 O  O    . SER   A 1 297 ? 0.05800   26.93600 13.29200 1.000 9.78237  ? 731  SER   A O    1 
ATOM   2269 C  CB   . SER   A 1 297 ? -1.35300  29.18400 14.54200 1.000 9.54426  ? 731  SER   A CB   1 
ATOM   2270 O  OG   . SER   A 1 297 ? -0.71400  28.86400 15.76200 1.000 12.41779 ? 731  SER   A OG   1 
ATOM   2271 N  N    . LEU   A 1 298 ? -1.35500  25.65800 14.48800 1.000 13.78182 ? 732  LEU   A N    1 
ATOM   2272 C  CA   . LEU   A 1 298 ? -0.47800  24.50200 14.58400 1.000 8.98994  ? 732  LEU   A CA   1 
ATOM   2273 C  C    . LEU   A 1 298 ? -0.97800  23.37100 13.69500 1.000 13.62177 ? 732  LEU   A C    1 
ATOM   2274 O  O    . LEU   A 1 298 ? -2.15800  23.30200 13.34100 1.000 13.17408 ? 732  LEU   A O    1 
ATOM   2275 C  CB   . LEU   A 1 298 ? -0.39200  24.00400 16.03100 1.000 8.56444  ? 732  LEU   A CB   1 
ATOM   2276 C  CG   . LEU   A 1 298 ? -0.02400  25.00200 17.12500 1.000 11.20576 ? 732  LEU   A CG   1 
ATOM   2277 C  CD1  . LEU   A 1 298 ? -0.56300  24.52600 18.47500 1.000 7.98964  ? 732  LEU   A CD1  1 
ATOM   2278 C  CD2  . LEU   A 1 298 ? 1.48600   25.18500 17.18500 1.000 11.27120 ? 732  LEU   A CD2  1 
ATOM   2279 N  N    . ALA   A 1 299 ? -0.05100  22.47600 13.34100 1.000 12.94206 ? 733  ALA   A N    1 
ATOM   2280 C  CA   . ALA   A 1 299 ? -0.37400  21.19000 12.71700 1.000 14.02366 ? 733  ALA   A CA   1 
ATOM   2281 C  C    . ALA   A 1 299 ? -1.21000  21.35100 11.45000 1.000 18.95889 ? 733  ALA   A C    1 
ATOM   2282 O  O    . ALA   A 1 299 ? -2.09500  20.54000 11.16600 1.000 18.45958 ? 733  ALA   A O    1 
ATOM   2283 C  CB   . ALA   A 1 299 ? -1.08300  20.26900 13.71200 1.000 11.90175 ? 733  ALA   A CB   1 
ATOM   2284 N  N    . ALA   A 1 300 ? -0.92100  22.39900 10.67700 1.000 13.59411 ? 734  ALA   A N    1 
ATOM   2285 C  CA   . ALA   A 1 300 ? -1.67700  22.70700 9.46000  1.000 12.78863 ? 734  ALA   A CA   1 
ATOM   2286 C  C    . ALA   A 1 300 ? -3.17400  22.80700 9.73800  1.000 15.61416 ? 734  ALA   A C    1 
ATOM   2287 O  O    . ALA   A 1 300 ? -4.00000  22.47800 8.88500  1.000 12.87472 ? 734  ALA   A O    1 
ATOM   2288 C  CB   . ALA   A 1 300 ? -1.40400  21.67900 8.36000  1.000 11.06550 ? 734  ALA   A CB   1 
ATOM   2289 N  N    . GLY   A 1 301 ? -3.53000  23.26200 10.93800 1.000 13.03569 ? 735  GLY   A N    1 
ATOM   2290 C  CA   . GLY   A 1 301 ? -4.91500  23.43200 11.32700 1.000 9.29304  ? 735  GLY   A CA   1 
ATOM   2291 C  C    . GLY   A 1 301 ? -5.62800  22.17700 11.77600 1.000 8.99783  ? 735  GLY   A C    1 
ATOM   2292 O  O    . GLY   A 1 301 ? -6.84900  22.21700 11.96100 1.000 9.52506  ? 735  GLY   A O    1 
ATOM   2293 N  N    . ARG   A 1 302 ? -4.91100  21.06500 11.96100 1.000 9.20395  ? 736  ARG   A N    1 
ATOM   2294 C  CA   . ARG   A 1 302 ? -5.52100  19.77100 12.28200 1.000 10.22528 ? 736  ARG   A CA   1 
ATOM   2295 C  C    . ARG   A 1 302 ? -5.89200  19.73800 13.76100 1.000 16.68608 ? 736  ARG   A C    1 
ATOM   2296 O  O    . ARG   A 1 302 ? -5.16800  19.20800 14.60700 1.000 12.70095 ? 736  ARG   A O    1 
ATOM   2297 C  CB   . ARG   A 1 302 ? -4.57500  18.62500 11.94300 1.000 12.56357 ? 736  ARG   A CB   1 
ATOM   2298 C  CG   . ARG   A 1 302 ? -4.30800  18.39900 10.46100 1.000 11.87247 ? 736  ARG   A CG   1 
ATOM   2299 C  CD   . ARG   A 1 302 ? -3.49500  17.12200 10.27200 1.000 19.41942 ? 736  ARG   A CD   1 
ATOM   2300 N  NE   . ARG   A 1 302 ? -2.81600  17.06600 8.98300  1.000 22.77293 ? 736  ARG   A NE   1 
ATOM   2301 C  CZ   . ARG   A 1 302 ? -1.54900  17.40500 8.78800  1.000 23.91590 ? 736  ARG   A CZ   1 
ATOM   2302 N  NH1  . ARG   A 1 302 ? -0.78400  17.82600 9.78300  1.000 19.97991 ? 736  ARG   A NH1  1 
ATOM   2303 N  NH2  . ARG   A 1 302 ? -1.03400  17.31500 7.56500  1.000 26.20348 ? 736  ARG   A NH2  1 
ATOM   2304 N  N    . VAL   A 1 303 ? -7.06100  20.29000 14.07600 1.000 11.18934 ? 737  VAL   A N    1 
ATOM   2305 C  CA   . VAL   A 1 303 ? -7.51400  20.41200 15.45500 1.000 12.30093 ? 737  VAL   A CA   1 
ATOM   2306 C  C    . VAL   A 1 303 ? -8.82900  19.66200 15.62100 1.000 7.59236  ? 737  VAL   A C    1 
ATOM   2307 O  O    . VAL   A 1 303 ? -9.72900  19.77800 14.78400 1.000 12.69736 ? 737  VAL   A O    1 
ATOM   2308 C  CB   . VAL   A 1 303 ? -7.66700  21.88700 15.86900 1.000 15.86953 ? 737  VAL   A CB   1 
ATOM   2309 C  CG1  . VAL   A 1 303 ? -8.10300  21.98400 17.32100 1.000 10.66694 ? 737  VAL   A CG1  1 
ATOM   2310 C  CG2  . VAL   A 1 303 ? -6.35400  22.62700 15.64900 1.000 10.80353 ? 737  VAL   A CG2  1 
ATOM   2311 N  N    . LEU   A 1 304 ? -8.92600  18.88500 16.69600 1.000 13.56909 ? 738  LEU   A N    1 
ATOM   2312 C  CA   . LEU   A 1 304 ? -10.16100 18.23100 17.11000 1.000 8.89988  ? 738  LEU   A CA   1 
ATOM   2313 C  C    . LEU   A 1 304 ? -10.48100 18.69700 18.52200 1.000 10.59796 ? 738  LEU   A C    1 
ATOM   2314 O  O    . LEU   A 1 304 ? -9.64900  18.55700 19.42500 1.000 10.41957 ? 738  LEU   A O    1 
ATOM   2315 C  CB   . LEU   A 1 304 ? -10.03000 16.70800 17.06200 1.000 7.45244  ? 738  LEU   A CB   1 
ATOM   2316 C  CG   . LEU   A 1 304 ? -11.16500 15.94400 17.74700 1.000 7.39927  ? 738  LEU   A CG   1 
ATOM   2317 C  CD1  . LEU   A 1 304 ? -12.51000 16.25500 17.08500 1.000 7.52717  ? 738  LEU   A CD1  1 
ATOM   2318 C  CD2  . LEU   A 1 304 ? -10.89300 14.45100 17.74200 1.000 7.65410  ? 738  LEU   A CD2  1 
ATOM   2319 N  N    . ILE   A 1 305 ? -11.67300 19.25200 18.70700 1.000 17.20989 ? 739  ILE   A N    1 
ATOM   2320 C  CA   . ILE   A 1 305 ? -12.11500 19.79400 19.98700 1.000 6.71426  ? 739  ILE   A CA   1 
ATOM   2321 C  C    . ILE   A 1 305 ? -13.06900 18.78500 20.60900 1.000 6.71369  ? 739  ILE   A C    1 
ATOM   2322 O  O    . ILE   A 1 305 ? -14.17400 18.56900 20.10200 1.000 9.39020  ? 739  ILE   A O    1 
ATOM   2323 C  CB   . ILE   A 1 305 ? -12.78800 21.16100 19.81100 1.000 6.79098  ? 739  ILE   A CB   1 
ATOM   2324 C  CG1  . ILE   A 1 305 ? -11.77100 22.19700 19.32800 1.000 9.33607  ? 739  ILE   A CG1  1 
ATOM   2325 C  CG2  . ILE   A 1 305 ? -13.45400 21.60400 21.09700 1.000 6.69102  ? 739  ILE   A CG2  1 
ATOM   2326 C  CD1  . ILE   A 1 305 ? -12.38300 23.54400 19.00200 1.000 14.56869 ? 739  ILE   A CD1  1 
ATOM   2327 N  N    . ILE   A 1 306 ? -12.57900 18.19300 21.68200 1.000 6.58642  ? 740  ILE   A N    1 
ATOM   2328 C  CA   . ILE   A 1 306 ? -13.36600 17.14400 22.37600 1.000 7.93156  ? 740  ILE   A CA   1 
ATOM   2329 C  C    . ILE   A 1 306 ? -14.00400 17.72400 23.65300 1.000 11.23944 ? 740  ILE   A C    1 
ATOM   2330 O  O    . ILE   A 1 306 ? -13.27000 18.11000 24.57200 1.000 7.79750  ? 740  ILE   A O    1 
ATOM   2331 C  CB   . ILE   A 1 306 ? -12.52900 15.88700 22.64700 1.000 7.38561  ? 740  ILE   A CB   1 
ATOM   2332 C  CG1  . ILE   A 1 306 ? -11.95100 15.30400 21.36700 1.000 6.91717  ? 740  ILE   A CG1  1 
ATOM   2333 C  CG2  . ILE   A 1 306 ? -13.34600 14.84900 23.41700 1.000 6.86477  ? 740  ILE   A CG2  1 
ATOM   2334 C  CD1  . ILE   A 1 306 ? -10.91100 14.22800 21.60500 1.000 7.06746  ? 740  ILE   A CD1  1 
ATOM   2335 N  N    . LEU   A 1 307 ? -15.33300 17.76000 23.68000 1.000 6.70068  ? 741  LEU   A N    1 
ATOM   2336 C  CA   . LEU   A 1 307 ? -16.04200 18.22300 24.90100 1.000 6.72541  ? 741  LEU   A CA   1 
ATOM   2337 C  C    . LEU   A 1 307 ? -15.63700 17.36400 26.11100 1.000 8.82530  ? 741  LEU   A C    1 
ATOM   2338 O  O    . LEU   A 1 307 ? -15.63500 16.13900 25.99300 1.000 6.82236  ? 741  LEU   A O    1 
ATOM   2339 C  CB   . LEU   A 1 307 ? -17.55700 18.21200 24.75800 1.000 6.97280  ? 741  LEU   A CB   1 
ATOM   2340 C  CG   . LEU   A 1 307 ? -18.37200 18.55600 26.00900 1.000 7.11140  ? 741  LEU   A CG   1 
ATOM   2341 C  CD1  . LEU   A 1 307 ? -18.16100 20.00100 26.41000 1.000 7.07741  ? 741  LEU   A CD1  1 
ATOM   2342 C  CD2  . LEU   A 1 307 ? -19.85600 18.25500 25.83800 1.000 7.43965  ? 741  LEU   A CD2  1 
ATOM   2343 N  N    . GLU   A 1 308 ? -15.31100 18.00900 27.22500 1.000 6.65167  ? 742  GLU   A N    1 
ATOM   2344 C  CA   . GLU   A 1 308 ? -15.02200 17.26700 28.47600 1.000 7.91191  ? 742  GLU   A CA   1 
ATOM   2345 C  C    . GLU   A 1 308 ? -16.05500 17.71600 29.52800 1.000 7.27371  ? 742  GLU   A C    1 
ATOM   2346 O  O    . GLU   A 1 308 ? -17.22600 17.44800 29.35000 1.000 8.16622  ? 742  GLU   A O    1 
ATOM   2347 C  CB   . GLU   A 1 308 ? -13.55100 17.51900 28.84400 1.000 6.57381  ? 742  GLU   A CB   1 
ATOM   2348 C  CG   . GLU   A 1 308 ? -12.56000 16.87200 27.88700 1.000 7.16418  ? 742  GLU   A CG   1 
ATOM   2349 C  CD   . GLU   A 1 308 ? -12.16800 15.46100 28.27300 1.000 11.18735 ? 742  GLU   A CD   1 
ATOM   2350 O  OE1  . GLU   A 1 308 ? -12.80200 14.88600 29.17500 1.000 17.28726 ? 742  GLU   A OE1  1 
ATOM   2351 O  OE2  . GLU   A 1 308 ? -11.23200 14.94100 27.65100 1.000 9.97977  ? 742  GLU   A OE2  1 
ATOM   2352 N  N    . GLY   A 1 309 ? -15.59400 18.43400 30.55300 1.000 6.92578  ? 743  GLY   A N    1 
ATOM   2353 C  CA   . GLY   A 1 309 ? -16.48300 18.97500 31.58300 1.000 7.18917  ? 743  GLY   A CA   1 
ATOM   2354 C  C    . GLY   A 1 309 ? -17.17400 20.24500 31.12200 1.000 9.76948  ? 743  GLY   A C    1 
ATOM   2355 O  O    . GLY   A 1 309 ? -17.18100 20.51600 29.91600 1.000 11.38227 ? 743  GLY   A O    1 
ATOM   2356 N  N    . GLY   A 1 310 ? -17.65300 21.04700 32.06500 1.000 7.53435  ? 744  GLY   A N    1 
ATOM   2357 C  CA   . GLY   A 1 310 ? -18.48000 22.20100 31.69100 1.000 10.56769 ? 744  GLY   A CA   1 
ATOM   2358 C  C    . GLY   A 1 310 ? -19.87800 21.86800 32.16700 1.000 12.37907 ? 744  GLY   A C    1 
ATOM   2359 O  O    . GLY   A 1 310 ? -20.46600 20.94100 31.60800 1.000 12.10594 ? 744  GLY   A O    1 
ATOM   2360 N  N    . TYR   A 1 311 ? -20.39300 22.59000 33.17200 1.000 11.55528 ? 745  TYR   A N    1 
ATOM   2361 C  CA   . TYR   A 1 311 ? -21.67100 22.19400 33.83800 1.000 11.78029 ? 745  TYR   A CA   1 
ATOM   2362 C  C    . TYR   A 1 311 ? -22.71000 23.31300 33.88400 1.000 15.73698 ? 745  TYR   A C    1 
ATOM   2363 O  O    . TYR   A 1 311 ? -23.78000 23.07100 34.42100 1.000 18.30330 ? 745  TYR   A O    1 
ATOM   2364 C  CB   . TYR   A 1 311 ? -21.27900 21.63000 35.20400 1.000 11.17885 ? 745  TYR   A CB   1 
ATOM   2365 C  CG   . TYR   A 1 311 ? -20.29500 20.49000 35.01600 1.000 13.89737 ? 745  TYR   A CG   1 
ATOM   2366 C  CD1  . TYR   A 1 311 ? -20.72400 19.25700 34.54300 1.000 11.35549 ? 745  TYR   A CD1  1 
ATOM   2367 C  CD2  . TYR   A 1 311 ? -18.93600 20.67700 35.22800 1.000 8.43927  ? 745  TYR   A CD2  1 
ATOM   2368 C  CE1  . TYR   A 1 311 ? -19.83300 18.22300 34.32900 1.000 9.45643  ? 745  TYR   A CE1  1 
ATOM   2369 C  CE2  . TYR   A 1 311 ? -18.03600 19.65200 35.01500 1.000 9.37027  ? 745  TYR   A CE2  1 
ATOM   2370 C  CZ   . TYR   A 1 311 ? -18.48600 18.42300 34.56800 1.000 9.80035  ? 745  TYR   A CZ   1 
ATOM   2371 O  OH   . TYR   A 1 311 ? -17.61600 17.41000 34.34500 1.000 7.94507  ? 745  TYR   A OH   1 
ATOM   2372 N  N    . ASN   A 1 312 ? -22.34800 24.50700 33.43500 1.000 18.42255 ? 746  ASN   A N    1 
ATOM   2373 C  CA   . ASN   A 1 312 ? -23.34500 25.55200 33.24500 1.000 14.35268 ? 746  ASN   A CA   1 
ATOM   2374 C  C    . ASN   A 1 312 ? -23.86800 25.41900 31.81800 1.000 20.52772 ? 746  ASN   A C    1 
ATOM   2375 O  O    . ASN   A 1 312 ? -23.12600 25.64500 30.85700 1.000 13.75338 ? 746  ASN   A O    1 
ATOM   2376 C  CB   . ASN   A 1 312 ? -22.73500 26.92800 33.49700 1.000 13.95998 ? 746  ASN   A CB   1 
ATOM   2377 C  CG   . ASN   A 1 312 ? -23.75900 28.03800 33.44600 1.000 15.43417 ? 746  ASN   A CG   1 
ATOM   2378 O  OD1  . ASN   A 1 312 ? -24.28800 28.36200 32.38300 1.000 15.05554 ? 746  ASN   A OD1  1 
ATOM   2379 N  ND2  . ASN   A 1 312 ? -24.04100 28.63700 34.59900 1.000 13.61347 ? 746  ASN   A ND2  1 
ATOM   2380 N  N    . LEU   A 1 313 ? -25.14000 25.03500 31.67800 1.000 15.56326 ? 747  LEU   A N    1 
ATOM   2381 C  CA   . LEU   A 1 313 ? -25.66400 24.69300 30.35700 1.000 13.39447 ? 747  LEU   A CA   1 
ATOM   2382 C  C    . LEU   A 1 313 ? -25.54200 25.85800 29.38100 1.000 12.94097 ? 747  LEU   A C    1 
ATOM   2383 O  O    . LEU   A 1 313 ? -25.22700 25.65800 28.20400 1.000 11.44847 ? 747  LEU   A O    1 
ATOM   2384 C  CB   . LEU   A 1 313 ? -27.11700 24.23600 30.47000 1.000 12.99438 ? 747  LEU   A CB   1 
ATOM   2385 C  CG   . LEU   A 1 313 ? -27.36700 23.00900 31.34900 1.000 14.46095 ? 747  LEU   A CG   1 
ATOM   2386 C  CD1  . LEU   A 1 313 ? -28.83600 22.62800 31.33400 1.000 11.41005 ? 747  LEU   A CD1  1 
ATOM   2387 C  CD2  . LEU   A 1 313 ? -26.50200 21.84400 30.91600 1.000 13.36625 ? 747  LEU   A CD2  1 
ATOM   2388 N  N    . THR   A 1 314 ? -25.77700 27.08200 29.84900 1.000 12.65683 ? 748  THR   A N    1 
ATOM   2389 C  CA   . THR   A 1 314 ? -25.69200 28.23500 28.96000 1.000 14.18486 ? 748  THR   A CA   1 
ATOM   2390 C  C    . THR   A 1 314 ? -24.24200 28.58500 28.64100 1.000 13.74031 ? 748  THR   A C    1 
ATOM   2391 O  O    . THR   A 1 314 ? -23.89600 28.84500 27.48200 1.000 10.51357 ? 748  THR   A O    1 
ATOM   2392 C  CB   . THR   A 1 314 ? -26.41000 29.43000 29.58600 1.000 11.83466 ? 748  THR   A CB   1 
ATOM   2393 O  OG1  . THR   A 1 314 ? -27.79700 29.11300 29.74300 1.000 13.34907 ? 748  THR   A OG1  1 
ATOM   2394 C  CG2  . THR   A 1 314 ? -26.27100 30.66200 28.70600 1.000 12.14626 ? 748  THR   A CG2  1 
ATOM   2395 N  N    . SER   A 1 315 ? -23.37900 28.59600 29.65900 1.000 14.30098 ? 749  SER   A N    1 
ATOM   2396 C  CA   . SER   A 1 315 ? -21.98400 28.96400 29.43900 1.000 16.46747 ? 749  SER   A CA   1 
ATOM   2397 C  C    . SER   A 1 315 ? -21.28800 27.98000 28.50400 1.000 10.63058 ? 749  SER   A C    1 
ATOM   2398 O  O    . SER   A 1 315 ? -20.49400 28.38500 27.65000 1.000 11.41623 ? 749  SER   A O    1 
ATOM   2399 C  CB   . SER   A 1 315 ? -21.25200 29.04900 30.77700 1.000 13.01327 ? 749  SER   A CB   1 
ATOM   2400 O  OG   . SER   A 1 315 ? -21.92000 29.93600 31.65700 1.000 15.31645 ? 749  SER   A OG   1 
ATOM   2401 N  N    . ILE   A 1 316 ? -21.57000 26.68500 28.64900 1.000 9.13389  ? 750  ILE   A N    1 
ATOM   2402 C  CA   . ILE   A 1 316 ? -20.88100 25.70300 27.81800 1.000 8.51728  ? 750  ILE   A CA   1 
ATOM   2403 C  C    . ILE   A 1 316 ? -21.44300 25.69300 26.39800 1.000 10.22883 ? 750  ILE   A C    1 
ATOM   2404 O  O    . ILE   A 1 316 ? -20.70900 25.42600 25.44100 1.000 13.47846 ? 750  ILE   A O    1 
ATOM   2405 C  CB   . ILE   A 1 316 ? -20.94600 24.30600 28.45900 1.000 8.59046  ? 750  ILE   A CB   1 
ATOM   2406 C  CG1  . ILE   A 1 316 ? -22.36900 23.74600 28.40300 1.000 11.53021 ? 750  ILE   A CG1  1 
ATOM   2407 C  CG2  . ILE   A 1 316 ? -20.45600 24.35400 29.89100 1.000 9.75164  ? 750  ILE   A CG2  1 
ATOM   2408 C  CD1  . ILE   A 1 316 ? -22.51300 22.37800 29.05000 1.000 13.79144 ? 750  ILE   A CD1  1 
ATOM   2409 N  N    . SER   A 1 317 ? -22.73100 25.98600 26.22700 1.000 10.07147 ? 751  SER   A N    1 
ATOM   2410 C  CA   . SER   A 1 317 ? -23.26600 26.10400 24.87700 1.000 11.31981 ? 751  SER   A CA   1 
ATOM   2411 C  C    . SER   A 1 317 ? -22.70200 27.33400 24.17900 1.000 11.59814 ? 751  SER   A C    1 
ATOM   2412 O  O    . SER   A 1 317 ? -22.31200 27.26900 23.00700 1.000 10.10597 ? 751  SER   A O    1 
ATOM   2413 C  CB   . SER   A 1 317 ? -24.79300 26.15400 24.91900 1.000 9.85358  ? 751  SER   A CB   1 
ATOM   2414 O  OG   . SER   A 1 317 ? -25.32200 24.97400 25.50000 1.000 9.79052  ? 751  SER   A OG   1 
ATOM   2415 N  N    . GLU   A 1 318 ? -22.63800 28.46000 24.88900 1.000 10.30050 ? 752  GLU   A N    1 
ATOM   2416 C  CA   . GLU   A 1 318 ? -22.04200 29.66100 24.31700 1.000 16.46965 ? 752  GLU   A CA   1 
ATOM   2417 C  C    . GLU   A 1 318 ? -20.55700 29.45700 24.02600 1.000 9.37980  ? 752  GLU   A C    1 
ATOM   2418 O  O    . GLU   A 1 318 ? -20.05600 29.88800 22.98100 1.000 11.85116 ? 752  GLU   A O    1 
ATOM   2419 C  CB   . GLU   A 1 318 ? -22.24500 30.84200 25.26600 1.000 14.24324 ? 752  GLU   A CB   1 
ATOM   2420 C  CG   . GLU   A 1 318 ? -22.38500 32.17200 24.56000 1.000 23.26329 ? 752  GLU   A CG   1 
ATOM   2421 C  CD   . GLU   A 1 318 ? -23.63900 32.23700 23.71900 1.000 17.30954 ? 752  GLU   A CD   1 
ATOM   2422 O  OE1  . GLU   A 1 318 ? -24.71300 31.86600 24.23300 1.000 18.37500 ? 752  GLU   A OE1  1 
ATOM   2423 O  OE2  . GLU   A 1 318 ? -23.55000 32.64200 22.54300 1.000 14.68405 ? 752  GLU   A OE2  1 
ATOM   2424 N  N    . SER   A 1 319 ? -19.84100 28.79200 24.93300 1.000 9.58035  ? 753  SER   A N    1 
ATOM   2425 C  CA   . SER   A 1 319 ? -18.39400 28.66000 24.78900 1.000 8.52240  ? 753  SER   A CA   1 
ATOM   2426 C  C    . SER   A 1 319 ? -18.02600 27.77400 23.60400 1.000 12.18947 ? 753  SER   A C    1 
ATOM   2427 O  O    . SER   A 1 319 ? -17.24500 28.17800 22.73500 1.000 16.11075 ? 753  SER   A O    1 
ATOM   2428 C  CB   . SER   A 1 319 ? -17.79000 28.10800 26.08000 1.000 8.22343  ? 753  SER   A CB   1 
ATOM   2429 O  OG   . SER   A 1 319 ? -17.63200 29.12400 27.05100 1.000 12.09038 ? 753  SER   A OG   1 
ATOM   2430 N  N    . MET   A 1 320 ? -18.56600 26.55300 23.55900 1.000 8.36562  ? 754  MET   A N    1 
ATOM   2431 C  CA   . MET   A 1 320 ? -18.19700 25.63800 22.48600 1.000 11.06374 ? 754  MET   A CA   1 
ATOM   2432 C  C    . MET   A 1 320 ? -18.68400 26.14100 21.13800 1.000 8.60386  ? 754  MET   A C    1 
ATOM   2433 O  O    . MET   A 1 320 ? -18.05100 25.86600 20.11300 1.000 8.06156  ? 754  MET   A O    1 
ATOM   2434 C  CB   . MET   A 1 320 ? -18.73900 24.23700 22.76800 1.000 11.54996 ? 754  MET   A CB   1 
ATOM   2435 C  CG   . MET   A 1 320 ? -18.01200 23.12000 22.02300 1.000 9.08890  ? 754  MET   A CG   1 
ATOM   2436 S  SD   . MET   A 1 320 ? -18.50600 21.49600 22.63400 1.000 8.22777  ? 754  MET   A SD   1 
ATOM   2437 C  CE   . MET   A 1 320 ? -17.32200 20.42900 21.82200 1.000 7.89115  ? 754  MET   A CE   1 
ATOM   2438 N  N    . SER   A 1 321 ? -19.79900 26.87800 21.11700 1.000 10.90940 ? 755  SER   A N    1 
ATOM   2439 C  CA   . SER   A 1 321 ? -20.21600 27.54100 19.88600 1.000 9.01909  ? 755  SER   A CA   1 
ATOM   2440 C  C    . SER   A 1 321 ? -19.13800 28.49700 19.39500 1.000 10.15108 ? 755  SER   A C    1 
ATOM   2441 O  O    . SER   A 1 321 ? -18.82800 28.53500 18.19800 1.000 13.25649 ? 755  SER   A O    1 
ATOM   2442 C  CB   . SER   A 1 321 ? -21.53400 28.28600 20.10400 1.000 9.58784  ? 755  SER   A CB   1 
ATOM   2443 O  OG   . SER   A 1 321 ? -22.62900 27.39000 20.14200 1.000 9.67609  ? 755  SER   A OG   1 
ATOM   2444 N  N    . MET   A 1 322 ? -18.55100 29.27300 20.30700 1.000 13.93075 ? 756  MET   A N    1 
ATOM   2445 C  CA   . MET   A 1 322 ? -17.49100 30.19700 19.92200 1.000 12.58285 ? 756  MET   A CA   1 
ATOM   2446 C  C    . MET   A 1 322 ? -16.31100 29.45800 19.30400 1.000 9.91082  ? 756  MET   A C    1 
ATOM   2447 O  O    . MET   A 1 322 ? -15.73800 29.91500 18.31000 1.000 13.01648 ? 756  MET   A O    1 
ATOM   2448 C  CB   . MET   A 1 322 ? -17.03500 31.01100 21.13400 1.000 14.15743 ? 756  MET   A CB   1 
ATOM   2449 C  CG   . MET   A 1 322 ? -17.77600 32.32300 21.34100 1.000 14.35661 ? 756  MET   A CG   1 
ATOM   2450 S  SD   . MET   A 1 322 ? -17.59700 33.43000 19.93100 1.000 23.87957 ? 756  MET   A SD   1 
ATOM   2451 C  CE   . MET   A 1 322 ? -17.59600 35.01800 20.74800 1.000 16.22843 ? 756  MET   A CE   1 
ATOM   2452 N  N    . CYS   A 1 323 ? -15.93700 28.31200 19.87900 1.000 10.33889 ? 757  CYS   A N    1 
ATOM   2453 C  CA   . CYS   A 1 323 ? -14.80800 27.54700 19.35500 1.000 11.81294 ? 757  CYS   A CA   1 
ATOM   2454 C  C    . CYS   A 1 323 ? -15.08800 27.04900 17.94200 1.000 12.83107 ? 757  CYS   A C    1 
ATOM   2455 O  O    . CYS   A 1 323 ? -14.26300 27.21900 17.03600 1.000 17.95409 ? 757  CYS   A O    1 
ATOM   2456 C  CB   . CYS   A 1 323 ? -14.49100 26.37500 20.28500 1.000 12.44785 ? 757  CYS   A CB   1 
ATOM   2457 S  SG   . CYS   A 1 323 ? -13.96800 26.86700 21.94400 1.000 10.82645 ? 757  CYS   A SG   1 
ATOM   2458 N  N    . THR   A 1 324 ? -16.24600 26.41300 17.74200 1.000 10.26203 ? 758  THR   A N    1 
ATOM   2459 C  CA   . THR   A 1 324 ? -16.62900 25.95400 16.41000 1.000 8.44907  ? 758  THR   A CA   1 
ATOM   2460 C  C    . THR   A 1 324 ? -16.54100 27.08200 15.39600 1.000 10.03818 ? 758  THR   A C    1 
ATOM   2461 O  O    . THR   A 1 324 ? -16.02700 26.89700 14.28700 1.000 9.99700  ? 758  THR   A O    1 
ATOM   2462 C  CB   . THR   A 1 324 ? -18.04800 25.39000 16.43600 1.000 11.61591 ? 758  THR   A CB   1 
ATOM   2463 O  OG1  . THR   A 1 324 ? -18.10500 24.27000 17.32500 1.000 15.92916 ? 758  THR   A OG1  1 
ATOM   2464 C  CG2  . THR   A 1 324 ? -18.46800 24.95000 15.04300 1.000 9.21487  ? 758  THR   A CG2  1 
ATOM   2465 N  N    . SER   A 1 325 ? -17.02900 28.26500 15.77300 1.000 10.26976 ? 759  SER   A N    1 
ATOM   2466 C  CA   . SER   A 1 325 ? -16.98700 29.41600 14.88100 1.000 14.50393 ? 759  SER   A CA   1 
ATOM   2467 C  C    . SER   A 1 325 ? -15.55800 29.74700 14.46600 1.000 12.47222 ? 759  SER   A C    1 
ATOM   2468 O  O    . SER   A 1 325 ? -15.31100 30.11300 13.31100 1.000 20.16493 ? 759  SER   A O    1 
ATOM   2469 C  CB   . SER   A 1 325 ? -17.65300 30.61500 15.55800 1.000 10.12788 ? 759  SER   A CB   1 
ATOM   2470 O  OG   . SER   A 1 325 ? -17.46600 31.80100 14.80900 1.000 10.70871 ? 759  SER   A OG   1 
ATOM   2471 N  N    . MET   A 1 326 ? -14.60000 29.61800 15.39000 1.000 11.62613 ? 760  MET   A N    1 
ATOM   2472 C  CA   . MET   A 1 326 ? -13.20300 29.85400 15.03600 1.000 10.25910 ? 760  MET   A CA   1 
ATOM   2473 C  C    . MET   A 1 326 ? -12.69800 28.80400 14.05800 1.000 12.26573 ? 760  MET   A C    1 
ATOM   2474 O  O    . MET   A 1 326 ? -11.99800 29.13600 13.09300 1.000 13.61280 ? 760  MET   A O    1 
ATOM   2475 C  CB   . MET   A 1 326 ? -12.33100 29.87400 16.29100 1.000 8.87388  ? 760  MET   A CB   1 
ATOM   2476 C  CG   . MET   A 1 326 ? -12.64400 31.00300 17.25500 1.000 13.29891 ? 760  MET   A CG   1 
ATOM   2477 S  SD   . MET   A 1 326 ? -12.52200 32.65600 16.53300 1.000 14.22829 ? 760  MET   A SD   1 
ATOM   2478 C  CE   . MET   A 1 326 ? -14.24600 32.99800 16.15700 1.000 10.25809 ? 760  MET   A CE   1 
ATOM   2479 N  N    . LEU   A 1 327 ? -13.03500 27.53300 14.29600 1.000 9.73191  ? 761  LEU   A N    1 
ATOM   2480 C  CA   . LEU   A 1 327 ? -12.68300 26.47200 13.35500 1.000 12.16188 ? 761  LEU   A CA   1 
ATOM   2481 C  C    . LEU   A 1 327 ? -13.21700 26.78000 11.96200 1.000 14.07488 ? 761  LEU   A C    1 
ATOM   2482 O  O    . LEU   A 1 327 ? -12.51300 26.60900 10.95900 1.000 9.66294  ? 761  LEU   A O    1 
ATOM   2483 C  CB   . LEU   A 1 327 ? -13.22800 25.12800 13.84400 1.000 8.64408  ? 761  LEU   A CB   1 
ATOM   2484 C  CG   . LEU   A 1 327 ? -12.77100 24.59000 15.19800 1.000 10.64653 ? 761  LEU   A CG   1 
ATOM   2485 C  CD1  . LEU   A 1 327 ? -13.48700 23.28800 15.50600 1.000 10.34655 ? 761  LEU   A CD1  1 
ATOM   2486 C  CD2  . LEU   A 1 327 ? -11.26700 24.38600 15.23000 1.000 9.85882  ? 761  LEU   A CD2  1 
ATOM   2487 N  N    . LEU   A 1 328 ? -14.46700 27.24800 11.88700 1.000 11.33899 ? 762  LEU   A N    1 
ATOM   2488 C  CA   . LEU   A 1 328 ? -15.08200 27.61600 10.61900 1.000 13.34456 ? 762  LEU   A CA   1 
ATOM   2489 C  C    . LEU   A 1 328 ? -14.41800 28.81800 9.96000  1.000 15.99185 ? 762  LEU   A C    1 
ATOM   2490 O  O    . LEU   A 1 328 ? -14.78000 29.15800 8.82800  1.000 15.75720 ? 762  LEU   A O    1 
ATOM   2491 C  CB   . LEU   A 1 328 ? -16.57100 27.89600 10.83300 1.000 16.75747 ? 762  LEU   A CB   1 
ATOM   2492 C  CG   . LEU   A 1 328 ? -17.41900 26.64900 11.07400 1.000 19.79663 ? 762  LEU   A CG   1 
ATOM   2493 C  CD1  . LEU   A 1 328 ? -18.76900 27.02000 11.65800 1.000 15.58174 ? 762  LEU   A CD1  1 
ATOM   2494 C  CD2  . LEU   A 1 328 ? -17.58400 25.89100 9.76300  1.000 10.62515 ? 762  LEU   A CD2  1 
ATOM   2495 N  N    . GLY   A 1 329 ? -13.47000 29.46500 10.63000 1.000 11.83602 ? 763  GLY   A N    1 
ATOM   2496 C  CA   . GLY   A 1 329 ? -12.70500 30.53900 10.03600 1.000 11.21613 ? 763  GLY   A CA   1 
ATOM   2497 C  C    . GLY   A 1 329 ? -13.21500 31.93600 10.30000 1.000 14.25196 ? 763  GLY   A C    1 
ATOM   2498 O  O    . GLY   A 1 329 ? -12.72600 32.88100 9.67100  1.000 15.70402 ? 763  GLY   A O    1 
ATOM   2499 N  N    . ASP   A 1 330 ? -14.17300 32.10300 11.20600 1.000 14.60670 ? 764  ASP   A N    1 
ATOM   2500 C  CA   . ASP   A 1 330 ? -14.69400 33.43100 11.49400 1.000 13.81283 ? 764  ASP   A CA   1 
ATOM   2501 C  C    . ASP   A 1 330 ? -13.65000 34.28400 12.21200 1.000 14.51431 ? 764  ASP   A C    1 
ATOM   2502 O  O    . ASP   A 1 330 ? -12.80700 33.78300 12.96200 1.000 11.24761 ? 764  ASP   A O    1 
ATOM   2503 C  CB   . ASP   A 1 330 ? -15.96700 33.33200 12.33200 1.000 11.73564 ? 764  ASP   A CB   1 
ATOM   2504 C  CG   . ASP   A 1 330 ? -17.10900 32.68200 11.57600 1.000 14.60103 ? 764  ASP   A CG   1 
ATOM   2505 O  OD1  . ASP   A 1 330 ? -17.18600 32.86500 10.34500 1.000 27.19717 ? 764  ASP   A OD1  1 
ATOM   2506 O  OD2  . ASP   A 1 330 ? -17.93200 31.98700 12.20500 1.000 16.35957 ? 764  ASP   A OD2  1 
ATOM   2507 N  N    . SER   A 1 331 ? -13.70900 35.58500 11.96000 1.000 21.97833 ? 765  SER   A N    1 
ATOM   2508 C  CA   . SER   A 1 331 ? -12.79000 36.51500 12.60100 1.000 22.82606 ? 765  SER   A CA   1 
ATOM   2509 C  C    . SER   A 1 331 ? -12.93400 36.43000 14.11800 1.000 21.19019 ? 765  SER   A C    1 
ATOM   2510 O  O    . SER   A 1 331 ? -14.05900 36.47100 14.63300 1.000 20.21503 ? 765  SER   A O    1 
ATOM   2511 C  CB   . SER   A 1 331 ? -13.06200 37.93800 12.11600 1.000 14.40906 ? 765  SER   A CB   1 
ATOM   2512 O  OG   . SER   A 1 331 ? -12.71600 38.89100 13.10500 1.000 46.82321 ? 765  SER   A OG   1 
ATOM   2513 N  N    . PRO   A 1 332 ? -11.83500 36.29500 14.86300 1.000 28.93286 ? 766  PRO   A N    1 
ATOM   2514 C  CA   . PRO   A 1 332 ? -11.95300 36.15300 16.31300 1.000 23.41991 ? 766  PRO   A CA   1 
ATOM   2515 C  C    . PRO   A 1 332 ? -12.48800 37.42500 16.94300 1.000 27.63754 ? 766  PRO   A C    1 
ATOM   2516 O  O    . PRO   A 1 332 ? -12.23300 38.53700 16.44900 1.000 27.42510 ? 766  PRO   A O    1 
ATOM   2517 C  CB   . PRO   A 1 332 ? -10.50900 35.86200 16.76100 1.000 14.40909 ? 766  PRO   A CB   1 
ATOM   2518 C  CG   . PRO   A 1 332 ? -9.65200  36.34900 15.65300 1.000 23.96760 ? 766  PRO   A CG   1 
ATOM   2519 C  CD   . PRO   A 1 332 ? -10.44500 36.15400 14.39800 1.000 19.84777 ? 766  PRO   A CD   1 
ATOM   2520 N  N    . PRO   A 1 333 ? -13.23700 37.31300 18.03700 1.000 22.76238 ? 767  PRO   A N    1 
ATOM   2521 C  CA   . PRO   A 1 333 ? -13.87800 38.49000 18.62900 1.000 22.82792 ? 767  PRO   A CA   1 
ATOM   2522 C  C    . PRO   A 1 333 ? -12.93200 39.26400 19.53400 1.000 24.98964 ? 767  PRO   A C    1 
ATOM   2523 O  O    . PRO   A 1 333 ? -11.94900 38.73600 20.05100 1.000 25.42646 ? 767  PRO   A O    1 
ATOM   2524 C  CB   . PRO   A 1 333 ? -15.02500 37.88000 19.44000 1.000 25.69859 ? 767  PRO   A CB   1 
ATOM   2525 C  CG   . PRO   A 1 333 ? -14.46000 36.56400 19.89300 1.000 19.05614 ? 767  PRO   A CG   1 
ATOM   2526 C  CD   . PRO   A 1 333 ? -13.57200 36.07800 18.76800 1.000 18.40344 ? 767  PRO   A CD   1 
ATOM   2527 N  N    . SER   A 1 334 ? -13.25700 40.54100 19.72700 1.000 26.07911 ? 768  SER   A N    1 
ATOM   2528 C  CA   . SER   A 1 334 ? -12.49000 41.37300 20.64400 1.000 23.43437 ? 768  SER   A CA   1 
ATOM   2529 C  C    . SER   A 1 334 ? -12.48000 40.75600 22.03800 1.000 24.16779 ? 768  SER   A C    1 
ATOM   2530 O  O    . SER   A 1 334 ? -13.44500 40.12000 22.47000 1.000 25.11779 ? 768  SER   A O    1 
ATOM   2531 C  CB   . SER   A 1 334 ? -13.07000 42.78400 20.69800 1.000 31.41594 ? 768  SER   A CB   1 
ATOM   2532 O  OG   . SER   A 1 334 ? -14.34900 42.78000 21.30500 1.000 51.85536 ? 768  SER   A OG   1 
ATOM   2533 N  N    . LEU   A 1 335 ? -11.37000 40.94700 22.74300 1.000 24.62159 ? 769  LEU   A N    1 
ATOM   2534 C  CA   . LEU   A 1 335 ? -11.14600 40.25900 24.00900 1.000 17.93530 ? 769  LEU   A CA   1 
ATOM   2535 C  C    . LEU   A 1 335 ? -10.57200 41.19200 25.07100 1.000 20.33110 ? 769  LEU   A C    1 
ATOM   2536 O  O    . LEU   A 1 335 ? -9.44500  41.67100 24.94700 1.000 19.50385 ? 769  LEU   A O    1 
ATOM   2537 C  CB   . LEU   A 1 335 ? -10.21100 39.06800 23.78900 1.000 27.39044 ? 769  LEU   A CB   1 
ATOM   2538 C  CG   . LEU   A 1 335 ? -10.04200 38.05700 24.92100 1.000 25.74561 ? 769  LEU   A CG   1 
ATOM   2539 C  CD1  . LEU   A 1 335 ? -11.37300 37.42300 25.26800 1.000 22.79198 ? 769  LEU   A CD1  1 
ATOM   2540 C  CD2  . LEU   A 1 335 ? -9.02800  36.99500 24.52800 1.000 25.11715 ? 769  LEU   A CD2  1 
ATOM   2541 N  N    . THR   A 1 339 ? -4.86800  43.74600 30.63000 1.000 25.97028 ? 773  THR   A N    1 
ATOM   2542 C  CA   . THR   A 1 339 ? -5.39600  43.42800 31.95300 1.000 30.36452 ? 773  THR   A CA   1 
ATOM   2543 C  C    . THR   A 1 339 ? -4.35500  42.65800 32.76500 1.000 37.39429 ? 773  THR   A C    1 
ATOM   2544 O  O    . THR   A 1 339 ? -3.80800  41.66200 32.29100 1.000 36.13496 ? 773  THR   A O    1 
ATOM   2545 C  CB   . THR   A 1 339 ? -6.69200  42.60500 31.85900 1.000 38.87181 ? 773  THR   A CB   1 
ATOM   2546 O  OG1  . THR   A 1 339 ? -7.46200  43.04900 30.73300 1.000 29.61833 ? 773  THR   A OG1  1 
ATOM   2547 C  CG2  . THR   A 1 339 ? -7.51900  42.76900 33.12900 1.000 17.74974 ? 773  THR   A CG2  1 
ATOM   2548 N  N    . PRO   A 1 340 ? -4.07800  43.12100 33.98500 1.000 39.61871 ? 774  PRO   A N    1 
ATOM   2549 C  CA   . PRO   A 1 340 ? -3.00400  42.51400 34.78000 1.000 33.93102 ? 774  PRO   A CA   1 
ATOM   2550 C  C    . PRO   A 1 340 ? -3.42000  41.19100 35.40400 1.000 30.96172 ? 774  PRO   A C    1 
ATOM   2551 O  O    . PRO   A 1 340 ? -4.51800  41.05100 35.94800 1.000 23.91886 ? 774  PRO   A O    1 
ATOM   2552 C  CB   . PRO   A 1 340 ? -2.73000  43.57000 35.85800 1.000 22.50227 ? 774  PRO   A CB   1 
ATOM   2553 C  CG   . PRO   A 1 340 ? -4.03600  44.25900 36.02500 1.000 32.59436 ? 774  PRO   A CG   1 
ATOM   2554 C  CD   . PRO   A 1 340 ? -4.66700  44.29200 34.65800 1.000 38.10081 ? 774  PRO   A CD   1 
ATOM   2555 N  N    . LEU   A 1 341 ? -2.51700  40.21500 35.32100 1.000 26.45786 ? 775  LEU   A N    1 
ATOM   2556 C  CA   . LEU   A 1 341 ? -2.75600  38.91500 35.92700 1.000 15.85399 ? 775  LEU   A CA   1 
ATOM   2557 C  C    . LEU   A 1 341 ? -2.79200  39.02900 37.44400 1.000 26.32216 ? 775  LEU   A C    1 
ATOM   2558 O  O    . LEU   A 1 341 ? -2.14900  39.89700 38.03900 1.000 22.63121 ? 775  LEU   A O    1 
ATOM   2559 C  CB   . LEU   A 1 341 ? -1.66200  37.92200 35.53400 1.000 12.07597 ? 775  LEU   A CB   1 
ATOM   2560 C  CG   . LEU   A 1 341 ? -1.22000  37.80800 34.07600 1.000 16.48327 ? 775  LEU   A CG   1 
ATOM   2561 C  CD1  . LEU   A 1 341 ? -0.27100  36.62000 33.92000 1.000 16.88190 ? 775  LEU   A CD1  1 
ATOM   2562 C  CD2  . LEU   A 1 341 ? -2.41100  37.67200 33.15900 1.000 11.41891 ? 775  LEU   A CD2  1 
ATOM   2563 N  N    . LYS   A 1 342 ? -3.54900  38.13400 38.07400 1.000 24.01622 ? 776  LYS   A N    1 
ATOM   2564 C  CA   . LYS   A 1 342 ? -3.42800  37.98100 39.51400 1.000 13.88128 ? 776  LYS   A CA   1 
ATOM   2565 C  C    . LYS   A 1 342 ? -2.02800  37.49000 39.85000 1.000 19.53932 ? 776  LYS   A C    1 
ATOM   2566 O  O    . LYS   A 1 342 ? -1.39700  36.76900 39.07100 1.000 19.57097 ? 776  LYS   A O    1 
ATOM   2567 C  CB   . LYS   A 1 342 ? -4.47800  37.00900 40.04900 1.000 12.78076 ? 776  LYS   A CB   1 
ATOM   2568 C  CG   . LYS   A 1 342 ? -5.90300  37.36900 39.65100 1.000 19.52225 ? 776  LYS   A CG   1 
ATOM   2569 C  CD   . LYS   A 1 342 ? -6.90000  36.93400 40.70500 1.000 29.94665 ? 776  LYS   A CD   1 
ATOM   2570 C  CE   . LYS   A 1 342 ? -6.64700  35.50600 41.15800 1.000 20.26282 ? 776  LYS   A CE   1 
ATOM   2571 N  NZ   . LYS   A 1 342 ? -7.75900  35.03300 42.02700 1.000 27.57395 ? 776  LYS   A NZ   1 
ATOM   2572 N  N    . THR   A 1 343 ? -1.53800  37.90200 41.02200 1.000 18.20465 ? 777  THR   A N    1 
ATOM   2573 C  CA   . THR   A 1 343 ? -0.15100  37.63300 41.38800 1.000 16.22425 ? 777  THR   A CA   1 
ATOM   2574 C  C    . THR   A 1 343 ? 0.16700   36.14300 41.32700 1.000 15.57183 ? 777  THR   A C    1 
ATOM   2575 O  O    . THR   A 1 343 ? 1.22800   35.74600 40.83400 1.000 13.80088 ? 777  THR   A O    1 
ATOM   2576 C  CB   . THR   A 1 343 ? 0.13500   38.18100 42.78800 1.000 21.37031 ? 777  THR   A CB   1 
ATOM   2577 O  OG1  . THR   A 1 343 ? -0.28700  39.54900 42.86400 1.000 29.97220 ? 777  THR   A OG1  1 
ATOM   2578 C  CG2  . THR   A 1 343 ? 1.62200   38.10100 43.10100 1.000 15.66310 ? 777  THR   A CG2  1 
ATOM   2579 N  N    . SER   A 1 344 ? -0.74800  35.30300 41.81500 1.000 12.79603 ? 778  SER   A N    1 
ATOM   2580 C  CA   . SER   A 1 344 ? -0.49300  33.86600 41.82800 1.000 18.08823 ? 778  SER   A CA   1 
ATOM   2581 C  C    . SER   A 1 344 ? -0.40300  33.29400 40.42000 1.000 12.90310 ? 778  SER   A C    1 
ATOM   2582 O  O    . SER   A 1 344 ? 0.26600   32.27800 40.20800 1.000 13.32598 ? 778  SER   A O    1 
ATOM   2583 C  CB   . SER   A 1 344 ? -1.58400  33.14700 42.60900 1.000 12.14442 ? 778  SER   A CB   1 
ATOM   2584 O  OG   . SER   A 1 344 ? -2.81600  33.24600 41.92400 1.000 11.82554 ? 778  SER   A OG   1 
ATOM   2585 N  N    . ALA   A 1 345 ? -1.08000  33.91500 39.45200 1.000 11.35469 ? 779  ALA   A N    1 
ATOM   2586 C  CA   . ALA   A 1 345 ? -0.98100  33.44500 38.07500 1.000 11.41022 ? 779  ALA   A CA   1 
ATOM   2587 C  C    . ALA   A 1 345 ? 0.39800   33.72900 37.49700 1.000 13.56167 ? 779  ALA   A C    1 
ATOM   2588 O  O    . ALA   A 1 345 ? 0.97200   32.88100 36.80500 1.000 13.93322 ? 779  ALA   A O    1 
ATOM   2589 C  CB   . ALA   A 1 345 ? -2.06300  34.09300 37.22100 1.000 10.68140 ? 779  ALA   A CB   1 
ATOM   2590 N  N    . THR   A 1 346 ? 0.93600   34.92300 37.76200 1.000 19.01171 ? 780  THR   A N    1 
ATOM   2591 C  CA   . THR   A 1 346 ? 2.32300   35.21000 37.41000 1.000 17.70112 ? 780  THR   A CA   1 
ATOM   2592 C  C    . THR   A 1 346 ? 3.26700   34.20100 38.04900 1.000 12.40318 ? 780  THR   A C    1 
ATOM   2593 O  O    . THR   A 1 346 ? 4.20100   33.71200 37.40100 1.000 11.55031 ? 780  THR   A O    1 
ATOM   2594 C  CB   . THR   A 1 346 ? 2.68400   36.63100 37.84400 1.000 13.41161 ? 780  THR   A CB   1 
ATOM   2595 O  OG1  . THR   A 1 346 ? 1.90100   37.56900 37.09700 1.000 18.21859 ? 780  THR   A OG1  1 
ATOM   2596 C  CG2  . THR   A 1 346 ? 4.16000   36.90600 37.61200 1.000 18.58775 ? 780  THR   A CG2  1 
ATOM   2597 N  N    . VAL   A 1 347 ? 3.02400   33.86200 39.31500 1.000 12.19592 ? 781  VAL   A N    1 
ATOM   2598 C  CA   . VAL   A 1 347 ? 3.87300   32.90200 40.01100 1.000 15.20620 ? 781  VAL   A CA   1 
ATOM   2599 C  C    . VAL   A 1 347 ? 3.75600   31.52500 39.37400 1.000 11.28301 ? 781  VAL   A C    1 
ATOM   2600 O  O    . VAL   A 1 347 ? 4.76300   30.83700 39.16400 1.000 18.49036 ? 781  VAL   A O    1 
ATOM   2601 C  CB   . VAL   A 1 347 ? 3.51700   32.86900 41.50900 1.000 12.37557 ? 781  VAL   A CB   1 
ATOM   2602 C  CG1  . VAL   A 1 347 ? 4.22300   31.71800 42.20300 1.000 12.41164 ? 781  VAL   A CG1  1 
ATOM   2603 C  CG2  . VAL   A 1 347 ? 3.87700   34.19400 42.16800 1.000 13.17685 ? 781  VAL   A CG2  1 
ATOM   2604 N  N    . SER   A 1 348 ? 2.53100   31.09900 39.05900 1.000 10.80329 ? 782  SER   A N    1 
ATOM   2605 C  CA   . SER   A 1 348 ? 2.33700   29.79700 38.43000 1.000 10.22904 ? 782  SER   A CA   1 
ATOM   2606 C  C    . SER   A 1 348 ? 3.05100   29.72900 37.08900 1.000 14.23743 ? 782  SER   A C    1 
ATOM   2607 O  O    . SER   A 1 348 ? 3.74600   28.75000 36.79000 1.000 11.31313 ? 782  SER   A O    1 
ATOM   2608 C  CB   . SER   A 1 348 ? 0.84600   29.50800 38.25900 1.000 9.83338  ? 782  SER   A CB   1 
ATOM   2609 O  OG   . SER   A 1 348 ? 0.21700   29.29700 39.51300 1.000 18.26893 ? 782  SER   A OG   1 
ATOM   2610 N  N    . ILE   A 1 349 ? 2.90900   30.77700 36.27500 1.000 12.26810 ? 783  ILE   A N    1 
ATOM   2611 C  CA   . ILE   A 1 349 ? 3.48700   30.77000 34.93400 1.000 10.13075 ? 783  ILE   A CA   1 
ATOM   2612 C  C    . ILE   A 1 349 ? 5.00900   30.71100 35.00700 1.000 15.48018 ? 783  ILE   A C    1 
ATOM   2613 O  O    . ILE   A 1 349 ? 5.65300   29.92800 34.29700 1.000 14.56839 ? 783  ILE   A O    1 
ATOM   2614 C  CB   . ILE   A 1 349 ? 2.99800   31.99300 34.13900 1.000 13.86706 ? 783  ILE   A CB   1 
ATOM   2615 C  CG1  . ILE   A 1 349 ? 1.51500   31.82500 33.78900 1.000 9.57838  ? 783  ILE   A CG1  1 
ATOM   2616 C  CG2  . ILE   A 1 349 ? 3.84800   32.20400 32.89200 1.000 15.82292 ? 783  ILE   A CG2  1 
ATOM   2617 C  CD1  . ILE   A 1 349 ? 0.92200   32.99000 33.02400 1.000 13.57884 ? 783  ILE   A CD1  1 
ATOM   2618 N  N    . ASN   A 1 350 ? 5.60900   31.52400 35.87800 1.000 17.59991 ? 784  ASN   A N    1 
ATOM   2619 C  CA   . ASN   A 1 350 ? 7.06200   31.50300 36.00800 1.000 13.31260 ? 784  ASN   A CA   1 
ATOM   2620 C  C    . ASN   A 1 350 ? 7.57000   30.22500 36.66500 1.000 14.65126 ? 784  ASN   A C    1 
ATOM   2621 O  O    . ASN   A 1 350 ? 8.72900   29.85300 36.45100 1.000 15.33342 ? 784  ASN   A O    1 
ATOM   2622 C  CB   . ASN   A 1 350 ? 7.54700   32.72900 36.78300 1.000 20.43783 ? 784  ASN   A CB   1 
ATOM   2623 C  CG   . ASN   A 1 350 ? 7.62900   33.97000 35.91000 1.000 30.09466 ? 784  ASN   A CG   1 
ATOM   2624 O  OD1  . ASN   A 1 350 ? 6.78100   34.85700 35.98900 1.000 34.22220 ? 784  ASN   A OD1  1 
ATOM   2625 N  ND2  . ASN   A 1 350 ? 8.64700   34.02700 35.05800 1.000 37.31787 ? 784  ASN   A ND2  1 
ATOM   2626 N  N    . ASN   A 1 351 ? 6.73900   29.54100 37.45400 1.000 12.35219 ? 785  ASN   A N    1 
ATOM   2627 C  CA   . ASN   A 1 351 ? 7.15600   28.24800 37.98600 1.000 12.97796 ? 785  ASN   A CA   1 
ATOM   2628 C  C    . ASN   A 1 351 ? 7.19400   27.19400 36.88800 1.000 10.60719 ? 785  ASN   A C    1 
ATOM   2629 O  O    . ASN   A 1 351 ? 8.13500   26.39500 36.82200 1.000 13.22792 ? 785  ASN   A O    1 
ATOM   2630 C  CB   . ASN   A 1 351 ? 6.23300   27.81100 39.12400 1.000 14.58700 ? 785  ASN   A CB   1 
ATOM   2631 C  CG   . ASN   A 1 351 ? 6.52200   28.54600 40.42500 1.000 15.87743 ? 785  ASN   A CG   1 
ATOM   2632 O  OD1  . ASN   A 1 351 ? 7.58100   29.15100 40.59000 1.000 12.11331 ? 785  ASN   A OD1  1 
ATOM   2633 N  ND2  . ASN   A 1 351 ? 5.57800   28.49100 41.35500 1.000 11.64060 ? 785  ASN   A ND2  1 
ATOM   2634 N  N    . VAL   A 1 352 ? 6.18200   27.17500 36.01700 1.000 10.08603 ? 786  VAL   A N    1 
ATOM   2635 C  CA   . VAL   A 1 352 ? 6.22600   26.28100 34.86500 1.000 9.75143  ? 786  VAL   A CA   1 
ATOM   2636 C  C    . VAL   A 1 352 ? 7.40900   26.63200 33.97200 1.000 11.40714 ? 786  VAL   A C    1 
ATOM   2637 O  O    . VAL   A 1 352 ? 8.12300   25.74500 33.48800 1.000 10.11117 ? 786  VAL   A O    1 
ATOM   2638 C  CB   . VAL   A 1 352 ? 4.89800   26.32900 34.08700 1.000 9.84636  ? 786  VAL   A CB   1 
ATOM   2639 C  CG1  . VAL   A 1 352 ? 4.89600   25.28600 32.96500 1.000 8.93385  ? 786  VAL   A CG1  1 
ATOM   2640 C  CG2  . VAL   A 1 352 ? 3.72300   26.11100 35.02300 1.000 12.14580 ? 786  VAL   A CG2  1 
ATOM   2641 N  N    . LEU   A 1 353 ? 7.63900   27.93200 33.75200 1.000 10.25347 ? 787  LEU   A N    1 
ATOM   2642 C  CA   . LEU   A 1 353 ? 8.73700   28.37700 32.89700 1.000 10.59202 ? 787  LEU   A CA   1 
ATOM   2643 C  C    . LEU   A 1 353 ? 10.08100  27.85500 33.39300 1.000 18.40103 ? 787  LEU   A C    1 
ATOM   2644 O  O    . LEU   A 1 353 ? 10.89000  27.34500 32.60800 1.000 11.97789 ? 787  LEU   A O    1 
ATOM   2645 C  CB   . LEU   A 1 353 ? 8.75600   29.90400 32.82100 1.000 10.88418 ? 787  LEU   A CB   1 
ATOM   2646 C  CG   . LEU   A 1 353 ? 7.86200   30.62100 31.80800 1.000 13.77172 ? 787  LEU   A CG   1 
ATOM   2647 C  CD1  . LEU   A 1 353 ? 8.01200   32.12500 31.96300 1.000 11.08331 ? 787  LEU   A CD1  1 
ATOM   2648 C  CD2  . LEU   A 1 353 ? 8.20600   30.19600 30.39000 1.000 11.72013 ? 787  LEU   A CD2  1 
ATOM   2649 N  N    . ARG   A 1 354 ? 10.34800  27.98800 34.69600 1.000 11.42922 ? 788  ARG   A N    1 
ATOM   2650 C  CA   . ARG   A 1 354 ? 11.62500  27.52400 35.22500 1.000 12.99709 ? 788  ARG   A CA   1 
ATOM   2651 C  C    . ARG   A 1 354 ? 11.74200  26.00500 35.17000 1.000 13.46271 ? 788  ARG   A C    1 
ATOM   2652 O  O    . ARG   A 1 354 ? 12.83800  25.47800 34.95400 1.000 17.86143 ? 788  ARG   A O    1 
ATOM   2653 C  CB   . ARG   A 1 354 ? 11.81900  28.00800 36.66100 1.000 14.67146 ? 788  ARG   A CB   1 
ATOM   2654 C  CG   . ARG   A 1 354 ? 12.45500  29.38500 36.79000 1.000 18.93417 ? 788  ARG   A CG   1 
ATOM   2655 C  CD   . ARG   A 1 354 ? 13.03400  29.57500 38.19000 1.000 23.87388 ? 788  ARG   A CD   1 
ATOM   2656 N  NE   . ARG   A 1 354 ? 12.25100  28.84700 39.18100 1.000 15.46352 ? 788  ARG   A NE   1 
ATOM   2657 C  CZ   . ARG   A 1 354 ? 11.16900  29.32500 39.77900 1.000 21.92198 ? 788  ARG   A CZ   1 
ATOM   2658 N  NH1  . ARG   A 1 354 ? 10.74100  30.55700 39.55400 1.000 19.56227 ? 788  ARG   A NH1  1 
ATOM   2659 N  NH2  . ARG   A 1 354 ? 10.50000  28.54800 40.62600 1.000 26.44750 ? 788  ARG   A NH2  1 
ATOM   2660 N  N    . ALA   A 1 355 ? 10.63600  25.28900 35.36200 1.000 11.60521 ? 789  ALA   A N    1 
ATOM   2661 C  CA   . ALA   A 1 355 ? 10.67800  23.83300 35.38100 1.000 13.57326 ? 789  ALA   A CA   1 
ATOM   2662 C  C    . ALA   A 1 355 ? 10.85400  23.22200 33.99700 1.000 12.97402 ? 789  ALA   A C    1 
ATOM   2663 O  O    . ALA   A 1 355 ? 11.35300  22.09500 33.89400 1.000 11.41192 ? 789  ALA   A O    1 
ATOM   2664 C  CB   . ALA   A 1 355 ? 9.40400   23.28100 36.02400 1.000 12.92855 ? 789  ALA   A CB   1 
ATOM   2665 N  N    . HIS   A 1 356 ? 10.46100  23.92700 32.93800 1.000 10.86401 ? 790  HIS   A N    1 
ATOM   2666 C  CA   . HIS   A 1 356 ? 10.53400  23.39200 31.58600 1.000 12.35474 ? 790  HIS   A CA   1 
ATOM   2667 C  C    . HIS   A 1 356 ? 11.60900  24.03500 30.72400 1.000 16.62277 ? 790  HIS   A C    1 
ATOM   2668 O  O    . HIS   A 1 356 ? 11.83800  23.56800 29.60100 1.000 18.70432 ? 790  HIS   A O    1 
ATOM   2669 C  CB   . HIS   A 1 356 ? 9.17000   23.52400 30.89400 1.000 15.90483 ? 790  HIS   A CB   1 
ATOM   2670 C  CG   . HIS   A 1 356 ? 8.22500   22.42000 31.24200 1.000 11.89826 ? 790  HIS   A CG   1 
ATOM   2671 N  ND1  . HIS   A 1 356 ? 8.26400   21.19000 30.62300 1.000 14.13082 ? 790  HIS   A ND1  1 
ATOM   2672 C  CD2  . HIS   A 1 356 ? 7.24000   22.34600 32.16800 1.000 10.88780 ? 790  HIS   A CD2  1 
ATOM   2673 C  CE1  . HIS   A 1 356 ? 7.33100   20.41000 31.14100 1.000 15.06962 ? 790  HIS   A CE1  1 
ATOM   2674 N  NE2  . HIS   A 1 356 ? 6.69900   21.08600 32.08400 1.000 10.15630 ? 790  HIS   A NE2  1 
ATOM   2675 N  N    . ALA   A 1 357 ? 12.26900  25.08000 31.21600 1.000 17.16718 ? 791  ALA   A N    1 
ATOM   2676 C  CA   . ALA   A 1 357 ? 13.44600  25.62300 30.54300 1.000 20.64055 ? 791  ALA   A CA   1 
ATOM   2677 C  C    . ALA   A 1 357 ? 14.45100  24.56000 30.10900 1.000 12.65540 ? 791  ALA   A C    1 
ATOM   2678 O  O    . ALA   A 1 357 ? 14.98000  24.67900 28.99100 1.000 12.88884 ? 791  ALA   A O    1 
ATOM   2679 C  CB   . ALA   A 1 357 ? 14.12200  26.66100 31.44800 1.000 12.55712 ? 791  ALA   A CB   1 
ATOM   2680 N  N    . PRO   A 1 358 ? 14.76100  23.52300 30.90100 1.000 14.04880 ? 792  PRO   A N    1 
ATOM   2681 C  CA   . PRO   A 1 358 ? 15.72400  22.51900 30.42000 1.000 14.14978 ? 792  PRO   A CA   1 
ATOM   2682 C  C    . PRO   A 1 358 ? 15.28700  21.79000 29.16100 1.000 13.01705 ? 792  PRO   A C    1 
ATOM   2683 O  O    . PRO   A 1 358 ? 16.14600  21.38600 28.36800 1.000 13.53009 ? 792  PRO   A O    1 
ATOM   2684 C  CB   . PRO   A 1 358 ? 15.85200  21.55200 31.60800 1.000 13.48421 ? 792  PRO   A CB   1 
ATOM   2685 C  CG   . PRO   A 1 358 ? 14.68900  21.84900 32.50100 1.000 12.90421 ? 792  PRO   A CG   1 
ATOM   2686 C  CD   . PRO   A 1 358 ? 14.43500  23.30300 32.32400 1.000 18.20776 ? 792  PRO   A CD   1 
ATOM   2687 N  N    . PHE   A 1 359 ? 13.98600  21.61500 28.94100 1.000 12.31761 ? 793  PHE   A N    1 
ATOM   2688 C  CA   . PHE   A 1 359 ? 13.51000  20.78500 27.84300 1.000 12.13057 ? 793  PHE   A CA   1 
ATOM   2689 C  C    . PHE   A 1 359 ? 13.06000  21.57300 26.61800 1.000 12.09160 ? 793  PHE   A C    1 
ATOM   2690 O  O    . PHE   A 1 359 ? 13.01700  21.00400 25.52300 1.000 17.04290 ? 793  PHE   A O    1 
ATOM   2691 C  CB   . PHE   A 1 359 ? 12.35500  19.89800 28.32200 1.000 12.86603 ? 793  PHE   A CB   1 
ATOM   2692 C  CG   . PHE   A 1 359 ? 12.60300  19.25400 29.65900 1.000 14.21086 ? 793  PHE   A CG   1 
ATOM   2693 C  CD1  . PHE   A 1 359 ? 13.36400  18.10100 29.76100 1.000 12.46392 ? 793  PHE   A CD1  1 
ATOM   2694 C  CD2  . PHE   A 1 359 ? 12.07400  19.80300 30.81200 1.000 15.13865 ? 793  PHE   A CD2  1 
ATOM   2695 C  CE1  . PHE   A 1 359 ? 13.59500  17.51100 30.99000 1.000 12.76666 ? 793  PHE   A CE1  1 
ATOM   2696 C  CE2  . PHE   A 1 359 ? 12.30200  19.21800 32.04400 1.000 11.89703 ? 793  PHE   A CE2  1 
ATOM   2697 C  CZ   . PHE   A 1 359 ? 13.06200  18.07100 32.13300 1.000 13.73961 ? 793  PHE   A CZ   1 
ATOM   2698 N  N    . TRP   A 1 360 ? 12.73000  22.85600 26.76300 1.000 11.61601 ? 794  TRP   A N    1 
ATOM   2699 C  CA   . TRP   A 1 360 ? 12.19000  23.65600 25.66400 1.000 11.38291 ? 794  TRP   A CA   1 
ATOM   2700 C  C    . TRP   A 1 360 ? 13.02500  24.92400 25.51000 1.000 11.99894 ? 794  TRP   A C    1 
ATOM   2701 O  O    . TRP   A 1 360 ? 12.83300  25.90100 26.24000 1.000 11.73810 ? 794  TRP   A O    1 
ATOM   2702 C  CB   . TRP   A 1 360 ? 10.71900  23.96700 25.90900 1.000 16.34225 ? 794  TRP   A CB   1 
ATOM   2703 C  CG   . TRP   A 1 360 ? 9.91900   22.71300 26.09900 1.000 10.32966 ? 794  TRP   A CG   1 
ATOM   2704 C  CD1  . TRP   A 1 360 ? 9.46400   22.19400 27.27800 1.000 10.52288 ? 794  TRP   A CD1  1 
ATOM   2705 C  CD2  . TRP   A 1 360 ? 9.51700   21.79600 25.07700 1.000 11.35207 ? 794  TRP   A CD2  1 
ATOM   2706 N  NE1  . TRP   A 1 360 ? 8.78100   21.02500 27.04800 1.000 9.89713  ? 794  TRP   A NE1  1 
ATOM   2707 C  CE2  . TRP   A 1 360 ? 8.80600   20.75600 25.70400 1.000 10.28210 ? 794  TRP   A CE2  1 
ATOM   2708 C  CE3  . TRP   A 1 360 ? 9.68400   21.75900 23.69100 1.000 10.43121 ? 794  TRP   A CE3  1 
ATOM   2709 C  CZ2  . TRP   A 1 360 ? 8.25700   19.69200 24.99200 1.000 13.91515 ? 794  TRP   A CZ2  1 
ATOM   2710 C  CZ3  . TRP   A 1 360 ? 9.14200   20.70000 22.98500 1.000 14.37255 ? 794  TRP   A CZ3  1 
ATOM   2711 C  CH2  . TRP   A 1 360 ? 8.43700   19.68100 23.63700 1.000 12.21910 ? 794  TRP   A CH2  1 
ATOM   2712 N  N    . SER   A 1 361 ? 13.94000  24.90200 24.53600 1.000 20.92549 ? 795  SER   A N    1 
ATOM   2713 C  CA   . SER   A 1 361 ? 14.94300  25.95200 24.39200 1.000 14.29115 ? 795  SER   A CA   1 
ATOM   2714 C  C    . SER   A 1 361 ? 14.34700  27.29400 23.98800 1.000 16.56746 ? 795  SER   A C    1 
ATOM   2715 O  O    . SER   A 1 361 ? 14.98900  28.32800 24.19700 1.000 13.20932 ? 795  SER   A O    1 
ATOM   2716 C  CB   . SER   A 1 361 ? 15.99200  25.52500 23.36600 1.000 13.61340 ? 795  SER   A CB   1 
ATOM   2717 O  OG   . SER   A 1 361 ? 16.90000  26.57700 23.10300 1.000 16.48585 ? 795  SER   A OG   1 
ATOM   2718 N  N    . SER   A 1 362 ? 13.14500  27.30800 23.41100 1.000 13.29235 ? 796  SER   A N    1 
ATOM   2719 C  CA   . SER   A 1 362 ? 12.53400  28.56300 22.99400 1.000 14.84534 ? 796  SER   A CA   1 
ATOM   2720 C  C    . SER   A 1 362 ? 11.92000  29.33400 24.15400 1.000 13.99817 ? 796  SER   A C    1 
ATOM   2721 O  O    . SER   A 1 362 ? 11.58200  30.51100 23.98700 1.000 13.57982 ? 796  SER   A O    1 
ATOM   2722 C  CB   . SER   A 1 362 ? 11.47200  28.30000 21.92500 1.000 15.64265 ? 796  SER   A CB   1 
ATOM   2723 O  OG   . SER   A 1 362 ? 10.46100  27.44200 22.41900 1.000 15.54917 ? 796  SER   A OG   1 
ATOM   2724 N  N    . LEU   A 1 363 ? 11.76700  28.70800 25.31400 1.000 18.53226 ? 797  LEU   A N    1 
ATOM   2725 C  CA   . LEU   A 1 363 ? 11.29300  29.40800 26.50000 1.000 15.51878 ? 797  LEU   A CA   1 
ATOM   2726 C  C    . LEU   A 1 363 ? 12.35200  30.38500 26.99700 1.000 12.27613 ? 797  LEU   A C    1 
ATOM   2727 O  O    . LEU   A 1 363 ? 12.06500  31.55800 27.23700 1.000 20.50356 ? 797  LEU   A O    1 
ATOM   2728 C  CB   . LEU   A 1 363 ? 10.92900  28.41400 27.60500 1.000 11.11593 ? 797  LEU   A CB   1 
ATOM   2729 C  CG   . LEU   A 1 363 ? 9.76400   27.46500 27.31300 1.000 16.10660 ? 797  LEU   A CG   1 
ATOM   2730 C  CD1  . LEU   A 1 363 ? 9.60700   26.43600 28.42000 1.000 11.61301 ? 797  LEU   A CD1  1 
ATOM   2731 C  CD2  . LEU   A 1 363 ? 8.47700   28.24900 27.12200 1.000 13.59031 ? 797  LEU   A CD2  1 
ATOM   2732 N  N    . PRO   B 1 8   ? -35.60200 29.99700 83.05200 1.000 30.96347 ? 442  PRO   B N    1 
ATOM   2733 C  CA   . PRO   B 1 8   ? -35.47600 29.48300 81.68600 1.000 30.20581 ? 442  PRO   B CA   1 
ATOM   2734 C  C    . PRO   B 1 8   ? -36.72600 29.76100 80.85600 1.000 30.84551 ? 442  PRO   B C    1 
ATOM   2735 O  O    . PRO   B 1 8   ? -37.55200 28.86800 80.67500 1.000 31.38620 ? 442  PRO   B O    1 
ATOM   2736 C  CB   . PRO   B 1 8   ? -35.28300 27.98000 81.90700 1.000 28.51500 ? 442  PRO   B CB   1 
ATOM   2737 C  CG   . PRO   B 1 8   ? -35.93700 27.69500 83.26700 1.000 31.72513 ? 442  PRO   B CG   1 
ATOM   2738 C  CD   . PRO   B 1 8   ? -36.26100 29.01800 83.93000 1.000 33.11121 ? 442  PRO   B CD   1 
ATOM   2739 N  N    . ILE   B 1 9   ? -36.85200 30.98600 80.34900 1.000 25.16933 ? 443  ILE   B N    1 
ATOM   2740 C  CA   . ILE   B 1 9   ? -38.09200 31.47700 79.76300 1.000 19.11196 ? 443  ILE   B CA   1 
ATOM   2741 C  C    . ILE   B 1 9   ? -37.88100 31.78200 78.28600 1.000 17.88744 ? 443  ILE   B C    1 
ATOM   2742 O  O    . ILE   B 1 9   ? -36.82900 32.29500 77.89100 1.000 17.56791 ? 443  ILE   B O    1 
ATOM   2743 C  CB   . ILE   B 1 9   ? -38.59300 32.73200 80.50900 1.000 21.71349 ? 443  ILE   B CB   1 
ATOM   2744 C  CG1  . ILE   B 1 9   ? -38.68800 32.46100 82.01100 1.000 23.07592 ? 443  ILE   B CG1  1 
ATOM   2745 C  CG2  . ILE   B 1 9   ? -39.93700 33.16900 79.97400 1.000 19.25417 ? 443  ILE   B CG2  1 
ATOM   2746 C  CD1  . ILE   B 1 9   ? -39.19600 33.64500 82.80600 1.000 26.12475 ? 443  ILE   B CD1  1 
ATOM   2747 N  N    . THR   B 1 10  ? -38.88800 31.47200 77.47500 1.000 21.73601 ? 444  THR   B N    1 
ATOM   2748 C  CA   . THR   B 1 10  ? -38.91700 31.83500 76.06500 1.000 16.27275 ? 444  THR   B CA   1 
ATOM   2749 C  C    . THR   B 1 10  ? -39.88500 32.99100 75.86600 1.000 16.32075 ? 444  THR   B C    1 
ATOM   2750 O  O    . THR   B 1 10  ? -41.03400 32.92400 76.31100 1.000 16.56739 ? 444  THR   B O    1 
ATOM   2751 C  CB   . THR   B 1 10  ? -39.34700 30.65500 75.19300 1.000 15.88760 ? 444  THR   B CB   1 
ATOM   2752 O  OG1  . THR   B 1 10  ? -38.41300 29.58200 75.34300 1.000 17.83870 ? 444  THR   B OG1  1 
ATOM   2753 C  CG2  . THR   B 1 10  ? -39.40800 31.06900 73.73000 1.000 14.91256 ? 444  THR   B CG2  1 
ATOM   2754 N  N    . GLY   B 1 11  ? -39.42000 34.04300 75.20900 1.000 15.51989 ? 445  GLY   B N    1 
ATOM   2755 C  CA   . GLY   B 1 11  ? -40.29500 35.12500 74.82800 1.000 15.27333 ? 445  GLY   B CA   1 
ATOM   2756 C  C    . GLY   B 1 11  ? -40.94400 34.88500 73.47600 1.000 20.54349 ? 445  GLY   B C    1 
ATOM   2757 O  O    . GLY   B 1 11  ? -40.44900 34.12200 72.64900 1.000 18.92258 ? 445  GLY   B O    1 
ATOM   2758 N  N    . LEU   B 1 12  ? -42.08500 35.53600 73.27100 1.000 14.41183 ? 446  LEU   B N    1 
ATOM   2759 C  CA   . LEU   B 1 12  ? -42.78300 35.50000 71.99500 1.000 16.61816 ? 446  LEU   B CA   1 
ATOM   2760 C  C    . LEU   B 1 12  ? -43.46600 36.84700 71.81700 1.000 15.20091 ? 446  LEU   B C    1 
ATOM   2761 O  O    . LEU   B 1 12  ? -44.17300 37.30400 72.71900 1.000 15.33238 ? 446  LEU   B O    1 
ATOM   2762 C  CB   . LEU   B 1 12  ? -43.80000 34.34800 71.95000 1.000 13.90361 ? 446  LEU   B CB   1 
ATOM   2763 C  CG   . LEU   B 1 12  ? -44.62600 34.02200 70.69700 1.000 13.39366 ? 446  LEU   B CG   1 
ATOM   2764 C  CD1  . LEU   B 1 12  ? -45.15400 32.60100 70.79600 1.000 13.73550 ? 446  LEU   B CD1  1 
ATOM   2765 C  CD2  . LEU   B 1 12  ? -45.79600 34.98800 70.50400 1.000 13.47407 ? 446  LEU   B CD2  1 
ATOM   2766 N  N    . VAL   B 1 13  ? -43.23800 37.49200 70.67500 1.000 13.50035 ? 447  VAL   B N    1 
ATOM   2767 C  CA   . VAL   B 1 13  ? -43.87200 38.76600 70.36500 1.000 13.83829 ? 447  VAL   B CA   1 
ATOM   2768 C  C    . VAL   B 1 13  ? -44.70800 38.59400 69.10600 1.000 18.37183 ? 447  VAL   B C    1 
ATOM   2769 O  O    . VAL   B 1 13  ? -44.26300 37.97800 68.12800 1.000 12.06644 ? 447  VAL   B O    1 
ATOM   2770 C  CB   . VAL   B 1 13  ? -42.85000 39.91300 70.21200 1.000 13.13367 ? 447  VAL   B CB   1 
ATOM   2771 C  CG1  . VAL   B 1 13  ? -41.95200 39.70800 69.01300 1.000 12.48206 ? 447  VAL   B CG1  1 
ATOM   2772 C  CG2  . VAL   B 1 13  ? -43.56800 41.25800 70.11500 1.000 13.41175 ? 447  VAL   B CG2  1 
ATOM   2773 N  N    . TYR   B 1 14  ? -45.93000 39.11600 69.15200 1.000 12.91881 ? 448  TYR   B N    1 
ATOM   2774 C  CA   . TYR   B 1 14  ? -46.86700 39.06400 68.04400 1.000 12.72489 ? 448  TYR   B CA   1 
ATOM   2775 C  C    . TYR   B 1 14  ? -47.88500 40.17200 68.24800 1.000 13.31108 ? 448  TYR   B C    1 
ATOM   2776 O  O    . TYR   B 1 14  ? -48.31200 40.42200 69.37700 1.000 22.96544 ? 448  TYR   B O    1 
ATOM   2777 C  CB   . TYR   B 1 14  ? -47.56700 37.70500 67.96000 1.000 12.63733 ? 448  TYR   B CB   1 
ATOM   2778 C  CG   . TYR   B 1 14  ? -48.77900 37.70800 67.05500 1.000 18.18284 ? 448  TYR   B CG   1 
ATOM   2779 C  CD1  . TYR   B 1 14  ? -48.63900 37.63200 65.67400 1.000 11.99705 ? 448  TYR   B CD1  1 
ATOM   2780 C  CD2  . TYR   B 1 14  ? -50.06700 37.78300 67.58100 1.000 18.49966 ? 448  TYR   B CD2  1 
ATOM   2781 C  CE1  . TYR   B 1 14  ? -49.74200 37.63500 64.84800 1.000 13.64151 ? 448  TYR   B CE1  1 
ATOM   2782 C  CE2  . TYR   B 1 14  ? -51.17600 37.78300 66.75900 1.000 13.34657 ? 448  TYR   B CE2  1 
ATOM   2783 C  CZ   . TYR   B 1 14  ? -51.00600 37.70900 65.39500 1.000 12.71115 ? 448  TYR   B CZ   1 
ATOM   2784 O  OH   . TYR   B 1 14  ? -52.10000 37.70800 64.57000 1.000 13.12994 ? 448  TYR   B OH   1 
ATOM   2785 N  N    . ASP   B 1 15  ? -48.26700 40.83400 67.15800 1.000 13.64143 ? 449  ASP   B N    1 
ATOM   2786 C  CA   . ASP   B 1 15  ? -49.23200 41.92600 67.24100 1.000 16.24736 ? 449  ASP   B CA   1 
ATOM   2787 C  C    . ASP   B 1 15  ? -50.02200 41.95700 65.94200 1.000 14.31973 ? 449  ASP   B C    1 
ATOM   2788 O  O    . ASP   B 1 15  ? -49.45600 42.22100 64.87900 1.000 18.58837 ? 449  ASP   B O    1 
ATOM   2789 C  CB   . ASP   B 1 15  ? -48.53500 43.25700 67.50000 1.000 29.00325 ? 449  ASP   B CB   1 
ATOM   2790 C  CG   . ASP   B 1 15  ? -49.48000 44.31500 68.03300 1.000 20.47499 ? 449  ASP   B CG   1 
ATOM   2791 O  OD1  . ASP   B 1 15  ? -50.48600 44.61200 67.35800 1.000 23.16028 ? 449  ASP   B OD1  1 
ATOM   2792 O  OD2  . ASP   B 1 15  ? -49.22200 44.84200 69.13100 1.000 16.54525 ? 449  ASP   B OD2  1 
ATOM   2793 N  N    . GLN   B 1 16  ? -51.32900 41.69400 66.03500 1.000 13.46007 ? 450  GLN   B N    1 
ATOM   2794 C  CA   . GLN   B 1 16  ? -52.15800 41.55800 64.84200 1.000 16.20472 ? 450  GLN   B CA   1 
ATOM   2795 C  C    . GLN   B 1 16  ? -52.20100 42.83300 64.00900 1.000 13.22622 ? 450  GLN   B C    1 
ATOM   2796 O  O    . GLN   B 1 16  ? -52.59200 42.77500 62.84000 1.000 15.20531 ? 450  GLN   B O    1 
ATOM   2797 C  CB   . GLN   B 1 16  ? -53.57900 41.14900 65.23500 1.000 17.20138 ? 450  GLN   B CB   1 
ATOM   2798 C  CG   . GLN   B 1 16  ? -54.50500 42.32500 65.49000 1.000 21.37781 ? 450  GLN   B CG   1 
ATOM   2799 C  CD   . GLN   B 1 16  ? -55.68200 41.96500 66.36800 1.000 30.95686 ? 450  GLN   B CD   1 
ATOM   2800 O  OE1  . GLN   B 1 16  ? -55.98300 40.78900 66.57600 1.000 41.05302 ? 450  GLN   B OE1  1 
ATOM   2801 N  NE2  . GLN   B 1 16  ? -56.35000 42.98100 66.90300 1.000 50.68423 ? 450  GLN   B NE2  1 
ATOM   2802 N  N    . ARG   B 1 17  ? -51.81200 43.97900 64.58000 1.000 13.59176 ? 451  ARG   B N    1 
ATOM   2803 C  CA   . ARG   B 1 17  ? -51.72300 45.21200 63.80000 1.000 14.31132 ? 451  ARG   B CA   1 
ATOM   2804 C  C    . ARG   B 1 17  ? -50.80700 45.05700 62.59300 1.000 14.76963 ? 451  ARG   B C    1 
ATOM   2805 O  O    . ARG   B 1 17  ? -50.96600 45.77200 61.59700 1.000 12.86134 ? 451  ARG   B O    1 
ATOM   2806 C  CB   . ARG   B 1 17  ? -51.21800 46.35800 64.67400 1.000 18.21488 ? 451  ARG   B CB   1 
ATOM   2807 C  CG   . ARG   B 1 17  ? -52.28500 47.12700 65.41400 1.000 19.80418 ? 451  ARG   B CG   1 
ATOM   2808 C  CD   . ARG   B 1 17  ? -51.64000 48.20000 66.27600 1.000 26.08413 ? 451  ARG   B CD   1 
ATOM   2809 N  NE   . ARG   B 1 17  ? -50.83200 47.61800 67.34100 1.000 23.27111 ? 451  ARG   B NE   1 
ATOM   2810 C  CZ   . ARG   B 1 17  ? -49.97000 48.29600 68.08700 1.000 25.18519 ? 451  ARG   B CZ   1 
ATOM   2811 N  NH1  . ARG   B 1 17  ? -49.74200 49.58200 67.88100 1.000 19.58685 ? 451  ARG   B NH1  1 
ATOM   2812 N  NH2  . ARG   B 1 17  ? -49.32000 47.66800 69.06100 1.000 19.22818 ? 451  ARG   B NH2  1 
ATOM   2813 N  N    . MET   B 1 18  ? -49.84000 44.14100 62.65800 1.000 13.37000 ? 452  MET   B N    1 
ATOM   2814 C  CA   . MET   B 1 18  ? -48.95400 43.93400 61.52200 1.000 11.77840 ? 452  MET   B CA   1 
ATOM   2815 C  C    . MET   B 1 18  ? -49.66600 43.30500 60.33000 1.000 13.50891 ? 452  MET   B C    1 
ATOM   2816 O  O    . MET   B 1 18  ? -49.05500 43.18100 59.26200 1.000 11.21748 ? 452  MET   B O    1 
ATOM   2817 C  CB   . MET   B 1 18  ? -47.75500 43.08300 61.94700 1.000 11.39742 ? 452  MET   B CB   1 
ATOM   2818 C  CG   . MET   B 1 18  ? -46.64800 43.89200 62.61500 1.000 11.59245 ? 452  MET   B CG   1 
ATOM   2819 S  SD   . MET   B 1 18  ? -45.23000 42.91900 63.17200 1.000 13.37295 ? 452  MET   B SD   1 
ATOM   2820 C  CE   . MET   B 1 18  ? -45.90200 42.16300 64.65200 1.000 16.81306 ? 452  MET   B CE   1 
ATOM   2821 N  N    . MET   B 1 19  ? -50.93800 42.91800 60.48100 1.000 14.26517 ? 453  MET   B N    1 
ATOM   2822 C  CA   . MET   B 1 19  ? -51.72200 42.39600 59.36700 1.000 11.78685 ? 453  MET   B CA   1 
ATOM   2823 C  C    . MET   B 1 19  ? -52.24300 43.49000 58.44600 1.000 13.67917 ? 453  MET   B C    1 
ATOM   2824 O  O    . MET   B 1 19  ? -52.59000 43.19800 57.29600 1.000 13.24735 ? 453  MET   B O    1 
ATOM   2825 C  CB   . MET   B 1 19  ? -52.90800 41.57600 59.88300 1.000 12.17349 ? 453  MET   B CB   1 
ATOM   2826 C  CG   . MET   B 1 19  ? -52.53000 40.28500 60.58800 1.000 12.01797 ? 453  MET   B CG   1 
ATOM   2827 S  SD   . MET   B 1 19  ? -53.97600 39.37900 61.18300 1.000 17.71675 ? 453  MET   B SD   1 
ATOM   2828 C  CE   . MET   B 1 19  ? -54.63400 38.71600 59.65300 1.000 12.69693 ? 453  MET   B CE   1 
ATOM   2829 N  N    . LEU   B 1 20  ? -52.30100 44.73800 58.91700 1.000 12.43751 ? 454  LEU   B N    1 
ATOM   2830 C  CA   . LEU   B 1 20  ? -52.88000 45.81000 58.11300 1.000 12.83895 ? 454  LEU   B CA   1 
ATOM   2831 C  C    . LEU   B 1 20  ? -52.11500 46.04200 56.81300 1.000 14.17929 ? 454  LEU   B C    1 
ATOM   2832 O  O    . LEU   B 1 20  ? -52.69700 46.55400 55.85300 1.000 12.85270 ? 454  LEU   B O    1 
ATOM   2833 C  CB   . LEU   B 1 20  ? -52.93800 47.10000 58.93400 1.000 13.41591 ? 454  LEU   B CB   1 
ATOM   2834 C  CG   . LEU   B 1 20  ? -53.73600 47.03400 60.24300 1.000 13.94880 ? 454  LEU   B CG   1 
ATOM   2835 C  CD1  . LEU   B 1 20  ? -53.42200 48.22600 61.13900 1.000 14.52159 ? 454  LEU   B CD1  1 
ATOM   2836 C  CD2  . LEU   B 1 20  ? -55.23800 46.96400 59.96600 1.000 14.50803 ? 454  LEU   B CD2  1 
ATOM   2837 N  N    . HIS   B 1 21  ? -50.83200 45.68100 56.76300 1.000 12.09003 ? 455  HIS   B N    1 
ATOM   2838 C  CA   . HIS   B 1 21  ? -50.04900 45.78900 55.53600 1.000 11.94491 ? 455  HIS   B CA   1 
ATOM   2839 C  C    . HIS   B 1 21  ? -50.59200 44.82800 54.48500 1.000 13.42170 ? 455  HIS   B C    1 
ATOM   2840 O  O    . HIS   B 1 21  ? -50.58200 43.61000 54.68500 1.000 17.06560 ? 455  HIS   B O    1 
ATOM   2841 C  CB   . HIS   B 1 21  ? -48.58400 45.48700 55.84000 1.000 11.60702 ? 455  HIS   B CB   1 
ATOM   2842 C  CG   . HIS   B 1 21  ? -47.74900 45.22100 54.62700 1.000 11.50768 ? 455  HIS   B CG   1 
ATOM   2843 N  ND1  . HIS   B 1 21  ? -47.54100 46.16200 53.64300 1.000 11.90579 ? 455  HIS   B ND1  1 
ATOM   2844 C  CD2  . HIS   B 1 21  ? -47.05800 44.12000 54.24700 1.000 11.19211 ? 455  HIS   B CD2  1 
ATOM   2845 C  CE1  . HIS   B 1 21  ? -46.75200 45.65600 52.71200 1.000 12.95223 ? 455  HIS   B CE1  1 
ATOM   2846 N  NE2  . HIS   B 1 21  ? -46.44900 44.41600 53.05200 1.000 11.42829 ? 455  HIS   B NE2  1 
ATOM   2847 N  N    . HIS   B 1 22  ? -51.07200 45.35800 53.36200 1.000 12.28105 ? 456  HIS   B N    1 
ATOM   2848 C  CA   . HIS   B 1 22  ? -51.75900 44.49100 52.41400 1.000 12.21237 ? 456  HIS   B CA   1 
ATOM   2849 C  C    . HIS   B 1 22  ? -51.54100 44.96300 50.98600 1.000 12.58066 ? 456  HIS   B C    1 
ATOM   2850 O  O    . HIS   B 1 22  ? -51.17900 46.11400 50.72900 1.000 13.58525 ? 456  HIS   B O    1 
ATOM   2851 C  CB   . HIS   B 1 22  ? -53.26000 44.41000 52.72000 1.000 17.40009 ? 456  HIS   B CB   1 
ATOM   2852 C  CG   . HIS   B 1 22  ? -53.99400 45.69300 52.48700 1.000 17.36951 ? 456  HIS   B CG   1 
ATOM   2853 N  ND1  . HIS   B 1 22  ? -53.94100 46.75200 53.36700 1.000 13.54244 ? 456  HIS   B ND1  1 
ATOM   2854 C  CD2  . HIS   B 1 22  ? -54.79500 46.08900 51.47000 1.000 13.66156 ? 456  HIS   B CD2  1 
ATOM   2855 C  CE1  . HIS   B 1 22  ? -54.67700 47.74500 52.90300 1.000 16.15474 ? 456  HIS   B CE1  1 
ATOM   2856 N  NE2  . HIS   B 1 22  ? -55.20800 47.36800 51.75400 1.000 15.38582 ? 456  HIS   B NE2  1 
ATOM   2857 N  N    . ASN   B 1 23  ? -51.77200 44.03700 50.05700 1.000 16.72585 ? 457  ASN   B N    1 
ATOM   2858 C  CA   . ASN   B 1 23  ? -51.71300 44.29500 48.62200 1.000 13.02117 ? 457  ASN   B CA   1 
ATOM   2859 C  C    . ASN   B 1 23  ? -53.13700 44.56000 48.14700 1.000 16.67429 ? 457  ASN   B C    1 
ATOM   2860 O  O    . ASN   B 1 23  ? -53.94200 43.63100 48.03100 1.000 17.93116 ? 457  ASN   B O    1 
ATOM   2861 C  CB   . ASN   B 1 23  ? -51.09300 43.10400 47.89200 1.000 12.92931 ? 457  ASN   B CB   1 
ATOM   2862 C  CG   . ASN   B 1 23  ? -50.79500 43.39400 46.42900 1.000 17.59426 ? 457  ASN   B CG   1 
ATOM   2863 O  OD1  . ASN   B 1 23  ? -51.61900 43.96200 45.70800 1.000 23.06264 ? 457  ASN   B OD1  1 
ATOM   2864 N  ND2  . ASN   B 1 23  ? -49.60600 43.00000 45.98300 1.000 13.50334 ? 457  ASN   B ND2  1 
ATOM   2865 N  N    . MET   B 1 24  ? -53.44900 45.82600 47.87700 1.000 16.90489 ? 458  MET   B N    1 
ATOM   2866 C  CA   . MET   B 1 24  ? -54.80300 46.20400 47.49100 1.000 14.61229 ? 458  MET   B CA   1 
ATOM   2867 C  C    . MET   B 1 24  ? -55.12500 45.89300 46.03600 1.000 21.22609 ? 458  MET   B C    1 
ATOM   2868 O  O    . MET   B 1 24  ? -56.26400 46.11600 45.61200 1.000 19.75356 ? 458  MET   B O    1 
ATOM   2869 C  CB   . MET   B 1 24  ? -55.02600 47.69300 47.75600 1.000 15.05040 ? 458  MET   B CB   1 
ATOM   2870 C  CG   . MET   B 1 24  ? -53.92500 48.57800 47.22300 1.000 17.55595 ? 458  MET   B CG   1 
ATOM   2871 S  SD   . MET   B 1 24  ? -54.18300 50.30800 47.63600 1.000 37.14890 ? 458  MET   B SD   1 
ATOM   2872 C  CE   . MET   B 1 24  ? -54.68800 50.14000 49.34000 1.000 19.69828 ? 458  MET   B CE   1 
ATOM   2873 N  N    . TRP   B 1 25  ? -54.16300 45.39200 45.26400 1.000 21.95193 ? 459  TRP   B N    1 
ATOM   2874 C  CA   . TRP   B 1 25  ? -54.38600 45.05300 43.86800 1.000 24.48937 ? 459  TRP   B CA   1 
ATOM   2875 C  C    . TRP   B 1 25  ? -54.36900 43.55700 43.60800 1.000 24.29675 ? 459  TRP   B C    1 
ATOM   2876 O  O    . TRP   B 1 25  ? -54.66300 43.13800 42.48400 1.000 41.47500 ? 459  TRP   B O    1 
ATOM   2877 C  CB   . TRP   B 1 25  ? -53.33500 45.74200 42.98400 1.000 19.34233 ? 459  TRP   B CB   1 
ATOM   2878 C  CG   . TRP   B 1 25  ? -53.26300 47.21400 43.23900 1.000 25.85325 ? 459  TRP   B CG   1 
ATOM   2879 C  CD1  . TRP   B 1 25  ? -54.03600 48.18400 42.66800 1.000 30.77742 ? 459  TRP   B CD1  1 
ATOM   2880 C  CD2  . TRP   B 1 25  ? -52.38500 47.88400 44.15000 1.000 33.52434 ? 459  TRP   B CD2  1 
ATOM   2881 N  NE1  . TRP   B 1 25  ? -53.68700 49.41800 43.16200 1.000 36.16748 ? 459  TRP   B NE1  1 
ATOM   2882 C  CE2  . TRP   B 1 25  ? -52.67700 49.26100 44.07400 1.000 34.67893 ? 459  TRP   B CE2  1 
ATOM   2883 C  CE3  . TRP   B 1 25  ? -51.37800 47.45400 45.02200 1.000 30.53268 ? 459  TRP   B CE3  1 
ATOM   2884 C  CZ2  . TRP   B 1 25  ? -51.99900 50.21000 44.83500 1.000 37.69949 ? 459  TRP   B CZ2  1 
ATOM   2885 C  CZ3  . TRP   B 1 25  ? -50.70400 48.40000 45.77600 1.000 36.11802 ? 459  TRP   B CZ3  1 
ATOM   2886 C  CH2  . TRP   B 1 25  ? -51.01800 49.76200 45.67700 1.000 39.86266 ? 459  TRP   B CH2  1 
ATOM   2887 N  N    . ASP   B 1 26  ? -54.04300 42.74600 44.61300 1.000 16.39828 ? 460  ASP   B N    1 
ATOM   2888 C  CA   . ASP   B 1 26  ? -54.02300 41.29000 44.45400 1.000 19.48512 ? 460  ASP   B CA   1 
ATOM   2889 C  C    . ASP   B 1 26  ? -54.08100 40.69900 45.86600 1.000 18.19248 ? 460  ASP   B C    1 
ATOM   2890 O  O    . ASP   B 1 26  ? -53.05000 40.52600 46.51500 1.000 18.69607 ? 460  ASP   B O    1 
ATOM   2891 C  CB   . ASP   B 1 26  ? -52.79200 40.81600 43.70700 1.000 14.86945 ? 460  ASP   B CB   1 
ATOM   2892 C  CG   . ASP   B 1 26  ? -52.72300 39.30000 43.58300 1.000 16.08469 ? 460  ASP   B CG   1 
ATOM   2893 O  OD1  . ASP   B 1 26  ? -53.73700 38.62400 43.86500 1.000 26.82507 ? 460  ASP   B OD1  1 
ATOM   2894 O  OD2  . ASP   B 1 26  ? -51.65100 38.78300 43.20800 1.000 14.94449 ? 460  ASP   B OD2  1 
ATOM   2895 N  N    . SER   B 1 27  ? -55.29700 40.38400 46.31500 1.000 17.20801 ? 461  SER   B N    1 
ATOM   2896 C  CA   . SER   B 1 27  ? -55.52400 39.81800 47.63900 1.000 17.19238 ? 461  SER   B CA   1 
ATOM   2897 C  C    . SER   B 1 27  ? -54.93900 38.42100 47.79500 1.000 22.45002 ? 461  SER   B C    1 
ATOM   2898 O  O    . SER   B 1 27  ? -55.01900 37.85800 48.89200 1.000 18.60917 ? 461  SER   B O    1 
ATOM   2899 C  CB   . SER   B 1 27  ? -57.02200 39.78000 47.93800 1.000 18.31041 ? 461  SER   B CB   1 
ATOM   2900 O  OG   . SER   B 1 27  ? -57.68400 38.87900 47.06600 1.000 22.48728 ? 461  SER   B OG   1 
ATOM   2901 N  N    . HIS   B 1 28  ? -54.37500 37.84100 46.73600 1.000 18.15415 ? 462  HIS   B N    1 
ATOM   2902 C  CA   . HIS   B 1 28  ? -53.74300 36.53100 46.81600 1.000 19.85286 ? 462  HIS   B CA   1 
ATOM   2903 C  C    . HIS   B 1 28  ? -52.22700 36.60500 46.69800 1.000 18.90577 ? 462  HIS   B C    1 
ATOM   2904 O  O    . HIS   B 1 28  ? -51.57400 35.55900 46.60300 1.000 13.57371 ? 462  HIS   B O    1 
ATOM   2905 C  CB   . HIS   B 1 28  ? -54.31200 35.60100 45.74300 1.000 19.52247 ? 462  HIS   B CB   1 
ATOM   2906 C  CG   . HIS   B 1 28  ? -55.71600 35.15800 46.01300 1.000 15.19110 ? 462  HIS   B CG   1 
ATOM   2907 N  ND1  . HIS   B 1 28  ? -56.01200 34.02400 46.73800 1.000 17.14128 ? 462  HIS   B ND1  1 
ATOM   2908 C  CD2  . HIS   B 1 28  ? -56.90500 35.70000 45.66000 1.000 15.83459 ? 462  HIS   B CD2  1 
ATOM   2909 C  CE1  . HIS   B 1 28  ? -57.32400 33.88300 46.81500 1.000 18.38123 ? 462  HIS   B CE1  1 
ATOM   2910 N  NE2  . HIS   B 1 28  ? -57.88900 34.88800 46.17000 1.000 16.16936 ? 462  HIS   B NE2  1 
ATOM   2911 N  N    . HIS   B 1 29  ? -51.65700 37.80800 46.68400 1.000 17.93789 ? 463  HIS   B N    1 
ATOM   2912 C  CA   . HIS   B 1 29  ? -50.21100 37.95000 46.73400 1.000 15.79414 ? 463  HIS   B CA   1 
ATOM   2913 C  C    . HIS   B 1 29  ? -49.67200 37.16500 47.92700 1.000 18.19965 ? 463  HIS   B C    1 
ATOM   2914 O  O    . HIS   B 1 29  ? -50.22500 37.27400 49.03100 1.000 21.28005 ? 463  HIS   B O    1 
ATOM   2915 C  CB   . HIS   B 1 29  ? -49.81700 39.42400 46.85000 1.000 16.98536 ? 463  HIS   B CB   1 
ATOM   2916 C  CG   . HIS   B 1 29  ? -48.34400 39.66400 46.73600 1.000 18.13157 ? 463  HIS   B CG   1 
ATOM   2917 N  ND1  . HIS   B 1 29  ? -47.46000 39.36200 47.75000 1.000 14.57330 ? 463  HIS   B ND1  1 
ATOM   2918 C  CD2  . HIS   B 1 29  ? -47.59800 40.17300 45.72600 1.000 19.02604 ? 463  HIS   B CD2  1 
ATOM   2919 C  CE1  . HIS   B 1 29  ? -46.23400 39.67300 47.36900 1.000 15.98594 ? 463  HIS   B CE1  1 
ATOM   2920 N  NE2  . HIS   B 1 29  ? -46.28900 40.16800 46.14600 1.000 13.64924 ? 463  HIS   B NE2  1 
ATOM   2921 N  N    . PRO   B 1 30  ? -48.60900 36.37500 47.75300 1.000 15.18305 ? 464  PRO   B N    1 
ATOM   2922 C  CA   . PRO   B 1 30  ? -48.24200 35.39900 48.79500 1.000 20.48402 ? 464  PRO   B CA   1 
ATOM   2923 C  C    . PRO   B 1 30  ? -47.87200 36.01100 50.13900 1.000 14.01513 ? 464  PRO   B C    1 
ATOM   2924 O  O    . PRO   B 1 30  ? -48.06000 35.35100 51.16800 1.000 12.00497 ? 464  PRO   B O    1 
ATOM   2925 C  CB   . PRO   B 1 30  ? -47.05300 34.65400 48.16800 1.000 12.45964 ? 464  PRO   B CB   1 
ATOM   2926 C  CG   . PRO   B 1 30  ? -46.49100 35.60900 47.17000 1.000 12.74498 ? 464  PRO   B CG   1 
ATOM   2927 C  CD   . PRO   B 1 30  ? -47.69000 36.32300 46.60500 1.000 13.83744 ? 464  PRO   B CD   1 
ATOM   2928 N  N    . GLU   B 1 31  ? -47.39000 37.26200 50.15600 1.000 12.54043 ? 465  GLU   B N    1 
ATOM   2929 C  CA   . GLU   B 1 31  ? -46.98200 37.94000 51.44000 1.000 16.06845 ? 465  GLU   B CA   1 
ATOM   2930 C  C    . GLU   B 1 31  ? -48.27200 38.43800 52.12400 1.000 17.06140 ? 465  GLU   B C    1 
ATOM   2931 O  O    . GLU   B 1 31  ? -48.45100 39.65200 52.21900 1.000 18.82703 ? 465  GLU   B O    1 
ATOM   2932 C  CB   . GLU   B 1 31  ? -45.84900 38.96400 51.28100 1.000 11.03466 ? 465  GLU   B CB   1 
ATOM   2933 C  CG   . GLU   B 1 31  ? -45.03500 39.21800 52.54700 1.000 14.79043 ? 465  GLU   B CG   1 
ATOM   2934 C  CD   . GLU   B 1 31  ? -45.77600 39.90300 53.67900 1.000 10.51462 ? 465  GLU   B CD   1 
ATOM   2935 O  OE1  . GLU   B 1 31  ? -46.37700 39.18300 54.48500 1.000 10.96466 ? 465  GLU   B OE1  1 
ATOM   2936 O  OE2  . GLU   B 1 31  ? -45.76400 41.13900 53.74100 1.000 10.63808 ? 465  GLU   B OE2  1 
ATOM   2937 N  N    . LEU   B 1 32  ? -49.07200 37.51000 52.62700 1.000 14.58157 ? 466  LEU   B N    1 
ATOM   2938 C  CA   . LEU   B 1 32  ? -50.40800 37.73500 53.15600 1.000 13.70928 ? 466  LEU   B CA   1 
ATOM   2939 C  C    . LEU   B 1 32  ? -50.37000 38.15100 54.62300 1.000 13.59365 ? 466  LEU   B C    1 
ATOM   2940 O  O    . LEU   B 1 32  ? -49.44900 37.78600 55.36300 1.000 11.26629 ? 466  LEU   B O    1 
ATOM   2941 C  CB   . LEU   B 1 32  ? -51.25300 36.47200 53.02100 1.000 11.45755 ? 466  LEU   B CB   1 
ATOM   2942 C  CG   . LEU   B 1 32  ? -51.63300 36.02500 51.61200 1.000 11.87875 ? 466  LEU   B CG   1 
ATOM   2943 C  CD1  . LEU   B 1 32  ? -52.13400 34.59400 51.63200 1.000 14.43795 ? 466  LEU   B CD1  1 
ATOM   2944 C  CD2  . LEU   B 1 32  ? -52.68300 36.94600 51.02100 1.000 15.84614 ? 466  LEU   B CD2  1 
ATOM   2945 N  N    . PRO   B 1 33  ? -51.36200 38.93200 55.05300 1.000 17.63219 ? 467  PRO   B N    1 
ATOM   2946 C  CA   . PRO   B 1 33  ? -51.55100 39.13000 56.49700 1.000 7.93766  ? 467  PRO   B CA   1 
ATOM   2947 C  C    . PRO   B 1 33  ? -51.73200 37.82500 57.24400 1.000 8.01270  ? 467  PRO   B C    1 
ATOM   2948 O  O    . PRO   B 1 33  ? -51.27200 37.69300 58.38500 1.000 12.07671 ? 467  PRO   B O    1 
ATOM   2949 C  CB   . PRO   B 1 33  ? -52.81000 40.00300 56.56100 1.000 8.28496  ? 467  PRO   B CB   1 
ATOM   2950 C  CG   . PRO   B 1 33  ? -52.80500 40.75100 55.27800 1.000 8.32481  ? 467  PRO   B CG   1 
ATOM   2951 C  CD   . PRO   B 1 33  ? -52.22700 39.81400 54.25100 1.000 9.33235  ? 467  PRO   B CD   1 
ATOM   2952 N  N    . GLN   B 1 34  ? -52.37800 36.84200 56.62000 1.000 8.22909  ? 468  GLN   B N    1 
ATOM   2953 C  CA   . GLN   B 1 34  ? -52.67600 35.58200 57.28800 1.000 9.42882  ? 468  GLN   B CA   1 
ATOM   2954 C  C    . GLN   B 1 34  ? -51.43900 34.72800 57.53200 1.000 8.97225  ? 468  GLN   B C    1 
ATOM   2955 O  O    . GLN   B 1 34  ? -51.54300 33.68900 58.19400 1.000 8.31506  ? 468  GLN   B O    1 
ATOM   2956 C  CB   . GLN   B 1 34  ? -53.71000 34.80000 56.47600 1.000 11.99123 ? 468  GLN   B CB   1 
ATOM   2957 C  CG   . GLN   B 1 34  ? -55.14100 35.31800 56.62800 1.000 9.18825  ? 468  GLN   B CG   1 
ATOM   2958 C  CD   . GLN   B 1 34  ? -55.30600 36.74200 56.15300 1.000 9.14816  ? 468  GLN   B CD   1 
ATOM   2959 O  OE1  . GLN   B 1 34  ? -54.73500 37.13800 55.14200 1.000 12.70796 ? 468  GLN   B OE1  1 
ATOM   2960 N  NE2  . GLN   B 1 34  ? -56.08400 37.52700 56.88900 1.000 12.72238 ? 468  GLN   B NE2  1 
ATOM   2961 N  N    . ARG   B 1 35  ? -50.27800 35.12700 57.01500 1.000 7.93795  ? 469  ARG   B N    1 
ATOM   2962 C  CA   . ARG   B 1 35  ? -49.04300 34.45200 57.39200 1.000 8.91902  ? 469  ARG   B CA   1 
ATOM   2963 C  C    . ARG   B 1 35  ? -48.85400 34.48300 58.90600 1.000 8.11104  ? 469  ARG   B C    1 
ATOM   2964 O  O    . ARG   B 1 35  ? -48.73400 33.43700 59.55200 1.000 10.14755 ? 469  ARG   B O    1 
ATOM   2965 C  CB   . ARG   B 1 35  ? -47.85900 35.10100 56.67400 1.000 9.74810  ? 469  ARG   B CB   1 
ATOM   2966 C  CG   . ARG   B 1 35  ? -47.97100 35.05700 55.15200 1.000 12.01175 ? 469  ARG   B CG   1 
ATOM   2967 C  CD   . ARG   B 1 35  ? -46.77000 35.70200 54.47100 1.000 14.39666 ? 469  ARG   B CD   1 
ATOM   2968 N  NE   . ARG   B 1 35  ? -45.51700 35.07900 54.87600 1.000 8.71868  ? 469  ARG   B NE   1 
ATOM   2969 C  CZ   . ARG   B 1 35  ? -44.59000 35.67300 55.61300 1.000 8.52694  ? 469  ARG   B CZ   1 
ATOM   2970 N  NH1  . ARG   B 1 35  ? -44.71500 36.93500 55.99200 1.000 6.80697  ? 469  ARG   B NH1  1 
ATOM   2971 N  NH2  . ARG   B 1 35  ? -43.50900 34.98600 55.97300 1.000 9.54523  ? 469  ARG   B NH2  1 
ATOM   2972 N  N    . ILE   B 1 36  ? -48.87500 35.67700 59.49600 1.000 13.16644 ? 470  ILE   B N    1 
ATOM   2973 C  CA   . ILE   B 1 36  ? -48.58800 35.78000 60.92300 1.000 13.63150 ? 470  ILE   B CA   1 
ATOM   2974 C  C    . ILE   B 1 36  ? -49.75800 35.29700 61.77200 1.000 15.23656 ? 470  ILE   B C    1 
ATOM   2975 O  O    . ILE   B 1 36  ? -49.54800 34.76000 62.86600 1.000 13.21852 ? 470  ILE   B O    1 
ATOM   2976 C  CB   . ILE   B 1 36  ? -48.18500 37.21900 61.29000 1.000 20.35517 ? 470  ILE   B CB   1 
ATOM   2977 C  CG1  . ILE   B 1 36  ? -49.30400 38.20500 60.95000 1.000 9.21572  ? 470  ILE   B CG1  1 
ATOM   2978 C  CG2  . ILE   B 1 36  ? -46.88700 37.60200 60.58500 1.000 12.38144 ? 470  ILE   B CG2  1 
ATOM   2979 C  CD1  . ILE   B 1 36  ? -49.02900 39.61500 61.40200 1.000 9.30500  ? 470  ILE   B CD1  1 
ATOM   2980 N  N    . SER   B 1 37  ? -50.99900 35.46700 61.30700 1.000 11.79561 ? 471  SER   B N    1 
ATOM   2981 C  CA   . SER   B 1 37  ? -52.13200 35.04300 62.12400 1.000 15.82628 ? 471  SER   B CA   1 
ATOM   2982 C  C    . SER   B 1 37  ? -52.30600 33.53000 62.11300 1.000 15.62290 ? 471  SER   B C    1 
ATOM   2983 O  O    . SER   B 1 37  ? -52.78700 32.96100 63.10000 1.000 13.04331 ? 471  SER   B O    1 
ATOM   2984 C  CB   . SER   B 1 37  ? -53.42000 35.73300 61.66200 1.000 8.83870  ? 471  SER   B CB   1 
ATOM   2985 O  OG   . SER   B 1 37  ? -53.74100 35.41000 60.32100 1.000 11.23298 ? 471  SER   B OG   1 
ATOM   2986 N  N    . ARG   B 1 38  ? -51.93300 32.86400 61.01700 1.000 11.07593 ? 472  ARG   B N    1 
ATOM   2987 C  CA   . ARG   B 1 38  ? -51.94300 31.40400 61.01200 1.000 12.64601 ? 472  ARG   B CA   1 
ATOM   2988 C  C    . ARG   B 1 38  ? -50.82800 30.84700 61.88900 1.000 14.56618 ? 472  ARG   B C    1 
ATOM   2989 O  O    . ARG   B 1 38  ? -51.02400 29.84800 62.58900 1.000 26.11808 ? 472  ARG   B O    1 
ATOM   2990 C  CB   . ARG   B 1 38  ? -51.81900 30.87400 59.58300 1.000 18.18760 ? 472  ARG   B CB   1 
ATOM   2991 C  CG   . ARG   B 1 38  ? -53.10900 30.92200 58.77800 1.000 13.49535 ? 472  ARG   B CG   1 
ATOM   2992 C  CD   . ARG   B 1 38  ? -54.06500 29.82100 59.19100 1.000 12.53749 ? 472  ARG   B CD   1 
ATOM   2993 N  NE   . ARG   B 1 38  ? -53.46800 28.50000 59.03000 1.000 21.55153 ? 472  ARG   B NE   1 
ATOM   2994 C  CZ   . ARG   B 1 38  ? -53.50800 27.78900 57.91300 1.000 18.18649 ? 472  ARG   B CZ   1 
ATOM   2995 N  NH1  . ARG   B 1 38  ? -54.11300 28.24000 56.82600 1.000 17.19218 ? 472  ARG   B NH1  1 
ATOM   2996 N  NH2  . ARG   B 1 38  ? -52.92100 26.59500 57.88300 1.000 21.55002 ? 472  ARG   B NH2  1 
ATOM   2997 N  N    . ILE   B 1 39  ? -49.65200 31.48000 61.86800 1.000 8.46229  ? 473  ILE   B N    1 
ATOM   2998 C  CA   . ILE   B 1 39  ? -48.55700 31.04000 62.73000 1.000 10.45969 ? 473  ILE   B CA   1 
ATOM   2999 C  C    . ILE   B 1 39  ? -48.95000 31.17900 64.19400 1.000 13.93975 ? 473  ILE   B C    1 
ATOM   3000 O  O    . ILE   B 1 39  ? -48.80500 30.24100 64.98800 1.000 10.49781 ? 473  ILE   B O    1 
ATOM   3001 C  CB   . ILE   B 1 39  ? -47.27500 31.83100 62.41400 1.000 8.03577  ? 473  ILE   B CB   1 
ATOM   3002 C  CG1  . ILE   B 1 39  ? -46.72300 31.42500 61.04600 1.000 13.77503 ? 473  ILE   B CG1  1 
ATOM   3003 C  CG2  . ILE   B 1 39  ? -46.24100 31.61700 63.50400 1.000 8.06639  ? 473  ILE   B CG2  1 
ATOM   3004 C  CD1  . ILE   B 1 39  ? -45.68800 32.37200 60.49900 1.000 14.86224 ? 473  ILE   B CD1  1 
ATOM   3005 N  N    . PHE   B 1 40  ? -49.45800 32.35400 64.57000 1.000 11.42464 ? 474  PHE   B N    1 
ATOM   3006 C  CA   . PHE   B 1 40  ? -49.88300 32.58400 65.94700 1.000 12.01042 ? 474  PHE   B CA   1 
ATOM   3007 C  C    . PHE   B 1 40  ? -50.94300 31.57200 66.36600 1.000 20.17374 ? 474  PHE   B C    1 
ATOM   3008 O  O    . PHE   B 1 40  ? -50.85700 30.97600 67.44600 1.000 13.74961 ? 474  PHE   B O    1 
ATOM   3009 C  CB   . PHE   B 1 40  ? -50.40300 34.01900 66.08700 1.000 10.57728 ? 474  PHE   B CB   1 
ATOM   3010 C  CG   . PHE   B 1 40  ? -50.82300 34.39200 67.48300 1.000 11.73280 ? 474  PHE   B CG   1 
ATOM   3011 C  CD1  . PHE   B 1 40  ? -49.87800 34.60100 68.47500 1.000 11.62436 ? 474  PHE   B CD1  1 
ATOM   3012 C  CD2  . PHE   B 1 40  ? -52.16300 34.56100 67.79500 1.000 14.31543 ? 474  PHE   B CD2  1 
ATOM   3013 C  CE1  . PHE   B 1 40  ? -50.26200 34.95500 69.75000 1.000 14.93407 ? 474  PHE   B CE1  1 
ATOM   3014 C  CE2  . PHE   B 1 40  ? -52.55500 34.91400 69.07600 1.000 15.14672 ? 474  PHE   B CE2  1 
ATOM   3015 C  CZ   . PHE   B 1 40  ? -51.60400 35.11100 70.05200 1.000 20.70556 ? 474  PHE   B CZ   1 
ATOM   3016 N  N    . SER   B 1 41  ? -51.94300 31.35100 65.50500 1.000 21.84996 ? 475  SER   B N    1 
ATOM   3017 C  CA   . SER   B 1 41  ? -53.01200 30.40900 65.82000 1.000 12.56988 ? 475  SER   B CA   1 
ATOM   3018 C  C    . SER   B 1 41  ? -52.46700 29.01400 66.09800 1.000 11.71694 ? 475  SER   B C    1 
ATOM   3019 O  O    . SER   B 1 41  ? -52.92200 28.33900 67.02900 1.000 14.29767 ? 475  SER   B O    1 
ATOM   3020 C  CB   . SER   B 1 41  ? -54.02800 30.36400 64.67800 1.000 22.79960 ? 475  SER   B CB   1 
ATOM   3021 O  OG   . SER   B 1 41  ? -54.85900 31.51300 64.68000 1.000 17.09242 ? 475  SER   B OG   1 
ATOM   3022 N  N    . ARG   B 1 42  ? -51.49200 28.56000 65.30500 1.000 17.66476 ? 476  ARG   B N    1 
ATOM   3023 C  CA   . ARG   B 1 42  ? -50.95300 27.22100 65.52300 1.000 19.01866 ? 476  ARG   B CA   1 
ATOM   3024 C  C    . ARG   B 1 42  ? -50.16800 27.14000 66.82800 1.000 12.53540 ? 476  ARG   B C    1 
ATOM   3025 O  O    . ARG   B 1 42  ? -50.12700 26.07700 67.45700 1.000 12.71388 ? 476  ARG   B O    1 
ATOM   3026 C  CB   . ARG   B 1 42  ? -50.08300 26.79100 64.33900 1.000 13.55124 ? 476  ARG   B CB   1 
ATOM   3027 C  CG   . ARG   B 1 42  ? -49.79700 25.28900 64.29400 1.000 10.32982 ? 476  ARG   B CG   1 
ATOM   3028 C  CD   . ARG   B 1 42  ? -51.00600 24.48800 63.82200 1.000 10.77955 ? 476  ARG   B CD   1 
ATOM   3029 N  NE   . ARG   B 1 42  ? -50.78600 23.04800 63.92700 1.000 11.24175 ? 476  ARG   B NE   1 
ATOM   3030 C  CZ   . ARG   B 1 42  ? -51.46000 22.23400 64.72900 1.000 15.67884 ? 476  ARG   B CZ   1 
ATOM   3031 N  NH1  . ARG   B 1 42  ? -52.45400 22.66900 65.48500 1.000 23.51314 ? 476  ARG   B NH1  1 
ATOM   3032 N  NH2  . ARG   B 1 42  ? -51.13300 20.94500 64.77000 1.000 20.98623 ? 476  ARG   B NH2  1 
ATOM   3033 N  N    . HIS   B 1 43  ? -49.54500 28.24500 67.25300 1.000 11.02944 ? 477  HIS   B N    1 
ATOM   3034 C  CA   . HIS   B 1 43  ? -48.93100 28.27400 68.57700 1.000 14.66231 ? 477  HIS   B CA   1 
ATOM   3035 C  C    . HIS   B 1 43  ? -49.97900 28.16000 69.67500 1.000 15.14489 ? 477  HIS   B C    1 
ATOM   3036 O  O    . HIS   B 1 43  ? -49.69100 27.63100 70.75500 1.000 11.27719 ? 477  HIS   B O    1 
ATOM   3037 C  CB   . HIS   B 1 43  ? -48.12100 29.55800 68.76900 1.000 16.23448 ? 477  HIS   B CB   1 
ATOM   3038 C  CG   . HIS   B 1 43  ? -46.77400 29.53600 68.11400 1.000 9.63389  ? 477  HIS   B CG   1 
ATOM   3039 N  ND1  . HIS   B 1 43  ? -46.59800 29.75900 66.76500 1.000 9.48818  ? 477  HIS   B ND1  1 
ATOM   3040 C  CD2  . HIS   B 1 43  ? -45.53800 29.33100 68.62600 1.000 9.40640  ? 477  HIS   B CD2  1 
ATOM   3041 C  CE1  . HIS   B 1 43  ? -45.31100 29.68800 66.47400 1.000 11.33079 ? 477  HIS   B CE1  1 
ATOM   3042 N  NE2  . HIS   B 1 43  ? -44.64700 29.42900 67.58600 1.000 9.55991  ? 477  HIS   B NE2  1 
ATOM   3043 N  N    . GLU   B 1 44  ? -51.19400 28.65000 69.41800 1.000 15.22710 ? 478  GLU   B N    1 
ATOM   3044 C  CA   . GLU   B 1 44  ? -52.25800 28.56900 70.41300 1.000 16.89511 ? 478  GLU   B CA   1 
ATOM   3045 C  C    . GLU   B 1 44  ? -52.77300 27.14500 70.55500 1.000 18.42215 ? 478  GLU   B C    1 
ATOM   3046 O  O    . GLU   B 1 44  ? -52.89300 26.62500 71.67100 1.000 12.33727 ? 478  GLU   B O    1 
ATOM   3047 C  CB   . GLU   B 1 44  ? -53.40400 29.50700 70.03600 1.000 15.12279 ? 478  GLU   B CB   1 
ATOM   3048 C  CG   . GLU   B 1 44  ? -53.13600 30.97900 70.27700 1.000 21.50303 ? 478  GLU   B CG   1 
ATOM   3049 C  CD   . GLU   B 1 44  ? -54.35300 31.83300 69.98300 1.000 29.57203 ? 478  GLU   B CD   1 
ATOM   3050 O  OE1  . GLU   B 1 44  ? -54.83500 31.80500 68.82800 1.000 15.99349 ? 478  GLU   B OE1  1 
ATOM   3051 O  OE2  . GLU   B 1 44  ? -54.84100 32.51300 70.91300 1.000 32.11283 ? 478  GLU   B OE2  1 
ATOM   3052 N  N    . GLU   B 1 45  ? -53.10000 26.50000 69.43300 1.000 11.81870 ? 479  GLU   B N    1 
ATOM   3053 C  CA   . GLU   B 1 45  ? -53.66300 25.15700 69.50300 1.000 18.62458 ? 479  GLU   B CA   1 
ATOM   3054 C  C    . GLU   B 1 45  ? -52.64400 24.11900 69.95400 1.000 17.90280 ? 479  GLU   B C    1 
ATOM   3055 O  O    . GLU   B 1 45  ? -53.04000 23.05700 70.44300 1.000 18.19438 ? 479  GLU   B O    1 
ATOM   3056 C  CB   . GLU   B 1 45  ? -54.26900 24.76300 68.15400 1.000 13.41890 ? 479  GLU   B CB   1 
ATOM   3057 C  CG   . GLU   B 1 45  ? -53.53400 25.29000 66.95200 1.000 18.04279 ? 479  GLU   B CG   1 
ATOM   3058 C  CD   . GLU   B 1 45  ? -54.42500 25.40300 65.72400 1.000 19.09469 ? 479  GLU   B CD   1 
ATOM   3059 O  OE1  . GLU   B 1 45  ? -55.53800 25.95500 65.84800 1.000 23.65292 ? 479  GLU   B OE1  1 
ATOM   3060 O  OE2  . GLU   B 1 45  ? -54.01800 24.94800 64.63600 1.000 15.44252 ? 479  GLU   B OE2  1 
ATOM   3061 N  N    . LEU   B 1 46  ? -51.35000 24.40600 69.82600 1.000 14.37691 ? 480  LEU   B N    1 
ATOM   3062 C  CA   . LEU   B 1 46  ? -50.30600 23.48800 70.26000 1.000 14.51053 ? 480  LEU   B CA   1 
ATOM   3063 C  C    . LEU   B 1 46  ? -49.84200 23.75500 71.68500 1.000 19.05902 ? 480  LEU   B C    1 
ATOM   3064 O  O    . LEU   B 1 46  ? -48.87200 23.13300 72.13000 1.000 20.07890 ? 480  LEU   B O    1 
ATOM   3065 C  CB   . LEU   B 1 46  ? -49.11600 23.55400 69.30300 1.000 11.80410 ? 480  LEU   B CB   1 
ATOM   3066 C  CG   . LEU   B 1 46  ? -49.35900 22.85000 67.96800 1.000 11.78406 ? 480  LEU   B CG   1 
ATOM   3067 C  CD1  . LEU   B 1 46  ? -48.16400 23.01100 67.03900 1.000 11.30865 ? 480  LEU   B CD1  1 
ATOM   3068 C  CD2  . LEU   B 1 46  ? -49.65900 21.37900 68.20100 1.000 12.46426 ? 480  LEU   B CD2  1 
ATOM   3069 N  N    . ARG   B 1 47  ? -50.51800 24.65400 72.40400 1.000 20.00259 ? 481  ARG   B N    1 
ATOM   3070 C  CA   . ARG   B 1 47  ? -50.18800 24.98500 73.79200 1.000 20.80559 ? 481  ARG   B CA   1 
ATOM   3071 C  C    . ARG   B 1 47  ? -48.74800 25.46900 73.92800 1.000 18.17527 ? 481  ARG   B C    1 
ATOM   3072 O  O    . ARG   B 1 47  ? -48.06800 25.17300 74.91000 1.000 26.18331 ? 481  ARG   B O    1 
ATOM   3073 C  CB   . ARG   B 1 47  ? -50.44800 23.80000 74.72900 1.000 20.50600 ? 481  ARG   B CB   1 
ATOM   3074 C  CG   . ARG   B 1 47  ? -51.89100 23.31900 74.74200 1.000 32.19863 ? 481  ARG   B CG   1 
ATOM   3075 C  CD   . ARG   B 1 47  ? -52.85000 24.47700 74.96500 1.000 36.19098 ? 481  ARG   B CD   1 
ATOM   3076 N  NE   . ARG   B 1 47  ? -52.47000 25.28500 76.11700 1.000 30.51331 ? 481  ARG   B NE   1 
ATOM   3077 C  CZ   . ARG   B 1 47  ? -52.82000 25.01800 77.36700 1.000 26.81410 ? 481  ARG   B CZ   1 
ATOM   3078 N  NH1  . ARG   B 1 47  ? -53.56500 23.96600 77.66600 1.000 30.32170 ? 481  ARG   B NH1  1 
ATOM   3079 N  NH2  . ARG   B 1 47  ? -52.40600 25.82200 78.34300 1.000 31.88629 ? 481  ARG   B NH2  1 
ATOM   3080 N  N    . LEU   B 1 48  ? -48.27400 26.21300 72.93100 1.000 20.08230 ? 482  LEU   B N    1 
ATOM   3081 C  CA   . LEU   B 1 48  ? -46.94700 26.81800 72.98300 1.000 17.59570 ? 482  LEU   B CA   1 
ATOM   3082 C  C    . LEU   B 1 48  ? -46.97400 28.25600 73.48200 1.000 15.07319 ? 482  LEU   B C    1 
ATOM   3083 O  O    . LEU   B 1 48  ? -46.10900 28.64700 74.26900 1.000 11.27017 ? 482  LEU   B O    1 
ATOM   3084 C  CB   . LEU   B 1 48  ? -46.28600 26.77100 71.60100 1.000 12.53610 ? 482  LEU   B CB   1 
ATOM   3085 C  CG   . LEU   B 1 48  ? -45.96500 25.37200 71.07400 1.000 11.31702 ? 482  LEU   B CG   1 
ATOM   3086 C  CD1  . LEU   B 1 48  ? -45.48200 25.44100 69.63500 1.000 11.58262 ? 482  LEU   B CD1  1 
ATOM   3087 C  CD2  . LEU   B 1 48  ? -44.93500 24.69200 71.95500 1.000 11.63898 ? 482  LEU   B CD2  1 
ATOM   3088 N  N    . LEU   B 1 49  ? -47.95800 29.04400 73.04500 1.000 20.99265 ? 483  LEU   B N    1 
ATOM   3089 C  CA   . LEU   B 1 49  ? -48.05100 30.43600 73.47400 1.000 19.08567 ? 483  LEU   B CA   1 
ATOM   3090 C  C    . LEU   B 1 49  ? -48.21000 30.54500 74.98500 1.000 13.93614 ? 483  LEU   B C    1 
ATOM   3091 O  O    . LEU   B 1 49  ? -47.63400 31.44100 75.61500 1.000 14.20336 ? 483  LEU   B O    1 
ATOM   3092 C  CB   . LEU   B 1 49  ? -49.22000 31.11500 72.76400 1.000 13.19271 ? 483  LEU   B CB   1 
ATOM   3093 C  CG   . LEU   B 1 49  ? -49.51400 32.56800 73.13000 1.000 22.17133 ? 483  LEU   B CG   1 
ATOM   3094 C  CD1  . LEU   B 1 49  ? -48.52600 33.50500 72.46200 1.000 13.82575 ? 483  LEU   B CD1  1 
ATOM   3095 C  CD2  . LEU   B 1 49  ? -50.94900 32.92700 72.76100 1.000 21.87581 ? 483  LEU   B CD2  1 
ATOM   3096 N  N    . SER   B 1 50  ? -48.98500 29.64200 75.58600 1.000 15.67363 ? 484  SER   B N    1 
ATOM   3097 C  CA   . SER   B 1 50  ? -49.17600 29.68400 77.03100 1.000 13.09405 ? 484  SER   B CA   1 
ATOM   3098 C  C    . SER   B 1 50  ? -47.87200 29.44100 77.78000 1.000 17.01553 ? 484  SER   B C    1 
ATOM   3099 O  O    . SER   B 1 50  ? -47.72200 29.88500 78.92300 1.000 16.17471 ? 484  SER   B O    1 
ATOM   3100 C  CB   . SER   B 1 50  ? -50.22500 28.65700 77.45400 1.000 13.14632 ? 484  SER   B CB   1 
ATOM   3101 O  OG   . SER   B 1 50  ? -49.78200 27.33500 77.20700 1.000 17.11162 ? 484  SER   B OG   1 
ATOM   3102 N  N    . ARG   B 1 51  ? -46.92300 28.74400 77.15800 1.000 12.42127 ? 485  ARG   B N    1 
ATOM   3103 C  CA   . ARG   B 1 51  ? -45.64200 28.46600 77.79200 1.000 12.83584 ? 485  ARG   B CA   1 
ATOM   3104 C  C    . ARG   B 1 51  ? -44.63400 29.59500 77.61700 1.000 12.14137 ? 485  ARG   B C    1 
ATOM   3105 O  O    . ARG   B 1 51  ? -43.58600 29.57400 78.27100 1.000 12.34103 ? 485  ARG   B O    1 
ATOM   3106 C  CB   . ARG   B 1 51  ? -45.06200 27.16100 77.23700 1.000 18.60261 ? 485  ARG   B CB   1 
ATOM   3107 C  CG   . ARG   B 1 51  ? -45.99600 25.96100 77.35800 1.000 19.17570 ? 485  ARG   B CG   1 
ATOM   3108 C  CD   . ARG   B 1 51  ? -45.45300 24.76100 76.59300 1.000 20.45819 ? 485  ARG   B CD   1 
ATOM   3109 N  NE   . ARG   B 1 51  ? -44.08600 24.44400 76.98500 1.000 25.00040 ? 485  ARG   B NE   1 
ATOM   3110 C  CZ   . ARG   B 1 51  ? -43.30400 23.58400 76.34800 1.000 24.94665 ? 485  ARG   B CZ   1 
ATOM   3111 N  NH1  . ARG   B 1 51  ? -43.72500 22.92400 75.28100 1.000 18.53652 ? 485  ARG   B NH1  1 
ATOM   3112 N  NH2  . ARG   B 1 51  ? -42.06700 23.38100 76.79300 1.000 19.81787 ? 485  ARG   B NH2  1 
ATOM   3113 N  N    . CYS   B 1 52  ? -44.92300 30.57600 76.76800 1.000 13.23884 ? 486  CYS   B N    1 
ATOM   3114 C  CA   . CYS   B 1 52  ? -44.00400 31.66800 76.48400 1.000 13.76733 ? 486  CYS   B CA   1 
ATOM   3115 C  C    . CYS   B 1 52  ? -44.37000 32.90800 77.29100 1.000 12.27568 ? 486  CYS   B C    1 
ATOM   3116 O  O    . CYS   B 1 52  ? -45.53100 33.12300 77.64100 1.000 17.64084 ? 486  CYS   B O    1 
ATOM   3117 C  CB   . CYS   B 1 52  ? -44.01000 32.01500 74.99200 1.000 12.43606 ? 486  CYS   B CB   1 
ATOM   3118 S  SG   . CYS   B 1 52  ? -43.42000 30.71300 73.88000 1.000 15.08096 ? 486  CYS   B SG   1 
ATOM   3119 N  N    . HIS   B 1 53  ? -43.36000 33.72600 77.58100 1.000 12.87756 ? 487  HIS   B N    1 
ATOM   3120 C  CA   . HIS   B 1 53  ? -43.59000 35.05500 78.13500 1.000 16.81734 ? 487  HIS   B CA   1 
ATOM   3121 C  C    . HIS   B 1 53  ? -43.87400 36.02300 76.99400 1.000 16.17955 ? 487  HIS   B C    1 
ATOM   3122 O  O    . HIS   B 1 53  ? -43.02500 36.22600 76.11900 1.000 19.35733 ? 487  HIS   B O    1 
ATOM   3123 C  CB   . HIS   B 1 53  ? -42.38900 35.52900 78.94900 1.000 13.86624 ? 487  HIS   B CB   1 
ATOM   3124 C  CG   . HIS   B 1 53  ? -42.48700 36.95900 79.38800 1.000 18.23193 ? 487  HIS   B CG   1 
ATOM   3125 N  ND1  . HIS   B 1 53  ? -43.12900 37.34100 80.54600 1.000 18.63007 ? 487  HIS   B ND1  1 
ATOM   3126 C  CD2  . HIS   B 1 53  ? -42.03700 38.10100 78.81500 1.000 15.22365 ? 487  HIS   B CD2  1 
ATOM   3127 C  CE1  . HIS   B 1 53  ? -43.06100 38.65400 80.67300 1.000 27.03048 ? 487  HIS   B CE1  1 
ATOM   3128 N  NE2  . HIS   B 1 53  ? -42.40500 39.14000 79.63500 1.000 20.64751 ? 487  HIS   B NE2  1 
ATOM   3129 N  N    . ARG   B 1 54  ? -45.06200 36.62000 77.00700 1.000 18.43434 ? 488  ARG   B N    1 
ATOM   3130 C  CA   . ARG   B 1 54  ? -45.48800 37.49400 75.92500 1.000 17.93564 ? 488  ARG   B CA   1 
ATOM   3131 C  C    . ARG   B 1 54  ? -44.77500 38.83500 76.03000 1.000 19.51029 ? 488  ARG   B C    1 
ATOM   3132 O  O    . ARG   B 1 54  ? -44.80800 39.48500 77.07900 1.000 14.26391 ? 488  ARG   B O    1 
ATOM   3133 C  CB   . ARG   B 1 54  ? -47.00600 37.68400 75.96500 1.000 11.77238 ? 488  ARG   B CB   1 
ATOM   3134 C  CG   . ARG   B 1 54  ? -47.57800 38.42700 74.77200 1.000 10.18837 ? 488  ARG   B CG   1 
ATOM   3135 C  CD   . ARG   B 1 54  ? -47.51400 37.59700 73.49200 1.000 11.10747 ? 488  ARG   B CD   1 
ATOM   3136 N  NE   . ARG   B 1 54  ? -48.24000 38.25300 72.41100 1.000 11.43381 ? 488  ARG   B NE   1 
ATOM   3137 C  CZ   . ARG   B 1 54  ? -49.51900 38.03700 72.13000 1.000 13.47499 ? 488  ARG   B CZ   1 
ATOM   3138 N  NH1  . ARG   B 1 54  ? -50.22900 37.13900 72.79200 1.000 11.46457 ? 488  ARG   B NH1  1 
ATOM   3139 N  NH2  . ARG   B 1 54  ? -50.09900 38.74100 71.16100 1.000 12.24265 ? 488  ARG   B NH2  1 
ATOM   3140 N  N    . ILE   B 1 55  ? -44.12700 39.23800 74.94700 1.000 14.07957 ? 489  ILE   B N    1 
ATOM   3141 C  CA   . ILE   B 1 55  ? -43.35600 40.47800 74.88900 1.000 15.95274 ? 489  ILE   B CA   1 
ATOM   3142 C  C    . ILE   B 1 55  ? -44.18300 41.52000 74.14400 1.000 14.47641 ? 489  ILE   B C    1 
ATOM   3143 O  O    . ILE   B 1 55  ? -44.69100 41.22100 73.05600 1.000 13.44999 ? 489  ILE   B O    1 
ATOM   3144 C  CB   . ILE   B 1 55  ? -41.99700 40.26000 74.19800 1.000 10.72776 ? 489  ILE   B CB   1 
ATOM   3145 C  CG1  . ILE   B 1 55  ? -41.12400 39.33200 75.04800 1.000 14.32528 ? 489  ILE   B CG1  1 
ATOM   3146 C  CG2  . ILE   B 1 55  ? -41.30200 41.58500 73.93400 1.000 9.31067  ? 489  ILE   B CG2  1 
ATOM   3147 C  CD1  . ILE   B 1 55  ? -39.85100 38.87500 74.36900 1.000 13.71872 ? 489  ILE   B CD1  1 
ATOM   3148 N  N    . PRO   B 1 56  ? -44.35800 42.72200 74.68700 1.000 16.37483 ? 490  PRO   B N    1 
ATOM   3149 C  CA   . PRO   B 1 56  ? -45.15600 43.73200 73.98400 1.000 9.66395  ? 490  PRO   B CA   1 
ATOM   3150 C  C    . PRO   B 1 56  ? -44.46000 44.22100 72.72600 1.000 15.38524 ? 490  PRO   B C    1 
ATOM   3151 O  O    . PRO   B 1 56  ? -43.23800 44.39000 72.69300 1.000 13.78701 ? 490  PRO   B O    1 
ATOM   3152 C  CB   . PRO   B 1 56  ? -45.29100 44.85800 75.01600 1.000 11.83901 ? 490  PRO   B CB   1 
ATOM   3153 C  CG   . PRO   B 1 56  ? -44.12000 44.68300 75.91500 1.000 14.91864 ? 490  PRO   B CG   1 
ATOM   3154 C  CD   . PRO   B 1 56  ? -43.89600 43.19900 76.00100 1.000 16.68638 ? 490  PRO   B CD   1 
ATOM   3155 N  N    . ALA   B 1 57  ? -45.25400 44.45500 71.68800 1.000 14.16849 ? 491  ALA   B N    1 
ATOM   3156 C  CA   . ALA   B 1 57  ? -44.74300 45.06400 70.47300 1.000 11.10261 ? 491  ALA   B CA   1 
ATOM   3157 C  C    . ALA   B 1 57  ? -44.65600 46.57400 70.64600 1.000 17.38807 ? 491  ALA   B C    1 
ATOM   3158 O  O    . ALA   B 1 57  ? -45.31700 47.16600 71.50400 1.000 15.02030 ? 491  ALA   B O    1 
ATOM   3159 C  CB   . ALA   B 1 57  ? -45.63600 44.72700 69.27900 1.000 9.43422  ? 491  ALA   B CB   1 
ATOM   3160 N  N    . ARG   B 1 58  ? -43.82100 47.20100 69.82000 1.000 17.45052 ? 492  ARG   B N    1 
ATOM   3161 C  CA   . ARG   B 1 58  ? -43.74100 48.65400 69.80700 1.000 13.91416 ? 492  ARG   B CA   1 
ATOM   3162 C  C    . ARG   B 1 58  ? -43.26700 49.11100 68.44100 1.000 13.31516 ? 492  ARG   B C    1 
ATOM   3163 O  O    . ARG   B 1 58  ? -42.76600 48.32000 67.63800 1.000 13.91490 ? 492  ARG   B O    1 
ATOM   3164 C  CB   . ARG   B 1 58  ? -42.81300 49.19100 70.90500 1.000 15.20820 ? 492  ARG   B CB   1 
ATOM   3165 C  CG   . ARG   B 1 58  ? -41.32000 49.01400 70.65000 1.000 14.58089 ? 492  ARG   B CG   1 
ATOM   3166 C  CD   . ARG   B 1 58  ? -40.52900 49.83200 71.67400 1.000 9.52584  ? 492  ARG   B CD   1 
ATOM   3167 N  NE   . ARG   B 1 58  ? -39.08800 49.61000 71.61200 1.000 9.48252  ? 492  ARG   B NE   1 
ATOM   3168 C  CZ   . ARG   B 1 58  ? -38.25400 50.28400 70.83300 1.000 12.44106 ? 492  ARG   B CZ   1 
ATOM   3169 N  NH1  . ARG   B 1 58  ? -38.68900 51.19700 69.98100 1.000 9.41209  ? 492  ARG   B NH1  1 
ATOM   3170 N  NH2  . ARG   B 1 58  ? -36.94900 50.03800 70.91500 1.000 10.99321 ? 492  ARG   B NH2  1 
ATOM   3171 N  N    . LEU   B 1 59  ? -43.45100 50.40100 68.17700 1.000 11.72720 ? 493  LEU   B N    1 
ATOM   3172 C  CA   . LEU   B 1 59  ? -42.89300 51.00900 66.98000 1.000 13.93351 ? 493  LEU   B CA   1 
ATOM   3173 C  C    . LEU   B 1 59  ? -41.39700 51.22600 67.15900 1.000 17.77112 ? 493  LEU   B C    1 
ATOM   3174 O  O    . LEU   B 1 59  ? -40.93000 51.58000 68.24500 1.000 18.68816 ? 493  LEU   B O    1 
ATOM   3175 C  CB   . LEU   B 1 59  ? -43.56300 52.35200 66.68500 1.000 13.38951 ? 493  LEU   B CB   1 
ATOM   3176 C  CG   . LEU   B 1 59  ? -45.06800 52.46800 66.44300 1.000 16.38470 ? 493  LEU   B CG   1 
ATOM   3177 C  CD1  . LEU   B 1 59  ? -45.45900 53.93700 66.46100 1.000 13.25685 ? 493  LEU   B CD1  1 
ATOM   3178 C  CD2  . LEU   B 1 59  ? -45.47500 51.83400 65.12400 1.000 8.92992  ? 493  LEU   B CD2  1 
ATOM   3179 N  N    . ALA   B 1 60  ? -40.64500 51.00100 66.09100 1.000 14.69292 ? 494  ALA   B N    1 
ATOM   3180 C  CA   . ALA   B 1 60  ? -39.29700 51.53400 66.02800 1.000 14.46632 ? 494  ALA   B CA   1 
ATOM   3181 C  C    . ALA   B 1 60  ? -39.36600 53.03600 65.78100 1.000 16.85479 ? 494  ALA   B C    1 
ATOM   3182 O  O    . ALA   B 1 60  ? -40.31400 53.53800 65.17300 1.000 14.55781 ? 494  ALA   B O    1 
ATOM   3183 C  CB   . ALA   B 1 60  ? -38.50600 50.85100 64.91600 1.000 11.07083 ? 494  ALA   B CB   1 
ATOM   3184 N  N    . THR   B 1 61  ? -38.36500 53.76000 66.27000 1.000 13.16504 ? 495  THR   B N    1 
ATOM   3185 C  CA   . THR   B 1 61  ? -38.30600 55.19000 66.00700 1.000 14.38629 ? 495  THR   B CA   1 
ATOM   3186 C  C    . THR   B 1 61  ? -37.45500 55.46300 64.77300 1.000 15.78785 ? 495  THR   B C    1 
ATOM   3187 O  O    . THR   B 1 61  ? -36.64500 54.63600 64.34800 1.000 13.08827 ? 495  THR   B O    1 
ATOM   3188 C  CB   . THR   B 1 61  ? -37.74400 55.96300 67.20500 1.000 20.60314 ? 495  THR   B CB   1 
ATOM   3189 O  OG1  . THR   B 1 61  ? -36.33700 55.71900 67.32000 1.000 10.99158 ? 495  THR   B OG1  1 
ATOM   3190 C  CG2  . THR   B 1 61  ? -38.45000 55.55300 68.50200 1.000 10.29065 ? 495  THR   B CG2  1 
ATOM   3191 N  N    . GLU   B 1 62  ? -37.65700 56.64900 64.19200 1.000 13.56941 ? 496  GLU   B N    1 
ATOM   3192 C  CA   . GLU   B 1 62  ? -36.88100 57.02700 63.01700 1.000 14.99869 ? 496  GLU   B CA   1 
ATOM   3193 C  C    . GLU   B 1 62  ? -35.39200 57.07600 63.32700 1.000 12.38473 ? 496  GLU   B C    1 
ATOM   3194 O  O    . GLU   B 1 62  ? -34.56600 56.78800 62.45300 1.000 22.37604 ? 496  GLU   B O    1 
ATOM   3195 C  CB   . GLU   B 1 62  ? -37.36100 58.37500 62.48400 1.000 13.02393 ? 496  GLU   B CB   1 
ATOM   3196 C  CG   . GLU   B 1 62  ? -38.82900 58.40200 62.10900 1.000 14.21209 ? 496  GLU   B CG   1 
ATOM   3197 C  CD   . GLU   B 1 62  ? -39.24400 59.71600 61.47700 1.000 16.18363 ? 496  GLU   B CD   1 
ATOM   3198 O  OE1  . GLU   B 1 62  ? -38.36100 60.43900 60.97100 1.000 19.85402 ? 496  GLU   B OE1  1 
ATOM   3199 O  OE2  . GLU   B 1 62  ? -40.45500 60.02400 61.48900 1.000 24.10341 ? 496  GLU   B OE2  1 
ATOM   3200 N  N    . GLU   B 1 63  ? -35.03100 57.43300 64.56100 1.000 10.53982 ? 497  GLU   B N    1 
ATOM   3201 C  CA   . GLU   B 1 63  ? -33.62800 57.40000 64.95900 1.000 14.11191 ? 497  GLU   B CA   1 
ATOM   3202 C  C    . GLU   B 1 63  ? -33.10500 55.97100 64.99200 1.000 13.99832 ? 497  GLU   B C    1 
ATOM   3203 O  O    . GLU   B 1 63  ? -31.94000 55.72000 64.66000 1.000 13.84976 ? 497  GLU   B O    1 
ATOM   3204 C  CB   . GLU   B 1 63  ? -33.44700 58.07100 66.32100 1.000 13.31126 ? 497  GLU   B CB   1 
ATOM   3205 N  N    . GLU   B 1 64  ? -33.95200 55.01900 65.39000 1.000 17.89832 ? 498  GLU   B N    1 
ATOM   3206 C  CA   . GLU   B 1 64  ? -33.53900 53.61900 65.38600 1.000 10.48168 ? 498  GLU   B CA   1 
ATOM   3207 C  C    . GLU   B 1 64  ? -33.42300 53.08200 63.96300 1.000 13.28657 ? 498  GLU   B C    1 
ATOM   3208 O  O    . GLU   B 1 64  ? -32.49200 52.32900 63.65300 1.000 15.44474 ? 498  GLU   B O    1 
ATOM   3209 C  CB   . GLU   B 1 64  ? -34.51700 52.78800 66.21600 1.000 9.76804  ? 498  GLU   B CB   1 
ATOM   3210 C  CG   . GLU   B 1 64  ? -34.45800 53.09800 67.70800 1.000 12.47238 ? 498  GLU   B CG   1 
ATOM   3211 C  CD   . GLU   B 1 64  ? -35.52000 52.37000 68.51300 1.000 12.66386 ? 498  GLU   B CD   1 
ATOM   3212 O  OE1  . GLU   B 1 64  ? -36.64100 52.18000 67.99700 1.000 15.99609 ? 498  GLU   B OE1  1 
ATOM   3213 O  OE2  . GLU   B 1 64  ? -35.23400 51.98700 69.66700 1.000 12.91001 ? 498  GLU   B OE2  1 
ATOM   3214 N  N    . LEU   B 1 65  ? -34.35100 53.46300 63.08100 1.000 14.74917 ? 499  LEU   B N    1 
ATOM   3215 C  CA   . LEU   B 1 65  ? -34.22900 53.09100 61.67400 1.000 10.34460 ? 499  LEU   B CA   1 
ATOM   3216 C  C    . LEU   B 1 65  ? -32.91600 53.59200 61.08900 1.000 12.07009 ? 499  LEU   B C    1 
ATOM   3217 O  O    . LEU   B 1 65  ? -32.30400 52.92000 60.25200 1.000 14.30471 ? 499  LEU   B O    1 
ATOM   3218 C  CB   . LEU   B 1 65  ? -35.40500 53.64800 60.86900 1.000 17.09821 ? 499  LEU   B CB   1 
ATOM   3219 C  CG   . LEU   B 1 65  ? -36.83800 53.16600 61.10600 1.000 14.48245 ? 499  LEU   B CG   1 
ATOM   3220 C  CD1  . LEU   B 1 65  ? -37.79000 53.94200 60.20700 1.000 8.75767  ? 499  LEU   B CD1  1 
ATOM   3221 C  CD2  . LEU   B 1 65  ? -36.97000 51.67300 60.85300 1.000 15.61184 ? 499  LEU   B CD2  1 
ATOM   3222 N  N    . ALA   B 1 66  ? -32.46700 54.77400 61.52000 1.000 15.28110 ? 500  ALA   B N    1 
ATOM   3223 C  CA   . ALA   B 1 66  ? -31.23300 55.36900 61.02000 1.000 10.21833 ? 500  ALA   B CA   1 
ATOM   3224 C  C    . ALA   B 1 66  ? -29.98400 54.60500 61.43900 1.000 12.18880 ? 500  ALA   B C    1 
ATOM   3225 O  O    . ALA   B 1 66  ? -28.88700 54.97300 61.00400 1.000 10.53832 ? 500  ALA   B O    1 
ATOM   3226 C  CB   . ALA   B 1 66  ? -31.12600 56.82300 61.48200 1.000 10.65032 ? 500  ALA   B CB   1 
ATOM   3227 N  N    . LEU   B 1 67  ? -30.10900 53.56900 62.27300 1.000 9.91712  ? 501  LEU   B N    1 
ATOM   3228 C  CA   . LEU   B 1 67  ? -28.95400 52.72700 62.56300 1.000 10.00768 ? 501  LEU   B CA   1 
ATOM   3229 C  C    . LEU   B 1 67  ? -28.47900 52.00100 61.31500 1.000 15.03156 ? 501  LEU   B C    1 
ATOM   3230 O  O    . LEU   B 1 67  ? -27.28000 51.74800 61.16300 1.000 18.55134 ? 501  LEU   B O    1 
ATOM   3231 C  CB   . LEU   B 1 67  ? -29.29000 51.71900 63.66200 1.000 14.84750 ? 501  LEU   B CB   1 
ATOM   3232 C  CG   . LEU   B 1 67  ? -29.62600 52.26900 65.04800 1.000 10.01919 ? 501  LEU   B CG   1 
ATOM   3233 C  CD1  . LEU   B 1 67  ? -30.02200 51.13000 65.98100 1.000 9.79775  ? 501  LEU   B CD1  1 
ATOM   3234 C  CD2  . LEU   B 1 67  ? -28.45100 53.05300 65.61800 1.000 10.61502 ? 501  LEU   B CD2  1 
ATOM   3235 N  N    . CYS   B 1 68  ? -29.39900 51.66500 60.41100 1.000 11.48628 ? 502  CYS   B N    1 
ATOM   3236 C  CA   . CYS   B 1 68  ? -29.05600 50.97400 59.17600 1.000 13.08760 ? 502  CYS   B CA   1 
ATOM   3237 C  C    . CYS   B 1 68  ? -29.53500 51.67100 57.91300 1.000 11.37147 ? 502  CYS   B C    1 
ATOM   3238 O  O    . CYS   B 1 68  ? -28.97900 51.40000 56.84300 1.000 19.94633 ? 502  CYS   B O    1 
ATOM   3239 C  CB   . CYS   B 1 68  ? -29.62500 49.54600 59.18000 1.000 14.30425 ? 502  CYS   B CB   1 
ATOM   3240 S  SG   . CYS   B 1 68  ? -29.10300 48.52800 60.56800 1.000 16.96279 ? 502  CYS   B SG   1 
ATOM   3241 N  N    . HIS   B 1 69  ? -30.52800 52.55200 57.98800 1.000 13.60557 ? 503  HIS   B N    1 
ATOM   3242 C  CA   . HIS   B 1 69  ? -31.14100 53.11900 56.79900 1.000 11.07884 ? 503  HIS   B CA   1 
ATOM   3243 C  C    . HIS   B 1 69  ? -30.86400 54.61200 56.68400 1.000 9.84589  ? 503  HIS   B C    1 
ATOM   3244 O  O    . HIS   B 1 69  ? -30.70200 55.31600 57.68400 1.000 10.09527 ? 503  HIS   B O    1 
ATOM   3245 C  CB   . HIS   B 1 69  ? -32.64900 52.86000 56.79500 1.000 13.52955 ? 503  HIS   B CB   1 
ATOM   3246 C  CG   . HIS   B 1 69  ? -33.00300 51.40700 56.72600 1.000 14.47008 ? 503  HIS   B CG   1 
ATOM   3247 N  ND1  . HIS   B 1 69  ? -32.93300 50.68100 55.55700 1.000 10.68582 ? 503  HIS   B ND1  1 
ATOM   3248 C  CD2  . HIS   B 1 69  ? -33.42500 50.54400 57.68100 1.000 10.63959 ? 503  HIS   B CD2  1 
ATOM   3249 C  CE1  . HIS   B 1 69  ? -33.29900 49.43400 55.79300 1.000 9.32830  ? 503  HIS   B CE1  1 
ATOM   3250 N  NE2  . HIS   B 1 69  ? -33.60000 49.32400 57.07400 1.000 13.58687 ? 503  HIS   B NE2  1 
ATOM   3251 N  N    . SER   B 1 70  ? -30.81700 55.08100 55.44200 1.000 11.52052 ? 504  SER   B N    1 
ATOM   3252 C  CA   . SER   B 1 70  ? -30.54400 56.47200 55.13300 1.000 14.45134 ? 504  SER   B CA   1 
ATOM   3253 C  C    . SER   B 1 70  ? -31.78500 57.33200 55.36000 1.000 21.75530 ? 504  SER   B C    1 
ATOM   3254 O  O    . SER   B 1 70  ? -32.92300 56.85200 55.35400 1.000 15.97297 ? 504  SER   B O    1 
ATOM   3255 C  CB   . SER   B 1 70  ? -30.07200 56.61200 53.68600 1.000 14.59874 ? 504  SER   B CB   1 
ATOM   3256 O  OG   . SER   B 1 70  ? -31.11100 56.28600 52.78000 1.000 14.06775 ? 504  SER   B OG   1 
ATOM   3257 N  N    . SER   B 1 71  ? -31.55000 58.63100 55.55000 1.000 13.14981 ? 505  SER   B N    1 
ATOM   3258 C  CA   . SER   B 1 71  ? -32.65900 59.54800 55.78900 1.000 17.01673 ? 505  SER   B CA   1 
ATOM   3259 C  C    . SER   B 1 71  ? -33.62300 59.56900 54.60900 1.000 15.63928 ? 505  SER   B C    1 
ATOM   3260 O  O    . SER   B 1 71  ? -34.84200 59.64500 54.79900 1.000 21.36933 ? 505  SER   B O    1 
ATOM   3261 C  CB   . SER   B 1 71  ? -32.12600 60.95100 56.08000 1.000 15.30162 ? 505  SER   B CB   1 
ATOM   3262 O  OG   . SER   B 1 71  ? -31.33800 61.43600 55.00700 1.000 21.79455 ? 505  SER   B OG   1 
ATOM   3263 N  N    . LYS   B 1 72  ? -33.09700 59.48600 53.38300 1.000 13.11026 ? 506  LYS   B N    1 
ATOM   3264 C  CA   . LYS   B 1 72  ? -33.95500 59.52200 52.20200 1.000 11.36243 ? 506  LYS   B CA   1 
ATOM   3265 C  C    . LYS   B 1 72  ? -34.92300 58.34700 52.18600 1.000 14.26786 ? 506  LYS   B C    1 
ATOM   3266 O  O    . LYS   B 1 72  ? -36.11900 58.51400 51.92200 1.000 15.15048 ? 506  LYS   B O    1 
ATOM   3267 C  CB   . LYS   B 1 72  ? -33.10500 59.52100 50.93100 1.000 16.26914 ? 506  LYS   B CB   1 
ATOM   3268 N  N    . HIS   B 1 73  ? -34.41600 57.14300 52.45100 1.000 15.86529 ? 507  HIS   B N    1 
ATOM   3269 C  CA   . HIS   B 1 73  ? -35.25900 55.95500 52.39100 1.000 12.73425 ? 507  HIS   B CA   1 
ATOM   3270 C  C    . HIS   B 1 73  ? -36.30200 55.95200 53.50300 1.000 18.11100 ? 507  HIS   B C    1 
ATOM   3271 O  O    . HIS   B 1 73  ? -37.45500 55.56000 53.28000 1.000 15.38190 ? 507  HIS   B O    1 
ATOM   3272 C  CB   . HIS   B 1 73  ? -34.38900 54.70500 52.47000 1.000 18.16246 ? 507  HIS   B CB   1 
ATOM   3273 C  CG   . HIS   B 1 73  ? -35.16800 53.44100 52.62600 1.000 12.79861 ? 507  HIS   B CG   1 
ATOM   3274 N  ND1  . HIS   B 1 73  ? -36.03800 52.98100 51.66100 1.000 10.68834 ? 507  HIS   B ND1  1 
ATOM   3275 C  CD2  . HIS   B 1 73  ? -35.20800 52.53800 53.63200 1.000 12.07399 ? 507  HIS   B CD2  1 
ATOM   3276 C  CE1  . HIS   B 1 73  ? -36.58200 51.84800 52.06800 1.000 12.91491 ? 507  HIS   B CE1  1 
ATOM   3277 N  NE2  . HIS   B 1 73  ? -36.09600 51.55800 53.26100 1.000 13.29857 ? 507  HIS   B NE2  1 
ATOM   3278 N  N    . ILE   B 1 74  ? -35.91500 56.37700 54.70700 1.000 18.01400 ? 508  ILE   B N    1 
ATOM   3279 C  CA   . ILE   B 1 74  ? -36.87700 56.49100 55.80000 1.000 17.61250 ? 508  ILE   B CA   1 
ATOM   3280 C  C    . ILE   B 1 74  ? -37.96900 57.48900 55.44000 1.000 16.24281 ? 508  ILE   B C    1 
ATOM   3281 O  O    . ILE   B 1 74  ? -39.16300 57.22400 55.61600 1.000 13.54876 ? 508  ILE   B O    1 
ATOM   3282 C  CB   . ILE   B 1 74  ? -36.16200 56.89100 57.10300 1.000 13.40768 ? 508  ILE   B CB   1 
ATOM   3283 C  CG1  . ILE   B 1 74  ? -35.28300 55.74700 57.60900 1.000 11.80210 ? 508  ILE   B CG1  1 
ATOM   3284 C  CG2  . ILE   B 1 74  ? -37.17700 57.32200 58.16200 1.000 12.91705 ? 508  ILE   B CG2  1 
ATOM   3285 C  CD1  . ILE   B 1 74  ? -34.22000 56.19900 58.58800 1.000 13.80885 ? 508  ILE   B CD1  1 
ATOM   3286 N  N    . SER   B 1 75  ? -37.57100 58.65100 54.91900 1.000 17.05817 ? 509  SER   B N    1 
ATOM   3287 C  CA   A SER   B 1 75  ? -38.54300 59.70000 54.62700 0.492 15.45975 ? 509  SER   B CA   1 
ATOM   3288 C  CA   B SER   B 1 75  ? -38.53900 59.70300 54.62200 0.508 15.46001 ? 509  SER   B CA   1 
ATOM   3289 C  C    . SER   B 1 75  ? -39.49800 59.27900 53.51700 1.000 16.62988 ? 509  SER   B C    1 
ATOM   3290 O  O    . SER   B 1 75  ? -40.69400 59.59200 53.57000 1.000 13.55171 ? 509  SER   B O    1 
ATOM   3291 C  CB   A SER   B 1 75  ? -37.81900 60.99600 54.25900 0.492 16.47731 ? 509  SER   B CB   1 
ATOM   3292 C  CB   B SER   B 1 75  ? -37.80800 60.98800 54.23700 0.508 16.47766 ? 509  SER   B CB   1 
ATOM   3293 O  OG   A SER   B 1 75  ? -36.93600 60.80300 53.17000 0.492 16.12014 ? 509  SER   B OG   1 
