data_9G67
# 
_entry.id   9G67 
# 
_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   9G67         pdb_00009g67 10.2210/pdb9g67/pdb 
WWPDB D_1292138274 ?            ?                   
# 
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 2025-01-15 ? 
2 'Structure model' 1 1 2025-03-19 ? 
# 
_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                        9G67 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 7os3 unspecified 
PDB . 7os5 unspecified 
PDB . 7os6 unspecified 
PDB . 7ou1 unspecified 
PDB . 7oz6 unspecified 
PDB . 8clz unspecified 
PDB . 8cly unspecified 
PDB . 8ori unspecified 
PDB . 8col unspecified 
PDB . 8osw unspecified 
PDB . 8rua unspecified 
PDB . 8rud unspecified 
PDB . 8rue unspecified 
PDB . 8ruf unspecified 
PDB . 8rug unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mariuszj@amu.edu.pl 
_pdbx_contact_author.name_first         Mariusz 
_pdbx_contact_author.name_last          Jaskolski 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1587-6489 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pokrywka, K.'      1 0000-0002-8165-5417 
'Grzechowiak, M.'   2 0000-0002-7605-1563 
'Sliwiak, J.'       3 0000-0003-1153-6380 
'Worsztynowicz, P.' 4 0000-0001-8218-0188 
'Loch, J.I.'        5 0000-0002-7345-4527 
'Ruszkowski, M.'    6 0000-0002-4415-3100 
'Gilski, M.'        7 0000-0002-3941-9947 
'Jaskolski, M.'     8 0000-0003-1587-6489 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? UK ? ? primary 'Febs J.'                        ? ? 1742-464X ? ? 292 ? 1159    1173    
;Controlling enzyme activity by mutagenesis and metal exchange to obtain crystal structures of stable substrate complexes of Class 3 l-asparaginase.
;
2025 ? 10.1111/febs.17388         39754186 ? ? 
? ? ? ? ? ? ? UK ? ? 1       Iucrj                            ? ? 2052-2525 ? ? 8   ? 514     531     
'Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.' 2021 ? 10.1107/S2052252521006011 
34258001 ? ? 
? ? ? ? ? ? ? UK ? ? 2       'Nat Commun'                     ? ? 2041-1723 ? ? 12  ? 6717    6717    
'Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.' 2021 ? 10.1038/s41467-021-27105-x 
34795296 ? ? 
? ? ? ? ? ? ? ?  ? ? 3       'Acta Crystallogr D Struct Biol' ? ? 2059-7983 ? ? 79  ? 775     791     
'Rhizobium etli has two L-asparaginases with low sequence identity but similar structure and catalytic center.' 2023 ? 
10.1107/S2059798323005648  37494066 ? ? 
? ? ? ? ? ? ? CH ? ? 4       'Front Chem'                     ? ? 2296-2646 ? ? 12  ? 1381032 1381032 
'Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV.' 2024 ? 
10.3389/fchem.2024.1381032 38638878 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pokrywka, K.'      1  ?                   
primary 'Grzechowiak, M.'   2  ?                   
primary 'Sliwiak, J.'       3  ?                   
primary 'Worsztynowicz, P.' 4  ?                   
primary 'Loch, J.I.'        5  ?                   
primary 'Ruszkowski, M.'    6  ?                   
primary 'Gilski, M.'        7  ?                   
primary 'Jaskolski, M.'     8  ?                   
1       'Loch, J.I.'        9  0000-0002-7345-4527 
1       'Jaskolski, M.'     10 0000-0003-1587-6489 
2       'Loch, J.I.'        11 ?                   
2       'Imiolczyk, B.'     12 ?                   
2       'Sliwiak, J.'       13 ?                   
2       'Wantuch, A.'       14 ?                   
2       'Bejger, M.'        15 0000-0003-1660-9745 
2       'Gilski, M.'        16 0000-0002-3941-9947 
2       'Jaskolski, M.'     17 0000-0003-1587-6489 
3       'Loch, J.I.'        18 0000-0002-7345-4527 
3       'Worsztynowicz, P.' 19 ?                   
3       'Sliwiak, J.'       20 ?                   
3       'Grzechowiak, M.'   21 0000-0002-7605-1563 
3       'Imiolczyk, B.'     22 ?                   
3       'Pokrywka, K.'      23 ?                   
3       'Chwastyk, M.'      24 0000-0003-4054-2632 
3       'Gilski, M.'        25 0000-0002-3941-9947 
3       'Jaskolski, M.'     26 0000-0003-1587-6489 
4       'Pokrywka, K.'      27 ?                   
4       'Grzechowiak, M.'   28 ?                   
4       'Sliwiak, J.'       29 ?                   
4       'Worsztynowicz, P.' 30 ?                   
4       'Loch, J.I.'        31 ?                   
4       'Ruszkowski, M.'    32 ?                   
4       'Gilski, M.'        33 ?                   
4       'Jaskolski, M.'     34 ?                   
# 
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 'L-asparaginase II protein' 39563.836 2   ? K138H ? 'point mutation K138H' 
2 non-polymer syn 1,2-ETHANEDIOL              62.068    14  ? ?     ? ?                      
3 non-polymer syn ASPARAGINE                  132.118   2   ? ?     ? ?                      
4 non-polymer syn 'CHLORIDE ION'              35.453    2   ? ?     ? ?                      
5 non-polymer syn 'CADMIUM ION'               112.411   2   ? ?     ? ?                      
6 water       nat water                       18.015    443 ? ?     ? ?                      
# 
_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       
;GIDPFTMTPSEDFVVTDRGGIVENSHRVHAAVVDAKGRLLYALGNPTRMTLARSAAKPAQALAILETEGVAGYGFDDADI
ALMCASHSSEDRHIARTRAMLSKIKAEEADLRCGGHPSLSEMVNRSWIKQDFIPTAVCSNCSGHHVGMLAGARAIGAGTD
GYHLPDHPMQGRVKRTVAELCDLDAGDVEWGTDGCNLPTPAFPLDRLGRIYAKLASAADGSDAGEGQSTRCAALAHIFRA
MARHPEMVAGEGRYCTMLMRAFDGALVGKLGADASYAIGVRASDATRQLGTDGALGISVKIEDGNLEMLYAVVTELLERL
GIGSPDVRSQLASFHHPQRVNTMGVTTGGVSFPFKLRGSKSNVDDPRLAAVAR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GIDPFTMTPSEDFVVTDRGGIVENSHRVHAAVVDAKGRLLYALGNPTRMTLARSAAKPAQALAILETEGVAGYGFDDADI
ALMCASHSSEDRHIARTRAMLSKIKAEEADLRCGGHPSLSEMVNRSWIKQDFIPTAVCSNCSGHHVGMLAGARAIGAGTD
GYHLPDHPMQGRVKRTVAELCDLDAGDVEWGTDGCNLPTPAFPLDRLGRIYAKLASAADGSDAGEGQSTRCAALAHIFRA
MARHPEMVAGEGRYCTMLMRAFDGALVGKLGADASYAIGVRASDATRQLGTDGALGISVKIEDGNLEMLYAVVTELLERL
GIGSPDVRSQLASFHHPQRVNTMGVTTGGVSFPFKLRGSKSNVDDPRLAAVAR
;
_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 1,2-ETHANEDIOL EDO 
3 ASPARAGINE     ASN 
4 'CHLORIDE ION' CL  
5 'CADMIUM ION'  CD  
6 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ILE n 
1 3   ASP n 
1 4   PRO n 
1 5   PHE n 
1 6   THR n 
1 7   MET n 
1 8   THR n 
1 9   PRO n 
1 10  SER n 
1 11  GLU n 
1 12  ASP n 
1 13  PHE n 
1 14  VAL n 
1 15  VAL n 
1 16  THR n 
1 17  ASP n 
1 18  ARG n 
1 19  GLY n 
1 20  GLY n 
1 21  ILE n 
1 22  VAL n 
1 23  GLU n 
1 24  ASN n 
1 25  SER n 
1 26  HIS n 
1 27  ARG n 
1 28  VAL n 
1 29  HIS n 
1 30  ALA n 
1 31  ALA n 
1 32  VAL n 
1 33  VAL n 
1 34  ASP n 
1 35  ALA n 
1 36  LYS n 
1 37  GLY n 
1 38  ARG n 
1 39  LEU n 
1 40  LEU n 
1 41  TYR n 
1 42  ALA n 
1 43  LEU n 
1 44  GLY n 
1 45  ASN n 
1 46  PRO n 
1 47  THR n 
1 48  ARG n 
1 49  MET n 
1 50  THR n 
1 51  LEU n 
1 52  ALA n 
1 53  ARG n 
1 54  SER n 
1 55  ALA n 
1 56  ALA n 
1 57  LYS n 
1 58  PRO n 
1 59  ALA n 
1 60  GLN n 
1 61  ALA n 
1 62  LEU n 
1 63  ALA n 
1 64  ILE n 
1 65  LEU n 
1 66  GLU n 
1 67  THR n 
1 68  GLU n 
1 69  GLY n 
1 70  VAL n 
1 71  ALA n 
1 72  GLY n 
1 73  TYR n 
1 74  GLY n 
1 75  PHE n 
1 76  ASP n 
1 77  ASP n 
1 78  ALA n 
1 79  ASP n 
1 80  ILE n 
1 81  ALA n 
1 82  LEU n 
1 83  MET n 
1 84  CYS n 
1 85  ALA n 
1 86  SER n 
1 87  HIS n 
1 88  SER n 
1 89  SER n 
1 90  GLU n 
1 91  ASP n 
1 92  ARG n 
1 93  HIS n 
1 94  ILE n 
1 95  ALA n 
1 96  ARG n 
1 97  THR n 
1 98  ARG n 
1 99  ALA n 
1 100 MET n 
1 101 LEU n 
1 102 SER n 
1 103 LYS n 
1 104 ILE n 
1 105 LYS n 
1 106 ALA n 
1 107 GLU n 
1 108 GLU n 
1 109 ALA n 
1 110 ASP n 
1 111 LEU n 
1 112 ARG n 
1 113 CYS n 
1 114 GLY n 
1 115 GLY n 
1 116 HIS n 
1 117 PRO n 
1 118 SER n 
1 119 LEU n 
1 120 SER n 
1 121 GLU n 
1 122 MET n 
1 123 VAL n 
1 124 ASN n 
1 125 ARG n 
1 126 SER n 
1 127 TRP n 
1 128 ILE n 
1 129 LYS n 
1 130 GLN n 
1 131 ASP n 
1 132 PHE n 
1 133 ILE n 
1 134 PRO n 
1 135 THR n 
1 136 ALA n 
1 137 VAL n 
1 138 CYS n 
1 139 SER n 
1 140 ASN n 
1 141 CYS n 
1 142 SER n 
1 143 GLY n 
1 144 HIS n 
1 145 HIS n 
1 146 VAL n 
1 147 GLY n 
1 148 MET n 
1 149 LEU n 
1 150 ALA n 
1 151 GLY n 
1 152 ALA n 
1 153 ARG n 
1 154 ALA n 
1 155 ILE n 
1 156 GLY n 
1 157 ALA n 
1 158 GLY n 
1 159 THR n 
1 160 ASP n 
1 161 GLY n 
1 162 TYR n 
1 163 HIS n 
1 164 LEU n 
1 165 PRO n 
1 166 ASP n 
1 167 HIS n 
1 168 PRO n 
1 169 MET n 
1 170 GLN n 
1 171 GLY n 
1 172 ARG n 
1 173 VAL n 
1 174 LYS n 
1 175 ARG n 
1 176 THR n 
1 177 VAL n 
1 178 ALA n 
1 179 GLU n 
1 180 LEU n 
1 181 CYS n 
1 182 ASP n 
1 183 LEU n 
1 184 ASP n 
1 185 ALA n 
1 186 GLY n 
1 187 ASP n 
1 188 VAL n 
1 189 GLU n 
1 190 TRP n 
1 191 GLY n 
1 192 THR n 
1 193 ASP n 
1 194 GLY n 
1 195 CYS n 
1 196 ASN n 
1 197 LEU n 
1 198 PRO n 
1 199 THR n 
1 200 PRO n 
1 201 ALA n 
1 202 PHE n 
1 203 PRO n 
1 204 LEU n 
1 205 ASP n 
1 206 ARG n 
1 207 LEU n 
1 208 GLY n 
1 209 ARG n 
1 210 ILE n 
1 211 TYR n 
1 212 ALA n 
1 213 LYS n 
1 214 LEU n 
1 215 ALA n 
1 216 SER n 
1 217 ALA n 
1 218 ALA n 
1 219 ASP n 
1 220 GLY n 
1 221 SER n 
1 222 ASP n 
1 223 ALA n 
1 224 GLY n 
1 225 GLU n 
1 226 GLY n 
1 227 GLN n 
1 228 SER n 
1 229 THR n 
1 230 ARG n 
1 231 CYS n 
1 232 ALA n 
1 233 ALA n 
1 234 LEU n 
1 235 ALA n 
1 236 HIS n 
1 237 ILE n 
1 238 PHE n 
1 239 ARG n 
1 240 ALA n 
1 241 MET n 
1 242 ALA n 
1 243 ARG n 
1 244 HIS n 
1 245 PRO n 
1 246 GLU n 
1 247 MET n 
1 248 VAL n 
1 249 ALA n 
1 250 GLY n 
1 251 GLU n 
1 252 GLY n 
1 253 ARG n 
1 254 TYR n 
1 255 CYS n 
1 256 THR n 
1 257 MET n 
1 258 LEU n 
1 259 MET n 
1 260 ARG n 
1 261 ALA n 
1 262 PHE n 
1 263 ASP n 
1 264 GLY n 
1 265 ALA n 
1 266 LEU n 
1 267 VAL n 
1 268 GLY n 
1 269 LYS n 
1 270 LEU n 
1 271 GLY n 
1 272 ALA n 
1 273 ASP n 
1 274 ALA n 
1 275 SER n 
1 276 TYR n 
1 277 ALA n 
1 278 ILE n 
1 279 GLY n 
1 280 VAL n 
1 281 ARG n 
1 282 ALA n 
1 283 SER n 
1 284 ASP n 
1 285 ALA n 
1 286 THR n 
1 287 ARG n 
1 288 GLN n 
1 289 LEU n 
1 290 GLY n 
1 291 THR n 
1 292 ASP n 
1 293 GLY n 
1 294 ALA n 
1 295 LEU n 
1 296 GLY n 
1 297 ILE n 
1 298 SER n 
1 299 VAL n 
1 300 LYS n 
1 301 ILE n 
1 302 GLU n 
1 303 ASP n 
1 304 GLY n 
1 305 ASN n 
1 306 LEU n 
1 307 GLU n 
1 308 MET n 
1 309 LEU n 
1 310 TYR n 
1 311 ALA n 
1 312 VAL n 
1 313 VAL n 
1 314 THR n 
1 315 GLU n 
1 316 LEU n 
1 317 LEU n 
1 318 GLU n 
1 319 ARG n 
1 320 LEU n 
1 321 GLY n 
1 322 ILE n 
1 323 GLY n 
1 324 SER n 
1 325 PRO n 
1 326 ASP n 
1 327 VAL n 
1 328 ARG n 
1 329 SER n 
1 330 GLN n 
1 331 LEU n 
1 332 ALA n 
1 333 SER n 
1 334 PHE n 
1 335 HIS n 
1 336 HIS n 
1 337 PRO n 
1 338 GLN n 
1 339 ARG n 
1 340 VAL n 
1 341 ASN n 
1 342 THR n 
1 343 MET n 
1 344 GLY n 
1 345 VAL n 
1 346 THR n 
1 347 THR n 
1 348 GLY n 
1 349 GLY n 
1 350 VAL n 
1 351 SER n 
1 352 PHE n 
1 353 PRO n 
1 354 PHE n 
1 355 LYS n 
1 356 LEU n 
1 357 ARG n 
1 358 GLY n 
1 359 SER n 
1 360 LYS n 
1 361 SER n 
1 362 ASN n 
1 363 VAL n 
1 364 ASP n 
1 365 ASP n 
1 366 PRO n 
1 367 ARG n 
1 368 LEU n 
1 369 ALA n 
1 370 ALA n 
1 371 VAL n 
1 372 ALA n 
1 373 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                   373 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ansA, RHE_PE00350' 
_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      'Rhizobium etli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     29449 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CD  non-polymer         . 'CADMIUM ION'   ?                 'Cd 2'           112.411 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
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 
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 
# 
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   GLY 1   -5  ?   ?   ?   A . n 
A 1 2   ILE 2   -4  ?   ?   ?   A . n 
A 1 3   ASP 3   -3  ?   ?   ?   A . n 
A 1 4   PRO 4   -2  ?   ?   ?   A . n 
A 1 5   PHE 5   -1  ?   ?   ?   A . n 
A 1 6   THR 6   0   ?   ?   ?   A . n 
A 1 7   MET 7   1   ?   ?   ?   A . n 
A 1 8   THR 8   2   2   THR THR A . n 
A 1 9   PRO 9   3   3   PRO PRO A . n 
A 1 10  SER 10  4   4   SER SER A . n 
A 1 11  GLU 11  5   5   GLU GLU A . n 
A 1 12  ASP 12  6   6   ASP ASP A . n 
A 1 13  PHE 13  7   7   PHE PHE A . n 
A 1 14  VAL 14  8   8   VAL VAL A . n 
A 1 15  VAL 15  9   9   VAL VAL A . n 
A 1 16  THR 16  10  10  THR THR A . n 
A 1 17  ASP 17  11  11  ASP ASP A . n 
A 1 18  ARG 18  12  12  ARG ARG A . n 
A 1 19  GLY 19  13  13  GLY GLY A . n 
A 1 20  GLY 20  14  14  GLY GLY A . n 
A 1 21  ILE 21  15  15  ILE ILE A . n 
A 1 22  VAL 22  16  16  VAL VAL A . n 
A 1 23  GLU 23  17  17  GLU GLU A . n 
A 1 24  ASN 24  18  18  ASN ASN A . n 
A 1 25  SER 25  19  19  SER SER A . n 
A 1 26  HIS 26  20  20  HIS HIS A . n 
A 1 27  ARG 27  21  21  ARG ARG A . n 
A 1 28  VAL 28  22  22  VAL VAL A . n 
A 1 29  HIS 29  23  23  HIS HIS A . n 
A 1 30  ALA 30  24  24  ALA ALA A . n 
A 1 31  ALA 31  25  25  ALA ALA A . n 
A 1 32  VAL 32  26  26  VAL VAL A . n 
A 1 33  VAL 33  27  27  VAL VAL A . n 
A 1 34  ASP 34  28  28  ASP ASP A . n 
A 1 35  ALA 35  29  29  ALA ALA A . n 
A 1 36  LYS 36  30  30  LYS LYS A . n 
A 1 37  GLY 37  31  31  GLY GLY A . n 
A 1 38  ARG 38  32  32  ARG ARG A . n 
A 1 39  LEU 39  33  33  LEU LEU A . n 
A 1 40  LEU 40  34  34  LEU LEU A . n 
A 1 41  TYR 41  35  35  TYR TYR A . n 
A 1 42  ALA 42  36  36  ALA ALA A . n 
A 1 43  LEU 43  37  37  LEU LEU A . n 
A 1 44  GLY 44  38  38  GLY GLY A . n 
A 1 45  ASN 45  39  39  ASN ASN A . n 
A 1 46  PRO 46  40  40  PRO PRO A . n 
A 1 47  THR 47  41  41  THR THR A . n 
A 1 48  ARG 48  42  42  ARG ARG A . n 
A 1 49  MET 49  43  43  MET MET A . n 
A 1 50  THR 50  44  44  THR THR A . n 
A 1 51  LEU 51  45  45  LEU LEU A . n 
A 1 52  ALA 52  46  46  ALA ALA A . n 
A 1 53  ARG 53  47  47  ARG ARG A . n 
A 1 54  SER 54  48  48  SER SER A . n 
A 1 55  ALA 55  49  49  ALA ALA A . n 
A 1 56  ALA 56  50  50  ALA ALA A . n 
A 1 57  LYS 57  51  51  LYS LYS A . n 
A 1 58  PRO 58  52  52  PRO PRO A . n 
A 1 59  ALA 59  53  53  ALA ALA A . n 
A 1 60  GLN 60  54  54  GLN GLN A . n 
A 1 61  ALA 61  55  55  ALA ALA A . n 
A 1 62  LEU 62  56  56  LEU LEU A . n 
A 1 63  ALA 63  57  57  ALA ALA A . n 
A 1 64  ILE 64  58  58  ILE ILE A . n 
A 1 65  LEU 65  59  59  LEU LEU A . n 
A 1 66  GLU 66  60  60  GLU GLU A . n 
A 1 67  THR 67  61  61  THR THR A . n 
A 1 68  GLU 68  62  62  GLU GLU A . n 
A 1 69  GLY 69  63  63  GLY GLY A . n 
A 1 70  VAL 70  64  64  VAL VAL A . n 
A 1 71  ALA 71  65  65  ALA ALA A . n 
A 1 72  GLY 72  66  66  GLY GLY A . n 
A 1 73  TYR 73  67  67  TYR TYR A . n 
A 1 74  GLY 74  68  68  GLY GLY A . n 
A 1 75  PHE 75  69  69  PHE PHE A . n 
A 1 76  ASP 76  70  70  ASP ASP A . n 
A 1 77  ASP 77  71  71  ASP ASP A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  ASP 79  73  73  ASP ASP A . n 
A 1 80  ILE 80  74  74  ILE ILE A . n 
A 1 81  ALA 81  75  75  ALA ALA A . n 
A 1 82  LEU 82  76  76  LEU LEU A . n 
A 1 83  MET 83  77  77  MET MET A . n 
A 1 84  CYS 84  78  78  CYS CYS A . n 
A 1 85  ALA 85  79  79  ALA ALA A . n 
A 1 86  SER 86  80  80  SER SER A . n 
A 1 87  HIS 87  81  81  HIS HIS A . n 
A 1 88  SER 88  82  82  SER SER A . n 
A 1 89  SER 89  83  83  SER SER A . n 
A 1 90  GLU 90  84  84  GLU GLU A . n 
A 1 91  ASP 91  85  85  ASP ASP A . n 
A 1 92  ARG 92  86  86  ARG ARG A . n 
A 1 93  HIS 93  87  87  HIS HIS A . n 
A 1 94  ILE 94  88  88  ILE ILE A . n 
A 1 95  ALA 95  89  89  ALA ALA A . n 
A 1 96  ARG 96  90  90  ARG ARG A . n 
A 1 97  THR 97  91  91  THR THR A . n 
A 1 98  ARG 98  92  92  ARG ARG A . n 
A 1 99  ALA 99  93  93  ALA ALA A . n 
A 1 100 MET 100 94  94  MET MET A . n 
A 1 101 LEU 101 95  95  LEU LEU A . n 
A 1 102 SER 102 96  96  SER SER A . n 
A 1 103 LYS 103 97  97  LYS LYS A . n 
A 1 104 ILE 104 98  98  ILE ILE A . n 
A 1 105 LYS 105 99  99  LYS LYS A . n 
A 1 106 ALA 106 100 100 ALA ALA A . n 
A 1 107 GLU 107 101 101 GLU GLU A . n 
A 1 108 GLU 108 102 102 GLU GLU A . n 
A 1 109 ALA 109 103 103 ALA ALA A . n 
A 1 110 ASP 110 104 104 ASP ASP A . n 
A 1 111 LEU 111 105 105 LEU LEU A . n 
A 1 112 ARG 112 106 106 ARG ARG A . n 
A 1 113 CYS 113 107 107 CYS CYS A . n 
A 1 114 GLY 114 108 108 GLY GLY A . n 
A 1 115 GLY 115 109 109 GLY GLY A . n 
A 1 116 HIS 116 110 110 HIS HIS A . n 
A 1 117 PRO 117 111 111 PRO PRO A . n 
A 1 118 SER 118 112 112 SER SER A . n 
A 1 119 LEU 119 113 113 LEU LEU A . n 
A 1 120 SER 120 114 114 SER SER A . n 
A 1 121 GLU 121 115 115 GLU GLU A . n 
A 1 122 MET 122 116 116 MET MET A . n 
A 1 123 VAL 123 117 117 VAL VAL A . n 
A 1 124 ASN 124 118 118 ASN ASN A . n 
A 1 125 ARG 125 119 119 ARG ARG A . n 
A 1 126 SER 126 120 120 SER SER A . n 
A 1 127 TRP 127 121 121 TRP TRP A . n 
A 1 128 ILE 128 122 122 ILE ILE A . n 
A 1 129 LYS 129 123 123 LYS LYS A . n 
A 1 130 GLN 130 124 124 GLN GLN A . n 
A 1 131 ASP 131 125 125 ASP ASP A . n 
A 1 132 PHE 132 126 126 PHE PHE A . n 
A 1 133 ILE 133 127 127 ILE ILE A . n 
A 1 134 PRO 134 128 128 PRO PRO A . n 
A 1 135 THR 135 129 129 THR THR A . n 
A 1 136 ALA 136 130 130 ALA ALA A . n 
A 1 137 VAL 137 131 131 VAL VAL A . n 
A 1 138 CYS 138 132 132 CYS CYS A . n 
A 1 139 SER 139 133 133 SER SER A . n 
A 1 140 ASN 140 134 134 ASN ASN A . n 
A 1 141 CYS 141 135 135 CYS CYS A . n 
A 1 142 SER 142 136 136 SER SER A . n 
A 1 143 GLY 143 137 137 GLY GLY A . n 
A 1 144 HIS 144 138 138 HIS HIS A . n 
A 1 145 HIS 145 139 139 HIS HIS A . n 
A 1 146 VAL 146 140 140 VAL VAL A . n 
A 1 147 GLY 147 141 141 GLY GLY A . n 
A 1 148 MET 148 142 142 MET MET A . n 
A 1 149 LEU 149 143 143 LEU LEU A . n 
A 1 150 ALA 150 144 144 ALA ALA A . n 
A 1 151 GLY 151 145 145 GLY GLY A . n 
A 1 152 ALA 152 146 146 ALA ALA A . n 
A 1 153 ARG 153 147 147 ARG ARG A . n 
A 1 154 ALA 154 148 148 ALA ALA A . n 
A 1 155 ILE 155 149 149 ILE ILE A . n 
A 1 156 GLY 156 150 150 GLY GLY A . n 
A 1 157 ALA 157 151 151 ALA ALA A . n 
A 1 158 GLY 158 152 152 GLY GLY A . n 
A 1 159 THR 159 153 153 THR THR A . n 
A 1 160 ASP 160 154 154 ASP ASP A . n 
A 1 161 GLY 161 155 155 GLY GLY A . n 
A 1 162 TYR 162 156 156 TYR TYR A . n 
A 1 163 HIS 163 157 157 HIS HIS A . n 
A 1 164 LEU 164 158 158 LEU LEU A . n 
A 1 165 PRO 165 159 159 PRO PRO A . n 
A 1 166 ASP 166 160 160 ASP ASP A . n 
A 1 167 HIS 167 161 161 HIS HIS A . n 
A 1 168 PRO 168 162 162 PRO PRO A . n 
A 1 169 MET 169 163 163 MET MET A . n 
A 1 170 GLN 170 164 164 GLN GLN A . n 
A 1 171 GLY 171 165 165 GLY GLY A . n 
A 1 172 ARG 172 166 166 ARG ARG A . n 
A 1 173 VAL 173 167 167 VAL VAL A . n 
A 1 174 LYS 174 168 168 LYS LYS A . n 
A 1 175 ARG 175 169 169 ARG ARG A . n 
A 1 176 THR 176 170 170 THR THR A . n 
A 1 177 VAL 177 171 171 VAL VAL A . n 
A 1 178 ALA 178 172 172 ALA ALA A . n 
A 1 179 GLU 179 173 173 GLU GLU A . n 
A 1 180 LEU 180 174 174 LEU LEU A . n 
A 1 181 CYS 181 175 175 CYS CYS A . n 
A 1 182 ASP 182 176 176 ASP ASP A . n 
A 1 183 LEU 183 177 177 LEU LEU A . n 
A 1 184 ASP 184 178 178 ASP ASP A . n 
A 1 185 ALA 185 179 179 ALA ALA A . n 
A 1 186 GLY 186 180 180 GLY GLY A . n 
A 1 187 ASP 187 181 181 ASP ASP A . n 
A 1 188 VAL 188 182 182 VAL VAL A . n 
A 1 189 GLU 189 183 183 GLU GLU A . n 
A 1 190 TRP 190 184 184 TRP TRP A . n 
A 1 191 GLY 191 185 185 GLY GLY A . n 
A 1 192 THR 192 186 186 THR THR A . n 
A 1 193 ASP 193 187 187 ASP ASP A . n 
A 1 194 GLY 194 188 188 GLY GLY A . n 
A 1 195 CYS 195 189 189 CYS CYS A . n 
A 1 196 ASN 196 190 190 ASN ASN A . n 
A 1 197 LEU 197 191 191 LEU LEU A . n 
A 1 198 PRO 198 192 192 PRO PRO A . n 
A 1 199 THR 199 193 193 THR THR A . n 
A 1 200 PRO 200 194 194 PRO PRO A . n 
A 1 201 ALA 201 195 195 ALA ALA A . n 
A 1 202 PHE 202 196 196 PHE PHE A . n 
A 1 203 PRO 203 197 197 PRO PRO A . n 
A 1 204 LEU 204 198 198 LEU LEU A . n 
A 1 205 ASP 205 199 199 ASP ASP A . n 
A 1 206 ARG 206 200 200 ARG ARG A . n 
A 1 207 LEU 207 201 201 LEU LEU A . n 
A 1 208 GLY 208 202 202 GLY GLY A . n 
A 1 209 ARG 209 203 203 ARG ARG A . n 
A 1 210 ILE 210 204 204 ILE ILE A . n 
A 1 211 TYR 211 205 205 TYR TYR A . n 
A 1 212 ALA 212 206 206 ALA ALA A . n 
A 1 213 LYS 213 207 207 LYS LYS A . n 
A 1 214 LEU 214 208 208 LEU LEU A . n 
A 1 215 ALA 215 209 209 ALA ALA A . n 
A 1 216 SER 216 210 210 SER SER A . n 
A 1 217 ALA 217 211 211 ALA ALA A . n 
A 1 218 ALA 218 212 212 ALA ALA A . n 
A 1 219 ASP 219 213 213 ASP ASP A . n 
A 1 220 GLY 220 214 214 GLY GLY A . n 
A 1 221 SER 221 215 215 SER SER A . n 
A 1 222 ASP 222 216 216 ASP ASP A . n 
A 1 223 ALA 223 217 217 ALA ALA A . n 
A 1 224 GLY 224 218 218 GLY GLY A . n 
A 1 225 GLU 225 219 219 GLU GLU A . n 
A 1 226 GLY 226 220 220 GLY GLY A . n 
A 1 227 GLN 227 221 221 GLN GLN A . n 
A 1 228 SER 228 222 222 SER SER A . n 
A 1 229 THR 229 223 223 THR THR A . n 
A 1 230 ARG 230 224 224 ARG ARG A . n 
A 1 231 CYS 231 225 225 CYS CYS A . n 
A 1 232 ALA 232 226 226 ALA ALA A . n 
A 1 233 ALA 233 227 227 ALA ALA A . n 
A 1 234 LEU 234 228 228 LEU LEU A . n 
A 1 235 ALA 235 229 229 ALA ALA A . n 
A 1 236 HIS 236 230 230 HIS HIS A . n 
A 1 237 ILE 237 231 231 ILE ILE A . n 
A 1 238 PHE 238 232 232 PHE PHE A . n 
A 1 239 ARG 239 233 233 ARG ARG A . n 
A 1 240 ALA 240 234 234 ALA ALA A . n 
A 1 241 MET 241 235 235 MET MET A . n 
A 1 242 ALA 242 236 236 ALA ALA A . n 
A 1 243 ARG 243 237 237 ARG ARG A . n 
A 1 244 HIS 244 238 238 HIS HIS A . n 
A 1 245 PRO 245 239 239 PRO PRO A . n 
A 1 246 GLU 246 240 240 GLU GLU A . n 
A 1 247 MET 247 241 241 MET MET A . n 
A 1 248 VAL 248 242 242 VAL VAL A . n 
A 1 249 ALA 249 243 243 ALA ALA A . n 
A 1 250 GLY 250 244 244 GLY GLY A . n 
A 1 251 GLU 251 245 245 GLU GLU A . n 
A 1 252 GLY 252 246 246 GLY GLY A . n 
A 1 253 ARG 253 247 247 ARG ARG A . n 
A 1 254 TYR 254 248 248 TYR TYR A . n 
A 1 255 CYS 255 249 249 CYS CYS A . n 
A 1 256 THR 256 250 250 THR THR A . n 
A 1 257 MET 257 251 251 MET MET A . n 
A 1 258 LEU 258 252 252 LEU LEU A . n 
A 1 259 MET 259 253 253 MET MET A . n 
A 1 260 ARG 260 254 254 ARG ARG A . n 
A 1 261 ALA 261 255 255 ALA ALA A . n 
A 1 262 PHE 262 256 256 PHE PHE A . n 
A 1 263 ASP 263 257 257 ASP ASP A . n 
A 1 264 GLY 264 258 258 GLY GLY A . n 
A 1 265 ALA 265 259 259 ALA ALA A . n 
A 1 266 LEU 266 260 260 LEU LEU A . n 
A 1 267 VAL 267 261 261 VAL VAL A . n 
A 1 268 GLY 268 262 262 GLY GLY A . n 
A 1 269 LYS 269 263 263 LYS LYS A . n 
A 1 270 LEU 270 264 264 LEU LEU A . n 
A 1 271 GLY 271 265 265 GLY GLY A . n 
A 1 272 ALA 272 266 266 ALA ALA A . n 
A 1 273 ASP 273 267 267 ASP ASP A . n 
A 1 274 ALA 274 268 268 ALA ALA A . n 
A 1 275 SER 275 269 269 SER SER A . n 
A 1 276 TYR 276 270 270 TYR TYR A . n 
A 1 277 ALA 277 271 271 ALA ALA A . n 
A 1 278 ILE 278 272 272 ILE ILE A . n 
A 1 279 GLY 279 273 273 GLY GLY A . n 
A 1 280 VAL 280 274 274 VAL VAL A . n 
A 1 281 ARG 281 275 275 ARG ARG A . n 
A 1 282 ALA 282 276 276 ALA ALA A . n 
A 1 283 SER 283 277 277 SER SER A . n 
A 1 284 ASP 284 278 278 ASP ASP A . n 
A 1 285 ALA 285 279 279 ALA ALA A . n 
A 1 286 THR 286 280 280 THR THR A . n 
A 1 287 ARG 287 281 281 ARG ARG A . n 
A 1 288 GLN 288 282 282 GLN GLN A . n 
A 1 289 LEU 289 283 283 LEU LEU A . n 
A 1 290 GLY 290 284 284 GLY GLY A . n 
A 1 291 THR 291 285 285 THR THR A . n 
A 1 292 ASP 292 286 286 ASP ASP A . n 
A 1 293 GLY 293 287 287 GLY GLY A . n 
A 1 294 ALA 294 288 288 ALA ALA A . n 
A 1 295 LEU 295 289 289 LEU LEU A . n 
A 1 296 GLY 296 290 290 GLY GLY A . n 
A 1 297 ILE 297 291 291 ILE ILE A . n 
A 1 298 SER 298 292 292 SER SER A . n 
A 1 299 VAL 299 293 293 VAL VAL A . n 
A 1 300 LYS 300 294 294 LYS LYS A . n 
A 1 301 ILE 301 295 295 ILE ILE A . n 
A 1 302 GLU 302 296 296 GLU GLU A . n 
A 1 303 ASP 303 297 297 ASP ASP A . n 
A 1 304 GLY 304 298 298 GLY GLY A . n 
A 1 305 ASN 305 299 299 ASN ASN A . n 
A 1 306 LEU 306 300 300 LEU LEU A . n 
A 1 307 GLU 307 301 301 GLU GLU A . n 
A 1 308 MET 308 302 302 MET MET A . n 
A 1 309 LEU 309 303 303 LEU LEU A . n 
A 1 310 TYR 310 304 304 TYR TYR A . n 
A 1 311 ALA 311 305 305 ALA ALA A . n 
A 1 312 VAL 312 306 306 VAL VAL A . n 
A 1 313 VAL 313 307 307 VAL VAL A . n 
A 1 314 THR 314 308 308 THR THR A . n 
A 1 315 GLU 315 309 309 GLU GLU A . n 
A 1 316 LEU 316 310 310 LEU LEU A . n 
A 1 317 LEU 317 311 311 LEU LEU A . n 
A 1 318 GLU 318 312 312 GLU GLU A . n 
A 1 319 ARG 319 313 313 ARG ARG A . n 
A 1 320 LEU 320 314 314 LEU LEU A . n 
A 1 321 GLY 321 315 315 GLY GLY A . n 
A 1 322 ILE 322 316 316 ILE ILE A . n 
A 1 323 GLY 323 317 317 GLY GLY A . n 
A 1 324 SER 324 318 318 SER SER A . n 
A 1 325 PRO 325 319 319 PRO PRO A . n 
A 1 326 ASP 326 320 320 ASP ASP A . n 
A 1 327 VAL 327 321 321 VAL VAL A . n 
A 1 328 ARG 328 322 322 ARG ARG A . n 
A 1 329 SER 329 323 323 SER SER A . n 
A 1 330 GLN 330 324 324 GLN GLN A . n 
A 1 331 LEU 331 325 325 LEU LEU A . n 
A 1 332 ALA 332 326 326 ALA ALA A . n 
A 1 333 SER 333 327 327 SER SER A . n 
A 1 334 PHE 334 328 328 PHE PHE A . n 
A 1 335 HIS 335 329 329 HIS HIS A . n 
A 1 336 HIS 336 330 330 HIS HIS A . n 
A 1 337 PRO 337 331 331 PRO PRO A . n 
A 1 338 GLN 338 332 332 GLN GLN A . n 
A 1 339 ARG 339 333 333 ARG ARG A . n 
A 1 340 VAL 340 334 334 VAL VAL A . n 
A 1 341 ASN 341 335 335 ASN ASN A . n 
A 1 342 THR 342 336 336 THR THR A . n 
A 1 343 MET 343 337 337 MET MET A . n 
A 1 344 GLY 344 338 338 GLY GLY A . n 
A 1 345 VAL 345 339 339 VAL VAL A . n 
A 1 346 THR 346 340 340 THR THR A . n 
A 1 347 THR 347 341 341 THR THR A . n 
A 1 348 GLY 348 342 342 GLY GLY A . n 
A 1 349 GLY 349 343 343 GLY GLY A . n 
A 1 350 VAL 350 344 344 VAL VAL A . n 
A 1 351 SER 351 345 345 SER SER A . n 
A 1 352 PHE 352 346 346 PHE PHE A . n 
A 1 353 PRO 353 347 347 PRO PRO A . n 
A 1 354 PHE 354 348 348 PHE PHE A . n 
A 1 355 LYS 355 349 349 LYS LYS A . n 
A 1 356 LEU 356 350 350 LEU LEU A . n 
A 1 357 ARG 357 351 351 ARG ARG A . n 
A 1 358 GLY 358 352 352 GLY GLY A . n 
A 1 359 SER 359 353 ?   ?   ?   A . n 
A 1 360 LYS 360 354 ?   ?   ?   A . n 
A 1 361 SER 361 355 ?   ?   ?   A . n 
A 1 362 ASN 362 356 ?   ?   ?   A . n 
A 1 363 VAL 363 357 ?   ?   ?   A . n 
A 1 364 ASP 364 358 ?   ?   ?   A . n 
A 1 365 ASP 365 359 ?   ?   ?   A . n 
A 1 366 PRO 366 360 ?   ?   ?   A . n 
A 1 367 ARG 367 361 ?   ?   ?   A . n 
A 1 368 LEU 368 362 ?   ?   ?   A . n 
A 1 369 ALA 369 363 ?   ?   ?   A . n 
A 1 370 ALA 370 364 ?   ?   ?   A . n 
A 1 371 VAL 371 365 ?   ?   ?   A . n 
A 1 372 ALA 372 366 ?   ?   ?   A . n 
A 1 373 ARG 373 367 ?   ?   ?   A . n 
B 1 1   GLY 1   -5  ?   ?   ?   B . n 
B 1 2   ILE 2   -4  ?   ?   ?   B . n 
B 1 3   ASP 3   -3  -3  ASP ASP B . n 
B 1 4   PRO 4   -2  -2  PRO PRO B . n 
B 1 5   PHE 5   -1  -1  PHE PHE B . n 
B 1 6   THR 6   0   0   THR THR B . n 
B 1 7   MET 7   1   1   MET MET B . n 
B 1 8   THR 8   2   2   THR THR B . n 
B 1 9   PRO 9   3   3   PRO PRO B . n 
B 1 10  SER 10  4   4   SER SER B . n 
B 1 11  GLU 11  5   5   GLU GLU B . n 
B 1 12  ASP 12  6   6   ASP ASP B . n 
B 1 13  PHE 13  7   7   PHE PHE B . n 
B 1 14  VAL 14  8   8   VAL VAL B . n 
B 1 15  VAL 15  9   9   VAL VAL B . n 
B 1 16  THR 16  10  10  THR THR B . n 
B 1 17  ASP 17  11  11  ASP ASP B . n 
B 1 18  ARG 18  12  12  ARG ARG B . n 
B 1 19  GLY 19  13  13  GLY GLY B . n 
B 1 20  GLY 20  14  14  GLY GLY B . n 
B 1 21  ILE 21  15  15  ILE ILE B . n 
B 1 22  VAL 22  16  16  VAL VAL B . n 
B 1 23  GLU 23  17  17  GLU GLU B . n 
B 1 24  ASN 24  18  18  ASN ASN B . n 
B 1 25  SER 25  19  19  SER SER B . n 
B 1 26  HIS 26  20  20  HIS HIS B . n 
B 1 27  ARG 27  21  21  ARG ARG B . n 
B 1 28  VAL 28  22  22  VAL VAL B . n 
B 1 29  HIS 29  23  23  HIS HIS B . n 
B 1 30  ALA 30  24  24  ALA ALA B . n 
B 1 31  ALA 31  25  25  ALA ALA B . n 
B 1 32  VAL 32  26  26  VAL VAL B . n 
B 1 33  VAL 33  27  27  VAL VAL B . n 
B 1 34  ASP 34  28  28  ASP ASP B . n 
B 1 35  ALA 35  29  29  ALA ALA B . n 
B 1 36  LYS 36  30  30  LYS LYS B . n 
B 1 37  GLY 37  31  31  GLY GLY B . n 
B 1 38  ARG 38  32  32  ARG ARG B . n 
B 1 39  LEU 39  33  33  LEU LEU B . n 
B 1 40  LEU 40  34  34  LEU LEU B . n 
B 1 41  TYR 41  35  35  TYR TYR B . n 
B 1 42  ALA 42  36  36  ALA ALA B . n 
B 1 43  LEU 43  37  37  LEU LEU B . n 
B 1 44  GLY 44  38  38  GLY GLY B . n 
B 1 45  ASN 45  39  39  ASN ASN B . n 
B 1 46  PRO 46  40  40  PRO PRO B . n 
B 1 47  THR 47  41  41  THR THR B . n 
B 1 48  ARG 48  42  42  ARG ARG B . n 
B 1 49  MET 49  43  43  MET MET B . n 
B 1 50  THR 50  44  44  THR THR B . n 
B 1 51  LEU 51  45  45  LEU LEU B . n 
B 1 52  ALA 52  46  46  ALA ALA B . n 
B 1 53  ARG 53  47  47  ARG ARG B . n 
B 1 54  SER 54  48  48  SER SER B . n 
B 1 55  ALA 55  49  49  ALA ALA B . n 
B 1 56  ALA 56  50  50  ALA ALA B . n 
B 1 57  LYS 57  51  51  LYS LYS B . n 
B 1 58  PRO 58  52  52  PRO PRO B . n 
B 1 59  ALA 59  53  53  ALA ALA B . n 
B 1 60  GLN 60  54  54  GLN GLN B . n 
B 1 61  ALA 61  55  55  ALA ALA B . n 
B 1 62  LEU 62  56  56  LEU LEU B . n 
B 1 63  ALA 63  57  57  ALA ALA B . n 
B 1 64  ILE 64  58  58  ILE ILE B . n 
B 1 65  LEU 65  59  59  LEU LEU B . n 
B 1 66  GLU 66  60  60  GLU GLU B . n 
B 1 67  THR 67  61  61  THR THR B . n 
B 1 68  GLU 68  62  62  GLU GLU B . n 
B 1 69  GLY 69  63  63  GLY GLY B . n 
B 1 70  VAL 70  64  64  VAL VAL B . n 
B 1 71  ALA 71  65  65  ALA ALA B . n 
B 1 72  GLY 72  66  66  GLY GLY B . n 
B 1 73  TYR 73  67  67  TYR TYR B . n 
B 1 74  GLY 74  68  68  GLY GLY B . n 
B 1 75  PHE 75  69  69  PHE PHE B . n 
B 1 76  ASP 76  70  70  ASP ASP B . n 
B 1 77  ASP 77  71  71  ASP ASP B . n 
B 1 78  ALA 78  72  72  ALA ALA B . n 
B 1 79  ASP 79  73  73  ASP ASP B . n 
B 1 80  ILE 80  74  74  ILE ILE B . n 
B 1 81  ALA 81  75  75  ALA ALA B . n 
B 1 82  LEU 82  76  76  LEU LEU B . n 
B 1 83  MET 83  77  77  MET MET B . n 
B 1 84  CYS 84  78  78  CYS CYS B . n 
B 1 85  ALA 85  79  79  ALA ALA B . n 
B 1 86  SER 86  80  80  SER SER B . n 
B 1 87  HIS 87  81  81  HIS HIS B . n 
B 1 88  SER 88  82  82  SER SER B . n 
B 1 89  SER 89  83  83  SER SER B . n 
B 1 90  GLU 90  84  84  GLU GLU B . n 
B 1 91  ASP 91  85  85  ASP ASP B . n 
B 1 92  ARG 92  86  86  ARG ARG B . n 
B 1 93  HIS 93  87  87  HIS HIS B . n 
B 1 94  ILE 94  88  88  ILE ILE B . n 
B 1 95  ALA 95  89  89  ALA ALA B . n 
B 1 96  ARG 96  90  90  ARG ARG B . n 
B 1 97  THR 97  91  91  THR THR B . n 
B 1 98  ARG 98  92  92  ARG ARG B . n 
B 1 99  ALA 99  93  93  ALA ALA B . n 
B 1 100 MET 100 94  94  MET MET B . n 
B 1 101 LEU 101 95  95  LEU LEU B . n 
B 1 102 SER 102 96  96  SER SER B . n 
B 1 103 LYS 103 97  97  LYS LYS B . n 
B 1 104 ILE 104 98  98  ILE ILE B . n 
B 1 105 LYS 105 99  99  LYS LYS B . n 
B 1 106 ALA 106 100 100 ALA ALA B . n 
B 1 107 GLU 107 101 101 GLU GLU B . n 
B 1 108 GLU 108 102 102 GLU GLU B . n 
B 1 109 ALA 109 103 103 ALA ALA B . n 
B 1 110 ASP 110 104 104 ASP ASP B . n 
B 1 111 LEU 111 105 105 LEU LEU B . n 
B 1 112 ARG 112 106 106 ARG ARG B . n 
B 1 113 CYS 113 107 107 CYS CYS B . n 
B 1 114 GLY 114 108 108 GLY GLY B . n 
B 1 115 GLY 115 109 109 GLY GLY B . n 
B 1 116 HIS 116 110 110 HIS HIS B . n 
B 1 117 PRO 117 111 111 PRO PRO B . n 
B 1 118 SER 118 112 112 SER SER B . n 
B 1 119 LEU 119 113 113 LEU LEU B . n 
B 1 120 SER 120 114 114 SER SER B . n 
B 1 121 GLU 121 115 115 GLU GLU B . n 
B 1 122 MET 122 116 116 MET MET B . n 
B 1 123 VAL 123 117 117 VAL VAL B . n 
B 1 124 ASN 124 118 118 ASN ASN B . n 
B 1 125 ARG 125 119 119 ARG ARG B . n 
B 1 126 SER 126 120 120 SER SER B . n 
B 1 127 TRP 127 121 121 TRP TRP B . n 
B 1 128 ILE 128 122 122 ILE ILE B . n 
B 1 129 LYS 129 123 123 LYS LYS B . n 
B 1 130 GLN 130 124 124 GLN GLN B . n 
B 1 131 ASP 131 125 125 ASP ASP B . n 
B 1 132 PHE 132 126 126 PHE PHE B . n 
B 1 133 ILE 133 127 127 ILE ILE B . n 
B 1 134 PRO 134 128 128 PRO PRO B . n 
B 1 135 THR 135 129 129 THR THR B . n 
B 1 136 ALA 136 130 130 ALA ALA B . n 
B 1 137 VAL 137 131 131 VAL VAL B . n 
B 1 138 CYS 138 132 132 CYS CYS B . n 
B 1 139 SER 139 133 133 SER SER B . n 
B 1 140 ASN 140 134 134 ASN ASN B . n 
B 1 141 CYS 141 135 135 CYS CYS B . n 
B 1 142 SER 142 136 136 SER SER B . n 
B 1 143 GLY 143 137 137 GLY GLY B . n 
B 1 144 HIS 144 138 138 HIS HIS B . n 
B 1 145 HIS 145 139 139 HIS HIS B . n 
B 1 146 VAL 146 140 140 VAL VAL B . n 
B 1 147 GLY 147 141 141 GLY GLY B . n 
B 1 148 MET 148 142 142 MET MET B . n 
B 1 149 LEU 149 143 143 LEU LEU B . n 
B 1 150 ALA 150 144 144 ALA ALA B . n 
B 1 151 GLY 151 145 145 GLY GLY B . n 
B 1 152 ALA 152 146 146 ALA ALA B . n 
B 1 153 ARG 153 147 147 ARG ARG B . n 
B 1 154 ALA 154 148 148 ALA ALA B . n 
B 1 155 ILE 155 149 149 ILE ILE B . n 
B 1 156 GLY 156 150 150 GLY GLY B . n 
B 1 157 ALA 157 151 151 ALA ALA B . n 
B 1 158 GLY 158 152 152 GLY GLY B . n 
B 1 159 THR 159 153 153 THR THR B . n 
B 1 160 ASP 160 154 154 ASP ASP B . n 
B 1 161 GLY 161 155 155 GLY GLY B . n 
B 1 162 TYR 162 156 156 TYR TYR B . n 
B 1 163 HIS 163 157 157 HIS HIS B . n 
B 1 164 LEU 164 158 158 LEU LEU B . n 
B 1 165 PRO 165 159 159 PRO PRO B . n 
B 1 166 ASP 166 160 160 ASP ASP B . n 
B 1 167 HIS 167 161 161 HIS HIS B . n 
B 1 168 PRO 168 162 162 PRO PRO B . n 
B 1 169 MET 169 163 163 MET MET B . n 
B 1 170 GLN 170 164 164 GLN GLN B . n 
B 1 171 GLY 171 165 165 GLY GLY B . n 
B 1 172 ARG 172 166 166 ARG ARG B . n 
B 1 173 VAL 173 167 167 VAL VAL B . n 
B 1 174 LYS 174 168 168 LYS LYS B . n 
B 1 175 ARG 175 169 169 ARG ARG B . n 
B 1 176 THR 176 170 170 THR THR B . n 
B 1 177 VAL 177 171 171 VAL VAL B . n 
B 1 178 ALA 178 172 172 ALA ALA B . n 
B 1 179 GLU 179 173 173 GLU GLU B . n 
B 1 180 LEU 180 174 174 LEU LEU B . n 
B 1 181 CYS 181 175 175 CYS CYS B . n 
B 1 182 ASP 182 176 176 ASP ASP B . n 
B 1 183 LEU 183 177 177 LEU LEU B . n 
B 1 184 ASP 184 178 178 ASP ASP B . n 
B 1 185 ALA 185 179 179 ALA ALA B . n 
B 1 186 GLY 186 180 180 GLY GLY B . n 
B 1 187 ASP 187 181 181 ASP ASP B . n 
B 1 188 VAL 188 182 182 VAL VAL B . n 
B 1 189 GLU 189 183 183 GLU GLU B . n 
B 1 190 TRP 190 184 184 TRP TRP B . n 
B 1 191 GLY 191 185 185 GLY GLY B . n 
B 1 192 THR 192 186 186 THR THR B . n 
B 1 193 ASP 193 187 187 ASP ASP B . n 
B 1 194 GLY 194 188 188 GLY GLY B . n 
B 1 195 CYS 195 189 189 CYS CYS B . n 
B 1 196 ASN 196 190 190 ASN ASN B . n 
B 1 197 LEU 197 191 191 LEU LEU B . n 
B 1 198 PRO 198 192 192 PRO PRO B . n 
B 1 199 THR 199 193 193 THR THR B . n 
B 1 200 PRO 200 194 194 PRO PRO B . n 
B 1 201 ALA 201 195 195 ALA ALA B . n 
B 1 202 PHE 202 196 196 PHE PHE B . n 
B 1 203 PRO 203 197 197 PRO PRO B . n 
B 1 204 LEU 204 198 198 LEU LEU B . n 
B 1 205 ASP 205 199 199 ASP ASP B . n 
B 1 206 ARG 206 200 200 ARG ARG B . n 
B 1 207 LEU 207 201 201 LEU LEU B . n 
B 1 208 GLY 208 202 202 GLY GLY B . n 
B 1 209 ARG 209 203 203 ARG ARG B . n 
B 1 210 ILE 210 204 204 ILE ILE B . n 
B 1 211 TYR 211 205 205 TYR TYR B . n 
B 1 212 ALA 212 206 206 ALA ALA B . n 
B 1 213 LYS 213 207 207 LYS LYS B . n 
B 1 214 LEU 214 208 208 LEU LEU B . n 
B 1 215 ALA 215 209 209 ALA ALA B . n 
B 1 216 SER 216 210 210 SER SER B . n 
B 1 217 ALA 217 211 211 ALA ALA B . n 
B 1 218 ALA 218 212 212 ALA ALA B . n 
B 1 219 ASP 219 213 213 ASP ASP B . n 
B 1 220 GLY 220 214 214 GLY GLY B . n 
B 1 221 SER 221 215 215 SER SER B . n 
B 1 222 ASP 222 216 216 ASP ASP B . n 
B 1 223 ALA 223 217 217 ALA ALA B . n 
B 1 224 GLY 224 218 218 GLY GLY B . n 
B 1 225 GLU 225 219 219 GLU GLU B . n 
B 1 226 GLY 226 220 220 GLY GLY B . n 
B 1 227 GLN 227 221 221 GLN GLN B . n 
B 1 228 SER 228 222 222 SER SER B . n 
B 1 229 THR 229 223 223 THR THR B . n 
B 1 230 ARG 230 224 224 ARG ARG B . n 
B 1 231 CYS 231 225 225 CYS CYS B . n 
B 1 232 ALA 232 226 226 ALA ALA B . n 
B 1 233 ALA 233 227 227 ALA ALA B . n 
B 1 234 LEU 234 228 228 LEU LEU B . n 
B 1 235 ALA 235 229 229 ALA ALA B . n 
B 1 236 HIS 236 230 230 HIS HIS B . n 
B 1 237 ILE 237 231 231 ILE ILE B . n 
B 1 238 PHE 238 232 232 PHE PHE B . n 
B 1 239 ARG 239 233 233 ARG ARG B . n 
B 1 240 ALA 240 234 234 ALA ALA B . n 
B 1 241 MET 241 235 235 MET MET B . n 
B 1 242 ALA 242 236 236 ALA ALA B . n 
B 1 243 ARG 243 237 237 ARG ARG B . n 
B 1 244 HIS 244 238 238 HIS HIS B . n 
B 1 245 PRO 245 239 239 PRO PRO B . n 
B 1 246 GLU 246 240 240 GLU GLU B . n 
B 1 247 MET 247 241 241 MET MET B . n 
B 1 248 VAL 248 242 242 VAL VAL B . n 
B 1 249 ALA 249 243 243 ALA ALA B . n 
B 1 250 GLY 250 244 244 GLY GLY B . n 
B 1 251 GLU 251 245 245 GLU GLU B . n 
B 1 252 GLY 252 246 246 GLY GLY B . n 
B 1 253 ARG 253 247 247 ARG ARG B . n 
B 1 254 TYR 254 248 248 TYR TYR B . n 
B 1 255 CYS 255 249 249 CYS CYS B . n 
B 1 256 THR 256 250 250 THR THR B . n 
B 1 257 MET 257 251 251 MET MET B . n 
B 1 258 LEU 258 252 252 LEU LEU B . n 
B 1 259 MET 259 253 253 MET MET B . n 
B 1 260 ARG 260 254 254 ARG ARG B . n 
B 1 261 ALA 261 255 255 ALA ALA B . n 
B 1 262 PHE 262 256 256 PHE PHE B . n 
B 1 263 ASP 263 257 257 ASP ASP B . n 
B 1 264 GLY 264 258 258 GLY GLY B . n 
B 1 265 ALA 265 259 259 ALA ALA B . n 
B 1 266 LEU 266 260 260 LEU LEU B . n 
B 1 267 VAL 267 261 261 VAL VAL B . n 
B 1 268 GLY 268 262 262 GLY GLY B . n 
B 1 269 LYS 269 263 263 LYS LYS B . n 
B 1 270 LEU 270 264 264 LEU LEU B . n 
B 1 271 GLY 271 265 265 GLY GLY B . n 
B 1 272 ALA 272 266 266 ALA ALA B . n 
B 1 273 ASP 273 267 267 ASP ASP B . n 
B 1 274 ALA 274 268 268 ALA ALA B . n 
B 1 275 SER 275 269 269 SER SER B . n 
B 1 276 TYR 276 270 270 TYR TYR B . n 
B 1 277 ALA 277 271 271 ALA ALA B . n 
B 1 278 ILE 278 272 272 ILE ILE B . n 
B 1 279 GLY 279 273 273 GLY GLY B . n 
B 1 280 VAL 280 274 274 VAL VAL B . n 
B 1 281 ARG 281 275 275 ARG ARG B . n 
B 1 282 ALA 282 276 276 ALA ALA B . n 
B 1 283 SER 283 277 277 SER SER B . n 
B 1 284 ASP 284 278 278 ASP ASP B . n 
B 1 285 ALA 285 279 279 ALA ALA B . n 
B 1 286 THR 286 280 280 THR THR B . n 
B 1 287 ARG 287 281 281 ARG ARG B . n 
B 1 288 GLN 288 282 282 GLN GLN B . n 
B 1 289 LEU 289 283 283 LEU LEU B . n 
B 1 290 GLY 290 284 284 GLY GLY B . n 
B 1 291 THR 291 285 285 THR THR B . n 
B 1 292 ASP 292 286 286 ASP ASP B . n 
B 1 293 GLY 293 287 287 GLY GLY B . n 
B 1 294 ALA 294 288 288 ALA ALA B . n 
B 1 295 LEU 295 289 289 LEU LEU B . n 
B 1 296 GLY 296 290 290 GLY GLY B . n 
B 1 297 ILE 297 291 291 ILE ILE B . n 
B 1 298 SER 298 292 292 SER SER B . n 
B 1 299 VAL 299 293 293 VAL VAL B . n 
B 1 300 LYS 300 294 294 LYS LYS B . n 
B 1 301 ILE 301 295 295 ILE ILE B . n 
B 1 302 GLU 302 296 296 GLU GLU B . n 
B 1 303 ASP 303 297 297 ASP ASP B . n 
B 1 304 GLY 304 298 298 GLY GLY B . n 
B 1 305 ASN 305 299 299 ASN ASN B . n 
B 1 306 LEU 306 300 300 LEU LEU B . n 
B 1 307 GLU 307 301 301 GLU GLU B . n 
B 1 308 MET 308 302 302 MET MET B . n 
B 1 309 LEU 309 303 303 LEU LEU B . n 
B 1 310 TYR 310 304 304 TYR TYR B . n 
B 1 311 ALA 311 305 305 ALA ALA B . n 
B 1 312 VAL 312 306 306 VAL VAL B . n 
B 1 313 VAL 313 307 307 VAL VAL B . n 
B 1 314 THR 314 308 308 THR THR B . n 
B 1 315 GLU 315 309 309 GLU GLU B . n 
B 1 316 LEU 316 310 310 LEU LEU B . n 
B 1 317 LEU 317 311 311 LEU LEU B . n 
B 1 318 GLU 318 312 312 GLU GLU B . n 
B 1 319 ARG 319 313 313 ARG ARG B . n 
B 1 320 LEU 320 314 314 LEU LEU B . n 
B 1 321 GLY 321 315 315 GLY GLY B . n 
B 1 322 ILE 322 316 316 ILE ILE B . n 
B 1 323 GLY 323 317 317 GLY GLY B . n 
B 1 324 SER 324 318 318 SER SER B . n 
B 1 325 PRO 325 319 319 PRO PRO B . n 
B 1 326 ASP 326 320 320 ASP ASP B . n 
B 1 327 VAL 327 321 321 VAL VAL B . n 
B 1 328 ARG 328 322 322 ARG ARG B . n 
B 1 329 SER 329 323 323 SER SER B . n 
B 1 330 GLN 330 324 324 GLN GLN B . n 
B 1 331 LEU 331 325 325 LEU LEU B . n 
B 1 332 ALA 332 326 326 ALA ALA B . n 
B 1 333 SER 333 327 327 SER SER B . n 
B 1 334 PHE 334 328 328 PHE PHE B . n 
B 1 335 HIS 335 329 329 HIS HIS B . n 
B 1 336 HIS 336 330 330 HIS HIS B . n 
B 1 337 PRO 337 331 331 PRO PRO B . n 
B 1 338 GLN 338 332 332 GLN GLN B . n 
B 1 339 ARG 339 333 333 ARG ARG B . n 
B 1 340 VAL 340 334 334 VAL VAL B . n 
B 1 341 ASN 341 335 335 ASN ASN B . n 
B 1 342 THR 342 336 336 THR THR B . n 
B 1 343 MET 343 337 337 MET MET B . n 
B 1 344 GLY 344 338 338 GLY GLY B . n 
B 1 345 VAL 345 339 339 VAL VAL B . n 
B 1 346 THR 346 340 340 THR THR B . n 
B 1 347 THR 347 341 341 THR THR B . n 
B 1 348 GLY 348 342 342 GLY GLY B . n 
B 1 349 GLY 349 343 343 GLY GLY B . n 
B 1 350 VAL 350 344 344 VAL VAL B . n 
B 1 351 SER 351 345 345 SER SER B . n 
B 1 352 PHE 352 346 346 PHE PHE B . n 
B 1 353 PRO 353 347 347 PRO PRO B . n 
B 1 354 PHE 354 348 348 PHE PHE B . n 
B 1 355 LYS 355 349 349 LYS LYS B . n 
B 1 356 LEU 356 350 350 LEU LEU B . n 
B 1 357 ARG 357 351 351 ARG ARG B . n 
B 1 358 GLY 358 352 352 GLY GLY B . n 
B 1 359 SER 359 353 ?   ?   ?   B . n 
B 1 360 LYS 360 354 ?   ?   ?   B . n 
B 1 361 SER 361 355 ?   ?   ?   B . n 
B 1 362 ASN 362 356 ?   ?   ?   B . n 
B 1 363 VAL 363 357 ?   ?   ?   B . n 
B 1 364 ASP 364 358 358 ASP ASP B . n 
B 1 365 ASP 365 359 359 ASP ASP B . n 
B 1 366 PRO 366 360 360 PRO PRO B . n 
B 1 367 ARG 367 361 361 ARG ARG B . n 
B 1 368 LEU 368 362 362 LEU LEU B . n 
B 1 369 ALA 369 363 363 ALA ALA B . n 
B 1 370 ALA 370 364 364 ALA ALA B . n 
B 1 371 VAL 371 365 365 VAL VAL B . n 
B 1 372 ALA 372 366 366 ALA ALA B . n 
B 1 373 ARG 373 367 367 ARG ARG B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ASN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ASN 
_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 EDO 1   501 501 EDO EDO A . 
D 2 EDO 1   502 502 EDO EDO A . 
E 2 EDO 1   503 503 EDO EDO A . 
F 2 EDO 1   504 508 EDO EDO A . 
G 3 ASN 1   505 509 ASN ASN A . 
H 2 EDO 1   506 604 EDO EDO A . 
I 2 EDO 1   507 605 EDO EDO A . 
J 4 CL  1   508 2   CL  CL  A . 
K 5 CD  1   509 1   CD  CD  A . 
L 2 EDO 1   401 401 EDO EDO B . 
M 2 EDO 1   402 501 EDO EDO B . 
N 2 EDO 1   403 503 EDO EDO B . 
O 2 EDO 1   404 506 EDO EDO B . 
P 2 EDO 1   405 509 EDO EDO B . 
Q 2 EDO 1   406 510 EDO EDO B . 
R 2 EDO 1   407 511 EDO EDO B . 
S 3 ASN 1   408 512 ASN ASN B . 
T 2 EDO 1   409 601 EDO EDO B . 
U 4 CL  1   410 3   CL  CL  B . 
V 5 CD  1   411 2   CD  CD  B . 
W 6 HOH 1   601 59  HOH HOH A . 
W 6 HOH 2   602 55  HOH HOH A . 
W 6 HOH 3   603 251 HOH HOH A . 
W 6 HOH 4   604 437 HOH HOH A . 
W 6 HOH 5   605 229 HOH HOH A . 
W 6 HOH 6   606 106 HOH HOH A . 
W 6 HOH 7   607 99  HOH HOH A . 
W 6 HOH 8   608 94  HOH HOH A . 
W 6 HOH 9   609 260 HOH HOH A . 
W 6 HOH 10  610 149 HOH HOH A . 
W 6 HOH 11  611 139 HOH HOH A . 
W 6 HOH 12  612 204 HOH HOH A . 
W 6 HOH 13  613 202 HOH HOH A . 
W 6 HOH 14  614 242 HOH HOH A . 
W 6 HOH 15  615 185 HOH HOH A . 
W 6 HOH 16  616 93  HOH HOH A . 
W 6 HOH 17  617 200 HOH HOH A . 
W 6 HOH 18  618 222 HOH HOH A . 
W 6 HOH 19  619 186 HOH HOH A . 
W 6 HOH 20  620 247 HOH HOH A . 
W 6 HOH 21  621 85  HOH HOH A . 
W 6 HOH 22  622 215 HOH HOH A . 
W 6 HOH 23  623 210 HOH HOH A . 
W 6 HOH 24  624 206 HOH HOH A . 
W 6 HOH 25  625 41  HOH HOH A . 
W 6 HOH 26  626 273 HOH HOH A . 
W 6 HOH 27  627 190 HOH HOH A . 
W 6 HOH 28  628 175 HOH HOH A . 
W 6 HOH 29  629 122 HOH HOH A . 
W 6 HOH 30  630 120 HOH HOH A . 
W 6 HOH 31  631 249 HOH HOH A . 
W 6 HOH 32  632 32  HOH HOH A . 
W 6 HOH 33  633 45  HOH HOH A . 
W 6 HOH 34  634 216 HOH HOH A . 
W 6 HOH 35  635 137 HOH HOH A . 
W 6 HOH 36  636 207 HOH HOH A . 
W 6 HOH 37  637 161 HOH HOH A . 
W 6 HOH 38  638 35  HOH HOH A . 
W 6 HOH 39  639 189 HOH HOH A . 
W 6 HOH 40  640 362 HOH HOH A . 
W 6 HOH 41  641 110 HOH HOH A . 
W 6 HOH 42  642 148 HOH HOH A . 
W 6 HOH 43  643 121 HOH HOH A . 
W 6 HOH 44  644 69  HOH HOH A . 
W 6 HOH 45  645 234 HOH HOH A . 
W 6 HOH 46  646 26  HOH HOH A . 
W 6 HOH 47  647 399 HOH HOH A . 
W 6 HOH 48  648 48  HOH HOH A . 
W 6 HOH 49  649 52  HOH HOH A . 
W 6 HOH 50  650 102 HOH HOH A . 
W 6 HOH 51  651 4   HOH HOH A . 
W 6 HOH 52  652 461 HOH HOH A . 
W 6 HOH 53  653 170 HOH HOH A . 
W 6 HOH 54  654 160 HOH HOH A . 
W 6 HOH 55  655 289 HOH HOH A . 
W 6 HOH 56  656 163 HOH HOH A . 
W 6 HOH 57  657 211 HOH HOH A . 
W 6 HOH 58  658 20  HOH HOH A . 
W 6 HOH 59  659 56  HOH HOH A . 
W 6 HOH 60  660 31  HOH HOH A . 
W 6 HOH 61  661 435 HOH HOH A . 
W 6 HOH 62  662 263 HOH HOH A . 
W 6 HOH 63  663 42  HOH HOH A . 
W 6 HOH 64  664 22  HOH HOH A . 
W 6 HOH 65  665 9   HOH HOH A . 
W 6 HOH 66  666 117 HOH HOH A . 
W 6 HOH 67  667 82  HOH HOH A . 
W 6 HOH 68  668 27  HOH HOH A . 
W 6 HOH 69  669 468 HOH HOH A . 
W 6 HOH 70  670 7   HOH HOH A . 
W 6 HOH 71  671 264 HOH HOH A . 
W 6 HOH 72  672 218 HOH HOH A . 
W 6 HOH 73  673 254 HOH HOH A . 
W 6 HOH 74  674 78  HOH HOH A . 
W 6 HOH 75  675 221 HOH HOH A . 
W 6 HOH 76  676 6   HOH HOH A . 
W 6 HOH 77  677 159 HOH HOH A . 
W 6 HOH 78  678 165 HOH HOH A . 
W 6 HOH 79  679 14  HOH HOH A . 
W 6 HOH 80  680 231 HOH HOH A . 
W 6 HOH 81  681 97  HOH HOH A . 
W 6 HOH 82  682 171 HOH HOH A . 
W 6 HOH 83  683 144 HOH HOH A . 
W 6 HOH 84  684 104 HOH HOH A . 
W 6 HOH 85  685 155 HOH HOH A . 
W 6 HOH 86  686 154 HOH HOH A . 
W 6 HOH 87  687 238 HOH HOH A . 
W 6 HOH 88  688 119 HOH HOH A . 
W 6 HOH 89  689 105 HOH HOH A . 
W 6 HOH 90  690 141 HOH HOH A . 
W 6 HOH 91  691 434 HOH HOH A . 
W 6 HOH 92  692 262 HOH HOH A . 
W 6 HOH 93  693 103 HOH HOH A . 
W 6 HOH 94  694 118 HOH HOH A . 
W 6 HOH 95  695 481 HOH HOH A . 
W 6 HOH 96  696 153 HOH HOH A . 
W 6 HOH 97  697 241 HOH HOH A . 
W 6 HOH 98  698 407 HOH HOH A . 
W 6 HOH 99  699 108 HOH HOH A . 
W 6 HOH 100 700 237 HOH HOH A . 
W 6 HOH 101 701 219 HOH HOH A . 
W 6 HOH 102 702 40  HOH HOH A . 
W 6 HOH 103 703 265 HOH HOH A . 
W 6 HOH 104 704 232 HOH HOH A . 
W 6 HOH 105 705 436 HOH HOH A . 
W 6 HOH 106 706 15  HOH HOH A . 
W 6 HOH 107 707 58  HOH HOH A . 
W 6 HOH 108 708 192 HOH HOH A . 
W 6 HOH 109 709 81  HOH HOH A . 
W 6 HOH 110 710 205 HOH HOH A . 
W 6 HOH 111 711 76  HOH HOH A . 
W 6 HOH 112 712 147 HOH HOH A . 
W 6 HOH 113 713 72  HOH HOH A . 
W 6 HOH 114 714 74  HOH HOH A . 
W 6 HOH 115 715 19  HOH HOH A . 
W 6 HOH 116 716 240 HOH HOH A . 
W 6 HOH 117 717 166 HOH HOH A . 
W 6 HOH 118 718 201 HOH HOH A . 
W 6 HOH 119 719 12  HOH HOH A . 
W 6 HOH 120 720 162 HOH HOH A . 
W 6 HOH 121 721 164 HOH HOH A . 
W 6 HOH 122 722 98  HOH HOH A . 
W 6 HOH 123 723 50  HOH HOH A . 
W 6 HOH 124 724 272 HOH HOH A . 
W 6 HOH 125 725 38  HOH HOH A . 
W 6 HOH 126 726 179 HOH HOH A . 
W 6 HOH 127 727 469 HOH HOH A . 
W 6 HOH 128 728 217 HOH HOH A . 
W 6 HOH 129 729 291 HOH HOH A . 
W 6 HOH 130 730 91  HOH HOH A . 
W 6 HOH 131 731 188 HOH HOH A . 
W 6 HOH 132 732 255 HOH HOH A . 
W 6 HOH 133 733 177 HOH HOH A . 
W 6 HOH 134 734 151 HOH HOH A . 
W 6 HOH 135 735 256 HOH HOH A . 
W 6 HOH 136 736 101 HOH HOH A . 
W 6 HOH 137 737 112 HOH HOH A . 
W 6 HOH 138 738 445 HOH HOH A . 
W 6 HOH 139 739 433 HOH HOH A . 
W 6 HOH 140 740 115 HOH HOH A . 
W 6 HOH 141 741 408 HOH HOH A . 
W 6 HOH 142 742 173 HOH HOH A . 
W 6 HOH 143 743 17  HOH HOH A . 
W 6 HOH 144 744 150 HOH HOH A . 
W 6 HOH 145 745 36  HOH HOH A . 
W 6 HOH 146 746 100 HOH HOH A . 
W 6 HOH 147 747 183 HOH HOH A . 
W 6 HOH 148 748 466 HOH HOH A . 
W 6 HOH 149 749 61  HOH HOH A . 
W 6 HOH 150 750 193 HOH HOH A . 
W 6 HOH 151 751 145 HOH HOH A . 
W 6 HOH 152 752 39  HOH HOH A . 
W 6 HOH 153 753 411 HOH HOH A . 
W 6 HOH 154 754 473 HOH HOH A . 
W 6 HOH 155 755 208 HOH HOH A . 
W 6 HOH 156 756 479 HOH HOH A . 
W 6 HOH 157 757 158 HOH HOH A . 
W 6 HOH 158 758 178 HOH HOH A . 
W 6 HOH 159 759 246 HOH HOH A . 
W 6 HOH 160 760 194 HOH HOH A . 
W 6 HOH 161 761 245 HOH HOH A . 
W 6 HOH 162 762 412 HOH HOH A . 
W 6 HOH 163 763 244 HOH HOH A . 
W 6 HOH 164 764 182 HOH HOH A . 
W 6 HOH 165 765 191 HOH HOH A . 
W 6 HOH 166 766 454 HOH HOH A . 
W 6 HOH 167 767 88  HOH HOH A . 
W 6 HOH 168 768 248 HOH HOH A . 
W 6 HOH 169 769 157 HOH HOH A . 
W 6 HOH 170 770 400 HOH HOH A . 
W 6 HOH 171 771 388 HOH HOH A . 
W 6 HOH 172 772 180 HOH HOH A . 
W 6 HOH 173 773 156 HOH HOH A . 
W 6 HOH 174 774 462 HOH HOH A . 
W 6 HOH 175 775 480 HOH HOH A . 
W 6 HOH 176 776 214 HOH HOH A . 
W 6 HOH 177 777 239 HOH HOH A . 
W 6 HOH 178 778 235 HOH HOH A . 
W 6 HOH 179 779 460 HOH HOH A . 
W 6 HOH 180 780 401 HOH HOH A . 
W 6 HOH 181 781 243 HOH HOH A . 
W 6 HOH 182 782 459 HOH HOH A . 
W 6 HOH 183 783 444 HOH HOH A . 
W 6 HOH 184 784 181 HOH HOH A . 
W 6 HOH 185 785 133 HOH HOH A . 
W 6 HOH 186 786 236 HOH HOH A . 
W 6 HOH 187 787 402 HOH HOH A . 
W 6 HOH 188 788 409 HOH HOH A . 
W 6 HOH 189 789 494 HOH HOH A . 
W 6 HOH 190 790 252 HOH HOH A . 
W 6 HOH 191 791 172 HOH HOH A . 
W 6 HOH 192 792 472 HOH HOH A . 
W 6 HOH 193 793 168 HOH HOH A . 
W 6 HOH 194 794 253 HOH HOH A . 
W 6 HOH 195 795 266 HOH HOH A . 
W 6 HOH 196 796 257 HOH HOH A . 
W 6 HOH 197 797 167 HOH HOH A . 
W 6 HOH 198 798 87  HOH HOH A . 
W 6 HOH 199 799 209 HOH HOH A . 
W 6 HOH 200 800 213 HOH HOH A . 
W 6 HOH 201 801 427 HOH HOH A . 
W 6 HOH 202 802 152 HOH HOH A . 
W 6 HOH 203 803 432 HOH HOH A . 
W 6 HOH 204 804 439 HOH HOH A . 
W 6 HOH 205 805 140 HOH HOH A . 
W 6 HOH 206 806 271 HOH HOH A . 
W 6 HOH 207 807 392 HOH HOH A . 
W 6 HOH 208 808 109 HOH HOH A . 
W 6 HOH 209 809 261 HOH HOH A . 
W 6 HOH 210 810 138 HOH HOH A . 
W 6 HOH 211 811 83  HOH HOH A . 
W 6 HOH 212 812 146 HOH HOH A . 
X 6 HOH 1   501 367 HOH HOH B . 
X 6 HOH 2   502 326 HOH HOH B . 
X 6 HOH 3   503 485 HOH HOH B . 
X 6 HOH 4   504 381 HOH HOH B . 
X 6 HOH 5   505 394 HOH HOH B . 
X 6 HOH 6   506 331 HOH HOH B . 
X 6 HOH 7   507 310 HOH HOH B . 
X 6 HOH 8   508 62  HOH HOH B . 
X 6 HOH 9   509 492 HOH HOH B . 
X 6 HOH 10  510 57  HOH HOH B . 
X 6 HOH 11  511 463 HOH HOH B . 
X 6 HOH 12  512 380 HOH HOH B . 
X 6 HOH 13  513 130 HOH HOH B . 
X 6 HOH 14  514 64  HOH HOH B . 
X 6 HOH 15  515 348 HOH HOH B . 
X 6 HOH 16  516 340 HOH HOH B . 
X 6 HOH 17  517 294 HOH HOH B . 
X 6 HOH 18  518 268 HOH HOH B . 
X 6 HOH 19  519 431 HOH HOH B . 
X 6 HOH 20  520 337 HOH HOH B . 
X 6 HOH 21  521 346 HOH HOH B . 
X 6 HOH 22  522 111 HOH HOH B . 
X 6 HOH 23  523 2   HOH HOH B . 
X 6 HOH 24  524 77  HOH HOH B . 
X 6 HOH 25  525 278 HOH HOH B . 
X 6 HOH 26  526 354 HOH HOH B . 
X 6 HOH 27  527 307 HOH HOH B . 
X 6 HOH 28  528 187 HOH HOH B . 
X 6 HOH 29  529 60  HOH HOH B . 
X 6 HOH 30  530 379 HOH HOH B . 
X 6 HOH 31  531 375 HOH HOH B . 
X 6 HOH 32  532 25  HOH HOH B . 
X 6 HOH 33  533 13  HOH HOH B . 
X 6 HOH 34  534 325 HOH HOH B . 
X 6 HOH 35  535 11  HOH HOH B . 
X 6 HOH 36  536 296 HOH HOH B . 
X 6 HOH 37  537 456 HOH HOH B . 
X 6 HOH 38  538 387 HOH HOH B . 
X 6 HOH 39  539 467 HOH HOH B . 
X 6 HOH 40  540 465 HOH HOH B . 
X 6 HOH 41  541 34  HOH HOH B . 
X 6 HOH 42  542 316 HOH HOH B . 
X 6 HOH 43  543 269 HOH HOH B . 
X 6 HOH 44  544 33  HOH HOH B . 
X 6 HOH 45  545 66  HOH HOH B . 
X 6 HOH 46  546 292 HOH HOH B . 
X 6 HOH 47  547 308 HOH HOH B . 
X 6 HOH 48  548 405 HOH HOH B . 
X 6 HOH 49  549 10  HOH HOH B . 
X 6 HOH 50  550 341 HOH HOH B . 
X 6 HOH 51  551 68  HOH HOH B . 
X 6 HOH 52  552 333 HOH HOH B . 
X 6 HOH 53  553 30  HOH HOH B . 
X 6 HOH 54  554 79  HOH HOH B . 
X 6 HOH 55  555 124 HOH HOH B . 
X 6 HOH 56  556 16  HOH HOH B . 
X 6 HOH 57  557 29  HOH HOH B . 
X 6 HOH 58  558 3   HOH HOH B . 
X 6 HOH 59  559 328 HOH HOH B . 
X 6 HOH 60  560 65  HOH HOH B . 
X 6 HOH 61  561 23  HOH HOH B . 
X 6 HOH 62  562 493 HOH HOH B . 
X 6 HOH 63  563 53  HOH HOH B . 
X 6 HOH 64  564 80  HOH HOH B . 
X 6 HOH 65  565 225 HOH HOH B . 
X 6 HOH 66  566 415 HOH HOH B . 
X 6 HOH 67  567 5   HOH HOH B . 
X 6 HOH 68  568 223 HOH HOH B . 
X 6 HOH 69  569 230 HOH HOH B . 
X 6 HOH 70  570 364 HOH HOH B . 
X 6 HOH 71  571 258 HOH HOH B . 
X 6 HOH 72  572 21  HOH HOH B . 
X 6 HOH 73  573 455 HOH HOH B . 
X 6 HOH 74  574 90  HOH HOH B . 
X 6 HOH 75  575 284 HOH HOH B . 
X 6 HOH 76  576 70  HOH HOH B . 
X 6 HOH 77  577 96  HOH HOH B . 
X 6 HOH 78  578 477 HOH HOH B . 
X 6 HOH 79  579 198 HOH HOH B . 
X 6 HOH 80  580 73  HOH HOH B . 
X 6 HOH 81  581 443 HOH HOH B . 
X 6 HOH 82  582 321 HOH HOH B . 
X 6 HOH 83  583 195 HOH HOH B . 
X 6 HOH 84  584 44  HOH HOH B . 
X 6 HOH 85  585 131 HOH HOH B . 
X 6 HOH 86  586 343 HOH HOH B . 
X 6 HOH 87  587 54  HOH HOH B . 
X 6 HOH 88  588 327 HOH HOH B . 
X 6 HOH 89  589 107 HOH HOH B . 
X 6 HOH 90  590 309 HOH HOH B . 
X 6 HOH 91  591 355 HOH HOH B . 
X 6 HOH 92  592 37  HOH HOH B . 
X 6 HOH 93  593 280 HOH HOH B . 
X 6 HOH 94  594 128 HOH HOH B . 
X 6 HOH 95  595 373 HOH HOH B . 
X 6 HOH 96  596 464 HOH HOH B . 
X 6 HOH 97  597 293 HOH HOH B . 
X 6 HOH 98  598 212 HOH HOH B . 
X 6 HOH 99  599 393 HOH HOH B . 
X 6 HOH 100 600 457 HOH HOH B . 
X 6 HOH 101 601 336 HOH HOH B . 
X 6 HOH 102 602 1   HOH HOH B . 
X 6 HOH 103 603 376 HOH HOH B . 
X 6 HOH 104 604 478 HOH HOH B . 
X 6 HOH 105 605 369 HOH HOH B . 
X 6 HOH 106 606 404 HOH HOH B . 
X 6 HOH 107 607 281 HOH HOH B . 
X 6 HOH 108 608 49  HOH HOH B . 
X 6 HOH 109 609 322 HOH HOH B . 
X 6 HOH 110 610 92  HOH HOH B . 
X 6 HOH 111 611 450 HOH HOH B . 
X 6 HOH 112 612 300 HOH HOH B . 
X 6 HOH 113 613 358 HOH HOH B . 
X 6 HOH 114 614 116 HOH HOH B . 
X 6 HOH 115 615 51  HOH HOH B . 
X 6 HOH 116 616 418 HOH HOH B . 
X 6 HOH 117 617 126 HOH HOH B . 
X 6 HOH 118 618 63  HOH HOH B . 
X 6 HOH 119 619 476 HOH HOH B . 
X 6 HOH 120 620 270 HOH HOH B . 
X 6 HOH 121 621 84  HOH HOH B . 
X 6 HOH 122 622 451 HOH HOH B . 
X 6 HOH 123 623 114 HOH HOH B . 
X 6 HOH 124 624 282 HOH HOH B . 
X 6 HOH 125 625 197 HOH HOH B . 
X 6 HOH 126 626 305 HOH HOH B . 
X 6 HOH 127 627 226 HOH HOH B . 
X 6 HOH 128 628 366 HOH HOH B . 
X 6 HOH 129 629 71  HOH HOH B . 
X 6 HOH 130 630 359 HOH HOH B . 
X 6 HOH 131 631 365 HOH HOH B . 
X 6 HOH 132 632 378 HOH HOH B . 
X 6 HOH 133 633 317 HOH HOH B . 
X 6 HOH 134 634 320 HOH HOH B . 
X 6 HOH 135 635 184 HOH HOH B . 
X 6 HOH 136 636 312 HOH HOH B . 
X 6 HOH 137 637 495 HOH HOH B . 
X 6 HOH 138 638 67  HOH HOH B . 
X 6 HOH 139 639 227 HOH HOH B . 
X 6 HOH 140 640 421 HOH HOH B . 
X 6 HOH 141 641 323 HOH HOH B . 
X 6 HOH 142 642 350 HOH HOH B . 
X 6 HOH 143 643 199 HOH HOH B . 
X 6 HOH 144 644 335 HOH HOH B . 
X 6 HOH 145 645 306 HOH HOH B . 
X 6 HOH 146 646 75  HOH HOH B . 
X 6 HOH 147 647 299 HOH HOH B . 
X 6 HOH 148 648 28  HOH HOH B . 
X 6 HOH 149 649 344 HOH HOH B . 
X 6 HOH 150 650 285 HOH HOH B . 
X 6 HOH 151 651 349 HOH HOH B . 
X 6 HOH 152 652 319 HOH HOH B . 
X 6 HOH 153 653 276 HOH HOH B . 
X 6 HOH 154 654 382 HOH HOH B . 
X 6 HOH 155 655 389 HOH HOH B . 
X 6 HOH 156 656 324 HOH HOH B . 
X 6 HOH 157 657 430 HOH HOH B . 
X 6 HOH 158 658 132 HOH HOH B . 
X 6 HOH 159 659 297 HOH HOH B . 
X 6 HOH 160 660 250 HOH HOH B . 
X 6 HOH 161 661 47  HOH HOH B . 
X 6 HOH 162 662 259 HOH HOH B . 
X 6 HOH 163 663 275 HOH HOH B . 
X 6 HOH 164 664 113 HOH HOH B . 
X 6 HOH 165 665 423 HOH HOH B . 
X 6 HOH 166 666 475 HOH HOH B . 
X 6 HOH 167 667 123 HOH HOH B . 
X 6 HOH 168 668 342 HOH HOH B . 
X 6 HOH 169 669 129 HOH HOH B . 
X 6 HOH 170 670 125 HOH HOH B . 
X 6 HOH 171 671 363 HOH HOH B . 
X 6 HOH 172 672 169 HOH HOH B . 
X 6 HOH 173 673 347 HOH HOH B . 
X 6 HOH 174 674 196 HOH HOH B . 
X 6 HOH 175 675 288 HOH HOH B . 
X 6 HOH 176 676 395 HOH HOH B . 
X 6 HOH 177 677 334 HOH HOH B . 
X 6 HOH 178 678 368 HOH HOH B . 
X 6 HOH 179 679 383 HOH HOH B . 
X 6 HOH 180 680 386 HOH HOH B . 
X 6 HOH 181 681 43  HOH HOH B . 
X 6 HOH 182 682 374 HOH HOH B . 
X 6 HOH 183 683 417 HOH HOH B . 
X 6 HOH 184 684 438 HOH HOH B . 
X 6 HOH 185 685 413 HOH HOH B . 
X 6 HOH 186 686 458 HOH HOH B . 
X 6 HOH 187 687 453 HOH HOH B . 
X 6 HOH 188 688 391 HOH HOH B . 
X 6 HOH 189 689 134 HOH HOH B . 
X 6 HOH 190 690 283 HOH HOH B . 
X 6 HOH 191 691 452 HOH HOH B . 
X 6 HOH 192 692 483 HOH HOH B . 
X 6 HOH 193 693 89  HOH HOH B . 
X 6 HOH 194 694 385 HOH HOH B . 
X 6 HOH 195 695 298 HOH HOH B . 
X 6 HOH 196 696 390 HOH HOH B . 
X 6 HOH 197 697 441 HOH HOH B . 
X 6 HOH 198 698 442 HOH HOH B . 
X 6 HOH 199 699 301 HOH HOH B . 
X 6 HOH 200 700 318 HOH HOH B . 
X 6 HOH 201 701 384 HOH HOH B . 
X 6 HOH 202 702 314 HOH HOH B . 
X 6 HOH 203 703 370 HOH HOH B . 
X 6 HOH 204 704 290 HOH HOH B . 
X 6 HOH 205 705 313 HOH HOH B . 
X 6 HOH 206 706 486 HOH HOH B . 
X 6 HOH 207 707 279 HOH HOH B . 
X 6 HOH 208 708 338 HOH HOH B . 
X 6 HOH 209 709 397 HOH HOH B . 
X 6 HOH 210 710 424 HOH HOH B . 
X 6 HOH 211 711 488 HOH HOH B . 
X 6 HOH 212 712 449 HOH HOH B . 
X 6 HOH 213 713 490 HOH HOH B . 
X 6 HOH 214 714 474 HOH HOH B . 
X 6 HOH 215 715 332 HOH HOH B . 
X 6 HOH 216 716 482 HOH HOH B . 
X 6 HOH 217 717 377 HOH HOH B . 
X 6 HOH 218 718 95  HOH HOH B . 
X 6 HOH 219 719 372 HOH HOH B . 
X 6 HOH 220 720 396 HOH HOH B . 
X 6 HOH 221 721 86  HOH HOH B . 
X 6 HOH 222 722 489 HOH HOH B . 
X 6 HOH 223 723 416 HOH HOH B . 
X 6 HOH 224 724 471 HOH HOH B . 
X 6 HOH 225 725 277 HOH HOH B . 
X 6 HOH 226 726 426 HOH HOH B . 
X 6 HOH 227 727 295 HOH HOH B . 
X 6 HOH 228 728 311 HOH HOH B . 
X 6 HOH 229 729 127 HOH HOH B . 
X 6 HOH 230 730 361 HOH HOH B . 
X 6 HOH 231 731 487 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G67 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.233 
_cell.length_a_esd                 ? 
_cell.length_b                     91.687 
_cell.length_b_esd                 ? 
_cell.length_c                     106.283 
_cell.length_c_esd                 ? 
_cell.volume                       762362.546 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9G67 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G67 
_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             2.50 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.89 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9.0 
_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    '22% PEG 4000, 0.2 M MgCl2, 0.1 M Bicine pH 9.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-08-28 
_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                    ? 
_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   0.7749 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.7749 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          22.75 
_reflns.entry_id                                       9G67 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               69.42 
_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                                     55231 
_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                           94.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.40 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.159 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.151 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.70 
_reflns_shell.d_res_low                                     1.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.50 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2762 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.854 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.582 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.781 
_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                               29.73 
_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                                 9G67 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             63.00 
_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                     55196 
_refine.ls_number_reflns_R_free                  999 
_refine.ls_number_reflns_R_work                  54197 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    64.97 
_refine.ls_percent_reflns_R_free                 1.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1761 
_refine.ls_R_factor_R_free                       0.2158 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1754 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               '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                 27.8062 
_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                            0.1641 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        63.00 
_refine_hist.number_atoms_solvent             443 
_refine_hist.number_atoms_total               5838 
_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        5317 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_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' ? 0.0104  ? 5558 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0797  ? 7507 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0625  ? 836  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0111  ? 999  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.1145 ? 2056 ? 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' 1.70 1.79  . . 18  940   8.00  . . . . 0.3100 . . . . . . . . . . . 0.4785 
'X-RAY DIFFRACTION' 1.79 1.90  . . 79  3177  27.16 . . . . 0.2620 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 1.90 2.05  . . 103 5891  49.90 . . . . 0.2335 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 2.05 2.25  . . 140 8607  72.58 . . . . 0.2125 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 2.25 2.58  . . 206 11317 94.97 . . . . 0.2007 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 2.58 3.25  . . 217 11975 99.88 . . . . 0.1777 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 3.25 63.00 . . 236 12290 99.69 . . . . 0.1462 . . . . . . . . . . . 0.1871 
# 
_struct.entry_id                     9G67 
_struct.title                        'Crystal structure of Rhizobium etli L-asparaginase ReAV K138H mutant in complex with L-Asn' 
_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        9G67 
_struct_keywords.text            'Rhizobium etli; amidohydrolases; L-asparaginases; site-directed mutagenesis, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 5 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 2 ? 
Q N N 2 ? 
R N N 2 ? 
S N N 3 ? 
T N N 2 ? 
U N N 4 ? 
V N N 5 ? 
W N N 6 ? 
X N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q2K0Z2_RHIEC 
_struct_ref.pdbx_db_accession          Q2K0Z2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTPSEDFVVTDRGGIVENSHRVHAAVVDAKGRLLYALGNPTRMTLARSAAKPAQALAILETEGVAGYGFDDADIALMCAS
HSSEDRHIARTRAMLSKIKAEEADLRCGGHPSLSEMVNRSWIKQDFIPTAVCSNCSGKHVGMLAGARAIGAGTDGYHLPD
HPMQGRVKRTVAELCDLDAGDVEWGTDGCNLPTPAFPLDRLGRIYAKLASAADGSDAGEGQSTRCAALAHIFRAMARHPE
MVAGEGRYCTMLMRAFDGALVGKLGADASYAIGVRASDATRQLGTDGALGISVKIEDGNLEMLYAVVTELLERLGIGSPD
VRSQLASFHHPQRVNTMGVTTGGVSFPFKLRGSKSNVDDPRLAAVAR
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G67 A 7 ? 373 ? Q2K0Z2 1 ? 367 ? 1 367 
2 1 9G67 B 7 ? 373 ? Q2K0Z2 1 ? 367 ? 1 367 
# 
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 9G67 GLY A 1   ? UNP Q2K0Z2 ?   ?   'expression tag'      -5  1  
1 9G67 ILE A 2   ? UNP Q2K0Z2 ?   ?   'expression tag'      -4  2  
1 9G67 ASP A 3   ? UNP Q2K0Z2 ?   ?   'expression tag'      -3  3  
1 9G67 PRO A 4   ? UNP Q2K0Z2 ?   ?   'expression tag'      -2  4  
1 9G67 PHE A 5   ? UNP Q2K0Z2 ?   ?   'expression tag'      -1  5  
1 9G67 THR A 6   ? UNP Q2K0Z2 ?   ?   'expression tag'      0   6  
1 9G67 HIS A 144 ? UNP Q2K0Z2 LYS 138 'engineered mutation' 138 7  
2 9G67 GLY B 1   ? UNP Q2K0Z2 ?   ?   'expression tag'      -5  8  
2 9G67 ILE B 2   ? UNP Q2K0Z2 ?   ?   'expression tag'      -4  9  
2 9G67 ASP B 3   ? UNP Q2K0Z2 ?   ?   'expression tag'      -3  10 
2 9G67 PRO B 4   ? UNP Q2K0Z2 ?   ?   'expression tag'      -2  11 
2 9G67 PHE B 5   ? UNP Q2K0Z2 ?   ?   'expression tag'      -1  12 
2 9G67 THR B 6   ? UNP Q2K0Z2 ?   ?   'expression tag'      0   13 
2 9G67 HIS B 144 ? UNP Q2K0Z2 LYS 138 'engineered mutation' 138 14 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6390  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  26210 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ARG A 53  ? ALA A 55  ? ARG A 47  ALA A 49  5 ? 3  
HELX_P HELX_P2  AA2 ALA A 56  ? GLU A 66  ? ALA A 50  GLU A 60  1 ? 11 
HELX_P HELX_P3  AA3 GLY A 69  ? GLY A 74  ? GLY A 63  GLY A 68  5 ? 6  
HELX_P HELX_P4  AA4 ASP A 76  ? CYS A 84  ? ASP A 70  CYS A 78  1 ? 9  
HELX_P HELX_P5  AA5 GLU A 90  ? ILE A 104 ? GLU A 84  ILE A 98  1 ? 15 
HELX_P HELX_P6  AA6 GLU A 107 ? LEU A 111 ? GLU A 101 LEU A 105 5 ? 5  
HELX_P HELX_P7  AA7 SER A 120 ? GLN A 130 ? SER A 114 GLN A 124 1 ? 11 
HELX_P HELX_P8  AA8 THR A 135 ? SER A 139 ? THR A 129 SER A 133 5 ? 5  
HELX_P HELX_P9  AA9 CYS A 141 ? ILE A 155 ? CYS A 135 ILE A 149 1 ? 15 
HELX_P HELX_P10 AB1 HIS A 167 ? ASP A 182 ? HIS A 161 ASP A 176 1 ? 16 
HELX_P HELX_P11 AB2 ASP A 184 ? VAL A 188 ? ASP A 178 VAL A 182 5 ? 5  
HELX_P HELX_P12 AB3 LEU A 204 ? ALA A 223 ? LEU A 198 ALA A 217 1 ? 20 
HELX_P HELX_P13 AB4 SER A 228 ? HIS A 244 ? SER A 222 HIS A 238 1 ? 17 
HELX_P HELX_P14 AB5 HIS A 244 ? ALA A 249 ? HIS A 238 ALA A 243 1 ? 6  
HELX_P HELX_P15 AB6 ARG A 253 ? ASP A 263 ? ARG A 247 ASP A 257 1 ? 11 
HELX_P HELX_P16 AB7 SER A 283 ? LEU A 289 ? SER A 277 LEU A 283 1 ? 7  
HELX_P HELX_P17 AB8 ASN A 305 ? GLY A 321 ? ASN A 299 GLY A 315 1 ? 17 
HELX_P HELX_P18 AB9 SER A 324 ? GLN A 330 ? SER A 318 GLN A 324 1 ? 7  
HELX_P HELX_P19 AC1 LEU A 331 ? HIS A 336 ? LEU A 325 HIS A 330 1 ? 6  
HELX_P HELX_P20 AC2 ASP B 3   ? MET B 7   ? ASP B -3  MET B 1   5 ? 5  
HELX_P HELX_P21 AC3 THR B 8   ? GLU B 11  ? THR B 2   GLU B 5   5 ? 4  
HELX_P HELX_P22 AC4 ARG B 53  ? ALA B 55  ? ARG B 47  ALA B 49  5 ? 3  
HELX_P HELX_P23 AC5 ALA B 56  ? GLU B 66  ? ALA B 50  GLU B 60  1 ? 11 
HELX_P HELX_P24 AC6 GLY B 69  ? GLY B 74  ? GLY B 63  GLY B 68  5 ? 6  
HELX_P HELX_P25 AC7 ASP B 76  ? CYS B 84  ? ASP B 70  CYS B 78  1 ? 9  
HELX_P HELX_P26 AC8 GLU B 90  ? ILE B 104 ? GLU B 84  ILE B 98  1 ? 15 
HELX_P HELX_P27 AC9 GLU B 107 ? LEU B 111 ? GLU B 101 LEU B 105 5 ? 5  
HELX_P HELX_P28 AD1 SER B 120 ? GLN B 130 ? SER B 114 GLN B 124 1 ? 11 
HELX_P HELX_P29 AD2 THR B 135 ? SER B 139 ? THR B 129 SER B 133 5 ? 5  
HELX_P HELX_P30 AD3 CYS B 141 ? ILE B 155 ? CYS B 135 ILE B 149 1 ? 15 
HELX_P HELX_P31 AD4 HIS B 167 ? ASP B 182 ? HIS B 161 ASP B 176 1 ? 16 
HELX_P HELX_P32 AD5 ASP B 184 ? VAL B 188 ? ASP B 178 VAL B 182 5 ? 5  
HELX_P HELX_P33 AD6 LEU B 204 ? ALA B 223 ? LEU B 198 ALA B 217 1 ? 20 
HELX_P HELX_P34 AD7 SER B 228 ? HIS B 244 ? SER B 222 HIS B 238 1 ? 17 
HELX_P HELX_P35 AD8 HIS B 244 ? ALA B 249 ? HIS B 238 ALA B 243 1 ? 6  
HELX_P HELX_P36 AD9 ARG B 253 ? ASP B 263 ? ARG B 247 ASP B 257 1 ? 11 
HELX_P HELX_P37 AE1 SER B 283 ? LEU B 289 ? SER B 277 LEU B 283 1 ? 7  
HELX_P HELX_P38 AE2 ASN B 305 ? GLY B 321 ? ASN B 299 GLY B 315 1 ? 17 
HELX_P HELX_P39 AE3 SER B 324 ? SER B 329 ? SER B 318 SER B 323 1 ? 6  
HELX_P HELX_P40 AE4 LEU B 331 ? HIS B 336 ? LEU B 325 HIS B 330 1 ? 6  
# 
_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 LYS 57  NZ  ? ? ? 1_555 K CD . CD ? ? A LYS 51  A CD 509 1_555 ? ? ? ? ? ? ? 2.697 ? ? 
metalc2  metalc ? ? A CYS 141 SG  ? ? ? 1_555 K CD . CD ? ? A CYS 135 A CD 509 1_555 ? ? ? ? ? ? ? 2.608 ? ? 
metalc3  metalc ? ? A CYS 195 SG  ? ? ? 1_555 K CD . CD ? ? A CYS 189 A CD 509 1_555 ? ? ? ? ? ? ? 2.554 ? ? 
metalc4  metalc ? ? G ASN .   N   ? ? ? 1_555 K CD . CD ? ? A ASN 505 A CD 509 1_555 ? ? ? ? ? ? ? 2.569 ? ? 
metalc5  metalc ? ? G ASN .   O   ? ? ? 1_555 K CD . CD ? ? A ASN 505 A CD 509 1_555 ? ? ? ? ? ? ? 2.646 ? ? 
metalc6  metalc ? ? B LYS 57  NZ  ? ? ? 1_555 V CD . CD ? ? B LYS 51  B CD 411 1_555 ? ? ? ? ? ? ? 2.688 ? ? 
metalc7  metalc ? ? B CYS 141 SG  ? ? ? 1_555 V CD . CD ? ? B CYS 135 B CD 411 1_555 ? ? ? ? ? ? ? 2.583 ? ? 
metalc8  metalc ? ? B CYS 195 SG  ? ? ? 1_555 V CD . CD ? ? B CYS 189 B CD 411 1_555 ? ? ? ? ? ? ? 2.582 ? ? 
metalc9  metalc ? ? S ASN .   N   ? ? ? 1_555 V CD . CD ? ? B ASN 408 B CD 411 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc10 metalc ? ? S ASN .   OXT ? ? ? 1_555 V CD . CD ? ? B ASN 408 B CD 411 1_555 ? ? ? ? ? ? ? 2.574 ? ? 
# 
_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  NZ ? A LYS 57  ? A LYS 51  ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 SG  ? A CYS 141 ? A CYS 135 ? 1_555 101.0 ? 
2  NZ ? A LYS 57  ? A LYS 51  ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 SG  ? A CYS 195 ? A CYS 189 ? 1_555 102.2 ? 
3  SG ? A CYS 141 ? A CYS 135 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 SG  ? A CYS 195 ? A CYS 189 ? 1_555 107.0 ? 
4  NZ ? A LYS 57  ? A LYS 51  ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 N   ? G ASN .   ? A ASN 505 ? 1_555 94.2  ? 
5  SG ? A CYS 141 ? A CYS 135 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 N   ? G ASN .   ? A ASN 505 ? 1_555 100.8 ? 
6  SG ? A CYS 195 ? A CYS 189 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 N   ? G ASN .   ? A ASN 505 ? 1_555 144.0 ? 
7  NZ ? A LYS 57  ? A LYS 51  ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 O   ? G ASN .   ? A ASN 505 ? 1_555 157.1 ? 
8  SG ? A CYS 141 ? A CYS 135 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 O   ? G ASN .   ? A ASN 505 ? 1_555 93.3  ? 
9  SG ? A CYS 195 ? A CYS 189 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 O   ? G ASN .   ? A ASN 505 ? 1_555 90.4  ? 
10 N  ? G ASN .   ? A ASN 505 ? 1_555 CD ? K CD . ? A CD 509 ? 1_555 O   ? G ASN .   ? A ASN 505 ? 1_555 65.3  ? 
11 NZ ? B LYS 57  ? B LYS 51  ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 SG  ? B CYS 141 ? B CYS 135 ? 1_555 102.1 ? 
12 NZ ? B LYS 57  ? B LYS 51  ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 SG  ? B CYS 195 ? B CYS 189 ? 1_555 104.6 ? 
13 SG ? B CYS 141 ? B CYS 135 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 SG  ? B CYS 195 ? B CYS 189 ? 1_555 102.6 ? 
14 NZ ? B LYS 57  ? B LYS 51  ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 N   ? S ASN .   ? B ASN 408 ? 1_555 90.1  ? 
15 SG ? B CYS 141 ? B CYS 135 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 N   ? S ASN .   ? B ASN 408 ? 1_555 96.2  ? 
16 SG ? B CYS 195 ? B CYS 189 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 N   ? S ASN .   ? B ASN 408 ? 1_555 152.9 ? 
17 NZ ? B LYS 57  ? B LYS 51  ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 OXT ? S ASN .   ? B ASN 408 ? 1_555 155.7 ? 
18 SG ? B CYS 141 ? B CYS 135 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 OXT ? S ASN .   ? B ASN 408 ? 1_555 90.7  ? 
19 SG ? B CYS 195 ? B CYS 189 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 OXT ? S ASN .   ? B ASN 408 ? 1_555 92.5  ? 
20 N  ? S ASN .   ? B ASN 408 ? 1_555 CD ? V CD . ? B CD 411 ? 1_555 OXT ? S ASN .   ? B ASN 408 ? 1_555 67.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-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 LEU A 39  ? LEU A 43  ? LEU A 33  LEU A 37  
AA1 2 ILE A 21  ? ASP A 34  ? ILE A 15  ASP A 28  
AA1 3 LEU A 295 ? ILE A 301 ? LEU A 289 ILE A 295 
AA1 4 SER A 275 ? VAL A 280 ? SER A 269 VAL A 274 
AA1 5 LEU A 266 ? GLY A 271 ? LEU A 260 GLY A 265 
AA2 1 LEU A 39  ? LEU A 43  ? LEU A 33  LEU A 37  
AA2 2 ILE A 21  ? ASP A 34  ? ILE A 15  ASP A 28  
AA2 3 PHE A 13  ? ARG A 18  ? PHE A 7   ARG A 12  
AA2 4 GLY A 348 ? SER A 351 ? GLY A 342 SER A 345 
AA3 1 MET A 49  ? LEU A 51  ? MET A 43  LEU A 45  
AA3 2 PRO A 198 ? PRO A 203 ? PRO A 192 PRO A 197 
AA3 3 GLU A 189 ? THR A 192 ? GLU A 183 THR A 186 
AA4 1 LEU B 39  ? LEU B 43  ? LEU B 33  LEU B 37  
AA4 2 ILE B 21  ? ASP B 34  ? ILE B 15  ASP B 28  
AA4 3 LEU B 295 ? ILE B 301 ? LEU B 289 ILE B 295 
AA4 4 SER B 275 ? VAL B 280 ? SER B 269 VAL B 274 
AA4 5 LEU B 266 ? GLY B 271 ? LEU B 260 GLY B 265 
AA5 1 LEU B 39  ? LEU B 43  ? LEU B 33  LEU B 37  
AA5 2 ILE B 21  ? ASP B 34  ? ILE B 15  ASP B 28  
AA5 3 PHE B 13  ? ARG B 18  ? PHE B 7   ARG B 12  
AA5 4 GLY B 348 ? SER B 351 ? GLY B 342 SER B 345 
AA6 1 MET B 49  ? LEU B 51  ? MET B 43  LEU B 45  
AA6 2 PRO B 198 ? PRO B 203 ? PRO B 192 PRO B 197 
AA6 3 GLU B 189 ? THR B 192 ? GLU B 183 THR B 186 
# 
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 LEU A 40  ? O LEU A 34  N VAL A 32  ? N VAL A 26  
AA1 2 3 N VAL A 33  ? N VAL A 27  O GLY A 296 ? O GLY A 290 
AA1 3 4 O LEU A 295 ? O LEU A 289 N VAL A 280 ? N VAL A 274 
AA1 4 5 O SER A 275 ? O SER A 269 N GLY A 271 ? N GLY A 265 
AA2 1 2 O LEU A 40  ? O LEU A 34  N VAL A 32  ? N VAL A 26  
AA2 2 3 O GLU A 23  ? O GLU A 17  N THR A 16  ? N THR A 10  
AA2 3 4 N VAL A 15  ? N VAL A 9   O SER A 351 ? O SER A 345 
AA3 1 2 N THR A 50  ? N THR A 44  O PHE A 202 ? O PHE A 196 
AA3 2 3 O ALA A 201 ? O ALA A 195 N GLU A 189 ? N GLU A 183 
AA4 1 2 O LEU B 40  ? O LEU B 34  N VAL B 32  ? N VAL B 26  
AA4 2 3 N VAL B 33  ? N VAL B 27  O GLY B 296 ? O GLY B 290 
AA4 3 4 O LEU B 295 ? O LEU B 289 N VAL B 280 ? N VAL B 274 
AA4 4 5 O SER B 275 ? O SER B 269 N GLY B 271 ? N GLY B 265 
AA5 1 2 O LEU B 40  ? O LEU B 34  N VAL B 32  ? N VAL B 26  
AA5 2 3 O GLU B 23  ? O GLU B 17  N THR B 16  ? N THR B 10  
AA5 3 4 N VAL B 15  ? N VAL B 9   O SER B 351 ? O SER B 345 
AA6 1 2 N THR B 50  ? N THR B 44  O PHE B 202 ? O PHE B 196 
AA6 2 3 O ALA B 201 ? O ALA B 195 N GLU B 189 ? N GLU B 183 
# 
_pdbx_entry_details.entry_id                   9G67 
_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 GLU A 17  ? ? -92.31  -73.89  
2  1 ARG A 47  ? ? 53.26   -137.96 
3  1 ASN A 190 ? ? 80.49   10.49   
4  1 ALA A 243 ? ? -147.41 -87.18  
5  1 ALA A 268 ? ? 71.50   50.12   
6  1 PRO A 347 ? ? -76.99  44.24   
7  1 GLU B 17  ? ? -96.94  -72.89  
8  1 ARG B 47  ? ? 57.41   -140.72 
9  1 ASN B 190 ? ? 81.58   21.10   
10 1 ALA B 243 ? ? -140.29 -84.01  
11 1 ALA B 268 ? ? 73.91   52.92   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 13.269  6.245   19.075 0.0913666524242 0.125302808061  0.184750057643 0.00816481887959 
0.011487754985    -0.0190301611195 7.51077912633  4.06831515165  1.2204613485   4.89134654823    1.70874518601     0.830514087807  
-0.136205548423  0.027216551638   0.066031307858    0.268678921036   0.0509876853964 0.0923639376063 -0.338515673247 
-0.0767406835879 -0.00858454797004 
'X-RAY DIFFRACTION' 2  ? refined -0.486  -12.421 35.307 0.156365287515  0.214735610181  0.238741408314 -0.079969104174  
0.0481181595828   -0.0519363467971 0.927169206983 1.7945581514   0.371820147758 0.324241762411   -0.443810932736   -0.290395411091 
0.0724527852663  -0.0947325636065 -0.0201802993607  -0.122857901277  -0.12029418155  0.256879835685  0.299511275902  
0.130296602482   -0.137610127282   
'X-RAY DIFFRACTION' 3  ? refined 8.442   -15.996 45.698 0.250629078687  0.219852959684  0.209492481407 -0.0859795780651 
-0.00160768138453 0.0378627015893  3.12573163221  1.7392958404   2.70069333903  0.865967252518   1.41036546774     1.8872265958    
0.192393244054   -0.0473247050213 -0.118509826035   -0.178048597456  -0.107141358197 -0.234331227451 0.37186363386   
0.173851771428   0.115445405357    
'X-RAY DIFFRACTION' 4  ? refined 1.181   -17.175 25.567 0.128085242219  0.177083224732  0.273261679507 -0.103999138044  
0.0218667337046   -0.0841374837238 1.90785286332  0.731630065793 0.85862377533  0.117365868272   0.553685035459    -0.64142343757  
0.018155371481   -0.141027622394  0.0226966684126   0.0991498571803  -0.110477406162 0.113796858294  -0.042849748241 
0.239510341142   -0.290928464745   
'X-RAY DIFFRACTION' 5  ? refined -13.060 -12.597 31.668 0.190725106994  0.479379998183  0.387203548316 -0.133893998224  
0.068576421872    -0.0581684236531 2.89406436629  6.98001715999  0.659301459104 -0.0957253927259 -1.3217669921     -0.582105881405 
-0.0185850620622 -0.0495126999379 -0.0487977450305  0.559714145519   -0.227504588644 0.924042012816  -0.189046920112 
0.259503010967   -0.740932594498   
'X-RAY DIFFRACTION' 6  ? refined 1.618   5.005   28.276 0.0466130977107 0.142181796605  0.269712803966 0.00697738910783 
0.0354882203498   -0.0647845488169 1.07774454655  1.09470668636  1.14994058306  0.181663680895   -0.392106463396   -0.157175606863 
0.109001351554   -0.0885406428177 -0.00714809410624 -0.124447160501  0.241537238173  0.27972058043   0.169777793086  
-0.081355145423  -0.253264214509   
'X-RAY DIFFRACTION' 7  ? refined 10.350  -10.606 35.286 0.398591769146  0.379699475407  0.503534076199 -0.150541945671  
0.060977999473    0.145222090375   3.818777945    8.32560309395  1.99998028561  -1.34806927439   0.864889912784    -6.32932338966  
0.147433364803   -0.444271416763  0.237241218264    0.604269543288   2.28108119331   -0.807456493752 -0.92958993254  
0.330290929258   -0.045891844638   
'X-RAY DIFFRACTION' 8  ? refined 29.861  0.585   16.857 0.0884812478589 0.117745447573  0.177212096548 0.0105670764848  
-0.00581636336879 0.00578066949969 2.41546167542  2.16291771181  1.52623611942  0.975016500286   -0.866468710018   -0.498722329384 
-0.133322762167  0.00653773304898 0.097853921281    0.172931632636   -0.140433882864 -0.142036851826 -0.230722597777 
0.0578495365947  0.0231780750176   
'X-RAY DIFFRACTION' 9  ? refined 34.917  20.854  41.706 0.242896140162  0.203259486734  0.228371487893 -0.127066759649  
0.0363871326291   -0.0522880066239 1.29426277657  1.24543827907  0.730820679363 0.544569464944   -0.312936198632   -0.218536544433 
0.225966976424   -0.214525246988  -0.0192154219771  -0.338618083122  0.197405739245  0.203538705444  0.466932930302  
-0.109944314113  -0.107113106454   
'X-RAY DIFFRACTION' 10 ? refined 40.848  9.261   28.085 0.0789051196711 0.134669097488  0.209027627007 -0.027938918632  
-0.00771618909127 0.0197518012617  1.46296291848  1.29856418192  0.941927049953 0.599705842592   0.000360180949851 0.212176543202  
0.085757067051   -0.064860955363  -0.0188538634719  -0.0946866733632 -0.052893972436 -0.27424712036  0.102346863301  
-0.013032872841  0.184157679536    
'X-RAY DIFFRACTION' 11 ? refined 32.294  -7.412  23.643 0.158804956722  0.0880416378999 0.246130136556 0.0113668967146  
0.0120521025547   -0.010021627599  2.5281701448   1.58895446791  2.79777433739  0.819927306387   -0.4056381951     -0.643820199612 
-0.111576366793  -0.0326248676227 0.131422193423    0.092444311707   -0.334516516722 -0.254944101851 -0.143959655235 
0.0729504504039  0.0256347707815   
'X-RAY DIFFRACTION' 12 ? refined 28.385  14.558  35.015 0.287009071549  0.526193896821  0.728361525916 -0.0924781827362 
-0.0593458486834  -0.182942906727  7.65541164439  4.8925110524   7.31724691861  -5.19839847137   0.196654067448    3.02295435607   
-0.0850019675209 0.382364909554   -0.33878357829    0.720630804287   -2.31716620623  0.260348923879  -0.546581836625 
0.357981300727   0.315192067772    
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  A 2   A 28  '( CHAIN A AND RESID 2:28 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 29  A 97  '( CHAIN A AND RESID 29:97 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 98  A 161 '( CHAIN A AND RESID 98:161 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 162 A 216 '( CHAIN A AND RESID 162:216 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 217 A 237 '( CHAIN A AND RESID 217:237 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 238 A 352 '( CHAIN A AND RESID 238:352 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  A 505 A 505 '( CHAIN A AND RESID 505:505 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B -3  B 46  '( CHAIN B AND RESID -3:46 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 47  B 175 '( CHAIN B AND RESID 47:175 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 176 B 314 '( CHAIN B AND RESID 176:314 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 315 B 367 '( CHAIN B AND RESID 315:367 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 408 B 408 '( CHAIN B AND RESID 408:408 )' ? ? ? ? ? 
# 
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 GLY -5  ? A GLY 1   
2  1 Y 1 A ILE -4  ? A ILE 2   
3  1 Y 1 A ASP -3  ? A ASP 3   
4  1 Y 1 A PRO -2  ? A PRO 4   
5  1 Y 1 A PHE -1  ? A PHE 5   
6  1 Y 1 A THR 0   ? A THR 6   
7  1 Y 1 A MET 1   ? A MET 7   
8  1 Y 1 A SER 353 ? A SER 359 
9  1 Y 1 A LYS 354 ? A LYS 360 
10 1 Y 1 A SER 355 ? A SER 361 
11 1 Y 1 A ASN 356 ? A ASN 362 
12 1 Y 1 A VAL 357 ? A VAL 363 
13 1 Y 1 A ASP 358 ? A ASP 364 
14 1 Y 1 A ASP 359 ? A ASP 365 
15 1 Y 1 A PRO 360 ? A PRO 366 
16 1 Y 1 A ARG 361 ? A ARG 367 
17 1 Y 1 A LEU 362 ? A LEU 368 
18 1 Y 1 A ALA 363 ? A ALA 369 
19 1 Y 1 A ALA 364 ? A ALA 370 
20 1 Y 1 A VAL 365 ? A VAL 371 
21 1 Y 1 A ALA 366 ? A ALA 372 
22 1 Y 1 A ARG 367 ? A ARG 373 
23 1 Y 1 B GLY -5  ? B GLY 1   
24 1 Y 1 B ILE -4  ? B ILE 2   
25 1 Y 1 B SER 353 ? B SER 359 
26 1 Y 1 B LYS 354 ? B LYS 360 
27 1 Y 1 B SER 355 ? B SER 361 
28 1 Y 1 B ASN 356 ? B ASN 362 
29 1 Y 1 B VAL 357 ? B VAL 363 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CD  CD   CD N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
EDO C1   C  N N 90  
EDO O1   O  N N 91  
EDO C2   C  N N 92  
EDO O2   O  N N 93  
EDO H11  H  N N 94  
EDO H12  H  N N 95  
EDO HO1  H  N N 96  
EDO H21  H  N N 97  
EDO H22  H  N N 98  
EDO HO2  H  N N 99  
GLN N    N  N N 100 
GLN CA   C  N S 101 
GLN C    C  N N 102 
GLN O    O  N N 103 
GLN CB   C  N N 104 
GLN CG   C  N N 105 
GLN CD   C  N N 106 
GLN OE1  O  N N 107 
GLN NE2  N  N N 108 
GLN OXT  O  N N 109 
GLN H    H  N N 110 
GLN H2   H  N N 111 
GLN HA   H  N N 112 
GLN HB2  H  N N 113 
GLN HB3  H  N N 114 
GLN HG2  H  N N 115 
GLN HG3  H  N N 116 
GLN HE21 H  N N 117 
GLN HE22 H  N N 118 
GLN HXT  H  N N 119 
GLU N    N  N N 120 
GLU CA   C  N S 121 
GLU C    C  N N 122 
GLU O    O  N N 123 
GLU CB   C  N N 124 
GLU CG   C  N N 125 
GLU CD   C  N N 126 
GLU OE1  O  N N 127 
GLU OE2  O  N N 128 
GLU OXT  O  N N 129 
GLU H    H  N N 130 
GLU H2   H  N N 131 
GLU HA   H  N N 132 
GLU HB2  H  N N 133 
GLU HB3  H  N N 134 
GLU HG2  H  N N 135 
GLU HG3  H  N N 136 
GLU HE2  H  N N 137 
GLU HXT  H  N N 138 
GLY N    N  N N 139 
GLY CA   C  N N 140 
GLY C    C  N N 141 
GLY O    O  N N 142 
GLY OXT  O  N N 143 
GLY H    H  N N 144 
GLY H2   H  N N 145 
GLY HA2  H  N N 146 
GLY HA3  H  N N 147 
GLY HXT  H  N N 148 
HIS N    N  N N 149 
HIS CA   C  N S 150 
HIS C    C  N N 151 
HIS O    O  N N 152 
HIS CB   C  N N 153 
HIS CG   C  Y N 154 
HIS ND1  N  Y N 155 
HIS CD2  C  Y N 156 
HIS CE1  C  Y N 157 
HIS NE2  N  Y N 158 
HIS OXT  O  N N 159 
HIS H    H  N N 160 
HIS H2   H  N N 161 
HIS HA   H  N N 162 
HIS HB2  H  N N 163 
HIS HB3  H  N N 164 
HIS HD1  H  N N 165 
HIS HD2  H  N N 166 
HIS HE1  H  N N 167 
HIS HE2  H  N N 168 
HIS HXT  H  N N 169 
HOH O    O  N N 170 
HOH H1   H  N N 171 
HOH H2   H  N N 172 
ILE N    N  N N 173 
ILE CA   C  N S 174 
ILE C    C  N N 175 
ILE O    O  N N 176 
ILE CB   C  N S 177 
ILE CG1  C  N N 178 
ILE CG2  C  N N 179 
ILE CD1  C  N N 180 
ILE OXT  O  N N 181 
ILE H    H  N N 182 
ILE H2   H  N N 183 
ILE HA   H  N N 184 
ILE HB   H  N N 185 
ILE HG12 H  N N 186 
ILE HG13 H  N N 187 
ILE HG21 H  N N 188 
ILE HG22 H  N N 189 
ILE HG23 H  N N 190 
ILE HD11 H  N N 191 
ILE HD12 H  N N 192 
ILE HD13 H  N N 193 
ILE HXT  H  N N 194 
LEU N    N  N N 195 
LEU CA   C  N S 196 
LEU C    C  N N 197 
LEU O    O  N N 198 
LEU CB   C  N N 199 
LEU CG   C  N N 200 
LEU CD1  C  N N 201 
LEU CD2  C  N N 202 
LEU OXT  O  N N 203 
LEU H    H  N N 204 
LEU H2   H  N N 205 
LEU HA   H  N N 206 
LEU HB2  H  N N 207 
LEU HB3  H  N N 208 
LEU HG   H  N N 209 
LEU HD11 H  N N 210 
LEU HD12 H  N N 211 
LEU HD13 H  N N 212 
LEU HD21 H  N N 213 
LEU HD22 H  N N 214 
LEU HD23 H  N N 215 
LEU HXT  H  N N 216 
LYS N    N  N N 217 
LYS CA   C  N S 218 
LYS C    C  N N 219 
LYS O    O  N N 220 
LYS CB   C  N N 221 
LYS CG   C  N N 222 
LYS CD   C  N N 223 
LYS CE   C  N N 224 
LYS NZ   N  N N 225 
LYS OXT  O  N N 226 
LYS H    H  N N 227 
LYS H2   H  N N 228 
LYS HA   H  N N 229 
LYS HB2  H  N N 230 
LYS HB3  H  N N 231 
LYS HG2  H  N N 232 
LYS HG3  H  N N 233 
LYS HD2  H  N N 234 
LYS HD3  H  N N 235 
LYS HE2  H  N N 236 
LYS HE3  H  N N 237 
LYS HZ1  H  N N 238 
LYS HZ2  H  N N 239 
LYS HZ3  H  N N 240 
LYS HXT  H  N N 241 
MET N    N  N N 242 
MET CA   C  N S 243 
MET C    C  N N 244 
MET O    O  N N 245 
MET CB   C  N N 246 
MET CG   C  N N 247 
MET SD   S  N N 248 
MET CE   C  N N 249 
MET OXT  O  N N 250 
MET H    H  N N 251 
MET H2   H  N N 252 
MET HA   H  N N 253 
MET HB2  H  N N 254 
MET HB3  H  N N 255 
MET HG2  H  N N 256 
MET HG3  H  N N 257 
MET HE1  H  N N 258 
MET HE2  H  N N 259 
MET HE3  H  N N 260 
MET HXT  H  N N 261 
PHE N    N  N N 262 
PHE CA   C  N S 263 
PHE C    C  N N 264 
PHE O    O  N N 265 
PHE CB   C  N N 266 
PHE CG   C  Y N 267 
PHE CD1  C  Y N 268 
PHE CD2  C  Y N 269 
PHE CE1  C  Y N 270 
PHE CE2  C  Y N 271 
PHE CZ   C  Y N 272 
PHE OXT  O  N N 273 
PHE H    H  N N 274 
PHE H2   H  N N 275 
PHE HA   H  N N 276 
PHE HB2  H  N N 277 
PHE HB3  H  N N 278 
PHE HD1  H  N N 279 
PHE HD2  H  N N 280 
PHE HE1  H  N N 281 
PHE HE2  H  N N 282 
PHE HZ   H  N N 283 
PHE HXT  H  N N 284 
PRO N    N  N N 285 
PRO CA   C  N S 286 
PRO C    C  N N 287 
PRO O    O  N N 288 
PRO CB   C  N N 289 
PRO CG   C  N N 290 
PRO CD   C  N N 291 
PRO OXT  O  N N 292 
PRO H    H  N N 293 
PRO HA   H  N N 294 
PRO HB2  H  N N 295 
PRO HB3  H  N N 296 
PRO HG2  H  N N 297 
PRO HG3  H  N N 298 
PRO HD2  H  N N 299 
PRO HD3  H  N N 300 
PRO HXT  H  N N 301 
SER N    N  N N 302 
SER CA   C  N S 303 
SER C    C  N N 304 
SER O    O  N N 305 
SER CB   C  N N 306 
SER OG   O  N N 307 
SER OXT  O  N N 308 
SER H    H  N N 309 
SER H2   H  N N 310 
SER HA   H  N N 311 
SER HB2  H  N N 312 
SER HB3  H  N N 313 
SER HG   H  N N 314 
SER HXT  H  N N 315 
THR N    N  N N 316 
THR CA   C  N S 317 
THR C    C  N N 318 
THR O    O  N N 319 
THR CB   C  N R 320 
THR OG1  O  N N 321 
THR CG2  C  N N 322 
THR OXT  O  N N 323 
THR H    H  N N 324 
THR H2   H  N N 325 
THR HA   H  N N 326 
THR HB   H  N N 327 
THR HG1  H  N N 328 
THR HG21 H  N N 329 
THR HG22 H  N N 330 
THR HG23 H  N N 331 
THR HXT  H  N N 332 
TRP N    N  N N 333 
TRP CA   C  N S 334 
TRP C    C  N N 335 
TRP O    O  N N 336 
TRP CB   C  N N 337 
TRP CG   C  Y N 338 
TRP CD1  C  Y N 339 
TRP CD2  C  Y N 340 
TRP NE1  N  Y N 341 
TRP CE2  C  Y N 342 
TRP CE3  C  Y N 343 
TRP CZ2  C  Y N 344 
TRP CZ3  C  Y N 345 
TRP CH2  C  Y N 346 
TRP OXT  O  N N 347 
TRP H    H  N N 348 
TRP H2   H  N N 349 
TRP HA   H  N N 350 
TRP HB2  H  N N 351 
TRP HB3  H  N N 352 
TRP HD1  H  N N 353 
TRP HE1  H  N N 354 
TRP HE3  H  N N 355 
TRP HZ2  H  N N 356 
TRP HZ3  H  N N 357 
TRP HH2  H  N N 358 
TRP HXT  H  N N 359 
TYR N    N  N N 360 
TYR CA   C  N S 361 
TYR C    C  N N 362 
TYR O    O  N N 363 
TYR CB   C  N N 364 
TYR CG   C  Y N 365 
TYR CD1  C  Y N 366 
TYR CD2  C  Y N 367 
TYR CE1  C  Y N 368 
TYR CE2  C  Y N 369 
TYR CZ   C  Y N 370 
TYR OH   O  N N 371 
TYR OXT  O  N N 372 
TYR H    H  N N 373 
TYR H2   H  N N 374 
TYR HA   H  N N 375 
TYR HB2  H  N N 376 
TYR HB3  H  N N 377 
TYR HD1  H  N N 378 
TYR HD2  H  N N 379 
TYR HE1  H  N N 380 
TYR HE2  H  N N 381 
TYR HH   H  N N 382 
TYR HXT  H  N N 383 
VAL N    N  N N 384 
VAL CA   C  N S 385 
VAL C    C  N N 386 
VAL O    O  N N 387 
VAL CB   C  N N 388 
VAL CG1  C  N N 389 
VAL CG2  C  N N 390 
VAL OXT  O  N N 391 
VAL H    H  N N 392 
VAL H2   H  N N 393 
VAL HA   H  N N 394 
VAL HB   H  N N 395 
VAL HG11 H  N N 396 
VAL HG12 H  N N 397 
VAL HG13 H  N N 398 
VAL HG21 H  N N 399 
VAL HG22 H  N N 400 
VAL HG23 H  N N 401 
VAL HXT  H  N N 402 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'Polish National Science Centre' 
_pdbx_audit_support.country                Poland 
_pdbx_audit_support.grant_number           2020/37/B/NZ1/03250 
_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   7os5 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_related_exp_data_set.ordinal              1 
_pdbx_related_exp_data_set.data_reference       10.60884/GJ5MZ0 
_pdbx_related_exp_data_set.metadata_reference   10.60884/GJ5MZ0 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9G67 
_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]   0.012782 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010907 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009409 
_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.
;
? 
CD ? ? 36.69012 11.13669 ? ? 1.60906  22.94611 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341  ? ? 1.04373  23.83732 ? ? 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.
;
? 
# 
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   . THR A 1 8   ? 8.89000   -3.09200  5.15400  1.000 63.37000 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 8   ? 10.25500  -2.96200  5.67500  1.000 70.93000 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 8   ? 10.28900  -1.90700  6.81400  1.000 69.18000 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 8   ? 9.97500   -0.73000  6.59900  1.000 68.22000 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 8   ? 11.27500  -2.62700  4.51400  1.000 75.77000 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 8   ? 12.61600  -2.47500  5.01600  1.000 66.32000 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 8   ? 10.85800  -1.37800  3.73100  1.000 80.62000 ? 2   THR A CG2 1 
ATOM   8    N  N   . PRO A 1 9   ? 10.63500  -2.35100  8.03000  1.000 65.23000 ? 3   PRO A N   1 
ATOM   9    C  CA  . PRO A 1 9   ? 10.50300  -1.48300  9.21000  1.000 58.46000 ? 3   PRO A CA  1 
ATOM   10   C  C   . PRO A 1 9   ? 11.24600  -0.16300  9.06400  1.000 60.56000 ? 3   PRO A C   1 
ATOM   11   O  O   . PRO A 1 9   ? 12.35100  -0.10300  8.51600  1.000 62.25000 ? 3   PRO A O   1 
ATOM   12   C  CB  . PRO A 1 9   ? 11.09900  -2.33500  10.33800 1.000 49.05000 ? 3   PRO A CB  1 
ATOM   13   C  CG  . PRO A 1 9   ? 10.77400  -3.72600  9.92600  1.000 53.42000 ? 3   PRO A CG  1 
ATOM   14   C  CD  . PRO A 1 9   ? 10.97500  -3.73300  8.41800  1.000 66.56000 ? 3   PRO A CD  1 
ATOM   15   N  N   . SER A 1 10  ? 10.62600  0.89900   9.57300  1.000 46.09000 ? 4   SER A N   1 
ATOM   16   C  CA  . SER A 1 10  ? 11.22500  2.21900   9.49800  1.000 49.16000 ? 4   SER A CA  1 
ATOM   17   C  C   . SER A 1 10  ? 12.04300  2.49100   10.76300 1.000 41.93000 ? 4   SER A C   1 
ATOM   18   O  O   . SER A 1 10  ? 12.05300  1.70500   11.71300 1.000 39.13000 ? 4   SER A O   1 
ATOM   19   C  CB  . SER A 1 10  ? 10.14100  3.27700   9.29000  1.000 45.67000 ? 4   SER A CB  1 
ATOM   20   O  OG  . SER A 1 10  ? 9.28600   3.33000   10.41700 1.000 49.05000 ? 4   SER A OG  1 
ATOM   21   N  N   . GLU A 1 11  ? 12.74100  3.61700   10.76300 1.000 39.17000 ? 5   GLU A N   1 
ATOM   22   C  CA  . GLU A 1 11  ? 13.65500  3.98300   11.84100 1.000 38.56000 ? 5   GLU A CA  1 
ATOM   23   C  C   . GLU A 1 11  ? 12.94000  4.90500   12.81400 1.000 35.14000 ? 5   GLU A C   1 
ATOM   24   O  O   . GLU A 1 11  ? 12.93000  6.12300   12.61800 1.000 32.21000 ? 5   GLU A O   1 
ATOM   25   C  CB  . GLU A 1 11  ? 14.87600  4.67700   11.26000 1.000 46.02000 ? 5   GLU A CB  1 
ATOM   26   C  CG  . GLU A 1 11  ? 15.51800  3.90300   10.13700 1.000 53.45000 ? 5   GLU A CG  1 
ATOM   27   C  CD  . GLU A 1 11  ? 16.45100  2.83600   10.66600 1.000 57.53000 ? 5   GLU A CD  1 
ATOM   28   O  OE1 . GLU A 1 11  ? 17.63700  3.16800   10.95200 1.000 57.55000 ? 5   GLU A OE1 1 
ATOM   29   O  OE2 . GLU A 1 11  ? 15.97800  1.68400   10.81600 1.000 50.71000 ? 5   GLU A OE2 1 
ATOM   30   N  N   . ASP A 1 12  ? 12.37400  4.33900   13.88500 1.000 24.76000 ? 6   ASP A N   1 
ATOM   31   C  CA  . ASP A 1 12  ? 11.54100  5.08900   14.82500 1.000 26.04000 ? 6   ASP A CA  1 
ATOM   32   C  C   . ASP A 1 12  ? 12.23200  5.17300   16.18400 1.000 24.63000 ? 6   ASP A C   1 
ATOM   33   O  O   . ASP A 1 12  ? 12.51600  4.14100   16.81100 1.000 19.52000 ? 6   ASP A O   1 
ATOM   34   C  CB  . ASP A 1 12  ? 10.15800  4.43600   14.94600 1.000 23.40000 ? 6   ASP A CB  1 
ATOM   35   C  CG  . ASP A 1 12  ? 9.37900   4.49300   13.65400 1.000 26.10000 ? 6   ASP A CG  1 
ATOM   36   O  OD1 . ASP A 1 12  ? 9.39000   5.55600   13.00500 1.000 33.30000 ? 6   ASP A OD1 1 
ATOM   37   O  OD2 . ASP A 1 12  ? 8.75900   3.48600   13.26000 1.000 24.51000 ? 6   ASP A OD2 1 
ATOM   38   N  N   . PHE A 1 13  ? 12.48800  6.39500   16.64100 1.000 21.94000 ? 7   PHE A N   1 
ATOM   39   C  CA  . PHE A 1 13  ? 13.29100  6.65600   17.83300 1.000 21.48000 ? 7   PHE A CA  1 
ATOM   40   C  C   . PHE A 1 13  ? 12.54900  7.56800   18.80500 1.000 21.53000 ? 7   PHE A C   1 
ATOM   41   O  O   . PHE A 1 13  ? 11.77400  8.43800   18.39800 1.000 22.62000 ? 7   PHE A O   1 
ATOM   42   C  CB  . PHE A 1 13  ? 14.65500  7.32900   17.44200 1.000 18.96000 ? 7   PHE A CB  1 
ATOM   43   C  CG  . PHE A 1 13  ? 15.56700  6.40800   16.69900 1.000 24.92000 ? 7   PHE A CG  1 
ATOM   44   C  CD1 . PHE A 1 13  ? 15.50700  6.31300   15.31700 1.000 28.60000 ? 7   PHE A CD1 1 
ATOM   45   C  CD2 . PHE A 1 13  ? 16.44700  5.58400   17.39300 1.000 23.59000 ? 7   PHE A CD2 1 
ATOM   46   C  CE1 . PHE A 1 13  ? 16.33700  5.41900   14.63500 1.000 37.56000 ? 7   PHE A CE1 1 
ATOM   47   C  CE2 . PHE A 1 13  ? 17.28300  4.67200   16.72300 1.000 27.93000 ? 7   PHE A CE2 1 
ATOM   48   C  CZ  . PHE A 1 13  ? 17.23800  4.59700   15.34400 1.000 34.66000 ? 7   PHE A CZ  1 
ATOM   49   N  N   . VAL A 1 14  ? 12.78600  7.35900   20.10300 1.000 17.28000 ? 8   VAL A N   1 
ATOM   50   C  CA  . VAL A 1 14  ? 12.54400  8.37800   21.12300 1.000 17.02000 ? 8   VAL A CA  1 
ATOM   51   C  C   . VAL A 1 14  ? 13.91300  8.95200   21.47400 1.000 17.83000 ? 8   VAL A C   1 
ATOM   52   O  O   . VAL A 1 14  ? 14.89500  8.21200   21.56100 1.000 16.81000 ? 8   VAL A O   1 
ATOM   53   C  CB  . VAL A 1 14  ? 11.81000  7.79700   22.35800 1.000 19.18000 ? 8   VAL A CB  1 
ATOM   54   C  CG1 . VAL A 1 14  ? 12.47400  6.54000   22.86300 1.000 20.46000 ? 8   VAL A CG1 1 
ATOM   55   C  CG2 . VAL A 1 14  ? 11.73900  8.81400   23.45900 1.000 17.49000 ? 8   VAL A CG2 1 
ATOM   56   N  N   . VAL A 1 15  ? 14.01100  10.27400  21.56400 1.000 16.63000 ? 9   VAL A N   1 
ATOM   57   C  CA  . VAL A 1 15  ? 15.30500  10.94500  21.60700 1.000 16.85000 ? 9   VAL A CA  1 
ATOM   58   C  C   . VAL A 1 15  ? 15.31100  11.83700  22.83300 1.000 17.16000 ? 9   VAL A C   1 
ATOM   59   O  O   . VAL A 1 15  ? 14.33600  12.54200  23.08500 1.000 17.94000 ? 9   VAL A O   1 
ATOM   60   C  CB  . VAL A 1 15  ? 15.55800  11.76000  20.32200 1.000 19.50000 ? 9   VAL A CB  1 
ATOM   61   C  CG1 . VAL A 1 15  ? 16.85900  12.53400  20.42500 1.000 21.31000 ? 9   VAL A CG1 1 
ATOM   62   C  CG2 . VAL A 1 15  ? 15.58300  10.83800  19.07100 1.000 16.82000 ? 9   VAL A CG2 1 
ATOM   63   N  N   . THR A 1 16  ? 16.39000  11.79300  23.61600 1.000 20.36000 ? 10  THR A N   1 
ATOM   64   C  CA  . THR A 1 16  ? 16.53800  12.75000  24.70500 1.000 17.44000 ? 10  THR A CA  1 
ATOM   65   C  C   . THR A 1 16  ? 17.62200  13.75400  24.34700 1.000 19.71000 ? 10  THR A C   1 
ATOM   66   O  O   . THR A 1 16  ? 18.57900  13.43200  23.65100 1.000 19.09000 ? 10  THR A O   1 
ATOM   67   C  CB  . THR A 1 16  ? 16.85900  12.04300  26.01400 1.000 19.29000 ? 10  THR A CB  1 
ATOM   68   O  OG1 . THR A 1 16  ? 18.16700  11.48700  25.93800 1.000 19.88000 ? 10  THR A OG1 1 
ATOM   69   C  CG2 . THR A 1 16  ? 15.91100  10.90500  26.16400 1.000 23.31000 ? 10  THR A CG2 1 
ATOM   70   N  N   . ASP A 1 17  ? 17.45100  14.98900  24.78900 1.000 19.54000 ? 11  ASP A N   1 
ATOM   71   C  CA  . ASP A 1 17  ? 18.36300  16.06100  24.42600 1.000 19.12000 ? 11  ASP A CA  1 
ATOM   72   C  C   . ASP A 1 17  ? 18.79900  16.81100  25.67500 1.000 19.47000 ? 11  ASP A C   1 
ATOM   73   O  O   . ASP A 1 17  ? 18.08900  16.85900  26.67800 1.000 21.53000 ? 11  ASP A O   1 
ATOM   74   C  CB  . ASP A 1 17  ? 17.73200  17.08700  23.43200 1.000 19.98000 ? 11  ASP A CB  1 
ATOM   75   C  CG  . ASP A 1 17  ? 16.63500  17.96500  24.09000 1.000 25.78000 ? 11  ASP A CG  1 
ATOM   76   O  OD1 . ASP A 1 17  ? 15.46600  17.50500  24.19700 1.000 24.66000 ? 11  ASP A OD1 1 
ATOM   77   O  OD2 . ASP A 1 17  ? 16.92300  19.11200  24.51500 1.000 27.82000 ? 11  ASP A OD2 1 
ATOM   78   N  N   . ARG A 1 18  ? 19.96500  17.43600  25.58100 1.000 19.08000 ? 12  ARG A N   1 
ATOM   79   C  CA  . ARG A 1 18  ? 20.43500  18.38600  26.57100 1.000 21.35000 ? 12  ARG A CA  1 
ATOM   80   C  C   . ARG A 1 18  ? 20.59900  19.69900  25.81800 1.000 20.90000 ? 12  ARG A C   1 
ATOM   81   O  O   . ARG A 1 18  ? 21.51200  19.83800  25.00100 1.000 19.10000 ? 12  ARG A O   1 
ATOM   82   C  CB  . ARG A 1 18  ? 21.74300  17.88700  27.20300 1.000 18.82000 ? 12  ARG A CB  1 
ATOM   83   C  CG  . ARG A 1 18  ? 22.26200  18.71600  28.37800 1.000 20.20000 ? 12  ARG A CG  1 
ATOM   84   C  CD  . ARG A 1 18  ? 23.46300  18.02600  29.09300 1.000 21.78000 ? 12  ARG A CD  1 
ATOM   85   N  NE  . ARG A 1 18  ? 23.02900  16.76800  29.69700 1.000 19.95000 ? 12  ARG A NE  1 
ATOM   86   C  CZ  . ARG A 1 18  ? 22.55000  16.66200  30.93300 1.000 26.22000 ? 12  ARG A CZ  1 
ATOM   87   N  NH1 . ARG A 1 18  ? 22.56400  17.69400  31.77300 1.000 23.38000 ? 12  ARG A NH1 1 
ATOM   88   N  NH2 . ARG A 1 18  ? 22.02100  15.50700  31.32500 1.000 20.78000 ? 12  ARG A NH2 1 
ATOM   89   N  N   . GLY A 1 19  ? 19.68100  20.63700  26.03800 1.000 22.43000 ? 13  GLY A N   1 
ATOM   90   C  CA  . GLY A 1 19  ? 19.80200  21.92700  25.39400 1.000 26.33000 ? 13  GLY A CA  1 
ATOM   91   C  C   . GLY A 1 19  ? 19.65500  21.88200  23.88600 1.000 25.58000 ? 13  GLY A C   1 
ATOM   92   O  O   . GLY A 1 19  ? 20.30800  22.66500  23.19100 1.000 29.23000 ? 13  GLY A O   1 
ATOM   93   N  N   . GLY A 1 20  ? 18.81100  20.99200  23.36200 1.000 25.39000 ? 14  GLY A N   1 
ATOM   94   C  CA  . GLY A 1 20  ? 18.69800  20.75600  21.93100 1.000 25.12000 ? 14  GLY A CA  1 
ATOM   95   C  C   . GLY A 1 20  ? 19.74500  19.81600  21.34100 1.000 26.51000 ? 14  GLY A C   1 
ATOM   96   O  O   . GLY A 1 20  ? 19.57600  19.35300  20.20000 1.000 28.52000 ? 14  GLY A O   1 
ATOM   97   N  N   . ILE A 1 21  ? 20.80600  19.50300  22.07100 1.000 19.70000 ? 15  ILE A N   1 
ATOM   98   C  CA  . ILE A 1 21  ? 21.85200  18.59600  21.60300 1.000 18.38000 ? 15  ILE A CA  1 
ATOM   99   C  C   . ILE A 1 21  ? 21.45800  17.16300  21.96100 1.000 17.06000 ? 15  ILE A C   1 
ATOM   100  O  O   . ILE A 1 21  ? 21.15700  16.86900  23.12700 1.000 17.16000 ? 15  ILE A O   1 
ATOM   101  C  CB  . ILE A 1 21  ? 23.20200  18.96400  22.25000 1.000 16.51000 ? 15  ILE A CB  1 
ATOM   102  C  CG1 . ILE A 1 21  ? 23.50100  20.46300  22.11300 1.000 16.34000 ? 15  ILE A CG1 1 
ATOM   103  C  CG2 . ILE A 1 21  ? 24.33700  18.09400  21.71000 1.000 17.82000 ? 15  ILE A CG2 1 
ATOM   104  C  CD1 . ILE A 1 21  ? 24.52100  20.95700  23.10600 1.000 18.02000 ? 15  ILE A CD1 1 
ATOM   105  N  N   . VAL A 1 22  ? 21.49900  16.24900  20.97900 1.000 17.55000 ? 16  VAL A N   1 
ATOM   106  C  CA  . VAL A 1 22  ? 21.08700  14.85600  21.23800 1.000 17.77000 ? 16  VAL A CA  1 
ATOM   107  C  C   . VAL A 1 22  ? 21.95900  14.23400  22.31900 1.000 15.81000 ? 16  VAL A C   1 
ATOM   108  O  O   . VAL A 1 22  ? 23.19700  14.28100  22.26200 1.000 15.03000 ? 16  VAL A O   1 
ATOM   109  C  CB  . VAL A 1 22  ? 21.14300  14.01000  19.95700 1.000 18.60000 ? 16  VAL A CB  1 
ATOM   110  C  CG1 . VAL A 1 22  ? 20.81600  12.54900  20.28900 1.000 17.67000 ? 16  VAL A CG1 1 
ATOM   111  C  CG2 . VAL A 1 22  ? 20.17100  14.55800  18.87900 1.000 22.94000 ? 16  VAL A CG2 1 
ATOM   112  N  N   . GLU A 1 23  ? 21.30600  13.70200  23.34000 1.000 16.51000 ? 17  GLU A N   1 
ATOM   113  C  CA  . GLU A 1 23  ? 21.98500  12.94300  24.38800 1.000 15.99000 ? 17  GLU A CA  1 
ATOM   114  C  C   . GLU A 1 23  ? 21.95600  11.46700  23.98600 1.000 17.14000 ? 17  GLU A C   1 
ATOM   115  O  O   . GLU A 1 23  ? 22.98100  10.90800  23.58400 1.000 14.82000 ? 17  GLU A O   1 
ATOM   116  C  CB  . GLU A 1 23  ? 21.30800  13.19400  25.74700 1.000 16.97000 ? 17  GLU A CB  1 
ATOM   117  C  CG  . GLU A 1 23  ? 22.00100  12.54700  26.92700 1.000 19.64000 ? 17  GLU A CG  1 
ATOM   118  C  CD  . GLU A 1 23  ? 22.96700  13.48100  27.65000 1.000 26.34000 ? 17  GLU A CD  1 
ATOM   119  O  OE1 . GLU A 1 23  ? 22.46200  14.39500  28.36700 1.000 23.01000 ? 17  GLU A OE1 1 
ATOM   120  O  OE2 . GLU A 1 23  ? 24.21900  13.30900  27.49500 1.000 20.55000 ? 17  GLU A OE2 1 
ATOM   121  N  N   . ASN A 1 24  ? 20.78300  10.82600  24.10000 1.000 16.97000 ? 18  ASN A N   1 
ATOM   122  C  CA  . ASN A 1 24  ? 20.59300  9.39500   23.83400 1.000 16.98000 ? 18  ASN A CA  1 
ATOM   123  C  C   . ASN A 1 24  ? 19.45800  9.21100   22.84300 1.000 16.41000 ? 18  ASN A C   1 
ATOM   124  O  O   . ASN A 1 24  ? 18.53100  10.01500  22.77400 1.000 14.99000 ? 18  ASN A O   1 
ATOM   125  C  CB  . ASN A 1 24  ? 20.19700  8.58300   25.08000 1.000 15.84000 ? 18  ASN A CB  1 
ATOM   126  C  CG  . ASN A 1 24  ? 21.20400  8.70600   26.21700 1.000 18.38000 ? 18  ASN A CG  1 
ATOM   127  O  OD1 . ASN A 1 24  ? 22.40400  8.67600   26.00600 1.000 16.82000 ? 18  ASN A OD1 1 
ATOM   128  N  ND2 . ASN A 1 24  ? 20.69600  8.81500   27.44100 1.000 19.02000 ? 18  ASN A ND2 1 
ATOM   129  N  N   . SER A 1 25  ? 19.47200  8.10100   22.12400 1.000 14.71000 ? 19  SER A N   1 
ATOM   130  C  CA  . SER A 1 25  ? 18.30300  7.76900   21.32800 1.000 14.45000 ? 19  SER A CA  1 
ATOM   131  C  C   . SER A 1 25  ? 18.02300  6.27700   21.47800 1.000 16.06000 ? 19  SER A C   1 
ATOM   132  O  O   . SER A 1 25  ? 18.95800  5.48400   21.66400 1.000 16.39000 ? 19  SER A O   1 
ATOM   133  C  CB  . SER A 1 25  ? 18.51100  8.17000   19.86600 1.000 18.07000 ? 19  SER A CB  1 
ATOM   134  O  OG  . SER A 1 25  ? 19.47700  7.32600   19.27100 1.000 21.72000 ? 19  SER A OG  1 
ATOM   135  N  N   . HIS A 1 26  ? 16.73700  5.91800   21.40300 1.000 14.65000 ? 20  HIS A N   1 
ATOM   136  C  CA  . HIS A 1 26  ? 16.22600  4.58600   21.72300 1.000 16.56000 ? 20  HIS A CA  1 
ATOM   137  C  C   . HIS A 1 26  ? 15.29000  4.13100   20.60900 1.000 16.48000 ? 20  HIS A C   1 
ATOM   138  O  O   . HIS A 1 26  ? 14.32500  4.82800   20.29200 1.000 17.39000 ? 20  HIS A O   1 
ATOM   139  C  CB  . HIS A 1 26  ? 15.47700  4.59900   23.06700 1.000 14.71000 ? 20  HIS A CB  1 
ATOM   140  C  CG  . HIS A 1 26  ? 16.24800  5.24800   24.17900 1.000 14.20000 ? 20  HIS A CG  1 
ATOM   141  N  ND1 . HIS A 1 26  ? 16.89900  4.51900   25.15100 1.000 14.85000 ? 20  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A 1 26  ? 16.46800  6.56000   24.47900 1.000 18.07000 ? 20  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A 1 26  ? 17.50300  5.35300   25.99200 1.000 20.11000 ? 20  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A 1 26  ? 17.25500  6.59700   25.60800 1.000 16.74000 ? 20  HIS A NE2 1 
ATOM   145  N  N   . ARG A 1 27  ? 15.57000  2.97100   20.01800 1.000 17.11000 ? 21  ARG A N   1 
ATOM   146  C  CA  . ARG A 1 27  ? 14.73100  2.46300   18.94400 1.000 16.97000 ? 21  ARG A CA  1 
ATOM   147  C  C   . ARG A 1 27  ? 13.45200  1.86600   19.52300 1.000 16.24000 ? 21  ARG A C   1 
ATOM   148  O  O   . ARG A 1 27  ? 13.50400  1.12000   20.50400 1.000 16.72000 ? 21  ARG A O   1 
ATOM   149  C  CB  . ARG A 1 27  ? 15.52300  1.43400   18.12800 1.000 20.61000 ? 21  ARG A CB  1 
ATOM   150  C  CG  . ARG A 1 27  ? 14.77000  0.90000   16.96300 1.000 24.03000 ? 21  ARG A CG  1 
ATOM   151  C  CD  . ARG A 1 27  ? 15.47200  -0.26800  16.27500 1.000 32.59000 ? 21  ARG A CD  1 
ATOM   152  N  NE  . ARG A 1 27  ? 16.60200  0.17700   15.46500 1.000 46.25000 ? 21  ARG A NE  1 
ATOM   153  C  CZ  . ARG A 1 27  ? 16.49200  0.86500   14.33100 1.000 48.53000 ? 21  ARG A CZ  1 
ATOM   154  N  NH1 . ARG A 1 27  ? 15.30400  1.21500   13.84300 1.000 42.63000 ? 21  ARG A NH1 1 
ATOM   155  N  NH2 . ARG A 1 27  ? 17.60000  1.21700   13.67200 1.000 42.81000 ? 21  ARG A NH2 1 
ATOM   156  N  N   . VAL A 1 28  ? 12.30100  2.21600   18.94300 1.000 15.57000 ? 22  VAL A N   1 
ATOM   157  C  CA  . VAL A 1 28  ? 10.98500  1.78700   19.42700 1.000 13.85000 ? 22  VAL A CA  1 
ATOM   158  C  C   . VAL A 1 28  ? 10.41100  0.80100   18.41900 1.000 18.06000 ? 22  VAL A C   1 
ATOM   159  O  O   . VAL A 1 28  ? 10.46800  1.04600   17.20400 1.000 19.15000 ? 22  VAL A O   1 
ATOM   160  C  CB  . VAL A 1 28  ? 9.99700   2.96200   19.60400 1.000 16.66000 ? 22  VAL A CB  1 
ATOM   161  C  CG1 . VAL A 1 28  ? 8.67700   2.43200   20.20600 1.000 18.47000 ? 22  VAL A CG1 1 
ATOM   162  C  CG2 . VAL A 1 28  ? 10.57200  4.07400   20.44300 1.000 20.83000 ? 22  VAL A CG2 1 
ATOM   163  N  N   . HIS A 1 29  ? 9.85400   -0.30400  18.92000 1.000 16.88000 ? 23  HIS A N   1 
ATOM   164  C  CA  . HIS A 1 29  ? 9.00800   -1.21600  18.16600 1.000 15.69000 ? 23  HIS A CA  1 
ATOM   165  C  C   . HIS A 1 29  ? 7.63500   -1.23100  18.81200 1.000 16.19000 ? 23  HIS A C   1 
ATOM   166  O  O   . HIS A 1 29  ? 7.52700   -1.26800  20.04900 1.000 16.46000 ? 23  HIS A O   1 
ATOM   167  C  CB  . HIS A 1 29  ? 9.58900   -2.61500  18.17900 1.000 17.03000 ? 23  HIS A CB  1 
ATOM   168  C  CG  . HIS A 1 29  ? 11.00900  -2.66100  17.73900 1.000 19.18000 ? 23  HIS A CG  1 
ATOM   169  N  ND1 . HIS A 1 29  ? 11.36500  -2.72100  16.40600 1.000 22.13000 ? 23  HIS A ND1 1 
ATOM   170  C  CD2 . HIS A 1 29  ? 12.17300  -2.68300  18.44400 1.000 18.56000 ? 23  HIS A CD2 1 
ATOM   171  C  CE1 . HIS A 1 29  ? 12.68400  -2.75400  16.31000 1.000 24.98000 ? 23  HIS A CE1 1 
ATOM   172  N  NE2 . HIS A 1 29  ? 13.19800  -2.72600  17.53100 1.000 18.84000 ? 23  HIS A NE2 1 
ATOM   173  N  N   . ALA A 1 30  ? 6.58500   -1.16300  17.99900 1.000 16.61000 ? 24  ALA A N   1 
ATOM   174  C  CA  . ALA A 1 30  ? 5.23000   -1.15900  18.54000 1.000 16.49000 ? 24  ALA A CA  1 
ATOM   175  C  C   . ALA A 1 30  ? 4.31600   -1.83500  17.53900 1.000 18.67000 ? 24  ALA A C   1 
ATOM   176  O  O   . ALA A 1 30  ? 4.54100   -1.73900  16.33400 1.000 20.83000 ? 24  ALA A O   1 
ATOM   177  C  CB  . ALA A 1 30  ? 4.74800   0.27100   18.86500 1.000 16.84000 ? 24  ALA A CB  1 
ATOM   178  N  N   . ALA A 1 31  ? 3.29700   -2.55000  18.05100 1.000 15.05000 ? 25  ALA A N   1 
ATOM   179  C  CA  . ALA A 1 31  ? 2.25400   -3.17400  17.25700 1.000 16.01000 ? 25  ALA A CA  1 
ATOM   180  C  C   . ALA A 1 31  ? 0.92300   -2.76800  17.86800 1.000 18.30000 ? 25  ALA A C   1 
ATOM   181  O  O   . ALA A 1 31  ? 0.78500   -2.77400  19.09500 1.000 20.07000 ? 25  ALA A O   1 
ATOM   182  C  CB  . ALA A 1 31  ? 2.38200   -4.72100  17.23100 1.000 17.21000 ? 25  ALA A CB  1 
ATOM   183  N  N   . VAL A 1 32  ? -0.01700  -2.35600  17.03000 1.000 19.42000 ? 26  VAL A N   1 
ATOM   184  C  CA  . VAL A 1 32  ? -1.40800  -2.13100  17.42800 1.000 21.42000 ? 26  VAL A CA  1 
ATOM   185  C  C   . VAL A 1 32  ? -2.26100  -3.07100  16.59100 1.000 24.18000 ? 26  VAL A C   1 
ATOM   186  O  O   . VAL A 1 32  ? -2.26800  -2.96600  15.35100 1.000 24.49000 ? 26  VAL A O   1 
ATOM   187  C  CB  . VAL A 1 32  ? -1.85800  -0.67100  17.22100 1.000 21.93000 ? 26  VAL A CB  1 
ATOM   188  C  CG1 . VAL A 1 32  ? -3.31100  -0.49400  17.65300 1.000 19.98000 ? 26  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A 1 32  ? -0.97600  0.31300   17.97200 1.000 19.71000 ? 26  VAL A CG2 1 
ATOM   190  N  N   . VAL A 1 33  ? -3.00300  -3.97400  17.24700 1.000 21.70000 ? 27  VAL A N   1 
ATOM   191  C  CA  . VAL A 1 33  ? -3.68800  -5.03200  16.51300 1.000 22.10000 ? 27  VAL A CA  1 
ATOM   192  C  C   . VAL A 1 33  ? -5.15500  -5.08400  16.92500 1.000 27.50000 ? 27  VAL A C   1 
ATOM   193  O  O   . VAL A 1 33  ? -5.55400  -4.62800  18.00900 1.000 22.83000 ? 27  VAL A O   1 
ATOM   194  C  CB  . VAL A 1 33  ? -3.03100  -6.41500  16.71900 1.000 24.60000 ? 27  VAL A CB  1 
ATOM   195  C  CG1 . VAL A 1 33  ? -1.53400  -6.34500  16.41300 1.000 24.30000 ? 27  VAL A CG1 1 
ATOM   196  C  CG2 . VAL A 1 33  ? -3.25000  -6.91500  18.14100 1.000 20.71000 ? 27  VAL A CG2 1 
ATOM   197  N  N   . ASP A 1 34  ? -5.96700  -5.64500  16.03600 1.000 27.32000 ? 28  ASP A N   1 
ATOM   198  C  CA  . ASP A 1 34  ? -7.36900  -5.83200  16.37100 1.000 29.76000 ? 28  ASP A CA  1 
ATOM   199  C  C   . ASP A 1 34  ? -7.55100  -7.19000  17.05900 1.000 26.56000 ? 28  ASP A C   1 
ATOM   200  O  O   . ASP A 1 34  ? -6.58900  -7.92700  17.28300 1.000 27.62000 ? 28  ASP A O   1 
ATOM   201  C  CB  . ASP A 1 34  ? -8.23900  -5.63100  15.12000 1.000 28.65000 ? 28  ASP A CB  1 
ATOM   202  C  CG  . ASP A 1 34  ? -8.19600  -6.80800  14.12400 1.000 33.42000 ? 28  ASP A CG  1 
ATOM   203  O  OD1 . ASP A 1 34  ? -7.61800  -7.89000  14.38200 1.000 34.46000 ? 28  ASP A OD1 1 
ATOM   204  O  OD2 . ASP A 1 34  ? -8.78000  -6.63200  13.03400 1.000 33.89000 ? 28  ASP A OD2 1 
ATOM   205  N  N   . ALA A 1 35  ? -8.81100  -7.52500  17.38200 1.000 30.98000 ? 29  ALA A N   1 
ATOM   206  C  CA  . ALA A 1 35  ? -9.12800  -8.68900  18.21400 1.000 28.24000 ? 29  ALA A CA  1 
ATOM   207  C  C   . ALA A 1 35  ? -8.72900  -10.02100 17.56700 1.000 31.81000 ? 29  ALA A C   1 
ATOM   208  O  O   . ALA A 1 35  ? -8.54100  -11.02300 18.27400 1.000 31.88000 ? 29  ALA A O   1 
ATOM   209  C  CB  . ALA A 1 35  ? -10.62500 -8.69200  18.53600 1.000 26.72000 ? 29  ALA A CB  1 
ATOM   210  N  N   . LYS A 1 36  ? -8.64000  -10.08200 16.24100 1.000 27.25000 ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 36  ? -8.10200  -11.27100 15.59900 1.000 29.27000 ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 36  ? -6.58700  -11.19900 15.42600 1.000 32.33000 ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 36  ? -5.97800  -12.19600 15.02400 1.000 31.69000 ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 36  ? -8.77200  -11.49600 14.24300 1.000 32.09000 ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 36  ? -10.31800 -11.33300 14.27900 1.000 39.72000 ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 36  ? -11.05200 -12.57900 13.84500 1.000 42.75000 ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 36  ? -12.54200 -12.52700 14.21400 1.000 42.29000 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 36  ? -13.37400 -11.74600 13.23000 1.000 56.29000 ? 30  LYS A NZ  1 
ATOM   219  N  N   . GLY A 1 37  ? -5.96700  -10.06000 15.73800 1.000 28.79000 ? 31  GLY A N   1 
ATOM   220  C  CA  . GLY A 1 37  ? -4.53900  -9.91000  15.59900 1.000 28.54000 ? 31  GLY A CA  1 
ATOM   221  C  C   . GLY A 1 37  ? -4.07200  -9.26500  14.31800 1.000 25.92000 ? 31  GLY A C   1 
ATOM   222  O  O   . GLY A 1 37  ? -2.86300  -9.23500  14.07200 1.000 25.76000 ? 31  GLY A O   1 
ATOM   223  N  N   . ARG A 1 38  ? -4.97100  -8.72000  13.51200 1.000 27.75000 ? 32  ARG A N   1 
ATOM   224  C  CA  . ARG A 1 38  ? -4.54000  -8.03300  12.30800 1.000 28.81000 ? 32  ARG A CA  1 
ATOM   225  C  C   . ARG A 1 38  ? -3.84500  -6.74400  12.67700 1.000 24.72000 ? 32  ARG A C   1 
ATOM   226  O  O   . ARG A 1 38  ? -4.26900  -6.02400  13.58600 1.000 27.57000 ? 32  ARG A O   1 
ATOM   227  C  CB  . ARG A 1 38  ? -5.72800  -7.74900  11.40400 1.000 29.02000 ? 32  ARG A CB  1 
ATOM   228  C  CG  . ARG A 1 38  ? -6.60900  -8.94500  11.37200 1.000 40.47000 ? 32  ARG A CG  1 
ATOM   229  C  CD  . ARG A 1 38  ? -7.20900  -9.25600  9.99400  1.000 51.22000 ? 32  ARG A CD  1 
ATOM   230  N  NE  . ARG A 1 38  ? -8.40200  -8.47000  9.67900  1.000 55.45000 ? 32  ARG A NE  1 
ATOM   231  C  CZ  . ARG A 1 38  ? -9.56200  -8.53500  10.32500 1.000 54.70000 ? 32  ARG A CZ  1 
ATOM   232  N  NH1 . ARG A 1 38  ? -9.70400  -9.25300  11.43100 1.000 54.49000 ? 32  ARG A NH1 1 
ATOM   233  N  NH2 . ARG A 1 38  ? -10.60700 -7.85500  9.85400  1.000 55.62000 ? 32  ARG A NH2 1 
ATOM   234  N  N   . LEU A 1 39  ? -2.77400  -6.44300  11.96100 1.000 24.64000 ? 33  LEU A N   1 
ATOM   235  C  CA  . LEU A 1 39  ? -1.95400  -5.28400  12.28900 1.000 25.30000 ? 33  LEU A CA  1 
ATOM   236  C  C   . LEU A 1 39  ? -2.63800  -4.00900  11.81000 1.000 28.45000 ? 33  LEU A C   1 
ATOM   237  O  O   . LEU A 1 39  ? -2.93200  -3.87500  10.61700 1.000 26.16000 ? 33  LEU A O   1 
ATOM   238  C  CB  . LEU A 1 39  ? -0.57900  -5.42800  11.64200 1.000 21.53000 ? 33  LEU A CB  1 
ATOM   239  C  CG  . LEU A 1 39  ? 0.41700   -4.38100  12.08000 1.000 25.23000 ? 33  LEU A CG  1 
ATOM   240  C  CD1 . LEU A 1 39  ? 0.79200   -4.66900  13.55100 1.000 22.60000 ? 33  LEU A CD1 1 
ATOM   241  C  CD2 . LEU A 1 39  ? 1.64000   -4.43500  11.14900 1.000 29.98000 ? 33  LEU A CD2 1 
ATOM   242  N  N   . LEU A 1 40  ? -2.88200  -3.06800  12.72500 1.000 24.02000 ? 34  LEU A N   1 
ATOM   243  C  CA  . LEU A 1 40  ? -3.52300  -1.81100  12.35900 1.000 24.25000 ? 34  LEU A CA  1 
ATOM   244  C  C   . LEU A 1 40  ? -2.54900  -0.64400  12.26900 1.000 27.05000 ? 34  LEU A C   1 
ATOM   245  O  O   . LEU A 1 40  ? -2.67000  0.17200   11.35000 1.000 24.40000 ? 34  LEU A O   1 
ATOM   246  C  CB  . LEU A 1 40  ? -4.64300  -1.47100  13.35000 1.000 26.73000 ? 34  LEU A CB  1 
ATOM   247  C  CG  . LEU A 1 40  ? -5.71200  -2.57600  13.42400 1.000 27.65000 ? 34  LEU A CG  1 
ATOM   248  C  CD1 . LEU A 1 40  ? -6.66700  -2.28300  14.53900 1.000 30.24000 ? 34  LEU A CD1 1 
ATOM   249  C  CD2 . LEU A 1 40  ? -6.50100  -2.71100  12.14200 1.000 27.69000 ? 34  LEU A CD2 1 
ATOM   250  N  N   . TYR A 1 41  ? -1.59000  -0.54200  13.19400 1.000 22.27000 ? 35  TYR A N   1 
ATOM   251  C  CA  . TYR A 1 41  ? -0.52600  0.46500   13.14700 1.000 27.84000 ? 35  TYR A CA  1 
ATOM   252  C  C   . TYR A 1 41  ? 0.75500   -0.13700  13.71700 1.000 22.25000 ? 35  TYR A C   1 
ATOM   253  O  O   . TYR A 1 41  ? 0.72000   -1.07000  14.52800 1.000 20.39000 ? 35  TYR A O   1 
ATOM   254  C  CB  . TYR A 1 41  ? -0.87000  1.76500   13.93100 1.000 22.90000 ? 35  TYR A CB  1 
ATOM   255  C  CG  . TYR A 1 41  ? -2.17500  2.37300   13.54000 1.000 26.03000 ? 35  TYR A CG  1 
ATOM   256  C  CD1 . TYR A 1 41  ? -2.25400  3.27900   12.50800 1.000 28.46000 ? 35  TYR A CD1 1 
ATOM   257  C  CD2 . TYR A 1 41  ? -3.33800  2.00000   14.18100 1.000 28.48000 ? 35  TYR A CD2 1 
ATOM   258  C  CE1 . TYR A 1 41  ? -3.47900  3.80000   12.12900 1.000 31.55000 ? 35  TYR A CE1 1 
ATOM   259  C  CE2 . TYR A 1 41  ? -4.56500  2.51200   13.80900 1.000 28.12000 ? 35  TYR A CE2 1 
ATOM   260  C  CZ  . TYR A 1 41  ? -4.62500  3.41700   12.79100 1.000 30.80000 ? 35  TYR A CZ  1 
ATOM   261  O  OH  . TYR A 1 41  ? -5.85700  3.90700   12.41700 1.000 34.78000 ? 35  TYR A OH  1 
ATOM   262  N  N   . ALA A 1 42  ? 1.89700   0.43600   13.32500 1.000 21.41000 ? 36  ALA A N   1 
ATOM   263  C  CA  . ALA A 1 42  ? 3.17900   -0.09100  13.77700 1.000 18.54000 ? 36  ALA A CA  1 
ATOM   264  C  C   . ALA A 1 42  ? 4.19800   1.02100   13.89600 1.000 22.67000 ? 36  ALA A C   1 
ATOM   265  O  O   . ALA A 1 42  ? 4.10700   2.03500   13.20000 1.000 24.40000 ? 36  ALA A O   1 
ATOM   266  C  CB  . ALA A 1 42  ? 3.72100   -1.14500  12.80700 1.000 24.21000 ? 36  ALA A CB  1 
ATOM   267  N  N   . LEU A 1 43  ? 5.15700   0.82600   14.79900 1.000 20.91000 ? 37  LEU A N   1 
ATOM   268  C  CA  . LEU A 1 43  ? 6.46700   1.48300   14.81100 1.000 20.71000 ? 37  LEU A CA  1 
ATOM   269  C  C   . LEU A 1 43  ? 7.54000   0.40900   14.72000 1.000 23.76000 ? 37  LEU A C   1 
ATOM   270  O  O   . LEU A 1 43  ? 7.35600   -0.70900  15.23100 1.000 18.95000 ? 37  LEU A O   1 
ATOM   271  C  CB  . LEU A 1 43  ? 6.71900   2.28900   16.10300 1.000 19.28000 ? 37  LEU A CB  1 
ATOM   272  C  CG  . LEU A 1 43  ? 5.74500   3.40700   16.42200 1.000 24.49000 ? 37  LEU A CG  1 
ATOM   273  C  CD1 . LEU A 1 43  ? 5.92700   3.95800   17.85300 1.000 22.20000 ? 37  LEU A CD1 1 
ATOM   274  C  CD2 . LEU A 1 43  ? 5.84200   4.50600   15.33800 1.000 23.52000 ? 37  LEU A CD2 1 
ATOM   275  N  N   . GLY A 1 44  ? 8.67000   0.73800   14.07800 1.000 20.58000 ? 38  GLY A N   1 
ATOM   276  C  CA  . GLY A 1 44  ? 9.79800   -0.17100  14.13000 1.000 19.90000 ? 38  GLY A CA  1 
ATOM   277  C  C   . GLY A 1 44  ? 9.43900   -1.46900  13.44100 1.000 23.25000 ? 38  GLY A C   1 
ATOM   278  O  O   . GLY A 1 44  ? 8.79900   -1.48200  12.38200 1.000 24.68000 ? 38  GLY A O   1 
ATOM   279  N  N   . ASN A 1 45  ? 9.87100   -2.58400  14.03200 1.000 20.66000 ? 39  ASN A N   1 
ATOM   280  C  CA  . ASN A 1 45  ? 9.53900   -3.91300  13.52500 1.000 20.76000 ? 39  ASN A CA  1 
ATOM   281  C  C   . ASN A 1 45  ? 8.42600   -4.50000  14.38600 1.000 19.69000 ? 39  ASN A C   1 
ATOM   282  O  O   . ASN A 1 45  ? 8.70700   -5.06200  15.45900 1.000 20.67000 ? 39  ASN A O   1 
ATOM   283  C  CB  . ASN A 1 45  ? 10.77600  -4.82400  13.54400 1.000 21.78000 ? 39  ASN A CB  1 
ATOM   284  C  CG  . ASN A 1 45  ? 10.47800  -6.19800  13.01100 1.000 23.59000 ? 39  ASN A CG  1 
ATOM   285  O  OD1 . ASN A 1 45  ? 9.37600   -6.42000  12.51200 1.000 23.98000 ? 39  ASN A OD1 1 
ATOM   286  N  ND2 . ASN A 1 45  ? 11.44500  -7.13500  13.11000 1.000 20.52000 ? 39  ASN A ND2 1 
ATOM   287  N  N   . PRO A 1 46  ? 7.16000   -4.42900  13.96700 1.000 22.17000 ? 40  PRO A N   1 
ATOM   288  C  CA  . PRO A 1 46  ? 6.07800   -4.93200  14.83200 1.000 20.68000 ? 40  PRO A CA  1 
ATOM   289  C  C   . PRO A 1 46  ? 6.07200   -6.44400  14.99100 1.000 21.02000 ? 40  PRO A C   1 
ATOM   290  O  O   . PRO A 1 46  ? 5.26600   -6.94500  15.78600 1.000 20.60000 ? 40  PRO A O   1 
ATOM   291  C  CB  . PRO A 1 46  ? 4.81100   -4.45500  14.10900 1.000 22.07000 ? 40  PRO A CB  1 
ATOM   292  C  CG  . PRO A 1 46  ? 5.23400   -4.39700  12.69000 1.000 22.02000 ? 40  PRO A CG  1 
ATOM   293  C  CD  . PRO A 1 46  ? 6.64200   -3.92100  12.68500 1.000 20.36000 ? 40  PRO A CD  1 
ATOM   294  N  N   . THR A 1 47  ? 6.88000   -7.19600  14.23200 1.000 17.15000 ? 41  THR A N   1 
ATOM   295  C  CA  . THR A 1 47  ? 6.96800   -8.64600  14.41400 1.000 18.50000 ? 41  THR A CA  1 
ATOM   296  C  C   . THR A 1 47  ? 8.28700   -9.06400  15.06000 1.000 19.34000 ? 41  THR A C   1 
ATOM   297  O  O   . THR A 1 47  ? 8.63000   -10.25300 15.01700 1.000 19.91000 ? 41  THR A O   1 
ATOM   298  C  CB  . THR A 1 47  ? 6.77200   -9.40300  13.09000 1.000 21.75000 ? 41  THR A CB  1 
ATOM   299  O  OG1 . THR A 1 47  ? 7.85300   -9.11300  12.18500 1.000 24.95000 ? 41  THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 47  ? 5.44300   -9.02600  12.42000 1.000 18.59000 ? 41  THR A CG2 1 
ATOM   301  N  N   . ARG A 1 48  ? 9.00300   -8.11800  15.69700 1.000 17.88000 ? 42  ARG A N   1 
ATOM   302  C  CA  . ARG A 1 48  ? 10.26900  -8.40700  16.34700 1.000 18.54000 ? 42  ARG A CA  1 
ATOM   303  C  C   . ARG A 1 48  ? 10.11900  -9.56300  17.31400 1.000 20.52000 ? 42  ARG A C   1 
ATOM   304  O  O   . ARG A 1 48  ? 9.25000   -9.53000  18.19600 1.000 19.35000 ? 42  ARG A O   1 
ATOM   305  C  CB  . ARG A 1 48  ? 10.76400  -7.16900  17.11800 1.000 19.02000 ? 42  ARG A CB  1 
ATOM   306  C  CG  . ARG A 1 48  ? 12.17800  -7.33900  17.84000 1.000 17.95000 ? 42  ARG A CG  1 
ATOM   307  C  CD  . ARG A 1 48  ? 12.36000  -6.28500  18.92600 1.000 21.24000 ? 42  ARG A CD  1 
ATOM   308  N  NE  . ARG A 1 48  ? 13.66400  -6.27600  19.60000 1.000 19.92000 ? 42  ARG A NE  1 
ATOM   309  C  CZ  . ARG A 1 48  ? 13.96800  -6.97700  20.69000 1.000 20.13000 ? 42  ARG A CZ  1 
ATOM   310  N  NH1 . ARG A 1 48  ? 13.08100  -7.79500  21.27300 1.000 15.51000 ? 42  ARG A NH1 1 
ATOM   311  N  NH2 . ARG A 1 48  ? 15.19500  -6.87000  21.20500 1.000 17.14000 ? 42  ARG A NH2 1 
ATOM   312  N  N   . MET A 1 49  ? 11.01200  -10.54900 17.20400 1.000 16.24000 ? 43  MET A N   1 
ATOM   313  C  CA  . MET A 1 49  ? 10.99900  -11.64900 18.16200 1.000 19.19000 ? 43  MET A CA  1 
ATOM   314  C  C   . MET A 1 49  ? 11.36600  -11.08500 19.52900 1.000 20.26000 ? 43  MET A C   1 
ATOM   315  O  O   . MET A 1 49  ? 12.44400  -10.51900 19.68500 1.000 18.75000 ? 43  MET A O   1 
ATOM   316  C  CB  . MET A 1 49  ? 11.99000  -12.73000 17.73700 1.000 20.79000 ? 43  MET A CB  1 
ATOM   317  C  CG  . MET A 1 49  ? 12.04200  -13.94700 18.67800 1.000 27.15000 ? 43  MET A CG  1 
ATOM   318  S  SD  . MET A 1 49  ? 10.55200  -14.95600 18.54600 1.000 32.57000 ? 43  MET A SD  1 
ATOM   319  C  CE  . MET A 1 49  ? 10.36900  -15.09200 16.76700 1.000 31.82000 ? 43  MET A CE  1 
ATOM   320  N  N   . THR A 1 50  ? 10.48400  -11.22200 20.51300 1.000 16.09000 ? 44  THR A N   1 
ATOM   321  C  CA  . THR A 1 50  ? 10.63700  -10.47300 21.75600 1.000 18.27000 ? 44  THR A CA  1 
ATOM   322  C  C   . THR A 1 50  ? 10.31800  -11.34200 22.95800 1.000 19.24000 ? 44  THR A C   1 
ATOM   323  O  O   . THR A 1 50  ? 9.23400   -11.92100 23.04100 1.000 17.43000 ? 44  THR A O   1 
ATOM   324  C  CB  . THR A 1 50  ? 9.73300   -9.22000  21.78500 1.000 17.78000 ? 44  THR A CB  1 
ATOM   325  O  OG1 . THR A 1 50  ? 10.12100  -8.34700  20.72500 1.000 15.32000 ? 44  THR A OG1 1 
ATOM   326  C  CG2 . THR A 1 50  ? 9.90500   -8.42400  23.10400 1.000 17.60000 ? 44  THR A CG2 1 
ATOM   327  N  N   . LEU A 1 51  ? 11.23600  -11.37300 23.91400 1.000 16.89000 ? 45  LEU A N   1 
ATOM   328  C  CA  . LEU A 1 51  ? 10.93400  -11.94400 25.22300 1.000 16.51000 ? 45  LEU A CA  1 
ATOM   329  C  C   . LEU A 1 51  ? 9.87800   -11.10600 25.93400 1.000 18.71000 ? 45  LEU A C   1 
ATOM   330  O  O   . LEU A 1 51  ? 10.12000  -9.93200  26.24600 1.000 17.59000 ? 45  LEU A O   1 
ATOM   331  C  CB  . LEU A 1 51  ? 12.21700  -11.99800 26.05900 1.000 15.40000 ? 45  LEU A CB  1 
ATOM   332  C  CG  . LEU A 1 51  ? 13.26900  -13.01300 25.60100 1.000 18.29000 ? 45  LEU A CG  1 
ATOM   333  C  CD1 . LEU A 1 51  ? 14.68100  -12.52900 25.94600 1.000 15.89000 ? 45  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A 1 51  ? 12.98000  -14.37500 26.22400 1.000 16.52000 ? 45  LEU A CD2 1 
ATOM   335  N  N   . ALA A 1 52  ? 8.70400   -11.71000 26.21500 1.000 16.58000 ? 46  ALA A N   1 
ATOM   336  C  CA  . ALA A 1 52  ? 7.60200   -10.97600 26.81700 1.000 18.02000 ? 46  ALA A CA  1 
ATOM   337  C  C   . ALA A 1 52  ? 7.78900   -10.78300 28.31100 1.000 21.37000 ? 46  ALA A C   1 
ATOM   338  O  O   . ALA A 1 52  ? 7.19600   -9.85400  28.87500 1.000 19.75000 ? 46  ALA A O   1 
ATOM   339  C  CB  . ALA A 1 52  ? 6.27100   -11.70600 26.56700 1.000 15.87000 ? 46  ALA A CB  1 
ATOM   340  N  N   . ARG A 1 53  ? 8.57600   -11.65300 28.95600 1.000 19.79000 ? 47  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 53  ? 8.86800   -11.53600 30.37200 1.000 20.44000 ? 47  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 53  ? 7.53300   -11.44300 31.10800 1.000 20.84000 ? 47  ARG A C   1 
ATOM   343  O  O   . ARG A 1 53  ? 6.59900   -12.16900 30.75200 1.000 19.11000 ? 47  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 53  ? 9.80400   -10.34600 30.61900 1.000 21.76000 ? 47  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 53  ? 11.08800  -10.45400 29.77700 1.000 21.94000 ? 47  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 53  ? 11.97400  -11.64800 30.18700 1.000 16.57000 ? 47  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 53  ? 12.53800  -11.48200 31.53300 1.000 20.29000 ? 47  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 53  ? 13.47200  -10.60400 31.89300 1.000 22.68000 ? 47  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 53  ? 14.04700  -9.79000  31.01800 1.000 19.28000 ? 47  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 53  ? 13.82400  -10.51900 33.17600 1.000 23.15000 ? 47  ARG A NH2 1 
ATOM   351  N  N   . SER A 1 54  ? 7.39700   -10.57000 32.11000 1.000 20.03000 ? 48  SER A N   1 
ATOM   352  C  CA  . SER A 1 54  ? 6.12900   -10.56300 32.83600 1.000 21.16000 ? 48  SER A CA  1 
ATOM   353  C  C   . SER A 1 54  ? 4.95400   -10.00000 32.05900 1.000 25.84000 ? 48  SER A C   1 
ATOM   354  O  O   . SER A 1 54  ? 3.83400   -10.07900 32.57400 1.000 22.78000 ? 48  SER A O   1 
ATOM   355  C  CB  . SER A 1 54  ? 6.24500   -9.78800  34.13100 1.000 25.99000 ? 48  SER A CB  1 
ATOM   356  O  OG  . SER A 1 54  ? 6.97900   -10.55600 35.06500 1.000 34.25000 ? 48  SER A OG  1 
ATOM   357  N  N   . ALA A 1 55  ? 5.14700   -9.42600  30.86100 1.000 19.06000 ? 49  ALA A N   1 
ATOM   358  C  CA  . ALA A 1 55  ? 3.94600   -9.12300  30.09200 1.000 18.74000 ? 49  ALA A CA  1 
ATOM   359  C  C   . ALA A 1 55  ? 3.22700   -10.38800 29.65200 1.000 20.41000 ? 49  ALA A C   1 
ATOM   360  O  O   . ALA A 1 55  ? 2.05200   -10.31400 29.27100 1.000 19.86000 ? 49  ALA A O   1 
ATOM   361  C  CB  . ALA A 1 55  ? 4.27300   -8.25300  28.86800 1.000 18.18000 ? 49  ALA A CB  1 
ATOM   362  N  N   . ALA A 1 56  ? 3.87000   -11.55400 29.74800 1.000 21.41000 ? 50  ALA A N   1 
ATOM   363  C  CA  . ALA A 1 56  ? 3.18500   -12.82200 29.52600 1.000 24.48000 ? 50  ALA A CA  1 