ATOM   3294 O  OG   B SER   B 1 75  ? -38.71300 62.06700 54.08400 0.508 17.05180 ? 509  SER   B OG   1 
ATOM   3295 N  N    . ILE   B 1 76  ? -38.99400 58.56600 52.50800 1.000 15.91004 ? 510  ILE   B N    1 
ATOM   3296 C  CA   . ILE   B 1 76  ? -39.85000 58.13300 51.40800 1.000 16.37699 ? 510  ILE   B CA   1 
ATOM   3297 C  C    . ILE   B 1 76  ? -40.88700 57.13200 51.90100 1.000 15.53362 ? 510  ILE   B C    1 
ATOM   3298 O  O    . ILE   B 1 76  ? -42.08900 57.29500 51.66700 1.000 12.77614 ? 510  ILE   B O    1 
ATOM   3299 C  CB   . ILE   B 1 76  ? -39.00000 57.55700 50.26200 1.000 12.71160 ? 510  ILE   B CB   1 
ATOM   3300 C  CG1  . ILE   B 1 76  ? -38.39000 58.69400 49.43800 1.000 12.85271 ? 510  ILE   B CG1  1 
ATOM   3301 C  CG2  . ILE   B 1 76  ? -39.83300 56.63900 49.38500 1.000 11.18847 ? 510  ILE   B CG2  1 
ATOM   3302 C  CD1  . ILE   B 1 76  ? -37.27100 58.25300 48.52100 1.000 23.01900 ? 510  ILE   B CD1  1 
ATOM   3303 N  N    . ILE   B 1 77  ? -40.44100 56.08400 52.59800 1.000 16.05431 ? 511  ILE   B N    1 
ATOM   3304 C  CA   . ILE   B 1 77  ? -41.38300 55.07200 53.06400 1.000 12.78068 ? 511  ILE   B CA   1 
ATOM   3305 C  C    . ILE   B 1 77  ? -42.33100 55.65800 54.10300 1.000 18.04695 ? 511  ILE   B C    1 
ATOM   3306 O  O    . ILE   B 1 77  ? -43.50300 55.26700 54.17700 1.000 14.56549 ? 511  ILE   B O    1 
ATOM   3307 C  CB   . ILE   B 1 77  ? -40.62300 53.84600 53.60000 1.000 11.30550 ? 511  ILE   B CB   1 
ATOM   3308 C  CG1  . ILE   B 1 77  ? -39.73600 53.25100 52.50300 1.000 16.28590 ? 511  ILE   B CG1  1 
ATOM   3309 C  CG2  . ILE   B 1 77  ? -41.58900 52.79400 54.12000 1.000 15.73982 ? 511  ILE   B CG2  1 
ATOM   3310 C  CD1  . ILE   B 1 77  ? -40.49500 52.79100 51.27800 1.000 12.79478 ? 511  ILE   B CD1  1 
ATOM   3311 N  N    . LYS   B 1 78  ? -41.85800 56.60900 54.91100 1.000 17.58257 ? 512  LYS   B N    1 
ATOM   3312 C  CA   . LYS   B 1 78  ? -42.75500 57.28600 55.84100 1.000 15.04709 ? 512  LYS   B CA   1 
ATOM   3313 C  C    . LYS   B 1 78  ? -43.84200 58.04400 55.09300 1.000 17.52089 ? 512  LYS   B C    1 
ATOM   3314 O  O    . LYS   B 1 78  ? -45.01700 58.00000 55.47700 1.000 15.49506 ? 512  LYS   B O    1 
ATOM   3315 C  CB   . LYS   B 1 78  ? -41.96100 58.22800 56.74500 1.000 10.17484 ? 512  LYS   B CB   1 
ATOM   3316 C  CG   . LYS   B 1 78  ? -42.81300 59.19000 57.56100 1.000 20.53837 ? 512  LYS   B CG   1 
ATOM   3317 C  CD   . LYS   B 1 78  ? -41.98000 59.88300 58.62800 1.000 21.52119 ? 512  LYS   B CD   1 
ATOM   3318 C  CE   . LYS   B 1 78  ? -42.38300 61.33700 58.79700 1.000 26.16770 ? 512  LYS   B CE   1 
ATOM   3319 N  NZ   . LYS   B 1 78  ? -41.53500 62.03000 59.80600 1.000 21.70436 ? 512  LYS   B NZ   1 
ATOM   3320 N  N    . SER   B 1 79  ? -43.47200 58.72300 54.00200 1.000 10.77680 ? 513  SER   B N    1 
ATOM   3321 C  CA   . SER   B 1 79  ? -44.43800 59.51200 53.24900 1.000 11.08957 ? 513  SER   B CA   1 
ATOM   3322 C  C    . SER   B 1 79  ? -45.55100 58.64900 52.67000 1.000 17.78044 ? 513  SER   B C    1 
ATOM   3323 O  O    . SER   B 1 79  ? -46.65900 59.14700 52.44000 1.000 19.23554 ? 513  SER   B O    1 
ATOM   3324 C  CB   . SER   B 1 79  ? -43.73700 60.27500 52.12600 1.000 15.66828 ? 513  SER   B CB   1 
ATOM   3325 O  OG   . SER   B 1 79  ? -43.58600 59.46100 50.97300 1.000 14.92851 ? 513  SER   B OG   1 
ATOM   3326 N  N    . SER   B 1 80  ? -45.28200 57.36100 52.43200 1.000 11.46264 ? 514  SER   B N    1 
ATOM   3327 C  CA   . SER   B 1 80  ? -46.27600 56.49500 51.80400 1.000 14.30940 ? 514  SER   B CA   1 
ATOM   3328 C  C    . SER   B 1 80  ? -47.54200 56.35700 52.64100 1.000 15.19109 ? 514  SER   B C    1 
ATOM   3329 O  O    . SER   B 1 80  ? -48.61000 56.07800 52.08700 1.000 22.03282 ? 514  SER   B O    1 
ATOM   3330 C  CB   . SER   B 1 80  ? -45.67600 55.11300 51.54300 1.000 12.16005 ? 514  SER   B CB   1 
ATOM   3331 O  OG   . SER   B 1 80  ? -45.59500 54.36300 52.73900 1.000 16.25259 ? 514  SER   B OG   1 
ATOM   3332 N  N    . GLU   B 1 81  ? -47.44900 56.55500 53.95800 1.000 11.04439 ? 515  GLU   B N    1 
ATOM   3333 C  CA   . GLU   B 1 81  ? -48.61100 56.42000 54.83000 1.000 20.03751 ? 515  GLU   B CA   1 
ATOM   3334 C  C    . GLU   B 1 81  ? -49.75400 57.35300 54.44300 1.000 18.37811 ? 515  GLU   B C    1 
ATOM   3335 O  O    . GLU   B 1 81  ? -50.91500 57.05200 54.74200 1.000 17.37158 ? 515  GLU   B O    1 
ATOM   3336 C  CB   . GLU   B 1 81  ? -48.18400 56.67300 56.27900 1.000 24.33716 ? 515  GLU   B CB   1 
ATOM   3337 C  CG   . GLU   B 1 81  ? -49.32600 56.81800 57.27300 1.000 18.47426 ? 515  GLU   B CG   1 
ATOM   3338 C  CD   . GLU   B 1 81  ? -48.84500 56.87900 58.71000 1.000 23.60508 ? 515  GLU   B CD   1 
ATOM   3339 O  OE1  . GLU   B 1 81  ? -47.61600 56.94600 58.92400 1.000 18.94009 ? 515  GLU   B OE1  1 
ATOM   3340 O  OE2  . GLU   B 1 81  ? -49.69700 56.85200 59.62300 1.000 32.88306 ? 515  GLU   B OE2  1 
ATOM   3341 N  N    . HIS   B 1 82  ? -49.46400 58.46900 53.77500 1.000 20.23288 ? 516  HIS   B N    1 
ATOM   3342 C  CA   . HIS   B 1 82  ? -50.48200 59.46200 53.45100 1.000 23.88327 ? 516  HIS   B CA   1 
ATOM   3343 C  C    . HIS   B 1 82  ? -50.77600 59.54400 51.95600 1.000 23.49892 ? 516  HIS   B C    1 
ATOM   3344 O  O    . HIS   B 1 82  ? -51.40500 60.50700 51.50800 1.000 22.23302 ? 516  HIS   B O    1 
ATOM   3345 C  CB   . HIS   B 1 82  ? -50.06400 60.83500 53.97900 1.000 20.34109 ? 516  HIS   B CB   1 
ATOM   3346 C  CG   . HIS   B 1 82  ? -49.81100 60.86100 55.45400 1.000 29.96524 ? 516  HIS   B CG   1 
ATOM   3347 N  ND1  . HIS   B 1 82  ? -50.82700 60.79600 56.38300 1.000 34.92989 ? 516  HIS   B ND1  1 
ATOM   3348 C  CD2  . HIS   B 1 82  ? -48.65900 60.94400 56.16000 1.000 42.33106 ? 516  HIS   B CD2  1 
ATOM   3349 C  CE1  . HIS   B 1 82  ? -50.31100 60.83600 57.59900 1.000 35.10719 ? 516  HIS   B CE1  1 
ATOM   3350 N  NE2  . HIS   B 1 82  ? -48.99800 60.92800 57.49200 1.000 48.13163 ? 516  HIS   B NE2  1 
ATOM   3351 N  N    . MET   B 1 83  ? -50.35000 58.55500 51.17700 1.000 16.61550 ? 517  MET   B N    1 
ATOM   3352 C  CA   . MET   B 1 83  ? -50.49100 58.61400 49.73000 1.000 28.12283 ? 517  MET   B CA   1 
ATOM   3353 C  C    . MET   B 1 83  ? -51.83700 58.06900 49.26600 1.000 22.95150 ? 517  MET   B C    1 
ATOM   3354 O  O    . MET   B 1 83  ? -52.44300 57.20800 49.91000 1.000 20.47281 ? 517  MET   B O    1 
ATOM   3355 C  CB   . MET   B 1 83  ? -49.37000 57.83500 49.04700 1.000 21.60114 ? 517  MET   B CB   1 
ATOM   3356 C  CG   . MET   B 1 83  ? -48.07600 58.60100 48.91300 1.000 16.58339 ? 517  MET   B CG   1 
ATOM   3357 S  SD   . MET   B 1 83  ? -46.76800 57.56100 48.24700 1.000 25.70127 ? 517  MET   B SD   1 
ATOM   3358 C  CE   . MET   B 1 83  ? -45.40900 58.72500 48.25500 1.000 16.27837 ? 517  MET   B CE   1 
ATOM   3359 N  N    . LYS   B 1 84  ? -52.29800 58.59000 48.13200 1.000 20.02116 ? 518  LYS   B N    1 
ATOM   3360 C  CA   . LYS   B 1 84  ? -53.43900 58.00400 47.45300 1.000 19.30239 ? 518  LYS   B CA   1 
ATOM   3361 C  C    . LYS   B 1 84  ? -53.09000 56.58400 47.00700 1.000 24.79964 ? 518  LYS   B C    1 
ATOM   3362 O  O    . LYS   B 1 84  ? -51.93500 56.29800 46.67500 1.000 17.20531 ? 518  LYS   B O    1 
ATOM   3363 C  CB   . LYS   B 1 84  ? -53.84100 58.85300 46.24900 1.000 26.48135 ? 518  LYS   B CB   1 
ATOM   3364 C  CG   . LYS   B 1 84  ? -54.66800 60.08400 46.59100 1.000 21.28776 ? 518  LYS   B CG   1 
ATOM   3365 C  CD   . LYS   B 1 84  ? -56.07200 59.69100 47.01500 1.000 20.90383 ? 518  LYS   B CD   1 
ATOM   3366 C  CE   . LYS   B 1 84  ? -57.00800 60.89200 47.02500 1.000 22.16031 ? 518  LYS   B CE   1 
ATOM   3367 N  NZ   . LYS   B 1 84  ? -58.41000 60.49100 47.33300 1.000 26.72301 ? 518  LYS   B NZ   1 
ATOM   3368 N  N    . PRO   B 1 85  ? -54.06900 55.67200 47.00300 1.000 27.91304 ? 519  PRO   B N    1 
ATOM   3369 C  CA   . PRO   B 1 85  ? -53.77000 54.27300 46.64600 1.000 16.90008 ? 519  PRO   B CA   1 
ATOM   3370 C  C    . PRO   B 1 85  ? -53.04900 54.11600 45.31500 1.000 25.38481 ? 519  PRO   B C    1 
ATOM   3371 O  O    . PRO   B 1 85  ? -52.17400 53.25000 45.19000 1.000 23.63158 ? 519  PRO   B O    1 
ATOM   3372 C  CB   . PRO   B 1 85  ? -55.16100 53.62400 46.62500 1.000 17.22512 ? 519  PRO   B CB   1 
ATOM   3373 C  CG   . PRO   B 1 85  ? -55.96900 54.44900 47.56600 1.000 17.73217 ? 519  PRO   B CG   1 
ATOM   3374 C  CD   . PRO   B 1 85  ? -55.47800 55.85400 47.39400 1.000 19.11233 ? 519  PRO   B CD   1 
ATOM   3375 N  N    . ARG   B 1 86  ? -53.37400 54.94300 44.32200 1.000 22.95928 ? 520  ARG   B N    1 
ATOM   3376 C  CA   . ARG   B 1 86  ? -52.71900 54.83200 43.02600 1.000 18.03633 ? 520  ARG   B CA   1 
ATOM   3377 C  C    . ARG   B 1 86  ? -51.30100 55.38500 43.04600 1.000 17.80715 ? 520  ARG   B C    1 
ATOM   3378 O  O    . ARG   B 1 86  ? -50.42700 54.86100 42.34700 1.000 18.96774 ? 520  ARG   B O    1 
ATOM   3379 C  CB   . ARG   B 1 86  ? -53.56000 55.54000 41.96800 1.000 19.18445 ? 520  ARG   B CB   1 
ATOM   3380 C  CG   . ARG   B 1 86  ? -54.81700 54.76600 41.64000 1.000 28.08645 ? 520  ARG   B CG   1 
ATOM   3381 C  CD   . ARG   B 1 86  ? -54.45100 53.43900 41.00600 1.000 22.82528 ? 520  ARG   B CD   1 
ATOM   3382 N  NE   . ARG   B 1 86  ? -55.42500 52.40000 41.30800 1.000 29.57701 ? 520  ARG   B NE   1 
ATOM   3383 C  CZ   . ARG   B 1 86  ? -55.33900 51.15100 40.87400 1.000 30.11686 ? 520  ARG   B CZ   1 
ATOM   3384 N  NH1  . ARG   B 1 86  ? -54.34500 50.75900 40.09500 1.000 36.90733 ? 520  ARG   B NH1  1 
ATOM   3385 N  NH2  . ARG   B 1 86  ? -56.28500 50.27900 41.21000 1.000 32.35233 ? 520  ARG   B NH2  1 
ATOM   3386 N  N    . ASP   B 1 87  ? -51.05300 56.43600 43.83100 1.000 25.40610 ? 521  ASP   B N    1 
ATOM   3387 C  CA   . ASP   B 1 87  ? -49.68100 56.89400 44.02200 1.000 27.92363 ? 521  ASP   B CA   1 
ATOM   3388 C  C    . ASP   B 1 87  ? -48.85200 55.83300 44.72900 1.000 16.63503 ? 521  ASP   B C    1 
ATOM   3389 O  O    . ASP   B 1 87  ? -47.66200 55.66800 44.43700 1.000 17.73704 ? 521  ASP   B O    1 
ATOM   3390 C  CB   . ASP   B 1 87  ? -49.66500 58.20400 44.80700 1.000 21.06688 ? 521  ASP   B CB   1 
ATOM   3391 C  CG   . ASP   B 1 87  ? -50.07400 59.39100 43.96400 1.000 28.22899 ? 521  ASP   B CG   1 
ATOM   3392 O  OD1  . ASP   B 1 87  ? -49.60300 59.48400 42.81000 1.000 32.83695 ? 521  ASP   B OD1  1 
ATOM   3393 O  OD2  . ASP   B 1 87  ? -50.87000 60.22400 44.45100 1.000 32.49724 ? 521  ASP   B OD2  1 
ATOM   3394 N  N    . LEU   B 1 88  ? -49.46100 55.11200 45.67200 1.000 16.91274 ? 522  LEU   B N    1 
ATOM   3395 C  CA   . LEU   B 1 88  ? -48.78300 53.98300 46.29900 1.000 15.08524 ? 522  LEU   B CA   1 
ATOM   3396 C  C    . LEU   B 1 88  ? -48.44300 52.90300 45.28300 1.000 17.86246 ? 522  LEU   B C    1 
ATOM   3397 O  O    . LEU   B 1 88  ? -47.41000 52.23600 45.40800 1.000 21.71618 ? 522  LEU   B O    1 
ATOM   3398 C  CB   . LEU   B 1 88  ? -49.65600 53.40300 47.41100 1.000 19.98818 ? 522  LEU   B CB   1 
ATOM   3399 C  CG   . LEU   B 1 88  ? -49.70500 54.19000 48.71900 1.000 22.03947 ? 522  LEU   B CG   1 
ATOM   3400 C  CD1  . LEU   B 1 88  ? -50.67000 53.53800 49.69100 1.000 14.46391 ? 522  LEU   B CD1  1 
ATOM   3401 C  CD2  . LEU   B 1 88  ? -48.31400 54.27700 49.31900 1.000 19.13630 ? 522  LEU   B CD2  1 
ATOM   3402 N  N    . ASN   B 1 89  ? -49.29900 52.70900 44.27800 1.000 22.86389 ? 523  ASN   B N    1 
ATOM   3403 C  CA   . ASN   B 1 89  ? -49.00200 51.72400 43.24700 1.000 23.54296 ? 523  ASN   B CA   1 
ATOM   3404 C  C    . ASN   B 1 89  ? -47.76800 52.12200 42.45000 1.000 21.36991 ? 523  ASN   B C    1 
ATOM   3405 O  O    . ASN   B 1 89  ? -46.90800 51.28300 42.16400 1.000 21.53602 ? 523  ASN   B O    1 
ATOM   3406 C  CB   . ASN   B 1 89  ? -50.20300 51.55100 42.32000 1.000 22.50526 ? 523  ASN   B CB   1 
ATOM   3407 C  CG   . ASN   B 1 89  ? -50.10100 50.30400 41.46500 1.000 29.67370 ? 523  ASN   B CG   1 
ATOM   3408 O  OD1  . ASN   B 1 89  ? -49.76100 50.36900 40.28700 1.000 25.30431 ? 523  ASN   B OD1  1 
ATOM   3409 N  ND2  . ASN   B 1 89  ? -50.39300 49.15500 42.06200 1.000 35.97747 ? 523  ASN   B ND2  1 
ATOM   3410 N  N    . ARG   B 1 90  ? -47.66500 53.40200 42.08300 1.000 24.90643 ? 524  ARG   B N    1 
ATOM   3411 C  CA   . ARG   B 1 90  ? -46.51600 53.86400 41.31300 1.000 20.55208 ? 524  ARG   B CA   1 
ATOM   3412 C  C    . ARG   B 1 90  ? -45.23700 53.80800 42.13700 1.000 20.50680 ? 524  ARG   B C    1 
ATOM   3413 O  O    . ARG   B 1 90  ? -44.18100 53.41500 41.62700 1.000 16.89930 ? 524  ARG   B O    1 
ATOM   3414 C  CB   . ARG   B 1 90  ? -46.76700 55.28100 40.80400 1.000 17.46987 ? 524  ARG   B CB   1 
ATOM   3415 N  N    . LEU   B 1 91  ? -45.31100 54.20300 43.41000 1.000 16.53645 ? 525  LEU   B N    1 
ATOM   3416 C  CA   . LEU   B 1 91  ? -44.14700 54.10900 44.28500 1.000 14.89907 ? 525  LEU   B CA   1 
ATOM   3417 C  C    . LEU   B 1 91  ? -43.68000 52.66400 44.41500 1.000 20.65059 ? 525  LEU   B C    1 
ATOM   3418 O  O    . LEU   B 1 91  ? -42.48800 52.36800 44.27500 1.000 16.82360 ? 525  LEU   B O    1 
ATOM   3419 C  CB   . LEU   B 1 91  ? -44.47700 54.69900 45.65500 1.000 14.73379 ? 525  LEU   B CB   1 
ATOM   3420 C  CG   . LEU   B 1 91  ? -43.42200 54.53700 46.75700 1.000 23.78583 ? 525  LEU   B CG   1 
ATOM   3421 C  CD1  . LEU   B 1 91  ? -42.07000 55.07200 46.31000 1.000 14.49401 ? 525  LEU   B CD1  1 
ATOM   3422 C  CD2  . LEU   B 1 91  ? -43.87900 55.22900 48.03300 1.000 14.09858 ? 525  LEU   B CD2  1 
ATOM   3423 N  N    . GLY   B 1 92  ? -44.61400 51.74700 44.67200 1.000 17.77211 ? 526  GLY   B N    1 
ATOM   3424 C  CA   . GLY   B 1 92  ? -44.24400 50.34900 44.81500 1.000 12.98088 ? 526  GLY   B CA   1 
ATOM   3425 C  C    . GLY   B 1 92  ? -43.58300 49.78300 43.57200 1.000 22.31432 ? 526  GLY   B C    1 
ATOM   3426 O  O    . GLY   B 1 92  ? -42.64100 48.99300 43.66700 1.000 23.53123 ? 526  GLY   B O    1 
ATOM   3427 N  N    . ASP   B 1 93  ? -44.06100 50.18200 42.39000 1.000 16.88978 ? 527  ASP   B N    1 
ATOM   3428 C  CA   . ASP   B 1 93  ? -43.46100 49.70800 41.14600 1.000 19.78489 ? 527  ASP   B CA   1 
ATOM   3429 C  C    . ASP   B 1 93  ? -42.01900 50.16400 40.98400 1.000 26.17116 ? 527  ASP   B C    1 
ATOM   3430 O  O    . ASP   B 1 93  ? -41.25700 49.52200 40.25100 1.000 28.29458 ? 527  ASP   B O    1 
ATOM   3431 C  CB   . ASP   B 1 93  ? -44.27800 50.18100 39.94600 1.000 24.30896 ? 527  ASP   B CB   1 
ATOM   3432 C  CG   . ASP   B 1 93  ? -45.55200 49.39000 39.76200 1.000 31.18330 ? 527  ASP   B CG   1 
ATOM   3433 O  OD1  . ASP   B 1 93  ? -45.71000 48.34400 40.43400 1.000 25.38328 ? 527  ASP   B OD1  1 
ATOM   3434 O  OD2  . ASP   B 1 93  ? -46.39500 49.82100 38.94600 1.000 33.47460 ? 527  ASP   B OD2  1 
ATOM   3435 N  N    . GLU   B 1 94  ? -41.62700 51.25500 41.64500 1.000 22.27902 ? 528  GLU   B N    1 
ATOM   3436 C  CA   . GLU   B 1 94  ? -40.25400 51.73300 41.55700 1.000 20.77598 ? 528  GLU   B CA   1 
ATOM   3437 C  C    . GLU   B 1 94  ? -39.26800 50.83200 42.28100 1.000 18.66888 ? 528  GLU   B C    1 
ATOM   3438 O  O    . GLU   B 1 94  ? -38.05800 51.00600 42.10500 1.000 27.74508 ? 528  GLU   B O    1 
ATOM   3439 C  CB   . GLU   B 1 94  ? -40.15500 53.15900 42.10100 1.000 15.01089 ? 528  GLU   B CB   1 
ATOM   3440 C  CG   . GLU   B 1 94  ? -40.43100 54.21800 41.05300 1.000 16.05340 ? 528  GLU   B CG   1 
ATOM   3441 C  CD   . GLU   B 1 94  ? -40.67000 55.58900 41.64700 1.000 27.95349 ? 528  GLU   B CD   1 
ATOM   3442 O  OE1  . GLU   B 1 94  ? -40.06400 55.90200 42.69400 1.000 26.35013 ? 528  GLU   B OE1  1 
ATOM   3443 O  OE2  . GLU   B 1 94  ? -41.47300 56.35200 41.06700 1.000 28.86077 ? 528  GLU   B OE2  1 
ATOM   3444 N  N    . TYR   B 1 95  ? -39.74000 49.88200 43.08000 1.000 17.40375 ? 529  TYR   B N    1 
ATOM   3445 C  CA   . TYR   B 1 95  ? -38.86600 48.93000 43.74500 1.000 12.55439 ? 529  TYR   B CA   1 
ATOM   3446 C  C    . TYR   B 1 95  ? -39.02300 47.55600 43.11200 1.000 13.93052 ? 529  TYR   B C    1 
ATOM   3447 O  O    . TYR   B 1 95  ? -39.93900 47.30500 42.32600 1.000 14.25594 ? 529  TYR   B O    1 
ATOM   3448 C  CB   . TYR   B 1 95  ? -39.15900 48.85200 45.24800 1.000 13.14819 ? 529  TYR   B CB   1 
ATOM   3449 C  CG   . TYR   B 1 95  ? -39.09700 50.17600 45.96300 1.000 14.33184 ? 529  TYR   B CG   1 
ATOM   3450 C  CD1  . TYR   B 1 95  ? -37.88400 50.70900 46.38000 1.000 12.19656 ? 529  TYR   B CD1  1 
ATOM   3451 C  CD2  . TYR   B 1 95  ? -40.25600 50.89100 46.23300 1.000 14.17272 ? 529  TYR   B CD2  1 
ATOM   3452 C  CE1  . TYR   B 1 95  ? -37.83100 51.92400 47.03900 1.000 14.39338 ? 529  TYR   B CE1  1 
ATOM   3453 C  CE2  . TYR   B 1 95  ? -40.21300 52.10200 46.88900 1.000 12.62825 ? 529  TYR   B CE2  1 
ATOM   3454 C  CZ   . TYR   B 1 95  ? -39.00100 52.61400 47.29100 1.000 12.82032 ? 529  TYR   B CZ   1 
ATOM   3455 O  OH   . TYR   B 1 95  ? -38.96400 53.82400 47.94300 1.000 25.53925 ? 529  TYR   B OH   1 
ATOM   3456 N  N    . ASN   B 1 96  ? -38.10500 46.66600 43.47700 1.000 11.76531 ? 530  ASN   B N    1 
ATOM   3457 C  CA   . ASN   B 1 96  ? -38.08200 45.29500 42.98300 1.000 16.50506 ? 530  ASN   B CA   1 
ATOM   3458 C  C    . ASN   B 1 96  ? -38.94700 44.43400 43.90100 1.000 11.38854 ? 530  ASN   B C    1 
ATOM   3459 O  O    . ASN   B 1 96  ? -38.59100 44.20300 45.06100 1.000 11.04998 ? 530  ASN   B O    1 
ATOM   3460 C  CB   . ASN   B 1 96  ? -36.63800 44.79900 42.92600 1.000 19.84179 ? 530  ASN   B CB   1 
ATOM   3461 C  CG   . ASN   B 1 96  ? -36.51500 43.37700 42.42900 1.000 22.68544 ? 530  ASN   B CG   1 
ATOM   3462 O  OD1  . ASN   B 1 96  ? -37.50300 42.73400 42.07000 1.000 25.63492 ? 530  ASN   B OD1  1 
ATOM   3463 N  ND2  . ASN   B 1 96  ? -35.28200 42.87700 42.39000 1.000 27.40537 ? 530  ASN   B ND2  1 
ATOM   3464 N  N    . SER   B 1 97  ? -40.08400 43.97100 43.38000 1.000 11.60643 ? 531  SER   B N    1 
ATOM   3465 C  CA   . SER   B 1 97  ? -41.01900 43.10400 44.10100 1.000 10.74426 ? 531  SER   B CA   1 
ATOM   3466 C  C    . SER   B 1 97  ? -41.45300 43.73700 45.42700 1.000 11.69846 ? 531  SER   B C    1 
ATOM   3467 O  O    . SER   B 1 97  ? -41.10900 43.27100 46.51300 1.000 14.35331 ? 531  SER   B O    1 
ATOM   3468 C  CB   . SER   B 1 97  ? -40.40800 41.71900 44.34200 1.000 10.27946 ? 531  SER   B CB   1 
ATOM   3469 O  OG   . SER   B 1 97  ? -39.84500 41.18300 43.16200 1.000 14.48927 ? 531  SER   B OG   1 
ATOM   3470 N  N    . ILE   B 1 98  ? -42.23100 44.81400 45.31300 1.000 13.98710 ? 532  ILE   B N    1 
ATOM   3471 C  CA   . ILE   B 1 98  ? -42.71400 45.55800 46.47300 1.000 10.63274 ? 532  ILE   B CA   1 
ATOM   3472 C  C    . ILE   B 1 98  ? -44.12900 46.05300 46.20300 1.000 14.23346 ? 532  ILE   B C    1 
ATOM   3473 O  O    . ILE   B 1 98  ? -44.38400 46.68700 45.17400 1.000 19.85168 ? 532  ILE   B O    1 
ATOM   3474 C  CB   . ILE   B 1 98  ? -41.79800 46.75100 46.81800 1.000 10.76321 ? 532  ILE   B CB   1 
ATOM   3475 C  CG1  . ILE   B 1 98  ? -40.52100 46.28200 47.51900 1.000 11.12703 ? 532  ILE   B CG1  1 
ATOM   3476 C  CG2  . ILE   B 1 98  ? -42.54000 47.76700 47.68100 1.000 12.70585 ? 532  ILE   B CG2  1 
ATOM   3477 C  CD1  . ILE   B 1 98  ? -40.72600 45.84200 48.94000 1.000 11.62410 ? 532  ILE   B CD1  1 
ATOM   3478 N  N    . PHE   B 1 99  ? -45.04500 45.77200 47.13100 1.000 12.11948 ? 533  PHE   B N    1 
ATOM   3479 C  CA   . PHE   B 1 99  ? -46.36000 46.39500 47.15700 1.000 12.67386 ? 533  PHE   B CA   1 
ATOM   3480 C  C    . PHE   B 1 99  ? -46.49500 47.21400 48.43600 1.000 14.98840 ? 533  PHE   B C    1 
ATOM   3481 O  O    . PHE   B 1 99  ? -45.92200 46.87100 49.47500 1.000 12.46471 ? 533  PHE   B O    1 
ATOM   3482 C  CB   . PHE   B 1 99  ? -47.49300 45.35100 47.06400 1.000 11.32490 ? 533  PHE   B CB   1 
ATOM   3483 C  CG   . PHE   B 1 99  ? -47.57000 44.41500 48.24200 1.000 10.83234 ? 533  PHE   B CG   1 
ATOM   3484 C  CD1  . PHE   B 1 99  ? -48.23400 44.78400 49.40300 1.000 11.60218 ? 533  PHE   B CD1  1 
ATOM   3485 C  CD2  . PHE   B 1 99  ? -47.00300 43.15500 48.17800 1.000 14.85545 ? 533  PHE   B CD2  1 
ATOM   3486 C  CE1  . PHE   B 1 99  ? -48.31500 43.92100 50.47900 1.000 13.33542 ? 533  PHE   B CE1  1 
ATOM   3487 C  CE2  . PHE   B 1 99  ? -47.08000 42.28900 49.25400 1.000 14.07019 ? 533  PHE   B CE2  1 
ATOM   3488 C  CZ   . PHE   B 1 99  ? -47.73300 42.67500 50.40700 1.000 10.10659 ? 533  PHE   B CZ   1 
ATOM   3489 N  N    . ILE   B 1 100 ? -47.25000 48.30900 48.35800 1.000 16.02272 ? 534  ILE   B N    1 
ATOM   3490 C  CA   . ILE   B 1 100 ? -47.38800 49.24100 49.47200 1.000 15.21928 ? 534  ILE   B CA   1 
ATOM   3491 C  C    . ILE   B 1 100 ? -48.86200 49.55000 49.69600 1.000 14.06250 ? 534  ILE   B C    1 
ATOM   3492 O  O    . ILE   B 1 100 ? -49.63800 49.65700 48.74000 1.000 14.83238 ? 534  ILE   B O    1 
ATOM   3493 C  CB   . ILE   B 1 100 ? -46.60000 50.54600 49.22500 1.000 14.14907 ? 534  ILE   B CB   1 
ATOM   3494 C  CG1  . ILE   B 1 100 ? -45.20400 50.24400 48.68200 1.000 18.86369 ? 534  ILE   B CG1  1 
ATOM   3495 C  CG2  . ILE   B 1 100 ? -46.48100 51.34500 50.50600 1.000 13.48807 ? 534  ILE   B CG2  1 
ATOM   3496 C  CD1  . ILE   B 1 100 ? -44.40300 51.48200 48.35700 1.000 14.54741 ? 534  ILE   B CD1  1 
ATOM   3497 N  N    . SER   B 1 101 ? -49.24400 49.68300 50.96400 1.000 17.47786 ? 535  SER   B N    1 
ATOM   3498 C  CA   . SER   B 1 101 ? -50.54000 50.19600 51.38600 1.000 19.21586 ? 535  SER   B CA   1 
ATOM   3499 C  C    . SER   B 1 101 ? -50.29700 51.34600 52.35700 1.000 16.34061 ? 535  SER   B C    1 
ATOM   3500 O  O    . SER   B 1 101 ? -49.15400 51.66400 52.70000 1.000 16.41983 ? 535  SER   B O    1 
ATOM   3501 C  CB   . SER   B 1 101 ? -51.40100 49.10000 52.02900 1.000 14.85374 ? 535  SER   B CB   1 
ATOM   3502 O  OG   . SER   B 1 101 ? -50.94900 48.79000 53.33800 1.000 15.36741 ? 535  SER   B OG   1 
ATOM   3503 N  N    . ASN   B 1 102 ? -51.38200 51.98100 52.80400 1.000 17.77290 ? 536  ASN   B N    1 
ATOM   3504 C  CA   . ASN   B 1 102 ? -51.24800 53.13100 53.69200 1.000 13.62850 ? 536  ASN   B CA   1 
ATOM   3505 C  C    . ASN   B 1 102 ? -50.75700 52.73900 55.07600 1.000 13.05985 ? 536  ASN   B C    1 
ATOM   3506 O  O    . ASN   B 1 102 ? -50.30500 53.60800 55.82700 1.000 15.72784 ? 536  ASN   B O    1 
ATOM   3507 C  CB   . ASN   B 1 102 ? -52.58000 53.87700 53.80300 1.000 14.46291 ? 536  ASN   B CB   1 
ATOM   3508 C  CG   . ASN   B 1 102 ? -52.85600 54.75900 52.60000 1.000 19.66867 ? 536  ASN   B CG   1 
ATOM   3509 O  OD1  . ASN   B 1 102 ? -53.60900 54.39100 51.69800 1.000 31.20160 ? 536  ASN   B OD1  1 
ATOM   3510 N  ND2  . ASN   B 1 102 ? -52.23600 55.93000 52.57700 1.000 22.83801 ? 536  ASN   B ND2  1 
ATOM   3511 N  N    . GLU   B 1 103 ? -50.82900 51.45700 55.42600 1.000 12.55245 ? 537  GLU   B N    1 
ATOM   3512 C  CA   . GLU   B 1 103 ? -50.39500 50.97200 56.72700 1.000 12.06711 ? 537  GLU   B CA   1 
ATOM   3513 C  C    . GLU   B 1 103 ? -49.02400 50.30900 56.68100 1.000 13.24461 ? 537  GLU   B C    1 
ATOM   3514 O  O    . GLU   B 1 103 ? -48.52700 49.88100 57.72800 1.000 10.97636 ? 537  GLU   B O    1 
ATOM   3515 C  CB   . GLU   B 1 103 ? -51.42200 49.98300 57.29200 1.000 12.34812 ? 537  GLU   B CB   1 
ATOM   3516 C  CG   . GLU   B 1 103 ? -52.86700 50.49100 57.30900 1.000 12.86695 ? 537  GLU   B CG   1 
ATOM   3517 C  CD   . GLU   B 1 103 ? -53.63500 50.16200 56.03200 1.000 13.23091 ? 537  GLU   B CD   1 
ATOM   3518 O  OE1  . GLU   B 1 103 ? -53.03400 49.62500 55.08100 1.000 18.66014 ? 537  GLU   B OE1  1 
ATOM   3519 O  OE2  . GLU   B 1 103 ? -54.85100 50.43500 55.97900 1.000 19.88140 ? 537  GLU   B OE2  1 
ATOM   3520 N  N    . SER   B 1 104 ? -48.40200 50.22900 55.49800 1.000 12.46257 ? 538  SER   B N    1 
ATOM   3521 C  CA   . SER   B 1 104 ? -47.13600 49.51400 55.35000 1.000 11.14541 ? 538  SER   B CA   1 
ATOM   3522 C  C    . SER   B 1 104 ? -46.07300 50.06500 56.28600 1.000 10.48876 ? 538  SER   B C    1 
ATOM   3523 O  O    . SER   B 1 104 ? -45.44200 49.31200 57.03300 1.000 10.02241 ? 538  SER   B O    1 
ATOM   3524 C  CB   . SER   B 1 104 ? -46.64800 49.59400 53.90300 1.000 10.82032 ? 538  SER   B CB   1 
ATOM   3525 O  OG   . SER   B 1 104 ? -47.54400 48.94800 53.02400 1.000 11.18728 ? 538  SER   B OG   1 
ATOM   3526 N  N    . TYR   B 1 105 ? -45.85600 51.38200 56.24700 1.000 10.89109 ? 539  TYR   B N    1 
ATOM   3527 C  CA   . TYR   B 1 105 ? -44.81700 51.99900 57.06700 1.000 10.78462 ? 539  TYR   B CA   1 
ATOM   3528 C  C    . TYR   B 1 105 ? -45.00000 51.65900 58.54300 1.000 10.97262 ? 539  TYR   B C    1 
ATOM   3529 O  O    . TYR   B 1 105 ? -44.03700 51.29300 59.22800 1.000 10.16075 ? 539  TYR   B O    1 
ATOM   3530 C  CB   . TYR   B 1 105 ? -44.82500 53.51000 56.84000 1.000 11.41512 ? 539  TYR   B CB   1 
ATOM   3531 C  CG   . TYR   B 1 105 ? -43.89700 54.29900 57.72900 1.000 13.64543 ? 539  TYR   B CG   1 
ATOM   3532 C  CD1  . TYR   B 1 105 ? -42.52300 54.08800 57.69900 1.000 11.15572 ? 539  TYR   B CD1  1 
ATOM   3533 C  CD2  . TYR   B 1 105 ? -44.39200 55.27700 58.58000 1.000 16.43967 ? 539  TYR   B CD2  1 
ATOM   3534 C  CE1  . TYR   B 1 105 ? -41.67200 54.81700 58.50700 1.000 11.26980 ? 539  TYR   B CE1  1 
ATOM   3535 C  CE2  . TYR   B 1 105 ? -43.55000 56.01000 59.39000 1.000 11.98822 ? 539  TYR   B CE2  1 
ATOM   3536 C  CZ   . TYR   B 1 105 ? -42.19300 55.77700 59.35100 1.000 15.45535 ? 539  TYR   B CZ   1 
ATOM   3537 O  OH   . TYR   B 1 105 ? -41.35700 56.51100 60.15700 1.000 13.06830 ? 539  TYR   B OH   1 
ATOM   3538 N  N    . THR   B 1 106 ? -46.23800 51.73800 59.04000 1.000 14.44468 ? 540  THR   B N    1 
ATOM   3539 C  CA   . THR   B 1 106 ? -46.50400 51.42300 60.44100 1.000 10.69623 ? 540  THR   B CA   1 
ATOM   3540 C  C    . THR   B 1 106 ? -46.15200 49.97700 60.77000 1.000 11.01939 ? 540  THR   B C    1 
ATOM   3541 O  O    . THR   B 1 106 ? -45.53200 49.70400 61.80500 1.000 9.88134  ? 540  THR   B O    1 
ATOM   3542 C  CB   . THR   B 1 106 ? -47.97000 51.70700 60.76900 1.000 11.20306 ? 540  THR   B CB   1 
ATOM   3543 O  OG1  . THR   B 1 106 ? -48.16800 53.12300 60.85800 1.000 25.40842 ? 540  THR   B OG1  1 
ATOM   3544 C  CG2  . THR   B 1 106 ? -48.36400 51.05800 62.09100 1.000 11.09202 ? 540  THR   B CG2  1 
ATOM   3545 N  N    . CYS   B 1 107 ? -46.52900 49.03800 59.89600 1.000 15.02189 ? 541  CYS   B N    1 
ATOM   3546 C  CA   . CYS   B 1 107 ? -46.25600 47.62700 60.16400 1.000 13.89416 ? 541  CYS   B CA   1 
ATOM   3547 C  C    . CYS   B 1 107 ? -44.76700 47.31400 60.09900 1.000 9.14268  ? 541  CYS   B C    1 
ATOM   3548 O  O    . CYS   B 1 107 ? -44.29100 46.42400 60.81400 1.000 10.28758 ? 541  CYS   B O    1 
ATOM   3549 C  CB   . CYS   B 1 107 ? -47.02500 46.74400 59.18200 1.000 12.31403 ? 541  CYS   B CB   1 
ATOM   3550 S  SG   . CYS   B 1 107 ? -48.83100 46.93200 59.27100 1.000 17.27948 ? 541  CYS   B SG   1 
ATOM   3551 N  N    . ALA   B 1 108 ? -44.02100 48.01400 59.24600 1.000 9.18898  ? 542  ALA   B N    1 
ATOM   3552 C  CA   . ALA   B 1 108 ? -42.57100 47.85300 59.24700 1.000 10.02733 ? 542  ALA   B CA   1 
ATOM   3553 C  C    . ALA   B 1 108 ? -41.97700 48.35300 60.55500 1.000 11.43300 ? 542  ALA   B C    1 
ATOM   3554 O  O    . ALA   B 1 108 ? -41.06800 47.72700 61.11200 1.000 14.49573 ? 542  ALA   B O    1 
ATOM   3555 C  CB   . ALA   B 1 108 ? -41.95800 48.59000 58.05800 1.000 9.09017  ? 542  ALA   B CB   1 
ATOM   3556 N  N    . LEU   B 1 109 ? -42.49300 49.47600 61.06300 1.000 11.05012 ? 543  LEU   B N    1 
ATOM   3557 C  CA   . LEU   B 1 109 ? -42.05200 49.99200 62.35400 1.000 9.27421  ? 543  LEU   B CA   1 
ATOM   3558 C  C    . LEU   B 1 109 ? -42.33300 49.00100 63.47100 1.000 9.20529  ? 543  LEU   B C    1 
ATOM   3559 O  O    . LEU   B 1 109 ? -41.49300 48.79500 64.35500 1.000 16.61036 ? 543  LEU   B O    1 
ATOM   3560 C  CB   . LEU   B 1 109 ? -42.74300 51.32100 62.64900 1.000 9.78352  ? 543  LEU   B CB   1 
ATOM   3561 C  CG   . LEU   B 1 109 ? -42.40600 52.47500 61.71400 1.000 10.15208 ? 543  LEU   B CG   1 
ATOM   3562 C  CD1  . LEU   B 1 109 ? -43.06900 53.75300 62.20200 1.000 10.72266 ? 543  LEU   B CD1  1 
ATOM   3563 C  CD2  . LEU   B 1 109 ? -40.90000 52.63500 61.62500 1.000 12.29877 ? 543  LEU   B CD2  1 
ATOM   3564 N  N    . LEU   B 1 110 ? -43.51400 48.38300 63.45500 1.000 9.10858  ? 544  LEU   B N    1 
ATOM   3565 C  CA   . LEU   B 1 110 ? -43.84400 47.40900 64.48700 1.000 10.33121 ? 544  LEU   B CA   1 
ATOM   3566 C  C    . LEU   B 1 110 ? -42.98600 46.15800 64.36200 1.000 9.99494  ? 544  LEU   B C    1 
ATOM   3567 O  O    . LEU   B 1 110 ? -42.60000 45.56500 65.37300 1.000 15.66859 ? 544  LEU   B O    1 
ATOM   3568 C  CB   . LEU   B 1 110 ? -45.32500 47.05400 64.41900 1.000 9.27472  ? 544  LEU   B CB   1 
ATOM   3569 C  CG   . LEU   B 1 110 ? -46.26100 48.14700 64.91900 1.000 16.37325 ? 544  LEU   B CG   1 
ATOM   3570 C  CD1  . LEU   B 1 110 ? -47.70900 47.72800 64.74000 1.000 15.35793 ? 544  LEU   B CD1  1 
ATOM   3571 C  CD2  . LEU   B 1 110 ? -45.95600 48.44500 66.38300 1.000 16.80287 ? 544  LEU   B CD2  1 
ATOM   3572 N  N    . ALA   B 1 111 ? -42.67800 45.73900 63.13400 1.000 8.42543  ? 545  ALA   B N    1 
ATOM   3573 C  CA   . ALA   B 1 111 ? -41.83200 44.56400 62.95800 1.000 12.17054 ? 545  ALA   B CA   1 
ATOM   3574 C  C    . ALA   B 1 111 ? -40.47100 44.76600 63.61100 1.000 7.98465  ? 545  ALA   B C    1 
ATOM   3575 O  O    . ALA   B 1 111 ? -39.97800 43.88200 64.32300 1.000 8.68480  ? 545  ALA   B O    1 
ATOM   3576 C  CB   . ALA   B 1 111 ? -41.67700 44.24600 61.47100 1.000 14.19722 ? 545  ALA   B CB   1 
ATOM   3577 N  N    . ALA   B 1 112 ? -39.86000 45.93100 63.40100 1.000 8.09265  ? 546  ALA   B N    1 
ATOM   3578 C  CA   . ALA   B 1 112 ? -38.55700 46.19700 63.99700 1.000 8.06131  ? 546  ALA   B CA   1 
ATOM   3579 C  C    . ALA   B 1 112 ? -38.67200 46.38700 65.50500 1.000 12.67165 ? 546  ALA   B C    1 
ATOM   3580 O  O    . ALA   B 1 112 ? -37.88700 45.81600 66.27100 1.000 11.65377 ? 546  ALA   B O    1 
ATOM   3581 C  CB   . ALA   B 1 112 ? -37.92300 47.42400 63.34200 1.000 13.02032 ? 546  ALA   B CB   1 
ATOM   3582 N  N    . GLY   B 1 113 ? -39.65300 47.18000 65.94900 1.000 10.91202 ? 547  GLY   B N    1 
ATOM   3583 C  CA   . GLY   B 1 113 ? -39.79800 47.44100 67.37400 1.000 8.59524  ? 547  GLY   B CA   1 
ATOM   3584 C  C    . GLY   B 1 113 ? -40.09900 46.18700 68.17100 1.000 11.48331 ? 547  GLY   B C    1 
ATOM   3585 O  O    . GLY   B 1 113 ? -39.63900 46.03700 69.30600 1.000 11.08584 ? 547  GLY   B O    1 
ATOM   3586 N  N    . SER   B 1 114 ? -40.88100 45.27300 67.58900 1.000 11.81947 ? 548  SER   B N    1 
ATOM   3587 C  CA   . SER   B 1 114 ? -41.08000 43.96000 68.19400 1.000 15.00975 ? 548  SER   B CA   1 
ATOM   3588 C  C    . SER   B 1 114 ? -39.74500 43.29000 68.47800 1.000 10.09423 ? 548  SER   B C    1 
ATOM   3589 O  O    . SER   B 1 114 ? -39.51000 42.78000 69.58100 1.000 16.42169 ? 548  SER   B O    1 
ATOM   3590 C  CB   . SER   B 1 114 ? -41.92600 43.07500 67.27400 1.000 8.33023  ? 548  SER   B CB   1 
ATOM   3591 O  OG   . SER   B 1 114 ? -43.21800 43.61900 67.07800 1.000 15.12229 ? 548  SER   B OG   1 
ATOM   3592 N  N    . CYS   B 1 115 ? -38.84800 43.29900 67.49000 1.000 10.80596 ? 549  CYS   B N    1 
ATOM   3593 C  CA   . CYS   B 1 115 ? -37.57200 42.60700 67.62500 1.000 8.29884  ? 549  CYS   B CA   1 
ATOM   3594 C  C    . CYS   B 1 115 ? -36.58600 43.37700 68.49200 1.000 8.26393  ? 549  CYS   B C    1 
ATOM   3595 O  O    . CYS   B 1 115 ? -35.74100 42.75900 69.14500 1.000 16.57954 ? 549  CYS   B O    1 
ATOM   3596 C  CB   . CYS   B 1 115 ? -36.97700 42.33900 66.24400 1.000 10.77107 ? 549  CYS   B CB   1 
ATOM   3597 S  SG   . CYS   B 1 115 ? -38.00700 41.25100 65.23200 1.000 9.94172  ? 549  CYS   B SG   1 
ATOM   3598 N  N    . PHE   B 1 116 ? -36.66600 44.70900 68.51100 1.000 8.13701  ? 550  PHE   B N    1 
ATOM   3599 C  CA   . PHE   B 1 116 ? -35.90400 45.48400 69.48600 1.000 8.35012  ? 550  PHE   B CA   1 
ATOM   3600 C  C    . PHE   B 1 116 ? -36.28900 45.08100 70.90500 1.000 10.65203 ? 550  PHE   B C    1 
ATOM   3601 O  O    . PHE   B 1 116 ? -35.43400 44.71500 71.72100 1.000 13.18991 ? 550  PHE   B O    1 
ATOM   3602 C  CB   . PHE   B 1 116 ? -36.14700 46.98500 69.29300 1.000 11.03312 ? 550  PHE   B CB   1 
ATOM   3603 C  CG   . PHE   B 1 116 ? -35.75100 47.51800 67.94200 1.000 8.49828  ? 550  PHE   B CG   1 
ATOM   3604 C  CD1  . PHE   B 1 116 ? -35.03100 46.74900 67.03900 1.000 8.90634  ? 550  PHE   B CD1  1 
ATOM   3605 C  CD2  . PHE   B 1 116 ? -36.08600 48.81500 67.59100 1.000 14.63105 ? 550  PHE   B CD2  1 
ATOM   3606 C  CE1  . PHE   B 1 116 ? -34.66700 47.25800 65.80700 1.000 9.86860  ? 550  PHE   B CE1  1 
ATOM   3607 C  CE2  . PHE   B 1 116 ? -35.72900 49.33100 66.36000 1.000 10.05786 ? 550  PHE   B CE2  1 
ATOM   3608 C  CZ   . PHE   B 1 116 ? -35.01700 48.55200 65.46600 1.000 14.98139 ? 550  PHE   B CZ   1 
ATOM   3609 N  N    . ASN   B 1 117 ? -37.58900 45.15600 71.21400 1.000 11.31010 ? 551  ASN   B N    1 
ATOM   3610 C  CA   . ASN   B 1 117 ? -38.07800 44.78200 72.53800 1.000 9.37582  ? 551  ASN   B CA   1 
ATOM   3611 C  C    . ASN   B 1 117 ? -37.68300 43.35600 72.89700 1.000 9.29660  ? 551  ASN   B C    1 
ATOM   3612 O  O    . ASN   B 1 117 ? -37.37000 43.06300 74.05700 1.000 15.95737 ? 551  ASN   B O    1 
ATOM   3613 C  CB   . ASN   B 1 117 ? -39.59800 44.93500 72.59700 1.000 9.11417  ? 551  ASN   B CB   1 
ATOM   3614 C  CG   . ASN   B 1 117 ? -40.03200 46.33700 72.98000 1.000 10.78166 ? 551  ASN   B CG   1 
ATOM   3615 O  OD1  . ASN   B 1 117 ? -39.20700 47.23600 73.12600 1.000 11.77170 ? 551  ASN   B OD1  1 
ATOM   3616 N  ND2  . ASN   B 1 117 ? -41.33600 46.52800 73.14600 1.000 9.56833  ? 551  ASN   B ND2  1 
ATOM   3617 N  N    . SER   B 1 118 ? -37.69300 42.45200 71.91500 1.000 8.60122  ? 552  SER   B N    1 
ATOM   3618 C  CA   . SER   B 1 118 ? -37.36800 41.05700 72.19500 1.000 13.10698 ? 552  SER   B CA   1 
ATOM   3619 C  C    . SER   B 1 118 ? -35.87400 40.87000 72.43200 1.000 14.51575 ? 552  SER   B C    1 
ATOM   3620 O  O    . SER   B 1 118 ? -35.47100 40.09900 73.30900 1.000 14.32100 ? 552  SER   B O    1 
ATOM   3621 C  CB   . SER   B 1 118 ? -37.84800 40.16800 71.04700 1.000 13.83564 ? 552  SER   B CB   1 
ATOM   3622 O  OG   . SER   B 1 118 ? -39.25600 40.26600 70.88200 1.000 18.53907 ? 552  SER   B OG   1 
ATOM   3623 N  N    . ALA   B 1 119 ? -35.03600 41.55700 71.65700 1.000 11.62894 ? 553  ALA   B N    1 
ATOM   3624 C  CA   . ALA   B 1 119 ? -33.59900 41.47700 71.89000 1.000 9.74952  ? 553  ALA   B CA   1 
ATOM   3625 C  C    . ALA   B 1 119 ? -33.22700 42.11400 73.22200 1.000 12.79524 ? 553  ALA   B C    1 
ATOM   3626 O  O    . ALA   B 1 119 ? -32.32700 41.63400 73.92000 1.000 9.12166  ? 553  ALA   B O    1 
ATOM   3627 C  CB   . ALA   B 1 119 ? -32.84600 42.14300 70.73900 1.000 8.43012  ? 553  ALA   B CB   1 
ATOM   3628 N  N    . GLN   B 1 120 ? -33.91000 43.20100 73.58700 1.000 14.28283 ? 554  GLN   B N    1 
ATOM   3629 C  CA   . GLN   B 1 120 ? -33.70400 43.80200 74.89900 1.000 17.69134 ? 554  GLN   B CA   1 
ATOM   3630 C  C    . GLN   B 1 120 ? -34.07800 42.82900 76.00800 1.000 16.19289 ? 554  GLN   B C    1 
ATOM   3631 O  O    . GLN   B 1 120 ? -33.35000 42.69700 76.99800 1.000 18.28708 ? 554  GLN   B O    1 
ATOM   3632 C  CB   . GLN   B 1 120 ? -34.51700 45.09300 75.01400 1.000 14.24361 ? 554  GLN   B CB   1 
ATOM   3633 C  CG   . GLN   B 1 120 ? -34.29100 45.86900 76.30300 1.000 14.81162 ? 554  GLN   B CG   1 
ATOM   3634 C  CD   . GLN   B 1 120 ? -35.01200 47.20800 76.31600 1.000 15.67487 ? 554  GLN   B CD   1 
ATOM   3635 O  OE1  . GLN   B 1 120 ? -36.14600 47.32800 75.84300 1.000 15.93911 ? 554  GLN   B OE1  1 
ATOM   3636 N  NE2  . GLN   B 1 120 ? -34.34800 48.22700 76.84600 1.000 24.92680 ? 554  GLN   B NE2  1 
ATOM   3637 N  N    . ALA   B 1 121 ? -35.20600 42.13000 75.85600 1.000 18.99626 ? 555  ALA   B N    1 
ATOM   3638 C  CA   . ALA   B 1 121 ? -35.61100 41.15100 76.86000 1.000 17.10891 ? 555  ALA   B CA   1 
ATOM   3639 C  C    . ALA   B 1 121 ? -34.54600 40.07900 77.04200 1.000 13.68225 ? 555  ALA   B C    1 
ATOM   3640 O  O    . ALA   B 1 121 ? -34.24500 39.67300 78.17100 1.000 18.88674 ? 555  ALA   B O    1 
ATOM   3641 C  CB   . ALA   B 1 121 ? -36.94900 40.52000 76.47100 1.000 10.94882 ? 555  ALA   B CB   1 
ATOM   3642 N  N    . ILE   B 1 122 ? -33.95200 39.62100 75.94100 1.000 14.14995 ? 556  ILE   B N    1 
ATOM   3643 C  CA   . ILE   B 1 122 ? -32.91400 38.59900 76.02400 1.000 9.81824  ? 556  ILE   B CA   1 
ATOM   3644 C  C    . ILE   B 1 122 ? -31.67300 39.15600 76.71200 1.000 13.53909 ? 556  ILE   B C    1 
ATOM   3645 O  O    . ILE   B 1 122 ? -31.16000 38.57000 77.67100 1.000 12.63032 ? 556  ILE   B O    1 
ATOM   3646 C  CB   . ILE   B 1 122 ? -32.58800 38.06000 74.62000 1.000 10.75134 ? 556  ILE   B CB   1 
ATOM   3647 C  CG1  . ILE   B 1 122 ? -33.82600 37.41200 73.99300 1.000 9.33640  ? 556  ILE   B CG1  1 
ATOM   3648 C  CG2  . ILE   B 1 122 ? -31.43200 37.08000 74.68100 1.000 9.74270  ? 556  ILE   B CG2  1 
ATOM   3649 C  CD1  . ILE   B 1 122 ? -33.64300 37.00300 72.54900 1.000 9.02761  ? 556  ILE   B CD1  1 
ATOM   3650 N  N    . LEU   B 1 123 ? -31.18200 40.30500 76.24100 1.000 16.34546 ? 557  LEU   B N    1 
ATOM   3651 C  CA   . LEU   B 1 123 ? -29.90900 40.83700 76.71800 1.000 16.53471 ? 557  LEU   B CA   1 
ATOM   3652 C  C    . LEU   B 1 123 ? -29.97700 41.35500 78.15000 1.000 13.31453 ? 557  LEU   B C    1 
ATOM   3653 O  O    . LEU   B 1 123 ? -28.93100 41.48200 78.79500 1.000 13.68296 ? 557  LEU   B O    1 
ATOM   3654 C  CB   . LEU   B 1 123 ? -29.42700 41.95600 75.79300 1.000 9.96349  ? 557  LEU   B CB   1 
ATOM   3655 C  CG   . LEU   B 1 123 ? -29.16200 41.57400 74.33900 1.000 9.65033  ? 557  LEU   B CG   1 
ATOM   3656 C  CD1  . LEU   B 1 123 ? -28.88900 42.82000 73.52800 1.000 9.53851  ? 557  LEU   B CD1  1 
ATOM   3657 C  CD2  . LEU   B 1 123 ? -27.99600 40.59800 74.24100 1.000 9.87710  ? 557  LEU   B CD2  1 
ATOM   3658 N  N    . THR   B 1 124 ? -31.16700 41.66600 78.66200 1.000 11.26424 ? 558  THR   B N    1 
ATOM   3659 C  CA   . THR   B 1 124 ? -31.30300 42.14000 80.03300 1.000 12.34376 ? 558  THR   B CA   1 
ATOM   3660 C  C    . THR   B 1 124 ? -31.67300 41.02900 81.00600 1.000 14.49755 ? 558  THR   B C    1 
ATOM   3661 O  O    . THR   B 1 124 ? -31.81500 41.29800 82.20300 1.000 20.41472 ? 558  THR   B O    1 
ATOM   3662 C  CB   . THR   B 1 124 ? -32.33900 43.26800 80.11600 1.000 14.52661 ? 558  THR   B CB   1 
ATOM   3663 O  OG1  . THR   B 1 124 ? -33.62400 42.78600 79.70000 1.000 11.92571 ? 558  THR   B OG1  1 
ATOM   3664 C  CG2  . THR   B 1 124 ? -31.92500 44.44000 79.23900 1.000 12.68168 ? 558  THR   B CG2  1 
ATOM   3665 N  N    . GLY   B 1 125 ? -31.83600 39.79600 80.52800 1.000 11.29634 ? 559  GLY   B N    1 
ATOM   3666 C  CA   . GLY   B 1 125 ? -32.04500 38.65500 81.39600 1.000 11.75737 ? 559  GLY   B CA   1 
ATOM   3667 C  C    . GLY   B 1 125 ? -33.48700 38.28600 81.67000 1.000 16.95025 ? 559  GLY   B C    1 
ATOM   3668 O  O    . GLY   B 1 125 ? -33.73100 37.32800 82.41700 1.000 16.74054 ? 559  GLY   B O    1 
ATOM   3669 N  N    . GLN   B 1 126 ? -34.45000 39.00600 81.08900 1.000 18.48296 ? 560  GLN   B N    1 
ATOM   3670 C  CA   . GLN   B 1 126 ? -35.85700 38.71300 81.34800 1.000 12.15298 ? 560  GLN   B CA   1 
ATOM   3671 C  C    . GLN   B 1 126 ? -36.26800 37.38000 80.73800 1.000 11.87229 ? 560  GLN   B C    1 
ATOM   3672 O  O    . GLN   B 1 126 ? -37.05500 36.63400 81.33100 1.000 15.02932 ? 560  GLN   B O    1 
ATOM   3673 C  CB   . GLN   B 1 126 ? -36.73100 39.83900 80.80100 1.000 14.50491 ? 560  GLN   B CB   1 
ATOM   3674 C  CG   . GLN   B 1 126 ? -36.25800 41.22900 81.19000 1.000 24.09571 ? 560  GLN   B CG   1 
ATOM   3675 C  CD   . GLN   B 1 126 ? -36.99000 42.32200 80.43600 1.000 34.59306 ? 560  GLN   B CD   1 
ATOM   3676 O  OE1  . GLN   B 1 126 ? -38.08100 42.10200 79.90300 1.000 39.02733 ? 560  GLN   B OE1  1 
ATOM   3677 N  NE2  . GLN   B 1 126 ? -36.38700 43.50700 80.37600 1.000 25.55833 ? 560  GLN   B NE2  1 
ATOM   3678 N  N    . VAL   B 1 127 ? -35.76300 37.07400 79.54200 1.000 12.14159 ? 561  VAL   B N    1 
ATOM   3679 C  CA   . VAL   B 1 127 ? -36.00500 35.80100 78.87900 1.000 11.21944 ? 561  VAL   B CA   1 
ATOM   3680 C  C    . VAL   B 1 127 ? -34.67300 35.25400 78.38500 1.000 14.43129 ? 561  VAL   B C    1 
ATOM   3681 O  O    . VAL   B 1 127 ? -33.70800 35.99100 78.17300 1.000 13.93646 ? 561  VAL   B O    1 
ATOM   3682 C  CB   . VAL   B 1 127 ? -36.99700 35.92200 77.70100 1.000 10.81063 ? 561  VAL   B CB   1 
ATOM   3683 C  CG1  . VAL   B 1 127 ? -38.33100 36.48400 78.17100 1.000 10.99384 ? 561  VAL   B CG1  1 
ATOM   3684 C  CG2  . VAL   B 1 127 ? -36.40400 36.78600 76.59900 1.000 10.23035 ? 561  VAL   B CG2  1 
ATOM   3685 N  N    . ARG   B 1 128 ? -34.63400 33.93300 78.20600 1.000 14.71993 ? 562  ARG   B N    1 
ATOM   3686 C  CA   . ARG   B 1 128 ? -33.45000 33.27900 77.66500 1.000 13.82547 ? 562  ARG   B CA   1 
ATOM   3687 C  C    . ARG   B 1 128 ? -33.36300 33.46800 76.15500 1.000 16.17412 ? 562  ARG   B C    1 
ATOM   3688 O  O    . ARG   B 1 128 ? -32.33100 33.90300 75.63300 1.000 16.75588 ? 562  ARG   B O    1 
ATOM   3689 C  CB   . ARG   B 1 128 ? -33.46600 31.79000 78.02200 1.000 14.54609 ? 562  ARG   B CB   1 
ATOM   3690 N  N    . ASN   B 1 129 ? -34.44200 33.15100 75.44300 1.000 12.93505 ? 563  ASN   B N    1 
ATOM   3691 C  CA   . ASN   B 1 129 ? -34.51600 33.26600 73.99400 1.000 22.79707 ? 563  ASN   B CA   1 
ATOM   3692 C  C    . ASN   B 1 129 ? -35.92100 33.73000 73.63000 1.000 17.75936 ? 563  ASN   B C    1 
ATOM   3693 O  O    . ASN   B 1 129 ? -36.79200 33.83600 74.49400 1.000 13.06519 ? 563  ASN   B O    1 
ATOM   3694 C  CB   . ASN   B 1 129 ? -34.16000 31.93500 73.31700 1.000 15.65936 ? 563  ASN   B CB   1 
ATOM   3695 C  CG   . ASN   B 1 129 ? -34.87200 30.74900 73.94000 1.000 14.04997 ? 563  ASN   B CG   1 
ATOM   3696 O  OD1  . ASN   B 1 129 ? -36.03900 30.83600 74.31800 1.000 15.26943 ? 563  ASN   B OD1  1 
ATOM   3697 N  ND2  . ASN   B 1 129 ? -34.16600 29.63100 74.05300 1.000 11.23253 ? 563  ASN   B ND2  1 
ATOM   3698 N  N    . ALA   B 1 130 ? -36.15100 34.00700 72.34500 1.000 16.49059 ? 564  ALA   B N    1 
ATOM   3699 C  CA   . ALA   B 1 130 ? -37.43700 34.57200 71.94800 1.000 12.31822 ? 564  ALA   B CA   1 
ATOM   3700 C  C    . ALA   B 1 130 ? -37.73100 34.28400 70.47900 1.000 20.32375 ? 564  ALA   B C    1 
ATOM   3701 O  O    . ALA   B 1 130 ? -36.84200 33.92300 69.70100 1.000 9.36778  ? 564  ALA   B O    1 
ATOM   3702 C  CB   . ALA   B 1 130 ? -37.48100 36.08100 72.21300 1.000 9.11583  ? 564  ALA   B CB   1 
ATOM   3703 N  N    . VAL   B 1 131 ? -39.00200 34.46600 70.11200 1.000 11.71411 ? 565  VAL   B N    1 
ATOM   3704 C  CA   . VAL   B 1 131 ? -39.48500 34.25400 68.75000 1.000 12.72693 ? 565  VAL   B CA   1 
ATOM   3705 C  C    . VAL   B 1 131 ? -40.41000 35.40700 68.37100 1.000 13.13024 ? 565  VAL   B C    1 
ATOM   3706 O  O    . VAL   B 1 131 ? -41.31000 35.77100 69.13600 1.000 8.90288  ? 565  VAL   B O    1 
ATOM   3707 C  CB   . VAL   B 1 131 ? -40.20100 32.89400 68.59800 1.000 10.52235 ? 565  VAL   B CB   1 
ATOM   3708 C  CG1  . VAL   B 1 131 ? -41.30400 32.73000 69.63400 1.000 14.28114 ? 565  VAL   B CG1  1 
ATOM   3709 C  CG2  . VAL   B 1 131 ? -40.76300 32.74500 67.20700 1.000 11.95360 ? 565  VAL   B CG2  1 
ATOM   3710 N  N    . ALA   B 1 132 ? -40.18800 35.98200 67.18900 1.000 11.87342 ? 566  ALA   B N    1 
ATOM   3711 C  CA   . ALA   B 1 132 ? -40.91400 37.15800 66.71900 1.000 8.22351  ? 566  ALA   B CA   1 
ATOM   3712 C  C    . ALA   B 1 132 ? -41.70400 36.78700 65.47000 1.000 9.86046  ? 566  ALA   B C    1 
ATOM   3713 O  O    . ALA   B 1 132 ? -41.11800 36.48500 64.42500 1.000 9.36934  ? 566  ALA   B O    1 
ATOM   3714 C  CB   . ALA   B 1 132 ? -39.95600 38.31400 66.43300 1.000 7.95741  ? 566  ALA   B CB   1 
ATOM   3715 N  N    . ILE   B 1 133 ? -43.02600 36.81900 65.57700 1.000 9.45810  ? 567  ILE   B N    1 
ATOM   3716 C  CA   . ILE   B 1 133 ? -43.91600 36.52500 64.45600 1.000 9.57663  ? 567  ILE   B CA   1 
ATOM   3717 C  C    . ILE   B 1 133 ? -44.30600 37.87700 63.86900 1.000 11.03699 ? 567  ILE   B C    1 
ATOM   3718 O  O    . ILE   B 1 133 ? -45.28300 38.50300 64.27800 1.000 11.50145 ? 567  ILE   B O    1 
ATOM   3719 C  CB   . ILE   B 1 133 ? -45.12600 35.70300 64.89000 1.000 14.70969 ? 567  ILE   B CB   1 
ATOM   3720 C  CG1  . ILE   B 1 133 ? -44.65800 34.46500 65.65800 1.000 13.22754 ? 567  ILE   B CG1  1 
ATOM   3721 C  CG2  . ILE   B 1 133 ? -45.95800 35.30000 63.67700 1.000 12.57277 ? 567  ILE   B CG2  1 
ATOM   3722 C  CD1  . ILE   B 1 133 ? -45.72900 33.83000 66.50500 1.000 11.50560 ? 567  ILE   B CD1  1 
ATOM   3723 N  N    . VAL   B 1 134 ? -43.52700 38.33400 62.89400 1.000 8.67153  ? 568  VAL   B N    1 
ATOM   3724 C  CA   . VAL   B 1 134 ? -43.63700 39.68800 62.37400 1.000 8.11541  ? 568  VAL   B CA   1 
ATOM   3725 C  C    . VAL   B 1 134 ? -43.74500 39.65700 60.85700 1.000 12.95812 ? 568  VAL   B C    1 
ATOM   3726 O  O    . VAL   B 1 134 ? -43.25200 38.73900 60.19300 1.000 12.34804 ? 568  VAL   B O    1 
ATOM   3727 C  CB   . VAL   B 1 134 ? -42.43400 40.55400 62.80900 1.000 9.00556  ? 568  VAL   B CB   1 
ATOM   3728 C  CG1  . VAL   B 1 134 ? -42.47900 40.81600 64.30700 1.000 10.22407 ? 568  VAL   B CG1  1 
ATOM   3729 C  CG2  . VAL   B 1 134 ? -41.12300 39.87300 62.42400 1.000 7.68508  ? 568  VAL   B CG2  1 
ATOM   3730 N  N    . ARG   B 1 135 ? -44.40000 40.67900 60.31500 1.000 10.51954 ? 569  ARG   B N    1 
ATOM   3731 C  CA   . ARG   B 1 135 ? -44.43600 40.96500 58.88800 1.000 13.13558 ? 569  ARG   B CA   1 
ATOM   3732 C  C    . ARG   B 1 135 ? -44.59000 42.46900 58.73200 1.000 9.16823  ? 569  ARG   B C    1 
ATOM   3733 O  O    . ARG   B 1 135 ? -45.07300 43.14100 59.65200 1.000 10.72015 ? 569  ARG   B O    1 
ATOM   3734 C  CB   . ARG   B 1 135 ? -45.58900 40.23200 58.19000 1.000 10.34475 ? 569  ARG   B CB   1 
ATOM   3735 C  CG   . ARG   B 1 135 ? -46.96500 40.70700 58.62900 1.000 10.73949 ? 569  ARG   B CG   1 
ATOM   3736 C  CD   . ARG   B 1 135 ? -48.06300 39.94900 57.90700 1.000 12.55882 ? 569  ARG   B CD   1 
ATOM   3737 N  NE   . ARG   B 1 135 ? -48.07200 40.26000 56.48400 1.000 12.20727 ? 569  ARG   B NE   1 
ATOM   3738 C  CZ   . ARG   B 1 135 ? -48.80000 41.22100 55.93600 1.000 9.79345  ? 569  ARG   B CZ   1 
ATOM   3739 N  NH1  . ARG   B 1 135 ? -49.60300 41.97900 56.66400 1.000 9.88896  ? 569  ARG   B NH1  1 
ATOM   3740 N  NH2  . ARG   B 1 135 ? -48.71700 41.42800 54.62600 1.000 9.68211  ? 569  ARG   B NH2  1 
ATOM   3741 N  N    . PRO   B 1 136 ? -44.15800 43.04000 57.59900 1.000 10.93663 ? 570  PRO   B N    1 
ATOM   3742 C  CA   . PRO   B 1 136 ? -43.45600 42.44200 56.44600 1.000 11.76665 ? 570  PRO   B CA   1 
ATOM   3743 C  C    . PRO   B 1 136 ? -42.03100 41.99800 56.77900 1.000 9.27677  ? 570  PRO   B C    1 
ATOM   3744 O  O    . PRO   B 1 136 ? -41.48300 42.41800 57.79200 1.000 10.62712 ? 570  PRO   B O    1 
ATOM   3745 C  CB   . PRO   B 1 136 ? -43.46100 43.58500 55.42000 1.000 8.52288  ? 570  PRO   B CB   1 
ATOM   3746 C  CG   . PRO   B 1 136 ? -43.46700 44.82700 56.26000 1.000 8.81215  ? 570  PRO   B CG   1 
ATOM   3747 C  CD   . PRO   B 1 136 ? -44.36900 44.48700 57.41000 1.000 8.65789  ? 570  PRO   B CD   1 
ATOM   3748 N  N    . PRO   B 1 137 ? -41.37900 41.12100 55.96500 1.000 7.89019  ? 571  PRO   B N    1 
ATOM   3749 C  CA   . PRO   B 1 137 ? -39.99100 40.75700 56.20800 1.000 7.70591  ? 571  PRO   B CA   1 
ATOM   3750 C  C    . PRO   B 1 137 ? -38.98600 41.88500 56.03900 1.000 10.89396 ? 571  PRO   B C    1 
ATOM   3751 O  O    . PRO   B 1 137 ? -39.40300 42.99700 55.74600 1.000 8.46590  ? 571  PRO   B O    1 
ATOM   3752 C  CB   . PRO   B 1 137 ? -39.77700 39.64800 55.16900 1.000 11.93770 ? 571  PRO   B CB   1 
ATOM   3753 C  CG   . PRO   B 1 137 ? -40.65400 40.04300 54.02400 1.000 12.58633 ? 571  PRO   B CG   1 
ATOM   3754 C  CD   . PRO   B 1 137 ? -41.89600 40.44100 54.76600 1.000 8.02242  ? 571  PRO   B CD   1 
ATOM   3755 N  N    . GLY   B 1 138 ? -37.67700 41.58800 56.20800 1.000 11.23735 ? 572  GLY   B N    1 
ATOM   3756 C  CA   . GLY   B 1 138 ? -36.66100 42.63600 56.12800 1.000 7.80058  ? 572  GLY   B CA   1 
ATOM   3757 C  C    . GLY   B 1 138 ? -35.35300 42.33200 55.40900 1.000 8.84767  ? 572  GLY   B C    1 
ATOM   3758 O  O    . GLY   B 1 138 ? -34.77500 43.29500 54.90600 1.000 9.19723  ? 572  GLY   B O    1 
ATOM   3759 N  N    . HIS   B 1 139 ? -34.87900 41.08600 55.37200 1.000 11.41178 ? 573  HIS   B N    1 
ATOM   3760 C  CA   . HIS   B 1 139 ? -33.51100 40.72500 54.86800 1.000 11.64672 ? 573  HIS   B CA   1 
ATOM   3761 C  C    . HIS   B 1 139 ? -33.13400 41.29800 53.48400 1.000 14.16417 ? 573  HIS   B C    1 
ATOM   3762 O  O    . HIS   B 1 139 ? -31.95600 41.51600 53.26100 1.000 9.32959  ? 573  HIS   B O    1 
ATOM   3763 C  CB   . HIS   B 1 139 ? -33.27800 39.21300 54.93000 1.000 10.57403 ? 573  HIS   B CB   1 
ATOM   3764 C  CG   . HIS   B 1 139 ? -34.07700 38.36100 54.01400 1.000 10.63847 ? 573  HIS   B CG   1 
ATOM   3765 N  ND1  . HIS   B 1 139 ? -33.60300 37.13100 53.62000 1.000 7.99162  ? 573  HIS   B ND1  1 
ATOM   3766 C  CD2  . HIS   B 1 139 ? -35.27100 38.50300 53.44000 1.000 7.88026  ? 573  HIS   B CD2  1 
ATOM   3767 C  CE1  . HIS   B 1 139 ? -34.48600 36.56800 52.82200 1.000 8.02370  ? 573  HIS   B CE1  1 
ATOM   3768 N  NE2  . HIS   B 1 139 ? -35.51200 37.37100 52.71500 1.000 15.73443 ? 573  HIS   B NE2  1 
ATOM   3769 N  N    . HIS   B 1 140 ? -34.11800 41.51100 52.61100 1.000 10.58526 ? 574  HIS   B N    1 
ATOM   3770 C  CA   . HIS   B 1 140 ? -33.85700 42.10300 51.26700 1.000 8.89656  ? 574  HIS   B CA   1 
ATOM   3771 C  C    . HIS   B 1 140 ? -33.74600 43.63000 51.31400 1.000 9.36662  ? 574  HIS   B C    1 
ATOM   3772 O  O    . HIS   B 1 140 ? -33.36400 44.20700 50.30300 1.000 15.03507 ? 574  HIS   B O    1 
ATOM   3773 C  CB   . HIS   B 1 140 ? -34.92400 41.66700 50.25900 1.000 8.75374  ? 574  HIS   B CB   1 
ATOM   3774 C  CG   . HIS   B 1 140 ? -35.04800 40.19800 50.05800 1.000 11.84272 ? 574  HIS   B CG   1 
ATOM   3775 N  ND1  . HIS   B 1 140 ? -33.99600 39.40600 49.66600 1.000 12.85708 ? 574  HIS   B ND1  1 
ATOM   3776 C  CD2  . HIS   B 1 140 ? -36.09900 39.38500 50.16900 1.000 10.53926 ? 574  HIS   B CD2  1 
ATOM   3777 C  CE1  . HIS   B 1 140 ? -34.41100 38.15700 49.55900 1.000 9.79185  ? 574  HIS   B CE1  1 
ATOM   3778 N  NE2  . HIS   B 1 140 ? -35.67900 38.12000 49.86600 1.000 10.29903 ? 574  HIS   B NE2  1 
ATOM   3779 N  N    . ALA   B 1 141 ? -34.06500 44.25200 52.44100 1.000 9.23846  ? 575  ALA   B N    1 
ATOM   3780 C  CA   . ALA   B 1 141 ? -34.06800 45.70600 52.48600 1.000 9.13639  ? 575  ALA   B CA   1 
ATOM   3781 C  C    . ALA   B 1 141 ? -32.64700 46.23600 52.60600 1.000 9.42735  ? 575  ALA   B C    1 
ATOM   3782 O  O    . ALA   B 1 141 ? -31.88100 45.79500 53.46800 1.000 13.16727 ? 575  ALA   B O    1 
ATOM   3783 C  CB   . ALA   B 1 141 ? -34.91300 46.20400 53.65700 1.000 9.32206  ? 575  ALA   B CB   1 
ATOM   3784 N  N    . GLU   B 1 142 ? -32.30900 47.19700 51.75600 1.000 12.58916 ? 576  GLU   B N    1 
ATOM   3785 C  CA   . GLU   B 1 142 ? -30.98500 47.79300 51.71400 1.000 13.26712 ? 576  GLU   B CA   1 
ATOM   3786 C  C    . GLU   B 1 142 ? -30.95300 49.06900 52.55200 1.000 17.62000 ? 576  GLU   B C    1 
ATOM   3787 O  O    . GLU   B 1 142 ? -31.96500 49.51600 53.09900 1.000 17.96196 ? 576  GLU   B O    1 
ATOM   3788 C  CB   . GLU   B 1 142 ? -30.58300 48.08900 50.26800 1.000 10.95238 ? 576  GLU   B CB   1 
ATOM   3789 C  CG   . GLU   B 1 142 ? -30.64000 46.88800 49.34200 1.000 11.03057 ? 576  GLU   B CG   1 
ATOM   3790 C  CD   . GLU   B 1 142 ? -29.36200 46.07200 49.35400 1.000 12.73890 ? 576  GLU   B CD   1 
ATOM   3791 O  OE1  . GLU   B 1 142 ? -28.60100 46.15900 50.34100 1.000 13.28633 ? 576  GLU   B OE1  1 
ATOM   3792 O  OE2  . GLU   B 1 142 ? -29.11500 45.34900 48.36600 1.000 19.03170 ? 576  GLU   B OE2  1 
ATOM   3793 N  N    . LYS   B 1 143 ? -29.76700 49.67800 52.63000 1.000 11.48016 ? 577  LYS   B N    1 
ATOM   3794 C  CA   . LYS   B 1 143 ? -29.61500 50.90900 53.39800 1.000 15.62053 ? 577  LYS   B CA   1 
ATOM   3795 C  C    . LYS   B 1 143 ? -30.53700 52.00500 52.87700 1.000 17.73158 ? 577  LYS   B C    1 
ATOM   3796 O  O    . LYS   B 1 143 ? -31.07200 52.80000 53.65900 1.000 13.31165 ? 577  LYS   B O    1 
ATOM   3797 C  CB   . LYS   B 1 143 ? -28.15500 51.36700 53.36800 1.000 11.98166 ? 577  LYS   B CB   1 
ATOM   3798 C  CG   . LYS   B 1 143 ? -27.90500 52.70400 54.05100 1.000 12.71128 ? 577  LYS   B CG   1 
ATOM   3799 C  CD   . LYS   B 1 143 ? -26.41400 52.99200 54.21400 1.000 15.67375 ? 577  LYS   B CD   1 
ATOM   3800 C  CE   . LYS   B 1 143 ? -25.97900 54.17800 53.36100 1.000 15.79252 ? 577  LYS   B CE   1 
ATOM   3801 N  NZ   . LYS   B 1 143 ? -26.90100 55.34000 53.52900 1.000 24.51106 ? 577  LYS   B NZ   1 
ATOM   3802 N  N    . ASP   B 1 144 ? -30.76200 52.05500 51.56300 1.000 14.79579 ? 578  ASP   B N    1 
ATOM   3803 C  CA   . ASP   B 1 144 ? -31.51200 53.16800 50.99300 1.000 16.50762 ? 578  ASP   B CA   1 
ATOM   3804 C  C    . ASP   B 1 144 ? -32.58800 52.70700 50.01500 1.000 18.56736 ? 578  ASP   B C    1 
ATOM   3805 O  O    . ASP   B 1 144 ? -32.99700 53.47400 49.14000 1.000 23.25805 ? 578  ASP   B O    1 
ATOM   3806 C  CB   . ASP   B 1 144 ? -30.57500 54.16700 50.31500 1.000 15.15844 ? 578  ASP   B CB   1 
ATOM   3807 N  N    . THR   B 1 145 ? -33.06900 51.48300 50.18200 1.000 11.76388 ? 579  THR   B N    1 
ATOM   3808 C  CA   . THR   B 1 145 ? -34.13400 51.03100 49.28600 1.000 15.46633 ? 579  THR   B CA   1 
ATOM   3809 C  C    . THR   B 1 145 ? -34.88700 49.84200 49.82000 1.000 13.11480 ? 579  THR   B C    1 
ATOM   3810 O  O    . THR   B 1 145 ? -34.33000 49.06300 50.57900 1.000 14.60596 ? 579  THR   B O    1 
ATOM   3811 C  CB   . THR   B 1 145 ? -33.60400 50.75300 47.86800 1.000 15.08044 ? 579  THR   B CB   1 
ATOM   3812 O  OG1  . THR   B 1 145 ? -34.62200 51.17300 46.97000 1.000 20.99766 ? 579  THR   B OG1  1 
ATOM   3813 C  CG2  . THR   B 1 145 ? -33.25900 49.29300 47.63600 1.000 11.77477 ? 579  THR   B CG2  1 
ATOM   3814 N  N    . ALA   B 1 146 ? -36.13500 49.74900 49.39900 1.000 15.77546 ? 580  ALA   B N    1 
ATOM   3815 C  CA   . ALA   B 1 146 ? -36.95100 48.58500 49.70400 1.000 13.53078 ? 580  ALA   B CA   1 
ATOM   3816 C  C    . ALA   B 1 146 ? -36.83800 47.56900 48.57500 1.000 10.47884 ? 580  ALA   B C    1 
ATOM   3817 O  O    . ALA   B 1 146 ? -36.52100 47.90900 47.43500 1.000 10.86287 ? 580  ALA   B O    1 
ATOM   3818 C  CB   . ALA   B 1 146 ? -38.41300 48.98100 49.91200 1.000 19.68484 ? 580  ALA   B CB   1 
ATOM   3819 N  N    . CYS   B 1 147 ? -37.11600 46.30900 48.90600 1.000 10.46442 ? 581  CYS   B N    1 
ATOM   3820 C  CA   . CYS   B 1 147 ? -36.86500 45.20700 47.98700 1.000 9.88975  ? 581  CYS   B CA   1 
ATOM   3821 C  C    . CYS   B 1 147 ? -37.52200 43.94800 48.52900 1.000 12.35674 ? 581  CYS   B C    1 
ATOM   3822 O  O    . CYS   B 1 147 ? -37.54300 43.73300 49.74100 1.000 9.07503  ? 581  CYS   B O    1 
ATOM   3823 C  CB   . CYS   B 1 147 ? -35.35600 44.97500 47.79900 1.000 9.99236  ? 581  CYS   B CB   1 
ATOM   3824 S  SG   . CYS   B 1 147 ? -34.90900 43.68000 46.59500 1.000 15.69252 ? 581  CYS   B SG   1 
ATOM   3825 N  N    . GLY   B 1 148 ? -38.05900 43.13100 47.62400 1.000 10.74210 ? 582  GLY   B N    1 
ATOM   3826 C  CA   . GLY   B 1 148 ? -38.56500 41.81100 47.95200 1.000 15.79865 ? 582  GLY   B CA   1 
ATOM   3827 C  C    . GLY   B 1 148 ? -39.42400 41.71700 49.19600 1.000 10.77603 ? 582  GLY   B C    1 
ATOM   3828 O  O    . GLY   B 1 148 ? -39.09800 40.97000 50.12400 1.000 11.13288 ? 582  GLY   B O    1 
ATOM   3829 N  N    . PHE   B 1 149 ? -40.51400 42.48300 49.22700 1.000 11.26017 ? 583  PHE   B N    1 
ATOM   3830 C  CA   . PHE   B 1 149 ? -41.51400 42.53500 50.29200 1.000 10.45179 ? 583  PHE   B CA   1 
ATOM   3831 C  C    . PHE   B 1 149 ? -40.95800 43.14000 51.57500 1.000 12.25091 ? 583  PHE   B C    1 
ATOM   3832 O  O    . PHE   B 1 149 ? -41.67800 43.19700 52.57600 1.000 11.12957 ? 583  PHE   B O    1 
ATOM   3833 C  CB   . PHE   B 1 149 ? -42.12300 41.15900 50.61600 1.000 13.79817 ? 583  PHE   B CB   1 
ATOM   3834 C  CG   . PHE   B 1 149 ? -42.45900 40.32200 49.39800 1.000 15.81530 ? 583  PHE   B CG   1 
ATOM   3835 C  CD1  . PHE   B 1 149 ? -42.69000 40.90400 48.15800 1.000 14.22808 ? 583  PHE   B CD1  1 
ATOM   3836 C  CD2  . PHE   B 1 149 ? -42.55400 38.94300 49.50500 1.000 14.57141 ? 583  PHE   B CD2  1 
ATOM   3837 C  CE1  . PHE   B 1 149 ? -42.98400 40.12500 47.04700 1.000 14.73895 ? 583  PHE   B CE1  1 
ATOM   3838 C  CE2  . PHE   B 1 149 ? -42.85400 38.16200 48.40600 1.000 9.46536  ? 583  PHE   B CE2  1 
ATOM   3839 C  CZ   . PHE   B 1 149 ? -43.06800 38.75300 47.17400 1.000 10.40338 ? 583  PHE   B CZ   1 
ATOM   3840 N  N    . CYS   B 1 150 ? -39.71100 43.60300 51.57800 1.000 12.76506 ? 584  CYS   B N    1 
ATOM   3841 C  CA   . CYS   B 1 150 ? -39.06900 44.18100 52.74900 1.000 8.86322  ? 584  CYS   B CA   1 
ATOM   3842 C  C    . CYS   B 1 150 ? -38.94500 45.68900 52.57900 1.000 9.01246  ? 584  CYS   B C    1 
ATOM   3843 O  O    . CYS   B 1 150 ? -38.59600 46.17200 51.49900 1.000 9.21841  ? 584  CYS   B O    1 
ATOM   3844 C  CB   . CYS   B 1 150 ? -37.67900 43.57900 52.96800 1.000 8.37562  ? 584  CYS   B CB   1 
ATOM   3845 S  SG   . CYS   B 1 150 ? -37.62000 41.77200 52.95200 1.000 11.28389 ? 584  CYS   B SG   1 
ATOM   3846 N  N    . PHE   B 1 151 ? -39.22200 46.42400 53.65300 1.000 10.63036 ? 585  PHE   B N    1 
ATOM   3847 C  CA   . PHE   B 1 151 ? -39.06800 47.87400 53.68800 1.000 13.45854 ? 585  PHE   B CA   1 
ATOM   3848 C  C    . PHE   B 1 151 ? -37.89100 48.31300 54.54700 1.000 13.30503 ? 585  PHE   B C    1 
ATOM   3849 O  O    . PHE   B 1 151 ? -37.10000 49.15900 54.12500 1.000 9.55884  ? 585  PHE   B O    1 
ATOM   3850 C  CB   . PHE   B 1 151 ? -40.35900 48.53400 54.19900 1.000 9.42105  ? 585  PHE   B CB   1 
ATOM   3851 C  CG   . PHE   B 1 151 ? -41.53700 48.35100 53.28500 1.000 10.21697 ? 585  PHE   B CG   1 
ATOM   3852 C  CD1  . PHE   B 1 151 ? -42.36000 47.24400 53.40800 1.000 13.19244 ? 585  PHE   B CD1  1 
ATOM   3853 C  CD2  . PHE   B 1 151 ? -41.82500 49.28800 52.30700 1.000 13.81514 ? 585  PHE   B CD2  1 
ATOM   3854 C  CE1  . PHE   B 1 151 ? -43.45100 47.07300 52.57200 1.000 11.27635 ? 585  PHE   B CE1  1 
ATOM   3855 C  CE2  . PHE   B 1 151 ? -42.91500 49.12300 51.46200 1.000 16.80073 ? 585  PHE   B CE2  1 
ATOM   3856 C  CZ   . PHE   B 1 151 ? -43.72900 48.01300 51.59500 1.000 10.52997 ? 585  PHE   B CZ   1 
ATOM   3857 N  N    . PHE   B 1 152 ? -37.76400 47.76600 55.75400 1.000 11.22743 ? 586  PHE   B N    1 
ATOM   3858 C  CA   . PHE   B 1 152 ? -36.60400 47.98200 56.60300 1.000 8.82040  ? 586  PHE   B CA   1 
ATOM   3859 C  C    . PHE   B 1 152 ? -36.04600 46.62800 57.01500 1.000 12.23122 ? 586  PHE   B C    1 
ATOM   3860 O  O    . PHE   B 1 152 ? -36.79400 45.66000 57.18100 1.000 9.93487  ? 586  PHE   B O    1 
ATOM   3861 C  CB   . PHE   B 1 152 ? -36.94800 48.81700 57.84500 1.000 8.89573  ? 586  PHE   B CB   1 
ATOM   3862 C  CG   . PHE   B 1 152 ? -37.62200 50.12600 57.53200 1.000 9.33295  ? 586  PHE   B CG   1 
ATOM   3863 C  CD1  . PHE   B 1 152 ? -36.98000 51.08900 56.77300 1.000 9.77917  ? 586  PHE   B CD1  1 
ATOM   3864 C  CD2  . PHE   B 1 152 ? -38.89300 50.39700 58.01100 1.000 9.38786  ? 586  PHE   B CD2  1 
ATOM   3865 C  CE1  . PHE   B 1 152 ? -37.59900 52.29700 56.48900 1.000 14.05667 ? 586  PHE   B CE1  1 
ATOM   3866 C  CE2  . PHE   B 1 152 ? -39.51400 51.60000 57.73300 1.000 9.86966  ? 586  PHE   B CE2  1 
ATOM   3867 C  CZ   . PHE   B 1 152 ? -38.86500 52.55300 56.97400 1.000 10.31252 ? 586  PHE   B CZ   1 
ATOM   3868 N  N    . ASN   B 1 153 ? -34.72200 46.55400 57.15500 1.000 9.69474  ? 587  ASN   B N    1 
ATOM   3869 C  CA   . ASN   B 1 153 ? -34.06600 45.28100 57.45600 1.000 11.18474 ? 587  ASN   B CA   1 
ATOM   3870 C  C    . ASN   B 1 153 ? -34.17800 45.02000 58.95300 1.000 13.52618 ? 587  ASN   B C    1 
ATOM   3871 O  O    . ASN   B 1 153 ? -33.34500 45.45000 59.75200 1.000 10.48291 ? 587  ASN   B O    1 
ATOM   3872 C  CB   . ASN   B 1 153 ? -32.61600 45.28500 56.98900 1.000 8.47314  ? 587  ASN   B CB   1 
ATOM   3873 C  CG   . ASN   B 1 153 ? -32.03300 43.88800 56.90500 1.000 10.36703 ? 587  ASN   B CG   1 
ATOM   3874 O  OD1  . ASN   B 1 153 ? -32.20000 43.07800 57.81800 1.000 10.85797 ? 587  ASN   B OD1  1 
ATOM   3875 N  ND2  . ASN   B 1 153 ? -31.35800 43.59300 55.80100 1.000 8.52182  ? 587  ASN   B ND2  1 
ATOM   3876 N  N    . THR   B 1 154 ? -35.22100 44.27000 59.32100 1.000 19.87032 ? 588  THR   B N    1 
ATOM   3877 C  CA   . THR   B 1 154 ? -35.54700 44.05300 60.72700 1.000 9.04684  ? 588  THR   B CA   1 
ATOM   3878 C  C    . THR   B 1 154 ? -34.40000 43.38600 61.47900 1.000 12.21273 ? 588  THR   B C    1 
ATOM   3879 O  O    . THR   B 1 154 ? -34.06700 43.78900 62.59900 1.000 9.26244  ? 588  THR   B O    1 
ATOM   3880 C  CB   . THR   B 1 154 ? -36.81700 43.20900 60.82700 1.000 7.56681  ? 588  THR   B CB   1 
ATOM   3881 O  OG1  . THR   B 1 154 ? -37.91500 43.92300 60.24200 1.000 7.68244  ? 588  THR   B OG1  1 
ATOM   3882 C  CG2  . THR   B 1 154 ? -37.13400 42.87800 62.27100 1.000 7.53000  ? 588  THR   B CG2  1 
ATOM   3883 N  N    . ALA   B 1 155 ? -33.78000 42.36700 60.87900 1.000 11.56634 ? 589  ALA   B N    1 
ATOM   3884 C  CA   . ALA   B 1 155 ? -32.71900 41.64000 61.56900 1.000 14.44575 ? 589  ALA   B CA   1 
ATOM   3885 C  C    . ALA   B 1 155 ? -31.43900 42.46400 61.65800 1.000 11.07825 ? 589  ALA   B C    1 
ATOM   3886 O  O    . ALA   B 1 155 ? -30.71600 42.39300 62.66000 1.000 8.01662  ? 589  ALA   B O    1 
ATOM   3887 C  CB   . ALA   B 1 155 ? -32.45700 40.31200 60.86300 1.000 19.24141 ? 589  ALA   B CB   1 
ATOM   3888 N  N    . ALA   B 1 156 ? -31.13400 43.24100 60.61800 1.000 8.38480  ? 590  ALA   B N    1 
ATOM   3889 C  CA   . ALA   B 1 156 ? -29.94700 44.08600 60.66100 1.000 10.15564 ? 590  ALA   B CA   1 
ATOM   3890 C  C    . ALA   B 1 156 ? -30.12100 45.22200 61.66000 1.000 18.83211 ? 590  ALA   B C    1 
ATOM   3891 O  O    . ALA   B 1 156 ? -29.19300 45.55200 62.40700 1.000 12.57469 ? 590  ALA   B O    1 
ATOM   3892 C  CB   . ALA   B 1 156 ? -29.64800 44.63500 59.26900 1.000 11.62355 ? 590  ALA   B CB   1 
ATOM   3893 N  N    . LEU   B 1 157 ? -31.30600 45.83300 61.68500 1.000 9.91473  ? 591  LEU   B N    1 
ATOM   3894 C  CA   . LEU   B 1 157 ? -31.57300 46.89200 62.65000 1.000 13.92698 ? 591  LEU   B CA   1 
ATOM   3895 C  C    . LEU   B 1 157 ? -31.49700 46.36900 64.07900 1.000 13.07862 ? 591  LEU   B C    1 
ATOM   3896 O  O    . LEU   B 1 157 ? -31.04100 47.07800 64.98100 1.000 12.92645 ? 591  LEU   B O    1 
ATOM   3897 C  CB   . LEU   B 1 157 ? -32.94100 47.51600 62.38000 1.000 12.16678 ? 591  LEU   B CB   1 
ATOM   3898 C  CG   . LEU   B 1 157 ? -33.00700 48.49600 61.21100 1.000 11.44459 ? 591  LEU   B CG   1 
ATOM   3899 C  CD1  . LEU   B 1 157 ? -34.45200 48.73000 60.78000 1.000 12.15766 ? 591  LEU   B CD1  1 
ATOM   3900 C  CD2  . LEU   B 1 157 ? -32.34000 49.80100 61.58100 1.000 9.23913  ? 591  LEU   B CD2  1 
ATOM   3901 N  N    . THR   B 1 158 ? -31.93800 45.12800 64.30500 1.000 11.88796 ? 592  THR   B N    1 
ATOM   3902 C  CA   . THR   B 1 158 ? -31.92700 44.57900 65.65700 1.000 8.14971  ? 592  THR   B CA   1 
ATOM   3903 C  C    . THR   B 1 158 ? -30.50700 44.27900 66.12300 1.000 13.59438 ? 592  THR   B C    1 
ATOM   3904 O  O    . THR   B 1 158 ? -30.19200 44.43800 67.30700 1.000 8.51373  ? 592  THR   B O    1 
ATOM   3905 C  CB   . THR   B 1 158 ? -32.79800 43.32600 65.72200 1.000 7.91045  ? 592  THR   B CB   1 
ATOM   3906 O  OG1  . THR   B 1 158 ? -34.13900 43.66500 65.35500 1.000 8.75775  ? 592  THR   B OG1  1 
ATOM   3907 C  CG2  . THR   B 1 158 ? -32.81800 42.75300 67.12200 1.000 8.14756  ? 592  THR   B CG2  1 
ATOM   3908 N  N    . ALA   B 1 159 ? -29.63300 43.84700 65.21100 1.000 13.83988 ? 593  ALA   B N    1 
ATOM   3909 C  CA   . ALA   B 1 159 ? -28.22500 43.68800 65.56400 1.000 11.72802 ? 593  ALA   B CA   1 
ATOM   3910 C  C    . ALA   B 1 159 ? -27.63900 45.01100 66.04200 1.000 11.69177 ? 593  ALA   B C    1 
ATOM   3911 O  O    . ALA   B 1 159 ? -26.98400 45.07400 67.08900 1.000 13.89842 ? 593  ALA   B O    1 
ATOM   3912 C  CB   . ALA   B 1 159 ? -27.43700 43.14700 64.37000 1.000 9.85691  ? 593  ALA   B CB   1 
ATOM   3913 N  N    . ARG   B 1 160 ? -27.88100 46.08400 65.28900 1.000 16.59918 ? 594  ARG   B N    1 
ATOM   3914 C  CA   . ARG   B 1 160 ? -27.37600 47.39700 65.67300 1.000 16.26216 ? 594  ARG   B CA   1 
ATOM   3915 C  C    . ARG   B 1 160 ? -28.06300 47.90900 66.93000 1.000 11.23088 ? 594  ARG   B C    1 
ATOM   3916 O  O    . ARG   B 1 160 ? -27.42600 48.55600 67.76900 1.000 12.65124 ? 594  ARG   B O    1 
ATOM   3917 C  CB   . ARG   B 1 160 ? -27.56000 48.38400 64.52200 1.000 11.72745 ? 594  ARG   B CB   1 
ATOM   3918 C  CG   . ARG   B 1 160 ? -26.63900 48.12500 63.33800 1.000 19.63117 ? 594  ARG   B CG   1 
ATOM   3919 C  CD   . ARG   B 1 160 ? -25.28000 48.77400 63.54500 1.000 15.21556 ? 594  ARG   B CD   1 
ATOM   3920 N  NE   . ARG   B 1 160 ? -24.39700 48.56800 62.40300 1.000 18.42750 ? 594  ARG   B NE   1 
ATOM   3921 C  CZ   . ARG   B 1 160 ? -23.29200 47.83700 62.43200 1.000 18.88474 ? 594  ARG   B CZ   1 
ATOM   3922 N  NH1  . ARG   B 1 160 ? -22.88000 47.24800 63.54500 1.000 14.70397 ? 594  ARG   B NH1  1 
ATOM   3923 N  NH2  . ARG   B 1 160 ? -22.57600 47.70000 61.32000 1.000 21.20821 ? 594  ARG   B NH2  1 
ATOM   3924 N  N    . TYR   B 1 161 ? -29.36600 47.64700 67.07300 1.000 13.28780 ? 595  TYR   B N    1 
ATOM   3925 C  CA   . TYR   B 1 161 ? -30.05500 48.03900 68.29700 1.000 9.92715  ? 595  TYR   B CA   1 
ATOM   3926 C  C    . TYR   B 1 161 ? -29.45400 47.33400 69.50400 1.000 15.50928 ? 595  TYR   B C    1 
ATOM   3927 O  O    . TYR   B 1 161 ? -29.21900 47.95300 70.54900 1.000 14.17720 ? 595  TYR   B O    1 
ATOM   3928 C  CB   . TYR   B 1 161 ? -31.55200 47.73600 68.20800 1.000 17.49365 ? 595  TYR   B CB   1 
ATOM   3929 C  CG   . TYR   B 1 161 ? -32.21500 47.90600 69.55700 1.000 11.88935 ? 595  TYR   B CG   1 
ATOM   3930 C  CD1  . TYR   B 1 161 ? -32.59200 49.16300 70.00700 1.000 9.25710  ? 595  TYR   B CD1  1 
ATOM   3931 C  CD2  . TYR   B 1 161 ? -32.41100 46.81800 70.40400 1.000 9.08282  ? 595  TYR   B CD2  1 
ATOM   3932 C  CE1  . TYR   B 1 161 ? -33.16400 49.32800 71.24600 1.000 9.39478  ? 595  TYR   B CE1  1 
ATOM   3933 C  CE2  . TYR   B 1 161 ? -32.98000 46.97500 71.64800 1.000 9.01614  ? 595  TYR   B CE2  1 
ATOM   3934 C  CZ   . TYR   B 1 161 ? -33.35900 48.23100 72.06100 1.000 9.27126  ? 595  TYR   B CZ   1 
ATOM   3935 O  OH   . TYR   B 1 161 ? -33.92700 48.39900 73.30100 1.000 12.85746 ? 595  TYR   B OH   1 
ATOM   3936 N  N    . ALA   B 1 162 ? -29.22900 46.02300 69.38500 1.000 9.61419  ? 596  ALA   B N    1 
ATOM   3937 C  CA   . ALA   B 1 162 ? -28.65100 45.26600 70.48800 1.000 11.76238 ? 596  ALA   B CA   1 
ATOM   3938 C  C    . ALA   B 1 162 ? -27.30900 45.84800 70.90700 1.000 11.53196 ? 596  ALA   B C    1 
ATOM   3939 O  O    . ALA   B 1 162 ? -27.01200 45.94800 72.10500 1.000 10.74456 ? 596  ALA   B O    1 
ATOM   3940 C  CB   . ALA   B 1 162 ? -28.50300 43.79700 70.09300 1.000 9.08451  ? 596  ALA   B CB   1 
ATOM   3941 N  N    . GLN   B 1 163 ? -26.49400 46.26000 69.93500 1.000 9.87011  ? 597  GLN   B N    1 
ATOM   3942 C  CA   . GLN   B 1 163 ? -25.20800 46.86500 70.26000 1.000 13.43335 ? 597  GLN   B CA   1 
ATOM   3943 C  C    . GLN   B 1 163 ? -25.38600 48.21700 70.93800 1.000 14.70217 ? 597  GLN   B C    1 
ATOM   3944 O  O    . GLN   B 1 163 ? -24.63100 48.56000 71.85700 1.000 14.01919 ? 597  GLN   B O    1 
ATOM   3945 C  CB   . GLN   B 1 163 ? -24.36100 47.00700 68.99800 1.000 12.17069 ? 597  GLN   B CB   1 
ATOM   3946 C  CG   . GLN   B 1 163 ? -23.93000 45.68900 68.39200 1.000 24.49753 ? 597  GLN   B CG   1 
ATOM   3947 C  CD   . GLN   B 1 163 ? -23.12700 45.87000 67.11900 1.000 25.02458 ? 597  GLN   B CD   1 
ATOM   3948 O  OE1  . GLN   B 1 163 ? -23.27000 46.86900 66.41100 1.000 21.13020 ? 597  GLN   B OE1  1 
ATOM   3949 N  NE2  . GLN   B 1 163 ? -22.26500 44.90800 66.82900 1.000 18.86414 ? 597  GLN   B NE2  1 
ATOM   3950 N  N    . SER   B 1 164 ? -26.38200 48.99700 70.50800 1.000 10.50179 ? 598  SER   B N    1 
ATOM   3951 C  CA   . SER   B 1 164 ? -26.57200 50.32400 71.08100 1.000 12.32093 ? 598  SER   B CA   1 
ATOM   3952 C  C    . SER   B 1 164 ? -26.94400 50.26700 72.55900 1.000 15.93659 ? 598  SER   B C    1 
ATOM   3953 O  O    . SER   B 1 164 ? -26.69500 51.23700 73.28400 1.000 20.31618 ? 598  SER   B O    1 
ATOM   3954 C  CB   . SER   B 1 164 ? -27.63200 51.10400 70.29200 1.000 12.27071 ? 598  SER   B CB   1 
ATOM   3955 O  OG   . SER   B 1 164 ? -28.93600 50.58100 70.47900 1.000 10.25815 ? 598  SER   B OG   1 
ATOM   3956 N  N    . ILE   B 1 165 ? -27.51400 49.15400 73.03000 1.000 11.39583 ? 599  ILE   B N    1 
ATOM   3957 C  CA   . ILE   B 1 165 ? -27.89500 49.02600 74.43400 1.000 10.68184 ? 599  ILE   B CA   1 
ATOM   3958 C  C    . ILE   B 1 165 ? -26.92400 48.16800 75.23200 1.000 12.68361 ? 599  ILE   B C    1 
ATOM   3959 O  O    . ILE   B 1 165 ? -27.09500 48.03100 76.45000 1.000 21.43446 ? 599  ILE   B O    1 
ATOM   3960 C  CB   . ILE   B 1 165 ? -29.32600 48.47100 74.58400 1.000 10.30119 ? 599  ILE   B CB   1 
ATOM   3961 C  CG1  . ILE   B 1 165 ? -29.42400 47.06000 74.00400 1.000 11.06527 ? 599  ILE   B CG1  1 
ATOM   3962 C  CG2  . ILE   B 1 165 ? -30.33900 49.40700 73.93400 1.000 10.19184 ? 599  ILE   B CG2  1 
ATOM   3963 C  CD1  . ILE   B 1 165 ? -30.71200 46.34400 74.37300 1.000 13.24187 ? 599  ILE   B CD1  1 
ATOM   3964 N  N    . THR   B 1 166 ? -25.91400 47.57600 74.58800 1.000 16.79477 ? 600  THR   B N    1 
ATOM   3965 C  CA   . THR   B 1 166 ? -24.88000 46.83600 75.31000 1.000 18.54795 ? 600  THR   B CA   1 
ATOM   3966 C  C    . THR   B 1 166 ? -23.51100 47.46500 75.08500 1.000 15.79187 ? 600  THR   B C    1 
ATOM   3967 O  O    . THR   B 1 166 ? -22.97700 48.10600 75.99500 1.000 15.06044 ? 600  THR   B O    1 
ATOM   3968 C  CB   . THR   B 1 166 ? -24.89200 45.35700 74.90700 1.000 19.49983 ? 600  THR   B CB   1 
ATOM   3969 O  OG1  . THR   B 1 166 ? -24.82400 45.23400 73.47900 1.000 10.74698 ? 600  THR   B OG1  1 
ATOM   3970 C  CG2  . THR   B 1 166 ? -26.15500 44.67100 75.41500 1.000 19.81061 ? 600  THR   B CG2  1 
ATOM   3971 N  N    . ARG   B 1 167 ? -22.92300 47.29400 73.90500 1.000 13.28275 ? 601  ARG   B N    1 
ATOM   3972 C  CA   . ARG   B 1 167 ? -21.68600 47.95000 73.50500 1.000 12.31595 ? 601  ARG   B CA   1 
ATOM   3973 C  C    . ARG   B 1 167 ? -21.50500 47.69000 72.01900 1.000 12.64820 ? 601  ARG   B C    1 
ATOM   3974 O  O    . ARG   B 1 167 ? -22.11300 46.77200 71.46200 1.000 13.47764 ? 601  ARG   B O    1 
ATOM   3975 C  CB   . ARG   B 1 167 ? -20.48400 47.44500 74.30700 1.000 15.94850 ? 601  ARG   B CB   1 
ATOM   3976 C  CG   . ARG   B 1 167 ? -20.49200 45.95000 74.51800 1.000 15.20787 ? 601  ARG   B CG   1 
ATOM   3977 C  CD   . ARG   B 1 167 ? -19.31100 45.48400 75.34000 1.000 20.41630 ? 601  ARG   B CD   1 
ATOM   3978 N  NE   . ARG   B 1 167 ? -18.75200 44.26600 74.77000 1.000 31.59053 ? 601  ARG   B NE   1 
ATOM   3979 C  CZ   . ARG   B 1 167 ? -19.31700 43.07100 74.86400 1.000 23.34145 ? 601  ARG   B CZ   1 
ATOM   3980 N  NH1  . ARG   B 1 167 ? -20.44800 42.89100 75.52800 1.000 25.72673 ? 601  ARG   B NH1  1 
ATOM   3981 N  NH2  . ARG   B 1 167 ? -18.73700 42.03400 74.27000 1.000 20.65039 ? 601  ARG   B NH2  1 
ATOM   3982 N  N    . GLU   B 1 168 ? -20.67200 48.51100 71.37800 1.000 12.59959 ? 602  GLU   B N    1 
ATOM   3983 C  CA   . GLU   B 1 168 ? -20.52200 48.38200 69.93300 1.000 19.49331 ? 602  GLU   B CA   1 
ATOM   3984 C  C    . GLU   B 1 168 ? -19.73800 47.13700 69.53400 1.000 24.33768 ? 602  GLU   B C    1 
ATOM   3985 O  O    . GLU   B 1 168 ? -19.85000 46.69700 68.38500 1.000 21.91543 ? 602  GLU   B O    1 
ATOM   3986 C  CB   . GLU   B 1 168 ? -19.86700 49.63400 69.34200 1.000 19.50107 ? 602  GLU   B CB   1 
ATOM   3987 C  CG   . GLU   B 1 168 ? -18.62500 50.11400 70.05800 1.000 30.24396 ? 602  GLU   B CG   1 
ATOM   3988 C  CD   . GLU   B 1 168 ? -17.94800 51.26000 69.32300 1.000 36.13130 ? 602  GLU   B CD   1 
ATOM   3989 O  OE1  . GLU   B 1 168 ? -18.25100 51.45400 68.12500 1.000 32.98178 ? 602  GLU   B OE1  1 
ATOM   3990 O  OE2  . GLU   B 1 168 ? -17.11600 51.96500 69.93800 1.000 40.96110 ? 602  GLU   B OE2  1 
ATOM   3991 N  N    . SER   B 1 169 ? -18.96900 46.54600 70.44700 1.000 17.30774 ? 603  SER   B N    1 
ATOM   3992 C  CA   . SER   B 1 169 ? -18.21900 45.33500 70.14000 1.000 16.49893 ? 603  SER   B CA   1 
ATOM   3993 C  C    . SER   B 1 169 ? -19.01700 44.06400 70.40600 1.000 19.35734 ? 603  SER   B C    1 
ATOM   3994 O  O    . SER   B 1 169 ? -18.46400 42.96400 70.28800 1.000 16.16607 ? 603  SER   B O    1 
ATOM   3995 C  CB   . SER   B 1 169 ? -16.90700 45.30300 70.93400 1.000 13.87614 ? 603  SER   B CB   1 
ATOM   3996 O  OG   . SER   B 1 169 ? -17.13500 45.02600 72.30600 1.000 22.11032 ? 603  SER   B OG   1 
ATOM   3997 N  N    . LEU   B 1 170 ? -20.29300 44.18700 70.77000 1.000 14.11534 ? 604  LEU   B N    1 
ATOM   3998 C  CA   . LEU   B 1 170 ? -21.12500 43.00900 70.97900 1.000 20.18091 ? 604  LEU   B CA   1 
ATOM   3999 C  C    . LEU   B 1 170 ? -21.17900 42.17800 69.70400 1.000 20.72042 ? 604  LEU   B C    1 
ATOM   4000 O  O    . LEU   B 1 170 ? -21.52600 42.68200 68.63200 1.000 23.77481 ? 604  LEU   B O    1 
ATOM   4001 C  CB   . LEU   B 1 170 ? -22.53700 43.41400 71.40000 1.000 14.62576 ? 604  LEU   B CB   1 
ATOM   4002 C  CG   . LEU   B 1 170 ? -23.43300 42.23200 71.79000 1.000 17.89825 ? 604  LEU   B CG   1 
ATOM   4003 C  CD1  . LEU   B 1 170 ? -23.27000 41.89200 73.26700 1.000 17.64308 ? 604  LEU   B CD1  1 
ATOM   4004 C  CD2  . LEU   B 1 170 ? -24.88900 42.49400 71.44000 1.000 10.16827 ? 604  LEU   B CD2  1 
ATOM   4005 N  N    . ARG   B 1 171 ? -20.83200 40.89900 69.82300 1.000 17.84069 ? 605  ARG   B N    1 
ATOM   4006 C  CA   . ARG   B 1 171 ? -20.71300 40.01300 68.67000 1.000 12.12640 ? 605  ARG   B CA   1 
ATOM   4007 C  C    . ARG   B 1 171 ? -22.07000 39.39300 68.37400 1.000 11.82386 ? 605  ARG   B C    1 
ATOM   4008 O  O    . ARG   B 1 171 ? -22.57100 38.58000 69.15700 1.000 11.26356 ? 605  ARG   B O    1 
ATOM   4009 C  CB   . ARG   B 1 171 ? -19.66300 38.93700 68.93100 1.000 12.00907 ? 605  ARG   B CB   1 
ATOM   4010 C  CG   . ARG   B 1 171 ? -18.26200 39.48200 69.14000 1.000 13.40911 ? 605  ARG   B CG   1 
ATOM   4011 C  CD   . ARG   B 1 171 ? -17.25000 38.34900 69.24900 1.000 18.84398 ? 605  ARG   B CD   1 
ATOM   4012 N  NE   . ARG   B 1 171 ? -17.52200 37.50900 70.40700 1.000 26.65647 ? 605  ARG   B NE   1 
ATOM   4013 C  CZ   . ARG   B 1 171 ? -16.94400 37.65500 71.59200 1.000 31.36114 ? 605  ARG   B CZ   1 
ATOM   4014 N  NH1  . ARG   B 1 171 ? -16.02000 38.57800 71.79900 1.000 28.72223 ? 605  ARG   B NH1  1 
ATOM   4015 N  NH2  . ARG   B 1 171 ? -17.30300 36.85500 72.59300 1.000 22.01625 ? 605  ARG   B NH2  1 
ATOM   4016 N  N    . VAL   B 1 172 ? -22.66300 39.76600 67.24400 1.000 10.39783 ? 606  VAL   B N    1 
ATOM   4017 C  CA   . VAL   B 1 172 ? -23.96300 39.25000 66.83000 1.000 9.88064  ? 606  VAL   B CA   1 
ATOM   4018 C  C    . VAL   B 1 172 ? -23.76600 38.32900 65.63800 1.000 14.35864 ? 606  VAL   B C    1 
ATOM   4019 O  O    . VAL   B 1 172 ? -23.16000 38.71700 64.63300 1.000 10.05254 ? 606  VAL   B O    1 
ATOM   4020 C  CB   . VAL   B 1 172 ? -24.95000 40.37900 66.48400 1.000 14.25733 ? 606  VAL   B CB   1 
ATOM   4021 C  CG1  . VAL   B 1 172 ? -26.30400 39.79000 66.11100 1.000 11.39865 ? 606  VAL   B CG1  1 
ATOM   4022 C  CG2  . VAL   B 1 172 ? -25.09300 41.34800 67.65200 1.000 9.58757  ? 606  VAL   B CG2  1 
ATOM   4023 N  N    . LEU   B 1 173 ? -24.27200 37.11000 65.75600 1.000 15.46243 ? 607  LEU   B N    1 
ATOM   4024 C  CA   . LEU   B 1 173 ? -24.36400 36.17800 64.64500 1.000 9.74977  ? 607  LEU   B CA   1 
ATOM   4025 C  C    . LEU   B 1 173 ? -25.76900 36.26100 64.06400 1.000 19.76498 ? 607  LEU   B C    1 
ATOM   4026 O  O    . LEU   B 1 173 ? -26.75400 36.21600 64.81000 1.000 12.51838 ? 607  LEU   B O    1 
ATOM   4027 C  CB   . LEU   B 1 173 ? -24.06100 34.75700 65.11500 1.000 10.04873 ? 607  LEU   B CB   1 
ATOM   4028 C  CG   . LEU   B 1 173 ? -24.49000 33.61100 64.20800 1.000 10.00441 ? 607  LEU   B CG   1 
ATOM   4029 C  CD1  . LEU   B 1 173 ? -23.67000 33.60900 62.92200 1.000 14.76145 ? 607  LEU   B CD1  1 
ATOM   4030 C  CD2  . LEU   B 1 173 ? -24.36100 32.28800 64.94000 1.000 10.34916 ? 607  LEU   B CD2  1 
ATOM   4031 N  N    . ILE   B 1 174 ? -25.85800 36.40700 62.74400 1.000 13.42183 ? 608  ILE   B N    1 
ATOM   4032 C  CA   . ILE   B 1 174 ? -27.13200 36.45400 62.03400 1.000 11.69987 ? 608  ILE   B CA   1 
ATOM   4033 C  C    . ILE   B 1 174 ? -27.13800 35.28800 61.05800 1.000 9.18478  ? 608  ILE   B C    1 
ATOM   4034 O  O    . ILE   B 1 174 ? -26.48700 35.35100 60.00800 1.000 9.04632  ? 608  ILE   B O    1 
ATOM   4035 C  CB   . ILE   B 1 174 ? -27.35300 37.78000 61.30000 1.000 13.42660 ? 608  ILE   B CB   1 
ATOM   4036 C  CG1  . ILE   B 1 174 ? -27.39800 38.95200 62.28000 1.000 8.60662  ? 608  ILE   B CG1  1 
ATOM   4037 C  CG2  . ILE   B 1 174 ? -28.64100 37.72400 60.49300 1.000 14.73919 ? 608  ILE   B CG2  1 
ATOM   4038 C  CD1  . ILE   B 1 174 ? -27.70700 40.27600 61.61700 1.000 8.55129  ? 608  ILE   B CD1  1 
ATOM   4039 N  N    . VAL   B 1 175 ? -27.86600 34.22600 61.39100 1.000 8.79274  ? 609  VAL   B N    1 
ATOM   4040 C  CA   . VAL   B 1 175 ? -28.05500 33.10200 60.48200 1.000 10.63812 ? 609  VAL   B CA   1 
ATOM   4041 C  C    . VAL   B 1 175 ? -29.34500 33.33200 59.70900 1.000 9.23147  ? 609  VAL   B C    1 
ATOM   4042 O  O    . VAL   B 1 175 ? -30.42600 33.43400 60.29700 1.000 13.04390 ? 609  VAL   B O    1 
ATOM   4043 C  CB   . VAL   B 1 175 ? -28.09200 31.76300 61.23200 1.000 9.14557  ? 609  VAL   B CB   1 
ATOM   4044 C  CG1  . VAL   B 1 175 ? -28.14000 30.61500 60.23500 1.000 14.04731 ? 609  VAL   B CG1  1 
ATOM   4045 C  CG2  . VAL   B 1 175 ? -26.87900 31.62900 62.13700 1.000 9.52100  ? 609  VAL   B CG2  1 
ATOM   4046 N  N    . ASP   B 1 176 ? -29.23000 33.42000 58.39200 1.000 11.17319 ? 610  ASP   B N    1 
ATOM   4047 C  CA   . ASP   B 1 176 ? -30.34900 33.70700 57.50000 1.000 12.89220 ? 610  ASP   B CA   1 
ATOM   4048 C  C    . ASP   B 1 176 ? -30.65200 32.42000 56.74000 1.000 10.97175 ? 610  ASP   B C    1 
ATOM   4049 O  O    . ASP   B 1 176 ? -30.07700 32.16400 55.68100 1.000 11.20179 ? 610  ASP   B O    1 
ATOM   4050 C  CB   . ASP   B 1 176 ? -29.99200 34.86300 56.55300 1.000 14.82439 ? 610  ASP   B CB   1 
ATOM   4051 C  CG   . ASP   B 1 176 ? -31.16500 35.32300 55.70300 1.000 8.18000  ? 610  ASP   B CG   1 
ATOM   4052 O  OD1  . ASP   B 1 176 ? -32.11600 34.54400 55.49400 1.000 9.02294  ? 610  ASP   B OD1  1 
ATOM   4053 O  OD2  . ASP   B 1 176 ? -31.12400 36.48200 55.23800 1.000 9.81152  ? 610  ASP   B OD2  1 
ATOM   4054 N  N    . TRP   B 1 177 ? -31.55400 31.60100 57.28600 1.000 8.53479  ? 611  TRP   B N    1 
ATOM   4055 C  CA   . TRP   B 1 177 ? -31.94100 30.36700 56.61900 1.000 8.71918  ? 611  TRP   B CA   1 
ATOM   4056 C  C    . TRP   B 1 177 ? -33.22300 30.51900 55.80900 1.000 11.91741 ? 611  TRP   B C    1 
ATOM   4057 O  O    . TRP   B 1 177 ? -33.81300 29.51300 55.40700 1.000 14.30196 ? 611  TRP   B O    1 
ATOM   4058 C  CB   . TRP   B 1 177 ? -32.04700 29.21000 57.62600 1.000 8.95769  ? 611  TRP   B CB   1 
ATOM   4059 C  CG   . TRP   B 1 177 ? -33.20800 29.21200 58.60100 1.000 17.46625 ? 611  TRP   B CG   1 
ATOM   4060 C  CD1  . TRP   B 1 177 ? -34.49700 29.61700 58.37100 1.000 18.36607 ? 611  TRP   B CD1  1 
ATOM   4061 C  CD2  . TRP   B 1 177 ? -33.17300 28.75200 59.95800 1.000 15.48660 ? 611  TRP   B CD2  1 
ATOM   4062 N  NE1  . TRP   B 1 177 ? -35.25800 29.44300 59.50200 1.000 16.42552 ? 611  TRP   B NE1  1 
ATOM   4063 C  CE2  . TRP   B 1 177 ? -34.47000 28.91700 60.49100 1.000 17.84164 ? 611  TRP   B CE2  1 
ATOM   4064 C  CE3  . TRP   B 1 177 ? -32.16800 28.22400 60.77700 1.000 9.29996  ? 611  TRP   B CE3  1 
ATOM   4065 C  CZ2  . TRP   B 1 177 ? -34.78800 28.57300 61.80400 1.000 16.22445 ? 611  TRP   B CZ2  1 
ATOM   4066 C  CZ3  . TRP   B 1 177 ? -32.48500 27.88000 62.07800 1.000 15.71681 ? 611  TRP   B CZ3  1 
ATOM   4067 C  CH2  . TRP   B 1 177 ? -33.78400 28.05900 62.58100 1.000 21.02702 ? 611  TRP   B CH2  1 
ATOM   4068 N  N    . ASP   B 1 178 ? -33.66500 31.75200 55.56800 1.000 9.05551  ? 612  ASP   B N    1 
ATOM   4069 C  CA   . ASP   B 1 178 ? -34.63500 32.00700 54.51200 1.000 9.89860  ? 612  ASP   B CA   1 
ATOM   4070 C  C    . ASP   B 1 178 ? -34.06900 31.51300 53.18200 1.000 15.28338 ? 612  ASP   B C    1 
ATOM   4071 O  O    . ASP   B 1 178 ? -32.86600 31.61500 52.92800 1.000 12.38207 ? 612  ASP   B O    1 
ATOM   4072 C  CB   . ASP   B 1 178 ? -34.95000 33.50700 54.45200 1.000 13.32495 ? 612  ASP   B CB   1 
ATOM   4073 C  CG   . ASP   B 1 178 ? -36.07000 33.84700 53.47700 1.000 15.36609 ? 612  ASP   B CG   1 
ATOM   4074 O  OD1  . ASP   B 1 178 ? -35.89900 33.63300 52.25600 1.000 16.23760 ? 612  ASP   B OD1  1 
ATOM   4075 O  OD2  . ASP   B 1 178 ? -37.12000 34.34100 53.94100 1.000 9.06253  ? 612  ASP   B OD2  1 
ATOM   4076 N  N    . VAL   B 1 179 ? -34.93800 30.95800 52.33100 1.000 14.45970 ? 613  VAL   B N    1 
ATOM   4077 C  CA   . VAL   B 1 179 ? -34.45000 30.33100 51.10500 1.000 9.00795  ? 613  VAL   B CA   1 
ATOM   4078 C  C    . VAL   B 1 179 ? -33.83800 31.34600 50.14800 1.000 10.39279 ? 613  VAL   B C    1 
ATOM   4079 O  O    . VAL   B 1 179 ? -33.04500 30.96700 49.27900 1.000 14.38382 ? 613  VAL   B O    1 
ATOM   4080 C  CB   . VAL   B 1 179 ? -35.57200 29.54200 50.40700 1.000 12.02993 ? 613  VAL   B CB   1 
ATOM   4081 C  CG1  . VAL   B 1 179 ? -36.43000 30.46300 49.55200 1.000 12.25940 ? 613  VAL   B CG1  1 
ATOM   4082 C  CG2  . VAL   B 1 179 ? -34.98600 28.42300 49.56400 1.000 10.10553 ? 613  VAL   B CG2  1 
ATOM   4083 N  N    . HIS   B 1 180 ? -34.18700 32.62200 50.27400 1.000 9.06806  ? 614  HIS   B N    1 
ATOM   4084 C  CA   . HIS   B 1 180 ? -33.58900 33.67400 49.46900 1.000 12.92332 ? 614  HIS   B CA   1 
ATOM   4085 C  C    . HIS   B 1 180 ? -32.41400 34.30100 50.21300 1.000 12.18757 ? 614  HIS   B C    1 
ATOM   4086 O  O    . HIS   B 1 180 ? -32.36100 34.30500 51.44600 1.000 11.83603 ? 614  HIS   B O    1 
ATOM   4087 C  CB   . HIS   B 1 180 ? -34.61500 34.75900 49.12600 1.000 11.86689 ? 614  HIS   B CB   1 
ATOM   4088 C  CG   . HIS   B 1 180 ? -35.81700 34.25700 48.38100 1.000 19.56646 ? 614  HIS   B CG   1 
ATOM   4089 N  ND1  . HIS   B 1 180 ? -36.90600 33.69500 49.01300 1.000 12.81830 ? 614  HIS   B ND1  1 
ATOM   4090 C  CD2  . HIS   B 1 180 ? -36.10800 34.25000 47.05900 1.000 9.39363  ? 614  HIS   B CD2  1 
ATOM   4091 C  CE1  . HIS   B 1 180 ? -37.81200 33.35900 48.11400 1.000 8.88319  ? 614  HIS   B CE1  1 
ATOM   4092 N  NE2  . HIS   B 1 180 ? -37.35300 33.68500 46.92000 1.000 12.21871 ? 614  HIS   B NE2  1 
ATOM   4093 N  N    . HIS   B 1 181 ? -31.47200 34.84100 49.45000 1.000 13.24573 ? 615  HIS   B N    1 
ATOM   4094 C  CA   . HIS   B 1 181 ? -30.30600 35.47300 50.04500 1.000 11.04419 ? 615  HIS   B CA   1 
ATOM   4095 C  C    . HIS   B 1 181 ? -30.68000 36.84100 50.59100 1.000 10.24567 ? 615  HIS   B C    1 
ATOM   4096 O  O    . HIS   B 1 181 ? -31.38700 37.61100 49.93600 1.000 9.39640  ? 615  HIS   B O    1 
ATOM   4097 C  CB   . HIS   B 1 181 ? -29.18300 35.61700 49.01800 1.000 12.84596 ? 615  HIS   B CB   1 
ATOM   4098 C  CG   . HIS   B 1 181 ? -27.95000 36.26800 49.56600 1.000 9.87074  ? 615  HIS   B CG   1 
ATOM   4099 N  ND1  . HIS   B 1 181 ? -27.42600 37.43000 49.04300 1.000 12.50759 ? 615  HIS   B ND1  1 
ATOM   4100 C  CD2  . HIS   B 1 181 ? -27.14700 35.92500 50.60100 1.000 13.23269 ? 615  HIS   B CD2  1 
ATOM   4101 C  CE1  . HIS   B 1 181 ? -26.34700 37.76900 49.72500 1.000 16.90057 ? 615  HIS   B CE1  1 
ATOM   4102 N  NE2  . HIS   B 1 181 ? -26.15800 36.87500 50.67900 1.000 13.27987 ? 615  HIS   B NE2  1 
ATOM   4103 N  N    . GLY   B 1 182 ? -30.19900 37.14000 51.79700 1.000 11.38255 ? 616  GLY   B N    1 
ATOM   4104 C  CA   . GLY   B 1 182 ? -30.42000 38.44300 52.39600 1.000 11.77457 ? 616  GLY   B CA   1 
ATOM   4105 C  C    . GLY   B 1 182 ? -29.42500 39.47500 51.90800 1.000 12.60393 ? 616  GLY   B C    1 
ATOM   4106 O  O    . GLY   B 1 182 ? -28.45800 39.80000 52.60400 1.000 12.73397 ? 616  GLY   B O    1 
ATOM   4107 N  N    . ASN   B 1 183 ? -29.64900 39.98400 50.69500 1.000 14.60126 ? 617  ASN   B N    1 
ATOM   4108 C  CA   . ASN   B 1 183 ? -28.74300 40.97200 50.11600 1.000 15.39697 ? 617  ASN   B CA   1 
ATOM   4109 C  C    . ASN   B 1 183 ? -28.60000 42.19200 51.01500 1.000 15.71108 ? 617  ASN   B C    1 
ATOM   4110 O  O    . ASN   B 1 183 ? -27.50900 42.76200 51.13600 1.000 15.89902 ? 617  ASN   B O    1 
ATOM   4111 C  CB   . ASN   B 1 183 ? -29.24500 41.38200 48.73200 1.000 13.81951 ? 617  ASN   B CB   1 
ATOM   4112 C  CG   . ASN   B 1 183 ? -30.72700 41.73300 48.73100 1.000 20.59308 ? 617  ASN   B CG   1 
ATOM   4113 O  OD1  . ASN   B 1 183 ? -31.58300 40.85100 48.67800 1.000 15.42191 ? 617  ASN   B OD1  1 
ATOM   4114 N  ND2  . ASN   B 1 183 ? -31.03400 43.02300 48.79700 1.000 20.39399 ? 617  ASN   B ND2  1 
ATOM   4115 N  N    . GLY   B 1 184 ? -29.69100 42.61100 51.65400 1.000 11.16159 ? 618  GLY   B N    1 
ATOM   4116 C  CA   . GLY   B 1 184 ? -29.62000 43.78000 52.51300 1.000 13.84058 ? 618  GLY   B CA   1 
ATOM   4117 C  C    . GLY   B 1 184 ? -28.75800 43.55700 53.74100 1.000 14.46016 ? 618  GLY   B C    1 
ATOM   4118 O  O    . GLY   B 1 184 ? -27.95100 44.41500 54.10600 1.000 12.14193 ? 618  GLY   B O    1 
ATOM   4119 N  N    . THR   B 1 185 ? -28.91800 42.40600 54.39600 1.000 13.05941 ? 619  THR   B N    1 
ATOM   4120 C  CA   . THR   B 1 185 ? -28.13200 42.12000 55.59100 1.000 10.97250 ? 619  THR   B CA   1 
ATOM   4121 C  C    . THR   B 1 185 ? -26.65000 41.98300 55.25400 1.000 13.30473 ? 619  THR   B C    1 
ATOM   4122 O  O    . THR   B 1 185 ? -25.79000 42.53500 55.95200 1.000 12.20726 ? 619  THR   B O    1 
ATOM   4123 C  CB   . THR   B 1 185 ? -28.65800 40.85500 56.26700 1.000 8.70567  ? 619  THR   B CB   1 
ATOM   4124 O  OG1  . THR   B 1 185 ? -30.08900 40.89700 56.29500 1.000 10.48192 ? 619  THR   B OG1  1 
ATOM   4125 C  CG2  . THR   B 1 185 ? -28.15500 40.76600 57.68900 1.000 12.44347 ? 619  THR   B CG2  1 
ATOM   4126 N  N    . GLN   B 1 186 ? -26.33100 41.26000 54.17600 1.000 14.39309 ? 620  GLN   B N    1 
ATOM   4127 C  CA   . GLN   B 1 186 ? -24.93100 41.09400 53.78600 1.000 10.28347 ? 620  GLN   B CA   1 
ATOM   4128 C  C    . GLN   B 1 186 ? -24.28000 42.43100 53.46000 1.000 14.20299 ? 620  GLN   B C    1 
ATOM   4129 O  O    . GLN   B 1 186 ? -23.13900 42.68900 53.86400 1.000 18.80243 ? 620  GLN   B O    1 
ATOM   4130 C  CB   . GLN   B 1 186 ? -24.81700 40.15000 52.59000 1.000 12.45944 ? 620  GLN   B CB   1 
ATOM   4131 C  CG   . GLN   B 1 186 ? -23.53900 40.34800 51.78800 1.000 12.25721 ? 620  GLN   B CG   1 
ATOM   4132 C  CD   . GLN   B 1 186 ? -23.33400 39.29100 50.71700 1.000 14.63175 ? 620  GLN   B CD   1 
ATOM   4133 O  OE1  . GLN   B 1 186 ? -23.62700 38.11700 50.92600 1.000 12.18918 ? 620  GLN   B OE1  1 
ATOM   4134 N  NE2  . GLN   B 1 186 ? -22.81900 39.70500 49.56700 1.000 11.95063 ? 620  GLN   B NE2  1 
ATOM   4135 N  N    . HIS   B 1 187 ? -24.98900 43.29800 52.73400 1.000 10.80769 ? 621  HIS   B N    1 
ATOM   4136 C  CA   . HIS   B 1 187 ? -24.41300 44.59100 52.37600 1.000 11.38022 ? 621  HIS   B CA   1 
ATOM   4137 C  C    . HIS   B 1 187 ? -24.21800 45.47000 53.60200 1.000 12.46256 ? 621  HIS   B C    1 
ATOM   4138 O  O    . HIS   B 1 187 ? -23.20200 46.16400 53.71800 1.000 17.01996 ? 621  HIS   B O    1 
ATOM   4139 C  CB   . HIS   B 1 187 ? -25.29400 45.30000 51.34800 1.000 15.77998 ? 621  HIS   B CB   1 
ATOM   4140 C  CG   . HIS   B 1 187 ? -25.26700 44.67200 49.98800 1.000 14.48025 ? 621  HIS   B CG   1 
ATOM   4141 N  ND1  . HIS   B 1 187 ? -26.34400 44.71000 49.13000 1.000 15.41180 ? 621  HIS   B ND1  1 
ATOM   4142 C  CD2  . HIS   B 1 187 ? -24.29000 43.99800 49.33500 1.000 14.16355 ? 621  HIS   B CD2  1 
ATOM   4143 C  CE1  . HIS   B 1 187 ? -26.03500 44.08400 48.00800 1.000 15.25514 ? 621  HIS   B CE1  1 
ATOM   4144 N  NE2  . HIS   B 1 187 ? -24.79400 43.64200 48.10600 1.000 12.19088 ? 621  HIS   B NE2  1 
ATOM   4145 N  N    . ILE   B 1 188 ? -25.17000 45.44200 54.53500 1.000 15.74624 ? 622  ILE   B N    1 
ATOM   4146 C  CA   . ILE   B 1 188 ? -25.11100 46.35200 55.67600 1.000 19.96905 ? 622  ILE   B CA   1 
ATOM   4147 C  C    . ILE   B 1 188 ? -23.91500 46.04100 56.57000 1.000 11.07841 ? 622  ILE   B C    1 
ATOM   4148 O  O    . ILE   B 1 188 ? -23.29200 46.95700 57.11900 1.000 11.47822 ? 622  ILE   B O    1 
ATOM   4149 C  CB   . ILE   B 1 188 ? -26.44600 46.30400 56.44400 1.000 16.46516 ? 622  ILE   B CB   1 
ATOM   4150 C  CG1  . ILE   B 1 188 ? -27.49200 47.15700 55.72100 1.000 12.54866 ? 622  ILE   B CG1  1 
ATOM   4151 C  CG2  . ILE   B 1 188 ? -26.27200 46.76300 57.88500 1.000 14.14732 ? 622  ILE   B CG2  1 
ATOM   4152 C  CD1  . ILE   B 1 188 ? -28.91100 46.93900 56.19800 1.000 11.86521 ? 622  ILE   B CD1  1 
ATOM   4153 N  N    . PHE   B 1 189 ? -23.54700 44.76600 56.70300 1.000 10.92200 ? 623  PHE   B N    1 
ATOM   4154 C  CA   . PHE   B 1 189 ? -22.45300 44.35900 57.57900 1.000 16.84380 ? 623  PHE   B CA   1 
ATOM   4155 C  C    . PHE   B 1 189 ? -21.22500 43.87500 56.80900 1.000 18.81624 ? 623  PHE   B C    1 
ATOM   4156 O  O    . PHE   B 1 189 ? -20.36300 43.21100 57.39400 1.000 15.61419 ? 623  PHE   B O    1 
ATOM   4157 C  CB   . PHE   B 1 189 ? -22.91700 43.26200 58.54100 1.000 10.67194 ? 623  PHE   B CB   1 
ATOM   4158 C  CG   . PHE   B 1 189 ? -24.12600 43.63200 59.35500 1.000 21.09123 ? 623  PHE   B CG   1 
ATOM   4159 C  CD1  . PHE   B 1 189 ? -24.02400 44.53800 60.39700 1.000 11.55106 ? 623  PHE   B CD1  1 
ATOM   4160 C  CD2  . PHE   B 1 189 ? -25.35900 43.05400 59.09100 1.000 17.15085 ? 623  PHE   B CD2  1 
ATOM   4161 C  CE1  . PHE   B 1 189 ? -25.12700 44.87600 61.14700 1.000 13.43713 ? 623  PHE   B CE1  1 
ATOM   4162 C  CE2  . PHE   B 1 189 ? -26.46800 43.38400 59.84000 1.000 14.73087 ? 623  PHE   B CE2  1 
ATOM   4163 C  CZ   . PHE   B 1 189 ? -26.35300 44.29800 60.87200 1.000 14.38541 ? 623  PHE   B CZ   1 
ATOM   4164 N  N    . GLU   B 1 190 ? -21.12200 44.19500 55.51500 1.000 14.88229 ? 624  GLU   B N    1 
ATOM   4165 C  CA   . GLU   B 1 190 ? -20.08900 43.58200 54.68200 1.000 17.29314 ? 624  GLU   B CA   1 
ATOM   4166 C  C    . GLU   B 1 190 ? -18.68400 43.93000 55.17000 1.000 19.50831 ? 624  GLU   B C    1 
ATOM   4167 O  O    . GLU   B 1 190 ? -17.78300 43.08400 55.14100 1.000 16.89416 ? 624  GLU   B O    1 
ATOM   4168 C  CB   . GLU   B 1 190 ? -20.27600 43.99800 53.22500 1.000 14.71792 ? 624  GLU   B CB   1 
ATOM   4169 C  CG   . GLU   B 1 190 ? -19.91100 42.89900 52.23700 1.000 25.37595 ? 624  GLU   B CG   1 
ATOM   4170 C  CD   . GLU   B 1 190 ? -20.61300 43.05300 50.89900 1.000 23.81640 ? 624  GLU   B CD   1 
ATOM   4171 O  OE1  . GLU   B 1 190 ? -21.22800 44.11700 50.66800 1.000 21.63747 ? 624  GLU   B OE1  1 
ATOM   4172 O  OE2  . GLU   B 1 190 ? -20.55900 42.10500 50.08700 1.000 19.56563 ? 624  GLU   B OE2  1 
ATOM   4173 N  N    . GLU   B 1 191 ? -18.47700 45.16300 55.62500 1.000 18.06303 ? 625  GLU   B N    1 
ATOM   4174 C  CA   . GLU   B 1 191 ? -17.19500 45.57700 56.18100 1.000 18.62687 ? 625  GLU   B CA   1 
ATOM   4175 C  C    . GLU   B 1 191 ? -17.15900 45.48100 57.70100 1.000 17.57751 ? 625  GLU   B C    1 
ATOM   4176 O  O    . GLU   B 1 191 ? -16.21300 45.97300 58.32400 1.000 20.97862 ? 625  GLU   B O    1 
ATOM   4177 C  CB   . GLU   B 1 191 ? -16.87100 47.00600 55.73300 1.000 15.07628 ? 625  GLU   B CB   1 
ATOM   4178 C  CG   . GLU   B 1 191 ? -16.67300 47.13600 54.23200 1.000 28.90415 ? 625  GLU   B CG   1 
ATOM   4179 C  CD   . GLU   B 1 191 ? -16.77300 48.56900 53.74100 1.000 34.08930 ? 625  GLU   B CD   1 
ATOM   4180 O  OE1  . GLU   B 1 191 ? -15.89200 49.39000 54.07800 1.000 25.55926 ? 625  GLU   B OE1  1 
ATOM   4181 O  OE2  . GLU   B 1 191 ? -17.74500 48.87500 53.01900 1.000 35.76352 ? 625  GLU   B OE2  1 
ATOM   4182 N  N    . ASP   B 1 192 ? -18.15000 44.83400 58.30500 1.000 19.96752 ? 626  ASP   B N    1 
ATOM   4183 C  CA   . ASP   B 1 192 ? -18.34100 44.83200 59.74800 1.000 17.48982 ? 626  ASP   B CA   1 
ATOM   4184 C  C    . ASP   B 1 192 ? -17.91200 43.48300 60.31100 1.000 17.46411 ? 626  ASP   B C    1 
ATOM   4185 O  O    . ASP   B 1 192 ? -18.47600 42.44700 59.94200 1.000 17.98112 ? 626  ASP   B O    1 
ATOM   4186 C  CB   . ASP   B 1 192 ? -19.80300 45.12800 60.08500 1.000 17.20648 ? 626  ASP   B CB   1 
ATOM   4187 C  CG   . ASP   B 1 192 ? -20.03900 45.31100 61.57100 1.000 25.80307 ? 626  ASP   B CG   1 
ATOM   4188 O  OD1  . ASP   B 1 192 ? -20.10200 44.29900 62.29800 1.000 18.49471 ? 626  ASP   B OD1  1 
ATOM   4189 O  OD2  . ASP   B 1 192 ? -20.15400 46.47100 62.01500 1.000 26.55748 ? 626  ASP   B OD2  1 
ATOM   4190 N  N    . ASP   B 1 193 ? -16.92100 43.49700 61.20300 1.000 13.48628 ? 627  ASP   B N    1 
ATOM   4191 C  CA   . ASP   B 1 193 ? -16.45800 42.27800 61.85400 1.000 14.54503 ? 627  ASP   B CA   1 
ATOM   4192 C  C    . ASP   B 1 193 ? -17.12200 42.03200 63.20300 1.000 17.75676 ? 627  ASP   B C    1 
ATOM   4193 O  O    . ASP   B 1 193 ? -16.78500 41.05200 63.87400 1.000 14.84181 ? 627  ASP   B O    1 
ATOM   4194 C  CB   . ASP   B 1 193 ? -14.92900 42.30300 62.01900 1.000 20.36133 ? 627  ASP   B CB   1 
ATOM   4195 C  CG   . ASP   B 1 193 ? -14.43500 43.47100 62.86900 1.000 18.04991 ? 627  ASP   B CG   1 
ATOM   4196 O  OD1  . ASP   B 1 193 ? -15.23700 44.09500 63.59400 1.000 24.25179 ? 627  ASP   B OD1  1 
ATOM   4197 O  OD2  . ASP   B 1 193 ? -13.22300 43.76600 62.80800 1.000 19.80094 ? 627  ASP   B OD2  1 
ATOM   4198 N  N    . SER   B 1 194 ? -18.04000 42.89500 63.62600 1.000 12.69688 ? 628  SER   B N    1 
ATOM   4199 C  CA   . SER   B 1 194 ? -18.77300 42.66000 64.86200 1.000 20.11125 ? 628  SER   B CA   1 
ATOM   4200 C  C    . SER   B 1 194 ? -20.06900 41.89500 64.63600 1.000 20.64543 ? 628  SER   B C    1 
ATOM   4201 O  O    . SER   B 1 194 ? -20.69900 41.46800 65.60900 1.000 14.57246 ? 628  SER   B O    1 
ATOM   4202 C  CB   . SER   B 1 194 ? -19.07500 43.98700 65.57000 1.000 14.26891 ? 628  SER   B CB   1 
ATOM   4203 O  OG   . SER   B 1 194 ? -20.15200 44.66900 64.95600 1.000 13.01552 ? 628  SER   B OG   1 
ATOM   4204 N  N    . VAL   B 1 195 ? -20.47700 41.70500 63.38300 1.000 16.08489 ? 629  VAL   B N    1 
ATOM   4205 C  CA   . VAL   B 1 195 ? -21.69300 40.97800 63.04400 1.000 10.89341 ? 629  VAL   B CA   1 
ATOM   4206 C  C    . VAL   B 1 195 ? -21.33500 39.93800 61.98600 1.000 21.51454 ? 629  VAL   B C    1 
ATOM   4207 O  O    . VAL   B 1 195 ? -20.97700 40.29100 60.85600 1.000 13.57485 ? 629  VAL   B O    1 
ATOM   4208 C  CB   . VAL   B 1 195 ? -22.80800 41.91000 62.54600 1.000 22.10709 ? 629  VAL   B CB   1 
ATOM   4209 C  CG1  . VAL   B 1 195 ? -24.05700 41.11300 62.20100 1.000 13.44564 ? 629  VAL   B CG1  1 
ATOM   4210 C  CG2  . VAL   B 1 195 ? -23.12200 42.97900 63.58900 1.000 12.86479 ? 629  VAL   B CG2  1 
ATOM   4211 N  N    . LEU   B 1 196 ? -21.43000 38.66300 62.35000 1.000 12.68653 ? 630  LEU   B N    1 
ATOM   4212 C  CA   . LEU   B 1 196 ? -21.17900 37.56300 61.43000 1.000 10.88228 ? 630  LEU   B CA   1 
ATOM   4213 C  C    . LEU   B 1 196 ? -22.47100 37.22500 60.69300 1.000 13.74845 ? 630  LEU   B C    1 
ATOM   4214 O  O    . LEU   B 1 196 ? -23.47400 36.87700 61.32500 1.000 11.38326 ? 630  LEU   B O    1 
ATOM   4215 C  CB   . LEU   B 1 196 ? -20.65900 36.34300 62.18800 1.000 11.16747 ? 630  LEU   B CB   1 
ATOM   4216 C  CG   . LEU   B 1 196 ? -20.35000 35.09300 61.35700 1.000 18.28458 ? 630  LEU   B CG   1 
ATOM   4217 C  CD1  . LEU   B 1 196 ? -19.23500 35.36700 60.36800 1.000 11.96764 ? 630  LEU   B CD1  1 
ATOM   4218 C  CD2  . LEU   B 1 196 ? -19.99500 33.91400 62.25100 1.000 18.71821 ? 630  LEU   B CD2  1 
ATOM   4219 N  N    . TYR   B 1 197 ? -22.44600 37.32300 59.36500 1.000 10.41709 ? 631  TYR   B N    1 
ATOM   4220 C  CA   . TYR   B 1 197 ? -23.60300 37.01200 58.53400 1.000 10.00737 ? 631  TYR   B CA   1 
ATOM   4221 C  C    . TYR   B 1 197 ? -23.38800 35.66900 57.84900 1.000 18.82180 ? 631  TYR   B C    1 
ATOM   4222 O  O    . TYR   B 1 197 ? -22.39900 35.48500 57.13200 1.000 15.62750 ? 631  TYR   B O    1 
ATOM   4223 C  CB   . TYR   B 1 197 ? -23.84900 38.10400 57.49300 1.000 9.98728  ? 631  TYR   B CB   1 
ATOM   4224 C  CG   . TYR   B 1 197 ? -25.08700 37.85000 56.66800 1.000 9.60890  ? 631  TYR   B CG   1 
ATOM   4225 C  CD1  . TYR   B 1 197 ? -26.33100 37.76500 57.26900 1.000 10.51358 ? 631  TYR   B CD1  1 
ATOM   4226 C  CD2  . TYR   B 1 197 ? -25.01300 37.68500 55.29500 1.000 17.11083 ? 631  TYR   B CD2  1 
ATOM   4227 C  CE1  . TYR   B 1 197 ? -27.47000 37.52600 56.52900 1.000 10.68091 ? 631  TYR   B CE1  1 
ATOM   4228 C  CE2  . TYR   B 1 197 ? -26.14700 37.44200 54.54400 1.000 11.00698 ? 631  TYR   B CE2  1 
ATOM   4229 C  CZ   . TYR   B 1 197 ? -27.37500 37.36800 55.17000 1.000 14.57958 ? 631  TYR   B CZ   1 
ATOM   4230 O  OH   . TYR   B 1 197 ? -28.51400 37.13000 54.43600 1.000 13.18688 ? 631  TYR   B OH   1 
ATOM   4231 N  N    . ILE   B 1 198 ? -24.31500 34.74000 58.06400 1.000 15.21600 ? 632  ILE   B N    1 
ATOM   4232 C  CA   . ILE   B 1 198 ? -24.28100 33.42200 57.44500 1.000 10.09766 ? 632  ILE   B CA   1 
ATOM   4233 C  C    . ILE   B 1 198 ? -25.63500 33.18300 56.79400 1.000 14.72863 ? 632  ILE   B C    1 
ATOM   4234 O  O    . ILE   B 1 198 ? -26.66400 33.21300 57.47500 1.000 15.82875 ? 632  ILE   B O    1 
ATOM   4235 C  CB   . ILE   B 1 198 ? -23.97100 32.31300 58.46400 1.000 10.93232 ? 632  ILE   B CB   1 
ATOM   4236 C  CG1  . ILE   B 1 198 ? -22.59600 32.53300 59.09500 1.000 12.71047 ? 632  ILE   B CG1  1 
ATOM   4237 C  CG2  . ILE   B 1 198 ? -24.05000 30.95000 57.80200 1.000 10.56135 ? 632  ILE   B CG2  1 
ATOM   4238 C  CD1  . ILE   B 1 198 ? -22.29000 31.58000 60.23100 1.000 17.89171 ? 632  ILE   B CD1  1 
ATOM   4239 N  N    . SER   B 1 199 ? -25.63900 32.93200 55.48700 1.000 13.82897 ? 633  SER   B N    1 
ATOM   4240 C  CA   . SER   B 1 199 ? -26.88200 32.73300 54.75400 1.000 14.19593 ? 633  SER   B CA   1 
ATOM   4241 C  C    . SER   B 1 199 ? -26.82000 31.45900 53.92800 1.000 11.87853 ? 633  SER   B C    1 
ATOM   4242 O  O    . SER   B 1 199 ? -25.87900 31.26000 53.15300 1.000 14.16371 ? 633  SER   B O    1 
ATOM   4243 C  CB   . SER   B 1 199 ? -27.18000 33.92200 53.83900 1.000 11.99965 ? 633  SER   B CB   1 
ATOM   4244 O  OG   . SER   B 1 199 ? -28.30200 33.64700 53.01700 1.000 11.32340 ? 633  SER   B OG   1 
ATOM   4245 N  N    . LEU   B 1 200 ? -27.82600 30.60800 54.09500 1.000 15.13025 ? 634  LEU   B N    1 
ATOM   4246 C  CA   . LEU   B 1 200 ? -28.10100 29.49900 53.19300 1.000 13.96296 ? 634  LEU   B CA   1 
ATOM   4247 C  C    . LEU   B 1 200 ? -29.23000 29.91400 52.26200 1.000 15.73252 ? 634  LEU   B C    1 
ATOM   4248 O  O    . LEU   B 1 200 ? -30.22200 30.50000 52.70800 1.000 13.86562 ? 634  LEU   B O    1 
ATOM   4249 C  CB   . LEU   B 1 200 ? -28.49700 28.23900 53.96600 1.000 10.06051 ? 634  LEU   B CB   1 
ATOM   4250 C  CG   . LEU   B 1 200 ? -27.56300 27.74800 55.07400 1.000 10.34753 ? 634  LEU   B CG   1 
ATOM   4251 C  CD1  . LEU   B 1 200 ? -27.87500 28.40800 56.41100 1.000 10.01241 ? 634  LEU   B CD1  1 
ATOM   4252 C  CD2  . LEU   B 1 200 ? -27.64900 26.23100 55.18600 1.000 12.82201 ? 634  LEU   B CD2  1 
ATOM   4253 N  N    . HIS   B 1 201 ? -29.07900 29.62600 50.96800 1.000 11.31724 ? 635  HIS   B N    1 
ATOM   4254 C  CA   . HIS   B 1 201 ? -30.05000 30.16300 50.02500 1.000 11.66437 ? 635  HIS   B CA   1 
ATOM   4255 C  C    . HIS   B 1 201 ? -29.92700 29.47600 48.67100 1.000 10.96569 ? 635  HIS   B C    1 
ATOM   4256 O  O    . HIS   B 1 201 ? -28.82300 29.18100 48.21000 1.000 10.61777 ? 635  HIS   B O    1 
ATOM   4257 C  CB   . HIS   B 1 201 ? -29.86900 31.68000 49.86300 1.000 9.62449  ? 635  HIS   B CB   1 
ATOM   4258 C  CG   . HIS   B 1 201 ? -28.46300 32.08600 49.55700 1.000 17.86408 ? 635  HIS   B CG   1 
ATOM   4259 N  ND1  . HIS   B 1 201 ? -27.52600 32.32900 50.54000 1.000 11.45992 ? 635  HIS   B ND1  1 
ATOM   4260 C  CD2  . HIS   B 1 201 ? -27.82700 32.27600 48.37700 1.000 13.85112 ? 635  HIS   B CD2  1 
ATOM   4261 C  CE1  . HIS   B 1 201 ? -26.37700 32.65600 49.97900 1.000 15.93099 ? 635  HIS   B CE1  1 
ATOM   4262 N  NE2  . HIS   B 1 201 ? -26.53200 32.63100 48.66700 1.000 13.21343 ? 635  HIS   B NE2  1 
ATOM   4263 N  N    . ARG   B 1 202 ? -31.07500 29.23600 48.04400 1.000 10.13433 ? 636  ARG   B N    1 
ATOM   4264 C  CA   . ARG   B 1 202 ? -31.09700 28.82500 46.64800 1.000 11.32637 ? 636  ARG   B CA   1 
ATOM   4265 C  C    . ARG   B 1 202 ? -30.48300 29.91800 45.78100 1.000 12.60040 ? 636  ARG   B C    1 
ATOM   4266 O  O    . ARG   B 1 202 ? -30.78700 31.10200 45.94200 1.000 20.07637 ? 636  ARG   B O    1 
ATOM   4267 C  CB   . ARG   B 1 202 ? -32.53400 28.53200 46.21500 1.000 10.42189 ? 636  ARG   B CB   1 
ATOM   4268 C  CG   . ARG   B 1 202 ? -32.65900 28.05900 44.77900 1.000 12.34047 ? 636  ARG   B CG   1 
ATOM   4269 C  CD   . ARG   B 1 202 ? -33.98900 27.37500 44.52200 1.000 10.89015 ? 636  ARG   B CD   1 
ATOM   4270 N  NE   . ARG   B 1 202 ? -33.98400 26.69500 43.23200 1.000 11.39220 ? 636  ARG   B NE   1 
ATOM   4271 C  CZ   . ARG   B 1 202 ? -35.00400 26.01100 42.73100 1.000 11.59736 ? 636  ARG   B CZ   1 
ATOM   4272 N  NH1  . ARG   B 1 202 ? -36.14800 25.89500 43.38500 1.000 11.37261 ? 636  ARG   B NH1  1 
ATOM   4273 N  NH2  . ARG   B 1 202 ? -34.87300 25.43200 41.54100 1.000 22.38985 ? 636  ARG   B NH2  1 
ATOM   4274 N  N    . TYR   B 1 203 ? -29.61300 29.52200 44.85500 1.000 12.88767 ? 637  TYR   B N    1 
ATOM   4275 C  CA   . TYR   B 1 203 ? -28.82700 30.49900 44.11300 1.000 11.43726 ? 637  TYR   B CA   1 
ATOM   4276 C  C    . TYR   B 1 203 ? -28.96400 30.31600 42.60500 1.000 12.60183 ? 637  TYR   B C    1 
ATOM   4277 O  O    . TYR   B 1 203 ? -29.28300 31.27300 41.89000 1.000 15.07476 ? 637  TYR   B O    1 
ATOM   4278 C  CB   . TYR   B 1 203 ? -27.36200 30.40700 44.55100 1.000 11.75148 ? 637  TYR   B CB   1 
ATOM   4279 C  CG   . TYR   B 1 203 ? -26.41200 31.30900 43.80100 1.000 12.18821 ? 637  TYR   B CG   1 
ATOM   4280 C  CD1  . TYR   B 1 203 ? -26.59000 32.68600 43.78900 1.000 13.51767 ? 637  TYR   B CD1  1 
ATOM   4281 C  CD2  . TYR   B 1 203 ? -25.31400 30.78300 43.12700 1.000 18.42343 ? 637  TYR   B CD2  1 
ATOM   4282 C  CE1  . TYR   B 1 203 ? -25.71200 33.51200 43.10700 1.000 14.11661 ? 637  TYR   B CE1  1 
ATOM   4283 C  CE2  . TYR   B 1 203 ? -24.42900 31.60100 42.45000 1.000 13.36527 ? 637  TYR   B CE2  1 
ATOM   4284 C  CZ   . TYR   B 1 203 ? -24.63600 32.96200 42.43800 1.000 14.86946 ? 637  TYR   B CZ   1 
ATOM   4285 O  OH   . TYR   B 1 203 ? -23.76600 33.77700 41.75500 1.000 13.79571 ? 637  TYR   B OH   1 
ATOM   4286 N  N    . GLU   B 1 204 ? -28.71900 29.09800 42.11600 1.000 12.29662 ? 638  GLU   B N    1 
ATOM   4287 C  CA   . GLU   B 1 204 ? -28.85500 28.77000 40.69400 1.000 14.36095 ? 638  GLU   B CA   1 
ATOM   4288 C  C    . GLU   B 1 204 ? -28.06600 29.73900 39.81600 1.000 19.38298 ? 638  GLU   B C    1 
ATOM   4289 O  O    . GLU   B 1 204 ? -28.53200 30.17500 38.76100 1.000 18.07226 ? 638  GLU   B O    1 
ATOM   4290 C  CB   . GLU   B 1 204 ? -30.32700 28.73300 40.27400 1.000 14.95756 ? 638  GLU   B CB   1 
ATOM   4291 C  CG   . GLU   B 1 204 ? -31.23900 27.91400 41.18000 1.000 12.19675 ? 638  GLU   B CG   1 
ATOM   4292 C  CD   . GLU   B 1 204 ? -30.98100 26.41500 41.10500 1.000 15.53547 ? 638  GLU   B CD   1 
ATOM   4293 O  OE1  . GLU   B 1 204 ? -30.02800 25.98500 40.42000 1.000 19.58140 ? 638  GLU   B OE1  1 
ATOM   4294 O  OE2  . GLU   B 1 204 ? -31.74000 25.66000 41.74000 1.000 15.54896 ? 638  GLU   B OE2  1 
ATOM   4295 N  N    . ASP   B 1 205 ? -26.85700 30.07300 40.26500 1.000 18.42321 ? 639  ASP   B N    1 
ATOM   4296 C  CA   . ASP   B 1 205 ? -25.95700 30.99200 39.56800 1.000 13.90171 ? 639  ASP   B CA   1 
ATOM   4297 C  C    . ASP   B 1 205 ? -26.67300 32.26700 39.13000 1.000 20.59402 ? 639  ASP   B C    1 
ATOM   4298 O  O    . ASP   B 1 205 ? -26.62000 32.67800 37.96900 1.000 44.41357 ? 639  ASP   B O    1 
ATOM   4299 C  CB   . ASP   B 1 205 ? -25.27400 30.30200 38.38800 1.000 22.03012 ? 639  ASP   B CB   1 
ATOM   4300 C  CG   . ASP   B 1 205 ? -24.00700 29.57200 38.80600 1.000 38.19208 ? 639  ASP   B CG   1 
ATOM   4301 O  OD1  . ASP   B 1 205 ? -24.09600 28.40200 39.23000 1.000 32.19563 ? 639  ASP   B OD1  1 
ATOM   4302 O  OD2  . ASP   B 1 205 ? -22.91800 30.17900 38.74400 1.000 35.85295 ? 639  ASP   B OD2  1 
ATOM   4303 N  N    . GLY   B 1 206 ? -27.35300 32.90000 40.08600 1.000 16.66677 ? 640  GLY   B N    1 
ATOM   4304 C  CA   . GLY   B 1 206 ? -27.96500 34.19200 39.86900 1.000 20.51775 ? 640  GLY   B CA   1 
ATOM   4305 C  C    . GLY   B 1 206 ? -29.36300 34.17100 39.28600 1.000 21.56368 ? 640  GLY   B C    1 
ATOM   4306 O  O    . GLY   B 1 206 ? -29.98100 35.23700 39.17200 1.000 29.89478 ? 640  GLY   B O    1 
ATOM   4307 N  N    . ALA   B 1 207 ? -29.88400 33.00600 38.90900 1.000 22.29119 ? 641  ALA   B N    1 
ATOM   4308 C  CA   . ALA   B 1 207 ? -31.21300 32.94700 38.31500 1.000 15.09021 ? 641  ALA   B CA   1 
ATOM   4309 C  C    . ALA   B 1 207 ? -32.32800 33.01300 39.34600 1.000 16.96958 ? 641  ALA   B C    1 
ATOM   4310 O  O    . ALA   B 1 207 ? -33.48600 33.22800 38.97200 1.000 28.49665 ? 641  ALA   B O    1 
ATOM   4311 C  CB   . ALA   B 1 207 ? -31.36700 31.67200 37.48200 1.000 18.95981 ? 641  ALA   B CB   1 
ATOM   4312 N  N    . PHE   B 1 208 ? -32.01900 32.83100 40.62200 1.000 15.31245 ? 642  PHE   B N    1 
ATOM   4313 C  CA   . PHE   B 1 208 ? -33.02300 32.86600 41.67200 1.000 19.71820 ? 642  PHE   B CA   1 
ATOM   4314 C  C    . PHE   B 1 208 ? -32.95200 34.20000 42.40100 1.000 18.21523 ? 642  PHE   B C    1 
ATOM   4315 O  O    . PHE   B 1 208 ? -31.86000 34.69700 42.68700 1.000 22.39456 ? 642  PHE   B O    1 
ATOM   4316 C  CB   . PHE   B 1 208 ? -32.82200 31.71100 42.65400 1.000 12.85067 ? 642  PHE   B CB   1 
ATOM   4317 C  CG   . PHE   B 1 208 ? -34.08500 31.27100 43.33100 1.000 14.66513 ? 642  PHE   B CG   1 
ATOM   4318 C  CD1  . PHE   B 1 208 ? -35.04200 30.55300 42.63300 1.000 14.83752 ? 642  PHE   B CD1  1 
ATOM   4319 C  CD2  . PHE   B 1 208 ? -34.31900 31.57900 44.65800 1.000 10.09111 ? 642  PHE   B CD2  1 
ATOM   4320 C  CE1  . PHE   B 1 208 ? -36.20700 30.14500 43.24700 1.000 19.55824 ? 642  PHE   B CE1  1 
ATOM   4321 C  CE2  . PHE   B 1 208 ? -35.48100 31.17200 45.27700 1.000 11.47028 ? 642  PHE   B CE2  1 
ATOM   4322 C  CZ   . PHE   B 1 208 ? -36.42700 30.45500 44.56900 1.000 11.07870 ? 642  PHE   B CZ   1 
ATOM   4323 N  N    . PHE   B 1 209 ? -34.12100 34.77500 42.68200 1.000 20.95426 ? 643  PHE   B N    1 
ATOM   4324 C  CA   . PHE   B 1 209 ? -34.22000 36.05900 43.36600 1.000 18.83316 ? 643  PHE   B CA   1 
ATOM   4325 C  C    . PHE   B 1 209 ? -33.33100 36.05900 44.60900 1.000 15.15980 ? 643  PHE   B C    1 
ATOM   4326 O  O    . PHE   B 1 209 ? -33.21200 35.02500 45.27800 1.000 19.77745 ? 643  PHE   B O    1 
ATOM   4327 C  CB   . PHE   B 1 209 ? -35.68000 36.33400 43.75100 1.000 13.65439 ? 643  PHE   B CB   1 
ATOM   4328 C  CG   . PHE   B 1 209 ? -35.89100 37.65700 44.42300 1.000 15.24872 ? 643  PHE   B CG   1 
ATOM   4329 C  CD1  . PHE   B 1 209 ? -35.78300 37.77600 45.80100 1.000 14.87375 ? 643  PHE   B CD1  1 
ATOM   4330 C  CD2  . PHE   B 1 209 ? -36.18200 38.78500 43.67900 1.000 10.51078 ? 643  PHE   B CD2  1 
ATOM   4331 C  CE1  . PHE   B 1 209 ? -35.95100 38.99200 46.42000 1.000 12.64105 ? 643  PHE   B CE1  1 
ATOM   4332 C  CE2  . PHE   B 1 209 ? -36.35900 40.00600 44.29500 1.000 15.50838 ? 643  PHE   B CE2  1 
ATOM   4333 C  CZ   . PHE   B 1 209 ? -36.24800 40.10800 45.67100 1.000 18.98621 ? 643  PHE   B CZ   1 
ATOM   4334 N  N    . PRO   B 1 210 ? -32.68700 37.19000 44.95600 1.000 17.73816 ? 644  PRO   B N    1 
ATOM   4335 C  CA   . PRO   B 1 210 ? -32.71700 38.51900 44.31700 1.000 15.64039 ? 644  PRO   B CA   1 
ATOM   4336 C  C    . PRO   B 1 210 ? -31.83600 38.65400 43.07600 1.000 12.92488 ? 644  PRO   B C    1 
ATOM   4337 O  O    . PRO   B 1 210 ? -31.52100 39.76500 42.65500 1.000 17.03786 ? 644  PRO   B O    1 
ATOM   4338 C  CB   . PRO   B 1 210 ? -32.23700 39.43800 45.44500 1.000 13.61320 ? 644  PRO   B CB   1 
ATOM   4339 C  CG   . PRO   B 1 210 ? -31.28500 38.59000 46.21100 1.000 10.81079 ? 644  PRO   B CG   1 
ATOM   4340 C  CD   . PRO   B 1 210 ? -31.88700 37.21000 46.19300 1.000 11.13101 ? 644  PRO   B CD   1 
ATOM   4341 N  N    . ASN   B 1 211 ? -31.41900 37.53300 42.48900 1.000 11.14573 ? 645  ASN   B N    1 
ATOM   4342 C  CA   . ASN   B 1 211 ? -30.86100 37.49300 41.13500 1.000 18.88021 ? 645  ASN   B CA   1 
ATOM   4343 C  C    . ASN   B 1 211 ? -29.50200 38.19100 41.03600 1.000 18.26839 ? 645  ASN   B C    1 
ATOM   4344 O  O    . ASN   B 1 211 ? -29.21200 38.86700 40.04800 1.000 17.08348 ? 645  ASN   B O    1 
ATOM   4345 C  CB   . ASN   B 1 211 ? -31.84300 38.08900 40.12000 1.000 18.68625 ? 645  ASN   B CB   1 
ATOM   4346 C  CG   . ASN   B 1 211 ? -33.25200 37.55400 40.28800 1.000 19.92130 ? 645  ASN   B CG   1 
ATOM   4347 O  OD1  . ASN   B 1 211 ? -34.16900 38.29100 40.65400 1.000 23.25175 ? 645  ASN   B OD1  1 
ATOM   4348 N  ND2  . ASN   B 1 211 ? -33.43300 36.26700 40.01900 1.000 23.98955 ? 645  ASN   B ND2  1 
ATOM   4349 N  N    . SER   B 1 212 ? -28.64700 38.00100 42.03900 1.000 17.24142 ? 646  SER   B N    1 
ATOM   4350 C  CA   . SER   B 1 212 ? -27.37100 38.70100 42.09000 1.000 13.78689 ? 646  SER   B CA   1 
ATOM   4351 C  C    . SER   B 1 212 ? -26.25600 37.74800 42.49400 1.000 12.66165 ? 646  SER   B C    1 
ATOM   4352 O  O    . SER   B 1 212 ? -26.45100 36.86900 43.33700 1.000 12.21128 ? 646  SER   B O    1 
ATOM   4353 C  CB   . SER   B 1 212 ? -27.43100 39.87800 43.07200 1.000 12.27879 ? 646  SER   B CB   1 
ATOM   4354 O  OG   . SER   B 1 212 ? -26.21600 40.60000 43.08500 1.000 12.81481 ? 646  SER   B OG   1 
ATOM   4355 N  N    . GLU   B 1 213 ? -25.08100 37.93400 41.89400 1.000 13.36796 ? 647  GLU   B N    1 
ATOM   4356 C  CA   . GLU   B 1 213 ? -23.92800 37.11500 42.24500 1.000 17.03073 ? 647  GLU   B CA   1 
ATOM   4357 C  C    . GLU   B 1 213 ? -23.33200 37.48900 43.59600 1.000 13.41685 ? 647  GLU   B C    1 
ATOM   4358 O  O    . GLU   B 1 213 ? -22.40900 36.80800 44.05500 1.000 13.62747 ? 647  GLU   B O    1 
ATOM   4359 C  CB   . GLU   B 1 213 ? -22.86200 37.21300 41.15100 1.000 21.62580 ? 647  GLU   B CB   1 
ATOM   4360 C  CG   . GLU   B 1 213 ? -23.37000 36.79600 39.77700 1.000 16.72637 ? 647  GLU   B CG   1 
ATOM   4361 C  CD   . GLU   B 1 213 ? -22.25700 36.62700 38.76200 1.000 20.10684 ? 647  GLU   B CD   1 
ATOM   4362 O  OE1  . GLU   B 1 213 ? -21.47300 35.66000 38.88500 1.000 23.49644 ? 647  GLU   B OE1  1 
ATOM   4363 O  OE2  . GLU   B 1 213 ? -22.16900 37.46500 37.84000 1.000 25.21008 ? 647  GLU   B OE2  1 
ATOM   4364 N  N    . ASP   B 1 214 ? -23.83800 38.54600 44.23700 1.000 14.23288 ? 648  ASP   B N    1 
ATOM   4365 C  CA   . ASP   B 1 214 ? -23.45100 38.85200 45.61100 1.000 12.77689 ? 648  ASP   B CA   1 
ATOM   4366 C  C    . ASP   B 1 214 ? -23.68600 37.66700 46.53500 1.000 16.49097 ? 648  ASP   B C    1 
ATOM   4367 O  O    . ASP   B 1 214 ? -22.96800 37.49600 47.52600 1.000 15.90443 ? 648  ASP   B O    1 
ATOM   4368 C  CB   . ASP   B 1 214 ? -24.23600 40.06600 46.11600 1.000 12.41734 ? 648  ASP   B CB   1 
ATOM   4369 C  CG   . ASP   B 1 214 ? -23.90500 41.33300 45.35200 1.000 16.51888 ? 648  ASP   B CG   1 
ATOM   4370 O  OD1  . ASP   B 1 214 ? -22.89800 41.32800 44.61000 1.000 14.71726 ? 648  ASP   B OD1  1 
ATOM   4371 O  OD2  . ASP   B 1 214 ? -24.65000 42.32800 45.49200 1.000 16.10712 ? 648  ASP   B OD2  1 
ATOM   4372 N  N    . ALA   B 1 215 ? -24.68600 36.84500 46.23200 1.000 12.66778 ? 649  ALA   B N    1 
ATOM   4373 C  CA   . ALA   B 1 215 ? -25.01200 35.68400 47.04600 1.000 14.02561 ? 649  ALA   B CA   1 
ATOM   4374 C  C    . ALA   B 1 215 ? -24.04300 34.51900 46.86700 1.000 11.95951 ? 649  ALA   B C    1 
ATOM   4375 O  O    . ALA   B 1 215 ? -24.23700 33.48300 47.50800 1.000 13.23016 ? 649  ALA   B O    1 
ATOM   4376 C  CB   . ALA   B 1 215 ? -26.43200 35.21900 46.72400 1.000 11.08473 ? 649  ALA   B CB   1 
ATOM   4377 N  N    . ASN   B 1 216 ? -23.01900 34.63100 46.03000 1.000 12.64301 ? 650  ASN   B N    1 
ATOM   4378 C  CA   . ASN   B 1 216 ? -22.20600 33.44900 45.80100 1.000 15.38260 ? 650  ASN   B CA   1 
ATOM   4379 C  C    . ASN   B 1 216 ? -21.19700 33.25700 46.93000 1.000 16.07752 ? 650  ASN   B C    1 
ATOM   4380 O  O    . ASN   B 1 216 ? -20.88700 34.17800 47.68900 1.000 14.94168 ? 650  ASN   B O    1 
ATOM   4381 C  CB   . ASN   B 1 216 ? -21.48800 33.52500 44.45600 1.000 14.03023 ? 650  ASN   B CB   1 
ATOM   4382 C  CG   . ASN   B 1 216 ? -21.30000 32.16000 43.83000 1.000 14.27003 ? 650  ASN   B CG   1 
ATOM   4383 O  OD1  . ASN   B 1 216 ? -21.50900 31.13600 44.48200 1.000 14.04118 ? 650  ASN   B OD1  1 
ATOM   4384 N  ND2  . ASN   B 1 216 ? -20.90800 32.13400 42.56000 1.000 20.81841 ? 650  ASN   B ND2  1 
ATOM   4385 N  N    . TYR   B 1 217 ? -20.68000 32.02800 47.02000 1.000 18.40107 ? 651  TYR   B N    1 
ATOM   4386 C  CA   . TYR   B 1 217 ? -19.79800 31.63700 48.11400 1.000 17.01018 ? 651  TYR   B CA   1 
ATOM   4387 C  C    . TYR   B 1 217 ? -18.51700 32.46000 48.16800 1.000 18.87543 ? 651  TYR   B C    1 
ATOM   4388 O  O    . TYR   B 1 217 ? -17.90300 32.55400 49.23500 1.000 14.49888 ? 651  TYR   B O    1 
ATOM   4389 C  CB   . TYR   B 1 217 ? -19.44700 30.14800 47.99700 1.000 14.22678 ? 651  TYR   B CB   1 
ATOM   4390 C  CG   . TYR   B 1 217 ? -18.70000 29.76900 46.72800 1.000 15.02758 ? 651  TYR   B CG   1 
ATOM   4391 C  CD1  . TYR   B 1 217 ? -17.31800 29.90400 46.64400 1.000 15.83714 ? 651  TYR   B CD1  1 
ATOM   4392 C  CD2  . TYR   B 1 217 ? -19.37400 29.25900 45.62500 1.000 16.04421 ? 651  TYR   B CD2  1 
ATOM   4393 C  CE1  . TYR   B 1 217 ? -16.63500 29.56500 45.49500 1.000 16.64440 ? 651  TYR   B CE1  1 
ATOM   4394 C  CE2  . TYR   B 1 217 ? -18.69700 28.91100 44.46800 1.000 16.81402 ? 651  TYR   B CE2  1 
ATOM   4395 C  CZ   . TYR   B 1 217 ? -17.32700 29.06700 44.40900 1.000 16.63145 ? 651  TYR   B CZ   1 
ATOM   4396 O  OH   . TYR   B 1 217 ? -16.64600 28.71900 43.26400 1.000 17.96585 ? 651  TYR   B OH   1 
ATOM   4397 N  N    . ASP   B 1 218 ? -18.09500 33.04500 47.04900 1.000 15.11216 ? 652  ASP   B N    1 
ATOM   4398 C  CA   . ASP   B 1 218 ? -16.83100 33.76700 46.98800 1.000 15.84900 ? 652  ASP   B CA   1 
ATOM   4399 C  C    . ASP   B 1 218 ? -16.92900 35.18500 47.52700 1.000 16.15258 ? 652  ASP   B C    1 
ATOM   4400 O  O    . ASP   B 1 218 ? -15.92500 35.90500 47.50900 1.000 16.08850 ? 652  ASP   B O    1 
ATOM   4401 C  CB   . ASP   B 1 218 ? -16.31600 33.81400 45.55000 1.000 19.68535 ? 652  ASP   B CB   1 
ATOM   4402 C  CG   . ASP   B 1 218 ? -17.11600 34.75900 44.68000 1.000 19.80084 ? 652  ASP   B CG   1 
ATOM   4403 O  OD1  . ASP   B 1 218 ? -18.36400 34.70300 44.73100 1.000 19.24692 ? 652  ASP   B OD1  1 
ATOM   4404 O  OD2  . ASP   B 1 218 ? -16.49200 35.56600 43.95600 1.000 19.60334 ? 652  ASP   B OD2  1 
ATOM   4405 N  N    . LYS   B 1 219 ? -18.10500 35.61100 47.98300 1.000 15.50188 ? 653  LYS   B N    1 
ATOM   4406 C  CA   . LYS   B 1 219 ? -18.26000 36.92000 48.61800 1.000 14.98737 ? 653  LYS   B CA   1 
ATOM   4407 C  C    . LYS   B 1 219 ? -18.11000 36.70300 50.11900 1.000 14.03011 ? 653  LYS   B C    1 
ATOM   4408 O  O    . LYS   B 1 219 ? -19.07000 36.40500 50.82900 1.000 13.30975 ? 653  LYS   B O    1 
ATOM   4409 C  CB   . LYS   B 1 219 ? -19.60000 37.54300 48.24900 1.000 13.73600 ? 653  LYS   B CB   1 
ATOM   4410 C  CG   . LYS   B 1 219 ? -19.93700 37.45000 46.76100 1.000 14.36507 ? 653  LYS   B CG   1 
ATOM   4411 C  CD   . LYS   B 1 219 ? -18.91000 38.16700 45.90200 1.000 14.91266 ? 653  LYS   B CD   1 
ATOM   4412 C  CE   . LYS   B 1 219 ? -19.40100 38.33100 44.47200 1.000 18.80114 ? 653  LYS   B CE   1 
ATOM   4413 N  NZ   . LYS   B 1 219 ? -19.53100 37.04200 43.73900 1.000 17.08401 ? 653  LYS   B NZ   1 
ATOM   4414 N  N    . VAL   B 1 220 ? -16.87300 36.82800 50.60700 1.000 14.65079 ? 654  VAL   B N    1 
ATOM   4415 C  CA   . VAL   B 1 220 ? -16.55300 36.49500 51.99000 1.000 14.51865 ? 654  VAL   B CA   1 
ATOM   4416 C  C    . VAL   B 1 220 ? -16.44900 37.72300 52.87800 1.000 14.42323 ? 654  VAL   B C    1 
ATOM   4417 O  O    . VAL   B 1 220 ? -16.13900 37.58700 54.07100 1.000 14.37565 ? 654  VAL   B O    1 
ATOM   4418 C  CB   . VAL   B 1 220 ? -15.25200 35.67200 52.06900 1.000 15.62177 ? 654  VAL   B CB   1 
ATOM   4419 C  CG1  . VAL   B 1 220 ? -15.40000 34.35900 51.30900 1.000 15.43975 ? 654  VAL   B CG1  1 
ATOM   4420 C  CG2  . VAL   B 1 220 ? -14.07100 36.47400 51.52000 1.000 16.25678 ? 654  VAL   B CG2  1 
ATOM   4421 N  N    . GLY   B 1 221 ? -16.69200 38.91100 52.34400 1.000 17.22483 ? 655  GLY   B N    1 
ATOM   4422 C  CA   . GLY   B 1 221 ? -16.58600 40.14300 53.09900 1.000 15.40294 ? 655  GLY   B CA   1 
ATOM   4423 C  C    . GLY   B 1 221 ? -15.59700 41.11300 52.47500 1.000 21.56266 ? 655  GLY   B C    1 
ATOM   4424 O  O    . GLY   B 1 221 ? -14.89400 40.80700 51.51400 1.000 18.21261 ? 655  GLY   B O    1 
ATOM   4425 N  N    . LEU   B 1 222 ? -15.56300 42.31000 53.06000 1.000 20.63704 ? 656  LEU   B N    1 
ATOM   4426 C  CA   . LEU   B 1 222 ? -14.70900 43.39700 52.60000 1.000 23.03044 ? 656  LEU   B CA   1 
ATOM   4427 C  C    . LEU   B 1 222 ? -13.92700 43.96400 53.77400 1.000 19.14317 ? 656  LEU   B C    1 
ATOM   4428 O  O    . LEU   B 1 222 ? -14.48400 44.15300 54.85800 1.000 21.90896 ? 656  LEU   B O    1 
ATOM   4429 C  CB   . LEU   B 1 222 ? -15.52200 44.53200 51.96200 1.000 25.43133 ? 656  LEU   B CB   1 
ATOM   4430 C  CG   . LEU   B 1 222 ? -16.74500 44.23900 51.09300 1.000 19.51983 ? 656  LEU   B CG   1 
ATOM   4431 C  CD1  . LEU   B 1 222 ? -17.60100 45.49200 50.98800 1.000 30.94612 ? 656  LEU   B CD1  1 
ATOM   4432 C  CD2  . LEU   B 1 222 ? -16.34100 43.75900 49.71000 1.000 29.65898 ? 656  LEU   B CD2  1 
ATOM   4433 N  N    . GLY   B 1 223 ? -12.64500 44.24600 53.54800 1.000 20.93292 ? 657  GLY   B N    1 
ATOM   4434 C  CA   . GLY   B 1 223 ? -11.84500 44.95000 54.54200 1.000 18.26530 ? 657  GLY   B CA   1 
ATOM   4435 C  C    . GLY   B 1 223 ? -11.80400 44.22700 55.87400 1.000 27.25448 ? 657  GLY   B C    1 
ATOM   4436 O  O    . GLY   B 1 223 ? -11.55800 43.01700 55.94400 1.000 23.71457 ? 657  GLY   B O    1 
ATOM   4437 N  N    . LYS   B 1 224 ? -12.04900 44.98000 56.95200 1.000 25.50678 ? 658  LYS   B N    1 
ATOM   4438 C  CA   . LYS   B 1 224 ? -12.10500 44.38700 58.28600 1.000 21.90338 ? 658  LYS   B CA   1 
ATOM   4439 C  C    . LYS   B 1 224 ? -13.15500 43.28900 58.36800 1.000 29.76503 ? 658  LYS   B C    1 
ATOM   4440 O  O    . LYS   B 1 224 ? -13.03600 42.37800 59.19500 1.000 28.85354 ? 658  LYS   B O    1 
ATOM   4441 C  CB   . LYS   B 1 224 ? -12.39600 45.46400 59.33200 1.000 21.25768 ? 658  LYS   B CB   1 
ATOM   4442 C  CG   . LYS   B 1 224 ? -11.23400 46.40200 59.62400 1.000 30.71598 ? 658  LYS   B CG   1 
ATOM   4443 C  CD   . LYS   B 1 224 ? -11.70800 47.61300 60.41900 1.000 43.68132 ? 658  LYS   B CD   1 
ATOM   4444 C  CE   . LYS   B 1 224 ? -10.55000 48.34400 61.08000 1.000 46.59785 ? 658  LYS   B CE   1 
ATOM   4445 N  NZ   . LYS   B 1 224 ? -9.94500  47.52600 62.16900 1.000 20.40694 ? 658  LYS   B NZ   1 
ATOM   4446 N  N    . GLY   B 1 225 ? -14.18300 43.35600 57.52700 1.000 21.39720 ? 659  GLY   B N    1 
ATOM   4447 C  CA   . GLY   B 1 225 ? -15.22700 42.35700 57.47500 1.000 20.84779 ? 659  GLY   B CA   1 
ATOM   4448 C  C    . GLY   B 1 225 ? -14.90100 41.11300 56.68800 1.000 15.08009 ? 659  GLY   B C    1 
ATOM   4449 O  O    . GLY   B 1 225 ? -15.72200 40.19600 56.64800 1.000 16.51707 ? 659  GLY   B O    1 
ATOM   4450 N  N    . ARG   B 1 226 ? -13.72900 41.05100 56.06200 1.000 19.47014 ? 660  ARG   B N    1 
ATOM   4451 C  CA   . ARG   B 1 226 ? -13.33700 39.86100 55.31500 1.000 20.40259 ? 660  ARG   B CA   1 
ATOM   4452 C  C    . ARG   B 1 226 ? -13.33100 38.63600 56.22100 1.000 18.83523 ? 660  ARG   B C    1 
ATOM   4453 O  O    . ARG   B 1 226 ? -12.75500 38.65100 57.31400 1.000 24.17758 ? 660  ARG   B O    1 
ATOM   4454 C  CB   . ARG   B 1 226 ? -11.96100 40.06500 54.68000 1.000 20.38152 ? 660  ARG   B CB   1 
ATOM   4455 C  CG   . ARG   B 1 226 ? -12.01200 40.68900 53.29900 1.000 20.69264 ? 660  ARG   B CG   1 
ATOM   4456 C  CD   . ARG   B 1 226 ? -10.65500 41.20600 52.87000 1.000 28.55413 ? 660  ARG   B CD   1 
ATOM   4457 N  NE   . ARG   B 1 226 ? -9.56200  40.37700 53.36300 1.000 49.32519 ? 660  ARG   B NE   1 
ATOM   4458 C  CZ   . ARG   B 1 226 ? -9.23800  39.19000 52.86800 1.000 42.78018 ? 660  ARG   B CZ   1 
ATOM   4459 N  NH1  . ARG   B 1 226 ? -9.93900  38.63200 51.89400 1.000 31.18425 ? 660  ARG   B NH1  1 
ATOM   4460 N  NH2  . ARG   B 1 226 ? -8.18700  38.54400 53.36600 1.000 20.50671 ? 660  ARG   B NH2  1 
ATOM   4461 N  N    . GLY   B 1 227 ? -13.97500 37.57000 55.75800 1.000 15.50271 ? 661  GLY   B N    1 
ATOM   4462 C  CA   . GLY   B 1 227 ? -14.16400 36.37800 56.54300 1.000 15.25590 ? 661  GLY   B CA   1 
ATOM   4463 C  C    . GLY   B 1 227 ? -15.45200 36.34700 57.33400 1.000 14.31374 ? 661  GLY   B C    1 
ATOM   4464 O  O    . GLY   B 1 227 ? -15.86300 35.27100 57.78000 1.000 14.05463 ? 661  GLY   B O    1 
ATOM   4465 N  N    . TYR   B 1 228 ? -16.11000 37.49400 57.50600 1.000 13.87008 ? 662  TYR   B N    1 
ATOM   4466 C  CA   . TYR   B 1 228 ? -17.30600 37.59500 58.33200 1.000 13.06713 ? 662  TYR   B CA   1 
ATOM   4467 C  C    . TYR   B 1 228 ? -18.58500 37.64400 57.50300 1.000 14.10719 ? 662  TYR   B C    1 
ATOM   4468 O  O    . TYR   B 1 228 ? -19.59100 38.21100 57.94400 1.000 12.88658 ? 662  TYR   B O    1 
ATOM   4469 C  CB   . TYR   B 1 228 ? -17.20200 38.81000 59.25200 1.000 23.36484 ? 662  TYR   B CB   1 
ATOM   4470 C  CG   . TYR   B 1 228 ? -16.10700 38.68200 60.29300 1.000 21.20752 ? 662  TYR   B CG   1 
ATOM   4471 C  CD1  . TYR   B 1 228 ? -14.80200 39.05800 60.00900 1.000 18.39077 ? 662  TYR   B CD1  1 
ATOM   4472 C  CD2  . TYR   B 1 228 ? -16.37900 38.17500 61.55800 1.000 27.69289 ? 662  TYR   B CD2  1 
ATOM   4473 C  CE1  . TYR   B 1 228 ? -13.79800 38.94000 60.96100 1.000 24.80362 ? 662  TYR   B CE1  1 
ATOM   4474 C  CE2  . TYR   B 1 228 ? -15.38100 38.05500 62.51700 1.000 18.88939 ? 662  TYR   B CE2  1 
ATOM   4475 C  CZ   . TYR   B 1 228 ? -14.09700 38.43900 62.21000 1.000 18.60538 ? 662  TYR   B CZ   1 
ATOM   4476 O  OH   . TYR   B 1 228 ? -13.10600 38.31800 63.15600 1.000 42.46952 ? 662  TYR   B OH   1 
ATOM   4477 N  N    . ASN   B 1 229 ? -18.56200 37.04600 56.31300 1.000 12.59186 ? 663  ASN   B N    1 
ATOM   4478 C  CA   . ASN   B 1 229 ? -19.74300 36.89800 55.46300 1.000 12.08156 ? 663  ASN   B CA   1 
ATOM   4479 C  C    . ASN   B 1 229 ? -19.66000 35.51700 54.82500 1.000 14.37684 ? 663  ASN   B C    1 
ATOM   4480 O  O    . ASN   B 1 229 ? -18.76700 35.26400 54.01200 1.000 15.83103 ? 663  ASN   B O    1 
ATOM   4481 C  CB   . ASN   B 1 229 ? -19.80300 37.99700 54.40100 1.000 12.23146 ? 663  ASN   B CB   1 
ATOM   4482 C  CG   . ASN   B 1 229 ? -21.16700 38.10900 53.75000 1.000 11.66812 ? 663  ASN   B CG   1 
ATOM   4483 O  OD1  . ASN   B 1 229 ? -22.05500 38.78600 54.26200 1.000 16.28666 ? 663  ASN   B OD1  1 
ATOM   4484 N  ND2  . ASN   B 1 229 ? -21.33700 37.45200 52.61000 1.000 11.78061 ? 663  ASN   B ND2  1 
ATOM   4485 N  N    . VAL   B 1 230 ? -20.57300 34.62400 55.19500 1.000 18.92705 ? 664  VAL   B N    1 
ATOM   4486 C  CA   . VAL   B 1 230 ? -20.53300 33.22700 54.76900 1.000 19.27577 ? 664  VAL   B CA   1 
ATOM   4487 C  C    . VAL   B 1 230 ? -21.78600 32.94200 53.95000 1.000 12.64901 ? 664  VAL   B C    1 
ATOM   4488 O  O    . VAL   B 1 230 ? -22.89200 32.86500 54.49800 1.000 10.99443 ? 664  VAL   B O    1 
ATOM   4489 C  CB   . VAL   B 1 230 ? -20.42400 32.26900 55.96300 1.000 12.02147 ? 664  VAL   B CB   1 
ATOM   4490 C  CG1  . VAL   B 1 230 ? -20.30000 30.83700 55.48000 1.000 12.36111 ? 664  VAL   B CG1  1 
ATOM   4491 C  CG2  . VAL   B 1 230 ? -19.24000 32.64800 56.84500 1.000 12.47888 ? 664  VAL   B CG2  1 
ATOM   4492 N  N    . ASN   B 1 231 ? -21.61600 32.78000 52.64200 1.000 11.83673 ? 665  ASN   B N    1 
ATOM   4493 C  CA   . ASN   B 1 231 ? -22.71200 32.45300 51.73800 1.000 14.27880 ? 665  ASN   B CA   1 
ATOM   4494 C  C    . ASN   B 1 231 ? -22.65500 30.97600 51.37600 1.000 17.72305 ? 665  ASN   B C    1 
ATOM   4495 O  O    . ASN   B 1 231 ? -21.61400 30.48000 50.93200 1.000 12.45124 ? 665  ASN   B O    1 
ATOM   4496 C  CB   . ASN   B 1 231 ? -22.65100 33.30100 50.46800 1.000 11.72921 ? 665  ASN   B CB   1 
ATOM   4497 C  CG   . ASN   B 1 231 ? -23.29200 34.65700 50.64400 1.000 11.33018 ? 665  ASN   B CG   1 
ATOM   4498 O  OD1  . ASN   B 1 231 ? -24.26600 34.80300 51.37700 1.000 10.77779 ? 665  ASN   B OD1  1 
ATOM   4499 N  ND2  . ASN   B 1 231 ? -22.75200 35.65700 49.96400 1.000 11.68728 ? 665  ASN   B ND2  1 
ATOM   4500 N  N    . ILE   B 1 232 ? -23.77400 30.28400 51.55700 1.000 11.54597 ? 666  ILE   B N    1 
ATOM   4501 C  CA   . ILE   B 1 232 ? -23.88900 28.86900 51.21800 1.000 12.51299 ? 666  ILE   B CA   1 
ATOM   4502 C  C    . ILE   B 1 232 ? -24.88700 28.73800 50.07000 1.000 19.03975 ? 666  ILE   B C    1 
ATOM   4503 O  O    . ILE   B 1 232 ? -26.09200 28.56600 50.30900 1.000 16.26671 ? 666  ILE   B O    1 
ATOM   4504 C  CB   . ILE   B 1 232 ? -24.30200 28.04900 52.44900 1.000 11.58081 ? 666  ILE   B CB   1 
ATOM   4505 C  CG1  . ILE   B 1 232 ? -23.32100 28.30900 53.59900 1.000 11.75706 ? 666  ILE   B CG1  1 
ATOM   4506 C  CG2  . ILE   B 1 232 ? -24.36000 26.57100 52.12600 1.000 11.99556 ? 666  ILE   B CG2  1 
ATOM   4507 C  CD1  . ILE   B 1 232 ? -23.64500 27.55800 54.87600 1.000 11.69995 ? 666  ILE   B CD1  1 
ATOM   4508 N  N    . PRO   B 1 233 ? -24.43900 28.84100 48.81300 1.000 11.96885 ? 667  PRO   B N    1 
ATOM   4509 C  CA   . PRO   B 1 233 ? -25.38300 28.85900 47.68400 1.000 14.60738 ? 667  PRO   B CA   1 
ATOM   4510 C  C    . PRO   B 1 233 ? -25.78800 27.47000 47.21100 1.000 12.73081 ? 667  PRO   B C    1 
ATOM   4511 O  O    . PRO   B 1 233 ? -24.93100 26.62500 46.95200 1.000 12.69447 ? 667  PRO   B O    1 
ATOM   4512 C  CB   . PRO   B 1 233 ? -24.60000 29.59200 46.59300 1.000 17.94994 ? 667  PRO   B CB   1 
ATOM   4513 C  CG   . PRO   B 1 233 ? -23.17000 29.23100 46.87300 1.000 13.12914 ? 667  PRO   B CG   1 
ATOM   4514 C  CD   . PRO   B 1 233 ? -23.05500 29.11400 48.38500 1.000 12.57017 ? 667  PRO   B CD   1 
ATOM   4515 N  N    . TRP   B 1 234 ? -27.08900 27.23000 47.07700 1.000 13.24494 ? 668  TRP   B N    1 
ATOM   4516 C  CA   . TRP   B 1 234 ? -27.56400 25.97800 46.50900 1.000 12.08610 ? 668  TRP   B CA   1 
ATOM   4517 C  C    . TRP   B 1 234 ? -27.74700 26.12500 45.00500 1.000 13.92658 ? 668  TRP   B C    1 
ATOM   4518 O  O    . TRP   B 1 234 ? -28.25300 27.14100 44.52200 1.000 12.20272 ? 668  TRP   B O    1 
ATOM   4519 C  CB   . TRP   B 1 234 ? -28.88200 25.53900 47.15500 1.000 17.34410 ? 668  TRP   B CB   1 
ATOM   4520 C  CG   . TRP   B 1 234 ? -28.81700 25.36300 48.64700 1.000 21.12215 ? 668  TRP   B CG   1 
ATOM   4521 C  CD1  . TRP   B 1 234 ? -29.60100 25.98300 49.58000 1.000 10.96528 ? 668  TRP   B CD1  1 
ATOM   4522 C  CD2  . TRP   B 1 234 ? -27.91500 24.51900 49.37800 1.000 15.92399 ? 668  TRP   B CD2  1 
ATOM   4523 N  NE1  . TRP   B 1 234 ? -29.24600 25.57400 50.84600 1.000 15.27807 ? 668  TRP   B NE1  1 
ATOM   4524 C  CE2  . TRP   B 1 234 ? -28.21300 24.67700 50.74900 1.000 15.69983 ? 668  TRP   B CE2  1 
ATOM   4525 C  CE3  . TRP   B 1 234 ? -26.88500 23.64600 49.00700 1.000 15.71090 ? 668  TRP   B CE3  1 
ATOM   4526 C  CZ2  . TRP   B 1 234 ? -27.51900 23.99400 51.74800 1.000 12.88775 ? 668  TRP   B CZ2  1 
ATOM   4527 C  CZ3  . TRP   B 1 234 ? -26.19700 22.97000 49.99900 1.000 12.84763 ? 668  TRP   B CZ3  1 
ATOM   4528 C  CH2  . TRP   B 1 234 ? -26.51600 23.14700 51.35300 1.000 14.06345 ? 668  TRP   B CH2  1 
ATOM   4529 N  N    . ASN   B 1 235 ? -27.30600 25.11500 44.26800 1.000 17.08368 ? 669  ASN   B N    1 
ATOM   4530 C  CA   . ASN   B 1 235 ? -27.55800 25.00600 42.84000 1.000 13.30736 ? 669  ASN   B CA   1 
ATOM   4531 C  C    . ASN   B 1 235 ? -28.18400 23.64900 42.56800 1.000 14.70133 ? 669  ASN   B C    1 
ATOM   4532 O  O    . ASN   B 1 235 ? -27.96600 22.69400 43.31600 1.000 15.06248 ? 669  ASN   B O    1 
ATOM   4533 C  CB   . ASN   B 1 235 ? -26.27300 25.15500 42.01100 1.000 13.93826 ? 669  ASN   B CB   1 
ATOM   4534 C  CG   . ASN   B 1 235 ? -25.56700 26.47800 42.24800 1.000 13.78781 ? 669  ASN   B CG   1 
ATOM   4535 O  OD1  . ASN   B 1 235 ? -26.02600 27.51900 41.79500 1.000 13.54671 ? 669  ASN   B OD1  1 
ATOM   4536 N  ND2  . ASN   B 1 235 ? -24.43300 26.43800 42.94700 1.000 15.85047 ? 669  ASN   B ND2  1 
ATOM   4537 N  N    . GLY   B 1 236 ? -28.96500 23.56600 41.49400 1.000 13.73299 ? 670  GLY   B N    1 
ATOM   4538 C  CA   . GLY   B 1 236 ? -29.52600 22.29800 41.07800 1.000 20.20456 ? 670  GLY   B CA   1 
ATOM   4539 C  C    . GLY   B 1 236 ? -30.84800 21.92200 41.70500 1.000 22.33278 ? 670  GLY   B C    1 
ATOM   4540 O  O    . GLY   B 1 236 ? -31.13100 20.72900 41.85900 1.000 17.63589 ? 670  GLY   B O    1 
ATOM   4541 N  N    . GLY   B 1 237 ? -31.67100 22.89500 42.07600 1.000 14.32497 ? 671  GLY   B N    1 
ATOM   4542 C  CA   . GLY   B 1 237 ? -33.02500 22.60200 42.49500 1.000 19.78649 ? 671  GLY   B CA   1 
ATOM   4543 C  C    . GLY   B 1 237 ? -33.19700 22.10500 43.91900 1.000 18.27436 ? 671  GLY   B C    1 
ATOM   4544 O  O    . GLY   B 1 237 ? -32.48200 22.52100 44.83000 1.000 16.52411 ? 671  GLY   B O    1 
ATOM   4545 N  N    . LYS   B 1 238 ? -34.13600 21.17500 44.09200 1.000 22.32855 ? 672  LYS   B N    1 
ATOM   4546 C  CA   . LYS   B 1 238 ? -34.69900 20.86500 45.40100 1.000 27.37873 ? 672  LYS   B CA   1 
ATOM   4547 C  C    . LYS   B 1 238 ? -33.64000 20.40100 46.39400 1.000 16.48308 ? 672  LYS   B C    1 
ATOM   4548 O  O    . LYS   B 1 238 ? -32.86300 19.48700 46.10900 1.000 18.79123 ? 672  LYS   B O    1 
ATOM   4549 C  CB   . LYS   B 1 238 ? -35.77700 19.79200 45.24400 1.000 13.19664 ? 672  LYS   B CB   1 
ATOM   4550 C  CG   . LYS   B 1 238 ? -36.79600 19.75400 46.36400 1.000 21.12515 ? 672  LYS   B CG   1 
ATOM   4551 C  CD   . LYS   B 1 238 ? -37.89000 18.73500 46.07700 1.000 34.84549 ? 672  LYS   B CD   1 
ATOM   4552 C  CE   . LYS   B 1 238 ? -37.29400 17.35300 45.84600 1.000 38.45817 ? 672  LYS   B CE   1 
ATOM   4553 N  NZ   . LYS   B 1 238 ? -38.30500 16.27900 46.05600 1.000 36.65416 ? 672  LYS   B NZ   1 
ATOM   4554 N  N    . MET   B 1 239 ? -33.62300 21.03700 47.56600 1.000 12.41531 ? 673  MET   B N    1 
ATOM   4555 C  CA   . MET   B 1 239 ? -32.78400 20.64700 48.69000 1.000 12.52356 ? 673  MET   B CA   1 
ATOM   4556 C  C    . MET   B 1 239 ? -33.66200 20.43300 49.91600 1.000 16.33974 ? 673  MET   B C    1 
ATOM   4557 O  O    . MET   B 1 239 ? -34.75100 20.99900 50.02600 1.000 19.62378 ? 673  MET   B O    1 
ATOM   4558 C  CB   . MET   B 1 239 ? -31.71800 21.70900 49.00600 1.000 15.22792 ? 673  MET   B CB   1 
ATOM   4559 C  CG   . MET   B 1 239 ? -30.80000 22.04900 47.84300 1.000 12.36572 ? 673  MET   B CG   1 
ATOM   4560 S  SD   . MET   B 1 239 ? -29.68300 20.69500 47.43700 1.000 13.22653 ? 673  MET   B SD   1 
ATOM   4561 C  CE   . MET   B 1 239 ? -29.10000 21.25100 45.84600 1.000 14.60807 ? 673  MET   B CE   1 
ATOM   4562 N  N    . GLY   B 1 240 ? -33.17500 19.62300 50.85000 1.000 16.59216 ? 674  GLY   B N    1 
ATOM   4563 C  CA   . GLY   B 1 240 ? -33.95100 19.32900 52.03900 1.000 12.72850 ? 674  GLY   B CA   1 
ATOM   4564 C  C    . GLY   B 1 240 ? -33.14800 19.23700 53.32000 1.000 16.16615 ? 674  GLY   B C    1 
ATOM   4565 O  O    . GLY   B 1 240 ? -32.05200 19.79800 53.41900 1.000 16.56305 ? 674  GLY   B O    1 
ATOM   4566 N  N    . ASP   B 1 241 ? -33.70100 18.52800 54.30900 1.000 18.67953 ? 675  ASP   B N    1 
ATOM   4567 C  CA   . ASP   B 1 241 ? -33.03800 18.34000 55.60000 1.000 13.27860 ? 675  ASP   B CA   1 
ATOM   4568 C  C    . ASP   B 1 241 ? -31.59300 17.86700 55.49500 1.000 17.78898 ? 675  ASP   B C    1 
ATOM   4569 O  O    . ASP   B 1 241 ? -30.73900 18.43800 56.19100 1.000 17.52477 ? 675  ASP   B O    1 
ATOM   4570 C  CB   . ASP   B 1 241 ? -33.84200 17.35500 56.46000 1.000 13.81375 ? 675  ASP   B CB   1 
ATOM   4571 C  CG   . ASP   B 1 241 ? -35.15100 17.93100 56.95000 1.000 15.28536 ? 675  ASP   B CG   1 
ATOM   4572 O  OD1  . ASP   B 1 241 ? -35.43800 19.11600 56.66400 1.000 15.09670 ? 675  ASP   B OD1  1 
ATOM   4573 O  OD2  . ASP   B 1 241 ? -35.89000 17.19000 57.63300 1.000 17.43434 ? 675  ASP   B OD2  1 
ATOM   4574 N  N    . PRO   B 1 242 ? -31.24400 16.85000 54.68800 1.000 15.12470 ? 676  PRO   B N    1 
ATOM   4575 C  CA   . PRO   B 1 242 ? -29.84600 16.37700 54.69900 1.000 15.29391 ? 676  PRO   B CA   1 
ATOM   4576 C  C    . PRO   B 1 242 ? -28.85000 17.44000 54.28200 1.000 17.44416 ? 676  PRO   B C    1 
ATOM   4577 O  O    . PRO   B 1 242 ? -27.79400 17.57900 54.91100 1.000 18.57426 ? 676  PRO   B O    1 
ATOM   4578 C  CB   . PRO   B 1 242 ? -29.86200 15.20200 53.71000 1.000 15.57065 ? 676  PRO   B CB   1 
ATOM   4579 C  CG   . PRO   B 1 242 ? -31.28600 14.77900 53.64000 1.000 15.60620 ? 676  PRO   B CG   1 
ATOM   4580 C  CD   . PRO   B 1 242 ? -32.07500 16.04200 53.77900 1.000 14.70814 ? 676  PRO   B CD   1 
ATOM   4581 N  N    . GLU   B 1 243 ? -29.16600 18.20200 53.23500 1.000 17.25742 ? 677  GLU   B N    1 
ATOM   4582 C  CA   . GLU   B 1 243 ? -28.27400 19.26500 52.79300 1.000 13.62910 ? 677  GLU   B CA   1 
ATOM   4583 C  C    . GLU   B 1 243 ? -28.11700 20.33700 53.86700 1.000 15.38120 ? 677  GLU   B C    1 
ATOM   4584 O  O    . GLU   B 1 243 ? -27.01500 20.85500 54.08600 1.000 13.11808 ? 677  GLU   B O    1 
ATOM   4585 C  CB   . GLU   B 1 243 ? -28.80500 19.87200 51.49600 1.000 15.36952 ? 677  GLU   B CB   1 
ATOM   4586 C  CG   . GLU   B 1 243 ? -28.73300 18.94000 50.29100 1.000 13.88047 ? 677  GLU   B CG   1 
ATOM   4587 C  CD   . GLU   B 1 243 ? -29.71000 17.78400 50.35000 1.000 21.70921 ? 677  GLU   B CD   1 
ATOM   4588 O  OE1  . GLU   B 1 243 ? -30.81500 17.96400 50.90300 1.000 22.41248 ? 677  GLU   B OE1  1 
ATOM   4589 O  OE2  . GLU   B 1 243 ? -29.36600 16.69200 49.84800 1.000 14.97656 ? 677  GLU   B OE2  1 
ATOM   4590 N  N    . TYR   B 1 244 ? -29.20600 20.67800 54.55200 1.000 17.03829 ? 678  TYR   B N    1 
ATOM   4591 C  CA   . TYR   B 1 244 ? -29.13000 21.72300 55.56300 1.000 12.15664 ? 678  TYR   B CA   1 
ATOM   4592 C  C    . TYR   B 1 244 ? -28.45000 21.22700 56.83400 1.000 13.35749 ? 678  TYR   B C    1 
ATOM   4593 O  O    . TYR   B 1 244 ? -27.66000 21.96100 57.43800 1.000 20.53887 ? 678  TYR   B O    1 
ATOM   4594 C  CB   . TYR   B 1 244 ? -30.52800 22.27000 55.85000 1.000 11.69119 ? 678  TYR   B CB   1 
ATOM   4595 C  CG   . TYR   B 1 244 ? -30.93900 23.31100 54.83500 1.000 14.94964 ? 678  TYR   B CG   1 
ATOM   4596 C  CD1  . TYR   B 1 244 ? -31.28900 22.94500 53.53900 1.000 17.39203 ? 678  TYR   B CD1  1 
ATOM   4597 C  CD2  . TYR   B 1 244 ? -30.95600 24.66100 55.16300 1.000 12.55650 ? 678  TYR   B CD2  1 
ATOM   4598 C  CE1  . TYR   B 1 244 ? -31.64900 23.89100 52.59700 1.000 10.93040 ? 678  TYR   B CE1  1 
ATOM   4599 C  CE2  . TYR   B 1 244 ? -31.31700 25.61400 54.22800 1.000 11.73020 ? 678  TYR   B CE2  1 
ATOM   4600 C  CZ   . TYR   B 1 244 ? -31.65900 25.22000 52.94400 1.000 13.67238 ? 678  TYR   B CZ   1 
ATOM   4601 O  OH   . TYR   B 1 244 ? -32.01600 26.16000 52.00700 1.000 10.14705 ? 678  TYR   B OH   1 
ATOM   4602 N  N    . MET   B 1 245 ? -28.73100 19.98800 57.24700 1.000 13.13466 ? 679  MET   B N    1 
ATOM   4603 C  CA   . MET   B 1 245 ? -28.01400 19.40300 58.37600 1.000 13.61205 ? 679  MET   B CA   1 
ATOM   4604 C  C    . MET   B 1 245 ? -26.51800 19.33700 58.09900 1.000 16.45825 ? 679  MET   B C    1 
ATOM   4605 O  O    . MET   B 1 245 ? -25.70200 19.64200 58.97600 1.000 17.84913 ? 679  MET   B O    1 
ATOM   4606 C  CB   . MET   B 1 245 ? -28.56000 18.00700 58.67900 1.000 18.45830 ? 679  MET   B CB   1 
ATOM   4607 C  CG   . MET   B 1 245 ? -29.99000 17.99300 59.19400 1.000 29.14578 ? 679  MET   B CG   1 
ATOM   4608 S  SD   . MET   B 1 245 ? -30.11100 18.62900 60.87300 1.000 28.78809 ? 679  MET   B SD   1 
ATOM   4609 C  CE   . MET   B 1 245 ? -29.23300 17.34700 61.76600 1.000 14.87393 ? 679  MET   B CE   1 
ATOM   4610 N  N    . ALA   B 1 246 ? -26.14000 18.94600 56.87800 1.000 14.29291 ? 680  ALA   B N    1 
ATOM   4611 C  CA   . ALA   B 1 246 ? -24.72600 18.86900 56.52700 1.000 14.77151 ? 680  ALA   B CA   1 
ATOM   4612 C  C    . ALA   B 1 246 ? -24.08400 20.24800 56.48000 1.000 17.76166 ? 680  ALA   B C    1 
ATOM   4613 O  O    . ALA   B 1 246 ? -22.90600 20.39600 56.82600 1.000 17.88675 ? 680  ALA   B O    1 
ATOM   4614 C  CB   . ALA   B 1 246 ? -24.55400 18.15400 55.18600 1.000 16.52148 ? 680  ALA   B CB   1 
ATOM   4615 N  N    . ALA   B 1 247 ? -24.83800 21.26800 56.06400 1.000 16.87975 ? 681  ALA   B N    1 
ATOM   4616 C  CA   . ALA   B 1 247 ? -24.29400 22.62000 56.03200 1.000 13.12415 ? 681  ALA   B CA   1 
ATOM   4617 C  C    . ALA   B 1 247 ? -24.05900 23.15300 57.44000 1.000 16.84747 ? 681  ALA   B C    1 
ATOM   4618 O  O    . ALA   B 1 247 ? -23.03600 23.79600 57.70200 1.000 15.43249 ? 681  ALA   B O    1 
ATOM   4619 C  CB   . ALA   B 1 247 ? -25.23100 23.54200 55.25600 1.000 15.09936 ? 681  ALA   B CB   1 
ATOM   4620 N  N    . PHE   B 1 248 ? -24.99500 22.90000 58.35800 1.000 13.65692 ? 682  PHE   B N    1 
ATOM   4621 C  CA   . PHE   B 1 248 ? -24.79100 23.29000 59.74800 1.000 17.60565 ? 682  PHE   B CA   1 
ATOM   4622 C  C    . PHE   B 1 248 ? -23.60100 22.55900 60.35300 1.000 15.47664 ? 682  PHE   B C    1 
ATOM   4623 O  O    . PHE   B 1 248 ? -22.83300 23.13900 61.12800 1.000 14.80654 ? 682  PHE   B O    1 
ATOM   4624 C  CB   . PHE   B 1 248 ? -26.05700 23.01800 60.56000 1.000 14.25398 ? 682  PHE   B CB   1 
ATOM   4625 C  CG   . PHE   B 1 248 ? -26.95600 24.21000 60.69500 1.000 11.85558 ? 682  PHE   B CG   1 
ATOM   4626 C  CD1  . PHE   B 1 248 ? -27.23600 25.01300 59.60100 1.000 15.98255 ? 682  PHE   B CD1  1 
ATOM   4627 C  CD2  . PHE   B 1 248 ? -27.53200 24.52400 61.91600 1.000 13.80856 ? 682  PHE   B CD2  1 
ATOM   4628 C  CE1  . PHE   B 1 248 ? -28.06900 26.11400 59.72400 1.000 13.58563 ? 682  PHE   B CE1  1 
ATOM   4629 C  CE2  . PHE   B 1 248 ? -28.36700 25.62300 62.04900 1.000 15.09812 ? 682  PHE   B CE2  1 
ATOM   4630 C  CZ   . PHE   B 1 248 ? -28.63700 26.41800 60.95200 1.000 15.65723 ? 682  PHE   B CZ   1 
ATOM   4631 N  N    . HIS   B 1 249 ? -23.42300 21.28700 59.99200 1.000 16.40809 ? 683  HIS   B N    1 
ATOM   4632 C  CA   . HIS   B 1 249 ? -22.36100 20.48500 60.58900 1.000 14.95101 ? 683  HIS   B CA   1 
ATOM   4633 C  C    . HIS   B 1 249 ? -20.98700 20.93800 60.11300 1.000 18.03506 ? 683  HIS   B C    1 
ATOM   4634 O  O    . HIS   B 1 249 ? -20.09100 21.18500 60.92700 1.000 26.54318 ? 683  HIS   B O    1 
ATOM   4635 C  CB   . HIS   B 1 249 ? -22.58500 19.00600 60.27200 1.000 15.62625 ? 683  HIS   B CB   1 
ATOM   4636 C  CG   . HIS   B 1 249 ? -21.55600 18.09600 60.86800 1.000 21.58407 ? 683  HIS   B CG   1 
ATOM   4637 N  ND1  . HIS   B 1 249 ? -20.58300 17.47700 60.11400 1.000 23.44707 ? 683  HIS   B ND1  1 
ATOM   4638 C  CD2  . HIS   B 1 249 ? -21.35000 17.69900 62.14600 1.000 19.86250 ? 683  HIS   B CD2  1 
ATOM   4639 C  CE1  . HIS   B 1 249 ? -19.82200 16.73700 60.90100 1.000 18.17320 ? 683  HIS   B CE1  1 
ATOM   4640 N  NE2  . HIS   B 1 249 ? -20.26900 16.85100 62.13900 1.000 18.03177 ? 683  HIS   B NE2  1 
ATOM   4641 N  N    . HIS   B 1 250 ? -20.79900 21.05700 58.79600 1.000 20.37330 ? 684  HIS   B N    1 
ATOM   4642 C  CA   . HIS   B 1 250 ? -19.47700 21.35600 58.25600 1.000 15.69944 ? 684  HIS   B CA   1 
ATOM   4643 C  C    . HIS   B 1 250 ? -19.15700 22.84500 58.23200 1.000 15.19460 ? 684  HIS   B C    1 
ATOM   4644 O  O    . HIS   B 1 250 ? -17.97500 23.20600 58.17800 1.000 15.65587 ? 684  HIS   B O    1 
ATOM   4645 C  CB   . HIS   B 1 250 ? -19.34200 20.79900 56.83500 1.000 16.03071 ? 684  HIS   B CB   1 
ATOM   4646 C  CG   . HIS   B 1 250 ? -19.42000 19.30600 56.75700 1.000 16.73141 ? 684  HIS   B CG   1 
ATOM   4647 N  ND1  . HIS   B 1 250 ? -18.31300 18.49500 56.88900 1.000 17.71855 ? 684  HIS   B ND1  1 
ATOM   4648 C  CD2  . HIS   B 1 250 ? -20.47000 18.47800 56.54500 1.000 16.92082 ? 684  HIS   B CD2  1 
ATOM   4649 C  CE1  . HIS   B 1 250 ? -18.68000 17.23100 56.77000 1.000 18.23182 ? 684  HIS   B CE1  1 
ATOM   4650 N  NE2  . HIS   B 1 250 ? -19.98400 17.19300 56.56000 1.000 17.61330 ? 684  HIS   B NE2  1 
ATOM   4651 N  N    . LEU   B 1 251 ? -20.16600 23.71600 58.27100 1.000 12.92664 ? 685  LEU   B N    1 
ATOM   4652 C  CA   . LEU   B 1 251 ? -19.92600 25.13900 58.04900 1.000 15.29572 ? 685  LEU   B CA   1 
ATOM   4653 C  C    . LEU   B 1 251 ? -20.49400 26.03100 59.14500 1.000 12.61895 ? 685  LEU   B C    1 
ATOM   4654 O  O    . LEU   B 1 251 ? -19.74200 26.71700 59.84500 1.000 19.45427 ? 685  LEU   B O    1 
ATOM   4655 C  CB   . LEU   B 1 251 ? -20.51000 25.56600 56.70100 1.000 12.45878 ? 685  LEU   B CB   1 
ATOM   4656 C  CG   . LEU   B 1 251 ? -19.84300 25.01800 55.44100 1.000 17.69535 ? 685  LEU   B CG   1 
ATOM   4657 C  CD1  . LEU   B 1 251 ? -20.67700 25.35900 54.21600 1.000 13.94652 ? 685  LEU   B CD1  1 
ATOM   4658 C  CD2  . LEU   B 1 251 ? -18.44100 25.57700 55.30500 1.000 14.80938 ? 685  LEU   B CD2  1 
ATOM   4659 N  N    . VAL   B 1 252 ? -21.82200 26.03900 59.29200 1.000 15.20695 ? 686  VAL   B N    1 
ATOM   4660 C  CA   . VAL   B 1 252 ? -22.48100 27.05900 60.10700 1.000 19.19584 ? 686  VAL   B CA   1 
ATOM   4661 C  C    . VAL   B 1 252 ? -22.03400 26.96800 61.56200 1.000 14.89272 ? 686  VAL   B C    1 
ATOM   4662 O  O    . VAL   B 1 252 ? -21.68000 27.97700 62.18100 1.000 12.52845 ? 686  VAL   B O    1 
ATOM   4663 C  CB   . VAL   B 1 252 ? -24.01100 26.94000 59.97900 1.000 16.48744 ? 686  VAL   B CB   1 
ATOM   4664 C  CG1  . VAL   B 1 252 ? -24.69400 27.90300 60.93600 1.000 11.52953 ? 686  VAL   B CG1  1 
ATOM   4665 C  CG2  . VAL   B 1 252 ? -24.44100 27.20700 58.55100 1.000 11.49904 ? 686  VAL   B CG2  1 
ATOM   4666 N  N    . MET   B 1 253 ? -22.04900 25.76500 62.13200 1.000 12.58938 ? 687  MET   B N    1 
ATOM   4667 C  CA   . MET   B 1 253 ? -21.73700 25.60700 63.54900 1.000 12.93400 ? 687  MET   B CA   1 
ATOM   4668 C  C    . MET   B 1 253 ? -20.24000 25.69600 63.85200 1.000 15.43748 ? 687  MET   B C    1 
ATOM   4669 O  O    . MET   B 1 253 ? -19.87400 26.24800 64.89800 1.000 13.75823 ? 687  MET   B O    1 
ATOM   4670 C  CB   . MET   B 1 253 ? -22.30700 24.28800 64.08000 1.000 13.00874 ? 687  MET   B CB   1 
ATOM   4671 C  CG   . MET   B 1 253 ? -23.83500 24.22900 64.08400 1.000 12.59499 ? 687  MET   B CG   1 
ATOM   4672 S  SD   . MET   B 1 253 ? -24.65100 25.60900 64.93000 1.000 12.54387 ? 687  MET   B SD   1 
ATOM   4673 C  CE   . MET   B 1 253 ? -23.94100 25.48200 66.56900 1.000 12.93028 ? 687  MET   B CE   1 
ATOM   4674 N  N    . PRO   B 1 254 ? -19.33900 25.16600 63.00800 1.000 19.68422 ? 688  PRO   B N    1 
ATOM   4675 C  CA   . PRO   B 1 254 ? -17.90600 25.38700 63.28500 1.000 14.13671 ? 688  PRO   B CA   1 
ATOM   4676 C  C    . PRO   B 1 254 ? -17.51000 26.85200 63.21900 1.000 16.42953 ? 688  PRO   B C    1 
ATOM   4677 O  O    . PRO   B 1 254 ? -16.79800 27.34100 64.10700 1.000 14.93287 ? 688  PRO   B O    1 
ATOM   4678 C  CB   . PRO   B 1 254 ? -17.20600 24.55200 62.20300 1.000 20.10632 ? 688  PRO   B CB   1 
ATOM   4679 C  CG   . PRO   B 1 254 ? -18.19300 23.52300 61.82400 1.000 16.91913 ? 688  PRO   B CG   1 
ATOM   4680 C  CD   . PRO   B 1 254 ? -19.52700 24.19300 61.91600 1.000 15.00758 ? 688  PRO   B CD   1 
ATOM   4681 N  N    . ILE   B 1 255 ? -17.95800 27.56900 62.18500 1.000 17.19885 ? 689  ILE   B N    1 
ATOM   4682 C  CA   . ILE   B 1 255 ? -17.66600 28.99700 62.07800 1.000 15.45146 ? 689  ILE   B CA   1 
ATOM   4683 C  C    . ILE   B 1 255 ? -18.28000 29.75800 63.24900 1.000 18.72891 ? 689  ILE   B C    1 
ATOM   4684 O  O    . ILE   B 1 255 ? -17.63100 30.60600 63.87400 1.000 14.13189 ? 689  ILE   B O    1 
ATOM   4685 C  CB   . ILE   B 1 255 ? -18.16800 29.54700 60.73000 1.000 16.31050 ? 689  ILE   B CB   1 
ATOM   4686 C  CG1  . ILE   B 1 255 ? -17.42700 28.88700 59.56400 1.000 15.01212 ? 689  ILE   B CG1  1 
ATOM   4687 C  CG2  . ILE   B 1 255 ? -18.01200 31.06000 60.68200 1.000 17.05288 ? 689  ILE   B CG2  1 
ATOM   4688 C  CD1  . ILE   B 1 255 ? -18.01500 29.20600 58.20900 1.000 14.73464 ? 689  ILE   B CD1  1 
ATOM   4689 N  N    . ALA   B 1 256 ? -19.54600 29.47200 63.55700 1.000 13.43038 ? 690  ALA   B N    1 
ATOM   4690 C  CA   . ALA   B 1 256 ? -20.22100 30.20700 64.62100 1.000 14.09129 ? 690  ALA   B CA   1 
ATOM   4691 C  C    . ALA   B 1 256 ? -19.52100 30.01300 65.95900 1.000 18.26516 ? 690  ALA   B C    1 
ATOM   4692 O  O    . ALA   B 1 256 ? -19.36600 30.96800 66.72600 1.000 15.60795 ? 690  ALA   B O    1 
ATOM   4693 C  CB   . ALA   B 1 256 ? -21.68400 29.77900 64.71600 1.000 12.95283 ? 690  ALA   B CB   1 
ATOM   4694 N  N    . ARG   B 1 257 ? -19.08300 28.78500 66.25500 1.000 20.25536 ? 691  ARG   B N    1 
ATOM   4695 C  CA   . ARG   B 1 257 ? -18.40800 28.52400 67.52300 1.000 14.78392 ? 691  ARG   B CA   1 
ATOM   4696 C  C    . ARG   B 1 257 ? -17.06300 29.23500 67.60800 1.000 15.30708 ? 691  ARG   B C    1 
ATOM   4697 O  O    . ARG   B 1 257 ? -16.64700 29.64300 68.70000 1.000 15.80266 ? 691  ARG   B O    1 
ATOM   4698 C  CB   . ARG   B 1 257 ? -18.22300 27.02100 67.72200 1.000 14.95517 ? 691  ARG   B CB   1 
ATOM   4699 C  CG   . ARG   B 1 257 ? -19.42900 26.32200 68.31600 1.000 14.72605 ? 691  ARG   B CG   1 
ATOM   4700 C  CD   . ARG   B 1 257 ? -19.10200 24.89300 68.71200 1.000 17.23233 ? 691  ARG   B CD   1 
ATOM   4701 N  NE   . ARG   B 1 257 ? -18.71900 24.08600 67.56100 1.000 22.02394 ? 691  ARG   B NE   1 
ATOM   4702 C  CZ   . ARG   B 1 257 ? -19.57700 23.45800 66.77000 1.000 21.48891 ? 691  ARG   B CZ   1 
ATOM   4703 N  NH1  . ARG   B 1 257 ? -20.88200 23.52300 66.97500 1.000 19.37477 ? 691  ARG   B NH1  1 
ATOM   4704 N  NH2  . ARG   B 1 257 ? -19.11400 22.74600 65.74600 1.000 14.53636 ? 691  ARG   B NH2  1 
ATOM   4705 N  N    . GLU   B 1 258 ? -16.36800 29.38700 66.47900 1.000 15.25842 ? 692  GLU   B N    1 
ATOM   4706 C  CA   . GLU   B 1 258 ? -15.11800 30.13700 66.48400 1.000 15.76632 ? 692  GLU   B CA   1 
ATOM   4707 C  C    . GLU   B 1 258 ? -15.38300 31.62900 66.63800 1.000 18.07234 ? 692  GLU   B C    1 
ATOM   4708 O  O    . GLU   B 1 258 ? -14.61800 32.34000 67.30000 1.000 18.39477 ? 692  GLU   B O    1 
ATOM   4709 C  CB   . GLU   B 1 258 ? -14.33400 29.85000 65.20500 1.000 15.73929 ? 692  GLU   B CB   1 
ATOM   4710 C  CG   . GLU   B 1 258 ? -12.86600 30.24300 65.24800 1.000 16.38127 ? 692  GLU   B CG   1 
ATOM   4711 C  CD   . GLU   B 1 258 ? -12.11700 29.76200 64.01900 1.000 21.16020 ? 692  GLU   B CD   1 
ATOM   4712 O  OE1  . GLU   B 1 258 ? -12.70600 28.98100 63.23800 1.000 19.38219 ? 692  GLU   B OE1  1 
ATOM   4713 O  OE2  . GLU   B 1 258 ? -10.95000 30.16600 63.82700 1.000 22.19604 ? 692  GLU   B OE2  1 
ATOM   4714 N  N    . PHE   B 1 259 ? -16.47300 32.11500 66.04300 1.000 15.15850 ? 693  PHE   B N    1 
ATOM   4715 C  CA   . PHE   B 1 259 ? -16.85800 33.51200 66.19600 1.000 18.03151 ? 693  PHE   B CA   1 
ATOM   4716 C  C    . PHE   B 1 259 ? -17.25000 33.83100 67.63300 1.000 15.43102 ? 693  PHE   B C    1 
ATOM   4717 O  O    . PHE   B 1 259 ? -17.08700 34.97200 68.07700 1.000 15.74586 ? 693  PHE   B O    1 
ATOM   4718 C  CB   . PHE   B 1 259 ? -18.00700 33.82700 65.23700 1.000 18.72481 ? 693  PHE   B CB   1 
ATOM   4719 C  CG   . PHE   B 1 259 ? -18.50800 35.24200 65.31400 1.000 17.25981 ? 693  PHE   B CG   1 
ATOM   4720 C  CD1  . PHE   B 1 259 ? -17.69700 36.30200 64.94100 1.000 14.72864 ? 693  PHE   B CD1  1 
ATOM   4721 C  CD2  . PHE   B 1 259 ? -19.80300 35.51000 65.73800 1.000 16.20642 ? 693  PHE   B CD2  1 
ATOM   4722 C  CE1  . PHE   B 1 259 ? -18.16600 37.60500 64.99900 1.000 14.73556 ? 693  PHE   B CE1  1 
ATOM   4723 C  CE2  . PHE   B 1 259 ? -20.27700 36.81100 65.80100 1.000 14.07983 ? 693  PHE   B CE2  1 
ATOM   4724 C  CZ   . PHE   B 1 259 ? -19.45700 37.85900 65.43000 1.000 14.41207 ? 693  PHE   B CZ   1 
ATOM   4725 N  N    . ALA   B 1 260 ? -17.75000 32.83800 68.36400 1.000 15.38895 ? 694  ALA   B N    1 
ATOM   4726 C  CA   . ALA   B 1 260 ? -18.21300 32.99700 69.73900 1.000 15.67212 ? 694  ALA   B CA   1 
ATOM   4727 C  C    . ALA   B 1 260 ? -19.19200 34.16300 69.88400 1.000 15.44616 ? 694  ALA   B C    1 
ATOM   4728 O  O    . ALA   B 1 260 ? -18.90100 35.14300 70.58100 1.000 17.29084 ? 694  ALA   B O    1 
ATOM   4729 C  CB   . ALA   B 1 260 ? -17.03500 33.15900 70.68900 1.000 16.48904 ? 694  ALA   B CB   1 
ATOM   4730 N  N    . PRO   B 1 261 ? -20.35700 34.09400 69.24900 1.000 14.79812 ? 695  PRO   B N    1 
ATOM   4731 C  CA   . PRO   B 1 261 ? -21.29900 35.20900 69.33900 1.000 17.01215 ? 695  PRO   B CA   1 
ATOM   4732 C  C    . PRO   B 1 261 ? -21.88100 35.32900 70.73600 1.000 18.34775 ? 695  PRO   B C    1 
ATOM   4733 O  O    . PRO   B 1 261 ? -21.96500 34.35700 71.49200 1.000 15.02766 ? 695  PRO   B O    1 
ATOM   4734 C  CB   . PRO   B 1 261 ? -22.37800 34.84300 68.31400 1.000 13.87842 ? 695  PRO   B CB   1 
ATOM   4735 C  CG   . PRO   B 1 261 ? -22.35500 33.36000 68.28800 1.000 13.75861 ? 695  PRO   B CG   1 
ATOM   4736 C  CD   . PRO   B 1 261 ? -20.91300 32.96800 68.48000 1.000 14.27385 ? 695  PRO   B CD   1 
ATOM   4737 N  N    . GLU   B 1 262 ? -22.26200 36.55500 71.08300 1.000 15.03857 ? 696  GLU   B N    1 
ATOM   4738 C  CA   . GLU   B 1 262 ? -22.97600 36.82100 72.32200 1.000 16.75528 ? 696  GLU   B CA   1 
ATOM   4739 C  C    . GLU   B 1 262 ? -24.48200 36.89800 72.12700 1.000 15.60733 ? 696  GLU   B C    1 
ATOM   4740 O  O    . GLU   B 1 262 ? -25.22300 36.80600 73.11000 1.000 20.24501 ? 696  GLU   B O    1 
ATOM   4741 C  CB   . GLU   B 1 262 ? -22.48100 38.12600 72.95200 1.000 15.92164 ? 696  GLU   B CB   1 
ATOM   4742 C  CG   . GLU   B 1 262 ? -21.02600 38.09000 73.37600 1.000 16.61966 ? 696  GLU   B CG   1 
ATOM   4743 C  CD   . GLU   B 1 262 ? -20.46800 39.46900 73.64000 1.000 23.27484 ? 696  GLU   B CD   1 
ATOM   4744 O  OE1  . GLU   B 1 262 ? -20.12200 40.16100 72.66100 1.000 17.08036 ? 696  GLU   B OE1  1 
ATOM   4745 O  OE2  . GLU   B 1 262 ? -20.39000 39.86600 74.82500 1.000 25.47508 ? 696  GLU   B OE2  1 
ATOM   4746 N  N    . LEU   B 1 263 ? -24.94300 37.06300 70.88900 1.000 15.97189 ? 697  LEU   B N    1 
ATOM   4747 C  CA   . LEU   B 1 263 ? -26.36300 37.06300 70.57100 1.000 13.63290 ? 697  LEU   B CA   1 
ATOM   4748 C  C    . LEU   B 1 263 ? -26.53600 36.50500 69.16800 1.000 15.71482 ? 697  LEU   B C    1 
ATOM   4749 O  O    . LEU   B 1 263 ? -25.76600 36.83800 68.26100 1.000 14.00565 ? 697  LEU   B O    1 
ATOM   4750 C  CB   . LEU   B 1 263 ? -26.96300 38.47000 70.66500 1.000 13.70423 ? 697  LEU   B CB   1 
ATOM   4751 C  CG   . LEU   B 1 263 ? -28.44300 38.59200 70.29400 1.000 24.67934 ? 697  LEU   B CG   1 
ATOM   4752 C  CD1  . LEU   B 1 263 ? -29.31000 37.80300 71.27400 1.000 23.08830 ? 697  LEU   B CD1  1 
ATOM   4753 C  CD2  . LEU   B 1 263 ? -28.87300 40.05000 70.24200 1.000 16.84616 ? 697  LEU   B CD2  1 
ATOM   4754 N  N    . VAL   B 1 264 ? -27.54200 35.65400 68.99600 1.000 13.88738 ? 698  VAL   B N    1 
ATOM   4755 C  CA   . VAL   B 1 264 ? -27.82400 35.01200 67.71900 1.000 16.60128 ? 698  VAL   B CA   1 
ATOM   4756 C  C    . VAL   B 1 264 ? -29.20000 35.46400 67.25400 1.000 11.73703 ? 698  VAL   B C    1 
ATOM   4757 O  O    . VAL   B 1 264 ? -30.20500 35.19000 67.92200 1.000 11.66370 ? 698  VAL   B O    1 
ATOM   4758 C  CB   . VAL   B 1 264 ? -27.76000 33.48100 67.82500 1.000 12.08937 ? 698  VAL   B CB   1 
ATOM   4759 C  CG1  . VAL   B 1 264 ? -28.07000 32.84900 66.48600 1.000 11.64862 ? 698  VAL   B CG1  1 
ATOM   4760 C  CG2  . VAL   B 1 264 ? -26.39700 33.04500 68.32700 1.000 12.55387 ? 698  VAL   B CG2  1 
ATOM   4761 N  N    . LEU   B 1 265 ? -29.24200 36.16000 66.12000 1.000 11.50882 ? 699  LEU   B N    1 
ATOM   4762 C  CA   . LEU   B 1 265 ? -30.48300 36.52100 65.44800 1.000 11.12034 ? 699  LEU   B CA   1 
ATOM   4763 C  C    . LEU   B 1 265 ? -30.67500 35.60500 64.25200 1.000 13.96278 ? 699  LEU   B C    1 
ATOM   4764 O  O    . LEU   B 1 265 ? -29.79500 35.51200 63.39100 1.000 13.32734 ? 699  LEU   B O    1 
ATOM   4765 C  CB   . LEU   B 1 265 ? -30.46100 37.97600 64.97600 1.000 12.50822 ? 699  LEU   B CB   1 
ATOM   4766 C  CG   . LEU   B 1 265 ? -30.01600 39.05400 65.96000 1.000 11.64680 ? 699  LEU   B CG   1 
ATOM   4767 C  CD1  . LEU   B 1 265 ? -30.13200 40.42900 65.31700 1.000 11.68295 ? 699  LEU   B CD1  1 
ATOM   4768 C  CD2  . LEU   B 1 265 ? -30.83300 38.98100 67.24100 1.000 13.09863 ? 699  LEU   B CD2  1 
ATOM   4769 N  N    . VAL   B 1 266 ? -31.81900 34.93500 64.19200 1.000 10.58670 ? 700  VAL   B N    1 
ATOM   4770 C  CA   . VAL   B 1 266 ? -32.14200 34.05700 63.07600 1.000 10.19112 ? 700  VAL   B CA   1 
ATOM   4771 C  C    . VAL   B 1 266 ? -33.08700 34.79600 62.14400 1.000 12.67806 ? 700  VAL   B C    1 
ATOM   4772 O  O    . VAL   B 1 266 ? -34.21800 35.11900 62.52200 1.000 10.92281 ? 700  VAL   B O    1 
ATOM   4773 C  CB   . VAL   B 1 266 ? -32.76000 32.73500 63.54900 1.000 10.54834 ? 700  VAL   B CB   1 
ATOM   4774 C  CG1  . VAL   B 1 266 ? -32.89700 31.77300 62.37300 1.000 10.29298 ? 700  VAL   B CG1  1 
ATOM   4775 C  CG2  . VAL   B 1 266 ? -31.91400 32.11900 64.64700 1.000 12.89835 ? 700  VAL   B CG2  1 
ATOM   4776 N  N    . SER   B 1 267 ? -32.61700 35.08800 60.93200 1.000 13.81804 ? 701  SER   B N    1 
ATOM   4777 C  CA   . SER   B 1 267 ? -33.50400 35.52400 59.85900 1.000 10.64808 ? 701  SER   B CA   1 
ATOM   4778 C  C    . SER   B 1 267 ? -34.18000 34.26500 59.34700 1.000 10.76867 ? 701  SER   B C    1 
ATOM   4779 O  O    . SER   B 1 267 ? -33.67200 33.56300 58.46800 1.000 13.20700 ? 701  SER   B O    1 
ATOM   4780 C  CB   . SER   B 1 267 ? -32.74000 36.26200 58.76900 1.000 9.65573  ? 701  SER   B CB   1 
ATOM   4781 O  OG   . SER   B 1 267 ? -32.63100 37.63800 59.09100 1.000 13.50870 ? 701  SER   B OG   1 
ATOM   4782 N  N    . ALA   B 1 268 ? -35.33500 33.97100 59.93100 1.000 9.35134  ? 702  ALA   B N    1 
ATOM   4783 C  CA   . ALA   B 1 268 ? -35.95900 32.66200 59.84700 1.000 13.43954 ? 702  ALA   B CA   1 
ATOM   4784 C  C    . ALA   B 1 268 ? -37.17600 32.71400 58.92800 1.000 11.01789 ? 702  ALA   B C    1 
ATOM   4785 O  O    . ALA   B 1 268 ? -38.32200 32.55900 59.35700 1.000 13.10847 ? 702  ALA   B O    1 
ATOM   4786 C  CB   . ALA   B 1 268 ? -36.33700 32.17100 61.25000 1.000 9.37947  ? 702  ALA   B CB   1 
ATOM   4787 N  N    . GLY   B 1 269 ? -36.91700 32.93600 57.64400 1.000 10.98354 ? 703  GLY   B N    1 
ATOM   4788 C  CA   . GLY   B 1 269 ? -37.91500 32.62900 56.64400 1.000 9.53011  ? 703  GLY   B CA   1 
ATOM   4789 C  C    . GLY   B 1 269 ? -38.14200 31.13300 56.57300 1.000 10.99842 ? 703  GLY   B C    1 
ATOM   4790 O  O    . GLY   B 1 269 ? -37.25100 30.33300 56.85000 1.000 18.49575 ? 703  GLY   B O    1 
ATOM   4791 N  N    . PHE   B 1 270 ? -39.36400 30.74500 56.23200 1.000 13.88764 ? 704  PHE   B N    1 
ATOM   4792 C  CA   . PHE   B 1 270 ? -39.69400 29.33200 56.10900 1.000 9.84513  ? 704  PHE   B CA   1 
ATOM   4793 C  C    . PHE   B 1 270 ? -40.12400 28.99300 54.69000 1.000 9.20002  ? 704  PHE   B C    1 
ATOM   4794 O  O    . PHE   B 1 270 ? -40.93700 28.09600 54.47200 1.000 9.32044  ? 704  PHE   B O    1 
ATOM   4795 C  CB   . PHE   B 1 270 ? -40.75800 28.93900 57.13100 1.000 9.13966  ? 704  PHE   B CB   1 
ATOM   4796 C  CG   . PHE   B 1 270 ? -40.27600 29.04700 58.54800 1.000 9.72809  ? 704  PHE   B CG   1 
ATOM   4797 C  CD1  . PHE   B 1 270 ? -39.48100 28.05700 59.09500 1.000 10.53818 ? 704  PHE   B CD1  1 
ATOM   4798 C  CD2  . PHE   B 1 270 ? -40.57600 30.15800 59.31700 1.000 11.36413 ? 704  PHE   B CD2  1 
ATOM   4799 C  CE1  . PHE   B 1 270 ? -39.01300 28.15800 60.39300 1.000 13.32811 ? 704  PHE   B CE1  1 
ATOM   4800 C  CE2  . PHE   B 1 270 ? -40.11300 30.26500 60.61600 1.000 10.36783 ? 704  PHE   B CE2  1 
ATOM   4801 C  CZ   . PHE   B 1 270 ? -39.33400 29.26300 61.15400 1.000 11.98696 ? 704  PHE   B CZ   1 
ATOM   4802 N  N    . ASP   B 1 271 ? -39.56900 29.71200 53.71700 1.000 12.47420 ? 705  ASP   B N    1 
ATOM   4803 C  CA   . ASP   B 1 271 ? -39.80700 29.44400 52.30500 1.000 11.26798 ? 705  ASP   B CA   1 
ATOM   4804 C  C    . ASP   B 1 271 ? -38.87700 28.37600 51.73600 1.000 11.57636 ? 705  ASP   B C    1 
ATOM   4805 O  O    . ASP   B 1 271 ? -38.89100 28.14200 50.52300 1.000 10.80509 ? 705  ASP   B O    1 
ATOM   4806 C  CB   . ASP   B 1 271 ? -39.70700 30.74200 51.48400 1.000 10.24366 ? 705  ASP   B CB   1 
ATOM   4807 C  CG   . ASP   B 1 271 ? -38.54800 31.63900 51.90200 1.000 11.34040 ? 705  ASP   B CG   1 
ATOM   4808 O  OD1  . ASP   B 1 271 ? -37.68200 31.22500 52.69700 1.000 10.94312 ? 705  ASP   B OD1  1 
ATOM   4809 O  OD2  . ASP   B 1 271 ? -38.50200 32.77900 51.41200 1.000 9.12751  ? 705  ASP   B OD2  1 
ATOM   4810 N  N    . ALA   B 1 272 ? -38.07500 27.72100 52.57400 1.000 9.52500  ? 706  ALA   B N    1 
ATOM   4811 C  CA   . ALA   B 1 272 ? -37.39700 26.49600 52.17500 1.000 9.78350  ? 706  ALA   B CA   1 
ATOM   4812 C  C    . ALA   B 1 272 ? -38.16500 25.25200 52.59800 1.000 9.92372  ? 706  ALA   B C    1 
ATOM   4813 O  O    . ALA   B 1 272 ? -37.65800 24.13700 52.43400 1.000 11.04830 ? 706  ALA   B O    1 
ATOM   4814 C  CB   . ALA   B 1 272 ? -35.97600 26.45100 52.74500 1.000 9.77911  ? 706  ALA   B CB   1 
ATOM   4815 N  N    . ALA   B 1 273 ? -39.37500 25.42000 53.12600 1.000 12.33775 ? 707  ALA   B N    1 
ATOM   4816 C  CA   . ALA   B 1 273 ? -40.20400 24.30200 53.54200 1.000 10.08072 ? 707  ALA   B CA   1 
ATOM   4817 C  C    . ALA   B 1 273 ? -40.98300 23.73700 52.35800 1.000 13.03076 ? 707  ALA   B C    1 
ATOM   4818 O  O    . ALA   B 1 273 ? -41.14900 24.38400 51.32100 1.000 10.26246 ? 707  ALA   B O    1 
ATOM   4819 C  CB   . ALA   B 1 273 ? -41.17000 24.73300 54.65000 1.000 10.78927 ? 707  ALA   B CB   1 
ATOM   4820 N  N    . ARG   B 1 274 ? -41.45700 22.50600 52.54800 1.000 13.52406 ? 708  ARG   B N    1 
ATOM   4821 C  CA   . ARG   B 1 274 ? -42.31100 21.82400 51.54800 1.000 15.47235 ? 708  ARG   B CA   1 
ATOM   4822 C  C    . ARG   B 1 274 ? -43.55100 22.67000 51.20000 1.000 29.29292 ? 708  ARG   B C    1 
ATOM   4823 O  O    . ARG   B 1 274 ? -44.04300 23.41200 52.08600 1.000 24.70591 ? 708  ARG   B O    1 
ATOM   4824 C  CB   . ARG   B 1 274 ? -42.72400 20.49300 52.17000 1.000 15.97969 ? 708  ARG   B CB   1 
ATOM   4825 C  CG   . ARG   B 1 274 ? -44.06600 20.46800 52.88700 1.000 27.79716 ? 708  ARG   B CG   1 
ATOM   4826 C  CD   . ARG   B 1 274 ? -44.99300 19.33300 52.48200 1.000 40.10844 ? 708  ARG   B CD   1 
ATOM   4827 N  NE   . ARG   B 1 274 ? -45.40200 19.40300 51.07700 1.000 38.61852 ? 708  ARG   B NE   1 
ATOM   4828 C  CZ   . ARG   B 1 274 ? -46.40500 20.13500 50.61600 1.000 37.20291 ? 708  ARG   B CZ   1 
ATOM   4829 N  NH1  . ARG   B 1 274 ? -47.15700 20.83000 51.44800 1.000 30.14073 ? 708  ARG   B NH1  1 
ATOM   4830 N  NH2  . ARG   B 1 274 ? -46.64300 20.17600 49.32100 1.000 26.30468 ? 708  ARG   B NH2  1 
ATOM   4831 N  N    . GLY   B 1 275 ? -44.00600 22.60900 49.94600 1.000 16.58073 ? 709  GLY   B N    1 
ATOM   4832 C  CA   . GLY   B 1 275 ? -45.22100 23.34500 49.55200 1.000 19.75907 ? 709  GLY   B CA   1 
ATOM   4833 C  C    . GLY   B 1 275 ? -45.04300 24.84100 49.30100 1.000 16.62319 ? 709  GLY   B C    1 
ATOM   4834 O  O    . GLY   B 1 275 ? -46.04800 25.52700 49.14200 1.000 11.13052 ? 709  GLY   B O    1 
ATOM   4835 N  N    . ASP   B 1 276 ? -43.80500 25.32500 49.30200 1.000 14.61754 ? 710  ASP   B N    1 
ATOM   4836 C  CA   . ASP   B 1 276 ? -43.56900 26.78200 49.13100 1.000 12.83498 ? 710  ASP   B CA   1 
ATOM   4837 C  C    . ASP   B 1 276 ? -43.28700 27.09100 47.66000 1.000 13.67297 ? 710  ASP   B C    1 
ATOM   4838 O  O    . ASP   B 1 276 ? -42.18000 26.80300 47.18500 1.000 17.73723 ? 710  ASP   B O    1 
ATOM   4839 C  CB   . ASP   B 1 276 ? -42.55500 27.35300 50.10700 1.000 11.43262 ? 710  ASP   B CB   1 
ATOM   4840 C  CG   . ASP   B 1 276 ? -42.56900 28.87200 50.21100 1.000 12.60006 ? 710  ASP   B CG   1 
ATOM   4841 O  OD1  . ASP   B 1 276 ? -42.42100 29.53400 49.17200 1.000 13.92581 ? 710  ASP   B OD1  1 
ATOM   4842 O  OD2  . ASP   B 1 276 ? -42.74600 29.38300 51.32400 1.000 10.55353 ? 710  ASP   B OD2  1 
ATOM   4843 N  N    . PRO   B 1 277 ? -44.22800 27.74100 46.95300 1.000 15.81161 ? 711  PRO   B N    1 
ATOM   4844 C  CA   . PRO   B 1 277 ? -44.07100 28.11100 45.50500 1.000 20.39205 ? 711  PRO   B CA   1 
ATOM   4845 C  C    . PRO   B 1 277 ? -42.84800 29.00000 45.23700 1.000 16.46259 ? 711  PRO   B C    1 
ATOM   4846 O  O    . PRO   B 1 277 ? -42.38500 29.06300 44.08500 1.000 12.48487 ? 711  PRO   B O    1 
ATOM   4847 C  CB   . PRO   B 1 277 ? -45.42800 28.76400 45.21000 1.000 10.86875 ? 711  PRO   B CB   1 
ATOM   4848 C  CG   . PRO   B 1 277 ? -46.36700 28.13800 46.20600 1.000 11.48843 ? 711  PRO   B CG   1 
ATOM   4849 C  CD   . PRO   B 1 277 ? -45.56700 28.16100 47.45300 1.000 16.04191 ? 711  PRO   B CD   1 
ATOM   4850 N  N    . LEU   B 1 278 ? -42.31100 29.64400 46.27400 1.000 15.19811 ? 712  LEU   B N    1 
ATOM   4851 C  CA   . LEU   B 1 278 ? -41.21600 30.62100 46.10000 1.000 16.58942 ? 712  LEU   B CA   1 
ATOM   4852 C  C    . LEU   B 1 278 ? -39.87100 30.03500 46.54000 1.000 18.42251 ? 712  LEU   B C    1 
ATOM   4853 O  O    . LEU   B 1 278 ? -38.89800 30.79400 46.59100 1.000 22.64095 ? 712  LEU   B O    1 
ATOM   4854 C  CB   . LEU   B 1 278 ? -41.57800 31.87400 46.89100 1.000 12.50157 ? 712  LEU   B CB   1 
ATOM   4855 C  CG   . LEU   B 1 278 ? -42.55400 32.83600 46.20700 1.000 15.77342 ? 712  LEU   B CG   1 
ATOM   4856 C  CD1  . LEU   B 1 278 ? -43.00900 33.93400 47.14200 1.000 14.87000 ? 712  LEU   B CD1  1 
ATOM   4857 C  CD2  . LEU   B 1 278 ? -41.94700 33.43300 44.95600 1.000 13.53703 ? 712  LEU   B CD2  1 
ATOM   4858 N  N    . GLY   B 1 279 ? -39.84000 28.76000 46.87700 1.000 11.33343 ? 713  GLY   B N    1 
ATOM   4859 C  CA   . GLY   B 1 279 ? -38.60800 28.11200 47.32400 1.000 10.13824 ? 713  GLY   B CA   1 
ATOM   4860 C  C    . GLY   B 1 279 ? -38.32200 26.85000 46.55000 1.000 12.83617 ? 713  GLY   B C    1 
ATOM   4861 O  O    . GLY   B 1 279 ? -37.25900 26.77500 45.93700 1.000 13.48100 ? 713  GLY   B O    1 
ATOM   4862 N  N    . GLY   B 1 280 ? -39.25900 25.91000 46.56400 1.000 10.68521 ? 714  GLY   B N    1 
ATOM   4863 C  CA   . GLY   B 1 280 ? -39.09300 24.65300 45.82100 1.000 11.10815 ? 714  GLY   B CA   1 
ATOM   4864 C  C    . GLY   B 1 280 ? -38.26100 23.63800 46.58900 1.000 12.81879 ? 714  GLY   B C    1 
ATOM   4865 O  O    . GLY   B 1 280 ? -37.86100 22.65000 45.96700 1.000 11.97548 ? 714  GLY   B O    1 
ATOM   4866 N  N    . PHE   B 1 281 ? -38.01100 23.88700 47.87700 1.000 12.80098 ? 715  PHE   B N    1 
ATOM   4867 C  CA   . PHE   B 1 281 ? -37.25800 22.96500 48.76900 1.000 10.91776 ? 715  PHE   B CA   1 
ATOM   4868 C  C    . PHE   B 1 281 ? -38.19900 22.17000 49.67900 1.000 10.96722 ? 715  PHE   B C    1 
ATOM   4869 O  O    . PHE   B 1 281 ? -39.40900 22.42800 49.72300 1.000 15.12133 ? 715  PHE   B O    1 
ATOM   4870 C  CB   . PHE   B 1 281 ? -36.19300 23.72100 49.56700 1.000 10.63675 ? 715  PHE   B CB   1 
ATOM   4871 C  CG   . PHE   B 1 281 ? -34.98400 24.22000 48.79300 1.000 10.68387 ? 715  PHE   B CG   1 
ATOM   4872 C  CD1  . PHE   B 1 281 ? -34.90100 24.08200 47.41400 1.000 11.06108 ? 715  PHE   B CD1  1 
ATOM   4873 C  CD2  . PHE   B 1 281 ? -33.93300 24.83700 49.45700 1.000 11.20353 ? 715  PHE   B CD2  1 
ATOM   4874 C  CE1  . PHE   B 1 281 ? -33.79200 24.53900 46.72800 1.000 11.01380 ? 715  PHE   B CE1  1 
ATOM   4875 C  CE2  . PHE   B 1 281 ? -32.82800 25.29200 48.76500 1.000 13.78142 ? 715  PHE   B CE2  1 
ATOM   4876 C  CZ   . PHE   B 1 281 ? -32.76000 25.14000 47.40200 1.000 10.83616 ? 715  PHE   B CZ   1 
ATOM   4877 N  N    . GLN   B 1 282 ? -37.64000 21.22200 50.40600 1.000 11.10740 ? 716  GLN   B N    1 
ATOM   4878 C  CA   . GLN   B 1 282 ? -38.44600 20.34900 51.26000 1.000 11.22817 ? 716  GLN   B CA   1 
ATOM   4879 C  C    . GLN   B 1 282 ? -37.80900 20.18300 52.64100 1.000 13.34813 ? 716  GLN   B C    1 
ATOM   4880 O  O    . GLN   B 1 282 ? -37.72500 19.08100 53.18600 1.000 17.10614 ? 716  GLN   B O    1 
ATOM   4881 C  CB   . GLN   B 1 282 ? -38.66400 18.99400 50.59000 1.000 11.73285 ? 716  GLN   B CB   1 
ATOM   4882 C  CG   . GLN   B 1 282 ? -37.38900 18.27200 50.20400 1.000 18.86367 ? 716  GLN   B CG   1 
ATOM   4883 C  CD   . GLN   B 1 282 ? -37.65500 16.96200 49.48500 1.000 28.64478 ? 716  GLN   B CD   1 
ATOM   4884 O  OE1  . GLN   B 1 282 ? -38.75300 16.72600 48.98100 1.000 29.09175 ? 716  GLN   B OE1  1 
ATOM   4885 N  NE2  . GLN   B 1 282 ? -36.64700 16.10000 49.43700 1.000 26.28448 ? 716  GLN   B NE2  1 
ATOM   4886 N  N    . VAL   B 1 283 ? -37.36400 21.28800 53.23900 1.000 12.00673 ? 717  VAL   B N    1 
ATOM   4887 C  CA   . VAL   B 1 283 ? -36.95800 21.24800 54.64100 1.000 10.66847 ? 717  VAL   B CA   1 
ATOM   4888 C  C    . VAL   B 1 283 ? -38.19800 21.05000 55.50000 1.000 10.84701 ? 717  VAL   B C    1 
ATOM   4889 O  O    . VAL   B 1 283 ? -39.17300 21.80200 55.38800 1.000 10.44061 ? 717  VAL   B O    1 
ATOM   4890 C  CB   . VAL   B 1 283 ? -36.20800 22.52700 55.03600 1.000 14.73128 ? 717  VAL   B CB   1 
ATOM   4891 C  CG1  . VAL   B 1 283 ? -35.82900 22.47400 56.51000 1.000 16.58745 ? 717  VAL   B CG1  1 
ATOM   4892 C  CG2  . VAL   B 1 283 ? -34.96900 22.70500 54.17500 1.000 10.45058 ? 717  VAL   B CG2  1 
ATOM   4893 N  N    . THR   B 1 284 ? -38.17600 20.02300 56.34300 1.000 10.85929 ? 718  THR   B N    1 
ATOM   4894 C  CA   . THR   B 1 284 ? -39.33200 19.68100 57.15500 1.000 11.79680 ? 718  THR   B CA   1 
ATOM   4895 C  C    . THR   B 1 284 ? -39.31900 20.45700 58.46600 1.000 16.97478 ? 718  THR   B C    1 
ATOM   4896 O  O    . THR   B 1 284 ? -38.27500 20.96200 58.89300 1.000 16.05677 ? 718  THR   B O    1 
ATOM   4897 C  CB   . THR   B 1 284 ? -39.34700 18.18200 57.44300 1.000 11.32304 ? 718  THR   B CB   1 
ATOM   4898 O  OG1  . THR   B 1 284 ? -38.38800 17.88700 58.46400 1.000 11.39821 ? 718  THR   B OG1  1 
ATOM   4899 C  CG2  . THR   B 1 284 ? -39.00500 17.40000 56.19300 1.000 14.11653 ? 718  THR   B CG2  1 
ATOM   4900 N  N    . PRO   B 1 285 ? -40.47700 20.59300 59.11900 1.000 16.04970 ? 719  PRO   B N    1 
ATOM   4901 C  CA   . PRO   B 1 285 ? -40.49100 21.23400 60.44400 1.000 17.93800 ? 719  PRO   B CA   1 
ATOM   4902 C  C    . PRO   B 1 285 ? -39.53800 20.58800 61.43700 1.000 16.58402 ? 719  PRO   B C    1 
ATOM   4903 O  O    . PRO   B 1 285 ? -38.96600 21.29000 62.28100 1.000 18.02086 ? 719  PRO   B O    1 
ATOM   4904 C  CB   . PRO   B 1 285 ? -41.95400 21.08700 60.88100 1.000 14.05090 ? 719  PRO   B CB   1 
ATOM   4905 C  CG   . PRO   B 1 285 ? -42.71800 21.05300 59.60900 1.000 11.83621 ? 719  PRO   B CG   1 
ATOM   4906 C  CD   . PRO   B 1 285 ? -41.83900 20.32000 58.62400 1.000 13.19948 ? 719  PRO   B CD   1 
ATOM   4907 N  N    . GLU   B 1 286 ? -39.34700 19.26900 61.35700 1.000 18.76449 ? 720  GLU   B N    1 
ATOM   4908 C  CA   . GLU   B 1 286 ? -38.38500 18.60100 62.22800 1.000 13.35559 ? 720  GLU   B CA   1 
ATOM   4909 C  C    . GLU   B 1 286 ? -36.95900 19.01700 61.89200 1.000 18.97425 ? 720  GLU   B C    1 
ATOM   4910 O  O    . GLU   B 1 286 ? -36.11900 19.15700 62.79000 1.000 12.33668 ? 720  GLU   B O    1 
ATOM   4911 C  CB   . GLU   B 1 286 ? -38.53700 17.08300 62.12300 1.000 11.69163 ? 720  GLU   B CB   1 
ATOM   4912 C  CG   . GLU   B 1 286 ? -39.88400 16.55200 62.58400 1.000 12.50231 ? 720  GLU   B CG   1 
ATOM   4913 C  CD   . GLU   B 1 286 ? -40.95400 16.63100 61.51100 1.000 13.66550 ? 720  GLU   B CD   1 
ATOM   4914 O  OE1  . GLU   B 1 286 ? -40.65700 17.09600 60.39400 1.000 16.49956 ? 720  GLU   B OE1  1 
ATOM   4915 O  OE2  . GLU   B 1 286 ? -42.09700 16.21800 61.78300 1.000 17.86064 ? 720  GLU   B OE2  1 
ATOM   4916 N  N    . GLY   B 1 287 ? -36.66500 19.20300 60.60100 1.000 11.22921 ? 721  GLY   B N    1 
ATOM   4917 C  CA   . GLY   B 1 287 ? -35.38300 19.76900 60.21900 1.000 11.04748 ? 721  GLY   B CA   1 
ATOM   4918 C  C    . GLY   B 1 287 ? -35.16700 21.15200 60.80200 1.000 12.27052 ? 721  GLY   B C    1 
ATOM   4919 O  O    . GLY   B 1 287 ? -34.08800 21.45700 61.31800 1.000 14.18117 ? 721  GLY   B O    1 
ATOM   4920 N  N    . TYR   B 1 288 ? -36.19600 22.00200 60.74400 1.000 10.49667 ? 722  TYR   B N    1 
ATOM   4921 C  CA   . TYR   B 1 288 ? -36.09700 23.32300 61.35600 1.000 11.46035 ? 722  TYR   B CA   1 
ATOM   4922 C  C    . TYR   B 1 288 ? -35.90700 23.22500 62.86100 1.000 18.44364 ? 722  TYR   B C    1 
ATOM   4923 O  O    . TYR   B 1 288 ? -35.21600 24.06200 63.45700 1.000 17.83561 ? 722  TYR   B O    1 
ATOM   4924 C  CB   . TYR   B 1 288 ? -37.33900 24.15300 61.03600 1.000 10.78513 ? 722  TYR   B CB   1 
ATOM   4925 C  CG   . TYR   B 1 288 ? -37.36200 24.69800 59.63200 1.000 9.86581  ? 722  TYR   B CG   1 
ATOM   4926 C  CD1  . TYR   B 1 288 ? -36.45700 25.67200 59.23400 1.000 9.75634  ? 722  TYR   B CD1  1 
ATOM   4927 C  CD2  . TYR   B 1 288 ? -38.29100 24.24600 58.70500 1.000 11.47831 ? 722  TYR   B CD2  1 
ATOM   4928 C  CE1  . TYR   B 1 288 ? -36.47100 26.17500 57.95100 1.000 9.64615  ? 722  TYR   B CE1  1 
ATOM   4929 C  CE2  . TYR   B 1 288 ? -38.31600 24.74200 57.42100 1.000 11.11783 ? 722  TYR   B CE2  1 
ATOM   4930 C  CZ   . TYR   B 1 288 ? -37.40400 25.70700 57.04700 1.000 9.65742  ? 722  TYR   B CZ   1 
ATOM   4931 O  OH   . TYR   B 1 288 ? -37.42900 26.20500 55.76400 1.000 14.24699 ? 722  TYR   B OH   1 
ATOM   4932 N  N    . ALA   B 1 289 ? -36.51500 22.21600 63.49100 1.000 15.93431 ? 723  ALA   B N    1 
ATOM   4933 C  CA   . ALA   B 1 289 ? -36.31800 22.00100 64.91800 1.000 10.86248 ? 723  ALA   B CA   1 
ATOM   4934 C  C    . ALA   B 1 289 ? -34.85200 21.73400 65.23400 1.000 16.67415 ? 723  ALA   B C    1 
ATOM   4935 O  O    . ALA   B 1 289 ? -34.30700 22.28300 66.19900 1.000 13.53586 ? 723  ALA   B O    1 
ATOM   4936 C  CB   . ALA   B 1 289 ? -37.19100 20.84400 65.40100 1.000 11.08612 ? 723  ALA   B CB   1 
ATOM   4937 N  N    A HIS   B 1 290 ? -34.19700 20.89100 64.43000 0.514 13.29420 ? 724  HIS   B N    1 
ATOM   4938 N  N    B HIS   B 1 290 ? -34.19100 20.89700 64.42600 0.486 13.29793 ? 724  HIS   B N    1 
ATOM   4939 C  CA   A HIS   B 1 290 ? -32.79800 20.56500 64.68400 0.514 12.84805 ? 724  HIS   B CA   1 
ATOM   4940 C  CA   B HIS   B 1 290 ? -32.79600 20.56500 64.69900 0.486 12.86003 ? 724  HIS   B CA   1 
ATOM   4941 C  C    A HIS   B 1 290 ? -31.89100 21.75800 64.42300 0.514 11.36935 ? 724  HIS   B C    1 
ATOM   4942 C  C    B HIS   B 1 290 ? -31.87900 21.75000 64.41600 0.486 11.37168 ? 724  HIS   B C    1 
ATOM   4943 O  O    A HIS   B 1 290 ? -30.94300 21.99900 65.17900 0.514 13.90167 ? 724  HIS   B O    1 
ATOM   4944 O  O    B HIS   B 1 290 ? -30.91400 21.97900 65.15400 0.486 13.87734 ? 724  HIS   B O    1 
ATOM   4945 C  CB   A HIS   B 1 290 ? -32.37300 19.36900 63.83400 0.514 14.21383 ? 724  HIS   B CB   1 
ATOM   4946 C  CB   B HIS   B 1 290 ? -32.36800 19.34200 63.88400 0.486 14.23088 ? 724  HIS   B CB   1 
ATOM   4947 C  CG   A HIS   B 1 290 ? -32.74500 18.05000 64.43100 0.514 12.08324 ? 724  HIS   B CG   1 
ATOM   4948 C  CG   B HIS   B 1 290 ? -31.37600 18.46400 64.58600 0.486 18.03978 ? 724  HIS   B CG   1 
ATOM   4949 N  ND1  A HIS   B 1 290 ? -31.81000 17.16900 64.92900 0.514 18.00541 ? 724  HIS   B ND1  1 
ATOM   4950 N  ND1  B HIS   B 1 290 ? -30.02400 18.73300 64.60500 0.486 18.08751 ? 724  HIS   B ND1  1 
ATOM   4951 C  CD2  A HIS   B 1 290 ? -33.95200 17.46900 64.62600 0.514 12.11616 ? 724  HIS   B CD2  1 
ATOM   4952 C  CD2  B HIS   B 1 290 ? -31.54000 17.32400 65.29800 0.486 18.07658 ? 724  HIS   B CD2  1 
ATOM   4953 C  CE1  A HIS   B 1 290 ? -32.42300 16.09800 65.39700 0.514 12.78266 ? 724  HIS   B CE1  1 
ATOM   4954 C  CE1  B HIS   B 1 290 ? -29.39800 17.79600 65.29300 0.486 12.77571 ? 724  HIS   B CE1  1 
ATOM   4955 N  NE2  A HIS   B 1 290 ? -33.72300 16.25400 65.22400 0.514 12.55522 ? 724  HIS   B NE2  1 
ATOM   4956 N  NE2  B HIS   B 1 290 ? -30.29500 16.92900 65.72700 0.486 12.91229 ? 724  HIS   B NE2  1 
ATOM   4957 N  N    . LEU   B 1 291 ? -32.16200 22.51600 63.35700 1.000 11.05395 ? 725  LEU   B N    1 
ATOM   4958 C  CA   . LEU   B 1 291 ? -31.38000 23.72100 63.09400 1.000 11.30792 ? 725  LEU   B CA   1 
ATOM   4959 C  C    . LEU   B 1 291 ? -31.49000 24.69800 64.25700 1.000 15.34534 ? 725  LEU   B C    1 
ATOM   4960 O  O    . LEU   B 1 291 ? -30.50400 25.34300 64.63700 1.000 14.24293 ? 725  LEU   B O    1 
ATOM   4961 C  CB   . LEU   B 1 291 ? -31.84200 24.39200 61.80000 1.000 13.28061 ? 725  LEU   B CB   1 
ATOM   4962 C  CG   . LEU   B 1 291 ? -31.80000 23.62400 60.47500 1.000 14.52047 ? 725  LEU   B CG   1 
ATOM   4963 C  CD1  . LEU   B 1 291 ? -32.08400 24.56800 59.31600 1.000 17.47046 ? 725  LEU   B CD1  1 
ATOM   4964 C  CD2  . LEU   B 1 291 ? -30.46900 22.91500 60.27600 1.000 16.75101 ? 725  LEU   B CD2  1 
ATOM   4965 N  N    . THR   B 1 292 ? -32.68600 24.80800 64.84000 1.000 11.95557 ? 726  THR   B N    1 
ATOM   4966 C  CA   . THR   B 1 292 ? -32.88700 25.65900 66.00600 1.000 10.88589 ? 726  THR   B CA   1 
ATOM   4967 C  C    . THR   B 1 292 ? -32.17100 25.10000 67.22800 1.000 11.98304 ? 726  THR   B C    1 
ATOM   4968 O  O    . THR   B 1 292 ? -31.53400 25.84700 67.97800 1.000 14.73116 ? 726  THR   B O    1 
ATOM   4969 C  CB   . THR   B 1 292 ? -34.38300 25.80200 66.29000 1.000 17.26872 ? 726  THR   B CB   1 
ATOM   4970 O  OG1  . THR   B 1 292 ? -35.01600 26.50300 65.21400 1.000 14.68365 ? 726  THR   B OG1  1 
ATOM   4971 C  CG2  . THR   B 1 292 ? -34.62200 26.55500 67.59100 1.000 10.84944 ? 726  THR   B CG2  1 
ATOM   4972 N  N    . HIS   B 1 293 ? -32.27200 23.78900 67.44900 1.000 11.48639 ? 727  HIS   B N    1 
ATOM   4973 C  CA   . HIS   B 1 293 ? -31.63200 23.18300 68.60900 1.000 11.92192 ? 727  HIS   B CA   1 
ATOM   4974 C  C    . HIS   B 1 293 ? -30.11400 23.30300 68.54100 1.000 19.00793 ? 727  HIS   B C    1 
ATOM   4975 O  O    . HIS   B 1 293 ? -29.44900 23.36500 69.58200 1.000 17.30753 ? 727  HIS   B O    1 
ATOM   4976 C  CB   . HIS   B 1 293 ? -32.04700 21.71700 68.72200 1.000 12.10728 ? 727  HIS   B CB   1 
ATOM   4977 C  CG   . HIS   B 1 293 ? -31.68500 21.08500 70.02900 1.000 19.55247 ? 727  HIS   B CG   1 
ATOM   4978 N  ND1  . HIS   B 1 293 ? -30.56300 20.30200 70.19400 1.000 28.27507 ? 727  HIS   B ND1  1 
ATOM   4979 C  CD2  . HIS   B 1 293 ? -32.30000 21.11900 71.23600 1.000 19.94350 ? 727  HIS   B CD2  1 
ATOM   4980 C  CE1  . HIS   B 1 293 ? -30.50300 19.87900 71.44500 1.000 26.80333 ? 727  HIS   B CE1  1 
ATOM   4981 N  NE2  . HIS   B 1 293 ? -31.54700 20.35800 72.09700 1.000 21.80407 ? 727  HIS   B NE2  1 
ATOM   4982 N  N    . GLN   B 1 294 ? -29.55000 23.33700 67.33000 1.000 12.01329 ? 728  GLN   B N    1 
ATOM   4983 C  CA   . GLN   B 1 294 ? -28.10800 23.50500 67.18900 1.000 12.25970 ? 728  GLN   B CA   1 
ATOM   4984 C  C    . GLN   B 1 294 ? -27.67700 24.93100 67.51700 1.000 12.25450 ? 728  GLN   B C    1 
ATOM   4985 O  O    . GLN   B 1 294 ? -26.66600 25.14000 68.19600 1.000 12.63130 ? 728  GLN   B O    1 
ATOM   4986 C  CB   . GLN   B 1 294 ? -27.67500 23.12200 65.77500 1.000 12.12741 ? 728  GLN   B CB   1 
ATOM   4987 C  CG   . GLN   B 1 294 ? -27.68900 21.61600 65.50500 1.000 12.32046 ? 728  GLN   B CG   1 
ATOM   4988 C  CD   . GLN   B 1 294 ? -27.24900 21.26800 64.09200 1.000 23.65265 ? 728  GLN   B CD   1 
ATOM   4989 O  OE1  . GLN   B 1 294 ? -26.37400 21.92300 63.52700 1.000 40.40639 ? 728  GLN   B OE1  1 
ATOM   4990 N  NE2  . GLN   B 1 294 ? -27.85800 20.23700 63.51200 1.000 17.60291 ? 728  GLN   B NE2  1 
ATOM   4991 N  N    . LEU   B 1 295 ? -28.42300 25.92800 67.04000 1.000 11.89067 ? 729  LEU   B N    1 
ATOM   4992 C  CA   . LEU   B 1 295 ? -28.06700 27.30800 67.33600 1.000 11.92233 ? 729  LEU   B CA   1 
ATOM   4993 C  C    . LEU   B 1 295 ? -28.23100 27.63800 68.81400 1.000 12.22564 ? 729  LEU   B C    1 
ATOM   4994 O  O    . LEU   B 1 295 ? -27.57400 28.56100 69.30500 1.000 12.47464 ? 729  LEU   B O    1 
ATOM   4995 C  CB   . LEU   B 1 295 ? -28.89900 28.25700 66.47500 1.000 11.49311 ? 729  LEU   B CB   1 
ATOM   4996 C  CG   . LEU   B 1 295 ? -28.63400 28.10000 64.97600 1.000 11.25665 ? 729  LEU   B CG   1 
ATOM   4997 C  CD1  . LEU   B 1 295 ? -29.74700 28.70900 64.15700 1.000 10.85061 ? 729  LEU   B CD1  1 
ATOM   4998 C  CD2  . LEU   B 1 295 ? -27.28100 28.71200 64.59900 1.000 11.45054 ? 729  LEU   B CD2  1 
ATOM   4999 N  N    . MET   B 1 296 ? -29.07000 26.89100 69.53600 1.000 15.24513 ? 730  MET   B N    1 
ATOM   5000 C  CA   . MET   B 1 296 ? -29.23800 27.12900 70.96600 1.000 12.73794 ? 730  MET   B CA   1 
ATOM   5001 C  C    . MET   B 1 296 ? -27.96900 26.84400 71.75900 1.000 13.16365 ? 730  MET   B C    1 
ATOM   5002 O  O    . MET   B 1 296 ? -27.82600 27.35000 72.87800 1.000 13.53439 ? 730  MET   B O    1 
ATOM   5003 C  CB   . MET   B 1 296 ? -30.39900 26.29200 71.50700 1.000 13.98700 ? 730  MET   B CB   1 
ATOM   5004 C  CG   . MET   B 1 296 ? -31.76900 26.82200 71.10500 1.000 12.14116 ? 730  MET   B CG   1 
ATOM   5005 S  SD   . MET   B 1 296 ? -33.11200 25.71700 71.56000 1.000 12.10914 ? 730  MET   B SD   1 
ATOM   5006 C  CE   . MET   B 1 296 ? -32.96300 25.69700 73.34300 1.000 12.66203 ? 730  MET   B CE   1 
ATOM   5007 N  N    . SER   B 1 297 ? -27.04300 26.05500 71.21700 1.000 13.27965 ? 731  SER   B N    1 
ATOM   5008 C  CA   . SER   B 1 297 ? -25.78400 25.85200 71.92500 1.000 20.53745 ? 731  SER   B CA   1 
ATOM   5009 C  C    . SER   B 1 297 ? -24.85900 27.06100 71.84000 1.000 17.01265 ? 731  SER   B C    1 
ATOM   5010 O  O    . SER   B 1 297 ? -23.75500 27.01500 72.39300 1.000 14.78298 ? 731  SER   B O    1 
ATOM   5011 C  CB   . SER   B 1 297 ? -25.06700 24.60900 71.39100 1.000 13.97738 ? 731  SER   B CB   1 
ATOM   5012 O  OG   . SER   B 1 297 ? -24.67200 24.78400 70.04400 1.000 13.67582 ? 731  SER   B OG   1 
ATOM   5013 N  N    . LEU   B 1 298 ? -25.28600 28.13500 71.18000 1.000 13.64468 ? 732  LEU   B N    1 
ATOM   5014 C  CA   . LEU   B 1 298 ? -24.48000 29.33200 71.00300 1.000 14.78939 ? 732  LEU   B CA   1 
ATOM   5015 C  C    . LEU   B 1 298 ? -24.96500 30.45700 71.91000 1.000 15.10534 ? 732  LEU   B C    1 
ATOM   5016 O  O    . LEU   B 1 298 ? -26.14700 30.53400 72.25900 1.000 14.00437 ? 732  LEU   B O    1 
ATOM   5017 C  CB   . LEU   B 1 298 ? -24.52500 29.79900 69.54800 1.000 13.34409 ? 732  LEU   B CB   1 
ATOM   5018 C  CG   . LEU   B 1 298 ? -24.11700 28.75700 68.51100 1.000 13.17893 ? 732  LEU   B CG   1 
ATOM   5019 C  CD1  . LEU   B 1 298 ? -24.43200 29.25000 67.11100 1.000 12.71139 ? 732  LEU   B CD1  1 
ATOM   5020 C  CD2  . LEU   B 1 298 ? -22.63200 28.44300 68.66000 1.000 15.54100 ? 732  LEU   B CD2  1 
ATOM   5021 N  N    . ALA   B 1 299 ? -24.03000 31.33100 72.28800 1.000 14.49722 ? 733  ALA   B N    1 
ATOM   5022 C  CA   . ALA   B 1 299 ? -24.34300 32.58700 72.97200 1.000 16.37397 ? 733  ALA   B CA   1 
ATOM   5023 C  C    . ALA   B 1 299 ? -25.12000 32.35400 74.26300 1.000 15.29913 ? 733  ALA   B C    1 
ATOM   5024 O  O    . ALA   B 1 299 ? -25.99300 33.14200 74.62900 1.000 19.08736 ? 733  ALA   B O    1 
ATOM   5025 C  CB   . ALA   B 1 299 ? -25.10900 33.53500 72.04500 1.000 14.13099 ? 733  ALA   B CB   1 
ATOM   5026 N  N    . ALA   B 1 300 ? -24.80400 31.25500 74.95200 1.000 15.17321 ? 734  ALA   B N    1 
ATOM   5027 C  CA   . ALA   B 1 300 ? -25.47100 30.88100 76.20200 1.000 15.45700 ? 734  ALA   B CA   1 
ATOM   5028 C  C    . ALA   B 1 300 ? -26.98400 30.78500 76.02400 1.000 14.92694 ? 734  ALA   B C    1 
ATOM   5029 O  O    . ALA   B 1 300 ? -27.74800 30.99900 76.96600 1.000 17.53076 ? 734  ALA   B O    1 
ATOM   5030 C  CB   . ALA   B 1 300 ? -25.12100 31.84900 77.33800 1.000 16.11274 ? 734  ALA   B CB   1 
ATOM   5031 N  N    . GLY   B 1 301 ? -27.42400 30.46900 74.80800 1.000 15.25280 ? 735  GLY   B N    1 
ATOM   5032 C  CA   . GLY   B 1 301 ? -28.83100 30.30800 74.51700 1.000 13.82617 ? 735  GLY   B CA   1 
ATOM   5033 C  C    . GLY   B 1 301 ? -29.55400 31.56100 74.07400 1.000 13.52184 ? 735  GLY   B C    1 
ATOM   5034 O  O    . GLY   B 1 301 ? -30.76800 31.49900 73.83300 1.000 13.14630 ? 735  GLY   B O    1 
ATOM   5035 N  N    . ARG   B 1 302 ? -28.85800 32.69400 73.96100 1.000 13.71428 ? 736  ARG   B N    1 
ATOM   5036 C  CA   . ARG   B 1 302 ? -29.47900 33.93000 73.50200 1.000 13.47944 ? 736  ARG   B CA   1 
ATOM   5037 C  C    . ARG   B 1 302 ? -29.80500 33.84100 72.01700 1.000 13.71098 ? 736  ARG   B C    1 
ATOM   5038 O  O    . ARG   B 1 302 ? -28.96600 34.18300 71.17800 1.000 12.82799 ? 736  ARG   B O    1 
ATOM   5039 C  CB   . ARG   B 1 302 ? -28.56200 35.12900 73.75900 1.000 13.92571 ? 736  ARG   B CB   1 
ATOM   5040 C  CG   . ARG   B 1 302 ? -28.16600 35.34500 75.21700 1.000 14.62907 ? 736  ARG   B CG   1 
ATOM   5041 C  CD   . ARG   B 1 302 ? -27.40300 36.65400 75.36900 1.000 15.08376 ? 736  ARG   B CD   1 
ATOM   5042 N  NE   . ARG   B 1 302 ? -26.81300 36.82300 76.69100 1.000 17.73184 ? 736  ARG   B NE   1 
ATOM   5043 C  CZ   . ARG   B 1 302 ? -25.52600 36.65900 76.96500 1.000 26.33377 ? 736  ARG   B CZ   1 
ATOM   5044 N  NH1  . ARG   B 1 302 ? -24.65700 36.31200 76.02900 1.000 25.25092 ? 736  ARG   B NH1  1 
ATOM   5045 N  NH2  . ARG   B 1 302 ? -25.09800 36.85400 78.21000 1.000 25.28529 ? 736  ARG   B NH2  1 
ATOM   5046 N  N    . VAL   B 1 303 ? -31.01000 33.38500 71.67800 1.000 12.45757 ? 737  VAL   B N    1 
ATOM   5047 C  CA   . VAL   B 1 303 ? -31.41900 33.19900 70.29000 1.000 11.93354 ? 737  VAL   B CA   1 
ATOM   5048 C  C    . VAL   B 1 303 ? -32.74800 33.91000 70.06600 1.000 11.67678 ? 737  VAL   B C    1 
ATOM   5049 O  O    . VAL   B 1 303 ? -33.74800 33.58200 70.71300 1.000 17.27366 ? 737  VAL   B O    1 
ATOM   5050 C  CB   . VAL   B 1 303 ? -31.53700 31.71300 69.92000 1.000 11.74874 ? 737  VAL   B CB   1 
ATOM   5051 C  CG1  . VAL   B 1 303 ? -32.11500 31.56700 68.53000 1.000 12.25023 ? 737  VAL   B CG1  1 
ATOM   5052 C  CG2  . VAL   B 1 303 ? -30.17400 31.03600 70.01300 1.000 12.04770 ? 737  VAL   B CG2  1 
ATOM   5053 N  N    . LEU   B 1 304 ? -32.75700 34.83700 69.11900 1.000 14.84131 ? 738  LEU   B N    1 
ATOM   5054 C  CA   . LEU   B 1 304 ? -33.96900 35.57100 68.69800 1.000 14.65156 ? 738  LEU   B CA   1 
ATOM   5055 C  C    . LEU   B 1 304 ? -34.33700 35.07900 67.27900 1.000 14.10034 ? 738  LEU   B C    1 
ATOM   5056 O  O    . LEU   B 1 304 ? -33.57300 35.35800 66.34600 1.000 15.03382 ? 738  LEU   B O    1 
ATOM   5057 C  CB   . LEU   B 1 304 ? -33.73600 37.07300 68.73900 1.000 11.37133 ? 738  LEU   B CB   1 
ATOM   5058 C  CG   . LEU   B 1 304 ? -34.80500 37.96900 68.10400 1.000 11.12975 ? 738  LEU   B CG   1 
ATOM   5059 C  CD1  . LEU   B 1 304 ? -36.17700 37.69500 68.66400 1.000 11.03455 ? 738  LEU   B CD1  1 
ATOM   5060 C  CD2  . LEU   B 1 304 ? -34.46100 39.43600 68.24700 1.000 11.42780 ? 738  LEU   B CD2  1 
ATOM   5061 N  N    . ILE   B 1 305 ? -35.42100 34.32300 67.18000 1.000 17.53240 ? 739  ILE   B N    1 
ATOM   5062 C  CA   . ILE   B 1 305 ? -35.92400 33.83000 65.85700 1.000 16.54559 ? 739  ILE   B CA   1 
ATOM   5063 C  C    . ILE   B 1 305 ? -36.87300 34.87500 65.24800 1.000 11.42358 ? 739  ILE   B C    1 
ATOM   5064 O  O    . ILE   B 1 305 ? -37.93500 35.15300 65.81400 1.000 13.50246 ? 739  ILE   B O    1 
ATOM   5065 C  CB   . ILE   B 1 305 ? -36.56700 32.43500 65.96800 1.000 10.04419 ? 739  ILE   B CB   1 
ATOM   5066 C  CG1  . ILE   B 1 305 ? -35.54000 31.36900 66.33200 1.000 17.59045 ? 739  ILE   B CG1  1 
ATOM   5067 C  CG2  . ILE   B 1 305 ? -37.33000 32.08200 64.69500 1.000 9.74057  ? 739  ILE   B CG2  1 
ATOM   5068 C  CD1  . ILE   B 1 305 ? -35.35000 30.30100 65.27200 1.000 15.53732 ? 739  ILE   B CD1  1 
ATOM   5069 N  N    . ILE   B 1 306 ? -36.51200 35.36000 64.09200 1.000 14.19136 ? 740  ILE   B N    1 
ATOM   5070 C  CA   . ILE   B 1 306 ? -37.31300 36.41500 63.43400 1.000 14.39607 ? 740  ILE   B CA   1 
ATOM   5071 C  C    . ILE   B 1 306 ? -37.90900 35.87600 62.12500 1.000 11.53707 ? 740  ILE   B C    1 
ATOM   5072 O  O    . ILE   B 1 306 ? -37.14400 35.54700 61.21600 1.000 9.34864  ? 740  ILE   B O    1 
ATOM   5073 C  CB   . ILE   B 1 306 ? -36.42600 37.65100 63.22400 1.000 12.49831 ? 740  ILE   B CB   1 
ATOM   5074 C  CG1  . ILE   B 1 306 ? -35.89900 38.18000 64.55300 1.000 14.10718 ? 740  ILE   B CG1  1 
ATOM   5075 C  CG2  . ILE   B 1 306 ? -37.15100 38.73600 62.42800 1.000 15.42266 ? 740  ILE   B CG2  1 
ATOM   5076 C  CD1  . ILE   B 1 306 ? -34.90900 39.31900 64.41600 1.000 15.29642 ? 740  ILE   B CD1  1 
ATOM   5077 N  N    . LEU   B 1 307 ? -39.23800 35.82500 62.05900 1.000 11.25608 ? 741  LEU   B N    1 
ATOM   5078 C  CA   . LEU   B 1 307 ? -39.91600 35.38200 60.81800 1.000 9.36203  ? 741  LEU   B CA   1 
ATOM   5079 C  C    . LEU   B 1 307 ? -39.48200 36.26900 59.65100 1.000 11.58844 ? 741  LEU   B C    1 
ATOM   5080 O  O    . LEU   B 1 307 ? -39.54300 37.49900 59.78500 1.000 12.70993 ? 741  LEU   B O    1 
ATOM   5081 C  CB   . LEU   B 1 307 ? -41.43700 35.38500 60.94000 1.000 9.05273  ? 741  LEU   B CB   1 
ATOM   5082 C  CG   . LEU   B 1 307 ? -42.23700 34.94000 59.71600 1.000 9.87407  ? 741  LEU   B CG   1 
ATOM   5083 C  CD1  . LEU   B 1 307 ? -42.13300 33.44100 59.55700 1.000 8.92284  ? 741  LEU   B CD1  1 
ATOM   5084 C  CD2  . LEU   B 1 307 ? -43.68300 35.36900 59.89300 1.000 8.94719  ? 741  LEU   B CD2  1 
ATOM   5085 N  N    . GLU   B 1 308 ? -39.05000 35.66900 58.55700 1.000 8.98815  ? 742  GLU   B N    1 
ATOM   5086 C  CA   . GLU   B 1 308 ? -38.77800 36.47600 57.34400 1.000 9.63293  ? 742  GLU   B CA   1 
ATOM   5087 C  C    . GLU   B 1 308 ? -39.83500 36.05000 56.30700 1.000 14.19946 ? 742  GLU   B C    1 
ATOM   5088 O  O    . GLU   B 1 308 ? -41.00400 36.33800 56.50400 1.000 8.86536  ? 742  GLU   B O    1 
ATOM   5089 C  CB   . GLU   B 1 308 ? -37.33300 36.26300 56.89900 1.000 9.61628  ? 742  GLU   B CB   1 
ATOM   5090 C  CG   . GLU   B 1 308 ? -36.30700 36.89800 57.83000 1.000 9.73804  ? 742  GLU   B CG   1 
ATOM   5091 C  CD   . GLU   B 1 308 ? -35.98000 38.33800 57.48100 1.000 12.95889 ? 742  GLU   B CD   1 
ATOM   5092 O  OE1  . GLU   B 1 308 ? -36.71700 38.94700 56.69300 1.000 9.82303  ? 742  GLU   B OE1  1 
ATOM   5093 O  OE2  . GLU   B 1 308 ? -34.98200 38.84200 58.01600 1.000 12.55135 ? 742  GLU   B OE2  1 
ATOM   5094 N  N    . GLY   B 1 309 ? -39.40100 35.29500 55.28700 1.000 14.14254 ? 743  GLY   B N    1 
ATOM   5095 C  CA   . GLY   B 1 309 ? -40.34500 34.78200 54.27700 1.000 8.87414  ? 743  GLY   B CA   1 
ATOM   5096 C  C    . GLY   B 1 309 ? -41.06500 33.53000 54.72700 1.000 8.98739  ? 743  GLY   B C    1 
ATOM   5097 O  O    . GLY   B 1 309 ? -41.09600 33.25800 55.92800 1.000 11.08647 ? 743  GLY   B O    1 
ATOM   5098 N  N    . GLY   B 1 310 ? -41.59300 32.76400 53.77600 1.000 8.94538  ? 744  GLY   B N    1 
ATOM   5099 C  CA   . GLY   B 1 310 ? -42.39700 31.58800 54.13200 1.000 9.00822  ? 744  GLY   B CA   1 
ATOM   5100 C  C    . GLY   B 1 310 ? -43.80600 31.86300 53.66000 1.000 14.61381 ? 744  GLY   B C    1 
ATOM   5101 O  O    . GLY   B 1 310 ? -44.45800 32.71600 54.27100 1.000 9.00138  ? 744  GLY   B O    1 
ATOM   5102 N  N    . TYR   B 1 311 ? -44.25900 31.17800 52.58700 1.000 9.22666  ? 745  TYR   B N    1 
ATOM   5103 C  CA   . TYR   B 1 311 ? -45.54400 31.53900 51.91300 1.000 11.98382 ? 745  TYR   B CA   1 
ATOM   5104 C  C    . TYR   B 1 311 ? -46.58700 30.42300 51.94000 1.000 17.96995 ? 745  TYR   B C    1 
ATOM   5105 O  O    . TYR   B 1 311 ? -47.75000 30.67900 51.64100 1.000 17.41519 ? 745  TYR   B O    1 
ATOM   5106 C  CB   . TYR   B 1 311 ? -45.07400 32.05600 50.55100 1.000 17.23534 ? 745  TYR   B CB   1 
ATOM   5107 C  CG   . TYR   B 1 311 ? -44.14500 33.24300 50.75000 1.000 9.66813  ? 745  TYR   B CG   1 
ATOM   5108 C  CD1  . TYR   B 1 311 ? -44.64800 34.47300 51.15300 1.000 10.36381 ? 745  TYR   B CD1  1 
ATOM   5109 C  CD2  . TYR   B 1 311 ? -42.77000 33.11700 50.60300 1.000 9.87532  ? 745  TYR   B CD2  1 
ATOM   5110 C  CE1  . TYR   B 1 311 ? -43.81800 35.55800 51.36400 1.000 11.43875 ? 745  TYR   B CE1  1 
ATOM   5111 C  CE2  . TYR   B 1 311 ? -41.92800 34.19300 50.81200 1.000 9.12244  ? 745  TYR   B CE2  1 
ATOM   5112 C  CZ   . TYR   B 1 311 ? -42.45300 35.41400 51.19400 1.000 12.30630 ? 745  TYR   B CZ   1 
ATOM   5113 O  OH   . TYR   B 1 311 ? -41.63500 36.47500 51.41100 1.000 10.11348 ? 745  TYR   B OH   1 
ATOM   5114 N  N    . ASN   B 1 312 ? -46.16200 29.20100 52.25000 1.000 14.00683 ? 746  ASN   B N    1 
ATOM   5115 C  CA   . ASN   B 1 312 ? -47.17200 28.16800 52.47700 1.000 13.44153 ? 746  ASN   B CA   1 
ATOM   5116 C  C    . ASN   B 1 312 ? -47.68600 28.32000 53.90300 1.000 18.62680 ? 746  ASN   B C    1 
ATOM   5117 O  O    . ASN   B 1 312 ? -46.92700 28.12800 54.86000 1.000 12.96224 ? 746  ASN   B O    1 
ATOM   5118 C  CB   . ASN   B 1 312 ? -46.60600 26.76200 52.26500 1.000 12.42709 ? 746  ASN   B CB   1 
ATOM   5119 C  CG   . ASN   B 1 312 ? -47.68000 25.67200 52.35400 1.000 23.06796 ? 746  ASN   B CG   1 
ATOM   5120 O  OD1  . ASN   B 1 312 ? -48.29700 25.46300 53.40100 1.000 13.03284 ? 746  ASN   B OD1  1 
ATOM   5121 N  ND2  . ASN   B 1 312 ? -47.89200 24.96600 51.24800 1.000 20.68108 ? 746  ASN   B ND2  1 
ATOM   5122 N  N    . LEU   B 1 313 ? -48.97300 28.65700 54.04400 1.000 13.34520 ? 747  LEU   B N    1 
ATOM   5123 C  CA   . LEU   B 1 313 ? -49.51100 29.01300 55.35500 1.000 11.90602 ? 747  LEU   B CA   1 
ATOM   5124 C  C    . LEU   B 1 313 ? -49.39200 27.85900 56.34300 1.000 10.95448 ? 747  LEU   B C    1 
ATOM   5125 O  O    . LEU   B 1 313 ? -49.00900 28.06100 57.50100 1.000 15.13070 ? 747  LEU   B O    1 
ATOM   5126 C  CB   . LEU   B 1 313 ? -50.96700 29.45800 55.22000 1.000 15.27062 ? 747  LEU   B CB   1 
ATOM   5127 C  CG   . LEU   B 1 313 ? -51.22100 30.73500 54.41500 1.000 13.84229 ? 747  LEU   B CG   1 
ATOM   5128 C  CD1  . LEU   B 1 313 ? -52.71300 31.00300 54.30900 1.000 20.73476 ? 747  LEU   B CD1  1 
ATOM   5129 C  CD2  . LEU   B 1 313 ? -50.51000 31.92300 55.02800 1.000 9.54202  ? 747  LEU   B CD2  1 
ATOM   5130 N  N    . THR   B 1 314 ? -49.71300 26.64200 55.90600 1.000 15.10053 ? 748  THR   B N    1 
ATOM   5131 C  CA   . THR   B 1 314 ? -49.58600 25.48600 56.78600 1.000 14.58243 ? 748  THR   B CA   1 
ATOM   5132 C  C    . THR   B 1 314 ? -48.12500 25.20800 57.12200 1.000 17.17679 ? 748  THR   B C    1 
ATOM   5133 O  O    . THR   B 1 314 ? -47.77200 25.02900 58.29300 1.000 12.90330 ? 748  THR   B O    1 
ATOM   5134 C  CB   . THR   B 1 314 ? -50.22200 24.25600 56.13800 1.000 13.78455 ? 748  THR   B CB   1 
ATOM   5135 O  OG1  . THR   B 1 314 ? -51.60700 24.51200 55.87900 1.000 19.84725 ? 748  THR   B OG1  1 
ATOM   5136 C  CG2  . THR   B 1 314 ? -50.09500 23.04800 57.05300 1.000 17.03432 ? 748  THR   B CG2  1 
ATOM   5137 N  N    . SER   B 1 315 ? -47.27600 25.15500 56.09000 1.000 12.40698 ? 749  SER   B N    1 
ATOM   5138 C  CA   . SER   B 1 315 ? -45.84100 24.81400 56.29800 1.000 16.24673 ? 749  SER   B CA   1 
ATOM   5139 C  C    . SER   B 1 315 ? -45.17600 25.80400 57.28100 1.000 11.24575 ? 749  SER   B C    1 
ATOM   5140 O  O    . SER   B 1 315 ? -44.49400 25.33900 58.19000 1.000 10.39474 ? 749  SER   B O    1 
ATOM   5141 C  CB   . SER   B 1 315 ? -45.05700 24.60400 54.96600 1.000 10.91155 ? 749  SER   B CB   1 
ATOM   5142 O  OG   . SER   B 1 315 ? -45.63300 23.59000 54.16000 1.000 18.98027 ? 749  SER   B OG   1 
ATOM   5143 N  N    . ILE   B 1 316 ? -45.43300 27.10100 57.13900 1.000 11.77316 ? 750  ILE   B N    1 
ATOM   5144 C  CA   . ILE   B 1 316 ? -44.78400 28.06300 58.02600 1.000 9.30893  ? 750  ILE   B CA   1 
ATOM   5145 C  C    . ILE   B 1 316 ? -45.36400 27.99000 59.43400 1.000 15.11482 ? 750  ILE   B C    1 
ATOM   5146 O  O    . ILE   B 1 316 ? -44.66300 28.27600 60.41500 1.000 10.91034 ? 750  ILE   B O    1 
ATOM   5147 C  CB   . ILE   B 1 316 ? -44.87400 29.49100 57.45400 1.000 9.15758  ? 750  ILE   B CB   1 
ATOM   5148 C  CG1  . ILE   B 1 316 ? -46.31200 30.00800 57.47900 1.000 11.31849 ? 750  ILE   B CG1  1 
ATOM   5149 C  CG2  . ILE   B 1 316 ? -44.32100 29.53500 56.04900 1.000 9.16396  ? 750  ILE   B CG2  1 
ATOM   5150 C  CD1  . ILE   B 1 316 ? -46.44900 31.42700 56.95300 1.000 13.55296 ? 750  ILE   B CD1  1 
ATOM   5151 N  N    . SER   B 1 317 ? -46.63600 27.60700 59.56700 1.000 9.47063  ? 751  SER   B N    1 
ATOM   5152 C  CA   . SER   B 1 317 ? -47.21100 27.41800 60.89400 1.000 15.09530 ? 751  SER   B CA   1 
ATOM   5153 C  C    . SER   B 1 317 ? -46.54600 26.25200 61.61000 1.000 18.29569 ? 751  SER   B C    1 
ATOM   5154 O  O    . SER   B 1 317 ? -46.08600 26.38800 62.75100 1.000 15.99713 ? 751  SER   B O    1 
ATOM   5155 C  CB   . SER   B 1 317 ? -48.72000 27.19000 60.79000 1.000 11.15155 ? 751  SER   B CB   1 
ATOM   5156 O  OG   . SER   B 1 317 ? -49.35500 28.31300 60.21200 1.000 12.37117 ? 751  SER   B OG   1 
ATOM   5157 N  N    . GLU   B 1 318 ? -46.48300 25.09600 60.94500 1.000 13.56962 ? 752  GLU   B N    1 
ATOM   5158 C  CA   . GLU   B 1 318 ? -45.87400 23.91400 61.54400 1.000 13.51125 ? 752  GLU   B CA   1 
ATOM   5159 C  C    . GLU   B 1 318 ? -44.39500 24.13600 61.82900 1.000 12.11742 ? 752  GLU   B C    1 
ATOM   5160 O  O    . GLU   B 1 318 ? -43.88500 23.71300 62.87300 1.000 16.06023 ? 752  GLU   B O    1 
ATOM   5161 C  CB   . GLU   B 1 318 ? -46.06000 22.71300 60.61700 1.000 13.14493 ? 752  GLU   B CB   1 
ATOM   5162 C  CG   . GLU   B 1 318 ? -46.36200 21.42600 61.33900 1.000 20.31271 ? 752  GLU   B CG   1 
ATOM   5163 C  CD   . GLU   B 1 318 ? -47.68500 21.48100 62.05300 1.000 15.44758 ? 752  GLU   B CD   1 
ATOM   5164 O  OE1  . GLU   B 1 318 ? -48.72000 21.56900 61.36500 1.000 15.26472 ? 752  GLU   B OE1  1 
ATOM   5165 O  OE2  . GLU   B 1 318 ? -47.69000 21.44800 63.30000 1.000 20.04066 ? 752  GLU   B OE2  1 
ATOM   5166 N  N    . SER   B 1 319 ? -43.68900 24.80200 60.91400 1.000 12.11085 ? 753  SER   B N    1 
ATOM   5167 C  CA   . SER   B 1 319 ? -42.23700 24.90400 61.02700 1.000 11.13679 ? 753  SER   B CA   1 
ATOM   5168 C  C    . SER   B 1 319 ? -41.82900 25.84800 62.15100 1.000 11.78045 ? 753  SER   B C    1 
ATOM   5169 O  O    . SER   B 1 319 ? -40.96700 25.51300 62.97100 1.000 12.30370 ? 753  SER   B O    1 
ATOM   5170 C  CB   . SER   B 1 319 ? -41.63800 25.35600 59.69500 1.000 9.66965  ? 753  SER   B CB   1 
ATOM   5171 O  OG   . SER   B 1 319 ? -41.74900 24.33400 58.71700 1.000 9.97734  ? 753  SER   B OG   1 
ATOM   5172 N  N    . MET   B 1 320 ? -42.42900 27.04000 62.20000 1.000 13.15818 ? 754  MET   B N    1 
ATOM   5173 C  CA   . MET   B 1 320 ? -42.06200 27.98900 63.24300 1.000 13.83791 ? 754  MET   B CA   1 
ATOM   5174 C  C    . MET   B 1 320 ? -42.50400 27.50600 64.61500 1.000 14.80313 ? 754  MET   B C    1 
ATOM   5175 O  O    . MET   B 1 320 ? -41.81900 27.77100 65.60900 1.000 13.17551 ? 754  MET   B O    1 
ATOM   5176 C  CB   . MET   B 1 320 ? -42.65100 29.36400 62.94600 1.000 9.41309  ? 754  MET   B CB   1 
ATOM   5177 C  CG   . MET   B 1 320 ? -41.98900 30.48800 63.72100 1.000 12.76716 ? 754  MET   B CG   1 
ATOM   5178 S  SD   . MET   B 1 320 ? -42.51200 32.11100 63.13800 1.000 17.43588 ? 754  MET   B SD   1 
ATOM   5179 C  CE   . MET   B 1 320 ? -41.19700 33.13700 63.78000 1.000 9.33810  ? 754  MET   B CE   1 
ATOM   5180 N  N    . SER   B 1 321 ? -43.63900 26.80400 64.69400 1.000 13.20732 ? 755  SER   B N    1 
ATOM   5181 C  CA   A SER   B 1 321 ? -44.04100 26.18600 65.95500 0.887 13.84938 ? 755  SER   B CA   1 
ATOM   5182 C  CA   B SER   B 1 321 ? -44.02600 26.21000 65.96800 0.113 13.83859 ? 755  SER   B CA   1 
ATOM   5183 C  C    . SER   B 1 321 ? -42.99700 25.18100 66.42000 1.000 16.33216 ? 755  SER   B C    1 
ATOM   5184 O  O    . SER   B 1 321 ? -42.73500 25.04800 67.62000 1.000 26.50416 ? 755  SER   B O    1 
ATOM   5185 C  CB   A SER   B 1 321 ? -45.40200 25.50000 65.80300 0.887 10.10005 ? 755  SER   B CB   1 
ATOM   5186 C  CB   B SER   B 1 321 ? -45.41600 25.58300 65.86500 0.113 10.09605 ? 755  SER   B CB   1 
ATOM   5187 O  OG   A SER   B 1 321 ? -46.45300 26.43700 65.64200 0.887 9.98886  ? 755  SER   B OG   1 
ATOM   5188 O  OG   B SER   B 1 321 ? -45.41100 24.44700 65.02200 0.113 13.13834 ? 755  SER   B OG   1 
ATOM   5189 N  N    . MET   B 1 322 ? -42.39600 24.45700 65.47400 1.000 15.14672 ? 756  MET   B N    1 
ATOM   5190 C  CA   . MET   B 1 322 ? -41.35400 23.49900 65.82500 1.000 19.80830 ? 756  MET   B CA   1 
ATOM   5191 C  C    . MET   B 1 322 ? -40.14700 24.19800 66.43400 1.000 13.34030 ? 756  MET   B C    1 
ATOM   5192 O  O    . MET   B 1 322 ? -39.54400 23.69500 67.38800 1.000 15.24998 ? 756  MET   B O    1 
ATOM   5193 C  CB   . MET   B 1 322 ? -40.94200 22.69900 64.59000 1.000 16.59989 ? 756  MET   B CB   1 
ATOM   5194 C  CG   . MET   B 1 322 ? -41.70300 21.40000 64.39800 1.000 19.35754 ? 756  MET   B CG   1 
ATOM   5195 S  SD   . MET   B 1 322 ? -41.22600 20.14000 65.59300 1.000 30.48037 ? 756  MET   B SD   1 
ATOM   5196 C  CE   . MET   B 1 322 ? -42.67600 20.09600 66.64300 1.000 23.38989 ? 756  MET   B CE   1 
ATOM   5197 N  N    . CYS   B 1 323 ? -39.78200 25.36400 65.89800 1.000 12.99046 ? 757  CYS   B N    1 
ATOM   5198 C  CA   . CYS   B 1 323 ? -38.63900 26.09800 66.43200 1.000 14.96339 ? 757  CYS   B CA   1 
ATOM   5199 C  C    . CYS   B 1 323 ? -38.92700 26.62200 67.83400 1.000 21.27049 ? 757  CYS   B C    1 
ATOM   5200 O  O    . CYS   B 1 323 ? -38.08100 26.52100 68.72900 1.000 16.12301 ? 757  CYS   B O    1 
ATOM   5201 C  CB   . CYS   B 1 323 ? -38.26700 27.24700 65.49500 1.000 13.68630 ? 757  CYS   B CB   1 
ATOM   5202 S  SG   . CYS   B 1 323 ? -37.79400 26.71600 63.84400 1.000 9.89425  ? 757  CYS   B SG   1 
ATOM   5203 N  N    . THR   B 1 324 ? -40.11400 27.20300 68.03700 1.000 15.86504 ? 758  THR   B N    1 
ATOM   5204 C  CA   . THR   B 1 324 ? -40.48900 27.67400 69.36800 1.000 11.23070 ? 758  THR   B CA   1 
ATOM   5205 C  C    . THR   B 1 324 ? -40.49600 26.52800 70.37100 1.000 10.86364 ? 758  THR   B C    1 
ATOM   5206 O  O    . THR   B 1 324 ? -40.04500 26.68600 71.51000 1.000 13.05936 ? 758  THR   B O    1 
ATOM   5207 C  CB   . THR   B 1 324 ? -41.85700 28.35100 69.31900 1.000 12.05777 ? 758  THR   B CB   1 
ATOM   5208 O  OG1  . THR   B 1 324 ? -41.83700 29.39600 68.34000 1.000 18.50910 ? 758  THR   B OG1  1 
ATOM   5209 C  CG2  . THR   B 1 324 ? -42.20700 28.94100 70.67800 1.000 11.34858 ? 758  THR   B CG2  1 
ATOM   5210 N  N    . SER   B 1 325 ? -40.99500 25.36100 69.95500 1.000 19.08312 ? 759  SER   B N    1 
ATOM   5211 C  CA   . SER   B 1 325 ? -40.93000 24.17200 70.79700 1.000 18.42984 ? 759  SER   B CA   1 
ATOM   5212 C  C    . SER   B 1 325 ? -39.50100 23.87400 71.23200 1.000 17.79392 ? 759  SER   B C    1 
ATOM   5213 O  O    . SER   B 1 325 ? -39.26400 23.47600 72.37800 1.000 20.09083 ? 759  SER   B O    1 
ATOM   5214 C  CB   . SER   B 1 325 ? -41.51900 22.97400 70.05100 1.000 11.19759 ? 759  SER   B CB   1 
ATOM   5215 O  OG   . SER   B 1 325 ? -41.23600 21.76200 70.72700 1.000 11.55948 ? 759  SER   B OG   1 
ATOM   5216 N  N    . MET   B 1 326 ? -38.53400 24.06100 70.32900 1.000 15.84523 ? 760  MET   B N    1 
ATOM   5217 C  CA   . MET   B 1 326 ? -37.14100 23.82100 70.69100 1.000 12.14230 ? 760  MET   B CA   1 
ATOM   5218 C  C    . MET   B 1 326 ? -36.63000 24.88600 71.65100 1.000 13.27045 ? 760  MET   B C    1 
ATOM   5219 O  O    . MET   B 1 326 ? -35.91300 24.57000 72.60700 1.000 18.91797 ? 760  MET   B O    1 
ATOM   5220 C  CB   . MET   B 1 326 ? -36.26600 23.76700 69.43900 1.000 11.35527 ? 760  MET   B CB   1 
ATOM   5221 C  CG   . MET   B 1 326 ? -36.50100 22.55800 68.54300 1.000 11.32998 ? 760  MET   B CG   1 
ATOM   5222 S  SD   . MET   B 1 326 ? -36.41200 20.96000 69.38200 1.000 11.79382 ? 760  MET   B SD   1 
ATOM   5223 C  CE   . MET   B 1 326 ? -38.15400 20.59100 69.60300 1.000 13.15362 ? 760  MET   B CE   1 
ATOM   5224 N  N    . LEU   B 1 327 ? -36.98500 26.15400 71.41300 1.000 20.07762 ? 761  LEU   B N    1 
ATOM   5225 C  CA   . LEU   B 1 327 ? -36.58400 27.22200 72.32600 1.000 14.22546 ? 761  LEU   B CA   1 
ATOM   5226 C  C    . LEU   B 1 327 ? -37.09600 26.96300 73.73700 1.000 15.73610 ? 761  LEU   B C    1 
ATOM   5227 O  O    . LEU   B 1 327 ? -36.43200 27.30900 74.72100 1.000 12.43485 ? 761  LEU   B O    1 
ATOM   5228 C  CB   . LEU   B 1 327 ? -37.09300 28.57500 71.82300 1.000 14.31655 ? 761  LEU   B CB   1 
ATOM   5229 C  CG   . LEU   B 1 327 ? -36.66300 29.08600 70.44700 1.000 12.77253 ? 761  LEU   B CG   1 
ATOM   5230 C  CD1  . LEU   B 1 327 ? -37.24300 30.47100 70.20600 1.000 10.91212 ? 761  LEU   B CD1  1 
ATOM   5231 C  CD2  . LEU   B 1 327 ? -35.14700 29.11300 70.31000 1.000 13.76516 ? 761  LEU   B CD2  1 
ATOM   5232 N  N    . LEU   B 1 328 ? -38.27900 26.36100 73.85500 1.000 18.87599 ? 762  LEU   B N    1 
ATOM   5233 C  CA   . LEU   B 1 328 ? -38.84100 26.03100 75.15800 1.000 16.40411 ? 762  LEU   B CA   1 
ATOM   5234 C  C    . LEU   B 1 328 ? -38.13100 24.86500 75.83200 1.000 16.89997 ? 762  LEU   B C    1 
ATOM   5235 O  O    . LEU   B 1 328 ? -38.38500 24.60900 77.01200 1.000 19.49617 ? 762  LEU   B O    1 
ATOM   5236 C  CB   . LEU   B 1 328 ? -40.33100 25.72000 75.01000 1.000 16.26583 ? 762  LEU   B CB   1 
ATOM   5237 C  CG   . LEU   B 1 328 ? -41.22400 26.92800 74.72800 1.000 17.83461 ? 762  LEU   B CG   1 
ATOM   5238 C  CD1  . LEU   B 1 328 ? -42.56800 26.48200 74.16800 1.000 18.71224 ? 762  LEU   B CD1  1 
ATOM   5239 C  CD2  . LEU   B 1 328 ? -41.41400 27.74000 76.00300 1.000 12.28333 ? 762  LEU   B CD2  1 
ATOM   5240 N  N    . GLY   B 1 329 ? -37.25800 24.15700 75.12000 1.000 15.72815 ? 763  GLY   B N    1 
ATOM   5241 C  CA   . GLY   B 1 329 ? -36.50100 23.06700 75.69500 1.000 13.93876 ? 763  GLY   B CA   1 
ATOM   5242 C  C    . GLY   B 1 329 ? -37.00100 21.67600 75.37800 1.000 18.70037 ? 763  GLY   B C    1 
ATOM   5243 O  O    . GLY   B 1 329 ? -36.47100 20.70800 75.93600 1.000 18.29514 ? 763  GLY   B O    1 
ATOM   5244 N  N    . ASP   B 1 330 ? -37.99600 21.54300 74.50800 1.000 23.57876 ? 764  ASP   B N    1 
ATOM   5245 C  CA   . ASP   B 1 330 ? -38.53400 20.23000 74.18700 1.000 16.32551 ? 764  ASP   B CA   1 
ATOM   5246 C  C    . ASP   B 1 330 ? -37.50100 19.39100 73.44000 1.000 18.68561 ? 764  ASP   B C    1 
ATOM   5247 O  O    . ASP   B 1 330 ? -36.65100 19.91100 72.71300 1.000 14.06921 ? 764  ASP   B O    1 
ATOM   5248 C  CB   . ASP   B 1 330 ? -39.81000 20.36900 73.35600 1.000 14.27203 ? 764  ASP   B CB   1 
ATOM   5249 C  CG   . ASP   B 1 330 ? -40.89600 21.15200 74.07700 1.000 22.47215 ? 764  ASP   B CG   1 
ATOM   5250 O  OD1  . ASP   B 1 330 ? -40.87800 21.17800 75.32700 1.000 26.80926 ? 764  ASP   B OD1  1 
ATOM   5251 O  OD2  . ASP   B 1 330 ? -41.77100 21.73600 73.39900 1.000 19.86978 ? 764  ASP   B OD2  1 
ATOM   5252 N  N    . SER   B 1 331 ? -37.58400 18.07900 73.62700 1.000 17.92231 ? 765  SER   B N    1 
ATOM   5253 C  CA   . SER   B 1 331 ? -36.62400 17.17500 73.00900 1.000 27.59307 ? 765  SER   B CA   1 
ATOM   5254 C  C    . SER   B 1 331 ? -36.71900 17.26300 71.48700 1.000 20.42478 ? 765  SER   B C    1 
ATOM   5255 O  O    . SER   B 1 331 ? -37.82900 17.27400 70.93900 1.000 22.89936 ? 765  SER   B O    1 
ATOM   5256 C  CB   . SER   B 1 331 ? -36.86500 15.73800 73.46900 1.000 26.87714 ? 765  SER   B CB   1 
ATOM   5257 O  OG   . SER   B 1 331 ? -36.53800 15.57500 74.84000 1.000 34.45146 ? 765  SER   B OG   1 
ATOM   5258 N  N    . PRO   B 1 332 ? -35.59700 17.33800 70.77800 1.000 25.93062 ? 766  PRO   B N    1 
ATOM   5259 C  CA   . PRO   B 1 332 ? -35.64000 17.34300 69.31200 1.000 23.39452 ? 766  PRO   B CA   1 
ATOM   5260 C  C    . PRO   B 1 332 ? -36.30700 16.08700 68.78600 1.000 24.37762 ? 766  PRO   B C    1 
ATOM   5261 O  O    . PRO   B 1 332 ? -36.13100 14.99700 69.35200 1.000 24.31600 ? 766  PRO   B O    1 
ATOM   5262 C  CB   . PRO   B 1 332 ? -34.15900 17.39600 68.91100 1.000 22.78395 ? 766  PRO   B CB   1 
ATOM   5263 C  CG   . PRO   B 1 332 ? -33.46900 17.99600 70.09000 1.000 30.04969 ? 766  PRO   B CG   1 
ATOM   5264 C  CD   . PRO   B 1 332 ? -34.22800 17.51600 71.29600 1.000 28.72287 ? 766  PRO   B CD   1 
ATOM   5265 N  N    . PRO   B 1 333 ? -37.08500 16.19600 67.71200 1.000 26.07007 ? 767  PRO   B N    1 
ATOM   5266 C  CA   . PRO   B 1 333 ? -37.74100 15.01100 67.15200 1.000 32.03232 ? 767  PRO   B CA   1 
ATOM   5267 C  C    . PRO   B 1 333 ? -36.73600 14.10100 66.46400 1.000 16.96514 ? 767  PRO   B C    1 
ATOM   5268 O  O    . PRO   B 1 333 ? -35.62400 14.50200 66.12200 1.000 31.86434 ? 767  PRO   B O    1 
ATOM   5269 C  CB   . PRO   B 1 333 ? -38.73400 15.60000 66.14700 1.000 22.68815 ? 767  PRO   B CB   1 
ATOM   5270 C  CG   . PRO   B 1 333 ? -38.10200 16.88900 65.72600 1.000 17.43778 ? 767  PRO   B CG   1 
ATOM   5271 C  CD   . PRO   B 1 333 ? -37.38800 17.41500 66.94200 1.000 21.15524 ? 767  PRO   B CD   1 
ATOM   5272 N  N    . PRO   B 1 340 ? -27.54300 10.52900 52.28000 1.000 42.05483 ? 774  PRO   B N    1 
ATOM   5273 C  CA   . PRO   B 1 340 ? -26.57100 11.12000 51.35400 1.000 37.08632 ? 774  PRO   B CA   1 
ATOM   5274 C  C    . PRO   B 1 340 ? -27.10700 12.36500 50.66800 1.000 21.59011 ? 774  PRO   B C    1 
ATOM   5275 O  O    . PRO   B 1 340 ? -28.30600 12.50900 50.41900 1.000 27.83373 ? 774  PRO   B O    1 
ATOM   5276 C  CB   . PRO   B 1 340 ? -26.32400 10.00000 50.33500 1.000 25.26507 ? 774  PRO   B CB   1 
ATOM   5277 C  CG   . PRO   B 1 340 ? -26.88300 8.75300  50.96500 1.000 41.99582 ? 774  PRO   B CG   1 
ATOM   5278 C  CD   . PRO   B 1 340 ? -28.01900 9.22000  51.80800 1.000 38.41028 ? 774  PRO   B CD   1 
ATOM   5279 N  N    . LEU   B 1 341 ? -26.18600 13.26600 50.35100 1.000 14.63271 ? 775  LEU   B N    1 
ATOM   5280 C  CA   . LEU   B 1 341 ? -26.54100 14.55100 49.77400 1.000 14.84107 ? 775  LEU   B CA   1 
ATOM   5281 C  C    . LEU   B 1 341 ? -26.63700 14.45200 48.25800 1.000 16.97995 ? 775  LEU   B C    1 
ATOM   5282 O  O    . LEU   B 1 341 ? -26.06400 13.56000 47.62800 1.000 25.10729 ? 775  LEU   B O    1 
ATOM   5283 C  CB   . LEU   B 1 341 ? -25.51200 15.61900 50.14800 1.000 15.02094 ? 775  LEU   B CB   1 
ATOM   5284 C  CG   . LEU   B 1 341 ? -24.94700 15.67400 51.57100 1.000 13.81434 ? 775  LEU   B CG   1 
ATOM   5285 C  CD1  . LEU   B 1 341 ? -24.18500 16.97700 51.76500 1.000 13.51102 ? 775  LEU   B CD1  1 
ATOM   5286 C  CD2  . LEU   B 1 341 ? -26.03600 15.51900 52.62800 1.000 13.59194 ? 775  LEU   B CD2  1 
ATOM   5287 N  N    . LYS   B 1 342 ? -27.37700 15.38800 47.67300 1.000 22.37760 ? 776  LYS   B N    1 
ATOM   5288 C  CA   . LYS   B 1 342 ? -27.28800 15.58400 46.23600 1.000 19.17931 ? 776  LYS   B CA   1 
ATOM   5289 C  C    . LYS   B 1 342 ? -25.88000 16.04400 45.88800 1.000 16.72197 ? 776  LYS   B C    1 
ATOM   5290 O  O    . LYS   B 1 342 ? -25.23100 16.74900 46.66500 1.000 14.06209 ? 776  LYS   B O    1 
ATOM   5291 C  CB   . LYS   B 1 342 ? -28.32300 16.60700 45.77400 1.000 23.64845 ? 776  LYS   B CB   1 
ATOM   5292 C  CG   . LYS   B 1 342 ? -29.75800 16.15300 45.98200 1.000 32.84231 ? 776  LYS   B CG   1 
ATOM   5293 C  CD   . LYS   B 1 342 ? -30.74400 17.23300 45.59100 1.000 22.45636 ? 776  LYS   B CD   1 
ATOM   5294 C  CE   . LYS   B 1 342 ? -30.41600 17.80600 44.22300 1.000 27.58439 ? 776  LYS   B CE   1 
ATOM   5295 N  NZ   . LYS   B 1 342 ? -31.50300 18.70400 43.73600 1.000 26.37515 ? 776  LYS   B NZ   1 
ATOM   5296 N  N    . THR   B 1 343 ? -25.39400 15.61200 44.72000 1.000 20.48669 ? 777  THR   B N    1 
ATOM   5297 C  CA   . THR   B 1 343 ? -24.02300 15.92800 44.32800 1.000 15.56610 ? 777  THR   B CA   1 
ATOM   5298 C  C    . THR   B 1 343 ? -23.76900 17.43000 44.35900 1.000 19.42783 ? 777  THR   B C    1 
ATOM   5299 O  O    . THR   B 1 343 ? -22.73700 17.88500 44.86800 1.000 14.43800 ? 777  THR   B O    1 
ATOM   5300 C  CB   . THR   B 1 343 ? -23.73200 15.36600 42.93600 1.000 15.90307 ? 777  THR   B CB   1 
ATOM   5301 O  OG1  . THR   B 1 343 ? -23.51000 13.95400 43.02700 1.000 32.34788 ? 777  THR   B OG1  1 
ATOM   5302 C  CG2  . THR   B 1 343 ? -22.50400 16.02600 42.33600 1.000 15.67970 ? 777  THR   B CG2  1 
ATOM   5303 N  N    . SER   B 1 344 ? -24.72000 18.21600 43.84900 1.000 17.40064 ? 778  SER   B N    1 
ATOM   5304 C  CA   . SER   B 1 344 ? -24.53700 19.66200 43.78300 1.000 17.26940 ? 778  SER   B CA   1 
ATOM   5305 C  C    . SER   B 1 344 ? -24.36100 20.26500 45.17000 1.000 17.18716 ? 778  SER   B C    1 
ATOM   5306 O  O    . SER   B 1 344 ? -23.56000 21.18700 45.35500 1.000 13.23724 ? 778  SER   B O    1 
ATOM   5307 C  CB   . SER   B 1 344 ? -25.72200 20.30800 43.07100 1.000 13.59857 ? 778  SER   B CB   1 
ATOM   5308 O  OG   . SER   B 1 344 ? -26.89800 20.17700 43.84400 1.000 13.31791 ? 778  SER   B OG   1 
ATOM   5309 N  N    . ALA   B 1 345 ? -25.10400 19.75900 46.15800 1.000 15.89939 ? 779  ALA   B N    1 
ATOM   5310 C  CA   . ALA   B 1 345 ? -24.97600 20.27400 47.51800 1.000 12.88464 ? 779  ALA   B CA   1 
ATOM   5311 C  C    . ALA   B 1 345 ? -23.59700 19.98500 48.09200 1.000 16.92096 ? 779  ALA   B C    1 
ATOM   5312 O  O    . ALA   B 1 345 ? -23.02500 20.82100 48.80300 1.000 19.56593 ? 779  ALA   B O    1 
ATOM   5313 C  CB   . ALA   B 1 345 ? -26.05400 19.66600 48.40300 1.000 20.31340 ? 779  ALA   B CB   1 
ATOM   5314 N  N    . THR   B 1 346 ? -23.05800 18.79800 47.80700 1.000 21.39950 ? 780  THR   B N    1 
ATOM   5315 C  CA   . THR   B 1 346 ? -21.68600 18.48600 48.18800 1.000 17.22174 ? 780  THR   B CA   1 
ATOM   5316 C  C    . THR   B 1 346 ? -20.70700 19.47700 47.57500 1.000 13.93676 ? 780  THR   B C    1 
ATOM   5317 O  O    . THR   B 1 346 ? -19.77200 19.93200 48.24300 1.000 13.95274 ? 780  THR   B O    1 
ATOM   5318 C  CB   . THR   B 1 346 ? -21.34500 17.05900 47.76400 1.000 14.49531 ? 780  THR   B CB   1 
ATOM   5319 O  OG1  . THR   B 1 346 ? -22.19100 16.14300 48.47300 1.000 18.03880 ? 780  THR   B OG1  1 
ATOM   5320 C  CG2  . THR   B 1 346 ? -19.88500 16.73800 48.06300 1.000 16.15184 ? 780  THR   B CG2  1 
ATOM   5321 N  N    . VAL   B 1 347 ? -20.91300 19.83300 46.30800 1.000 14.93778 ? 781  VAL   B N    1 
ATOM   5322 C  CA   . VAL   B 1 347 ? -20.04600 20.81600 45.66500 1.000 14.00336 ? 781  VAL   B CA   1 
ATOM   5323 C  C    . VAL   B 1 347 ? -20.17500 22.16800 46.35400 1.000 14.35569 ? 781  VAL   B C    1 
ATOM   5324 O  O    . VAL   B 1 347 ? -19.17500 22.85000 46.60700 1.000 25.00786 ? 781  VAL   B O    1 
ATOM   5325 C  CB   . VAL   B 1 347 ? -20.36900 20.91200 44.16200 1.000 14.16197 ? 781  VAL   B CB   1 
ATOM   5326 C  CG1  . VAL   B 1 347 ? -19.45900 21.92200 43.48500 1.000 14.23691 ? 781  VAL   B CG1  1 
ATOM   5327 C  CG2  . VAL   B 1 347 ? -20.24700 19.55000 43.50000 1.000 14.69371 ? 781  VAL   B CG2  1 
ATOM   5328 N  N    . SER   B 1 348 ? -21.40500 22.57400 46.67000 1.000 13.12735 ? 782  SER   B N    1 
ATOM   5329 C  CA   . SER   B 1 348 ? -21.62000 23.86400 47.32000 1.000 16.48325 ? 782  SER   B CA   1 
ATOM   5330 C  C    . SER   B 1 348 ? -20.91700 23.92500 48.67100 1.000 15.43314 ? 782  SER   B C    1 
ATOM   5331 O  O    . SER   B 1 348 ? -20.19400 24.88600 48.96500 1.000 12.71119 ? 782  SER   B O    1 
ATOM   5332 C  CB   . SER   B 1 348 ? -23.11900 24.12200 47.47800 1.000 12.33666 ? 782  SER   B CB   1 
ATOM   5333 O  OG   . SER   B 1 348 ? -23.74300 24.27100 46.21300 1.000 18.26179 ? 782  SER   B OG   1 
ATOM   5334 N  N    . ILE   B 1 349 ? -21.11800 22.90500 49.50800 1.000 15.88302 ? 783  ILE   B N    1 
ATOM   5335 C  CA   . ILE   B 1 349 ? -20.48400 22.88900 50.82400 1.000 14.28610 ? 783  ILE   B CA   1 
ATOM   5336 C  C    . ILE   B 1 349 ? -18.96800 22.90800 50.68200 1.000 15.38213 ? 783  ILE   B C    1 
ATOM   5337 O  O    . ILE   B 1 349 ? -18.26800 23.61100 51.42100 1.000 16.05138 ? 783  ILE   B O    1 
ATOM   5338 C  CB   . ILE   B 1 349 ? -20.96500 21.67200 51.63600 1.000 13.26357 ? 783  ILE   B CB   1 
ATOM   5339 C  CG1  . ILE   B 1 349 ? -22.45800 21.79300 51.94400 1.000 12.57717 ? 783  ILE   B CG1  1 
ATOM   5340 C  CG2  . ILE   B 1 349 ? -20.16100 21.53100 52.92400 1.000 16.21488 ? 783  ILE   B CG2  1 
ATOM   5341 C  CD1  . ILE   B 1 349 ? -22.97900 20.72800 52.89500 1.000 14.35225 ? 783  ILE   B CD1  1 
ATOM   5342 N  N    . ASN   B 1 350 ? -18.44600 22.18900 49.68700 1.000 18.59854 ? 784  ASN   B N    1 
ATOM   5343 C  CA   . ASN   B 1 350 ? -16.97700 22.09500 49.43600 1.000 15.86185 ? 784  ASN   B CA   1 
ATOM   5344 C  C    . ASN   B 1 350 ? -16.44900 23.47000 49.02000 1.000 20.01472 ? 784  ASN   B C    1 
ATOM   5345 O  O    . ASN   B 1 350 ? -15.36800 23.86000 49.49300 1.000 14.22893 ? 784  ASN   B O    1 
ATOM   5346 C  CB   . ASN   B 1 350 ? -16.65000 20.98700 48.43800 1.000 14.60623 ? 784  ASN   B CB   1 