ATOM   364  C  C   . ALA A 1 56  ? 2.51800   -13.39200 30.77500 1.000 24.32000 ? 50  ALA A C   1 
ATOM   365  O  O   . ALA A 1 56  ? 1.84600   -14.42200 30.66900 1.000 25.06000 ? 50  ALA A O   1 
ATOM   366  C  CB  . ALA A 1 56  ? 4.15000   -13.88400 28.95800 1.000 17.33000 ? 50  ALA A CB  1 
ATOM   367  N  N   . LYS A 1 57  ? 2.69400   -12.78800 31.95100 1.000 21.22000 ? 51  LYS A N   1 
ATOM   368  C  CA  . LYS A 1 57  ? 2.03700   -13.31300 33.15600 1.000 25.05000 ? 51  LYS A CA  1 
ATOM   369  C  C   . LYS A 1 57  ? 0.53500   -13.54100 33.01500 1.000 22.32000 ? 51  LYS A C   1 
ATOM   370  O  O   . LYS A 1 57  ? 0.06000   -14.59700 33.45200 1.000 27.01000 ? 51  LYS A O   1 
ATOM   371  C  CB  . LYS A 1 57  ? 2.31300   -12.38700 34.35300 1.000 27.07000 ? 51  LYS A CB  1 
ATOM   372  C  CG  . LYS A 1 57  ? 3.18400   -12.93400 35.43500 1.000 29.04000 ? 51  LYS A CG  1 
ATOM   373  C  CD  . LYS A 1 57  ? 4.39300   -13.62200 34.88400 1.000 31.20000 ? 51  LYS A CD  1 
ATOM   374  C  CE  . LYS A 1 57  ? 5.46600   -13.80100 35.96600 1.000 38.95000 ? 51  LYS A CE  1 
ATOM   375  N  NZ  . LYS A 1 57  ? 6.61000   -14.59200 35.41300 1.000 36.02000 ? 51  LYS A NZ  1 
ATOM   376  N  N   . PRO A 1 58  ? -0.26800  -12.63300 32.45500 1.000 23.69000 ? 52  PRO A N   1 
ATOM   377  C  CA  . PRO A 1 58  ? -1.70300  -12.93500 32.32500 1.000 21.43000 ? 52  PRO A CA  1 
ATOM   378  C  C   . PRO A 1 58  ? -1.99500  -14.17400 31.48900 1.000 23.29000 ? 52  PRO A C   1 
ATOM   379  O  O   . PRO A 1 58  ? -2.91700  -14.93400 31.81200 1.000 26.45000 ? 52  PRO A O   1 
ATOM   380  C  CB  . PRO A 1 58  ? -2.25800  -11.64900 31.68400 1.000 21.74000 ? 52  PRO A CB  1 
ATOM   381  C  CG  . PRO A 1 58  ? -1.30400  -10.57000 32.19300 1.000 23.90000 ? 52  PRO A CG  1 
ATOM   382  C  CD  . PRO A 1 58  ? 0.03200   -11.24900 32.04600 1.000 24.70000 ? 52  PRO A CD  1 
ATOM   383  N  N   . ALA A 1 59  ? -1.23100  -14.40600 30.42100 1.000 23.28000 ? 53  ALA A N   1 
ATOM   384  C  CA  . ALA A 1 59  ? -1.40800  -15.60300 29.59900 1.000 24.95000 ? 53  ALA A CA  1 
ATOM   385  C  C   . ALA A 1 59  ? -1.02100  -16.86300 30.36200 1.000 26.36000 ? 53  ALA A C   1 
ATOM   386  O  O   . ALA A 1 59  ? -1.69600  -17.90100 30.25600 1.000 26.42000 ? 53  ALA A O   1 
ATOM   387  C  CB  . ALA A 1 59  ? -0.57100  -15.49400 28.33000 1.000 21.37000 ? 53  ALA A CB  1 
ATOM   388  N  N   . GLN A 1 60  ? 0.07700   -16.79700 31.12200 1.000 24.29000 ? 54  GLN A N   1 
ATOM   389  C  CA  . GLN A 1 60  ? 0.47900   -17.92700 31.95000 1.000 24.92000 ? 54  GLN A CA  1 
ATOM   390  C  C   . GLN A 1 60  ? -0.53000  -18.16900 33.05300 1.000 26.21000 ? 54  GLN A C   1 
ATOM   391  O  O   . GLN A 1 60  ? -0.81000  -19.32800 33.39300 1.000 27.83000 ? 54  GLN A O   1 
ATOM   392  C  CB  . GLN A 1 60  ? 1.88300   -17.68500 32.52000 1.000 27.69000 ? 54  GLN A CB  1 
ATOM   393  C  CG  . GLN A 1 60  ? 2.96000   -17.55200 31.44300 1.000 25.81000 ? 54  GLN A CG  1 
ATOM   394  C  CD  . GLN A 1 60  ? 4.35700   -17.30600 31.98500 1.000 31.37000 ? 54  GLN A CD  1 
ATOM   395  O  OE1 . GLN A 1 60  ? 5.30000   -17.15700 31.21400 1.000 33.97000 ? 54  GLN A OE1 1 
ATOM   396  N  NE2 . GLN A 1 60  ? 4.49800   -17.25600 33.29600 1.000 32.78000 ? 54  GLN A NE2 1 
ATOM   397  N  N   . ALA A 1 61  ? -1.14600  -17.09900 33.56400 1.000 25.09000 ? 55  ALA A N   1 
ATOM   398  C  CA  . ALA A 1 61  ? -2.19500  -17.22600 34.57900 1.000 26.77000 ? 55  ALA A CA  1 
ATOM   399  C  C   . ALA A 1 61  ? -3.44700  -17.91800 34.05800 1.000 27.20000 ? 55  ALA A C   1 
ATOM   400  O  O   . ALA A 1 61  ? -4.19800  -18.51300 34.84900 1.000 25.88000 ? 55  ALA A O   1 
ATOM   401  C  CB  . ALA A 1 61  ? -2.57300  -15.85300 35.10700 1.000 24.99000 ? 55  ALA A CB  1 
ATOM   402  N  N   . LEU A 1 62  ? -3.72200  -17.82400 32.75100 1.000 27.64000 ? 56  LEU A N   1 
ATOM   403  C  CA  . LEU A 1 62  ? -4.86100  -18.54600 32.18900 1.000 28.21000 ? 56  LEU A CA  1 
ATOM   404  C  C   . LEU A 1 62  ? -4.66700  -20.05900 32.31900 1.000 29.12000 ? 56  LEU A C   1 
ATOM   405  O  O   . LEU A 1 62  ? -5.62800  -20.79300 32.57100 1.000 29.71000 ? 56  LEU A O   1 
ATOM   406  C  CB  . LEU A 1 62  ? -5.07500  -18.14300 30.72500 1.000 25.93000 ? 56  LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 62  ? -6.17600  -18.90400 29.96500 1.000 25.94000 ? 56  LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 62  ? -7.49000  -18.51900 30.54300 1.000 23.13000 ? 56  LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 62  ? -6.16700  -18.62000 28.47100 1.000 22.79000 ? 56  LEU A CD2 1 
ATOM   410  N  N   . ALA A 1 63  ? -3.42400  -20.54100 32.18700 1.000 26.07000 ? 57  ALA A N   1 
ATOM   411  C  CA  . ALA A 1 63  ? -3.15600  -21.95700 32.43200 1.000 24.80000 ? 57  ALA A CA  1 
ATOM   412  C  C   . ALA A 1 63  ? -3.51900  -22.35800 33.86500 1.000 28.82000 ? 57  ALA A C   1 
ATOM   413  O  O   . ALA A 1 63  ? -4.10600  -23.42100 34.10200 1.000 28.00000 ? 57  ALA A O   1 
ATOM   414  C  CB  . ALA A 1 63  ? -1.68200  -22.23900 32.15500 1.000 23.86000 ? 57  ALA A CB  1 
ATOM   415  N  N   . ILE A 1 64  ? -3.17400  -21.51900 34.83700 1.000 25.49000 ? 58  ILE A N   1 
ATOM   416  C  CA  . ILE A 1 64  ? -3.51100  -21.80700 36.22600 1.000 27.44000 ? 58  ILE A CA  1 
ATOM   417  C  C   . ILE A 1 64  ? -5.02300  -21.84300 36.41600 1.000 29.09000 ? 58  ILE A C   1 
ATOM   418  O  O   . ILE A 1 64  ? -5.57100  -22.77000 37.02600 1.000 28.23000 ? 58  ILE A O   1 
ATOM   419  C  CB  . ILE A 1 64  ? -2.85900  -20.75800 37.14800 1.000 25.56000 ? 58  ILE A CB  1 
ATOM   420  C  CG1 . ILE A 1 64  ? -1.33900  -20.82900 37.05900 1.000 24.62000 ? 58  ILE A CG1 1 
ATOM   421  C  CG2 . ILE A 1 64  ? -3.35300  -20.94900 38.57500 1.000 24.87000 ? 58  ILE A CG2 1 
ATOM   422  C  CD1 . ILE A 1 64  ? -0.64300  -19.55100 37.51000 1.000 22.51000 ? 58  ILE A CD1 1 
ATOM   423  N  N   . LEU A 1 65  ? -5.72700  -20.81800 35.91200 1.000 27.22000 ? 59  LEU A N   1 
ATOM   424  C  CA  . LEU A 1 65  ? -7.17400  -20.76300 36.09500 1.000 27.44000 ? 59  LEU A CA  1 
ATOM   425  C  C   . LEU A 1 65  ? -7.88200  -21.90400 35.37400 1.000 25.58000 ? 59  LEU A C   1 
ATOM   426  O  O   . LEU A 1 65  ? -8.94800  -22.35000 35.81400 1.000 29.40000 ? 59  LEU A O   1 
ATOM   427  C  CB  . LEU A 1 65  ? -7.72700  -19.42900 35.60400 1.000 22.05000 ? 59  LEU A CB  1 
ATOM   428  C  CG  . LEU A 1 65  ? -7.32200  -18.17800 36.40000 1.000 32.90000 ? 59  LEU A CG  1 
ATOM   429  C  CD1 . LEU A 1 65  ? -8.05500  -16.95700 35.87100 1.000 33.75000 ? 59  LEU A CD1 1 
ATOM   430  C  CD2 . LEU A 1 65  ? -7.61500  -18.37300 37.89000 1.000 33.75000 ? 59  LEU A CD2 1 
ATOM   431  N  N   . GLU A 1 66  ? -7.31900  -22.39100 34.27100 1.000 26.22000 ? 60  GLU A N   1 
ATOM   432  C  CA  . GLU A 1 66  ? -7.95500  -23.50700 33.57300 1.000 31.77000 ? 60  GLU A CA  1 
ATOM   433  C  C   . GLU A 1 66  ? -7.59700  -24.87100 34.16400 1.000 32.17000 ? 60  GLU A C   1 
ATOM   434  O  O   . GLU A 1 66  ? -8.09700  -25.89600 33.68000 1.000 33.69000 ? 60  GLU A O   1 
ATOM   435  C  CB  . GLU A 1 66  ? -7.58900  -23.45700 32.09000 1.000 35.00000 ? 60  GLU A CB  1 
ATOM   436  C  CG  . GLU A 1 66  ? -8.24300  -22.27300 31.35400 1.000 30.32000 ? 60  GLU A CG  1 
ATOM   437  C  CD  . GLU A 1 66  ? -7.93400  -22.28000 29.86800 1.000 35.11000 ? 60  GLU A CD  1 
ATOM   438  O  OE1 . GLU A 1 66  ? -6.82600  -22.74000 29.49700 1.000 37.00000 ? 60  GLU A OE1 1 
ATOM   439  O  OE2 . GLU A 1 66  ? -8.80600  -21.85000 29.07300 1.000 36.37000 ? 60  GLU A OE2 1 
ATOM   440  N  N   . THR A 1 67  ? -6.78300  -24.92200 35.21500 1.000 29.04000 ? 61  THR A N   1 
ATOM   441  C  CA  . THR A 1 67  ? -6.39700  -26.20300 35.78800 1.000 27.95000 ? 61  THR A CA  1 
ATOM   442  C  C   . THR A 1 67  ? -7.52000  -26.76300 36.64300 1.000 30.83000 ? 61  THR A C   1 
ATOM   443  O  O   . THR A 1 67  ? -8.11000  -26.04500 37.45600 1.000 30.27000 ? 61  THR A O   1 
ATOM   444  C  CB  . THR A 1 67  ? -5.11300  -26.04800 36.59300 1.000 28.83000 ? 61  THR A CB  1 
ATOM   445  O  OG1 . THR A 1 67  ? -4.05100  -25.75700 35.68300 1.000 27.92000 ? 61  THR A OG1 1 
ATOM   446  C  CG2 . THR A 1 67  ? -4.77800  -27.33400 37.31500 1.000 30.65000 ? 61  THR A CG2 1 
ATOM   447  N  N   . GLU A 1 68  ? -7.83800  -28.03700 36.42500 1.000 29.41000 ? 62  GLU A N   1 
ATOM   448  C  CA  . GLU A 1 68  ? -8.91900  -28.69900 37.14900 1.000 32.55000 ? 62  GLU A CA  1 
ATOM   449  C  C   . GLU A 1 68  ? -8.69400  -28.61500 38.65600 1.000 31.15000 ? 62  GLU A C   1 
ATOM   450  O  O   . GLU A 1 68  ? -7.62400  -28.96600 39.15500 1.000 38.30000 ? 62  GLU A O   1 
ATOM   451  C  CB  . GLU A 1 68  ? -9.00100  -30.16900 36.72300 1.000 31.41000 ? 62  GLU A CB  1 
ATOM   452  C  CG  . GLU A 1 68  ? -9.25300  -30.41100 35.22400 1.000 30.73000 ? 62  GLU A CG  1 
ATOM   453  C  CD  . GLU A 1 68  ? -8.01000  -30.39100 34.34400 1.000 29.25000 ? 62  GLU A CD  1 
ATOM   454  O  OE1 . GLU A 1 68  ? -6.95900  -29.83700 34.75600 1.000 31.26000 ? 62  GLU A OE1 1 
ATOM   455  O  OE2 . GLU A 1 68  ? -8.10900  -30.88500 33.19100 1.000 26.47000 ? 62  GLU A OE2 1 
ATOM   456  N  N   . GLY A 1 69  ? -9.70000  -28.15200 39.38800 1.000 32.33000 ? 63  GLY A N   1 
ATOM   457  C  CA  . GLY A 1 69  ? -9.61900  -28.08000 40.82800 1.000 33.27000 ? 63  GLY A CA  1 
ATOM   458  C  C   . GLY A 1 69  ? -9.13600  -26.76000 41.39900 1.000 33.47000 ? 63  GLY A C   1 
ATOM   459  O  O   . GLY A 1 69  ? -9.36900  -26.50000 42.58500 1.000 35.32000 ? 63  GLY A O   1 
ATOM   460  N  N   . VAL A 1 70  ? -8.48100  -25.91200 40.60200 1.000 28.66000 ? 64  VAL A N   1 
ATOM   461  C  CA  . VAL A 1 70  ? -7.98800  -24.64300 41.13300 1.000 30.95000 ? 64  VAL A CA  1 
ATOM   462  C  C   . VAL A 1 70  ? -9.13500  -23.78400 41.67200 1.000 36.45000 ? 64  VAL A C   1 
ATOM   463  O  O   . VAL A 1 70  ? -8.96700  -23.05500 42.65800 1.000 35.35000 ? 64  VAL A O   1 
ATOM   464  C  CB  . VAL A 1 70  ? -7.15400  -23.90500 40.05700 1.000 32.90000 ? 64  VAL A CB  1 
ATOM   465  C  CG1 . VAL A 1 70  ? -6.97500  -22.43700 40.39400 1.000 31.79000 ? 64  VAL A CG1 1 
ATOM   466  C  CG2 . VAL A 1 70  ? -5.76800  -24.53800 39.92100 1.000 30.83000 ? 64  VAL A CG2 1 
ATOM   467  N  N   . ALA A 1 71  ? -10.32400 -23.87500 41.07300 1.000 35.61000 ? 65  ALA A N   1 
ATOM   468  C  CA  . ALA A 1 71  ? -11.43600 -23.07500 41.56700 1.000 32.18000 ? 65  ALA A CA  1 
ATOM   469  C  C   . ALA A 1 71  ? -11.77500 -23.39000 43.02300 1.000 35.69000 ? 65  ALA A C   1 
ATOM   470  O  O   . ALA A 1 71  ? -12.33200 -22.53600 43.72300 1.000 36.51000 ? 65  ALA A O   1 
ATOM   471  C  CB  . ALA A 1 71  ? -12.65900 -23.29500 40.68100 1.000 36.91000 ? 65  ALA A CB  1 
ATOM   472  N  N   . GLY A 1 72  ? -11.43700 -24.58300 43.51000 1.000 36.27000 ? 66  GLY A N   1 
ATOM   473  C  CA  . GLY A 1 72  ? -11.81800 -24.93000 44.86800 1.000 36.33000 ? 66  GLY A CA  1 
ATOM   474  C  C   . GLY A 1 72  ? -11.03900 -24.19800 45.94400 1.000 37.62000 ? 66  GLY A C   1 
ATOM   475  O  O   . GLY A 1 72  ? -11.47300 -24.17900 47.11000 1.000 36.73000 ? 66  GLY A O   1 
ATOM   476  N  N   . TYR A 1 73  ? -9.88900  -23.61300 45.59500 1.000 33.53000 ? 67  TYR A N   1 
ATOM   477  C  CA  . TYR A 1 73  ? -9.10200  -22.89900 46.59800 1.000 34.74000 ? 67  TYR A CA  1 
ATOM   478  C  C   . TYR A 1 73  ? -9.69400  -21.55900 47.01000 1.000 31.59000 ? 67  TYR A C   1 
ATOM   479  O  O   . TYR A 1 73  ? -9.22100  -20.98500 47.99500 1.000 38.50000 ? 67  TYR A O   1 
ATOM   480  C  CB  . TYR A 1 73  ? -7.68600  -22.64900 46.09900 1.000 36.14000 ? 67  TYR A CB  1 
ATOM   481  C  CG  . TYR A 1 73  ? -6.87800  -23.90300 45.94200 1.000 36.72000 ? 67  TYR A CG  1 
ATOM   482  C  CD1 . TYR A 1 73  ? -6.68900  -24.77600 47.01200 1.000 38.30000 ? 67  TYR A CD1 1 
ATOM   483  C  CD2 . TYR A 1 73  ? -6.28700  -24.21400 44.72600 1.000 32.92000 ? 67  TYR A CD2 1 
ATOM   484  C  CE1 . TYR A 1 73  ? -5.93300  -25.93800 46.85700 1.000 40.77000 ? 67  TYR A CE1 1 
ATOM   485  C  CE2 . TYR A 1 73  ? -5.53200  -25.35700 44.56900 1.000 31.32000 ? 67  TYR A CE2 1 
ATOM   486  C  CZ  . TYR A 1 73  ? -5.35000  -26.20700 45.62200 1.000 38.06000 ? 67  TYR A CZ  1 
ATOM   487  O  OH  . TYR A 1 73  ? -4.59700  -27.34700 45.41700 1.000 45.59000 ? 67  TYR A OH  1 
ATOM   488  N  N   . GLY A 1 74  ? -10.67200 -21.02700 46.28000 1.000 31.05000 ? 68  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 74  ? -11.25300 -19.74800 46.67100 1.000 36.86000 ? 68  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 74  ? -10.36800 -18.52800 46.47000 1.000 36.05000 ? 68  GLY A C   1 
ATOM   491  O  O   . GLY A 1 74  ? -10.43200 -17.58100 47.26800 1.000 37.83000 ? 68  GLY A O   1 
ATOM   492  N  N   . PHE A 1 75  ? -9.54100  -18.51800 45.43400 1.000 30.37000 ? 69  PHE A N   1 
ATOM   493  C  CA  . PHE A 1 75  ? -8.80900  -17.30100 45.09700 1.000 34.95000 ? 69  PHE A CA  1 
ATOM   494  C  C   . PHE A 1 75  ? -9.77300  -16.19600 44.68000 1.000 32.10000 ? 69  PHE A C   1 
ATOM   495  O  O   . PHE A 1 75  ? -10.75100 -16.44200 43.96900 1.000 31.65000 ? 69  PHE A O   1 
ATOM   496  C  CB  . PHE A 1 75  ? -7.83700  -17.57500 43.96700 1.000 37.00000 ? 69  PHE A CB  1 
ATOM   497  C  CG  . PHE A 1 75  ? -6.69900  -18.45400 44.34800 1.000 38.10000 ? 69  PHE A CG  1 
ATOM   498  C  CD1 . PHE A 1 75  ? -5.93200  -18.17000 45.47400 1.000 35.37000 ? 69  PHE A CD1 1 
ATOM   499  C  CD2 . PHE A 1 75  ? -6.37500  -19.55500 43.56100 1.000 31.41000 ? 69  PHE A CD2 1 
ATOM   500  C  CE1 . PHE A 1 75  ? -4.85600  -18.97200 45.80000 1.000 32.00000 ? 69  PHE A CE1 1 
ATOM   501  C  CE2 . PHE A 1 75  ? -5.31100  -20.35800 43.88500 1.000 31.67000 ? 69  PHE A CE2 1 
ATOM   502  C  CZ  . PHE A 1 75  ? -4.55200  -20.07600 45.00500 1.000 33.07000 ? 69  PHE A CZ  1 
ATOM   503  N  N   . ASP A 1 76  ? -9.51300  -14.96800 45.12900 1.000 31.93000 ? 70  ASP A N   1 
ATOM   504  C  CA  . ASP A 1 76  ? -10.41900 -13.90700 44.73100 1.000 34.23000 ? 70  ASP A CA  1 
ATOM   505  C  C   . ASP A 1 76  ? -9.72900  -13.05300 43.67400 1.000 33.32000 ? 70  ASP A C   1 
ATOM   506  O  O   . ASP A 1 76  ? -8.62300  -13.37300 43.21200 1.000 33.10000 ? 70  ASP A O   1 
ATOM   507  C  CB  . ASP A 1 76  ? -10.91800 -13.09800 45.93900 1.000 36.08000 ? 70  ASP A CB  1 
ATOM   508  C  CG  . ASP A 1 76  ? -9.79900  -12.35800 46.67400 1.000 35.99000 ? 70  ASP A CG  1 
ATOM   509  O  OD1 . ASP A 1 76  ? -8.67400  -12.19400 46.12900 1.000 37.85000 ? 70  ASP A OD1 1 
ATOM   510  O  OD2 . ASP A 1 76  ? -10.04900 -11.93100 47.82500 1.000 42.87000 ? 70  ASP A OD2 1 
ATOM   511  N  N   . ASP A 1 77  ? -10.40000 -11.96800 43.27900 1.000 33.65000 ? 71  ASP A N   1 
ATOM   512  C  CA  . ASP A 1 77  ? -9.91500  -11.15800 42.17100 1.000 30.13000 ? 71  ASP A CA  1 
ATOM   513  C  C   . ASP A 1 77  ? -8.58500  -10.50000 42.49900 1.000 31.28000 ? 71  ASP A C   1 
ATOM   514  O  O   . ASP A 1 77  ? -7.69000  -10.44300 41.64900 1.000 29.25000 ? 71  ASP A O   1 
ATOM   515  C  CB  . ASP A 1 77  ? -10.95700 -10.11300 41.81000 1.000 31.14000 ? 71  ASP A CB  1 
ATOM   516  C  CG  . ASP A 1 77  ? -12.14500 -10.71300 41.10700 1.000 39.25000 ? 71  ASP A CG  1 
ATOM   517  O  OD1 . ASP A 1 77  ? -12.20900 -11.95500 41.03100 1.000 39.40000 ? 71  ASP A OD1 1 
ATOM   518  O  OD2 . ASP A 1 77  ? -13.01600 -9.95000  40.62900 1.000 43.79000 ? 71  ASP A OD2 1 
ATOM   519  N  N   . ALA A 1 78  ? -8.44800  -9.97100  43.71500 1.000 30.48000 ? 72  ALA A N   1 
ATOM   520  C  CA  . ALA A 1 78  ? -7.16700  -9.40000  44.12500 1.000 30.19000 ? 72  ALA A CA  1 
ATOM   521  C  C   . ALA A 1 78  ? -6.07100  -10.46000 44.09700 1.000 30.17000 ? 72  ALA A C   1 
ATOM   522  O  O   . ALA A 1 78  ? -4.95000  -10.18900 43.64900 1.000 29.82000 ? 72  ALA A O   1 
ATOM   523  C  CB  . ALA A 1 78  ? -7.29300  -8.78800  45.51700 1.000 29.63000 ? 72  ALA A CB  1 
ATOM   524  N  N   . ASP A 1 79  ? -6.39300  -11.68200 44.53700 1.000 29.29000 ? 73  ASP A N   1 
ATOM   525  C  CA  . ASP A 1 79  ? -5.47500  -12.81300 44.39800 1.000 32.69000 ? 73  ASP A CA  1 
ATOM   526  C  C   . ASP A 1 79  ? -5.09300  -13.04500 42.93700 1.000 28.31000 ? 73  ASP A C   1 
ATOM   527  O  O   . ASP A 1 79  ? -3.93700  -13.34200 42.62200 1.000 27.12000 ? 73  ASP A O   1 
ATOM   528  C  CB  . ASP A 1 79  ? -6.11500  -14.10100 44.94900 1.000 31.01000 ? 73  ASP A CB  1 
ATOM   529  C  CG  . ASP A 1 79  ? -6.25600  -14.12000 46.46000 1.000 35.36000 ? 73  ASP A CG  1 
ATOM   530  O  OD1 . ASP A 1 79  ? -5.51600  -13.38900 47.15600 1.000 36.48000 ? 73  ASP A OD1 1 
ATOM   531  O  OD2 . ASP A 1 79  ? -7.11600  -14.89300 46.94600 1.000 31.78000 ? 73  ASP A OD2 1 
ATOM   532  N  N   . ILE A 1 80  ? -6.07600  -13.02500 42.04200 1.000 29.59000 ? 74  ILE A N   1 
ATOM   533  C  CA  . ILE A 1 80  ? -5.75700  -13.27400 40.64400 1.000 30.31000 ? 74  ILE A CA  1 
ATOM   534  C  C   . ILE A 1 80  ? -4.92500  -12.12700 40.09300 1.000 29.10000 ? 74  ILE A C   1 
ATOM   535  O  O   . ILE A 1 80  ? -3.99700  -12.33200 39.29400 1.000 23.44000 ? 74  ILE A O   1 
ATOM   536  C  CB  . ILE A 1 80  ? -7.04400  -13.49800 39.83100 1.000 28.24000 ? 74  ILE A CB  1 
ATOM   537  C  CG1 . ILE A 1 80  ? -7.64600  -14.84700 40.16900 1.000 29.17000 ? 74  ILE A CG1 1 
ATOM   538  C  CG2 . ILE A 1 80  ? -6.77200  -13.44200 38.31100 1.000 27.95000 ? 74  ILE A CG2 1 
ATOM   539  C  CD1 . ILE A 1 80  ? -9.08700  -14.92300 39.79400 1.000 32.77000 ? 74  ILE A CD1 1 
ATOM   540  N  N   . ALA A 1 81  ? -5.22300  -10.90100 40.52700 1.000 26.58000 ? 75  ALA A N   1 
ATOM   541  C  CA  . ALA A 1 81  ? -4.41100  -9.78300  40.07900 1.000 25.12000 ? 75  ALA A CA  1 
ATOM   542  C  C   . ALA A 1 81  ? -2.96900  -9.96800  40.51700 1.000 24.34000 ? 75  ALA A C   1 
ATOM   543  O  O   . ALA A 1 81  ? -2.04500  -9.66700  39.75800 1.000 26.70000 ? 75  ALA A O   1 
ATOM   544  C  CB  . ALA A 1 81  ? -4.98800  -8.46700  40.59400 1.000 28.14000 ? 75  ALA A CB  1 
ATOM   545  N  N   . LEU A 1 82  ? -2.74900  -10.52400 41.70600 1.000 24.18000 ? 76  LEU A N   1 
ATOM   546  C  CA  . LEU A 1 82  ? -1.37400  -10.80200 42.11900 1.000 24.80000 ? 76  LEU A CA  1 
ATOM   547  C  C   . LEU A 1 82  ? -0.70900  -11.84800 41.21900 1.000 24.14000 ? 76  LEU A C   1 
ATOM   548  O  O   . LEU A 1 82  ? 0.49600   -11.77500 40.94900 1.000 24.86000 ? 76  LEU A O   1 
ATOM   549  C  CB  . LEU A 1 82  ? -1.34700  -11.26500 43.57400 1.000 25.77000 ? 76  LEU A CB  1 
ATOM   550  C  CG  . LEU A 1 82  ? 0.06300   -11.03500 44.14000 1.000 26.62000 ? 76  LEU A CG  1 
ATOM   551  C  CD1 . LEU A 1 82  ? 0.36200   -9.55100  44.23600 1.000 30.30000 ? 76  LEU A CD1 1 
ATOM   552  C  CD2 . LEU A 1 82  ? 0.24600   -11.68900 45.51700 1.000 26.95000 ? 76  LEU A CD2 1 
ATOM   553  N  N   . MET A 1 83  ? -1.45400  -12.85700 40.79000 1.000 24.06000 ? 77  MET A N   1 
ATOM   554  C  CA  . MET A 1 83  ? -0.91000  -13.84000 39.85000 1.000 24.69000 ? 77  MET A CA  1 
ATOM   555  C  C   . MET A 1 83  ? -0.50600  -13.22100 38.52400 1.000 25.45000 ? 77  MET A C   1 
ATOM   556  O  O   . MET A 1 83  ? 0.31600   -13.80800 37.80400 1.000 29.54000 ? 77  MET A O   1 
ATOM   557  C  CB  . MET A 1 83  ? -1.92600  -14.94800 39.54100 1.000 26.01000 ? 77  MET A CB  1 
ATOM   558  C  CG  . MET A 1 83  ? -2.33100  -15.82900 40.67600 1.000 26.34000 ? 77  MET A CG  1 
ATOM   559  S  SD  . MET A 1 83  ? -3.37800  -17.18700 40.08600 1.000 30.60000 ? 77  MET A SD  1 
ATOM   560  C  CE  . MET A 1 83  ? -3.78200  -17.96500 41.63000 1.000 28.97000 ? 77  MET A CE  1 
ATOM   561  N  N   . CYS A 1 84  ? -1.09800  -12.09000 38.14600 1.000 24.86000 ? 78  CYS A N   1 
ATOM   562  C  CA  . CYS A 1 84  ? -0.72800  -11.41000 36.90800 1.000 27.42000 ? 78  CYS A CA  1 
ATOM   563  C  C   . CYS A 1 84  ? 0.32200   -10.32000 37.11000 1.000 24.97000 ? 78  CYS A C   1 
ATOM   564  O  O   . CYS A 1 84  ? 0.50300   -9.49000  36.21700 1.000 29.13000 ? 78  CYS A O   1 
ATOM   565  C  CB  . CYS A 1 84  ? -1.96500  -10.77000 36.24900 1.000 25.42000 ? 78  CYS A CB  1 
ATOM   566  S  SG  . CYS A 1 84  ? -3.29000  -11.85900 35.85400 1.000 29.07000 ? 78  CYS A SG  1 
ATOM   567  N  N   . ALA A 1 85  ? 1.00600   -10.28300 38.24500 1.000 25.12000 ? 79  ALA A N   1 
ATOM   568  C  CA  . ALA A 1 85  ? 1.69400   -9.07600  38.67400 1.000 28.64000 ? 79  ALA A CA  1 
ATOM   569  C  C   . ALA A 1 85  ? 3.21300   -9.15600  38.51000 1.000 30.48000 ? 79  ALA A C   1 
ATOM   570  O  O   . ALA A 1 85  ? 3.79100   -10.24000 38.39300 1.000 28.41000 ? 79  ALA A O   1 
ATOM   571  C  CB  . ALA A 1 85  ? 1.36300   -8.76500  40.13800 1.000 22.82000 ? 79  ALA A CB  1 
ATOM   572  N  N   . SER A 1 86  ? 3.83100   -7.96000  38.43800 1.000 29.19000 ? 80  SER A N   1 
ATOM   573  C  CA  . SER A 1 86  ? 5.22600   -7.64700  38.80700 1.000 25.62000 ? 80  SER A CA  1 
ATOM   574  C  C   . SER A 1 86  ? 5.11100   -6.59300  39.90200 1.000 24.36000 ? 80  SER A C   1 
ATOM   575  O  O   . SER A 1 86  ? 5.28900   -5.38800  39.67000 1.000 23.42000 ? 80  SER A O   1 
ATOM   576  C  CB  . SER A 1 86  ? 6.09000   -7.11400  37.61700 1.000 24.62000 ? 80  SER A CB  1 
ATOM   577  O  OG  . SER A 1 86  ? 5.95400   -7.94600  36.47900 1.000 27.27000 ? 80  SER A OG  1 
ATOM   578  N  N   . HIS A 1 87  ? 4.76200   -7.03600  41.09300 1.000 25.36000 ? 81  HIS A N   1 
ATOM   579  C  CA  . HIS A 1 87  ? 4.41700   -6.09200  42.14300 1.000 24.82000 ? 81  HIS A CA  1 
ATOM   580  C  C   . HIS A 1 87  ? 5.67700   -5.49900  42.76400 1.000 24.52000 ? 81  HIS A C   1 
ATOM   581  O  O   . HIS A 1 87  ? 6.80000   -5.95700  42.52000 1.000 21.79000 ? 81  HIS A O   1 
ATOM   582  C  CB  . HIS A 1 87  ? 3.52600   -6.77000  43.18600 1.000 24.76000 ? 81  HIS A CB  1 
ATOM   583  C  CG  . HIS A 1 87  ? 4.17500   -7.91700  43.90600 1.000 25.40000 ? 81  HIS A CG  1 
ATOM   584  N  ND1 . HIS A 1 87  ? 5.20100   -7.74400  44.81700 1.000 24.79000 ? 81  HIS A ND1 1 
ATOM   585  C  CD2 . HIS A 1 87  ? 3.92100   -9.24800  43.87500 1.000 25.79000 ? 81  HIS A CD2 1 
ATOM   586  C  CE1 . HIS A 1 87  ? 5.55500   -8.91700  45.31000 1.000 25.50000 ? 81  HIS A CE1 1 
ATOM   587  N  NE2 . HIS A 1 87  ? 4.78900   -9.84600  44.76400 1.000 26.87000 ? 81  HIS A NE2 1 
ATOM   588  N  N   . SER A 1 88  ? 5.48800   -4.43200  43.54600 1.000 25.79000 ? 82  SER A N   1 
ATOM   589  C  CA  . SER A 1 88  ? 6.59700   -3.66700  44.10600 1.000 25.25000 ? 82  SER A CA  1 
ATOM   590  C  C   . SER A 1 88  ? 7.12100   -4.23400  45.42500 1.000 25.75000 ? 82  SER A C   1 
ATOM   591  O  O   . SER A 1 88  ? 7.94000   -3.58000  46.08000 1.000 26.13000 ? 82  SER A O   1 
ATOM   592  C  CB  . SER A 1 88  ? 6.18100   -2.20200  44.31200 1.000 26.06000 ? 82  SER A CB  1 
ATOM   593  O  OG  . SER A 1 88  ? 6.02100   -1.53100  43.07200 1.000 24.96000 ? 82  SER A OG  1 
ATOM   594  N  N   . SER A 1 89  ? 6.66000   -5.41700  45.83400 1.000 26.12000 ? 83  SER A N   1 
ATOM   595  C  CA  . SER A 1 89  ? 7.00600   -6.01700  47.13300 1.000 24.73000 ? 83  SER A CA  1 
ATOM   596  C  C   . SER A 1 89  ? 6.63500   -5.10100  48.29600 1.000 28.08000 ? 83  SER A C   1 
ATOM   597  O  O   . SER A 1 89  ? 7.32500   -5.06300  49.32900 1.000 29.93000 ? 83  SER A O   1 
ATOM   598  C  CB  . SER A 1 89  ? 8.48700   -6.40200  47.21400 1.000 25.28000 ? 83  SER A CB  1 
ATOM   599  O  OG  . SER A 1 89  ? 8.94700   -6.91600  45.97600 1.000 29.57000 ? 83  SER A OG  1 
ATOM   600  N  N   . GLU A 1 90  ? 5.53500   -4.36800  48.15900 1.000 27.81000 ? 84  GLU A N   1 
ATOM   601  C  CA  . GLU A 1 90  ? 5.00400   -3.66100  49.31200 1.000 29.18000 ? 84  GLU A CA  1 
ATOM   602  C  C   . GLU A 1 90  ? 4.54600   -4.67600  50.33800 1.000 32.34000 ? 84  GLU A C   1 
ATOM   603  O  O   . GLU A 1 90  ? 4.29100   -5.83900  50.01000 1.000 30.97000 ? 84  GLU A O   1 
ATOM   604  C  CB  . GLU A 1 90  ? 3.84900   -2.75200  48.90400 1.000 26.58000 ? 84  GLU A CB  1 
ATOM   605  C  CG  . GLU A 1 90  ? 4.35300   -1.55300  48.10900 1.000 33.77000 ? 84  GLU A CG  1 
ATOM   606  C  CD  . GLU A 1 90  ? 3.30400   -0.95700  47.19000 1.000 34.28000 ? 84  GLU A CD  1 
ATOM   607  O  OE1 . GLU A 1 90  ? 2.12300   -1.33900  47.32500 1.000 37.62000 ? 84  GLU A OE1 1 
ATOM   608  O  OE2 . GLU A 1 90  ? 3.67000   -0.09800  46.35000 1.000 32.53000 ? 84  GLU A OE2 1 
ATOM   609  N  N   . ASP A 1 91  ? 4.45000   -4.23100  51.60400 1.000 31.86000 ? 85  ASP A N   1 
ATOM   610  C  CA  . ASP A 1 91  ? 4.03000   -5.14500  52.66200 1.000 31.15000 ? 85  ASP A CA  1 
ATOM   611  C  C   . ASP A 1 91  ? 2.69100   -5.79500  52.32200 1.000 33.26000 ? 85  ASP A C   1 
ATOM   612  O  O   . ASP A 1 91  ? 2.44900   -6.95600  52.70200 1.000 29.05000 ? 85  ASP A O   1 
ATOM   613  C  CB  . ASP A 1 91  ? 3.95800   -4.41400  54.02700 1.000 36.89000 ? 85  ASP A CB  1 
ATOM   614  C  CG  . ASP A 1 91  ? 5.35200   -4.08400  54.61900 1.000 42.42000 ? 85  ASP A CG  1 
ATOM   615  O  OD1 . ASP A 1 91  ? 6.38600   -4.49000  54.01800 1.000 41.11000 ? 85  ASP A OD1 1 
ATOM   616  O  OD2 . ASP A 1 91  ? 5.41600   -3.40500  55.68200 1.000 41.51000 ? 85  ASP A OD2 1 
ATOM   617  N  N   . ARG A 1 92  ? 1.81800   -5.08200  51.57400 1.000 31.61000 ? 86  ARG A N   1 
ATOM   618  C  CA  . ARG A 1 92  ? 0.50100   -5.64200  51.23900 1.000 32.62000 ? 86  ARG A CA  1 
ATOM   619  C  C   . ARG A 1 92  ? 0.59700   -6.71100  50.15700 1.000 32.41000 ? 86  ARG A C   1 
ATOM   620  O  O   . ARG A 1 92  ? -0.26200  -7.59800  50.09600 1.000 36.73000 ? 86  ARG A O   1 
ATOM   621  C  CB  . ARG A 1 92  ? -0.47800  -4.54200  50.80000 1.000 31.50000 ? 86  ARG A CB  1 
ATOM   622  C  CG  . ARG A 1 92  ? -0.11000  -3.84000  49.49500 1.000 31.71000 ? 86  ARG A CG  1 
ATOM   623  C  CD  . ARG A 1 92  ? -1.06300  -2.68800  49.15900 1.000 30.69000 ? 86  ARG A CD  1 
ATOM   624  N  NE  . ARG A 1 92  ? -0.45300  -1.78800  48.17700 1.000 31.46000 ? 86  ARG A NE  1 
ATOM   625  C  CZ  . ARG A 1 92  ? -1.06500  -0.75200  47.61400 1.000 34.61000 ? 86  ARG A CZ  1 
ATOM   626  N  NH1 . ARG A 1 92  ? -2.33500  -0.48000  47.85900 1.000 34.04000 ? 86  ARG A NH1 1 
ATOM   627  N  NH2 . ARG A 1 92  ? -0.38400  0.03900   46.79400 1.000 37.74000 ? 86  ARG A NH2 1 
ATOM   628  N  N   . HIS A 1 93  ? 1.62100   -6.65300  49.29800 1.000 31.45000 ? 87  HIS A N   1 
ATOM   629  C  CA  . HIS A 1 93  ? 1.85100   -7.74400  48.34700 1.000 30.07000 ? 87  HIS A CA  1 
ATOM   630  C  C   . HIS A 1 93  ? 2.39900   -8.97100  49.05200 1.000 29.87000 ? 87  HIS A C   1 
ATOM   631  O  O   . HIS A 1 93  ? 2.02300   -10.10100 48.72000 1.000 30.19000 ? 87  HIS A O   1 
ATOM   632  C  CB  . HIS A 1 93  ? 2.81700   -7.31000  47.25000 1.000 30.38000 ? 87  HIS A CB  1 
ATOM   633  C  CG  . HIS A 1 93  ? 2.35400   -6.12300  46.46700 1.000 29.00000 ? 87  HIS A CG  1 
ATOM   634  N  ND1 . HIS A 1 93  ? 3.12600   -4.99200  46.30100 1.000 27.96000 ? 87  HIS A ND1 1 
ATOM   635  C  CD2 . HIS A 1 93  ? 1.20200   -5.89600  45.79400 1.000 26.85000 ? 87  HIS A CD2 1 
ATOM   636  C  CE1 . HIS A 1 93  ? 2.46700   -4.11400  45.56300 1.000 28.24000 ? 87  HIS A CE1 1 
ATOM   637  N  NE2 . HIS A 1 93  ? 1.29700   -4.64100  45.24100 1.000 26.33000 ? 87  HIS A NE2 1 
ATOM   638  N  N   . ILE A 1 94  ? 3.29400   -8.76600  50.02600 1.000 31.35000 ? 88  ILE A N   1 
ATOM   639  C  CA  . ILE A 1 94  ? 3.82200   -9.87800  50.82600 1.000 33.48000 ? 88  ILE A CA  1 
ATOM   640  C  C   . ILE A 1 94  ? 2.69200   -10.57500 51.56900 1.000 32.98000 ? 88  ILE A C   1 
ATOM   641  O  O   . ILE A 1 94  ? 2.61400   -11.81300 51.61800 1.000 31.10000 ? 88  ILE A O   1 
ATOM   642  C  CB  . ILE A 1 94  ? 4.88600   -9.37200  51.81800 1.000 34.48000 ? 88  ILE A CB  1 
ATOM   643  C  CG1 . ILE A 1 94  ? 5.88500   -8.46500  51.12700 1.000 35.94000 ? 88  ILE A CG1 1 
ATOM   644  C  CG2 . ILE A 1 94  ? 5.61900   -10.53900 52.44300 1.000 36.39000 ? 88  ILE A CG2 1 
ATOM   645  C  CD1 . ILE A 1 94  ? 6.59200   -9.18200  50.02900 1.000 33.22000 ? 88  ILE A CD1 1 
ATOM   646  N  N   . ALA A 1 95  ? 1.82200   -9.78400  52.19900 1.000 35.15000 ? 89  ALA A N   1 
ATOM   647  C  CA  . ALA A 1 95  ? 0.74100   -10.36000 52.98500 1.000 35.88000 ? 89  ALA A CA  1 
ATOM   648  C  C   . ALA A 1 95  ? -0.19100  -11.18000 52.10800 1.000 34.33000 ? 89  ALA A C   1 
ATOM   649  O  O   . ALA A 1 95  ? -0.63600  -12.26600 52.50800 1.000 31.63000 ? 89  ALA A O   1 
ATOM   650  C  CB  . ALA A 1 95  ? -0.03200  -9.25600  53.71400 1.000 33.41000 ? 89  ALA A CB  1 
ATOM   651  N  N   . ARG A 1 96  ? -0.50500  -10.68200 50.90800 1.000 34.13000 ? 90  ARG A N   1 
ATOM   652  C  CA  . ARG A 1 96  ? -1.38700  -11.46200 50.03400 1.000 30.68000 ? 90  ARG A CA  1 
ATOM   653  C  C   . ARG A 1 96  ? -0.70000  -12.71700 49.52700 1.000 29.04000 ? 90  ARG A C   1 
ATOM   654  O  O   . ARG A 1 96  ? -1.35900  -13.73800 49.30300 1.000 30.05000 ? 90  ARG A O   1 
ATOM   655  C  CB  . ARG A 1 96  ? -1.87100  -10.61000 48.86000 1.000 32.58000 ? 90  ARG A CB  1 
ATOM   656  C  CG  . ARG A 1 96  ? -2.83300  -11.32800 47.90300 1.000 30.23000 ? 90  ARG A CG  1 
ATOM   657  C  CD  . ARG A 1 96  ? -3.57700  -10.33900 46.99200 1.000 29.30000 ? 90  ARG A CD  1 
ATOM   658  N  NE  . ARG A 1 96  ? -4.38600  -9.43700  47.80300 1.000 37.42000 ? 90  ARG A NE  1 
ATOM   659  C  CZ  . ARG A 1 96  ? -5.51900  -9.77600  48.39800 1.000 31.63000 ? 90  ARG A CZ  1 
ATOM   660  N  NH1 . ARG A 1 96  ? -6.04800  -10.97300 48.24100 1.000 28.92000 ? 90  ARG A NH1 1 
ATOM   661  N  NH2 . ARG A 1 96  ? -6.13500  -8.89200  49.17700 1.000 35.76000 ? 90  ARG A NH2 1 
ATOM   662  N  N   . THR A 1 97  ? 0.61300   -12.65900 49.30100 1.000 31.52000 ? 91  THR A N   1 
ATOM   663  C  CA  . THR A 1 97  ? 1.32600   -13.87100 48.91800 1.000 28.95000 ? 91  THR A CA  1 
ATOM   664  C  C   . THR A 1 97  ? 1.22200   -14.91500 50.02000 1.000 32.40000 ? 91  THR A C   1 
ATOM   665  O  O   . THR A 1 97  ? 0.92300   -16.08300 49.75100 1.000 33.93000 ? 91  THR A O   1 
ATOM   666  C  CB  . THR A 1 97  ? 2.79100   -13.55000 48.58100 1.000 30.46000 ? 91  THR A CB  1 
ATOM   667  O  OG1 . THR A 1 97  ? 2.84700   -12.62800 47.47500 1.000 29.74000 ? 91  THR A OG1 1 
ATOM   668  C  CG2 . THR A 1 97  ? 3.52500   -14.80400 48.18300 1.000 25.49000 ? 91  THR A CG2 1 
ATOM   669  N  N   . ARG A 1 98  ? 1.39700   -14.50300 51.27700 1.000 31.91000 ? 92  ARG A N   1 
ATOM   670  C  CA  . ARG A 1 98  ? 1.24500   -15.44900 52.37700 1.000 32.88000 ? 92  ARG A CA  1 
ATOM   671  C  C   . ARG A 1 98  ? -0.20700  -15.91300 52.52800 1.000 37.08000 ? 92  ARG A C   1 
ATOM   672  O  O   . ARG A 1 98  ? -0.45700  -17.08000 52.84900 1.000 35.07000 ? 92  ARG A O   1 
ATOM   673  C  CB  . ARG A 1 98  ? 1.76700   -14.82100 53.66800 1.000 34.65000 ? 92  ARG A CB  1 
ATOM   674  C  CG  . ARG A 1 98  ? 3.25600   -14.48500 53.58700 1.000 35.65000 ? 92  ARG A CG  1 
ATOM   675  C  CD  . ARG A 1 98  ? 3.79700   -13.82500 54.88200 1.000 41.22000 ? 92  ARG A CD  1 
ATOM   676  N  NE  . ARG A 1 98  ? 5.25400   -13.94900 54.95400 1.000 40.41000 ? 92  ARG A NE  1 
ATOM   677  C  CZ  . ARG A 1 98  ? 6.08800   -13.07100 55.49900 1.000 47.97000 ? 92  ARG A CZ  1 
ATOM   678  N  NH1 . ARG A 1 98  ? 5.65300   -11.94000 56.05700 1.000 48.87000 ? 92  ARG A NH1 1 
ATOM   679  N  NH2 . ARG A 1 98  ? 7.39700   -13.32600 55.47300 1.000 46.02000 ? 92  ARG A NH2 1 
ATOM   680  N  N   . ALA A 1 99  ? -1.17500  -15.01700 52.30800 1.000 36.49000 ? 93  ALA A N   1 
ATOM   681  C  CA  . ALA A 1 99  ? -2.57800  -15.41400 52.37200 1.000 32.91000 ? 93  ALA A CA  1 
ATOM   682  C  C   . ALA A 1 99  ? -2.89900  -16.48400 51.33200 1.000 37.07000 ? 93  ALA A C   1 
ATOM   683  O  O   . ALA A 1 99  ? -3.59800  -17.46600 51.63000 1.000 35.26000 ? 93  ALA A O   1 
ATOM   684  C  CB  . ALA A 1 99  ? -3.46300  -14.18600 52.17000 1.000 32.57000 ? 93  ALA A CB  1 
ATOM   685  N  N   . MET A 1 100 ? -2.40400  -16.30700 50.10000 1.000 34.45000 ? 94  MET A N   1 
ATOM   686  C  CA  . MET A 1 100 ? -2.66900  -17.28100 49.04000 1.000 36.87000 ? 94  MET A CA  1 
ATOM   687  C  C   . MET A 1 100 ? -1.97100  -18.60900 49.32200 1.000 39.05000 ? 94  MET A C   1 
ATOM   688  O  O   . MET A 1 100 ? -2.50400  -19.67400 48.99200 1.000 36.96000 ? 94  MET A O   1 
ATOM   689  C  CB  . MET A 1 100 ? -2.22900  -16.72800 47.68100 1.000 32.99000 ? 94  MET A CB  1 
ATOM   690  C  CG  . MET A 1 100 ? -2.92800  -15.45000 47.25200 1.000 31.45000 ? 94  MET A CG  1 
ATOM   691  S  SD  . MET A 1 100 ? -2.17800  -14.68800 45.80600 1.000 30.41000 ? 94  MET A SD  1 
ATOM   692  C  CE  . MET A 1 100 ? -2.36400  -16.05100 44.62700 1.000 25.97000 ? 94  MET A CE  1 
ATOM   693  N  N   . LEU A 1 101 ? -0.77200  -18.56500 49.91600 1.000 34.43000 ? 95  LEU A N   1 
ATOM   694  C  CA  . LEU A 1 101 ? -0.12900  -19.79900 50.35300 1.000 36.08000 ? 95  LEU A CA  1 
ATOM   695  C  C   . LEU A 1 101 ? -0.97800  -20.51700 51.38600 1.000 38.77000 ? 95  LEU A C   1 
ATOM   696  O  O   . LEU A 1 101 ? -0.99300  -21.75200 51.42800 1.000 35.97000 ? 95  LEU A O   1 
ATOM   697  C  CB  . LEU A 1 101 ? 1.27200   -19.51300 50.91400 1.000 35.84000 ? 95  LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 101 ? 2.38000   -19.24000 49.86900 1.000 36.08000 ? 95  LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 101 ? 3.61800   -18.63700 50.51500 1.000 36.60000 ? 95  LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 101 ? 2.74600   -20.52600 49.12500 1.000 33.96000 ? 95  LEU A CD2 1 
ATOM   701  N  N   . SER A 1 102 ? -1.71100  -19.77400 52.22100 1.000 38.46000 ? 96  SER A N   1 
ATOM   702  C  CA  . SER A 1 102 ? -2.55700  -20.45600 53.19300 1.000 37.43000 ? 96  SER A CA  1 
ATOM   703  C  C   . SER A 1 102 ? -3.75300  -21.10500 52.52800 1.000 37.39000 ? 96  SER A C   1 
ATOM   704  O  O   . SER A 1 102 ? -4.20200  -22.15500 52.98000 1.000 36.61000 ? 96  SER A O   1 
ATOM   705  C  CB  . SER A 1 102 ? -3.03600  -19.50400 54.27400 1.000 36.43000 ? 96  SER A CB  1 
ATOM   706  O  OG  . SER A 1 102 ? -1.93200  -19.08900 55.04800 1.000 47.77000 ? 96  SER A OG  1 
ATOM   707  N  N   . LYS A 1 103 ? -4.28500  -20.50400 51.46300 1.000 36.96000 ? 97  LYS A N   1 
ATOM   708  C  CA  . LYS A 1 103 ? -5.44200  -21.10900 50.81400 1.000 39.68000 ? 97  LYS A CA  1 
ATOM   709  C  C   . LYS A 1 103 ? -5.10300  -22.47300 50.21700 1.000 39.50000 ? 97  LYS A C   1 
ATOM   710  O  O   . LYS A 1 103 ? -5.96400  -23.35400 50.16100 1.000 36.97000 ? 97  LYS A O   1 
ATOM   711  C  CB  . LYS A 1 103 ? -5.99500  -20.15800 49.74800 1.000 39.29000 ? 97  LYS A CB  1 
ATOM   712  C  CG  . LYS A 1 103 ? -6.71500  -18.97000 50.34700 1.000 40.11000 ? 97  LYS A CG  1 
ATOM   713  C  CD  . LYS A 1 103 ? -7.09900  -17.96200 49.28900 1.000 38.22000 ? 97  LYS A CD  1 
ATOM   714  C  CE  . LYS A 1 103 ? -8.01800  -16.91100 49.87800 1.000 38.45000 ? 97  LYS A CE  1 
ATOM   715  N  NZ  . LYS A 1 103 ? -8.30400  -15.85600 48.86200 1.000 39.00000 ? 97  LYS A NZ  1 
ATOM   716  N  N   . ILE A 1 104 ? -3.86100  -22.67900 49.77600 1.000 39.14000 ? 98  ILE A N   1 
ATOM   717  C  CA  . ILE A 1 104 ? -3.47000  -23.95700 49.18100 1.000 38.28000 ? 98  ILE A CA  1 
ATOM   718  C  C   . ILE A 1 104 ? -2.62800  -24.80700 50.13600 1.000 41.63000 ? 98  ILE A C   1 
ATOM   719  O  O   . ILE A 1 104 ? -2.10100  -25.85100 49.72600 1.000 39.41000 ? 98  ILE A O   1 
ATOM   720  C  CB  . ILE A 1 104 ? -2.74000  -23.74200 47.84800 1.000 36.67000 ? 98  ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 104 ? -1.38500  -23.05800 48.06900 1.000 37.45000 ? 98  ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 104 ? -3.58800  -22.88100 46.89700 1.000 33.05000 ? 98  ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 104 ? -0.51000  -23.06900 46.83300 1.000 27.30000 ? 98  ILE A CD1 1 
ATOM   724  N  N   . LYS A 1 105 ? -2.47700  -24.37500 51.39900 1.000 35.47000 ? 99  LYS A N   1 
ATOM   725  C  CA  . LYS A 1 105 ? -1.81100  -25.16000 52.44500 1.000 35.69000 ? 99  LYS A CA  1 
ATOM   726  C  C   . LYS A 1 105 ? -0.34000  -25.41100 52.10100 1.000 43.77000 ? 99  LYS A C   1 
ATOM   727  O  O   . LYS A 1 105 ? 0.20100   -26.49300 52.35200 1.000 42.13000 ? 99  LYS A O   1 
ATOM   728  C  CB  . LYS A 1 105 ? -2.54100  -26.48900 52.70800 1.000 44.91000 ? 99  LYS A CB  1 
ATOM   729  C  CG  . LYS A 1 105 ? -4.07700  -26.39900 52.89400 1.000 46.12000 ? 99  LYS A CG  1 
ATOM   730  C  CD  . LYS A 1 105 ? -4.79100  -27.79100 52.86900 1.000 52.42000 ? 99  LYS A CD  1 
ATOM   731  C  CE  . LYS A 1 105 ? -4.58000  -28.61500 51.53800 1.000 54.65000 ? 99  LYS A CE  1 
ATOM   732  N  NZ  . LYS A 1 105 ? -5.09000  -28.01500 50.23000 1.000 46.51000 ? 99  LYS A NZ  1 
ATOM   733  N  N   . ALA A 1 106 ? 0.30800   -24.40800 51.51100 1.000 34.03000 ? 100 ALA A N   1 
ATOM   734  C  CA  . ALA A 1 106 ? 1.72700   -24.42900 51.19600 1.000 37.22000 ? 100 ALA A CA  1 
ATOM   735  C  C   . ALA A 1 106 ? 2.45700   -23.47500 52.14000 1.000 41.07000 ? 100 ALA A C   1 
ATOM   736  O  O   . ALA A 1 106 ? 1.85000   -22.82200 52.98900 1.000 39.04000 ? 100 ALA A O   1 
ATOM   737  C  CB  . ALA A 1 106 ? 1.95100   -24.05400 49.73300 1.000 32.53000 ? 100 ALA A CB  1 
ATOM   738  N  N   . GLU A 1 107 ? 3.77700   -23.40500 52.01000 1.000 38.69000 ? 101 GLU A N   1 
ATOM   739  C  CA  . GLU A 1 107 ? 4.55700   -22.44700 52.78300 1.000 40.26000 ? 101 GLU A CA  1 
ATOM   740  C  C   . GLU A 1 107 ? 5.63700   -21.84200 51.90200 1.000 39.19000 ? 101 GLU A C   1 
ATOM   741  O  O   . GLU A 1 107 ? 5.84300   -22.26700 50.75700 1.000 36.57000 ? 101 GLU A O   1 
ATOM   742  C  CB  . GLU A 1 107 ? 5.17600   -23.08900 54.01900 1.000 43.95000 ? 101 GLU A CB  1 
ATOM   743  C  CG  . GLU A 1 107 ? 6.02900   -24.30400 53.72300 1.000 49.77000 ? 101 GLU A CG  1 
ATOM   744  C  CD  . GLU A 1 107 ? 6.01700   -25.29600 54.88500 1.000 63.91000 ? 101 GLU A CD  1 
ATOM   745  O  OE1 . GLU A 1 107 ? 5.51700   -24.92400 55.97800 1.000 61.16000 ? 101 GLU A OE1 1 
ATOM   746  O  OE2 . GLU A 1 107 ? 6.48800   -26.44500 54.70100 1.000 66.52000 ? 101 GLU A OE2 1 
ATOM   747  N  N   . GLU A 1 108 ? 6.32700   -20.83000 52.45100 1.000 37.92000 ? 102 GLU A N   1 
ATOM   748  C  CA  . GLU A 1 108 ? 7.29400   -20.06600 51.65900 1.000 35.99000 ? 102 GLU A CA  1 
ATOM   749  C  C   . GLU A 1 108 ? 8.43000   -20.94100 51.15500 1.000 37.87000 ? 102 GLU A C   1 
ATOM   750  O  O   . GLU A 1 108 ? 8.95500   -20.69800 50.06600 1.000 35.97000 ? 102 GLU A O   1 
ATOM   751  C  CB  . GLU A 1 108 ? 7.86900   -18.91000 52.47200 1.000 37.27000 ? 102 GLU A CB  1 
ATOM   752  C  CG  . GLU A 1 108 ? 6.81300   -17.93800 52.98800 1.000 43.87000 ? 102 GLU A CG  1 
ATOM   753  C  CD  . GLU A 1 108 ? 7.40100   -16.81300 53.85300 1.000 51.55000 ? 102 GLU A CD  1 
ATOM   754  O  OE1 . GLU A 1 108 ? 8.62000   -16.49400 53.70200 1.000 50.20000 ? 102 GLU A OE1 1 
ATOM   755  O  OE2 . GLU A 1 108 ? 6.63400   -16.25400 54.68300 1.000 46.77000 ? 102 GLU A OE2 1 
ATOM   756  N  N   . ALA A 1 109 ? 8.81600   -21.96500 51.92300 1.000 39.17000 ? 103 ALA A N   1 
ATOM   757  C  CA  . ALA A 1 109 ? 9.85400   -22.88900 51.47400 1.000 38.37000 ? 103 ALA A CA  1 
ATOM   758  C  C   . ALA A 1 109 ? 9.46600   -23.61700 50.18800 1.000 39.30000 ? 103 ALA A C   1 
ATOM   759  O  O   . ALA A 1 109 ? 10.35100  -24.10500 49.47600 1.000 35.77000 ? 103 ALA A O   1 
ATOM   760  C  CB  . ALA A 1 109 ? 10.16800  -23.90200 52.58300 1.000 37.71000 ? 103 ALA A CB  1 
ATOM   761  N  N   . ASP A 1 110 ? 8.16600   -23.70200 49.87700 1.000 33.58000 ? 104 ASP A N   1 
ATOM   762  C  CA  . ASP A 1 110 ? 7.73100   -24.34900 48.64800 1.000 38.58000 ? 104 ASP A CA  1 
ATOM   763  C  C   . ASP A 1 110 ? 8.00700   -23.49400 47.42100 1.000 38.31000 ? 104 ASP A C   1 
ATOM   764  O  O   . ASP A 1 110 ? 8.12800   -24.04200 46.31800 1.000 34.32000 ? 104 ASP A O   1 
ATOM   765  C  CB  . ASP A 1 110 ? 6.23800   -24.70400 48.73000 1.000 38.00000 ? 104 ASP A CB  1 
ATOM   766  C  CG  . ASP A 1 110 ? 5.93800   -25.73000 49.83000 1.000 42.27000 ? 104 ASP A CG  1 
ATOM   767  O  OD1 . ASP A 1 110 ? 6.64300   -26.76500 49.91800 1.000 40.19000 ? 104 ASP A OD1 1 
ATOM   768  O  OD2 . ASP A 1 110 ? 4.99500   -25.49900 50.62300 1.000 43.36000 ? 104 ASP A OD2 1 
ATOM   769  N  N   . LEU A 1 111 ? 8.13800   -22.17800 47.59300 1.000 34.48000 ? 105 LEU A N   1 
ATOM   770  C  CA  . LEU A 1 111 ? 8.40100   -21.28200 46.48000 1.000 33.78000 ? 105 LEU A CA  1 
ATOM   771  C  C   . LEU A 1 111 ? 9.76900   -21.53500 45.84000 1.000 35.42000 ? 105 LEU A C   1 
ATOM   772  O  O   . LEU A 1 111 ? 10.76300  -21.79200 46.52400 1.000 35.02000 ? 105 LEU A O   1 
ATOM   773  C  CB  . LEU A 1 111 ? 8.31900   -19.83800 46.96900 1.000 33.66000 ? 105 LEU A CB  1 
ATOM   774  C  CG  . LEU A 1 111 ? 6.89800   -19.38100 47.31700 1.000 37.77000 ? 105 LEU A CG  1 
ATOM   775  C  CD1 . LEU A 1 111 ? 6.90500   -17.94800 47.87300 1.000 35.88000 ? 105 LEU A CD1 1 
ATOM   776  C  CD2 . LEU A 1 111 ? 5.94000   -19.50400 46.10500 1.000 29.41000 ? 105 LEU A CD2 1 
ATOM   777  N  N   . ARG A 1 112 ? 9.82800   -21.42000 44.51300 1.000 30.97000 ? 106 ARG A N   1 
ATOM   778  C  CA  . ARG A 1 112 ? 11.06900  -21.62300 43.77300 1.000 32.16000 ? 106 ARG A CA  1 
ATOM   779  C  C   . ARG A 1 112 ? 11.57500  -20.35100 43.10800 1.000 31.53000 ? 106 ARG A C   1 
ATOM   780  O  O   . ARG A 1 112 ? 12.44800  -20.42600 42.22700 1.000 29.89000 ? 106 ARG A O   1 
ATOM   781  C  CB  . ARG A 1 112 ? 10.89300  -22.71700 42.72500 1.000 31.29000 ? 106 ARG A CB  1 
ATOM   782  C  CG  . ARG A 1 112 ? 10.90400  -24.10700 43.32600 1.000 38.66000 ? 106 ARG A CG  1 
ATOM   783  C  CD  . ARG A 1 112 ? 12.11400  -24.27400 44.22900 1.000 38.21000 ? 106 ARG A CD  1 
ATOM   784  N  NE  . ARG A 1 112 ? 11.98900  -25.52600 44.96200 1.000 47.74000 ? 106 ARG A NE  1 
ATOM   785  C  CZ  . ARG A 1 112 ? 11.77300  -25.61900 46.27100 1.000 51.25000 ? 106 ARG A CZ  1 
ATOM   786  N  NH1 . ARG A 1 112 ? 11.77100  -24.54600 47.05900 1.000 42.67000 ? 106 ARG A NH1 1 
ATOM   787  N  NH2 . ARG A 1 112 ? 11.55400  -26.81900 46.80300 1.000 49.90000 ? 106 ARG A NH2 1 
ATOM   788  N  N   . CYS A 1 113 ? 11.02600  -19.19600 43.47700 1.000 30.25000 ? 107 CYS A N   1 
ATOM   789  C  CA  . CYS A 1 113 ? 11.55700  -17.89700 43.08900 1.000 26.37000 ? 107 CYS A CA  1 
ATOM   790  C  C   . CYS A 1 113 ? 12.41100  -17.33200 44.21400 1.000 32.19000 ? 107 CYS A C   1 
ATOM   791  O  O   . CYS A 1 113 ? 12.34200  -17.77900 45.36900 1.000 30.44000 ? 107 CYS A O   1 
ATOM   792  C  CB  . CYS A 1 113 ? 10.42800  -16.92300 42.76000 1.000 32.85000 ? 107 CYS A CB  1 
ATOM   793  S  SG  . CYS A 1 113 ? 9.05800   -16.85200 44.00100 1.000 32.22000 ? 107 CYS A SG  1 
ATOM   794  N  N   . GLY A 1 114 ? 13.23000  -16.33600 43.86700 1.000 26.17000 ? 108 GLY A N   1 
ATOM   795  C  CA  . GLY A 1 114 ? 14.18000  -15.77600 44.82400 1.000 27.43000 ? 108 GLY A CA  1 
ATOM   796  C  C   . GLY A 1 114 ? 13.92500  -14.29400 45.01400 1.000 31.89000 ? 108 GLY A C   1 
ATOM   797  O  O   . GLY A 1 114 ? 13.31200  -13.64300 44.14500 1.000 28.76000 ? 108 GLY A O   1 
ATOM   798  N  N   . GLY A 1 115 ? 14.35200  -13.73900 46.14300 1.000 28.84000 ? 109 GLY A N   1 
ATOM   799  C  CA  . GLY A 1 115 ? 14.16000  -12.31800 46.36700 1.000 28.11000 ? 109 GLY A CA  1 
ATOM   800  C  C   . GLY A 1 115 ? 15.10400  -11.47900 45.52600 1.000 29.96000 ? 109 GLY A C   1 
ATOM   801  O  O   . GLY A 1 115 ? 16.07800  -11.97300 44.94900 1.000 30.17000 ? 109 GLY A O   1 
ATOM   802  N  N   . HIS A 1 116 ? 14.81900  -10.17500 45.47600 1.000 27.23000 ? 110 HIS A N   1 
ATOM   803  C  CA  . HIS A 1 116 ? 15.59700  -9.24000  44.67000 1.000 28.88000 ? 110 HIS A CA  1 
ATOM   804  C  C   . HIS A 1 116 ? 15.27700  -7.82600  45.13100 1.000 27.60000 ? 110 HIS A C   1 
ATOM   805  O  O   . HIS A 1 116 ? 14.24100  -7.60000  45.76200 1.000 25.92000 ? 110 HIS A O   1 
ATOM   806  C  CB  . HIS A 1 116 ? 15.25400  -9.39200  43.18700 1.000 27.40000 ? 110 HIS A CB  1 
ATOM   807  C  CG  . HIS A 1 116 ? 13.79100  -9.29100  42.93100 1.000 28.56000 ? 110 HIS A CG  1 
ATOM   808  N  ND1 . HIS A 1 116 ? 13.13200  -8.08000  42.90300 1.000 30.58000 ? 110 HIS A ND1 1 
ATOM   809  C  CD2 . HIS A 1 116 ? 12.84400  -10.24400 42.77000 1.000 30.15000 ? 110 HIS A CD2 1 
ATOM   810  C  CE1 . HIS A 1 116 ? 11.84000  -8.28900  42.69500 1.000 33.23000 ? 110 HIS A CE1 1 
ATOM   811  N  NE2 . HIS A 1 116 ? 11.63900  -9.59400  42.60900 1.000 29.38000 ? 110 HIS A NE2 1 
ATOM   812  N  N   . PRO A 1 117 ? 16.11800  -6.84600  44.79000 1.000 30.59000 ? 111 PRO A N   1 
ATOM   813  C  CA  . PRO A 1 117 ? 15.79000  -5.45400  45.13600 1.000 30.33000 ? 111 PRO A CA  1 
ATOM   814  C  C   . PRO A 1 117 ? 14.42500  -5.09000  44.57600 1.000 29.63000 ? 111 PRO A C   1 
ATOM   815  O  O   . PRO A 1 117 ? 14.03600  -5.54700  43.49700 1.000 32.11000 ? 111 PRO A O   1 
ATOM   816  C  CB  . PRO A 1 117 ? 16.91400  -4.64100  44.47700 1.000 28.88000 ? 111 PRO A CB  1 
ATOM   817  C  CG  . PRO A 1 117 ? 18.03700  -5.60600  44.26700 1.000 27.13000 ? 111 PRO A CG  1 
ATOM   818  C  CD  . PRO A 1 117 ? 17.38900  -6.94700  44.04400 1.000 28.65000 ? 111 PRO A CD  1 
ATOM   819  N  N   . SER A 1 118 ? 13.67400  -4.29700  45.33700 1.000 32.80000 ? 112 SER A N   1 
ATOM   820  C  CA  . SER A 1 118 ? 12.30100  -4.01500  44.94600 1.000 29.90000 ? 112 SER A CA  1 
ATOM   821  C  C   . SER A 1 118 ? 12.27100  -3.20400  43.64600 1.000 33.40000 ? 112 SER A C   1 
ATOM   822  O  O   . SER A 1 118 ? 13.17500  -2.40400  43.36300 1.000 30.49000 ? 112 SER A O   1 
ATOM   823  C  CB  . SER A 1 118 ? 11.56600  -3.27500  46.06600 1.000 31.19000 ? 112 SER A CB  1 
ATOM   824  O  OG  . SER A 1 118 ? 10.35900  -2.65600  45.60700 1.000 28.72000 ? 112 SER A OG  1 
ATOM   825  N  N   . LEU A 1 119 ? 11.23000  -3.45300  42.83500 1.000 28.09000 ? 113 LEU A N   1 
ATOM   826  C  CA  . LEU A 1 119 ? 10.94500  -2.62300  41.66600 1.000 26.17000 ? 113 LEU A CA  1 
ATOM   827  C  C   . LEU A 1 119 ? 10.61500  -1.18000  42.03600 1.000 30.74000 ? 113 LEU A C   1 
ATOM   828  O  O   . LEU A 1 119 ? 10.76000  -0.28900  41.19000 1.000 32.92000 ? 113 LEU A O   1 
ATOM   829  C  CB  . LEU A 1 119 ? 9.78300   -3.24000  40.87800 1.000 28.27000 ? 113 LEU A CB  1 
ATOM   830  C  CG  . LEU A 1 119 ? 10.07600  -4.65700  40.37300 1.000 26.02000 ? 113 LEU A CG  1 
ATOM   831  C  CD1 . LEU A 1 119 ? 8.97000   -5.11700  39.45600 1.000 24.06000 ? 113 LEU A CD1 1 
ATOM   832  C  CD2 . LEU A 1 119 ? 11.39000  -4.62800  39.63200 1.000 29.68000 ? 113 LEU A CD2 1 
ATOM   833  N  N   . SER A 1 120 ? 10.17600  -0.92400  43.27000 1.000 31.26000 ? 114 SER A N   1 
ATOM   834  C  CA  . SER A 1 120 ? 9.97600   0.43600   43.76400 1.000 30.29000 ? 114 SER A CA  1 
ATOM   835  C  C   . SER A 1 120 ? 11.22700  0.92100   44.49200 1.000 35.74000 ? 114 SER A C   1 
ATOM   836  O  O   . SER A 1 120 ? 11.67100  0.28400   45.45800 1.000 30.06000 ? 114 SER A O   1 
ATOM   837  C  CB  . SER A 1 120 ? 8.78200   0.50900   44.71300 1.000 33.10000 ? 114 SER A CB  1 
ATOM   838  O  OG  . SER A 1 120 ? 8.89700   1.67300   45.55300 1.000 36.12000 ? 114 SER A OG  1 
ATOM   839  N  N   . GLU A 1 121 ? 11.77800  2.06200   44.03800 1.000 37.07000 ? 115 GLU A N   1 
ATOM   840  C  CA  . GLU A 1 121 ? 12.94400  2.66200   44.69000 1.000 36.75000 ? 115 GLU A CA  1 
ATOM   841  C  C   . GLU A 1 121 ? 12.64300  3.01500   46.14300 1.000 40.13000 ? 115 GLU A C   1 
ATOM   842  O  O   . GLU A 1 121 ? 13.47500  2.80800   47.03400 1.000 36.82000 ? 115 GLU A O   1 
ATOM   843  C  CB  . GLU A 1 121 ? 13.39900  3.91100   43.92200 1.000 43.26000 ? 115 GLU A CB  1 
ATOM   844  C  CG  . GLU A 1 121 ? 14.53100  3.68600   42.92400 1.000 51.67000 ? 115 GLU A CG  1 
ATOM   845  C  CD  . GLU A 1 121 ? 15.53600  4.84900   42.90000 1.000 71.92000 ? 115 GLU A CD  1 
ATOM   846  O  OE1 . GLU A 1 121 ? 16.04800  5.23700   43.98700 1.000 71.15000 ? 115 GLU A OE1 1 
ATOM   847  O  OE2 . GLU A 1 121 ? 15.81000  5.38400   41.79600 1.000 73.45000 ? 115 GLU A OE2 1 
ATOM   848  N  N   . MET A 1 122 ? 11.45000  3.54000   46.40200 1.000 38.92000 ? 116 MET A N   1 
ATOM   849  C  CA  . MET A 1 122 ? 11.10200  3.91700   47.76300 1.000 40.04000 ? 116 MET A CA  1 
ATOM   850  C  C   . MET A 1 122 ? 11.03800  2.70600   48.68600 1.000 39.29000 ? 116 MET A C   1 
ATOM   851  O  O   . MET A 1 122 ? 11.48600  2.77500   49.83500 1.000 35.68000 ? 116 MET A O   1 
ATOM   852  C  CB  . MET A 1 122 ? 9.77800   4.65200   47.76000 1.000 40.95000 ? 116 MET A CB  1 
ATOM   853  C  CG  . MET A 1 122 ? 9.37600   5.08900   49.11100 1.000 41.90000 ? 116 MET A CG  1 
ATOM   854  S  SD  . MET A 1 122 ? 7.96300   6.15400   48.91200 1.000 50.43000 ? 116 MET A SD  1 
ATOM   855  C  CE  . MET A 1 122 ? 8.73100   7.49800   47.98500 1.000 48.61000 ? 116 MET A CE  1 
ATOM   856  N  N   . VAL A 1 123 ? 10.47100  1.59500   48.20800 1.000 36.58000 ? 117 VAL A N   1 
ATOM   857  C  CA  . VAL A 1 123 ? 10.42300  0.37000   49.00700 1.000 34.72000 ? 117 VAL A CA  1 
ATOM   858  C  C   . VAL A 1 123 ? 11.82700  -0.11700  49.30500 1.000 32.91000 ? 117 VAL A C   1 
ATOM   859  O  O   . VAL A 1 123 ? 12.13000  -0.55000  50.42100 1.000 35.57000 ? 117 VAL A O   1 
ATOM   860  C  CB  . VAL A 1 123 ? 9.62800   -0.73300  48.28600 1.000 36.02000 ? 117 VAL A CB  1 
ATOM   861  C  CG1 . VAL A 1 123 ? 9.74000   -2.06300  49.08600 1.000 29.22000 ? 117 VAL A CG1 1 
ATOM   862  C  CG2 . VAL A 1 123 ? 8.17700   -0.33100  48.06300 1.000 30.68000 ? 117 VAL A CG2 1 
ATOM   863  N  N   . ASN A 1 124 ? 12.69100  -0.10400  48.28600 1.000 35.47000 ? 118 ASN A N   1 
ATOM   864  C  CA  . ASN A 1 124 ? 14.04600  -0.62700  48.43500 1.000 33.42000 ? 118 ASN A CA  1 
ATOM   865  C  C   . ASN A 1 124 ? 14.86600  0.21100   49.41100 1.000 34.27000 ? 118 ASN A C   1 
ATOM   866  O  O   . ASN A 1 124 ? 15.67900  -0.33300  50.16800 1.000 32.07000 ? 118 ASN A O   1 
ATOM   867  C  CB  . ASN A 1 124 ? 14.73400  -0.68800  47.06900 1.000 34.96000 ? 118 ASN A CB  1 
ATOM   868  C  CG  . ASN A 1 124 ? 15.82200  -1.74000  47.02100 1.000 34.94000 ? 118 ASN A CG  1 
ATOM   869  O  OD1 . ASN A 1 124 ? 15.54900  -2.92200  47.23600 1.000 35.93000 ? 118 ASN A OD1 1 
ATOM   870  N  ND2 . ASN A 1 124 ? 17.05600  -1.32300  46.73200 1.000 31.68000 ? 118 ASN A ND2 1 
ATOM   871  N  N   . ARG A 1 125 ? 14.70500  1.54300   49.38300 1.000 35.77000 ? 119 ARG A N   1 
ATOM   872  C  CA  . ARG A 1 125 ? 15.40900  2.38600   50.35000 1.000 35.31000 ? 119 ARG A CA  1 
ATOM   873  C  C   . ARG A 1 125 ? 14.93300  2.09500   51.77000 1.000 34.83000 ? 119 ARG A C   1 
ATOM   874  O  O   . ARG A 1 125 ? 15.72200  2.14400   52.72900 1.000 36.51000 ? 119 ARG A O   1 
ATOM   875  C  CB  . ARG A 1 125 ? 15.21900  3.87500   50.01700 1.000 39.03000 ? 119 ARG A CB  1 
ATOM   876  C  CG  . ARG A 1 125 ? 15.92100  4.36200   48.72200 1.000 41.29000 ? 119 ARG A CG  1 
ATOM   877  C  CD  . ARG A 1 125 ? 15.98100  5.91400   48.64800 1.000 46.68000 ? 119 ARG A CD  1 
ATOM   878  N  NE  . ARG A 1 125 ? 14.69100  6.50600   48.99500 1.000 53.31000 ? 119 ARG A NE  1 
ATOM   879  C  CZ  . ARG A 1 125 ? 13.74400  6.82800   48.12000 1.000 56.44000 ? 119 ARG A CZ  1 
ATOM   880  N  NH1 . ARG A 1 125 ? 13.94500  6.72700   46.81000 1.000 53.04000 ? 119 ARG A NH1 1 
ATOM   881  N  NH2 . ARG A 1 125 ? 12.56000  7.25300   48.56900 1.000 56.40000 ? 119 ARG A NH2 1 
ATOM   882  N  N   . SER A 1 126 ? 13.63200  1.84200   51.92500 1.000 36.79000 ? 120 SER A N   1 
ATOM   883  C  CA  . SER A 1 126 ? 13.07900  1.39900   53.20200 1.000 38.05000 ? 120 SER A CA  1 
ATOM   884  C  C   . SER A 1 126 ? 13.72700  0.08700   53.65500 1.000 35.58000 ? 120 SER A C   1 
ATOM   885  O  O   . SER A 1 126 ? 14.10700  -0.06500  54.82100 1.000 32.21000 ? 120 SER A O   1 
ATOM   886  C  CB  . SER A 1 126 ? 11.55400  1.25100   53.05400 1.000 38.72000 ? 120 SER A CB  1 
ATOM   887  O  OG  . SER A 1 126 ? 10.90500  1.00700   54.28500 1.000 42.10000 ? 120 SER A OG  1 
ATOM   888  N  N   . TRP A 1 127 ? 13.87100  -0.87000  52.73500 1.000 32.57000 ? 121 TRP A N   1 
ATOM   889  C  CA  . TRP A 1 127 ? 14.52400  -2.13400  53.07000 1.000 29.93000 ? 121 TRP A CA  1 
ATOM   890  C  C   . TRP A 1 127 ? 15.98000  -1.92700  53.45200 1.000 31.93000 ? 121 TRP A C   1 
ATOM   891  O  O   . TRP A 1 127 ? 16.47200  -2.54400  54.40300 1.000 29.71000 ? 121 TRP A O   1 
ATOM   892  C  CB  . TRP A 1 127 ? 14.46300  -3.08900  51.89300 1.000 29.21000 ? 121 TRP A CB  1 
ATOM   893  C  CG  . TRP A 1 127 ? 13.15400  -3.66000  51.58200 1.000 35.88000 ? 121 TRP A CG  1 
ATOM   894  C  CD1 . TRP A 1 127 ? 11.97400  -3.49000  52.26700 1.000 36.43000 ? 121 TRP A CD1 1 
ATOM   895  C  CD2 . TRP A 1 127 ? 12.86500  -4.54600  50.49100 1.000 34.84000 ? 121 TRP A CD2 1 
ATOM   896  N  NE1 . TRP A 1 127 ? 10.97400  -4.22100  51.66300 1.000 34.74000 ? 121 TRP A NE1 1 
ATOM   897  C  CE2 . TRP A 1 127 ? 11.49200  -4.86500  50.56600 1.000 32.42000 ? 121 TRP A CE2 1 
ATOM   898  C  CE3 . TRP A 1 127 ? 13.63600  -5.09300  49.45400 1.000 32.33000 ? 121 TRP A CE3 1 
ATOM   899  C  CZ2 . TRP A 1 127 ? 10.87100  -5.71300  49.64600 1.000 31.85000 ? 121 TRP A CZ2 1 
ATOM   900  C  CZ3 . TRP A 1 127 ? 13.01300  -5.94300  48.54400 1.000 31.51000 ? 121 TRP A CZ3 1 
ATOM   901  C  CH2 . TRP A 1 127 ? 11.64700  -6.24400  48.65500 1.000 27.31000 ? 121 TRP A CH2 1 
ATOM   902  N  N   . ILE A 1 128 ? 16.70200  -1.09400  52.69000 1.000 32.84000 ? 122 ILE A N   1 
ATOM   903  C  CA  . ILE A 1 128 ? 18.11500  -0.86800  52.97000 1.000 36.55000 ? 122 ILE A CA  1 
ATOM   904  C  C   . ILE A 1 128 ? 18.27500  -0.22100  54.33200 1.000 33.35000 ? 122 ILE A C   1 
ATOM   905  O  O   . ILE A 1 128 ? 19.15000  -0.60500  55.12200 1.000 35.94000 ? 122 ILE A O   1 
ATOM   906  C  CB  . ILE A 1 128 ? 18.75600  -0.01200  51.85700 1.000 33.77000 ? 122 ILE A CB  1 
ATOM   907  C  CG1 . ILE A 1 128 ? 18.94900  -0.86200  50.59700 1.000 36.00000 ? 122 ILE A CG1 1 
ATOM   908  C  CG2 . ILE A 1 128 ? 20.06000  0.65700   52.35200 1.000 33.71000 ? 122 ILE A CG2 1 
ATOM   909  C  CD1 . ILE A 1 128 ? 19.14800  -0.04200  49.31500 1.000 38.25000 ? 122 ILE A CD1 1 
ATOM   910  N  N   . LYS A 1 129 ? 17.40800  0.75300   54.64100 1.000 33.53000 ? 123 LYS A N   1 
ATOM   911  C  CA  . LYS A 1 129 ? 17.45400  1.41600   55.94000 1.000 34.68000 ? 123 LYS A CA  1 
ATOM   912  C  C   . LYS A 1 129 ? 17.28900  0.40900   57.07600 1.000 36.55000 ? 123 LYS A C   1 
ATOM   913  O  O   . LYS A 1 129 ? 17.82600  0.61900   58.17300 1.000 37.63000 ? 123 LYS A O   1 
ATOM   914  C  CB  . LYS A 1 129 ? 16.36600  2.51100   56.03100 1.000 33.61000 ? 123 LYS A CB  1 
ATOM   915  C  CG  . LYS A 1 129 ? 16.48300  3.37600   57.27300 1.000 37.38000 ? 123 LYS A CG  1 
ATOM   916  C  CD  . LYS A 1 129 ? 15.35000  4.40000   57.42900 1.000 39.71000 ? 123 LYS A CD  1 
ATOM   917  C  CE  . LYS A 1 129 ? 15.51500  5.16800   58.75300 1.000 46.90000 ? 123 LYS A CE  1 
ATOM   918  N  NZ  . LYS A 1 129 ? 14.43100  6.17000   59.01100 1.000 46.87000 ? 123 LYS A NZ  1 
ATOM   919  N  N   . GLN A 1 130 ? 16.56900  -0.69000  56.83200 1.000 33.84000 ? 124 GLN A N   1 
ATOM   920  C  CA  . GLN A 1 130 ? 16.24700  -1.65600  57.87600 1.000 34.48000 ? 124 GLN A CA  1 
ATOM   921  C  C   . GLN A 1 130 ? 17.05000  -2.94600  57.75800 1.000 34.08000 ? 124 GLN A C   1 
ATOM   922  O  O   . GLN A 1 130 ? 16.77700  -3.89800  58.49700 1.000 31.17000 ? 124 GLN A O   1 
ATOM   923  C  CB  . GLN A 1 130 ? 14.74500  -1.94900  57.86300 1.000 33.63000 ? 124 GLN A CB  1 
ATOM   924  C  CG  . GLN A 1 130 ? 13.92600  -0.65300  58.03500 1.000 36.41000 ? 124 GLN A CG  1 
ATOM   925  C  CD  . GLN A 1 130 ? 12.42900  -0.84800  57.76000 1.000 41.41000 ? 124 GLN A CD  1 
ATOM   926  O  OE1 . GLN A 1 130 ? 11.95900  -0.67000  56.62800 1.000 43.28000 ? 124 GLN A OE1 1 
ATOM   927  N  NE2 . GLN A 1 130 ? 11.67800  -1.21400  58.79600 1.000 34.22000 ? 124 GLN A NE2 1 
ATOM   928  N  N   . ASP A 1 131 ? 18.04800  -2.98800  56.86900 1.000 33.43000 ? 125 ASP A N   1 
ATOM   929  C  CA  . ASP A 1 131 ? 18.92000  -4.16100  56.69900 1.000 38.13000 ? 125 ASP A CA  1 
ATOM   930  C  C   . ASP A 1 131 ? 18.11500  -5.40800  56.34100 1.000 38.17000 ? 125 ASP A C   1 
ATOM   931  O  O   . ASP A 1 131 ? 18.45400  -6.53000  56.75500 1.000 34.62000 ? 125 ASP A O   1 
ATOM   932  C  CB  . ASP A 1 131 ? 19.77400  -4.42800  57.95100 1.000 40.04000 ? 125 ASP A CB  1 
ATOM   933  C  CG  . ASP A 1 131 ? 20.86000  -3.35700  58.18900 1.000 45.00000 ? 125 ASP A CG  1 
ATOM   934  O  OD1 . ASP A 1 131 ? 21.55000  -2.95200  57.22000 1.000 50.95000 ? 125 ASP A OD1 1 
ATOM   935  O  OD2 . ASP A 1 131 ? 21.04800  -2.93900  59.36000 1.000 49.20000 ? 125 ASP A OD2 1 
ATOM   936  N  N   . PHE A 1 132 ? 17.04100  -5.22400  55.57300 1.000 33.72000 ? 126 PHE A N   1 
ATOM   937  C  CA  . PHE A 1 132 ? 16.14400  -6.32000  55.22200 1.000 33.02000 ? 126 PHE A CA  1 
ATOM   938  C  C   . PHE A 1 132 ? 16.66100  -7.05600  53.99500 1.000 33.18000 ? 126 PHE A C   1 
ATOM   939  O  O   . PHE A 1 132 ? 16.95600  -6.43100  52.96800 1.000 33.03000 ? 126 PHE A O   1 
ATOM   940  C  CB  . PHE A 1 132 ? 14.73500  -5.80200  54.95700 1.000 31.69000 ? 126 PHE A CB  1 
ATOM   941  C  CG  . PHE A 1 132 ? 13.77600  -6.86700  54.50900 1.000 34.46000 ? 126 PHE A CG  1 
ATOM   942  C  CD1 . PHE A 1 132 ? 13.35100  -7.86400  55.39300 1.000 32.99000 ? 126 PHE A CD1 1 
ATOM   943  C  CD2 . PHE A 1 132 ? 13.30300  -6.88700  53.19500 1.000 32.66000 ? 126 PHE A CD2 1 
ATOM   944  C  CE1 . PHE A 1 132 ? 12.46500  -8.85300  54.97100 1.000 36.09000 ? 126 PHE A CE1 1 
ATOM   945  C  CE2 . PHE A 1 132 ? 12.42300  -7.88000  52.76600 1.000 32.17000 ? 126 PHE A CE2 1 
ATOM   946  C  CZ  . PHE A 1 132 ? 12.00200  -8.86300  53.65000 1.000 29.89000 ? 126 PHE A CZ  1 
ATOM   947  N  N   . ILE A 1 133 ? 16.77800  -8.37600  54.11000 1.000 30.12000 ? 127 ILE A N   1 
ATOM   948  C  CA  . ILE A 1 133 ? 17.16400  -9.24000  52.99600 1.000 35.03000 ? 127 ILE A CA  1 
ATOM   949  C  C   . ILE A 1 133 ? 15.88700  -9.84400  52.41200 1.000 32.84000 ? 127 ILE A C   1 
ATOM   950  O  O   . ILE A 1 133 ? 15.23300  -10.66200 53.09000 1.000 30.19000 ? 127 ILE A O   1 
ATOM   951  C  CB  . ILE A 1 133 ? 18.13400  -10.34500 53.42800 1.000 36.41000 ? 127 ILE A CB  1 
ATOM   952  C  CG1 . ILE A 1 133 ? 19.27000  -9.77900  54.27200 1.000 36.89000 ? 127 ILE A CG1 1 
ATOM   953  C  CG2 . ILE A 1 133 ? 18.67200  -11.03400 52.19800 1.000 32.70000 ? 127 ILE A CG2 1 
ATOM   954  C  CD1 . ILE A 1 133 ? 20.17600  -8.85000  53.51800 1.000 39.81000 ? 127 ILE A CD1 1 
ATOM   955  N  N   . PRO A 1 134 ? 15.48200  -9.46500  51.19400 1.000 31.03000 ? 128 PRO A N   1 
ATOM   956  C  CA  . PRO A 1 134 ? 14.24700  -10.02600 50.62200 1.000 30.63000 ? 128 PRO A CA  1 
ATOM   957  C  C   . PRO A 1 134 ? 14.36800  -11.53000 50.41300 1.000 34.63000 ? 128 PRO A C   1 
ATOM   958  O  O   . PRO A 1 134 ? 15.43800  -12.04100 50.07400 1.000 32.79000 ? 128 PRO A O   1 
ATOM   959  C  CB  . PRO A 1 134 ? 14.09600  -9.28300  49.28300 1.000 29.24000 ? 128 PRO A CB  1 
ATOM   960  C  CG  . PRO A 1 134 ? 15.48000  -8.79500  48.93400 1.000 29.45000 ? 128 PRO A CG  1 
ATOM   961  C  CD  . PRO A 1 134 ? 16.17600  -8.54300  50.26400 1.000 31.52000 ? 128 PRO A CD  1 
ATOM   962  N  N   . THR A 1 135 ? 13.25400  -12.23900 50.62400 1.000 34.61000 ? 129 THR A N   1 
ATOM   963  C  CA  . THR A 1 135 ? 13.18900  -13.68600 50.44300 1.000 35.75000 ? 129 THR A CA  1 
ATOM   964  C  C   . THR A 1 135 ? 12.22500  -14.03600 49.31300 1.000 29.43000 ? 129 THR A C   1 
ATOM   965  O  O   . THR A 1 135 ? 11.68000  -13.15600 48.63700 1.000 29.84000 ? 129 THR A O   1 
ATOM   966  C  CB  . THR A 1 135 ? 12.77200  -14.36400 51.74200 1.000 32.69000 ? 129 THR A CB  1 
ATOM   967  O  OG1 . THR A 1 135 ? 11.54800  -13.77400 52.19200 1.000 33.73000 ? 129 THR A OG1 1 
ATOM   968  C  CG2 . THR A 1 135 ? 13.82600  -14.14600 52.76000 1.000 34.59000 ? 129 THR A CG2 1 
ATOM   969  N  N   . ALA A 1 136 ? 11.98800  -15.34200 49.14000 1.000 29.80000 ? 130 ALA A N   1 
ATOM   970  C  CA  . ALA A 1 136 ? 11.15900  -15.81100 48.02800 1.000 32.78000 ? 130 ALA A CA  1 
ATOM   971  C  C   . ALA A 1 136 ? 9.78800   -15.14000 48.00700 1.000 30.52000 ? 130 ALA A C   1 
ATOM   972  O  O   . ALA A 1 136 ? 9.26700   -14.79400 46.93600 1.000 27.28000 ? 130 ALA A O   1 
ATOM   973  C  CB  . ALA A 1 136 ? 11.01100  -17.33300 48.09700 1.000 29.54000 ? 130 ALA A CB  1 
ATOM   974  N  N   . VAL A 1 137 ? 9.19500   -14.92100 49.18200 1.000 29.73000 ? 131 VAL A N   1 
ATOM   975  C  CA  . VAL A 1 137 ? 7.85500   -14.34300 49.24600 1.000 31.00000 ? 131 VAL A CA  1 
ATOM   976  C  C   . VAL A 1 137 ? 7.82900   -12.88700 48.79200 1.000 31.60000 ? 131 VAL A C   1 
ATOM   977  O  O   . VAL A 1 137 ? 6.74100   -12.32800 48.53900 1.000 31.92000 ? 131 VAL A O   1 
ATOM   978  C  CB  . VAL A 1 137 ? 7.33600   -14.52900 50.69100 1.000 37.71000 ? 131 VAL A CB  1 
ATOM   979  C  CG1 . VAL A 1 137 ? 7.94300   -13.47300 51.63500 1.000 33.15000 ? 131 VAL A CG1 1 
ATOM   980  C  CG2 . VAL A 1 137 ? 5.81100   -14.55200 50.75800 1.000 34.14000 ? 131 VAL A CG2 1 
ATOM   981  N  N   . CYS A 1 138 ? 8.99800   -12.25600 48.67300 1.000 26.99000 ? 132 CYS A N   1 
ATOM   982  C  CA  . CYS A 1 138 ? 9.08300   -10.86600 48.24300 1.000 27.73000 ? 132 CYS A CA  1 
ATOM   983  C  C   . CYS A 1 138 ? 9.24600   -10.72200 46.74500 1.000 26.47000 ? 132 CYS A C   1 
ATOM   984  O  O   . CYS A 1 138 ? 9.19600   -9.59200  46.24200 1.000 30.41000 ? 132 CYS A O   1 
ATOM   985  C  CB  . CYS A 1 138 ? 10.25900  -10.17200 48.91600 1.000 27.37000 ? 132 CYS A CB  1 
ATOM   986  S  SG  . CYS A 1 138 ? 10.24600  -10.25900 50.69500 1.000 35.54000 ? 132 CYS A SG  1 
ATOM   987  N  N   . SER A 1 139 ? 9.49500   -11.82000 46.04100 1.000 22.11000 ? 133 SER A N   1 
ATOM   988  C  CA  . SER A 1 139 ? 9.66400   -11.78000 44.59200 1.000 28.59000 ? 133 SER A CA  1 
ATOM   989  C  C   . SER A 1 139 ? 8.47400   -11.09700 43.93700 1.000 25.79000 ? 133 SER A C   1 
ATOM   990  O  O   . SER A 1 139 ? 7.32000   -11.31000 44.31800 1.000 25.17000 ? 133 SER A O   1 
ATOM   991  C  CB  . SER A 1 139 ? 9.83700   -13.20500 44.02900 1.000 28.68000 ? 133 SER A CB  1 
ATOM   992  O  OG  . SER A 1 139 ? 9.35700   -13.32300 42.69700 1.000 30.73000 ? 133 SER A OG  1 
ATOM   993  N  N   . ASN A 1 140 ? 8.77100   -10.23700 42.96200 1.000 25.14000 ? 134 ASN A N   1 
ATOM   994  C  CA  . ASN A 1 140 ? 7.71800   -9.51900  42.25700 1.000 26.21000 ? 134 ASN A CA  1 
ATOM   995  C  C   . ASN A 1 140 ? 6.76600   -10.48000 41.55200 1.000 28.11000 ? 134 ASN A C   1 
ATOM   996  O  O   . ASN A 1 140 ? 5.64100   -10.09300 41.20100 1.000 26.01000 ? 134 ASN A O   1 
ATOM   997  C  CB  . ASN A 1 140 ? 8.35100   -8.54300  41.26300 1.000 24.85000 ? 134 ASN A CB  1 
ATOM   998  C  CG  . ASN A 1 140 ? 8.86100   -9.24400  39.99900 1.000 33.15000 ? 134 ASN A CG  1 
ATOM   999  O  OD1 . ASN A 1 140 ? 8.15900   -9.29300  38.98200 1.000 36.97000 ? 134 ASN A OD1 1 
ATOM   1000 N  ND2 . ASN A 1 140 ? 10.06300  -9.80300  40.06200 1.000 29.99000 ? 134 ASN A ND2 1 
ATOM   1001 N  N   . CYS A 1 141 ? 7.19200   -11.72800 41.35300 1.000 23.31000 ? 135 CYS A N   1 
ATOM   1002 C  CA  . CYS A 1 141 ? 6.39500   -12.77000 40.73200 1.000 27.51000 ? 135 CYS A CA  1 
ATOM   1003 C  C   . CYS A 1 141 ? 5.86900   -13.78700 41.74300 1.000 23.25000 ? 135 CYS A C   1 
ATOM   1004 O  O   . CYS A 1 141 ? 5.40700   -14.85200 41.34300 1.000 23.74000 ? 135 CYS A O   1 
ATOM   1005 C  CB  . CYS A 1 141 ? 7.22500   -13.47600 39.65900 1.000 26.10000 ? 135 CYS A CB  1 
ATOM   1006 S  SG  . CYS A 1 141 ? 8.06800   -12.35400 38.51600 1.000 34.30000 ? 135 CYS A SG  1 
ATOM   1007 N  N   . SER A 1 142 ? 5.91700   -13.47700 43.03700 1.000 21.86000 ? 136 SER A N   1 
ATOM   1008 C  CA  . SER A 1 142 ? 5.47600   -14.43000 44.05400 1.000 23.83000 ? 136 SER A CA  1 
ATOM   1009 C  C   . SER A 1 142 ? 4.04900   -14.91500 43.81700 1.000 26.39000 ? 136 SER A C   1 
ATOM   1010 O  O   . SER A 1 142 ? 3.76700   -16.10700 43.97600 1.000 27.66000 ? 136 SER A O   1 
ATOM   1011 C  CB  . SER A 1 142 ? 5.57800   -13.81500 45.45200 1.000 24.66000 ? 136 SER A CB  1 
ATOM   1012 O  OG  . SER A 1 142 ? 4.68600   -12.69700 45.60500 1.000 26.72000 ? 136 SER A OG  1 
ATOM   1013 N  N   . GLY A 1 143 ? 3.12400   -14.00500 43.48600 1.000 26.44000 ? 137 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 143 ? 1.73700   -14.41600 43.31500 1.000 24.38000 ? 137 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 143 ? 1.57100   -15.39700 42.17100 1.000 24.35000 ? 137 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 143 ? 0.75800   -16.31100 42.23400 1.000 24.44000 ? 137 GLY A O   1 
ATOM   1017 N  N   . HIS A 1 144 ? 2.36200   -15.22100 41.11400 1.000 26.48000 ? 138 HIS A N   1 
ATOM   1018 C  CA  . HIS A 1 144 ? 2.36500   -16.16200 40.00100 1.000 26.87000 ? 138 HIS A CA  1 
ATOM   1019 C  C   . HIS A 1 144 ? 2.87600   -17.53400 40.42700 1.000 27.09000 ? 138 HIS A C   1 
ATOM   1020 O  O   . HIS A 1 144 ? 2.28400   -18.57300 40.08700 1.000 25.33000 ? 138 HIS A O   1 
ATOM   1021 C  CB  . HIS A 1 144 ? 3.23000   -15.59400 38.88800 1.000 27.19000 ? 138 HIS A CB  1 
ATOM   1022 C  CG  . HIS A 1 144 ? 3.13000   -16.36700 37.62400 1.000 31.53000 ? 138 HIS A CG  1 
ATOM   1023 N  ND1 . HIS A 1 144 ? 2.04400   -16.25800 36.77800 1.000 34.53000 ? 138 HIS A ND1 1 
ATOM   1024 C  CD2 . HIS A 1 144 ? 3.95500   -17.28400 37.07500 1.000 29.04000 ? 138 HIS A CD2 1 
ATOM   1025 C  CE1 . HIS A 1 144 ? 2.21600   -17.06900 35.75000 1.000 32.21000 ? 138 HIS A CE1 1 
ATOM   1026 N  NE2 . HIS A 1 144 ? 3.36300   -17.70600 35.90900 1.000 35.09000 ? 138 HIS A NE2 1 
ATOM   1027 N  N   . HIS A 1 145 ? 3.96700   -17.55600 41.19400 1.000 25.19000 ? 139 HIS A N   1 
ATOM   1028 C  CA  . HIS A 1 145 ? 4.49500   -18.81400 41.71200 1.000 26.19000 ? 139 HIS A CA  1 
ATOM   1029 C  C   . HIS A 1 145 ? 3.50600   -19.51900 42.62100 1.000 26.97000 ? 139 HIS A C   1 
ATOM   1030 O  O   . HIS A 1 145 ? 3.47200   -20.75900 42.66700 1.000 25.06000 ? 139 HIS A O   1 
ATOM   1031 C  CB  . HIS A 1 145 ? 5.79100   -18.55500 42.46300 1.000 24.29000 ? 139 HIS A CB  1 
ATOM   1032 C  CG  . HIS A 1 145 ? 6.96000   -18.44400 41.55600 1.000 26.50000 ? 139 HIS A CG  1 
ATOM   1033 N  ND1 . HIS A 1 145 ? 7.89400   -19.44800 41.42300 1.000 26.65000 ? 139 HIS A ND1 1 
ATOM   1034 C  CD2 . HIS A 1 145 ? 7.32200   -17.46800 40.69000 1.000 27.84000 ? 139 HIS A CD2 1 
ATOM   1035 C  CE1 . HIS A 1 145 ? 8.80000   -19.08200 40.53100 1.000 31.07000 ? 139 HIS A CE1 1 
ATOM   1036 N  NE2 . HIS A 1 145 ? 8.48500   -17.87800 40.08300 1.000 30.23000 ? 139 HIS A NE2 1 
ATOM   1037 N  N   . VAL A 1 146 ? 2.73800   -18.75300 43.40900 1.000 25.67000 ? 140 VAL A N   1 
ATOM   1038 C  CA  . VAL A 1 146 ? 1.75900   -19.40500 44.26600 1.000 26.89000 ? 140 VAL A CA  1 
ATOM   1039 C  C   . VAL A 1 146 ? 0.67100   -20.01500 43.40500 1.000 26.57000 ? 140 VAL A C   1 
ATOM   1040 O  O   . VAL A 1 146 ? 0.17400   -21.11400 43.68900 1.000 28.06000 ? 140 VAL A O   1 
ATOM   1041 C  CB  . VAL A 1 146 ? 1.17800   -18.43300 45.31300 1.000 26.23000 ? 140 VAL A CB  1 
ATOM   1042 C  CG1 . VAL A 1 146 ? 0.02900   -19.12100 46.07500 1.000 28.31000 ? 140 VAL A CG1 1 
ATOM   1043 C  CG2 . VAL A 1 146 ? 2.26200   -17.96000 46.29200 1.000 25.73000 ? 140 VAL A CG2 1 
ATOM   1044 N  N   . GLY A 1 147 ? 0.30600   -19.32600 42.32000 1.000 24.32000 ? 141 GLY A N   1 
ATOM   1045 C  CA  . GLY A 1 147 ? -0.61900  -19.91100 41.35900 1.000 23.13000 ? 141 GLY A CA  1 
ATOM   1046 C  C   . GLY A 1 147 ? -0.10800  -21.21300 40.76000 1.000 24.17000 ? 141 GLY A C   1 
ATOM   1047 O  O   . GLY A 1 147 ? -0.86400  -22.17400 40.60200 1.000 27.62000 ? 141 GLY A O   1 
ATOM   1048 N  N   . MET A 1 148 ? 1.17000   -21.25400 40.38500 1.000 23.78000 ? 142 MET A N   1 
ATOM   1049 C  CA  . MET A 1 148 ? 1.72600   -22.47700 39.82000 1.000 22.63000 ? 142 MET A CA  1 
ATOM   1050 C  C   . MET A 1 148 ? 1.72900   -23.59600 40.85400 1.000 26.10000 ? 142 MET A C   1 
ATOM   1051 O  O   . MET A 1 148 ? 1.38800   -24.73900 40.54200 1.000 28.08000 ? 142 MET A O   1 
ATOM   1052 C  CB  . MET A 1 148 ? 3.13600   -22.22000 39.28800 1.000 22.71000 ? 142 MET A CB  1 
ATOM   1053 C  CG  . MET A 1 148 ? 3.20300   -21.22300 38.14600 1.000 28.90000 ? 142 MET A CG  1 
ATOM   1054 S  SD  . MET A 1 148 ? 2.43600   -21.88700 36.63700 1.000 32.99000 ? 142 MET A SD  1 
ATOM   1055 C  CE  . MET A 1 148 ? 3.32700   -23.40800 36.57800 1.000 35.39000 ? 142 MET A CE  1 
ATOM   1056 N  N   . LEU A 1 149 ? 2.07300   -23.28400 42.09900 1.000 23.96000 ? 143 LEU A N   1 
ATOM   1057 C  CA  . LEU A 1 149 ? 1.93600   -24.28500 43.15500 1.000 25.98000 ? 143 LEU A CA  1 
ATOM   1058 C  C   . LEU A 1 149 ? 0.50200   -24.79500 43.26000 1.000 29.01000 ? 143 LEU A C   1 
ATOM   1059 O  O   . LEU A 1 149 ? 0.26900   -26.00400 43.42300 1.000 30.33000 ? 143 LEU A O   1 
ATOM   1060 C  CB  . LEU A 1 149 ? 2.37200   -23.68600 44.49400 1.000 26.75000 ? 143 LEU A CB  1 
ATOM   1061 C  CG  . LEU A 1 149 ? 3.87800   -23.55300 44.74300 1.000 32.72000 ? 143 LEU A CG  1 
ATOM   1062 C  CD1 . LEU A 1 149 ? 4.07100   -22.73500 46.01800 1.000 36.60000 ? 143 LEU A CD1 1 
ATOM   1063 C  CD2 . LEU A 1 149 ? 4.57500   -24.92600 44.85200 1.000 32.96000 ? 143 LEU A CD2 1 
ATOM   1064 N  N   . ALA A 1 150 ? -0.47100  -23.87800 43.17900 1.000 31.38000 ? 144 ALA A N   1 
ATOM   1065 C  CA  . ALA A 1 150 ? -1.87900  -24.24500 43.28200 1.000 27.39000 ? 144 ALA A CA  1 
ATOM   1066 C  C   . ALA A 1 150 ? -2.27200  -25.23900 42.19100 1.000 28.80000 ? 144 ALA A C   1 
ATOM   1067 O  O   . ALA A 1 150 ? -2.92800  -26.25500 42.46300 1.000 30.12000 ? 144 ALA A O   1 
ATOM   1068 C  CB  . ALA A 1 150 ? -2.74200  -22.96900 43.22000 1.000 25.07000 ? 144 ALA A CB  1 
ATOM   1069 N  N   . GLY A 1 151 ? -1.89700  -24.95300 40.93800 1.000 27.26000 ? 145 GLY A N   1 
ATOM   1070 C  CA  . GLY A 1 151 ? -2.19900  -25.88400 39.85400 1.000 27.46000 ? 145 GLY A CA  1 
ATOM   1071 C  C   . GLY A 1 151 ? -1.50500  -27.22600 40.02300 1.000 32.76000 ? 145 GLY A C   1 
ATOM   1072 O  O   . GLY A 1 151 ? -2.10200  -28.28000 39.78300 1.000 28.10000 ? 145 GLY A O   1 
ATOM   1073 N  N   . ALA A 1 152 ? -0.23700  -27.20800 40.44300 1.000 28.05000 ? 146 ALA A N   1 
ATOM   1074 C  CA  . ALA A 1 152 ? 0.46500   -28.46200 40.72200 1.000 33.84000 ? 146 ALA A CA  1 
ATOM   1075 C  C   . ALA A 1 152 ? -0.30000  -29.32000 41.72300 1.000 31.04000 ? 146 ALA A C   1 
ATOM   1076 O  O   . ALA A 1 152 ? -0.53400  -30.51600 41.49000 1.000 32.47000 ? 146 ALA A O   1 
ATOM   1077 C  CB  . ALA A 1 152 ? 1.85900   -28.14800 41.24500 1.000 27.99000 ? 146 ALA A CB  1 
ATOM   1078 N  N   . ARG A 1 153 ? -0.68600  -28.72400 42.86300 1.000 32.81000 ? 147 ARG A N   1 
ATOM   1079 C  CA  . ARG A 1 153 ? -1.42300  -29.46000 43.89400 1.000 33.63000 ? 147 ARG A CA  1 
ATOM   1080 C  C   . ARG A 1 153 ? -2.78900  -29.89700 43.39900 1.000 35.04000 ? 147 ARG A C   1 
ATOM   1081 O  O   . ARG A 1 153 ? -3.25800  -30.98200 43.74900 1.000 33.45000 ? 147 ARG A O   1 
ATOM   1082 C  CB  . ARG A 1 153 ? -1.60800  -28.60800 45.15900 1.000 33.17000 ? 147 ARG A CB  1 
ATOM   1083 C  CG  . ARG A 1 153 ? -0.42500  -28.57100 46.08300 1.000 43.33000 ? 147 ARG A CG  1 
ATOM   1084 C  CD  . ARG A 1 153 ? -0.67000  -29.20300 47.45800 1.000 47.03000 ? 147 ARG A CD  1 
ATOM   1085 N  NE  . ARG A 1 153 ? 0.60400   -29.30700 48.17100 1.000 51.28000 ? 147 ARG A NE  1 
ATOM   1086 C  CZ  . ARG A 1 153 ? 1.02800   -28.45900 49.10100 1.000 52.31000 ? 147 ARG A CZ  1 
ATOM   1087 N  NH1 . ARG A 1 153 ? 0.23900   -27.50200 49.57500 1.000 51.45000 ? 147 ARG A NH1 1 
ATOM   1088 N  NH2 . ARG A 1 153 ? 2.27800   -28.56500 49.56000 1.000 50.85000 ? 147 ARG A NH2 1 
ATOM   1089 N  N   . ALA A 1 154 ? -3.45500  -29.04400 42.61100 1.000 32.23000 ? 148 ALA A N   1 
ATOM   1090 C  CA  . ALA A 1 154 ? -4.80700  -29.32800 42.13200 1.000 34.57000 ? 148 ALA A CA  1 
ATOM   1091 C  C   . ALA A 1 154 ? -4.87500  -30.62200 41.30600 1.000 34.56000 ? 148 ALA A C   1 
ATOM   1092 O  O   . ALA A 1 154 ? -5.82700  -31.40100 41.44700 1.000 31.98000 ? 148 ALA A O   1 
ATOM   1093 C  CB  . ALA A 1 154 ? -5.32100  -28.12400 41.32600 1.000 34.30000 ? 148 ALA A CB  1 
ATOM   1094 N  N   . ILE A 1 155 ? -3.88700  -30.87400 40.43600 1.000 33.68000 ? 149 ILE A N   1 
ATOM   1095 C  CA  . ILE A 1 155 ? -3.93000  -32.09700 39.63200 1.000 33.99000 ? 149 ILE A CA  1 
ATOM   1096 C  C   . ILE A 1 155 ? -3.09200  -33.20500 40.26600 1.000 35.11000 ? 149 ILE A C   1 
ATOM   1097 O  O   . ILE A 1 155 ? -2.91300  -34.28100 39.67500 1.000 33.71000 ? 149 ILE A O   1 
ATOM   1098 C  CB  . ILE A 1 155 ? -3.49200  -31.85100 38.17400 1.000 31.67000 ? 149 ILE A CB  1 
ATOM   1099 C  CG1 . ILE A 1 155 ? -2.09100  -31.21900 38.12000 1.000 26.17000 ? 149 ILE A CG1 1 
ATOM   1100 C  CG2 . ILE A 1 155 ? -4.55000  -31.01300 37.43200 1.000 31.93000 ? 149 ILE A CG2 1 
ATOM   1101 C  CD1 . ILE A 1 155 ? -1.54400  -31.11900 36.74100 1.000 31.29000 ? 149 ILE A CD1 1 
ATOM   1102 N  N   . GLY A 1 156 ? -2.61300  -32.98200 41.48900 1.000 34.82000 ? 150 GLY A N   1 
ATOM   1103 C  CA  . GLY A 1 156 ? -1.83700  -34.02300 42.14000 1.000 33.25000 ? 150 GLY A CA  1 
ATOM   1104 C  C   . GLY A 1 156 ? -0.47500  -34.22800 41.51500 1.000 38.11000 ? 150 GLY A C   1 
ATOM   1105 O  O   . GLY A 1 156 ? 0.06800   -35.34200 41.55300 1.000 41.48000 ? 150 GLY A O   1 
ATOM   1106 N  N   . ALA A 1 157 ? 0.07500   -33.18300 40.90200 1.000 37.53000 ? 151 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 157 ? 1.37500   -33.25500 40.24800 1.000 41.62000 ? 151 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 157 ? 2.54800   -33.24400 41.22200 1.000 44.38000 ? 151 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 157 ? 3.64400   -33.68900 40.85600 1.000 46.78000 ? 151 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 157 ? 1.53200   -32.08600 39.28200 1.000 35.17000 ? 151 ALA A CB  1 
ATOM   1111 N  N   . GLY A 1 158 ? 2.36400   -32.73200 42.43500 1.000 37.97000 ? 152 GLY A N   1 
ATOM   1112 C  CA  . GLY A 1 158 ? 3.51000   -32.59300 43.30500 1.000 44.03000 ? 152 GLY A CA  1 
ATOM   1113 C  C   . GLY A 1 158 ? 4.11200   -31.21300 43.14300 1.000 40.25000 ? 152 GLY A C   1 
ATOM   1114 O  O   . GLY A 1 158 ? 4.24400   -30.71300 42.02400 1.000 41.08000 ? 152 GLY A O   1 
ATOM   1115 N  N   . THR A 1 159 ? 4.45600   -30.57700 44.25100 1.000 40.40000 ? 153 THR A N   1 
ATOM   1116 C  CA  . THR A 1 159 ? 4.91400   -29.20300 44.20900 1.000 38.57000 ? 153 THR A CA  1 
ATOM   1117 C  C   . THR A 1 159 ? 6.41100   -29.08700 43.97800 1.000 44.16000 ? 153 THR A C   1 
ATOM   1118 O  O   . THR A 1 159 ? 6.87000   -28.03000 43.53100 1.000 38.74000 ? 153 THR A O   1 
ATOM   1119 C  CB  . THR A 1 159 ? 4.52200   -28.49800 45.50700 1.000 44.57000 ? 153 THR A CB  1 
ATOM   1120 O  OG1 . THR A 1 159 ? 4.93200   -29.29300 46.63200 1.000 44.32000 ? 153 THR A OG1 1 
ATOM   1121 C  CG2 . THR A 1 159 ? 3.01800   -28.31900 45.54000 1.000 42.86000 ? 153 THR A CG2 1 
ATOM   1122 N  N   . ASP A 1 160 ? 7.18500   -30.12400 44.30200 1.000 43.40000 ? 154 ASP A N   1 
ATOM   1123 C  CA  A ASP A 1 160 ? 8.59900   -30.11700 43.96600 0.500 44.75000 ? 154 ASP A CA  1 
ATOM   1124 C  CA  B ASP A 1 160 ? 8.60500   -30.13300 43.96200 0.500 44.75000 ? 154 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 160 ? 8.75100   -30.04500 42.44700 1.000 43.91000 ? 154 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 160 ? 8.16500   -30.85300 41.71100 1.000 43.16000 ? 154 ASP A O   1 
ATOM   1127 C  CB  A ASP A 1 160 ? 9.28200   -31.37000 44.52900 0.500 46.39000 ? 154 ASP A CB  1 
ATOM   1128 C  CB  B ASP A 1 160 ? 9.27200   -31.40600 44.50400 0.500 46.39000 ? 154 ASP A CB  1 
ATOM   1129 C  CG  A ASP A 1 160 ? 9.15600   -31.48600 46.05600 0.500 46.67000 ? 154 ASP A CG  1 
ATOM   1130 C  CG  B ASP A 1 160 ? 10.80800  -31.37700 44.40400 0.500 47.95000 ? 154 ASP A CG  1 
ATOM   1131 O  OD1 A ASP A 1 160 ? 9.12000   -30.44400 46.75300 0.500 45.21000 ? 154 ASP A OD1 1 
ATOM   1132 O  OD1 B ASP A 1 160 ? 11.46200  -30.62200 45.16200 0.500 49.00000 ? 154 ASP A OD1 1 
ATOM   1133 O  OD2 A ASP A 1 160 ? 9.09800   -32.62600 46.55800 0.500 46.39000 ? 154 ASP A OD2 1 
ATOM   1134 O  OD2 B ASP A 1 160 ? 11.36500  -32.13600 43.58200 0.500 46.95000 ? 154 ASP A OD2 1 
ATOM   1135 N  N   . GLY A 1 161 ? 9.50400   -29.05100 41.98000 1.000 41.91000 ? 155 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 161 ? 9.78800   -28.92200 40.56200 1.000 37.86000 ? 155 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 161 ? 8.68000   -28.35300 39.70500 1.000 33.19000 ? 155 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 161 ? 8.68700   -28.57300 38.48800 1.000 30.94000 ? 155 GLY A O   1 
ATOM   1139 N  N   . TYR A 1 162 ? 7.72100   -27.62700 40.29500 1.000 31.86000 ? 156 TYR A N   1 
ATOM   1140 C  CA  . TYR A 1 162 ? 6.64200   -27.02800 39.51600 1.000 31.12000 ? 156 TYR A CA  1 
ATOM   1141 C  C   . TYR A 1 162 ? 7.16500   -26.05700 38.47600 1.000 30.41000 ? 156 TYR A C   1 
ATOM   1142 O  O   . TYR A 1 162 ? 6.45200   -25.74500 37.50800 1.000 26.57000 ? 156 TYR A O   1 
ATOM   1143 C  CB  . TYR A 1 162 ? 5.65600   -26.28600 40.42600 1.000 33.39000 ? 156 TYR A CB  1 
ATOM   1144 C  CG  . TYR A 1 162 ? 6.19700   -25.01200 41.05100 1.000 30.20000 ? 156 TYR A CG  1 
ATOM   1145 C  CD1 . TYR A 1 162 ? 6.85800   -25.04400 42.27500 1.000 31.26000 ? 156 TYR A CD1 1 
ATOM   1146 C  CD2 . TYR A 1 162 ? 6.06300   -23.78200 40.41300 1.000 27.61000 ? 156 TYR A CD2 1 
ATOM   1147 C  CE1 . TYR A 1 162 ? 7.36600   -23.88700 42.85100 1.000 32.30000 ? 156 TYR A CE1 1 
ATOM   1148 C  CE2 . TYR A 1 162 ? 6.56700   -22.61300 40.98900 1.000 25.12000 ? 156 TYR A CE2 1 
ATOM   1149 C  CZ  . TYR A 1 162 ? 7.20900   -22.67800 42.20600 1.000 31.52000 ? 156 TYR A CZ  1 
ATOM   1150 O  OH  . TYR A 1 162 ? 7.71500   -21.52700 42.78400 1.000 32.82000 ? 156 TYR A OH  1 
ATOM   1151 N  N   . HIS A 1 163 ? 8.39900   -25.59500 38.64700 1.000 27.84000 ? 157 HIS A N   1 
ATOM   1152 C  CA  . HIS A 1 163 ? 8.99800   -24.58500 37.79300 1.000 31.85000 ? 157 HIS A CA  1 
ATOM   1153 C  C   . HIS A 1 163 ? 9.82000   -25.16800 36.66000 1.000 32.35000 ? 157 HIS A C   1 
ATOM   1154 O  O   . HIS A 1 163 ? 10.37400  -24.39800 35.87400 1.000 32.85000 ? 157 HIS A O   1 
ATOM   1155 C  CB  . HIS A 1 163 ? 9.89100   -23.68100 38.63000 1.000 27.43000 ? 157 HIS A CB  1 
ATOM   1156 C  CG  . HIS A 1 163 ? 11.04000  -24.40400 39.25600 1.000 35.06000 ? 157 HIS A CG  1 
ATOM   1157 N  ND1 . HIS A 1 163 ? 10.86700  -25.38700 40.20300 1.000 35.73000 ? 157 HIS A ND1 1 
ATOM   1158 C  CD2 . HIS A 1 163 ? 12.37900  -24.28500 39.07500 1.000 34.98000 ? 157 HIS A CD2 1 
ATOM   1159 C  CE1 . HIS A 1 163 ? 12.04800  -25.84800 40.57600 1.000 38.93000 ? 157 HIS A CE1 1 
ATOM   1160 N  NE2 . HIS A 1 163 ? 12.98200  -25.18800 39.91400 1.000 36.42000 ? 157 HIS A NE2 1 
ATOM   1161 N  N   . LEU A 1 164 ? 9.95700   -26.55000 36.58100 1.000 29.47000 ? 158 LEU A N   1 
ATOM   1162 C  CA  . LEU A 1 164 ? 10.80200  -27.14500 35.55800 1.000 29.90000 ? 158 LEU A CA  1 
ATOM   1163 C  C   . LEU A 1 164 ? 9.97900   -27.45900 34.31900 1.000 33.42000 ? 158 LEU A C   1 
ATOM   1164 O  O   . LEU A 1 164 ? 8.77600   -27.71700 34.41800 1.000 35.25000 ? 158 LEU A O   1 
ATOM   1165 C  CB  . LEU A 1 164 ? 11.46300  -28.42000 36.08000 1.000 32.01000 ? 158 LEU A CB  1 
ATOM   1166 C  CG  . LEU A 1 164 ? 12.31100  -28.24400 37.35600 1.000 34.06000 ? 158 LEU A CG  1 
ATOM   1167 C  CD1 . LEU A 1 164 ? 12.87800  -29.57900 37.78100 1.000 42.60000 ? 158 LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A 1 164 ? 13.44100  -27.21900 37.20100 1.000 34.90000 ? 158 LEU A CD2 1 
ATOM   1169 N  N   . PRO A 1 165 ? 10.59700  -27.44600 33.13800 1.000 31.64000 ? 159 PRO A N   1 
ATOM   1170 C  CA  . PRO A 1 165 ? 9.80500   -27.60500 31.90300 1.000 35.13000 ? 159 PRO A CA  1 
ATOM   1171 C  C   . PRO A 1 165 ? 9.09700   -28.94700 31.78500 1.000 39.75000 ? 159 PRO A C   1 
ATOM   1172 O  O   . PRO A 1 165 ? 8.08400   -29.02900 31.07800 1.000 37.56000 ? 159 PRO A O   1 
ATOM   1173 C  CB  . PRO A 1 165 ? 10.85000  -27.43100 30.79800 1.000 30.87000 ? 159 PRO A CB  1 
ATOM   1174 C  CG  . PRO A 1 165 ? 11.85600  -26.53600 31.41500 1.000 36.75000 ? 159 PRO A CG  1 
ATOM   1175 C  CD  . PRO A 1 165 ? 11.94600  -26.92900 32.87000 1.000 28.69000 ? 159 PRO A CD  1 
ATOM   1176 N  N   . ASP A 1 166 ? 9.59800   -30.00600 32.43900 1.000 39.14000 ? 160 ASP A N   1 
ATOM   1177 C  CA  . ASP A 1 166 ? 8.96700   -31.32500 32.34000 1.000 37.80000 ? 160 ASP A CA  1 
ATOM   1178 C  C   . ASP A 1 166 ? 7.82000   -31.53100 33.33000 1.000 34.30000 ? 160 ASP A C   1 
ATOM   1179 O  O   . ASP A 1 166 ? 7.13800   -32.55500 33.23800 1.000 34.99000 ? 160 ASP A O   1 
ATOM   1180 C  CB  . ASP A 1 166 ? 10.00000  -32.43800 32.54700 1.000 44.59000 ? 160 ASP A CB  1 
ATOM   1181 C  CG  . ASP A 1 166 ? 10.62500  -32.92200 31.23800 1.000 62.96000 ? 160 ASP A CG  1 
ATOM   1182 O  OD1 . ASP A 1 166 ? 11.54600  -32.22400 30.74100 1.000 67.60000 ? 160 ASP A OD1 1 
ATOM   1183 O  OD2 . ASP A 1 166 ? 10.21300  -34.00800 30.72200 1.000 64.29000 ? 160 ASP A OD2 1 
ATOM   1184 N  N   . HIS A 1 167 ? 7.61000   -30.61000 34.27200 1.000 30.99000 ? 161 HIS A N   1 
ATOM   1185 C  CA  . HIS A 1 167 ? 6.43700   -30.65400 35.14500 1.000 33.77000 ? 161 HIS A CA  1 
ATOM   1186 C  C   . HIS A 1 167 ? 5.15700   -30.40700 34.35000 1.000 33.16000 ? 161 HIS A C   1 
ATOM   1187 O  O   . HIS A 1 167 ? 5.12200   -29.53200 33.47400 1.000 32.60000 ? 161 HIS A O   1 
ATOM   1188 C  CB  . HIS A 1 167 ? 6.55800   -29.59400 36.23900 1.000 31.41000 ? 161 HIS A CB  1 
ATOM   1189 C  CG  . HIS A 1 167 ? 5.61200   -29.78700 37.37800 1.000 32.80000 ? 161 HIS A CG  1 
ATOM   1190 N  ND1 . HIS A 1 167 ? 4.29400   -29.38800 37.32500 1.000 30.11000 ? 161 HIS A ND1 1 
ATOM   1191 C  CD2 . HIS A 1 167 ? 5.79700   -30.32500 38.60900 1.000 33.65000 ? 161 HIS A CD2 1 
ATOM   1192 C  CE1 . HIS A 1 167 ? 3.70200   -29.68000 38.47100 1.000 33.99000 ? 161 HIS A CE1 1 
ATOM   1193 N  NE2 . HIS A 1 167 ? 4.59500   -30.24200 39.27000 1.000 33.05000 ? 161 HIS A NE2 1 
ATOM   1194 N  N   . PRO A 1 168 ? 4.07800   -31.13200 34.64800 1.000 31.67000 ? 162 PRO A N   1 
ATOM   1195 C  CA  . PRO A 1 168 ? 2.83400   -30.94500 33.87800 1.000 33.70000 ? 162 PRO A CA  1 
ATOM   1196 C  C   . PRO A 1 168 ? 2.31700   -29.51000 33.86000 1.000 30.83000 ? 162 PRO A C   1 
ATOM   1197 O  O   . PRO A 1 168 ? 1.65300   -29.11300 32.88700 1.000 28.90000 ? 162 PRO A O   1 
ATOM   1198 C  CB  . PRO A 1 168 ? 1.83700   -31.87400 34.59100 1.000 27.76000 ? 162 PRO A CB  1 
ATOM   1199 C  CG  . PRO A 1 168 ? 2.67300   -32.86700 35.29900 1.000 30.15000 ? 162 PRO A CG  1 
ATOM   1200 C  CD  . PRO A 1 168 ? 3.97100   -32.21800 35.63800 1.000 28.98000 ? 162 PRO A CD  1 
ATOM   1201 N  N   . MET A 1 169 ? 2.53700   -28.74300 34.93200 1.000 28.08000 ? 163 MET A N   1 
ATOM   1202 C  CA  . MET A 1 169 ? 2.07600   -27.36000 34.92500 1.000 27.55000 ? 163 MET A CA  1 
ATOM   1203 C  C   . MET A 1 169 ? 2.76800   -26.56600 33.83500 1.000 31.01000 ? 163 MET A C   1 
ATOM   1204 O  O   . MET A 1 169 ? 2.11700   -25.79400 33.11500 1.000 28.50000 ? 163 MET A O   1 
ATOM   1205 C  CB  . MET A 1 169 ? 2.31200   -26.69400 36.27700 1.000 30.22000 ? 163 MET A CB  1 
ATOM   1206 C  CG  . MET A 1 169 ? 1.23500   -26.99700 37.27400 1.000 36.94000 ? 163 MET A CG  1 
ATOM   1207 S  SD  . MET A 1 169 ? -0.42500  -26.65600 36.61500 1.000 44.84000 ? 163 MET A SD  1 
ATOM   1208 C  CE  . MET A 1 169 ? -0.26600  -24.91700 36.33000 1.000 25.81000 ? 163 MET A CE  1 
ATOM   1209 N  N   . GLN A 1 170 ? 4.08900   -26.74900 33.69000 1.000 25.53000 ? 164 GLN A N   1 
ATOM   1210 C  CA  . GLN A 1 170 ? 4.80700   -26.05600 32.62400 1.000 30.26000 ? 164 GLN A CA  1 
ATOM   1211 C  C   . GLN A 1 170 ? 4.37500   -26.53700 31.25200 1.000 26.17000 ? 164 GLN A C   1 
ATOM   1212 O  O   . GLN A 1 170 ? 4.30700   -25.74200 30.30700 1.000 28.24000 ? 164 GLN A O   1 
ATOM   1213 C  CB  . GLN A 1 170 ? 6.31100   -26.22700 32.79100 1.000 31.33000 ? 164 GLN A CB  1 
ATOM   1214 C  CG  . GLN A 1 170 ? 6.85600   -25.51700 33.99800 1.000 29.58000 ? 164 GLN A CG  1 
ATOM   1215 C  CD  . GLN A 1 170 ? 6.28900   -24.12300 34.18100 1.000 34.26000 ? 164 GLN A CD  1 
ATOM   1216 O  OE1 . GLN A 1 170 ? 5.82700   -23.78600 35.26800 1.000 35.71000 ? 164 GLN A OE1 1 
ATOM   1217 N  NE2 . GLN A 1 170 ? 6.31500   -23.31100 33.13500 1.000 27.76000 ? 164 GLN A NE2 1 
ATOM   1218 N  N   . GLY A 1 171 ? 4.07000   -27.82100 31.12200 1.000 27.66000 ? 165 GLY A N   1 
ATOM   1219 C  CA  . GLY A 1 171 ? 3.49200   -28.30100 29.87800 1.000 29.11000 ? 165 GLY A CA  1 
ATOM   1220 C  C   . GLY A 1 171 ? 2.21400   -27.56500 29.53400 1.000 29.54000 ? 165 GLY A C   1 
ATOM   1221 O  O   . GLY A 1 171 ? 2.01000   -27.16200 28.37900 1.000 26.96000 ? 165 GLY A O   1 
ATOM   1222 N  N   . ARG A 1 172 ? 1.34600   -27.35300 30.54100 1.000 25.76000 ? 166 ARG A N   1 
ATOM   1223 C  CA  . ARG A 1 172 ? 0.11200   -26.58100 30.32500 1.000 26.82000 ? 166 ARG A CA  1 
ATOM   1224 C  C   . ARG A 1 172 ? 0.41100   -25.11700 29.97400 1.000 26.86000 ? 166 ARG A C   1 
ATOM   1225 O  O   . ARG A 1 172 ? -0.17700  -24.56200 29.03100 1.000 26.54000 ? 166 ARG A O   1 
ATOM   1226 C  CB  . ARG A 1 172 ? -0.80200  -26.67600 31.55800 1.000 25.94000 ? 166 ARG A CB  1 
ATOM   1227 C  CG  . ARG A 1 172 ? -1.57000  -28.01100 31.66000 1.000 23.26000 ? 166 ARG A CG  1 
ATOM   1228 C  CD  . ARG A 1 172 ? -1.84800  -28.44600 33.12700 1.000 25.14000 ? 166 ARG A CD  1 
ATOM   1229 N  NE  . ARG A 1 172 ? -2.59100  -29.70100 33.17300 1.000 25.68000 ? 166 ARG A NE  1 
ATOM   1230 C  CZ  . ARG A 1 172 ? -3.88600  -29.75300 33.44900 1.000 29.89000 ? 166 ARG A CZ  1 
ATOM   1231 N  NH1 . ARG A 1 172 ? -4.55600  -28.65600 33.77800 1.000 28.07000 ? 166 ARG A NH1 1 
ATOM   1232 N  NH2 . ARG A 1 172 ? -4.52600  -30.92600 33.39600 1.000 25.79000 ? 166 ARG A NH2 1 
ATOM   1233 N  N   . VAL A 1 173 ? 1.31200   -24.46300 30.71400 1.000 25.75000 ? 167 VAL A N   1 
ATOM   1234 C  CA  . VAL A 1 173 ? 1.66200   -23.07200 30.37800 1.000 22.15000 ? 167 VAL A CA  1 
ATOM   1235 C  C   . VAL A 1 173 ? 2.18200   -22.98300 28.94900 1.000 26.53000 ? 167 VAL A C   1 
ATOM   1236 O  O   . VAL A 1 173 ? 1.76900   -22.12100 28.16300 1.000 26.24000 ? 167 VAL A O   1 
ATOM   1237 C  CB  . VAL A 1 173 ? 2.69600   -22.51600 31.36400 1.000 25.09000 ? 167 VAL A CB  1 
ATOM   1238 C  CG1 . VAL A 1 173 ? 3.21400   -21.12600 30.86800 1.000 25.32000 ? 167 VAL A CG1 1 
ATOM   1239 C  CG2 . VAL A 1 173 ? 2.09900   -22.45100 32.76900 1.000 23.46000 ? 167 VAL A CG2 1 
ATOM   1240 N  N   . LYS A 1 174 ? 3.10600   -23.87300 28.59400 1.000 25.35000 ? 168 LYS A N   1 
ATOM   1241 C  CA  . LYS A 1 174 ? 3.72600   -23.81600 27.27700 1.000 27.80000 ? 168 LYS A CA  1 
ATOM   1242 C  C   . LYS A 1 174 ? 2.66600   -23.92900 26.18100 1.000 29.46000 ? 168 LYS A C   1 
ATOM   1243 O  O   . LYS A 1 174 ? 2.65400   -23.15800 25.20700 1.000 26.76000 ? 168 LYS A O   1 
ATOM   1244 C  CB  . LYS A 1 174 ? 4.78700   -24.93700 27.18300 1.000 31.24000 ? 168 LYS A CB  1 
ATOM   1245 C  CG  . LYS A 1 174 ? 5.84500   -24.83200 26.06800 1.000 32.92000 ? 168 LYS A CG  1 
ATOM   1246 C  CD  . LYS A 1 174 ? 7.13700   -25.64900 26.39000 1.000 36.37000 ? 168 LYS A CD  1 
ATOM   1247 C  CE  . LYS A 1 174 ? 8.26600   -24.79900 27.08600 1.000 41.20000 ? 168 LYS A CE  1 
ATOM   1248 N  NZ  . LYS A 1 174 ? 8.19400   -24.60300 28.61500 1.000 32.79000 ? 168 LYS A NZ  1 
ATOM   1249 N  N   . ARG A 1 175 ? 1.74700   -24.87600 26.34600 1.000 27.32000 ? 169 ARG A N   1 
ATOM   1250 C  CA  A ARG A 1 175 ? 0.69300   -25.07500 25.36300 0.600 29.15000 ? 169 ARG A CA  1 
ATOM   1251 C  CA  B ARG A 1 175 ? 0.69000   -25.07500 25.36500 0.400 29.13000 ? 169 ARG A CA  1 
ATOM   1252 C  C   . ARG A 1 175 ? -0.24000  -23.86800 25.30300 1.000 28.72000 ? 169 ARG A C   1 
ATOM   1253 O  O   . ARG A 1 175 ? -0.67200  -23.46300 24.21100 1.000 27.54000 ? 169 ARG A O   1 
ATOM   1254 C  CB  A ARG A 1 175 ? -0.06700  -26.36100 25.70700 0.600 29.82000 ? 169 ARG A CB  1 
ATOM   1255 C  CB  B ARG A 1 175 ? -0.07600  -26.35700 25.70900 0.400 29.80000 ? 169 ARG A CB  1 
ATOM   1256 C  CG  A ARG A 1 175 ? -0.94700  -26.92900 24.62200 0.600 28.94000 ? 169 ARG A CG  1 
ATOM   1257 C  CG  B ARG A 1 175 ? -1.26500  -26.66400 24.83100 0.400 29.17000 ? 169 ARG A CG  1 
ATOM   1258 C  CD  A ARG A 1 175 ? -1.35900  -28.33600 24.97800 0.600 27.79000 ? 169 ARG A CD  1 
ATOM   1259 C  CD  B ARG A 1 175 ? -1.95000  -27.94400 25.27900 0.400 28.70000 ? 169 ARG A CD  1 
ATOM   1260 N  NE  A ARG A 1 175 ? -1.79400  -28.49200 26.36500 0.600 28.45000 ? 169 ARG A NE  1 
ATOM   1261 N  NE  B ARG A 1 175 ? -2.42900  -27.89400 26.65800 0.400 28.69000 ? 169 ARG A NE  1 
ATOM   1262 C  CZ  A ARG A 1 175 ? -1.15500  -29.21600 27.27800 0.600 26.36000 ? 169 ARG A CZ  1 
ATOM   1263 C  CZ  B ARG A 1 175 ? -3.53200  -27.26700 27.05100 0.400 29.57000 ? 169 ARG A CZ  1 
ATOM   1264 N  NH1 A ARG A 1 175 ? 0.03200   -29.74600 27.03200 0.600 26.12000 ? 169 ARG A NH1 1 
ATOM   1265 N  NH1 B ARG A 1 175 ? -4.25600  -26.54900 26.20700 0.400 28.00000 ? 169 ARG A NH1 1 
ATOM   1266 N  NH2 A ARG A 1 175 ? -1.73300  -29.43500 28.45500 0.600 24.18000 ? 169 ARG A NH2 1 
ATOM   1267 N  NH2 B ARG A 1 175 ? -3.91900  -27.36600 28.32300 0.400 26.86000 ? 169 ARG A NH2 1 
ATOM   1268 N  N   . THR A 1 176 ? -0.54300  -23.26100 26.46400 1.000 26.50000 ? 170 THR A N   1 
ATOM   1269 C  CA  . THR A 1 176 ? -1.52500  -22.17100 26.52600 1.000 23.45000 ? 170 THR A CA  1 
ATOM   1270 C  C   . THR A 1 176 ? -0.99700  -20.87600 25.89900 1.000 24.93000 ? 170 THR A C   1 
ATOM   1271 O  O   . THR A 1 176 ? -1.74600  -20.14600 25.24000 1.000 25.28000 ? 170 THR A O   1 
ATOM   1272 C  CB  . THR A 1 176 ? -1.91300  -21.91200 27.98200 1.000 28.74000 ? 170 THR A CB  1 
ATOM   1273 O  OG1 . THR A 1 176 ? -2.36200  -23.13100 28.57600 1.000 32.71000 ? 170 THR A OG1 1 
ATOM   1274 C  CG2 . THR A 1 176 ? -3.01900  -20.86500 28.07500 1.000 25.96000 ? 170 THR A CG2 1 
ATOM   1275 N  N   . VAL A 1 177 ? 0.27900   -20.56100 26.11700 1.000 24.07000 ? 171 VAL A N   1 
ATOM   1276 C  CA  . VAL A 1 177 ? 0.88700   -19.38400 25.49700 1.000 25.98000 ? 171 VAL A CA  1 
ATOM   1277 C  C   . VAL A 1 177 ? 0.80000   -19.46200 23.97000 1.000 25.12000 ? 171 VAL A C   1 
ATOM   1278 O  O   . VAL A 1 177 ? 0.41500   -18.48800 23.30300 1.000 26.06000 ? 171 VAL A O   1 
ATOM   1279 C  CB  . VAL A 1 177 ? 2.33600   -19.23600 25.98100 1.000 24.51000 ? 171 VAL A CB  1 
ATOM   1280 C  CG1 . VAL A 1 177 ? 3.03900   -18.10900 25.23600 1.000 20.20000 ? 171 VAL A CG1 1 
ATOM   1281 C  CG2 . VAL A 1 177 ? 2.33200   -19.02100 27.49300 1.000 23.61000 ? 171 VAL A CG2 1 
ATOM   1282 N  N   . ALA A 1 178 ? 1.16900   -20.61300 23.39200 1.000 23.32000 ? 172 ALA A N   1 
ATOM   1283 C  CA  . ALA A 1 178 ? 1.13500   -20.75300 21.93600 1.000 25.62000 ? 172 ALA A CA  1 
ATOM   1284 C  C   . ALA A 1 178 ? -0.29300  -20.64400 21.41000 1.000 25.62000 ? 172 ALA A C   1 
ATOM   1285 O  O   . ALA A 1 178 ? -0.53400  -20.03400 20.36200 1.000 27.35000 ? 172 ALA A O   1 
ATOM   1286 C  CB  . ALA A 1 178 ? 1.75100   -22.09200 21.50500 1.000 24.30000 ? 172 ALA A CB  1 
ATOM   1287 N  N   . GLU A 1 179 ? -1.25100  -21.24500 22.11400 1.000 24.97000 ? 173 GLU A N   1 
ATOM   1288 C  CA  . GLU A 1 179 ? -2.64500  -21.15300 21.68800 1.000 28.60000 ? 173 GLU A CA  1 
ATOM   1289 C  C   . GLU A 1 179 ? -3.14100  -19.70100 21.69400 1.000 27.72000 ? 173 GLU A C   1 
ATOM   1290 O  O   . GLU A 1 179 ? -3.77300  -19.25800 20.72800 1.000 31.13000 ? 173 GLU A O   1 
ATOM   1291 C  CB  . GLU A 1 179 ? -3.52100  -22.05500 22.56900 1.000 30.57000 ? 173 GLU A CB  1 
ATOM   1292 C  CG  . GLU A 1 179 ? -3.27800  -23.56500 22.34600 1.000 33.00000 ? 173 GLU A CG  1 
ATOM   1293 C  CD  . GLU A 1 179 ? -3.96200  -24.46000 23.39600 1.000 36.48000 ? 173 GLU A CD  1 
ATOM   1294 O  OE1 . GLU A 1 179 ? -4.55100  -23.92700 24.36900 1.000 35.59000 ? 173 GLU A OE1 1 
ATOM   1295 O  OE2 . GLU A 1 179 ? -3.91500  -25.71300 23.24200 1.000 39.40000 ? 173 GLU A OE2 1 
ATOM   1296 N  N   . LEU A 1 180 ? -2.83000  -18.93000 22.74100 1.000 23.52000 ? 174 LEU A N   1 
ATOM   1297 C  CA  . LEU A 1 180 ? -3.26900  -17.53500 22.77900 1.000 24.30000 ? 174 LEU A CA  1 
ATOM   1298 C  C   . LEU A 1 180 ? -2.61800  -16.70500 21.68100 1.000 26.11000 ? 174 LEU A C   1 
ATOM   1299 O  O   . LEU A 1 180 ? -3.23900  -15.76900 21.14700 1.000 24.85000 ? 174 LEU A O   1 
ATOM   1300 C  CB  . LEU A 1 180 ? -2.95900  -16.91400 24.13200 1.000 24.38000 ? 174 LEU A CB  1 
ATOM   1301 C  CG  . LEU A 1 180 ? -3.91700  -17.34300 25.23600 1.000 30.86000 ? 174 LEU A CG  1 
ATOM   1302 C  CD1 . LEU A 1 180 ? -3.51800  -16.69300 26.55800 1.000 22.92000 ? 174 LEU A CD1 1 
ATOM   1303 C  CD2 . LEU A 1 180 ? -5.35700  -17.00400 24.84500 1.000 27.40000 ? 174 LEU A CD2 1 
ATOM   1304 N  N   . CYS A 1 181 ? -1.35900  -17.00000 21.36400 1.000 23.39000 ? 175 CYS A N   1 
ATOM   1305 C  CA  . CYS A 1 181 ? -0.65600  -16.31800 20.28400 1.000 23.79000 ? 175 CYS A CA  1 
ATOM   1306 C  C   . CYS A 1 181 ? -1.11400  -16.76500 18.90800 1.000 28.93000 ? 175 CYS A C   1 
ATOM   1307 O  O   . CYS A 1 181 ? -0.71500  -16.13700 17.91800 1.000 26.31000 ? 175 CYS A O   1 
ATOM   1308 C  CB  . CYS A 1 181 ? 0.83800   -16.57400 20.37600 1.000 23.81000 ? 175 CYS A CB  1 
ATOM   1309 S  SG  . CYS A 1 181 ? 1.60400   -15.81800 21.77400 1.000 26.59000 ? 175 CYS A SG  1 
ATOM   1310 N  N   . ASP A 1 182 ? -1.88400  -17.85700 18.82600 1.000 27.24000 ? 176 ASP A N   1 
ATOM   1311 C  CA  . ASP A 1 182 ? -2.20700  -18.52700 17.56200 1.000 29.93000 ? 176 ASP A CA  1 
ATOM   1312 C  C   . ASP A 1 182 ? -0.94500  -18.92600 16.80400 1.000 28.03000 ? 176 ASP A C   1 
ATOM   1313 O  O   . ASP A 1 182 ? -0.82800  -18.69900 15.59900 1.000 30.31000 ? 176 ASP A O   1 
ATOM   1314 C  CB  . ASP A 1 182 ? -3.10500  -17.65300 16.69400 1.000 30.14000 ? 176 ASP A CB  1 
ATOM   1315 C  CG  . ASP A 1 182 ? -4.39300  -17.29300 17.39300 1.000 29.72000 ? 176 ASP A CG  1 
ATOM   1316 O  OD1 . ASP A 1 182 ? -4.95700  -18.17100 18.11100 1.000 30.44000 ? 176 ASP A OD1 1 
ATOM   1317 O  OD2 . ASP A 1 182 ? -4.83900  -16.13600 17.23300 1.000 31.01000 ? 176 ASP A OD2 1 
ATOM   1318 N  N   . LEU A 1 183 ? -0.00400  -19.55200 17.52100 1.000 26.16000 ? 177 LEU A N   1 
ATOM   1319 C  CA  . LEU A 1 183 ? 1.26700   -20.00000 16.97500 1.000 24.51000 ? 177 LEU A CA  1 
ATOM   1320 C  C   . LEU A 1 183 ? 1.44200   -21.49900 17.18600 1.000 30.23000 ? 177 LEU A C   1 
ATOM   1321 O  O   . LEU A 1 183 ? 0.90200   -22.07600 18.13500 1.000 30.68000 ? 177 LEU A O   1 
ATOM   1322 C  CB  . LEU A 1 183 ? 2.44300   -19.25900 17.64900 1.000 25.32000 ? 177 LEU A CB  1 
ATOM   1323 C  CG  . LEU A 1 183 ? 2.56600   -17.77300 17.35800 1.000 28.83000 ? 177 LEU A CG  1 
ATOM   1324 C  CD1 . LEU A 1 183 ? 3.59300   -17.14800 18.29700 1.000 27.96000 ? 177 LEU A CD1 1 
ATOM   1325 C  CD2 . LEU A 1 183 ? 2.96000   -17.56500 15.87500 1.000 29.40000 ? 177 LEU A CD2 1 
ATOM   1326 N  N   . ASP A 1 184 ? 2.22200   -22.13200 16.31500 1.000 32.51000 ? 178 ASP A N   1 
ATOM   1327 C  CA  . ASP A 1 184 ? 2.63900   -23.50300 16.58500 1.000 33.93000 ? 178 ASP A CA  1 
ATOM   1328 C  C   . ASP A 1 184 ? 3.67300   -23.52300 17.70600 1.000 31.13000 ? 178 ASP A C   1 
ATOM   1329 O  O   . ASP A 1 184 ? 4.39000   -22.54800 17.93100 1.000 28.22000 ? 178 ASP A O   1 
ATOM   1330 C  CB  . ASP A 1 184 ? 3.24400   -24.14300 15.34900 1.000 38.04000 ? 178 ASP A CB  1 
ATOM   1331 C  CG  . ASP A 1 184 ? 2.27000   -24.24600 14.20700 1.000 49.95000 ? 178 ASP A CG  1 
ATOM   1332 O  OD1 . ASP A 1 184 ? 1.16900   -24.82900 14.38400 1.000 50.15000 ? 178 ASP A OD1 1 
ATOM   1333 O  OD2 . ASP A 1 184 ? 2.62800   -23.74200 13.11600 1.000 59.11000 ? 178 ASP A OD2 1 
ATOM   1334 N  N   . ALA A 1 185 ? 3.74200   -24.65700 18.41000 1.000 29.57000 ? 179 ALA A N   1 
ATOM   1335 C  CA  . ALA A 1 185 ? 4.69200   -24.81000 19.51500 1.000 31.74000 ? 179 ALA A CA  1 
ATOM   1336 C  C   . ALA A 1 185 ? 6.10600   -24.38100 19.12300 1.000 32.27000 ? 179 ALA A C   1 
ATOM   1337 O  O   . ALA A 1 185 ? 6.78800   -23.68300 19.88500 1.000 32.51000 ? 179 ALA A O   1 
ATOM   1338 C  CB  . ALA A 1 185 ? 4.68300   -26.27000 20.01000 1.000 27.71000 ? 179 ALA A CB  1 
ATOM   1339 N  N   . GLY A 1 186 ? 6.57400   -24.78900 17.95000 1.000 33.88000 ? 180 GLY A N   1 
ATOM   1340 C  CA  . GLY A 1 186 ? 7.92600   -24.40500 17.61500 1.000 27.03000 ? 180 GLY A CA  1 
ATOM   1341 C  C   . GLY A 1 186 ? 8.10900   -22.96900 17.20400 1.000 32.21000 ? 180 GLY A C   1 
ATOM   1342 O  O   . GLY A 1 186 ? 9.23500   -22.56300 16.90200 1.000 32.47000 ? 180 GLY A O   1 
ATOM   1343 N  N   . ASP A 1 187 ? 7.04800   -22.16900 17.15500 1.000 31.36000 ? 181 ASP A N   1 
ATOM   1344 C  CA  . ASP A 1 187 ? 7.22000   -20.75000 16.86600 1.000 30.58000 ? 181 ASP A CA  1 
ATOM   1345 C  C   . ASP A 1 187 ? 7.31300   -19.91400 18.11800 1.000 24.39000 ? 181 ASP A C   1 
ATOM   1346 O  O   . ASP A 1 187 ? 7.39000   -18.69200 18.00700 1.000 31.21000 ? 181 ASP A O   1 
ATOM   1347 C  CB  . ASP A 1 187 ? 6.08700   -20.22700 15.98000 1.000 30.93000 ? 181 ASP A CB  1 
ATOM   1348 C  CG  . ASP A 1 187 ? 6.36400   -20.46600 14.50400 1.000 41.51000 ? 181 ASP A CG  1 
ATOM   1349 O  OD1 . ASP A 1 187 ? 7.37100   -21.12900 14.20800 1.000 41.71000 ? 181 ASP A OD1 1 
ATOM   1350 O  OD2 . ASP A 1 187 ? 5.61000   -19.97600 13.63800 1.000 51.93000 ? 181 ASP A OD2 1 
ATOM   1351 N  N   . VAL A 1 188 ? 7.29600   -20.53000 19.29800 1.000 26.22000 ? 182 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 188 ? 7.50900   -19.83900 20.56700 1.000 22.77000 ? 182 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 188 ? 8.80100   -20.36800 21.17600 1.000 22.93000 ? 182 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 188 ? 8.95000   -21.58200 21.36900 1.000 25.44000 ? 182 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 188 ? 6.33700   -20.05800 21.54300 1.000 23.28000 ? 182 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 188 ? 6.68000   -19.44800 22.94200 1.000 21.18000 ? 182 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 188 ? 5.07600   -19.44300 20.99100 1.000 24.17000 ? 182 VAL A CG2 1 
ATOM   1358 N  N   . GLU A 1 189 ? 9.72900   -19.47400 21.48800 1.000 20.36000 ? 183 GLU A N   1 
ATOM   1359 C  CA  . GLU A 1 189 ? 11.01200  -19.89300 22.03200 1.000 23.43000 ? 183 GLU A CA  1 
ATOM   1360 C  C   . GLU A 1 189 ? 11.02100  -19.61100 23.52600 1.000 22.73000 ? 183 GLU A C   1 
ATOM   1361 O  O   . GLU A 1 189 ? 10.25200  -18.78500 24.00600 1.000 22.58000 ? 183 GLU A O   1 
ATOM   1362 C  CB  . GLU A 1 189 ? 12.16100  -19.18200 21.31200 1.000 26.95000 ? 183 GLU A CB  1 
ATOM   1363 C  CG  . GLU A 1 189 ? 12.40700  -19.77300 19.93600 1.000 31.76000 ? 183 GLU A CG  1 
ATOM   1364 C  CD  . GLU A 1 189 ? 13.08300  -18.81100 19.00600 1.000 44.24000 ? 183 GLU A CD  1 
ATOM   1365 O  OE1 . GLU A 1 189 ? 13.66500  -17.83300 19.51300 1.000 44.96000 ? 183 GLU A OE1 1 
ATOM   1366 O  OE2 . GLU A 1 189 ? 13.02100  -19.02100 17.76700 1.000 49.38000 ? 183 GLU A OE2 1 
ATOM   1367 N  N   . TRP A 1 190 ? 11.82500  -20.35600 24.27300 1.000 19.93000 ? 184 TRP A N   1 
ATOM   1368 C  CA  . TRP A 1 190 ? 11.72000  -20.31000 25.72500 1.000 22.23000 ? 184 TRP A CA  1 
ATOM   1369 C  C   . TRP A 1 190 ? 13.09500  -20.12500 26.32500 1.000 19.60000 ? 184 TRP A C   1 
ATOM   1370 O  O   . TRP A 1 190 ? 14.03400  -20.79700 25.91000 1.000 23.13000 ? 184 TRP A O   1 
ATOM   1371 C  CB  . TRP A 1 190 ? 11.04700  -21.58400 26.28900 1.000 20.23000 ? 184 TRP A CB  1 
ATOM   1372 C  CG  . TRP A 1 190 ? 9.59400   -21.68800 25.85900 1.000 21.68000 ? 184 TRP A CG  1 
ATOM   1373 C  CD1 . TRP A 1 190 ? 9.12500   -22.17700 24.67300 1.000 18.83000 ? 184 TRP A CD1 1 
ATOM   1374 C  CD2 . TRP A 1 190 ? 8.45000   -21.22300 26.58400 1.000 21.53000 ? 184 TRP A CD2 1 
ATOM   1375 N  NE1 . TRP A 1 190 ? 7.76000   -22.06000 24.62600 1.000 21.66000 ? 184 TRP A NE1 1 
ATOM   1376 C  CE2 . TRP A 1 190 ? 7.32200   -21.46600 25.78300 1.000 25.46000 ? 184 TRP A CE2 1 
ATOM   1377 C  CE3 . TRP A 1 190 ? 8.27000   -20.60200 27.82900 1.000 22.53000 ? 184 TRP A CE3 1 
ATOM   1378 C  CZ2 . TRP A 1 190 ? 6.03200   -21.16200 26.20400 1.000 22.23000 ? 184 TRP A CZ2 1 
ATOM   1379 C  CZ3 . TRP A 1 190 ? 6.98200   -20.31600 28.24400 1.000 21.05000 ? 184 TRP A CZ3 1 
ATOM   1380 C  CH2 . TRP A 1 190 ? 5.88600   -20.59400 27.43400 1.000 24.17000 ? 184 TRP A CH2 1 
ATOM   1381 N  N   . GLY A 1 191 ? 13.21800  -19.20300 27.28400 1.000 22.06000 ? 185 GLY A N   1 
ATOM   1382 C  CA  . GLY A 1 191 ? 14.43600  -19.10000 28.07000 1.000 22.08000 ? 185 GLY A CA  1 
ATOM   1383 C  C   . GLY A 1 191 ? 14.09200  -19.28500 29.52800 1.000 24.27000 ? 185 GLY A C   1 
ATOM   1384 O  O   . GLY A 1 191 ? 13.00100  -19.76300 29.84300 1.000 25.35000 ? 185 GLY A O   1 
ATOM   1385 N  N   . THR A 1 192 ? 14.96700  -18.85800 30.43600 1.000 21.50000 ? 186 THR A N   1 
ATOM   1386 C  CA  . THR A 1 192 ? 14.70000  -18.92000 31.86700 1.000 23.28000 ? 186 THR A CA  1 
ATOM   1387 C  C   . THR A 1 192 ? 14.60900  -17.50500 32.44800 1.000 22.73000 ? 186 THR A C   1 
ATOM   1388 O  O   . THR A 1 192 ? 15.49000  -16.66500 32.20400 1.000 23.02000 ? 186 THR A O   1 
ATOM   1389 C  CB  . THR A 1 192 ? 15.79500  -19.73100 32.56700 1.000 24.97000 ? 186 THR A CB  1 
ATOM   1390 O  OG1 . THR A 1 192 ? 15.85000  -21.05100 31.98900 1.000 25.17000 ? 186 THR A OG1 1 
ATOM   1391 C  CG2 . THR A 1 192 ? 15.49900  -19.83900 34.06800 1.000 25.99000 ? 186 THR A CG2 1 
ATOM   1392 N  N   . ASP A 1 193 ? 13.56300  -17.24700 33.23000 1.000 24.46000 ? 187 ASP A N   1 
ATOM   1393 C  CA  . ASP A 1 193 ? 13.27600  -15.90500 33.75500 1.000 25.07000 ? 187 ASP A CA  1 
ATOM   1394 C  C   . ASP A 1 193 ? 14.10400  -15.58700 35.00500 1.000 25.74000 ? 187 ASP A C   1 
ATOM   1395 O  O   . ASP A 1 193 ? 14.73000  -16.46100 35.60500 1.000 21.09000 ? 187 ASP A O   1 
ATOM   1396 C  CB  . ASP A 1 193 ? 11.78800  -15.77800 34.09700 1.000 27.42000 ? 187 ASP A CB  1 
ATOM   1397 C  CG  . ASP A 1 193 ? 11.17600  -14.49200 33.55600 1.000 30.64000 ? 187 ASP A CG  1 
ATOM   1398 O  OD1 . ASP A 1 193 ? 11.96600  -13.57100 33.19600 1.000 28.86000 ? 187 ASP A OD1 1 
ATOM   1399 O  OD2 . ASP A 1 193 ? 9.90800   -14.41000 33.50000 1.000 31.72000 ? 187 ASP A OD2 1 
ATOM   1400 N  N   . GLY A 1 194 ? 14.07100  -14.30900 35.43200 1.000 24.29000 ? 188 GLY A N   1 
ATOM   1401 C  CA  . GLY A 1 194 ? 14.74300  -13.95200 36.68200 1.000 26.60000 ? 188 GLY A CA  1 
ATOM   1402 C  C   . GLY A 1 194 ? 14.18500  -14.69900 37.88400 1.000 28.95000 ? 188 GLY A C   1 
ATOM   1403 O  O   . GLY A 1 194 ? 14.89800  -14.95200 38.87000 1.000 25.42000 ? 188 GLY A O   1 
ATOM   1404 N  N   . CYS A 1 195 ? 12.91200  -15.07000 37.82300 1.000 29.14000 ? 189 CYS A N   1 
ATOM   1405 C  CA  . CYS A 1 195 ? 12.25300  -15.78900 38.90100 1.000 29.78000 ? 189 CYS A CA  1 
ATOM   1406 C  C   . CYS A 1 195 ? 12.40000  -17.30000 38.77000 1.000 26.51000 ? 189 CYS A C   1 
ATOM   1407 O  O   . CYS A 1 195 ? 11.79500  -18.02800 39.55400 1.000 29.96000 ? 189 CYS A O   1 
ATOM   1408 C  CB  . CYS A 1 195 ? 10.76800  -15.40900 38.96000 1.000 26.96000 ? 189 CYS A CB  1 
ATOM   1409 S  SG  . CYS A 1 195 ? 9.82400   -15.98100 37.52100 1.000 29.96000 ? 189 CYS A SG  1 
ATOM   1410 N  N   . ASN A 1 196 ? 13.17100  -17.77400 37.79000 1.000 29.66000 ? 190 ASN A N   1 
ATOM   1411 C  CA  . ASN A 1 196 ? 13.58000  -19.16300 37.60600 1.000 30.36000 ? 190 ASN A CA  1 
ATOM   1412 C  C   . ASN A 1 196 ? 12.51600  -20.04100 36.94600 1.000 31.03000 ? 190 ASN A C   1 
ATOM   1413 O  O   . ASN A 1 196 ? 12.68400  -21.28900 36.92000 1.000 30.41000 ? 190 ASN A O   1 
ATOM   1414 C  CB  . ASN A 1 196 ? 13.99600  -19.80200 38.93300 1.000 30.90000 ? 190 ASN A CB  1 
ATOM   1415 C  CG  . ASN A 1 196 ? 14.99100  -20.91900 38.74900 1.000 30.06000 ? 190 ASN A CG  1 
ATOM   1416 O  OD1 . ASN A 1 196 ? 15.79200  -20.89800 37.81900 1.000 29.59000 ? 190 ASN A OD1 1 
ATOM   1417 N  ND2 . ASN A 1 196 ? 14.95000  -21.90200 39.63700 1.000 36.76000 ? 190 ASN A ND2 1 
ATOM   1418 N  N   . LEU A 1 197 ? 11.42100  -19.45500 36.40500 1.000 27.33000 ? 191 LEU A N   1 
ATOM   1419 C  CA  . LEU A 1 197 ? 10.43200  -20.13600 35.57300 1.000 27.86000 ? 191 LEU A CA  1 
ATOM   1420 C  C   . LEU A 1 197 ? 10.80800  -20.04600 34.09700 1.000 28.19000 ? 191 LEU A C   1 
ATOM   1421 O  O   . LEU A 1 197 ? 11.55900  -19.15900 33.69400 1.000 25.02000 ? 191 LEU A O   1 
ATOM   1422 C  CB  . LEU A 1 197 ? 9.06600   -19.49700 35.77400 1.000 26.32000 ? 191 LEU A CB  1 
ATOM   1423 C  CG  . LEU A 1 197 ? 8.35200   -19.79800 37.07300 1.000 28.42000 ? 191 LEU A CG  1 
ATOM   1424 C  CD1 . LEU A 1 197 ? 7.13400   -18.91800 37.15500 1.000 28.37000 ? 191 LEU A CD1 1 
ATOM   1425 C  CD2 . LEU A 1 197 ? 7.92800   -21.27200 37.08200 1.000 29.31000 ? 191 LEU A CD2 1 
ATOM   1426 N  N   . PRO A 1 198 ? 10.28900  -20.92900 33.24400 1.000 27.41000 ? 192 PRO A N   1 
ATOM   1427 C  CA  . PRO A 1 198 ? 10.45700  -20.71500 31.79400 1.000 21.40000 ? 192 PRO A CA  1 
ATOM   1428 C  C   . PRO A 1 198 ? 9.70400   -19.46500 31.35800 1.000 24.89000 ? 192 PRO A C   1 
ATOM   1429 O  O   . PRO A 1 198 ? 8.66400   -19.10300 31.92100 1.000 25.55000 ? 192 PRO A O   1 
ATOM   1430 C  CB  . PRO A 1 198 ? 9.86000   -21.98100 31.15700 1.000 22.24000 ? 192 PRO A CB  1 
ATOM   1431 C  CG  . PRO A 1 198 ? 9.69000   -22.97400 32.30900 1.000 24.70000 ? 192 PRO A CG  1 
ATOM   1432 C  CD  . PRO A 1 198 ? 9.49700   -22.13700 33.54500 1.000 28.22000 ? 192 PRO A CD  1 
ATOM   1433 N  N   . THR A 1 199 ? 10.22200  -18.80800 30.32600 1.000 21.04000 ? 193 THR A N   1 
ATOM   1434 C  CA  . THR A 1 199 ? 9.64900   -17.53200 29.91800 1.000 21.69000 ? 193 THR A CA  1 
ATOM   1435 C  C   . THR A 1 199 ? 9.68300   -17.48300 28.39000 1.000 23.25000 ? 193 THR A C   1 
ATOM   1436 O  O   . THR A 1 199 ? 10.69100  -17.90400 27.77300 1.000 21.24000 ? 193 THR A O   1 
ATOM   1437 C  CB  . THR A 1 199 ? 10.41300  -16.34500 30.57500 1.000 21.86000 ? 193 THR A CB  1 
ATOM   1438 O  OG1 . THR A 1 199 ? 9.67300   -15.13700 30.41500 1.000 23.13000 ? 193 THR A OG1 1 
ATOM   1439 C  CG2 . THR A 1 199 ? 11.83600  -16.14000 30.01800 1.000 26.19000 ? 193 THR A CG2 1 
ATOM   1440 N  N   . PRO A 1 200 ? 8.59500   -17.06600 27.74700 1.000 19.96000 ? 194 PRO A N   1 
ATOM   1441 C  CA  . PRO A 1 200 ? 8.49300   -17.20100 26.28400 1.000 19.93000 ? 194 PRO A CA  1 
ATOM   1442 C  C   . PRO A 1 200 ? 8.97300   -15.98700 25.49400 1.000 18.41000 ? 194 PRO A C   1 
ATOM   1443 O  O   . PRO A 1 200 ? 8.95800   -14.84300 25.95000 1.000 18.79000 ? 194 PRO A O   1 
ATOM   1444 C  CB  . PRO A 1 200 ? 6.98800   -17.41500 26.08400 1.000 19.06000 ? 194 PRO A CB  1 
ATOM   1445 C  CG  . PRO A 1 200 ? 6.39100   -16.46800 27.17800 1.000 20.54000 ? 194 PRO A CG  1 
ATOM   1446 C  CD  . PRO A 1 200 ? 7.33000   -16.64800 28.36800 1.000 19.67000 ? 194 PRO A CD  1 
ATOM   1447 N  N   . ALA A 1 201 ? 9.39300   -16.25800 24.26200 1.000 19.76000 ? 195 ALA A N   1 
ATOM   1448 C  CA  . ALA A 1 201 ? 9.67500   -15.22300 23.27400 1.000 16.00000 ? 195 ALA A CA  1 
ATOM   1449 C  C   . ALA A 1 201 ? 8.85800   -15.52700 22.02000 1.000 20.72000 ? 195 ALA A C   1 
ATOM   1450 O  O   . ALA A 1 201 ? 8.77600   -16.69500 21.60600 1.000 20.63000 ? 195 ALA A O   1 
ATOM   1451 C  CB  . ALA A 1 201 ? 11.17800  -15.15400 22.96000 1.000 16.99000 ? 195 ALA A CB  1 
ATOM   1452 N  N   . PHE A 1 202 ? 8.18100   -14.50700 21.47600 1.000 19.67000 ? 196 PHE A N   1 
ATOM   1453 C  CA  . PHE A 1 202 ? 7.37800   -14.64300 20.26300 1.000 18.73000 ? 196 PHE A CA  1 
ATOM   1454 C  C   . PHE A 1 202 ? 7.31300   -13.28400 19.57500 1.000 19.73000 ? 196 PHE A C   1 
ATOM   1455 O  O   . PHE A 1 202 ? 7.79300   -12.28000 20.11400 1.000 21.96000 ? 196 PHE A O   1 
ATOM   1456 C  CB  . PHE A 1 202 ? 5.97100   -15.20700 20.55500 1.000 19.58000 ? 196 PHE A CB  1 
ATOM   1457 C  CG  . PHE A 1 202 ? 5.31700   -14.69400 21.84300 1.000 20.14000 ? 196 PHE A CG  1 
ATOM   1458 C  CD1 . PHE A 1 202 ? 4.67800   -13.45000 21.87900 1.000 19.07000 ? 196 PHE A CD1 1 
ATOM   1459 C  CD2 . PHE A 1 202 ? 5.29600   -15.49500 22.99300 1.000 19.89000 ? 196 PHE A CD2 1 
ATOM   1460 C  CE1 . PHE A 1 202 ? 4.05300   -12.98700 23.04300 1.000 21.13000 ? 196 PHE A CE1 1 
ATOM   1461 C  CE2 . PHE A 1 202 ? 4.68600   -15.05000 24.18000 1.000 18.34000 ? 196 PHE A CE2 1 
ATOM   1462 C  CZ  . PHE A 1 202 ? 4.05700   -13.78800 24.20800 1.000 22.98000 ? 196 PHE A CZ  1 
ATOM   1463 N  N   . PRO A 1 203 ? 6.81600   -13.22600 18.33600 1.000 21.86000 ? 197 PRO A N   1 
ATOM   1464 C  CA  . PRO A 1 203 ? 6.73300   -11.92100 17.66100 1.000 19.03000 ? 197 PRO A CA  1 
ATOM   1465 C  C   . PRO A 1 203 ? 5.95800   -10.89600 18.48000 1.000 18.91000 ? 197 PRO A C   1 
ATOM   1466 O  O   . PRO A 1 203 ? 4.92200   -11.19100 19.06900 1.000 18.46000 ? 197 PRO A O   1 
ATOM   1467 C  CB  . PRO A 1 203 ? 6.02000   -12.24500 16.34500 1.000 20.43000 ? 197 PRO A CB  1 
ATOM   1468 C  CG  . PRO A 1 203 ? 6.49200   -13.64200 16.03800 1.000 24.34000 ? 197 PRO A CG  1 
ATOM   1469 C  CD  . PRO A 1 203 ? 6.46200   -14.32400 17.40900 1.000 24.11000 ? 197 PRO A CD  1 
ATOM   1470 N  N   . LEU A 1 204 ? 6.47100   -9.66300  18.49400 1.000 19.74000 ? 198 LEU A N   1 
ATOM   1471 C  CA  . LEU A 1 204 ? 5.85900   -8.60500  19.29200 1.000 19.40000 ? 198 LEU A CA  1 
ATOM   1472 C  C   . LEU A 1 204 ? 4.37100   -8.43100  18.98900 1.000 21.74000 ? 198 LEU A C   1 
ATOM   1473 O  O   . LEU A 1 204 ? 3.55900   -8.19600  19.90500 1.000 19.08000 ? 198 LEU A O   1 
ATOM   1474 C  CB  . LEU A 1 204 ? 6.64900   -7.30800  19.04700 1.000 19.95000 ? 198 LEU A CB  1 
ATOM   1475 C  CG  . LEU A 1 204 ? 6.21000   -6.06600  19.80500 1.000 22.34000 ? 198 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A 1 204 ? 6.40400   -6.31400  21.27400 1.000 17.75000 ? 198 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A 1 204 ? 7.06300   -4.87100  19.35100 1.000 19.64000 ? 198 LEU A CD2 1 
ATOM   1478 N  N   . ASP A 1 205 ? 3.95600   -8.59400  17.72700 1.000 18.79000 ? 199 ASP A N   1 
ATOM   1479 C  CA  . ASP A 1 205 ? 2.52800   -8.41100  17.46300 1.000 20.77000 ? 199 ASP A CA  1 
ATOM   1480 C  C   . ASP A 1 205 ? 1.64600   -9.45900  18.16800 1.000 20.08000 ? 199 ASP A C   1 
ATOM   1481 O  O   . ASP A 1 205 ? 0.50100   -9.17000  18.53500 1.000 18.82000 ? 199 ASP A O   1 
ATOM   1482 C  CB  . ASP A 1 205 ? 2.25300   -8.40900  15.95800 1.000 24.24000 ? 199 ASP A CB  1 
ATOM   1483 C  CG  . ASP A 1 205 ? 2.46700   -9.75900  15.32900 1.000 22.38000 ? 199 ASP A CG  1 
ATOM   1484 O  OD1 . ASP A 1 205 ? 3.62600   -10.23800 15.30900 1.000 26.02000 ? 199 ASP A OD1 1 
ATOM   1485 O  OD2 . ASP A 1 205 ? 1.47400   -10.36500 14.89600 1.000 27.59000 ? 199 ASP A OD2 1 
ATOM   1486 N  N   . ARG A 1 206 ? 2.15000   -10.67500 18.37800 1.000 21.09000 ? 200 ARG A N   1 
ATOM   1487 C  CA  . ARG A 1 206 ? 1.37400   -11.67100 19.10900 1.000 21.80000 ? 200 ARG A CA  1 
ATOM   1488 C  C   . ARG A 1 206 ? 1.14600   -11.29400 20.57400 1.000 19.76000 ? 200 ARG A C   1 
ATOM   1489 O  O   . ARG A 1 206 ? 0.18400   -11.76800 21.19300 1.000 23.87000 ? 200 ARG A O   1 
ATOM   1490 C  CB  . ARG A 1 206 ? 2.08100   -13.01500 19.00600 1.000 22.44000 ? 200 ARG A CB  1 
ATOM   1491 C  CG  . ARG A 1 206 ? 2.29500   -13.47000 17.56400 1.000 22.95000 ? 200 ARG A CG  1 
ATOM   1492 C  CD  . ARG A 1 206 ? 1.00200   -13.30600 16.75500 1.000 25.96000 ? 200 ARG A CD  1 
ATOM   1493 N  NE  . ARG A 1 206 ? 1.19500   -13.67900 15.35600 1.000 28.03000 ? 200 ARG A NE  1 
ATOM   1494 C  CZ  . ARG A 1 206 ? 0.67900   -14.76100 14.79400 1.000 33.09000 ? 200 ARG A CZ  1 
ATOM   1495 N  NH1 . ARG A 1 206 ? -0.07700  -15.60100 15.48100 1.000 31.26000 ? 200 ARG A NH1 1 
ATOM   1496 N  NH2 . ARG A 1 206 ? 0.90300   -14.99400 13.50400 1.000 33.40000 ? 200 ARG A NH2 1 
ATOM   1497 N  N   . LEU A 1 207 ? 2.03900   -10.50800 21.15900 1.000 16.95000 ? 201 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 207 ? 1.81500   -9.97000  22.49500 1.000 18.04000 ? 201 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 207 ? 0.62900   -9.02200  22.48700 1.000 19.54000 ? 201 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 207 ? -0.25100  -9.08800  23.35200 1.000 19.09000 ? 201 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 207 ? 3.08600   -9.25000  22.99000 1.000 20.29000 ? 201 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 207 ? 3.03600   -8.73600  24.45400 1.000 18.53000 ? 201 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 207 ? 2.68700   -9.91000  25.42800 1.000 20.20000 ? 201 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 207 ? 4.27800   -8.00800  24.93900 1.000 16.65000 ? 201 LEU A CD2 1 
ATOM   1505 N  N   . GLY A 1 208 ? 0.59000   -8.11800  21.51900 1.000 19.47000 ? 202 GLY A N   1 
ATOM   1506 C  CA  . GLY A 1 208 ? -0.60800  -7.32300  21.34300 1.000 17.89000 ? 202 GLY A CA  1 
ATOM   1507 C  C   . GLY A 1 208 ? -1.84200  -8.18600  21.16600 1.000 22.80000 ? 202 GLY A C   1 
ATOM   1508 O  O   . GLY A 1 208 ? -2.91500  -7.86900  21.69300 1.000 24.92000 ? 202 GLY A O   1 
ATOM   1509 N  N   . ARG A 1 209 ? -1.70400  -9.29900  20.42000 1.000 22.78000 ? 203 ARG A N   1 
ATOM   1510 C  CA  . ARG A 1 209 ? -2.85200  -10.16000 20.14900 1.000 21.35000 ? 203 ARG A CA  1 
ATOM   1511 C  C   . ARG A 1 209 ? -3.37800  -10.76500 21.44000 1.000 20.40000 ? 203 ARG A C   1 
ATOM   1512 O  O   . ARG A 1 209 ? -4.58900  -10.77900 21.67700 1.000 21.94000 ? 203 ARG A O   1 
ATOM   1513 C  CB  . ARG A 1 209 ? -2.49000  -11.25300 19.12500 1.000 22.59000 ? 203 ARG A CB  1 
ATOM   1514 C  CG  . ARG A 1 209 ? -3.67800  -12.05000 18.57700 1.000 22.39000 ? 203 ARG A CG  1 
ATOM   1515 C  CD  . ARG A 1 209 ? -3.27800  -13.26300 17.70800 1.000 23.77000 ? 203 ARG A CD  1 
ATOM   1516 N  NE  . ARG A 1 209 ? -2.66600  -12.86000 16.44200 1.000 26.14000 ? 203 ARG A NE  1 
ATOM   1517 C  CZ  . ARG A 1 209 ? -2.78700  -13.50900 15.28600 1.000 29.85000 ? 203 ARG A CZ  1 
ATOM   1518 N  NH1 . ARG A 1 209 ? -3.53500  -14.60600 15.16600 1.000 26.42000 ? 203 ARG A NH1 1 
ATOM   1519 N  NH2 . ARG A 1 209 ? -2.15800  -13.03800 14.21400 1.000 26.97000 ? 203 ARG A NH2 1 
ATOM   1520 N  N   . ILE A 1 210 ? -2.48200  -11.20600 22.32300 1.000 19.31000 ? 204 ILE A N   1 
ATOM   1521 C  CA  . ILE A 1 210 ? -2.94400  -11.74400 23.60700 1.000 23.69000 ? 204 ILE A CA  1 
ATOM   1522 C  C   . ILE A 1 210 ? -3.79400  -10.71900 24.35000 1.000 20.84000 ? 204 ILE A C   1 
ATOM   1523 O  O   . ILE A 1 210 ? -4.84800  -11.04000 24.90100 1.000 23.21000 ? 204 ILE A O   1 
ATOM   1524 C  CB  . ILE A 1 210 ? -1.74800  -12.18000 24.47100 1.000 23.91000 ? 204 ILE A CB  1 
ATOM   1525 C  CG1 . ILE A 1 210 ? -1.15700  -13.51000 23.96300 1.000 20.67000 ? 204 ILE A CG1 1 
ATOM   1526 C  CG2 . ILE A 1 210 ? -2.17600  -12.26100 25.93000 1.000 18.46000 ? 204 ILE A CG2 1 
ATOM   1527 C  CD1 . ILE A 1 210 ? 0.29300   -13.66500 24.30400 1.000 21.45000 ? 204 ILE A CD1 1 
ATOM   1528 N  N   . TYR A 1 211 ? -3.34900  -9.46600  24.38100 1.000 22.78000 ? 205 TYR A N   1 
ATOM   1529 C  CA  . TYR A 1 211 ? -4.06700  -8.45400  25.13800 1.000 20.73000 ? 205 TYR A CA  1 
ATOM   1530 C  C   . TYR A 1 211 ? -5.34400  -7.99400  24.44200 1.000 20.16000 ? 205 TYR A C   1 
ATOM   1531 O  O   . TYR A 1 211 ? -6.32200  -7.65500  25.11900 1.000 22.75000 ? 205 TYR A O   1 
ATOM   1532 C  CB  . TYR A 1 211 ? -3.13400  -7.28900  25.42400 1.000 16.80000 ? 205 TYR A CB  1 
ATOM   1533 C  CG  . TYR A 1 211 ? -2.28500  -7.61600  26.58900 1.000 22.13000 ? 205 TYR A CG  1 
ATOM   1534 C  CD1 . TYR A 1 211 ? -1.34300  -8.62100  26.49700 1.000 17.86000 ? 205 TYR A CD1 1 
ATOM   1535 C  CD2 . TYR A 1 211 ? -2.48300  -6.99000  27.81900 1.000 21.05000 ? 205 TYR A CD2 1 
ATOM   1536 C  CE1 . TYR A 1 211 ? -0.56800  -8.97200  27.57300 1.000 17.11000 ? 205 TYR A CE1 1 
ATOM   1537 C  CE2 . TYR A 1 211 ? -1.70400  -7.31900  28.90100 1.000 17.92000 ? 205 TYR A CE2 1 
ATOM   1538 C  CZ  . TYR A 1 211 ? -0.75300  -8.31700  28.77200 1.000 19.18000 ? 205 TYR A CZ  1 
ATOM   1539 O  OH  . TYR A 1 211 ? 0.02800   -8.69600  29.85800 1.000 21.82000 ? 205 TYR A OH  1 
ATOM   1540 N  N   . ALA A 1 212 ? -5.37400  -8.01800  23.10000 1.000 21.63000 ? 206 ALA A N   1 
ATOM   1541 C  CA  . ALA A 1 212 ? -6.63000  -7.79700  22.39300 1.000 23.62000 ? 206 ALA A CA  1 
ATOM   1542 C  C   . ALA A 1 212 ? -7.65700  -8.85800  22.77400 1.000 26.62000 ? 206 ALA A C   1 
ATOM   1543 O  O   . ALA A 1 212 ? -8.86000  -8.57000  22.88500 1.000 25.52000 ? 206 ALA A O   1 
ATOM   1544 C  CB  . ALA A 1 212 ? -6.37400  -7.78100  20.88600 1.000 22.48000 ? 206 ALA A CB  1 
ATOM   1545 N  N   . LYS A 1 213 ? -7.19800  -10.09100 23.00700 1.000 25.25000 ? 207 LYS A N   1 
ATOM   1546 C  CA  . LYS A 1 213 ? -8.11800  -11.15900 23.35700 1.000 22.00000 ? 207 LYS A CA  1 
ATOM   1547 C  C   . LYS A 1 213 ? -8.61700  -10.99500 24.78300 1.000 27.57000 ? 207 LYS A C   1 
ATOM   1548 O  O   . LYS A 1 213 ? -9.78200  -11.28000 25.06400 1.000 29.82000 ? 207 LYS A O   1 
ATOM   1549 C  CB  . LYS A 1 213 ? -7.44600  -12.51500 23.15100 1.000 25.28000 ? 207 LYS A CB  1 
ATOM   1550 C  CG  . LYS A 1 213 ? -7.19500  -12.84900 21.67700 1.000 24.18000 ? 207 LYS A CG  1 
ATOM   1551 C  CD  . LYS A 1 213 ? -6.35800  -14.12400 21.50600 1.000 25.07000 ? 207 LYS A CD  1 
ATOM   1552 C  CE  . LYS A 1 213 ? -6.69500  -14.84800 20.23300 1.000 25.59000 ? 207 LYS A CE  1 
ATOM   1553 N  NZ  . LYS A 1 213 ? -5.88300  -16.06800 20.09000 1.000 25.74000 ? 207 LYS A NZ  1 
ATOM   1554 N  N   . LEU A 1 214 ? -7.75100  -10.54400 25.69600 1.000 22.24000 ? 208 LEU A N   1 
ATOM   1555 C  CA  . LEU A 1 214 ? -8.20500  -10.18100 27.04000 1.000 24.34000 ? 208 LEU A CA  1 
ATOM   1556 C  C   . LEU A 1 214 ? -9.32800  -9.15200  26.99100 1.000 26.77000 ? 208 LEU A C   1 
ATOM   1557 O  O   . LEU A 1 214 ? -10.40900 -9.35700  27.55200 1.000 27.66000 ? 208 LEU A O   1 
ATOM   1558 C  CB  . LEU A 1 214 ? -7.02300  -9.64100  27.86100 1.000 26.66000 ? 208 LEU A CB  1 
ATOM   1559 C  CG  . LEU A 1 214 ? -6.06700  -10.69700 28.39800 1.000 23.15000 ? 208 LEU A CG  1 
ATOM   1560 C  CD1 . LEU A 1 214 ? -4.81300  -10.03400 28.95700 1.000 19.95000 ? 208 LEU A CD1 1 
ATOM   1561 C  CD2 . LEU A 1 214 ? -6.76600  -11.48000 29.48800 1.000 23.13000 ? 208 LEU A CD2 1 
ATOM   1562 N  N   . ALA A 1 215 ? -9.08800  -8.02400  26.32700 1.000 26.57000 ? 209 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 215 ? -10.10700 -6.97700  26.28100 1.000 27.84000 ? 209 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 215 ? -11.35300 -7.45100  25.54400 1.000 29.54000 ? 209 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 215 ? -12.48600 -7.11900  25.93000 1.000 28.16000 ? 209 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 215 ? -9.53400  -5.72000  25.62100 1.000 24.29000 ? 209 ALA A CB  1 
ATOM   1567 N  N   . SER A 1 216 ? -11.16800 -8.22500  24.47500 1.000 25.41000 ? 210 SER A N   1 
ATOM   1568 C  CA  . SER A 1 216 ? -12.31600 -8.76600  23.75600 1.000 30.27000 ? 210 SER A CA  1 
ATOM   1569 C  C   . SER A 1 216 ? -13.12300 -9.71100  24.63600 1.000 27.81000 ? 210 SER A C   1 
ATOM   1570 O  O   . SER A 1 216 ? -14.35900 -9.73500  24.56900 1.000 26.52000 ? 210 SER A O   1 
ATOM   1571 C  CB  . SER A 1 216 ? -11.83800 -9.48200  22.49900 1.000 29.90000 ? 210 SER A CB  1 
ATOM   1572 O  OG  . SER A 1 216 ? -12.95900 -9.83400  21.71100 1.000 30.71000 ? 210 SER A OG  1 
ATOM   1573 N  N   . ALA A 1 217 ? -12.45500 -10.49900 25.47800 1.000 27.87000 ? 211 ALA A N   1 
ATOM   1574 C  CA  . ALA A 1 217 ? -13.22100 -11.37000 26.35800 1.000 32.80000 ? 211 ALA A CA  1 
ATOM   1575 C  C   . ALA A 1 217 ? -14.00800 -10.55300 27.37400 1.000 34.81000 ? 211 ALA A C   1 
ATOM   1576 O  O   . ALA A 1 217 ? -15.16800 -10.87000 27.66600 1.000 33.42000 ? 211 ALA A O   1 
ATOM   1577 C  CB  . ALA A 1 217 ? -12.31600 -12.38600 27.04500 1.000 30.81000 ? 211 ALA A CB  1 
ATOM   1578 N  N   . ALA A 1 218 ? -13.41200 -9.47400  27.88800 1.000 29.77000 ? 212 ALA A N   1 
ATOM   1579 C  CA  . ALA A 1 218 ? -14.14500 -8.58700  28.79400 1.000 28.99000 ? 212 ALA A CA  1 
ATOM   1580 C  C   . ALA A 1 218 ? -15.38500 -8.01000  28.12200 1.000 35.14000 ? 212 ALA A C   1 
ATOM   1581 O  O   . ALA A 1 218 ? -16.46000 -7.95000  28.72600 1.000 35.92000 ? 212 ALA A O   1 
ATOM   1582 C  CB  . ALA A 1 218 ? -13.21800 -7.47300  29.27900 1.000 31.29000 ? 212 ALA A CB  1 
ATOM   1583 N  N   . ASP A 1 219 ? -15.25700 -7.59800  26.85900 1.000 31.20000 ? 213 ASP A N   1 
ATOM   1584 C  CA  . ASP A 1 219 ? -16.39800 -7.09000  26.11100 1.000 34.39000 ? 213 ASP A CA  1 
ATOM   1585 C  C   . ASP A 1 219 ? -17.50700 -8.13700  25.99400 1.000 37.51000 ? 213 ASP A C   1 
ATOM   1586 O  O   . ASP A 1 219 ? -18.68800 -7.83400  26.21100 1.000 41.24000 ? 213 ASP A O   1 
ATOM   1587 C  CB  . ASP A 1 219 ? -15.94200 -6.63600  24.73200 1.000 31.54000 ? 213 ASP A CB  1 
ATOM   1588 C  CG  . ASP A 1 219 ? -15.24700 -5.29100  24.76000 1.000 34.62000 ? 213 ASP A CG  1 
ATOM   1589 O  OD1 . ASP A 1 219 ? -15.46800 -4.50300  25.71200 1.000 37.74000 ? 213 ASP A OD1 1 
ATOM   1590 O  OD2 . ASP A 1 219 ? -14.50600 -5.00900  23.80400 1.000 31.04000 ? 213 ASP A OD2 1 
ATOM   1591 N  N   . GLY A 1 220 ? -17.14700 -9.37400  25.64700 1.000 33.35000 ? 214 GLY A N   1 
ATOM   1592 C  CA  . GLY A 1 220 ? -18.15900 -10.40700 25.49100 1.000 40.39000 ? 214 GLY A CA  1 
ATOM   1593 C  C   . GLY A 1 220 ? -18.80000 -10.80400 26.80700 1.000 51.37000 ? 214 GLY A C   1 
ATOM   1594 O  O   . GLY A 1 220 ? -19.99900 -11.09700 26.86300 1.000 54.66000 ? 214 GLY A O   1 
ATOM   1595 N  N   . SER A 1 221 ? -18.01000 -10.82900 27.88200 1.000 44.37000 ? 215 SER A N   1 
ATOM   1596 C  CA  . SER A 1 221 ? -18.55700 -11.11200 29.20300 1.000 43.38000 ? 215 SER A CA  1 
ATOM   1597 C  C   . SER A 1 221 ? -19.51600 -10.01800 29.63500 1.000 51.16000 ? 215 SER A C   1 
ATOM   1598 O  O   . SER A 1 221 ? -20.60900 -10.29700 30.14200 1.000 53.06000 ? 215 SER A O   1 
ATOM   1599 C  CB  . SER A 1 221 ? -17.43000 -11.26200 30.22100 1.000 43.07000 ? 215 SER A CB  1 
ATOM   1600 O  OG  . SER A 1 221 ? -17.95700 -11.52700 31.50800 1.000 47.34000 ? 215 SER A OG  1 
ATOM   1601 N  N   . ASP A 1 222 ? -19.12500 -8.75800  29.43800 1.000 55.37000 ? 216 ASP A N   1 
ATOM   1602 C  CA  . ASP A 1 222 ? -19.98200 -7.64800  29.84000 1.000 57.67000 ? 216 ASP A CA  1 
ATOM   1603 C  C   . ASP A 1 222 ? -21.28500 -7.61500  29.05800 1.000 61.79000 ? 216 ASP A C   1 
ATOM   1604 O  O   . ASP A 1 222 ? -22.23500 -6.94500  29.48600 1.000 69.18000 ? 216 ASP A O   1 
ATOM   1605 C  CB  . ASP A 1 222 ? -19.25200 -6.31900  29.65600 1.000 60.16000 ? 216 ASP A CB  1 
ATOM   1606 C  CG  . ASP A 1 222 ? -19.19000 -5.49500  30.93500 1.000 69.37000 ? 216 ASP A CG  1 
ATOM   1607 O  OD1 . ASP A 1 222 ? -18.43700 -5.88700  31.86000 1.000 73.25000 ? 216 ASP A OD1 1 
ATOM   1608 O  OD2 . ASP A 1 222 ? -19.87600 -4.44800  31.00300 1.000 71.39000 ? 216 ASP A OD2 1 
ATOM   1609 N  N   . ALA A 1 223 ? -21.35200 -8.31800  27.92400 1.000 57.36000 ? 217 ALA A N   1 
ATOM   1610 C  CA  . ALA A 1 223 ? -22.53100 -8.31400  27.06200 1.000 65.23000 ? 217 ALA A CA  1 
ATOM   1611 C  C   . ALA A 1 223 ? -23.35300 -9.60800  27.13500 1.000 59.97000 ? 217 ALA A C   1 
ATOM   1612 O  O   . ALA A 1 223 ? -24.31300 -9.75200  26.37100 1.000 63.51000 ? 217 ALA A O   1 