ATOM   5347 C  CG   . ASN   B 1 350 ? -15.63100 21.37700 47.39700 1.000 19.80047 ? 784  ASN   B CG   1 
ATOM   5348 O  OD1  . ASN   B 1 350 ? -14.45000 21.53400 47.71600 1.000 31.97062 ? 784  ASN   B OD1  1 
ATOM   5349 N  ND2  . ASN   B 1 350 ? -16.05800 21.51300 46.15200 1.000 23.34861 ? 784  ASN   B ND2  1 
ATOM   5350 N  N    . ASN   B 1 351 ? -17.24600 24.20200 48.25100 1.000 18.96777 ? 785  ASN   B N    1 
ATOM   5351 C  CA   . ASN   B 1 351 ? -16.79300 25.50700 47.77400 1.000 17.87592 ? 785  ASN   B CA   1 
ATOM   5352 C  C    . ASN   B 1 351 ? -16.72500 26.52600 48.90600 1.000 13.43407 ? 785  ASN   B C    1 
ATOM   5353 O  O    . ASN   B 1 351 ? -15.83100 27.38000 48.92300 1.000 13.60789 ? 785  ASN   B O    1 
ATOM   5354 C  CB   . ASN   B 1 351 ? -17.70400 26.01800 46.65800 1.000 16.42308 ? 785  ASN   B CB   1 
ATOM   5355 C  CG   . ASN   B 1 351 ? -17.56400 25.21700 45.37400 1.000 16.62944 ? 785  ASN   B CG   1 
ATOM   5356 O  OD1  . ASN   B 1 351 ? -16.61100 24.46200 45.20000 1.000 14.14977 ? 785  ASN   B OD1  1 
ATOM   5357 N  ND2  . ASN   B 1 351 ? -18.52100 25.38300 44.46800 1.000 13.57362 ? 785  ASN   B ND2  1 
ATOM   5358 N  N    . VAL   B 1 352 ? -17.66400 26.46500 49.85400 1.000 17.25987 ? 786  VAL   B N    1 
ATOM   5359 C  CA   . VAL   B 1 352 ? -17.63900 27.40200 50.97400 1.000 12.97025 ? 786  VAL   B CA   1 
ATOM   5360 C  C    . VAL   B 1 352 ? -16.51600 27.04900 51.93700 1.000 13.34674 ? 786  VAL   B C    1 
ATOM   5361 O  O    . VAL   B 1 352 ? -15.79500 27.93200 52.41900 1.000 13.50114 ? 786  VAL   B O    1 
ATOM   5362 C  CB   . VAL   B 1 352 ? -19.00100 27.43300 51.68800 1.000 15.08769 ? 786  VAL   B CB   1 
ATOM   5363 C  CG1  . VAL   B 1 352 ? -19.00700 28.51400 52.76400 1.000 13.29546 ? 786  VAL   B CG1  1 
ATOM   5364 C  CG2  . VAL   B 1 352 ? -20.12000 27.65600 50.68800 1.000 12.24642 ? 786  VAL   B CG2  1 
ATOM   5365 N  N    . LEU   B 1 353 ? -16.35900 25.75600 52.24100 1.000 13.54986 ? 787  LEU   B N    1 
ATOM   5366 C  CA   . LEU   B 1 353 ? -15.24100 25.29200 53.05700 1.000 13.98750 ? 787  LEU   B CA   1 
ATOM   5367 C  C    . LEU   B 1 353 ? -13.91300 25.79100 52.50700 1.000 14.37743 ? 787  LEU   B C    1 
ATOM   5368 O  O    . LEU   B 1 353 ? -13.06000 26.28200 53.25500 1.000 14.65135 ? 787  LEU   B O    1 
ATOM   5369 C  CB   . LEU   B 1 353 ? -15.23600 23.76100 53.12600 1.000 14.21454 ? 787  LEU   B CB   1 
ATOM   5370 C  CG   . LEU   B 1 353 ? -16.04100 23.04300 54.21100 1.000 19.52610 ? 787  LEU   B CG   1 
ATOM   5371 C  CD1  . LEU   B 1 353 ? -15.93500 21.53700 54.02700 1.000 14.39759 ? 787  LEU   B CD1  1 
ATOM   5372 C  CD2  . LEU   B 1 353 ? -15.56400 23.44600 55.59500 1.000 21.97749 ? 787  LEU   B CD2  1 
ATOM   5373 N  N    . ARG   B 1 354 ? -13.72100 25.66900 51.19300 1.000 15.08766 ? 788  ARG   B N    1 
ATOM   5374 C  CA   . ARG   B 1 354 ? -12.47000 26.10900 50.58700 1.000 16.71916 ? 788  ARG   B CA   1 
ATOM   5375 C  C    . ARG   B 1 354 ? -12.32300 27.62300 50.66600 1.000 14.75191 ? 788  ARG   B C    1 
ATOM   5376 O  O    . ARG   B 1 354 ? -11.25500 28.13100 51.02700 1.000 15.12010 ? 788  ARG   B O    1 
ATOM   5377 C  CB   . ARG   B 1 354 ? -12.39600 25.63700 49.13400 1.000 14.98407 ? 788  ARG   B CB   1 
ATOM   5378 C  CG   . ARG   B 1 354 ? -11.02000 25.76300 48.52400 1.000 19.25193 ? 788  ARG   B CG   1 
ATOM   5379 C  CD   . ARG   B 1 354 ? -11.04400 25.57500 47.01100 1.000 23.43196 ? 788  ARG   B CD   1 
ATOM   5380 N  NE   . ARG   B 1 354 ? -11.66100 24.31700 46.60900 1.000 18.19024 ? 788  ARG   B NE   1 
ATOM   5381 C  CZ   . ARG   B 1 354 ? -12.82900 24.22100 45.98700 1.000 20.65333 ? 788  ARG   B CZ   1 
ATOM   5382 N  NH1  . ARG   B 1 354 ? -13.53000 25.29500 45.66300 1.000 21.11711 ? 788  ARG   B NH1  1 
ATOM   5383 N  NH2  . ARG   B 1 354 ? -13.30200 23.01800 45.67700 1.000 21.03740 ? 788  ARG   B NH2  1 
ATOM   5384 N  N    . ALA   B 1 355 ? -13.39200 28.36100 50.35200 1.000 15.24044 ? 789  ALA   B N    1 
ATOM   5385 C  CA   . ALA   B 1 355 ? -13.30800 29.81800 50.34000 1.000 14.22778 ? 789  ALA   B CA   1 
ATOM   5386 C  C    . ALA   B 1 355 ? -13.07900 30.39200 51.73400 1.000 14.30030 ? 789  ALA   B C    1 
ATOM   5387 O  O    . ALA   B 1 355 ? -12.50600 31.47900 51.86600 1.000 14.49403 ? 789  ALA   B O    1 
ATOM   5388 C  CB   . ALA   B 1 355 ? -14.57600 30.41200 49.72600 1.000 13.75340 ? 789  ALA   B CB   1 
ATOM   5389 N  N    . HIS   B 1 356 ? -13.50500 29.68900 52.77900 1.000 14.20357 ? 790  HIS   B N    1 
ATOM   5390 C  CA   . HIS   B 1 356 ? -13.43100 30.22300 54.13200 1.000 18.22739 ? 790  HIS   B CA   1 
ATOM   5391 C  C    . HIS   B 1 356 ? -12.34800 29.58400 54.98700 1.000 16.40088 ? 790  HIS   B C    1 
ATOM   5392 O  O    . HIS   B 1 356 ? -12.15100 30.01300 56.13000 1.000 14.96364 ? 790  HIS   B O    1 
ATOM   5393 C  CB   . HIS   B 1 356 ? -14.79300 30.10200 54.82200 1.000 13.82512 ? 790  HIS   B CB   1 
ATOM   5394 C  CG   . HIS   B 1 356 ? -15.68800 31.27000 54.56100 1.000 13.45719 ? 790  HIS   B CG   1 
ATOM   5395 N  ND1  . HIS   B 1 356 ? -15.56600 32.46300 55.24000 1.000 13.55048 ? 790  HIS   B ND1  1 
ATOM   5396 C  CD2  . HIS   B 1 356 ? -16.69100 31.44500 53.66900 1.000 14.27827 ? 790  HIS   B CD2  1 
ATOM   5397 C  CE1  . HIS   B 1 356 ? -16.46700 33.31700 54.78900 1.000 19.53607 ? 790  HIS   B CE1  1 
ATOM   5398 N  NE2  . HIS   B 1 356 ? -17.16000 32.72500 53.83300 1.000 12.90098 ? 790  HIS   B NE2  1 
ATOM   5399 N  N    . ALA   B 1 357 ? -11.64100 28.58400 54.46600 1.000 19.34303 ? 791  ALA   B N    1 
ATOM   5400 C  CA   . ALA   B 1 357 ? -10.46100 28.06100 55.15000 1.000 15.65137 ? 791  ALA   B CA   1 
ATOM   5401 C  C    . ALA   B 1 357 ? -9.48500  29.14200 55.60800 1.000 22.53726 ? 791  ALA   B C    1 
ATOM   5402 O  O    . ALA   B 1 357 ? -9.00600  29.04800 56.75200 1.000 18.11429 ? 791  ALA   B O    1 
ATOM   5403 C  CB   . ALA   B 1 357 ? -9.74900  27.04500 54.24300 1.000 15.95376 ? 791  ALA   B CB   1 
ATOM   5404 N  N    . PRO   B 1 358 ? -9.15300  30.17100 54.81400 1.000 16.10110 ? 792  PRO   B N    1 
ATOM   5405 C  CA   . PRO   B 1 358 ? -8.18100  31.16600 55.30200 1.000 22.04175 ? 792  PRO   B CA   1 
ATOM   5406 C  C    . PRO   B 1 358 ? -8.61700  31.89400 56.56000 1.000 17.87658 ? 792  PRO   B C    1 
ATOM   5407 O  O    . PRO   B 1 358 ? -7.75600  32.32600 57.33700 1.000 18.36917 ? 792  PRO   B O    1 
ATOM   5408 C  CB   . PRO   B 1 358 ? -8.04100  32.13600 54.11800 1.000 16.53307 ? 792  PRO   B CB   1 
ATOM   5409 C  CG   . PRO   B 1 358 ? -9.24700  31.89300 53.26500 1.000 15.91431 ? 792  PRO   B CG   1 
ATOM   5410 C  CD   . PRO   B 1 358 ? -9.52300  30.43600 53.41000 1.000 15.81603 ? 792  PRO   B CD   1 
ATOM   5411 N  N    . PHE   B 1 359 ? -9.92300  32.03500 56.79400 1.000 15.99194 ? 793  PHE   B N    1 
ATOM   5412 C  CA   . PHE   B 1 359 ? -10.42100 32.86200 57.88300 1.000 15.95666 ? 793  PHE   B CA   1 
ATOM   5413 C  C    . PHE   B 1 359 ? -10.86100 32.06800 59.10200 1.000 18.67315 ? 793  PHE   B C    1 
ATOM   5414 O  O    . PHE   B 1 359 ? -10.91000 32.63300 60.20100 1.000 17.29875 ? 793  PHE   B O    1 
ATOM   5415 C  CB   . PHE   B 1 359 ? -11.59900 33.72000 57.39800 1.000 15.40758 ? 793  PHE   B CB   1 
ATOM   5416 C  CG   . PHE   B 1 359 ? -11.38800 34.32000 56.03700 1.000 16.79436 ? 793  PHE   B CG   1 
ATOM   5417 C  CD1  . PHE   B 1 359 ? -10.47700 35.34600 55.85000 1.000 17.81859 ? 793  PHE   B CD1  1 
ATOM   5418 C  CD2  . PHE   B 1 359 ? -12.09600 33.85500 54.94300 1.000 14.90733 ? 793  PHE   B CD2  1 
ATOM   5419 C  CE1  . PHE   B 1 359 ? -10.27700 35.89600 54.59400 1.000 20.28286 ? 793  PHE   B CE1  1 
ATOM   5420 C  CE2  . PHE   B 1 359 ? -11.90200 34.40600 53.68300 1.000 14.88875 ? 793  PHE   B CE2  1 
ATOM   5421 C  CZ   . PHE   B 1 359 ? -10.99400 35.42700 53.51000 1.000 15.31270 ? 793  PHE   B CZ   1 
ATOM   5422 N  N    . TRP   B 1 360 ? -11.17300 30.78200 58.94700 1.000 15.75132 ? 794  TRP   B N    1 
ATOM   5423 C  CA   . TRP   B 1 360 ? -11.72700 29.97100 60.03200 1.000 15.70035 ? 794  TRP   B CA   1 
ATOM   5424 C  C    . TRP   B 1 360 ? -10.85400 28.73500 60.21400 1.000 16.13493 ? 794  TRP   B C    1 
ATOM   5425 O  O    . TRP   B 1 360 ? -11.03600 27.72600 59.52900 1.000 15.97673 ? 794  TRP   B O    1 
ATOM   5426 C  CB   . TRP   B 1 360 ? -13.18200 29.62500 59.74600 1.000 15.04626 ? 794  TRP   B CB   1 
ATOM   5427 C  CG   . TRP   B 1 360 ? -13.98200 30.86600 59.54200 1.000 14.68008 ? 794  TRP   B CG   1 
ATOM   5428 C  CD1  . TRP   B 1 360 ? -14.44700 31.36300 58.35900 1.000 16.26376 ? 794  TRP   B CD1  1 
ATOM   5429 C  CD2  . TRP   B 1 360 ? -14.35400 31.81100 60.54900 1.000 14.71968 ? 794  TRP   B CD2  1 
ATOM   5430 N  NE1  . TRP   B 1 360 ? -15.11600 32.54500 58.57400 1.000 14.11065 ? 794  TRP   B NE1  1 
ATOM   5431 C  CE2  . TRP   B 1 360 ? -15.06900 32.84200 59.91100 1.000 14.35476 ? 794  TRP   B CE2  1 
ATOM   5432 C  CE3  . TRP   B 1 360 ? -14.16500 31.87600 61.93100 1.000 15.35710 ? 794  TRP   B CE3  1 
ATOM   5433 C  CZ2  . TRP   B 1 360 ? -15.59500 33.92700 60.61000 1.000 16.73008 ? 794  TRP   B CZ2  1 
ATOM   5434 C  CZ3  . TRP   B 1 360 ? -14.68700 32.95300 62.62300 1.000 19.34302 ? 794  TRP   B CZ3  1 
ATOM   5435 C  CH2  . TRP   B 1 360 ? -15.39000 33.96700 61.96100 1.000 14.68775 ? 794  TRP   B CH2  1 
ATOM   5436 N  N    . SER   B 1 361 ? -9.91500  28.83000 61.16000 1.000 16.73601 ? 795  SER   B N    1 
ATOM   5437 C  CA   . SER   B 1 361 ? -8.98000  27.74900 61.43700 1.000 17.25736 ? 795  SER   B CA   1 
ATOM   5438 C  C    . SER   B 1 361 ? -9.68000  26.46000 61.84800 1.000 17.08123 ? 795  SER   B C    1 
ATOM   5439 O  O    . SER   B 1 361 ? -9.06400  25.39100 61.78600 1.000 18.23952 ? 795  SER   B O    1 
ATOM   5440 C  CB   . SER   B 1 361 ? -7.99800  28.19200 62.52500 1.000 17.95490 ? 795  SER   B CB   1 
ATOM   5441 O  OG   . SER   B 1 361 ? -7.09600  27.15800 62.86500 1.000 18.51287 ? 795  SER   B OG   1 
ATOM   5442 N  N    . SER   B 1 362 ? -10.95000 26.52900 62.25100 1.000 16.58846 ? 796  SER   B N    1 
ATOM   5443 C  CA   . SER   B 1 362 ? -11.68000 25.33400 62.65700 1.000 16.44039 ? 796  SER   B CA   1 
ATOM   5444 C  C    . SER   B 1 362 ? -12.25100 24.54900 61.48100 1.000 16.04322 ? 796  SER   B C    1 
ATOM   5445 O  O    . SER   B 1 362 ? -12.74300 23.43400 61.68400 1.000 23.76282 ? 796  SER   B O    1 
ATOM   5446 C  CB   . SER   B 1 362 ? -12.81400 25.71000 63.61400 1.000 16.13316 ? 796  SER   B CB   1 
ATOM   5447 O  OG   . SER   B 1 362 ? -13.88800 26.32400 62.91900 1.000 18.81699 ? 796  SER   B OG   1 
ATOM   5448 N  N    . LEU   B 1 363 ? -12.20200 25.08800 60.26800 1.000 15.80111 ? 797  LEU   B N    1 
ATOM   5449 C  CA   . LEU   B 1 363 ? -12.78000 24.40000 59.11500 1.000 15.88053 ? 797  LEU   B CA   1 
ATOM   5450 C  C    . LEU   B 1 363 ? -11.85100 23.31600 58.58300 1.000 15.91479 ? 797  LEU   B C    1 
ATOM   5451 O  O    . LEU   B 1 363 ? -10.78200 23.08200 59.13900 1.000 21.57481 ? 797  LEU   B O    1 
ATOM   5452 C  CB   . LEU   B 1 363 ? -13.11200 25.39600 58.00300 1.000 16.41675 ? 797  LEU   B CB   1 
ATOM   5453 C  CG   . LEU   B 1 363 ? -14.24300 26.38800 58.28700 1.000 21.06074 ? 797  LEU   B CG   1 
ATOM   5454 C  CD1  . LEU   B 1 363 ? -14.44100 27.33500 57.11300 1.000 14.30672 ? 797  LEU   B CD1  1 
ATOM   5455 C  CD2  . LEU   B 1 363 ? -15.54000 25.65500 58.60400 1.000 14.21905 ? 797  LEU   B CD2  1 
HETATM 5456 C  C13  . A1BNN C 2 .   ? -15.85700 15.33400 46.71800 1.000 25.02867 ? 801  A1BNN A C13  1 
HETATM 5457 C  C02  . A1BNN C 2 .   ? -15.09100 16.25100 35.77700 1.000 7.89230  ? 801  A1BNN A C02  1 
HETATM 5458 C  C03  . A1BNN C 2 .   ? -14.94500 17.19000 36.96200 1.000 12.18659 ? 801  A1BNN A C03  1 
HETATM 5459 C  C04  . A1BNN C 2 .   ? -14.93700 16.38300 38.25300 1.000 17.51135 ? 801  A1BNN A C04  1 
HETATM 5460 C  C05  . A1BNN C 2 .   ? -15.79900 16.89800 39.38700 1.000 7.01148  ? 801  A1BNN A C05  1 
HETATM 5461 C  C06  . A1BNN C 2 .   ? -15.80900 15.88600 40.52000 1.000 8.47464  ? 801  A1BNN A C06  1 
HETATM 5462 C  C07  . A1BNN C 2 .   ? -15.84300 16.49600 41.92500 1.000 13.63197 ? 801  A1BNN A C07  1 
HETATM 5463 C  C09  . A1BNN C 2 .   ? -16.16500 15.98900 44.42900 1.000 19.53179 ? 801  A1BNN A C09  1 
HETATM 5464 C  C10  . A1BNN C 2 .   ? -16.52400 17.25700 44.84600 1.000 13.69348 ? 801  A1BNN A C10  1 
HETATM 5465 C  C11  . A1BNN C 2 .   ? -16.54500 17.56400 46.18800 1.000 18.35401 ? 801  A1BNN A C11  1 
HETATM 5466 C  C12  . A1BNN C 2 .   ? -16.21700 16.60300 47.12100 1.000 18.99909 ? 801  A1BNN A C12  1 
HETATM 5467 C  C14  . A1BNN C 2 .   ? -15.83300 15.03100 45.37100 1.000 25.07747 ? 801  A1BNN A C14  1 
HETATM 5468 N  N08  . A1BNN C 2 .   ? -16.11300 15.60300 43.03300 1.000 13.24556 ? 801  A1BNN A N08  1 
HETATM 5469 O  O15  . A1BNN C 2 .   ? -15.65800 17.64600 42.08100 1.000 11.70846 ? 801  A1BNN A O15  1 
HETATM 5470 SE SE01 . A1BNN C 2 .   ? -14.54000 17.09900 34.12300 1.000 17.46521 ? 801  A1BNN A SE01 1 
HETATM 5471 C  C1   . EDO   D 3 .   ? -0.57000  13.81200 7.46600  1.000 28.28319 ? 802  EDO   A C1   1 
HETATM 5472 O  O1   . EDO   D 3 .   ? 0.59900   14.36800 8.01300  1.000 23.07780 ? 802  EDO   A O1   1 
HETATM 5473 C  C2   . EDO   D 3 .   ? -0.99100  12.56700 8.14700  1.000 24.17254 ? 802  EDO   A C2   1 
HETATM 5474 O  O2   . EDO   D 3 .   ? -0.87300  12.67100 9.54300  1.000 25.92971 ? 802  EDO   A O2   1 
HETATM 5475 ZN ZN   . ZN    E 4 .   ? -13.57300 19.32500 34.62200 1.000 11.53840 ? 803  ZN    A ZN   1 
HETATM 5476 K  K    . K     F 5 .   ? -6.91600  20.68600 32.43000 1.000 8.51150  ? 804  K     A K    1 
HETATM 5477 K  K    . K     G 5 .   ? 3.78000   12.87600 27.48100 1.000 13.23326 ? 805  K     A K    1 
HETATM 5478 C  C1   . EDO   H 3 .   ? -22.69900 22.15200 41.77500 1.000 13.47459 ? 801  EDO   B C1   1 
HETATM 5479 O  O1   . EDO   H 3 .   ? -23.41100 21.98900 40.57400 1.000 8.61718  ? 801  EDO   B O1   1 
HETATM 5480 C  C2   . EDO   H 3 .   ? -23.51800 22.96600 42.74900 1.000 23.08635 ? 801  EDO   B C2   1 
HETATM 5481 O  O2   . EDO   H 3 .   ? -22.73400 23.96000 43.36700 1.000 19.94740 ? 801  EDO   B O2   1 
HETATM 5482 C  C13  . A1BNN I 2 .   ? -40.73600 36.41000 39.77600 1.000 32.16731 ? 802  A1BNN B C13  1 
HETATM 5483 C  C02  . A1BNN I 2 .   ? -38.47800 36.58700 49.65500 1.000 18.48888 ? 802  A1BNN B C02  1 
HETATM 5484 C  C03  . A1BNN I 2 .   ? -39.49300 37.56600 49.11700 1.000 17.62495 ? 802  A1BNN B C03  1 
HETATM 5485 C  C04  . A1BNN I 2 .   ? -39.06700 38.08300 47.75800 1.000 16.82855 ? 802  A1BNN B C04  1 
HETATM 5486 C  C05  . A1BNN I 2 .   ? -39.51900 37.21400 46.59800 1.000 10.72278 ? 802  A1BNN B C05  1 
HETATM 5487 C  C06  . A1BNN I 2 .   ? -39.56300 38.09100 45.36300 1.000 17.28003 ? 802  A1BNN B C06  1 
HETATM 5488 C  C07  . A1BNN I 2 .   ? -39.69900 37.38800 44.01500 1.000 19.90255 ? 802  A1BNN B C07  1 
HETATM 5489 C  C09  . A1BNN I 2 .   ? -40.25200 37.93700 41.53800 1.000 27.26025 ? 802  A1BNN B C09  1 
HETATM 5490 C  C10  . A1BNN I 2 .   ? -40.15300 38.96100 40.61800 1.000 25.17525 ? 802  A1BNN B C10  1 
HETATM 5491 C  C11  . A1BNN I 2 .   ? -40.34100 38.71500 39.28000 1.000 26.57383 ? 802  A1BNN B C11  1 
HETATM 5492 C  C12  . A1BNN I 2 .   ? -40.63400 37.43500 38.86000 1.000 32.94911 ? 802  A1BNN B C12  1 
HETATM 5493 C  C14  . A1BNN I 2 .   ? -40.54700 36.66200 41.11500 1.000 21.51835 ? 802  A1BNN B C14  1 
HETATM 5494 N  N08  . A1BNN I 2 .   ? -40.05000 38.27200 42.92700 1.000 18.97841 ? 802  A1BNN B N08  1 
HETATM 5495 O  O15  . A1BNN I 2 .   ? -39.52700 36.22500 43.89700 1.000 20.18268 ? 802  A1BNN B O15  1 
HETATM 5496 SE SE01 . A1BNN I 2 .   ? -38.48400 36.58000 51.59400 1.000 18.02046 ? 802  A1BNN B SE01 1 
HETATM 5497 ZN ZN   . ZN    J 4 .   ? -37.50400 34.31500 51.13400 1.000 10.48736 ? 803  ZN    B ZN   1 
HETATM 5498 K  K    . K     K 5 .   ? -30.83900 32.97800 53.39100 1.000 9.93732  ? 804  K     B K    1 
HETATM 5499 K  K    . K     L 5 .   ? -20.18000 40.83600 58.31300 1.000 14.63140 ? 805  K     B K    1 
HETATM 5500 O  O    . HOH   M 6 .   ? -12.71700 5.55900  12.61000 1.000 12.76161 ? 901  HOH   A O    1 
HETATM 5501 O  O    . HOH   M 6 .   ? -28.94000 25.54300 24.19100 1.000 11.52073 ? 902  HOH   A O    1 
HETATM 5502 O  O    . HOH   M 6 .   ? -10.40600 12.45700 27.50400 1.000 8.33058  ? 903  HOH   A O    1 
HETATM 5503 O  O    . HOH   M 6 .   ? -12.38400 25.09500 30.89100 1.000 14.06214 ? 904  HOH   A O    1 
HETATM 5504 O  O    . HOH   M 6 .   ? -28.89800 16.00000 13.94200 1.000 21.65838 ? 905  HOH   A O    1 
HETATM 5505 O  O    . HOH   M 6 .   ? -5.47300  19.55100 43.06400 1.000 13.58804 ? 906  HOH   A O    1 
HETATM 5506 O  O    . HOH   M 6 .   ? -15.69400 11.62100 25.92400 1.000 13.60631 ? 907  HOH   A O    1 
HETATM 5507 O  O    . HOH   M 6 .   ? -31.54000 20.10100 25.87000 1.000 3.28095  ? 908  HOH   A O    1 
HETATM 5508 O  O    . HOH   M 6 .   ? -8.36600  24.98200 32.57600 1.000 7.34893  ? 909  HOH   A O    1 
HETATM 5509 O  O    . HOH   M 6 .   ? -4.74300  16.45200 41.09900 1.000 11.47500 ? 910  HOH   A O    1 
HETATM 5510 O  O    . HOH   M 6 .   ? -19.67500 26.07800 32.55200 1.000 11.94304 ? 911  HOH   A O    1 
HETATM 5511 O  O    . HOH   M 6 .   ? -25.24600 20.80700 34.21000 1.000 17.62954 ? 912  HOH   A O    1 
HETATM 5512 O  O    . HOH   M 6 .   ? -27.28900 20.42200 38.37600 1.000 20.89233 ? 913  HOH   A O    1 
HETATM 5513 O  O    . HOH   M 6 .   ? 5.53900   13.08200 29.52200 1.000 10.78878 ? 914  HOH   A O    1 
HETATM 5514 O  O    . HOH   M 6 .   ? -3.51000  5.44400  33.95400 1.000 15.73744 ? 915  HOH   A O    1 
HETATM 5515 O  O    . HOH   M 6 .   ? -7.51100  20.21300 38.80300 1.000 10.91274 ? 916  HOH   A O    1 
HETATM 5516 O  O    . HOH   M 6 .   ? -22.88000 13.14200 14.29600 1.000 23.50671 ? 917  HOH   A O    1 
HETATM 5517 O  O    . HOH   M 6 .   ? 4.90100   20.00100 34.15700 1.000 13.47372 ? 918  HOH   A O    1 
HETATM 5518 O  O    . HOH   M 6 .   ? -23.20800 0.59700  31.60700 1.000 14.18797 ? 919  HOH   A O    1 
HETATM 5519 O  O    . HOH   M 6 .   ? 6.01600   13.31400 35.76400 1.000 13.93932 ? 920  HOH   A O    1 
HETATM 5520 O  O    . HOH   M 6 .   ? -14.27300 13.82700 26.54700 1.000 9.22778  ? 921  HOH   A O    1 
HETATM 5521 O  O    . HOH   M 6 .   ? 8.95800   27.50000 19.98500 1.000 17.40429 ? 922  HOH   A O    1 
HETATM 5522 O  O    . HOH   M 6 .   ? -12.35600 0.17800  36.84100 1.000 14.65667 ? 923  HOH   A O    1 
HETATM 5523 O  O    . HOH   M 6 .   ? -24.00600 19.40500 9.84100  1.000 22.95239 ? 924  HOH   A O    1 
HETATM 5524 O  O    . HOH   M 6 .   ? -18.84800 15.51900 28.26800 1.000 15.58945 ? 925  HOH   A O    1 
HETATM 5525 O  O    . HOH   M 6 .   ? -9.64600  36.32900 37.41800 1.000 22.04189 ? 926  HOH   A O    1 
HETATM 5526 O  O    . HOH   M 6 .   ? -20.51400 10.97700 33.94600 1.000 8.69254  ? 927  HOH   A O    1 
HETATM 5527 O  O    . HOH   M 6 .   ? 0.38700   4.51300  27.00800 1.000 9.02162  ? 928  HOH   A O    1 
HETATM 5528 O  O    . HOH   M 6 .   ? -12.05100 32.67700 43.75300 1.000 17.17860 ? 929  HOH   A O    1 
HETATM 5529 O  O    . HOH   M 6 .   ? 1.96500   29.57700 15.93700 1.000 17.86868 ? 930  HOH   A O    1 
HETATM 5530 O  O    . HOH   M 6 .   ? -6.75600  15.39600 28.65600 1.000 9.12183  ? 931  HOH   A O    1 
HETATM 5531 O  O    . HOH   M 6 .   ? 2.63500   22.06200 14.20100 1.000 9.23481  ? 932  HOH   A O    1 
HETATM 5532 O  O    . HOH   M 6 .   ? 6.04300   25.47000 44.63400 1.000 10.62997 ? 933  HOH   A O    1 
HETATM 5533 O  O    . HOH   M 6 .   ? -31.58100 10.84600 28.92600 1.000 12.73851 ? 934  HOH   A O    1 
HETATM 5534 O  O    . HOH   M 6 .   ? -26.58100 13.92900 35.52100 1.000 9.01571  ? 935  HOH   A O    1 
HETATM 5535 O  O    . HOH   M 6 .   ? -11.96100 6.44600  41.01500 1.000 16.53031 ? 936  HOH   A O    1 
HETATM 5536 O  O    . HOH   M 6 .   ? 4.14700   2.98800  12.36200 1.000 13.04328 ? 937  HOH   A O    1 
HETATM 5537 O  O    . HOH   M 6 .   ? -27.59100 5.76900  37.29600 1.000 12.83034 ? 938  HOH   A O    1 
HETATM 5538 O  O    . HOH   M 6 .   ? -17.05500 23.72800 6.96900  1.000 16.35500 ? 939  HOH   A O    1 
HETATM 5539 O  O    . HOH   M 6 .   ? 8.54300   14.41400 36.47200 1.000 17.15137 ? 940  HOH   A O    1 
HETATM 5540 O  O    . HOH   M 6 .   ? -21.08200 11.77600 41.44300 1.000 15.67483 ? 941  HOH   A O    1 
HETATM 5541 O  O    . HOH   M 6 .   ? 17.713    29.278   23.442   1.000 14.83711 ? 942  HOH   A O    1 
HETATM 5542 O  O    . HOH   M 6 .   ? -16.56300 10.34400 45.24700 1.000 16.73080 ? 943  HOH   A O    1 
HETATM 5543 O  O    . HOH   M 6 .   ? -12.20300 36.63900 31.75700 1.000 16.91227 ? 944  HOH   A O    1 
HETATM 5544 O  O    . HOH   M 6 .   ? -5.39500  7.27300  7.91500  1.000 10.17692 ? 945  HOH   A O    1 
HETATM 5545 O  O    . HOH   M 6 .   ? 0.77400   29.83300 42.33100 1.000 10.59615 ? 946  HOH   A O    1 
HETATM 5546 O  O    . HOH   M 6 .   ? -27.88000 27.92000 25.79900 1.000 9.76364  ? 947  HOH   A O    1 
HETATM 5547 O  O    . HOH   M 6 .   ? 3.56800   33.25300 21.58900 1.000 22.75770 ? 948  HOH   A O    1 
HETATM 5548 O  O    . HOH   M 6 .   ? -1.13900  3.73000  8.27100  1.000 23.01198 ? 949  HOH   A O    1 
HETATM 5549 O  O    . HOH   M 6 .   ? -15.88500 7.99600  29.28200 1.000 13.15089 ? 950  HOH   A O    1 
HETATM 5550 O  O    . HOH   M 6 .   ? -30.95300 16.71000 21.06300 1.000 23.35627 ? 951  HOH   A O    1 
HETATM 5551 O  O    . HOH   M 6 .   ? 3.46700   6.59700  29.08200 1.000 9.66122  ? 952  HOH   A O    1 
HETATM 5552 O  O    . HOH   M 6 .   ? -1.95000  4.23400  25.43400 1.000 20.09183 ? 953  HOH   A O    1 
HETATM 5553 O  O    . HOH   M 6 .   ? -15.44800 7.44100  26.64800 1.000 8.56076  ? 954  HOH   A O    1 
HETATM 5554 O  O    . HOH   M 6 .   ? -18.43900 11.61200 6.76200  1.000 20.13915 ? 955  HOH   A O    1 
HETATM 5555 O  O    . HOH   M 6 .   ? -29.76800 27.36500 31.03400 1.000 9.15256  ? 956  HOH   A O    1 
HETATM 5556 O  O    . HOH   M 6 .   ? 12.09800  9.74700  34.79300 1.000 18.35005 ? 957  HOH   A O    1 
HETATM 5557 O  O    . HOH   M 6 .   ? 2.00300   12.75500 29.95400 1.000 11.91237 ? 958  HOH   A O    1 
HETATM 5558 O  O    . HOH   M 6 .   ? -12.30000 18.03500 45.64000 1.000 15.47347 ? 959  HOH   A O    1 
HETATM 5559 O  O    . HOH   M 6 .   ? -18.65100 7.67400  43.26100 1.000 21.52899 ? 960  HOH   A O    1 
HETATM 5560 O  O    . HOH   M 6 .   ? -3.91800  14.59400 39.18500 1.000 7.75894  ? 961  HOH   A O    1 
HETATM 5561 O  O    . HOH   M 6 .   ? -30.06200 1.82100  34.28400 1.000 11.16731 ? 962  HOH   A O    1 
HETATM 5562 O  O    . HOH   M 6 .   ? -12.85100 20.17100 43.74300 1.000 11.71892 ? 963  HOH   A O    1 
HETATM 5563 O  O    . HOH   M 6 .   ? 1.98700   11.09800 38.07200 1.000 12.73619 ? 964  HOH   A O    1 
HETATM 5564 O  O    . HOH   M 6 .   ? -7.95600  5.95200  7.55200  1.000 16.85897 ? 965  HOH   A O    1 
HETATM 5565 O  O    . HOH   M 6 .   ? -28.94900 12.35700 35.37600 1.000 17.76086 ? 966  HOH   A O    1 
HETATM 5566 O  O    . HOH   M 6 .   ? -33.82300 12.08300 41.28200 1.000 20.90623 ? 967  HOH   A O    1 
HETATM 5567 O  O    . HOH   M 6 .   ? -33.809   17.155   26.714   1.000 17.30996 ? 968  HOH   A O    1 
HETATM 5568 O  O    . HOH   M 6 .   ? 7.98300   32.18400 40.18500 1.000 16.14641 ? 969  HOH   A O    1 
HETATM 5569 O  O    . HOH   M 6 .   ? 1.26700   24.81000 11.38300 1.000 22.83210 ? 970  HOH   A O    1 
HETATM 5570 O  O    . HOH   M 6 .   ? 4.14400   18.76400 12.04400 1.000 17.68123 ? 971  HOH   A O    1 
HETATM 5571 O  O    . HOH   M 6 .   ? -18.03700 32.98900 37.35800 1.000 13.45353 ? 972  HOH   A O    1 
HETATM 5572 O  O    . HOH   M 6 .   ? -19.04600 4.99800  11.28900 1.000 13.71481 ? 973  HOH   A O    1 
HETATM 5573 O  O    . HOH   M 6 .   ? -5.63600  39.14600 21.95100 1.000 20.47880 ? 974  HOH   A O    1 
HETATM 5574 O  O    . HOH   M 6 .   ? 12.29100  18.28600 24.02100 1.000 21.07081 ? 975  HOH   A O    1 
HETATM 5575 O  O    . HOH   M 6 .   ? -25.08700 25.19100 36.41400 1.000 16.96606 ? 976  HOH   A O    1 
HETATM 5576 O  O    . HOH   M 6 .   ? -26.96000 25.34100 34.28400 1.000 12.64409 ? 977  HOH   A O    1 
HETATM 5577 O  O    . HOH   M 6 .   ? -12.93800 28.86000 6.21200  1.000 23.14458 ? 978  HOH   A O    1 
HETATM 5578 O  O    . HOH   M 6 .   ? -24.49000 10.12200 14.33800 1.000 9.67039  ? 979  HOH   A O    1 
HETATM 5579 O  O    . HOH   M 6 .   ? -30.38200 12.32600 46.10700 1.000 24.44375 ? 980  HOH   A O    1 
HETATM 5580 O  O    . HOH   M 6 .   ? -15.03800 8.82800  9.58100  1.000 18.78360 ? 981  HOH   A O    1 
HETATM 5581 O  O    . HOH   M 6 .   ? 2.03400   19.38000 10.45600 1.000 11.37113 ? 982  HOH   A O    1 
HETATM 5582 O  O    . HOH   M 6 .   ? -27.49000 27.69200 32.84600 1.000 18.66585 ? 983  HOH   A O    1 
HETATM 5583 O  O    . HOH   M 6 .   ? -24.72900 1.00900  17.28300 1.000 12.65764 ? 984  HOH   A O    1 
HETATM 5584 O  O    . HOH   M 6 .   ? 3.11500   24.40000 45.07500 1.000 14.52706 ? 985  HOH   A O    1 
HETATM 5585 O  O    . HOH   M 6 .   ? -22.45000 -2.13600 23.77800 1.000 15.88849 ? 986  HOH   A O    1 
HETATM 5586 O  O    . HOH   M 6 .   ? -5.30400  19.59000 40.33200 1.000 8.38343  ? 987  HOH   A O    1 
HETATM 5587 O  O    . HOH   M 6 .   ? -32.83100 18.12600 35.59000 1.000 18.41458 ? 988  HOH   A O    1 
HETATM 5588 O  O    . HOH   M 6 .   ? -22.43500 33.73400 35.28700 1.000 25.99772 ? 989  HOH   A O    1 
HETATM 5589 O  O    . HOH   M 6 .   ? 3.50700   27.62800 14.00400 1.000 23.64931 ? 990  HOH   A O    1 
HETATM 5590 O  O    . HOH   M 6 .   ? 14.413    22.847   36.938   1.000 15.70121 ? 991  HOH   A O    1 
HETATM 5591 O  O    . HOH   M 6 .   ? -31.53600 11.52000 34.77600 1.000 15.01962 ? 992  HOH   A O    1 
HETATM 5592 O  O    . HOH   M 6 .   ? 17.30200  24.89100 33.28400 1.000 16.29094 ? 993  HOH   A O    1 
HETATM 5593 O  O    . HOH   M 6 .   ? -5.534    4.375    39.624   1.000 21.42435 ? 994  HOH   A O    1 
HETATM 5594 O  O    . HOH   M 6 .   ? 7.29800   34.86100 24.06300 1.000 13.98979 ? 995  HOH   A O    1 
HETATM 5595 O  O    . HOH   M 6 .   ? -31.317   29.531   31.604   1.000 9.97464  ? 996  HOH   A O    1 
HETATM 5596 O  O    . HOH   M 6 .   ? 14.908    15.316   22.499   1.000 18.89903 ? 997  HOH   A O    1 
HETATM 5597 O  O    . HOH   M 6 .   ? -24.704   19.261   5.339    1.000 18.32811 ? 998  HOH   A O    1 
HETATM 5598 O  O    . HOH   M 6 .   ? -24.54200 11.19700 9.91200  1.000 14.69098 ? 999  HOH   A O    1 
HETATM 5599 O  O    . HOH   M 6 .   ? 1.21800   32.24100 44.77600 1.000 0.89647  ? 1000 HOH   A O    1 
HETATM 5600 O  O    . HOH   N 6 .   ? -43.61100 27.87300 53.26600 1.000 6.80557  ? 901  HOH   B O    1 
HETATM 5601 O  O    . HOH   N 6 .   ? -46.73400 40.23000 71.57500 1.000 18.44821 ? 902  HOH   B O    1 
HETATM 5602 O  O    . HOH   N 6 .   ? -36.49500 48.01100 72.92100 1.000 7.17059  ? 903  HOH   B O    1 
HETATM 5603 O  O    . HOH   N 6 .   ? -51.36600 60.93200 46.95300 1.000 23.30538 ? 904  HOH   B O    1 
HETATM 5604 O  O    . HOH   N 6 .   ? -52.58900 27.93300 61.61500 1.000 16.42249 ? 905  HOH   B O    1 
HETATM 5605 O  O    . HOH   N 6 .   ? -48.48400 52.48100 39.29700 1.000 20.62788 ? 906  HOH   B O    1 
HETATM 5606 O  O    . HOH   N 6 .   ? -25.68300 26.27900 38.95100 1.000 30.53168 ? 907  HOH   B O    1 
HETATM 5607 O  O    . HOH   N 6 .   ? -54.10100 51.77400 51.82500 1.000 12.06327 ? 908  HOH   B O    1 
HETATM 5608 O  O    . HOH   N 6 .   ? -44.43200 42.88300 52.20400 1.000 22.50730 ? 909  HOH   B O    1 
HETATM 5609 O  O    . HOH   N 6 .   ? -18.34200 40.66000 56.36800 1.000 18.39439 ? 910  HOH   B O    1 
HETATM 5610 O  O    . HOH   N 6 .   ? -37.47600 28.61300 77.65800 1.000 18.62990 ? 911  HOH   B O    1 
HETATM 5611 O  O    . HOH   N 6 .   ? -39.67200 41.95000 59.71900 1.000 11.14412 ? 912  HOH   B O    1 
HETATM 5612 O  O    . HOH   N 6 .   ? -22.26400 32.59500 39.84600 1.000 23.25868 ? 913  HOH   B O    1 
HETATM 5613 O  O    . HOH   N 6 .   ? -30.85400 38.41100 57.20800 1.000 8.70820  ? 914  HOH   B O    1 
HETATM 5614 O  O    . HOH   N 6 .   ? -47.39800 53.10700 54.31900 1.000 14.83545 ? 915  HOH   B O    1 
HETATM 5615 O  O    . HOH   N 6 .   ? -38.42000 33.48500 44.43900 1.000 22.23479 ? 916  HOH   B O    1 
HETATM 5616 O  O    . HOH   N 6 .   ? -34.42900 41.47600 58.35400 1.000 10.46721 ? 917  HOH   B O    1 
HETATM 5617 O  O    . HOH   N 6 .   ? -42.38300 46.29300 42.94400 1.000 13.17450 ? 918  HOH   B O    1 
HETATM 5618 O  O    . HOH   N 6 .   ? -39.43100 25.62300 49.61700 1.000 11.35335 ? 919  HOH   B O    1 
HETATM 5619 O  O    . HOH   N 6 .   ? -41.65600 55.90300 65.10100 1.000 15.71884 ? 920  HOH   B O    1 
HETATM 5620 O  O    . HOH   N 6 .   ? -55.62400 33.47900 59.96200 1.000 5.03445  ? 921  HOH   B O    1 
HETATM 5621 O  O    . HOH   N 6 .   ? -36.35500 28.62500 54.92300 1.000 12.60924 ? 922  HOH   B O    1 
HETATM 5622 O  O    . HOH   N 6 .   ? -33.18700 53.38900 70.80800 1.000 7.53267  ? 923  HOH   B O    1 
HETATM 5623 O  O    . HOH   N 6 .   ? -32.10600 28.60800 53.32000 1.000 8.34303  ? 924  HOH   B O    1 
HETATM 5624 O  O    . HOH   N 6 .   ? -26.35200 23.03800 45.79900 1.000 15.36961 ? 925  HOH   B O    1 
HETATM 5625 O  O    . HOH   N 6 .   ? -28.72800 37.26500 44.83200 1.000 15.34230 ? 926  HOH   B O    1 
HETATM 5626 O  O    . HOH   N 6 .   ? -49.07000 19.19400 64.07100 1.000 31.46184 ? 927  HOH   B O    1 
HETATM 5627 O  O    . HOH   N 6 .   ? -10.39600 37.32500 49.51400 1.000 25.29103 ? 928  HOH   B O    1 
HETATM 5628 O  O    . HOH   N 6 .   ? -42.84300 38.30100 57.48800 1.000 10.79500 ? 929  HOH   B O    1 
HETATM 5629 O  O    . HOH   N 6 .   ? -21.11500 29.30300 40.64100 1.000 16.65751 ? 930  HOH   B O    1 
HETATM 5630 O  O    . HOH   N 6 .   ? -21.73300 41.05600 55.81200 1.000 12.32351 ? 931  HOH   B O    1 
HETATM 5631 O  O    . HOH   N 6 .   ? -35.74800 47.70100 44.77700 1.000 20.02288 ? 932  HOH   B O    1 
HETATM 5632 O  O    . HOH   N 6 .   ? -50.34800 41.74900 52.40100 1.000 24.26646 ? 933  HOH   B O    1 
HETATM 5633 O  O    . HOH   N 6 .   ? -30.85300 24.77200 44.59700 1.000 8.57069  ? 934  HOH   B O    1 
HETATM 5634 O  O    . HOH   N 6 .   ? -34.82300 22.01900 72.90100 1.000 18.17205 ? 935  HOH   B O    1 
HETATM 5635 O  O    . HOH   N 6 .   ? -55.95300 31.89500 62.14100 1.000 11.35478 ? 936  HOH   B O    1 
HETATM 5636 O  O    . HOH   N 6 .   ? -41.84800 53.49900 70.05700 1.000 21.76993 ? 937  HOH   B O    1 
HETATM 5637 O  O    . HOH   N 6 .   ? -31.29300 33.69900 46.84100 1.000 12.99270 ? 938  HOH   B O    1 
HETATM 5638 O  O    . HOH   N 6 .   ? -45.15900 21.71200 64.45800 1.000 13.48815 ? 939  HOH   B O    1 
HETATM 5639 O  O    . HOH   N 6 .   ? -23.22000 28.70600 74.56400 1.000 13.56069 ? 940  HOH   B O    1 
HETATM 5640 O  O    . HOH   N 6 .   ? -36.39000 54.22400 49.00200 1.000 10.02550 ? 941  HOH   B O    1 
HETATM 5641 O  O    . HOH   N 6 .   ? -8.84400  21.51700 60.48600 1.000 24.42955 ? 942  HOH   B O    1 
HETATM 5642 O  O    . HOH   N 6 .   ? -27.37500 41.85900 46.10700 1.000 20.28523 ? 943  HOH   B O    1 
HETATM 5643 O  O    . HOH   N 6 .   ? -18.97500 33.54200 51.66400 1.000 17.32237 ? 944  HOH   B O    1 
HETATM 5644 O  O    . HOH   N 6 .   ? -36.57000 33.59300 41.87300 1.000 11.48989 ? 945  HOH   B O    1 
HETATM 5645 O  O    . HOH   N 6 .   ? -18.25700 40.44700 50.19000 1.000 8.53190  ? 946  HOH   B O    1 
HETATM 5646 O  O    . HOH   N 6 .   ? -37.133   36.641   84.175   1.000 10.54714 ? 947  HOH   B O    1 
HETATM 5647 O  O    . HOH   N 6 .   ? -26.24700 50.61800 57.01300 1.000 5.31321  ? 948  HOH   B O    1 
HETATM 5648 O  O    . HOH   N 6 .   ? -39.80600 45.74900 56.40100 1.000 12.64170 ? 949  HOH   B O    1 
HETATM 5649 O  O    . HOH   N 6 .   ? -32.84400 16.14900 50.02400 1.000 13.70986 ? 950  HOH   B O    1 
HETATM 5650 O  O    . HOH   N 6 .   ? -50.32100 40.11800 50.09200 1.000 15.41391 ? 951  HOH   B O    1 
HETATM 5651 O  O    . HOH   N 6 .   ? -30.71300 57.30800 50.12600 1.000 23.87971 ? 952  HOH   B O    1 
HETATM 5652 O  O    . HOH   N 6 .   ? -35.92800 16.84800 53.61400 1.000 12.78344 ? 953  HOH   B O    1 
HETATM 5653 O  O    . HOH   N 6 .   ? -28.70800 59.03400 55.38400 1.000 23.14962 ? 954  HOH   B O    1 
HETATM 5654 O  O    . HOH   N 6 .   ? -20.34700 46.73800 57.14700 1.000 17.75341 ? 955  HOH   B O    1 
HETATM 5655 O  O    . HOH   N 6 .   ? -11.486   35.140   61.520   1.000 22.80236 ? 956  HOH   B O    1 
HETATM 5656 O  O    . HOH   N 6 .   ? -21.11700 31.59200 71.39000 1.000 9.21249  ? 957  HOH   B O    1 
HETATM 5657 O  O    . HOH   N 6 .   ? -47.99500 51.14800 69.58300 1.000 21.62388 ? 958  HOH   B O    1 
HETATM 5658 O  O    . HOH   N 6 .   ? -15.48600 39.02600 49.27200 1.000 18.49118 ? 959  HOH   B O    1 
HETATM 5659 O  O    . HOH   N 6 .   ? -52.524   51.532   37.944   1.000 18.59062 ? 960  HOH   B O    1 
HETATM 5660 O  O    . HOH   N 6 .   ? -53.86100 26.44800 54.52300 1.000 13.66135 ? 961  HOH   B O    1 
HETATM 5661 O  O    . HOH   N 6 .   ? -48.86600 43.96800 43.28600 1.000 19.50252 ? 962  HOH   B O    1 
HETATM 5662 O  O    . HOH   N 6 .   ? -35.93700 21.39900 41.75000 1.000 21.03158 ? 963  HOH   B O    1 
HETATM 5663 O  O    . HOH   N 6 .   ? -21.76700 42.39500 47.38600 1.000 18.86730 ? 964  HOH   B O    1 
HETATM 5664 O  O    . HOH   N 6 .   ? -48.31500 43.15700 71.41100 1.000 14.82836 ? 965  HOH   B O    1 
HETATM 5665 O  O    . HOH   N 6 .   ? -26.408   43.030   78.357   1.000 19.18896 ? 966  HOH   B O    1 
HETATM 5666 O  O    . HOH   N 6 .   ? -42.66700 48.81500 74.57100 1.000 17.52678 ? 967  HOH   B O    1 
HETATM 5667 O  O    . HOH   N 6 .   ? -57.65000 48.17800 50.19100 1.000 17.45978 ? 968  HOH   B O    1 
HETATM 5668 O  O    . HOH   N 6 .   ? -19.62200 34.98200 41.54400 1.000 22.45383 ? 969  HOH   B O    1 
HETATM 5669 O  O    . HOH   N 6 .   ? -51.24700 25.67600 52.81900 1.000 10.20169 ? 970  HOH   B O    1 
HETATM 5670 O  O    . HOH   N 6 .   ? -39.16500 46.42600 59.11100 1.000 9.71763  ? 971  HOH   B O    1 
HETATM 5671 O  O    . HOH   N 6 .   ? -42.81000 24.96800 79.67400 1.000 23.12880 ? 972  HOH   B O    1 
HETATM 5672 O  O    . HOH   N 6 .   ? -57.70300 36.64100 59.29800 1.000 17.50780 ? 973  HOH   B O    1 
HETATM 5673 O  O    . HOH   N 6 .   ? -36.30600 59.12300 66.73600 1.000 15.64702 ? 974  HOH   B O    1 
HETATM 5674 O  O    . HOH   N 6 .   ? -50.97100 28.24000 51.77400 1.000 11.44385 ? 975  HOH   B O    1 
HETATM 5675 O  O    . HOH   N 6 .   ? -45.36900 51.97600 69.97000 1.000 26.27242 ? 976  HOH   B O    1 
HETATM 5676 O  O    . HOH   N 6 .   ? -32.84200 20.34400 74.88100 1.000 21.02935 ? 977  HOH   B O    1 
HETATM 5677 O  O    . HOH   N 6 .   ? -41.54300 18.77200 70.07800 1.000 20.35674 ? 978  HOH   B O    1 
HETATM 5678 O  O    . HOH   N 6 .   ? -23.16900 12.94900 50.90900 1.000 22.44332 ? 979  HOH   B O    1 
HETATM 5679 O  O    . HOH   N 6 .   ? -49.83400 35.90900 75.59300 1.000 23.30331 ? 980  HOH   B O    1 
HETATM 5680 O  O    . HOH   N 6 .   ? -51.56000 28.54200 74.25800 1.000 13.01342 ? 981  HOH   B O    1 
HETATM 5681 O  O    . HOH   N 6 .   ? -19.42900 17.61300 65.05300 1.000 28.68352 ? 982  HOH   B O    1 
HETATM 5682 O  O    . HOH   N 6 .   ? -8.263    40.606   56.214   1.000 12.86979 ? 983  HOH   B O    1 
HETATM 5683 O  O    . HOH   N 6 .   ? -45.28600 42.52800 44.31900 1.000 22.12320 ? 984  HOH   B O    1 
HETATM 5684 O  O    . HOH   N 6 .   ? -16.55400 52.42600 53.56500 1.000 29.87464 ? 985  HOH   B O    1 
HETATM 5685 O  O    . HOH   N 6 .   ? -15.21000 22.09400 43.17500 1.000 17.73779 ? 986  HOH   B O    1 
HETATM 5686 O  O    . HOH   N 6 .   ? -56.610   35.579   50.383   1.000 13.08186 ? 987  HOH   B O    1 
HETATM 5687 O  O    . HOH   N 6 .   ? -52.82900 41.09200 50.66200 1.000 14.91713 ? 988  HOH   B O    1 
HETATM 5688 O  O    . HOH   N 6 .   ? -28.76400 44.60400 79.48300 1.000 14.88671 ? 989  HOH   B O    1 
HETATM 5689 O  O    . HOH   N 6 .   ? -40.94400 43.69200 40.27300 1.000 11.58914 ? 990  HOH   B O    1 
HETATM 5690 O  O    . HOH   N 6 .   ? -55.15200 58.92100 50.53600 1.000 17.29670 ? 991  HOH   B O    1 
HETATM 5691 O  O    . HOH   N 6 .   ? -10.637   40.457   62.218   1.000 16.20740 ? 992  HOH   B O    1 
HETATM 5692 O  O    . HOH   N 6 .   ? -21.67600 34.16000 74.89400 1.000 17.55407 ? 993  HOH   B O    1 
HETATM 5693 O  O    . HOH   N 6 .   ? -28.63100 27.42200 36.63100 1.000 21.98560 ? 994  HOH   B O    1 
HETATM 5694 O  O    . HOH   N 6 .   ? -36.62700 23.98200 38.81500 1.000 13.91440 ? 995  HOH   B O    1 
HETATM 5695 O  O    . HOH   N 6 .   ? -43.36100 39.34300 42.05200 1.000 27.87349 ? 996  HOH   B O    1 
HETATM 5696 O  O    . HOH   N 6 .   ? -55.95600 43.40000 55.61000 1.000 15.14164 ? 997  HOH   B O    1 
HETATM 5697 O  O    . HOH   N 6 .   ? -52.588   30.812   75.727   1.000 20.10459 ? 998  HOH   B O    1 
HETATM 5698 O  O    . HOH   N 6 .   ? -12.11900 20.47900 56.57100 1.000 19.87469 ? 999  HOH   B O    1 
HETATM 5699 O  O    . HOH   N 6 .   ? -8.982    37.944   63.178   1.000 26.61458 ? 1000 HOH   B O    1 
HETATM 5700 O  O    . HOH   N 6 .   ? -19.88400 25.57000 71.95400 1.000 17.55216 ? 1001 HOH   B O    1 
HETATM 5701 O  O    . HOH   N 6 .   ? -15.84400 18.98900 50.97300 1.000 19.01735 ? 1002 HOH   B O    1 
HETATM 5702 O  O    . HOH   N 6 .   ? -53.05200 30.61700 51.06700 1.000 15.08092 ? 1003 HOH   B O    1 
HETATM 5703 O  O    . HOH   N 6 .   ? -48.68200 54.09400 72.16900 1.000 23.33276 ? 1004 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 
1    N N   . PRO A 8   ? 0.38567 0.35392 0.30012 0.07179  0.04939  0.07642  442 PRO A N   
2    C CA  . PRO A 8   ? 0.42345 0.39370 0.35014 0.06407  0.04589  0.07108  442 PRO A CA  
3    C C   . PRO A 8   ? 0.36909 0.34194 0.29572 0.06392  0.03607  0.06425  442 PRO A C   
4    O O   . PRO A 8   ? 0.43254 0.40231 0.35686 0.06683  0.03408  0.06615  442 PRO A O   
5    C CB  . PRO A 8   ? 0.31281 0.27762 0.25278 0.05824  0.05205  0.07533  442 PRO A CB  
6    C CG  . PRO A 8   ? 0.31033 0.27093 0.24620 0.06172  0.06046  0.08304  442 PRO A CG  
7    C CD  . PRO A 8   ? 0.33994 0.30209 0.26039 0.07039  0.05687  0.08289  442 PRO A CD  
8    N N   . ILE A 9   ? 0.28030 0.25868 0.20983 0.06063  0.03028  0.05654  443 ILE A N   
9    C CA  . ILE A 9   ? 0.30238 0.28397 0.23298 0.05967  0.02144  0.04971  443 ILE A CA  
10   C C   . ILE A 9   ? 0.19994 0.18334 0.14458 0.05096  0.01962  0.04498  443 ILE A C   
11   O O   . ILE A 9   ? 0.17152 0.15675 0.12098 0.04717  0.02154  0.04334  443 ILE A O   
12   C CB  . ILE A 9   ? 0.36311 0.34934 0.28361 0.06411  0.01567  0.04444  443 ILE A CB  
13   C CG1 . ILE A 9   ? 0.38439 0.36986 0.28964 0.07373  0.01687  0.04862  443 ILE A CG1 
14   C CG2 . ILE A 9   ? 0.23901 0.22881 0.16295 0.06196  0.00714  0.03725  443 ILE A CG2 
15   C CD1 . ILE A 9   ? 0.37841 0.36887 0.27371 0.07858  0.01061  0.04239  443 ILE A CD1 
16   N N   . THR A 10  ? 0.22153 0.20492 0.17226 0.04839  0.01585  0.04273  444 THR A N   
17   C CA  . THR A 10  ? 0.14818 0.13414 0.11052 0.04105  0.01313  0.03774  444 THR A CA  
18   C C   . THR A 10  ? 0.13732 0.12794 0.09774 0.04072  0.00552  0.03114  444 THR A C   
19   O O   . THR A 10  ? 0.26214 0.25400 0.21740 0.04464  0.00133  0.02986  444 THR A O   
20   C CB  . THR A 10  ? 0.16385 0.14726 0.13476 0.03827  0.01420  0.03904  444 THR A CB  
21   O OG1 . THR A 10  ? 0.14447 0.12297 0.11912 0.03756  0.02160  0.04473  444 THR A OG1 
22   C CG2 . THR A 10  ? 0.14398 0.13105 0.12545 0.03146  0.01098  0.03352  444 THR A CG2 
23   N N   . GLY A 11  ? 0.13827 0.13150 0.10319 0.03621  0.00383  0.02701  445 GLY A N   
24   C CA  . GLY A 11  ? 0.19301 0.18975 0.15775 0.03483  -0.00257 0.02100  445 GLY A CA  
25   C C   . GLY A 11  ? 0.20252 0.20135 0.17693 0.02923  -0.00501 0.01816  445 GLY A C   
26   O O   . GLY A 11  ? 0.13594 0.13395 0.11781 0.02557  -0.00199 0.01972  445 GLY A O   
27   N N   . LEU A 12  ? 0.13207 0.13413 0.10655 0.02861  -0.01049 0.01359  446 LEU A N   
28   C CA  . LEU A 12  ? 0.10584 0.11077 0.08878 0.02359  -0.01275 0.01074  446 LEU A CA  
29   C C   . LEU A 12  ? 0.14700 0.15480 0.13039 0.02136  -0.01741 0.00562  446 LEU A C   
30   O O   . LEU A 12  ? 0.22079 0.22998 0.19900 0.02465  -0.02091 0.00310  446 LEU A O   
31   C CB  . LEU A 12  ? 0.11437 0.12055 0.09897 0.02550  -0.01380 0.01138  446 LEU A CB  
32   C CG  . LEU A 12  ? 0.09829 0.10825 0.09142 0.02124  -0.01571 0.00857  446 LEU A CG  
33   C CD1 . LEU A 12  ? 0.10074 0.10984 0.09556 0.02390  -0.01462 0.01075  446 LEU A CD1 
34   C CD2 . LEU A 12  ? 0.09657 0.11163 0.09064 0.02004  -0.02086 0.00357  446 LEU A CD2 
35   N N   . VAL A 13  ? 0.12648 0.13518 0.11618 0.01591  -0.01745 0.00401  447 VAL A N   
36   C CA  . VAL A 13  ? 0.14601 0.15632 0.13732 0.01299  -0.02102 -0.00019 447 VAL A CA  
37   C C   . VAL A 13  ? 0.19894 0.21289 0.19801 0.00832  -0.02187 -0.00159 447 VAL A C   
38   O O   . VAL A 13  ? 0.14365 0.15787 0.14697 0.00600  -0.01923 0.00033  447 VAL A O   
39   C CB  . VAL A 13  ? 0.11223 0.11929 0.10223 0.01153  -0.01996 -0.00034 447 VAL A CB  
40   C CG1 . VAL A 13  ? 0.16968 0.17610 0.16415 0.00865  -0.01640 0.00236  447 VAL A CG1 
41   C CG2 . VAL A 13  ? 0.14087 0.14807 0.13269 0.00856  -0.02339 -0.00442 447 VAL A CG2 
42   N N   . TYR A 14  ? 0.12420 0.14162 0.12539 0.00710  -0.02550 -0.00531 448 TYR A N   
43   C CA  . TYR A 14  ? 0.14088 0.16277 0.14940 0.00280  -0.02617 -0.00691 448 TYR A CA  
44   C C   . TYR A 14  ? 0.16162 0.18604 0.17240 0.00070  -0.02976 -0.01131 448 TYR A C   
45   O O   . TYR A 14  ? 0.24133 0.26685 0.24900 0.00394  -0.03291 -0.01400 448 TYR A O   
46   C CB  . TYR A 14  ? 0.13914 0.16478 0.15011 0.00476  -0.02609 -0.00636 448 TYR A CB  
47   C CG  . TYR A 14  ? 0.12750 0.15940 0.14569 0.00132  -0.02743 -0.00905 448 TYR A CG  
48   C CD1 . TYR A 14  ? 0.10873 0.14216 0.13182 -0.00272 -0.02503 -0.00821 448 TYR A CD1 
49   C CD2 . TYR A 14  ? 0.14220 0.17937 0.16241 0.00237  -0.03107 -0.01269 448 TYR A CD2 
50   C CE1 . TYR A 14  ? 0.11709 0.15683 0.14647 -0.00564 -0.02564 -0.01044 448 TYR A CE1 
51   C CE2 . TYR A 14  ? 0.12520 0.16906 0.15290 -0.00089 -0.03182 -0.01521 448 TYR A CE2 
52   C CZ  . TYR A 14  ? 0.19398 0.23895 0.22604 -0.00492 -0.02880 -0.01383 448 TYR A CZ  
53   O OH  . TYR A 14  ? 0.14090 0.19307 0.18009 -0.00796 -0.02894 -0.01610 448 TYR A OH  
54   N N   . ASP A 15  ? 0.16693 0.19244 0.18326 -0.00463 -0.02919 -0.01211 449 ASP A N   
55   C CA  . ASP A 15  ? 0.12512 0.15278 0.14564 -0.00782 -0.03187 -0.01619 449 ASP A CA  
56   C C   . ASP A 15  ? 0.15663 0.18958 0.18497 -0.01258 -0.03064 -0.01640 449 ASP A C   
57   O O   . ASP A 15  ? 0.31399 0.34544 0.34349 -0.01543 -0.02752 -0.01347 449 ASP A O   
58   C CB  . ASP A 15  ? 0.12876 0.14996 0.14721 -0.00962 -0.03182 -0.01664 449 ASP A CB  
59   C CG  . ASP A 15  ? 0.17072 0.19287 0.19266 -0.01166 -0.03527 -0.02187 449 ASP A CG  
60   O OD1 . ASP A 15  ? 0.17294 0.19992 0.20254 -0.01588 -0.03568 -0.02382 449 ASP A OD1 
61   O OD2 . ASP A 15  ? 0.19115 0.20964 0.20863 -0.00905 -0.03752 -0.02442 449 ASP A OD2 
62   N N   . GLN A 16  ? 0.12480 0.16467 0.15836 -0.01304 -0.03311 -0.02002 450 GLN A N   
63   C CA  . GLN A 16  ? 0.11658 0.16291 0.15813 -0.01731 -0.03174 -0.02062 450 GLN A CA  
64   C C   . GLN A 16  ? 0.11935 0.16289 0.16424 -0.02324 -0.02932 -0.01954 450 GLN A C   
65   O O   . GLN A 16  ? 0.10583 0.15267 0.15466 -0.02645 -0.02637 -0.01772 450 GLN A O   
66   C CB  . GLN A 16  ? 0.15376 0.20849 0.20116 -0.01678 -0.03530 -0.02559 450 GLN A CB  
67   N N   . ARG A 17  ? 0.09854 0.13567 0.14145 -0.02435 -0.03033 -0.02046 451 ARG A N   
68   C CA  . ARG A 17  ? 0.08441 0.11723 0.13019 -0.02962 -0.02790 -0.01896 451 ARG A CA  
69   C C   . ARG A 17  ? 0.12705 0.15666 0.16930 -0.03007 -0.02385 -0.01341 451 ARG A C   
70   O O   . ARG A 17  ? 0.18533 0.21370 0.23032 -0.03423 -0.02103 -0.01115 451 ARG A O   
71   C CB  . ARG A 17  ? 0.12202 0.14702 0.16530 -0.02959 -0.02987 -0.02102 451 ARG A CB  
72   C CG  . ARG A 17  ? 0.20782 0.23617 0.25602 -0.03025 -0.03411 -0.02758 451 ARG A CG  
73   C CD  . ARG A 17  ? 0.29581 0.31586 0.34089 -0.02967 -0.03613 -0.03013 451 ARG A CD  
74   N NE  . ARG A 17  ? 0.23994 0.25658 0.27515 -0.02315 -0.03753 -0.02947 451 ARG A NE  
75   C CZ  . ARG A 17  ? 0.21688 0.22569 0.24689 -0.02122 -0.03830 -0.03029 451 ARG A CZ  
76   N NH1 . ARG A 17  ? 0.30954 0.31186 0.34303 -0.02514 -0.03803 -0.03174 451 ARG A NH1 
77   N NH2 . ARG A 17  ? 0.18016 0.18739 0.20146 -0.01511 -0.03905 -0.02952 451 ARG A NH2 
78   N N   . MET A 18  ? 0.13899 0.16741 0.17540 -0.02580 -0.02342 -0.01118 452 MET A N   
79   C CA  . MET A 18  ? 0.17559 0.20256 0.20943 -0.02594 -0.02019 -0.00693 452 MET A CA  
80   C C   . MET A 18  ? 0.12008 0.15437 0.15833 -0.02813 -0.01803 -0.00618 452 MET A C   
81   O O   . MET A 18  ? 0.14667 0.18072 0.18330 -0.02887 -0.01538 -0.00308 452 MET A O   
82   C CB  . MET A 18  ? 0.10152 0.12641 0.12991 -0.02132 -0.02022 -0.00551 452 MET A CB  
83   C CG  . MET A 18  ? 0.11447 0.13171 0.13756 -0.01935 -0.02067 -0.00463 452 MET A CG  
84   S SD  . MET A 18  ? 0.15603 0.17168 0.17413 -0.01446 -0.01985 -0.00283 452 MET A SD  
85   C CE  . MET A 18  ? 0.11892 0.13760 0.13662 -0.01121 -0.02205 -0.00528 452 MET A CE  
86   N N   . MET A 19  ? 0.12097 0.16235 0.16457 -0.02873 -0.01923 -0.00922 453 MET A N   
87   C CA  . MET A 19  ? 0.11010 0.15931 0.15850 -0.03075 -0.01706 -0.00910 453 MET A CA  
88   C C   . MET A 19  ? 0.07143 0.12121 0.12357 -0.03597 -0.01423 -0.00756 453 MET A C   
89   O O   . MET A 19  ? 0.08238 0.13839 0.13730 -0.03760 -0.01148 -0.00655 453 MET A O   
90   C CB  . MET A 19  ? 0.08020 0.13729 0.13390 -0.02952 -0.01928 -0.01308 453 MET A CB  
91   C CG  . MET A 19  ? 0.06646 0.12328 0.11670 -0.02402 -0.02143 -0.01392 453 MET A CG  
92   S SD  . MET A 19  ? 0.19696 0.26357 0.25342 -0.02190 -0.02384 -0.01812 453 MET A SD  
93   C CE  . MET A 19  ? 0.09040 0.16440 0.15135 -0.02392 -0.02013 -0.01740 453 MET A CE  
94   N N   . LEU A 20  ? 0.07683 0.12005 0.12912 -0.03850 -0.01455 -0.00729 454 LEU A N   
95   C CA  . LEU A 20  ? 0.08180 0.12474 0.13874 -0.04391 -0.01143 -0.00560 454 LEU A CA  
96   C C   . LEU A 20  ? 0.08360 0.12403 0.13569 -0.04422 -0.00733 0.00001  454 LEU A C   
97   O O   . LEU A 20  ? 0.08674 0.13018 0.14207 -0.04784 -0.00358 0.00234  454 LEU A O   
98   C CB  . LEU A 20  ? 0.09306 0.12840 0.15186 -0.04643 -0.01295 -0.00718 454 LEU A CB  
99   C CG  . LEU A 20  ? 0.08822 0.12746 0.15281 -0.04658 -0.01722 -0.01356 454 LEU A CG  
100  C CD1 . LEU A 20  ? 0.11858 0.15039 0.18588 -0.04958 -0.01860 -0.01586 454 LEU A CD1 
101  C CD2 . LEU A 20  ? 0.12596 0.17683 0.19964 -0.04920 -0.01661 -0.01624 454 LEU A CD2 
102  N N   . HIS A 21  ? 0.08235 0.11786 0.12679 -0.04029 -0.00791 0.00220  455 HIS A N   
103  C CA  . HIS A 21  ? 0.09170 0.12667 0.13093 -0.03923 -0.00494 0.00675  455 HIS A CA  
104  C C   . HIS A 21  ? 0.12971 0.17480 0.17107 -0.03935 -0.00283 0.00657  455 HIS A C   
105  O O   . HIS A 21  ? 0.13844 0.18916 0.18104 -0.03688 -0.00460 0.00345  455 HIS A O   
106  C CB  . HIS A 21  ? 0.08108 0.11188 0.11370 -0.03452 -0.00683 0.00732  455 HIS A CB  
107  C CG  . HIS A 21  ? 0.08922 0.12090 0.11662 -0.03249 -0.00483 0.01084  455 HIS A CG  
108  N ND1 . HIS A 21  ? 0.09082 0.11988 0.11553 -0.03390 -0.00182 0.01532  455 HIS A ND1 
109  C CD2 . HIS A 21  ? 0.07754 0.11255 0.10199 -0.02890 -0.00555 0.01031  455 HIS A CD2 
110  C CE1 . HIS A 21  ? 0.08857 0.12001 0.10810 -0.03072 -0.00118 0.01728  455 HIS A CE1 
111  N NE2 . HIS A 21  ? 0.08149 0.11684 0.10141 -0.02792 -0.00354 0.01385  455 HIS A NE2 
112  N N   . HIS A 22  ? 0.08834 0.13556 0.13001 -0.04198 0.00122  0.01001  456 HIS A N   
113  C CA  . HIS A 22  ? 0.08483 0.14257 0.12910 -0.04228 0.00356  0.00936  456 HIS A CA  
114  C C   . HIS A 22  ? 0.10065 0.15924 0.13998 -0.04250 0.00799  0.01457  456 HIS A C   
115  O O   . HIS A 22  ? 0.19388 0.24496 0.23017 -0.04404 0.01007  0.01914  456 HIS A O   
116  C CB  . HIS A 22  ? 0.16478 0.22884 0.21860 -0.04629 0.00421  0.00637  456 HIS A CB  
117  C CG  . HIS A 22  ? 0.10377 0.16472 0.16159 -0.05173 0.00774  0.00931  456 HIS A CG  
118  N ND1 . HIS A 22  ? 0.09800 0.15012 0.15795 -0.05426 0.00624  0.00900  456 HIS A ND1 
119  C CD2 . HIS A 22  ? 0.13640 0.20166 0.19685 -0.05521 0.01305  0.01262  456 HIS A CD2 
120  C CE1 . HIS A 22  ? 0.10914 0.15955 0.17355 -0.05943 0.01043  0.01192  456 HIS A CE1 
121  N NE2 . HIS A 22  ? 0.22272 0.28105 0.28744 -0.06018 0.01489  0.01455  456 HIS A NE2 
122  N N   . ASN A 23  ? 0.10001 0.16775 0.13825 -0.04050 0.00942  0.01378  457 ASN A N   
123  C CA  . ASN A 23  ? 0.09227 0.16329 0.12507 -0.03979 0.01365  0.01819  457 ASN A CA  
124  C C   . ASN A 23  ? 0.12764 0.20599 0.16648 -0.04389 0.01824  0.01902  457 ASN A C   
125  O O   . ASN A 23  ? 0.18741 0.27559 0.23115 -0.04359 0.01822  0.01494  457 ASN A O   
126  C CB  . ASN A 23  ? 0.08841 0.16564 0.11630 -0.03472 0.01220  0.01591  457 ASN A CB  
127  C CG  . ASN A 23  ? 0.13965 0.22042 0.15995 -0.03268 0.01581  0.02016  457 ASN A CG  
128  O OD1 . ASN A 23  ? 0.11195 0.19451 0.13213 -0.03528 0.02063  0.02436  457 ASN A OD1 
129  N ND2 . ASN A 23  ? 0.13867 0.22090 0.15272 -0.02785 0.01356  0.01899  457 ASN A ND2 
130  N N   . MET A 24  ? 0.15198 0.22552 0.19089 -0.04766 0.02246  0.02440  458 MET A N   
131  C CA  . MET A 24  ? 0.15817 0.23807 0.20456 -0.05260 0.02742  0.02545  458 MET A CA  
132  C C   . MET A 24  ? 0.24222 0.33131 0.28423 -0.05101 0.03254  0.02850  458 MET A C   
133  O O   . MET A 24  ? 0.17330 0.27041 0.22207 -0.05456 0.03692  0.02862  458 MET A O   
134  C CB  . MET A 24  ? 0.24756 0.31783 0.29708 -0.05793 0.03047  0.03000  458 MET A CB  
135  C CG  . MET A 24  ? 0.25853 0.32013 0.29793 -0.05633 0.03382  0.03789  458 MET A CG  
136  S SD  . MET A 24  ? 0.45790 0.50770 0.50217 -0.06305 0.03864  0.04371  458 MET A SD  
137  C CE  . MET A 24  ? 0.33985 0.38000 0.38911 -0.06400 0.03156  0.03779  458 MET A CE  
138  N N   . TRP A 25  ? 0.17893 0.26787 0.21008 -0.04562 0.03213  0.03065  459 TRP A N   
139  C CA  . TRP A 25  ? 0.20362 0.30196 0.22919 -0.04308 0.03653  0.03298  459 TRP A CA  
140  C C   . TRP A 25  ? 0.23182 0.34086 0.25742 -0.03873 0.03351  0.02620  459 TRP A C   
141  O O   . TRP A 25  ? 0.43876 0.55742 0.46084 -0.03645 0.03687  0.02655  459 TRP A O   
142  C CB  . TRP A 25  ? 0.20831 0.30086 0.22122 -0.03929 0.03818  0.03962  459 TRP A CB  
143  C CG  . TRP A 25  ? 0.29197 0.37246 0.30416 -0.04290 0.04126  0.04668  459 TRP A CG  
144  C CD1 . TRP A 25  ? 0.30107 0.38030 0.31355 -0.04657 0.04847  0.05362  459 TRP A CD1 
145  C CD2 . TRP A 25  ? 0.31920 0.38667 0.33076 -0.04319 0.03750  0.04744  459 TRP A CD2 
146  N NE1 . TRP A 25  ? 0.28247 0.34775 0.29477 -0.04925 0.04929  0.05860  459 TRP A NE1 
147  C CE2 . TRP A 25  ? 0.31177 0.36990 0.32334 -0.04701 0.04242  0.05464  459 TRP A CE2 
148  C CE3 . TRP A 25  ? 0.28052 0.34328 0.29169 -0.04055 0.03081  0.04278  459 TRP A CE3 
149  C CZ2 . TRP A 25  ? 0.26910 0.31328 0.28022 -0.04794 0.04040  0.05671  459 TRP A CZ2 
150  C CZ3 . TRP A 25  ? 0.25787 0.30779 0.26821 -0.04136 0.02905  0.04503  459 TRP A CZ3 
151  C CH2 . TRP A 25  ? 0.25548 0.29620 0.26575 -0.04486 0.03358  0.05164  459 TRP A CH2 
152  N N   . ASP A 26  ? 0.10181 0.20920 0.13130 -0.03740 0.02755  0.02011  460 ASP A N   
153  C CA  . ASP A 26  ? 0.11592 0.23136 0.14573 -0.03313 0.02447  0.01365  460 ASP A CA  
154  C C   . ASP A 26  ? 0.11939 0.23213 0.15711 -0.03395 0.01955  0.00821  460 ASP A C   
155  O O   . ASP A 26  ? 0.10763 0.21326 0.14314 -0.03198 0.01524  0.00684  460 ASP A O   
156  C CB  . ASP A 26  ? 0.11048 0.22474 0.13064 -0.02774 0.02215  0.01355  460 ASP A CB  
157  C CG  . ASP A 26  ? 0.18021 0.30130 0.20180 -0.02371 0.01869  0.00623  460 ASP A CG  
158  O OD1 . ASP A 26  ? 0.23608 0.36368 0.26488 -0.02442 0.01881  0.00187  460 ASP A OD1 
159  O OD2 . ASP A 26  ? 0.23658 0.35649 0.25259 -0.01973 0.01576  0.00461  460 ASP A OD2 
160  N N   . SER A 27  ? 0.10318 0.22225 0.14998 -0.03652 0.02042  0.00526  461 SER A N   
161  C CA  . SER A 27  ? 0.13801 0.25508 0.19178 -0.03675 0.01585  0.00050  461 SER A CA  
162  C C   . SER A 27  ? 0.14854 0.26610 0.20067 -0.03173 0.01163  -0.00435 461 SER A C   
163  O O   . SER A 27  ? 0.06863 0.18239 0.12432 -0.03100 0.00772  -0.00728 461 SER A O   
164  C CB  . SER A 27  ? 0.13943 0.26522 0.20345 -0.03971 0.01748  -0.00216 461 SER A CB  
165  O OG  . SER A 27  ? 0.14881 0.28612 0.21399 -0.03747 0.01992  -0.00463 461 SER A OG  
166  N N   . HIS A 28  ? 0.10410 0.22597 0.15092 -0.02817 0.01239  -0.00530 462 HIS A N   
167  C CA  . HIS A 28  ? 0.07734 0.19933 0.12366 -0.02385 0.00873  -0.01027 462 HIS A CA  
168  C C   . HIS A 28  ? 0.14683 0.26179 0.18624 -0.02172 0.00657  -0.00901 462 HIS A C   
169  O O   . HIS A 28  ? 0.09856 0.21445 0.13744 -0.01835 0.00423  -0.01311 462 HIS A O   
170  C CB  . HIS A 28  ? 0.12066 0.25358 0.16772 -0.02098 0.01037  -0.01428 462 HIS A CB  
171  C CG  . HIS A 28  ? 0.13908 0.27894 0.19466 -0.02127 0.01065  -0.01804 462 HIS A CG  
172  N ND1 . HIS A 28  ? 0.10389 0.24189 0.16453 -0.01904 0.00689  -0.02259 462 HIS A ND1 
173  C CD2 . HIS A 28  ? 0.09854 0.24760 0.15870 -0.02321 0.01437  -0.01785 462 HIS A CD2 
174  C CE1 . HIS A 28  ? 0.13699 0.28283 0.20467 -0.01916 0.00779  -0.02524 462 HIS A CE1 
175  N NE2 . HIS A 28  ? 0.06250 0.21569 0.13057 -0.02187 0.01232  -0.02273 462 HIS A NE2 
176  N N   . HIS A 29  ? 0.08299 0.19119 0.11780 -0.02352 0.00732  -0.00378 463 HIS A N   
177  C CA  . HIS A 29  ? 0.07043 0.17218 0.09980 -0.02133 0.00487  -0.00288 463 HIS A CA  
178  C C   . HIS A 29  ? 0.09307 0.18971 0.12653 -0.02034 0.00095  -0.00649 463 HIS A C   
179  O O   . HIS A 29  ? 0.10942 0.20303 0.14762 -0.02216 0.00006  -0.00687 463 HIS A O   
180  C CB  . HIS A 29  ? 0.12236 0.21642 0.14722 -0.02335 0.00608  0.00328  463 HIS A CB  
181  C CG  . HIS A 29  ? 0.13950 0.22835 0.15854 -0.02059 0.00385  0.00443  463 HIS A CG  
182  N ND1 . HIS A 29  ? 0.10850 0.19163 0.12947 -0.01967 0.00036  0.00222  463 HIS A ND1 
183  C CD2 . HIS A 29  ? 0.08240 0.17153 0.09386 -0.01823 0.00469  0.00758  463 HIS A CD2 
184  C CE1 . HIS A 29  ? 0.11911 0.19976 0.13494 -0.01721 -0.00086 0.00356  463 HIS A CE1 
185  N NE2 . HIS A 29  ? 0.09744 0.18168 0.10727 -0.01604 0.00140  0.00668  463 HIS A NE2 
186  N N   . PRO A 30  ? 0.08981 0.18575 0.12181 -0.01738 -0.00132 -0.00926 464 PRO A N   
187  C CA  . PRO A 30  ? 0.05961 0.15139 0.09628 -0.01641 -0.00410 -0.01266 464 PRO A CA  
188  C C   . PRO A 30  ? 0.08662 0.16923 0.12340 -0.01780 -0.00543 -0.00991 464 PRO A C   
189  O O   . PRO A 30  ? 0.11445 0.19382 0.15503 -0.01726 -0.00697 -0.01175 464 PRO A O   
190  C CB  . PRO A 30  ? 0.05752 0.15104 0.09302 -0.01357 -0.00562 -0.01602 464 PRO A CB  
191  C CG  . PRO A 30  ? 0.09844 0.19468 0.12710 -0.01284 -0.00456 -0.01324 464 PRO A CG  
192  C CD  . PRO A 30  ? 0.06579 0.16590 0.09253 -0.01460 -0.00134 -0.01002 464 PRO A CD  
193  N N   . GLU A 31  ? 0.05888 0.13687 0.09130 -0.01913 -0.00483 -0.00553 465 GLU A N   
194  C CA  . GLU A 31  ? 0.07442 0.14368 0.10646 -0.02010 -0.00614 -0.00332 465 GLU A CA  
195  C C   . GLU A 31  ? 0.10902 0.17794 0.14453 -0.02272 -0.00572 -0.00293 465 GLU A C   
196  O O   . GLU A 31  ? 0.12282 0.18849 0.15695 -0.02511 -0.00471 0.00012  465 GLU A O   
197  C CB  . GLU A 31  ? 0.09896 0.16322 0.12551 -0.01980 -0.00602 0.00038  465 GLU A CB  
198  C CG  . GLU A 31  ? 0.14773 0.20420 0.17390 -0.01920 -0.00779 0.00103  465 GLU A CG  
199  C CD  . GLU A 31  ? 0.06094 0.11247 0.08877 -0.02116 -0.00825 0.00176  465 GLU A CD  
200  O OE1 . GLU A 31  ? 0.05785 0.10995 0.08922 -0.02082 -0.00932 -0.00069 465 GLU A OE1 
201  O OE2 . GLU A 31  ? 0.06504 0.11218 0.09065 -0.02278 -0.00762 0.00458  465 GLU A OE2 
202  N N   . LEU A 32  ? 0.10999 0.18202 0.15023 -0.02204 -0.00666 -0.00620 466 LEU A N   
203  C CA  . LEU A 32  ? 0.12372 0.19868 0.16847 -0.02394 -0.00656 -0.00710 466 LEU A CA  
204  C C   . LEU A 32  ? 0.18366 0.25226 0.22896 -0.02421 -0.00885 -0.00687 466 LEU A C   
205  O O   . LEU A 32  ? 0.06977 0.13320 0.11320 -0.02183 -0.01055 -0.00710 466 LEU A O   
206  C CB  . LEU A 32  ? 0.07076 0.15260 0.12018 -0.02206 -0.00689 -0.01103 466 LEU A CB  
207  C CG  . LEU A 32  ? 0.05342 0.14379 0.10338 -0.02175 -0.00454 -0.01240 466 LEU A CG  
208  C CD1 . LEU A 32  ? 0.10590 0.20067 0.15994 -0.01868 -0.00557 -0.01694 466 LEU A CD1 
209  C CD2 . LEU A 32  ? 0.05603 0.15213 0.10813 -0.02501 -0.00181 -0.01089 466 LEU A CD2 
210  N N   . PRO A 33  ? 0.12026 0.18965 0.16839 -0.02708 -0.00875 -0.00665 467 PRO A N   
211  C CA  . PRO A 33  ? 0.05736 0.12269 0.10658 -0.02674 -0.01154 -0.00787 467 PRO A CA  
212  C C   . PRO A 33  ? 0.07451 0.14125 0.12515 -0.02291 -0.01385 -0.01058 467 PRO A C   
213  O O   . PRO A 33  ? 0.14841 0.20972 0.19649 -0.02067 -0.01597 -0.01057 467 PRO A O   
214  C CB  . PRO A 33  ? 0.05971 0.12915 0.11438 -0.03068 -0.01093 -0.00874 467 PRO A CB  
215  C CG  . PRO A 33  ? 0.07408 0.14490 0.12788 -0.03369 -0.00711 -0.00564 467 PRO A CG  
216  C CD  . PRO A 33  ? 0.09347 0.16727 0.14395 -0.03086 -0.00589 -0.00525 467 PRO A CD  
217  N N   . GLN A 34  ? 0.05273 0.12640 0.10700 -0.02169 -0.01325 -0.01271 468 GLN A N   
218  C CA  . GLN A 34  ? 0.05155 0.12621 0.10753 -0.01768 -0.01522 -0.01504 468 GLN A CA  
219  C C   . GLN A 34  ? 0.05112 0.11925 0.10329 -0.01461 -0.01534 -0.01395 468 GLN A C   
220  O O   . GLN A 34  ? 0.05160 0.11840 0.10449 -0.01106 -0.01658 -0.01497 468 GLN A O   
221  C CB  . GLN A 34  ? 0.05023 0.13397 0.11150 -0.01702 -0.01432 -0.01786 468 GLN A CB  
222  C CG  . GLN A 34  ? 0.05076 0.14223 0.11793 -0.01901 -0.01478 -0.01990 468 GLN A CG  
223  C CD  . GLN A 34  ? 0.06316 0.15570 0.13108 -0.02429 -0.01256 -0.01802 468 GLN A CD  
224  O OE1 . GLN A 34  ? 0.12366 0.21627 0.18911 -0.02609 -0.00957 -0.01580 468 GLN A OE1 
225  N NE2 . GLN A 34  ? 0.07609 0.16933 0.14745 -0.02661 -0.01406 -0.01899 468 GLN A NE2 
226  N N   . ARG A 35  ? 0.09715 0.16124 0.14570 -0.01575 -0.01397 -0.01184 469 ARG A N   
227  C CA  . ARG A 35  ? 0.10674 0.16517 0.15308 -0.01340 -0.01388 -0.01106 469 ARG A CA  
228  C C   . ARG A 35  ? 0.05274 0.10492 0.09649 -0.01127 -0.01536 -0.00972 469 ARG A C   
229  O O   . ARG A 35  ? 0.06208 0.11137 0.10606 -0.00823 -0.01549 -0.00973 469 ARG A O   
230  C CB  . ARG A 35  ? 0.11865 0.17519 0.16208 -0.01490 -0.01255 -0.00939 469 ARG A CB  
231  C CG  . ARG A 35  ? 0.12464 0.18757 0.16925 -0.01589 -0.01113 -0.01073 469 ARG A CG  
232  C CD  . ARG A 35  ? 0.11877 0.18038 0.15963 -0.01667 -0.01032 -0.00891 469 ARG A CD  
233  N NE  . ARG A 35  ? 0.07296 0.13019 0.11352 -0.01504 -0.01077 -0.00904 469 ARG A NE  
234  C CZ  . ARG A 35  ? 0.05065 0.10210 0.08846 -0.01491 -0.01107 -0.00668 469 ARG A CZ  
235  N NH1 . ARG A 35  ? 0.08026 0.12877 0.11487 -0.01616 -0.01129 -0.00422 469 ARG A NH1 
236  N NH2 . ARG A 35  ? 0.05008 0.09865 0.08897 -0.01355 -0.01097 -0.00706 469 ARG A NH2 
237  N N   . ILE A 36  ? 0.08275 0.13265 0.12390 -0.01259 -0.01634 -0.00859 470 ILE A N   
238  C CA  . ILE A 36  ? 0.09213 0.13661 0.12971 -0.01005 -0.01779 -0.00760 470 ILE A CA  
239  C C   . ILE A 36  ? 0.13497 0.18222 0.17397 -0.00747 -0.02008 -0.00945 470 ILE A C   
240  O O   . ILE A 36  ? 0.14237 0.18590 0.17828 -0.00362 -0.02091 -0.00853 470 ILE A O   
241  C CB  . ILE A 36  ? 0.06876 0.10946 0.10288 -0.01188 -0.01829 -0.00646 470 ILE A CB  
242  C CG1 . ILE A 36  ? 0.05975 0.10437 0.09680 -0.01516 -0.01927 -0.00810 470 ILE A CG1 
243  C CG2 . ILE A 36  ? 0.05805 0.09578 0.09019 -0.01317 -0.01629 -0.00439 470 ILE A CG2 
244  C CD1 . ILE A 36  ? 0.08227 0.12212 0.11662 -0.01664 -0.02023 -0.00772 470 ILE A CD1 
245  N N   . SER A 37  ? 0.07904 0.13322 0.12263 -0.00918 -0.02104 -0.01194 471 SER A N   
246  C CA  . SER A 37  ? 0.12174 0.17983 0.16728 -0.00624 -0.02374 -0.01424 471 SER A CA  
247  C C   . SER A 37  ? 0.11180 0.17049 0.15859 -0.00218 -0.02340 -0.01439 471 SER A C   
248  O O   . SER A 37  ? 0.11314 0.17141 0.15858 0.00231  -0.02547 -0.01470 471 SER A O   
249  C CB  . SER A 37  ? 0.05891 0.12526 0.11050 -0.00950 -0.02468 -0.01725 471 SER A CB  
250  O OG  . SER A 37  ? 0.09439 0.16563 0.15002 -0.01228 -0.02203 -0.01751 471 SER A OG  
251  N N   . ARG A 38  ? 0.11588 0.17530 0.16503 -0.00325 -0.02095 -0.01432 472 ARG A N   
252  C CA  . ARG A 38  ? 0.11203 0.17030 0.16274 0.00053  -0.02041 -0.01466 472 ARG A CA  
253  C C   . ARG A 38  ? 0.11250 0.16159 0.15869 0.00342  -0.01953 -0.01146 472 ARG A C   
254  O O   . ARG A 38  ? 0.12515 0.17134 0.17083 0.00787  -0.01989 -0.01071 472 ARG A O   
255  C CB  . ARG A 38  ? 0.05566 0.11735 0.11030 -0.00140 -0.01823 -0.01635 472 ARG A CB  
256  C CG  . ARG A 38  ? 0.05384 0.12533 0.11364 -0.00238 -0.01853 -0.01963 472 ARG A CG  
257  C CD  . ARG A 38  ? 0.05623 0.13033 0.11925 0.00230  -0.02010 -0.02173 472 ARG A CD  
258  N NE  . ARG A 38  ? 0.11300 0.18248 0.17686 0.00526  -0.01891 -0.02202 472 ARG A NE  
259  C CZ  . ARG A 38  ? 0.12799 0.20128 0.19571 0.00498  -0.01748 -0.02492 472 ARG A CZ  
260  N NH1 . ARG A 38  ? 0.05383 0.13596 0.12402 0.00208  -0.01662 -0.02715 472 ARG A NH1 
261  N NH2 . ARG A 38  ? 0.12009 0.18809 0.18927 0.00778  -0.01668 -0.02565 472 ARG A NH2 
262  N N   . ILE A 39  ? 0.06139 0.10580 0.10437 0.00117  -0.01806 -0.00927 473 ILE A N   
263  C CA  . ILE A 39  ? 0.06505 0.10150 0.10423 0.00360  -0.01661 -0.00604 473 ILE A CA  
264  C C   . ILE A 39  ? 0.08705 0.12121 0.12104 0.00759  -0.01855 -0.00453 473 ILE A C   
265  O O   . ILE A 39  ? 0.07562 0.10503 0.10720 0.01189  -0.01782 -0.00218 473 ILE A O   
266  C CB  . ILE A 39  ? 0.10519 0.13866 0.14263 0.00052  -0.01481 -0.00452 473 ILE A CB  
267  C CG1 . ILE A 39  ? 0.06916 0.10469 0.11131 -0.00207 -0.01304 -0.00611 473 ILE A CG1 
268  C CG2 . ILE A 39  ? 0.06725 0.09355 0.10050 0.00296  -0.01318 -0.00105 473 ILE A CG2 
269  C CD1 . ILE A 39  ? 0.11920 0.15428 0.16014 -0.00498 -0.01205 -0.00539 473 ILE A CD1 
270  N N   . PHE A 40  ? 0.06981 0.10733 0.10201 0.00643  -0.02105 -0.00596 474 PHE A N   
271  C CA  . PHE A 40  ? 0.07527 0.11185 0.10227 0.01043  -0.02362 -0.00560 474 PHE A CA  
272  C C   . PHE A 40  ? 0.10045 0.13957 0.12825 0.01541  -0.02551 -0.00636 474 PHE A C   
273  O O   . PHE A 40  ? 0.14013 0.17507 0.16249 0.02079  -0.02576 -0.00382 474 PHE A O   
274  C CB  . PHE A 40  ? 0.07407 0.11472 0.10123 0.00757  -0.02631 -0.00843 474 PHE A CB  
275  C CG  . PHE A 40  ? 0.14265 0.18270 0.16420 0.01151  -0.02940 -0.00910 474 PHE A CG  
276  C CD1 . PHE A 40  ? 0.08416 0.11795 0.09855 0.01354  -0.02845 -0.00655 474 PHE A CD1 
277  C CD2 . PHE A 40  ? 0.08208 0.12878 0.10572 0.01339  -0.03339 -0.01277 474 PHE A CD2 
278  C CE1 . PHE A 40  ? 0.13286 0.16666 0.14123 0.01772  -0.03145 -0.00763 474 PHE A CE1 
279  C CE2 . PHE A 40  ? 0.13897 0.18604 0.15721 0.01749  -0.03684 -0.01419 474 PHE A CE2 
280  C CZ  . PHE A 40  ? 0.12512 0.16557 0.13521 0.01982  -0.03589 -0.01162 474 PHE A CZ  
281  N N   . SER A 41  ? 0.08156 0.12772 0.11584 0.01415  -0.02668 -0.00963 475 SER A N   
282  C CA  A SER A 41  ? 0.09742 0.14694 0.13313 0.01932  -0.02883 -0.01083 475 SER A CA  
283  C CA  B SER A 41  ? 0.09779 0.14735 0.13358 0.01929  -0.02881 -0.01085 475 SER A CA  
284  C C   . SER A 41  ? 0.09369 0.13565 0.12723 0.02377  -0.02641 -0.00722 475 SER A C   
285  O O   . SER A 41  ? 0.14484 0.18488 0.17456 0.03004  -0.02786 -0.00563 475 SER A O   
286  C CB  A SER A 41  ? 0.08148 0.14021 0.12545 0.01686  -0.02961 -0.01500 475 SER A CB  
287  C CB  B SER A 41  ? 0.08591 0.14452 0.12997 0.01680  -0.02949 -0.01496 475 SER A CB  
288  O OG  A SER A 41  ? 0.10798 0.17062 0.15384 0.02233  -0.03191 -0.01652 475 SER A OG  
289  O OG  B SER A 41  ? 0.11011 0.17599 0.15714 0.01302  -0.03158 -0.01816 475 SER A OG  
290  N N   . ARG A 42  ? 0.12092 0.15847 0.15705 0.02078  -0.02272 -0.00593 476 ARG A N   
291  C CA  . ARG A 42  ? 0.13747 0.16709 0.17315 0.02414  -0.01995 -0.00277 476 ARG A CA  
292  C C   . ARG A 42  ? 0.13120 0.15280 0.15910 0.02748  -0.01847 0.00233  476 ARG A C   
293  O O   . ARG A 42  ? 0.14303 0.15861 0.16837 0.03265  -0.01721 0.00570  476 ARG A O   
294  C CB  . ARG A 42  ? 0.11125 0.13889 0.15247 0.01964  -0.01667 -0.00361 476 ARG A CB  
295  C CG  . ARG A 42  ? 0.12080 0.14076 0.16448 0.02220  -0.01378 -0.00171 476 ARG A CG  
296  C CD  . ARG A 42  ? 0.16489 0.18686 0.21174 0.02664  -0.01542 -0.00373 476 ARG A CD  
297  N NE  . ARG A 42  ? 0.19385 0.20696 0.24341 0.02908  -0.01247 -0.00187 476 ARG A NE  
298  C CZ  . ARG A 42  ? 0.16061 0.17023 0.21010 0.03509  -0.01299 -0.00079 476 ARG A CZ  
299  N NH1 . ARG A 42  ? 0.16585 0.18119 0.21269 0.03974  -0.01673 -0.00163 476 ARG A NH1 
300  N NH2 . ARG A 42  ? 0.15628 0.15635 0.20888 0.03661  -0.00973 0.00108  476 ARG A NH2 
301  N N   . HIS A 43  ? 0.12516 0.14639 0.14899 0.02494  -0.01834 0.00315  477 HIS A N   
302  C CA  . HIS A 43  ? 0.15966 0.17489 0.17522 0.02870  -0.01717 0.00755  477 HIS A CA  
303  C C   . HIS A 43  ? 0.13626 0.15343 0.14590 0.03548  -0.02074 0.00783  477 HIS A C   
304  O O   . HIS A 43  ? 0.14100 0.15226 0.14386 0.04108  -0.01926 0.01242  477 HIS A O   
305  C CB  . HIS A 43  ? 0.10727 0.12293 0.11988 0.02507  -0.01698 0.00728  477 HIS A CB  
306  C CG  . HIS A 43  ? 0.09297 0.10437 0.10831 0.02094  -0.01270 0.00911  477 HIS A CG  
307  N ND1 . HIS A 43  ? 0.11244 0.12652 0.13511 0.01578  -0.01192 0.00647  477 HIS A ND1 
308  C CD2 . HIS A 43  ? 0.10525 0.11084 0.11721 0.02147  -0.00904 0.01303  477 HIS A CD2 
309  C CE1 . HIS A 43  ? 0.14548 0.15583 0.16949 0.01338  -0.00846 0.00829  477 HIS A CE1 
310  N NE2 . HIS A 43  ? 0.09097 0.09623 0.10912 0.01650  -0.00647 0.01229  477 HIS A NE2 
311  N N   . GLU A 44  ? 0.14487 0.17072 0.15709 0.03525  -0.02536 0.00299  478 GLU A N   
312  C CA  . GLU A 44  ? 0.12429 0.15385 0.13226 0.04200  -0.02953 0.00214  478 GLU A CA  
313  C C   . GLU A 44  ? 0.12479 0.15142 0.13367 0.04754  -0.02878 0.00440  478 GLU A C   
314  O O   . GLU A 44  ? 0.17783 0.20030 0.17928 0.05483  -0.02905 0.00820  478 GLU A O   
315  C CB  . GLU A 44  ? 0.20015 0.24071 0.21325 0.03957  -0.03440 -0.00429 478 GLU A CB  
316  C CG  . GLU A 44  ? 0.17398 0.21710 0.18587 0.03517  -0.03596 -0.00690 478 GLU A CG  
317  C CD  . GLU A 44  ? 0.34115 0.39474 0.36054 0.03162  -0.03985 -0.01317 478 GLU A CD  
318  O OE1 . GLU A 44  ? 0.19070 0.24796 0.21817 0.02675  -0.03841 -0.01492 478 GLU A OE1 
319  O OE2 . GLU A 44  ? 0.40385 0.46239 0.42131 0.03378  -0.04423 -0.01655 478 GLU A OE2 
320  N N   . GLU A 45  ? 0.11128 0.13978 0.12882 0.04457  -0.02774 0.00215  479 GLU A N   
321  C CA  . GLU A 45  ? 0.12375 0.14957 0.14338 0.04976  -0.02729 0.00336  479 GLU A CA  
322  C C   . GLU A 45  ? 0.26351 0.27667 0.27847 0.05309  -0.02260 0.01011  479 GLU A C   
323  O O   . GLU A 45  ? 0.31356 0.32222 0.32634 0.05983  -0.02247 0.01295  479 GLU A O   
324  C CB  . GLU A 45  ? 0.14330 0.17341 0.17318 0.04529  -0.02656 -0.00088 479 GLU A CB  
325  C CG  . GLU A 45  ? 0.14043 0.18343 0.17569 0.04269  -0.03053 -0.00701 479 GLU A CG  
326  C CD  . GLU A 45  ? 0.10173 0.14917 0.14544 0.03632  -0.02872 -0.01067 479 GLU A CD  
327  O OE1 . GLU A 45  ? 0.09405 0.13496 0.13952 0.03399  -0.02499 -0.00917 479 GLU A OE1 
328  O OE2 . GLU A 45  ? 0.15435 0.21226 0.20307 0.03367  -0.03097 -0.01519 479 GLU A OE2 
329  N N   . LEU A 46  ? 0.28000 0.28730 0.29382 0.04859  -0.01852 0.01286  480 LEU A N   
330  C CA  . LEU A 46  ? 0.16049 0.15614 0.17120 0.05063  -0.01324 0.01932  480 LEU A CA  
331  C C   . LEU A 46  ? 0.20959 0.20151 0.20887 0.05574  -0.01265 0.02454  480 LEU A C   
332  O O   . LEU A 46  ? 0.31648 0.29892 0.31238 0.05732  -0.00754 0.03069  480 LEU A O   
333  C CB  . LEU A 46  ? 0.13366 0.12597 0.15064 0.04306  -0.00889 0.01908  480 LEU A CB  
334  C CG  . LEU A 46  ? 0.17252 0.16636 0.20001 0.03940  -0.00852 0.01474  480 LEU A CG  
335  C CD1 . LEU A 46  ? 0.11318 0.10622 0.14677 0.03205  -0.00542 0.01320  480 LEU A CD1 
336  C CD2 . LEU A 46  ? 0.16299 0.14877 0.19232 0.04438  -0.00650 0.01743  480 LEU A CD2 
337  N N   . ARG A 47  ? 0.22323 0.22272 0.21681 0.05841  -0.01765 0.02196  481 ARG A N   
338  C CA  . ARG A 47  ? 0.27793 0.27564 0.25977 0.06375  -0.01796 0.02566  481 ARG A CA  
339  C C   . ARG A 47  ? 0.20140 0.19398 0.18080 0.05963  -0.01309 0.02886  481 ARG A C   
340  O O   . ARG A 47  ? 0.20779 0.19491 0.17809 0.06419  -0.01018 0.03446  481 ARG A O   
341  C CB  . ARG A 47  ? 0.16586 0.15725 0.13988 0.07328  -0.01696 0.03168  481 ARG A CB  
342  N N   . LEU A 48  ? 0.20189 0.19663 0.18922 0.05139  -0.01202 0.02546  482 LEU A N   
343  C CA  . LEU A 48  ? 0.23189 0.22355 0.21792 0.04741  -0.00812 0.02745  482 LEU A CA  
344  C C   . LEU A 48  ? 0.21948 0.21693 0.20046 0.04668  -0.01168 0.02410  482 LEU A C   
345  O O   . LEU A 48  ? 0.19534 0.19006 0.17078 0.04703  -0.00905 0.02669  482 LEU A O   
346  C CB  . LEU A 48  ? 0.16168 0.15277 0.15847 0.03961  -0.00534 0.02546  482 LEU A CB  
347  C CG  . LEU A 48  ? 0.15448 0.13905 0.15780 0.03924  -0.00131 0.02796  482 LEU A CG  
348  C CD1 . LEU A 48  ? 0.12413 0.11083 0.13817 0.03176  -0.00023 0.02392  482 LEU A CD1 
349  C CD2 . LEU A 48  ? 0.21013 0.18535 0.20914 0.04211  0.00474  0.03525  482 LEU A CD2 
350  N N   . LEU A 49  ? 0.25033 0.25574 0.23370 0.04563  -0.01741 0.01817  483 LEU A N   
351  C CA  . LEU A 49  ? 0.19941 0.20972 0.17915 0.04462  -0.02100 0.01431  483 LEU A CA  
352  C C   . LEU A 49  ? 0.18517 0.19480 0.15313 0.05228  -0.02253 0.01624  483 LEU A C   
353  O O   . LEU A 49  ? 0.26780 0.27724 0.23027 0.05235  -0.02255 0.01568  483 LEU A O   
354  C CB  . LEU A 49  ? 0.24602 0.26491 0.23223 0.04160  -0.02634 0.00765  483 LEU A CB  
355  C CG  . LEU A 49  ? 0.14742 0.17117 0.13143 0.04023  -0.03047 0.00285  483 LEU A CG  
356  C CD1 . LEU A 49  ? 0.13488 0.15574 0.12054 0.03428  -0.02778 0.00286  483 LEU A CD1 
357  C CD2 . LEU A 49  ? 0.17273 0.20528 0.16373 0.03808  -0.03549 -0.00332 483 LEU A CD2 
358  N N   . SER A 50  ? 0.16873 0.17811 0.13216 0.05937  -0.02392 0.01841  484 SER A N   
359  C CA  . SER A 50  ? 0.17029 0.17950 0.12119 0.06780  -0.02553 0.02049  484 SER A CA  
360  C C   . SER A 50  ? 0.20797 0.20891 0.15104 0.07022  -0.01900 0.02779  484 SER A C   
361  O O   . SER A 50  ? 0.27715 0.27842 0.20918 0.07588  -0.01963 0.02898  484 SER A O   
362  C CB  . SER A 50  ? 0.25824 0.26932 0.20602 0.07552  -0.02869 0.02143  484 SER A CB  
363  O OG  . SER A 50  ? 0.21781 0.22230 0.16991 0.07567  -0.02433 0.02639  484 SER A OG  
364  N N   . ARG A 51  ? 0.22249 0.21664 0.17137 0.06608  -0.01268 0.03231  485 ARG A N   
365  C CA  . ARG A 51  ? 0.20784 0.19472 0.15156 0.06725  -0.00568 0.03915  485 ARG A CA  
366  C C   . ARG A 51  ? 0.19206 0.18045 0.13646 0.06229  -0.00423 0.03701  485 ARG A C   
367  O O   . ARG A 51  ? 0.25281 0.23699 0.19209 0.06381  0.00119  0.04194  485 ARG A O   
368  C CB  . ARG A 51  ? 0.24446 0.22374 0.19587 0.06435  0.00048  0.04412  485 ARG A CB  
369  C CG  . ARG A 51  ? 0.22535 0.20094 0.17573 0.06998  0.00011  0.04733  485 ARG A CG  
370  C CD  . ARG A 51  ? 0.21726 0.18479 0.17691 0.06621  0.00610  0.05113  485 ARG A CD  
371  N NE  . ARG A 51  ? 0.28519 0.24598 0.24381 0.06456  0.01381  0.05716  485 ARG A NE  
372  C CZ  . ARG A 51  ? 0.24511 0.19882 0.21256 0.06035  0.01993  0.06036  485 ARG A CZ  
373  N NH1 . ARG A 51  ? 0.22748 0.17917 0.20474 0.05769  0.01920  0.05807  485 ARG A NH1 
374  N NH2 . ARG A 51  ? 0.34770 0.29667 0.31469 0.05873  0.02698  0.06552  485 ARG A NH2 
375  N N   . CYS A 52  ? 0.22653 0.22069 0.17712 0.05672  -0.00862 0.03009  486 CYS A N   
376  C CA  . CYS A 52  ? 0.16105 0.15617 0.11316 0.05202  -0.00754 0.02785  486 CYS A CA  
377  C C   . CYS A 52  ? 0.21804 0.21766 0.16242 0.05514  -0.01251 0.02329  486 CYS A C   
378  O O   . CYS A 52  ? 0.23610 0.24001 0.17701 0.05903  -0.01803 0.01991  486 CYS A O   
379  C CB  . CYS A 52  ? 0.20450 0.20191 0.16867 0.04362  -0.00848 0.02372  486 CYS A CB  
380  S SG  . CYS A 52  ? 0.12935 0.12241 0.10394 0.03915  -0.00318 0.02715  486 CYS A SG  
381  N N   . HIS A 53  ? 0.19858 0.19751 0.14083 0.05357  -0.01064 0.02271  487 HIS A N   
382  C CA  . HIS A 53  ? 0.28747 0.29012 0.22481 0.05488  -0.01539 0.01702  487 HIS A CA  
383  C C   . HIS A 53  ? 0.24836 0.25367 0.19557 0.04735  -0.01873 0.01116  487 HIS A C   
384  O O   . HIS A 53  ? 0.14173 0.14508 0.09591 0.04172  -0.01553 0.01220  487 HIS A O   
385  C CB  . HIS A 53  ? 0.16357 0.16395 0.09341 0.05758  -0.01160 0.01915  487 HIS A CB  
386  C CG  . HIS A 53  ? 0.20005 0.20326 0.12654 0.05795  -0.01612 0.01260  487 HIS A CG  
387  N ND1 . HIS A 53  ? 0.28120 0.28736 0.19767 0.06466  -0.02044 0.00931  487 HIS A ND1 
388  C CD2 . HIS A 53  ? 0.23467 0.23789 0.16663 0.05267  -0.01716 0.00846  487 HIS A CD2 
389  C CE1 . HIS A 53  ? 0.25635 0.26395 0.17297 0.06308  -0.02391 0.00297  487 HIS A CE1 
390  N NE2 . HIS A 53  ? 0.28608 0.29143 0.21190 0.05589  -0.02183 0.00272  487 HIS A NE2 
391  N N   . ARG A 54  ? 0.21025 0.22026 0.15821 0.04737  -0.02506 0.00507  488 ARG A N   
392  C CA  . ARG A 54  ? 0.22149 0.23386 0.17896 0.04026  -0.02790 0.00002  488 ARG A CA  
393  C C   . ARG A 54  ? 0.24235 0.25286 0.19867 0.03813  -0.02807 -0.00279 488 ARG A C   
394  O O   . ARG A 54  ? 0.22813 0.23941 0.17753 0.04215  -0.03090 -0.00611 488 ARG A O   
395  C CB  . ARG A 54  ? 0.15765 0.17610 0.11773 0.04074  -0.03412 -0.00549 488 ARG A CB  
396  C CG  . ARG A 54  ? 0.12144 0.14259 0.09233 0.03314  -0.03611 -0.00970 488 ARG A CG  
397  C CD  . ARG A 54  ? 0.12477 0.14554 0.10339 0.02893  -0.03277 -0.00634 488 ARG A CD  
398  N NE  . ARG A 54  ? 0.12006 0.14418 0.10805 0.02229  -0.03442 -0.01002 488 ARG A NE  
399  C CZ  . ARG A 54  ? 0.10396 0.13427 0.09762 0.02121  -0.03770 -0.01348 488 ARG A CZ  
400  N NH1 . ARG A 54  ? 0.11808 0.15212 0.10929 0.02659  -0.04021 -0.01401 488 ARG A NH1 
401  N NH2 . ARG A 54  ? 0.17647 0.20955 0.17845 0.01486  -0.03828 -0.01628 488 ARG A NH2 
402  N N   . ILE A 55  ? 0.24935 0.25753 0.21221 0.03232  -0.02530 -0.00178 489 ILE A N   
403  C CA  . ILE A 55  ? 0.22916 0.23483 0.19174 0.03029  -0.02511 -0.00390 489 ILE A CA  
404  C C   . ILE A 55  ? 0.20982 0.21686 0.17934 0.02489  -0.02904 -0.00902 489 ILE A C   
405  O O   . ILE A 55  ? 0.18369 0.19245 0.16079 0.02025  -0.02877 -0.00849 489 ILE A O   
406  C CB  . ILE A 55  ? 0.26423 0.26683 0.22956 0.02790  -0.01965 0.00054  489 ILE A CB  
407  C CG1 . ILE A 55  ? 0.19101 0.19209 0.15017 0.03287  -0.01503 0.00563  489 ILE A CG1 
408  C CG2 . ILE A 55  ? 0.21656 0.21678 0.18263 0.02577  -0.01992 -0.00186 489 ILE A CG2 
409  C CD1 . ILE A 55  ? 0.11987 0.11913 0.08328 0.03040  -0.00957 0.00954  489 ILE A CD1 
410  N N   . PRO A 56  ? 0.22025 0.22642 0.18772 0.02527  -0.03236 -0.01400 490 PRO A N   
411  C CA  . PRO A 56  ? 0.14732 0.15408 0.12224 0.01972  -0.03558 -0.01859 490 PRO A CA  
412  C C   . PRO A 56  ? 0.19932 0.20229 0.17968 0.01433  -0.03263 -0.01634 490 PRO A C   
413  O O   . PRO A 56  ? 0.35271 0.35210 0.33024 0.01547  -0.02944 -0.01344 490 PRO A O   
414  C CB  . PRO A 56  ? 0.17448 0.18028 0.14514 0.02235  -0.03963 -0.02465 490 PRO A CB  
415  C CG  . PRO A 56  ? 0.24367 0.24667 0.20490 0.02815  -0.03708 -0.02227 490 PRO A CG  
416  C CD  . PRO A 56  ? 0.28641 0.29104 0.24475 0.03097  -0.03325 -0.01593 490 PRO A CD  
417  N N   . ALA A 57  ? 0.19168 0.19610 0.17989 0.00876  -0.03364 -0.01766 491 ALA A N   
418  C CA  . ALA A 57  ? 0.13276 0.13386 0.12567 0.00387  -0.03136 -0.01572 491 ALA A CA  
419  C C   . ALA A 57  ? 0.14364 0.13964 0.13691 0.00229  -0.03323 -0.01934 491 ALA A C   
420  O O   . ALA A 57  ? 0.19339 0.18969 0.18592 0.00337  -0.03689 -0.02452 491 ALA A O   
421  C CB  . ALA A 57  ? 0.16753 0.17262 0.16807 -0.00107 -0.03095 -0.01496 491 ALA A CB  
422  N N   . ARG A 58  ? 0.13877 0.12999 0.13334 -0.00001 -0.03086 -0.01683 492 ARG A N   
423  C CA  . ARG A 58  ? 0.21702 0.20192 0.21275 -0.00188 -0.03213 -0.01957 492 ARG A CA  
424  C C   . ARG A 58  ? 0.14053 0.12188 0.13956 -0.00553 -0.02927 -0.01549 492 ARG A C   
425  O O   . ARG A 58  ? 0.18666 0.17070 0.18584 -0.00558 -0.02656 -0.01113 492 ARG A O   
426  C CB  . ARG A 58  ? 0.15573 0.13633 0.14462 0.00323  -0.03290 -0.02171 492 ARG A CB  
427  C CG  . ARG A 58  ? 0.19427 0.17285 0.17922 0.00619  -0.02935 -0.01728 492 ARG A CG  
428  C CD  . ARG A 58  ? 0.12916 0.10336 0.10813 0.01100  -0.03010 -0.02010 492 ARG A CD  
429  N NE  . ARG A 58  ? 0.13686 0.11073 0.11255 0.01434  -0.02662 -0.01632 492 ARG A NE  
430  C CZ  . ARG A 58  ? 0.14938 0.11928 0.12664 0.01371  -0.02498 -0.01422 492 ARG A CZ  
431  N NH1 . ARG A 58  ? 0.12949 0.09430 0.11075 0.00990  -0.02599 -0.01456 492 ARG A NH1 
432  N NH2 . ARG A 58  ? 0.22553 0.19676 0.20043 0.01719  -0.02209 -0.01156 492 ARG A NH2 
433  N N   . LEU A 59  ? 0.12486 0.10000 0.12657 -0.00840 -0.02996 -0.01711 493 LEU A N   
434  C CA  . LEU A 59  ? 0.12610 0.09650 0.12941 -0.01084 -0.02730 -0.01288 493 LEU A CA  
435  C C   . LEU A 59  ? 0.21834 0.18423 0.21613 -0.00630 -0.02609 -0.01100 493 LEU A C   
436  O O   . LEU A 59  ? 0.23589 0.19782 0.23015 -0.00295 -0.02767 -0.01433 493 LEU A O   
437  C CB  . LEU A 59  ? 0.14779 0.11189 0.15607 -0.01544 -0.02794 -0.01469 493 LEU A CB  
438  C CG  . LEU A 59  ? 0.19845 0.16649 0.21433 -0.02104 -0.02865 -0.01676 493 LEU A CG  
439  C CD1 . LEU A 59  ? 0.13566 0.09546 0.15651 -0.02523 -0.02890 -0.01882 493 LEU A CD1 
440  C CD2 . LEU A 59  ? 0.20159 0.17535 0.22006 -0.02379 -0.02566 -0.01186 493 LEU A CD2 
441  N N   . ALA A 60  ? 0.17990 0.14715 0.17716 -0.00589 -0.02344 -0.00616 494 ALA A N   
442  C CA  . ALA A 60  ? 0.18436 0.14742 0.17792 -0.00206 -0.02235 -0.00439 494 ALA A CA  
443  C C   . ALA A 60  ? 0.24313 0.19647 0.23708 -0.00303 -0.02291 -0.00489 494 ALA A C   
444  O O   . ALA A 60  ? 0.20052 0.15084 0.19835 -0.00761 -0.02278 -0.00431 494 ALA A O   
445  C CB  . ALA A 60  ? 0.11448 0.08196 0.10840 -0.00160 -0.01993 0.00026  494 ALA A CB  
446  N N   . THR A 61  ? 0.28453 0.23272 0.27477 0.00136  -0.02325 -0.00598 495 THR A N   
447  C CA  . THR A 61  ? 0.23476 0.17243 0.22503 0.00135  -0.02359 -0.00616 495 THR A CA  
448  C C   . THR A 61  ? 0.22914 0.16495 0.21841 0.00263  -0.02141 -0.00046 495 THR A C   
449  O O   . THR A 61  ? 0.26105 0.20396 0.24909 0.00486  -0.02017 0.00220  495 THR A O   
450  C CB  . THR A 61  ? 0.21606 0.14885 0.20264 0.00616  -0.02526 -0.01074 495 THR A CB  
451  O OG1 . THR A 61  ? 0.16189 0.09762 0.14468 0.01158  -0.02383 -0.00870 495 THR A OG1 
452  C CG2 . THR A 61  ? 0.15457 0.09172 0.14029 0.00658  -0.02756 -0.01629 495 THR A CG2 
453  N N   . GLU A 62  ? 0.21875 0.14478 0.20877 0.00135  -0.02101 0.00128  496 GLU A N   
454  C CA  . GLU A 62  ? 0.32113 0.24456 0.30906 0.00356  -0.01925 0.00691  496 GLU A CA  
455  C C   . GLU A 62  ? 0.23698 0.16208 0.22108 0.01037  -0.01955 0.00670  496 GLU A C   
456  O O   . GLU A 62  ? 0.26384 0.19377 0.24663 0.01295  -0.01853 0.01043  496 GLU A O   
457  C CB  . GLU A 62  ? 0.27076 0.18143 0.25951 0.00176  -0.01855 0.00895  496 GLU A CB  
458  C CG  . GLU A 62  ? 0.26173 0.17098 0.25532 -0.00534 -0.01734 0.01005  496 GLU A CG  
459  C CD  . GLU A 62  ? 0.35966 0.25495 0.35483 -0.00737 -0.01613 0.01197  496 GLU A CD  
460  O OE1 . GLU A 62  ? 0.43724 0.32348 0.42938 -0.00281 -0.01669 0.01196  496 GLU A OE1 
461  O OE2 . GLU A 62  ? 0.25283 0.14607 0.25268 -0.01346 -0.01435 0.01355  496 GLU A OE2 
462  N N   . GLU A 63  ? 0.20271 0.12461 0.18527 0.01354  -0.02100 0.00194  497 GLU A N   
463  C CA  . GLU A 63  ? 0.25072 0.17517 0.23025 0.02008  -0.02090 0.00128  497 GLU A CA  
464  C C   . GLU A 63  ? 0.24139 0.17876 0.22143 0.02091  -0.01979 0.00198  497 GLU A C   
465  O O   . GLU A 63  ? 0.25719 0.19933 0.23670 0.02503  -0.01889 0.00355  497 GLU A O   
466  C CB  . GLU A 63  ? 0.16941 0.08841 0.14687 0.02326  -0.02247 -0.00449 497 GLU A CB  
467  C CG  . GLU A 63  ? 0.27528 0.18027 0.25307 0.02276  -0.02368 -0.00611 497 GLU A CG  
468  C CD  . GLU A 63  ? 0.32636 0.22728 0.30811 0.01581  -0.02452 -0.00778 497 GLU A CD  
469  O OE1 . GLU A 63  ? 0.26851 0.17753 0.25181 0.01263  -0.02504 -0.00965 497 GLU A OE1 
470  O OE2 . GLU A 63  ? 0.40612 0.29576 0.38995 0.01357  -0.02452 -0.00715 497 GLU A OE2 
471  N N   . GLU A 64  ? 0.19178 0.13492 0.17349 0.01711  -0.01981 0.00069  498 GLU A N   
472  C CA  . GLU A 64  ? 0.13908 0.09321 0.12201 0.01729  -0.01839 0.00179  498 GLU A CA  
473  C C   . GLU A 64  ? 0.27955 0.23833 0.26493 0.01522  -0.01740 0.00600  498 GLU A C   
474  O O   . GLU A 64  ? 0.21383 0.18041 0.20062 0.01701  -0.01628 0.00715  498 GLU A O   
475  C CB  . GLU A 64  ? 0.15214 0.11011 0.13559 0.01460  -0.01882 -0.00068 498 GLU A CB  
476  C CG  . GLU A 64  ? 0.13197 0.08972 0.11189 0.01835  -0.01929 -0.00460 498 GLU A CG  
477  C CD  . GLU A 64  ? 0.15532 0.11434 0.13471 0.01614  -0.02082 -0.00759 498 GLU A CD  
478  O OE1 . GLU A 64  ? 0.13250 0.09160 0.11512 0.01137  -0.02174 -0.00716 498 GLU A OE1 
479  O OE2 . GLU A 64  ? 0.30736 0.26789 0.28294 0.01958  -0.02109 -0.01043 498 GLU A OE2 
480  N N   . LEU A 65  ? 0.29132 0.24583 0.27750 0.01148  -0.01766 0.00809  499 LEU A N   
481  C CA  . LEU A 65  ? 0.19859 0.15743 0.18581 0.01026  -0.01673 0.01207  499 LEU A CA  
482  C C   . LEU A 65  ? 0.27528 0.23366 0.26048 0.01524  -0.01668 0.01443  499 LEU A C   
483  O O   . LEU A 65  ? 0.19938 0.16545 0.18553 0.01626  -0.01632 0.01622  499 LEU A O   
484  C CB  . LEU A 65  ? 0.24091 0.19473 0.22879 0.00565  -0.01637 0.01430  499 LEU A CB  
485  C CG  . LEU A 65  ? 0.22007 0.17590 0.21114 0.00020  -0.01642 0.01246  499 LEU A CG  
486  C CD1 . LEU A 65  ? 0.18421 0.13437 0.17638 -0.00383 -0.01537 0.01527  499 LEU A CD1 
487  C CD2 . LEU A 65  ? 0.19864 0.16540 0.19186 -0.00100 -0.01590 0.01229  499 LEU A CD2 
488  N N   . ALA A 66  ? 0.21720 0.16699 0.19987 0.01873  -0.01733 0.01400  500 ALA A N   
489  C CA  . ALA A 66  ? 0.20090 0.15001 0.18155 0.02434  -0.01758 0.01612  500 ALA A CA  
490  C C   . ALA A 66  ? 0.15286 0.11211 0.13539 0.02824  -0.01744 0.01414  500 ALA A C   
491  O O   . ALA A 66  ? 0.17839 0.14047 0.16051 0.03288  -0.01788 0.01555  500 ALA A O   
492  C CB  . ALA A 66  ? 0.16473 0.10133 0.14256 0.02740  -0.01828 0.01571  500 ALA A CB  
493  N N   . LEU A 67  ? 0.13088 0.09583 0.11569 0.02661  -0.01670 0.01107  501 LEU A N   
494  C CA  . LEU A 67  ? 0.15909 0.13405 0.14691 0.02937  -0.01568 0.00962  501 LEU A CA  
495  C C   . LEU A 67  ? 0.13384 0.11792 0.12492 0.02920  -0.01573 0.01142  501 LEU A C   
496  O O   . LEU A 67  ? 0.22990 0.22110 0.22377 0.03287  -0.01557 0.01068  501 LEU A O   
497  C CB  . LEU A 67  ? 0.11865 0.09765 0.10803 0.02692  -0.01427 0.00725  501 LEU A CB  
498  C CG  . LEU A 67  ? 0.12361 0.09727 0.10972 0.02859  -0.01416 0.00436  501 LEU A CG  
499  C CD1 . LEU A 67  ? 0.16262 0.14181 0.14972 0.02670  -0.01252 0.00314  501 LEU A CD1 
500  C CD2 . LEU A 67  ? 0.12926 0.10220 0.11410 0.03466  -0.01380 0.00299  501 LEU A CD2 
501  N N   . CYS A 68  ? 0.17232 0.15704 0.16347 0.02512  -0.01601 0.01329  502 CYS A N   
502  C CA  . CYS A 68  ? 0.24067 0.23413 0.23427 0.02508  -0.01643 0.01438  502 CYS A CA  
503  C C   . CYS A 68  ? 0.17856 0.16814 0.16806 0.02544  -0.01743 0.01806  502 CYS A C   
504  O O   . CYS A 68  ? 0.25793 0.25434 0.24778 0.02783  -0.01839 0.01894  502 CYS A O   
505  C CB  . CYS A 68  ? 0.12423 0.12468 0.12203 0.02031  -0.01545 0.01298  502 CYS A CB  
506  S SG  . CYS A 68  ? 0.11142 0.11748 0.11427 0.01993  -0.01345 0.00981  502 CYS A SG  
507  N N   . HIS A 69  ? 0.21764 0.19688 0.20345 0.02325  -0.01712 0.02018  503 HIS A N   
508  C CA  . HIS A 69  ? 0.25745 0.23309 0.23962 0.02246  -0.01700 0.02442  503 HIS A CA  
509  C C   . HIS A 69  ? 0.15285 0.11706 0.13023 0.02609  -0.01723 0.02759  503 HIS A C   
510  O O   . HIS A 69  ? 0.33377 0.28996 0.31087 0.02704  -0.01736 0.02598  503 HIS A O   
511  C CB  . HIS A 69  ? 0.20795 0.18152 0.19105 0.01602  -0.01573 0.02483  503 HIS A CB  
512  C CG  . HIS A 69  ? 0.18474 0.16879 0.17206 0.01291  -0.01549 0.02229  503 HIS A CG  
513  N ND1 . HIS A 69  ? 0.11355 0.10606 0.10122 0.01294  -0.01558 0.02314  503 HIS A ND1 
514  C CD2 . HIS A 69  ? 0.17899 0.16611 0.17014 0.01018  -0.01520 0.01887  503 HIS A CD2 
515  C CE1 . HIS A 69  ? 0.20800 0.20776 0.20022 0.01001  -0.01532 0.02009  503 HIS A CE1 
516  N NE2 . HIS A 69  ? 0.16717 0.16357 0.16140 0.00837  -0.01496 0.01788  503 HIS A NE2 
517  N N   . SER A 70  ? 0.20960 0.17292 0.18285 0.02849  -0.01724 0.03211  504 SER A N   
518  C CA  . SER A 70  ? 0.25772 0.20939 0.22591 0.03244  -0.01715 0.03618  504 SER A CA  
519  C C   . SER A 70  ? 0.23481 0.17376 0.20231 0.02738  -0.01518 0.03830  504 SER A C   
520  O O   . SER A 70  ? 0.25929 0.20017 0.22911 0.02122  -0.01380 0.03808  504 SER A O   
521  C CB  . SER A 70  ? 0.28365 0.23861 0.24672 0.03707  -0.01759 0.04100  504 SER A CB  
522  O OG  . SER A 70  ? 0.20005 0.15612 0.16126 0.03282  -0.01574 0.04436  504 SER A OG  
523  N N   . SER A 71  ? 0.24056 0.16650 0.20555 0.03009  -0.01506 0.04004  505 SER A N   
524  C CA  . SER A 71  ? 0.19229 0.10501 0.15765 0.02529  -0.01311 0.04190  505 SER A CA  
525  C C   . SER A 71  ? 0.31200 0.22434 0.27546 0.02158  -0.01043 0.04767  505 SER A C   
526  O O   . SER A 71  ? 0.22268 0.13193 0.18960 0.01475  -0.00853 0.04745  505 SER A O   
527  C CB  . SER A 71  ? 0.20716 0.10533 0.16972 0.02983  -0.01331 0.04357  505 SER A CB  
528  O OG  . SER A 71  ? 0.40604 0.30423 0.37049 0.03298  -0.01544 0.03770  505 SER A OG  
529  N N   . LYS A 72  ? 0.22206 0.13836 0.18002 0.02632  -0.01022 0.05268  506 LYS A N   
530  C CA  . LYS A 72  ? 0.22119 0.13742 0.17591 0.02380  -0.00725 0.05875  506 LYS A CA  
531  C C   . LYS A 72  ? 0.23671 0.16406 0.19589 0.01738  -0.00646 0.05585  506 LYS A C   
532  O O   . LYS A 72  ? 0.20527 0.12929 0.16618 0.01148  -0.00343 0.05811  506 LYS A O   
533  C CB  . LYS A 72  ? 0.30422 0.22512 0.25134 0.03125  -0.00789 0.06375  506 LYS A CB  
534  C CG  . LYS A 72  ? 0.31934 0.24432 0.26245 0.02923  -0.00497 0.06916  506 LYS A CG  
535  C CD  . LYS A 72  ? 0.38956 0.31521 0.32317 0.03732  -0.00514 0.07559  506 LYS A CD  
536  C CE  . LYS A 72  ? 0.41163 0.33580 0.34003 0.03499  -0.00073 0.08281  506 LYS A CE  
537  N NZ  . LYS A 72  ? 0.58201 0.50519 0.49945 0.04342  -0.00041 0.09028  506 LYS A NZ  
538  N N   . HIS A 73  ? 0.18581 0.12642 0.14749 0.01844  -0.00895 0.05078  507 HIS A N   
539  C CA  . HIS A 73  ? 0.16704 0.11805 0.13285 0.01315  -0.00839 0.04790  507 HIS A CA  
540  C C   . HIS A 73  ? 0.23790 0.18465 0.20983 0.00642  -0.00759 0.04441  507 HIS A C   
541  O O   . HIS A 73  ? 0.23312 0.18380 0.20791 0.00114  -0.00588 0.04425  507 HIS A O   
542  C CB  . HIS A 73  ? 0.19961 0.16404 0.16771 0.01572  -0.01112 0.04298  507 HIS A CB  
543  C CG  . HIS A 73  ? 0.25993 0.23344 0.23316 0.01055  -0.01083 0.03910  507 HIS A CG  
544  N ND1 . HIS A 73  ? 0.14175 0.12076 0.11423 0.00783  -0.00909 0.04096  507 HIS A ND1 
545  C CD2 . HIS A 73  ? 0.20294 0.18067 0.18181 0.00805  -0.01189 0.03371  507 HIS A CD2 
546  C CE1 . HIS A 73  ? 0.18067 0.16683 0.15856 0.00395  -0.00936 0.03652  507 HIS A CE1 
547  N NE2 . HIS A 73  ? 0.26841 0.25358 0.25004 0.00403  -0.01102 0.03237  507 HIS A NE2 
548  N N   . ILE A 74  ? 0.20086 0.14035 0.17484 0.00693  -0.00899 0.04118  508 ILE A N   
549  C CA  . ILE A 74  ? 0.19208 0.12823 0.17154 0.00126  -0.00892 0.03710  508 ILE A CA  
550  C C   . ILE A 74  ? 0.25931 0.18605 0.24010 -0.00368 -0.00607 0.04057  508 ILE A C   
551  O O   . ILE A 74  ? 0.30706 0.23624 0.29292 -0.00966 -0.00509 0.03860  508 ILE A O   
552  C CB  . ILE A 74  ? 0.16594 0.09705 0.14634 0.00386  -0.01123 0.03247  508 ILE A CB  
553  C CG1 . ILE A 74  ? 0.15217 0.09372 0.13245 0.00795  -0.01318 0.02925  508 ILE A CG1 
554  C CG2 . ILE A 74  ? 0.22252 0.15017 0.20789 -0.00133 -0.01168 0.02782  508 ILE A CG2 
555  C CD1 . ILE A 74  ? 0.15354 0.09131 0.13381 0.01156  -0.01488 0.02526  508 ILE A CD1 
556  N N   . SER A 75  ? 0.18547 0.10149 0.16214 -0.00120 -0.00447 0.04596  509 SER A N   
557  C CA  . SER A 75  ? 0.22921 0.13405 0.20799 -0.00607 -0.00121 0.04949  509 SER A CA  
558  C C   . SER A 75  ? 0.30243 0.21236 0.28094 -0.00986 0.00256  0.05449  509 SER A C   
559  O O   . SER A 75  ? 0.32386 0.22825 0.30703 -0.01601 0.00562  0.05592  509 SER A O   
560  C CB  . SER A 75  ? 0.22760 0.11787 0.20185 -0.00172 -0.00035 0.05418  509 SER A CB  
561  O OG  . SER A 75  ? 0.36474 0.25815 0.33112 0.00494  -0.00018 0.05966  509 SER A OG  
562  N N   . ILE A 76  ? 0.25846 0.17913 0.23204 -0.00635 0.00251  0.05684  510 ILE A N   
563  C CA  . ILE A 76  ? 0.24541 0.17210 0.21822 -0.00949 0.00614  0.06104  510 ILE A CA  
564  C C   . ILE A 76  ? 0.28214 0.21958 0.26207 -0.01513 0.00572  0.05548  510 ILE A C   
565  O O   . ILE A 76  ? 0.24057 0.17890 0.22447 -0.02080 0.00910  0.05701  510 ILE A O   
566  C CB  . ILE A 76  ? 0.21507 0.14921 0.17933 -0.00305 0.00605  0.06529  510 ILE A CB  
567  C CG1 . ILE A 76  ? 0.31397 0.25728 0.27758 -0.00604 0.00935  0.06790  510 ILE A CG1 
568  C CG2 . ILE A 76  ? 0.27032 0.21439 0.23410 0.00175  0.00133  0.05973  510 ILE A CG2 
569  C CD1 . ILE A 76  ? 0.49278 0.44367 0.44764 0.00034  0.00916  0.07160  510 ILE A CD1 
570  N N   . ILE A 77  ? 0.22606 0.17189 0.20796 -0.01349 0.00186  0.04920  511 ILE A N   
571  C CA  . ILE A 77  ? 0.18604 0.14033 0.17470 -0.01823 0.00110  0.04376  511 ILE A CA  
572  C C   . ILE A 77  ? 0.25738 0.20417 0.25281 -0.02366 0.00131  0.04088  511 ILE A C   
573  O O   . ILE A 77  ? 0.23248 0.18397 0.23402 -0.02899 0.00239  0.03871  511 ILE A O   
574  C CB  . ILE A 77  ? 0.15474 0.11754 0.14380 -0.01496 -0.00271 0.03830  511 ILE A CB  
575  C CG1 . ILE A 77  ? 0.16345 0.13378 0.14705 -0.00969 -0.00329 0.04029  511 ILE A CG1 
576  C CG2 . ILE A 77  ? 0.18322 0.15435 0.17845 -0.01907 -0.00338 0.03339  511 ILE A CG2 
577  C CD1 . ILE A 77  ? 0.18397 0.16220 0.16603 -0.01096 -0.00082 0.04305  511 ILE A CD1 
578  N N   . LYS A 78  ? 0.30160 0.23704 0.29644 -0.02217 0.00010  0.04032  512 LYS A N   
579  C CA  . LYS A 78  ? 0.25439 0.18209 0.25586 -0.02707 -0.00009 0.03683  512 LYS A CA  
580  C C   . LYS A 78  ? 0.30752 0.23000 0.31285 -0.03288 0.00446  0.04123  512 LYS A C   
581  O O   . LYS A 78  ? 0.21427 0.13809 0.22779 -0.03898 0.00494  0.03769  512 LYS A O   
582  C CB  . LYS A 78  ? 0.20452 0.12077 0.20380 -0.02341 -0.00226 0.03527  512 LYS A CB  
583  C CG  . LYS A 78  ? 0.42000 0.32915 0.42586 -0.02732 -0.00381 0.02951  512 LYS A CG  
584  C CD  . LYS A 78  ? 0.30724 0.20845 0.30971 -0.02203 -0.00676 0.02656  512 LYS A CD  
585  C CE  . LYS A 78  ? 0.36291 0.24874 0.36851 -0.02419 -0.00602 0.02615  512 LYS A CE  
586  N NZ  . LYS A 78  ? 0.44160 0.32681 0.45419 -0.02802 -0.00878 0.01778  512 LYS A NZ  
587  N N   . SER A 79  ? 0.23549 0.15258 0.23514 -0.03091 0.00800  0.04905  513 SER A N   
588  C CA  . SER A 79  ? 0.27454 0.18525 0.27736 -0.03624 0.01334  0.05448  513 SER A CA  
589  C C   . SER A 79  ? 0.24593 0.16871 0.25353 -0.04134 0.01605  0.05440  513 SER A C   
590  O O   . SER A 79  ? 0.23499 0.15453 0.24914 -0.04771 0.02019  0.05637  513 SER A O   
591  C CB  . SER A 79  ? 0.27790 0.18067 0.27170 -0.03170 0.01669  0.06375  513 SER A CB  
592  O OG  . SER A 79  ? 0.21052 0.12460 0.19695 -0.02730 0.01705  0.06699  513 SER A OG  
593  N N   . SER A 80  ? 0.24547 0.18205 0.25064 -0.03876 0.01402  0.05200  514 SER A N   
594  C CA  . SER A 80  ? 0.21290 0.16130 0.22240 -0.04285 0.01646  0.05155  514 SER A CA  
595  C C   . SER A 80  ? 0.18737 0.13903 0.20821 -0.04920 0.01528  0.04483  514 SER A C   
596  O O   . SER A 80  ? 0.17985 0.14029 0.20611 -0.05341 0.01785  0.04447  514 SER A O   
597  C CB  . SER A 80  ? 0.19450 0.15607 0.19907 -0.03821 0.01418  0.04983  514 SER A CB  
598  O OG  . SER A 80  ? 0.18835 0.15384 0.19520 -0.03656 0.00900  0.04266  514 SER A OG  
599  N N   . GLU A 81  ? 0.22857 0.17419 0.25298 -0.04951 0.01132  0.03920  515 GLU A N   
600  C CA  . GLU A 81  ? 0.23597 0.18526 0.27082 -0.05484 0.00947  0.03219  515 GLU A CA  
601  C C   . GLU A 81  ? 0.28434 0.22972 0.32815 -0.06239 0.01411  0.03410  515 GLU A C   
602  O O   . GLU A 81  ? 0.24200 0.19452 0.29564 -0.06743 0.01361  0.02898  515 GLU A O   
603  C CB  . GLU A 81  ? 0.28692 0.22985 0.32237 -0.05282 0.00432  0.02593  515 GLU A CB  
604  C CG  . GLU A 81  ? 0.30432 0.25337 0.34863 -0.05631 0.00089  0.01756  515 GLU A CG  
605  C CD  . GLU A 81  ? 0.32693 0.27294 0.36878 -0.05222 -0.00460 0.01139  515 GLU A CD  
606  O OE1 . GLU A 81  ? 0.35626 0.29868 0.38960 -0.04634 -0.00576 0.01337  515 GLU A OE1 
607  O OE2 . GLU A 81  ? 0.60491 0.55284 0.65335 -0.05462 -0.00773 0.00437  515 GLU A OE2 
608  N N   . HIS A 82  ? 0.32949 0.26399 0.37047 -0.06317 0.01882  0.04155  516 HIS A N   
609  C CA  . HIS A 82  ? 0.29802 0.22707 0.34795 -0.07071 0.02418  0.04427  516 HIS A CA  
610  C C   . HIS A 82  ? 0.22454 0.15564 0.27031 -0.07138 0.03125  0.05377  516 HIS A C   
611  O O   . HIS A 82  ? 0.29813 0.22166 0.34774 -0.07624 0.03678  0.05842  516 HIS A O   
612  C CB  . HIS A 82  ? 0.25414 0.16560 0.30608 -0.07199 0.02415  0.04454  516 HIS A CB  
613  C CG  . HIS A 82  ? 0.42658 0.33581 0.48161 -0.07072 0.01734  0.03507  516 HIS A CG  
614  N ND1 . HIS A 82  ? 0.41492 0.33131 0.48079 -0.07540 0.01420  0.02620  516 HIS A ND1 
615  C CD2 . HIS A 82  ? 0.32950 0.23082 0.37784 -0.06481 0.01309  0.03298  516 HIS A CD2 
616  C CE1 . HIS A 82  ? 0.31578 0.22855 0.38064 -0.07224 0.00831  0.01922  516 HIS A CE1 
617  N NE2 . HIS A 82  ? 0.40280 0.30640 0.45728 -0.06597 0.00777  0.02319  516 HIS A NE2 
618  N N   . MET A 83  ? 0.27703 0.21868 0.31428 -0.06629 0.03105  0.05609  517 MET A N   
619  C CA  . MET A 83  ? 0.28920 0.23307 0.31998 -0.06527 0.03730  0.06510  517 MET A CA  
620  C C   . MET A 83  ? 0.23744 0.19326 0.27635 -0.07118 0.04189  0.06496  517 MET A C   
621  O O   . MET A 83  ? 0.21824 0.18502 0.26521 -0.07373 0.03889  0.05737  517 MET A O   
622  C CB  . MET A 83  ? 0.20077 0.15111 0.21874 -0.05674 0.03475  0.06695  517 MET A CB  
623  C CG  . MET A 83  ? 0.20973 0.14814 0.21723 -0.05031 0.03360  0.07186  517 MET A CG  
624  S SD  . MET A 83  ? 0.23892 0.18712 0.23321 -0.04067 0.03040  0.07305  517 MET A SD  
625  C CE  . MET A 83  ? 0.30760 0.24009 0.29214 -0.03413 0.02973  0.07914  517 MET A CE  
626  N N   . LYS A 84  ? 0.28686 0.24058 0.32271 -0.07271 0.04920  0.07333  518 LYS A N   
627  C CA  . LYS A 84  ? 0.26081 0.22706 0.30026 -0.07632 0.05391  0.07352  518 LYS A CA  
628  C C   . LYS A 84  ? 0.24946 0.23041 0.28249 -0.07085 0.05273  0.07395  518 LYS A C   
629  O O   . LYS A 84  ? 0.29384 0.27318 0.31516 -0.06340 0.04934  0.07534  518 LYS A O   
630  C CB  . LYS A 84  ? 0.23632 0.19544 0.27014 -0.07787 0.06067  0.08110  518 LYS A CB  
631  N N   . PRO A 85  ? 0.33801 0.33379 0.37749 -0.07365 0.05435  0.07054  519 PRO A N   
632  C CA  . PRO A 85  ? 0.35837 0.36776 0.39029 -0.06769 0.05229  0.06865  519 PRO A CA  
633  C C   . PRO A 85  ? 0.28077 0.28929 0.29773 -0.06118 0.05528  0.07670  519 PRO A C   
634  O O   . PRO A 85  ? 0.23141 0.24467 0.23978 -0.05435 0.05058  0.07434  519 PRO A O   
635  C CB  . PRO A 85  ? 0.22980 0.25335 0.27198 -0.07268 0.05579  0.06560  519 PRO A CB  
636  C CG  . PRO A 85  ? 0.31643 0.33286 0.36941 -0.08053 0.05993  0.06543  519 PRO A CG  
637  C CD  . PRO A 85  ? 0.24119 0.24251 0.29490 -0.08122 0.05593  0.06477  519 PRO A CD  
638  N N   . ARG A 86  ? 0.21176 0.21431 0.22497 -0.06264 0.06265  0.08526  520 ARG A N   
639  C CA  . ARG A 86  ? 0.22217 0.22305 0.21948 -0.05530 0.06475  0.09237  520 ARG A CA  
640  C C   . ARG A 86  ? 0.22168 0.21361 0.21058 -0.04907 0.05947  0.09420  520 ARG A C   
641  O O   . ARG A 86  ? 0.28356 0.28110 0.26141 -0.04141 0.05650  0.09437  520 ARG A O   
642  C CB  . ARG A 86  ? 0.24296 0.23500 0.23612 -0.05748 0.07169  0.09882  520 ARG A CB  
643  N N   . ASP A 87  ? 0.26433 0.24239 0.25821 -0.05171 0.05737  0.09344  521 ASP A N   
644  C CA  . ASP A 87  ? 0.26239 0.23164 0.24848 -0.04532 0.05167  0.09307  521 ASP A CA  
645  C C   . ASP A 87  ? 0.23154 0.21004 0.21841 -0.04188 0.04366  0.08350  521 ASP A C   
646  O O   . ASP A 87  ? 0.21518 0.19338 0.19328 -0.03478 0.03941  0.08324  521 ASP A O   
647  C CB  . ASP A 87  ? 0.23283 0.18489 0.22450 -0.04898 0.05165  0.09408  521 ASP A CB  
648  C CG  . ASP A 87  ? 0.29478 0.23450 0.28028 -0.04913 0.05686  0.10142  521 ASP A CG  
649  O OD1 . ASP A 87  ? 0.41144 0.35375 0.38513 -0.04377 0.05932  0.10728  521 ASP A OD1 
650  O OD2 . ASP A 87  ? 0.55307 0.48096 0.54534 -0.05443 0.05778  0.10065  521 ASP A OD2 
651  N N   . LEU A 88  ? 0.20215 0.18895 0.19968 -0.04664 0.04162  0.07573  522 LEU A N   
652  C CA  . LEU A 88  ? 0.20512 0.20054 0.20338 -0.04344 0.03481  0.06737  522 LEU A CA  
653  C C   . LEU A 88  ? 0.20224 0.21007 0.19260 -0.03790 0.03442  0.06736  522 LEU A C   
654  O O   . LEU A 88  ? 0.16553 0.17677 0.15163 -0.03263 0.02921  0.06348  522 LEU A O   
655  C CB  . LEU A 88  ? 0.26495 0.26632 0.27583 -0.04925 0.03309  0.05977  522 LEU A CB  
656  C CG  . LEU A 88  ? 0.21355 0.20483 0.23268 -0.05358 0.03080  0.05633  522 LEU A CG  
657  C CD1 . LEU A 88  ? 0.23422 0.23338 0.26581 -0.05943 0.03019  0.04979  522 LEU A CD1 
658  C CD2 . LEU A 88  ? 0.16866 0.15497 0.18373 -0.04867 0.02440  0.05245  522 LEU A CD2 
659  N N   . ASN A 89  ? 0.24755 0.26267 0.23638 -0.03908 0.04000  0.07128  523 ASN A N   
660  C CA  . ASN A 89  ? 0.30277 0.32988 0.28352 -0.03344 0.03973  0.07096  523 ASN A CA  
661  C C   . ASN A 89  ? 0.30013 0.32270 0.26773 -0.02598 0.03870  0.07619  523 ASN A C   
662  O O   . ASN A 89  ? 0.22870 0.25774 0.19116 -0.02015 0.03389  0.07222  523 ASN A O   
663  C CB  . ASN A 89  ? 0.20797 0.24389 0.18959 -0.03613 0.04651  0.07426  523 ASN A CB  
664  C CG  . ASN A 89  ? 0.28869 0.33909 0.26431 -0.03090 0.04551  0.07121  523 ASN A CG  
665  O OD1 . ASN A 89  ? 0.51114 0.56562 0.47724 -0.02721 0.04961  0.07680  523 ASN A OD1 
666  N ND2 . ASN A 89  ? 0.53584 0.59385 0.51671 -0.03022 0.04004  0.06224  523 ASN A ND2 
667  N N   . ARG A 90  ? 0.29798 0.30933 0.26052 -0.02598 0.04313  0.08499  524 ARG A N   
668  C CA  . ARG A 90  ? 0.23962 0.24602 0.18926 -0.01822 0.04214  0.09061  524 ARG A CA  
669  C C   . ARG A 90  ? 0.24207 0.24482 0.19153 -0.01427 0.03461  0.08530  524 ARG A C   
670  O O   . ARG A 90  ? 0.30492 0.31353 0.24672 -0.00717 0.03071  0.08380  524 ARG A O   
671  C CB  . ARG A 90  ? 0.34394 0.33624 0.28969 -0.01948 0.04830  0.10111  524 ARG A CB  
672  N N   . LEU A 91  ? 0.19816 0.19202 0.15639 -0.01873 0.03250  0.08197  525 LEU A N   
673  C CA  . LEU A 91  ? 0.19104 0.18133 0.14940 -0.01515 0.02606  0.07719  525 LEU A CA  
674  C C   . LEU A 91  ? 0.20851 0.21205 0.16864 -0.01274 0.02098  0.06895  525 LEU A C   
675  O O   . LEU A 91  ? 0.23475 0.24062 0.19026 -0.00681 0.01665  0.06689  525 LEU A O   
676  C CB  . LEU A 91  ? 0.18887 0.16834 0.15641 -0.02058 0.02507  0.07450  525 LEU A CB  
677  C CG  . LEU A 91  ? 0.23680 0.21355 0.20599 -0.01774 0.01882  0.06862  525 LEU A CG  
678  C CD1 . LEU A 91  ? 0.21250 0.18516 0.17204 -0.00990 0.01684  0.07230  525 LEU A CD1 
679  C CD2 . LEU A 91  ? 0.18035 0.14654 0.15767 -0.02281 0.01823  0.06606  525 LEU A CD2 
680  N N   . GLY A 92  ? 0.17475 0.18703 0.14220 -0.01724 0.02153  0.06405  526 GLY A N   
681  C CA  . GLY A 92  ? 0.18051 0.20419 0.15027 -0.01521 0.01718  0.05642  526 GLY A CA  
682  C C   . GLY A 92  ? 0.23151 0.26481 0.19268 -0.00889 0.01640  0.05684  526 GLY A C   
683  O O   . GLY A 92  ? 0.17390 0.21327 0.13506 -0.00523 0.01172  0.05132  526 GLY A O   
684  N N   . ASP A 93  ? 0.16673 0.20177 0.12064 -0.00745 0.02106  0.06324  527 ASP A N   
685  C CA  . ASP A 93  ? 0.23771 0.28262 0.18225 -0.00073 0.02022  0.06353  527 ASP A CA  
686  C C   . ASP A 93  ? 0.32077 0.36184 0.25728 0.00629  0.01664  0.06564  527 ASP A C   
687  O O   . ASP A 93  ? 0.27084 0.32128 0.20092 0.01250  0.01395  0.06354  527 ASP A O   
688  C CB  . ASP A 93  ? 0.25656 0.30454 0.19457 -0.00069 0.02675  0.07039  527 ASP A CB  
689  C CG  . ASP A 93  ? 0.43427 0.49009 0.38006 -0.00639 0.03000  0.06716  527 ASP A CG  
690  O OD1 . ASP A 93  ? 0.41167 0.47087 0.36713 -0.00961 0.02665  0.05942  527 ASP A OD1 
691  O OD2 . ASP A 93  ? 0.67314 0.73191 0.61528 -0.00734 0.03613  0.07261  527 ASP A OD2 
692  N N   . GLU A 94  ? 0.23496 0.26302 0.17203 0.00573  0.01630  0.06917  528 GLU A N   
693  C CA  . GLU A 94  ? 0.30222 0.32668 0.23240 0.01275  0.01275  0.07095  528 GLU A CA  
694  C C   . GLU A 94  ? 0.24107 0.27208 0.17624 0.01500  0.00625  0.06220  528 GLU A C   
695  O O   . GLU A 94  ? 0.17669 0.20993 0.10666 0.02167  0.00265  0.06188  528 GLU A O   
696  C CB  . GLU A 94  ? 0.21206 0.22010 0.14190 0.01156  0.01455  0.07701  528 GLU A CB  
697  C CG  . GLU A 94  ? 0.22393 0.22377 0.14898 0.00948  0.02149  0.08661  528 GLU A CG  
698  C CD  . GLU A 94  ? 0.28977 0.27223 0.21553 0.00809  0.02316  0.09196  528 GLU A CD  
699  O OE1 . GLU A 94  ? 0.21516 0.19248 0.14542 0.00849  0.01885  0.08763  528 GLU A OE1 
700  O OE2 . GLU A 94  ? 0.46342 0.43716 0.38539 0.00663  0.02906  0.10050  528 GLU A OE2 
701  N N   . TYR A 95  ? 0.21581 0.25015 0.16110 0.00980  0.00486  0.05531  529 TYR A N   
702  C CA  . TYR A 95  ? 0.17414 0.21420 0.12521 0.01107  -0.00034 0.04737  529 TYR A CA  
703  C C   . TYR A 95  ? 0.22653 0.28055 0.17918 0.01194  -0.00185 0.04127  529 TYR A C   
704  O O   . TYR A 95  ? 0.18422 0.24365 0.13429 0.01101  0.00112  0.04250  529 TYR A O   
705  C CB  . TYR A 95  ? 0.20704 0.24089 0.16781 0.00543  -0.00096 0.04384  529 TYR A CB  
706  C CG  . TYR A 95  ? 0.16789 0.18798 0.12854 0.00419  0.00002  0.04810  529 TYR A CG  
707  C CD1 . TYR A 95  ? 0.22101 0.23282 0.18228 -0.00046 0.00421  0.05280  529 TYR A CD1 
708  C CD2 . TYR A 95  ? 0.23828 0.25399 0.19916 0.00751  -0.00320 0.04680  529 TYR A CD2 
709  C CE1 . TYR A 95  ? 0.23739 0.23621 0.19932 -0.00173 0.00490  0.05582  529 TYR A CE1 
710  C CE2 . TYR A 95  ? 0.29569 0.29874 0.25654 0.00674  -0.00247 0.04995  529 TYR A CE2 
711  C CZ  . TYR A 95  ? 0.28150 0.27577 0.24279 0.00212  0.00144  0.05430  529 TYR A CZ  
712  O OH  . TYR A 95  ? 0.29696 0.27813 0.25885 0.00123  0.00201  0.05671  529 TYR A OH  
713  N N   . ASN A 96  ? 0.22744 0.28719 0.18511 0.01359  -0.00630 0.03434  530 ASN A N   
714  C CA  . ASN A 96  ? 0.29223 0.36399 0.25369 0.01387  -0.00825 0.02713  530 ASN A CA  
715  C C   . ASN A 96  ? 0.17401 0.24458 0.14512 0.00761  -0.00735 0.02313  530 ASN A C   
716  O O   . ASN A 96  ? 0.15495 0.22100 0.13262 0.00552  -0.00898 0.02057  530 ASN A O   
717  C CB  . ASN A 96  ? 0.33671 0.41498 0.30010 0.01836  -0.01322 0.02154  530 ASN A CB  
718  C CG  . ASN A 96  ? 0.41406 0.50516 0.38001 0.01976  -0.01542 0.01413  530 ASN A CG  
719  O OD1 . ASN A 96  ? 0.58991 0.68514 0.55560 0.01782  -0.01324 0.01314  530 ASN A OD1 
720  N ND2 . ASN A 96  ? 0.30236 0.40021 0.27141 0.02322  -0.01977 0.00844  530 ASN A ND2 
721  N N   . SER A 97  ? 0.22806 0.30289 0.19960 0.00508  -0.00458 0.02287  531 SER A N   
722  C CA  . SER A 97  ? 0.13579 0.21160 0.11604 0.00020  -0.00400 0.01858  531 SER A CA  
723  C C   . SER A 97  ? 0.18107 0.24637 0.16585 -0.00439 -0.00284 0.02105  531 SER A C   
724  O O   . SER A 97  ? 0.11137 0.17407 0.10249 -0.00600 -0.00488 0.01742  531 SER A O   
725  C CB  . SER A 97  ? 0.09959 0.18157 0.08628 0.00119  -0.00770 0.01060  531 SER A CB  
726  O OG  . SER A 97  ? 0.15757 0.24973 0.14077 0.00543  -0.00928 0.00715  531 SER A OG  
727  N N   . ILE A 98  ? 0.16707 0.22646 0.14856 -0.00644 0.00065  0.02721  532 ILE A N   
728  C CA  . ILE A 98  ? 0.17173 0.22150 0.15755 -0.01088 0.00173  0.02912  532 ILE A CA  
729  C C   . ILE A 98  ? 0.19405 0.24380 0.18118 -0.01515 0.00615  0.03229  532 ILE A C   
730  O O   . ILE A 98  ? 0.17231 0.22421 0.15366 -0.01409 0.00945  0.03689  532 ILE A O   
731  C CB  . ILE A 98  ? 0.13027 0.16978 0.11199 -0.00908 0.00113  0.03347  532 ILE A CB  
732  C CG1 . ILE A 98  ? 0.13601 0.17523 0.11943 -0.00608 -0.00306 0.02949  532 ILE A CG1 
733  C CG2 . ILE A 98  ? 0.11762 0.14710 0.10272 -0.01377 0.00308  0.03608  532 ILE A CG2 
734  C CD1 . ILE A 98  ? 0.12495 0.16133 0.11590 -0.00928 -0.00451 0.02531  532 ILE A CD1 
735  N N   . PHE A 99  ? 0.13747 0.18553 0.13234 -0.01977 0.00630  0.02974  533 PHE A N   
736  C CA  . PHE A 99  ? 0.14882 0.19530 0.14729 -0.02473 0.01017  0.03239  533 PHE A CA  
737  C C   . PHE A 99  ? 0.16473 0.20091 0.16754 -0.02803 0.00924  0.03262  533 PHE A C   
738  O O   . PHE A 99  ? 0.18163 0.21507 0.18673 -0.02710 0.00549  0.02884  533 PHE A O   
739  C CB  . PHE A 99  ? 0.10437 0.16064 0.10921 -0.02702 0.01093  0.02797  533 PHE A CB  
740  C CG  . PHE A 99  ? 0.09418 0.15106 0.10583 -0.02777 0.00715  0.02185  533 PHE A CG  
741  C CD1 . PHE A 99  ? 0.09989 0.15220 0.11781 -0.03162 0.00664  0.02070  533 PHE A CD1 
742  C CD2 . PHE A 99  ? 0.09625 0.15829 0.10810 -0.02446 0.00418  0.01719  533 PHE A CD2 
743  C CE1 . PHE A 99  ? 0.13788 0.19086 0.16072 -0.03144 0.00322  0.01561  533 PHE A CE1 
744  C CE2 . PHE A 99  ? 0.08693 0.14863 0.10442 -0.02482 0.00129  0.01252  533 PHE A CE2 
745  C CZ  . PHE A 99  ? 0.08908 0.14630 0.11137 -0.02798 0.00082  0.01203  533 PHE A CZ  
746  N N   . ILE A 100 ? 0.12003 0.15046 0.12406 -0.03183 0.01284  0.03698  534 ILE A N   
747  C CA  . ILE A 100 ? 0.12224 0.14215 0.13011 -0.03486 0.01202  0.03707  534 ILE A CA  
748  C C   . ILE A 100 ? 0.12428 0.14498 0.14049 -0.04123 0.01497  0.03670  534 ILE A C   
749  O O   . ILE A 100 ? 0.14785 0.17207 0.16429 -0.04348 0.01975  0.04050  534 ILE A O   
750  C CB  . ILE A 100 ? 0.13735 0.14613 0.13861 -0.03283 0.01319  0.04301  534 ILE A CB  
751  C CG1 . ILE A 100 ? 0.14846 0.15969 0.14102 -0.02615 0.01128  0.04431  534 ILE A CG1 
752  C CG2 . ILE A 100 ? 0.13425 0.13245 0.13871 -0.03418 0.01068  0.04110  534 ILE A CG2 
753  C CD1 . ILE A 100 ? 0.17741 0.17811 0.16318 -0.02287 0.01161  0.04970  534 ILE A CD1 
754  N N   . SER A 101 ? 0.12008 0.13805 0.14323 -0.04394 0.01219  0.03202  535 SER A N   
755  C CA  . SER A 101 ? 0.14502 0.16253 0.17739 -0.05014 0.01404  0.03070  535 SER A CA  
756  C C   . SER A 101 ? 0.12808 0.13358 0.16250 -0.05183 0.01216  0.02989  535 SER A C   
757  O O   . SER A 101 ? 0.13168 0.13020 0.16039 -0.04788 0.00930  0.02998  535 SER A O   
758  C CB  . SER A 101 ? 0.13587 0.16398 0.17579 -0.05146 0.01178  0.02421  535 SER A CB  
759  O OG  . SER A 101 ? 0.13786 0.16392 0.17831 -0.04915 0.00642  0.01909  535 SER A OG  
760  N N   . ASN A 102 ? 0.19501 0.19868 0.23839 -0.05778 0.01375  0.02852  536 ASN A N   
761  C CA  . ASN A 102 ? 0.14983 0.14189 0.19613 -0.05988 0.01213  0.02708  536 ASN A CA  
762  C C   . ASN A 102 ? 0.19015 0.18156 0.23613 -0.05675 0.00586  0.02049  536 ASN A C   
763  O O   . ASN A 102 ? 0.19326 0.17445 0.23797 -0.05603 0.00384  0.01948  536 ASN A O   
764  C CB  . ASN A 102 ? 0.14518 0.13702 0.20303 -0.06744 0.01491  0.02573  536 ASN A CB  
765  C CG  . ASN A 102 ? 0.20671 0.19133 0.26422 -0.07086 0.02160  0.03358  536 ASN A CG  
766  O OD1 . ASN A 102 ? 0.22269 0.19809 0.27114 -0.06739 0.02306  0.03953  536 ASN A OD1 
767  N ND2 . ASN A 102 ? 0.25477 0.24373 0.32231 -0.07750 0.02590  0.03384  536 ASN A ND2 
768  N N   . GLU A 103 ? 0.17128 0.17296 0.21799 -0.05454 0.00298  0.01621  537 GLU A N   
769  C CA  . GLU A 103 ? 0.12551 0.12723 0.17122 -0.05117 -0.00238 0.01066  537 GLU A CA  
770  C C   . GLU A 103 ? 0.13945 0.14013 0.17602 -0.04493 -0.00402 0.01221  537 GLU A C   
771  O O   . GLU A 103 ? 0.10647 0.10637 0.14121 -0.04173 -0.00774 0.00858  537 GLU A O   
772  C CB  . GLU A 103 ? 0.10723 0.12010 0.15937 -0.05202 -0.00458 0.00522  537 GLU A CB  
773  C CG  . GLU A 103 ? 0.15889 0.17612 0.22176 -0.05827 -0.00289 0.00304  537 GLU A CG  
774  C CD  . GLU A 103 ? 0.19279 0.21762 0.25810 -0.06084 0.00218  0.00688  537 GLU A CD  
775  O OE1 . GLU A 103 ? 0.14228 0.16884 0.20030 -0.05745 0.00397  0.01090  537 GLU A OE1 
776  O OE2 . GLU A 103 ? 0.24632 0.27603 0.32115 -0.06617 0.00442  0.00554  537 GLU A OE2 
777  N N   . SER A 104 ? 0.12623 0.12737 0.15725 -0.04305 -0.00124 0.01738  538 SER A N   
778  C CA  . SER A 104 ? 0.10660 0.10917 0.13072 -0.03752 -0.00280 0.01808  538 SER A CA  
779  C C   . SER A 104 ? 0.10868 0.10275 0.12898 -0.03432 -0.00546 0.01720  538 SER A C   
780  O O   . SER A 104 ? 0.10254 0.09881 0.12124 -0.03098 -0.00815 0.01431  538 SER A O   
781  C CB  . SER A 104 ? 0.10990 0.11394 0.12865 -0.03592 0.00032  0.02350  538 SER A CB  
782  O OG  . SER A 104 ? 0.11580 0.12928 0.13722 -0.03785 0.00267  0.02370  538 SER A OG  
783  N N   . TYR A 105 ? 0.16246 0.14654 0.18138 -0.03518 -0.00440 0.01982  539 TYR A N   
784  C CA  . TYR A 105 ? 0.15236 0.12811 0.16748 -0.03171 -0.00667 0.01897  539 TYR A CA  
785  C C   . TYR A 105 ? 0.14701 0.12361 0.16476 -0.03125 -0.01025 0.01285  539 TYR A C   
786  O O   . TYR A 105 ? 0.16035 0.13730 0.17443 -0.02693 -0.01232 0.01123  539 TYR A O   
787  C CB  . TYR A 105 ? 0.16712 0.13123 0.18182 -0.03337 -0.00484 0.02220  539 TYR A CB  
788  C CG  . TYR A 105 ? 0.21684 0.17150 0.22812 -0.02975 -0.00708 0.02094  539 TYR A CG  
789  C CD1 . TYR A 105 ? 0.13739 0.09170 0.14221 -0.02392 -0.00795 0.02274  539 TYR A CD1 
790  C CD2 . TYR A 105 ? 0.17658 0.12313 0.19166 -0.03208 -0.00835 0.01746  539 TYR A CD2 
791  C CE1 . TYR A 105 ? 0.19541 0.14178 0.19739 -0.02026 -0.00977 0.02142  539 TYR A CE1 
792  C CE2 . TYR A 105 ? 0.17513 0.11317 0.18692 -0.02836 -0.01036 0.01584  539 TYR A CE2 
793  C CZ  . TYR A 105 ? 0.19345 0.13151 0.19855 -0.02235 -0.01091 0.01802  539 TYR A CZ  
794  O OH  . TYR A 105 ? 0.19538 0.12565 0.19749 -0.01833 -0.01269 0.01622  539 TYR A OH  
795  N N   . THR A 106 ? 0.11967 0.09744 0.14390 -0.03551 -0.01089 0.00935  540 THR A N   
796  C CA  . THR A 106 ? 0.12697 0.10654 0.15323 -0.03463 -0.01463 0.00327  540 THR A CA  
797  C C   . THR A 106 ? 0.16854 0.15618 0.19214 -0.03080 -0.01608 0.00203  540 THR A C   
798  O O   . THR A 106 ? 0.15073 0.13710 0.17076 -0.02690 -0.01832 -0.00020 540 THR A O   
799  C CB  . THR A 106 ? 0.16794 0.15064 0.20266 -0.03986 -0.01515 -0.00048 540 THR A CB  
800  O OG1 . THR A 106 ? 0.28473 0.25815 0.32282 -0.04330 -0.01453 -0.00089 540 THR A OG1 
801  C CG2 . THR A 106 ? 0.18453 0.17274 0.22072 -0.03798 -0.01929 -0.00664 540 THR A CG2 
802  N N   . CYS A 107 ? 0.14032 0.13608 0.16569 -0.03178 -0.01448 0.00352  541 CYS A N   
803  C CA  . CYS A 107 ? 0.16343 0.16610 0.18742 -0.02856 -0.01561 0.00222  541 CYS A CA  
804  C C   . CYS A 107 ? 0.11473 0.11506 0.13287 -0.02414 -0.01545 0.00425  541 CYS A C   
805  O O   . CYS A 107 ? 0.13856 0.14029 0.15487 -0.02092 -0.01685 0.00255  541 CYS A O   
806  C CB  . CYS A 107 ? 0.14097 0.15221 0.16830 -0.03038 -0.01380 0.00310  541 CYS A CB  
807  S SG  . CYS A 107 ? 0.13674 0.15358 0.17261 -0.03540 -0.01381 0.00012  541 CYS A SG  
808  N N   . ALA A 108 ? 0.09322 0.09027 0.10852 -0.02374 -0.01361 0.00800  542 ALA A N   
809  C CA  . ALA A 108 ? 0.13929 0.13505 0.15013 -0.01951 -0.01370 0.00940  542 ALA A CA  
810  C C   . ALA A 108 ? 0.09544 0.08494 0.10376 -0.01689 -0.01540 0.00759  542 ALA A C   
811  O O   . ALA A 108 ? 0.12966 0.12034 0.13575 -0.01333 -0.01575 0.00717  542 ALA A O   
812  C CB  . ALA A 108 ? 0.16266 0.15657 0.17066 -0.01895 -0.01187 0.01362  542 ALA A CB  
813  N N   . LEU A 109 ? 0.12453 0.10765 0.13362 -0.01864 -0.01628 0.00617  543 LEU A N   
814  C CA  . LEU A 109 ? 0.10665 0.08452 0.11329 -0.01590 -0.01823 0.00333  543 LEU A CA  
815  C C   . LEU A 109 ? 0.11724 0.10009 0.12392 -0.01425 -0.01997 -0.00015 543 LEU A C   
816  O O   . LEU A 109 ? 0.13290 0.11496 0.13589 -0.01023 -0.02053 -0.00110 543 LEU A O   
817  C CB  . LEU A 109 ? 0.15431 0.12435 0.16277 -0.01850 -0.01907 0.00162  543 LEU A CB  
818  C CG  . LEU A 109 ? 0.12849 0.09071 0.13593 -0.01931 -0.01717 0.00553  543 LEU A CG  
819  C CD1 . LEU A 109 ? 0.13183 0.08493 0.14175 -0.02169 -0.01814 0.00295  543 LEU A CD1 
820  C CD2 . LEU A 109 ? 0.12932 0.08952 0.13138 -0.01412 -0.01682 0.00787  543 LEU A CD2 
821  N N   . LEU A 110 ? 0.14024 0.12842 0.15090 -0.01695 -0.02063 -0.00186 544 LEU A N   
822  C CA  . LEU A 110 ? 0.09513 0.08797 0.10530 -0.01475 -0.02236 -0.00466 544 LEU A CA  
823  C C   . LEU A 110 ? 0.08936 0.08608 0.09732 -0.01166 -0.02083 -0.00242 544 LEU A C   
824  O O   . LEU A 110 ? 0.16263 0.15982 0.16746 -0.00809 -0.02138 -0.00334 544 LEU A O   
825  C CB  . LEU A 110 ? 0.13756 0.13600 0.15312 -0.01798 -0.02345 -0.00689 544 LEU A CB  
826  C CG  . LEU A 110 ? 0.21192 0.20805 0.23082 -0.02052 -0.02585 -0.01106 544 LEU A CG  
827  C CD1 . LEU A 110 ? 0.30534 0.30884 0.33092 -0.02377 -0.02672 -0.01337 544 LEU A CD1 
828  C CD2 . LEU A 110 ? 0.12556 0.11922 0.14004 -0.01639 -0.02878 -0.01480 544 LEU A CD2 
829  N N   . ALA A 111 ? 0.08516 0.08475 0.09480 -0.01294 -0.01876 0.00043  545 ALA A N   
830  C CA  . ALA A 111 ? 0.08019 0.08342 0.08930 -0.01059 -0.01732 0.00187  545 ALA A CA  
831  C C   . ALA A 111 ? 0.13075 0.13063 0.13620 -0.00709 -0.01662 0.00273  545 ALA A C   
832  O O   . ALA A 111 ? 0.11313 0.11473 0.11776 -0.00455 -0.01571 0.00292  545 ALA A O   
833  C CB  . ALA A 111 ? 0.07638 0.08369 0.08811 -0.01251 -0.01572 0.00378  545 ALA A CB  
834  N N   . ALA A 112 ? 0.08657 0.08156 0.09008 -0.00678 -0.01673 0.00345  546 ALA A N   
835  C CA  . ALA A 112 ? 0.08948 0.08189 0.08992 -0.00308 -0.01610 0.00390  546 ALA A CA  
836  C C   . ALA A 112 ? 0.12553 0.11513 0.12253 -0.00043 -0.01717 0.00151  546 ALA A C   
837  O O   . ALA A 112 ? 0.09794 0.08882 0.09296 0.00284  -0.01590 0.00180  546 ALA A O   
838  C CB  . ALA A 112 ? 0.12032 0.10805 0.11947 -0.00280 -0.01609 0.00536  546 ALA A CB  
839  N N   . GLY A 113 ? 0.11836 0.10461 0.11483 -0.00173 -0.01938 -0.00105 547 GLY A N   
840  C CA  . GLY A 113 ? 0.10246 0.08669 0.09504 0.00132  -0.02099 -0.00413 547 GLY A CA  
841  C C   . GLY A 113 ? 0.14670 0.13585 0.13791 0.00334  -0.02078 -0.00431 547 GLY A C   
842  O O   . GLY A 113 ? 0.16907 0.15786 0.15554 0.00751  -0.02052 -0.00499 547 GLY A O   
843  N N   . SER A 114 ? 0.10883 0.10248 0.10381 0.00083  -0.02067 -0.00349 548 SER A N   
844  C CA  . SER A 114 ? 0.13808 0.13559 0.13189 0.00309  -0.02023 -0.00302 548 SER A CA  
845  C C   . SER A 114 ? 0.13566 0.13362 0.12771 0.00593  -0.01688 0.00001  548 SER A C   
846  O O   . SER A 114 ? 0.12881 0.12722 0.11702 0.00955  -0.01596 0.00067  548 SER A O   
847  C CB  . SER A 114 ? 0.11241 0.11446 0.11133 0.00003  -0.02042 -0.00265 548 SER A CB  
848  O OG  . SER A 114 ? 0.15151 0.15431 0.15292 -0.00260 -0.02321 -0.00565 548 SER A OG  
849  N N   . CYS A 115 ? 0.14905 0.14724 0.14404 0.00447  -0.01489 0.00191  549 CYS A N   
850  C CA  . CYS A 115 ? 0.12024 0.11984 0.11561 0.00647  -0.01159 0.00424  549 CYS A CA  
851  C C   . CYS A 115 ? 0.12819 0.12512 0.11897 0.01018  -0.01073 0.00399  549 CYS A C   
852  O O   . CYS A 115 ? 0.11240 0.11050 0.10180 0.01289  -0.00784 0.00563  549 CYS A O   
853  C CB  . CYS A 115 ? 0.08167 0.08396 0.08247 0.00391  -0.01037 0.00544  549 CYS A CB  
854  S SG  . CYS A 115 ? 0.13476 0.14129 0.14087 0.00055  -0.01049 0.00555  549 CYS A SG  
855  N N   . PHE A 116 ? 0.09615 0.08931 0.08478 0.01040  -0.01284 0.00203  550 PHE A N   
856  C CA  . PHE A 116 ? 0.11224 0.10269 0.09600 0.01450  -0.01242 0.00095  550 PHE A CA  
857  C C   . PHE A 116 ? 0.18009 0.17082 0.15819 0.01802  -0.01249 0.00001  550 PHE A C   
858  O O   . PHE A 116 ? 0.16752 0.15956 0.14258 0.02165  -0.00953 0.00152  550 PHE A O   
859  C CB  . PHE A 116 ? 0.12633 0.11137 0.10881 0.01414  -0.01516 -0.00162 550 PHE A CB  
860  C CG  . PHE A 116 ? 0.10877 0.09272 0.09525 0.01159  -0.01507 -0.00007 550 PHE A CG  
861  C CD1 . PHE A 116 ? 0.10117 0.08975 0.09153 0.01083  -0.01286 0.00263  550 PHE A CD1 
862  C CD2 . PHE A 116 ? 0.12744 0.10558 0.11373 0.01021  -0.01721 -0.00140 550 PHE A CD2 
863  C CE1 . PHE A 116 ? 0.09725 0.08549 0.09014 0.00938  -0.01315 0.00396  550 PHE A CE1 
864  C CE2 . PHE A 116 ? 0.10818 0.08488 0.09689 0.00860  -0.01689 0.00080  550 PHE A CE2 
865  C CZ  . PHE A 116 ? 0.10234 0.08448 0.09379 0.00852  -0.01504 0.00347  550 PHE A CZ  
866  N N   . ASN A 117 ? 0.14102 0.13114 0.11774 0.01719  -0.01575 -0.00246 551 ASN A N   
867  C CA  . ASN A 117 ? 0.13655 0.12772 0.10729 0.02111  -0.01658 -0.00358 551 ASN A CA  
868  C C   . ASN A 117 ? 0.17255 0.16672 0.14248 0.02305  -0.01270 0.00070  551 ASN A C   
869  O O   . ASN A 117 ? 0.17679 0.17125 0.14029 0.02785  -0.01105 0.00165  551 ASN A O   
870  C CB  . ASN A 117 ? 0.15450 0.14646 0.12628 0.01922  -0.02086 -0.00685 551 ASN A CB  
871  C CG  . ASN A 117 ? 0.12726 0.11576 0.09800 0.01889  -0.02472 -0.01207 551 ASN A CG  
872  O OD1 . ASN A 117 ? 0.18419 0.16884 0.15311 0.02018  -0.02430 -0.01312 551 ASN A OD1 
873  N ND2 . ASN A 117 ? 0.14726 0.13721 0.11990 0.01716  -0.02853 -0.01571 551 ASN A ND2 
874  N N   . SER A 118 ? 0.11099 0.10716 0.08733 0.01949  -0.01097 0.00334  552 SER A N   
875  C CA  . SER A 118 ? 0.11959 0.11752 0.09654 0.02074  -0.00707 0.00731  552 SER A CA  
876  C C   . SER A 118 ? 0.20416 0.20232 0.18089 0.02265  -0.00242 0.00984  552 SER A C   
877  O O   . SER A 118 ? 0.15549 0.15370 0.12807 0.02625  0.00093  0.01257  552 SER A O   
878  C CB  . SER A 118 ? 0.18369 0.18359 0.16833 0.01636  -0.00673 0.00843  552 SER A CB  
879  O OG  . SER A 118 ? 0.15421 0.15495 0.13888 0.01552  -0.01011 0.00669  552 SER A OG  
880  N N   . ALA A 119 ? 0.18336 0.18201 0.16458 0.02054  -0.00198 0.00914  553 ALA A N   
881  C CA  . ALA A 119 ? 0.17996 0.18010 0.16215 0.02240  0.00219  0.01086  553 ALA A CA  
882  C C   . ALA A 119 ? 0.13736 0.13609 0.11107 0.02775  0.00292  0.01021  553 ALA A C   
883  O O   . ALA A 119 ? 0.11688 0.11729 0.08922 0.03050  0.00759  0.01280  553 ALA A O   
884  C CB  . ALA A 119 ? 0.09998 0.10129 0.08769 0.02013  0.00144  0.00954  553 ALA A CB  
885  N N   . GLN A 120 ? 0.13566 0.13157 0.10391 0.02927  -0.00145 0.00654  554 GLN A N   
886  C CA  . GLN A 120 ? 0.19953 0.19435 0.15909 0.03482  -0.00142 0.00486  554 GLN A CA  
887  C C   . GLN A 120 ? 0.18461 0.18050 0.13755 0.03861  0.00043  0.00727  554 GLN A C   
888  O O   . GLN A 120 ? 0.19553 0.19236 0.14223 0.04353  0.00376  0.00867  554 GLN A O   
889  C CB  . GLN A 120 ? 0.21008 0.20136 0.16662 0.03505  -0.00700 -0.00053 554 GLN A CB  
890  C CG  . GLN A 120 ? 0.27354 0.26377 0.22098 0.04104  -0.00784 -0.00366 554 GLN A CG  
891  C CD  . GLN A 120 ? 0.28697 0.27302 0.23325 0.04069  -0.01332 -0.00976 554 GLN A CD  
892  O OE1 . GLN A 120 ? 0.31341 0.29850 0.26141 0.03785  -0.01738 -0.01223 554 GLN A OE1 
893  N NE2 . GLN A 120 ? 0.48054 0.46409 0.42471 0.04346  -0.01328 -0.01241 554 GLN A NE2 
894  N N   . ALA A 121 ? 0.21056 0.20650 0.16439 0.03688  -0.00150 0.00801  555 ALA A N   
895  C CA  . ALA A 121 ? 0.25556 0.25212 0.20289 0.04102  0.00028  0.01102  555 ALA A CA  
896  C C   . ALA A 121 ? 0.18114 0.17855 0.13023 0.04172  0.00747  0.01703  555 ALA A C   
897  O O   . ALA A 121 ? 0.27560 0.27318 0.21704 0.04691  0.01100  0.02002  555 ALA A O   
898  C CB  . ALA A 121 ? 0.15412 0.15086 0.10359 0.03895  -0.00313 0.01068  555 ALA A CB  
899  N N   . ILE A 122 ? 0.19057 0.18876 0.14988 0.03657  0.00985  0.01872  556 ILE A N   
900  C CA  . ILE A 122 ? 0.12996 0.12922 0.09350 0.03616  0.01677  0.02373  556 ILE A CA  
901  C C   . ILE A 122 ? 0.13505 0.13618 0.09561 0.03947  0.02068  0.02424  556 ILE A C   
902  O O   . ILE A 122 ? 0.18054 0.18213 0.13752 0.04271  0.02643  0.02857  556 ILE A O   
903  C CB  . ILE A 122 ? 0.18434 0.18502 0.16032 0.02985  0.01747  0.02375  556 ILE A CB  
904  C CG1 . ILE A 122 ? 0.15620 0.15544 0.13505 0.02710  0.01449  0.02355  556 ILE A CG1 
905  C CG2 . ILE A 122 ? 0.13237 0.13482 0.11474 0.02883  0.02456  0.02777  556 ILE A CG2 
906  C CD1 . ILE A 122 ? 0.10633 0.10749 0.09599 0.02134  0.01351  0.02189  556 ILE A CD1 
907  N N   . LEU A 123 ? 0.13210 0.13422 0.09402 0.03897  0.01791  0.02004  557 LEU A N   
908  C CA  . LEU A 123 ? 0.14102 0.14583 0.10269 0.04159  0.02178  0.02015  557 LEU A CA  
909  C C   . LEU A 123 ? 0.23439 0.23880 0.18382 0.04854  0.02282  0.01999  557 LEU A C   
910  O O   . LEU A 123 ? 0.18313 0.19038 0.13108 0.05163  0.02839  0.02221  557 LEU A O   
911  C CB  . LEU A 123 ? 0.12978 0.13522 0.09638 0.03961  0.01823  0.01580  557 LEU A CB  
912  C CG  . LEU A 123 ? 0.17513 0.18298 0.15370 0.03396  0.01836  0.01606  557 LEU A CG  
913  C CD1 . LEU A 123 ? 0.11627 0.12325 0.09687 0.03293  0.01364  0.01204  557 LEU A CD1 
914  C CD2 . LEU A 123 ? 0.11928 0.13222 0.10527 0.03334  0.02484  0.01896  557 LEU A CD2 
915  N N   . THR A 124 ? 0.15118 0.15290 0.09207 0.05123  0.01763  0.01706  558 THR A N   
916  C CA  . THR A 124 ? 0.16299 0.16490 0.09135 0.05843  0.01791  0.01619  558 THR A CA  
917  C C   . THR A 124 ? 0.17058 0.17246 0.09189 0.06197  0.02135  0.02154  558 THR A C   
918  O O   . THR A 124 ? 0.18160 0.18405 0.09104 0.06870  0.02134  0.02115  558 THR A O   
919  C CB  . THR A 124 ? 0.16541 0.16503 0.08825 0.06006  0.01012  0.00926  558 THR A CB  
920  O OG1 . THR A 124 ? 0.16098 0.15899 0.08601 0.05677  0.00553  0.00851  558 THR A OG1 
921  C CG2 . THR A 124 ? 0.16095 0.15926 0.08920 0.05770  0.00734  0.00449  558 THR A CG2 
922  N N   . GLY A 125 ? 0.16601 0.16698 0.09387 0.05808  0.02411  0.02637  559 GLY A N   
923  C CA  . GLY A 125 ? 0.17428 0.17406 0.09606 0.06153  0.02821  0.03248  559 GLY A CA  
924  C C   . GLY A 125 ? 0.18930 0.18720 0.10430 0.06400  0.02265  0.03135  559 GLY A C   
925  O O   . GLY A 125 ? 0.18652 0.18317 0.09441 0.06835  0.02560  0.03653  559 GLY A O   
926  N N   . GLN A 126 ? 0.17134 0.16918 0.08849 0.06157  0.01491  0.02492  560 GLN A N   
927  C CA  . GLN A 126 ? 0.25137 0.24879 0.16375 0.06363  0.00936  0.02317  560 GLN A CA  
928  C C   . GLN A 126 ? 0.16983 0.16541 0.08838 0.06053  0.01117  0.02792  560 GLN A C   
929  O O   . GLN A 126 ? 0.17674 0.17162 0.08892 0.06478  0.01041  0.03043  560 GLN A O   
930  C CB  . GLN A 126 ? 0.21279 0.21089 0.12825 0.06072  0.00137  0.01511  560 GLN A CB  
931  C CG  . GLN A 126 ? 0.28008 0.27894 0.18949 0.06408  -0.00113 0.00954  560 GLN A CG  
932  C CD  . GLN A 126 ? 0.60586 0.60400 0.52064 0.05992  -0.00801 0.00210  560 GLN A CD  
933  O OE1 . GLN A 126 ? 0.51085 0.50782 0.42656 0.05938  -0.00895 -0.00177 560 GLN A OE1 
934  N NE2 . GLN A 126 ? 0.45308 0.45175 0.37176 0.05704  -0.01258 0.00019  560 GLN A NE2 
935  N N   . VAL A 127 ? 0.24250 0.23737 0.17326 0.05362  0.01330  0.02887  561 VAL A N   
936  C CA  . VAL A 127 ? 0.17786 0.17069 0.11577 0.05037  0.01586  0.03308  561 VAL A CA  
937  C C   . VAL A 127 ? 0.18765 0.18008 0.13400 0.04663  0.02293  0.03689  561 VAL A C   
938  O O   . VAL A 127 ? 0.15371 0.14836 0.10262 0.04527  0.02426  0.03503  561 VAL A O   
939  C CB  . VAL A 127 ? 0.14686 0.14036 0.09291 0.04508  0.01014  0.02880  561 VAL A CB  
940  C CG1 . VAL A 127 ? 0.14704 0.14240 0.08715 0.04756  0.00279  0.02331  561 VAL A CG1 
941  C CG2 . VAL A 127 ? 0.19048 0.18531 0.14694 0.03856  0.01013  0.02610  561 VAL A CG2 
942  N N   . ARG A 128 ? 0.19775 0.18741 0.14900 0.04511  0.02746  0.04200  562 ARG A N   
943  C CA  . ARG A 128 ? 0.22816 0.21799 0.18973 0.04069  0.03391  0.04477  562 ARG A CA  
944  C C   . ARG A 128 ? 0.19879 0.19044 0.17322 0.03355  0.03103  0.04057  562 ARG A C   
945  O O   . ARG A 128 ? 0.20815 0.20293 0.19017 0.03008  0.03279  0.03892  562 ARG A O   
946  C CB  . ARG A 128 ? 0.18126 0.16658 0.14348 0.04188  0.04086  0.05214  562 ARG A CB  
947  C CG  . ARG A 128 ? 0.45539 0.43750 0.40371 0.04952  0.04115  0.05639  562 ARG A CG  
948  C CD  . ARG A 128 ? 0.56734 0.55183 0.50348 0.05574  0.04276  0.05721  562 ARG A CD  
949  N NE  . ARG A 128 ? 0.42281 0.40627 0.34452 0.06345  0.03928  0.05804  562 ARG A NE  
950  C CZ  . ARG A 128 ? 0.47855 0.46485 0.38794 0.06972  0.03760  0.05631  562 ARG A CZ  
951  N NH1 . ARG A 128 ? 0.42424 0.41403 0.33372 0.06934  0.03917  0.05375  562 ARG A NH1 
952  N NH2 . ARG A 128 ? 0.58257 0.56859 0.47933 0.07694  0.03395  0.05668  562 ARG A NH2 
953  N N   . ASN A 129 ? 0.13349 0.12390 0.11016 0.03180  0.02655  0.03865  563 ASN A N   
954  C CA  . ASN A 129 ? 0.21061 0.20311 0.19790 0.02575  0.02349  0.03456  563 ASN A CA  
955  C C   . ASN A 129 ? 0.21253 0.20569 0.19658 0.02599  0.01643  0.03057  563 ASN A C   
956  O O   . ASN A 129 ? 0.21497 0.20708 0.18993 0.03060  0.01399  0.03088  563 ASN A O   
957  C CB  . ASN A 129 ? 0.12793 0.11841 0.12536 0.02214  0.02756  0.03698  563 ASN A CB  
958  C CG  . ASN A 129 ? 0.16013 0.14533 0.15347 0.02542  0.02918  0.04131  563 ASN A CG  
959  O OD1 . ASN A 129 ? 0.13857 0.12319 0.12521 0.02849  0.02456  0.04023  563 ASN A OD1 
960  N ND2 . ASN A 129 ? 0.13517 0.11648 0.13299 0.02490  0.03586  0.04626  563 ASN A ND2 
961  N N   . ALA A 130 ? 0.15781 0.15339 0.14948 0.02115  0.01316  0.02665  564 ALA A N   
962  C CA  . ALA A 130 ? 0.14241 0.13945 0.13220 0.02066  0.00699  0.02271  564 ALA A CA  
963  C C   . ALA A 130 ? 0.18197 0.18116 0.18105 0.01554  0.00533  0.02017  564 ALA A C   
964  O O   . ALA A 130 ? 0.10552 0.10600 0.11199 0.01221  0.00769  0.02001  564 ALA A O   
965  C CB  . ALA A 130 ? 0.10547 0.10391 0.09030 0.02145  0.00356  0.01938  564 ALA A CB  
966  N N   . VAL A 131 ? 0.15046 0.15087 0.14912 0.01522  0.00112  0.01778  565 VAL A N   
967  C CA  . VAL A 131 ? 0.09621 0.09938 0.10227 0.01105  -0.00079 0.01508  565 VAL A CA  
968  C C   . VAL A 131 ? 0.11476 0.12065 0.11919 0.00967  -0.00553 0.01142  565 VAL A C   
969  O O   . VAL A 131 ? 0.12206 0.12783 0.12095 0.01227  -0.00826 0.01046  565 VAL A O   
970  C CB  . VAL A 131 ? 0.10906 0.11120 0.11786 0.01192  -0.00030 0.01606  565 VAL A CB  
971  C CG1 . VAL A 131 ? 0.17583 0.17713 0.17749 0.01658  -0.00275 0.01668  565 VAL A CG1 
972  C CG2 . VAL A 131 ? 0.11738 0.12315 0.13320 0.00811  -0.00233 0.01272  565 VAL A CG2 
973  N N   . ALA A 132 ? 0.09267 0.10113 0.10201 0.00567  -0.00642 0.00933  566 ALA A N   
974  C CA  . ALA A 132 ? 0.07642 0.08658 0.08488 0.00373  -0.00988 0.00662  566 ALA A CA  
975  C C   . ALA A 132 ? 0.07643 0.09039 0.09049 0.00043  -0.01107 0.00482  566 ALA A C   
976  O O   . ALA A 132 ? 0.06741 0.08318 0.08588 -0.00183 -0.00973 0.00469  566 ALA A O   
977  C CB  . ALA A 132 ? 0.07604 0.08510 0.08344 0.00281  -0.00949 0.00651  566 ALA A CB  
978  N N   . ILE A 133 ? 0.08810 0.10409 0.10205 0.00042  -0.01367 0.00306  567 ILE A N   
979  C CA  . ILE A 133 ? 0.06752 0.08798 0.08655 -0.00228 -0.01460 0.00123  567 ILE A CA  
980  C C   . ILE A 133 ? 0.07030 0.09207 0.08947 -0.00537 -0.01622 -0.00022 567 ILE A C   
981  O O   . ILE A 133 ? 0.11653 0.13920 0.13502 -0.00568 -0.01855 -0.00198 567 ILE A O   
982  C CB  . ILE A 133 ? 0.06899 0.09161 0.08881 -0.00020 -0.01612 0.00020  567 ILE A CB  
983  C CG1 . ILE A 133 ? 0.07228 0.09154 0.09082 0.00345  -0.01406 0.00265  567 ILE A CG1 
984  C CG2 . ILE A 133 ? 0.07768 0.10573 0.10322 -0.00272 -0.01664 -0.00192 567 ILE A CG2 
985  C CD1 . ILE A 133 ? 0.07705 0.09649 0.09281 0.00761  -0.01590 0.00265  567 ILE A CD1 
986  N N   . VAL A 134 ? 0.07166 0.09348 0.09196 -0.00758 -0.01495 0.00049  568 VAL A N   
987  C CA  . VAL A 134 ? 0.06525 0.08636 0.08478 -0.01006 -0.01573 0.00029  568 VAL A CA  
988  C C   . VAL A 134 ? 0.10568 0.13067 0.12828 -0.01272 -0.01471 0.00049  568 VAL A C   
989  O O   . VAL A 134 ? 0.08419 0.11193 0.10899 -0.01237 -0.01349 0.00047  568 VAL A O   
990  C CB  . VAL A 134 ? 0.13700 0.15313 0.15258 -0.00880 -0.01532 0.00158  568 VAL A CB  
991  C CG1 . VAL A 134 ? 0.07230 0.08506 0.08381 -0.00584 -0.01638 0.00102  568 VAL A CG1 
992  C CG2 . VAL A 134 ? 0.06585 0.08254 0.08235 -0.00786 -0.01322 0.00301  568 VAL A CG2 
993  N N   . ARG A 135 ? 0.09302 0.11818 0.11578 -0.01533 -0.01509 0.00057  569 ARG A N   
994  C CA  . ARG A 135 ? 0.09166 0.11978 0.11546 -0.01743 -0.01375 0.00163  569 ARG A CA  
995  C C   . ARG A 135 ? 0.08857 0.11257 0.11048 -0.01942 -0.01367 0.00317  569 ARG A C   
996  O O   . ARG A 135 ? 0.12583 0.14604 0.14740 -0.01994 -0.01497 0.00222  569 ARG A O   
997  C CB  . ARG A 135 ? 0.08715 0.12197 0.11502 -0.01894 -0.01334 0.00012  569 ARG A CB  
998  C CG  . ARG A 135 ? 0.14670 0.18302 0.17725 -0.02108 -0.01426 -0.00127 569 ARG A CG  
999  C CD  . ARG A 135 ? 0.07342 0.11749 0.10849 -0.02211 -0.01357 -0.00292 569 ARG A CD  
1000 N NE  . ARG A 135 ? 0.11156 0.15903 0.14664 -0.02407 -0.01124 -0.00138 569 ARG A NE  
1001 C CZ  . ARG A 135 ? 0.09236 0.14074 0.12860 -0.02734 -0.00978 -0.00006 569 ARG A CZ  
1002 N NH1 . ARG A 135 ? 0.06629 0.11239 0.10491 -0.02959 -0.01068 -0.00076 569 ARG A NH1 
1003 N NH2 . ARG A 135 ? 0.06515 0.11696 0.10029 -0.02834 -0.00724 0.00189  569 ARG A NH2 
1004 N N   . PRO A 136 ? 0.07059 0.09481 0.09100 -0.02022 -0.01219 0.00551  570 PRO A N   
1005 C CA  . PRO A 136 ? 0.06757 0.09644 0.08745 -0.01903 -0.01113 0.00619  570 PRO A CA  
1006 C C   . PRO A 136 ? 0.08724 0.11486 0.10584 -0.01598 -0.01168 0.00592  570 PRO A C   
1007 O O   . PRO A 136 ? 0.10458 0.12711 0.12161 -0.01469 -0.01237 0.00610  570 PRO A O   
1008 C CB  . PRO A 136 ? 0.07282 0.10046 0.08989 -0.02023 -0.00967 0.00938  570 PRO A CB  
1009 C CG  . PRO A 136 ? 0.11903 0.13842 0.13438 -0.02093 -0.01014 0.01071  570 PRO A CG  
1010 C CD  . PRO A 136 ? 0.07597 0.09499 0.09469 -0.02214 -0.01158 0.00768  570 PRO A CD  
1011 N N   . PRO A 137 ? 0.12154 0.15424 0.14124 -0.01470 -0.01134 0.00505  571 PRO A N   
1012 C CA  . PRO A 137 ? 0.06178 0.09417 0.08188 -0.01231 -0.01164 0.00445  571 PRO A CA  
1013 C C   . PRO A 137 ? 0.11462 0.14379 0.13091 -0.01063 -0.01190 0.00665  571 PRO A C   
1014 O O   . PRO A 137 ? 0.08657 0.11251 0.09949 -0.01133 -0.01174 0.00901  571 PRO A O   
1015 C CB  . PRO A 137 ? 0.09582 0.13519 0.11921 -0.01192 -0.01152 0.00206  571 PRO A CB  
1016 C CG  . PRO A 137 ? 0.11320 0.15634 0.13479 -0.01307 -0.01113 0.00269  571 PRO A CG  
1017 C CD  . PRO A 137 ? 0.11602 0.15556 0.13705 -0.01533 -0.01069 0.00408  571 PRO A CD  
1018 N N   . GLY A 138 ? 0.12794 0.15752 0.14509 -0.00834 -0.01213 0.00604  572 GLY A N   
1019 C CA  . GLY A 138 ? 0.15168 0.17890 0.16526 -0.00601 -0.01262 0.00798  572 GLY A CA  
1020 C C   . GLY A 138 ? 0.11961 0.15228 0.13500 -0.00339 -0.01324 0.00671  572 GLY A C   
1021 O O   . GLY A 138 ? 0.11207 0.14373 0.12394 -0.00098 -0.01396 0.00850  572 GLY A O   
1022 N N   . HIS A 139 ? 0.08179 0.12001 0.10286 -0.00376 -0.01305 0.00359  573 HIS A N   
1023 C CA  . HIS A 139 ? 0.12324 0.16740 0.14825 -0.00164 -0.01373 0.00131  573 HIS A CA  
1024 C C   . HIS A 139 ? 0.09582 0.14506 0.11784 0.00083  -0.01556 0.00137  573 HIS A C   
1025 O O   . HIS A 139 ? 0.10671 0.16008 0.13089 0.00341  -0.01662 -0.00004 573 HIS A O   
1026 C CB  . HIS A 139 ? 0.09481 0.14335 0.12761 -0.00333 -0.01290 -0.00234 573 HIS A CB  
1027 C CG  . HIS A 139 ? 0.09656 0.15025 0.13152 -0.00468 -0.01354 -0.00504 573 HIS A CG  
1028 N ND1 . HIS A 139 ? 0.05697 0.11623 0.09957 -0.00535 -0.01360 -0.00941 573 HIS A ND1 
1029 C CD2 . HIS A 139 ? 0.05882 0.11319 0.09009 -0.00547 -0.01393 -0.00444 573 HIS A CD2 
1030 C CE1 . HIS A 139 ? 0.05302 0.11600 0.09588 -0.00611 -0.01433 -0.01166 573 HIS A CE1 
1031 N NE2 . HIS A 139 ? 0.08885 0.14928 0.12476 -0.00614 -0.01436 -0.00853 573 HIS A NE2 
1032 N N   . HIS A 140 ? 0.08656 0.13612 0.10395 0.00030  -0.01576 0.00292  574 HIS A N   
1033 C CA  . HIS A 140 ? 0.09372 0.14801 0.10647 0.00330  -0.01721 0.00376  574 HIS A CA  
1034 C C   . HIS A 140 ? 0.10214 0.14964 0.10776 0.00565  -0.01715 0.00878  574 HIS A C   
1035 O O   . HIS A 140 ? 0.08602 0.13624 0.08675 0.00914  -0.01827 0.01045  574 HIS A O   
1036 C CB  . HIS A 140 ? 0.08640 0.14481 0.09718 0.00199  -0.01680 0.00333  574 HIS A CB  
1037 C CG  . HIS A 140 ? 0.12875 0.19403 0.14605 0.00050  -0.01720 -0.00203 574 HIS A CG  
1038 N ND1 . HIS A 140 ? 0.13430 0.20727 0.15665 0.00222  -0.01910 -0.00688 574 HIS A ND1 
1039 C CD2 . HIS A 140 ? 0.10098 0.16658 0.12102 -0.00239 -0.01604 -0.00363 574 HIS A CD2 
1040 C CE1 . HIS A 140 ? 0.10065 0.17739 0.12868 0.00016  -0.01892 -0.01124 574 HIS A CE1 
1041 N NE2 . HIS A 140 ? 0.12411 0.19640 0.15045 -0.00235 -0.01708 -0.00916 574 HIS A NE2 
1042 N N   . ALA A 141 ? 0.09673 0.13534 0.10147 0.00400  -0.01591 0.01107  575 ALA A N   
1043 C CA  . ALA A 141 ? 0.10270 0.13325 0.10125 0.00584  -0.01567 0.01557  575 ALA A CA  
1044 C C   . ALA A 141 ? 0.09322 0.12446 0.09141 0.01053  -0.01722 0.01536  575 ALA A C   
1045 O O   . ALA A 141 ? 0.08681 0.11975 0.09002 0.01070  -0.01740 0.01250  575 ALA A O   
1046 C CB  . ALA A 141 ? 0.13926 0.16062 0.13750 0.00282  -0.01434 0.01701  575 ALA A CB  
1047 N N   . GLU A 142 ? 0.09939 0.12944 0.09165 0.01437  -0.01801 0.01863  576 GLU A N   
1048 C CA  . GLU A 142 ? 0.16540 0.19605 0.15684 0.01962  -0.01972 0.01870  576 GLU A CA  
1049 C C   . GLU A 142 ? 0.19472 0.21349 0.18286 0.02047  -0.01887 0.02185  576 GLU A C   
1050 O O   . GLU A 142 ? 0.19653 0.20695 0.18307 0.01684  -0.01716 0.02385  576 GLU A O   
1051 C CB  . GLU A 142 ? 0.14470 0.18079 0.13094 0.02456  -0.02150 0.02043  576 GLU A CB  
1052 C CG  . GLU A 142 ? 0.16750 0.21544 0.15613 0.02408  -0.02267 0.01677  576 GLU A CG  
1053 C CD  . GLU A 142 ? 0.17059 0.22935 0.16649 0.02635  -0.02521 0.01092  576 GLU A CD  
1054 O OE1 . GLU A 142 ? 0.12973 0.18714 0.13019 0.02705  -0.02529 0.00952  576 GLU A OE1 
1055 O OE2 . GLU A 142 ? 0.22893 0.29797 0.22641 0.02740  -0.02702 0.00737  576 GLU A OE2 
1056 N N   . LYS A 143 ? 0.21388 0.23229 0.20153 0.02548  -0.02024 0.02178  577 LYS A N   
1057 C CA  . LYS A 143 ? 0.17350 0.18044 0.15782 0.02718  -0.01969 0.02429  577 LYS A CA  
1058 C C   . LYS A 143 ? 0.21650 0.21361 0.19369 0.02713  -0.01864 0.02991  577 LYS A C   
1059 O O   . LYS A 143 ? 0.20208 0.18782 0.17757 0.02589  -0.01753 0.03166  577 LYS A O   
1060 C CB  . LYS A 143 ? 0.12309 0.13257 0.10798 0.03352  -0.02146 0.02324  577 LYS A CB  
1061 N N   . ASP A 144 ? 0.22289 0.12894 0.22446 -0.00505 -0.03479 0.03597  578 ASP A N   
1062 C CA  . ASP A 144 ? 0.21443 0.11075 0.21163 -0.01033 -0.03861 0.04357  578 ASP A CA  
1063 C C   . ASP A 144 ? 0.26018 0.16677 0.24957 -0.01806 -0.03848 0.04853  578 ASP A C   
1064 O O   . ASP A 144 ? 0.28000 0.18204 0.26534 -0.02281 -0.04205 0.05650  578 ASP A O   
1065 C CB  . ASP A 144 ? 0.22615 0.11471 0.22773 -0.00582 -0.04397 0.05010  578 ASP A CB  
1066 C CG  . ASP A 144 ? 0.35936 0.26135 0.36144 -0.00394 -0.04588 0.05430  578 ASP A CG  
1067 O OD1 . ASP A 144 ? 0.37358 0.28948 0.37492 -0.00375 -0.04250 0.04989  578 ASP A OD1 
1068 O OD2 . ASP A 144 ? 0.50249 0.40078 0.50564 -0.00281 -0.05107 0.06217  578 ASP A OD2 
1069 N N   . THR A 145 ? 0.18743 0.10743 0.17481 -0.01942 -0.03433 0.04392  579 THR A N   
1070 C CA  . THR A 145 ? 0.31081 0.24201 0.29152 -0.02590 -0.03374 0.04786  579 THR A CA  
1071 C C   . THR A 145 ? 0.24761 0.18982 0.22670 -0.02778 -0.02884 0.04194  579 THR A C   
1072 O O   . THR A 145 ? 0.23436 0.17947 0.21749 -0.02302 -0.02614 0.03534  579 THR A O   
1073 C CB  . THR A 145 ? 0.28002 0.22031 0.25958 -0.02467 -0.03602 0.05242  579 THR A CB  
1074 O OG1 . THR A 145 ? 0.45341 0.40315 0.42587 -0.03156 -0.03533 0.05619  579 THR A OG1 
1075 C CG2 . THR A 145 ? 0.32071 0.27114 0.30400 -0.01922 -0.03369 0.04660  579 THR A CG2 
1076 N N   . ALA A 146 ? 0.20859 0.15632 0.18241 -0.03460 -0.02786 0.04450  580 ALA A N   
1077 C CA  . ALA A 146 ? 0.20316 0.16349 0.17587 -0.03608 -0.02360 0.03999  580 ALA A CA  
1078 C C   . ALA A 146 ? 0.15532 0.12903 0.12562 -0.03594 -0.02281 0.04122  580 ALA A C   
1079 O O   . ALA A 146 ? 0.16207 0.13699 0.12895 -0.03819 -0.02549 0.04711  580 ALA A O   
1080 C CB  . ALA A 146 ? 0.16493 0.12616 0.13420 -0.04338 -0.02259 0.04142  580 ALA A CB  
1081 N N   . CYS A 147 ? 0.14392 0.12732 0.11579 -0.03338 -0.01925 0.03556  581 CYS A N   
1082 C CA  . CYS A 147 ? 0.14345 0.13811 0.11354 -0.03230 -0.01828 0.03496  581 CYS A CA  
1083 C C   . CYS A 147 ? 0.15841 0.16234 0.13008 -0.03076 -0.01403 0.02893  581 CYS A C   
1084 O O   . CYS A 147 ? 0.12681 0.12772 0.10222 -0.02839 -0.01246 0.02488  581 CYS A O   
1085 C CB  . CYS A 147 ? 0.13843 0.13045 0.11118 -0.02719 -0.02059 0.03466  581 CYS A CB  
1086 S SG  . CYS A 147 ? 0.23104 0.23586 0.20193 -0.02562 -0.01935 0.03192  581 CYS A SG  
1087 N N   . GLY A 148 ? 0.15487 0.17015 0.12356 -0.03208 -0.01225 0.02839  582 GLY A N   
1088 C CA  . GLY A 148 ? 0.14368 0.16745 0.11441 -0.02954 -0.00852 0.02265  582 GLY A CA  
1089 C C   . GLY A 148 ? 0.11385 0.13794 0.08777 -0.02963 -0.00632 0.02025  582 GLY A C   
1090 O O   . GLY A 148 ? 0.11100 0.13394 0.08894 -0.02555 -0.00498 0.01594  582 GLY A O   
1091 N N   . PHE A 149 ? 0.13777 0.16382 0.10978 -0.03481 -0.00623 0.02346  583 PHE A N   
1092 C CA  . PHE A 149 ? 0.12646 0.15466 0.10088 -0.03641 -0.00466 0.02213  583 PHE A CA  
1093 C C   . PHE A 149 ? 0.11594 0.13244 0.09261 -0.03534 -0.00620 0.02109  583 PHE A C   
1094 O O   . PHE A 149 ? 0.15178 0.16927 0.12991 -0.03712 -0.00542 0.01996  583 PHE A O   
1095 C CB  . PHE A 149 ? 0.14251 0.18078 0.12049 -0.03286 -0.00136 0.01746  583 PHE A CB  
1096 C CG  . PHE A 149 ? 0.10656 0.15569 0.08310 -0.03195 0.00079  0.01617  583 PHE A CG  
1097 C CD1 . PHE A 149 ? 0.11296 0.16661 0.08443 -0.03621 0.00034  0.01975  583 PHE A CD1 
1098 C CD2 . PHE A 149 ? 0.16653 0.22122 0.14657 -0.02695 0.00330  0.01121  583 PHE A CD2 
1099 C CE1 . PHE A 149 ? 0.12164 0.18605 0.09116 -0.03550 0.00271  0.01762  583 PHE A CE1 
1100 C CE2 . PHE A 149 ? 0.10132 0.16529 0.08004 -0.02580 0.00557  0.00883  583 PHE A CE2 
1101 C CZ  . PHE A 149 ? 0.10746 0.17683 0.08070 -0.03010 0.00548  0.01164  583 PHE A CZ  
1102 N N   . CYS A 150 ? 0.19023 0.19663 0.16735 -0.03250 -0.00831 0.02121  584 CYS A N   
1103 C CA  . CYS A 150 ? 0.13051 0.12647 0.11003 -0.03059 -0.00920 0.01908  584 CYS A CA  
1104 C C   . CYS A 150 ? 0.23030 0.21513 0.20778 -0.03398 -0.01213 0.02286  584 CYS A C   
1105 O O   . CYS A 150 ? 0.16636 0.14886 0.14162 -0.03525 -0.01437 0.02737  584 CYS A O   
1106 C CB  . CYS A 150 ? 0.11468 0.10768 0.09741 -0.02445 -0.00922 0.01601  584 CYS A CB  
1107 S SG  . CYS A 150 ? 0.10424 0.10758 0.08928 -0.02056 -0.00638 0.01194  584 CYS A SG  
1108 N N   . PHE A 151 ? 0.16235 0.13991 0.14037 -0.03557 -0.01229 0.02103  585 PHE A N   
1109 C CA  . PHE A 151 ? 0.17677 0.14157 0.15315 -0.03881 -0.01503 0.02371  585 PHE A CA  
1110 C C   . PHE A 151 ? 0.18773 0.14080 0.16720 -0.03380 -0.01582 0.02023  585 PHE A C   
1111 O O   . PHE A 151 ? 0.16813 0.11251 0.14852 -0.03166 -0.01838 0.02283  585 PHE A O   
1112 C CB  . PHE A 151 ? 0.16456 0.12953 0.13858 -0.04567 -0.01478 0.02402  585 PHE A CB  
1113 C CG  . PHE A 151 ? 0.16994 0.14463 0.14099 -0.05173 -0.01469 0.02891  585 PHE A CG  
1114 C CD1 . PHE A 151 ? 0.19548 0.18581 0.16742 -0.05163 -0.01189 0.02769  585 PHE A CD1 
1115 C CD2 . PHE A 151 ? 0.16304 0.13150 0.13066 -0.05741 -0.01735 0.03487  585 PHE A CD2 
1116 C CE1 . PHE A 151 ? 0.14808 0.14903 0.11777 -0.05692 -0.01127 0.03166  585 PHE A CE1 
1117 C CE2 . PHE A 151 ? 0.17285 0.15178 0.13750 -0.06358 -0.01693 0.03954  585 PHE A CE2 
1118 C CZ  . PHE A 151 ? 0.15440 0.15034 0.12020 -0.06322 -0.01364 0.03760  585 PHE A CZ  
1119 N N   . PHE A 152 ? 0.16418 0.11750 0.14544 -0.03183 -0.01371 0.01453  586 PHE A N   
1120 C CA  . PHE A 152 ? 0.14581 0.09138 0.13040 -0.02650 -0.01343 0.01014  586 PHE A CA  
1121 C C   . PHE A 152 ? 0.21780 0.17284 0.20526 -0.02183 -0.01086 0.00656  586 PHE A C   
1122 O O   . PHE A 152 ? 0.13736 0.10227 0.12394 -0.02330 -0.00908 0.00599  586 PHE A O   
1123 C CB  . PHE A 152 ? 0.16980 0.10664 0.15314 -0.02900 -0.01311 0.00611  586 PHE A CB  
1124 C CG  . PHE A 152 ? 0.16637 0.09346 0.14645 -0.03496 -0.01568 0.00953  586 PHE A CG  
1125 C CD1 . PHE A 152 ? 0.17932 0.09502 0.16019 -0.03379 -0.01868 0.01330  586 PHE A CD1 
1126 C CD2 . PHE A 152 ? 0.16873 0.09824 0.14520 -0.04203 -0.01542 0.00949  586 PHE A CD2 
1127 C CE1 . PHE A 152 ? 0.19015 0.09564 0.16787 -0.03982 -0.02134 0.01710  586 PHE A CE1 
1128 C CE2 . PHE A 152 ? 0.22172 0.14210 0.19509 -0.04847 -0.01791 0.01286  586 PHE A CE2 
1129 C CZ  . PHE A 152 ? 0.19256 0.10022 0.16634 -0.04752 -0.02086 0.01676  586 PHE A CZ  
1130 N N   . ASN A 153 ? 0.19387 0.14602 0.18522 -0.01620 -0.01083 0.00448  587 ASN A N   
1131 C CA  . ASN A 153 ? 0.14583 0.10637 0.14009 -0.01223 -0.00874 0.00177  587 ASN A CA  
1132 C C   . ASN A 153 ? 0.23679 0.19819 0.23116 -0.01218 -0.00619 -0.00338 587 ASN A C   
1133 O O   . ASN A 153 ? 0.23257 0.18905 0.22913 -0.00941 -0.00540 -0.00714 587 ASN A O   
1134 C CB  . ASN A 153 ? 0.12314 0.08213 0.12183 -0.00698 -0.00987 0.00205  587 ASN A CB  
1135 C CG  . ASN A 153 ? 0.12616 0.09462 0.12725 -0.00432 -0.00838 0.00070  587 ASN A CG  
1136 O OD1 . ASN A 153 ? 0.10749 0.08082 0.10850 -0.00459 -0.00592 -0.00227 587 ASN A OD1 
1137 N ND2 . ASN A 153 ? 0.12267 0.09362 0.12570 -0.00215 -0.01017 0.00318  587 ASN A ND2 
1138 N N   . THR A 154 ? 0.27249 0.24120 0.26457 -0.01521 -0.00487 -0.00349 588 THR A N   
1139 C CA  . THR A 154 ? 0.20073 0.17116 0.19165 -0.01650 -0.00302 -0.00732 588 THR A CA  
1140 C C   . THR A 154 ? 0.11074 0.08375 0.10463 -0.01232 -0.00107 -0.01073 588 THR A C   
1141 O O   . THR A 154 ? 0.11431 0.08508 0.10762 -0.01228 0.00033  -0.01481 588 THR A O   
1142 C CB  . THR A 154 ? 0.13874 0.11807 0.12774 -0.01986 -0.00254 -0.00562 588 THR A CB  
1143 O OG1 . THR A 154 ? 0.17201 0.15006 0.15841 -0.02453 -0.00408 -0.00273 588 THR A OG1 
1144 C CG2 . THR A 154 ? 0.10908 0.09160 0.09670 -0.02131 -0.00113 -0.00874 588 THR A CG2 
1145 N N   . ALA A 155 ? 0.10404 0.08214 0.10085 -0.00926 -0.00087 -0.00933 589 ALA A N   
1146 C CA  . ALA A 155 ? 0.17715 0.15856 0.17700 -0.00609 0.00091  -0.01198 589 ALA A CA  
1147 C C   . ALA A 155 ? 0.16651 0.14246 0.16957 -0.00272 0.00104  -0.01461 589 ALA A C   
1148 O O   . ALA A 155 ? 0.10668 0.08379 0.11092 -0.00146 0.00319  -0.01850 589 ALA A O   
1149 C CB  . ALA A 155 ? 0.17450 0.16192 0.17662 -0.00437 0.00076  -0.00990 589 ALA A CB  
1150 N N   . ALA A 156 ? 0.14032 0.11089 0.14502 -0.00112 -0.00124 -0.01239 590 ALA A N   
1151 C CA  . ALA A 156 ? 0.14835 0.11356 0.15735 0.00300  -0.00153 -0.01447 590 ALA A CA  
1152 C C   . ALA A 156 ? 0.13031 0.08798 0.13764 0.00229  -0.00038 -0.01882 590 ALA A C   
1153 O O   . ALA A 156 ? 0.14519 0.10192 0.15586 0.00572  0.00146  -0.02335 590 ALA A O   
1154 C CB  . ALA A 156 ? 0.11970 0.08035 0.13042 0.00451  -0.00496 -0.01003 590 ALA A CB  
1155 N N   . LEU A 157 ? 0.12904 0.08185 0.13127 -0.00237 -0.00133 -0.01789 591 LEU A N   
1156 C CA  . LEU A 157 ? 0.13873 0.08379 0.13842 -0.00410 -0.00044 -0.02251 591 LEU A CA  
1157 C C   . LEU A 157 ? 0.13612 0.08763 0.13412 -0.00487 0.00293  -0.02768 591 LEU A C   
1158 O O   . LEU A 157 ? 0.14377 0.09098 0.14171 -0.00371 0.00475  -0.03347 591 LEU A O   
1159 C CB  . LEU A 157 ? 0.19315 0.13323 0.18756 -0.01014 -0.00243 -0.01988 591 LEU A CB  
1160 C CG  . LEU A 157 ? 0.19856 0.13012 0.19355 -0.01047 -0.00584 -0.01489 591 LEU A CG  
1161 C CD1 . LEU A 157 ? 0.15056 0.08341 0.14064 -0.01719 -0.00740 -0.01059 591 LEU A CD1 
1162 C CD2 . LEU A 157 ? 0.16433 0.08182 0.16083 -0.00845 -0.00672 -0.01800 591 LEU A CD2 
1163 N N   . THR A 158 ? 0.18042 0.14216 0.17688 -0.00684 0.00380  -0.02569 592 THR A N   
1164 C CA  . THR A 158 ? 0.18830 0.15677 0.18255 -0.00823 0.00656  -0.02934 592 THR A CA  
1165 C C   . THR A 158 ? 0.12407 0.09615 0.12278 -0.00366 0.00910  -0.03279 592 THR A C   
1166 O O   . THR A 158 ? 0.12761 0.10190 0.12464 -0.00412 0.01181  -0.03784 592 THR A O   
1167 C CB  . THR A 158 ? 0.11578 0.09339 0.10804 -0.01105 0.00627  -0.02536 592 THR A CB  
1168 O OG1 . THR A 158 ? 0.12660 0.10267 0.11527 -0.01537 0.00430  -0.02276 592 THR A OG1 
1169 C CG2 . THR A 158 ? 0.11469 0.09949 0.10449 -0.01273 0.00860  -0.02785 592 THR A CG2 
1170 N N   . ALA A 159 ? 0.12975 0.10368 0.13403 0.00035  0.00833  -0.03022 593 ALA A N   
1171 C CA  . ALA A 159 ? 0.15305 0.13122 0.16274 0.00470  0.01056  -0.03334 593 ALA A CA  
1172 C C   . ALA A 159 ? 0.12923 0.10030 0.14084 0.00777  0.01181  -0.03905 593 ALA A C   
1173 O O   . ALA A 159 ? 0.13465 0.10977 0.14699 0.00895  0.01522  -0.04451 593 ALA A O   
1174 C CB  . ALA A 159 ? 0.11278 0.09383 0.12824 0.00802  0.00873  -0.02932 593 ALA A CB  
1175 N N   . ARG A 160 ? 0.13622 0.09640 0.14842 0.00890  0.00914  -0.03796 594 ARG A N   
1176 C CA  . ARG A 160 ? 0.14841 0.09935 0.16292 0.01233  0.00991  -0.04340 594 ARG A CA  
1177 C C   . ARG A 160 ? 0.15612 0.10383 0.16414 0.00840  0.01223  -0.04952 594 ARG A C   
1178 O O   . ARG A 160 ? 0.16385 0.11043 0.17333 0.01114  0.01527  -0.05668 594 ARG A O   
1179 C CB  . ARG A 160 ? 0.15533 0.09418 0.17150 0.01371  0.00585  -0.03954 594 ARG A CB  
1180 C CG  . ARG A 160 ? 0.23321 0.17507 0.25588 0.01799  0.00329  -0.03404 594 ARG A CG  
1181 C CD  . ARG A 160 ? 0.14964 0.09801 0.18049 0.02446  0.00555  -0.03773 594 ARG A CD  
1182 N NE  . ARG A 160 ? 0.24039 0.18930 0.27825 0.02912  0.00230  -0.03287 594 ARG A NE  
1183 C CZ  . ARG A 160 ? 0.15804 0.11586 0.20396 0.03422  0.00324  -0.03380 594 ARG A CZ  
1184 N NH1 . ARG A 160 ? 0.16062 0.12789 0.20859 0.03516  0.00767  -0.03925 594 ARG A NH1 
1185 N NH2 . ARG A 160 ? 0.27753 0.23582 0.32946 0.03798  -0.00046 -0.02880 594 ARG A NH2 
1186 N N   . TYR A 161 ? 0.18182 0.12866 0.18276 0.00194  0.01085  -0.04713 595 TYR A N   
1187 C CA  . TYR A 161 ? 0.20808 0.15370 0.20218 -0.00280 0.01265  -0.05258 595 TYR A CA  
1188 C C   . TYR A 161 ? 0.18303 0.14005 0.17622 -0.00255 0.01677  -0.05708 595 TYR A C   
1189 O O   . TYR A 161 ? 0.20191 0.15745 0.19244 -0.00289 0.01959  -0.06460 595 TYR A O   
1190 C CB  . TYR A 161 ? 0.17481 0.12167 0.16251 -0.00986 0.01031  -0.04816 595 TYR A CB  
1191 C CG  . TYR A 161 ? 0.16392 0.11374 0.14442 -0.01532 0.01199  -0.05301 595 TYR A CG  
1192 C CD1 . TYR A 161 ? 0.17768 0.11713 0.15399 -0.01830 0.01177  -0.05849 595 TYR A CD1 
1193 C CD2 . TYR A 161 ? 0.15631 0.11900 0.13399 -0.01774 0.01357  -0.05209 595 TYR A CD2 
1194 C CE1 . TYR A 161 ? 0.18333 0.12619 0.15240 -0.02385 0.01313  -0.06334 595 TYR A CE1 
1195 C CE2 . TYR A 161 ? 0.16517 0.13160 0.13582 -0.02302 0.01474  -0.05608 595 TYR A CE2 
1196 C CZ  . TYR A 161 ? 0.17509 0.13211 0.14126 -0.02618 0.01455  -0.06192 595 TYR A CZ  
1197 O OH  . TYR A 161 ? 0.18434 0.14589 0.14285 -0.03203 0.01550  -0.06615 595 TYR A OH  
1198 N N   . ALA A 162 ? 0.14706 0.11544 0.14197 -0.00241 0.01718  -0.05258 596 ALA A N   
1199 C CA  . ALA A 162 ? 0.14446 0.12426 0.13833 -0.00297 0.02084  -0.05547 596 ALA A CA  
1200 C C   . ALA A 162 ? 0.21871 0.19908 0.21753 0.00231  0.02437  -0.06236 596 ALA A C   
1201 O O   . ALA A 162 ? 0.19207 0.17734 0.18750 0.00096  0.02804  -0.06856 596 ALA A O   
1202 C CB  . ALA A 162 ? 0.13197 0.12151 0.12823 -0.00316 0.02019  -0.04893 596 ALA A CB  
1203 N N   . GLN A 163 ? 0.17525 0.15137 0.18219 0.00842  0.02332  -0.06146 597 GLN A N   
1204 C CA  . GLN A 163 ? 0.15740 0.13464 0.17079 0.01451  0.02653  -0.06793 597 GLN A CA  
1205 C C   . GLN A 163 ? 0.17253 0.13860 0.18343 0.01542  0.02782  -0.07594 597 GLN A C   
1206 O O   . GLN A 163 ? 0.17990 0.14935 0.19247 0.01831  0.03211  -0.08392 597 GLN A O   
1207 C CB  . GLN A 163 ? 0.15382 0.12992 0.17708 0.02088  0.02428  -0.06404 597 GLN A CB  
1208 C CG  . GLN A 163 ? 0.18739 0.17365 0.21303 0.01973  0.02284  -0.05684 597 GLN A CG  
1209 C CD  . GLN A 163 ? 0.14415 0.12978 0.17875 0.02525  0.02006  -0.05290 597 GLN A CD  
1210 O OE1 . GLN A 163 ? 0.16037 0.13519 0.19710 0.02807  0.01696  -0.05146 597 GLN A OE1 
1211 N NE2 . GLN A 163 ? 0.12961 0.12707 0.16936 0.02636  0.02090  -0.05083 597 GLN A NE2 
1212 N N   . SER A 164 ? 0.17825 0.13119 0.18505 0.01267  0.02434  -0.07430 598 SER A N   
1213 C CA  . SER A 164 ? 0.19431 0.13466 0.19817 0.01267  0.02514  -0.08198 598 SER A CA  
1214 C C   . SER A 164 ? 0.20785 0.15401 0.20334 0.00761  0.02899  -0.08930 598 SER A C   
1215 O O   . SER A 164 ? 0.24108 0.18192 0.23577 0.00950  0.03197  -0.09874 598 SER A O   
1216 C CB  . SER A 164 ? 0.23200 0.15805 0.23240 0.00904  0.02034  -0.07767 598 SER A CB  
1217 O OG  . SER A 164 ? 0.19545 0.12492 0.18688 0.00061  0.01923  -0.07517 598 SER A OG  
1218 N N   . ILE A 165 ? 0.21892 0.17606 0.20812 0.00130  0.02891  -0.08521 599 ILE A N   
1219 C CA  . ILE A 165 ? 0.21716 0.18137 0.19758 -0.00435 0.03193  -0.09082 599 ILE A CA  
1220 C C   . ILE A 165 ? 0.19067 0.17082 0.17242 -0.00303 0.03644  -0.09277 599 ILE A C   
1221 O O   . ILE A 165 ? 0.23463 0.22320 0.20867 -0.00813 0.03900  -0.09632 599 ILE A O   
1222 C CB  . ILE A 165 ? 0.21505 0.18182 0.18727 -0.01263 0.02873  -0.08505 599 ILE A CB  
1223 C CG1 . ILE A 165 ? 0.25066 0.22814 0.22545 -0.01303 0.02711  -0.07539 599 ILE A CG1 
1224 C CG2 . ILE A 165 ? 0.19617 0.14848 0.16672 -0.01505 0.02455  -0.08331 599 ILE A CG2 
1225 C CD1 . ILE A 165 ? 0.16935 0.15326 0.13689 -0.02030 0.02493  -0.07038 599 ILE A CD1 
1226 N N   . THR A 166 ? 0.22391 0.20930 0.21494 0.00302  0.03731  -0.09013 600 THR A N   
1227 C CA  . THR A 166 ? 0.25335 0.25410 0.24653 0.00416  0.04190  -0.09239 600 THR A CA  
1228 C C   . THR A 166 ? 0.19174 0.19231 0.19500 0.01270  0.04494  -0.09832 600 THR A C   
1229 O O   . THR A 166 ? 0.19832 0.19783 0.20035 0.01452  0.04753  -0.10474 600 THR A O   
1230 C CB  . THR A 166 ? 0.17936 0.19056 0.17421 0.00201  0.04020  -0.08272 600 THR A CB  
1231 O OG1 . THR A 166 ? 0.15727 0.16234 0.15956 0.00607  0.03630  -0.07639 600 THR A OG1 
1232 C CG2 . THR A 166 ? 0.16114 0.17484 0.14642 -0.00591 0.03796  -0.07775 600 THR A CG2 
1233 N N   . ARG A 167 ? 0.18076 0.18237 0.19368 0.01781  0.04289  -0.09268 601 ARG A N   
1234 C CA  . ARG A 167 ? 0.21015 0.21184 0.23407 0.02648  0.04468  -0.09675 601 ARG A CA  
1235 C C   . ARG A 167 ? 0.22216 0.21960 0.25441 0.03056  0.03992  -0.08879 601 ARG A C   
1236 O O   . ARG A 167 ? 0.19876 0.19752 0.22847 0.02648  0.03640  -0.08034 601 ARG A O   
1237 C CB  . ARG A 167 ? 0.22869 0.24766 0.25563 0.02743  0.04929  -0.09853 601 ARG A CB  
1238 C CG  . ARG A 167 ? 0.21531 0.24849 0.24309 0.02357  0.04982  -0.09286 601 ARG A CG  
1239 C CD  . ARG A 167 ? 0.21196 0.26182 0.24311 0.02390  0.05409  -0.09407 601 ARG A CD  
1240 N NE  . ARG A 167 ? 0.23391 0.29474 0.27168 0.02359  0.05350  -0.08802 601 ARG A NE  
1241 C CZ  . ARG A 167 ? 0.14444 0.21147 0.17657 0.01656  0.05243  -0.08141 601 ARG A CZ  
1242 N NH1 . ARG A 167 ? 0.20233 0.26841 0.22307 0.00979  0.05271  -0.08102 601 ARG A NH1 
1243 N NH2 . ARG A 167 ? 0.13489 0.20887 0.17297 0.01622  0.05061  -0.07469 601 ARG A NH2 
1244 N N   . GLU A 168 ? 0.23843 0.23084 0.28061 0.03882  0.03968  -0.09151 602 GLU A N   
1245 C CA  . GLU A 168 ? 0.30052 0.28815 0.35023 0.04280  0.03456  -0.08382 602 GLU A CA  
1246 C C   . GLU A 168 ? 0.22253 0.22467 0.27579 0.04124  0.03381  -0.07687 602 GLU A C   
1247 O O   . GLU A 168 ? 0.20534 0.20460 0.25875 0.03978  0.02911  -0.06880 602 GLU A O   
1248 C CB  . GLU A 168 ? 0.37117 0.35323 0.43076 0.05192  0.03427  -0.08666 602 GLU A CB  
1249 C CG  . GLU A 168 ? 0.41407 0.38815 0.48128 0.05641  0.02851  -0.07985 602 GLU A CG  
1250 C CD  . GLU A 168 ? 0.55170 0.50766 0.61918 0.06043  0.02578  -0.08038 602 GLU A CD  
1251 O OE1 . GLU A 168 ? 0.50996 0.45995 0.57264 0.06049  0.02873  -0.08689 602 GLU A OE1 
1252 O OE2 . GLU A 168 ? 0.54001 0.48762 0.61206 0.06319  0.02055  -0.07401 602 GLU A OE2 
1253 N N   . SER A 169 ? 0.19891 0.21676 0.25450 0.04089  0.03846  -0.08003 603 SER A N   
1254 C CA  . SER A 169 ? 0.14440 0.17614 0.20468 0.03961  0.03802  -0.07425 603 SER A CA  
1255 C C   . SER A 169 ? 0.13578 0.17252 0.18682 0.03091  0.03777  -0.06937 603 SER A C   
1256 O O   . SER A 169 ? 0.15718 0.20601 0.21093 0.02869  0.03840  -0.06578 603 SER A O   
1257 C CB  . SER A 169 ? 0.14615 0.19345 0.21516 0.04369  0.04310  -0.07960 603 SER A CB  
1258 O OG  . SER A 169 ? 0.20255 0.25769 0.26439 0.03903  0.04831  -0.08463 603 SER A OG  
1259 N N   . LEU A 170 ? 0.13771 0.16562 0.17843 0.02590  0.03668  -0.06896 604 LEU A N   
1260 C CA  . LEU A 170 ? 0.13000 0.16196 0.16305 0.01852  0.03571  -0.06347 604 LEU A CA  
1261 C C   . LEU A 170 ? 0.14025 0.17266 0.17696 0.01827  0.03153  -0.05540 604 LEU A C   
1262 O O   . LEU A 170 ? 0.20172 0.22531 0.24115 0.02119  0.02769  -0.05262 604 LEU A O   
1263 C CB  . LEU A 170 ? 0.13371 0.15576 0.15658 0.01396  0.03421  -0.06361 604 LEU A CB  
1264 C CG  . LEU A 170 ? 0.15346 0.18048 0.16861 0.00681  0.03347  -0.05849 604 LEU A CG  
1265 C CD1 . LEU A 170 ? 0.14395 0.18246 0.15488 0.00319  0.03806  -0.06209 604 LEU A CD1 
1266 C CD2 . LEU A 170 ? 0.12877 0.14591 0.13644 0.00316  0.03029  -0.05631 604 LEU A CD2 
1267 N N   . ARG A 171 ? 0.11326 0.15594 0.14986 0.01451  0.03226  -0.05173 605 ARG A N   
1268 C CA  . ARG A 171 ? 0.10501 0.14872 0.14474 0.01374  0.02869  -0.04505 605 ARG A CA  
1269 C C   . ARG A 171 ? 0.15525 0.19191 0.18714 0.00913  0.02567  -0.04012 605 ARG A C   
1270 O O   . ARG A 171 ? 0.13287 0.17226 0.15842 0.00430  0.02694  -0.03921 605 ARG A O   
1271 C CB  . ARG A 171 ? 0.10102 0.15826 0.14487 0.01161  0.03079  -0.04364 605 ARG A CB  
1272 C CG  . ARG A 171 ? 0.10380 0.17069 0.15716 0.01643  0.03373  -0.04807 605 ARG A CG  
1273 C CD  . ARG A 171 ? 0.16895 0.24979 0.22698 0.01342  0.03513  -0.04559 605 ARG A CD  
1274 N NE  . ARG A 171 ? 0.19261 0.27917 0.24353 0.00669  0.03789  -0.04463 605 ARG A NE  
1275 C CZ  . ARG A 171 ? 0.14824 0.24452 0.19804 0.00542  0.04298  -0.04915 605 ARG A CZ  
1276 N NH1 . ARG A 171 ? 0.12518 0.22684 0.18115 0.01092  0.04642  -0.05588 605 ARG A NH1 
1277 N NH2 . ARG A 171 ? 0.15742 0.25835 0.19977 -0.00143 0.04466  -0.04684 605 ARG A NH2 
1278 N N   . VAL A 172 ? 0.12768 0.15611 0.16016 0.01067  0.02167  -0.03679 606 VAL A N   
1279 C CA  . VAL A 172 ? 0.12958 0.15169 0.15562 0.00719  0.01897  -0.03270 606 VAL A CA  
1280 C C   . VAL A 172 ? 0.16919 0.19172 0.19784 0.00707  0.01589  -0.02773 606 VAL A C   
1281 O O   . VAL A 172 ? 0.14529 0.16645 0.17893 0.01045  0.01387  -0.02699 606 VAL A O   
1282 C CB  . VAL A 172 ? 0.18678 0.19831 0.20943 0.00813  0.01735  -0.03389 606 VAL A CB  
1283 C CG1 . VAL A 172 ? 0.12004 0.12732 0.13720 0.00462  0.01468  -0.02944 606 VAL A CG1 
1284 C CG2 . VAL A 172 ? 0.15041 0.16081 0.16954 0.00752  0.02037  -0.03965 606 VAL A CG2 
1285 N N   . LEU A 173 ? 0.20923 0.23348 0.23440 0.00321  0.01536  -0.02439 607 LEU A N   
1286 C CA  . LEU A 173 ? 0.10626 0.12978 0.13261 0.00258  0.01262  -0.02049 607 LEU A CA  
1287 C C   . LEU A 173 ? 0.14675 0.16330 0.16817 0.00165  0.01039  -0.01824 607 LEU A C   
1288 O O   . LEU A 173 ? 0.16688 0.18246 0.18358 -0.00084 0.01096  -0.01756 607 LEU A O   
1289 C CB  . LEU A 173 ? 0.09720 0.12626 0.12366 -0.00082 0.01347  -0.01846 607 LEU A CB  
1290 C CG  . LEU A 173 ? 0.11467 0.14109 0.14064 -0.00221 0.01086  -0.01505 607 LEU A CG  
1291 C CD1 . LEU A 173 ? 0.11834 0.14597 0.14923 -0.00026 0.00888  -0.01502 607 LEU A CD1 
1292 C CD2 . LEU A 173 ? 0.07893 0.10808 0.10385 -0.00604 0.01159  -0.01276 607 LEU A CD2 
1293 N N   . ILE A 174 ? 0.14296 0.15589 0.16560 0.00345  0.00782  -0.01686 608 ILE A N   
1294 C CA  . ILE A 174 ? 0.07956 0.08775 0.09812 0.00240  0.00590  -0.01460 608 ILE A CA  
1295 C C   . ILE A 174 ? 0.07626 0.08616 0.09550 0.00163  0.00447  -0.01248 608 ILE A C   
1296 O O   . ILE A 174 ? 0.07590 0.08705 0.09815 0.00291  0.00294  -0.01213 608 ILE A O   
1297 C CB  . ILE A 174 ? 0.08290 0.08573 0.10124 0.00422  0.00409  -0.01438 608 ILE A CB  
1298 C CG1 . ILE A 174 ? 0.08807 0.08743 0.10571 0.00493  0.00550  -0.01728 608 ILE A CG1 
1299 C CG2 . ILE A 174 ? 0.08809 0.08804 0.10225 0.00246  0.00243  -0.01181 608 ILE A CG2 
1300 C CD1 . ILE A 174 ? 0.09333 0.08538 0.11049 0.00622  0.00347  -0.01665 608 ILE A CD1 
1301 N N   . VAL A 175 ? 0.07478 0.08478 0.09141 -0.00038 0.00481  -0.01122 609 VAL A N   
1302 C CA  . VAL A 175 ? 0.07829 0.08828 0.09513 -0.00095 0.00362  -0.00998 609 VAL A CA  
1303 C C   . VAL A 175 ? 0.07336 0.08078 0.08703 -0.00074 0.00254  -0.00903 609 VAL A C   
1304 O O   . VAL A 175 ? 0.09132 0.09807 0.10250 -0.00143 0.00310  -0.00832 609 VAL A O   
1305 C CB  . VAL A 175 ? 0.07324 0.08437 0.09019 -0.00285 0.00456  -0.00906 609 VAL A CB  
1306 C CG1 . VAL A 175 ? 0.14738 0.15630 0.16410 -0.00303 0.00332  -0.00840 609 VAL A CG1 
1307 C CG2 . VAL A 175 ? 0.07358 0.08869 0.09387 -0.00385 0.00563  -0.00970 609 VAL A CG2 
1308 N N   . ASP A 176 ? 0.07365 0.08081 0.08732 -0.00012 0.00099  -0.00896 610 ASP A N   
1309 C CA  . ASP A 176 ? 0.14926 0.15555 0.15986 -0.00017 0.00020  -0.00816 610 ASP A CA  
1310 C C   . ASP A 176 ? 0.10803 0.11503 0.11820 -0.00028 0.00006  -0.00892 610 ASP A C   
1311 O O   . ASP A 176 ? 0.08763 0.09546 0.09788 -0.00036 -0.00112 -0.00976 610 ASP A O   
1312 C CB  . ASP A 176 ? 0.07637 0.08203 0.08646 0.00033  -0.00151 -0.00734 610 ASP A CB  
1313 C CG  . ASP A 176 ? 0.08383 0.08937 0.09017 -0.00062 -0.00213 -0.00593 610 ASP A CG  
1314 O OD1 . ASP A 176 ? 0.10245 0.10982 0.10724 -0.00111 -0.00125 -0.00635 610 ASP A OD1 
1315 O OD2 . ASP A 176 ? 0.12763 0.13142 0.13287 -0.00085 -0.00349 -0.00426 610 ASP A OD2 
1316 N N   . TRP A 177 ? 0.10076 0.10746 0.11058 -0.00020 0.00111  -0.00878 611 TRP A N   
1317 C CA  . TRP A 177 ? 0.07590 0.08210 0.08582 0.00042  0.00122  -0.01010 611 TRP A CA  
1318 C C   . TRP A 177 ? 0.07674 0.08512 0.08448 0.00115  0.00161  -0.01045 611 TRP A C   
1319 O O   . TRP A 177 ? 0.18528 0.19360 0.19343 0.00239  0.00223  -0.01210 611 TRP A O   
1320 C CB  . TRP A 177 ? 0.07662 0.08078 0.08859 0.00061  0.00187  -0.00948 611 TRP A CB  
1321 C CG  . TRP A 177 ? 0.13038 0.13562 0.14228 0.00122  0.00252  -0.00746 611 TRP A CG  
1322 C CD1 . TRP A 177 ? 0.07556 0.08359 0.08655 0.00220  0.00285  -0.00708 611 TRP A CD1 
1323 C CD2 . TRP A 177 ? 0.11352 0.11835 0.12638 0.00047  0.00270  -0.00522 611 TRP A CD2 
1324 N NE1 . TRP A 177 ? 0.12519 0.13471 0.13696 0.00226  0.00296  -0.00478 611 TRP A NE1 
1325 C CE2 . TRP A 177 ? 0.19222 0.19961 0.20473 0.00118  0.00278  -0.00350 611 TRP A CE2 
1326 C CE3 . TRP A 177 ? 0.09544 0.09905 0.10928 -0.00118 0.00278  -0.00423 611 TRP A CE3 
1327 C CZ2 . TRP A 177 ? 0.09835 0.10681 0.11109 0.00038  0.00256  -0.00068 611 TRP A CZ2 
1328 C CZ3 . TRP A 177 ? 0.18090 0.18546 0.19452 -0.00218 0.00290  -0.00142 611 TRP A CZ3 
1329 C CH2 . TRP A 177 ? 0.14123 0.14803 0.15412 -0.00135 0.00261  0.00040  611 TRP A CH2 
1330 N N   . ASP A 178 ? 0.07608 0.08638 0.08174 0.00035  0.00137  -0.00902 612 ASP A N   
1331 C CA  . ASP A 178 ? 0.07761 0.09139 0.08074 0.00007  0.00163  -0.00915 612 ASP A CA  
1332 C C   . ASP A 178 ? 0.12650 0.14106 0.12806 0.00004  0.00107  -0.01137 612 ASP A C   
1333 O O   . ASP A 178 ? 0.08080 0.09361 0.08278 -0.00047 -0.00031 -0.01171 612 ASP A O   
1334 C CB  . ASP A 178 ? 0.07791 0.09219 0.07884 -0.00180 0.00086  -0.00662 612 ASP A CB  
1335 C CG  . ASP A 178 ? 0.07974 0.09874 0.07797 -0.00308 0.00138  -0.00579 612 ASP A CG  
1336 O OD1 . ASP A 178 ? 0.11650 0.13831 0.11258 -0.00331 0.00137  -0.00685 612 ASP A OD1 
1337 O OD2 . ASP A 178 ? 0.08706 0.10777 0.08508 -0.00436 0.00181  -0.00409 612 ASP A OD2 
1338 N N   . VAL A 179 ? 0.10135 0.11954 0.10119 0.00048  0.00221  -0.01319 613 VAL A N   
1339 C CA  . VAL A 179 ? 0.11210 0.13143 0.10961 0.00011  0.00190  -0.01621 613 VAL A CA  
1340 C C   . VAL A 179 ? 0.20020 0.22155 0.19417 -0.00228 -0.00012 -0.01421 613 VAL A C   
1341 O O   . VAL A 179 ? 0.20176 0.22401 0.19374 -0.00323 -0.00129 -0.01605 613 VAL A O   
1342 C CB  . VAL A 179 ? 0.15320 0.17678 0.14958 0.00141  0.00413  -0.01941 613 VAL A CB  
1343 C CG1 . VAL A 179 ? 0.18985 0.22031 0.18262 -0.00042 0.00473  -0.01753 613 VAL A CG1 
1344 C CG2 . VAL A 179 ? 0.13712 0.15970 0.13187 0.00159  0.00421  -0.02430 613 VAL A CG2 
1345 N N   . HIS A 180 ? 0.14066 0.16238 0.13380 -0.00345 -0.00089 -0.01029 614 HIS A N   
1346 C CA  . HIS A 180 ? 0.11648 0.13898 0.10677 -0.00542 -0.00329 -0.00730 614 HIS A CA  
1347 C C   . HIS A 180 ? 0.09320 0.11104 0.08685 -0.00464 -0.00526 -0.00538 614 HIS A C   
1348 O O   . HIS A 180 ? 0.14009 0.15456 0.13702 -0.00343 -0.00439 -0.00537 614 HIS A O   
1349 C CB  . HIS A 180 ? 0.10306 0.12810 0.09024 -0.00757 -0.00312 -0.00391 614 HIS A CB  
1350 C CG  . HIS A 180 ? 0.22968 0.26159 0.21387 -0.00847 -0.00084 -0.00570 614 HIS A CG  
1351 N ND1 . HIS A 180 ? 0.11699 0.15141 0.10336 -0.00729 0.00178  -0.00717 614 HIS A ND1 
1352 C CD2 . HIS A 180 ? 0.12032 0.15824 0.09972 -0.01033 -0.00067 -0.00647 614 HIS A CD2 
1353 C CE1 . HIS A 180 ? 0.11672 0.15855 0.10051 -0.00792 0.00374  -0.00904 614 HIS A CE1 
1354 N NE2 . HIS A 180 ? 0.10851 0.15257 0.08755 -0.00999 0.00248  -0.00887 614 HIS A NE2 
1355 N N   . HIS A 181 ? 0.09078 0.10938 0.08363 -0.00527 -0.00793 -0.00382 615 HIS A N   
1356 C CA  . HIS A 181 ? 0.11555 0.13101 0.11242 -0.00392 -0.00986 -0.00195 615 HIS A CA  
1357 C C   . HIS A 181 ? 0.09112 0.10238 0.08824 -0.00380 -0.01007 0.00117  615 HIS A C   
1358 O O   . HIS A 181 ? 0.09897 0.11045 0.09227 -0.00578 -0.01081 0.00406  615 HIS A O   
1359 C CB  . HIS A 181 ? 0.09383 0.11223 0.09012 -0.00448 -0.01320 -0.00023 615 HIS A CB  
1360 C CG  . HIS A 181 ? 0.09341 0.11019 0.09530 -0.00230 -0.01519 0.00132  615 HIS A CG  
1361 N ND1 . HIS A 181 ? 0.10596 0.12161 0.10858 -0.00157 -0.01828 0.00567  615 HIS A ND1 
1362 C CD2 . HIS A 181 ? 0.08989 0.10657 0.09736 -0.00054 -0.01446 -0.00085 615 HIS A CD2 
1363 C CE1 . HIS A 181 ? 0.09670 0.11189 0.10576 0.00123  -0.01923 0.00562  615 HIS A CE1 
1364 N NE2 . HIS A 181 ? 0.10291 0.11940 0.11482 0.00162  -0.01676 0.00161  615 HIS A NE2 
1365 N N   . GLY A 182 ? 0.08878 0.09629 0.09008 -0.00195 -0.00934 0.00039  616 GLY A N   
1366 C CA  . GLY A 182 ? 0.14909 0.15143 0.15077 -0.00178 -0.00971 0.00242  616 GLY A CA  
1367 C C   . GLY A 182 ? 0.13740 0.13717 0.14112 -0.00035 -0.01282 0.00529  616 GLY A C   
1368 O O   . GLY A 182 ? 0.20050 0.19842 0.20921 0.00246  -0.01301 0.00420  616 GLY A O   
1369 N N   . ASN A 183 ? 0.17577 0.17609 0.17585 -0.00217 -0.01530 0.00916  617 ASN A N   
1370 C CA  . ASN A 183 ? 0.18750 0.18578 0.18964 -0.00066 -0.01905 0.01297  617 ASN A CA  
1371 C C   . ASN A 183 ? 0.15061 0.14042 0.15630 0.00160  -0.01952 0.01377  617 ASN A C   
1372 O O   . ASN A 183 ? 0.15180 0.13992 0.16297 0.00526  -0.02136 0.01433  617 ASN A O   
1373 C CB  . ASN A 183 ? 0.14394 0.14428 0.14029 -0.00394 -0.02166 0.01781  617 ASN A CB  
1374 C CG  . ASN A 183 ? 0.13646 0.13428 0.12777 -0.00760 -0.02032 0.01952  617 ASN A CG  
1375 O OD1 . ASN A 183 ? 0.13124 0.13304 0.12005 -0.00938 -0.01725 0.01667  617 ASN A OD1 
1376 N ND2 . ASN A 183 ? 0.15623 0.14752 0.14647 -0.00879 -0.02280 0.02440  617 ASN A ND2 
1377 N N   . GLY A 184 ? 0.15481 0.13954 0.15778 -0.00046 -0.01784 0.01343  618 GLY A N   
1378 C CA  . GLY A 184 ? 0.17773 0.15328 0.18329 0.00119  -0.01819 0.01331  618 GLY A CA  
1379 C C   . GLY A 184 ? 0.14629 0.12160 0.15740 0.00501  -0.01583 0.00817  618 GLY A C   
1380 O O   . GLY A 184 ? 0.14705 0.11718 0.16287 0.00863  -0.01674 0.00761  618 GLY A O   
1381 N N   . THR A 185 ? 0.18484 0.16587 0.19560 0.00432  -0.01272 0.00443  619 THR A N   
1382 C CA  . THR A 185 ? 0.13508 0.11732 0.15037 0.00708  -0.01027 -0.00003 619 THR A CA  
1383 C C   . THR A 185 ? 0.12875 0.11509 0.15028 0.01089  -0.01159 -0.00008 619 THR A C   
1384 O O   . THR A 185 ? 0.10509 0.09009 0.13192 0.01443  -0.01088 -0.00237 619 THR A O   
1385 C CB  . THR A 185 ? 0.09768 0.08520 0.11099 0.00504  -0.00729 -0.00269 619 THR A CB  
1386 O OG1 . THR A 185 ? 0.20359 0.18964 0.21164 0.00152  -0.00673 -0.00169 619 THR A OG1 
1387 C CG2 . THR A 185 ? 0.09475 0.08265 0.11088 0.00652  -0.00453 -0.00676 619 THR A CG2 
1388 N N   . GLN A 186 ? 0.16734 0.15950 0.18847 0.01011  -0.01349 0.00211  620 GLN A N   
1389 C CA  . GLN A 186 ? 0.10045 0.09772 0.12760 0.01310  -0.01547 0.00270  620 GLN A CA  
1390 C C   . GLN A 186 ? 0.12059 0.11290 0.15201 0.01685  -0.01835 0.00538  620 GLN A C   
1391 O O   . GLN A 186 ? 0.17347 0.16789 0.21230 0.02111  -0.01832 0.00382  620 GLN A O   
1392 C CB  . GLN A 186 ? 0.12023 0.12382 0.14479 0.01074  -0.01766 0.00481  620 GLN A CB  
1393 C CG  . GLN A 186 ? 0.11983 0.12875 0.14994 0.01320  -0.02112 0.00696  620 GLN A CG  
1394 C CD  . GLN A 186 ? 0.10150 0.11736 0.12839 0.01015  -0.02327 0.00817  620 GLN A CD  
1395 O OE1 . GLN A 186 ? 0.11926 0.13882 0.14443 0.00776  -0.02125 0.00495  620 GLN A OE1 
1396 N NE2 . GLN A 186 ? 0.10539 0.12277 0.13131 0.01010  -0.02757 0.01283  620 GLN A NE2 
1397 N N   . HIS A 187 ? 0.11475 0.10053 0.14198 0.01538  -0.02088 0.00958  621 HIS A N   
1398 C CA  . HIS A 187 ? 0.12399 0.10379 0.15528 0.01893  -0.02443 0.01323  621 HIS A CA  
1399 C C   . HIS A 187 ? 0.19097 0.16261 0.22643 0.02251  -0.02242 0.00957  621 HIS A C   
1400 O O   . HIS A 187 ? 0.19404 0.16336 0.23678 0.02786  -0.02407 0.00987  621 HIS A O   
1401 C CB  . HIS A 187 ? 0.13095 0.10558 0.15589 0.01542  -0.02776 0.01937  621 HIS A CB  
1402 C CG  . HIS A 187 ? 0.12919 0.11224 0.15041 0.01257  -0.03034 0.02315  621 HIS A CG  
1403 N ND1 . HIS A 187 ? 0.19449 0.17759 0.20751 0.00738  -0.03126 0.02677  621 HIS A ND1 
1404 C CD2 . HIS A 187 ? 0.12607 0.11846 0.15040 0.01380  -0.03211 0.02350  621 HIS A CD2 
1405 C CE1 . HIS A 187 ? 0.14048 0.13234 0.15122 0.00571  -0.03330 0.02877  621 HIS A CE1 
1406 N NE2 . HIS A 187 ? 0.18260 0.17985 0.19999 0.00937  -0.03407 0.02688  621 HIS A NE2 
1407 N N   . ILE A 188 ? 0.12698 0.09459 0.15809 0.01979  -0.01892 0.00585  622 ILE A N   
1408 C CA  . ILE A 188 ? 0.13282 0.09237 0.16645 0.02237  -0.01687 0.00160  622 ILE A CA  
1409 C C   . ILE A 188 ? 0.17581 0.14174 0.21705 0.02720  -0.01421 -0.00352 622 ILE A C   
1410 O O   . ILE A 188 ? 0.13672 0.09776 0.18365 0.03207  -0.01380 -0.00622 622 ILE A O   
1411 C CB  . ILE A 188 ? 0.16583 0.12142 0.19238 0.01741  -0.01405 -0.00103 622 ILE A CB  
1412 C CG1 . ILE A 188 ? 0.18780 0.13557 0.20843 0.01316  -0.01683 0.00399  622 ILE A CG1 
1413 C CG2 . ILE A 188 ? 0.13630 0.08655 0.16480 0.01948  -0.01099 -0.00728 622 ILE A CG2 
1414 C CD1 . ILE A 188 ? 0.20531 0.15312 0.21892 0.00727  -0.01465 0.00279  622 ILE A CD1 
1415 N N   . PHE A 189 ? 0.11976 0.09680 0.16156 0.02596  -0.01235 -0.00495 623 PHE A N   
1416 C CA  . PHE A 189 ? 0.15152 0.13641 0.20005 0.02929  -0.00944 -0.00950 623 PHE A CA  
1417 C C   . PHE A 189 ? 0.22758 0.22230 0.28296 0.03186  -0.01172 -0.00719 623 PHE A C   
1418 O O   . PHE A 189 ? 0.21978 0.22370 0.28035 0.03318  -0.00928 -0.01034 623 PHE A O   
1419 C CB  . PHE A 189 ? 0.11531 0.10543 0.15963 0.02530  -0.00534 -0.01305 623 PHE A CB  
1420 C CG  . PHE A 189 ? 0.11151 0.09427 0.14955 0.02254  -0.00313 -0.01558 623 PHE A CG  
1421 C CD1 . PHE A 189 ? 0.11798 0.09622 0.15780 0.02500  -0.00075 -0.02044 623 PHE A CD1 
1422 C CD2 . PHE A 189 ? 0.11032 0.09148 0.14087 0.01746  -0.00339 -0.01350 623 PHE A CD2 
1423 C CE1 . PHE A 189 ? 0.13455 0.10652 0.16808 0.02174  0.00100  -0.02304 623 PHE A CE1 
1424 C CE2 . PHE A 189 ? 0.21450 0.19035 0.23970 0.01455  -0.00172 -0.01555 623 PHE A CE2 
1425 C CZ  . PHE A 189 ? 0.12596 0.09709 0.15227 0.01632  0.00032  -0.02027 623 PHE A CZ  
1426 N N   . GLU A 190 ? 0.14688 0.14070 0.20229 0.03212  -0.01646 -0.00156 624 GLU A N   
1427 C CA  . GLU A 190 ? 0.17335 0.17784 0.23400 0.03322  -0.01907 0.00087  624 GLU A CA  
1428 C C   . GLU A 190 ? 0.17585 0.18643 0.24790 0.03949  -0.01864 -0.00132 624 GLU A C   
1429 O O   . GLU A 190 ? 0.13686 0.15936 0.21408 0.03957  -0.01857 -0.00187 624 GLU A O   
1430 C CB  . GLU A 190 ? 0.12395 0.12648 0.18188 0.03222  -0.02455 0.00760  624 GLU A CB  
1431 C CG  . GLU A 190 ? 0.24565 0.25949 0.30380 0.02977  -0.02696 0.00977  624 GLU A CG  
1432 C CD  . GLU A 190 ? 0.19850 0.21096 0.25023 0.02663  -0.03150 0.01575  624 GLU A CD  
1433 O OE1 . GLU A 190 ? 0.23952 0.24272 0.28842 0.02712  -0.03351 0.01945  624 GLU A OE1 
1434 O OE2 . GLU A 190 ? 0.26052 0.28116 0.30965 0.02321  -0.03300 0.01662  624 GLU A OE2 
1435 N N   . GLU A 191 ? 0.18111 0.18397 0.25754 0.04470  -0.01822 -0.00292 625 GLU A N   
1436 C CA  . GLU A 191 ? 0.12647 0.13506 0.21464 0.05171  -0.01733 -0.00574 625 GLU A CA  
1437 C C   . GLU A 191 ? 0.16642 0.17622 0.25593 0.05278  -0.01106 -0.01353 625 GLU A C   
1438 O O   . GLU A 191 ? 0.23654 0.24649 0.33434 0.05920  -0.00943 -0.01729 625 GLU A O   
1439 C CB  . GLU A 191 ? 0.14990 0.14910 0.24346 0.05794  -0.02133 -0.00251 625 GLU A CB  
1440 C CG  . GLU A 191 ? 0.26556 0.27206 0.36607 0.06097  -0.02713 0.00394  625 GLU A CG  
1441 C CD  . GLU A 191 ? 0.39531 0.39247 0.50290 0.06826  -0.03108 0.00721  625 GLU A CD  
1442 O OE1 . GLU A 191 ? 0.39920 0.38065 0.50097 0.06743  -0.03212 0.00872  625 GLU A OE1 
1443 O OE2 . GLU A 191 ? 0.51118 0.51670 0.63062 0.07482  -0.03326 0.00840  625 GLU A OE2 
1444 N N   . ASP A 192 ? 0.16083 0.17210 0.24248 0.04674  -0.00754 -0.01605 626 ASP A N   
1445 C CA  . ASP A 192 ? 0.17823 0.18926 0.25833 0.04637  -0.00191 -0.02276 626 ASP A CA  
1446 C C   . ASP A 192 ? 0.22586 0.25015 0.30616 0.04262  0.00136  -0.02460 626 ASP A C   
1447 O O   . ASP A 192 ? 0.14350 0.16943 0.21758 0.03692  0.00054  -0.02182 626 ASP A O   
1448 C CB  . ASP A 192 ? 0.12894 0.12766 0.19844 0.04206  -0.00110 -0.02343 626 ASP A CB  
1449 C CG  . ASP A 192 ? 0.14186 0.13877 0.20946 0.04211  0.00402  -0.03048 626 ASP A CG  
1450 O OD1 . ASP A 192 ? 0.21589 0.22162 0.28981 0.04523  0.00751  -0.03511 626 ASP A OD1 
1451 O OD2 . ASP A 192 ? 0.14489 0.13240 0.20450 0.03866  0.00459  -0.03150 626 ASP A OD2 
1452 N N   . ASP A 193 ? 0.12067 0.15424 0.20816 0.04576  0.00516  -0.02934 627 ASP A N   
1453 C CA  . ASP A 193 ? 0.10339 0.14955 0.19106 0.04168  0.00866  -0.03105 627 ASP A CA  
1454 C C   . ASP A 193 ? 0.16662 0.21084 0.24691 0.03799  0.01354  -0.03546 627 ASP A C   
1455 O O   . ASP A 193 ? 0.22373 0.27799 0.30366 0.03433  0.01673  -0.03672 627 ASP A O   
1456 C CB  . ASP A 193 ? 0.22422 0.28476 0.32413 0.04621  0.01019  -0.03316 627 ASP A CB  
1457 C CG  . ASP A 193 ? 0.19964 0.25880 0.30617 0.05359  0.01313  -0.03896 627 ASP A CG  
1458 O OD1 . ASP A 193 ? 0.15574 0.20345 0.25625 0.05398  0.01497  -0.04247 627 ASP A OD1 
1459 O OD2 . ASP A 193 ? 0.17053 0.24041 0.28875 0.05913  0.01356  -0.04029 627 ASP A OD2 
1460 N N   . SER A 194 ? 0.12866 0.16059 0.20287 0.03832  0.01395  -0.03750 628 SER A N   
1461 C CA  . SER A 194 ? 0.14270 0.17289 0.20894 0.03419  0.01789  -0.04128 628 SER A CA  
1462 C C   . SER A 194 ? 0.17739 0.20208 0.23370 0.02774  0.01614  -0.03725 628 SER A C   
1463 O O   . SER A 194 ? 0.11767 0.14394 0.16767 0.02338  0.01887  -0.03887 628 SER A O   
1464 C CB  . SER A 194 ? 0.12036 0.14093 0.18544 0.03762  0.01960  -0.04679 628 SER A CB  
1465 O OG  . SER A 194 ? 0.12370 0.13012 0.18337 0.03670  0.01592  -0.04394 628 SER A OG  
1466 N N   . VAL A 195 ? 0.16190 0.18103 0.21682 0.02713  0.01170  -0.03206 629 VAL A N   
1467 C CA  . VAL A 195 ? 0.15022 0.16528 0.19694 0.02177  0.01013  -0.02843 629 VAL A CA  
1468 C C   . VAL A 195 ? 0.10907 0.12932 0.15768 0.02032  0.00744  -0.02400 629 VAL A C   
1469 O O   . VAL A 195 ? 0.10557 0.12499 0.15798 0.02291  0.00410  -0.02141 629 VAL A O   
1470 C CB  . VAL A 195 ? 0.16823 0.17115 0.20983 0.02149  0.00773  -0.02703 629 VAL A CB  
1471 C CG1 . VAL A 195 ? 0.09787 0.09893 0.13228 0.01643  0.00630  -0.02333 629 VAL A CG1 
1472 C CG2 . VAL A 195 ? 0.11216 0.10928 0.15123 0.02206  0.01031  -0.03207 629 VAL A CG2 
1473 N N   . LEU A 196 ? 0.08696 0.11226 0.13276 0.01600  0.00868  -0.02311 630 LEU A N   
1474 C CA  . LEU A 196 ? 0.08231 0.11163 0.12907 0.01382  0.00643  -0.01982 630 LEU A CA  
1475 C C   . LEU A 196 ? 0.16408 0.18640 0.20397 0.01120  0.00422  -0.01698 630 LEU A C   
1476 O O   . LEU A 196 ? 0.08242 0.10151 0.11675 0.00863  0.00560  -0.01713 630 LEU A O   
1477 C CB  . LEU A 196 ? 0.07940 0.11688 0.12721 0.01043  0.00890  -0.02035 630 LEU A CB  
1478 C CG  . LEU A 196 ? 0.13373 0.17462 0.18222 0.00721  0.00692  -0.01767 630 LEU A CG  
1479 C CD1 . LEU A 196 ? 0.07607 0.12246 0.13147 0.00954  0.00434  -0.01695 630 LEU A CD1 
1480 C CD2 . LEU A 196 ? 0.07507 0.12182 0.12350 0.00309  0.00949  -0.01776 630 LEU A CD2 
1481 N N   . TYR A 197 ? 0.08069 0.10171 0.12108 0.01186  0.00081  -0.01440 631 TYR A N   
1482 C CA  . TYR A 197 ? 0.12872 0.14472 0.16302 0.00961  -0.00102 -0.01209 631 TYR A CA  
1483 C C   . TYR A 197 ? 0.10469 0.12455 0.13862 0.00698  -0.00206 -0.01115 631 TYR A C   
1484 O O   . TYR A 197 ? 0.12749 0.15246 0.16565 0.00741  -0.00379 -0.01070 631 TYR A O   
1485 C CB  . TYR A 197 ? 0.13871 0.15013 0.17229 0.01151  -0.00406 -0.00981 631 TYR A CB  
1486 C CG  . TYR A 197 ? 0.08330 0.09111 0.11038 0.00884  -0.00531 -0.00771 631 TYR A CG  
1487 C CD1 . TYR A 197 ? 0.12478 0.12908 0.14707 0.00684  -0.00349 -0.00828 631 TYR A CD1 
1488 C CD2 . TYR A 197 ? 0.15265 0.16188 0.17844 0.00818  -0.00824 -0.00528 631 TYR A CD2 
1489 C CE1 . TYR A 197 ? 0.11730 0.12000 0.13460 0.00470  -0.00426 -0.00661 631 TYR A CE1 
1490 C CE2 . TYR A 197 ? 0.13643 0.14379 0.15628 0.00574  -0.00878 -0.00394 631 TYR A CE2 
1491 C CZ  . TYR A 197 ? 0.12177 0.12607 0.13786 0.00424  -0.00665 -0.00467 631 TYR A CZ  
1492 O OH  . TYR A 197 ? 0.20460 0.20864 0.21574 0.00214  -0.00686 -0.00354 631 TYR A OH  
1493 N N   . ILE A 198 ? 0.07535 0.09279 0.10457 0.00430  -0.00116 -0.01101 632 ILE A N   
1494 C CA  . ILE A 198 ? 0.07548 0.09447 0.10389 0.00181  -0.00191 -0.01084 632 ILE A CA  
1495 C C   . ILE A 198 ? 0.13969 0.15426 0.16258 0.00096  -0.00248 -0.01020 632 ILE A C   
1496 O O   . ILE A 198 ? 0.07603 0.08771 0.09611 0.00067  -0.00096 -0.01005 632 ILE A O   
1497 C CB  . ILE A 198 ? 0.07325 0.09430 0.10296 -0.00043 0.00022  -0.01153 632 ILE A CB  
1498 C CG1 . ILE A 198 ? 0.07563 0.10320 0.11113 0.00015  0.00130  -0.01239 632 ILE A CG1 
1499 C CG2 . ILE A 198 ? 0.13774 0.15802 0.16647 -0.00309 -0.00082 -0.01151 632 ILE A CG2 
1500 C CD1 . ILE A 198 ? 0.15396 0.18498 0.19077 -0.00302 0.00325  -0.01241 632 ILE A CD1 
1501 N N   . SER A 199 ? 0.16448 0.17967 0.18591 0.00046  -0.00462 -0.00993 633 SER A N   
1502 C CA  . SER A 199 ? 0.08454 0.09724 0.10094 -0.00014 -0.00488 -0.00975 633 SER A CA  
1503 C C   . SER A 199 ? 0.09186 0.10531 0.10694 -0.00184 -0.00552 -0.01154 633 SER A C   
1504 O O   . SER A 199 ? 0.10231 0.11883 0.11866 -0.00279 -0.00746 -0.01202 633 SER A O   
1505 C CB  . SER A 199 ? 0.09419 0.10676 0.10845 0.00063  -0.00676 -0.00775 633 SER A CB  
1506 O OG  . SER A 199 ? 0.08595 0.09797 0.09530 -0.00046 -0.00664 -0.00764 633 SER A OG  
1507 N N   . LEU A 200 ? 0.08871 0.09942 0.10154 -0.00215 -0.00403 -0.01273 634 LEU A N   
1508 C CA  . LEU A 200 ? 0.08929 0.09927 0.09995 -0.00317 -0.00434 -0.01526 634 LEU A CA  
1509 C C   . LEU A 200 ? 0.13880 0.14979 0.14508 -0.00256 -0.00408 -0.01546 634 LEU A C   
1510 O O   . LEU A 200 ? 0.16466 0.17528 0.17011 -0.00150 -0.00287 -0.01389 634 LEU A O   
1511 C CB  . LEU A 200 ? 0.08482 0.09067 0.09676 -0.00333 -0.00286 -0.01655 634 LEU A CB  
1512 C CG  . LEU A 200 ? 0.08240 0.08739 0.09813 -0.00436 -0.00238 -0.01519 634 LEU A CG  
1513 C CD1 . LEU A 200 ? 0.08775 0.09249 0.10381 -0.00312 -0.00082 -0.01282 634 LEU A CD1 
1514 C CD2 . LEU A 200 ? 0.08677 0.08731 0.10346 -0.00593 -0.00232 -0.01661 634 LEU A CD2 
1515 N N   . HIS A 201 ? 0.08790 0.10111 0.09111 -0.00374 -0.00522 -0.01740 635 HIS A N   
1516 C CA  . HIS A 201 ? 0.09210 0.10820 0.09073 -0.00379 -0.00495 -0.01707 635 HIS A CA  
1517 C C   . HIS A 201 ? 0.14628 0.16506 0.14090 -0.00544 -0.00561 -0.02055 635 HIS A C   
1518 O O   . HIS A 201 ? 0.09765 0.11747 0.09250 -0.00716 -0.00770 -0.02157 635 HIS A O   
1519 C CB  . HIS A 201 ? 0.08878 0.10686 0.08667 -0.00407 -0.00669 -0.01278 635 HIS A CB  
1520 C CG  . HIS A 201 ? 0.15834 0.17775 0.15870 -0.00451 -0.00946 -0.01132 635 HIS A CG  
1521 N ND1 . HIS A 201 ? 0.08903 0.10684 0.09466 -0.00324 -0.00957 -0.01021 635 HIS A ND1 
1522 C CD2 . HIS A 201 ? 0.17562 0.19902 0.17427 -0.00602 -0.01225 -0.01081 635 HIS A CD2 
1523 C CE1 . HIS A 201 ? 0.08712 0.10812 0.09506 -0.00351 -0.01219 -0.00913 635 HIS A CE1 
1524 N NE2 . HIS A 201 ? 0.10567 0.13000 0.10944 -0.00526 -0.01415 -0.00917 635 HIS A NE2 
1525 N N   . ARG A 202 ? 0.09813 0.11903 0.08908 -0.00511 -0.00375 -0.02257 636 ARG A N   
1526 C CA  . ARG A 202 ? 0.14738 0.17230 0.13309 -0.00696 -0.00403 -0.02611 636 ARG A CA  
1527 C C   . ARG A 202 ? 0.14326 0.17341 0.12528 -0.00947 -0.00696 -0.02239 636 ARG A C   
1528 O O   . ARG A 202 ? 0.14528 0.17695 0.12667 -0.00947 -0.00742 -0.01763 636 ARG A O   
1529 C CB  . ARG A 202 ? 0.23695 0.26459 0.22004 -0.00569 -0.00083 -0.02902 636 ARG A CB  
1530 C CG  . ARG A 202 ? 0.14099 0.17328 0.11817 -0.00747 -0.00028 -0.03404 636 ARG A CG  
1531 C CD  . ARG A 202 ? 0.15642 0.19102 0.13296 -0.00507 0.00368  -0.03849 636 ARG A CD  
1532 N NE  . ARG A 202 ? 0.19088 0.22956 0.16165 -0.00658 0.00471  -0.04481 636 ARG A NE  
1533 C CZ  . ARG A 202 ? 0.13188 0.17438 0.10123 -0.00462 0.00841  -0.05012 636 ARG A CZ  
1534 N NH1 . ARG A 202 ? 0.12843 0.17194 0.10230 -0.00096 0.01118  -0.04936 636 ARG A NH1 
1535 N NH2 . ARG A 202 ? 0.14105 0.18730 0.10443 -0.00638 0.00937  -0.05660 636 ARG A NH2 
1536 N N   . TYR A 203 ? 0.17783 0.21053 0.15740 -0.01188 -0.00927 -0.02431 637 TYR A N   
1537 C CA  . TYR A 203 ? 0.16141 0.19921 0.13845 -0.01414 -0.01300 -0.02004 637 TYR A CA  
1538 C C   . TYR A 203 ? 0.12562 0.17020 0.09461 -0.01740 -0.01365 -0.02230 637 TYR A C   
1539 O O   . TYR A 203 ? 0.15332 0.20268 0.11776 -0.01886 -0.01449 -0.01825 637 TYR A O   
1540 C CB  . TYR A 203 ? 0.11137 0.14837 0.09343 -0.01449 -0.01601 -0.01912 637 TYR A CB  
1541 C CG  . TYR A 203 ? 0.11378 0.15637 0.09507 -0.01604 -0.02048 -0.01430 637 TYR A CG  
1542 C CD1 . TYR A 203 ? 0.11278 0.15568 0.09440 -0.01483 -0.02191 -0.00799 637 TYR A CD1 
1543 C CD2 . TYR A 203 ? 0.18778 0.23506 0.16840 -0.01879 -0.02363 -0.01582 637 TYR A CD2 
1544 C CE1 . TYR A 203 ? 0.11616 0.16353 0.09779 -0.01567 -0.02645 -0.00291 637 TYR A CE1 
1545 C CE2 . TYR A 203 ? 0.16836 0.22172 0.14897 -0.01990 -0.02823 -0.01079 637 TYR A CE2 
1546 C CZ  . TYR A 203 ? 0.17084 0.22400 0.15218 -0.01799 -0.02968 -0.00413 637 TYR A CZ  
1547 O OH  . TYR A 203 ? 0.14731 0.20589 0.12932 -0.01854 -0.03469 0.00151  637 TYR A OH  
1548 N N   . GLU A 204 ? 0.12610 0.17114 0.09277 -0.01906 -0.01338 -0.02865 638 GLU A N   
1549 C CA  . GLU A 204 ? 0.13502 0.18678 0.09320 -0.02244 -0.01350 -0.03242 638 GLU A CA  
1550 C C   . GLU A 204 ? 0.20962 0.26886 0.16365 -0.02584 -0.01815 -0.02681 638 GLU A C   
1551 O O   . GLU A 204 ? 0.21845 0.28441 0.16539 -0.02816 -0.01826 -0.02495 638 GLU A O   
1552 C CB  . GLU A 204 ? 0.23577 0.29020 0.18978 -0.02146 -0.00919 -0.03481 638 GLU A CB  
1553 C CG  . GLU A 204 ? 0.19192 0.23973 0.15106 -0.01728 -0.00493 -0.03912 638 GLU A CG  
1554 C CD  . GLU A 204 ? 0.18298 0.22630 0.14207 -0.01700 -0.00352 -0.04775 638 GLU A CD  
1555 O OE1 . GLU A 204 ? 0.20128 0.24631 0.15647 -0.02051 -0.00589 -0.05081 638 GLU A OE1 
1556 O OE2 . GLU A 204 ? 0.20510 0.24290 0.16817 -0.01335 -0.00027 -0.05142 638 GLU A OE2 
1557 N N   . ASP A 205 ? 0.13705 0.19585 0.09585 -0.02618 -0.02214 -0.02376 639 ASP A N   
1558 C CA  . ASP A 205 ? 0.17721 0.24310 0.13388 -0.02870 -0.02738 -0.01775 639 ASP A CA  
1559 C C   . ASP A 205 ? 0.14609 0.21339 0.10101 -0.02792 -0.02816 -0.00998 639 ASP A C   
1560 O O   . ASP A 205 ? 0.27096 0.34500 0.22025 -0.03088 -0.03157 -0.00532 639 ASP A O   
1561 C CB  . ASP A 205 ? 0.28411 0.35786 0.23214 -0.03379 -0.02926 -0.02178 639 ASP A CB  
1562 C CG  . ASP A 205 ? 0.30466 0.38651 0.25124 -0.03654 -0.03553 -0.01524 639 ASP A CG  
1563 O OD1 . ASP A 205 ? 0.38027 0.46089 0.33500 -0.03414 -0.03863 -0.00980 639 ASP A OD1 
1564 O OD2 . ASP A 205 ? 0.25667 0.34674 0.19403 -0.04094 -0.03736 -0.01538 639 ASP A OD2 
1565 N N   . GLY A 206 ? 0.22743 0.28824 0.18682 -0.02443 -0.02526 -0.00824 640 GLY A N   
1566 C CA  . GLY A 206 ? 0.19919 0.25990 0.15700 -0.02427 -0.02588 -0.00125 640 GLY A CA  
1567 C C   . GLY A 206 ? 0.20838 0.27313 0.15850 -0.02664 -0.02270 -0.00230 640 GLY A C   
1568 O O   . GLY A 206 ? 0.33905 0.40452 0.28680 -0.02780 -0.02349 0.00400  640 GLY A O   
1569 N N   . ALA A 207 ? 0.15461 0.22206 0.10101 -0.02744 -0.01904 -0.01011 641 ALA A N   
1570 C CA  . ALA A 207 ? 0.14353 0.21654 0.08347 -0.02922 -0.01530 -0.01198 641 ALA A CA  
1571 C C   . ALA A 207 ? 0.18839 0.25698 0.13305 -0.02601 -0.01107 -0.01249 641 ALA A C   
1572 O O   . ALA A 207 ? 0.33331 0.40747 0.27400 -0.02735 -0.00797 -0.01286 641 ALA A O   
1573 C CB  . ALA A 207 ? 0.18835 0.26644 0.12268 -0.03084 -0.01284 -0.02105 641 ALA A CB  
1574 N N   . PHE A 208 ? 0.22606 0.28611 0.17896 -0.02218 -0.01087 -0.01246 642 PHE A N   
1575 C CA  . PHE A 208 ? 0.16480 0.22100 0.12231 -0.01936 -0.00747 -0.01260 642 PHE A CA  
1576 C C   . PHE A 208 ? 0.15101 0.20315 0.11132 -0.01933 -0.00961 -0.00493 642 PHE A C   
1577 O O   . PHE A 208 ? 0.25796 0.30654 0.22057 -0.01907 -0.01336 -0.00102 642 PHE A O   
1578 C CB  . PHE A 208 ? 0.15105 0.20049 0.11514 -0.01555 -0.00572 -0.01773 642 PHE A CB  
1579 C CG  . PHE A 208 ? 0.13241 0.18109 0.09941 -0.01289 -0.00154 -0.02041 642 PHE A CG  
1580 C CD1 . PHE A 208 ? 0.24459 0.29895 0.20849 -0.01268 0.00192  -0.02575 642 PHE A CD1 
1581 C CD2 . PHE A 208 ? 0.10830 0.15150 0.08124 -0.01051 -0.00109 -0.01776 642 PHE A CD2 
1582 C CE1 . PHE A 208 ? 0.21204 0.26687 0.17976 -0.00964 0.00553  -0.02792 642 PHE A CE1 
1583 C CE2 . PHE A 208 ? 0.18491 0.22857 0.16078 -0.00817 0.00222  -0.01966 642 PHE A CE2 
1584 C CZ  . PHE A 208 ? 0.20768 0.25731 0.18145 -0.00749 0.00541  -0.02449 642 PHE A CZ  
1585 N N   . PHE A 209 ? 0.16990 0.22275 0.13035 -0.01957 -0.00722 -0.00310 643 PHE A N   
1586 C CA  . PHE A 209 ? 0.17622 0.22385 0.13917 -0.01985 -0.00894 0.00325  643 PHE A CA  
1587 C C   . PHE A 209 ? 0.26428 0.30327 0.23437 -0.01622 -0.01015 0.00291  643 PHE A C   
1588 O O   . PHE A 209 ? 0.14462 0.18169 0.11854 -0.01351 -0.00809 -0.00203 643 PHE A O   
1589 C CB  . PHE A 209 ? 0.12660 0.17658 0.08963 -0.02071 -0.00570 0.00375  643 PHE A CB  
1590 C CG  . PHE A 209 ? 0.11599 0.16067 0.08020 -0.02229 -0.00750 0.01001  643 PHE A CG  
1591 C CD1 . PHE A 209 ? 0.12312 0.17001 0.08217 -0.02679 -0.00953 0.01617  643 PHE A CD1 
1592 C CD2 . PHE A 209 ? 0.11062 0.14773 0.08066 -0.01968 -0.00725 0.00972  643 PHE A CD2 
1593 C CE1 . PHE A 209 ? 0.12534 0.16557 0.08545 -0.02851 -0.01142 0.02175  643 PHE A CE1 
1594 C CE2 . PHE A 209 ? 0.11260 0.14386 0.08335 -0.02133 -0.00889 0.01456  643 PHE A CE2 
1595 C CZ  . PHE A 209 ? 0.18729 0.21940 0.15328 -0.02568 -0.01103 0.02049  643 PHE A CZ  
1596 N N   . PRO A 210 ? 0.15328 0.18694 0.12549 -0.01601 -0.01338 0.00805  644 PRO A N   
1597 C CA  . PRO A 210 ? 0.11863 0.15173 0.08745 -0.01881 -0.01650 0.01500  644 PRO A CA  
1598 C C   . PRO A 210 ? 0.22423 0.26138 0.18945 -0.02047 -0.02043 0.01801  644 PRO A C   
1599 O O   . PRO A 210 ? 0.17800 0.21272 0.14217 -0.02174 -0.02415 0.02465  644 PRO A O   
1600 C CB  . PRO A 210 ? 0.17335 0.19699 0.14793 -0.01635 -0.01787 0.01754  644 PRO A CB  
1601 C CG  . PRO A 210 ? 0.11063 0.13240 0.09107 -0.01242 -0.01721 0.01289  644 PRO A CG  
1602 C CD  . PRO A 210 ? 0.12713 0.15387 0.10625 -0.01248 -0.01374 0.00707  644 PRO A CD  
1603 N N   . ASN A 211 ? 0.21516 0.25807 0.17855 -0.02058 -0.02002 0.01336  645 ASN A N   
1604 C CA  . ASN A 211 ? 0.17485 0.22461 0.13254 -0.02357 -0.02327 0.01542  645 ASN A CA  
1605 C C   . ASN A 211 ? 0.18092 0.22799 0.14210 -0.02235 -0.02873 0.02111  645 ASN A C   
1606 O O   . ASN A 211 ? 0.23501 0.28458 0.19210 -0.02494 -0.03258 0.02769  645 ASN A O   
1607 C CB  . ASN A 211 ? 0.18880 0.24493 0.13808 -0.02837 -0.02278 0.01892  645 ASN A CB  
1608 C CG  . ASN A 211 ? 0.19486 0.25590 0.14148 -0.02910 -0.01722 0.01288  645 ASN A CG  
1609 O OD1 . ASN A 211 ? 0.20440 0.26391 0.15223 -0.02926 -0.01466 0.01396  645 ASN A OD1 
1610 N ND2 . ASN A 211 ? 0.32192 0.38901 0.26534 -0.02945 -0.01539 0.00621  645 ASN A ND2 
1611 N N   . SER A 212 ? 0.22438 0.26703 0.19344 -0.01834 -0.02912 0.01877  646 SER A N   
1612 C CA  . SER A 212 ? 0.13077 0.17204 0.10503 -0.01615 -0.03389 0.02332  646 SER A CA  
1613 C C   . SER A 212 ? 0.12573 0.16916 0.10569 -0.01400 -0.03392 0.01833  646 SER A C   
1614 O O   . SER A 212 ? 0.11926 0.16020 0.10204 -0.01263 -0.03005 0.01250  646 SER A O   
1615 C CB  . SER A 212 ? 0.14782 0.17983 0.12781 -0.01292 -0.03449 0.02740  646 SER A CB  
1616 O OG  . SER A 212 ? 0.13746 0.16855 0.12356 -0.00987 -0.03897 0.03141  646 SER A OG  
1617 N N   . GLU A 213 ? 0.13279 0.18130 0.11456 -0.01406 -0.03858 0.02115  647 GLU A N   
1618 C CA  . GLU A 213 ? 0.13832 0.18982 0.12645 -0.01252 -0.03912 0.01727  647 GLU A CA  
1619 C C   . GLU A 213 ? 0.18347 0.22958 0.18176 -0.00750 -0.03830 0.01746  647 GLU A C   
1620 O O   . GLU A 213 ? 0.18855 0.23777 0.19297 -0.00631 -0.03839 0.01453  647 GLU A O   
1621 C CB  . GLU A 213 ? 0.14464 0.20504 0.13197 -0.01448 -0.04469 0.02045  647 GLU A CB  
1622 C CG  . GLU A 213 ? 0.13828 0.20515 0.11453 -0.01995 -0.04564 0.02011  647 GLU A CG  
1623 C CD  . GLU A 213 ? 0.29688 0.37352 0.27181 -0.02249 -0.05149 0.02313  647 GLU A CD  
1624 O OE1 . GLU A 213 ? 0.39831 0.47957 0.37614 -0.02345 -0.05212 0.01854  647 GLU A OE1 
1625 O OE2 . GLU A 213 ? 0.26549 0.34534 0.23648 -0.02389 -0.05574 0.03052  647 GLU A OE2 
1626 N N   . ASP A 214 ? 0.11979 0.15833 0.11980 -0.00496 -0.03742 0.02054  648 ASP A N   
1627 C CA  . ASP A 214 ? 0.15028 0.18342 0.15872 -0.00046 -0.03545 0.01901  648 ASP A CA  
1628 C C   . ASP A 214 ? 0.11606 0.14838 0.12562 -0.00074 -0.03062 0.01228  648 ASP A C   
1629 O O   . ASP A 214 ? 0.21901 0.24998 0.23553 0.00218  -0.02901 0.01021  648 ASP A O   
1630 C CB  . ASP A 214 ? 0.13393 0.15799 0.14214 0.00123  -0.03487 0.02231  648 ASP A CB  
1631 C CG  . ASP A 214 ? 0.19602 0.21862 0.20460 0.00216  -0.04003 0.02979  648 ASP A CG  
1632 O OD1 . ASP A 214 ? 0.12988 0.15940 0.14006 0.00228  -0.04425 0.03269  648 ASP A OD1 
1633 O OD2 . ASP A 214 ? 0.26466 0.27899 0.27192 0.00251  -0.04016 0.03309  648 ASP A OD2 
1634 N N   . ALA A 215 ? 0.12849 0.16184 0.13151 -0.00408 -0.02828 0.00895  649 ALA A N   
1635 C CA  . ALA A 215 ? 0.12097 0.15246 0.12463 -0.00433 -0.02409 0.00332  649 ALA A CA  
1636 C C   . ALA A 215 ? 0.14020 0.17642 0.14603 -0.00576 -0.02453 -0.00042 649 ALA A C   
1637 O O   . ALA A 215 ? 0.14071 0.17475 0.14704 -0.00631 -0.02149 -0.00469 649 ALA A O   
1638 C CB  . ALA A 215 ? 0.11664 0.14666 0.11321 -0.00652 -0.02133 0.00142  649 ALA A CB  
1639 N N   . ASN A 216 ? 0.10321 0.14579 0.11041 -0.00670 -0.02850 0.00136  650 ASN A N   
1640 C CA  . ASN A 216 ? 0.10680 0.15404 0.11522 -0.00927 -0.02909 -0.00247 650 ASN A CA  
1641 C C   . ASN A 216 ? 0.12172 0.16980 0.13918 -0.00739 -0.02823 -0.00337 650 ASN A C   
1642 O O   . ASN A 216 ? 0.13852 0.18529 0.16166 -0.00364 -0.02787 -0.00088 650 ASN A O   
1643 C CB  . ASN A 216 ? 0.11690 0.17225 0.12277 -0.01196 -0.03391 -0.00050 650 ASN A CB  
1644 C CG  . ASN A 216 ? 0.11239 0.17094 0.11455 -0.01647 -0.03398 -0.00586 650 ASN A CG  
1645 O OD1 . ASN A 216 ? 0.16242 0.21616 0.16449 -0.01725 -0.03051 -0.01082 650 ASN A OD1 
1646 N ND2 . ASN A 216 ? 0.18733 0.25360 0.18615 -0.01967 -0.03818 -0.00486 650 ASN A ND2 
1647 N N   . TYR A 217 ? 0.13203 0.18235 0.15061 -0.01035 -0.02777 -0.00725 651 TYR A N   
1648 C CA  . TYR A 217 ? 0.09744 0.14929 0.12385 -0.00975 -0.02638 -0.00831 651 TYR A CA  
1649 C C   . TYR A 217 ? 0.15252 0.21234 0.18719 -0.00731 -0.02923 -0.00488 651 TYR A C   
1650 O O   . TYR A 217 ? 0.12635 0.18784 0.16821 -0.00533 -0.02734 -0.00509 651 TYR A O   
1651 C CB  . TYR A 217 ? 0.09740 0.15007 0.12297 -0.01449 -0.02610 -0.01254 651 TYR A CB  
1652 C CG  . TYR A 217 ? 0.14319 0.20351 0.16734 -0.01830 -0.03040 -0.01299 651 TYR A CG  
1653 C CD1 . TYR A 217 ? 0.11843 0.18832 0.14993 -0.01911 -0.03335 -0.01124 651 TYR A CD1 
1654 C CD2 . TYR A 217 ? 0.12700 0.18608 0.14248 -0.02128 -0.03146 -0.01545 651 TYR A CD2 
1655 C CE1 . TYR A 217 ? 0.20104 0.27896 0.23118 -0.02308 -0.03773 -0.01145 651 TYR A CE1 
1656 C CE2 . TYR A 217 ? 0.16348 0.23011 0.17672 -0.02538 -0.03555 -0.01618 651 TYR A CE2 
1657 C CZ  . TYR A 217 ? 0.11332 0.18930 0.13387 -0.02643 -0.03893 -0.01396 651 TYR A CZ  
1658 O OH  . TYR A 217 ? 0.19488 0.27946 0.21323 -0.03099 -0.04347 -0.01447 651 TYR A OH  
1659 N N   . ASP A 218 ? 0.09800 0.16349 0.13206 -0.00727 -0.03370 -0.00164 652 ASP A N   
1660 C CA  . ASP A 218 ? 0.09978 0.17381 0.14282 -0.00443 -0.03694 0.00184  652 ASP A CA  
1661 C C   . ASP A 218 ? 0.15492 0.22504 0.20224 0.00175  -0.03652 0.00536  652 ASP A C   
1662 O O   . ASP A 218 ? 0.19658 0.27295 0.25195 0.00536  -0.03934 0.00850  652 ASP A O   
1663 C CB  . ASP A 218 ? 0.10405 0.18661 0.14517 -0.00703 -0.04267 0.00451  652 ASP A CB  
1664 C CG  . ASP A 218 ? 0.22524 0.30429 0.25863 -0.00658 -0.04498 0.00833  652 ASP A CG  
1665 O OD1 . ASP A 218 ? 0.15107 0.22140 0.17729 -0.00697 -0.04182 0.00694  652 ASP A OD1 
1666 O OD2 . ASP A 218 ? 0.32705 0.41296 0.36172 -0.00611 -0.05018 0.01318  652 ASP A OD2 
1667 N N   . LYS A 219 ? 0.10500 0.16503 0.14763 0.00311  -0.03320 0.00472  653 LYS A N   
1668 C CA  . LYS A 219 ? 0.13686 0.19134 0.18294 0.00834  -0.03243 0.00710  653 LYS A CA  
1669 C C   . LYS A 219 ? 0.09177 0.14485 0.14327 0.01035  -0.02778 0.00344  653 LYS A C   
1670 O O   . LYS A 219 ? 0.08907 0.13542 0.13617 0.00923  -0.02393 0.00088  653 LYS A O   
1671 C CB  . LYS A 219 ? 0.17151 0.21679 0.20909 0.00772  -0.03184 0.00873  653 LYS A CB  
1672 C CG  . LYS A 219 ? 0.17290 0.21842 0.20792 0.00819  -0.03669 0.01456  653 LYS A CG  
1673 C CD  . LYS A 219 ? 0.10897 0.16386 0.14187 0.00471  -0.04073 0.01581  653 LYS A CD  
1674 C CE  . LYS A 219 ? 0.11674 0.17217 0.14499 0.00406  -0.04553 0.02212  653 LYS A CE  
1675 N NZ  . LYS A 219 ? 0.19677 0.26038 0.21850 -0.00124 -0.04836 0.02196  653 LYS A NZ  
1676 N N   . VAL A 220 ? 0.09106 0.15171 0.15236 0.01331  -0.02817 0.00334  654 VAL A N   
1677 C CA  . VAL A 220 ? 0.08700 0.14932 0.15351 0.01439  -0.02367 -0.00030 654 VAL A CA  
1678 C C   . VAL A 220 ? 0.12019 0.17894 0.19194 0.02043  -0.02189 -0.00052 654 VAL A C   
1679 O O   . VAL A 220 ? 0.08632 0.14770 0.16262 0.02173  -0.01797 -0.00378 654 VAL A O   
1680 C CB  . VAL A 220 ? 0.10279 0.17774 0.17679 0.01262  -0.02430 -0.00132 654 VAL A CB  
1681 C CG1 . VAL A 220 ? 0.19311 0.27004 0.26134 0.00611  -0.02617 -0.00186 654 VAL A CG1 
1682 C CG2 . VAL A 220 ? 0.11392 0.19789 0.19760 0.01725  -0.02802 0.00160  654 VAL A CG2 
1683 N N   . GLY A 221 ? 0.09372 0.14632 0.16465 0.02384  -0.02458 0.00271  655 GLY A N   
1684 C CA  . GLY A 221 ? 0.18473 0.23207 0.26059 0.02971  -0.02329 0.00217  655 GLY A CA  
1685 C C   . GLY A 221 ? 0.17343 0.22515 0.25828 0.03529  -0.02763 0.00578  655 GLY A C   
1686 O O   . GLY A 221 ? 0.21810 0.27842 0.30551 0.03434  -0.03183 0.00904  655 GLY A O   
1687 N N   . LEU A 222 ? 0.13266 0.17805 0.22240 0.04127  -0.02673 0.00504  656 LEU A N   
1688 C CA  . LEU A 222 ? 0.20557 0.25276 0.30481 0.04799  -0.03081 0.00856  656 LEU A CA  
1689 C C   . LEU A 222 ? 0.11795 0.16657 0.22729 0.05476  -0.02705 0.00367  656 LEU A C   
1690 O O   . LEU A 222 ? 0.17112 0.21262 0.27710 0.05461  -0.02213 -0.00133 656 LEU A O   
1691 C CB  . LEU A 222 ? 0.12993 0.16412 0.22409 0.04900  -0.03490 0.01395  656 LEU A CB  
1692 C CG  . LEU A 222 ? 0.17635 0.20918 0.25997 0.04256  -0.03856 0.01902  656 LEU A CG  
1693 C CD1 . LEU A 222 ? 0.18949 0.20984 0.26886 0.04352  -0.04223 0.02467  656 LEU A CD1 
1694 C CD2 . LEU A 222 ? 0.12242 0.16904 0.20924 0.04105  -0.04290 0.02234  656 LEU A CD2 
1695 N N   . GLY A 223 ? 0.12078 0.17946 0.24255 0.06068  -0.02938 0.00496  657 GLY A N   
1696 C CA  . GLY A 223 ? 0.12457 0.18548 0.25723 0.06828  -0.02588 0.00008  657 GLY A CA  
1697 C C   . GLY A 223 ? 0.23216 0.29995 0.36438 0.06555  -0.01882 -0.00715 657 GLY A C   
1698 O O   . GLY A 223 ? 0.17889 0.25810 0.31009 0.06003  -0.01777 -0.00752 657 GLY A O   
1699 N N   . LYS A 224 ? 0.17403 0.23437 0.30644 0.06895  -0.01402 -0.01291 658 LYS A N   
1700 C CA  . LYS A 224 ? 0.15547 0.22181 0.28610 0.06598  -0.00719 -0.01955 658 LYS A CA  
1701 C C   . LYS A 224 ? 0.17089 0.23517 0.28899 0.05646  -0.00607 -0.01870 658 LYS A C   
1702 O O   . LYS A 224 ? 0.15527 0.22847 0.27247 0.05234  -0.00199 -0.02175 658 LYS A O   
1703 C CB  . LYS A 224 ? 0.18565 0.24197 0.31584 0.07032  -0.00276 -0.02584 658 LYS A CB  
1704 C CG  . LYS A 224 ? 0.16797 0.22550 0.31137 0.08068  -0.00298 -0.02817 658 LYS A CG  
1705 C CD  . LYS A 224 ? 0.21961 0.26135 0.36002 0.08438  -0.00011 -0.03370 658 LYS A CD  
1706 C CE  . LYS A 224 ? 0.22826 0.26899 0.37624 0.09264  0.00083  -0.03501 658 LYS A CE  
1707 N NZ  . LYS A 224 ? 0.41228 0.47007 0.56663 0.09424  0.00658  -0.03989 658 LYS A NZ  
1708 N N   . GLY A 225 ? 0.10876 0.16179 0.21749 0.05292  -0.00965 -0.01438 659 GLY A N   
1709 C CA  . GLY A 225 ? 0.10246 0.15234 0.19984 0.04497  -0.00872 -0.01373 659 GLY A CA  
1710 C C   . GLY A 225 ? 0.09631 0.15531 0.19263 0.03986  -0.01121 -0.01057 659 GLY A C   
1711 O O   . GLY A 225 ? 0.11131 0.16673 0.19856 0.03382  -0.01075 -0.01004 659 GLY A O   
1712 N N   . ARG A 226 ? 0.13509 0.20591 0.24060 0.04203  -0.01392 -0.00868 660 ARG A N   
1713 C CA  . ARG A 226 ? 0.10104 0.18035 0.20515 0.03644  -0.01656 -0.00617 660 ARG A CA  
1714 C C   . ARG A 226 ? 0.12273 0.20776 0.22473 0.03084  -0.01214 -0.00961 660 ARG A C   
1715 O O   . ARG A 226 ? 0.17502 0.26720 0.28299 0.03243  -0.00800 -0.01309 660 ARG A O   
1716 C CB  . ARG A 226 ? 0.15863 0.25065 0.27374 0.03981  -0.02073 -0.00332 660 ARG A CB  
1717 C CG  . ARG A 226 ? 0.20343 0.28949 0.32075 0.04535  -0.02584 0.00129  660 ARG A CG  
1718 C CD  . ARG A 226 ? 0.16779 0.26651 0.29377 0.04717  -0.03147 0.00570  660 ARG A CD  
1719 N NE  . ARG A 226 ? 0.21438 0.32969 0.34789 0.04489  -0.02990 0.00341  660 ARG A NE  
1720 C CZ  . ARG A 226 ? 0.20979 0.33401 0.34137 0.03843  -0.03268 0.00507  660 ARG A CZ  
1721 N NH1 . ARG A 226 ? 0.13978 0.25870 0.26203 0.03400  -0.03697 0.00856  660 ARG A NH1 
1722 N NH2 . ARG A 226 ? 0.12448 0.26360 0.26348 0.03599  -0.03102 0.00294  660 ARG A NH2 
1723 N N   . GLY A 227 ? 0.08855 0.17041 0.18203 0.02426  -0.01300 -0.00856 661 GLY A N   
1724 C CA  . GLY A 227 ? 0.07931 0.16232 0.16878 0.01862  -0.00929 -0.01095 661 GLY A CA  
1725 C C   . GLY A 227 ? 0.16183 0.23307 0.24233 0.01733  -0.00608 -0.01255 661 GLY A C   
1726 O O   . GLY A 227 ? 0.08732 0.15686 0.16251 0.01221  -0.00422 -0.01323 661 GLY A O   
1727 N N   . TYR A 228 ? 0.13087 0.19371 0.20970 0.02167  -0.00576 -0.01288 662 TYR A N   
1728 C CA  . TYR A 228 ? 0.15400 0.20726 0.22538 0.02063  -0.00267 -0.01470 662 TYR A CA  
1729 C C   . TYR A 228 ? 0.10915 0.15193 0.17177 0.01870  -0.00505 -0.01226 662 TYR A C   
1730 O O   . TYR A 228 ? 0.17558 0.21001 0.23286 0.01877  -0.00349 -0.01312 662 TYR A O   
1731 C CB  . TYR A 228 ? 0.14968 0.20064 0.22470 0.02589  -0.00018 -0.01767 662 TYR A CB  
1732 C CG  . TYR A 228 ? 0.16748 0.22970 0.24998 0.02725  0.00363  -0.02117 662 TYR A CG  
1733 C CD1 . TYR A 228 ? 0.12361 0.19707 0.21654 0.03045  0.00238  -0.02082 662 TYR A CD1 
1734 C CD2 . TYR A 228 ? 0.14911 0.21212 0.22826 0.02501  0.00843  -0.02460 662 TYR A CD2 
1735 C CE1 . TYR A 228 ? 0.23246 0.31801 0.33270 0.03151  0.00626  -0.02414 662 TYR A CE1 
1736 C CE2 . TYR A 228 ? 0.13955 0.21418 0.22496 0.02569  0.01229  -0.02779 662 TYR A CE2 
1737 C CZ  . TYR A 228 ? 0.15730 0.24337 0.25345 0.02899  0.01141  -0.02772 662 TYR A CZ  
1738 O OH  . TYR A 228 ? 0.43058 0.52994 0.53345 0.02952  0.01566  -0.03104 662 TYR A OH  
1739 N N   . ASN A 229 ? 0.09952 0.14362 0.16047 0.01659  -0.00867 -0.00950 663 ASN A N   
1740 C CA  . ASN A 229 ? 0.08181 0.11843 0.13428 0.01399  -0.01037 -0.00763 663 ASN A CA  
1741 C C   . ASN A 229 ? 0.11401 0.15461 0.16418 0.00944  -0.01145 -0.00757 663 ASN A C   
1742 O O   . ASN A 229 ? 0.09668 0.14401 0.15043 0.00896  -0.01435 -0.00643 663 ASN A O   
1743 C CB  . ASN A 229 ? 0.08640 0.11942 0.13833 0.01654  -0.01423 -0.00424 663 ASN A CB  
1744 C CG  . ASN A 229 ? 0.13083 0.15695 0.17376 0.01370  -0.01522 -0.00249 663 ASN A CG  
1745 O OD1 . ASN A 229 ? 0.22425 0.24290 0.26348 0.01415  -0.01404 -0.00235 663 ASN A OD1 
1746 N ND2 . ASN A 229 ? 0.08696 0.11624 0.12635 0.01050  -0.01730 -0.00146 663 ASN A ND2 
1747 N N   . VAL A 230 ? 0.09511 0.13154 0.13961 0.00615  -0.00934 -0.00886 664 VAL A N   
1748 C CA  . VAL A 230 ? 0.14234 0.18040 0.18459 0.00191  -0.00993 -0.00960 664 VAL A CA  
1749 C C   . VAL A 230 ? 0.07843 0.11018 0.11300 0.00057  -0.01072 -0.00931 664 VAL A C   
1750 O O   . VAL A 230 ? 0.07747 0.10357 0.10807 0.00058  -0.00854 -0.00975 664 VAL A O   
1751 C CB  . VAL A 230 ? 0.07537 0.11407 0.11854 -0.00065 -0.00683 -0.01122 664 VAL A CB  
1752 C CG1 . VAL A 230 ? 0.07676 0.11483 0.11760 -0.00504 -0.00777 -0.01201 664 VAL A CG1 
1753 C CG2 . VAL A 230 ? 0.17415 0.22103 0.22493 0.00037  -0.00549 -0.01171 664 VAL A CG2 
1754 N N   . ASN A 231 ? 0.08129 0.11520 0.11384 -0.00071 -0.01380 -0.00866 665 ASN A N   
1755 C CA  . ASN A 231 ? 0.17945 0.20944 0.20474 -0.00228 -0.01429 -0.00902 665 ASN A CA  
1756 C C   . ASN A 231 ? 0.12473 0.15466 0.14793 -0.00583 -0.01409 -0.01200 665 ASN A C   
1757 O O   . ASN A 231 ? 0.08634 0.12118 0.11215 -0.00801 -0.01601 -0.01275 665 ASN A O   
1758 C CB  . ASN A 231 ? 0.11098 0.14343 0.13398 -0.00187 -0.01777 -0.00643 665 ASN A CB  
1759 C CG  . ASN A 231 ? 0.08732 0.11571 0.10913 0.00080  -0.01776 -0.00351 665 ASN A CG  
1760 O OD1 . ASN A 231 ? 0.08527 0.10862 0.10598 0.00166  -0.01497 -0.00415 665 ASN A OD1 
1761 N ND2 . ASN A 231 ? 0.10040 0.13085 0.12228 0.00174  -0.02122 0.00003  665 ASN A ND2 
1762 N N   . ILE A 232 ? 0.09768 0.12206 0.11656 -0.00639 -0.01194 -0.01375 666 ILE A N   
1763 C CA  . ILE A 232 ? 0.08833 0.11037 0.10502 -0.00914 -0.01162 -0.01705 666 ILE A CA  
1764 C C   . ILE A 232 ? 0.12346 0.14395 0.13373 -0.00922 -0.01168 -0.01870 666 ILE A C   
1765 O O   . ILE A 232 ? 0.10646 0.12293 0.11443 -0.00775 -0.00938 -0.01929 666 ILE A O   
1766 C CB  . ILE A 232 ? 0.12033 0.13732 0.13875 -0.00928 -0.00895 -0.01771 666 ILE A CB  
1767 C CG1 . ILE A 232 ? 0.08408 0.10453 0.10833 -0.00958 -0.00850 -0.01594 666 ILE A CG1 
1768 C CG2 . ILE A 232 ? 0.09235 0.10505 0.10913 -0.01189 -0.00894 -0.02100 666 ILE A CG2 
1769 C CD1 . ILE A 232 ? 0.08345 0.10012 0.10894 -0.01029 -0.00609 -0.01553 666 ILE A CD1 
1770 N N   . PRO A 233 ? 0.09684 0.12168 0.10410 -0.01100 -0.01423 -0.01936 667 PRO A N   
1771 C CA  . PRO A 233 ? 0.11816 0.14337 0.11870 -0.01134 -0.01399 -0.02083 667 PRO A CA  
1772 C C   . PRO A 233 ? 0.10553 0.12836 0.10262 -0.01345 -0.01315 -0.02649 667 PRO A C   
1773 O O   . PRO A 233 ? 0.10897 0.13227 0.10715 -0.01626 -0.01476 -0.02886 667 PRO A O   
1774 C CB  . PRO A 233 ? 0.10175 0.13364 0.10061 -0.01242 -0.01757 -0.01784 667 PRO A CB  
1775 C CG  . PRO A 233 ? 0.11739 0.15281 0.12142 -0.01397 -0.02002 -0.01775 667 PRO A CG  
1776 C CD  . PRO A 233 ? 0.13132 0.16265 0.14141 -0.01261 -0.01763 -0.01797 667 PRO A CD  
1777 N N   . TRP A 234 ? 0.10757 0.12796 0.10086 -0.01214 -0.01060 -0.02899 668 TRP A N   
1778 C CA  . TRP A 234 ? 0.13788 0.15502 0.12822 -0.01316 -0.00932 -0.03522 668 TRP A CA  
1779 C C   . TRP A 234 ? 0.15973 0.18270 0.14286 -0.01519 -0.01002 -0.03801 668 TRP A C   
1780 O O   . TRP A 234 ? 0.11960 0.14781 0.09945 -0.01473 -0.00999 -0.03501 668 TRP A O   
1781 C CB  . TRP A 234 ? 0.15382 0.16537 0.14542 -0.00977 -0.00581 -0.03690 668 TRP A CB  
1782 C CG  . TRP A 234 ? 0.16166 0.16822 0.15921 -0.00792 -0.00500 -0.03363 668 TRP A CG  
1783 C CD1 . TRP A 234 ? 0.10266 0.10929 0.10212 -0.00520 -0.00347 -0.02998 668 TRP A CD1 
1784 C CD2 . TRP A 234 ? 0.11219 0.11366 0.11392 -0.00935 -0.00572 -0.03366 668 TRP A CD2 
1785 N NE1 . TRP A 234 ? 0.10863 0.11089 0.11274 -0.00472 -0.00319 -0.02787 668 TRP A NE1 
1786 C CE2 . TRP A 234 ? 0.12357 0.12272 0.12920 -0.00726 -0.00446 -0.02979 668 TRP A CE2 
1787 C CE3 . TRP A 234 ? 0.11479 0.11395 0.11708 -0.01286 -0.00741 -0.03643 668 TRP A CE3 
1788 C CZ2 . TRP A 234 ? 0.10367 0.09871 0.11338 -0.00853 -0.00466 -0.02828 668 TRP A CZ2 
1789 C CZ3 . TRP A 234 ? 0.14299 0.13761 0.14988 -0.01426 -0.00764 -0.03482 668 TRP A CZ3 
1790 C CH2 . TRP A 234 ? 0.10906 0.10189 0.11947 -0.01206 -0.00618 -0.03060 668 TRP A CH2 
1791 N N   . ASN A 235 ? 0.21289 0.23484 0.19309 -0.01795 -0.01065 -0.04382 669 ASN A N   
1792 C CA  . ASN A 235 ? 0.17827 0.20598 0.15063 -0.02040 -0.01098 -0.04779 669 ASN A CA  
1793 C C   . ASN A 235 ? 0.17924 0.20135 0.14920 -0.01989 -0.00808 -0.05630 669 ASN A C   
1794 O O   . ASN A 235 ? 0.21925 0.23269 0.19327 -0.01957 -0.00768 -0.05918 669 ASN A O   
1795 C CB  . ASN A 235 ? 0.14043 0.17416 0.11047 -0.02513 -0.01541 -0.04710 669 ASN A CB  
1796 C CG  . ASN A 235 ? 0.13692 0.17594 0.11057 -0.02475 -0.01851 -0.03877 669 ASN A CG  
1797 O OD1 . ASN A 235 ? 0.12993 0.17220 0.10208 -0.02301 -0.01826 -0.03408 669 ASN A OD1 
1798 N ND2 . ASN A 235 ? 0.13133 0.17114 0.11018 -0.02638 -0.02142 -0.03698 669 ASN A ND2 
1799 N N   . GLY A 236 ? 0.20406 0.23103 0.16763 -0.01970 -0.00592 -0.06021 670 GLY A N   
1800 C CA  . GLY A 236 ? 0.39118 0.41389 0.35187 -0.01914 -0.00314 -0.06956 670 GLY A CA  
1801 C C   . GLY A 236 ? 0.28221 0.29767 0.24793 -0.01346 0.00088  -0.07199 670 GLY A C   
1802 O O   . GLY A 236 ? 0.24998 0.25533 0.21890 -0.01233 0.00149  -0.07669 670 GLY A O   
1803 N N   . GLY A 237 ? 0.21237 0.23287 0.17907 -0.01006 0.00334  -0.06853 671 GLY A N   
1804 C CA  . GLY A 237 ? 0.27968 0.29665 0.25030 -0.00460 0.00733  -0.07181 671 GLY A CA  
1805 C C   . GLY A 237 ? 0.27802 0.28691 0.25718 -0.00102 0.00719  -0.06707 671 GLY A C   
1806 O O   . GLY A 237 ? 0.17812 0.18576 0.16017 -0.00244 0.00468  -0.06034 671 GLY A O   
1807 N N   . LYS A 238 ? 0.31116 0.31477 0.29449 0.00390  0.01000  -0.07100 672 LYS A N   
1808 C CA  . LYS A 238 ? 0.35348 0.35231 0.34442 0.00799  0.01038  -0.06602 672 LYS A CA  
1809 C C   . LYS A 238 ? 0.28520 0.27395 0.27997 0.00619  0.00743  -0.06261 672 LYS A C   
1810 O O   . LYS A 238 ? 0.35251 0.33305 0.34686 0.00435  0.00632  -0.06701 672 LYS A O   
1811 C CB  . LYS A 238 ? 0.21505 0.21098 0.21004 0.01406  0.01369  -0.07118 672 LYS A CB  
1812 N N   . MET A 239 ? 0.27470 0.26452 0.27292 0.00623  0.00626  -0.05495 673 MET A N   
1813 C CA  . MET A 239 ? 0.22391 0.20599 0.22632 0.00493  0.00415  -0.05088 673 MET A CA  
1814 C C   . MET A 239 ? 0.20382 0.18253 0.21194 0.00928  0.00516  -0.04722 673 MET A C   
1815 O O   . MET A 239 ? 0.19575 0.18016 0.20488 0.01283  0.00709  -0.04655 673 MET A O   
1816 C CB  . MET A 239 ? 0.18738 0.17443 0.18889 0.00111  0.00194  -0.04524 673 MET A CB  
1817 C CG  . MET A 239 ? 0.13549 0.12741 0.13198 -0.00306 0.00024  -0.04753 673 MET A CG  
1818 S SD  . MET A 239 ? 0.17723 0.16134 0.17303 -0.00695 -0.00158 -0.05308 673 MET A SD  
1819 C CE  . MET A 239 ? 0.14000 0.13356 0.12887 -0.01132 -0.00349 -0.05558 673 MET A CE  
1820 N N   . GLY A 240 ? 0.25807 0.22835 0.26988 0.00854  0.00364  -0.04439 674 GLY A N   
1821 C CA  . GLY A 240 ? 0.13914 0.10597 0.15611 0.01223  0.00394  -0.04025 674 GLY A CA  
1822 C C   . GLY A 240 ? 0.17027 0.13252 0.18965 0.00945  0.00195  -0.03424 674 GLY A C   
1823 O O   . GLY A 240 ? 0.23224 0.19705 0.24977 0.00499  0.00075  -0.03238 674 GLY A O   
1824 N N   . ASP A 241 ? 0.13688 0.09322 0.16059 0.01213  0.00156  -0.03097 675 ASP A N   
1825 C CA  . ASP A 241 ? 0.14991 0.10277 0.17540 0.00918  -0.00017 -0.02467 675 ASP A CA  
1826 C C   . ASP A 241 ? 0.20824 0.15557 0.23258 0.00355  -0.00170 -0.02537 675 ASP A C   
1827 O O   . ASP A 241 ? 0.14524 0.09636 0.16924 -0.00035 -0.00241 -0.02105 675 ASP A O   
1828 C CB  . ASP A 241 ? 0.19949 0.14522 0.22961 0.01278  -0.00091 -0.02119 675 ASP A CB  
1829 C CG  . ASP A 241 ? 0.19742 0.15055 0.22970 0.01756  0.00003  -0.01855 675 ASP A CG  
1830 O OD1 . ASP A 241 ? 0.14658 0.11004 0.17646 0.01701  0.00112  -0.01811 675 ASP A OD1 
1831 O OD2 . ASP A 241 ? 0.25953 0.20781 0.29628 0.02173  -0.00062 -0.01660 675 ASP A OD2 
1832 N N   . PRO A 242 ? 0.19867 0.13755 0.22264 0.00260  -0.00222 -0.03068 676 PRO A N   
1833 C CA  . PRO A 242 ? 0.20134 0.13607 0.22450 -0.00379 -0.00397 -0.03079 676 PRO A CA  
1834 C C   . PRO A 242 ? 0.14236 0.08762 0.16268 -0.00765 -0.00414 -0.03123 676 PRO A C   
1835 O O   . PRO A 242 ? 0.17596 0.12343 0.19714 -0.01235 -0.00524 -0.02780 676 PRO A O   
1836 C CB  . PRO A 242 ? 0.20274 0.12656 0.22540 -0.00370 -0.00436 -0.03778 676 PRO A CB  
1837 C CG  . PRO A 242 ? 0.24379 0.16957 0.26599 0.00274  -0.00221 -0.04263 676 PRO A CG  
1838 C CD  . PRO A 242 ? 0.15687 0.08871 0.18177 0.00709  -0.00130 -0.03670 676 PRO A CD  
1839 N N   . GLU A 243 ? 0.14550 0.09795 0.16279 -0.00572 -0.00312 -0.03499 677 GLU A N   
1840 C CA  . GLU A 243 ? 0.18905 0.15123 0.20403 -0.00878 -0.00377 -0.03475 677 GLU A CA  
1841 C C   . GLU A 243 ? 0.12573 0.09496 0.14240 -0.00872 -0.00349 -0.02854 677 GLU A C   
1842 O O   . GLU A 243 ? 0.19251 0.16672 0.20997 -0.01214 -0.00447 -0.02661 677 GLU A O   
1843 C CB  . GLU A 243 ? 0.14914 0.11714 0.16004 -0.00675 -0.00289 -0.03916 677 GLU A CB  
1844 C CG  . GLU A 243 ? 0.14072 0.10426 0.14855 -0.00823 -0.00325 -0.04648 677 GLU A CG  
1845 C CD  . GLU A 243 ? 0.23818 0.19218 0.24722 -0.00434 -0.00174 -0.05054 677 GLU A CD  
1846 O OE1 . GLU A 243 ? 0.24017 0.19378 0.25210 0.00040  -0.00025 -0.04770 677 GLU A OE1 
1847 O OE2 . GLU A 243 ? 0.18726 0.13424 0.19462 -0.00597 -0.00216 -0.05678 677 GLU A OE2 
1848 N N   . TYR A 244 ? 0.24484 0.21515 0.26232 -0.00484 -0.00214 -0.02575 678 TYR A N   
1849 C CA  . TYR A 244 ? 0.13768 0.11426 0.15599 -0.00492 -0.00173 -0.02080 678 TYR A CA  
1850 C C   . TYR A 244 ? 0.13131 0.10548 0.15217 -0.00789 -0.00224 -0.01670 678 TYR A C   
1851 O O   . TYR A 244 ? 0.10357 0.08368 0.12505 -0.00993 -0.00210 -0.01423 678 TYR A O   
1852 C CB  . TYR A 244 ? 0.11250 0.09145 0.13055 -0.00075 -0.00039 -0.01922 678 TYR A CB  
1853 C CG  . TYR A 244 ? 0.10010 0.08543 0.11528 0.00065  0.00025  -0.02136 678 TYR A CG  
1854 C CD1 . TYR A 244 ? 0.14458 0.12949 0.15761 0.00165  0.00059  -0.02616 678 TYR A CD1 
1855 C CD2 . TYR A 244 ? 0.09307 0.08459 0.10731 0.00056  0.00049  -0.01864 678 TYR A CD2 
1856 C CE1 . TYR A 244 ? 0.11740 0.10884 0.12718 0.00215  0.00110  -0.02740 678 TYR A CE1 
1857 C CE2 . TYR A 244 ? 0.09082 0.08733 0.10227 0.00120  0.00072  -0.01974 678 TYR A CE2 
1858 C CZ  . TYR A 244 ? 0.16031 0.15724 0.16940 0.00179  0.00099  -0.02372 678 TYR A CZ  
1859 O OH  . TYR A 244 ? 0.11802 0.12063 0.12372 0.00173  0.00118  -0.02415 678 TYR A OH  
1860 N N   . MET A 245 ? 0.12246 0.08801 0.14489 -0.00820 -0.00279 -0.01590 679 MET A N   
1861 C CA  . MET A 245 ? 0.11933 0.08260 0.14362 -0.01195 -0.00343 -0.01133 679 MET A CA  
1862 C C   . MET A 245 ? 0.13356 0.09894 0.15844 -0.01736 -0.00429 -0.01239 679 MET A C   
1863 O O   . MET A 245 ? 0.17342 0.14398 0.19955 -0.02068 -0.00401 -0.00891 679 MET A O   
1864 C CB  . MET A 245 ? 0.12992 0.08215 0.15587 -0.01112 -0.00438 -0.00965 679 MET A CB  
1865 C CG  . MET A 245 ? 0.23200 0.18382 0.25876 -0.00603 -0.00391 -0.00687 679 MET A CG  
1866 S SD  . MET A 245 ? 0.35566 0.31472 0.38206 -0.00763 -0.00360 0.00047  679 MET A SD  
1867 C CE  . MET A 245 ? 0.27597 0.22691 0.30379 -0.01271 -0.00535 0.00570  679 MET A CE  
1868 N N   . ALA A 246 ? 0.12522 0.08778 0.14923 -0.01855 -0.00529 -0.01740 680 ALA A N   
1869 C CA  . ALA A 246 ? 0.15168 0.11757 0.17664 -0.02406 -0.00653 -0.01843 680 ALA A CA  
1870 C C   . ALA A 246 ? 0.15441 0.13283 0.17988 -0.02396 -0.00609 -0.01781 680 ALA A C   
1871 O O   . ALA A 246 ? 0.18184 0.16646 0.20993 -0.02783 -0.00642 -0.01605 680 ALA A O   
1872 C CB  . ALA A 246 ? 0.13510 0.09522 0.15832 -0.02565 -0.00797 -0.02437 680 ALA A CB  
1873 N N   . ALA A 247 ? 0.12157 0.10400 0.14503 -0.01954 -0.00536 -0.01908 681 ALA A N   
1874 C CA  . ALA A 247 ? 0.11878 0.11135 0.14307 -0.01875 -0.00516 -0.01803 681 ALA A CA  
1875 C C   . ALA A 247 ? 0.14946 0.14613 0.17602 -0.01875 -0.00359 -0.01389 681 ALA A C   
1876 O O   . ALA A 247 ? 0.19768 0.20228 0.22691 -0.01988 -0.00342 -0.01301 681 ALA A O   
1877 C CB  . ALA A 247 ? 0.09908 0.09356 0.12030 -0.01457 -0.00485 -0.01957 681 ALA A CB  
1878 N N   . PHE A 248 ? 0.10691 0.09898 0.13255 -0.01739 -0.00244 -0.01148 682 PHE A N   
1879 C CA  . PHE A 248 ? 0.13419 0.13042 0.16094 -0.01822 -0.00095 -0.00778 682 PHE A CA  
1880 C C   . PHE A 248 ? 0.12082 0.11879 0.15020 -0.02350 -0.00106 -0.00587 682 PHE A C   
1881 O O   . PHE A 248 ? 0.17545 0.18145 0.20668 -0.02499 0.00032  -0.00439 682 PHE A O   
1882 C CB  . PHE A 248 ? 0.17397 0.16556 0.19880 -0.01608 -0.00028 -0.00518 682 PHE A CB  
1883 C CG  . PHE A 248 ? 0.13598 0.13133 0.15897 -0.01238 0.00078  -0.00524 682 PHE A CG  
1884 C CD1 . PHE A 248 ? 0.14828 0.14356 0.16988 -0.00930 0.00043  -0.00803 682 PHE A CD1 
1885 C CD2 . PHE A 248 ? 0.24354 0.24263 0.26572 -0.01263 0.00208  -0.00252 682 PHE A CD2 
1886 C CE1 . PHE A 248 ? 0.15729 0.15553 0.17717 -0.00676 0.00121  -0.00774 682 PHE A CE1 
1887 C CE2 . PHE A 248 ? 0.20040 0.20221 0.22065 -0.00994 0.00285  -0.00290 682 PHE A CE2 
1888 C CZ  . PHE A 248 ? 0.15486 0.15592 0.17420 -0.00712 0.00233  -0.00533 682 PHE A CZ  
1889 N N   . HIS A 249 ? 0.19072 0.18141 0.22040 -0.02658 -0.00257 -0.00617 683 HIS A N   
1890 C CA  . HIS A 249 ? 0.19127 0.18276 0.22322 -0.03261 -0.00284 -0.00362 683 HIS A CA  
1891 C C   . HIS A 249 ? 0.19033 0.19178 0.22562 -0.03562 -0.00309 -0.00534 683 HIS A C   
1892 O O   . HIS A 249 ? 0.17076 0.18002 0.20876 -0.03921 -0.00192 -0.00290 683 HIS A O   
1893 C CB  . HIS A 249 ? 0.12321 0.10233 0.15458 -0.03523 -0.00474 -0.00367 683 HIS A CB  
1894 C CG  . HIS A 249 ? 0.22385 0.20247 0.25731 -0.04249 -0.00546 -0.00078 683 HIS A CG  
1895 N ND1 . HIS A 249 ? 0.20958 0.18992 0.24329 -0.04564 -0.00448 0.00495  683 HIS A ND1 
1896 C CD2 . HIS A 249 ? 0.20843 0.18545 0.24353 -0.04793 -0.00716 -0.00265 683 HIS A CD2 
1897 C CE1 . HIS A 249 ? 0.18155 0.16138 0.21713 -0.05278 -0.00541 0.00683  683 HIS A CE1 
1898 N NE2 . HIS A 249 ? 0.21093 0.18859 0.24761 -0.05435 -0.00711 0.00218  683 HIS A NE2 
1899 N N   . HIS A 250 ? 0.11553 0.11796 0.15083 -0.03431 -0.00463 -0.00938 684 HIS A N   
1900 C CA  . HIS A 250 ? 0.11610 0.12833 0.15514 -0.03715 -0.00564 -0.01074 684 HIS A CA  
1901 C C   . HIS A 250 ? 0.09844 0.12142 0.13970 -0.03294 -0.00467 -0.01103 684 HIS A C   
1902 O O   . HIS A 250 ? 0.09652 0.13000 0.14258 -0.03471 -0.00493 -0.01098 684 HIS A O   
1903 C CB  . HIS A 250 ? 0.16304 0.17138 0.20068 -0.03883 -0.00841 -0.01474 684 HIS A CB  
1904 C CG  . HIS A 250 ? 0.17506 0.17257 0.21139 -0.04370 -0.00968 -0.01539 684 HIS A CG  
1905 N ND1 . HIS A 250 ? 0.23128 0.23085 0.27056 -0.05084 -0.01092 -0.01460 684 HIS A ND1 
1906 C CD2 . HIS A 250 ? 0.15316 0.13731 0.18600 -0.04238 -0.00997 -0.01683 684 HIS A CD2 
1907 C CE1 . HIS A 250 ? 0.16031 0.14680 0.19746 -0.05405 -0.01211 -0.01548 684 HIS A CE1 
1908 N NE2 . HIS A 250 ? 0.14026 0.11708 0.17376 -0.04855 -0.01151 -0.01697 684 HIS A NE2 
1909 N N   . LEU A 251 ? 0.09411 0.11478 0.13252 -0.02748 -0.00369 -0.01129 685 LEU A N   
1910 C CA  . LEU A 251 ? 0.08782 0.11604 0.12797 -0.02331 -0.00340 -0.01189 685 LEU A CA  
1911 C C   . LEU A 251 ? 0.09948 0.12861 0.13885 -0.02000 -0.00072 -0.01046 685 LEU A C   
1912 O O   . LEU A 251 ? 0.15668 0.19381 0.19973 -0.01974 0.00096  -0.00996 685 LEU A O   
1913 C CB  . LEU A 251 ? 0.08753 0.11267 0.12449 -0.02044 -0.00541 -0.01401 685 LEU A CB  
1914 C CG  . LEU A 251 ? 0.11426 0.14031 0.15126 -0.02357 -0.00832 -0.01621 685 LEU A CG  
1915 C CD1 . LEU A 251 ? 0.13606 0.15639 0.16752 -0.02153 -0.00951 -0.01852 685 LEU A CD1 
1916 C CD2 . LEU A 251 ? 0.11578 0.15319 0.15797 -0.02373 -0.00992 -0.01580 685 LEU A CD2 
1917 N N   . VAL A 252 ? 0.13721 0.15890 0.17196 -0.01754 -0.00025 -0.01019 686 VAL A N   
1918 C CA  . VAL A 252 ? 0.15481 0.17737 0.18810 -0.01441 0.00171  -0.00946 686 VAL A CA  
1919 C C   . VAL A 252 ? 0.14676 0.17355 0.18125 -0.01668 0.00411  -0.00769 686 VAL A C   
1920 O O   . VAL A 252 ? 0.11144 0.14404 0.14734 -0.01504 0.00598  -0.00836 686 VAL A O   
1921 C CB  . VAL A 252 ? 0.13835 0.15333 0.16691 -0.01225 0.00153  -0.00918 686 VAL A CB  
1922 C CG1 . VAL A 252 ? 0.07774 0.09376 0.10449 -0.01010 0.00328  -0.00842 686 VAL A CG1 
1923 C CG2 . VAL A 252 ? 0.22384 0.23661 0.25080 -0.01024 -0.00032 -0.01113 686 VAL A CG2 
1924 N N   . MET A 253 ? 0.12433 0.14822 0.15811 -0.02062 0.00412  -0.00549 687 MET A N   
1925 C CA  . MET A 253 ? 0.15446 0.18254 0.18813 -0.02355 0.00632  -0.00300 687 MET A CA  
1926 C C   . MET A 253 ? 0.22185 0.26035 0.26042 -0.02656 0.00765  -0.00332 687 MET A C   
1927 O O   . MET A 253 ? 0.13414 0.18002 0.17315 -0.02718 0.01040  -0.00301 687 MET A O   
1928 C CB  . MET A 253 ? 0.15072 0.17133 0.18178 -0.02680 0.00544  0.00059  687 MET A CB  
1929 C CG  . MET A 253 ? 0.19112 0.20426 0.21816 -0.02353 0.00479  0.00155  687 MET A CG  
1930 S SD  . MET A 253 ? 0.23417 0.25263 0.25852 -0.02043 0.00694  0.00086  687 MET A SD  
1931 C CE  . MET A 253 ? 0.09773 0.12322 0.12111 -0.02526 0.00919  0.00412  687 MET A CE  
1932 N N   . PRO A 254 ? 0.16342 0.20393 0.20578 -0.02883 0.00592  -0.00411 688 PRO A N   
1933 C CA  . PRO A 254 ? 0.13038 0.18337 0.17867 -0.03098 0.00724  -0.00467 688 PRO A CA  
1934 C C   . PRO A 254 ? 0.12158 0.18239 0.17321 -0.02559 0.00869  -0.00749 688 PRO A C   
1935 O O   . PRO A 254 ? 0.11428 0.18538 0.16944 -0.02584 0.01156  -0.00807 688 PRO A O   
1936 C CB  . PRO A 254 ? 0.11254 0.16511 0.16373 -0.03420 0.00423  -0.00521 688 PRO A CB  
1937 C CG  . PRO A 254 ? 0.11974 0.15899 0.16596 -0.03605 0.00232  -0.00409 688 PRO A CG  