ATOM   1613 C  CB  . ALA A 1 223 ? -22.11300 -8.02400  25.61300 1.000 59.24000 ? 217 ALA A CB  1 
ATOM   1614 N  N   . GLY A 1 224 ? -23.00000 -10.54600 28.02200 1.000 60.90000 ? 218 GLY A N   1 
ATOM   1615 C  CA  . GLY A 1 224 ? -23.78100 -11.76000 28.24000 1.000 69.84000 ? 218 GLY A CA  1 
ATOM   1616 C  C   . GLY A 1 224 ? -23.69800 -12.81600 27.15000 1.000 74.13000 ? 218 GLY A C   1 
ATOM   1617 O  O   . GLY A 1 224 ? -24.66100 -13.56400 26.94700 1.000 70.13000 ? 218 GLY A O   1 
ATOM   1618 N  N   . GLU A 1 225 ? -22.60300 -12.75600 26.38800 1.000 79.51000 ? 219 GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 225 ? -22.46600 -13.57600 25.16000 1.000 81.18000 ? 219 GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 225 ? -22.05300 -15.02300 25.40700 1.000 81.35000 ? 219 GLU A C   1 
ATOM   1621 O  O   . GLU A 1 225 ? -21.51500 -15.32900 26.48500 1.000 76.52000 ? 219 GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 225 ? -21.40700 -12.93600 24.26200 1.000 80.50000 ? 219 GLU A CB  1 
ATOM   1623 C  CG  . GLU A 1 225 ? -21.86700 -11.69300 23.53600 1.000 80.73000 ? 219 GLU A CG  1 
ATOM   1624 C  CD  . GLU A 1 225 ? -20.83500 -11.20700 22.53300 1.000 85.84000 ? 219 GLU A CD  1 
ATOM   1625 O  OE1 . GLU A 1 225 ? -19.75300 -11.82000 22.46600 1.000 79.14000 ? 219 GLU A OE1 1 
ATOM   1626 O  OE2 . GLU A 1 225 ? -21.11500 -10.22500 21.82500 1.000 93.53000 ? 219 GLU A OE2 1 
ATOM   1627 N  N   . GLY A 1 226 ? -22.30900 -15.87000 24.40900 1.000 78.69000 ? 220 GLY A N   1 
ATOM   1628 C  CA  . GLY A 1 226 ? -21.91000 -17.28100 24.51300 1.000 76.06000 ? 220 GLY A CA  1 
ATOM   1629 C  C   . GLY A 1 226 ? -20.40400 -17.39900 24.58800 1.000 75.64000 ? 220 GLY A C   1 
ATOM   1630 O  O   . GLY A 1 226 ? -19.75600 -17.35700 23.53500 1.000 76.78000 ? 220 GLY A O   1 
ATOM   1631 N  N   . GLN A 1 227 ? -19.87100 -17.54800 25.79600 1.000 71.13000 ? 221 GLN A N   1 
ATOM   1632 C  CA  . GLN A 1 227 ? -18.39900 -17.57200 25.93600 1.000 61.90000 ? 221 GLN A CA  1 
ATOM   1633 C  C   . GLN A 1 227 ? -17.93500 -18.94400 26.37000 1.000 62.53000 ? 221 GLN A C   1 
ATOM   1634 O  O   . GLN A 1 227 ? -18.52900 -19.52400 27.28800 1.000 63.54000 ? 221 GLN A O   1 
ATOM   1635 C  CB  . GLN A 1 227 ? -17.92200 -16.57900 26.99400 1.000 55.90000 ? 221 GLN A CB  1 
ATOM   1636 C  CG  . GLN A 1 227 ? -17.71200 -15.17300 26.46600 1.000 53.60000 ? 221 GLN A CG  1 
ATOM   1637 C  CD  . GLN A 1 227 ? -17.08900 -14.30200 27.52600 1.000 51.89000 ? 221 GLN A CD  1 
ATOM   1638 O  OE1 . GLN A 1 227 ? -17.22100 -14.55900 28.72000 1.000 50.55000 ? 221 GLN A OE1 1 
ATOM   1639 N  NE2 . GLN A 1 227 ? -16.40000 -13.26300 27.09100 1.000 39.06000 ? 221 GLN A NE2 1 
ATOM   1640 N  N   . SER A 1 228 ? -16.89500 -19.42700 25.72100 1.000 58.38000 ? 222 SER A N   1 
ATOM   1641 C  CA  . SER A 1 228 ? -16.29700 -20.66700 26.17400 1.000 50.09000 ? 222 SER A CA  1 
ATOM   1642 C  C   . SER A 1 228 ? -15.70600 -20.47500 27.56800 1.000 47.94000 ? 222 SER A C   1 
ATOM   1643 O  O   . SER A 1 228 ? -15.54200 -19.35000 28.07000 1.000 47.20000 ? 222 SER A O   1 
ATOM   1644 C  CB  . SER A 1 228 ? -15.21500 -21.12100 25.19900 1.000 49.61000 ? 222 SER A CB  1 
ATOM   1645 O  OG  . SER A 1 228 ? -14.22800 -20.11100 25.08100 1.000 50.29000 ? 222 SER A OG  1 
ATOM   1646 N  N   . THR A 1 229 ? -15.38300 -21.60100 28.20000 1.000 44.90000 ? 223 THR A N   1 
ATOM   1647 C  CA  . THR A 1 229 ? -14.66500 -21.54700 29.46100 1.000 38.91000 ? 223 THR A CA  1 
ATOM   1648 C  C   . THR A 1 229 ? -13.40400 -20.69900 29.33000 1.000 40.15000 ? 223 THR A C   1 
ATOM   1649 O  O   . THR A 1 229 ? -13.07500 -19.93800 30.24300 1.000 36.03000 ? 223 THR A O   1 
ATOM   1650 C  CB  . THR A 1 229 ? -14.32200 -22.96400 29.92700 1.000 41.70000 ? 223 THR A CB  1 
ATOM   1651 O  OG1 . THR A 1 229 ? -13.52800 -23.62100 28.92500 1.000 40.95000 ? 223 THR A OG1 1 
ATOM   1652 C  CG2 . THR A 1 229 ? -15.60100 -23.78300 30.19200 1.000 42.14000 ? 223 THR A CG2 1 
ATOM   1653 N  N   . ARG A 1 230 ? -12.69000 -20.79700 28.19400 1.000 37.43000 ? 224 ARG A N   1 
ATOM   1654 C  CA  . ARG A 1 230 ? -11.46900 -19.99900 28.05300 1.000 39.20000 ? 224 ARG A CA  1 
ATOM   1655 C  C   . ARG A 1 230 ? -11.78200 -18.50800 27.96900 1.000 37.36000 ? 224 ARG A C   1 
ATOM   1656 O  O   . ARG A 1 230 ? -11.11300 -17.68700 28.62000 1.000 35.06000 ? 224 ARG A O   1 
ATOM   1657 C  CB  . ARG A 1 230 ? -10.65300 -20.42700 26.83300 1.000 37.60000 ? 224 ARG A CB  1 
ATOM   1658 C  CG  . ARG A 1 230 ? -9.44900  -19.48200 26.61100 1.000 33.33000 ? 224 ARG A CG  1 
ATOM   1659 C  CD  . ARG A 1 230 ? -8.41400  -20.13000 25.74300 1.000 34.51000 ? 224 ARG A CD  1 
ATOM   1660 N  NE  . ARG A 1 230 ? -7.83500  -21.30100 26.39000 1.000 34.22000 ? 224 ARG A NE  1 
ATOM   1661 C  CZ  . ARG A 1 230 ? -6.78500  -21.96500 25.92100 1.000 38.43000 ? 224 ARG A CZ  1 
ATOM   1662 N  NH1 . ARG A 1 230 ? -6.21800  -21.63800 24.77100 1.000 37.58000 ? 224 ARG A NH1 1 
ATOM   1663 N  NH2 . ARG A 1 230 ? -6.28900  -22.98400 26.62700 1.000 38.30000 ? 224 ARG A NH2 1 
ATOM   1664 N  N   . CYS A 1 231 ? -12.78700 -18.12700 27.17300 1.000 36.87000 ? 225 CYS A N   1 
ATOM   1665 C  CA  . CYS A 1 231 ? -13.11400 -16.71200 27.10500 1.000 37.32000 ? 225 CYS A CA  1 
ATOM   1666 C  C   . CYS A 1 231 ? -13.57200 -16.20600 28.46000 1.000 35.66000 ? 225 CYS A C   1 
ATOM   1667 O  O   . CYS A 1 231 ? -13.22100 -15.09100 28.86100 1.000 33.43000 ? 225 CYS A O   1 
ATOM   1668 C  CB  . CYS A 1 231 ? -14.16500 -16.45300 26.03400 1.000 41.23000 ? 225 CYS A CB  1 
ATOM   1669 S  SG  . CYS A 1 231 ? -13.41100 -16.15400 24.42800 1.000 51.96000 ? 225 CYS A SG  1 
ATOM   1670 N  N   . ALA A 1 232 ? -14.32200 -17.02900 29.19700 1.000 38.35000 ? 226 ALA A N   1 
ATOM   1671 C  CA  . ALA A 1 232 ? -14.78200 -16.62800 30.52600 1.000 37.26000 ? 226 ALA A CA  1 
ATOM   1672 C  C   . ALA A 1 232 ? -13.60400 -16.36000 31.45900 1.000 34.55000 ? 226 ALA A C   1 
ATOM   1673 O  O   . ALA A 1 232 ? -13.61500 -15.39000 32.23000 1.000 36.16000 ? 226 ALA A O   1 
ATOM   1674 C  CB  . ALA A 1 232 ? -15.71500 -17.69800 31.10800 1.000 36.29000 ? 226 ALA A CB  1 
ATOM   1675 N  N   . ALA A 1 233 ? -12.56800 -17.19900 31.39700 1.000 34.67000 ? 227 ALA A N   1 
ATOM   1676 C  CA  . ALA A 1 233 ? -11.41300 -16.98200 32.24500 1.000 28.57000 ? 227 ALA A CA  1 
ATOM   1677 C  C   . ALA A 1 233 ? -10.58500 -15.79100 31.76600 1.000 31.85000 ? 227 ALA A C   1 
ATOM   1678 O  O   . ALA A 1 233 ? -9.99600  -15.09000 32.59700 1.000 28.51000 ? 227 ALA A O   1 
ATOM   1679 C  CB  . ALA A 1 233 ? -10.55600 -18.24600 32.30500 1.000 30.14000 ? 227 ALA A CB  1 
ATOM   1680 N  N   . LEU A 1 234 ? -10.50200 -15.55200 30.44600 1.000 26.80000 ? 228 LEU A N   1 
ATOM   1681 C  CA  . LEU A 1 234 ? -9.80100  -14.35500 29.98700 1.000 27.55000 ? 228 LEU A CA  1 
ATOM   1682 C  C   . LEU A 1 234 ? -10.49900 -13.10500 30.50100 1.000 33.09000 ? 228 LEU A C   1 
ATOM   1683 O  O   . LEU A 1 234 ? -9.85000  -12.15200 30.95700 1.000 26.61000 ? 228 LEU A O   1 
ATOM   1684 C  CB  . LEU A 1 234 ? -9.73600  -14.32800 28.47000 1.000 30.20000 ? 228 LEU A CB  1 
ATOM   1685 C  CG  . LEU A 1 234 ? -8.84400  -15.37600 27.83700 1.000 27.47000 ? 228 LEU A CG  1 
ATOM   1686 C  CD1 . LEU A 1 234 ? -9.08700  -15.38900 26.37800 1.000 29.72000 ? 228 LEU A CD1 1 
ATOM   1687 C  CD2 . LEU A 1 234 ? -7.40900  -14.99000 28.17600 1.000 28.44000 ? 228 LEU A CD2 1 
ATOM   1688 N  N   . ALA A 1 235 ? -11.83300 -13.10700 30.44900 1.000 28.04000 ? 229 ALA A N   1 
ATOM   1689 C  CA  . ALA A 1 235 ? -12.61000 -12.00900 31.00200 1.000 28.64000 ? 229 ALA A CA  1 
ATOM   1690 C  C   . ALA A 1 235 ? -12.34100 -11.83500 32.48800 1.000 27.44000 ? 229 ALA A C   1 
ATOM   1691 O  O   . ALA A 1 235 ? -12.29000 -10.70600 32.99300 1.000 33.10000 ? 229 ALA A O   1 
ATOM   1692 C  CB  . ALA A 1 235 ? -14.10000 -12.26000 30.76000 1.000 30.04000 ? 229 ALA A CB  1 
ATOM   1693 N  N   . HIS A 1 236 ? -12.20900 -12.94000 33.21700 1.000 28.73000 ? 230 HIS A N   1 
ATOM   1694 C  CA  . HIS A 1 236 ? -11.94400 -12.83400 34.64300 1.000 28.03000 ? 230 HIS A CA  1 
ATOM   1695 C  C   . HIS A 1 236 ? -10.58000 -12.19400 34.89500 1.000 29.23000 ? 230 HIS A C   1 
ATOM   1696 O  O   . HIS A 1 236 ? -10.44000 -11.31200 35.75300 1.000 28.74000 ? 230 HIS A O   1 
ATOM   1697 C  CB  . HIS A 1 236 ? -12.02400 -14.21500 35.28400 1.000 30.27000 ? 230 HIS A CB  1 
ATOM   1698 C  CG  . HIS A 1 236 ? -12.15500 -14.18100 36.77400 1.000 35.71000 ? 230 HIS A CG  1 
ATOM   1699 N  ND1 . HIS A 1 236 ? -12.30800 -15.32200 37.53100 1.000 37.30000 ? 230 HIS A ND1 1 
ATOM   1700 C  CD2 . HIS A 1 236 ? -12.17600 -13.14300 37.64700 1.000 36.68000 ? 230 HIS A CD2 1 
ATOM   1701 C  CE1 . HIS A 1 236 ? -12.41300 -14.98900 38.80600 1.000 38.93000 ? 230 HIS A CE1 1 
ATOM   1702 N  NE2 . HIS A 1 236 ? -12.33800 -13.67200 38.90400 1.000 39.45000 ? 230 HIS A NE2 1 
ATOM   1703 N  N   . ILE A 1 237 ? -9.56900  -12.60200 34.13200 1.000 28.59000 ? 231 ILE A N   1 
ATOM   1704 C  CA  . ILE A 1 237 ? -8.23900  -12.01500 34.27700 1.000 26.29000 ? 231 ILE A CA  1 
ATOM   1705 C  C   . ILE A 1 237 ? -8.28600  -10.51600 34.01400 1.000 24.86000 ? 231 ILE A C   1 
ATOM   1706 O  O   . ILE A 1 237 ? -7.74200  -9.71800  34.78000 1.000 27.87000 ? 231 ILE A O   1 
ATOM   1707 C  CB  . ILE A 1 237 ? -7.25000  -12.72600 33.34100 1.000 26.92000 ? 231 ILE A CB  1 
ATOM   1708 C  CG1 . ILE A 1 237 ? -7.04300  -14.16200 33.84500 1.000 25.47000 ? 231 ILE A CG1 1 
ATOM   1709 C  CG2 . ILE A 1 237 ? -5.94800  -11.95800 33.27700 1.000 21.23000 ? 231 ILE A CG2 1 
ATOM   1710 C  CD1 . ILE A 1 237 ? -6.30300  -15.06800 32.86300 1.000 24.95000 ? 231 ILE A CD1 1 
ATOM   1711 N  N   . PHE A 1 238 ? -8.96100  -10.10500 32.94300 1.000 26.94000 ? 232 PHE A N   1 
ATOM   1712 C  CA  . PHE A 1 238 ? -9.05100  -8.68000  32.66200 1.000 25.76000 ? 232 PHE A CA  1 
ATOM   1713 C  C   . PHE A 1 238 ? -9.73600  -7.94000  33.81700 1.000 29.84000 ? 232 PHE A C   1 
ATOM   1714 O  O   . PHE A 1 238 ? -9.23000  -6.91500  34.28700 1.000 25.45000 ? 232 PHE A O   1 
ATOM   1715 C  CB  . PHE A 1 238 ? -9.75800  -8.46100  31.32400 1.000 25.51000 ? 232 PHE A CB  1 
ATOM   1716 C  CG  . PHE A 1 238 ? -9.87900  -7.01600  30.92700 1.000 28.94000 ? 232 PHE A CG  1 
ATOM   1717 C  CD1 . PHE A 1 238 ? -10.78700 -6.18000  31.56500 1.000 26.93000 ? 232 PHE A CD1 1 
ATOM   1718 C  CD2 . PHE A 1 238 ? -9.09400  -6.49300  29.90600 1.000 29.00000 ? 232 PHE A CD2 1 
ATOM   1719 C  CE1 . PHE A 1 238 ? -10.89900 -4.84400  31.21200 1.000 26.45000 ? 232 PHE A CE1 1 
ATOM   1720 C  CE2 . PHE A 1 238 ? -9.19300  -5.14200  29.54000 1.000 25.72000 ? 232 PHE A CE2 1 
ATOM   1721 C  CZ  . PHE A 1 238 ? -10.12400 -4.32500  30.19700 1.000 24.56000 ? 232 PHE A CZ  1 
ATOM   1722 N  N   . ARG A 1 239 ? -10.88200 -8.45100  34.29400 1.000 25.95000 ? 233 ARG A N   1 
ATOM   1723 C  CA  A ARG A 1 239 ? -11.59900 -7.81300  35.40100 0.500 30.35000 ? 233 ARG A CA  1 
ATOM   1724 C  CA  B ARG A 1 239 ? -11.58700 -7.78800  35.39300 0.500 30.34000 ? 233 ARG A CA  1 
ATOM   1725 C  C   . ARG A 1 239 ? -10.73900 -7.74000  36.66200 1.000 31.68000 ? 233 ARG A C   1 
ATOM   1726 O  O   . ARG A 1 239 ? -10.71700 -6.71500  37.35600 1.000 29.68000 ? 233 ARG A O   1 
ATOM   1727 C  CB  A ARG A 1 239 ? -12.89800 -8.57300  35.68700 0.500 30.50000 ? 233 ARG A CB  1 
ATOM   1728 C  CB  B ARG A 1 239 ? -12.92700 -8.47500  35.67700 0.500 30.50000 ? 233 ARG A CB  1 
ATOM   1729 C  CG  A ARG A 1 239 ? -13.66500 -8.10100  36.91100 0.500 33.84000 ? 233 ARG A CG  1 
ATOM   1730 C  CG  B ARG A 1 239 ? -14.05800 -8.07200  34.73300 0.500 33.45000 ? 233 ARG A CG  1 
ATOM   1731 C  CD  A ARG A 1 239 ? -13.99400 -9.26600  37.84700 0.500 37.43000 ? 233 ARG A CD  1 
ATOM   1732 C  CD  B ARG A 1 239 ? -15.38500 -8.68400  35.16500 0.500 33.61000 ? 233 ARG A CD  1 
ATOM   1733 N  NE  A ARG A 1 239 ? -15.42500 -9.44500  38.03400 0.500 38.25000 ? 233 ARG A NE  1 
ATOM   1734 N  NE  B ARG A 1 239 ? -15.22400 -10.03100 35.71200 0.500 36.64000 ? 233 ARG A NE  1 
ATOM   1735 C  CZ  A ARG A 1 239 ? -15.99100 -10.46800 38.66500 0.500 39.52000 ? 233 ARG A CZ  1 
ATOM   1736 C  CZ  B ARG A 1 239 ? -15.49100 -11.15700 35.06000 0.500 33.25000 ? 233 ARG A CZ  1 
ATOM   1737 N  NH1 A ARG A 1 239 ? -15.27000 -11.43100 39.22300 0.500 35.70000 ? 233 ARG A NH1 1 
ATOM   1738 N  NH1 B ARG A 1 239 ? -15.94500 -11.14700 33.81800 0.500 32.45000 ? 233 ARG A NH1 1 
ATOM   1739 N  NH2 A ARG A 1 239 ? -17.31600 -10.53000 38.73200 0.500 37.12000 ? 233 ARG A NH2 1 
ATOM   1740 N  NH2 B ARG A 1 239 ? -15.30900 -12.32000 35.67700 0.500 30.58000 ? 233 ARG A NH2 1 
ATOM   1741 N  N   . ALA A 1 240 ? -10.01900 -8.82400  36.98200 1.000 30.40000 ? 234 ALA A N   1 
ATOM   1742 C  CA  . ALA A 1 240 ? -9.19100  -8.81400  38.19000 1.000 26.90000 ? 234 ALA A CA  1 
ATOM   1743 C  C   . ALA A 1 240 ? -8.09600  -7.75300  38.11800 1.000 27.70000 ? 234 ALA A C   1 
ATOM   1744 O  O   . ALA A 1 240 ? -7.84900  -7.04600  39.10300 1.000 25.59000 ? 234 ALA A O   1 
ATOM   1745 C  CB  . ALA A 1 240 ? -8.56900  -10.18900 38.42400 1.000 26.01000 ? 234 ALA A CB  1 
ATOM   1746 N  N   . MET A 1 241 ? -7.42200  -7.62800  36.97000 1.000 23.91000 ? 235 MET A N   1 
ATOM   1747 C  CA  . MET A 1 241 ? -6.36700  -6.62200  36.84700 1.000 25.42000 ? 235 MET A CA  1 
ATOM   1748 C  C   . MET A 1 241 ? -6.93000  -5.20900  36.90600 1.000 25.36000 ? 235 MET A C   1 
ATOM   1749 O  O   . MET A 1 241 ? -6.37500  -4.34300  37.58800 1.000 24.20000 ? 235 MET A O   1 
ATOM   1750 C  CB  . MET A 1 241 ? -5.58300  -6.82000  35.54600 1.000 24.62000 ? 235 MET A CB  1 
ATOM   1751 C  CG  . MET A 1 241 ? -4.78100  -8.10200  35.50100 1.000 23.00000 ? 235 MET A CG  1 
ATOM   1752 S  SD  . MET A 1 241 ? -4.03000  -8.37300  33.86500 1.000 23.56000 ? 235 MET A SD  1 
ATOM   1753 C  CE  . MET A 1 241 ? -2.63800  -7.22400  33.90300 1.000 17.90000 ? 235 MET A CE  1 
ATOM   1754 N  N   . ALA A 1 242 ? -8.03000  -4.95600  36.20000 1.000 25.85000 ? 236 ALA A N   1 
ATOM   1755 C  CA  . ALA A 1 242 ? -8.57800  -3.60800  36.16800 1.000 27.45000 ? 236 ALA A CA  1 
ATOM   1756 C  C   . ALA A 1 242 ? -9.12200  -3.19700  37.52600 1.000 31.58000 ? 236 ALA A C   1 
ATOM   1757 O  O   . ALA A 1 242 ? -9.04600  -2.01600  37.88800 1.000 30.76000 ? 236 ALA A O   1 
ATOM   1758 C  CB  . ALA A 1 242 ? -9.67300  -3.50900  35.11200 1.000 27.15000 ? 236 ALA A CB  1 
ATOM   1759 N  N   . ARG A 1 243 ? -9.64800  -4.15300  38.29200 1.000 29.28000 ? 237 ARG A N   1 
ATOM   1760 C  CA  . ARG A 1 243 ? -10.23300 -3.86400  39.59200 1.000 26.98000 ? 237 ARG A CA  1 
ATOM   1761 C  C   . ARG A 1 243 ? -9.19500  -3.79700  40.71700 1.000 32.34000 ? 237 ARG A C   1 
ATOM   1762 O  O   . ARG A 1 243 ? -9.42500  -3.12100  41.73100 1.000 31.17000 ? 237 ARG A O   1 
ATOM   1763 C  CB  . ARG A 1 243 ? -11.30000 -4.90700  39.91900 1.000 36.56000 ? 237 ARG A CB  1 
ATOM   1764 C  CG  . ARG A 1 243 ? -12.60400 -4.74400  39.11500 1.000 43.18000 ? 237 ARG A CG  1 
ATOM   1765 C  CD  . ARG A 1 243 ? -13.63800 -5.77000  39.55800 1.000 49.07000 ? 237 ARG A CD  1 
ATOM   1766 N  NE  . ARG A 1 243 ? -13.42600 -6.12900  40.96100 1.000 56.50000 ? 237 ARG A NE  1 
ATOM   1767 C  CZ  . ARG A 1 243 ? -13.92200 -7.20800  41.55900 1.000 56.70000 ? 237 ARG A CZ  1 
ATOM   1768 N  NH1 . ARG A 1 243 ? -14.70500 -8.06300  40.90700 1.000 56.19000 ? 237 ARG A NH1 1 
ATOM   1769 N  NH2 . ARG A 1 243 ? -13.62100 -7.43900  42.84400 1.000 53.15000 ? 237 ARG A NH2 1 
ATOM   1770 N  N   . HIS A 1 244 ? -8.05200  -4.46300  40.58000 1.000 29.94000 ? 238 HIS A N   1 
ATOM   1771 C  CA  . HIS A 1 244 ? -7.00200  -4.39800  41.59500 1.000 27.39000 ? 238 HIS A CA  1 
ATOM   1772 C  C   . HIS A 1 244 ? -5.66100  -4.04000  40.95900 1.000 26.53000 ? 238 HIS A C   1 
ATOM   1773 O  O   . HIS A 1 244 ? -4.68600  -4.78100  41.06900 1.000 25.11000 ? 238 HIS A O   1 
ATOM   1774 C  CB  . HIS A 1 244 ? -6.94300  -5.72200  42.35000 1.000 27.97000 ? 238 HIS A CB  1 
ATOM   1775 C  CG  . HIS A 1 244 ? -8.25100  -6.09900  42.97300 1.000 31.85000 ? 238 HIS A CG  1 
ATOM   1776 N  ND1 . HIS A 1 244 ? -8.60800  -5.70000  44.24700 1.000 34.56000 ? 238 HIS A ND1 1 
ATOM   1777 C  CD2 . HIS A 1 244 ? -9.30400  -6.80500  42.49000 1.000 30.39000 ? 238 HIS A CD2 1 
ATOM   1778 C  CE1 . HIS A 1 244 ? -9.81500  -6.16400  44.53100 1.000 32.53000 ? 238 HIS A CE1 1 
ATOM   1779 N  NE2 . HIS A 1 244 ? -10.26200 -6.83300  43.48000 1.000 35.85000 ? 238 HIS A NE2 1 
ATOM   1780 N  N   . PRO A 1 245 ? -5.57100  -2.88000  40.30300 1.000 28.70000 ? 239 PRO A N   1 
ATOM   1781 C  CA  . PRO A 1 245 ? -4.31700  -2.53300  39.61800 1.000 25.58000 ? 239 PRO A CA  1 
ATOM   1782 C  C   . PRO A 1 245 ? -3.13600  -2.35300  40.56500 1.000 27.83000 ? 239 PRO A C   1 
ATOM   1783 O  O   . PRO A 1 245 ? -1.98000  -2.44900  40.12700 1.000 23.66000 ? 239 PRO A O   1 
ATOM   1784 C  CB  . PRO A 1 245 ? -4.66500  -1.23100  38.89400 1.000 27.44000 ? 239 PRO A CB  1 
ATOM   1785 C  CG  . PRO A 1 245 ? -5.75400  -0.62700  39.73100 1.000 29.46000 ? 239 PRO A CG  1 
ATOM   1786 C  CD  . PRO A 1 245 ? -6.56800  -1.79000  40.24100 1.000 28.98000 ? 239 PRO A CD  1 
ATOM   1787 N  N   . GLU A 1 246 ? -3.38600  -2.09100  41.85100 1.000 29.25000 ? 240 GLU A N   1 
ATOM   1788 C  CA  . GLU A 1 246 ? -2.27000  -1.95400  42.77500 1.000 29.38000 ? 240 GLU A CA  1 
ATOM   1789 C  C   . GLU A 1 246 ? -1.63900  -3.29200  43.09500 1.000 27.46000 ? 240 GLU A C   1 
ATOM   1790 O  O   . GLU A 1 246 ? -0.47900  -3.32300  43.51500 1.000 25.67000 ? 240 GLU A O   1 
ATOM   1791 C  CB  . GLU A 1 246 ? -2.71000  -1.28400  44.06900 1.000 32.00000 ? 240 GLU A CB  1 
ATOM   1792 C  CG  . GLU A 1 246 ? -3.61900  -2.15100  44.86600 1.000 38.73000 ? 240 GLU A CG  1 
ATOM   1793 C  CD  . GLU A 1 246 ? -5.06100  -2.08400  44.38300 1.000 40.50000 ? 240 GLU A CD  1 
ATOM   1794 O  OE1 . GLU A 1 246 ? -5.39700  -1.13100  43.61900 1.000 42.43000 ? 240 GLU A OE1 1 
ATOM   1795 O  OE2 . GLU A 1 246 ? -5.85000  -2.97300  44.79000 1.000 43.20000 ? 240 GLU A OE2 1 
ATOM   1796 N  N   . MET A 1 247 ? -2.37900  -4.39200  42.93400 1.000 25.80000 ? 241 MET A N   1 
ATOM   1797 C  CA  . MET A 1 247 ? -1.75000  -5.70000  43.04900 1.000 25.36000 ? 241 MET A CA  1 
ATOM   1798 C  C   . MET A 1 247 ? -0.89700  -5.99600  41.82300 1.000 23.65000 ? 241 MET A C   1 
ATOM   1799 O  O   . MET A 1 247 ? 0.11200   -6.69400  41.93000 1.000 23.50000 ? 241 MET A O   1 
ATOM   1800 C  CB  . MET A 1 247 ? -2.80100  -6.80400  43.22500 1.000 24.82000 ? 241 MET A CB  1 
ATOM   1801 C  CG  . MET A 1 247 ? -3.60900  -6.76700  44.52700 1.000 27.87000 ? 241 MET A CG  1 
ATOM   1802 S  SD  . MET A 1 247 ? -2.54800  -7.04600  45.96700 1.000 32.94000 ? 241 MET A SD  1 
ATOM   1803 C  CE  . MET A 1 247 ? -2.43800  -5.39800  46.69600 1.000 31.88000 ? 241 MET A CE  1 
ATOM   1804 N  N   . VAL A 1 248 ? -1.28400  -5.48600  40.65200 1.000 25.01000 ? 242 VAL A N   1 
ATOM   1805 C  CA  . VAL A 1 248 ? -0.50700  -5.77700  39.45500 1.000 22.13000 ? 242 VAL A CA  1 
ATOM   1806 C  C   . VAL A 1 248 ? 0.84700   -5.09400  39.50800 1.000 24.50000 ? 242 VAL A C   1 
ATOM   1807 O  O   . VAL A 1 248 ? 1.79900   -5.56000  38.87200 1.000 25.93000 ? 242 VAL A O   1 
ATOM   1808 C  CB  . VAL A 1 248 ? -1.30700  -5.38300  38.19300 1.000 26.94000 ? 242 VAL A CB  1 
ATOM   1809 C  CG1 . VAL A 1 248 ? -0.48000  -5.66100  36.89700 1.000 24.40000 ? 242 VAL A CG1 1 
ATOM   1810 C  CG2 . VAL A 1 248 ? -2.65800  -6.14600  38.15100 1.000 21.07000 ? 242 VAL A CG2 1 
ATOM   1811 N  N   . ALA A 1 249 ? 0.97700   -4.00300  40.26400 1.000 24.31000 ? 243 ALA A N   1 
ATOM   1812 C  CA  . ALA A 1 249 ? 2.25500   -3.30200  40.36600 1.000 22.00000 ? 243 ALA A CA  1 
ATOM   1813 C  C   . ALA A 1 249 ? 2.41100   -2.68900  41.74500 1.000 22.74000 ? 243 ALA A C   1 
ATOM   1814 O  O   . ALA A 1 249 ? 2.98300   -3.32500  42.63300 1.000 25.35000 ? 243 ALA A O   1 
ATOM   1815 C  CB  . ALA A 1 249 ? 2.38900   -2.23300  39.27600 1.000 19.99000 ? 243 ALA A CB  1 
ATOM   1816 N  N   . GLY A 1 250 ? 1.91400   -1.47400  41.94700 1.000 24.53000 ? 244 GLY A N   1 
ATOM   1817 C  CA  . GLY A 1 250 ? 1.94200   -0.87700  43.26800 1.000 26.32000 ? 244 GLY A CA  1 
ATOM   1818 C  C   . GLY A 1 250 ? 1.82300   0.63500   43.18900 1.000 27.65000 ? 244 GLY A C   1 
ATOM   1819 O  O   . GLY A 1 250 ? 1.59000   1.20800   42.12600 1.000 25.59000 ? 244 GLY A O   1 
ATOM   1820 N  N   . GLU A 1 251 ? 1.99600   1.26700   44.34200 1.000 30.26000 ? 245 GLU A N   1 
ATOM   1821 C  CA  . GLU A 1 251 ? 1.83200   2.71500   44.43600 1.000 33.60000 ? 245 GLU A CA  1 
ATOM   1822 C  C   . GLU A 1 251 ? 2.87200   3.43300   43.57400 1.000 26.95000 ? 245 GLU A C   1 
ATOM   1823 O  O   . GLU A 1 251 ? 4.05900   3.12200   43.62000 1.000 25.46000 ? 245 GLU A O   1 
ATOM   1824 C  CB  . GLU A 1 251 ? 1.94800   3.15800   45.90200 1.000 36.18000 ? 245 GLU A CB  1 
ATOM   1825 C  CG  . GLU A 1 251 ? 1.18800   4.44700   46.25500 1.000 45.55000 ? 245 GLU A CG  1 
ATOM   1826 C  CD  . GLU A 1 251 ? -0.33200  4.33800   46.02200 1.000 50.90000 ? 245 GLU A CD  1 
ATOM   1827 O  OE1 . GLU A 1 251 ? -0.92100  3.21400   46.10700 1.000 52.88000 ? 245 GLU A OE1 1 
ATOM   1828 O  OE2 . GLU A 1 251 ? -0.93600  5.39600   45.73200 1.000 56.65000 ? 245 GLU A OE2 1 
ATOM   1829 N  N   . GLY A 1 252 ? 2.42200   4.39500   42.77900 1.000 27.26000 ? 246 GLY A N   1 
ATOM   1830 C  CA  . GLY A 1 252 ? 3.34100   5.15200   41.95300 1.000 29.01000 ? 246 GLY A CA  1 
ATOM   1831 C  C   . GLY A 1 252 ? 3.82800   4.43900   40.70800 1.000 29.49000 ? 246 GLY A C   1 
ATOM   1832 O  O   . GLY A 1 252 ? 4.59300   5.03300   39.93400 1.000 25.60000 ? 246 GLY A O   1 
ATOM   1833 N  N   . ARG A 1 253 ? 3.44600   3.18100   40.50400 1.000 19.73000 ? 247 ARG A N   1 
ATOM   1834 C  CA  . ARG A 1 253 ? 3.92300   2.43200   39.35800 1.000 22.21000 ? 247 ARG A CA  1 
ATOM   1835 C  C   . ARG A 1 253 ? 3.07400   2.74800   38.12400 1.000 26.74000 ? 247 ARG A C   1 
ATOM   1836 O  O   . ARG A 1 253 ? 1.86000   2.95400   38.21700 1.000 24.03000 ? 247 ARG A O   1 
ATOM   1837 C  CB  . ARG A 1 253 ? 3.87400   0.93300   39.66800 1.000 22.26000 ? 247 ARG A CB  1 
ATOM   1838 C  CG  . ARG A 1 253 ? 4.80000   0.48800   40.79100 1.000 22.44000 ? 247 ARG A CG  1 
ATOM   1839 C  CD  . ARG A 1 253 ? 6.21900   0.17300   40.23400 1.000 22.68000 ? 247 ARG A CD  1 
ATOM   1840 N  NE  . ARG A 1 253 ? 6.20300   -0.74100  39.08800 1.000 22.03000 ? 247 ARG A NE  1 
ATOM   1841 C  CZ  . ARG A 1 253 ? 6.06600   -2.06000  39.18000 1.000 24.35000 ? 247 ARG A CZ  1 
ATOM   1842 N  NH1 . ARG A 1 253 ? 5.92100   -2.65800  40.35300 1.000 21.29000 ? 247 ARG A NH1 1 
ATOM   1843 N  NH2 . ARG A 1 253 ? 6.00700   -2.79200  38.06400 1.000 19.36000 ? 247 ARG A NH2 1 
ATOM   1844 N  N   . TYR A 1 254 ? 3.71900   2.73900   36.95400 1.000 24.65000 ? 248 TYR A N   1 
ATOM   1845 C  CA  . TYR A 1 254 ? 3.02000   3.09900   35.72000 1.000 24.55000 ? 248 TYR A CA  1 
ATOM   1846 C  C   . TYR A 1 254 ? 1.77700   2.24500   35.49400 1.000 21.40000 ? 248 TYR A C   1 
ATOM   1847 O  O   . TYR A 1 254 ? 0.71100   2.77200   35.15000 1.000 21.65000 ? 248 TYR A O   1 
ATOM   1848 C  CB  . TYR A 1 254 ? 3.96800   2.98500   34.51100 1.000 21.69000 ? 248 TYR A CB  1 
ATOM   1849 C  CG  . TYR A 1 254 ? 3.32600   3.48700   33.23500 1.000 18.21000 ? 248 TYR A CG  1 
ATOM   1850 C  CD1 . TYR A 1 254 ? 3.29100   4.84500   32.93900 1.000 20.01000 ? 248 TYR A CD1 1 
ATOM   1851 C  CD2 . TYR A 1 254 ? 2.74600   2.61400   32.35000 1.000 19.00000 ? 248 TYR A CD2 1 
ATOM   1852 C  CE1 . TYR A 1 254 ? 2.68400   5.30800   31.78000 1.000 22.70000 ? 248 TYR A CE1 1 
ATOM   1853 C  CE2 . TYR A 1 254 ? 2.14400   3.05400   31.18100 1.000 22.04000 ? 248 TYR A CE2 1 
ATOM   1854 C  CZ  . TYR A 1 254 ? 2.11700   4.40500   30.90000 1.000 21.38000 ? 248 TYR A CZ  1 
ATOM   1855 O  OH  . TYR A 1 254 ? 1.49300   4.83900   29.74500 1.000 20.76000 ? 248 TYR A OH  1 
ATOM   1856 N  N   . CYS A 1 255 ? 1.88200   0.91500   35.65400 1.000 21.70000 ? 249 CYS A N   1 
ATOM   1857 C  CA  . CYS A 1 255 ? 0.72900   0.06700   35.33100 1.000 22.84000 ? 249 CYS A CA  1 
ATOM   1858 C  C   . CYS A 1 255 ? -0.43000  0.37500   36.25800 1.000 24.00000 ? 249 CYS A C   1 
ATOM   1859 O  O   . CYS A 1 255 ? -1.60000  0.35200   35.84300 1.000 24.03000 ? 249 CYS A O   1 
ATOM   1860 C  CB  . CYS A 1 255 ? 1.06500   -1.42900  35.44700 1.000 20.45000 ? 249 CYS A CB  1 
ATOM   1861 S  SG  . CYS A 1 255 ? 2.56100   -2.04800  34.72900 1.000 27.26000 ? 249 CYS A SG  1 
ATOM   1862 N  N   . THR A 1 256 ? -0.13000  0.64400   37.53200 1.000 23.20000 ? 250 THR A N   1 
ATOM   1863 C  CA  . THR A 1 256 ? -1.19900  0.93900   38.47800 1.000 23.54000 ? 250 THR A CA  1 
ATOM   1864 C  C   . THR A 1 256 ? -1.85600  2.27500   38.16000 1.000 25.58000 ? 250 THR A C   1 
ATOM   1865 O  O   . THR A 1 256 ? -3.08500  2.43200   38.28200 1.000 25.07000 ? 250 THR A O   1 
ATOM   1866 C  CB  . THR A 1 256 ? -0.63600  0.92600   39.90200 1.000 23.39000 ? 250 THR A CB  1 
ATOM   1867 O  OG1 . THR A 1 256 ? -0.19800  -0.40200  40.22300 1.000 24.49000 ? 250 THR A OG1 1 
ATOM   1868 C  CG2 . THR A 1 256 ? -1.71600  1.35700   40.92700 1.000 29.47000 ? 250 THR A CG2 1 
ATOM   1869 N  N   . MET A 1 257 ? -1.05000  3.25200   37.77600 1.000 25.57000 ? 251 MET A N   1 
ATOM   1870 C  CA  . MET A 1 257 ? -1.59700  4.57100   37.55400 1.000 26.66000 ? 251 MET A CA  1 
ATOM   1871 C  C   . MET A 1 257 ? -2.30100  4.62100   36.21200 1.000 25.16000 ? 251 MET A C   1 
ATOM   1872 O  O   . MET A 1 257 ? -3.33400  5.27500   36.07900 1.000 26.55000 ? 251 MET A O   1 
ATOM   1873 C  CB  . MET A 1 257 ? -0.46900  5.59100   37.65800 1.000 31.38000 ? 251 MET A CB  1 
ATOM   1874 C  CG  . MET A 1 257 ? 0.10300   5.73200   39.09500 1.000 25.81000 ? 251 MET A CG  1 
ATOM   1875 S  SD  . MET A 1 257 ? 1.49000   6.93000   39.12600 1.000 32.93000 ? 251 MET A SD  1 
ATOM   1876 C  CE  . MET A 1 257 ? 0.72200   8.39500   38.38600 1.000 35.16000 ? 251 MET A CE  1 
ATOM   1877 N  N   . LEU A 1 258 ? -1.74900  3.93700   35.20900 1.000 23.82000 ? 252 LEU A N   1 
ATOM   1878 C  CA  . LEU A 1 258 ? -2.44100  3.79900   33.93600 1.000 22.46000 ? 252 LEU A CA  1 
ATOM   1879 C  C   . LEU A 1 258 ? -3.80600  3.15900   34.13100 1.000 26.49000 ? 252 LEU A C   1 
ATOM   1880 O  O   . LEU A 1 258 ? -4.82400  3.67800   33.65100 1.000 27.50000 ? 252 LEU A O   1 
ATOM   1881 C  CB  . LEU A 1 258 ? -1.58000  2.99000   32.95800 1.000 20.60000 ? 252 LEU A CB  1 
ATOM   1882 C  CG  . LEU A 1 258 ? -2.24500  2.52200   31.65500 1.000 23.63000 ? 252 LEU A CG  1 
ATOM   1883 C  CD1 . LEU A 1 258 ? -2.34400  3.66700   30.68400 1.000 25.66000 ? 252 LEU A CD1 1 
ATOM   1884 C  CD2 . LEU A 1 258 ? -1.49600  1.33900   31.05700 1.000 20.83000 ? 252 LEU A CD2 1 
ATOM   1885 N  N   . MET A 1 259 ? -3.87300  2.04600   34.87100 1.000 24.78000 ? 253 MET A N   1 
ATOM   1886 C  CA  . MET A 1 259 ? -5.15900  1.35900   34.95400 1.000 25.09000 ? 253 MET A CA  1 
ATOM   1887 C  C   . MET A 1 259 ? -6.15900  2.13900   35.79400 1.000 27.42000 ? 253 MET A C   1 
ATOM   1888 O  O   . MET A 1 259 ? -7.34800  2.19400   35.45000 1.000 27.27000 ? 253 MET A O   1 
ATOM   1889 C  CB  . MET A 1 259 ? -4.98900  -0.06300  35.48100 1.000 18.93000 ? 253 MET A CB  1 
ATOM   1890 C  CG  . MET A 1 259 ? -4.43100  -0.98700  34.40100 1.000 23.28000 ? 253 MET A CG  1 
ATOM   1891 S  SD  . MET A 1 259 ? -4.44300  -2.77000  34.72500 1.000 23.96000 ? 253 MET A SD  1 
ATOM   1892 C  CE  . MET A 1 259 ? -3.07900  -2.89200  35.89000 1.000 23.37000 ? 253 MET A CE  1 
ATOM   1893 N  N   . ARG A 1 260 ? -5.69800  2.76500   36.88100 1.000 28.35000 ? 254 ARG A N   1 
ATOM   1894 C  CA  . ARG A 1 260 ? -6.57700  3.62400   37.66500 1.000 29.69000 ? 254 ARG A CA  1 
ATOM   1895 C  C   . ARG A 1 260 ? -7.13100  4.76400   36.81300 1.000 28.45000 ? 254 ARG A C   1 
ATOM   1896 O  O   . ARG A 1 260 ? -8.33500  5.03100   36.82600 1.000 31.40000 ? 254 ARG A O   1 
ATOM   1897 C  CB  . ARG A 1 260 ? -5.82800  4.16000   38.89000 1.000 29.97000 ? 254 ARG A CB  1 
ATOM   1898 C  CG  . ARG A 1 260 ? -5.93600  3.22200   40.10000 1.000 37.77000 ? 254 ARG A CG  1 
ATOM   1899 C  CD  . ARG A 1 260 ? -5.10200  3.63700   41.32400 1.000 43.11000 ? 254 ARG A CD  1 
ATOM   1900 N  NE  . ARG A 1 260 ? -5.22500  2.62900   42.38100 1.000 54.61000 ? 254 ARG A NE  1 
ATOM   1901 C  CZ  . ARG A 1 260 ? -4.42400  2.49400   43.43700 1.000 51.01000 ? 254 ARG A CZ  1 
ATOM   1902 N  NH1 . ARG A 1 260 ? -3.41000  3.33400   43.66900 1.000 43.35000 ? 254 ARG A NH1 1 
ATOM   1903 N  NH2 . ARG A 1 260 ? -4.63000  1.47600   44.27000 1.000 51.38000 ? 254 ARG A NH2 1 
ATOM   1904 N  N   . ALA A 1 261 ? -6.26800  5.42400   36.04700 1.000 27.49000 ? 255 ALA A N   1 
ATOM   1905 C  CA  . ALA A 1 261 ? -6.69000  6.53600   35.20200 1.000 28.32000 ? 255 ALA A CA  1 
ATOM   1906 C  C   . ALA A 1 261 ? -7.81200  6.12400   34.27000 1.000 33.79000 ? 255 ALA A C   1 
ATOM   1907 O  O   . ALA A 1 261 ? -8.77800  6.87900   34.07400 1.000 28.32000 ? 255 ALA A O   1 
ATOM   1908 C  CB  . ALA A 1 261 ? -5.50600  7.04300   34.38100 1.000 30.90000 ? 255 ALA A CB  1 
ATOM   1909 N  N   . PHE A 1 262 ? -7.71000  4.91500   33.70000 1.000 28.09000 ? 256 PHE A N   1 
ATOM   1910 C  CA  . PHE A 1 262 ? -8.66800  4.45300   32.70100 1.000 29.42000 ? 256 PHE A CA  1 
ATOM   1911 C  C   . PHE A 1 262 ? -9.89400  3.76000   33.28900 1.000 32.85000 ? 256 PHE A C   1 
ATOM   1912 O  O   . PHE A 1 262 ? -10.91300 3.63900   32.58800 1.000 26.98000 ? 256 PHE A O   1 
ATOM   1913 C  CB  . PHE A 1 262 ? -7.95500  3.56000   31.68600 1.000 28.42000 ? 256 PHE A CB  1 
ATOM   1914 C  CG  . PHE A 1 262 ? -7.27200  4.34900   30.62000 1.000 24.17000 ? 256 PHE A CG  1 
ATOM   1915 C  CD1 . PHE A 1 262 ? -5.96100  4.76500   30.77500 1.000 25.83000 ? 256 PHE A CD1 1 
ATOM   1916 C  CD2 . PHE A 1 262 ? -7.98100  4.76400   29.49300 1.000 31.83000 ? 256 PHE A CD2 1 
ATOM   1917 C  CE1 . PHE A 1 262 ? -5.36600  5.54600   29.81400 1.000 28.06000 ? 256 PHE A CE1 1 
ATOM   1918 C  CE2 . PHE A 1 262 ? -7.37500  5.53800   28.51100 1.000 31.49000 ? 256 PHE A CE2 1 
ATOM   1919 C  CZ  . PHE A 1 262 ? -6.06900  5.93000   28.67000 1.000 30.07000 ? 256 PHE A CZ  1 
ATOM   1920 N  N   . ASP A 1 263 ? -9.83600  3.32300   34.55200 1.000 29.49000 ? 257 ASP A N   1 
ATOM   1921 C  CA  . ASP A 1 263 ? -11.04000 2.96900   35.30500 1.000 33.40000 ? 257 ASP A CA  1 
ATOM   1922 C  C   . ASP A 1 263 ? -11.84600 1.85300   34.62800 1.000 31.95000 ? 257 ASP A C   1 
ATOM   1923 O  O   . ASP A 1 263 ? -13.08400 1.85000   34.63800 1.000 33.65000 ? 257 ASP A O   1 
ATOM   1924 C  CB  . ASP A 1 263 ? -11.89900 4.21800   35.52900 1.000 34.16000 ? 257 ASP A CB  1 
ATOM   1925 C  CG  . ASP A 1 263 ? -13.02000 3.99800   36.55000 1.000 43.32000 ? 257 ASP A CG  1 
ATOM   1926 O  OD1 . ASP A 1 263 ? -12.73000 3.38300   37.60100 1.000 46.36000 ? 257 ASP A OD1 1 
ATOM   1927 O  OD2 . ASP A 1 263 ? -14.17900 4.43600   36.30600 1.000 42.01000 ? 257 ASP A OD2 1 
ATOM   1928 N  N   . GLY A 1 264 ? -11.14200 0.88100   34.05000 1.000 28.47000 ? 258 GLY A N   1 
ATOM   1929 C  CA  . GLY A 1 264 ? -11.76400 -0.28900  33.48200 1.000 25.82000 ? 258 GLY A CA  1 
ATOM   1930 C  C   . GLY A 1 264 ? -11.75700 -0.34900  31.97400 1.000 29.00000 ? 258 GLY A C   1 
ATOM   1931 O  O   . GLY A 1 264 ? -12.14600 -1.38200  31.41200 1.000 30.82000 ? 258 GLY A O   1 
ATOM   1932 N  N   . ALA A 1 265 ? -11.36200 0.71600   31.29300 1.000 28.20000 ? 259 ALA A N   1 
ATOM   1933 C  CA  . ALA A 1 265 ? -11.42000 0.70900   29.84000 1.000 26.44000 ? 259 ALA A CA  1 
ATOM   1934 C  C   . ALA A 1 265 ? -10.25800 -0.05300  29.19700 1.000 29.01000 ? 259 ALA A C   1 
ATOM   1935 O  O   . ALA A 1 265 ? -10.34300 -0.38500  28.00400 1.000 26.15000 ? 259 ALA A O   1 
ATOM   1936 C  CB  . ALA A 1 265 ? -11.45500 2.15500   29.32800 1.000 27.75000 ? 259 ALA A CB  1 
ATOM   1937 N  N   . LEU A 1 266 ? -9.19700  -0.35500  29.95100 1.000 22.99000 ? 260 LEU A N   1 
ATOM   1938 C  CA  . LEU A 1 266 ? -8.06400  -1.10000  29.42400 1.000 23.36000 ? 260 LEU A CA  1 
ATOM   1939 C  C   . LEU A 1 266 ? -7.29700  -1.72600  30.58400 1.000 25.53000 ? 260 LEU A C   1 
ATOM   1940 O  O   . LEU A 1 266 ? -7.45600  -1.33500  31.74600 1.000 21.73000 ? 260 LEU A O   1 
ATOM   1941 C  CB  . LEU A 1 266 ? -7.14900  -0.19000  28.59200 1.000 22.60000 ? 260 LEU A CB  1 
ATOM   1942 C  CG  . LEU A 1 266 ? -6.54100  1.13100   29.10900 1.000 26.07000 ? 260 LEU A CG  1 
ATOM   1943 C  CD1 . LEU A 1 266 ? -5.41000  0.92000   30.17500 1.000 24.11000 ? 260 LEU A CD1 1 
ATOM   1944 C  CD2 . LEU A 1 266 ? -5.97300  1.95100   27.93200 1.000 26.24000 ? 260 LEU A CD2 1 
ATOM   1945 N  N   . VAL A 1 267 ? -6.45400  -2.69200  30.25500 1.000 19.45000 ? 261 VAL A N   1 
ATOM   1946 C  CA  . VAL A 1 267 ? -5.44400  -3.16600  31.19900 1.000 18.51000 ? 261 VAL A CA  1 
ATOM   1947 C  C   . VAL A 1 267 ? -4.09300  -2.99600  30.54400 1.000 19.13000 ? 261 VAL A C   1 
ATOM   1948 O  O   . VAL A 1 267 ? -3.98200  -2.95300  29.31800 1.000 19.41000 ? 261 VAL A O   1 
ATOM   1949 C  CB  . VAL A 1 267 ? -5.64300  -4.63300  31.64500 1.000 21.45000 ? 261 VAL A CB  1 
ATOM   1950 C  CG1 . VAL A 1 267 ? -6.90200  -4.76200  32.47400 1.000 24.30000 ? 261 VAL A CG1 1 
ATOM   1951 C  CG2 . VAL A 1 267 ? -5.70600  -5.57000  30.45500 1.000 21.21000 ? 261 VAL A CG2 1 
ATOM   1952 N  N   . GLY A 1 268 ? -3.05700  -2.86300  31.37100 1.000 19.89000 ? 262 GLY A N   1 
ATOM   1953 C  CA  . GLY A 1 268 ? -1.69900  -2.74700  30.87600 1.000 19.12000 ? 262 GLY A CA  1 
ATOM   1954 C  C   . GLY A 1 268 ? -0.76100  -3.48800  31.80500 1.000 18.79000 ? 262 GLY A C   1 
ATOM   1955 O  O   . GLY A 1 268 ? -1.09200  -3.76000  32.95800 1.000 24.42000 ? 262 GLY A O   1 
ATOM   1956 N  N   . LYS A 1 269 ? 0.38700   -3.87400  31.26900 1.000 16.63000 ? 263 LYS A N   1 
ATOM   1957 C  CA  . LYS A 1 269 ? 1.29300   -4.72700  32.03200 1.000 18.87000 ? 263 LYS A CA  1 
ATOM   1958 C  C   . LYS A 1 269 ? 2.70600   -4.53600  31.51100 1.000 16.47000 ? 263 LYS A C   1 
ATOM   1959 O  O   . LYS A 1 269 ? 2.92200   -4.55600  30.29600 1.000 15.61000 ? 263 LYS A O   1 
ATOM   1960 C  CB  . LYS A 1 269 ? 0.85900   -6.20600  31.93000 1.000 19.99000 ? 263 LYS A CB  1 
ATOM   1961 C  CG  . LYS A 1 269 ? 1.78100   -7.21000  32.60500 1.000 18.85000 ? 263 LYS A CG  1 
ATOM   1962 C  CD  . LYS A 1 269 ? 1.61800   -7.09500  34.12600 1.000 19.96000 ? 263 LYS A CD  1 
ATOM   1963 C  CE  . LYS A 1 269 ? 2.73800   -7.83700  34.85900 1.000 22.67000 ? 263 LYS A CE  1 
ATOM   1964 N  NZ  . LYS A 1 269 ? 3.88900   -6.97400  35.12300 1.000 24.63000 ? 263 LYS A NZ  1 
ATOM   1965 N  N   . LEU A 1 270 ? 3.65600   -4.37500  32.43000 1.000 17.11000 ? 264 LEU A N   1 
ATOM   1966 C  CA  . LEU A 1 270 ? 5.08000   -4.22900  32.11600 1.000 18.31000 ? 264 LEU A CA  1 
ATOM   1967 C  C   . LEU A 1 270 ? 5.77500   -5.57900  31.94700 1.000 18.69000 ? 264 LEU A C   1 
ATOM   1968 O  O   . LEU A 1 270 ? 5.49800   -6.53000  32.68900 1.000 20.43000 ? 264 LEU A O   1 
ATOM   1969 C  CB  . LEU A 1 270 ? 5.77700   -3.45400  33.23600 1.000 19.95000 ? 264 LEU A CB  1 
ATOM   1970 C  CG  . LEU A 1 270 ? 7.29200   -3.45300  33.26400 1.000 21.21000 ? 264 LEU A CG  1 
ATOM   1971 C  CD1 . LEU A 1 270 ? 7.80700   -2.39000  32.28200 1.000 18.79000 ? 264 LEU A CD1 1 
ATOM   1972 C  CD2 . LEU A 1 270 ? 7.74600   -3.14200  34.69300 1.000 19.17000 ? 264 LEU A CD2 1 
ATOM   1973 N  N   . GLY A 1 271 ? 6.68000   -5.65200  30.97200 1.000 18.38000 ? 265 GLY A N   1 
ATOM   1974 C  CA  . GLY A 1 271 ? 7.66100   -6.72400  30.87900 1.000 16.59000 ? 265 GLY A CA  1 
ATOM   1975 C  C   . GLY A 1 271 ? 9.05000   -6.16800  31.16000 1.000 16.74000 ? 265 GLY A C   1 
ATOM   1976 O  O   . GLY A 1 271 ? 9.44400   -5.13300  30.59900 1.000 15.89000 ? 265 GLY A O   1 
ATOM   1977 N  N   . ALA A 1 272 ? 9.80100   -6.87700  32.01400 1.000 20.52000 ? 266 ALA A N   1 
ATOM   1978 C  CA  . ALA A 1 272 ? 11.18100  -6.49400  32.27000 1.000 18.25000 ? 266 ALA A CA  1 
ATOM   1979 C  C   . ALA A 1 272 ? 11.97700  -6.34600  30.97200 1.000 21.77000 ? 266 ALA A C   1 
ATOM   1980 O  O   . ALA A 1 272 ? 11.70200  -7.00300  29.94800 1.000 17.15000 ? 266 ALA A O   1 
ATOM   1981 C  CB  . ALA A 1 272 ? 11.84900  -7.51900  33.18200 1.000 22.00000 ? 266 ALA A CB  1 
ATOM   1982 N  N   . ASP A 1 273 ? 12.98700  -5.46800  31.03600 1.000 22.16000 ? 267 ASP A N   1 
ATOM   1983 C  CA  . ASP A 1 273 ? 13.76900  -5.02800  29.87400 1.000 18.19000 ? 267 ASP A CA  1 
ATOM   1984 C  C   . ASP A 1 273 ? 12.90100  -4.32400  28.83400 1.000 18.79000 ? 267 ASP A C   1 
ATOM   1985 O  O   . ASP A 1 273 ? 13.18500  -4.34900  27.61900 1.000 15.96000 ? 267 ASP A O   1 
ATOM   1986 C  CB  . ASP A 1 273 ? 14.56400  -6.18800  29.27600 1.000 17.44000 ? 267 ASP A CB  1 
ATOM   1987 C  CG  . ASP A 1 273 ? 15.74400  -6.53500  30.13900 1.000 21.10000 ? 267 ASP A CG  1 
ATOM   1988 O  OD1 . ASP A 1 273 ? 16.52400  -5.60400  30.45900 1.000 19.93000 ? 267 ASP A OD1 1 
ATOM   1989 O  OD2 . ASP A 1 273 ? 15.87600  -7.69600  30.54700 1.000 25.64000 ? 267 ASP A OD2 1 
ATOM   1990 N  N   . ALA A 1 274 ? 11.86500  -3.65400  29.33000 1.000 16.73000 ? 268 ALA A N   1 
ATOM   1991 C  CA  . ALA A 1 274 ? 11.12900  -2.60700  28.59600 1.000 15.74000 ? 268 ALA A CA  1 
ATOM   1992 C  C   . ALA A 1 274 ? 10.25500  -3.13500  27.44800 1.000 14.37000 ? 268 ALA A C   1 
ATOM   1993 O  O   . ALA A 1 274 ? 10.27600  -2.60700  26.33600 1.000 18.38000 ? 268 ALA A O   1 
ATOM   1994 C  CB  . ALA A 1 274 ? 12.07800  -1.51800  28.09600 1.000 13.57000 ? 268 ALA A CB  1 
ATOM   1995 N  N   . SER A 1 275 ? 9.44500   -4.13100  27.73700 1.000 13.84000 ? 269 SER A N   1 
ATOM   1996 C  CA  A SER A 1 275 ? 8.26200   -4.43900  26.94600 0.600 14.61000 ? 269 SER A CA  1 
ATOM   1997 C  CA  B SER A 1 275 ? 8.27200   -4.39400  26.92300 0.400 14.63000 ? 269 SER A CA  1 
ATOM   1998 C  C   . SER A 1 275 ? 7.02800   -3.91300  27.66100 1.000 14.12000 ? 269 SER A C   1 
ATOM   1999 O  O   . SER A 1 275 ? 7.03000   -3.72600  28.88300 1.000 17.48000 ? 269 SER A O   1 
ATOM   2000 C  CB  A SER A 1 275 ? 8.11800   -5.94600  26.71700 0.600 16.59000 ? 269 SER A CB  1 
ATOM   2001 C  CB  B SER A 1 275 ? 8.15800   -5.88100  26.56600 0.400 16.57000 ? 269 SER A CB  1 
ATOM   2002 O  OG  A SER A 1 275 ? 9.06600   -6.43500  25.79100 0.600 16.37000 ? 269 SER A OG  1 
ATOM   2003 O  OG  B SER A 1 275 ? 8.00600   -6.70500  27.70900 0.400 17.54000 ? 269 SER A OG  1 
ATOM   2004 N  N   . TYR A 1 276 ? 5.96400   -3.67600  26.89600 1.000 14.18000 ? 270 TYR A N   1 
ATOM   2005 C  CA  . TYR A 1 276 ? 4.70000   -3.24400  27.49400 1.000 16.37000 ? 270 TYR A CA  1 
ATOM   2006 C  C   . TYR A 1 276 ? 3.53000   -3.76000  26.67000 1.000 15.26000 ? 270 TYR A C   1 
ATOM   2007 O  O   . TYR A 1 276 ? 3.60200   -3.78000  25.44000 1.000 16.37000 ? 270 TYR A O   1 
ATOM   2008 C  CB  . TYR A 1 276 ? 4.58900   -1.70500  27.61100 1.000 16.68000 ? 270 TYR A CB  1 
ATOM   2009 C  CG  . TYR A 1 276 ? 3.70700   -1.35000  28.76300 1.000 15.76000 ? 270 TYR A CG  1 
ATOM   2010 C  CD1 . TYR A 1 276 ? 4.23200   -1.31800  30.06700 1.000 17.10000 ? 270 TYR A CD1 1 
ATOM   2011 C  CD2 . TYR A 1 276 ? 2.33100   -1.17000  28.59300 1.000 17.09000 ? 270 TYR A CD2 1 
ATOM   2012 C  CE1 . TYR A 1 276 ? 3.42200   -1.07900  31.14200 1.000 16.64000 ? 270 TYR A CE1 1 
ATOM   2013 C  CE2 . TYR A 1 276 ? 1.50100   -0.92900  29.67400 1.000 16.05000 ? 270 TYR A CE2 1 
ATOM   2014 C  CZ  . TYR A 1 276 ? 2.06000   -0.87400  30.94500 1.000 19.23000 ? 270 TYR A CZ  1 
ATOM   2015 O  OH  . TYR A 1 276 ? 1.23700   -0.63200  32.02500 1.000 21.92000 ? 270 TYR A OH  1 
ATOM   2016 N  N   . ALA A 1 277 ? 2.43300   -4.14100  27.33700 1.000 13.32000 ? 271 ALA A N   1 
ATOM   2017 C  CA  . ALA A 1 277 ? 1.26000   -4.60100  26.61700 1.000 14.22000 ? 271 ALA A CA  1 
ATOM   2018 C  C   . ALA A 1 277 ? 0.00400   -3.94400  27.17500 1.000 15.99000 ? 271 ALA A C   1 
ATOM   2019 O  O   . ALA A 1 277 ? -0.13500  -3.81700  28.39500 1.000 16.47000 ? 271 ALA A O   1 
ATOM   2020 C  CB  . ALA A 1 277 ? 1.14000   -6.11800  26.70800 1.000 17.67000 ? 271 ALA A CB  1 
ATOM   2021 N  N   . ILE A 1 278 ? -0.93300  -3.57100  26.28500 1.000 19.08000 ? 272 ILE A N   1 
ATOM   2022 C  CA  . ILE A 1 278 ? -2.23000  -3.00300  26.66300 1.000 16.31000 ? 272 ILE A CA  1 
ATOM   2023 C  C   . ILE A 1 278 ? -3.35200  -3.69200  25.89700 1.000 18.20000 ? 272 ILE A C   1 
ATOM   2024 O  O   . ILE A 1 278 ? -3.25300  -3.88700  24.68200 1.000 19.05000 ? 272 ILE A O   1 
ATOM   2025 C  CB  . ILE A 1 278 ? -2.27700  -1.48400  26.40000 1.000 17.17000 ? 272 ILE A CB  1 
ATOM   2026 C  CG1 . ILE A 1 278 ? -1.15300  -0.81800  27.16300 1.000 15.05000 ? 272 ILE A CG1 1 
ATOM   2027 C  CG2 . ILE A 1 278 ? -3.64000  -0.91600  26.83000 1.000 17.20000 ? 272 ILE A CG2 1 
ATOM   2028 C  CD1 . ILE A 1 278 ? -1.04600  0.71800   26.92600 1.000 16.48000 ? 272 ILE A CD1 1 
ATOM   2029 N  N   . GLY A 1 279 ? -4.41900  -4.05200  26.60200 1.000 17.25000 ? 273 GLY A N   1 
ATOM   2030 C  CA  . GLY A 1 279 ? -5.64200  -4.54500  25.98600 1.000 17.02000 ? 273 GLY A CA  1 
ATOM   2031 C  C   . GLY A 1 279 ? -6.70700  -3.50100  26.19700 1.000 23.43000 ? 273 GLY A C   1 
ATOM   2032 O  O   . GLY A 1 279 ? -6.97800  -3.14500  27.35200 1.000 21.66000 ? 273 GLY A O   1 
ATOM   2033 N  N   . VAL A 1 280 ? -7.28400  -2.97300  25.11400 1.000 21.26000 ? 274 VAL A N   1 
ATOM   2034 C  CA  . VAL A 1 280 ? -8.21900  -1.85200  25.16400 1.000 21.91000 ? 274 VAL A CA  1 
ATOM   2035 C  C   . VAL A 1 280 ? -9.60400  -2.35100  24.76700 1.000 26.45000 ? 274 VAL A C   1 
ATOM   2036 O  O   . VAL A 1 280 ? -9.80000  -2.87900  23.66500 1.000 24.55000 ? 274 VAL A O   1 
ATOM   2037 C  CB  . VAL A 1 280 ? -7.77100  -0.70400  24.24500 1.000 20.69000 ? 274 VAL A CB  1 
ATOM   2038 C  CG1 . VAL A 1 280 ? -8.78600  0.48800   24.27800 1.000 23.49000 ? 274 VAL A CG1 1 
ATOM   2039 C  CG2 . VAL A 1 280 ? -6.32200  -0.29600  24.55900 1.000 21.58000 ? 274 VAL A CG2 1 
ATOM   2040 N  N   . ARG A 1 281 ? -10.56900 -2.15200  25.65100 1.000 24.07000 ? 275 ARG A N   1 
ATOM   2041 C  CA  . ARG A 1 281 ? -11.94900 -2.53200  25.37600 1.000 29.00000 ? 275 ARG A CA  1 
ATOM   2042 C  C   . ARG A 1 281 ? -12.54500 -1.65500  24.27300 1.000 25.46000 ? 275 ARG A C   1 
ATOM   2043 O  O   . ARG A 1 281 ? -12.12100 -0.51900  24.05700 1.000 25.27000 ? 275 ARG A O   1 
ATOM   2044 C  CB  . ARG A 1 281 ? -12.76200 -2.42500  26.66100 1.000 25.44000 ? 275 ARG A CB  1 
ATOM   2045 C  CG  . ARG A 1 281 ? -12.54500 -3.60200  27.60100 1.000 29.20000 ? 275 ARG A CG  1 
ATOM   2046 C  CD  . ARG A 1 281 ? -13.52400 -3.52400  28.79100 1.000 29.88000 ? 275 ARG A CD  1 
ATOM   2047 N  NE  . ARG A 1 281 ? -14.88000 -3.89300  28.39100 1.000 35.56000 ? 275 ARG A NE  1 
ATOM   2048 C  CZ  . ARG A 1 281 ? -15.95000 -3.78500  29.16900 1.000 39.24000 ? 275 ARG A CZ  1 
ATOM   2049 N  NH1 . ARG A 1 281 ? -15.85500 -3.36800  30.42100 1.000 40.32000 ? 275 ARG A NH1 1 
ATOM   2050 N  NH2 . ARG A 1 281 ? -17.14600 -4.08800  28.67200 1.000 33.38000 ? 275 ARG A NH2 1 
ATOM   2051 N  N   . ALA A 1 282 ? -13.51200 -2.21300  23.54300 1.000 29.84000 ? 276 ALA A N   1 
ATOM   2052 C  CA  . ALA A 1 282 ? -14.15700 -1.47700  22.45900 1.000 30.20000 ? 276 ALA A CA  1 
ATOM   2053 C  C   . ALA A 1 282 ? -14.69400 -0.13900  22.95700 1.000 28.45000 ? 276 ALA A C   1 
ATOM   2054 O  O   . ALA A 1 282 ? -15.35000 -0.07000  23.99900 1.000 28.60000 ? 276 ALA A O   1 
ATOM   2055 C  CB  . ALA A 1 282 ? -15.29700 -2.30500  21.87200 1.000 32.95000 ? 276 ALA A CB  1 
ATOM   2056 N  N   . SER A 1 283 ? -14.42900 0.92000   22.19500 1.000 28.12000 ? 277 SER A N   1 
ATOM   2057 C  CA  . SER A 1 283 ? -14.76000 2.27700   22.61300 1.000 27.34000 ? 277 SER A CA  1 
ATOM   2058 C  C   . SER A 1 283 ? -14.92800 3.18300   21.39800 1.000 30.66000 ? 277 SER A C   1 
ATOM   2059 O  O   . SER A 1 283 ? -14.69100 2.78600   20.24700 1.000 32.60000 ? 277 SER A O   1 
ATOM   2060 C  CB  . SER A 1 283 ? -13.68300 2.85000   23.52300 1.000 29.56000 ? 277 SER A CB  1 
ATOM   2061 O  OG  . SER A 1 283 ? -12.50200 3.08700   22.75700 1.000 26.59000 ? 277 SER A OG  1 
ATOM   2062 N  N   . ASP A 1 284 ? -15.26700 4.43300   21.66400 1.000 31.40000 ? 278 ASP A N   1 
ATOM   2063 C  CA  . ASP A 1 284 ? -15.35100 5.41900   20.57500 1.000 29.10000 ? 278 ASP A CA  1 
ATOM   2064 C  C   . ASP A 1 284 ? -13.95800 5.55300   19.96800 1.000 33.17000 ? 278 ASP A C   1 
ATOM   2065 O  O   . ASP A 1 284 ? -13.85100 5.68300   18.75000 1.000 31.87000 ? 278 ASP A O   1 
ATOM   2066 C  CB  . ASP A 1 284 ? -15.80000 6.76100   21.13300 1.000 30.52000 ? 278 ASP A CB  1 
ATOM   2067 C  CG  . ASP A 1 284 ? -17.30300 6.92400   21.27800 1.000 39.70000 ? 278 ASP A CG  1 
ATOM   2068 O  OD1 . ASP A 1 284 ? -18.03200 5.96700   20.97900 1.000 37.01000 ? 278 ASP A OD1 1 
ATOM   2069 O  OD2 . ASP A 1 284 ? -17.72400 8.01500   21.69000 1.000 43.65000 ? 278 ASP A OD2 1 
ATOM   2070 N  N   . ALA A 1 285 ? -12.94000 5.53200   20.82700 1.000 34.00000 ? 279 ALA A N   1 
ATOM   2071 C  CA  . ALA A 1 285 ? -11.53200 5.62000   20.37500 1.000 33.31000 ? 279 ALA A CA  1 
ATOM   2072 C  C   . ALA A 1 285 ? -11.19500 4.47000   19.42400 1.000 30.32000 ? 279 ALA A C   1 
ATOM   2073 O  O   . ALA A 1 285 ? -10.66900 4.72700   18.34900 1.000 28.65000 ? 279 ALA A O   1 
ATOM   2074 C  CB  . ALA A 1 285 ? -10.66500 5.56000   21.58700 1.000 32.38000 ? 279 ALA A CB  1 
ATOM   2075 N  N   . THR A 1 286 ? -11.50300 3.24500   19.83400 1.000 30.13000 ? 280 THR A N   1 
ATOM   2076 C  CA  . THR A 1 286 ? -11.13700 2.13100   18.96100 1.000 27.33000 ? 280 THR A CA  1 
ATOM   2077 C  C   . THR A 1 286 ? -11.92700 2.15500   17.65700 1.000 30.96000 ? 280 THR A C   1 
ATOM   2078 O  O   . THR A 1 286 ? -11.39300 1.79800   16.59700 1.000 25.43000 ? 280 THR A O   1 
ATOM   2079 C  CB  . THR A 1 286 ? -11.30700 0.78300   19.68000 1.000 29.88000 ? 280 THR A CB  1 
ATOM   2080 O  OG1 . THR A 1 286 ? -12.67900 0.54100   20.00300 1.000 31.79000 ? 280 THR A OG1 1 
ATOM   2081 C  CG2 . THR A 1 286 ? -10.43600 0.74100   20.94400 1.000 28.75000 ? 280 THR A CG2 1 
ATOM   2082 N  N   . ARG A 1 287 ? -13.20400 2.56700   17.71400 1.000 32.72000 ? 281 ARG A N   1 
ATOM   2083 C  CA  A ARG A 1 287 ? -13.99000 2.66100   16.48900 0.700 32.74000 ? 281 ARG A CA  1 
ATOM   2084 C  CA  B ARG A 1 287 ? -14.02700 2.70600   16.51300 0.300 32.73000 ? 281 ARG A CA  1 
ATOM   2085 C  C   . ARG A 1 287 ? -13.41600 3.70700   15.54000 1.000 33.64000 ? 281 ARG A C   1 
ATOM   2086 O  O   . ARG A 1 287 ? -13.37400 3.47300   14.32500 1.000 33.43000 ? 281 ARG A O   1 
ATOM   2087 C  CB  A ARG A 1 287 ? -15.45800 2.95900   16.81300 0.700 30.09000 ? 281 ARG A CB  1 
ATOM   2088 C  CB  B ARG A 1 287 ? -15.43900 3.15400   16.91500 0.300 30.23000 ? 281 ARG A CB  1 
ATOM   2089 C  CG  A ARG A 1 287 ? -16.20300 1.73700   17.34100 0.700 31.13000 ? 281 ARG A CG  1 
ATOM   2090 C  CG  B ARG A 1 287 ? -16.58600 2.45000   16.21400 0.300 32.15000 ? 281 ARG A CG  1 
ATOM   2091 C  CD  A ARG A 1 287 ? -17.67100 2.03300   17.67000 0.700 31.21000 ? 281 ARG A CD  1 
ATOM   2092 C  CD  B ARG A 1 287 ? -17.94900 2.92600   16.73400 0.300 30.48000 ? 281 ARG A CD  1 
ATOM   2093 N  NE  A ARG A 1 287 ? -17.85200 2.71000   18.95200 0.700 28.20000 ? 281 ARG A NE  1 
ATOM   2094 N  NE  B ARG A 1 287 ? -18.08600 2.78100   18.18200 0.300 29.74000 ? 281 ARG A NE  1 
ATOM   2095 C  CZ  A ARG A 1 287 ? -17.93400 2.08800   20.11700 0.700 27.66000 ? 281 ARG A CZ  1 
ATOM   2096 C  CZ  B ARG A 1 287 ? -18.20500 3.79000   19.03700 0.300 28.61000 ? 281 ARG A CZ  1 
ATOM   2097 N  NH1 A ARG A 1 287 ? -17.87100 0.77500   20.19600 0.700 27.30000 ? 281 ARG A NH1 1 
ATOM   2098 N  NH1 B ARG A 1 287 ? -18.24400 5.04700   18.62400 0.300 29.13000 ? 281 ARG A NH1 1 
ATOM   2099 N  NH2 A ARG A 1 287 ? -18.07000 2.80600   21.23200 0.700 27.86000 ? 281 ARG A NH2 1 
ATOM   2100 N  NH2 B ARG A 1 287 ? -18.28900 3.53000   20.34000 0.300 28.44000 ? 281 ARG A NH2 1 
ATOM   2101 N  N   . GLN A 1 288 ? -12.96300 4.86200   16.06600 1.000 31.84000 ? 282 GLN A N   1 
ATOM   2102 C  CA  . GLN A 1 288 ? -12.30600 5.85400   15.21600 1.000 33.13000 ? 282 GLN A CA  1 
ATOM   2103 C  C   . GLN A 1 288 ? -11.03700 5.29700   14.59300 1.000 34.54000 ? 282 GLN A C   1 
ATOM   2104 O  O   . GLN A 1 288 ? -10.65400 5.71500   13.49400 1.000 37.44000 ? 282 GLN A O   1 
ATOM   2105 C  CB  . GLN A 1 288 ? -11.94500 7.11900   15.99600 1.000 37.33000 ? 282 GLN A CB  1 
ATOM   2106 C  CG  . GLN A 1 288 ? -13.08700 8.04200   16.40500 1.000 46.63000 ? 282 GLN A CG  1 
ATOM   2107 C  CD  . GLN A 1 288 ? -12.62700 9.03000   17.50000 1.000 59.56000 ? 282 GLN A CD  1 
ATOM   2108 O  OE1 . GLN A 1 288 ? -11.45600 9.46500   17.50500 1.000 64.72000 ? 282 GLN A OE1 1 
ATOM   2109 N  NE2 . GLN A 1 288 ? -13.52800 9.35100   18.45400 1.000 53.41000 ? 282 GLN A NE2 1 
ATOM   2110 N  N   . LEU A 1 289 ? -10.35400 4.37800   15.28600 1.000 30.74000 ? 283 LEU A N   1 
ATOM   2111 C  CA  . LEU A 1 289 ? -9.13600  3.78800   14.75200 1.000 31.23000 ? 283 LEU A CA  1 
ATOM   2112 C  C   . LEU A 1 289 ? -9.43000  2.77900   13.65500 1.000 35.26000 ? 283 LEU A C   1 
ATOM   2113 O  O   . LEU A 1 289 ? -8.49100  2.24200   13.05500 1.000 37.95000 ? 283 LEU A O   1 
ATOM   2114 C  CB  . LEU A 1 289 ? -8.33200  3.15200   15.89700 1.000 29.82000 ? 283 LEU A CB  1 
ATOM   2115 C  CG  . LEU A 1 289 ? -7.67800  4.19200   16.82800 1.000 28.49000 ? 283 LEU A CG  1 
ATOM   2116 C  CD1 . LEU A 1 289 ? -7.12200  3.55400   18.07900 1.000 25.07000 ? 283 LEU A CD1 1 
ATOM   2117 C  CD2 . LEU A 1 289 ? -6.56100  4.87600   16.08000 1.000 28.31000 ? 283 LEU A CD2 1 
ATOM   2118 N  N   . GLY A 1 290 ? -10.70600 2.50200   13.40100 1.000 34.46000 ? 284 GLY A N   1 
ATOM   2119 C  CA  . GLY A 1 290 ? -11.11700 1.69300   12.27800 1.000 36.11000 ? 284 GLY A CA  1 
ATOM   2120 C  C   . GLY A 1 290 ? -11.48100 0.25600   12.57700 1.000 38.33000 ? 284 GLY A C   1 
ATOM   2121 O  O   . GLY A 1 290 ? -11.65000 -0.52300  11.63100 1.000 43.28000 ? 284 GLY A O   1 
ATOM   2122 N  N   . THR A 1 291 ? -11.62400 -0.12700  13.84600 1.000 35.08000 ? 285 THR A N   1 
ATOM   2123 C  CA  . THR A 1 291 ? -11.94700 -1.50100  14.18800 1.000 34.27000 ? 285 THR A CA  1 
ATOM   2124 C  C   . THR A 1 291 ? -13.22300 -1.54600  15.01700 1.000 34.36000 ? 285 THR A C   1 
ATOM   2125 O  O   . THR A 1 291 ? -13.56500 -0.59300  15.73000 1.000 35.71000 ? 285 THR A O   1 
ATOM   2126 C  CB  . THR A 1 291 ? -10.78700 -2.18300  14.92600 1.000 33.15000 ? 285 THR A CB  1 
ATOM   2127 O  OG1 . THR A 1 291 ? -11.16100 -3.53500  15.23100 1.000 34.52000 ? 285 THR A OG1 1 
ATOM   2128 C  CG2 . THR A 1 291 ? -10.45100 -1.44600  16.20500 1.000 30.00000 ? 285 THR A CG2 1 
ATOM   2129 N  N   . ASP A 1 292 ? -13.95300 -2.64500  14.90900 1.000 33.51000 ? 286 ASP A N   1 
ATOM   2130 C  CA  . ASP A 1 292 ? -15.24000 -2.71100  15.59100 1.000 37.42000 ? 286 ASP A CA  1 
ATOM   2131 C  C   . ASP A 1 292 ? -15.19100 -3.54200  16.87000 1.000 41.17000 ? 286 ASP A C   1 
ATOM   2132 O  O   . ASP A 1 292 ? -16.22700 -3.72900  17.52300 1.000 35.50000 ? 286 ASP A O   1 
ATOM   2133 C  CB  . ASP A 1 292 ? -16.32200 -3.20800  14.63500 1.000 43.45000 ? 286 ASP A CB  1 
ATOM   2134 C  CG  . ASP A 1 292 ? -17.22900 -2.06900  14.16600 1.000 56.53000 ? 286 ASP A CG  1 
ATOM   2135 O  OD1 . ASP A 1 292 ? -17.85500 -1.40400  15.04700 1.000 55.25000 ? 286 ASP A OD1 1 
ATOM   2136 O  OD2 . ASP A 1 292 ? -17.30000 -1.81900  12.93300 1.000 59.98000 ? 286 ASP A OD2 1 
ATOM   2137 N  N   . GLY A 1 293 ? -14.00300 -3.97800  17.28800 1.000 31.08000 ? 287 GLY A N   1 
ATOM   2138 C  CA  . GLY A 1 293 ? -13.91500 -4.72300  18.52300 1.000 33.07000 ? 287 GLY A CA  1 
ATOM   2139 C  C   . GLY A 1 293 ? -12.82000 -4.16400  19.40000 1.000 28.14000 ? 287 GLY A C   1 
ATOM   2140 O  O   . GLY A 1 293 ? -12.44700 -3.00200  19.24700 1.000 29.99000 ? 287 GLY A O   1 
ATOM   2141 N  N   . ALA A 1 294 ? -12.28400 -5.01100  20.25700 1.000 26.27000 ? 288 ALA A N   1 
ATOM   2142 C  CA  . ALA A 1 294 ? -11.21000 -4.58900  21.16900 1.000 24.33000 ? 288 ALA A CA  1 
ATOM   2143 C  C   . ALA A 1 294 ? -9.89800  -4.41200  20.40800 1.000 27.06000 ? 288 ALA A C   1 
ATOM   2144 O  O   . ALA A 1 294 ? -9.82400  -4.76900  19.23400 1.000 28.03000 ? 288 ALA A O   1 
ATOM   2145 C  CB  . ALA A 1 294 ? -11.05100 -5.60300  22.24500 1.000 25.01000 ? 288 ALA A CB  1 
ATOM   2146 N  N   . LEU A 1 295 ? -8.89500  -3.89900  21.11000 1.000 24.28000 ? 289 LEU A N   1 
ATOM   2147 C  CA  . LEU A 1 295 ? -7.61100  -3.59000  20.44300 1.000 23.66000 ? 289 LEU A CA  1 
ATOM   2148 C  C   . LEU A 1 295 ? -6.47000  -3.96200  21.38600 1.000 24.59000 ? 289 LEU A C   1 
ATOM   2149 O  O   . LEU A 1 295 ? -6.65000  -3.90300  22.59600 1.000 22.36000 ? 289 LEU A O   1 
ATOM   2150 C  CB  . LEU A 1 295 ? -7.63200  -2.09300  20.12600 1.000 28.60000 ? 289 LEU A CB  1 
ATOM   2151 C  CG  . LEU A 1 295 ? -6.44800  -1.45300  19.41800 1.000 30.99000 ? 289 LEU A CG  1 
ATOM   2152 C  CD1 . LEU A 1 295 ? -6.95800  -0.62200  18.25500 1.000 34.26000 ? 289 LEU A CD1 1 
ATOM   2153 C  CD2 . LEU A 1 295 ? -5.71100  -0.55200  20.39100 1.000 30.75000 ? 289 LEU A CD2 1 
ATOM   2154 N  N   . GLY A 1 296 ? -5.36000  -4.38700  20.80500 1.000 21.00000 ? 290 GLY A N   1 
ATOM   2155 C  CA  . GLY A 1 296 ? -4.16200  -4.69000  21.58600 1.000 19.72000 ? 290 GLY A CA  1 
ATOM   2156 C  C   . GLY A 1 296 ? -2.98700  -3.82300  21.17200 1.000 22.11000 ? 290 GLY A C   1 
ATOM   2157 O  O   . GLY A 1 296 ? -2.83000  -3.49300  19.98800 1.000 23.80000 ? 290 GLY A O   1 
ATOM   2158 N  N   . ILE A 1 297 ? -2.16600  -3.44000  22.14900 1.000 20.09000 ? 291 ILE A N   1 
ATOM   2159 C  CA  . ILE A 1 297 ? -0.99200  -2.59700  21.90900 1.000 18.16000 ? 291 ILE A CA  1 
ATOM   2160 C  C   . ILE A 1 297 ? 0.19800   -3.29100  22.55800 1.000 17.19000 ? 291 ILE A C   1 
ATOM   2161 O  O   . ILE A 1 297 ? 0.13200   -3.65400  23.74400 1.000 18.06000 ? 291 ILE A O   1 
ATOM   2162 C  CB  . ILE A 1 297 ? -1.14900  -1.15900  22.49300 1.000 14.04000 ? 291 ILE A CB  1 
ATOM   2163 C  CG1 . ILE A 1 297 ? -2.44800  -0.46300  22.05200 1.000 18.91000 ? 291 ILE A CG1 1 
ATOM   2164 C  CG2 . ILE A 1 297 ? 0.10900   -0.29000  22.16900 1.000 17.65000 ? 291 ILE A CG2 1 
ATOM   2165 C  CD1 . ILE A 1 297 ? -2.66100  0.93000   22.72800 1.000 17.48000 ? 291 ILE A CD1 1 
ATOM   2166 N  N   . SER A 1 298 ? 1.28900   -3.47500  21.80600 1.000 16.37000 ? 292 SER A N   1 
ATOM   2167 C  CA  . SER A 1 298 ? 2.52000   -3.97100  22.40900 1.000 14.75000 ? 292 SER A CA  1 
ATOM   2168 C  C   . SER A 1 298 ? 3.69900   -3.13600  21.96200 1.000 16.49000 ? 292 SER A C   1 
ATOM   2169 O  O   . SER A 1 298 ? 3.73800   -2.64600  20.83300 1.000 16.91000 ? 292 SER A O   1 
ATOM   2170 C  CB  . SER A 1 298 ? 2.79700   -5.42300  22.07300 1.000 17.92000 ? 292 SER A CB  1 
ATOM   2171 O  OG  . SER A 1 298 ? 2.66400   -5.69500  20.68500 1.000 19.20000 ? 292 SER A OG  1 
ATOM   2172 N  N   . VAL A 1 299 ? 4.68400   -3.00300  22.85100 1.000 17.63000 ? 293 VAL A N   1 
ATOM   2173 C  CA  . VAL A 1 299 ? 5.78800   -2.05300  22.68900 1.000 15.69000 ? 293 VAL A CA  1 
ATOM   2174 C  C   . VAL A 1 299 ? 7.05700   -2.67200  23.25700 1.000 15.41000 ? 293 VAL A C   1 
ATOM   2175 O  O   . VAL A 1 299 ? 7.03000   -3.33400  24.30100 1.000 13.74000 ? 293 VAL A O   1 
ATOM   2176 C  CB  . VAL A 1 299 ? 5.50300   -0.67800  23.36700 1.000 14.33000 ? 293 VAL A CB  1 
ATOM   2177 C  CG1 . VAL A 1 299 ? 6.71200   0.27700   23.18500 1.000 17.48000 ? 293 VAL A CG1 1 
ATOM   2178 C  CG2 . VAL A 1 299 ? 4.21700   -0.04900  22.81300 1.000 16.09000 ? 293 VAL A CG2 1 
ATOM   2179 N  N   . LYS A 1 300 ? 8.17900   -2.46700  22.56300 1.000 15.03000 ? 294 LYS A N   1 
ATOM   2180 C  CA  . LYS A 1 300 ? 9.49600   -2.89300  23.04500 1.000 14.32000 ? 294 LYS A CA  1 
ATOM   2181 C  C   . LYS A 1 300 ? 10.46300  -1.76000  22.73600 1.000 16.34000 ? 294 LYS A C   1 
ATOM   2182 O  O   . LYS A 1 300 ? 10.50100  -1.28600  21.58900 1.000 15.50000 ? 294 LYS A O   1 
ATOM   2183 C  CB  . LYS A 1 300 ? 9.95400   -4.18200  22.34500 1.000 15.66000 ? 294 LYS A CB  1 
ATOM   2184 C  CG  . LYS A 1 300 ? 11.46700  -4.51900  22.47800 1.000 13.52000 ? 294 LYS A CG  1 
ATOM   2185 C  CD  . LYS A 1 300 ? 11.84100  -4.94900  23.90200 1.000 15.90000 ? 294 LYS A CD  1 
ATOM   2186 C  CE  . LYS A 1 300 ? 13.34700  -5.28800  23.92000 1.000 16.34000 ? 294 LYS A CE  1 
ATOM   2187 N  NZ  . LYS A 1 300 ? 13.93600  -5.62200  25.25300 1.000 17.86000 ? 294 LYS A NZ  1 
ATOM   2188 N  N   . ILE A 1 301 ? 11.21000  -1.29800  23.75000 1.000 12.42000 ? 295 ILE A N   1 
ATOM   2189 C  CA  . ILE A 1 301 ? 12.33700  -0.40000  23.54600 1.000 14.10000 ? 295 ILE A CA  1 
ATOM   2190 C  C   . ILE A 1 301 ? 13.55400  -1.29700  23.34400 1.000 14.17000 ? 295 ILE A C   1 
ATOM   2191 O  O   . ILE A 1 301 ? 13.89700  -2.10300  24.23100 1.000 13.86000 ? 295 ILE A O   1 
ATOM   2192 C  CB  . ILE A 1 301 ? 12.51400  0.56300   24.73400 1.000 15.85000 ? 295 ILE A CB  1 
ATOM   2193 C  CG1 . ILE A 1 301 ? 11.19900  1.31600   25.01100 1.000 13.81000 ? 295 ILE A CG1 1 
ATOM   2194 C  CG2 . ILE A 1 301 ? 13.75900  1.52300   24.54600 1.000 13.18000 ? 295 ILE A CG2 1 
ATOM   2195 C  CD1 . ILE A 1 301 ? 10.80100  2.29800   23.89100 1.000 14.32000 ? 295 ILE A CD1 1 
ATOM   2196 N  N   . GLU A 1 302 ? 14.19000  -1.18300  22.16000 1.000 11.58000 ? 296 GLU A N   1 
ATOM   2197 C  CA  . GLU A 1 302 ? 15.24600  -2.11000  21.75900 1.000 13.25000 ? 296 GLU A CA  1 
ATOM   2198 C  C   . GLU A 1 302 ? 16.36500  -2.23800  22.79000 1.000 16.11000 ? 296 GLU A C   1 
ATOM   2199 O  O   . GLU A 1 302 ? 16.86500  -3.34700  23.01800 1.000 14.69000 ? 296 GLU A O   1 
ATOM   2200 C  CB  . GLU A 1 302 ? 15.82900  -1.67700  20.41300 1.000 14.50000 ? 296 GLU A CB  1 
ATOM   2201 C  CG  . GLU A 1 302 ? 16.87800  -2.60100  19.89600 1.000 13.45000 ? 296 GLU A CG  1 
ATOM   2202 C  CD  . GLU A 1 302 ? 16.33300  -4.00000  19.58100 1.000 19.99000 ? 296 GLU A CD  1 
ATOM   2203 O  OE1 . GLU A 1 302 ? 15.19900  -4.12600  19.06900 1.000 20.08000 ? 296 GLU A OE1 1 
ATOM   2204 O  OE2 . GLU A 1 302 ? 17.04700  -4.98500  19.86500 1.000 22.01000 ? 296 GLU A OE2 1 
ATOM   2205 N  N   . ASP A 1 303 ? 16.78600  -1.13100  23.42100 1.000 14.89000 ? 297 ASP A N   1 
ATOM   2206 C  CA  . ASP A 1 303 ? 17.89500  -1.16500  24.38100 1.000 14.81000 ? 297 ASP A CA  1 
ATOM   2207 C  C   . ASP A 1 303 ? 17.45800  -1.43400  25.81900 1.000 14.65000 ? 297 ASP A C   1 
ATOM   2208 O  O   . ASP A 1 303 ? 18.33100  -1.49000  26.71300 1.000 14.39000 ? 297 ASP A O   1 
ATOM   2209 C  CB  . ASP A 1 303 ? 18.66500  0.16700   24.35600 1.000 15.75000 ? 297 ASP A CB  1 
ATOM   2210 C  CG  . ASP A 1 303 ? 17.71100  1.34500   24.48600 1.000 17.84000 ? 297 ASP A CG  1 
ATOM   2211 O  OD1 . ASP A 1 303 ? 17.18000  1.82600   23.44000 1.000 16.63000 ? 297 ASP A OD1 1 
ATOM   2212 O  OD2 . ASP A 1 303 ? 17.43700  1.76100   25.64600 1.000 15.22000 ? 297 ASP A OD2 1 
ATOM   2213 N  N   . GLY A 1 304 ? 16.15500  -1.52800  26.08400 1.000 16.32000 ? 298 GLY A N   1 
ATOM   2214 C  CA  . GLY A 1 304 ? 15.66100  -1.95900  27.38300 1.000 15.53000 ? 298 GLY A CA  1 
ATOM   2215 C  C   . GLY A 1 304 ? 15.39800  -0.86000  28.39100 1.000 19.66000 ? 298 GLY A C   1 
ATOM   2216 O  O   . GLY A 1 304 ? 15.17300  -1.17500  29.57000 1.000 17.11000 ? 298 GLY A O   1 
ATOM   2217 N  N   . ASN A 1 305 ? 15.38500  0.41800   27.97200 1.000 17.83000 ? 299 ASN A N   1 
ATOM   2218 C  CA  . ASN A 1 305 ? 15.22100  1.53800   28.91000 1.000 18.01000 ? 299 ASN A CA  1 
ATOM   2219 C  C   . ASN A 1 305 ? 13.75300  1.73600   29.32700 1.000 15.49000 ? 299 ASN A C   1 
ATOM   2220 O  O   . ASN A 1 305 ? 12.88700  1.99500   28.48200 1.000 16.09000 ? 299 ASN A O   1 
ATOM   2221 C  CB  . ASN A 1 305 ? 15.77400  2.81100   28.28100 1.000 18.72000 ? 299 ASN A CB  1 
ATOM   2222 C  CG  . ASN A 1 305 ? 15.82900  3.96200   29.25500 1.000 21.13000 ? 299 ASN A CG  1 
ATOM   2223 O  OD1 . ASN A 1 305 ? 14.80500  4.47600   29.67100 1.000 19.83000 ? 299 ASN A OD1 1 
ATOM   2224 N  ND2 . ASN A 1 305 ? 17.03900  4.40500   29.59000 1.000 21.35000 ? 299 ASN A ND2 1 
ATOM   2225 N  N   . LEU A 1 306 ? 13.46800  1.67100   30.64100 1.000 16.20000 ? 300 LEU A N   1 
ATOM   2226 C  CA  . LEU A 1 306 ? 12.07900  1.72100   31.11500 1.000 19.27000 ? 300 LEU A CA  1 
ATOM   2227 C  C   . LEU A 1 306 ? 11.51500  3.13800   31.13000 1.000 19.73000 ? 300 LEU A C   1 
ATOM   2228 O  O   . LEU A 1 306 ? 10.32800  3.34100   30.82700 1.000 15.95000 ? 300 LEU A O   1 
ATOM   2229 C  CB  . LEU A 1 306 ? 11.93800  1.16000   32.53400 1.000 23.20000 ? 300 LEU A CB  1 
ATOM   2230 C  CG  . LEU A 1 306 ? 12.23200  -0.30700  32.86600 1.000 31.89000 ? 300 LEU A CG  1 
ATOM   2231 C  CD1 . LEU A 1 306 ? 11.67700  -0.62000  34.25800 1.000 35.18000 ? 300 LEU A CD1 1 
ATOM   2232 C  CD2 . LEU A 1 306 ? 11.61000  -1.23100  31.84400 1.000 26.14000 ? 300 LEU A CD2 1 
ATOM   2233 N  N   . GLU A 1 307 ? 12.31000  4.11900   31.57100 1.000 17.00000 ? 301 GLU A N   1 
ATOM   2234 C  CA  . GLU A 1 307 ? 11.85000  5.50100   31.49300 1.000 19.57000 ? 301 GLU A CA  1 
ATOM   2235 C  C   . GLU A 1 307 ? 11.33900  5.81000   30.09700 1.000 19.48000 ? 301 GLU A C   1 
ATOM   2236 O  O   . GLU A 1 307 ? 10.27500  6.40900   29.92000 1.000 18.54000 ? 301 GLU A O   1 
ATOM   2237 C  CB  . GLU A 1 307 ? 12.99300  6.44700   31.84900 1.000 19.44000 ? 301 GLU A CB  1 
ATOM   2238 C  CG  . GLU A 1 307 ? 12.53300  7.86000   32.13800 1.000 25.63000 ? 301 GLU A CG  1 
ATOM   2239 C  CD  . GLU A 1 307 ? 13.70300  8.80500   32.41100 1.000 26.46000 ? 301 GLU A CD  1 
ATOM   2240 O  OE1 . GLU A 1 307 ? 14.80400  8.57800   31.86300 1.000 29.02000 ? 301 GLU A OE1 1 
ATOM   2241 O  OE2 . GLU A 1 307 ? 13.52900  9.77300   33.16400 1.000 28.02000 ? 301 GLU A OE2 1 
ATOM   2242 N  N   . MET A 1 308 ? 12.10000  5.38800   29.08500 1.000 18.70000 ? 302 MET A N   1 
ATOM   2243 C  CA  . MET A 1 308 ? 11.71000  5.68000   27.71600 1.000 17.92000 ? 302 MET A CA  1 
ATOM   2244 C  C   . MET A 1 308 ? 10.48200  4.89400   27.30800 1.000 15.45000 ? 302 MET A C   1 
ATOM   2245 O  O   . MET A 1 308 ? 9.65100   5.40300   26.55000 1.000 17.56000 ? 302 MET A O   1 
ATOM   2246 C  CB  . MET A 1 308 ? 12.89000  5.39700   26.79600 1.000 17.40000 ? 302 MET A CB  1 
ATOM   2247 C  CG  . MET A 1 308 ? 14.02800  6.35600   27.06800 1.000 15.81000 ? 302 MET A CG  1 
ATOM   2248 S  SD  . MET A 1 308 ? 13.67700  8.08200   26.66200 1.000 21.66000 ? 302 MET A SD  1 
ATOM   2249 C  CE  . MET A 1 308 ? 13.26500  8.82000   28.27400 1.000 17.47000 ? 302 MET A CE  1 
ATOM   2250 N  N   . LEU A 1 309 ? 10.37200  3.63400   27.74600 1.000 14.43000 ? 303 LEU A N   1 
ATOM   2251 C  CA  . LEU A 1 309 ? 9.15200   2.85400   27.51200 1.000 14.79000 ? 303 LEU A CA  1 
ATOM   2252 C  C   . LEU A 1 309 ? 7.88500   3.61100   27.91800 1.000 16.85000 ? 303 LEU A C   1 
ATOM   2253 O  O   . LEU A 1 309 ? 6.93700   3.73200   27.13400 1.000 16.26000 ? 303 LEU A O   1 
ATOM   2254 C  CB  . LEU A 1 309 ? 9.24400   1.51900   28.27200 1.000 13.32000 ? 303 LEU A CB  1 
ATOM   2255 C  CG  . LEU A 1 309 ? 8.01600   0.59000   28.14400 1.000 14.34000 ? 303 LEU A CG  1 
ATOM   2256 C  CD1 . LEU A 1 309 ? 7.85400   0.10900   26.67600 1.000 14.70000 ? 303 LEU A CD1 1 
ATOM   2257 C  CD2 . LEU A 1 309 ? 8.07400   -0.60500  29.12200 1.000 11.74000 ? 303 LEU A CD2 1 
ATOM   2258 N  N   . TYR A 1 310 ? 7.83200   4.08200   29.16500 1.000 16.54000 ? 304 TYR A N   1 
ATOM   2259 C  CA  . TYR A 1 310 ? 6.63300   4.71400   29.68000 1.000 17.25000 ? 304 TYR A CA  1 
ATOM   2260 C  C   . TYR A 1 310 ? 6.32000   5.99700   28.92400 1.000 19.76000 ? 304 TYR A C   1 
ATOM   2261 O  O   . TYR A 1 310 ? 5.15000   6.34600   28.71000 1.000 20.73000 ? 304 TYR A O   1 
ATOM   2262 C  CB  . TYR A 1 310 ? 6.83500   5.03200   31.15600 1.000 19.44000 ? 304 TYR A CB  1 
ATOM   2263 C  CG  . TYR A 1 310 ? 6.95700   3.80900   32.01500 1.000 18.94000 ? 304 TYR A CG  1 
ATOM   2264 C  CD1 . TYR A 1 310 ? 6.25000   2.66700   31.71100 1.000 22.32000 ? 304 TYR A CD1 1 
ATOM   2265 C  CD2 . TYR A 1 310 ? 7.79100   3.79400   33.13300 1.000 23.15000 ? 304 TYR A CD2 1 
ATOM   2266 C  CE1 . TYR A 1 310 ? 6.33700   1.54400   32.51700 1.000 23.41000 ? 304 TYR A CE1 1 
ATOM   2267 C  CE2 . TYR A 1 310 ? 7.90600   2.67000   33.93200 1.000 23.66000 ? 304 TYR A CE2 1 
ATOM   2268 C  CZ  . TYR A 1 310 ? 7.15400   1.55800   33.62600 1.000 25.63000 ? 304 TYR A CZ  1 
ATOM   2269 O  OH  . TYR A 1 310 ? 7.23500   0.43400   34.41000 1.000 26.94000 ? 304 TYR A OH  1 
ATOM   2270 N  N   . ALA A 1 311 ? 7.36000   6.73800   28.55700 1.000 18.02000 ? 305 ALA A N   1 
ATOM   2271 C  CA  . ALA A 1 311 ? 7.16900   7.93600   27.75700 1.000 18.56000 ? 305 ALA A CA  1 
ATOM   2272 C  C   . ALA A 1 311 ? 6.51700   7.59400   26.42200 1.000 16.58000 ? 305 ALA A C   1 
ATOM   2273 O  O   . ALA A 1 311 ? 5.53000   8.23100   26.03400 1.000 16.64000 ? 305 ALA A O   1 
ATOM   2274 C  CB  . ALA A 1 311 ? 8.51300   8.65700   27.56700 1.000 18.74000 ? 305 ALA A CB  1 
ATOM   2275 N  N   . VAL A 1 312 ? 7.04400   6.57000   25.72400 1.000 14.86000 ? 306 VAL A N   1 
ATOM   2276 C  CA  A VAL A 1 312 ? 6.54500   6.16400   24.40100 0.700 17.10000 ? 306 VAL A CA  1 
ATOM   2277 C  CA  B VAL A 1 312 ? 6.51800   6.24600   24.40100 0.300 17.08000 ? 306 VAL A CA  1 
ATOM   2278 C  C   . VAL A 1 312 ? 5.12600   5.61500   24.48600 1.000 18.59000 ? 306 VAL A C   1 
ATOM   2279 O  O   . VAL A 1 312 ? 4.27400   5.88800   23.62700 1.000 18.51000 ? 306 VAL A O   1 
ATOM   2280 C  CB  A VAL A 1 312 ? 7.48100   5.12100   23.77200 0.700 17.12000 ? 306 VAL A CB  1 
ATOM   2281 C  CB  B VAL A 1 312 ? 7.51200   5.37300   23.61100 0.300 17.18000 ? 306 VAL A CB  1 
ATOM   2282 C  CG1 A VAL A 1 312 ? 6.87200   4.58300   22.46000 0.700 17.28000 ? 306 VAL A CG1 1 
ATOM   2283 C  CG1 B VAL A 1 312 ? 8.85400   6.04900   23.56000 0.300 18.87000 ? 306 VAL A CG1 1 
ATOM   2284 C  CG2 A VAL A 1 312 ? 8.80500   5.70300   23.52600 0.700 18.71000 ? 306 VAL A CG2 1 
ATOM   2285 C  CG2 B VAL A 1 312 ? 7.64000   3.98100   24.19500 0.300 16.07000 ? 306 VAL A CG2 1 
ATOM   2286 N  N   . VAL A 1 313 ? 4.84600   4.77900   25.49600 1.000 17.98000 ? 307 VAL A N   1 
ATOM   2287 C  CA  A VAL A 1 313 ? 3.48600   4.22800   25.62400 0.700 18.12000 ? 307 VAL A CA  1 
ATOM   2288 C  CA  B VAL A 1 313 ? 3.49000   4.23500   25.57900 0.300 17.61000 ? 307 VAL A CA  1 
ATOM   2289 C  C   . VAL A 1 313 ? 2.47900   5.35800   25.79200 1.000 20.35000 ? 307 VAL A C   1 
ATOM   2290 O  O   . VAL A 1 313 ? 1.44000   5.39300   25.13000 1.000 18.66000 ? 307 VAL A O   1 
ATOM   2291 C  CB  A VAL A 1 313 ? 3.40600   3.19000   26.77600 0.700 16.44000 ? 307 VAL A CB  1 
ATOM   2292 C  CB  B VAL A 1 313 ? 3.37500   3.13600   26.65800 0.300 16.49000 ? 307 VAL A CB  1 
ATOM   2293 C  CG1 A VAL A 1 313 ? 1.94600   2.71800   27.04200 0.700 13.05000 ? 307 VAL A CG1 1 
ATOM   2294 C  CG1 B VAL A 1 313 ? 4.22000   1.90900   26.28500 0.300 15.47000 ? 307 VAL A CG1 1 
ATOM   2295 C  CG2 A VAL A 1 313 ? 4.26400   1.95200   26.45300 0.700 15.40000 ? 307 VAL A CG2 1 
ATOM   2296 C  CG2 B VAL A 1 313 ? 3.74900   3.65600   28.00300 0.300 16.43000 ? 307 VAL A CG2 1 
ATOM   2297 N  N   . THR A 1 314 ? 2.79000   6.33500   26.64900 1.000 17.22000 ? 308 THR A N   1 
ATOM   2298 C  CA  . THR A 1 314 ? 1.85000   7.43700   26.83700 1.000 19.04000 ? 308 THR A CA  1 
ATOM   2299 C  C   . THR A 1 314 ? 1.72900   8.31100   25.58100 1.000 19.70000 ? 308 THR A C   1 
ATOM   2300 O  O   . THR A 1 314 ? 0.63100   8.79100   25.25100 1.000 22.59000 ? 308 THR A O   1 
ATOM   2301 C  CB  . THR A 1 314 ? 2.26900   8.28600   28.03900 1.000 19.06000 ? 308 THR A CB  1 
ATOM   2302 O  OG1 . THR A 1 314 ? 2.67300   7.41100   29.10100 1.000 18.21000 ? 308 THR A OG1 1 
ATOM   2303 C  CG2 . THR A 1 314 ? 1.08300   9.16300   28.49500 1.000 22.27000 ? 308 THR A CG2 1 
ATOM   2304 N  N   . GLU A 1 315 ? 2.83600   8.52800   24.86900 1.000 17.74000 ? 309 GLU A N   1 
ATOM   2305 C  CA  . GLU A 1 315 ? 2.75600   9.26900   23.61500 1.000 20.49000 ? 309 GLU A CA  1 
ATOM   2306 C  C   . GLU A 1 315 ? 1.89800   8.51300   22.60700 1.000 21.80000 ? 309 GLU A C   1 
ATOM   2307 O  O   . GLU A 1 315 ? 1.13400   9.12000   21.85000 1.000 21.54000 ? 309 GLU A O   1 
ATOM   2308 C  CB  . GLU A 1 315 ? 4.17100   9.52000   23.07000 1.000 19.22000 ? 309 GLU A CB  1 
ATOM   2309 C  CG  . GLU A 1 315 ? 4.21400   10.14600  21.64100 1.000 21.03000 ? 309 GLU A CG  1 
ATOM   2310 C  CD  . GLU A 1 315 ? 3.82800   11.62900  21.59900 1.000 24.80000 ? 309 GLU A CD  1 
ATOM   2311 O  OE1 . GLU A 1 315 ? 3.61800   12.25000  22.67200 1.000 23.28000 ? 309 GLU A OE1 1 
ATOM   2312 O  OE2 . GLU A 1 315 ? 3.74600   12.19400  20.47300 1.000 25.79000 ? 309 GLU A OE2 1 
ATOM   2313 N  N   . LEU A 1 316 ? 1.98700   7.17800   22.62700 1.000 19.86000 ? 310 LEU A N   1 
ATOM   2314 C  CA  . LEU A 1 316 ? 1.18600   6.32500   21.74900 1.000 19.48000 ? 310 LEU A CA  1 
ATOM   2315 C  C   . LEU A 1 316 ? -0.29400  6.39900   22.08000 1.000 20.80000 ? 310 LEU A C   1 
ATOM   2316 O  O   . LEU A 1 316 ? -1.14000  6.50400   21.17500 1.000 21.54000 ? 310 LEU A O   1 
ATOM   2317 C  CB  . LEU A 1 316 ? 1.67700   4.88800   21.89000 1.000 19.49000 ? 310 LEU A CB  1 
ATOM   2318 C  CG  . LEU A 1 316 ? 1.96900   4.06400   20.65700 1.000 31.66000 ? 310 LEU A CG  1 
ATOM   2319 C  CD1 . LEU A 1 316 ? 2.49400   4.93800   19.57100 1.000 27.94000 ? 310 LEU A CD1 1 
ATOM   2320 C  CD2 . LEU A 1 316 ? 3.07000   3.12500   21.06100 1.000 23.36000 ? 310 LEU A CD2 1 
ATOM   2321 N  N   . LEU A 1 317 ? -0.63700  6.34300   23.37100 1.000 20.61000 ? 311 LEU A N   1 
ATOM   2322 C  CA  . LEU A 1 317 ? -2.02700  6.53300   23.74700 1.000 22.74000 ? 311 LEU A CA  1 
ATOM   2323 C  C   . LEU A 1 317 ? -2.54500  7.87600   23.23800 1.000 25.03000 ? 311 LEU A C   1 
ATOM   2324 O  O   . LEU A 1 317 ? -3.65300  7.94500   22.71200 1.000 25.45000 ? 311 LEU A O   1 
ATOM   2325 C  CB  . LEU A 1 317 ? -2.18700  6.41600   25.26800 1.000 22.14000 ? 311 LEU A CB  1 
ATOM   2326 C  CG  . LEU A 1 317 ? -1.84000  5.05200   25.86800 1.000 22.02000 ? 311 LEU A CG  1 
ATOM   2327 C  CD1 . LEU A 1 317 ? -1.90000  5.10900   27.41100 1.000 21.79000 ? 311 LEU A CD1 1 
ATOM   2328 C  CD2 . LEU A 1 317 ? -2.74100  3.96400   25.30100 1.000 19.06000 ? 311 LEU A CD2 1 
ATOM   2329 N  N   . GLU A 1 318 ? -1.73900  8.94500   23.34600 1.000 20.95000 ? 312 GLU A N   1 
ATOM   2330 C  CA  . GLU A 1 318 ? -2.14300  10.24700  22.82300 1.000 23.09000 ? 312 GLU A CA  1 
ATOM   2331 C  C   . GLU A 1 318 ? -2.29300  10.22200  21.30600 1.000 27.14000 ? 312 GLU A C   1 
ATOM   2332 O  O   . GLU A 1 318 ? -3.28500  10.72500  20.77200 1.000 29.44000 ? 312 GLU A O   1 
ATOM   2333 C  CB  . GLU A 1 318 ? -1.14900  11.34400  23.23000 1.000 22.36000 ? 312 GLU A CB  1 
ATOM   2334 C  CG  . GLU A 1 318 ? -1.59100  12.75000  22.73200 1.000 27.65000 ? 312 GLU A CG  1 
ATOM   2335 C  CD  . GLU A 1 318 ? -0.82500  13.88000  23.39700 1.000 28.42000 ? 312 GLU A CD  1 
ATOM   2336 O  OE1 . GLU A 1 318 ? 0.27100   14.24600  22.92400 1.000 29.75000 ? 312 GLU A OE1 1 
ATOM   2337 O  OE2 . GLU A 1 318 ? -1.31800  14.40200  24.41000 1.000 32.87000 ? 312 GLU A OE2 1 
ATOM   2338 N  N   . ARG A 1 319 ? -1.31300  9.68100   20.58400 1.000 23.33000 ? 313 ARG A N   1 
ATOM   2339 C  CA  . ARG A 1 319 ? -1.48200  9.60900   19.13800 1.000 24.69000 ? 313 ARG A CA  1 
ATOM   2340 C  C   . ARG A 1 319 ? -2.74900  8.84700   18.76700 1.000 28.21000 ? 313 ARG A C   1 
ATOM   2341 O  O   . ARG A 1 319 ? -3.45500  9.22900   17.82800 1.000 28.06000 ? 313 ARG A O   1 
ATOM   2342 C  CB  . ARG A 1 319 ? -0.29000  8.92600   18.47800 1.000 24.44000 ? 313 ARG A CB  1 
ATOM   2343 C  CG  . ARG A 1 319 ? 1.06600   9.48000   18.79100 1.000 28.71000 ? 313 ARG A CG  1 
ATOM   2344 C  CD  . ARG A 1 319 ? 1.47900   10.55700  17.85700 1.000 25.37000 ? 313 ARG A CD  1 
ATOM   2345 N  NE  . ARG A 1 319 ? 2.81800   10.99300  18.22500 1.000 24.52000 ? 313 ARG A NE  1 
ATOM   2346 C  CZ  . ARG A 1 319 ? 3.91100   10.80300  17.50100 1.000 23.52000 ? 313 ARG A CZ  1 
ATOM   2347 N  NH1 . ARG A 1 319 ? 3.87700   10.17500  16.33800 1.000 25.76000 ? 313 ARG A NH1 1 
ATOM   2348 N  NH2 . ARG A 1 319 ? 5.07000   11.27700  17.94300 1.000 22.83000 ? 313 ARG A NH2 1 
ATOM   2349 N  N   . LEU A 1 320 ? -3.03200  7.74200   19.47600 1.000 21.79000 ? 314 LEU A N   1 
ATOM   2350 C  CA  . LEU A 1 320 ? -4.16500  6.88000   19.15800 1.000 23.60000 ? 314 LEU A CA  1 
ATOM   2351 C  C   . LEU A 1 320 ? -5.48500  7.45000   19.65500 1.000 24.86000 ? 314 LEU A C   1 
ATOM   2352 O  O   . LEU A 1 320 ? -6.55300  6.89700   19.33500 1.000 25.63000 ? 314 LEU A O   1 
ATOM   2353 C  CB  . LEU A 1 320 ? -3.93100  5.48400   19.73600 1.000 18.82000 ? 314 LEU A CB  1 
ATOM   2354 C  CG  . LEU A 1 320 ? -2.78500  4.68500   19.13800 1.000 21.97000 ? 314 LEU A CG  1 
ATOM   2355 C  CD1 . LEU A 1 320 ? -2.46500  3.47900   20.06800 1.000 20.40000 ? 314 LEU A CD1 1 
ATOM   2356 C  CD2 . LEU A 1 320 ? -3.05800  4.19200   17.73100 1.000 20.42000 ? 314 LEU A CD2 1 
ATOM   2357 N  N   . GLY A 1 321 ? -5.44900  8.54600   20.40400 1.000 22.41000 ? 315 GLY A N   1 
ATOM   2358 C  CA  . GLY A 1 321 ? -6.67900  9.09600   20.92200 1.000 27.11000 ? 315 GLY A CA  1 
ATOM   2359 C  C   . GLY A 1 321 ? -7.34900  8.21100   21.94000 1.000 31.22000 ? 315 GLY A C   1 
ATOM   2360 O  O   . GLY A 1 321 ? -8.56000  8.32000   22.14400 1.000 29.95000 ? 315 GLY A O   1 
ATOM   2361 N  N   . ILE A 1 322 ? -6.60100  7.32400   22.58200 1.000 27.09000 ? 316 ILE A N   1 
ATOM   2362 C  CA  . ILE A 1 322 ? -7.18000  6.41900   23.56600 1.000 31.61000 ? 316 ILE A CA  1 
ATOM   2363 C  C   . ILE A 1 322 ? -7.23000  7.14800   24.90400 1.000 33.52000 ? 316 ILE A C   1 
ATOM   2364 O  O   . ILE A 1 322 ? -6.19900  7.56600   25.44300 1.000 34.88000 ? 316 ILE A O   1 
ATOM   2365 C  CB  . ILE A 1 322 ? -6.40000  5.09400   23.63600 1.000 29.07000 ? 316 ILE A CB  1 
ATOM   2366 C  CG1 . ILE A 1 322 ? -6.80500  4.23500   22.43300 1.000 29.43000 ? 316 ILE A CG1 1 
ATOM   2367 C  CG2 . ILE A 1 322 ? -6.68200  4.32900   24.95100 1.000 25.15000 ? 316 ILE A CG2 1 
ATOM   2368 C  CD1 . ILE A 1 322 ? -5.78700  3.31100   21.97000 1.000 31.87000 ? 316 ILE A CD1 1 
ATOM   2369 N  N   . GLY A 1 323 ? -8.43600  7.34800   25.41500 1.000 35.32000 ? 317 GLY A N   1 
ATOM   2370 C  CA  . GLY A 1 323 ? -8.64400  8.11400   26.62500 1.000 34.17000 ? 317 GLY A CA  1 
ATOM   2371 C  C   . GLY A 1 323 ? -9.04200  9.54800   26.32200 1.000 42.83000 ? 317 GLY A C   1 
ATOM   2372 O  O   . GLY A 1 323 ? -9.01700  10.01700  25.17900 1.000 47.13000 ? 317 GLY A O   1 
ATOM   2373 N  N   . SER A 1 324 ? -9.43700  10.24200  27.35900 1.000 42.45000 ? 318 SER A N   1 
ATOM   2374 C  CA  . SER A 1 324 ? -9.58100  11.66900  27.14700 1.000 45.13000 ? 318 SER A CA  1 
ATOM   2375 C  C   . SER A 1 324 ? -8.25000  12.35400  27.41400 1.000 44.70000 ? 318 SER A C   1 
ATOM   2376 O  O   . SER A 1 324 ? -7.32000  11.74100  27.95700 1.000 44.78000 ? 318 SER A O   1 
ATOM   2377 C  CB  . SER A 1 324 ? -10.65600 12.22800  28.05900 1.000 42.42000 ? 318 SER A CB  1 
ATOM   2378 O  OG  . SER A 1 324 ? -10.23000 12.16500  29.40300 1.000 41.65000 ? 318 SER A OG  1 
ATOM   2379 N  N   . PRO A 1 325 ? -8.10300  13.62100  27.00500 1.000 47.22000 ? 319 PRO A N   1 
ATOM   2380 C  CA  . PRO A 1 325 ? -6.93700  14.39200  27.47600 1.000 46.50000 ? 319 PRO A CA  1 
ATOM   2381 C  C   . PRO A 1 325 ? -6.84700  14.47200  28.99600 1.000 42.71000 ? 319 PRO A C   1 
ATOM   2382 O  O   . PRO A 1 325 ? -5.73900  14.40600  29.54900 1.000 39.60000 ? 319 PRO A O   1 
ATOM   2383 C  CB  . PRO A 1 325 ? -7.15700  15.77200  26.82800 1.000 47.81000 ? 319 PRO A CB  1 
ATOM   2384 C  CG  . PRO A 1 325 ? -7.87100  15.45400  25.55600 1.000 46.40000 ? 319 PRO A CG  1 
ATOM   2385 C  CD  . PRO A 1 325 ? -8.83500  14.33600  25.94200 1.000 45.55000 ? 319 PRO A CD  1 
ATOM   2386 N  N   . ASP A 1 326 ? -7.98600  14.61700  29.68600 1.000 43.55000 ? 320 ASP A N   1 
ATOM   2387 C  CA  . ASP A 1 326 ? -7.97600  14.64400  31.14800 1.000 45.82000 ? 320 ASP A CA  1 
ATOM   2388 C  C   . ASP A 1 326 ? -7.48100  13.32400  31.72100 1.000 39.79000 ? 320 ASP A C   1 
ATOM   2389 O  O   . ASP A 1 326 ? -6.73000  13.31400  32.70400 1.000 43.70000 ? 320 ASP A O   1 
ATOM   2390 C  CB  . ASP A 1 326 ? -9.37600  14.95900  31.71100 1.000 44.27000 ? 320 ASP A CB  1 
ATOM   2391 C  CG  . ASP A 1 326 ? -9.82800  16.38000  31.43000 1.000 57.09000 ? 320 ASP A CG  1 
ATOM   2392 O  OD1 . ASP A 1 326 ? -9.00500  17.33100  31.53600 1.000 55.66000 ? 320 ASP A OD1 1 
ATOM   2393 O  OD2 . ASP A 1 326 ? -11.03200 16.54400  31.11200 1.000 70.69000 ? 320 ASP A OD2 1 
ATOM   2394 N  N   . VAL A 1 327 ? -7.90100  12.19800  31.14100 1.000 35.69000 ? 321 VAL A N   1 
ATOM   2395 C  CA  . VAL A 1 327 ? -7.46300  10.90700  31.66300 1.000 39.16000 ? 321 VAL A CA  1 
ATOM   2396 C  C   . VAL A 1 327 ? -5.95100  10.75700  31.50600 1.000 38.12000 ? 321 VAL A C   1 
ATOM   2397 O  O   . VAL A 1 327 ? -5.23300  10.40300  32.45500 1.000 34.70000 ? 321 VAL A O   1 
ATOM   2398 C  CB  . VAL A 1 327 ? -8.22500  9.76500   30.97400 1.000 38.34000 ? 321 VAL A CB  1 
ATOM   2399 C  CG1 . VAL A 1 327 ? -7.51900  8.43800   31.22000 1.000 33.58000 ? 321 VAL A CG1 1 
ATOM   2400 C  CG2 . VAL A 1 327 ? -9.65000  9.71900   31.48000 1.000 36.80000 ? 321 VAL A CG2 1 
ATOM   2401 N  N   . ARG A 1 328 ? -5.43600  11.07400  30.31800 1.000 32.69000 ? 322 ARG A N   1 
ATOM   2402 C  CA  . ARG A 1 328 ? -4.01700  10.84600  30.07300 1.000 37.16000 ? 322 ARG A CA  1 
ATOM   2403 C  C   . ARG A 1 328 ? -3.12400  11.83300  30.83100 1.000 37.92000 ? 322 ARG A C   1 
ATOM   2404 O  O   . ARG A 1 328 ? -1.96900  11.50500  31.13200 1.000 38.18000 ? 322 ARG A O   1 
ATOM   2405 C  CB  . ARG A 1 328 ? -3.73400  10.90200  28.57100 1.000 35.12000 ? 322 ARG A CB  1 
ATOM   2406 C  CG  . ARG A 1 328 ? -4.38700  9.78000   27.77600 1.000 36.91000 ? 322 ARG A CG  1 
ATOM   2407 C  CD  . ARG A 1 328 ? -3.88400  9.77900   26.33600 1.000 30.28000 ? 322 ARG A CD  1 
ATOM   2408 N  NE  . ARG A 1 328 ? -4.08100  11.07500  25.69700 1.000 41.15000 ? 322 ARG A NE  1 
ATOM   2409 C  CZ  . ARG A 1 328 ? -5.14300  11.39000  24.96700 1.000 37.93000 ? 322 ARG A CZ  1 
ATOM   2410 N  NH1 . ARG A 1 328 ? -6.08700  10.50300  24.70500 1.000 37.13000 ? 322 ARG A NH1 1 
ATOM   2411 N  NH2 . ARG A 1 328 ? -5.26100  12.62700  24.48700 1.000 41.11000 ? 322 ARG A NH2 1 
ATOM   2412 N  N   . SER A 1 329 ? -3.62400  13.03300  31.15300 1.000 35.58000 ? 323 SER A N   1 
ATOM   2413 C  CA  . SER A 1 329 ? -2.82100  13.98300  31.91800 1.000 35.28000 ? 323 SER A CA  1 
ATOM   2414 C  C   . SER A 1 329 ? -2.43100  13.43300  33.28700 1.000 32.57000 ? 323 SER A C   1 
ATOM   2415 O  O   . SER A 1 329 ? -1.46400  13.91200  33.88900 1.000 31.84000 ? 323 SER A O   1 
ATOM   2416 C  CB  . SER A 1 329 ? -3.57200  15.30700  32.08300 1.000 39.60000 ? 323 SER A CB  1 
ATOM   2417 O  OG  . SER A 1 329 ? -4.52300  15.19100  33.12500 1.000 43.34000 ? 323 SER A OG  1 
ATOM   2418 N  N   . GLN A 1 330 ? -3.14700  12.42900  33.78300 1.000 31.42000 ? 324 GLN A N   1 
ATOM   2419 C  CA  . GLN A 1 330 ? -2.69500  11.70300  34.96500 1.000 33.45000 ? 324 GLN A CA  1 
ATOM   2420 C  C   . GLN A 1 330 ? -1.33600  11.03300  34.77100 1.000 32.56000 ? 324 GLN A C   1 
ATOM   2421 O  O   . GLN A 1 330 ? -0.65400  10.75500  35.76500 1.000 31.66000 ? 324 GLN A O   1 
ATOM   2422 C  CB  . GLN A 1 330 ? -3.76300  10.68100  35.35300 1.000 32.95000 ? 324 GLN A CB  1 
ATOM   2423 C  CG  . GLN A 1 330 ? -5.13800  11.34500  35.49200 1.000 34.63000 ? 324 GLN A CG  1 
ATOM   2424 C  CD  . GLN A 1 330 ? -6.19000  10.46900  36.16300 1.000 39.46000 ? 324 GLN A CD  1 
ATOM   2425 O  OE1 . GLN A 1 330 ? -5.87100  9.52800   36.91400 1.000 35.88000 ? 324 GLN A OE1 1 
ATOM   2426 N  NE2 . GLN A 1 330 ? -7.45900  10.76800  35.88300 1.000 34.49000 ? 324 GLN A NE2 1 
ATOM   2427 N  N   . LEU A 1 331 ? -0.91100  10.77000  33.53000 1.000 28.61000 ? 325 LEU A N   1 
ATOM   2428 C  CA  . LEU A 1 331 ? 0.39000   10.14800  33.28800 1.000 30.10000 ? 325 LEU A CA  1 
ATOM   2429 C  C   . LEU A 1 331 ? 1.44000   11.14100  32.78100 1.000 26.04000 ? 325 LEU A C   1 
ATOM   2430 O  O   . LEU A 1 331 ? 2.48700   10.72000  32.26300 1.000 24.52000 ? 325 LEU A O   1 
ATOM   2431 C  CB  . LEU A 1 331 ? 0.24400   8.97000   32.31500 1.000 29.85000 ? 325 LEU A CB  1 
ATOM   2432 C  CG  . LEU A 1 331 ? -0.88900  7.97300   32.63000 1.000 29.19000 ? 325 LEU A CG  1 
ATOM   2433 C  CD1 . LEU A 1 331 ? -1.11300  7.04900   31.45000 1.000 26.23000 ? 325 LEU A CD1 1 
ATOM   2434 C  CD2 . LEU A 1 331 ? -0.58400  7.16600   33.91100 1.000 25.98000 ? 325 LEU A CD2 1 
ATOM   2435 N  N   . ALA A 1 332 ? 1.19900   12.44400  32.97200 1.000 30.65000 ? 326 ALA A N   1 
ATOM   2436 C  CA  . ALA A 1 332 ? 2.08600   13.48500  32.44700 1.000 31.45000 ? 326 ALA A CA  1 
ATOM   2437 C  C   . ALA A 1 332 ? 3.53600   13.33500  32.92400 1.000 29.59000 ? 326 ALA A C   1 
ATOM   2438 O  O   . ALA A 1 332 ? 4.47500   13.65800  32.17300 1.000 25.06000 ? 326 ALA A O   1 
ATOM   2439 C  CB  . ALA A 1 332 ? 1.53700   14.86500  32.82200 1.000 29.24000 ? 326 ALA A CB  1 
ATOM   2440 N  N   . SER A 1 333 ? 3.75900   12.86700  34.15800 1.000 25.03000 ? 327 SER A N   1 
ATOM   2441 C  CA  A SER A 1 333 ? 5.12200   12.73000  34.65300 0.600 27.67000 ? 327 SER A CA  1 
ATOM   2442 C  CA  B SER A 1 333 ? 5.13700   12.75800  34.61300 0.400 27.67000 ? 327 SER A CA  1 
ATOM   2443 C  C   . SER A 1 333 ? 5.88400   11.62300  33.91300 1.000 28.26000 ? 327 SER A C   1 
ATOM   2444 O  O   . SER A 1 333 ? 7.12200   11.66900  33.81000 1.000 25.77000 ? 327 SER A O   1 
ATOM   2445 C  CB  A SER A 1 333 ? 5.08300   12.48100  36.16400 0.600 27.29000 ? 327 SER A CB  1 
ATOM   2446 C  CB  B SER A 1 333 ? 5.18000   12.58800  36.13100 0.400 27.34000 ? 327 SER A CB  1 
ATOM   2447 O  OG  A SER A 1 333 ? 4.63600   11.16100  36.46000 0.600 26.74000 ? 327 SER A OG  1 
ATOM   2448 O  OG  B SER A 1 333 ? 6.52500   12.45200  36.56000 0.400 28.68000 ? 327 SER A OG  1 
ATOM   2449 N  N   . PHE A 1 334 ? 5.17200   10.62400  33.39400 1.000 27.20000 ? 328 PHE A N   1 
ATOM   2450 C  CA  . PHE A 1 334 ? 5.80400   9.56800   32.60700 1.000 23.72000 ? 328 PHE A CA  1 
ATOM   2451 C  C   . PHE A 1 334 ? 5.95100   9.98700   31.16300 1.000 23.80000 ? 328 PHE A C   1 
ATOM   2452 O  O   . PHE A 1 334 ? 6.90400   9.58600   30.48900 1.000 24.89000 ? 328 PHE A O   1 
ATOM   2453 C  CB  . PHE A 1 334 ? 4.96600   8.28100   32.63900 1.000 23.31000 ? 328 PHE A CB  1 
ATOM   2454 C  CG  . PHE A 1 334 ? 4.94500   7.59400   33.97900 1.000 25.27000 ? 328 PHE A CG  1 
ATOM   2455 C  CD1 . PHE A 1 334 ? 5.97600   6.75300   34.34600 1.000 26.47000 ? 328 PHE A CD1 1 
ATOM   2456 C  CD2 . PHE A 1 334 ? 3.90600   7.79800   34.87100 1.000 27.75000 ? 328 PHE A CD2 1 
ATOM   2457 C  CE1 . PHE A 1 334 ? 5.97600   6.10500   35.57300 1.000 27.63000 ? 328 PHE A CE1 1 
ATOM   2458 C  CE2 . PHE A 1 334 ? 3.89800   7.14500   36.10800 1.000 29.91000 ? 328 PHE A CE2 1 
ATOM   2459 C  CZ  . PHE A 1 334 ? 4.95500   6.30700   36.45400 1.000 26.25000 ? 328 PHE A CZ  1 
ATOM   2460 N  N   . HIS A 1 335 ? 5.00000   10.78000  30.67500 1.000 24.36000 ? 329 HIS A N   1 
ATOM   2461 C  CA  . HIS A 1 335 ? 4.96700   11.12100  29.25900 1.000 23.87000 ? 329 HIS A CA  1 
ATOM   2462 C  C   . HIS A 1 335 ? 6.18600   11.95900  28.87800 1.000 22.92000 ? 329 HIS A C   1 
ATOM   2463 O  O   . HIS A 1 335 ? 6.81900   11.72000  27.84300 1.000 22.84000 ? 329 HIS A O   1 
ATOM   2464 C  CB  . HIS A 1 335 ? 3.65600   11.85400  28.96500 1.000 23.48000 ? 329 HIS A CB  1 
ATOM   2465 C  CG  . HIS A 1 335 ? 3.38700   12.05600  27.51200 1.000 20.98000 ? 329 HIS A CG  1 
ATOM   2466 N  ND1 . HIS A 1 335 ? 2.25600   12.69800  27.05300 1.000 27.33000 ? 329 HIS A ND1 1 
ATOM   2467 C  CD2 . HIS A 1 335 ? 4.10500   11.71600  26.41300 1.000 20.67000 ? 329 HIS A CD2 1 
ATOM   2468 C  CE1 . HIS A 1 335 ? 2.28400   12.73900  25.73000 1.000 29.80000 ? 329 HIS A CE1 1 
ATOM   2469 N  NE2 . HIS A 1 335 ? 3.39400   12.15000  25.31500 1.000 21.26000 ? 329 HIS A NE2 1 
ATOM   2470 N  N   . HIS A 1 336 ? 6.55900   12.90000  29.73100 1.000 23.53000 ? 330 HIS A N   1 
ATOM   2471 C  CA  . HIS A 1 336 ? 7.65600   13.83200  29.48700 1.000 24.85000 ? 330 HIS A CA  1 
ATOM   2472 C  C   . HIS A 1 336 ? 8.49300   13.81600  30.75700 1.000 25.17000 ? 330 HIS A C   1 
ATOM   2473 O  O   . HIS A 1 336 ? 8.31000   14.67000  31.63200 1.000 31.10000 ? 330 HIS A O   1 
ATOM   2474 C  CB  . HIS A 1 336 ? 7.12000   15.23300  29.15200 1.000 23.06000 ? 330 HIS A CB  1 
ATOM   2475 C  CG  . HIS A 1 336 ? 6.28000   15.26200  27.90400 1.000 24.18000 ? 330 HIS A CG  1 
ATOM   2476 N  ND1 . HIS A 1 336 ? 4.90200   15.20800  27.92900 1.000 30.19000 ? 330 HIS A ND1 1 
ATOM   2477 C  CD2 . HIS A 1 336 ? 6.63400   15.27900  26.58800 1.000 23.08000 ? 330 HIS A CD2 1 
ATOM   2478 C  CE1 . HIS A 1 336 ? 4.44200   15.19700  26.68600 1.000 31.11000 ? 330 HIS A CE1 1 
ATOM   2479 N  NE2 . HIS A 1 336 ? 5.47200   15.23500  25.85400 1.000 25.85000 ? 330 HIS A NE2 1 
ATOM   2480 N  N   . PRO A 1 337 ? 9.39300   12.83400  30.90800 1.000 24.93000 ? 331 PRO A N   1 
ATOM   2481 C  CA  . PRO A 1 337 ? 10.15800  12.71500  32.15500 1.000 25.19000 ? 331 PRO A CA  1 
ATOM   2482 C  C   . PRO A 1 337 ? 10.92000  13.99400  32.45100 1.000 29.32000 ? 331 PRO A C   1 
ATOM   2483 O  O   . PRO A 1 337 ? 11.36100  14.70400  31.54500 1.000 28.55000 ? 331 PRO A O   1 
ATOM   2484 C  CB  . PRO A 1 337 ? 11.12500  11.55000  31.88700 1.000 26.67000 ? 331 PRO A CB  1 
ATOM   2485 C  CG  . PRO A 1 337 ? 10.60300  10.83000  30.74400 1.000 28.17000 ? 331 PRO A CG  1 
ATOM   2486 C  CD  . PRO A 1 337 ? 9.70700   11.77100  29.95000 1.000 25.22000 ? 331 PRO A CD  1 
ATOM   2487 N  N   . GLN A 1 338 ? 11.07600  14.26800  33.73900 1.000 29.04000 ? 332 GLN A N   1 
ATOM   2488 C  CA  . GLN A 1 338 ? 11.79600  15.44400  34.18900 1.000 33.71000 ? 332 GLN A CA  1 
ATOM   2489 C  C   . GLN A 1 338 ? 13.25200  15.40200  33.73300 1.000 31.05000 ? 332 GLN A C   1 
ATOM   2490 O  O   . GLN A 1 338 ? 13.90500  14.35100  33.76200 1.000 28.00000 ? 332 GLN A O   1 
ATOM   2491 C  CB  . GLN A 1 338 ? 11.73400  15.52500  35.71200 1.000 38.95000 ? 332 GLN A CB  1 
ATOM   2492 C  CG  . GLN A 1 338 ? 10.35600  15.78600  36.24800 1.000 47.31000 ? 332 GLN A CG  1 
ATOM   2493 C  CD  . GLN A 1 338 ? 10.21900  17.20700  36.74000 1.000 56.67000 ? 332 GLN A CD  1 
ATOM   2494 O  OE1 . GLN A 1 338 ? 10.67400  17.53800  37.84700 1.000 55.75000 ? 332 GLN A OE1 1 
ATOM   2495 N  NE2 . GLN A 1 338 ? 9.61200   18.07400  35.90900 1.000 54.86000 ? 332 GLN A NE2 1 
ATOM   2496 N  N   . ARG A 1 339 ? 13.76400  16.55900  33.31700 1.000 29.43000 ? 333 ARG A N   1 
ATOM   2497 C  CA  . ARG A 1 339 ? 15.17200  16.71300  32.93800 1.000 29.34000 ? 333 ARG A CA  1 
ATOM   2498 C  C   . ARG A 1 339 ? 15.68600  17.95100  33.66000 1.000 31.71000 ? 333 ARG A C   1 
ATOM   2499 O  O   . ARG A 1 339 ? 15.85000  19.02400  33.06600 1.000 32.25000 ? 333 ARG A O   1 
ATOM   2500 C  CB  . ARG A 1 339 ? 15.32400  16.80000  31.44300 1.000 28.39000 ? 333 ARG A CB  1 
ATOM   2501 C  CG  . ARG A 1 339 ? 15.21800  15.42400  30.75100 1.000 26.76000 ? 333 ARG A CG  1 
ATOM   2502 C  CD  . ARG A 1 339 ? 16.31700  14.48400  31.24000 1.000 29.28000 ? 333 ARG A CD  1 
ATOM   2503 N  NE  . ARG A 1 339 ? 16.33800  13.20200  30.53500 1.000 33.50000 ? 333 ARG A NE  1 
ATOM   2504 C  CZ  . ARG A 1 339 ? 15.65700  12.11600  30.88500 1.000 36.55000 ? 333 ARG A CZ  1 
ATOM   2505 N  NH1 . ARG A 1 339 ? 14.80300  12.12200  31.90100 1.000 29.89000 ? 333 ARG A NH1 1 
ATOM   2506 N  NH2 . ARG A 1 339 ? 15.82800  10.99300  30.19000 1.000 34.09000 ? 333 ARG A NH2 1 
ATOM   2507 N  N   . VAL A 1 340 ? 15.93000  17.80200  34.96100 1.000 32.58000 ? 334 VAL A N   1 
ATOM   2508 C  CA  . VAL A 1 340 ? 16.24600  18.92100  35.84200 1.000 33.98000 ? 334 VAL A CA  1 
ATOM   2509 C  C   . VAL A 1 340 ? 17.50200  18.58600  36.64200 1.000 34.95000 ? 334 VAL A C   1 
ATOM   2510 O  O   . VAL A 1 340 ? 17.60600  17.49200  37.21500 1.000 36.80000 ? 334 VAL A O   1 
ATOM   2511 C  CB  . VAL A 1 340 ? 15.06300  19.23900  36.77100 1.000 34.62000 ? 334 VAL A CB  1 
ATOM   2512 C  CG1 . VAL A 1 340 ? 15.48500  20.20800  37.83400 1.000 36.05000 ? 334 VAL A CG1 1 
ATOM   2513 C  CG2 . VAL A 1 340 ? 13.93900  19.83800  35.97000 1.000 35.29000 ? 334 VAL A CG2 1 
ATOM   2514 N  N   . ASN A 1 341 ? 18.46300  19.51400  36.67100 1.000 30.93000 ? 335 ASN A N   1 
ATOM   2515 C  CA  . ASN A 1 341 ? 19.76300  19.16200  37.22800 1.000 31.36000 ? 335 ASN A CA  1 
ATOM   2516 C  C   . ASN A 1 341 ? 19.72900  19.31600  38.74300 1.000 33.95000 ? 335 ASN A C   1 
ATOM   2517 O  O   . ASN A 1 341 ? 18.70800  19.68900  39.32000 1.000 32.88000 ? 335 ASN A O   1 
ATOM   2518 C  CB  . ASN A 1 341 ? 20.88100  19.97600  36.55900 1.000 33.17000 ? 335 ASN A CB  1 
ATOM   2519 C  CG  . ASN A 1 341 ? 20.84400  21.46100  36.87800 1.000 34.70000 ? 335 ASN A CG  1 
ATOM   2520 O  OD1 . ASN A 1 341 ? 20.20600  21.90000  37.83100 1.000 33.75000 ? 335 ASN A OD1 1 
ATOM   2521 N  ND2 . ASN A 1 341 ? 21.58000  22.25000  36.08300 1.000 30.49000 ? 335 ASN A ND2 1 
ATOM   2522 N  N   . THR A 1 342 ? 20.86600  19.05800  39.39900 1.000 32.49000 ? 336 THR A N   1 
ATOM   2523 C  CA  . THR A 1 342 ? 20.96300  19.10900  40.86500 1.000 35.41000 ? 336 THR A CA  1 
ATOM   2524 C  C   . THR A 1 342 ? 20.70100  20.49100  41.46600 1.000 35.49000 ? 336 THR A C   1 
ATOM   2525 O  O   . THR A 1 342 ? 20.69300  20.62300  42.69800 1.000 37.65000 ? 336 THR A O   1 
ATOM   2526 C  CB  . THR A 1 342 ? 22.35400  18.64600  41.30200 1.000 34.11000 ? 336 THR A CB  1 
ATOM   2527 O  OG1 . THR A 1 342 ? 23.35200  19.53100  40.74800 1.000 33.72000 ? 336 THR A OG1 1 
ATOM   2528 C  CG2 . THR A 1 342 ? 22.60600  17.22500  40.81700 1.000 30.78000 ? 336 THR A CG2 1 
ATOM   2529 N  N   . MET A 1 343 ? 20.56000  21.53400  40.64600 1.000 36.90000 ? 337 MET A N   1 
ATOM   2530 C  CA  . MET A 1 343 ? 20.26500  22.88100  41.13100 1.000 32.97000 ? 337 MET A CA  1 
ATOM   2531 C  C   . MET A 1 343 ? 18.90000  23.36600  40.66100 1.000 32.80000 ? 337 MET A C   1 
ATOM   2532 O  O   . MET A 1 343 ? 18.66300  24.57600  40.63300 1.000 36.19000 ? 337 MET A O   1 
ATOM   2533 C  CB  . MET A 1 343 ? 21.33600  23.87600  40.67500 1.000 38.64000 ? 337 MET A CB  1 
ATOM   2534 C  CG  . MET A 1 343 ? 22.71800  23.59000  41.19600 1.000 39.07000 ? 337 MET A CG  1 
ATOM   2535 S  SD  . MET A 1 343 ? 22.75600  23.81500  42.97400 1.000 41.28000 ? 337 MET A SD  1 
ATOM   2536 C  CE  . MET A 1 343 ? 22.69200  25.59200  43.09400 1.000 39.63000 ? 337 MET A CE  1 
ATOM   2537 N  N   . GLY A 1 344 ? 18.03600  22.45200  40.22800 1.000 34.54000 ? 338 GLY A N   1 
ATOM   2538 C  CA  . GLY A 1 344 ? 16.68300  22.77100  39.83500 1.000 38.53000 ? 338 GLY A CA  1 
ATOM   2539 C  C   . GLY A 1 344 ? 16.51600  23.38900  38.46300 1.000 39.95000 ? 338 GLY A C   1 
ATOM   2540 O  O   . GLY A 1 344 ? 15.44300  23.93000  38.18000 1.000 36.70000 ? 338 GLY A O   1 
ATOM   2541 N  N   . VAL A 1 345 ? 17.52400  23.31600  37.59100 1.000 38.20000 ? 339 VAL A N   1 
ATOM   2542 C  CA  . VAL A 1 345 ? 17.48500  23.95500  36.27400 1.000 35.93000 ? 339 VAL A CA  1 
ATOM   2543 C  C   . VAL A 1 345 ? 17.08600  22.92100  35.22600 1.000 33.12000 ? 339 VAL A C   1 
ATOM   2544 O  O   . VAL A 1 345 ? 17.58500  21.78900  35.23700 1.000 30.40000 ? 339 VAL A O   1 
ATOM   2545 C  CB  . VAL A 1 345 ? 18.85400  24.58200  35.94900 1.000 34.88000 ? 339 VAL A CB  1 
ATOM   2546 C  CG1 . VAL A 1 345 ? 18.87200  25.18900  34.53600 1.000 32.98000 ? 339 VAL A CG1 1 
ATOM   2547 C  CG2 . VAL A 1 345 ? 19.22400  25.61500  37.00800 1.000 33.06000 ? 339 VAL A CG2 1 
ATOM   2548 N  N   . THR A 1 346 ? 16.19800  23.30000  34.30800 1.000 31.29000 ? 340 THR A N   1 
ATOM   2549 C  CA  . THR A 1 346 ? 15.76400  22.37000  33.27100 1.000 33.05000 ? 340 THR A CA  1 
ATOM   2550 C  C   . THR A 1 346 ? 16.82800  22.28000  32.18600 1.000 33.21000 ? 340 THR A C   1 
ATOM   2551 O  O   . THR A 1 346 ? 17.11800  23.26800  31.51300 1.000 33.86000 ? 340 THR A O   1 
ATOM   2552 C  CB  . THR A 1 346 ? 14.43900  22.81200  32.66700 1.000 38.02000 ? 340 THR A CB  1 
ATOM   2553 O  OG1 . THR A 1 346 ? 13.40700  22.63300  33.64300 1.000 38.22000 ? 340 THR A OG1 1 
ATOM   2554 C  CG2 . THR A 1 346 ? 14.12800  21.96400  31.41700 1.000 29.56000 ? 340 THR A CG2 1 
ATOM   2555 N  N   . THR A 1 347 ? 17.39900  21.09600  31.99700 1.000 28.37000 ? 341 THR A N   1 
ATOM   2556 C  CA  . THR A 1 347 ? 18.53200  20.96400  31.10800 1.000 26.68000 ? 341 THR A CA  1 
ATOM   2557 C  C   . THR A 1 347 ? 18.19400  20.31300  29.76500 1.000 27.34000 ? 341 THR A C   1 
ATOM   2558 O  O   . THR A 1 347 ? 19.01100  20.39200  28.84100 1.000 24.64000 ? 341 THR A O   1 
ATOM   2559 C  CB  . THR A 1 347 ? 19.64300  20.17200  31.82000 1.000 27.67000 ? 341 THR A CB  1 
ATOM   2560 O  OG1 . THR A 1 347 ? 19.16000  18.88100  32.16800 1.000 29.41000 ? 341 THR A OG1 1 
ATOM   2561 C  CG2 . THR A 1 347 ? 20.05000  20.87900  33.09500 1.000 26.61000 ? 341 THR A CG2 1 
ATOM   2562 N  N   . GLY A 1 348 ? 17.02200  19.70400  29.60200 1.000 26.39000 ? 342 GLY A N   1 
ATOM   2563 C  CA  . GLY A 1 348 ? 16.76400  19.00300  28.36200 1.000 24.33000 ? 342 GLY A CA  1 
ATOM   2564 C  C   . GLY A 1 348 ? 15.37900  18.41600  28.34100 1.000 24.84000 ? 342 GLY A C   1 
ATOM   2565 O  O   . GLY A 1 348 ? 14.51400  18.83700  29.09900 1.000 24.59000 ? 342 GLY A O   1 
ATOM   2566 N  N   . GLY A 1 349 ? 15.17100  17.44200  27.46200 1.000 25.26000 ? 343 GLY A N   1 
ATOM   2567 C  CA  . GLY A 1 349 ? 13.84800  16.87000  27.34100 1.000 22.35000 ? 343 GLY A CA  1 
ATOM   2568 C  C   . GLY A 1 349 ? 13.83000  15.60400  26.50800 1.000 23.14000 ? 343 GLY A C   1 
ATOM   2569 O  O   . GLY A 1 349 ? 14.87100  15.03900  26.16400 1.000 22.01000 ? 343 GLY A O   1 
ATOM   2570 N  N   . VAL A 1 350 ? 12.60600  15.18500  26.19300 1.000 21.09000 ? 344 VAL A N   1 
ATOM   2571 C  CA  A VAL A 1 350 ? 12.30900  13.97200  25.44000 0.500 19.51000 ? 344 VAL A CA  1 
ATOM   2572 C  CA  B VAL A 1 350 ? 12.32400  13.97700  25.43400 0.500 19.51000 ? 344 VAL A CA  1 
ATOM   2573 C  C   . VAL A 1 350 ? 11.49500  14.36000  24.21300 1.000 22.32000 ? 344 VAL A C   1 
ATOM   2574 O  O   . VAL A 1 350 ? 10.62300  15.22900  24.28200 1.000 24.19000 ? 344 VAL A O   1 
ATOM   2575 C  CB  A VAL A 1 350 ? 11.54000  12.93700  26.29300 0.500 21.91000 ? 344 VAL A CB  1 
ATOM   2576 C  CB  B VAL A 1 350 ? 11.59500  12.94600  26.31900 0.500 21.91000 ? 344 VAL A CB  1 
ATOM   2577 C  CG1 A VAL A 1 350 ? 10.10800  13.41700  26.61100 0.500 18.95000 ? 344 VAL A CG1 1 
ATOM   2578 C  CG1 B VAL A 1 350 ? 11.23800  11.67400  25.52200 0.500 21.07000 ? 344 VAL A CG1 1 
ATOM   2579 C  CG2 A VAL A 1 350 ? 11.51400  11.57000  25.58900 0.500 21.19000 ? 344 VAL A CG2 1 
ATOM   2580 C  CG2 B VAL A 1 350 ? 12.45200  12.62800  27.55800 0.500 21.47000 ? 344 VAL A CG2 1 
ATOM   2581 N  N   . SER A 1 351 ? 11.78500  13.73300  23.08900 1.000 19.22000 ? 345 SER A N   1 
ATOM   2582 C  CA  . SER A 1 351 ? 11.07800  13.98400  21.83900 1.000 22.76000 ? 345 SER A CA  1 
ATOM   2583 C  C   . SER A 1 351 ? 10.71900  12.65500  21.19500 1.000 23.77000 ? 345 SER A C   1 
ATOM   2584 O  O   . SER A 1 351 ? 11.39600  11.65100  21.39500 1.000 19.44000 ? 345 SER A O   1 
ATOM   2585 C  CB  . SER A 1 351 ? 11.94200  14.76500  20.83600 1.000 22.11000 ? 345 SER A CB  1 
ATOM   2586 O  OG  . SER A 1 351 ? 12.09400  16.08900  21.27400 1.000 37.19000 ? 345 SER A OG  1 
ATOM   2587 N  N   . PHE A 1 352 ? 9.71100   12.70100  20.33500 1.000 21.19000 ? 346 PHE A N   1 
ATOM   2588 C  CA  . PHE A 1 352 ? 9.15600   11.51700  19.68700 1.000 21.03000 ? 346 PHE A CA  1 
ATOM   2589 C  C   . PHE A 1 352 ? 9.13200   11.71000  18.17600 1.000 22.19000 ? 346 PHE A C   1 
ATOM   2590 O  O   . PHE A 1 352 ? 8.05200   11.78900  17.56300 1.000 23.60000 ? 346 PHE A O   1 
ATOM   2591 C  CB  . PHE A 1 352 ? 7.74800   11.27600  20.22100 1.000 18.41000 ? 346 PHE A CB  1 
ATOM   2592 C  CG  . PHE A 1 352 ? 7.67200   11.21600  21.71500 1.000 17.99000 ? 346 PHE A CG  1 
ATOM   2593 C  CD1 . PHE A 1 352 ? 8.04100   10.04400  22.39500 1.000 18.28000 ? 346 PHE A CD1 1 
ATOM   2594 C  CD2 . PHE A 1 352 ? 7.20700   12.30300  22.45400 1.000 21.71000 ? 346 PHE A CD2 1 
ATOM   2595 C  CE1 . PHE A 1 352 ? 7.94700   9.97300   23.81400 1.000 17.83000 ? 346 PHE A CE1 1 
ATOM   2596 C  CE2 . PHE A 1 352 ? 7.10300   12.22400  23.86200 1.000 19.22000 ? 346 PHE A CE2 1 
ATOM   2597 C  CZ  . PHE A 1 352 ? 7.48700   11.06600  24.52800 1.000 15.74000 ? 346 PHE A CZ  1 
ATOM   2598 N  N   . PRO A 1 353 ? 10.29500  11.75800  17.53800 1.000 19.66000 ? 347 PRO A N   1 
ATOM   2599 C  CA  . PRO A 1 353 ? 10.33500  12.06100  16.09500 1.000 24.88000 ? 347 PRO A CA  1 
ATOM   2600 C  C   . PRO A 1 353 ? 9.94000   10.89000  15.19900 1.000 29.48000 ? 347 PRO A C   1 
ATOM   2601 O  O   . PRO A 1 353 ? 10.61100  10.60900  14.20200 1.000 32.67000 ? 347 PRO A O   1 
ATOM   2602 C  CB  . PRO A 1 353 ? 11.80400  12.44500  15.87800 1.000 24.47000 ? 347 PRO A CB  1 
ATOM   2603 C  CG  . PRO A 1 353 ? 12.52800  11.57100  16.88000 1.000 20.16000 ? 347 PRO A CG  1 
ATOM   2604 C  CD  . PRO A 1 353 ? 11.65900  11.58800  18.09400 1.000 17.71000 ? 347 PRO A CD  1 
ATOM   2605 N  N   . PHE A 1 354 ? 8.88200   10.18000  15.54000 1.000 28.11000 ? 348 PHE A N   1 
ATOM   2606 C  CA  . PHE A 1 354 ? 8.41700   9.08500   14.70300 1.000 31.67000 ? 348 PHE A CA  1 
ATOM   2607 C  C   . PHE A 1 354 ? 6.96500   9.30900   14.30300 1.000 32.82000 ? 348 PHE A C   1 
ATOM   2608 O  O   . PHE A 1 354 ? 6.25100   10.14900  14.87200 1.000 30.36000 ? 348 PHE A O   1 
ATOM   2609 C  CB  . PHE A 1 354 ? 8.54800   7.74300   15.41000 1.000 27.44000 ? 348 PHE A CB  1 
ATOM   2610 C  CG  . PHE A 1 354 ? 7.88800   7.70500   16.74300 1.000 27.14000 ? 348 PHE A CG  1 
ATOM   2611 C  CD1 . PHE A 1 354 ? 6.50600   7.67800   16.85500 1.000 26.80000 ? 348 PHE A CD1 1 
ATOM   2612 C  CD2 . PHE A 1 354 ? 8.65900   7.67700   17.89900 1.000 24.89000 ? 348 PHE A CD2 1 
ATOM   2613 C  CE1 . PHE A 1 354 ? 5.88600   7.62700   18.09900 1.000 26.68000 ? 348 PHE A CE1 1 
ATOM   2614 C  CE2 . PHE A 1 354 ? 8.04100   7.61300   19.14700 1.000 22.52000 ? 348 PHE A CE2 1 
ATOM   2615 C  CZ  . PHE A 1 354 ? 6.66900   7.60200   19.24800 1.000 21.78000 ? 348 PHE A CZ  1 
ATOM   2616 N  N   . LYS A 1 355 ? 6.52900   8.50100   13.33300 1.000 30.52000 ? 349 LYS A N   1 
ATOM   2617 C  CA  . LYS A 1 355 ? 5.16900   8.54500   12.81400 1.000 24.82000 ? 349 LYS A CA  1 
ATOM   2618 C  C   . LYS A 1 355 ? 4.60900   7.13300   12.85500 1.000 25.91000 ? 349 LYS A C   1 
ATOM   2619 O  O   . LYS A 1 355 ? 5.28000   6.19000   12.42100 1.000 23.26000 ? 349 LYS A O   1 
ATOM   2620 C  CB  . LYS A 1 355 ? 5.13600   9.07500   11.37800 1.000 31.88000 ? 349 LYS A CB  1 
ATOM   2621 C  CG  . LYS A 1 355 ? 5.63500   10.52600  11.15400 1.000 35.97000 ? 349 LYS A CG  1 
ATOM   2622 C  CD  . LYS A 1 355 ? 5.79200   10.75700  9.64800  1.000 39.43000 ? 349 LYS A CD  1 
ATOM   2623 C  CE  . LYS A 1 355 ? 5.51300   12.17900  9.20300  1.000 43.49000 ? 349 LYS A CE  1 
ATOM   2624 N  NZ  . LYS A 1 355 ? 5.73100   12.28500  7.72800  1.000 47.15000 ? 349 LYS A NZ  1 
ATOM   2625 N  N   . LEU A 1 356 ? 3.38900   6.97600   13.36600 1.000 25.00000 ? 350 LEU A N   1 
ATOM   2626 C  CA  . LEU A 1 356 ? 2.73800   5.67400   13.29600 1.000 26.11000 ? 350 LEU A CA  1 
ATOM   2627 C  C   . LEU A 1 356 ? 2.43700   5.36900   11.84600 1.000 25.88000 ? 350 LEU A C   1 
ATOM   2628 O  O   . LEU A 1 356 ? 1.86100   6.19500   11.15200 1.000 29.27000 ? 350 LEU A O   1 
ATOM   2629 C  CB  . LEU A 1 356 ? 1.42500   5.67000   14.07900 1.000 25.59000 ? 350 LEU A CB  1 
ATOM   2630 C  CG  . LEU A 1 356 ? 1.47800   5.37600   15.56700 1.000 33.25000 ? 350 LEU A CG  1 
ATOM   2631 C  CD1 . LEU A 1 356 ? 0.09500   5.46300   16.21000 1.000 26.38000 ? 350 LEU A CD1 1 
ATOM   2632 C  CD2 . LEU A 1 356 ? 2.03500   3.99400   15.72500 1.000 26.86000 ? 350 LEU A CD2 1 
ATOM   2633 N  N   . ARG A 1 357 ? 2.79000   4.17000   11.42400 1.000 27.88000 ? 351 ARG A N   1 
ATOM   2634 C  CA  . ARG A 1 357 ? 2.44400   3.76700   10.04800 1.000 31.68000 ? 351 ARG A CA  1 
ATOM   2635 C  C   . ARG A 1 357 ? 1.18400   2.90800   10.09700 1.000 34.28000 ? 351 ARG A C   1 
ATOM   2636 O  O   . ARG A 1 357 ? 1.03500   2.13200   11.03600 1.000 31.99000 ? 351 ARG A O   1 
ATOM   2637 C  CB  . ARG A 1 357 ? 3.62900   3.09100   9.35300  1.000 35.08000 ? 351 ARG A CB  1 
ATOM   2638 C  CG  . ARG A 1 357 ? 3.92400   1.65900   9.75700  1.000 33.17000 ? 351 ARG A CG  1 
ATOM   2639 C  CD  . ARG A 1 357 ? 5.16200   1.26400   8.97900  1.000 40.55000 ? 351 ARG A CD  1 
ATOM   2640 N  NE  . ARG A 1 357 ? 5.54500   -0.11700  9.19600  1.000 43.92000 ? 351 ARG A NE  1 
ATOM   2641 C  CZ  . ARG A 1 357 ? 6.46700   -0.51500  10.06100 1.000 43.48000 ? 351 ARG A CZ  1 
ATOM   2642 N  NH1 . ARG A 1 357 ? 7.13100   0.37100   10.78200 1.000 31.81000 ? 351 ARG A NH1 1 
ATOM   2643 N  NH2 . ARG A 1 357 ? 6.71800   -1.80300  10.19400 1.000 35.76000 ? 351 ARG A NH2 1 
ATOM   2644 N  N   . GLY A 1 358 ? 0.29400   3.12200   9.13600  1.000 35.65000 ? 352 GLY A N   1 
ATOM   2645 C  CA  . GLY A 1 358 ? -0.90800  2.28800   9.02600  1.000 38.72000 ? 352 GLY A CA  1 
ATOM   2646 C  C   . GLY A 1 358 ? -0.79700  1.40100   7.80000  1.000 43.29000 ? 352 GLY A C   1 
ATOM   2647 O  O   . GLY A 1 358 ? -1.40100  0.31900   7.84500  1.000 55.50000 ? 352 GLY A O   1 
ATOM   2648 N  N   . ASP B 1 3   ? 25.48800  -12.55500 6.02700  1.000 64.45000 ? -3  ASP B N   1 
ATOM   2649 C  CA  . ASP B 1 3   ? 26.68200  -12.44300 5.18500  1.000 69.64000 ? -3  ASP B CA  1 
ATOM   2650 C  C   . ASP B 1 3   ? 27.75900  -11.52700 5.80900  1.000 65.13000 ? -3  ASP B C   1 
ATOM   2651 O  O   . ASP B 1 3   ? 27.53100  -10.31700 5.97100  1.000 59.97000 ? -3  ASP B O   1 
ATOM   2652 C  CB  . ASP B 1 3   ? 26.29900  -11.92900 3.78800  1.000 65.17000 ? -3  ASP B CB  1 
ATOM   2653 C  CG  . ASP B 1 3   ? 27.50500  -11.80800 2.85000  1.000 67.00000 ? -3  ASP B CG  1 
ATOM   2654 O  OD1 . ASP B 1 3   ? 28.48800  -12.57400 3.00100  1.000 66.88000 ? -3  ASP B OD1 1 
ATOM   2655 O  OD2 . ASP B 1 3   ? 27.47500  -10.92900 1.95900  1.000 67.55000 ? -3  ASP B OD2 1 
ATOM   2656 N  N   . PRO B 1 4   ? 28.93100  -12.10000 6.13400  1.000 66.61000 ? -2  PRO B N   1 
ATOM   2657 C  CA  . PRO B 1 4   ? 29.99100  -11.31700 6.79500  1.000 63.99000 ? -2  PRO B CA  1 
ATOM   2658 C  C   . PRO B 1 4   ? 30.80200  -10.43900 5.85300  1.000 63.38000 ? -2  PRO B C   1 
ATOM   2659 O  O   . PRO B 1 4   ? 31.64700  -9.66500  6.32800  1.000 64.86000 ? -2  PRO B O   1 
ATOM   2660 C  CB  . PRO B 1 4   ? 30.88300  -12.40300 7.41300  1.000 56.87000 ? -2  PRO B CB  1 
ATOM   2661 C  CG  . PRO B 1 4   ? 30.81100  -13.50600 6.38900  1.000 55.54000 ? -2  PRO B CG  1 
ATOM   2662 C  CD  . PRO B 1 4   ? 29.36800  -13.49300 5.88600  1.000 63.02000 ? -2  PRO B CD  1 
ATOM   2663 N  N   . PHE B 1 5   ? 30.58400  -10.54000 4.54300  1.000 60.63000 ? -1  PHE B N   1 
ATOM   2664 C  CA  . PHE B 1 5   ? 31.33600  -9.76700  3.56600  1.000 62.58000 ? -1  PHE B CA  1 
ATOM   2665 C  C   . PHE B 1 5   ? 30.61200  -8.48900  3.15400  1.000 59.89000 ? -1  PHE B C   1 
ATOM   2666 O  O   . PHE B 1 5   ? 31.06900  -7.79400  2.24100  1.000 56.07000 ? -1  PHE B O   1 
ATOM   2667 C  CB  . PHE B 1 5   ? 31.65600  -10.64300 2.35200  1.000 62.59000 ? -1  PHE B CB  1 
ATOM   2668 C  CG  . PHE B 1 5   ? 32.54500  -11.81900 2.68100  1.000 60.47000 ? -1  PHE B CG  1 
ATOM   2669 C  CD1 . PHE B 1 5   ? 33.87400  -11.61600 3.06800  1.000 60.98000 ? -1  PHE B CD1 1 
ATOM   2670 C  CD2 . PHE B 1 5   ? 32.05300  -13.12200 2.63000  1.000 62.78000 ? -1  PHE B CD2 1 
ATOM   2671 C  CE1 . PHE B 1 5   ? 34.70500  -12.70000 3.38700  1.000 55.50000 ? -1  PHE B CE1 1 
ATOM   2672 C  CE2 . PHE B 1 5   ? 32.87500  -14.21600 2.94100  1.000 56.32000 ? -1  PHE B CE2 1 
ATOM   2673 C  CZ  . PHE B 1 5   ? 34.20400  -14.00300 3.32000  1.000 51.87000 ? -1  PHE B CZ  1 
ATOM   2674 N  N   . THR B 1 6   ? 29.49700  -8.16400  3.81800  1.000 58.95000 ? 0   THR B N   1 
ATOM   2675 C  CA  . THR B 1 6   ? 28.78100  -6.90600  3.64000  1.000 56.60000 ? 0   THR B CA  1 
ATOM   2676 C  C   . THR B 1 6   ? 28.38300  -6.31800  4.99200  1.000 55.60000 ? 0   THR B C   1 
ATOM   2677 O  O   . THR B 1 6   ? 27.30900  -5.70200  5.11300  1.000 49.70000 ? 0   THR B O   1 
ATOM   2678 C  CB  . THR B 1 6   ? 27.52100  -7.07300  2.75700  1.000 55.30000 ? 0   THR B CB  1 
ATOM   2679 O  OG1 . THR B 1 6   ? 26.56900  -7.94300  3.39600  1.000 52.87000 ? 0   THR B OG1 1 
ATOM   2680 C  CG2 . THR B 1 6   ? 27.87100  -7.62400  1.36700  1.000 56.04000 ? 0   THR B CG2 1 
ATOM   2681 N  N   . MET B 1 7   ? 29.21300  -6.52900  6.02200  1.000 51.27000 ? 1   MET B N   1 
ATOM   2682 C  CA  . MET B 1 7   ? 28.94200  -5.95100  7.33300  1.000 48.38000 ? 1   MET B CA  1 
ATOM   2683 C  C   . MET B 1 7   ? 29.18600  -4.44600  7.29500  1.000 48.42000 ? 1   MET B C   1 
ATOM   2684 O  O   . MET B 1 7   ? 30.07100  -3.96100  6.57800  1.000 47.92000 ? 1   MET B O   1 
ATOM   2685 C  CB  . MET B 1 7   ? 29.81700  -6.59400  8.41500  1.000 49.97000 ? 1   MET B CB  1 
ATOM   2686 C  CG  . MET B 1 7   ? 29.48900  -8.05700  8.72400  1.000 52.12000 ? 1   MET B CG  1 
ATOM   2687 S  SD  . MET B 1 7   ? 27.72300  -8.41500  9.01200  1.000 52.13000 ? 1   MET B SD  1 
ATOM   2688 C  CE  . MET B 1 7   ? 27.35900  -7.55200  10.55400 1.000 40.37000 ? 1   MET B CE  1 
ATOM   2689 N  N   . THR B 1 8   ? 28.39900  -3.70200  8.07200  1.000 40.31000 ? 2   THR B N   1 
ATOM   2690 C  CA  . THR B 1 8   ? 28.37900  -2.24800  7.97700  1.000 40.55000 ? 2   THR B CA  1 
ATOM   2691 C  C   . THR B 1 8   ? 28.46100  -1.60000  9.35500  1.000 36.99000 ? 2   THR B C   1 
ATOM   2692 O  O   . THR B 1 8   ? 28.09100  -2.22000  10.36100 1.000 35.87000 ? 2   THR B O   1 
ATOM   2693 C  CB  . THR B 1 8   ? 27.10200  -1.77800  7.25300  1.000 42.93000 ? 2   THR B CB  1 
ATOM   2694 O  OG1 . THR B 1 8   ? 25.95500  -2.13700  8.03600  1.000 38.81000 ? 2   THR B OG1 1 
ATOM   2695 C  CG2 . THR B 1 8   ? 26.99100  -2.40700  5.84400  1.000 36.67000 ? 2   THR B CG2 1 
ATOM   2696 N  N   . PRO B 1 9   ? 28.94700  -0.33300  9.43600  1.000 35.62000 ? 3   PRO B N   1 
ATOM   2697 C  CA  . PRO B 1 9   ? 28.91100  0.40000   10.72400 1.000 30.66000 ? 3   PRO B CA  1 
ATOM   2698 C  C   . PRO B 1 9   ? 27.56700  0.34900   11.44800 1.000 32.52000 ? 3   PRO B C   1 
ATOM   2699 O  O   . PRO B 1 9   ? 27.53100  0.27300   12.68500 1.000 30.61000 ? 3   PRO B O   1 
ATOM   2700 C  CB  . PRO B 1 9   ? 29.25000  1.83800   10.30300 1.000 31.84000 ? 3   PRO B CB  1 
ATOM   2701 C  CG  . PRO B 1 9   ? 30.17200  1.66200   9.14400  1.000 36.54000 ? 3   PRO B CG  1 
ATOM   2702 C  CD  . PRO B 1 9   ? 29.63200  0.45000   8.38500  1.000 36.76000 ? 3   PRO B CD  1 
ATOM   2703 N  N   . SER B 1 10  ? 26.45500  0.41100   10.71300 1.000 33.43000 ? 4   SER B N   1 
ATOM   2704 C  CA  . SER B 1 10  ? 25.14000  0.40400   11.33900 1.000 32.08000 ? 4   SER B CA  1 
ATOM   2705 C  C   . SER B 1 10  ? 24.84300  -0.91500  12.04500 1.000 31.53000 ? 4   SER B C   1 
ATOM   2706 O  O   . SER B 1 10  ? 23.81600  -1.01500  12.73000 1.000 32.14000 ? 4   SER B O   1 
ATOM   2707 C  CB  . SER B 1 10  ? 24.06700  0.69600   10.28400 1.000 34.33000 ? 4   SER B CB  1 
ATOM   2708 O  OG  . SER B 1 10  ? 24.08500  -0.30700  9.26800  1.000 33.44000 ? 4   SER B OG  1 
ATOM   2709 N  N   . GLU B 1 11  ? 25.70300  -1.92500  11.88400 1.000 28.83000 ? 5   GLU B N   1 
ATOM   2710 C  CA  . GLU B 1 11  ? 25.53600  -3.22100  12.53600 1.000 32.59000 ? 5   GLU B CA  1 
ATOM   2711 C  C   . GLU B 1 11  ? 26.46100  -3.37800  13.74100 1.000 25.40000 ? 5   GLU B C   1 
ATOM   2712 O  O   . GLU B 1 11  ? 26.66100  -4.50000  14.22200 1.000 22.77000 ? 5   GLU B O   1 
ATOM   2713 C  CB  . GLU B 1 11  ? 25.74500  -4.35900  11.51900 1.000 31.23000 ? 5   GLU B CB  1 
ATOM   2714 C  CG  . GLU B 1 11  ? 24.64200  -4.39000  10.44700 1.000 35.51000 ? 5   GLU B CG  1 
ATOM   2715 C  CD  . GLU B 1 11  ? 25.01400  -5.16500  9.17700  1.000 44.17000 ? 5   GLU B CD  1 
ATOM   2716 O  OE1 . GLU B 1 11  ? 25.97900  -4.76300  8.47200  1.000 44.39000 ? 5   GLU B OE1 1 
ATOM   2717 O  OE2 . GLU B 1 11  ? 24.31400  -6.16600  8.87000  1.000 48.68000 ? 5   GLU B OE2 1 
ATOM   2718 N  N   . ASP B 1 12  ? 26.99800  -2.27300  14.26500 1.000 23.09000 ? 6   ASP B N   1 
ATOM   2719 C  CA  . ASP B 1 12  ? 27.94800  -2.35300  15.37200 1.000 21.74000 ? 6   ASP B CA  1 
ATOM   2720 C  C   . ASP B 1 12  ? 27.15800  -2.31600  16.67600 1.000 21.06000 ? 6   ASP B C   1 
ATOM   2721 O  O   . ASP B 1 12  ? 26.75600  -1.25300  17.14100 1.000 17.97000 ? 6   ASP B O   1 
ATOM   2722 C  CB  . ASP B 1 12  ? 28.97000  -1.23300  15.26800 1.000 18.80000 ? 6   ASP B CB  1 
ATOM   2723 C  CG  . ASP B 1 12  ? 30.01900  -1.52000  14.21400 1.000 22.01000 ? 6   ASP B CG  1 
ATOM   2724 O  OD1 . ASP B 1 12  ? 30.28800  -2.72800  13.91200 1.000 23.17000 ? 6   ASP B OD1 1 
ATOM   2725 O  OD2 . ASP B 1 12  ? 30.58000  -0.54200  13.67600 1.000 20.70000 ? 6   ASP B OD2 1 
ATOM   2726 N  N   . PHE B 1 13  ? 26.91800  -3.49700  17.26300 1.000 18.38000 ? 7   PHE B N   1 
ATOM   2727 C  CA  . PHE B 1 13  ? 26.04000  -3.61800  18.41200 1.000 19.33000 ? 7   PHE B CA  1 
ATOM   2728 C  C   . PHE B 1 13  ? 26.73300  -4.35600  19.53400 1.000 17.67000 ? 7   PHE B C   1 
ATOM   2729 O  O   . PHE B 1 13  ? 27.60800  -5.19100  19.31100 1.000 19.32000 ? 7   PHE B O   1 
ATOM   2730 C  CB  . PHE B 1 13  ? 24.77000  -4.41500  18.10100 1.000 18.93000 ? 7   PHE B CB  1 
ATOM   2731 C  CG  . PHE B 1 13  ? 23.80000  -3.71900  17.22700 1.000 19.86000 ? 7   PHE B CG  1 
ATOM   2732 C  CD1 . PHE B 1 13  ? 22.82400  -2.88900  17.77300 1.000 20.64000 ? 7   PHE B CD1 1 
ATOM   2733 C  CD2 . PHE B 1 13  ? 23.79900  -3.94100  15.85600 1.000 26.00000 ? 7   PHE B CD2 1 
ATOM   2734 C  CE1 . PHE B 1 13  ? 21.87200  -2.27500  16.97000 1.000 26.36000 ? 7   PHE B CE1 1 
ATOM   2735 C  CE2 . PHE B 1 13  ? 22.84500  -3.31000  15.03600 1.000 30.37000 ? 7   PHE B CE2 1 
ATOM   2736 C  CZ  . PHE B 1 13  ? 21.87900  -2.48400  15.60400 1.000 29.04000 ? 7   PHE B CZ  1 
ATOM   2737 N  N   . VAL B 1 14  ? 26.25800  -4.09700  20.75300 1.000 17.38000 ? 8   VAL B N   1 
ATOM   2738 C  CA  . VAL B 1 14  ? 26.49800  -4.98800  21.87800 1.000 17.11000 ? 8   VAL B CA  1 
ATOM   2739 C  C   . VAL B 1 14  ? 25.12800  -5.49700  22.31300 1.000 15.85000 ? 8   VAL B C   1 
ATOM   2740 O  O   . VAL B 1 14  ? 24.18500  -4.71300  22.44000 1.000 16.02000 ? 8   VAL B O   1 
ATOM   2741 C  CB  . VAL B 1 14  ? 27.29000  -4.30100  23.01900 1.000 16.57000 ? 8   VAL B CB  1 
ATOM   2742 C  CG1 . VAL B 1 14  ? 26.64500  -3.00000  23.50100 1.000 17.37000 ? 8   VAL B CG1 1 
ATOM   2743 C  CG2 . VAL B 1 14  ? 27.55000  -5.28400  24.18900 1.000 18.55000 ? 8   VAL B CG2 1 
ATOM   2744 N  N   . VAL B 1 15  ? 25.01100  -6.80800  22.48900 1.000 16.50000 ? 9   VAL B N   1 
ATOM   2745 C  CA  . VAL B 1 15  ? 23.71700  -7.49100  22.58600 1.000 16.35000 ? 9   VAL B CA  1 
ATOM   2746 C  C   . VAL B 1 15  ? 23.71800  -8.35700  23.84800 1.000 17.62000 ? 9   VAL B C   1 
ATOM   2747 O  O   . VAL B 1 15  ? 24.70900  -9.03600  24.13400 1.000 19.24000 ? 9   VAL B O   1 
ATOM   2748 C  CB  . VAL B 1 15  ? 23.51000  -8.34700  21.31500 1.000 19.56000 ? 9   VAL B CB  1 
ATOM   2749 C  CG1 . VAL B 1 15  ? 22.29200  -9.22400  21.42100 1.000 20.89000 ? 9   VAL B CG1 1 
ATOM   2750 C  CG2 . VAL B 1 15  ? 23.47300  -7.44700  20.06500 1.000 18.29000 ? 9   VAL B CG2 1 
ATOM   2751 N  N   . THR B 1 16  ? 22.62300  -8.34300  24.60600 1.000 18.23000 ? 10  THR B N   1 
ATOM   2752 C  CA  . THR B 1 16  ? 22.44900  -9.30700  25.68100 1.000 17.20000 ? 10  THR B CA  1 
ATOM   2753 C  C   . THR B 1 16  ? 21.40600  -10.32700 25.26100 1.000 20.52000 ? 10  THR B C   1 
ATOM   2754 O  O   . THR B 1 16  ? 20.46100  -10.00500 24.52900 1.000 20.32000 ? 10  THR B O   1 
ATOM   2755 C  CB  . THR B 1 16  ? 22.00800  -8.65900  27.00300 1.000 16.92000 ? 10  THR B CB  1 
ATOM   2756 O  OG1 . THR B 1 16  ? 20.82000  -7.93700  26.78800 1.000 20.18000 ? 10  THR B OG1 1 
ATOM   2757 C  CG2 . THR B 1 16  ? 23.04900  -7.66200  27.49700 1.000 21.98000 ? 10  THR B CG2 1 
ATOM   2758 N  N   . ASP B 1 17  ? 21.55200  -11.54700 25.76100 1.000 17.87000 ? 11  ASP B N   1 
ATOM   2759 C  CA  . ASP B 1 17  ? 20.62000  -12.60200 25.41600 1.000 20.16000 ? 11  ASP B CA  1 
ATOM   2760 C  C   . ASP B 1 17  ? 20.12700  -13.30700 26.66000 1.000 18.85000 ? 11  ASP B C   1 
ATOM   2761 O  O   . ASP B 1 17  ? 20.75200  -13.28500 27.72400 1.000 21.16000 ? 11  ASP B O   1 
ATOM   2762 C  CB  . ASP B 1 17  ? 21.23300  -13.65000 24.46400 1.000 20.51000 ? 11  ASP B CB  1 
ATOM   2763 C  CG  . ASP B 1 17  ? 22.34800  -14.50000 25.13800 1.000 25.64000 ? 11  ASP B CG  1 
ATOM   2764 O  OD1 . ASP B 1 17  ? 23.48100  -13.99000 25.26400 1.000 26.31000 ? 11  ASP B OD1 1 
ATOM   2765 O  OD2 . ASP B 1 17  ? 22.10300  -15.66000 25.56100 1.000 24.35000 ? 11  ASP B OD2 1 
ATOM   2766 N  N   . ARG B 1 18  ? 19.02200  -14.00400 26.48300 1.000 20.15000 ? 12  ARG B N   1 
ATOM   2767 C  CA  . ARG B 1 18  ? 18.50200  -14.91800 27.48500 1.000 21.55000 ? 12  ARG B CA  1 
ATOM   2768 C  C   . ARG B 1 18  ? 18.37400  -16.26800 26.78800 1.000 23.73000 ? 12  ARG B C   1 
ATOM   2769 O  O   . ARG B 1 18  ? 17.55700  -16.42500 25.87600 1.000 24.84000 ? 12  ARG B O   1 
ATOM   2770 C  CB  . ARG B 1 18  ? 17.17400  -14.38000 28.04000 1.000 21.25000 ? 12  ARG B CB  1 
ATOM   2771 C  CG  . ARG B 1 18  ? 16.59400  -15.15200 29.21700 1.000 24.25000 ? 12  ARG B CG  1 
ATOM   2772 C  CD  . ARG B 1 18  ? 15.40600  -14.39100 29.81800 1.000 20.28000 ? 12  ARG B CD  1 
ATOM   2773 N  NE  . ARG B 1 18  ? 15.86700  -13.11300 30.34200 1.000 23.66000 ? 12  ARG B NE  1 
ATOM   2774 C  CZ  . ARG B 1 18  ? 16.25200  -12.90800 31.59900 1.000 27.46000 ? 12  ARG B CZ  1 
ATOM   2775 N  NH1 . ARG B 1 18  ? 16.18500  -13.87200 32.51400 1.000 22.62000 ? 12  ARG B NH1 1 
ATOM   2776 N  NH2 . ARG B 1 18  ? 16.73400  -11.71200 31.94200 1.000 23.31000 ? 12  ARG B NH2 1 
ATOM   2777 N  N   . GLY B 1 19  ? 19.23400  -17.22500 27.15600 1.000 25.41000 ? 13  GLY B N   1 
ATOM   2778 C  CA  . GLY B 1 19  ? 19.17000  -18.53200 26.52300 1.000 25.30000 ? 13  GLY B CA  1 
ATOM   2779 C  C   . GLY B 1 19  ? 19.38300  -18.48000 25.02700 1.000 25.10000 ? 13  GLY B C   1 
ATOM   2780 O  O   . GLY B 1 19  ? 18.84000  -19.31300 24.29200 1.000 27.11000 ? 13  GLY B O   1 
ATOM   2781 N  N   . GLY B 1 20  ? 20.14700  -17.52100 24.55400 1.000 25.62000 ? 14  GLY B N   1 
ATOM   2782 C  CA  . GLY B 1 20  ? 20.37200  -17.36600 23.14000 1.000 23.55000 ? 14  GLY B CA  1 
ATOM   2783 C  C   . GLY B 1 20  ? 19.34600  -16.50500 22.43000 1.000 26.72000 ? 14  GLY B C   1 
ATOM   2784 O  O   . GLY B 1 20  ? 19.55600  -16.18000 21.26100 1.000 27.27000 ? 14  GLY B O   1 
ATOM   2785 N  N   . ILE B 1 21  ? 18.23800  -16.13300 23.08900 1.000 20.85000 ? 15  ILE B N   1 
ATOM   2786 C  CA  . ILE B 1 21  ? 17.23800  -15.24600 22.51000 1.000 20.85000 ? 15  ILE B CA  1 
ATOM   2787 C  C   . ILE B 1 21  ? 17.62600  -13.80400 22.80800 1.000 20.93000 ? 15  ILE B C   1 
ATOM   2788 O  O   . ILE B 1 21  ? 17.89900  -13.46700 23.96600 1.000 17.82000 ? 15  ILE B O   1 
ATOM   2789 C  CB  . ILE B 1 21  ? 15.85300  -15.55200 23.09500 1.000 19.93000 ? 15  ILE B CB  1 
ATOM   2790 C  CG1 . ILE B 1 21  ? 15.53200  -17.04000 22.93200 1.000 22.24000 ? 15  ILE B CG1 1 
ATOM   2791 C  CG2 . ILE B 1 21  ? 14.84100  -14.61100 22.49600 1.000 20.27000 ? 15  ILE B CG2 1 
ATOM   2792 C  CD1 . ILE B 1 21  ? 14.49500  -17.57000 23.92900 1.000 21.54000 ? 15  ILE B CD1 1 
ATOM   2793 N  N   . VAL B 1 22  ? 17.64700  -12.94000 21.77800 1.000 20.84000 ? 16  VAL B N   1 
ATOM   2794 C  CA  . VAL B 1 22  ? 18.07300  -11.54900 21.99000 1.000 20.28000 ? 16  VAL B CA  1 
ATOM   2795 C  C   . VAL B 1 22  ? 17.13000  -10.84100 22.96400 1.000 19.37000 ? 16  VAL B C   1 
ATOM   2796 O  O   . VAL B 1 22  ? 15.90100  -10.85900 22.80300 1.000 18.52000 ? 16  VAL B O   1 
ATOM   2797 C  CB  . VAL B 1 22  ? 18.16100  -10.77000 20.66600 1.000 20.51000 ? 16  VAL B CB  1 
ATOM   2798 C  CG1 . VAL B 1 22  ? 18.30100  -9.27700  20.96500 1.000 18.13000 ? 16  VAL B CG1 1 
ATOM   2799 C  CG2 . VAL B 1 22  ? 19.36200  -11.23100 19.86000 1.000 20.05000 ? 16  VAL B CG2 1 
ATOM   2800 N  N   . GLU B 1 23  ? 17.71700  -10.19200 23.97400 1.000 16.68000 ? 17  GLU B N   1 
ATOM   2801 C  CA  . GLU B 1 23  ? 16.97200  -9.45200  24.97000 1.000 17.96000 ? 17  GLU B CA  1 
ATOM   2802 C  C   . GLU B 1 23  ? 16.98400  -7.98500  24.53700 1.000 17.43000 ? 17  GLU B C   1 
ATOM   2803 O  O   . GLU B 1 23  ? 15.96100  -7.43500  24.07900 1.000 15.22000 ? 17  GLU B O   1 
ATOM   2804 C  CB  . GLU B 1 23  ? 17.60300  -9.65600  26.36600 1.000 18.13000 ? 17  GLU B CB  1 
ATOM   2805 C  CG  . GLU B 1 23  ? 16.84700  -8.94800  27.52500 1.000 24.01000 ? 17  GLU B CG  1 
ATOM   2806 C  CD  . GLU B 1 23  ? 15.82900  -9.83800  28.22500 1.000 22.27000 ? 17  GLU B CD  1 
ATOM   2807 O  OE1 . GLU B 1 23  ? 16.29400  -10.79200 28.89600 1.000 23.54000 ? 17  GLU B OE1 1 
ATOM   2808 O  OE2 . GLU B 1 23  ? 14.56400  -9.62100  28.10200 1.000 21.95000 ? 17  GLU B OE2 1 
ATOM   2809 N  N   . ASN B 1 24  ? 18.13900  -7.35100  24.68500 1.000 16.95000 ? 18  ASN B N   1 
ATOM   2810 C  CA  . ASN B 1 24  ? 18.36100  -5.95100  24.32400 1.000 17.44000 ? 18  ASN B CA  1 
ATOM   2811 C  C   . ASN B 1 24  ? 19.51700  -5.85700  23.34600 1.000 17.96000 ? 18  ASN B C   1 
ATOM   2812 O  O   . ASN B 1 24  ? 20.45700  -6.64300  23.41900 1.000 17.15000 ? 18  ASN B O   1 
ATOM   2813 C  CB  . ASN B 1 24  ? 18.75600  -5.10300  25.52600 1.000 15.96000 ? 18  ASN B CB  1 
ATOM   2814 C  CG  . ASN B 1 24  ? 17.74800  -5.15000  26.61700 1.000 18.77000 ? 18  ASN B CG  1 
ATOM   2815 O  OD1 . ASN B 1 24  ? 16.55000  -5.15500  26.36200 1.000 18.29000 ? 18  ASN B OD1 1 
ATOM   2816 N  ND2 . ASN B 1 24  ? 18.22400  -5.19300  27.85600 1.000 19.19000 ? 18  ASN B ND2 1 
ATOM   2817 N  N   . SER B 1 25  ? 19.52800  -4.81300  22.51100 1.000 15.59000 ? 19  SER B N   1 
ATOM   2818 C  CA  . SER B 1 25  ? 20.75800  -4.50500  21.78900 1.000 14.85000 ? 19  SER B CA  1 
ATOM   2819 C  C   . SER B 1 25  ? 21.00100  -3.00800  21.79600 1.000 16.10000 ? 19  SER B C   1 
ATOM   2820 O  O   . SER B 1 25  ? 20.06100  -2.21100  21.86300 1.000 16.05000 ? 19  SER B O   1 
ATOM   2821 C  CB  . SER B 1 25  ? 20.73200  -5.01000  20.35400 1.000 18.45000 ? 19  SER B CB  1 
ATOM   2822 O  OG  . SER B 1 25  ? 19.65900  -4.37500  19.66500 1.000 20.05000 ? 19  SER B OG  1 
ATOM   2823 N  N   . HIS B 1 26  ? 22.28500  -2.64300  21.72200 1.000 15.60000 ? 20  HIS B N   1 
ATOM   2824 C  CA  . HIS B 1 26  ? 22.77000  -1.28900  21.96300 1.000 14.91000 ? 20  HIS B CA  1 
ATOM   2825 C  C   . HIS B 1 26  ? 23.74000  -0.91700  20.84800 1.000 13.41000 ? 20  HIS B C   1 
ATOM   2826 O  O   . HIS B 1 26  ? 24.67900  -1.66700  20.57900 1.000 14.95000 ? 20  HIS B O   1 
ATOM   2827 C  CB  . HIS B 1 26  ? 23.48000  -1.21500  23.32700 1.000 14.86000 ? 20  HIS B CB  1 
ATOM   2828 C  CG  . HIS B 1 26  ? 22.68700  -1.81700  24.45100 1.000 15.31000 ? 20  HIS B CG  1 
ATOM   2829 N  ND1 . HIS B 1 26  ? 21.99800  -1.05200  25.36600 1.000 13.80000 ? 20  HIS B ND1 1 
ATOM   2830 C  CD2 . HIS B 1 26  ? 22.48400  -3.10900  24.81400 1.000 17.50000 ? 20  HIS B CD2 1 
ATOM   2831 C  CE1 . HIS B 1 26  ? 21.38000  -1.84300  26.22900 1.000 17.89000 ? 20  HIS B CE1 1 
ATOM   2832 N  NE2 . HIS B 1 26  ? 21.67300  -3.09800  25.92700 1.000 15.42000 ? 20  HIS B NE2 1 
ATOM   2833 N  N   . ARG B 1 27  ? 23.50600  0.21500   20.18700 1.000 14.40000 ? 21  ARG B N   1 
ATOM   2834 C  CA  . ARG B 1 27  ? 24.42000  0.67600   19.15300 1.000 15.20000 ? 21  ARG B CA  1 
ATOM   2835 C  C   . ARG B 1 27  ? 25.68800  1.26800   19.76300 1.000 14.59000 ? 21  ARG B C   1 
ATOM   2836 O  O   . ARG B 1 27  ? 25.62500  2.00600   20.73800 1.000 14.30000 ? 21  ARG B O   1 
ATOM   2837 C  CB  . ARG B 1 27  ? 23.75000  1.72700   18.27500 1.000 17.54000 ? 21  ARG B CB  1 
ATOM   2838 C  CG  . ARG B 1 27  ? 22.96500  1.15900   17.11500 1.000 22.29000 ? 21  ARG B CG  1 
ATOM   2839 C  CD  . ARG B 1 27  ? 23.84200  0.28500   16.17600 1.000 26.33000 ? 21  ARG B CD  1 
ATOM   2840 N  NE  . ARG B 1 27  ? 25.17700  0.85800   15.96600 1.000 26.61000 ? 21  ARG B NE  1 
ATOM   2841 C  CZ  . ARG B 1 27  ? 25.44300  1.90500   15.19300 1.000 29.43000 ? 21  ARG B CZ  1 
ATOM   2842 N  NH1 . ARG B 1 27  ? 24.50600  2.48400   14.44600 1.000 25.65000 ? 21  ARG B NH1 1 
ATOM   2843 N  NH2 . ARG B 1 27  ? 26.66800  2.39800   15.19300 1.000 21.26000 ? 21  ARG B NH2 1 
ATOM   2844 N  N   . VAL B 1 28  ? 26.83500  0.97400   19.16700 1.000 17.14000 ? 22  VAL B N   1 
ATOM   2845 C  CA  . VAL B 1 28  ? 28.13500  1.40300   19.68500 1.000 17.00000 ? 22  VAL B CA  1 
ATOM   2846 C  C   . VAL B 1 28  ? 28.76400  2.36000   18.67800 1.000 17.98000 ? 22  VAL B C   1 
ATOM   2847 O  O   . VAL B 1 28  ? 28.77600  2.07500   17.47400 1.000 17.01000 ? 22  VAL B O   1 
ATOM   2848 C  CB  . VAL B 1 28  ? 29.07500  0.19700   19.93600 1.000 16.70000 ? 22  VAL B CB  1 
ATOM   2849 C  CG1 . VAL B 1 28  ? 30.49300  0.65400   20.34400 1.000 17.12000 ? 22  VAL B CG1 1 
ATOM   2850 C  CG2 . VAL B 1 28  ? 28.45800  -0.77500  20.96100 1.000 18.97000 ? 22  VAL B CG2 1 
ATOM   2851 N  N   . HIS B 1 29  ? 29.34300  3.45600   19.17900 1.000 13.92000 ? 23  HIS B N   1 
ATOM   2852 C  CA  . HIS B 1 29  ? 30.20500  4.33300   18.39600 1.000 13.71000 ? 23  HIS B CA  1 
ATOM   2853 C  C   . HIS B 1 29  ? 31.55400  4.39000   19.08200 1.000 14.88000 ? 23  HIS B C   1 
ATOM   2854 O  O   . HIS B 1 29  ? 31.63200  4.49700   20.31200 1.000 16.25000 ? 23  HIS B O   1 
ATOM   2855 C  CB  . HIS B 1 29  ? 29.61500  5.75300   18.27400 1.000 14.27000 ? 23  HIS B CB  1 
ATOM   2856 C  CG  . HIS B 1 29  ? 28.19400  5.76400   17.83200 1.000 14.73000 ? 23  HIS B CG  1 
ATOM   2857 N  ND1 . HIS B 1 29  ? 27.83600  5.57500   16.51200 1.000 16.21000 ? 23  HIS B ND1 1 
ATOM   2858 C  CD2 . HIS B 1 29  ? 27.03200  5.93200   18.51800 1.000 15.96000 ? 23  HIS B CD2 1 
ATOM   2859 C  CE1 . HIS B 1 29  ? 26.51900  5.63400   16.40100 1.000 16.40000 ? 23  HIS B CE1 1 
ATOM   2860 N  NE2 . HIS B 1 29  ? 26.00900  5.87300   17.59800 1.000 16.68000 ? 23  HIS B NE2 1 
ATOM   2861 N  N   . ALA B 1 30  ? 32.61800  4.29900   18.29300 1.000 16.20000 ? 24  ALA B N   1 
ATOM   2862 C  CA  . ALA B 1 30  ? 33.95700  4.35000   18.85100 1.000 12.50000 ? 24  ALA B CA  1 
ATOM   2863 C  C   . ALA B 1 30  ? 34.91100  4.99400   17.85900 1.000 16.68000 ? 24  ALA B C   1 
ATOM   2864 O  O   . ALA B 1 30  ? 34.76100  4.84400   16.64300 1.000 15.29000 ? 24  ALA B O   1 
ATOM   2865 C  CB  . ALA B 1 30  ? 34.44600  2.95000   19.20900 1.000 13.09000 ? 24  ALA B CB  1 
ATOM   2866 N  N   . ALA B 1 31  ? 35.90000  5.72200   18.39400 1.000 15.88000 ? 25  ALA B N   1 
ATOM   2867 C  CA  . ALA B 1 31  ? 36.99700  6.27600   17.60000 1.000 16.92000 ? 25  ALA B CA  1 