1938 C CD  . PRO A 254 ? 0.12150 0.15383 0.16297 -0.03077 0.00293  -0.00436 688 PRO A CD  
1939 N N   . ILE A 255 ? 0.09344 0.14952 0.14408 -0.02069 0.00684  -0.00928 689 ILE A N   
1940 C CA  . ILE A 255 ? 0.07622 0.13769 0.13029 -0.01534 0.00763  -0.01154 689 ILE A CA  
1941 C C   . ILE A 255 ? 0.15975 0.22054 0.21087 -0.01308 0.01082  -0.01242 689 ILE A C   
1942 O O   . ILE A 255 ? 0.09447 0.16271 0.14948 -0.01048 0.01318  -0.01460 689 ILE A O   
1943 C CB  . ILE A 255 ? 0.10793 0.16380 0.16091 -0.01164 0.00440  -0.01225 689 ILE A CB  
1944 C CG1 . ILE A 255 ? 0.23534 0.29379 0.29107 -0.01427 0.00120  -0.01198 689 ILE A CG1 
1945 C CG2 . ILE A 255 ? 0.08091 0.13993 0.13714 -0.00594 0.00482  -0.01384 689 ILE A CG2 
1946 C CD1 . ILE A 255 ? 0.09303 0.14654 0.14626 -0.01175 -0.00207 -0.01236 689 ILE A CD1 
1947 N N   . ALA A 256 ? 0.15089 0.20312 0.19532 -0.01392 0.01089  -0.01108 690 ALA A N   
1948 C CA  . ALA A 256 ? 0.07724 0.12896 0.11806 -0.01250 0.01347  -0.01200 690 ALA A CA  
1949 C C   . ALA A 256 ? 0.08289 0.14367 0.12465 -0.01575 0.01693  -0.01193 690 ALA A C   
1950 O O   . ALA A 256 ? 0.08391 0.14925 0.12561 -0.01382 0.01979  -0.01469 690 ALA A O   
1951 C CB  . ALA A 256 ? 0.07780 0.12007 0.11190 -0.01313 0.01235  -0.00998 690 ALA A CB  
1952 N N   . ARG A 257 ? 0.09209 0.15556 0.13449 -0.02103 0.01681  -0.00897 691 ARG A N   
1953 C CA  . ARG A 257 ? 0.08472 0.15820 0.12779 -0.02504 0.02018  -0.00829 691 ARG A CA  
1954 C C   . ARG A 257 ? 0.13982 0.22588 0.19034 -0.02295 0.02262  -0.01188 691 ARG A C   
1955 O O   . ARG A 257 ? 0.15754 0.25208 0.20822 -0.02281 0.02653  -0.01414 691 ARG A O   
1956 C CB  . ARG A 257 ? 0.13762 0.21039 0.18003 -0.03175 0.01905  -0.00363 691 ARG A CB  
1957 C CG  . ARG A 257 ? 0.15870 0.22231 0.19402 -0.03426 0.01795  0.00047  691 ARG A CG  
1958 C CD  . ARG A 257 ? 0.10208 0.16516 0.13709 -0.04124 0.01710  0.00552  691 ARG A CD  
1959 N NE  . ARG A 257 ? 0.15909 0.21503 0.19691 -0.04223 0.01377  0.00603  691 ARG A NE  
1960 C CZ  . ARG A 257 ? 0.31164 0.35468 0.34662 -0.04159 0.01075  0.00773  691 ARG A CZ  
1961 N NH1 . ARG A 257 ? 0.25690 0.29320 0.28690 -0.03978 0.01032  0.00981  691 ARG A NH1 
1962 N NH2 . ARG A 257 ? 0.27031 0.30769 0.30770 -0.04278 0.00812  0.00704  691 ARG A NH2 
1963 N N   . GLU A 258 ? 0.10583 0.19410 0.16276 -0.02121 0.02040  -0.01263 692 GLU A N   
1964 C CA  . GLU A 258 ? 0.08025 0.18118 0.14567 -0.01821 0.02229  -0.01581 692 GLU A CA  
1965 C C   . GLU A 258 ? 0.09669 0.19621 0.16270 -0.01104 0.02379  -0.02009 692 GLU A C   
1966 O O   . GLU A 258 ? 0.13527 0.24517 0.20676 -0.00824 0.02709  -0.02360 692 GLU A O   
1967 C CB  . GLU A 258 ? 0.08320 0.18696 0.15524 -0.01802 0.01876  -0.01508 692 GLU A CB  
1968 C CG  . GLU A 258 ? 0.08745 0.20711 0.16994 -0.01585 0.02040  -0.01732 692 GLU A CG  
1969 C CD  . GLU A 258 ? 0.10345 0.22783 0.19229 -0.01727 0.01649  -0.01586 692 GLU A CD  
1970 O OE1 . GLU A 258 ? 0.13303 0.24895 0.21759 -0.02142 0.01308  -0.01338 692 GLU A OE1 
1971 O OE2 . GLU A 258 ? 0.12481 0.26180 0.22314 -0.01413 0.01677  -0.01744 692 GLU A OE2 
1972 N N   . PHE A 259 ? 0.15238 0.23918 0.21299 -0.00814 0.02154  -0.02004 693 PHE A N   
1973 C CA  . PHE A 259 ? 0.11810 0.20129 0.17853 -0.00213 0.02252  -0.02378 693 PHE A CA  
1974 C C   . PHE A 259 ? 0.08330 0.16770 0.13850 -0.00317 0.02661  -0.02629 693 PHE A C   
1975 O O   . PHE A 259 ? 0.08615 0.17164 0.14289 0.00123  0.02890  -0.03089 693 PHE A O   
1976 C CB  . PHE A 259 ? 0.07831 0.14837 0.13446 0.00013  0.01866  -0.02236 693 PHE A CB  
1977 C CG  . PHE A 259 ? 0.08056 0.14473 0.13584 0.00538  0.01902  -0.02545 693 PHE A CG  
1978 C CD1 . PHE A 259 ? 0.08218 0.14941 0.14484 0.01100  0.01879  -0.02789 693 PHE A CD1 
1979 C CD2 . PHE A 259 ? 0.10940 0.16468 0.15684 0.00461  0.01923  -0.02567 693 PHE A CD2 
1980 C CE1 . PHE A 259 ? 0.08605 0.14596 0.14796 0.01568  0.01885  -0.03060 693 PHE A CE1 
1981 C CE2 . PHE A 259 ? 0.08530 0.13425 0.13170 0.00860  0.01935  -0.02855 693 PHE A CE2 
1982 C CZ  . PHE A 259 ? 0.08779 0.13817 0.14124 0.01409  0.01917  -0.03105 693 PHE A CZ  
1983 N N   . ALA A 260 ? 0.08423 0.16828 0.13318 -0.00900 0.02738  -0.02335 694 ALA A N   
1984 C CA  . ALA A 260 ? 0.10080 0.18672 0.14338 -0.01123 0.03074  -0.02485 694 ALA A CA  
1985 C C   . ALA A 260 ? 0.08979 0.16659 0.12764 -0.00751 0.03046  -0.02799 694 ALA A C   
1986 O O   . ALA A 260 ? 0.16942 0.24947 0.20731 -0.00506 0.03367  -0.03323 694 ALA A O   
1987 C CB  . ALA A 260 ? 0.09147 0.19185 0.13806 -0.01183 0.03562  -0.02837 694 ALA A CB  
1988 N N   . PRO A 261 ? 0.08756 0.15317 0.12132 -0.00727 0.02684  -0.02524 695 PRO A N   
1989 C CA  . PRO A 261 ? 0.18208 0.23942 0.21147 -0.00465 0.02636  -0.02782 695 PRO A CA  
1990 C C   . PRO A 261 ? 0.16531 0.22528 0.18776 -0.00784 0.02919  -0.02963 695 PRO A C   
1991 O O   . PRO A 261 ? 0.10962 0.17431 0.12838 -0.01278 0.02994  -0.02641 695 PRO A O   
1992 C CB  . PRO A 261 ? 0.11331 0.16109 0.13975 -0.00520 0.02220  -0.02352 695 PRO A CB  
1993 C CG  . PRO A 261 ? 0.08436 0.13484 0.11009 -0.00958 0.02146  -0.01892 695 PRO A CG  
1994 C CD  . PRO A 261 ? 0.08456 0.14505 0.11636 -0.01036 0.02352  -0.01976 695 PRO A CD  
1995 N N   . GLU A 262 ? 0.17546 0.23226 0.19597 -0.00526 0.03060  -0.03479 696 GLU A N   
1996 C CA  . GLU A 262 ? 0.20958 0.26758 0.22217 -0.00860 0.03266  -0.03701 696 GLU A CA  
1997 C C   . GLU A 262 ? 0.18417 0.23321 0.19037 -0.01043 0.02938  -0.03419 696 GLU A C   
1998 O O   . GLU A 262 ? 0.22817 0.27909 0.22723 -0.01446 0.03000  -0.03401 696 GLU A O   
1999 C CB  . GLU A 262 ? 0.24151 0.30066 0.25488 -0.00536 0.03617  -0.04512 696 GLU A CB  
2000 C CG  . GLU A 262 ? 0.11301 0.18384 0.13265 -0.00359 0.04038  -0.04885 696 GLU A CG  
2001 C CD  . GLU A 262 ? 0.20185 0.27152 0.22456 0.00176  0.04335  -0.05734 696 GLU A CD  
2002 O OE1 . GLU A 262 ? 0.11956 0.18224 0.14880 0.00755  0.04133  -0.05833 696 GLU A OE1 
2003 O OE2 . GLU A 262 ? 0.20879 0.28411 0.22713 0.00015  0.04755  -0.06303 696 GLU A OE2 
2004 N N   . LEU A 263 ? 0.17418 0.21481 0.18280 -0.00782 0.02589  -0.03185 697 LEU A N   
2005 C CA  . LEU A 263 ? 0.11193 0.14536 0.11572 -0.00930 0.02286  -0.02908 697 LEU A CA  
2006 C C   . LEU A 263 ? 0.16921 0.19791 0.17670 -0.00746 0.01955  -0.02476 697 LEU A C   
2007 O O   . LEU A 263 ? 0.15710 0.18407 0.17003 -0.00389 0.01896  -0.02571 697 LEU A O   
2008 C CB  . LEU A 263 ? 0.11874 0.14556 0.11985 -0.00804 0.02290  -0.03367 697 LEU A CB  
2009 C CG  . LEU A 263 ? 0.15572 0.17604 0.15269 -0.00983 0.01969  -0.03077 697 LEU A CG  
2010 C CD1 . LEU A 263 ? 0.18221 0.20718 0.17265 -0.01482 0.01959  -0.02861 697 LEU A CD1 
2011 C CD2 . LEU A 263 ? 0.10880 0.12080 0.10487 -0.00833 0.01914  -0.03474 697 LEU A CD2 
2012 N N   . VAL A 264 ? 0.20524 0.23239 0.20982 -0.00976 0.01735  -0.02017 698 VAL A N   
2013 C CA  . VAL A 264 ? 0.14969 0.17297 0.15689 -0.00839 0.01458  -0.01661 698 VAL A CA  
2014 C C   . VAL A 264 ? 0.13407 0.15196 0.13824 -0.00833 0.01249  -0.01566 698 VAL A C   
2015 O O   . VAL A 264 ? 0.08659 0.10544 0.08652 -0.01086 0.01213  -0.01431 698 VAL A O   
2016 C CB  . VAL A 264 ? 0.13366 0.15956 0.14117 -0.01062 0.01391  -0.01228 698 VAL A CB  
2017 C CG1 . VAL A 264 ? 0.12104 0.14257 0.13115 -0.00894 0.01141  -0.00998 698 VAL A CG1 
2018 C CG2 . VAL A 264 ? 0.09018 0.12243 0.10027 -0.01196 0.01610  -0.01278 698 VAL A CG2 
2019 N N   . LEU A 265 ? 0.18732 0.20053 0.19369 -0.00580 0.01097  -0.01598 699 LEU A N   
2020 C CA  . LEU A 265 ? 0.08853 0.09762 0.09265 -0.00609 0.00897  -0.01444 699 LEU A CA  
2021 C C   . LEU A 265 ? 0.13506 0.14372 0.14127 -0.00499 0.00727  -0.01153 699 LEU A C   
2022 O O   . LEU A 265 ? 0.13437 0.14297 0.14399 -0.00319 0.00692  -0.01176 699 LEU A O   
2023 C CB  . LEU A 265 ? 0.08716 0.09084 0.09128 -0.00473 0.00847  -0.01677 699 LEU A CB  
2024 C CG  . LEU A 265 ? 0.09384 0.09608 0.09661 -0.00490 0.01033  -0.02118 699 LEU A CG  
2025 C CD1 . LEU A 265 ? 0.09824 0.09267 0.10093 -0.00374 0.00906  -0.02260 699 LEU A CD1 
2026 C CD2 . LEU A 265 ? 0.09542 0.10078 0.09302 -0.00869 0.01134  -0.02183 699 LEU A CD2 
2027 N N   . VAL A 266 ? 0.13263 0.14168 0.13701 -0.00603 0.00623  -0.00913 700 VAL A N   
2028 C CA  . VAL A 266 ? 0.07559 0.08434 0.08162 -0.00481 0.00503  -0.00727 700 VAL A CA  
2029 C C   . VAL A 266 ? 0.13269 0.13990 0.13731 -0.00468 0.00391  -0.00683 700 VAL A C   
2030 O O   . VAL A 266 ? 0.09432 0.10291 0.09690 -0.00615 0.00365  -0.00581 700 VAL A O   
2031 C CB  . VAL A 266 ? 0.11170 0.12252 0.11788 -0.00536 0.00486  -0.00488 700 VAL A CB  
2032 C CG1 . VAL A 266 ? 0.08491 0.09443 0.09320 -0.00357 0.00400  -0.00428 700 VAL A CG1 
2033 C CG2 . VAL A 266 ? 0.11158 0.12419 0.11820 -0.00669 0.00589  -0.00444 700 VAL A CG2 
2034 N N   . SER A 267 ? 0.08833 0.09359 0.09397 -0.00337 0.00309  -0.00722 701 SER A N   
2035 C CA  . SER A 267 ? 0.09873 0.10366 0.10281 -0.00370 0.00203  -0.00608 701 SER A CA  
2036 C C   . SER A 267 ? 0.11598 0.12399 0.12064 -0.00304 0.00216  -0.00532 701 SER A C   
2037 O O   . SER A 267 ? 0.08173 0.08990 0.08733 -0.00184 0.00183  -0.00587 701 SER A O   
2038 C CB  . SER A 267 ? 0.15967 0.16217 0.16423 -0.00276 0.00080  -0.00608 701 SER A CB  
2039 O OG  . SER A 267 ? 0.17080 0.16932 0.17473 -0.00316 0.00041  -0.00642 701 SER A OG  
2040 N N   . ALA A 268 ? 0.09131 0.10198 0.09559 -0.00374 0.00256  -0.00427 702 ALA A N   
2041 C CA  . ALA A 268 ? 0.09885 0.11208 0.10494 -0.00223 0.00279  -0.00365 702 ALA A CA  
2042 C C   . ALA A 268 ? 0.10172 0.11863 0.10738 -0.00202 0.00284  -0.00332 702 ALA A C   
2043 O O   . ALA A 268 ? 0.07319 0.09437 0.07910 -0.00267 0.00290  -0.00197 702 ALA A O   
2044 C CB  . ALA A 268 ? 0.07321 0.08828 0.07992 -0.00272 0.00284  -0.00201 702 ALA A CB  
2045 N N   . GLY A 269 ? 0.07389 0.09029 0.07884 -0.00142 0.00280  -0.00452 703 GLY A N   
2046 C CA  . GLY A 269 ? 0.11001 0.13105 0.11481 -0.00077 0.00345  -0.00491 703 GLY A CA  
2047 C C   . GLY A 269 ? 0.11835 0.14021 0.12622 0.00233  0.00426  -0.00639 703 GLY A C   
2048 O O   . GLY A 269 ? 0.11436 0.13178 0.12364 0.00349  0.00399  -0.00728 703 GLY A O   
2049 N N   . PHE A 270 ? 0.14939 0.17703 0.15876 0.00368  0.00526  -0.00658 704 PHE A N   
2050 C CA  . PHE A 270 ? 0.10314 0.13104 0.11621 0.00749  0.00607  -0.00833 704 PHE A CA  
2051 C C   . PHE A 270 ? 0.12673 0.15859 0.13924 0.00897  0.00768  -0.01169 704 PHE A C   
2052 O O   . PHE A 270 ? 0.18540 0.22032 0.20143 0.01248  0.00896  -0.01352 704 PHE A O   
2053 C CB  . PHE A 270 ? 0.09230 0.12429 0.10924 0.00903  0.00588  -0.00584 704 PHE A CB  
2054 C CG  . PHE A 270 ? 0.11888 0.14731 0.13572 0.00749  0.00437  -0.00290 704 PHE A CG  
2055 C CD1 . PHE A 270 ? 0.10639 0.12838 0.12453 0.00868  0.00372  -0.00271 704 PHE A CD1 
2056 C CD2 . PHE A 270 ? 0.07412 0.10569 0.08904 0.00425  0.00366  -0.00053 704 PHE A CD2 
2057 C CE1 . PHE A 270 ? 0.08504 0.10507 0.10247 0.00674  0.00264  0.00006  704 PHE A CE1 
2058 C CE2 . PHE A 270 ? 0.07393 0.10306 0.08795 0.00257  0.00260  0.00148  704 PHE A CE2 
2059 C CZ  . PHE A 270 ? 0.07532 0.09928 0.09051 0.00384  0.00220  0.00190  704 PHE A CZ  
2060 N N   . ASP A 271 ? 0.15601 0.18817 0.16413 0.00642  0.00761  -0.01255 705 ASP A N   
2061 C CA  . ASP A 271 ? 0.13344 0.16984 0.13947 0.00690  0.00911  -0.01592 705 ASP A CA  
2062 C C   . ASP A 271 ? 0.24163 0.27234 0.24698 0.00827  0.00899  -0.01997 705 ASP A C   
2063 O O   . ASP A 271 ? 0.17630 0.20993 0.17841 0.00775  0.00989  -0.02318 705 ASP A O   
2064 C CB  . ASP A 271 ? 0.09576 0.13621 0.09675 0.00281  0.00872  -0.01401 705 ASP A CB  
2065 C CG  . ASP A 271 ? 0.11474 0.14896 0.11352 0.00010  0.00627  -0.01107 705 ASP A CG  
2066 O OD1 . ASP A 271 ? 0.08632 0.11413 0.08699 0.00113  0.00522  -0.01124 705 ASP A OD1 
2067 O OD2 . ASP A 271 ? 0.12220 0.15817 0.11756 -0.00309 0.00543  -0.00848 705 ASP A OD2 
2068 N N   . ALA A 272 ? 0.13802 0.16117 0.14591 0.00934  0.00783  -0.01984 706 ALA A N   
2069 C CA  . ALA A 272 ? 0.12838 0.14569 0.13679 0.01071  0.00779  -0.02389 706 ALA A CA  
2070 C C   . ALA A 272 ? 0.19217 0.20681 0.20556 0.01499  0.00880  -0.02556 706 ALA A C   
2071 O O   . ALA A 272 ? 0.17170 0.17936 0.18620 0.01620  0.00857  -0.02870 706 ALA A O   
2072 C CB  . ALA A 272 ? 0.11310 0.12384 0.12121 0.00843  0.00571  -0.02250 706 ALA A CB  
2073 N N   . ALA A 273 ? 0.19774 0.21763 0.21445 0.01723  0.00964  -0.02333 707 ALA A N   
2074 C CA  . ALA A 273 ? 0.13044 0.14879 0.15291 0.02211  0.01030  -0.02425 707 ALA A CA  
2075 C C   . ALA A 273 ? 0.15359 0.17637 0.17695 0.02558  0.01298  -0.03008 707 ALA A C   
2076 O O   . ALA A 273 ? 0.10362 0.13409 0.12314 0.02379  0.01458  -0.03209 707 ALA A O   
2077 C CB  . ALA A 273 ? 0.09705 0.12078 0.12325 0.02306  0.00972  -0.01913 707 ALA A CB  
2078 N N   . ARG A 274 ? 0.14769 0.16546 0.17618 0.03058  0.01348  -0.03275 708 ARG A N   
2079 C CA  . ARG A 274 ? 0.13448 0.15631 0.16497 0.03501  0.01645  -0.03914 708 ARG A CA  
2080 C C   . ARG A 274 ? 0.21189 0.24839 0.24441 0.03622  0.01856  -0.03794 708 ARG A C   
2081 O O   . ARG A 274 ? 0.16771 0.20910 0.20325 0.03589  0.01736  -0.03211 708 ARG A O   
2082 C CB  . ARG A 274 ? 0.15043 0.16321 0.18763 0.04099  0.01621  -0.04128 708 ARG A CB  
2083 C CG  . ARG A 274 ? 0.40359 0.41459 0.44677 0.04300  0.01380  -0.03413 708 ARG A CG  
2084 C CD  . ARG A 274 ? 0.47548 0.47388 0.52427 0.04764  0.01241  -0.03466 708 ARG A CD  
2085 N NE  . ARG A 274 ? 0.62222 0.62306 0.67808 0.05138  0.01065  -0.02832 708 ARG A NE  
2086 C CZ  . ARG A 274 ? 0.42411 0.41447 0.48421 0.05351  0.00791  -0.02439 708 ARG A CZ  
2087 N NH1 . ARG A 274 ? 0.41993 0.39589 0.47813 0.05191  0.00668  -0.02610 708 ARG A NH1 
2088 N NH2 . ARG A 274 ? 0.58245 0.57726 0.64875 0.05681  0.00607  -0.01813 708 ARG A NH2 
2089 N N   . GLY A 275 ? 0.24614 0.29052 0.27651 0.03693  0.02175  -0.04358 709 GLY A N   
2090 C CA  . GLY A 275 ? 0.15552 0.21530 0.18753 0.03735  0.02421  -0.04289 709 GLY A CA  
2091 C C   . GLY A 275 ? 0.12488 0.19215 0.15008 0.03035  0.02384  -0.03908 709 GLY A C   
2092 O O   . GLY A 275 ? 0.13574 0.21628 0.16160 0.02947  0.02589  -0.03821 709 GLY A O   
2093 N N   . ASP A 276 ? 0.21704 0.27574 0.23655 0.02560  0.02112  -0.03653 710 ASP A N   
2094 C CA  . ASP A 276 ? 0.14411 0.20747 0.15746 0.01918  0.02010  -0.03226 710 ASP A CA  
2095 C C   . ASP A 276 ? 0.17632 0.24446 0.18278 0.01644  0.02179  -0.03621 710 ASP A C   
2096 O O   . ASP A 276 ? 0.17249 0.23364 0.17550 0.01620  0.02121  -0.04007 710 ASP A O   
2097 C CB  . ASP A 276 ? 0.11481 0.16923 0.12631 0.01581  0.01657  -0.02717 710 ASP A CB  
2098 C CG  . ASP A 276 ? 0.12637 0.18505 0.13385 0.01039  0.01540  -0.02208 710 ASP A CG  
2099 O OD1 . ASP A 276 ? 0.15110 0.21288 0.15290 0.00698  0.01565  -0.02246 710 ASP A OD1 
2100 O OD2 . ASP A 276 ? 0.14844 0.20696 0.15824 0.00942  0.01407  -0.01775 710 ASP A OD2 
2101 N N   . PRO A 277 ? 0.16350 0.24384 0.16750 0.01357  0.02358  -0.03481 711 PRO A N   
2102 C CA  . PRO A 277 ? 0.12291 0.21011 0.11957 0.01024  0.02530  -0.03779 711 PRO A CA  
2103 C C   . PRO A 277 ? 0.28856 0.37019 0.27784 0.00446  0.02194  -0.03386 711 PRO A C   
2104 O O   . PRO A 277 ? 0.15841 0.24255 0.14097 0.00177  0.02221  -0.03635 711 PRO A O   
2105 C CB  . PRO A 277 ? 0.16461 0.26706 0.16282 0.00918  0.02818  -0.03627 711 PRO A CB  
2106 C CG  . PRO A 277 ? 0.11808 0.22189 0.12518 0.01280  0.02804  -0.03361 711 PRO A CG  
2107 C CD  . PRO A 277 ? 0.19100 0.28061 0.19876 0.01257  0.02404  -0.03003 711 PRO A CD  
2108 N N   . LEU A 278 ? 0.17201 0.24647 0.16257 0.00272  0.01871  -0.02795 712 LEU A N   
2109 C CA  . LEU A 278 ? 0.18330 0.25261 0.16827 -0.00194 0.01538  -0.02384 712 LEU A CA  
2110 C C   . LEU A 278 ? 0.30338 0.36103 0.28958 -0.00026 0.01295  -0.02520 712 LEU A C   
2111 O O   . LEU A 278 ? 0.33754 0.38988 0.32201 -0.00278 0.00993  -0.02119 712 LEU A O   
2112 C CB  . LEU A 278 ? 0.21344 0.28301 0.19852 -0.00540 0.01364  -0.01692 712 LEU A CB  
2113 C CG  . LEU A 278 ? 0.18894 0.26946 0.17040 -0.00976 0.01497  -0.01403 712 LEU A CG  
2114 C CD1 . LEU A 278 ? 0.16413 0.24881 0.15001 -0.01044 0.01558  -0.01072 712 LEU A CD1 
2115 C CD2 . LEU A 278 ? 0.14683 0.22489 0.12171 -0.01501 0.01206  -0.00920 712 LEU A CD2 
2116 N N   . GLY A 279 ? 0.15906 0.21291 0.14873 0.00387  0.01421  -0.03044 713 GLY A N   
2117 C CA  . GLY A 279 ? 0.16586 0.20902 0.15715 0.00479  0.01198  -0.03134 713 GLY A CA  
2118 C C   . GLY A 279 ? 0.21121 0.25164 0.20157 0.00654  0.01304  -0.03832 713 GLY A C   
2119 O O   . GLY A 279 ? 0.20822 0.24448 0.19543 0.00423  0.01100  -0.03953 713 GLY A O   
2120 N N   . GLY A 280 ? 0.19144 0.23449 0.18478 0.01051  0.01607  -0.04292 714 GLY A N   
2121 C CA  . GLY A 280 ? 0.15831 0.19783 0.15085 0.01259  0.01749  -0.05079 714 GLY A CA  
2122 C C   . GLY A 280 ? 0.20242 0.22916 0.19876 0.01417  0.01558  -0.05189 714 GLY A C   
2123 O O   . GLY A 280 ? 0.25558 0.27719 0.25028 0.01445  0.01588  -0.05820 714 GLY A O   
2124 N N   . PHE A 281 ? 0.17077 0.19271 0.17168 0.01473  0.01377  -0.04611 715 PHE A N   
2125 C CA  . PHE A 281 ? 0.17507 0.18537 0.17979 0.01569  0.01196  -0.04601 715 PHE A CA  
2126 C C   . PHE A 281 ? 0.13896 0.14580 0.15068 0.02107  0.01305  -0.04581 715 PHE A C   
2127 O O   . PHE A 281 ? 0.13578 0.15029 0.14991 0.02418  0.01516  -0.04579 715 PHE A O   
2128 C CB  . PHE A 281 ? 0.20989 0.21777 0.21426 0.01207  0.00908  -0.03982 715 PHE A CB  
2129 C CG  . PHE A 281 ? 0.23609 0.24453 0.23537 0.00751  0.00716  -0.04037 715 PHE A CG  
2130 C CD1 . PHE A 281 ? 0.17357 0.18539 0.16774 0.00604  0.00777  -0.04557 715 PHE A CD1 
2131 C CD2 . PHE A 281 ? 0.14971 0.15636 0.14947 0.00478  0.00473  -0.03573 715 PHE A CD2 
2132 C CE1 . PHE A 281 ? 0.13583 0.14918 0.12559 0.00177  0.00543  -0.04541 715 PHE A CE1 
2133 C CE2 . PHE A 281 ? 0.20092 0.20917 0.19723 0.00119  0.00267  -0.03586 715 PHE A CE2 
2134 C CZ  . PHE A 281 ? 0.11445 0.12607 0.10579 -0.00040 0.00275  -0.04034 715 PHE A CZ  
2135 N N   . GLN A 282 ? 0.12574 0.12190 0.14087 0.02177  0.01133  -0.04490 716 GLN A N   
2136 C CA  . GLN A 282 ? 0.20523 0.19654 0.22726 0.02700  0.01163  -0.04401 716 GLN A CA  
2137 C C   . GLN A 282 ? 0.14689 0.13154 0.17173 0.02557  0.00891  -0.03732 716 GLN A C   
2138 O O   . GLN A 282 ? 0.18806 0.16354 0.21713 0.02803  0.00798  -0.03701 716 GLN A O   
2139 C CB  . GLN A 282 ? 0.14075 0.12409 0.16417 0.03026  0.01278  -0.05153 716 GLN A CB  
2140 C CG  . GLN A 282 ? 0.26435 0.23828 0.28378 0.02586  0.01111  -0.05487 716 GLN A CG  
2141 C CD  . GLN A 282 ? 0.29093 0.25534 0.31160 0.02883  0.01215  -0.06287 716 GLN A CD  
2142 O OE1 . GLN A 282 ? 0.21267 0.17597 0.23837 0.03516  0.01404  -0.06565 716 GLN A OE1 
2143 N NE2 . GLN A 282 ? 0.52124 0.47875 0.53766 0.02431  0.01083  -0.06694 716 GLN A NE2 
2144 N N   . VAL A 283 ? 0.13946 0.12863 0.16187 0.02168  0.00775  -0.03223 717 VAL A N   
2145 C CA  . VAL A 283 ? 0.20823 0.19325 0.23286 0.02026  0.00573  -0.02614 717 VAL A CA  
2146 C C   . VAL A 283 ? 0.13850 0.12599 0.16819 0.02440  0.00578  -0.02249 717 VAL A C   
2147 O O   . VAL A 283 ? 0.14340 0.14026 0.17366 0.02596  0.00699  -0.02185 717 VAL A O   
2148 C CB  . VAL A 283 ? 0.18262 0.17238 0.20368 0.01567  0.00488  -0.02251 717 VAL A CB  
2149 C CG1 . VAL A 283 ? 0.17109 0.15791 0.19394 0.01407  0.00333  -0.01689 717 VAL A CG1 
2150 C CG2 . VAL A 283 ? 0.18143 0.16987 0.19851 0.01206  0.00438  -0.02560 717 VAL A CG2 
2151 N N   . THR A 284 ? 0.11846 0.09797 0.15201 0.02590  0.00419  -0.01966 718 THR A N   
2152 C CA  . THR A 284 ? 0.19739 0.17871 0.23654 0.03042  0.00364  -0.01593 718 THR A CA  
2153 C C   . THR A 284 ? 0.15259 0.13906 0.19105 0.02760  0.00207  -0.00881 718 THR A C   
2154 O O   . THR A 284 ? 0.19960 0.18522 0.23397 0.02255  0.00138  -0.00685 718 THR A O   
2155 C CB  . THR A 284 ? 0.14902 0.11835 0.19278 0.03362  0.00223  -0.01577 718 THR A CB  
2156 O OG1 . THR A 284 ? 0.17199 0.13471 0.21448 0.02929  -0.00018 -0.01033 718 THR A OG1 
2157 C CG2 . THR A 284 ? 0.18318 0.14490 0.22602 0.03468  0.00356  -0.02369 718 THR A CG2 
2158 N N   . PRO A 285 ? 0.21730 0.21013 0.25980 0.03075  0.00154  -0.00516 719 PRO A N   
2159 C CA  . PRO A 285 ? 0.15860 0.15603 0.19998 0.02769  -0.00026 0.00146  719 PRO A CA  
2160 C C   . PRO A 285 ? 0.15731 0.14640 0.19748 0.02460  -0.00235 0.00572  719 PRO A C   
2161 O O   . PRO A 285 ? 0.11441 0.10634 0.15062 0.01987  -0.00292 0.00891  719 PRO A O   
2162 C CB  . PRO A 285 ? 0.11225 0.11656 0.15969 0.03252  -0.00105 0.00447  719 PRO A CB  
2163 C CG  . PRO A 285 ? 0.11973 0.12801 0.17008 0.03703  0.00151  -0.00152 719 PRO A CG  
2164 C CD  . PRO A 285 ? 0.17056 0.16857 0.21878 0.03701  0.00271  -0.00730 719 PRO A CD  
2165 N N   . GLU A 286 ? 0.13052 0.10926 0.17398 0.02698  -0.00339 0.00567  720 GLU A N   
2166 C CA  . GLU A 286 ? 0.12575 0.09623 0.16803 0.02332  -0.00540 0.01012  720 GLU A CA  
2167 C C   . GLU A 286 ? 0.20707 0.17584 0.24401 0.01746  -0.00438 0.00760  720 GLU A C   
2168 O O   . GLU A 286 ? 0.20144 0.16950 0.23594 0.01277  -0.00533 0.01174  720 GLU A O   
2169 C CB  . GLU A 286 ? 0.13818 0.09637 0.18535 0.02702  -0.00686 0.01021  720 GLU A CB  
2170 C CG  . GLU A 286 ? 0.28817 0.24711 0.34200 0.03321  -0.00870 0.01450  720 GLU A CG  
2171 C CD  . GLU A 286 ? 0.19506 0.16183 0.25300 0.03951  -0.00666 0.00962  720 GLU A CD  
2172 O OE1 . GLU A 286 ? 0.27927 0.24733 0.33512 0.03971  -0.00384 0.00217  720 GLU A OE1 
2173 O OE2 . GLU A 286 ? 0.33140 0.30413 0.39478 0.04406  -0.00795 0.01350  720 GLU A OE2 
2174 N N   . GLY A 287 ? 0.21708 0.18627 0.25232 0.01762  -0.00249 0.00101  721 GLY A N   
2175 C CA  . GLY A 287 ? 0.16369 0.13269 0.19474 0.01255  -0.00186 -0.00115 721 GLY A CA  
2176 C C   . GLY A 287 ? 0.13974 0.11785 0.16736 0.00945  -0.00123 0.00084  721 GLY A C   
2177 O O   . GLY A 287 ? 0.22236 0.20074 0.24786 0.00516  -0.00137 0.00242  721 GLY A O   
2178 N N   . TYR A 288 ? 0.11142 0.09718 0.13868 0.01148  -0.00040 0.00048  722 TYR A N   
2179 C CA  . TYR A 288 ? 0.10722 0.10020 0.13129 0.00861  0.00001  0.00224  722 TYR A CA  
2180 C C   . TYR A 288 ? 0.14420 0.13795 0.16772 0.00616  -0.00116 0.00766  722 TYR A C   
2181 O O   . TYR A 288 ? 0.23294 0.23027 0.25330 0.00268  -0.00064 0.00835  722 TYR A O   
2182 C CB  . TYR A 288 ? 0.12427 0.12468 0.14835 0.01065  0.00072  0.00152  722 TYR A CB  
2183 C CG  . TYR A 288 ? 0.17740 0.17950 0.20013 0.01140  0.00213  -0.00329 722 TYR A CG  
2184 C CD1 . TYR A 288 ? 0.16422 0.16680 0.18344 0.00846  0.00257  -0.00508 722 TYR A CD1 
2185 C CD2 . TYR A 288 ? 0.09790 0.10190 0.12297 0.01516  0.00302  -0.00587 722 TYR A CD2 
2186 C CE1 . TYR A 288 ? 0.18320 0.18770 0.20065 0.00873  0.00340  -0.00856 722 TYR A CE1 
2187 C CE2 . TYR A 288 ? 0.11782 0.12447 0.14073 0.01518  0.00440  -0.01002 722 TYR A CE2 
2188 C CZ  . TYR A 288 ? 0.11115 0.11786 0.12992 0.01171  0.00436  -0.01095 722 TYR A CZ  
2189 O OH  . TYR A 288 ? 0.17073 0.18041 0.18686 0.01134  0.00529  -0.01419 722 TYR A OH  
2190 N N   . ALA A 289 ? 0.14136 0.13194 0.16788 0.00799  -0.00277 0.01153  723 ALA A N   
2191 C CA  . ALA A 289 ? 0.13074 0.12232 0.15604 0.00506  -0.00419 0.01743  723 ALA A CA  
2192 C C   . ALA A 289 ? 0.17215 0.15971 0.19540 0.00052  -0.00391 0.01798  723 ALA A C   
2193 O O   . ALA A 289 ? 0.12654 0.11848 0.14662 -0.00348 -0.00366 0.02063  723 ALA A O   
2194 C CB  . ALA A 289 ? 0.11125 0.09970 0.14075 0.00833  -0.00655 0.02226  723 ALA A CB  
2195 N N   A HIS A 290 ? 0.14176 0.12185 0.16671 0.00075  -0.00381 0.01516  724 HIS A N   
2196 N N   B HIS A 290 ? 0.14348 0.12354 0.16843 0.00073  -0.00381 0.01517  724 HIS A N   
2197 C CA  A HIS A 290 ? 0.15152 0.12878 0.17524 -0.00406 -0.00364 0.01577  724 HIS A CA  
2198 C CA  B HIS A 290 ? 0.15241 0.12972 0.17611 -0.00410 -0.00365 0.01585  724 HIS A CA  
2199 C C   A HIS A 290 ? 0.14771 0.13133 0.16893 -0.00653 -0.00166 0.01207  724 HIS A C   
2200 C C   B HIS A 290 ? 0.14773 0.13137 0.16894 -0.00654 -0.00166 0.01209  724 HIS A C   
2201 O O   A HIS A 290 ? 0.17399 0.16073 0.19374 -0.01071 -0.00100 0.01362  724 HIS A O   
2202 O O   B HIS A 290 ? 0.17460 0.16139 0.19433 -0.01072 -0.00098 0.01361  724 HIS A O   
2203 C CB  A HIS A 290 ? 0.17811 0.14513 0.20447 -0.00362 -0.00453 0.01381  724 HIS A CB  
2204 C CB  B HIS A 290 ? 0.17845 0.14545 0.20478 -0.00379 -0.00457 0.01401  724 HIS A CB  
2205 C CG  A HIS A 290 ? 0.18976 0.14855 0.21854 -0.00328 -0.00682 0.01909  724 HIS A CG  
2206 C CG  B HIS A 290 ? 0.21093 0.17323 0.23717 -0.00891 -0.00561 0.01802  724 HIS A CG  
2207 N ND1 A HIS A 290 ? 0.19458 0.14954 0.22271 -0.00847 -0.00793 0.02377  724 HIS A ND1 
2208 N ND1 B HIS A 290 ? 0.20256 0.17050 0.22668 -0.01421 -0.00442 0.01841  724 HIS A ND1 
2209 C CD2 A HIS A 290 ? 0.15177 0.10571 0.18400 0.00169  -0.00838 0.02096  724 HIS A CD2 
2210 C CD2 B HIS A 290 ? 0.20377 0.15639 0.23205 -0.00974 -0.00773 0.02202  724 HIS A CD2 
2211 C CE1 A HIS A 290 ? 0.16878 0.11557 0.19944 -0.00693 -0.01037 0.02869  724 HIS A CE1 
2212 C CE1 B HIS A 290 ? 0.13175 0.09476 0.15631 -0.01866 -0.00560 0.02260  724 HIS A CE1 
2213 N NE2 A HIS A 290 ? 0.15136 0.09730 0.18493 -0.00033 -0.01072 0.02694  724 HIS A NE2 
2214 N NE2 B HIS A 290 ? 0.14072 0.09359 0.16756 -0.01626 -0.00781 0.02509  724 HIS A NE2 
2215 N N   . LEU A 291 ? 0.17957 0.16554 0.20052 -0.00393 -0.00072 0.00740  725 LEU A N   
2216 C CA  . LEU A 291 ? 0.15995 0.15154 0.17904 -0.00550 0.00072  0.00453  725 LEU A CA  
2217 C C   . LEU A 291 ? 0.14377 0.14182 0.16039 -0.00708 0.00156  0.00664  725 LEU A C   
2218 O O   . LEU A 291 ? 0.19432 0.19622 0.20995 -0.00955 0.00278  0.00579  725 LEU A O   
2219 C CB  . LEU A 291 ? 0.15512 0.14773 0.17391 -0.00262 0.00112  0.00030  725 LEU A CB  
2220 C CG  . LEU A 291 ? 0.15538 0.14298 0.17546 -0.00107 0.00064  -0.00317 725 LEU A CG  
2221 C CD1 . LEU A 291 ? 0.09520 0.08632 0.11369 0.00044  0.00122  -0.00678 725 LEU A CD1 
2222 C CD2 . LEU A 291 ? 0.16262 0.14660 0.18370 -0.00429 0.00008  -0.00388 725 LEU A CD2 
2223 N N   . THR A 292 ? 0.14813 0.14801 0.16392 -0.00567 0.00094  0.00907  726 THR A N   
2224 C CA  . THR A 292 ? 0.12106 0.12693 0.13375 -0.00781 0.00147  0.01090  726 THR A CA  
2225 C C   . THR A 292 ? 0.10323 0.11031 0.11462 -0.01173 0.00158  0.01444  726 THR A C   
2226 O O   . THR A 292 ? 0.14956 0.16174 0.15837 -0.01447 0.00321  0.01349  726 THR A O   
2227 C CB  . THR A 292 ? 0.19180 0.20008 0.20429 -0.00597 0.00020  0.01329  726 THR A CB  
2228 O OG1 . THR A 292 ? 0.13290 0.14163 0.14639 -0.00306 0.00049  0.01004  726 THR A OG1 
2229 C CG2 . THR A 292 ? 0.09556 0.11021 0.10405 -0.00898 0.00044  0.01494  726 THR A CG2 
2230 N N   . HIS A 293 ? 0.09895 0.10127 0.11212 -0.01208 -0.00007 0.01852  727 HIS A N   
2231 C CA  . HIS A 293 ? 0.10441 0.10775 0.11606 -0.01651 -0.00030 0.02313  727 HIS A CA  
2232 C C   . HIS A 293 ? 0.19661 0.20230 0.20816 -0.01990 0.00179  0.02058  727 HIS A C   
2233 O O   . HIS A 293 ? 0.14612 0.15812 0.15498 -0.02380 0.00323  0.02199  727 HIS A O   
2234 C CB  . HIS A 293 ? 0.12608 0.12139 0.14047 -0.01593 -0.00286 0.02789  727 HIS A CB  
2235 C CG  . HIS A 293 ? 0.13612 0.13203 0.14857 -0.02077 -0.00381 0.03444  727 HIS A CG  
2236 N ND1 . HIS A 293 ? 0.23050 0.23122 0.24000 -0.02213 -0.00514 0.03991  727 HIS A ND1 
2237 C CD2 . HIS A 293 ? 0.12529 0.11811 0.13808 -0.02518 -0.00384 0.03686  727 HIS A CD2 
2238 C CE1 . HIS A 293 ? 0.22405 0.22462 0.23174 -0.02713 -0.00588 0.04566  727 HIS A CE1 
2239 N NE2 . HIS A 293 ? 0.19688 0.19256 0.20667 -0.02917 -0.00501 0.04397  727 HIS A NE2 
2240 N N   . GLN A 294 ? 0.16968 0.17150 0.18424 -0.01856 0.00202  0.01671  728 GLN A N   
2241 C CA  . GLN A 294 ? 0.10012 0.10542 0.11578 -0.02150 0.00366  0.01441  728 GLN A CA  
2242 C C   . GLN A 294 ? 0.21951 0.23294 0.23374 -0.02108 0.00606  0.01077  728 GLN A C   
2243 O O   . GLN A 294 ? 0.21329 0.23319 0.22741 -0.02412 0.00801  0.01046  728 GLN A O   
2244 C CB  . GLN A 294 ? 0.09980 0.09975 0.11875 -0.02021 0.00281  0.01107  728 GLN A CB  
2245 C CG  . GLN A 294 ? 0.17559 0.16613 0.19612 -0.02090 0.00064  0.01362  728 GLN A CG  
2246 C CD  . GLN A 294 ? 0.30208 0.28782 0.32503 -0.02061 -0.00009 0.00949  728 GLN A CD  
2247 O OE1 . GLN A 294 ? 0.43318 0.42361 0.45733 -0.02283 0.00070  0.00705  728 GLN A OE1 
2248 N NE2 . GLN A 294 ? 0.33456 0.31157 0.35840 -0.01779 -0.00161 0.00843  728 GLN A NE2 
2249 N N   . LEU A 295 ? 0.16149 0.17472 0.17486 -0.01739 0.00605  0.00790  729 LEU A N   
2250 C CA  . LEU A 295 ? 0.11154 0.13043 0.12358 -0.01680 0.00805  0.00439  729 LEU A CA  
2251 C C   . LEU A 295 ? 0.15279 0.17735 0.16090 -0.01963 0.00945  0.00600  729 LEU A C   
2252 O O   . LEU A 295 ? 0.13500 0.16526 0.14243 -0.02053 0.01186  0.00305  729 LEU A O   
2253 C CB  . LEU A 295 ? 0.14309 0.15950 0.15457 -0.01312 0.00735  0.00182  729 LEU A CB  
2254 C CG  . LEU A 295 ? 0.13871 0.15147 0.15311 -0.01066 0.00636  -0.00053 729 LEU A CG  
2255 C CD1 . LEU A 295 ? 0.08238 0.09335 0.09549 -0.00786 0.00566  -0.00202 729 LEU A CD1 
2256 C CD2 . LEU A 295 ? 0.10569 0.12185 0.12278 -0.01095 0.00742  -0.00321 729 LEU A CD2 
2257 N N   . MET A 296 ? 0.19545 0.21900 0.20106 -0.02098 0.00793  0.01059  730 MET A N   
2258 C CA  . MET A 296 ? 0.15674 0.18646 0.15767 -0.02445 0.00883  0.01277  730 MET A CA  
2259 C C   . MET A 296 ? 0.13498 0.17023 0.13541 -0.02882 0.01084  0.01401  730 MET A C   
2260 O O   . MET A 296 ? 0.12459 0.16684 0.12056 -0.03207 0.01245  0.01450  730 MET A O   
2261 C CB  . MET A 296 ? 0.15180 0.17963 0.15090 -0.02491 0.00601  0.01863  730 MET A CB  
2262 C CG  . MET A 296 ? 0.09729 0.12320 0.09645 -0.02139 0.00441  0.01765  730 MET A CG  
2263 S SD  . MET A 296 ? 0.11324 0.13847 0.11214 -0.02125 0.00082  0.02506  730 MET A SD  
2264 C CE  . MET A 296 ? 0.15611 0.18947 0.14866 -0.02740 0.00132  0.02900  730 MET A CE  
2265 N N   . SER A 297 ? 0.11377 0.14688 0.11834 -0.02955 0.01083  0.01447  731 SER A N   
2266 C CA  . SER A 297 ? 0.17029 0.21020 0.17504 -0.03420 0.01301  0.01553  731 SER A CA  
2267 C C   . SER A 297 ? 0.16627 0.21403 0.17256 -0.03327 0.01655  0.00929  731 SER A C   
2268 O O   . SER A 297 ? 0.10294 0.15870 0.11004 -0.03682 0.01903  0.00928  731 SER A O   
2269 C CB  . SER A 297 ? 0.10626 0.14126 0.11512 -0.03613 0.01147  0.01840  731 SER A CB  
2270 O OG  . SER A 297 ? 0.14157 0.17496 0.15529 -0.03328 0.01165  0.01369  731 SER A OG  
2271 N N   . LEU A 298 ? 0.15690 0.20281 0.16394 -0.02862 0.01685  0.00423  732 LEU A N   
2272 C CA  . LEU A 298 ? 0.09354 0.14495 0.10309 -0.02643 0.01972  -0.00179 732 LEU A CA  
2273 C C   . LEU A 298 ? 0.15278 0.20730 0.15748 -0.02596 0.02169  -0.00527 732 LEU A C   
2274 O O   . LEU A 298 ? 0.14980 0.20107 0.14968 -0.02646 0.02013  -0.00353 732 LEU A O   
2275 C CB  . LEU A 298 ? 0.08844 0.13427 0.10271 -0.02157 0.01818  -0.00477 732 LEU A CB  
2276 C CG  . LEU A 298 ? 0.12188 0.16355 0.14033 -0.02168 0.01583  -0.00257 732 LEU A CG  
2277 C CD1 . LEU A 298 ? 0.08295 0.11775 0.10287 -0.01725 0.01359  -0.00452 732 LEU A CD1 
2278 C CD2 . LEU A 298 ? 0.11848 0.16766 0.14211 -0.02336 0.01742  -0.00371 732 LEU A CD2 
2279 N N   . ALA A 299 ? 0.14137 0.20259 0.14778 -0.02495 0.02513  -0.01057 733 ALA A N   
2280 C CA  . ALA A 299 ? 0.15584 0.21835 0.15865 -0.02349 0.02723  -0.01598 733 ALA A CA  
2281 C C   . ALA A 299 ? 0.22010 0.28561 0.21464 -0.02798 0.02754  -0.01404 733 ALA A C   
2282 O O   . ALA A 299 ? 0.21626 0.27879 0.20633 -0.02746 0.02711  -0.01655 733 ALA A O   
2283 C CB  . ALA A 299 ? 0.13167 0.18487 0.13567 -0.01879 0.02506  -0.01849 733 ALA A CB  
2284 N N   . ALA A 300 ? 0.15084 0.22254 0.14313 -0.03295 0.02803  -0.00920 734 ALA A N   
2285 C CA  . ALA A 300 ? 0.14204 0.21764 0.12624 -0.03786 0.02770  -0.00583 734 ALA A CA  
2286 C C   . ALA A 300 ? 0.18138 0.24909 0.16279 -0.03695 0.02349  -0.00240 734 ALA A C   
2287 O O   . ALA A 300 ? 0.14804 0.21824 0.12290 -0.03944 0.02301  -0.00218 734 ALA A O   
2288 C CB  . ALA A 300 ? 0.11919 0.20303 0.09822 -0.03945 0.03180  -0.01224 734 ALA A CB  
2289 N N   . GLY A 301 ? 0.14989 0.20908 0.13633 -0.03354 0.02048  0.00005  735 GLY A N   
2290 C CA  . GLY A 301 ? 0.10498 0.15781 0.09030 -0.03210 0.01676  0.00323  735 GLY A CA  
2291 C C   . GLY A 301 ? 0.10273 0.15182 0.08732 -0.02910 0.01651  -0.00177 735 GLY A C   
2292 O O   . GLY A 301 ? 0.11087 0.15690 0.09414 -0.02859 0.01372  0.00067  735 GLY A O   
2293 N N   . ARG A 302 ? 0.10485 0.15415 0.09071 -0.02709 0.01921  -0.00845 736 ARG A N   
2294 C CA  . ARG A 302 ? 0.11968 0.16451 0.10433 -0.02496 0.01901  -0.01326 736 ARG A CA  
2295 C C   . ARG A 302 ? 0.20246 0.23948 0.19205 -0.02093 0.01657  -0.01227 736 ARG A C   
2296 O O   . ARG A 302 ? 0.15157 0.18545 0.14555 -0.01758 0.01729  -0.01536 736 ARG A O   
2297 C CB  . ARG A 302 ? 0.14859 0.19533 0.13343 -0.02375 0.02265  -0.02065 736 ARG A CB  
2298 C CG  . ARG A 302 ? 0.13911 0.19412 0.11787 -0.02780 0.02569  -0.02351 736 ARG A CG  
2299 C CD  . ARG A 302 ? 0.23426 0.28951 0.21408 -0.02528 0.02937  -0.03218 736 ARG A CD  
2300 N NE  . ARG A 302 ? 0.27475 0.34004 0.25047 -0.02844 0.03347  -0.03575 736 ARG A NE  
2301 C CZ  . ARG A 302 ? 0.28534 0.35833 0.26502 -0.02792 0.03678  -0.03691 736 ARG A CZ  
2302 N NH1 . ARG A 302 ? 0.23317 0.30483 0.22115 -0.02448 0.03618  -0.03481 736 ARG A NH1 
2303 N NH2 . ARG A 302 ? 0.31240 0.39573 0.28748 -0.03133 0.04083  -0.04040 736 ARG A NH2 
2304 N N   . VAL A 303 ? 0.13387 0.16853 0.12274 -0.02121 0.01359  -0.00786 737 VAL A N   
2305 C CA  . VAL A 303 ? 0.14858 0.17733 0.14147 -0.01789 0.01150  -0.00666 737 VAL A CA  
2306 C C   . VAL A 303 ? 0.09042 0.11720 0.08085 -0.01816 0.00985  -0.00698 737 VAL A C   
2307 O O   . VAL A 303 ? 0.15512 0.18549 0.14183 -0.02091 0.00882  -0.00491 737 VAL A O   
2308 C CB  . VAL A 303 ? 0.19310 0.22103 0.18884 -0.01738 0.00973  -0.00145 737 VAL A CB  
2309 C CG1 . VAL A 303 ? 0.12775 0.15044 0.12710 -0.01399 0.00810  -0.00133 737 VAL A CG1 
2310 C CG2 . VAL A 303 ? 0.12752 0.15753 0.12544 -0.01835 0.01121  -0.00087 737 VAL A CG2 
2311 N N   . LEU A 304 ? 0.16710 0.18888 0.15959 -0.01576 0.00939  -0.00916 738 LEU A N   
2312 C CA  . LEU A 304 ? 0.10909 0.12895 0.10011 -0.01628 0.00769  -0.00886 738 LEU A CA  
2313 C C   . LEU A 304 ? 0.13018 0.14740 0.12509 -0.01347 0.00627  -0.00669 738 LEU A C   
2314 O O   . LEU A 304 ? 0.12811 0.14200 0.12579 -0.01107 0.00666  -0.00806 738 LEU A O   
2315 C CB  . LEU A 304 ? 0.09281 0.10865 0.08171 -0.01690 0.00849  -0.01353 738 LEU A CB  
2316 C CG  . LEU A 304 ? 0.09347 0.10622 0.08145 -0.01784 0.00663  -0.01299 738 LEU A CG  
2317 C CD1 . LEU A 304 ? 0.09420 0.11244 0.07935 -0.02121 0.00511  -0.01026 738 LEU A CD1 
2318 C CD2 . LEU A 304 ? 0.09937 0.10584 0.08560 -0.01843 0.00719  -0.01745 738 LEU A CD2 
2319 N N   . ILE A 305 ? 0.21303 0.23264 0.20823 -0.01370 0.00465  -0.00345 739 ILE A N   
2320 C CA  . ILE A 305 ? 0.07936 0.09785 0.07790 -0.01108 0.00370  -0.00188 739 ILE A CA  
2321 C C   . ILE A 305 ? 0.07979 0.09810 0.07720 -0.01207 0.00296  -0.00239 739 ILE A C   
2322 O O   . ILE A 305 ? 0.11284 0.13516 0.10878 -0.01427 0.00205  -0.00103 739 ILE A O   
2323 C CB  . ILE A 305 ? 0.07855 0.10020 0.07928 -0.00998 0.00266  0.00183  739 ILE A CB  
2324 C CG1 . ILE A 305 ? 0.11081 0.13125 0.11266 -0.00959 0.00317  0.00291  739 ILE A CG1 
2325 C CG2 . ILE A 305 ? 0.07632 0.09771 0.08019 -0.00720 0.00210  0.00238  739 ILE A CG2 
2326 C CD1 . ILE A 305 ? 0.17590 0.19775 0.17989 -0.00860 0.00176  0.00712  739 ILE A CD1 
2327 N N   . ILE A 306 ? 0.07931 0.09348 0.07747 -0.01082 0.00314  -0.00394 740 ILE A N   
2328 C CA  . ILE A 306 ? 0.09715 0.11032 0.09390 -0.01240 0.00236  -0.00392 740 ILE A CA  
2329 C C   . ILE A 306 ? 0.13746 0.15325 0.13634 -0.01075 0.00195  -0.00216 740 ILE A C   
2330 O O   . ILE A 306 ? 0.09408 0.10773 0.09446 -0.00841 0.00216  -0.00270 740 ILE A O   
2331 C CB  . ILE A 306 ? 0.09283 0.09943 0.08836 -0.01268 0.00246  -0.00627 740 ILE A CB  
2332 C CG1 . ILE A 306 ? 0.08824 0.09280 0.08178 -0.01393 0.00342  -0.00914 740 ILE A CG1 
2333 C CG2 . ILE A 306 ? 0.08744 0.09207 0.08131 -0.01494 0.00130  -0.00529 740 ILE A CG2 
2334 C CD1 . ILE A 306 ? 0.09226 0.09001 0.08626 -0.01260 0.00378  -0.01196 740 ILE A CD1 
2335 N N   . LEU A 307 ? 0.07812 0.09937 0.07711 -0.01218 0.00144  -0.00041 741 LEU A N   
2336 C CA  . LEU A 307 ? 0.07643 0.10169 0.07741 -0.01068 0.00160  0.00062  741 LEU A CA  
2337 C C   . LEU A 307 ? 0.10484 0.12644 0.10403 -0.01144 0.00149  0.00013  741 LEU A C   
2338 O O   . LEU A 307 ? 0.08149 0.09962 0.07810 -0.01445 0.00079  0.00026  741 LEU A O   
2339 C CB  . LEU A 307 ? 0.07651 0.10989 0.07853 -0.01233 0.00124  0.00254  741 LEU A CB  
2340 C CG  . LEU A 307 ? 0.07558 0.11491 0.07971 -0.01104 0.00199  0.00305  741 LEU A CG  
2341 C CD1 . LEU A 307 ? 0.07369 0.11381 0.08141 -0.00604 0.00288  0.00212  741 LEU A CD1 
2342 C CD2 . LEU A 307 ? 0.07614 0.12492 0.08161 -0.01354 0.00167  0.00501  741 LEU A CD2 
2343 N N   . GLU A 308 ? 0.07678 0.09886 0.07709 -0.00898 0.00196  -0.00036 742 GLU A N   
2344 C CA  . GLU A 308 ? 0.09408 0.11429 0.09225 -0.01002 0.00150  0.00002  742 GLU A CA  
2345 C C   . GLU A 308 ? 0.08340 0.11113 0.08184 -0.00999 0.00240  0.00055  742 GLU A C   
2346 O O   . GLU A 308 ? 0.09271 0.12617 0.09140 -0.01204 0.00269  0.00188  742 GLU A O   
2347 C CB  . GLU A 308 ? 0.07872 0.09372 0.07733 -0.00773 0.00111  -0.00137 742 GLU A CB  
2348 C CG  . GLU A 308 ? 0.08812 0.09720 0.08688 -0.00778 0.00062  -0.00213 742 GLU A CG  
2349 C CD  . GLU A 308 ? 0.14142 0.14529 0.13837 -0.00928 -0.00072 -0.00123 742 GLU A CD  
2350 O OE1 . GLU A 308 ? 0.21908 0.22383 0.21392 -0.01134 -0.00151 0.00084  742 GLU A OE1 
2351 O OE2 . GLU A 308 ? 0.12744 0.12647 0.12528 -0.00835 -0.00092 -0.00252 742 GLU A OE2 
2352 N N   . GLY A 309 ? 0.07875 0.10712 0.07728 -0.00775 0.00293  -0.00090 743 GLY A N   
2353 C CA  . GLY A 309 ? 0.07949 0.11553 0.07814 -0.00719 0.00438  -0.00159 743 GLY A CA  
2354 C C   . GLY A 309 ? 0.10927 0.14964 0.11228 -0.00368 0.00578  -0.00323 743 GLY A C   
2355 O O   . GLY A 309 ? 0.12959 0.16794 0.13494 -0.00280 0.00523  -0.00253 743 GLY A O   
2356 N N   . GLY A 310 ? 0.07885 0.12458 0.08285 -0.00147 0.00747  -0.00552 744 GLY A N   
2357 C CA  . GLY A 310 ? 0.11409 0.16421 0.12323 0.00254  0.00878  -0.00696 744 GLY A CA  
2358 C C   . GLY A 310 ? 0.13281 0.19442 0.14312 0.00154  0.01035  -0.00628 744 GLY A C   
2359 O O   . GLY A 310 ? 0.12836 0.19329 0.13832 -0.00197 0.00949  -0.00307 744 GLY A O   
2360 N N   . TYR A 311 ? 0.11981 0.18780 0.13144 0.00422  0.01272  -0.00956 745 TYR A N   
2361 C CA  . TYR A 311 ? 0.11803 0.19917 0.13040 0.00270  0.01480  -0.00920 745 TYR A CA  
2362 C C   . TYR A 311 ? 0.16294 0.25274 0.18226 0.00830  0.01718  -0.01206 745 TYR A C   
2363 O O   . TYR A 311 ? 0.19070 0.29312 0.21162 0.00748  0.01931  -0.01216 745 TYR A O   
2364 C CB  . TYR A 311 ? 0.11208 0.19472 0.11794 -0.00076 0.01564  -0.01011 745 TYR A CB  
2365 C CG  . TYR A 311 ? 0.15128 0.22489 0.15186 -0.00543 0.01274  -0.00651 745 TYR A CG  
2366 C CD1 . TYR A 311 ? 0.11919 0.19383 0.11843 -0.01032 0.01133  -0.00202 745 TYR A CD1 
2367 C CD2 . TYR A 311 ? 0.08636 0.15018 0.08411 -0.00468 0.01127  -0.00780 745 TYR A CD2 
2368 C CE1 . TYR A 311 ? 0.09961 0.16485 0.09484 -0.01374 0.00872  0.00078  745 TYR A CE1 
2369 C CE2 . TYR A 311 ? 0.10186 0.15798 0.09619 -0.00792 0.00865  -0.00466 745 TYR A CE2 
2370 C CZ  . TYR A 311 ? 0.10764 0.16394 0.10079 -0.01210 0.00745  -0.00053 745 TYR A CZ  
2371 O OH  . TYR A 311 ? 0.08791 0.13565 0.07832 -0.01457 0.00496  0.00208  745 TYR A OH  
2372 N N   . ASN A 312 ? 0.19786 0.28095 0.22117 0.01378  0.01692  -0.01443 746 ASN A N   
2373 C CA  . ASN A 312 ? 0.14145 0.23112 0.17277 0.01992  0.01848  -0.01631 746 ASN A CA  
2374 C C   . ASN A 312 ? 0.21759 0.30873 0.25364 0.02007  0.01603  -0.01126 746 ASN A C   
2375 O O   . ASN A 312 ? 0.13531 0.21633 0.17092 0.02016  0.01351  -0.00916 746 ASN A O   
2376 C CB  . ASN A 312 ? 0.13886 0.21939 0.17217 0.02560  0.01909  -0.02114 746 ASN A CB  
2377 C CG  . ASN A 312 ? 0.15266 0.23898 0.19479 0.03290  0.02085  -0.02371 746 ASN A CG  
2378 O OD1 . ASN A 312 ? 0.14543 0.23274 0.19387 0.03569  0.01911  -0.02009 746 ASN A OD1 
2379 N ND2 . ASN A 312 ? 0.12803 0.21848 0.17074 0.03623  0.02427  -0.03010 746 ASN A ND2 
2380 N N   . LEU A 313 ? 0.14873 0.25356 0.18905 0.01953  0.01673  -0.00918 747 LEU A N   
2381 C CA  . LEU A 313 ? 0.11916 0.22708 0.16268 0.01801  0.01398  -0.00401 747 LEU A CA  
2382 C C   . LEU A 313 ? 0.11354 0.21544 0.16272 0.02381  0.01209  -0.00296 747 LEU A C   
2383 O O   . LEU A 313 ? 0.09664 0.19364 0.14471 0.02165  0.00910  0.00101  747 LEU A O   
2384 C CB  . LEU A 313 ? 0.10663 0.23214 0.15496 0.01676  0.01508  -0.00230 747 LEU A CB  
2385 C CG  . LEU A 313 ? 0.12476 0.25719 0.16750 0.00978  0.01662  -0.00201 747 LEU A CG  
2386 C CD1 . LEU A 313 ? 0.07806 0.22902 0.12646 0.00807  0.01755  0.00014  747 LEU A CD1 
2387 C CD2 . LEU A 313 ? 0.11715 0.23903 0.15167 0.00264  0.01403  0.00087  747 LEU A CD2 
2388 N N   . THR A 314 ? 0.10805 0.20982 0.16303 0.03103  0.01376  -0.00650 748 THR A N   
2389 C CA  . THR A 314 ? 0.12774 0.22273 0.18849 0.03666  0.01163  -0.00484 748 THR A CA  
2390 C C   . THR A 314 ? 0.12960 0.20757 0.18489 0.03533  0.01004  -0.00508 748 THR A C   
2391 O O   . THR A 314 ? 0.09058 0.16255 0.14633 0.03493  0.00707  -0.00078 748 THR A O   
2392 C CB  . THR A 314 ? 0.09382 0.19277 0.16308 0.04521  0.01391  -0.00894 748 THR A CB  
2393 O OG1 . THR A 314 ? 0.10486 0.22181 0.18053 0.04662  0.01532  -0.00813 748 THR A OG1 
2394 C CG2 . THR A 314 ? 0.09885 0.18851 0.17414 0.05116  0.01128  -0.00668 748 THR A CG2 
2395 N N   . SER A 315 ? 0.14074 0.21191 0.19073 0.03422  0.01192  -0.00988 749 SER A N   
2396 C CA  . SER A 315 ? 0.17455 0.23103 0.22010 0.03280  0.01051  -0.01038 749 SER A CA  
2397 C C   . SER A 315 ? 0.10349 0.15675 0.14367 0.02663  0.00818  -0.00591 749 SER A C   
2398 O O   . SER A 315 ? 0.11665 0.16107 0.15605 0.02607  0.00620  -0.00367 749 SER A O   
2399 C CB  . SER A 315 ? 0.13382 0.18602 0.17460 0.03211  0.01272  -0.01633 749 SER A CB  
2400 O OG  . SER A 315 ? 0.16038 0.21600 0.20558 0.03774  0.01534  -0.02156 749 SER A OG  
2401 N N   . ILE A 316 ? 0.08347 0.14369 0.11988 0.02180  0.00850  -0.00471 750 ILE A N   
2402 C CA  . ILE A 316 ? 0.07871 0.13496 0.10995 0.01630  0.00662  -0.00161 750 ILE A CA  
2403 C C   . ILE A 316 ? 0.09840 0.15799 0.13226 0.01576  0.00434  0.00313  750 ILE A C   
2404 O O   . ILE A 316 ? 0.14253 0.19647 0.17313 0.01286  0.00269  0.00528  750 ILE A O   
2405 C CB  . ILE A 316 ? 0.07995 0.14035 0.10610 0.01116  0.00739  -0.00190 750 ILE A CB  
2406 C CG1 . ILE A 316 ? 0.11200 0.18521 0.14089 0.00983  0.00774  0.00008  750 ILE A CG1 
2407 C CG2 . ILE A 316 ? 0.09621 0.15484 0.11946 0.01151  0.00930  -0.00591 750 ILE A CG2 
2408 C CD1 . ILE A 316 ? 0.14111 0.21791 0.16499 0.00408  0.00829  0.00046  750 ILE A CD1 
2409 N N   . SER A 317 ? 0.09104 0.16080 0.13083 0.01844  0.00420  0.00479  751 SER A N   
2410 C CA  . SER A 317 ? 0.10466 0.17830 0.14715 0.01810  0.00149  0.00972  751 SER A CA  
2411 C C   . SER A 317 ? 0.11028 0.17520 0.15519 0.02182  -0.00016 0.01156  751 SER A C   
2412 O O   . SER A 317 ? 0.09315 0.15522 0.13562 0.01910  -0.00245 0.01530  751 SER A O   
2413 C CB  . SER A 317 ? 0.07897 0.16709 0.12833 0.02038  0.00147  0.01135  751 SER A CB  
2414 O OG  . SER A 317 ? 0.07624 0.17276 0.12300 0.01569  0.00283  0.01035  751 SER A OG  
2415 N N   . GLU A 318 ? 0.09392 0.15426 0.14320 0.02762  0.00101  0.00887  752 GLU A N   
2416 C CA  . GLU A 318 ? 0.17476 0.22484 0.22617 0.03067  -0.00069 0.01069  752 GLU A CA  
2417 C C   . GLU A 318 ? 0.09090 0.13020 0.13529 0.02604  -0.00100 0.01037  752 GLU A C   
2418 O O   . GLU A 318 ? 0.12417 0.15836 0.16775 0.02477  -0.00316 0.01440  752 GLU A O   
2419 C CB  . GLU A 318 ? 0.14604 0.19198 0.20316 0.03754  0.00089  0.00662  752 GLU A CB  
2420 C CG  . GLU A 318 ? 0.26036 0.29988 0.32366 0.04260  -0.00155 0.01016  752 GLU A CG  
2421 C CD  . GLU A 318 ? 0.17912 0.22957 0.24899 0.04533  -0.00387 0.01576  752 GLU A CD  
2422 O OE1 . GLU A 318 ? 0.18703 0.24992 0.26122 0.04764  -0.00234 0.01409  752 GLU A OE1 
2423 O OE2 . GLU A 318 ? 0.14654 0.19422 0.21717 0.04475  -0.00731 0.02212  752 GLU A OE2 
2424 N N   . SER A 319 ? 0.09593 0.13269 0.13539 0.02335  0.00105  0.00596  753 SER A N   
2425 C CA  . SER A 319 ? 0.08734 0.11494 0.12152 0.01975  0.00091  0.00516  753 SER A CA  
2426 C C   . SER A 319 ? 0.13470 0.16387 0.16458 0.01467  -0.00041 0.00866  753 SER A C   
2427 O O   . SER A 319 ? 0.18658 0.21049 0.21507 0.01305  -0.00157 0.01106  753 SER A O   
2428 C CB  . SER A 319 ? 0.08531 0.11133 0.11582 0.01839  0.00298  0.00010  753 SER A CB  
2429 O OG  . SER A 319 ? 0.13513 0.15636 0.16789 0.02209  0.00408  -0.00389 753 SER A OG  
2430 N N   . MET A 320 ? 0.08468 0.12104 0.11214 0.01170  -0.00010 0.00873  754 MET A N   
2431 C CA  . MET A 320 ? 0.12013 0.15729 0.14295 0.00678  -0.00104 0.01071  754 MET A CA  
2432 C C   . MET A 320 ? 0.08741 0.12783 0.11167 0.00653  -0.00330 0.01564  754 MET A C   
2433 O O   . MET A 320 ? 0.08241 0.12125 0.10264 0.00295  -0.00403 0.01726  754 MET A O   
2434 C CB  . MET A 320 ? 0.12534 0.16820 0.14531 0.00339  -0.00047 0.00952  754 MET A CB  
2435 C CG  . MET A 320 ? 0.09695 0.13723 0.11116 -0.00157 -0.00066 0.00911  754 MET A CG  
2436 S SD  . MET A 320 ? 0.08613 0.12939 0.09709 -0.00547 -0.00008 0.00727  754 MET A SD  
2437 C CE  . MET A 320 ? 0.08604 0.12259 0.09120 -0.00949 0.00000  0.00552  754 MET A CE  
2438 N N   . SER A 321 ? 0.11291 0.15862 0.14298 0.01040  -0.00446 0.01814  755 SER A N   
2439 C CA  . SER A 321 ? 0.08743 0.13575 0.11951 0.01080  -0.00725 0.02380  755 SER A CA  
2440 C C   . SER A 321 ? 0.10532 0.14398 0.13640 0.01098  -0.00795 0.02567  755 SER A C   
2441 O O   . SER A 321 ? 0.14554 0.18468 0.17346 0.00764  -0.00964 0.02968  755 SER A O   
2442 C CB  . SER A 321 ? 0.08968 0.14477 0.12985 0.01631  -0.00844 0.02606  755 SER A CB  
2443 O OG  . SER A 321 ? 0.08654 0.15349 0.12762 0.01466  -0.00856 0.02620  755 SER A OG  
2444 N N   . MET A 322 ? 0.15524 0.18550 0.18857 0.01421  -0.00667 0.02275  756 MET A N   
2445 C CA  . MET A 322 ? 0.14162 0.16232 0.17416 0.01361  -0.00735 0.02445  756 MET A CA  
2446 C C   . MET A 322 ? 0.11046 0.12987 0.13624 0.00765  -0.00654 0.02400  756 MET A C   
2447 O O   . MET A 322 ? 0.15118 0.16836 0.17503 0.00501  -0.00777 0.02796  756 MET A O   
2448 C CB  . MET A 322 ? 0.16349 0.17553 0.19890 0.01721  -0.00595 0.02010  756 MET A CB  
2449 C CG  . MET A 322 ? 0.16489 0.17319 0.20741 0.02332  -0.00729 0.02168  756 MET A CG  
2450 S SD  . MET A 322 ? 0.28685 0.28959 0.33088 0.02271  -0.01099 0.03009  756 MET A SD  
2451 C CE  . MET A 322 ? 0.19202 0.18186 0.24273 0.02896  -0.01141 0.02823  756 MET A CE  
2452 N N   . CYS A 323 ? 0.11646 0.13757 0.13880 0.00555  -0.00445 0.01933  757 CYS A N   
2453 C CA  . CYS A 323 ? 0.13723 0.15742 0.15419 0.00086  -0.00337 0.01807  757 CYS A CA  
2454 C C   . CYS A 323 ? 0.14934 0.17558 0.16260 -0.00293 -0.00447 0.02149  757 CYS A C   
2455 O O   . CYS A 323 ? 0.21554 0.24090 0.22574 -0.00611 -0.00444 0.02328  757 CYS A O   
2456 C CB  . CYS A 323 ? 0.14587 0.16636 0.16072 0.00014  -0.00141 0.01289  757 CYS A CB  
2457 S SG  . CYS A 323 ? 0.12648 0.14096 0.14392 0.00334  -0.00018 0.00860  757 CYS A SG  
2458 N N   . THR A 324 ? 0.11445 0.14780 0.12765 -0.00317 -0.00538 0.02224  758 THR A N   
2459 C CA  . THR A 324 ? 0.09061 0.13055 0.09987 -0.00719 -0.00680 0.02525  758 THR A CA  
2460 C C   . THR A 324 ? 0.11061 0.15052 0.12028 -0.00756 -0.00899 0.03137  758 THR A C   
2461 O O   . THR A 324 ? 0.11106 0.15324 0.11554 -0.01201 -0.00915 0.03310  758 THR A O   
2462 C CB  . THR A 324 ? 0.12748 0.17567 0.13820 -0.00707 -0.00816 0.02604  758 THR A CB  
2463 O OG1 . THR A 324 ? 0.18261 0.23049 0.19214 -0.00781 -0.00627 0.02100  758 THR A OG1 
2464 C CG2 . THR A 324 ? 0.09613 0.15170 0.10229 -0.01182 -0.01005 0.02904  758 THR A CG2 
2465 N N   . SER A 325 ? 0.11243 0.14958 0.12820 -0.00293 -0.01065 0.03469  759 SER A N   
2466 C CA  . SER A 325 ? 0.16623 0.20178 0.18307 -0.00294 -0.01329 0.04150  759 SER A CA  
2467 C C   . SER A 325 ? 0.14382 0.17337 0.15670 -0.00659 -0.01207 0.04176  759 SER A C   
2468 O O   . SER A 325 ? 0.24166 0.27332 0.25120 -0.01023 -0.01362 0.04708  759 SER A O   
2469 C CB  . SER A 325 ? 0.10959 0.14064 0.13458 0.00361  -0.01493 0.04376  759 SER A CB  
2470 O OG  . SER A 325 ? 0.11799 0.14451 0.14439 0.00379  -0.01766 0.05056  759 SER A OG  
2471 N N   . MET A 326 ? 0.13514 0.15833 0.14826 -0.00606 -0.00937 0.03634  760 MET A N   
2472 C CA  . MET A 326 ? 0.12014 0.13948 0.13018 -0.00983 -0.00798 0.03621  760 MET A CA  
2473 C C   . MET A 326 ? 0.14543 0.17182 0.14879 -0.01514 -0.00640 0.03493  760 MET A C   
2474 O O   . MET A 326 ? 0.16312 0.19107 0.16304 -0.01931 -0.00632 0.03814  760 MET A O   
2475 C CB  . MET A 326 ? 0.10411 0.11671 0.11635 -0.00811 -0.00577 0.03053  760 MET A CB  
2476 C CG  . MET A 326 ? 0.16089 0.16551 0.17890 -0.00344 -0.00691 0.03067  760 MET A CG  
2477 S SD  . MET A 326 ? 0.17425 0.17168 0.19468 -0.00385 -0.00986 0.03824  760 MET A SD  
2478 C CE  . MET A 326 ? 0.12131 0.12267 0.14578 0.00087  -0.01302 0.04329  760 MET A CE  
2479 N N   . LEU A 327 ? 0.11263 0.14319 0.11395 -0.01527 -0.00500 0.03006  761 LEU A N   
2480 C CA  . LEU A 327 ? 0.14350 0.18012 0.13847 -0.01990 -0.00347 0.02787  761 LEU A CA  
2481 C C   . LEU A 327 ? 0.16681 0.21017 0.15780 -0.02353 -0.00569 0.03370  761 LEU A C   
2482 O O   . LEU A 327 ? 0.11143 0.15871 0.09701 -0.02814 -0.00448 0.03406  761 LEU A O   
2483 C CB  . LEU A 327 ? 0.09866 0.13723 0.09254 -0.01935 -0.00249 0.02253  761 LEU A CB  
2484 C CG  . LEU A 327 ? 0.12491 0.15798 0.12164 -0.01638 -0.00059 0.01709  761 LEU A CG  
2485 C CD1 . LEU A 327 ? 0.12097 0.15610 0.11605 -0.01681 -0.00032 0.01349  761 LEU A CD1 
2486 C CD2 . LEU A 327 ? 0.11614 0.14655 0.11190 -0.01749 0.00199  0.01375  761 LEU A CD2 
2487 N N   . LEU A 328 ? 0.13043 0.17622 0.12418 -0.02147 -0.00899 0.03842  762 LEU A N   
2488 C CA  . LEU A 328 ? 0.15453 0.20740 0.14510 -0.02461 -0.01200 0.04510  762 LEU A CA  
2489 C C   . LEU A 328 ? 0.18913 0.23937 0.17912 -0.02640 -0.01323 0.05167  762 LEU A C   
2490 O O   . LEU A 328 ? 0.18534 0.24165 0.17172 -0.02979 -0.01587 0.05808  762 LEU A O   
2491 C CB  . LEU A 328 ? 0.19487 0.25135 0.19049 -0.02098 -0.01550 0.04889  762 LEU A CB  
2492 C CG  . LEU A 328 ? 0.23169 0.29429 0.22620 -0.02164 -0.01509 0.04426  762 LEU A CG  
2493 C CD1 . LEU A 328 ? 0.17476 0.24060 0.17667 -0.01682 -0.01771 0.04703  762 LEU A CD1 
2494 C CD2 . LEU A 328 ? 0.11528 0.18678 0.10165 -0.02820 -0.01587 0.04476  762 LEU A CD2 
2495 N N   . GLY A 329 ? 0.13829 0.17998 0.13145 -0.02481 -0.01167 0.05061  763 GLY A N   
2496 C CA  . GLY A 329 ? 0.13178 0.17035 0.12403 -0.02765 -0.01253 0.05653  763 GLY A CA  
2497 C C   . GLY A 329 ? 0.17067 0.20172 0.16911 -0.02389 -0.01622 0.06342  763 GLY A C   
2498 O O   . GLY A 329 ? 0.19039 0.21852 0.18777 -0.02688 -0.01780 0.06998  763 GLY A O   
2499 N N   . ASP A 330 ? 0.17409 0.20182 0.17907 -0.01749 -0.01756 0.06211  764 ASP A N   
2500 C CA  . ASP A 330 ? 0.16441 0.18425 0.17617 -0.01285 -0.02089 0.06778  764 ASP A CA  
2501 C C   . ASP A 330 ? 0.17649 0.18412 0.19087 -0.01240 -0.01963 0.06619  764 ASP A C   
2502 O O   . ASP A 330 ? 0.13614 0.14159 0.14963 -0.01313 -0.01616 0.05904  764 ASP A O   
2503 C CB  . ASP A 330 ? 0.13549 0.15643 0.15399 -0.00581 -0.02188 0.06552  764 ASP A CB  
2504 C CG  . ASP A 330 ? 0.16813 0.20147 0.18518 -0.00651 -0.02408 0.06851  764 ASP A CG  
2505 O OD1 . ASP A 330 ? 0.32726 0.36597 0.34014 -0.01071 -0.02674 0.07546  764 ASP A OD1 
2506 O OD2 . ASP A 330 ? 0.18780 0.22620 0.20759 -0.00344 -0.02329 0.06412  764 ASP A OD2 
2507 N N   . SER A 331 ? 0.27261 0.27215 0.29032 -0.01145 -0.02284 0.07325  765 SER A N   
2508 C CA  . SER A 331 ? 0.28671 0.27353 0.30705 -0.01159 -0.02227 0.07225  765 SER A CA  
2509 C C   . SER A 331 ? 0.26626 0.24709 0.29178 -0.00566 -0.02019 0.06357  765 SER A C   
2510 O O   . SER A 331 ? 0.25207 0.23336 0.28265 0.00078  -0.02119 0.06235  765 SER A O   
2511 C CB  . SER A 331 ? 0.18202 0.15958 0.20588 -0.01070 -0.02672 0.08161  765 SER A CB  
2512 O OG  . SER A 331 ? 0.59559 0.55864 0.62484 -0.00753 -0.02678 0.07894  765 SER A OG  
2513 N N   . PRO A 332 ? 0.36613 0.34264 0.39055 -0.00779 -0.01729 0.05747  766 PRO A N   
2514 C CA  . PRO A 332 ? 0.29652 0.26865 0.32468 -0.00287 -0.01538 0.04921  766 PRO A CA  
2515 C C   . PRO A 332 ? 0.35175 0.31192 0.38643 0.00263  -0.01753 0.05001  766 PRO A C   
2516 O O   . PRO A 332 ? 0.35159 0.30276 0.38767 0.00117  -0.02013 0.05600  766 PRO A O   
2517 C CB  . PRO A 332 ? 0.18388 0.15451 0.20909 -0.00757 -0.01263 0.04430  766 PRO A CB  
2518 C CG  . PRO A 332 ? 0.30611 0.27640 0.32815 -0.01417 -0.01355 0.05073  766 PRO A CG  
2519 C CD  . PRO A 332 ? 0.25225 0.23008 0.27179 -0.01506 -0.01549 0.05767  766 PRO A CD  
2520 N N   . PRO A 333 ? 0.28887 0.24832 0.32768 0.00895  -0.01645 0.04402  767 PRO A N   
2521 C CA  . PRO A 333 ? 0.29100 0.23977 0.33660 0.01529  -0.01814 0.04380  767 PRO A CA  
2522 C C   . PRO A 333 ? 0.32250 0.25836 0.36863 0.01421  -0.01726 0.03881  767 PRO A C   
2523 O O   . PRO A 333 ? 0.32888 0.26617 0.37104 0.01001  -0.01490 0.03372  767 PRO A O   
2524 C CB  . PRO A 333 ? 0.32367 0.28008 0.37268 0.02174  -0.01650 0.03844  767 PRO A CB  
2525 C CG  . PRO A 333 ? 0.23862 0.20343 0.28200 0.01788  -0.01322 0.03268  767 PRO A CG  
2526 C CD  . PRO A 333 ? 0.23102 0.19980 0.26843 0.01054  -0.01356 0.03724  767 PRO A CD  
2527 N N   . SER A 334 ? 0.33881 0.26181 0.39027 0.01821  -0.01947 0.04029  768 SER A N   
2528 C CA  . SER A 334 ? 0.30959 0.21898 0.36183 0.01744  -0.01893 0.03482  768 SER A CA  
2529 C C   . SER A 334 ? 0.31789 0.23108 0.36930 0.01981  -0.01537 0.02408  768 SER A C   
2530 O O   . SER A 334 ? 0.32636 0.24848 0.37952 0.02500  -0.01380 0.02085  768 SER A O   
2531 C CB  . SER A 334 ? 0.41348 0.30783 0.47236 0.02290  -0.02178 0.03710  768 SER A CB  
2532 O OG  . SER A 334 ? 0.66943 0.56667 0.73417 0.03213  -0.02100 0.03312  768 SER A OG  
2533 N N   . LEU A 335 ? 0.32660 0.23373 0.37517 0.01540  -0.01428 0.01892  769 LEU A N   
2534 C CA  . LEU A 335 ? 0.24102 0.15319 0.28725 0.01589  -0.01123 0.00964  769 LEU A CA  
2535 C C   . LEU A 335 ? 0.27545 0.17490 0.32214 0.01543  -0.01109 0.00277  769 LEU A C   
2536 O O   . LEU A 335 ? 0.26797 0.16043 0.31266 0.00913  -0.01221 0.00368  769 LEU A O   
2537 C CB  . LEU A 335 ? 0.35894 0.28215 0.39963 0.00959  -0.00978 0.00990  769 LEU A CB  
2538 C CG  . LEU A 335 ? 0.33634 0.26771 0.37417 0.00988  -0.00709 0.00239  769 LEU A CG  
2539 C CD1 . LEU A 335 ? 0.29571 0.23514 0.33514 0.01600  -0.00572 0.00052  769 LEU A CD1 
2540 C CD2 . LEU A 335 ? 0.32678 0.26719 0.36037 0.00400  -0.00626 0.00379  769 LEU A CD2 
2541 N N   . THR A 339 ? 0.36384 0.22771 0.39521 -0.01247 -0.01173 -0.03619 773 THR A N   
2542 C CA  . THR A 339 ? 0.41897 0.28706 0.44768 -0.00825 -0.00957 -0.04562 773 THR A CA  
2543 C C   . THR A 339 ? 0.50585 0.38527 0.52970 -0.01422 -0.00951 -0.04918 773 THR A C   
2544 O O   . THR A 339 ? 0.48593 0.37779 0.50924 -0.01694 -0.00954 -0.04387 773 THR A O   
2545 C CB  . THR A 339 ? 0.52294 0.40093 0.55308 -0.00001 -0.00714 -0.04449 773 THR A CB  
2546 O OG1 . THR A 339 ? 0.40605 0.27801 0.44130 0.00426  -0.00797 -0.03757 773 THR A OG1 
2547 C CG2 . THR A 339 ? 0.25602 0.13355 0.28483 0.00552  -0.00480 -0.05435 773 THR A CG2 
2548 N N   . PRO A 340 ? 0.53655 0.41181 0.55697 -0.01613 -0.00954 -0.05828 774 PRO A N   
2549 C CA  . PRO A 340 ? 0.46254 0.34817 0.47851 -0.02247 -0.01032 -0.06124 774 PRO A CA  
2550 C C   . PRO A 340 ? 0.42055 0.32236 0.43349 -0.01902 -0.00835 -0.06236 774 PRO A C   
2551 O O   . PRO A 340 ? 0.33126 0.23439 0.34316 -0.01277 -0.00602 -0.06651 774 PRO A O   
2552 C CB  . PRO A 340 ? 0.32256 0.19702 0.33540 -0.02549 -0.01115 -0.07101 774 PRO A CB  
2553 C CG  . PRO A 340 ? 0.45340 0.31704 0.46799 -0.01743 -0.00914 -0.07565 774 PRO A CG  
2554 C CD  . PRO A 340 ? 0.52227 0.38252 0.54287 -0.01294 -0.00915 -0.06639 774 PRO A CD  
2555 N N   . LEU A 341 ? 0.35965 0.27405 0.37158 -0.02323 -0.00934 -0.05841 775 LEU A N   
2556 C CA  . LEU A 341 ? 0.22150 0.15043 0.23045 -0.02093 -0.00815 -0.05863 775 LEU A CA  
2557 C C   . LEU A 341 ? 0.35532 0.28629 0.35851 -0.02187 -0.00796 -0.06738 775 LEU A C   
2558 O O   . LEU A 341 ? 0.31147 0.23586 0.31255 -0.02665 -0.00954 -0.07288 775 LEU A O   
2559 C CB  . LEU A 341 ? 0.16944 0.11006 0.17932 -0.02511 -0.00964 -0.05283 775 LEU A CB  
2560 C CG  . LEU A 341 ? 0.22359 0.16436 0.23833 -0.02652 -0.01001 -0.04480 775 LEU A CG  
2561 C CD1 . LEU A 341 ? 0.22373 0.17840 0.23930 -0.02899 -0.01074 -0.04081 775 LEU A CD1 
2562 C CD2 . LEU A 341 ? 0.15967 0.09759 0.17661 -0.02047 -0.00807 -0.04081 775 LEU A CD2 
2563 N N   . LYS A 342 ? 0.32392 0.26449 0.32410 -0.01787 -0.00608 -0.06865 776 LYS A N   
2564 C CA  . LYS A 342 ? 0.19577 0.14226 0.18939 -0.01992 -0.00615 -0.07556 776 LYS A CA  
2565 C C   . LYS A 342 ? 0.26531 0.21994 0.25715 -0.02679 -0.00945 -0.07355 776 LYS A C   
2566 O O   . LYS A 342 ? 0.26254 0.22299 0.25808 -0.02798 -0.01073 -0.06621 776 LYS A O   
2567 C CB  . LYS A 342 ? 0.17939 0.13608 0.17014 -0.01510 -0.00360 -0.07570 776 LYS A CB  
2568 C CG  . LYS A 342 ? 0.26543 0.21707 0.25926 -0.00788 -0.00031 -0.07682 776 LYS A CG  
2569 C CD  . LYS A 342 ? 0.39616 0.35630 0.38538 -0.00467 0.00257  -0.08171 776 LYS A CD  
2570 C CE  . LYS A 342 ? 0.27008 0.24457 0.25524 -0.00705 0.00175  -0.07724 776 LYS A CE  
2571 N NZ  . LYS A 342 ? 0.36107 0.34445 0.34216 -0.00404 0.00485  -0.08048 776 LYS A NZ  
2572 N N   . THR A 343 ? 0.24993 0.20552 0.23625 -0.03127 -0.01083 -0.08048 777 THR A N   
2573 C CA  . THR A 343 ? 0.22269 0.18583 0.20792 -0.03832 -0.01456 -0.07908 777 THR A CA  
2574 C C   . THR A 343 ? 0.20927 0.18708 0.19531 -0.03741 -0.01558 -0.07180 777 THR A C   
2575 O O   . THR A 343 ? 0.18364 0.16695 0.17378 -0.04057 -0.01801 -0.06648 777 THR A O   
2576 C CB  . THR A 343 ? 0.29012 0.25394 0.26791 -0.04298 -0.01584 -0.08806 777 THR A CB  
2577 O OG1 . THR A 343 ? 0.40443 0.35292 0.38146 -0.04289 -0.01448 -0.09580 777 THR A OG1 
2578 C CG2 . THR A 343 ? 0.21551 0.18653 0.19309 -0.05095 -0.02028 -0.08669 777 THR A CG2 
2579 N N   . SER A 344 ? 0.17312 0.15738 0.15569 -0.03306 -0.01369 -0.07147 778 SER A N   
2580 C CA  . SER A 344 ? 0.23592 0.23243 0.21893 -0.03219 -0.01491 -0.06462 778 SER A CA  
2581 C C   . SER A 344 ? 0.16800 0.16392 0.15834 -0.02930 -0.01433 -0.05695 778 SER A C   
2582 O O   . SER A 344 ? 0.16973 0.17407 0.16253 -0.02970 -0.01611 -0.05130 778 SER A O   
2583 C CB  . SER A 344 ? 0.16052 0.16288 0.13803 -0.02876 -0.01286 -0.06561 778 SER A CB  
2584 O OG  . SER A 344 ? 0.15757 0.15424 0.13751 -0.02309 -0.00916 -0.06525 778 SER A OG  
2585 N N   . ALA A 345 ? 0.15042 0.13673 0.14427 -0.02621 -0.01190 -0.05670 779 ALA A N   
2586 C CA  . ALA A 345 ? 0.14918 0.13526 0.14910 -0.02419 -0.01132 -0.04981 779 ALA A CA  
2587 C C   . ALA A 345 ? 0.17468 0.16161 0.17898 -0.02905 -0.01363 -0.04725 779 ALA A C   
2588 O O   . ALA A 345 ? 0.17584 0.16945 0.18410 -0.02878 -0.01411 -0.04175 779 ALA A O   
2589 C CB  . ALA A 345 ? 0.14241 0.11882 0.14461 -0.02008 -0.00865 -0.04978 779 ALA A CB  
2590 N N   . THR A 346 ? 0.24606 0.22639 0.24990 -0.03365 -0.01492 -0.05146 780 THR A N   
2591 C CA  . THR A 346 ? 0.22724 0.21040 0.23492 -0.03956 -0.01739 -0.04942 780 THR A CA  
2592 C C   . THR A 346 ? 0.15537 0.15268 0.16322 -0.04152 -0.01996 -0.04752 780 THR A C   
2593 O O   . THR A 346 ? 0.14026 0.14499 0.15361 -0.04294 -0.02096 -0.04275 780 THR A O   
2594 C CB  . THR A 346 ? 0.17671 0.15024 0.18263 -0.04499 -0.01876 -0.05518 780 THR A CB  
2595 O OG1 . THR A 346 ? 0.24181 0.20134 0.24907 -0.04282 -0.01679 -0.05566 780 THR A OG1 
2596 C CG2 . THR A 346 ? 0.23936 0.21776 0.24913 -0.05224 -0.02160 -0.05318 780 THR A CG2 
2597 N N   . VAL A 347 ? 0.15316 0.15501 0.15522 -0.04139 -0.02104 -0.05100 781 VAL A N   
2598 C CA  . VAL A 347 ? 0.18685 0.20207 0.18885 -0.04303 -0.02412 -0.04856 781 VAL A CA  
2599 C C   . VAL A 347 ? 0.13366 0.15548 0.13957 -0.03792 -0.02331 -0.04182 781 VAL A C   
2600 O O   . VAL A 347 ? 0.22017 0.25126 0.23112 -0.03865 -0.02540 -0.03764 781 VAL A O   
2601 C CB  . VAL A 347 ? 0.15272 0.17109 0.14640 -0.04430 -0.02540 -0.05344 781 VAL A CB  
2602 C CG1 . VAL A 347 ? 0.14863 0.18091 0.14205 -0.04499 -0.02884 -0.04930 781 VAL A CG1 
2603 C CG2 . VAL A 347 ? 0.16600 0.17874 0.15592 -0.05032 -0.02672 -0.06083 781 VAL A CG2 
2604 N N   . SER A 348 ? 0.12970 0.14703 0.13374 -0.03267 -0.02030 -0.04092 782 SER A N   
2605 C CA  . SER A 348 ? 0.11986 0.14176 0.12704 -0.02817 -0.01946 -0.03514 782 SER A CA  
2606 C C   . SER A 348 ? 0.16791 0.19046 0.18258 -0.02808 -0.01879 -0.03139 782 SER A C   
2607 O O   . SER A 348 ? 0.12681 0.15714 0.14590 -0.02676 -0.01982 -0.02741 782 SER A O   
2608 C CB  . SER A 348 ? 0.11770 0.13431 0.12161 -0.02355 -0.01632 -0.03526 782 SER A CB  
2609 O OG  . SER A 348 ? 0.22596 0.24506 0.22311 -0.02349 -0.01667 -0.03789 782 SER A OG  
2610 N N   . ILE A 349 ? 0.14511 0.15968 0.16134 -0.02951 -0.01707 -0.03261 783 ILE A N   
2611 C CA  . ILE A 349 ? 0.11566 0.13120 0.13806 -0.02993 -0.01595 -0.02890 783 ILE A CA  
2612 C C   . ILE A 349 ? 0.17854 0.20367 0.20596 -0.03406 -0.01841 -0.02771 783 ILE A C   
2613 O O   . ILE A 349 ? 0.16261 0.19539 0.19553 -0.03262 -0.01798 -0.02413 783 ILE A O   
2614 C CB  . ILE A 349 ? 0.16664 0.17126 0.18898 -0.03129 -0.01415 -0.02979 783 ILE A CB  
2615 C CG1 . ILE A 349 ? 0.11548 0.11341 0.13505 -0.02608 -0.01159 -0.02951 783 ILE A CG1 
2616 C CG2 . ILE A 349 ? 0.18874 0.19573 0.21673 -0.03400 -0.01352 -0.02609 783 ILE A CG2 
2617 C CD1 . ILE A 349 ? 0.16967 0.15667 0.18959 -0.02640 -0.01025 -0.02964 783 ILE A CD1 
2618 N N   . ASN A 350 ? 0.20577 0.23134 0.23160 -0.03925 -0.02098 -0.03107 784 ASN A N   
2619 C CA  . ASN A 350 ? 0.14615 0.18243 0.17724 -0.04370 -0.02370 -0.02988 784 ASN A CA  
2620 C C   . ASN A 350 ? 0.15839 0.20687 0.19142 -0.04094 -0.02606 -0.02750 784 ASN A C   
2621 O O   . ASN A 350 ? 0.16105 0.22059 0.20096 -0.04221 -0.02765 -0.02497 784 ASN A O   
2622 C CB  . ASN A 350 ? 0.23826 0.27157 0.26672 -0.05077 -0.02620 -0.03436 784 ASN A CB  
2623 C CG  . ASN A 350 ? 0.36320 0.38704 0.39322 -0.05507 -0.02480 -0.03492 784 ASN A CG  
2624 O OD1 . ASN A 350 ? 0.42142 0.43201 0.44686 -0.05525 -0.02370 -0.03826 784 ASN A OD1 
2625 N ND2 . ASN A 350 ? 0.45007 0.48092 0.48692 -0.05842 -0.02480 -0.03140 784 ASN A ND2 
2626 N N   . ASN A 351 ? 0.13153 0.17871 0.15909 -0.03720 -0.02642 -0.02788 785 ASN A N   
2627 C CA  . ASN A 351 ? 0.13541 0.19271 0.16498 -0.03414 -0.02885 -0.02438 785 ASN A CA  
2628 C C   . ASN A 351 ? 0.10260 0.16211 0.13831 -0.02872 -0.02668 -0.02014 785 ASN A C   
2629 O O   . ASN A 351 ? 0.13028 0.19974 0.17257 -0.02708 -0.02848 -0.01709 785 ASN A O   
2630 C CB  . ASN A 351 ? 0.15920 0.21444 0.18060 -0.03246 -0.02982 -0.02536 785 ASN A CB  
2631 C CG  . ASN A 351 ? 0.17660 0.23438 0.19229 -0.03793 -0.03297 -0.02936 785 ASN A CG  
2632 O OD1 . ASN A 351 ? 0.12615 0.18924 0.14486 -0.04289 -0.03548 -0.03053 785 ASN A OD1 
2633 N ND2 . ASN A 351 ? 0.12677 0.18153 0.13398 -0.03745 -0.03277 -0.03170 785 ASN A ND2 
2634 N N   . VAL A 352 ? 0.09957 0.15022 0.13343 -0.02577 -0.02288 -0.02016 786 VAL A N   
2635 C CA  . VAL A 352 ? 0.09308 0.14530 0.13213 -0.02145 -0.02050 -0.01712 786 VAL A CA  
2636 C C   . VAL A 352 ? 0.10918 0.16827 0.15597 -0.02380 -0.01984 -0.01637 786 VAL A C   
2637 O O   . VAL A 352 ? 0.08788 0.15499 0.14131 -0.02084 -0.01962 -0.01417 786 VAL A O   
2638 C CB  . VAL A 352 ? 0.09900 0.14108 0.13403 -0.01893 -0.01685 -0.01746 786 VAL A CB  
2639 C CG1 . VAL A 352 ? 0.08549 0.12928 0.12468 -0.01471 -0.01456 -0.01491 786 VAL A CG1 
2640 C CG2 . VAL A 352 ? 0.13232 0.16914 0.16002 -0.01736 -0.01725 -0.01851 786 VAL A CG2 
2641 N N   . LEU A 353 ? 0.09573 0.15187 0.14198 -0.02924 -0.01947 -0.01825 787 LEU A N   
2642 C CA  . LEU A 353 ? 0.09540 0.15850 0.14854 -0.03277 -0.01868 -0.01723 787 LEU A CA  
2643 C C   . LEU A 353 ? 0.18705 0.26475 0.24736 -0.03339 -0.02163 -0.01603 787 LEU A C   
2644 O O   . LEU A 353 ? 0.09994 0.18719 0.16798 -0.03189 -0.02026 -0.01420 787 LEU A O   
2645 C CB  . LEU A 353 ? 0.10223 0.15847 0.15285 -0.03948 -0.01875 -0.01919 787 LEU A CB  
2646 C CG  . LEU A 353 ? 0.14371 0.18837 0.19118 -0.03982 -0.01556 -0.01886 787 LEU A CG  
2647 C CD1 . LEU A 353 ? 0.11283 0.14996 0.15833 -0.04661 -0.01666 -0.02072 787 LEU A CD1 
2648 C CD2 . LEU A 353 ? 0.11426 0.16439 0.16666 -0.03868 -0.01244 -0.01570 787 LEU A CD2 
2649 N N   . ARG A 354 ? 0.09855 0.17913 0.15657 -0.03563 -0.02572 -0.01717 788 ARG A N   
2650 C CA  . ARG A 354 ? 0.11104 0.20655 0.17624 -0.03632 -0.02925 -0.01551 788 ARG A CA  
2651 C C   . ARG A 354 ? 0.11329 0.21495 0.18328 -0.02863 -0.02954 -0.01236 788 ARG A C   
2652 O O   . ARG A 354 ? 0.16154 0.27611 0.24100 -0.02705 -0.03055 -0.01039 788 ARG A O   
2653 C CB  . ARG A 354 ? 0.13323 0.23052 0.19370 -0.04090 -0.03394 -0.01736 788 ARG A CB  
2654 C CG  . ARG A 354 ? 0.18702 0.28500 0.24740 -0.04967 -0.03522 -0.02013 788 ARG A CG  
2655 C CD  . ARG A 354 ? 0.24784 0.35326 0.30600 -0.05411 -0.04064 -0.02150 788 ARG A CD  
2656 N NE  . ARG A 354 ? 0.14461 0.24718 0.19575 -0.05001 -0.04232 -0.02137 788 ARG A NE  
2657 C CZ  . ARG A 354 ? 0.23375 0.32461 0.27458 -0.05088 -0.04154 -0.02512 788 ARG A CZ  
2658 N NH1 . ARG A 354 ? 0.20901 0.28876 0.24551 -0.05523 -0.03951 -0.02962 788 ARG A NH1 
2659 N NH2 . ARG A 354 ? 0.29316 0.38356 0.32816 -0.04725 -0.04281 -0.02422 788 ARG A NH2 
2660 N N   . ALA A 355 ? 0.09471 0.18740 0.15883 -0.02380 -0.02870 -0.01187 789 ALA A N   
2661 C CA  . ALA A 355 ? 0.11723 0.21329 0.18520 -0.01681 -0.02940 -0.00880 789 ALA A CA  
2662 C C   . ALA A 355 ? 0.10704 0.20435 0.18156 -0.01239 -0.02527 -0.00833 789 ALA A C   
2663 O O   . ALA A 355 ? 0.08305 0.18629 0.16426 -0.00683 -0.02599 -0.00630 789 ALA A O   
2664 C CB  . ALA A 355 ? 0.11541 0.20127 0.17454 -0.01414 -0.02980 -0.00825 789 ALA A CB  
2665 N N   . HIS A 356 ? 0.08275 0.17460 0.15543 -0.01464 -0.02107 -0.01019 790 HIS A N   
2666 C CA  . HIS A 356 ? 0.09972 0.19279 0.17691 -0.01115 -0.01680 -0.01025 790 HIS A CA  
2667 C C   . HIS A 356 ? 0.14797 0.25136 0.23226 -0.01478 -0.01476 -0.01075 790 HIS A C   
2668 O O   . HIS A 356 ? 0.17162 0.27880 0.26026 -0.01210 -0.01102 -0.01114 790 HIS A O   
2669 C CB  . HIS A 356 ? 0.15168 0.23163 0.22100 -0.01059 -0.01340 -0.01122 790 HIS A CB  
2670 C CG  . HIS A 356 ? 0.10474 0.17734 0.17000 -0.00538 -0.01387 -0.01043 790 HIS A CG  
2671 N ND1 . HIS A 356 ? 0.13153 0.20483 0.20054 0.00022  -0.01228 -0.01002 790 HIS A ND1 
2672 C CD2 . HIS A 356 ? 0.09704 0.16176 0.15489 -0.00529 -0.01576 -0.01003 790 HIS A CD2 
2673 C CE1 . HIS A 356 ? 0.14778 0.21304 0.21176 0.00310  -0.01344 -0.00897 790 HIS A CE1 
2674 N NE2 . HIS A 356 ? 0.08929 0.15009 0.14651 -0.00024 -0.01547 -0.00875 790 HIS A NE2 
2675 N N   . ALA A 357 ? 0.15288 0.26122 0.23817 -0.02124 -0.01702 -0.01095 791 ALA A N   
2676 C CA  . ALA A 357 ? 0.19012 0.31085 0.28328 -0.02542 -0.01570 -0.01080 791 ALA A CA  
2677 C C   . ALA A 357 ? 0.08038 0.21579 0.18467 -0.02000 -0.01468 -0.01009 791 ALA A C   
2678 O O   . ALA A 357 ? 0.07912 0.22210 0.18849 -0.02100 -0.01074 -0.01054 791 ALA A O   
2679 C CB  . ALA A 357 ? 0.08610 0.21143 0.17959 -0.03288 -0.01968 -0.01099 791 ALA A CB  
2680 N N   . PRO A 358 ? 0.09493 0.23523 0.20363 -0.01416 -0.01791 -0.00894 792 PRO A N   
2681 C CA  . PRO A 358 ? 0.08775 0.24160 0.20828 -0.00803 -0.01670 -0.00862 792 PRO A CA  
2682 C C   . PRO A 358 ? 0.07467 0.22441 0.19550 -0.00276 -0.01117 -0.01048 792 PRO A C   
2683 O O   . PRO A 358 ? 0.07392 0.23601 0.20415 0.00002  -0.00815 -0.01164 792 PRO A O   
2684 C CB  . PRO A 358 ? 0.07803 0.23326 0.20105 -0.00247 -0.02195 -0.00629 792 PRO A CB  
2685 C CG  . PRO A 358 ? 0.07980 0.22012 0.19038 -0.00489 -0.02451 -0.00578 792 PRO A CG  
2686 C CD  . PRO A 358 ? 0.15049 0.28659 0.25473 -0.01351 -0.02323 -0.00760 792 PRO A CD  
2687 N N   . PHE A 359 ? 0.07442 0.20821 0.18538 -0.00150 -0.00962 -0.01116 793 PHE A N   
2688 C CA  . PHE A 359 ? 0.07370 0.20302 0.18419 0.00359  -0.00502 -0.01316 793 PHE A CA  
2689 C C   . PHE A 359 ? 0.07605 0.20215 0.18123 -0.00123 -0.00021 -0.01460 793 PHE A C   
2690 O O   . PHE A 359 ? 0.13779 0.26545 0.24431 0.00178  0.00418  -0.01676 793 PHE A O   
2691 C CB  . PHE A 359 ? 0.09015 0.20493 0.19377 0.00830  -0.00656 -0.01266 793 PHE A CB  
2692 C CG  . PHE A 359 ? 0.10601 0.22168 0.21226 0.01169  -0.01207 -0.00999 793 PHE A CG  
2693 C CD1 . PHE A 359 ? 0.07838 0.20091 0.19429 0.01885  -0.01325 -0.00941 793 PHE A CD1 
2694 C CD2 . PHE A 359 ? 0.12212 0.23195 0.22113 0.00780  -0.01612 -0.00804 793 PHE A CD2 
2695 C CE1 . PHE A 359 ? 0.08114 0.20458 0.19935 0.02180  -0.01888 -0.00591 793 PHE A CE1 
2696 C CE2 . PHE A 359 ? 0.07998 0.19158 0.18047 0.01023  -0.02136 -0.00509 793 PHE A CE2 
2697 C CZ  . PHE A 359 ? 0.09789 0.21623 0.20792 0.01710  -0.02301 -0.00351 793 PHE A CZ  
2698 N N   . TRP A 360 ? 0.07358 0.19508 0.17270 -0.00861 -0.00102 -0.01347 794 TRP A N   
2699 C CA  . TRP A 360 ? 0.07417 0.19084 0.16749 -0.01333 0.00272  -0.01365 794 TRP A CA  
2700 C C   . TRP A 360 ? 0.07840 0.20309 0.17441 -0.02139 0.00263  -0.01237 794 TRP A C   
2701 O O   . TRP A 360 ? 0.07841 0.19711 0.17047 -0.02655 -0.00046 -0.01127 794 TRP A O   
2702 C CB  . TRP A 360 ? 0.14623 0.24598 0.22873 -0.01396 0.00179  -0.01313 794 TRP A CB  
2703 C CG  . TRP A 360 ? 0.07333 0.16584 0.15332 -0.00706 0.00165  -0.01403 794 TRP A CG  
2704 C CD1 . TRP A 360 ? 0.07851 0.16501 0.15630 -0.00405 -0.00203 -0.01336 794 TRP A CD1 
2705 C CD2 . TRP A 360 ? 0.08709 0.17790 0.16634 -0.00294 0.00528  -0.01575 794 TRP A CD2 
2706 N NE1 . TRP A 360 ? 0.07324 0.15366 0.14914 0.00145  -0.00103 -0.01406 794 TRP A NE1 
2707 C CE2 . TRP A 360 ? 0.07708 0.15969 0.15391 0.00229  0.00340  -0.01591 794 TRP A CE2 
2708 C CE3 . TRP A 360 ? 0.07362 0.16925 0.15347 -0.00371 0.00993  -0.01727 794 TRP A CE3 
2709 C CZ2 . TRP A 360 ? 0.12516 0.20315 0.20040 0.00665  0.00585  -0.01780 794 TRP A CZ2 
2710 C CZ3 . TRP A 360 ? 0.12548 0.21726 0.20336 0.00086  0.01252  -0.01964 794 TRP A CZ3 
2711 C CH2 . TRP A 360 ? 0.10200 0.18452 0.17775 0.00594  0.01039  -0.02003 794 TRP A CH2 
2712 N N   . SER A 361 ? 0.18476 0.32298 0.28733 -0.02274 0.00624  -0.01279 795 SER A N   
2713 C CA  . SER A 361 ? 0.09561 0.24469 0.20269 -0.03062 0.00617  -0.01127 795 SER A CA  
2714 C C   . SER A 361 ? 0.13062 0.26935 0.22952 -0.03873 0.00643  -0.00909 795 SER A C   
2715 O O   . SER A 361 ? 0.08614 0.22887 0.18689 -0.04634 0.00483  -0.00746 795 SER A O   
2716 C CB  . SER A 361 ? 0.07804 0.24522 0.19399 -0.02985 0.01071  -0.01234 795 SER A CB  
2717 O OG  . SER A 361 ? 0.10950 0.28761 0.22927 -0.03858 0.01110  -0.01038 795 SER A OG  
2718 N N   . SER A 362 ? 0.09640 0.22194 0.18670 -0.03742 0.00813  -0.00882 796 SER A N   
2719 C CA  . SER A 362 ? 0.12195 0.23701 0.20510 -0.04423 0.00806  -0.00619 796 SER A CA  
2720 C C   . SER A 362 ? 0.11744 0.21877 0.19566 -0.04615 0.00356  -0.00602 796 SER A C   
2721 O O   . SER A 362 ? 0.11659 0.20900 0.19038 -0.05210 0.00276  -0.00400 796 SER A O   
2722 C CB  . SER A 362 ? 0.13688 0.24430 0.21317 -0.04201 0.01122  -0.00563 796 SER A CB  
2723 O OG  . SER A 362 ? 0.14020 0.23801 0.21259 -0.03492 0.01019  -0.00758 796 SER A OG  
2724 N N   . LEU A 363 ? 0.17536 0.27468 0.25410 -0.04132 0.00064  -0.00809 797 LEU A N   
2725 C CA  . LEU A 363 ? 0.14231 0.23088 0.21646 -0.04333 -0.00338 -0.00882 797 LEU A CA  
2726 C C   . LEU A 363 ? 0.09796 0.19253 0.17594 -0.05102 -0.00592 -0.00852 797 LEU A C   
2727 O O   . LEU A 363 ? 0.20698 0.29147 0.28059 -0.05669 -0.00753 -0.00833 797 LEU A O   
2728 C CB  . LEU A 363 ? 0.08729 0.17434 0.16072 -0.03679 -0.00579 -0.01068 797 LEU A CB  
2729 C CG  . LEU A 363 ? 0.15464 0.23387 0.22347 -0.02992 -0.00400 -0.01107 797 LEU A CG  
2730 C CD1 . LEU A 363 ? 0.09755 0.17708 0.16662 -0.02439 -0.00665 -0.01202 797 LEU A CD1 
2731 C CD2 . LEU A 363 ? 0.13042 0.19492 0.19102 -0.03133 -0.00353 -0.01074 797 LEU A CD2 
2732 N N   . PRO B 8   ? 0.44740 0.47692 0.25215 -0.02002 -0.04060 0.09366  442 PRO B N   
2733 C CA  . PRO B 8   ? 0.42605 0.46452 0.25711 -0.02288 -0.04331 0.09433  442 PRO B CA  
2734 C C   . PRO B 8   ? 0.42891 0.47131 0.27177 -0.02480 -0.03160 0.09598  442 PRO B C   
2735 O O   . PRO B 8   ? 0.43293 0.47477 0.28483 -0.02527 -0.02759 0.10354  442 PRO B O   
2736 C CB  . PRO B 8   ? 0.40406 0.43919 0.24018 -0.02150 -0.04981 0.10234  442 PRO B CB  
2737 C CG  . PRO B 8   ? 0.45511 0.48032 0.26998 -0.01935 -0.04430 0.10904  442 PRO B CG  
2738 C CD  . PRO B 8   ? 0.48020 0.50255 0.27532 -0.01788 -0.03678 0.10333  442 PRO B CD  
2739 N N   . ILE B 9   ? 0.35555 0.40159 0.19918 -0.02605 -0.02704 0.08897  443 ILE B N   
2740 C CA  . ILE B 9   ? 0.27559 0.32392 0.12666 -0.02659 -0.01521 0.08938  443 ILE B CA  
2741 C C   . ILE B 9   ? 0.25034 0.30773 0.12158 -0.02929 -0.01685 0.08562  443 ILE B C   
2742 O O   . ILE B 9   ? 0.24431 0.30585 0.11733 -0.03099 -0.02406 0.07981  443 ILE B O   
2743 C CB  . ILE B 9   ? 0.31697 0.35947 0.14858 -0.02431 -0.00722 0.08451  443 ILE B CB  
2744 C CG1 . ILE B 9   ? 0.34514 0.37839 0.15324 -0.02066 -0.00612 0.08775  443 ILE B CG1 
2745 C CG2 . ILE B 9   ? 0.28214 0.32696 0.12246 -0.02373 0.00504  0.08517  443 ILE B CG2 
2746 C CD1 . ILE B 9   ? 0.39357 0.41972 0.17933 -0.01692 0.00146  0.08258  443 ILE B CD1 
2747 N N   . THR B 10  ? 0.29281 0.35363 0.17943 -0.02974 -0.01038 0.08905  444 THR B N   
2748 C CA  . THR B 10  ? 0.21540 0.28380 0.11908 -0.03140 -0.01006 0.08579  444 THR B CA  
2749 C C   . THR B 10  ? 0.21684 0.28421 0.11906 -0.03085 0.00044  0.08217  444 THR B C   
2750 O O   . THR B 10  ? 0.22156 0.28583 0.12210 -0.02899 0.00882  0.08540  444 THR B O   
2751 C CB  . THR B 10  ? 0.20316 0.27506 0.12544 -0.03165 -0.01222 0.09160  444 THR B CB  
2752 O OG1 . THR B 10  ? 0.22760 0.29900 0.15118 -0.03101 -0.02303 0.09443  444 THR B OG1 
2753 C CG2 . THR B 10  ? 0.18335 0.26256 0.12070 -0.03242 -0.01167 0.08807  444 THR B CG2 
2754 N N   . GLY B 11  ? 0.20542 0.27557 0.10869 -0.03245 -0.00030 0.07578  445 GLY B N   
2755 C CA  . GLY B 11  ? 0.20259 0.27117 0.10656 -0.03163 0.00832  0.07235  445 GLY B CA  
2756 C C   . GLY B 11  ? 0.26049 0.33482 0.18525 -0.03184 0.01077  0.07356  445 GLY B C   
2757 O O   . GLY B 11  ? 0.23382 0.31419 0.17097 -0.03315 0.00479  0.07535  445 GLY B O   
2758 N N   . LEU B 12  ? 0.18262 0.25485 0.11011 -0.02976 0.01919  0.07250  446 LEU B N   
2759 C CA  . LEU B 12  ? 0.20314 0.27954 0.14873 -0.02948 0.02109  0.07264  446 LEU B CA  
2760 C C   . LEU B 12  ? 0.18750 0.26046 0.12961 -0.02772 0.02809  0.06844  446 LEU B C   
2761 O O   . LEU B 12  ? 0.19410 0.26286 0.12560 -0.02490 0.03483  0.06849  446 LEU B O   
2762 C CB  . LEU B 12  ? 0.16407 0.24250 0.12171 -0.02848 0.02265  0.07897  446 LEU B CB  
2763 C CG  . LEU B 12  ? 0.14982 0.23254 0.12654 -0.02823 0.02260  0.08034  446 LEU B CG  
2764 C CD1 . LEU B 12  ? 0.15010 0.23476 0.13703 -0.02927 0.01976  0.08796  446 LEU B CD1 
2765 C CD2 . LEU B 12  ? 0.15028 0.23201 0.12967 -0.02577 0.03051  0.07806  446 LEU B CD2 
2766 N N   . VAL B 13  ? 0.16277 0.23760 0.11257 -0.02906 0.02658  0.06518  447 VAL B N   
2767 C CA  . VAL B 13  ? 0.16905 0.24023 0.11651 -0.02756 0.03224  0.06213  447 VAL B CA  
2768 C C   . VAL B 13  ? 0.21935 0.29403 0.18466 -0.02616 0.03316  0.06313  447 VAL B C   
2769 O O   . VAL B 13  ? 0.13432 0.21364 0.11051 -0.02769 0.02761  0.06354  447 VAL B O   
2770 C CB  . VAL B 13  ? 0.16450 0.23260 0.10193 -0.03136 0.02905  0.05772  447 VAL B CB  
2771 C CG1 . VAL B 13  ? 0.15031 0.22405 0.09990 -0.03499 0.02265  0.05691  447 VAL B CG1 
2772 C CG2 . VAL B 13  ? 0.17232 0.23225 0.10502 -0.02868 0.03419  0.05378  447 VAL B CG2 
2773 N N   . TYR B 14  ? 0.15001 0.22340 0.11744 -0.02271 0.03999  0.06365  448 TYR B N   
2774 C CA  . TYR B 14  ? 0.14114 0.21793 0.12442 -0.02107 0.04064  0.06484  448 TYR B CA  
2775 C C   . TYR B 14  ? 0.15005 0.22516 0.13055 -0.01711 0.04853  0.06425  448 TYR B C   
2776 O O   . TYR B 14  ? 0.27599 0.34999 0.24660 -0.01427 0.05472  0.06452  448 TYR B O   
2777 C CB  . TYR B 14  ? 0.13380 0.21600 0.13036 -0.02080 0.03887  0.06961  448 TYR B CB  
2778 C CG  . TYR B 14  ? 0.19752 0.28387 0.20947 -0.01876 0.04005  0.07162  448 TYR B CG  
2779 C CD1 . TYR B 14  ? 0.11542 0.20358 0.13683 -0.01936 0.03470  0.07100  448 TYR B CD1 
2780 C CD2 . TYR B 14  ? 0.19869 0.28847 0.21574 -0.01601 0.04642  0.07460  448 TYR B CD2 
2781 C CE1 . TYR B 14  ? 0.13038 0.22247 0.16546 -0.01747 0.03488  0.07340  448 TYR B CE1 
2782 C CE2 . TYR B 14  ? 0.12644 0.22151 0.15916 -0.01422 0.04672  0.07708  448 TYR B CE2 
2783 C CZ  . TYR B 14  ? 0.11528 0.21088 0.15680 -0.01506 0.04053  0.07650  448 TYR B CZ  
2784 O OH  . TYR B 14  ? 0.11369 0.21451 0.17068 -0.01328 0.03998  0.07941  448 TYR B OH  
2785 N N   . ASP B 15  ? 0.15148 0.22693 0.13990 -0.01611 0.04849  0.06375  449 ASP B N   
2786 C CA  . ASP B 15  ? 0.18513 0.25983 0.17237 -0.01105 0.05598  0.06391  449 ASP B CA  
2787 C C   . ASP B 15  ? 0.15368 0.23251 0.15790 -0.00964 0.05441  0.06606  449 ASP B C   
2788 O O   . ASP B 15  ? 0.20801 0.28405 0.21422 -0.01217 0.04897  0.06484  449 ASP B O   
2789 C CB  . ASP B 15  ? 0.35632 0.41843 0.32724 -0.01071 0.05529  0.05748  449 ASP B CB  
2790 C CG  . ASP B 15  ? 0.25229 0.30853 0.21713 -0.00319 0.06203  0.05423  449 ASP B CG  
2791 O OD1 . ASP B 15  ? 0.28126 0.34049 0.25823 0.00100  0.06451  0.05572  449 ASP B OD1 
2792 O OD2 . ASP B 15  ? 0.21087 0.25938 0.15840 -0.00070 0.06436  0.04976  449 ASP B OD2 
2793 N N   . GLN B 16  ? 0.13652 0.22213 0.15278 -0.00557 0.05856  0.06906  450 GLN B N   
2794 C CA  . GLN B 16  ? 0.16354 0.25460 0.19756 -0.00430 0.05598  0.07197  450 GLN B CA  
2795 C C   . GLN B 16  ? 0.12890 0.21284 0.16079 -0.00147 0.05542  0.06905  450 GLN B C   
2796 O O   . GLN B 16  ? 0.14960 0.23528 0.19285 -0.00114 0.05069  0.07040  450 GLN B O   
2797 C CB  . GLN B 16  ? 0.16844 0.26884 0.21629 -0.00057 0.06049  0.07584  450 GLN B CB  
2798 C CG  . GLN B 16  ? 0.22003 0.32302 0.26921 0.00706  0.06956  0.07586  450 GLN B CG  
2799 C CD  . GLN B 16  ? 0.33540 0.44817 0.39264 0.01082  0.07583  0.07869  450 GLN B CD  
2800 O OE1 . GLN B 16  ? 0.45867 0.57680 0.52436 0.00679  0.07261  0.08236  450 GLN B OE1 
2801 N NE2 . GLN B 16  ? 0.58555 0.70054 0.63968 0.01912  0.08517  0.07721  450 GLN B NE2 
2802 N N   . ARG B 17  ? 0.14246 0.21527 0.15870 0.00071  0.05800  0.06376  451 ARG B N   
2803 C CA  . ARG B 17  ? 0.15678 0.21794 0.16905 0.00247  0.05485  0.06004  451 ARG B CA  
2804 C C   . ARG B 17  ? 0.16308 0.22192 0.17618 -0.00355 0.04685  0.06065  451 ARG B C   
2805 O O   . ARG B 17  ? 0.14019 0.19323 0.15525 -0.00248 0.04353  0.06053  451 ARG B O   
2806 C CB  . ARG B 17  ? 0.21713 0.26408 0.21087 0.00416  0.05671  0.05391  451 ARG B CB  
2807 C CG  . ARG B 17  ? 0.23900 0.28320 0.23027 0.01362  0.06375  0.05115  451 ARG B CG  
2808 C CD  . ARG B 17  ? 0.33121 0.35841 0.30146 0.01513  0.06347  0.04375  451 ARG B CD  
2809 N NE  . ARG B 17  ? 0.29919 0.32789 0.25711 0.01130  0.06438  0.04266  451 ARG B NE  
2810 C CZ  . ARG B 17  ? 0.33444 0.34900 0.27349 0.00992  0.06148  0.03645  451 ARG B CZ  
2811 N NH1 . ARG B 17  ? 0.27236 0.26899 0.20286 0.01115  0.05707  0.03086  451 ARG B NH1 
2812 N NH2 . ARG B 17  ? 0.26154 0.27898 0.19006 0.00704  0.06194  0.03606  451 ARG B NH2 
2813 N N   . MET B 18  ? 0.14442 0.20808 0.15550 -0.00925 0.04382  0.06154  452 MET B N   
2814 C CA  . MET B 18  ? 0.12383 0.18803 0.13567 -0.01372 0.03735  0.06202  452 MET B CA  
2815 C C   . MET B 18  ? 0.13894 0.21000 0.16434 -0.01169 0.03382  0.06510  452 MET B C   
2816 O O   . MET B 18  ? 0.10986 0.18161 0.13474 -0.01375 0.02884  0.06531  452 MET B O   
2817 C CB  . MET B 18  ? 0.11906 0.18783 0.12616 -0.01879 0.03500  0.06161  452 MET B CB  
2818 C CG  . MET B 18  ? 0.12881 0.18960 0.12204 -0.02270 0.03464  0.05816  452 MET B CG  
2819 S SD  . MET B 18  ? 0.15048 0.21801 0.13962 -0.02796 0.03110  0.05770  452 MET B SD  
2820 C CE  . MET B 18  ? 0.19422 0.26382 0.18078 -0.02500 0.03563  0.05873  452 MET B CE  
2821 N N   . MET B 19  ? 0.14260 0.21935 0.18006 -0.00758 0.03608  0.06758  453 MET B N   
2822 C CA  . MET B 19  ? 0.10485 0.18699 0.15601 -0.00557 0.03124  0.07014  453 MET B CA  
2823 C C   . MET B 19  ? 0.13086 0.20654 0.18234 -0.00186 0.02950  0.06971  453 MET B C   
2824 O O   . MET B 19  ? 0.12244 0.20019 0.18071 -0.00063 0.02353  0.07107  453 MET B O   
2825 C CB  . MET B 19  ? 0.10122 0.19321 0.16811 -0.00359 0.03357  0.07403  453 MET B CB  
2826 C CG  . MET B 19  ? 0.09648 0.19462 0.16553 -0.00759 0.03330  0.07630  453 MET B CG  
2827 S SD  . MET B 19  ? 0.15843 0.26769 0.24703 -0.00659 0.03579  0.08246  453 MET B SD  
2828 C CE  . MET B 19  ? 0.08753 0.20074 0.19416 -0.00659 0.02532  0.08459  453 MET B CE  
2829 N N   . LEU B 20  ? 0.12093 0.18745 0.16419 0.00035  0.03361  0.06766  454 LEU B N   
2830 C CA  . LEU B 20  ? 0.12842 0.18713 0.17227 0.00454  0.03150  0.06777  454 LEU B CA  
2831 C C   . LEU B 20  ? 0.14925 0.20301 0.18648 0.00132  0.02509  0.06877  454 LEU B C   
2832 O O   . LEU B 20  ? 0.13277 0.18275 0.17283 0.00471  0.02129  0.07046  454 LEU B O   
2833 C CB  . LEU B 20  ? 0.14290 0.18981 0.17704 0.00758  0.03612  0.06456  454 LEU B CB  
2834 C CG  . LEU B 20  ? 0.14675 0.19869 0.18456 0.01273  0.04386  0.06313  454 LEU B CG  
2835 C CD1 . LEU B 20  ? 0.16388 0.20156 0.18631 0.01526  0.04730  0.05797  454 LEU B CD1 
2836 C CD2 . LEU B 20  ? 0.14494 0.20586 0.20043 0.02002  0.04528  0.06572  454 LEU B CD2 
2837 N N   . HIS B 21  ? 0.12536 0.18011 0.15390 -0.00468 0.02401  0.06818  455 HIS B N   
2838 C CA  . HIS B 21  ? 0.12591 0.17963 0.14832 -0.00749 0.01933  0.06984  455 HIS B CA  
2839 C C   . HIS B 21  ? 0.13915 0.20092 0.16988 -0.00441 0.01399  0.07115  455 HIS B C   
2840 O O   . HIS B 21  ? 0.18025 0.25076 0.21740 -0.00469 0.01266  0.07022  455 HIS B O   
2841 C CB  . HIS B 21  ? 0.12331 0.18018 0.13753 -0.01386 0.02014  0.06885  455 HIS B CB  
2842 C CG  . HIS B 21  ? 0.12176 0.18368 0.13180 -0.01592 0.01661  0.07071  455 HIS B CG  
2843 N ND1 . HIS B 21  ? 0.13097 0.18699 0.13440 -0.01686 0.01507  0.07401  455 HIS B ND1 
2844 C CD2 . HIS B 21  ? 0.11399 0.18656 0.12470 -0.01652 0.01461  0.06985  455 HIS B CD2 
2845 C CE1 . HIS B 21  ? 0.14264 0.20711 0.14238 -0.01798 0.01327  0.07539  455 HIS B CE1 
2846 N NE2 . HIS B 21  ? 0.11853 0.19303 0.12266 -0.01720 0.01283  0.07225  455 HIS B NE2 
2847 N N   . HIS B 22  ? 0.12636 0.18389 0.15637 -0.00132 0.00983  0.07326  456 HIS B N   
2848 C CA  . HIS B 22  ? 0.12085 0.18446 0.15871 0.00251  0.00337  0.07371  456 HIS B CA  
2849 C C   . HIS B 22  ? 0.13004 0.18951 0.15845 0.00401  -0.00163 0.07591  456 HIS B C   
2850 O O   . HIS B 22  ? 0.14882 0.19972 0.16763 0.00252  0.00001  0.07849  456 HIS B O   
2851 C CB  . HIS B 22  ? 0.18061 0.24624 0.23428 0.00732  0.00247  0.07431  456 HIS B CB  
2852 C CG  . HIS B 22  ? 0.18316 0.24008 0.23672 0.01146  0.00263  0.07597  456 HIS B CG  
2853 N ND1 . HIS B 22  ? 0.13889 0.18777 0.18789 0.01163  0.00874  0.07525  456 HIS B ND1 
2854 C CD2 . HIS B 22  ? 0.13618 0.18993 0.19297 0.01625  -0.00355 0.07799  456 HIS B CD2 
2855 C CE1 . HIS B 22  ? 0.17437 0.21512 0.22432 0.01661  0.00648  0.07673  456 HIS B CE1 
2856 N NE2 . HIS B 22  ? 0.16186 0.20589 0.21684 0.01935  -0.00088 0.07880  456 HIS B NE2 
2857 N N   . ASN B 23  ? 0.18004 0.24491 0.21055 0.00700  -0.00835 0.07505  457 ASN B N   
2858 C CA  . ASN B 23  ? 0.13736 0.19947 0.15792 0.00999  -0.01404 0.07690  457 ASN B CA  
2859 C C   . ASN B 23  ? 0.18178 0.24008 0.21169 0.01550  -0.02028 0.07819  457 ASN B C   
2860 O O   . ASN B 23  ? 0.19192 0.25535 0.23403 0.01835  -0.02626 0.07616  457 ASN B O   
2861 C CB  . ASN B 23  ? 0.13549 0.20504 0.15073 0.01141  -0.01855 0.07383  457 ASN B CB  
2862 C CG  . ASN B 23  ? 0.20016 0.26799 0.20036 0.01478  -0.02279 0.07570  457 ASN B CG  
2863 O OD1 . ASN B 23  ? 0.27190 0.33350 0.27088 0.01843  -0.02774 0.07826  457 ASN B OD1 
2864 N ND2 . ASN B 23  ? 0.15017 0.22440 0.13849 0.01413  -0.02073 0.07468  457 ASN B ND2 
2865 N N   . MET B 24  ? 0.18935 0.23835 0.21461 0.01685  -0.01972 0.08185  458 MET B N   
2866 C CA  . MET B 24  ? 0.15817 0.20368 0.19335 0.02278  -0.02562 0.08329  458 MET B CA  
2867 C C   . MET B 24  ? 0.24409 0.28901 0.27339 0.02723  -0.03582 0.08420  458 MET B C   
2868 O O   . MET B 24  ? 0.22314 0.26600 0.26140 0.03244  -0.04262 0.08534  458 MET B O   
2869 C CB  . MET B 24  ? 0.16876 0.20252 0.20057 0.02368  -0.02228 0.08649  458 MET B CB  
2870 C CG  . MET B 24  ? 0.21007 0.23461 0.22237 0.01956  -0.02031 0.09042  458 MET B CG  
2871 S SD  . MET B 24  ? 0.46520 0.47220 0.47409 0.02015  -0.01804 0.09379  458 MET B SD  
2872 C CE  . MET B 24  ? 0.23777 0.24878 0.26189 0.02123  -0.01102 0.08797  458 MET B CE  
2873 N N   . TRP B 25  ? 0.25754 0.30477 0.27176 0.02607  -0.03725 0.08350  459 TRP B N   
2874 C CA  . TRP B 25  ? 0.29314 0.33948 0.29787 0.03123  -0.04694 0.08352  459 TRP B CA  
2875 C C   . TRP B 25  ? 0.28700 0.34096 0.29521 0.03320  -0.05330 0.07751  459 TRP B C   
2876 O O   . TRP B 25  ? 0.50750 0.56009 0.50826 0.03847  -0.06309 0.07590  459 TRP B O   
2877 C CB  . TRP B 25  ? 0.23700 0.27951 0.21841 0.03011  -0.04409 0.08797  459 TRP B CB  
2878 C CG  . TRP B 25  ? 0.32409 0.35658 0.30163 0.02707  -0.03896 0.09441  459 TRP B CG  
2879 C CD1 . TRP B 25  ? 0.39081 0.41267 0.36593 0.03072  -0.04403 0.09924  459 TRP B CD1 
2880 C CD2 . TRP B 25  ? 0.42248 0.45291 0.39838 0.01993  -0.02918 0.09644  459 TRP B CD2 
2881 N NE1 . TRP B 25  ? 0.46346 0.47554 0.43519 0.02639  -0.03802 0.10410  459 TRP B NE1 
2882 C CE2 . TRP B 25  ? 0.44283 0.45983 0.41498 0.01947  -0.02913 0.10229  459 TRP B CE2 
2883 C CE3 . TRP B 25  ? 0.38170 0.41948 0.35892 0.01403  -0.02158 0.09376  459 TRP B CE3 
2884 C CZ2 . TRP B 25  ? 0.48440 0.49408 0.45393 0.01295  -0.02226 0.10508  459 TRP B CZ2 
2885 C CZ3 . TRP B 25  ? 0.45516 0.48715 0.43001 0.00749  -0.01465 0.09670  459 TRP B CZ3 
2886 C CH2 . TRP B 25  ? 0.50870 0.52624 0.47966 0.00681  -0.01526 0.10210  459 TRP B CH2 
2887 N N   . ASP B 26  ? 0.18141 0.24189 0.19977 0.02944  -0.04894 0.07404  460 ASP B N   
2888 C CA  . ASP B 26  ? 0.21738 0.28288 0.24009 0.03105  -0.05586 0.06834  460 ASP B CA  
2889 C C   . ASP B 26  ? 0.19355 0.26433 0.23335 0.02607  -0.05052 0.06722  460 ASP B C   
2890 O O   . ASP B 26  ? 0.20062 0.27456 0.23518 0.02233  -0.04295 0.06627  460 ASP B O   
2891 C CB  . ASP B 26  ? 0.16482 0.23257 0.16758 0.03292  -0.05565 0.06529  460 ASP B CB  
2892 C CG  . ASP B 26  ? 0.17810 0.24866 0.18439 0.03560  -0.06360 0.05830  460 ASP B CG  
2893 O OD1 . ASP B 26  ? 0.30865 0.37811 0.33247 0.03562  -0.07148 0.05662  460 ASP B OD1 
2894 O OD2 . ASP B 26  ? 0.16717 0.24118 0.15948 0.03777  -0.06220 0.05468  460 ASP B OD2 
2895 N N   . SER B 27  ? 0.17357 0.24621 0.23404 0.02611  -0.05474 0.06796  461 SER B N   
2896 C CA  . SER B 27  ? 0.16580 0.24426 0.24317 0.02157  -0.04972 0.06841  461 SER B CA  
2897 C C   . SER B 27  ? 0.23143 0.31234 0.30923 0.01984  -0.05359 0.06443  461 SER B C   
2898 O O   . SER B 27  ? 0.17732 0.26248 0.26726 0.01565  -0.04971 0.06552  461 SER B O   
2899 C CB  . SER B 27  ? 0.17083 0.25322 0.27166 0.02232  -0.05363 0.07127  461 SER B CB  
2900 O OG  . SER B 27  ? 0.22218 0.30317 0.32906 0.02439  -0.06658 0.06811  461 SER B OG  
2901 N N   . HIS B 28  ? 0.18256 0.26044 0.24677 0.02364  -0.06133 0.05989  462 HIS B N   
2902 C CA  . HIS B 28  ? 0.20438 0.28281 0.26713 0.02360  -0.06586 0.05506  462 HIS B CA  
2903 C C   . HIS B 28  ? 0.19830 0.27849 0.24154 0.02447  -0.05915 0.05241  462 HIS B C   
2904 O O   . HIS B 28  ? 0.13203 0.21253 0.17118 0.02643  -0.06327 0.04746  462 HIS B O   
2905 C CB  . HIS B 28  ? 0.20233 0.27478 0.26465 0.02845  -0.08017 0.04915  462 HIS B CB  
2906 C CG  . HIS B 28  ? 0.14166 0.21189 0.22364 0.02543  -0.08438 0.04912  462 HIS B CG  
2907 N ND1 . HIS B 28  ? 0.16221 0.23153 0.25756 0.02078  -0.08617 0.04805  462 HIS B ND1 
2908 C CD2 . HIS B 28  ? 0.14704 0.21658 0.23802 0.02597  -0.08711 0.05110  462 HIS B CD2 
2909 C CE1 . HIS B 28  ? 0.17241 0.24140 0.28459 0.01791  -0.08956 0.05004  462 HIS B CE1 
2910 N NE2 . HIS B 28  ? 0.14476 0.21455 0.25505 0.02130  -0.09013 0.05142  462 HIS B NE2 
2911 N N   . HIS B 29  ? 0.18932 0.27076 0.22148 0.02317  -0.04958 0.05575  463 HIS B N   
2912 C CA  . HIS B 29  ? 0.16547 0.25139 0.18325 0.02231  -0.04206 0.05477  463 HIS B CA  
2913 C C   . HIS B 29  ? 0.19200 0.28167 0.21784 0.01841  -0.03861 0.05322  463 HIS B C   
2914 O O   . HIS B 29  ? 0.22679 0.31605 0.26570 0.01370  -0.03503 0.05618  463 HIS B O   
2915 C CB  . HIS B 29  ? 0.18320 0.26890 0.19327 0.01875  -0.03237 0.06026  463 HIS B CB  
2916 C CG  . HIS B 29  ? 0.20012 0.29206 0.19674 0.01721  -0.02534 0.06050  463 HIS B CG  
2917 N ND1 . HIS B 29  ? 0.15217 0.24953 0.15202 0.01292  -0.01953 0.05954  463 HIS B ND1 
2918 C CD2 . HIS B 29  ? 0.21567 0.31076 0.19647 0.01926  -0.02318 0.06230  463 HIS B CD2 
2919 C CE1 . HIS B 29  ? 0.17149 0.27590 0.16000 0.01228  -0.01441 0.06046  463 HIS B CE1 
2920 N NE2 . HIS B 29  ? 0.14597 0.24974 0.12290 0.01588  -0.01588 0.06253  463 HIS B NE2 
2921 N N   . PRO B 30  ? 0.15507 0.24880 0.17302 0.02090  -0.03948 0.04879  464 PRO B N   
2922 C CA  . PRO B 30  ? 0.21880 0.31420 0.24530 0.01842  -0.03954 0.04697  464 PRO B CA  
2923 C C   . PRO B 30  ? 0.13445 0.23275 0.16531 0.01130  -0.02931 0.05122  464 PRO B C   
2924 O O   . PRO B 30  ? 0.10585 0.20355 0.14673 0.00824  -0.02959 0.05187  464 PRO B O   
2925 C CB  . PRO B 30  ? 0.11963 0.21955 0.13423 0.02425  -0.04190 0.04110  464 PRO B CB  
2926 C CG  . PRO B 30  ? 0.12674 0.23139 0.12612 0.02683  -0.03703 0.04230  464 PRO B CG  
2927 C CD  . PRO B 30  ? 0.14243 0.24017 0.14315 0.02687  -0.04025 0.04550  464 PRO B CD  
2928 N N   . GLU B 31  ? 0.11769 0.21799 0.14080 0.00848  -0.02106 0.05442  465 GLU B N   
2929 C CA  . GLU B 31  ? 0.16138 0.26264 0.18650 0.00193  -0.01232 0.05751  465 GLU B CA  
2930 C C   . GLU B 31  ? 0.17239 0.26804 0.20783 -0.00022 -0.01069 0.06083  465 GLU B C   
2931 O O   . GLU B 31  ? 0.19697 0.28915 0.22923 -0.00204 -0.00571 0.06358  465 GLU B O   
2932 C CB  . GLU B 31  ? 0.10004 0.20504 0.11419 -0.00103 -0.00558 0.05934  465 GLU B CB  
2933 C CG  . GLU B 31  ? 0.14661 0.25392 0.16144 -0.00691 0.00030  0.06013  465 GLU B CG  
2934 C CD  . GLU B 31  ? 0.09325 0.19332 0.11294 -0.01080 0.00422  0.06242  465 GLU B CD  
2935 O OE1 . GLU B 31  ? 0.09664 0.19572 0.12426 -0.01056 0.00313  0.06191  465 GLU B OE1 
2936 O OE2 . GLU B 31  ? 0.09794 0.19312 0.11314 -0.01368 0.00818  0.06486  465 GLU B OE2 
2937 N N   . LEU B 32  ? 0.13703 0.23229 0.18471 -0.00002 -0.01460 0.06083  466 LEU B N   
2938 C CA  . LEU B 32  ? 0.12224 0.21578 0.18287 -0.00089 -0.01369 0.06424  466 LEU B CA  
2939 C C   . LEU B 32  ? 0.11988 0.21423 0.18238 -0.00496 -0.00484 0.06673  466 LEU B C   
2940 O O   . LEU B 32  ? 0.09156 0.18755 0.14896 -0.00763 -0.00222 0.06581  466 LEU B O   
2941 C CB  . LEU B 32  ? 0.08887 0.18308 0.16338 0.00019  -0.02229 0.06425  466 LEU B CB  
2942 C CG  . LEU B 32  ? 0.09514 0.18670 0.16950 0.00498  -0.03317 0.06127  466 LEU B CG  
2943 C CD1 . LEU B 32  ? 0.12379 0.21419 0.21060 0.00484  -0.04308 0.06038  466 LEU B CD1 
2944 C CD2 . LEU B 32  ? 0.14444 0.23449 0.22315 0.00709  -0.03410 0.06362  466 LEU B CD2 
2945 N N   . PRO B 33  ? 0.18896 0.26068 0.22030 0.00685  -0.00855 -0.01915 467 PRO B N   
2946 C CA  . PRO B 33  ? 0.06170 0.14197 0.09793 0.00189  -0.00699 -0.02060 467 PRO B CA  
2947 C C   . PRO B 33  ? 0.06120 0.14503 0.09822 -0.00562 -0.00434 -0.02003 467 PRO B C   
2948 O O   . PRO B 33  ? 0.11174 0.19761 0.14952 -0.01024 -0.00206 -0.01741 467 PRO B O   
2949 C CB  . PRO B 33  ? 0.06116 0.15116 0.10247 0.00450  -0.00969 -0.02824 467 PRO B CB  
2950 C CG  . PRO B 33  ? 0.06481 0.14841 0.10308 0.01230  -0.01296 -0.02846 467 PRO B CG  
2951 C CD  . PRO B 33  ? 0.08276 0.15691 0.11492 0.01281  -0.01244 -0.02421 467 PRO B CD  
2952 N N   . GLN B 34  ? 0.06418 0.14810 0.10039 -0.00719 -0.00473 -0.02229 468 GLN B N   
2953 C CA  . GLN B 34  ? 0.07832 0.16493 0.11500 -0.01475 -0.00226 -0.02215 468 GLN B CA  
2954 C C   . GLN B 34  ? 0.07745 0.15411 0.10935 -0.01711 0.00054  -0.01441 468 GLN B C   
2955 O O   . GLN B 34  ? 0.06914 0.14628 0.10051 -0.02342 0.00275  -0.01314 468 GLN B O   
2956 C CB  . GLN B 34  ? 0.10995 0.19866 0.14700 -0.01592 -0.00376 -0.02702 468 GLN B CB  
2957 C CG  . GLN B 34  ? 0.06746 0.17013 0.11152 -0.01628 -0.00590 -0.03521 468 GLN B CG  
2958 C CD  . GLN B 34  ? 0.06554 0.17050 0.11155 -0.00840 -0.00917 -0.03782 468 GLN B CD  
2959 O OE1 . GLN B 34  ? 0.11524 0.21106 0.15654 -0.00225 -0.01110 -0.03526 468 GLN B OE1 
2960 N NE2 . GLN B 34  ? 0.10470 0.22140 0.15729 -0.00845 -0.00958 -0.04287 468 GLN B NE2 
2961 N N   . ARG B 35  ? 0.06841 0.13620 0.09700 -0.01219 0.00056  -0.00911 469 ARG B N   
2962 C CA  . ARG B 35  ? 0.08430 0.14461 0.10997 -0.01390 0.00314  -0.00166 469 ARG B CA  
2963 C C   . ARG B 35  ? 0.07131 0.13757 0.09931 -0.01941 0.00459  0.00017  469 ARG B C   
2964 O O   . ARG B 35  ? 0.09800 0.16300 0.12456 -0.02461 0.00653  0.00290  469 ARG B O   
2965 C CB  . ARG B 35  ? 0.09818 0.15066 0.12155 -0.00775 0.00304  0.00321  469 ARG B CB  
2966 C CG  . ARG B 35  ? 0.13044 0.17610 0.14986 -0.00224 0.00192  0.00190  469 ARG B CG  
2967 C CD  . ARG B 35  ? 0.16399 0.20213 0.18088 0.00332  0.00255  0.00707  469 ARG B CD  
2968 N NE  . ARG B 35  ? 0.09382 0.12717 0.11028 0.00203  0.00546  0.01407  469 ARG B NE  
2969 C CZ  . ARG B 35  ? 0.08990 0.12490 0.10918 0.00152  0.00615  0.01848  469 ARG B CZ  
2970 N NH1 . ARG B 35  ? 0.06562 0.10544 0.08757 0.00217  0.00444  0.01667  469 ARG B NH1 
2971 N NH2 . ARG B 35  ? 0.10386 0.13546 0.12335 0.00046  0.00842  0.02473  469 ARG B NH2 
2972 N N   . ILE B 36  ? 0.13234 0.20467 0.16326 -0.01844 0.00358  -0.00154 470 ILE B N   
2973 C CA  . ILE B 36  ? 0.13621 0.21357 0.16816 -0.02344 0.00480  0.00033  470 ILE B CA  
2974 C C   . ILE B 36  ? 0.15294 0.23935 0.18662 -0.02973 0.00592  -0.00449 470 ILE B C   
2975 O O   . ILE B 36  ? 0.12724 0.21548 0.15952 -0.03542 0.00771  -0.00173 470 ILE B O   
2976 C CB  . ILE B 36  ? 0.21991 0.29981 0.25369 -0.02067 0.00346  -0.00020 470 ILE B CB  
2977 C CG1 . ILE B 36  ? 0.07575 0.16176 0.11265 -0.01747 0.00160  -0.00792 470 ILE B CG1 
2978 C CG2 . ILE B 36  ? 0.12240 0.19349 0.15456 -0.01586 0.00301  0.00566  470 ILE B CG2 
2979 C CD1 . ILE B 36  ? 0.07581 0.16360 0.11414 -0.01515 0.00041  -0.00923 470 ILE B CD1 
2980 N N   . SER B 37  ? 0.10626 0.19891 0.14300 -0.02900 0.00492  -0.01157 471 SER B N   
2981 C CA  . SER B 37  ? 0.15306 0.25581 0.19245 -0.03533 0.00644  -0.01641 471 SER B CA  
2982 C C   . SER B 37  ? 0.15263 0.25164 0.18933 -0.04101 0.00835  -0.01425 471 SER B C   
2983 O O   . SER B 37  ? 0.11812 0.22258 0.15489 -0.04805 0.01068  -0.01490 471 SER B O   
2984 C CB  . SER B 37  ? 0.05956 0.17181 0.10446 -0.03262 0.00462  -0.02490 471 SER B CB  
2985 O OG  . SER B 37  ? 0.09135 0.19946 0.13599 -0.02885 0.00250  -0.02648 471 SER B OG  
2986 N N   . ARG B 38  ? 0.09930 0.18850 0.13304 -0.03823 0.00763  -0.01176 472 ARG B N   
2987 C CA  . ARG B 38  ? 0.12244 0.20543 0.15263 -0.04338 0.00953  -0.00908 472 ARG B CA  
2988 C C   . ARG B 38  ? 0.15034 0.22674 0.17637 -0.04612 0.01154  -0.00111 472 ARG B C   
2989 O O   . ARG B 38  ? 0.29780 0.37310 0.32146 -0.05273 0.01367  0.00078  472 ARG B O   
2990 C CB  . ARG B 38  ? 0.19670 0.27023 0.22412 -0.03923 0.00826  -0.00903 472 ARG B CB  
2991 C CG  . ARG B 38  ? 0.13417 0.21388 0.16472 -0.03897 0.00621  -0.01687 472 ARG B CG  
2992 C CD  . ARG B 38  ? 0.12052 0.20394 0.15190 -0.04738 0.00786  -0.01981 472 ARG B CD  
2993 N NE  . ARG B 38  ? 0.24107 0.31153 0.26626 -0.05030 0.00974  -0.01475 472 ARG B NE  
2994 C CZ  . ARG B 38  ? 0.20259 0.26421 0.22420 -0.04877 0.00882  -0.01564 472 ARG B CZ  
2995 N NH1 . ARG B 38  ? 0.18851 0.25302 0.21169 -0.04457 0.00574  -0.02115 472 ARG B NH1 
2996 N NH2 . ARG B 38  ? 0.25131 0.30038 0.26711 -0.05130 0.01090  -0.01092 472 ARG B NH2 
2997 N N   . ILE B 39  ? 0.07478 0.14684 0.09991 -0.04125 0.01077  0.00381  473 ILE B N   
2998 C CA  . ILE B 39  ? 0.10268 0.17000 0.12474 -0.04333 0.01201  0.01142  473 ILE B CA  
2999 C C   . ILE B 39  ? 0.14381 0.21980 0.16604 -0.04984 0.01309  0.01071  473 ILE B C   
3000 O O   . ILE B 39  ? 0.10254 0.17539 0.12094 -0.05484 0.01462  0.01460  473 ILE B O   
3001 C CB  . ILE B 39  ? 0.07317 0.13645 0.09570 -0.03706 0.01074  0.01606  473 ILE B CB  
3002 C CG1 . ILE B 39  ? 0.14979 0.20298 0.17063 -0.03132 0.01068  0.01824  473 ILE B CG1 
3003 C CG2 . ILE B 39  ? 0.07451 0.13662 0.09535 -0.03953 0.01124  0.02304  473 ILE B CG2 
3004 C CD1 . ILE B 39  ? 0.16396 0.21464 0.18609 -0.02492 0.00968  0.02120  473 ILE B CD1 
3005 N N   . PHE B 40  ? 0.10751 0.19328 0.13330 -0.04921 0.01224  0.00556  474 PHE B N   
3006 C CA  . PHE B 40  ? 0.11419 0.20436 0.13779 -0.05254 0.01278  0.00368  474 PHE B CA  
3007 C C   . PHE B 40  ? 0.21819 0.30881 0.23951 -0.05760 0.01457  0.00107  474 PHE B C   
3008 O O   . PHE B 40  ? 0.13932 0.22738 0.15572 -0.06128 0.01557  0.00385  474 PHE B O   
3009 C CB  . PHE B 40  ? 0.09202 0.19054 0.11933 -0.04960 0.01163  -0.00257 474 PHE B CB  
3010 C CG  . PHE B 40  ? 0.10630 0.20894 0.13055 -0.05236 0.01240  -0.00492 474 PHE B CG  
3011 C CD1 . PHE B 40  ? 0.10710 0.20733 0.12724 -0.05354 0.01194  -0.00036 474 PHE B CD1 
3012 C CD2 . PHE B 40  ? 0.13624 0.24590 0.16178 -0.05378 0.01354  -0.01184 474 PHE B CD2 
3013 C CE1 . PHE B 40  ? 0.14866 0.25339 0.16538 -0.05655 0.01271  -0.00282 474 PHE B CE1 
3014 C CE2 . PHE B 40  ? 0.14632 0.26047 0.16872 -0.05656 0.01475  -0.01414 474 PHE B CE2 
3015 C CZ  . PHE B 40  ? 0.21912 0.33079 0.23680 -0.05813 0.01437  -0.00974 474 PHE B CZ  
3016 N N   . SER B 41  ? 0.23708 0.33115 0.26197 -0.05793 0.01477  -0.00424 475 SER B N   
3017 C CA  . SER B 41  ? 0.11971 0.21475 0.14314 -0.06301 0.01645  -0.00703 475 SER B CA  
3018 C C   . SER B 41  ? 0.11417 0.19905 0.13197 -0.06715 0.01789  -0.00057 475 SER B C   
3019 O O   . SER B 41  ? 0.14835 0.23248 0.16241 -0.07169 0.01941  -0.00012 475 SER B O   
3020 C CB  . SER B 41  ? 0.24595 0.34578 0.27455 -0.06235 0.01576  -0.01338 475 SER B CB  
3021 O OG  . SER B 41  ? 0.16886 0.27844 0.20213 -0.05888 0.01464  -0.02008 475 SER B OG  
3022 N N   . ARG B 42  ? 0.19259 0.26917 0.20942 -0.06546 0.01758  0.00465  476 ARG B N   
3023 C CA  . ARG B 42  ? 0.21538 0.28067 0.22658 -0.06843 0.01890  0.01093  476 ARG B CA  
3024 C C   . ARG B 42  ? 0.13584 0.19794 0.14251 -0.06850 0.01876  0.01649  476 ARG B C   
3025 O O   . ARG B 42  ? 0.14189 0.19744 0.14375 -0.07189 0.01988  0.01995  476 ARG B O   
3026 C CB  . ARG B 42  ? 0.14931 0.20566 0.15992 -0.06595 0.01890  0.01529  476 ARG B CB  
3027 C CG  . ARG B 42  ? 0.11481 0.15803 0.11965 -0.06888 0.02046  0.02021  476 ARG B CG  
3028 C CD  . ARG B 42  ? 0.12069 0.16347 0.12541 -0.07445 0.02165  0.01478  476 ARG B CD  
3029 N NE  . ARG B 42  ? 0.13313 0.16233 0.13167 -0.07758 0.02318  0.01927  476 ARG B NE  
3030 C CZ  . ARG B 42  ? 0.19068 0.21852 0.18653 -0.08265 0.02434  0.01871  476 ARG B CZ  
3031 N NH1 . ARG B 42  ? 0.28525 0.32449 0.28365 -0.08550 0.02445  0.01377  476 ARG B NH1 
3032 N NH2 . ARG B 42  ? 0.26435 0.27853 0.25450 -0.08466 0.02558  0.02333  476 ARG B NH2 
3033 N N   . HIS B 43  ? 0.11483 0.18140 0.12284 -0.06499 0.01720  0.01723  477 HIS B N   
3034 C CA  . HIS B 43  ? 0.16258 0.22818 0.16634 -0.06584 0.01661  0.02116  477 HIS B CA  
3035 C C   . HIS B 43  ? 0.16772 0.23888 0.16883 -0.07086 0.01787  0.01726  477 HIS B C   
3036 O O   . HIS B 43  ? 0.12144 0.18973 0.11731 -0.07360 0.01809  0.02093  477 HIS B O   
3037 C CB  . HIS B 43  ? 0.18039 0.25022 0.18623 -0.06180 0.01453  0.02187  477 HIS B CB  
3038 C CG  . HIS B 43  ? 0.09859 0.16196 0.10550 -0.05718 0.01325  0.02804  477 HIS B CG  
3039 N ND1 . HIS B 43  ? 0.09587 0.15788 0.10677 -0.05361 0.01332  0.02785  477 HIS B ND1 
3040 C CD2 . HIS B 43  ? 0.09804 0.15661 0.10275 -0.05533 0.01182  0.03451  477 HIS B CD2 
3041 C CE1 . HIS B 43  ? 0.12113 0.17728 0.13211 -0.04955 0.01236  0.03412  477 HIS B CE1 
3042 N NE2 . HIS B 43  ? 0.10042 0.15467 0.10815 -0.05035 0.01129  0.03797  477 HIS B NE2 
3043 N N   . GLU B 44  ? 0.16484 0.24423 0.16949 -0.07192 0.01871  0.00989  478 GLU B N   
3044 C CA  . GLU B 44  ? 0.18467 0.27010 0.18717 -0.07652 0.02037  0.00586  478 GLU B CA  
3045 C C   . GLU B 44  ? 0.20693 0.28694 0.20609 -0.08170 0.02232  0.00748  478 GLU B C   
3046 O O   . GLU B 44  ? 0.13196 0.21091 0.12589 -0.08583 0.02346  0.00950  478 GLU B O   
3047 C CB  . GLU B 44  ? 0.15688 0.25283 0.16489 -0.07527 0.02070  -0.00255 478 GLU B CB  
3048 C CG  . GLU B 44  ? 0.23491 0.33705 0.24505 -0.07128 0.01935  -0.00518 478 GLU B CG  
3049 C CD  . GLU B 44  ? 0.33203 0.44411 0.34746 -0.06970 0.01986  -0.01360 478 GLU B CD  
3050 O OE1 . GLU B 44  ? 0.15792 0.27126 0.17850 -0.06739 0.01923  -0.01665 478 GLU B OE1 
3051 O OE2 . GLU B 44  ? 0.36231 0.48115 0.37669 -0.07077 0.02084  -0.01733 478 GLU B OE2 
3052 N N   . GLU B 45  ? 0.12361 0.20004 0.12541 -0.08194 0.02272  0.00647  479 GLU B N   
3053 C CA  . GLU B 45  ? 0.21267 0.28357 0.21141 -0.08733 0.02463  0.00743  479 GLU B CA  
3054 C C   . GLU B 45  ? 0.20970 0.26830 0.20223 -0.08822 0.02480  0.01567  479 GLU B C   
3055 O O   . GLU B 45  ? 0.21637 0.27015 0.20478 -0.09312 0.02650  0.01731  479 GLU B O   
3056 C CB  . GLU B 45  ? 0.14562 0.21574 0.14849 -0.08777 0.02475  0.00371  479 GLU B CB  
3057 C CG  . GLU B 45  ? 0.20371 0.27176 0.21008 -0.08243 0.02291  0.00429  479 GLU B CG  
3058 C CD  . GLU B 45  ? 0.21358 0.28652 0.22541 -0.08249 0.02241  -0.00231 479 GLU B CD  
3059 O OE1 . GLU B 45  ? 0.26635 0.35008 0.28228 -0.08303 0.02239  -0.00893 479 GLU B OE1 
3060 O OE2 . GLU B 45  ? 0.16962 0.23565 0.18148 -0.08186 0.02198  -0.00102 479 GLU B OE2 
3061 N N   . LEU B 46  ? 0.16692 0.22050 0.15884 -0.08340 0.02307  0.02092  480 LEU B N   
3062 C CA  . LEU B 46  ? 0.17411 0.21646 0.16076 -0.08289 0.02292  0.02882  480 LEU B CA  
3063 C C   . LEU B 46  ? 0.23236 0.27699 0.21481 -0.08361 0.02212  0.03186  480 LEU B C   
3064 O O   . LEU B 46  ? 0.24932 0.28584 0.22774 -0.08237 0.02143  0.03850  480 LEU B O   
3065 C CB  . LEU B 46  ? 0.14156 0.17699 0.12996 -0.07696 0.02158  0.03312  480 LEU B CB  
3066 C CG  . LEU B 46  ? 0.14323 0.17169 0.13283 -0.07707 0.02265  0.03228  480 LEU B CG  
3067 C CD1 . LEU B 46  ? 0.13893 0.16096 0.12979 -0.07085 0.02164  0.03658  480 LEU B CD1 
3068 C CD2 . LEU B 46  ? 0.15692 0.17522 0.14144 -0.08148 0.02447  0.03480  480 LEU B CD2 
3069 N N   . ARG B 47  ? 0.24053 0.29591 0.22357 -0.08555 0.02218  0.02700  481 ARG B N   
3070 C CA  . ARG B 47  ? 0.25124 0.30973 0.22955 -0.08720 0.02144  0.02900  481 ARG B CA  
3071 C C   . ARG B 47  ? 0.21886 0.27483 0.19689 -0.08246 0.01853  0.03421  481 ARG B C   
3072 O O   . ARG B 47  ? 0.32288 0.37609 0.29587 -0.08345 0.01742  0.03910  481 ARG B O   
3073 C CB  . ARG B 47  ? 0.25151 0.30451 0.22311 -0.09252 0.02312  0.03243  481 ARG B CB  
3074 C CG  . ARG B 47  ? 0.39844 0.45481 0.37015 -0.09807 0.02610  0.02736  481 ARG B CG  
3075 C CD  . ARG B 47  ? 0.44345 0.51312 0.41852 -0.09897 0.02674  0.01960  481 ARG B CD  
3076 N NE  . ARG B 47  ? 0.37095 0.44596 0.34245 -0.09921 0.02574  0.02002  481 ARG B NE  
3077 C CZ  . ARG B 47  ? 0.32547 0.40245 0.29090 -0.10432 0.02716  0.02057  481 ARG B CZ  
3078 N NH1 . ARG B 47  ? 0.37190 0.44594 0.33425 -0.10960 0.02979  0.02101  481 ARG B NH1 
3079 N NH2 . ARG B 47  ? 0.38920 0.47110 0.35123 -0.10452 0.02594  0.02072  481 ARG B NH2 
3080 N N   . LEU B 48  ? 0.24076 0.29797 0.22430 -0.07742 0.01718  0.03325  482 LEU B N   
3081 C CA  . LEU B 48  ? 0.20923 0.26564 0.19369 -0.07293 0.01437  0.03751  482 LEU B CA  
3082 C C   . LEU B 48  ? 0.17349 0.23983 0.15939 -0.07257 0.01289  0.03371  482 LEU B C   
3083 O O   . LEU B 48  ? 0.12567 0.19326 0.10929 -0.07224 0.01061  0.03703  482 LEU B O   
3084 C CB  . LEU B 48  ? 0.14533 0.19646 0.13453 -0.06759 0.01393  0.03946  482 LEU B CB  
3085 C CG  . LEU B 48  ? 0.13442 0.17397 0.12160 -0.06697 0.01521  0.04412  482 LEU B CG  
3086 C CD1 . LEU B 48  ? 0.13773 0.17309 0.12926 -0.06202 0.01525  0.04487  482 LEU B CD1 
3087 C CD2 . LEU B 48  ? 0.14206 0.17546 0.12470 -0.06628 0.01392  0.05104  482 LEU B CD2 
3088 N N   . LEU B 49  ? 0.24487 0.31830 0.23446 -0.07268 0.01406  0.02667  483 LEU B N   
3089 C CA  . LEU B 49  ? 0.21741 0.29952 0.20823 -0.07208 0.01308  0.02245  483 LEU B CA  
3090 C C   . LEU B 49  ? 0.15290 0.23913 0.13747 -0.07678 0.01312  0.02223  483 LEU B C   
3091 O O   . LEU B 49  ? 0.15542 0.24564 0.13860 -0.07660 0.01128  0.02246  483 LEU B O   
3092 C CB  . LEU B 49  ? 0.13894 0.22756 0.13476 -0.07117 0.01465  0.01459  483 LEU B CB  
3093 C CG  . LEU B 49  ? 0.24922 0.34653 0.24666 -0.07018 0.01427  0.00901  483 LEU B CG  
3094 C CD1 . LEU B 49  ? 0.14253 0.23891 0.14387 -0.06522 0.01197  0.01067  483 LEU B CD1 
3095 C CD2 . LEU B 49  ? 0.24190 0.34615 0.24314 -0.07036 0.01634  0.00090  483 LEU B CD2 
3096 N N   . SER B 50  ? 0.17656 0.26195 0.15701 -0.08146 0.01526  0.02179  484 SER B N   
3097 C CA  . SER B 50  ? 0.14482 0.23405 0.11865 -0.08641 0.01561  0.02167  484 SER B CA  
3098 C C   . SER B 50  ? 0.19746 0.28241 0.16664 -0.08651 0.01268  0.02900  484 SER B C   
3099 O O   . SER B 50  ? 0.18697 0.27645 0.15114 -0.08972 0.01180  0.02895  484 SER B O   
3100 C CB  . SER B 50  ? 0.14693 0.23519 0.11738 -0.09149 0.01867  0.02047  484 SER B CB  
3101 O OG  . SER B 50  ? 0.20118 0.27928 0.16970 -0.09171 0.01867  0.02670  484 SER B OG  
3102 N N   . ARG B 51  ? 0.14149 0.21817 0.11229 -0.08305 0.01112  0.03518  485 ARG B N   
3103 C CA  . ARG B 51  ? 0.14906 0.22204 0.11660 -0.08237 0.00802  0.04234  485 ARG B CA  
3104 C C   . ARG B 51  ? 0.13772 0.21471 0.10889 -0.07885 0.00473  0.04322  485 ARG B C   
3105 O O   . ARG B 51  ? 0.14113 0.21770 0.11007 -0.07884 0.00162  0.04850  485 ARG B O   
3106 C CB  . ARG B 51  ? 0.22561 0.28781 0.19339 -0.07986 0.00811  0.04849  485 ARG B CB  
3107 C CG  . ARG B 51  ? 0.23590 0.29276 0.19993 -0.08364 0.01140  0.04823  485 ARG B CG  
3108 C CD  . ARG B 51  ? 0.25571 0.30114 0.22047 -0.08055 0.01189  0.05346  485 ARG B CD  
3109 N NE  . ARG B 51  ? 0.31542 0.35609 0.27839 -0.07754 0.00895  0.06063  485 ARG B NE  
3110 C CZ  . ARG B 51  ? 0.31756 0.34873 0.28157 -0.07333 0.00879  0.06561  485 ARG B CZ  
3111 N NH1 . ARG B 51  ? 0.23791 0.26239 0.20400 -0.07199 0.01143  0.06449  485 ARG B NH1 
3112 N NH2 . ARG B 51  ? 0.25387 0.28238 0.21673 -0.07043 0.00584  0.07174  485 ARG B NH2 
3113 N N   . CYS B 52  ? 0.14840 0.22944 0.12517 -0.07606 0.00524  0.03833  486 CYS B N   
3114 C CA  . CYS B 52  ? 0.15276 0.23695 0.13338 -0.07278 0.00249  0.03907  486 CYS B CA  
3115 C C   . CYS B 52  ? 0.13173 0.22472 0.10996 -0.07587 0.00223  0.03392  486 CYS B C   
3116 O O   . CYS B 52  ? 0.19893 0.29629 0.17506 -0.07884 0.00493  0.02785  486 CYS B O   
3117 C CB  . CYS B 52  ? 0.13412 0.21628 0.12211 -0.06750 0.00329  0.03725  486 CYS B CB  
3118 S SG  . CYS B 52  ? 0.17009 0.24187 0.16105 -0.06329 0.00375  0.04296  486 CYS B SG  
3119 N N   . HIS B 53  ? 0.13825 0.23404 0.11700 -0.07525 -0.00093 0.03624  487 HIS B N   
3120 C CA  . HIS B 53  ? 0.18612 0.28955 0.16332 -0.07757 -0.00108 0.03100  487 HIS B CA  
3121 C C   . HIS B 53  ? 0.17540 0.27977 0.15958 -0.07313 0.00013  0.02616  487 HIS B C   
3122 O O   . HIS B 53  ? 0.21495 0.31598 0.20456 -0.06879 -0.00157 0.02949  487 HIS B O   
3123 C CB  . HIS B 53  ? 0.14871 0.25487 0.12327 -0.07962 -0.00515 0.03551  487 HIS B CB  
3124 C CG  . HIS B 53  ? 0.20215 0.31522 0.17536 -0.08191 -0.00530 0.03017  487 HIS B CG  
3125 N ND1 . HIS B 53  ? 0.20756 0.32667 0.17363 -0.08764 -0.00402 0.02558  487 HIS B ND1 
3126 C CD2 . HIS B 53  ? 0.16196 0.27632 0.14015 -0.07928 -0.00623 0.02829  487 HIS B CD2 
3127 C CE1 . HIS B 53  ? 0.31219 0.43618 0.27867 -0.08849 -0.00407 0.02090  487 HIS B CE1 
3128 N NE2 . HIS B 53  ? 0.22991 0.35063 0.20397 -0.08338 -0.00553 0.02248  487 HIS B NE2 
3129 N N   . ARG B 54  ? 0.20229 0.31143 0.18670 -0.07403 0.00307  0.01828  488 ARG B N   
3130 C CA  . ARG B 54  ? 0.19332 0.30347 0.18469 -0.06959 0.00422  0.01313  488 ARG B CA  
3131 C C   . ARG B 54  ? 0.21179 0.32458 0.20493 -0.06880 0.00223  0.01196  488 ARG B C   
3132 O O   . ARG B 54  ? 0.14513 0.26312 0.13371 -0.07280 0.00209  0.00920  488 ARG B O   
3133 C CB  . ARG B 54  ? 0.11337 0.22872 0.10520 -0.07051 0.00771  0.00489  488 ARG B CB  
3134 C CG  . ARG B 54  ? 0.09035 0.20684 0.08992 -0.06545 0.00858  -0.00044 488 ARG B CG  
3135 C CD  . ARG B 54  ? 0.10255 0.21291 0.10658 -0.06178 0.00841  0.00289  488 ARG B CD  
3136 N NE  . ARG B 54  ? 0.10370 0.21631 0.11442 -0.05748 0.00909  -0.00278 488 ARG B NE  
3137 C CZ  . ARG B 54  ? 0.12765 0.24396 0.14038 -0.05733 0.01115  -0.00840 488 ARG B CZ  
3138 N NH1 . ARG B 54  ? 0.10306 0.22071 0.11183 -0.06150 0.01311  -0.00899 488 ARG B NH1 
3139 N NH2 . ARG B 54  ? 0.10907 0.22801 0.12809 -0.05288 0.01098  -0.01350 488 ARG B NH2 
3140 N N   . ILE B 55  ? 0.14214 0.25116 0.14167 -0.06402 0.00078  0.01395  489 ILE B N   
3141 C CA  . ILE B 55  ? 0.16466 0.27452 0.16694 -0.06297 -0.00146 0.01339  489 ILE B CA  
3142 C C   . ILE B 55  ? 0.14347 0.25543 0.15114 -0.05974 -0.00008 0.00572  489 ILE B C   
3143 O O   . ILE B 55  ? 0.12963 0.23958 0.14183 -0.05588 0.00113  0.00474  489 ILE B O   
3144 C CB  . ILE B 55  ? 0.09906 0.20341 0.10514 -0.05985 -0.00416 0.02107  489 ILE B CB  
3145 C CG1 . ILE B 55  ? 0.14643 0.25005 0.14781 -0.06278 -0.00630 0.02838  489 ILE B CG1 
3146 C CG2 . ILE B 55  ? 0.07979 0.18413 0.08984 -0.05845 -0.00625 0.01990  489 ILE B CG2 
3147 C CD1 . ILE B 55  ? 0.13880 0.23783 0.14461 -0.05916 -0.00855 0.03604  489 ILE B CD1 
3148 N N   . PRO B 56  ? 0.16629 0.28233 0.17354 -0.06116 -0.00048 -0.00004 490 PRO B N   
3149 C CA  . PRO B 56  ? 0.07875 0.19691 0.09152 -0.05753 0.00030  -0.00768 490 PRO B CA  
3150 C C   . PRO B 56  ? 0.15101 0.26363 0.16993 -0.05263 -0.00187 -0.00496 490 PRO B C   
3151 O O   . PRO B 56  ? 0.13204 0.24066 0.15115 -0.05303 -0.00434 0.00078  490 PRO B O   
3152 C CB  . PRO B 56  ? 0.10585 0.22843 0.11555 -0.06067 -0.00015 -0.01398 490 PRO B CB  
3153 C CG  . PRO B 56  ? 0.14734 0.26803 0.15148 -0.06500 -0.00255 -0.00787 490 PRO B CG  
3154 C CD  . PRO B 56  ? 0.17120 0.29032 0.17249 -0.06626 -0.00183 -0.00046 490 PRO B CD  
3155 N N   . ALA B 57  ? 0.13470 0.24584 0.15779 -0.04725 -0.00089 -0.00901 491 ALA B N   
3156 C CA  . ALA B 57  ? 0.09713 0.20074 0.12398 -0.04140 -0.00257 -0.00728 491 ALA B CA  
3157 C C   . ALA B 57  ? 0.17776 0.27855 0.20437 -0.03964 -0.00410 -0.01219 491 ALA B C   
3158 O O   . ALA B 57  ? 0.14710 0.25210 0.17150 -0.04137 -0.00342 -0.01885 491 ALA B O   
3159 C CB  . ALA B 57  ? 0.07513 0.17781 0.10552 -0.03622 -0.00142 -0.00959 491 ALA B CB  
3160 N N   . ARG B 58  ? 0.18045 0.27355 0.20904 -0.03627 -0.00592 -0.00891 492 ARG B N   
3161 C CA  . ARG B 58  ? 0.13742 0.22557 0.16568 -0.03419 -0.00738 -0.01328 492 ARG B CA  
3162 C C   . ARG B 58  ? 0.13186 0.21120 0.16285 -0.02873 -0.00835 -0.01009 492 ARG B C   
3163 O O   . ARG B 58  ? 0.13946 0.21694 0.17230 -0.02736 -0.00796 -0.00388 492 ARG B O   
3164 C CB  . ARG B 58  ? 0.15482 0.24302 0.18001 -0.03978 -0.00914 -0.01214 492 ARG B CB  
3165 C CG  . ARG B 58  ? 0.14752 0.23217 0.17432 -0.04170 -0.01102 -0.00352 492 ARG B CG  
3166 C CD  . ARG B 58  ? 0.08446 0.16890 0.10857 -0.04689 -0.01340 -0.00412 492 ARG B CD  
3167 N NE  . ARG B 58  ? 0.08337 0.16703 0.10989 -0.04964 -0.01544 0.00400  492 ARG B NE  
3168 C CZ  . ARG B 58  ? 0.12183 0.19913 0.15175 -0.04799 -0.01648 0.00708  492 ARG B CZ  
3169 N NH1 . ARG B 58  ? 0.08582 0.15549 0.11630 -0.04334 -0.01584 0.00340  492 ARG B NH1 
3170 N NH2 . ARG B 58  ? 0.10199 0.18081 0.13489 -0.05110 -0.01822 0.01421  492 ARG B NH2 
3171 N N   . LEU B 59  ? 0.11387 0.18720 0.14452 -0.02547 -0.00941 -0.01451 493 LEU B N   
3172 C CA  . LEU B 59  ? 0.14460 0.20830 0.17651 -0.02103 -0.01037 -0.01118 493 LEU B CA  
3173 C C   . LEU B 59  ? 0.19429 0.25449 0.22644 -0.02519 -0.01154 -0.00464 493 LEU B C   
3174 O O   . LEU B 59  ? 0.20567 0.26815 0.23624 -0.03049 -0.01266 -0.00553 493 LEU B O   
3175 C CB  . LEU B 59  ? 0.14022 0.19744 0.17109 -0.01628 -0.01129 -0.01775 493 LEU B CB  
3176 C CG  . LEU B 59  ? 0.17683 0.23719 0.20852 -0.01092 -0.01072 -0.02520 493 LEU B CG  
3177 C CD1 . LEU B 59  ? 0.14012 0.19327 0.17031 -0.00710 -0.01201 -0.03130 493 LEU B CD1 
3178 C CD2 . LEU B 59  ? 0.08215 0.14137 0.11577 -0.00558 -0.01050 -0.02272 493 LEU B CD2 
3179 N N   . ALA B 60  ? 0.15627 0.21153 0.19047 -0.02290 -0.01125 0.00180  494 ALA B N   
3180 C CA  . ALA B 60  ? 0.15446 0.20529 0.18990 -0.02573 -0.01225 0.00711  494 ALA B CA  
3181 C C   . ALA B 60  ? 0.18847 0.22992 0.22202 -0.02397 -0.01339 0.00326  494 ALA B C   
3182 O O   . ALA B 60  ? 0.16157 0.19810 0.19346 -0.01843 -0.01321 -0.00131 494 ALA B O   
3183 C CB  . ALA B 60  ? 0.11125 0.15988 0.14952 -0.02349 -0.01089 0.01489  494 ALA B CB  
3184 N N   . THR B 61  ? 0.14253 0.18134 0.17634 -0.02875 -0.01482 0.00506  495 THR B N   
3185 C CA  . THR B 61  ? 0.16227 0.19040 0.19394 -0.02770 -0.01584 0.00210  495 THR B CA  
3186 C C   . THR B 61  ? 0.18209 0.20231 0.21546 -0.02582 -0.01499 0.00866  495 THR B C   
3187 O O   . THR B 61  ? 0.14541 0.16958 0.18231 -0.02682 -0.01380 0.01564  495 THR B O   
3188 C CB  . THR B 61  ? 0.24146 0.26966 0.27171 -0.03443 -0.01792 -0.00047 495 THR B CB  
3189 O OG1 . THR B 61  ? 0.11757 0.14859 0.15147 -0.03993 -0.01866 0.00671  495 THR B OG1 
3190 C CG2 . THR B 61  ? 0.10863 0.14587 0.13650 -0.03717 -0.01834 -0.00611 495 THR B CG2 
3191 N N   . GLU B 62  ? 0.15886 0.16738 0.18934 -0.02285 -0.01541 0.00633  496 GLU B N   
3192 C CA  . GLU B 62  ? 0.17971 0.17955 0.21062 -0.02139 -0.01429 0.01244  496 GLU B CA  
3193 C C   . GLU B 62  ? 0.14447 0.14667 0.17942 -0.02855 -0.01433 0.01847  496 GLU B C   
3194 O O   . GLU B 62  ? 0.27046 0.27163 0.30810 -0.02829 -0.01243 0.02539  496 GLU B O   
3195 C CB  . GLU B 62  ? 0.16100 0.14674 0.18712 -0.01755 -0.01507 0.00879  496 GLU B CB  
3196 C CG  . GLU B 62  ? 0.17773 0.16155 0.20071 -0.00973 -0.01546 0.00288  496 GLU B CG  
3197 C CD  . GLU B 62  ? 0.20929 0.17819 0.22743 -0.00500 -0.01649 0.00025  496 GLU B CD  
3198 O OE1 . GLU B 62  ? 0.25963 0.21845 0.27628 -0.00708 -0.01615 0.00476  496 GLU B OE1 
3199 O OE2 . GLU B 62  ? 0.31084 0.27816 0.32682 0.00084  -0.01761 -0.00624 496 GLU B OE2 
3200 N N   . GLU B 63  ? 0.11966 0.12563 0.15518 -0.03498 -0.01646 0.01582  497 GLU B N   
3201 C CA  . GLU B 63  ? 0.16175 0.17235 0.20209 -0.04217 -0.01715 0.02132  497 GLU B CA  
3202 C C   . GLU B 63  ? 0.15444 0.17738 0.20005 -0.04276 -0.01614 0.02729  497 GLU B C   
3203 O O   . GLU B 63  ? 0.14965 0.17584 0.20074 -0.04543 -0.01534 0.03414  497 GLU B O   
3204 C CB  . GLU B 63  ? 0.15161 0.16374 0.19041 -0.04890 -0.02023 0.01645  497 GLU B CB  
3205 N N   . GLU B 64  ? 0.20196 0.23186 0.24624 -0.04028 -0.01601 0.02481  498 GLU B N   
3206 C CA  . GLU B 64  ? 0.10332 0.14318 0.15175 -0.04022 -0.01498 0.03040  498 GLU B CA  
3207 C C   . GLU B 64  ? 0.13941 0.17594 0.18948 -0.03454 -0.01180 0.03538  498 GLU B C   
3208 O O   . GLU B 64  ? 0.16337 0.20498 0.21848 -0.03517 -0.01049 0.04209  498 GLU B O   
3209 C CB  . GLU B 64  ? 0.09285 0.13977 0.13853 -0.03975 -0.01551 0.02625  498 GLU B CB  
3210 C CG  . GLU B 64  ? 0.12603 0.17811 0.16976 -0.04603 -0.01839 0.02246  498 GLU B CG  
3211 C CD  . GLU B 64  ? 0.12761 0.18595 0.16761 -0.04573 -0.01829 0.01793  498 GLU B CD  
3212 O OE1 . GLU B 64  ? 0.17125 0.22737 0.20916 -0.04055 -0.01647 0.01419  498 GLU B OE1 
3213 O OE2 . GLU B 64  ? 0.12855 0.19435 0.16762 -0.05090 -0.02010 0.01819  498 GLU B OE2 
3214 N N   . LEU B 65  ? 0.16219 0.19030 0.20791 -0.02873 -0.01061 0.03211  499 LEU B N   
3215 C CA  . LEU B 65  ? 0.10790 0.13147 0.15367 -0.02347 -0.00775 0.03654  499 LEU B CA  
3216 C C   . LEU B 65  ? 0.12973 0.14993 0.17895 -0.02589 -0.00630 0.04286  499 LEU B C   
3217 O O   . LEU B 65  ? 0.15668 0.17828 0.20855 -0.02385 -0.00352 0.04868  499 LEU B O   
3218 C CB  . LEU B 65  ? 0.19849 0.21279 0.23837 -0.01719 -0.00760 0.03178  499 LEU B CB  
3219 C CG  . LEU B 65  ? 0.16528 0.18267 0.20232 -0.01341 -0.00842 0.02546  499 LEU B CG  
3220 C CD1 . LEU B 65  ? 0.09765 0.10531 0.12979 -0.00707 -0.00880 0.02158  499 LEU B CD1 
3221 C CD2 . LEU B 65  ? 0.17658 0.20125 0.21535 -0.01177 -0.00679 0.02820  499 LEU B CD2 
3222 N N   . ALA B 66  ? 0.17191 0.18759 0.22111 -0.03045 -0.00793 0.04159  500 ALA B N   
3223 C CA  . ALA B 66  ? 0.10766 0.12015 0.16044 -0.03384 -0.00653 0.04722  500 ALA B CA  
3224 C C   . ALA B 66  ? 0.12581 0.15026 0.18705 -0.03842 -0.00616 0.05329  500 ALA B C   
3225 O O   . ALA B 66  ? 0.10347 0.12762 0.16932 -0.04140 -0.00457 0.05844  500 ALA B O   
3226 C CB  . ALA B 66  ? 0.11669 0.12091 0.16706 -0.03831 -0.00872 0.04367  500 ALA B CB  
3227 N N   . LEU B 67  ? 0.09274 0.12775 0.15631 -0.03910 -0.00760 0.05299  501 LEU B N   
3228 C CA  . LEU B 67  ? 0.08742 0.13370 0.15913 -0.04196 -0.00733 0.05933  501 LEU B CA  
3229 C C   . LEU B 67  ? 0.15081 0.19630 0.22402 -0.03616 -0.00311 0.06412  501 LEU B C   
3230 O O   . LEU B 67  ? 0.19278 0.24242 0.26966 -0.03575 -0.00235 0.06683  501 LEU B O   
3231 C CB  . LEU B 67  ? 0.14562 0.20125 0.21726 -0.04270 -0.00976 0.05777  501 LEU B CB  
3232 C CG  . LEU B 67  ? 0.08448 0.14264 0.15356 -0.04834 -0.01399 0.05251  501 LEU B CG  
3233 C CD1 . LEU B 67  ? 0.07982 0.14572 0.14673 -0.04776 -0.01546 0.05136  501 LEU B CD1 
3234 C CD2 . LEU B 67  ? 0.09063 0.15031 0.16238 -0.05378 -0.01621 0.05324  501 LEU B CD2 
3235 N N   . CYS B 68  ? 0.10936 0.14888 0.17818 -0.03061 -0.00066 0.06362  502 CYS B N   
3236 C CA  . CYS B 68  ? 0.13028 0.16805 0.19894 -0.02487 0.00337  0.06718  502 CYS B CA  
3237 C C   . CYS B 68  ? 0.11435 0.14025 0.17747 -0.02133 0.00614  0.06761  502 CYS B C   
3238 O O   . CYS B 68  ? 0.22396 0.24775 0.28616 -0.01750 0.00947  0.06969  502 CYS B O   
3239 C CB  . CYS B 68  ? 0.14466 0.18672 0.21212 -0.02044 0.00387  0.06668  502 CYS B CB  
3240 S SG  . CYS B 68  ? 0.17332 0.22670 0.24449 -0.02277 0.00053  0.06648  502 CYS B SG  
3241 N N   . HIS B 69  ? 0.14770 0.16517 0.20408 -0.02043 0.00395  0.06185  503 HIS B N   
3242 C CA  . HIS B 69  ? 0.12217 0.12766 0.17111 -0.01531 0.00557  0.06082  503 HIS B CA  
3243 C C   . HIS B 69  ? 0.11054 0.10638 0.15718 -0.01831 0.00494  0.06046  503 HIS B C   
3244 O O   . HIS B 69  ? 0.11269 0.10954 0.16134 -0.02363 0.00211  0.05787  503 HIS B O   
3245 C CB  . HIS B 69  ? 0.15623 0.15897 0.19886 -0.01024 0.00356  0.05444  503 HIS B CB  
3246 C CG  . HIS B 69  ? 0.16542 0.17534 0.20904 -0.00721 0.00453  0.05478  503 HIS B CG  
3247 N ND1 . HIS B 69  ? 0.11901 0.12657 0.16043 -0.00241 0.00776  0.05801  503 HIS B ND1 
3248 C CD2 . HIS B 69  ? 0.11326 0.13182 0.15918 -0.00857 0.00282  0.05228  503 HIS B CD2 
3249 C CE1 . HIS B 69  ? 0.09928 0.11329 0.14186 -0.00095 0.00786  0.05730  503 HIS B CE1 
3250 N NE2 . HIS B 69  ? 0.15006 0.17076 0.19541 -0.00472 0.00494  0.05410  503 HIS B NE2 
3251 N N   . SER B 70  ? 0.13682 0.12251 0.17839 -0.01492 0.00764  0.06310  504 SER B N   
3252 C CA  . SER B 70  ? 0.17890 0.15314 0.21705 -0.01731 0.00765  0.06368  504 SER B CA  
3253 C C   . SER B 70  ? 0.27712 0.24158 0.30790 -0.01439 0.00401  0.05677  504 SER B C   
3254 O O   . SER B 70  ? 0.20473 0.17013 0.23203 -0.00901 0.00235  0.05222  504 SER B O   
3255 C CB  . SER B 70  ? 0.18467 0.15111 0.21890 -0.01450 0.01214  0.06943  504 SER B CB  
3256 O OG  . SER B 70  ? 0.18285 0.14293 0.20873 -0.00665 0.01232  0.06753  504 SER B OG  
3257 N N   . SER B 71  ? 0.17202 0.12691 0.20070 -0.01803 0.00285  0.05593  505 SER B N   
3258 C CA  . SER B 71  ? 0.22662 0.17132 0.24862 -0.01499 -0.00053 0.04932  505 SER B CA  
3259 C C   . SER B 71  ? 0.21504 0.15047 0.22871 -0.00626 -0.00018 0.04874  505 SER B C   
3260 O O   . SER B 71  ? 0.28936 0.22310 0.29948 -0.00116 -0.00306 0.04259  505 SER B O   
3261 C CB  . SER B 71  ? 0.20895 0.14292 0.22953 -0.02049 -0.00143 0.04919  505 SER B CB  
3262 O OG  . SER B 71  ? 0.29498 0.21995 0.31317 -0.02151 0.00195  0.05582  505 SER B OG  
3263 N N   . LYS B 72  ? 0.18584 0.11591 0.19638 -0.00441 0.00333  0.05503  506 LYS B N   
3264 C CA  . LYS B 72  ? 0.16977 0.09061 0.17134 0.00375  0.00337  0.05495  506 LYS B CA  
3265 C C   . LYS B 72  ? 0.20331 0.13349 0.20531 0.00927  0.00213  0.05126  506 LYS B C   
3266 O O   . LYS B 72  ? 0.21772 0.14351 0.21442 0.01553  -0.00072 0.04660  506 LYS B O   
3267 C CB  . LYS B 72  ? 0.23516 0.14995 0.23304 0.00399  0.00796  0.06273  506 LYS B CB  
3268 N N   . HIS B 73  ? 0.21709 0.16013 0.22559 0.00703  0.00418  0.05337  507 HIS B N   
3269 C CA  . HIS B 73  ? 0.17464 0.12583 0.18337 0.01150  0.00344  0.05038  507 HIS B CA  
3270 C C   . HIS B 73  ? 0.24015 0.19692 0.25107 0.01170  -0.00058 0.04273  507 HIS B C   
3271 O O   . HIS B 73  ? 0.20610 0.16414 0.21420 0.01702  -0.00247 0.03830  507 HIS B O   
3272 C CB  . HIS B 73  ? 0.23757 0.19988 0.25264 0.00883  0.00670  0.05475  507 HIS B CB  
3273 C CG  . HIS B 73  ? 0.16644 0.13729 0.18255 0.01189  0.00589  0.05159  507 HIS B CG  
3274 N ND1 . HIS B 73  ? 0.14301 0.11033 0.15277 0.01829  0.00572  0.05000  507 HIS B ND1 
3275 C CD2 . HIS B 73  ? 0.15137 0.13369 0.17370 0.00907  0.00513  0.04982  507 HIS B CD2 
3276 C CE1 . HIS B 73  ? 0.16732 0.14358 0.17981 0.01892  0.00503  0.04718  507 HIS B CE1 
3277 N NE2 . HIS B 73  ? 0.16678 0.15186 0.18664 0.01347  0.00480  0.04721  507 HIS B NE2 
3278 N N   . ILE B 74  ? 0.23594 0.19662 0.25188 0.00575  -0.00184 0.04094  508 ILE B N   
3279 C CA  . ILE B 74  ? 0.22885 0.19424 0.24610 0.00564  -0.00517 0.03343  508 ILE B CA  
3280 C C   . ILE B 74  ? 0.21706 0.17203 0.22807 0.01137  -0.00777 0.02835  508 ILE B C   
3281 O O   . ILE B 74  ? 0.18191 0.14064 0.19224 0.01571  -0.00983 0.02253  508 ILE B O   
3282 C CB  . ILE B 74  ? 0.17241 0.14230 0.19471 -0.00209 -0.00605 0.03266  508 ILE B CB  
3283 C CG1 . ILE B 74  ? 0.14560 0.12813 0.17470 -0.00682 -0.00441 0.03685  508 ILE B CG1 
3284 C CG2 . ILE B 74  ? 0.16581 0.13749 0.18749 -0.00191 -0.00919 0.02436  508 ILE B CG2 
3285 C CD1 . ILE B 74  ? 0.16823 0.15420 0.20224 -0.01478 -0.00506 0.03849  508 ILE B CD1 
3286 N N   . SER B 75  ? 0.23328 0.17501 0.23985 0.01153  -0.00768 0.03065  509 SER B N   
3287 C CA  A SER B 75  ? 0.21884 0.14923 0.21933 0.01723  -0.01047 0.02612  509 SER B CA  
3288 C CA  B SER B 75  ? 0.21888 0.14920 0.21934 0.01723  -0.01046 0.02615  509 SER B CA  
3289 C C   . SER B 75  ? 0.23593 0.16441 0.23151 0.02564  -0.01129 0.02561  509 SER B C   
3290 O O   . SER B 75  ? 0.19799 0.12524 0.19168 0.03134  -0.01438 0.01960  509 SER B O   
3291 C CB  A SER B 75  ? 0.23830 0.15342 0.23435 0.01511  -0.00997 0.02963  509 SER B CB  
3292 C CB  B SER B 75  ? 0.23833 0.15341 0.23434 0.01513  -0.00991 0.02976  509 SER B CB  
3293 O OG  A SER B 75  ? 0.23607 0.14678 0.22964 0.01447  -0.00665 0.03759  509 SER B OG  
3294 O OG  B SER B 75  ? 0.25157 0.15461 0.24172 0.02061  -0.01289 0.02525  509 SER B OG  
3295 N N   . ILE B 76  ? 0.22741 0.15610 0.22100 0.02662  -0.00864 0.03160  510 ILE B N   
3296 C CA  . ILE B 76  ? 0.23582 0.16254 0.22389 0.03420  -0.00964 0.03120  510 ILE B CA  
3297 C C   . ILE B 76  ? 0.21932 0.15914 0.21175 0.03630  -0.01145 0.02527  510 ILE B C   
3298 O O   . ILE B 76  ? 0.18532 0.12463 0.17549 0.04240  -0.01469 0.02020  510 ILE B O   
3299 C CB  . ILE B 76  ? 0.19149 0.11556 0.17593 0.03419  -0.00586 0.03873  510 ILE B CB  
3300 C CG1 . ILE B 76  ? 0.20095 0.10933 0.17807 0.03458  -0.00466 0.04390  510 ILE B CG1 
3301 C CG2 . ILE B 76  ? 0.17242 0.09964 0.15305 0.04038  -0.00669 0.03750  510 ILE B CG2 
3302 C CD1 . ILE B 76  ? 0.33107 0.23764 0.30590 0.03251  0.00029  0.05178  510 ILE B CD1 
3303 N N   . ILE B 77  ? 0.21973 0.17160 0.21866 0.03121  -0.00945 0.02591  511 ILE B N   
3304 C CA  . ILE B 77  ? 0.17301 0.13687 0.17573 0.03233  -0.01069 0.02081  511 ILE B CA  
3305 C C   . ILE B 77  ? 0.23757 0.20500 0.24313 0.03272  -0.01365 0.01313  511 ILE B C   
3306 O O   . ILE B 77  ? 0.19095 0.16479 0.19768 0.03636  -0.01563 0.00758  511 ILE B O   
3307 C CB  . ILE B 77  ? 0.14896 0.12333 0.15726 0.02669  -0.00782 0.02390  511 ILE B CB  
3308 C CG1 . ILE B 77  ? 0.21411 0.18501 0.21967 0.02730  -0.00451 0.03099  511 ILE B CG1 
3309 C CG2 . ILE B 77  ? 0.20018 0.18598 0.21188 0.02705  -0.00886 0.01889  511 ILE B CG2 
3310 C CD1 . ILE B 77  ? 0.17302 0.14065 0.17247 0.03379  -0.00513 0.03037  511 ILE B CD1 
3311 N N   . LYS B 78  ? 0.23259 0.19613 0.23934 0.02894  -0.01390 0.01235  512 LYS B N   
3312 C CA  . LYS B 78  ? 0.19934 0.16465 0.20773 0.02997  -0.01640 0.00466  512 LYS B CA  
3313 C C   . LYS B 78  ? 0.23473 0.19229 0.23870 0.03847  -0.01936 0.00089  512 LYS B C   
3314 O O   . LYS B 78  ? 0.20610 0.17018 0.21247 0.04211  -0.02140 -0.00602 512 LYS B O   
3315 C CB  . LYS B 78  ? 0.13899 0.09946 0.14815 0.02426  -0.01617 0.00468  512 LYS B CB  
3316 C CG  . LYS B 78  ? 0.27100 0.22934 0.28002 0.02616  -0.01855 -0.00327 512 LYS B CG  
3317 C CD  . LYS B 78  ? 0.28395 0.23976 0.29400 0.01899  -0.01819 -0.00375 512 LYS B CD  
3318 C CE  . LYS B 78  ? 0.34830 0.29151 0.35444 0.02195  -0.02023 -0.00852 512 LYS B CE  
3319 N NZ  . LYS B 78  ? 0.29280 0.23260 0.29926 0.01439  -0.02005 -0.00921 512 LYS B NZ  
3320 N N   . SER B 79  ? 0.15597 0.10000 0.15351 0.04186  -0.01961 0.00555  513 SER B N   
3321 C CA  . SER B 79  ? 0.16457 0.09976 0.15703 0.05039  -0.02291 0.00278  513 SER B CA  
3322 C C   . SER B 79  ? 0.24616 0.19005 0.23936 0.05617  -0.02481 -0.00024 513 SER B C   
3323 O O   . SER B 79  ? 0.26536 0.20788 0.25762 0.06322  -0.02831 -0.00519 513 SER B O   
3324 C CB  . SER B 79  ? 0.23079 0.14952 0.21502 0.05227  -0.02245 0.00957  513 SER B CB  
3325 O OG  . SER B 79  ? 0.22251 0.14175 0.20295 0.05448  -0.02133 0.01451  513 SER B OG  
3326 N N   . SER B 80  ? 0.16252 0.11538 0.15763 0.05338  -0.02271 0.00251  514 SER B N   
3327 C CA  . SER B 80  ? 0.19602 0.15638 0.19129 0.05809  -0.02452 -0.00011 514 SER B CA  
3328 C C   . SER B 80  ? 0.20104 0.17327 0.20288 0.05981  -0.02679 -0.00873 514 SER B C   
3329 O O   . SER B 80  ? 0.28615 0.26285 0.28815 0.06541  -0.02964 -0.01233 514 SER B O   
3330 C CB  . SER B 80  ? 0.16621 0.13334 0.16248 0.05384  -0.02140 0.00409  514 SER B CB  
3331 O OG  . SER B 80  ? 0.21155 0.19081 0.21517 0.04770  -0.01962 0.00172  514 SER B OG  
3332 N N   . GLU B 81  ? 0.14487 0.12271 0.15205 0.05500  -0.02559 -0.01223 515 GLU B N   
3333 C CA  . GLU B 81  ? 0.25265 0.24254 0.26614 0.05603  -0.02687 -0.02051 515 GLU B CA  
3334 C C   . GLU B 81  ? 0.23298 0.21949 0.24581 0.06487  -0.03084 -0.02594 515 GLU B C   
3335 O O   . GLU B 81  ? 0.21458 0.21262 0.23285 0.06765  -0.03234 -0.03255 515 GLU B O   
3336 C CB  . GLU B 81  ? 0.30457 0.29833 0.32180 0.04944  -0.02477 -0.02286 515 GLU B CB  
3337 C CG  . GLU B 81  ? 0.22493 0.22928 0.24773 0.05060  -0.02554 -0.03181 515 GLU B CG  
3338 C CD  . GLU B 81  ? 0.28756 0.29652 0.31281 0.04320  -0.02315 -0.03375 515 GLU B CD  
3339 O OE1 . GLU B 81  ? 0.23119 0.23435 0.25409 0.03757  -0.02157 -0.02821 515 GLU B OE1 
3340 O OE2 . GLU B 81  ? 0.40031 0.41925 0.42984 0.04293  -0.02284 -0.04084 515 GLU B OE2 
3341 N N   . HIS B 82  ? 0.26370 0.23485 0.27020 0.06944  -0.03258 -0.02321 516 HIS B N   
3342 C CA  . HIS B 82  ? 0.31191 0.27813 0.31741 0.07844  -0.03663 -0.02798 516 HIS B CA  
3343 C C   . HIS B 82  ? 0.31153 0.27113 0.31019 0.08321  -0.03885 -0.02377 516 HIS B C   
3344 O O   . HIS B 82  ? 0.29853 0.25217 0.29405 0.08740  -0.04103 -0.02490 516 HIS B O   
3345 C CB  . HIS B 82  ? 0.27232 0.22548 0.27506 0.07865  -0.03663 -0.02870 516 HIS B CB  
3346 C CG  . HIS B 82  ? 0.39018 0.35019 0.39817 0.07178  -0.03391 -0.03282 516 HIS B CG  
3347 N ND1 . HIS B 82  ? 0.44667 0.41905 0.46146 0.07312  -0.03420 -0.04137 516 HIS B ND1 
3348 C CD2 . HIS B 82  ? 0.54818 0.50483 0.55538 0.06343  -0.03092 -0.02963 516 HIS B CD2 
3349 C CE1 . HIS B 82  ? 0.44715 0.42273 0.46403 0.06587  -0.03143 -0.04321 516 HIS B CE1 
3350 N NE2 . HIS B 82  ? 0.61668 0.58294 0.62916 0.05994  -0.02973 -0.03620 516 HIS B NE2 
3351 N N   . MET B 83  ? 0.26006 0.17859 0.19266 0.09667  -0.06385 -0.02147 517 MET B N   
3352 C CA  . MET B 83  ? 0.41232 0.32289 0.33332 0.10211  -0.06789 -0.01724 517 MET B CA  
3353 C C   . MET B 83  ? 0.33845 0.26671 0.26689 0.11169  -0.07285 -0.02493 517 MET B C   
3354 O O   . MET B 83  ? 0.29423 0.24500 0.23864 0.11018  -0.07074 -0.03207 517 MET B O   
3355 C CB  . MET B 83  ? 0.33112 0.24128 0.24835 0.09223  -0.06216 -0.00925 517 MET B CB  
3356 C CG  . MET B 83  ? 0.27913 0.16753 0.18344 0.08506  -0.05918 -0.00010 517 MET B CG  
3357 S SD  . MET B 83  ? 0.39325 0.28677 0.29651 0.07341  -0.05163 0.00755  517 MET B SD  
3358 C CE  . MET B 83  ? 0.28697 0.15535 0.17618 0.06547  -0.04871 0.01671  517 MET B CE  
3359 N N   . LYS B 84  ? 0.30899 0.22658 0.22514 0.12136  -0.07959 -0.02340 518 LYS B N   
3360 C CA  . LYS B 84  ? 0.29250 0.22662 0.21429 0.12992  -0.08460 -0.02980 518 LYS B CA  
3361 C C   . LYS B 84  ? 0.35448 0.30451 0.28329 0.12166  -0.07946 -0.02829 518 LYS B C   
3362 O O   . LYS B 84  ? 0.26336 0.20496 0.18540 0.11280  -0.07425 -0.02012 518 LYS B O   
3363 C CB  . LYS B 84  ? 0.39383 0.31285 0.29949 0.13650  -0.08975 -0.02759 518 LYS B CB  
3364 C CG  . LYS B 84  ? 0.33191 0.24293 0.23400 0.14424  -0.09474 -0.03284 518 LYS B CG  
3365 C CD  . LYS B 84  ? 0.31351 0.24933 0.23141 0.14963  -0.09713 -0.04492 518 LYS B CD  
3366 C CE  . LYS B 84  ? 0.33400 0.26229 0.24570 0.15896  -0.10334 -0.05028 518 LYS B CE  
3367 N NZ  . LYS B 84  ? 0.37849 0.33199 0.30488 0.16390  -0.10561 -0.06215 518 LYS B NZ  
3368 N N   . PRO B 85  ? 0.38150 0.35492 0.32415 0.12422  -0.08083 -0.03649 519 PRO B N   
3369 C CA  . PRO B 85  ? 0.23489 0.22274 0.18450 0.11617  -0.07619 -0.03576 519 PRO B CA  
3370 C C   . PRO B 85  ? 0.35124 0.32716 0.28610 0.11549  -0.07652 -0.02775 519 PRO B C   
3371 O O   . PRO B 85  ? 0.32773 0.30648 0.26369 0.10609  -0.07051 -0.02346 519 PRO B O   
3372 C CB  . PRO B 85  ? 0.22649 0.23783 0.19016 0.12194  -0.08016 -0.04644 519 PRO B CB  
3373 C CG  . PRO B 85  ? 0.22985 0.24422 0.19967 0.12661  -0.08189 -0.05321 519 PRO B CG  
3374 C CD  . PRO B 85  ? 0.26155 0.24993 0.21471 0.13134  -0.08473 -0.04721 519 PRO B CD  
3375 N N   . ARG B 86  ? 0.32991 0.29216 0.25028 0.12495  -0.08300 -0.02566 520 ARG B N   
3376 C CA  . ARG B 86  ? 0.27638 0.22734 0.18158 0.12381  -0.08259 -0.01809 520 ARG B CA  
3377 C C   . ARG B 86  ? 0.28471 0.21512 0.17676 0.11685  -0.07787 -0.00732 520 ARG B C   
3378 O O   . ARG B 86  ? 0.30244 0.23038 0.18787 0.11078  -0.07365 -0.00120 520 ARG B O   
3379 C CB  . ARG B 86  ? 0.29687 0.24037 0.19168 0.13204  -0.08798 -0.01998 520 ARG B CB  
3380 C CG  . ARG B 86  ? 0.39856 0.36333 0.30526 0.13620  -0.09100 -0.02990 520 ARG B CG  
3381 C CD  . ARG B 86  ? 0.32701 0.30323 0.23702 0.13116  -0.08822 -0.02892 520 ARG B CD  
3382 N NE  . ARG B 86  ? 0.39846 0.39891 0.32642 0.13055  -0.08866 -0.03882 520 ARG B NE  
3383 C CZ  . ARG B 86  ? 0.39921 0.41216 0.33293 0.12622  -0.08678 -0.04032 520 ARG B CZ  
3384 N NH1 . ARG B 86  ? 0.49141 0.49636 0.41454 0.12293  -0.08450 -0.03307 520 ARG B NH1 
3385 N NH2 . ARG B 86  ? 0.41520 0.44888 0.36516 0.12483  -0.08700 -0.04953 520 ARG B NH2 
3386 N N   . ASP B 87  ? 0.38665 0.30311 0.27555 0.11638  -0.07765 -0.00552 521 ASP B N   
3387 C CA  . ASP B 87  ? 0.42696 0.32694 0.30708 0.10659  -0.07150 0.00352  521 ASP B CA  
3388 C C   . ASP B 87  ? 0.27465 0.18919 0.16821 0.09431  -0.06300 0.00371  521 ASP B C   
3389 O O   . ASP B 87  ? 0.29264 0.20103 0.18026 0.08578  -0.05735 0.01091  521 ASP B O   
3390 C CB  . ASP B 87  ? 0.34744 0.23023 0.22277 0.10857  -0.07356 0.00409  521 ASP B CB  
3391 C CG  . ASP B 87  ? 0.45125 0.31286 0.30847 0.11766  -0.08026 0.00688  521 ASP B CG  
3392 O OD1 . ASP B 87  ? 0.51758 0.36915 0.36093 0.11577  -0.07919 0.01361  521 ASP B OD1 
3393 O OD2 . ASP B 87  ? 0.50595 0.36394 0.36485 0.12399  -0.08457 0.00129  521 ASP B OD2 
3394 N N   . LEU B 88  ? 0.26578 0.19970 0.17713 0.09331  -0.06201 -0.00423 522 LEU B N   
3395 C CA  . LEU B 88  ? 0.23400 0.18182 0.15735 0.08276  -0.05481 -0.00446 522 LEU B CA  
3396 C C   . LEU B 88  ? 0.26728 0.22256 0.18885 0.08034  -0.05293 -0.00227 522 LEU B C   
3397 O O   . LEU B 88  ? 0.31446 0.27252 0.23814 0.07150  -0.04680 0.00140  522 LEU B O   
3398 C CB  . LEU B 88  ? 0.28402 0.25050 0.22494 0.08281  -0.05462 -0.01346 522 LEU B CB  
3399 C CG  . LEU B 88  ? 0.30971 0.27242 0.25528 0.08190  -0.05387 -0.01585 522 LEU B CG  
3400 C CD1 . LEU B 88  ? 0.20146 0.18452 0.16359 0.08225  -0.05344 -0.02499 522 LEU B CD1 
3401 C CD2 . LEU B 88  ? 0.27637 0.23073 0.21999 0.07145  -0.04751 -0.00959 522 LEU B CD2 
3402 N N   . ASN B 89  ? 0.33066 0.28967 0.24840 0.08858  -0.05848 -0.00502 523 ASN B N   
3403 C CA  . ASN B 89  ? 0.33822 0.30337 0.25294 0.08707  -0.05726 -0.00336 523 ASN B CA  
3404 C C   . ASN B 89  ? 0.32118 0.27074 0.22004 0.08321  -0.05382 0.00634  523 ASN B C   
3405 O O   . ASN B 89  ? 0.32135 0.27600 0.22092 0.07662  -0.04866 0.00910  523 ASN B O   
3406 C CB  . ASN B 89  ? 0.32355 0.29513 0.23642 0.09735  -0.06473 -0.00865 523 ASN B CB  
3407 C CG  . ASN B 89  ? 0.41031 0.39281 0.32435 0.09559  -0.06376 -0.00971 523 ASN B CG  
3408 O OD1 . ASN B 89  ? 0.36218 0.33690 0.26237 0.09836  -0.06505 -0.00518 523 ASN B OD1 
3409 N ND2 . ASN B 89  ? 0.47909 0.47898 0.40891 0.09081  -0.06145 -0.01574 523 ASN B ND2 
3410 N N   . ARG B 90  ? 0.37732 0.30761 0.26140 0.08719  -0.05658 0.01148  524 ARG B N   
3411 C CA  . ARG B 90  ? 0.33270 0.24751 0.20067 0.08270  -0.05290 0.02104  524 ARG B CA  
3412 C C   . ARG B 90  ? 0.33062 0.24472 0.20382 0.07085  -0.04489 0.02503  524 ARG B C   
3413 O O   . ARG B 90  ? 0.28640 0.20067 0.15502 0.06431  -0.03941 0.03022  524 ARG B O   
3414 C CB  . ARG B 90  ? 0.30711 0.19943 0.15723 0.08935  -0.05803 0.02562  524 ARG B CB  
3415 N N   . LEU B 91  ? 0.27713 0.19125 0.15994 0.06830  -0.04424 0.02225  525 LEU B N   
3416 C CA  . LEU B 91  ? 0.25396 0.16908 0.14305 0.05748  -0.03733 0.02498  525 LEU B CA  
3417 C C   . LEU B 91  ? 0.31680 0.25039 0.21743 0.05194  -0.03257 0.02278  525 LEU B C   
3418 O O   . LEU B 91  ? 0.26861 0.20279 0.16782 0.04440  -0.02687 0.02733  525 LEU B O   
3419 C CB  . LEU B 91  ? 0.24949 0.16306 0.14727 0.05703  -0.03836 0.02100  525 LEU B CB  
3420 C CG  . LEU B 91  ? 0.36009 0.27710 0.26656 0.04666  -0.03218 0.02209  525 LEU B CG  
3421 C CD1 . LEU B 91  ? 0.24997 0.15470 0.14604 0.03897  -0.02761 0.03040  525 LEU B CD1 
3422 C CD2 . LEU B 91  ? 0.23625 0.15033 0.14910 0.04773  -0.03414 0.01774  525 LEU B CD2 
3423 N N   . GLY B 92  ? 0.27150 0.22028 0.18349 0.05563  -0.03497 0.01554  526 GLY B N   
3424 C CA  . GLY B 92  ? 0.20234 0.16655 0.12432 0.05077  -0.03114 0.01319  526 GLY B CA  
3425 C C   . GLY B 92  ? 0.32318 0.28796 0.23671 0.05004  -0.02914 0.01710  526 GLY B C   
3426 O O   . GLY B 92  ? 0.33508 0.30647 0.25253 0.04389  -0.02413 0.01841  526 GLY B O   
3427 N N   . ASP B 93  ? 0.26084 0.21878 0.16212 0.05685  -0.03321 0.01877  527 ASP B N   
3428 C CA  . ASP B 93  ? 0.30072 0.25882 0.19219 0.05671  -0.03133 0.02247  527 ASP B CA  
3429 C C   . ASP B 93  ? 0.38691 0.33693 0.27055 0.04917  -0.02492 0.03021  527 ASP B C   
3430 O O   . ASP B 93  ? 0.41343 0.36832 0.29332 0.04665  -0.02118 0.03243  527 ASP B O   
3431 C CB  . ASP B 93  ? 0.36499 0.31567 0.24296 0.06593  -0.03741 0.02307  527 ASP B CB  
3432 C CG  . ASP B 93  ? 0.44523 0.40850 0.33110 0.07290  -0.04320 0.01484  527 ASP B CG  
3433 O OD1 . ASP B 93  ? 0.36206 0.33961 0.26277 0.06955  -0.04165 0.00930  527 ASP B OD1 
3434 O OD2 . ASP B 93  ? 0.47882 0.43739 0.35567 0.08158  -0.04948 0.01386  527 ASP B OD2 
3435 N N   . GLU B 94  ? 0.34226 0.28066 0.22359 0.04542  -0.02357 0.03391  528 GLU B N   
3436 C CA  . GLU B 94  ? 0.32755 0.25915 0.20269 0.03706  -0.01730 0.04085  528 GLU B CA  
3437 C C   . GLU B 94  ? 0.29195 0.23729 0.18010 0.02930  -0.01146 0.03932  528 GLU B C   
3438 O O   . GLU B 94  ? 0.40837 0.35262 0.29319 0.02231  -0.00584 0.04411  528 GLU B O   
3439 C CB  . GLU B 94  ? 0.26222 0.17665 0.13147 0.03491  -0.01807 0.04460  528 GLU B CB  
3440 C CG  . GLU B 94  ? 0.28826 0.18385 0.13785 0.03942  -0.02122 0.05028  528 GLU B CG  
3441 C CD  . GLU B 94  ? 0.44701 0.32411 0.29098 0.03980  -0.02418 0.05228  528 GLU B CD  
3442 O OE1 . GLU B 94  ? 0.42428 0.30071 0.27619 0.03264  -0.02103 0.05221  528 GLU B OE1 
3443 O OE2 . GLU B 94  ? 0.46753 0.33035 0.29870 0.04778  -0.03012 0.05357  528 GLU B OE2 
3444 N N   . TYR B 95  ? 0.26691 0.22505 0.16930 0.03027  -0.01266 0.03278  529 TYR B N   
3445 C CA  . TYR B 95  ? 0.19766 0.16807 0.11129 0.02421  -0.00805 0.03104  529 TYR B CA  
3446 C C   . TYR B 95  ? 0.21008 0.19261 0.12661 0.02719  -0.00833 0.02743  529 TYR B C   
3447 O O   . TYR B 95  ? 0.21555 0.19844 0.12767 0.03371  -0.01247 0.02521  529 TYR B O   
3448 C CB  . TYR B 95  ? 0.19962 0.17382 0.12613 0.02204  -0.00875 0.02680  529 TYR B CB  
3449 C CG  . TYR B 95  ? 0.21932 0.18159 0.14363 0.01973  -0.00917 0.02912  529 TYR B CG  
3450 C CD1 . TYR B 95  ? 0.19362 0.15216 0.11763 0.01205  -0.00474 0.03312  529 TYR B CD1 
3451 C CD2 . TYR B 95  ? 0.22013 0.17531 0.14306 0.02541  -0.01428 0.02669  529 TYR B CD2 
3452 C CE1 . TYR B 95  ? 0.22623 0.17275 0.14790 0.00967  -0.00549 0.03484  529 TYR B CE1 
3453 C CE2 . TYR B 95  ? 0.20545 0.14860 0.12577 0.02393  -0.01512 0.02828  529 TYR B CE2 
3454 C CZ  . TYR B 95  ? 0.20987 0.14799 0.12926 0.01585  -0.01076 0.03244  529 TYR B CZ  
3455 O OH  . TYR B 95  ? 0.37631 0.30135 0.29272 0.01414  -0.01194 0.03365  529 TYR B OH  
3456 N N   . ASN B 96  ? 0.17694 0.16922 0.10087 0.02261  -0.00427 0.02647  530 ASN B N   
3457 C CA  . ASN B 96  ? 0.23240 0.23536 0.15935 0.02483  -0.00424 0.02280  530 ASN B CA  
3458 C C   . ASN B 96  ? 0.16162 0.17098 0.10011 0.02605  -0.00727 0.01647  530 ASN B C   
3459 O O   . ASN B 96  ? 0.15337 0.16576 0.10073 0.02181  -0.00557 0.01524  530 ASN B O   
3460 C CB  . ASN B 96  ? 0.27187 0.28156 0.20047 0.01997  0.00131  0.02467  530 ASN B CB  
3461 C CG  . ASN B 96  ? 0.30375 0.32338 0.23481 0.02272  0.00122  0.02062  530 ASN B CG  
3462 O OD1 . ASN B 96  ? 0.34056 0.36170 0.27175 0.02762  -0.00291 0.01656  530 ASN B OD1 
3463 N ND2 . ASN B 96  ? 0.36046 0.38721 0.29361 0.01969  0.00559  0.02128  530 ASN B ND2 
3464 N N   . SER B 97  ? 0.16385 0.17534 0.10181 0.03154  -0.01174 0.01242  531 SER B N   
3465 C CA  . SER B 97  ? 0.14731 0.16540 0.09553 0.03219  -0.01451 0.00616  531 SER B CA  
3466 C C   . SER B 97  ? 0.15765 0.17378 0.11306 0.02977  -0.01483 0.00520  531 SER B C   
3467 O O   . SER B 97  ? 0.18748 0.20709 0.15079 0.02528  -0.01267 0.00395  531 SER B O   
3468 C CB  . SER B 97  ? 0.13705 0.16254 0.09098 0.02943  -0.01237 0.00371  531 SER B CB  
3469 O OG  . SER B 97  ? 0.19200 0.21946 0.13907 0.03171  -0.01154 0.00448  531 SER B OG  
3470 N N   . ILE B 98  ? 0.18987 0.19999 0.14159 0.03345  -0.01790 0.00560  532 ILE B N   
3471 C CA  . ILE B 98  ? 0.14633 0.15408 0.10359 0.03240  -0.01864 0.00426  532 ILE B CA  
3472 C C   . ILE B 98  ? 0.19218 0.19966 0.14897 0.03913  -0.02407 0.00045  532 ILE B C   
3473 O O   . ILE B 98  ? 0.26872 0.26978 0.21578 0.04443  -0.02700 0.00248  532 ILE B O   
3474 C CB  . ILE B 98  ? 0.15306 0.15063 0.10526 0.02911  -0.01603 0.00986  532 ILE B CB  
3475 C CG1 . ILE B 98  ? 0.15503 0.15588 0.11186 0.02202  -0.01103 0.01180  532 ILE B CG1 
3476 C CG2 . ILE B 98  ? 0.17862 0.17105 0.13310 0.03077  -0.01847 0.00810  532 ILE B CG2 
3477 C CD1 . ILE B 98  ? 0.15597 0.16231 0.12338 0.01886  -0.01042 0.00802  532 ILE B CD1 
3478 N N   . PHE B 99  ? 0.15959 0.17437 0.12652 0.03906  -0.02543 -0.00519 533 PHE B N   
3479 C CA  . PHE B 99  ? 0.16556 0.18172 0.13427 0.04524  -0.03027 -0.00962 533 PHE B CA  
3480 C C   . PHE B 99  ? 0.19417 0.20779 0.16753 0.04369  -0.02939 -0.01053 533 PHE B C   
3481 O O   . PHE B 99  ? 0.15957 0.17541 0.13862 0.03735  -0.02539 -0.01015 533 PHE B O   
3482 C CB  . PHE B 99  ? 0.14108 0.17069 0.11852 0.04685  -0.03282 -0.01685 533 PHE B CB  
3483 C CG  . PHE B 99  ? 0.12811 0.16668 0.11679 0.04019  -0.02947 -0.02028 533 PHE B CG  
3484 C CD1 . PHE B 99  ? 0.13380 0.17678 0.13025 0.03924  -0.02916 -0.02400 533 PHE B CD1 
3485 C CD2 . PHE B 99  ? 0.17727 0.21933 0.16783 0.03522  -0.02679 -0.01993 533 PHE B CD2 
3486 C CE1 . PHE B 99  ? 0.15039 0.20079 0.15550 0.03279  -0.02582 -0.02667 533 PHE B CE1 
3487 C CE2 . PHE B 99  ? 0.16252 0.21060 0.16148 0.02913  -0.02400 -0.02255 533 PHE B CE2 
3488 C CZ  . PHE B 99  ? 0.10866 0.16080 0.11454 0.02759  -0.02331 -0.02563 533 PHE B CZ  
3489 N N   . ILE B 100 ? 0.21004 0.21851 0.18025 0.05009  -0.03353 -0.01196 534 ILE B N   
3490 C CA  . ILE B 100 ? 0.20036 0.20466 0.17324 0.04993  -0.03335 -0.01306 534 ILE B CA  
3491 C C   . ILE B 100 ? 0.18123 0.19309 0.15999 0.05701  -0.03806 -0.02046 534 ILE B C   
3492 O O   . ILE B 100 ? 0.19157 0.20484 0.16715 0.06426  -0.04298 -0.02264 534 ILE B O   
3493 C CB  . ILE B 100 ? 0.19670 0.18314 0.15776 0.05062  -0.03359 -0.00665 534 ILE B CB  
3494 C CG1 . ILE B 100 ? 0.26039 0.24132 0.21502 0.04441  -0.02925 0.00040  534 ILE B CG1 
3495 C CG2 . ILE B 100 ? 0.18875 0.17066 0.15307 0.04849  -0.03248 -0.00767 534 ILE B CG2 
3496 C CD1 . ILE B 100 ? 0.21547 0.17911 0.15815 0.04359  -0.02889 0.00701  534 ILE B CD1 
3497 N N   . SER B 101 ? 0.21966 0.23737 0.20705 0.05515  -0.03660 -0.02470 535 SER B N   
3498 C CA  . SER B 101 ? 0.23729 0.26218 0.23064 0.06181  -0.04042 -0.03202 535 SER B CA  
3499 C C   . SER B 101 ? 0.20474 0.22010 0.19602 0.06240  -0.04004 -0.03156 535 SER B C   
3500 O O   . SER B 101 ? 0.21120 0.21542 0.19726 0.05691  -0.03681 -0.02579 535 SER B O   
3501 C CB  . SER B 101 ? 0.17089 0.21548 0.17801 0.05859  -0.03855 -0.03914 535 SER B CB  
3502 O OG  . SER B 101 ? 0.17465 0.22204 0.18720 0.05089  -0.03319 -0.03906 535 SER B OG  
3503 N N   . ASN B 102 ? 0.21973 0.24012 0.21544 0.06931  -0.04356 -0.03828 536 ASN B N   
3504 C CA  . ASN B 102 ? 0.17133 0.18202 0.16447 0.07118  -0.04403 -0.03883 536 ASN B CA  
3505 C C   . ASN B 102 ? 0.15998 0.17618 0.16005 0.06259  -0.03812 -0.03953 536 ASN B C   
3506 O O   . ASN B 102 ? 0.19828 0.20438 0.19493 0.06199  -0.03764 -0.03857 536 ASN B O   
3507 C CB  . ASN B 102 ? 0.17906 0.19502 0.17545 0.08196  -0.04965 -0.04683 536 ASN B CB  
3508 C CG  . ASN B 102 ? 0.25332 0.25580 0.23820 0.09203  -0.05668 -0.04491 536 ASN B CG  
3509 O OD1 . ASN B 102 ? 0.39632 0.40681 0.38239 0.09772  -0.06059 -0.04769 536 ASN B OD1 
3510 N ND2 . ASN B 102 ? 0.30459 0.28566 0.27749 0.09408  -0.05852 -0.04007 536 ASN B ND2 
3511 N N   . GLU B 103 ? 0.14578 0.17661 0.15454 0.05599  -0.03394 -0.04116 537 GLU B N   
3512 C CA  . GLU B 103 ? 0.13609 0.17213 0.15028 0.04796  -0.02851 -0.04162 537 GLU B CA  
3513 C C   . GLU B 103 ? 0.15441 0.18405 0.16477 0.03947  -0.02445 -0.03437 537 GLU B C   
3514 O O   . GLU B 103 ? 0.12376 0.15614 0.13716 0.03292  -0.02034 -0.03401 537 GLU B O   
3515 C CB  . GLU B 103 ? 0.12916 0.18512 0.15489 0.04577  -0.02632 -0.04845 537 GLU B CB  
3516 C CG  . GLU B 103 ? 0.12994 0.19704 0.16190 0.05414  -0.03009 -0.05697 537 GLU B CG  
3517 C CD  . GLU B 103 ? 0.13192 0.20541 0.16538 0.05966  -0.03450 -0.05921 537 GLU B CD  
3518 O OE1 . GLU B 103 ? 0.20435 0.27195 0.23270 0.05747  -0.03479 -0.05385 537 GLU B OE1 
3519 O OE2 . GLU B 103 ? 0.21002 0.29540 0.24999 0.06651  -0.03785 -0.06687 537 GLU B OE2 
3520 N N   . SER B 104 ? 0.14951 0.17109 0.15292 0.03989  -0.02565 -0.02886 538 SER B N   
3521 C CA  . SER B 104 ? 0.13491 0.15294 0.13563 0.03261  -0.02191 -0.02282 538 SER B CA  
3522 C C   . SER B 104 ? 0.13016 0.13984 0.12852 0.02766  -0.01925 -0.01963 538 SER B C   
3523 O O   . SER B 104 ? 0.12172 0.13563 0.12345 0.02123  -0.01556 -0.01873 538 SER B O   
3524 C CB  . SER B 104 ? 0.13622 0.14630 0.12861 0.03481  -0.02369 -0.01769 538 SER B CB  
3525 O OG  . SER B 104 ? 0.13737 0.15583 0.13187 0.03893  -0.02625 -0.02077 538 SER B OG  
3526 N N   . TYR B 105 ? 0.14160 0.13861 0.13360 0.03067  -0.02150 -0.01800 539 TYR B N   
3527 C CA  . TYR B 105 ? 0.14399 0.13227 0.13350 0.02572  -0.01948 -0.01523 539 TYR B CA  
3528 C C   . TYR B 105 ? 0.14111 0.13799 0.13781 0.02250  -0.01708 -0.01966 539 TYR B C   
3529 O O   . TYR B 105 ? 0.13046 0.12751 0.12809 0.01608  -0.01398 -0.01744 539 TYR B O   
3530 C CB  . TYR B 105 ? 0.15986 0.13249 0.14137 0.03010  -0.02300 -0.01408 539 TYR B CB  
3531 C CG  . TYR B 105 ? 0.19213 0.15506 0.17127 0.02532  -0.02170 -0.01241 539 TYR B CG  
3532 C CD1 . TYR B 105 ? 0.16231 0.12186 0.13970 0.01756  -0.01841 -0.00702 539 TYR B CD1 
3533 C CD2 . TYR B 105 ? 0.22941 0.18702 0.20820 0.02882  -0.02404 -0.01680 539 TYR B CD2 
3534 C CE1 . TYR B 105 ? 0.16691 0.11849 0.14280 0.01284  -0.01757 -0.00606 539 TYR B CE1 
3535 C CE2 . TYR B 105 ? 0.17692 0.12523 0.15335 0.02434  -0.02327 -0.01579 539 TYR B CE2 
3536 C CZ  . TYR B 105 ? 0.22221 0.16765 0.19738 0.01608  -0.02009 -0.01040 539 TYR B CZ  
3537 O OH  . TYR B 105 ? 0.19531 0.13242 0.16881 0.01130  -0.01966 -0.00996 539 TYR B OH  
3538 N N   . THR B 106 ? 0.18068 0.18575 0.18240 0.02703  -0.01844 -0.02617 540 THR B N   
3539 C CA  . THR B 106 ? 0.12831 0.14218 0.13592 0.02402  -0.01575 -0.03057 540 THR B CA  
3540 C C   . THR B 106 ? 0.12788 0.15122 0.13958 0.01715  -0.01169 -0.02923 540 THR B C   
3541 O O   . THR B 106 ? 0.11312 0.13703 0.12529 0.01197  -0.00893 -0.02864 540 THR B O   
3542 C CB  . THR B 106 ? 0.12984 0.15318 0.14265 0.03028  -0.01757 -0.03823 540 THR B CB  
3543 O OG1 . THR B 106 ? 0.31471 0.32760 0.32309 0.03657  -0.02131 -0.04012 540 THR B OG1 
3544 C CG2 . THR B 106 ? 0.12209 0.15801 0.14134 0.02612  -0.01366 -0.04269 540 THR B CG2 
3545 N N   . CYS B 107 ? 0.17568 0.20553 0.18955 0.01731  -0.01171 -0.02884 541 CYS B N   
3546 C CA  . CYS B 107 ? 0.15802 0.19506 0.17483 0.01118  -0.00837 -0.02779 541 CYS B CA  
3547 C C   . CYS B 107 ? 0.10176 0.13138 0.11424 0.00646  -0.00677 -0.02171 541 CYS B C   
3548 O O   . CYS B 107 ? 0.11492 0.14751 0.12845 0.00135  -0.00412 -0.02086 541 CYS B O   
3549 C CB  . CYS B 107 ? 0.13443 0.17916 0.15429 0.01266  -0.00935 -0.02936 541 CYS B CB  
3550 S SG  . CYS B 107 ? 0.19047 0.24827 0.21780 0.01769  -0.01113 -0.03772 541 CYS B SG  
3551 N N   . ALA B 108 ? 0.10720 0.12743 0.11451 0.00808  -0.00835 -0.01753 542 ALA B N   
3552 C CA  . ALA B 108 ? 0.12059 0.13555 0.12485 0.00351  -0.00663 -0.01247 542 ALA B CA  
3553 C C   . ALA B 108 ? 0.13923 0.15148 0.14369 0.00018  -0.00547 -0.01294 542 ALA B C   
3554 O O   . ALA B 108 ? 0.17738 0.19110 0.18229 -0.00433 -0.00356 -0.01116 542 ALA B O   
3555 C CB  . ALA B 108 ? 0.11363 0.11968 0.11207 0.00526  -0.00801 -0.00806 542 ALA B CB  
3556 N N   . LEU B 109 ? 0.13594 0.14417 0.13975 0.00294  -0.00705 -0.01578 543 LEU B N   
3557 C CA  . LEU B 109 ? 0.11423 0.12012 0.11802 0.00029  -0.00634 -0.01724 543 LEU B CA  
3558 C C   . LEU B 109 ? 0.10907 0.12434 0.11635 -0.00264 -0.00389 -0.01998 543 LEU B C   
3559 O O   . LEU B 109 ? 0.20330 0.21802 0.20980 -0.00671 -0.00262 -0.01901 543 LEU B O   
3560 C CB  . LEU B 109 ? 0.12315 0.12318 0.12539 0.00493  -0.00887 -0.02083 543 LEU B CB  
3561 C CG  . LEU B 109 ? 0.13412 0.12103 0.13058 0.00744  -0.01161 -0.01778 543 LEU B CG  
3562 C CD1 . LEU B 109 ? 0.14446 0.12420 0.13875 0.01235  -0.01456 -0.02198 543 LEU B CD1 
3563 C CD2 . LEU B 109 ? 0.16451 0.14468 0.15811 0.00136  -0.01031 -0.01258 543 LEU B CD2 
3564 N N   . LEU B 110 ? 0.10379 0.12773 0.11456 -0.00085 -0.00327 -0.02346 544 LEU B N   
3565 C CA  . LEU B 110 ? 0.11587 0.14789 0.12878 -0.00450 -0.00045 -0.02564 544 LEU B CA  
3566 C C   . LEU B 110 ? 0.11198 0.14420 0.12358 -0.00903 0.00107  -0.02154 544 LEU B C   
3567 O O   . LEU B 110 ? 0.18395 0.21731 0.19408 -0.01281 0.00284  -0.02126 544 LEU B O   
3568 C CB  . LEU B 110 ? 0.09759 0.13966 0.11515 -0.00239 0.00015  -0.03052 544 LEU B CB  
3569 C CG  . LEU B 110 ? 0.18597 0.23066 0.20548 0.00228  -0.00092 -0.03615 544 LEU B CG  
3570 C CD1 . LEU B 110 ? 0.16689 0.22418 0.19246 0.00433  -0.00031 -0.04145 544 LEU B CD1 
3571 C CD2 . LEU B 110 ? 0.19220 0.23646 0.20978 -0.00029 0.00095  -0.03787 544 LEU B CD2 
3572 N N   . ALA B 111 ? 0.09269 0.12343 0.10401 -0.00817 0.00014  -0.01852 545 ALA B N   
3573 C CA  . ALA B 111 ? 0.14065 0.17124 0.15053 -0.01142 0.00114  -0.01516 545 ALA B CA  
3574 C C   . ALA B 111 ? 0.08997 0.11610 0.09731 -0.01396 0.00130  -0.01248 545 ALA B C   
3575 O O   . ALA B 111 ? 0.09904 0.12604 0.10490 -0.01683 0.00227  -0.01167 545 ALA B O   
3576 C CB  . ALA B 111 ? 0.16671 0.19643 0.17628 -0.00928 -0.00005 -0.01284 545 ALA B CB  
3577 N N   . ALA B 112 ? 0.09334 0.11433 0.09981 -0.01303 0.00013  -0.01126 546 ALA B N   
3578 C CA  . ALA B 112 ? 0.09434 0.11243 0.09953 -0.01586 0.00007  -0.00938 546 ALA B CA  
3579 C C   . ALA B 112 ? 0.15275 0.17149 0.15723 -0.01747 0.00040  -0.01219 546 ALA B C   
3580 O O   . ALA B 112 ? 0.13999 0.15967 0.14314 -0.01995 0.00064  -0.01142 546 ALA B O   
3581 C CB  . ALA B 112 ? 0.15949 0.17143 0.16378 -0.01555 -0.00103 -0.00741 546 ALA B CB  
3582 N N   . GLY B 113 ? 0.13043 0.14888 0.13530 -0.01551 0.00020  -0.01579 547 GLY B N   
3583 C CA  . GLY B 113 ? 0.10122 0.12060 0.10476 -0.01667 0.00068  -0.01893 547 GLY B CA  
3584 C C   . GLY B 113 ? 0.13649 0.16121 0.13862 -0.01905 0.00277  -0.01942 547 GLY B C   
3585 O O   . GLY B 113 ? 0.13257 0.15702 0.13162 -0.02115 0.00307  -0.01993 547 GLY B O   
3586 N N   . SER B 114 ? 0.13886 0.16776 0.14247 -0.01894 0.00407  -0.01926 548 SER B N   
3587 C CA  . SER B 114 ? 0.17916 0.21087 0.18027 -0.02213 0.00607  -0.01876 548 SER B CA  
3588 C C   . SER B 114 ? 0.11953 0.14718 0.11682 -0.02402 0.00509  -0.01515 548 SER B C   
3589 O O   . SER B 114 ? 0.20149 0.22834 0.19413 -0.02623 0.00574  -0.01505 548 SER B O   
3590 C CB  . SER B 114 ? 0.09251 0.12789 0.09611 -0.02218 0.00697  -0.01876 548 SER B CB  
3591 O OG  . SER B 114 ? 0.17521 0.21634 0.18303 -0.02014 0.00761  -0.02287 548 SER B OG  
3592 N N   . CYS B 115 ? 0.12877 0.15421 0.12760 -0.02283 0.00343  -0.01234 549 CYS B N   
3593 C CA  . CYS B 115 ? 0.09849 0.12196 0.09487 -0.02371 0.00222  -0.00955 549 CYS B CA  
3594 C C   . CYS B 115 ? 0.09879 0.12094 0.09426 -0.02440 0.00079  -0.00995 549 CYS B C   
3595 O O   . CYS B 115 ? 0.20536 0.22691 0.19769 -0.02512 -0.00035 -0.00895 549 CYS B O   
3596 C CB  . CYS B 115 ? 0.12895 0.15251 0.12779 -0.02213 0.00138  -0.00707 549 CYS B CB  
3597 S SG  . CYS B 115 ? 0.11789 0.14271 0.11714 -0.02132 0.00232  -0.00698 549 CYS B SG  
3598 N N   . PHE B 116 ? 0.09674 0.11789 0.09454 -0.02398 0.00036  -0.01164 550 PHE B N   
3599 C CA  . PHE B 116 ? 0.10028 0.11996 0.09702 -0.02516 -0.00110 -0.01303 550 PHE B CA  
3600 C C   . PHE B 116 ? 0.13088 0.15120 0.12265 -0.02601 -0.00055 -0.01510 550 PHE B C   
3601 O O   . PHE B 116 ? 0.16419 0.18427 0.15269 -0.02693 -0.00200 -0.01472 550 PHE B O   
3602 C CB  . PHE B 116 ? 0.13460 0.15106 0.13355 -0.02454 -0.00172 -0.01496 550 PHE B CB  
3603 C CG  . PHE B 116 ? 0.10227 0.11639 0.10423 -0.02421 -0.00212 -0.01247 550 PHE B CG  
3604 C CD1 . PHE B 116 ? 0.10616 0.12271 0.10953 -0.02461 -0.00183 -0.00914 550 PHE B CD1 
3605 C CD2 . PHE B 116 ? 0.18160 0.19033 0.18399 -0.02330 -0.00287 -0.01353 550 PHE B CD2 
3606 C CE1 . PHE B 116 ? 0.11839 0.13309 0.12349 -0.02462 -0.00170 -0.00675 550 PHE B CE1 
3607 C CE2 . PHE B 116 ? 0.12458 0.12967 0.12790 -0.02338 -0.00307 -0.01068 550 PHE B CE2 
3608 C CZ  . PHE B 116 ? 0.18533 0.19392 0.18998 -0.02431 -0.00220 -0.00719 550 PHE B CZ  
3609 N N   . ASN B 117 ? 0.13901 0.16078 0.12994 -0.02558 0.00154  -0.01753 551 ASN B N   
3610 C CA  . ASN B 117 ? 0.11592 0.13894 0.10138 -0.02689 0.00298  -0.01949 551 ASN B CA  
3611 C C   . ASN B 117 ? 0.11715 0.13900 0.09707 -0.02862 0.00321  -0.01648 551 ASN B C   
3612 O O   . ASN B 117 ? 0.20417 0.22458 0.17756 -0.02969 0.00285  -0.01671 551 ASN B O   
3613 C CB  . ASN B 117 ? 0.11080 0.13792 0.09758 -0.02643 0.00587  -0.02265 551 ASN B CB  
3614 C CG  . ASN B 117 ? 0.13117 0.15868 0.11981 -0.02417 0.00536  -0.02712 551 ASN B CG  
3615 O OD1 . ASN B 117 ? 0.14505 0.16836 0.13386 -0.02348 0.00279  -0.02758 551 ASN B OD1 
3616 N ND2 . ASN B 117 ? 0.11354 0.14628 0.10373 -0.02301 0.00768  -0.03086 551 ASN B ND2 
3617 N N   . SER B 118 ? 0.10797 0.12944 0.08940 -0.02858 0.00346  -0.01371 552 SER B N   
3618 C CA  . SER B 118 ? 0.16815 0.18644 0.14341 -0.02978 0.00326  -0.01092 552 SER B CA  
3619 C C   . SER B 118 ? 0.18746 0.20342 0.16065 -0.02834 -0.00028 -0.00918 552 SER B C   
3620 O O   . SER B 118 ? 0.18873 0.20113 0.15427 -0.02865 -0.00141 -0.00801 552 SER B O   
3621 C CB  . SER B 118 ? 0.17669 0.19480 0.15420 -0.02987 0.00420  -0.00921 552 SER B CB  
3622 O OG  . SER B 118 ? 0.23421 0.25602 0.21417 -0.03136 0.00722  -0.01141 552 SER B OG  
3623 N N   . ALA B 119 ? 0.14804 0.16616 0.12765 -0.02678 -0.00210 -0.00908 553 ALA B N   
3624 C CA  . ALA B 119 ? 0.12413 0.14275 0.10356 -0.02559 -0.00539 -0.00838 553 ALA B CA  
3625 C C   . ALA B 119 ? 0.16388 0.18237 0.13991 -0.02625 -0.00695 -0.01065 553 ALA B C   
3626 O O   . ALA B 119 ? 0.11893 0.13687 0.09077 -0.02521 -0.00981 -0.01035 553 ALA B O   
3627 C CB  . ALA B 119 ? 0.10353 0.12574 0.09104 -0.02493 -0.00611 -0.00797 553 ALA B CB  
3628 N N   . GLN B 120 ? 0.18210 0.20103 0.15955 -0.02740 -0.00553 -0.01334 554 GLN B N   
3629 C CA  . GLN B 120 ? 0.22680 0.24528 0.20011 -0.02790 -0.00688 -0.01614 554 GLN B CA  
3630 C C   . GLN B 120 ? 0.21211 0.22797 0.17518 -0.02820 -0.00626 -0.01549 554 GLN B C   
3631 O O   . GLN B 120 ? 0.24090 0.25568 0.19825 -0.02760 -0.00898 -0.01607 554 GLN B O   
3632 C CB  . GLN B 120 ? 0.18211 0.20079 0.15829 -0.02837 -0.00536 -0.01958 554 GLN B CB  
3633 C CG  . GLN B 120 ? 0.19078 0.20888 0.16312 -0.02862 -0.00700 -0.02330 554 GLN B CG  
3634 C CD  . GLN B 120 ? 0.20097 0.21822 0.17638 -0.02824 -0.00615 -0.02717 554 GLN B CD  
3635 O OE1 . GLN B 120 ? 0.20349 0.22142 0.18071 -0.02737 -0.00341 -0.02779 554 GLN B OE1 
3636 N NE2 . GLN B 120 ? 0.31847 0.33409 0.29454 -0.02862 -0.00894 -0.03020 554 GLN B NE2 
3637 N N   . ALA B 121 ? 0.24898 0.26365 0.20914 -0.02938 -0.00276 -0.01429 555 ALA B N   
3638 C CA  . ALA B 121 ? 0.22995 0.24092 0.17919 -0.03079 -0.00149 -0.01301 555 ALA B CA  
3639 C C   . ALA B 121 ? 0.19027 0.19637 0.13323 -0.02919 -0.00506 -0.00982 555 ALA B C   
3640 O O   . ALA B 121 ? 0.26087 0.26308 0.19367 -0.02899 -0.00655 -0.00934 555 ALA B O   
3641 C CB  . ALA B 121 ? 0.15205 0.16319 0.10076 -0.03333 0.00301  -0.01217 555 ALA B CB  
3642 N N   . ILE B 122 ? 0.19437 0.20059 0.14267 -0.02745 -0.00673 -0.00786 556 ILE B N   
3643 C CA  . ILE B 122 ? 0.14260 0.14476 0.08569 -0.02472 -0.01062 -0.00549 556 ILE B CA  
3644 C C   . ILE B 122 ? 0.18862 0.19381 0.13199 -0.02233 -0.01510 -0.00743 556 ILE B C   
3645 O O   . ILE B 122 ? 0.18172 0.18268 0.11550 -0.02055 -0.01816 -0.00676 556 ILE B O   
3646 C CB  . ILE B 122 ? 0.15190 0.15504 0.10156 -0.02294 -0.01116 -0.00385 556 ILE B CB  
3647 C CG1 . ILE B 122 ? 0.13538 0.13525 0.08411 -0.02541 -0.00732 -0.00234 556 ILE B CG1 
3648 C CG2 . ILE B 122 ? 0.14168 0.14166 0.08684 -0.01890 -0.01574 -0.00232 556 ILE B CG2 
3649 C CD1 . ILE B 122 ? 0.12879 0.13009 0.08412 -0.02367 -0.00760 -0.00136 556 ILE B CD1 
3650 N N   . LEU B 123 ? 0.21835 0.23050 0.17221 -0.02247 -0.01573 -0.00992 557 LEU B N   
3651 C CA  . LEU B 123 ? 0.21839 0.23503 0.17482 -0.02087 -0.02014 -0.01223 557 LEU B CA  
3652 C C   . LEU B 123 ? 0.18043 0.19569 0.12978 -0.02149 -0.02145 -0.01478 557 LEU B C   
3653 O O   . LEU B 123 ? 0.18459 0.20241 0.13289 -0.01963 -0.02599 -0.01665 557 LEU B O   
3654 C CB  . LEU B 123 ? 0.12865 0.15214 0.09777 -0.02226 -0.01984 -0.01400 557 LEU B CB  
3655 C CG  . LEU B 123 ? 0.12132 0.14769 0.09767 -0.02146 -0.01877 -0.01187 557 LEU B CG  
3656 C CD1 . LEU B 123 ? 0.11485 0.14613 0.10144 -0.02397 -0.01757 -0.01318 557 LEU B CD1 
3657 C CD2 . LEU B 123 ? 0.12345 0.15259 0.09925 -0.01769 -0.02259 -0.01120 557 LEU B CD2 
3658 N N   . THR B 124 ? 0.15698 0.16931 0.10170 -0.02380 -0.01772 -0.01544 558 THR B N   
3659 C CA  . THR B 124 ? 0.17361 0.18481 0.11058 -0.02417 -0.01853 -0.01816 558 THR B CA  
3660 C C   . THR B 124 ? 0.20811 0.21259 0.13015 -0.02375 -0.01817 -0.01565 558 THR B C   
3661 O O   . THR B 124 ? 0.28639 0.28950 0.19978 -0.02392 -0.01861 -0.01756 558 THR B O   
3662 C CB  . THR B 124 ? 0.19952 0.21246 0.13997 -0.02647 -0.01477 -0.02134 558 THR B CB  
3663 O OG1 . THR B 124 ? 0.16749 0.17894 0.10669 -0.02810 -0.00969 -0.01948 558 THR B OG1 
3664 C CG2 . THR B 124 ? 0.17065 0.18756 0.12364 -0.02700 -0.01565 -0.02354 558 THR B CG2 
3665 N N   . GLY B 125 ? 0.17065 0.17003 0.08853 -0.02338 -0.01740 -0.01143 559 GLY B N   
3666 C CA  . GLY B 125 ? 0.18464 0.17519 0.08690 -0.02322 -0.01763 -0.00827 559 GLY B CA  
3667 C C   . GLY B 125 ? 0.25397 0.24071 0.14935 -0.02772 -0.01141 -0.00670 559 GLY B C   
3668 O O   . GLY B 125 ? 0.25898 0.23714 0.13995 -0.02875 -0.01089 -0.00358 559 GLY B O   
3669 N N   . GLN B 126 ? 0.26817 0.26103 0.17307 -0.03050 -0.00674 -0.00884 560 GLN B N   
3670 C CA  . GLN B 126 ? 0.18980 0.18197 0.08999 -0.03498 -0.00059 -0.00836 560 GLN B CA  
3671 C C   . GLN B 126 ? 0.18975 0.17524 0.08610 -0.03723 0.00117  -0.00389 560 GLN B C   
3672 O O   . GLN B 126 ? 0.23497 0.21536 0.12071 -0.04131 0.00485  -0.00176 560 GLN B O   
3673 C CB  . GLN B 126 ? 0.21247 0.21376 0.12489 -0.03612 0.00299  -0.01247 560 GLN B CB  
3674 C CG  . GLN B 126 ? 0.33055 0.33687 0.24811 -0.03369 0.00059  -0.01712 560 GLN B CG  
3675 C CD  . GLN B 126 ? 0.45723 0.47020 0.38695 -0.03364 0.00292  -0.02077 560 GLN B CD  
3676 O OE1 . GLN B 126 ? 0.51134 0.52708 0.44444 -0.03552 0.00709  -0.02074 560 GLN B OE1 
3677 N NE2 . GLN B 126 ? 0.33995 0.35508 0.27606 -0.03147 -0.00011 -0.02407 560 GLN B NE2 
3678 N N   . VAL B 127 ? 0.19047 0.17579 0.09507 -0.03503 -0.00118 -0.00260 561 VAL B N   
3679 C CA  . VAL B 127 ? 0.18234 0.16039 0.08356 -0.03637 -0.00059 0.00115  561 VAL B CA  
3680 C C   . VAL B 127 ? 0.22434 0.19820 0.12578 -0.03108 -0.00659 0.00291  561 VAL B C   
3681 O O   . VAL B 127 ? 0.21346 0.19350 0.12256 -0.02722 -0.01013 0.00077  561 VAL B O   
3682 C CB  . VAL B 127 ? 0.17156 0.15526 0.08394 -0.03898 0.00336  0.00008  561 VAL B CB  
3683 C CG1 . VAL B 127 ? 0.17137 0.16143 0.08491 -0.04349 0.00910  -0.00258 561 VAL B CG1 
3684 C CG2 . VAL B 127 ? 0.15703 0.14820 0.08348 -0.03517 0.00103  -0.00202 561 VAL B CG2 
3685 N N   . ARG B 128 ? 0.23440 0.19768 0.12722 -0.03107 -0.00770 0.00655  562 ARG B N   
3686 C CA  . ARG B 128 ? 0.22441 0.18368 0.11722 -0.02530 -0.01339 0.00779  562 ARG B CA  
3687 C C   . ARG B 128 ? 0.24706 0.21333 0.15415 -0.02388 -0.01307 0.00648  562 ARG B C   
3688 O O   . ARG B 128 ? 0.24941 0.22239 0.16485 -0.01939 -0.01645 0.00481  562 ARG B O   
3689 C CB  . ARG B 128 ? 0.24409 0.18745 0.12114 -0.02527 -0.01512 0.01198  562 ARG B CB  
3690 N N   . ASN B 129 ? 0.20538 0.17082 0.11527 -0.02792 -0.00893 0.00703  563 ASN B N   
3691 C CA  . ASN B 129 ? 0.32442 0.29561 0.24615 -0.02680 -0.00838 0.00592  563 ASN B CA  
3692 C C   . ASN B 129 ? 0.25687 0.23335 0.18456 -0.03204 -0.00292 0.00450  563 ASN B C   
3693 O O   . ASN B 129 ? 0.19933 0.17513 0.12196 -0.03652 0.00052  0.00433  563 ASN B O   
3694 C CB  . ASN B 129 ? 0.23866 0.20067 0.15566 -0.02425 -0.01114 0.00801  563 ASN B CB  
3695 C CG  . ASN B 129 ? 0.22760 0.17567 0.13057 -0.02827 -0.01000 0.01099  563 ASN B CG  
3696 O OD1 . ASN B 129 ? 0.24367 0.19177 0.14473 -0.03468 -0.00519 0.01113  563 ASN B OD1 
3697 N ND2 . ASN B 129 ? 0.19935 0.13529 0.09215 -0.02456 -0.01443 0.01325  563 ASN B ND2 
3698 N N   . ALA B 130 ? 0.23527 0.21774 0.17355 -0.03121 -0.00215 0.00318  564 ALA B N   
3699 C CA  . ALA B 130 ? 0.17794 0.16705 0.12305 -0.03493 0.00218  0.00110  564 ALA B CA  
3700 C C   . ALA B 130 ? 0.27618 0.26746 0.22857 -0.03395 0.00218  0.00063  564 ALA B C   
3701 O O   . ALA B 130 ? 0.13746 0.12713 0.09134 -0.02994 -0.00088 0.00151  564 ALA B O   
3702 C CB  . ALA B 130 ? 0.13196 0.13018 0.08422 -0.03417 0.00317  -0.00167 564 ALA B CB  
3703 N N   . VAL B 131 ? 0.16399 0.16004 0.12105 -0.03737 0.00559  -0.00126 565 VAL B N   
3704 C CA  . VAL B 131 ? 0.17359 0.17257 0.13741 -0.03672 0.00566  -0.00233 565 VAL B CA  
3705 C C   . VAL B 131 ? 0.17216 0.18152 0.14521 -0.03697 0.00793  -0.00557 565 VAL B C   
3706 O O   . VAL B 131 ? 0.11725 0.13062 0.09039 -0.04024 0.01092  -0.00748 565 VAL B O   
3707 C CB  . VAL B 131 ? 0.14970 0.14186 0.10825 -0.04089 0.00662  -0.00158 565 VAL B CB  
3708 C CG1 . VAL B 131 ? 0.19855 0.19106 0.15301 -0.04753 0.01075  -0.00222 565 VAL B CG1 
3709 C CG2 . VAL B 131 ? 0.16400 0.16028 0.12990 -0.04014 0.00641  -0.00348 565 VAL B CG2 
3710 N N   . ALA B 132 ? 0.15244 0.16605 0.13264 -0.03315 0.00645  -0.00631 566 ALA B N   
3711 C CA  . ALA B 132 ? 0.10094 0.12261 0.08891 -0.03183 0.00747  -0.00909 566 ALA B CA  
3712 C C   . ALA B 132 ? 0.11912 0.14385 0.11167 -0.03136 0.00735  -0.01055 566 ALA B C   
3713 O O   . ALA B 132 ? 0.11333 0.13611 0.10655 -0.02849 0.00527  -0.00924 566 ALA B O   
3714 C CB  . ALA B 132 ? 0.09616 0.11900 0.08719 -0.02787 0.00563  -0.00845 566 ALA B CB  
3715 N N   . ILE B 133 ? 0.11098 0.14153 0.10686 -0.03401 0.00954  -0.01369 567 ILE B N   
3716 C CA  . ILE B 133 ? 0.10924 0.14438 0.11025 -0.03366 0.00914  -0.01605 567 ILE B CA  
3717 C C   . ILE B 133 ? 0.12330 0.16525 0.13081 -0.02904 0.00823  -0.01843 567 ILE B C   
3718 O O   . ILE B 133 ? 0.12544 0.17456 0.13700 -0.02940 0.00971  -0.02199 567 ILE B O   
3719 C CB  . ILE B 133 ? 0.17300 0.21149 0.17441 -0.03966 0.01187  -0.01856 567 ILE B CB  
3720 C CG1 . ILE B 133 ? 0.16056 0.18912 0.15291 -0.04444 0.01272  -0.01539 567 ILE B CG1 
3721 C CG2 . ILE B 133 ? 0.14247 0.18582 0.14942 -0.03937 0.01074  -0.02138 567 ILE B CG2 
3722 C CD1 . ILE B 133 ? 0.13865 0.16932 0.12919 -0.05196 0.01659  -0.01700 567 ILE B CD1 
3723 N N   . VAL B 134 ? 0.09405 0.13346 0.10197 -0.02448 0.00574  -0.01651 568 VAL B N   
3724 C CA  . VAL B 134 ? 0.08496 0.12704 0.09635 -0.01994 0.00447  -0.01749 568 VAL B CA  
3725 C C   . VAL B 134 ? 0.14554 0.18829 0.15852 -0.01624 0.00223  -0.01738 568 VAL B C   
3726 O O   . VAL B 134 ? 0.13951 0.17939 0.15027 -0.01642 0.00143  -0.01564 568 VAL B O   
3727 C CB  . VAL B 134 ? 0.09874 0.13589 0.10754 -0.01862 0.00396  -0.01468 568 VAL B CB  
3728 C CG1 . VAL B 134 ? 0.11465 0.15196 0.12187 -0.02135 0.00572  -0.01572 568 VAL B CG1 
3729 C CG2 . VAL B 134 ? 0.08486 0.11697 0.09017 -0.01863 0.00303  -0.01089 568 VAL B CG2 
3730 N N   . ARG B 135 ? 0.11250 0.15862 0.12858 -0.01230 0.00091  -0.01947 569 ARG B N   
3731 C CA  . ARG B 135 ? 0.14582 0.19148 0.16179 -0.00776 -0.00160 -0.01894 569 ARG B CA  
3732 C C   . ARG B 135 ? 0.09602 0.14023 0.11210 -0.00339 -0.00303 -0.01925 569 ARG B C   
3733 O O   . ARG B 135 ? 0.11434 0.16053 0.13245 -0.00346 -0.00235 -0.02171 569 ARG B O   
3734 C CB  . ARG B 135 ? 0.10712 0.15929 0.12664 -0.00741 -0.00268 -0.02273 569 ARG B CB  
3735 C CG  . ARG B 135 ? 0.10730 0.16813 0.13263 -0.00678 -0.00259 -0.02804 569 ARG B CG  
3736 C CD  . ARG B 135 ? 0.12621 0.19493 0.15604 -0.00695 -0.00387 -0.03229 569 ARG B CD  
3737 N NE  . ARG B 135 ? 0.12262 0.19020 0.15101 -0.00109 -0.00753 -0.03197 569 ARG B NE  
3738 C CZ  . ARG B 135 ? 0.09013 0.16145 0.12052 0.00490  -0.01039 -0.03469 569 ARG B CZ  
3739 N NH1 . ARG B 135 ? 0.08781 0.16516 0.12276 0.00632  -0.01015 -0.03854 569 ARG B NH1 
3740 N NH2 . ARG B 135 ? 0.09068 0.15944 0.11775 0.01010  -0.01377 -0.03368 569 ARG B NH2 
3741 N N   . PRO B 136 ? 0.12095 0.16074 0.13385 0.00048  -0.00501 -0.01672 570 PRO B N   
3742 C CA  . PRO B 136 ? 0.13342 0.17076 0.14290 0.00129  -0.00564 -0.01368 570 PRO B CA  
3743 C C   . PRO B 136 ? 0.10404 0.13754 0.11089 -0.00201 -0.00375 -0.00979 570 PRO B C   
3744 O O   . PRO B 136 ? 0.12181 0.15322 0.12875 -0.00441 -0.00246 -0.00883 570 PRO B O   
3745 C CB  . PRO B 136 ? 0.09502 0.12801 0.10080 0.00628  -0.00784 -0.01202 570 PRO B CB  
3746 C CG  . PRO B 136 ? 0.10000 0.12908 0.10574 0.00660  -0.00777 -0.01212 570 PRO B CG  
3747 C CD  . PRO B 136 ? 0.09387 0.12980 0.10529 0.00476  -0.00683 -0.01680 570 PRO B CD  
3748 N N   . PRO B 137 ? 0.08736 0.12049 0.09194 -0.00182 -0.00379 -0.00802 571 PRO B N   
3749 C CA  . PRO B 137 ? 0.08641 0.11733 0.08905 -0.00382 -0.00240 -0.00496 571 PRO B CA  
3750 C C   . PRO B 137 ? 0.12850 0.15627 0.12915 -0.00370 -0.00166 -0.00157 571 PRO B C   
3751 O O   . PRO B 137 ? 0.09898 0.12412 0.09857 -0.00202 -0.00237 -0.00120 571 PRO B O   
3752 C CB  . PRO B 137 ? 0.14026 0.17233 0.14099 -0.00220 -0.00311 -0.00499 571 PRO B CB  
3753 C CG  . PRO B 137 ? 0.14839 0.18161 0.14822 0.00146  -0.00486 -0.00617 571 PRO B CG  
3754 C CD  . PRO B 137 ? 0.08856 0.12395 0.09231 0.00082  -0.00545 -0.00941 571 PRO B CD  
3755 N N   . GLY B 138 ? 0.13297 0.16096 0.13304 -0.00546 -0.00043 0.00064  572 GLY B N   
3756 C CA  . GLY B 138 ? 0.09040 0.11650 0.08949 -0.00678 0.00069  0.00357  572 GLY B CA  
3757 C C   . GLY B 138 ? 0.10308 0.13202 0.10107 -0.00706 0.00207  0.00593  572 GLY B C   
3758 O O   . GLY B 138 ? 0.10862 0.13596 0.10488 -0.00816 0.00328  0.00854  572 GLY B O   
3759 N N   . HIS B 139 ? 0.13406 0.16682 0.13272 -0.00619 0.00197  0.00496  573 HIS B N   
3760 C CA  . HIS B 139 ? 0.13536 0.17301 0.13416 -0.00600 0.00330  0.00622  573 HIS B CA  
3761 C C   . HIS B 139 ? 0.16783 0.20682 0.16353 -0.00512 0.00503  0.00863  573 HIS B C   
3762 O O   . HIS B 139 ? 0.10472 0.14835 0.10141 -0.00671 0.00706  0.01005  573 HIS B O   
3763 C CB  . HIS B 139 ? 0.12096 0.16100 0.11980 -0.00363 0.00208  0.00411  573 HIS B CB  
3764 C CG  . HIS B 139 ? 0.12307 0.16199 0.11915 -0.00042 0.00088  0.00258  573 HIS B CG  
3765 N ND1 . HIS B 139 ? 0.08935 0.13011 0.08419 0.00241  -0.00002 0.00100  573 HIS B ND1 
3766 C CD2 . HIS B 139 ? 0.08951 0.12594 0.08397 0.00070  -0.00003 0.00181  573 HIS B CD2 
3767 C CE1 . HIS B 139 ? 0.09121 0.13009 0.08357 0.00461  -0.00130 -0.00060 573 HIS B CE1 
3768 N NE2 . HIS B 139 ? 0.18950 0.22638 0.18196 0.00353  -0.00136 -0.00022 573 HIS B NE2 
3769 N N   . HIS B 140 ? 0.12491 0.16047 0.11682 -0.00271 0.00420  0.00886  574 HIS B N   
3770 C CA  . HIS B 140 ? 0.10535 0.14057 0.09210 -0.00166 0.00572  0.01162  574 HIS B CA  
3771 C C   . HIS B 140 ? 0.11403 0.14343 0.09843 -0.00472 0.00688  0.01492  574 HIS B C   
3772 O O   . HIS B 140 ? 0.18805 0.21605 0.16716 -0.00505 0.00867  0.01802  574 HIS B O   
3773 C CB  . HIS B 140 ? 0.10546 0.13910 0.08804 0.00286  0.00369  0.01032  574 HIS B CB  
3774 C CG  . HIS B 140 ? 0.14285 0.18054 0.12659 0.00558  0.00237  0.00702  574 HIS B CG  
3775 N ND1 . HIS B 140 ? 0.15389 0.19706 0.13756 0.00657  0.00374  0.00665  574 HIS B ND1 
3776 C CD2 . HIS B 140 ? 0.12631 0.16305 0.11108 0.00745  -0.00028 0.00368  574 HIS B CD2 
3777 C CE1 . HIS B 140 ? 0.11484 0.15853 0.09868 0.00931  0.00157  0.00328  574 HIS B CE1 
3778 N NE2 . HIS B 140 ? 0.12235 0.16206 0.10691 0.00930  -0.00073 0.00159  574 HIS B NE2 
3779 N N   . ALA B 141 ? 0.11275 0.13816 0.10010 -0.00695 0.00589  0.01425  575 ALA B N   
3780 C CA  . ALA B 141 ? 0.11507 0.13275 0.09932 -0.00938 0.00629  0.01691  575 ALA B CA  
3781 C C   . ALA B 141 ? 0.11760 0.13750 0.10309 -0.01483 0.00935  0.01942  575 ALA B C   
3782 O O   . ALA B 141 ? 0.16087 0.18707 0.15236 -0.01722 0.00994  0.01776  575 ALA B O   
3783 C CB  . ALA B 141 ? 0.11811 0.13107 0.10501 -0.00943 0.00404  0.01456  575 ALA B CB  
3784 N N   . GLU B 142 ? 0.16142 0.17601 0.14091 -0.01697 0.01117  0.02334  576 GLU B N   
3785 C CA  . GLU B 142 ? 0.16893 0.18590 0.14926 -0.02328 0.01466  0.02592  576 GLU B CA  
3786 C C   . GLU B 142 ? 0.22718 0.23485 0.20745 -0.02782 0.01397  0.02679  576 GLU B C   
3787 O O   . GLU B 142 ? 0.23475 0.23405 0.21368 -0.02528 0.01084  0.02541  576 GLU B O   
3788 C CB  . GLU B 142 ? 0.14247 0.15856 0.11510 -0.02411 0.01772  0.03006  576 GLU B CB  
3789 C CG  . GLU B 142 ? 0.14101 0.16559 0.11251 -0.01911 0.01821  0.02886  576 GLU B CG  
3790 C CD  . GLU B 142 ? 0.15577 0.19463 0.13362 -0.02100 0.02123  0.02731  576 GLU B CD  
3791 O OE1 . GLU B 142 ? 0.15856 0.20238 0.14388 -0.02497 0.02176  0.02586  576 GLU B OE1 
3792 O OE2 . GLU B 142 ? 0.23411 0.27963 0.20937 -0.01803 0.02280  0.02713  576 GLU B OE2 
3793 N N   . LYS B 143 ? 0.14823 0.15786 0.13010 -0.03472 0.01696  0.02870  577 LYS B N   
3794 C CA  . LYS B 143 ? 0.20389 0.20411 0.18551 -0.03987 0.01629  0.02930  577 LYS B CA  
3795 C C   . LYS B 143 ? 0.23973 0.22287 0.21111 -0.03830 0.01456  0.03230  577 LYS B C   
3796 O O   . LYS B 143 ? 0.18739 0.16048 0.15791 -0.03823 0.01175  0.03100  577 LYS B O   
3797 C CB  . LYS B 143 ? 0.15484 0.16073 0.13968 -0.04841 0.02015  0.03094  577 LYS B CB  
3798 C CG  . LYS B 143 ? 0.16804 0.16304 0.15189 -0.05493 0.01957  0.03169  577 LYS B CG  
3799 C CD  . LYS B 143 ? 0.20047 0.20463 0.19043 -0.06404 0.02317  0.03190  577 LYS B CD  
3800 C CE  . LYS B 143 ? 0.20822 0.20177 0.19006 -0.07168 0.02655  0.03725  577 LYS B CE  
3801 N NZ  . LYS B 143 ? 0.32903 0.30071 0.30157 -0.07110 0.02331  0.03913  577 LYS B NZ  
3802 N N   . ASP B 144 ? 0.20669 0.18597 0.16951 -0.03627 0.01581  0.03602  578 ASP B N   
3803 C CA  . ASP B 144 ? 0.23802 0.19974 0.18945 -0.03469 0.01390  0.03942  578 ASP B CA  
3804 C C   . ASP B 144 ? 0.26698 0.22672 0.21177 -0.02637 0.01165  0.03980  578 ASP B C   
3805 O O   . ASP B 144 ? 0.33454 0.28140 0.26776 -0.02470 0.01074  0.04370  578 ASP B O   
3806 C CB  . ASP B 144 ? 0.22618 0.17979 0.16998 -0.04263 0.01769  0.04510  578 ASP B CB  
3807 N N   . THR B 145 ? 0.17470 0.14613 0.12615 -0.02117 0.01034  0.03566  579 THR B N   
3808 C CA  . THR B 145 ? 0.22375 0.19410 0.16980 -0.01349 0.00772  0.03519  579 THR B CA  
3809 C C   . THR B 145 ? 0.18773 0.16838 0.14219 -0.00857 0.00536  0.02963  579 THR B C   
3810 O O   . THR B 145 ? 0.20039 0.19103 0.16354 -0.01104 0.00679  0.02711  579 THR B O   
3811 C CB  . THR B 145 ? 0.22059 0.19337 0.15902 -0.01369 0.01077  0.03909  579 THR B CB  
3812 O OG1 . THR B 145 ? 0.30247 0.26503 0.23031 -0.00758 0.00749  0.04072  579 THR B OG1 
3813 C CG2 . THR B 145 ? 0.17127 0.15992 0.11619 -0.01193 0.01237  0.03618  579 THR B CG2 
3814 N N   . ALA B 146 ? 0.22353 0.20113 0.17473 -0.00183 0.00162  0.02785  580 ALA B N   
3815 C CA  . ALA B 146 ? 0.18960 0.17675 0.14776 0.00237  -0.00045 0.02271  580 ALA B CA  
3816 C C   . ALA B 146 ? 0.14943 0.14357 0.10514 0.00494  0.00034  0.02290  580 ALA B C   
3817 O O   . ALA B 146 ? 0.15853 0.14880 0.10541 0.00558  0.00143  0.02669  580 ALA B O   
3818 C CB  . ALA B 146 ? 0.26918 0.25182 0.22693 0.00814  -0.00505 0.01947  580 ALA B CB  
3819 N N   . CYS B 147 ? 0.14371 0.14743 0.10646 0.00634  -0.00027 0.01869  581 CYS B N   
3820 C CA  . CYS B 147 ? 0.13451 0.14528 0.09597 0.00837  0.00049  0.01803  581 CYS B CA  
3821 C C   . CYS B 147 ? 0.16099 0.17875 0.12975 0.01008  -0.00144 0.01279  581 CYS B C   
3822 O O   . CYS B 147 ? 0.11657 0.13613 0.09212 0.00748  -0.00132 0.01078  581 CYS B O   
3823 C CB  . CYS B 147 ? 0.13411 0.14981 0.09574 0.00414  0.00492  0.02065  581 CYS B CB  
3824 S SG  . CYS B 147 ? 0.20424 0.22872 0.16329 0.00735  0.00611  0.01950  581 CYS B SG  
3825 N N   . GLY B 148 ? 0.14020 0.16121 0.10674 0.01415  -0.00324 0.01064  582 GLY B N   
3826 C CA  . GLY B 148 ? 0.20040 0.22724 0.17264 0.01499  -0.00478 0.00592  582 GLY B CA  
3827 C C   . GLY B 148 ? 0.13424 0.16162 0.11358 0.01340  -0.00622 0.00263  582 GLY B C   
3828 O O   . GLY B 148 ? 0.13622 0.16621 0.12058 0.01035  -0.00514 0.00122  582 GLY B O   
3829 N N   . PHE B 149 ? 0.14121 0.16620 0.12043 0.01573  -0.00869 0.00133  583 PHE B N   
3830 C CA  . PHE B 149 ? 0.12817 0.15508 0.11387 0.01491  -0.01001 -0.00240 583 PHE B CA  
3831 C C   . PHE B 149 ? 0.15083 0.17521 0.13943 0.01084  -0.00781 -0.00092 583 PHE B C   
3832 O O   . PHE B 149 ? 0.13432 0.16064 0.12791 0.00976  -0.00824 -0.00394 583 PHE B O   
3833 C CB  . PHE B 149 ? 0.16661 0.19985 0.15781 0.01361  -0.01066 -0.00690 583 PHE B CB  
3834 C CG  . PHE B 149 ? 0.19211 0.22805 0.18075 0.01675  -0.01273 -0.00882 583 PHE B CG  
3835 C CD1 . PHE B 149 ? 0.17464 0.20883 0.15714 0.02169  -0.01485 -0.00779 583 PHE B CD1 
3836 C CD2 . PHE B 149 ? 0.17435 0.21351 0.16579 0.01481  -0.01285 -0.01176 583 PHE B CD2 
3837 C CE1 . PHE B 149 ? 0.18116 0.21805 0.16080 0.02480  -0.01701 -0.00997 583 PHE B CE1 
3838 C CE2 . PHE B 149 ? 0.10984 0.15099 0.09881 0.01762  -0.01506 -0.01410 583 PHE B CE2 
3839 C CZ  . PHE B 149 ? 0.12375 0.16444 0.10709 0.02273  -0.01715 -0.01341 583 PHE B CZ  
3840 N N   . CYS B 150 ? 0.15946 0.18036 0.14519 0.00838  -0.00541 0.00325  584 CYS B N   
3841 C CA  . CYS B 150 ? 0.10992 0.12862 0.09822 0.00434  -0.00365 0.00443  584 CYS B CA  
3842 C C   . CYS B 150 ? 0.11602 0.12663 0.09979 0.00465  -0.00393 0.00728  584 CYS B C   
3843 O O   . CYS B 150 ? 0.12218 0.12861 0.09947 0.00591  -0.00371 0.01064  584 CYS B O   
3844 C CB  . CYS B 150 ? 0.10241 0.12402 0.09180 0.00082  -0.00100 0.00638  584 CYS B CB  
3845 S SG  . CYS B 150 ? 0.13623 0.16424 0.12827 0.00130  -0.00116 0.00368  584 CYS B SG  
3846 N N   . PHE B 151 ? 0.13667 0.14428 0.12295 0.00339  -0.00440 0.00595  585 PHE B N   
3847 C CA  . PHE B 151 ? 0.17717 0.17517 0.15903 0.00323  -0.00498 0.00824  585 PHE B CA  
3848 C C   . PHE B 151 ? 0.17537 0.17135 0.15882 -0.00253 -0.00266 0.01009  585 PHE B C   
3849 O O   . PHE B 151 ? 0.13169 0.12102 0.11049 -0.00506 -0.00155 0.01393  585 PHE B O   
3850 C CB  . PHE B 151 ? 0.12655 0.12191 0.10950 0.00727  -0.00803 0.00444  585 PHE B CB  
3851 C CG  . PHE B 151 ? 0.13657 0.13378 0.11785 0.01347  -0.01106 0.00230  585 PHE B CG  
3852 C CD1 . PHE B 151 ? 0.16884 0.17631 0.15610 0.01471  -0.01159 -0.00204 585 PHE B CD1 
3853 C CD2 . PHE B 151 ? 0.18781 0.17606 0.16104 0.01791  -0.01361 0.00453  585 PHE B CD2 
3854 C CE1 . PHE B 151 ? 0.14374 0.15429 0.13042 0.02021  -0.01473 -0.00474 585 PHE B CE1 
3855 C CE2 . PHE B 151 ? 0.22539 0.21598 0.19698 0.02433  -0.01710 0.00210  585 PHE B CE2 
3856 C CZ  . PHE B 151 ? 0.13947 0.14212 0.11850 0.02545  -0.01772 -0.00286 585 PHE B CZ  
3857 N N   . PHE B 152 ? 0.14520 0.14666 0.13473 -0.00496 -0.00197 0.00738  586 PHE B N   
3858 C CA  . PHE B 152 ? 0.11388 0.11558 0.10568 -0.01013 -0.00022 0.00840  586 PHE B CA  
3859 C C   . PHE B 152 ? 0.15260 0.16337 0.14876 -0.01166 0.00106  0.00736  586 PHE B C   
3860 O O   . PHE B 152 ? 0.12146 0.13651 0.11950 -0.00955 0.00039  0.00487  586 PHE B O   
3861 C CB  . PHE B 152 ? 0.11574 0.11322 0.10904 -0.01103 -0.00140 0.00585  586 PHE B CB  
3862 C CG  . PHE B 152 ? 0.12628 0.11350 0.11483 -0.00830 -0.00349 0.00603  586 PHE B CG  
3863 C CD1 . PHE B 152 ? 0.13693 0.11498 0.11966 -0.01010 -0.00320 0.01016  586 PHE B CD1 
3864 C CD2 . PHE B 152 ? 0.12687 0.11344 0.11639 -0.00393 -0.00576 0.00193  586 PHE B CD2 
3865 C CE1 . PHE B 152 ? 0.19709 0.16318 0.17382 -0.00713 -0.00570 0.01057  586 PHE B CE1 
3866 C CE2 . PHE B 152 ? 0.13789 0.11447 0.12264 -0.00022 -0.00838 0.00161  586 PHE B CE2 
3867 C CZ  . PHE B 152 ? 0.14964 0.11481 0.12739 -0.00161 -0.00863 0.00610  586 PHE B CZ  
3868 N N   . ASN B 153 ? 0.11908 0.13263 0.11665 -0.01535 0.00275  0.00914  587 ASN B N   
3869 C CA  . ASN B 153 ? 0.13425 0.15565 0.13506 -0.01578 0.00339  0.00822  587 ASN B CA  
3870 C C   . ASN B 153 ? 0.16265 0.18500 0.16628 -0.01708 0.00244  0.00553  587 ASN B C   
3871 O O   . ASN B 153 ? 0.12330 0.14622 0.12879 -0.02014 0.00255  0.00540  587 ASN B O   
3872 C CB  . ASN B 153 ? 0.09805 0.12402 0.09987 -0.01841 0.00534  0.01043  587 ASN B CB  
3873 C CG  . ASN B 153 ? 0.11871 0.15253 0.12267 -0.01671 0.00547  0.00933  587 ASN B CG  
3874 O OD1 . ASN B 153 ? 0.12394 0.15910 0.12952 -0.01586 0.00405  0.00711  587 ASN B OD1 
3875 N ND2 . ASN B 153 ? 0.09411 0.13250 0.09718 -0.01595 0.00712  0.01083  587 ASN B ND2 
3876 N N   . THR B 154 ? 0.24279 0.26572 0.24646 -0.01500 0.00156  0.00323  588 THR B N   
3877 C CA  . THR B 154 ? 0.10531 0.12839 0.11004 -0.01626 0.00104  0.00080  588 THR B CA  
3878 C C   . THR B 154 ? 0.14407 0.17028 0.14967 -0.01803 0.00092  0.00101  588 THR B C   
3879 O O   . THR B 154 ? 0.10676 0.13237 0.11280 -0.02000 0.00043  -0.00004 588 THR B O   
3880 C CB  . THR B 154 ? 0.08629 0.11048 0.09074 -0.01463 0.00081  -0.00140 588 THR B CB  
3881 O OG1 . THR B 154 ? 0.08826 0.11090 0.09273 -0.01236 0.00032  -0.00249 588 THR B OG1 
3882 C CG2 . THR B 154 ? 0.08574 0.11030 0.09006 -0.01652 0.00096  -0.00351 588 THR B CG2 
3883 N N   . ALA B 155 ? 0.13478 0.16438 0.14031 -0.01675 0.00096  0.00195  589 ALA B N   
3884 C CA  . ALA B 155 ? 0.17005 0.20274 0.17608 -0.01710 0.00009  0.00167  589 ALA B CA  
3885 C C   . ALA B 155 ? 0.12515 0.16148 0.13429 -0.01929 0.00034  0.00234  589 ALA B C   
3886 O O   . ALA B 155 ? 0.08534 0.12372 0.09553 -0.02035 -0.00093 0.00124  589 ALA B O   
3887 C CB  . ALA B 155 ? 0.23049 0.26529 0.23531 -0.01420 -0.00038 0.00186  589 ALA B CB  
3888 N N   . ALA B 156 ? 0.09036 0.12758 0.10065 -0.02028 0.00192  0.00408  590 ALA B N   
3889 C CA  . ALA B 156 ? 0.11050 0.15133 0.12404 -0.02376 0.00268  0.00471  590 ALA B CA  
3890 C C   . ALA B 156 ? 0.22193 0.25785 0.23575 -0.02699 0.00191  0.00374  590 ALA B C   
3891 O O   . ALA B 156 ? 0.14055 0.17986 0.15737 -0.02973 0.00115  0.00256  590 ALA B O   
3892 C CB  . ALA B 156 ? 0.12894 0.17066 0.14205 -0.02479 0.00510  0.00732  590 ALA B CB  
3893 N N   . LEU B 157 ? 0.11247 0.14088 0.12336 -0.02631 0.00178  0.00367  591 LEU B N   
3894 C CA  . LEU B 157 ? 0.16519 0.18825 0.17572 -0.02843 0.00076  0.00206  591 LEU B CA  
3895 C C   . LEU B 157 ? 0.15357 0.17889 0.16447 -0.02834 -0.00084 -0.00067 591 LEU B C   
3896 O O   . LEU B 157 ? 0.15167 0.17600 0.16348 -0.03087 -0.00195 -0.00233 591 LEU B O   
3897 C CB  . LEU B 157 ? 0.14643 0.16208 0.15377 -0.02621 0.00057  0.00176  591 LEU B CB  
3898 C CG  . LEU B 157 ? 0.14007 0.14975 0.14502 -0.02663 0.00130  0.00443  591 LEU B CG  
3899 C CD1 . LEU B 157 ? 0.15190 0.15633 0.15370 -0.02230 0.00042  0.00375  591 LEU B CD1 
3900 C CD2 . LEU B 157 ? 0.11410 0.11807 0.11888 -0.03098 0.00099  0.00468  591 LEU B CD2 
3901 N N   . THR B 158 ? 0.13827 0.16579 0.14762 -0.02562 -0.00112 -0.00116 592 THR B N   
3902 C CA  . THR B 158 ? 0.09131 0.11945 0.09889 -0.02551 -0.00254 -0.00316 592 THR B CA  
3903 C C   . THR B 158 ? 0.15780 0.19128 0.16745 -0.02638 -0.00414 -0.00352 592 THR B C   
3904 O O   . THR B 158 ? 0.09377 0.12731 0.10240 -0.02730 -0.00586 -0.00543 592 THR B O   
3905 C CB  . THR B 158 ? 0.08965 0.11704 0.09387 -0.02317 -0.00223 -0.00312 592 THR B CB  
3906 O OG1 . THR B 158 ? 0.10156 0.12605 0.10514 -0.02248 -0.00095 -0.00369 592 THR B OG1 
3907 C CG2 . THR B 158 ? 0.09424 0.12071 0.09462 -0.02345 -0.00340 -0.00453 592 THR B CG2 
3908 N N   . ALA B 159 ? 0.15812 0.19702 0.17071 -0.02574 -0.00376 -0.00216 593 ALA B N   
3909 C CA  . ALA B 159 ? 0.12773 0.17398 0.14390 -0.02635 -0.00537 -0.00323 593 ALA B CA  
3910 C C   . ALA B 159 ? 0.12585 0.17290 0.14548 -0.03085 -0.00570 -0.00454 593 ALA B C   
3911 O O   . ALA B 159 ? 0.15249 0.20248 0.17311 -0.03160 -0.00815 -0.00688 593 ALA B O   
3912 C CB  . ALA B 159 ? 0.10054 0.15392 0.12007 -0.02493 -0.00425 -0.00204 593 ALA B CB  
3913 N N   . ARG B 160 ? 0.18884 0.23229 0.20957 -0.03387 -0.00360 -0.00312 594 ARG B N   
3914 C CA  . ARG B 160 ? 0.18428 0.22612 0.20748 -0.03884 -0.00393 -0.00425 594 ARG B CA  
3915 C C   . ARG B 160 ? 0.12391 0.15905 0.14376 -0.03881 -0.00590 -0.00681 594 ARG B C   
3916 O O   . ARG B 160 ? 0.14097 0.17703 0.16269 -0.04180 -0.00773 -0.00931 594 ARG B O   
3917 C CB  . ARG B 160 ? 0.12866 0.16534 0.15159 -0.04181 -0.00134 -0.00153 594 ARG B CB  
3918 C CG  . ARG B 160 ? 0.22498 0.26953 0.25139 -0.04338 0.00111  0.00071  594 ARG B CG  
3919 C CD  . ARG B 160 ? 0.16467 0.21633 0.19712 -0.04938 0.00131  -0.00055 594 ARG B CD  
3920 N NE  . ARG B 160 ? 0.20107 0.26192 0.23717 -0.05136 0.00438  0.00129  594 ARG B NE  
3921 C CZ  . ARG B 160 ? 0.20003 0.27512 0.24237 -0.05081 0.00420  -0.00070 594 ARG B CZ  
3922 N NH1 . ARG B 160 ? 0.14419 0.22512 0.18937 -0.04826 0.00061  -0.00432 594 ARG B NH1 
3923 N NH2 . ARG B 160 ? 0.22550 0.30944 0.27087 -0.05249 0.00759  0.00077  594 ARG B NH2 
3924 N N   . TYR B 161 ? 0.15352 0.18272 0.16863 -0.03558 -0.00549 -0.00669 595 TYR B N   
3925 C CA  . TYR B 161 ? 0.11368 0.13814 0.12536 -0.03510 -0.00690 -0.00958 595 TYR B CA  
3926 C C   . TYR B 161 ? 0.18318 0.21233 0.19377 -0.03444 -0.00921 -0.01165 595 TYR B C   
3927 O O   . TYR B 161 ? 0.16698 0.19497 0.17672 -0.03594 -0.01115 -0.01457 595 TYR B O   
3928 C CB  . TYR B 161 ? 0.21227 0.23240 0.22001 -0.03182 -0.00559 -0.00948 595 TYR B CB  
3929 C CG  . TYR B 161 ? 0.14330 0.16111 0.14733 -0.03109 -0.00651 -0.01279 595 TYR B CG  
3930 C CD1 . TYR B 161 ? 0.11202 0.12440 0.11531 -0.03186 -0.00721 -0.01544 595 TYR B CD1 
3931 C CD2 . TYR B 161 ? 0.10809 0.12854 0.10847 -0.02967 -0.00673 -0.01333 595 TYR B CD2 
3932 C CE1 . TYR B 161 ? 0.11533 0.12661 0.11502 -0.03092 -0.00786 -0.01897 595 TYR B CE1 
3933 C CE2 . TYR B 161 ? 0.10921 0.12808 0.10528 -0.02937 -0.00708 -0.01623 595 TYR B CE2 
3934 C CZ  . TYR B 161 ? 0.11368 0.12881 0.10977 -0.02985 -0.00752 -0.01927 595 TYR B CZ  
3935 O OH  . TYR B 161 ? 0.16085 0.17528 0.15240 -0.02920 -0.00766 -0.02267 595 TYR B OH  
3936 N N   . ALA B 162 ? 0.10741 0.14089 0.11700 -0.03176 -0.00943 -0.01032 596 ALA B N   
3937 C CA  . ALA B 162 ? 0.13449 0.17103 0.14139 -0.03025 -0.01219 -0.01186 596 ALA B CA  
3938 C C   . ALA B 162 ? 0.12796 0.17050 0.13970 -0.03260 -0.01476 -0.01414 596 ALA B C   
3939 O O   . ALA B 162 ? 0.11873 0.16159 0.12793 -0.03253 -0.01754 -0.01681 596 ALA B O   
3940 C CB  . ALA B 162 ? 0.10050 0.13929 0.10539 -0.02669 -0.01243 -0.00987 596 ALA B CB  
3941 N N   . GLN B 163 ? 0.10286 0.15069 0.12148 -0.03504 -0.01376 -0.01335 597 GLN B N   
3942 C CA  . GLN B 163 ? 0.14352 0.19867 0.16821 -0.03840 -0.01582 -0.01592 597 GLN B CA  
3943 C C   . GLN B 163 ? 0.16158 0.21101 0.18603 -0.04260 -0.01660 -0.01837 597 GLN B C   
3944 O O   . GLN B 163 ? 0.15104 0.20430 0.17733 -0.04429 -0.01973 -0.02187 597 GLN B O   
3945 C CB  . GLN B 163 ? 0.12257 0.18530 0.15456 -0.04097 -0.01360 -0.01439 597 GLN B CB  
3946 C CG  . GLN B 163 ? 0.27580 0.34608 0.30892 -0.03636 -0.01355 -0.01322 597 GLN B CG  
3947 C CD  . GLN B 163 ? 0.27729 0.35618 0.31735 -0.03893 -0.01071 -0.01202 597 GLN B CD  
3948 O OE1 . GLN B 163 ? 0.22858 0.30415 0.27012 -0.04387 -0.00770 -0.01028 597 GLN B OE1 
3949 N NE2 . GLN B 163 ? 0.19445 0.28419 0.23811 -0.03539 -0.01169 -0.01303 597 GLN B NE2 
3950 N N   . SER B 164 ? 0.11236 0.15238 0.13428 -0.04384 -0.01426 -0.01702 598 SER B N   
3951 C CA  . SER B 164 ? 0.13804 0.17097 0.15913 -0.04728 -0.01528 -0.01961 598 SER B CA  
3952 C C   . SER B 164 ? 0.18626 0.21706 0.20220 -0.04504 -0.01805 -0.02331 598 SER B C   
3953 O O   . SER B 164 ? 0.24268 0.27051 0.25873 -0.04783 -0.02016 -0.02681 598 SER B O   
3954 C CB  . SER B 164 ? 0.14179 0.16427 0.16017 -0.04750 -0.01279 -0.01756 598 SER B CB  
3955 O OG  . SER B 164 ? 0.11941 0.13793 0.13243 -0.04259 -0.01189 -0.01722 598 SER B OG  
3956 N N   . ILE B 165 ? 0.13014 0.16195 0.14090 -0.04042 -0.01806 -0.02265 599 ILE B N   
3957 C CA  . ILE B 165 ? 0.12393 0.15373 0.12820 -0.03842 -0.02012 -0.02569 599 ILE B CA  
3958 C C   . ILE B 165 ? 0.14737 0.18410 0.15045 -0.03675 -0.02357 -0.02686 599 ILE B C   
3959 O O   . ILE B 165 ? 0.26088 0.29608 0.25745 -0.03510 -0.02569 -0.02927 599 ILE B O   
3960 C CB  . ILE B 165 ? 0.12296 0.14790 0.12053 -0.03511 -0.01755 -0.02443 599 ILE B CB  
3961 C CG1 . ILE B 165 ? 0.13210 0.15988 0.12845 -0.03254 -0.01619 -0.02066 599 ILE B CG1 
3962 C CG2 . ILE B 165 ? 0.12337 0.14197 0.12191 -0.03562 -0.01508 -0.02441 599 ILE B CG2 
3963 C CD1 . ILE B 165 ? 0.16322 0.18734 0.15258 -0.03031 -0.01394 -0.01983 599 ILE B CD1 
3964 N N   . THR B 166 ? 0.19501 0.23949 0.20362 -0.03659 -0.02437 -0.02544 600 THR B N   
3965 C CA  . THR B 166 ? 0.21492 0.26669 0.22312 -0.03419 -0.02855 -0.02722 600 THR B CA  
3966 C C   . THR B 166 ? 0.17345 0.23494 0.19162 -0.03781 -0.03071 -0.02995 600 THR B C   
3967 O O   . THR B 166 ? 0.16322 0.22679 0.18222 -0.03972 -0.03410 -0.03411 600 THR B O   
3968 C CB  . THR B 166 ? 0.22751 0.28081 0.23258 -0.02936 -0.02836 -0.02400 600 THR B CB  
3969 O OG1 . THR B 166 ? 0.11361 0.16972 0.12500 -0.03019 -0.02518 -0.02124 600 THR B OG1 
3970 C CG2 . THR B 166 ? 0.23810 0.28218 0.23243 -0.02673 -0.02679 -0.02194 600 THR B CG2 
3971 N N   . ARG B 167 ? 0.13687 0.20513 0.16268 -0.03907 -0.02874 -0.02806 601 ARG B N   
3972 C CA  . ARG B 167 ? 0.11764 0.19630 0.15401 -0.04390 -0.02941 -0.03039 601 ARG B CA  
3973 C C   . ARG B 167 ? 0.11855 0.20164 0.16038 -0.04486 -0.02528 -0.02690 601 ARG B C   
3974 O O   . ARG B 167 ? 0.13143 0.21154 0.16911 -0.04037 -0.02345 -0.02358 601 ARG B O   
3975 C CB  . ARG B 167 ? 0.15858 0.24913 0.19826 -0.04150 -0.03469 -0.03452 601 ARG B CB  
3976 C CG  . ARG B 167 ? 0.15064 0.24266 0.18453 -0.03344 -0.03689 -0.03317 601 ARG B CG  
3977 C CD  . ARG B 167 ? 0.21211 0.31522 0.24839 -0.02995 -0.04299 -0.03755 601 ARG B CD  
3978 N NE  . ARG B 167 ? 0.35056 0.46119 0.38855 -0.02392 -0.04406 -0.03660 601 ARG B NE  
3979 C CZ  . ARG B 167 ? 0.25199 0.35476 0.28013 -0.01728 -0.04481 -0.03360 601 ARG B CZ  
3980 N NH1 . ARG B 167 ? 0.29093 0.37946 0.30711 -0.01629 -0.04420 -0.03112 601 ARG B NH1 
3981 N NH2 . ARG B 167 ? 0.21501 0.32436 0.24525 -0.01173 -0.04606 -0.03330 601 ARG B NH2 
3982 N N   . GLU B 168 ? 0.11267 0.20270 0.16336 -0.05118 -0.02370 -0.02776 602 GLU B N   
3983 C CA  . GLU B 168 ? 0.19731 0.29120 0.25215 -0.05273 -0.01917 -0.02430 602 GLU B CA  
3984 C C   . GLU B 168 ? 0.25288 0.36010 0.31174 -0.04754 -0.01998 -0.02476 602 GLU B C   
3985 O O   . GLU B 168 ? 0.22135 0.33040 0.28093 -0.04631 -0.01645 -0.02172 602 GLU B O   
3986 C CB  . GLU B 168 ? 0.19408 0.29079 0.25607 -0.06189 -0.01659 -0.02463 602 GLU B CB  
3987 C CG  . GLU B 168 ? 0.32345 0.43184 0.39384 -0.06655 -0.01977 -0.02990 602 GLU B CG  
3988 C CD  . GLU B 168 ? 0.39459 0.50608 0.47215 -0.07680 -0.01635 -0.02971 602 GLU B CD  
3989 O OE1 . GLU B 168 ? 0.35649 0.46389 0.43278 -0.07921 -0.01135 -0.02511 602 GLU B OE1 
3990 O OE2 . GLU B 168 ? 0.45160 0.56923 0.53551 -0.08277 -0.01869 -0.03413 602 GLU B OE2 
3991 N N   . SER B 169 ? 0.16027 0.27634 0.22101 -0.04377 -0.02490 -0.02872 603 SER B N   
3992 C CA  . SER B 169 ? 0.14501 0.27300 0.20887 -0.03745 -0.02660 -0.02980 603 SER B CA  
3993 C C   . SER B 169 ? 0.18782 0.30650 0.24117 -0.02899 -0.02839 -0.02751 603 SER B C   
3994 O O   . SER B 169 ? 0.14493 0.27059 0.19872 -0.02246 -0.03084 -0.02856 603 SER B O   
3995 C CB  . SER B 169 ? 0.10422 0.24736 0.17565 -0.03683 -0.03170 -0.03565 603 SER B CB  
3996 O OG  . SER B 169 ? 0.21310 0.35000 0.27699 -0.03264 -0.03718 -0.03763 603 SER B OG  
3997 N N   . LEU B 170 ? 0.12974 0.23292 0.17365 -0.02903 -0.02730 -0.02470 604 LEU B N   
3998 C CA  . LEU B 170 ? 0.21310 0.30682 0.24687 -0.02259 -0.02822 -0.02223 604 LEU B CA  
3999 C C   . LEU B 170 ? 0.21882 0.31468 0.25378 -0.01946 -0.02556 -0.01974 604 LEU B C   
4000 O O   . LEU B 170 ? 0.25668 0.35193 0.29473 -0.02304 -0.02099 -0.01748 604 LEU B O   
4001 C CB  . LEU B 170 ? 0.15041 0.22951 0.17579 -0.02450 -0.02621 -0.01992 604 LEU B CB  
4002 C CG  . LEU B 170 ? 0.19878 0.26802 0.21325 -0.01931 -0.02696 -0.01761 604 LEU B CG  
4003 C CD1 . LEU B 170 ? 0.19897 0.26536 0.20602 -0.01662 -0.03161 -0.01958 604 LEU B CD1 
4004 C CD2 . LEU B 170 ? 0.10594 0.16460 0.11581 -0.02144 -0.02275 -0.01471 604 LEU B CD2 
4005 N N   . ARG B 171 ? 0.18295 0.28043 0.21449 -0.01239 -0.02879 -0.02027 605 ARG B N   
4006 C CA  . ARG B 171 ? 0.10914 0.20971 0.14189 -0.00836 -0.02721 -0.01901 605 ARG B CA  
4007 C C   . ARG B 171 ? 0.11337 0.19926 0.13662 -0.00691 -0.02514 -0.01511 605 ARG B C   
4008 O O   . ARG B 171 ? 0.11269 0.18879 0.12649 -0.00334 -0.02787 -0.01430 605 ARG B O   
4009 C CB  . ARG B 171 ? 0.10470 0.21343 0.13815 -0.00075 -0.03230 -0.02209 605 ARG B CB  
4010 C CG  . ARG B 171 ? 0.11277 0.23928 0.15744 -0.00188 -0.03448 -0.02686 605 ARG B CG  
4011 C CD  . ARG B 171 ? 0.17814 0.31386 0.22399 0.00716  -0.03974 -0.03040 605 ARG B CD  
4012 N NE  . ARG B 171 ? 0.28495 0.40896 0.31892 0.01336  -0.04555 -0.03015 605 ARG B NE  
4013 C CZ  . ARG B 171 ? 0.34378 0.47096 0.37684 0.01501  -0.05097 -0.03325 605 ARG B CZ  
4014 N NH1 . ARG B 171 ? 0.30132 0.44411 0.34588 0.01098  -0.05172 -0.03751 605 ARG B NH1 
4015 N NH2 . ARG B 171 ? 0.23424 0.34829 0.25399 0.02052  -0.05579 -0.03208 605 ARG B NH2 
4016 N N   . VAL B 172 ? 0.09512 0.17948 0.12047 -0.00989 -0.02039 -0.01274 606 VAL B N   
4017 C CA  . VAL B 172 ? 0.09496 0.16744 0.11301 -0.00901 -0.01830 -0.00965 606 VAL B CA  
4018 C C   . VAL B 172 ? 0.15041 0.22594 0.16921 -0.00477 -0.01747 -0.00919 606 VAL B C   
4019 O O   . VAL B 172 ? 0.09031 0.17552 0.11611 -0.00591 -0.01500 -0.00962 606 VAL B O   
4020 C CB  . VAL B 172 ? 0.15199 0.21913 0.17059 -0.01472 -0.01425 -0.00767 606 VAL B CB  
4021 C CG1 . VAL B 172 ? 0.12144 0.17825 0.13341 -0.01351 -0.01259 -0.00531 606 VAL B CG1 
4022 C CG2 . VAL B 172 ? 0.09397 0.15833 0.11198 -0.01851 -0.01526 -0.00887 606 VAL B CG2 
4023 N N   . LEU B 173 ? 0.16989 0.23674 0.18087 -0.00015 -0.01943 -0.00842 607 LEU B N   
4024 C CA  . LEU B 173 ? 0.09813 0.16444 0.10788 0.00392  -0.01879 -0.00806 607 LEU B CA  
4025 C C   . LEU B 173 ? 0.22937 0.28632 0.23528 0.00103  -0.01547 -0.00540 607 LEU B C   
4026 O O   . LEU B 173 ? 0.14285 0.18991 0.14288 -0.00107 -0.01554 -0.00409 607 LEU B O   
4027 C CB  . LEU B 173 ? 0.10610 0.16687 0.10884 0.01078  -0.02356 -0.00912 607 LEU B CB  
4028 C CG  . LEU B 173 ? 0.10927 0.16363 0.10722 0.01498  -0.02368 -0.00866 607 LEU B CG  
4029 C CD1 . LEU B 173 ? 0.16276 0.22987 0.16824 0.01783  -0.02215 -0.01068 607 LEU B CD1 
4030 C CD2 . LEU B 173 ? 0.12029 0.16430 0.10863 0.02084  -0.02886 -0.00910 607 LEU B CD2 
4031 N N   . ILE B 174 ? 0.14655 0.20759 0.15583 0.00092  -0.01253 -0.00488 608 ILE B N   
4032 C CA  . ILE B 174 ? 0.12814 0.18197 0.13443 -0.00090 -0.00994 -0.00296 608 ILE B CA  
4033 C C   . ILE B 174 ? 0.09752 0.15029 0.10117 0.00401  -0.01064 -0.00364 608 ILE B C   
4034 O O   . ILE B 174 ? 0.09160 0.15289 0.09923 0.00583  -0.00921 -0.00440 608 ILE B O   
4035 C CB  . ILE B 174 ? 0.14714 0.20490 0.15810 -0.00534 -0.00615 -0.00160 608 ILE B CB  
4036 C CG1 . ILE B 174 ? 0.08569 0.14272 0.09860 -0.01007 -0.00584 -0.00137 608 ILE B CG1 
4037 C CG2 . ILE B 174 ? 0.16705 0.21824 0.17474 -0.00577 -0.00434 -0.00019 608 ILE B CG2 
4038 C CD1 . ILE B 174 ? 0.08390 0.14140 0.09961 -0.01432 -0.00265 0.00020  608 ILE B CD1 
4039 N N   . VAL B 175 ? 0.09846 0.14063 0.09500 0.00586  -0.01270 -0.00351 609 VAL B N   
4040 C CA  . VAL B 175 ? 0.12420 0.16278 0.11722 0.01007  -0.01368 -0.00441 609 VAL B CA  
4041 C C   . VAL B 175 ? 0.10805 0.14250 0.10020 0.00705  -0.01105 -0.00330 609 VAL B C   
4042 O O   . VAL B 175 ? 0.15968 0.18691 0.14902 0.00332  -0.01051 -0.00226 609 VAL B O   
4043 C CB  . VAL B 175 ? 0.11163 0.13936 0.09650 0.01349  -0.01777 -0.00497 609 VAL B CB  
4044 C CG1 . VAL B 175 ? 0.17618 0.20000 0.15755 0.01831  -0.01927 -0.00655 609 VAL B CG1 
4045 C CG2 . VAL B 175 ? 0.11504 0.14654 0.10018 0.01694  -0.02111 -0.00616 609 VAL B CG2 
4046 N N   . ASP B 176 ? 0.13002 0.16996 0.12455 0.00883  -0.00944 -0.00384 610 ASP B N   
4047 C CA  . ASP B 176 ? 0.15273 0.19041 0.14670 0.00693  -0.00743 -0.00317 610 ASP B CA  
4048 C C   . ASP B 176 ? 0.13153 0.16432 0.12103 0.01089  -0.00933 -0.00504 610 ASP B C   
4049 O O   . ASP B 176 ? 0.13240 0.17068 0.12254 0.01479  -0.00909 -0.00637 610 ASP B O   
4050 C CB  . ASP B 176 ? 0.17276 0.21928 0.17122 0.00582  -0.00427 -0.00207 610 ASP B CB  
4051 C CG  . ASP B 176 ? 0.08993 0.13373 0.08714 0.00433  -0.00276 -0.00121 610 ASP B CG  
4052 O OD1 . ASP B 176 ? 0.10369 0.14150 0.09764 0.00520  -0.00416 -0.00239 610 ASP B OD1 
4053 O OD2 . ASP B 176 ? 0.10871 0.15612 0.10796 0.00223  -0.00039 0.00055  610 ASP B OD2 
4054 N N   . TRP B 177 ? 0.10577 0.12812 0.09039 0.00956  -0.01109 -0.00535 611 TRP B N   
4055 C CA  . TRP B 177 ? 0.11191 0.12762 0.09176 0.01240  -0.01321 -0.00736 611 TRP B CA  
4056 C C   . TRP B 177 ? 0.15268 0.16723 0.13289 0.00988  -0.01196 -0.00790 611 TRP B C   
4057 O O   . TRP B 177 ? 0.18648 0.19418 0.16275 0.01059  -0.01381 -0.00980 611 TRP B O   
4058 C CB  . TRP B 177 ? 0.12126 0.12481 0.09428 0.01242  -0.01630 -0.00755 611 TRP B CB  
4059 C CG  . TRP B 177 ? 0.23257 0.22819 0.20288 0.00606  -0.01549 -0.00608 611 TRP B CG  
4060 C CD1 . TRP B 177 ? 0.24310 0.23914 0.21558 0.00124  -0.01327 -0.00615 611 TRP B CD1 
4061 C CD2 . TRP B 177 ? 0.21239 0.19915 0.17689 0.00407  -0.01685 -0.00462 611 TRP B CD2 
4062 N NE1 . TRP B 177 ? 0.22185 0.21115 0.19109 -0.00400 -0.01266 -0.00508 611 TRP B NE1 
4063 C CE2 . TRP B 177 ? 0.24381 0.22666 0.20743 -0.00260 -0.01467 -0.00379 611 TRP B CE2 
4064 C CE3 . TRP B 177 ? 0.13720 0.11935 0.09680 0.00761  -0.01985 -0.00409 611 TRP B CE3 
4065 C CZ2 . TRP B 177 ? 0.22827 0.20256 0.18563 -0.00648 -0.01475 -0.00209 611 TRP B CZ2 
4066 C CZ3 . TRP B 177 ? 0.22408 0.19640 0.17668 0.00428  -0.02058 -0.00217 611 TRP B CZ3 
4067 C CH2 . TRP B 177 ? 0.29312 0.26147 0.24434 -0.00304 -0.01772 -0.00100 611 TRP B CH2 
4068 N N   . ASP B 178 ? 0.11294 0.13359 0.09754 0.00716  -0.00930 -0.00655 612 ASP B N   
4069 C CA  . ASP B 178 ? 0.12288 0.14507 0.10815 0.00687  -0.00863 -0.00748 612 ASP B CA  
4070 C C   . ASP B 178 ? 0.19059 0.21601 0.17410 0.01205  -0.00936 -0.00913 612 ASP B C   
4071 O O   . ASP B 178 ? 0.15173 0.18274 0.13599 0.01520  -0.00873 -0.00880 612 ASP B O   
4072 C CB  . ASP B 178 ? 0.16315 0.19077 0.15237 0.00451  -0.00615 -0.00551 612 ASP B CB  
4073 C CG  . ASP B 178 ? 0.18857 0.21727 0.17800 0.00468  -0.00614 -0.00653 612 ASP B CG  
4074 O OD1 . ASP B 178 ? 0.19946 0.23051 0.18698 0.00820  -0.00656 -0.00738 612 ASP B OD1 
4075 O OD2 . ASP B 178 ? 0.10837 0.13620 0.09976 0.00169  -0.00584 -0.00680 612 ASP B OD2 
4076 N N   . VAL B 179 ? 0.18176 0.20455 0.16310 0.01294  -0.01069 -0.01141 613 VAL B N   
4077 C CA  . VAL B 179 ? 0.11297 0.13784 0.09145 0.01827  -0.01178 -0.01367 613 VAL B CA  
4078 C C   . VAL B 179 ? 0.12688 0.16133 0.10666 0.02040  -0.00910 -0.01210 613 VAL B C   
4079 O O   . VAL B 179 ? 0.17667 0.21542 0.15443 0.02502  -0.00900 -0.01353 613 VAL B O   
4080 C CB  . VAL B 179 ? 0.15383 0.17368 0.12957 0.01839  -0.01416 -0.01691 613 VAL B CB  
4081 C CG1 . VAL B 179 ? 0.15446 0.17955 0.13179 0.01778  -0.01316 -0.01670 613 VAL B CG1 
4082 C CG2 . VAL B 179 ? 0.13163 0.14947 0.10287 0.02403  -0.01647 -0.02020 613 VAL B CG2 
4083 N N   . HIS B 180 ? 0.10824 0.14565 0.09065 0.01717  -0.00688 -0.00926 614 HIS B N   
4084 C CA  . HIS B 180 ? 0.15473 0.19915 0.13715 0.01801  -0.00404 -0.00689 614 HIS B CA  
4085 C C   . HIS B 180 ? 0.14268 0.19172 0.12867 0.01610  -0.00173 -0.00455 614 HIS B C   
4086 O O   . HIS B 180 ? 0.13825 0.18454 0.12693 0.01346  -0.00235 -0.00411 614 HIS B O   
4087 C CB  . HIS B 180 ? 0.14184 0.18515 0.12389 0.01600  -0.00347 -0.00513 614 HIS B CB  
4088 C CG  . HIS B 180 ? 0.24112 0.28170 0.22062 0.01785  -0.00608 -0.00791 614 HIS B CG  
4089 N ND1 . HIS B 180 ? 0.15649 0.19260 0.13795 0.01570  -0.00836 -0.01034 614 HIS B ND1 
4090 C CD2 . HIS B 180 ? 0.11314 0.15548 0.08830 0.02138  -0.00678 -0.00889 614 HIS B CD2 
4091 C CE1 . HIS B 180 ? 0.10739 0.14329 0.08685 0.01766  -0.01055 -0.01306 614 HIS B CE1 
4092 N NE2 . HIS B 180 ? 0.14989 0.18919 0.12517 0.02151  -0.00992 -0.01227 614 HIS B NE2 
4093 N N   . HIS B 181 ? 0.15364 0.21020 0.13944 0.01712  0.00103  -0.00320 615 HIS B N   
4094 C CA  . HIS B 181 ? 0.12227 0.18504 0.11232 0.01473  0.00338  -0.00148 615 HIS B CA  
4095 C C   . HIS B 181 ? 0.11249 0.17254 0.10426 0.00942  0.00493  0.00191  615 HIS B C   
4096 O O   . HIS B 181 ? 0.10376 0.16082 0.09244 0.00851  0.00576  0.00385  615 HIS B O   
4097 C CB  . HIS B 181 ? 0.14182 0.21480 0.13147 0.01662  0.00649  -0.00138 615 HIS B CB  
4098 C CG  . HIS B 181 ? 0.09951 0.18088 0.09465 0.01349  0.00910  -0.00020 615 HIS B CG  
4099 N ND1 . HIS B 181 ? 0.13101 0.21776 0.12647 0.00943  0.01333  0.00293  615 HIS B ND1 
4100 C CD2 . HIS B 181 ? 0.13909 0.22426 0.13943 0.01355  0.00784  -0.00187 615 HIS B CD2 
4101 C CE1 . HIS B 181 ? 0.18199 0.27650 0.18366 0.00660  0.01476  0.00277  615 HIS B CE1 
4102 N NE2 . HIS B 181 ? 0.13517 0.22935 0.14006 0.00946  0.01125  -0.00028 615 HIS B NE2 
4103 N N   . GLY B 182 ? 0.12528 0.18582 0.12139 0.00644  0.00486  0.00235  616 GLY B N   
4104 C CA  . GLY B 182 ? 0.13059 0.18841 0.12839 0.00156  0.00610  0.00499  616 GLY B CA  
4105 C C   . GLY B 182 ? 0.13868 0.20255 0.13766 -0.00147 0.00965  0.00749  616 GLY B C   
4106 O O   . GLY B 182 ? 0.13705 0.20606 0.14072 -0.00426 0.01056  0.00746  616 GLY B O   
4107 N N   . ASN B 183 ? 0.16573 0.22902 0.16003 -0.00120 0.01163  0.00960  617 ASN B N   
4108 C CA  . ASN B 183 ? 0.17442 0.24235 0.16825 -0.00501 0.01563  0.01257  617 ASN B CA  
4109 C C   . ASN B 183 ? 0.17885 0.24278 0.17532 -0.01093 0.01629  0.01469  617 ASN B C   
4110 O O   . ASN B 183 ? 0.17803 0.24816 0.17790 -0.01538 0.01905  0.01570  617 ASN B O   
4111 C CB  . ASN B 183 ? 0.15823 0.22275 0.14409 -0.00372 0.01714  0.01512  617 ASN B CB  
4112 C CG  . ASN B 183 ? 0.24920 0.30249 0.23075 -0.00213 0.01413  0.01576  617 ASN B CG  
4113 O OD1 . ASN B 183 ? 0.18450 0.23596 0.16550 0.00206  0.01111  0.01297  617 ASN B OD1 
4114 N ND2 . ASN B 183 ? 0.25014 0.29597 0.22878 -0.00547 0.01475  0.01908  617 ASN B ND2 
4115 N N   . GLY B 184 ? 0.12489 0.17906 0.12014 -0.01116 0.01377  0.01491  618 GLY B N   
4116 C CA  . GLY B 184 ? 0.15987 0.20911 0.15690 -0.01615 0.01397  0.01637  618 GLY B CA  
4117 C C   . GLY B 184 ? 0.16338 0.21852 0.16752 -0.01851 0.01341  0.01415  618 GLY B C   
4118 O O   . GLY B 184 ? 0.13243 0.18949 0.13941 -0.02365 0.01502  0.01516  618 GLY B O   
4119 N N   . THR B 185 ? 0.14409 0.20153 0.15058 -0.01495 0.01089  0.01108  619 THR B N   
4120 C CA  . THR B 185 ? 0.11423 0.17654 0.12613 -0.01616 0.00960  0.00890  619 THR B CA  
4121 C C   . THR B 185 ? 0.13816 0.21273 0.15463 -0.01720 0.01162  0.00823  619 THR B C   
4122 O O   . THR B 185 ? 0.12097 0.20044 0.14242 -0.02112 0.01195  0.00760  619 THR B O   
4123 C CB  . THR B 185 ? 0.08646 0.14664 0.09767 -0.01189 0.00641  0.00633  619 THR B CB  
4124 O OG1 . THR B 185 ? 0.11321 0.16445 0.12060 -0.01103 0.00532  0.00664  619 THR B OG1 
4125 C CG2 . THR B 185 ? 0.13229 0.19373 0.14678 -0.01317 0.00440  0.00461  619 THR B CG2 
4126 N N   . GLN B 186 ? 0.15034 0.23100 0.16553 -0.01369 0.01298  0.00782  620 GLN B N   
4127 C CA  . GLN B 186 ? 0.09202 0.18659 0.11212 -0.01418 0.01528  0.00650  620 GLN B CA  
4128 C C   . GLN B 186 ? 0.13989 0.23791 0.16185 -0.02153 0.01936  0.00917  620 GLN B C   
4129 O O   . GLN B 186 ? 0.19232 0.30094 0.22115 -0.02495 0.02051  0.00763  620 GLN B O   
4130 C CB  . GLN B 186 ? 0.11874 0.21864 0.13602 -0.00877 0.01630  0.00541  620 GLN B CB  
4131 C CG  . GLN B 186 ? 0.11008 0.22465 0.13099 -0.01047 0.02054  0.00498  620 GLN B CG  
4132 C CD  . GLN B 186 ? 0.13876 0.26000 0.15717 -0.00400 0.02117  0.00274  620 GLN B CD  
4133 O OE1 . GLN B 186 ? 0.10902 0.22783 0.12628 0.00254  0.01737  -0.00029 620 GLN B OE1 
4134 N NE2 . GLN B 186 ? 0.10273 0.23181 0.11953 -0.00598 0.02604  0.00419  620 GLN B NE2 
4135 N N   . HIS B 187 ? 0.10208 0.19089 0.11767 -0.02418 0.02136  0.01305  621 HIS B N   
4136 C CA  . HIS B 187 ? 0.10930 0.19844 0.12466 -0.03179 0.02528  0.01624  621 HIS B CA  
4137 C C   . HIS B 187 ? 0.12282 0.20818 0.14252 -0.03730 0.02387  0.01588  621 HIS B C   
4138 O O   . HIS B 187 ? 0.17672 0.26887 0.20109 -0.04388 0.02645  0.01608  621 HIS B O   
4139 C CB  . HIS B 187 ? 0.17224 0.24959 0.17773 -0.03240 0.02686  0.02071  621 HIS B CB  
4140 C CG  . HIS B 187 ? 0.15581 0.23807 0.15630 -0.02848 0.02916  0.02142  621 HIS B CG  
4141 N ND1 . HIS B 187 ? 0.17400 0.24630 0.16529 -0.02484 0.02833  0.02367  621 HIS B ND1 
4142 C CD2 . HIS B 187 ? 0.14605 0.24277 0.14933 -0.02723 0.03210  0.01968  621 HIS B CD2 
4143 C CE1 . HIS B 187 ? 0.17064 0.25032 0.15867 -0.02173 0.03063  0.02347  621 HIS B CE1 
4144 N NE2 . HIS B 187 ? 0.12449 0.21906 0.11964 -0.02304 0.03313  0.02102  621 HIS B NE2 
4145 N N   . ILE B 188 ? 0.16818 0.24352 0.18659 -0.03498 0.01989  0.01494  622 ILE B N   
4146 C CA  . ILE B 188 ? 0.22248 0.29268 0.24357 -0.03976 0.01836  0.01443  622 ILE B CA  
4147 C C   . ILE B 188 ? 0.10271 0.18551 0.13270 -0.04157 0.01750  0.01080  622 ILE B C   
4148 O O   . ILE B 188 ? 0.10616 0.19001 0.13995 -0.04794 0.01798  0.01046  622 ILE B O   
4149 C CB  . ILE B 188 ? 0.18331 0.24155 0.20074 -0.03615 0.01463  0.01372  622 ILE B CB  
4150 C CG1 . ILE B 188 ? 0.14061 0.18589 0.15029 -0.03626 0.01519  0.01706  622 ILE B CG1 
4151 C CG2 . ILE B 188 ? 0.15324 0.20976 0.17453 -0.03892 0.01218  0.01135  622 ILE B CG2 
4152 C CD1 . ILE B 188 ? 0.13594 0.17244 0.14245 -0.03151 0.01197  0.01582  622 ILE B CD1 
4153 N N   . PHE B 189 ? 0.09648 0.18881 0.12970 -0.03590 0.01589  0.00780  623 PHE B N   
4154 C CA  . PHE B 189 ? 0.16482 0.26921 0.20596 -0.03586 0.01402  0.00385  623 PHE B CA  
4155 C C   . PHE B 189 ? 0.18216 0.30371 0.22906 -0.03534 0.01666  0.00210  623 PHE B C   
4156 O O   . PHE B 189 ? 0.13563 0.26876 0.18888 -0.03250 0.01435  -0.00196 623 PHE B O   
4157 C CB  . PHE B 189 ? 0.08815 0.18938 0.12795 -0.02917 0.00920  0.00126  623 PHE B CB  
4158 C CG  . PHE B 189 ? 0.22669 0.31339 0.26130 -0.02946 0.00699  0.00232  623 PHE B CG  
4159 C CD1 . PHE B 189 ? 0.10629 0.18982 0.14278 -0.03394 0.00567  0.00149  623 PHE B CD1 
4160 C CD2 . PHE B 189 ? 0.18206 0.25930 0.21029 -0.02522 0.00620  0.00353  623 PHE B CD2 
4161 C CE1 . PHE B 189 ? 0.13576 0.20723 0.16755 -0.03372 0.00387  0.00185  623 PHE B CE1 
4162 C CE2 . PHE B 189 ? 0.15638 0.22258 0.18074 -0.02550 0.00457  0.00388  623 PHE B CE2 
4163 C CZ  . PHE B 189 ? 0.15238 0.21582 0.17837 -0.02949 0.00351  0.00303  623 PHE B CZ  
4164 N N   . GLU B 190 ? 0.13241 0.25622 0.17683 -0.03762 0.02136  0.00483  624 GLU B N   
4165 C CA  . GLU B 190 ? 0.15577 0.29656 0.20473 -0.03583 0.02423  0.00278  624 GLU B CA  
4166 C C   . GLU B 190 ? 0.17459 0.33220 0.23443 -0.04078 0.02525  -0.00059 624 GLU B C   
4167 O O   . GLU B 190 ? 0.13393 0.30764 0.20033 -0.03632 0.02460  -0.00496 624 GLU B O   
4168 C CB  . GLU B 190 ? 0.12569 0.26496 0.16857 -0.03830 0.02956  0.00677  624 GLU B CB  
4169 C CG  . GLU B 190 ? 0.25702 0.40756 0.29958 -0.03171 0.03108  0.00468  624 GLU B CG  
4170 C CD  . GLU B 190 ? 0.24306 0.38614 0.27572 -0.03113 0.03437  0.00876  624 GLU B CD  
4171 O OE1 . GLU B 190 ? 0.22176 0.35220 0.24817 -0.03656 0.03597  0.01351  624 GLU B OE1 
4172 O OE2 . GLU B 190 ? 0.18791 0.33710 0.21840 -0.02473 0.03489  0.00696  624 GLU B OE2 
4173 N N   . GLU B 191 ? 0.15661 0.31099 0.21870 -0.04975 0.02650  0.00088  625 GLU B N   
4174 C CA  . GLU B 191 ? 0.15484 0.32496 0.22795 -0.05551 0.02703  -0.00276 625 GLU B CA  
4175 C C   . GLU B 191 ? 0.14085 0.30909 0.21792 -0.05375 0.02091  -0.00636 625 GLU B C   
4176 O O   . GLU B 191 ? 0.17735 0.35650 0.26324 -0.05908 0.02040  -0.00959 625 GLU B O   
4177 C CB  . GLU B 191 ? 0.11054 0.27857 0.18372 -0.06756 0.03223  0.00069  625 GLU B CB  
4178 C CG  . GLU B 191 ? 0.28578 0.45764 0.35481 -0.07005 0.03878  0.00413  625 GLU B CG  
4179 C CD  . GLU B 191 ? 0.35819 0.51628 0.42077 -0.07983 0.04266  0.00940  625 GLU B CD  
4180 O OE1 . GLU B 191 ? 0.24764 0.40810 0.31539 -0.08678 0.04349  0.00814  625 GLU B OE1 
4181 O OE2 . GLU B 191 ? 0.38761 0.53185 0.43940 -0.08025 0.04456  0.01478  625 GLU B OE2 
4182 N N   . ASP B 192 ? 0.17755 0.33294 0.24818 -0.04659 0.01634  -0.00610 626 ASP B N   
4183 C CA  . ASP B 192 ? 0.14781 0.29767 0.21905 -0.04522 0.01088  -0.00848 626 ASP B CA  
4184 C C   . ASP B 192 ? 0.14378 0.30227 0.21750 -0.03608 0.00619  -0.01280 626 ASP B C   
4185 O O   . ASP B 192 ? 0.15381 0.30752 0.22186 -0.02860 0.00510  -0.01213 626 ASP B O   
4186 C CB  . ASP B 192 ? 0.15448 0.28337 0.21592 -0.04437 0.00944  -0.00503 626 ASP B CB  
4187 C CG  . ASP B 192 ? 0.26553 0.38823 0.32665 -0.04416 0.00466  -0.00725 626 ASP B CG  
4188 O OD1 . ASP B 192 ? 0.17310 0.29662 0.23300 -0.03741 0.00052  -0.00959 626 ASP B OD1 
4189 O OD2 . ASP B 192 ? 0.27720 0.39344 0.33842 -0.05072 0.00495  -0.00668 626 ASP B OD2 
4190 N N   . ASP B 193 ? 0.08679 0.25720 0.16843 -0.03656 0.00302  -0.01738 627 ASP B N   
4191 C CA  . ASP B 193 ? 0.09738 0.27480 0.18046 -0.02737 -0.00242 -0.02165 627 ASP B CA  
4192 C C   . ASP B 193 ? 0.14472 0.30873 0.22123 -0.02405 -0.00806 -0.02184 627 ASP B C   
4193 O O   . ASP B 193 ? 0.10713 0.27404 0.18276 -0.01646 -0.01321 -0.02490 627 ASP B O   
4194 C CB  . ASP B 193 ? 0.15918 0.35962 0.25484 -0.02823 -0.00331 -0.02733 627 ASP B CB  
4195 C CG  . ASP B 193 ? 0.12653 0.33069 0.22860 -0.03692 -0.00409 -0.02917 627 ASP B CG  
4196 O OD1 . ASP B 193 ? 0.21242 0.40064 0.30840 -0.04017 -0.00552 -0.02687 627 ASP B OD1 
4197 O OD2 . ASP B 193 ? 0.13982 0.36072 0.25180 -0.04002 -0.00324 -0.03304 627 ASP B OD2 
4198 N N   . SER B 194 ? 0.08726 0.23664 0.15853 -0.02924 -0.00729 -0.01881 628 SER B N   
4199 C CA  . SER B 194 ? 0.18781 0.32449 0.25183 -0.02629 -0.01179 -0.01884 628 SER B CA  
4200 C C   . SER B 194 ? 0.20307 0.32468 0.25669 -0.02148 -0.01161 -0.01538 628 SER B C   
4201 O O   . SER B 194 ? 0.13178 0.24342 0.17848 -0.01843 -0.01496 -0.01528 628 SER B O   
4202 C CB  . SER B 194 ? 0.11614 0.24583 0.18018 -0.03387 -0.01152 -0.01847 628 SER B CB  
4203 O OG  . SER B 194 ? 0.10633 0.22308 0.16512 -0.03760 -0.00763 -0.01419 628 SER B OG  
4204 N N   . VAL B 195 ? 0.14628 0.26643 0.19844 -0.02103 -0.00772 -0.01271 629 VAL B N   
4205 C CA  . VAL B 195 ? 0.08772 0.19506 0.13111 -0.01698 -0.00747 -0.00995 629 VAL B CA  
4206 C C   . VAL B 195 ? 0.21992 0.33376 0.26377 -0.01141 -0.00672 -0.01049 629 VAL B C   
4207 O O   . VAL B 195 ? 0.11562 0.23692 0.16323 -0.01360 -0.00273 -0.00976 629 VAL B O   
4208 C CB  . VAL B 195 ? 0.23456 0.33112 0.27429 -0.02186 -0.00388 -0.00629 629 VAL B CB  
4209 C CG1 . VAL B 195 ? 0.13113 0.21666 0.16309 -0.01774 -0.00390 -0.00427 629 VAL B CG1 
4210 C CG2 . VAL B 195 ? 0.11976 0.20998 0.15907 -0.02680 -0.00483 -0.00648 629 VAL B CG2 
4211 N N   . LEU B 196 ? 0.11090 0.22112 0.15001 -0.00424 -0.01056 -0.01179 630 LEU B N   
4212 C CA  . LEU B 196 ? 0.08711 0.20112 0.12524 0.00216  -0.01072 -0.01286 630 LEU B CA  
4213 C C   . LEU B 196 ? 0.13004 0.23151 0.16082 0.00263  -0.00876 -0.00976 630 LEU B C   
4214 O O   . LEU B 196 ? 0.10683 0.19507 0.13062 0.00301  -0.01054 -0.00829 630 LEU B O   
4215 C CB  . LEU B 196 ? 0.09166 0.20560 0.12704 0.01000  -0.01649 -0.01587 630 LEU B CB  
4216 C CG  . LEU B 196 ? 0.18162 0.29802 0.21510 0.01800  -0.01782 -0.01783 630 LEU B CG  
4217 C CD1 . LEU B 196 ? 0.09202 0.22757 0.13513 0.01836  -0.01487 -0.02059 630 LEU B CD1 
4218 C CD2 . LEU B 196 ? 0.19052 0.30204 0.21865 0.02596  -0.02440 -0.02023 630 LEU B CD2 
4219 N N   . TYR B 197 ? 0.08573 0.19206 0.11801 0.00242  -0.00506 -0.00901 631 TYR B N   
4220 C CA  . TYR B 197 ? 0.08599 0.18231 0.11193 0.00325  -0.00350 -0.00670 631 TYR B CA  
4221 C C   . TYR B 197 ? 0.19808 0.29576 0.22130 0.01071  -0.00522 -0.00895 631 TYR B C   
4222 O O   . TYR B 197 ? 0.15191 0.26227 0.17960 0.01343  -0.00403 -0.01122 631 TYR B O   
4223 C CB  . TYR B 197 ? 0.08453 0.18304 0.11191 -0.00191 0.00147  -0.00404 631 TYR B CB  
4224 C CG  . TYR B 197 ? 0.08519 0.17383 0.10607 -0.00073 0.00243  -0.00203 631 TYR B CG  
4225 C CD1 . TYR B 197 ? 0.10244 0.17850 0.11853 -0.00142 0.00073  -0.00086 631 TYR B CD1 
4226 C CD2 . TYR B 197 ? 0.17919 0.27212 0.19882 0.00111  0.00501  -0.00172 631 TYR B CD2 
4227 C CE1 . TYR B 197 ? 0.10862 0.17732 0.11988 -0.00040 0.00126  0.00024  631 TYR B CE1 
4228 C CE2 . TYR B 197 ? 0.10668 0.19113 0.12041 0.00252  0.00526  -0.00041 631 TYR B CE2 
4229 C CZ  . TYR B 197 ? 0.15707 0.22973 0.16716 0.00170  0.00322  0.00042  631 TYR B CZ  
4230 O OH  . TYR B 197 ? 0.14331 0.20911 0.14862 0.00299  0.00316  0.00105  631 TYR B OH  
4231 N N   . ILE B 198 ? 0.15916 0.24396 0.17501 0.01377  -0.00788 -0.00861 632 ILE B N   
4232 C CA  . ILE B 198 ? 0.09655 0.17892 0.10819 0.02071  -0.01008 -0.01079 632 ILE B CA  
4233 C C   . ILE B 198 ? 0.16087 0.23214 0.16661 0.01955  -0.00903 -0.00898 632 ILE B C   
4234 O O   . ILE B 198 ? 0.17980 0.24002 0.18161 0.01643  -0.00982 -0.00718 632 ILE B O   
4235 C CB  . ILE B 198 ? 0.11070 0.18663 0.11805 0.02603  -0.01558 -0.01276 632 ILE B CB  
4236 C CG1 . ILE B 198 ? 0.12689 0.21541 0.14063 0.02810  -0.01739 -0.01531 632 ILE B CG1 
4237 C CG2 . ILE B 198 ? 0.10979 0.18006 0.11144 0.03309  -0.01821 -0.01499 632 ILE B CG2 
4238 C CD1 . ILE B 198 ? 0.19676 0.27790 0.20514 0.03347  -0.02342 -0.01686 632 ILE B CD1 
4239 N N   . SER B 199 ? 0.14837 0.22349 0.15357 0.02211  -0.00728 -0.00986 633 SER B N   
4240 C CA  . SER B 199 ? 0.15761 0.22396 0.15782 0.02133  -0.00660 -0.00878 633 SER B CA  
4241 C C   . SER B 199 ? 0.13037 0.19465 0.12631 0.02791  -0.00876 -0.01187 633 SER B C   
4242 O O   . SER B 199 ? 0.15514 0.22977 0.15324 0.03218  -0.00789 -0.01418 633 SER B O   
4243 C CB  . SER B 199 ? 0.12746 0.19880 0.12967 0.01722  -0.00220 -0.00638 633 SER B CB  
4244 O OG  . SER B 199 ? 0.12276 0.18726 0.12022 0.01780  -0.00221 -0.00613 633 SER B OG  
4245 N N   . LEU B 200 ? 0.17791 0.22912 0.16784 0.02843  -0.01144 -0.01223 634 LEU B N   
4246 C CA  . LEU B 200 ? 0.16639 0.21281 0.15132 0.03338  -0.01345 -0.01506 634 LEU B CA  
4247 C C   . LEU B 200 ? 0.18986 0.23442 0.17349 0.03038  -0.01135 -0.01405 634 LEU B C   
4248 O O   . LEU B 200 ? 0.16773 0.20740 0.15170 0.02493  -0.01045 -0.01169 634 LEU B O   
4249 C CB  . LEU B 200 ? 0.12402 0.15582 0.10242 0.03524  -0.01808 -0.01628 634 LEU B CB  
4250 C CG  . LEU B 200 ? 0.12864 0.15852 0.10601 0.03853  -0.02135 -0.01692 634 LEU B CG  
4251 C CD1 . LEU B 200 ? 0.12528 0.15166 0.10348 0.03259  -0.02082 -0.01362 634 LEU B CD1 
4252 C CD2 . LEU B 200 ? 0.16745 0.18342 0.13631 0.04375  -0.02637 -0.01937 634 LEU B CD2 
4253 N N   . HIS B 201 ? 0.13295 0.18209 0.11496 0.03442  -0.01075 -0.01621 635 HIS B N   
4254 C CA  . HIS B 201 ? 0.13787 0.18682 0.11851 0.03211  -0.00891 -0.01519 635 HIS B CA  
4255 C C   . HIS B 201 ? 0.12950 0.18095 0.10620 0.03776  -0.00953 -0.01856 635 HIS B C   
4256 O O   . HIS B 201 ? 0.12218 0.18187 0.09938 0.04267  -0.00890 -0.02068 635 HIS B O   
4257 C CB  . HIS B 201 ? 0.10798 0.16517 0.09254 0.02787  -0.00461 -0.01148 635 HIS B CB  
4258 C CG  . HIS B 201 ? 0.20702 0.27675 0.19499 0.02951  -0.00180 -0.01145 635 HIS B CG  
4259 N ND1 . HIS B 201 ? 0.12262 0.19723 0.11558 0.02832  -0.00157 -0.01105 635 HIS B ND1 
4260 C CD2 . HIS B 201 ? 0.15320 0.23263 0.14045 0.03201  0.00103  -0.01210 635 HIS B CD2 
4261 C CE1 . HIS B 201 ? 0.17381 0.26146 0.17004 0.02968  0.00133  -0.01172 635 HIS B CE1 
4262 N NE2 . HIS B 201 ? 0.13956 0.23033 0.13216 0.03176  0.00328  -0.01219 635 HIS B NE2 
4263 N N   . ARG B 202 ? 0.12223 0.16753 0.09530 0.03715  -0.01083 -0.01951 636 ARG B N   
4264 C CA  . ARG B 202 ? 0.13772 0.18604 0.10659 0.04193  -0.01111 -0.02247 636 ARG B CA  
4265 C C   . ARG B 202 ? 0.14957 0.20992 0.11927 0.04204  -0.00652 -0.02014 636 ARG B C   
4266 O O   . ARG B 202 ? 0.24301 0.30508 0.21473 0.03719  -0.00389 -0.01602 636 ARG B O   
4267 C CB  . ARG B 202 ? 0.13001 0.17031 0.09566 0.04031  -0.01354 -0.02385 636 ARG B CB  
4268 C CG  . ARG B 202 ? 0.15531 0.19779 0.11578 0.04541  -0.01457 -0.02744 636 ARG B CG  
4269 C CD  . ARG B 202 ? 0.14087 0.17428 0.09862 0.04429  -0.01844 -0.03050 636 ARG B CD  
4270 N NE  . ARG B 202 ? 0.14877 0.18316 0.10092 0.05001  -0.02035 -0.03502 636 ARG B NE  
4271 C CZ  . ARG B 202 ? 0.15449 0.18250 0.10366 0.05013  -0.02408 -0.03892 636 ARG B CZ  
4272 N NH1 . ARG B 202 ? 0.15311 0.17411 0.10489 0.04442  -0.02602 -0.03893 636 ARG B NH1 
4273 N NH2 . ARG B 202 ? 0.29252 0.32205 0.23614 0.05592  -0.02582 -0.04330 636 ARG B NH2 
4274 N N   . TYR B 203 ? 0.15130 0.21957 0.11880 0.04755  -0.00547 -0.02284 637 TYR B N   
4275 C CA  . TYR B 203 ? 0.12863 0.20926 0.09667 0.04700  -0.00033 -0.02048 637 TYR B CA  
4276 C C   . TYR B 203 ? 0.14443 0.22872 0.10567 0.05126  0.00053  -0.02250 637 TYR B C   
4277 O O   . TYR B 203 ? 0.17610 0.26262 0.13405 0.04879  0.00343  -0.01911 637 TYR B O   
4278 C CB  . TYR B 203 ? 0.12727 0.21863 0.10059 0.04878  0.00160  -0.02158 637 TYR B CB  
4279 C CG  . TYR B 203 ? 0.12758 0.23342 0.10210 0.04750  0.00750  -0.01970 637 TYR B CG  
4280 C CD1 . TYR B 203 ? 0.14386 0.25077 0.11897 0.04056  0.01142  -0.01412 637 TYR B CD1 
4281 C CD2 . TYR B 203 ? 0.20227 0.32063 0.17711 0.05306  0.00928  -0.02368 637 TYR B CD2 
4282 C CE1 . TYR B 203 ? 0.14737 0.26634 0.12266 0.03822  0.01720  -0.01198 637 TYR B CE1 
4283 C CE2 . TYR B 203 ? 0.13300 0.26577 0.10905 0.05088  0.01543  -0.02198 637 TYR B CE2 