ATOM   2868 C  C   . ALA B 1 31  ? 38.32400  5.96600   18.25500 1.000 15.62000 ? 25  ALA B C   1 
ATOM   2869 O  O   . ALA B 1 31  ? 38.45600  6.09200   19.48000 1.000 16.34000 ? 25  ALA B O   1 
ATOM   2870 C  CB  . ALA B 1 31  ? 36.85800  7.79900   17.44500 1.000 14.25000 ? 25  ALA B CB  1 
ATOM   2871 N  N   . VAL B 1 32  ? 39.30600  5.56300   17.44100 1.000 18.24000 ? 26  VAL B N   1 
ATOM   2872 C  CA  . VAL B 1 32  ? 40.68700  5.34800   17.87300 1.000 15.79000 ? 26  VAL B CA  1 
ATOM   2873 C  C   . VAL B 1 32  ? 41.53600  6.26000   17.00100 1.000 19.11000 ? 26  VAL B C   1 
ATOM   2874 O  O   . VAL B 1 32  ? 41.51700  6.13600   15.76800 1.000 19.71000 ? 26  VAL B O   1 
ATOM   2875 C  CB  . VAL B 1 32  ? 41.13400  3.87500   17.72800 1.000 18.69000 ? 26  VAL B CB  1 
ATOM   2876 C  CG1 . VAL B 1 32  ? 42.54400  3.64500   18.27100 1.000 16.22000 ? 26  VAL B CG1 1 
ATOM   2877 C  CG2 . VAL B 1 32  ? 40.14100  2.88800   18.40300 1.000 17.39000 ? 26  VAL B CG2 1 
ATOM   2878 N  N   . VAL B 1 33  ? 42.26100  7.19900   17.62000 1.000 18.43000 ? 27  VAL B N   1 
ATOM   2879 C  CA  . VAL B 1 33  ? 42.92400  8.24800   16.85400 1.000 20.26000 ? 27  VAL B CA  1 
ATOM   2880 C  C   . VAL B 1 33  ? 44.37100  8.33300   17.28400 1.000 21.94000 ? 27  VAL B C   1 
ATOM   2881 O  O   . VAL B 1 33  ? 44.74700  7.88100   18.37000 1.000 19.05000 ? 27  VAL B O   1 
ATOM   2882 C  CB  . VAL B 1 33  ? 42.26600  9.63600   17.00500 1.000 19.25000 ? 27  VAL B CB  1 
ATOM   2883 C  CG1 . VAL B 1 33  ? 40.81100  9.57100   16.65600 1.000 19.07000 ? 27  VAL B CG1 1 
ATOM   2884 C  CG2 . VAL B 1 33  ? 42.45200  10.15500  18.41500 1.000 18.44000 ? 27  VAL B CG2 1 
ATOM   2885 N  N   . ASP B 1 34  ? 45.19600  8.93700   16.42300 1.000 19.65000 ? 28  ASP B N   1 
ATOM   2886 C  CA  . ASP B 1 34  ? 46.57800  9.09500   16.81200 1.000 22.46000 ? 28  ASP B CA  1 
ATOM   2887 C  C   . ASP B 1 34  ? 46.73400  10.46200  17.48500 1.000 23.15000 ? 28  ASP B C   1 
ATOM   2888 O  O   . ASP B 1 34  ? 45.74800  11.16900  17.72900 1.000 23.69000 ? 28  ASP B O   1 
ATOM   2889 C  CB  . ASP B 1 34  ? 47.51400  8.85900   15.61400 1.000 26.00000 ? 28  ASP B CB  1 
ATOM   2890 C  CG  . ASP B 1 34  ? 47.48000  9.98500   14.58100 1.000 32.51000 ? 28  ASP B CG  1 
ATOM   2891 O  OD1 . ASP B 1 34  ? 46.81300  11.02600  14.79000 1.000 27.42000 ? 28  ASP B OD1 1 
ATOM   2892 O  OD2 . ASP B 1 34  ? 48.15800  9.82100   13.54100 1.000 33.81000 ? 28  ASP B OD2 1 
ATOM   2893 N  N   . ALA B 1 35  ? 47.98200  10.81200  17.81500 1.000 26.70000 ? 29  ALA B N   1 
ATOM   2894 C  CA  . ALA B 1 35  ? 48.30400  12.02400  18.57700 1.000 27.43000 ? 29  ALA B CA  1 
ATOM   2895 C  C   . ALA B 1 35  ? 47.92500  13.30500  17.85000 1.000 28.85000 ? 29  ALA B C   1 
ATOM   2896 O  O   . ALA B 1 35  ? 47.79000  14.35000  18.49100 1.000 31.31000 ? 29  ALA B O   1 
ATOM   2897 C  CB  . ALA B 1 35  ? 49.79600  12.05000  18.89700 1.000 30.33000 ? 29  ALA B CB  1 
ATOM   2898 N  N   . LYS B 1 36  ? 47.75700  13.26000  16.53600 1.000 29.90000 ? 30  LYS B N   1 
ATOM   2899 C  CA  . LYS B 1 36  ? 47.26100  14.40300  15.78800 1.000 29.54000 ? 30  LYS B CA  1 
ATOM   2900 C  C   . LYS B 1 36  ? 45.76100  14.33000  15.50900 1.000 28.81000 ? 30  LYS B C   1 
ATOM   2901 O  O   . LYS B 1 36  ? 45.22500  15.23900  14.86800 1.000 29.99000 ? 30  LYS B O   1 
ATOM   2902 C  CB  . LYS B 1 36  ? 48.02700  14.53300  14.46600 1.000 32.11000 ? 30  LYS B CB  1 
ATOM   2903 C  CG  . LYS B 1 36  ? 49.50100  14.81700  14.62900 1.000 36.28000 ? 30  LYS B CG  1 
ATOM   2904 C  CD  . LYS B 1 36  ? 50.17100  15.12300  13.27000 1.000 43.80000 ? 30  LYS B CD  1 
ATOM   2905 C  CE  . LYS B 1 36  ? 51.64100  15.53000  13.43800 1.000 46.84000 ? 30  LYS B CE  1 
ATOM   2906 N  NZ  . LYS B 1 36  ? 51.79800  16.56500  14.51500 1.000 49.80000 ? 30  LYS B NZ  1 
ATOM   2907 N  N   . GLY B 1 37  ? 45.07200  13.27800  15.96600 1.000 28.13000 ? 31  GLY B N   1 
ATOM   2908 C  CA  . GLY B 1 37  ? 43.65100  13.10300  15.73200 1.000 25.79000 ? 31  GLY B CA  1 
ATOM   2909 C  C   . GLY B 1 37  ? 43.29900  12.34300  14.47300 1.000 25.58000 ? 31  GLY B C   1 
ATOM   2910 O  O   . GLY B 1 37  ? 42.10800  12.18400  14.17500 1.000 26.85000 ? 31  GLY B O   1 
ATOM   2911 N  N   . ARG B 1 38  ? 44.29200  11.86800  13.72800 1.000 27.93000 ? 32  ARG B N   1 
ATOM   2912 C  CA  . ARG B 1 38  ? 44.02700  10.99800  12.59100 1.000 25.50000 ? 32  ARG B CA  1 
ATOM   2913 C  C   . ARG B 1 38  ? 43.30600  9.74000   13.03900 1.000 23.13000 ? 32  ARG B C   1 
ATOM   2914 O  O   . ARG B 1 38  ? 43.68400  9.11200   14.02400 1.000 23.38000 ? 32  ARG B O   1 
ATOM   2915 C  CB  . ARG B 1 38  ? 45.33000  10.61500  11.93600 1.000 32.11000 ? 32  ARG B CB  1 
ATOM   2916 C  CG  . ARG B 1 38  ? 45.25700  9.98200   10.55500 1.000 37.95000 ? 32  ARG B CG  1 
ATOM   2917 C  CD  . ARG B 1 38  ? 46.67900  10.14400  9.97200  1.000 47.74000 ? 32  ARG B CD  1 
ATOM   2918 N  NE  . ARG B 1 38  ? 47.34000  11.22900  10.70500 1.000 50.26000 ? 32  ARG B NE  1 
ATOM   2919 C  CZ  . ARG B 1 38  ? 48.64000  11.50800  10.69900 1.000 46.52000 ? 32  ARG B CZ  1 
ATOM   2920 N  NH1 . ARG B 1 38  ? 49.48100  10.89400  9.88000  1.000 51.61000 ? 32  ARG B NH1 1 
ATOM   2921 N  NH2 . ARG B 1 38  ? 49.10900  12.41500  11.55700 1.000 47.09000 ? 32  ARG B NH2 1 
ATOM   2922 N  N   . LEU B 1 39  ? 42.30300  9.34700   12.27000 1.000 22.76000 ? 33  LEU B N   1 
ATOM   2923 C  CA  . LEU B 1 39  ? 41.42100  8.23900   12.62200 1.000 26.79000 ? 33  LEU B CA  1 
ATOM   2924 C  C   . LEU B 1 39  ? 42.04200  6.92400   12.15600 1.000 24.62000 ? 33  LEU B C   1 
ATOM   2925 O  O   . LEU B 1 39  ? 42.25800  6.73300   10.95600 1.000 24.15000 ? 33  LEU B O   1 
ATOM   2926 C  CB  . LEU B 1 39  ? 40.05400  8.45200   11.97900 1.000 26.58000 ? 33  LEU B CB  1 
ATOM   2927 C  CG  . LEU B 1 39  ? 39.04600  7.35400   12.27900 1.000 27.31000 ? 33  LEU B CG  1 
ATOM   2928 C  CD1 . LEU B 1 39  ? 38.63900  7.44600   13.75300 1.000 19.88000 ? 33  LEU B CD1 1 
ATOM   2929 C  CD2 . LEU B 1 39  ? 37.84300  7.46400   11.33900 1.000 25.40000 ? 33  LEU B CD2 1 
ATOM   2930 N  N   . LEU B 1 40  ? 42.33500  6.02400   13.10200 1.000 20.06000 ? 34  LEU B N   1 
ATOM   2931 C  CA  . LEU B 1 40  ? 42.95900  4.73700   12.80600 1.000 23.57000 ? 34  LEU B CA  1 
ATOM   2932 C  C   . LEU B 1 40  ? 41.95800  3.58300   12.75900 1.000 20.65000 ? 34  LEU B C   1 
ATOM   2933 O  O   . LEU B 1 40  ? 42.08400  2.70700   11.90400 1.000 22.82000 ? 34  LEU B O   1 
ATOM   2934 C  CB  . LEU B 1 40  ? 44.04800  4.42300   13.84900 1.000 18.62000 ? 34  LEU B CB  1 
ATOM   2935 C  CG  . LEU B 1 40  ? 45.10700  5.50100   14.13500 1.000 27.61000 ? 34  LEU B CG  1 
ATOM   2936 C  CD1 . LEU B 1 40  ? 45.98600  5.12100   15.32600 1.000 25.31000 ? 34  LEU B CD1 1 
ATOM   2937 C  CD2 . LEU B 1 40  ? 45.99800  5.77600   12.91600 1.000 25.67000 ? 34  LEU B CD2 1 
ATOM   2938 N  N   . TYR B 1 41  ? 40.99400  3.54600   13.68000 1.000 19.55000 ? 35  TYR B N   1 
ATOM   2939 C  CA  . TYR B 1 41  ? 39.99000  2.49600   13.79300 1.000 19.30000 ? 35  TYR B CA  1 
ATOM   2940 C  C   . TYR B 1 41  ? 38.67100  3.12900   14.22100 1.000 18.89000 ? 35  TYR B C   1 
ATOM   2941 O  O   . TYR B 1 41  ? 38.64000  4.21500   14.81000 1.000 19.48000 ? 35  TYR B O   1 
ATOM   2942 C  CB  . TYR B 1 41  ? 40.39900  1.36700   14.80000 1.000 18.96000 ? 35  TYR B CB  1 
ATOM   2943 C  CG  . TYR B 1 41  ? 41.71200  0.73000   14.42500 1.000 20.55000 ? 35  TYR B CG  1 
ATOM   2944 C  CD1 . TYR B 1 41  ? 41.77400  -0.34000  13.52900 1.000 26.98000 ? 35  TYR B CD1 1 
ATOM   2945 C  CD2 . TYR B 1 41  ? 42.90100  1.25000   14.90100 1.000 22.59000 ? 35  TYR B CD2 1 
ATOM   2946 C  CE1 . TYR B 1 41  ? 43.01300  -0.89400  13.14000 1.000 25.82000 ? 35  TYR B CE1 1 
ATOM   2947 C  CE2 . TYR B 1 41  ? 44.12200  0.72700   14.51700 1.000 26.56000 ? 35  TYR B CE2 1 
ATOM   2948 C  CZ  . TYR B 1 41  ? 44.17100  -0.35400  13.63700 1.000 28.93000 ? 35  TYR B CZ  1 
ATOM   2949 O  OH  . TYR B 1 41  ? 45.39800  -0.86400  13.28100 1.000 29.24000 ? 35  TYR B OH  1 
ATOM   2950 N  N   . ALA B 1 42  ? 37.56400  2.44800   13.92000 1.000 17.96000 ? 36  ALA B N   1 
ATOM   2951 C  CA  . ALA B 1 42  ? 36.25100  3.02100   14.20300 1.000 17.12000 ? 36  ALA B CA  1 
ATOM   2952 C  C   . ALA B 1 42  ? 35.23500  1.91000   14.37800 1.000 17.50000 ? 36  ALA B C   1 
ATOM   2953 O  O   . ALA B 1 42  ? 35.39400  0.80600   13.84800 1.000 19.59000 ? 36  ALA B O   1 
ATOM   2954 C  CB  . ALA B 1 42  ? 35.76300  3.94900   13.07900 1.000 18.54000 ? 36  ALA B CB  1 
ATOM   2955 N  N   . LEU B 1 43  ? 34.18800  2.23300   15.12800 1.000 16.81000 ? 37  LEU B N   1 
ATOM   2956 C  CA  . LEU B 1 43  ? 32.93300  1.51100   15.13800 1.000 15.56000 ? 37  LEU B CA  1 
ATOM   2957 C  C   . LEU B 1 43  ? 31.82000  2.52600   14.98100 1.000 18.58000 ? 37  LEU B C   1 
ATOM   2958 O  O   . LEU B 1 43  ? 31.94500  3.68700   15.41400 1.000 17.17000 ? 37  LEU B O   1 
ATOM   2959 C  CB  . LEU B 1 43  ? 32.70800  0.74700   16.45800 1.000 16.34000 ? 37  LEU B CB  1 
ATOM   2960 C  CG  . LEU B 1 43  ? 33.74400  -0.27900  16.89100 1.000 24.10000 ? 37  LEU B CG  1 
ATOM   2961 C  CD1 . LEU B 1 43  ? 33.49400  -0.61700  18.35300 1.000 20.64000 ? 37  LEU B CD1 1 
ATOM   2962 C  CD2 . LEU B 1 43  ? 33.68000  -1.51500  16.01000 1.000 20.58000 ? 37  LEU B CD2 1 
ATOM   2963 N  N   . GLY B 1 44  ? 30.69800  2.07300   14.42100 1.000 19.56000 ? 38  GLY B N   1 
ATOM   2964 C  CA  . GLY B 1 44  ? 29.56700  2.98500   14.31700 1.000 17.94000 ? 38  GLY B CA  1 
ATOM   2965 C  C   . GLY B 1 44  ? 29.93200  4.24900   13.55000 1.000 23.08000 ? 38  GLY B C   1 
ATOM   2966 O  O   . GLY B 1 44  ? 30.58800  4.20700   12.50000 1.000 21.85000 ? 38  GLY B O   1 
ATOM   2967 N  N   . ASN B 1 45  ? 29.51200  5.39500   14.08800 1.000 20.31000 ? 39  ASN B N   1 
ATOM   2968 C  CA  . ASN B 1 45  ? 29.85700  6.70200   13.53100 1.000 19.35000 ? 39  ASN B CA  1 
ATOM   2969 C  C   . ASN B 1 45  ? 30.90500  7.34700   14.41500 1.000 19.66000 ? 39  ASN B C   1 
ATOM   2970 O  O   . ASN B 1 45  ? 30.55700  7.95700   15.43700 1.000 18.11000 ? 39  ASN B O   1 
ATOM   2971 C  CB  . ASN B 1 45  ? 28.61800  7.58800   13.43700 1.000 21.83000 ? 39  ASN B CB  1 
ATOM   2972 C  CG  . ASN B 1 45  ? 28.94000  9.01000   13.00900 1.000 25.27000 ? 39  ASN B CG  1 
ATOM   2973 O  OD1 . ASN B 1 45  ? 30.06200  9.33300   12.60300 1.000 18.36000 ? 39  ASN B OD1 1 
ATOM   2974 N  ND2 . ASN B 1 45  ? 27.94400  9.86500   13.09200 1.000 23.36000 ? 39  ASN B ND2 1 
ATOM   2975 N  N   . PRO B 1 46  ? 32.18900  7.30100   14.04100 1.000 18.36000 ? 40  PRO B N   1 
ATOM   2976 C  CA  . PRO B 1 46  ? 33.23500  7.88100   14.89800 1.000 15.75000 ? 40  PRO B CA  1 
ATOM   2977 C  C   . PRO B 1 46  ? 33.20200  9.41100   14.97500 1.000 18.36000 ? 40  PRO B C   1 
ATOM   2978 O  O   . PRO B 1 46  ? 33.90800  9.98300   15.82200 1.000 19.80000 ? 40  PRO B O   1 
ATOM   2979 C  CB  . PRO B 1 46  ? 34.53400  7.37900   14.24000 1.000 17.46000 ? 40  PRO B CB  1 
ATOM   2980 C  CG  . PRO B 1 46  ? 34.15300  7.27100   12.76100 1.000 18.36000 ? 40  PRO B CG  1 
ATOM   2981 C  CD  . PRO B 1 46  ? 32.73900  6.74100   12.79000 1.000 18.87000 ? 40  PRO B CD  1 
ATOM   2982 N  N   . THR B 1 47  ? 32.43100  10.11600  14.13100 1.000 17.52000 ? 41  THR B N   1 
ATOM   2983 C  CA  . THR B 1 47  ? 32.33900  11.56800  14.25300 1.000 17.58000 ? 41  THR B CA  1 
ATOM   2984 C  C   . THR B 1 47  ? 30.99000  12.03100  14.81300 1.000 18.86000 ? 41  THR B C   1 
ATOM   2985 O  O   . THR B 1 47  ? 30.62600  13.21200  14.65900 1.000 19.71000 ? 41  THR B O   1 
ATOM   2986 C  CB  . THR B 1 47  ? 32.60900  12.26800  12.91700 1.000 21.16000 ? 41  THR B CB  1 
ATOM   2987 O  OG1 . THR B 1 47  ? 31.57600  11.93500  11.98100 1.000 24.13000 ? 41  THR B OG1 1 
ATOM   2988 C  CG2 . THR B 1 47  ? 33.97500  11.90700  12.37200 1.000 17.17000 ? 41  THR B CG2 1 
ATOM   2989 N  N   . ARG B 1 48  ? 30.27000  11.14000  15.48900 1.000 21.33000 ? 42  ARG B N   1 
ATOM   2990 C  CA  . ARG B 1 48  ? 28.98400  11.47100  16.08600 1.000 17.81000 ? 42  ARG B CA  1 
ATOM   2991 C  C   . ARG B 1 48  ? 29.11600  12.66600  17.01300 1.000 20.18000 ? 42  ARG B C   1 
ATOM   2992 O  O   . ARG B 1 48  ? 29.93500  12.64800  17.94200 1.000 15.61000 ? 42  ARG B O   1 
ATOM   2993 C  CB  . ARG B 1 48  ? 28.45500  10.27900  16.87100 1.000 16.03000 ? 42  ARG B CB  1 
ATOM   2994 C  CG  . ARG B 1 48  ? 27.06500  10.48800  17.52400 1.000 16.15000 ? 42  ARG B CG  1 
ATOM   2995 C  CD  . ARG B 1 48  ? 26.85900  9.44300   18.65700 1.000 15.71000 ? 42  ARG B CD  1 
ATOM   2996 N  NE  . ARG B 1 48  ? 25.51300  9.49200   19.24900 1.000 19.11000 ? 42  ARG B NE  1 
ATOM   2997 C  CZ  . ARG B 1 48  ? 25.19500  10.23800  20.30300 1.000 17.48000 ? 42  ARG B CZ  1 
ATOM   2998 N  NH1 . ARG B 1 48  ? 26.06500  11.06500  20.84600 1.000 14.15000 ? 42  ARG B NH1 1 
ATOM   2999 N  NH2 . ARG B 1 48  ? 23.99500  10.10300  20.86300 1.000 17.24000 ? 42  ARG B NH2 1 
ATOM   3000 N  N   . MET B 1 49  ? 28.29000  13.68700  16.77600 1.000 17.53000 ? 43  MET B N   1 
ATOM   3001 C  CA  A MET B 1 49  ? 28.18900  14.80100  17.71600 0.400 18.92000 ? 43  MET B CA  1 
ATOM   3002 C  CA  B MET B 1 49  ? 28.17600  14.80100  17.70900 0.600 19.03000 ? 43  MET B CA  1 
ATOM   3003 C  C   . MET B 1 49  ? 27.76300  14.27500  19.07800 1.000 16.93000 ? 43  MET B C   1 
ATOM   3004 O  O   . MET B 1 49  ? 26.67900  13.72000  19.21900 1.000 15.88000 ? 43  MET B O   1 
ATOM   3005 C  CB  A MET B 1 49  ? 27.18800  15.84200  17.21300 0.400 20.28000 ? 43  MET B CB  1 
ATOM   3006 C  CB  B MET B 1 49  ? 27.14500  15.79700  17.18000 0.600 20.32000 ? 43  MET B CB  1 
ATOM   3007 C  CG  A MET B 1 49  ? 26.86500  16.94100  18.23400 0.400 21.68000 ? 43  MET B CG  1 
ATOM   3008 C  CG  B MET B 1 49  ? 27.28600  17.20900  17.71700 0.600 22.42000 ? 43  MET B CG  1 
ATOM   3009 S  SD  A MET B 1 49  ? 28.31300  17.91000  18.72200 0.400 20.92000 ? 43  MET B SD  1 
ATOM   3010 S  SD  B MET B 1 49  ? 28.92900  17.92600  17.44000 0.600 23.22000 ? 43  MET B SD  1 
ATOM   3011 C  CE  A MET B 1 49  ? 28.39900  19.10500  17.39100 0.400 22.66000 ? 43  MET B CE  1 
ATOM   3012 C  CE  B MET B 1 49  ? 28.66400  19.50700  18.21500 0.600 21.69000 ? 43  MET B CE  1 
ATOM   3013 N  N   . THR B 1 50  ? 28.63600  14.43800  20.08500 1.000 18.43000 ? 44  THR B N   1 
ATOM   3014 C  CA  . THR B 1 50  ? 28.45100  13.76400  21.37700 1.000 15.92000 ? 44  THR B CA  1 
ATOM   3015 C  C   . THR B 1 50  ? 28.74400  14.70100  22.54100 1.000 19.40000 ? 44  THR B C   1 
ATOM   3016 O  O   . THR B 1 50  ? 29.80500  15.33800  22.58900 1.000 17.85000 ? 44  THR B O   1 
ATOM   3017 C  CB  . THR B 1 50  ? 29.35400  12.52000  21.47500 1.000 15.77000 ? 44  THR B CB  1 
ATOM   3018 O  OG1 . THR B 1 50  ? 29.03400  11.62500  20.39500 1.000 14.61000 ? 44  THR B OG1 1 
ATOM   3019 C  CG2 . THR B 1 50  ? 29.14000  11.74400  22.82600 1.000 14.81000 ? 44  THR B CG2 1 
ATOM   3020 N  N   . LEU B 1 51  ? 27.81900  14.75000  23.49700 1.000 15.35000 ? 45  LEU B N   1 
ATOM   3021 C  CA  . LEU B 1 51  ? 28.07300  15.40100  24.77900 1.000 16.89000 ? 45  LEU B CA  1 
ATOM   3022 C  C   . LEU B 1 51  ? 29.12400  14.61700  25.55800 1.000 18.52000 ? 45  LEU B C   1 
ATOM   3023 O  O   . LEU B 1 51  ? 28.88100  13.49100  26.00300 1.000 18.96000 ? 45  LEU B O   1 
ATOM   3024 C  CB  . LEU B 1 51  ? 26.77300  15.49500  25.57300 1.000 15.16000 ? 45  LEU B CB  1 
ATOM   3025 C  CG  . LEU B 1 51  ? 25.78800  16.49500  24.96800 1.000 19.95000 ? 45  LEU B CG  1 
ATOM   3026 C  CD1 . LEU B 1 51  ? 24.35000  16.09000  25.30500 1.000 21.15000 ? 45  LEU B CD1 1 
ATOM   3027 C  CD2 . LEU B 1 51  ? 26.08900  17.83900  25.49000 1.000 17.53000 ? 45  LEU B CD2 1 
ATOM   3028 N  N   . ALA B 1 52  ? 30.30700  15.20800  25.71900 1.000 17.32000 ? 46  ALA B N   1 
ATOM   3029 C  CA  . ALA B 1 52  ? 31.39200  14.55900  26.44200 1.000 18.17000 ? 46  ALA B CA  1 
ATOM   3030 C  C   . ALA B 1 52  ? 31.08100  14.37000  27.92600 1.000 18.12000 ? 46  ALA B C   1 
ATOM   3031 O  O   . ALA B 1 52  ? 31.60000  13.43700  28.55600 1.000 19.71000 ? 46  ALA B O   1 
ATOM   3032 C  CB  . ALA B 1 52  ? 32.66500  15.41000  26.27600 1.000 17.92000 ? 46  ALA B CB  1 
ATOM   3033 N  N   . ARG B 1 53  ? 30.30900  15.27000  28.51900 1.000 19.03000 ? 47  ARG B N   1 
ATOM   3034 C  CA  . ARG B 1 53  ? 29.94100  15.15800  29.94600 1.000 19.71000 ? 47  ARG B CA  1 
ATOM   3035 C  C   . ARG B 1 53  ? 31.25400  15.11200  30.74000 1.000 21.21000 ? 47  ARG B C   1 
ATOM   3036 O  O   . ARG B 1 53  ? 32.21500  15.83000  30.41600 1.000 20.38000 ? 47  ARG B O   1 
ATOM   3037 C  CB  . ARG B 1 53  ? 28.99400  14.01700  30.14200 1.000 18.79000 ? 47  ARG B CB  1 
ATOM   3038 C  CG  . ARG B 1 53  ? 27.71500  14.14600  29.34000 1.000 20.93000 ? 47  ARG B CG  1 
ATOM   3039 C  CD  . ARG B 1 53  ? 26.81900  15.36000  29.75100 1.000 19.90000 ? 47  ARG B CD  1 
ATOM   3040 N  NE  . ARG B 1 53  ? 26.29000  15.23300  31.11400 1.000 23.78000 ? 47  ARG B NE  1 
ATOM   3041 C  CZ  . ARG B 1 53  ? 25.32600  14.39800  31.48200 1.000 23.78000 ? 47  ARG B CZ  1 
ATOM   3042 N  NH1 . ARG B 1 53  ? 24.71400  13.60100  30.60700 1.000 20.86000 ? 47  ARG B NH1 1 
ATOM   3043 N  NH2 . ARG B 1 53  ? 24.95800  14.35100  32.76100 1.000 24.75000 ? 47  ARG B NH2 1 
ATOM   3044 N  N   . SER B 1 54  ? 31.37300  14.30600  31.78700 1.000 20.75000 ? 48  SER B N   1 
ATOM   3045 C  CA  . SER B 1 54  ? 32.60300  14.41900  32.55600 1.000 20.68000 ? 48  SER B CA  1 
ATOM   3046 C  C   . SER B 1 54  ? 33.82900  13.85200  31.85100 1.000 22.75000 ? 48  SER B C   1 
ATOM   3047 O  O   . SER B 1 54  ? 34.92700  14.01100  32.37700 1.000 20.65000 ? 48  SER B O   1 
ATOM   3048 C  CB  . SER B 1 54  ? 32.43000  13.74700  33.89800 1.000 25.01000 ? 48  SER B CB  1 
ATOM   3049 O  OG  . SER B 1 54  ? 31.69000  14.61300  34.73600 1.000 30.13000 ? 48  SER B OG  1 
ATOM   3050 N  N   . ALA B 1 55  ? 33.68800  13.18300  30.70200 1.000 20.26000 ? 49  ALA B N   1 
ATOM   3051 C  CA  . ALA B 1 55  ? 34.90600  12.88200  29.95400 1.000 20.43000 ? 49  ALA B CA  1 
ATOM   3052 C  C   . ALA B 1 55  ? 35.60200  14.14200  29.46500 1.000 21.37000 ? 49  ALA B C   1 
ATOM   3053 O  O   . ALA B 1 55  ? 36.79000  14.07700  29.10300 1.000 19.49000 ? 49  ALA B O   1 
ATOM   3054 C  CB  . ALA B 1 55  ? 34.58000  11.91800  28.79900 1.000 17.62000 ? 49  ALA B CB  1 
ATOM   3055 N  N   . ALA B 1 56  ? 34.93700  15.30100  29.52200 1.000 20.17000 ? 50  ALA B N   1 
ATOM   3056 C  CA  . ALA B 1 56  ? 35.58400  16.58300  29.24900 1.000 22.29000 ? 50  ALA B CA  1 
ATOM   3057 C  C   . ALA B 1 56  ? 36.27900  17.21800  30.46100 1.000 22.27000 ? 50  ALA B C   1 
ATOM   3058 O  O   . ALA B 1 56  ? 37.05000  18.16400  30.27300 1.000 21.60000 ? 50  ALA B O   1 
ATOM   3059 C  CB  . ALA B 1 56  ? 34.56900  17.58600  28.67600 1.000 19.05000 ? 50  ALA B CB  1 
ATOM   3060 N  N   . LYS B 1 57  ? 36.04300  16.74200  31.68600 1.000 21.63000 ? 51  LYS B N   1 
ATOM   3061 C  CA  . LYS B 1 57  ? 36.64000  17.37900  32.86800 1.000 25.20000 ? 51  LYS B CA  1 
ATOM   3062 C  C   . LYS B 1 57  ? 38.15700  17.54700  32.83500 1.000 24.26000 ? 51  LYS B C   1 
ATOM   3063 O  O   . LYS B 1 57  ? 38.63300  18.59900  33.29100 1.000 25.87000 ? 51  LYS B O   1 
ATOM   3064 C  CB  . LYS B 1 57  ? 36.26100  16.62600  34.15600 1.000 25.81000 ? 51  LYS B CB  1 
ATOM   3065 C  CG  . LYS B 1 57  ? 34.79400  16.71100  34.55100 1.000 26.44000 ? 51  LYS B CG  1 
ATOM   3066 C  CD  . LYS B 1 57  ? 34.45100  18.01400  35.21700 1.000 31.74000 ? 51  LYS B CD  1 
ATOM   3067 C  CE  . LYS B 1 57  ? 33.03800  17.98900  35.79400 1.000 38.10000 ? 51  LYS B CE  1 
ATOM   3068 N  NZ  . LYS B 1 57  ? 32.01900  18.50500  34.80200 1.000 40.66000 ? 51  LYS B NZ  1 
ATOM   3069 N  N   . PRO B 1 58  ? 38.96700  16.58600  32.37800 1.000 21.99000 ? 52  PRO B N   1 
ATOM   3070 C  CA  . PRO B 1 58  ? 40.41600  16.85500  32.26400 1.000 24.75000 ? 52  PRO B CA  1 
ATOM   3071 C  C   . PRO B 1 58  ? 40.75600  18.01300  31.32400 1.000 23.04000 ? 52  PRO B C   1 
ATOM   3072 O  O   . PRO B 1 58  ? 41.70700  18.75100  31.60200 1.000 22.72000 ? 52  PRO B O   1 
ATOM   3073 C  CB  . PRO B 1 58  ? 40.97500  15.51000  31.76900 1.000 21.72000 ? 52  PRO B CB  1 
ATOM   3074 C  CG  . PRO B 1 58  ? 39.99200  14.50900  32.31500 1.000 22.67000 ? 52  PRO B CG  1 
ATOM   3075 C  CD  . PRO B 1 58  ? 38.65600  15.16100  32.11700 1.000 21.77000 ? 52  PRO B CD  1 
ATOM   3076 N  N   . ALA B 1 59  ? 39.98600  18.23300  30.24300 1.000 21.88000 ? 53  ALA B N   1 
ATOM   3077 C  CA  . ALA B 1 59  ? 40.21400  19.41600  29.40900 1.000 23.47000 ? 53  ALA B CA  1 
ATOM   3078 C  C   . ALA B 1 59  ? 39.77800  20.68700  30.12000 1.000 25.05000 ? 53  ALA B C   1 
ATOM   3079 O  O   . ALA B 1 59  ? 40.43400  21.72600  30.00800 1.000 27.95000 ? 53  ALA B O   1 
ATOM   3080 C  CB  . ALA B 1 59  ? 39.47300  19.29800  28.06900 1.000 26.70000 ? 53  ALA B CB  1 
ATOM   3081 N  N   . GLN B 1 60  ? 38.65400  20.64200  30.83300 1.000 24.02000 ? 54  GLN B N   1 
ATOM   3082 C  CA  . GLN B 1 60  ? 38.27400  21.80800  31.61600 1.000 22.38000 ? 54  GLN B CA  1 
ATOM   3083 C  C   . GLN B 1 60  ? 39.28600  22.07000  32.71900 1.000 25.42000 ? 54  GLN B C   1 
ATOM   3084 O  O   . GLN B 1 60  ? 39.55300  23.22500  33.05700 1.000 24.69000 ? 54  GLN B O   1 
ATOM   3085 C  CB  . GLN B 1 60  ? 36.86500  21.60800  32.17700 1.000 27.07000 ? 54  GLN B CB  1 
ATOM   3086 C  CG  . GLN B 1 60  ? 35.84400  21.40900  31.09200 1.000 26.74000 ? 54  GLN B CG  1 
ATOM   3087 C  CD  . GLN B 1 60  ? 34.42300  21.16900  31.59400 1.000 30.53000 ? 54  GLN B CD  1 
ATOM   3088 O  OE1 . GLN B 1 60  ? 33.60600  20.63000  30.87000 1.000 38.30000 ? 54  GLN B OE1 1 
ATOM   3089 N  NE2 . GLN B 1 60  ? 34.11900  21.59400  32.80700 1.000 34.37000 ? 54  GLN B NE2 1 
ATOM   3090 N  N   . ALA B 1 61  ? 39.88900  21.01700  33.27100 1.000 23.35000 ? 55  ALA B N   1 
ATOM   3091 C  CA  . ALA B 1 61  ? 40.87600  21.19900  34.32800 1.000 25.50000 ? 55  ALA B CA  1 
ATOM   3092 C  C   . ALA B 1 61  ? 42.13900  21.86300  33.80300 1.000 22.17000 ? 55  ALA B C   1 
ATOM   3093 O  O   . ALA B 1 61  ? 42.83700  22.55100  34.56000 1.000 24.53000 ? 55  ALA B O   1 
ATOM   3094 C  CB  . ALA B 1 61  ? 41.21100  19.84600  34.96200 1.000 25.21000 ? 55  ALA B CB  1 
ATOM   3095 N  N   . LEU B 1 62  ? 42.46900  21.65700  32.52000 1.000 22.27000 ? 56  LEU B N   1 
ATOM   3096 C  CA  . LEU B 1 62  ? 43.62500  22.34600  31.95300 1.000 22.57000 ? 56  LEU B CA  1 
ATOM   3097 C  C   . LEU B 1 62  ? 43.40500  23.84300  31.92900 1.000 23.77000 ? 56  LEU B C   1 
ATOM   3098 O  O   . LEU B 1 62  ? 44.35600  24.60700  32.07800 1.000 22.40000 ? 56  LEU B O   1 
ATOM   3099 C  CB  . LEU B 1 62  ? 43.89800  21.86700  30.52900 1.000 19.84000 ? 56  LEU B CB  1 
ATOM   3100 C  CG  . LEU B 1 62  ? 44.96300  22.60900  29.73000 1.000 23.57000 ? 56  LEU B CG  1 
ATOM   3101 C  CD1 . LEU B 1 62  ? 46.28900  22.32700  30.34100 1.000 24.09000 ? 56  LEU B CD1 1 
ATOM   3102 C  CD2 . LEU B 1 62  ? 44.93400  22.16600  28.26700 1.000 24.46000 ? 56  LEU B CD2 1 
ATOM   3103 N  N   . ALA B 1 63  ? 42.16200  24.27700  31.71900 1.000 21.41000 ? 57  ALA B N   1 
ATOM   3104 C  CA  . ALA B 1 63  ? 41.87000  25.70400  31.79800 1.000 19.98000 ? 57  ALA B CA  1 
ATOM   3105 C  C   . ALA B 1 63  ? 42.14600  26.23800  33.19500 1.000 22.06000 ? 57  ALA B C   1 
ATOM   3106 O  O   . ALA B 1 63  ? 42.75700  27.30900  33.35500 1.000 24.14000 ? 57  ALA B O   1 
ATOM   3107 C  CB  . ALA B 1 63  ? 40.42100  25.96600  31.38100 1.000 21.00000 ? 57  ALA B CB  1 
ATOM   3108 N  N   . ILE B 1 64  ? 41.72300  25.50200  34.22200 1.000 20.63000 ? 58  ILE B N   1 
ATOM   3109 C  CA  . ILE B 1 64  ? 42.05000  25.87800  35.59600 1.000 22.25000 ? 58  ILE B CA  1 
ATOM   3110 C  C   . ILE B 1 64  ? 43.55600  25.95200  35.79800 1.000 24.54000 ? 58  ILE B C   1 
ATOM   3111 O  O   . ILE B 1 64  ? 44.07900  26.94800  36.32300 1.000 24.01000 ? 58  ILE B O   1 
ATOM   3112 C  CB  . ILE B 1 64  ? 41.42800  24.88000  36.58800 1.000 25.25000 ? 58  ILE B CB  1 
ATOM   3113 C  CG1 . ILE B 1 64  ? 39.90500  24.88200  36.48000 1.000 22.61000 ? 58  ILE B CG1 1 
ATOM   3114 C  CG2 . ILE B 1 64  ? 41.91300  25.20000  38.01100 1.000 25.16000 ? 58  ILE B CG2 1 
ATOM   3115 C  CD1 . ILE B 1 64  ? 39.25900  23.59200  37.09400 1.000 26.07000 ? 58  ILE B CD1 1 
ATOM   3116 N  N   . LEU B 1 65  ? 44.28600  24.89300  35.40600 1.000 20.90000 ? 59  LEU B N   1 
ATOM   3117 C  CA  . LEU B 1 65  ? 45.73000  24.86600  35.66700 1.000 26.61000 ? 59  LEU B CA  1 
ATOM   3118 C  C   . LEU B 1 65  ? 46.50300  25.92200  34.88600 1.000 24.69000 ? 59  LEU B C   1 
ATOM   3119 O  O   . LEU B 1 65  ? 47.60700  26.29200  35.29100 1.000 25.11000 ? 59  LEU B O   1 
ATOM   3120 C  CB  . LEU B 1 65  ? 46.32100  23.48700  35.34600 1.000 25.12000 ? 59  LEU B CB  1 
ATOM   3121 C  CG  . LEU B 1 65  ? 45.94900  22.27900  36.18800 1.000 28.29000 ? 59  LEU B CG  1 
ATOM   3122 C  CD1 . LEU B 1 65  ? 46.74800  21.09300  35.65800 1.000 26.97000 ? 59  LEU B CD1 1 
ATOM   3123 C  CD2 . LEU B 1 65  ? 46.24400  22.49300  37.66200 1.000 27.35000 ? 59  LEU B CD2 1 
ATOM   3124 N  N   . GLU B 1 66  ? 45.97100  26.40900  33.78100 1.000 22.04000 ? 60  GLU B N   1 
ATOM   3125 C  CA  . GLU B 1 66  ? 46.62500  27.45600  33.03400 1.000 22.90000 ? 60  GLU B CA  1 
ATOM   3126 C  C   . GLU B 1 66  ? 46.17800  28.84100  33.46200 1.000 26.27000 ? 60  GLU B C   1 
ATOM   3127 O  O   . GLU B 1 66  ? 46.56400  29.82700  32.82200 1.000 27.38000 ? 60  GLU B O   1 
ATOM   3128 C  CB  . GLU B 1 66  ? 46.36900  27.28700  31.54100 1.000 26.07000 ? 60  GLU B CB  1 
ATOM   3129 C  CG  . GLU B 1 66  ? 46.96400  26.02300  30.94900 1.000 26.52000 ? 60  GLU B CG  1 
ATOM   3130 C  CD  . GLU B 1 66  ? 46.87700  26.03000  29.44300 1.000 26.85000 ? 60  GLU B CD  1 
ATOM   3131 O  OE1 . GLU B 1 66  ? 45.84800  26.48500  28.89700 1.000 32.49000 ? 60  GLU B OE1 1 
ATOM   3132 O  OE2 . GLU B 1 66  ? 47.84700  25.60400  28.79400 1.000 30.64000 ? 60  GLU B OE2 1 
ATOM   3133 N  N   . THR B 1 67  ? 45.37000  28.94600  34.51600 1.000 22.05000 ? 61  THR B N   1 
ATOM   3134 C  CA  . THR B 1 67  ? 44.94400  30.25300  34.99000 1.000 24.62000 ? 61  THR B CA  1 
ATOM   3135 C  C   . THR B 1 67  ? 46.03700  30.81900  35.88600 1.000 30.08000 ? 61  THR B C   1 
ATOM   3136 O  O   . THR B 1 67  ? 46.44600  30.17100  36.86100 1.000 25.30000 ? 61  THR B O   1 
ATOM   3137 C  CB  . THR B 1 67  ? 43.62000  30.18200  35.74300 1.000 23.99000 ? 61  THR B CB  1 
ATOM   3138 O  OG1 . THR B 1 67  ? 42.59400  29.68100  34.87900 1.000 23.95000 ? 61  THR B OG1 1 
ATOM   3139 C  CG2 . THR B 1 67  ? 43.25000  31.57400  36.17300 1.000 22.20000 ? 61  THR B CG2 1 
ATOM   3140 N  N   . GLU B 1 68  ? 46.51700  32.01400  35.52400 1.000 24.62000 ? 62  GLU B N   1 
ATOM   3141 C  CA  . GLU B 1 68  ? 47.57900  32.71000  36.23600 1.000 20.42000 ? 62  GLU B CA  1 
ATOM   3142 C  C   . GLU B 1 68  ? 47.18500  32.89800  37.69300 1.000 30.74000 ? 62  GLU B C   1 
ATOM   3143 O  O   . GLU B 1 68  ? 46.12100  33.45800  37.99100 1.000 25.69000 ? 62  GLU B O   1 
ATOM   3144 C  CB  . GLU B 1 68  ? 47.83400  34.06700  35.57500 1.000 22.15000 ? 62  GLU B CB  1 
ATOM   3145 C  CG  . GLU B 1 68  ? 48.25500  34.00000  34.08500 1.000 23.06000 ? 62  GLU B CG  1 
ATOM   3146 C  CD  . GLU B 1 68  ? 47.09800  33.93800  33.08200 1.000 25.45000 ? 62  GLU B CD  1 
ATOM   3147 O  OE1 . GLU B 1 68  ? 45.95100  33.57400  33.47900 1.000 26.21000 ? 62  GLU B OE1 1 
ATOM   3148 O  OE2 . GLU B 1 68  ? 47.34800  34.22000  31.86500 1.000 23.89000 ? 62  GLU B OE2 1 
ATOM   3149 N  N   . GLY B 1 69  ? 48.02700  32.41100  38.60600 1.000 25.54000 ? 63  GLY B N   1 
ATOM   3150 C  CA  . GLY B 1 69  ? 47.81600  32.56300  40.02400 1.000 28.78000 ? 63  GLY B CA  1 
ATOM   3151 C  C   . GLY B 1 69  ? 47.41400  31.28100  40.72600 1.000 30.17000 ? 63  GLY B C   1 
ATOM   3152 O  O   . GLY B 1 69  ? 47.69700  31.13100  41.92000 1.000 32.42000 ? 63  GLY B O   1 
ATOM   3153 N  N   . VAL B 1 70  ? 46.74700  30.36300  40.01900 1.000 27.68000 ? 64  VAL B N   1 
ATOM   3154 C  CA  . VAL B 1 70  ? 46.24300  29.13400  40.63400 1.000 30.75000 ? 64  VAL B CA  1 
ATOM   3155 C  C   . VAL B 1 70  ? 47.37200  28.32000  41.25300 1.000 27.86000 ? 64  VAL B C   1 
ATOM   3156 O  O   . VAL B 1 70  ? 47.18800  27.66700  42.28800 1.000 32.91000 ? 64  VAL B O   1 
ATOM   3157 C  CB  . VAL B 1 70  ? 45.47200  28.30800  39.59400 1.000 27.23000 ? 64  VAL B CB  1 
ATOM   3158 C  CG1 . VAL B 1 70  ? 45.22100  26.86600  40.11300 1.000 26.51000 ? 64  VAL B CG1 1 
ATOM   3159 C  CG2 . VAL B 1 70  ? 44.17200  29.02500  39.24900 1.000 26.98000 ? 64  VAL B CG2 1 
ATOM   3160 N  N   . ALA B 1 71  ? 48.54900  28.33400  40.62900 1.000 30.92000 ? 65  ALA B N   1 
ATOM   3161 C  CA  . ALA B 1 71  ? 49.67800  27.57200  41.14900 1.000 30.92000 ? 65  ALA B CA  1 
ATOM   3162 C  C   . ALA B 1 71  ? 49.99400  27.95500  42.58900 1.000 32.53000 ? 65  ALA B C   1 
ATOM   3163 O  O   . ALA B 1 71  ? 50.48700  27.11700  43.34900 1.000 31.35000 ? 65  ALA B O   1 
ATOM   3164 C  CB  . ALA B 1 71  ? 50.91400  27.78200  40.26900 1.000 27.40000 ? 65  ALA B CB  1 
ATOM   3165 N  N   . GLY B 1 72  ? 49.71100  29.20600  42.98200 1.000 29.21000 ? 66  GLY B N   1 
ATOM   3166 C  CA  . GLY B 1 72  ? 50.02000  29.67200  44.32800 1.000 33.18000 ? 66  GLY B CA  1 
ATOM   3167 C  C   . GLY B 1 72  ? 49.27600  28.95100  45.43800 1.000 34.43000 ? 66  GLY B C   1 
ATOM   3168 O  O   . GLY B 1 72  ? 49.73900  28.94500  46.57900 1.000 35.54000 ? 66  GLY B O   1 
ATOM   3169 N  N   . TYR B 1 73  ? 48.13500  28.33300  45.13200 1.000 36.23000 ? 67  TYR B N   1 
ATOM   3170 C  CA  . TYR B 1 73  ? 47.32700  27.69600  46.17300 1.000 35.30000 ? 67  TYR B CA  1 
ATOM   3171 C  C   . TYR B 1 73  ? 47.91900  26.39900  46.69800 1.000 30.72000 ? 67  TYR B C   1 
ATOM   3172 O  O   . TYR B 1 73  ? 47.43700  25.88900  47.71200 1.000 32.45000 ? 67  TYR B O   1 
ATOM   3173 C  CB  . TYR B 1 73  ? 45.93500  27.39900  45.64100 1.000 31.69000 ? 67  TYR B CB  1 
ATOM   3174 C  CG  . TYR B 1 73  ? 45.17200  28.64400  45.35300 1.000 33.26000 ? 67  TYR B CG  1 
ATOM   3175 C  CD1 . TYR B 1 73  ? 44.95000  29.57500  46.35400 1.000 34.04000 ? 67  TYR B CD1 1 
ATOM   3176 C  CD2 . TYR B 1 73  ? 44.68100  28.90200  44.08200 1.000 30.38000 ? 67  TYR B CD2 1 
ATOM   3177 C  CE1 . TYR B 1 73  ? 44.25400  30.73800  46.09500 1.000 39.80000 ? 67  TYR B CE1 1 
ATOM   3178 C  CE2 . TYR B 1 73  ? 43.96900  30.05800  43.81400 1.000 30.92000 ? 67  TYR B CE2 1 
ATOM   3179 C  CZ  . TYR B 1 73  ? 43.75700  30.96800  44.82000 1.000 37.08000 ? 67  TYR B CZ  1 
ATOM   3180 O  OH  . TYR B 1 73  ? 43.06000  32.13000  44.56200 1.000 41.81000 ? 67  TYR B OH  1 
ATOM   3181 N  N   . GLY B 1 74  ? 48.88200  25.81300  45.99600 1.000 33.61000 ? 68  GLY B N   1 
ATOM   3182 C  CA  . GLY B 1 74  ? 49.46800  24.56400  46.44400 1.000 31.59000 ? 68  GLY B CA  1 
ATOM   3183 C  C   . GLY B 1 74  ? 48.61700  23.33500  46.26000 1.000 31.18000 ? 68  GLY B C   1 
ATOM   3184 O  O   . GLY B 1 74  ? 48.71500  22.39500  47.06100 1.000 32.62000 ? 68  GLY B O   1 
ATOM   3185 N  N   . PHE B 1 75  ? 47.77500  23.30100  45.23600 1.000 30.69000 ? 69  PHE B N   1 
ATOM   3186 C  CA  . PHE B 1 75  ? 47.05100  22.07400  44.94700 1.000 32.96000 ? 69  PHE B CA  1 
ATOM   3187 C  C   . PHE B 1 75  ? 48.06400  20.98600  44.61700 1.000 33.00000 ? 69  PHE B C   1 
ATOM   3188 O  O   . PHE B 1 75  ? 49.01600  21.22900  43.87300 1.000 29.99000 ? 69  PHE B O   1 
ATOM   3189 C  CB  . PHE B 1 75  ? 46.08800  22.28500  43.77700 1.000 28.88000 ? 69  PHE B CB  1 
ATOM   3190 C  CG  . PHE B 1 75  ? 44.89700  23.15100  44.10200 1.000 28.49000 ? 69  PHE B CG  1 
ATOM   3191 C  CD1 . PHE B 1 75  ? 44.14600  22.92500  45.24700 1.000 26.89000 ? 69  PHE B CD1 1 
ATOM   3192 C  CD2 . PHE B 1 75  ? 44.53500  24.20600  43.25100 1.000 29.48000 ? 69  PHE B CD2 1 
ATOM   3193 C  CE1 . PHE B 1 75  ? 43.03800  23.72500  45.53900 1.000 28.33000 ? 69  PHE B CE1 1 
ATOM   3194 C  CE2 . PHE B 1 75  ? 43.42400  25.01200  43.52300 1.000 31.35000 ? 69  PHE B CE2 1 
ATOM   3195 C  CZ  . PHE B 1 75  ? 42.66800  24.76900  44.67800 1.000 31.54000 ? 69  PHE B CZ  1 
ATOM   3196 N  N   . ASP B 1 76  ? 47.89200  19.80400  45.20700 1.000 28.86000 ? 70  ASP B N   1 
ATOM   3197 C  CA  . ASP B 1 76  ? 48.78000  18.68200  44.94900 1.000 31.06000 ? 70  ASP B CA  1 
ATOM   3198 C  C   . ASP B 1 76  ? 48.13700  17.72800  43.93400 1.000 32.07000 ? 70  ASP B C   1 
ATOM   3199 O  O   . ASP B 1 76  ? 47.02800  17.95700  43.43500 1.000 28.77000 ? 70  ASP B O   1 
ATOM   3200 C  CB  . ASP B 1 76  ? 49.15400  17.97100  46.25900 1.000 31.45000 ? 70  ASP B CB  1 
ATOM   3201 C  CG  . ASP B 1 76  ? 47.95400  17.33800  46.97800 1.000 37.46000 ? 70  ASP B CG  1 
ATOM   3202 O  OD1 . ASP B 1 76  ? 46.90600  17.04400  46.34300 1.000 30.49000 ? 70  ASP B OD1 1 
ATOM   3203 O  OD2 . ASP B 1 76  ? 48.05900  17.12900  48.21800 1.000 42.09000 ? 70  ASP B OD2 1 
ATOM   3204 N  N   . ASP B 1 77  ? 48.84100  16.63100  43.63300 1.000 30.51000 ? 71  ASP B N   1 
ATOM   3205 C  CA  . ASP B 1 77  ? 48.40500  15.75300  42.55400 1.000 29.56000 ? 71  ASP B CA  1 
ATOM   3206 C  C   . ASP B 1 77  ? 47.03700  15.16800  42.84400 1.000 27.70000 ? 71  ASP B C   1 
ATOM   3207 O  O   . ASP B 1 77  ? 46.22000  15.01700  41.93300 1.000 23.93000 ? 71  ASP B O   1 
ATOM   3208 C  CB  . ASP B 1 77  ? 49.41900  14.62800  42.31900 1.000 30.58000 ? 71  ASP B CB  1 
ATOM   3209 C  CG  . ASP B 1 77  ? 50.59400  15.06500  41.44500 1.000 38.63000 ? 71  ASP B CG  1 
ATOM   3210 O  OD1 . ASP B 1 77  ? 50.63400  16.23600  41.02100 1.000 37.98000 ? 71  ASP B OD1 1 
ATOM   3211 O  OD2 . ASP B 1 77  ? 51.47700  14.22900  41.17000 1.000 43.60000 ? 71  ASP B OD2 1 
ATOM   3212 N  N   . ALA B 1 78  ? 46.76800  14.82400  44.09900 1.000 29.14000 ? 72  ALA B N   1 
ATOM   3213 C  CA  . ALA B 1 78  ? 45.47100  14.25800  44.42200 1.000 24.89000 ? 72  ALA B CA  1 
ATOM   3214 C  C   . ALA B 1 78  ? 44.37500  15.29600  44.24400 1.000 26.81000 ? 72  ALA B C   1 
ATOM   3215 O  O   . ALA B 1 78  ? 43.26500  14.95200  43.81600 1.000 23.57000 ? 72  ALA B O   1 
ATOM   3216 C  CB  . ALA B 1 78  ? 45.47400  13.72100  45.84400 1.000 25.34000 ? 72  ALA B CB  1 
ATOM   3217 N  N   . ASP B 1 79  ? 44.65700  16.55900  44.60300 1.000 26.40000 ? 73  ASP B N   1 
ATOM   3218 C  CA  . ASP B 1 79  ? 43.69500  17.63800  44.37800 1.000 29.49000 ? 73  ASP B CA  1 
ATOM   3219 C  C   . ASP B 1 79  ? 43.35200  17.74800  42.89800 1.000 27.45000 ? 73  ASP B C   1 
ATOM   3220 O  O   . ASP B 1 79  ? 42.18300  17.93400  42.53700 1.000 23.51000 ? 73  ASP B O   1 
ATOM   3221 C  CB  . ASP B 1 79  ? 44.22900  19.00100  44.85300 1.000 28.21000 ? 73  ASP B CB  1 
ATOM   3222 C  CG  . ASP B 1 79  ? 44.46700  19.09000  46.35200 1.000 32.73000 ? 73  ASP B CG  1 
ATOM   3223 O  OD1 . ASP B 1 79  ? 43.79600  18.38500  47.13600 1.000 31.92000 ? 73  ASP B OD1 1 
ATOM   3224 O  OD2 . ASP B 1 79  ? 45.33100  19.90500  46.75200 1.000 32.69000 ? 73  ASP B OD2 1 
ATOM   3225 N  N   . ILE B 1 80  ? 44.37000  17.65000  42.03000 1.000 29.34000 ? 74  ILE B N   1 
ATOM   3226 C  CA  . ILE B 1 80  ? 44.16900  17.78600  40.58800 1.000 25.50000 ? 74  ILE B CA  1 
ATOM   3227 C  C   . ILE B 1 80  ? 43.39800  16.58600  40.02700 1.000 25.91000 ? 74  ILE B C   1 
ATOM   3228 O  O   . ILE B 1 80  ? 42.51200  16.74800  39.16300 1.000 22.97000 ? 74  ILE B O   1 
ATOM   3229 C  CB  . ILE B 1 80  ? 45.53100  18.00100  39.90000 1.000 23.25000 ? 74  ILE B CB  1 
ATOM   3230 C  CG1 . ILE B 1 80  ? 46.12700  19.33000  40.36400 1.000 26.22000 ? 74  ILE B CG1 1 
ATOM   3231 C  CG2 . ILE B 1 80  ? 45.40300  17.97100  38.36700 1.000 20.94000 ? 74  ILE B CG2 1 
ATOM   3232 C  CD1 . ILE B 1 80  ? 47.54100  19.58300  39.89000 1.000 34.94000 ? 74  ILE B CD1 1 
ATOM   3233 N  N   . ALA B 1 81  ? 43.68300  15.36700  40.52500 1.000 21.72000 ? 75  ALA B N   1 
ATOM   3234 C  CA  . ALA B 1 81  ? 42.86300  14.21600  40.14900 1.000 23.46000 ? 75  ALA B CA  1 
ATOM   3235 C  C   . ALA B 1 81  ? 41.40400  14.45000  40.50900 1.000 24.44000 ? 75  ALA B C   1 
ATOM   3236 O  O   . ALA B 1 81  ? 40.50400  14.07200  39.75100 1.000 25.42000 ? 75  ALA B O   1 
ATOM   3237 C  CB  . ALA B 1 81  ? 43.38100  12.93700  40.81300 1.000 24.03000 ? 75  ALA B CB  1 
ATOM   3238 N  N   . LEU B 1 82  ? 41.14100  15.11500  41.63900 1.000 23.53000 ? 76  LEU B N   1 
ATOM   3239 C  CA  . LEU B 1 82  ? 39.74900  15.36800  41.99000 1.000 22.98000 ? 76  LEU B CA  1 
ATOM   3240 C  C   . LEU B 1 82  ? 39.10500  16.41100  41.07600 1.000 24.80000 ? 76  LEU B C   1 
ATOM   3241 O  O   . LEU B 1 82  ? 37.89200  16.35300  40.82600 1.000 27.40000 ? 76  LEU B O   1 
ATOM   3242 C  CB  . LEU B 1 82  ? 39.64700  15.79800  43.44400 1.000 25.62000 ? 76  LEU B CB  1 
ATOM   3243 C  CG  . LEU B 1 82  ? 38.26700  15.61400  44.08200 1.000 25.31000 ? 76  LEU B CG  1 
ATOM   3244 C  CD1 . LEU B 1 82  ? 37.96800  14.16900  44.39200 1.000 22.87000 ? 76  LEU B CD1 1 
ATOM   3245 C  CD2 . LEU B 1 82  ? 38.22200  16.43900  45.37400 1.000 28.00000 ? 76  LEU B CD2 1 
ATOM   3246 N  N   . MET B 1 83  ? 39.87200  17.37500  40.58900 1.000 20.51000 ? 77  MET B N   1 
ATOM   3247 C  CA  . MET B 1 83  ? 39.37400  18.27800  39.55300 1.000 25.41000 ? 77  MET B CA  1 
ATOM   3248 C  C   . MET B 1 83  ? 39.02100  17.54300  38.26500 1.000 25.79000 ? 77  MET B C   1 
ATOM   3249 O  O   . MET B 1 83  ? 38.20900  18.05100  37.47300 1.000 27.97000 ? 77  MET B O   1 
ATOM   3250 C  CB  . MET B 1 83  ? 40.40900  19.36500  39.22400 1.000 22.82000 ? 77  MET B CB  1 
ATOM   3251 C  CG  . MET B 1 83  ? 40.70100  20.33100  40.32900 1.000 23.12000 ? 77  MET B CG  1 
ATOM   3252 S  SD  . MET B 1 83  ? 41.89900  21.53700  39.74900 1.000 29.48000 ? 77  MET B SD  1 
ATOM   3253 C  CE  . MET B 1 83  ? 42.47900  22.15500  41.31600 1.000 25.99000 ? 77  MET B CE  1 
ATOM   3254 N  N   . CYS B 1 84  ? 39.61800  16.37600  38.02400 1.000 23.47000 ? 78  CYS B N   1 
ATOM   3255 C  CA  . CYS B 1 84  ? 39.31700  15.57600  36.84000 1.000 24.47000 ? 78  CYS B CA  1 
ATOM   3256 C  C   . CYS B 1 84  ? 38.25800  14.51200  37.08300 1.000 24.54000 ? 78  CYS B C   1 
ATOM   3257 O  O   . CYS B 1 84  ? 38.05200  13.66000  36.21100 1.000 25.53000 ? 78  CYS B O   1 
ATOM   3258 C  CB  . CYS B 1 84  ? 40.59000  14.88900  36.32900 1.000 22.99000 ? 78  CYS B CB  1 
ATOM   3259 S  SG  . CYS B 1 84  ? 41.91600  16.00700  35.87400 1.000 25.03000 ? 78  CYS B SG  1 
ATOM   3260 N  N   . ALA B 1 85  ? 37.61200  14.57400  38.22700 1.000 23.99000 ? 79  ALA B N   1 
ATOM   3261 C  CA  . ALA B 1 85  ? 36.80800  13.41400  38.64600 1.000 24.37000 ? 79  ALA B CA  1 
ATOM   3262 C  C   . ALA B 1 85  ? 35.29400  13.40700  38.53300 1.000 30.30000 ? 79  ALA B C   1 
ATOM   3263 O  O   . ALA B 1 85  ? 34.69000  14.46600  38.36500 1.000 29.71000 ? 79  ALA B O   1 
ATOM   3264 C  CB  . ALA B 1 85  ? 37.09300  13.22000  40.11200 1.000 24.96000 ? 79  ALA B CB  1 
ATOM   3265 N  N   . SER B 1 86  ? 34.75400  12.18400  38.58900 1.000 28.44000 ? 80  SER B N   1 
ATOM   3266 C  CA  . SER B 1 86  ? 33.31000  11.94300  38.79300 1.000 26.18000 ? 80  SER B CA  1 
ATOM   3267 C  C   . SER B 1 86  ? 33.37200  11.00900  40.00600 1.000 24.60000 ? 80  SER B C   1 
ATOM   3268 O  O   . SER B 1 86  ? 33.11300  9.81500   39.84400 1.000 28.72000 ? 80  SER B O   1 
ATOM   3269 C  CB  . SER B 1 86  ? 32.64700  11.31600  37.60300 1.000 26.47000 ? 80  SER B CB  1 
ATOM   3270 O  OG  . SER B 1 86  ? 32.55100  12.22900  36.53200 1.000 27.98000 ? 80  SER B OG  1 
ATOM   3271 N  N   . HIS B 1 87  ? 33.75900  11.53800  41.16900 1.000 24.99000 ? 81  HIS B N   1 
ATOM   3272 C  CA  . HIS B 1 87  ? 34.03600  10.67700  42.30600 1.000 25.43000 ? 81  HIS B CA  1 
ATOM   3273 C  C   . HIS B 1 87  ? 32.74900  10.09700  42.92100 1.000 24.76000 ? 81  HIS B C   1 
ATOM   3274 O  O   . HIS B 1 87  ? 31.60100  10.48700  42.60700 1.000 20.53000 ? 81  HIS B O   1 
ATOM   3275 C  CB  . HIS B 1 87  ? 34.88000  11.42700  43.34100 1.000 24.04000 ? 81  HIS B CB  1 
ATOM   3276 C  CG  . HIS B 1 87  ? 34.18300  12.59400  43.96900 1.000 26.77000 ? 81  HIS B CG  1 
ATOM   3277 N  ND1 . HIS B 1 87  ? 33.01700  12.47000  44.70100 1.000 24.33000 ? 81  HIS B ND1 1 
ATOM   3278 C  CD2 . HIS B 1 87  ? 34.50700  13.90800  44.00400 1.000 26.49000 ? 81  HIS B CD2 1 
ATOM   3279 C  CE1 . HIS B 1 87  ? 32.63600  13.65900  45.13500 1.000 22.78000 ? 81  HIS B CE1 1 
ATOM   3280 N  NE2 . HIS B 1 87  ? 33.52300  14.54700  44.72900 1.000 25.24000 ? 81  HIS B NE2 1 
ATOM   3281 N  N   . SER B 1 88  ? 32.95500  9.11800   43.80300 1.000 24.45000 ? 82  SER B N   1 
ATOM   3282 C  CA  . SER B 1 88  ? 31.87400  8.34800   44.40200 1.000 25.40000 ? 82  SER B CA  1 
ATOM   3283 C  C   . SER B 1 88  ? 31.30600  8.97900   45.66400 1.000 25.84000 ? 82  SER B C   1 
ATOM   3284 O  O   . SER B 1 88  ? 30.47600  8.34400   46.33100 1.000 29.46000 ? 82  SER B O   1 
ATOM   3285 C  CB  . SER B 1 88  ? 32.36200  6.95300   44.73900 1.000 23.48000 ? 82  SER B CB  1 
ATOM   3286 O  OG  . SER B 1 88  ? 32.43300  6.16500   43.57200 1.000 23.96000 ? 82  SER B OG  1 
ATOM   3287 N  N   . SER B 1 89  ? 31.73300  10.19900  45.99300 1.000 23.81000 ? 83  SER B N   1 
ATOM   3288 C  CA  . SER B 1 89  ? 31.35800  10.89500  47.23000 1.000 24.79000 ? 83  SER B CA  1 
ATOM   3289 C  C   . SER B 1 89  ? 31.67900  10.06100  48.45700 1.000 26.84000 ? 83  SER B C   1 
ATOM   3290 O  O   . SER B 1 89  ? 30.95300  10.09700  49.45100 1.000 28.08000 ? 83  SER B O   1 
ATOM   3291 C  CB  . SER B 1 89  ? 29.87600  11.28500  47.23300 1.000 28.47000 ? 83  SER B CB  1 
ATOM   3292 O  OG  . SER B 1 89  ? 29.43400  11.64100  45.92700 1.000 28.10000 ? 83  SER B OG  1 
ATOM   3293 N  N   . GLU B 1 90  ? 32.74800  9.27300   48.39300 1.000 28.23000 ? 84  GLU B N   1 
ATOM   3294 C  CA  . GLU B 1 90  ? 33.27900  8.66200   49.60500 1.000 27.79000 ? 84  GLU B CA  1 
ATOM   3295 C  C   . GLU B 1 90  ? 33.73900  9.75700   50.56200 1.000 31.09000 ? 84  GLU B C   1 
ATOM   3296 O  O   . GLU B 1 90  ? 33.93400  10.92000  50.18500 1.000 30.68000 ? 84  GLU B O   1 
ATOM   3297 C  CB  . GLU B 1 90  ? 34.43100  7.70700   49.26000 1.000 27.64000 ? 84  GLU B CB  1 
ATOM   3298 C  CG  . GLU B 1 90  ? 33.96000  6.49900   48.40800 1.000 31.32000 ? 84  GLU B CG  1 
ATOM   3299 C  CD  . GLU B 1 90  ? 35.09500  5.74700   47.65400 1.000 35.86000 ? 84  GLU B CD  1 
ATOM   3300 O  OE1 . GLU B 1 90  ? 36.29700  6.00500   47.91500 1.000 33.72000 ? 84  GLU B OE1 1 
ATOM   3301 O  OE2 . GLU B 1 90  ? 34.77000  4.87900   46.79500 1.000 34.64000 ? 84  GLU B OE2 1 
ATOM   3302 N  N   . ASP B 1 91  ? 33.91200  9.39800   51.83100 1.000 33.73000 ? 85  ASP B N   1 
ATOM   3303 C  CA  . ASP B 1 91  ? 34.27800  10.44600  52.77800 1.000 35.39000 ? 85  ASP B CA  1 
ATOM   3304 C  C   . ASP B 1 91  ? 35.63700  11.05900  52.43400 1.000 32.74000 ? 85  ASP B C   1 
ATOM   3305 O  O   . ASP B 1 91  ? 35.85900  12.25000  52.68200 1.000 30.10000 ? 85  ASP B O   1 
ATOM   3306 C  CB  . ASP B 1 91  ? 34.22300  9.90700   54.21500 1.000 35.42000 ? 85  ASP B CB  1 
ATOM   3307 C  CG  . ASP B 1 91  ? 32.76300  9.74800   54.74400 1.000 40.65000 ? 85  ASP B CG  1 
ATOM   3308 O  OD1 . ASP B 1 91  ? 31.78900  10.14600  54.05100 1.000 43.43000 ? 85  ASP B OD1 1 
ATOM   3309 O  OD2 . ASP B 1 91  ? 32.58100  9.21900   55.86000 1.000 47.09000 ? 85  ASP B OD2 1 
ATOM   3310 N  N   . ARG B 1 92  ? 36.55000  10.29900  51.82500 1.000 30.81000 ? 86  ARG B N   1 
ATOM   3311 C  CA  . ARG B 1 92  ? 37.82700  10.92500  51.48200 1.000 31.33000 ? 86  ARG B CA  1 
ATOM   3312 C  C   . ARG B 1 92  ? 37.66500  11.94900  50.35600 1.000 32.21000 ? 86  ARG B C   1 
ATOM   3313 O  O   . ARG B 1 92  ? 38.41400  12.93500  50.31700 1.000 32.45000 ? 86  ARG B O   1 
ATOM   3314 C  CB  . ARG B 1 92  ? 38.87100  9.86900   51.11300 1.000 33.65000 ? 86  ARG B CB  1 
ATOM   3315 C  CG  . ARG B 1 92  ? 38.46300  9.01400   49.92100 1.000 34.85000 ? 86  ARG B CG  1 
ATOM   3316 C  CD  . ARG B 1 92  ? 39.50000  7.93700   49.59400 1.000 36.76000 ? 86  ARG B CD  1 
ATOM   3317 N  NE  . ARG B 1 92  ? 38.92500  6.94000   48.69400 1.000 36.68000 ? 86  ARG B NE  1 
ATOM   3318 C  CZ  . ARG B 1 92  ? 39.56300  5.87000   48.22900 1.000 35.63000 ? 86  ARG B CZ  1 
ATOM   3319 N  NH1 . ARG B 1 92  ? 40.82700  5.63500   48.53000 1.000 34.84000 ? 86  ARG B NH1 1 
ATOM   3320 N  NH2 . ARG B 1 92  ? 38.91100  5.01700   47.44000 1.000 33.53000 ? 86  ARG B NH2 1 
ATOM   3321 N  N   . HIS B 1 93  ? 36.68500  11.76100  49.45500 1.000 27.08000 ? 87  HIS B N   1 
ATOM   3322 C  CA  . HIS B 1 93  ? 36.42700  12.77300  48.42500 1.000 29.37000 ? 87  HIS B CA  1 
ATOM   3323 C  C   . HIS B 1 93  ? 35.83000  14.03700  49.03400 1.000 30.52000 ? 87  HIS B C   1 
ATOM   3324 O  O   . HIS B 1 93  ? 36.23800  15.15400  48.69800 1.000 31.07000 ? 87  HIS B O   1 
ATOM   3325 C  CB  . HIS B 1 93  ? 35.47700  12.23100  47.36100 1.000 28.28000 ? 87  HIS B CB  1 
ATOM   3326 C  CG  . HIS B 1 93  ? 35.96600  11.00000  46.66400 1.000 28.97000 ? 87  HIS B CG  1 
ATOM   3327 N  ND1 . HIS B 1 93  ? 35.24500  9.82200   46.64100 1.000 29.05000 ? 87  HIS B ND1 1 
ATOM   3328 C  CD2 . HIS B 1 93  ? 37.07700  10.77500  45.92500 1.000 27.66000 ? 87  HIS B CD2 1 
ATOM   3329 C  CE1 . HIS B 1 93  ? 35.90100  8.91800   45.93400 1.000 28.94000 ? 87  HIS B CE1 1 
ATOM   3330 N  NE2 . HIS B 1 93  ? 37.02000  9.46900   45.49300 1.000 23.94000 ? 87  HIS B NE2 1 
ATOM   3331 N  N   . ILE B 1 94  ? 34.83600  13.87300  49.91300 1.000 30.48000 ? 88  ILE B N   1 
ATOM   3332 C  CA  . ILE B 1 94  ? 34.24000  15.00400  50.61800 1.000 31.76000 ? 88  ILE B CA  1 
ATOM   3333 C  C   . ILE B 1 94  ? 35.29700  15.72400  51.44700 1.000 34.01000 ? 88  ILE B C   1 
ATOM   3334 O  O   . ILE B 1 94  ? 35.35700  16.96100  51.47900 1.000 31.17000 ? 88  ILE B O   1 
ATOM   3335 C  CB  . ILE B 1 94  ? 33.06400  14.52700  51.49900 1.000 31.76000 ? 88  ILE B CB  1 
ATOM   3336 C  CG1 . ILE B 1 94  ? 31.96400  13.84500  50.67100 1.000 31.81000 ? 88  ILE B CG1 1 
ATOM   3337 C  CG2 . ILE B 1 94  ? 32.48300  15.69000  52.29800 1.000 32.40000 ? 88  ILE B CG2 1 
ATOM   3338 C  CD1 . ILE B 1 94  ? 30.85900  13.18200  51.57100 1.000 31.54000 ? 88  ILE B CD1 1 
ATOM   3339 N  N   . ALA B 1 95  ? 36.16800  14.96700  52.10900 1.000 31.14000 ? 89  ALA B N   1 
ATOM   3340 C  CA  . ALA B 1 95  ? 37.21700  15.60200  52.89800 1.000 32.83000 ? 89  ALA B CA  1 
ATOM   3341 C  C   . ALA B 1 95  ? 38.18000  16.38300  52.00900 1.000 35.09000 ? 89  ALA B C   1 
ATOM   3342 O  O   . ALA B 1 95  ? 38.57500  17.51500  52.33600 1.000 31.09000 ? 89  ALA B O   1 
ATOM   3343 C  CB  . ALA B 1 95  ? 37.96500  14.54500  53.70300 1.000 31.53000 ? 89  ALA B CB  1 
ATOM   3344 N  N   . ARG B 1 96  ? 38.56400  15.80800  50.87100 1.000 31.88000 ? 90  ARG B N   1 
ATOM   3345 C  CA  . ARG B 1 96  ? 39.51400  16.52000  50.02900 1.000 29.86000 ? 90  ARG B CA  1 
ATOM   3346 C  C   . ARG B 1 96  ? 38.88500  17.77000  49.43200 1.000 29.08000 ? 90  ARG B C   1 
ATOM   3347 O  O   . ARG B 1 96  ? 39.57300  18.76900  49.24600 1.000 29.62000 ? 90  ARG B O   1 
ATOM   3348 C  CB  . ARG B 1 96  ? 40.04900  15.60400  48.93400 1.000 27.35000 ? 90  ARG B CB  1 
ATOM   3349 C  CG  . ARG B 1 96  ? 41.11600  16.29700  48.05900 1.000 28.50000 ? 90  ARG B CG  1 
ATOM   3350 C  CD  . ARG B 1 96  ? 41.86200  15.28800  47.20700 1.000 27.86000 ? 90  ARG B CD  1 
ATOM   3351 N  NE  . ARG B 1 96  ? 42.65900  14.38700  48.03600 1.000 32.91000 ? 90  ARG B NE  1 
ATOM   3352 C  CZ  . ARG B 1 96  ? 43.84400  14.70200  48.55300 1.000 35.67000 ? 90  ARG B CZ  1 
ATOM   3353 N  NH1 . ARG B 1 96  ? 44.37700  15.90100  48.38200 1.000 33.00000 ? 90  ARG B NH1 1 
ATOM   3354 N  NH2 . ARG B 1 96  ? 44.52300  13.78500  49.24100 1.000 31.03000 ? 90  ARG B NH2 1 
ATOM   3355 N  N   . THR B 1 97  ? 37.58000  17.73600  49.14400 1.000 28.96000 ? 91  THR B N   1 
ATOM   3356 C  CA  . THR B 1 97  ? 36.88600  18.93500  48.68200 1.000 28.49000 ? 91  THR B CA  1 
ATOM   3357 C  C   . THR B 1 97  ? 36.93200  20.04500  49.73500 1.000 31.84000 ? 91  THR B C   1 
ATOM   3358 O  O   . THR B 1 97  ? 37.19700  21.20800  49.40500 1.000 30.77000 ? 91  THR B O   1 
ATOM   3359 C  CB  . THR B 1 97  ? 35.43800  18.59000  48.30800 1.000 30.46000 ? 91  THR B CB  1 
ATOM   3360 O  OG1 . THR B 1 97  ? 35.42300  17.59300  47.27800 1.000 27.57000 ? 91  THR B OG1 1 
ATOM   3361 C  CG2 . THR B 1 97  ? 34.71800  19.81500  47.78500 1.000 27.31000 ? 91  THR B CG2 1 
ATOM   3362 N  N   . ARG B 1 98  ? 36.69300  19.70800  51.01100 1.000 30.20000 ? 92  ARG B N   1 
ATOM   3363 C  CA  . ARG B 1 98  ? 36.81000  20.71100  52.07000 1.000 31.31000 ? 92  ARG B CA  1 
ATOM   3364 C  C   . ARG B 1 98  ? 38.25200  21.21300  52.22200 1.000 34.37000 ? 92  ARG B C   1 
ATOM   3365 O  O   . ARG B 1 98  ? 38.48000  22.41500  52.41900 1.000 35.15000 ? 92  ARG B O   1 
ATOM   3366 C  CB  . ARG B 1 98  ? 36.26300  20.13400  53.37600 1.000 31.83000 ? 92  ARG B CB  1 
ATOM   3367 C  CG  . ARG B 1 98  ? 34.75800  19.93500  53.31100 1.000 31.93000 ? 92  ARG B CG  1 
ATOM   3368 C  CD  . ARG B 1 98  ? 34.17100  19.25700  54.54700 1.000 38.24000 ? 92  ARG B CD  1 
ATOM   3369 N  NE  . ARG B 1 98  ? 32.71400  19.38800  54.59400 1.000 35.58000 ? 92  ARG B NE  1 
ATOM   3370 C  CZ  . ARG B 1 98  ? 31.88000  18.46200  55.06200 1.000 47.74000 ? 92  ARG B CZ  1 
ATOM   3371 N  NH1 . ARG B 1 98  ? 32.32200  17.30200  55.53000 1.000 46.11000 ? 92  ARG B NH1 1 
ATOM   3372 N  NH2 . ARG B 1 98  ? 30.56400  18.69800  55.04200 1.000 47.29000 ? 92  ARG B NH2 1 
ATOM   3373 N  N   . ALA B 1 99  ? 39.24400  20.32400  52.08200 1.000 31.99000 ? 93  ALA B N   1 
ATOM   3374 C  CA  . ALA B 1 99  ? 40.64300  20.75600  52.10200 1.000 30.38000 ? 93  ALA B CA  1 
ATOM   3375 C  C   . ALA B 1 99  ? 40.93500  21.77500  51.00500 1.000 33.68000 ? 93  ALA B C   1 
ATOM   3376 O  O   . ALA B 1 99  ? 41.66400  22.75300  51.22400 1.000 34.49000 ? 93  ALA B O   1 
ATOM   3377 C  CB  . ALA B 1 99  ? 41.55400  19.54100  51.93100 1.000 29.81000 ? 93  ALA B CB  1 
ATOM   3378 N  N   . MET B 1 100 ? 40.41800  21.53100  49.80200 1.000 31.12000 ? 94  MET B N   1 
ATOM   3379 C  CA  . MET B 1 100 ? 40.67700  22.42300  48.68100 1.000 32.41000 ? 94  MET B CA  1 
ATOM   3380 C  C   . MET B 1 100 ? 39.97400  23.76400  48.87900 1.000 33.50000 ? 94  MET B C   1 
ATOM   3381 O  O   . MET B 1 100 ? 40.53600  24.82200  48.57100 1.000 33.13000 ? 94  MET B O   1 
ATOM   3382 C  CB  . MET B 1 100 ? 40.23000  21.74200  47.38500 1.000 27.90000 ? 94  MET B CB  1 
ATOM   3383 C  CG  . MET B 1 100 ? 41.03000  20.48900  47.06900 1.000 27.79000 ? 94  MET B CG  1 
ATOM   3384 S  SD  . MET B 1 100 ? 40.41500  19.54900  45.65200 1.000 31.61000 ? 94  MET B SD  1 
ATOM   3385 C  CE  . MET B 1 100 ? 40.49300  20.73600  44.30100 1.000 25.05000 ? 94  MET B CE  1 
ATOM   3386 N  N   . LEU B 1 101 ? 38.74900  23.73900  49.41700 1.000 32.61000 ? 95  LEU B N   1 
ATOM   3387 C  CA  . LEU B 1 101 ? 38.06200  24.98400  49.73900 1.000 30.25000 ? 95  LEU B CA  1 
ATOM   3388 C  C   . LEU B 1 101 ? 38.87400  25.81100  50.72200 1.000 36.13000 ? 95  LEU B C   1 
ATOM   3389 O  O   . LEU B 1 101 ? 39.00300  27.03600  50.56100 1.000 35.41000 ? 95  LEU B O   1 
ATOM   3390 C  CB  . LEU B 1 101 ? 36.67700  24.69600  50.31700 1.000 29.96000 ? 95  LEU B CB  1 
ATOM   3391 C  CG  . LEU B 1 101 ? 35.55100  24.36300  49.34100 1.000 33.69000 ? 95  LEU B CG  1 
ATOM   3392 C  CD1 . LEU B 1 101 ? 34.32000  23.84700  50.11100 1.000 33.39000 ? 95  LEU B CD1 1 
ATOM   3393 C  CD2 . LEU B 1 101 ? 35.21800  25.58600  48.46100 1.000 29.39000 ? 95  LEU B CD2 1 
ATOM   3394 N  N   . SER B 1 102 ? 39.44200  25.16500  51.74500 1.000 31.48000 ? 96  SER B N   1 
ATOM   3395 C  CA  . SER B 1 102 ? 40.28100  25.91200  52.67700 1.000 34.56000 ? 96  SER B CA  1 
ATOM   3396 C  C   . SER B 1 102 ? 41.50000  26.49700  51.98000 1.000 37.90000 ? 96  SER B C   1 
ATOM   3397 O  O   . SER B 1 102 ? 41.88300  27.63500  52.26100 1.000 33.62000 ? 96  SER B O   1 
ATOM   3398 C  CB  . SER B 1 102 ? 40.69700  25.03300  53.84800 1.000 34.55000 ? 96  SER B CB  1 
ATOM   3399 O  OG  . SER B 1 102 ? 39.52900  24.54500  54.50800 1.000 42.50000 ? 96  SER B OG  1 
ATOM   3400 N  N   . LYS B 1 103 ? 42.10900  25.75300  51.03900 1.000 36.64000 ? 97  LYS B N   1 
ATOM   3401 C  CA  . LYS B 1 103 ? 43.31300  26.27200  50.39500 1.000 35.35000 ? 97  LYS B CA  1 
ATOM   3402 C  C   . LYS B 1 103 ? 43.04500  27.56200  49.64200 1.000 36.32000 ? 97  LYS B C   1 
ATOM   3403 O  O   . LYS B 1 103 ? 43.95100  28.39300  49.50500 1.000 41.12000 ? 97  LYS B O   1 
ATOM   3404 C  CB  . LYS B 1 103 ? 43.91000  25.25400  49.44100 1.000 35.18000 ? 97  LYS B CB  1 
ATOM   3405 C  CG  . LYS B 1 103 ? 44.47400  24.05400  50.13400 1.000 36.88000 ? 97  LYS B CG  1 
ATOM   3406 C  CD  . LYS B 1 103 ? 45.23100  23.21300  49.13600 1.000 33.48000 ? 97  LYS B CD  1 
ATOM   3407 C  CE  . LYS B 1 103 ? 45.91600  22.06500  49.83100 1.000 34.61000 ? 97  LYS B CE  1 
ATOM   3408 N  NZ  . LYS B 1 103 ? 46.54300  21.18900  48.81900 1.000 35.09000 ? 97  LYS B NZ  1 
ATOM   3409 N  N   . ILE B 1 104 ? 41.82900  27.75600  49.13400 1.000 30.72000 ? 98  ILE B N   1 
ATOM   3410 C  CA  . ILE B 1 104 ? 41.51400  28.99400  48.43400 1.000 31.89000 ? 98  ILE B CA  1 
ATOM   3411 C  C   . ILE B 1 104 ? 40.67400  29.92700  49.29200 1.000 35.23000 ? 98  ILE B C   1 
ATOM   3412 O  O   . ILE B 1 104 ? 40.22700  30.97200  48.80700 1.000 33.26000 ? 98  ILE B O   1 
ATOM   3413 C  CB  . ILE B 1 104 ? 40.83400  28.72900  47.07800 1.000 35.15000 ? 98  ILE B CB  1 
ATOM   3414 C  CG1 . ILE B 1 104 ? 39.41300  28.19700  47.27100 1.000 32.59000 ? 98  ILE B CG1 1 
ATOM   3415 C  CG2 . ILE B 1 104 ? 41.68500  27.76100  46.23600 1.000 30.06000 ? 98  ILE B CG2 1 
ATOM   3416 C  CD1 . ILE B 1 104 ? 38.58800  28.08600  45.99400 1.000 30.89000 ? 98  ILE B CD1 1 
ATOM   3417 N  N   . LYS B 1 105 ? 40.47300  29.58700  50.56900 1.000 32.70000 ? 99  LYS B N   1 
ATOM   3418 C  CA  . LYS B 1 105 ? 39.71500  30.40800  51.52400 1.000 33.49000 ? 99  LYS B CA  1 
ATOM   3419 C  C   . LYS B 1 105 ? 38.28800  30.68100  51.03100 1.000 40.24000 ? 99  LYS B C   1 
ATOM   3420 O  O   . LYS B 1 105 ? 37.79100  31.80600  51.08200 1.000 40.51000 ? 99  LYS B O   1 
ATOM   3421 C  CB  . LYS B 1 105 ? 40.45200  31.71400  51.85100 1.000 36.40000 ? 99  LYS B CB  1 
ATOM   3422 C  CG  . LYS B 1 105 ? 41.77300  31.48900  52.56000 1.000 41.31000 ? 99  LYS B CG  1 
ATOM   3423 C  CD  . LYS B 1 105 ? 42.49100  32.78000  52.95000 1.000 48.19000 ? 99  LYS B CD  1 
ATOM   3424 C  CE  . LYS B 1 105 ? 43.79700  32.45900  53.68100 1.000 51.71000 ? 99  LYS B CE  1 
ATOM   3425 N  NZ  . LYS B 1 105 ? 44.56500  33.68200  54.10000 1.000 60.25000 ? 99  LYS B NZ  1 
ATOM   3426 N  N   . ALA B 1 106 ? 37.61600  29.62900  50.57000 1.000 35.31000 ? 100 ALA B N   1 
ATOM   3427 C  CA  . ALA B 1 106 ? 36.20300  29.67000  50.20800 1.000 36.17000 ? 100 ALA B CA  1 
ATOM   3428 C  C   . ALA B 1 106 ? 35.41900  28.74500  51.13600 1.000 38.39000 ? 100 ALA B C   1 
ATOM   3429 O  O   . ALA B 1 106 ? 35.98900  28.00500  51.94100 1.000 36.59000 ? 100 ALA B O   1 
ATOM   3430 C  CB  . ALA B 1 106 ? 35.99600  29.26900  48.73700 1.000 33.83000 ? 100 ALA B CB  1 
ATOM   3431 N  N   . GLU B 1 107 ? 34.09400  28.78100  51.02100 1.000 39.13000 ? 101 GLU B N   1 
ATOM   3432 C  CA  . GLU B 1 107 ? 33.23400  27.94900  51.85500 1.000 40.54000 ? 101 GLU B CA  1 
ATOM   3433 C  C   . GLU B 1 107 ? 32.30900  27.11700  50.96900 1.000 40.07000 ? 101 GLU B C   1 
ATOM   3434 O  O   . GLU B 1 107 ? 32.13900  27.39200  49.77500 1.000 34.15000 ? 101 GLU B O   1 
ATOM   3435 C  CB  . GLU B 1 107 ? 32.40300  28.78600  52.83800 1.000 39.60000 ? 101 GLU B CB  1 
ATOM   3436 C  CG  . GLU B 1 107 ? 33.13200  29.98000  53.46400 1.000 48.35000 ? 101 GLU B CG  1 
ATOM   3437 C  CD  . GLU B 1 107 ? 33.84000  29.67200  54.79700 1.000 61.58000 ? 101 GLU B CD  1 
ATOM   3438 O  OE1 . GLU B 1 107 ? 33.87300  28.49100  55.22500 1.000 61.64000 ? 101 GLU B OE1 1 
ATOM   3439 O  OE2 . GLU B 1 107 ? 34.36700  30.63200  55.42400 1.000 69.21000 ? 101 GLU B OE2 1 
ATOM   3440 N  N   . GLU B 1 108 ? 31.69900  26.08700  51.57000 1.000 37.29000 ? 102 GLU B N   1 
ATOM   3441 C  CA  . GLU B 1 108 ? 30.80200  25.23700  50.79000 1.000 39.93000 ? 102 GLU B CA  1 
ATOM   3442 C  C   . GLU B 1 108 ? 29.66700  26.04600  50.19300 1.000 37.38000 ? 102 GLU B C   1 
ATOM   3443 O  O   . GLU B 1 108 ? 29.18500  25.72800  49.10100 1.000 37.60000 ? 102 GLU B O   1 
ATOM   3444 C  CB  . GLU B 1 108 ? 30.23800  24.11000  51.64300 1.000 38.77000 ? 102 GLU B CB  1 
ATOM   3445 C  CG  . GLU B 1 108 ? 31.29900  23.33400  52.39200 1.000 43.20000 ? 102 GLU B CG  1 
ATOM   3446 C  CD  . GLU B 1 108 ? 30.72100  22.14600  53.16400 1.000 46.51000 ? 102 GLU B CD  1 
ATOM   3447 O  OE1 . GLU B 1 108 ? 29.50100  21.82100  53.01100 1.000 41.22000 ? 102 GLU B OE1 1 
ATOM   3448 O  OE2 . GLU B 1 108 ? 31.50300  21.53800  53.93400 1.000 48.57000 ? 102 GLU B OE2 1 
ATOM   3449 N  N   . ALA B 1 109 ? 29.25600  27.11500  50.87100 1.000 34.90000 ? 103 ALA B N   1 
ATOM   3450 C  CA  . ALA B 1 109 ? 28.19400  27.95500  50.34800 1.000 35.20000 ? 103 ALA B CA  1 
ATOM   3451 C  C   . ALA B 1 109 ? 28.57500  28.62600  49.03100 1.000 36.89000 ? 103 ALA B C   1 
ATOM   3452 O  O   . ALA B 1 109 ? 27.68100  29.11800  48.33400 1.000 35.69000 ? 103 ALA B O   1 
ATOM   3453 C  CB  . ALA B 1 109 ? 27.80200  28.99400  51.39700 1.000 36.63000 ? 103 ALA B CB  1 
ATOM   3454 N  N   . ASP B 1 110 ? 29.86400  28.63500  48.66000 1.000 34.07000 ? 104 ASP B N   1 
ATOM   3455 C  CA  . ASP B 1 110 ? 30.30600  29.22100  47.39800 1.000 34.14000 ? 104 ASP B CA  1 
ATOM   3456 C  C   . ASP B 1 110 ? 30.14700  28.26700  46.21800 1.000 36.35000 ? 104 ASP B C   1 
ATOM   3457 O  O   . ASP B 1 110 ? 30.29500  28.69300  45.06600 1.000 30.32000 ? 104 ASP B O   1 
ATOM   3458 C  CB  . ASP B 1 110 ? 31.77500  29.65000  47.48000 1.000 35.69000 ? 104 ASP B CB  1 
ATOM   3459 C  CG  . ASP B 1 110 ? 32.01100  30.81500  48.43100 1.000 39.29000 ? 104 ASP B CG  1 
ATOM   3460 O  OD1 . ASP B 1 110 ? 31.23000  31.79900  48.40200 1.000 39.78000 ? 104 ASP B OD1 1 
ATOM   3461 O  OD2 . ASP B 1 110 ? 32.99900  30.74600  49.20600 1.000 41.33000 ? 104 ASP B OD2 1 
ATOM   3462 N  N   . LEU B 1 111 ? 29.85400  26.99500  46.47100 1.000 36.11000 ? 105 LEU B N   1 
ATOM   3463 C  CA  . LEU B 1 111 ? 29.63800  26.03900  45.39400 1.000 34.53000 ? 105 LEU B CA  1 
ATOM   3464 C  C   . LEU B 1 111 ? 28.27500  26.24600  44.74200 1.000 38.22000 ? 105 LEU B C   1 
ATOM   3465 O  O   . LEU B 1 111 ? 27.26500  26.46600  45.42000 1.000 36.48000 ? 105 LEU B O   1 
ATOM   3466 C  CB  . LEU B 1 111 ? 29.74700  24.61000  45.93800 1.000 32.58000 ? 105 LEU B CB  1 
ATOM   3467 C  CG  . LEU B 1 111 ? 31.11900  24.24900  46.51900 1.000 33.43000 ? 105 LEU B CG  1 
ATOM   3468 C  CD1 . LEU B 1 111 ? 31.02100  22.91300  47.28600 1.000 30.31000 ? 105 LEU B CD1 1 
ATOM   3469 C  CD2 . LEU B 1 111 ? 32.15600  24.16500  45.38900 1.000 27.85000 ? 105 LEU B CD2 1 
ATOM   3470 N  N   . ARG B 1 112 ? 28.25100  26.16500  43.41000 1.000 36.77000 ? 106 ARG B N   1 
ATOM   3471 C  CA  . ARG B 1 112 ? 27.01200  26.24500  42.64100 1.000 37.69000 ? 106 ARG B CA  1 
ATOM   3472 C  C   . ARG B 1 112 ? 26.58500  24.89600  42.07100 1.000 32.60000 ? 106 ARG B C   1 
ATOM   3473 O  O   . ARG B 1 112 ? 25.73800  24.86300  41.17600 1.000 37.57000 ? 106 ARG B O   1 
ATOM   3474 C  CB  . ARG B 1 112 ? 27.16000  27.26900  41.50700 1.000 39.58000 ? 106 ARG B CB  1 
ATOM   3475 C  CG  . ARG B 1 112 ? 27.25900  28.69700  42.00800 1.000 41.27000 ? 106 ARG B CG  1 
ATOM   3476 C  CD  . ARG B 1 112 ? 26.02400  29.08100  42.84900 1.000 43.92000 ? 106 ARG B CD  1 
ATOM   3477 N  NE  . ARG B 1 112 ? 26.25500  30.37300  43.48400 1.000 49.54000 ? 106 ARG B NE  1 
ATOM   3478 C  CZ  . ARG B 1 112 ? 26.55400  30.55000  44.76400 1.000 46.01000 ? 106 ARG B CZ  1 
ATOM   3479 N  NH1 . ARG B 1 112 ? 26.50800  29.54900  45.63200 1.000 45.35000 ? 106 ARG B NH1 1 
ATOM   3480 N  NH2 . ARG B 1 112 ? 26.90400  31.76300  45.18400 1.000 50.40000 ? 106 ARG B NH2 1 
ATOM   3481 N  N   . CYS B 1 113 ? 27.20300  23.79600  42.51300 1.000 32.02000 ? 107 CYS B N   1 
ATOM   3482 C  CA  . CYS B 1 113 ? 26.79000  22.43900  42.16000 1.000 35.34000 ? 107 CYS B CA  1 
ATOM   3483 C  C   . CYS B 1 113 ? 25.98000  21.88000  43.30200 1.000 37.55000 ? 107 CYS B C   1 
ATOM   3484 O  O   . CYS B 1 113 ? 26.03100  22.39700  44.42100 1.000 36.61000 ? 107 CYS B O   1 
ATOM   3485 C  CB  . CYS B 1 113 ? 27.98200  21.52400  41.89000 1.000 37.62000 ? 107 CYS B CB  1 
ATOM   3486 S  SG  . CYS B 1 113 ? 29.15500  21.47600  43.26200 1.000 34.50000 ? 107 CYS B SG  1 
ATOM   3487 N  N   . GLY B 1 114 ? 25.22100  20.81900  43.02100 1.000 35.66000 ? 108 GLY B N   1 
ATOM   3488 C  CA  . GLY B 1 114 ? 24.26000  20.32800  43.97700 1.000 35.41000 ? 108 GLY B CA  1 
ATOM   3489 C  C   . GLY B 1 114 ? 24.46500  18.85300  44.26400 1.000 34.36000 ? 108 GLY B C   1 
ATOM   3490 O  O   . GLY B 1 114 ? 25.03100  18.10900  43.46200 1.000 32.01000 ? 108 GLY B O   1 
ATOM   3491 N  N   . GLY B 1 115 ? 23.96300  18.43300  45.42000 1.000 33.58000 ? 109 GLY B N   1 
ATOM   3492 C  CA  . GLY B 1 115 ? 24.06300  17.03300  45.79400 1.000 31.91000 ? 109 GLY B CA  1 
ATOM   3493 C  C   . GLY B 1 115 ? 23.23000  16.12500  44.90800 1.000 33.77000 ? 109 GLY B C   1 
ATOM   3494 O  O   . GLY B 1 115 ? 22.29200  16.54600  44.22700 1.000 33.78000 ? 109 GLY B O   1 
ATOM   3495 N  N   . HIS B 1 116 ? 23.56600  14.83800  44.94900 1.000 29.61000 ? 110 HIS B N   1 
ATOM   3496 C  CA  . HIS B 1 116 ? 22.83400  13.81600  44.21500 1.000 34.00000 ? 110 HIS B CA  1 
ATOM   3497 C  C   . HIS B 1 116 ? 23.13400  12.47500  44.86300 1.000 30.98000 ? 110 HIS B C   1 
ATOM   3498 O  O   . HIS B 1 116 ? 24.11400  12.35600  45.60500 1.000 31.30000 ? 110 HIS B O   1 
ATOM   3499 C  CB  . HIS B 1 116 ? 23.26700  13.79000  42.74800 1.000 27.24000 ? 110 HIS B CB  1 
ATOM   3500 C  CG  . HIS B 1 116 ? 24.74700  13.61100  42.59300 1.000 31.60000 ? 110 HIS B CG  1 
ATOM   3501 N  ND1 . HIS B 1 116 ? 25.37300  12.40700  42.84500 1.000 33.14000 ? 110 HIS B ND1 1 
ATOM   3502 C  CD2 . HIS B 1 116 ? 25.72800  14.49000  42.27600 1.000 30.25000 ? 110 HIS B CD2 1 
ATOM   3503 C  CE1 . HIS B 1 116 ? 26.67500  12.54300  42.66100 1.000 30.46000 ? 110 HIS B CE1 1 
ATOM   3504 N  NE2 . HIS B 1 116 ? 26.91800  13.79600  42.31300 1.000 31.19000 ? 110 HIS B NE2 1 
ATOM   3505 N  N   . PRO B 1 117 ? 22.34500  11.44000  44.56900 1.000 32.35000 ? 111 PRO B N   1 
ATOM   3506 C  CA  . PRO B 1 117 ? 22.68800  10.10100  45.06100 1.000 30.69000 ? 111 PRO B CA  1 
ATOM   3507 C  C   . PRO B 1 117 ? 24.07000  9.67900   44.58000 1.000 32.03000 ? 111 PRO B C   1 
ATOM   3508 O  O   . PRO B 1 117 ? 24.46000  9.95900   43.44800 1.000 34.26000 ? 111 PRO B O   1 
ATOM   3509 C  CB  . PRO B 1 117 ? 21.57900  9.22200   44.47800 1.000 32.52000 ? 111 PRO B CB  1 
ATOM   3510 C  CG  . PRO B 1 117 ? 20.41900  10.15500  44.38100 1.000 33.44000 ? 111 PRO B CG  1 
ATOM   3511 C  CD  . PRO B 1 117 ? 20.99400  11.47800  43.98000 1.000 31.03000 ? 111 PRO B CD  1 
ATOM   3512 N  N   . SER B 1 118 ? 24.83200  9.04600   45.47300 1.000 30.20000 ? 112 SER B N   1 
ATOM   3513 C  CA  . SER B 1 118 ? 26.20300  8.67600   45.14900 1.000 31.96000 ? 112 SER B CA  1 
ATOM   3514 C  C   . SER B 1 118 ? 26.27300  7.83900   43.87500 1.000 33.29000 ? 112 SER B C   1 
ATOM   3515 O  O   . SER B 1 118 ? 25.34900  7.08900   43.55700 1.000 33.44000 ? 112 SER B O   1 
ATOM   3516 C  CB  . SER B 1 118 ? 26.82900  7.88000   46.29000 1.000 32.86000 ? 112 SER B CB  1 
ATOM   3517 O  OG  . SER B 1 118 ? 28.11900  7.42900   45.87700 1.000 33.72000 ? 112 SER B OG  1 
ATOM   3518 N  N   . LEU B 1 119 ? 27.39800  7.95700   43.14000 1.000 28.31000 ? 113 LEU B N   1 
ATOM   3519 C  CA  . LEU B 1 119 ? 27.65700  7.04500   42.01900 1.000 32.10000 ? 113 LEU B CA  1 
ATOM   3520 C  C   . LEU B 1 119 ? 28.09000  5.65000   42.46800 1.000 29.85000 ? 113 LEU B C   1 
ATOM   3521 O  O   . LEU B 1 119 ? 28.26000  4.76400   41.62200 1.000 33.38000 ? 113 LEU B O   1 
ATOM   3522 C  CB  . LEU B 1 119 ? 28.72300  7.61600   41.07900 1.000 26.58000 ? 113 LEU B CB  1 
ATOM   3523 C  CG  . LEU B 1 119 ? 28.42100  8.97200   40.40600 1.000 31.09000 ? 113 LEU B CG  1 
ATOM   3524 C  CD1 . LEU B 1 119 ? 29.52100  9.37900   39.45700 1.000 28.01000 ? 113 LEU B CD1 1 
ATOM   3525 C  CD2 . LEU B 1 119 ? 27.09300  8.96200   39.68500 1.000 32.77000 ? 113 LEU B CD2 1 
ATOM   3526 N  N   . SER B 1 120 ? 28.29500  5.44100   43.76500 1.000 32.84000 ? 114 SER B N   1 
ATOM   3527 C  CA  . SER B 1 120 ? 28.63400  4.13800   44.32300 1.000 35.44000 ? 114 SER B CA  1 
ATOM   3528 C  C   . SER B 1 120 ? 27.43700  3.60600   45.09300 1.000 33.20000 ? 114 SER B C   1 
ATOM   3529 O  O   . SER B 1 120 ? 26.90700  4.29500   45.97200 1.000 36.14000 ? 114 SER B O   1 
ATOM   3530 C  CB  . SER B 1 120 ? 29.84600  4.22800   45.25400 1.000 33.92000 ? 114 SER B CB  1 
ATOM   3531 O  OG  . SER B 1 120 ? 29.81400  3.17500   46.21700 1.000 33.81000 ? 114 SER B OG  1 
ATOM   3532 N  N   . GLU B 1 121 ? 27.01000  2.38600   44.76400 1.000 36.02000 ? 115 GLU B N   1 
ATOM   3533 C  CA  . GLU B 1 121 ? 25.91900  1.77100   45.50400 1.000 37.49000 ? 115 GLU B CA  1 
ATOM   3534 C  C   . GLU B 1 121 ? 26.25900  1.64300   46.98200 1.000 37.64000 ? 115 GLU B C   1 
ATOM   3535 O  O   . GLU B 1 121 ? 25.40600  1.86200   47.85500 1.000 38.33000 ? 115 GLU B O   1 
ATOM   3536 C  CB  . GLU B 1 121 ? 25.60400  0.40500   44.90000 1.000 47.69000 ? 115 GLU B CB  1 
ATOM   3537 C  CG  . GLU B 1 121 ? 24.46800  0.48200   43.91600 1.000 56.67000 ? 115 GLU B CG  1 
ATOM   3538 C  CD  . GLU B 1 121 ? 23.27000  1.22300   44.51600 1.000 63.78000 ? 115 GLU B CD  1 
ATOM   3539 O  OE1 . GLU B 1 121 ? 22.63700  0.65700   45.44900 1.000 66.01000 ? 115 GLU B OE1 1 
ATOM   3540 O  OE2 . GLU B 1 121 ? 22.98600  2.37700   44.07700 1.000 61.15000 ? 115 GLU B OE2 1 
ATOM   3541 N  N   . MET B 1 122 ? 27.50900  1.29600   47.28100 1.000 39.25000 ? 116 MET B N   1 
ATOM   3542 C  CA  . MET B 1 122 ? 27.91900  1.10000   48.66900 1.000 38.67000 ? 116 MET B CA  1 
ATOM   3543 C  C   . MET B 1 122 ? 27.81400  2.39800   49.47000 1.000 38.45000 ? 116 MET B C   1 
ATOM   3544 O  O   . MET B 1 122 ? 27.34400  2.39000   50.61500 1.000 36.41000 ? 116 MET B O   1 
ATOM   3545 C  CB  . MET B 1 122 ? 29.34100  0.52800   48.69200 1.000 40.31000 ? 116 MET B CB  1 
ATOM   3546 C  CG  . MET B 1 122 ? 29.44100  -0.87400  49.33900 1.000 51.80000 ? 116 MET B CG  1 
ATOM   3547 S  SD  . MET B 1 122 ? 28.11700  -2.05000  48.91800 1.000 67.67000 ? 116 MET B SD  1 
ATOM   3548 C  CE  . MET B 1 122 ? 27.54700  -2.55900  50.55800 1.000 50.96000 ? 116 MET B CE  1 
ATOM   3549 N  N   . VAL B 1 123 ? 28.22600  3.52800   48.87900 1.000 34.03000 ? 117 VAL B N   1 
ATOM   3550 C  CA  . VAL B 1 123 ? 28.11200  4.82200   49.56200 1.000 36.44000 ? 117 VAL B CA  1 
ATOM   3551 C  C   . VAL B 1 123 ? 26.64900  5.19000   49.74300 1.000 35.31000 ? 117 VAL B C   1 
ATOM   3552 O  O   . VAL B 1 123 ? 26.21000  5.61200   50.82500 1.000 36.65000 ? 117 VAL B O   1 
ATOM   3553 C  CB  . VAL B 1 123 ? 28.86500  5.91700   48.78300 1.000 32.58000 ? 117 VAL B CB  1 
ATOM   3554 C  CG1 . VAL B 1 123 ? 28.67900  7.32700   49.43800 1.000 29.08000 ? 117 VAL B CG1 1 
ATOM   3555 C  CG2 . VAL B 1 123 ? 30.34700  5.55400   48.64100 1.000 30.24000 ? 117 VAL B CG2 1 
ATOM   3556 N  N   . ASN B 1 124 ? 25.87500  5.03800   48.67900 1.000 34.51000 ? 118 ASN B N   1 
ATOM   3557 C  CA  . ASN B 1 124 ? 24.46300  5.36200   48.75200 1.000 35.51000 ? 118 ASN B CA  1 
ATOM   3558 C  C   . ASN B 1 124 ? 23.76500  4.56400   49.84500 1.000 38.65000 ? 118 ASN B C   1 
ATOM   3559 O  O   . ASN B 1 124 ? 22.97900  5.11500   50.62900 1.000 35.99000 ? 118 ASN B O   1 
ATOM   3560 C  CB  . ASN B 1 124 ? 23.81900  5.11100   47.40300 1.000 34.45000 ? 118 ASN B CB  1 
ATOM   3561 C  CG  . ASN B 1 124 ? 22.76300  6.10000   47.13500 1.000 40.93000 ? 118 ASN B CG  1 
ATOM   3562 O  OD1 . ASN B 1 124 ? 23.03300  7.32100   47.13900 1.000 39.66000 ? 118 ASN B OD1 1 
ATOM   3563 N  ND2 . ASN B 1 124 ? 21.52600  5.62300   47.00100 1.000 42.51000 ? 118 ASN B ND2 1 
ATOM   3564 N  N   . ARG B 1 125 ? 24.05000  3.25900   49.90900 1.000 37.27000 ? 119 ARG B N   1 
ATOM   3565 C  CA  . ARG B 1 125 ? 23.48400  2.39600   50.93900 1.000 36.62000 ? 119 ARG B CA  1 
ATOM   3566 C  C   . ARG B 1 125 ? 23.75700  2.94500   52.33900 1.000 39.99000 ? 119 ARG B C   1 
ATOM   3567 O  O   . ARG B 1 125 ? 22.85800  2.98600   53.19700 1.000 38.17000 ? 119 ARG B O   1 
ATOM   3568 C  CB  . ARG B 1 125 ? 24.07700  1.00000   50.74000 1.000 41.51000 ? 119 ARG B CB  1 
ATOM   3569 C  CG  . ARG B 1 125 ? 23.66400  -0.09900  51.67800 1.000 50.48000 ? 119 ARG B CG  1 
ATOM   3570 C  CD  . ARG B 1 125 ? 24.15500  -1.43300  51.07100 1.000 55.55000 ? 119 ARG B CD  1 
ATOM   3571 N  NE  . ARG B 1 125 ? 24.19400  -1.38000  49.60600 1.000 56.97000 ? 119 ARG B NE  1 
ATOM   3572 C  CZ  . ARG B 1 125 ? 23.19500  -1.73800  48.80200 1.000 58.46000 ? 119 ARG B CZ  1 
ATOM   3573 N  NH1 . ARG B 1 125 ? 22.05000  -2.20600  49.28200 1.000 56.85000 ? 119 ARG B NH1 1 
ATOM   3574 N  NH2 . ARG B 1 125 ? 23.34500  -1.62200  47.48400 1.000 56.62000 ? 119 ARG B NH2 1 
ATOM   3575 N  N   . SER B 1 126 ? 24.99200  3.39200   52.58100 1.000 36.37000 ? 120 SER B N   1 
ATOM   3576 C  CA  . SER B 1 126 ? 25.31500  3.98100   53.87100 1.000 36.72000 ? 120 SER B CA  1 
ATOM   3577 C  C   . SER B 1 126 ? 24.54100  5.27800   54.09400 1.000 43.31000 ? 120 SER B C   1 
ATOM   3578 O  O   . SER B 1 126 ? 23.99900  5.50400   55.18100 1.000 45.04000 ? 120 SER B O   1 
ATOM   3579 C  CB  . SER B 1 126 ? 26.81900  4.21600   53.96600 1.000 44.93000 ? 120 SER B CB  1 
ATOM   3580 O  OG  . SER B 1 126 ? 27.09800  5.26300   54.88400 1.000 54.65000 ? 120 SER B OG  1 
ATOM   3581 N  N   . TRP B 1 127 ? 24.47100  6.13900   53.07200 1.000 39.48000 ? 121 TRP B N   1 
ATOM   3582 C  CA  . TRP B 1 127 ? 23.70200  7.37300   53.19200 1.000 36.46000 ? 121 TRP B CA  1 
ATOM   3583 C  C   . TRP B 1 127 ? 22.24600  7.09500   53.55500 1.000 40.82000 ? 121 TRP B C   1 
ATOM   3584 O  O   . TRP B 1 127 ? 21.66700  7.79200   54.39700 1.000 40.08000 ? 121 TRP B O   1 
ATOM   3585 C  CB  . TRP B 1 127 ? 23.77500  8.14400   51.88000 1.000 35.59000 ? 121 TRP B CB  1 
ATOM   3586 C  CG  . TRP B 1 127 ? 25.09200  8.79700   51.61400 1.000 37.13000 ? 121 TRP B CG  1 
ATOM   3587 C  CD1 . TRP B 1 127 ? 26.19900  8.77900   52.40900 1.000 35.96000 ? 121 TRP B CD1 1 
ATOM   3588 C  CD2 . TRP B 1 127 ? 25.43300  9.58700   50.46800 1.000 35.48000 ? 121 TRP B CD2 1 
ATOM   3589 N  NE1 . TRP B 1 127 ? 27.21500  9.51300   51.82700 1.000 31.74000 ? 121 TRP B NE1 1 
ATOM   3590 C  CE2 . TRP B 1 127 ? 26.76900  10.01500  50.63400 1.000 34.64000 ? 121 TRP B CE2 1 
ATOM   3591 C  CE3 . TRP B 1 127 ? 24.73800  9.97100   49.31800 1.000 30.38000 ? 121 TRP B CE3 1 
ATOM   3592 C  CZ2 . TRP B 1 127 ? 27.42300  10.80700  49.69900 1.000 32.62000 ? 121 TRP B CZ2 1 
ATOM   3593 C  CZ3 . TRP B 1 127 ? 25.39500  10.77300  48.39100 1.000 33.93000 ? 121 TRP B CZ3 1 
ATOM   3594 C  CH2 . TRP B 1 127 ? 26.72200  11.17500  48.58900 1.000 31.28000 ? 121 TRP B CH2 1 
ATOM   3595 N  N   . ILE B 1 128 ? 21.63600  6.09300   52.91300 1.000 38.09000 ? 122 ILE B N   1 
ATOM   3596 C  CA  . ILE B 1 128 ? 20.23200  5.77000   53.15900 1.000 39.32000 ? 122 ILE B CA  1 
ATOM   3597 C  C   . ILE B 1 128 ? 20.02300  5.34700   54.60600 1.000 43.74000 ? 122 ILE B C   1 
ATOM   3598 O  O   . ILE B 1 128 ? 19.03900  5.74100   55.25500 1.000 47.26000 ? 122 ILE B O   1 
ATOM   3599 C  CB  . ILE B 1 128 ? 19.76600  4.67700   52.18100 1.000 34.53000 ? 122 ILE B CB  1 
ATOM   3600 C  CG1 . ILE B 1 128 ? 19.71500  5.24900   50.76800 1.000 36.65000 ? 122 ILE B CG1 1 
ATOM   3601 C  CG2 . ILE B 1 128 ? 18.42300  4.10700   52.60000 1.000 34.25000 ? 122 ILE B CG2 1 
ATOM   3602 C  CD1 . ILE B 1 128 ? 19.56000  4.17800   49.68500 1.000 39.54000 ? 122 ILE B CD1 1 
ATOM   3603 N  N   . LYS B 1 129 ? 20.94000  4.53800   55.13800 1.000 43.02000 ? 123 LYS B N   1 
ATOM   3604 C  CA  . LYS B 1 129 ? 20.76800  4.05000   56.50000 1.000 40.57000 ? 123 LYS B CA  1 
ATOM   3605 C  C   . LYS B 1 129 ? 20.75500  5.19700   57.50800 1.000 50.93000 ? 123 LYS B C   1 
ATOM   3606 O  O   . LYS B 1 129 ? 20.05700  5.12300   58.53100 1.000 51.54000 ? 123 LYS B O   1 
ATOM   3607 C  CB  . LYS B 1 129 ? 21.87100  3.04300   56.82200 1.000 40.54000 ? 123 LYS B CB  1 
ATOM   3608 C  CG  . LYS B 1 129 ? 21.38100  1.76700   57.48600 1.000 50.79000 ? 123 LYS B CG  1 
ATOM   3609 C  CD  . LYS B 1 129 ? 22.28900  0.60900   57.14400 1.000 47.21000 ? 123 LYS B CD  1 
ATOM   3610 C  CE  . LYS B 1 129 ? 22.74200  0.74200   55.70500 1.000 40.28000 ? 123 LYS B CE  1 
ATOM   3611 N  NZ  . LYS B 1 129 ? 23.17900  -0.58100  55.14600 1.000 49.05000 ? 123 LYS B NZ  1 
ATOM   3612 N  N   . GLN B 1 130 ? 21.49400  6.27300   57.22800 1.000 47.83000 ? 124 GLN B N   1 
ATOM   3613 C  CA  . GLN B 1 130 ? 21.58000  7.41500   58.12800 1.000 49.96000 ? 124 GLN B CA  1 
ATOM   3614 C  C   . GLN B 1 130 ? 20.64000  8.55300   57.75200 1.000 50.62000 ? 124 GLN B C   1 
ATOM   3615 O  O   . GLN B 1 130 ? 20.70600  9.61700   58.37000 1.000 55.39000 ? 124 GLN B O   1 
ATOM   3616 C  CB  . GLN B 1 130 ? 23.01400  7.92400   58.16300 1.000 47.69000 ? 124 GLN B CB  1 
ATOM   3617 C  CG  . GLN B 1 130 ? 24.02300  6.79900   58.16700 1.000 52.21000 ? 124 GLN B CG  1 
ATOM   3618 C  CD  . GLN B 1 130 ? 25.42500  7.29200   57.88400 1.000 66.66000 ? 124 GLN B CD  1 
ATOM   3619 O  OE1 . GLN B 1 130 ? 25.66900  8.50600   57.82300 1.000 65.76000 ? 124 GLN B OE1 1 
ATOM   3620 N  NE2 . GLN B 1 130 ? 26.36100  6.35200   57.69100 1.000 67.07000 ? 124 GLN B NE2 1 
ATOM   3621 N  N   . ASP B 1 131 ? 19.77300  8.36200   56.75500 1.000 52.40000 ? 125 ASP B N   1 
ATOM   3622 C  CA  . ASP B 1 131 ? 18.90000  9.42700   56.24600 1.000 53.03000 ? 125 ASP B CA  1 
ATOM   3623 C  C   . ASP B 1 131 ? 19.69900  10.66400  55.83400 1.000 54.69000 ? 125 ASP B C   1 
ATOM   3624 O  O   . ASP B 1 131 ? 19.22000  11.78900  55.97600 1.000 53.13000 ? 125 ASP B O   1 
ATOM   3625 C  CB  . ASP B 1 131 ? 17.82100  9.81700   57.26300 1.000 54.73000 ? 125 ASP B CB  1 
ATOM   3626 C  CG  . ASP B 1 131 ? 16.79700  8.71900   57.48200 1.000 59.28000 ? 125 ASP B CG  1 
ATOM   3627 O  OD1 . ASP B 1 131 ? 15.94900  8.48200   56.57900 1.000 60.11000 ? 125 ASP B OD1 1 
ATOM   3628 O  OD2 . ASP B 1 131 ? 16.86200  8.08000   58.55600 1.000 57.47000 ? 125 ASP B OD2 1 
ATOM   3629 N  N   . PHE B 1 132 ? 20.91000  10.45800  55.31500 1.000 47.00000 ? 126 PHE B N   1 
ATOM   3630 C  CA  . PHE B 1 132 ? 21.77500  11.55800  54.90500 1.000 49.19000 ? 126 PHE B CA  1 
ATOM   3631 C  C   . PHE B 1 132 ? 21.28700  12.16900  53.59700 1.000 47.93000 ? 126 PHE B C   1 
ATOM   3632 O  O   . PHE B 1 132 ? 21.00400  11.45800  52.62400 1.000 46.44000 ? 126 PHE B O   1 
ATOM   3633 C  CB  . PHE B 1 132 ? 23.21500  11.07400  54.75100 1.000 44.07000 ? 126 PHE B CB  1 
ATOM   3634 C  CG  . PHE B 1 132 ? 24.17500  12.14300  54.30600 1.000 43.41000 ? 126 PHE B CG  1 
ATOM   3635 C  CD1 . PHE B 1 132 ? 24.38300  13.27300  55.08400 1.000 44.62000 ? 126 PHE B CD1 1 
ATOM   3636 C  CD2 . PHE B 1 132 ? 24.90000  12.00200  53.12400 1.000 43.49000 ? 126 PHE B CD2 1 
ATOM   3637 C  CE1 . PHE B 1 132 ? 25.27300  14.24000  54.69300 1.000 38.99000 ? 126 PHE B CE1 1 
ATOM   3638 C  CE2 . PHE B 1 132 ? 25.79800  12.97300  52.71000 1.000 42.08000 ? 126 PHE B CE2 1 
ATOM   3639 C  CZ  . PHE B 1 132 ? 25.98300  14.09400  53.48500 1.000 45.94000 ? 126 PHE B CZ  1 
ATOM   3640 N  N   . ILE B 1 133 ? 21.19600  13.49400  53.57400 1.000 47.58000 ? 127 ILE B N   1 
ATOM   3641 C  CA  . ILE B 1 133 ? 20.80600  14.23400  52.37800 1.000 43.26000 ? 127 ILE B CA  1 
ATOM   3642 C  C   . ILE B 1 133 ? 22.07100  14.85200  51.79500 1.000 40.12000 ? 127 ILE B C   1 
ATOM   3643 O  O   . ILE B 1 133 ? 22.67900  15.71700  52.44600 1.000 39.89000 ? 127 ILE B O   1 
ATOM   3644 C  CB  . ILE B 1 133 ? 19.75100  15.30300  52.69400 1.000 47.44000 ? 127 ILE B CB  1 
ATOM   3645 C  CG1 . ILE B 1 133 ? 18.34200  14.69500  52.67900 1.000 50.60000 ? 127 ILE B CG1 1 
ATOM   3646 C  CG2 . ILE B 1 133 ? 19.84700  16.47700  51.69900 1.000 48.29000 ? 127 ILE B CG2 1 
ATOM   3647 C  CD1 . ILE B 1 133 ? 18.09700  13.60300  53.69700 1.000 56.96000 ? 127 ILE B CD1 1 
ATOM   3648 N  N   . PRO B 1 134 ? 22.53100  14.41700  50.62000 1.000 39.07000 ? 128 PRO B N   1 
ATOM   3649 C  CA  . PRO B 1 134 ? 23.76300  14.97800  50.04900 1.000 36.86000 ? 128 PRO B CA  1 
ATOM   3650 C  C   . PRO B 1 134 ? 23.64800  16.47400  49.78800 1.000 38.19000 ? 128 PRO B C   1 
ATOM   3651 O  O   . PRO B 1 134 ? 22.57000  16.99600  49.48500 1.000 35.73000 ? 128 PRO B O   1 
ATOM   3652 C  CB  . PRO B 1 134 ? 23.94600  14.20200  48.73500 1.000 35.37000 ? 128 PRO B CB  1 
ATOM   3653 C  CG  . PRO B 1 134 ? 22.66500  13.39800  48.54400 1.000 31.55000 ? 128 PRO B CG  1 
ATOM   3654 C  CD  . PRO B 1 134 ? 22.02500  13.25200  49.87500 1.000 35.47000 ? 128 PRO B CD  1 
ATOM   3655 N  N   . THR B 1 135 ? 24.78700  17.16200  49.91700 1.000 35.25000 ? 129 THR B N   1 
ATOM   3656 C  CA  . THR B 1 135 ? 24.89100  18.61100  49.75200 1.000 37.09000 ? 129 THR B CA  1 
ATOM   3657 C  C   . THR B 1 135 ? 25.88700  18.92200  48.63700 1.000 36.25000 ? 129 THR B C   1 
ATOM   3658 O  O   . THR B 1 135 ? 26.46200  18.01600  48.02800 1.000 30.42000 ? 129 THR B O   1 
ATOM   3659 C  CB  . THR B 1 135 ? 25.29400  19.29900  51.06400 1.000 32.18000 ? 129 THR B CB  1 
ATOM   3660 O  OG1 . THR B 1 135 ? 26.66600  19.03600  51.35100 1.000 36.67000 ? 129 THR B OG1 1 
ATOM   3661 C  CG2 . THR B 1 135 ? 24.49400  18.76800  52.20400 1.000 36.52000 ? 129 THR B CG2 1 
ATOM   3662 N  N   . ALA B 1 136 ? 26.10400  20.22600  48.39200 1.000 35.47000 ? 130 ALA B N   1 
ATOM   3663 C  CA  . ALA B 1 136 ? 26.94100  20.65800  47.27100 1.000 32.69000 ? 130 ALA B CA  1 
ATOM   3664 C  C   . ALA B 1 136 ? 28.31200  20.01000  47.33100 1.000 30.01000 ? 130 ALA B C   1 
ATOM   3665 O  O   . ALA B 1 136 ? 28.85700  19.57800  46.30100 1.000 32.07000 ? 130 ALA B O   1 
ATOM   3666 C  CB  . ALA B 1 136 ? 27.08300  22.18600  47.27000 1.000 29.75000 ? 130 ALA B CB  1 
ATOM   3667 N  N   . VAL B 1 137 ? 28.87700  19.91400  48.53900 1.000 32.18000 ? 131 VAL B N   1 
ATOM   3668 C  CA  . VAL B 1 137 ? 30.22900  19.39900  48.73500 1.000 31.46000 ? 131 VAL B CA  1 
ATOM   3669 C  C   . VAL B 1 137 ? 30.32800  17.91700  48.40000 1.000 34.92000 ? 131 VAL B C   1 
ATOM   3670 O  O   . VAL B 1 137 ? 31.43300  17.39100  48.22200 1.000 35.92000 ? 131 VAL B O   1 
ATOM   3671 C  CB  . VAL B 1 137 ? 30.64700  19.72400  50.18500 1.000 34.22000 ? 131 VAL B CB  1 
ATOM   3672 C  CG1 . VAL B 1 137 ? 29.94800  18.82200  51.16900 1.000 32.93000 ? 131 VAL B CG1 1 
ATOM   3673 C  CG2 . VAL B 1 137 ? 32.15500  19.70300  50.35600 1.000 36.30000 ? 131 VAL B CG2 1 
ATOM   3674 N  N   . CYS B 1 138 ? 29.19200  17.24200  48.26100 1.000 31.32000 ? 132 CYS B N   1 
ATOM   3675 C  CA  . CYS B 1 138 ? 29.15600  15.82200  47.93600 1.000 31.70000 ? 132 CYS B CA  1 
ATOM   3676 C  C   . CYS B 1 138 ? 29.09600  15.54800  46.44400 1.000 32.70000 ? 132 CYS B C   1 
ATOM   3677 O  O   . CYS B 1 138 ? 29.30100  14.39300  46.04200 1.000 34.26000 ? 132 CYS B O   1 
ATOM   3678 C  CB  . CYS B 1 138 ? 27.94100  15.16800  48.59000 1.000 30.11000 ? 132 CYS B CB  1 
ATOM   3679 S  SG  . CYS B 1 138 ? 27.90100  15.27000  50.38700 1.000 37.55000 ? 132 CYS B SG  1 
ATOM   3680 N  N   . SER B 1 139 ? 28.76800  16.56600  45.63500 1.000 29.72000 ? 133 SER B N   1 
ATOM   3681 C  CA  . SER B 1 139 ? 28.67000  16.42800  44.18700 1.000 30.06000 ? 133 SER B CA  1 
ATOM   3682 C  C   . SER B 1 139 ? 29.86800  15.67600  43.63900 1.000 30.86000 ? 133 SER B C   1 
ATOM   3683 O  O   . SER B 1 139 ? 31.00800  15.91900  44.04800 1.000 27.96000 ? 133 SER B O   1 
ATOM   3684 C  CB  . SER B 1 139 ? 28.59100  17.80600  43.52500 1.000 32.56000 ? 133 SER B CB  1 
ATOM   3685 O  OG  . SER B 1 139 ? 28.85000  17.74200  42.12300 1.000 31.44000 ? 133 SER B OG  1 
ATOM   3686 N  N   . ASN B 1 140 ? 29.60200  14.77200  42.69500 1.000 27.36000 ? 134 ASN B N   1 
ATOM   3687 C  CA  . ASN B 1 140 ? 30.67600  14.03500  42.04600 1.000 25.88000 ? 134 ASN B CA  1 
ATOM   3688 C  C   . ASN B 1 140 ? 31.63900  14.96300  41.31700 1.000 25.92000 ? 134 ASN B C   1 
ATOM   3689 O  O   . ASN B 1 140 ? 32.77200  14.56100  41.03000 1.000 25.94000 ? 134 ASN B O   1 
ATOM   3690 C  CB  . ASN B 1 140 ? 30.07700  12.97900  41.10300 1.000 27.28000 ? 134 ASN B CB  1 
ATOM   3691 C  CG  . ASN B 1 140 ? 29.52700  13.57200  39.80300 1.000 32.56000 ? 134 ASN B CG  1 
ATOM   3692 O  OD1 . ASN B 1 140 ? 30.22300  13.59600  38.79300 1.000 38.96000 ? 134 ASN B OD1 1 
ATOM   3693 N  ND2 . ASN B 1 140 ? 28.27700  14.00500  39.81300 1.000 31.13000 ? 134 ASN B ND2 1 
ATOM   3694 N  N   . CYS B 1 141 ? 31.24200  16.21900  41.07700 1.000 26.02000 ? 135 CYS B N   1 
ATOM   3695 C  CA  . CYS B 1 141 ? 32.04200  17.20600  40.36200 1.000 28.95000 ? 135 CYS B CA  1 
ATOM   3696 C  C   . CYS B 1 141 ? 32.55600  18.29800  41.29000 1.000 28.23000 ? 135 CYS B C   1 
ATOM   3697 O  O   . CYS B 1 141 ? 32.91400  19.38400  40.82700 1.000 29.34000 ? 135 CYS B O   1 
ATOM   3698 C  CB  . CYS B 1 141 ? 31.23400  17.83500  39.22000 1.000 31.20000 ? 135 CYS B CB  1 
ATOM   3699 S  SG  . CYS B 1 141 ? 30.45100  16.63200  38.09500 1.000 34.15000 ? 135 CYS B SG  1 
ATOM   3700 N  N   . SER B 1 142 ? 32.58200  18.02500  42.59100 1.000 24.71000 ? 136 SER B N   1 
ATOM   3701 C  CA  . SER B 1 142 ? 32.89700  19.04700  43.57300 1.000 27.58000 ? 136 SER B CA  1 
ATOM   3702 C  C   . SER B 1 142 ? 34.33000  19.54400  43.43400 1.000 28.33000 ? 136 SER B C   1 
ATOM   3703 O  O   . SER B 1 142 ? 34.59400  20.74200  43.62200 1.000 28.19000 ? 136 SER B O   1 
ATOM   3704 C  CB  . SER B 1 142 ? 32.67200  18.49500  44.97400 1.000 31.49000 ? 136 SER B CB  1 
ATOM   3705 O  OG  . SER B 1 142 ? 33.57500  17.42600  45.22800 1.000 29.41000 ? 136 SER B OG  1 
ATOM   3706 N  N   . GLY B 1 143 ? 35.28100  18.65100  43.14500 1.000 26.66000 ? 137 GLY B N   1 
ATOM   3707 C  CA  . GLY B 1 143 ? 36.66000  19.10500  43.02400 1.000 25.32000 ? 137 GLY B CA  1 
ATOM   3708 C  C   . GLY B 1 143 ? 36.85700  19.97100  41.80000 1.000 25.20000 ? 137 GLY B C   1 
ATOM   3709 O  O   . GLY B 1 143 ? 37.69900  20.86700  41.78300 1.000 23.34000 ? 137 GLY B O   1 
ATOM   3710 N  N   . HIS B 1 144 ? 36.07700  19.71700  40.76300 1.000 27.87000 ? 138 HIS B N   1 
ATOM   3711 C  CA  . HIS B 1 144 ? 36.11400  20.57900  39.59600 1.000 24.91000 ? 138 HIS B CA  1 
ATOM   3712 C  C   . HIS B 1 144 ? 35.51700  21.95500  39.89700 1.000 26.41000 ? 138 HIS B C   1 
ATOM   3713 O  O   . HIS B 1 144 ? 36.06500  22.99200  39.48100 1.000 27.25000 ? 138 HIS B O   1 
ATOM   3714 C  CB  . HIS B 1 144 ? 35.35400  19.89400  38.46500 1.000 26.92000 ? 138 HIS B CB  1 
ATOM   3715 C  CG  . HIS B 1 144 ? 35.45700  20.62800  37.18000 1.000 31.46000 ? 138 HIS B CG  1 
ATOM   3716 N  ND1 . HIS B 1 144 ? 36.57100  20.54100  36.37200 1.000 33.33000 ? 138 HIS B ND1 1 
ATOM   3717 C  CD2 . HIS B 1 144 ? 34.62700  21.52400  36.59600 1.000 37.08000 ? 138 HIS B CD2 1 
ATOM   3718 C  CE1 . HIS B 1 144 ? 36.40700  21.33500  35.32700 1.000 35.76000 ? 138 HIS B CE1 1 
ATOM   3719 N  NE2 . HIS B 1 144 ? 35.24000  21.94800  35.44200 1.000 35.52000 ? 138 HIS B NE2 1 
ATOM   3720 N  N   . HIS B 1 145 ? 34.38500  21.99600  40.60600 1.000 24.80000 ? 139 HIS B N   1 
ATOM   3721 C  CA  . HIS B 1 145 ? 33.83600  23.29300  40.99600 1.000 25.27000 ? 139 HIS B CA  1 
ATOM   3722 C  C   . HIS B 1 145 ? 34.78900  24.07700  41.89900 1.000 27.10000 ? 139 HIS B C   1 
ATOM   3723 O  O   . HIS B 1 145 ? 34.82600  25.31400  41.84300 1.000 26.67000 ? 139 HIS B O   1 
ATOM   3724 C  CB  . HIS B 1 145 ? 32.48900  23.09400  41.67200 1.000 28.00000 ? 139 HIS B CB  1 
ATOM   3725 C  CG  . HIS B 1 145 ? 31.37500  22.90300  40.69900 1.000 30.54000 ? 139 HIS B CG  1 
ATOM   3726 N  ND1 . HIS B 1 145 ? 30.40100  23.85800  40.49000 1.000 32.72000 ? 139 HIS B ND1 1 
ATOM   3727 C  CD2 . HIS B 1 145 ? 31.09800  21.88600  39.84800 1.000 28.74000 ? 139 HIS B CD2 1 
ATOM   3728 C  CE1 . HIS B 1 145 ? 29.55200  23.42000  39.57600 1.000 32.33000 ? 139 HIS B CE1 1 
ATOM   3729 N  NE2 . HIS B 1 145 ? 29.95500  22.22900  39.16600 1.000 31.47000 ? 139 HIS B NE2 1 
ATOM   3730 N  N   . VAL B 1 146 ? 35.58100  23.40200  42.72600 1.000 22.36000 ? 140 VAL B N   1 
ATOM   3731 C  CA  . VAL B 1 146 ? 36.51000  24.16800  43.54700 1.000 25.61000 ? 140 VAL B CA  1 
ATOM   3732 C  C   . VAL B 1 146 ? 37.62700  24.73400  42.67600 1.000 27.40000 ? 140 VAL B C   1 
ATOM   3733 O  O   . VAL B 1 146 ? 38.10300  25.85600  42.89600 1.000 26.75000 ? 140 VAL B O   1 
ATOM   3734 C  CB  . VAL B 1 146 ? 37.05900  23.31200  44.70400 1.000 23.56000 ? 140 VAL B CB  1 
ATOM   3735 C  CG1 . VAL B 1 146 ? 38.12800  24.07500  45.45200 1.000 26.57000 ? 140 VAL B CG1 1 
ATOM   3736 C  CG2 . VAL B 1 146 ? 35.95000  22.96300  45.63500 1.000 26.26000 ? 140 VAL B CG2 1 
ATOM   3737 N  N   . GLY B 1 147 ? 38.05900  23.96400  41.67600 1.000 25.90000 ? 141 GLY B N   1 
ATOM   3738 C  CA  . GLY B 1 147 ? 39.02300  24.47700  40.71800 1.000 21.52000 ? 141 GLY B CA  1 
ATOM   3739 C  C   . GLY B 1 147 ? 38.53700  25.73300  40.02300 1.000 26.51000 ? 141 GLY B C   1 
ATOM   3740 O  O   . GLY B 1 147 ? 39.27700  26.70700  39.89500 1.000 21.69000 ? 141 GLY B O   1 
ATOM   3741 N  N   . MET B 1 148 ? 37.28100  25.72700  39.56500 1.000 26.39000 ? 142 MET B N   1 
ATOM   3742 C  CA  . MET B 1 148 ? 36.71400  26.90200  38.91200 1.000 25.30000 ? 142 MET B CA  1 
ATOM   3743 C  C   . MET B 1 148 ? 36.67400  28.10100  39.85500 1.000 27.28000 ? 142 MET B C   1 
ATOM   3744 O  O   . MET B 1 148 ? 36.98700  29.23200  39.44900 1.000 29.58000 ? 142 MET B O   1 
ATOM   3745 C  CB  . MET B 1 148 ? 35.30900  26.59100  38.38900 1.000 22.61000 ? 142 MET B CB  1 
ATOM   3746 C  CG  . MET B 1 148 ? 35.27000  25.62100  37.22700 1.000 27.97000 ? 142 MET B CG  1 
ATOM   3747 S  SD  . MET B 1 148 ? 35.98200  26.33400  35.73700 1.000 33.21000 ? 142 MET B SD  1 
ATOM   3748 C  CE  . MET B 1 148 ? 36.69100  24.86600  35.01000 1.000 36.53000 ? 142 MET B CE  1 
ATOM   3749 N  N   . LEU B 1 149 ? 36.28300  27.88300  41.11400 1.000 26.01000 ? 143 LEU B N   1 
ATOM   3750 C  CA  . LEU B 1 149 ? 36.35400  28.95500  42.11300 1.000 27.22000 ? 143 LEU B CA  1 
ATOM   3751 C  C   . LEU B 1 149 ? 37.78200  29.46100  42.29700 1.000 29.49000 ? 143 LEU B C   1 
ATOM   3752 O  O   . LEU B 1 149 ? 38.01700  30.67800  42.42300 1.000 27.55000 ? 143 LEU B O   1 
ATOM   3753 C  CB  . LEU B 1 149 ? 35.81400  28.44200  43.44200 1.000 26.12000 ? 143 LEU B CB  1 
ATOM   3754 C  CG  . LEU B 1 149 ? 34.30900  28.36400  43.62000 1.000 32.38000 ? 143 LEU B CG  1 
ATOM   3755 C  CD1 . LEU B 1 149 ? 33.98600  27.55100  44.87600 1.000 32.31000 ? 143 LEU B CD1 1 
ATOM   3756 C  CD2 . LEU B 1 149 ? 33.74700  29.75400  43.73700 1.000 30.85000 ? 143 LEU B CD2 1 
ATOM   3757 N  N   . ALA B 1 150 ? 38.75100  28.53800  42.33800 1.000 26.50000 ? 144 ALA B N   1 
ATOM   3758 C  CA  . ALA B 1 150 ? 40.14400  28.93900  42.49300 1.000 27.32000 ? 144 ALA B CA  1 
ATOM   3759 C  C   . ALA B 1 150 ? 40.57200  29.83700  41.34400 1.000 26.06000 ? 144 ALA B C   1 
ATOM   3760 O  O   . ALA B 1 150 ? 41.15800  30.90300  41.55600 1.000 29.28000 ? 144 ALA B O   1 
ATOM   3761 C  CB  . ALA B 1 150 ? 41.03000  27.70300  42.58500 1.000 28.24000 ? 144 ALA B CB  1 
ATOM   3762 N  N   . GLY B 1 151 ? 40.23200  29.44700  40.11900 1.000 27.32000 ? 145 GLY B N   1 
ATOM   3763 C  CA  . GLY B 1 151 ? 40.57600  30.26800  38.97000 1.000 30.54000 ? 145 GLY B CA  1 
ATOM   3764 C  C   . GLY B 1 151 ? 39.94500  31.64600  39.01700 1.000 29.59000 ? 145 GLY B C   1 
ATOM   3765 O  O   . GLY B 1 151 ? 40.60700  32.65300  38.73600 1.000 25.60000 ? 145 GLY B O   1 
ATOM   3766 N  N   . ALA B 1 152 ? 38.65600  31.71300  39.35600 1.000 27.54000 ? 146 ALA B N   1 
ATOM   3767 C  CA  . ALA B 1 152 ? 37.99200  33.01000  39.46400 1.000 30.27000 ? 146 ALA B CA  1 
ATOM   3768 C  C   . ALA B 1 152 ? 38.69600  33.90500  40.47500 1.000 32.22000 ? 146 ALA B C   1 
ATOM   3769 O  O   . ALA B 1 152 ? 38.91700  35.09600  40.20900 1.000 34.07000 ? 146 ALA B O   1 
ATOM   3770 C  CB  . ALA B 1 152 ? 36.51600  32.82500  39.83800 1.000 31.17000 ? 146 ALA B CB  1 
ATOM   3771 N  N   . ARG B 1 153 ? 39.07600  33.34900  41.63600 1.000 28.65000 ? 147 ARG B N   1 
ATOM   3772 C  CA  . ARG B 1 153 ? 39.72600  34.17300  42.65500 1.000 29.26000 ? 147 ARG B CA  1 
ATOM   3773 C  C   . ARG B 1 153 ? 41.10400  34.61400  42.19900 1.000 30.70000 ? 147 ARG B C   1 
ATOM   3774 O  O   . ARG B 1 153 ? 41.50600  35.76500  42.43700 1.000 32.04000 ? 147 ARG B O   1 
ATOM   3775 C  CB  . ARG B 1 153 ? 39.83300  33.42300  43.98300 1.000 27.95000 ? 147 ARG B CB  1 
ATOM   3776 C  CG  . ARG B 1 153 ? 38.51400  33.36300  44.74500 1.000 40.13000 ? 147 ARG B CG  1 
ATOM   3777 C  CD  . ARG B 1 153 ? 38.59500  34.04500  46.11800 1.000 42.64000 ? 147 ARG B CD  1 
ATOM   3778 N  NE  . ARG B 1 153 ? 37.26500  34.24800  46.69500 1.000 51.30000 ? 147 ARG B NE  1 
ATOM   3779 C  CZ  . ARG B 1 153 ? 36.77200  33.56600  47.72600 1.000 51.35000 ? 147 ARG B CZ  1 
ATOM   3780 N  NH1 . ARG B 1 153 ? 37.49100  32.64700  48.35400 1.000 48.55000 ? 147 ARG B NH1 1 
ATOM   3781 N  NH2 . ARG B 1 153 ? 35.52800  33.81600  48.14200 1.000 48.84000 ? 147 ARG B NH2 1 
ATOM   3782 N  N   . ALA B 1 154 ? 41.82200  33.72100  41.50900 1.000 28.41000 ? 148 ALA B N   1 
ATOM   3783 C  CA  . ALA B 1 154 ? 43.20300  34.01100  41.12500 1.000 29.59000 ? 148 ALA B CA  1 
ATOM   3784 C  C   . ALA B 1 154 ? 43.27700  35.22800  40.22400 1.000 29.41000 ? 148 ALA B C   1 
ATOM   3785 O  O   . ALA B 1 154 ? 44.18700  36.06300  40.36100 1.000 32.17000 ? 148 ALA B O   1 
ATOM   3786 C  CB  . ALA B 1 154 ? 43.82000  32.79700  40.43800 1.000 26.75000 ? 148 ALA B CB  1 
ATOM   3787 N  N   . ILE B 1 155 ? 42.30300  35.38200  39.32700 1.000 25.27000 ? 149 ILE B N   1 
ATOM   3788 C  CA  . ILE B 1 155 ? 42.36000  36.47300  38.36400 1.000 28.48000 ? 149 ILE B CA  1 
ATOM   3789 C  C   . ILE B 1 155 ? 41.54800  37.67800  38.80300 1.000 29.98000 ? 149 ILE B C   1 
ATOM   3790 O  O   . ILE B 1 155 ? 41.51700  38.69400  38.08200 1.000 31.31000 ? 149 ILE B O   1 
ATOM   3791 C  CB  . ILE B 1 155 ? 41.91300  35.99600  36.96700 1.000 32.09000 ? 149 ILE B CB  1 
ATOM   3792 C  CG1 . ILE B 1 155 ? 40.49800  35.43000  37.00900 1.000 27.21000 ? 149 ILE B CG1 1 
ATOM   3793 C  CG2 . ILE B 1 155 ? 42.96200  35.01700  36.36300 1.000 26.57000 ? 149 ILE B CG2 1 
ATOM   3794 C  CD1 . ILE B 1 155 ? 39.95900  34.93700  35.65000 1.000 28.82000 ? 149 ILE B CD1 1 
ATOM   3795 N  N   . GLY B 1 156 ? 40.92300  37.61900  39.98200 1.000 32.79000 ? 150 GLY B N   1 
ATOM   3796 C  CA  . GLY B 1 156 ? 40.18200  38.75700  40.50000 1.000 32.25000 ? 150 GLY B CA  1 
ATOM   3797 C  C   . GLY B 1 156 ? 38.81000  38.93200  39.89300 1.000 36.86000 ? 150 GLY B C   1 
ATOM   3798 O  O   . GLY B 1 156 ? 38.27700  40.04500  39.89800 1.000 33.90000 ? 150 GLY B O   1 
ATOM   3799 N  N   . ALA B 1 157 ? 38.22900  37.85600  39.36200 1.000 40.69000 ? 151 ALA B N   1 
ATOM   3800 C  CA  . ALA B 1 157 ? 36.92500  37.91200  38.70900 1.000 46.19000 ? 151 ALA B CA  1 
ATOM   3801 C  C   . ALA B 1 157 ? 35.76900  37.91300  39.70000 1.000 52.75000 ? 151 ALA B C   1 
ATOM   3802 O  O   . ALA B 1 157 ? 34.70400  38.47400  39.40400 1.000 54.86000 ? 151 ALA B O   1 
ATOM   3803 C  CB  . ALA B 1 157 ? 36.77100  36.71700  37.76300 1.000 35.41000 ? 151 ALA B CB  1 
ATOM   3804 N  N   . GLY B 1 158 ? 35.94400  37.27500  40.85900 1.000 46.80000 ? 152 GLY B N   1 
ATOM   3805 C  CA  . GLY B 1 158 ? 34.84500  37.14600  41.78900 1.000 44.80000 ? 152 GLY B CA  1 
ATOM   3806 C  C   . GLY B 1 158 ? 34.17600  35.79200  41.66700 1.000 48.84000 ? 152 GLY B C   1 
ATOM   3807 O  O   . GLY B 1 158 ? 34.04100  35.25200  40.56100 1.000 40.97000 ? 152 GLY B O   1 
ATOM   3808 N  N   . THR B 1 159 ? 33.75300  35.24100  42.81200 1.000 46.92000 ? 153 THR B N   1 
ATOM   3809 C  CA  . THR B 1 159 ? 33.23700  33.88000  42.86700 1.000 48.97000 ? 153 THR B CA  1 
ATOM   3810 C  C   . THR B 1 159 ? 31.76800  33.79100  42.47300 1.000 46.99000 ? 153 THR B C   1 
ATOM   3811 O  O   . THR B 1 159 ? 31.34100  32.75300  41.95900 1.000 44.69000 ? 153 THR B O   1 
ATOM   3812 C  CB  . THR B 1 159 ? 33.43900  33.30400  44.26700 1.000 48.79000 ? 153 THR B CB  1 
ATOM   3813 O  OG1 . THR B 1 159 ? 32.75300  34.12000  45.22700 1.000 51.21000 ? 153 THR B OG1 1 
ATOM   3814 C  CG2 . THR B 1 159 ? 34.91600  33.27400  44.59100 1.000 45.06000 ? 153 THR B CG2 1 
ATOM   3815 N  N   . ASP B 1 160 ? 30.98500  34.84000  42.70600 1.000 46.59000 ? 154 ASP B N   1 
ATOM   3816 C  CA  . ASP B 1 160 ? 29.61500  34.86500  42.20600 1.000 50.73000 ? 154 ASP B CA  1 
ATOM   3817 C  C   . ASP B 1 160 ? 29.61000  34.60400  40.70300 1.000 51.42000 ? 154 ASP B C   1 
ATOM   3818 O  O   . ASP B 1 160 ? 30.32200  35.27300  39.94000 1.000 51.40000 ? 154 ASP B O   1 
ATOM   3819 C  CB  . ASP B 1 160 ? 28.95200  36.21800  42.49100 1.000 52.68000 ? 154 ASP B CB  1 
ATOM   3820 C  CG  . ASP B 1 160 ? 29.00100  36.61000  43.96000 1.000 64.26000 ? 154 ASP B CG  1 
ATOM   3821 O  OD1 . ASP B 1 160 ? 28.37800  35.91500  44.79600 1.000 54.47000 ? 154 ASP B OD1 1 
ATOM   3822 O  OD2 . ASP B 1 160 ? 29.67300  37.62500  44.27300 1.000 73.77000 ? 154 ASP B OD2 1 
ATOM   3823 N  N   . GLY B 1 161 ? 28.81800  33.61400  40.28300 1.000 43.26000 ? 155 GLY B N   1 
ATOM   3824 C  CA  . GLY B 1 161 ? 28.62400  33.34300  38.87100 1.000 37.38000 ? 155 GLY B CA  1 
ATOM   3825 C  C   . GLY B 1 161 ? 29.75600  32.64200  38.14500 1.000 35.35000 ? 155 GLY B C   1 
ATOM   3826 O  O   . GLY B 1 161 ? 29.73500  32.61700  36.90800 1.000 32.89000 ? 155 GLY B O   1 
ATOM   3827 N  N   . TYR B 1 162 ? 30.73900  32.05900  38.85600 1.000 35.53000 ? 156 TYR B N   1 
ATOM   3828 C  CA  . TYR B 1 162 ? 31.81300  31.32200  38.18100 1.000 35.82000 ? 156 TYR B CA  1 
ATOM   3829 C  C   . TYR B 1 162 ? 31.27700  30.26000  37.22400 1.000 33.78000 ? 156 TYR B C   1 
ATOM   3830 O  O   . TYR B 1 162 ? 31.95800  29.89500  36.26000 1.000 33.35000 ? 156 TYR B O   1 
ATOM   3831 C  CB  . TYR B 1 162 ? 32.73800  30.65100  39.20700 1.000 35.45000 ? 156 TYR B CB  1 
ATOM   3832 C  CG  . TYR B 1 162 ? 32.15300  29.43000  39.91100 1.000 28.78000 ? 156 TYR B CG  1 
ATOM   3833 C  CD1 . TYR B 1 162 ? 31.38800  29.56300  41.05100 1.000 36.36000 ? 156 TYR B CD1 1 
ATOM   3834 C  CD2 . TYR B 1 162 ? 32.38300  28.15500  39.43600 1.000 34.03000 ? 156 TYR B CD2 1 
ATOM   3835 C  CE1 . TYR B 1 162 ? 30.85100  28.45600  41.70600 1.000 32.54000 ? 156 TYR B CE1 1 
ATOM   3836 C  CE2 . TYR B 1 162 ? 31.85000  27.04800  40.06600 1.000 32.21000 ? 156 TYR B CE2 1 
ATOM   3837 C  CZ  . TYR B 1 162 ? 31.08900  27.20000  41.20600 1.000 34.73000 ? 156 TYR B CZ  1 
ATOM   3838 O  OH  . TYR B 1 162 ? 30.56200  26.08600  41.84100 1.000 33.52000 ? 156 TYR B OH  1 
ATOM   3839 N  N   . HIS B 1 163 ? 30.06900  29.77500  37.46000 1.000 28.94000 ? 157 HIS B N   1 
ATOM   3840 C  CA  . HIS B 1 163 ? 29.46800  28.69500  36.69300 1.000 35.33000 ? 157 HIS B CA  1 
ATOM   3841 C  C   . HIS B 1 163 ? 28.69600  29.18100  35.47100 1.000 37.61000 ? 157 HIS B C   1 
ATOM   3842 O  O   . HIS B 1 163 ? 28.19300  28.34700  34.70300 1.000 34.48000 ? 157 HIS B O   1 
ATOM   3843 C  CB  . HIS B 1 163 ? 28.53200  27.90300  37.59800 1.000 32.76000 ? 157 HIS B CB  1 
ATOM   3844 C  CG  . HIS B 1 163 ? 27.37600  28.71600  38.08600 1.000 38.38000 ? 157 HIS B CG  1 
ATOM   3845 N  ND1 . HIS B 1 163 ? 27.53700  29.96100  38.65800 1.000 35.71000 ? 157 HIS B ND1 1 
ATOM   3846 C  CD2 . HIS B 1 163 ? 26.04000  28.48000  38.07100 1.000 36.51000 ? 157 HIS B CD2 1 
ATOM   3847 C  CE1 . HIS B 1 163 ? 26.35600  30.45600  38.97900 1.000 33.72000 ? 157 HIS B CE1 1 
ATOM   3848 N  NE2 . HIS B 1 163 ? 25.43200  29.57800  38.63400 1.000 39.53000 ? 157 HIS B NE2 1 
ATOM   3849 N  N   . LEU B 1 164 ? 28.58700  30.49800  35.27100 1.000 32.48000 ? 158 LEU B N   1 
ATOM   3850 C  CA  . LEU B 1 164 ? 27.80700  31.09100  34.18700 1.000 37.57000 ? 158 LEU B CA  1 
ATOM   3851 C  C   . LEU B 1 164 ? 28.69200  31.33700  32.96600 1.000 38.90000 ? 158 LEU B C   1 
ATOM   3852 O  O   . LEU B 1 164 ? 29.85800  31.70100  33.11800 1.000 38.01000 ? 158 LEU B O   1 
ATOM   3853 C  CB  . LEU B 1 164 ? 27.18500  32.41500  34.63200 1.000 38.53000 ? 158 LEU B CB  1 
ATOM   3854 C  CG  . LEU B 1 164 ? 26.37300  32.38000  35.93200 1.000 40.91000 ? 158 LEU B CG  1 
ATOM   3855 C  CD1 . LEU B 1 164 ? 25.82200  33.76100  36.20900 1.000 40.08000 ? 158 LEU B CD1 1 
ATOM   3856 C  CD2 . LEU B 1 164 ? 25.24600  31.32000  35.90800 1.000 35.04000 ? 158 LEU B CD2 1 
ATOM   3857 N  N   . PRO B 1 165 ? 28.15900  31.17500  31.74800 1.000 38.67000 ? 159 PRO B N   1 
ATOM   3858 C  CA  . PRO B 1 165 ? 28.99800  31.35500  30.53700 1.000 38.61000 ? 159 PRO B CA  1 
ATOM   3859 C  C   . PRO B 1 165 ? 29.64600  32.73100  30.39100 1.000 40.71000 ? 159 PRO B C   1 
ATOM   3860 O  O   . PRO B 1 165 ? 30.72400  32.82700  29.78600 1.000 37.38000 ? 159 PRO B O   1 
ATOM   3861 C  CB  . PRO B 1 165 ? 28.01200  31.08800  29.39200 1.000 44.79000 ? 159 PRO B CB  1 
ATOM   3862 C  CG  . PRO B 1 165 ? 26.96900  30.17700  29.99300 1.000 36.12000 ? 159 PRO B CG  1 
ATOM   3863 C  CD  . PRO B 1 165 ? 26.82900  30.61200  31.43500 1.000 37.45000 ? 159 PRO B CD  1 
ATOM   3864 N  N   . ASP B 1 166 ? 29.04100  33.80100  30.91800 1.000 47.52000 ? 160 ASP B N   1 
ATOM   3865 C  CA  . ASP B 1 166 ? 29.66800  35.11900  30.77000 1.000 47.07000 ? 160 ASP B CA  1 
ATOM   3866 C  C   . ASP B 1 166 ? 30.88000  35.31200  31.68000 1.000 42.63000 ? 160 ASP B C   1 
ATOM   3867 O  O   . ASP B 1 166 ? 31.62000  36.28800  31.49700 1.000 42.49000 ? 160 ASP B O   1 
ATOM   3868 C  CB  . ASP B 1 166 ? 28.64900  36.24700  31.01500 1.000 50.94000 ? 160 ASP B CB  1 
ATOM   3869 C  CG  . ASP B 1 166 ? 27.94400  36.15000  32.39200 1.000 61.60000 ? 160 ASP B CG  1 
ATOM   3870 O  OD1 . ASP B 1 166 ? 27.44200  35.04900  32.75000 1.000 58.51000 ? 160 ASP B OD1 1 
ATOM   3871 O  OD2 . ASP B 1 166 ? 27.87700  37.19200  33.10800 1.000 60.76000 ? 160 ASP B OD2 1 
ATOM   3872 N  N   . HIS B 1 167 ? 31.09900  34.41900  32.64200 1.000 34.49000 ? 161 HIS B N   1 
ATOM   3873 C  CA  . HIS B 1 167 ? 32.20900  34.57300  33.56100 1.000 31.57000 ? 161 HIS B CA  1 
ATOM   3874 C  C   . HIS B 1 167 ? 33.52700  34.32000  32.83000 1.000 31.28000 ? 161 HIS B C   1 
ATOM   3875 O  O   . HIS B 1 167 ? 33.57100  33.50400  31.90100 1.000 31.50000 ? 161 HIS B O   1 
ATOM   3876 C  CB  . HIS B 1 167 ? 32.04100  33.60100  34.72400 1.000 32.62000 ? 161 HIS B CB  1 
ATOM   3877 C  CG  . HIS B 1 167 ? 33.00300  33.83500  35.84300 1.000 34.77000 ? 161 HIS B CG  1 
ATOM   3878 N  ND1 . HIS B 1 167 ? 34.29000  33.33900  35.83100 1.000 30.62000 ? 161 HIS B ND1 1 
ATOM   3879 C  CD2 . HIS B 1 167 ? 32.86900  34.52200  37.00400 1.000 31.91000 ? 161 HIS B CD2 1 
ATOM   3880 C  CE1 . HIS B 1 167 ? 34.90600  33.70300  36.94600 1.000 30.16000 ? 161 HIS B CE1 1 
ATOM   3881 N  NE2 . HIS B 1 167 ? 34.06400  34.41900  37.67300 1.000 36.12000 ? 161 HIS B NE2 1 
ATOM   3882 N  N   . PRO B 1 168 ? 34.61100  35.03200  33.18400 1.000 32.34000 ? 162 PRO B N   1 
ATOM   3883 C  CA  . PRO B 1 168 ? 35.90300  34.77400  32.50300 1.000 29.20000 ? 162 PRO B CA  1 
ATOM   3884 C  C   . PRO B 1 168 ? 36.40500  33.33900  32.60900 1.000 28.23000 ? 162 PRO B C   1 
ATOM   3885 O  O   . PRO B 1 168 ? 37.10200  32.85900  31.69500 1.000 26.06000 ? 162 PRO B O   1 
ATOM   3886 C  CB  . PRO B 1 168 ? 36.87900  35.75900  33.19000 1.000 27.27000 ? 162 PRO B CB  1 
ATOM   3887 C  CG  . PRO B 1 168 ? 36.10300  36.41300  34.31500 1.000 25.45000 ? 162 PRO B CG  1 
ATOM   3888 C  CD  . PRO B 1 168 ? 34.64200  36.28200  33.96800 1.000 25.88000 ? 162 PRO B CD  1 
ATOM   3889 N  N   . MET B 1 169 ? 36.12400  32.64100  33.70800 1.000 25.44000 ? 163 MET B N   1 
ATOM   3890 C  CA  . MET B 1 169 ? 36.53600  31.24000  33.76000 1.000 28.02000 ? 163 MET B CA  1 
ATOM   3891 C  C   . MET B 1 169 ? 35.84900  30.41500  32.68200 1.000 28.76000 ? 163 MET B C   1 
ATOM   3892 O  O   . MET B 1 169 ? 36.46900  29.51400  32.09700 1.000 24.18000 ? 163 MET B O   1 
ATOM   3893 C  CB  . MET B 1 169 ? 36.27000  30.64900  35.14000 1.000 26.37000 ? 163 MET B CB  1 
ATOM   3894 C  CG  . MET B 1 169 ? 37.24000  31.22400  36.16900 1.000 28.42000 ? 163 MET B CG  1 
ATOM   3895 S  SD  . MET B 1 169 ? 38.96900  30.95500  35.65200 1.000 34.60000 ? 163 MET B SD  1 
ATOM   3896 C  CE  . MET B 1 169 ? 38.99400  29.13900  35.53600 1.000 20.44000 ? 163 MET B CE  1 
ATOM   3897 N  N   . GLN B 1 170 ? 34.57300  30.70100  32.39100 1.000 25.52000 ? 164 GLN B N   1 
ATOM   3898 C  CA  . GLN B 1 170 ? 33.89400  29.91100  31.36200 1.000 28.18000 ? 164 GLN B CA  1 
ATOM   3899 C  C   . GLN B 1 170 ? 34.36300  30.30700  29.96900 1.000 26.40000 ? 164 GLN B C   1 
ATOM   3900 O  O   . GLN B 1 170 ? 34.46500  29.45400  29.08500 1.000 28.00000 ? 164 GLN B O   1 
ATOM   3901 C  CB  . GLN B 1 170 ? 32.36900  30.03700  31.49400 1.000 31.33000 ? 164 GLN B CB  1 
ATOM   3902 C  CG  . GLN B 1 170 ? 31.79900  29.51100  32.85400 1.000 32.32000 ? 164 GLN B CG  1 
ATOM   3903 C  CD  . GLN B 1 170 ? 32.25100  28.10500  33.23000 1.000 34.96000 ? 164 GLN B CD  1 
ATOM   3904 O  OE1 . GLN B 1 170 ? 32.46700  27.26300  32.37400 1.000 31.38000 ? 164 GLN B OE1 1 
ATOM   3905 N  NE2 . GLN B 1 170 ? 32.41400  27.86200  34.52700 1.000 36.27000 ? 164 GLN B NE2 1 
ATOM   3906 N  N   . GLY B 1 171 ? 34.69700  31.57900  29.76300 1.000 27.88000 ? 165 GLY B N   1 
ATOM   3907 C  CA  . GLY B 1 171 ? 35.38500  31.94500  28.54100 1.000 23.96000 ? 165 GLY B CA  1 
ATOM   3908 C  C   . GLY B 1 171 ? 36.67000  31.16100  28.35700 1.000 25.05000 ? 165 GLY B C   1 
ATOM   3909 O  O   . GLY B 1 171 ? 36.98000  30.69500  27.25200 1.000 25.97000 ? 165 GLY B O   1 
ATOM   3910 N  N   . ARG B 1 172 ? 37.44800  31.01000  29.42900 1.000 22.25000 ? 166 ARG B N   1 
ATOM   3911 C  CA  . ARG B 1 172 ? 38.69400  30.26500  29.29600 1.000 22.03000 ? 166 ARG B CA  1 
ATOM   3912 C  C   . ARG B 1 172 ? 38.42500  28.78400  29.01700 1.000 21.65000 ? 166 ARG B C   1 
ATOM   3913 O  O   . ARG B 1 172 ? 39.09100  28.17200  28.17100 1.000 22.94000 ? 166 ARG B O   1 
ATOM   3914 C  CB  . ARG B 1 172 ? 39.54500  30.45400  30.55400 1.000 22.02000 ? 166 ARG B CB  1 
ATOM   3915 C  CG  . ARG B 1 172 ? 40.32600  31.76900  30.57900 1.000 22.60000 ? 166 ARG B CG  1 
ATOM   3916 C  CD  . ARG B 1 172 ? 40.65700  32.15900  31.99800 1.000 23.60000 ? 166 ARG B CD  1 
ATOM   3917 N  NE  . ARG B 1 172 ? 41.47800  33.35900  32.00800 1.000 24.09000 ? 166 ARG B NE  1 
ATOM   3918 C  CZ  . ARG B 1 172 ? 42.79300  33.35100  32.18100 1.000 25.19000 ? 166 ARG B CZ  1 
ATOM   3919 N  NH1 . ARG B 1 172 ? 43.45500  32.22800  32.44000 1.000 23.14000 ? 166 ARG B NH1 1 
ATOM   3920 N  NH2 . ARG B 1 172 ? 43.47000  34.48600  32.04000 1.000 20.05000 ? 166 ARG B NH2 1 
ATOM   3921 N  N   . VAL B 1 173 ? 37.44900  28.18900  29.70300 1.000 20.34000 ? 167 VAL B N   1 
ATOM   3922 C  CA  . VAL B 1 173 ? 37.10600  26.78900  29.45000 1.000 19.17000 ? 167 VAL B CA  1 
ATOM   3923 C  C   . VAL B 1 173 ? 36.68500  26.58400  27.98900 1.000 20.83000 ? 167 VAL B C   1 
ATOM   3924 O  O   . VAL B 1 173 ? 37.13000  25.63500  27.31700 1.000 21.21000 ? 167 VAL B O   1 
ATOM   3925 C  CB  . VAL B 1 173 ? 36.00000  26.34600  30.42500 1.000 23.00000 ? 167 VAL B CB  1 
ATOM   3926 C  CG1 . VAL B 1 173 ? 35.38300  25.01300  30.01300 1.000 21.50000 ? 167 VAL B CG1 1 
ATOM   3927 C  CG2 . VAL B 1 173 ? 36.55600  26.26100  31.84200 1.000 24.67000 ? 167 VAL B CG2 1 
ATOM   3928 N  N   . LYS B 1 174 ? 35.79100  27.44400  27.48200 1.000 22.75000 ? 168 LYS B N   1 
ATOM   3929 C  CA  . LYS B 1 174 ? 35.28000  27.25400  26.11900 1.000 23.77000 ? 168 LYS B CA  1 
ATOM   3930 C  C   . LYS B 1 174 ? 36.40900  27.32400  25.09700 1.000 23.48000 ? 168 LYS B C   1 
ATOM   3931 O  O   . LYS B 1 174 ? 36.47700  26.49700  24.17100 1.000 22.98000 ? 168 LYS B O   1 
ATOM   3932 C  CB  . LYS B 1 174 ? 34.19100  28.28900  25.78500 1.000 27.52000 ? 168 LYS B CB  1 
ATOM   3933 C  CG  . LYS B 1 174 ? 32.83000  27.96800  26.39800 1.000 31.46000 ? 168 LYS B CG  1 
ATOM   3934 C  CD  . LYS B 1 174 ? 31.69600  28.85000  25.80600 1.000 37.44000 ? 168 LYS B CD  1 
ATOM   3935 C  CE  . LYS B 1 174 ? 30.33300  28.53200  26.46700 1.000 38.94000 ? 168 LYS B CE  1 
ATOM   3936 N  NZ  . LYS B 1 174 ? 30.39400  28.52900  27.98100 1.000 38.03000 ? 168 LYS B NZ  1 
ATOM   3937 N  N   . ARG B 1 175 ? 37.29200  28.31600  25.24200 1.000 22.27000 ? 169 ARG B N   1 
ATOM   3938 C  CA  A ARG B 1 175 ? 38.44400  28.43100  24.34800 0.500 22.96000 ? 169 ARG B CA  1 
ATOM   3939 C  CA  B ARG B 1 175 ? 38.43900  28.43600  24.35000 0.500 22.96000 ? 169 ARG B CA  1 
ATOM   3940 C  C   . ARG B 1 175 ? 39.31000  27.18400  24.41200 1.000 22.72000 ? 169 ARG B C   1 
ATOM   3941 O  O   . ARG B 1 175 ? 39.70100  26.63000  23.37700 1.000 21.00000 ? 169 ARG B O   1 
ATOM   3942 C  CB  A ARG B 1 175 ? 39.28100  29.66300  24.70500 0.500 23.24000 ? 169 ARG B CB  1 
ATOM   3943 C  CB  B ARG B 1 175 ? 39.23100  29.69100  24.72900 0.500 23.24000 ? 169 ARG B CB  1 
ATOM   3944 C  CG  A ARG B 1 175 ? 39.10600  30.83800  23.77200 0.500 24.57000 ? 169 ARG B CG  1 
ATOM   3945 C  CG  B ARG B 1 175 ? 40.47400  29.93100  23.92800 0.500 25.38000 ? 169 ARG B CG  1 
ATOM   3946 C  CD  A ARG B 1 175 ? 40.29700  31.80500  23.84900 0.500 23.47000 ? 169 ARG B CD  1 
ATOM   3947 C  CD  B ARG B 1 175 ? 41.12800  31.26400  24.27900 0.500 23.94000 ? 169 ARG B CD  1 
ATOM   3948 N  NE  A ARG B 1 175 ? 40.75700  32.04800  25.21100 0.500 23.61000 ? 169 ARG B NE  1 
ATOM   3949 N  NE  B ARG B 1 175 ? 41.47400  31.39500  25.69300 0.500 25.62000 ? 169 ARG B NE  1 
ATOM   3950 C  CZ  A ARG B 1 175 ? 40.12900  32.81400  26.09100 0.500 25.37000 ? 169 ARG B CZ  1 
ATOM   3951 C  CZ  B ARG B 1 175 ? 42.48900  30.77600  26.28500 0.500 25.19000 ? 169 ARG B CZ  1 
ATOM   3952 N  NH1 A ARG B 1 175 ? 38.96100  33.36500  25.80900 0.500 23.60000 ? 169 ARG B NH1 1 
ATOM   3953 N  NH1 B ARG B 1 175 ? 43.21600  29.87400  25.64900 0.500 24.31000 ? 169 ARG B NH1 1 
ATOM   3954 N  NH2 A ARG B 1 175 ? 40.69400  33.04000  27.27700 0.500 24.37000 ? 169 ARG B NH2 1 
ATOM   3955 N  NH2 B ARG B 1 175 ? 42.79800  31.09000  27.54000 0.500 23.00000 ? 169 ARG B NH2 1 
ATOM   3956 N  N   . THR B 1 176 ? 39.61400  26.71600  25.63100 1.000 20.33000 ? 170 THR B N   1 
ATOM   3957 C  CA  . THR B 1 176 ? 40.55700  25.61900  25.80400 1.000 21.80000 ? 170 THR B CA  1 
ATOM   3958 C  C   . THR B 1 176 ? 40.03300  24.31400  25.22700 1.000 19.66000 ? 170 THR B C   1 
ATOM   3959 O  O   . THR B 1 176 ? 40.80300  23.51800  24.65900 1.000 20.42000 ? 170 THR B O   1 
ATOM   3960 C  CB  . THR B 1 176 ? 40.85100  25.45200  27.28000 1.000 20.88000 ? 170 THR B CB  1 
ATOM   3961 O  OG1 . THR B 1 176 ? 41.30900  26.70600  27.78700 1.000 21.91000 ? 170 THR B OG1 1 
ATOM   3962 C  CG2 . THR B 1 176 ? 41.90100  24.38400  27.49400 1.000 19.10000 ? 170 THR B CG2 1 
ATOM   3963 N  N   . VAL B 1 177 ? 38.74200  24.04700  25.41800 1.000 21.02000 ? 171 VAL B N   1 
ATOM   3964 C  CA  . VAL B 1 177 ? 38.13500  22.83900  24.87900 1.000 19.74000 ? 171 VAL B CA  1 
ATOM   3965 C  C   . VAL B 1 177 ? 38.23000  22.82700  23.36100 1.000 21.22000 ? 171 VAL B C   1 
ATOM   3966 O  O   . VAL B 1 177 ? 38.67800  21.84100  22.75700 1.000 22.31000 ? 171 VAL B O   1 
ATOM   3967 C  CB  . VAL B 1 177 ? 36.68200  22.73200  25.35900 1.000 20.24000 ? 171 VAL B CB  1 
ATOM   3968 C  CG1 . VAL B 1 177 ? 35.96900  21.63300  24.55200 1.000 20.38000 ? 171 VAL B CG1 1 
ATOM   3969 C  CG2 . VAL B 1 177 ? 36.69300  22.39700  26.82100 1.000 19.54000 ? 171 VAL B CG2 1 
ATOM   3970 N  N   . ALA B 1 178 ? 37.82400  23.93100  22.71800 1.000 21.35000 ? 172 ALA B N   1 
ATOM   3971 C  CA  . ALA B 1 178 ? 37.89800  24.01000  21.25500 1.000 23.20000 ? 172 ALA B CA  1 
ATOM   3972 C  C   . ALA B 1 178 ? 39.34100  23.89400  20.75100 1.000 22.18000 ? 172 ALA B C   1 
ATOM   3973 O  O   . ALA B 1 178 ? 39.59700  23.28100  19.69900 1.000 23.75000 ? 172 ALA B O   1 
ATOM   3974 C  CB  . ALA B 1 178 ? 37.26700  25.32300  20.76300 1.000 18.25000 ? 172 ALA B CB  1 
ATOM   3975 N  N   . GLU B 1 179 ? 40.29300  24.49900  21.46200 1.000 18.84000 ? 173 GLU B N   1 
ATOM   3976 C  CA  . GLU B 1 179 ? 41.69600  24.39500  21.06600 1.000 20.22000 ? 173 GLU B CA  1 
ATOM   3977 C  C   . GLU B 1 179 ? 42.19300  22.95400  21.15100 1.000 23.84000 ? 173 GLU B C   1 
ATOM   3978 O  O   . GLU B 1 179 ? 42.85800  22.45900  20.22700 1.000 24.77000 ? 173 GLU B O   1 
ATOM   3979 C  CB  . GLU B 1 179 ? 42.54800  25.29600  21.94200 1.000 21.08000 ? 173 GLU B CB  1 
ATOM   3980 C  CG  . GLU B 1 179 ? 42.38100  26.77800  21.61600 1.000 21.38000 ? 173 GLU B CG  1 
ATOM   3981 C  CD  . GLU B 1 179 ? 43.04300  27.68100  22.61300 1.000 27.43000 ? 173 GLU B CD  1 
ATOM   3982 O  OE1 . GLU B 1 179 ? 43.59200  27.19700  23.63800 1.000 27.89000 ? 173 GLU B OE1 1 
ATOM   3983 O  OE2 . GLU B 1 179 ? 43.03700  28.90000  22.35900 1.000 34.79000 ? 173 GLU B OE2 1 
ATOM   3984 N  N   . LEU B 1 180 ? 41.91000  22.27100  22.27000 1.000 19.40000 ? 174 LEU B N   1 
ATOM   3985 C  CA  . LEU B 1 180 ? 42.32600  20.87600  22.39500 1.000 19.77000 ? 174 LEU B CA  1 
ATOM   3986 C  C   . LEU B 1 180 ? 41.68900  19.99800  21.34000 1.000 21.24000 ? 174 LEU B C   1 
ATOM   3987 O  O   . LEU B 1 180 ? 42.29400  19.00400  20.92200 1.000 22.70000 ? 174 LEU B O   1 
ATOM   3988 C  CB  . LEU B 1 180 ? 42.00200  20.31800  23.77200 1.000 17.06000 ? 174 LEU B CB  1 
ATOM   3989 C  CG  . LEU B 1 180 ? 42.90500  20.86600  24.85700 1.000 23.77000 ? 174 LEU B CG  1 
ATOM   3990 C  CD1 . LEU B 1 180 ? 42.32900  20.36700  26.15100 1.000 20.87000 ? 174 LEU B CD1 1 
ATOM   3991 C  CD2 . LEU B 1 180 ? 44.35700  20.40300  24.65300 1.000 21.21000 ? 174 LEU B CD2 1 
ATOM   3992 N  N   . CYS B 1 181 ? 40.43400  20.28500  20.96000 1.000 19.75000 ? 175 CYS B N   1 
ATOM   3993 C  CA  . CYS B 1 181 ? 39.77600  19.55100  19.87800 1.000 19.92000 ? 175 CYS B CA  1 
ATOM   3994 C  C   . CYS B 1 181 ? 40.28300  19.92200  18.49300 1.000 20.14000 ? 175 CYS B C   1 
ATOM   3995 O  O   . CYS B 1 181 ? 39.99000  19.18500  17.53800 1.000 21.48000 ? 175 CYS B O   1 
ATOM   3996 C  CB  . CYS B 1 181 ? 38.26300  19.79200  19.89000 1.000 19.54000 ? 175 CYS B CB  1 
ATOM   3997 S  SG  . CYS B 1 181 ? 37.37700  19.12300  21.32400 1.000 22.02000 ? 175 CYS B SG  1 
ATOM   3998 N  N   . ASP B 1 182 ? 41.01400  21.03000  18.36600 1.000 22.51000 ? 176 ASP B N   1 
ATOM   3999 C  CA  . ASP B 1 182 ? 41.36200  21.66500  17.07900 1.000 25.89000 ? 176 ASP B CA  1 
ATOM   4000 C  C   . ASP B 1 182 ? 40.11600  22.04800  16.26400 1.000 25.58000 ? 176 ASP B C   1 
ATOM   4001 O  O   . ASP B 1 182 ? 40.05600  21.87600  15.04000 1.000 26.11000 ? 176 ASP B O   1 
ATOM   4002 C  CB  . ASP B 1 182 ? 42.31300  20.78000  16.27000 1.000 25.60000 ? 176 ASP B CB  1 
ATOM   4003 C  CG  . ASP B 1 182 ? 43.58700  20.44400  17.04500 1.000 29.14000 ? 176 ASP B CG  1 
ATOM   4004 O  OD1 . ASP B 1 182 ? 44.10200  21.32700  17.77900 1.000 30.35000 ? 176 ASP B OD1 1 
ATOM   4005 O  OD2 . ASP B 1 182 ? 44.05400  19.27900  16.94500 1.000 28.67000 ? 176 ASP B OD2 1 
ATOM   4006 N  N   . LEU B 1 183 ? 39.12200  22.61300  16.94100 1.000 23.55000 ? 177 LEU B N   1 
ATOM   4007 C  CA  . LEU B 1 183 ? 37.86000  22.99200  16.32600 1.000 24.80000 ? 177 LEU B CA  1 
ATOM   4008 C  C   . LEU B 1 183 ? 37.66600  24.49400  16.45400 1.000 27.40000 ? 177 LEU B C   1 
ATOM   4009 O  O   . LEU B 1 183 ? 38.15400  25.10900  17.40000 1.000 25.14000 ? 177 LEU B O   1 
ATOM   4010 C  CB  . LEU B 1 183 ? 36.69100  22.25500  16.98900 1.000 23.50000 ? 177 LEU B CB  1 
ATOM   4011 C  CG  . LEU B 1 183 ? 36.55800  20.74900  16.75700 1.000 25.69000 ? 177 LEU B CG  1 
ATOM   4012 C  CD1 . LEU B 1 183 ? 35.39500  20.21100  17.57500 1.000 22.24000 ? 177 LEU B CD1 1 
ATOM   4013 C  CD2 . LEU B 1 183 ? 36.34300  20.50300  15.26300 1.000 25.43000 ? 177 LEU B CD2 1 
ATOM   4014 N  N   . ASP B 1 184 ? 36.95800  25.08500  15.49500 1.000 23.93000 ? 178 ASP B N   1 
ATOM   4015 C  CA  . ASP B 1 184 ? 36.48000  26.43500  15.69700 1.000 30.04000 ? 178 ASP B CA  1 
ATOM   4016 C  C   . ASP B 1 184 ? 35.39300  26.44100  16.76300 1.000 29.10000 ? 178 ASP B C   1 
ATOM   4017 O  O   . ASP B 1 184 ? 34.72700  25.43700  17.00700 1.000 24.17000 ? 178 ASP B O   1 
ATOM   4018 C  CB  . ASP B 1 184 ? 35.93200  27.02700  14.40600 1.000 32.53000 ? 178 ASP B CB  1 
ATOM   4019 C  CG  . ASP B 1 184 ? 36.98900  27.18500  13.35000 1.000 38.44000 ? 178 ASP B CG  1 
ATOM   4020 O  OD1 . ASP B 1 184 ? 38.07100  27.77300  13.63200 1.000 42.01000 ? 178 ASP B OD1 1 
ATOM   4021 O  OD2 . ASP B 1 184 ? 36.72200  26.71400  12.21900 1.000 46.60000 ? 178 ASP B OD2 1 
ATOM   4022 N  N   . ALA B 1 185 ? 35.22100  27.59800  17.40100 1.000 28.43000 ? 179 ALA B N   1 
ATOM   4023 C  CA  . ALA B 1 185 ? 34.22000  27.73300  18.45600 1.000 28.14000 ? 179 ALA B CA  1 
ATOM   4024 C  C   . ALA B 1 185 ? 32.83900  27.26400  17.99600 1.000 26.06000 ? 179 ALA B C   1 
ATOM   4025 O  O   . ALA B 1 185 ? 32.13100  26.55700  18.72000 1.000 24.40000 ? 179 ALA B O   1 
ATOM   4026 C  CB  . ALA B 1 185 ? 34.17400  29.19500  18.91400 1.000 25.94000 ? 179 ALA B CB  1 
ATOM   4027 N  N   . GLY B 1 186 ? 32.42700  27.66400  16.79700 1.000 28.93000 ? 180 GLY B N   1 
ATOM   4028 C  CA  . GLY B 1 186 ? 31.09800  27.29500  16.35800 1.000 26.07000 ? 180 GLY B CA  1 
ATOM   4029 C  C   . GLY B 1 186 ? 30.90500  25.82000  16.12600 1.000 31.51000 ? 180 GLY B C   1 
ATOM   4030 O  O   . GLY B 1 186 ? 29.76200  25.40100  15.93200 1.000 30.69000 ? 180 GLY B O   1 
ATOM   4031 N  N   . ASP B 1 187 ? 31.98000  25.02300  16.12900 1.000 26.45000 ? 181 ASP B N   1 
ATOM   4032 C  CA  . ASP B 1 187 ? 31.88000  23.57700  15.98300 1.000 26.56000 ? 181 ASP B CA  1 
ATOM   4033 C  C   . ASP B 1 187 ? 31.78900  22.82500  17.31800 1.000 24.63000 ? 181 ASP B C   1 
ATOM   4034 O  O   . ASP B 1 187 ? 31.62800  21.59200  17.31600 1.000 26.29000 ? 181 ASP B O   1 
ATOM   4035 C  CB  . ASP B 1 187 ? 33.06600  23.07500  15.15900 1.000 30.65000 ? 181 ASP B CB  1 
ATOM   4036 C  CG  . ASP B 1 187 ? 32.90800  23.37900  13.66800 1.000 32.91000 ? 181 ASP B CG  1 
ATOM   4037 O  OD1 . ASP B 1 187 ? 31.76500  23.32700  13.16500 1.000 41.10000 ? 181 ASP B OD1 1 
ATOM   4038 O  OD2 . ASP B 1 187 ? 33.91600  23.65700  12.98900 1.000 39.31000 ? 181 ASP B OD2 1 
ATOM   4039 N  N   . VAL B 1 188 ? 31.87000  23.52600  18.45000 1.000 23.90000 ? 182 VAL B N   1 
ATOM   4040 C  CA  . VAL B 1 188 ? 31.58800  22.97000  19.77600 1.000 19.63000 ? 182 VAL B CA  1 
ATOM   4041 C  C   . VAL B 1 188 ? 30.26500  23.56000  20.24000 1.000 26.62000 ? 182 VAL B C   1 
ATOM   4042 O  O   . VAL B 1 188 ? 30.10700  24.78800  20.28200 1.000 25.06000 ? 182 VAL B O   1 
ATOM   4043 C  CB  . VAL B 1 188 ? 32.70400  23.28500  20.78900 1.000 21.56000 ? 182 VAL B CB  1 
ATOM   4044 C  CG1 . VAL B 1 188 ? 32.40500  22.59000  22.14600 1.000 19.76000 ? 182 VAL B CG1 1 
ATOM   4045 C  CG2 . VAL B 1 188 ? 34.05000  22.83000  20.23300 1.000 20.52000 ? 182 VAL B CG2 1 
ATOM   4046 N  N   . GLU B 1 189 ? 29.31000  22.69800  20.56900 1.000 22.40000 ? 183 GLU B N   1 
ATOM   4047 C  CA  . GLU B 1 189 ? 28.03900  23.13400  21.13300 1.000 24.60000 ? 183 GLU B CA  1 
ATOM   4048 C  C   . GLU B 1 189 ? 28.04800  22.94300  22.64800 1.000 19.18000 ? 183 GLU B C   1 
ATOM   4049 O  O   . GLU B 1 189 ? 28.80500  22.12200  23.18000 1.000 21.23000 ? 183 GLU B O   1 
ATOM   4050 C  CB  . GLU B 1 189 ? 26.89300  22.35900  20.47500 1.000 25.35000 ? 183 GLU B CB  1 
ATOM   4051 C  CG  . GLU B 1 189 ? 26.65900  22.78800  19.02600 1.000 30.09000 ? 183 GLU B CG  1 
ATOM   4052 C  CD  . GLU B 1 189 ? 25.77400  21.80500  18.27800 1.000 42.22000 ? 183 GLU B CD  1 
ATOM   4053 O  OE1 . GLU B 1 189 ? 24.81100  21.30000  18.90000 1.000 43.36000 ? 183 GLU B OE1 1 
ATOM   4054 O  OE2 . GLU B 1 189 ? 26.04300  21.50800  17.07900 1.000 47.75000 ? 183 GLU B OE2 1 
ATOM   4055 N  N   . TRP B 1 190 ? 27.20300  23.71800  23.34800 1.000 22.06000 ? 184 TRP B N   1 
ATOM   4056 C  CA  . TRP B 1 190 ? 27.23000  23.77500  24.81200 1.000 17.73000 ? 184 TRP B CA  1 
ATOM   4057 C  C   . TRP B 1 190 ? 25.83900  23.62200  25.39100 1.000 24.01000 ? 184 TRP B C   1 
ATOM   4058 O  O   . TRP B 1 190 ? 24.92200  24.33200  24.97800 1.000 23.40000 ? 184 TRP B O   1 
ATOM   4059 C  CB  . TRP B 1 190 ? 27.83700  25.11000  25.29500 1.000 20.15000 ? 184 TRP B CB  1 
ATOM   4060 C  CG  . TRP B 1 190 ? 29.27900  25.22000  24.89600 1.000 18.28000 ? 184 TRP B CG  1 
ATOM   4061 C  CD1 . TRP B 1 190 ? 29.77200  25.68200  23.70600 1.000 21.80000 ? 184 TRP B CD1 1 
ATOM   4062 C  CD2 . TRP B 1 190 ? 30.41000  24.77600  25.65300 1.000 21.50000 ? 184 TRP B CD2 1 
ATOM   4063 N  NE1 . TRP B 1 190 ? 31.14200  25.56400  23.68600 1.000 22.46000 ? 184 TRP B NE1 1 
ATOM   4064 C  CE2 . TRP B 1 190 ? 31.55700  25.01300  24.87200 1.000 22.34000 ? 184 TRP B CE2 1 
ATOM   4065 C  CE3 . TRP B 1 190 ? 30.56300  24.19700  26.92000 1.000 22.87000 ? 184 TRP B CE3 1 
ATOM   4066 C  CZ2 . TRP B 1 190 ? 32.84000  24.70600  25.31800 1.000 23.14000 ? 184 TRP B CZ2 1 
ATOM   4067 C  CZ3 . TRP B 1 190 ? 31.82600  23.88700  27.35300 1.000 19.94000 ? 184 TRP B CZ3 1 
ATOM   4068 C  CH2 . TRP B 1 190 ? 32.95100  24.15000  26.56500 1.000 21.99000 ? 184 TRP B CH2 1 
ATOM   4069 N  N   . GLY B 1 191 ? 25.69200  22.71300  26.36000 1.000 23.42000 ? 185 GLY B N   1 
ATOM   4070 C  CA  . GLY B 1 191 ? 24.47000  22.57700  27.13500 1.000 23.75000 ? 185 GLY B CA  1 
ATOM   4071 C  C   . GLY B 1 191 ? 24.76100  22.84300  28.59800 1.000 24.04000 ? 185 GLY B C   1 
ATOM   4072 O  O   . GLY B 1 191 ? 25.80700  23.39900  28.91300 1.000 23.53000 ? 185 GLY B O   1 
ATOM   4073 N  N   . THR B 1 192 ? 23.86100  22.47900  29.50100 1.000 23.94000 ? 186 THR B N   1 
ATOM   4074 C  CA  . THR B 1 192 ? 24.05100  22.67900  30.93900 1.000 23.10000 ? 186 THR B CA  1 
ATOM   4075 C  C   . THR B 1 192 ? 24.10800  21.31200  31.61200 1.000 25.09000 ? 186 THR B C   1 
ATOM   4076 O  O   . THR B 1 192 ? 23.23000  20.46600  31.37600 1.000 23.38000 ? 186 THR B O   1 
ATOM   4077 C  CB  . THR B 1 192 ? 22.92000  23.50800  31.54700 1.000 22.69000 ? 186 THR B CB  1 
ATOM   4078 O  OG1 . THR B 1 192 ? 22.92200  24.83600  30.99400 1.000 26.07000 ? 186 THR B OG1 1 
ATOM   4079 C  CG2 . THR B 1 192 ? 23.07300  23.58300  33.09300 1.000 26.17000 ? 186 THR B CG2 1 
ATOM   4080 N  N   . ASP B 1 193 ? 25.13100  21.09700  32.44300 1.000 24.46000 ? 187 ASP B N   1 
ATOM   4081 C  CA  . ASP B 1 193 ? 25.42000  19.78300  33.01300 1.000 24.12000 ? 187 ASP B CA  1 
ATOM   4082 C  C   . ASP B 1 193 ? 24.57200  19.52600  34.24400 1.000 23.77000 ? 187 ASP B C   1 
ATOM   4083 O  O   . ASP B 1 193 ? 23.89100  20.41600  34.76300 1.000 24.83000 ? 187 ASP B O   1 
ATOM   4084 C  CB  . ASP B 1 193 ? 26.88900  19.68500  33.41600 1.000 27.09000 ? 187 ASP B CB  1 
ATOM   4085 C  CG  . ASP B 1 193 ? 27.51600  18.34000  33.04800 1.000 31.14000 ? 187 ASP B CG  1 
ATOM   4086 O  OD1 . ASP B 1 193 ? 26.75800  17.35900  32.88300 1.000 28.23000 ? 187 ASP B OD1 1 
ATOM   4087 O  OD2 . ASP B 1 193 ? 28.77600  18.25800  32.91500 1.000 29.72000 ? 187 ASP B OD2 1 
ATOM   4088 N  N   . GLY B 1 194 ? 24.66100  18.29200  34.75300 1.000 24.80000 ? 188 GLY B N   1 
ATOM   4089 C  CA  . GLY B 1 194 ? 23.99000  17.97100  36.00700 1.000 29.57000 ? 188 GLY B CA  1 
ATOM   4090 C  C   . GLY B 1 194 ? 24.52000  18.75200  37.20000 1.000 30.36000 ? 188 GLY B C   1 
ATOM   4091 O  O   . GLY B 1 194 ? 23.77500  19.02100  38.15000 1.000 27.64000 ? 188 GLY B O   1 
ATOM   4092 N  N   . CYS B 1 195 ? 25.80600  19.12400  37.17800 1.000 26.54000 ? 189 CYS B N   1 
ATOM   4093 C  CA  . CYS B 1 195 ? 26.39900  19.92200  38.25300 1.000 32.37000 ? 189 CYS B CA  1 
ATOM   4094 C  C   . CYS B 1 195 ? 26.23300  21.42200  38.04800 1.000 30.45000 ? 189 CYS B C   1 
ATOM   4095 O  O   . CYS B 1 195 ? 26.79400  22.19400  38.83200 1.000 29.85000 ? 189 CYS B O   1 
ATOM   4096 C  CB  . CYS B 1 195 ? 27.88800  19.59900  38.39500 1.000 32.38000 ? 189 CYS B CB  1 
ATOM   4097 S  SG  . CYS B 1 195 ? 28.83100  20.13700  36.93700 1.000 31.12000 ? 189 CYS B SG  1 
ATOM   4098 N  N   . ASN B 1 196 ? 25.52400  21.83900  36.98300 1.000 28.59000 ? 190 ASN B N   1 
ATOM   4099 C  CA  . ASN B 1 196 ? 25.09400  23.21100  36.70000 1.000 25.60000 ? 190 ASN B CA  1 
ATOM   4100 C  C   . ASN B 1 196 ? 26.17500  24.08500  36.05800 1.000 29.46000 ? 190 ASN B C   1 
ATOM   4101 O  O   . ASN B 1 196 ? 26.08500  25.33400  36.10400 1.000 34.25000 ? 190 ASN B O   1 
ATOM   4102 C  CB  . ASN B 1 196 ? 24.55800  23.87100  37.96000 1.000 30.32000 ? 190 ASN B CB  1 
ATOM   4103 C  CG  . ASN B 1 196 ? 23.50500  24.88300  37.67200 1.000 34.32000 ? 190 ASN B CG  1 
ATOM   4104 O  OD1 . ASN B 1 196 ? 22.83800  24.83100  36.63700 1.000 32.53000 ? 190 ASN B OD1 1 
ATOM   4105 N  ND2 . ASN B 1 196 ? 23.35900  25.83800  38.57200 1.000 36.90000 ? 190 ASN B ND2 1 
ATOM   4106 N  N   . LEU B 1 197 ? 27.20900  23.47000  35.42300 1.000 27.11000 ? 191 LEU B N   1 
ATOM   4107 C  CA  . LEU B 1 197 ? 28.23700  24.12300  34.61600 1.000 28.40000 ? 191 LEU B CA  1 
ATOM   4108 C  C   . LEU B 1 197 ? 27.94600  23.93600  33.13800 1.000 26.95000 ? 191 LEU B C   1 
ATOM   4109 O  O   . LEU B 1 197 ? 27.30200  22.95800  32.73400 1.000 22.23000 ? 191 LEU B O   1 
ATOM   4110 C  CB  . LEU B 1 197 ? 29.62100  23.52000  34.90400 1.000 26.86000 ? 191 LEU B CB  1 
ATOM   4111 C  CG  . LEU B 1 197 ? 30.31500  23.86300  36.21400 1.000 33.82000 ? 191 LEU B CG  1 
ATOM   4112 C  CD1 . LEU B 1 197 ? 31.46300  22.89500  36.36500 1.000 34.14000 ? 191 LEU B CD1 1 
ATOM   4113 C  CD2 . LEU B 1 197 ? 30.82300  25.31000  36.19400 1.000 30.28000 ? 191 LEU B CD2 1 
ATOM   4114 N  N   . PRO B 1 198 ? 28.46100  24.80700  32.28000 1.000 25.01000 ? 192 PRO B N   1 
ATOM   4115 C  CA  . PRO B 1 198 ? 28.36900  24.52100  30.84500 1.000 25.16000 ? 192 PRO B CA  1 
ATOM   4116 C  C   . PRO B 1 198 ? 29.09000  23.21200  30.54300 1.000 21.63000 ? 192 PRO B C   1 
ATOM   4117 O  O   . PRO B 1 198 ? 30.10300  22.88600  31.16100 1.000 22.57000 ? 192 PRO B O   1 
ATOM   4118 C  CB  . PRO B 1 198 ? 29.05000  25.73800  30.19500 1.000 29.03000 ? 192 PRO B CB  1 
ATOM   4119 C  CG  . PRO B 1 198 ? 28.95300  26.85900  31.26800 1.000 28.54000 ? 192 PRO B CG  1 
ATOM   4120 C  CD  . PRO B 1 198 ? 29.13200  26.09800  32.55500 1.000 25.64000 ? 192 PRO B CD  1 
ATOM   4121 N  N   . THR B 1 199 ? 28.52100  22.41800  29.62900 1.000 23.80000 ? 193 THR B N   1 
ATOM   4122 C  CA  . THR B 1 199 ? 29.16700  21.16800  29.24700 1.000 23.14000 ? 193 THR B CA  1 
ATOM   4123 C  C   . THR B 1 199 ? 29.20300  21.04900  27.72600 1.000 23.68000 ? 193 THR B C   1 
ATOM   4124 O  O   . THR B 1 199 ? 28.20800  21.33600  27.06400 1.000 20.10000 ? 193 THR B O   1 
ATOM   4125 C  CB  . THR B 1 199 ? 28.44100  19.95700  29.89000 1.000 21.82000 ? 193 THR B CB  1 
ATOM   4126 O  OG1 . THR B 1 199 ? 29.20800  18.75900  29.66900 1.000 20.81000 ? 193 THR B OG1 1 
ATOM   4127 C  CG2 . THR B 1 199 ? 26.94700  19.77600  29.36200 1.000 22.57000 ? 193 THR B CG2 1 
ATOM   4128 N  N   . PRO B 1 200 ? 30.32000  20.61600  27.14200 1.000 20.29000 ? 194 PRO B N   1 
ATOM   4129 C  CA  . PRO B 1 200 ? 30.47100  20.70300  25.68500 1.000 20.55000 ? 194 PRO B CA  1 
ATOM   4130 C  C   . PRO B 1 200 ? 30.03000  19.45300  24.93300 1.000 19.47000 ? 194 PRO B C   1 
ATOM   4131 O  O   . PRO B 1 200 ? 30.04400  18.32600  25.44400 1.000 18.92000 ? 194 PRO B O   1 
ATOM   4132 C  CB  . PRO B 1 200 ? 31.98600  20.94300  25.53600 1.000 19.42000 ? 194 PRO B CB  1 
ATOM   4133 C  CG  . PRO B 1 200 ? 32.55700  20.04000  26.64600 1.000 17.19000 ? 194 PRO B CG  1 
ATOM   4134 C  CD  . PRO B 1 200 ? 31.58600  20.28700  27.81300 1.000 18.81000 ? 194 PRO B CD  1 
ATOM   4135 N  N   . ALA B 1 201 ? 29.64100  19.66600  23.66500 1.000 17.62000 ? 195 ALA B N   1 
ATOM   4136 C  CA  . ALA B 1 201 ? 29.40100  18.57000  22.72800 1.000 16.35000 ? 195 ALA B CA  1 
ATOM   4137 C  C   . ALA B 1 201 ? 30.26500  18.81000  21.50400 1.000 18.97000 ? 195 ALA B C   1 
ATOM   4138 O  O   . ALA B 1 201 ? 30.38100  19.94600  21.04700 1.000 18.23000 ? 195 ALA B O   1 
ATOM   4139 C  CB  . ALA B 1 201 ? 27.92000  18.45300  22.29900 1.000 18.25000 ? 195 ALA B CB  1 
ATOM   4140 N  N   . PHE B 1 202 ? 30.86500  17.75400  20.97000 1.000 18.07000 ? 196 PHE B N   1 
ATOM   4141 C  CA  . PHE B 1 202 ? 31.66900  17.86600  19.75800 1.000 16.85000 ? 196 PHE B CA  1 
ATOM   4142 C  C   . PHE B 1 202 ? 31.79000  16.47000  19.15100 1.000 16.90000 ? 196 PHE B C   1 
ATOM   4143 O  O   . PHE B 1 202 ? 31.32500  15.49300  19.75300 1.000 18.18000 ? 196 PHE B O   1 
ATOM   4144 C  CB  . PHE B 1 202 ? 33.04000  18.50400  20.07000 1.000 17.81000 ? 196 PHE B CB  1 
ATOM   4145 C  CG  . PHE B 1 202 ? 33.68100  18.00600  21.36400 1.000 18.23000 ? 196 PHE B CG  1 
ATOM   4146 C  CD1 . PHE B 1 202 ? 34.31400  16.76300  21.41400 1.000 17.20000 ? 196 PHE B CD1 1 
ATOM   4147 C  CD2 . PHE B 1 202 ? 33.68200  18.81000  22.51600 1.000 17.08000 ? 196 PHE B CD2 1 
ATOM   4148 C  CE1 . PHE B 1 202 ? 34.95000  16.29400  22.59600 1.000 17.38000 ? 196 PHE B CE1 1 
ATOM   4149 C  CE2 . PHE B 1 202 ? 34.28900  18.35700  23.71500 1.000 18.14000 ? 196 PHE B CE2 1 
ATOM   4150 C  CZ  . PHE B 1 202 ? 34.93800  17.09700  23.75500 1.000 17.38000 ? 196 PHE B CZ  1 
ATOM   4151 N  N   . PRO B 1 203 ? 32.34000  16.34200  17.92900 1.000 17.13000 ? 197 PRO B N   1 
ATOM   4152 C  CA  . PRO B 1 203 ? 32.43000  15.00500  17.31500 1.000 16.42000 ? 197 PRO B CA  1 
ATOM   4153 C  C   . PRO B 1 203 ? 33.23800  14.04100  18.17600 1.000 16.04000 ? 197 PRO B C   1 
ATOM   4154 O  O   . PRO B 1 203 ? 34.24900  14.40900  18.77700 1.000 15.64000 ? 197 PRO B O   1 
ATOM   4155 C  CB  . PRO B 1 203 ? 33.10400  15.27500  15.95300 1.000 15.37000 ? 197 PRO B CB  1 
ATOM   4156 C  CG  . PRO B 1 203 ? 32.70900  16.71100  15.62800 1.000 18.59000 ? 197 PRO B CG  1 
ATOM   4157 C  CD  . PRO B 1 203 ? 32.72900  17.41800  16.97600 1.000 18.64000 ? 197 PRO B CD  1 
ATOM   4158 N  N   . LEU B 1 204 ? 32.77500  12.78000  18.21800 1.000 18.15000 ? 198 LEU B N   1 
ATOM   4159 C  CA  . LEU B 1 204 ? 33.29800  11.81300  19.18100 1.000 15.66000 ? 198 LEU B CA  1 
ATOM   4160 C  C   . LEU B 1 204 ? 34.80600  11.62700  19.00200 1.000 16.55000 ? 198 LEU B C   1 
ATOM   4161 O  O   . LEU B 1 204 ? 35.55200  11.44900  19.97800 1.000 17.28000 ? 198 LEU B O   1 
ATOM   4162 C  CB  . LEU B 1 204 ? 32.52600  10.48100  19.03300 1.000 13.25000 ? 198 LEU B CB  1 
ATOM   4163 C  CG  . LEU B 1 204 ? 32.96700  9.29400   19.89000 1.000 13.44000 ? 198 LEU B CG  1 
ATOM   4164 C  CD1 . LEU B 1 204 ? 32.75900  9.61300   21.37600 1.000 12.69000 ? 198 LEU B CD1 1 
ATOM   4165 C  CD2 . LEU B 1 204 ? 32.21900  7.99500   19.51000 1.000 14.64000 ? 198 LEU B CD2 1 
ATOM   4166 N  N   . ASP B 1 205 ? 35.28700  11.66800  17.75800 1.000 19.10000 ? 199 ASP B N   1 
ATOM   4167 C  CA  . ASP B 1 205 ? 36.70900  11.42100  17.55100 1.000 18.64000 ? 199 ASP B CA  1 
ATOM   4168 C  C   . ASP B 1 205 ? 37.56000  12.51000  18.20000 1.000 16.80000 ? 199 ASP B C   1 
ATOM   4169 O  O   . ASP B 1 205 ? 38.71700  12.25800  18.56500 1.000 17.49000 ? 199 ASP B O   1 
ATOM   4170 C  CB  . ASP B 1 205 ? 37.03800  11.34900  16.06000 1.000 19.99000 ? 199 ASP B CB  1 
ATOM   4171 C  CG  . ASP B 1 205 ? 36.80000  12.69600  15.36300 1.000 23.09000 ? 199 ASP B CG  1 
ATOM   4172 O  OD1 . ASP B 1 205 ? 35.63200  13.13800  15.34700 1.000 24.67000 ? 199 ASP B OD1 1 
ATOM   4173 O  OD2 . ASP B 1 205 ? 37.75700  13.35900  14.89400 1.000 24.63000 ? 199 ASP B OD2 1 
ATOM   4174 N  N   . ARG B 1 206 ? 37.03800  13.73900  18.30300 1.000 15.77000 ? 200 ARG B N   1 
ATOM   4175 C  CA  . ARG B 1 206 ? 37.82200  14.77600  18.95300 1.000 17.16000 ? 200 ARG B CA  1 
ATOM   4176 C  C   . ARG B 1 206 ? 37.93700  14.55700  20.46000 1.000 17.56000 ? 200 ARG B C   1 
ATOM   4177 O  O   . ARG B 1 206 ? 38.87500  15.08800  21.06700 1.000 18.22000 ? 200 ARG B O   1 
ATOM   4178 C  CB  . ARG B 1 206 ? 37.22300  16.14800  18.65200 1.000 18.98000 ? 200 ARG B CB  1 
ATOM   4179 C  CG  . ARG B 1 206 ? 37.01200  16.39500  17.17000 1.000 18.74000 ? 200 ARG B CG  1 
ATOM   4180 C  CD  . ARG B 1 206 ? 38.32500  16.47500  16.46700 1.000 21.51000 ? 200 ARG B CD  1 
ATOM   4181 N  NE  . ARG B 1 206 ? 38.14800  16.60100  15.02400 1.000 26.19000 ? 200 ARG B NE  1 
ATOM   4182 C  CZ  . ARG B 1 206 ? 38.56400  17.61800  14.27800 1.000 26.94000 ? 200 ARG B CZ  1 
ATOM   4183 N  NH1 . ARG B 1 206 ? 39.11300  18.69400  14.81000 1.000 22.15000 ? 200 ARG B NH1 1 
ATOM   4184 N  NH2 . ARG B 1 206 ? 38.45400  17.53400  12.95700 1.000 28.37000 ? 200 ARG B NH2 1 
ATOM   4185 N  N   . LEU B 1 207 ? 37.00100  13.81000  21.06800 1.000 14.88000 ? 201 LEU B N   1 
ATOM   4186 C  CA  . LEU B 1 207 ? 37.19800  13.32900  22.43000 1.000 15.88000 ? 201 LEU B CA  1 
ATOM   4187 C  C   . LEU B 1 207 ? 38.40000  12.40300  22.49600 1.000 17.39000 ? 201 LEU B C   1 
ATOM   4188 O  O   . LEU B 1 207 ? 39.26400  12.54600  23.36400 1.000 17.06000 ? 201 LEU B O   1 
ATOM   4189 C  CB  . LEU B 1 207 ? 35.93800  12.61000  22.93200 1.000 14.95000 ? 201 LEU B CB  1 
ATOM   4190 C  CG  . LEU B 1 207 ? 35.98500  12.21400  24.42000 1.000 13.59000 ? 201 LEU B CG  1 
ATOM   4191 C  CD1 . LEU B 1 207 ? 36.32700  13.42200  25.35900 1.000 15.82000 ? 201 LEU B CD1 1 
ATOM   4192 C  CD2 . LEU B 1 207 ? 34.69200  11.56500  24.80700 1.000 14.02000 ? 201 LEU B CD2 1 
ATOM   4193 N  N   . GLY B 1 208 ? 38.48700  11.44800  21.57000 1.000 17.44000 ? 202 GLY B N   1 
ATOM   4194 C  CA  . GLY B 1 208 ? 39.70600  10.66400  21.47100 1.000 17.67000 ? 202 GLY B CA  1 
ATOM   4195 C  C   . GLY B 1 208 ? 40.93800  11.53700  21.28000 1.000 17.11000 ? 202 GLY B C   1 
ATOM   4196 O  O   . GLY B 1 208 ? 42.00800  11.25500  21.82800 1.000 17.86000 ? 202 GLY B O   1 
ATOM   4197 N  N   . ARG B 1 209 ? 40.79100  12.64100  20.54300 1.000 17.46000 ? 203 ARG B N   1 
ATOM   4198 C  CA  . ARG B 1 209 ? 41.93900  13.46500  20.24200 1.000 17.72000 ? 203 ARG B CA  1 
ATOM   4199 C  C   . ARG B 1 209 ? 42.46100  14.14700  21.50700 1.000 18.82000 ? 203 ARG B C   1 
ATOM   4200 O  O   . ARG B 1 209 ? 43.67000  14.20000  21.73200 1.000 19.30000 ? 203 ARG B O   1 
ATOM   4201 C  CB  . ARG B 1 209 ? 41.58100  14.49500  19.16300 1.000 16.84000 ? 203 ARG B CB  1 
ATOM   4202 C  CG  . ARG B 1 209 ? 42.77000  15.35100  18.77500 1.000 21.45000 ? 203 ARG B CG  1 
ATOM   4203 C  CD  . ARG B 1 209 ? 42.46500  16.48200  17.76300 1.000 21.00000 ? 203 ARG B CD  1 
ATOM   4204 N  NE  . ARG B 1 209 ? 41.84300  15.96500  16.54400 1.000 20.86000 ? 203 ARG B NE  1 
ATOM   4205 C  CZ  . ARG B 1 209 ? 42.02400  16.48400  15.33500 1.000 25.18000 ? 203 ARG B CZ  1 
ATOM   4206 N  NH1 . ARG B 1 209 ? 42.78800  17.56000  15.14100 1.000 22.05000 ? 203 ARG B NH1 1 
ATOM   4207 N  NH2 . ARG B 1 209 ? 41.45900  15.88900  14.29000 1.000 24.93000 ? 203 ARG B NH2 1 
ATOM   4208 N  N   . ILE B 1 210 ? 41.55900  14.60900  22.36900 1.000 17.35000 ? 204 ILE B N   1 
ATOM   4209 C  CA  . ILE B 1 210 ? 41.95900  15.20900  23.63800 1.000 19.90000 ? 204 ILE B CA  1 
ATOM   4210 C  C   . ILE B 1 210 ? 42.78000  14.23000  24.46000 1.000 18.22000 ? 204 ILE B C   1 
ATOM   4211 O  O   . ILE B 1 210 ? 43.82200  14.58600  25.03300 1.000 19.19000 ? 204 ILE B O   1 
ATOM   4212 C  CB  . ILE B 1 210 ? 40.71300  15.67200  24.41600 1.000 17.09000 ? 204 ILE B CB  1 
ATOM   4213 C  CG1 . ILE B 1 210 ? 39.99700  16.81800  23.68300 1.000 19.01000 ? 204 ILE B CG1 1 
ATOM   4214 C  CG2 . ILE B 1 210 ? 41.10600  16.12400  25.80500 1.000 17.84000 ? 204 ILE B CG2 1 
ATOM   4215 C  CD1 . ILE B 1 210 ? 38.60000  17.01400  24.20400 1.000 16.35000 ? 204 ILE B CD1 1 
ATOM   4216 N  N   . TYR B 1 211 ? 42.35700  12.97400  24.50300 1.000 18.07000 ? 205 TYR B N   1 
ATOM   4217 C  CA  . TYR B 1 211 ? 43.08400  12.02800  25.33700 1.000 17.03000 ? 205 TYR B CA  1 
ATOM   4218 C  C   . TYR B 1 211 ? 44.35700  11.52100  24.67000 1.000 16.99000 ? 205 TYR B C   1 
ATOM   4219 O  O   . TYR B 1 211 ? 45.34500  11.24100  25.36100 1.000 18.96000 ? 205 TYR B O   1 
ATOM   4220 C  CB  . TYR B 1 211 ? 42.14100  10.88400  25.71300 1.000 14.86000 ? 205 TYR B CB  1 
ATOM   4221 C  CG  . TYR B 1 211 ? 41.23400  11.30900  26.85000 1.000 15.81000 ? 205 TYR B CG  1 
ATOM   4222 C  CD1 . TYR B 1 211 ? 40.24600  12.25200  26.64800 1.000 15.11000 ? 205 TYR B CD1 1 
ATOM   4223 C  CD2 . TYR B 1 211 ? 41.37300  10.75200  28.13000 1.000 15.48000 ? 205 TYR B CD2 1 
ATOM   4224 C  CE1 . TYR B 1 211 ? 39.40800  12.64300  27.67700 1.000 15.14000 ? 205 TYR B CE1 1 
ATOM   4225 C  CE2 . TYR B 1 211 ? 40.52800  11.13600  29.15700 1.000 17.20000 ? 205 TYR B CE2 1 
ATOM   4226 C  CZ  . TYR B 1 211 ? 39.54800  12.08600  28.91900 1.000 17.20000 ? 205 TYR B CZ  1 
ATOM   4227 O  OH  . TYR B 1 211 ? 38.69000  12.50800  29.93000 1.000 19.94000 ? 205 TYR B OH  1 
ATOM   4228 N  N   . ALA B 1 212 ? 44.41000  11.47800  23.33700 1.000 17.73000 ? 206 ALA B N   1 
ATOM   4229 C  CA  . ALA B 1 212 ? 45.70400  11.22400  22.69800 1.000 17.84000 ? 206 ALA B CA  1 
ATOM   4230 C  C   . ALA B 1 212 ? 46.70000  12.33600  23.00200 1.000 22.00000 ? 206 ALA B C   1 
ATOM   4231 O  O   . ALA B 1 212 ? 47.91100  12.08100  23.12000 1.000 20.94000 ? 206 ALA B O   1 
ATOM   4232 C  CB  . ALA B 1 212 ? 45.53200  11.04900  21.18900 1.000 17.95000 ? 206 ALA B CB  1 
ATOM   4233 N  N   . LYS B 1 213 ? 46.22900  13.57700  23.14100 1.000 17.59000 ? 207 LYS B N   1 
ATOM   4234 C  CA  . LYS B 1 213 ? 47.15700  14.64400  23.48100 1.000 19.94000 ? 207 LYS B CA  1 
ATOM   4235 C  C   . LYS B 1 213 ? 47.60000  14.56600  24.94200 1.000 20.69000 ? 207 LYS B C   1 
ATOM   4236 O  O   . LYS B 1 213 ? 48.74400  14.91500  25.25600 1.000 24.42000 ? 207 LYS B O   1 
ATOM   4237 C  CB  . LYS B 1 213 ? 46.53300  15.99800  23.19300 1.000 19.29000 ? 207 LYS B CB  1 
ATOM   4238 C  CG  . LYS B 1 213 ? 46.31200  16.28900  21.73200 1.000 22.21000 ? 207 LYS B CG  1 
ATOM   4239 C  CD  . LYS B 1 213 ? 45.68700  17.66900  21.56200 1.000 23.21000 ? 207 LYS B CD  1 
ATOM   4240 C  CE  . LYS B 1 213 ? 45.69300  18.10300  20.09100 1.000 22.44000 ? 207 LYS B CE  1 
ATOM   4241 N  NZ  . LYS B 1 213 ? 44.92900  19.36300  19.89300 1.000 24.65000 ? 207 LYS B NZ  1 
ATOM   4242 N  N   . LEU B 1 214 ? 46.71900  14.12900  25.84200 1.000 17.90000 ? 208 LEU B N   1 
ATOM   4243 C  CA  . LEU B 1 214 ? 47.11000  13.94400  27.24200 1.000 21.15000 ? 208 LEU B CA  1 
ATOM   4244 C  C   . LEU B 1 214 ? 48.22900  12.92400  27.35400 1.000 20.22000 ? 208 LEU B C   1 
ATOM   4245 O  O   . LEU B 1 214 ? 49.24000  13.15300  28.02100 1.000 22.02000 ? 208 LEU B O   1 
ATOM   4246 C  CB  . LEU B 1 214 ? 45.90700  13.48500  28.07500 1.000 19.53000 ? 208 LEU B CB  1 
ATOM   4247 C  CG  . LEU B 1 214 ? 44.96200  14.53400  28.67100 1.000 20.91000 ? 208 LEU B CG  1 
ATOM   4248 C  CD1 . LEU B 1 214 ? 43.74000  13.82800  29.19400 1.000 20.27000 ? 208 LEU B CD1 1 
ATOM   4249 C  CD2 . LEU B 1 214 ? 45.69800  15.27600  29.82000 1.000 23.28000 ? 208 LEU B CD2 1 
ATOM   4250 N  N   . ALA B 1 215 ? 48.05700  11.78600  26.70500 1.000 21.95000 ? 209 ALA B N   1 
ATOM   4251 C  CA  . ALA B 1 215 ? 49.04800  10.72100  26.79100 1.000 20.50000 ? 209 ALA B CA  1 
ATOM   4252 C  C   . ALA B 1 215 ? 50.33400  11.09400  26.06400 1.000 22.38000 ? 209 ALA B C   1 
ATOM   4253 O  O   . ALA B 1 215 ? 51.44400  10.75400  26.51500 1.000 25.02000 ? 209 ALA B O   1 
ATOM   4254 C  CB  . ALA B 1 215 ? 48.42900  9.43500   26.22500 1.000 20.18000 ? 209 ALA B CB  1 
ATOM   4255 N  N   . SER B 1 216 ? 50.21300  11.83100  24.96400 1.000 22.04000 ? 210 SER B N   1 
ATOM   4256 C  CA  . SER B 1 216 ? 51.40100  12.28900  24.24400 1.000 23.39000 ? 210 SER B CA  1 
ATOM   4257 C  C   . SER B 1 216 ? 52.22200  13.23500  25.10000 1.000 21.67000 ? 210 SER B C   1 
ATOM   4258 O  O   . SER B 1 216 ? 53.45500  13.16100  25.12700 1.000 24.61000 ? 210 SER B O   1 
ATOM   4259 C  CB  . SER B 1 216 ? 50.96400  12.97400  22.95300 1.000 20.46000 ? 210 SER B CB  1 
ATOM   4260 O  OG  . SER B 1 216 ? 52.09500  13.26900  22.19400 1.000 26.62000 ? 210 SER B OG  1 
ATOM   4261 N  N   . ALA B 1 217 ? 51.55500  14.15100  25.79500 1.000 22.97000 ? 211 ALA B N   1 
ATOM   4262 C  CA  . ALA B 1 217 ? 52.25400  15.04500  26.71300 1.000 22.87000 ? 211 ALA B CA  1 
ATOM   4263 C  C   . ALA B 1 217 ? 52.94900  14.26600  27.82600 1.000 26.98000 ? 211 ALA B C   1 
ATOM   4264 O  O   . ALA B 1 217 ? 54.07500  14.59900  28.22700 1.000 28.57000 ? 211 ALA B O   1 
ATOM   4265 C  CB  . ALA B 1 217 ? 51.25700  16.05100  27.28900 1.000 23.72000 ? 211 ALA B CB  1 
ATOM   4266 N  N   . ALA B 1 218 ? 52.29400  13.22300  28.33700 1.000 25.47000 ? 212 ALA B N   1 
ATOM   4267 C  CA  . ALA B 1 218 ? 52.93200  12.34100  29.30700 1.000 21.95000 ? 212 ALA B CA  1 
ATOM   4268 C  C   . ALA B 1 218 ? 54.19700  11.72100  28.73500 1.000 26.11000 ? 212 ALA B C   1 
ATOM   4269 O  O   . ALA B 1 218 ? 55.23200  11.67200  29.41200 1.000 28.09000 ? 212 ALA B O   1 
ATOM   4270 C  CB  . ALA B 1 218 ? 51.93800  11.26200  29.74800 1.000 22.74000 ? 212 ALA B CB  1 
ATOM   4271 N  N   . ASP B 1 219 ? 54.15100  11.26000  27.47700 1.000 26.25000 ? 213 ASP B N   1 
ATOM   4272 C  CA  . ASP B 1 219 ? 55.36600  10.72100  26.85700 1.000 25.33000 ? 213 ASP B CA  1 
ATOM   4273 C  C   . ASP B 1 219 ? 56.44900  11.78700  26.70600 1.000 26.48000 ? 213 ASP B C   1 
ATOM   4274 O  O   . ASP B 1 219 ? 57.63100  11.51100  26.92100 1.000 28.38000 ? 213 ASP B O   1 
ATOM   4275 C  CB  . ASP B 1 219 ? 55.05100  10.11400  25.49500 1.000 25.63000 ? 213 ASP B CB  1 
ATOM   4276 C  CG  . ASP B 1 219 ? 54.30700  8.78900   25.59100 1.000 29.48000 ? 213 ASP B CG  1 
ATOM   4277 O  OD1 . ASP B 1 219 ? 54.41000  8.09900   26.64300 1.000 31.41000 ? 213 ASP B OD1 1 
ATOM   4278 O  OD2 . ASP B 1 219 ? 53.65000  8.42300   24.59000 1.000 24.49000 ? 213 ASP B OD2 1 
ATOM   4279 N  N   . GLY B 1 220 ? 56.08400  13.00400  26.31200 1.000 26.35000 ? 214 GLY B N   1 
ATOM   4280 C  CA  . GLY B 1 220 ? 57.11000  14.02300  26.13800 1.000 28.14000 ? 214 GLY B CA  1 
ATOM   4281 C  C   . GLY B 1 220 ? 57.76800  14.37500  27.46200 1.000 38.76000 ? 214 GLY B C   1 
ATOM   4282 O  O   . GLY B 1 220 ? 58.98000  14.60600  27.53200 1.000 39.56000 ? 214 GLY B O   1 
ATOM   4283 N  N   . SER B 1 221 ? 56.98000  14.38600  28.53600 1.000 31.02000 ? 215 SER B N   1 
ATOM   4284 C  CA  . SER B 1 221 ? 57.50500  14.73400  29.84600 1.000 34.05000 ? 215 SER B CA  1 
ATOM   4285 C  C   . SER B 1 221 ? 58.43900  13.64500  30.36100 1.000 39.17000 ? 215 SER B C   1 
ATOM   4286 O  O   . SER B 1 221 ? 59.56700  13.93500  30.78000 1.000 35.61000 ? 215 SER B O   1 
ATOM   4287 C  CB  . SER B 1 221 ? 56.35100  14.97300  30.82300 1.000 31.37000 ? 215 SER B CB  1 
ATOM   4288 O  OG  . SER B 1 221 ? 56.85100  15.08300  32.15400 1.000 39.24000 ? 215 SER B OG  1 
ATOM   4289 N  N   . ASP B 1 222 ? 57.99200  12.37800  30.28900 1.000 35.30000 ? 216 ASP B N   1 
ATOM   4290 C  CA  . ASP B 1 222 ? 58.79700  11.24200  30.74700 1.000 40.66000 ? 216 ASP B CA  1 
ATOM   4291 C  C   . ASP B 1 222 ? 60.13500  11.17200  30.02600 1.000 37.59000 ? 216 ASP B C   1 
ATOM   4292 O  O   . ASP B 1 222 ? 61.14000  10.73500  30.60600 1.000 40.88000 ? 216 ASP B O   1 
ATOM   4293 C  CB  . ASP B 1 222 ? 58.00700  9.93600   30.54100 1.000 37.83000 ? 216 ASP B CB  1 
ATOM   4294 C  CG  . ASP B 1 222 ? 58.35400  8.84300   31.57900 1.000 42.28000 ? 216 ASP B CG  1 
ATOM   4295 O  OD1 . ASP B 1 222 ? 59.03000  9.14700   32.58200 1.000 49.14000 ? 216 ASP B OD1 1 
ATOM   4296 O  OD2 . ASP B 1 222 ? 57.95200  7.66700   31.39400 1.000 49.20000 ? 216 ASP B OD2 1 
ATOM   4297 N  N   . ALA B 1 223 ? 60.16800  11.60000  28.76400 1.000 40.54000 ? 217 ALA B N   1 
ATOM   4298 C  CA  . ALA B 1 223 ? 61.36400  11.57900  27.93200 1.000 42.00000 ? 217 ALA B CA  1 
ATOM   4299 C  C   . ALA B 1 223 ? 62.31800  12.74600  28.20600 1.000 48.23000 ? 217 ALA B C   1 
ATOM   4300 O  O   . ALA B 1 223 ? 63.40900  12.78500  27.62000 1.000 47.74000 ? 217 ALA B O   1 
ATOM   4301 C  CB  . ALA B 1 223 ? 60.95900  11.58400  26.45500 1.000 43.52000 ? 217 ALA B CB  1 
ATOM   4302 N  N   . GLY B 1 224 ? 61.95200  13.68400  29.08000 1.000 45.04000 ? 218 GLY B N   1 
ATOM   4303 C  CA  . GLY B 1 224 ? 62.82400  14.81000  29.33800 1.000 48.64000 ? 218 GLY B CA  1 
ATOM   4304 C  C   . GLY B 1 224 ? 62.80000  15.87700  28.27400 1.000 53.68000 ? 218 GLY B C   1 
ATOM   4305 O  O   . GLY B 1 224 ? 63.67900  16.75200  28.27300 1.000 54.26000 ? 218 GLY B O   1 
ATOM   4306 N  N   . GLU B 1 225 ? 61.80900  15.84400  27.38300 1.000 58.38000 ? 219 GLU B N   1 
ATOM   4307 C  CA  . GLU B 1 225 ? 61.70900  16.82100  26.30800 1.000 60.93000 ? 219 GLU B CA  1 
ATOM   4308 C  C   . GLU B 1 225 ? 61.23600  18.16600  26.84500 1.000 60.93000 ? 219 GLU B C   1 
ATOM   4309 O  O   . GLU B 1 225 ? 60.35000  18.23400  27.70700 1.000 59.85000 ? 219 GLU B O   1 
ATOM   4310 C  CB  . GLU B 1 225 ? 60.74200  16.32700  25.23000 1.000 58.77000 ? 219 GLU B CB  1 
ATOM   4311 C  CG  . GLU B 1 225 ? 61.02300  14.90100  24.75100 1.000 58.17000 ? 219 GLU B CG  1 
ATOM   4312 C  CD  . GLU B 1 225 ? 60.00100  14.40100  23.73100 1.000 62.25000 ? 219 GLU B CD  1 
ATOM   4313 O  OE1 . GLU B 1 225 ? 58.88100  14.97200  23.64300 1.000 60.64000 ? 219 GLU B OE1 1 
ATOM   4314 O  OE2 . GLU B 1 225 ? 60.33300  13.43500  23.00800 1.000 68.12000 ? 219 GLU B OE2 1 
ATOM   4315 N  N   . GLY B 1 226 ? 61.85300  19.23600  26.34400 1.000 53.54000 ? 220 GLY B N   1 
ATOM   4316 C  CA  . GLY B 1 226 ? 61.30000  20.56300  26.55600 1.000 48.04000 ? 220 GLY B CA  1 
ATOM   4317 C  C   . GLY B 1 226 ? 59.87200  20.62600  26.03800 1.000 46.51000 ? 220 GLY B C   1 
ATOM   4318 O  O   . GLY B 1 226 ? 59.55200  20.08100  24.97800 1.000 45.04000 ? 220 GLY B O   1 
ATOM   4319 N  N   . GLN B 1 227 ? 59.00000  21.27600  26.81500 1.000 43.43000 ? 221 GLN B N   1 
ATOM   4320 C  CA  . GLN B 1 227 ? 57.56600  21.28300  26.55500 1.000 40.62000 ? 221 GLN B CA  1 
ATOM   4321 C  C   . GLN B 1 227 ? 57.02700  22.69700  26.70600 1.000 37.04000 ? 221 GLN B C   1 
ATOM   4322 O  O   . GLN B 1 227 ? 57.51100  23.48700  27.52900 1.000 33.80000 ? 221 GLN B O   1 
ATOM   4323 C  CB  . GLN B 1 227 ? 56.80100  20.33000  27.51300 1.000 35.08000 ? 221 GLN B CB  1 
ATOM   4324 C  CG  . GLN B 1 227 ? 57.01200  18.82200  27.23400 1.000 39.01000 ? 221 GLN B CG  1 
ATOM   4325 C  CD  . GLN B 1 227 ? 56.03500  17.92400  27.99100 1.000 38.94000 ? 221 GLN B CD  1 
ATOM   4326 O  OE1 . GLN B 1 227 ? 55.91300  18.02700  29.21400 1.000 37.17000 ? 221 GLN B OE1 1 
ATOM   4327 N  NE2 . GLN B 1 227 ? 55.31400  17.05100  27.26100 1.000 32.51000 ? 221 GLN B NE2 1 
ATOM   4328 N  N   . SER B 1 228 ? 56.01900  23.01200  25.89800 1.000 34.32000 ? 222 SER B N   1 
ATOM   4329 C  CA  . SER B 1 228 ? 55.28800  24.24000  26.12200 1.000 32.48000 ? 222 SER B CA  1 
ATOM   4330 C  C   . SER B 1 228 ? 54.62800  24.18800  27.49500 1.000 34.01000 ? 222 SER B C   1 
ATOM   4331 O  O   . SER B 1 228 ? 54.47200  23.12500  28.10000 1.000 32.19000 ? 222 SER B O   1 
ATOM   4332 C  CB  . SER B 1 228 ? 54.21900  24.41600  25.05600 1.000 33.15000 ? 222 SER B CB  1 
ATOM   4333 O  OG  . SER B 1 228 ? 53.30500  23.34400  25.15600 1.000 36.12000 ? 222 SER B OG  1 
ATOM   4334 N  N   . THR B 1 229 ? 54.23200  25.35500  27.99900 1.000 30.87000 ? 223 THR B N   1 
ATOM   4335 C  CA  . THR B 1 229 ? 53.46800  25.34700  29.23900 1.000 29.23000 ? 223 THR B CA  1 
ATOM   4336 C  C   . THR B 1 229 ? 52.22800  24.45100  29.12700 1.000 30.42000 ? 223 THR B C   1 
ATOM   4337 O  O   . THR B 1 229 ? 51.86100  23.77600  30.09600 1.000 30.74000 ? 223 THR B O   1 
ATOM   4338 C  CB  . THR B 1 229 ? 53.08100  26.78200  29.63400 1.000 32.61000 ? 223 THR B CB  1 
ATOM   4339 O  OG1 . THR B 1 229 ? 52.39200  27.40700  28.54400 1.000 32.02000 ? 223 THR B OG1 1 
ATOM   4340 C  CG2 . THR B 1 229 ? 54.31700  27.61700  30.03500 1.000 27.97000 ? 223 THR B CG2 1 
ATOM   4341 N  N   . ARG B 1 230 ? 51.57200  24.41500  27.95200 1.000 27.00000 ? 224 ARG B N   1 
ATOM   4342 C  CA  . ARG B 1 230 ? 50.35300  23.61300  27.81900 1.000 29.17000 ? 224 ARG B CA  1 
ATOM   4343 C  C   . ARG B 1 230 ? 50.65500  22.12000  27.86300 1.000 28.23000 ? 224 ARG B C   1 
ATOM   4344 O  O   . ARG B 1 230 ? 49.96000  21.35500  28.54200 1.000 24.09000 ? 224 ARG B O   1 
ATOM   4345 C  CB  . ARG B 1 230 ? 49.60400  23.93900  26.52500 1.000 27.14000 ? 224 ARG B CB  1 
ATOM   4346 C  CG  . ARG B 1 230 ? 48.45300  22.94900  26.30800 1.000 23.63000 ? 224 ARG B CG  1 
ATOM   4347 C  CD  . ARG B 1 230 ? 47.37300  23.51300  25.45500 1.000 29.12000 ? 224 ARG B CD  1 
ATOM   4348 N  NE  . ARG B 1 230 ? 46.67600  24.63400  26.07400 1.000 28.67000 ? 224 ARG B NE  1 
ATOM   4349 C  CZ  . ARG B 1 230 ? 45.72500  25.33600  25.46600 1.000 32.77000 ? 224 ARG B CZ  1 
ATOM   4350 N  NH1 . ARG B 1 230 ? 45.33100  25.03500  24.24500 1.000 28.49000 ? 224 ARG B NH1 1 
ATOM   4351 N  NH2 . ARG B 1 230 ? 45.17900  26.38500  26.09200 1.000 28.37000 ? 224 ARG B NH2 1 
ATOM   4352 N  N   . CYS B 1 231 ? 51.68000  21.68100  27.12600 1.000 29.46000 ? 225 CYS B N   1 
ATOM   4353 C  CA  . CYS B 1 231 ? 52.04100  20.27100  27.17300 1.000 27.49000 ? 225 CYS B CA  1 
ATOM   4354 C  C   . CYS B 1 231 ? 52.48700  19.86900  28.57600 1.000 25.81000 ? 225 CYS B C   1 
ATOM   4355 O  O   . CYS B 1 231 ? 52.12800  18.79000  29.04800 1.000 24.46000 ? 225 CYS B O   1 
ATOM   4356 C  CB  . CYS B 1 231 ? 53.11800  19.97500  26.13200 1.000 30.95000 ? 225 CYS B CB  1 
ATOM   4357 S  SG  . CYS B 1 231 ? 52.44100  19.77200  24.43500 1.000 47.40000 ? 225 CYS B SG  1 
ATOM   4358 N  N   . ALA B 1 232 ? 53.23600  20.73900  29.27100 1.000 27.14000 ? 226 ALA B N   1 
ATOM   4359 C  CA  . ALA B 1 232 ? 53.60600  20.44000  30.65400 1.000 26.69000 ? 226 ALA B CA  1 
ATOM   4360 C  C   . ALA B 1 232 ? 52.36200  20.27900  31.51800 1.000 28.62000 ? 226 ALA B C   1 
ATOM   4361 O  O   . ALA B 1 232 ? 52.27600  19.35300  32.33000 1.000 26.73000 ? 226 ALA B O   1 
ATOM   4362 C  CB  . ALA B 1 232 ? 54.51800  21.52900  31.22100 1.000 26.97000 ? 226 ALA B CB  1 
ATOM   4363 N  N   . ALA B 1 233 ? 51.35600  21.13500  31.31500 1.000 26.42000 ? 227 ALA B N   1 
ATOM   4364 C  CA  . ALA B 1 233 ? 50.14000  21.04200  32.11100 1.000 25.87000 ? 227 ALA B CA  1 
ATOM   4365 C  C   . ALA B 1 233 ? 49.32900  19.79200  31.77000 1.000 26.73000 ? 227 ALA B C   1 
ATOM   4366 O  O   . ALA B 1 233 ? 48.70200  19.18900  32.65200 1.000 22.29000 ? 227 ALA B O   1 
ATOM   4367 C  CB  . ALA B 1 233 ? 49.30400  22.30300  31.91100 1.000 23.66000 ? 227 ALA B CB  1 
ATOM   4368 N  N   . LEU B 1 234 ? 49.30600  19.40000  30.49400 1.000 23.03000 ? 228 LEU B N   1 
ATOM   4369 C  CA  . LEU B 1 234 ? 48.65400  18.15200  30.12200 1.000 24.11000 ? 228 LEU B CA  1 
ATOM   4370 C  C   . LEU B 1 234 ? 49.37300  16.93900  30.71200 1.000 21.49000 ? 228 LEU B C   1 
ATOM   4371 O  O   . LEU B 1 234 ? 48.72100  15.95600  31.11200 1.000 19.99000 ? 228 LEU B O   1 
ATOM   4372 C  CB  . LEU B 1 234 ? 48.57800  18.04400  28.60100 1.000 24.08000 ? 228 LEU B CB  1 
ATOM   4373 C  CG  . LEU B 1 234 ? 47.55700  18.93100  27.90300 1.000 23.42000 ? 228 LEU B CG  1 
ATOM   4374 C  CD1 . LEU B 1 234 ? 47.87500  18.90900  26.41500 1.000 25.73000 ? 228 LEU B CD1 1 
ATOM   4375 C  CD2 . LEU B 1 234 ? 46.13400  18.46400  28.19500 1.000 16.81000 ? 228 LEU B CD2 1 
ATOM   4376 N  N   . ALA B 1 235 ? 50.70600  16.97600  30.76300 1.000 21.02000 ? 229 ALA B N   1 
ATOM   4377 C  CA  . ALA B 1 235 ? 51.43600  15.86200  31.34900 1.000 21.71000 ? 229 ALA B CA  1 
ATOM   4378 C  C   . ALA B 1 235 ? 51.14900  15.77400  32.84800 1.000 24.30000 ? 229 ALA B C   1 
ATOM   4379 O  O   . ALA B 1 235 ? 50.99300  14.68100  33.39900 1.000 26.32000 ? 229 ALA B O   1 
ATOM   4380 C  CB  . ALA B 1 235 ? 52.93900  16.01000  31.06100 1.000 21.67000 ? 229 ALA B CB  1 
ATOM   4381 N  N   . HIS B 1 236 ? 51.01800  16.92400  33.50400 1.000 24.20000 ? 230 HIS B N   1 
ATOM   4382 C  CA  . HIS B 1 236 ? 50.63100  16.95700  34.90700 1.000 25.89000 ? 230 HIS B CA  1 
ATOM   4383 C  C   . HIS B 1 236 ? 49.23800  16.36500  35.13400 1.000 25.35000 ? 230 HIS B C   1 
ATOM   4384 O  O   . HIS B 1 236 ? 49.00500  15.66800  36.13100 1.000 28.56000 ? 230 HIS B O   1 
ATOM   4385 C  CB  . HIS B 1 236 ? 50.69200  18.40000  35.40400 1.000 30.85000 ? 230 HIS B CB  1 
ATOM   4386 C  CG  . HIS B 1 236 ? 50.68600  18.52600  36.89000 1.000 34.83000 ? 230 HIS B CG  1 
ATOM   4387 N  ND1 . HIS B 1 236 ? 50.85700  19.73300  37.53500 1.000 37.69000 ? 230 HIS B ND1 1 
ATOM   4388 C  CD2 . HIS B 1 236 ? 50.55000  17.59500  37.86300 1.000 36.42000 ? 230 HIS B CD2 1 
ATOM   4389 C  CE1 . HIS B 1 236 ? 50.83000  19.54100  38.84300 1.000 38.19000 ? 230 HIS B CE1 1 
ATOM   4390 N  NE2 . HIS B 1 236 ? 50.63500  18.25400  39.06900 1.000 42.22000 ? 230 HIS B NE2 1 
ATOM   4391 N  N   . ILE B 1 237 ? 48.27900  16.66000  34.25400 1.000 23.54000 ? 231 ILE B N   1 
ATOM   4392 C  CA  . ILE B 1 237 ? 46.94700  16.06800  34.38600 1.000 23.38000 ? 231 ILE B CA  1 
ATOM   4393 C  C   . ILE B 1 237 ? 47.02800  14.55400  34.22300 1.000 22.96000 ? 231 ILE B C   1 
ATOM   4394 O  O   . ILE B 1 237 ? 46.47300  13.78800  35.02900 1.000 22.84000 ? 231 ILE B O   1 
ATOM   4395 C  CB  . ILE B 1 237 ? 45.96800  16.70200  33.37400 1.000 21.68000 ? 231 ILE B CB  1 
ATOM   4396 C  CG1 . ILE B 1 237 ? 45.62300  18.12900  33.80300 1.000 25.12000 ? 231 ILE B CG1 1 
ATOM   4397 C  CG2 . ILE B 1 237 ? 44.66000  15.95500  33.31700 1.000 20.02000 ? 231 ILE B CG2 1 
ATOM   4398 C  CD1 . ILE B 1 237 ? 45.09500  18.98700  32.66900 1.000 26.38000 ? 231 ILE B CD1 1 
ATOM   4399 N  N   . PHE B 1 238 ? 47.70800  14.09500  33.17000 1.000 22.11000 ? 232 PHE B N   1 
ATOM   4400 C  CA  . PHE B 1 238 ? 47.85500  12.65400  32.99100 1.000 19.95000 ? 232 PHE B CA  1 
ATOM   4401 C  C   . PHE B 1 238 ? 48.43800  12.00700  34.25100 1.000 24.82000 ? 232 PHE B C   1 
ATOM   4402 O  O   . PHE B 1 238 ? 47.91200  11.00900  34.76900 1.000 24.60000 ? 232 PHE B O   1 
ATOM   4403 C  CB  . PHE B 1 238 ? 48.74500  12.34800  31.77900 1.000 21.46000 ? 232 PHE B CB  1 
ATOM   4404 C  CG  . PHE B 1 238 ? 48.81800  10.86600  31.45500 1.000 21.86000 ? 232 PHE B CG  1 
ATOM   4405 C  CD1 . PHE B 1 238 ? 49.55600  10.01300  32.23500 1.000 28.01000 ? 232 PHE B CD1 1 
ATOM   4406 C  CD2 . PHE B 1 238 ? 48.11600  10.34100  30.39000 1.000 18.76000 ? 232 PHE B CD2 1 
ATOM   4407 C  CE1 . PHE B 1 238 ? 49.61200  8.65700   31.95700 1.000 24.16000 ? 232 PHE B CE1 1 
ATOM   4408 C  CE2 . PHE B 1 238 ? 48.15900  8.99100   30.11500 1.000 19.79000 ? 232 PHE B CE2 1 
ATOM   4409 C  CZ  . PHE B 1 238 ? 48.92700  8.14700   30.90400 1.000 18.57000 ? 232 PHE B CZ  1 
ATOM   4410 N  N   . ARG B 1 239 ? 49.56000  12.52700  34.71900 1.000 25.23000 ? 233 ARG B N   1 
ATOM   4411 C  CA  . ARG B 1 239 ? 50.21900  11.92500  35.86700 1.000 25.60000 ? 233 ARG B CA  1 
ATOM   4412 C  C   . ARG B 1 239 ? 49.32200  11.94800  37.10900 1.000 27.27000 ? 233 ARG B C   1 
ATOM   4413 O  O   . ARG B 1 239 ? 49.25800  10.96200  37.84900 1.000 25.82000 ? 233 ARG B O   1 
ATOM   4414 C  CB  . ARG B 1 239 ? 51.53700  12.64500  36.11900 1.000 28.38000 ? 233 ARG B CB  1 
ATOM   4415 C  CG  . ARG B 1 239 ? 52.02200  12.49800  37.52300 1.000 40.79000 ? 233 ARG B CG  1 
ATOM   4416 C  CD  . ARG B 1 239 ? 53.43500  12.99900  37.64500 1.000 50.54000 ? 233 ARG B CD  1 
ATOM   4417 N  NE  . ARG B 1 239 ? 53.58900  14.06900  38.62800 1.000 53.88000 ? 233 ARG B NE  1 
ATOM   4418 C  CZ  . ARG B 1 239 ? 54.11300  13.90300  39.83600 1.000 62.47000 ? 233 ARG B CZ  1 
ATOM   4419 N  NH1 . ARG B 1 239 ? 54.43000  12.69400  40.29300 1.000 59.86000 ? 233 ARG B NH1 1 
ATOM   4420 N  NH2 . ARG B 1 239 ? 54.32900  14.97500  40.60400 1.000 65.70000 ? 233 ARG B NH2 1 
ATOM   4421 N  N   . ALA B 1 240 ? 48.62500  13.06600  37.35900 1.000 24.25000 ? 234 ALA B N   1 
ATOM   4422 C  CA  . ALA B 1 240 ? 47.71700  13.14600  38.50700 1.000 23.53000 ? 234 ALA B CA  1 
ATOM   4423 C  C   . ALA B 1 240 ? 46.63800  12.06900  38.45800 1.000 25.48000 ? 234 ALA B C   1 
ATOM   4424 O  O   . ALA B 1 240 ? 46.32700  11.43000  39.48000 1.000 23.11000 ? 234 ALA B O   1 
ATOM   4425 C  CB  . ALA B 1 240 ? 47.06700  14.53200  38.55900 1.000 24.34000 ? 234 ALA B CB  1 
ATOM   4426 N  N   . MET B 1 241 ? 46.00500  11.88800  37.28200 1.000 22.45000 ? 235 MET B N   1 
ATOM   4427 C  CA  . MET B 1 241 ? 44.95200  10.89500  37.16000 1.000 20.18000 ? 235 MET B CA  1 
ATOM   4428 C  C   . MET B 1 241 ? 45.50400  9.49500   37.38100 1.000 23.85000 ? 235 MET B C   1 
ATOM   4429 O  O   . MET B 1 241 ? 44.89900  8.68600   38.08800 1.000 26.11000 ? 235 MET B O   1 
ATOM   4430 C  CB  . MET B 1 241 ? 44.28900  11.00000  35.78600 1.000 22.90000 ? 235 MET B CB  1 
ATOM   4431 C  CG  . MET B 1 241 ? 43.48300  12.27100  35.60500 1.000 22.17000 ? 235 MET B CG  1 
ATOM   4432 S  SD  . MET B 1 241 ? 42.76800  12.44400  33.94800 1.000 23.17000 ? 235 MET B SD  1 
ATOM   4433 C  CE  . MET B 1 241 ? 41.43000  11.23600  33.91600 1.000 18.32000 ? 235 MET B CE  1 
ATOM   4434 N  N   . ALA B 1 242 ? 46.65600  9.19500   36.78500 1.000 22.27000 ? 236 ALA B N   1 
ATOM   4435 C  CA  . ALA B 1 242 ? 47.18200  7.84400   36.85100 1.000 26.27000 ? 236 ALA B CA  1 
ATOM   4436 C  C   . ALA B 1 242 ? 47.73000  7.51900   38.23800 1.000 26.96000 ? 236 ALA B C   1 
ATOM   4437 O  O   . ALA B 1 242 ? 47.73000  6.35100   38.64600 1.000 29.64000 ? 236 ALA B O   1 
ATOM   4438 C  CB  . ALA B 1 242 ? 48.24900  7.66100   35.77900 1.000 24.66000 ? 236 ALA B CB  1 
ATOM   4439 N  N   . ARG B 1 243 ? 48.20800  8.51500   38.97700 1.000 25.56000 ? 237 ARG B N   1 
ATOM   4440 C  CA  . ARG B 1 243 ? 48.72800  8.22900   40.30600 1.000 25.14000 ? 237 ARG B CA  1 
ATOM   4441 C  C   . ARG B 1 243 ? 47.64800  8.22600   41.37600 1.000 27.84000 ? 237 ARG B C   1 
ATOM   4442 O  O   . ARG B 1 243 ? 47.83400  7.61200   42.42700 1.000 31.03000 ? 237 ARG B O   1 
ATOM   4443 C  CB  . ARG B 1 243 ? 49.82800  9.23300   40.66500 1.000 31.10000 ? 237 ARG B CB  1 
ATOM   4444 C  CG  . ARG B 1 243 ? 51.00300  9.13200   39.70900 1.000 39.15000 ? 237 ARG B CG  1 
ATOM   4445 C  CD  . ARG B 1 243 ? 52.29600  9.69700   40.29500 1.000 52.29000 ? 237 ARG B CD  1 
ATOM   4446 N  NE  . ARG B 1 243 ? 53.33200  9.77400   39.26700 1.000 62.91000 ? 237 ARG B NE  1 
ATOM   4447 C  CZ  . ARG B 1 243 ? 54.14100  8.77600   38.92400 1.000 65.28000 ? 237 ARG B CZ  1 
ATOM   4448 N  NH1 . ARG B 1 243 ? 54.10700  7.60800   39.55400 1.000 66.02000 ? 237 ARG B NH1 1 
ATOM   4449 N  NH2 . ARG B 1 243 ? 55.00600  8.95400   37.92500 1.000 59.09000 ? 237 ARG B NH2 1 
ATOM   4450 N  N   . HIS B 1 244 ? 46.52400  8.88800   41.14200 1.000 23.83000 ? 238 HIS B N   1 
ATOM   4451 C  CA  . HIS B 1 244 ? 45.45100  8.96900   42.13000 1.000 26.75000 ? 238 HIS B CA  1 
ATOM   4452 C  C   . HIS B 1 244 ? 44.13500  8.60100   41.48200 1.000 22.99000 ? 238 HIS B C   1 
ATOM   4453 O  O   . HIS B 1 244 ? 43.15600  9.35100   41.54400 1.000 23.48000 ? 238 HIS B O   1 
ATOM   4454 C  CB  . HIS B 1 244 ? 45.41300  10.36600  42.74400 1.000 26.71000 ? 238 HIS B CB  1 
ATOM   4455 C  CG  . HIS B 1 244 ? 46.70600  10.74500  43.39600 1.000 26.98000 ? 238 HIS B CG  1 
ATOM   4456 N  ND1 . HIS B 1 244 ? 47.06300  10.30200  44.65100 1.000 31.10000 ? 238 HIS B ND1 1 
ATOM   4457 C  CD2 . HIS B 1 244 ? 47.74600  11.48300  42.94800 1.000 26.88000 ? 238 HIS B CD2 1 
ATOM   4458 C  CE1 . HIS B 1 244 ? 48.25400  10.77900  44.96100 1.000 28.74000 ? 238 HIS B CE1 1 
ATOM   4459 N  NE2 . HIS B 1 244 ? 48.69100  11.49800  43.94300 1.000 29.54000 ? 238 HIS B NE2 1 
ATOM   4460 N  N   . PRO B 1 245 ? 44.05800  7.41800   40.87200 1.000 23.51000 ? 239 PRO B N   1 
ATOM   4461 C  CA  . PRO B 1 245 ? 42.83700  7.06700   40.15100 1.000 22.56000 ? 239 PRO B CA  1 
ATOM   4462 C  C   . PRO B 1 245 ? 41.64000  6.89500   41.05900 1.000 22.01000 ? 239 PRO B C   1 
ATOM   4463 O  O   . PRO B 1 245 ? 40.50600  6.93100   40.58400 1.000 24.44000 ? 239 PRO B O   1 
ATOM   4464 C  CB  . PRO B 1 245 ? 43.21100  5.75500   39.45700 1.000 25.97000 ? 239 PRO B CB  1 
ATOM   4465 C  CG  . PRO B 1 245 ? 44.18600  5.11800   40.42000 1.000 26.26000 ? 239 PRO B CG  1 
ATOM   4466 C  CD  . PRO B 1 245 ? 44.98700  6.27800   40.98200 1.000 26.91000 ? 239 PRO B CD  1 
ATOM   4467 N  N   . GLU B 1 246 ? 41.83700  6.69800   42.34400 1.000 22.48000 ? 240 GLU B N   1 
ATOM   4468 C  CA  . GLU B 1 246 ? 40.68700  6.59400   43.22400 1.000 23.27000 ? 240 GLU B CA  1 
ATOM   4469 C  C   . GLU B 1 246 ? 40.07800  7.95400   43.51000 1.000 25.59000 ? 240 GLU B C   1 
ATOM   4470 O  O   . GLU B 1 246 ? 38.91800  8.03000   43.94100 1.000 21.60000 ? 240 GLU B O   1 
ATOM   4471 C  CB  . GLU B 1 246 ? 41.09100  5.91800   44.53400 1.000 31.11000 ? 240 GLU B CB  1 
ATOM   4472 C  CG  . GLU B 1 246 ? 42.09500  6.75000   45.37300 1.000 37.30000 ? 240 GLU B CG  1 
ATOM   4473 C  CD  . GLU B 1 246 ? 43.54400  6.66400   44.86600 1.000 38.69000 ? 240 GLU B CD  1 
ATOM   4474 O  OE1 . GLU B 1 246 ? 43.87200  5.67900   44.15000 1.000 44.63000 ? 240 GLU B OE1 1 
ATOM   4475 O  OE2 . GLU B 1 246 ? 44.34600  7.57100   45.19800 1.000 42.02000 ? 240 GLU B OE2 1 
ATOM   4476 N  N   . MET B 1 247 ? 40.84800  9.02900   43.31400 1.000 23.70000 ? 241 MET B N   1 
ATOM   4477 C  CA  . MET B 1 247 ? 40.25200  10.36400  43.36200 1.000 24.70000 ? 241 MET B CA  1 
ATOM   4478 C  C   . MET B 1 247 ? 39.40500  10.62200  42.13100 1.000 22.17000 ? 241 MET B C   1 
ATOM   4479 O  O   . MET B 1 247 ? 38.39600  11.33600  42.20900 1.000 20.82000 ? 241 MET B O   1 
ATOM   4480 C  CB  . MET B 1 247 ? 41.33100  11.43700  43.48000 1.000 20.81000 ? 241 MET B CB  1 
ATOM   4481 C  CG  . MET B 1 247 ? 42.07100  11.41100  44.80000 1.000 25.44000 ? 241 MET B CG  1 
ATOM   4482 S  SD  . MET B 1 247 ? 40.98000  11.86500  46.16900 1.000 27.24000 ? 241 MET B SD  1 
ATOM   4483 C  CE  . MET B 1 247 ? 40.77200  10.30500  47.04700 1.000 25.21000 ? 241 MET B CE  1 
ATOM   4484 N  N   . VAL B 1 248 ? 39.78300  10.02300  41.00000 1.000 22.35000 ? 242 VAL B N   1 
ATOM   4485 C  CA  . VAL B 1 248 ? 39.03200  10.21600  39.76600 1.000 21.68000 ? 242 VAL B CA  1 
ATOM   4486 C  C   . VAL B 1 248 ? 37.67300  9.52100   39.83100 1.000 23.24000 ? 242 VAL B C   1 
ATOM   4487 O  O   . VAL B 1 248 ? 36.70000  10.00800  39.23900 1.000 22.67000 ? 242 VAL B O   1 
ATOM   4488 C  CB  . VAL B 1 248 ? 39.86300  9.74600   38.55800 1.000 17.65000 ? 242 VAL B CB  1 
ATOM   4489 C  CG1 . VAL B 1 248 ? 39.04100  9.83500   37.25900 1.000 16.35000 ? 242 VAL B CG1 1 
ATOM   4490 C  CG2 . VAL B 1 248 ? 41.12600  10.61200  38.44600 1.000 19.37000 ? 242 VAL B CG2 1 
ATOM   4491 N  N   . ALA B 1 249 ? 37.55400  8.40000   40.55000 1.000 22.20000 ? 243 ALA B N   1 
ATOM   4492 C  CA  . ALA B 1 249 ? 36.25100  7.75200   40.65800 1.000 18.98000 ? 243 ALA B CA  1 
ATOM   4493 C  C   . ALA B 1 249 ? 36.03500  7.23100   42.07300 1.000 23.79000 ? 243 ALA B C   1 
ATOM   4494 O  O   . ALA B 1 249 ? 35.41500  7.91900   42.89200 1.000 23.82000 ? 243 ALA B O   1 
ATOM   4495 C  CB  . ALA B 1 249 ? 36.10500  6.62100   39.62200 1.000 18.55000 ? 243 ALA B CB  1 
ATOM   4496 N  N   . GLY B 1 250 ? 36.53700  6.04200   42.38600 1.000 20.98000 ? 244 GLY B N   1 
ATOM   4497 C  CA  . GLY B 1 250 ? 36.45400  5.53400   43.74400 1.000 24.05000 ? 244 GLY B CA  1 
ATOM   4498 C  C   . GLY B 1 250 ? 36.55300  4.02200   43.76000 1.000 26.70000 ? 244 GLY B C   1 
ATOM   4499 O  O   . GLY B 1 250 ? 36.77900  3.38700   42.74000 1.000 23.81000 ? 244 GLY B O   1 
ATOM   4500 N  N   . GLU B 1 251 ? 36.39200  3.44400   44.94600 1.000 27.98000 ? 245 GLU B N   1 
ATOM   4501 C  CA  . GLU B 1 251 ? 36.60500  1.99900   45.02800 1.000 32.51000 ? 245 GLU B CA  1 
ATOM   4502 C  C   . GLU B 1 251 ? 35.52700  1.24100   44.24100 1.000 28.10000 ? 245 GLU B C   1 
ATOM   4503 O  O   . GLU B 1 251 ? 34.35600  1.64800   44.17700 1.000 23.74000 ? 245 GLU B O   1 
ATOM   4504 C  CB  . GLU B 1 251 ? 36.67300  1.53300   46.48700 1.000 35.60000 ? 245 GLU B CB  1 
ATOM   4505 C  CG  . GLU B 1 251 ? 37.83000  0.51200   46.77500 1.000 43.53000 ? 245 GLU B CG  1 
ATOM   4506 C  CD  . GLU B 1 251 ? 39.29500  1.09900   46.76300 1.000 51.18000 ? 245 GLU B CD  1 
ATOM   4507 O  OE1 . GLU B 1 251 ? 39.52900  2.32700   46.94200 1.000 45.48000 ? 245 GLU B OE1 1 
ATOM   4508 O  OE2 . GLU B 1 251 ? 40.24300  0.29400   46.58000 1.000 55.85000 ? 245 GLU B OE2 1 
ATOM   4509 N  N   . GLY B 1 252 ? 35.94900  0.16200   43.57000 1.000 25.69000 ? 246 GLY B N   1 
ATOM   4510 C  CA  . GLY B 1 252 ? 35.04200  -0.60000  42.74100 1.000 24.49000 ? 246 GLY B CA  1 
ATOM   4511 C  C   . GLY B 1 252 ? 34.62000  0.04400   41.44100 1.000 26.41000 ? 246 GLY B C   1 
ATOM   4512 O  O   . GLY B 1 252 ? 33.92300  -0.61200  40.65600 1.000 24.12000 ? 246 GLY B O   1 
ATOM   4513 N  N   . ARG B 1 253 ? 35.00000  1.29900   41.18700 1.000 20.05000 ? 247 ARG B N   1 
ATOM   4514 C  CA  . ARG B 1 253 ? 34.58200  2.00900   39.98600 1.000 21.54000 ? 247 ARG B CA  1 
ATOM   4515 C  C   . ARG B 1 253 ? 35.48300  1.65300   38.80100 1.000 20.83000 ? 247 ARG B C   1 
ATOM   4516 O  O   . ARG B 1 253 ? 36.69700  1.49000   38.94700 1.000 21.41000 ? 247 ARG B O   1 
ATOM   4517 C  CB  . ARG B 1 253 ? 34.62700  3.52700   40.22400 1.000 20.39000 ? 247 ARG B CB  1 
ATOM   4518 C  CG  . ARG B 1 253 ? 33.68000  4.03600   41.31000 1.000 23.20000 ? 247 ARG B CG  1 
ATOM   4519 C  CD  . ARG B 1 253 ? 32.26400  4.32800   40.75500 1.000 22.65000 ? 247 ARG B CD  1 
ATOM   4520 N  NE  . ARG B 1 253 ? 32.36300  5.18700   39.57600 1.000 23.55000 ? 247 ARG B NE  1 
ATOM   4521 C  CZ  . ARG B 1 253 ? 32.48400  6.51100   39.61300 1.000 26.89000 ? 247 ARG B CZ  1 
ATOM   4522 N  NH1 . ARG B 1 253 ? 32.50000  7.17900   40.76400 1.000 21.68000 ? 247 ARG B NH1 1 
ATOM   4523 N  NH2 . ARG B 1 253 ? 32.59300  7.18600   38.46800 1.000 21.48000 ? 247 ARG B NH2 1 
ATOM   4524 N  N   . TYR B 1 254 ? 34.88400  1.61000   37.60600 1.000 20.04000 ? 248 TYR B N   1 
ATOM   4525 C  CA  . TYR B 1 254 ? 35.60700  1.17500   36.41100 1.000 21.16000 ? 248 TYR B CA  1 
ATOM   4526 C  C   . TYR B 1 254 ? 36.86500  2.01400   36.15300 1.000 20.08000 ? 248 TYR B C   1 
ATOM   4527 O  O   . TYR B 1 254 ? 37.94600  1.44700   35.92400 1.000 21.95000 ? 248 TYR B O   1 
ATOM   4528 C  CB  . TYR B 1 254 ? 34.68700  1.20700   35.18500 1.000 22.11000 ? 248 TYR B CB  1 
ATOM   4529 C  CG  . TYR B 1 254 ? 35.35600  0.68300   33.92100 1.000 20.90000 ? 248 TYR B CG  1 
ATOM   4530 C  CD1 . TYR B 1 254 ? 35.46300  -0.68600  33.70000 1.000 21.16000 ? 248 TYR B CD1 1 
ATOM   4531 C  CD2 . TYR B 1 254 ? 35.91000  1.55800   32.96200 1.000 19.68000 ? 248 TYR B CD2 1 
ATOM   4532 C  CE1 . TYR B 1 254 ? 36.06600  -1.19200  32.57400 1.000 19.67000 ? 248 TYR B CE1 1 
ATOM   4533 C  CE2 . TYR B 1 254 ? 36.54000  1.05200   31.80900 1.000 19.19000 ? 248 TYR B CE2 1 
ATOM   4534 C  CZ  . TYR B 1 254 ? 36.60400  -0.33800  31.63000 1.000 18.02000 ? 248 TYR B CZ  1 
ATOM   4535 O  OH  . TYR B 1 254 ? 37.20400  -0.91900  30.52500 1.000 19.60000 ? 248 TYR B OH  1 
ATOM   4536 N  N   . CYS B 1 255 ? 36.75300  3.36500   36.17500 1.000 18.66000 ? 249 CYS B N   1 
ATOM   4537 C  CA  . CYS B 1 255 ? 37.92400  4.19600   35.88900 1.000 19.73000 ? 249 CYS B CA  1 
ATOM   4538 C  C   . CYS B 1 255 ? 39.07000  3.90200   36.84400 1.000 18.49000 ? 249 CYS B C   1 
ATOM   4539 O  O   . CYS B 1 255 ? 40.23800  3.85300   36.43300 1.000 19.00000 ? 249 CYS B O   1 
ATOM   4540 C  CB  . CYS B 1 255 ? 37.58200  5.69000   35.97800 1.000 16.96000 ? 249 CYS B CB  1 
ATOM   4541 S  SG  . CYS B 1 255 ? 36.06200  6.22000   35.19300 1.000 25.82000 ? 249 CYS B SG  1 
ATOM   4542 N  N   . THR B 1 256 ? 38.76000  3.75400   38.13700 1.000 21.08000 ? 250 THR B N   1 
ATOM   4543 C  CA  . THR B 1 256 ? 39.78100  3.46100   39.14000 1.000 19.80000 ? 250 THR B CA  1 
ATOM   4544 C  C   . THR B 1 256 ? 40.41900  2.09400   38.89900 1.000 23.53000 ? 250 THR B C   1 
ATOM   4545 O  O   . THR B 1 256 ? 41.65000  1.94000   38.98600 1.000 24.99000 ? 250 THR B O   1 
ATOM   4546 C  CB  . THR B 1 256 ? 39.14700  3.53600   40.52800 1.000 19.80000 ? 250 THR B CB  1 
ATOM   4547 O  OG1 . THR B 1 256 ? 38.65200  4.87600   40.74200 1.000 21.19000 ? 250 THR B OG1 1 
ATOM   4548 C  CG2 . THR B 1 256 ? 40.12400  3.19100   41.59900 1.000 25.58000 ? 250 THR B CG2 1 
ATOM   4549 N  N   . MET B 1 257 ? 39.60500  1.09200   38.58800 1.000 26.35000 ? 251 MET B N   1 
ATOM   4550 C  CA  . MET B 1 257 ? 40.14500  -0.24900  38.40200 1.000 20.05000 ? 251 MET B CA  1 
ATOM   4551 C  C   . MET B 1 257 ? 40.91400  -0.35500  37.09600 1.000 23.96000 ? 251 MET B C   1 
ATOM   4552 O  O   . MET B 1 257 ? 41.95300  -1.02100  37.02900 1.000 24.53000 ? 251 MET B O   1 
ATOM   4553 C  CB  . MET B 1 257 ? 39.00200  -1.26100  38.46600 1.000 25.08000 ? 251 MET B CB  1 
ATOM   4554 C  CG  . MET B 1 257 ? 38.37700  -1.34200  39.88000 1.000 19.22000 ? 251 MET B CG  1 
ATOM   4555 S  SD  . MET B 1 257 ? 37.02900  -2.52700  39.99100 1.000 31.27000 ? 251 MET B SD  1 
ATOM   4556 C  CE  . MET B 1 257 ? 37.97800  -4.04300  39.73200 1.000 29.10000 ? 251 MET B CE  1 
ATOM   4557 N  N   . LEU B 1 258 ? 40.42300  0.29800   36.04400 1.000 22.47000 ? 252 LEU B N   1 
ATOM   4558 C  CA  . LEU B 1 258 ? 41.14400  0.33600   34.77800 1.000 19.98000 ? 252 LEU B CA  1 
ATOM   4559 C  C   . LEU B 1 258 ? 42.53400  0.97100   34.94000 1.000 23.80000 ? 252 LEU B C   1 
ATOM   4560 O  O   . LEU B 1 258 ? 43.54900  0.36800   34.56200 1.000 25.08000 ? 252 LEU B O   1 
ATOM   4561 C  CB  . LEU B 1 258 ? 40.29100  1.08900   33.75000 1.000 23.76000 ? 252 LEU B CB  1 
ATOM   4562 C  CG  . LEU B 1 258 ? 40.97500  1.46400   32.44100 1.000 22.47000 ? 252 LEU B CG  1 
ATOM   4563 C  CD1 . LEU B 1 258 ? 41.02900  0.20900   31.60800 1.000 20.60000 ? 252 LEU B CD1 1 
ATOM   4564 C  CD2 . LEU B 1 258 ? 40.23100  2.59300   31.74400 1.000 22.75000 ? 252 LEU B CD2 1 
ATOM   4565 N  N   . MET B 1 259 ? 42.61000  2.19400   35.50700 1.000 22.21000 ? 253 MET B N   1 
ATOM   4566 C  CA  . MET B 1 259 ? 43.91000  2.85100   35.67500 1.000 22.65000 ? 253 MET B CA  1 
ATOM   4567 C  C   . MET B 1 259 ? 44.80800  2.13500   36.67400 1.000 24.16000 ? 253 MET B C   1 
ATOM   4568 O  O   . MET B 1 259 ? 46.02800  2.12100   36.49200 1.000 28.95000 ? 253 MET B O   1 
ATOM   4569 C  CB  . MET B 1 259 ? 43.72600  4.30600   36.09100 1.000 17.46000 ? 253 MET B CB  1 
ATOM   4570 C  CG  . MET B 1 259 ? 43.09100  5.12500   34.96500 1.000 21.96000 ? 253 MET B CG  1 
ATOM   4571 S  SD  . MET B 1 259 ? 43.06800  6.90800   35.26600 1.000 22.35000 ? 253 MET B SD  1 
ATOM   4572 C  CE  . MET B 1 259 ? 41.56000  7.06100   36.23100 1.000 17.76000 ? 253 MET B CE  1 
ATOM   4573 N  N   . ARG B 1 260 ? 44.26000  1.52600   37.73000 1.000 26.08000 ? 254 ARG B N   1 
ATOM   4574 C  CA  . ARG B 1 260 ? 45.15400  0.75100   38.59400 1.000 29.18000 ? 254 ARG B CA  1 
ATOM   4575 C  C   . ARG B 1 260 ? 45.73500  -0.43200  37.83600 1.000 30.30000 ? 254 ARG B C   1 
ATOM   4576 O  O   . ARG B 1 260 ? 46.94200  -0.70300  37.92800 1.000 32.56000 ? 254 ARG B O   1 
ATOM   4577 C  CB  . ARG B 1 260 ? 44.45000  0.27800   39.86800 1.000 27.33000 ? 254 ARG B CB  1 
ATOM   4578 C  CG  . ARG B 1 260 ? 44.25700  1.39800   40.87500 1.000 34.87000 ? 254 ARG B CG  1 
ATOM   4579 C  CD  . ARG B 1 260 ? 44.53000  0.97100   42.31500 1.000 42.66000 ? 254 ARG B CD  1 
ATOM   4580 N  NE  . ARG B 1 260 ? 43.29900  0.86300   43.10200 1.000 52.46000 ? 254 ARG B NE  1 
ATOM   4581 C  CZ  . ARG B 1 260 ? 42.88400  1.75000   44.00500 1.000 49.75000 ? 254 ARG B CZ  1 
ATOM   4582 N  NH1 . ARG B 1 260 ? 43.56400  2.87300   44.24500 1.000 42.77000 ? 254 ARG B NH1 1 
ATOM   4583 N  NH2 . ARG B 1 260 ? 41.76000  1.50500   44.68500 1.000 44.45000 ? 254 ARG B NH2 1 
ATOM   4584 N  N   . ALA B 1 261 ? 44.91100  -1.09500  37.01800 1.000 29.14000 ? 255 ALA B N   1 
ATOM   4585 C  CA  . ALA B 1 261 ? 45.36800  -2.28000  36.29900 1.000 28.12000 ? 255 ALA B CA  1 
ATOM   4586 C  C   . ALA B 1 261 ? 46.52800  -1.95300  35.37100 1.000 31.47000 ? 255 ALA B C   1 
ATOM   4587 O  O   . ALA B 1 261 ? 47.47700  -2.74000  35.25100 1.000 31.54000 ? 255 ALA B O   1 
ATOM   4588 C  CB  . ALA B 1 261 ? 44.21200  -2.89000  35.51200 1.000 28.27000 ? 255 ALA B CB  1 
ATOM   4589 N  N   . PHE B 1 262 ? 46.48200  -0.79700  34.71100 1.000 28.26000 ? 256 PHE B N   1 
ATOM   4590 C  CA  . PHE B 1 262 ? 47.49900  -0.45100  33.71600 1.000 29.77000 ? 256 PHE B CA  1 
ATOM   4591 C  C   . PHE B 1 262 ? 48.67100  0.31500   34.30200 1.000 30.09000 ? 256 PHE B C   1 
ATOM   4592 O  O   . PHE B 1 262 ? 49.68900  0.50100   33.61100 1.000 29.30000 ? 256 PHE B O   1 
ATOM   4593 C  CB  . PHE B 1 262 ? 46.87500  0.36800   32.57100 1.000 30.04000 ? 256 PHE B CB  1 
ATOM   4594 C  CG  . PHE B 1 262 ? 46.12900  -0.46300  31.57200 1.000 27.15000 ? 256 PHE B CG  1 
ATOM   4595 C  CD1 . PHE B 1 262 ? 44.78500  -0.76000  31.76800 1.000 22.15000 ? 256 PHE B CD1 1 
ATOM   4596 C  CD2 . PHE B 1 262 ? 46.76600  -0.95700  30.44100 1.000 26.80000 ? 256 PHE B CD2 1 
ATOM   4597 C  CE1 . PHE B 1 262 ? 44.08600  -1.52500  30.83300 1.000 26.82000 ? 256 PHE B CE1 1 
ATOM   4598 C  CE2 . PHE B 1 262 ? 46.06300  -1.74100  29.52000 1.000 26.24000 ? 256 PHE B CE2 1 
ATOM   4599 C  CZ  . PHE B 1 262 ? 44.74100  -2.01400  29.71800 1.000 28.00000 ? 256 PHE B CZ  1 
ATOM   4600 N  N   . ASP B 1 263 ? 48.54800  0.77800   35.53900 1.000 30.06000 ? 257 ASP B N   1 
ATOM   4601 C  CA  . ASP B 1 263 ? 49.70500  1.20300   36.32700 1.000 32.06000 ? 257 ASP B CA  1 
ATOM   4602 C  C   . ASP B 1 263 ? 50.57200  2.21900   35.57400 1.000 30.89000 ? 257 ASP B C   1 
ATOM   4603 O  O   . ASP B 1 263 ? 51.77700  2.04100   35.38600 1.000 33.36000 ? 257 ASP B O   1 
ATOM   4604 C  CB  . ASP B 1 263 ? 50.51900  -0.02100  36.74900 1.000 34.14000 ? 257 ASP B CB  1 
ATOM   4605 C  CG  . ASP B 1 263 ? 51.56800  0.31000   37.78000 1.000 39.28000 ? 257 ASP B CG  1 
ATOM   4606 O  OD1 . ASP B 1 263 ? 51.34900  1.24900   38.58600 1.000 41.36000 ? 257 ASP B OD1 1 
ATOM   4607 O  OD2 . ASP B 1 263 ? 52.63200  -0.34100  37.74600 1.000 40.54000 ? 257 ASP B OD2 1 
ATOM   4608 N  N   . GLY B 1 264 ? 49.94200  3.29300   35.11800 1.000 30.91000 ? 258 GLY B N   1 
ATOM   4609 C  CA  . GLY B 1 264 ? 50.64000  4.35800   34.45000 1.000 28.57000 ? 258 GLY B CA  1 
ATOM   4610 C  C   . GLY B 1 264 ? 50.55800  4.33100   32.93800 1.000 29.27000 ? 258 GLY B C   1 
ATOM   4611 O  O   . GLY B 1 264 ? 50.87400  5.34100   32.30300 1.000 31.33000 ? 258 GLY B O   1 
ATOM   4612 N  N   . ALA B 1 265 ? 50.17500  3.20500   32.34200 1.000 24.12000 ? 259 ALA B N   1 
ATOM   4613 C  CA  . ALA B 1 265 ? 50.20900  3.08800   30.88900 1.000 24.25000 ? 259 ALA B CA  1 
ATOM   4614 C  C   . ALA B 1 265 ? 49.10600  3.87700   30.17800 1.000 28.25000 ? 259 ALA B C   1 
ATOM   4615 O  O   . ALA B 1 265 ? 49.23900  4.14600   28.97200 1.000 24.32000 ? 259 ALA B O   1 
ATOM   4616 C  CB  . ALA B 1 265 ? 50.10000  1.62700   30.48800 1.000 24.00000 ? 259 ALA B CB  1 
ATOM   4617 N  N   . LEU B 1 266 ? 48.03200  4.25400   30.87600 1.000 21.81000 ? 260 LEU B N   1 
ATOM   4618 C  CA  . LEU B 1 266 ? 46.93000  4.97600   30.25000 1.000 19.53000 ? 260 LEU B CA  1 
ATOM   4619 C  C   . LEU B 1 266 ? 46.11800  5.65300   31.33500 1.000 19.92000 ? 260 LEU B C   1 
ATOM   4620 O  O   . LEU B 1 266 ? 46.23500  5.31500   32.51300 1.000 22.11000 ? 260 LEU B O   1 
ATOM   4621 C  CB  . LEU B 1 266 ? 46.03600  4.04400   29.42100 1.000 19.55000 ? 260 LEU B CB  1 
ATOM   4622 C  CG  . LEU B 1 266 ? 45.37200  2.78700   30.03000 1.000 23.82000 ? 260 LEU B CG  1 
ATOM   4623 C  CD1 . LEU B 1 266 ? 44.18700  3.06600   31.00600 1.000 19.54000 ? 260 LEU B CD1 1 
ATOM   4624 C  CD2 . LEU B 1 266 ? 44.91800  1.84900   28.92600 1.000 22.31000 ? 260 LEU B CD2 1 
ATOM   4625 N  N   . VAL B 1 267 ? 45.26500  6.59100   30.92400 1.000 16.63000 ? 261 VAL B N   1 
ATOM   4626 C  CA  . VAL B 1 267 ? 44.21400  7.11700   31.79000 1.000 15.34000 ? 261 VAL B CA  1 
ATOM   4627 C  C   . VAL B 1 267 ? 42.87700  6.92000   31.09300 1.000 19.71000 ? 261 VAL B C   1 
ATOM   4628 O  O   . VAL B 1 267 ? 42.79400  6.89600   29.85500 1.000 20.05000 ? 261 VAL B O   1 
ATOM   4629 C  CB  . VAL B 1 267 ? 44.40300  8.61700   32.16700 1.000 20.04000 ? 261 VAL B CB  1 
ATOM   4630 C  CG1 . VAL B 1 267 ? 45.66200  8.82100   33.01100 1.000 19.88000 ? 261 VAL B CG1 1 
ATOM   4631 C  CG2 . VAL B 1 267 ? 44.44400  9.46800   30.94300 1.000 18.57000 ? 261 VAL B CG2 1 
ATOM   4632 N  N   . GLY B 1 268 ? 41.82900  6.76300   31.90000 1.000 18.19000 ? 262 GLY B N   1 
ATOM   4633 C  CA  . GLY B 1 268 ? 40.48300  6.60800   31.38100 1.000 15.70000 ? 262 GLY B CA  1 
ATOM   4634 C  C   . GLY B 1 268 ? 39.52700  7.43000   32.21200 1.000 17.91000 ? 262 GLY B C   1 
ATOM   4635 O  O   . GLY B 1 268 ? 39.77000  7.69200   33.38600 1.000 23.16000 ? 262 GLY B O   1 
ATOM   4636 N  N   . LYS B 1 269 ? 38.41900  7.82100   31.59900 1.000 16.04000 ? 263 LYS B N   1 
ATOM   4637 C  CA  . LYS B 1 269 ? 37.47000  8.70200   32.27400 1.000 16.20000 ? 263 LYS B CA  1 
ATOM   4638 C  C   . LYS B 1 269 ? 36.08000  8.47600   31.68800 1.000 17.44000 ? 263 LYS B C   1 
ATOM   4639 O  O   . LYS B 1 269 ? 35.91500  8.42000   30.46300 1.000 18.15000 ? 263 LYS B O   1 
ATOM   4640 C  CB  . LYS B 1 269 ? 37.88900  10.18300  32.12200 1.000 19.79000 ? 263 LYS B CB  1 
ATOM   4641 C  CG  . LYS B 1 269 ? 36.91600  11.15100  32.77400 1.000 17.01000 ? 263 LYS B CG  1 
ATOM   4642 C  CD  . LYS B 1 269 ? 36.96200  10.99800  34.31100 1.000 22.04000 ? 263 LYS B CD  1 
ATOM   4643 C  CE  . LYS B 1 269 ? 35.85300  11.81700  35.00400 1.000 18.59000 ? 263 LYS B CE  1 
ATOM   4644 N  NZ  . LYS B 1 269 ? 34.58900  11.05800  35.10200 1.000 20.27000 ? 263 LYS B NZ  1 
ATOM   4645 N  N   . LEU B 1 270 ? 35.10900  8.31900   32.57900 1.000 16.11000 ? 264 LEU B N   1 
ATOM   4646 C  CA  . LEU B 1 270 ? 33.69200  8.20500   32.25600 1.000 16.44000 ? 264 LEU B CA  1 
ATOM   4647 C  C   . LEU B 1 270 ? 33.02400  9.55700   31.97600 1.000 15.41000 ? 264 LEU B C   1 
ATOM   4648 O  O   . LEU B 1 270 ? 33.28800  10.54700  32.65600 1.000 18.82000 ? 264 LEU B O   1 
ATOM   4649 C  CB  . LEU B 1 270 ? 32.98400  7.55100   33.44100 1.000 20.66000 ? 264 LEU B CB  1 
ATOM   4650 C  CG  . LEU B 1 270 ? 31.47200  7.50800   33.42400 1.000 21.26000 ? 264 LEU B CG  1 
ATOM   4651 C  CD1 . LEU B 1 270 ? 31.01800  6.49300   32.37000 1.000 18.75000 ? 264 LEU B CD1 1 
ATOM   4652 C  CD2 . LEU B 1 270 ? 30.97700  7.11400   34.80900 1.000 21.40000 ? 264 LEU B CD2 1 
ATOM   4653 N  N   . GLY B 1 271 ? 32.10100  9.58600   31.01400 1.000 18.08000 ? 265 GLY B N   1 
ATOM   4654 C  CA  . GLY B 1 271 ? 31.10400  10.64500  30.91600 1.000 14.34000 ? 265 GLY B CA  1 
ATOM   4655 C  C   . GLY B 1 271 ? 29.70700  10.09200  31.16400 1.000 18.28000 ? 265 GLY B C   1 
ATOM   4656 O  O   . GLY B 1 271 ? 29.37800  8.97800   30.72700 1.000 16.90000 ? 265 GLY B O   1 
ATOM   4657 N  N   . ALA B 1 272 ? 28.87400  10.86200  31.86100 1.000 15.27000 ? 266 ALA B N   1 
ATOM   4658 C  CA  . ALA B 1 272 ? 27.51900  10.39400  32.13300 1.000 18.91000 ? 266 ALA B CA  1 
ATOM   4659 C  C   . ALA B 1 272 ? 26.78700  10.13400  30.83100 1.000 19.37000 ? 266 ALA B C   1 
ATOM   4660 O  O   . ALA B 1 272 ? 27.11500  10.71400  29.78600 1.000 18.22000 ? 266 ALA B O   1 
ATOM   4661 C  CB  . ALA B 1 272 ? 26.74500  11.41000  32.98100 1.000 22.39000 ? 266 ALA B CB  1 
ATOM   4662 N  N   . ASP B 1 273 ? 25.79200  9.23100   30.89700 1.000 20.14000 ? 267 ASP B N   1 
ATOM   4663 C  CA  . ASP B 1 273 ? 25.06800  8.72100   29.71500 1.000 19.06000 ? 267 ASP B CA  1 
ATOM   4664 C  C   . ASP B 1 273 ? 25.97000  7.98400   28.72100 1.000 17.93000 ? 267 ASP B C   1 
ATOM   4665 O  O   . ASP B 1 273 ? 25.71400  7.97500   27.49600 1.000 16.36000 ? 267 ASP B O   1 
ATOM   4666 C  CB  . ASP B 1 273 ? 24.27200  9.82700   29.03100 1.000 19.20000 ? 267 ASP B CB  1 
ATOM   4667 C  CG  . ASP B 1 273 ? 23.04700  10.20700  29.85500 1.000 23.52000 ? 267 ASP B CG  1 
ATOM   4668 O  OD1 . ASP B 1 273 ? 22.20500  9.32700   30.13600 1.000 21.62000 ? 267 ASP B OD1 1 
ATOM   4669 O  OD2 . ASP B 1 273 ? 22.94400  11.36000  30.27300 1.000 25.93000 ? 267 ASP B OD2 1 
ATOM   4670 N  N   . ALA B 1 274 ? 27.00400  7.34000   29.26900 1.000 15.26000 ? 268 ALA B N   1 
ATOM   4671 C  CA  . ALA B 1 274 ? 27.72800  6.25100   28.61100 1.000 17.65000 ? 268 ALA B CA  1 
ATOM   4672 C  C   . ALA B 1 274 ? 28.63100  6.75500   27.48900 1.000 15.19000 ? 268 ALA B C   1 
ATOM   4673 O  O   . ALA B 1 274 ? 28.57100  6.27100   26.36100 1.000 16.64000 ? 268 ALA B O   1 
ATOM   4674 C  CB  . ALA B 1 274 ? 26.78200  5.15700   28.09800 1.000 15.38000 ? 268 ALA B CB  1 
ATOM   4675 N  N   . SER B 1 275 ? 29.48000  7.72000   27.80700 1.000 15.61000 ? 269 SER B N   1 
ATOM   4676 C  CA  A SER B 1 275 ? 30.66300  7.98400   27.00900 0.600 13.70000 ? 269 SER B CA  1 
ATOM   4677 C  CA  B SER B 1 275 ? 30.66100  7.96900   26.99900 0.400 13.34000 ? 269 SER B CA  1 
ATOM   4678 C  C   . SER B 1 275 ? 31.89900  7.57600   27.79700 1.000 14.88000 ? 269 SER B C   1 
ATOM   4679 O  O   . SER B 1 275 ? 31.87300  7.49300   29.03000 1.000 14.79000 ? 269 SER B O   1 
ATOM   4680 C  CB  A SER B 1 275 ? 30.74300  9.45300   26.59700 0.600 14.59000 ? 269 SER B CB  1 
ATOM   4681 C  CB  B SER B 1 275 ? 30.73800  9.43000   26.52900 0.400 14.55000 ? 269 SER B CB  1 
ATOM   4682 O  OG  A SER B 1 275 ? 29.67800  9.76600   25.72500 0.600 14.24000 ? 269 SER B OG  1 
ATOM   4683 O  OG  B SER B 1 275 ? 31.08500  10.32800  27.56800 0.400 14.21000 ? 269 SER B OG  1 
ATOM   4684 N  N   . TYR B 1 276 ? 32.97900  7.28700   27.07300 1.000 12.86000 ? 270 TYR B N   1 
ATOM   4685 C  CA  . TYR B 1 276 ? 34.23800  6.88500   27.69100 1.000 16.04000 ? 270 TYR B CA  1 
ATOM   4686 C  C   . TYR B 1 276 ? 35.40700  7.40300   26.85400 1.000 15.91000 ? 270 TYR B C   1 
ATOM   4687 O  O   . TYR B 1 276 ? 35.33200  7.45500   25.62300 1.000 16.65000 ? 270 TYR B O   1 
ATOM   4688 C  CB  . TYR B 1 276 ? 34.38600  5.34700   27.89400 1.000 14.27000 ? 270 TYR B CB  1 
ATOM   4689 C  CG  . TYR B 1 276 ? 35.20500  5.10800   29.12900 1.000 14.78000 ? 270 TYR B CG  1 
ATOM   4690 C  CD1 . TYR B 1 276 ? 34.60400  5.17900   30.38900 1.000 16.15000 ? 270 TYR B CD1 1 
ATOM   4691 C  CD2 . TYR B 1 276 ? 36.58800  4.93600   29.05900 1.000 15.10000 ? 270 TYR B CD2 1 
ATOM   4692 C  CE1 . TYR B 1 276 ? 35.34900  5.03100   31.53800 1.000 16.27000 ? 270 TYR B CE1 1 
ATOM   4693 C  CE2 . TYR B 1 276 ? 37.34500  4.77400   30.21100 1.000 15.27000 ? 270 TYR B CE2 1 
ATOM   4694 C  CZ  . TYR B 1 276 ? 36.71500  4.84400   31.45400 1.000 20.76000 ? 270 TYR B CZ  1 
ATOM   4695 O  OH  . TYR B 1 276 ? 37.45900  4.73000   32.63200 1.000 20.31000 ? 270 TYR B OH  1 
ATOM   4696 N  N   . ALA B 1 277 ? 36.50300  7.77400   27.53200 1.000 14.69000 ? 271 ALA B N   1 
ATOM   4697 C  CA  . ALA B 1 277 ? 37.70300  8.22800   26.83500 1.000 12.70000 ? 271 ALA B CA  1 
ATOM   4698 C  C   . ALA B 1 277 ? 38.94500  7.66000   27.49400 1.000 15.30000 ? 271 ALA B C   1 
ATOM   4699 O  O   . ALA B 1 277 ? 38.99100  7.53300   28.73100 1.000 15.50000 ? 271 ALA B O   1 
ATOM   4700 C  CB  . ALA B 1 277 ? 37.77300  9.76300   26.79600 1.000 15.22000 ? 271 ALA B CB  1 
ATOM   4701 N  N   . ILE B 1 278 ? 39.93100  7.29300   26.65400 1.000 15.96000 ? 272 ILE B N   1 
ATOM   4702 C  CA  . ILE B 1 278 ? 41.19300  6.66300   27.07400 1.000 13.13000 ? 272 ILE B CA  1 
ATOM   4703 C  C   . ILE B 1 278 ? 42.34600  7.28100   26.30300 1.000 17.18000 ? 272 ILE B C   1 
ATOM   4704 O  O   . ILE B 1 278 ? 42.28700  7.41700   25.07400 1.000 15.65000 ? 272 ILE B O   1 
ATOM   4705 C  CB  . ILE B 1 278 ? 41.17500  5.12000   26.89500 1.000 15.50000 ? 272 ILE B CB  1 
ATOM   4706 C  CG1 . ILE B 1 278 ? 40.13700  4.50600   27.81900 1.000 16.37000 ? 272 ILE B CG1 1 
ATOM   4707 C  CG2 . ILE B 1 278 ? 42.53500  4.50700   27.24800 1.000 15.39000 ? 272 ILE B CG2 1 
ATOM   4708 C  CD1 . ILE B 1 278 ? 39.96800  3.00500   27.65200 1.000 19.74000 ? 272 ILE B CD1 1 
ATOM   4709 N  N   . GLY B 1 279 ? 43.38000  7.71200   27.03600 1.000 17.14000 ? 273 GLY B N   1 
ATOM   4710 C  CA  . GLY B 1 279 ? 44.61100  8.19000   26.43000 1.000 15.74000 ? 273 GLY B CA  1 
ATOM   4711 C  C   . GLY B 1 279 ? 45.69100  7.17800   26.75300 1.000 19.71000 ? 273 GLY B C   1 
ATOM   4712 O  O   . GLY B 1 279 ? 45.90100  6.86000   27.92900 1.000 18.66000 ? 273 GLY B O   1 
ATOM   4713 N  N   . VAL B 1 280 ? 46.35200  6.65000   25.71900 1.000 21.20000 ? 274 VAL B N   1 
ATOM   4714 C  CA  . VAL B 1 280 ? 47.24600  5.50100   25.81000 1.000 20.17000 ? 274 VAL B CA  1 
ATOM   4715 C  C   . VAL B 1 280 ? 48.65500  5.97500   25.46800 1.000 20.02000 ? 274 VAL B C   1 
ATOM   4716 O  O   . VAL B 1 280 ? 48.89600  6.48900   24.36100 1.000 19.49000 ? 274 VAL B O   1 
ATOM   4717 C  CB  . VAL B 1 280 ? 46.81000  4.37600   24.85100 1.000 16.05000 ? 274 VAL B CB  1 
ATOM   4718 C  CG1 . VAL B 1 280 ? 47.84100  3.24300   24.86200 1.000 20.69000 ? 274 VAL B CG1 1 
ATOM   4719 C  CG2 . VAL B 1 280 ? 45.37300  3.91700   25.14900 1.000 18.22000 ? 274 VAL B CG2 1 
ATOM   4720 N  N   . ARG B 1 281 ? 49.57900  5.84400   26.41500 1.000 20.43000 ? 275 ARG B N   1 
ATOM   4721 C  CA  . ARG B 1 281 ? 50.95500  6.22100   26.11800 1.000 18.98000 ? 275 ARG B CA  1 
ATOM   4722 C  C   . ARG B 1 281 ? 51.53400  5.27000   25.07900 1.000 21.12000 ? 275 ARG B C   1 
ATOM   4723 O  O   . ARG B 1 281 ? 51.12300  4.10700   24.96800 1.000 22.27000 ? 275 ARG B O   1 
ATOM   4724 C  CB  . ARG B 1 281 ? 51.81900  6.18800   27.38400 1.000 23.47000 ? 275 ARG B CB  1 
ATOM   4725 C  CG  . ARG B 1 281 ? 51.46000  7.31000   28.38800 1.000 26.46000 ? 275 ARG B CG  1 
ATOM   4726 C  CD  . ARG B 1 281 ? 52.42600  7.30200   29.57100 1.000 26.82000 ? 275 ARG B CD  1 
ATOM   4727 N  NE  . ARG B 1 281 ? 53.79800  7.55400   29.14100 1.000 29.39000 ? 275 ARG B NE  1 
ATOM   4728 C  CZ  . ARG B 1 281 ? 54.85500  7.47100   29.93600 1.000 34.03000 ? 275 ARG B CZ  1 
ATOM   4729 N  NH1 . ARG B 1 281 ? 54.73200  7.17500   31.22200 1.000 33.62000 ? 275 ARG B NH1 1 
ATOM   4730 N  NH2 . ARG B 1 281 ? 56.07300  7.69000   29.42700 1.000 32.02000 ? 275 ARG B NH2 1 
ATOM   4731 N  N   . ALA B 1 282 ? 52.51100  5.76400   24.32800 1.000 22.82000 ? 276 ALA B N   1 
ATOM   4732 C  CA  . ALA B 1 282 ? 53.12700  4.94000   23.30000 1.000 24.93000 ? 276 ALA B CA  1 
ATOM   4733 C  C   . ALA B 1 282 ? 53.75100  3.66700   23.88500 1.000 24.06000 ? 276 ALA B C   1 
ATOM   4734 O  O   . ALA B 1 282 ? 54.40200  3.68400   24.93800 1.000 29.70000 ? 276 ALA B O   1 
ATOM   4735 C  CB  . ALA B 1 282 ? 54.17600  5.75500   22.54700 1.000 22.35000 ? 276 ALA B CB  1 
ATOM   4736 N  N   . SER B 1 283 ? 53.59500  2.56500   23.16200 1.000 24.80000 ? 277 SER B N   1 
ATOM   4737 C  CA  . SER B 1 283 ? 53.92800  1.23900   23.66000 1.000 28.44000 ? 277 SER B CA  1 
ATOM   4738 C  C   . SER B 1 283 ? 54.06500  0.28400   22.47500 1.000 29.81000 ? 277 SER B C   1 
ATOM   4739 O  O   . SER B 1 283 ? 53.75600  0.63900   21.33000 1.000 27.11000 ? 277 SER B O   1 
ATOM   4740 C  CB  . SER B 1 283 ? 52.83300  0.75700   24.60800 1.000 23.73000 ? 277 SER B CB  1 
ATOM   4741 O  OG  . SER B 1 283 ? 51.65900  0.50200   23.85700 1.000 23.20000 ? 277 SER B OG  1 
ATOM   4742 N  N   . ASP B 1 284 ? 54.52100  -0.94800  22.75800 1.000 29.22000 ? 278 ASP B N   1 
ATOM   4743 C  CA  . ASP B 1 284 ? 54.51800  -1.95800  21.70800 1.000 27.67000 ? 278 ASP B CA  1 
ATOM   4744 C  C   . ASP B 1 284 ? 53.12200  -2.10300  21.12900 1.000 28.81000 ? 278 ASP B C   1 
ATOM   4745 O  O   . ASP B 1 284 ? 52.96200  -2.24700  19.91300 1.000 29.04000 ? 278 ASP B O   1 
ATOM   4746 C  CB  . ASP B 1 284 ? 55.00400  -3.31200  22.22800 1.000 28.67000 ? 278 ASP B CB  1 
ATOM   4747 C  CG  . ASP B 1 284 ? 56.45200  -3.30700  22.62300 1.000 41.32000 ? 278 ASP B CG  1 
ATOM   4748 O  OD1 . ASP B 1 284 ? 57.24800  -2.42300  22.17500 1.000 41.95000 ? 278 ASP B OD1 1 
ATOM   4749 O  OD2 . ASP B 1 284 ? 56.80600  -4.22400  23.39900 1.000 49.72000 ? 278 ASP B OD2 1 
ATOM   4750 N  N   . ALA B 1 285 ? 52.09100  -2.03500  21.98700 1.000 23.94000 ? 279 ALA B N   1 
ATOM   4751 C  CA  . ALA B 1 285 ? 50.71000  -2.17100  21.51600 1.000 25.21000 ? 279 ALA B CA  1 
ATOM   4752 C  C   . ALA B 1 285 ? 50.32200  -1.05500  20.53400 1.000 26.78000 ? 279 ALA B C   1 
ATOM   4753 O  O   . ALA B 1 285 ? 49.74800  -1.33500  19.47300 1.000 24.60000 ? 279 ALA B O   1 
ATOM   4754 C  CB  . ALA B 1 285 ? 49.75300  -2.21500  22.71300 1.000 25.88000 ? 279 ALA B CB  1 
ATOM   4755 N  N   . THR B 1 286 ? 50.62300  0.22100   20.85900 1.000 24.93000 ? 280 THR B N   1 
ATOM   4756 C  CA  . THR B 1 286 ? 50.28400  1.29800   19.92500 1.000 23.98000 ? 280 THR B CA  1 
ATOM   4757 C  C   . THR B 1 286 ? 51.06400  1.15900   18.62000 1.000 23.76000 ? 280 THR B C   1 
ATOM   4758 O  O   . THR B 1 286 ? 50.54100  1.45500   17.53900 1.000 23.58000 ? 280 THR B O   1 
ATOM   4759 C  CB  . THR B 1 286 ? 50.55100  2.67700   20.54400 1.000 26.75000 ? 280 THR B CB  1 
ATOM   4760 O  OG1 . THR B 1 286 ? 51.92800  2.80200   20.92400 1.000 26.51000 ? 280 THR B OG1 1 
ATOM   4761 C  CG2 . THR B 1 286 ? 49.64800  2.94300   21.75800 1.000 23.16000 ? 280 THR B CG2 1 
ATOM   4762 N  N   . ARG B 1 287 ? 52.32500  0.72200   18.69800 1.000 25.62000 ? 281 ARG B N   1 
ATOM   4763 C  CA  A ARG B 1 287 ? 53.13000  0.58000   17.48300 0.700 26.46000 ? 281 ARG B CA  1 
ATOM   4764 C  CA  B ARG B 1 287 ? 53.13100  0.57700   17.48700 0.300 26.52000 ? 281 ARG B CA  1 
ATOM   4765 C  C   . ARG B 1 287 ? 52.58000  -0.51700  16.57600 1.000 29.84000 ? 281 ARG B C   1 
ATOM   4766 O  O   . ARG B 1 287 ? 52.53800  -0.34900  15.35100 1.000 32.93000 ? 281 ARG B O   1 
ATOM   4767 C  CB  A ARG B 1 287 ? 54.60200  0.29500   17.82900 0.700 26.83000 ? 281 ARG B CB  1 
ATOM   4768 C  CB  B ARG B 1 287 ? 54.58800  0.28900   17.86200 0.300 26.89000 ? 281 ARG B CB  1 
ATOM   4769 C  CG  A ARG B 1 287 ? 55.34100  1.47000   18.46200 0.700 24.87000 ? 281 ARG B CG  1 
ATOM   4770 C  CG  B ARG B 1 287 ? 55.60000  1.06000   17.04100 0.300 29.05000 ? 281 ARG B CG  1 
ATOM   4771 C  CD  A ARG B 1 287 ? 56.82000  1.15300   18.76000 0.700 26.85000 ? 281 ARG B CD  1 
ATOM   4772 C  CD  B ARG B 1 287 ? 56.98200  1.08000   17.70100 0.300 27.72000 ? 281 ARG B CD  1 
ATOM   4773 N  NE  A ARG B 1 287 ? 57.02100  0.45700   20.03300 0.700 27.99000 ? 281 ARG B NE  1 
ATOM   4774 N  NE  B ARG B 1 287 ? 56.94600  1.69100   19.02500 0.300 26.88000 ? 281 ARG B NE  1 
ATOM   4775 C  CZ  A ARG B 1 287 ? 57.06100  1.06200   21.21800 0.700 27.77000 ? 281 ARG B CZ  1 
ATOM   4776 C  CZ  B ARG B 1 287 ? 57.14100  1.03700   20.16500 0.300 27.83000 ? 281 ARG B CZ  1 
ATOM   4777 N  NH1 A ARG B 1 287 ? 56.90700  2.37300   21.33000 0.700 25.88000 ? 281 ARG B NH1 1 
ATOM   4778 N  NH1 B ARG B 1 287 ? 57.44200  -0.25600  20.18300 0.300 27.60000 ? 281 ARG B NH1 1 
ATOM   4779 N  NH2 A ARG B 1 287 ? 57.26900  0.33200   22.31800 0.700 28.17000 ? 281 ARG B NH2 1 
ATOM   4780 N  NH2 B ARG B 1 287 ? 57.03900  1.69800   21.31600 0.300 27.16000 ? 281 ARG B NH2 1 
ATOM   4781 N  N   . GLN B 1 288 ? 52.17100  -1.65900  17.15500 1.000 25.79000 ? 282 GLN B N   1 
ATOM   4782 C  CA  . GLN B 1 288 ? 51.53600  -2.71000  16.36200 1.000 31.26000 ? 282 GLN B CA  1 
ATOM   4783 C  C   . GLN B 1 288 ? 50.26100  -2.20900  15.71000 1.000 27.96000 ? 282 GLN B C   1 
ATOM   4784 O  O   . GLN B 1 288 ? 49.88600  -2.71600  14.65300 1.000 28.03000 ? 282 GLN B O   1 
ATOM   4785 C  CB  . GLN B 1 288 ? 51.19900  -3.93500  17.22000 1.000 28.82000 ? 282 GLN B CB  1 
ATOM   4786 C  CG  . GLN B 1 288 ? 52.29000  -4.97900  17.34000 1.000 43.35000 ? 282 GLN B CG  1 
ATOM   4787 C  CD  . GLN B 1 288 ? 52.04100  -5.90400  18.51800 1.000 46.79000 ? 282 GLN B CD  1 
ATOM   4788 O  OE1 . GLN B 1 288 ? 52.88600  -6.04400  19.40800 1.000 48.86000 ? 282 GLN B OE1 1 
ATOM   4789 N  NE2 . GLN B 1 288 ? 50.86200  -6.53100  18.53700 1.000 52.00000 ? 282 GLN B NE2 1 
ATOM   4790 N  N   . LEU B 1 289 ? 49.57300  -1.23300  16.32500 1.000 25.63000 ? 283 LEU B N   1 
ATOM   4791 C  CA  . LEU B 1 289 ? 48.36100  -0.65900  15.76300 1.000 29.78000 ? 283 LEU B CA  1 
ATOM   4792 C  C   . LEU B 1 289 ? 48.64900  0.33000   14.64500 1.000 33.83000 ? 283 LEU B C   1 
ATOM   4793 O  O   . LEU B 1 289 ? 47.69800  0.85700   14.06000 1.000 33.62000 ? 283 LEU B O   1 
ATOM   4794 C  CB  . LEU B 1 289 ? 47.52200  0.04400   16.85000 1.000 25.06000 ? 283 LEU B CB  1 
ATOM   4795 C  CG  . LEU B 1 289 ? 46.87200  -0.86500  17.89500 1.000 21.64000 ? 283 LEU B CG  1 
ATOM   4796 C  CD1 . LEU B 1 289 ? 46.35000  -0.03100  19.08700 1.000 21.80000 ? 283 LEU B CD1 1 
ATOM   4797 C  CD2 . LEU B 1 289 ? 45.75700  -1.69200  17.25200 1.000 22.57000 ? 283 LEU B CD2 1 
ATOM   4798 N  N   . GLY B 1 290 ? 49.91300  0.62400   14.37200 1.000 28.79000 ? 284 GLY B N   1 
ATOM   4799 C  CA  . GLY B 1 290 ? 50.28400  1.42000   13.22300 1.000 31.95000 ? 284 GLY B CA  1 
ATOM   4800 C  C   . GLY B 1 290 ? 50.54300  2.89700   13.45800 1.000 36.36000 ? 284 GLY B C   1 
ATOM   4801 O  O   . GLY B 1 290 ? 50.41200  3.67700   12.51000 1.000 39.64000 ? 284 GLY B O   1 
ATOM   4802 N  N   . THR B 1 291 ? 50.89900  3.31400   14.67600 1.000 34.09000 ? 285 THR B N   1 
ATOM   4803 C  CA  . THR B 1 291 ? 51.27600  4.69600   14.92500 1.000 30.50000 ? 285 THR B CA  1 
ATOM   4804 C  C   . THR B 1 291 ? 52.53300  4.74100   15.78600 1.000 30.04000 ? 285 THR B C   1 
ATOM   4805 O  O   . THR B 1 291 ? 52.78800  3.85100   16.60000 1.000 27.96000 ? 285 THR B O   1 
ATOM   4806 C  CB  . THR B 1 291 ? 50.12400  5.50000   15.57700 1.000 31.90000 ? 285 THR B CB  1 
ATOM   4807 O  OG1 . THR B 1 291 ? 50.49200  6.87800   15.67100 1.000 33.60000 ? 285 THR B OG1 1 
ATOM   4808 C  CG2 . THR B 1 291 ? 49.77600  4.98300   16.96300 1.000 30.06000 ? 285 THR B CG2 1 
ATOM   4809 N  N   . ASP B 1 292 ? 53.33300  5.78200   15.57000 1.000 32.44000 ? 286 ASP B N   1 
ATOM   4810 C  CA  . ASP B 1 292 ? 54.60300  5.95800   16.26100 1.000 31.00000 ? 286 ASP B CA  1 
ATOM   4811 C  C   . ASP B 1 292 ? 54.47200  6.78600   17.54400 1.000 30.86000 ? 286 ASP B C   1 
ATOM   4812 O  O   . ASP B 1 292 ? 55.47200  7.00000   18.22800 1.000 30.68000 ? 286 ASP B O   1 
ATOM   4813 C  CB  . ASP B 1 292 ? 55.63000  6.60100   15.30400 1.000 35.29000 ? 286 ASP B CB  1 
ATOM   4814 C  CG  . ASP B 1 292 ? 55.06000  7.82200   14.54300 1.000 43.76000 ? 286 ASP B CG  1 
ATOM   4815 O  OD1 . ASP B 1 292 ? 53.87400  8.18900   14.74900 1.000 48.94000 ? 286 ASP B OD1 1 
ATOM   4816 O  OD2 . ASP B 1 292 ? 55.80200  8.42600   13.73100 1.000 52.10000 ? 286 ASP B OD2 1 
ATOM   4817 N  N   . GLY B 1 293 ? 53.27300  7.25000   17.89800 1.000 26.94000 ? 287 GLY B N   1 
ATOM   4818 C  CA  . GLY B 1 293 ? 53.09700  8.05300   19.08500 1.000 27.80000 ? 287 GLY B CA  1 
ATOM   4819 C  C   . GLY B 1 293 ? 52.01600  7.48400   19.98800 1.000 31.83000 ? 287 GLY B C   1 
ATOM   4820 O  O   . GLY B 1 293 ? 51.72000  6.27900   19.97200 1.000 27.37000 ? 287 GLY B O   1 
ATOM   4821 N  N   . ALA B 1 294 ? 51.40700  8.38000   20.77500 1.000 25.65000 ? 288 ALA B N   1 
ATOM   4822 C  CA  . ALA B 1 294 ? 50.35200  7.99000   21.69600 1.000 23.49000 ? 288 ALA B CA  1 
ATOM   4823 C  C   . ALA B 1 294 ? 49.04000  7.78200   20.93900 1.000 22.59000 ? 288 ALA B C   1 
ATOM   4824 O  O   . ALA B 1 294 ? 48.91500  8.07100   19.74700 1.000 21.64000 ? 288 ALA B O   1 
ATOM   4825 C  CB  . ALA B 1 294 ? 50.17900  9.03800   22.80300 1.000 22.18000 ? 288 ALA B CB  1 
ATOM   4826 N  N   . LEU B 1 295 ? 48.03200  7.31500   21.66000 1.000 19.88000 ? 289 LEU B N   1 
ATOM   4827 C  CA  . LEU B 1 295 ? 46.76600  6.93500   21.05100 1.000 18.17000 ? 289 LEU B CA  1 
ATOM   4828 C  C   . LEU B 1 295 ? 45.63700  7.42500   21.92800 1.000 19.04000 ? 289 LEU B C   1 
ATOM   4829 O  O   . LEU B 1 295 ? 45.77900  7.46800   23.15100 1.000 22.75000 ? 289 LEU B O   1 
ATOM   4830 C  CB  . LEU B 1 295 ? 46.74400  5.40900   20.91600 1.000 22.67000 ? 289 LEU B CB  1 
ATOM   4831 C  CG  . LEU B 1 295 ? 45.73700  4.59500   20.18300 1.000 25.36000 ? 289 LEU B CG  1 
ATOM   4832 C  CD1 . LEU B 1 295 ? 46.52700  3.63300   19.35000 1.000 29.19000 ? 289 LEU B CD1 1 
ATOM   4833 C  CD2 . LEU B 1 295 ? 45.00100  3.84000   21.26400 1.000 26.47000 ? 289 LEU B CD2 1 
ATOM   4834 N  N   . GLY B 1 296 ? 44.51000  7.76800   21.31000 1.000 18.14000 ? 290 GLY B N   1 
ATOM   4835 C  CA  . GLY B 1 296 ? 43.27900  8.07500   22.03600 1.000 15.48000 ? 290 GLY B CA  1 
ATOM   4836 C  C   . GLY B 1 296 ? 42.12000  7.21400   21.58000 1.000 15.81000 ? 290 GLY B C   1 
ATOM   4837 O  O   . GLY B 1 296 ? 42.01800  6.86800   20.39700 1.000 18.18000 ? 290 GLY B O   1 
ATOM   4838 N  N   . ILE B 1 297 ? 41.27200  6.82600   22.53000 1.000 15.32000 ? 291 ILE B N   1 
ATOM   4839 C  CA  . ILE B 1 297 ? 40.07800  6.02800   22.25600 1.000 14.82000 ? 291 ILE B CA  1 
ATOM   4840 C  C   . ILE B 1 297 ? 38.86800  6.73800   22.85800 1.000 15.52000 ? 291 ILE B C   1 
ATOM   4841 O  O   . ILE B 1 297 ? 38.92800  7.20800   24.00000 1.000 15.51000 ? 291 ILE B O   1 
ATOM   4842 C  CB  . ILE B 1 297 ? 40.21600  4.60500   22.84900 1.000 15.60000 ? 291 ILE B CB  1 
ATOM   4843 C  CG1 . ILE B 1 297 ? 41.52200  3.93500   22.41100 1.000 15.94000 ? 291 ILE B CG1 1 
ATOM   4844 C  CG2 . ILE B 1 297 ? 38.96000  3.73500   22.53200 1.000 14.86000 ? 291 ILE B CG2 1 
ATOM   4845 C  CD1 . ILE B 1 297 ? 41.77300  2.71900   23.22600 1.000 19.73000 ? 291 ILE B CD1 1 
ATOM   4846 N  N   . SER B 1 298 ? 37.76500  6.82400   22.10600 1.000 15.10000 ? 292 SER B N   1 
ATOM   4847 C  CA  . SER B 1 298 ? 36.52700  7.36200   22.66400 1.000 12.76000 ? 292 SER B CA  1 
ATOM   4848 C  C   . SER B 1 298 ? 35.35500  6.51400   22.21900 1.000 14.98000 ? 292 SER B C   1 
ATOM   4849 O  O   . SER B 1 298 ? 35.37300  5.92000   21.13500 1.000 14.43000 ? 292 SER B O   1 
ATOM   4850 C  CB  . SER B 1 298 ? 36.31100  8.82200   22.27800 1.000 14.31000 ? 292 SER B CB  1 
ATOM   4851 O  OG  . SER B 1 298 ? 36.39800  8.92300   20.89400 1.000 15.42000 ? 292 SER B OG  1 
ATOM   4852 N  N   . VAL B 1 299 ? 34.36900  6.38400   23.10800 1.000 12.67000 ? 293 VAL B N   1 
ATOM   4853 C  CA  . VAL B 1 299 ? 33.27800  5.42500   22.95500 1.000 14.65000 ? 293 VAL B CA  1 
ATOM   4854 C  C   . VAL B 1 299 ? 31.98800  6.10400   23.38400 1.000 12.96000 ? 293 VAL B C   1 
ATOM   4855 O  O   . VAL B 1 299 ? 31.98000  6.87600   24.34400 1.000 13.01000 ? 293 VAL B O   1 
ATOM   4856 C  CB  . VAL B 1 299 ? 33.51700  4.12800   23.77900 1.000 11.69000 ? 293 VAL B CB  1 
ATOM   4857 C  CG1 . VAL B 1 299 ? 32.33800  3.15600   23.56700 1.000 14.16000 ? 293 VAL B CG1 1 
ATOM   4858 C  CG2 . VAL B 1 299 ? 34.86000  3.45700   23.37700 1.000 14.75000 ? 293 VAL B CG2 1 
ATOM   4859 N  N   . LYS B 1 300 ? 30.88100  5.81400   22.68600 1.000 15.07000 ? 294 LYS B N   1 
ATOM   4860 C  CA  . LYS B 1 300 ? 29.54900  6.22600   23.14200 1.000 14.79000 ? 294 LYS B CA  1 
ATOM   4861 C  C   . LYS B 1 300 ? 28.57500  5.08300   22.87300 1.000 13.82000 ? 294 LYS B C   1 
ATOM   4862 O  O   . LYS B 1 300 ? 28.56300  4.52700   21.77000 1.000 12.49000 ? 294 LYS B O   1 
ATOM   4863 C  CB  . LYS B 1 300 ? 29.11100  7.53400   22.45000 1.000 13.00000 ? 294 LYS B CB  1 
ATOM   4864 C  CG  . LYS B 1 300 ? 27.57200  7.81600   22.51900 1.000 13.38000 ? 294 LYS B CG  1 
ATOM   4865 C  CD  . LYS B 1 300 ? 27.10100  8.34000   23.87200 1.000 14.22000 ? 294 LYS B CD  1 
ATOM   4866 C  CE  . LYS B 1 300 ? 25.60900  8.74200   23.76200 1.000 13.37000 ? 294 LYS B CE  1 
ATOM   4867 N  NZ  . LYS B 1 300 ? 25.02600  9.23800   25.07800 1.000 17.65000 ? 294 LYS B NZ  1 
ATOM   4868 N  N   . ILE B 1 301 ? 27.77900  4.69400   23.88400 1.000 12.81000 ? 295 ILE B N   1 
ATOM   4869 C  CA  . ILE B 1 301 ? 26.66100  3.77900   23.68400 1.000 12.65000 ? 295 ILE B CA  1 
ATOM   4870 C  C   . ILE B 1 301 ? 25.45200  4.66300   23.37500 1.000 13.38000 ? 295 ILE B C   1 
ATOM   4871 O  O   . ILE B 1 301 ? 25.11800  5.54000   24.17100 1.000 13.18000 ? 295 ILE B O   1 
ATOM   4872 C  CB  . ILE B 1 301 ? 26.42300  2.90500   24.92700 1.000 11.68000 ? 295 ILE B CB  1 
ATOM   4873 C  CG1 . ILE B 1 301 ? 27.72400  2.17100   25.32300 1.000 14.62000 ? 295 ILE B CG1 1 
ATOM   4874 C  CG2 . ILE B 1 301 ? 25.16900  1.99100   24.77100 1.000 11.85000 ? 295 ILE B CG2 1 
ATOM   4875 C  CD1 . ILE B 1 301 ? 28.31500  1.29200   24.23500 1.000 15.63000 ? 295 ILE B CD1 1 
ATOM   4876 N  N   . GLU B 1 302 ? 24.82500  4.45800   22.21100 1.000 13.79000 ? 296 GLU B N   1 
ATOM   4877 C  CA  . GLU B 1 302 ? 23.80000  5.37600   21.71300 1.000 16.26000 ? 296 GLU B CA  1 
ATOM   4878 C  C   . GLU B 1 302 ? 22.70000  5.63000   22.73400 1.000 15.63000 ? 296 GLU B C   1 
ATOM   4879 O  O   . GLU B 1 302 ? 22.26200  6.77300   22.91000 1.000 14.32000 ? 296 GLU B O   1 
ATOM   4880 C  CB  . GLU B 1 302 ? 23.18700  4.83100   20.41500 1.000 16.71000 ? 296 GLU B CB  1 
ATOM   4881 C  CG  . GLU B 1 302 ? 22.16800  5.77400   19.76700 1.000 18.75000 ? 296 GLU B CG  1 
ATOM   4882 C  CD  . GLU B 1 302 ? 22.75800  7.14000   19.42500 1.000 24.34000 ? 296 GLU B CD  1 
ATOM   4883 O  OE1 . GLU B 1 302 ? 23.93400  7.21700   18.98600 1.000 19.76000 ? 296 GLU B OE1 1 
ATOM   4884 O  OE2 . GLU B 1 302 ? 22.05100  8.16000   19.59700 1.000 20.89000 ? 296 GLU B OE2 1 
ATOM   4885 N  N   . ASP B 1 303 ? 22.24500  4.58600   23.41200 1.000 13.08000 ? 297 ASP B N   1 
ATOM   4886 C  CA  . ASP B 1 303 ? 21.07800  4.64700   24.30100 1.000 14.48000 ? 297 ASP B CA  1 
ATOM   4887 C  C   . ASP B 1 303 ? 21.44500  4.98900   25.74000 1.000 15.25000 ? 297 ASP B C   1 
ATOM   4888 O  O   . ASP B 1 303 ? 20.54700  5.03200   26.59500 1.000 15.13000 ? 297 ASP B O   1 
ATOM   4889 C  CB  . ASP B 1 303 ? 20.36200  3.30900   24.29900 1.000 17.16000 ? 297 ASP B CB  1 
ATOM   4890 C  CG  . ASP B 1 303 ? 21.33000  2.17300   24.58300 1.000 16.83000 ? 297 ASP B CG  1 
ATOM   4891 O  OD1 . ASP B 1 303 ? 21.99000  1.70300   23.62500 1.000 16.54000 ? 297 ASP B OD1 1 
ATOM   4892 O  OD2 . ASP B 1 303 ? 21.47400  1.79800   25.77900 1.000 14.77000 ? 297 ASP B OD2 1 
ATOM   4893 N  N   . GLY B 1 304 ? 22.73200  5.12100   26.04300 1.000 14.55000 ? 298 GLY B N   1 
ATOM   4894 C  CA  . GLY B 1 304 ? 23.19400  5.61300   27.33800 1.000 18.97000 ? 298 GLY B CA  1 
ATOM   4895 C  C   . GLY B 1 304 ? 23.45300  4.57600   28.41800 1.000 18.88000 ? 298 GLY B C   1 
ATOM   4896 O  O   . GLY B 1 304 ? 23.61300  4.96300   29.58400 1.000 18.20000 ? 298 GLY B O   1 
ATOM   4897 N  N   . ASN B 1 305 ? 23.52200  3.28000   28.07600 1.000 15.51000 ? 299 ASN B N   1 
ATOM   4898 C  CA  . ASN B 1 305 ? 23.64100  2.21000   29.07400 1.000 18.02000 ? 299 ASN B CA  1 
ATOM   4899 C  C   . ASN B 1 305 ? 25.09000  2.02900   29.54900 1.000 17.35000 ? 299 ASN B C   1 
ATOM   4900 O  O   . ASN B 1 305 ? 25.96700  1.66100   28.76500 1.000 15.49000 ? 299 ASN B O   1 
ATOM   4901 C  CB  . ASN B 1 305 ? 23.10700  0.89500   28.49700 1.000 17.33000 ? 299 ASN B CB  1 
ATOM   4902 C  CG  . ASN B 1 305 ? 22.98300  -0.18800  29.55000 1.000 19.73000 ? 299 ASN B CG  1 
ATOM   4903 O  OD1 . ASN B 1 305 ? 23.96700  -0.72700  29.96900 1.000 16.66000 ? 299 ASN B OD1 1 
ATOM   4904 N  ND2 . ASN B 1 305 ? 21.75600  -0.50800  29.97600 1.000 20.88000 ? 299 ASN B ND2 1 
ATOM   4905 N  N   . LEU B 1 306 ? 25.32800  2.24900   30.85300 1.000 16.41000 ? 300 LEU B N   1 
ATOM   4906 C  CA  . LEU B 1 306 ? 26.68000  2.22500   31.40600 1.000 18.30000 ? 300 LEU B CA  1 
ATOM   4907 C  C   . LEU B 1 306 ? 27.24800  0.80900   31.49500 1.000 17.11000 ? 300 LEU B C   1 
ATOM   4908 O  O   . LEU B 1 306 ? 28.43900  0.61100   31.24900 1.000 16.94000 ? 300 LEU B O   1 
ATOM   4909 C  CB  . LEU B 1 306 ? 26.68600  2.85200   32.80800 1.000 19.19000 ? 300 LEU B CB  1 
ATOM   4910 C  CG  . LEU B 1 306 ? 26.53600  4.36100   32.92900 1.000 34.80000 ? 300 LEU B CG  1 
ATOM   4911 C  CD1 . LEU B 1 306 ? 26.64000  4.79800   34.41000 1.000 36.03000 ? 300 LEU B CD1 1 
ATOM   4912 C  CD2 . LEU B 1 306 ? 27.62100  5.02300   32.09800 1.000 26.98000 ? 300 LEU B CD2 1 
ATOM   4913 N  N   . GLU B 1 307 ? 26.44600  -0.17200  31.94100 1.000 17.52000 ? 301 GLU B N   1 
ATOM   4914 C  CA  . GLU B 1 307 ? 26.93900  -1.54600  31.99000 1.000 16.48000 ? 301 GLU B CA  1 
ATOM   4915 C  C   . GLU B 1 307 ? 27.45700  -1.98900  30.61600 1.000 17.36000 ? 301 GLU B C   1 
ATOM   4916 O  O   . GLU B 1 307 ? 28.53500  -2.58800  30.50300 1.000 18.61000 ? 301 GLU B O   1 
ATOM   4917 C  CB  . GLU B 1 307 ? 25.82600  -2.47900  32.46900 1.000 18.40000 ? 301 GLU B CB  1 
ATOM   4918 C  CG  . GLU B 1 307 ? 26.26900  -3.93400  32.75400 1.000 22.77000 ? 301 GLU B CG  1 
ATOM   4919 C  CD  . GLU B 1 307 ? 25.08000  -4.87100  32.97400 1.000 24.96000 ? 301 GLU B CD  1 
ATOM   4920 O  OE1 . GLU B 1 307 ? 24.05400  -4.71000  32.24700 1.000 27.29000 ? 301 GLU B OE1 1 
ATOM   4921 O  OE2 . GLU B 1 307 ? 25.15900  -5.77300  33.84800 1.000 24.74000 ? 301 GLU B OE2 1 
ATOM   4922 N  N   . MET B 1 308 ? 26.70000  -1.69100  29.56100 1.000 13.65000 ? 302 MET B N   1 
ATOM   4923 C  CA  . MET B 1 308 ? 27.16100  -1.99700  28.21200 1.000 14.41000 ? 302 MET B CA  1 
ATOM   4924 C  C   . MET B 1 308 ? 28.39700  -1.19900  27.82200 1.000 15.12000 ? 302 MET B C   1 
ATOM   4925 O  O   . MET B 1 308 ? 29.21200  -1.69600  27.04800 1.000 13.32000 ? 302 MET B O   1 
ATOM   4926 C  CB  . MET B 1 308 ? 26.02400  -1.75200  27.21700 1.000 13.55000 ? 302 MET B CB  1 
ATOM   4927 C  CG  . MET B 1 308 ? 24.82900  -2.69300  27.41700 1.000 16.03000 ? 302 MET B CG  1 
ATOM   4928 S  SD  . MET B 1 308 ? 25.24700  -4.45900  27.24300 1.000 19.28000 ? 302 MET B SD  1 
ATOM   4929 C  CE  . MET B 1 308 ? 25.55100  -4.97600  28.95400 1.000 16.83000 ? 302 MET B CE  1 
ATOM   4930 N  N   . LEU B 1 309 ? 28.52400  0.04800   28.28800 1.000 13.68000 ? 303 LEU B N   1 
ATOM   4931 C  CA  . LEU B 1 309 ? 29.71300  0.83400   27.99500 1.000 14.96000 ? 303 LEU B CA  1 
ATOM   4932 C  C   . LEU B 1 309 ? 30.97000  0.14600   28.51600 1.000 13.92000 ? 303 LEU B C   1 
ATOM   4933 O  O   . LEU B 1 309 ? 31.97600  0.03300   27.80800 1.000 14.41000 ? 303 LEU B O   1 
ATOM   4934 C  CB  . LEU B 1 309 ? 29.57300  2.23100   28.61300 1.000 14.82000 ? 303 LEU B CB  1 
ATOM   4935 C  CG  . LEU B 1 309 ? 30.83200  3.09600   28.47200 1.000 15.33000 ? 303 LEU B CG  1 
ATOM   4936 C  CD1 . LEU B 1 309 ? 30.99600  3.54300   26.99100 1.000 10.62000 ? 303 LEU B CD1 1 
ATOM   4937 C  CD2 . LEU B 1 309 ? 30.75900  4.29600   29.43900 1.000 13.12000 ? 303 LEU B CD2 1 
ATOM   4938 N  N   . TYR B 1 310 ? 30.95600  -0.25700  29.79200 1.000 15.96000 ? 304 TYR B N   1 
ATOM   4939 C  CA  . TYR B 1 310 ? 32.15200  -0.85500  30.38300 1.000 15.69000 ? 304 TYR B CA  1 
ATOM   4940 C  C   . TYR B 1 310 ? 32.49100  -2.18600  29.71700 1.000 16.17000 ? 304 TYR B C   1 
ATOM   4941 O  O   . TYR B 1 310 ? 33.67400  -2.48900  29.52400 1.000 19.06000 ? 304 TYR B O   1 
ATOM   4942 C  CB  . TYR B 1 310 ? 31.95900  -1.07000  31.88400 1.000 16.01000 ? 304 TYR B CB  1 
ATOM   4943 C  CG  . TYR B 1 310 ? 31.73700  0.18300   32.67800 1.000 19.26000 ? 304 TYR B CG  1 
ATOM   4944 C  CD1 . TYR B 1 310 ? 32.42900  1.35200   32.36300 1.000 20.73000 ? 304 TYR B CD1 1 
ATOM   4945 C  CD2 . TYR B 1 310 ? 30.87700  0.19500   33.78800 1.000 19.10000 ? 304 TYR B CD2 1 
ATOM   4946 C  CE1 . TYR B 1 310 ? 32.26500  2.52000   33.10700 1.000 19.34000 ? 304 TYR B CE1 1 
ATOM   4947 C  CE2 . TYR B 1 310 ? 30.70500  1.38000   34.54500 1.000 20.66000 ? 304 TYR B CE2 1 
ATOM   4948 C  CZ  . TYR B 1 310 ? 31.40500  2.52300   34.18800 1.000 22.09000 ? 304 TYR B CZ  1 
ATOM   4949 O  OH  . TYR B 1 310 ? 31.28100  3.69900   34.89400 1.000 27.32000 ? 304 TYR B OH  1 
ATOM   4950 N  N   . ALA B 1 311 ? 31.46800  -2.98300  29.36400 1.000 14.40000 ? 305 ALA B N   1 
ATOM   4951 C  CA  . ALA B 1 311 ? 31.69000  -4.22300  28.61300 1.000 14.37000 ? 305 ALA B CA  1 
ATOM   4952 C  C   . ALA B 1 311 ? 32.38900  -3.93500  27.28400 1.000 17.82000 ? 305 ALA B C   1 
ATOM   4953 O  O   . ALA B 1 311 ? 33.40600  -4.57000  26.94900 1.000 16.53000 ? 305 ALA B O   1 
ATOM   4954 C  CB  . ALA B 1 311 ? 30.35600  -4.97400  28.39500 1.000 14.33000 ? 305 ALA B CB  1 
ATOM   4955 N  N   . VAL B 1 312 ? 31.85500  -2.96900  26.52800 1.000 13.38000 ? 306 VAL B N   1 
ATOM   4956 C  CA  . VAL B 1 312 ? 32.35900  -2.61300  25.19800 1.000 13.84000 ? 306 VAL B CA  1 
ATOM   4957 C  C   . VAL B 1 312 ? 33.76500  -2.03900  25.27600 1.000 15.97000 ? 306 VAL B C   1 
ATOM   4958 O  O   . VAL B 1 312 ? 34.63200  -2.40700  24.47900 1.000 13.65000 ? 306 VAL B O   1 
ATOM   4959 C  CB  . VAL B 1 312 ? 31.40200  -1.61600  24.51600 1.000 15.48000 ? 306 VAL B CB  1 
ATOM   4960 C  CG1 . VAL B 1 312 ? 32.07300  -0.95900  23.28500 1.000 14.96000 ? 306 VAL B CG1 1 
ATOM   4961 C  CG2 . VAL B 1 312 ? 30.11900  -2.32200  24.14600 1.000 16.25000 ? 306 VAL B CG2 1 
ATOM   4962 N  N   . VAL B 1 313 ? 34.01600  -1.11500  26.22200 1.000 15.31000 ? 307 VAL B N   1 
ATOM   4963 C  CA  . VAL B 1 313 ? 35.35700  -0.54400  26.35000 1.000 15.01000 ? 307 VAL B CA  1 
ATOM   4964 C  C   . VAL B 1 313 ? 36.36400  -1.64800  26.63200 1.000 16.89000 ? 307 VAL B C   1 
ATOM   4965 O  O   . VAL B 1 313 ? 37.45700  -1.66600  26.06200 1.000 18.51000 ? 307 VAL B O   1 
ATOM   4966 C  CB  . VAL B 1 313 ? 35.41600  0.54100   27.44500 1.000 14.71000 ? 307 VAL B CB  1 
ATOM   4967 C  CG1 . VAL B 1 313 ? 36.88300  0.99800   27.66800 1.000 13.00000 ? 307 VAL B CG1 1 
ATOM   4968 C  CG2 . VAL B 1 313 ? 34.57800  1.77200   27.06200 1.000 14.53000 ? 307 VAL B CG2 1 
ATOM   4969 N  N   . THR B 1 314 ? 36.01200  -2.58900  27.51800 1.000 15.01000 ? 308 THR B N   1 
ATOM   4970 C  CA  . THR B 1 314 ? 36.94600  -3.66400  27.86200 1.000 19.87000 ? 308 THR B CA  1 
ATOM   4971 C  C   . THR B 1 314 ? 37.17600  -4.59800  26.67200 1.000 18.80000 ? 308 THR B C   1 
ATOM   4972 O  O   . THR B 1 314 ? 38.31100  -5.01700  26.41300 1.000 17.51000 ? 308 THR B O   1 
ATOM   4973 C  CB  . THR B 1 314 ? 36.44400  -4.46500  29.08400 1.000 17.32000 ? 308 THR B CB  1 
ATOM   4974 O  OG1 . THR B 1 314 ? 36.14500  -3.56900  30.16500 1.000 18.10000 ? 308 THR B OG1 1 
ATOM   4975 C  CG2 . THR B 1 314 ? 37.53100  -5.39300  29.58100 1.000 18.78000 ? 308 THR B CG2 1 
ATOM   4976 N  N   . GLU B 1 315 ? 36.11900  -4.90600  25.92400 1.000 16.40000 ? 309 GLU B N   1 
ATOM   4977 C  CA  . GLU B 1 315 ? 36.27300  -5.71700  24.72500 1.000 17.32000 ? 309 GLU B CA  1 
ATOM   4978 C  C   . GLU B 1 315 ? 37.11600  -4.98600  23.69400 1.000 18.00000 ? 309 GLU B C   1 
ATOM   4979 O  O   . GLU B 1 315 ? 37.89700  -5.60900  22.96600 1.000 18.87000 ? 309 GLU B O   1 
ATOM   4980 C  CB  . GLU B 1 315 ? 34.88100  -6.05400  24.18000 1.000 17.07000 ? 309 GLU B CB  1 
ATOM   4981 C  CG  . GLU B 1 315 ? 34.82800  -6.71000  22.79300 1.000 16.53000 ? 309 GLU B CG  1 
ATOM   4982 C  CD  . GLU B 1 315 ? 35.26500  -8.14700  22.80800 1.000 19.84000 ? 309 GLU B CD  1 
ATOM   4983 O  OE1 . GLU B 1 315 ? 35.48000  -8.68800  23.93100 1.000 20.55000 ? 309 GLU B OE1 1 
ATOM   4984 O  OE2 . GLU B 1 315 ? 35.41600  -8.76300  21.71500 1.000 20.21000 ? 309 GLU B OE2 1 
ATOM   4985 N  N   . LEU B 1 316 ? 36.97900  -3.66300  23.63700 1.000 18.17000 ? 310 LEU B N   1 
ATOM   4986 C  CA  . LEU B 1 316 ? 37.74300  -2.87300  22.67900 1.000 18.22000 ? 310 LEU B CA  1 
ATOM   4987 C  C   . LEU B 1 316 ? 39.22600  -2.89300  23.01500 1.000 16.00000 ? 310 LEU B C   1 
ATOM   4988 O  O   . LEU B 1 316 ? 40.06200  -3.04900  22.12300 1.000 17.69000 ? 310 LEU B O   1 
ATOM   4989 C  CB  . LEU B 1 316 ? 37.16500  -1.44800  22.61400 1.000 18.05000 ? 310 LEU B CB  1 
ATOM   4990 C  CG  . LEU B 1 316 ? 37.70400  -0.48500  21.55300 1.000 22.97000 ? 310 LEU B CG  1 
ATOM   4991 C  CD1 . LEU B 1 316 ? 37.69100  -1.11900  20.15500 1.000 19.79000 ? 310 LEU B CD1 1 
ATOM   4992 C  CD2 . LEU B 1 316 ? 36.82600  0.77300   21.53600 1.000 24.00000 ? 310 LEU B CD2 1 
ATOM   4993 N  N   . LEU B 1 317 ? 39.57700  -2.77900  24.29700 1.000 17.84000 ? 311 LEU B N   1 
ATOM   4994 C  CA  . LEU B 1 317 ? 40.98200  -2.87300  24.68100 1.000 21.95000 ? 311 LEU B CA  1 
ATOM   4995 C  C   . LEU B 1 317 ? 41.55500  -4.23600  24.31500 1.000 20.40000 ? 311 LEU B C   1 
ATOM   4996 O  O   . LEU B 1 317 ? 42.69500  -4.34100  23.85000 1.000 20.48000 ? 311 LEU B O   1 
ATOM   4997 C  CB  . LEU B 1 317 ? 41.12600  -2.61700  26.18100 1.000 21.14000 ? 311 LEU B CB  1 
ATOM   4998 C  CG  . LEU B 1 317 ? 40.86000  -1.18200  26.62800 1.000 20.96000 ? 311 LEU B CG  1 
ATOM   4999 C  CD1 . LEU B 1 317 ? 40.85300  -1.09400  28.14600 1.000 23.64000 ? 311 LEU B CD1 1 
ATOM   5000 C  CD2 . LEU B 1 317 ? 41.94200  -0.28300  26.08100 1.000 23.48000 ? 311 LEU B CD2 1 
ATOM   5001 N  N   . GLU B 1 318 ? 40.77500  -5.29500  24.51600 1.000 16.98000 ? 312 GLU B N   1 
ATOM   5002 C  CA  . GLU B 1 318 ? 41.22100  -6.61300  24.08200 1.000 20.58000 ? 312 GLU B CA  1 
ATOM   5003 C  C   . GLU B 1 318 ? 41.41900  -6.66400  22.56600 1.000 19.76000 ? 312 GLU B C   1 
ATOM   5004 O  O   . GLU B 1 318 ? 42.41500  -7.21900  22.09200 1.000 19.84000 ? 312 GLU B O   1 
ATOM   5005 C  CB  . GLU B 1 318 ? 40.23100  -7.69400  24.52800 1.000 20.36000 ? 312 GLU B CB  1 
ATOM   5006 C  CG  . GLU B 1 318 ? 40.67100  -9.13700  24.13100 1.000 24.38000 ? 312 GLU B CG  1 
ATOM   5007 C  CD  . GLU B 1 318 ? 39.75800  -10.20800 24.69200 1.000 34.02000 ? 312 GLU B CD  1 
ATOM   5008 O  OE1 . GLU B 1 318 ? 38.72800  -10.55200 24.05600 1.000 32.13000 ? 312 GLU B OE1 1 
ATOM   5009 O  OE2 . GLU B 1 318 ? 40.07100  -10.72200 25.78900 1.000 38.57000 ? 312 GLU B OE2 1 
ATOM   5010 N  N   . ARG B 1 319 ? 40.46800  -6.11600  21.78100 1.000 18.27000 ? 313 ARG B N   1 
ATOM   5011 C  CA  . ARG B 1 319 ? 40.63900  -6.21900  20.32800 1.000 19.57000 ? 313 ARG B CA  1 
ATOM   5012 C  C   . ARG B 1 319 ? 41.82400  -5.40200  19.82200 1.000 23.36000 ? 313 ARG B C   1 
ATOM   5013 O  O   . ARG B 1 319 ? 42.45200  -5.78900  18.83200 1.000 22.17000 ? 313 ARG B O   1 
ATOM   5014 C  CB  . ARG B 1 319 ? 39.37800  -5.80700  19.59700 1.000 22.97000 ? 313 ARG B CB  1 
ATOM   5015 C  CG  . ARG B 1 319 ? 38.28500  -6.87000  19.73900 1.000 23.76000 ? 313 ARG B CG  1 
ATOM   5016 C  CD  . ARG B 1 319 ? 37.19900  -6.66200  18.77800 1.000 24.66000 ? 313 ARG B CD  1 
ATOM   5017 N  NE  . ARG B 1 319 ? 36.00500  -7.38100  19.19300 1.000 23.15000 ? 313 ARG B NE  1 
ATOM   5018 C  CZ  . ARG B 1 319 ? 34.91200  -7.44200  18.44500 1.000 24.25000 ? 313 ARG B CZ  1 
ATOM   5019 N  NH1 . ARG B 1 319 ? 34.88600  -6.91200  17.23000 1.000 21.70000 ? 313 ARG B NH1 1 
ATOM   5020 N  NH2 . ARG B 1 319 ? 33.82700  -8.06100  18.91700 1.000 22.14000 ? 313 ARG B NH2 1 
ATOM   5021 N  N   . LEU B 1 320 ? 42.15400  -4.29000  20.48400 1.000 19.23000 ? 314 LEU B N   1 
ATOM   5022 C  CA  . LEU B 1 320 ? 43.30900  -3.48500  20.09100 1.000 22.62000 ? 314 LEU B CA  1 
ATOM   5023 C  C   . LEU B 1 320 ? 44.61600  -4.01400  20.66900 1.000 20.71000 ? 314 LEU B C   1 
ATOM   5024 O  O   . LEU B 1 320 ? 45.68700  -3.47600  20.35200 1.000 23.24000 ? 314 LEU B O   1 
ATOM   5025 C  CB  . LEU B 1 320 ? 43.10400  -2.02500  20.50900 1.000 22.59000 ? 314 LEU B CB  1 
ATOM   5026 C  CG  . LEU B 1 320 ? 41.92200  -1.23800  19.91600 1.000 19.71000 ? 314 LEU B CG  1 
ATOM   5027 C  CD1 . LEU B 1 320 ? 41.61200  -0.00100  20.77600 1.000 15.80000 ? 314 LEU B CD1 1 
ATOM   5028 C  CD2 . LEU B 1 320 ? 42.11900  -0.85400  18.45600 1.000 19.72000 ? 314 LEU B CD2 1 
ATOM   5029 N  N   . GLY B 1 321 ? 44.55600  -5.05500  21.49400 1.000 20.87000 ? 315 GLY B N   1 
ATOM   5030 C  CA  . GLY B 1 321 ? 45.75700  -5.63000  22.07500 1.000 23.64000 ? 315 GLY B CA  1 
ATOM   5031 C  C   . GLY B 1 321 ? 46.40300  -4.77500  23.14600 1.000 29.87000 ? 315 GLY B C   1 
ATOM   5032 O  O   . GLY B 1 321 ? 47.61400  -4.85300  23.34700 1.000 24.01000 ? 315 GLY B O   1 
ATOM   5033 N  N   . ILE B 1 322 ? 45.62900  -3.96400  23.85500 1.000 25.48000 ? 316 ILE B N   1 
ATOM   5034 C  CA  . ILE B 1 322 ? 46.19100  -3.03600  24.81900 1.000 26.11000 ? 316 ILE B CA  1 
ATOM   5035 C  C   . ILE B 1 322 ? 46.13400  -3.68900  26.19200 1.000 34.20000 ? 316 ILE B C   1 
ATOM   5036 O  O   . ILE B 1 322 ? 45.06400  -4.08600  26.66200 1.000 30.34000 ? 316 ILE B O   1 
ATOM   5037 C  CB  . ILE B 1 322 ? 45.46600  -1.68400  24.77900 1.000 23.32000 ? 316 ILE B CB  1 
ATOM   5038 C  CG1 . ILE B 1 322 ? 45.67400  -1.08900  23.37600 1.000 25.92000 ? 316 ILE B CG1 1 
ATOM   5039 C  CG2 . ILE B 1 322 ? 45.99500  -0.76900  25.89800 1.000 21.34000 ? 316 ILE B CG2 1 
ATOM   5040 C  CD1 . ILE B 1 322 ? 44.86300  0.21800   23.04700 1.000 29.81000 ? 316 ILE B CD1 1 
ATOM   5041 N  N   . GLY B 1 323 ? 47.29300  -3.82000  26.82800 1.000 43.59000 ? 317 GLY B N   1 
ATOM   5042 C  CA  . GLY B 1 323 ? 47.38700  -4.56300  28.06100 1.000 45.85000 ? 317 GLY B CA  1 
ATOM   5043 C  C   . GLY B 1 323 ? 47.61500  -6.04100  27.81300 1.000 50.09000 ? 317 GLY B C   1 
ATOM   5044 O  O   . GLY B 1 323 ? 47.63900  -6.53200  26.68400 1.000 52.92000 ? 317 GLY B O   1 
ATOM   5045 N  N   . SER B 1 324 ? 47.79600  -6.74000  28.87800 1.000 51.31000 ? 318 SER B N   1 
ATOM   5046 C  CA  . SER B 1 324 ? 47.97500  -8.17400  28.85100 1.000 47.75000 ? 318 SER B CA  1 
ATOM   5047 C  C   . SER B 1 324 ? 46.67700  -8.85700  29.23000 1.000 49.07000 ? 318 SER B C   1 
ATOM   5048 O  O   . SER B 1 324 ? 45.78300  -8.22900  29.81000 1.000 45.31000 ? 318 SER B O   1 
ATOM   5049 C  CB  . SER B 1 324 ? 49.07500  -8.57600  29.83200 1.000 46.26000 ? 318 SER B CB  1 
ATOM   5050 O  OG  . SER B 1 324 ? 48.75900  -8.10400  31.12800 1.000 48.92000 ? 318 SER B OG  1 
ATOM   5051 N  N   . PRO B 1 325 ? 46.52400  -10.15000 28.90600 1.000 57.99000 ? 319 PRO B N   1 
ATOM   5052 C  CA  . PRO B 1 325 ? 45.35200  -10.88300 29.42000 1.000 57.85000 ? 319 PRO B CA  1 
ATOM   5053 C  C   . PRO B 1 325 ? 45.20900  -10.75700 30.92800 1.000 55.52000 ? 319 PRO B C   1 
ATOM   5054 O  O   . PRO B 1 325 ? 44.08200  -10.67800 31.43800 1.000 54.92000 ? 319 PRO B O   1 
ATOM   5055 C  CB  . PRO B 1 325 ? 45.62600  -12.33400 28.98500 1.000 59.25000 ? 319 PRO B CB  1 
ATOM   5056 C  CG  . PRO B 1 325 ? 46.48400  -12.19300 27.75000 1.000 57.54000 ? 319 PRO B CG  1 
ATOM   5057 C  CD  . PRO B 1 325 ? 47.34800  -10.97800 28.00000 1.000 56.02000 ? 319 PRO B CD  1 
ATOM   5058 N  N   . ASP B 1 326 ? 46.33700  -10.66400 31.64200 1.000 45.04000 ? 320 ASP B N   1 
ATOM   5059 C  CA  . ASP B 1 326 ? 46.36000  -10.61600 33.10000 1.000 44.15000 ? 320 ASP B CA  1 
ATOM   5060 C  C   . ASP B 1 326 ? 46.02600  -9.22700  33.63200 1.000 45.96000 ? 320 ASP B C   1 
ATOM   5061 O  O   . ASP B 1 326 ? 45.28200  -9.09900  34.61300 1.000 47.08000 ? 320 ASP B O   1 
ATOM   5062 C  CB  . ASP B 1 326 ? 47.73000  -11.08300 33.56900 1.000 48.91000 ? 320 ASP B CB  1 
ATOM   5063 C  CG  . ASP B 1 326 ? 48.30500  -12.16300 32.64400 1.000 62.17000 ? 320 ASP B CG  1 
ATOM   5064 O  OD1 . ASP B 1 326 ? 48.93800  -11.81200 31.60800 1.000 56.31000 ? 320 ASP B OD1 1 
ATOM   5065 O  OD2 . ASP B 1 326 ? 48.06800  -13.36500 32.92200 1.000 66.61000 ? 320 ASP B OD2 1 
ATOM   5066 N  N   . VAL B 1 327 ? 46.55600  -8.18100  32.99400 1.000 45.30000 ? 321 VAL B N   1 
ATOM   5067 C  CA  . VAL B 1 327 ? 46.11000  -6.81800  33.28400 1.000 43.80000 ? 321 VAL B CA  1 
ATOM   5068 C  C   . VAL B 1 327 ? 44.60100  -6.70900  33.07400 1.000 40.02000 ? 321 VAL B C   1 
ATOM   5069 O  O   . VAL B 1 327 ? 43.83800  -6.40100  33.99900 1.000 39.72000 ? 321 VAL B O   1 
ATOM   5070 C  CB  . VAL B 1 327 ? 46.88700  -5.80500  32.41800 1.000 41.50000 ? 321 VAL B CB  1 
ATOM   5071 C  CG1 . VAL B 1 327 ? 46.17300  -4.44100  32.39000 1.000 39.20000 ? 321 VAL B CG1 1 
ATOM   5072 C  CG2 . VAL B 1 327 ? 48.31600  -5.64000  32.92200 1.000 40.61000 ? 321 VAL B CG2 1 
ATOM   5073 N  N   . ARG B 1 328 ? 44.13900  -7.01800  31.86000 1.000 39.42000 ? 322 ARG B N   1 
ATOM   5074 C  CA  . ARG B 1 328 ? 42.72200  -6.84300  31.55500 1.000 39.91000 ? 322 ARG B CA  1 
ATOM   5075 C  C   . ARG B 1 328 ? 41.81400  -7.79500  32.33200 1.000 43.17000 ? 322 ARG B C   1 
ATOM   5076 O  O   . ARG B 1 328 ? 40.62300  -7.48700  32.49800 1.000 37.98000 ? 322 ARG B O   1 
ATOM   5077 C  CB  . ARG B 1 328 ? 42.48600  -6.98000  30.04700 1.000 36.39000 ? 322 ARG B CB  1 
ATOM   5078 C  CG  . ARG B 1 328 ? 43.21800  -5.90300  29.20700 1.000 35.59000 ? 322 ARG B CG  1 
ATOM   5079 C  CD  . ARG B 1 328 ? 42.82400  -5.97900  27.74800 1.000 31.05000 ? 322 ARG B CD  1 
ATOM   5080 N  NE  . ARG B 1 328 ? 43.06900  -7.31200  27.21200 1.000 37.49000 ? 322 ARG B NE  1 
ATOM   5081 C  CZ  . ARG B 1 328 ? 44.10300  -7.63700  26.44400 1.000 40.45000 ? 322 ARG B CZ  1 
ATOM   5082 N  NH1 . ARG B 1 328 ? 44.95800  -6.71900  26.00600 1.000 35.40000 ? 322 ARG B NH1 1 
ATOM   5083 N  NH2 . ARG B 1 328 ? 44.28600  -8.91500  26.10300 1.000 41.20000 ? 322 ARG B NH2 1 
ATOM   5084 N  N   . SER B 1 329 ? 42.32000  -8.93800  32.81300 1.000 39.10000 ? 323 SER B N   1 
ATOM   5085 C  CA  . SER B 1 329 ? 41.44500  -9.81500  33.58400 1.000 37.27000 ? 323 SER B CA  1 
ATOM   5086 C  C   . SER B 1 329 ? 40.98700  -9.17800  34.89800 1.000 36.12000 ? 323 SER B C   1 
ATOM   5087 O  O   . SER B 1 329 ? 40.01300  -9.64700  35.49800 1.000 36.89000 ? 323 SER B O   1 
ATOM   5088 C  CB  . SER B 1 329 ? 42.14500  -11.12900 33.87700 1.000 36.25000 ? 323 SER B CB  1 
ATOM   5089 O  OG  . SER B 1 329 ? 43.18200  -10.88500 34.79800 1.000 44.39000 ? 323 SER B OG  1 
ATOM   5090 N  N   . GLN B 1 330 ? 41.66500  -8.12300  35.36200 1.000 39.33000 ? 324 GLN B N   1 
ATOM   5091 C  CA  . GLN B 1 330 ? 41.18500  -7.38200  36.52100 1.000 32.36000 ? 324 GLN B CA  1 
ATOM   5092 C  C   . GLN B 1 330 ? 39.82800  -6.73800  36.24800 1.000 31.80000 ? 324 GLN B C   1 
ATOM   5093 O  O   . GLN B 1 330 ? 39.09300  -6.42800  37.19500 1.000 33.82000 ? 324 GLN B O   1 
ATOM   5094 C  CB  . GLN B 1 330 ? 42.25600  -6.35400  36.93300 1.000 32.21000 ? 324 GLN B CB  1 
ATOM   5095 C  CG  . GLN B 1 330 ? 43.62000  -7.03900  37.19200 1.000 38.54000 ? 324 GLN B CG  1 
ATOM   5096 C  CD  . GLN B 1 330 ? 44.77000  -6.08700  37.57800 1.000 50.11000 ? 324 GLN B CD  1 
ATOM   5097 O  OE1 . GLN B 1 330 ? 44.56400  -5.07000  38.26100 1.000 50.80000 ? 324 GLN B OE1 1 
ATOM   5098 N  NE2 . GLN B 1 330 ? 45.99800  -6.42700  37.14600 1.000 45.36000 ? 324 GLN B NE2 1 
ATOM   5099 N  N   . LEU B 1 331 ? 39.44600  -6.60000  34.97600 1.000 29.42000 ? 325 LEU B N   1 
ATOM   5100 C  CA  . LEU B 1 331 ? 38.18900  -5.97100  34.57700 1.000 29.33000 ? 325 LEU B CA  1 
ATOM   5101 C  C   . LEU B 1 331 ? 37.14300  -6.98000  34.10100 1.000 25.91000 ? 325 LEU B C   1 
ATOM   5102 O  O   . LEU B 1 331 ? 36.14500  -6.58600  33.48000 1.000 23.89000 ? 325 LEU B O   1 
ATOM   5103 C  CB  . LEU B 1 331 ? 38.46100  -4.94400  33.47900 1.000 27.26000 ? 325 LEU B CB  1 
ATOM   5104 C  CG  . LEU B 1 331 ? 39.55300  -3.94900  33.89900 1.000 26.11000 ? 325 LEU B CG  1 
ATOM   5105 C  CD1 . LEU B 1 331 ? 39.86800  -3.00900  32.75100 1.000 24.28000 ? 325 LEU B CD1 1 
ATOM   5106 C  CD2 . LEU B 1 331 ? 39.02500  -3.15900  35.09500 1.000 25.33000 ? 325 LEU B CD2 1 
ATOM   5107 N  N   . ALA B 1 332 ? 37.36300  -8.26900  34.38700 1.000 29.34000 ? 326 ALA B N   1 
ATOM   5108 C  CA  . ALA B 1 332 ? 36.52800  -9.34100  33.84800 1.000 26.12000 ? 326 ALA B CA  1 
ATOM   5109 C  C   . ALA B 1 332 ? 35.07200  -9.20700  34.25900 1.000 24.36000 ? 326 ALA B C   1 
ATOM   5110 O  O   . ALA B 1 332 ? 34.17400  -9.58200  33.49900 1.000 25.11000 ? 326 ALA B O   1 
ATOM   5111 C  CB  . ALA B 1 332 ? 37.09300  -10.69300 34.31000 1.000 30.77000 ? 326 ALA B CB  1 
ATOM   5112 N  N   . SER B 1 333 ? 34.80000  -8.70100  35.46000 1.000 23.96000 ? 327 SER B N   1 
ATOM   5113 C  CA  . SER B 1 333 ? 33.40000  -8.53300  35.85400 1.000 27.71000 ? 327 SER B CA  1 
ATOM   5114 C  C   . SER B 1 333 ? 32.68900  -7.47200  35.00600 1.000 25.09000 ? 327 SER B C   1 
ATOM   5115 O  O   . SER B 1 333 ? 31.46800  -7.56200  34.78000 1.000 24.80000 ? 327 SER B O   1 
ATOM   5116 C  CB  . SER B 1 333 ? 33.32000  -8.17700  37.34200 1.000 28.16000 ? 327 SER B CB  1 
ATOM   5117 O  OG  . SER B 1 333 ? 34.05400  -6.97500  37.59500 1.000 35.83000 ? 327 SER B OG  1 
ATOM   5118 N  N   . PHE B 1 334 ? 33.43200  -6.48200  34.50200 1.000 25.67000 ? 328 PHE B N   1 
ATOM   5119 C  CA  . PHE B 1 334 ? 32.86000  -5.50200  33.58100 1.000 23.06000 ? 328 PHE B CA  1 
ATOM   5120 C  C   . PHE B 1 334 ? 32.78400  -6.03600  32.16300 1.000 20.89000 ? 328 PHE B C   1 
ATOM   5121 O  O   . PHE B 1 334 ? 31.84600  -5.70600  31.44200 1.000 22.00000 ? 328 PHE B O   1 
ATOM   5122 C  CB  . PHE B 1 334 ? 33.69400  -4.21300  33.56400 1.000 23.31000 ? 328 PHE B CB  1 
ATOM   5123 C  CG  . PHE B 1 334 ? 33.68300  -3.46000  34.86300 1.000 22.50000 ? 328 PHE B CG  1 
ATOM   5124 C  CD1 . PHE B 1 334 ? 32.60500  -2.64700  35.20200 1.000 22.01000 ? 328 PHE B CD1 1 
ATOM   5125 C  CD2 . PHE B 1 334 ? 34.74300  -3.55800  35.73100 1.000 24.46000 ? 328 PHE B CD2 1 
ATOM   5126 C  CE1 . PHE B 1 334 ? 32.59600  -1.94500  36.41400 1.000 25.53000 ? 328 PHE B CE1 1 
ATOM   5127 C  CE2 . PHE B 1 334 ? 34.75600  -2.84900  36.93300 1.000 24.74000 ? 328 PHE B CE2 1 
ATOM   5128 C  CZ  . PHE B 1 334 ? 33.68400  -2.04200  37.27700 1.000 23.13000 ? 328 PHE B CZ  1 
ATOM   5129 N  N   . HIS B 1 335 ? 33.76900  -6.83600  31.74200 1.000 19.87000 ? 329 HIS B N   1 
ATOM   5130 C  CA  . HIS B 1 335 ? 33.85000  -7.29300  30.35900 1.000 20.58000 ? 329 HIS B CA  1 
ATOM   5131 C  C   . HIS B 1 335 ? 32.67100  -8.19600  29.99500 1.000 23.87000 ? 329 HIS B C   1 
ATOM   5132 O  O   . HIS B 1 335 ? 32.08100  -8.07100  28.90700 1.000 20.45000 ? 329 HIS B O   1 
ATOM   5133 C  CB  . HIS B 1 335 ? 35.18300  -8.01600  30.16000 1.000 21.39000 ? 329 HIS B CB  1 
ATOM   5134 C  CG  . HIS B 1 335 ? 35.51900  -8.31900  28.72900 1.000 22.34000 ? 329 HIS B CG  1 
ATOM   5135 N  ND1 . HIS B 1 335 ? 36.59500  -9.10800  28.37300 1.000 27.63000 ? 329 HIS B ND1 1 
ATOM   5136 C  CD2 . HIS B 1 335 ? 34.94000  -7.92200  27.56600 1.000 23.49000 ? 329 HIS B CD2 1 
ATOM   5137 C  CE1 . HIS B 1 335 ? 36.65100  -9.20900  27.05400 1.000 27.59000 ? 329 HIS B CE1 1 
ATOM   5138 N  NE2 . HIS B 1 335 ? 35.66500  -8.48800  26.53900 1.000 22.52000 ? 329 HIS B NE2 1 
ATOM   5139 N  N   . HIS B 1 336 ? 32.30800  -9.10100  30.89000 1.000 23.01000 ? 330 HIS B N   1 
ATOM   5140 C  CA  . HIS B 1 336 ? 31.25500  -10.09000 30.64400 1.000 25.40000 ? 330 HIS B CA  1 
ATOM   5141 C  C   . HIS B 1 336 ? 30.32300  -10.03100 31.84400 1.000 23.88000 ? 330 HIS B C   1 
ATOM   5142 O  O   . HIS B 1 336 ? 30.46900  -10.81200 32.78900 1.000 26.40000 ? 330 HIS B O   1 
ATOM   5143 C  CB  . HIS B 1 336 ? 31.84300  -11.48800 30.42300 1.000 25.70000 ? 330 HIS B CB  1 
ATOM   5144 C  CG  . HIS B 1 336 ? 32.72900  -11.56900 29.21100 1.000 29.13000 ? 330 HIS B CG  1 
ATOM   5145 N  ND1 . HIS B 1 336 ? 34.09900  -11.71000 29.29000 1.000 33.48000 ? 330 HIS B ND1 1 
ATOM   5146 C  CD2 . HIS B 1 336 ? 32.44200  -11.46500 27.89200 1.000 27.21000 ? 330 HIS B CD2 1 
ATOM   5147 C  CE1 . HIS B 1 336 ? 34.61600  -11.71700 28.07300 1.000 31.37000 ? 330 HIS B CE1 1 
ATOM   5148 N  NE2 . HIS B 1 336 ? 33.62900  -11.56700 27.20600 1.000 28.28000 ? 330 HIS B NE2 1 
ATOM   5149 N  N   . PRO B 1 337 ? 29.38200  -9.07700  31.85200 1.000 23.47000 ? 331 PRO B N   1 
ATOM   5150 C  CA  . PRO B 1 337 ? 28.51200  -8.88800  33.01500 1.000 27.34000 ? 331 PRO B CA  1 
ATOM   5151 C  C   . PRO B 1 337 ? 27.77400  -10.16900 33.38800 1.000 26.92000 ? 331 PRO B C   1 
ATOM   5152 O  O   . PRO B 1 337 ? 27.30800  -10.90600 32.52500 1.000 27.10000 ? 331 PRO B O   1 
ATOM   5153 C  CB  . PRO B 1 337 ? 27.53700  -7.80600  32.54900 1.000 25.14000 ? 331 PRO B CB  1 
ATOM   5154 C  CG  . PRO B 1 337 ? 28.23300  -7.06700  31.44700 1.000 24.52000 ? 331 PRO B CG  1 
ATOM   5155 C  CD  . PRO B 1 337 ? 29.24000  -8.00700  30.84600 1.000 22.82000 ? 331 PRO B CD  1 
ATOM   5156 N  N   . GLN B 1 338 ? 27.68200  -10.41500 34.69800 1.000 31.65000 ? 332 GLN B N   1 
ATOM   5157 C  CA  . GLN B 1 338 ? 26.88200  -11.50000 35.26300 1.000 32.00000 ? 332 GLN B CA  1 
ATOM   5158 C  C   . GLN B 1 338 ? 25.45200  -11.43400 34.75800 1.000 29.19000 ? 332 GLN B C   1 
ATOM   5159 O  O   . GLN B 1 338 ? 24.81800  -10.37500 34.82300 1.000 30.15000 ? 332 GLN B O   1 
ATOM   5160 C  CB  . GLN B 1 338 ? 26.86000  -11.37100 36.79100 1.000 30.77000 ? 332 GLN B CB  1 
ATOM   5161 C  CG  . GLN B 1 338 ? 28.18300  -11.61000 37.47000 1.000 40.46000 ? 332 GLN B CG  1 
ATOM   5162 C  CD  . GLN B 1 338 ? 28.61700  -13.05300 37.34400 1.000 51.85000 ? 332 GLN B CD  1 
ATOM   5163 O  OE1 . GLN B 1 338 ? 29.38200  -13.40000 36.43300 1.000 53.68000 ? 332 GLN B OE1 1 
ATOM   5164 N  NE2 . GLN B 1 338 ? 28.11400  -13.91500 38.24500 1.000 53.45000 ? 332 GLN B NE2 1 
ATOM   5165 N  N   . ARG B 1 339 ? 24.93700  -12.55500 34.25800 1.000 28.76000 ? 333 ARG B N   1 
ATOM   5166 C  CA  . ARG B 1 339 ? 23.49700  -12.67100 33.96800 1.000 28.39000 ? 333 ARG B CA  1 
ATOM   5167 C  C   . ARG B 1 339 ? 22.93900  -13.87000 34.74300 1.000 30.54000 ? 333 ARG B C   1 
ATOM   5168 O  O   . ARG B 1 339 ? 22.73800  -14.95700 34.18600 1.000 28.84000 ? 333 ARG B O   1 
ATOM   5169 C  CB  . ARG B 1 339 ? 23.25400  -12.77700 32.46700 1.000 32.54000 ? 333 ARG B CB  1 
ATOM   5170 C  CG  . ARG B 1 339 ? 23.37200  -11.44800 31.71800 1.000 27.89000 ? 333 ARG B CG  1 
ATOM   5171 C  CD  . ARG B 1 339 ? 22.33500  -10.47900 32.24000 1.000 31.83000 ? 333 ARG B CD  1 
ATOM   5172 N  NE  . ARG B 1 339 ? 22.35400  -9.20400  31.52800 1.000 31.96000 ? 333 ARG B NE  1 
ATOM   5173 C  CZ  . ARG B 1 339 ? 23.06500  -8.14000  31.88700 1.000 33.04000 ? 333 ARG B CZ  1 
ATOM   5174 N  NH1 . ARG B 1 339 ? 23.91400  -8.18000  32.90900 1.000 26.75000 ? 333 ARG B NH1 1 
ATOM   5175 N  NH2 . ARG B 1 339 ? 22.91600  -7.00000  31.20600 1.000 29.36000 ? 333 ARG B NH2 1 
ATOM   5176 N  N   . VAL B 1 340 ? 22.67100  -13.65500 36.04100 1.000 29.23000 ? 334 VAL B N   1 
ATOM   5177 C  CA  . VAL B 1 340 ? 22.31600  -14.71500 36.98600 1.000 30.45000 ? 334 VAL B CA  1 
ATOM   5178 C  C   . VAL B 1 340 ? 21.00300  -14.35500 37.68800 1.000 31.99000 ? 334 VAL B C   1 
ATOM   5179 O  O   . VAL B 1 340 ? 20.86700  -13.25300 38.24000 1.000 30.60000 ? 334 VAL B O   1 
ATOM   5180 C  CB  . VAL B 1 340 ? 23.44200  -14.93000 38.01300 1.000 33.95000 ? 334 VAL B CB  1 
ATOM   5181 C  CG1 . VAL B 1 340 ? 23.00200  -15.87500 39.08300 1.000 31.09000 ? 334 VAL B CG1 1 
ATOM   5182 C  CG2 . VAL B 1 340 ? 24.74300  -15.43400 37.30800 1.000 33.37000 ? 334 VAL B CG2 1 
ATOM   5183 N  N   . ASN B 1 341 ? 20.03300  -15.27600 37.66800 1.000 30.84000 ? 335 ASN B N   1 
ATOM   5184 C  CA  . ASN B 1 341 ? 18.69100  -14.94300 38.13300 1.000 25.87000 ? 335 ASN B CA  1 
ATOM   5185 C  C   . ASN B 1 341 ? 18.64600  -15.00700 39.67000 1.000 28.20000 ? 335 ASN B C   1 
ATOM   5186 O  O   . ASN B 1 341 ? 19.67300  -15.15800 40.33600 1.000 30.60000 ? 335 ASN B O   1 
ATOM   5187 C  CB  . ASN B 1 341 ? 17.66300  -15.83700 37.44000 1.000 25.70000 ? 335 ASN B CB  1 
ATOM   5188 C  CG  . ASN B 1 341 ? 17.67000  -17.28000 37.93800 1.000 28.49000 ? 335 ASN B CG  1 
ATOM   5189 O  OD1 . ASN B 1 341 ? 18.37400  -17.65500 38.90700 1.000 30.65000 ? 335 ASN B OD1 1 
ATOM   5190 N  ND2 . ASN B 1 341 ? 16.83200  -18.10400 37.30200 1.000 28.33000 ? 335 ASN B ND2 1 
ATOM   5191 N  N   . THR B 1 342 ? 17.45000  -14.91900 40.25900 1.000 25.40000 ? 336 THR B N   1 
ATOM   5192 C  CA  . THR B 1 342 ? 17.33200  -14.82000 41.71600 1.000 33.20000 ? 336 THR B CA  1 
ATOM   5193 C  C   . THR B 1 342 ? 17.59800  -16.14000 42.44400 1.000 35.74000 ? 336 THR B C   1 
ATOM   5194 O  O   . THR B 1 342 ? 17.63100  -16.15200 43.68300 1.000 30.22000 ? 336 THR B O   1 
ATOM   5195 C  CB  . THR B 1 342 ? 15.94100  -14.28700 42.10300 1.000 32.38000 ? 336 THR B CB  1 
ATOM   5196 O  OG1 . THR B 1 342 ? 14.93300  -15.23900 41.73300 1.000 28.63000 ? 336 THR B OG1 1 
ATOM   5197 C  CG2 . THR B 1 342 ? 15.65800  -12.94400 41.39400 1.000 30.65000 ? 336 THR B CG2 1 
ATOM   5198 N  N   . MET B 1 343 ? 17.76700  -17.25000 41.71700 1.000 35.34000 ? 337 MET B N   1 
ATOM   5199 C  CA  . MET B 1 343 ? 18.09500  -18.53900 42.31600 1.000 33.00000 ? 337 MET B CA  1 
ATOM   5200 C  C   . MET B 1 343 ? 19.48200  -19.00700 41.90200 1.000 33.14000 ? 337 MET B C   1 
ATOM   5201 O  O   . MET B 1 343 ? 19.78100  -20.20700 41.97600 1.000 32.14000 ? 337 MET B O   1 
ATOM   5202 C  CB  . MET B 1 343 ? 17.04600  -19.59000 41.94700 1.000 28.70000 ? 337 MET B CB  1 
ATOM   5203 C  CG  . MET B 1 343 ? 15.64500  -19.20700 42.42100 1.000 33.74000 ? 337 MET B CG  1 
ATOM   5204 S  SD  . MET B 1 343 ? 15.49400  -19.26900 44.23400 1.000 35.51000 ? 337 MET B SD  1 
ATOM   5205 C  CE  . MET B 1 343 ? 15.22500  -21.03800 44.47100 1.000 33.72000 ? 337 MET B CE  1 
ATOM   5206 N  N   . GLY B 1 344 ? 20.29700  -18.08700 41.40400 1.000 32.78000 ? 338 GLY B N   1 
ATOM   5207 C  CA  . GLY B 1 344 ? 21.68000  -18.36700 41.10200 1.000 35.33000 ? 338 GLY B CA  1 
ATOM   5208 C  C   . GLY B 1 344 ? 21.91600  -19.15400 39.84100 1.000 35.61000 ? 338 GLY B C   1 
ATOM   5209 O  O   . GLY B 1 344 ? 22.99500  -19.74000 39.67900 1.000 37.00000 ? 338 GLY B O   1 
ATOM   5210 N  N   . VAL B 1 345 ? 20.94200  -19.20500 38.94700 1.000 33.88000 ? 339 VAL B N   1 
ATOM   5211 C  CA  . VAL B 1 345 ? 21.12100  -19.83800 37.64000 1.000 38.55000 ? 339 VAL B CA  1 
ATOM   5212 C  C   . VAL B 1 345 ? 21.55800  -18.78300 36.63100 1.000 31.44000 ? 339 VAL B C   1 
ATOM   5213 O  O   . VAL B 1 345 ? 20.96900  -17.68800 36.56200 1.000 24.94000 ? 339 VAL B O   1 
ATOM   5214 C  CB  . VAL B 1 345 ? 19.82300  -20.52800 37.18600 1.000 32.32000 ? 339 VAL B CB  1 
ATOM   5215 C  CG1 . VAL B 1 345 ? 20.03900  -21.26900 35.89300 1.000 31.40000 ? 339 VAL B CG1 1 
ATOM   5216 C  CG2 . VAL B 1 345 ? 19.35700  -21.46300 38.25900 1.000 31.70000 ? 339 VAL B CG2 1 
ATOM   5217 N  N   . THR B 1 346 ? 22.59200  -19.10900 35.84400 1.000 31.86000 ? 340 THR B N   1 
ATOM   5218 C  CA  . THR B 1 346 ? 22.98800  -18.23900 34.74100 1.000 26.65000 ? 340 THR B CA  1 
ATOM   5219 C  C   . THR B 1 346 ? 21.93800  -18.32600 33.63600 1.000 27.81000 ? 340 THR B C   1 
ATOM   5220 O  O   . THR B 1 346 ? 21.68300  -19.41100 33.12200 1.000 30.79000 ? 340 THR B O   1 
ATOM   5221 C  CB  . THR B 1 346 ? 24.35300  -18.64200 34.19300 1.000 33.55000 ? 340 THR B CB  1 
ATOM   5222 O  OG1 . THR B 1 346 ? 25.36300  -18.31000 35.14800 1.000 33.75000 ? 340 THR B OG1 1 
ATOM   5223 C  CG2 . THR B 1 346 ? 24.64000  -17.86200 32.90500 1.000 27.71000 ? 340 THR B CG2 1 
ATOM   5224 N  N   . THR B 1 347 ? 21.35200  -17.18000 33.25000 1.000 25.21000 ? 341 THR B N   1 
ATOM   5225 C  CA  . THR B 1 347 ? 20.26700  -17.14500 32.28200 1.000 24.12000 ? 341 THR B CA  1 
ATOM   5226 C  C   . THR B 1 347 ? 20.67600  -16.59200 30.92600 1.000 21.64000 ? 341 THR B C   1 
ATOM   5227 O  O   . THR B 1 347 ? 19.89300  -16.69400 29.97900 1.000 22.36000 ? 341 THR B O   1 
ATOM   5228 C  CB  . THR B 1 347 ? 19.08600  -16.32000 32.82100 1.000 23.05000 ? 341 THR B CB  1 
ATOM   5229 O  OG1 . THR B 1 347 ? 19.55100  -15.03300 33.21900 1.000 24.27000 ? 341 THR B OG1 1 
ATOM   5230 C  CG2 . THR B 1 347 ? 18.47600  -16.98300 34.02700 1.000 26.81000 ? 341 THR B CG2 1 
ATOM   5231 N  N   . GLY B 1 348 ? 21.87800  -16.04400 30.78600 1.000 25.71000 ? 342 GLY B N   1 
ATOM   5232 C  CA  . GLY B 1 348 ? 22.29400  -15.52200 29.49500 1.000 19.89000 ? 342 GLY B CA  1 
ATOM   5233 C  C   . GLY B 1 348 ? 23.61700  -14.80400 29.61300 1.000 22.78000 ? 342 GLY B C   1 
ATOM   5234 O  O   . GLY B 1 348 ? 24.37000  -15.03100 30.56700 1.000 24.32000 ? 342 GLY B O   1 
ATOM   5235 N  N   . GLY B 1 349 ? 23.87500  -13.91600 28.65400 1.000 20.69000 ? 343 GLY B N   1 
ATOM   5236 C  CA  . GLY B 1 349 ? 25.11600  -13.16700 28.68600 1.000 21.61000 ? 343 GLY B CA  1 
ATOM   5237 C  C   . GLY B 1 349 ? 25.16400  -12.01400 27.69300 1.000 23.47000 ? 343 GLY B C   1 
ATOM   5238 O  O   . GLY B 1 349 ? 24.15400  -11.63200 27.10200 1.000 23.80000 ? 343 GLY B O   1 
ATOM   5239 N  N   . VAL B 1 350 ? 26.37700  -11.50600 27.47900 1.000 20.54000 ? 344 VAL B N   1 
ATOM   5240 C  CA  A VAL B 1 350 ? 26.64400  -10.36200 26.61000 0.500 19.45000 ? 344 VAL B CA  1 
ATOM   5241 C  CA  B VAL B 1 350 ? 26.64500  -10.36500 26.61300 0.500 19.45000 ? 344 VAL B CA  1 
ATOM   5242 C  C   . VAL B 1 350 ? 27.47200  -10.84100 25.42600 1.000 20.39000 ? 344 VAL B C   1 
ATOM   5243 O  O   . VAL B 1 350 ? 28.32900  -11.71400 25.56800 1.000 23.14000 ? 344 VAL B O   1 
ATOM   5244 C  CB  A VAL B 1 350 ? 27.37000  -9.22600  27.36000 0.500 21.02000 ? 344 VAL B CB  1 
ATOM   5245 C  CB  B VAL B 1 350 ? 27.37700  -9.27300  27.40800 0.500 21.02000 ? 344 VAL B CB  1 
ATOM   5246 C  CG1 A VAL B 1 350 ? 28.86800  -9.55800  27.59600 0.500 21.24000 ? 344 VAL B CG1 1 
ATOM   5247 C  CG1 B VAL B 1 350 ? 27.76000  -8.08900  26.51100 0.500 17.33000 ? 344 VAL B CG1 1 
ATOM   5248 C  CG2 A VAL B 1 350 ? 27.23900  -7.91300  26.59400 0.500 17.52000 ? 344 VAL B CG2 1 
ATOM   5249 C  CG2 B VAL B 1 350 ? 26.53100  -8.84700  28.59700 0.500 21.12000 ? 344 VAL B CG2 1 
ATOM   5250 N  N   . SER B 1 351 ? 27.20200  -10.30000 24.24700 1.000 18.15000 ? 345 SER B N   1 
ATOM   5251 C  CA  . SER B 1 351 ? 28.05500  -10.60200 23.10200 1.000 16.05000 ? 345 SER B CA  1 
ATOM   5252 C  C   . SER B 1 351 ? 28.30600  -9.31000  22.32300 1.000 19.38000 ? 345 SER B C   1 
ATOM   5253 O  O   . SER B 1 351 ? 27.62000  -8.29600  22.51100 1.000 19.05000 ? 345 SER B O   1 
ATOM   5254 C  CB  . SER B 1 351 ? 27.46100  -11.70300 22.24000 1.000 22.74000 ? 345 SER B CB  1 
ATOM   5255 O  OG  . SER B 1 351 ? 26.17500  -11.34100 21.84200 1.000 27.17000 ? 345 SER B OG  1 
ATOM   5256 N  N   . PHE B 1 352 ? 29.30800  -9.35200  21.43700 1.000 17.01000 ? 346 PHE B N   1 
ATOM   5257 C  CA  . PHE B 1 352 ? 29.86300  -8.15400  20.80600 1.000 16.99000 ? 346 PHE B CA  1 
ATOM   5258 C  C   . PHE B 1 352 ? 29.87200  -8.29200  19.29200 1.000 20.23000 ? 346 PHE B C   1 
ATOM   5259 O  O   . PHE B 1 352 ? 30.93900  -8.32400  18.66600 1.000 20.27000 ? 346 PHE B O   1 
ATOM   5260 C  CB  . PHE B 1 352 ? 31.27800  -7.92300  21.32900 1.000 19.11000 ? 346 PHE B CB  1 
ATOM   5261 C  CG  . PHE B 1 352 ? 31.35300  -7.77400  22.81000 1.000 14.95000 ? 346 PHE B CG  1 
ATOM   5262 C  CD1 . PHE B 1 352 ? 30.90100  -6.61300  23.41700 1.000 15.76000 ? 346 PHE B CD1 1 
ATOM   5263 C  CD2 . PHE B 1 352 ? 31.86700  -8.79600  23.58900 1.000 18.63000 ? 346 PHE B CD2 1 
ATOM   5264 C  CE1 . PHE B 1 352 ? 30.97000  -6.47300  24.79900 1.000 17.21000 ? 346 PHE B CE1 1 
ATOM   5265 C  CE2 . PHE B 1 352 ? 31.94700  -8.67500  24.97500 1.000 17.66000 ? 346 PHE B CE2 1 
ATOM   5266 C  CZ  . PHE B 1 352 ? 31.50000  -7.51000  25.57400 1.000 15.50000 ? 346 PHE B CZ  1 
ATOM   5267 N  N   . PRO B 1 353 ? 28.69500  -8.39000  18.66300 1.000 20.23000 ? 347 PRO B N   1 
ATOM   5268 C  CA  . PRO B 1 353 ? 28.67600  -8.42600  17.18800 1.000 22.01000 ? 347 PRO B CA  1 
ATOM   5269 C  C   . PRO B 1 353 ? 28.92500  -7.04200  16.61300 1.000 24.21000 ? 347 PRO B C   1 
ATOM   5270 O  O   . PRO B 1 353 ? 28.02200  -6.36800  16.08400 1.000 26.65000 ? 347 PRO B O   1 
ATOM   5271 C  CB  . PRO B 1 353 ? 27.26300  -8.94300  16.88300 1.000 18.15000 ? 347 PRO B CB  1 
ATOM   5272 C  CG  . PRO B 1 353 ? 26.44900  -8.33700  17.96200 1.000 20.61000 ? 347 PRO B CG  1 
ATOM   5273 C  CD  . PRO B 1 353 ? 27.33100  -8.34500  19.22500 1.000 18.33000 ? 347 PRO B CD  1 
ATOM   5274 N  N   . PHE B 1 354 ? 30.14700  -6.55200  16.78800 1.000 21.53000 ? 348 PHE B N   1 
ATOM   5275 C  CA  . PHE B 1 354 ? 30.61900  -5.39000  16.05800 1.000 21.60000 ? 348 PHE B CA  1 
ATOM   5276 C  C   . PHE B 1 354 ? 31.97200  -5.74500  15.46700 1.000 25.65000 ? 348 PHE B C   1 
ATOM   5277 O  O   . PHE B 1 354 ? 32.60400  -6.73800  15.84100 1.000 24.43000 ? 348 PHE B O   1 
ATOM   5278 C  CB  . PHE B 1 354 ? 30.68000  -4.10200  16.92300 1.000 21.42000 ? 348 PHE B CB  1 
ATOM   5279 C  CG  . PHE B 1 354 ? 31.51500  -4.20000  18.19600 1.000 21.45000 ? 348 PHE B CG  1 
ATOM   5280 C  CD1 . PHE B 1 354 ? 32.90300  -4.27600  18.14500 1.000 20.34000 ? 348 PHE B CD1 1 
ATOM   5281 C  CD2 . PHE B 1 354 ? 30.90100  -4.12400  19.43600 1.000 21.51000 ? 348 PHE B CD2 1 
ATOM   5282 C  CE1 . PHE B 1 354 ? 33.67100  -4.32600  19.31200 1.000 19.00000 ? 348 PHE B CE1 1 
ATOM   5283 C  CE2 . PHE B 1 354 ? 31.65200  -4.17100  20.62200 1.000 22.19000 ? 348 PHE B CE2 1 
ATOM   5284 C  CZ  . PHE B 1 354 ? 33.04000  -4.28500  20.56000 1.000 19.33000 ? 348 PHE B CZ  1 
ATOM   5285 N  N   . LYS B 1 355 ? 32.39200  -4.95500  14.50600 1.000 23.32000 ? 349 LYS B N   1 
ATOM   5286 C  CA  . LYS B 1 355 ? 33.57000  -5.27600  13.72500 1.000 23.40000 ? 349 LYS B CA  1 
ATOM   5287 C  C   . LYS B 1 355 ? 34.40100  -4.00700  13.62900 1.000 22.43000 ? 349 LYS B C   1 
ATOM   5288 O  O   . LYS B 1 355 ? 33.98000  -3.01200  13.03200 1.000 22.43000 ? 349 LYS B O   1 
ATOM   5289 C  CB  . LYS B 1 355 ? 33.15700  -5.81500  12.36400 1.000 25.58000 ? 349 LYS B CB  1 
ATOM   5290 C  CG  . LYS B 1 355 ? 34.23300  -6.46800  11.57900 1.000 29.13000 ? 349 LYS B CG  1 
ATOM   5291 C  CD  . LYS B 1 355 ? 33.61000  -7.15600  10.39900 1.000 33.37000 ? 349 LYS B CD  1 
ATOM   5292 C  CE  . LYS B 1 355 ? 34.64800  -7.59000  9.43500  1.000 33.61000 ? 349 LYS B CE  1 
ATOM   5293 N  NZ  . LYS B 1 355 ? 34.03600  -8.23600  8.22600  1.000 45.85000 ? 349 LYS B NZ  1 
ATOM   5294 N  N   . LEU B 1 356 ? 35.57000  -4.02600  14.25000 1.000 23.60000 ? 350 LEU B N   1 
ATOM   5295 C  CA  . LEU B 1 356 ? 36.45000  -2.88200  14.17200 1.000 22.96000 ? 350 LEU B CA  1 
ATOM   5296 C  C   . LEU B 1 356 ? 36.83400  -2.66300  12.72300 1.000 27.11000 ? 350 LEU B C   1 
ATOM   5297 O  O   . LEU B 1 356 ? 37.13600  -3.61400  11.99800 1.000 24.94000 ? 350 LEU B O   1 
ATOM   5298 C  CB  . LEU B 1 356 ? 37.69700  -3.14500  15.00600 1.000 27.92000 ? 350 LEU B CB  1 
ATOM   5299 C  CG  . LEU B 1 356 ? 38.44300  -1.99900  15.64600 1.000 28.53000 ? 350 LEU B CG  1 
ATOM   5300 C  CD1 . LEU B 1 356 ? 37.50100  -1.04400  16.41200 1.000 21.41000 ? 350 LEU B CD1 1 
ATOM   5301 C  CD2 . LEU B 1 356 ? 39.46700  -2.65100  16.57200 1.000 31.20000 ? 350 LEU B CD2 1 
ATOM   5302 N  N   . ARG B 1 357 ? 36.83100  -1.42400  12.27500 1.000 20.48000 ? 351 ARG B N   1 
ATOM   5303 C  CA  . ARG B 1 357 ? 37.30500  -1.19500  10.91700 1.000 25.02000 ? 351 ARG B CA  1 
ATOM   5304 C  C   . ARG B 1 357 ? 38.45300  -0.19200  10.93200 1.000 26.10000 ? 351 ARG B C   1 
ATOM   5305 O  O   . ARG B 1 357 ? 38.45500  0.74200   11.72900 1.000 24.76000 ? 351 ARG B O   1 
ATOM   5306 C  CB  . ARG B 1 357 ? 36.14800  -0.74800  10.00900 1.000 26.15000 ? 351 ARG B CB  1 
ATOM   5307 C  CG  . ARG B 1 357 ? 35.67200  0.69100   10.20600 1.000 28.85000 ? 351 ARG B CG  1 
ATOM   5308 C  CD  . ARG B 1 357 ? 34.33100  0.95400   9.47200  1.000 31.11000 ? 351 ARG B CD  1 
ATOM   5309 N  NE  . ARG B 1 357 ? 33.89600  2.35400   9.52500  1.000 29.87000 ? 351 ARG B NE  1 
ATOM   5310 C  CZ  . ARG B 1 357 ? 33.09200  2.86600   10.45600 1.000 29.15000 ? 351 ARG B CZ  1 
ATOM   5311 N  NH1 . ARG B 1 357 ? 32.61900  2.13000   11.45000 1.000 23.96000 ? 351 ARG B NH1 1 
ATOM   5312 N  NH2 . ARG B 1 357 ? 32.74700  4.14900   10.38200 1.000 29.17000 ? 351 ARG B NH2 1 
ATOM   5313 N  N   . GLY B 1 358 ? 39.45400  -0.41800  10.07800 1.000 26.27000 ? 352 GLY B N   1 
ATOM   5314 C  CA  . GLY B 1 358 ? 40.58300  0.48500   9.89800  1.000 26.63000 ? 352 GLY B CA  1 
ATOM   5315 C  C   . GLY B 1 358 ? 40.41600  1.38300   8.67600  1.000 41.89000 ? 352 GLY B C   1 
ATOM   5316 O  O   . GLY B 1 358 ? 41.26800  2.24500   8.37500  1.000 55.10000 ? 352 GLY B O   1 
ATOM   5317 N  N   . ASP B 1 364 ? 38.53400  -6.05100  3.20200  1.000 74.91000 ? 358 ASP B N   1 
ATOM   5318 C  CA  . ASP B 1 364 ? 37.29700  -5.55900  2.59400  1.000 73.40000 ? 358 ASP B CA  1 
ATOM   5319 C  C   . ASP B 1 364 ? 37.48700  -5.27800  1.10400  1.000 70.73000 ? 358 ASP B C   1 
ATOM   5320 O  O   . ASP B 1 364 ? 38.49800  -4.69000  0.70300  1.000 72.29000 ? 358 ASP B O   1 
ATOM   5321 C  CB  . ASP B 1 364 ? 36.80600  -4.27400  3.28800  1.000 80.06000 ? 358 ASP B CB  1 
ATOM   5322 C  CG  . ASP B 1 364 ? 36.15800  -4.53200  4.64600  1.000 78.60000 ? 358 ASP B CG  1 
ATOM   5323 O  OD1 . ASP B 1 364 ? 35.58500  -5.63000  4.83400  1.000 80.01000 ? 358 ASP B OD1 1 
ATOM   5324 O  OD2 . ASP B 1 364 ? 36.21200  -3.62400  5.51600  1.000 79.17000 ? 358 ASP B OD2 1 
ATOM   5325 N  N   . ASP B 1 365 ? 36.51400  -5.70500  0.29500  1.000 67.29000 ? 359 ASP B N   1 
ATOM   5326 C  CA  . ASP B 1 365 ? 36.43600  -5.28400  -1.10500 1.000 59.55000 ? 359 ASP B CA  1 
ATOM   5327 C  C   . ASP B 1 365 ? 36.33500  -3.75900  -1.16400 1.000 58.64000 ? 359 ASP B C   1 
ATOM   5328 O  O   . ASP B 1 365 ? 35.56600  -3.16700  -0.38500 1.000 55.64000 ? 359 ASP B O   1 
ATOM   5329 C  CB  . ASP B 1 365 ? 35.20900  -5.92800  -1.77700 1.000 55.03000 ? 359 ASP B CB  1 
ATOM   5330 C  CG  . ASP B 1 365 ? 35.24700  -5.86600  -3.32100 1.000 59.99000 ? 359 ASP B CG  1 
ATOM   5331 O  OD1 . ASP B 1 365 ? 35.60000  -4.81600  -3.91100 1.000 59.45000 ? 359 ASP B OD1 1 
ATOM   5332 O  OD2 . ASP B 1 365 ? 34.91200  -6.88700  -3.96400 1.000 56.31000 ? 359 ASP B OD2 1 
ATOM   5333 N  N   . PRO B 1 366 ? 37.08800  -3.08200  -2.05200 1.000 57.16000 ? 360 PRO B N   1 
ATOM   5334 C  CA  . PRO B 1 366 ? 36.92600  -1.61600  -2.18200 1.000 53.34000 ? 360 PRO B CA  1 
ATOM   5335 C  C   . PRO B 1 366 ? 35.47100  -1.16200  -2.36400 1.000 49.88000 ? 360 PRO B C   1 
ATOM   5336 O  O   . PRO B 1 366 ? 35.12900  -0.02300  -1.99900 1.000 44.38000 ? 360 PRO B O   1 
ATOM   5337 C  CB  . PRO B 1 366 ? 37.77800  -1.27700  -3.41700 1.000 47.01000 ? 360 PRO B CB  1 
ATOM   5338 C  CG  . PRO B 1 366 ? 38.77000  -2.38300  -3.53100 1.000 52.18000 ? 360 PRO B CG  1 
ATOM   5339 C  CD  . PRO B 1 366 ? 38.13200  -3.61400  -2.95500 1.000 56.84000 ? 360 PRO B CD  1 
ATOM   5340 N  N   . ARG B 1 367 ? 34.60000  -2.03200  -2.89800 1.000 50.96000 ? 361 ARG B N   1 
ATOM   5341 C  CA  . ARG B 1 367 ? 33.19400  -1.71300  -3.13000 1.000 46.30000 ? 361 ARG B CA  1 
ATOM   5342 C  C   . ARG B 1 367 ? 32.30700  -1.85000  -1.89000 1.000 47.15000 ? 361 ARG B C   1 
ATOM   5343 O  O   . ARG B 1 367 ? 31.11200  -1.54400  -1.98200 1.000 45.38000 ? 361 ARG B O   1 
ATOM   5344 C  CB  . ARG B 1 367 ? 32.64600  -2.58300  -4.26700 1.000 44.74000 ? 361 ARG B CB  1 
ATOM   5345 C  CG  . ARG B 1 367 ? 33.24200  -2.23300  -5.62600 1.000 45.28000 ? 361 ARG B CG  1 
ATOM   5346 C  CD  . ARG B 1 367 ? 32.90700  -3.29500  -6.64600 1.000 47.75000 ? 361 ARG B CD  1 
ATOM   5347 N  NE  . ARG B 1 367 ? 33.46500  -4.59100  -6.27700 1.000 47.51000 ? 361 ARG B NE  1 
ATOM   5348 C  CZ  . ARG B 1 367 ? 33.52000  -5.65000  -7.07800 1.000 51.24000 ? 361 ARG B CZ  1 
ATOM   5349 N  NH1 . ARG B 1 367 ? 33.03500  -5.61700  -8.31500 1.000 52.54000 ? 361 ARG B NH1 1 
ATOM   5350 N  NH2 . ARG B 1 367 ? 34.07000  -6.77300  -6.62400 1.000 53.66000 ? 361 ARG B NH2 1 
ATOM   5351 N  N   . LEU B 1 368 ? 32.87600  -2.26900  -0.76900 1.000 47.07000 ? 362 LEU B N   1 
ATOM   5352 C  CA  . LEU B 1 368 ? 32.06800  -2.29000  0.47600  1.000 48.59000 ? 362 LEU B CA  1 
ATOM   5353 C  C   . LEU B 1 368 ? 32.12400  -0.89900  1.11100  1.000 49.88000 ? 362 LEU B C   1 
ATOM   5354 O  O   . LEU B 1 368 ? 33.18200  -0.52600  1.61900  1.000 51.08000 ? 362 LEU B O   1 
ATOM   5355 C  CB  . LEU B 1 368 ? 32.59400  -3.36500  1.42900  1.000 52.50000 ? 362 LEU B CB  1 
ATOM   5356 C  CG  . LEU B 1 368 ? 31.93800  -3.39500  2.81100  1.000 58.08000 ? 362 LEU B CG  1 
ATOM   5357 C  CD1 . LEU B 1 368 ? 30.43100  -3.56900  2.70100  1.000 49.19000 ? 362 LEU B CD1 1 
ATOM   5358 C  CD2 . LEU B 1 368 ? 32.53700  -4.49400  3.67300  1.000 58.91000 ? 362 LEU B CD2 1 
ATOM   5359 N  N   . ALA B 1 369 ? 31.00900  -0.18000  1.08100  1.000 48.81000 ? 363 ALA B N   1 
ATOM   5360 C  CA  . ALA B 1 369 ? 30.95400  1.17900   1.65800  1.000 44.54000 ? 363 ALA B CA  1 
ATOM   5361 C  C   . ALA B 1 369 ? 30.79600  1.13800   3.18100  1.000 45.40000 ? 363 ALA B C   1 
ATOM   5362 O  O   . ALA B 1 369 ? 29.90600  0.42100   3.66400  1.000 41.61000 ? 363 ALA B O   1 
ATOM   5363 C  CB  . ALA B 1 369 ? 29.83200  1.95100   1.02500  1.000 40.72000 ? 363 ALA B CB  1 
ATOM   5364 N  N   . ALA B 1 370 ? 31.61500  1.90900   3.88900  1.000 43.72000 ? 364 ALA B N   1 
ATOM   5365 C  CA  . ALA B 1 370 ? 31.53000  2.02800   5.34700  1.000 42.00000 ? 364 ALA B CA  1 
ATOM   5366 C  C   . ALA B 1 370 ? 30.85500  3.36000   5.69100  1.000 45.19000 ? 364 ALA B C   1 
ATOM   5367 O  O   . ALA B 1 370 ? 31.50200  4.37400   6.00100  1.000 38.49000 ? 364 ALA B O   1 
ATOM   5368 C  CB  . ALA B 1 370 ? 32.91600  1.90600   5.97800  1.000 41.88000 ? 364 ALA B CB  1 
ATOM   5369 N  N   . VAL B 1 371 ? 29.52200  3.34500   5.63700  1.000 40.59000 ? 365 VAL B N   1 
ATOM   5370 C  CA  . VAL B 1 371 ? 28.71200  4.53200   5.90400  1.000 39.66000 ? 365 VAL B CA  1 
ATOM   5371 C  C   . VAL B 1 371 ? 28.61300  4.71600   7.42100  1.000 43.31000 ? 365 VAL B C   1 
ATOM   5372 O  O   . VAL B 1 371 ? 27.93600  3.94700   8.11700  1.000 41.52000 ? 365 VAL B O   1 
ATOM   5373 C  CB  . VAL B 1 371 ? 27.32200  4.42500   5.25800  1.000 38.55000 ? 365 VAL B CB  1 
ATOM   5374 C  CG1 . VAL B 1 371 ? 26.53500  5.73300   5.42800  1.000 41.17000 ? 365 VAL B CG1 1 
ATOM   5375 C  CG2 . VAL B 1 371 ? 27.44700  4.04700   3.77600  1.000 36.86000 ? 365 VAL B CG2 1 
ATOM   5376 N  N   . ALA B 1 372 ? 29.30100  5.73700   7.93900  1.000 36.96000 ? 366 ALA B N   1 
ATOM   5377 C  CA  . ALA B 1 372 ? 29.26100  6.06100   9.36200  1.000 36.27000 ? 366 ALA B CA  1 