4284 C CZ  . TYR B 203 ? 0.15219 0.28466 0.12813 0.04296  0.01951  -0.01584 637 TYR B CZ  
4285 O OH  . TYR B 203 ? 0.13419 0.27968 0.11031 0.03968  0.02597  -0.01372 637 TYR B OH  
4286 N N   . GLU B 204 ? 0.14168 0.22573 0.09980 0.05800  -0.00225 -0.02807 638 GLU B N   
4287 C CA  . GLU B 204 ? 0.16920 0.25635 0.12009 0.06295  -0.00208 -0.03105 638 GLU B CA  
4288 C C   . GLU B 204 ? 0.22893 0.32945 0.17808 0.06226  0.00420  -0.02825 638 GLU B C   
4289 O O   . GLU B 204 ? 0.21445 0.31554 0.15667 0.06254  0.00561  -0.02699 638 GLU B O   
4290 C CB  . GLU B 204 ? 0.18183 0.25861 0.12788 0.06166  -0.00541 -0.03113 638 GLU B CB  
4291 C CG  . GLU B 204 ? 0.15056 0.21425 0.09861 0.06006  -0.01076 -0.03319 638 GLU B CG  
4292 C CD  . GLU B 204 ? 0.19548 0.25389 0.14091 0.06604  -0.01504 -0.03951 638 GLU B CD  
4293 O OE1 . GLU B 204 ? 0.24503 0.31097 0.18801 0.07236  -0.01408 -0.04286 638 GLU B OE1 
4294 O OE2 . GLU B 204 ? 0.19965 0.24601 0.14513 0.06434  -0.01936 -0.04128 638 GLU B OE2 
4295 N N   . ASP B 205 ? 0.21116 0.32252 0.16631 0.06111  0.00794  -0.02731 639 ASP B N   
4296 C CA  . ASP B 205 ? 0.14942 0.27470 0.10408 0.05896  0.01472  -0.02458 639 ASP B CA  
4297 C C   . ASP B 205 ? 0.23737 0.35816 0.18695 0.05282  0.01752  -0.01811 639 ASP B C   
4298 O O   . ASP B 205 ? 0.54014 0.66532 0.48206 0.05345  0.02090  -0.01672 639 ASP B O   
4299 C CB  . ASP B 205 ? 0.25039 0.38638 0.20027 0.06618  0.01641  -0.02966 639 ASP B CB  
4300 C CG  . ASP B 205 ? 0.44884 0.59651 0.40577 0.07098  0.01661  -0.03478 639 ASP B CG  
4301 O OD1 . ASP B 205 ? 0.37479 0.51596 0.33253 0.07704  0.01090  -0.03997 639 ASP B OD1 
4302 O OD2 . ASP B 205 ? 0.41245 0.57563 0.37417 0.06855  0.02230  -0.03370 639 ASP B OD2 
4303 N N   . GLY B 206 ? 0.18958 0.30097 0.14271 0.04722  0.01589  -0.01420 640 GLY B N   
4304 C CA  . GLY B 206 ? 0.24143 0.34760 0.19055 0.04160  0.01804  -0.00807 640 GLY B CA  
4305 C C   . GLY B 206 ? 0.26076 0.35610 0.20247 0.04352  0.01415  -0.00794 640 GLY B C   
4306 O O   . GLY B 206 ? 0.36944 0.45891 0.30752 0.03980  0.01486  -0.00313 640 GLY B O   
4307 N N   . ALA B 207 ? 0.27179 0.36412 0.21106 0.04933  0.00971  -0.01338 641 ALA B N   
4308 C CA  . ALA B 207 ? 0.18551 0.26929 0.11856 0.05118  0.00565  -0.01414 641 ALA B CA  
4309 C C   . ALA B 207 ? 0.21084 0.28475 0.14918 0.04786  0.00150  -0.01375 641 ALA B C   
4310 O O   . ALA B 207 ? 0.35998 0.42805 0.29472 0.04832  -0.00159 -0.01384 641 ALA B O   
4311 C CB  . ALA B 207 ? 0.23589 0.32024 0.16426 0.05817  0.00230  -0.02070 641 ALA B CB  
4312 N N   . PHE B 208 ? 0.18751 0.26020 0.13410 0.04477  0.00129  -0.01364 642 PHE B N   
4313 C CA  . PHE B 208 ? 0.24445 0.30879 0.19596 0.04125  -0.00195 -0.01340 642 PHE B CA  
4314 C C   . PHE B 208 ? 0.22449 0.28825 0.17936 0.03561  0.00087  -0.00789 642 PHE B C   
4315 O O   . PHE B 208 ? 0.27474 0.34411 0.23204 0.03339  0.00474  -0.00532 642 PHE B O   
4316 C CB  . PHE B 208 ? 0.15676 0.21807 0.11344 0.04164  -0.00454 -0.01699 642 PHE B CB  
4317 C CG  . PHE B 208 ? 0.18199 0.23431 0.14091 0.03932  -0.00864 -0.01876 642 PHE B CG  
4318 C CD1 . PHE B 208 ? 0.18666 0.23506 0.14204 0.04174  -0.01240 -0.02282 642 PHE B CD1 
4319 C CD2 . PHE B 208 ? 0.12342 0.17200 0.08800 0.03439  -0.00857 -0.01668 642 PHE B CD2 
4320 C CE1 . PHE B 208 ? 0.24776 0.28939 0.20598 0.03863  -0.01570 -0.02478 642 PHE B CE1 
4321 C CE2 . PHE B 208 ? 0.14251 0.18417 0.10914 0.03165  -0.01160 -0.01842 642 PHE B CE2 
4322 C CZ  . PHE B 208 ? 0.13952 0.17807 0.10335 0.03344  -0.01500 -0.02246 642 PHE B CZ  
4323 N N   . PHE B 209 ? 0.26118 0.31861 0.21637 0.03346  -0.00127 -0.00664 643 PHE B N   
4324 C CA  . PHE B 209 ? 0.23431 0.28936 0.19190 0.02876  0.00058  -0.00202 643 PHE B CA  
4325 C C   . PHE B 209 ? 0.18472 0.24183 0.14945 0.02506  0.00251  -0.00110 643 PHE B C   
4326 O O   . PHE B 209 ? 0.24204 0.29879 0.21062 0.02580  0.00064  -0.00432 643 PHE B O   
4327 C CB  . PHE B 209 ? 0.17034 0.21908 0.12939 0.02794  -0.00302 -0.00287 643 PHE B CB  
4328 C CG  . PHE B 209 ? 0.19109 0.23640 0.15190 0.02417  -0.00177 0.00113  643 PHE B CG  
4329 C CD1 . PHE B 209 ? 0.18441 0.22849 0.15223 0.02013  -0.00131 0.00143  643 PHE B CD1 
4330 C CD2 . PHE B 209 ? 0.13422 0.17653 0.08861 0.02496  -0.00132 0.00455  643 PHE B CD2 
4331 C CE1 . PHE B 209 ? 0.15687 0.19745 0.12598 0.01699  -0.00038 0.00453  643 PHE B CE1 
4332 C CE2 . PHE B 209 ? 0.19883 0.23634 0.15407 0.02189  -0.00060 0.00794  643 PHE B CE2 
4333 C CZ  . PHE B 209 ? 0.24047 0.27743 0.20348 0.01792  -0.00013 0.00766  643 PHE B CZ  
4334 N N   . PRO B 210 ? 0.21646 0.27500 0.18250 0.02101  0.00591  0.00314  644 PRO B N   
4335 C CA  . PRO B 210 ? 0.19237 0.24890 0.15299 0.01908  0.00834  0.00779  644 PRO B CA  
4336 C C   . PRO B 210 ? 0.15810 0.22069 0.11229 0.02038  0.01207  0.00948  644 PRO B C   
4337 O O   . PRO B 210 ? 0.21224 0.27342 0.16170 0.01735  0.01524  0.01411  644 PRO B O   
4338 C CB  . PRO B 210 ? 0.16531 0.22064 0.13129 0.01339  0.01028  0.01068  644 PRO B CB  
4339 C CG  . PRO B 210 ? 0.12527 0.18737 0.09812 0.01299  0.01084  0.00810  644 PRO B CG  
4340 C CD  . PRO B 210 ? 0.12962 0.19054 0.10277 0.01757  0.00709  0.00345  644 PRO B CD  
4341 N N   . ASN B 211 ? 0.13373 0.20267 0.08708 0.02471  0.01189  0.00571  645 ASN B N   
4342 C CA  . ASN B 211 ? 0.23229 0.30711 0.17796 0.02740  0.01484  0.00620  645 ASN B CA  
4343 C C   . ASN B 211 ? 0.22148 0.30466 0.16798 0.02306  0.02100  0.00954  645 ASN B C   
4344 O O   . ASN B 211 ? 0.20868 0.29329 0.14713 0.02195  0.02470  0.01302  645 ASN B O   
4345 C CB  . ASN B 211 ? 0.23556 0.30340 0.17104 0.02935  0.01340  0.00846  645 ASN B CB  
4346 C CG  . ASN B 211 ? 0.25325 0.31420 0.18947 0.03265  0.00729  0.00493  645 ASN B CG  
4347 O OD1 . ASN B 211 ? 0.29785 0.35154 0.23407 0.03119  0.00507  0.00677  645 ASN B OD1 
4348 N ND2 . ASN B 211 ? 0.30368 0.36712 0.24070 0.03705  0.00448  -0.00056 645 ASN B ND2 
4349 N N   . SER B 212 ? 0.20333 0.29253 0.15923 0.02045  0.02214  0.00831  646 SER B N   
4350 C CA  . SER B 212 ? 0.15552 0.25397 0.11435 0.01530  0.02779  0.01088  646 SER B CA  
4351 C C   . SER B 212 ? 0.13421 0.24557 0.10131 0.01766  0.02844  0.00608  646 SER B C   
4352 O O   . SER B 212 ? 0.12737 0.23671 0.09989 0.02080  0.02412  0.00230  646 SER B O   
4353 C CB  . SER B 212 ? 0.13725 0.22942 0.09986 0.00816  0.02842  0.01500  646 SER B CB  
4354 O OG  . SER B 212 ? 0.14015 0.24110 0.10565 0.00213  0.03390  0.01737  646 SER B OG  
4355 N N   . GLU B 213 ? 0.13854 0.26319 0.10619 0.01615  0.03387  0.00620  647 GLU B N   
4356 C CA  . GLU B 213 ? 0.17729 0.31636 0.15345 0.01893  0.03455  0.00116  647 GLU B CA  
4357 C C   . GLU B 213 ? 0.12701 0.26908 0.11369 0.01413  0.03417  0.00129  647 GLU B C   
4358 O O   . GLU B 213 ? 0.12328 0.27679 0.11771 0.01700  0.03362  -0.00323 647 GLU B O   
4359 C CB  . GLU B 213 ? 0.23090 0.38572 0.20506 0.01877  0.04092  0.00061  647 GLU B CB  
4360 C CG  . GLU B 213 ? 0.17327 0.32618 0.13608 0.02415  0.04133  -0.00002 647 GLU B CG  
4361 C CD  . GLU B 213 ? 0.21068 0.38127 0.17201 0.02550  0.04742  -0.00212 647 GLU B CD  
4362 O OE1 . GLU B 213 ? 0.24721 0.43040 0.21514 0.03115  0.04678  -0.00847 647 GLU B OE1 
4363 O OE2 . GLU B 213 ? 0.27782 0.44914 0.23091 0.02106  0.05272  0.00252  647 GLU B OE2 
4364 N N   . ASP B 214 ? 0.14066 0.27269 0.12743 0.00756  0.03401  0.00591  648 ASP B N   
4365 C CA  . ASP B 214 ? 0.11896 0.25164 0.11486 0.00358  0.03254  0.00557  648 ASP B CA  
4366 C C   . ASP B 214 ? 0.16547 0.29550 0.16561 0.00966  0.02663  0.00092  648 ASP B C   
4367 O O   . ASP B 214 ? 0.15339 0.28944 0.16147 0.00910  0.02533  -0.00134 648 ASP B O   
4368 C CB  . ASP B 214 ? 0.11978 0.23885 0.11317 -0.00284 0.03217  0.01065  648 ASP B CB  
4369 C CG  . ASP B 214 ? 0.17326 0.29260 0.16179 -0.00984 0.03778  0.01582  648 ASP B CG  
4370 O OD1 . ASP B 214 ? 0.14581 0.27844 0.13494 -0.01130 0.04276  0.01545  648 ASP B OD1 
4371 O OD2 . ASP B 214 ? 0.17410 0.28015 0.15775 -0.01383 0.03726  0.02015  648 ASP B OD2 
4372 N N   . ALA B 215 ? 0.12210 0.24269 0.11652 0.01524  0.02285  -0.00054 649 ALA B N   
4373 C CA  . ALA B 215 ? 0.14041 0.25572 0.13678 0.02035  0.01732  -0.00441 649 ALA B CA  
4374 C C   . ALA B 215 ? 0.10984 0.23564 0.10893 0.02720  0.01625  -0.00984 649 ALA B C   
4375 O O   . ALA B 215 ? 0.12778 0.24779 0.12711 0.03191  0.01137  -0.01303 649 ALA B O   
4376 C CB  . ALA B 215 ? 0.10994 0.21182 0.09941 0.02300  0.01388  -0.00439 649 ALA B CB  
4377 N N   . ASN B 216 ? 0.11305 0.25366 0.11367 0.02810  0.02054  -0.01116 650 ASN B N   
4378 C CA  . ASN B 216 ? 0.14384 0.29410 0.14652 0.03616  0.01890  -0.01722 650 ASN B CA  
4379 C C   . ASN B 216 ? 0.14675 0.30547 0.15865 0.03685  0.01711  -0.01996 650 ASN B C   
4380 O O   . ASN B 216 ? 0.12959 0.29100 0.14713 0.03013  0.01869  -0.01729 650 ASN B O   
4381 C CB  . ASN B 216 ? 0.12248 0.28726 0.12335 0.03790  0.02419  -0.01864 650 ASN B CB  
4382 C CG  . ASN B 216 ? 0.12557 0.29331 0.12332 0.04811  0.02137  -0.02492 650 ASN B CG  
4383 O OD1 . ASN B 216 ? 0.12529 0.28504 0.12318 0.05383  0.01536  -0.02841 650 ASN B OD1 
4384 N ND2 . ASN B 216 ? 0.20624 0.38456 0.20021 0.05047  0.02564  -0.02641 650 ASN B ND2 
4385 N N   . TYR B 217 ? 0.17460 0.33707 0.18749 0.04563  0.01329  -0.02575 651 TYR B N   
4386 C CA  . TYR B 217 ? 0.15247 0.32116 0.17267 0.04851  0.00991  -0.02910 651 TYR B CA  
4387 C C   . TYR B 217 ? 0.16575 0.35542 0.19601 0.04438  0.01461  -0.02989 651 TYR B C   
4388 O O   . TYR B 217 ? 0.10641 0.30082 0.14366 0.04376  0.01223  -0.03127 651 TYR B O   
4389 C CB  . TYR B 217 ? 0.11803 0.28657 0.13595 0.05995  0.00481  -0.03553 651 TYR B CB  
4390 C CG  . TYR B 217 ? 0.12281 0.30713 0.14104 0.06574  0.00804  -0.04013 651 TYR B CG  
4391 C CD1 . TYR B 217 ? 0.12246 0.32940 0.14988 0.06773  0.01076  -0.04424 651 TYR B CD1 
4392 C CD2 . TYR B 217 ? 0.14081 0.31843 0.15037 0.06936  0.00829  -0.04094 651 TYR B CD2 
4393 C CE1 . TYR B 217 ? 0.12879 0.34817 0.15544 0.07175  0.01346  -0.04806 651 TYR B CE1 
4394 C CE2 . TYR B 217 ? 0.14585 0.33811 0.15489 0.07496  0.01136  -0.04545 651 TYR B CE2 
4395 C CZ  . TYR B 217 ? 0.13421 0.34622 0.15149 0.07555  0.01381  -0.04858 651 TYR B CZ  
4396 O OH  . TYR B 217 ? 0.14855 0.37013 0.16394 0.07859  0.01558  -0.05177 651 TYR B OH  
4397 N N   . ASP B 218 ? 0.11361 0.31614 0.14444 0.04129  0.02121  -0.02919 652 ASP B N   
4398 C CA  . ASP B 218 ? 0.11241 0.33670 0.15308 0.03668  0.02641  -0.03046 652 ASP B CA  
4399 C C   . ASP B 218 ? 0.11597 0.33788 0.15988 0.02472  0.02973  -0.02469 652 ASP B C   
4400 O O   . ASP B 218 ? 0.10728 0.34498 0.15904 0.01878  0.03408  -0.02514 652 ASP B O   
4401 C CB  . ASP B 218 ? 0.15812 0.39372 0.19611 0.03685  0.03194  -0.03143 652 ASP B CB  
4402 C CG  . ASP B 218 ? 0.16467 0.39310 0.19458 0.02961  0.03754  -0.02489 652 ASP B CG  
4403 O OD1 . ASP B 218 ? 0.16653 0.37640 0.18836 0.03011  0.03473  -0.02158 652 ASP B OD1 
4404 O OD2 . ASP B 218 ? 0.15961 0.39541 0.18981 0.02270  0.04316  -0.02253 652 ASP B OD2 
4405 N N   . LYS B 219 ? 0.11653 0.31820 0.15427 0.02081  0.02754  -0.01957 653 LYS B N   
4406 C CA  . LYS B 219 ? 0.11076 0.30774 0.15095 0.01046  0.02957  -0.01466 653 LYS B CA  
4407 C C   . LYS B 219 ? 0.09773 0.29165 0.14370 0.01149  0.02392  -0.01669 653 LYS B C   
4408 O O   . LYS B 219 ? 0.09583 0.27293 0.13695 0.01325  0.01921  -0.01525 653 LYS B O   
4409 C CB  . LYS B 219 ? 0.10454 0.28257 0.13480 0.00651  0.03025  -0.00862 653 LYS B CB  
4410 C CG  . LYS B 219 ? 0.11532 0.29332 0.13717 0.00835  0.03395  -0.00719 653 LYS B CG  
4411 C CD  . LYS B 219 ? 0.11593 0.31048 0.14020 0.00287  0.04142  -0.00631 653 LYS B CD  
4412 C CE  . LYS B 219 ? 0.16999 0.36104 0.18332 0.00317  0.04536  -0.00329 653 LYS B CE  
4413 N NZ  . LYS B 219 ? 0.14864 0.34258 0.15789 0.01352  0.04319  -0.00804 653 LYS B NZ  
4414 N N   . VAL B 220 ? 0.09629 0.30766 0.15271 0.01047  0.02439  -0.02041 654 VAL B N   
4415 C CA  . VAL B 220 ? 0.09297 0.30396 0.15471 0.01304  0.01848  -0.02334 654 VAL B CA  
4416 C C   . VAL B 220 ? 0.09057 0.30031 0.15714 0.00324  0.01939  -0.02061 654 VAL B C   
4417 O O   . VAL B 220 ? 0.08835 0.29854 0.15932 0.00452  0.01464  -0.02299 654 VAL B O   
4418 C CB  . VAL B 220 ? 0.09732 0.32860 0.16764 0.02050  0.01656  -0.03062 654 VAL B CB  
4419 C CG1 . VAL B 220 ? 0.09741 0.32729 0.16194 0.03153  0.01440  -0.03401 654 VAL B CG1 
4420 C CG2 . VAL B 220 ? 0.09610 0.34690 0.17468 0.01376  0.02254  -0.03189 654 VAL B CG2 
4421 N N   . GLY B 221 ? 0.12741 0.33463 0.19242 -0.00622 0.02497  -0.01582 655 GLY B N   
4422 C CA  . GLY B 221 ? 0.10382 0.30868 0.17274 -0.01594 0.02598  -0.01337 655 GLY B CA  
4423 C C   . GLY B 221 ? 0.17431 0.39513 0.24985 -0.02505 0.03278  -0.01293 655 GLY B C   
4424 O O   . GLY B 221 ? 0.12747 0.36035 0.20418 -0.02335 0.03631  -0.01479 655 GLY B O   
4425 N N   . LEU B 222 ? 0.16332 0.37960 0.24119 -0.03480 0.03391  -0.01035 656 LEU B N   
4426 C CA  . LEU B 222 ? 0.19120 0.41218 0.27168 -0.04446 0.03902  -0.00894 656 LEU B CA  
4427 C C   . LEU B 222 ? 0.13756 0.36294 0.22686 -0.04924 0.03622  -0.01200 656 LEU B C   
4428 O O   . LEU B 222 ? 0.17519 0.39231 0.26494 -0.04981 0.03199  -0.01185 656 LEU B O   
4429 C CB  . LEU B 222 ? 0.23001 0.43513 0.30114 -0.05267 0.04342  -0.00169 656 LEU B CB  
4430 C CG  . LEU B 222 ? 0.16278 0.35641 0.22247 -0.04888 0.04479  0.00276  656 LEU B CG  
4431 C CD1 . LEU B 222 ? 0.31724 0.49065 0.36792 -0.05636 0.04622  0.00930  656 LEU B CD1 
4432 C CD2 . LEU B 222 ? 0.28954 0.49170 0.34567 -0.04568 0.04914  0.00256  656 LEU B CD2 
4433 N N   . GLY B 223 ? 0.15353 0.39219 0.24963 -0.05275 0.03858  -0.01494 657 GLY B N   
4434 C CA  . GLY B 223 ? 0.11561 0.35858 0.21981 -0.05859 0.03663  -0.01765 657 GLY B CA  
4435 C C   . GLY B 223 ? 0.22674 0.47287 0.33593 -0.05157 0.02917  -0.02254 657 GLY B C   
4436 O O   . GLY B 223 ? 0.17834 0.43330 0.28941 -0.04145 0.02579  -0.02676 657 GLY B O   
4437 N N   . LYS B 224 ? 0.20702 0.44470 0.31742 -0.05664 0.02623  -0.02202 658 LYS B N   
4438 C CA  . LYS B 224 ? 0.16009 0.39858 0.27356 -0.05045 0.01891  -0.02609 658 LYS B CA  
4439 C C   . LYS B 224 ? 0.26387 0.49578 0.37129 -0.04102 0.01551  -0.02528 658 LYS B C   
4440 O O   . LYS B 224 ? 0.25060 0.48602 0.35968 -0.03269 0.00941  -0.02926 658 LYS B O   
4441 C CB  . LYS B 224 ? 0.15541 0.38323 0.26906 -0.05794 0.01676  -0.02501 658 LYS B CB  
4442 C CG  . LYS B 224 ? 0.27009 0.50567 0.39131 -0.06580 0.01791  -0.02754 658 LYS B CG  
4443 C CD  . LYS B 224 ? 0.43979 0.66098 0.55892 -0.07402 0.01673  -0.02545 658 LYS B CD  
4444 C CE  . LYS B 224 ? 0.47106 0.70076 0.59869 -0.07986 0.01555  -0.02953 658 LYS B CE  
4445 N NZ  . LYS B 224 ? 0.13356 0.37466 0.26715 -0.07215 0.00887  -0.03592 658 LYS B NZ  
4446 N N   . GLY B 225 ? 0.16380 0.38558 0.26361 -0.04201 0.01910  -0.02015 659 GLY B N   
4447 C CA  . GLY B 225 ? 0.16401 0.37326 0.25485 -0.03280 0.01601  -0.01864 659 GLY B CA  
4448 C C   . GLY B 225 ? 0.08757 0.30691 0.17850 -0.02346 0.01603  -0.02140 659 GLY B C   
4449 O O   . GLY B 225 ? 0.11258 0.31972 0.19527 -0.01551 0.01294  -0.02051 659 GLY B O   
4450 N N   . ARG B 226 ? 0.13434 0.37266 0.23278 -0.02400 0.01918  -0.02481 660 ARG B N   
4451 C CA  . ARG B 226 ? 0.14342 0.39056 0.24123 -0.01428 0.01880  -0.02822 660 ARG B CA  
4452 C C   . ARG B 226 ? 0.12337 0.37068 0.22160 -0.00295 0.01096  -0.03273 660 ARG B C   
4453 O O   . ARG B 226 ? 0.18836 0.43898 0.29130 -0.00212 0.00628  -0.03598 660 ARG B O   
4454 C CB  . ARG B 226 ? 0.13587 0.39881 0.23972 -0.01670 0.02241  -0.03148 660 ARG B CB  
4455 C CG  . ARG B 226 ? 0.14110 0.40410 0.24102 -0.02312 0.03012  -0.02741 660 ARG B CG  
4456 C CD  . ARG B 226 ? 0.23337 0.51137 0.34019 -0.02863 0.03406  -0.02997 660 ARG B CD  
4457 N NE  . ARG B 226 ? 0.48881 0.78202 0.60330 -0.02128 0.02976  -0.03739 660 ARG B NE  
4458 C CZ  . ARG B 226 ? 0.40356 0.70466 0.51724 -0.01092 0.02801  -0.04168 660 ARG B CZ  
4459 N NH1 . ARG B 226 ? 0.26116 0.55669 0.36701 -0.00637 0.02993  -0.03958 660 ARG B NH1 
4460 N NH2 . ARG B 226 ? 0.11486 0.42912 0.23518 -0.00464 0.02388  -0.04852 660 ARG B NH2 
4461 N N   . GLY B 227 ? 0.08617 0.32586 0.17700 0.00597  0.00908  -0.03258 661 GLY B N   
4462 C CA  . GLY B 227 ? 0.08729 0.31870 0.17367 0.01656  0.00140  -0.03533 661 GLY B CA  
4463 C C   . GLY B 227 ? 0.08719 0.29360 0.16306 0.01588  -0.00209 -0.03072 661 GLY B C   
4464 O O   . GLY B 227 ? 0.09002 0.28514 0.15885 0.02410  -0.00756 -0.03164 661 GLY B O   
4465 N N   . TYR B 228 ? 0.08520 0.28240 0.15940 0.00626  0.00103  -0.02592 662 TYR B N   
4466 C CA  . TYR B 228 ? 0.08497 0.26097 0.15055 0.00496  -0.00182 -0.02215 662 TYR B CA  
4467 C C   . TYR B 228 ? 0.10617 0.26706 0.16278 0.00358  0.00117  -0.01738 662 TYR B C   
4468 O O   . TYR B 228 ? 0.09724 0.24364 0.14875 -0.00073 0.00117  -0.01373 662 TYR B O   
4469 C CB  . TYR B 228 ? 0.21421 0.38968 0.28387 -0.00354 -0.00161 -0.02108 662 TYR B CB  
4470 C CG  . TYR B 228 ? 0.18020 0.36811 0.25748 -0.00148 -0.00614 -0.02611 662 TYR B CG  
4471 C CD1 . TYR B 228 ? 0.13323 0.34320 0.22234 -0.00403 -0.00415 -0.03013 662 TYR B CD1 
4472 C CD2 . TYR B 228 ? 0.26721 0.44540 0.33959 0.00298  -0.01245 -0.02703 662 TYR B CD2 
4473 C CE1 . TYR B 228 ? 0.20762 0.43038 0.30443 -0.00173 -0.00889 -0.03543 662 TYR B CE1 
4474 C CE2 . TYR B 228 ? 0.14997 0.33930 0.22844 0.00558  -0.01729 -0.03180 662 TYR B CE2 
4475 C CZ  . TYR B 228 ? 0.13463 0.34655 0.22574 0.00347  -0.01576 -0.03622 662 TYR B CZ  
4476 O OH  . TYR B 228 ? 0.43048 0.65481 0.52835 0.00646  -0.02111 -0.04161 662 TYR B OH  
4477 N N   . ASN B 229 ? 0.08631 0.25112 0.14100 0.00770  0.00342  -0.01791 663 ASN B N   
4478 C CA  . ASN B 229 ? 0.08716 0.23875 0.13313 0.00803  0.00530  -0.01436 663 ASN B CA  
4479 C C   . ASN B 229 ? 0.11701 0.26976 0.15949 0.01748  0.00314  -0.01752 663 ASN B C   
4480 O O   . ASN B 229 ? 0.12901 0.29676 0.17574 0.02041  0.00535  -0.02053 663 ASN B O   
4481 C CB  . ASN B 229 ? 0.08768 0.24292 0.13413 0.00091  0.01177  -0.01097 663 ASN B CB  
4482 C CG  . ASN B 229 ? 0.08881 0.22850 0.12603 0.00032  0.01287  -0.00691 663 ASN B CG  
4483 O OD1 . ASN B 229 ? 0.15249 0.27980 0.18653 -0.00390 0.01233  -0.00377 663 ASN B OD1 
4484 N ND2 . ASN B 229 ? 0.09118 0.23222 0.12421 0.00495  0.01418  -0.00748 663 ASN B ND2 
4485 N N   . VAL B 230 ? 0.18244 0.31959 0.21711 0.02203  -0.00108 -0.01715 664 VAL B N   
4486 C CA  . VAL B 230 ? 0.18912 0.32394 0.21933 0.03123  -0.00435 -0.02045 664 VAL B CA  
4487 C C   . VAL B 230 ? 0.11229 0.23401 0.13431 0.03119  -0.00332 -0.01804 664 VAL B C   
4488 O O   . VAL B 230 ? 0.09830 0.20467 0.11477 0.02904  -0.00518 -0.01550 664 VAL B O   
4489 C CB  . VAL B 230 ? 0.10093 0.22772 0.12810 0.03689  -0.01101 -0.02260 664 VAL B CB  
4490 C CG1 . VAL B 230 ? 0.10816 0.23140 0.13011 0.04667  -0.01471 -0.02627 664 VAL B CG1 
4491 C CG2 . VAL B 230 ? 0.09961 0.23957 0.13496 0.03682  -0.01264 -0.02514 664 VAL B CG2 
4492 N N   . ASN B 231 ? 0.09990 0.22860 0.12124 0.03358  -0.00034 -0.01920 665 ASN B N   
4493 C CA  . ASN B 231 ? 0.13684 0.25507 0.15061 0.03444  0.00021  -0.01783 665 ASN B CA  
4494 C C   . ASN B 231 ? 0.18332 0.29773 0.19234 0.04356  -0.00385 -0.02222 665 ASN B C   
4495 O O   . ASN B 231 ? 0.11147 0.23817 0.12345 0.04952  -0.00392 -0.02644 665 ASN B O   
4496 C CB  . ASN B 231 ? 0.10162 0.22832 0.11572 0.03096  0.00609  -0.01591 665 ASN B CB  
4497 C CG  . ASN B 231 ? 0.09825 0.21988 0.11237 0.02223  0.00914  -0.01065 665 ASN B CG  
4498 O OD1 . ASN B 231 ? 0.09640 0.20516 0.10794 0.01976  0.00684  -0.00854 665 ASN B OD1 
4499 N ND2 . ASN B 231 ? 0.09869 0.23015 0.11522 0.01750  0.01441  -0.00863 665 ASN B ND2 
4500 N N   . ILE B 232 ? 0.11309 0.21073 0.11487 0.04451  -0.00719 -0.02156 666 ILE B N   
4501 C CA  . ILE B 232 ? 0.12989 0.21995 0.12560 0.05233  -0.01147 -0.02549 666 ILE B CA  
4502 C C   . ILE B 232 ? 0.21631 0.30055 0.20657 0.05184  -0.01012 -0.02512 666 ILE B C   
4503 O O   . ILE B 232 ? 0.18736 0.25768 0.17302 0.04866  -0.01175 -0.02328 666 ILE B O   
4504 C CB  . ILE B 232 ? 0.12493 0.19921 0.11588 0.05348  -0.01697 -0.02538 666 ILE B CB  
4505 C CG1 . ILE B 232 ? 0.12334 0.20406 0.11931 0.05393  -0.01850 -0.02559 666 ILE B CG1 
4506 C CG2 . ILE B 232 ? 0.13591 0.20025 0.11962 0.06142  -0.02180 -0.02943 666 ILE B CG2 
4507 C CD1 . ILE B 232 ? 0.12991 0.19489 0.11975 0.05509  -0.02383 -0.02497 666 ILE B CD1 
4508 N N   . PRO B 233 ? 0.12291 0.21831 0.11354 0.05470  -0.00705 -0.02701 667 PRO B N   
4509 C CA  . PRO B 233 ? 0.15970 0.25053 0.14478 0.05408  -0.00575 -0.02650 667 PRO B CA  
4510 C C   . PRO B 233 ? 0.14146 0.22252 0.11973 0.06084  -0.01033 -0.03103 667 PRO B C   
4511 O O   . PRO B 233 ? 0.13963 0.22535 0.11735 0.06844  -0.01227 -0.03577 667 PRO B O   
4512 C CB  . PRO B 233 ? 0.19570 0.30316 0.18315 0.05413  -0.00020 -0.02643 667 PRO B CB  
4513 C CG  . PRO B 233 ? 0.12830 0.24909 0.12146 0.05899  -0.00026 -0.03022 667 PRO B CG  
4514 C CD  . PRO B 233 ? 0.12219 0.23663 0.11879 0.05757  -0.00395 -0.02941 667 PRO B CD  
4515 N N   . TRP B 234 ? 0.15404 0.22192 0.12729 0.05823  -0.01225 -0.03011 668 TRP B N   
4516 C CA  . TRP B 234 ? 0.14488 0.20294 0.11140 0.06351  -0.01645 -0.03455 668 TRP B CA  
4517 C C   . TRP B 234 ? 0.16704 0.23175 0.13036 0.06593  -0.01426 -0.03633 668 TRP B C   
4518 O O   . TRP B 234 ? 0.14366 0.21247 0.10752 0.06120  -0.01073 -0.03285 668 TRP B O   
4519 C CB  . TRP B 234 ? 0.21837 0.25926 0.18136 0.05893  -0.01985 -0.03338 668 TRP B CB  
4520 C CG  . TRP B 234 ? 0.26856 0.30128 0.23270 0.05613  -0.02189 -0.03126 668 TRP B CG  
4521 C CD1 . TRP B 234 ? 0.14104 0.16848 0.10711 0.04852  -0.02091 -0.02710 668 TRP B CD1 
4522 C CD2 . TRP B 234 ? 0.20449 0.23345 0.16710 0.06146  -0.02544 -0.03339 668 TRP B CD2 
4523 N NE1 . TRP B 234 ? 0.19825 0.21873 0.16352 0.04833  -0.02333 -0.02625 668 TRP B NE1 
4524 C CE2 . TRP B 234 ? 0.20429 0.22506 0.16718 0.05633  -0.02639 -0.02990 668 TRP B CE2 
4525 C CE3 . TRP B 234 ? 0.20149 0.23334 0.16211 0.07071  -0.02816 -0.03822 668 TRP B CE3 
4526 C CZ2 . TRP B 234 ? 0.17162 0.18608 0.13198 0.06005  -0.03019 -0.03062 668 TRP B CZ2 
4527 C CZ3 . TRP B 234 ? 0.16782 0.19366 0.12667 0.07488  -0.03223 -0.03927 668 TRP B CZ3 
4528 C CH2 . TRP B 234 ? 0.18642 0.20319 0.14473 0.06952  -0.03333 -0.03526 668 TRP B CH2 
4529 N N   . ASN B 235 ? 0.20818 0.27356 0.16736 0.07385  -0.01659 -0.04191 669 ASN B N   
4530 C CA  . ASN B 235 ? 0.16066 0.23011 0.11485 0.07721  -0.01559 -0.04465 669 ASN B CA  
4531 C C   . ASN B 235 ? 0.18530 0.24057 0.13272 0.08177  -0.02156 -0.04992 669 ASN B C   
4532 O O   . ASN B 235 ? 0.19360 0.23893 0.13978 0.08474  -0.02595 -0.05233 669 ASN B O   
4533 C CB  . ASN B 235 ? 0.16236 0.24946 0.11777 0.08298  -0.01179 -0.04727 669 ASN B CB  
4534 C CG  . ASN B 235 ? 0.15344 0.25484 0.11560 0.07762  -0.00560 -0.04233 669 ASN B CG  
4535 O OD1 . ASN B 235 ? 0.14975 0.25387 0.11110 0.07200  -0.00171 -0.03784 669 ASN B OD1 
4536 N ND2 . ASN B 235 ? 0.17448 0.28476 0.14300 0.07949  -0.00501 -0.04339 669 ASN B ND2 
4537 N N   . GLY B 236 ? 0.17532 0.22881 0.11766 0.08229  -0.02204 -0.05176 670 GLY B N   
4538 C CA  . GLY B 236 ? 0.26367 0.30460 0.19941 0.08653  -0.02767 -0.05754 670 GLY B CA  
4539 C C   . GLY B 236 ? 0.29649 0.32097 0.23108 0.08018  -0.03150 -0.05659 670 GLY B C   
4540 O O   . GLY B 236 ? 0.24316 0.25381 0.17311 0.08243  -0.03669 -0.06079 670 GLY B O   
4541 N N   . GLY B 237 ? 0.19345 0.21887 0.13197 0.07220  -0.02911 -0.05146 671 GLY B N   
4542 C CA  . GLY B 237 ? 0.26688 0.27995 0.20497 0.06595  -0.03211 -0.05131 671 GLY B CA  
4543 C C   . GLY B 237 ? 0.25139 0.25215 0.19081 0.06148  -0.03413 -0.04952 671 GLY B C   
4544 O O   . GLY B 237 ? 0.22707 0.23078 0.17000 0.06060  -0.03208 -0.04593 671 GLY B O   
4545 N N   . LYS B 238 ? 0.30861 0.29524 0.24454 0.05851  -0.03826 -0.05226 672 LYS B N   
4546 C CA  . LYS B 238 ? 0.37640 0.35089 0.31297 0.05149  -0.03938 -0.04968 672 LYS B CA  
4547 C C   . LYS B 238 ? 0.24109 0.20956 0.17563 0.05459  -0.04038 -0.04827 672 LYS B C   
4548 O O   . LYS B 238 ? 0.27379 0.23709 0.20310 0.06211  -0.04363 -0.05211 672 LYS B O   
4549 C CB  . LYS B 238 ? 0.20309 0.16318 0.13514 0.04800  -0.04372 -0.05374 672 LYS B CB  
4550 C CG  . LYS B 238 ? 0.30582 0.25707 0.23977 0.03792  -0.04342 -0.05088 672 LYS B CG  
4551 C CD  . LYS B 238 ? 0.48496 0.42380 0.41522 0.03344  -0.04727 -0.05538 672 LYS B CD  
4552 C CE  . LYS B 238 ? 0.53890 0.46242 0.45991 0.03922  -0.05225 -0.05969 672 LYS B CE  
4553 N NZ  . LYS B 238 ? 0.52330 0.42966 0.43973 0.03222  -0.05584 -0.06259 672 LYS B NZ  
4554 N N   . MET B 239 ? 0.18804 0.15725 0.12644 0.04931  -0.03796 -0.04312 673 MET B N   
4555 C CA  . MET B 239 ? 0.19242 0.15486 0.12856 0.05115  -0.03933 -0.04129 673 MET B CA  
4556 C C   . MET B 239 ? 0.24574 0.19510 0.17999 0.04251  -0.03980 -0.03805 673 MET B C   
4557 O O   . MET B 239 ? 0.28532 0.23691 0.22339 0.03480  -0.03741 -0.03631 673 MET B O   
4558 C CB  . MET B 239 ? 0.21943 0.19726 0.16190 0.05340  -0.03566 -0.03818 673 MET B CB  
4559 C CG  . MET B 239 ? 0.17729 0.17037 0.12219 0.06068  -0.03391 -0.04082 673 MET B CG  
4560 S SD  . MET B 239 ? 0.19183 0.18022 0.13050 0.07232  -0.03877 -0.04698 673 MET B SD  
4561 C CE  . MET B 239 ? 0.20183 0.20980 0.14341 0.07803  -0.03517 -0.05006 673 MET B CE  
4562 N N   . GLY B 240 ? 0.25550 0.19152 0.18341 0.04411  -0.04288 -0.03734 674 GLY B N   
4563 C CA  . GLY B 240 ? 0.21238 0.13472 0.13652 0.03582  -0.04312 -0.03404 674 GLY B CA  
4564 C C   . GLY B 240 ? 0.25915 0.17552 0.17957 0.03732  -0.04415 -0.03063 674 GLY B C   
4565 O O   . GLY B 240 ? 0.25901 0.18690 0.18342 0.04317  -0.04343 -0.03006 674 GLY B O   
4566 N N   . ASP B 241 ? 0.29961 0.19809 0.21203 0.03167  -0.04582 -0.02842 675 ASP B N   
4567 C CA  . ASP B 241 ? 0.23604 0.12599 0.14249 0.03290  -0.04743 -0.02494 675 ASP B CA  
4568 C C   . ASP B 241 ? 0.29444 0.18400 0.19746 0.04496  -0.05184 -0.02727 675 ASP B C   
4569 O O   . ASP B 241 ? 0.28746 0.18516 0.19325 0.04803  -0.05139 -0.02522 675 ASP B O   
4570 C CB  . ASP B 241 ? 0.25437 0.12117 0.14932 0.02579  -0.04935 -0.02280 675 ASP B CB  
4571 C CG  . ASP B 241 ? 0.27079 0.14025 0.16973 0.01341  -0.04437 -0.01992 675 ASP B CG  
4572 O OD1 . ASP B 241 ? 0.25831 0.14666 0.16864 0.01109  -0.03997 -0.01959 675 ASP B OD1 
4573 O OD2 . ASP B 241 ? 0.30662 0.15895 0.19686 0.00600  -0.04486 -0.01809 675 ASP B OD2 
4574 N N   . PRO B 242 ? 0.26542 0.14653 0.16272 0.05242  -0.05638 -0.03198 676 PRO B N   
4575 C CA  . PRO B 242 ? 0.26857 0.14987 0.16265 0.06473  -0.06093 -0.03470 676 PRO B CA  
4576 C C   . PRO B 242 ? 0.28317 0.19036 0.18927 0.07017  -0.05780 -0.03583 676 PRO B C   
4577 O O   . PRO B 242 ? 0.29548 0.20786 0.20241 0.07608  -0.05950 -0.03551 676 PRO B O   
4578 C CB  . PRO B 242 ? 0.27844 0.14775 0.16542 0.07099  -0.06563 -0.04038 676 PRO B CB  
4579 C CG  . PRO B 242 ? 0.28526 0.13998 0.16772 0.06048  -0.06491 -0.03936 676 PRO B CG  
4580 C CD  . PRO B 242 ? 0.26500 0.13566 0.15818 0.05051  -0.05813 -0.03564 676 PRO B CD  
4581 N N   . GLU B 243 ? 0.27237 0.19586 0.18747 0.06802  -0.05332 -0.03715 677 GLU B N   
4582 C CA  . GLU B 243 ? 0.21482 0.16231 0.14072 0.07158  -0.04957 -0.03770 677 GLU B CA  
4583 C C   . GLU B 243 ? 0.23230 0.18805 0.16406 0.06603  -0.04631 -0.03270 677 GLU B C   
4584 O O   . GLU B 243 ? 0.19715 0.16666 0.13461 0.07053  -0.04575 -0.03309 677 GLU B O   
4585 C CB  . GLU B 243 ? 0.23070 0.19065 0.16262 0.06923  -0.04542 -0.03917 677 GLU B CB  
4586 C CG  . GLU B 243 ? 0.21462 0.17091 0.14186 0.07632  -0.04843 -0.04511 677 GLU B CG  
4587 C CD  . GLU B 243 ? 0.32467 0.25810 0.24209 0.07364  -0.05271 -0.04647 677 GLU B CD  
4588 O OE1 . GLU B 243 ? 0.33648 0.26183 0.25327 0.06375  -0.05125 -0.04286 677 GLU B OE1 
4589 O OE2 . GLU B 243 ? 0.24500 0.16868 0.15536 0.08132  -0.05752 -0.05147 677 GLU B OE2 
4590 N N   . TYR B 244 ? 0.25616 0.20436 0.18686 0.05621  -0.04417 -0.02847 678 TYR B N   
4591 C CA  . TYR B 244 ? 0.19016 0.14577 0.12596 0.05091  -0.04109 -0.02416 678 TYR B CA  
4592 C C   . TYR B 244 ? 0.21072 0.15675 0.14005 0.05403  -0.04511 -0.02276 678 TYR B C   
4593 O O   . TYR B 244 ? 0.29621 0.25338 0.23079 0.05525  -0.04427 -0.02160 678 TYR B O   
4594 C CB  . TYR B 244 ? 0.18496 0.13723 0.12202 0.04014  -0.03739 -0.02083 678 TYR B CB  
4595 C CG  . TYR B 244 ? 0.21807 0.18575 0.16420 0.03747  -0.03283 -0.02118 678 TYR B CG  
4596 C CD1 . TYR B 244 ? 0.24868 0.21753 0.19460 0.03977  -0.03313 -0.02452 678 TYR B CD1 
4597 C CD2 . TYR B 244 ? 0.18105 0.16113 0.13491 0.03309  -0.02861 -0.01827 678 TYR B CD2 
4598 C CE1 . TYR B 244 ? 0.16030 0.14217 0.11284 0.03795  -0.02939 -0.02457 678 TYR B CE1 
4599 C CE2 . TYR B 244 ? 0.16442 0.15642 0.12485 0.03113  -0.02490 -0.01824 678 TYR B CE2 
4600 C CZ  . TYR B 244 ? 0.18908 0.18191 0.14850 0.03370  -0.02533 -0.02122 678 TYR B CZ  
4601 O OH  . TYR B 244 ? 0.13921 0.14279 0.10355 0.03225  -0.02204 -0.02091 678 TYR B OH  
4602 N N   . MET B 245 ? 0.21898 0.14380 0.13628 0.05536  -0.04977 -0.02292 679 MET B N   
4603 C CA  . MET B 245 ? 0.23154 0.14525 0.14040 0.05999  -0.05460 -0.02177 679 MET B CA  
4604 C C   . MET B 245 ? 0.26224 0.18808 0.17502 0.07176  -0.05785 -0.02582 679 MET B C   
4605 O O   . MET B 245 ? 0.27785 0.20870 0.19163 0.07482  -0.05955 -0.02492 679 MET B O   
4606 C CB  . MET B 245 ? 0.30697 0.19370 0.20066 0.05985  -0.05934 -0.02142 679 MET B CB  
4607 C CG  . MET B 245 ? 0.44796 0.32238 0.33706 0.04739  -0.05617 -0.01730 679 MET B CG  
4608 S SD  . MET B 245 ? 0.44515 0.31744 0.33123 0.04086  -0.05423 -0.01135 679 MET B SD  
4609 C CE  . MET B 245 ? 0.28218 0.13183 0.15113 0.04949  -0.06241 -0.01074 679 MET B CE  
4610 N N   . ALA B 246 ? 0.23195 0.16382 0.14729 0.07856  -0.05877 -0.03078 680 ALA B N   
4611 C CA  . ALA B 246 ? 0.23171 0.17770 0.15183 0.08992  -0.06135 -0.03551 680 ALA B CA  
4612 C C   . ALA B 246 ? 0.25617 0.22820 0.19049 0.08780  -0.05619 -0.03497 680 ALA B C   
4613 O O   . ALA B 246 ? 0.25234 0.23617 0.19111 0.09446  -0.05825 -0.03724 680 ALA B O   
4614 C CB  . ALA B 246 ? 0.25382 0.20086 0.17306 0.09723  -0.06286 -0.04125 680 ALA B CB  
4615 N N   . ALA B 247 ? 0.23966 0.22063 0.18106 0.07859  -0.04978 -0.03219 681 ALA B N   
4616 C CA  . ALA B 247 ? 0.18066 0.18368 0.13432 0.07542  -0.04480 -0.03116 681 ALA B CA  
4617 C C   . ALA B 247 ? 0.22774 0.23030 0.18209 0.07199  -0.04551 -0.02784 681 ALA B C   
4618 O O   . ALA B 247 ? 0.20174 0.22051 0.16411 0.07422  -0.04499 -0.02906 681 ALA B O   
4619 C CB  . ALA B 247 ? 0.20182 0.21115 0.16074 0.06697  -0.03856 -0.02880 681 ALA B CB  
4620 N N   . PHE B 248 ? 0.19603 0.18082 0.14205 0.06623  -0.04657 -0.02390 682 PHE B N   
4621 C CA  . PHE B 248 ? 0.24730 0.22984 0.19179 0.06366  -0.04776 -0.02096 682 PHE B CA  
4622 C C   . PHE B 248 ? 0.22237 0.20308 0.16259 0.07375  -0.05433 -0.02371 682 PHE B C   
4623 O O   . PHE B 248 ? 0.20907 0.19972 0.15379 0.07479  -0.05524 -0.02371 682 PHE B O   
4624 C CB  . PHE B 248 ? 0.21452 0.17772 0.14935 0.05581  -0.04741 -0.01651 682 PHE B CB  
4625 C CG  . PHE B 248 ? 0.17975 0.14967 0.12104 0.04555  -0.04132 -0.01327 682 PHE B CG  
4626 C CD1 . PHE B 248 ? 0.22441 0.20764 0.17522 0.04273  -0.03658 -0.01408 682 PHE B CD1 
4627 C CD2 . PHE B 248 ? 0.20846 0.17084 0.14537 0.03918  -0.04051 -0.00955 682 PHE B CD2 
4628 C CE1 . PHE B 248 ? 0.19063 0.17891 0.14666 0.03431  -0.03167 -0.01138 682 PHE B CE1 
4629 C CE2 . PHE B 248 ? 0.22069 0.18943 0.16354 0.03064  -0.03522 -0.00727 682 PHE B CE2 
4630 C CZ  . PHE B 248 ? 0.22037 0.20169 0.17285 0.02848  -0.03107 -0.00825 682 PHE B CZ  
4631 N N   . HIS B 249 ? 0.24128 0.20938 0.17277 0.08172  -0.05942 -0.02653 683 HIS B N   
4632 C CA  . HIS B 249 ? 0.22631 0.18988 0.15188 0.09257  -0.06674 -0.02934 683 HIS B CA  
4633 C C   . HIS B 249 ? 0.25266 0.24164 0.19095 0.10031  -0.06696 -0.03467 683 HIS B C   
4634 O O   . HIS B 249 ? 0.35677 0.35393 0.29782 0.10428  -0.07001 -0.03575 683 HIS B O   
4635 C CB  . HIS B 249 ? 0.24671 0.18824 0.15877 0.09920  -0.07234 -0.03118 683 HIS B CB  
4636 C CG  . HIS B 249 ? 0.32749 0.26121 0.23140 0.11152  -0.08081 -0.03415 683 HIS B CG  
4637 N ND1 . HIS B 249 ? 0.34786 0.28900 0.25402 0.12403  -0.08496 -0.04083 683 HIS B ND1 
4638 C CD2 . HIS B 249 ? 0.31423 0.23332 0.20713 0.11388  -0.08621 -0.03157 683 HIS B CD2 
4639 C CE1 . HIS B 249 ? 0.28678 0.21893 0.18479 0.13083  -0.09068 -0.04271 683 HIS B CE1 
4640 N NE2 . HIS B 249 ? 0.29255 0.21060 0.18198 0.12572  -0.09217 -0.03694 683 HIS B NE2 
4641 N N   . HIS B 250 ? 0.27511 0.27770 0.22128 0.10234  -0.06364 -0.03829 684 HIS B N   
4642 C CA  . HIS B 250 ? 0.20383 0.23107 0.16160 0.10987  -0.06351 -0.04396 684 HIS B CA  
4643 C C   . HIS B 250 ? 0.18488 0.23539 0.15705 0.10207  -0.05694 -0.04260 684 HIS B C   
4644 O O   . HIS B 250 ? 0.18036 0.25188 0.16261 0.10670  -0.05714 -0.04674 684 HIS B O   
4645 C CB  . HIS B 250 ? 0.20595 0.23824 0.16491 0.11592  -0.06264 -0.04882 684 HIS B CB  
4646 C CG  . HIS B 250 ? 0.22627 0.23751 0.17193 0.12545  -0.06985 -0.05173 684 HIS B CG  
4647 N ND1 . HIS B 250 ? 0.23916 0.25184 0.18222 0.13602  -0.07507 -0.05738 684 HIS B ND1 
4648 C CD2 . HIS B 250 ? 0.24072 0.22791 0.17428 0.12343  -0.07154 -0.04994 684 HIS B CD2 
4649 C CE1 . HIS B 250 ? 0.25803 0.24746 0.18724 0.14053  -0.08005 -0.05869 684 HIS B CE1 
4650 N NE2 . HIS B 250 ? 0.25735 0.23091 0.18097 0.13510  -0.07918 -0.05435 684 HIS B NE2 
4651 N N   . LEU B 251 ? 0.09201 0.23346 0.16568 0.03331  -0.02312 -0.04987 685 LEU B N   
4652 C CA  . LEU B 251 ? 0.11655 0.26673 0.19788 0.02924  -0.02196 -0.05051 685 LEU B CA  
4653 C C   . LEU B 251 ? 0.08361 0.23223 0.16362 0.02356  -0.02281 -0.05125 685 LEU B C   
4654 O O   . LEU B 251 ? 0.16638 0.32214 0.25066 0.02178  -0.02479 -0.05171 685 LEU B O   
4655 C CB  . LEU B 251 ? 0.07974 0.23013 0.16351 0.02823  -0.01806 -0.05095 685 LEU B CB  
4656 C CG  . LEU B 251 ? 0.14387 0.29822 0.23025 0.03344  -0.01650 -0.05066 685 LEU B CG  
4657 C CD1 . LEU B 251 ? 0.09671 0.25006 0.18313 0.03210  -0.01293 -0.05113 685 LEU B CD1 
4658 C CD2 . LEU B 251 ? 0.10007 0.26681 0.19581 0.03527  -0.01690 -0.04966 685 LEU B CD2 
4659 N N   . VAL B 252 ? 0.12138 0.26082 0.19559 0.02060  -0.02124 -0.05147 686 VAL B N   
4660 C CA  . VAL B 252 ? 0.17269 0.31045 0.24621 0.01508  -0.02068 -0.05222 686 VAL B CA  
4661 C C   . VAL B 252 ? 0.11924 0.25739 0.18923 0.01474  -0.02436 -0.05255 686 VAL B C   
4662 O O   . VAL B 252 ? 0.08655 0.22970 0.15977 0.01119  -0.02509 -0.05401 686 VAL B O   
4663 C CB  . VAL B 252 ? 0.14356 0.27144 0.21144 0.01270  -0.01818 -0.05167 686 VAL B CB  
4664 C CG1 . VAL B 252 ? 0.08219 0.20740 0.14847 0.00768  -0.01730 -0.05216 686 VAL B CG1 
4665 C CG2 . VAL B 252 ? 0.07854 0.20804 0.15033 0.01248  -0.01475 -0.05136 686 VAL B CG2 
4666 N N   . MET B 253 ? 0.09404 0.22698 0.15732 0.01840  -0.02665 -0.05125 687 MET B N   
4667 C CA  . MET B 253 ? 0.09982 0.23308 0.15854 0.01848  -0.03009 -0.05101 687 MET B CA  
4668 C C   . MET B 253 ? 0.12596 0.27065 0.18994 0.02058  -0.03355 -0.05111 687 MET B C   
4669 O O   . MET B 253 ? 0.10348 0.25252 0.16675 0.01819  -0.03621 -0.05220 687 MET B O   
4670 C CB  . MET B 253 ? 0.10676 0.23059 0.15692 0.02190  -0.03091 -0.04878 687 MET B CB  
4671 C CG  . MET B 253 ? 0.10701 0.21984 0.15171 0.01914  -0.02808 -0.04838 687 MET B CG  
4672 S SD  . MET B 253 ? 0.10739 0.21893 0.15029 0.01267  -0.02668 -0.04985 687 MET B SD  
4673 C CE  . MET B 253 ? 0.11295 0.22774 0.15060 0.01378  -0.03101 -0.04976 687 MET B CE  
4674 N N   . PRO B 254 ? 0.17618 0.32637 0.24536 0.02502  -0.03372 -0.05001 688 PRO B N   
4675 C CA  . PRO B 254 ? 0.09962 0.26220 0.17531 0.02655  -0.03689 -0.04974 688 PRO B CA  
4676 C C   . PRO B 254 ? 0.12316 0.29420 0.20688 0.02117  -0.03668 -0.05216 688 PRO B C   
4677 O O   . PRO B 254 ? 0.10102 0.27954 0.18682 0.01915  -0.04012 -0.05316 688 PRO B O   
4678 C CB  . PRO B 254 ? 0.17299 0.33828 0.25268 0.03253  -0.03579 -0.04786 688 PRO B CB  
4679 C CG  . PRO B 254 ? 0.13925 0.29212 0.21148 0.03501  -0.03357 -0.04711 688 PRO B CG  
4680 C CD  . PRO B 254 ? 0.11882 0.26412 0.18728 0.02940  -0.03147 -0.04881 688 PRO B CD  
4681 N N   . ILE B 255 ? 0.13159 0.30181 0.22008 0.01872  -0.03265 -0.05307 689 ILE B N   
4682 C CA  . ILE B 255 ? 0.10439 0.28148 0.20121 0.01348  -0.03155 -0.05510 689 ILE B CA  
4683 C C   . ILE B 255 ? 0.14880 0.32183 0.24098 0.00791  -0.03243 -0.05760 689 ILE B C   
4684 O O   . ILE B 255 ? 0.08710 0.26646 0.18338 0.00426  -0.03438 -0.05962 689 ILE B O   
4685 C CB  . ILE B 255 ? 0.11477 0.28925 0.21571 0.01244  -0.02616 -0.05436 689 ILE B CB  
4686 C CG1 . ILE B 255 ? 0.09667 0.27339 0.20034 0.01773  -0.02479 -0.05159 689 ILE B CG1 
4687 C CG2 . ILE B 255 ? 0.12235 0.29717 0.22841 0.00671  -0.02348 -0.05479 689 ILE B CG2 
4688 C CD1 . ILE B 255 ? 0.09416 0.26684 0.19885 0.01755  -0.01975 -0.05033 689 ILE B CD1 
4689 N N   . ALA B 256 ? 0.08841 0.25020 0.17169 0.00708  -0.03073 -0.05744 690 ALA B N   
4690 C CA  . ALA B 256 ? 0.10002 0.25709 0.17830 0.00216  -0.03072 -0.05967 690 ALA B CA  
4691 C C   . ALA B 256 ? 0.15289 0.31409 0.22702 0.00225  -0.03590 -0.06079 690 ALA B C   
4692 O O   . ALA B 256 ? 0.11822 0.28194 0.19288 -0.00243 -0.03697 -0.06391 690 ALA B O   
4693 C CB  . ALA B 256 ? 0.09264 0.23735 0.16216 0.00211  -0.02801 -0.05843 690 ALA B CB  
4694 N N   . ARG B 257 ? 0.17919 0.34129 0.24913 0.00760  -0.03909 -0.05829 691 ARG B N   
4695 C CA  . ARG B 257 ? 0.10959 0.27680 0.17534 0.00834  -0.04419 -0.05858 691 ARG B CA  
4696 C C   . ARG B 257 ? 0.10859 0.28950 0.18352 0.00641  -0.04744 -0.06045 691 ARG B C   
4697 O O   . ARG B 257 ? 0.11398 0.29984 0.18660 0.00376  -0.05125 -0.06267 691 ARG B O   
4698 C CB  . ARG B 257 ? 0.11416 0.27953 0.17454 0.01512  -0.04621 -0.05461 691 ARG B CB  
4699 C CG  . ARG B 257 ? 0.11903 0.27209 0.16840 0.01628  -0.04489 -0.05300 691 ARG B CG  
4700 C CD  . ARG B 257 ? 0.15265 0.30480 0.19730 0.02287  -0.04715 -0.04896 691 ARG B CD  
4701 N NE  . ARG B 257 ? 0.21166 0.36383 0.26131 0.02755  -0.04561 -0.04682 691 ARG B NE  
4702 C CZ  . ARG B 257 ? 0.20894 0.35100 0.25655 0.02910  -0.04203 -0.04578 691 ARG B CZ  
4703 N NH1 . ARG B 257 ? 0.18768 0.31924 0.22923 0.02637  -0.03960 -0.04609 691 ARG B NH1 
4704 N NH2 . ARG B 257 ? 0.11928 0.26197 0.17106 0.03345  -0.04082 -0.04445 691 ARG B NH2 
4705 N N   . GLU B 258 ? 0.10228 0.28984 0.18763 0.00765  -0.04605 -0.05959 692 GLU B N   
4706 C CA  . GLU B 258 ? 0.10371 0.29887 0.19647 0.00527  -0.04714 -0.05954 692 GLU B CA  
4707 C C   . GLU B 258 ? 0.13273 0.32560 0.22834 -0.00205 -0.04483 -0.06315 692 GLU B C   
4708 O O   . GLU B 258 ? 0.13461 0.33191 0.23239 -0.00570 -0.04717 -0.06476 692 GLU B O   
4709 C CB  . GLU B 258 ? 0.09949 0.29821 0.20032 0.00903  -0.04485 -0.05609 692 GLU B CB  
4710 C CG  . GLU B 258 ? 0.10229 0.30969 0.21044 0.00834  -0.04682 -0.05447 692 GLU B CG  
4711 C CD  . GLU B 258 ? 0.15959 0.37007 0.27433 0.01311  -0.04453 -0.05048 692 GLU B CD  
4712 O OE1 . GLU B 258 ? 0.13940 0.34533 0.25171 0.01747  -0.04199 -0.04927 692 GLU B OE1 
4713 O OE2 . GLU B 258 ? 0.16793 0.38522 0.29019 0.01244  -0.04523 -0.04863 692 GLU B OE2 
4714 N N   . PHE B 259 ? 0.09805 0.28401 0.19389 -0.00423 -0.04016 -0.06438 693 PHE B N   
4715 C CA  . PHE B 259 ? 0.13467 0.31739 0.23305 -0.01077 -0.03721 -0.06762 693 PHE B CA  
4716 C C   . PHE B 259 ? 0.10520 0.28556 0.19555 -0.01451 -0.04001 -0.07163 693 PHE B C   
4717 O O   . PHE B 259 ? 0.10865 0.28854 0.20108 -0.01994 -0.03929 -0.07488 693 PHE B O   
4718 C CB  . PHE B 259 ? 0.14516 0.32118 0.24512 -0.01144 -0.03136 -0.06710 693 PHE B CB  
4719 C CG  . PHE B 259 ? 0.12693 0.29891 0.22995 -0.01756 -0.02734 -0.06981 693 PHE B CG  
4720 C CD1 . PHE B 259 ? 0.09108 0.26593 0.20261 -0.02048 -0.02557 -0.06981 693 PHE B CD1 
4721 C CD2 . PHE B 259 ? 0.11763 0.28271 0.21543 -0.02026 -0.02500 -0.07209 693 PHE B CD2 
4722 C CE1 . PHE B 259 ? 0.09155 0.26206 0.20628 -0.02578 -0.02144 -0.07218 693 PHE B CE1 
4723 C CE2 . PHE B 259 ? 0.09102 0.25196 0.19199 -0.02559 -0.02064 -0.07442 693 PHE B CE2 
4724 C CZ  . PHE B 259 ? 0.09157 0.25502 0.20100 -0.02823 -0.01879 -0.07453 693 PHE B CZ  
4725 N N   . ALA B 260 ? 0.10849 0.28694 0.18928 -0.01149 -0.04306 -0.07135 694 ALA B N   
4726 C CA  . ALA B 260 ? 0.11666 0.29153 0.18728 -0.01404 -0.04542 -0.07440 694 ALA B CA  
4727 C C   . ALA B 260 ? 0.11717 0.28343 0.18628 -0.01975 -0.04067 -0.07781 694 ALA B C   
4728 O O   . ALA B 260 ? 0.13996 0.30762 0.20939 -0.02483 -0.04150 -0.08215 694 ALA B O   
4729 C CB  . ALA B 260 ? 0.12485 0.30699 0.19467 -0.01511 -0.05047 -0.07543 694 ALA B CB  
4730 N N   . PRO B 261 ? 0.11292 0.26929 0.18005 -0.01895 -0.03526 -0.07555 695 PRO B N   
4731 C CA  . PRO B 261 ? 0.14382 0.29226 0.21030 -0.02388 -0.03012 -0.07803 695 PRO B CA  
4732 C C   . PRO B 261 ? 0.16692 0.30890 0.22131 -0.02569 -0.03115 -0.08061 695 PRO B C   
4733 O O   . PRO B 261 ? 0.12845 0.26919 0.17334 -0.02215 -0.03454 -0.07891 695 PRO B O   
4734 C CB  . PRO B 261 ? 0.10654 0.24747 0.17330 -0.02143 -0.02490 -0.07381 695 PRO B CB  
4735 C CG  . PRO B 261 ? 0.10711 0.24753 0.16813 -0.01551 -0.02793 -0.07006 695 PRO B CG  
4736 C CD  . PRO B 261 ? 0.10860 0.26028 0.17346 -0.01356 -0.03360 -0.07065 695 PRO B CD  
4737 N N   . GLU B 262 ? 0.12622 0.26406 0.18112 -0.03111 -0.02785 -0.08468 696 GLU B N   
4738 C CA  . GLU B 262 ? 0.15445 0.28458 0.19759 -0.03301 -0.02735 -0.08736 696 GLU B CA  
4739 C C   . GLU B 262 ? 0.14555 0.26350 0.18396 -0.03251 -0.02085 -0.08459 696 GLU B C   
4740 O O   . GLU B 262 ? 0.21041 0.32113 0.23768 -0.03239 -0.02014 -0.08512 696 GLU B O   
4741 C CB  . GLU B 262 ? 0.14246 0.27461 0.18788 -0.03939 -0.02762 -0.09421 696 GLU B CB  
4742 C CG  . GLU B 262 ? 0.14591 0.29065 0.19491 -0.04063 -0.03478 -0.09744 696 GLU B CG  
4743 C CD  . GLU B 262 ? 0.22854 0.37302 0.28279 -0.04654 -0.03338 -0.10205 696 GLU B CD  
4744 O OE1 . GLU B 262 ? 0.14526 0.29171 0.21201 -0.04849 -0.03011 -0.10148 696 GLU B OE1 
4745 O OE2 . GLU B 262 ? 0.26010 0.40206 0.30577 -0.04906 -0.03534 -0.10605 696 GLU B OE2 
4746 N N   . LEU B 263 ? 0.14800 0.26423 0.19463 -0.03207 -0.01611 -0.08139 697 LEU B N   
4747 C CA  . LEU B 263 ? 0.12273 0.22902 0.16624 -0.03133 -0.01019 -0.07788 697 LEU B CA  
4748 C C   . LEU B 263 ? 0.14595 0.25436 0.19679 -0.02832 -0.00853 -0.07306 697 LEU B C   
4749 O O   . LEU B 263 ? 0.11835 0.23413 0.17967 -0.02884 -0.00859 -0.07332 697 LEU B O   
4750 C CB  . LEU B 263 ? 0.12469 0.22524 0.17076 -0.03615 -0.00403 -0.08055 697 LEU B CB  
4751 C CG  . LEU B 263 ? 0.26740 0.35866 0.31164 -0.03551 0.00266  -0.07638 697 LEU B CG  
4752 C CD1 . LEU B 263 ? 0.25413 0.33795 0.28517 -0.03303 0.00197  -0.07451 697 LEU B CD1 
4753 C CD2 . LEU B 263 ? 0.16807 0.25484 0.21717 -0.03996 0.00924  -0.07865 697 LEU B CD2 
4754 N N   . VAL B 264 ? 0.12674 0.22888 0.17204 -0.02523 -0.00706 -0.06871 698 VAL B N   
4755 C CA  . VAL B 264 ? 0.15902 0.26234 0.20941 -0.02238 -0.00579 -0.06448 698 VAL B CA  
4756 C C   . VAL B 264 ? 0.09955 0.19588 0.15052 -0.02368 0.00053  -0.06156 698 VAL B C   
4757 O O   . VAL B 264 ? 0.10390 0.19240 0.14686 -0.02338 0.00207  -0.05990 698 VAL B O   
4758 C CB  . VAL B 264 ? 0.10414 0.20679 0.14841 -0.01757 -0.01000 -0.06178 698 VAL B CB  
4759 C CG1 . VAL B 264 ? 0.09676 0.20004 0.14580 -0.01505 -0.00859 -0.05828 698 VAL B CG1 
4760 C CG2 . VAL B 264 ? 0.10758 0.21787 0.15154 -0.01587 -0.01602 -0.06398 698 VAL B CG2 
4761 N N   . LEU B 265 ? 0.09227 0.19202 0.15299 -0.02493 0.00432  -0.06047 699 LEU B N   
4762 C CA  . LEU B 265 ? 0.08807 0.18346 0.15099 -0.02557 0.01015  -0.05672 699 LEU B CA  
4763 C C   . LEU B 265 ? 0.12221 0.22055 0.18776 -0.02239 0.00933  -0.05304 699 LEU B C   
4764 O O   . LEU B 265 ? 0.10946 0.21533 0.18159 -0.02110 0.00774  -0.05344 699 LEU B O   
4765 C CB  . LEU B 265 ? 0.10187 0.19932 0.17406 -0.02895 0.01556  -0.05747 699 LEU B CB  
4766 C CG  . LEU B 265 ? 0.09160 0.18727 0.16366 -0.03278 0.01654  -0.06233 699 LEU B CG  
4767 C CD1 . LEU B 265 ? 0.08823 0.18498 0.17068 -0.03577 0.02296  -0.06208 699 LEU B CD1 
4768 C CD2 . LEU B 265 ? 0.11682 0.20325 0.17762 -0.03344 0.01722  -0.06322 699 LEU B CD2 
4769 N N   . VAL B 266 ? 0.08308 0.17560 0.14357 -0.02121 0.01049  -0.04958 700 VAL B N   
4770 C CA  . VAL B 266 ? 0.07689 0.17128 0.13905 -0.01873 0.00979  -0.04655 700 VAL B CA  
4771 C C   . VAL B 266 ? 0.10611 0.20140 0.17420 -0.02028 0.01535  -0.04318 700 VAL B C   
4772 O O   . VAL B 266 ? 0.08656 0.17623 0.15223 -0.02182 0.01894  -0.04078 700 VAL B O   
4773 C CB  . VAL B 266 ? 0.08643 0.17439 0.13998 -0.01657 0.00703  -0.04484 700 VAL B CB  
4774 C CG1 . VAL B 266 ? 0.08191 0.17195 0.13723 -0.01421 0.00564  -0.04296 700 VAL B CG1 
4775 C CG2 . VAL B 266 ? 0.11863 0.20553 0.16592 -0.01492 0.00224  -0.04744 700 VAL B CG2 
4776 N N   . SER B 267 ? 0.11535 0.21827 0.19141 -0.01962 0.01631  -0.04259 701 SER B N   
4777 C CA  . SER B 267 ? 0.07262 0.17801 0.15395 -0.02011 0.02081  -0.03859 701 SER B CA  
4778 C C   . SER B 267 ? 0.07629 0.17990 0.15297 -0.01815 0.01833  -0.03650 701 SER B C   
4779 O O   . SER B 267 ? 0.10530 0.21345 0.18306 -0.01581 0.01565  -0.03702 701 SER B O   
4780 C CB  . SER B 267 ? 0.05618 0.16672 0.14397 -0.01909 0.02198  -0.03724 701 SER B CB  
4781 O OG  . SER B 267 ? 0.10531 0.21242 0.19555 -0.02101 0.02548  -0.03641 701 SER B OG  
4782 N N   . ALA B 268 ? 0.06242 0.15902 0.13387 -0.01919 0.01937  -0.03424 702 ALA B N   
4783 C CA  . ALA B 268 ? 0.11744 0.21000 0.18320 -0.01790 0.01636  -0.03297 702 ALA B CA  
4784 C C   . ALA B 268 ? 0.08522 0.17952 0.15390 -0.01894 0.01923  -0.02868 702 ALA B C   
4785 O O   . ALA B 268 ? 0.11432 0.20348 0.18027 -0.02029 0.02081  -0.02569 702 ALA B O   
4786 C CB  . ALA B 268 ? 0.07164 0.15534 0.12940 -0.01814 0.01502  -0.03323 702 ALA B CB  
4787 N N   . GLY B 269 ? 0.08018 0.18253 0.15461 -0.01820 0.01991  -0.02811 703 GLY B N   
4788 C CA  . GLY B 269 ? 0.06029 0.16559 0.13622 -0.01862 0.02076  -0.02473 703 GLY B CA  
4789 C C   . GLY B 269 ? 0.08240 0.18330 0.15218 -0.01768 0.01602  -0.02603 703 GLY B C   
4790 O O   . GLY B 269 ? 0.17947 0.27783 0.24545 -0.01563 0.01215  -0.02961 703 GLY B O   
4791 N N   . PHE B 270 ? 0.11955 0.21940 0.18872 -0.01925 0.01649  -0.02288 704 PHE B N   
4792 C CA  . PHE B 270 ? 0.07159 0.16676 0.13572 -0.01897 0.01233  -0.02408 704 PHE B CA  
4793 C C   . PHE B 270 ? 0.06052 0.16222 0.12682 -0.01931 0.01146  -0.02349 704 PHE B C   
4794 O O   . PHE B 270 ? 0.06385 0.16257 0.12771 -0.02069 0.00939  -0.02293 704 PHE B O   
4795 C CB  . PHE B 270 ? 0.06663 0.15343 0.12720 -0.02086 0.01277  -0.02140 704 PHE B CB  
4796 C CG  . PHE B 270 ? 0.07769 0.15772 0.13421 -0.02002 0.01282  -0.02261 704 PHE B CG  
4797 C CD1 . PHE B 270 ? 0.09139 0.16633 0.14269 -0.01781 0.00884  -0.02589 704 PHE B CD1 
4798 C CD2 . PHE B 270 ? 0.09830 0.17738 0.15610 -0.02122 0.01698  -0.02054 704 PHE B CD2 
4799 C CE1 . PHE B 270 ? 0.12974 0.19972 0.17695 -0.01687 0.00859  -0.02686 704 PHE B CE1 
4800 C CE2 . PHE B 270 ? 0.08914 0.16246 0.14233 -0.02052 0.01677  -0.02218 704 PHE B CE2 
4801 C CZ  . PHE B 270 ? 0.11278 0.18207 0.16059 -0.01836 0.01236  -0.02524 704 PHE B CZ  
4802 N N   . ASP B 271 ? 0.09735 0.20828 0.16833 -0.01811 0.01302  -0.02364 705 ASP B N   
4803 C CA  . ASP B 271 ? 0.07905 0.19760 0.15148 -0.01782 0.01210  -0.02349 705 ASP B CA  
4804 C C   . ASP B 271 ? 0.08458 0.20240 0.15287 -0.01512 0.00793  -0.02862 705 ASP B C   
4805 O O   . ASP B 271 ? 0.07256 0.19686 0.14113 -0.01435 0.00706  -0.02943 705 ASP B O   
4806 C CB  . ASP B 271 ? 0.06307 0.18682 0.13932 -0.01657 0.01567  -0.01940 705 ASP B CB  
4807 C CG  . ASP B 271 ? 0.07755 0.19853 0.15481 -0.01443 0.01728  -0.01973 705 ASP B CG  
4808 O OD1 . ASP B 271 ? 0.07255 0.19344 0.14979 -0.01402 0.01573  -0.02442 705 ASP B OD1 
4809 O OD2 . ASP B 271 ? 0.04966 0.16870 0.12845 -0.01318 0.01997  -0.01520 705 ASP B OD2 
4810 N N   . ALA B 272 ? 0.06244 0.17277 0.12669 -0.01341 0.00550  -0.03193 706 ALA B N   
4811 C CA  . ALA B 272 ? 0.06829 0.17553 0.12791 -0.01090 0.00168  -0.03636 706 ALA B CA  
4812 C C   . ALA B 272 ? 0.07504 0.17258 0.12944 -0.01245 -0.00108 -0.03719 706 ALA B C   
4813 O O   . ALA B 272 ? 0.09229 0.18498 0.14252 -0.01042 -0.00398 -0.04088 706 ALA B O   
4814 C CB  . ALA B 272 ? 0.06890 0.17475 0.12791 -0.00753 0.00071  -0.03910 706 ALA B CB  
4815 N N   . ALA B 273 ? 0.10641 0.20094 0.16143 -0.01589 0.00011  -0.03359 707 ALA B N   
4816 C CA  . ALA B 273 ? 0.08201 0.16767 0.13334 -0.01782 -0.00208 -0.03360 707 ALA B CA  
4817 C C   . ALA B 273 ? 0.11835 0.20711 0.16965 -0.01998 -0.00375 -0.03440 707 ALA B C   
4818 O O   . ALA B 273 ? 0.07898 0.17761 0.13334 -0.02045 -0.00265 -0.03353 707 ALA B O   
4819 C CB  . ALA B 273 ? 0.09206 0.17351 0.14437 -0.02043 0.00017  -0.02898 707 ALA B CB  
4820 N N   . ARG B 274 ? 0.12860 0.20881 0.17644 -0.02134 -0.00641 -0.03603 708 ARG B N   
4821 C CA  . ARG B 274 ? 0.15294 0.23459 0.20035 -0.02432 -0.00859 -0.03735 708 ARG B CA  
4822 C C   . ARG B 274 ? 0.32360 0.41348 0.37592 -0.02817 -0.00673 -0.03222 708 ARG B C   
4823 O O   . ARG B 274 ? 0.26470 0.35408 0.31993 -0.02918 -0.00384 -0.02729 708 ARG B O   
4824 C CB  . ARG B 274 ? 0.16451 0.23392 0.20873 -0.02574 -0.01091 -0.03878 708 ARG B CB  
4825 C CG  . ARG B 274 ? 0.31449 0.38042 0.36126 -0.02992 -0.01009 -0.03383 708 ARG B CG  
4826 C CD  . ARG B 274 ? 0.47216 0.53326 0.51851 -0.03383 -0.01288 -0.03528 708 ARG B CD  
4827 N NE  . ARG B 274 ? 0.44991 0.52013 0.49728 -0.03622 -0.01460 -0.03731 708 ARG B NE  
4828 C CZ  . ARG B 274 ? 0.42729 0.50712 0.47913 -0.03960 -0.01375 -0.03312 708 ARG B CZ  
4829 N NH1 . ARG B 274 ? 0.33621 0.41686 0.39215 -0.04110 -0.01090 -0.02666 708 ARG B NH1 
4830 N NH2 . ARG B 274 ? 0.28617 0.37511 0.33817 -0.04116 -0.01557 -0.03523 708 ARG B NH2 
4831 N N   . GLY B 275 ? 0.15969 0.25751 0.21278 -0.02991 -0.00812 -0.03319 709 GLY B N   
4832 C CA  . GLY B 275 ? 0.19528 0.30208 0.25339 -0.03346 -0.00659 -0.02780 709 GLY B CA  
4833 C C   . GLY B 275 ? 0.15033 0.26797 0.21330 -0.03180 -0.00240 -0.02347 709 GLY B C   
4834 O O   . GLY B 275 ? 0.07687 0.20143 0.14461 -0.03425 -0.00032 -0.01798 709 GLY B O   
4835 N N   . ASP B 276 ? 0.12470 0.24361 0.18710 -0.02777 -0.00097 -0.02555 710 ASP B N   
4836 C CA  . ASP B 276 ? 0.09720 0.22542 0.16505 -0.02623 0.00352  -0.02143 710 ASP B CA  
4837 C C   . ASP B 276 ? 0.10337 0.24377 0.17237 -0.02471 0.00342  -0.02217 710 ASP B C   
4838 O O   . ASP B 276 ? 0.15559 0.29655 0.22179 -0.02143 0.00217  -0.02669 710 ASP B O   
4839 C CB  . ASP B 276 ? 0.08087 0.20438 0.14914 -0.02354 0.00584  -0.02198 710 ASP B CB  
4840 C CG  . ASP B 276 ? 0.09122 0.22164 0.16588 -0.02312 0.01109  -0.01716 710 ASP B CG  
4841 O OD1 . ASP B 276 ? 0.10643 0.24123 0.18146 -0.02099 0.01229  -0.01491 710 ASP B OD1 
4842 O OD2 . ASP B 276 ? 0.06673 0.19172 0.14254 -0.02384 0.01364  -0.01489 710 ASP B OD2 
4843 N N   . PRO B 277 ? 0.12580 0.27609 0.19887 -0.02646 0.00512  -0.01718 711 PRO B N   
4844 C CA  . PRO B 277 ? 0.18168 0.34001 0.25312 -0.02404 0.00515  -0.01639 711 PRO B CA  
4845 C C   . PRO B 277 ? 0.13236 0.28979 0.20335 -0.01908 0.00804  -0.01587 711 PRO B C   
4846 O O   . PRO B 277 ? 0.08032 0.24457 0.14947 -0.01667 0.00764  -0.01699 711 PRO B O   
4847 C CB  . PRO B 277 ? 0.06050 0.21930 0.13317 -0.02562 0.00671  -0.00913 711 PRO B CB  
4848 C CG  . PRO B 277 ? 0.06940 0.22336 0.14375 -0.02999 0.00544  -0.00847 711 PRO B CG  
4849 C CD  . PRO B 277 ? 0.12941 0.27576 0.20435 -0.02906 0.00692  -0.01058 711 PRO B CD  
4850 N N   . LEU B 278 ? 0.11855 0.26781 0.19110 -0.01779 0.01067  -0.01443 712 LEU B N   
4851 C CA  . LEU B 278 ? 0.13689 0.28352 0.20991 -0.01391 0.01333  -0.01312 712 LEU B CA  
4852 C C   . LEU B 278 ? 0.16040 0.30682 0.23275 -0.01210 0.01185  -0.01921 712 LEU B C   
4853 O O   . LEU B 278 ? 0.21450 0.35799 0.28776 -0.00945 0.01375  -0.01820 712 LEU B O   
4854 C CB  . LEU B 278 ? 0.08713 0.22481 0.16307 -0.01390 0.01722  -0.00745 712 LEU B CB  
4855 C CG  . LEU B 278 ? 0.12827 0.26517 0.20587 -0.01364 0.01971  -0.00148 712 LEU B CG  
4856 C CD1 . LEU B 278 ? 0.11897 0.24606 0.19996 -0.01380 0.02367  0.00224  712 LEU B CD1 
4857 C CD2 . LEU B 278 ? 0.09872 0.23944 0.17618 -0.01075 0.02058  -0.00049 712 LEU B CD2 
4858 N N   . GLY B 279 ? 0.07008 0.21883 0.14171 -0.01357 0.00845  -0.02524 713 GLY B N   
4859 C CA  . GLY B 279 ? 0.05660 0.20204 0.12657 -0.01106 0.00653  -0.03090 713 GLY B CA  
4860 C C   . GLY B 279 ? 0.09356 0.23708 0.15707 -0.00955 0.00253  -0.03619 713 GLY B C   
4861 O O   . GLY B 279 ? 0.10073 0.24795 0.16353 -0.00575 0.00248  -0.03886 713 GLY B O   
4862 N N   . GLY B 280 ? 0.06959 0.20751 0.12889 -0.01251 -0.00045 -0.03756 714 GLY B N   
4863 C CA  . GLY B 280 ? 0.07816 0.21294 0.13096 -0.01166 -0.00418 -0.04319 714 GLY B CA  
4864 C C   . GLY B 280 ? 0.10533 0.22807 0.15365 -0.00951 -0.00629 -0.04765 714 GLY B C   
4865 O O   . GLY B 280 ? 0.09741 0.21706 0.14054 -0.00773 -0.00861 -0.05269 714 GLY B O   
4866 N N   . PHE B 281 ? 0.10659 0.22309 0.15670 -0.00950 -0.00531 -0.04579 715 PHE B N   
4867 C CA  . PHE B 281 ? 0.08767 0.19318 0.13398 -0.00731 -0.00716 -0.04893 715 PHE B CA  
4868 C C   . PHE B 281 ? 0.09273 0.18738 0.13660 -0.01062 -0.00881 -0.04833 715 PHE B C   
4869 O O   . PHE B 281 ? 0.14435 0.24012 0.19008 -0.01473 -0.00837 -0.04518 715 PHE B O   
4870 C CB  . PHE B 281 ? 0.08260 0.18947 0.13208 -0.00458 -0.00534 -0.04760 715 PHE B CB  
4871 C CG  . PHE B 281 ? 0.07951 0.19507 0.13136 -0.00050 -0.00410 -0.04885 715 PHE B CG  
4872 C CD1 . PHE B 281 ? 0.08237 0.20475 0.13316 0.00100  -0.00411 -0.05065 715 PHE B CD1 
4873 C CD2 . PHE B 281 ? 0.08437 0.20169 0.13963 0.00177  -0.00291 -0.04813 715 PHE B CD2 
4874 C CE1 . PHE B 281 ? 0.07825 0.20872 0.13150 0.00507  -0.00256 -0.05124 715 PHE B CE1 
4875 C CE2 . PHE B 281 ? 0.11321 0.23878 0.17164 0.00537  -0.00162 -0.04882 715 PHE B CE2 
4876 C CZ  . PHE B 281 ? 0.07406 0.20609 0.13157 0.00721  -0.00125 -0.05013 715 PHE B CZ  
4877 N N   . GLN B 282 ? 0.09902 0.18371 0.13930 -0.00860 -0.01042 -0.05076 716 GLN B N   
4878 C CA  . GLN B 282 ? 0.10494 0.17871 0.14297 -0.01116 -0.01179 -0.05011 716 GLN B CA  
4879 C C   . GLN B 282 ? 0.13451 0.20114 0.17152 -0.00880 -0.01157 -0.04897 716 GLN B C   
4880 O O   . GLN B 282 ? 0.18653 0.24321 0.22022 -0.00780 -0.01305 -0.05034 716 GLN B O   
4881 C CB  . GLN B 282 ? 0.11497 0.18209 0.14873 -0.01160 -0.01438 -0.05465 716 GLN B CB  
4882 C CG  . GLN B 282 ? 0.20742 0.27169 0.23763 -0.00654 -0.01520 -0.05941 716 GLN B CG  
4883 C CD  . GLN B 282 ? 0.33523 0.39217 0.36097 -0.00720 -0.01730 -0.06445 716 GLN B CD  
4884 O OE1 . GLN B 282 ? 0.34095 0.39788 0.36653 -0.01176 -0.01852 -0.06499 716 GLN B OE1 
4885 N NE2 . GLN B 282 ? 0.30856 0.35925 0.33087 -0.00269 -0.01766 -0.06819 716 GLN B NE2 
4886 N N   . VAL B 283 ? 0.11484 0.18659 0.15477 -0.00794 -0.00963 -0.04637 717 VAL B N   
4887 C CA  . VAL B 283 ? 0.10025 0.16619 0.13891 -0.00653 -0.00956 -0.04484 717 VAL B CA  
4888 C C   . VAL B 283 ? 0.10501 0.16420 0.14293 -0.01002 -0.00907 -0.04140 717 VAL B C   
4889 O O   . VAL B 283 ? 0.09763 0.16060 0.13846 -0.01348 -0.00724 -0.03833 717 VAL B O   
4890 C CB  . VAL B 283 ? 0.14815 0.22144 0.19013 -0.00539 -0.00772 -0.04353 717 VAL B CB  
4891 C CG1 . VAL B 283 ? 0.17421 0.24201 0.21403 -0.00420 -0.00806 -0.04230 717 VAL B CG1 
4892 C CG2 . VAL B 283 ? 0.09100 0.17144 0.13463 -0.00185 -0.00802 -0.04640 717 VAL B CG2 
4893 N N   . THR B 284 ? 0.10959 0.15900 0.14401 -0.00886 -0.01038 -0.04142 718 THR B N   
4894 C CA  . THR B 284 ? 0.12403 0.16640 0.15780 -0.01178 -0.00981 -0.03791 718 THR B CA  
4895 C C   . THR B 284 ? 0.18985 0.23188 0.22323 -0.01144 -0.00797 -0.03440 718 THR B C   
4896 O O   . THR B 284 ? 0.17738 0.22259 0.21012 -0.00863 -0.00796 -0.03541 718 THR B O   
4897 C CB  . THR B 284 ? 0.12268 0.15430 0.15324 -0.01056 -0.01163 -0.03917 718 THR B CB  
4898 O OG1 . THR B 284 ? 0.12586 0.15362 0.15360 -0.00632 -0.01197 -0.03887 718 THR B OG1 
4899 C CG2 . THR B 284 ? 0.15842 0.18973 0.18822 -0.00981 -0.01344 -0.04402 718 THR B CG2 
4900 N N   . PRO B 285 ? 0.17915 0.21771 0.21296 -0.01438 -0.00632 -0.03030 719 PRO B N   
4901 C CA  . PRO B 285 ? 0.20415 0.24114 0.23628 -0.01376 -0.00441 -0.02724 719 PRO B CA  
4902 C C   . PRO B 285 ? 0.19025 0.22205 0.21782 -0.00972 -0.00599 -0.02813 719 PRO B C   
4903 O O   . PRO B 285 ? 0.20831 0.24224 0.23416 -0.00823 -0.00532 -0.02777 719 PRO B O   
4904 C CB  . PRO B 285 ? 0.15616 0.18858 0.18913 -0.01709 -0.00259 -0.02262 719 PRO B CB  
4905 C CG  . PRO B 285 ? 0.12533 0.16193 0.16246 -0.02044 -0.00289 -0.02292 719 PRO B CG  
4906 C CD  . PRO B 285 ? 0.14263 0.18001 0.17888 -0.01858 -0.00590 -0.02813 719 PRO B CD  
4907 N N   . GLU B 286 ? 0.22071 0.24589 0.24637 -0.00791 -0.00802 -0.02928 720 GLU B N   
4908 C CA  . GLU B 286 ? 0.15486 0.17593 0.17666 -0.00347 -0.00943 -0.02961 720 GLU B CA  
4909 C C   . GLU B 286 ? 0.22358 0.25170 0.24566 -0.00028 -0.01084 -0.03313 720 GLU B C   
4910 O O   . GLU B 286 ? 0.13993 0.16921 0.15960 0.00268  -0.01156 -0.03279 720 GLU B O   
4911 C CB  . GLU B 286 ? 0.13725 0.14916 0.15783 -0.00217 -0.01063 -0.02979 720 GLU B CB  
4912 C CG  . GLU B 286 ? 0.14991 0.15428 0.17083 -0.00514 -0.00930 -0.02585 720 GLU B CG  
4913 C CD  . GLU B 286 ? 0.16286 0.16861 0.18775 -0.01011 -0.00902 -0.02644 720 GLU B CD  
4914 O OE1 . GLU B 286 ? 0.19584 0.20843 0.22264 -0.01101 -0.00980 -0.02991 720 GLU B OE1 
4915 O OE2 . GLU B 286 ? 0.21726 0.21780 0.24357 -0.01307 -0.00805 -0.02315 720 GLU B OE2 
4916 N N   . GLY B 287 ? 0.12271 0.15615 0.14779 -0.00079 -0.01130 -0.03634 721 GLY B N   
4917 C CA  . GLY B 287 ? 0.11726 0.15868 0.14382 0.00186  -0.01209 -0.03910 721 GLY B CA  
4918 C C   . GLY B 287 ? 0.13003 0.17812 0.15807 0.00065  -0.01078 -0.03809 721 GLY B C   
4919 O O   . GLY B 287 ? 0.15309 0.20498 0.18074 0.00318  -0.01184 -0.03907 721 GLY B O   
4920 N N   . TYR B 288 ? 0.10644 0.15598 0.13641 -0.00331 -0.00837 -0.03609 722 TYR B N   
4921 C CA  . TYR B 288 ? 0.11666 0.17091 0.14787 -0.00471 -0.00646 -0.03521 722 TYR B CA  
4922 C C   . TYR B 288 ? 0.20819 0.25804 0.23454 -0.00336 -0.00696 -0.03386 722 TYR B C   
4923 O O   . TYR B 288 ? 0.19914 0.25320 0.22534 -0.00303 -0.00689 -0.03492 722 TYR B O   
4924 C CB  . TYR B 288 ? 0.10667 0.16228 0.14084 -0.00879 -0.00319 -0.03264 722 TYR B CB  
4925 C CG  . TYR B 288 ? 0.09071 0.15394 0.13021 -0.01003 -0.00222 -0.03369 722 TYR B CG  
4926 C CD1 . TYR B 288 ? 0.08537 0.15665 0.12867 -0.00932 -0.00142 -0.03546 722 TYR B CD1 
4927 C CD2 . TYR B 288 ? 0.11076 0.17368 0.15169 -0.01197 -0.00211 -0.03275 722 TYR B CD2 
4928 C CE1 . TYR B 288 ? 0.07985 0.15860 0.12806 -0.01000 -0.00018 -0.03581 722 TYR B CE1 
4929 C CE2 . TYR B 288 ? 0.10213 0.17294 0.14735 -0.01280 -0.00129 -0.03346 722 TYR B CE2 
4930 C CZ  . TYR B 288 ? 0.07982 0.15852 0.12859 -0.01156 -0.00014 -0.03475 722 TYR B CZ  
4931 O OH  . TYR B 288 ? 0.13373 0.22075 0.18683 -0.01195 0.00103  -0.03485 722 TYR B OH  
4932 N N   . ALA B 289 ? 0.18046 0.22209 0.20288 -0.00266 -0.00743 -0.03150 723 ALA B N   
4933 C CA  . ALA B 289 ? 0.11929 0.15700 0.13643 -0.00069 -0.00795 -0.02978 723 ALA B CA  
4934 C C   . ALA B 289 ? 0.19218 0.23352 0.20785 0.00329  -0.01094 -0.03211 723 ALA B C   
4935 O O   . ALA B 289 ? 0.15243 0.19647 0.16540 0.00409  -0.01152 -0.03234 723 ALA B O   
4936 C CB  . ALA B 289 ? 0.12623 0.15462 0.14037 -0.00020 -0.00771 -0.02637 723 ALA B CB  
4937 N N   A HIS B 290 ? 0.14869 0.19038 0.16605 0.00584  -0.01283 -0.03389 724 HIS B N   
4938 N N   B HIS B 290 ? 0.14871 0.19046 0.16609 0.00584  -0.01284 -0.03392 724 HIS B N   
4939 C CA  A HIS B 290 ? 0.14196 0.18756 0.15864 0.01007  -0.01549 -0.03545 724 HIS B CA  
4940 C CA  B HIS B 290 ? 0.14213 0.18772 0.15877 0.01008  -0.01550 -0.03543 724 HIS B CA  
4941 C C   A HIS B 290 ? 0.11863 0.17436 0.13900 0.00931  -0.01592 -0.03818 724 HIS B C   
4942 C C   B HIS B 290 ? 0.11864 0.17440 0.13903 0.00935  -0.01595 -0.03820 724 HIS B C   
4943 O O   A HIS B 290 ? 0.14960 0.20981 0.16879 0.01120  -0.01782 -0.03875 724 HIS B O   
4944 O O   B HIS B 290 ? 0.14923 0.20954 0.16851 0.01130  -0.01788 -0.03880 724 HIS B O   
4945 C CB  A HIS B 290 ? 0.15985 0.20262 0.17759 0.01320  -0.01668 -0.03657 724 HIS B CB  
4946 C CB  B HIS B 290 ? 0.16019 0.20277 0.17774 0.01331  -0.01672 -0.03646 724 HIS B CB  
4947 C CG  A HIS B 290 ? 0.13732 0.17049 0.15129 0.01559  -0.01692 -0.03390 724 HIS B CG  
4948 C CG  B HIS B 290 ? 0.20963 0.25122 0.22457 0.01850  -0.01883 -0.03552 724 HIS B CG  
4949 N ND1 A HIS B 290 ? 0.21337 0.24535 0.22540 0.02069  -0.01860 -0.03306 724 HIS B ND1 
4950 N ND1 B HIS B 290 ? 0.20693 0.25673 0.22358 0.02147  -0.02078 -0.03707 724 HIS B ND1 
4951 C CD2 A HIS B 290 ? 0.14114 0.16564 0.15358 0.01363  -0.01544 -0.03142 724 HIS B CD2 
4952 C CD2 B HIS B 290 ? 0.21389 0.24775 0.22519 0.02142  -0.01910 -0.03265 724 HIS B CD2 
4953 C CE1 A HIS B 290 ? 0.15126 0.17375 0.16067 0.02190  -0.01790 -0.03017 724 HIS B CE1 
4954 C CE1 B HIS B 290 ? 0.14127 0.18888 0.15527 0.02613  -0.02228 -0.03510 724 HIS B CE1 
4955 N NE2 A HIS B 290 ? 0.14986 0.16759 0.15959 0.01751  -0.01606 -0.02925 724 HIS B NE2 
4956 N NE2 B HIS B 290 ? 0.14741 0.18515 0.15805 0.02632  -0.02114 -0.03234 724 HIS B NE2 
4957 N N   . LEU B 291 ? 0.11162 0.17153 0.13685 0.00652  -0.01418 -0.03968 725 LEU B N   
4958 C CA  . LEU B 291 ? 0.11023 0.17942 0.14000 0.00543  -0.01393 -0.04184 725 LEU B CA  
4959 C C   . LEU B 291 ? 0.16174 0.23181 0.18951 0.00317  -0.01321 -0.04152 725 LEU B C   
4960 O O   . LEU B 291 ? 0.14512 0.22159 0.17445 0.00343  -0.01456 -0.04344 725 LEU B O   
4961 C CB  . LEU B 291 ? 0.13212 0.20515 0.16733 0.00282  -0.01145 -0.04252 725 LEU B CB  
4962 C CG  . LEU B 291 ? 0.14712 0.22041 0.18418 0.00446  -0.01181 -0.04354 725 LEU B CG  
4963 C CD1 . LEU B 291 ? 0.18043 0.26031 0.22306 0.00205  -0.00935 -0.04397 725 LEU B CD1 
4964 C CD2 . LEU B 291 ? 0.17437 0.25039 0.21169 0.00911  -0.01435 -0.04535 725 LEU B CD2 
4965 N N   . THR B 292 ? 0.12209 0.18577 0.14640 0.00088  -0.01104 -0.03920 726 THR B N   
4966 C CA  . THR B 292 ? 0.10984 0.17292 0.13085 -0.00097 -0.00994 -0.03899 726 THR B CA  
4967 C C   . THR B 292 ? 0.12596 0.18832 0.14102 0.00206  -0.01308 -0.03895 726 THR B C   
4968 O O   . THR B 292 ? 0.15978 0.22642 0.17352 0.00142  -0.01408 -0.04092 726 THR B O   
4969 C CB  . THR B 292 ? 0.19374 0.24994 0.21246 -0.00352 -0.00645 -0.03587 726 THR B CB  
4970 O OG1 . THR B 292 ? 0.15823 0.21682 0.18286 -0.00645 -0.00342 -0.03560 726 THR B OG1 
4971 C CG2 . THR B 292 ? 0.11472 0.16899 0.12852 -0.00478 -0.00502 -0.03563 726 THR B CG2 
4972 N N   . HIS B 293 ? 0.12258 0.17972 0.13412 0.00532  -0.01462 -0.03665 727 HIS B N   
4973 C CA  . HIS B 293 ? 0.13007 0.18693 0.13598 0.00880  -0.01739 -0.03565 727 HIS B CA  
4974 C C   . HIS B 293 ? 0.21594 0.28183 0.22444 0.01104  -0.02083 -0.03829 727 HIS B C   
4975 O O   . HIS B 293 ? 0.19456 0.26387 0.19918 0.01260  -0.02326 -0.03843 727 HIS B O   
4976 C CB  . HIS B 293 ? 0.13596 0.18511 0.13896 0.01208  -0.01771 -0.03219 727 HIS B CB  
4977 C CG  . HIS B 293 ? 0.23285 0.28060 0.22946 0.01575  -0.01958 -0.02970 727 HIS B CG  
4978 N ND1 . HIS B 293 ? 0.34227 0.39342 0.33863 0.02039  -0.02266 -0.02936 727 HIS B ND1 
4979 C CD2 . HIS B 293 ? 0.24127 0.28509 0.23140 0.01583  -0.01859 -0.02700 727 HIS B CD2 
4980 C CE1 . HIS B 293 ? 0.32617 0.37596 0.31627 0.02315  -0.02365 -0.02640 727 HIS B CE1 
4981 N NE2 . HIS B 293 ? 0.26575 0.31100 0.25170 0.02047  -0.02124 -0.02504 727 HIS B NE2 
4982 N N   . GLN B 294 ? 0.12365 0.19410 0.13870 0.01132  -0.02110 -0.04020 728 GLN B N   
4983 C CA  . GLN B 294 ? 0.12242 0.20222 0.14117 0.01337  -0.02403 -0.04232 728 GLN B CA  
4984 C C   . GLN B 294 ? 0.11911 0.20613 0.14038 0.00972  -0.02413 -0.04523 728 GLN B C   
4985 O O   . GLN B 294 ? 0.12175 0.21548 0.14270 0.01069  -0.02722 -0.04648 728 GLN B O   
4986 C CB  . GLN B 294 ? 0.11790 0.20018 0.14271 0.01503  -0.02372 -0.04326 728 GLN B CB  
4987 C CG  . GLN B 294 ? 0.12313 0.19928 0.14571 0.01948  -0.02435 -0.04127 728 GLN B CG  
4988 C CD  . GLN B 294 ? 0.26421 0.34258 0.29190 0.02121  -0.02381 -0.04281 728 GLN B CD  
4989 O OE1 . GLN B 294 ? 0.47167 0.55884 0.50475 0.02126  -0.02427 -0.04471 728 GLN B OE1 
4990 N NE2 . GLN B 294 ? 0.19082 0.26117 0.21684 0.02258  -0.02272 -0.04208 728 GLN B NE2 
4991 N N   . LEU B 295 ? 0.11388 0.19986 0.13806 0.00543  -0.02073 -0.04630 729 LEU B N   
4992 C CA  . LEU B 295 ? 0.11147 0.20301 0.13851 0.00170  -0.02014 -0.04921 729 LEU B CA  
4993 C C   . LEU B 295 ? 0.11850 0.20785 0.13817 0.00053  -0.02104 -0.04976 729 LEU B C   
4994 O O   . LEU B 295 ? 0.11939 0.21432 0.14027 -0.00178 -0.02218 -0.05291 729 LEU B O   
4995 C CB  . LEU B 295 ? 0.10480 0.19508 0.13681 -0.00213 -0.01558 -0.04948 729 LEU B CB  
4996 C CG  . LEU B 295 ? 0.09801 0.19233 0.13736 -0.00109 -0.01473 -0.04933 729 LEU B CG  
4997 C CD1 . LEU B 295 ? 0.09267 0.18443 0.13517 -0.00402 -0.01020 -0.04811 729 LEU B CD1 
4998 C CD2 . LEU B 295 ? 0.09467 0.19922 0.14118 -0.00097 -0.01633 -0.05184 729 LEU B CD2 
4999 N N   . MET B 296 ? 0.16189 0.24340 0.17396 0.00210  -0.02056 -0.04684 730 MET B N   
5000 C CA  . MET B 296 ? 0.13351 0.21301 0.13746 0.00166  -0.02128 -0.04704 730 MET B CA  
5001 C C   . MET B 296 ? 0.13726 0.22415 0.13875 0.00419  -0.02636 -0.04831 730 MET B C   
5002 O O   . MET B 296 ? 0.14341 0.23172 0.13911 0.00299  -0.02761 -0.05003 730 MET B O   
5003 C CB  . MET B 296 ? 0.15485 0.22474 0.15184 0.00339  -0.01941 -0.04277 730 MET B CB  
5004 C CG  . MET B 296 ? 0.13336 0.19654 0.13142 0.00010  -0.01429 -0.04145 730 MET B CG  
5005 S SD  . MET B 296 ? 0.13846 0.19107 0.13056 0.00211  -0.01214 -0.03580 730 MET B SD  
5006 C CE  . MET B 296 ? 0.14941 0.20095 0.13073 0.00402  -0.01354 -0.03518 730 MET B CE  
5007 N N   . SER B 297 ? 0.13567 0.22766 0.14123 0.00774  -0.02928 -0.04747 731 SER B N   
5008 C CA  . SER B 297 ? 0.22507 0.32576 0.22949 0.01012  -0.03416 -0.04827 731 SER B CA  
5009 C C   . SER B 297 ? 0.17530 0.28560 0.18550 0.00639  -0.03582 -0.05295 731 SER B C   
5010 O O   . SER B 297 ? 0.14406 0.26321 0.15442 0.00765  -0.04024 -0.05397 731 SER B O   
5011 C CB  . SER B 297 ? 0.14021 0.24331 0.14756 0.01557  -0.03629 -0.04541 731 SER B CB  
5012 O OG  . SER B 297 ? 0.13230 0.23870 0.14862 0.01512  -0.03525 -0.04673 731 SER B OG  
5013 N N   . LEU B 298 ? 0.13135 0.24039 0.14669 0.00180  -0.03233 -0.05553 732 LEU B N   
5014 C CA  . LEU B 298 ? 0.14085 0.25802 0.16305 -0.00218 -0.03308 -0.05986 732 LEU B CA  
5015 C C   . LEU B 298 ? 0.14738 0.26159 0.16497 -0.00698 -0.03152 -0.06333 732 LEU B C   
5016 O O   . LEU B 298 ? 0.13855 0.24353 0.15002 -0.00782 -0.02798 -0.06214 732 LEU B O   
5017 C CB  . LEU B 298 ? 0.11875 0.23717 0.15109 -0.00366 -0.02973 -0.06009 732 LEU B CB  
5018 C CG  . LEU B 298 ? 0.11450 0.23503 0.15120 0.00094  -0.03049 -0.05723 732 LEU B CG  
5019 C CD1 . LEU B 298 ? 0.10588 0.22643 0.15067 -0.00060 -0.02648 -0.05722 732 LEU B CD1 
5020 C CD2 . LEU B 298 ? 0.13959 0.27085 0.18005 0.00356  -0.03530 -0.05772 732 LEU B CD2 
5021 N N   . ALA B 299 ? 0.13595 0.25811 0.15677 -0.01017 -0.03409 -0.06771 733 ALA B N   
5022 C CA  . ALA B 299 ? 0.16136 0.28110 0.17968 -0.01553 -0.03222 -0.07227 733 ALA B CA  
5023 C C   . ALA B 299 ? 0.15450 0.26718 0.15962 -0.01484 -0.03211 -0.07196 733 ALA B C   
5024 O O   . ALA B 299 ? 0.20622 0.31155 0.20746 -0.01799 -0.02796 -0.07375 733 ALA B O   
5025 C CB  . ALA B 299 ? 0.13245 0.24695 0.15751 -0.01906 -0.02590 -0.07280 733 ALA B CB  
5026 N N   . ALA B 300 ? 0.15442 0.26937 0.15272 -0.01028 -0.03631 -0.06922 734 ALA B N   
5027 C CA  . ALA B 300 ? 0.16420 0.27346 0.14964 -0.00859 -0.03644 -0.06796 734 ALA B CA  
5028 C C   . ALA B 300 ? 0.16281 0.25972 0.14463 -0.00837 -0.03035 -0.06476 734 ALA B C   
5029 O O   . ALA B 300 ? 0.20098 0.29166 0.17345 -0.00886 -0.02835 -0.06491 734 ALA B O   
5030 C CB  . ALA B 300 ? 0.17351 0.28580 0.15290 -0.01247 -0.03844 -0.07374 734 ALA B CB  
5031 N N   . GLY B 301 ? 0.16551 0.25929 0.15473 -0.00762 -0.02737 -0.06179 735 GLY B N   
5032 C CA  . GLY B 301 ? 0.15153 0.23498 0.13882 -0.00749 -0.02202 -0.05826 735 GLY B CA  
5033 C C   . GLY B 301 ? 0.14772 0.22700 0.13905 -0.01222 -0.01654 -0.06042 735 GLY B C   
5034 O O   . GLY B 301 ? 0.14595 0.21735 0.13620 -0.01228 -0.01188 -0.05716 735 GLY B O   
5035 N N   . ARG B 302 ? 0.14671 0.23115 0.14322 -0.01616 -0.01674 -0.06549 736 ARG B N   
5036 C CA  . ARG B 302 ? 0.14339 0.22395 0.14482 -0.02047 -0.01102 -0.06731 736 ARG B CA  
5037 C C   . ARG B 302 ? 0.14283 0.22381 0.15431 -0.02019 -0.00809 -0.06415 736 ARG B C   
5038 O O   . ARG B 302 ? 0.12619 0.21426 0.14695 -0.02123 -0.00917 -0.06579 736 ARG B O   
5039 C CB  . ARG B 302 ? 0.14596 0.23196 0.15119 -0.02487 -0.01208 -0.07367 736 ARG B CB  
5040 C CG  . ARG B 302 ? 0.15802 0.24467 0.15316 -0.02587 -0.01537 -0.07792 736 ARG B CG  
5041 C CD  . ARG B 302 ? 0.16080 0.25155 0.16076 -0.03129 -0.01560 -0.08475 736 ARG B CD  
5042 N NE  . ARG B 302 ? 0.19640 0.29003 0.18729 -0.03257 -0.02007 -0.08965 736 ARG B NE  
5043 C CZ  . ARG B 302 ? 0.30116 0.40549 0.29391 -0.03295 -0.02675 -0.09251 736 ARG B CZ  
5044 N NH1 . ARG B 302 ? 0.28100 0.39393 0.28449 -0.03189 -0.02954 -0.09086 736 ARG B NH1 
5045 N NH2 . ARG B 302 ? 0.29007 0.39704 0.27361 -0.03434 -0.03072 -0.09706 736 ARG B NH2 
5046 N N   . VAL B 303 ? 0.12983 0.20385 0.13965 -0.01880 -0.00445 -0.05952 737 VAL B N   
5047 C CA  . VAL B 303 ? 0.12024 0.19486 0.13832 -0.01838 -0.00201 -0.05634 737 VAL B CA  
5048 C C   . VAL B 303 ? 0.11886 0.18690 0.13790 -0.02060 0.00459  -0.05403 737 VAL B C   
5049 O O   . VAL B 303 ? 0.19445 0.25537 0.20650 -0.01978 0.00658  -0.05128 737 VAL B O   
5050 C CB  . VAL B 303 ? 0.11878 0.19259 0.13502 -0.01420 -0.00483 -0.05247 737 VAL B CB  
5051 C CG1 . VAL B 303 ? 0.12273 0.19653 0.14619 -0.01422 -0.00209 -0.04962 737 VAL B CG1 
5052 C CG2 . VAL B 303 ? 0.12004 0.20099 0.13673 -0.01154 -0.01076 -0.05419 737 VAL B CG2 
5053 N N   . LEU B 304 ? 0.15491 0.22586 0.18313 -0.02301 0.00813  -0.05447 738 LEU B N   
5054 C CA  . LEU B 304 ? 0.15303 0.21936 0.18430 -0.02485 0.01482  -0.05152 738 LEU B CA  
5055 C C   . LEU B 304 ? 0.14262 0.21220 0.18093 -0.02356 0.01556  -0.04748 738 LEU B C   
5056 O O   . LEU B 304 ? 0.14944 0.22606 0.19572 -0.02379 0.01483  -0.04866 738 LEU B O   
5057 C CB  . LEU B 304 ? 0.10953 0.17656 0.14597 -0.02851 0.01894  -0.05480 738 LEU B CB  
5058 C CG  . LEU B 304 ? 0.10553 0.16960 0.14775 -0.03017 0.02638  -0.05142 738 LEU B CG  
5059 C CD1 . LEU B 304 ? 0.10930 0.16529 0.14467 -0.02932 0.02977  -0.04738 738 LEU B CD1 
5060 C CD2 . LEU B 304 ? 0.10766 0.17157 0.15497 -0.03367 0.03058  -0.05507 738 LEU B CD2 
5061 N N   . ILE B 305 ? 0.18873 0.25365 0.22377 -0.02219 0.01659  -0.04307 739 ILE B N   
5062 C CA  . ILE B 305 ? 0.17340 0.24109 0.21417 -0.02136 0.01723  -0.03940 739 ILE B CA  
5063 C C   . ILE B 305 ? 0.10647 0.17422 0.15336 -0.02359 0.02368  -0.03638 739 ILE B C   
5064 O O   . ILE B 305 ? 0.13580 0.19767 0.17957 -0.02445 0.02755  -0.03367 739 ILE B O   
5065 C CB  . ILE B 305 ? 0.09435 0.15764 0.12965 -0.01914 0.01470  -0.03634 739 ILE B CB  
5066 C CG1 . ILE B 305 ? 0.19100 0.25531 0.22204 -0.01633 0.00870  -0.03869 739 ILE B CG1 
5067 C CG2 . ILE B 305 ? 0.08807 0.15336 0.12867 -0.01924 0.01605  -0.03276 739 ILE B CG2 
5068 C CD1 . ILE B 305 ? 0.16326 0.23007 0.19701 -0.01423 0.00584  -0.03774 739 ILE B CD1 
5069 N N   . ILE B 306 ? 0.13638 0.21100 0.19183 -0.02403 0.02488  -0.03622 740 ILE B N   
5070 C CA  . ILE B 306 ? 0.13618 0.21224 0.19856 -0.02577 0.03126  -0.03285 740 ILE B CA  
5071 C C   . ILE B 306 ? 0.09694 0.17773 0.16369 -0.02477 0.03128  -0.02872 740 ILE B C   
5072 O O   . ILE B 306 ? 0.06581 0.15310 0.13629 -0.02351 0.02847  -0.02999 740 ILE B O   
5073 C CB  . ILE B 306 ? 0.10831 0.18878 0.17779 -0.02738 0.03369  -0.03579 740 ILE B CB  
5074 C CG1 . ILE B 306 ? 0.13195 0.20756 0.19650 -0.02897 0.03339  -0.04049 740 ILE B CG1 
5075 C CG2 . ILE B 306 ? 0.14177 0.22458 0.21963 -0.02863 0.04063  -0.03176 740 ILE B CG2 
5076 C CD1 . ILE B 306 ? 0.14322 0.22295 0.21502 -0.03108 0.03501  -0.04421 740 ILE B CD1 
5077 N N   . LEU B 307 ? 0.09452 0.17239 0.16077 -0.02534 0.03447  -0.02392 741 LEU B N   
5078 C CA  . LEU B 307 ? 0.06741 0.15046 0.13785 -0.02493 0.03451  -0.01992 741 LEU B CA  
5079 C C   . LEU B 307 ? 0.09220 0.17993 0.16817 -0.02366 0.03542  -0.01790 741 LEU B C   
5080 O O   . LEU B 307 ? 0.10738 0.19149 0.18405 -0.02337 0.03840  -0.01551 741 LEU B O   
5081 C CB  . LEU B 307 ? 0.06470 0.14454 0.13473 -0.02596 0.03810  -0.01432 741 LEU B CB  
5082 C CG  . LEU B 307 ? 0.07298 0.15673 0.14546 -0.02528 0.03685  -0.00947 741 LEU B CG  
5083 C CD1 . LEU B 307 ? 0.06190 0.14604 0.13109 -0.02519 0.03159  -0.01189 741 LEU B CD1 
5084 C CD2 . LEU B 307 ? 0.06308 0.14237 0.13450 -0.02512 0.03979  -0.00232 741 LEU B CD2 
5085 N N   . GLU B 308 ? 0.05703 0.15003 0.13445 -0.02205 0.03204  -0.01804 742 GLU B N   
5086 C CA  . GLU B 308 ? 0.06388 0.15834 0.14379 -0.01968 0.03230  -0.01386 742 GLU B CA  
5087 C C   . GLU B 308 ? 0.12125 0.21708 0.20119 -0.01867 0.03188  -0.00856 742 GLU B C   
5088 O O   . GLU B 308 ? 0.05486 0.14768 0.13430 -0.01906 0.03408  -0.00370 742 GLU B O   
5089 C CB  . GLU B 308 ? 0.06150 0.16071 0.14316 -0.01845 0.02941  -0.01822 742 GLU B CB  
5090 C CG  . GLU B 308 ? 0.06280 0.16138 0.14583 -0.01959 0.02991  -0.02273 742 GLU B CG  
5091 C CD  . GLU B 308 ? 0.10324 0.19995 0.18919 -0.01902 0.03264  -0.01940 742 GLU B CD  
5092 O OE1 . GLU B 308 ? 0.06377 0.15933 0.15013 -0.01754 0.03457  -0.01275 742 GLU B OE1 
5093 O OE2 . GLU B 308 ? 0.09714 0.19449 0.18526 -0.02010 0.03260  -0.02345 742 GLU B OE2 
5094 N N   . GLY B 309 ? 0.11872 0.21949 0.19914 -0.01752 0.02889  -0.01017 743 GLY B N   
5095 C CA  . GLY B 309 ? 0.05125 0.15410 0.13183 -0.01721 0.02816  -0.00684 743 GLY B CA  
5096 C C   . GLY B 309 ? 0.05303 0.15707 0.13139 -0.01966 0.02616  -0.00914 743 GLY B C   
5097 O O   . GLY B 309 ? 0.08092 0.18237 0.15794 -0.02146 0.02659  -0.01163 743 GLY B O   
5098 N N   . GLY B 310 ? 0.05116 0.15938 0.12934 -0.01996 0.02400  -0.00865 744 GLY B N   
5099 C CA  . GLY B 310 ? 0.05194 0.16140 0.12893 -0.02287 0.02205  -0.01002 744 GLY B CA  
5100 C C   . GLY B 310 ? 0.12293 0.23127 0.20106 -0.02372 0.02357  -0.00378 744 GLY B C   
5101 O O   . GLY B 310 ? 0.05343 0.15595 0.13264 -0.02346 0.02720  0.00064  744 GLY B O   
5102 N N   . TYR B 311 ? 0.05285 0.16672 0.13100 -0.02450 0.02090  -0.00384 745 TYR B N   
5103 C CA  . TYR B 311 ? 0.08723 0.20114 0.16696 -0.02487 0.02210  0.00162  745 TYR B CA  
5104 C C   . TYR B 311 ? 0.16227 0.27870 0.24181 -0.02866 0.01943  0.00204  745 TYR B C   
5105 O O   . TYR B 311 ? 0.15498 0.27080 0.23591 -0.02930 0.02047  0.00648  745 TYR B O   
5106 C CB  . TYR B 311 ? 0.15217 0.27047 0.23223 -0.02222 0.02189  0.00172  745 TYR B CB  
5107 C CG  . TYR B 311 ? 0.05746 0.17097 0.13891 -0.01922 0.02507  0.00212  745 TYR B CG  
5108 C CD1 . TYR B 311 ? 0.06790 0.17387 0.15201 -0.01835 0.02969  0.00544  745 TYR B CD1 
5109 C CD2 . TYR B 311 ? 0.05959 0.17560 0.14002 -0.01762 0.02362  -0.00176 745 TYR B CD2 
5110 C CE1 . TYR B 311 ? 0.08232 0.18362 0.16869 -0.01637 0.03271  0.00528  745 TYR B CE1 
5111 C CE2 . TYR B 311 ? 0.05079 0.16264 0.13319 -0.01546 0.02627  -0.00095 745 TYR B CE2 
5112 C CZ  . TYR B 311 ? 0.09240 0.19706 0.17813 -0.01493 0.03073  0.00301  745 TYR B CZ  
5113 O OH  . TYR B 311 ? 0.06496 0.16578 0.15352 -0.01322 0.03339  0.00386  745 TYR B OH  
5114 N N   . ASN B 312 ? 0.11168 0.23053 0.18998 -0.03123 0.01593  -0.00320 746 ASN B N   
5115 C CA  . ASN B 312 ? 0.10592 0.22160 0.18320 -0.03470 0.01325  -0.00242 746 ASN B CA  
5116 C C   . ASN B 312 ? 0.17477 0.28146 0.25151 -0.03540 0.01596  0.00084  746 ASN B C   
5117 O O   . ASN B 312 ? 0.10731 0.20541 0.17979 -0.03356 0.01568  -0.00212 746 ASN B O   
5118 C CB  . ASN B 312 ? 0.09708 0.20663 0.16847 -0.03442 0.00764  -0.00890 746 ASN B CB  
5119 C CG  . ASN B 312 ? 0.23368 0.33861 0.30418 -0.03804 0.00465  -0.00816 746 ASN B CG  
5120 O OD1 . ASN B 312 ? 0.10908 0.20657 0.17953 -0.03935 0.00577  -0.00521 746 ASN B OD1 
5121 N ND2 . ASN B 312 ? 0.20222 0.31157 0.27200 -0.03971 0.00088  -0.01097 746 ASN B ND2 
5122 N N   . LEU B 313 ? 0.10609 0.21435 0.18662 -0.03753 0.01850  0.00711  747 LEU B N   
5123 C CA  . LEU B 313 ? 0.09057 0.19103 0.17078 -0.03754 0.02224  0.01096  747 LEU B CA  
5124 C C   . LEU B 313 ? 0.08380 0.17366 0.15876 -0.03812 0.01936  0.00838  747 LEU B C   
5125 O O   . LEU B 313 ? 0.14043 0.22258 0.21188 -0.03638 0.02129  0.00797  747 LEU B O   
5126 C CB  . LEU B 313 ? 0.13364 0.23115 0.21542 -0.03716 0.02452  0.01646  747 LEU B CB  
5127 C CG  . LEU B 313 ? 0.11535 0.21326 0.19733 -0.03379 0.02729  0.01753  747 LEU B CG  
5128 C CD1 . LEU B 313 ? 0.20311 0.29957 0.28515 -0.03429 0.02864  0.02163  747 LEU B CD1 
5129 C CD2 . LEU B 313 ? 0.06334 0.15564 0.14358 -0.03093 0.03158  0.01595  747 LEU B CD2 
5130 N N   . THR B 314 ? 0.13727 0.22545 0.21103 -0.04012 0.01470  0.00647  748 THR B N   
5131 C CA  . THR B 314 ? 0.13619 0.21286 0.20502 -0.03998 0.01207  0.00421  748 THR B CA  
5132 C C   . THR B 314 ? 0.17274 0.24409 0.23581 -0.03641 0.01016  -0.00193 748 THR B C   
5133 O O   . THR B 314 ? 0.12273 0.18577 0.18177 -0.03458 0.01087  -0.00218 748 THR B O   
5134 C CB  . THR B 314 ? 0.12607 0.20202 0.19566 -0.04321 0.00767  0.00307  748 THR B CB  
5135 O OG1 . THR B 314 ? 0.19890 0.28070 0.27451 -0.04679 0.00921  0.00925  748 THR B OG1 
5136 C CG2 . THR B 314 ? 0.17281 0.23633 0.23809 -0.04287 0.00554  0.00125  748 THR B CG2 
5137 N N   . SER B 315 ? 0.11068 0.18738 0.17335 -0.03523 0.00773  -0.00661 749 SER B N   
5138 C CA  . SER B 315 ? 0.16226 0.23490 0.22014 -0.03167 0.00564  -0.01233 749 SER B CA  
5139 C C   . SER B 315 ? 0.09970 0.17101 0.15658 -0.02928 0.00890  -0.01168 749 SER B C   
5140 O O   . SER B 315 ? 0.09289 0.15693 0.14513 -0.02715 0.00768  -0.01389 749 SER B O   
5141 C CB  . SER B 315 ? 0.09255 0.17167 0.15037 -0.03051 0.00291  -0.01714 749 SER B CB  
5142 O OG  . SER B 315 ? 0.19493 0.27385 0.25238 -0.03287 -0.00044 -0.01876 749 SER B OG  
5143 N N   . ILE B 316 ? 0.10276 0.18064 0.16392 -0.02976 0.01302  -0.00853 750 ILE B N   
5144 C CA  . ILE B 316 ? 0.07239 0.14866 0.13265 -0.02796 0.01610  -0.00875 750 ILE B CA  
5145 C C   . ILE B 316 ? 0.14990 0.21756 0.20684 -0.02826 0.01803  -0.00594 750 ILE B C   
5146 O O   . ILE B 316 ? 0.09938 0.16265 0.15251 -0.02647 0.01868  -0.00781 750 ILE B O   
5147 C CB  . ILE B 316 ? 0.06555 0.15055 0.13184 -0.02832 0.02057  -0.00624 750 ILE B CB  
5148 C CG1 . ILE B 316 ? 0.09086 0.17788 0.16131 -0.03069 0.02457  0.00036  750 ILE B CG1 
5149 C CG2 . ILE B 316 ? 0.06157 0.15567 0.13094 -0.02763 0.01885  -0.00847 750 ILE B CG2 
5150 C CD1 . ILE B 316 ? 0.11503 0.20871 0.19121 -0.03013 0.02938  0.00376  750 ILE B CD1 
5151 N N   . SER B 317 ? 0.07867 0.14424 0.13693 -0.03049 0.01893  -0.00137 751 SER B N   
5152 C CA  . SER B 317 ? 0.15383 0.21106 0.20866 -0.03040 0.02083  0.00167  751 SER B CA  
5153 C C   . SER B 317 ? 0.19920 0.24822 0.24773 -0.02849 0.01697  -0.00166 751 SER B C   
5154 O O   . SER B 317 ? 0.17351 0.21721 0.21710 -0.02645 0.01785  -0.00231 751 SER B O   
5155 C CB  . SER B 317 ? 0.10246 0.16007 0.16119 -0.03323 0.02253  0.00775  751 SER B CB  
5156 O OG  . SER B 317 ? 0.11323 0.17881 0.17801 -0.03452 0.02663  0.01173  751 SER B OG  
5157 N N   . GLU B 318 ? 0.13969 0.18769 0.18820 -0.02902 0.01277  -0.00381 752 GLU B N   
5158 C CA  . GLU B 318 ? 0.14335 0.18338 0.18663 -0.02694 0.00945  -0.00649 752 GLU B CA  
5159 C C   . GLU B 318 ? 0.12683 0.16727 0.16631 -0.02347 0.00801  -0.01121 752 GLU B C   
5160 O O   . GLU B 318 ? 0.18043 0.21491 0.21487 -0.02102 0.00722  -0.01179 752 GLU B O   
5161 C CB  . GLU B 318 ? 0.13863 0.17759 0.18324 -0.02836 0.00566  -0.00850 752 GLU B CB  
5162 C CG  . GLU B 318 ? 0.23360 0.26269 0.27549 -0.02808 0.00412  -0.00745 752 GLU B CG  
5163 C CD  . GLU B 318 ? 0.17235 0.19838 0.21621 -0.03035 0.00707  -0.00109 752 GLU B CD  
5164 O OE1 . GLU B 318 ? 0.16692 0.19704 0.21603 -0.03402 0.00757  0.00158  752 GLU B OE1 
5165 O OE2 . GLU B 318 ? 0.23371 0.25387 0.27387 -0.02832 0.00892  0.00146  752 GLU B OE2 
5166 N N   . SER B 319 ? 0.12329 0.17141 0.16546 -0.02313 0.00769  -0.01424 753 SER B N   
5167 C CA  . SER B 319 ? 0.11130 0.16081 0.15104 -0.02003 0.00581  -0.01880 753 SER B CA  
5168 C C   . SER B 319 ? 0.12045 0.16926 0.15789 -0.01901 0.00816  -0.01847 753 SER B C   
5169 O O   . SER B 319 ? 0.12968 0.17526 0.16255 -0.01648 0.00626  -0.02060 753 SER B O   
5170 C CB  . SER B 319 ? 0.08840 0.14671 0.13229 -0.01994 0.00516  -0.02162 753 SER B CB  
5171 O OG  . SER B 319 ? 0.09224 0.15047 0.13638 -0.02020 0.00222  -0.02343 753 SER B OG  
5172 N N   . MET B 320 ? 0.13581 0.18780 0.17634 -0.02092 0.01236  -0.01589 754 MET B N   
5173 C CA  . MET B 320 ? 0.14565 0.19640 0.18373 -0.02031 0.01486  -0.01630 754 MET B CA  
5174 C C   . MET B 320 ? 0.16274 0.20521 0.19450 -0.01947 0.01528  -0.01416 754 MET B C   
5175 O O   . MET B 320 ? 0.14444 0.18479 0.17137 -0.01789 0.01499  -0.01617 754 MET B O   
5176 C CB  . MET B 320 ? 0.08646 0.14159 0.12961 -0.02240 0.01998  -0.01388 754 MET B CB  
5177 C CG  . MET B 320 ? 0.12938 0.18450 0.17121 -0.02205 0.02241  -0.01609 754 MET B CG  
5178 S SD  . MET B 320 ? 0.18419 0.24474 0.23355 -0.02417 0.02884  -0.01359 754 MET B SD  
5179 C CE  . MET B 320 ? 0.08175 0.14294 0.13012 -0.02376 0.02944  -0.01890 754 MET B CE  
5180 N N   . SER B 321 ? 0.14395 0.18215 0.17572 -0.02053 0.01593  -0.00998 755 SER B N   
5181 C CA  A SER B 321 ? 0.15665 0.18698 0.18259 -0.01925 0.01625  -0.00742 755 SER B CA  
5182 C CA  B SER B 321 ? 0.15652 0.18689 0.18240 -0.01923 0.01629  -0.00747 755 SER B CA  
5183 C C   . SER B 321 ? 0.19085 0.21799 0.21171 -0.01615 0.01186  -0.01049 755 SER B C   
5184 O O   . SER B 321 ? 0.32310 0.34607 0.33786 -0.01402 0.01188  -0.01009 755 SER B O   
5185 C CB  A SER B 321 ? 0.10946 0.13642 0.13788 -0.02114 0.01740  -0.00225 755 SER B CB  
5186 C CB  B SER B 321 ? 0.10946 0.13641 0.13773 -0.02112 0.01771  -0.00213 755 SER B CB  
5187 O OG  A SER B 321 ? 0.10579 0.13538 0.13837 -0.02348 0.02205  0.00184  755 SER B OG  
5188 O OG  B SER B 321 ? 0.14733 0.17395 0.17791 -0.02167 0.01397  -0.00317 755 SER B OG  
5189 N N   . MET B 322 ? 0.17435 0.20365 0.19751 -0.01559 0.00825  -0.01339 756 MET B N   
5190 C CA  . MET B 322 ? 0.23559 0.26230 0.25473 -0.01223 0.00442  -0.01601 756 MET B CA  
5191 C C   . MET B 322 ? 0.15348 0.18383 0.16957 -0.01016 0.00353  -0.01931 756 MET B C   
5192 O O   . MET B 322 ? 0.18038 0.20791 0.19114 -0.00727 0.00170  -0.01959 756 MET B O   
5193 C CB  . MET B 322 ? 0.19327 0.22175 0.21571 -0.01198 0.00138  -0.01878 756 MET B CB  
5194 C CG  . MET B 322 ? 0.23033 0.25212 0.25305 -0.01256 0.00037  -0.01672 756 MET B CG  
5195 S SD  . MET B 322 ? 0.37601 0.38926 0.39285 -0.00845 -0.00139 -0.01551 756 MET B SD  
5196 C CE  . MET B 322 ? 0.28874 0.29572 0.30425 -0.01015 0.00208  -0.00902 756 MET B CE  
5197 N N   . CYS B 323 ? 0.14559 0.18262 0.16537 -0.01168 0.00481  -0.02163 757 CYS B N   
5198 C CA  . CYS B 323 ? 0.16989 0.21084 0.18781 -0.01047 0.00390  -0.02510 757 CYS B CA  
5199 C C   . CYS B 323 ? 0.25297 0.29018 0.26503 -0.01045 0.00597  -0.02386 757 CYS B C   
5200 O O   . CYS B 323 ? 0.18942 0.22675 0.19643 -0.00833 0.00369  -0.02581 757 CYS B O   
5201 C CB  . CYS B 323 ? 0.14906 0.19760 0.17336 -0.01241 0.00541  -0.02745 757 CYS B CB  
5202 S SG  . CYS B 323 ? 0.09719 0.15130 0.12744 -0.01185 0.00308  -0.02930 757 CYS B SG  
5203 N N   . THR B 324 ? 0.18532 0.21965 0.19782 -0.01267 0.01037  -0.02054 758 THR B N   
5204 C CA  . THR B 324 ? 0.13018 0.16017 0.13636 -0.01240 0.01294  -0.01921 758 THR B CA  
5205 C C   . THR B 324 ? 0.12971 0.15418 0.12888 -0.00937 0.01077  -0.01712 758 THR B C   
5206 O O   . THR B 324 ? 0.16020 0.18352 0.15248 -0.00766 0.01020  -0.01821 758 THR B O   
5207 C CB  . THR B 324 ? 0.14070 0.16823 0.14921 -0.01482 0.01849  -0.01509 758 THR B CB  
5208 O OG1 . THR B 324 ? 0.21818 0.25130 0.23379 -0.01723 0.02078  -0.01641 758 THR B OG1 
5209 C CG2 . THR B 324 ? 0.13560 0.15849 0.13710 -0.01429 0.02177  -0.01415 758 THR B CG2 
5210 N N   . SER B 325 ? 0.23432 0.25552 0.23523 -0.00870 0.00957  -0.01412 759 SER B N   
5211 C CA  . SER B 325 ? 0.22961 0.24555 0.22509 -0.00550 0.00762  -0.01176 759 SER B CA  
5212 C C   . SER B 325 ? 0.22181 0.24087 0.21341 -0.00228 0.00341  -0.01533 759 SER B C   
5213 O O   . SER B 325 ? 0.25397 0.27062 0.23877 0.00061  0.00258  -0.01392 759 SER B O   
5214 C CB  . SER B 325 ? 0.13785 0.15013 0.13748 -0.00576 0.00667  -0.00911 759 SER B CB  
5215 O OG  . SER B 325 ? 0.14541 0.15287 0.14093 -0.00229 0.00460  -0.00726 759 SER B OG  
5216 N N   . MET B 326 ? 0.19366 0.21875 0.18964 -0.00252 0.00079  -0.01957 760 MET B N   
5217 C CA  . MET B 326 ? 0.14623 0.17551 0.13961 0.00050  -0.00323 -0.02266 760 MET B CA  
5218 C C   . MET B 326 ? 0.16086 0.19366 0.14970 0.00006  -0.00308 -0.02517 760 MET B C   
5219 O O   . MET B 326 ? 0.23392 0.26790 0.21698 0.00291  -0.00569 -0.02558 760 MET B O   
5220 C CB  . MET B 326 ? 0.13219 0.16728 0.13198 0.00046  -0.00563 -0.02618 760 MET B CB  
5221 C CG  . MET B 326 ? 0.13198 0.16361 0.13490 0.00156  -0.00665 -0.02487 760 MET B CG  
5222 S SD  . MET B 326 ? 0.14192 0.16648 0.13971 0.00610  -0.00850 -0.02142 760 MET B SD  
5223 C CE  . MET B 326 ? 0.16219 0.17796 0.15962 0.00368  -0.00481 -0.01629 760 MET B CE  
5224 N N   . LEU B 327 ? 0.24560 0.28024 0.23702 -0.00347 0.00002  -0.02691 761 LEU B N   
5225 C CA  . LEU B 327 ? 0.17222 0.20902 0.15926 -0.00448 0.00064  -0.02990 761 LEU B CA  
5226 C C   . LEU B 327 ? 0.19632 0.22773 0.17386 -0.00263 0.00171  -0.02724 761 LEU B C   
5227 O O   . LEU B 327 ? 0.15586 0.18950 0.12711 -0.00173 -0.00004 -0.02982 761 LEU B O   
5228 C CB  . LEU B 327 ? 0.17149 0.20920 0.16327 -0.00850 0.00502  -0.03134 761 LEU B CB  
5229 C CG  . LEU B 327 ? 0.14675 0.19046 0.14809 -0.01051 0.00500  -0.03364 761 LEU B CG  
5230 C CD1 . LEU B 327 ? 0.12190 0.16570 0.12701 -0.01402 0.01016  -0.03418 761 LEU B CD1 
5231 C CD2 . LEU B 327 ? 0.15632 0.20728 0.15942 -0.00950 0.00046  -0.03808 761 LEU B CD2 
5232 N N   . LEU B 328 ? 0.23867 0.26341 0.21511 -0.00208 0.00455  -0.02200 762 LEU B N   
5233 C CA  . LEU B 328 ? 0.21203 0.23150 0.17976 0.00017  0.00608  -0.01851 762 LEU B CA  
5234 C C   . LEU B 328 ? 0.21988 0.23971 0.18253 0.00463  0.00195  -0.01707 762 LEU B C   
5235 O O   . LEU B 328 ? 0.25644 0.27334 0.21098 0.00714  0.00271  -0.01439 762 LEU B O   
5236 C CB  . LEU B 328 ? 0.21187 0.22467 0.18149 -0.00067 0.01057  -0.01272 762 LEU B CB  
5237 C CG  . LEU B 328 ? 0.23109 0.24287 0.20367 -0.00425 0.01582  -0.01258 762 LEU B CG  
5238 C CD1 . LEU B 328 ? 0.24185 0.24946 0.21967 -0.00548 0.01913  -0.00680 762 LEU B CD1 
5239 C CD2 . LEU B 328 ? 0.16451 0.17381 0.12839 -0.00374 0.01882  -0.01323 762 LEU B CD2 
5240 N N   . GLY B 329 ? 0.20234 0.22579 0.16947 0.00605  -0.00203 -0.01841 763 GLY B N   
5241 C CA  . GLY B 329 ? 0.18066 0.20503 0.14392 0.01065  -0.00571 -0.01679 763 GLY B CA  
5242 C C   . GLY B 329 ? 0.24217 0.26054 0.20782 0.01303  -0.00543 -0.01185 763 GLY B C   
5243 O O   . GLY B 329 ? 0.23821 0.25631 0.20061 0.01736  -0.00769 -0.00948 763 GLY B O   
5244 N N   . ASP B 330 ? 0.30356 0.31732 0.27501 0.01030  -0.00271 -0.01015 764 ASP B N   
5245 C CA  . ASP B 330 ? 0.21291 0.22029 0.18710 0.01180  -0.00237 -0.00593 764 ASP B CA  
5246 C C   . ASP B 330 ? 0.24082 0.25040 0.21874 0.01409  -0.00606 -0.00810 764 ASP B C   
5247 O O   . ASP B 330 ? 0.17913 0.19509 0.16034 0.01313  -0.00820 -0.01283 764 ASP B O   
5248 C CB  . ASP B 330 ? 0.18630 0.18962 0.16635 0.00765  0.00091  -0.00424 764 ASP B CB  
5249 C CG  . ASP B 330 ? 0.29201 0.29284 0.26899 0.00581  0.00523  -0.00127 764 ASP B CG  
5250 O OD1 . ASP B 330 ? 0.34990 0.34935 0.31938 0.00846  0.00606  0.00090  764 ASP B OD1 
5251 O OD2 . ASP B 330 ? 0.25750 0.25805 0.23941 0.00199  0.00797  -0.00085 764 ASP B OD2 
5252 N N   . SER B 331 ? 0.23311 0.23708 0.21078 0.01732  -0.00639 -0.00434 765 SER B N   
5253 C CA  . SER B 331 ? 0.35431 0.35911 0.33500 0.02023  -0.00927 -0.00588 765 SER B CA  
5254 C C   . SER B 331 ? 0.26095 0.26625 0.24885 0.01688  -0.00950 -0.00969 765 SER B C   
5255 O O   . SER B 331 ? 0.29265 0.29358 0.28384 0.01323  -0.00723 -0.00867 765 SER B O   
5256 C CB  . SER B 331 ? 0.34815 0.34518 0.32788 0.02407  -0.00857 -0.00069 765 SER B CB  
5257 O OG  . SER B 331 ? 0.44598 0.44419 0.41883 0.02828  -0.00884 0.00296  765 SER B OG  
5258 N N   . PRO B 332 ? 0.32787 0.33901 0.31836 0.01808  -0.01215 -0.01384 766 PRO B N   
5259 C CA  . PRO B 332 ? 0.29348 0.30530 0.29011 0.01555  -0.01231 -0.01734 766 PRO B CA  
5260 C C   . PRO B 332 ? 0.30815 0.31098 0.30711 0.01566  -0.01141 -0.01553 766 PRO B C   
5261 O O   . PRO B 332 ? 0.30988 0.30713 0.30689 0.01945  -0.01157 -0.01256 766 PRO B O   
5262 C CB  . PRO B 332 ? 0.28284 0.30201 0.28083 0.01853  -0.01525 -0.02094 766 PRO B CB  
5263 C CG  . PRO B 332 ? 0.37445 0.39943 0.36787 0.02039  -0.01665 -0.02045 766 PRO B CG  
5264 C CD  . PRO B 332 ? 0.36161 0.38016 0.34957 0.02170  -0.01513 -0.01545 766 PRO B CD  
5265 N N   . PRO B 333 ? 0.32864 0.32995 0.33195 0.01151  -0.01040 -0.01717 767 PRO B N   
5266 C CA  . PRO B 333 ? 0.40619 0.39892 0.41198 0.01082  -0.00983 -0.01627 767 PRO B CA  
5267 C C   . PRO B 333 ? 0.21543 0.20686 0.22231 0.01434  -0.01167 -0.01931 767 PRO B C   
5268 O O   . PRO B 333 ? 0.40174 0.40020 0.40875 0.01653  -0.01335 -0.02248 767 PRO B O   
5269 C CB  . PRO B 333 ? 0.28593 0.28024 0.29588 0.00516  -0.00880 -0.01781 767 PRO B CB  
5270 C CG  . PRO B 333 ? 0.21579 0.22023 0.22654 0.00432  -0.00940 -0.02114 767 PRO B CG  
5271 C CD  . PRO B 333 ? 0.26320 0.27100 0.26960 0.00724  -0.00972 -0.01990 767 PRO B CD  
5272 N N   . PRO B 340 ? 0.52363 0.53745 0.53681 0.04506  -0.01236 -0.07237 774 PRO B N   
5273 C CA  . PRO B 340 ? 0.45666 0.48125 0.47121 0.04859  -0.01148 -0.07396 774 PRO B CA  
5274 C C   . PRO B 340 ? 0.25621 0.29164 0.27248 0.04382  -0.01214 -0.07462 774 PRO B C   
5275 O O   . PRO B 340 ? 0.33657 0.36962 0.35136 0.03805  -0.01298 -0.07589 774 PRO B O   
5276 C CB  . PRO B 340 ? 0.31127 0.32738 0.32131 0.05214  -0.00963 -0.07915 774 PRO B CB  
5277 C CG  . PRO B 340 ? 0.52925 0.52973 0.53667 0.05167  -0.00938 -0.07944 774 PRO B CG  
5278 C CD  . PRO B 340 ? 0.48353 0.48343 0.49246 0.04513  -0.01137 -0.07643 774 PRO B CD  
5279 N N   . LEU B 341 ? 0.16271 0.21053 0.18274 0.04646  -0.01156 -0.07334 775 LEU B N   
5280 C CA  . LEU B 341 ? 0.16058 0.21981 0.18351 0.04271  -0.01161 -0.07291 775 LEU B CA  
5281 C C   . LEU B 341 ? 0.18784 0.24955 0.20777 0.04341  -0.01038 -0.07723 775 LEU B C   
5282 O O   . LEU B 341 ? 0.29354 0.35054 0.30988 0.04804  -0.00915 -0.08052 775 LEU B O   
5283 C CB  . LEU B 341 ? 0.15662 0.22824 0.18586 0.04486  -0.01135 -0.06935 775 LEU B CB  
5284 C CG  . LEU B 341 ? 0.14043 0.21197 0.17249 0.04615  -0.01261 -0.06549 775 LEU B CG  
5285 C CD1 . LEU B 341 ? 0.12981 0.21495 0.16860 0.04611  -0.01263 -0.06281 775 LEU B CD1 
5286 C CD2 . LEU B 341 ? 0.14098 0.20450 0.17095 0.04147  -0.01407 -0.06386 775 LEU B CD2 
5287 N N   . LYS B 342 ? 0.25323 0.32257 0.27444 0.03895  -0.01049 -0.07706 776 LYS B N   
5288 C CA  . LYS B 342 ? 0.21121 0.28704 0.23048 0.04024  -0.00920 -0.08009 776 LYS B CA  
5289 C C   . LYS B 342 ? 0.17561 0.26107 0.19868 0.04626  -0.00722 -0.07870 776 LYS B C   
5290 O O   . LYS B 342 ? 0.13786 0.22940 0.16704 0.04710  -0.00719 -0.07465 776 LYS B O   
5291 C CB  . LYS B 342 ? 0.26456 0.34838 0.28560 0.03460  -0.00952 -0.07884 776 LYS B CB  
5292 C CG  . LYS B 342 ? 0.38484 0.46042 0.40260 0.02854  -0.01144 -0.08007 776 LYS B CG  
5293 C CD  . LYS B 342 ? 0.24934 0.33407 0.26983 0.02338  -0.01150 -0.07776 776 LYS B CD  
5294 C CE  . LYS B 342 ? 0.31049 0.40677 0.33082 0.02555  -0.00995 -0.07888 776 LYS B CE  
5295 N NZ  . LYS B 342 ? 0.29167 0.39642 0.31404 0.02062  -0.00999 -0.07662 776 LYS B NZ  
5296 N N   . THR B 343 ? 0.22410 0.31084 0.24346 0.05050  -0.00553 -0.08220 777 THR B N   
5297 C CA  . THR B 343 ? 0.15764 0.25315 0.18064 0.05687  -0.00326 -0.08074 777 THR B CA  
5298 C C   . THR B 343 ? 0.19900 0.30900 0.23016 0.05533  -0.00255 -0.07613 777 THR B C   
5299 O O   . THR B 343 ? 0.13159 0.24785 0.16915 0.05823  -0.00194 -0.07278 777 THR B O   
5300 C CB  . THR B 343 ? 0.16388 0.25943 0.18093 0.06115  -0.00118 -0.08527 777 THR B CB  
5301 O OG1 . THR B 343 ? 0.37866 0.46072 0.38969 0.06451  -0.00092 -0.08912 777 THR B OG1 
5302 C CG2 . THR B 343 ? 0.15524 0.26336 0.17716 0.06686  0.00160  -0.08283 777 THR B CG2 
5303 N N   . SER B 344 ? 0.17138 0.28686 0.20290 0.05056  -0.00261 -0.07573 778 SER B N   
5304 C CA  . SER B 344 ? 0.16263 0.29135 0.20218 0.04910  -0.00125 -0.07133 778 SER B CA  
5305 C C   . SER B 344 ? 0.15936 0.28837 0.20531 0.04653  -0.00245 -0.06754 778 SER B C   
5306 O O   . SER B 344 ? 0.10362 0.24212 0.15721 0.04767  -0.00123 -0.06429 778 SER B O   
5307 C CB  . SER B 344 ? 0.11492 0.24832 0.15344 0.04436  -0.00101 -0.07114 778 SER B CB  
5308 O OG  . SER B 344 ? 0.11449 0.24027 0.15126 0.03844  -0.00329 -0.07105 778 SER B OG  
5309 N N   . ALA B 345 ? 0.14746 0.26624 0.19040 0.04296  -0.00479 -0.06798 779 ALA B N   
5310 C CA  . ALA B 345 ? 0.10779 0.22635 0.15541 0.04063  -0.00604 -0.06477 779 ALA B CA  
5311 C C   . ALA B 345 ? 0.15741 0.27746 0.20805 0.04567  -0.00633 -0.06373 779 ALA B C   
5312 O O   . ALA B 345 ? 0.18654 0.31322 0.24365 0.04495  -0.00661 -0.06084 779 ALA B O   
5313 C CB  . ALA B 345 ? 0.20727 0.31427 0.25027 0.03653  -0.00817 -0.06531 779 ALA B CB  
5314 N N   . THR B 346 ? 0.21766 0.33160 0.26382 0.05071  -0.00624 -0.06607 780 THR B N   
5315 C CA  . THR B 346 ? 0.16272 0.27945 0.21217 0.05637  -0.00609 -0.06461 780 THR B CA  
5316 C C   . THR B 346 ? 0.11388 0.24473 0.17092 0.05876  -0.00414 -0.06250 780 THR B C   
5317 O O   . THR B 346 ? 0.10965 0.24720 0.17330 0.06009  -0.00473 -0.05963 780 THR B O   
5318 C CB  . THR B 346 ? 0.13331 0.24091 0.17653 0.06179  -0.00534 -0.06755 780 THR B CB  
5319 O OG1 . THR B 346 ? 0.18454 0.27878 0.22207 0.05946  -0.00704 -0.06892 780 THR B OG1 
5320 C CG2 . THR B 346 ? 0.15163 0.26324 0.19883 0.06837  -0.00470 -0.06539 780 THR B CG2 
5321 N N   . VAL B 347 ? 0.12502 0.26107 0.18148 0.05923  -0.00183 -0.06369 781 VAL B N   
5322 C CA  . VAL B 347 ? 0.10602 0.25578 0.17026 0.06148  0.00057  -0.06115 781 VAL B CA  
5323 C C   . VAL B 347 ? 0.10572 0.26211 0.17762 0.05604  0.00003  -0.05755 781 VAL B C   
5324 O O   . VAL B 347 ? 0.23782 0.39771 0.31465 0.05533  0.00028  -0.05322 781 VAL B O   
5325 C CB  . VAL B 347 ? 0.10778 0.26150 0.16881 0.06300  0.00328  -0.06288 781 VAL B CB  
5326 C CG1 . VAL B 347 ? 0.10519 0.26538 0.17037 0.06244  0.00539  -0.05707 781 VAL B CG1 
5327 C CG2 . VAL B 347 ? 0.12032 0.26555 0.17243 0.06788  0.00384  -0.06708 781 VAL B CG2 
5328 N N   . SER B 348 ? 0.09173 0.24500 0.16205 0.05034  -0.00080 -0.05802 782 SER B N   
5329 C CA  . SER B 348 ? 0.13096 0.28809 0.20723 0.04480  -0.00081 -0.05468 782 SER B CA  
5330 C C   . SER B 348 ? 0.11633 0.27349 0.19657 0.04456  -0.00316 -0.05364 782 SER B C   
5331 O O   . SER B 348 ? 0.07948 0.23929 0.16419 0.04208  -0.00273 -0.04990 782 SER B O   
5332 C CB  . SER B 348 ? 0.08057 0.23398 0.15419 0.03954  -0.00109 -0.05554 782 SER B CB  
5333 O OG  . SER B 348 ? 0.15519 0.31192 0.22676 0.03952  0.00103  -0.05604 782 SER B OG  
5334 N N   . ILE B 349 ? 0.12677 0.27510 0.20161 0.04538  -0.00577 -0.05532 783 ILE B N   
5335 C CA  . ILE B 349 ? 0.10579 0.25398 0.18303 0.04526  -0.00835 -0.05401 783 ILE B CA  
5336 C C   . ILE B 349 ? 0.11446 0.27183 0.19816 0.05028  -0.00815 -0.05254 783 ILE B C   
5337 O O   . ILE B 349 ? 0.11931 0.28200 0.20857 0.04845  -0.00938 -0.05035 783 ILE B O   
5338 C CB  . ILE B 349 ? 0.09968 0.23545 0.16882 0.04583  -0.01070 -0.05514 783 ILE B CB  
5339 C CG1 . ILE B 349 ? 0.09525 0.22307 0.15956 0.04021  -0.01101 -0.05584 783 ILE B CG1 
5340 C CG2 . ILE B 349 ? 0.13600 0.27294 0.20715 0.04703  -0.01339 -0.05340 783 ILE B CG2 
5341 C CD1 . ILE B 349 ? 0.12394 0.23992 0.18147 0.04013  -0.01314 -0.05621 783 ILE B CD1 
5342 N N   . ASN B 350 ? 0.15555 0.31349 0.23762 0.05594  -0.00637 -0.05330 784 ASN B N   
5343 C CA  . ASN B 350 ? 0.11822 0.28072 0.20373 0.06006  -0.00562 -0.05034 784 ASN B CA  
5344 C C   . ASN B 350 ? 0.16748 0.33486 0.25813 0.05563  -0.00380 -0.04616 784 ASN B C   
5345 O O   . ASN B 350 ? 0.09094 0.26267 0.18703 0.05553  -0.00453 -0.04311 784 ASN B O   
5346 C CB  . ASN B 350 ? 0.10477 0.26442 0.18578 0.06684  -0.00357 -0.05208 784 ASN B CB  
5347 C CG  . ASN B 350 ? 0.16840 0.33230 0.25162 0.06853  -0.00068 -0.04866 784 ASN B CG  
5348 O OD1 . ASN B 350 ? 0.31943 0.48757 0.40774 0.06997  -0.00089 -0.04509 784 ASN B OD1 
5349 N ND2 . ASN B 350 ? 0.21475 0.37800 0.29439 0.06853  0.00197  -0.04958 784 ASN B ND2 
5350 N N   . ASN B 351 ? 0.15497 0.32141 0.24431 0.05193  -0.00165 -0.04593 785 ASN B N   
5351 C CA  . ASN B 351 ? 0.13843 0.30802 0.23276 0.04835  0.00062  -0.04162 785 ASN B CA  
5352 C C   . ASN B 351 ? 0.08009 0.25073 0.17961 0.04295  -0.00087 -0.04007 785 ASN B C   
5353 O O   . ASN B 351 ? 0.07906 0.25311 0.18487 0.04140  -0.00000 -0.03669 785 ASN B O   
5354 C CB  . ASN B 351 ? 0.12152 0.28960 0.21289 0.04627  0.00336  -0.04117 785 ASN B CB  
5355 C CG  . ASN B 351 ? 0.12555 0.29403 0.21226 0.05147  0.00520  -0.04236 785 ASN B CG  
5356 O OD1 . ASN B 351 ? 0.09376 0.26343 0.18044 0.05660  0.00530  -0.04255 785 ASN B OD1 
5357 N ND2 . ASN B 351 ? 0.08848 0.25617 0.17109 0.05026  0.00672  -0.04313 785 ASN B ND2 
5358 N N   . VAL B 352 ? 0.13026 0.29801 0.22753 0.04005  -0.00300 -0.04268 786 VAL B N   
5359 C CA  . VAL B 352 ? 0.07434 0.24285 0.17562 0.03504  -0.00440 -0.04193 786 VAL B CA  
5360 C C   . VAL B 352 ? 0.07658 0.24931 0.18122 0.03699  -0.00751 -0.04181 786 VAL B C   
5361 O O   . VAL B 352 ? 0.07547 0.25172 0.18579 0.03410  -0.00797 -0.03993 786 VAL B O   
5362 C CB  . VAL B 352 ? 0.10380 0.26800 0.20146 0.03148  -0.00548 -0.04460 786 VAL B CB  
5363 C CG1 . VAL B 352 ? 0.07976 0.24437 0.18105 0.02617  -0.00630 -0.04407 786 VAL B CG1 
5364 C CG2 . VAL B 352 ? 0.07005 0.23089 0.16436 0.03000  -0.00261 -0.04437 786 VAL B CG2 
5365 N N   . LEU B 353 ? 0.08031 0.25279 0.18174 0.04204  -0.00974 -0.04371 787 LEU B N   
5366 C CA  . LEU B 353 ? 0.08341 0.26035 0.18771 0.04494  -0.01264 -0.04273 787 LEU B CA  
5367 C C   . LEU B 353 ? 0.08444 0.26683 0.19500 0.04581  -0.01109 -0.03899 787 LEU B C   
5368 O O   . LEU B 353 ? 0.08442 0.27191 0.20036 0.04403  -0.01307 -0.03737 787 LEU B O   
5369 C CB  . LEU B 353 ? 0.08850 0.26323 0.18836 0.05172  -0.01401 -0.04436 787 LEU B CB  
5370 C CG  . LEU B 353 ? 0.15821 0.32953 0.25416 0.05240  -0.01729 -0.04707 787 LEU B CG  
5371 C CD1 . LEU B 353 ? 0.09795 0.26165 0.18744 0.05871  -0.01717 -0.04718 787 LEU B CD1 
5372 C CD2 . LEU B 353 ? 0.18691 0.36260 0.28553 0.04984  -0.02105 -0.04600 787 LEU B CD2 
5373 N N   . ARG B 354 ? 0.09382 0.27552 0.20393 0.04853  -0.00763 -0.03762 788 ARG B N   
5374 C CA  . ARG B 354 ? 0.11066 0.29737 0.22723 0.04972  -0.00579 -0.03373 788 ARG B CA  
5375 C C   . ARG B 354 ? 0.08286 0.27164 0.20600 0.04364  -0.00479 -0.03152 788 ARG B C   
5376 O O   . ARG B 354 ? 0.08321 0.27748 0.21381 0.04267  -0.00565 -0.02908 788 ARG B O   
5377 C CB  . ARG B 354 ? 0.09017 0.27524 0.20392 0.05406  -0.00215 -0.03301 788 ARG B CB  
5378 C CG  . ARG B 354 ? 0.14043 0.33058 0.26048 0.05691  -0.00028 -0.02908 788 ARG B CG  
5379 C CD  . ARG B 354 ? 0.19487 0.38337 0.31206 0.06011  0.00376  -0.02834 788 ARG B CD  
5380 N NE  . ARG B 354 ? 0.13296 0.31695 0.24123 0.06492  0.00399  -0.03193 788 ARG B NE  
5381 C CZ  . ARG B 354 ? 0.16784 0.34744 0.26945 0.06405  0.00506  -0.03476 788 ARG B CZ  
5382 N NH1 . ARG B 354 ? 0.17360 0.35268 0.27608 0.05882  0.00621  -0.03383 788 ARG B NH1 
5383 N NH2 . ARG B 354 ? 0.17657 0.35204 0.27072 0.06866  0.00505  -0.03855 788 ARG B NH2 
5384 N N   . ALA B 355 ? 0.09124 0.27567 0.21217 0.03958  -0.00293 -0.03222 789 ALA B N   
5385 C CA  . ALA B 355 ? 0.07604 0.26125 0.20329 0.03437  -0.00126 -0.02981 789 ALA B CA  
5386 C C   . ALA B 355 ? 0.07485 0.26259 0.20591 0.03017  -0.00447 -0.03101 789 ALA B C   
5387 O O   . ALA B 355 ? 0.07386 0.26446 0.21239 0.02682  -0.00379 -0.02891 789 ALA B O   
5388 C CB  . ALA B 355 ? 0.07316 0.25272 0.19669 0.03151  0.00156  -0.02988 789 ALA B CB  
5389 N N   . HIS B 356 ? 0.07550 0.26239 0.20178 0.03035  -0.00801 -0.03443 790 HIS B N   
5390 C CA  . HIS B 356 ? 0.12505 0.31403 0.25348 0.02611  -0.01125 -0.03624 790 HIS B CA  
5391 C C   . HIS B 356 ? 0.09904 0.29437 0.22975 0.02854  -0.01540 -0.03617 790 HIS B C   
5392 O O   . HIS B 356 ? 0.07931 0.27748 0.21176 0.02506  -0.01859 -0.03767 790 HIS B O   
5393 C CB  . HIS B 356 ? 0.07337 0.25680 0.19512 0.02361  -0.01225 -0.03985 790 HIS B CB  
5394 C CG  . HIS B 356 ? 0.07002 0.24898 0.19231 0.01865  -0.00905 -0.03968 790 HIS B CG  
5395 N ND1 . HIS B 356 ? 0.06934 0.24929 0.19622 0.01347  -0.00910 -0.04007 790 HIS B ND1 
5396 C CD2 . HIS B 356 ? 0.08326 0.25692 0.20232 0.01830  -0.00556 -0.03885 790 HIS B CD2 
5397 C CE1 . HIS B 356 ? 0.14693 0.32188 0.27347 0.01048  -0.00547 -0.03923 790 HIS B CE1 
5398 N NE2 . HIS B 356 ? 0.06569 0.23698 0.18751 0.01332  -0.00339 -0.03816 790 HIS B NE2 
5399 N N   . ALA B 357 ? 0.13558 0.33324 0.26613 0.03446  -0.01536 -0.03437 791 ALA B N   
5400 C CA  . ALA B 357 ? 0.08536 0.28987 0.21945 0.03713  -0.01877 -0.03294 791 ALA B CA  
5401 C C   . ALA B 357 ? 0.16733 0.37856 0.31043 0.03286  -0.02011 -0.03127 791 ALA B C   
5402 O O   . ALA B 357 ? 0.10934 0.32538 0.25354 0.03177  -0.02445 -0.03198 791 ALA B O   
5403 C CB  . ALA B 357 ? 0.08873 0.29449 0.22294 0.04411  -0.01700 -0.03038 791 ALA B CB  
5404 N N   . PRO B 358 ? 0.08331 0.29535 0.23312 0.03034  -0.01684 -0.02901 792 PRO B N   
5405 C CA  . PRO B 358 ? 0.15310 0.37189 0.31249 0.02630  -0.01843 -0.02759 792 PRO B CA  
5406 C C   . PRO B 358 ? 0.10063 0.31949 0.25910 0.02023  -0.02160 -0.03123 792 PRO B C   
5407 O O   . PRO B 358 ? 0.10268 0.32824 0.26702 0.01754  -0.02490 -0.03117 792 PRO B O   
5408 C CB  . PRO B 358 ? 0.08160 0.29915 0.24743 0.02496  -0.01353 -0.02449 792 PRO B CB  
5409 C CG  . PRO B 358 ? 0.07915 0.28839 0.23713 0.02641  -0.00990 -0.02531 792 PRO B CG  
5410 C CD  . PRO B 358 ? 0.08121 0.28882 0.23091 0.03151  -0.01170 -0.02712 792 PRO B CD  
5411 N N   . PHE B 359 ? 0.08154 0.29325 0.23283 0.01793  -0.02074 -0.03452 793 PHE B N   
5412 C CA  . PHE B 359 ? 0.08175 0.29240 0.23213 0.01188  -0.02276 -0.03823 793 PHE B CA  
5413 C C   . PHE B 359 ? 0.11891 0.32907 0.26152 0.01238  -0.02722 -0.04161 793 PHE B C   
5414 O O   . PHE B 359 ? 0.10120 0.31267 0.24340 0.00780  -0.03012 -0.04458 793 PHE B O   
5415 C CB  . PHE B 359 ? 0.07799 0.28096 0.22647 0.00851  -0.01841 -0.03927 793 PHE B CB  
5416 C CG  . PHE B 359 ? 0.09402 0.29603 0.24806 0.00932  -0.01347 -0.03507 793 PHE B CG  
5417 C CD1 . PHE B 359 ? 0.10212 0.30880 0.26611 0.00668  -0.01252 -0.03262 793 PHE B CD1 
5418 C CD2 . PHE B 359 ? 0.07345 0.27012 0.22284 0.01273  -0.00991 -0.03339 793 PHE B CD2 
5419 C CE1 . PHE B 359 ? 0.13183 0.33769 0.30114 0.00783  -0.00785 -0.02802 793 PHE B CE1 
5420 C CE2 . PHE B 359 ? 0.07198 0.26781 0.22592 0.01371  -0.00547 -0.02915 793 PHE B CE2 
5421 C CZ  . PHE B 359 ? 0.07251 0.27281 0.23649 0.01145  -0.00431 -0.02620 793 PHE B CZ  
5422 N N   . TRP B 360 ? 0.08466 0.29281 0.22101 0.01787  -0.02783 -0.04119 794 TRP B N   
5423 C CA  . TRP B 360 ? 0.08708 0.29380 0.21567 0.01898  -0.03163 -0.04371 794 TRP B CA  
5424 C C   . TRP B 360 ? 0.09108 0.30286 0.21911 0.02521  -0.03453 -0.04116 794 TRP B C   
5425 O O   . TRP B 360 ? 0.09096 0.30004 0.21605 0.03084  -0.03291 -0.03981 794 TRP B O   
5426 C CB  . TRP B 360 ? 0.08402 0.28221 0.20546 0.01945  -0.02932 -0.04572 794 TRP B CB  
5427 C CG  . TRP B 360 ? 0.08049 0.27411 0.20317 0.01367  -0.02603 -0.04738 794 TRP B CG  
5428 C CD1 . TRP B 360 ? 0.10131 0.29086 0.22578 0.01319  -0.02108 -0.04589 794 TRP B CD1 
5429 C CD2 . TRP B 360 ? 0.08140 0.27415 0.20373 0.00769  -0.02723 -0.05050 794 TRP B CD2 
5430 N NE1 . TRP B 360 ? 0.07482 0.26089 0.20042 0.00758  -0.01895 -0.04745 794 TRP B NE1 
5431 C CE2 . TRP B 360 ? 0.07771 0.26551 0.20219 0.00407  -0.02251 -0.05064 794 TRP B CE2 
5432 C CE3 . TRP B 360 ? 0.08943 0.28486 0.20921 0.00521  -0.03177 -0.05312 794 TRP B CE3 
5433 C CZ2 . TRP B 360 ? 0.10855 0.29377 0.23335 -0.00182 -0.02182 -0.05356 794 TRP B CZ2 
5434 C CZ3 . TRP B 360 ? 0.14093 0.33372 0.26029 -0.00092 -0.03133 -0.05649 794 TRP B CZ3 
5435 C CH2 . TRP B 360 ? 0.08272 0.27038 0.20497 -0.00434 -0.02621 -0.05682 794 TRP B CH2 
5436 N N   . SER B 361 ? 0.09534 0.31442 0.22613 0.02415  -0.03878 -0.04055 795 SER B N   
5437 C CA  . SER B 361 ? 0.09988 0.32479 0.23103 0.02991  -0.04162 -0.03736 795 SER B CA  
5438 C C   . SER B 361 ? 0.10199 0.32267 0.22435 0.03508  -0.04299 -0.03764 795 SER B C   
5439 O O   . SER B 361 ? 0.11580 0.33922 0.23800 0.04143  -0.04382 -0.03448 795 SER B O   
5440 C CB  . SER B 361 ? 0.10459 0.33811 0.23951 0.02682  -0.04641 -0.03697 795 SER B CB  
5441 O OG  . SER B 361 ? 0.10946 0.34912 0.24482 0.03244  -0.04920 -0.03330 795 SER B OG  
5442 N N   . SER B 362 ? 0.10030 0.31417 0.21582 0.03278  -0.04300 -0.04103 796 SER B N   
5443 C CA  . SER B 362 ? 0.10251 0.31195 0.21020 0.03759  -0.04436 -0.04114 796 SER B CA  
5444 C C   . SER B 362 ? 0.10007 0.30326 0.20624 0.04249  -0.04045 -0.04081 796 SER B C   
5445 O O   . SER B 362 ? 0.20089 0.40027 0.30172 0.04756  -0.04131 -0.04052 796 SER B O   
5446 C CB  . SER B 362 ? 0.10238 0.30716 0.20345 0.03312  -0.04614 -0.04468 796 SER B CB  
5447 O OG  . SER B 362 ? 0.13877 0.33675 0.23944 0.02958  -0.04229 -0.04733 796 SER B OG  
5448 N N   . LEU B 363 ? 0.09603 0.29787 0.20647 0.04129  -0.03621 -0.04076 797 LEU B N   
5449 C CA  . LEU B 363 ? 0.09981 0.29564 0.20794 0.04545  -0.03249 -0.04098 797 LEU B CA  
5450 C C   . LEU B 363 ? 0.09909 0.29710 0.20850 0.05302  -0.03178 -0.03789 797 LEU B C   
5451 O O   . LEU B 363 ? 0.16760 0.37209 0.28005 0.05510  -0.03419 -0.03505 797 LEU B O   
5452 C CB  . LEU B 363 ? 0.10641 0.29985 0.21750 0.04145  -0.02808 -0.04163 797 LEU B CB  
5453 C CG  . LEU B 363 ? 0.16722 0.35641 0.27658 0.03478  -0.02730 -0.04447 797 LEU B CG  
5454 C CD1 . LEU B 363 ? 0.08126 0.26843 0.19390 0.03184  -0.02259 -0.04376 797 LEU B CD1 
5455 C CD2 . LEU B 363 ? 0.08502 0.26782 0.18742 0.03589  -0.02803 -0.04698 797 LEU B CD2 
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