ATOM   5378 C  C   . ALA B 1 372 ? 27.81400  6.22400   9.82900  1.000 38.28000 ? 366 ALA B C   1 
ATOM   5379 O  O   . ALA B 1 372 ? 27.11900  7.16500   9.42200  1.000 44.03000 ? 366 ALA B O   1 
ATOM   5380 C  CB  . ALA B 1 372 ? 30.07800  7.33500   9.63800  1.000 30.69000 ? 366 ALA B CB  1 
ATOM   5381 N  N   . ARG B 1 373 ? 27.34100  5.29900   10.65500 1.000 37.92000 ? 367 ARG B N   1 
ATOM   5382 C  CA  . ARG B 1 373 ? 25.95700  5.33100   11.16500 1.000 40.09000 ? 367 ARG B CA  1 
ATOM   5383 C  C   . ARG B 1 373 ? 25.96200  4.79200   12.58800 1.000 36.95000 ? 367 ARG B C   1 
ATOM   5384 O  O   . ARG B 1 373 ? 26.93200  4.08000   12.97600 1.000 26.14000 ? 367 ARG B O   1 
ATOM   5385 C  CB  . ARG B 1 373 ? 24.99100  4.47800   10.31600 1.000 33.65000 ? 367 ARG B CB  1 
ATOM   5386 C  CG  . ARG B 1 373 ? 24.63000  5.02300   8.97900  1.000 43.07000 ? 367 ARG B CG  1 
ATOM   5387 C  CD  . ARG B 1 373 ? 23.26000  5.66500   8.97900  1.000 47.84000 ? 367 ARG B CD  1 
ATOM   5388 N  NE  . ARG B 1 373 ? 22.93200  6.09700   7.62100  1.000 51.08000 ? 367 ARG B NE  1 
ATOM   5389 C  CZ  . ARG B 1 373 ? 23.49700  7.13200   7.01000  1.000 52.40000 ? 367 ARG B CZ  1 
ATOM   5390 N  NH1 . ARG B 1 373 ? 24.36700  7.91200   7.63500  1.000 59.54000 ? 367 ARG B NH1 1 
ATOM   5391 N  NH2 . ARG B 1 373 ? 23.20200  7.37800   5.73300  1.000 45.59000 ? 367 ARG B NH2 1 
ATOM   5392 O  OXT . ARG B 1 373 ? 24.97100  5.01200   13.31300 1.000 31.23000 ? 367 ARG B OXT 1 
HETATM 5393 C  C1  . EDO C 2 .   ? 16.93300  -8.53100  17.56000 0.900 36.42000 ? 501 EDO A C1  1 
HETATM 5394 O  O1  . EDO C 2 .   ? 16.77400  -7.12600  17.83600 0.900 32.87000 ? 501 EDO A O1  1 
HETATM 5395 C  C2  . EDO C 2 .   ? 15.58600  -9.18200  17.27200 0.900 28.96000 ? 501 EDO A C2  1 
HETATM 5396 O  O2  . EDO C 2 .   ? 15.10700  -9.77500  18.49000 0.900 33.56000 ? 501 EDO A O2  1 
HETATM 5397 C  C1  . EDO D 2 .   ? 13.19100  -28.35900 44.03600 1.000 50.43000 ? 502 EDO A C1  1 
HETATM 5398 O  O1  . EDO D 2 .   ? 11.76000  -28.14600 44.04100 1.000 50.78000 ? 502 EDO A O1  1 
HETATM 5399 C  C2  . EDO D 2 .   ? 13.73100  -28.23700 42.61300 1.000 50.24000 ? 502 EDO A C2  1 
HETATM 5400 O  O2  . EDO D 2 .   ? 13.24300  -29.34600 41.82700 1.000 50.25000 ? 502 EDO A O2  1 
HETATM 5401 C  C1  . EDO E 2 .   ? 3.97800   -32.09100 47.84900 1.000 50.29000 ? 503 EDO A C1  1 
HETATM 5402 O  O1  . EDO E 2 .   ? 4.07800   -32.70400 46.55000 1.000 52.17000 ? 503 EDO A O1  1 
HETATM 5403 C  C2  . EDO E 2 .   ? 2.51400   -32.06600 48.25000 1.000 48.03000 ? 503 EDO A C2  1 
HETATM 5404 O  O2  . EDO E 2 .   ? 1.73200   -31.71000 47.10100 1.000 48.99000 ? 503 EDO A O2  1 
HETATM 5405 C  C1  . EDO F 2 .   ? 15.03100  -5.37800  16.01000 0.700 27.67000 ? 504 EDO A C1  1 
HETATM 5406 O  O1  . EDO F 2 .   ? 15.64000  -4.08500  16.19000 0.700 35.61000 ? 504 EDO A O1  1 
HETATM 5407 C  C2  . EDO F 2 .   ? 14.37200  -5.40200  14.63400 0.700 23.99000 ? 504 EDO A C2  1 
HETATM 5408 O  O2  . EDO F 2 .   ? 13.79800  -6.69000  14.47000 0.700 30.31000 ? 504 EDO A O2  1 
HETATM 5409 N  N   . ASN G 3 .   ? 9.38300   -11.98600 34.76700 1.000 31.60000 ? 505 ASN A N   1 
HETATM 5410 C  CA  . ASN G 3 .   ? 10.52500  -11.12200 35.03500 1.000 33.32000 ? 505 ASN A CA  1 
HETATM 5411 C  C   . ASN G 3 .   ? 11.59900  -11.85600 35.80100 1.000 31.76000 ? 505 ASN A C   1 
HETATM 5412 O  O   . ASN G 3 .   ? 11.36100  -12.75000 36.61800 1.000 28.84000 ? 505 ASN A O   1 
HETATM 5413 C  CB  . ASN G 3 .   ? 10.07800  -9.86200  35.78700 1.000 34.26000 ? 505 ASN A CB  1 
HETATM 5414 C  CG  . ASN G 3 .   ? 9.27700   -8.93600  34.89400 1.000 36.66000 ? 505 ASN A CG  1 
HETATM 5415 O  OD1 . ASN G 3 .   ? 9.22000   -9.17800  33.68300 1.000 37.92000 ? 505 ASN A OD1 1 
HETATM 5416 N  ND2 . ASN G 3 .   ? 8.65000   -7.87500  35.46600 1.000 37.73000 ? 505 ASN A ND2 1 
HETATM 5417 O  OXT . ASN G 3 .   ? 12.74500  -11.55600 35.57400 1.000 33.74000 ? 505 ASN A OXT 1 
HETATM 5418 C  C1  . EDO H 2 .   ? 9.96000   5.28800   42.31800 1.000 51.31000 ? 506 EDO A C1  1 
HETATM 5419 O  O1  . EDO H 2 .   ? 9.43300   6.61300   42.48900 1.000 55.07000 ? 506 EDO A O1  1 
HETATM 5420 C  C2  . EDO H 2 .   ? 10.02800  4.63600   43.68600 1.000 37.60000 ? 506 EDO A C2  1 
HETATM 5421 O  O2  . EDO H 2 .   ? 8.72100   4.17300   44.03300 1.000 43.98000 ? 506 EDO A O2  1 
HETATM 5422 C  C1  . EDO I 2 .   ? -7.57400  -18.53800 20.98500 1.000 41.91000 ? 507 EDO A C1  1 
HETATM 5423 O  O1  . EDO I 2 .   ? -7.17700  -17.96600 22.25400 1.000 40.04000 ? 507 EDO A O1  1 
HETATM 5424 C  C2  . EDO I 2 .   ? -7.11400  -19.98900 20.92600 1.000 40.86000 ? 507 EDO A C2  1 
HETATM 5425 O  O2  . EDO I 2 .   ? -7.49700  -20.60000 22.17500 1.000 41.52000 ? 507 EDO A O2  1 
HETATM 5426 CL CL  . CL  J 4 .   ? 20.74300  17.00400  34.39300 1.000 44.68000 ? 508 CL  A CL  1 
HETATM 5427 CD CD  . CD  K 5 .   ? 8.93500   -13.80200 36.52800 0.700 26.01000 ? 509 CD  A CD  1 
HETATM 5428 C  C1  . EDO L 2 .   ? 20.63600  -19.90700 30.22500 0.900 36.49000 ? 401 EDO B C1  1 
HETATM 5429 O  O1  . EDO L 2 .   ? 21.54400  -19.36300 29.22300 0.900 31.60000 ? 401 EDO B O1  1 
HETATM 5430 C  C2  . EDO L 2 .   ? 19.89900  -21.20500 29.88500 0.900 33.22000 ? 401 EDO B C2  1 
HETATM 5431 O  O2  . EDO L 2 .   ? 18.97800  -21.03200 28.78900 0.900 42.97000 ? 401 EDO B O2  1 
HETATM 5432 C  C1  . EDO M 2 .   ? 20.95400  -7.18100  17.14300 1.000 38.47000 ? 402 EDO B C1  1 
HETATM 5433 O  O1  . EDO M 2 .   ? 22.06200  -7.18500  16.21900 1.000 43.34000 ? 402 EDO B O1  1 
HETATM 5434 C  C2  . EDO M 2 .   ? 19.66000  -6.79000  16.44100 1.000 41.74000 ? 402 EDO B C2  1 
HETATM 5435 O  O2  . EDO M 2 .   ? 19.81500  -5.51700  15.79500 1.000 44.76000 ? 402 EDO B O2  1 
HETATM 5436 C  C1  . EDO N 2 .   ? 43.35200  18.30300  11.60900 1.000 39.78000 ? 403 EDO B C1  1 
HETATM 5437 O  O1  . EDO N 2 .   ? 42.10800  18.91600  11.98100 1.000 38.71000 ? 403 EDO B O1  1 
HETATM 5438 C  C2  . EDO N 2 .   ? 42.99900  16.97300  10.96600 1.000 43.17000 ? 403 EDO B C2  1 
HETATM 5439 O  O2  . EDO N 2 .   ? 41.83200  16.46600  11.63500 1.000 43.41000 ? 403 EDO B O2  1 
HETATM 5440 C  C1  . EDO O 2 .   ? 53.82300  15.95500  36.17900 1.000 36.30000 ? 404 EDO B C1  1 
HETATM 5441 O  O1  . EDO O 2 .   ? 53.81400  17.33100  36.60300 1.000 42.82000 ? 404 EDO B O1  1 
HETATM 5442 C  C2  . EDO O 2 .   ? 54.30700  15.75900  34.74800 1.000 33.34000 ? 404 EDO B C2  1 
HETATM 5443 O  O2  . EDO O 2 .   ? 54.57300  14.36400  34.48400 1.000 40.00000 ? 404 EDO B O2  1 
HETATM 5444 C  C1  . EDO P 2 .   ? 46.64300  23.21100  22.00800 1.000 27.86000 ? 405 EDO B C1  1 
HETATM 5445 O  O1  . EDO P 2 .   ? 46.26900  21.81700  21.79900 1.000 36.18000 ? 405 EDO B O1  1 
HETATM 5446 C  C2  . EDO P 2 .   ? 46.11200  24.16400  20.93800 1.000 34.17000 ? 405 EDO B C2  1 
HETATM 5447 O  O2  . EDO P 2 .   ? 45.63900  23.46100  19.75300 1.000 41.36000 ? 405 EDO B O2  1 
HETATM 5448 C  C1  . EDO Q 2 .   ? 51.39500  14.08600  45.11200 1.000 43.74000 ? 406 EDO B C1  1 
HETATM 5449 O  O1  . EDO Q 2 .   ? 51.51600  15.53100  45.11200 1.000 48.02000 ? 406 EDO B O1  1 
HETATM 5450 C  C2  . EDO Q 2 .   ? 50.30000  13.57800  46.06600 1.000 43.25000 ? 406 EDO B C2  1 
HETATM 5451 O  O2  . EDO Q 2 .   ? 49.05900  14.33000  46.02400 1.000 36.04000 ? 406 EDO B O2  1 
HETATM 5452 C  C1  . EDO R 2 .   ? 34.44400  37.99500  45.18800 1.000 51.31000 ? 407 EDO B C1  1 
HETATM 5453 O  O1  . EDO R 2 .   ? 35.20800  36.85800  45.63000 1.000 51.00000 ? 407 EDO B O1  1 
HETATM 5454 C  C2  . EDO R 2 .   ? 32.93900  37.68800  45.22900 1.000 53.14000 ? 407 EDO B C2  1 
HETATM 5455 O  O2  . EDO R 2 .   ? 32.34000  37.70300  43.91600 1.000 49.49000 ? 407 EDO B O2  1 
HETATM 5456 N  N   . ASN S 3 .   ? 29.46700  15.87000  34.51700 1.000 38.48000 ? 408 ASN B N   1 
HETATM 5457 C  CA  . ASN S 3 .   ? 28.25400  15.07900  34.71600 1.000 39.68000 ? 408 ASN B CA  1 
HETATM 5458 C  C   . ASN S 3 .   ? 27.14400  15.86800  35.37800 1.000 37.08000 ? 408 ASN B C   1 
HETATM 5459 O  O   . ASN S 3 .   ? 25.99100  15.57600  35.15500 1.000 38.27000 ? 408 ASN B O   1 
HETATM 5460 C  CB  . ASN S 3 .   ? 28.58200  13.83300  35.54600 1.000 41.85000 ? 408 ASN B CB  1 
HETATM 5461 C  CG  . ASN S 3 .   ? 29.42400  12.83900  34.76300 1.000 45.44000 ? 408 ASN B CG  1 
HETATM 5462 O  OD1 . ASN S 3 .   ? 29.41800  12.87700  33.52900 1.000 46.89000 ? 408 ASN B OD1 1 
HETATM 5463 N  ND2 . ASN S 3 .   ? 30.15700  11.95400  35.46400 1.000 47.35000 ? 408 ASN B ND2 1 
HETATM 5464 O  OXT . ASN S 3 .   ? 27.35000  16.81400  36.14500 1.000 34.19000 ? 408 ASN B OXT 1 
HETATM 5465 C  C1  . EDO T 2 .   ? 24.79200  13.37400  38.45700 1.000 44.60000 ? 409 EDO B C1  1 
HETATM 5466 O  O1  . EDO T 2 .   ? 24.06100  14.62300  38.51400 1.000 40.14000 ? 409 EDO B O1  1 
HETATM 5467 C  C2  . EDO T 2 .   ? 25.20700  13.03600  37.01000 1.000 40.50000 ? 409 EDO B C2  1 
HETATM 5468 O  O2  . EDO T 2 .   ? 25.93200  11.78100  36.99800 1.000 48.59000 ? 409 EDO B O2  1 
HETATM 5469 CL CL  . CL  U 4 .   ? 18.19300  -13.13500 35.16300 1.000 43.72000 ? 410 CL  B CL  1 
HETATM 5470 CD CD  . CD  V 5 .   ? 29.68000  17.89500  35.97800 0.700 27.18000 ? 411 CD  B CD  1 
HETATM 5471 O  O   . HOH W 6 .   ? -11.12100 -5.17400  16.80000 1.000 27.73000 ? 601 HOH A O   1 
HETATM 5472 O  O   . HOH W 6 .   ? -6.96600  -29.93200 31.46500 1.000 23.47000 ? 602 HOH A O   1 
HETATM 5473 O  O   . HOH W 6 .   ? -13.80600 -2.69600  32.26500 1.000 32.33000 ? 603 HOH A O   1 
HETATM 5474 O  O   . HOH W 6 .   ? 7.99300   -28.48500 47.32000 1.000 41.35000 ? 604 HOH A O   1 
HETATM 5475 O  O   . HOH W 6 .   ? 7.23700   -4.02300  3.79500  1.000 41.62000 ? 605 HOH A O   1 
HETATM 5476 O  O   . HOH W 6 .   ? 5.86700   -10.47100 37.34700 1.000 37.38000 ? 606 HOH A O   1 
HETATM 5477 O  O   . HOH W 6 .   ? 8.41900   0.56400   36.44300 1.000 32.41000 ? 607 HOH A O   1 
HETATM 5478 O  O   . HOH W 6 .   ? 9.96500   -16.22300 51.75700 1.000 35.21000 ? 608 HOH A O   1 
HETATM 5479 O  O   . HOH W 6 .   ? -18.10300 1.00100   22.80700 1.000 33.08000 ? 609 HOH A O   1 
HETATM 5480 O  O   . HOH W 6 .   ? 5.25200   -33.16500 31.84900 1.000 31.77000 ? 610 HOH A O   1 
HETATM 5481 O  O   . HOH W 6 .   ? -10.49800 -4.94800  12.63500 1.000 38.03000 ? 611 HOH A O   1 
HETATM 5482 O  O   . HOH W 6 .   ? 5.30200   7.38300   39.89800 1.000 34.80000 ? 612 HOH A O   1 
HETATM 5483 O  O   . HOH W 6 .   ? -16.48100 -2.28800  25.39400 1.000 35.75000 ? 613 HOH A O   1 
HETATM 5484 O  O   . HOH W 6 .   ? -2.95800  -27.38700 21.70200 1.000 41.31000 ? 614 HOH A O   1 
HETATM 5485 O  O   . HOH W 6 .   ? 15.06400  -11.53300 55.40300 1.000 39.68000 ? 615 HOH A O   1 
HETATM 5486 O  O   . HOH W 6 .   ? 6.21600   -23.26200 30.65200 1.000 29.54000 ? 616 HOH A O   1 
HETATM 5487 O  O   . HOH W 6 .   ? 16.24100  -22.78100 36.25400 1.000 39.09000 ? 617 HOH A O   1 
HETATM 5488 O  O   . HOH W 6 .   ? 11.56700  20.94900  33.67200 1.000 37.88000 ? 618 HOH A O   1 
HETATM 5489 O  O   . HOH W 6 .   ? 20.05700  -8.41000  57.13100 1.000 46.75000 ? 619 HOH A O   1 
HETATM 5490 O  O   . HOH W 6 .   ? 3.21400   -20.68100 13.80300 1.000 40.24000 ? 620 HOH A O   1 
HETATM 5491 O  O   . HOH W 6 .   ? -15.31800 -6.05000  21.66900 1.000 27.88000 ? 621 HOH A O   1 
HETATM 5492 O  O   . HOH W 6 .   ? -3.55200  14.65300  25.53200 1.000 41.61000 ? 622 HOH A O   1 
HETATM 5493 O  O   . HOH W 6 .   ? -15.91700 6.60600   17.64700 1.000 35.98000 ? 623 HOH A O   1 
HETATM 5494 O  O   . HOH W 6 .   ? -6.95900  8.26600   38.81100 1.000 37.50000 ? 624 HOH A O   1 
HETATM 5495 O  O   . HOH W 6 .   ? -14.14300 -0.95300  18.16600 1.000 30.26000 ? 625 HOH A O   1 
HETATM 5496 O  O   . HOH W 6 .   ? -3.23400  0.00500   6.13000  1.000 49.71000 ? 626 HOH A O   1 
HETATM 5497 O  O   . HOH W 6 .   ? 1.618     8.463     10.048   1.000 35.50000 ? 627 HOH A O   1 
HETATM 5498 O  O   . HOH W 6 .   ? 9.63000   -14.59700 55.08000 1.000 44.38000 ? 628 HOH A O   1 
HETATM 5499 O  O   . HOH W 6 .   ? 22.04100  24.48500  23.65700 1.000 36.78000 ? 629 HOH A O   1 
HETATM 5500 O  O   . HOH W 6 .   ? 13.40000  19.01000  24.32400 1.000 35.88000 ? 630 HOH A O   1 
HETATM 5501 O  O   . HOH W 6 .   ? 15.52600  -16.22500 18.78100 1.000 33.73000 ? 631 HOH A O   1 
HETATM 5502 O  O   . HOH W 6 .   ? 14.45500  -11.78600 20.68100 1.000 28.98000 ? 632 HOH A O   1 
HETATM 5503 O  O   . HOH W 6 .   ? 7.87100   -4.07900  51.95000 1.000 34.51000 ? 633 HOH A O   1 
HETATM 5504 O  O   . HOH W 6 .   ? 3.57300   15.47900  30.12400 1.000 30.88000 ? 634 HOH A O   1 
HETATM 5505 O  O   . HOH W 6 .   ? 9.13500   -12.53400 13.90600 1.000 31.74000 ? 635 HOH A O   1 
HETATM 5506 O  O   . HOH W 6 .   ? -17.29300 -1.22500  18.65800 1.000 37.76000 ? 636 HOH A O   1 
HETATM 5507 O  O   . HOH W 6 .   ? 12.23500  -9.14200  46.30900 1.000 29.26000 ? 637 HOH A O   1 
HETATM 5508 O  O   . HOH W 6 .   ? -1.89500  -36.43300 38.65400 1.000 26.89000 ? 638 HOH A O   1 
HETATM 5509 O  O   . HOH W 6 .   ? 6.68300   -32.96800 41.47400 1.000 41.33000 ? 639 HOH A O   1 
HETATM 5510 O  O   . HOH W 6 .   ? 21.24800  -2.46500  54.68800 1.000 46.47000 ? 640 HOH A O   1 
HETATM 5511 O  O   . HOH W 6 .   ? 1.16100   13.66300  20.54600 1.000 28.48000 ? 641 HOH A O   1 
HETATM 5512 O  O   . HOH W 6 .   ? 7.64000   -27.30200 29.17100 1.000 37.42000 ? 642 HOH A O   1 
HETATM 5513 O  O   . HOH W 6 .   ? 15.54800  20.90100  25.82900 1.000 32.17000 ? 643 HOH A O   1 
HETATM 5514 O  O   . HOH W 6 .   ? 11.65400  -13.93200 41.59300 1.000 27.97000 ? 644 HOH A O   1 
HETATM 5515 O  O   . HOH W 6 .   ? -10.33600 -24.72800 37.89700 1.000 36.30000 ? 645 HOH A O   1 
HETATM 5516 O  O   . HOH W 6 .   ? 10.10100  -13.87200 28.15100 1.000 19.54000 ? 646 HOH A O   1 
HETATM 5517 O  O   . HOH W 6 .   ? 13.04500  -23.34600 35.32300 1.000 34.23000 ? 647 HOH A O   1 
HETATM 5518 O  O   . HOH W 6 .   ? -3.65200  7.38700   37.62400 1.000 31.30000 ? 648 HOH A O   1 
HETATM 5519 O  O   . HOH W 6 .   ? 25.62000  11.89400  25.76400 1.000 21.69000 ? 649 HOH A O   1 
HETATM 5520 O  O   . HOH W 6 .   ? -15.73400 -14.36900 33.42600 1.000 33.96000 ? 650 HOH A O   1 
HETATM 5521 O  O   . HOH W 6 .   ? 17.77100  1.56700   20.87800 1.000 15.85000 ? 651 HOH A O   1 
HETATM 5522 O  O   . HOH W 6 .   ? 5.04300   -34.24900 38.67200 1.000 42.18000 ? 652 HOH A O   1 
HETATM 5523 O  O   . HOH W 6 .   ? 3.67400   -1.49900  56.31400 1.000 47.87000 ? 653 HOH A O   1 
HETATM 5524 O  O   . HOH W 6 .   ? 9.41900   -5.75400  43.61700 1.000 27.56000 ? 654 HOH A O   1 
HETATM 5525 O  O   . HOH W 6 .   ? 18.84700  -6.33700  31.56800 1.000 37.34000 ? 655 HOH A O   1 
HETATM 5526 O  O   . HOH W 6 .   ? 17.71600  -13.97700 45.65700 1.000 34.52000 ? 656 HOH A O   1 
HETATM 5527 O  O   . HOH W 6 .   ? -20.65900 6.25700   21.46500 1.000 29.22000 ? 657 HOH A O   1 
HETATM 5528 O  O   . HOH W 6 .   ? -1.18200  -10.51200 15.74000 1.000 24.69000 ? 658 HOH A O   1 
HETATM 5529 O  O   . HOH W 6 .   ? 5.27400   0.76100   44.36700 1.000 25.63000 ? 659 HOH A O   1 
HETATM 5530 O  O   . HOH W 6 .   ? -9.60300  -20.52700 43.33000 1.000 32.73000 ? 660 HOH A O   1 
HETATM 5531 O  O   . HOH W 6 .   ? -10.19500 -27.27000 32.69800 1.000 41.79000 ? 661 HOH A O   1 
HETATM 5532 O  O   . HOH W 6 .   ? 6.50600   9.44400   37.36600 1.000 36.06000 ? 662 HOH A O   1 
HETATM 5533 O  O   . HOH W 6 .   ? 3.74200   -12.37800 13.67400 1.000 25.99000 ? 663 HOH A O   1 
HETATM 5534 O  O   . HOH W 6 .   ? 3.56400   -4.60200  36.36400 1.000 20.37000 ? 664 HOH A O   1 
HETATM 5535 O  O   . HOH W 6 .   ? 14.77600  15.48300  22.55100 1.000 20.16000 ? 665 HOH A O   1 
HETATM 5536 O  O   . HOH W 6 .   ? 13.41200  -0.67400  13.47800 1.000 38.16000 ? 666 HOH A O   1 
HETATM 5537 O  O   . HOH W 6 .   ? 17.59000  -18.69900 29.81500 1.000 23.12000 ? 667 HOH A O   1 
HETATM 5538 O  O   . HOH W 6 .   ? 21.02000  22.18900  28.65000 1.000 22.73000 ? 668 HOH A O   1 
HETATM 5539 O  O   . HOH W 6 .   ? 16.60900  -2.92900  31.04100 1.000 31.20000 ? 669 HOH A O   1 
HETATM 5540 O  O   . HOH W 6 .   ? 11.07700  -7.61200  27.26100 1.000 19.99000 ? 670 HOH A O   1 
HETATM 5541 O  O   . HOH W 6 .   ? 11.60700  9.92900   35.07300 1.000 32.67000 ? 671 HOH A O   1 
HETATM 5542 O  O   . HOH W 6 .   ? -10.26600 9.40900   19.94300 1.000 36.67000 ? 672 HOH A O   1 
HETATM 5543 O  O   . HOH W 6 .   ? -7.58600  1.29200   42.47500 1.000 38.99000 ? 673 HOH A O   1 
HETATM 5544 O  O   . HOH W 6 .   ? -8.42600  0.60400   33.38700 1.000 29.04000 ? 674 HOH A O   1 
HETATM 5545 O  O   . HOH W 6 .   ? 1.98000   11.43500  35.78400 1.000 38.54000 ? 675 HOH A O   1 
HETATM 5546 O  O   . HOH W 6 .   ? 19.51400  3.54000   19.84100 1.000 15.53000 ? 676 HOH A O   1 
HETATM 5547 O  O   . HOH W 6 .   ? -6.25200  -4.95900  46.61400 1.000 40.97000 ? 677 HOH A O   1 
HETATM 5548 O  O   . HOH W 6 .   ? 17.26600  -4.52700  48.62200 1.000 31.02000 ? 678 HOH A O   1 
HETATM 5549 O  O   . HOH W 6 .   ? 12.26000  1.53600   15.20100 1.000 22.43000 ? 679 HOH A O   1 
HETATM 5550 O  O   . HOH W 6 .   ? -7.30600  -15.08400 16.70800 1.000 37.61000 ? 680 HOH A O   1 
HETATM 5551 O  O   . HOH W 6 .   ? 6.70600   3.31800   11.46000 1.000 33.44000 ? 681 HOH A O   1 
HETATM 5552 O  O   . HOH W 6 .   ? -2.77300  -7.70400  51.20000 1.000 33.97000 ? 682 HOH A O   1 
HETATM 5553 O  O   . HOH W 6 .   ? 12.61100  -10.71700 14.97700 1.000 31.13000 ? 683 HOH A O   1 
HETATM 5554 O  O   . HOH W 6 .   ? -11.59500 1.25400   26.09300 1.000 25.68000 ? 684 HOH A O   1 
HETATM 5555 O  O   . HOH W 6 .   ? 8.040     16.030    23.779   1.000 36.29000 ? 685 HOH A O   1 
HETATM 5556 O  O   . HOH W 6 .   ? -4.71200  -24.44500 29.93600 1.000 32.33000 ? 686 HOH A O   1 
HETATM 5557 O  O   . HOH W 6 .   ? 3.16000   -10.81300 55.74000 1.000 40.84000 ? 687 HOH A O   1 
HETATM 5558 O  O   . HOH W 6 .   ? 19.75800  14.62600  28.84200 1.000 30.72000 ? 688 HOH A O   1 
HETATM 5559 O  O   . HOH W 6 .   ? -13.52900 -7.55200  20.27300 1.000 27.02000 ? 689 HOH A O   1 
HETATM 5560 O  O   . HOH W 6 .   ? -10.87100 -13.33600 23.57200 1.000 33.93000 ? 690 HOH A O   1 
HETATM 5561 O  O   . HOH W 6 .   ? 16.90500  -14.32500 50.60800 1.000 34.81000 ? 691 HOH A O   1 
HETATM 5562 O  O   . HOH W 6 .   ? 9.11500   12.87900  35.30500 1.000 36.10000 ? 692 HOH A O   1 
HETATM 5563 O  O   . HOH W 6 .   ? -14.20500 -19.94200 32.77500 1.000 36.29000 ? 693 HOH A O   1 
HETATM 5564 O  O   . HOH W 6 .   ? 18.25800  11.70400  28.70400 1.000 38.77000 ? 694 HOH A O   1 
HETATM 5565 O  O   . HOH W 6 .   ? 3.68900   -8.04100  54.93900 1.000 34.16000 ? 695 HOH A O   1 
HETATM 5566 O  O   . HOH W 6 .   ? -3.433    14.931    28.090   1.000 40.01000 ? 696 HOH A O   1 
HETATM 5567 O  O   . HOH W 6 .   ? 6.45800   -33.27600 45.23300 1.000 41.59000 ? 697 HOH A O   1 
HETATM 5568 O  O   . HOH W 6 .   ? 12.40300  8.20300   14.53000 1.000 25.20000 ? 698 HOH A O   1 
HETATM 5569 O  O   . HOH W 6 .   ? -10.60600 3.27800   24.78400 1.000 29.13000 ? 699 HOH A O   1 
HETATM 5570 O  O   . HOH W 6 .   ? -1.10200  -12.40400 55.25300 1.000 40.50000 ? 700 HOH A O   1 
HETATM 5571 O  O   . HOH W 6 .   ? -12.28600 13.46300  30.77600 1.000 48.35000 ? 701 HOH A O   1 
HETATM 5572 O  O   . HOH W 6 .   ? 3.22200   -11.82900 41.57700 1.000 24.13000 ? 702 HOH A O   1 
HETATM 5573 O  O   . HOH W 6 .   ? 16.65000  7.47500   30.07200 1.000 39.40000 ? 703 HOH A O   1 
HETATM 5574 O  O   . HOH W 6 .   ? -1.86000  -8.32000  10.08700 1.000 35.14000 ? 704 HOH A O   1 
HETATM 5575 O  O   . HOH W 6 .   ? 11.86400  4.79300   51.74700 1.000 42.09000 ? 705 HOH A O   1 
HETATM 5576 O  O   . HOH W 6 .   ? 4.61000   14.86000  22.97000 1.000 22.00000 ? 706 HOH A O   1 
HETATM 5577 O  O   . HOH W 6 .   ? 8.71100   7.86600   31.77800 1.000 19.29000 ? 707 HOH A O   1 
HETATM 5578 O  O   . HOH W 6 .   ? 9.74200   -24.27600 21.35100 1.000 37.39000 ? 708 HOH A O   1 
HETATM 5579 O  O   . HOH W 6 .   ? -9.18500  7.13600   18.36500 1.000 25.82000 ? 709 HOH A O   1 
HETATM 5580 O  O   . HOH W 6 .   ? -8.67400  0.79000   37.50200 1.000 36.56000 ? 710 HOH A O   1 
HETATM 5581 O  O   . HOH W 6 .   ? 3.77800   -24.32500 22.89800 1.000 26.04000 ? 711 HOH A O   1 
HETATM 5582 O  O   . HOH W 6 .   ? 7.04400   -14.73500 31.85000 1.000 31.84000 ? 712 HOH A O   1 
HETATM 5583 O  O   . HOH W 6 .   ? 6.18000   -23.49100 22.64100 1.000 25.82000 ? 713 HOH A O   1 
HETATM 5584 O  O   . HOH W 6 .   ? 10.75700  -9.82600  12.55700 1.000 30.57000 ? 714 HOH A O   1 
HETATM 5585 O  O   . HOH W 6 .   ? 17.72200  8.42800   27.72200 1.000 20.48000 ? 715 HOH A O   1 
HETATM 5586 O  O   . HOH W 6 .   ? 8.81100   -26.66200 45.45800 1.000 41.79000 ? 716 HOH A O   1 
HETATM 5587 O  O   . HOH W 6 .   ? 15.11000  -5.50000  40.86400 1.000 38.49000 ? 717 HOH A O   1 
HETATM 5588 O  O   . HOH W 6 .   ? 6.25900   -20.47200 32.58800 1.000 30.55000 ? 718 HOH A O   1 
HETATM 5589 O  O   . HOH W 6 .   ? 25.50200  12.91100  23.22300 1.000 16.87000 ? 719 HOH A O   1 
HETATM 5590 O  O   . HOH W 6 .   ? 15.77500  -15.44800 47.93500 1.000 34.89000 ? 720 HOH A O   1 
HETATM 5591 O  O   . HOH W 6 .   ? 18.55300  -11.32100 43.63400 1.000 35.66000 ? 721 HOH A O   1 
HETATM 5592 O  O   . HOH W 6 .   ? 13.84600  -4.15100  33.44700 1.000 28.69000 ? 722 HOH A O   1 
HETATM 5593 O  O   . HOH W 6 .   ? 18.91600  16.85500  30.13600 1.000 25.64000 ? 723 HOH A O   1 
HETATM 5594 O  O   . HOH W 6 .   ? 1.06900   5.23100   7.31800  1.000 39.00000 ? 724 HOH A O   1 
HETATM 5595 O  O   . HOH W 6 .   ? 14.91400  3.85600   32.81200 1.000 26.69000 ? 725 HOH A O   1 
HETATM 5596 O  O   . HOH W 6 .   ? 6.78200   3.37600   42.03400 1.000 38.32000 ? 726 HOH A O   1 
HETATM 5597 O  O   . HOH W 6 .   ? 16.26400  10.36300  33.91900 1.000 42.65000 ? 727 HOH A O   1 
HETATM 5598 O  O   . HOH W 6 .   ? 0.00900   12.45300  29.23000 1.000 33.71000 ? 728 HOH A O   1 
HETATM 5599 O  O   . HOH W 6 .   ? 19.76400  1.44100   15.61700 1.000 37.97000 ? 729 HOH A O   1 
HETATM 5600 O  O   . HOH W 6 .   ? -11.01500 6.00000   25.14500 1.000 32.02000 ? 730 HOH A O   1 
HETATM 5601 O  O   . HOH W 6 .   ? 0.38200   -32.67000 44.69300 1.000 36.05000 ? 731 HOH A O   1 
HETATM 5602 O  O   . HOH W 6 .   ? -0.37300  5.27400   42.77300 1.000 38.29000 ? 732 HOH A O   1 
HETATM 5603 O  O   . HOH W 6 .   ? -5.77000  -17.05000 53.55200 1.000 39.35000 ? 733 HOH A O   1 
HETATM 5604 O  O   . HOH W 6 .   ? 3.49800   -28.11000 26.03500 1.000 29.88000 ? 734 HOH A O   1 
HETATM 5605 O  O   . HOH W 6 .   ? -3.64700  2.15500   47.83700 1.000 41.71000 ? 735 HOH A O   1 
HETATM 5606 O  O   . HOH W 6 .   ? 12.27000  -11.99200 39.31900 1.000 29.61000 ? 736 HOH A O   1 
HETATM 5607 O  O   . HOH W 6 .   ? 23.17100  16.78500  18.60700 1.000 25.78000 ? 737 HOH A O   1 
HETATM 5608 O  O   . HOH W 6 .   ? -19.29000 -5.03700  25.45500 1.000 43.92000 ? 738 HOH A O   1 
HETATM 5609 O  O   . HOH W 6 .   ? 13.80300  -17.26100 50.50200 1.000 38.45000 ? 739 HOH A O   1 
HETATM 5610 O  O   . HOH W 6 .   ? 18.87600  -0.43700  17.27800 1.000 28.16000 ? 740 HOH A O   1 
HETATM 5611 O  O   . HOH W 6 .   ? -4.84100  1.48600   9.76600  1.000 43.03000 ? 741 HOH A O   1 
HETATM 5612 O  O   . HOH W 6 .   ? 11.82800  -20.91800 49.24700 1.000 34.43000 ? 742 HOH A O   1 
HETATM 5613 O  O   . HOH W 6 .   ? 5.02100   -0.68700  36.16300 1.000 23.06000 ? 743 HOH A O   1 
HETATM 5614 O  O   . HOH W 6 .   ? 5.75100   -30.86300 30.61700 1.000 38.93000 ? 744 HOH A O   1 
HETATM 5615 O  O   . HOH W 6 .   ? 7.64000   -16.79600 33.55200 1.000 26.64000 ? 745 HOH A O   1 
HETATM 5616 O  O   . HOH W 6 .   ? 6.69700   2.53300   37.31800 1.000 26.64000 ? 746 HOH A O   1 
HETATM 5617 O  O   . HOH W 6 .   ? 18.28100  -4.24800  51.37000 1.000 37.46000 ? 747 HOH A O   1 
HETATM 5618 O  O   . HOH W 6 .   ? 6.62400   -10.49800 22.50800 1.000 25.99000 ? 748 HOH A O   1 
HETATM 5619 O  O   . HOH W 6 .   ? -4.21900  -25.59400 32.00600 1.000 25.95000 ? 749 HOH A O   1 
HETATM 5620 O  O   . HOH W 6 .   ? 13.35600  -22.33400 22.57600 1.000 32.87000 ? 750 HOH A O   1 
HETATM 5621 O  O   . HOH W 6 .   ? 15.89000  -8.35800  33.64000 1.000 36.04000 ? 751 HOH A O   1 
HETATM 5622 O  O   . HOH W 6 .   ? 15.83100  1.16900   32.47500 1.000 23.61000 ? 752 HOH A O   1 
HETATM 5623 O  O   . HOH W 6 .   ? -13.10300 -16.16900 47.57000 1.000 46.72000 ? 753 HOH A O   1 
HETATM 5624 O  O   . HOH W 6 .   ? -2.280    10.496    15.323   1.000 34.65000 ? 754 HOH A O   1 
HETATM 5625 O  O   . HOH W 6 .   ? -13.07800 6.44600   23.73100 1.000 36.78000 ? 755 HOH A O   1 
HETATM 5626 O  O   . HOH W 6 .   ? -12.45800 -26.83200 39.13500 1.000 43.50000 ? 756 HOH A O   1 
HETATM 5627 O  O   . HOH W 6 .   ? -9.73100  -8.92900  48.42700 1.000 43.56000 ? 757 HOH A O   1 
HETATM 5628 O  O   . HOH W 6 .   ? 11.39500  7.29700   44.77200 1.000 42.71000 ? 758 HOH A O   1 
HETATM 5629 O  O   . HOH W 6 .   ? -2.22300  -15.48800 12.30000 1.000 42.94000 ? 759 HOH A O   1 
HETATM 5630 O  O   . HOH W 6 .   ? 8.03100   -16.97300 15.49500 1.000 35.23000 ? 760 HOH A O   1 
HETATM 5631 O  O   . HOH W 6 .   ? -0.49200  -17.65100 12.66500 1.000 42.32000 ? 761 HOH A O   1 
HETATM 5632 O  O   . HOH W 6 .   ? -0.63000  -24.30200 19.70600 1.000 43.67000 ? 762 HOH A O   1 
HETATM 5633 O  O   . HOH W 6 .   ? 15.49600  -20.09300 20.66000 1.000 39.88000 ? 763 HOH A O   1 
HETATM 5634 O  O   . HOH W 6 .   ? 12.18900  3.40400   55.85700 1.000 42.45000 ? 764 HOH A O   1 
HETATM 5635 O  O   . HOH W 6 .   ? -4.37600  -21.25900 18.29100 1.000 36.99000 ? 765 HOH A O   1 
HETATM 5636 O  O   . HOH W 6 .   ? -10.09200 4.34500   39.34700 1.000 40.67000 ? 766 HOH A O   1 
HETATM 5637 O  O   . HOH W 6 .   ? 0.66900   -36.86300 38.86000 1.000 29.18000 ? 767 HOH A O   1 
HETATM 5638 O  O   . HOH W 6 .   ? 12.71600  -22.87900 30.21900 1.000 33.48000 ? 768 HOH A O   1 
HETATM 5639 O  O   . HOH W 6 .   ? -10.98300 -9.47400  45.57400 1.000 33.37000 ? 769 HOH A O   1 
HETATM 5640 O  O   . HOH W 6 .   ? 13.51700  -23.08100 32.74700 1.000 33.02000 ? 770 HOH A O   1 
HETATM 5641 O  O   . HOH W 6 .   ? -20.912   4.286     17.030   1.000 33.04000 ? 771 HOH A O   1 
HETATM 5642 O  O   . HOH W 6 .   ? 7.58500   3.86700   39.55800 1.000 36.58000 ? 772 HOH A O   1 
HETATM 5643 O  O   . HOH W 6 .   ? -13.20700 -10.85600 44.43600 1.000 33.37000 ? 773 HOH A O   1 
HETATM 5644 O  O   . HOH W 6 .   ? 9.15600   -10.62700 55.18800 1.000 41.34000 ? 774 HOH A O   1 
HETATM 5645 O  O   . HOH W 6 .   ? -8.51100  -32.40000 39.94000 1.000 36.11000 ? 775 HOH A O   1 
HETATM 5646 O  O   . HOH W 6 .   ? 16.61900  5.95400   32.45200 1.000 34.16000 ? 776 HOH A O   1 
HETATM 5647 O  O   . HOH W 6 .   ? 8.98600   -6.16700  55.03200 1.000 42.17000 ? 777 HOH A O   1 
HETATM 5648 O  O   . HOH W 6 .   ? -4.09000  -6.36100  49.48600 1.000 40.34000 ? 778 HOH A O   1 
HETATM 5649 O  O   . HOH W 6 .   ? 6.05100   -20.13000 55.68600 1.000 46.33000 ? 779 HOH A O   1 
HETATM 5650 O  O   . HOH W 6 .   ? -6.44300  -22.80700 19.90400 1.000 45.09000 ? 780 HOH A O   1 
HETATM 5651 O  O   . HOH W 6 .   ? 0.71900   -30.20500 23.76800 1.000 42.25000 ? 781 HOH A O   1 
HETATM 5652 O  O   . HOH W 6 .   ? 8.31200   -21.80600 55.28500 1.000 38.87000 ? 782 HOH A O   1 
HETATM 5653 O  O   . HOH W 6 .   ? 14.72400  -16.30600 16.56300 1.000 45.51000 ? 783 HOH A O   1 
HETATM 5654 O  O   . HOH W 6 .   ? 13.61900  4.77200   53.76200 1.000 38.06000 ? 784 HOH A O   1 
HETATM 5655 O  O   . HOH W 6 .   ? 20.64000  6.22800   16.20100 1.000 35.51000 ? 785 HOH A O   1 
HETATM 5656 O  O   . HOH W 6 .   ? -3.59900  -10.08100 52.38100 1.000 39.82000 ? 786 HOH A O   1 
HETATM 5657 O  O   . HOH W 6 .   ? -9.77700  -15.68700 22.71600 1.000 37.46000 ? 787 HOH A O   1 
HETATM 5658 O  O   . HOH W 6 .   ? 6.21500   -16.52400 13.48100 1.000 42.00000 ? 788 HOH A O   1 
HETATM 5659 O  O   . HOH W 6 .   ? -14.86700 -5.78900  13.62700 1.000 44.30000 ? 789 HOH A O   1 
HETATM 5660 O  O   . HOH W 6 .   ? -14.25000 1.59900   27.06200 1.000 30.22000 ? 790 HOH A O   1 
HETATM 5661 O  O   . HOH W 6 .   ? 11.63000  -18.41500 51.28100 1.000 39.90000 ? 791 HOH A O   1 
HETATM 5662 O  O   . HOH W 6 .   ? -19.621   -21.682   24.458   1.000 44.40000 ? 792 HOH A O   1 
HETATM 5663 O  O   . HOH W 6 .   ? 13.37500  -8.54400  38.86400 1.000 37.11000 ? 793 HOH A O   1 
HETATM 5664 O  O   . HOH W 6 .   ? -14.79200 -0.10100  28.87900 1.000 35.41000 ? 794 HOH A O   1 
HETATM 5665 O  O   . HOH W 6 .   ? 19.68800  12.95900  32.89800 1.000 42.52000 ? 795 HOH A O   1 
HETATM 5666 O  O   . HOH W 6 .   ? -9.11700  1.37500   39.60800 1.000 41.39000 ? 796 HOH A O   1 
HETATM 5667 O  O   . HOH W 6 .   ? 14.87100  -10.45000 38.69600 1.000 34.94000 ? 797 HOH A O   1 
HETATM 5668 O  O   . HOH W 6 .   ? 18.32000  1.04900   31.25900 1.000 28.91000 ? 798 HOH A O   1 
HETATM 5669 O  O   . HOH W 6 .   ? -13.05000 9.06900   22.61600 1.000 39.19000 ? 799 HOH A O   1 
HETATM 5670 O  O   . HOH W 6 .   ? 20.31900  3.08900   31.40500 1.000 29.75000 ? 800 HOH A O   1 
HETATM 5671 O  O   . HOH W 6 .   ? 8.45300   8.66000   36.29900 1.000 41.72000 ? 801 HOH A O   1 
HETATM 5672 O  O   . HOH W 6 .   ? 3.89900   -27.26200 23.71400 1.000 31.86000 ? 802 HOH A O   1 
HETATM 5673 O  O   . HOH W 6 .   ? -11.51900 5.90800   27.80400 1.000 37.44000 ? 803 HOH A O   1 
HETATM 5674 O  O   . HOH W 6 .   ? -4.22400  3.36900   8.12900  1.000 40.70000 ? 804 HOH A O   1 
HETATM 5675 O  O   . HOH W 6 .   ? -14.54100 -8.53900  17.93700 1.000 33.56000 ? 805 HOH A O   1 
HETATM 5676 O  O   . HOH W 6 .   ? 16.16000  16.05600  19.85800 1.000 36.02000 ? 806 HOH A O   1 
HETATM 5677 O  O   . HOH W 6 .   ? 19.62500  4.87600   33.04400 1.000 40.10000 ? 807 HOH A O   1 
HETATM 5678 O  O   . HOH W 6 .   ? 9.43200   7.94400   34.11800 1.000 29.47000 ? 808 HOH A O   1 
HETATM 5679 O  O   . HOH W 6 .   ? 10.39200  5.28400   35.38300 1.000 33.16000 ? 809 HOH A O   1 
HETATM 5680 O  O   . HOH W 6 .   ? 5.84400   -13.07700 12.59400 1.000 29.23000 ? 810 HOH A O   1 
HETATM 5681 O  O   . HOH W 6 .   ? 20.42500  3.42000   17.17400 1.000 28.27000 ? 811 HOH A O   1 
HETATM 5682 O  O   . HOH W 6 .   ? 12.22500  -4.18600  35.74900 1.000 33.77000 ? 812 HOH A O   1 
HETATM 5683 O  O   . HOH X 6 .   ? 36.15300  23.60500  13.00000 1.000 34.80000 ? 501 HOH B O   1 
HETATM 5684 O  O   . HOH X 6 .   ? 51.53600  25.09000  43.23900 1.000 43.15000 ? 502 HOH B O   1 
HETATM 5685 O  O   . HOH X 6 .   ? 57.34000  -2.13600  18.82800 1.000 34.23000 ? 503 HOH B O   1 
HETATM 5686 O  O   . HOH X 6 .   ? 45.63500  -3.60800  39.74900 1.000 41.12000 ? 504 HOH B O   1 
HETATM 5687 O  O   . HOH X 6 .   ? 42.24200  -11.04200 29.96500 1.000 46.72000 ? 505 HOH B O   1 
HETATM 5688 O  O   . HOH X 6 .   ? 46.23200  27.71900  49.68700 1.000 42.47000 ? 506 HOH B O   1 
HETATM 5689 O  O   . HOH X 6 .   ? 40.00500  20.01900  11.71900 1.000 38.23000 ? 507 HOH B O   1 
HETATM 5690 O  O   . HOH X 6 .   ? 37.985    -9.909    21.863   1.000 25.33000 ? 508 HOH B O   1 
HETATM 5691 O  O   . HOH X 6 .   ? 32.49200  14.64700  37.00800 1.000 38.89000 ? 509 HOH B O   1 
HETATM 5692 O  O   . HOH X 6 .   ? 33.23600  4.21500   45.04300 1.000 26.21000 ? 510 HOH B O   1 
HETATM 5693 O  O   . HOH X 6 .   ? 26.22900  -13.00500 8.30000  1.000 55.24000 ? 511 HOH B O   1 
HETATM 5694 O  O   . HOH X 6 .   ? 45.71600  3.98100   43.72500 1.000 42.53000 ? 512 HOH B O   1 
HETATM 5695 O  O   . HOH X 6 .   ? 21.89400  6.93300   30.77200 1.000 26.39000 ? 513 HOH B O   1 
HETATM 5696 O  O   . HOH X 6 .   ? 24.65600  15.02300  19.93700 1.000 25.44000 ? 514 HOH B O   1 
HETATM 5697 O  O   . HOH X 6 .   ? 30.37100  9.41400   52.09700 1.000 32.47000 ? 515 HOH B O   1 
HETATM 5698 O  O   . HOH X 6 .   ? 44.08400  19.19000  49.51500 1.000 38.92000 ? 516 HOH B O   1 
HETATM 5699 O  O   . HOH X 6 .   ? 56.32000  4.21000   19.69000 1.000 28.93000 ? 517 HOH B O   1 
HETATM 5700 O  O   . HOH X 6 .   ? 26.04500  13.97200  45.94500 1.000 33.72000 ? 518 HOH B O   1 
HETATM 5701 O  O   . HOH X 6 .   ? 36.58800  -7.17000  37.72600 1.000 36.14000 ? 519 HOH B O   1 
HETATM 5702 O  O   . HOH X 6 .   ? 39.00400  18.08400  54.78000 1.000 36.97000 ? 520 HOH B O   1 
HETATM 5703 O  O   . HOH X 6 .   ? 33.23200  -3.06100  40.74900 1.000 32.93000 ? 521 HOH B O   1 
HETATM 5704 O  O   . HOH X 6 .   ? 24.00500  19.13000  17.83600 1.000 31.84000 ? 522 HOH B O   1 
HETATM 5705 O  O   . HOH X 6 .   ? 28.82600  17.41800  27.52800 1.000 17.07000 ? 523 HOH B O   1 
HETATM 5706 O  O   . HOH X 6 .   ? 43.58300  27.69000  29.08800 1.000 25.80000 ? 524 HOH B O   1 
HETATM 5707 O  O   . HOH X 6 .   ? 29.82300  -4.06900  11.76100 1.000 28.56000 ? 525 HOH B O   1 
HETATM 5708 O  O   . HOH X 6 .   ? 31.53500  37.49000  39.38400 1.000 44.03000 ? 526 HOH B O   1 
HETATM 5709 O  O   . HOH X 6 .   ? 49.99600  26.90600  29.43200 1.000 34.44000 ? 527 HOH B O   1 
HETATM 5710 O  O   . HOH X 6 .   ? 26.342    1.900     8.107    1.000 32.25000 ? 528 HOH B O   1 
HETATM 5711 O  O   . HOH X 6 .   ? 33.52200  1.61100   -0.78100 1.000 34.42000 ? 529 HOH B O   1 
HETATM 5712 O  O   . HOH X 6 .   ? 47.38000  3.81400   38.21700 1.000 34.05000 ? 530 HOH B O   1 
HETATM 5713 O  O   . HOH X 6 .   ? 49.88400  -5.65700  24.34800 1.000 37.23000 ? 531 HOH B O   1 
HETATM 5714 O  O   . HOH X 6 .   ? 54.24000  9.61800   22.33400 1.000 23.11000 ? 532 HOH B O   1 
HETATM 5715 O  O   . HOH X 6 .   ? 13.31600  -8.33900  26.18600 1.000 20.41000 ? 533 HOH B O   1 
HETATM 5716 O  O   . HOH X 6 .   ? 45.91000  33.37000  29.84400 1.000 21.75000 ? 534 HOH B O   1 
HETATM 5717 O  O   . HOH X 6 .   ? 27.85500  11.09000  27.07300 1.000 18.76000 ? 535 HOH B O   1 
HETATM 5718 O  O   . HOH X 6 .   ? 50.27900  8.73700   17.60400 1.000 27.50000 ? 536 HOH B O   1 
HETATM 5719 O  O   . HOH X 6 .   ? 31.91000  18.62600  31.10100 1.000 31.93000 ? 537 HOH B O   1 
HETATM 5720 O  O   . HOH X 6 .   ? 57.40400  2.34000   24.02500 1.000 33.88000 ? 538 HOH B O   1 
HETATM 5721 O  O   . HOH X 6 .   ? 54.11500  1.22100   13.93200 1.000 38.44000 ? 539 HOH B O   1 
HETATM 5722 O  O   . HOH X 6 .   ? 34.25000  41.04800  38.99100 1.000 42.92000 ? 540 HOH B O   1 
HETATM 5723 O  O   . HOH X 6 .   ? 33.766    36.831    30.044   1.000 28.09000 ? 541 HOH B O   1 
HETATM 5724 O  O   . HOH X 6 .   ? 44.95500  14.87800  12.25800 1.000 40.30000 ? 542 HOH B O   1 
HETATM 5725 O  O   . HOH X 6 .   ? 20.35700  9.30300   51.22200 1.000 37.62000 ? 543 HOH B O   1 
HETATM 5726 O  O   . HOH X 6 .   ? 48.21300  -3.82900  19.62500 1.000 25.77000 ? 544 HOH B O   1 
HETATM 5727 O  O   . HOH X 6 .   ? 26.52200  18.44500  41.06100 1.000 32.12000 ? 545 HOH B O   1 
HETATM 5728 O  O   . HOH X 6 .   ? 50.11100  7.84900   13.23000 1.000 36.00000 ? 546 HOH B O   1 
HETATM 5729 O  O   . HOH X 6 .   ? 52.52400  24.18800  32.63400 1.000 33.96000 ? 547 HOH B O   1 
HETATM 5730 O  O   . HOH X 6 .   ? 30.04200  15.63200  13.71900 1.000 31.95000 ? 548 HOH B O   1 
HETATM 5731 O  O   . HOH X 6 .   ? 53.45400  4.13800   19.16100 1.000 22.32000 ? 549 HOH B O   1 
HETATM 5732 O  O   . HOH X 6 .   ? 30.21700  3.81200   37.33200 1.000 31.61000 ? 550 HOH B O   1 
HETATM 5733 O  O   . HOH X 6 .   ? 24.30800  -12.06500 23.61900 1.000 19.67000 ? 551 HOH B O   1 
HETATM 5734 O  O   . HOH X 6 .   ? 43.60800  22.81000  53.04900 1.000 36.77000 ? 552 HOH B O   1 
HETATM 5735 O  O   . HOH X 6 .   ? 35.49900  15.13500  13.57500 1.000 23.23000 ? 553 HOH B O   1 
HETATM 5736 O  O   . HOH X 6 .   ? 19.45300  1.75700   27.52900 1.000 24.11000 ? 554 HOH B O   1 
HETATM 5737 O  O   . HOH X 6 .   ? 28.71400  27.01400  19.77800 1.000 32.15000 ? 555 HOH B O   1 
HETATM 5738 O  O   . HOH X 6 .   ? 29.06200  10.36100  43.60500 1.000 22.20000 ? 556 HOH B O   1 
HETATM 5739 O  O   . HOH X 6 .   ? 32.58400  -0.76500  11.89900 1.000 24.48000 ? 557 HOH B O   1 
HETATM 5740 O  O   . HOH X 6 .   ? 21.34500  1.71100   21.01400 1.000 12.75000 ? 558 HOH B O   1 
HETATM 5741 O  O   . HOH X 6 .   ? 47.17300  18.75400  50.17100 1.000 37.92000 ? 559 HOH B O   1 
HETATM 5742 O  O   . HOH X 6 .   ? 55.47800  5.62500   26.53100 1.000 23.70000 ? 560 HOH B O   1 
HETATM 5743 O  O   . HOH X 6 .   ? 50.59800  2.55700   27.26800 1.000 21.07000 ? 561 HOH B O   1 
HETATM 5744 O  O   . HOH X 6 .   ? 21.22400  -4.82900  27.95000 1.000 21.47000 ? 562 HOH B O   1 
HETATM 5745 O  O   . HOH X 6 .   ? 34.50900  -11.26600 24.67100 1.000 22.10000 ? 563 HOH B O   1 
HETATM 5746 O  O   . HOH X 6 .   ? 52.73400  7.08600   33.21200 1.000 27.60000 ? 564 HOH B O   1 
HETATM 5747 O  O   . HOH X 6 .   ? 22.57500  20.12000  47.02400 1.000 36.02000 ? 565 HOH B O   1 
HETATM 5748 O  O   . HOH X 6 .   ? 40.49900  4.79600   8.87700  1.000 40.06000 ? 566 HOH B O   1 
HETATM 5749 O  O   . HOH X 6 .   ? 19.52800  -0.32100  19.98600 1.000 13.61000 ? 567 HOH B O   1 
HETATM 5750 O  O   . HOH X 6 .   ? 26.13900  16.34900  38.80400 1.000 35.40000 ? 568 HOH B O   1 
HETATM 5751 O  O   . HOH X 6 .   ? 19.79300  3.98400   28.98900 1.000 31.89000 ? 569 HOH B O   1 
HETATM 5752 O  O   . HOH X 6 .   ? 32.49400  27.14600  29.65500 1.000 33.77000 ? 570 HOH B O   1 
HETATM 5753 O  O   . HOH X 6 .   ? 18.86200  -10.86500 29.81600 1.000 26.02000 ? 571 HOH B O   1 
HETATM 5754 O  O   . HOH X 6 .   ? 40.30500  13.58100  15.85000 1.000 22.34000 ? 572 HOH B O   1 
HETATM 5755 O  O   . HOH X 6 .   ? 16.45900  -22.00000 29.21400 1.000 41.97000 ? 573 HOH B O   1 
HETATM 5756 O  O   . HOH X 6 .   ? 49.56500  0.21200   25.58900 1.000 24.00000 ? 574 HOH B O   1 
HETATM 5757 O  O   . HOH X 6 .   ? 33.22300  5.29100   7.94300  1.000 42.09000 ? 575 HOH B O   1 
HETATM 5758 O  O   . HOH X 6 .   ? 25.73200  27.18600  34.12100 1.000 28.65000 ? 576 HOH B O   1 
HETATM 5759 O  O   . HOH X 6 .   ? 27.74900  21.61400  50.91400 1.000 32.23000 ? 577 HOH B O   1 
HETATM 5760 O  O   . HOH X 6 .   ? 48.67800  30.96800  31.50000 1.000 36.90000 ? 578 HOH B O   1 
HETATM 5761 O  O   . HOH X 6 .   ? 27.58000  -16.71600 34.88500 1.000 37.47000 ? 579 HOH B O   1 
HETATM 5762 O  O   . HOH X 6 .   ? 35.23000  16.39100  41.49900 1.000 25.06000 ? 580 HOH B O   1 
HETATM 5763 O  O   . HOH X 6 .   ? 30.991    -12.388   25.369   1.000 30.69000 ? 581 HOH B O   1 
HETATM 5764 O  O   . HOH X 6 .   ? 30.93800  20.86100  32.83600 1.000 29.58000 ? 582 HOH B O   1 
HETATM 5765 O  O   . HOH X 6 .   ? 23.45600  -17.88200 26.48100 1.000 32.55000 ? 583 HOH B O   1 
HETATM 5766 O  O   . HOH X 6 .   ? 35.05200  8.84200   36.68300 1.000 25.24000 ? 584 HOH B O   1 
HETATM 5767 O  O   . HOH X 6 .   ? 24.88900  8.20600   33.30100 1.000 26.38000 ? 585 HOH B O   1 
HETATM 5768 O  O   . HOH X 6 .   ? 27.05400  -5.67200  35.86000 1.000 32.59000 ? 586 HOH B O   1 
HETATM 5769 O  O   . HOH X 6 .   ? 29.95700  -4.01000  32.54900 1.000 17.82000 ? 587 HOH B O   1 
HETATM 5770 O  O   . HOH X 6 .   ? 50.58800  19.74900  42.13400 1.000 37.03000 ? 588 HOH B O   1 
HETATM 5771 O  O   . HOH X 6 .   ? 47.21900  3.47300   34.38100 1.000 26.85000 ? 589 HOH B O   1 
HETATM 5772 O  O   . HOH X 6 .   ? 54.48200  18.49400  33.78500 1.000 31.80000 ? 590 HOH B O   1 
HETATM 5773 O  O   . HOH X 6 .   ? 32.90500  34.26500  28.83700 1.000 33.96000 ? 591 HOH B O   1 
HETATM 5774 O  O   . HOH X 6 .   ? 52.55600  10.91100  20.66600 1.000 22.48000 ? 592 HOH B O   1 
HETATM 5775 O  O   . HOH X 6 .   ? 31.18000  -1.54200  5.75700  1.000 45.87000 ? 593 HOH B O   1 
HETATM 5776 O  O   . HOH X 6 .   ? 26.70200  13.70100  14.48700 1.000 27.08000 ? 594 HOH B O   1 
HETATM 5777 O  O   . HOH X 6 .   ? 49.79900  -2.61800  26.59900 1.000 35.69000 ? 595 HOH B O   1 
HETATM 5778 O  O   . HOH X 6 .   ? 24.23200  -11.90600 8.43600  1.000 50.79000 ? 596 HOH B O   1 
HETATM 5779 O  O   . HOH X 6 .   ? 52.81500  7.10600   12.40000 1.000 41.70000 ? 597 HOH B O   1 
HETATM 5780 O  O   . HOH X 6 .   ? 19.07500  -0.15700  29.25100 1.000 30.42000 ? 598 HOH B O   1 
HETATM 5781 O  O   . HOH X 6 .   ? 38.66800  -8.64600  30.85500 1.000 35.77000 ? 599 HOH B O   1 
HETATM 5782 O  O   . HOH X 6 .   ? 42.652    -11.036   26.944   1.000 39.02000 ? 600 HOH B O   1 
HETATM 5783 O  O   . HOH X 6 .   ? 32.06600  25.83700  54.34300 1.000 45.25000 ? 601 HOH B O   1 
HETATM 5784 O  O   . HOH X 6 .   ? 13.55800  -9.56300  23.65500 1.000 14.57000 ? 602 HOH B O   1 
HETATM 5785 O  O   . HOH X 6 .   ? 49.27800  -5.66700  21.21800 1.000 33.57000 ? 603 HOH B O   1 
HETATM 5786 O  O   . HOH X 6 .   ? 59.369    -5.202    22.729   1.000 43.25000 ? 604 HOH B O   1 
HETATM 5787 O  O   . HOH X 6 .   ? 55.51300  21.01100  23.96000 1.000 42.27000 ? 605 HOH B O   1 
HETATM 5788 O  O   . HOH X 6 .   ? 38.60200  14.09900  12.29500 1.000 37.23000 ? 606 HOH B O   1 
HETATM 5789 O  O   . HOH X 6 .   ? 32.17100  -6.90400  5.90900  1.000 54.99000 ? 607 HOH B O   1 
HETATM 5790 O  O   . HOH X 6 .   ? 32.51100  26.98600  21.63700 1.000 23.29000 ? 608 HOH B O   1 
HETATM 5791 O  O   . HOH X 6 .   ? 32.33400  24.41800  32.22700 1.000 29.42000 ? 609 HOH B O   1 
HETATM 5792 O  O   . HOH X 6 .   ? 42.12400  -3.12600  38.94900 1.000 28.24000 ? 610 HOH B O   1 
HETATM 5793 O  O   . HOH X 6 .   ? 40.86200  13.19600  51.76400 1.000 34.80000 ? 611 HOH B O   1 
HETATM 5794 O  O   . HOH X 6 .   ? 46.31900  17.92500  15.84300 1.000 33.43000 ? 612 HOH B O   1 
HETATM 5795 O  O   . HOH X 6 .   ? 24.93100  28.34000  48.44300 1.000 49.61000 ? 613 HOH B O   1 
HETATM 5796 O  O   . HOH X 6 .   ? 18.40400  -3.17900  16.65000 1.000 36.29000 ? 614 HOH B O   1 
HETATM 5797 O  O   . HOH X 6 .   ? 36.41900  7.49300   52.39600 1.000 34.91000 ? 615 HOH B O   1 
HETATM 5798 O  O   . HOH X 6 .   ? 34.95900  16.17400  55.42800 1.000 39.33000 ? 616 HOH B O   1 
HETATM 5799 O  O   . HOH X 6 .   ? 22.40800  10.21100  17.62000 1.000 27.34000 ? 617 HOH B O   1 
HETATM 5800 O  O   . HOH X 6 .   ? 35.22300  27.78500  21.93000 1.000 24.64000 ? 618 HOH B O   1 
HETATM 5801 O  O   . HOH X 6 .   ? 50.01900  30.40600  38.08800 1.000 38.09000 ? 619 HOH B O   1 
HETATM 5802 O  O   . HOH X 6 .   ? 21.31900  9.12000   48.59000 1.000 33.81000 ? 620 HOH B O   1 
HETATM 5803 O  O   . HOH X 6 .   ? 48.07700  24.86200  42.83200 1.000 30.96000 ? 621 HOH B O   1 
HETATM 5804 O  O   . HOH X 6 .   ? 43.63500  24.22900  17.82600 1.000 34.71000 ? 622 HOH B O   1 
HETATM 5805 O  O   . HOH X 6 .   ? 21.89200  1.40700   13.87400 1.000 30.74000 ? 623 HOH B O   1 
HETATM 5806 O  O   . HOH X 6 .   ? 34.22000  -8.10900  4.22200  1.000 59.29000 ? 624 HOH B O   1 
HETATM 5807 O  O   . HOH X 6 .   ? 28.02600  -11.87300 29.89100 1.000 29.33000 ? 625 HOH B O   1 
HETATM 5808 O  O   . HOH X 6 .   ? 50.16300  16.84300  23.59800 1.000 29.17000 ? 626 HOH B O   1 
HETATM 5809 O  O   . HOH X 6 .   ? 24.22900  22.15200  49.51500 1.000 38.95000 ? 627 HOH B O   1 
HETATM 5810 O  O   . HOH X 6 .   ? 39.50000  29.05200  15.82500 1.000 40.52000 ? 628 HOH B O   1 
HETATM 5811 O  O   . HOH X 6 .   ? 29.11700  -6.43700  13.38500 1.000 27.81000 ? 629 HOH B O   1 
HETATM 5812 O  O   . HOH X 6 .   ? 29.81700  31.41200  44.12800 1.000 43.47000 ? 630 HOH B O   1 
HETATM 5813 O  O   . HOH X 6 .   ? 37.16500  29.70900  16.87700 1.000 37.34000 ? 631 HOH B O   1 
HETATM 5814 O  O   . HOH X 6 .   ? 45.01200  -6.36700  17.54500 1.000 42.50000 ? 632 HOH B O   1 
HETATM 5815 O  O   . HOH X 6 .   ? 41.62200  10.71300  9.77700  1.000 33.84000 ? 633 HOH B O   1 
HETATM 5816 O  O   . HOH X 6 .   ? 32.40600  14.05900  22.18700 1.000 22.17000 ? 634 HOH B O   1 
HETATM 5817 O  O   . HOH X 6 .   ? 22.802    9.478     3.729    1.000 37.80000 ? 635 HOH B O   1 
HETATM 5818 O  O   . HOH X 6 .   ? 31.07000  20.01500  14.90300 1.000 31.12000 ? 636 HOH B O   1 
HETATM 5819 O  O   . HOH X 6 .   ? 27.81400  -14.58700 25.91500 1.000 32.85000 ? 637 HOH B O   1 
HETATM 5820 O  O   . HOH X 6 .   ? 33.43100  4.93800   36.76800 1.000 24.59000 ? 638 HOH B O   1 
HETATM 5821 O  O   . HOH X 6 .   ? 26.14300  25.73400  48.04600 1.000 34.75000 ? 639 HOH B O   1 
HETATM 5822 O  O   . HOH X 6 .   ? 57.00800  24.33600  30.30900 1.000 35.81000 ? 640 HOH B O   1 
HETATM 5823 O  O   . HOH X 6 .   ? 25.21600  26.62800  31.51300 1.000 30.85000 ? 641 HOH B O   1 
HETATM 5824 O  O   . HOH X 6 .   ? 36.64600  5.25800   50.75500 1.000 38.89000 ? 642 HOH B O   1 
HETATM 5825 O  O   . HOH X 6 .   ? 23.66700  -21.86900 35.79800 1.000 41.94000 ? 643 HOH B O   1 
HETATM 5826 O  O   . HOH X 6 .   ? 36.01400  26.08000  54.19300 1.000 41.68000 ? 644 HOH B O   1 
HETATM 5827 O  O   . HOH X 6 .   ? 51.87000  26.43600  25.79000 1.000 34.57000 ? 645 HOH B O   1 
HETATM 5828 O  O   . HOH X 6 .   ? 15.98100  -13.51600 19.37900 1.000 22.40000 ? 646 HOH B O   1 
HETATM 5829 O  O   . HOH X 6 .   ? 55.12300  16.78900  24.29500 1.000 41.07000 ? 647 HOH B O   1 
HETATM 5830 O  O   . HOH X 6 .   ? 42.92200  29.41900  31.24900 1.000 19.49000 ? 648 HOH B O   1 
HETATM 5831 O  O   . HOH X 6 .   ? 29.20200  -8.55600  36.47700 1.000 32.45000 ? 649 HOH B O   1 
HETATM 5832 O  O   . HOH X 6 .   ? 35.74500  3.69100   7.59400  1.000 39.87000 ? 650 HOH B O   1 
HETATM 5833 O  O   . HOH X 6 .   ? 33.54900  6.51300   52.55100 1.000 37.78000 ? 651 HOH B O   1 
HETATM 5834 O  O   . HOH X 6 .   ? 38.73100  -2.53400  8.08200  1.000 33.78000 ? 652 HOH B O   1 
HETATM 5835 O  O   . HOH X 6 .   ? 46.654    36.407    38.147   1.000 26.95000 ? 653 HOH B O   1 
HETATM 5836 O  O   . HOH X 6 .   ? 48.24900  -4.49700  37.61100 1.000 39.05000 ? 654 HOH B O   1 
HETATM 5837 O  O   . HOH X 6 .   ? 52.21300  -5.65200  22.32400 1.000 38.35000 ? 655 HOH B O   1 
HETATM 5838 O  O   . HOH X 6 .   ? 22.06200  27.01300  34.69700 1.000 38.09000 ? 656 HOH B O   1 
HETATM 5839 O  O   . HOH X 6 .   ? 50.41300  -1.93200  31.96400 1.000 35.06000 ? 657 HOH B O   1 
HETATM 5840 O  O   . HOH X 6 .   ? 22.65000  12.37900  33.10700 1.000 35.69000 ? 658 HOH B O   1 
HETATM 5841 O  O   . HOH X 6 .   ? 55.24600  13.00400  22.68300 1.000 33.66000 ? 659 HOH B O   1 
HETATM 5842 O  O   A HOH X 6 .   ? 59.860    -2.773    20.667   0.500 27.09000 ? 660 HOH B O   1 
HETATM 5843 O  O   B HOH X 6 .   ? 59.655    -2.699    22.596   0.500 26.33000 ? 660 HOH B O   1 
HETATM 5844 O  O   . HOH X 6 .   ? 23.68800  0.26500   33.13500 1.000 23.84000 ? 661 HOH B O   1 
HETATM 5845 O  O   . HOH X 6 .   ? 19.85800  -13.17800 30.82900 1.000 26.32000 ? 662 HOH B O   1 
HETATM 5846 O  O   . HOH X 6 .   ? 25.05400  -7.03300  14.74000 1.000 34.67000 ? 663 HOH B O   1 
HETATM 5847 O  O   . HOH X 6 .   ? 25.26000  8.91800   14.18600 1.000 32.85000 ? 664 HOH B O   1 
HETATM 5848 O  O   . HOH X 6 .   ? 29.83900  -13.79900 32.79500 1.000 40.16000 ? 665 HOH B O   1 
HETATM 5849 O  O   . HOH X 6 .   ? 41.18100  30.43200  20.47200 1.000 40.01000 ? 666 HOH B O   1 
HETATM 5850 O  O   . HOH X 6 .   ? 25.86200  25.96200  21.75100 1.000 27.00000 ? 667 HOH B O   1 
HETATM 5851 O  O   . HOH X 6 .   ? 31.84600  1.67900   37.99900 1.000 24.26000 ? 668 HOH B O   1 
HETATM 5852 O  O   . HOH X 6 .   ? 28.59800  12.71400  12.15800 1.000 32.95000 ? 669 HOH B O   1 
HETATM 5853 O  O   . HOH X 6 .   ? 33.63100  29.44900  14.58800 1.000 37.01000 ? 670 HOH B O   1 
HETATM 5854 O  O   . HOH X 6 .   ? 35.56000  31.90100  24.77800 1.000 36.54000 ? 671 HOH B O   1 
HETATM 5855 O  O   . HOH X 6 .   ? 37.343    1.990     -1.182   1.000 32.15000 ? 672 HOH B O   1 
HETATM 5856 O  O   . HOH X 6 .   ? 28.38200  0.64000   42.58300 1.000 42.77000 ? 673 HOH B O   1 
HETATM 5857 O  O   . HOH X 6 .   ? 26.90400  -14.63400 32.34200 1.000 40.25000 ? 674 HOH B O   1 
HETATM 5858 O  O   . HOH X 6 .   ? 19.70600  -8.59900  29.98700 1.000 37.46000 ? 675 HOH B O   1 
HETATM 5859 O  O   . HOH X 6 .   ? 23.17200  -11.08400 37.74300 1.000 38.90000 ? 676 HOH B O   1 
HETATM 5860 O  O   . HOH X 6 .   ? 36.08700  23.68200  53.97800 1.000 35.80000 ? 677 HOH B O   1 
HETATM 5861 O  O   . HOH X 6 .   ? 25.72800  26.52200  29.12400 1.000 38.40000 ? 678 HOH B O   1 
HETATM 5862 O  O   . HOH X 6 .   ? 38.94000  -0.81200  43.64100 1.000 44.28000 ? 679 HOH B O   1 
HETATM 5863 O  O   . HOH X 6 .   ? 58.22300  8.42200   27.11100 1.000 35.50000 ? 680 HOH B O   1 
HETATM 5864 O  O   . HOH X 6 .   ? 22.85300  2.78700   32.73300 1.000 21.22000 ? 681 HOH B O   1 
HETATM 5865 O  O   . HOH X 6 .   ? 52.04600  -2.88800  25.02900 1.000 32.36000 ? 682 HOH B O   1 
HETATM 5866 O  O   . HOH X 6 .   ? 49.26600  23.00400  41.20200 1.000 43.62000 ? 683 HOH B O   1 
HETATM 5867 O  O   . HOH X 6 .   ? 23.82100  27.73700  45.68500 1.000 46.52000 ? 684 HOH B O   1 
HETATM 5868 O  O   . HOH X 6 .   ? 18.01100  -19.75000 21.17500 1.000 38.86000 ? 685 HOH B O   1 
HETATM 5869 O  O   . HOH X 6 .   ? 45.73300  30.60600  23.68600 1.000 45.17000 ? 686 HOH B O   1 
HETATM 5870 O  O   . HOH X 6 .   ? 42.34100  11.42700  49.87900 1.000 38.22000 ? 687 HOH B O   1 
HETATM 5871 O  O   . HOH X 6 .   ? 22.01200  -2.17500  32.78500 1.000 31.28000 ? 688 HOH B O   1 
HETATM 5872 O  O   . HOH X 6 .   ? 23.15500  5.19300   16.13300 1.000 33.27000 ? 689 HOH B O   1 
HETATM 5873 O  O   . HOH X 6 .   ? 30.50400  7.59600   5.50000  1.000 38.37000 ? 690 HOH B O   1 
HETATM 5874 O  O   . HOH X 6 .   ? 48.81200  19.80500  22.73000 1.000 37.72000 ? 691 HOH B O   1 
HETATM 5875 O  O   . HOH X 6 .   ? 33.810    -1.495    6.563    1.000 49.43000 ? 692 HOH B O   1 
HETATM 5876 O  O   . HOH X 6 .   ? 23.87800  12.64400  17.67000 1.000 26.36000 ? 693 HOH B O   1 
HETATM 5877 O  O   . HOH X 6 .   ? 26.11600  8.62400   35.75900 1.000 42.60000 ? 694 HOH B O   1 
HETATM 5878 O  O   . HOH X 6 .   ? 52.95600  16.47200  23.03900 1.000 34.50000 ? 695 HOH B O   1 
HETATM 5879 O  O   . HOH X 6 .   ? 55.08900  -3.47200  17.36300 1.000 36.46000 ? 696 HOH B O   1 
HETATM 5880 O  O   . HOH X 6 .   ? 41.62500  25.21500  16.85600 1.000 38.35000 ? 697 HOH B O   1 
HETATM 5881 O  O   . HOH X 6 .   ? 40.77600  25.69200  14.48400 1.000 41.36000 ? 698 HOH B O   1 
HETATM 5882 O  O   . HOH X 6 .   ? 48.31500  17.64300  17.36900 1.000 40.73000 ? 699 HOH B O   1 
HETATM 5883 O  O   . HOH X 6 .   ? 38.40800  3.84800   10.07100 1.000 35.19000 ? 700 HOH B O   1 
HETATM 5884 O  O   . HOH X 6 .   ? 41.32700  -1.82800  41.91100 1.000 40.96000 ? 701 HOH B O   1 
HETATM 5885 O  O   . HOH X 6 .   ? 27.20100  26.49200  18.13500 1.000 43.00000 ? 702 HOH B O   1 
HETATM 5886 O  O   . HOH X 6 .   ? 56.01300  4.23800   28.57500 1.000 37.17000 ? 703 HOH B O   1 
HETATM 5887 O  O   . HOH X 6 .   ? 18.77200  -9.29800  33.68100 1.000 42.71000 ? 704 HOH B O   1 
HETATM 5888 O  O   . HOH X 6 .   ? 28.89300  21.45700  14.36900 1.000 41.13000 ? 705 HOH B O   1 
HETATM 5889 O  O   . HOH X 6 .   ? 34.60600  40.98500  42.04900 1.000 42.73000 ? 706 HOH B O   1 
HETATM 5890 O  O   . HOH X 6 .   ? 31.95700  -2.39600  9.84900  1.000 35.96000 ? 707 HOH B O   1 
HETATM 5891 O  O   . HOH X 6 .   ? 41.85000  15.38100  52.47600 1.000 32.48000 ? 708 HOH B O   1 
HETATM 5892 O  O   . HOH X 6 .   ? 51.522    33.621    38.181   1.000 33.58000 ? 709 HOH B O   1 
HETATM 5893 O  O   . HOH X 6 .   ? 17.22100  -11.89500 38.07600 1.000 36.88000 ? 710 HOH B O   1 
HETATM 5894 O  O   . HOH X 6 .   ? 39.16100  28.59900  20.20000 1.000 37.65000 ? 711 HOH B O   1 
HETATM 5895 O  O   . HOH X 6 .   ? 43.06100  8.49200   49.58900 1.000 46.84000 ? 712 HOH B O   1 
HETATM 5896 O  O   A HOH X 6 .   ? 30.49200  -4.86400  37.24300 0.500 22.90000 ? 713 HOH B O   1 
HETATM 5897 O  O   B HOH X 6 .   ? 31.81900  -4.99200  38.30100 0.500 23.87000 ? 713 HOH B O   1 
HETATM 5898 O  O   . HOH X 6 .   ? 46.887    -16.092   30.513   1.000 44.93000 ? 714 HOH B O   1 
HETATM 5899 O  O   . HOH X 6 .   ? 44.70700  25.02000  53.75000 1.000 42.13000 ? 715 HOH B O   1 
HETATM 5900 O  O   . HOH X 6 .   ? 35.986    0.153     6.207    1.000 47.16000 ? 716 HOH B O   1 
HETATM 5901 O  O   . HOH X 6 .   ? 47.38300  -4.96900  17.17100 1.000 35.97000 ? 717 HOH B O   1 
HETATM 5902 O  O   . HOH X 6 .   ? 35.49200  30.46500  22.48000 1.000 33.94000 ? 718 HOH B O   1 
HETATM 5903 O  O   . HOH X 6 .   ? 52.93000  1.81600   28.07500 1.000 28.96000 ? 719 HOH B O   1 
HETATM 5904 O  O   . HOH X 6 .   ? 50.583    35.218    39.812   1.000 33.69000 ? 720 HOH B O   1 
HETATM 5905 O  O   . HOH X 6 .   ? 29.31200  -4.16300  35.00700 1.000 26.74000 ? 721 HOH B O   1 
HETATM 5906 O  O   . HOH X 6 .   ? 47.56200  3.58500   42.19000 1.000 42.63000 ? 722 HOH B O   1 
HETATM 5907 O  O   . HOH X 6 .   ? 39.62400  7.39700   7.94500  1.000 40.07000 ? 723 HOH B O   1 
HETATM 5908 O  O   . HOH X 6 .   ? 49.99300  -2.54800  29.72400 1.000 45.12000 ? 724 HOH B O   1 
HETATM 5909 O  O   . HOH X 6 .   ? 48.311    36.873    39.944   1.000 31.61000 ? 725 HOH B O   1 
HETATM 5910 O  O   . HOH X 6 .   ? 33.28300  19.37900  13.17600 1.000 38.92000 ? 726 HOH B O   1 
HETATM 5911 O  O   . HOH X 6 .   ? 53.55300  11.73800  18.49900 1.000 38.93000 ? 727 HOH B O   1 
HETATM 5912 O  O   . HOH X 6 .   ? 33.19900  16.02700  12.15700 1.000 32.63000 ? 728 HOH B O   1 
HETATM 5913 O  O   . HOH X 6 .   ? 24.39600  12.20200  15.24700 1.000 36.87000 ? 729 HOH B O   1 
HETATM 5914 O  O   . HOH X 6 .   ? 27.17000  -1.76800  42.32500 1.000 50.61000 ? 730 HOH B O   1 
HETATM 5915 O  O   . HOH X 6 .   ? 43.677    -3.084    9.063    1.000 48.19000 ? 731 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   . THR A 8   ? 0.77320 0.96950 0.66520 -0.21830 0.08510  -0.20200 2   THR A N   
2    C CA  . THR A 8   ? 0.85570 1.05520 0.78420 -0.20530 0.10200  -0.21750 2   THR A CA  
3    C C   . THR A 8   ? 0.84570 1.01620 0.76670 -0.18070 0.08170  -0.18830 2   THR A C   
4    O O   . THR A 8   ? 0.84990 1.01800 0.72420 -0.19560 0.06130  -0.15630 2   THR A O   
5    C CB  . THR A 8   ? 0.90930 1.14850 0.82090 -0.24580 0.12220  -0.23170 2   THR A CB  
6    O OG1 . THR A 8   ? 0.77570 1.01750 0.72670 -0.23360 0.13560  -0.24640 2   THR A OG1 
7    C CG2 . THR A 8   ? 0.99160 1.23910 0.83250 -0.28120 0.10290  -0.19400 2   THR A CG2 
8    N N   . PRO A 9   ? 0.78520 0.93480 0.75860 -0.14530 0.08440  -0.19680 3   PRO A N   
9    C CA  . PRO A 9   ? 0.70840 0.83250 0.68030 -0.12310 0.06620  -0.17350 3   PRO A CA  
10   C C   . PRO A 9   ? 0.74340 0.87340 0.68410 -0.13430 0.06320  -0.15390 3   PRO A C   
11   O O   . PRO A 9   ? 0.75810 0.90830 0.69890 -0.14950 0.08290  -0.17000 3   PRO A O   
12   C CB  . PRO A 9   ? 0.57130 0.68030 0.61220 -0.09100 0.07510  -0.18600 3   PRO A CB  
13   C CG  . PRO A 9   ? 0.61320 0.72930 0.68720 -0.09210 0.08280  -0.20610 3   PRO A CG  
14   C CD  . PRO A 9   ? 0.77990 0.92780 0.82130 -0.12640 0.09810  -0.22300 3   PRO A CD  
15   N N   . SER A 10  ? 0.56990 0.68190 0.49940 -0.12320 0.03670  -0.11260 4   SER A N   
16   C CA  . SER A 10  ? 0.61570 0.72850 0.52370 -0.13170 0.02800  -0.08810 4   SER A CA  
17   C C   . SER A 10  ? 0.51610 0.61310 0.46390 -0.10030 0.03460  -0.08520 4   SER A C   
18   O O   . SER A 10  ? 0.47060 0.55640 0.45960 -0.07500 0.04120  -0.09610 4   SER A O   
19   C CB  . SER A 10  ? 0.58160 0.68410 0.46940 -0.13930 -0.00700 -0.04720 4   SER A CB  
20   O OG  . SER A 10  ? 0.61860 0.69870 0.54640 -0.10580 -0.02010 -0.03500 4   SER A OG  
21   N N   . GLU A 11  ? 0.48560 0.58300 0.41970 -0.10620 0.03010  -0.06750 5   GLU A N   
22   C CA  . GLU A 11  ? 0.47130 0.55780 0.43600 -0.08320 0.03670  -0.06470 5   GLU A CA  
23   C C   . GLU A 11  ? 0.43020 0.49510 0.40980 -0.06310 0.01430  -0.03610 5   GLU A C   
24   O O   . GLU A 11  ? 0.39870 0.45920 0.36580 -0.07100 -0.00190 -0.01290 5   GLU A O   
25   C CB  . GLU A 11  ? 0.56780 0.66980 0.51100 -0.10340 0.04700  -0.06580 5   GLU A CB  
26   C CG  . GLU A 11  ? 0.65700 0.78990 0.58370 -0.13200 0.07230  -0.10070 5   GLU A CG  
27   C CD  . GLU A 11  ? 0.68920 0.82680 0.67000 -0.11380 0.09840  -0.13660 5   GLU A CD  
28   O OE1 . GLU A 11  ? 0.68170 0.82360 0.68110 -0.11010 0.10860  -0.14060 5   GLU A OE1 
29   O OE2 . GLU A 11  ? 0.59380 0.72780 0.60520 -0.10280 0.10360  -0.15700 5   GLU A OE2 
30   N N   . ASP A 12  ? 0.29190 0.34590 0.30310 -0.04020 0.01350  -0.03960 6   ASP A N   
31   C CA  . ASP A 12  ? 0.30590 0.34750 0.33610 -0.02510 -0.00260 -0.02310 6   ASP A CA  
32   C C   . ASP A 12  ? 0.28120 0.31850 0.33620 -0.00930 0.00590  -0.02530 6   ASP A C   
33   O O   . ASP A 12  ? 0.21040 0.24930 0.28190 -0.00290 0.01550  -0.03560 6   ASP A O   
34   C CB  . ASP A 12  ? 0.26940 0.30970 0.30980 -0.02010 -0.01090 -0.02570 6   ASP A CB  
35   C CG  . ASP A 12  ? 0.31020 0.35490 0.32640 -0.03840 -0.02460 -0.01860 6   ASP A CG  
36   O OD1 . ASP A 12  ? 0.40620 0.45000 0.40910 -0.05180 -0.04080 0.00070  6   ASP A OD1 
37   O OD2 . ASP A 12  ? 0.29030 0.33980 0.30090 -0.04280 -0.02210 -0.02950 6   ASP A OD2 
38   N N   . PHE A 13  ? 0.24700 0.27910 0.30760 -0.00620 -0.00060 -0.01380 7   PHE A N   
39   C CA  . PHE A 13  ? 0.23630 0.26740 0.31270 0.00210  0.00700  -0.01480 7   PHE A CA  
40   C C   . PHE A 13  ? 0.23030 0.25950 0.32820 0.00870  -0.00080 -0.01310 7   PHE A C   
41   O O   . PHE A 13  ? 0.24210 0.26670 0.35080 0.00860  -0.01460 -0.00760 7   PHE A O   
42   C CB  . PHE A 13  ? 0.20820 0.23940 0.27280 -0.00420 0.01230  -0.00950 7   PHE A CB  
43   C CG  . PHE A 13  ? 0.28350 0.32380 0.33950 -0.01180 0.02680  -0.02130 7   PHE A CG  
44   C CD1 . PHE A 13  ? 0.33590 0.38510 0.36570 -0.02890 0.02840  -0.02530 7   PHE A CD1 
45   C CD2 . PHE A 13  ? 0.25740 0.30080 0.33800 -0.00520 0.03790  -0.03020 7   PHE A CD2 
46   C CE1 . PHE A 13  ? 0.44430 0.50870 0.47410 -0.03870 0.04730  -0.04700 7   PHE A CE1 
47   C CE2 . PHE A 13  ? 0.30500 0.35870 0.39760 -0.01050 0.05250  -0.04850 7   PHE A CE2 
48   C CZ  . PHE A 13  ? 0.39430 0.46030 0.46230 -0.02690 0.06040  -0.06130 7   PHE A CZ  
49   N N   . VAL A 14  ? 0.17050 0.20600 0.28020 0.01100  0.00710  -0.01910 8   VAL A N   
50   C CA  . VAL A 14  ? 0.15920 0.19930 0.28820 0.01150  0.00700  -0.02500 8   VAL A CA  
51   C C   . VAL A 14  ? 0.17230 0.20980 0.29510 0.00910  0.01200  -0.01930 8   VAL A C   
52   O O   . VAL A 14  ? 0.16280 0.20140 0.27460 0.00650  0.01780  -0.01390 8   VAL A O   
53   C CB  . VAL A 14  ? 0.17770 0.23460 0.31640 0.00590  0.01320  -0.03730 8   VAL A CB  
54   C CG1 . VAL A 14  ? 0.19700 0.25860 0.32190 -0.00140 0.01690  -0.02950 8   VAL A CG1 
55   C CG2 . VAL A 14  ? 0.14600 0.21550 0.30300 0.00010  0.01920  -0.05150 8   VAL A CG2 
56   N N   . VAL A 15  ? 0.15400 0.18680 0.29100 0.01020  0.00760  -0.02010 9   VAL A N   
57   C CA  . VAL A 15  ? 0.16110 0.18870 0.29060 0.00780  0.00980  -0.01190 9   VAL A CA  
58   C C   . VAL A 15  ? 0.15560 0.19050 0.30600 0.00460  0.01410  -0.02500 9   VAL A C   
59   O O   . VAL A 15  ? 0.15420 0.19160 0.33610 0.00690  0.01070  -0.03970 9   VAL A O   
60   C CB  . VAL A 15  ? 0.20080 0.21500 0.32520 0.00680  -0.00250 0.00280  9   VAL A CB  
61   C CG1 . VAL A 15  ? 0.22680 0.23740 0.34550 0.00270  -0.00030 0.01070  9   VAL A CG1 
62   C CG2 . VAL A 15  ? 0.17570 0.19070 0.27280 0.00180  -0.00280 0.01000  9   VAL A CG2 
63   N N   . THR A 16  ? 0.19800 0.23900 0.33670 -0.00270 0.02180  -0.02260 10  THR A N   
64   C CA  . THR A 16  ? 0.15290 0.20310 0.30670 -0.01060 0.02720  -0.03690 10  THR A CA  
65   C C   . THR A 16  ? 0.18580 0.22250 0.34040 -0.00870 0.02300  -0.02650 10  THR A C   
66   O O   . THR A 16  ? 0.18730 0.21610 0.32210 -0.00690 0.02110  -0.00810 10  THR A O   
67   C CB  . THR A 16  ? 0.17460 0.24600 0.31220 -0.02820 0.03590  -0.04030 10  THR A CB  
68   O OG1 . THR A 16  ? 0.18970 0.25620 0.30940 -0.03050 0.03320  -0.01850 10  THR A OG1 
69   C CG2 . THR A 16  ? 0.22470 0.30570 0.35510 -0.03150 0.03590  -0.04220 10  THR A CG2 
70   N N   . ASP A 17  ? 0.17430 0.21020 0.35790 -0.01000 0.02230  -0.04120 11  ASP A N   
71   C CA  . ASP A 17  ? 0.17170 0.19300 0.36200 -0.00890 0.01520  -0.03060 11  ASP A CA  
72   C C   . ASP A 17  ? 0.16790 0.20080 0.37090 -0.01990 0.02490  -0.05000 11  ASP A C   
73   O O   . ASP A 17  ? 0.18210 0.23460 0.40130 -0.02880 0.03590  -0.07830 11  ASP A O   
74   C CB  . ASP A 17  ? 0.17690 0.17830 0.40370 -0.00050 -0.00420 -0.02470 11  ASP A CB  
75   C CG  . ASP A 17  ? 0.22810 0.23360 0.51760 0.00240  -0.00550 -0.05540 11  ASP A CG  
76   O OD1 . ASP A 17  ? 0.20560 0.22090 0.51040 0.00470  -0.00350 -0.07030 11  ASP A OD1 
77   O OD2 . ASP A 17  ? 0.24320 0.24740 0.56650 0.00090  -0.00770 -0.06630 11  ASP A OD2 
78   N N   . ARG A 18  ? 0.16860 0.19240 0.36390 -0.02260 0.02190  -0.03680 12  ARG A N   
79   C CA  . ARG A 18  ? 0.18970 0.22050 0.40090 -0.03330 0.02830  -0.05440 12  ARG A CA  
80   C C   . ARG A 18  ? 0.18030 0.18730 0.42670 -0.02510 0.01270  -0.04770 12  ARG A C   
81   O O   . ARG A 18  ? 0.16890 0.16170 0.39510 -0.02360 0.00320  -0.01920 12  ARG A O   
82   C CB  . ARG A 18  ? 0.16690 0.20870 0.33930 -0.04670 0.03490  -0.04030 12  ARG A CB  
83   C CG  . ARG A 18  ? 0.18150 0.23380 0.35230 -0.06130 0.04130  -0.05690 12  ARG A CG  
84   C CD  . ARG A 18  ? 0.21160 0.27540 0.34050 -0.07530 0.04100  -0.03620 12  ARG A CD  
85   N NE  . ARG A 18  ? 0.19230 0.27020 0.29560 -0.08200 0.04080  -0.03120 12  ARG A NE  
86   C CZ  . ARG A 18  ? 0.27240 0.36690 0.35700 -0.09730 0.04570  -0.04750 12  ARG A CZ  
87   N NH1 . ARG A 18  ? 0.23340 0.33660 0.31840 -0.10870 0.05450  -0.07230 12  ARG A NH1 
88   N NH2 . ARG A 18  ? 0.20700 0.31030 0.27220 -0.10280 0.04280  -0.04100 12  ARG A NH2 
89   N N   . GLY A 19  ? 0.18290 0.18810 0.48120 -0.01880 0.00880  -0.07170 13  GLY A N   
90   C CA  . GLY A 19  ? 0.22550 0.21350 0.56140 -0.01040 -0.01110 -0.05990 13  GLY A CA  
91   C C   . GLY A 19  ? 0.22370 0.19260 0.55560 -0.00570 -0.03610 -0.02350 13  GLY A C   
92   O O   . GLY A 19  ? 0.27430 0.23060 0.60590 -0.00860 -0.05370 0.00090  13  GLY A O   
93   N N   . GLY A 20  ? 0.22380 0.19370 0.54720 -0.00220 -0.03850 -0.01910 14  GLY A N   
94   C CA  . GLY A 20  ? 0.23140 0.18830 0.53470 -0.00420 -0.05920 0.01530  14  GLY A CA  
95   C C   . GLY A 20  ? 0.27140 0.22540 0.51060 -0.01260 -0.05070 0.03850  14  GLY A C   
96   O O   . GLY A 20  ? 0.30630 0.25830 0.51900 -0.01830 -0.06090 0.06020  14  GLY A O   
97   N N   . ILE A 21  ? 0.19080 0.15600 0.40180 -0.01550 -0.03090 0.03160  15  ILE A N   
98   C CA  . ILE A 21  ? 0.18780 0.16280 0.34780 -0.02150 -0.01950 0.04630  15  ILE A CA  
99   C C   . ILE A 21  ? 0.17210 0.16200 0.31400 -0.01620 -0.00400 0.03400  15  ILE A C   
100  O O   . ILE A 21  ? 0.16700 0.16690 0.31830 -0.01440 0.00610  0.01550  15  ILE A O   
101  C CB  . ILE A 21  ? 0.16570 0.14500 0.31680 -0.02720 -0.01030 0.04740  15  ILE A CB  
102  C CG1 . ILE A 21  ? 0.16010 0.12320 0.33760 -0.03220 -0.02660 0.05630  15  ILE A CG1 
103  C CG2 . ILE A 21  ? 0.19010 0.18150 0.30560 -0.03280 0.00090  0.05930  15  ILE A CG2 
104  C CD1 . ILE A 21  ? 0.17910 0.14650 0.35890 -0.03660 -0.01710 0.04850  15  ILE A CD1 
105  N N   . VAL A 22  ? 0.18550 0.17990 0.30130 -0.01810 -0.00190 0.04340  16  VAL A N   
106  C CA  . VAL A 22  ? 0.18760 0.19320 0.29440 -0.01290 0.00950  0.03270  16  VAL A CA  
107  C C   . VAL A 22  ? 0.15940 0.17640 0.26500 -0.01390 0.02190  0.02770  16  VAL A C   
108  O O   . VAL A 22  ? 0.15010 0.17060 0.25040 -0.01830 0.02640  0.03510  16  VAL A O   
109  C CB  . VAL A 22  ? 0.20400 0.21460 0.28810 -0.01730 0.01190  0.03870  16  VAL A CB  
110  C CG1 . VAL A 22  ? 0.18890 0.20890 0.27360 -0.01110 0.02240  0.02670  16  VAL A CG1 
111  C CG2 . VAL A 22  ? 0.26300 0.26470 0.34390 -0.02300 -0.00580 0.04950  16  VAL A CG2 
112  N N   . GLU A 23  ? 0.16330 0.18810 0.27600 -0.01350 0.02510  0.01680  17  GLU A N   
113  C CA  . GLU A 23  ? 0.15310 0.19040 0.26430 -0.02090 0.02990  0.01880  17  GLU A CA  
114  C C   . GLU A 23  ? 0.16590 0.20700 0.27830 -0.01730 0.03100  0.02290  17  GLU A C   
115  O O   . GLU A 23  ? 0.13330 0.17620 0.25350 -0.01640 0.03340  0.02950  17  GLU A O   
116  C CB  . GLU A 23  ? 0.16020 0.20970 0.27470 -0.03190 0.03160  0.00570  17  GLU A CB  
117  C CG  . GLU A 23  ? 0.19240 0.25690 0.29700 -0.04870 0.03000  0.01400  17  GLU A CG  
118  C CD  . GLU A 23  ? 0.27830 0.34640 0.37620 -0.05940 0.02910  0.01580  17  GLU A CD  
119  O OE1 . GLU A 23  ? 0.23410 0.30720 0.33310 -0.06580 0.03320  -0.00180 17  GLU A OE1 
120  O OE2 . GLU A 23  ? 0.20960 0.26860 0.30270 -0.05630 0.02600  0.02690  17  GLU A OE2 
121  N N   . ASN A 24  ? 0.16290 0.20660 0.27530 -0.01580 0.02970  0.01590  18  ASN A N   
122  C CA  . ASN A 24  ? 0.15980 0.20600 0.27920 -0.01330 0.02880  0.01800  18  ASN A CA  
123  C C   . ASN A 24  ? 0.15670 0.19720 0.26960 -0.00520 0.02930  0.00940  18  ASN A C   
124  O O   . ASN A 24  ? 0.14090 0.17840 0.25020 -0.00330 0.02670  0.00330  18  ASN A O   
125  C CB  . ASN A 24  ? 0.14010 0.19770 0.26410 -0.02560 0.02270  0.02260  18  ASN A CB  
126  C CG  . ASN A 24  ? 0.17390 0.23520 0.28920 -0.03840 0.01580  0.03220  18  ASN A CG  
127  O OD1 . ASN A 24  ? 0.15320 0.20880 0.27710 -0.03420 0.01350  0.03990  18  ASN A OD1 
128  N ND2 . ASN A 24  ? 0.18390 0.25550 0.28310 -0.05480 0.01420  0.02820  18  ASN A ND2 
129  N N   . SER A 25  ? 0.13320 0.17370 0.25220 -0.00160 0.03120  0.00730  19  SER A N   
130  C CA  . SER A 25  ? 0.13350 0.17110 0.24430 0.00230  0.03010  -0.00010 19  SER A CA  
131  C C   . SER A 25  ? 0.14750 0.18840 0.27440 0.00290  0.02930  -0.00300 19  SER A C   
132  O O   . SER A 25  ? 0.14280 0.18590 0.29390 0.00210  0.02990  -0.00080 19  SER A O   
133  C CB  . SER A 25  ? 0.18550 0.22060 0.28070 0.00080  0.03330  -0.00220 19  SER A CB  
134  O OG  . SER A 25  ? 0.22600 0.26840 0.33070 -0.00160 0.04380  -0.01020 19  SER A OG  
135  N N   . HIS A 26  ? 0.13150 0.17230 0.25290 0.00410  0.02560  -0.00750 20  HIS A N   
136  C CA  . HIS A 26  ? 0.14980 0.19300 0.28630 0.00260  0.02140  -0.00800 20  HIS A CA  
137  C C   . HIS A 26  ? 0.15240 0.19260 0.28110 0.00670  0.02290  -0.01860 20  HIS A C   
138  O O   . HIS A 26  ? 0.16960 0.20900 0.28220 0.00780  0.02020  -0.02050 20  HIS A O   
139  C CB  . HIS A 26  ? 0.12420 0.17660 0.25810 -0.00720 0.01500  -0.00210 20  HIS A CB  
140  C CG  . HIS A 26  ? 0.11590 0.17590 0.24770 -0.01790 0.01390  0.00650  20  HIS A CG  
141  N ND1 . HIS A 26  ? 0.11870 0.18430 0.26130 -0.03180 0.00400  0.02260  20  HIS A ND1 
142  C CD2 . HIS A 26  ? 0.16770 0.23020 0.28880 -0.01930 0.01910  0.00200  20  HIS A CD2 
143  C CE1 . HIS A 26  ? 0.18850 0.25970 0.31570 -0.04160 0.00460  0.02590  20  HIS A CE1 
144  N NE2 . HIS A 26  ? 0.14740 0.21980 0.26880 -0.03480 0.01550  0.01270  20  HIS A NE2 
145  N N   . ARG A 27  ? 0.15460 0.19410 0.30160 0.00770  0.02580  -0.02690 21  ARG A N   
146  C CA  . ARG A 27  ? 0.15610 0.19530 0.29330 0.00750  0.02820  -0.03940 21  ARG A CA  
147  C C   . ARG A 27  ? 0.14610 0.18480 0.28600 0.00750  0.01880  -0.03550 21  ARG A C   
148  O O   . ARG A 27  ? 0.14460 0.18400 0.30650 0.00480  0.01180  -0.02740 21  ARG A O   
149  C CB  . ARG A 27  ? 0.19230 0.23490 0.35570 0.00630  0.03850  -0.05810 21  ARG A CB  
150  C CG  . ARG A 27  ? 0.23880 0.28540 0.38890 0.00070  0.04370  -0.07540 21  ARG A CG  
151  C CD  . ARG A 27  ? 0.33310 0.38580 0.51930 -0.00280 0.05590  -0.10220 21  ARG A CD  
152  N NE  . ARG A 27  ? 0.50510 0.56930 0.68290 -0.01270 0.07030  -0.11610 21  ARG A NE  
153  C CZ  . ARG A 27  ? 0.54210 0.62320 0.67860 -0.02820 0.08310  -0.12790 21  ARG A CZ  
154  N NH1 . ARG A 27  ? 0.48250 0.56180 0.57550 -0.03620 0.07320  -0.11750 21  ARG A NH1 
155  N NH2 . ARG A 27  ? 0.46780 0.56150 0.59720 -0.04150 0.09480  -0.13890 21  ARG A NH2 
156  N N   . VAL A 28  ? 0.14430 0.18350 0.26370 0.00730  0.01600  -0.03840 22  VAL A N   
157  C CA  . VAL A 28  ? 0.12070 0.16280 0.24290 0.00660  0.00850  -0.03710 22  VAL A CA  
158  C C   . VAL A 28  ? 0.17490 0.21500 0.29640 0.00520  0.00840  -0.04740 22  VAL A C   
159  O O   . VAL A 28  ? 0.19450 0.23470 0.29820 0.00160  0.01180  -0.05460 22  VAL A O   
160  C CB  . VAL A 28  ? 0.15770 0.20390 0.27150 0.00780  0.00370  -0.03530 22  VAL A CB  
161  C CG1 . VAL A 28  ? 0.17450 0.22980 0.29750 0.00500  -0.00060 -0.03860 22  VAL A CG1 
162  C CG2 . VAL A 28  ? 0.20840 0.25760 0.32540 0.00790  0.00620  -0.03180 22  VAL A CG2 
163  N N   . HIS A 29  ? 0.15400 0.19450 0.29290 0.00360  0.00330  -0.04730 23  HIS A N   
164  C CA  . HIS A 29  ? 0.13900 0.17830 0.27890 0.00160  0.00120  -0.05710 23  HIS A CA  
165  C C   . HIS A 29  ? 0.14420 0.18970 0.28120 -0.00050 -0.00760 -0.05030 23  HIS A C   
166  O O   . HIS A 29  ? 0.14240 0.19490 0.28810 -0.00520 -0.01120 -0.04080 23  HIS A O   
167  C CB  . HIS A 29  ? 0.14580 0.17960 0.32140 0.00090  0.00130  -0.06470 23  HIS A CB  
168  C CG  . HIS A 29  ? 0.16720 0.19950 0.36220 0.00290  0.01190  -0.07640 23  HIS A CG  
169  N ND1 . HIS A 29  ? 0.20540 0.24310 0.39230 -0.00150 0.02610  -0.10060 23  HIS A ND1 
170  C CD2 . HIS A 29  ? 0.15010 0.18010 0.37500 0.00540  0.01070  -0.06900 23  HIS A CD2 
171  C CE1 . HIS A 29  ? 0.23170 0.27210 0.44540 -0.00030 0.03630  -0.11150 23  HIS A CE1 
172  N NE2 . HIS A 29  ? 0.14800 0.18150 0.38640 0.00550  0.02540  -0.09050 23  HIS A NE2 
173  N N   . ALA A 30  ? 0.15320 0.20030 0.27770 -0.00120 -0.01110 -0.05540 24  ALA A N   
174  C CA  . ALA A 30  ? 0.14700 0.20340 0.27610 -0.00310 -0.01810 -0.05280 24  ALA A CA  
175  C C   . ALA A 30  ? 0.17710 0.23160 0.30070 -0.00590 -0.02350 -0.05890 24  ALA A C   
176  O O   . ALA A 30  ? 0.21160 0.26150 0.31850 -0.00880 -0.02290 -0.06390 24  ALA A O   
177  C CB  . ALA A 30  ? 0.14810 0.21260 0.27910 0.00020  -0.01970 -0.05110 24  ALA A CB  
178  N N   . ALA A 31  ? 0.12530 0.18650 0.26000 -0.00960 -0.02870 -0.05850 25  ALA A N   
179  C CA  . ALA A 31  ? 0.13840 0.19980 0.27000 -0.01320 -0.03540 -0.06330 25  ALA A CA  
180  C C   . ALA A 31  ? 0.15820 0.23500 0.30190 -0.01420 -0.04120 -0.06120 25  ALA A C   
181  O O   . ALA A 31  ? 0.17250 0.26220 0.32790 -0.01840 -0.03750 -0.05990 25  ALA A O   
182  C CB  . ALA A 31  ? 0.15180 0.20610 0.29590 -0.01800 -0.03600 -0.06850 25  ALA A CB  
183  N N   . VAL A 32  ? 0.17180 0.25090 0.31530 -0.01380 -0.05060 -0.06140 26  VAL A N   
184  C CA  . VAL A 32  ? 0.18370 0.27910 0.35110 -0.01460 -0.05690 -0.06380 26  VAL A CA  
185  C C   . VAL A 32  ? 0.22180 0.31470 0.38240 -0.02070 -0.06630 -0.06380 26  VAL A C   
186  O O   . VAL A 32  ? 0.23440 0.31850 0.37760 -0.02440 -0.07540 -0.05990 26  VAL A O   
187  C CB  . VAL A 32  ? 0.18180 0.28060 0.37090 -0.00790 -0.06430 -0.06150 26  VAL A CB  
188  C CG1 . VAL A 32  ? 0.14590 0.25460 0.35850 -0.00690 -0.06380 -0.06570 26  VAL A CG1 
189  C CG2 . VAL A 32  ? 0.15140 0.25050 0.34720 -0.00240 -0.05440 -0.06390 26  VAL A CG2 
190  N N   . VAL A 33  ? 0.18590 0.28620 0.35240 -0.02560 -0.06330 -0.06540 27  VAL A N   
191  C CA  . VAL A 33  ? 0.19480 0.29070 0.35410 -0.03210 -0.07090 -0.06620 27  VAL A CA  
192  C C   . VAL A 33  ? 0.25430 0.36390 0.42670 -0.03430 -0.07260 -0.06410 27  VAL A C   
193  O O   . VAL A 33  ? 0.18600 0.30990 0.37150 -0.03410 -0.06380 -0.06590 27  VAL A O   
194  C CB  . VAL A 33  ? 0.23140 0.31650 0.38660 -0.03760 -0.06720 -0.06860 27  VAL A CB  
195  C CG1 . VAL A 33  ? 0.23430 0.30580 0.38340 -0.03390 -0.06060 -0.07320 27  VAL A CG1 
196  C CG2 . VAL A 33  ? 0.17690 0.27070 0.33920 -0.04370 -0.06280 -0.05960 27  VAL A CG2 
197  N N   . ASP A 34  ? 0.25410 0.36140 0.42240 -0.03910 -0.08290 -0.06300 28  ASP A N   
198  C CA  . ASP A 34  ? 0.27560 0.39650 0.45850 -0.04200 -0.08460 -0.06200 28  ASP A CA  
199  C C   . ASP A 34  ? 0.23680 0.35960 0.41290 -0.05180 -0.07990 -0.06130 28  ASP A C   
200  O O   . ASP A 34  ? 0.25720 0.36850 0.42380 -0.05470 -0.07720 -0.06010 28  ASP A O   
201  C CB  . ASP A 34  ? 0.26140 0.38110 0.44600 -0.04420 -0.10070 -0.05720 28  ASP A CB  
202  C CG  . ASP A 34  ? 0.33370 0.44340 0.49270 -0.05550 -0.10750 -0.05860 28  ASP A CG  
203  O OD1 . ASP A 34  ? 0.35300 0.45390 0.50220 -0.05900 -0.10010 -0.06500 28  ASP A OD1 
204  O OD2 . ASP A 34  ? 0.34170 0.45250 0.49340 -0.06280 -0.12130 -0.05340 28  ASP A OD2 
205  N N   . ALA A 35  ? 0.26660 0.44490 0.46570 -0.05680 -0.05950 -0.05070 29  ALA A N   
206  C CA  . ALA A 35  ? 0.23300 0.40590 0.43420 -0.06230 -0.05450 -0.05350 29  ALA A CA  
207  C C   . ALA A 35  ? 0.28720 0.44890 0.47270 -0.06870 -0.06000 -0.05960 29  ALA A C   
208  O O   . ALA A 35  ? 0.29190 0.44520 0.47440 -0.07190 -0.05410 -0.06290 29  ALA A O   
209  C CB  . ALA A 35  ? 0.20260 0.38770 0.42480 -0.06580 -0.05540 -0.04870 29  ALA A CB  
210  N N   . LYS A 36  ? 0.23340 0.39380 0.40810 -0.07100 -0.07090 -0.06100 30  LYS A N   
211  C CA  . LYS A 36  ? 0.26990 0.41620 0.42580 -0.07660 -0.07450 -0.06760 30  LYS A CA  
212  C C   . LYS A 36  ? 0.31910 0.45320 0.45590 -0.07190 -0.06960 -0.07270 30  LYS A C   
213  O O   . LYS A 36  ? 0.32120 0.44130 0.44160 -0.07570 -0.06940 -0.07850 30  LYS A O   
214  C CB  . LYS A 36  ? 0.30700 0.45520 0.45700 -0.08290 -0.08880 -0.06740 30  LYS A CB  
215  C CG  . LYS A 36  ? 0.39100 0.55580 0.56230 -0.08740 -0.09490 -0.06110 30  LYS A CG  
216  C CD  . LYS A 36  ? 0.43140 0.59260 0.60030 -0.09790 -0.10190 -0.06370 30  LYS A CD  
217  C CE  . LYS A 36  ? 0.41140 0.59060 0.60480 -0.10210 -0.10380 -0.05840 30  LYS A CE  
218  N NZ  . LYS A 36  ? 0.58090 0.77770 0.78020 -0.10370 -0.11490 -0.05430 30  LYS A NZ  
219  N N   . GLY A 37  ? 0.27210 0.41060 0.41130 -0.06400 -0.06470 -0.07050 31  GLY A N   
220  C CA  . GLY A 37  ? 0.27740 0.40600 0.40100 -0.05950 -0.05990 -0.07470 31  GLY A CA  
221  C C   . GLY A 37  ? 0.24880 0.37670 0.35930 -0.05690 -0.06700 -0.07610 31  GLY A C   
222  O O   . GLY A 37  ? 0.25480 0.37310 0.35110 -0.05380 -0.06300 -0.08050 31  GLY A O   
223  N N   . ARG A 38  ? 0.26730 0.40480 0.38230 -0.05800 -0.07730 -0.07210 32  ARG A N   
224  C CA  . ARG A 38  ? 0.28550 0.42250 0.38660 -0.05510 -0.08440 -0.07270 32  ARG A CA  
225  C C   . ARG A 38  ? 0.22920 0.37290 0.33710 -0.04540 -0.07830 -0.07000 32  ARG A C   
226  O O   . ARG A 38  ? 0.25520 0.40910 0.38310 -0.04140 -0.07300 -0.06440 32  ARG A O   
227  C CB  . ARG A 38  ? 0.28360 0.43020 0.38890 -0.05890 -0.09800 -0.06750 32  ARG A CB  
228  C CG  . ARG A 38  ? 0.42940 0.57260 0.53580 -0.06860 -0.10280 -0.06880 32  ARG A CG  
229  C CD  . ARG A 38  ? 0.57110 0.71180 0.66320 -0.07590 -0.11780 -0.06870 32  ARG A CD  
230  N NE  . ARG A 38  ? 0.61270 0.77230 0.72200 -0.07690 -0.12750 -0.05960 32  ARG A NE  
231  C CZ  . ARG A 38  ? 0.58990 0.76480 0.72360 -0.08010 -0.12710 -0.05460 32  ARG A CZ  
232  N NH1 . ARG A 38  ? 0.58460 0.75640 0.72950 -0.08160 -0.11780 -0.05660 32  ARG A NH1 
233  N NH2 . ARG A 38  ? 0.59020 0.78600 0.73710 -0.08070 -0.13440 -0.04890 32  ARG A NH2 
234  N N   . LEU A 39  ? 0.23890 0.37110 0.32630 -0.04080 -0.07630 -0.07140 33  LEU A N   
235  C CA  . LEU A 39  ? 0.24630 0.37880 0.33620 -0.03090 -0.06800 -0.06720 33  LEU A CA  
236  C C   . LEU A 39  ? 0.27740 0.42460 0.37890 -0.02630 -0.07460 -0.06000 33  LEU A C   
237  O O   . LEU A 39  ? 0.25280 0.39910 0.34210 -0.02760 -0.08440 -0.05820 33  LEU A O   
238  C CB  . LEU A 39  ? 0.21350 0.32640 0.27810 -0.02740 -0.06220 -0.06980 33  LEU A CB  
239  C CG  . LEU A 39  ? 0.25980 0.37120 0.32780 -0.01780 -0.05260 -0.06630 33  LEU A CG  
240  C CD1 . LEU A 39  ? 0.22170 0.33390 0.30290 -0.01760 -0.04350 -0.06790 33  LEU A CD1 
241  C CD2 . LEU A 39  ? 0.33420 0.42700 0.37790 -0.01440 -0.04820 -0.06790 33  LEU A CD2 
242  N N   . LEU A 40  ? 0.20970 0.36930 0.33380 -0.02110 -0.06900 -0.05580 34  LEU A N   
243  C CA  . LEU A 40  ? 0.20290 0.37660 0.34170 -0.01600 -0.07370 -0.04820 34  LEU A CA  
244  C C   . LEU A 40  ? 0.24130 0.41060 0.37560 -0.00630 -0.06600 -0.04480 34  LEU A C   
245  O O   . LEU A 40  ? 0.20780 0.38010 0.33920 -0.00220 -0.07140 -0.03920 34  LEU A O   
246  C CB  . LEU A 40  ? 0.22150 0.40730 0.38680 -0.01700 -0.07030 -0.04290 34  LEU A CB  
247  C CG  . LEU A 40  ? 0.23150 0.41860 0.40050 -0.02640 -0.07620 -0.04330 34  LEU A CG  
248  C CD1 . LEU A 40  ? 0.25470 0.44920 0.44490 -0.02660 -0.06890 -0.03780 34  LEU A CD1 
249  C CD2 . LEU A 40  ? 0.23130 0.42410 0.39680 -0.03080 -0.09160 -0.04030 34  LEU A CD2 
250  N N   . TYR A 41  ? 0.18340 0.34540 0.31730 -0.00290 -0.05390 -0.04760 35  TYR A N   
251  C CA  . TYR A 41  ? 0.25750 0.41350 0.38670 0.00560  -0.04590 -0.04540 35  TYR A CA  
252  C C   . TYR A 41  ? 0.19590 0.33690 0.31260 0.00580  -0.03690 -0.05070 35  TYR A C   
253  O O   . TYR A 41  ? 0.17250 0.31120 0.29080 0.00060  -0.03480 -0.05500 35  TYR A O   
254  C CB  . TYR A 41  ? 0.18260 0.35150 0.33590 0.01140  -0.04000 -0.04080 35  TYR A CB  
255  C CG  . TYR A 41  ? 0.21180 0.39530 0.38200 0.01140  -0.04740 -0.03400 35  TYR A CG  
256  C CD1 . TYR A 41  ? 0.24100 0.42920 0.41110 0.01690  -0.05270 -0.02800 35  TYR A CD1 
257  C CD2 . TYR A 41  ? 0.23740 0.42530 0.41930 0.00550  -0.04780 -0.03130 35  TYR A CD2 
258  C CE1 . TYR A 41  ? 0.27090 0.47140 0.45660 0.01640  -0.06000 -0.01990 35  TYR A CE1 
259  C CE2 . TYR A 41  ? 0.22430 0.42360 0.42070 0.00500  -0.05370 -0.02320 35  TYR A CE2 
260  C CZ  . TYR A 41  ? 0.25520 0.46090 0.45400 0.01020  -0.06000 -0.01720 35  TYR A CZ  
261  O OH  . TYR A 41  ? 0.29640 0.51520 0.50990 0.00960  -0.06610 -0.00850 35  TYR A OH  
262  N N   . ALA A 42  ? 0.19210 0.32310 0.29830 0.01210  -0.03130 -0.04980 36  ALA A N   
263  C CA  . ALA A 42  ? 0.16350 0.28060 0.26020 0.01280  -0.02330 -0.05380 36  ALA A CA  
264  C C   . ALA A 42  ? 0.21600 0.32980 0.31540 0.02080  -0.01530 -0.05130 36  ALA A C   
265  O O   . ALA A 42  ? 0.23660 0.35360 0.33710 0.02610  -0.01600 -0.04690 36  ALA A O   
266  C CB  . ALA A 42  ? 0.24820 0.34950 0.32200 0.00960  -0.02520 -0.05730 36  ALA A CB  
267  N N   . LEU A 43  ? 0.19520 0.30260 0.29650 0.02150  -0.00820 -0.05390 37  LEU A N   
268  C CA  . LEU A 43  ? 0.19590 0.29500 0.29590 0.02770  -0.00060 -0.05300 37  LEU A CA  
269  C C   . LEU A 43  ? 0.24370 0.32750 0.33160 0.02600  0.00250  -0.05620 37  LEU A C   
270  O O   . LEU A 43  ? 0.18410 0.26580 0.27010 0.02010  0.00060  -0.05930 37  LEU A O   
271  C CB  . LEU A 43  ? 0.17280 0.27480 0.28500 0.02870  0.00460  -0.05110 37  LEU A CB  
272  C CG  . LEU A 43  ? 0.23460 0.34260 0.35320 0.02860  0.00420  -0.04500 37  LEU A CG  
273  C CD1 . LEU A 43  ? 0.20870 0.30920 0.32570 0.02560  0.00870  -0.04140 37  LEU A CD1 
274  C CD2 . LEU A 43  ? 0.22180 0.33090 0.34080 0.03520  0.00500  -0.04030 37  LEU A CD2 
275  N N   . GLY A 44  ? 0.20930 0.28220 0.29050 0.03120  0.00800  -0.05520 38  GLY A N   
276  C CA  . GLY A 44  ? 0.20740 0.26620 0.28230 0.03040  0.01270  -0.05760 38  GLY A CA  
277  C C   . GLY A 44  ? 0.25790 0.30820 0.31740 0.02470  0.00940  -0.06080 38  GLY A C   
278  O O   . GLY A 44  ? 0.28060 0.32960 0.32760 0.02360  0.00520  -0.06090 38  GLY A O   
279  N N   . ASN A 45  ? 0.22720 0.27080 0.28710 0.02080  0.01110  -0.06350 39  ASN A N   
280  C CA  . ASN A 45  ? 0.23570 0.27050 0.28270 0.01470  0.00880  -0.06730 39  ASN A CA  
281  C C   . ASN A 45  ? 0.21600 0.26180 0.27010 0.00800  0.00250  -0.06880 39  ASN A C   
282  O O   . ASN A 45  ? 0.22560 0.27150 0.28810 0.00580  0.00420  -0.06910 39  ASN A O   
283  C CB  . ASN A 45  ? 0.25490 0.27360 0.29900 0.01500  0.01620  -0.06880 39  ASN A CB  
284  C CG  . ASN A 45  ? 0.28590 0.29370 0.31680 0.00850  0.01540  -0.07320 39  ASN A CG  
285  O OD1 . ASN A 45  ? 0.29240 0.30430 0.31450 0.00370  0.00860  -0.07550 39  ASN A OD1 
286  N ND2 . ASN A 45  ? 0.25170 0.24560 0.28250 0.00810  0.02220  -0.07450 39  ASN A ND2 
287  N N   . PRO A 46  ? 0.24530 0.30000 0.29700 0.00450  -0.00490 -0.06930 40  PRO A N   
288  C CA  . PRO A 46  ? 0.21950 0.28520 0.28100 -0.00170 -0.00990 -0.07040 40  PRO A CA  
289  C C   . PRO A 46  ? 0.22880 0.28530 0.28450 -0.00840 -0.00980 -0.07440 40  PRO A C   
290  O O   . PRO A 46  ? 0.21800 0.28220 0.28230 -0.01360 -0.01260 -0.07510 40  PRO A O   
291  C CB  . PRO A 46  ? 0.23350 0.31020 0.29480 -0.00330 -0.01810 -0.06930 40  PRO A CB  
292  C CG  . PRO A 46  ? 0.24300 0.30820 0.28550 -0.00140 -0.01870 -0.06980 40  PRO A CG  
293  C CD  . PRO A 46  ? 0.22610 0.28120 0.26630 0.00550  -0.00960 -0.06840 40  PRO A CD  
294  N N   . THR A 47  ? 0.19000 0.22990 0.23180 -0.00880 -0.00600 -0.07700 41  THR A N   
295  C CA  . THR A 47  ? 0.21180 0.24150 0.24960 -0.01480 -0.00440 -0.08070 41  THR A CA  
296  C C   . THR A 47  ? 0.22430 0.24380 0.26690 -0.01180 0.00370  -0.07920 41  THR A C   
297  O O   . THR A 47  ? 0.23680 0.24430 0.27540 -0.01540 0.00700  -0.08170 41  THR A O   
298  C CB  . THR A 47  ? 0.26360 0.28060 0.28230 -0.01930 -0.00600 -0.08550 41  THR A CB  
299  O OG1 . THR A 47  ? 0.31300 0.31570 0.31920 -0.01410 0.00060  -0.08560 41  THR A OG1 
300  C CG2 . THR A 47  ? 0.22140 0.24920 0.23570 -0.02310 -0.01620 -0.08620 41  THR A CG2 
301  N N   . ARG A 48  ? 0.20070 0.22510 0.25350 -0.00560 0.00660  -0.07510 42  ARG A N   
302  C CA  . ARG A 48  ? 0.20930 0.22580 0.26920 -0.00260 0.01270  -0.07260 42  ARG A CA  
303  C C   . ARG A 48  ? 0.23310 0.24820 0.29850 -0.00810 0.01220  -0.07270 42  ARG A C   
304  O O   . ARG A 48  ? 0.21250 0.23890 0.28390 -0.01160 0.00790  -0.07210 42  ARG A O   
305  C CB  . ARG A 48  ? 0.20840 0.23410 0.28010 0.00290  0.01330  -0.06840 42  ARG A CB  
306  C CG  . ARG A 48  ? 0.19390 0.21270 0.27530 0.00610  0.01800  -0.06490 42  ARG A CG  
307  C CD  . ARG A 48  ? 0.22810 0.25810 0.32080 0.00860  0.01610  -0.06170 42  ARG A CD  
308  N NE  . ARG A 48  ? 0.20960 0.23500 0.31230 0.01130  0.01850  -0.05790 42  ARG A NE  
309  C CZ  . ARG A 48  ? 0.21060 0.23530 0.31910 0.00810  0.01650  -0.05530 42  ARG A CZ  
310  N NH1 . ARG A 48  ? 0.15250 0.17970 0.25720 0.00200  0.01330  -0.05630 42  ARG A NH1 
311  N NH2 . ARG A 48  ? 0.17050 0.19160 0.28920 0.01080  0.01740  -0.05120 42  ARG A NH2 
312  N N   . MET A 49  ? 0.18380 0.18480 0.24850 -0.00830 0.01750  -0.07270 43  MET A N   
313  C CA  . MET A 49  ? 0.21980 0.21850 0.29080 -0.01280 0.01750  -0.07140 43  MET A CA  
314  C C   . MET A 49  ? 0.22630 0.23420 0.30940 -0.01080 0.01560  -0.06600 43  MET A C   
315  O O   . MET A 49  ? 0.20570 0.21160 0.29510 -0.00540 0.01800  -0.06250 43  MET A O   
316  C CB  . MET A 49  ? 0.24620 0.22740 0.31650 -0.01250 0.02460  -0.07160 43  MET A CB  
317  C CG  . MET A 49  ? 0.32550 0.30290 0.40320 -0.01680 0.02510  -0.06930 43  MET A CG  
318  S SD  . MET A 49  ? 0.39630 0.37480 0.46620 -0.02600 0.02170  -0.07490 43  MET A SD  
319  C CE  . MET A 49  ? 0.39650 0.36340 0.44910 -0.02720 0.02430  -0.08250 43  MET A CE  
320  N N   . THR A 50  ? 0.16940 0.18660 0.25540 -0.01530 0.01150  -0.06530 44  THR A N   
321  C CA  . THR A 50  ? 0.19160 0.21790 0.28480 -0.01410 0.00930  -0.06130 44  THR A CA  
322  C C   . THR A 50  ? 0.20300 0.22960 0.29860 -0.01960 0.00800  -0.05880 44  THR A C   
323  O O   . THR A 50  ? 0.17990 0.20920 0.27310 -0.02490 0.00690  -0.06130 44  THR A O   
324  C CB  . THR A 50  ? 0.18090 0.22070 0.27420 -0.01330 0.00660  -0.06290 44  THR A CB  
325  O OG1 . THR A 50  ? 0.15050 0.18980 0.24170 -0.00770 0.00800  -0.06400 44  THR A OG1 
326  C CG2 . THR A 50  ? 0.17410 0.22140 0.27310 -0.01270 0.00560  -0.05970 44  THR A CG2 
327  N N   . LEU A 51  ? 0.17220 0.19640 0.27300 -0.01830 0.00760  -0.05350 45  LEU A N   
328  C CA  . LEU A 51  ? 0.16700 0.19240 0.26810 -0.02330 0.00570  -0.05000 45  LEU A CA  
329  C C   . LEU A 51  ? 0.19180 0.22880 0.29020 -0.02590 0.00400  -0.05170 45  LEU A C   
330  O O   . LEU A 51  ? 0.17530 0.21830 0.27460 -0.02300 0.00300  -0.05140 45  LEU A O   
331  C CB  . LEU A 51  ? 0.15260 0.17350 0.25900 -0.02120 0.00400  -0.04330 45  LEU A CB  
332  C CG  . LEU A 51  ? 0.19110 0.19990 0.30400 -0.01910 0.00650  -0.03990 45  LEU A CG  
333  C CD1 . LEU A 51  ? 0.15820 0.16520 0.28040 -0.01450 0.00460  -0.03410 45  LEU A CD1 
334  C CD2 . LEU A 51  ? 0.17080 0.17370 0.28340 -0.02430 0.00670  -0.03680 45  LEU A CD2 
335  N N   . ALA A 52  ? 0.16470 0.20450 0.26090 -0.03150 0.00450  -0.05360 46  ALA A N   
336  C CA  . ALA A 52  ? 0.17960 0.22980 0.27530 -0.03400 0.00460  -0.05550 46  ALA A CA  
337  C C   . ALA A 52  ? 0.22320 0.27330 0.31550 -0.03650 0.00460  -0.05150 46  ALA A C   
338  O O   . ALA A 52  ? 0.20050 0.25790 0.29190 -0.03730 0.00590  -0.05290 46  ALA A O   
339  C CB  . ALA A 52  ? 0.15100 0.20410 0.24780 -0.03940 0.00550  -0.05870 46  ALA A CB  
340  N N   . ARG A 53  ? 0.20670 0.24810 0.29700 -0.03800 0.00340  -0.04640 47  ARG A N   
341  C CA  . ARG A 53  ? 0.21760 0.25720 0.30180 -0.04080 0.00200  -0.04180 47  ARG A CA  
342  C C   . ARG A 53  ? 0.22270 0.26700 0.30220 -0.04620 0.00570  -0.04400 47  ARG A C   
343  O O   . ARG A 53  ? 0.19940 0.24470 0.28190 -0.04920 0.00830  -0.04620 47  ARG A O   
344  C CB  . ARG A 53  ? 0.23370 0.27540 0.31770 -0.03690 -0.00080 -0.04070 47  ARG A CB  
345  C CG  . ARG A 53  ? 0.23500 0.27210 0.32670 -0.03130 -0.00300 -0.03860 47  ARG A CG  
346  C CD  . ARG A 53  ? 0.16930 0.19690 0.26320 -0.03230 -0.00560 -0.03160 47  ARG A CD  
347  N NE  . ARG A 53  ? 0.21880 0.24480 0.30740 -0.03510 -0.01050 -0.02580 47  ARG A NE  
348  C CZ  . ARG A 53  ? 0.24800 0.27550 0.33830 -0.03290 -0.01490 -0.02360 47  ARG A CZ  
349  N NH1 . ARG A 53  ? 0.20110 0.23150 0.29990 -0.02720 -0.01430 -0.02640 47  ARG A NH1 
350  N NH2 . ARG A 53  ? 0.25730 0.28270 0.33970 -0.03690 -0.02020 -0.01870 47  ARG A NH2 
351  N N   . SER A 54  ? 0.21380 0.26060 0.28670 -0.04790 0.00660  -0.04380 48  SER A N   
352  C CA  . SER A 54  ? 0.22850 0.27810 0.29760 -0.05320 0.01190  -0.04570 48  SER A CA  
353  C C   . SER A 54  ? 0.28120 0.34100 0.35980 -0.05220 0.01570  -0.05150 48  SER A C   
354  O O   . SER A 54  ? 0.24120 0.30380 0.32040 -0.05650 0.02100  -0.05290 48  SER A O   
355  C CB  . SER A 54  ? 0.29410 0.34170 0.35160 -0.05590 0.01340  -0.04460 48  SER A CB  
356  O OG  . SER A 54  ? 0.40550 0.44340 0.45240 -0.05920 0.00980  -0.03820 48  SER A OG  
357  N N   . ALA A 55  ? 0.19090 0.25610 0.27730 -0.04680 0.01350  -0.05440 49  ALA A N   
358  C CA  . ALA A 55  ? 0.18030 0.25510 0.27650 -0.04670 0.01560  -0.05860 49  ALA A CA  
359  C C   . ALA A 55  ? 0.20050 0.27420 0.30080 -0.05070 0.01540  -0.05920 49  ALA A C   
360  O O   . ALA A 55  ? 0.18790 0.26960 0.29700 -0.05270 0.01690  -0.06200 49  ALA A O   
361  C CB  . ALA A 55  ? 0.16950 0.24980 0.27150 -0.04040 0.01270  -0.06080 49  ALA A CB  
362  N N   . ALA A 56  ? 0.21810 0.28190 0.31350 -0.05240 0.01370  -0.05640 50  ALA A N   
363  C CA  . ALA A 56  ? 0.25670 0.31780 0.35550 -0.05730 0.01460  -0.05710 50  ALA A CA  
364  C C   . ALA A 56  ? 0.25640 0.31490 0.35260 -0.06330 0.01950  -0.05460 50  ALA A C   
365  O O   . ALA A 56  ? 0.26510 0.32170 0.36550 -0.06780 0.02120  -0.05520 50  ALA A O   
366  C CB  . ALA A 56  ? 0.17050 0.22110 0.26700 -0.05630 0.01200  -0.05540 50  ALA A CB  
367  N N   . LYS A 57  ? 0.22030 0.27750 0.30850 -0.06400 0.02220  -0.05210 51  LYS A N   
368  C CA  . LYS A 57  ? 0.27190 0.32490 0.35500 -0.07010 0.02800  -0.04960 51  LYS A CA  
369  C C   . LYS A 57  ? 0.23120 0.29120 0.32560 -0.07420 0.03330  -0.05300 51  LYS A C   
370  O O   . LYS A 57  ? 0.29230 0.34720 0.38700 -0.07920 0.03670  -0.05110 51  LYS A O   
371  C CB  . LYS A 57  ? 0.30230 0.35320 0.37330 -0.07060 0.03070  -0.04790 51  LYS A CB  
372  C CG  . LYS A 57  ? 0.33620 0.37540 0.39190 -0.07310 0.02900  -0.04160 51  LYS A CG  
373  C CD  . LYS A 57  ? 0.36490 0.39880 0.42180 -0.06980 0.02160  -0.03770 51  LYS A CD  
374  C CE  . LYS A 57  ? 0.47090 0.49530 0.51380 -0.07100 0.01750  -0.03060 51  LYS A CE  
375  N NZ  . LYS A 57  ? 0.43370 0.45290 0.48200 -0.06760 0.01120  -0.02590 51  LYS A NZ  
376  N N   . PRO A 58  ? 0.24100 0.31250 0.34660 -0.07250 0.03440  -0.05720 52  PRO A N   
377  C CA  . PRO A 58  ? 0.20520 0.28400 0.32510 -0.07670 0.03880  -0.05960 52  PRO A CA  
378  C C   . PRO A 58  ? 0.22670 0.30430 0.35400 -0.07960 0.03500  -0.06080 52  PRO A C   
379  O O   . PRO A 58  ? 0.26470 0.34180 0.39850 -0.08460 0.03920  -0.06040 52  PRO A O   
380  C CB  . PRO A 58  ? 0.20100 0.29250 0.33240 -0.07270 0.03810  -0.06280 52  PRO A CB  
381  C CG  . PRO A 58  ? 0.23320 0.32190 0.35310 -0.06850 0.03870  -0.06200 52  PRO A CG  
382  C CD  . PRO A 58  ? 0.25090 0.32950 0.35830 -0.06690 0.03250  -0.05940 52  PRO A CD  
383  N N   . ALA A 59  ? 0.22790 0.30350 0.35320 -0.07630 0.02770  -0.06200 53  ALA A N   
384  C CA  . ALA A 59  ? 0.24920 0.32080 0.37810 -0.07900 0.02440  -0.06350 53  ALA A CA  
385  C C   . ALA A 59  ? 0.27300 0.33240 0.39610 -0.08330 0.02800  -0.06010 53  ALA A C   
386  O O   . ALA A 59  ? 0.27260 0.32950 0.40190 -0.08830 0.02970  -0.06100 53  ALA A O   
387  C CB  . ALA A 59  ? 0.20560 0.27540 0.33090 -0.07450 0.01750  -0.06580 53  ALA A CB  
388  N N   . GLN A 60  ? 0.25370 0.30470 0.36440 -0.08070 0.02850  -0.05520 54  GLN A N   
389  C CA  . GLN A 60  ? 0.26790 0.30680 0.37200 -0.08390 0.03140  -0.04990 54  GLN A CA  
390  C C   . GLN A 60  ? 0.28400 0.32300 0.38880 -0.08960 0.03890  -0.04810 54  GLN A C   
391  O O   . GLN A 60  ? 0.30640 0.33820 0.41260 -0.09420 0.04240  -0.04580 54  GLN A O   
392  C CB  . GLN A 60  ? 0.30960 0.34090 0.40140 -0.07980 0.02850  -0.04430 54  GLN A CB  
393  C CG  . GLN A 60  ? 0.28600 0.31560 0.37890 -0.07420 0.02260  -0.04550 54  GLN A CG  
394  C CD  . GLN A 60  ? 0.36130 0.38450 0.44590 -0.07020 0.01930  -0.03940 54  GLN A CD  
395  O OE1 . GLN A 60  ? 0.39430 0.41560 0.48090 -0.06530 0.01570  -0.03970 54  GLN A OE1 
396  N NE2 . GLN A 60  ? 0.38350 0.40300 0.45890 -0.07250 0.02050  -0.03390 54  GLN A NE2 
397  N N   . ALA A 61  ? 0.26720 0.31390 0.37230 -0.08950 0.04250  -0.04950 55  ALA A N   
398  C CA  . ALA A 61  ? 0.28800 0.33450 0.39460 -0.09480 0.05160  -0.04840 55  ALA A CA  
399  C C   . ALA A 61  ? 0.28560 0.33780 0.41030 -0.09950 0.05450  -0.05180 55  ALA A C   
400  O O   . ALA A 61  ? 0.26920 0.31780 0.39620 -0.10480 0.06250  -0.04990 55  ALA A O   
401  C CB  . ALA A 61  ? 0.26390 0.31700 0.36870 -0.09330 0.05590  -0.05000 55  ALA A CB  
402  N N   . LEU A 62  ? 0.28470 0.34500 0.42040 -0.09690 0.04750  -0.05620 56  LEU A N   
403  C CA  . LEU A 62  ? 0.28690 0.35030 0.43480 -0.09860 0.04660  -0.05760 56  LEU A CA  
404  C C   . LEU A 62  ? 0.30270 0.35490 0.44880 -0.10320 0.04820  -0.05590 56  LEU A C   
405  O O   . LEU A 62  ? 0.30780 0.35920 0.46170 -0.10690 0.05230  -0.05520 56  LEU A O   
406  C CB  . LEU A 62  ? 0.25310 0.32480 0.40730 -0.09450 0.03720  -0.06140 56  LEU A CB  
407  C CG  . LEU A 62  ? 0.24830 0.32320 0.41400 -0.09730 0.03390  -0.06320 56  LEU A CG  
408  C CD1 . LEU A 62  ? 0.20600 0.28880 0.38420 -0.09860 0.03900  -0.06180 56  LEU A CD1 
409  C CD2 . LEU A 62  ? 0.20640 0.28640 0.37330 -0.09450 0.02370  -0.06640 56  LEU A CD2 
410  N N   . ALA A 63  ? 0.27020 0.31310 0.40720 -0.10280 0.04570  -0.05460 57  ALA A N   
411  C CA  . ALA A 63  ? 0.25870 0.28930 0.39420 -0.10680 0.04850  -0.05180 57  ALA A CA  
412  C C   . ALA A 63  ? 0.31280 0.33720 0.44500 -0.11160 0.05810  -0.04640 57  ALA A C   
413  O O   . ALA A 63  ? 0.30270 0.32160 0.43970 -0.11520 0.06220  -0.04470 57  ALA A O   
414  C CB  . ALA A 63  ? 0.25300 0.27410 0.37950 -0.10390 0.04460  -0.04980 57  ALA A CB  
415  N N   . ILE A 64  ? 0.27480 0.29860 0.39520 -0.11000 0.06090  -0.04270 58  ILE A N   
416  C CA  . ILE A 64  ? 0.30490 0.32100 0.41680 -0.11400 0.06990  -0.03690 58  ILE A CA  
417  C C   . ILE A 64  ? 0.31880 0.34150 0.44510 -0.11840 0.07790  -0.03990 58  ILE A C   
418  O O   . ILE A 64  ? 0.30990 0.32550 0.43730 -0.12220 0.08460  -0.03650 58  ILE A O   
419  C CB  . ILE A 64  ? 0.28800 0.30190 0.38130 -0.11090 0.07000  -0.03330 58  ILE A CB  
420  C CG1 . ILE A 64  ? 0.28260 0.28950 0.36320 -0.10620 0.06140  -0.02890 58  ILE A CG1 
421  C CG2 . ILE A 64  ? 0.28580 0.29130 0.36780 -0.11570 0.08030  -0.02830 58  ILE A CG2 
422  C CD1 . ILE A 64  ? 0.26000 0.26870 0.32670 -0.10230 0.05800  -0.02810 58  ILE A CD1 
423  N N   . LEU A 65  ? 0.28760 0.32340 0.42320 -0.11490 0.07590  -0.04470 59  LEU A N   
424  C CA  . LEU A 65  ? 0.28410 0.32600 0.43270 -0.11580 0.08140  -0.04580 59  LEU A CA  
425  C C   . LEU A 65  ? 0.25570 0.29840 0.41800 -0.11760 0.07840  -0.04720 59  LEU A C   
426  O O   . LEU A 65  ? 0.30100 0.34380 0.47240 -0.12030 0.08490  -0.04620 59  LEU A O   
427  C CB  . LEU A 65  ? 0.20830 0.26370 0.36580 -0.11120 0.07870  -0.04960 59  LEU A CB  
428  C CG  . LEU A 65  ? 0.34950 0.40490 0.49560 -0.10960 0.08390  -0.04920 59  LEU A CG  
429  C CD1 . LEU A 65  ? 0.35190 0.42010 0.51040 -0.10470 0.08210  -0.05230 59  LEU A CD1 
430  C CD2 . LEU A 65  ? 0.36740 0.41240 0.50250 -0.11430 0.09700  -0.04530 59  LEU A CD2 
431  N N   . GLU A 66  ? 0.26340 0.30590 0.42690 -0.11630 0.06910  -0.04970 60  GLU A N   
432  C CA  . GLU A 66  ? 0.33040 0.37200 0.50460 -0.11890 0.06630  -0.05160 60  GLU A CA  
433  C C   . GLU A 66  ? 0.34180 0.36950 0.51120 -0.12290 0.07170  -0.04770 60  GLU A C   
434  O O   . GLU A 66  ? 0.35900 0.38440 0.53670 -0.12550 0.07060  -0.04920 60  GLU A O   
435  C CB  . GLU A 66  ? 0.36940 0.41530 0.54520 -0.11630 0.05490  -0.05640 60  GLU A CB  
436  C CG  . GLU A 66  ? 0.30260 0.36290 0.48650 -0.11290 0.04890  -0.05950 60  GLU A CG  
437  C CD  . GLU A 66  ? 0.36270 0.42560 0.54560 -0.11110 0.03790  -0.06370 60  GLU A CD  
438  O OE1 . GLU A 66  ? 0.39330 0.44700 0.56540 -0.11030 0.03550  -0.06460 60  GLU A OE1 
439  O OE2 . GLU A 66  ? 0.37210 0.44520 0.56480 -0.11090 0.03190  -0.06580 60  GLU A OE2 
440  N N   . THR A 67  ? 0.30990 0.32770 0.46570 -0.12380 0.07750  -0.04220 61  THR A N   
441  C CA  . THR A 67  ? 0.30240 0.30610 0.45340 -0.12710 0.08240  -0.03690 61  THR A CA  
442  C C   . THR A 67  ? 0.33770 0.33910 0.49450 -0.13090 0.09200  -0.03420 61  THR A C   
443  O O   . THR A 67  ? 0.33020 0.33470 0.48510 -0.13140 0.09860  -0.03290 61  THR A O   
444  C CB  . THR A 67  ? 0.32270 0.31610 0.45660 -0.12700 0.08410  -0.03050 61  THR A CB  
445  O OG1 . THR A 67  ? 0.31160 0.30610 0.44320 -0.12340 0.07520  -0.03310 61  THR A OG1 
446  C CG2 . THR A 67  ? 0.35250 0.33090 0.48130 -0.13020 0.08960  -0.02300 61  THR A CG2 
447  N N   . GLU A 68  ? 0.31930 0.31480 0.48350 -0.13350 0.09320  -0.03370 62  GLU A N   
448  C CA  . GLU A 68  ? 0.35740 0.35030 0.52900 -0.13710 0.10220  -0.03140 62  GLU A CA  
449  C C   . GLU A 68  ? 0.34800 0.33080 0.50460 -0.13870 0.11260  -0.02340 62  GLU A C   
450  O O   . GLU A 68  ? 0.44730 0.41850 0.58930 -0.13900 0.11310  -0.01720 62  GLU A O   
451  C CB  . GLU A 68  ? 0.34310 0.32840 0.52200 -0.13960 0.10190  -0.03140 62  GLU A CB  
452  C CG  . GLU A 68  ? 0.32820 0.32080 0.51880 -0.13930 0.09220  -0.03940 62  GLU A CG  
453  C CD  . GLU A 68  ? 0.31340 0.30240 0.49560 -0.13630 0.08400  -0.04150 62  GLU A CD  
454  O OE1 . GLU A 68  ? 0.34430 0.32950 0.51410 -0.13360 0.08360  -0.03770 62  GLU A OE1 
455  O OE2 . GLU A 68  ? 0.27580 0.26580 0.46400 -0.13700 0.07770  -0.04730 62  GLU A OE2 
456  N N   . GLY A 69  ? 0.36090 0.34710 0.52040 -0.13980 0.12080  -0.02310 63  GLY A N   
457  C CA  . GLY A 69  ? 0.38210 0.35720 0.52480 -0.14180 0.13170  -0.01600 63  GLY A CA  
458  C C   . GLY A 69  ? 0.38990 0.36580 0.51610 -0.14040 0.13300  -0.01530 63  GLY A C   
459  O O   . GLY A 69  ? 0.42060 0.38870 0.53270 -0.14230 0.14300  -0.01110 63  GLY A O   
460  N N   . VAL A 70  ? 0.32620 0.31050 0.45240 -0.13730 0.12360  -0.01960 64  VAL A N   
461  C CA  . VAL A 70  ? 0.36020 0.34510 0.47060 -0.13620 0.12490  -0.01940 64  VAL A CA  
462  C C   . VAL A 70  ? 0.42660 0.41710 0.54120 -0.13570 0.13380  -0.02220 64  VAL A C   
463  O O   . VAL A 70  ? 0.42100 0.40510 0.51720 -0.13670 0.14080  -0.02010 64  VAL A O   
464  C CB  . VAL A 70  ? 0.38090 0.37520 0.49400 -0.13240 0.11300  -0.02420 64  VAL A CB  
465  C CG1 . VAL A 70  ? 0.36840 0.36770 0.47190 -0.13070 0.11430  -0.02640 64  VAL A CG1 
466  C CG2 . VAL A 70  ? 0.36160 0.34610 0.46360 -0.13300 0.10680  -0.01970 64  VAL A CG2 
467  N N   . ALA A 71  ? 0.40470 0.40570 0.54260 -0.13450 0.13390  -0.02680 65  ALA A N   
468  C CA  . ALA A 71  ? 0.35730 0.36310 0.50210 -0.13360 0.14260  -0.02890 65  ALA A CA  
469  C C   . ALA A 71  ? 0.41170 0.40300 0.54130 -0.13700 0.15700  -0.02370 65  ALA A C   
470  O O   . ALA A 71  ? 0.42380 0.41420 0.54910 -0.13630 0.16590  -0.02480 65  ALA A O   
471  C CB  . ALA A 71  ? 0.40350 0.42200 0.57690 -0.13240 0.13950  -0.03300 65  ALA A CB  
472  N N   . GLY A 72  ? 0.42630 0.40540 0.54650 -0.14050 0.15960  -0.01790 66  GLY A N   
473  C CA  . GLY A 72  ? 0.43690 0.40160 0.54180 -0.14360 0.17310  -0.01250 66  GLY A CA  
474  C C   . GLY A 72  ? 0.46800 0.42070 0.54070 -0.14480 0.17770  -0.00880 66  GLY A C   
475  O O   . GLY A 72  ? 0.46570 0.40670 0.52300 -0.14690 0.18960  -0.00570 66  GLY A O   
476  N N   . TYR A 73  ? 0.41980 0.37400 0.48040 -0.14390 0.16850  -0.00910 67  TYR A N   
477  C CA  . TYR A 73  ? 0.44990 0.39230 0.47780 -0.14580 0.17150  -0.00560 67  TYR A CA  
478  C C   . TYR A 73  ? 0.41010 0.35560 0.43440 -0.14410 0.17880  -0.01130 67  TYR A C   
479  O O   . TYR A 73  ? 0.51150 0.44490 0.50630 -0.14630 0.18310  -0.00920 67  TYR A O   
480  C CB  . TYR A 73  ? 0.47100 0.41420 0.48810 -0.14560 0.15920  -0.00410 67  TYR A CB  
481  C CG  . TYR A 73  ? 0.48190 0.41730 0.49600 -0.14740 0.15290  0.00330  67  TYR A CG  
482  C CD1 . TYR A 73  ? 0.51430 0.43260 0.50810 -0.15100 0.15820  0.01290  67  TYR A CD1 
483  C CD2 . TYR A 73  ? 0.42520 0.36940 0.45640 -0.14510 0.14150  0.00100  67  TYR A CD2 
484  C CE1 . TYR A 73  ? 0.54850 0.45920 0.54160 -0.15200 0.15230  0.02060  67  TYR A CE1 
485  C CE2 . TYR A 73  ? 0.40790 0.34440 0.43780 -0.14510 0.13530  0.00760  67  TYR A CE2 
486  C CZ  . TYR A 73  ? 0.50470 0.42470 0.51680 -0.14870 0.14090  0.01760  67  TYR A CZ  
487  O OH  . TYR A 73  ? 0.60170 0.51480 0.61570 -0.14760 0.13440  0.02460  67  TYR A OH  
488  N N   . GLY A 74  ? 0.38910 0.34940 0.44120 -0.14030 0.17940  -0.01830 68  GLY A N   
489  C CA  . GLY A 74  ? 0.46250 0.42480 0.51320 -0.13810 0.18670  -0.02330 68  GLY A CA  
490  C C   . GLY A 74  ? 0.45520 0.42090 0.49360 -0.13620 0.18070  -0.02660 68  GLY A C   
491  O O   . GLY A 74  ? 0.48580 0.44430 0.50730 -0.13650 0.18820  -0.02860 68  GLY A O   
492  N N   . PHE A 75  ? 0.37750 0.35310 0.42340 -0.13450 0.16770  -0.02750 69  PHE A N   
493  C CA  . PHE A 75  ? 0.43560 0.41710 0.47520 -0.13200 0.16180  -0.03140 69  PHE A CA  
494  C C   . PHE A 75  ? 0.38860 0.38210 0.44910 -0.12670 0.16490  -0.03780 69  PHE A C   
495  O O   . PHE A 75  ? 0.36980 0.37440 0.45830 -0.12390 0.16380  -0.03960 69  PHE A O   
496  C CB  . PHE A 75  ? 0.45590 0.44640 0.50340 -0.13060 0.14750  -0.03140 69  PHE A CB  
497  C CG  . PHE A 75  ? 0.48110 0.45920 0.50740 -0.13490 0.14280  -0.02450 69  PHE A CG  
498  C CD1 . PHE A 75  ? 0.46280 0.42610 0.45510 -0.13680 0.14330  -0.02000 69  PHE A CD1 
499  C CD2 . PHE A 75  ? 0.39120 0.37200 0.43010 -0.13380 0.13360  -0.02210 69  PHE A CD2 
500  C CE1 . PHE A 75  ? 0.42980 0.38270 0.40340 -0.13700 0.13380  -0.01210 69  PHE A CE1 
501  C CE2 . PHE A 75  ? 0.40440 0.37380 0.42520 -0.13380 0.12590  -0.01470 69  PHE A CE2 
502  C CZ  . PHE A 75  ? 0.43700 0.39310 0.42630 -0.13520 0.12550  -0.00910 69  PHE A CZ  
503  N N   . ASP A 76  ? 0.39190 0.38260 0.43880 -0.12560 0.16840  -0.04090 70  ASP A N   
504  C CA  . ASP A 76  ? 0.41050 0.41160 0.47840 -0.12010 0.17120  -0.04610 70  ASP A CA  
505  C C   . ASP A 76  ? 0.39180 0.40600 0.46820 -0.11550 0.15960  -0.04930 70  ASP A C   
506  O O   . ASP A 76  ? 0.39100 0.40700 0.45960 -0.11650 0.14980  -0.04810 70  ASP A O   
507  C CB  . ASP A 76  ? 0.44340 0.43180 0.49580 -0.12120 0.18510  -0.04790 70  ASP A CB  
508  C CG  . ASP A 76  ? 0.45730 0.43390 0.47630 -0.12390 0.18540  -0.04890 70  ASP A CG  
509  O OD1 . ASP A 76  ? 0.48140 0.46300 0.49370 -0.12370 0.17460  -0.04870 70  ASP A OD1 
510  O OD2 . ASP A 76  ? 0.55630 0.51790 0.55480 -0.12660 0.19640  -0.04990 70  ASP A OD2 
511  N N   . ASP A 77  ? 0.38730 0.41040 0.48080 -0.11010 0.16070  -0.05310 71  ASP A N   
512  C CA  . ASP A 77  ? 0.33440 0.37100 0.43950 -0.10460 0.14970  -0.05570 71  ASP A CA  
513  C C   . ASP A 77  ? 0.35900 0.38960 0.43970 -0.10580 0.14720  -0.05700 71  ASP A C   
514  O O   . ASP A 77  ? 0.33000 0.36850 0.41270 -0.10390 0.13600  -0.05750 71  ASP A O   
515  C CB  . ASP A 77  ? 0.33720 0.38220 0.46380 -0.09880 0.15240  -0.05790 71  ASP A CB  
516  C CG  . ASP A 77  ? 0.42700 0.48240 0.58180 -0.09720 0.15000  -0.05620 71  ASP A CG  
517  O OD1 . ASP A 77  ? 0.42880 0.48310 0.58500 -0.10080 0.14800  -0.05400 71  ASP A OD1 
518  O OD2 . ASP A 77  ? 0.47480 0.53900 0.65010 -0.09250 0.14990  -0.05680 71  ASP A OD2 
519  N N   . ALA A 78  ? 0.36160 0.37790 0.41860 -0.10910 0.15730  -0.05800 72  ALA A N   
520  C CA  . ALA A 78  ? 0.36900 0.37830 0.39980 -0.11160 0.15460  -0.05900 72  ALA A CA  
521  C C   . ALA A 78  ? 0.37510 0.38080 0.39040 -0.11680 0.14690  -0.05440 72  ALA A C   
522  O O   . ALA A 78  ? 0.37210 0.38050 0.38040 -0.11410 0.13460  -0.05420 72  ALA A O   
523  C CB  . ALA A 78  ? 0.37640 0.36820 0.38110 -0.11540 0.16650  -0.06070 72  ALA A CB  
524  N N   . ASP A 79  ? 0.36800 0.36610 0.37890 -0.12120 0.15020  -0.04970 73  ASP A N   
525  C CA  . ASP A 79  ? 0.41590 0.40970 0.41650 -0.12270 0.13890  -0.04370 73  ASP A CA  
526  C C   . ASP A 79  ? 0.34770 0.35660 0.37150 -0.11650 0.12440  -0.04460 73  ASP A C   
527  O O   . ASP A 79  ? 0.33620 0.34340 0.35070 -0.11390 0.11110  -0.04160 73  ASP A O   
528  C CB  . ASP A 79  ? 0.39790 0.38310 0.39730 -0.12820 0.14690  -0.03880 73  ASP A CB  
529  C CG  . ASP A 79  ? 0.46950 0.43560 0.43850 -0.13450 0.15910  -0.03600 73  ASP A CG  
530  O OD1 . ASP A 79  ? 0.49600 0.45260 0.43750 -0.13590 0.15780  -0.03630 73  ASP A OD1 
531  O OD2 . ASP A 79  ? 0.42510 0.38500 0.39730 -0.13590 0.16710  -0.03360 73  ASP A OD2 
532  N N   . ILE A 80  ? 0.34900 0.37200 0.40330 -0.11480 0.12690  -0.04820 74  ILE A N   
533  C CA  . ILE A 80  ? 0.34760 0.38330 0.42080 -0.10980 0.11350  -0.04930 74  ILE A CA  
534  C C   . ILE A 80  ? 0.33120 0.37290 0.40170 -0.10370 0.10490  -0.05220 74  ILE A C   
535  O O   . ILE A 80  ? 0.25870 0.30310 0.32900 -0.09970 0.09210  -0.05130 74  ILE A O   
536  C CB  . ILE A 80  ? 0.30770 0.35510 0.41010 -0.10730 0.11420  -0.05140 74  ILE A CB  
537  C CG1 . ILE A 80  ? 0.32060 0.36170 0.42590 -0.11170 0.11820  -0.04800 74  ILE A CG1 
538  C CG2 . ILE A 80  ? 0.29410 0.35470 0.41340 -0.10200 0.10040  -0.05360 74  ILE A CG2 
539  C CD1 . ILE A 80  ? 0.35580 0.40490 0.48460 -0.10920 0.12090  -0.04930 74  ILE A CD1 
540  N N   . ALA A 81  ? 0.29950 0.34230 0.36800 -0.10310 0.11290  -0.05560 75  ALA A N   
541  C CA  . ALA A 81  ? 0.28050 0.32800 0.34610 -0.09760 0.10570  -0.05820 75  ALA A CA  
542  C C   . ALA A 81  ? 0.28290 0.31930 0.32240 -0.09750 0.09630  -0.05480 75  ALA A C   
543  O O   . ALA A 81  ? 0.31080 0.35180 0.35200 -0.09240 0.08500  -0.05500 75  ALA A O   
544  C CB  . ALA A 81  ? 0.31790 0.36630 0.38500 -0.09760 0.11760  -0.06260 75  ALA A CB  
545  N N   . LEU A 82  ? 0.29360 0.31530 0.30980 -0.10320 0.10030  -0.05100 76  LEU A N   
546  C CA  . LEU A 82  ? 0.31230 0.32420 0.30580 -0.10340 0.08960  -0.04640 76  LEU A CA  
547  C C   . LEU A 82  ? 0.29950 0.31490 0.30270 -0.10010 0.07740  -0.04230 76  LEU A C   
548  O O   . LEU A 82  ? 0.31110 0.32540 0.30830 -0.09680 0.06620  -0.04000 76  LEU A O   
549  C CB  . LEU A 82  ? 0.33940 0.33440 0.30520 -0.11060 0.09580  -0.04200 76  LEU A CB  
550  C CG  . LEU A 82  ? 0.36150 0.34740 0.30260 -0.11100 0.08480  -0.03830 76  LEU A CG  
551  C CD1 . LEU A 82  ? 0.40920 0.39710 0.34480 -0.10950 0.08550  -0.04440 76  LEU A CD1 
552  C CD2 . LEU A 82  ? 0.38140 0.34980 0.29270 -0.11840 0.08740  -0.03200 76  LEU A CD2 
553  N N   . MET A 83  ? 0.29260 0.31090 0.31060 -0.10140 0.08000  -0.04130 77  MET A N   
554  C CA  . MET A 83  ? 0.29630 0.31720 0.32460 -0.09870 0.07010  -0.03870 77  MET A CA  
555  C C   . MET A 83  ? 0.29690 0.32960 0.34050 -0.09200 0.06180  -0.04280 77  MET A C   
556  O O   . MET A 83  ? 0.34790 0.38000 0.39450 -0.08900 0.05280  -0.04070 77  MET A O   
557  C CB  . MET A 83  ? 0.30730 0.33000 0.35110 -0.10190 0.07520  -0.03850 77  MET A CB  
558  C CG  . MET A 83  ? 0.31950 0.33020 0.35120 -0.10820 0.08350  -0.03350 77  MET A CG  
559  S SD  . MET A 83  ? 0.36500 0.37870 0.41890 -0.11150 0.08760  -0.03360 77  MET A SD  
560  C CE  . MET A 83  ? 0.35570 0.35350 0.39150 -0.11870 0.09930  -0.02720 77  MET A CE  
561  N N   . CYS A 84  ? 0.28270 0.32530 0.33670 -0.08960 0.06540  -0.04830 78  CYS A N   
562  C CA  . CYS A 84  ? 0.30740 0.36050 0.37410 -0.08320 0.05800  -0.05170 78  CYS A CA  
563  C C   . CYS A 84  ? 0.28070 0.33210 0.33610 -0.07950 0.05380  -0.05210 78  CYS A C   
564  O O   . CYS A 84  ? 0.32710 0.38710 0.39260 -0.07420 0.05030  -0.05530 78  CYS A O   
565  C CB  . CYS A 84  ? 0.27060 0.33680 0.35830 -0.08200 0.06300  -0.05660 78  CYS A CB  
566  S SG  . CYS A 84  ? 0.30900 0.38030 0.41540 -0.08640 0.06680  -0.05700 78  CYS A SG  
567  N N   . ALA A 85  ? 0.29320 0.33350 0.32770 -0.08250 0.05390  -0.04890 79  ALA A N   
568  C CA  . ALA A 85  ? 0.34190 0.38060 0.36560 -0.08090 0.05270  -0.05060 79  ALA A CA  
569  C C   . ALA A 85  ? 0.36900 0.40370 0.38530 -0.07790 0.04090  -0.04690 79  ALA A C   
570  O O   . ALA A 85  ? 0.34480 0.37490 0.35990 -0.07810 0.03480  -0.04160 79  ALA A O   
571  C CB  . ALA A 85  ? 0.27850 0.30680 0.28190 -0.08730 0.06140  -0.05060 79  ALA A CB  
572  N N   . SER A 86  ? 0.35250 0.38960 0.36690 -0.07480 0.03850  -0.04970 80  SER A N   
573  C CA  . SER A 86  ? 0.31310 0.34450 0.31600 -0.07410 0.02950  -0.04670 80  SER A CA  
574  C C   . SER A 86  ? 0.30440 0.33040 0.29080 -0.07830 0.03490  -0.05000 80  SER A C   
575  O O   . SER A 86  ? 0.28980 0.32010 0.28000 -0.07550 0.03600  -0.05480 80  SER A O   
576  C CB  . SER A 86  ? 0.29300 0.33190 0.31050 -0.06650 0.02240  -0.04790 80  SER A CB  
577  O OG  . SER A 86  ? 0.32000 0.36370 0.35260 -0.06280 0.02020  -0.04690 80  SER A OG  
578  N N   . HIS A 87  ? 0.32690 0.34250 0.29410 -0.08540 0.03920  -0.04780 81  HIS A N   
579  C CA  . HIS A 87  ? 0.32830 0.33690 0.27800 -0.09050 0.04730  -0.05210 81  HIS A CA  
580  C C   . HIS A 87  ? 0.33250 0.33420 0.26490 -0.09250 0.03810  -0.05100 81  HIS A C   
581  O O   . HIS A 87  ? 0.29740 0.29920 0.23140 -0.09040 0.02540  -0.04540 81  HIS A O   
582  C CB  . HIS A 87  ? 0.33600 0.33470 0.27000 -0.09780 0.05690  -0.05040 81  HIS A CB  
583  C CG  . HIS A 87  ? 0.35360 0.34160 0.26970 -0.10210 0.04900  -0.04190 81  HIS A CG  
584  N ND1 . HIS A 87  ? 0.35730 0.33500 0.24970 -0.10630 0.04060  -0.03830 81  HIS A ND1 
585  C CD2 . HIS A 87  ? 0.35830 0.34420 0.27730 -0.10320 0.04840  -0.03590 81  HIS A CD2 
586  C CE1 . HIS A 87  ? 0.37240 0.34240 0.25420 -0.10940 0.03470  -0.02970 81  HIS A CE1 
587  N NE2 . HIS A 87  ? 0.38300 0.35740 0.28060 -0.10750 0.04000  -0.02820 81  HIS A NE2 
588  N N   . SER A 88  ? 0.35550 0.35120 0.27310 -0.09660 0.04480  -0.05660 82  SER A N   
589  C CA  . SER A 88  ? 0.35590 0.34560 0.25800 -0.09910 0.03660  -0.05730 82  SER A CA  
590  C C   . SER A 88  ? 0.37750 0.35220 0.24880 -0.10770 0.03050  -0.05180 82  SER A C   
591  O O   . SER A 88  ? 0.39020 0.35810 0.24450 -0.11180 0.02390  -0.05280 82  SER A O   
592  C CB  . SER A 88  ? 0.36710 0.35610 0.26700 -0.10000 0.04690  -0.06670 82  SER A CB  
593  O OG  . SER A 88  ? 0.33920 0.34210 0.26710 -0.09160 0.04900  -0.07040 82  SER A OG  
594  N N   . SER A 89  ? 0.38660 0.35590 0.25000 -0.11090 0.03250  -0.04590 83  SER A N   
595  C CA  . SER A 89  ? 0.38450 0.33840 0.21660 -0.11940 0.02790  -0.03970 83  SER A CA  
596  C C   . SER A 89  ? 0.44120 0.38180 0.24390 -0.12770 0.03700  -0.04610 83  SER A C   
597  O O   . SER A 89  ? 0.47850 0.40660 0.25220 -0.13500 0.02920  -0.04300 83  SER A O   
598  C CB  . SER A 89  ? 0.39300 0.34600 0.22180 -0.11910 0.00870  -0.03140 83  SER A CB  
599  O OG  . SER A 89  ? 0.43290 0.39860 0.29200 -0.11040 0.00180  -0.02790 83  SER A OG  
600  N N   . GLU A 90  ? 0.43490 0.37740 0.24430 -0.12710 0.05370  -0.05490 84  GLU A N   
601  C CA  . GLU A 90  ? 0.46680 0.39430 0.24760 -0.13550 0.06610  -0.06100 84  GLU A CA  
602  C C   . GLU A 90  ? 0.52030 0.43330 0.27530 -0.14290 0.07080  -0.05510 84  GLU A C   
603  O O   . GLU A 90  ? 0.49770 0.41480 0.26410 -0.14040 0.06910  -0.04800 84  GLU A O   
604  C CB  . GLU A 90  ? 0.42620 0.35920 0.22440 -0.13260 0.08460  -0.07060 84  GLU A CB  
605  C CG  . GLU A 90  ? 0.50740 0.45110 0.32450 -0.12670 0.08090  -0.07670 84  GLU A CG  
606  C CD  . GLU A 90  ? 0.49920 0.45580 0.34760 -0.11980 0.09440  -0.08250 84  GLU A CD  
607  O OE1 . GLU A 90  ? 0.54010 0.49580 0.39360 -0.12080 0.10810  -0.08300 84  GLU A OE1 
608  O OE2 . GLU A 90  ? 0.46690 0.43410 0.33510 -0.11340 0.09100  -0.08600 84  GLU A OE2 
609  N N   . ASP A 91  ? 0.53250 0.42700 0.25090 -0.15260 0.07730  -0.05830 85  ASP A N   
610  C CA  . ASP A 91  ? 0.53850 0.41690 0.22810 -0.16030 0.08260  -0.05240 85  ASP A CA  
611  C C   . ASP A 91  ? 0.55740 0.44000 0.26630 -0.15750 0.09930  -0.05240 85  ASP A C   
612  O O   . ASP A 91  ? 0.50900 0.38540 0.20940 -0.16000 0.09960  -0.04430 85  ASP A O   
613  C CB  . ASP A 91  ? 0.63000 0.48800 0.28360 -0.16950 0.08890  -0.05680 85  ASP A CB  
614  C CG  . ASP A 91  ? 0.70970 0.56110 0.34100 -0.17390 0.06900  -0.05350 85  ASP A CG  
615  O OD1 . ASP A 91  ? 0.68820 0.54880 0.32520 -0.17180 0.05100  -0.04790 85  ASP A OD1 
616  O OD2 . ASP A 91  ? 0.70990 0.54730 0.31990 -0.17950 0.07100  -0.05650 85  ASP A OD2 
617  N N   . ARG A 92  ? 0.52330 0.41730 0.26040 -0.15210 0.11250  -0.06060 86  ARG A N   
618  C CA  . ARG A 92  ? 0.52730 0.42650 0.28570 -0.14980 0.12800  -0.06080 86  ARG A CA  
619  C C   . ARG A 92  ? 0.50920 0.42430 0.29800 -0.14250 0.11750  -0.05390 86  ARG A C   
620  O O   . ARG A 92  ? 0.56020 0.47610 0.35920 -0.14270 0.12580  -0.05070 86  ARG A O   
621  C CB  . ARG A 92  ? 0.50240 0.40920 0.28520 -0.14570 0.14350  -0.07040 86  ARG A CB  
622  C CG  . ARG A 92  ? 0.48820 0.41470 0.30210 -0.13710 0.13610  -0.07410 86  ARG A CG  
623  C CD  . ARG A 92  ? 0.46490 0.39750 0.30370 -0.13230 0.14900  -0.08180 86  ARG A CD  
624  N NE  . ARG A 92  ? 0.46390 0.41040 0.32100 -0.12620 0.14210  -0.08570 86  ARG A NE  
625  C CZ  . ARG A 92  ? 0.49200 0.44690 0.37630 -0.11970 0.14770  -0.09030 86  ARG A CZ  
626  N NH1 . ARG A 92  ? 0.48080 0.43300 0.37940 -0.11800 0.15980  -0.09150 86  ARG A NH1 
627  N NH2 . ARG A 92  ? 0.52360 0.48940 0.42110 -0.11440 0.14060  -0.09300 86  ARG A NH2 
628  N N   . HIS A 93  ? 0.48820 0.41510 0.29170 -0.13640 0.10020  -0.05180 87  HIS A N   
629  C CA  . HIS A 93  ? 0.45870 0.39740 0.28620 -0.13040 0.08980  -0.04500 87  HIS A CA  
630  C C   . HIS A 93  ? 0.46680 0.39420 0.27370 -0.13490 0.08140  -0.03470 87  HIS A C   
631  O O   . HIS A 93  ? 0.46560 0.39590 0.28540 -0.13340 0.08210  -0.02930 87  HIS A O   
632  C CB  . HIS A 93  ? 0.45130 0.40380 0.29920 -0.12280 0.07540  -0.04570 87  HIS A CB  
633  C CG  . HIS A 93  ? 0.42270 0.38690 0.29220 -0.11760 0.08220  -0.05460 87  HIS A CG  
634  N ND1 . HIS A 93  ? 0.40920 0.37570 0.27740 -0.11550 0.07650  -0.05900 87  HIS A ND1 
635  C CD2 . HIS A 93  ? 0.38380 0.35820 0.27800 -0.11400 0.09390  -0.05930 87  HIS A CD2 
636  C CE1 . HIS A 93  ? 0.40180 0.37900 0.29230 -0.11060 0.08490  -0.06580 87  HIS A CE1 
637  N NE2 . HIS A 93  ? 0.37030 0.35280 0.27720 -0.10960 0.09510  -0.06580 87  HIS A NE2 
638  N N   . ILE A 94  ? 0.50050 0.41500 0.27580 -0.14070 0.07300  -0.03140 88  ILE A N   
639  C CA  . ILE A 94  ? 0.53890 0.44130 0.29170 -0.14560 0.06470  -0.02040 88  ILE A CA  
640  C C   . ILE A 94  ? 0.54090 0.43160 0.28040 -0.15120 0.08070  -0.01850 88  ILE A C   
641  O O   . ILE A 94  ? 0.51710 0.40550 0.25910 -0.15140 0.07880  -0.00990 88  ILE A O   
642  C CB  . ILE A 94  ? 0.56720 0.45700 0.28600 -0.15200 0.05300  -0.01800 88  ILE A CB  
643  C CG1 . ILE A 94  ? 0.57710 0.47820 0.31030 -0.14710 0.04020  -0.02170 88  ILE A CG1 
644  C CG2 . ILE A 94  ? 0.60020 0.48090 0.30180 -0.15550 0.04010  -0.00460 88  ILE A CG2 
645  C CD1 . ILE A 94  ? 0.52770 0.44300 0.29150 -0.13870 0.02710  -0.01540 88  ILE A CD1 
646  N N   . ALA A 95  ? 0.57620 0.45840 0.30120 -0.15600 0.09760  -0.02650 89  ALA A N   
647  C CA  . ALA A 95  ? 0.59430 0.46360 0.30530 -0.16180 0.11490  -0.02510 89  ALA A CA  
648  C C   . ALA A 95  ? 0.55850 0.44040 0.30530 -0.15650 0.12250  -0.02420 89  ALA A C   
649  O O   . ALA A 95  ? 0.52860 0.40300 0.27040 -0.15950 0.12780  -0.01750 89  ALA A O   
650  C CB  . ALA A 95  ? 0.57260 0.43110 0.26580 -0.16720 0.13330  -0.03500 89  ALA A CB  
651  N N   . ARG A 96  ? 0.53780 0.43850 0.32050 -0.14900 0.12290  -0.03060 90  ARG A N   
652  C CA  . ARG A 96  ? 0.47880 0.39170 0.29530 -0.14480 0.12850  -0.03000 90  ARG A CA  
653  C C   . ARG A 96  ? 0.45360 0.37040 0.27930 -0.14180 0.11400  -0.02100 90  ARG A C   
654  O O   . ARG A 96  ? 0.46110 0.37940 0.30120 -0.14190 0.11930  -0.01760 90  ARG A O   
655  C CB  . ARG A 96  ? 0.48500 0.41660 0.33610 -0.13780 0.13110  -0.03850 90  ARG A CB  
656  C CG  . ARG A 96  ? 0.43900 0.38400 0.32560 -0.13410 0.13570  -0.03860 90  ARG A CG  
657  C CD  . ARG A 96  ? 0.41170 0.37280 0.32870 -0.12890 0.14180  -0.04690 90  ARG A CD  
658  N NE  . ARG A 96  ? 0.52020 0.47350 0.42810 -0.13300 0.15970  -0.05250 90  ARG A NE  
659  C CZ  . ARG A 96  ? 0.44810 0.39440 0.35940 -0.13390 0.17150  -0.05240 90  ARG A CZ  
660  N NH1 . ARG A 96  ? 0.40920 0.35710 0.33240 -0.13460 0.17280  -0.04770 90  ARG A NH1 
661  N NH2 . ARG A 96  ? 0.50610 0.44290 0.40970 -0.13380 0.18180  -0.05720 90  ARG A NH2 
662  N N   . THR A 97  ? 0.48610 0.40490 0.30650 -0.13910 0.09620  -0.01720 91  THR A N   
663  C CA  . THR A 97  ? 0.45050 0.37090 0.27870 -0.13660 0.08350  -0.00790 91  THR A CA  
664  C C   . THR A 97  ? 0.50780 0.41160 0.31180 -0.14320 0.08680  0.00150  91  THR A C   
665  O O   . THR A 97  ? 0.52260 0.42690 0.33970 -0.14240 0.08820  0.00690  91  THR A O   
666  C CB  . THR A 97  ? 0.46860 0.39310 0.29550 -0.13280 0.06480  -0.00500 91  THR A CB  
667  O OG1 . THR A 97  ? 0.44630 0.38630 0.29730 -0.12620 0.06270  -0.01330 91  THR A OG1 
668  C CG2 . THR A 97  ? 0.40180 0.32740 0.23920 -0.12990 0.05310  0.00490  91  THR A CG2 
669  N N   . ARG A 98  ? 0.51890 0.40680 0.28660 -0.15020 0.08930  0.00310  92  ARG A N   
670  C CA  . ARG A 98  ? 0.54580 0.41630 0.28730 -0.15690 0.09340  0.01240  92  ARG A CA  
671  C C   . ARG A 98  ? 0.59740 0.46460 0.34690 -0.15940 0.11400  0.00990  92  ARG A C   
672  O O   . ARG A 98  ? 0.57530 0.43490 0.32230 -0.16170 0.11710  0.01810  92  ARG A O   
673  C CB  . ARG A 98  ? 0.58850 0.44170 0.28620 -0.16460 0.09090  0.01410  92  ARG A CB  
674  C CG  . ARG A 98  ? 0.60250 0.45880 0.29340 -0.16280 0.06890  0.01820  92  ARG A CG  
675  C CD  . ARG A 98  ? 0.69380 0.53270 0.33960 -0.17160 0.06450  0.01940  92  ARG A CD  
676  N NE  . ARG A 98  ? 0.68540 0.52540 0.32480 -0.17100 0.04130  0.02800  92  ARG A NE  
677  C CZ  . ARG A 98  ? 0.79060 0.62530 0.40670 -0.17530 0.03030  0.02650  92  ARG A CZ  
678  N NH1 . ARG A 98  ? 0.81240 0.63870 0.40590 -0.18090 0.04060  0.01580  92  ARG A NH1 
679  N NH2 . ARG A 98  ? 0.76470 0.60240 0.38160 -0.17400 0.00860  0.03580  92  ARG A NH2 
680  N N   . ALA A 99  ? 0.58440 0.45700 0.34510 -0.15910 0.12850  -0.00100 93  ALA A N   
681  C CA  . ALA A 99  ? 0.53490 0.40640 0.30910 -0.16110 0.14810  -0.00350 93  ALA A CA  
682  C C   . ALA A 99  ? 0.57110 0.45580 0.38140 -0.15620 0.14510  -0.00080 93  ALA A C   
683  O O   . ALA A 99  ? 0.54940 0.42770 0.36260 -0.15930 0.15480  0.00380  93  ALA A O   
684  C CB  . ALA A 99  ? 0.52440 0.40230 0.31080 -0.16040 0.16220  -0.01530 93  ALA A CB  
685  N N   . MET A 100 ? 0.52330 0.42530 0.36050 -0.14900 0.13230  -0.00370 94  MET A N   
686  C CA  . MET A 100 ? 0.53910 0.45290 0.40900 -0.14480 0.12890  -0.00230 94  MET A CA  
687  C C   . MET A 100 ? 0.57280 0.47740 0.43360 -0.14600 0.12050  0.00910  94  MET A C   
688  O O   . MET A 100 ? 0.54000 0.44580 0.41830 -0.14620 0.12480  0.01190  94  MET A O   
689  C CB  . MET A 100 ? 0.47510 0.40730 0.37120 -0.13720 0.11730  -0.00810 94  MET A CB  
690  C CG  . MET A 100 ? 0.44720 0.39030 0.35730 -0.13510 0.12470  -0.01850 94  MET A CG  
691  S SD  . MET A 100 ? 0.42040 0.38190 0.35300 -0.12640 0.10980  -0.02380 94  MET A SD  
692  C CE  . MET A 100 ? 0.35150 0.32210 0.31330 -0.12340 0.10400  -0.02120 94  MET A CE  
693  N N   . LEU A 101 ? 0.52570 0.42150 0.36100 -0.14680 0.10810  0.01600  95  LEU A N   
694  C CA  . LEU A 101 ? 0.55350 0.43900 0.37850 -0.14830 0.10090  0.02850  95  LEU A CA  
695  C C   . LEU A 101 ? 0.59830 0.46830 0.40630 -0.15510 0.11570  0.03360  95  LEU A C   
696  O O   . LEU A 101 ? 0.56280 0.42760 0.37640 -0.15570 0.11580  0.04190  95  LEU A O   
697  C CB  . LEU A 101 ? 0.56100 0.43980 0.36110 -0.14870 0.08470  0.03560  95  LEU A CB  
698  C CG  . LEU A 101 ? 0.55290 0.44520 0.37290 -0.14130 0.06780  0.03460  95  LEU A CG  
699  C CD1 . LEU A 101 ? 0.56950 0.45610 0.36500 -0.14260 0.05340  0.03950  95  LEU A CD1 
700  C CD2 . LEU A 101 ? 0.51700 0.41290 0.36050 -0.13710 0.06180  0.04160  95  LEU A CD2 
701  N N   . SER A 102 ? 0.60400 0.46540 0.39180 -0.16040 0.12950  0.02880  96  SER A N   
702  C CA  . SER A 102 ? 0.60170 0.44720 0.37330 -0.16690 0.14540  0.03370  96  SER A CA  
703  C C   . SER A 102 ? 0.58700 0.44090 0.39290 -0.16580 0.15850  0.03000  96  SER A C   
704  O O   . SER A 102 ? 0.57970 0.42550 0.38580 -0.16700 0.16460  0.03620  96  SER A O   
705  C CB  . SER A 102 ? 0.60260 0.43630 0.34540 -0.17140 0.15670  0.02850  96  SER A CB  
706  O OG  . SER A 102 ? 0.76240 0.58460 0.46810 -0.17490 0.14500  0.03360  96  SER A OG  
707  N N   . LYS A 103 ? 0.56470 0.43680 0.40270 -0.16130 0.16010  0.01950  97  LYS A N   
708  C CA  . LYS A 103 ? 0.58430 0.46610 0.45720 -0.15930 0.16920  0.01560  97  LYS A CA  
709  C C   . LYS A 103 ? 0.57630 0.45930 0.46530 -0.15900 0.16270  0.02260  97  LYS A C   
710  O O   . LYS A 103 ? 0.53800 0.42170 0.44490 -0.15840 0.16980  0.02330  97  LYS A O   
711  C CB  . LYS A 103 ? 0.56290 0.46410 0.46590 -0.15470 0.16970  0.00410  97  LYS A CB  
712  C CG  . LYS A 103 ? 0.57610 0.47600 0.47180 -0.15390 0.17990  -0.00340 97  LYS A CG  
713  C CD  . LYS A 103 ? 0.53640 0.45530 0.46050 -0.14880 0.17820  -0.01310 97  LYS A CD  
714  C CE  . LYS A 103 ? 0.54050 0.45730 0.46310 -0.14730 0.19000  -0.01990 97  LYS A CE  
715  N NZ  . LYS A 103 ? 0.53270 0.46740 0.48180 -0.14170 0.18690  -0.02810 97  LYS A NZ  
716  N N   . ILE A 104 ? 0.56740 0.53170 0.38800 -0.19930 0.05190  0.03300  98  ILE A N   
717  C CA  . ILE A 104 ? 0.56570 0.50170 0.38720 -0.19710 0.04190  0.04720  98  ILE A CA  
718  C C   . ILE A 104 ? 0.62700 0.53250 0.42210 -0.20610 0.02580  0.06570  98  ILE A C   
719  O O   . ILE A 104 ? 0.60810 0.48520 0.40410 -0.20290 0.01320  0.07790  98  ILE A O   
720  C CB  . ILE A 104 ? 0.53810 0.46910 0.38620 -0.17730 0.03910  0.04790  98  ILE A CB  
721  C CG1 . ILE A 104 ? 0.55100 0.47400 0.39810 -0.16790 0.03050  0.05470  98  ILE A CG1 
722  C CG2 . ILE A 104 ? 0.47470 0.43450 0.34670 -0.16880 0.05320  0.03040  98  ILE A CG2 
723  C CD1 . ILE A 104 ? 0.41760 0.33240 0.28710 -0.15240 0.02520  0.05730  98  ILE A CD1 
724  N N   . LYS A 105 ? 0.55510 0.46540 0.32720 -0.21740 0.02440  0.06710  99  LYS A N   
725  C CA  . LYS A 105 ? 0.57680 0.45970 0.31960 -0.22880 0.00830  0.08420  99  LYS A CA  
726  C C   . LYS A 105 ? 0.68660 0.54150 0.43480 -0.21330 -0.00990 0.09720  99  LYS A C   
727  O O   . LYS A 105 ? 0.68130 0.50350 0.41600 -0.21610 -0.02780 0.11200  99  LYS A O   
728  C CB  . LYS A 105 ? 0.70530 0.57070 0.43040 -0.24590 0.00470  0.09230  99  LYS A CB  
729  C CG  . LYS A 105 ? 0.71210 0.60590 0.43420 -0.26240 0.02260  0.07780  99  LYS A CG  
730  C CD  . LYS A 105 ? 0.80260 0.67720 0.51180 -0.27840 0.01960  0.08600  99  LYS A CD  
731  C CE  . LYS A 105 ? 0.83010 0.68310 0.56330 -0.26350 0.01370  0.09100  99  LYS A CE  
732  N NZ  . LYS A 105 ? 0.70650 0.58520 0.47540 -0.24760 0.02790  0.07400  99  LYS A NZ  
733  N N   . ALA A 106 ? 0.55230 0.41960 0.32090 -0.19720 -0.00660 0.09060  100 ALA A N   
734  C CA  . ALA A 106 ? 0.59690 0.44460 0.37280 -0.18320 -0.02270 0.09930  100 ALA A CA  
735  C C   . ALA A 106 ? 0.64760 0.50290 0.41010 -0.18480 -0.02550 0.09980  100 ALA A C   
736  O O   . ALA A 106 ? 0.61930 0.49530 0.36860 -0.19650 -0.01480 0.09270  100 ALA A O   
737  C CB  . ALA A 106 ? 0.52360 0.37970 0.33260 -0.16630 -0.01700 0.09180  100 ALA A CB  
738  N N   . GLU A 107 ? 0.62130 0.46090 0.38800 -0.17370 -0.04100 0.10690  101 GLU A N   
739  C CA  . GLU A 107 ? 0.64190 0.48960 0.39820 -0.17410 -0.04410 0.10670  101 GLU A CA  
740  C C   . GLU A 107 ? 0.62040 0.46870 0.40000 -0.15790 -0.04880 0.10490  101 GLU A C   
741  O O   . GLU A 107 ? 0.57900 0.42430 0.38640 -0.14370 -0.05130 0.10110  101 GLU A O   
742  C CB  . GLU A 107 ? 0.70620 0.53110 0.43250 -0.18210 -0.06410 0.11980  101 GLU A CB  
743  C CG  . GLU A 107 ? 0.79150 0.57980 0.51960 -0.17240 -0.08970 0.13220  101 GLU A CG  
744  C CD  . GLU A 107 ? 0.98950 0.75250 0.68620 -0.18530 -0.10610 0.14480  101 GLU A CD  
745  O OE1 . GLU A 107 ? 0.95840 0.73460 0.63060 -0.20220 -0.09780 0.14480  101 GLU A OE1 
746  O OE2 . GLU A 107 ? 1.03320 0.76350 0.73060 -0.17910 -0.12790 0.15390  101 GLU A OE2 
747  N N   . GLU A 108 ? 0.59850 0.46270 0.37950 -0.15360 -0.04920 0.09830  102 GLU A N   
748  C CA  . GLU A 108 ? 0.55710 0.43710 0.37330 -0.13380 -0.04970 0.08620  102 GLU A CA  
749  C C   . GLU A 108 ? 0.58080 0.44460 0.41360 -0.11840 -0.07050 0.08920  102 GLU A C   
750  O O   . GLU A 108 ? 0.54100 0.41870 0.40690 -0.10380 -0.06800 0.07870  102 GLU A O   
751  C CB  . GLU A 108 ? 0.56890 0.46560 0.38180 -0.13440 -0.04860 0.07890  102 GLU A CB  
752  C CG  . GLU A 108 ? 0.64920 0.56620 0.45140 -0.14700 -0.02950 0.07050  102 GLU A CG  
753  C CD  . GLU A 108 ? 0.74190 0.67480 0.54180 -0.14760 -0.03010 0.06130  102 GLU A CD  
754  O OE1 . GLU A 108 ? 0.71880 0.65270 0.53570 -0.13560 -0.04040 0.05820  102 GLU A OE1 
755  O OE2 . GLU A 108 ? 0.68220 0.62980 0.46500 -0.16060 -0.01990 0.05480  102 GLU A OE2 
756  N N   . ALA A 109 ? 0.61450 0.44930 0.42440 -0.12190 -0.09230 0.10240  103 ALA A N   
757  C CA  . ALA A 109 ? 0.60390 0.42170 0.43220 -0.10520 -0.11580 0.10240  103 ALA A CA  
758  C C   . ALA A 109 ? 0.60820 0.42330 0.46160 -0.09730 -0.11240 0.09800  103 ALA A C   
759  O O   . ALA A 109 ? 0.55370 0.36940 0.43610 -0.07970 -0.12630 0.08920  103 ALA A O   
760  C CB  . ALA A 109 ? 0.61960 0.39940 0.41390 -0.11140 -0.14290 0.11980  103 ALA A CB  
761  N N   . ASP A 110 ? 0.53850 0.35410 0.38320 -0.10960 -0.09450 0.10130  104 ASP A N   
762  C CA  . ASP A 110 ? 0.59380 0.40970 0.46230 -0.10260 -0.09020 0.09570  104 ASP A CA  
763  C C   . ASP A 110 ? 0.56660 0.41780 0.47130 -0.08880 -0.07530 0.07850  104 ASP A C   
764  O O   . ASP A 110 ? 0.50560 0.36200 0.43630 -0.07770 -0.07710 0.07030  104 ASP A O   
765  C CB  . ASP A 110 ? 0.59600 0.40380 0.44420 -0.12120 -0.07600 0.10320  104 ASP A CB  
766  C CG  . ASP A 110 ? 0.67450 0.44600 0.48560 -0.13790 -0.09090 0.12120  104 ASP A CG  
767  O OD1 . ASP A 110 ? 0.65820 0.39910 0.46960 -0.13050 -0.11630 0.12800  104 ASP A OD1 
768  O OD2 . ASP A 110 ? 0.69120 0.47560 0.48090 -0.15330 -0.07650 0.12120  104 ASP A OD2 
769  N N   . LEU A 111 ? 0.50980 0.38460 0.41580 -0.09020 -0.06190 0.07290  105 LEU A N   
770  C CA  . LEU A 111 ? 0.48160 0.38580 0.41610 -0.08090 -0.04860 0.05980  105 LEU A CA  
771  C C   . LEU A 111 ? 0.48920 0.40440 0.45210 -0.06560 -0.06110 0.04970  105 LEU A C   
772  O O   . LEU A 111 ? 0.48690 0.39460 0.44900 -0.06080 -0.07860 0.04960  105 LEU A O   
773  C CB  . LEU A 111 ? 0.47710 0.39700 0.40470 -0.08690 -0.03590 0.05720  105 LEU A CB  
774  C CG  . LEU A 111 ? 0.53490 0.45580 0.44450 -0.09940 -0.02020 0.05950  105 LEU A CG  
775  C CD1 . LEU A 111 ? 0.50720 0.44250 0.41350 -0.10330 -0.01130 0.05370  105 LEU A CD1 
776  C CD2 . LEU A 111 ? 0.42150 0.35090 0.34490 -0.09670 -0.00780 0.05510  105 LEU A CD2 
777  N N   . ARG A 112 ? 0.41720 0.35390 0.40560 -0.05830 -0.05210 0.03920  106 ARG A N   
778  C CA  . ARG A 112 ? 0.41570 0.37240 0.43400 -0.04570 -0.06050 0.02530  106 ARG A CA  
779  C C   . ARG A 112 ? 0.39260 0.38080 0.42480 -0.04720 -0.04570 0.01680  106 ARG A C   
780  O O   . ARG A 112 ? 0.35460 0.36840 0.41270 -0.04030 -0.04670 0.00310  106 ARG A O   
781  C CB  . ARG A 112 ? 0.39730 0.35650 0.43520 -0.03690 -0.06470 0.01750  106 ARG A CB  
782  C CG  . ARG A 112 ? 0.50340 0.42980 0.53580 -0.03240 -0.08720 0.02250  106 ARG A CG  
783  C CD  . ARG A 112 ? 0.50000 0.41800 0.53360 -0.02540 -0.10900 0.02080  106 ARG A CD  
784  N NE  . ARG A 112 ? 0.63920 0.51610 0.65850 -0.02380 -0.13300 0.03090  106 ARG A NE  
785  C CZ  . ARG A 112 ? 0.70570 0.55120 0.69030 -0.03390 -0.14290 0.04870  106 ARG A CZ  
786  N NH1 . ARG A 112 ? 0.60090 0.45500 0.56550 -0.04380 -0.13240 0.05500  106 ARG A NH1 
787  N NH2 . ARG A 112 ? 0.70790 0.51190 0.67630 -0.03510 -0.16470 0.06050  106 ARG A NH2 
788  N N   . CYS A 113 ? 0.38200 0.36940 0.39810 -0.05710 -0.03240 0.02360  107 CYS A N   
789  C CA  . CYS A 113 ? 0.32300 0.33140 0.34760 -0.06120 -0.02170 0.01860  107 CYS A CA  
790  C C   . CYS A 113 ? 0.39870 0.40570 0.41870 -0.06380 -0.02930 0.01770  107 CYS A C   
791  O O   . CYS A 113 ? 0.38830 0.37630 0.39190 -0.06400 -0.04060 0.02350  107 CYS A O   
792  C CB  . CYS A 113 ? 0.40980 0.41560 0.42260 -0.06870 -0.00560 0.02470  107 CYS A CB  
793  S SG  . CYS A 113 ? 0.41930 0.40080 0.40400 -0.07560 -0.00340 0.03420  107 CYS A SG  
794  N N   . GLY A 114 ? 0.31140 0.33870 0.34440 -0.06740 -0.02340 0.01050  108 GLY A N   
795  C CA  . GLY A 114 ? 0.32580 0.35690 0.35960 -0.06960 -0.03070 0.00620  108 GLY A CA  
796  C C   . GLY A 114 ? 0.38490 0.41560 0.41130 -0.08040 -0.01860 0.00880  108 GLY A C   
797  O O   . GLY A 114 ? 0.34490 0.37680 0.37100 -0.08540 -0.00580 0.01210  108 GLY A O   
798  N N   . GLY A 115 ? 0.34960 0.37690 0.36950 -0.08350 -0.02410 0.00700  109 GLY A N   
799  C CA  . GLY A 115 ? 0.34210 0.36760 0.35820 -0.09300 -0.01490 0.00680  109 GLY A CA  
800  C C   . GLY A 115 ? 0.35280 0.39730 0.38830 -0.09990 -0.00860 0.00000  109 GLY A C   
801  O O   . GLY A 115 ? 0.34240 0.40820 0.39580 -0.09780 -0.01150 -0.00800 109 GLY A O   
802  N N   . HIS A 116 ? 0.32170 0.35880 0.35400 -0.10940 -0.00060 0.00190  110 HIS A N   
803  C CA  . HIS A 116 ? 0.33420 0.38360 0.37960 -0.12080 0.00620  -0.00130 110 HIS A CA  
804  C C   . HIS A 116 ? 0.32570 0.35750 0.36530 -0.12960 0.00870  0.00030  110 HIS A C   
805  O O   . HIS A 116 ? 0.31500 0.32810 0.34190 -0.12520 0.00760  0.00320  110 HIS A O   
806  C CB  . HIS A 116 ? 0.31330 0.36770 0.36000 -0.12370 0.01520  0.00490  110 HIS A CB  
807  C CG  . HIS A 116 ? 0.34100 0.37240 0.37190 -0.11970 0.01870  0.01540  110 HIS A CG  
808  N ND1 . HIS A 116 ? 0.37630 0.38700 0.39880 -0.12570 0.02150  0.02090  110 HIS A ND1 
809  C CD2 . HIS A 116 ? 0.36540 0.39110 0.38890 -0.10970 0.01840  0.01940  110 HIS A CD2 
810  C CE1 . HIS A 116 ? 0.41790 0.41450 0.43010 -0.11840 0.02290  0.02650  110 HIS A CE1 
811  N NE2 . HIS A 116 ? 0.36600 0.37230 0.37810 -0.10980 0.02220  0.02590  110 HIS A NE2 
812  N N   . PRO A 117 ? 0.35810 0.39640 0.40790 -0.14290 0.01210  -0.00300 111 PRO A N   
813  C CA  . PRO A 117 ? 0.36330 0.37980 0.40930 -0.15130 0.01250  -0.00170 111 PRO A CA  
814  C C   . PRO A 117 ? 0.36730 0.35820 0.40030 -0.14820 0.01510  0.00900  111 PRO A C   
815  O O   . PRO A 117 ? 0.39980 0.39200 0.42820 -0.14720 0.01980  0.01750  111 PRO A O   
816  C CB  . PRO A 117 ? 0.33740 0.36450 0.39510 -0.16950 0.01700  -0.00360 111 PRO A CB  
817  C CG  . PRO A 117 ? 0.29850 0.36170 0.37060 -0.16860 0.01740  -0.01300 111 PRO A CG  
818  C CD  . PRO A 117 ? 0.31860 0.38510 0.38480 -0.15240 0.01560  -0.00950 111 PRO A CD  
819  N N   . SER A 118 ? 0.41570 0.38620 0.44430 -0.14550 0.01110  0.00600  112 SER A N   
820  C CA  . SER A 118 ? 0.38920 0.33830 0.40870 -0.13900 0.01110  0.01180  112 SER A CA  
821  C C   . SER A 118 ? 0.43990 0.37190 0.45730 -0.14880 0.01240  0.02330  112 SER A C   
822  O O   . SER A 118 ? 0.40270 0.33100 0.42470 -0.16360 0.01240  0.02520  112 SER A O   
823  C CB  . SER A 118 ? 0.40980 0.34560 0.42950 -0.13370 0.00550  0.00100  112 SER A CB  
824  O OG  . SER A 118 ? 0.38680 0.30070 0.40370 -0.12830 0.00290  0.00300  112 SER A OG  
825  N N   . LEU A 119 ? 0.37900 0.30090 0.38740 -0.14180 0.01320  0.03140  113 LEU A N   
826  C CA  . LEU A 119 ? 0.36460 0.26400 0.36570 -0.14930 0.01090  0.04400  113 LEU A CA  
827  C C   . LEU A 119 ? 0.43300 0.29910 0.43610 -0.15180 0.00060  0.04190  113 LEU A C   
828  O O   . LEU A 119 ? 0.47020 0.31340 0.46700 -0.16220 -0.00370 0.05350  113 LEU A O   
829  C CB  . LEU A 119 ? 0.39500 0.29190 0.38710 -0.13780 0.01170  0.05010  113 LEU A CB  
830  C CG  . LEU A 119 ? 0.35660 0.28370 0.34820 -0.13530 0.02040  0.05150  113 LEU A CG  
831  C CD1 . LEU A 119 ? 0.33570 0.25940 0.31900 -0.12630 0.02090  0.05760  113 LEU A CD1 
832  C CD2 . LEU A 119 ? 0.39670 0.34090 0.39020 -0.15000 0.02590  0.05600  113 LEU A CD2 
833  N N   . SER A 120 ? 0.43740 0.30120 0.44910 -0.14210 -0.00420 0.02680  114 SER A N   
834  C CA  . SER A 120 ? 0.43200 0.26760 0.45120 -0.14340 -0.01520 0.01950  114 SER A CA  
835  C C   . SER A 120 ? 0.49560 0.33790 0.52440 -0.15640 -0.01460 0.01260  114 SER A C   
836  O O   . SER A 120 ? 0.41300 0.28240 0.44690 -0.15340 -0.01000 0.00140  114 SER A O   
837  C CB  . SER A 120 ? 0.46540 0.30080 0.49150 -0.12610 -0.02050 0.00190  114 SER A CB  
838  O OG  . SER A 120 ? 0.50460 0.32430 0.54350 -0.12740 -0.03000 -0.01230 114 SER A OG  
839  N N   . GLU A 121 ? 0.52080 0.33660 0.55100 -0.17160 -0.02050 0.01950  115 GLU A N   
840  C CA  . GLU A 121 ? 0.51080 0.33280 0.55290 -0.18420 -0.02020 0.01120  115 GLU A CA  
841  C C   . GLU A 121 ? 0.54840 0.37230 0.60380 -0.17440 -0.02680 -0.01090 115 GLU A C   
842  O O   . GLU A 121 ? 0.49560 0.34400 0.55930 -0.17790 -0.02340 -0.02270 115 GLU A O   
843  C CB  . GLU A 121 ? 0.60120 0.39840 0.64380 -0.19360 -0.02360 0.02120  115 GLU A CB  
844  C CG  . GLU A 121 ? 0.70260 0.52080 0.74000 -0.20680 -0.01230 0.03390  115 GLU A CG  
845  C CD  . GLU A 121 ? 0.95980 0.76780 1.00530 -0.22240 -0.01330 0.03370  115 GLU A CD  
846  O OE1 . GLU A 121 ? 0.94280 0.75530 1.00540 -0.22520 -0.01610 0.01810  115 GLU A OE1 
847  O OE2 . GLU A 121 ? 0.98700 0.78280 1.02080 -0.23290 -0.01160 0.04890  115 GLU A OE2 
848  N N   . MET A 122 ? 0.53910 0.34190 0.59770 -0.16050 -0.03660 -0.01920 116 MET A N   
849  C CA  . MET A 122 ? 0.54600 0.35680 0.61840 -0.15060 -0.04200 -0.04370 116 MET A CA  
850  C C   . MET A 122 ? 0.52440 0.37650 0.59200 -0.14210 -0.03220 -0.05330 116 MET A C   
851  O O   . MET A 122 ? 0.47020 0.34100 0.54450 -0.14280 -0.03240 -0.06930 116 MET A O   
852  C CB  . MET A 122 ? 0.56380 0.34890 0.64320 -0.13610 -0.05460 -0.05370 116 MET A CB  
853  C CG  . MET A 122 ? 0.56630 0.36400 0.66180 -0.12640 -0.05980 -0.08260 116 MET A CG  
854  S SD  . MET A 122 ? 0.68050 0.44460 0.79100 -0.10980 -0.07850 -0.09700 116 MET A SD  
855  C CE  . MET A 122 ? 0.67510 0.38640 0.78530 -0.12400 -0.09150 -0.07840 116 MET A CE  
856  N N   . VAL A 123 ? 0.49010 0.35510 0.54470 -0.13490 -0.02490 -0.04330 117 VAL A N   
857  C CA  . VAL A 123 ? 0.45820 0.35650 0.50450 -0.12930 -0.01720 -0.04830 117 VAL A CA  
858  C C   . VAL A 123 ? 0.42890 0.34660 0.47490 -0.13880 -0.01360 -0.04530 117 VAL A C   
859  O O   . VAL A 123 ? 0.45620 0.39530 0.50000 -0.13710 -0.01360 -0.05580 117 VAL A O   
860  C CB  . VAL A 123 ? 0.47680 0.38110 0.51060 -0.12190 -0.01090 -0.03660 117 VAL A CB  
861  C CG1 . VAL A 123 ? 0.38490 0.31800 0.40750 -0.11940 -0.00470 -0.03830 117 VAL A CG1 
862  C CG2 . VAL A 123 ? 0.41290 0.30380 0.44900 -0.11070 -0.01500 -0.04320 117 VAL A CG2 
863  N N   . ASN A 124 ? 0.46250 0.37550 0.50990 -0.14930 -0.01080 -0.03160 118 ASN A N   
864  C CA  . ASN A 124 ? 0.42740 0.36380 0.47850 -0.15730 -0.00760 -0.03140 118 ASN A CA  
865  C C   . ASN A 124 ? 0.43260 0.37330 0.49630 -0.16440 -0.01280 -0.04650 118 ASN A C   
866  O O   . ASN A 124 ? 0.39560 0.36120 0.46170 -0.16410 -0.01350 -0.05430 118 ASN A O   
867  C CB  . ASN A 124 ? 0.44700 0.38250 0.49880 -0.16920 -0.00220 -0.01700 118 ASN A CB  
868  C CG  . ASN A 124 ? 0.43460 0.40280 0.49030 -0.17110 0.00200  -0.01800 118 ASN A CG  
869  O OD1 . ASN A 124 ? 0.44450 0.42700 0.49370 -0.15930 0.00250  -0.01740 118 ASN A OD1 
870  N ND2 . ASN A 124 ? 0.38540 0.36550 0.45280 -0.18640 0.00410  -0.02090 118 ASN A ND2 
871  N N   . ARG A 125 ? 0.45690 0.37230 0.52980 -0.17060 -0.01820 -0.05120 119 ARG A N   
872  C CA  . ARG A 125 ? 0.44520 0.36420 0.53220 -0.17700 -0.02370 -0.06820 119 ARG A CA  
873  C C   . ARG A 125 ? 0.43360 0.37120 0.51840 -0.16460 -0.02700 -0.08600 119 ARG A C   
874  O O   . ARG A 125 ? 0.44630 0.40380 0.53720 -0.16730 -0.02970 -0.09940 119 ARG A O   
875  C CB  . ARG A 125 ? 0.50100 0.38320 0.59870 -0.18550 -0.03130 -0.06990 119 ARG A CB  
876  C CG  . ARG A 125 ? 0.53630 0.39910 0.63340 -0.20510 -0.02890 -0.05190 119 ARG A CG  
877  C CD  . ARG A 125 ? 0.61130 0.44010 0.72230 -0.21070 -0.03850 -0.05440 119 ARG A CD  
878  N NE  . ARG A 125 ? 0.70550 0.50490 0.81520 -0.19870 -0.04900 -0.06390 119 ARG A NE  
879  C CZ  . ARG A 125 ? 0.75840 0.52760 0.85860 -0.19130 -0.05350 -0.05130 119 ARG A CZ  
880  N NH1 . ARG A 125 ? 0.72250 0.48280 0.80990 -0.19810 -0.04730 -0.02790 119 ARG A NH1 
881  N NH2 . ARG A 125 ? 0.76160 0.51410 0.86740 -0.17460 -0.06530 -0.06450 119 ARG A NH2 
882  N N   . SER A 126 ? 0.46300 0.39600 0.53880 -0.15230 -0.02700 -0.08770 120 SER A N   
883  C CA  . SER A 126 ? 0.47410 0.42950 0.54230 -0.14350 -0.02760 -0.10290 120 SER A CA  
884  C C   . SER A 126 ? 0.43880 0.42100 0.49210 -0.14310 -0.02450 -0.09650 120 SER A C   
885  O O   . SER A 126 ? 0.39080 0.39330 0.43990 -0.14310 -0.02810 -0.10870 120 SER A O   
886  C CB  . SER A 126 ? 0.48690 0.43590 0.54840 -0.13280 -0.02590 -0.10460 120 SER A CB  
887  O OG  . SER A 126 ? 0.52420 0.49650 0.57870 -0.12770 -0.02540 -0.12210 120 SER A OG  
888  N N   . TRP A 127 ? 0.40350 0.38530 0.44870 -0.14240 -0.01980 -0.07820 121 TRP A N   
889  C CA  . TRP A 127 ? 0.36710 0.36930 0.40100 -0.14030 -0.02050 -0.07230 121 TRP A CA  
890  C C   . TRP A 127 ? 0.38340 0.40050 0.42940 -0.14650 -0.02560 -0.07980 121 TRP A C   
891  O O   . TRP A 127 ? 0.35190 0.38700 0.38990 -0.14350 -0.03190 -0.08510 121 TRP A O   
892  C CB  . TRP A 127 ? 0.36060 0.35940 0.38980 -0.13790 -0.01560 -0.05470 121 TRP A CB  
893  C CG  . TRP A 127 ? 0.45240 0.44300 0.46800 -0.13100 -0.01110 -0.04710 121 TRP A CG  
894  C CD1 . TRP A 127 ? 0.46280 0.45200 0.46950 -0.12700 -0.01020 -0.05500 121 TRP A CD1 
895  C CD2 . TRP A 127 ? 0.44190 0.42880 0.45300 -0.12760 -0.00640 -0.03250 121 TRP A CD2 
896  N NE1 . TRP A 127 ? 0.44610 0.43060 0.44320 -0.12200 -0.00500 -0.04570 121 TRP A NE1 
897  C CE2 . TRP A 127 ? 0.41700 0.39840 0.41630 -0.12190 -0.00300 -0.03130 121 TRP A CE2 
898  C CE3 . TRP A 127 ? 0.40640 0.39800 0.42380 -0.12940 -0.00450 -0.02290 121 TRP A CE3 
899  C CZ2 . TRP A 127 ? 0.41310 0.39070 0.40650 -0.11760 0.00160  -0.01960 121 TRP A CZ2 
900  C CZ3 . TRP A 127 ? 0.39920 0.38770 0.41040 -0.12440 -0.00010 -0.01190 121 TRP A CZ3 
901  C CH2 . TRP A 127 ? 0.35270 0.33300 0.35190 -0.11850 0.00260  -0.00980 121 TRP A CH2 
902  N N   . ILE A 128 ? 0.39130 0.40120 0.45550 -0.15640 -0.02380 -0.07980 122 ILE A N   
903  C CA  . ILE A 128 ? 0.42720 0.45510 0.50650 -0.16420 -0.02750 -0.08920 122 ILE A CA  
904  C C   . ILE A 128 ? 0.38280 0.41890 0.46550 -0.16400 -0.03460 -0.10800 122 ILE A C   
905  O O   . ILE A 128 ? 0.40750 0.46650 0.49160 -0.16260 -0.04120 -0.11720 122 ILE A O   
906  C CB  . ILE A 128 ? 0.38970 0.40780 0.48570 -0.17950 -0.02230 -0.08520 122 ILE A CB  
907  C CG1 . ILE A 128 ? 0.41690 0.44070 0.51010 -0.18080 -0.01540 -0.07010 122 ILE A CG1 
908  C CG2 . ILE A 128 ? 0.37690 0.41150 0.49250 -0.19090 -0.02580 -0.10090 122 ILE A CG2 
909  C CD1 . ILE A 128 ? 0.44850 0.45670 0.54810 -0.19770 -0.00840 -0.06050 122 ILE A CD1 
910  N N   . LYS A 129 ? 0.39010 0.40900 0.47470 -0.16410 -0.03490 -0.11590 123 LYS A N   
911  C CA  . LYS A 129 ? 0.39970 0.42900 0.48880 -0.16370 -0.04130 -0.13720 123 LYS A CA  
912  C C   . LYS A 129 ? 0.42260 0.47590 0.49010 -0.15530 -0.04520 -0.14070 123 LYS A C   
913  O O   . LYS A 129 ? 0.42970 0.50200 0.49810 -0.15610 -0.05200 -0.15660 123 LYS A O   
914  C CB  . LYS A 129 ? 0.39090 0.39900 0.48710 -0.16200 -0.04210 -0.14740 123 LYS A CB  
915  C CG  . LYS A 129 ? 0.43120 0.45090 0.53820 -0.16270 -0.04890 -0.17360 123 LYS A CG  
916  C CD  . LYS A 129 ? 0.46310 0.46520 0.58070 -0.15800 -0.05180 -0.18870 123 LYS A CD  
917  C CE  . LYS A 129 ? 0.54530 0.56500 0.67160 -0.15530 -0.05800 -0.21420 123 LYS A CE  
918  N NZ  . LYS A 129 ? 0.54540 0.55240 0.68290 -0.14600 -0.06180 -0.22980 123 LYS A NZ  
919  N N   . GLN A 130 ? 0.39590 0.44760 0.44230 -0.14850 -0.04190 -0.12570 124 GLN A N   
920  C CA  . GLN A 130 ? 0.40730 0.47530 0.42740 -0.14370 -0.04590 -0.12540 124 GLN A CA  
921  C C   . GLN A 130 ? 0.40340 0.47890 0.41240 -0.14010 -0.05200 -0.11160 124 GLN A C   
922  O O   . GLN A 130 ? 0.37320 0.45520 0.35610 -0.13690 -0.05740 -0.10590 124 GLN A O   
923  C CB  . GLN A 130 ? 0.40450 0.46560 0.40770 -0.14040 -0.03900 -0.12110 124 GLN A CB  
924  C CG  . GLN A 130 ? 0.43650 0.49230 0.45480 -0.14100 -0.03600 -0.13960 124 GLN A CG  
925  C CD  . GLN A 130 ? 0.50460 0.55470 0.51400 -0.13680 -0.02870 -0.13790 124 GLN A CD  
926  O OE1 . GLN A 130 ? 0.53190 0.56140 0.55120 -0.13370 -0.02500 -0.12860 124 GLN A OE1 
927  N NE2 . GLN A 130 ? 0.41310 0.48390 0.40310 -0.13780 -0.02690 -0.14770 124 GLN A NE2 
928  N N   . ASP A 131 ? 0.38870 0.46430 0.41730 -0.14140 -0.05240 -0.10750 125 ASP A N   
929  C CA  . ASP A 131 ? 0.44570 0.53140 0.47150 -0.13580 -0.06050 -0.09960 125 ASP A CA  
930  C C   . ASP A 131 ? 0.45730 0.53150 0.46140 -0.12900 -0.05970 -0.08160 125 ASP A C   
931  O O   . ASP A 131 ? 0.41600 0.49380 0.40560 -0.12250 -0.07110 -0.07530 125 ASP A O   
932  C CB  . ASP A 131 ? 0.46580 0.57070 0.48490 -0.13290 -0.07540 -0.11040 125 ASP A CB  
933  C CG  . ASP A 131 ? 0.51410 0.63520 0.56030 -0.13930 -0.07780 -0.12990 125 ASP A CG  
934  O OD1 . ASP A 131 ? 0.58000 0.70370 0.65220 -0.14500 -0.07220 -0.13210 125 ASP A OD1 
935  O OD2 . ASP A 131 ? 0.56510 0.69840 0.60580 -0.14020 -0.08520 -0.14370 125 ASP A OD2 
936  N N   . PHE A 132 ? 0.40700 0.46530 0.40900 -0.13030 -0.04790 -0.07340 126 PHE A N   
937  C CA  . PHE A 132 ? 0.40810 0.45560 0.39100 -0.12540 -0.04550 -0.05800 126 PHE A CA  
938  C C   . PHE A 132 ? 0.40640 0.45240 0.40180 -0.12130 -0.04490 -0.04830 126 PHE A C   
939  O O   . PHE A 132 ? 0.39790 0.44370 0.41350 -0.12530 -0.03720 -0.04940 126 PHE A O   
940  C CB  . PHE A 132 ? 0.39700 0.43250 0.37460 -0.12750 -0.03400 -0.05690 126 PHE A CB  
941  C CG  . PHE A 132 ? 0.44070 0.46690 0.40160 -0.12400 -0.03000 -0.04270 126 PHE A CG  
942  C CD1 . PHE A 132 ? 0.43090 0.45850 0.36410 -0.12440 -0.03510 -0.03690 126 PHE A CD1 
943  C CD2 . PHE A 132 ? 0.41810 0.43360 0.38930 -0.12190 -0.02170 -0.03470 126 PHE A CD2 
944  C CE1 . PHE A 132 ? 0.47830 0.49610 0.39700 -0.12340 -0.03130 -0.02400 126 PHE A CE1 
945  C CE2 . PHE A 132 ? 0.41860 0.42700 0.37660 -0.11880 -0.01810 -0.02340 126 PHE A CE2 
946  C CZ  . PHE A 132 ? 0.39780 0.40700 0.33080 -0.11970 -0.02250 -0.01840 126 PHE A CZ  
947  N N   . ILE A 133 ? 0.37230 0.41720 0.35500 -0.11430 -0.05390 -0.03950 127 ILE A N   
948  C CA  . ILE A 133 ? 0.43020 0.47570 0.42500 -0.10840 -0.05470 -0.03290 127 ILE A CA  
949  C C   . ILE A 133 ? 0.41270 0.44190 0.39340 -0.10700 -0.04670 -0.01970 127 ILE A C   
950  O O   . ILE A 133 ? 0.39070 0.40950 0.34700 -0.10550 -0.05210 -0.01170 127 ILE A O   
951  C CB  . ILE A 133 ? 0.44550 0.49780 0.44000 -0.09930 -0.07320 -0.03410 127 ILE A CB  
952  C CG1 . ILE A 133 ? 0.44250 0.51230 0.44700 -0.10000 -0.08340 -0.04860 127 ILE A CG1 
953  C CG2 . ILE A 133 ? 0.38860 0.44880 0.40490 -0.09300 -0.07350 -0.03440 127 ILE A CG2 
954  C CD1 . ILE A 133 ? 0.46190 0.55140 0.49910 -0.10580 -0.07530 -0.06190 127 ILE A CD1 
955  N N   . PRO A 134 ? 0.38650 0.41300 0.37960 -0.10890 -0.03420 -0.01690 128 PRO A N   
956  C CA  . PRO A 134 ? 0.38960 0.40300 0.37110 -0.10680 -0.02700 -0.00630 128 PRO A CA  
957  C C   . PRO A 134 ? 0.44310 0.45350 0.41930 -0.09930 -0.03570 0.00120  128 PRO A C   
958  O O   . PRO A 134 ? 0.41110 0.43200 0.40270 -0.09380 -0.04410 -0.00280 128 PRO A O   
959  C CB  . PRO A 134 ? 0.36660 0.38000 0.36440 -0.11000 -0.01540 -0.00560 128 PRO A CB  
960  C CG  . PRO A 134 ? 0.35710 0.38620 0.37580 -0.11400 -0.01720 -0.01340 128 PRO A CG  
961  C CD  . PRO A 134 ? 0.38160 0.41750 0.39840 -0.11460 -0.02700 -0.02270 128 PRO A CD  
962  N N   . THR A 135 ? 0.45410 0.45080 0.41010 -0.09930 -0.03420 0.01030  129 THR A N   
963  C CA  . THR A 135 ? 0.47400 0.46120 0.42310 -0.09340 -0.04330 0.01870  129 THR A CA  
964  C C   . THR A 135 ? 0.39430 0.37670 0.34710 -0.09220 -0.03220 0.02390  129 THR A C   
965  O O   . THR A 135 ? 0.39550 0.38220 0.35610 -0.09500 -0.01890 0.02150  129 THR A O   
966  C CB  . THR A 135 ? 0.45030 0.42350 0.36840 -0.09760 -0.05320 0.02650  129 THR A CB  
967  O OG1 . THR A 135 ? 0.46930 0.44150 0.37080 -0.10720 -0.04030 0.02680  129 THR A OG1 
968  C CG2 . THR A 135 ? 0.47350 0.45240 0.38820 -0.09680 -0.06700 0.02130  129 THR A CG2 
969  N N   . ALA A 136 ? 0.40480 0.37610 0.35130 -0.08800 -0.03960 0.03110  130 ALA A N   
970  C CA  . ALA A 136 ? 0.44130 0.41020 0.39380 -0.08590 -0.03070 0.03420  130 ALA A CA  
971  C C   . ALA A 136 ? 0.41700 0.38400 0.35880 -0.09300 -0.01550 0.03560  130 ALA A C   
972  O O   . ALA A 136 ? 0.37030 0.34260 0.32350 -0.09110 -0.00510 0.03390  130 ALA A O   
973  C CB  . ALA A 136 ? 0.40840 0.36100 0.35280 -0.08210 -0.04280 0.04150  130 ALA A CB  
974  N N   . VAL A 137 ? 0.41580 0.37770 0.33600 -0.10120 -0.01490 0.03690  131 VAL A N   
975  C CA  . VAL A 137 ? 0.43340 0.39820 0.34640 -0.10710 -0.00170 0.03360  131 VAL A CA  
976  C C   . VAL A 137 ? 0.43250 0.40630 0.36190 -0.10500 0.00630  0.02430  131 VAL A C   
977  O O   . VAL A 137 ? 0.43520 0.41150 0.36610 -0.10570 0.01540  0.01910  131 VAL A O   
978  C CB  . VAL A 137 ? 0.52820 0.49100 0.41360 -0.11840 -0.00320 0.03470  131 VAL A CB  
979  C CG1 . VAL A 137 ? 0.46800 0.44000 0.35180 -0.12090 -0.00570 0.02630  131 VAL A CG1 
980  C CG2 . VAL A 137 ? 0.48450 0.45230 0.36030 -0.12620 0.00920  0.03120  131 VAL A CG2 
981  N N   . CYS A 138 ? 0.36830 0.34620 0.31080 -0.10260 0.00190  0.02140  132 CYS A N   
982  C CA  . CYS A 138 ? 0.37210 0.35280 0.32860 -0.10290 0.00720  0.01480  132 CYS A CA  
983  C C   . CYS A 138 ? 0.35100 0.33210 0.32260 -0.09950 0.01150  0.01850  132 CYS A C   
984  O O   . CYS A 138 ? 0.39920 0.37720 0.37900 -0.10120 0.01490  0.01620  132 CYS A O   
985  C CB  . CYS A 138 ? 0.36400 0.34980 0.32610 -0.10570 0.00110  0.00900  132 CYS A CB  
986  S SG  . CYS A 138 ? 0.47310 0.46190 0.41540 -0.11060 -0.00540 0.00400  132 CYS A SG  
987  N N   . SER A 139 ? 0.29350 0.27800 0.26840 -0.09550 0.01000  0.02370  133 SER A N   
988  C CA  . SER A 139 ? 0.36960 0.35980 0.35700 -0.09350 0.01460  0.02600  133 SER A CA  
989  C C   . SER A 139 ? 0.33750 0.32020 0.32230 -0.09310 0.02180  0.02760  133 SER A C   
990  O O   . SER A 139 ? 0.33420 0.31170 0.31050 -0.09110 0.02390  0.02620  133 SER A O   
991  C CB  . SER A 139 ? 0.36730 0.36340 0.35890 -0.08770 0.01150  0.02810  133 SER A CB  
992  O OG  . SER A 139 ? 0.38960 0.39080 0.38720 -0.08540 0.01810  0.02990  133 SER A OG  
993  N N   . ASN A 140 ? 0.32700 0.30960 0.31870 -0.09600 0.02450  0.02980  134 ASN A N   
994  C CA  . ASN A 140 ? 0.34490 0.31700 0.33390 -0.09420 0.02740  0.03210  134 ASN A CA  
995  C C   . ASN A 140 ? 0.36840 0.34470 0.35510 -0.08760 0.03060  0.03390  134 ASN A C   
996  O O   . ASN A 140 ? 0.34490 0.31410 0.32910 -0.08350 0.03160  0.03290  134 ASN A O   
997  C CB  . ASN A 140 ? 0.32790 0.29630 0.32010 -0.10130 0.02780  0.03780  134 ASN A CB  
998  C CG  . ASN A 140 ? 0.42660 0.41120 0.42160 -0.10330 0.03190  0.04260  134 ASN A CG  
999  O OD1 . ASN A 140 ? 0.47710 0.46010 0.46760 -0.10080 0.03390  0.04750  134 ASN A OD1 
1000 N ND2 . ASN A 140 ? 0.37750 0.38070 0.38130 -0.10680 0.03230  0.03890  134 ASN A ND2 
1001 N N   . CYS A 141 ? 0.30280 0.29050 0.29240 -0.08560 0.03070  0.03450  135 CYS A N   
1002 C CA  . CYS A 141 ? 0.35450 0.34680 0.34410 -0.08000 0.03310  0.03470  135 CYS A CA  
1003 C C   . CYS A 141 ? 0.30400 0.29230 0.28710 -0.07900 0.03120  0.03270  135 CYS A C   
1004 O O   . CYS A 141 ? 0.30900 0.29980 0.29330 -0.07600 0.03180  0.03280  135 CYS A O   
1005 C CB  . CYS A 141 ? 0.32800 0.33600 0.32750 -0.07890 0.03340  0.03510  135 CYS A CB  
1006 S SG  . CYS A 141 ? 0.42790 0.44490 0.43050 -0.08660 0.03680  0.03870  135 CYS A SG  
1007 N N   . SER A 142 ? 0.29140 0.27330 0.26610 -0.08320 0.02880  0.03110  136 SER A N   
1008 C CA  . SER A 142 ? 0.32200 0.29910 0.28460 -0.08640 0.02660  0.03170  136 SER A CA  
1009 C C   . SER A 142 ? 0.35550 0.33330 0.31400 -0.08680 0.03280  0.02950  136 SER A C   
1010 O O   . SER A 142 ? 0.37480 0.34870 0.32750 -0.08920 0.03120  0.03260  136 SER A O   
1011 C CB  . SER A 142 ? 0.33710 0.31140 0.28850 -0.09270 0.02470  0.02880  136 SER A CB  
1012 O OG  . SER A 142 ? 0.36210 0.33890 0.31420 -0.09340 0.03050  0.02080  136 SER A OG  
1013 N N   . GLY A 143 ? 0.35360 0.33540 0.31580 -0.08460 0.03850  0.02310  137 GLY A N   
1014 C CA  . GLY A 143 ? 0.32610 0.31330 0.28710 -0.08470 0.04430  0.01730  137 GLY A CA  
1015 C C   . GLY A 143 ? 0.32260 0.31220 0.29060 -0.08010 0.04500  0.02060  137 GLY A C   
1016 O O   . GLY A 143 ? 0.32400 0.31570 0.28910 -0.08360 0.04810  0.01860  137 GLY A O   
1017 N N   . HIS A 144 ? 0.34590 0.33710 0.32320 -0.07400 0.04250  0.02470  138 HIS A N   
1018 C CA  . HIS A 144 ? 0.34590 0.34360 0.33150 -0.06930 0.04260  0.02550  138 HIS A CA  
1019 C C   . HIS A 144 ? 0.35060 0.34310 0.33560 -0.07170 0.03750  0.02820  138 HIS A C   
1020 O O   . HIS A 144 ? 0.32730 0.32000 0.31520 -0.07130 0.03790  0.02620  138 HIS A O   
1021 C CB  . HIS A 144 ? 0.34500 0.34990 0.33830 -0.06540 0.04160  0.02820  138 HIS A CB  
1022 C CG  . HIS A 144 ? 0.39280 0.41020 0.39500 -0.06040 0.04280  0.02610  138 HIS A CG  
1023 N ND1 . HIS A 144 ? 0.42860 0.45170 0.43170 -0.05610 0.04620  0.02290  138 HIS A ND1 
1024 C CD2 . HIS A 144 ? 0.35440 0.38220 0.36670 -0.05830 0.04020  0.02390  138 HIS A CD2 
1025 C CE1 . HIS A 144 ? 0.39180 0.42850 0.40340 -0.05250 0.04650  0.02000  138 HIS A CE1 
1026 N NE2 . HIS A 144 ? 0.42480 0.46520 0.44310 -0.05360 0.04310  0.01960  138 HIS A NE2 
1027 N N   . HIS A 145 ? 0.32980 0.31580 0.31150 -0.07410 0.03080  0.03200  139 HIS A N   
1028 C CA  . HIS A 145 ? 0.34670 0.32220 0.32630 -0.07510 0.02130  0.03520  139 HIS A CA  
1029 C C   . HIS A 145 ? 0.36660 0.32860 0.32960 -0.08440 0.02170  0.03860  139 HIS A C   
1030 O O   . HIS A 145 ? 0.34680 0.29680 0.30860 -0.08580 0.01470  0.04170  139 HIS A O   
1031 C CB  . HIS A 145 ? 0.32430 0.29620 0.30250 -0.07520 0.01250  0.03750  139 HIS A CB  
1032 C CG  . HIS A 145 ? 0.34090 0.32780 0.33830 -0.06780 0.00950  0.03250  139 HIS A CG  
1033 N ND1 . HIS A 145 ? 0.33820 0.32630 0.34800 -0.06150 -0.00230 0.02870  139 HIS A ND1 
1034 C CD2 . HIS A 145 ? 0.34940 0.35260 0.35600 -0.06700 0.01650  0.02940  139 HIS A CD2 
1035 C CE1 . HIS A 145 ? 0.38080 0.39120 0.40850 -0.05740 -0.00050 0.02100  139 HIS A CE1 
1036 N NE2 . HIS A 145 ? 0.36870 0.38750 0.39240 -0.06240 0.01130  0.02300  139 HIS A NE2 
1037 N N   . VAL A 146 ? 0.35390 0.31760 0.30380 -0.09230 0.02910  0.03740  140 VAL A N   
1038 C CA  . VAL A 146 ? 0.37750 0.33420 0.31000 -0.10510 0.03190  0.03920  140 VAL A CA  
1039 C C   . VAL A 146 ? 0.36850 0.33140 0.30960 -0.10470 0.03850  0.03400  140 VAL A C   
1040 O O   . VAL A 146 ? 0.39380 0.34620 0.32620 -0.11430 0.03710  0.03760  140 VAL A O   
1041 C CB  . VAL A 146 ? 0.37080 0.33580 0.29000 -0.11410 0.03910  0.03420  140 VAL A CB  
1042 C CG1 . VAL A 146 ? 0.40280 0.36830 0.30440 -0.13040 0.04520  0.03340  140 VAL A CG1 
1043 C CG2 . VAL A 146 ? 0.37010 0.32860 0.27890 -0.11590 0.03150  0.03900  140 VAL A CG2 
1044 N N   . GLY A 147 ? 0.32930 0.30790 0.28680 -0.09450 0.04460  0.02590  141 GLY A N   
1045 C CA  . GLY A 147 ? 0.30790 0.29480 0.27610 -0.09170 0.04930  0.01960  141 GLY A CA  
1046 C C   . GLY A 147 ? 0.32130 0.29920 0.29760 -0.08850 0.04170  0.02320  141 GLY A C   
1047 O O   . GLY A 147 ? 0.36570 0.34070 0.34320 -0.09380 0.04310  0.02090  141 GLY A O   
1048 N N   . MET A 148 ? 0.31440 0.28990 0.29910 -0.07990 0.03330  0.02630  142 MET A N   
1049 C CA  . MET A 148 ? 0.29770 0.26730 0.29470 -0.07460 0.02400  0.02540  142 MET A CA  
1050 C C   . MET A 148 ? 0.35520 0.29790 0.33870 -0.08440 0.01400  0.03340  142 MET A C   
1051 O O   . MET A 148 ? 0.38180 0.31430 0.37100 -0.08570 0.00900  0.03200  142 MET A O   
1052 C CB  . MET A 148 ? 0.29110 0.26980 0.30180 -0.06400 0.01720  0.02330  142 MET A CB  
1053 C CG  . MET A 148 ? 0.35810 0.36120 0.37880 -0.05760 0.02590  0.01780  142 MET A CG  
1054 S SD  . MET A 148 ? 0.39870 0.41970 0.43520 -0.05100 0.03040  0.00750  142 MET A SD  
1055 C CE  . MET A 148 ? 0.42580 0.44020 0.47860 -0.04570 0.01650  0.00180  142 MET A CE  
1056 N N   . LEU A 149 ? 0.33920 0.26850 0.30290 -0.09270 0.01020  0.04230  143 LEU A N   
1057 C CA  . LEU A 149 ? 0.38110 0.28200 0.32410 -0.10590 0.00050  0.05310  143 LEU A CA  
1058 C C   . LEU A 149 ? 0.42340 0.32240 0.35650 -0.12080 0.01040  0.05260  143 LEU A C   
1059 O O   . LEU A 149 ? 0.44990 0.32580 0.37680 -0.12930 0.00190  0.05860  143 LEU A O   
1060 C CB  . LEU A 149 ? 0.40140 0.29420 0.32070 -0.11450 -0.00260 0.06180  143 LEU A CB  
1061 C CG  . LEU A 149 ? 0.47750 0.36400 0.40180 -0.10360 -0.01770 0.06450  143 LEU A CG  
1062 C CD1 . LEU A 149 ? 0.53460 0.42030 0.43580 -0.11300 -0.01660 0.07020  143 LEU A CD1 
1063 C CD2 . LEU A 149 ? 0.48950 0.34750 0.41520 -0.09960 -0.03980 0.07050  143 LEU A CD2 
1064 N N   . ALA A 150 ? 0.44550 0.36850 0.37840 -0.12460 0.02720  0.04440  144 ALA A N   
1065 C CA  . ALA A 150 ? 0.39470 0.32430 0.32160 -0.13910 0.03840  0.03950  144 ALA A CA  
1066 C C   . ALA A 150 ? 0.40690 0.33490 0.35250 -0.13440 0.03670  0.03390  144 ALA A C   
1067 O O   . ALA A 150 ? 0.43100 0.34500 0.36830 -0.14920 0.03600  0.03690  144 ALA A O   
1068 C CB  . ALA A 150 ? 0.35310 0.31390 0.28540 -0.13560 0.05290  0.02590  144 ALA A CB  
1069 N N   . GLY A 151 ? 0.37390 0.31750 0.34430 -0.11490 0.03620  0.02520  145 GLY A N   
1070 C CA  . GLY A 151 ? 0.36910 0.31510 0.35920 -0.10890 0.03390  0.01730  145 GLY A CA  
1071 C C   . GLY A 151 ? 0.44610 0.36150 0.43710 -0.11030 0.01700  0.02440  145 GLY A C   
1072 O O   . GLY A 151 ? 0.38920 0.29340 0.38510 -0.11720 0.01440  0.02200  145 GLY A O   
1073 N N   . ALA A 152 ? 0.39240 0.29290 0.38030 -0.10350 0.00350  0.03210  146 ALA A N   
1074 C CA  . ALA A 152 ? 0.47660 0.34380 0.46530 -0.10310 -0.01720 0.03850  146 ALA A CA  
1075 C C   . ALA A 152 ? 0.46080 0.29530 0.42320 -0.12630 -0.02080 0.05160  146 ALA A C   
1076 O O   . ALA A 152 ? 0.48460 0.29610 0.45300 -0.13030 -0.03120 0.05190  146 ALA A O   
1077 C CB  . ALA A 152 ? 0.40630 0.26490 0.39240 -0.09380 -0.03100 0.04420  146 ALA A CB  
1078 N N   . ARG A 153 ? 0.49400 0.32630 0.42640 -0.14350 -0.01270 0.06220  147 ARG A N   
1079 C CA  . ARG A 153 ? 0.51830 0.33410 0.42550 -0.16110 -0.01320 0.07160  147 ARG A CA  
1080 C C   . ARG A 153 ? 0.52880 0.35850 0.44400 -0.17060 0.00050  0.06220  147 ARG A C   
1081 O O   . ARG A 153 ? 0.51830 0.32810 0.42450 -0.18160 -0.00510 0.06780  147 ARG A O   
1082 C CB  . ARG A 153 ? 0.51660 0.34640 0.39750 -0.16900 -0.00490 0.07610  147 ARG A CB  
1083 C CG  . ARG A 153 ? 0.65820 0.46670 0.52140 -0.16640 -0.02170 0.08870  147 ARG A CG  
1084 C CD  . ARG A 153 ? 0.72210 0.51280 0.55200 -0.18270 -0.02890 0.10070  147 ARG A CD  
1085 N NE  . ARG A 153 ? 0.78840 0.55510 0.60480 -0.17770 -0.04960 0.11230  147 ARG A NE  
1086 C CZ  . ARG A 153 ? 0.80400 0.58020 0.60330 -0.18020 -0.04890 0.11480  147 ARG A CZ  
1087 N NH1 . ARG A 153 ? 0.78550 0.59280 0.57670 -0.18900 -0.02940 0.10670  147 ARG A NH1 
1088 N NH2 . ARG A 153 ? 0.79500 0.54970 0.58720 -0.17290 -0.06960 0.12370  147 ARG A NH2 
1089 N N   . ALA A 154 ? 0.47610 0.34060 0.40770 -0.16680 0.01800  0.04750  148 ALA A N   
1090 C CA  . ALA A 154 ? 0.49610 0.38020 0.43730 -0.17440 0.03130  0.03540  148 ALA A CA  
1091 C C   . ALA A 154 ? 0.49710 0.36060 0.45550 -0.17580 0.02200  0.03280  148 ALA A C   
1092 O O   . ALA A 154 ? 0.46600 0.32720 0.42200 -0.18800 0.02540  0.03110  148 ALA A O   
1093 C CB  . ALA A 154 ? 0.47350 0.39770 0.43190 -0.16510 0.04760  0.01860  148 ALA A CB  
1094 N N   . ILE A 155 ? 0.48210 0.33590 0.46160 -0.15870 0.00890  0.02930  149 ILE A N   
1095 C CA  . ILE A 155 ? 0.48390 0.32260 0.48520 -0.15420 -0.00220 0.02200  149 ILE A CA  
1096 C C   . ILE A 155 ? 0.51870 0.30570 0.50960 -0.15850 -0.02760 0.03720  149 ILE A C   
1097 O O   . ILE A 155 ? 0.50070 0.26820 0.51180 -0.15210 -0.04240 0.03100  149 ILE A O   
1098 C CB  . ILE A 155 ? 0.43190 0.30200 0.46930 -0.12650 -0.00210 0.00290  149 ILE A CB  
1099 C CG1 . ILE A 155 ? 0.35920 0.23380 0.40120 -0.10720 -0.01120 0.00530  149 ILE A CG1 
1100 C CG2 . ILE A 155 ? 0.41720 0.33150 0.46430 -0.12400 0.01920  -0.01180 149 ILE A CG2 
1101 C CD1 . ILE A 155 ? 0.40340 0.30790 0.47760 -0.08410 -0.01230 -0.01270 149 ILE A CD1 
1102 N N   . GLY A 156 ? 0.53020 0.30080 0.49220 -0.16380 -0.03280 0.05430  150 GLY A N   
1103 C CA  . GLY A 156 ? 0.52750 0.25670 0.47890 -0.16130 -0.05680 0.06710  150 GLY A CA  
1104 C C   . GLY A 156 ? 0.58550 0.30050 0.56210 -0.13840 -0.08000 0.06120  150 GLY A C   
1105 O O   . GLY A 156 ? 0.63610 0.32020 0.61960 -0.13080 -0.10280 0.06280  150 GLY A O   
1106 N N   . ALA A 157 ? 0.56100 0.30920 0.55570 -0.12260 -0.07270 0.05020  151 ALA A N   
1107 C CA  . ALA A 157 ? 0.60010 0.35660 0.62480 -0.09550 -0.08860 0.03760  151 ALA A CA  
1108 C C   . ALA A 157 ? 0.64890 0.37840 0.65900 -0.09100 -0.10960 0.05030  151 ALA A C   
1109 O O   . ALA A 157 ? 0.67230 0.39740 0.70760 -0.07050 -0.13030 0.03980  151 ALA A O   
1110 C CB  . ALA A 157 ? 0.49320 0.30460 0.53840 -0.08020 -0.06890 0.02140  151 ALA A CB  
1111 N N   . GLY A 158 ? 0.58520 0.30060 0.55700 -0.10870 -0.10540 0.06980  152 GLY A N   
1112 C CA  . GLY A 158 ? 0.67260 0.36880 0.63150 -0.10250 -0.12460 0.07990  152 GLY A CA  
1113 C C   . GLY A 158 ? 0.60740 0.34700 0.57500 -0.09060 -0.10990 0.07120  152 GLY A C   
1114 O O   . GLY A 158 ? 0.59480 0.37360 0.59250 -0.07600 -0.09750 0.05290  152 GLY A O   
1115 N N   . THR A 159 ? 0.62090 0.35370 0.56040 -0.09860 -0.11110 0.08450  153 THR A N   
1116 C CA  . THR A 159 ? 0.58340 0.35410 0.52800 -0.09130 -0.09620 0.07770  153 THR A CA  
1117 C C   . THR A 159 ? 0.64310 0.42290 0.61190 -0.06950 -0.11270 0.06730  153 THR A C   
1118 O O   . THR A 159 ? 0.55720 0.37370 0.54090 -0.06110 -0.09970 0.05670  153 THR A O   
1119 C CB  . THR A 159 ? 0.67430 0.43930 0.57970 -0.11080 -0.08780 0.09320  153 THR A CB  
1120 O OG1 . THR A 159 ? 0.69420 0.41770 0.57200 -0.11890 -0.11120 0.11010  153 THR A OG1 
1121 C CG2 . THR A 159 ? 0.65460 0.42910 0.54470 -0.13060 -0.06510 0.09530  153 THR A CG2 
1122 N N   . ASP A 160 ? 0.64310 0.39010 0.61590 -0.06110 -0.14220 0.06970  154 ASP A N   
1123 C CA  A ASP A 160 ? 0.64520 0.40660 0.64850 -0.03840 -0.15910 0.05390  154 ASP A CA  
1124 C CA  B ASP A 160 ? 0.64520 0.40640 0.64870 -0.03830 -0.15940 0.05380  154 ASP A CA  
1125 C C   . ASP A 160 ? 0.60660 0.40940 0.65230 -0.02330 -0.14780 0.02920  154 ASP A C   
1126 O O   . ASP A 160 ? 0.59420 0.39150 0.65410 -0.02170 -0.14840 0.02260  154 ASP A O   
1127 C CB  A ASP A 160 ? 0.68150 0.39690 0.68430 -0.03010 -0.19650 0.05870  154 ASP A CB  
1128 C CB  B ASP A 160 ? 0.68140 0.39630 0.68490 -0.02990 -0.19690 0.05840  154 ASP A CB  
1129 C CG  A ASP A 160 ? 0.71550 0.38770 0.67020 -0.04730 -0.21000 0.08580  154 ASP A CG  
1130 C CG  B ASP A 160 ? 0.68580 0.41620 0.71980 -0.00610 -0.21800 0.04060  154 ASP A CG  
1131 O OD1 A ASP A 160 ? 0.69950 0.38760 0.63090 -0.05760 -0.19510 0.09380  154 ASP A OD1 
1132 O OD1 B ASP A 160 ? 0.70080 0.43910 0.72200 -0.00640 -0.21950 0.04500  154 ASP A OD1 
1133 O OD2 A ASP A 160 ? 0.73010 0.36160 0.67080 -0.05060 -0.23290 0.09590  154 ASP A OD2 
1134 O OD2 B ASP A 160 ? 0.65820 0.39480 0.73090 0.01300  -0.23380 0.01970  154 ASP A OD2 
1135 N N   . GLY A 161 ? 0.56120 0.40640 0.62500 -0.01450 -0.13650 0.01580  155 GLY A N   
1136 C CA  . GLY A 161 ? 0.48320 0.37160 0.58380 -0.00250 -0.12610 -0.00740 155 GLY A CA  
1137 C C   . GLY A 161 ? 0.41740 0.32910 0.51470 -0.01130 -0.09840 -0.00750 155 GLY A C   
1138 O O   . GLY A 161 ? 0.37040 0.31080 0.49450 -0.00300 -0.09270 -0.02510 155 GLY A O   
1139 N N   . TYR A 162 ? 0.41400 0.31660 0.48010 -0.02750 -0.08210 0.00960  156 TYR A N   
1140 C CA  . TYR A 162 ? 0.39810 0.32250 0.46190 -0.03410 -0.05840 0.00830  156 TYR A CA  
1141 C C   . TYR A 162 ? 0.36860 0.33620 0.45050 -0.02720 -0.04490 -0.00440 156 TYR A C   
1142 O O   . TYR A 162 ? 0.31140 0.30000 0.39800 -0.02810 -0.02990 -0.00940 156 TYR A O   
1143 C CB  . TYR A 162 ? 0.44200 0.35400 0.47290 -0.05080 -0.04510 0.02480  156 TYR A CB  
1144 C CG  . TYR A 162 ? 0.40200 0.32450 0.42110 -0.05350 -0.03890 0.02970  156 TYR A CG  
1145 C CD1 . TYR A 162 ? 0.42770 0.32940 0.43070 -0.05670 -0.05230 0.03890  156 TYR A CD1 
1146 C CD2 . TYR A 162 ? 0.35820 0.30940 0.38160 -0.05310 -0.02160 0.02510  156 TYR A CD2 
1147 C CE1 . TYR A 162 ? 0.44010 0.35270 0.43440 -0.05910 -0.04700 0.04130  156 TYR A CE1 
1148 C CE2 . TYR A 162 ? 0.32750 0.28530 0.34180 -0.05620 -0.01730 0.02880  156 TYR A CE2 
1149 C CZ  . TYR A 162 ? 0.41880 0.35890 0.42000 -0.05910 -0.02930 0.03580  156 TYR A CZ  
1150 O OH  . TYR A 162 ? 0.43500 0.38300 0.42900 -0.06230 -0.02530 0.03750  156 TYR A OH  
1151 N N   . HIS A 163 ? 0.32850 0.30980 0.41940 -0.02150 -0.05070 -0.00960 157 HIS A N   
1152 C CA  . HIS A 163 ? 0.36220 0.38280 0.46540 -0.01980 -0.03770 -0.01920 157 HIS A CA  
1153 C C   . HIS A 163 ? 0.34650 0.39960 0.48320 -0.00820 -0.04260 -0.04160 157 HIS A C   
1154 O O   . HIS A 163 ? 0.33750 0.42700 0.48360 -0.00960 -0.03130 -0.05040 157 HIS A O   
1155 C CB  . HIS A 163 ? 0.30840 0.33020 0.40360 -0.02310 -0.03940 -0.01440 157 HIS A CB  
1156 C CG  . HIS A 163 ? 0.40320 0.41700 0.51190 -0.01350 -0.06140 -0.02180 157 HIS A CG  
1157 N ND1 . HIS A 163 ? 0.42820 0.40310 0.52620 -0.01140 -0.08050 -0.01320 157 HIS A ND1 
1158 C CD2 . HIS A 163 ? 0.38570 0.42560 0.51770 -0.00570 -0.06890 -0.03760 157 HIS A CD2 
1159 C CE1 . HIS A 163 ? 0.46350 0.43790 0.57770 -0.00040 -0.10110 -0.02290 157 HIS A CE1 
1160 N NE2 . HIS A 163 ? 0.41030 0.42640 0.54720 0.00380  -0.09390 -0.03950 157 HIS A NE2 
1161 N N   . LEU A 164 ? 0.30770 0.34850 0.46340 0.00270  -0.06070 -0.05240 158 LEU A N   
1162 C CA  . LEU A 164 ? 0.28930 0.36530 0.48160 0.01540  -0.06710 -0.07890 158 LEU A CA  
1163 C C   . LEU A 164 ? 0.32400 0.42030 0.52530 0.01570  -0.05550 -0.08820 158 LEU A C   
1164 O O   . LEU A 164 ? 0.36080 0.43260 0.54600 0.01010  -0.05110 -0.07600 158 LEU A O   
1165 C CB  . LEU A 164 ? 0.31690 0.37000 0.52940 0.02960  -0.09600 -0.08950 158 LEU A CB  
1166 C CG  . LEU A 164 ? 0.35350 0.38390 0.55670 0.03130  -0.11240 -0.08100 158 LEU A CG  
1167 C CD1 . LEU A 164 ? 0.46420 0.46720 0.68710 0.04700  -0.14490 -0.09120 158 LEU A CD1 
1168 C CD2 . LEU A 164 ? 0.34640 0.41870 0.56090 0.03100  -0.10410 -0.09220 158 LEU A CD2 
1169 N N   . PRO A 165 ? 0.27690 0.42150 0.50400 0.02110  -0.04990 -0.11110 159 PRO A N   
1170 C CA  . PRO A 165 ? 0.31120 0.48010 0.54340 0.02010  -0.03720 -0.11950 159 PRO A CA  
1171 C C   . PRO A 165 ? 0.37260 0.51920 0.61830 0.02840  -0.04980 -0.12690 159 PRO A C   
1172 O O   . PRO A 165 ? 0.34440 0.49730 0.58520 0.02500  -0.03910 -0.12650 159 PRO A O   
1173 C CB  . PRO A 165 ? 0.22890 0.45690 0.48710 0.02340  -0.03170 -0.14540 159 PRO A CB  
1174 C CG  . PRO A 165 ? 0.30310 0.53810 0.55530 0.01780  -0.03030 -0.14030 159 PRO A CG  
1175 C CD  . PRO A 165 ? 0.22010 0.40500 0.46490 0.02290  -0.04890 -0.12710 159 PRO A CD  
1176 N N   . ASP A 166 ? 0.36830 0.48750 0.63120 0.03920  -0.07390 -0.13400 160 ASP A N   
1177 C CA  . ASP A 166 ? 0.35570 0.44820 0.63230 0.04590  -0.08850 -0.14080 160 ASP A CA  
1178 C C   . ASP A 166 ? 0.34070 0.37750 0.58500 0.03390  -0.09000 -0.11290 160 ASP A C   
1179 O O   . ASP A 166 ? 0.35520 0.36760 0.60650 0.03480  -0.09930 -0.11560 160 ASP A O   
1180 C CB  . ASP A 166 ? 0.43330 0.51690 0.74410 0.06350  -0.11770 -0.16200 160 ASP A CB  
1181 C CG  . ASP A 166 ? 0.63310 0.77130 0.98780 0.07750  -0.11940 -0.20030 160 ASP A CG  
1182 O OD1 . ASP A 166 ? 0.67890 0.85760 1.03200 0.07590  -0.10630 -0.21180 160 ASP A OD1 
1183 O OD2 . ASP A 166 ? 0.64580 0.77600 1.02110 0.08540  -0.12990 -0.21600 160 ASP A OD2 
1184 N N   . HIS A 167 ? 0.31610 0.33450 0.52690 0.02150  -0.08130 -0.08830 161 HIS A N   
1185 C CA  . HIS A 167 ? 0.37590 0.35280 0.55450 0.00670  -0.07760 -0.06430 161 HIS A CA  
1186 C C   . HIS A 167 ? 0.36440 0.35810 0.53750 -0.00070 -0.05740 -0.06470 161 HIS A C   
1187 O O   . HIS A 167 ? 0.34320 0.37640 0.51900 0.00040  -0.04050 -0.07110 161 HIS A O   
1188 C CB  . HIS A 167 ? 0.36060 0.32490 0.50800 -0.00390 -0.07100 -0.04320 161 HIS A CB  
1189 C CG  . HIS A 167 ? 0.40320 0.32470 0.51830 -0.01950 -0.07190 -0.02090 161 HIS A CG  
1190 N ND1 . HIS A 167 ? 0.37460 0.29770 0.47180 -0.03260 -0.05330 -0.01270 161 HIS A ND1 
1191 C CD2 . HIS A 167 ? 0.43460 0.31290 0.53100 -0.02550 -0.08940 -0.00590 161 HIS A CD2 
1192 C CE1 . HIS A 167 ? 0.44490 0.33160 0.51490 -0.04750 -0.05710 0.00480  161 HIS A CE1 
1193 N NE2 . HIS A 167 ? 0.44410 0.30150 0.51030 -0.04450 -0.07890 0.01100  161 HIS A NE2 
1194 N N   . PRO A 168 ? 0.38640 0.32600 0.49080 -0.13800 -0.00310 0.01360  162 PRO A N   
1195 C CA  . PRO A 168 ? 0.40780 0.35280 0.51980 -0.13890 -0.00460 0.00640  162 PRO A CA  
1196 C C   . PRO A 168 ? 0.36490 0.32550 0.48080 -0.13400 -0.00090 0.00210  162 PRO A C   
1197 O O   . PRO A 168 ? 0.34050 0.30260 0.45510 -0.13280 0.00050  -0.00780 162 PRO A O   
1198 C CB  . PRO A 168 ? 0.32680 0.27850 0.44940 -0.14660 -0.00880 0.01330  162 PRO A CB  
1199 C CG  . PRO A 168 ? 0.36450 0.30610 0.47520 -0.15270 -0.01000 0.02100  162 PRO A CG  
1200 C CD  . PRO A 168 ? 0.35350 0.29260 0.45510 -0.14690 -0.00540 0.02230  162 PRO A CD  
1201 N N   . MET A 169 ? 0.32520 0.29760 0.44410 -0.13120 0.00250  0.00720  163 MET A N   
1202 C CA  . MET A 169 ? 0.31470 0.29980 0.43210 -0.12680 0.00670  0.00130  163 MET A CA  
1203 C C   . MET A 169 ? 0.36470 0.34270 0.47100 -0.11940 0.00890  -0.00680 163 MET A C   
1204 O O   . MET A 169 ? 0.33150 0.31560 0.43560 -0.11680 0.01160  -0.01590 163 MET A O   
1205 C CB  . MET A 169 ? 0.34380 0.33990 0.46470 -0.12550 0.01030  0.00680  163 MET A CB  
1206 C CG  . MET A 169 ? 0.42010 0.43030 0.55320 -0.13100 0.01260  0.01000  163 MET A CG  
1207 S SD  . MET A 169 ? 0.51630 0.53820 0.64940 -0.13410 0.01390  0.00060  163 MET A SD  
1208 C CE  . MET A 169 ? 0.27760 0.30570 0.39750 -0.12690 0.01850  -0.00910 163 MET A CE  
1209 N N   . GLN A 170 ? 0.30120 0.26730 0.40150 -0.11600 0.00820  -0.00340 164 GLN A N   
1210 C CA  . GLN A 170 ? 0.36540 0.32550 0.45880 -0.10870 0.01140  -0.01050 164 GLN A CA  
1211 C C   . GLN A 170 ? 0.31590 0.26910 0.40930 -0.10870 0.01220  -0.02040 164 GLN A C   
1212 O O   . GLN A 170 ? 0.34170 0.29790 0.43340 -0.10390 0.01510  -0.02840 164 GLN A O   
1213 C CB  . GLN A 170 ? 0.38420 0.33380 0.47230 -0.10550 0.01110  -0.00420 164 GLN A CB  
1214 C CG  . GLN A 170 ? 0.35990 0.31670 0.44720 -0.10490 0.01090  0.00350  164 GLN A CG  
1215 C CD  . GLN A 170 ? 0.41460 0.38420 0.50280 -0.10130 0.01250  -0.00040 164 GLN A CD  
1216 O OE1 . GLN A 170 ? 0.42830 0.40790 0.52070 -0.10380 0.01270  0.00260  164 GLN A OE1 
1217 N NE2 . GLN A 170 ? 0.33320 0.30270 0.41880 -0.09590 0.01470  -0.00790 164 GLN A NE2 
1218 N N   . GLY A 171 ? 0.33690 0.28110 0.43280 -0.11460 0.00910  -0.02000 165 GLY A N   
1219 C CA  . GLY A 171 ? 0.35710 0.29550 0.45360 -0.11570 0.00890  -0.03030 165 GLY A CA  
1220 C C   . GLY A 171 ? 0.35690 0.30980 0.45550 -0.11670 0.00920  -0.03640 165 GLY A C   
1221 O O   . GLY A 171 ? 0.32480 0.27860 0.42120 -0.11370 0.01090  -0.04590 165 GLY A O   
1222 N N   . ARG A 172 ? 0.30320 0.26900 0.40670 -0.12100 0.00790  -0.03090 166 ARG A N   
1223 C CA  . ARG A 172 ? 0.31060 0.29180 0.41650 -0.12170 0.00900  -0.03620 166 ARG A CA  
1224 C C   . ARG A 172 ? 0.31000 0.29900 0.41150 -0.11400 0.01320  -0.04090 166 ARG A C   
1225 O O   . ARG A 172 ? 0.30400 0.29920 0.40530 -0.11230 0.01380  -0.04850 166 ARG A O   
1226 C CB  . ARG A 172 ? 0.29250 0.28660 0.40620 -0.12750 0.00820  -0.02940 166 ARG A CB  
1227 C CG  . ARG A 172 ? 0.25680 0.24780 0.37900 -0.13650 0.00280  -0.02570 166 ARG A CG  
1228 C CD  . ARG A 172 ? 0.27430 0.27360 0.40720 -0.14170 0.00210  -0.01440 166 ARG A CD  
1229 N NE  . ARG A 172 ? 0.27800 0.27490 0.42290 -0.15020 -0.00380 -0.00990 166 ARG A NE  
1230 C CZ  . ARG A 172 ? 0.32290 0.33410 0.47880 -0.15520 -0.00360 -0.00940 166 ARG A CZ  
1231 N NH1 . ARG A 172 ? 0.29450 0.32350 0.44850 -0.15300 0.00230  -0.01290 166 ARG A NH1 
1232 N NH2 . ARG A 172 ? 0.26800 0.27570 0.43640 -0.16200 -0.00910 -0.00580 166 ARG A NH2 
1233 N N   . VAL A 173 ? 0.29670 0.28600 0.39570 -0.10960 0.01530  -0.03590 167 VAL A N   
1234 C CA  . VAL A 173 ? 0.25010 0.24520 0.34630 -0.10270 0.01790  -0.03950 167 VAL A CA  
1235 C C   . VAL A 173 ? 0.30850 0.29710 0.40250 -0.09850 0.01860  -0.04580 167 VAL A C   
1236 O O   . VAL A 173 ? 0.30180 0.29860 0.39670 -0.09570 0.01920  -0.05170 167 VAL A O   
1237 C CB  . VAL A 173 ? 0.28880 0.28220 0.38250 -0.09930 0.01870  -0.03250 167 VAL A CB  
1238 C CG1 . VAL A 173 ? 0.29110 0.28780 0.38310 -0.09230 0.02000  -0.03560 167 VAL A CG1 
1239 C CG2 . VAL A 173 ? 0.26400 0.26700 0.36060 -0.10360 0.01890  -0.02800 167 VAL A CG2 
1240 N N   . LYS A 174 ? 0.29890 0.27340 0.39080 -0.09820 0.01860  -0.04460 168 LYS A N   
1241 C CA  . LYS A 174 ? 0.33240 0.30100 0.42300 -0.09410 0.02050  -0.05120 168 LYS A CA  
1242 C C   . LYS A 174 ? 0.35130 0.32530 0.44280 -0.09670 0.01930  -0.06090 168 LYS A C   
1243 O O   . LYS A 174 ? 0.31470 0.29540 0.40650 -0.09340 0.02030  -0.06670 168 LYS A O   
1244 C CB  . LYS A 174 ? 0.38200 0.33370 0.47130 -0.09390 0.02120  -0.04910 168 LYS A CB  
1245 C CG  . LYS A 174 ? 0.40590 0.35010 0.49480 -0.08820 0.02510  -0.05420 168 LYS A CG  
1246 C CD  . LYS A 174 ? 0.45460 0.38360 0.54360 -0.08600 0.02690  -0.04850 168 LYS A CD  
1247 C CE  . LYS A 174 ? 0.51520 0.44640 0.60400 -0.08100 0.02820  -0.03820 168 LYS A CE  
1248 N NZ  . LYS A 174 ? 0.40780 0.34410 0.49390 -0.08380 0.02440  -0.02750 168 LYS A NZ  
1249 N N   . ARG A 175 ? 0.32440 0.29660 0.41710 -0.10320 0.01620  -0.06170 169 ARG A N   
1250 C CA  A ARG A 175 ? 0.34580 0.32270 0.43910 -0.10660 0.01370  -0.07000 169 ARG A CA  
1251 C CA  B ARG A 175 ? 0.34550 0.32250 0.43890 -0.10660 0.01370  -0.07000 169 ARG A CA  
1252 C C   . ARG A 175 ? 0.33330 0.32870 0.42940 -0.10560 0.01370  -0.07120 169 ARG A C   
1253 O O   . ARG A 175 ? 0.31610 0.31840 0.41200 -0.10480 0.01280  -0.07820 169 ARG A O   
1254 C CB  A ARG A 175 ? 0.35560 0.32610 0.45120 -0.11460 0.00920  -0.06860 169 ARG A CB  
1255 C CB  B ARG A 175 ? 0.35540 0.32590 0.45100 -0.11460 0.00920  -0.06860 169 ARG A CB  
1256 C CG  A ARG A 175 ? 0.34510 0.31440 0.44020 -0.11900 0.00510  -0.07720 169 ARG A CG  
1257 C CG  B ARG A 175 ? 0.34550 0.32060 0.44220 -0.11950 0.00510  -0.07580 169 ARG A CG  
1258 C CD  A ARG A 175 ? 0.33340 0.29120 0.43140 -0.12670 -0.00020 -0.07480 169 ARG A CD  
1259 C CD  B ARG A 175 ? 0.34080 0.30840 0.44140 -0.12810 -0.00040 -0.07260 169 ARG A CD  
1260 N NE  A ARG A 175 ? 0.33760 0.30120 0.44200 -0.13130 -0.00140 -0.06390 169 ARG A NE  
1261 N NE  B ARG A 175 ? 0.33550 0.31180 0.44270 -0.13170 -0.00070 -0.06230 169 ARG A NE  
1262 C CZ  A ARG A 175 ? 0.31390 0.26780 0.42000 -0.13320 -0.00230 -0.05580 169 ARG A CZ  
1263 C CZ  B ARG A 175 ? 0.33920 0.33280 0.45170 -0.13400 -0.00060 -0.06040 169 ARG A CZ  
1264 N NH1 A ARG A 175 ? 0.31770 0.25530 0.41950 -0.12990 -0.00110 -0.05690 169 ARG A NH1 
1265 N NH1 B ARG A 175 ? 0.31570 0.32020 0.42780 -0.13270 -0.00060 -0.06690 169 ARG A NH1 
1266 N NH2 A ARG A 175 ? 0.28110 0.24300 0.39460 -0.13870 -0.00440 -0.04620 169 ARG A NH2 
1267 N NH2 B ARG A 175 ? 0.30010 0.30130 0.41920 -0.13760 -0.00040 -0.05180 169 ARG A NH2 
1268 N N   . THR A 176 ? 0.30140 0.30540 0.40020 -0.10540 0.01470  -0.06490 170 THR A N   
1269 C CA  . THR A 176 ? 0.25570 0.27670 0.35840 -0.10450 0.01480  -0.06640 170 THR A CA  
1270 C C   . THR A 176 ? 0.27260 0.29940 0.37540 -0.09730 0.01610  -0.06880 170 THR A C   
1271 O O   . THR A 176 ? 0.27170 0.31050 0.37810 -0.09640 0.01480  -0.07270 170 THR A O   
1272 C CB  . THR A 176 ? 0.31950 0.34740 0.42500 -0.10610 0.01620  -0.06050 170 THR A CB  
1273 O OG1 . THR A 176 ? 0.37040 0.39420 0.47800 -0.11330 0.01430  -0.05670 170 THR A OG1 
1274 C CG2 . THR A 176 ? 0.27680 0.32220 0.38760 -0.10540 0.01680  -0.06330 170 THR A CG2 
1275 N N   . VAL A 177 ? 0.26500 0.28420 0.36540 -0.09260 0.01800  -0.06540 171 VAL A N   
1276 C CA  . VAL A 177 ? 0.28700 0.31090 0.38920 -0.08640 0.01820  -0.06640 171 VAL A CA  
1277 C C   . VAL A 177 ? 0.27480 0.30190 0.37770 -0.08640 0.01700  -0.07340 171 VAL A C   
1278 O O   . VAL A 177 ? 0.28110 0.32060 0.38850 -0.08410 0.01520  -0.07550 171 VAL A O   
1279 C CB  . VAL A 177 ? 0.27250 0.28640 0.37250 -0.08250 0.01990  -0.06040 171 VAL A CB  
1280 C CG1 . VAL A 177 ? 0.21500 0.23350 0.31900 -0.07700 0.01930  -0.06040 171 VAL A CG1 
1281 C CG2 . VAL A 177 ? 0.26150 0.27520 0.36050 -0.08300 0.02010  -0.05420 171 VAL A CG2 
1282 N N   . ALA A 178 ? 0.25710 0.27320 0.35570 -0.08910 0.01770  -0.07730 172 ALA A N   
1283 C CA  . ALA A 178 ? 0.28540 0.30470 0.38310 -0.08960 0.01660  -0.08600 172 ALA A CA  
1284 C C   . ALA A 178 ? 0.28070 0.31260 0.38000 -0.09350 0.01280  -0.09020 172 ALA A C   
1285 O O   . ALA A 178 ? 0.29810 0.34200 0.39910 -0.09250 0.01070  -0.09460 172 ALA A O   
1286 C CB  . ALA A 178 ? 0.27620 0.27900 0.36820 -0.09160 0.01800  -0.09120 172 ALA A CB  
1287 N N   . GLU A 179 ? 0.27280 0.30350 0.37240 -0.09830 0.01140  -0.08810 173 GLU A N   
1288 C CA  . GLU A 179 ? 0.31370 0.35650 0.41630 -0.10240 0.00770  -0.09080 173 GLU A CA  
1289 C C   . GLU A 179 ? 0.29460 0.35470 0.40400 -0.09840 0.00710  -0.08830 173 GLU A C   
1290 O O   . GLU A 179 ? 0.33300 0.40500 0.44490 -0.09890 0.00400  -0.09160 173 GLU A O   
1291 C CB  . GLU A 179 ? 0.33950 0.37870 0.44340 -0.10880 0.00630  -0.08770 173 GLU A CB  
1292 C CG  . GLU A 179 ? 0.37740 0.39990 0.47660 -0.11370 0.00430  -0.09060 173 GLU A CG  
1293 C CD  . GLU A 179 ? 0.42160 0.44010 0.52440 -0.12030 0.00230  -0.08490 173 GLU A CD  
1294 O OE1 . GLU A 179 ? 0.40490 0.43420 0.51310 -0.12080 0.00370  -0.07920 173 GLU A OE1 
1295 O OE2 . GLU A 179 ? 0.46370 0.46840 0.56470 -0.12520 -0.00090 -0.08650 173 GLU A OE2 
1296 N N   . LEU A 180 ? 0.24000 0.30130 0.35250 -0.09430 0.00960  -0.08270 174 LEU A N   
1297 C CA  . LEU A 180 ? 0.24260 0.31820 0.36250 -0.08990 0.00850  -0.08090 174 LEU A CA  
1298 C C   . LEU A 180 ? 0.26290 0.34410 0.38510 -0.08520 0.00650  -0.08180 174 LEU A C   
1299 O O   . LEU A 180 ? 0.24000 0.33500 0.36920 -0.08310 0.00330  -0.08120 174 LEU A O   
1300 C CB  . LEU A 180 ? 0.24360 0.31750 0.36520 -0.08650 0.01120  -0.07620 174 LEU A CB  
1301 C CG  . LEU A 180 ? 0.32410 0.40120 0.44710 -0.09100 0.01290  -0.07530 174 LEU A CG  
1302 C CD1 . LEU A 180 ? 0.22350 0.30010 0.34730 -0.08790 0.01570  -0.07240 174 LEU A CD1 
1303 C CD2 . LEU A 180 ? 0.27270 0.36540 0.40290 -0.09320 0.01070  -0.07760 174 LEU A CD2 
1304 N N   . CYS A 181 ? 0.23290 0.30480 0.35110 -0.08350 0.00810  -0.08220 175 CYS A N   
1305 C CA  . CYS A 181 ? 0.23430 0.31370 0.35580 -0.07990 0.00610  -0.08280 175 CYS A CA  
1306 C C   . CYS A 181 ? 0.29730 0.38540 0.41640 -0.08360 0.00330  -0.09000 175 CYS A C   
1307 O O   . CYS A 181 ? 0.25880 0.35920 0.38160 -0.08130 0.00070  -0.09040 175 CYS A O   
1308 C CB  . CYS A 181 ? 0.23920 0.30730 0.35830 -0.07770 0.00920  -0.08150 175 CYS A CB  
1309 S SG  . CYS A 181 ? 0.27610 0.33640 0.39800 -0.07270 0.01080  -0.07210 175 CYS A SG  
1310 N N   . ASP A 182 ? 0.27980 0.36240 0.39270 -0.08960 0.00310  -0.09520 176 ASP A N   
1311 C CA  . ASP A 182 ? 0.31450 0.40110 0.42170 -0.09390 0.00020  -0.10370 176 ASP A CA  
1312 C C   . ASP A 182 ? 0.29420 0.37570 0.39530 -0.09250 0.00210  -0.11020 176 ASP A C   
1313 O O   . ASP A 182 ? 0.31930 0.41410 0.41830 -0.09250 -0.00070 -0.11580 176 ASP A O   
1314 C CB  . ASP A 182 ? 0.30830 0.41570 0.42110 -0.09390 -0.00500 -0.10290 176 ASP A CB  
1315 C CG  . ASP A 182 ? 0.29900 0.41160 0.41860 -0.09530 -0.00650 -0.09760 176 ASP A CG  
1316 O OD1 . ASP A 182 ? 0.31210 0.41510 0.42920 -0.09980 -0.00520 -0.09830 176 ASP A OD1 
1317 O OD2 . ASP A 182 ? 0.30760 0.43450 0.43620 -0.09180 -0.00920 -0.09240 176 ASP A OD2 
1318 N N   . LEU A 183 ? 0.27750 0.34080 0.37550 -0.09120 0.00680  -0.10950 177 LEU A N   
1319 C CA  . LEU A 183 ? 0.26100 0.31620 0.35400 -0.08930 0.00990  -0.11570 177 LEU A CA  
1320 C C   . LEU A 183 ? 0.34400 0.37650 0.42780 -0.09150 0.01220  -0.12100 177 LEU A C   
1321 O O   . LEU A 183 ? 0.35290 0.37550 0.43740 -0.09430 0.01210  -0.11570 177 LEU A O   
1322 C CB  . LEU A 183 ? 0.26960 0.32260 0.37000 -0.08410 0.01350  -0.10730 177 LEU A CB  
1323 C CG  . LEU A 183 ? 0.30480 0.37740 0.41320 -0.07760 0.01050  -0.09770 177 LEU A CG  
1324 C CD1 . LEU A 183 ? 0.29410 0.35960 0.40860 -0.07210 0.01310  -0.08640 177 LEU A CD1 
1325 C CD2 . LEU A 183 ? 0.31050 0.39600 0.41070 -0.07080 0.00870  -0.09760 177 LEU A CD2 
1326 N N   . ASP A 184 ? 0.37840 0.40330 0.45370 -0.08960 0.01400  -0.13120 178 ASP A N   
1327 C CA  . ASP A 184 ? 0.40650 0.40730 0.47520 -0.08950 0.01650  -0.13470 178 ASP A CA  
1328 C C   . ASP A 184 ? 0.37360 0.36110 0.44810 -0.08630 0.02180  -0.12520 178 ASP A C   
1329 O O   . ASP A 184 ? 0.33240 0.32710 0.41290 -0.08250 0.02430  -0.11900 178 ASP A O   
1330 C CB  . ASP A 184 ? 0.46460 0.45970 0.52090 -0.08550 0.01770  -0.14890 178 ASP A CB  
1331 C CG  . ASP A 184 ? 0.61410 0.62170 0.66200 -0.08850 0.01170  -0.15810 178 ASP A CG  
1332 O OD1 . ASP A 184 ? 0.61780 0.62150 0.66620 -0.09480 0.00680  -0.15710 178 ASP A OD1 
1333 O OD2 . ASP A 184 ? 0.72780 0.75060 0.76740 -0.08240 0.01170  -0.16220 178 ASP A OD2 
1334 N N   . ALA A 185 ? 0.36050 0.32930 0.43380 -0.08790 0.02230  -0.12240 179 ALA A N   
1335 C CA  . ALA A 185 ? 0.39040 0.34700 0.46840 -0.08540 0.02640  -0.11220 179 ALA A CA  
1336 C C   . ALA A 185 ? 0.39800 0.35090 0.47720 -0.07860 0.03240  -0.11340 179 ALA A C   
1337 O O   . ALA A 185 ? 0.39830 0.35250 0.48450 -0.07650 0.03490  -0.10260 179 ALA A O   
1338 C CB  . ALA A 185 ? 0.34660 0.28370 0.42260 -0.08780 0.02510  -0.11150 179 ALA A CB  
1339 N N   . GLY A 186 ? 0.42230 0.37230 0.49270 -0.07250 0.03420  -0.12360 180 GLY A N   
1340 C CA  . GLY A 186 ? 0.33580 0.28800 0.40350 -0.05970 0.03910  -0.11560 180 GLY A CA  
1341 C C   . GLY A 186 ? 0.39290 0.36900 0.46180 -0.05370 0.03790  -0.10600 180 GLY A C   
1342 O O   . GLY A 186 ? 0.39500 0.37580 0.46280 -0.04340 0.04130  -0.09740 180 GLY A O   
1343 N N   . ASP A 187 ? 0.37560 0.36790 0.44790 -0.05960 0.03270  -0.10640 181 ASP A N   
1344 C CA  . ASP A 187 ? 0.35710 0.37080 0.43390 -0.05430 0.03050  -0.09580 181 ASP A CA  
1345 C C   . ASP A 187 ? 0.27470 0.28830 0.36370 -0.05680 0.02960  -0.08400 181 ASP A C   
1346 O O   . ASP A 187 ? 0.35370 0.38310 0.44880 -0.05320 0.02660  -0.07510 181 ASP A O   
1347 C CB  . ASP A 187 ? 0.35550 0.38920 0.43060 -0.05760 0.02500  -0.10180 181 ASP A CB  
1348 C CG  . ASP A 187 ? 0.49040 0.53410 0.55270 -0.05090 0.02540  -0.10810 181 ASP A CG  
1349 O OD1 . ASP A 187 ? 0.49880 0.53250 0.55350 -0.04350 0.03060  -0.10960 181 ASP A OD1 
1350 O OD2 . ASP A 187 ? 0.61670 0.67960 0.67680 -0.05250 0.02070  -0.11120 181 ASP A OD2 
1351 N N   . VAL A 188 ? 0.30220 0.29900 0.39500 -0.06310 0.03150  -0.08360 182 VAL A N   
1352 C CA  . VAL A 188 ? 0.25590 0.25130 0.35810 -0.06520 0.03120  -0.07310 182 VAL A CA  
1353 C C   . VAL A 188 ? 0.26350 0.24230 0.36560 -0.06160 0.03570  -0.06510 182 VAL A C   
1354 O O   . VAL A 188 ? 0.30180 0.26410 0.40090 -0.06440 0.03870  -0.07000 182 VAL A O   
1355 C CB  . VAL A 188 ? 0.26200 0.25590 0.36660 -0.07440 0.02900  -0.07610 182 VAL A CB  
1356 C CG1 . VAL A 188 ? 0.23580 0.22770 0.34140 -0.07180 0.02800  -0.06290 182 VAL A CG1 
1357 C CG2 . VAL A 188 ? 0.26710 0.27850 0.37280 -0.07660 0.02450  -0.08130 182 VAL A CG2 
1358 N N   . GLU A 189 ? 0.22800 0.21070 0.33470 -0.05570 0.03540  -0.05230 183 GLU A N   
1359 C CA  . GLU A 189 ? 0.27100 0.24020 0.37890 -0.05190 0.03920  -0.04280 183 GLU A CA  
1360 C C   . GLU A 189 ? 0.26220 0.22500 0.37650 -0.05870 0.03800  -0.03570 183 GLU A C   
1361 O O   . GLU A 189 ? 0.25700 0.23010 0.37070 -0.06040 0.03290  -0.03520 183 GLU A O   
1362 C CB  . GLU A 189 ? 0.31230 0.29080 0.42080 -0.04080 0.03960  -0.03200 183 GLU A CB  
1363 C CG  . GLU A 189 ? 0.37480 0.35730 0.47480 -0.03330 0.04300  -0.03880 183 GLU A CG  
1364 C CD  . GLU A 189 ? 0.52620 0.52750 0.62700 -0.02370 0.04190  -0.02940 183 GLU A CD  
1365 O OE1 . GLU A 189 ? 0.53090 0.53720 0.64020 -0.02210 0.03890  -0.01540 183 GLU A OE1 
1366 O OE2 . GLU A 189 ? 0.59060 0.60230 0.68340 -0.01820 0.04340  -0.03580 183 GLU A OE2 
1367 N N   . TRP A 190 ? 0.23220 0.18190 0.34310 -0.05730 0.03970  -0.02850 184 TRP A N   
1368 C CA  . TRP A 190 ? 0.26400 0.21360 0.36690 -0.05860 0.03440  -0.02080 184 TRP A CA  
1369 C C   . TRP A 190 ? 0.23240 0.17770 0.33470 -0.05390 0.03380  -0.00770 184 TRP A C   
1370 O O   . TRP A 190 ? 0.27880 0.21550 0.38460 -0.05030 0.03840  -0.00450 184 TRP A O   
1371 C CB  . TRP A 190 ? 0.24320 0.18570 0.33960 -0.06370 0.03380  -0.02500 184 TRP A CB  
1372 C CG  . TRP A 190 ? 0.25960 0.20870 0.35520 -0.06840 0.03260  -0.03600 184 TRP A CG  
1373 C CD1 . TRP A 190 ? 0.22350 0.17120 0.32080 -0.06980 0.03510  -0.04760 184 TRP A CD1 
1374 C CD2 . TRP A 190 ? 0.25540 0.21460 0.34820 -0.07190 0.02840  -0.03640 184 TRP A CD2 
1375 N NE1 . TRP A 190 ? 0.25690 0.21410 0.35210 -0.07410 0.03180  -0.05380 184 TRP A NE1 
1376 C CE2 . TRP A 190 ? 0.30330 0.26750 0.39680 -0.07510 0.02840  -0.04670 184 TRP A CE2 
1377 C CE3 . TRP A 190 ? 0.26720 0.23180 0.35700 -0.07260 0.02500  -0.02950 184 TRP A CE3 
1378 C CZ2 . TRP A 190 ? 0.25920 0.23350 0.35190 -0.07840 0.02540  -0.04880 184 TRP A CZ2 
1379 C CZ3 . TRP A 190 ? 0.24540 0.21930 0.33500 -0.07600 0.02300  -0.03320 184 TRP A CZ3 
1380 C CH2 . TRP A 190 ? 0.28260 0.26160 0.37420 -0.07860 0.02340  -0.04210 184 TRP A CH2 
1381 N N   . GLY A 191 ? 0.26320 0.21440 0.36050 -0.05380 0.02830  -0.00090 185 GLY A N   
1382 C CA  . GLY A 191 ? 0.26620 0.21390 0.35870 -0.05090 0.02620  0.00980  185 GLY A CA  
1383 C C   . GLY A 191 ? 0.29810 0.24500 0.37900 -0.05650 0.02200  0.01090  185 GLY A C   
1384 O O   . GLY A 191 ? 0.31210 0.26000 0.39110 -0.06170 0.02140  0.00530  185 GLY A O   
1385 N N   . THR A 192 ? 0.26570 0.21190 0.33950 -0.05580 0.01930  0.01780  186 THR A N   
1386 C CA  . THR A 192 ? 0.29140 0.23740 0.35590 -0.06180 0.01690  0.01850  186 THR A CA  
1387 C C   . THR A 192 ? 0.28290 0.23450 0.34630 -0.06160 0.01440  0.01820  186 THR A C   
1388 O O   . THR A 192 ? 0.28500 0.23740 0.35220 -0.05580 0.01350  0.02220  186 THR A O   
1389 C CB  . THR A 192 ? 0.31510 0.25480 0.37890 -0.06120 0.01840  0.02490  186 THR A CB  
1390 O OG1 . THR A 192 ? 0.31890 0.25220 0.38520 -0.06120 0.02070  0.02450  186 THR A OG1 
1391 C CG2 . THR A 192 ? 0.32990 0.26990 0.38760 -0.06820 0.01760  0.02560  186 THR A CG2 
1392 N N   . ASP A 193 ? 0.30440 0.26030 0.36450 -0.06760 0.01250  0.01430  187 ASP A N   
1393 C CA  . ASP A 193 ? 0.31070 0.27140 0.37040 -0.06810 0.01010  0.01210  187 ASP A CA  
1394 C C   . ASP A 193 ? 0.32180 0.27890 0.37720 -0.06960 0.01080  0.01530  187 ASP A C   
1395 O O   . ASP A 193 ? 0.26550 0.21780 0.31790 -0.07130 0.01310  0.01920  187 ASP A O   
1396 C CB  . ASP A 193 ? 0.33680 0.30560 0.39930 -0.07260 0.00750  0.00720  187 ASP A CB  
1397 C CG  . ASP A 193 ? 0.37240 0.34750 0.44420 -0.06880 0.00650  0.00130  187 ASP A CG  
1398 O OD1 . ASP A 193 ? 0.34980 0.32300 0.42390 -0.06410 0.00560  0.00310  187 ASP A OD1 
1399 O OD2 . ASP A 193 ? 0.38130 0.36390 0.46010 -0.06970 0.00690  -0.00540 187 ASP A OD2 
1400 N N   . GLY A 194 ? 0.30200 0.26160 0.35910 -0.06880 0.00860  0.01320  188 GLY A N   
1401 C CA  . GLY A 194 ? 0.33270 0.28960 0.38830 -0.07030 0.00910  0.01520  188 GLY A CA  
1402 C C   . GLY A 194 ? 0.36410 0.32310 0.41280 -0.07720 0.01300  0.01180  188 GLY A C   
1403 O O   . GLY A 194 ? 0.31940 0.27560 0.37080 -0.07780 0.01560  0.01510  188 GLY A O   
1404 N N   . CYS A 195 ? 0.36600 0.33240 0.40900 -0.08180 0.00870  0.01000  189 CYS A N   
1405 C CA  . CYS A 195 ? 0.36680 0.34320 0.42130 -0.08370 -0.00180 0.02060  189 CYS A CA  
1406 C C   . CYS A 195 ? 0.32800 0.30130 0.37770 -0.08670 0.00180  0.02330  189 CYS A C   
1407 O O   . CYS A 195 ? 0.35630 0.33770 0.44450 -0.08000 0.00560  0.02630  189 CYS A O   
1408 C CB  . CYS A 195 ? 0.32050 0.30590 0.39820 -0.08270 0.00120  0.01240  189 CYS A CB  
1409 S SG  . CYS A 195 ? 0.35860 0.34470 0.43490 -0.08350 0.00440  0.00660  189 CYS A SG  
1410 N N   . ASN A 196 ? 0.37520 0.33610 0.41550 -0.08550 0.01260  0.01690  190 ASN A N   
1411 C CA  . ASN A 196 ? 0.38610 0.34050 0.42690 -0.08640 0.01580  0.02000  190 ASN A CA  
1412 C C   . ASN A 196 ? 0.39010 0.34930 0.43980 -0.08770 0.01050  0.02190  190 ASN A C   
1413 O O   . ASN A 196 ? 0.38420 0.33770 0.43340 -0.09020 0.01270  0.02380  190 ASN A O   
1414 C CB  . ASN A 196 ? 0.39380 0.34500 0.43500 -0.08900 0.02460  0.01930  190 ASN A CB  
1415 C CG  . ASN A 196 ? 0.38510 0.32770 0.42950 -0.08800 0.02480  0.02700  190 ASN A CG  
1416 O OD1 . ASN A 196 ? 0.37990 0.31740 0.42700 -0.08330 0.02230  0.03120  190 ASN A OD1 
1417 N ND2 . ASN A 196 ? 0.46920 0.41090 0.51660 -0.09190 0.02870  0.02910  190 ASN A ND2 
1418 N N   . LEU A 197 ? 0.33700 0.30380 0.39770 -0.08540 0.00790  0.01840  191 LEU A N   
1419 C CA  . LEU A 197 ? 0.34080 0.30850 0.40940 -0.08630 0.00940  0.01400  191 LEU A CA  
1420 C C   . LEU A 197 ? 0.34750 0.30900 0.41440 -0.08150 0.01150  0.00990  191 LEU A C   
1421 O O   . LEU A 197 ? 0.30890 0.26890 0.37280 -0.07720 0.01160  0.01030  191 LEU A O   
1422 C CB  . LEU A 197 ? 0.31500 0.29340 0.39160 -0.08690 0.00970  0.00790  191 LEU A CB  
1423 C CG  . LEU A 197 ? 0.33660 0.32320 0.42010 -0.09140 0.01060  0.00950  191 LEU A CG  
1424 C CD1 . LEU A 197 ? 0.33200 0.32860 0.41720 -0.09160 0.01410  -0.00060 191 LEU A CD1 
1425 C CD2 . LEU A 197 ? 0.34720 0.33200 0.43430 -0.09600 0.01160  0.01190  191 LEU A CD2 
1426 N N   . PRO A 198 ? 0.33750 0.29630 0.40790 -0.08140 0.01320  0.00580  192 PRO A N   
1427 C CA  . PRO A 198 ? 0.26110 0.21710 0.33470 -0.07600 0.01640  0.00020  192 PRO A CA  
1428 C C   . PRO A 198 ? 0.30090 0.26620 0.37860 -0.07370 0.01660  -0.00600 192 PRO A C   
1429 O O   . PRO A 198 ? 0.30600 0.27940 0.38550 -0.07630 0.01580  -0.00940 192 PRO A O   
1430 C CB  . PRO A 198 ? 0.27230 0.22320 0.34940 -0.07840 0.01870  -0.00510 192 PRO A CB  
1431 C CG  . PRO A 198 ? 0.30500 0.25390 0.37970 -0.08470 0.01570  0.00090  192 PRO A CG  
1432 C CD  . PRO A 198 ? 0.34680 0.30490 0.42050 -0.08680 0.01330  0.00520  192 PRO A CD  
1433 N N   . THR A 199 ? 0.25100 0.21630 0.33220 -0.06860 0.01810  -0.00750 193 THR A N   
1434 C CA  . THR A 199 ? 0.25460 0.22900 0.34060 -0.06640 0.01710  -0.01200 193 THR A CA  
1435 C C   . THR A 199 ? 0.27140 0.24720 0.36480 -0.06330 0.01980  -0.01680 193 THR A C   
1436 O O   . THR A 199 ? 0.24750 0.21670 0.34290 -0.06060 0.02230  -0.01340 193 THR A O   
1437 C CB  . THR A 199 ? 0.25720 0.23240 0.34120 -0.06420 0.01380  -0.00610 193 THR A CB  
1438 O OG1 . THR A 199 ? 0.26830 0.25230 0.35830 -0.06280 0.01190  -0.01100 193 THR A OG1 
1439 C CG2 . THR A 199 ? 0.31340 0.28330 0.39830 -0.05930 0.01420  0.00070  193 THR A CG2 
1440 N N   . PRO A 200 ? 0.22510 0.21000 0.32320 -0.06400 0.01970  -0.02480 194 PRO A N   
1441 C CA  . PRO A 200 ? 0.22150 0.20950 0.32610 -0.06300 0.02200  -0.03090 194 PRO A CA  
1442 C C   . PRO A 200 ? 0.19630 0.19250 0.31070 -0.05870 0.02000  -0.02820 194 PRO A C   
1443 O O   . PRO A 200 ? 0.19840 0.20000 0.31540 -0.05640 0.01580  -0.02420 194 PRO A O   
1444 C CB  . PRO A 200 ? 0.20830 0.20400 0.31200 -0.06680 0.02150  -0.04000 194 PRO A CB  
1445 C CG  . PRO A 200 ? 0.22490 0.22730 0.32810 -0.06650 0.01830  -0.03780 194 PRO A CG  
1446 C CD  . PRO A 200 ? 0.21880 0.21210 0.31630 -0.06650 0.01790  -0.02940 194 PRO A CD  
1447 N N   . ALA A 201 ? 0.21040 0.20840 0.33220 -0.05780 0.02300  -0.03050 195 ALA A N   
1448 C CA  . ALA A 201 ? 0.15430 0.16590 0.28770 -0.05370 0.02040  -0.02730 195 ALA A CA  
1449 C C   . ALA A 201 ? 0.21190 0.23430 0.34120 -0.05310 0.02050  -0.03670 195 ALA A C   
1450 O O   . ALA A 201 ? 0.21590 0.23110 0.33700 -0.05480 0.02470  -0.04410 195 ALA A O   
1451 C CB  . ALA A 201 ? 0.16810 0.17600 0.30150 -0.04600 0.02150  -0.01460 195 ALA A CB  
1452 N N   . PHE A 202 ? 0.19080 0.22990 0.32650 -0.05160 0.01520  -0.03710 196 PHE A N   
1453 C CA  . PHE A 202 ? 0.17560 0.22810 0.30810 -0.05150 0.01400  -0.04470 196 PHE A CA  
1454 C C   . PHE A 202 ? 0.17890 0.25010 0.32090 -0.04620 0.00760  -0.03710 196 PHE A C   
1455 O O   . PHE A 202 ? 0.20360 0.27550 0.35530 -0.04330 0.00380  -0.02750 196 PHE A O   
1456 C CB  . PHE A 202 ? 0.18660 0.23920 0.31800 -0.06040 0.01440  -0.05740 196 PHE A CB  
1457 C CG  . PHE A 202 ? 0.19420 0.24340 0.32750 -0.06230 0.01260  -0.05540 196 PHE A CG  
1458 C CD1 . PHE A 202 ? 0.17470 0.23570 0.31440 -0.05910 0.00730  -0.05230 196 PHE A CD1 
1459 C CD2 . PHE A 202 ? 0.19950 0.23340 0.32300 -0.06460 0.01570  -0.05490 196 PHE A CD2 
1460 C CE1 . PHE A 202 ? 0.20280 0.26020 0.33990 -0.05850 0.00630  -0.05110 196 PHE A CE1 
1461 C CE2 . PHE A 202 ? 0.18090 0.21420 0.30180 -0.06430 0.01410  -0.05230 196 PHE A CE2 
1462 C CZ  . PHE A 202 ? 0.23350 0.27830 0.36120 -0.06130 0.01000  -0.05160 196 PHE A CZ  
1463 N N   . PRO A 203 ? 0.20140 0.28820 0.34110 -0.04480 0.00560  -0.04020 197 PRO A N   
1464 C CA  . PRO A 203 ? 0.15520 0.26160 0.30610 -0.04040 -0.00130 -0.03120 197 PRO A CA  
1465 C C   . PRO A 203 ? 0.14780 0.25720 0.31350 -0.04300 -0.00670 -0.03080 197 PRO A C   
1466 O O   . PRO A 203 ? 0.14290 0.24950 0.30910 -0.04910 -0.00560 -0.04080 197 PRO A O   
1467 C CB  . PRO A 203 ? 0.16990 0.29220 0.31430 -0.04130 -0.00230 -0.03770 197 PRO A CB  
1468 C CG  . PRO A 203 ? 0.22900 0.33920 0.35660 -0.04130 0.00480  -0.04550 197 PRO A CG  
1469 C CD  . PRO A 203 ? 0.23380 0.32170 0.36070 -0.04660 0.00890  -0.05070 197 PRO A CD  
1470 N N   . LEU A 204 ? 0.15200 0.26780 0.33040 -0.03790 -0.01280 -0.01870 198 LEU A N   
1471 C CA  . LEU A 204 ? 0.14880 0.25960 0.32880 -0.03670 -0.01720 -0.01690 198 LEU A CA  
1472 C C   . LEU A 204 ? 0.17570 0.29550 0.35460 -0.03930 -0.01880 -0.02370 198 LEU A C   
1473 O O   . LEU A 204 ? 0.14540 0.25770 0.32200 -0.04040 -0.01820 -0.02860 198 LEU A O   
1474 C CB  . LEU A 204 ? 0.15330 0.26650 0.33830 -0.02970 -0.02350 -0.00320 198 LEU A CB  
1475 C CG  . LEU A 204 ? 0.18570 0.29110 0.37230 -0.02690 -0.02790 -0.00210 198 LEU A CG  
1476 C CD1 . LEU A 204 ? 0.13450 0.22210 0.31780 -0.02870 -0.02510 -0.00700 198 LEU A CD1 
1477 C CD2 . LEU A 204 ? 0.15050 0.25540 0.34050 -0.02070 -0.03380 0.01100  198 LEU A CD2 
1478 N N   . ASP A 205 ? 0.13190 0.26910 0.31300 -0.04020 -0.02060 -0.02410 199 ASP A N   
1479 C CA  . ASP A 205 ? 0.15470 0.29930 0.33530 -0.04280 -0.02260 -0.02840 199 ASP A CA  
1480 C C   . ASP A 205 ? 0.15220 0.28630 0.32450 -0.04870 -0.01720 -0.04110 199 ASP A C   
1481 O O   . ASP A 205 ? 0.13580 0.27060 0.30880 -0.04970 -0.01800 -0.04350 199 ASP A O   
1482 C CB  . ASP A 205 ? 0.19080 0.35600 0.37440 -0.04320 -0.02630 -0.02580 199 ASP A CB  
1483 C CG  . ASP A 205 ? 0.16830 0.33800 0.34390 -0.04750 -0.02160 -0.03710 199 ASP A CG  
1484 O OD1 . ASP A 205 ? 0.21730 0.38260 0.38860 -0.04540 -0.01770 -0.03620 199 ASP A OD1 
1485 O OD2 . ASP A 205 ? 0.23480 0.40920 0.40430 -0.05270 -0.02120 -0.04610 199 ASP A OD2 
1486 N N   . ARG A 206 ? 0.17070 0.29550 0.33520 -0.05260 -0.01150 -0.04840 200 ARG A N   
1487 C CA  . ARG A 206 ? 0.18650 0.30010 0.34160 -0.05820 -0.00680 -0.05770 200 ARG A CA  
1488 C C   . ARG A 206 ? 0.16490 0.26690 0.31910 -0.05670 -0.00520 -0.05610 200 ARG A C   
1489 O O   . ARG A 206 ? 0.21930 0.31840 0.36920 -0.06010 -0.00280 -0.06110 200 ARG A O   
1490 C CB  . ARG A 206 ? 0.20060 0.30460 0.34730 -0.06250 -0.00130 -0.06440 200 ARG A CB  
1491 C CG  . ARG A 206 ? 0.20270 0.32060 0.34890 -0.06450 -0.00210 -0.06970 200 ARG A CG  
1492 C CD  . ARG A 206 ? 0.23620 0.36850 0.38180 -0.06680 -0.00660 -0.07280 200 ARG A CD  
1493 N NE  . ARG A 206 ? 0.25950 0.40580 0.39970 -0.06760 -0.00810 -0.07700 200 ARG A NE  
1494 C CZ  . ARG A 206 ? 0.32840 0.47230 0.45660 -0.07320 -0.00720 -0.08790 200 ARG A CZ  
1495 N NH1 . ARG A 206 ? 0.31070 0.44140 0.43550 -0.08010 -0.00520 -0.09550 200 ARG A NH1 
1496 N NH2 . ARG A 206 ? 0.33250 0.48640 0.45000 -0.07070 -0.00870 -0.08960 200 ARG A NH2 
1497 N N   . LEU A 207 ? 0.12970 0.22620 0.28800 -0.05220 -0.00660 -0.04940 201 LEU A N   
1498 C CA  . LEU A 207 ? 0.14610 0.23510 0.30440 -0.05050 -0.00600 -0.04940 201 LEU A CA  
1499 C C   . LEU A 207 ? 0.15900 0.25840 0.32500 -0.04840 -0.00930 -0.05050 201 LEU A C   
1500 O O   . LEU A 207 ? 0.15370 0.25260 0.31900 -0.04980 -0.00680 -0.05580 201 LEU A O   
1501 C CB  . LEU A 207 ? 0.17610 0.25720 0.33750 -0.04620 -0.00810 -0.04210 201 LEU A CB  
1502 C CG  . LEU A 207 ? 0.15690 0.22940 0.31760 -0.04490 -0.00760 -0.04360 201 LEU A CG  
1503 C CD1 . LEU A 207 ? 0.18430 0.24930 0.33410 -0.05020 -0.00120 -0.04930 201 LEU A CD1 
1504 C CD2 . LEU A 207 ? 0.13510 0.19890 0.29870 -0.04100 -0.01070 -0.03660 201 LEU A CD2 
1505 N N   . GLY A 208 ? 0.15180 0.26200 0.32600 -0.04490 -0.01480 -0.04490 202 GLY A N   
1506 C CA  . GLY A 208 ? 0.12570 0.24650 0.30760 -0.04330 -0.01780 -0.04550 202 GLY A CA  
1507 C C   . GLY A 208 ? 0.18700 0.31370 0.36550 -0.04860 -0.01500 -0.05200 202 GLY A C   
1508 O O   . GLY A 208 ? 0.21080 0.34210 0.39410 -0.04850 -0.01430 -0.05560 202 GLY A O   
1509 N N   . ARG A 209 ? 0.18900 0.31620 0.36020 -0.05340 -0.01330 -0.05440 203 ARG A N   
1510 C CA  . ARG A 209 ? 0.17050 0.30270 0.33810 -0.05900 -0.01170 -0.06040 203 ARG A CA  
1511 C C   . ARG A 209 ? 0.16260 0.28690 0.32560 -0.06190 -0.00650 -0.06570 203 ARG A C   
1512 O O   . ARG A 209 ? 0.17860 0.31020 0.34510 -0.06400 -0.00610 -0.06820 203 ARG A O   
1513 C CB  . ARG A 209 ? 0.18860 0.32130 0.34850 -0.06360 -0.01120 -0.06390 203 ARG A CB  
1514 C CG  . ARG A 209 ? 0.18500 0.32410 0.34160 -0.06980 -0.01150 -0.06950 203 ARG A CG  
1515 C CD  . ARG A 209 ? 0.20650 0.34340 0.35320 -0.07500 -0.01050 -0.07630 203 ARG A CD  
1516 N NE  . ARG A 209 ? 0.23170 0.38090 0.38050 -0.07300 -0.01430 -0.07450 203 ARG A NE  
1517 C CZ  . ARG A 209 ? 0.27780 0.43570 0.42060 -0.07720 -0.01610 -0.08060 203 ARG A CZ  
1518 N NH1 . ARG A 209 ? 0.23890 0.39190 0.37310 -0.08410 -0.01530 -0.08890 203 ARG A NH1 
1519 N NH2 . ARG A 209 ? 0.23570 0.40870 0.38040 -0.07450 -0.01940 -0.07780 203 ARG A NH2 
1520 N N   . ILE A 210 ? 0.15540 0.26640 0.31170 -0.06190 -0.00270 -0.06630 204 ILE A N   
1521 C CA  . ILE A 210 ? 0.21410 0.31980 0.36640 -0.06480 0.00200  -0.06980 204 ILE A CA  
1522 C C   . ILE A 210 ? 0.17190 0.28640 0.33370 -0.06170 0.00160  -0.07130 204 ILE A C   
1523 O O   . ILE A 210 ? 0.19930 0.32000 0.36250 -0.06480 0.00420  -0.07490 204 ILE A O   
1524 C CB  . ILE A 210 ? 0.22420 0.31520 0.36900 -0.06470 0.00520  -0.06810 204 ILE A CB  
1525 C CG1 . ILE A 210 ? 0.18940 0.27110 0.32480 -0.06890 0.00710  -0.06860 204 ILE A CG1 
1526 C CG2 . ILE A 210 ? 0.15610 0.24570 0.29960 -0.06610 0.00890  -0.07030 204 ILE A CG2 
1527 C CD1 . ILE A 210 ? 0.20500 0.27410 0.33600 -0.06700 0.00860  -0.06460 204 ILE A CD1 
1528 N N   . TYR A 211 ? 0.19340 0.30900 0.36320 -0.05540 -0.00170 -0.06870 205 TYR A N   
1529 C CA  . TYR A 211 ? 0.16150 0.28430 0.34180 -0.05160 -0.00190 -0.07210 205 TYR A CA  
1530 C C   . TYR A 211 ? 0.14610 0.28370 0.33610 -0.05110 -0.00450 -0.07230 205 TYR A C   
1531 O O   . TYR A 211 ? 0.17360 0.31980 0.37120 -0.05040 -0.00250 -0.07710 205 TYR A O   
1532 C CB  . TYR A 211 ? 0.11170 0.22850 0.29810 -0.04510 -0.00540 -0.06970 205 TYR A CB  
1533 C CG  . TYR A 211 ? 0.18540 0.29080 0.36490 -0.04610 -0.00200 -0.07160 205 TYR A CG  
1534 C CD1 . TYR A 211 ? 0.13880 0.23370 0.30630 -0.04970 0.00010  -0.06770 205 TYR A CD1 
1535 C CD2 . TYR A 211 ? 0.16950 0.27560 0.35470 -0.04380 -0.00050 -0.07800 205 TYR A CD2 
1536 C CE1 . TYR A 211 ? 0.13500 0.21960 0.29550 -0.05120 0.00300  -0.06770 205 TYR A CE1 
1537 C CE2 . TYR A 211 ? 0.13530 0.23230 0.31340 -0.04570 0.00240  -0.07920 205 TYR A CE2 
1538 C CZ  . TYR A 211 ? 0.15920 0.24510 0.32440 -0.04960 0.00400  -0.07290 205 TYR A CZ  
1539 O OH  . TYR A 211 ? 0.19840 0.27510 0.35560 -0.05200 0.00650  -0.07220 205 TYR A OH  
1540 N N   . ALA A 212 ? 0.16300 0.30540 0.35340 -0.05180 -0.00880 -0.06700 206 ALA A N   
1541 C CA  . ALA A 212 ? 0.18080 0.33770 0.37900 -0.05300 -0.01140 -0.06590 206 ALA A CA  
1542 C C   . ALA A 212 ? 0.21860 0.37970 0.41320 -0.05950 -0.00720 -0.07080 206 ALA A C   
1543 O O   . ALA A 212 ? 0.19750 0.37090 0.40120 -0.05990 -0.00730 -0.07190 206 ALA A O   
1544 C CB  . ALA A 212 ? 0.16490 0.32680 0.36250 -0.05390 -0.01670 -0.05920 206 ALA A CB  
1545 N N   . LYS A 213 ? 0.20870 0.35990 0.39090 -0.06470 -0.00380 -0.07310 207 LYS A N   
1546 C CA  . LYS A 213 ? 0.16770 0.32190 0.34650 -0.07160 -0.00070 -0.07620 207 LYS A CA  
1547 C C   . LYS A 213 ? 0.23560 0.39350 0.41820 -0.07130 0.00410  -0.07980 207 LYS A C   
1548 O O   . LYS A 213 ? 0.25890 0.42780 0.44640 -0.07490 0.00560  -0.08110 207 LYS A O   
1549 C CB  . LYS A 213 ? 0.21780 0.35940 0.38340 -0.07710 0.00080  -0.07700 207 LYS A CB  
1550 C CG  . LYS A 213 ? 0.20490 0.34670 0.36710 -0.07890 -0.00340 -0.07610 207 LYS A CG  
1551 C CD  . LYS A 213 ? 0.22490 0.35290 0.37490 -0.08310 -0.00150 -0.07860 207 LYS A CD  
1552 C CE  . LYS A 213 ? 0.23150 0.36270 0.37790 -0.08810 -0.00500 -0.08140 207 LYS A CE  
1553 N NZ  . LYS A 213 ? 0.24180 0.35880 0.37730 -0.09170 -0.00300 -0.08520 207 LYS A NZ  
1554 N N   . LEU A 214 ? 0.17140 0.32140 0.35230 -0.06730 0.00660  -0.08160 208 LEU A N   
1555 C CA  . LEU A 214 ? 0.19410 0.35050 0.38010 -0.06620 0.01100  -0.08670 208 LEU A CA  
1556 C C   . LEU A 214 ? 0.21420 0.38720 0.41560 -0.06200 0.00980  -0.08910 208 LEU A C   
1557 O O   . LEU A 214 ? 0.21950 0.40550 0.42610 -0.06470 0.01310  -0.09200 208 LEU A O   
1558 C CB  . LEU A 214 ? 0.22790 0.37370 0.41130 -0.06190 0.01220  -0.08840 208 LEU A CB  
1559 C CG  . LEU A 214 ? 0.19270 0.32460 0.36220 -0.06650 0.01520  -0.08630 208 LEU A CG  
1560 C CD1 . LEU A 214 ? 0.15610 0.27740 0.32430 -0.06190 0.01460  -0.08610 208 LEU A CD1 
1561 C CD2 . LEU A 214 ? 0.19120 0.32960 0.35800 -0.07260 0.02060  -0.08890 208 LEU A CD2 
1562 N N   . ALA A 215 ? 0.20880 0.38220 0.41860 -0.05540 0.00480  -0.08720 209 ALA A N   
1563 C CA  . ALA A 215 ? 0.21460 0.40260 0.44060 -0.05040 0.00320  -0.08900 209 ALA A CA  
1564 C C   . ALA A 215 ? 0.23040 0.43180 0.46040 -0.05510 0.00210  -0.08520 209 ALA A C   
1565 O O   . ALA A 215 ? 0.20410 0.42050 0.44550 -0.05410 0.00390  -0.08760 209 ALA A O   
1566 C CB  . ALA A 215 ? 0.16820 0.35230 0.40250 -0.04290 -0.00310 -0.08530 209 ALA A CB  
1567 N N   . SER A 216 ? 0.18240 0.37920 0.40390 -0.06030 -0.00110 -0.07960 210 SER A N   
1568 C CA  . SER A 216 ? 0.23890 0.44740 0.46390 -0.06590 -0.00310 -0.07620 210 SER A CA  
1569 C C   . SER A 216 ? 0.20630 0.42070 0.42970 -0.07210 0.00210  -0.07940 210 SER A C   
1570 O O   . SER A 216 ? 0.18160 0.41120 0.41480 -0.07440 0.00190  -0.07780 210 SER A O   
1571 C CB  . SER A 216 ? 0.23980 0.44120 0.45520 -0.07040 -0.00740 -0.07200 210 SER A CB  
1572 O OG  . SER A 216 ? 0.24430 0.45760 0.46500 -0.07550 -0.01080 -0.06880 210 SER A OG  
1573 N N   . ALA A 217 ? 0.21440 0.41810 0.42650 -0.07520 0.00650  -0.08250 211 ALA A N   
1574 C CA  . ALA A 217 ? 0.27470 0.48550 0.48620 -0.08150 0.01110  -0.08370 211 ALA A CA  
1575 C C   . ALA A 217 ? 0.29050 0.51780 0.51440 -0.07730 0.01540  -0.08780 211 ALA A C   
1576 O O   . ALA A 217 ? 0.26520 0.50810 0.49650 -0.08100 0.01730  -0.08650 211 ALA A O   
1577 C CB  . ALA A 217 ? 0.25900 0.45510 0.45640 -0.08590 0.01440  -0.08450 211 ALA A CB  
1578 N N   . ALA A 218 ? 0.22620 0.45120 0.45370 -0.06920 0.01670  -0.09290 212 ALA A N   
1579 C CA  . ALA A 218 ? 0.20650 0.44770 0.44710 -0.06370 0.02060  -0.09880 212 ALA A CA  
1580 C C   . ALA A 218 ? 0.27370 0.53150 0.53000 -0.06120 0.01780  -0.09560 212 ALA A C   
1581 O O   . ALA A 218 ? 0.27420 0.55030 0.54030 -0.06110 0.02190  -0.09720 212 ALA A O   
1582 C CB  . ALA A 218 ? 0.23750 0.47080 0.48060 -0.05500 0.02040  -0.10550 212 ALA A CB  
1583 N N   . ASP A 219 ? 0.22430 0.47760 0.48360 -0.05930 0.01100  -0.09000 213 ASP A N   
1584 C CA  . ASP A 219 ? 0.25450 0.52340 0.52880 -0.05790 0.00750  -0.08480 213 ASP A CA  
1585 C C   . ASP A 219 ? 0.28960 0.57060 0.56500 -0.06670 0.00860  -0.08030 213 ASP A C   
1586 O O   . ASP A 219 ? 0.32570 0.62550 0.61550 -0.06550 0.01020  -0.07890 213 ASP A O   
1587 C CB  . ASP A 219 ? 0.22080 0.48240 0.49500 -0.05630 -0.00030 -0.07790 213 ASP A CB  
1588 C CG  . ASP A 219 ? 0.25950 0.51530 0.54050 -0.04650 -0.00270 -0.07990 213 ASP A CG  
1589 O OD1 . ASP A 219 ? 0.29400 0.55500 0.58510 -0.03970 0.00060  -0.08710 213 ASP A OD1 
1590 O OD2 . ASP A 219 ? 0.21850 0.46530 0.49550 -0.04570 -0.00840 -0.07410 213 ASP A OD2 
1591 N N   . GLY A 220 ? 0.24510 0.51530 0.50650 -0.07540 0.00730  -0.07770 214 GLY A N   
1592 C CA  . GLY A 220 ? 0.33050 0.61010 0.59400 -0.08430 0.00690  -0.07310 214 GLY A CA  
1593 C C   . GLY A 220 ? 0.46430 0.75620 0.73120 -0.08660 0.01400  -0.07540 214 GLY A C   
1594 O O   . GLY A 220 ? 0.49680 0.80550 0.77460 -0.09050 0.01440  -0.07110 214 GLY A O   
1595 N N   . SER A 221 ? 0.38090 0.66570 0.63920 -0.08460 0.01950  -0.08130 215 SER A N   
1596 C CA  . SER A 221 ? 0.36280 0.66160 0.62390 -0.08630 0.02670  -0.08350 215 SER A CA  
1597 C C   . SER A 221 ? 0.44820 0.76880 0.72660 -0.07840 0.03020  -0.08630 215 SER A C   
1598 O O   . SER A 221 ? 0.46270 0.80290 0.75040 -0.08100 0.03390  -0.08350 215 SER A O   
1599 C CB  . SER A 221 ? 0.36720 0.65410 0.61520 -0.08560 0.03130  -0.08930 215 SER A CB  
1600 O OG  . SER A 221 ? 0.41550 0.71790 0.66540 -0.08750 0.03840  -0.09080 215 SER A OG  
1601 N N   . ASP A 222 ? 0.50060 0.81830 0.78490 -0.06840 0.02880  -0.09150 216 ASP A N   
1602 C CA  . ASP A 222 ? 0.51740 0.85420 0.81940 -0.05930 0.03170  -0.09520 216 ASP A CA  
1603 C C   . ASP A 222 ? 0.55900 0.91240 0.87650 -0.06090 0.02870  -0.08650 216 ASP A C   
1604 O O   . ASP A 222 ? 0.64070 1.01380 0.97410 -0.05470 0.03250  -0.08770 216 ASP A O   
1605 C CB  . ASP A 222 ? 0.55070 0.87780 0.85730 -0.04850 0.02890  -0.10160 216 ASP A CB  
1606 C CG  . ASP A 222 ? 0.66320 0.99760 0.97470 -0.03950 0.03520  -0.11340 216 ASP A CG  
1607 O OD1 . ASP A 222 ? 0.71890 1.04660 1.01760 -0.04160 0.03940  -0.11950 216 ASP A OD1 
1608 O OD2 . ASP A 222 ? 0.67920 1.02590 1.00750 -0.03020 0.03570  -0.11660 216 ASP A OD2 
1609 N N   . ALA A 223 ? 0.35370 0.91930 0.90640 -0.09710 -0.07390 -0.01040 217 ALA A N   
1610 C CA  . ALA A 223 ? 0.42340 1.02960 1.02550 -0.09830 -0.11180 -0.01800 217 ALA A CA  
1611 C C   . ALA A 223 ? 0.34770 0.97580 0.95520 -0.12600 -0.11710 -0.02140 217 ALA A C   
1612 O O   . ALA A 223 ? 0.36840 1.03200 1.01280 -0.13040 -0.15080 -0.03010 217 ALA A O   
1613 C CB  . ALA A 223 ? 0.36200 0.97910 0.90990 -0.09300 -0.15780 -0.00830 217 ALA A CB  
1614 N N   . GLY A 224 ? 0.37280 0.96210 0.97890 -0.13930 -0.09120 -0.01920 218 GLY A N   
1615 C CA  . GLY A 224 ? 0.47680 1.06680 1.11000 -0.15870 -0.09030 -0.03300 218 GLY A CA  
1616 C C   . GLY A 224 ? 0.53870 1.12340 1.15440 -0.17600 -0.13040 -0.05100 218 GLY A C   
1617 O O   . GLY A 224 ? 0.47000 1.07280 1.12170 -0.19120 -0.14400 -0.05960 218 GLY A O   
1618 N N   . GLU A 225 ? 0.63730 1.19440 1.18930 -0.17270 -0.14410 -0.06610 219 GLU A N   
1619 C CA  . GLU A 225 ? 0.67420 1.22470 1.18540 -0.18570 -0.18390 -0.08790 219 GLU A CA  
1620 C C   . GLU A 225 ? 0.69790 1.21250 1.18070 -0.20320 -0.16500 -0.10980 219 GLU A C   
1621 O O   . GLU A 225 ? 0.65270 1.13960 1.11490 -0.20090 -0.12330 -0.11080 219 GLU A O   
1622 C CB  . GLU A 225 ? 0.69460 1.24010 1.12400 -0.17350 -0.20170 -0.09210 219 GLU A CB  
1623 C CG  . GLU A 225 ? 0.68130 1.25910 1.12710 -0.15490 -0.23180 -0.07260 219 GLU A CG  
1624 C CD  . GLU A 225 ? 0.78140 1.34950 1.13050 -0.14370 -0.24700 -0.06970 219 GLU A CD  
1625 O OE1 . GLU A 225 ? 0.72800 1.26870 1.01030 -0.14710 -0.22170 -0.07880 219 GLU A OE1 
1626 O OE2 . GLU A 225 ? 0.87630 1.46050 1.21690 -0.13090 -0.28350 -0.05680 219 GLU A OE2 
1627 N N   . GLY A 226 ? 0.66660 1.17830 1.14500 -0.22030 -0.19790 -0.12640 220 GLY A N   
1628 C CA  . GLY A 226 ? 0.65570 1.13120 1.10310 -0.23620 -0.18420 -0.14890 220 GLY A CA  
1629 C C   . GLY A 226 ? 0.68950 1.12910 1.05520 -0.23150 -0.15910 -0.15990 220 GLY A C   
1630 O O   . GLY A 226 ? 0.73280 1.15430 1.03010 -0.23550 -0.17860 -0.17550 220 GLY A O   
1631 N N   . GLN A 227 ? 0.63650 1.06180 1.00440 -0.22350 -0.11510 -0.14970 221 GLN A N   
1632 C CA  . GLN A 227 ? 0.55290 0.94510 0.85400 -0.22080 -0.08930 -0.15490 221 GLN A CA  
1633 C C   . GLN A 227 ? 0.57710 0.93120 0.86760 -0.23300 -0.06600 -0.16840 221 GLN A C   
1634 O O   . GLN A 227 ? 0.57520 0.92580 0.91310 -0.23690 -0.05060 -0.16470 221 GLN A O   
1635 C CB  . GLN A 227 ? 0.47560 0.86780 0.78080 -0.20460 -0.05870 -0.13430 221 GLN A CB  
1636 C CG  . GLN A 227 ? 0.44390 0.86250 0.73010 -0.19070 -0.07390 -0.12270 221 GLN A CG  
1637 C CD  . GLN A 227 ? 0.42170 0.83580 0.71400 -0.17490 -0.04280 -0.10310 221 GLN A CD  
1638 O OE1 . GLN A 227 ? 0.40280 0.79720 0.72060 -0.17290 -0.01510 -0.09600 221 GLN A OE1 
1639 N NE2 . GLN A 227 ? 0.26960 0.68730 0.52700 -0.15850 -0.04670 -0.09060 221 GLN A NE2 
1640 N N   . SER A 228 ? 0.55570 0.87940 0.78320 -0.23800 -0.06090 -0.18200 222 SER A N   
1641 C CA  . SER A 228 ? 0.46680 0.75190 0.68460 -0.24550 -0.03280 -0.19010 222 SER A CA  
1642 C C   . SER A 228 ? 0.44180 0.71090 0.66870 -0.23340 0.00300  -0.17080 222 SER A C   
1643 O O   . SER A 228 ? 0.42760 0.70950 0.65610 -0.22050 0.00780  -0.15420 222 SER A O   
1644 C CB  . SER A 228 ? 0.49420 0.74630 0.64450 -0.25230 -0.03150 -0.20670 222 SER A CB  
1645 O OG  . SER A 228 ? 0.51820 0.76610 0.62650 -0.24240 -0.02460 -0.19770 222 SER A OG  
1646 N N   . THR A 229 ? 0.41290 0.65070 0.64230 -0.23660 0.02650  -0.17220 223 THR A N   
1647 C CA  . THR A 229 ? 0.34820 0.56030 0.57000 -0.22390 0.05490  -0.15410 223 THR A CA  
1648 C C   . THR A 229 ? 0.38240 0.58180 0.56130 -0.21480 0.05980  -0.14670 223 THR A C   
1649 O O   . THR A 229 ? 0.33280 0.52710 0.50930 -0.20110 0.06980  -0.12870 223 THR A O   
1650 C CB  . THR A 229 ? 0.39480 0.57330 0.61620 -0.22790 0.07440  -0.15760 223 THR A CB  
1651 O OG1 . THR A 229 ? 0.40210 0.56170 0.59210 -0.23670 0.07370  -0.17390 223 THR A OG1 
1652 C CG2 . THR A 229 ? 0.38020 0.57110 0.65000 -0.23670 0.07330  -0.16290 223 THR A CG2 
1653 N N   . ARG A 230 ? 0.36260 0.55370 0.50590 -0.22260 0.05320  -0.16080 224 ARG A N   
1654 C CA  . ARG A 230 ? 0.40120 0.57840 0.50990 -0.21520 0.06090  -0.15290 224 ARG A CA  
1655 C C   . ARG A 230 ? 0.36450 0.57770 0.47750 -0.20700 0.04680  -0.14290 224 ARG A C   
1656 O O   . ARG A 230 ? 0.33970 0.54500 0.44740 -0.19220 0.05790  -0.12490 224 ARG A O   
1657 C CB  . ARG A 230 ? 0.40330 0.55620 0.46920 -0.22650 0.06190  -0.17090 224 ARG A CB  
1658 C CG  . ARG A 230 ? 0.36760 0.50020 0.39840 -0.20890 0.07060  -0.15590 224 ARG A CG  
1659 C CD  . ARG A 230 ? 0.41060 0.49880 0.40170 -0.21210 0.08600  -0.16640 224 ARG A CD  
1660 N NE  . ARG A 230 ? 0.40840 0.46850 0.42320 -0.22360 0.10970  -0.17000 224 ARG A NE  
1661 C CZ  . ARG A 230 ? 0.48230 0.49920 0.47870 -0.22600 0.13160  -0.17540 224 ARG A CZ  
1662 N NH1 . ARG A 230 ? 0.49560 0.48830 0.44400 -0.21900 0.13600  -0.18020 224 ARG A NH1 
1663 N NH2 . ARG A 230 ? 0.47970 0.47640 0.49930 -0.21750 0.14710  -0.16600 224 ARG A NH2 
1664 N N   . CYS A 231 ? 0.34370 0.59230 0.46470 -0.21060 0.01980  -0.15070 225 CYS A N   
1665 C CA  . CYS A 231 ? 0.33930 0.61530 0.46340 -0.19190 0.00670  -0.13320 225 CYS A CA  
1666 C C   . CYS A 231 ? 0.29700 0.58950 0.46830 -0.18620 0.02170  -0.11820 225 CYS A C   
1667 O O   . CYS A 231 ? 0.27040 0.56380 0.43590 -0.16810 0.02780  -0.10040 225 CYS A O   
1668 C CB  . CYS A 231 ? 0.37600 0.68630 0.50440 -0.19550 -0.02880 -0.14130 225 CYS A CB  
1669 S SG  . CYS A 231 ? 0.54840 0.83280 0.59290 -0.18710 -0.04530 -0.14560 225 CYS A SG  
1670 N N   . ALA A 232 ? 0.32320 0.60730 0.52660 -0.19040 0.02990  -0.11920 226 ALA A N   
1671 C CA  . ALA A 232 ? 0.30220 0.58140 0.53230 -0.17880 0.04690  -0.10200 226 ALA A CA  
1672 C C   . ALA A 232 ? 0.29180 0.53340 0.48750 -0.16730 0.06710  -0.08940 226 ALA A C   
1673 O O   . ALA A 232 ? 0.31200 0.55250 0.50950 -0.15430 0.07480  -0.07490 226 ALA A O   
1674 C CB  . ALA A 232 ? 0.28070 0.55290 0.54510 -0.18680 0.05440  -0.10530 226 ALA A CB  
1675 N N   . ALA A 233 ? 0.31430 0.52270 0.48020 -0.17120 0.07420  -0.09440 227 ALA A N   
1676 C CA  . ALA A 233 ? 0.25800 0.43080 0.39690 -0.15980 0.08620  -0.08140 227 ALA A CA  
1677 C C   . ALA A 233 ? 0.30320 0.48230 0.42460 -0.15060 0.08200  -0.07500 227 ALA A C   
1678 O O   . ALA A 233 ? 0.27010 0.43170 0.38140 -0.13790 0.08720  -0.06150 227 ALA A O   
1679 C CB  . ALA A 233 ? 0.29520 0.43230 0.41780 -0.16450 0.09370  -0.08570 227 ALA A CB  
1680 N N   . LEU A 234 ? 0.23290 0.43640 0.34900 -0.15780 0.07260  -0.08500 228 LEU A N   
1681 C CA  . LEU A 234 ? 0.24950 0.45220 0.34510 -0.14000 0.06870  -0.07360 228 LEU A CA  
1682 C C   . LEU A 234 ? 0.30370 0.53350 0.42020 -0.12770 0.06560  -0.06130 228 LEU A C   
1683 O O   . LEU A 234 ? 0.22750 0.44610 0.33740 -0.11300 0.07170  -0.04850 228 LEU A O   
1684 C CB  . LEU A 234 ? 0.29100 0.49770 0.35870 -0.13840 0.05520  -0.08130 228 LEU A CB  
1685 C CG  . LEU A 234 ? 0.27770 0.44870 0.31720 -0.14730 0.06410  -0.09290 228 LEU A CG  
1686 C CD1 . LEU A 234 ? 0.31720 0.49090 0.32100 -0.14830 0.05000  -0.10340 228 LEU A CD1 
1687 C CD2 . LEU A 234 ? 0.30430 0.44150 0.33490 -0.13420 0.08090  -0.07950 228 LEU A CD2 
1688 N N   . ALA A 235 ? 0.21740 0.48240 0.36560 -0.13410 0.05710  -0.06550 229 ALA A N   
1689 C CA  . ALA A 235 ? 0.20670 0.49690 0.38480 -0.12370 0.05920  -0.05390 229 ALA A CA  
1690 C C   . ALA A 235 ? 0.20710 0.45820 0.37730 -0.11480 0.07740  -0.04360 229 ALA A C   
1691 O O   . ALA A 235 ? 0.27910 0.52800 0.45060 -0.10080 0.08300  -0.03220 229 ALA A O   
1692 C CB  . ALA A 235 ? 0.19850 0.52310 0.42000 -0.13140 0.04720  -0.05890 229 ALA A CB  
1693 N N   . HIS A 236 ? 0.23680 0.45730 0.39740 -0.12310 0.08580  -0.04770 230 HIS A N   
1694 C CA  . HIS A 236 ? 0.24440 0.43090 0.38990 -0.11710 0.09990  -0.03880 230 HIS A CA  
1695 C C   . HIS A 236 ? 0.27740 0.43950 0.39370 -0.10810 0.09940  -0.03230 230 HIS A C   
1696 O O   . HIS A 236 ? 0.27810 0.42800 0.38570 -0.09950 0.10580  -0.02460 230 HIS A O   
1697 C CB  . HIS A 236 ? 0.28280 0.44440 0.42280 -0.12760 0.10770  -0.04330 230 HIS A CB  
1698 C CG  . HIS A 236 ? 0.36580 0.49910 0.49190 -0.12480 0.12350  -0.03560 230 HIS A CG  
1699 N ND1 . HIS A 236 ? 0.39600 0.50540 0.51590 -0.13220 0.13410  -0.03660 230 HIS A ND1 
1700 C CD2 . HIS A 236 ? 0.38580 0.50860 0.49930 -0.11620 0.13240  -0.02780 230 HIS A CD2 
1701 C CE1 . HIS A 236 ? 0.43170 0.51590 0.53160 -0.12880 0.14900  -0.02950 230 HIS A CE1 
1702 N NE2 . HIS A 236 ? 0.43800 0.52860 0.53230 -0.11970 0.14830  -0.02520 230 HIS A NE2 
1703 N N   . ILE A 237 ? 0.27630 0.43020 0.37990 -0.11040 0.09280  -0.03580 231 ILE A N   
1704 C CA  . ILE A 237 ? 0.25970 0.39180 0.34750 -0.10190 0.09210  -0.02870 231 ILE A CA  
1705 C C   . ILE A 237 ? 0.23280 0.38400 0.32790 -0.08820 0.09100  -0.02180 231 ILE A C   
1706 O O   . ILE A 237 ? 0.27830 0.41320 0.36740 -0.08070 0.09400  -0.01520 231 ILE A O   
1707 C CB  . ILE A 237 ? 0.27370 0.39400 0.35510 -0.10600 0.08970  -0.03300 231 ILE A CB  
1708 C CG1 . ILE A 237 ? 0.26600 0.35980 0.34210 -0.11600 0.09210  -0.03680 231 ILE A CG1 
1709 C CG2 . ILE A 237 ? 0.20820 0.31140 0.28720 -0.09540 0.09000  -0.02440 231 ILE A CG2 
1710 C CD1 . ILE A 237 ? 0.26450 0.34570 0.33800 -0.12120 0.09350  -0.04360 231 ILE A CD1 
1711 N N   . PHE A 238 ? 0.24240 0.42960 0.35150 -0.08570 0.08620  -0.02350 232 PHE A N   
1712 C CA  . PHE A 238 ? 0.21810 0.42360 0.33700 -0.06990 0.08570  -0.01430 232 PHE A CA  
1713 C C   . PHE A 238 ? 0.26810 0.46840 0.39720 -0.06370 0.09300  -0.00840 232 PHE A C   
1714 O O   . PHE A 238 ? 0.21770 0.40550 0.34380 -0.05240 0.09740  -0.00160 232 PHE A O   
1715 C CB  . PHE A 238 ? 0.19920 0.44250 0.32740 -0.06720 0.07460  -0.01460 232 PHE A CB  
1716 C CG  . PHE A 238 ? 0.23310 0.49430 0.37230 -0.04840 0.07320  -0.00170 232 PHE A CG  
1717 C CD1 . PHE A 238 ? 0.19240 0.47030 0.36050 -0.04250 0.07840  0.00450  232 PHE A CD1 
1718 C CD2 . PHE A 238 ? 0.24220 0.49640 0.36340 -0.03520 0.06990  0.00530  232 PHE A CD2 
1719 C CE1 . PHE A 238 ? 0.17860 0.46660 0.35960 -0.02460 0.07830  0.01660  232 PHE A CE1 
1720 C CE2 . PHE A 238 ? 0.19160 0.46060 0.32500 -0.01660 0.07100  0.01940  232 PHE A CE2 
1721 C CZ  . PHE A 238 ? 0.15770 0.45050 0.32500 -0.01200 0.07480  0.02540  232 PHE A CZ  
1722 N N   . ARG A 239 ? 0.21160 0.42010 0.35440 -0.07160 0.09710  -0.01160 233 ARG A N   
1723 C CA  A ARG A 239 ? 0.26730 0.46840 0.41730 -0.06660 0.10980  -0.00590 233 ARG A CA  
1724 C CA  B ARG A 239 ? 0.26720 0.46850 0.41720 -0.06630 0.10970  -0.00570 233 ARG A CA  
1725 C C   . ARG A 239 ? 0.30950 0.46910 0.42530 -0.06750 0.11830  -0.00660 233 ARG A C   
1726 O O   . ARG A 239 ? 0.28980 0.43840 0.39930 -0.05960 0.12650  -0.00320 233 ARG A O   
1727 C CB  A ARG A 239 ? 0.25760 0.47090 0.43030 -0.07610 0.11560  -0.00880 233 ARG A CB  
1728 C CB  B ARG A 239 ? 0.25670 0.47140 0.43080 -0.07520 0.11580  -0.00820 233 ARG A CB  
1729 C CG  A ARG A 239 ? 0.30350 0.50410 0.47800 -0.07290 0.13340  -0.00430 233 ARG A CG  
1730 C CG  B ARG A 239 ? 0.26330 0.52340 0.48410 -0.07260 0.10840  -0.00470 233 ARG A CG  
1731 C CD  A ARG A 239 ? 0.36200 0.53680 0.52360 -0.08470 0.14570  -0.00990 233 ARG A CD  
1732 C CD  B ARG A 239 ? 0.25060 0.52290 0.50360 -0.08130 0.11570  -0.00540 233 ARG A CD  
1733 N NE  A ARG A 239 ? 0.35410 0.54680 0.55250 -0.08760 0.15610  -0.00880 233 ARG A NE  
1734 N NE  B ARG A 239 ? 0.30400 0.55030 0.53800 -0.09440 0.12140  -0.01460 233 ARG A NE  
1735 C CZ  A ARG A 239 ? 0.37450 0.55190 0.57540 -0.09690 0.16850  -0.01260 233 ARG A CZ  
1736 C CZ  B ARG A 239 ? 0.25190 0.51060 0.50080 -0.10730 0.11150  -0.02430 233 ARG A CZ  
1737 N NH1 A ARG A 239 ? 0.34930 0.49240 0.51450 -0.10390 0.17210  -0.01680 233 ARG A NH1 
1738 N NH1 B ARG A 239 ? 0.21840 0.51640 0.49810 -0.11130 0.09220  -0.02900 233 ARG A NH1 
1739 N NH2 A ARG A 239 ? 0.32360 0.52000 0.56690 -0.09890 0.17790  -0.01150 233 ARG A NH2 
1740 N NH2 B ARG A 239 ? 0.23330 0.46390 0.46470 -0.11680 0.11990  -0.03030 233 ARG A NH2 
1741 N N   . ALA A 240 ? 0.30900 0.44360 0.40230 -0.07850 0.11650  -0.01170 234 ALA A N   
1742 C CA  . ALA A 240 ? 0.28970 0.38300 0.34930 -0.08260 0.12330  -0.01180 234 ALA A CA  
1743 C C   . ALA A 240 ? 0.30470 0.38860 0.35930 -0.07410 0.11780  -0.00880 234 ALA A C   
1744 O O   . ALA A 240 ? 0.29510 0.35020 0.32710 -0.07020 0.12100  -0.00810 234 ALA A O   
1745 C CB  . ALA A 240 ? 0.29220 0.36170 0.33450 -0.09550 0.12000  -0.01390 234 ALA A CB  
1746 N N   . MET A 241 ? 0.24530 0.34570 0.31740 -0.06770 0.10580  -0.00670 235 MET A N   
1747 C CA  . MET A 241 ? 0.26750 0.35560 0.34290 -0.05500 0.09780  -0.00190 235 MET A CA  
1748 C C   . MET A 241 ? 0.25690 0.36070 0.34610 -0.04300 0.10660  0.00080  235 MET A C   
1749 O O   . MET A 241 ? 0.25240 0.33260 0.33430 -0.03680 0.10570  0.00120  235 MET A O   
1750 C CB  . MET A 241 ? 0.24840 0.34710 0.34000 -0.04980 0.09050  0.00090  235 MET A CB  
1751 C CG  . MET A 241 ? 0.23780 0.31430 0.32190 -0.05990 0.08450  -0.00100 235 MET A CG  
1752 S SD  . MET A 241 ? 0.23740 0.32180 0.33600 -0.05430 0.08540  0.00070  235 MET A SD  
1753 C CE  . MET A 241 ? 0.16570 0.22880 0.28570 -0.03850 0.08270  0.01000  235 MET A CE  
1754 N N   . ALA A 242 ? 0.24390 0.38480 0.35360 -0.03850 0.11070  0.00350  236 ALA A N   
1755 C CA  . ALA A 242 ? 0.25460 0.40970 0.37860 -0.02510 0.11390  0.00860  236 ALA A CA  
1756 C C   . ALA A 242 ? 0.31870 0.45120 0.43010 -0.02780 0.12840  0.00470  236 ALA A C   
1757 O O   . ALA A 242 ? 0.31020 0.43370 0.42510 -0.01880 0.13410  0.00540  236 ALA A O   
1758 C CB  . ALA A 242 ? 0.22900 0.42730 0.37520 -0.02200 0.10880  0.01180  236 ALA A CB  
1759 N N   . ARG A 243 ? 0.30020 0.41820 0.39420 -0.04010 0.13620  -0.00010 237 ARG A N   
1760 C CA  . ARG A 243 ? 0.28760 0.37690 0.36060 -0.04300 0.15420  -0.00410 237 ARG A CA  
1761 C C   . ARG A 243 ? 0.38890 0.42570 0.41430 -0.05020 0.16240  -0.01060 237 ARG A C   
1762 O O   . ARG A 243 ? 0.39390 0.39840 0.39220 -0.04920 0.17800  -0.01480 237 ARG A O   
1763 C CB  . ARG A 243 ? 0.40790 0.50000 0.48120 -0.05200 0.16140  -0.00500 237 ARG A CB  
1764 C CG  . ARG A 243 ? 0.46120 0.59870 0.58070 -0.04700 0.15940  0.00060  237 ARG A CG  
1765 C CD  . ARG A 243 ? 0.53390 0.66980 0.66060 -0.05670 0.17010  -0.00140 237 ARG A CD  
1766 N NE  . ARG A 243 ? 0.65980 0.74450 0.74240 -0.06290 0.18740  -0.00660 237 ARG A NE  
1767 C CZ  . ARG A 243 ? 0.67140 0.73870 0.74430 -0.07210 0.19830  -0.00880 237 ARG A CZ  
1768 N NH1 . ARG A 243 ? 0.64210 0.74040 0.75270 -0.07730 0.19440  -0.00800 237 ARG A NH1 
1769 N NH2 . ARG A 243 ? 0.66110 0.67560 0.68280 -0.07640 0.21360  -0.01180 237 ARG A NH2 
1770 N N   . HIS A 244 ? 0.28650 0.42500 0.42620 -0.07010 0.11680  -0.07010 238 HIS A N   
1771 C CA  . HIS A 244 ? 0.26420 0.39330 0.38330 -0.07370 0.12050  -0.07210 238 HIS A CA  
1772 C C   . HIS A 244 ? 0.25710 0.37880 0.37230 -0.07050 0.11210  -0.07200 238 HIS A C   
1773 O O   . HIS A 244 ? 0.24580 0.36030 0.34780 -0.07490 0.10930  -0.06790 238 HIS A O   
1774 C CB  . HIS A 244 ? 0.27800 0.40300 0.38190 -0.08280 0.12460  -0.06680 238 HIS A CB  
1775 C CG  . HIS A 244 ? 0.32320 0.45560 0.43150 -0.08630 0.13320  -0.06660 238 HIS A CG  
1776 N ND1 . HIS A 244 ? 0.36040 0.49380 0.45900 -0.08840 0.14350  -0.07060 238 HIS A ND1 
1777 C CD2 . HIS A 244 ? 0.29770 0.43760 0.41930 -0.08820 0.13310  -0.06310 238 HIS A CD2 
1778 C CE1 . HIS A 244 ? 0.32950 0.47080 0.43580 -0.09130 0.14970  -0.06920 238 HIS A CE1 
1779 N NE2 . HIS A 244 ? 0.36510 0.51090 0.48600 -0.09140 0.14350  -0.06470 238 HIS A NE2 
1780 N N   . PRO A 245 ? 0.28020 0.40330 0.40690 -0.06270 0.10830  -0.07590 239 PRO A N   
1781 C CA  . PRO A 245 ? 0.24360 0.36010 0.36820 -0.05950 0.10010  -0.07550 239 PRO A CA  
1782 C C   . PRO A 245 ? 0.28060 0.39040 0.38660 -0.06350 0.10290  -0.07830 239 PRO A C   
1783 O O   . PRO A 245 ? 0.23070 0.33580 0.33250 -0.06340 0.09640  -0.07610 239 PRO A O   
1784 C CB  . PRO A 245 ? 0.26120 0.38030 0.40110 -0.05050 0.09740  -0.07920 239 PRO A CB  
1785 C CG  . PRO A 245 ? 0.28370 0.40830 0.42740 -0.04980 0.10700  -0.08410 239 PRO A CG  
1786 C CD  . PRO A 245 ? 0.27670 0.40670 0.41770 -0.05650 0.11190  -0.08060 239 PRO A CD  
1787 N N   . GLU A 246 ? 0.30250 0.41230 0.39650 -0.06740 0.11220  -0.08290 240 GLU A N   
1788 C CA  . GLU A 246 ? 0.31300 0.41710 0.38600 -0.07210 0.11420  -0.08530 240 GLU A CA  
1789 C C   . GLU A 246 ? 0.29520 0.39610 0.35220 -0.07960 0.11270  -0.07720 240 GLU A C   
1790 O O   . GLU A 246 ? 0.28060 0.37480 0.32000 -0.08170 0.10840  -0.07540 240 GLU A O   
1791 C CB  . GLU A 246 ? 0.35030 0.45380 0.41170 -0.07420 0.12410  -0.09260 240 GLU A CB  
1792 C CG  . GLU A 246 ? 0.43700 0.54300 0.49140 -0.07960 0.13130  -0.08930 240 GLU A CG  
1793 C CD  . GLU A 246 ? 0.44960 0.56360 0.52570 -0.07540 0.13400  -0.08930 240 GLU A CD  
1794 O OE1 . GLU A 246 ? 0.46700 0.58390 0.56100 -0.06770 0.13140  -0.09290 240 GLU A OE1 
1795 O OE2 . GLU A 246 ? 0.48320 0.60060 0.55770 -0.07980 0.13870  -0.08530 240 GLU A OE2 
1796 N N   . MET A 247 ? 0.27260 0.37460 0.33310 -0.08240 0.11350  -0.07080 241 MET A N   
1797 C CA  . MET A 247 ? 0.27340 0.36950 0.32050 -0.08850 0.11110  -0.06170 241 MET A CA  
1798 C C   . MET A 247 ? 0.25020 0.34280 0.30550 -0.08520 0.10050  -0.05700 241 MET A C   
1799 O O   . MET A 247 ? 0.25660 0.33940 0.29700 -0.08610 0.09370  -0.04940 241 MET A O   
1800 C CB  . MET A 247 ? 0.26600 0.36260 0.31450 -0.09260 0.11520  -0.05650 241 MET A CB  
1801 C CG  . MET A 247 ? 0.30750 0.40620 0.34540 -0.09660 0.12570  -0.05910 241 MET A CG  
1802 S SD  . MET A 247 ? 0.38570 0.47610 0.38970 -0.10340 0.12900  -0.05590 241 MET A SD  
1803 C CE  . MET A 247 ? 0.37300 0.46670 0.37170 -0.10040 0.13330  -0.06830 241 MET A CE  
1804 N N   . VAL A 248 ? 0.25920 0.35590 0.33530 -0.07850 0.09550  -0.05950 242 VAL A N   
1805 C CA  . VAL A 248 ? 0.22170 0.31450 0.30480 -0.07520 0.08560  -0.05510 242 VAL A CA  
1806 C C   . VAL A 248 ? 0.25720 0.34310 0.33060 -0.07100 0.07820  -0.05530 242 VAL A C   
1807 O O   . VAL A 248 ? 0.27860 0.35740 0.34920 -0.06880 0.06940  -0.04920 242 VAL A O   
1808 C CB  . VAL A 248 ? 0.27450 0.37150 0.37750 -0.06800 0.08040  -0.05650 242 VAL A CB  
1809 C CG1 . VAL A 248 ? 0.24250 0.33410 0.35030 -0.06410 0.07000  -0.05200 242 VAL A CG1 
1810 C CG2 . VAL A 248 ? 0.19680 0.29800 0.30560 -0.07070 0.08390  -0.05460 242 VAL A CG2 
1811 N N   . ALA A 249 ? 0.25610 0.34350 0.32420 -0.07000 0.08160  -0.06220 243 ALA A N   
1812 C CA  . ALA A 249 ? 0.23200 0.31310 0.29090 -0.06690 0.07420  -0.06290 243 ALA A CA  
1813 C C   . ALA A 249 ? 0.24750 0.32760 0.28900 -0.07060 0.07960  -0.06850 243 ALA A C   
1814 O O   . ALA A 249 ? 0.28880 0.36460 0.30990 -0.07540 0.07840  -0.06380 243 ALA A O   
1815 C CB  . ALA A 249 ? 0.20000 0.28280 0.27690 -0.05970 0.06980  -0.06720 243 ALA A CB  
1816 N N   . GLY A 250 ? 0.26670 0.35020 0.31510 -0.06850 0.08560  -0.07850 244 GLY A N   
1817 C CA  . GLY A 250 ? 0.29550 0.37760 0.32670 -0.07260 0.09220  -0.08540 244 GLY A CA  
1818 C C   . GLY A 250 ? 0.30960 0.39130 0.34970 -0.06840 0.09550  -0.09620 244 GLY A C   
1819 O O   . GLY A 250 ? 0.27590 0.35950 0.33670 -0.06190 0.09360  -0.09770 244 GLY A O   
1820 N N   . GLU A 251 ? 0.34950 0.42800 0.37240 -0.07240 0.10070  -0.10370 245 GLU A N   
1821 C CA  . GLU A 251 ? 0.39070 0.46650 0.41950 -0.06920 0.10600  -0.11530 245 GLU A CA  
1822 C C   . GLU A 251 ? 0.30590 0.37600 0.34220 -0.06480 0.09560  -0.11510 245 GLU A C   
1823 O O   . GLU A 251 ? 0.29220 0.35860 0.31670 -0.06750 0.08550  -0.11010 245 GLU A O   
1824 C CB  . GLU A 251 ? 0.43280 0.50450 0.43740 -0.07580 0.11310  -0.12360 245 GLU A CB  
1825 C CG  . GLU A 251 ? 0.55020 0.61880 0.56160 -0.07280 0.12280  -0.13480 245 GLU A CG  
1826 C CD  . GLU A 251 ? 0.60950 0.68410 0.64020 -0.06800 0.12980  -0.13250 245 GLU A CD  
1827 O OE1 . GLU A 251 ? 0.63240 0.71380 0.66290 -0.07050 0.13190  -0.12590 245 GLU A OE1 
1828 O OE2 . GLU A 251 ? 0.67820 0.75020 0.72410 -0.06170 0.13270  -0.13680 245 GLU A OE2 
1829 N N   . GLY A 252 ? 0.30300 0.37280 0.35980 -0.05780 0.09820  -0.12000 246 GLY A N   
1830 C CA  . GLY A 252 ? 0.32460 0.38840 0.38910 -0.05380 0.08970  -0.12000 246 GLY A CA  
1831 C C   . GLY A 252 ? 0.32630 0.39230 0.40190 -0.05010 0.07890  -0.10910 246 GLY A C   
1832 O O   . GLY A 252 ? 0.27620 0.33760 0.35890 -0.04660 0.07210  -0.10820 246 GLY A O   
1833 N N   . ARG A 253 ? 0.20050 0.27240 0.27670 -0.05140 0.07750  -0.10110 247 ARG A N   
1834 C CA  . ARG A 253 ? 0.22880 0.30150 0.31340 -0.04840 0.06790  -0.09140 247 ARG A CA  
1835 C C   . ARG A 253 ? 0.27670 0.35420 0.38530 -0.04130 0.06890  -0.09110 247 ARG A C   
1836 O O   . ARG A 253 ? 0.23650 0.32060 0.35590 -0.03970 0.07730  -0.09510 247 ARG A O   
1837 C CB  . ARG A 253 ? 0.23210 0.30720 0.30640 -0.05320 0.06650  -0.08330 247 ARG A CB  
1838 C CG  . ARG A 253 ? 0.24380 0.31480 0.29410 -0.05940 0.06370  -0.08100 247 ARG A CG  
1839 C CD  . ARG A 253 ? 0.24930 0.31610 0.29640 -0.05800 0.05160  -0.07360 247 ARG A CD  
1840 N NE  . ARG A 253 ? 0.23720 0.30440 0.29550 -0.05440 0.04690  -0.06510 247 ARG A NE  
1841 C CZ  . ARG A 253 ? 0.26870 0.33550 0.32090 -0.05690 0.04660  -0.05740 247 ARG A CZ  
1842 N NH1 . ARG A 253 ? 0.23560 0.30220 0.27100 -0.06260 0.05050  -0.05590 247 ARG A NH1 
1843 N NH2 . ARG A 253 ? 0.20220 0.26820 0.26510 -0.05370 0.04300  -0.05150 247 ARG A NH2 
1844 N N   . TYR A 254 ? 0.24800 0.32330 0.36520 -0.03700 0.06020  -0.08570 248 TYR A N   
1845 C CA  . TYR A 254 ? 0.23810 0.31790 0.37650 -0.03000 0.05970  -0.08470 248 TYR A CA  
1846 C C   . TYR A 254 ? 0.19540 0.28040 0.33740 -0.03000 0.06100  -0.08050 248 TYR A C   
1847 O O   . TYR A 254 ? 0.19520 0.28140 0.34580 -0.02540 0.06250  -0.08090 248 TYR A O   
1848 C CB  . TYR A 254 ? 0.20200 0.27770 0.34450 -0.02650 0.04950  -0.07810 248 TYR A CB  
1849 C CG  . TYR A 254 ? 0.15580 0.22800 0.30790 -0.01870 0.04530  -0.07410 248 TYR A CG  
1850 C CD1 . TYR A 254 ? 0.17830 0.24540 0.33680 -0.01380 0.04590  -0.07720 248 TYR A CD1 
1851 C CD2 . TYR A 254 ? 0.16500 0.23880 0.31810 -0.01710 0.04080  -0.06710 248 TYR A CD2 
1852 C CE1 . TYR A 254 ? 0.21080 0.27560 0.37630 -0.00780 0.04190  -0.07200 248 TYR A CE1 
1853 C CE2 . TYR A 254 ? 0.20170 0.27410 0.36150 -0.01120 0.03680  -0.06320 248 TYR A CE2 
1854 C CZ  . TYR A 254 ? 0.19270 0.26110 0.35850 -0.00660 0.03720  -0.06520 248 TYR A CZ  
1855 O OH  . TYR A 254 ? 0.18310 0.25140 0.35440 -0.00130 0.03340  -0.06030 248 TYR A OH  
1856 N N   . CYS A 255 ? 0.20070 0.28820 0.33570 -0.03540 0.05980  -0.07550 249 CYS A N   
1857 C CA  . CYS A 255 ? 0.21260 0.30400 0.35110 -0.03570 0.06030  -0.07130 249 CYS A CA  
1858 C C   . CYS A 255 ? 0.22520 0.32190 0.36490 -0.03730 0.06960  -0.07640 249 CYS A C   
1859 O O   . CYS A 255 ? 0.22090 0.32230 0.36990 -0.03470 0.07020  -0.07500 249 CYS A O   
1860 C CB  . CYS A 255 ? 0.18540 0.27630 0.31510 -0.04200 0.05860  -0.06530 249 CYS A CB  
1861 S SG  . CYS A 255 ? 0.27570 0.35980 0.40040 -0.04200 0.04930  -0.05890 249 CYS A SG  
1862 N N   . THR A 256 ? 0.21860 0.31500 0.34790 -0.04210 0.07720  -0.08230 250 THR A N   
1863 C CA  . THR A 256 ? 0.22200 0.32210 0.35020 -0.04360 0.08680  -0.08730 250 THR A CA  
1864 C C   . THR A 256 ? 0.24390 0.34340 0.38460 -0.03610 0.08820  -0.09150 250 THR A C   
1865 O O   . THR A 256 ? 0.23300 0.33780 0.38160 -0.03420 0.09270  -0.09200 250 THR A O   
1866 C CB  . THR A 256 ? 0.22690 0.32510 0.33650 -0.05080 0.09430  -0.09250 250 THR A CB  
1867 O OG1 . THR A 256 ? 0.24470 0.34360 0.34220 -0.05800 0.09350  -0.08650 250 THR A OG1 
1868 C CG2 . THR A 256 ? 0.30430 0.40430 0.41100 -0.05180 0.10450  -0.09810 250 THR A CG2 
1869 N N   . MET A 257 ? 0.24530 0.33850 0.38800 -0.03210 0.08470  -0.09410 251 MET A N   
1870 C CA  . MET A 257 ? 0.25660 0.34710 0.40930 -0.02550 0.08660  -0.09750 251 MET A CA  
1871 C C   . MET A 257 ? 0.23150 0.32550 0.39900 -0.01880 0.07990  -0.09050 251 MET A C   
1872 O O   . MET A 257 ? 0.24470 0.34210 0.42220 -0.01400 0.08300  -0.09070 251 MET A O   
1873 C CB  . MET A 257 ? 0.32100 0.40210 0.46930 -0.02450 0.08560  -0.10250 251 MET A CB  
1874 C CG  . MET A 257 ? 0.25740 0.33510 0.38840 -0.03150 0.09310  -0.11100 251 MET A CG  
1875 S SD  . MET A 257 ? 0.35330 0.41940 0.47850 -0.03120 0.09050  -0.11730 251 MET A SD  
1876 C CE  . MET A 257 ? 0.37770 0.43800 0.52010 -0.02200 0.09090  -0.11680 251 MET A CE  
1877 N N   . LEU A 258 ? 0.21460 0.30810 0.38240 -0.01840 0.07100  -0.08400 252 LEU A N   
1878 C CA  . LEU A 258 ? 0.19260 0.29010 0.37060 -0.01340 0.06450  -0.07720 252 LEU A CA  
1879 C C   . LEU A 258 ? 0.23830 0.34640 0.42200 -0.01490 0.06830  -0.07570 252 LEU A C   
1880 O O   . LEU A 258 ? 0.24520 0.35950 0.44030 -0.01000 0.06860  -0.07410 252 LEU A O   
1881 C CB  . LEU A 258 ? 0.17170 0.26580 0.34520 -0.01410 0.05530  -0.07100 252 LEU A CB  
1882 C CG  . LEU A 258 ? 0.20650 0.30520 0.38620 -0.01120 0.04870  -0.06410 252 LEU A CG  
1883 C CD1 . LEU A 258 ? 0.23060 0.32700 0.41740 -0.00390 0.04480  -0.06190 252 LEU A CD1 
1884 C CD2 . LEU A 258 ? 0.17470 0.27010 0.34650 -0.01440 0.04240  -0.05920 252 LEU A CD2 
1885 N N   . MET A 259 ? 0.21800 0.32920 0.39430 -0.02200 0.07180  -0.07600 253 MET A N   
1886 C CA  . MET A 259 ? 0.21640 0.33800 0.39900 -0.02420 0.07490  -0.07390 253 MET A CA  
1887 C C   . MET A 259 ? 0.24190 0.36900 0.43080 -0.02230 0.08420  -0.07880 253 MET A C   
1888 O O   . MET A 259 ? 0.23260 0.36970 0.43380 -0.01960 0.08510  -0.07660 253 MET A O   
1889 C CB  . MET A 259 ? 0.14160 0.26370 0.31420 -0.03260 0.07640  -0.07200 253 MET A CB  
1890 C CG  . MET A 259 ? 0.19850 0.31750 0.36880 -0.03360 0.06710  -0.06570 253 MET A CG  
1891 S SD  . MET A 259 ? 0.21020 0.32890 0.37130 -0.04300 0.06800  -0.06150 253 MET A SD  
1892 C CE  . MET A 259 ? 0.21130 0.32120 0.35540 -0.04770 0.07190  -0.06370 253 MET A CE  
1893 N N   . ARG A 260 ? 0.25850 0.37950 0.43910 -0.02370 0.09120  -0.08540 254 ARG A N   
1894 C CA  . ARG A 260 ? 0.27280 0.39690 0.45830 -0.02120 0.10050  -0.09060 254 ARG A CA  
1895 C C   . ARG A 260 ? 0.25140 0.37740 0.45200 -0.01190 0.09810  -0.08910 254 ARG A C   
1896 O O   . ARG A 260 ? 0.28180 0.41720 0.49400 -0.00840 0.10230  -0.08850 254 ARG A O   
1897 C CB  . ARG A 260 ? 0.28420 0.39930 0.45540 -0.02460 0.10760  -0.09840 254 ARG A CB  
1898 C CG  . ARG A 260 ? 0.38680 0.50400 0.54420 -0.03330 0.11500  -0.10030 254 ARG A CG  
1899 C CD  . ARG A 260 ? 0.46350 0.57210 0.60220 -0.03810 0.12120  -0.10770 254 ARG A CD  
1900 N NE  . ARG A 260 ? 0.61350 0.72430 0.73720 -0.04650 0.12720  -0.10750 254 ARG A NE  
1901 C CZ  . ARG A 260 ? 0.57710 0.68190 0.67920 -0.05320 0.13090  -0.11120 254 ARG A CZ  
1902 N NH1 . ARG A 260 ? 0.48600 0.58240 0.57880 -0.05300 0.12960  -0.11690 254 ARG A NH1 
1903 N NH2 . ARG A 260 ? 0.58540 0.69250 0.67410 -0.06050 0.13560  -0.10870 254 ARG A NH2 
1904 N N   . ALA A 261 ? 0.24210 0.35970 0.44260 -0.00780 0.09130  -0.08800 255 ALA A N   
1905 C CA  . ALA A 261 ? 0.24850 0.36630 0.46120 0.00100  0.08880  -0.08560 255 ALA A CA  
1906 C C   . ALA A 261 ? 0.30890 0.44020 0.53460 0.00430  0.08480  -0.07880 255 ALA A C   
1907 O O   . ALA A 261 ? 0.23330 0.37150 0.47130 0.01070  0.08760  -0.07790 255 ALA A O   
1908 C CB  . ALA A 261 ? 0.28600 0.39290 0.49500 0.00340  0.08100  -0.08370 255 ALA A CB  
1909 N N   . PHE A 262 ? 0.23620 0.37180 0.45930 -0.00020 0.07830  -0.07410 256 PHE A N   
1910 C CA  . PHE A 262 ? 0.24500 0.39350 0.47910 0.00180  0.07320  -0.06770 256 PHE A CA  
1911 C C   . PHE A 262 ? 0.28150 0.44380 0.52270 -0.00190 0.07920  -0.06790 256 PHE A C   
1912 O O   . PHE A 262 ? 0.19850 0.37440 0.45230 0.00050  0.07670  -0.06350 256 PHE A O   
1913 C CB  . PHE A 262 ? 0.23560 0.38090 0.46320 -0.00120 0.06330  -0.06260 256 PHE A CB  
1914 C CG  . PHE A 262 ? 0.18440 0.32230 0.41150 0.00480  0.05610  -0.05950 256 PHE A CG  
1915 C CD1 . PHE A 262 ? 0.21350 0.33710 0.43070 0.00470  0.05490  -0.06180 256 PHE A CD1 
1916 C CD2 . PHE A 262 ? 0.27510 0.42170 0.51250 0.01060  0.05130  -0.05420 256 PHE A CD2 
1917 C CE1 . PHE A 262 ? 0.24410 0.36090 0.46110 0.00990  0.04910  -0.05860 256 PHE A CE1 
1918 C CE2 . PHE A 262 ? 0.27360 0.41330 0.50970 0.01610  0.04550  -0.05090 256 PHE A CE2 
1919 C CZ  . PHE A 262 ? 0.26410 0.38840 0.48990 0.01560  0.04460  -0.05300 256 PHE A CZ  
1920 N N   . ASP A 263 ? 0.24230 0.40240 0.47570 -0.00790 0.08730  -0.07280 257 ASP A N   
1921 C CA  . ASP A 263 ? 0.28550 0.45770 0.52590 -0.01050 0.09560  -0.07400 257 ASP A CA  
1922 C C   . ASP A 263 ? 0.26020 0.44550 0.50840 -0.01440 0.09100  -0.06820 257 ASP A C   
1923 O O   . ASP A 263 ? 0.27210 0.47240 0.53410 -0.01330 0.09450  -0.06670 257 ASP A O   
1924 C CB  . ASP A 263 ? 0.28900 0.46710 0.54200 -0.00250 0.10190  -0.07630 257 ASP A CB  
1925 C CG  . ASP A 263 ? 0.39940 0.58840 0.65810 -0.00490 0.11270  -0.07890 257 ASP A CG  
1926 O OD1 . ASP A 263 ? 0.44370 0.62780 0.68990 -0.01230 0.11890  -0.08260 257 ASP A OD1 
1927 O OD2 . ASP A 263 ? 0.37270 0.57570 0.64790 0.00050  0.11520  -0.07690 257 ASP A OD2 
1928 N N   . GLY A 264 ? 0.22070 0.40070 0.46040 -0.01940 0.08360  -0.06500 258 GLY A N   
1929 C CA  . GLY A 264 ? 0.18240 0.37190 0.42670 -0.02490 0.07960  -0.06030 258 GLY A CA  
1930 C C   . GLY A 264 ? 0.21960 0.41260 0.46940 -0.02200 0.06870  -0.05490 258 GLY A C   
1931 O O   . GLY A 264 ? 0.24000 0.43910 0.49180 -0.02740 0.06440  -0.05140 258 GLY A O   
1932 N N   . ALA A 265 ? 0.21010 0.39930 0.46200 -0.01390 0.06430  -0.05420 259 ALA A N   
1933 C CA  . ALA A 265 ? 0.18480 0.37860 0.44130 -0.01110 0.05450  -0.04870 259 ALA A CA  
1934 C C   . ALA A 265 ? 0.22610 0.40730 0.46870 -0.01480 0.04720  -0.04710 259 ALA A C   
1935 O O   . ALA A 265 ? 0.18810 0.37320 0.43240 -0.01490 0.03940  -0.04280 259 ALA A O   
1936 C CB  . ALA A 265 ? 0.19900 0.39320 0.46240 -0.00090 0.05310  -0.04780 259 ALA A CB  
1937 N N   . LEU A 266 ? 0.15910 0.32620 0.38810 -0.01810 0.04980  -0.05030 260 LEU A N   
1938 C CA  . LEU A 266 ? 0.17190 0.32740 0.38830 -0.02120 0.04380  -0.04850 260 LEU A CA  
1939 C C   . LEU A 266 ? 0.20660 0.35240 0.41090 -0.02690 0.04900  -0.05170 260 LEU A C   
1940 O O   . LEU A 266 ? 0.15850 0.30460 0.36240 -0.02750 0.05690  -0.05580 260 LEU A O   
1941 C CB  . LEU A 266 ? 0.16620 0.31300 0.37930 -0.01440 0.03800  -0.04720 260 LEU A CB  
1942 C CG  . LEU A 266 ? 0.21340 0.35210 0.42520 -0.00860 0.04120  -0.05050 260 LEU A CG  
1943 C CD1 . LEU A 266 ? 0.19650 0.32340 0.39610 -0.01240 0.04510  -0.05460 260 LEU A CD1 
1944 C CD2 . LEU A 266 ? 0.21730 0.35080 0.42890 -0.00220 0.03440  -0.04710 260 LEU A CD2 
1945 N N   . VAL A 267 ? 0.13580 0.27330 0.32970 -0.03110 0.04480  -0.04950 261 VAL A N   
1946 C CA  . VAL A 267 ? 0.13160 0.25870 0.31280 -0.03520 0.04830  -0.05120 261 VAL A CA  
1947 C C   . VAL A 267 ? 0.14580 0.26190 0.31910 -0.03200 0.04200  -0.04960 261 VAL A C   
1948 O O   . VAL A 267 ? 0.14890 0.26440 0.32430 -0.02890 0.03510  -0.04650 261 VAL A O   
1949 C CB  . VAL A 267 ? 0.17110 0.29770 0.34640 -0.04400 0.05090  -0.04950 261 VAL A CB  
1950 C CG1 . VAL A 267 ? 0.20140 0.33840 0.38360 -0.04760 0.05850  -0.05130 261 VAL A CG1 
1951 C CG2 . VAL A 267 ? 0.16820 0.29400 0.34360 -0.04630 0.04390  -0.04540 261 VAL A CG2 
1952 N N   . GLY A 268 ? 0.16090 0.26920 0.32540 -0.03310 0.04460  -0.05160 262 GLY A N   
1953 C CA  . GLY A 268 ? 0.15670 0.25530 0.31430 -0.03060 0.03920  -0.04980 262 GLY A CA  
1954 C C   . GLY A 268 ? 0.15830 0.25100 0.30480 -0.03610 0.04190  -0.04970 262 GLY A C   
1955 O O   . GLY A 268 ? 0.22970 0.32520 0.37290 -0.04120 0.04890  -0.05200 262 GLY A O   
1956 N N   . LYS A 269 ? 0.13540 0.22040 0.27590 -0.03550 0.03660  -0.04620 263 LYS A N   
1957 C CA  . LYS A 269 ? 0.16890 0.24870 0.29940 -0.04100 0.03820  -0.04430 263 LYS A CA  
1958 C C   . LYS A 269 ? 0.14200 0.21460 0.26900 -0.03760 0.03230  -0.04180 263 LYS A C   
1959 O O   . LYS A 269 ? 0.13160 0.20080 0.26070 -0.03330 0.02650  -0.03900 263 LYS A O   
1960 C CB  . LYS A 269 ? 0.18490 0.26270 0.31180 -0.04700 0.03910  -0.04040 263 LYS A CB  
1961 C CG  . LYS A 269 ? 0.17670 0.24690 0.29260 -0.05290 0.04080  -0.03660 263 LYS A CG  
1962 C CD  . LYS A 269 ? 0.19180 0.26540 0.30130 -0.05830 0.04890  -0.03890 263 LYS A CD  
1963 C CE  . LYS A 269 ? 0.23460 0.29860 0.32800 -0.06170 0.04850  -0.03340 263 LYS A CE  
1964 N NZ  . LYS A 269 ? 0.26240 0.32400 0.34960 -0.05680 0.04380  -0.03370 263 LYS A NZ  
1965 N N   . LEU A 270 ? 0.15260 0.22360 0.27380 -0.04020 0.03390  -0.04260 264 LEU A N   
1966 C CA  . LEU A 270 ? 0.17050 0.23620 0.28910 -0.03780 0.02830  -0.03990 264 LEU A CA  
1967 C C   . LEU A 270 ? 0.18130 0.23850 0.29030 -0.03980 0.02540  -0.03270 264 LEU A C   
1968 O O   . LEU A 270 ? 0.20720 0.26170 0.30720 -0.04490 0.02900  -0.03000 264 LEU A O   
1969 C CB  . LEU A 270 ? 0.19450 0.25920 0.30420 -0.03840 0.02930  -0.04240 264 LEU A CB  
1970 C CG  . LEU A 270 ? 0.21550 0.27390 0.31650 -0.03650 0.02300  -0.03800 264 LEU A CG  
1971 C CD1 . LEU A 270 ? 0.18120 0.23970 0.29290 -0.03080 0.01880  -0.03990 264 LEU A CD1 
1972 C CD2 . LEU A 270 ? 0.19410 0.25260 0.28170 -0.04030 0.02460  -0.03980 264 LEU A CD2 
1973 N N   . GLY A 271 ? 0.17870 0.23070 0.28920 -0.03530 0.01960  -0.02910 265 GLY A N   
1974 C CA  . GLY A 271 ? 0.16240 0.20490 0.26310 -0.03510 0.01670  -0.02200 265 GLY A CA  
1975 C C   . GLY A 271 ? 0.16640 0.20720 0.26250 -0.03150 0.01230  -0.01950 265 GLY A C   
1976 O O   . GLY A 271 ? 0.15220 0.19580 0.25590 -0.02750 0.00940  -0.02210 265 GLY A O   
1977 N N   . ALA A 272 ? 0.21960 0.25610 0.30380 -0.03290 0.01150  -0.01390 266 ALA A N   
1978 C CA  . ALA A 272 ? 0.19200 0.22860 0.27260 -0.02990 0.00650  -0.01060 266 ALA A CA  
1979 C C   . ALA A 272 ? 0.23480 0.26880 0.32380 -0.02410 0.00230  -0.00840 266 ALA A C   
1980 O O   . ALA A 272 ? 0.17660 0.20550 0.26930 -0.02230 0.00290  -0.00690 266 ALA A O   
1981 C CB  . ALA A 272 ? 0.24540 0.27780 0.31300 -0.03130 0.00560  -0.00280 266 ALA A CB  
1982 N N   . ASP A 273 ? 0.23780 0.27530 0.32900 -0.02170 -0.00160 -0.00850 267 ASP A N   
1983 C CA  . ASP A 273 ? 0.18480 0.22150 0.28490 -0.01660 -0.00490 -0.00730 267 ASP A CA  
1984 C C   . ASP A 273 ? 0.18880 0.22630 0.29880 -0.01500 -0.00330 -0.01270 267 ASP A C   
1985 O O   . ASP A 273 ? 0.15200 0.18670 0.26770 -0.01100 -0.00460 -0.01110 267 ASP A O   
1986 C CB  . ASP A 273 ? 0.17800 0.20840 0.27610 -0.01290 -0.00630 0.00040  267 ASP A CB  
1987 C CG  . ASP A 273 ? 0.22580 0.25790 0.31800 -0.01230 -0.00960 0.00670  267 ASP A CG  
1988 O OD1 . ASP A 273 ? 0.20780 0.24660 0.30290 -0.01230 -0.01310 0.00570  267 ASP A OD1 
1989 O OD2 . ASP A 273 ? 0.28740 0.31460 0.37220 -0.01220 -0.00880 0.01280  267 ASP A OD2 
1990 N N   . ALA A 274 ? 0.16060 0.20250 0.27270 -0.01790 -0.00020 -0.01900 268 ALA A N   
1991 C CA  . ALA A 274 ? 0.14530 0.18840 0.26440 -0.01510 0.00090  -0.02380 268 ALA A CA  
1992 C C   . ALA A 274 ? 0.12890 0.16880 0.24830 -0.01280 0.00150  -0.02270 268 ALA A C   
1993 O O   . ALA A 274 ? 0.18070 0.21690 0.30050 -0.00840 -0.00010 -0.02200 268 ALA A O   
1994 C CB  . ALA A 274 ? 0.11850 0.15900 0.23830 -0.01100 -0.00180 -0.02320 268 ALA A CB  
1995 N N   . SER A 275 ? 0.12190 0.16310 0.24080 -0.01690 0.00400  -0.02290 269 SER A N   
1996 C CA  A SER A 275 ? 0.13120 0.17270 0.25120 -0.01670 0.00500  -0.02400 269 SER A CA  
1997 C CA  B SER A 275 ? 0.13150 0.17290 0.25160 -0.01650 0.00490  -0.02410 269 SER A CA  
1998 C C   . SER A 275 ? 0.12200 0.16990 0.24450 -0.01880 0.00880  -0.02860 269 SER A C   
1999 O O   . SER A 275 ? 0.16360 0.21510 0.28560 -0.02230 0.01190  -0.03110 269 SER A O   
2000 C CB  A SER A 275 ? 0.15810 0.19590 0.27630 -0.02060 0.00570  -0.02140 269 SER A CB  
2001 C CB  B SER A 275 ? 0.15790 0.19540 0.27630 -0.01990 0.00530  -0.02130 269 SER A CB  
2002 O OG  A SER A 275 ? 0.15760 0.18890 0.27560 -0.01780 0.00290  -0.01770 269 SER A OG  
2003 O OG  B SER A 275 ? 0.17080 0.20860 0.28700 -0.02620 0.00880  -0.02080 269 SER A OG  
2004 N N   . TYR A 276 ? 0.12080 0.17120 0.24670 -0.01700 0.00860  -0.02990 270 TYR A N   
2005 C CA  . TYR A 276 ? 0.14470 0.20220 0.27510 -0.01860 0.01250  -0.03390 270 TYR A CA  
2006 C C   . TYR A 276 ? 0.12830 0.18960 0.26190 -0.01940 0.01170  -0.03340 270 TYR A C   
2007 O O   . TYR A 276 ? 0.14300 0.20230 0.27680 -0.01670 0.00770  -0.03130 270 TYR A O   
2008 C CB  . TYR A 276 ? 0.14660 0.20540 0.28180 -0.01420 0.01320  -0.03710 270 TYR A CB  
2009 C CG  . TYR A 276 ? 0.13150 0.19680 0.27050 -0.01690 0.01900  -0.04200 270 TYR A CG  
2010 C CD1 . TYR A 276 ? 0.14920 0.21540 0.28520 -0.02080 0.02290  -0.04500 270 TYR A CD1 
2011 C CD2 . TYR A 276 ? 0.14400 0.21570 0.28950 -0.01640 0.02110  -0.04350 270 TYR A CD2 
2012 C CE1 . TYR A 276 ? 0.14070 0.21290 0.27880 -0.02400 0.02950  -0.05010 270 TYR A CE1 
2013 C CE2 . TYR A 276 ? 0.12760 0.20560 0.27680 -0.01890 0.02750  -0.04800 270 TYR A CE2 
2014 C CZ  . TYR A 276 ? 0.16930 0.24690 0.31430 -0.02260 0.03210  -0.05160 270 TYR A CZ  
2015 O OH  . TYR A 276 ? 0.20080 0.28430 0.34790 -0.02550 0.03960  -0.05660 270 TYR A OH  
2016 N N   . ALA A 277 ? 0.10060 0.16840 0.23710 -0.02370 0.01580  -0.03540 271 ALA A N   
2017 C CA  . ALA A 277 ? 0.10860 0.18210 0.24940 -0.02530 0.01480  -0.03510 271 ALA A CA  
2018 C C   . ALA A 277 ? 0.12510 0.20840 0.27410 -0.02520 0.01860  -0.03810 271 ALA A C   
2019 O O   . ALA A 277 ? 0.13050 0.21570 0.27950 -0.02760 0.02410  -0.04080 271 ALA A O   
2020 C CB  . ALA A 277 ? 0.15460 0.22570 0.29110 -0.03220 0.01580  -0.03360 271 ALA A CB  
2021 N N   . ILE A 278 ? 0.15950 0.24980 0.31570 -0.02280 0.01600  -0.03760 272 ILE A N   
2022 C CA  . ILE A 278 ? 0.11740 0.21860 0.28360 -0.02230 0.01930  -0.03960 272 ILE A CA  
2023 C C   . ILE A 278 ? 0.13620 0.24700 0.30830 -0.02540 0.01690  -0.03780 272 ILE A C   
2024 O O   . ILE A 278 ? 0.14730 0.25780 0.31860 -0.02450 0.01120  -0.03540 272 ILE A O   
2025 C CB  . ILE A 278 ? 0.12610 0.22840 0.29800 -0.01490 0.01860  -0.04020 272 ILE A CB  
2026 C CG1 . ILE A 278 ? 0.10410 0.19710 0.27060 -0.01300 0.02090  -0.04250 272 ILE A CG1 
2027 C CG2 . ILE A 278 ? 0.11860 0.23280 0.30210 -0.01380 0.02270  -0.04200 272 ILE A CG2 
2028 C CD1 . ILE A 278 ? 0.12140 0.21240 0.29260 -0.00650 0.02060  -0.04340 272 ILE A CD1 
2029 N N   . GLY A 279 ? 0.11930 0.23890 0.29740 -0.02960 0.02140  -0.03930 273 GLY A N   
2030 C CA  . GLY A 279 ? 0.10960 0.24100 0.29610 -0.03290 0.01940  -0.03790 273 GLY A CA  
2031 C C   . GLY A 279 ? 0.18230 0.32630 0.38170 -0.02860 0.02190  -0.03860 273 GLY A C   
2032 O O   . GLY A 279 ? 0.15850 0.30420 0.36040 -0.02850 0.02870  -0.04140 273 GLY A O   
2033 N N   . VAL A 280 ? 0.14910 0.30220 0.35660 -0.02470 0.01680  -0.03600 274 VAL A N   
2034 C CA  . VAL A 280 ? 0.14900 0.31420 0.36940 -0.01890 0.01860  -0.03560 274 VAL A CA  
2035 C C   . VAL A 280 ? 0.19640 0.37950 0.42920 -0.02270 0.01710  -0.03360 274 VAL A C   
2036 O O   . VAL A 280 ? 0.17050 0.35850 0.40400 -0.02540 0.01050  -0.03070 274 VAL A O   
2037 C CB  . VAL A 280 ? 0.13420 0.29680 0.35500 -0.01060 0.01400  -0.03330 274 VAL A CB  
2038 C CG1 . VAL A 280 ? 0.16070 0.33600 0.39570 -0.00380 0.01620  -0.03230 274 VAL A CG1 
2039 C CG2 . VAL A 280 ? 0.15550 0.30030 0.36420 -0.00810 0.01470  -0.03500 274 VAL A CG2 
2040 N N   . ARG A 281 ? 0.15930 0.35270 0.40240 -0.02310 0.02340  -0.03500 275 ARG A N   
2041 C CA  . ARG A 281 ? 0.21080 0.42320 0.46800 -0.02660 0.02270  -0.03280 275 ARG A CA  
2042 C C   . ARG A 281 ? 0.15770 0.38370 0.42610 -0.01990 0.01700  -0.02860 275 ARG A C   
2043 O O   . ARG A 281 ? 0.15680 0.37870 0.42450 -0.01130 0.01650  -0.02810 275 ARG A O   
2044 C CB  . ARG A 281 ? 0.16040 0.38020 0.42590 -0.02770 0.03200  -0.03550 275 ARG A CB  
2045 C CG  . ARG A 281 ? 0.21360 0.42550 0.47030 -0.03680 0.03700  -0.03820 275 ARG A CG  
2046 C CD  . ARG A 281 ? 0.21560 0.43780 0.48180 -0.03850 0.04660  -0.04030 275 ARG A CD  
2047 N NE  . ARG A 281 ? 0.27570 0.51760 0.55800 -0.04200 0.04550  -0.03740 275 ARG A NE  
2048 C CZ  . ARG A 281 ? 0.31360 0.56910 0.60820 -0.04290 0.05290  -0.03810 275 ARG A CZ  
2049 N NH1 . ARG A 281 ? 0.32990 0.58060 0.62140 -0.04120 0.06250  -0.04210 275 ARG A NH1 
2050 N NH2 . ARG A 281 ? 0.22760 0.50240 0.53830 -0.04590 0.05060  -0.03480 275 ARG A NH2 
2051 N N   . ALA A 282 ? 0.20430 0.44660 0.48270 -0.02430 0.01230  -0.02530 276 ALA A N   
2052 C CA  . ALA A 282 ? 0.19980 0.45830 0.48960 -0.01860 0.00620  -0.02050 276 ALA A CA  
2053 C C   . ALA A 282 ? 0.17090 0.43790 0.47200 -0.00860 0.01150  -0.02020 276 ALA A C   
2054 O O   . ALA A 282 ? 0.16820 0.44120 0.47750 -0.00900 0.01920  -0.02250 276 ALA A O   
2055 C CB  . ALA A 282 ? 0.22410 0.50190 0.52600 -0.02610 0.00150  -0.01730 276 ALA A CB  
2056 N N   . SER A 283 ? 0.16650 0.43390 0.46810 0.00050  0.00780  -0.01760 277 SER A N   
2057 C CA  . SER A 283 ? 0.15250 0.42360 0.46260 0.01100  0.01290  -0.01780 277 SER A CA  
2058 C C   . SER A 283 ? 0.18980 0.47010 0.50490 0.01970  0.00640  -0.01290 277 SER A C   
2059 O O   . SER A 283 ? 0.21510 0.49810 0.52560 0.01740  -0.00190 -0.00960 277 SER A O   
2060 C CB  . SER A 283 ? 0.19210 0.44050 0.49040 0.01410  0.01910  -0.02260 277 SER A CB  
2061 O OG  . SER A 283 ? 0.16410 0.39700 0.44910 0.01620  0.01370  -0.02160 277 SER A OG  
2062 N N   . ASP A 284 ? 0.19450 0.47950 0.51890 0.02990  0.01070  -0.01270 278 ASP A N   
2063 C CA  . ASP A 284 ? 0.16290 0.45260 0.49010 0.03980  0.00560  -0.00890 278 ASP A CA  
2064 C C   . ASP A 284 ? 0.22740 0.49570 0.53710 0.04020  0.00140  -0.00870 278 ASP A C   
2065 O O   . ASP A 284 ? 0.21020 0.48310 0.51770 0.04300  -0.00620 -0.00490 278 ASP A O   
2066 C CB  . ASP A 284 ? 0.17710 0.46810 0.51430 0.05080  0.01240  -0.01010 278 ASP A CB  
2067 C CG  . ASP A 284 ? 0.27740 0.59570 0.63530 0.05450  0.01420  -0.00840 278 ASP A CG  
2068 O OD1 . ASP A 284 ? 0.23360 0.57260 0.60000 0.04800  0.01030  -0.00600 278 ASP A OD1 
2069 O OD2 . ASP A 284 ? 0.32430 0.64340 0.69080 0.06430  0.01970  -0.00960 278 ASP A OD2 
2070 N N   . ALA A 285 ? 0.24950 0.49520 0.54690 0.03750  0.00640  -0.01310 279 ALA A N   
2071 C CA  . ALA A 285 ? 0.25310 0.47820 0.53420 0.03720  0.00330  -0.01320 279 ALA A CA  
2072 C C   . ALA A 285 ? 0.21760 0.44400 0.49050 0.02990  -0.00440 -0.01120 279 ALA A C   
2073 O O   . ALA A 285 ? 0.20000 0.42240 0.46620 0.03260  -0.01020 -0.00830 279 ALA A O   
2074 C CB  . ALA A 285 ? 0.25130 0.45620 0.52270 0.03410  0.00990  -0.01880 279 ALA A CB  
2075 N N   . THR A 286 ? 0.21350 0.44460 0.48650 0.02040  -0.00420 -0.01300 280 THR A N   
2076 C CA  . THR A 286 ? 0.18110 0.41140 0.44590 0.01280  -0.01100 -0.01180 280 THR A CA  
2077 C C   . THR A 286 ? 0.21770 0.46800 0.49060 0.01410  -0.01880 -0.00680 280 THR A C   
2078 O O   . THR A 286 ? 0.15140 0.39890 0.41600 0.01210  -0.02540 -0.00510 280 THR A O   
2079 C CB  . THR A 286 ? 0.21440 0.44360 0.47730 0.00210  -0.00870 -0.01510 280 THR A CB  
2080 O OG1 . THR A 286 ? 0.22680 0.47610 0.50510 -0.00050 -0.00710 -0.01400 280 THR A OG1 
2081 C CG2 . THR A 286 ? 0.20960 0.41980 0.46300 0.00110  -0.00150 -0.02010 280 THR A CG2 
2082 N N   . ARG A 287 ? 0.22740 0.49930 0.51670 0.01740  -0.01830 -0.00450 281 ARG A N   
2083 C CA  A ARG A 287 ? 0.21750 0.51130 0.51520 0.01920  -0.02630 0.00030  281 ARG A CA  
2084 C CA  B ARG A 287 ? 0.21700 0.51140 0.51540 0.01950  -0.02610 0.00030  281 ARG A CA  
2085 C C   . ARG A 287 ? 0.23220 0.52150 0.52450 0.02930  -0.03030 0.00240  281 ARG A C   
2086 O O   . ARG A 287 ? 0.22930 0.52390 0.51690 0.02820  -0.03820 0.00450  281 ARG A O   
2087 C CB  A ARG A 287 ? 0.16900 0.48780 0.48630 0.02170  -0.02450 0.00200  281 ARG A CB  
2088 C CB  B ARG A 287 ? 0.17080 0.48900 0.48880 0.02350  -0.02350 0.00180  281 ARG A CB  
2089 C CG  A ARG A 287 ? 0.17700 0.50470 0.50110 0.00990  -0.02340 0.00150  281 ARG A CG  
2090 C CG  B ARG A 287 ? 0.18510 0.52470 0.51200 0.01700  -0.03000 0.00470  281 ARG A CG  
2091 C CD  A ARG A 287 ? 0.16350 0.51530 0.50720 0.01220  -0.02120 0.00330  281 ARG A CD  
2092 C CD  B ARG A 287 ? 0.15000 0.51170 0.49630 0.02140  -0.02630 0.00550  281 ARG A CD  
2093 N NE  A ARG A 287 ? 0.12290 0.47390 0.47460 0.01830  -0.01090 0.00050  281 ARG A NE  
2094 N NE  B ARG A 287 ? 0.13990 0.49790 0.49230 0.01930  -0.01630 0.00270  281 ARG A NE  
2095 C CZ  A ARG A 287 ? 0.11830 0.46230 0.47030 0.01170  -0.00360 -0.00300 281 ARG A CZ  
2096 C CZ  B ARG A 287 ? 0.12330 0.48090 0.48290 0.02880  -0.00830 0.00070  281 ARG A CZ  
2097 N NH1 A ARG A 287 ? 0.11650 0.45680 0.46400 -0.00060 -0.00540 -0.00370 281 ARG A NH1 
2098 N NH1 B ARG A 287 ? 0.12810 0.48780 0.49080 0.04140  -0.00900 0.00130  281 ARG A NH1 
2099 N NH2 A ARG A 287 ? 0.12090 0.46050 0.47720 0.01770  0.00590  -0.00640 281 ARG A NH2 
2100 N NH2 B ARG A 287 ? 0.12310 0.47320 0.48420 0.02530  0.00070  -0.00300 281 ARG A NH2 
2101 N N   . GLN A 288 ? 0.21440 0.49030 0.50520 0.03850  -0.02470 0.00130  282 GLN A N   
2102 C CA  . GLN A 288 ? 0.23570 0.50290 0.52020 0.04750  -0.02790 0.00340  282 GLN A CA  
2103 C C   . GLN A 288 ? 0.26500 0.51500 0.53250 0.04260  -0.03150 0.00330  282 GLN A C   
2104 O O   . GLN A 288 ? 0.30370 0.55270 0.56620 0.04730  -0.03710 0.00590  282 GLN A O   
2105 C CB  . GLN A 288 ? 0.29360 0.54590 0.57870 0.05610  -0.02080 0.00210  282 GLN A CB  
2106 C CG  . GLN A 288 ? 0.40110 0.66780 0.70300 0.06480  -0.01730 0.00250  282 GLN A CG  
2107 C CD  . GLN A 288 ? 0.57150 0.81950 0.87220 0.06970  -0.00830 -0.00040 282 GLN A CD  
2108 O OE1 . GLN A 288 ? 0.64820 0.87430 0.93640 0.07040  -0.00710 -0.00090 282 GLN A OE1 
2109 N NE2 . GLN A 288 ? 0.48610 0.74310 0.79990 0.07230  -0.00180 -0.00250 282 GLN A NE2 
2110 N N   . LEU A 289 ? 0.22450 0.46050 0.48310 0.03380  -0.02830 0.00000  283 LEU A N   
2111 C CA  . LEU A 289 ? 0.24110 0.46110 0.48440 0.02940  -0.03120 -0.00060 283 LEU A CA  
2112 C C   . LEU A 289 ? 0.28850 0.52070 0.53050 0.02280  -0.03920 0.00090  283 LEU A C   
2113 O O   . LEU A 289 ? 0.33040 0.55110 0.56030 0.01920  -0.04230 0.00030  283 LEU A O   
2114 C CB  . LEU A 289 ? 0.23210 0.43400 0.46700 0.02310  -0.02530 -0.00540 283 LEU A CB  
2115 C CG  . LEU A 289 ? 0.22130 0.40730 0.45360 0.02890  -0.01850 -0.00730 283 LEU A CG  
2116 C CD1 . LEU A 289 ? 0.18440 0.35750 0.41060 0.02280  -0.01300 -0.01230 283 LEU A CD1 
2117 C CD2 . LEU A 289 ? 0.22700 0.39910 0.44940 0.03370  -0.02060 -0.00510 283 LEU A CD2 
2118 N N   . GLY A 290 ? 0.26660 0.52200 0.52080 0.02050  -0.04270 0.00250  284 GLY A N   
2119 C CA  . GLY A 290 ? 0.28410 0.55120 0.53670 0.01400  -0.05100 0.00390  284 GLY A CA  
2120 C C   . GLY A 290 ? 0.31150 0.58050 0.56440 0.00060  -0.05200 0.00210  284 GLY A C   
2121 O O   . GLY A 290 ? 0.37430 0.64720 0.62290 -0.00650 -0.05920 0.00290  284 GLY A O   
2122 N N   . THR A 291 ? 0.26990 0.53540 0.52740 -0.00320 -0.04530 -0.00040 285 THR A N   
2123 C CA  . THR A 291 ? 0.25980 0.52460 0.51750 -0.01570 -0.04580 -0.00260 285 THR A CA  
2124 C C   . THR A 291 ? 0.25050 0.53070 0.52420 -0.01760 -0.04210 -0.00190 285 THR A C   
2125 O O   . THR A 291 ? 0.26280 0.54880 0.54510 -0.00950 -0.03630 -0.00150 285 THR A O   
2126 C CB  . THR A 291 ? 0.25880 0.49870 0.50200 -0.01950 -0.04050 -0.00810 285 THR A CB  
2127 O OG1 . THR A 291 ? 0.27660 0.51540 0.51980 -0.03100 -0.04080 -0.01070 285 THR A OG1 
2128 C CG2 . THR A 291 ? 0.22200 0.45220 0.46550 -0.01290 -0.03150 -0.01030 285 THR A CG2 
2129 N N   . ASP A 292 ? 0.23620 0.52230 0.51480 -0.02830 -0.04550 -0.00190 286 ASP A N   
2130 C CA  . ASP A 292 ? 0.27440 0.57710 0.57020 -0.03050 -0.04250 -0.00060 286 ASP A CA  
2131 C C   . ASP A 292 ? 0.32470 0.61920 0.62050 -0.03740 -0.03500 -0.00510 286 ASP A C   
2132 O O   . ASP A 292 ? 0.24360 0.55130 0.55370 -0.04040 -0.03170 -0.00460 286 ASP A O   
2133 C CB  . ASP A 292 ? 0.34230 0.65990 0.64880 -0.03680 -0.05160 0.00340  286 ASP A CB  
2134 C CG  . ASP A 292 ? 0.49650 0.83570 0.81580 -0.02780 -0.05380 0.00930  286 ASP A CG  
2135 O OD1 . ASP A 292 ? 0.47240 0.82360 0.80320 -0.02170 -0.04670 0.00940  286 ASP A OD1 
2136 O OD2 . ASP A 292 ? 0.53890 0.88330 0.85660 -0.02620 -0.06250 0.01360  286 ASP A OD2 
2137 N N   . GLY A 293 ? 0.21050 0.48160 0.48880 -0.03880 -0.03140 -0.01000 287 GLY A N   
2138 C CA  . GLY A 293 ? 0.24020 0.50100 0.51520 -0.04420 -0.02370 -0.01460 287 GLY A CA  
2139 C C   . GLY A 293 ? 0.18760 0.43040 0.45100 -0.03760 -0.01650 -0.01780 287 GLY A C   
2140 O O   . GLY A 293 ? 0.21140 0.45340 0.47450 -0.02790 -0.01620 -0.01640 287 GLY A O   
2141 N N   . ALA A 294 ? 0.17200 0.40020 0.42600 -0.04290 -0.01120 -0.02190 288 ALA A N   
2142 C CA  . ALA A 294 ? 0.15690 0.36790 0.39980 -0.03810 -0.00510 -0.02480 288 ALA A CA  
2143 C C   . ALA A 294 ? 0.20090 0.39710 0.43010 -0.03470 -0.00940 -0.02470 288 ALA A C   
2144 O O   . ALA A 294 ? 0.21370 0.41140 0.44010 -0.03700 -0.01640 -0.02310 288 ALA A O   
2145 C CB  . ALA A 294 ? 0.17080 0.37200 0.40740 -0.04540 0.00100  -0.02820 288 ALA A CB  
2146 N N   . LEU A 295 ? 0.17340 0.35520 0.39400 -0.02970 -0.00510 -0.02660 289 LEU A N   
2147 C CA  . LEU A 295 ? 0.17380 0.34210 0.38310 -0.02550 -0.00830 -0.02620 289 LEU A CA  
2148 C C   . LEU A 295 ? 0.19530 0.34620 0.39300 -0.02650 -0.00340 -0.02900 289 LEU A C   
2149 O O   . LEU A 295 ? 0.16690 0.31670 0.36610 -0.02730 0.00280  -0.03120 289 LEU A O   
2150 C CB  . LEU A 295 ? 0.23330 0.40560 0.44780 -0.01560 -0.00940 -0.02370 289 LEU A CB  
2151 C CG  . LEU A 295 ? 0.26900 0.43160 0.47670 -0.00840 -0.01190 -0.02210 289 LEU A CG  
2152 C CD1 . LEU A 295 ? 0.30220 0.47950 0.52020 -0.00240 -0.01570 -0.01810 289 LEU A CD1 
2153 C CD2 . LEU A 295 ? 0.27110 0.42180 0.47540 -0.00400 -0.00610 -0.02420 289 LEU A CD2 
2154 N N   . GLY A 296 ? 0.15770 0.29590 0.34420 -0.02680 -0.00620 -0.02900 290 GLY A N   
2155 C CA  . GLY A 296 ? 0.15020 0.27300 0.32620 -0.02700 -0.00250 -0.03070 290 GLY A CA  
2156 C C   . GLY A 296 ? 0.18560 0.29850 0.35580 -0.02000 -0.00430 -0.02960 290 GLY A C   
2157 O O   . GLY A 296 ? 0.20670 0.32090 0.37680 -0.01710 -0.00920 -0.02760 290 GLY A O   
2158 N N   . ILE A 297 ? 0.16460 0.26840 0.33040 -0.01770 -0.00020 -0.03080 291 ILE A N   
2159 C CA  . ILE A 297 ? 0.14520 0.23910 0.30580 -0.01190 -0.00140 -0.02980 291 ILE A CA  
2160 C C   . ILE A 297 ? 0.13970 0.22220 0.29120 -0.01430 0.00060  -0.03050 291 ILE A C   
2161 O O   . ILE A 297 ? 0.15100 0.23320 0.30180 -0.01760 0.00500  -0.03240 291 ILE A O   
2162 C CB  . ILE A 297 ? 0.09090 0.18590 0.25660 -0.00640 0.00140  -0.03060 291 ILE A CB  
2163 C CG1 . ILE A 297 ? 0.14460 0.25260 0.32130 -0.00360 0.00050  -0.02950 291 ILE A CG1 
2164 C CG2 . ILE A 297 ? 0.14230 0.22620 0.30230 -0.00160 -0.00010 -0.02930 291 ILE A CG2 
2165 C CD1 . ILE A 297 ? 0.12440 0.23270 0.30700 0.00170  0.00440  -0.03080 291 ILE A CD1 
2166 N N   . SER A 298 ? 0.13430 0.20830 0.27960 -0.01270 -0.00240 -0.02880 292 SER A N   
2167 C CA  . SER A 298 ? 0.11930 0.18340 0.25760 -0.01360 -0.00080 -0.02850 292 SER A CA  
2168 C C   . SER A 298 ? 0.14500 0.20160 0.28010 -0.00830 -0.00270 -0.02670 292 SER A C   
2169 O O   . SER A 298 ? 0.15010 0.20670 0.28590 -0.00510 -0.00600 -0.02510 292 SER A O   
2170 C CB  . SER A 298 ? 0.16230 0.22240 0.29630 -0.01860 -0.00150 -0.02800 292 SER A CB  
2171 O OG  . SER A 298 ? 0.17820 0.23900 0.31240 -0.01850 -0.00570 -0.02740 292 SER A OG  
2172 N N   . VAL A 299 ? 0.16240 0.21330 0.29400 -0.00790 -0.00080 -0.02670 293 VAL A N   
2173 C CA  . VAL A 299 ? 0.14070 0.18530 0.27000 -0.00380 -0.00190 -0.02530 293 VAL A CA  
2174 C C   . VAL A 299 ? 0.14050 0.17950 0.26530 -0.00490 -0.00150 -0.02390 293 VAL A C   
2175 O O   . VAL A 299 ? 0.11900 0.15980 0.24320 -0.00860 0.00090  -0.02480 293 VAL A O   
2176 C CB  . VAL A 299 ? 0.12180 0.16800 0.25470 -0.00170 0.00010  -0.02760 293 VAL A CB  
2177 C CG1 . VAL A 299 ? 0.16490 0.20390 0.29530 0.00110  -0.00110 -0.02620 293 VAL A CG1 
2178 C CG2 . VAL A 299 ? 0.13970 0.19260 0.27890 0.00010  -0.00030 -0.02810 293 VAL A CG2 
2179 N N   . LYS A 300 ? 0.13880 0.17160 0.26070 -0.00210 -0.00370 -0.02120 294 LYS A N   
2180 C CA  . LYS A 300 ? 0.13200 0.16060 0.25140 -0.00230 -0.00380 -0.01890 294 LYS A CA  
2181 C C   . LYS A 300 ? 0.15950 0.18400 0.27720 0.00070  -0.00500 -0.01750 294 LYS A C   
2182 O O   . LYS A 300 ? 0.15020 0.17200 0.26680 0.00270  -0.00630 -0.01610 294 LYS A O   
2183 C CB  . LYS A 300 ? 0.15020 0.17540 0.26920 -0.00290 -0.00480 -0.01640 294 LYS A CB  
2184 C CG  . LYS A 300 ? 0.12500 0.14570 0.24320 -0.00130 -0.00540 -0.01250 294 LYS A CG  
2185 C CD  . LYS A 300 ? 0.15380 0.17740 0.27290 -0.00420 -0.00430 -0.01170 294 LYS A CD  
2186 C CE  . LYS A 300 ? 0.16000 0.18090 0.28000 -0.00170 -0.00570 -0.00660 294 LYS A CE  
2187 N NZ  . LYS A 300 ? 0.17920 0.20240 0.29700 -0.00380 -0.00580 -0.00400 294 LYS A NZ  
2188 N N   . ILE A 301 ? 0.10970 0.13480 0.22750 0.00010  -0.00440 -0.01800 295 ILE A N   
2189 C CA  . ILE A 301 ? 0.13240 0.15400 0.24930 0.00170  -0.00550 -0.01640 295 ILE A CA  
2190 C C   . ILE A 301 ? 0.13480 0.15430 0.24940 0.00210  -0.00680 -0.01200 295 ILE A C   
2191 O O   . ILE A 301 ? 0.12950 0.15200 0.24510 0.00060  -0.00700 -0.01090 295 ILE A O   
2192 C CB  . ILE A 301 ? 0.15250 0.17710 0.27260 0.00040  -0.00450 -0.02000 295 ILE A CB  
2193 C CG1 . ILE A 301 ? 0.12450 0.15150 0.24880 0.00020  -0.00220 -0.02480 295 ILE A CG1 
2194 C CG2 . ILE A 301 ? 0.11940 0.14100 0.24050 0.00130  -0.00570 -0.01870 295 ILE A CG2 
2195 C CD1 . ILE A 301 ? 0.13160 0.15490 0.25750 0.00270  -0.00260 -0.02410 295 ILE A CD1 
2196 N N   . GLU A 302 ? 0.10430 0.11930 0.21620 0.00370  -0.00750 -0.00900 296 GLU A N   
2197 C CA  . GLU A 302 ? 0.12680 0.13980 0.23700 0.00450  -0.00780 -0.00470 296 GLU A CA  
2198 C C   . GLU A 302 ? 0.16150 0.17730 0.27320 0.00440  -0.00860 -0.00260 296 GLU A C   
2199 O O   . GLU A 302 ? 0.14310 0.15930 0.25560 0.00510  -0.00880 0.00080  296 GLU A O   
2200 C CB  . GLU A 302 ? 0.14470 0.15490 0.25150 0.00580  -0.00750 -0.00250 296 GLU A CB  
2201 C CG  . GLU A 302 ? 0.13250 0.14130 0.23710 0.00720  -0.00680 0.00140  296 GLU A CG  
2202 C CD  . GLU A 302 ? 0.21590 0.22280 0.32070 0.00780  -0.00620 0.00160  296 GLU A CD  
2203 O OE1 . GLU A 302 ? 0.21670 0.22340 0.32290 0.00720  -0.00660 -0.00100 296 GLU A OE1 
2204 O OE2 . GLU A 302 ? 0.24200 0.24750 0.34660 0.00910  -0.00520 0.00460  296 GLU A OE2 
2205 N N   . ASP A 303 ? 0.14470 0.16300 0.25820 0.00360  -0.00930 -0.00410 297 ASP A N   
2206 C CA  . ASP A 303 ? 0.14120 0.16460 0.25690 0.00290  -0.01120 -0.00210 297 ASP A CA  
2207 C C   . ASP A 303 ? 0.13610 0.16660 0.25420 0.00000  -0.01230 -0.00430 297 ASP A C   
2208 O O   . ASP A 303 ? 0.12990 0.16680 0.24980 -0.00180 -0.01490 -0.00240 297 ASP A O   
2209 C CB  . ASP A 303 ? 0.15230 0.17620 0.27020 0.00240  -0.01170 -0.00320 297 ASP A CB  
2210 C CG  . ASP A 303 ? 0.17840 0.20080 0.29850 0.00140  -0.01050 -0.00870 297 ASP A CG  
2211 O OD1 . ASP A 303 ? 0.16530 0.18210 0.28450 0.00280  -0.00900 -0.00910 297 ASP A OD1 
2212 O OD2 . ASP A 303 ? 0.14270 0.17020 0.26540 -0.00110 -0.01080 -0.01280 297 ASP A OD2 
2213 N N   . GLY A 304 ? 0.15710 0.18790 0.27510 -0.00160 -0.01050 -0.00830 298 GLY A N   
2214 C CA  . GLY A 304 ? 0.14450 0.18180 0.26370 -0.00590 -0.01050 -0.01030 298 GLY A CA  
2215 C C   . GLY A 304 ? 0.19520 0.23700 0.31490 -0.00980 -0.01000 -0.01630 298 GLY A C   
2216 O O   . GLY A 304 ? 0.16150 0.20870 0.28000 -0.01470 -0.01000 -0.01830 298 GLY A O   
2217 N N   . ASN A 305 ? 0.17260 0.21130 0.29360 -0.00810 -0.00900 -0.01960 299 ASN A N   
2218 C CA  . ASN A 305 ? 0.17320 0.21490 0.29620 -0.01180 -0.00800 -0.02620 299 ASN A CA  
2219 C C   . ASN A 305 ? 0.14050 0.18310 0.26480 -0.01310 -0.00350 -0.03230 299 ASN A C   
2220 O O   . ASN A 305 ? 0.14860 0.18740 0.27550 -0.00910 -0.00130 -0.03280 299 ASN A O   
2221 C CB  . ASN A 305 ? 0.18240 0.21970 0.30890 -0.00950 -0.00800 -0.02730 299 ASN A CB  
2222 C CG  . ASN A 305 ? 0.21160 0.25090 0.34040 -0.01400 -0.00700 -0.03460 299 ASN A CG  
2223 O OD1 . ASN A 305 ? 0.19450 0.23340 0.32570 -0.01500 -0.00310 -0.04100 299 ASN A OD1 
2224 N ND2 . ASN A 305 ? 0.21400 0.25520 0.34220 -0.01700 -0.01010 -0.03390 299 ASN A ND2 
2225 N N   . LEU A 306 ? 0.14830 0.19650 0.27070 -0.01910 -0.00210 -0.03730 300 LEU A N   
2226 C CA  . LEU A 306 ? 0.18600 0.23630 0.30980 -0.02080 0.00350  -0.04310 300 LEU A CA  
2227 C C   . LEU A 306 ? 0.19040 0.23880 0.32050 -0.01950 0.00750  -0.05040 300 LEU A C   
2228 O O   . LEU A 306 ? 0.14050 0.18930 0.27610 -0.01670 0.01170  -0.05280 300 LEU A O   
2229 C CB  . LEU A 306 ? 0.23940 0.29200 0.35010 -0.02660 0.00510  -0.04450 300 LEU A CB  
2230 C CG  . LEU A 306 ? 0.35260 0.40560 0.45360 -0.02820 0.00290  -0.03720 300 LEU A CG  
2231 C CD1 . LEU A 306 ? 0.39770 0.45270 0.48630 -0.03380 0.00670  -0.03990 300 LEU A CD1 
2232 C CD2 . LEU A 306 ? 0.27840 0.32960 0.38510 -0.02500 0.00370  -0.03290 300 LEU A CD2 
2233 N N   . GLU A 307 ? 0.15640 0.20320 0.28640 -0.02210 0.00650  -0.05450 301 GLU A N   
2234 C CA  . GLU A 307 ? 0.18770 0.23060 0.32540 -0.02060 0.01090  -0.06160 301 GLU A CA  
2235 C C   . GLU A 307 ? 0.18450 0.22380 0.33170 -0.01260 0.01120  -0.05760 301 GLU A C   
2236 O O   . GLU A 307 ? 0.17010 0.20890 0.32530 -0.00960 0.01580  -0.06150 301 GLU A O   
2237 C CB  . GLU A 307 ? 0.18820 0.22710 0.32340 -0.02400 0.00870  -0.06450 301 GLU A CB  
2238 C CG  . GLU A 307 ? 0.26720 0.29980 0.40680 -0.02430 0.01450  -0.07360 301 GLU A CG  
2239 C CD  . GLU A 307 ? 0.28060 0.30830 0.41650 -0.02790 0.01230  -0.07580 301 GLU A CD  
2240 O OE1 . GLU A 307 ? 0.31290 0.34180 0.44810 -0.02720 0.00660  -0.06850 301 GLU A OE1 
2241 O OE2 . GLU A 307 ? 0.30310 0.32570 0.43570 -0.03120 0.01680  -0.08420 301 GLU A OE2 
2242 N N   . MET A 308 ? 0.17700 0.21260 0.32100 -0.00910 0.00630  -0.04940 302 MET A N   
2243 C CA  . MET A 308 ? 0.16820 0.19750 0.31520 -0.00340 0.00560  -0.04520 302 MET A CA  
2244 C C   . MET A 308 ? 0.13740 0.16830 0.28150 -0.00190 0.00620  -0.04280 302 MET A C   
2245 O O   . MET A 308 ? 0.16400 0.19250 0.31090 0.00060  0.00660  -0.04180 302 MET A O   
2246 C CB  . MET A 308 ? 0.16450 0.18960 0.30700 -0.00180 0.00120  -0.03790 302 MET A CB  
2247 C CG  . MET A 308 ? 0.14330 0.16720 0.29020 -0.00330 0.00070  -0.03990 302 MET A CG  
2248 S SD  . MET A 308 ? 0.21530 0.23260 0.37500 -0.00170 0.00420  -0.04500 302 MET A SD  
2249 C CE  . MET A 308 ? 0.15900 0.18110 0.32380 -0.00660 0.00940  -0.05660 302 MET A CE  
2250 N N   . LEU A 309 ? 0.12470 0.16030 0.26310 -0.00410 0.00570  -0.04100 303 LEU A N   
2251 C CA  . LEU A 309 ? 0.12880 0.16720 0.26610 -0.00380 0.00690  -0.04000 303 LEU A CA  
2252 C C   . LEU A 309 ? 0.15160 0.19300 0.29560 -0.00340 0.01140  -0.04550 303 LEU A C   
2253 O O   . LEU A 309 ? 0.14330 0.18490 0.28940 -0.00090 0.01100  -0.04350 303 LEU A O   
2254 C CB  . LEU A 309 ? 0.11020 0.15340 0.24240 -0.00790 0.00710  -0.03880 303 LEU A CB  
2255 C CG  . LEU A 309 ? 0.12220 0.16880 0.25400 -0.00900 0.00890  -0.03810 303 LEU A CG  
2256 C CD1 . LEU A 309 ? 0.12870 0.17140 0.25860 -0.00580 0.00540  -0.03300 303 LEU A CD1 
2257 C CD2 . LEU A 309 ? 0.08920 0.14000 0.21690 -0.01470 0.01050  -0.03760 303 LEU A CD2 
2258 N N   . TYR A 310 ? 0.14520 0.19050 0.29260 -0.00650 0.01600  -0.05260 304 TYR A N   
2259 C CA  . TYR A 310 ? 0.15110 0.19970 0.30470 -0.00630 0.02170  -0.05830 304 TYR A CA  
2260 C C   . TYR A 310 ? 0.18260 0.22580 0.34240 -0.00180 0.02150  -0.05780 304 TYR A C   
2261 O O   . TYR A 310 ? 0.19270 0.23810 0.35680 0.00060  0.02360  -0.05760 304 TYR A O   
2262 C CB  . TYR A 310 ? 0.17710 0.23010 0.33140 -0.01130 0.02780  -0.06700 304 TYR A CB  
2263 C CG  . TYR A 310 ? 0.17110 0.23060 0.31780 -0.01760 0.02860  -0.06660 304 TYR A CG  
2264 C CD1 . TYR A 310 ? 0.21430 0.27610 0.35780 -0.01760 0.02770  -0.06140 304 TYR A CD1 
2265 C CD2 . TYR A 310 ? 0.22970 0.28690 0.36310 -0.02330 0.02840  -0.06900 304 TYR A CD2 
2266 C CE1 . TYR A 310 ? 0.22900 0.29520 0.36520 -0.02400 0.02900  -0.06040 304 TYR A CE1 
2267 C CE2 . TYR A 310 ? 0.23980 0.29900 0.36020 -0.02850 0.02800  -0.06610 304 TYR A CE2 
2268 C CZ  . TYR A 310 ? 0.26270 0.32590 0.38510 -0.02870 0.02890  -0.06180 304 TYR A CZ  
2269 O OH  . TYR A 310 ? 0.28360 0.34720 0.39290 -0.03370 0.02910  -0.05840 304 TYR A OH  
2270 N N   . ALA A 311 ? 0.16230 0.19930 0.32320 -0.00100 0.01920  -0.05720 305 ALA A N   
2271 C CA  . ALA A 311 ? 0.16930 0.20110 0.33500 0.00250  0.01890  -0.05500 305 ALA A CA  
2272 C C   . ALA A 311 ? 0.14480 0.17720 0.30800 0.00610  0.01480  -0.04700 305 ALA A C   
2273 O O   . ALA A 311 ? 0.14340 0.17750 0.31120 0.00950  0.01620  -0.04580 305 ALA A O   
2274 C CB  . ALA A 311 ? 0.17300 0.19880 0.34030 0.00150  0.01720  -0.05500 305 ALA A CB  
2275 N N   . VAL A 312 ? 0.12570 0.15750 0.28160 0.00550  0.01020  -0.04180 306 VAL A N   
2276 C CA  A VAL A 312 ? 0.15470 0.18760 0.30730 0.00810  0.00660  -0.03540 306 VAL A CA  
2277 C CA  B VAL A 312 ? 0.15440 0.18720 0.30740 0.00830  0.00680  -0.03550 306 VAL A CA  
2278 C C   . VAL A 312 ? 0.17010 0.21080 0.32540 0.00880  0.00780  -0.03610 306 VAL A C   
2279 O O   . VAL A 312 ? 0.16690 0.21120 0.32500 0.01200  0.00660  -0.03300 306 VAL A O   
2280 C CB  A VAL A 312 ? 0.15880 0.18880 0.30280 0.00690  0.00280  -0.03120 306 VAL A CB  
2281 C CB  B VAL A 312 ? 0.15970 0.18900 0.30420 0.00740  0.00270  -0.03070 306 VAL A CB  
2282 C CG1 A VAL A 312 ? 0.16110 0.19340 0.30200 0.00890  -0.00010 -0.02640 306 VAL A CG1 
2283 C CG1 B VAL A 312 ? 0.18330 0.20640 0.32740 0.00680  0.00200  -0.03010 306 VAL A CG1 
2284 C CG2 A VAL A 312 ? 0.18150 0.20530 0.32410 0.00660  0.00160  -0.02960 306 VAL A CG2 
2285 C CG2 B VAL A 312 ? 0.14630 0.17810 0.28620 0.00480  0.00250  -0.03150 306 VAL A CG2 
2286 N N   . VAL A 313 ? 0.16120 0.20610 0.31590 0.00560  0.01030  -0.03970 307 VAL A N   
2287 C CA  A VAL A 313 ? 0.15880 0.21240 0.31730 0.00530  0.01200  -0.04040 307 VAL A CA  
2288 C CA  B VAL A 313 ? 0.15240 0.20590 0.31080 0.00540  0.01180  -0.04020 307 VAL A CA  
2289 C C   . VAL A 313 ? 0.18280 0.24000 0.35030 0.00860  0.01540  -0.04240 307 VAL A C   
2290 O O   . VAL A 313 ? 0.15770 0.22150 0.32990 0.01130  0.01440  -0.03970 307 VAL A O   
2291 C CB  A VAL A 313 ? 0.13700 0.19450 0.29310 0.00050  0.01520  -0.04390 307 VAL A CB  
2292 C CB  B VAL A 313 ? 0.13770 0.19530 0.29360 0.00070  0.01470  -0.04330 307 VAL A CB  
2293 C CG1 A VAL A 313 ? 0.08910 0.15630 0.25050 -0.00060 0.01810  -0.04500 307 VAL A CG1 
2294 C CG1 B VAL A 313 ? 0.12850 0.18310 0.27620 -0.00160 0.01110  -0.03970 307 VAL A CG1 
2295 C CG2 A VAL A 313 ? 0.12760 0.18220 0.27540 -0.00190 0.01160  -0.04030 307 VAL A CG2 
2296 C CG2 B VAL A 313 ? 0.13670 0.19370 0.29400 -0.00150 0.01970  -0.04950 307 VAL A CG2 
2297 N N   . THR A 314 ? 0.14330 0.19680 0.31410 0.00870  0.01960  -0.04720 308 THR A N   
2298 C CA  . THR A 314 ? 0.16270 0.21860 0.34220 0.01240  0.02370  -0.04910 308 THR A CA  
2299 C C   . THR A 314 ? 0.17090 0.22470 0.35300 0.01780  0.02040  -0.04340 308 THR A C   
2300 O O   . THR A 314 ? 0.20310 0.26290 0.39220 0.02230  0.02160  -0.04170 308 THR A O   
2301 C CB  . THR A 314 ? 0.16390 0.21510 0.34540 0.01080  0.02980  -0.05640 308 THR A CB  
2302 O OG1 . THR A 314 ? 0.15410 0.20720 0.33070 0.00520  0.03210  -0.06130 308 THR A OG1 
2303 C CG2 . THR A 314 ? 0.20050 0.25510 0.39040 0.01430  0.03600  -0.05940 308 THR A CG2 
2304 N N   . GLU A 315 ? 0.15040 0.19660 0.32710 0.01780  0.01660  -0.04010 309 GLU A N   
2305 C CA  . GLU A 315 ? 0.18540 0.23020 0.36310 0.02260  0.01380  -0.03420 309 GLU A CA  
2306 C C   . GLU A 315 ? 0.19920 0.25270 0.37650 0.02460  0.00980  -0.02940 309 GLU A C   
2307 O O   . GLU A 315 ? 0.19260 0.25080 0.37490 0.02980  0.00900  -0.02590 309 GLU A O   
2308 C CB  . GLU A 315 ? 0.17430 0.21020 0.34580 0.02120  0.01100  -0.03170 309 GLU A CB  
2309 C CG  . GLU A 315 ? 0.19810 0.23250 0.36850 0.02580  0.00800  -0.02500 309 GLU A CG  
2310 C CD  . GLU A 315 ? 0.24430 0.27590 0.42200 0.03070  0.01130  -0.02470 309 GLU A CD  
2311 O OE1 . GLU A 315 ? 0.22400 0.25340 0.40740 0.03040  0.01630  -0.03000 309 GLU A OE1 
2312 O OE2 . GLU A 315 ? 0.25720 0.28820 0.43460 0.03530  0.00930  -0.01930 309 GLU A OE2 
2313 N N   . LEU A 316 ? 0.17540 0.23190 0.34740 0.02060  0.00750  -0.02960 310 LEU A N   
2314 C CA  . LEU A 316 ? 0.16740 0.23290 0.33970 0.02110  0.00400  -0.02620 310 LEU A CA  
2315 C C   . LEU A 316 ? 0.17690 0.25430 0.35920 0.02290  0.00630  -0.02730 310 LEU A C   
2316 O O   . LEU A 316 ? 0.18160 0.26810 0.36880 0.02640  0.00370  -0.02360 310 LEU A O   
2317 C CB  . LEU A 316 ? 0.17040 0.23490 0.33540 0.01580  0.00230  -0.02700 310 LEU A CB  
2318 C CG  . LEU A 316 ? 0.32630 0.39120 0.48550 0.01520  -0.00260 -0.02300 310 LEU A CG  
2319 C CD1 . LEU A 316 ? 0.28130 0.34200 0.43840 0.01920  -0.00500 -0.01890 310 LEU A CD1 
2320 C CD2 . LEU A 316 ? 0.22640 0.28380 0.37730 0.01110  -0.00270 -0.02420 310 LEU A CD2 
2321 N N   . LEU A 317 ? 0.17270 0.25160 0.35870 0.02070  0.01140  -0.03250 311 LEU A N   
2322 C CA  . LEU A 317 ? 0.19240 0.28280 0.38900 0.02280  0.01470  -0.03360 311 LEU A CA  
2323 C C   . LEU A 317 ? 0.21810 0.31030 0.42250 0.03020  0.01540  -0.03110 311 LEU A C   
2324 O O   . LEU A 317 ? 0.21670 0.32110 0.42930 0.03380  0.01430  -0.02820 311 LEU A O   
2325 C CB  . LEU A 317 ? 0.18420 0.27440 0.38270 0.01940  0.02140  -0.04010 311 LEU A CB  
2326 C CG  . LEU A 317 ? 0.18500 0.27510 0.37660 0.01250  0.02150  -0.04240 311 LEU A CG  
2327 C CD1 . LEU A 317 ? 0.18200 0.27150 0.37440 0.00930  0.02890  -0.04910 311 LEU A CD1 
2328 C CD2 . LEU A 317 ? 0.14310 0.24430 0.33700 0.01030  0.01870  -0.03940 311 LEU A CD2 
2329 N N   . GLU A 318 ? 0.17100 0.25180 0.37330 0.03250  0.01700  -0.03180 312 GLU A N   
2330 C CA  . GLU A 318 ? 0.19590 0.27660 0.40480 0.03980  0.01790  -0.02890 312 GLU A CA  
2331 C C   . GLU A 318 ? 0.24590 0.33150 0.45370 0.04360  0.01160  -0.02190 312 GLU A C   
2332 O O   . GLU A 318 ? 0.26910 0.36430 0.48530 0.04980  0.01100  -0.01880 312 GLU A O   
2333 C CB  . GLU A 318 ? 0.19220 0.25860 0.39860 0.04040  0.02110  -0.03120 312 GLU A CB  
2334 C CG  . GLU A 318 ? 0.25760 0.32220 0.47090 0.04840  0.02280  -0.02830 312 GLU A CG  
2335 C CD  . GLU A 318 ? 0.27190 0.32290 0.48500 0.04840  0.02790  -0.03210 312 GLU A CD  
2336 O OE1 . GLU A 318 ? 0.29390 0.33530 0.50110 0.04710  0.02570  -0.03010 312 GLU A OE1 
2337 O OE2 . GLU A 318 ? 0.32660 0.37680 0.54560 0.04940  0.03450  -0.03740 312 GLU A OE2 
2338 N N   . ARG A 319 ? 0.20300 0.28280 0.40080 0.04050  0.00700  -0.01950 313 ARG A N   
2339 C CA  . ARG A 319 ? 0.21880 0.30400 0.41510 0.04390  0.00140  -0.01350 313 ARG A CA  
2340 C C   . ARG A 319 ? 0.25540 0.35780 0.45860 0.04440  -0.00120 -0.01210 313 ARG A C   
2341 O O   . ARG A 319 ? 0.24860 0.36060 0.45710 0.04990  -0.00440 -0.00780 313 ARG A O   
2342 C CB  . ARG A 319 ? 0.22210 0.29960 0.40670 0.03980  -0.00240 -0.01190 313 ARG A CB  
2343 C CG  . ARG A 319 ? 0.28330 0.34610 0.46130 0.03800  -0.00040 -0.01300 313 ARG A CG  
2344 C CD  . ARG A 319 ? 0.24310 0.30070 0.42020 0.04300  -0.00140 -0.00860 313 ARG A CD  
2345 N NE  . ARG A 319 ? 0.23830 0.28310 0.41010 0.03990  0.00050  -0.00990 313 ARG A NE  
2346 C CZ  . ARG A 319 ? 0.23040 0.26930 0.39420 0.03810  -0.00180 -0.00730 313 ARG A CZ  
2347 N NH1 . ARG A 319 ? 0.25890 0.30200 0.41790 0.03920  -0.00590 -0.00340 313 ARG A NH1 
2348 N NH2 . ARG A 319 ? 0.22550 0.25480 0.38700 0.03510  0.00040  -0.00870 313 ARG A NH2 
2349 N N   . LEU A 320 ? 0.17260 0.27950 0.37570 0.03830  -0.00020 -0.01560 314 LEU A N   
2350 C CA  . LEU A 320 ? 0.18780 0.31130 0.39750 0.03680  -0.00280 -0.01460 314 LEU A CA  
2351 C C   . LEU A 320 ? 0.19500 0.33130 0.41850 0.04100  0.00060  -0.01500 314 LEU A C   
2352 O O   . LEU A 320 ? 0.19640 0.34940 0.42790 0.04040  -0.00160 -0.01350 314 LEU A O   
2353 C CB  . LEU A 320 ? 0.12950 0.25190 0.33380 0.02840  -0.00250 -0.01800 314 LEU A CB  
2354 C CG  . LEU A 320 ? 0.17670 0.28940 0.36880 0.02440  -0.00630 -0.01730 314 LEU A CG  
2355 C CD1 . LEU A 320 ? 0.15980 0.26840 0.34680 0.01710  -0.00410 -0.02140 314 LEU A CD1 
2356 C CD2 . LEU A 320 ? 0.15450 0.27560 0.34600 0.02460  -0.01260 -0.01330 314 LEU A CD2 
2357 N N   . GLY A 321 ? 0.16480 0.29450 0.39210 0.04530  0.00610  -0.01720 315 GLY A N   
2358 C CA  . GLY A 321 ? 0.21600 0.35730 0.45680 0.04990  0.01030  -0.01800 315 GLY A CA  
2359 C C   . GLY A 321 ? 0.26370 0.41330 0.50910 0.04430  0.01420  -0.02210 315 GLY A C   
2360 O O   . GLY A 321 ? 0.23840 0.40310 0.49640 0.04700  0.01640  -0.02180 315 GLY A O   
2361 N N   . ILE A 322 ? 0.21750 0.35820 0.45350 0.03660  0.01520  -0.02580 316 ILE A N   
2362 C CA  . ILE A 322 ? 0.27140 0.41900 0.51050 0.03080  0.01910  -0.02970 316 ILE A CA  
2363 C C   . ILE A 322 ? 0.29650 0.43850 0.53870 0.03210  0.02770  -0.03520 316 ILE A C   
2364 O O   . ILE A 322 ? 0.32140 0.44840 0.55560 0.03120  0.03000  -0.03850 316 ILE A O   
2365 C CB  . ILE A 322 ? 0.24530 0.38650 0.47280 0.02240  0.01650  -0.03090 316 ILE A CB  
2366 C CG1 . ILE A 322 ? 0.24620 0.39770 0.47430 0.02020  0.00950  -0.02640 316 ILE A CG1 
2367 C CG2 . ILE A 322 ? 0.19500 0.33780 0.42270 0.01630  0.02240  -0.03600 316 ILE A CG2 
2368 C CD1 . ILE A 322 ? 0.28450 0.42640 0.50010 0.01520  0.00530  -0.02610 316 ILE A CD1 
2369 N N   . GLY A 323 ? 0.31090 0.46570 0.56520 0.03440  0.03260  -0.03630 317 GLY A N   
2370 C CA  . GLY A 323 ? 0.29630 0.44710 0.55470 0.03650  0.04150  -0.04180 317 GLY A CA  
2371 C C   . GLY A 323 ? 0.40310 0.55410 0.67020 0.04620  0.04360  -0.04010 317 GLY A C   
2372 O O   . GLY A 323 ? 0.45660 0.60910 0.72520 0.05150  0.03780  -0.03460 317 GLY A O   
2373 N N   . SER A 324 ? 0.39700 0.54630 0.66950 0.04870  0.05230  -0.04510 318 SER A N   
2374 C CA  . SER A 324 ? 0.43050 0.57520 0.70900 0.05780  0.05480  -0.04430 318 SER A CA  
2375 C C   . SER A 324 ? 0.43580 0.55930 0.70310 0.05660  0.05590  -0.04750 318 SER A C   
2376 O O   . SER A 324 ? 0.44350 0.55800 0.69990 0.04890  0.05580  -0.05130 318 SER A O   
2377 C CB  . SER A 324 ? 0.38980 0.54200 0.68010 0.06220  0.06430  -0.04810 318 SER A CB  
2378 O OG  . SER A 324 ? 0.38570 0.52770 0.66910 0.05670  0.07220  -0.05610 318 SER A OG  
2379 N N   . PRO A 325 ? 0.46950 0.58510 0.73960 0.06390  0.05660  -0.04580 319 PRO A N   
2380 C CA  . PRO A 325 ? 0.46980 0.56580 0.73120 0.06210  0.05960  -0.05010 319 PRO A CA  
2381 C C   . PRO A 325 ? 0.42460 0.51460 0.68350 0.05760  0.06900  -0.05930 319 PRO A C   
2382 O O   . PRO A 325 ? 0.39270 0.47050 0.64120 0.05130  0.06970  -0.06390 319 PRO A O   
2383 C CB  . PRO A 325 ? 0.48570 0.57700 0.75370 0.07170  0.06030  -0.04660 319 PRO A CB  
2384 C CG  . PRO A 325 ? 0.46100 0.56700 0.73510 0.07680  0.05280  -0.03830 319 PRO A CG  
2385 C CD  . PRO A 325 ? 0.44240 0.56620 0.72230 0.07340  0.05340  -0.03930 319 PRO A CD  
2386 N N   . ASP A 326 ? 0.42910 0.52820 0.69730 0.06080  0.07630  -0.06230 320 ASP A N   
2387 C CA  . ASP A 326 ? 0.46070 0.55490 0.72520 0.05630  0.08590  -0.07140 320 ASP A CA  
2388 C C   . ASP A 326 ? 0.38690 0.48320 0.64170 0.04610  0.08440  -0.07430 320 ASP A C   
2389 O O   . ASP A 326 ? 0.44310 0.52950 0.68800 0.04010  0.08890  -0.08140 320 ASP A O   
2390 C CB  . ASP A 326 ? 0.43330 0.53880 0.71010 0.06180  0.09430  -0.07330 320 ASP A CB  
2391 C CG  . ASP A 326 ? 0.59400 0.69510 0.88000 0.07220  0.09810  -0.07230 320 ASP A CG  
2392 O OD1 . ASP A 326 ? 0.58370 0.66740 0.86370 0.07300  0.10010  -0.07510 320 ASP A OD1 
2393 O OD2 . ASP A 326 ? 0.75680 0.87230 1.05660 0.07960  0.09950  -0.06870 320 ASP A OD2 
2394 N N   . VAL A 327 ? 0.32990 0.43920 0.58690 0.04400  0.07840  -0.06920 321 VAL A N   
2395 C CA  . VAL A 327 ? 0.37650 0.48730 0.62430 0.03460  0.07720  -0.07150 321 VAL A CA  
2396 C C   . VAL A 327 ? 0.37200 0.46920 0.60710 0.02980  0.07200  -0.07230 321 VAL A C   
2397 O O   . VAL A 327 ? 0.33400 0.42500 0.55940 0.02320  0.07530  -0.07830 321 VAL A O   
2398 C CB  . VAL A 327 ? 0.35910 0.48560 0.61220 0.03320  0.07170  -0.06560 321 VAL A CB  
2399 C CG1 . VAL A 327 ? 0.30300 0.42780 0.54500 0.02400  0.06850  -0.06650 321 VAL A CG1 
2400 C CG2 . VAL A 327 ? 0.33060 0.47210 0.59580 0.03550  0.07850  -0.06650 321 VAL A CG2 
2401 N N   . ARG A 328 ? 0.30470 0.39780 0.53960 0.03320  0.06430  -0.06630 322 ARG A N   
2402 C CA  . ARG A 328 ? 0.36850 0.45070 0.59250 0.02880  0.05900  -0.06610 322 ARG A CA  
2403 C C   . ARG A 328 ? 0.38440 0.45280 0.60370 0.02760  0.06390  -0.07250 322 ARG A C   
2404 O O   . ARG A 328 ? 0.39300 0.45440 0.60320 0.02190  0.06210  -0.07520 322 ARG A O   
2405 C CB  . ARG A 328 ? 0.34270 0.42460 0.56700 0.03240  0.05000  -0.05780 322 ARG A CB  
2406 C CG  . ARG A 328 ? 0.36060 0.45510 0.58660 0.03170  0.04420  -0.05220 322 ARG A CG  
2407 C CD  . ARG A 328 ? 0.27860 0.37090 0.50120 0.03400  0.03570  -0.04510 322 ARG A CD  
2408 N NE  . ARG A 328 ? 0.41510 0.50480 0.64340 0.04170  0.03580  -0.04190 322 ARG A NE  
2409 C CZ  . ARG A 328 ? 0.36760 0.46840 0.60510 0.04820  0.03440  -0.03730 322 ARG A CZ  
2410 N NH1 . ARG A 328 ? 0.35080 0.46680 0.59340 0.04720  0.03220  -0.03520 322 ARG A NH1 
2411 N NH2 . ARG A 328 ? 0.40760 0.50470 0.64980 0.05560  0.03520  -0.03480 322 ARG A NH2 
2412 N N   . SER A 329 ? 0.35400 0.41860 0.57930 0.03280  0.07040  -0.07520 323 SER A N   
2413 C CA  . SER A 329 ? 0.35650 0.40750 0.57650 0.03090  0.07580  -0.08200 323 SER A CA  
2414 C C   . SER A 329 ? 0.32560 0.37530 0.53640 0.02290  0.08130  -0.09080 323 SER A C   
2415 O O   . SER A 329 ? 0.32250 0.36180 0.52540 0.01870  0.08370  -0.09670 323 SER A O   
2416 C CB  . SER A 329 ? 0.40990 0.45690 0.63780 0.03820  0.08280  -0.08370 323 SER A CB  
2417 O OG  . SER A 329 ? 0.45450 0.50740 0.68490 0.03800  0.09140  -0.08940 323 SER A OG  
2418 N N   . GLN A 330 ? 0.30760 0.36800 0.51830 0.02010  0.08350  -0.09170 324 GLN A N   
2419 C CA  . GLN A 330 ? 0.33700 0.39740 0.53660 0.01180  0.08760  -0.09870 324 GLN A CA  
2420 C C   . GLN A 330 ? 0.33000 0.38660 0.52030 0.00600  0.08080  -0.09810 324 GLN A C   
2421 O O   . GLN A 330 ? 0.32330 0.37710 0.50260 -0.00060 0.08420  -0.10470 324 GLN A O   
2422 C CB  . GLN A 330 ? 0.32560 0.39890 0.52750 0.01010  0.09060  -0.09800 324 GLN A CB  
2423 C CG  . GLN A 330 ? 0.34120 0.42030 0.55440 0.01650  0.09730  -0.09820 324 GLN A CG  
2424 C CD  . GLN A 330 ? 0.39750 0.48910 0.61260 0.01380  0.10280  -0.09920 324 GLN A CD  
2425 O OE1 . GLN A 330 ? 0.35520 0.44830 0.56000 0.00610  0.10460  -0.10220 324 GLN A OE1 
2426 N NE2 . GLN A 330 ? 0.32680 0.42820 0.55540 0.02020  0.10560  -0.09630 324 GLN A NE2 
2427 N N   . LEU A 331 ? 0.27880 0.33570 0.47240 0.00850  0.07150  -0.09030 325 LEU A N   
2428 C CA  . LEU A 331 ? 0.30130 0.35490 0.48730 0.00390  0.06530  -0.08920 325 LEU A CA  
2429 C C   . LEU A 331 ? 0.25340 0.29640 0.43940 0.00550  0.06210  -0.08860 325 LEU A C   
2430 O O   . LEU A 331 ? 0.23610 0.27700 0.41850 0.00340  0.05570  -0.08560 325 LEU A O   
2431 C CB  . LEU A 331 ? 0.29550 0.35620 0.48240 0.00430  0.05740  -0.08110 325 LEU A CB  
2432 C CG  . LEU A 331 ? 0.28290 0.35470 0.47150 0.00280  0.05990  -0.08020 325 LEU A CG  
2433 C CD1 . LEU A 331 ? 0.24310 0.32020 0.43320 0.00400  0.05180  -0.07190 325 LEU A CD1 
2434 C CD2 . LEU A 331 ? 0.24460 0.31860 0.42380 -0.00470 0.06520  -0.08630 325 LEU A CD2 
2435 N N   . ALA A 332 ? 0.31310 0.34910 0.50250 0.00880  0.06720  -0.09150 326 ALA A N   
2436 C CA  . ALA A 332 ? 0.32650 0.35200 0.51650 0.01030  0.06490  -0.09040 326 ALA A CA  
2437 C C   . ALA A 332 ? 0.30740 0.32790 0.48890 0.00360  0.06330  -0.09500 326 ALA A C   
2438 O O   . ALA A 332 ? 0.25150 0.26700 0.43370 0.00400  0.05800  -0.09110 326 ALA A O   
2439 C CB  . ALA A 332 ? 0.29970 0.31770 0.49350 0.01430  0.07250  -0.09420 326 ALA A CB  
2440 N N   . SER A 333 ? 0.25210 0.27430 0.42450 -0.00270 0.06770  -0.10310 327 SER A N   
2441 C CA  A SER A 333 ? 0.29010 0.30850 0.45280 -0.00920 0.06560  -0.10780 327 SER A CA  
2442 C CA  B SER A 333 ? 0.29010 0.30830 0.45310 -0.00900 0.06550  -0.10760 327 SER A CA  
2443 C C   . SER A 333 ? 0.29550 0.31960 0.45880 -0.00990 0.05720  -0.10190 327 SER A C   
2444 O O   . SER A 333 ? 0.26650 0.28670 0.42590 -0.01290 0.05290  -0.10230 327 SER A O   
2445 C CB  A SER A 333 ? 0.28970 0.30860 0.43880 -0.01600 0.07220  -0.11770 327 SER A CB  
2446 C CB  B SER A 333 ? 0.29060 0.30850 0.43970 -0.01600 0.07190  -0.11770 327 SER A CB  
2447 O OG  A SER A 333 ? 0.28020 0.30950 0.42620 -0.01800 0.07240  -0.11690 327 SER A OG  
2448 O OG  B SER A 333 ? 0.31270 0.32700 0.44990 -0.02280 0.06800  -0.12140 327 SER A OG  
2449 N N   . PHE A 334 ? 0.27780 0.31050 0.44540 -0.00740 0.05460  -0.09590 328 PHE A N   
2450 C CA  . PHE A 334 ? 0.23220 0.26910 0.40000 -0.00750 0.04680  -0.08930 328 PHE A CA  
2451 C C   . PHE A 334 ? 0.23250 0.26550 0.40650 -0.00230 0.04030  -0.08020 328 PHE A C   
2452 O O   . PHE A 334 ? 0.24710 0.27890 0.41980 -0.00260 0.03410  -0.07560 328 PHE A O   
2453 C CB  . PHE A 334 ? 0.22420 0.27060 0.39080 -0.00800 0.04650  -0.08600 328 PHE A CB  
2454 C CG  . PHE A 334 ? 0.24980 0.30210 0.40810 -0.01410 0.05260  -0.09310 328 PHE A CG  
2455 C CD1 . PHE A 334 ? 0.26870 0.32190 0.41520 -0.01970 0.04790  -0.09100 328 PHE A CD1 
2456 C CD2 . PHE A 334 ? 0.28130 0.33560 0.43750 -0.01540 0.06060  -0.09820 328 PHE A CD2 
2457 C CE1 . PHE A 334 ? 0.28800 0.34310 0.41870 -0.02660 0.05040  -0.09330 328 PHE A CE1 
2458 C CE2 . PHE A 334 ? 0.31090 0.37000 0.45570 -0.02190 0.06660  -0.10410 328 PHE A CE2 
2459 C CZ  . PHE A 334 ? 0.27010 0.32800 0.39940 -0.02800 0.06000  -0.10010 328 PHE A CZ  
2460 N N   . HIS A 335 ? 0.23840 0.26940 0.41780 0.00250  0.04200  -0.07730 329 HIS A N   
2461 C CA  . HIS A 335 ? 0.23200 0.26040 0.41450 0.00740  0.03640  -0.06830 329 HIS A CA  
2462 C C   . HIS A 335 ? 0.22260 0.24290 0.40530 0.00680  0.03450  -0.06750 329 HIS A C   
2463 O O   . HIS A 335 ? 0.22260 0.24150 0.40370 0.00770  0.02860  -0.06060 329 HIS A O   
2464 C CB  . HIS A 335 ? 0.22460 0.25410 0.41320 0.01310  0.03960  -0.06640 329 HIS A CB  
2465 C CG  . HIS A 335 ? 0.19240 0.22200 0.38280 0.01830  0.03420  -0.05730 329 HIS A CG  
2466 N ND1 . HIS A 335 ? 0.26990 0.30200 0.46650 0.02460  0.03600  -0.05430 329 HIS A ND1 
2467 C CD2 . HIS A 335 ? 0.19040 0.21830 0.37660 0.01850  0.02770  -0.05070 329 HIS A CD2 
2468 C CE1 . HIS A 335 ? 0.30130 0.33380 0.49700 0.02810  0.03050  -0.04650 329 HIS A CE1 
2469 N NE2 . HIS A 335 ? 0.19650 0.22600 0.38530 0.02430  0.02560  -0.04430 329 HIS A NE2 
2470 N N   . HIS A 336 ? 0.23210 0.24680 0.41530 0.00470  0.04000  -0.07460 330 HIS A N   
2471 C CA  . HIS A 336 ? 0.25130 0.25800 0.43500 0.00370  0.03940  -0.07470 330 HIS A CA  
2472 C C   . HIS A 336 ? 0.25800 0.26290 0.43550 -0.00280 0.04240  -0.08430 330 HIS A C   
2473 O O   . HIS A 336 ? 0.33610 0.33510 0.51050 -0.00470 0.04860  -0.09150 330 HIS A O   
2474 C CB  . HIS A 336 ? 0.22980 0.22860 0.41780 0.00830  0.04360  -0.07350 330 HIS A CB  
2475 C CG  . HIS A 336 ? 0.24200 0.24310 0.43370 0.01490  0.04030  -0.06430 330 HIS A CG  
2476 N ND1 . HIS A 336 ? 0.31540 0.32120 0.51030 0.01940  0.04270  -0.06350 330 HIS A ND1 
2477 C CD2 . HIS A 336 ? 0.22840 0.22880 0.41990 0.01760  0.03480  -0.05560 330 HIS A CD2 
2478 C CE1 . HIS A 336 ? 0.32580 0.33400 0.52230 0.02460  0.03830  -0.05500 330 HIS A CE1 
2479 N NE2 . HIS A 336 ? 0.26140 0.26590 0.45480 0.02340  0.03370  -0.05020 330 HIS A NE2 
2480 N N   . PRO A 337 ? 0.25490 0.26420 0.42830 -0.00660 0.03780  -0.08460 331 PRO A N   
2481 C CA  . PRO A 337 ? 0.26230 0.27000 0.42460 -0.01390 0.03900  -0.09300 331 PRO A CA  
2482 C C   . PRO A 337 ? 0.31920 0.31730 0.47770 -0.01690 0.04070  -0.09650 331 PRO A C   
2483 O O   . PRO A 337 ? 0.30880 0.30220 0.47380 -0.01400 0.03900  -0.09140 331 PRO A O   
2484 C CB  . PRO A 337 ? 0.28080 0.29330 0.43940 -0.01650 0.03120  -0.08870 331 PRO A CB  
2485 C CG  . PRO A 337 ? 0.29460 0.31240 0.46310 -0.01020 0.02850  -0.08100 331 PRO A CG  
2486 C CD  . PRO A 337 ? 0.25580 0.27080 0.43160 -0.00480 0.03090  -0.07660 331 PRO A CD  
2487 N N   . GLN A 338 ? 0.32060 0.31560 0.46720 -0.02350 0.04400  -0.10530 332 GLN A N   
2488 C CA  . GLN A 338 ? 0.38490 0.37040 0.52560 -0.02790 0.04560  -0.10990 332 GLN A CA  
2489 C C   . GLN A 338 ? 0.35180 0.33710 0.49070 -0.03140 0.03790  -0.10520 332 GLN A C   
2490 O O   . GLN A 338 ? 0.31220 0.30530 0.44660 -0.03420 0.03110  -0.10160 332 GLN A O   
2491 C CB  . GLN A 338 ? 0.45700 0.44080 0.58210 -0.03560 0.04920  -0.11980 332 GLN A CB  
2492 C CG  . GLN A 338 ? 0.56300 0.54550 0.68910 -0.03260 0.05830  -0.12500 332 GLN A CG  
2493 C CD  . GLN A 338 ? 0.68640 0.65690 0.80990 -0.03360 0.06500  -0.13140 332 GLN A CD  
2494 O OE1 . GLN A 338 ? 0.68100 0.64720 0.79000 -0.04140 0.06640  -0.13920 332 GLN A OE1 
2495 N NE2 . GLN A 338 ? 0.66110 0.62570 0.79770 -0.02610 0.06870  -0.12770 332 GLN A NE2 
2496 N N   . ARG A 339 ? 0.33300 0.30960 0.47550 -0.03120 0.03900  -0.10470 333 ARG A N   
2497 C CA  . ARG A 339 ? 0.33260 0.30840 0.47370 -0.03520 0.03280  -0.10090 333 ARG A CA  
2498 C C   . ARG A 339 ? 0.36840 0.33400 0.50240 -0.04170 0.03570  -0.10810 333 ARG A C   
2499 O O   . ARG A 339 ? 0.37620 0.33260 0.51650 -0.03980 0.03870  -0.10700 333 ARG A O   
2500 C CB  . ARG A 339 ? 0.31620 0.29200 0.47040 -0.02820 0.03110  -0.09150 333 ARG A CB  
2501 C CG  . ARG A 339 ? 0.29060 0.27700 0.44910 -0.02390 0.02600  -0.08400 333 ARG A CG  
2502 C CD  . ARG A 339 ? 0.32320 0.31690 0.47260 -0.03000 0.01870  -0.08240 333 ARG A CD  
2503 N NE  . ARG A 339 ? 0.37270 0.37480 0.52530 -0.02580 0.01390  -0.07460 333 ARG A NE  
2504 C CZ  . ARG A 339 ? 0.41030 0.41870 0.55980 -0.02500 0.01320  -0.07460 333 ARG A CZ  
2505 N NH1 . ARG A 339 ? 0.32770 0.33600 0.47190 -0.02770 0.01740  -0.08230 333 ARG A NH1 
2506 N NH2 . ARG A 339 ? 0.37650 0.39100 0.52780 -0.02160 0.00870  -0.06670 333 ARG A NH2 
2507 N N   . VAL A 340 ? 0.38370 0.35060 0.50370 -0.04980 0.03490  -0.11550 334 VAL A N   
2508 C CA  . VAL A 340 ? 0.40770 0.36480 0.51870 -0.05670 0.03810  -0.12410 334 VAL A CA  
2509 C C   . VAL A 340 ? 0.42220 0.38500 0.52080 -0.06710 0.03000  -0.12570 334 VAL A C   
2510 O O   . VAL A 340 ? 0.44470 0.41820 0.53540 -0.06990 0.02500  -0.12470 334 VAL A O   
2511 C CB  . VAL A 340 ? 0.41940 0.37170 0.52430 -0.05620 0.04670  -0.13280 334 VAL A CB  
2512 C CG1 . VAL A 340 ? 0.44480 0.38780 0.53730 -0.06470 0.04910  -0.14230 334 VAL A CG1 
2513 C CG2 . VAL A 340 ? 0.42550 0.37150 0.54400 -0.04630 0.05430  -0.13050 334 VAL A CG2 
2514 N N   . ASN A 341 ? 0.37390 0.33020 0.47110 -0.07300 0.02810  -0.12740 335 ASN A N   
2515 C CA  . ASN A 341 ? 0.37940 0.34370 0.46830 -0.08230 0.01870  -0.12660 335 ASN A CA  
2516 C C   . ASN A 341 ? 0.41820 0.38180 0.49010 -0.09090 0.01880  -0.13640 335 ASN A C   
2517 O O   . ASN A 341 ? 0.40880 0.36530 0.47530 -0.08940 0.02700  -0.14390 335 ASN A O   
2518 C CB  . ASN A 341 ? 0.40150 0.36140 0.49740 -0.08550 0.01580  -0.12340 335 ASN A CB  
2519 C CG  . ASN A 341 ? 0.42700 0.37120 0.52050 -0.08950 0.02210  -0.13170 335 ASN A CG  
2520 O OD1 . ASN A 341 ? 0.42020 0.35780 0.50420 -0.09190 0.02730  -0.14090 335 ASN A OD1 
2521 N ND2 . ASN A 341 ? 0.37290 0.31100 0.47480 -0.09050 0.02180  -0.12840 335 ASN A ND2 
2522 N N   . THR A 342 ? 0.39970 0.37140 0.46320 -0.09990 0.00970  -0.13620 336 THR A N   
2523 C CA  . THR A 342 ? 0.44200 0.41530 0.48790 -0.10870 0.00820  -0.14480 336 THR A CA  
2524 C C   . THR A 342 ? 0.45040 0.40830 0.48980 -0.11320 0.01570  -0.15610 336 THR A C   
2525 O O   . THR A 342 ? 0.48310 0.44080 0.50680 -0.12040 0.01570  -0.16420 336 THR A O   
2526 C CB  . THR A 342 ? 0.42290 0.40900 0.46420 -0.11700 -0.00420 -0.14100 336 THR A CB  
2527 O OG1 . THR A 342 ? 0.41650 0.39820 0.46650 -0.12060 -0.00700 -0.13960 336 THR A OG1 
2528 C CG2 . THR A 342 ? 0.37380 0.37500 0.42060 -0.11240 -0.01140 -0.12970 336 THR A CG2 
2529 N N   . MET A 343 ? 0.46880 0.41380 0.51930 -0.10940 0.02180  -0.15650 337 MET A N   
2530 C CA  . MET A 343 ? 0.42600 0.35480 0.47180 -0.11280 0.02980  -0.16670 337 MET A CA  
2531 C C   . MET A 343 ? 0.42510 0.34260 0.47850 -0.10280 0.04180  -0.16830 337 MET A C   
2532 O O   . MET A 343 ? 0.47250 0.37490 0.52770 -0.10270 0.04900  -0.17380 337 MET A O   
2533 C CB  . MET A 343 ? 0.49830 0.41990 0.55000 -0.11810 0.02700  -0.16640 337 MET A CB  
2534 C CG  . MET A 343 ? 0.50210 0.43470 0.54780 -0.12880 0.01530  -0.16550 337 MET A CG  
2535 S SD  . MET A 343 ? 0.53750 0.46980 0.56120 -0.13980 0.01440  -0.17830 337 MET A SD  
2536 C CE  . MET A 343 ? 0.52430 0.43400 0.54730 -0.14420 0.02340  -0.18900 337 MET A CE  
2537 N N   . GLY A 344 ? 0.44270 0.36760 0.50210 -0.09410 0.04360  -0.16280 338 GLY A N   
2538 C CA  . GLY A 344 ? 0.49290 0.41050 0.56050 -0.08440 0.05390  -0.16350 338 GLY A CA  
2539 C C   . GLY A 344 ? 0.50750 0.41800 0.59260 -0.07590 0.05690  -0.15660 338 GLY A C   
2540 O O   . GLY A 344 ? 0.46640 0.36910 0.55870 -0.06830 0.06560  -0.15740 338 GLY A O   
2541 N N   . VAL A 345 ? 0.48180 0.39550 0.57410 -0.07680 0.05010  -0.14910 339 VAL A N   
2542 C CA  . VAL A 345 ? 0.45040 0.35710 0.55780 -0.06960 0.05280  -0.14220 339 VAL A CA  
2543 C C   . VAL A 345 ? 0.40740 0.32520 0.52600 -0.06050 0.05000  -0.13180 339 VAL A C   
2544 O O   . VAL A 345 ? 0.36930 0.30020 0.48570 -0.06250 0.04250  -0.12770 339 VAL A O   
2545 C CB  . VAL A 345 ? 0.43820 0.34070 0.54620 -0.07680 0.04790  -0.14070 339 VAL A CB  
2546 C CG1 . VAL A 345 ? 0.41160 0.30730 0.53420 -0.06960 0.05060  -0.13260 339 VAL A CG1 
2547 C CG2 . VAL A 345 ? 0.42280 0.31390 0.51950 -0.08640 0.05040  -0.15170 339 VAL A CG2 
2548 N N   . THR A 346 ? 0.38180 0.29490 0.51230 -0.05070 0.05550  -0.12700 340 THR A N   
2549 C CA  . THR A 346 ? 0.39710 0.32050 0.53820 -0.04220 0.05270  -0.11730 340 THR A CA  
2550 C C   . THR A 346 ? 0.39600 0.32200 0.54370 -0.04220 0.04690  -0.10870 340 THR A C   
2551 O O   . THR A 346 ? 0.40570 0.32200 0.55900 -0.04100 0.04940  -0.10620 340 THR A O   
2552 C CB  . THR A 346 ? 0.45810 0.37710 0.60920 -0.03210 0.05940  -0.11430 340 THR A CB  
2553 O OG1 . THR A 346 ? 0.46210 0.38200 0.60800 -0.03160 0.06450  -0.12120 340 THR A OG1 
2554 C CG2 . THR A 346 ? 0.34400 0.27330 0.50600 -0.02410 0.05530  -0.10310 340 THR A CG2 
2555 N N   . THR A 347 ? 0.33060 0.26930 0.47790 -0.04330 0.03950  -0.10390 341 THR A N   
2556 C CA  . THR A 347 ? 0.30650 0.24840 0.45870 -0.04430 0.03410  -0.09640 341 THR A CA  
2557 C C   . THR A 347 ? 0.30900 0.25720 0.47240 -0.03500 0.03270  -0.08610 341 THR A C   
2558 O O   . THR A 347 ? 0.27290 0.22170 0.44170 -0.03440 0.03010  -0.07940 341 THR A O   
2559 C CB  . THR A 347 ? 0.31860 0.27050 0.46210 -0.05300 0.02610  -0.09730 341 THR A CB  
2560 O OG1 . THR A 347 ? 0.33810 0.30100 0.47820 -0.05080 0.02300  -0.09610 341 THR A OG1 
2561 C CG2 . THR A 347 ? 0.31100 0.25710 0.44280 -0.06300 0.02650  -0.10700 341 THR A CG2 
2562 N N   . GLY A 348 ? 0.29430 0.24720 0.46110 -0.02810 0.03430  -0.08450 342 GLY A N   
2563 C CA  . GLY A 348 ? 0.26300 0.22290 0.43870 -0.02060 0.03170  -0.07480 342 GLY A CA  
2564 C C   . GLY A 348 ? 0.26680 0.23180 0.44520 -0.01460 0.03350  -0.07420 342 GLY A C   
2565 O O   . GLY A 348 ? 0.26580 0.22680 0.44170 -0.01460 0.03840  -0.08040 342 GLY A O   
2566 N N   . GLY A 349 ? 0.26760 0.24130 0.45080 -0.00990 0.02940  -0.06660 343 GLY A N   
2567 C CA  . GLY A 349 ? 0.22810 0.20720 0.41370 -0.00510 0.03020  -0.06510 343 GLY A CA  
2568 C C   . GLY A 349 ? 0.23430 0.22310 0.42190 -0.00240 0.02440  -0.05760 343 GLY A C   
2569 O O   . GLY A 349 ? 0.21880 0.21100 0.40630 -0.00390 0.02020  -0.05430 343 GLY A O   
2570 N N   . VAL A 350 ? 0.20710 0.19940 0.39500 0.00130  0.02440  -0.05490 344 VAL A N   
2571 C CA  A VAL A 350 ? 0.18560 0.18460 0.37110 0.00300  0.01920  -0.04840 344 VAL A CA  
2572 C CA  B VAL A 350 ? 0.18550 0.18450 0.37110 0.00300  0.01920  -0.04830 344 VAL A CA  
2573 C C   . VAL A 350 ? 0.22260 0.21910 0.40640 0.00810  0.01860  -0.04070 344 VAL A C   
2574 O O   . VAL A 350 ? 0.24680 0.23950 0.43270 0.01130  0.02240  -0.04180 344 VAL A O   
2575 C CB  A VAL A 350 ? 0.21480 0.21990 0.39770 0.00190  0.01920  -0.05280 344 VAL A CB  
2576 C CB  B VAL A 350 ? 0.21480 0.21980 0.39770 0.00170  0.01920  -0.05300 344 VAL A CB  
2577 C CG1 A VAL A 350 ? 0.17740 0.18150 0.36100 0.00480  0.02370  -0.05530 344 VAL A CG1 
2578 C CG1 B VAL A 350 ? 0.20480 0.21390 0.38180 0.00320  0.01410  -0.04630 344 VAL A CG1 
2579 C CG2 A VAL A 350 ? 0.20620 0.21550 0.38330 0.00240  0.01360  -0.04660 344 VAL A CG2 
2580 C CG2 B VAL A 350 ? 0.20870 0.21600 0.39090 -0.00300 0.02010  -0.06110 344 VAL A CG2 
2581 N N   . SER A 351 ? 0.18440 0.18250 0.36330 0.00920  0.01400  -0.03330 345 SER A N   
2582 C CA  . SER A 351 ? 0.23090 0.22780 0.40610 0.01420  0.01290  -0.02630 345 SER A CA  
2583 C C   . SER A 351 ? 0.24470 0.24690 0.41140 0.01480  0.00850  -0.02230 345 SER A C   
2584 O O   . SER A 351 ? 0.19050 0.19480 0.35330 0.01140  0.00600  -0.02260 345 SER A O   
2585 C CB  . SER A 351 ? 0.22420 0.21610 0.39980 0.01530  0.01300  -0.02100 345 SER A CB  
2586 O OG  . SER A 351 ? 0.41520 0.40040 0.59750 0.01560  0.01770  -0.02420 345 SER A OG  
2587 N N   . PHE A 352 ? 0.21240 0.21630 0.37640 0.01950  0.00760  -0.01830 346 PHE A N   
2588 C CA  . PHE A 352 ? 0.21100 0.22030 0.36780 0.02050  0.00400  -0.01530 346 PHE A CA  
2589 C C   . PHE A 352 ? 0.22720 0.23630 0.37960 0.02450  0.00190  -0.00880 346 PHE A C   
2590 O O   . PHE A 352 ? 0.24370 0.25670 0.39640 0.02910  0.00090  -0.00650 346 PHE A O   
2591 C CB  . PHE A 352 ? 0.17490 0.18960 0.33480 0.02250  0.00490  -0.01810 346 PHE A CB  
2592 C CG  . PHE A 352 ? 0.16790 0.18300 0.33250 0.01920  0.00800  -0.02510 346 PHE A CG  
2593 C CD1 . PHE A 352 ? 0.17220 0.18940 0.33300 0.01490  0.00670  -0.02790 346 PHE A CD1 
2594 C CD2 . PHE A 352 ? 0.21320 0.22620 0.38560 0.02070  0.01270  -0.02920 346 PHE A CD2 
2595 C CE1 . PHE A 352 ? 0.16470 0.18310 0.32960 0.01200  0.01000  -0.03510 346 PHE A CE1 
2596 C CE2 . PHE A 352 ? 0.18010 0.19400 0.35630 0.01750  0.01630  -0.03680 346 PHE A CE2 
2597 C CZ  . PHE A 352 ? 0.13620 0.15330 0.30870 0.01310  0.01490  -0.03980 346 PHE A CZ  
2598 N N   . PRO A 353 ? 0.19760 0.20310 0.34640 0.02310  0.00120  -0.00570 347 PRO A N   
2599 C CA  . PRO A 353 ? 0.26530 0.26990 0.41020 0.02720  -0.00010 0.00010  347 PRO A CA  
2600 C C   . PRO A 353 ? 0.32440 0.33420 0.46160 0.02850  -0.00360 0.00250  347 PRO A C   
2601 O O   . PRO A 353 ? 0.36700 0.37560 0.49880 0.02900  -0.00480 0.00600  347 PRO A O   
2602 C CB  . PRO A 353 ? 0.26180 0.26120 0.40660 0.02450  0.00120  0.00180  347 PRO A CB  
2603 C CG  . PRO A 353 ? 0.20680 0.20770 0.35140 0.01900  0.00080  -0.00210 347 PRO A CG  
2604 C CD  . PRO A 353 ? 0.17360 0.17640 0.32300 0.01810  0.00180  -0.00750 347 PRO A CD  
2605 N N   . PHE A 354 ? 0.30490 0.32060 0.44270 0.02880  -0.00490 0.00030  348 PHE A N   
2606 C CA  . PHE A 354 ? 0.34980 0.37100 0.48260 0.02980  -0.00820 0.00210  348 PHE A CA  
2607 C C   . PHE A 354 ? 0.36020 0.38900 0.49780 0.03460  -0.00990 0.00320  348 PHE A C   
2608 O O   . PHE A 354 ? 0.32650 0.35630 0.47090 0.03690  -0.00800 0.00200  348 PHE A O   
2609 C CB  . PHE A 354 ? 0.29670 0.31950 0.42650 0.02510  -0.00870 -0.00140 348 PHE A CB  
2610 C CG  . PHE A 354 ? 0.29040 0.31520 0.42550 0.02310  -0.00710 -0.00590 348 PHE A CG  
2611 C CD1 . PHE A 354 ? 0.28190 0.31390 0.42230 0.02540  -0.00750 -0.00690 348 PHE A CD1 
2612 C CD2 . PHE A 354 ? 0.26320 0.28370 0.39890 0.01920  -0.00510 -0.00940 348 PHE A CD2 
2613 C CE1 . PHE A 354 ? 0.27800 0.31220 0.42350 0.02380  -0.00530 -0.01140 348 PHE A CE1 
2614 C CE2 . PHE A 354 ? 0.23090 0.25350 0.37140 0.01760  -0.00330 -0.01410 348 PHE A CE2 
2615 C CZ  . PHE A 354 ? 0.21780 0.24680 0.36300 0.01990  -0.00300 -0.01510 348 PHE A CZ  
2616 N N   . LYS A 355 ? 0.33000 0.36480 0.46470 0.03600  -0.01340 0.00530  349 LYS A N   
2617 C CA  . LYS A 355 ? 0.25260 0.29760 0.39270 0.04030  -0.01620 0.00690  349 LYS A CA  
2618 C C   . LYS A 355 ? 0.26390 0.31670 0.40390 0.03700  -0.01880 0.00470  349 LYS A C   
2619 O O   . LYS A 355 ? 0.23300 0.28360 0.36720 0.03410  -0.02030 0.00460  349 LYS A O   
2620 C CB  . LYS A 355 ? 0.34220 0.38860 0.48050 0.04600  -0.01930 0.01240  349 LYS A CB  
2621 C CG  . LYS A 355 ? 0.39660 0.43460 0.53540 0.04990  -0.01690 0.01540  349 LYS A CG  
2622 C CD  . LYS A 355 ? 0.44180 0.47990 0.57640 0.05470  -0.02050 0.02110  349 LYS A CD  
2623 C CE  . LYS A 355 ? 0.49320 0.52790 0.63140 0.06120  -0.02010 0.02530  349 LYS A CE  
2624 N NZ  . LYS A 355 ? 0.54150 0.57560 0.67440 0.06540  -0.02410 0.03130  349 LYS A NZ  
2625 N N   . LEU A 356 ? 0.24690 0.30900 0.39420 0.03720  -0.01920 0.00280  350 LEU A N   
2626 C CA  . LEU A 356 ? 0.25750 0.32850 0.40620 0.03360  -0.02200 0.00090  350 LEU A CA  
2627 C C   . LEU A 356 ? 0.25210 0.33100 0.40020 0.03600  -0.02760 0.00460  350 LEU A C   
2628 O O   . LEU A 356 ? 0.29180 0.37680 0.44360 0.04160  -0.02980 0.00830  350 LEU A O   
2629 C CB  . LEU A 356 ? 0.24430 0.32560 0.40220 0.03350  -0.02100 -0.00140 350 LEU A CB  
2630 C CG  . LEU A 356 ? 0.34250 0.41960 0.50140 0.02930  -0.01660 -0.00620 350 LEU A CG  
2631 C CD1 . LEU A 356 ? 0.24810 0.33680 0.41730 0.03000  -0.01530 -0.00790 350 LEU A CD1 
2632 C CD2 . LEU A 356 ? 0.26460 0.33840 0.41750 0.02340  -0.01740 -0.00860 350 LEU A CD2 
2633 N N   . ARG A 357 ? 0.27880 0.35790 0.42280 0.03210  -0.03050 0.00360  351 ARG A N   
2634 C CA  . ARG A 357 ? 0.32370 0.41200 0.46790 0.03370  -0.03690 0.00670  351 ARG A CA  
2635 C C   . ARG A 357 ? 0.34980 0.45240 0.50040 0.02950  -0.04070 0.00410  351 ARG A C   
2636 O O   . ARG A 357 ? 0.32070 0.42220 0.47250 0.02400  -0.03820 -0.00030 351 ARG A O   
2637 C CB  . ARG A 357 ? 0.37230 0.45240 0.50830 0.03260  -0.03870 0.00760  351 ARG A CB  
2638 C CG  . ARG A 357 ? 0.34980 0.42670 0.48380 0.02630  -0.03900 0.00310  351 ARG A CG  
2639 C CD  . ARG A 357 ? 0.44890 0.51600 0.57570 0.02680  -0.03950 0.00440  351 ARG A CD  
2640 N NE  . ARG A 357 ? 0.49260 0.55730 0.61880 0.02140  -0.04070 -0.00040 351 ARG A NE  
2641 C CZ  . ARG A 357 ? 0.49090 0.54600 0.61520 0.01920  -0.03560 -0.00290 351 ARG A CZ  
2642 N NH1 . ARG A 357 ? 0.34680 0.39370 0.46800 0.02090  -0.02960 -0.00150 351 ARG A NH1 
2643 N NH2 . ARG A 357 ? 0.39320 0.44730 0.51840 0.01470  -0.03710 -0.00730 351 ARG A NH2 
2644 N N   . GLY A 358 ? 0.36100 0.47770 0.51580 0.03200  -0.04650 0.00710  352 GLY A N   
2645 C CA  . GLY A 358 ? 0.39260 0.52540 0.55340 0.02720  -0.05120 0.00520  352 GLY A CA  
2646 C C   . GLY A 358 ? 0.45060 0.58800 0.60600 0.02330  -0.05910 0.00520  352 GLY A C   
2647 O O   . GLY A 358 ? 0.60030 0.75000 0.75840 0.01680  -0.06380 0.00270  352 GLY A O   
2648 N N   . ASP B 3   ? 0.87210 0.77640 0.80020 -0.11670 0.10740  -0.16310 -3  ASP B N   
2649 C CA  . ASP B 3   ? 0.94430 0.84060 0.86110 -0.11630 0.12330  -0.16690 -3  ASP B CA  
2650 C C   . ASP B 3   ? 0.88100 0.77960 0.81400 -0.09930 0.12550  -0.15620 -3  ASP B C   
2651 O O   . ASP B 3   ? 0.81130 0.72840 0.73880 -0.09610 0.10730  -0.14440 -3  ASP B O   
2652 C CB  . ASP B 3   ? 0.89760 0.80420 0.77460 -0.13410 0.11550  -0.17250 -3  ASP B CB  
2653 C CG  . ASP B 3   ? 0.92790 0.82620 0.79140 -0.13540 0.13270  -0.17660 -3  ASP B CG  
2654 O OD1 . ASP B 3   ? 0.92520 0.80670 0.80900 -0.12740 0.15410  -0.17990 -3  ASP B OD1 
2655 O OD2 . ASP B 3   ? 0.94080 0.85060 0.77510 -0.14440 0.12420  -0.17470 -3  ASP B OD2 
2656 N N   . PRO B 4   ? 0.89560 0.78160 0.85390 -0.08670 0.14450  -0.15350 -2  PRO B N   
2657 C CA  . PRO B 4   ? 0.85360 0.74470 0.83310 -0.06960 0.14670  -0.14120 -2  PRO B CA  
2658 C C   . PRO B 4   ? 0.85060 0.74720 0.81020 -0.07250 0.15170  -0.14190 -2  PRO B C   
2659 O O   . PRO B 4   ? 0.85970 0.76690 0.83760 -0.05920 0.14890  -0.12690 -2  PRO B O   
2660 C CB  . PRO B 4   ? 0.75520 0.63470 0.77080 -0.05720 0.16280  -0.13530 -2  PRO B CB  
2661 C CG  . PRO B 4   ? 0.74810 0.61280 0.74940 -0.07070 0.17770  -0.14940 -2  PRO B CG  
2662 C CD  . PRO B 4   ? 0.85170 0.72040 0.82230 -0.08800 0.16450  -0.16000 -2  PRO B CD  
2663 N N   . PHE B 5   ? 0.82790 0.72210 0.75380 -0.08930 0.15480  -0.15270 -1  PHE B N   
2664 C CA  . PHE B 5   ? 0.85830 0.75690 0.76280 -0.09370 0.16030  -0.15250 -1  PHE B CA  
2665 C C   . PHE B 5   ? 0.82840 0.74550 0.70180 -0.10230 0.13880  -0.14630 -1  PHE B C   
2666 O O   . PHE B 5   ? 0.78650 0.70830 0.63570 -0.10890 0.14140  -0.14520 -1  PHE B O   
2667 C CB  . PHE B 5   ? 0.86830 0.75350 0.75640 -0.10680 0.17680  -0.16520 -1  PHE B CB  
2668 C CG  . PHE B 5   ? 0.83590 0.70420 0.75730 -0.09760 0.19780  -0.16740 -1  PHE B CG  
2669 C CD1 . PHE B 5   ? 0.83290 0.70090 0.78310 -0.08230 0.20890  -0.15790 -1  PHE B CD1 
2670 C CD2 . PHE B 5   ? 0.86830 0.72280 0.79440 -0.10430 0.20570  -0.17710 -1  PHE B CD2 
2671 C CE1 . PHE B 5   ? 0.75710 0.61170 0.74000 -0.07370 0.22620  -0.15700 -1  PHE B CE1 
2672 C CE2 . PHE B 5   ? 0.78110 0.62030 0.73860 -0.09600 0.22510  -0.17720 -1  PHE B CE2 
2673 C CZ  . PHE B 5   ? 0.71510 0.55450 0.70120 -0.08060 0.23480  -0.16660 -1  PHE B CZ  
2674 N N   . THR B 6   ? 0.81000 0.74040 0.68930 -0.10090 0.11520  -0.13670 0   THR B N   
2675 C CA  . THR B 6   ? 0.77810 0.73000 0.64260 -0.10370 0.09020  -0.12210 0   THR B CA  
2676 C C   . THR B 6   ? 0.75060 0.71480 0.64700 -0.08790 0.07280  -0.10470 0   THR B C   
2677 O O   . THR B 6   ? 0.67230 0.65180 0.56410 -0.09060 0.05170  -0.09600 0   THR B O   
2678 C CB  . THR B 6   ? 0.77060 0.72930 0.60140 -0.12400 0.07760  -0.13030 0   THR B CB  
2679 O OG1 . THR B 6   ? 0.73620 0.69210 0.58070 -0.12610 0.07280  -0.13690 0   THR B OG1 
2680 C CG2 . THR B 6   ? 0.79580 0.74300 0.59070 -0.14200 0.09380  -0.14750 0   THR B CG2 
2681 N N   . MET B 7   ? 0.68680 0.64530 0.61600 -0.07210 0.08170  -0.09940 1   MET B N   
2682 C CA  . MET B 7   ? 0.63760 0.60690 0.59380 -0.05850 0.06680  -0.08390 1   MET B CA  
2683 C C   . MET B 7   ? 0.63430 0.61780 0.58750 -0.05380 0.05420  -0.06860 1   MET B C   
2684 O O   . MET B 7   ? 0.63190 0.61460 0.57430 -0.05540 0.06200  -0.06750 1   MET B O   
2685 C CB  . MET B 7   ? 0.64940 0.61040 0.63900 -0.04460 0.07880  -0.08120 1   MET B CB  
2686 C CG  . MET B 7   ? 0.67830 0.62410 0.67810 -0.04630 0.09020  -0.09270 1   MET B CG  
2687 S SD  . MET B 7   ? 0.67940 0.62950 0.67180 -0.05550 0.07430  -0.09650 1   MET B SD  
2688 C CE  . MET B 7   ? 0.51690 0.48300 0.53420 -0.04120 0.05590  -0.07700 1   MET B CE  
2689 N N   . THR B 8   ? 0.52430 0.51970 0.48770 -0.04830 0.03620  -0.05700 2   THR B N   
2690 C CA  . THR B 8   ? 0.52470 0.53170 0.48420 -0.04550 0.02340  -0.04300 2   THR B CA  
2691 C C   . THR B 8   ? 0.46890 0.48110 0.45530 -0.03230 0.01580  -0.03160 2   THR B C   
2692 O O   . THR B 8   ? 0.44950 0.46020 0.45320 -0.02730 0.01500  -0.03310 2   THR B O   
2693 C CB  . THR B 8   ? 0.55790 0.57590 0.49740 -0.05510 0.00740  -0.04010 2   THR B CB  
2694 O OG1 . THR B 8   ? 0.49940 0.52270 0.45270 -0.05340 -0.00260 -0.04020 2   THR B OG1 
2695 C CG2 . THR B 8   ? 0.49060 0.50490 0.39780 -0.07150 0.01350  -0.05210 2   THR B CG2 
2696 N N   . PRO B 9   ? 0.44900 0.46640 0.43800 -0.02770 0.01070  -0.02020 3   PRO B N   
2697 C CA  . PRO B 9   ? 0.37750 0.39930 0.38800 -0.01770 0.00290  -0.01080 3   PRO B CA  
2698 C C   . PRO B 9   ? 0.39700 0.42380 0.41490 -0.01600 -0.00840 -0.00960 3   PRO B C   
2699 O O   . PRO B 9   ? 0.36680 0.39370 0.40260 -0.00920 -0.00950 -0.00770 3   PRO B O   
2700 C CB  . PRO B 9   ? 0.39320 0.41860 0.39780 -0.01740 -0.00230 -0.00030 3   PRO B CB  
2701 C CG  . PRO B 9   ? 0.45940 0.48090 0.44800 -0.02360 0.00900  -0.00390 3   PRO B CG  
2702 C CD  . PRO B 9   ? 0.46880 0.48680 0.44100 -0.03220 0.01390  -0.01610 3   PRO B CD  
2703 N N   . SER B 10  ? 0.41090 0.44360 0.41580 -0.02270 -0.01710 -0.00990 4   SER B N   
2704 C CA  . SER B 10  ? 0.38780 0.42790 0.40310 -0.02130 -0.02730 -0.00800 4   SER B CA  
2705 C C   . SER B 10  ? 0.37930 0.41470 0.40400 -0.02160 -0.02160 -0.01740 4   SER B C   
2706 O O   . SER B 10  ? 0.38130 0.42240 0.41730 -0.02010 -0.02790 -0.01630 4   SER B O   
2707 C CB  . SER B 10  ? 0.41750 0.46830 0.41860 -0.02950 -0.03860 -0.00500 4   SER B CB  
2708 O OG  . SER B 10  ? 0.41390 0.46210 0.39460 -0.04140 -0.03370 -0.01590 4   SER B OG  
2709 N N   . GLU B 11  ? 0.34940 0.37440 0.37160 -0.02340 -0.00870 -0.02590 5   GLU B N   
2710 C CA  . GLU B 11  ? 0.39610 0.41370 0.42870 -0.02320 -0.00130 -0.03340 5   GLU B CA  
2711 C C   . GLU B 11  ? 0.30010 0.31300 0.35200 -0.01290 0.00500  -0.02870 5   GLU B C   
2712 O O   . GLU B 11  ? 0.26620 0.27100 0.32800 -0.01150 0.01370  -0.03280 5   GLU B O   
2713 C CB  . GLU B 11  ? 0.38680 0.39430 0.40530 -0.03280 0.01000  -0.04660 5   GLU B CB  
2714 C CG  . GLU B 11  ? 0.44560 0.46000 0.44360 -0.04610 0.00170  -0.05210 5   GLU B CG  
2715 C CD  . GLU B 11  ? 0.56630 0.57080 0.54130 -0.05850 0.01290  -0.06580 5   GLU B CD  
2716 O OE1 . GLU B 11  ? 0.57420 0.57530 0.53700 -0.05900 0.01990  -0.06560 5   GLU B OE1 
2717 O OE2 . GLU B 11  ? 0.62710 0.62720 0.59540 -0.06910 0.01550  -0.07750 5   GLU B OE2 
2718 N N   . ASP B 12  ? 0.26710 0.28520 0.32510 -0.00640 0.00030  -0.01940 6   ASP B N   
2719 C CA  . ASP B 12  ? 0.24500 0.26180 0.31940 0.00130  0.00430  -0.01400 6   ASP B CA  
2720 C C   . ASP B 12  ? 0.23170 0.25220 0.31620 0.00470  -0.00220 -0.01030 6   ASP B C   
2721 O O   . ASP B 12  ? 0.19060 0.21680 0.27550 0.00650  -0.01020 -0.00550 6   ASP B O   
2722 C CB  . ASP B 12  ? 0.20640 0.22700 0.28110 0.00400  0.00330  -0.00750 6   ASP B CB  
2723 C CG  . ASP B 12  ? 0.25020 0.26660 0.31960 0.00180  0.01410  -0.01080 6   ASP B CG  
2724 O OD1 . ASP B 12  ? 0.26640 0.27540 0.33840 0.00080  0.02510  -0.01770 6   ASP B OD1 
2725 O OD2 . ASP B 12  ? 0.23470 0.25390 0.29800 0.00080  0.01310  -0.00690 6   ASP B OD2 
2726 N N   . PHE B 13  ? 0.19680 0.21240 0.28940 0.00520  0.00270  -0.01270 7   PHE B N   
2727 C CA  . PHE B 13  ? 0.20550 0.22390 0.30520 0.00660  -0.00180 -0.01010 7   PHE B CA  
2728 C C   . PHE B 13  ? 0.18120 0.19670 0.29340 0.01140  0.00310  -0.00450 7   PHE B C   
2729 O O   . PHE B 13  ? 0.20180 0.21130 0.32080 0.01340  0.01150  -0.00420 7   PHE B O   
2730 C CB  . PHE B 13  ? 0.20160 0.21830 0.29920 0.00080  -0.00170 -0.01700 7   PHE B CB  
2731 C CG  . PHE B 13  ? 0.21410 0.23830 0.30230 -0.00430 -0.00970 -0.01980 7   PHE B CG  
2732 C CD1 . PHE B 13  ? 0.21930 0.25270 0.31230 -0.00270 -0.01790 -0.01570 7   PHE B CD1 
2733 C CD2 . PHE B 13  ? 0.29670 0.31940 0.37180 -0.01130 -0.00860 -0.02620 7   PHE B CD2 
2734 C CE1 . PHE B 13  ? 0.28990 0.33260 0.37890 -0.00650 -0.02610 -0.01570 7   PHE B CE1 
2735 C CE2 . PHE B 13  ? 0.35160 0.38430 0.41810 -0.01690 -0.01830 -0.02630 7   PHE B CE2 
2736 C CZ  . PHE B 13  ? 0.32800 0.37160 0.40370 -0.01370 -0.02760 -0.01990 7   PHE B CZ  
2737 N N   . VAL B 14  ? 0.17480 0.19470 0.29060 0.01290  -0.00170 0.00040  8   VAL B N   
2738 C CA  . VAL B 14  ? 0.16910 0.18680 0.29420 0.01540  0.00170  0.00660  8   VAL B CA  
2739 C C   . VAL B 14  ? 0.15380 0.16990 0.27860 0.01200  0.00180  0.00340  8   VAL B C   
2740 O O   . VAL B 14  ? 0.15560 0.17740 0.27580 0.01000  -0.00350 0.00090  8   VAL B O   
2741 C CB  . VAL B 14  ? 0.15900 0.18450 0.28620 0.01820  -0.00340 0.01590  8   VAL B CB  
2742 C CG1 . VAL B 14  ? 0.17020 0.20120 0.28840 0.01600  -0.01030 0.01420  8   VAL B CG1 
2743 C CG2 . VAL B 14  ? 0.18130 0.20640 0.31700 0.02020  -0.00120 0.02510  8   VAL B CG2 
2744 N N   . VAL B 15  ? 0.16220 0.17020 0.29430 0.01150  0.00890  0.00370  9   VAL B N   
2745 C CA  . VAL B 15  ? 0.16110 0.16590 0.29430 0.00640  0.01100  -0.00120 9   VAL B CA  
2746 C C   . VAL B 15  ? 0.17590 0.17670 0.31690 0.00800  0.01520  0.00750  9   VAL B C   
2747 O O   . VAL B 15  ? 0.19560 0.19080 0.34460 0.01240  0.01990  0.01510  9   VAL B O   
2748 C CB  . VAL B 15  ? 0.20510 0.20060 0.33750 0.00120  0.01740  -0.01150 9   VAL B CB  
2749 C CG1 . VAL B 15  ? 0.22220 0.21360 0.35800 -0.00560 0.02050  -0.01670 9   VAL B CG1 
2750 C CG2 . VAL B 15  ? 0.19090 0.19200 0.31190 -0.00180 0.01200  -0.01850 9   VAL B CG2 
2751 N N   . THR B 16  ? 0.18270 0.18700 0.32290 0.00470  0.01400  0.00780  10  THR B N   
2752 C CA  . THR B 16  ? 0.16950 0.16860 0.31540 0.00440  0.01920  0.01580  10  THR B CA  
2753 C C   . THR B 16  ? 0.21230 0.20330 0.36410 -0.00190 0.02580  0.00860  10  THR B C   
2754 O O   . THR B 16  ? 0.20880 0.20470 0.35870 -0.00730 0.02330  -0.00160 10  THR B O   
2755 C CB  . THR B 16  ? 0.16510 0.17310 0.30460 0.00370  0.01550  0.02180  10  THR B CB  
2756 O OG1 . THR B 16  ? 0.20500 0.21990 0.34200 0.00000  0.01330  0.01310  10  THR B OG1 
2757 C CG2 . THR B 16  ? 0.22920 0.24480 0.36130 0.00740  0.00890  0.02790  10  THR B CG2 
2758 N N   . ASP B 17  ? 0.17970 0.15930 0.34000 -0.00180 0.03390  0.01490  11  ASP B N   
2759 C CA  . ASP B 17  ? 0.20990 0.17930 0.37670 -0.00910 0.04160  0.00790  11  ASP B CA  
2760 C C   . ASP B 17  ? 0.19280 0.15870 0.36470 -0.01070 0.04660  0.01800  11  ASP B C   
2761 O O   . ASP B 17  ? 0.22190 0.18950 0.39270 -0.00550 0.04560  0.03220  11  ASP B O   
2762 C CB  . ASP B 17  ? 0.21780 0.16980 0.39180 -0.00960 0.05110  0.00240  11  ASP B CB  
2763 C CG  . ASP B 17  ? 0.28260 0.22290 0.46860 -0.00130 0.05860  0.01690  11  ASP B CG  
2764 O OD1 . ASP B 17  ? 0.28900 0.23510 0.47560 0.00680  0.05470  0.02490  11  ASP B OD1 
2765 O OD2 . ASP B 17  ? 0.26750 0.19360 0.46400 -0.00300 0.06810  0.02170  11  ASP B OD2 
2766 N N   . ARG B 18  ? 0.20910 0.16990 0.38640 -0.01910 0.05210  0.01100  12  ARG B N   
2767 C CA  . ARG B 18  ? 0.22710 0.18060 0.41100 -0.02230 0.05980  0.01970  12  ARG B CA  
2768 C C   . ARG B 18  ? 0.25760 0.19110 0.45270 -0.02780 0.07080  0.01340  12  ARG B C   
2769 O O   . ARG B 18  ? 0.27140 0.20470 0.46760 -0.03710 0.07160  -0.00160 12  ARG B O   
2770 C CB  . ARG B 18  ? 0.21940 0.18710 0.40090 -0.02860 0.05730  0.01670  12  ARG B CB  
2771 C CG  . ARG B 18  ? 0.25770 0.22040 0.44310 -0.03250 0.06550  0.02680  12  ARG B CG  
2772 C CD  . ARG B 18  ? 0.20280 0.18210 0.38550 -0.03720 0.06390  0.02380  12  ARG B CD  
2773 N NE  . ARG B 18  ? 0.24580 0.23750 0.41550 -0.03080 0.05650  0.02710  12  ARG B NE  
2774 C CZ  . ARG B 18  ? 0.29720 0.29060 0.45560 -0.02870 0.05740  0.03910  12  ARG B CZ  
2775 N NH1 . ARG B 18  ? 0.23870 0.22370 0.39710 -0.03160 0.06490  0.05100  12  ARG B NH1 
2776 N NH2 . ARG B 18  ? 0.24560 0.24900 0.39120 -0.02450 0.05050  0.03930  12  ARG B NH2 
2777 N N   . GLY B 19  ? 0.28160 0.19960 0.48430 -0.02180 0.07870  0.02430  13  GLY B N   
2778 C CA  . GLY B 19  ? 0.28370 0.18640 0.49120 -0.02420 0.08880  0.01650  13  GLY B CA  
2779 C C   . GLY B 19  ? 0.28380 0.18230 0.48750 -0.02760 0.09000  -0.00110 13  GLY B C   
2780 O O   . GLY B 19  ? 0.31260 0.20200 0.51560 -0.03560 0.09670  -0.01380 13  GLY B O   
2781 N N   . GLY B 20  ? 0.28960 0.19460 0.48920 -0.02270 0.08380  -0.00240 14  GLY B N   
2782 C CA  . GLY B 20  ? 0.26670 0.16880 0.45930 -0.02680 0.08470  -0.01850 14  GLY B CA  
2783 C C   . GLY B 20  ? 0.30570 0.22020 0.48920 -0.03780 0.07540  -0.03200 14  GLY B C   
2784 O O   . GLY B 20  ? 0.31560 0.23060 0.48990 -0.04180 0.07370  -0.04420 14  GLY B O   
2785 N N   . ILE B 21  ? 0.22650 0.15440 0.41130 -0.04260 0.06890  -0.02940 15  ILE B N   
2786 C CA  . ILE B 21  ? 0.22220 0.17030 0.39980 -0.04990 0.05740  -0.03850 15  ILE B CA  
2787 C C   . ILE B 21  ? 0.21970 0.18560 0.39000 -0.04010 0.04590  -0.03110 15  ILE B C   
2788 O O   . ILE B 21  ? 0.17850 0.14810 0.35060 -0.03230 0.04510  -0.01870 15  ILE B O   
2789 C CB  . ILE B 21  ? 0.20510 0.16070 0.39160 -0.05860 0.05760  -0.03880 15  ILE B CB  
2790 C CG1 . ILE B 21  ? 0.23950 0.17760 0.42790 -0.06530 0.06850  -0.04380 15  ILE B CG1 
2791 C CG2 . ILE B 21  ? 0.20230 0.18140 0.38650 -0.06480 0.04530  -0.04590 15  ILE B CG2 
2792 C CD1 . ILE B 21  ? 0.22700 0.16780 0.42360 -0.06920 0.07190  -0.03790 15  ILE B CD1 
2793 N N   . VAL B 22  ? 0.21810 0.19470 0.37890 -0.04160 0.03720  -0.03840 16  VAL B N   
2794 C CA  . VAL B 22  ? 0.20840 0.19920 0.36310 -0.03260 0.02760  -0.03180 16  VAL B CA  
2795 C C   . VAL B 22  ? 0.18990 0.19580 0.35000 -0.03120 0.02250  -0.02600 16  VAL B C   
2796 O O   . VAL B 22  ? 0.17360 0.18980 0.34040 -0.03860 0.02000  -0.03060 16  VAL B O   
2797 C CB  . VAL B 22  ? 0.21220 0.21120 0.35610 -0.03520 0.01950  -0.03940 16  VAL B CB  
2798 C CG1 . VAL B 22  ? 0.17820 0.19190 0.31900 -0.02720 0.00980  -0.03230 16  VAL B CG1 
2799 C CG2 . VAL B 22  ? 0.21380 0.19790 0.35030 -0.03410 0.02630  -0.04380 16  VAL B CG2 
2800 N N   . GLU B 23  ? 0.15600 0.16420 0.31370 -0.02250 0.02150  -0.01620 17  GLU B N   
2801 C CA  . GLU B 23  ? 0.16740 0.18730 0.32770 -0.02090 0.01940  -0.01170 17  GLU B CA  
2802 C C   . GLU B 23  ? 0.15790 0.19020 0.31410 -0.01670 0.01040  -0.01320 17  GLU B C   
2803 O O   . GLU B 23  ? 0.12350 0.16850 0.28640 -0.01940 0.00570  -0.01720 17  GLU B O   
2804 C CB  . GLU B 23  ? 0.17270 0.18670 0.32960 -0.01630 0.02420  -0.00080 17  GLU B CB  
2805 C CG  . GLU B 23  ? 0.24410 0.26800 0.40010 -0.01620 0.02500  0.00240  17  GLU B CG  
2806 C CD  . GLU B 23  ? 0.21990 0.24240 0.38380 -0.02250 0.03320  0.00380  17  GLU B CD  
2807 O OE1 . GLU B 23  ? 0.24030 0.25190 0.40230 -0.02300 0.03900  0.01200  17  GLU B OE1 
2808 O OE2 . GLU B 23  ? 0.20900 0.24210 0.38310 -0.02700 0.03410  -0.00190 17  GLU B OE2 
2809 N N   . ASN B 24  ? 0.15580 0.18510 0.30310 -0.01010 0.00810  -0.00880 18  ASN B N   
2810 C CA  . ASN B 24  ? 0.16080 0.19810 0.30370 -0.00570 0.00100  -0.00910 18  ASN B CA  
2811 C C   . ASN B 24  ? 0.17170 0.20370 0.30710 -0.00370 -0.00170 -0.01000 18  ASN B C   
2812 O O   . ASN B 24  ? 0.16520 0.18750 0.29910 -0.00250 0.00290  -0.00760 18  ASN B O   
2813 C CB  . ASN B 24  ? 0.14330 0.18180 0.28110 -0.00120 0.00150  -0.00370 18  ASN B CB  
2814 C CG  . ASN B 24  ? 0.17610 0.21850 0.31850 -0.00340 0.00660  -0.00300 18  ASN B CG  
2815 O OD1 . ASN B 24  ? 0.16400 0.21390 0.31720 -0.00610 0.00730  -0.00690 18  ASN B OD1 
2816 N ND2 . ASN B 24  ? 0.18530 0.22420 0.31950 -0.00300 0.01030  0.00240  18  ASN B ND2 
2817 N N   . SER B 25  ? 0.14070 0.17910 0.27260 -0.00240 -0.00830 -0.01170 19  SER B N   
2818 C CA  . SER B 25  ? 0.13560 0.16940 0.25930 0.00020  -0.00970 -0.01110 19  SER B CA  
2819 C C   . SER B 25  ? 0.15050 0.19000 0.27110 0.00440  -0.01530 -0.00800 19  SER B C   
2820 O O   . SER B 25  ? 0.14580 0.19290 0.27120 0.00500  -0.01890 -0.00790 19  SER B O   
2821 C CB  . SER B 25  ? 0.18340 0.21530 0.30210 -0.00520 -0.01010 -0.01760 19  SER B CB  
2822 O OG  . SER B 25  ? 0.19980 0.24310 0.31900 -0.00870 -0.01780 -0.01950 19  SER B OG  
2823 N N   . HIS B 26  ? 0.14750 0.18290 0.26250 0.00740  -0.01510 -0.00510 20  HIS B N   
2824 C CA  . HIS B 26  ? 0.13890 0.17650 0.25090 0.01070  -0.01860 -0.00180 20  HIS B CA  
2825 C C   . HIS B 26  ? 0.12260 0.15840 0.22860 0.01100  -0.02000 -0.00140 20  HIS B C   
2826 O O   . HIS B 26  ? 0.14380 0.17540 0.24890 0.01090  -0.01590 -0.00130 20  HIS B O   
2827 C CB  . HIS B 26  ? 0.13910 0.17500 0.25030 0.01220  -0.01650 0.00230  20  HIS B CB  
2828 C CG  . HIS B 26  ? 0.14370 0.18010 0.25780 0.01080  -0.01320 0.00260  20  HIS B CG  
2829 N ND1 . HIS B 26  ? 0.12410 0.16280 0.23740 0.01040  -0.01240 0.00160  20  HIS B ND1 
2830 C CD2 . HIS B 26  ? 0.17120 0.20490 0.28870 0.00920  -0.00910 0.00390  20  HIS B CD2 
2831 C CE1 . HIS B 26  ? 0.17530 0.21410 0.29030 0.00830  -0.00810 0.00230  20  HIS B CE1 
2832 N NE2 . HIS B 26  ? 0.14420 0.17990 0.26190 0.00760  -0.00650 0.00450  20  HIS B NE2 
2833 N N   . ARG B 27  ? 0.13500 0.17390 0.23840 0.01160  -0.02470 -0.00040 21  ARG B N   
2834 C CA  . ARG B 27  ? 0.14800 0.18520 0.24420 0.01110  -0.02550 0.00100  21  ARG B CA  
2835 C C   . ARG B 27  ? 0.14110 0.17570 0.23770 0.01330  -0.02380 0.00450  21  ARG B C   
2836 O O   . ARG B 27  ? 0.13640 0.17120 0.23570 0.01460  -0.02500 0.00610  21  ARG B O   
2837 C CB  . ARG B 27  ? 0.17710 0.21840 0.27090 0.01090  -0.03150 0.00360  21  ARG B CB  
2838 C CG  . ARG B 27  ? 0.23730 0.28370 0.32600 0.00610  -0.03490 0.00130  21  ARG B CG  
2839 C CD  . ARG B 27  ? 0.29410 0.33550 0.37080 0.00130  -0.02990 -0.00330 21  ARG B CD  
2840 N NE  . ARG B 27  ? 0.30070 0.33740 0.37300 0.00330  -0.02630 -0.00030 21  ARG B NE  
2841 C CZ  . ARG B 27  ? 0.33820 0.37630 0.40350 0.00290  -0.02960 0.00470  21  ARG B CZ  
2842 N NH1 . ARG B 27  ? 0.28990 0.33410 0.35070 0.00080  -0.03740 0.00860  21  ARG B NH1 
2843 N NH2 . ARG B 27  ? 0.23650 0.27060 0.30090 0.00440  -0.02540 0.00730  21  ARG B NH2 
2844 N N   . VAL B 28  ? 0.17470 0.20760 0.26890 0.01280  -0.02040 0.00520  22  VAL B N   
2845 C CA  . VAL B 28  ? 0.17160 0.20520 0.26920 0.01380  -0.01920 0.00920  22  VAL B CA  
2846 C C   . VAL B 28  ? 0.18590 0.21880 0.27840 0.01260  -0.01940 0.01100  22  VAL B C   
2847 O O   . VAL B 28  ? 0.17630 0.20780 0.26210 0.01090  -0.01690 0.00920  22  VAL B O   
2848 C CB  . VAL B 28  ? 0.16520 0.19920 0.27030 0.01520  -0.01360 0.01070  22  VAL B CB  
2849 C CG1 . VAL B 28  ? 0.16650 0.20570 0.27840 0.01570  -0.01360 0.01640  22  VAL B CG1 
2850 C CG2 . VAL B 28  ? 0.19240 0.22600 0.30240 0.01620  -0.01310 0.01100  22  VAL B CG2 
2851 N N   . HIS B 29  ? 0.13370 0.16710 0.22800 0.01210  -0.02150 0.01420  23  HIS B N   
2852 C CA  . HIS B 29  ? 0.13220 0.16470 0.22400 0.01020  -0.02040 0.01720  23  HIS B CA  
2853 C C   . HIS B 29  ? 0.14270 0.17990 0.24290 0.00890  -0.01890 0.01990  23  HIS B C   
2854 O O   . HIS B 29  ? 0.15780 0.19770 0.26200 0.00790  -0.02200 0.02030  23  HIS B O   
2855 C CB  . HIS B 29  ? 0.14200 0.16980 0.23050 0.00980  -0.02410 0.01920  23  HIS B CB  
2856 C CG  . HIS B 29  ? 0.14920 0.17600 0.23460 0.01180  -0.02750 0.01880  23  HIS B CG  
2857 N ND1 . HIS B 29  ? 0.17000 0.19830 0.24750 0.01070  -0.02860 0.02050  23  HIS B ND1 
2858 C CD2 . HIS B 29  ? 0.16320 0.18970 0.25330 0.01420  -0.03000 0.01730  23  HIS B CD2 
2859 C CE1 . HIS B 29  ? 0.17130 0.20200 0.25010 0.01220  -0.03350 0.02120  23  HIS B CE1 
2860 N NE2 . HIS B 29  ? 0.17200 0.20160 0.26030 0.01510  -0.03370 0.01940  23  HIS B NE2 
2861 N N   . ALA B 30  ? 0.15770 0.19730 0.26060 0.00800  -0.01410 0.02200  24  ALA B N   
2862 C CA  . ALA B 30  ? 0.10400 0.15180 0.21910 0.00650  -0.01310 0.02600  24  ALA B CA  
2863 C C   . ALA B 30  ? 0.15640 0.20490 0.27240 0.00370  -0.00830 0.02840  24  ALA B C   
2864 O O   . ALA B 30  ? 0.14320 0.18700 0.25080 0.00400  -0.00290 0.02690  24  ALA B O   
2865 C CB  . ALA B 30  ? 0.10530 0.15940 0.23250 0.01020  -0.00950 0.02770  24  ALA B CB  
2866 N N   . ALA B 31  ? 0.14110 0.19610 0.26610 -0.00030 -0.01010 0.03200  25  ALA B N   
2867 C CA  . ALA B 31  ? 0.15150 0.20970 0.28170 -0.00370 -0.00460 0.03520  25  ALA B CA  
2868 C C   . ALA B 31  ? 0.12300 0.19670 0.27380 -0.00520 -0.00450 0.04000  25  ALA B C   
2869 O O   . ALA B 31  ? 0.12790 0.20880 0.28430 -0.00790 -0.01250 0.04170  25  ALA B O   
2870 C CB  . ALA B 31  ? 0.12300 0.17320 0.24530 -0.00920 -0.00720 0.03590  25  ALA B CB  
2871 N N   . VAL B 32  ? 0.15020 0.23030 0.31250 -0.00400 0.00480  0.04270  26  VAL B N   
2872 C CA  . VAL B 32  ? 0.10480 0.20290 0.29230 -0.00520 0.00600  0.04930  26  VAL B CA  
2873 C C   . VAL B 32  ? 0.14540 0.24490 0.33570 -0.01090 0.01260  0.05090  26  VAL B C   
2874 O O   . VAL B 32  ? 0.15830 0.25010 0.34050 -0.00950 0.02350  0.04860  26  VAL B O   
2875 C CB  . VAL B 32  ? 0.13320 0.23840 0.33860 0.00300  0.01410  0.05180  26  VAL B CB  
2876 C CG1 . VAL B 32  ? 0.09090 0.21010 0.31520 0.00300  0.01320  0.05890  26  VAL B CG1 
2877 C CG2 . VAL B 32  ? 0.12050 0.22000 0.32030 0.00870  0.00970  0.05000  26  VAL B CG2 
2878 N N   . VAL B 33  ? 0.13050 0.23930 0.33030 -0.01880 0.00650  0.05440  27  VAL B N   
2879 C CA  . VAL B 33  ? 0.15410 0.26140 0.35430 -0.02590 0.01230  0.05580  27  VAL B CA  
2880 C C   . VAL B 33  ? 0.15900 0.28790 0.38650 -0.03080 0.01200  0.06210  27  VAL B C   
2881 O O   . VAL B 33  ? 0.11760 0.25600 0.35020 -0.02950 0.00300  0.06330  27  VAL B O   
2882 C CB  . VAL B 33  ? 0.15250 0.24440 0.33430 -0.03300 0.00640  0.05280  27  VAL B CB  
2883 C CG1 . VAL B 33  ? 0.16420 0.23770 0.32270 -0.02740 0.00530  0.04830  27  VAL B CG1 
2884 C CG2 . VAL B 33  ? 0.13800 0.23710 0.32570 -0.04040 -0.00510 0.05200  27  VAL B CG2 
2885 N N   . ASP B 34  ? 0.12750 0.25820 0.36090 -0.03560 0.02110  0.06410  28  ASP B N   
2886 C CA  . ASP B 34  ? 0.15280 0.29860 0.40210 -0.03930 0.01950  0.06700  28  ASP B CA  
2887 C C   . ASP B 34  ? 0.16340 0.30820 0.40810 -0.05210 0.01030  0.06570  28  ASP B C   
2888 O O   . ASP B 34  ? 0.17980 0.31060 0.40960 -0.05670 0.00540  0.06240  28  ASP B O   
2889 C CB  . ASP B 34  ? 0.19250 0.34260 0.45290 -0.03720 0.03520  0.06910  28  ASP B CB  
2890 C CG  . ASP B 34  ? 0.28160 0.42130 0.53230 -0.04550 0.04410  0.06910  28  ASP B CG  
2891 O OD1 . ASP B 34  ? 0.22530 0.35350 0.46310 -0.05290 0.03790  0.06850  28  ASP B OD1 
2892 O OD2 . ASP B 34  ? 0.29590 0.43740 0.55120 -0.04470 0.05820  0.07010  28  ASP B OD2 
2893 N N   . ALA B 35  ? 0.19890 0.35830 0.45750 -0.05830 0.00850  0.06780  29  ALA B N   
2894 C CA  . ALA B 35  ? 0.20870 0.36910 0.46450 -0.07200 0.00020  0.06500  29  ALA B CA  
2895 C C   . ALA B 35  ? 0.23660 0.37830 0.48140 -0.08050 0.00640  0.06260  29  ALA B C   
2896 O O   . ALA B 35  ? 0.27290 0.40680 0.51000 -0.09160 0.00050  0.05800  29  ALA B O   
2897 C CB  . ALA B 35  ? 0.23150 0.41340 0.50730 -0.07680 -0.00140 0.06840  29  ALA B CB  
2898 N N   . LYS B 36  ? 0.25370 0.38630 0.49610 -0.07620 0.01910  0.06570  30  LYS B N   
2899 C CA  . LYS B 36  ? 0.26060 0.37220 0.48970 -0.08260 0.02520  0.06610  30  LYS B CA  
2900 C C   . LYS B 36  ? 0.26460 0.35590 0.47400 -0.07620 0.02440  0.06530  30  LYS B C   
2901 O O   . LYS B 36  ? 0.29210 0.36230 0.48490 -0.07820 0.02840  0.06620  30  LYS B O   
2902 C CB  . LYS B 36  ? 0.29150 0.40420 0.52460 -0.08320 0.03980  0.07090  30  LYS B CB  
2903 C CG  . LYS B 36  ? 0.33220 0.46250 0.58360 -0.09040 0.04150  0.07140  30  LYS B CG  
2904 C CD  . LYS B 36  ? 0.42800 0.55600 0.68010 -0.09260 0.05730  0.07570  30  LYS B CD  
2905 C CE  . LYS B 36  ? 0.45390 0.59980 0.72610 -0.10110 0.05900  0.07630  30  LYS B CE  
2906 N NZ  . LYS B 36  ? 0.49140 0.63630 0.76470 -0.11360 0.04760  0.07240  30  LYS B NZ  
2907 N N   . GLY B 37  ? 0.25660 0.35100 0.46130 -0.06630 0.01880  0.06230  31  GLY B N   
2908 C CA  . GLY B 37  ? 0.24140 0.31650 0.42200 -0.05790 0.01680  0.05880  31  GLY B CA  
2909 C C   . GLY B 37  ? 0.24390 0.31470 0.41350 -0.04930 0.02610  0.06050  31  GLY B C   
2910 O O   . GLY B 37  ? 0.27100 0.32810 0.42100 -0.04330 0.02380  0.05830  31  GLY B O   
2911 N N   . ARG B 38  ? 0.26560 0.34830 0.44740 -0.04950 0.03700  0.06370  32  ARG B N   
2912 C CA  . ARG B 38  ? 0.23990 0.31900 0.41000 -0.04280 0.04740  0.06280  32  ARG B CA  
2913 C C   . ARG B 38  ? 0.21010 0.29080 0.37810 -0.03340 0.04310  0.05770  32  ARG B C   
2914 O O   . ARG B 38  ? 0.20220 0.29650 0.38970 -0.03070 0.03810  0.05760  32  ARG B O   
2915 C CB  . ARG B 38  ? 0.31270 0.40600 0.50140 -0.04460 0.06160  0.06560  32  ARG B CB  
2916 C CG  . ARG B 38  ? 0.39400 0.48090 0.56720 -0.04180 0.07680  0.06360  32  ARG B CG  
2917 C CD  . ARG B 38  ? 0.50690 0.60670 0.70040 -0.04700 0.09200  0.06760  32  ARG B CD  
2918 N NE  . ARG B 38  ? 0.53000 0.63790 0.74160 -0.05520 0.08450  0.07310  32  ARG B NE  
2919 C CZ  . ARG B 38  ? 0.47270 0.59310 0.70170 -0.05930 0.08840  0.07430  32  ARG B CZ  
2920 N NH1 . ARG B 38  ? 0.53260 0.66000 0.76830 -0.05660 0.10300  0.07300  32  ARG B NH1 
2921 N NH2 . ARG B 38  ? 0.47470 0.60040 0.71420 -0.06670 0.07750  0.07580  32  ARG B NH2 
2922 N N   . LEU B 39  ? 0.21750 0.28520 0.36200 -0.02930 0.04520  0.05450  33  LEU B N   
2923 C CA  . LEU B 39  ? 0.27100 0.33680 0.41020 -0.02170 0.04110  0.04900  33  LEU B CA  
2924 C C   . LEU B 39  ? 0.23730 0.31060 0.38760 -0.01710 0.05390  0.04600  33  LEU B C   
2925 O O   . LEU B 39  ? 0.23650 0.30530 0.37570 -0.01890 0.06660  0.04410  33  LEU B O   
2926 C CB  . LEU B 39  ? 0.28290 0.33320 0.39370 -0.02090 0.03710  0.04700  33  LEU B CB  
2927 C CG  . LEU B 39  ? 0.29510 0.34300 0.39960 -0.01460 0.03290  0.04100  33  LEU B CG  
2928 C CD1 . LEU B 39  ? 0.19640 0.24710 0.31170 -0.01200 0.02100  0.04070  33  LEU B CD1 
2929 C CD2 . LEU B 39  ? 0.28360 0.32030 0.36130 -0.01550 0.03070  0.03980  33  LEU B CD2 
2930 N N   . LEU B 40  ? 0.16880 0.25270 0.34060 -0.01140 0.05130  0.04600  34  LEU B N   
2931 C CA  . LEU B 40  ? 0.20560 0.29580 0.39440 -0.00540 0.06440  0.04420  34  LEU B CA  
2932 C C   . LEU B 40  ? 0.17600 0.25560 0.35310 0.00050  0.06530  0.03720  34  LEU B C   
2933 O O   . LEU B 40  ? 0.20620 0.28010 0.38070 0.00260  0.08010  0.03130  34  LEU B O   
2934 C CB  . LEU B 40  ? 0.12370 0.23450 0.34930 -0.00250 0.06160  0.05180  34  LEU B CB  
2935 C CG  . LEU B 40  ? 0.22830 0.35240 0.46830 -0.00970 0.05770  0.05840  34  LEU B CG  
2936 C CD1 . LEU B 40  ? 0.18900 0.32610 0.44660 -0.00700 0.04710  0.06330  34  LEU B CD1 
2937 C CD2 . LEU B 40  ? 0.20290 0.32730 0.44500 -0.01300 0.07400  0.05810  34  LEU B CD2 
2938 N N   . TYR B 41  ? 0.16530 0.24160 0.33570 0.00240  0.05130  0.03680  35  TYR B N   
2939 C CA  . TYR B 41  ? 0.16830 0.23550 0.32970 0.00700  0.05060  0.03090  35  TYR B CA  
2940 C C   . TYR B 41  ? 0.17240 0.23200 0.31330 0.00480  0.03630  0.02940  35  TYR B C   
2941 O O   . TYR B 41  ? 0.17920 0.24160 0.31940 0.00160  0.02640  0.03360  35  TYR B O   
2942 C CB  . TYR B 41  ? 0.15200 0.22800 0.34030 0.01450  0.05090  0.03470  35  TYR B CB  
2943 C CG  . TYR B 41  ? 0.16020 0.24510 0.37540 0.01850  0.06590  0.03770  35  TYR B CG  
2944 C CD1 . TYR B 41  ? 0.24480 0.31970 0.46050 0.02190  0.08350  0.03030  35  TYR B CD1 
2945 C CD2 . TYR B 41  ? 0.17510 0.27450 0.40880 0.01730  0.06190  0.04630  35  TYR B CD2 
2946 C CE1 . TYR B 41  ? 0.22420 0.30050 0.45610 0.02490  0.09570  0.03160  35  TYR B CE1 
2947 C CE2 . TYR B 41  ? 0.21920 0.32160 0.46840 0.02020  0.07250  0.04820  35  TYR B CE2 
2948 C CZ  . TYR B 41  ? 0.25320 0.34370 0.50230 0.02460  0.08950  0.04120  35  TYR B CZ  
2949 O OH  . TYR B 41  ? 0.25050 0.34330 0.51710 0.02780  0.10040  0.04340  35  TYR B OH  
2950 N N   . ALA B 42  ? 0.16910 0.21880 0.29450 0.00610  0.03600  0.02290  36  ALA B N   
2951 C CA  . ALA B 42  ? 0.16610 0.20990 0.27470 0.00450  0.02390  0.02190  36  ALA B CA  
2952 C C   . ALA B 42  ? 0.17430 0.21260 0.27810 0.00720  0.02310  0.01600  36  ALA B C   
2953 O O   . ALA B 42  ? 0.20170 0.23610 0.30670 0.00820  0.03350  0.01060  36  ALA B O   
2954 C CB  . ALA B 42  ? 0.19350 0.23080 0.28000 -0.00080 0.02290  0.02180  36  ALA B CB  
2955 N N   . LEU B 43  ? 0.16740 0.20460 0.26660 0.00770  0.01210  0.01640  37  LEU B N   
2956 C CA  . LEU B 43  ? 0.15610 0.18810 0.24680 0.00810  0.00940  0.01110  37  LEU B CA  
2957 C C   . LEU B 43  ? 0.19920 0.22960 0.27700 0.00590  -0.00030 0.01230  37  LEU B C   
2958 O O   . LEU B 43  ? 0.18020 0.21190 0.26030 0.00590  -0.00570 0.01730  37  LEU B O   
2959 C CB  . LEU B 43  ? 0.16090 0.19510 0.26500 0.01230  0.00660  0.01210  37  LEU B CB  
2960 C CG  . LEU B 43  ? 0.25180 0.28930 0.37470 0.01650  0.01430  0.01460  37  LEU B CG  
2961 C CD1 . LEU B 43  ? 0.20310 0.24490 0.33610 0.01940  0.00750  0.01950  37  LEU B CD1 
2962 C CD2 . LEU B 43  ? 0.21060 0.23950 0.33200 0.01670  0.02620  0.00740  37  LEU B CD2 
2963 N N   . GLY B 44  ? 0.21630 0.24410 0.28280 0.00380  -0.00250 0.00790  38  GLY B N   
2964 C CA  . GLY B 44  ? 0.19780 0.22660 0.25730 0.00300  -0.01230 0.01110  38  GLY B CA  
2965 C C   . GLY B 44  ? 0.26570 0.29390 0.31750 0.00090  -0.01390 0.01770  38  GLY B C   
2966 O O   . GLY B 44  ? 0.25390 0.28100 0.29530 -0.00300 -0.00810 0.01760  38  GLY B O   
2967 N N   . ASN B 45  ? 0.22890 0.25650 0.28610 0.00340  -0.02040 0.02330  39  ASN B N   
2968 C CA  . ASN B 45  ? 0.21910 0.24370 0.27250 0.00210  -0.02150 0.03110  39  ASN B CA  
2969 C C   . ASN B 45  ? 0.22010 0.24230 0.28480 0.00260  -0.01850 0.03210  39  ASN B C   
2970 O O   . ASN B 45  ? 0.19840 0.21800 0.27170 0.00480  -0.02190 0.03210  39  ASN B O   
2971 C CB  . ASN B 45  ? 0.25050 0.27440 0.30440 0.00440  -0.02980 0.03730  39  ASN B CB  
2972 C CG  . ASN B 45  ? 0.29620 0.31430 0.34960 0.00410  -0.03030 0.04690  39  ASN B CG  
2973 O OD1 . ASN B 45  ? 0.21100 0.22620 0.26040 0.00060  -0.02470 0.04880  39  ASN B OD1 
2974 N ND2 . ASN B 45  ? 0.27060 0.28660 0.33030 0.00790  -0.03600 0.05360  39  ASN B ND2 
2975 N N   . PRO B 46  ? 0.20290 0.22640 0.26820 -0.00030 -0.01170 0.03270  40  PRO B N   
2976 C CA  . PRO B 46  ? 0.16540 0.18990 0.24320 -0.00160 -0.01010 0.03390  40  PRO B CA  
2977 C C   . PRO B 46  ? 0.20070 0.21770 0.27910 -0.00360 -0.01250 0.03910  40  PRO B C   
2978 O O   . PRO B 46  ? 0.21590 0.23270 0.30360 -0.00650 -0.01220 0.03850  40  PRO B O   
2979 C CB  . PRO B 46  ? 0.18450 0.21420 0.26470 -0.00410 -0.00120 0.03410  40  PRO B CB  
2980 C CG  . PRO B 46  ? 0.20300 0.22910 0.26530 -0.00620 0.00220  0.03510  40  PRO B CG  
2981 C CD  . PRO B 46  ? 0.21260 0.23740 0.26700 -0.00370 -0.00450 0.03200  40  PRO B CD  
2982 N N   . THR B 47  ? 0.19520 0.20590 0.26460 -0.00300 -0.01480 0.04480  41  THR B N   
2983 C CA  . THR B 47  ? 0.19800 0.19870 0.27110 -0.00390 -0.01580 0.05060  41  THR B CA  
2984 C C   . THR B 47  ? 0.21460 0.20960 0.29250 0.00140  -0.02100 0.05100  41  THR B C   
2985 O O   . THR B 47  ? 0.22750 0.21250 0.30900 0.00250  -0.02110 0.05760  41  THR B O   
2986 C CB  . THR B 47  ? 0.24790 0.24460 0.31150 -0.00670 -0.01340 0.06050  41  THR B CB  
2987 O OG1 . THR B 47  ? 0.28860 0.28810 0.34030 -0.00440 -0.01820 0.06520  41  THR B OG1 
2988 C CG2 . THR B 47  ? 0.19660 0.19850 0.25740 -0.01220 -0.00570 0.05980  41  THR B CG2 
2989 N N   . ARG B 48  ? 0.24310 0.24380 0.32330 0.00470  -0.02390 0.04450  42  ARG B N   
2990 C CA  . ARG B 48  ? 0.19750 0.19470 0.28470 0.00980  -0.02710 0.04390  42  ARG B CA  
2991 C C   . ARG B 48  ? 0.22850 0.21370 0.32470 0.00900  -0.02350 0.04210  42  ARG B C   
2992 O O   . ARG B 48  ? 0.17050 0.15480 0.26770 0.00420  -0.02090 0.03520  42  ARG B O   
2993 C CB  . ARG B 48  ? 0.17190 0.17680 0.26060 0.01160  -0.02860 0.03590  42  ARG B CB  
2994 C CG  . ARG B 48  ? 0.17080 0.17430 0.26840 0.01660  -0.03040 0.03450  42  ARG B CG  
2995 C CD  . ARG B 48  ? 0.16320 0.17180 0.26200 0.01640  -0.02950 0.02570  42  ARG B CD  
2996 N NE  . ARG B 48  ? 0.20330 0.21220 0.31070 0.02070  -0.02970 0.02370  42  ARG B NE  
2997 C CZ  . ARG B 48  ? 0.18300 0.18410 0.29700 0.02140  -0.02510 0.01950  42  ARG B CZ  
2998 N NH1 . ARG B 48  ? 0.14480 0.13640 0.25630 0.01730  -0.02110 0.01670  42  ARG B NH1 
2999 N NH2 . ARG B 48  ? 0.17650 0.17950 0.29920 0.02530  -0.02340 0.01690  42  ARG B NH2 
3000 N N   . MET B 49  ? 0.19560 0.17160 0.29880 0.01330  -0.02340 0.04850  43  MET B N   
3001 C CA  A MET B 49  ? 0.21490 0.17610 0.32770 0.01310  -0.01770 0.04460  43  MET B CA  
3002 C CA  B MET B 49  ? 0.21620 0.17750 0.32920 0.01310  -0.01770 0.04470  43  MET B CA  
3003 C C   . MET B 49  ? 0.18830 0.15160 0.30330 0.01290  -0.01600 0.03260  43  MET B C   
3004 O O   . MET B 49  ? 0.17150 0.14100 0.29070 0.01850  -0.01810 0.03200  43  MET B O   
3005 C CB  A MET B 49  ? 0.23140 0.18300 0.35600 0.02020  -0.01690 0.05470  43  MET B CB  
3006 C CB  B MET B 49  ? 0.23180 0.18410 0.35630 0.02050  -0.01720 0.05490  43  MET B CB  
3007 C CG  A MET B 49  ? 0.25100 0.18460 0.38820 0.02120  -0.00810 0.04870  43  MET B CG  
3008 C CG  B MET B 49  ? 0.26180 0.19340 0.39660 0.01960  -0.00860 0.05380  43  MET B CG  
3009 S SD  A MET B 49  ? 0.24820 0.16550 0.38110 0.00990  -0.00050 0.04220  43  MET B SD  
3010 S SD  B MET B 49  ? 0.27770 0.19960 0.40480 0.00890  -0.00460 0.05440  43  MET B SD  
3011 C CE  A MET B 49  ? 0.27220 0.17690 0.41180 0.01290  0.00100  0.05990  43  MET B CE  
3012 C CE  B MET B 49  ? 0.26250 0.15740 0.40400 0.00850  0.00670  0.05050  43  MET B CE  
3013 N N   . THR B 50  ? 0.20990 0.16930 0.32120 0.00520  -0.01250 0.02360  44  THR B N   
3014 C CA  . THR B 50  ? 0.17760 0.14170 0.28560 0.00270  -0.01200 0.01320  44  THR B CA  
3015 C C   . THR B 50  ? 0.22650 0.17750 0.33320 -0.00490 -0.00550 0.00340  44  THR B C   
3016 O O   . THR B 50  ? 0.20940 0.15540 0.31360 -0.01310 -0.00430 0.00210  44  THR B O   
3017 C CB  . THR B 50  ? 0.17300 0.15280 0.27350 -0.00120 -0.01710 0.01240  44  THR B CB  
3018 O OG1 . THR B 50  ? 0.15530 0.14450 0.25530 0.00460  -0.02100 0.01890  44  THR B OG1 
3019 C CG2 . THR B 50  ? 0.16020 0.14600 0.25640 -0.00390 -0.01750 0.00450  44  THR B CG2 
3020 N N   . LEU B 51  ? 0.17640 0.12240 0.28430 -0.00340 -0.00060 -0.00440 45  LEU B N   
3021 C CA  . LEU B 51  ? 0.20190 0.13680 0.30320 -0.01300 0.00620  -0.01690 45  LEU B CA  
3022 C C   . LEU B 51  ? 0.22250 0.17110 0.31010 -0.02350 0.00000  -0.02100 45  LEU B C   
3023 O O   . LEU B 51  ? 0.22530 0.18710 0.30790 -0.02210 -0.00420 -0.02090 45  LEU B O   
3024 C CB  . LEU B 51  ? 0.18110 0.10880 0.28600 -0.00870 0.01450  -0.02440 45  LEU B CB  
3025 C CG  . LEU B 51  ? 0.24060 0.15350 0.36400 0.00140  0.02220  -0.02000 45  LEU B CG  
3026 C CD1 . LEU B 51  ? 0.25100 0.16760 0.38480 0.01040  0.02670  -0.02130 45  LEU B CD1 
3027 C CD2 . LEU B 51  ? 0.21730 0.10730 0.34150 -0.00540 0.03340  -0.02880 45  LEU B CD2 
3028 N N   . ALA B 52  ? 0.20950 0.15590 0.29270 -0.03440 -0.00100 -0.02330 46  ALA B N   
3029 C CA  . ALA B 52  ? 0.21810 0.18050 0.29180 -0.04500 -0.00840 -0.02480 46  ALA B CA  
3030 C C   . ALA B 52  ? 0.22200 0.18490 0.28150 -0.05330 -0.00690 -0.03540 46  ALA B C   
3031 O O   . ALA B 52  ? 0.23880 0.21920 0.29090 -0.05810 -0.01470 -0.03310 46  ALA B O   
3032 C CB  . ALA B 52  ? 0.21520 0.17550 0.29010 -0.05610 -0.00940 -0.02520 46  ALA B CB  
3033 N N   . ARG B 53  ? 0.18290 0.23710 0.30290 -0.06580 -0.00550 -0.00750 47  ARG B N   
3034 C CA  . ARG B 53  ? 0.19310 0.24380 0.31180 -0.07030 -0.00010 -0.00950 47  ARG B CA  
3035 C C   . ARG B 53  ? 0.22130 0.25910 0.32560 -0.07260 -0.00170 -0.00850 47  ARG B C   
3036 O O   . ARG B 53  ? 0.21330 0.24650 0.31470 -0.06980 -0.00410 -0.00820 47  ARG B O   
3037 C CB  . ARG B 53  ? 0.17960 0.23530 0.29890 -0.07410 0.00110  -0.00890 47  ARG B CB  
3038 C CG  . ARG B 53  ? 0.19730 0.26690 0.33120 -0.07210 0.00180  -0.00940 47  ARG B CG  
3039 C CD  . ARG B 53  ? 0.17590 0.25310 0.32710 -0.06920 0.00870  -0.01300 47  ARG B CD  
3040 N NE  . ARG B 53  ? 0.22590 0.30110 0.37650 -0.07360 0.01730  -0.01680 47  ARG B NE  
3041 C CZ  . ARG B 53  ? 0.22340 0.30410 0.37600 -0.07730 0.02050  -0.01710 47  ARG B CZ  
3042 N NH1 . ARG B 53  ? 0.18250 0.27130 0.33880 -0.07750 0.01550  -0.01390 47  ARG B NH1 
3043 N NH2 . ARG B 53  ? 0.23770 0.31550 0.38730 -0.08160 0.02940  -0.02110 47  ARG B NH2 
3044 N N   . SER B 54  ? 0.22010 0.25180 0.31670 -0.07710 -0.00070 -0.00760 48  SER B N   
3045 C CA  . SER B 54  ? 0.22590 0.24670 0.31310 -0.07800 -0.00280 -0.00650 48  SER B CA  
3046 C C   . SER B 54  ? 0.25380 0.26930 0.34140 -0.07120 -0.00700 -0.00540 48  SER B C   
3047 O O   . SER B 54  ? 0.23200 0.24120 0.31140 -0.07250 -0.00630 -0.00710 48  SER B O   
3048 C CB  . SER B 54  ? 0.28510 0.30160 0.36370 -0.08340 0.00180  -0.00800 48  SER B CB  
3049 O OG  . SER B 54  ? 0.34960 0.36800 0.42710 -0.08750 0.01000  -0.01380 48  SER B OG  
3050 N N   . ALA B 55  ? 0.22320 0.24440 0.30220 -0.07210 -0.00430 -0.00920 49  ALA B N   
3051 C CA  . ALA B 55  ? 0.22760 0.24460 0.30400 -0.06860 -0.00780 -0.00750 49  ALA B CA  
3052 C C   . ALA B 55  ? 0.23970 0.25610 0.31610 -0.06510 -0.01080 -0.00580 49  ALA B C   
3053 O O   . ALA B 55  ? 0.21850 0.23030 0.29150 -0.06160 -0.01350 -0.00360 49  ALA B O   
3054 C CB  . ALA B 55  ? 0.19030 0.21120 0.26810 -0.06750 -0.00880 -0.00750 49  ALA B CB  
3055 N N   . ALA B 56  ? 0.22130 0.24160 0.30350 -0.06550 -0.01050 -0.00600 50  ALA B N   
3056 C CA  . ALA B 56  ? 0.24790 0.26570 0.33340 -0.06170 -0.01240 -0.00500 50  ALA B CA  
3057 C C   . ALA B 56  ? 0.25240 0.26240 0.33150 -0.06510 -0.01120 -0.00630 50  ALA B C   
3058 O O   . ALA B 56  ? 0.24480 0.25120 0.32470 -0.06240 -0.01290 -0.00570 50  ALA B O   
3059 C CB  . ALA B 56  ? 0.19920 0.22450 0.29990 -0.05850 -0.01170 -0.00520 50  ALA B CB  
3060 N N   . LYS B 57  ? 0.24730 0.25440 0.32000 -0.07130 -0.00820 -0.00850 51  LYS B N   
3061 C CA  . LYS B 57  ? 0.29450 0.29420 0.36880 -0.07190 -0.00760 -0.01060 51  LYS B CA  
3062 C C   . LYS B 57  ? 0.28710 0.28180 0.35290 -0.07090 -0.01120 -0.00880 51  LYS B C   
3063 O O   . LYS B 57  ? 0.30940 0.29950 0.37410 -0.07220 -0.01150 -0.01050 51  LYS B O   
3064 C CB  . LYS B 57  ? 0.30590 0.30270 0.37190 -0.07830 -0.00760 -0.00880 51  LYS B CB  
3065 C CG  . LYS B 57  ? 0.31200 0.31340 0.37930 -0.08240 -0.00090 -0.01230 51  LYS B CG  
3066 C CD  . LYS B 57  ? 0.38040 0.37940 0.44630 -0.08540 0.00630  -0.01940 51  LYS B CD  
3067 C CE  . LYS B 57  ? 0.45810 0.46200 0.52770 -0.08910 0.01660  -0.02510 51  LYS B CE  
3068 N NZ  . LYS B 57  ? 0.48000 0.49380 0.57100 -0.08320 0.02010  -0.02710 51  LYS B NZ  
3069 N N   . PRO B 58  ? 0.25980 0.25440 0.32140 -0.06770 -0.01470 -0.00450 52  PRO B N   
3070 C CA  . PRO B 58  ? 0.29730 0.28840 0.35470 -0.06510 -0.01880 -0.00130 52  PRO B CA  
3071 C C   . PRO B 58  ? 0.27410 0.26580 0.33560 -0.06130 -0.01940 -0.00150 52  PRO B C   
3072 O O   . PRO B 58  ? 0.27200 0.26010 0.33130 -0.06130 -0.02120 -0.00100 52  PRO B O   
3073 C CB  . PRO B 58  ? 0.25920 0.25090 0.31520 -0.06230 -0.02140 0.00320  52  PRO B CB  
3074 C CG  . PRO B 58  ? 0.27120 0.26380 0.32650 -0.06580 -0.01910 0.00240  52  PRO B CG  
3075 C CD  . PRO B 58  ? 0.25640 0.25320 0.31780 -0.06710 -0.01480 -0.00250 52  PRO B CD  
3076 N N   . ALA B 59  ? 0.25580 0.25190 0.32380 -0.05820 -0.01850 -0.00150 53  ALA B N   
3077 C CA  . ALA B 59  ? 0.27380 0.27010 0.34790 -0.05430 -0.01980 -0.00050 53  ALA B CA  
3078 C C   . ALA B 59  ? 0.29400 0.28690 0.37100 -0.05730 -0.01740 -0.00380 53  ALA B C   
3079 O O   . ALA B 59  ? 0.33150 0.32040 0.41020 -0.05580 -0.01820 -0.00360 53  ALA B O   
3080 C CB  . ALA B 59  ? 0.30960 0.31230 0.39240 -0.05000 -0.02050 0.00120  53  ALA B CB  
3081 N N   . GLN B 60  ? 0.28010 0.27390 0.35880 -0.06150 -0.01400 -0.00710 54  GLN B N   
3082 C CA  . GLN B 60  ? 0.25970 0.24840 0.34210 -0.06430 -0.01050 -0.01140 54  GLN B CA  
3083 C C   . GLN B 60  ? 0.30590 0.28590 0.37420 -0.07050 -0.01170 -0.01300 54  GLN B C   
3084 O O   . GLN B 60  ? 0.29840 0.27200 0.36790 -0.07120 -0.01050 -0.01590 54  GLN B O   
3085 C CB  . GLN B 60  ? 0.31560 0.30810 0.40470 -0.06670 -0.00470 -0.01560 54  GLN B CB  
3086 C CG  . GLN B 60  ? 0.30290 0.30570 0.40730 -0.06120 -0.00390 -0.01390 54  GLN B CG  
3087 C CD  . GLN B 60  ? 0.34610 0.35500 0.45900 -0.06340 0.00310  -0.01820 54  GLN B CD  
3088 O OE1 . GLN B 60  ? 0.43830 0.45690 0.56010 -0.06080 0.00240  -0.01600 54  GLN B OE1 
3089 N NE2 . GLN B 60  ? 0.39760 0.40140 0.50700 -0.06840 0.01060  -0.02480 54  GLN B NE2 
3090 N N   . ALA B 61  ? 0.28140 0.26250 0.34310 -0.07270 -0.01200 -0.01340 55  ALA B N   
3091 C CA  . ALA B 61  ? 0.31220 0.28810 0.36860 -0.07490 -0.01530 -0.01370 55  ALA B CA  
3092 C C   . ALA B 61  ? 0.27110 0.24540 0.32590 -0.07220 -0.01770 -0.01190 55  ALA B C   
3093 O O   . ALA B 61  ? 0.30380 0.27330 0.35480 -0.07530 -0.01930 -0.01370 55  ALA B O   
3094 C CB  . ALA B 61  ? 0.31130 0.28860 0.35800 -0.07680 -0.01880 -0.00920 55  ALA B CB  
3095 N N   . LEU B 62  ? 0.26980 0.24800 0.32820 -0.06610 -0.01960 -0.00720 56  LEU B N   
3096 C CA  . LEU B 62  ? 0.27370 0.25050 0.33330 -0.06290 -0.02240 -0.00450 56  LEU B CA  
3097 C C   . LEU B 62  ? 0.28970 0.26110 0.35230 -0.06410 -0.01990 -0.00790 56  LEU B C   
3098 O O   . LEU B 62  ? 0.27400 0.24180 0.33520 -0.06490 -0.02110 -0.00810 56  LEU B O   
3099 C CB  . LEU B 62  ? 0.23570 0.21720 0.30080 -0.05580 -0.02470 0.00080  56  LEU B CB  
3100 C CG  . LEU B 62  ? 0.28200 0.26270 0.35090 -0.05200 -0.02700 0.00380  56  LEU B CG  
3101 C CD1 . LEU B 62  ? 0.29040 0.27010 0.35460 -0.05370 -0.03010 0.00570  56  LEU B CD1 
3102 C CD2 . LEU B 62  ? 0.28970 0.27490 0.36480 -0.04600 -0.02810 0.00780  56  LEU B CD2 
3103 N N   . ALA B 63  ? 0.25790 0.22870 0.32680 -0.06360 -0.01690 -0.00980 57  ALA B N   
3104 C CA  . ALA B 63  ? 0.23990 0.20420 0.31520 -0.06340 -0.01410 -0.01310 57  ALA B CA  
3105 C C   . ALA B 63  ? 0.27320 0.22810 0.33680 -0.07190 -0.01290 -0.01850 57  ALA B C   
3106 O O   . ALA B 63  ? 0.30220 0.25020 0.36490 -0.07290 -0.01270 -0.02040 57  ALA B O   
3107 C CB  . ALA B 63  ? 0.24650 0.21410 0.33720 -0.05930 -0.00960 -0.01500 57  ALA B CB  
3108 N N   . ILE B 64  ? 0.25800 0.21220 0.31370 -0.07770 -0.01420 -0.02000 58  ILE B N   
3109 C CA  . ILE B 64  ? 0.28220 0.23080 0.33240 -0.08240 -0.01380 -0.02580 58  ILE B CA  
3110 C C   . ILE B 64  ? 0.31060 0.26060 0.36100 -0.08250 -0.01830 -0.02480 58  ILE B C   
3111 O O   . ILE B 64  ? 0.30780 0.25090 0.35340 -0.08580 -0.01880 -0.02810 58  ILE B O   
3112 C CB  . ILE B 64  ? 0.32300 0.27430 0.36220 -0.08740 -0.01070 -0.02830 58  ILE B CB  
3113 C CG1 . ILE B 64  ? 0.28750 0.24040 0.33130 -0.08710 -0.00150 -0.03300 58  ILE B CG1 
3114 C CG2 . ILE B 64  ? 0.32980 0.27530 0.35100 -0.09560 -0.00980 -0.03320 58  ILE B CG2 
3115 C CD1 . ILE B 64  ? 0.33230 0.29020 0.36810 -0.09100 -0.00020 -0.03220 58  ILE B CD1 
3116 N N   . LEU B 65  ? 0.26250 0.22060 0.31090 -0.08020 -0.02050 -0.01980 59  LEU B N   
3117 C CA  . LEU B 65  ? 0.33650 0.29560 0.37890 -0.08130 -0.02580 -0.01630 59  LEU B CA  
3118 C C   . LEU B 65  ? 0.31080 0.26820 0.35920 -0.07880 -0.02480 -0.01660 59  LEU B C   
3119 O O   . LEU B 65  ? 0.31730 0.27400 0.36280 -0.08120 -0.02850 -0.01580 59  LEU B O   
3120 C CB  . LEU B 65  ? 0.31630 0.28200 0.35620 -0.07830 -0.03070 -0.00830 59  LEU B CB  
3121 C CG  . LEU B 65  ? 0.35900 0.32600 0.38990 -0.08180 -0.03310 -0.00570 59  LEU B CG  
3122 C CD1 . LEU B 65  ? 0.34010 0.31200 0.37260 -0.07760 -0.03790 0.00250  59  LEU B CD1 
3123 C CD2 . LEU B 65  ? 0.35330 0.31610 0.36960 -0.09070 -0.03600 -0.00720 59  LEU B CD2 
3124 N N   . GLU B 66  ? 0.27580 0.23230 0.32950 -0.07490 -0.02080 -0.01610 60  GLU B N   
3125 C CA  . GLU B 66  ? 0.28660 0.23980 0.34350 -0.07270 -0.02100 -0.01420 60  GLU B CA  
3126 C C   . GLU B 66  ? 0.33410 0.27600 0.38810 -0.07750 -0.01670 -0.02020 60  GLU B C   
3127 O O   . GLU B 66  ? 0.34780 0.28570 0.40680 -0.07460 -0.01710 -0.01830 60  GLU B O   
3128 C CB  . GLU B 66  ? 0.32230 0.28000 0.38810 -0.06420 -0.02240 -0.00780 60  GLU B CB  
3129 C CG  . GLU B 66  ? 0.32500 0.29100 0.39160 -0.05970 -0.02650 -0.00190 60  GLU B CG  
3130 C CD  . GLU B 66  ? 0.32490 0.29470 0.40050 -0.05230 -0.02730 0.00310  60  GLU B CD  
3131 O OE1 . GLU B 66  ? 0.39430 0.36360 0.47670 -0.04980 -0.02510 0.00260  60  GLU B OE1 
3132 O OE2 . GLU B 66  ? 0.37110 0.34450 0.44850 -0.04920 -0.03020 0.00760  60  GLU B OE2 
3133 N N   . THR B 67  ? 0.28600 0.22160 0.33000 -0.08310 -0.01520 -0.02480 61  THR B N   
3134 C CA  . THR B 67  ? 0.32110 0.24400 0.37040 -0.08400 -0.01680 -0.02840 61  THR B CA  
3135 C C   . THR B 67  ? 0.39110 0.31110 0.44070 -0.08740 -0.02190 -0.03140 61  THR B C   
3136 O O   . THR B 67  ? 0.32970 0.25550 0.37610 -0.09120 -0.02230 -0.03540 61  THR B O   
3137 C CB  . THR B 67  ? 0.31290 0.23490 0.36350 -0.08430 -0.00830 -0.03680 61  THR B CB  
3138 O OG1 . THR B 67  ? 0.30670 0.23530 0.36780 -0.07830 -0.00410 -0.03460 61  THR B OG1 
3139 C CG2 . THR B 67  ? 0.29320 0.20510 0.34530 -0.08500 0.00090  -0.04590 61  THR B CG2 
3140 N N   . GLU B 68  ? 0.32560 0.23700 0.37270 -0.08860 -0.02080 -0.03150 62  GLU B N   
3141 C CA  . GLU B 68  ? 0.27220 0.18150 0.32230 -0.09160 -0.02450 -0.03500 62  GLU B CA  
3142 C C   . GLU B 68  ? 0.40860 0.31310 0.44640 -0.09900 -0.01910 -0.04590 62  GLU B C   
3143 O O   . GLU B 68  ? 0.34890 0.24550 0.38140 -0.09970 -0.00940 -0.05300 62  GLU B O   
3144 C CB  . GLU B 68  ? 0.29910 0.19680 0.34560 -0.09270 -0.02120 -0.03460 62  GLU B CB  
3145 C CG  . GLU B 68  ? 0.30800 0.21130 0.35680 -0.08850 -0.01660 -0.02840 62  GLU B CG  
3146 C CD  . GLU B 68  ? 0.33130 0.23900 0.39670 -0.07760 -0.01150 -0.02660 62  GLU B CD  
3147 O OE1 . GLU B 68  ? 0.34020 0.24810 0.40760 -0.07630 -0.00840 -0.03010 62  GLU B OE1 
3148 O OE2 . GLU B 68  ? 0.30590 0.21810 0.38350 -0.07040 -0.01100 -0.02120 62  GLU B OE2 
3149 N N   . GLY B 69  ? 0.34360 0.25370 0.37310 -0.10470 -0.02300 -0.04720 63  GLY B N   
3150 C CA  . GLY B 69  ? 0.39320 0.29810 0.40210 -0.11390 -0.01970 -0.05500 63  GLY B CA  
3151 C C   . GLY B 69  ? 0.41330 0.32450 0.40840 -0.11760 -0.02040 -0.05350 63  GLY B C   
3152 O O   . GLY B 69  ? 0.44840 0.35870 0.42480 -0.12650 -0.02150 -0.05650 63  GLY B O   
3153 N N   . VAL B 70  ? 0.37710 0.29440 0.38020 -0.11150 -0.02000 -0.04840 64  VAL B N   
3154 C CA  . VAL B 70  ? 0.41840 0.34080 0.40910 -0.11480 -0.02010 -0.04640 64  VAL B CA  
3155 C C   . VAL B 70  ? 0.38320 0.31200 0.36350 -0.11960 -0.02890 -0.04010 64  VAL B C   
3156 O O   . VAL B 70  ? 0.45310 0.38220 0.41500 -0.12700 -0.02960 -0.04000 64  VAL B O   
3157 C CB  . VAL B 70  ? 0.36740 0.29570 0.37150 -0.10680 -0.01910 -0.04120 64  VAL B CB  
3158 C CG1 . VAL B 70  ? 0.35980 0.29450 0.35300 -0.10980 -0.02140 -0.03680 64  VAL B CG1 
3159 C CG2 . VAL B 70  ? 0.36440 0.28630 0.37420 -0.10420 -0.00950 -0.04750 64  VAL B CG2 
3160 N N   . ALA B 71  ? 0.41650 0.35060 0.40780 -0.11580 -0.03530 -0.03430 65  ALA B N   
3161 C CA  . ALA B 71  ? 0.41720 0.35750 0.40010 -0.11980 -0.04380 -0.02700 65  ALA B CA  
3162 C C   . ALA B 71  ? 0.44620 0.38180 0.40800 -0.13150 -0.04580 -0.03100 65  ALA B C   
3163 O O   . ALA B 71  ? 0.43430 0.37390 0.38310 -0.13730 -0.05230 -0.02480 65  ALA B O   
3164 C CB  . ALA B 71  ? 0.36600 0.31150 0.36360 -0.11470 -0.04820 -0.02180 65  ALA B CB  
3165 N N   . GLY B 72  ? 0.40840 0.33530 0.36610 -0.13540 -0.04020 -0.04100 66  GLY B N   
3166 C CA  . GLY B 72  ? 0.46750 0.38950 0.40390 -0.14720 -0.04090 -0.04610 66  GLY B CA  
3167 C C   . GLY B 72  ? 0.49130 0.41200 0.40490 -0.15550 -0.03840 -0.04740 66  GLY B C   
3168 O O   . GLY B 72  ? 0.51220 0.43200 0.40610 -0.16610 -0.04170 -0.04780 66  GLY B O   
3169 N N   . TYR B 73  ? 0.51330 0.43430 0.42900 -0.15150 -0.03260 -0.04770 67  TYR B N   
3170 C CA  . TYR B 73  ? 0.50920 0.42860 0.40360 -0.15990 -0.02840 -0.04980 67  TYR B CA  
3171 C C   . TYR B 73  ? 0.45240 0.37900 0.33570 -0.16470 -0.03820 -0.03840 67  TYR B C   
3172 O O   . TYR B 73  ? 0.48170 0.40690 0.34430 -0.17400 -0.03610 -0.03890 67  TYR B O   
3173 C CB  . TYR B 73  ? 0.46120 0.37960 0.36330 -0.15430 -0.01910 -0.05330 67  TYR B CB  
3174 C CG  . TYR B 73  ? 0.48120 0.39130 0.39100 -0.15130 -0.00790 -0.06470 67  TYR B CG  
3175 C CD1 . TYR B 73  ? 0.49940 0.40070 0.39330 -0.15970 0.00010  -0.07560 67  TYR B CD1 
3176 C CD2 . TYR B 73  ? 0.43690 0.34760 0.36990 -0.14020 -0.00490 -0.06420 67  TYR B CD2 
3177 C CE1 . TYR B 73  ? 0.57230 0.46510 0.47480 -0.15640 0.01140  -0.08590 67  TYR B CE1 
3178 C CE2 . TYR B 73  ? 0.44370 0.34620 0.38480 -0.13720 0.00550  -0.07350 67  TYR B CE2 
3179 C CZ  . TYR B 73  ? 0.52960 0.42300 0.45630 -0.14490 0.01390  -0.08440 67  TYR B CZ  
3180 O OH  . TYR B 73  ? 0.58910 0.47390 0.52560 -0.14120 0.02540  -0.09370 67  TYR B OH  
3181 N N   . GLY B 74  ? 0.48190 0.41590 0.37930 -0.15850 -0.04790 -0.02770 68  GLY B N   
3182 C CA  . GLY B 74  ? 0.45690 0.39710 0.34620 -0.16230 -0.05730 -0.01560 68  GLY B CA  
3183 C C   . GLY B 74  ? 0.45080 0.39360 0.34020 -0.16000 -0.05580 -0.01060 68  GLY B C   
3184 O O   . GLY B 74  ? 0.47350 0.41810 0.34810 -0.16740 -0.06080 -0.00320 68  GLY B O   
3185 N N   . PHE B 75  ? 0.43910 0.38220 0.34480 -0.15040 -0.04930 -0.01380 69  PHE B N   
3186 C CA  . PHE B 75  ? 0.46590 0.41220 0.37430 -0.14750 -0.04850 -0.00840 69  PHE B CA  
3187 C C   . PHE B 75  ? 0.46180 0.41450 0.37760 -0.14410 -0.05920 0.00500  69  PHE B C   
3188 O O   . PHE B 75  ? 0.41760 0.37350 0.34820 -0.13740 -0.06360 0.00850  69  PHE B O   
3189 C CB  . PHE B 75  ? 0.40780 0.35440 0.33520 -0.13720 -0.04060 -0.01360 69  PHE B CB  
3190 C CG  . PHE B 75  ? 0.40680 0.34710 0.32850 -0.14040 -0.02920 -0.02580 69  PHE B CG  
3191 C CD1 . PHE B 75  ? 0.39480 0.33150 0.29540 -0.15080 -0.02370 -0.03010 69  PHE B CD1 
3192 C CD2 . PHE B 75  ? 0.41490 0.35250 0.35260 -0.13320 -0.02330 -0.03270 69  PHE B CD2 
3193 C CE1 . PHE B 75  ? 0.41640 0.34710 0.31280 -0.15340 -0.01120 -0.04220 69  PHE B CE1 
3194 C CE2 . PHE B 75  ? 0.44190 0.37300 0.37640 -0.13550 -0.01190 -0.04370 69  PHE B CE2 
3195 C CZ  . PHE B 75  ? 0.45210 0.38000 0.36630 -0.14540 -0.00510 -0.04910 69  PHE B CZ  
3196 N N   . ASP B 76  ? 0.41240 0.36660 0.31770 -0.14930 -0.06290 0.01280  70  ASP B N   
3197 C CA  . ASP B 76  ? 0.43600 0.39520 0.34890 -0.14640 -0.07270 0.02620  70  ASP B CA  
3198 C C   . ASP B 76  ? 0.44280 0.40450 0.37140 -0.13700 -0.06970 0.02890  70  ASP B C   
3199 O O   . ASP B 76  ? 0.39960 0.36010 0.33330 -0.13300 -0.06070 0.02090  70  ASP B O   
3200 C CB  . ASP B 76  ? 0.44780 0.40670 0.34020 -0.15890 -0.08040 0.03520  70  ASP B CB  
3201 C CG  . ASP B 76  ? 0.53050 0.48660 0.40620 -0.16670 -0.07540 0.03360  70  ASP B CG  
3202 O OD1 . ASP B 76  ? 0.43950 0.39530 0.32370 -0.16090 -0.06770 0.02900  70  ASP B OD1 
3203 O OD2 . ASP B 76  ? 0.59710 0.55160 0.45060 -0.17960 -0.07900 0.03740  70  ASP B OD2 
3204 N N   . ASP B 77  ? 0.41910 0.38430 0.35600 -0.13370 -0.07720 0.04040  71  ASP B N   
3205 C CA  . ASP B 77  ? 0.40070 0.36820 0.35420 -0.12390 -0.07440 0.04240  71  ASP B CA  
3206 C C   . ASP B 77  ? 0.38020 0.34590 0.32630 -0.12710 -0.06810 0.03920  71  ASP B C   
3207 O O   . ASP B 77  ? 0.32820 0.29490 0.28630 -0.11960 -0.06110 0.03440  71  ASP B O   
3208 C CB  . ASP B 77  ? 0.40940 0.37990 0.37250 -0.12090 -0.08340 0.05530  71  ASP B CB  
3209 C CG  . ASP B 77  ? 0.50520 0.47850 0.48430 -0.11300 -0.08630 0.05710  71  ASP B CG  
3210 O OD1 . ASP B 77  ? 0.49590 0.46900 0.47800 -0.11010 -0.08170 0.04880  71  ASP B OD1 
3211 O OD2 . ASP B 77  ? 0.56360 0.53950 0.55330 -0.10980 -0.09290 0.06710  71  ASP B OD2 
3212 N N   . ALA B 78  ? 0.40600 0.36930 0.33210 -0.13890 -0.07030 0.04210  72  ALA B N   
3213 C CA  . ALA B 78  ? 0.35510 0.31680 0.27370 -0.14290 -0.06360 0.03920  72  ALA B CA  
3214 C C   . ALA B 78  ? 0.38030 0.34010 0.29820 -0.14210 -0.05210 0.02550  72  ALA B C   
3215 O O   . ALA B 78  ? 0.33690 0.29740 0.26120 -0.13890 -0.04460 0.02150  72  ALA B O   
3216 C CB  . ALA B 78  ? 0.36950 0.32900 0.26440 -0.15720 -0.06820 0.04550  72  ALA B CB  
3217 N N   . ASP B 79  ? 0.37840 0.33560 0.28910 -0.14530 -0.05050 0.01840  73  ASP B N   
3218 C CA  . ASP B 79  ? 0.41760 0.37240 0.33070 -0.14370 -0.03980 0.00560  73  ASP B CA  
3219 C C   . ASP B 79  ? 0.38220 0.34050 0.32030 -0.13040 -0.03630 0.00350  73  ASP B C   
3220 O O   . ASP B 79  ? 0.33030 0.28860 0.27430 -0.12820 -0.02780 -0.00300 73  ASP B O   
3221 C CB  . ASP B 79  ? 0.40540 0.35620 0.31030 -0.14770 -0.03920 -0.00130 73  ASP B CB  
3222 C CG  . ASP B 79  ? 0.47300 0.42000 0.35070 -0.16210 -0.04100 -0.00140 73  ASP B CG  
3223 O OD1 . ASP B 79  ? 0.46830 0.41420 0.33030 -0.17070 -0.03850 -0.00020 73  ASP B OD1 
3224 O OD2 . ASP B 79  ? 0.47510 0.42030 0.34660 -0.16530 -0.04470 -0.00290 73  ASP B OD2 
3225 N N   . ILE B 80  ? 0.40040 0.36180 0.35270 -0.12210 -0.04270 0.00910  74  ILE B N   
3226 C CA  . ILE B 80  ? 0.34350 0.30820 0.31720 -0.11040 -0.03970 0.00730  74  ILE B CA  
3227 C C   . ILE B 80  ? 0.34510 0.31300 0.32640 -0.10640 -0.03750 0.01040  74  ILE B C   
3228 O O   . ILE B 80  ? 0.30320 0.27320 0.29650 -0.10070 -0.03160 0.00580  74  ILE B O   
3229 C CB  . ILE B 80  ? 0.31090 0.27780 0.29470 -0.10430 -0.04590 0.01190  74  ILE B CB  
3230 C CG1 . ILE B 80  ? 0.35140 0.31520 0.32980 -0.10800 -0.04660 0.00720  74  ILE B CG1 
3231 C CG2 . ILE B 80  ? 0.27400 0.24460 0.27680 -0.09320 -0.04280 0.01110  74  ILE B CG2 
3232 C CD1 . ILE B 80  ? 0.45850 0.42450 0.44470 -0.10400 -0.05270 0.01200  74  ILE B CD1 
3233 N N   . ALA B 81  ? 0.29420 0.26230 0.26900 -0.10980 -0.04230 0.01840  75  ALA B N   
3234 C CA  . ALA B 81  ? 0.31370 0.28370 0.29410 -0.10740 -0.03940 0.02050  75  ALA B CA  
3235 C C   . ALA B 81  ? 0.32770 0.29730 0.30360 -0.11170 -0.03080 0.01340  75  ALA B C   
3236 O O   . ALA B 81  ? 0.33530 0.30790 0.32250 -0.10680 -0.02590 0.01110  75  ALA B O   
3237 C CB  . ALA B 81  ? 0.32370 0.29270 0.29680 -0.11200 -0.04600 0.03060  75  ALA B CB  
3238 N N   . LEU B 82  ? 0.32300 0.28900 0.28210 -0.12130 -0.02820 0.00910  76  LEU B N   
3239 C CA  . LEU B 82  ? 0.31750 0.28310 0.27260 -0.12570 -0.01840 0.00150  76  LEU B CA  
3240 C C   . LEU B 82  ? 0.33470 0.30220 0.30530 -0.11880 -0.01210 -0.00660 76  LEU B C   
3241 O O   . LEU B 82  ? 0.36440 0.33480 0.34170 -0.11810 -0.00460 -0.01090 76  LEU B O   
3242 C CB  . LEU B 82  ? 0.36050 0.32110 0.29190 -0.13860 -0.01560 -0.00210 76  LEU B CB  
3243 C CG  . LEU B 82  ? 0.35950 0.31970 0.28250 -0.14580 -0.00480 -0.00800 76  LEU B CG  
3244 C CD1 . LEU B 82  ? 0.32940 0.29140 0.24830 -0.14900 -0.00650 0.00000  76  LEU B CD1 
3245 C CD2 . LEU B 82  ? 0.40330 0.35750 0.30310 -0.15820 0.00030  -0.01530 76  LEU B CD2 
3246 N N   . MET B 83  ? 0.27870 0.24500 0.25560 -0.11420 -0.01510 -0.00820 77  MET B N   
3247 C CA  . MET B 83  ? 0.33450 0.30270 0.32830 -0.10700 -0.01090 -0.01350 77  MET B CA  
3248 C C   . MET B 83  ? 0.33140 0.30590 0.34280 -0.09830 -0.01210 -0.00970 77  MET B C   
3249 O O   . MET B 83  ? 0.35360 0.33110 0.37800 -0.09420 -0.00800 -0.01330 77  MET B O   
3250 C CB  . MET B 83  ? 0.30140 0.26680 0.29890 -0.10370 -0.01480 -0.01460 77  MET B CB  
3251 C CG  . MET B 83  ? 0.31260 0.27130 0.29470 -0.11160 -0.01280 -0.02030 77  MET B CG  
3252 S SD  . MET B 83  ? 0.39110 0.34740 0.38160 -0.10650 -0.01740 -0.02080 77  MET B SD  
3253 C CE  . MET B 83  ? 0.35710 0.30640 0.32410 -0.11800 -0.01780 -0.02510 77  MET B CE  
3254 N N   . CYS B 84  ? 0.30120 0.27750 0.31310 -0.09580 -0.01740 -0.00270 78  CYS B N   
3255 C CA  . CYS B 84  ? 0.30760 0.28890 0.33340 -0.08850 -0.01750 -0.00040 78  CYS B CA  
3256 C C   . CYS B 84  ? 0.30800 0.29150 0.33290 -0.09130 -0.01410 0.00040  78  CYS B C   
3257 O O   . CYS B 84  ? 0.31640 0.30320 0.35050 -0.08650 -0.01440 0.00230  78  CYS B O   
3258 C CB  . CYS B 84  ? 0.28840 0.26960 0.31570 -0.08390 -0.02340 0.00570  78  CYS B CB  
3259 S SG  . CYS B 84  ? 0.31370 0.29370 0.34360 -0.07990 -0.02710 0.00570  78  CYS B SG  
3260 N N   . ALA B 85  ? 0.30550 0.28720 0.31870 -0.09960 -0.01000 -0.00170 79  ALA B N   
3261 C CA  . ALA B 85  ? 0.31170 0.29430 0.31990 -0.10400 -0.00740 0.00060  79  ALA B CA  
3262 C C   . ALA B 85  ? 0.38210 0.37010 0.39900 -0.10420 0.00030  -0.00430 79  ALA B C   
3263 O O   . ALA B 85  ? 0.37210 0.36240 0.39450 -0.10380 0.00540  -0.01050 79  ALA B O   
3264 C CB  . ALA B 85  ? 0.32780 0.30540 0.31500 -0.11470 -0.00700 0.00190  79  ALA B CB  
3265 N N   . SER B 86  ? 0.35710 0.34730 0.37610 -0.10490 0.00130  -0.00130 80  SER B N   
3266 C CA  . SER B 86  ? 0.32680 0.32130 0.34680 -0.10920 0.00920  -0.00460 80  SER B CA  
3267 C C   . SER B 86  ? 0.31360 0.30370 0.31730 -0.11750 0.01020  -0.00070 80  SER B C   
3268 O O   . SER B 86  ? 0.36470 0.35530 0.37120 -0.11730 0.00940  0.00360  80  SER B O   
3269 C CB  . SER B 86  ? 0.32220 0.32380 0.35980 -0.10330 0.00930  -0.00410 80  SER B CB  
3270 O OG  . SER B 86  ? 0.33540 0.34140 0.38650 -0.09650 0.00750  -0.00640 80  SER B OG  
3271 N N   . HIS B 87  ? 0.32610 0.31120 0.31200 -0.12540 0.01200  -0.00210 81  HIS B N   
3272 C CA  . HIS B 87  ? 0.33930 0.31950 0.30730 -0.13390 0.01060  0.00350  81  HIS B CA  
3273 C C   . HIS B 87  ? 0.33120 0.31400 0.29570 -0.13980 0.01970  0.00160  81  HIS B C   
3274 O O   . HIS B 87  ? 0.27200 0.26080 0.24730 -0.13830 0.02810  -0.00510 81  HIS B O   
3275 C CB  . HIS B 87  ? 0.33040 0.30460 0.27830 -0.14170 0.00840  0.00310  81  HIS B CB  
3276 C CG  . HIS B 87  ? 0.36780 0.34160 0.30780 -0.14790 0.01850  -0.00720 81  HIS B CG  
3277 N ND1 . HIS B 87  ? 0.33860 0.31380 0.27190 -0.15490 0.02970  -0.01200 81  HIS B ND1 
3278 C CD2 . HIS B 87  ? 0.36580 0.33710 0.30370 -0.14810 0.02030  -0.01420 81  HIS B CD2 
3279 C CE1 . HIS B 87  ? 0.32130 0.29490 0.24950 -0.15910 0.03880  -0.02210 81  HIS B CE1 
3280 N NE2 . HIS B 87  ? 0.35250 0.32320 0.28330 -0.15520 0.03310  -0.02380 81  HIS B NE2 
3281 N N   . SER B 88  ? 0.33330 0.31200 0.28370 -0.14650 0.01770  0.00830  82  SER B N   
3282 C CA  . SER B 88  ? 0.34610 0.32640 0.29280 -0.15200 0.02520  0.00850  82  SER B CA  
3283 C C   . SER B 88  ? 0.35840 0.33720 0.28610 -0.16270 0.03480  0.00270  82  SER B C   
3284 O O   . SER B 88  ? 0.40610 0.38580 0.32770 -0.16830 0.04140  0.00330  82  SER B O   
3285 C CB  . SER B 88  ? 0.32500 0.30090 0.26630 -0.15380 0.01880  0.01900  82  SER B CB  
3286 O OG  . SER B 88  ? 0.32380 0.30160 0.28490 -0.14450 0.01460  0.02190  82  SER B OG  
3287 N N   . SER B 89  ? 0.33670 0.31300 0.25510 -0.16590 0.03630  -0.00320 83  SER B N   
3288 C CA  . SER B 89  ? 0.35710 0.33020 0.25460 -0.17720 0.04610  -0.01000 83  SER B CA  
3289 C C   . SER B 89  ? 0.39300 0.36090 0.26570 -0.18790 0.04340  -0.00250 83  SER B C   
3290 O O   . SER B 89  ? 0.41410 0.38110 0.27160 -0.19670 0.05330  -0.00670 83  SER B O   
3291 C CB  . SER B 89  ? 0.39840 0.37760 0.30600 -0.17690 0.06120  -0.01980 83  SER B CB  
3292 O OG  . SER B 89  ? 0.38200 0.36840 0.31720 -0.16560 0.06140  -0.02310 83  SER B OG  
3293 N N   . GLU B 90  ? 0.41280 0.37750 0.28230 -0.18670 0.03010  0.00890  84  GLU B N   
3294 C CA  . GLU B 90  ? 0.41720 0.37680 0.26200 -0.19730 0.02510  0.01700  84  GLU B CA  
3295 C C   . GLU B 90  ? 0.46870 0.42370 0.28880 -0.20840 0.02680  0.01150  84  GLU B C   
3296 O O   . GLU B 90  ? 0.46230 0.41700 0.28640 -0.20660 0.02920  0.00310  84  GLU B O   
3297 C CB  . GLU B 90  ? 0.41390 0.37170 0.26440 -0.19260 0.01010  0.03040  84  GLU B CB  
3298 C CG  . GLU B 90  ? 0.45230 0.41280 0.32490 -0.18320 0.00980  0.03520  84  GLU B CG  
3299 C CD  . GLU B 90  ? 0.50570 0.46490 0.39210 -0.17480 -0.00270 0.04500  84  GLU B CD  
3300 O OE1 . GLU B 90  ? 0.48190 0.43870 0.36050 -0.17660 -0.01260 0.05050  84  GLU B OE1 
3301 O OE2 . GLU B 90  ? 0.48330 0.44400 0.38900 -0.16670 -0.00220 0.04690  84  GLU B OE2 
3302 N N   . ASP B 91  ? 0.51220 0.46350 0.30610 -0.22020 0.02550  0.01600  85  ASP B N   
3303 C CA  . ASP B 91  ? 0.54340 0.49010 0.31140 -0.23200 0.02800  0.00940  85  ASP B CA  
3304 C C   . ASP B 91  ? 0.51060 0.45510 0.27820 -0.23150 0.01550  0.01270  85  ASP B C   
3305 O O   . ASP B 91  ? 0.48180 0.42300 0.23870 -0.23740 0.01950  0.00330  85  ASP B O   
3306 C CB  . ASP B 91  ? 0.55410 0.49780 0.29380 -0.24460 0.02750  0.01370  85  ASP B CB  
3307 C CG  . ASP B 91  ? 0.62090 0.56590 0.35750 -0.24740 0.04390  0.00550  85  ASP B CG  
3308 O OD1 . ASP B 91  ? 0.64870 0.59740 0.40420 -0.24030 0.05600  -0.00390 85  ASP B OD1 
3309 O OD2 . ASP B 91  ? 0.70970 0.65280 0.42670 -0.25640 0.04440  0.00890  85  ASP B OD2 
3310 N N   . ARG B 92  ? 0.48110 0.42730 0.26240 -0.22390 0.00120  0.02500  86  ARG B N   
3311 C CA  . ARG B 92  ? 0.48720 0.43240 0.27060 -0.22250 -0.01030 0.02750  86  ARG B CA  
3312 C C   . ARG B 92  ? 0.49070 0.43740 0.29580 -0.21170 -0.00530 0.01660  86  ARG B C   
3313 O O   . ARG B 92  ? 0.49530 0.44010 0.29750 -0.21260 -0.00930 0.01230  86  ARG B O   
3314 C CB  . ARG B 92  ? 0.51220 0.45940 0.30700 -0.21610 -0.02600 0.04300  86  ARG B CB  
3315 C CG  . ARG B 92  ? 0.51650 0.46730 0.34060 -0.20110 -0.02470 0.04550  86  ARG B CG  
3316 C CD  . ARG B 92  ? 0.53630 0.48820 0.37230 -0.19500 -0.03830 0.05970  86  ARG B CD  
3317 N NE  . ARG B 92  ? 0.52720 0.48080 0.38570 -0.18390 -0.03470 0.06130  86  ARG B NE  
3318 C CZ  . ARG B 92  ? 0.50880 0.46270 0.38230 -0.17670 -0.04240 0.07130  86  ARG B CZ  
3319 N NH1 . ARG B 92  ? 0.49940 0.45330 0.37110 -0.17800 -0.05500 0.08150  86  ARG B NH1 
3320 N NH2 . ARG B 92  ? 0.47600 0.43050 0.36760 -0.16830 -0.03720 0.07060  86  ARG B NH2 
3321 N N   . HIS B 93  ? 0.41700 0.36770 0.24430 -0.20110 0.00320  0.01180  87  HIS B N   
3322 C CA  . HIS B 93  ? 0.43840 0.39130 0.28600 -0.19090 0.00820  0.00170  87  HIS B CA  
3323 C C   . HIS B 93  ? 0.45820 0.40760 0.29380 -0.19860 0.02050  -0.01260 87  HIS B C   
3324 O O   . HIS B 93  ? 0.46420 0.41170 0.30470 -0.19510 0.02020  -0.01980 87  HIS B O   
3325 C CB  . HIS B 93  ? 0.41420 0.37310 0.28710 -0.17940 0.01340  0.00080  87  HIS B CB  
3326 C CG  . HIS B 93  ? 0.41770 0.37890 0.30420 -0.17120 0.00350  0.01230  87  HIS B CG  
3327 N ND1 . HIS B 93  ? 0.41630 0.37960 0.30780 -0.17030 0.00620  0.01690  87  HIS B ND1 
3328 C CD2 . HIS B 93  ? 0.39720 0.35880 0.29500 -0.16320 -0.00760 0.01920  87  HIS B CD2 
3329 C CE1 . HIS B 93  ? 0.41030 0.37420 0.31490 -0.16250 -0.00280 0.02550  87  HIS B CE1 
3330 N NE2 . HIS B 93  ? 0.34600 0.30900 0.25450 -0.15810 -0.01090 0.02710  87  HIS B NE2 
3331 N N   . ILE B 94  ? 0.46280 0.41130 0.28410 -0.20830 0.03250  -0.01720 88  ILE B N   
3332 C CA  . ILE B 94  ? 0.48440 0.42930 0.29310 -0.21390 0.04600  -0.03160 88  ILE B CA  
3333 C C   . ILE B 94  ? 0.52340 0.46130 0.30760 -0.22310 0.03960  -0.03370 88  ILE B C   
3334 O O   . ILE B 94  ? 0.48910 0.42290 0.27230 -0.22240 0.04500  -0.04550 88  ILE B O   
3335 C CB  . ILE B 94  ? 0.48840 0.43420 0.28430 -0.22200 0.05970  -0.03470 88  ILE B CB  
3336 C CG1 . ILE B 94  ? 0.47780 0.43150 0.29950 -0.21360 0.06620  -0.03320 88  ILE B CG1 
3337 C CG2 . ILE B 94  ? 0.50260 0.44390 0.28440 -0.22800 0.07490  -0.05040 88  ILE B CG2 
3338 C CD1 . ILE B 94  ? 0.47760 0.43300 0.28770 -0.22000 0.07750  -0.03440 88  ILE B CD1 
3339 N N   . ALA B 95  ? 0.49390 0.43050 0.25900 -0.23180 0.02750  -0.02180 89  ALA B N   
3340 C CA  . ALA B 95  ? 0.52480 0.45620 0.26650 -0.24150 0.01960  -0.02270 89  ALA B CA  
3341 C C   . ALA B 95  ? 0.54760 0.47900 0.30660 -0.23270 0.01040  -0.02390 89  ALA B C   
3342 O O   . ALA B 95  ? 0.50100 0.42850 0.25190 -0.23380 0.01260  -0.03220 89  ALA B O   
3343 C CB  . ALA B 95  ? 0.51490 0.44680 0.23620 -0.25180 0.00670  -0.00720 89  ALA B CB  
3344 N N   . ARG B 96  ? 0.49640 0.43320 0.28150 -0.21920 0.00190  -0.01420 90  ARG B N   
3345 C CA  . ARG B 96  ? 0.46480 0.40290 0.26690 -0.20760 -0.00570 -0.01370 90  ARG B CA  
3346 C C   . ARG B 96  ? 0.45080 0.38720 0.26710 -0.19990 0.00590  -0.02800 90  ARG B C   
3347 O O   . ARG B 96  ? 0.45710 0.39140 0.27670 -0.19600 0.00340  -0.03180 90  ARG B O   
3348 C CB  . ARG B 96  ? 0.42310 0.36710 0.24900 -0.19520 -0.01600 -0.00130 90  ARG B CB  
3349 C CG  . ARG B 96  ? 0.43150 0.37710 0.27440 -0.18400 -0.02360 -0.00010 90  ARG B CG  
3350 C CD  . ARG B 96  ? 0.41570 0.36620 0.27670 -0.17450 -0.03440 0.01270  90  ARG B CD  
3351 N NE  . ARG B 96  ? 0.48450 0.43500 0.33080 -0.18320 -0.04530 0.02530  90  ARG B NE  
3352 C CZ  . ARG B 96  ? 0.52270 0.47290 0.35980 -0.18790 -0.05500 0.03070  90  ARG B CZ  
3353 N NH1 . ARG B 96  ? 0.48820 0.43750 0.32810 -0.18480 -0.05440 0.02390  90  ARG B NH1 
3354 N NH2 . ARG B 96  ? 0.46710 0.41830 0.29350 -0.19560 -0.06580 0.04410  90  ARG B NH2 
3355 N N   . THR B 97  ? 0.44560 0.38310 0.27160 -0.19790 0.01860  -0.03530 91  THR B N   
3356 C CA  . THR B 97  ? 0.43580 0.37130 0.27530 -0.19190 0.03050  -0.04880 91  THR B CA  
3357 C C   . THR B 97  ? 0.48830 0.41550 0.30610 -0.20140 0.03830  -0.06080 91  THR B C   
3358 O O   . THR B 97  ? 0.47300 0.39690 0.29930 -0.19570 0.04070  -0.06790 91  THR B O   
3359 C CB  . THR B 97  ? 0.45450 0.39420 0.30850 -0.18880 0.04300  -0.05320 91  THR B CB  
3360 O OG1 . THR B 97  ? 0.40850 0.35600 0.28290 -0.17910 0.03550  -0.04240 91  THR B OG1 
3361 C CG2 . THR B 97  ? 0.40900 0.34780 0.28060 -0.18090 0.05480  -0.06550 91  THR B CG2 
3362 N N   . ARG B 98  ? 0.47810 0.40180 0.26740 -0.21610 0.04270  -0.06290 92  ARG B N   
3363 C CA  . ARG B 98  ? 0.50210 0.41840 0.26910 -0.22500 0.05010  -0.07350 92  ARG B CA  
3364 C C   . ARG B 98  ? 0.54310 0.45820 0.30440 -0.22470 0.03710  -0.06750 92  ARG B C   
3365 O O   . ARG B 98  ? 0.55510 0.46510 0.31530 -0.22420 0.04210  -0.07660 92  ARG B O   
3366 C CB  . ARG B 98  ? 0.51940 0.43340 0.25650 -0.24040 0.05710  -0.07520 92  ARG B CB  
3367 C CG  . ARG B 98  ? 0.51750 0.43290 0.26260 -0.23890 0.07410  -0.08350 92  ARG B CG  
3368 C CD  . ARG B 98  ? 0.60710 0.52180 0.32410 -0.25240 0.08190  -0.08330 92  ARG B CD  
3369 N NE  . ARG B 98  ? 0.56930 0.48600 0.29650 -0.24930 0.10170  -0.09310 92  ARG B NE  
3370 C CZ  . ARG B 98  ? 0.72410 0.64510 0.44480 -0.25390 0.10880  -0.08920 92  ARG B CZ  
3371 N NH1 . ARG B 98  ? 0.70860 0.63160 0.41200 -0.26170 0.09800  -0.07510 92  ARG B NH1 
3372 N NH2 . ARG B 98  ? 0.71310 0.63690 0.44680 -0.25030 0.12740  -0.09880 92  ARG B NH2 
3373 N N   . ALA B 99  ? 0.51170 0.43160 0.27210 -0.22450 0.02060  -0.05230 93  ALA B N   
3374 C CA  . ALA B 99  ? 0.49140 0.41170 0.25130 -0.22310 0.00800  -0.04610 93  ALA B CA  
3375 C C   . ALA B 99  ? 0.52490 0.44490 0.31000 -0.20970 0.00830  -0.05120 93  ALA B C   
3376 O O   . ALA B 99  ? 0.53720 0.45380 0.31950 -0.21050 0.00650  -0.05500 93  ALA B O   
3377 C CB  . ALA B 99  ? 0.48150 0.40800 0.24320 -0.22270 -0.00860 -0.02840 93  ALA B CB  
3378 N N   . MET B 100 ? 0.48270 0.40640 0.29320 -0.19770 0.00990  -0.05040 94  MET B N   
3379 C CA  . MET B 100 ? 0.49080 0.41460 0.32590 -0.18500 0.00960  -0.05350 94  MET B CA  
3380 C C   . MET B 100 ? 0.50700 0.42340 0.34230 -0.18540 0.02390  -0.06900 94  MET B C   
3381 O O   . MET B 100 ? 0.50080 0.41390 0.34410 -0.18110 0.02300  -0.07280 94  MET B O   
3382 C CB  . MET B 100 ? 0.42300 0.35320 0.28370 -0.17300 0.00790  -0.04790 94  MET B CB  
3383 C CG  . MET B 100 ? 0.41840 0.35490 0.28240 -0.17060 -0.00570 -0.03290 94  MET B CG  
3384 S SD  . MET B 100 ? 0.45520 0.39910 0.34660 -0.15770 -0.00630 -0.02670 94  MET B SD  
3385 C CE  . MET B 100 ? 0.36340 0.30770 0.28080 -0.14450 -0.00430 -0.03200 94  MET B CE  
3386 N N   . LEU B 101 ? 0.49930 0.41290 0.32670 -0.19090 0.03800  -0.07810 95  LEU B N   
3387 C CA  . LEU B 101 ? 0.47190 0.37800 0.29930 -0.19180 0.05330  -0.09320 95  LEU B CA  
3388 C C   . LEU B 101 ? 0.55530 0.45490 0.36250 -0.20030 0.05230  -0.09740 95  LEU B C   
3389 O O   . LEU B 101 ? 0.54550 0.43930 0.36070 -0.19660 0.05750  -0.10560 95  LEU B O   
3390 C CB  . LEU B 101 ? 0.47120 0.37590 0.29140 -0.19760 0.06910  -0.10200 95  LEU B CB  
3391 C CG  . LEU B 101 ? 0.50820 0.41770 0.35400 -0.18860 0.07620  -0.10350 95  LEU B CG  
3392 C CD1 . LEU B 101 ? 0.50820 0.41740 0.34290 -0.19720 0.09050  -0.11070 95  LEU B CD1 
3393 C CD2 . LEU B 101 ? 0.44610 0.35270 0.31800 -0.17700 0.08350  -0.11120 95  LEU B CD2 
3394 N N   . SER B 102 ? 0.50460 0.40530 0.28640 -0.21200 0.04540  -0.09130 96  SER B N   
3395 C CA  . SER B 102 ? 0.55130 0.44700 0.31460 -0.22090 0.04310  -0.09420 96  SER B CA  
3396 C C   . SER B 102 ? 0.58860 0.48540 0.36610 -0.21350 0.03100  -0.08930 96  SER B C   
3397 O O   . SER B 102 ? 0.53720 0.42790 0.31230 -0.21530 0.03420  -0.09700 96  SER B O   
3398 C CB  . SER B 102 ? 0.55990 0.45780 0.29520 -0.23480 0.03630  -0.08630 96  SER B CB  
3399 O OG  . SER B 102 ? 0.66540 0.56190 0.38750 -0.24220 0.04870  -0.09140 96  SER B OG  
3400 N N   . LYS B 103 ? 0.56480 0.46900 0.35840 -0.20500 0.01800  -0.07690 97  LYS B N   
3401 C CA  . LYS B 103 ? 0.54330 0.44910 0.35060 -0.19850 0.00700  -0.07200 97  LYS B CA  
3402 C C   . LYS B 103 ? 0.55120 0.45140 0.37740 -0.18980 0.01490  -0.08190 97  LYS B C   
3403 O O   . LYS B 103 ? 0.61130 0.50920 0.44190 -0.18860 0.01000  -0.08260 97  LYS B O   
3404 C CB  . LYS B 103 ? 0.53270 0.44730 0.35660 -0.18990 -0.00590 -0.05790 97  LYS B CB  
3405 C CG  . LYS B 103 ? 0.55790 0.47760 0.36590 -0.19780 -0.01630 -0.04580 97  LYS B CG  
3406 C CD  . LYS B 103 ? 0.50560 0.43320 0.33320 -0.18810 -0.02850 -0.03250 97  LYS B CD  
3407 C CE  . LYS B 103 ? 0.52290 0.45500 0.33690 -0.19560 -0.03960 -0.01930 97  LYS B CE  
3408 N NZ  . LYS B 103 ? 0.51980 0.45880 0.35470 -0.18540 -0.04930 -0.00710 97  LYS B NZ  
3409 N N   . ILE B 104 ? 0.47680 0.37480 0.31540 -0.18390 0.02700  -0.08900 98  ILE B N   
3410 C CA  . ILE B 104 ? 0.48740 0.37950 0.34480 -0.17570 0.03500  -0.09760 98  ILE B CA  
3411 C C   . ILE B 104 ? 0.53630 0.41900 0.38330 -0.18180 0.05170  -0.11240 98  ILE B C   
3412 O O   . ILE B 104 ? 0.50790 0.38470 0.37090 -0.17520 0.06090  -0.12030 98  ILE B O   
3413 C CB  . ILE B 104 ? 0.51810 0.41470 0.40260 -0.16280 0.03650  -0.09430 98  ILE B CB  
3414 C CG1 . ILE B 104 ? 0.48560 0.38310 0.36950 -0.16400 0.04870  -0.09940 98  ILE B CG1 
3415 C CG2 . ILE B 104 ? 0.44720 0.35310 0.34190 -0.15690 0.02080  -0.07980 98  ILE B CG2 
3416 C CD1 . ILE B 104 ? 0.45350 0.35520 0.36510 -0.15210 0.05210  -0.09790 98  ILE B CD1 
3417 N N   . LYS B 105 ? 0.51360 0.39460 0.33440 -0.19430 0.05610  -0.11580 99  LYS B N   
3418 C CA  . LYS B 105 ? 0.53050 0.40280 0.33900 -0.20160 0.07280  -0.13000 99  LYS B CA  
3419 C C   . LYS B 105 ? 0.61050 0.48080 0.43750 -0.19390 0.08920  -0.13850 99  LYS B C   
3420 O O   . LYS B 105 ? 0.61360 0.47630 0.44930 -0.19140 0.10220  -0.14950 99  LYS B O   
3421 C CB  . LYS B 105 ? 0.57120 0.43540 0.37650 -0.20430 0.07340  -0.13670 99  LYS B CB  
3422 C CG  . LYS B 105 ? 0.63950 0.50580 0.42450 -0.21410 0.05920  -0.12980 99  LYS B CG  
3423 C CD  . LYS B 105 ? 0.73060 0.58890 0.51140 -0.21820 0.06020  -0.13730 99  LYS B CD  
3424 C CE  . LYS B 105 ? 0.78050 0.64260 0.54170 -0.22850 0.04540  -0.12970 99  LYS B CE  
3425 N NZ  . LYS B 105 ? 0.89280 0.74760 0.64900 -0.23380 0.04530  -0.13700 99  LYS B NZ  
3426 N N   . ALA B 106 ? 0.54320 0.42080 0.37760 -0.19030 0.08880  -0.13330 100 ALA B N   
3427 C CA  . ALA B 106 ? 0.54840 0.42620 0.39960 -0.18450 0.10410  -0.14050 100 ALA B CA  
3428 C C   . ALA B 106 ? 0.58210 0.46230 0.41430 -0.19450 0.11170  -0.14260 100 ALA B C   
3429 O O   . ALA B 106 ? 0.56710 0.44920 0.37420 -0.20520 0.10360  -0.13670 100 ALA B O   
3430 C CB  . ALA B 106 ? 0.50680 0.39160 0.38690 -0.17130 0.09770  -0.13280 100 ALA B CB  
3431 N N   . GLU B 107 ? 0.58690 0.46750 0.43230 -0.19100 0.12740  -0.15050 101 GLU B N   
3432 C CA  . GLU B 107 ? 0.60920 0.49220 0.43890 -0.20000 0.13670  -0.15330 101 GLU B CA  
3433 C C   . GLU B 107 ? 0.59370 0.48450 0.44430 -0.19250 0.13890  -0.15060 101 GLU B C   
3434 O O   . GLU B 107 ? 0.50810 0.40160 0.38780 -0.18020 0.13680  -0.14880 101 GLU B O   
3435 C CB  . GLU B 107 ? 0.60160 0.47770 0.42520 -0.20540 0.15670  -0.16710 101 GLU B CB  
3436 C CG  . GLU B 107 ? 0.71910 0.58590 0.53200 -0.20990 0.15770  -0.17300 101 GLU B CG  
3437 C CD  . GLU B 107 ? 0.89970 0.76390 0.67630 -0.22620 0.15250  -0.17120 101 GLU B CD  
3438 O OE1 . GLU B 107 ? 0.90440 0.77420 0.66350 -0.23390 0.14620  -0.16360 101 GLU B OE1 
3439 O OE2 . GLU B 107 ? 1.00240 0.85890 0.76850 -0.23170 0.15460  -0.17730 101 GLU B OE2 
3440 N N   . GLU B 108 ? 0.56210 0.45680 0.39800 -0.20070 0.14310  -0.14990 102 GLU B N   
3441 C CA  . GLU B 108 ? 0.58380 0.49040 0.44300 -0.19180 0.14420  -0.14310 102 GLU B CA  
3442 C C   . GLU B 108 ? 0.54010 0.44900 0.43130 -0.17960 0.15940  -0.15120 102 GLU B C   
3443 O O   . GLU B 108 ? 0.52930 0.44920 0.45010 -0.16730 0.15580  -0.14330 102 GLU B O   
3444 C CB  . GLU B 108 ? 0.57380 0.48550 0.41390 -0.20140 0.14830  -0.13990 102 GLU B CB  
3445 C CG  . GLU B 108 ? 0.64200 0.55080 0.44870 -0.21450 0.13440  -0.13170 102 GLU B CG  
3446 C CD  . GLU B 108 ? 0.68790 0.60200 0.47740 -0.22350 0.13790  -0.12640 102 GLU B CD  
3447 O OE1 . GLU B 108 ? 0.61310 0.53440 0.41880 -0.21880 0.15020  -0.12820 102 GLU B OE1 
3448 O OE2 . GLU B 108 ? 0.72460 0.63600 0.48460 -0.23560 0.12790  -0.11980 102 GLU B OE2 
3449 N N   . ALA B 109 ? 0.51370 0.41230 0.40020 -0.18300 0.17630  -0.16670 103 ALA B N   
3450 C CA  . ALA B 109 ? 0.50590 0.40620 0.42510 -0.17110 0.19150  -0.17410 103 ALA B CA  
3451 C C   . ALA B 109 ? 0.51720 0.41850 0.46610 -0.15690 0.18240  -0.16870 103 ALA B C   
3452 O O   . ALA B 109 ? 0.48930 0.39590 0.47080 -0.14470 0.19090  -0.17000 103 ALA B O   
3453 C CB  . ALA B 109 ? 0.52950 0.42060 0.44160 -0.17640 0.20780  -0.18620 103 ALA B CB  
3454 N N   . ASP B 110 ? 0.48600 0.38330 0.42540 -0.15840 0.16520  -0.16190 104 ASP B N   
3455 C CA  . ASP B 110 ? 0.47790 0.37610 0.44310 -0.14590 0.15600  -0.15570 104 ASP B CA  
3456 C C   . ASP B 110 ? 0.49370 0.40780 0.47970 -0.13600 0.14330  -0.14040 104 ASP B C   
3457 O O   . ASP B 110 ? 0.40810 0.32540 0.41850 -0.12470 0.13700  -0.13470 104 ASP B O   
3458 C CB  . ASP B 110 ? 0.50610 0.39580 0.45420 -0.15080 0.14290  -0.15330 104 ASP B CB  
3459 C CG  . ASP B 110 ? 0.55970 0.43890 0.49430 -0.15570 0.15220  -0.16300 104 ASP B CG  
3460 O OD1 . ASP B 110 ? 0.56110 0.43620 0.51400 -0.14970 0.16720  -0.17170 104 ASP B OD1 
3461 O OD2 . ASP B 110 ? 0.59580 0.47160 0.50310 -0.16560 0.14400  -0.16110 104 ASP B OD2 
3462 N N   . LEU B 111 ? 0.49070 0.41420 0.46720 -0.14050 0.13970  -0.13380 105 LEU B N   
3463 C CA  . LEU B 111 ? 0.45960 0.39740 0.45480 -0.13230 0.12890  -0.12070 105 LEU B CA  
3464 C C   . LEU B 111 ? 0.49210 0.44040 0.51960 -0.12140 0.13920  -0.12160 105 LEU B C   
3465 O O   . LEU B 111 ? 0.46890 0.41780 0.49920 -0.12330 0.15530  -0.13030 105 LEU B O   
3466 C CB  . LEU B 111 ? 0.44000 0.38310 0.41480 -0.14140 0.12270  -0.11370 105 LEU B CB  
3467 C CG  . LEU B 111 ? 0.46320 0.39850 0.40840 -0.15170 0.11010  -0.10970 105 LEU B CG  
3468 C CD1 . LEU B 111 ? 0.42940 0.36870 0.35370 -0.16170 0.10760  -0.10390 105 LEU B CD1 
3469 C CD2 . LEU B 111 ? 0.38820 0.32560 0.34440 -0.14460 0.09320  -0.09940 105 LEU B CD2 
3470 N N   . ARG B 112 ? 0.46240 0.41990 0.51480 -0.11020 0.12960  -0.11230 106 ARG B N   
3471 C CA  . ARG B 112 ? 0.45890 0.42940 0.54360 -0.09970 0.13570  -0.11040 106 ARG B CA  
3472 C C   . ARG B 112 ? 0.38740 0.37280 0.47850 -0.09880 0.12750  -0.10020 106 ARG B C   
3473 O O   . ARG B 112 ? 0.43690 0.43500 0.55560 -0.08990 0.12770  -0.09590 106 ARG B O   
3474 C CB  . ARG B 112 ? 0.47450 0.44490 0.58450 -0.08760 0.13190  -0.10750 106 ARG B CB  
3475 C CG  . ARG B 112 ? 0.50020 0.45630 0.61150 -0.08670 0.14350  -0.11850 106 ARG B CG  
3476 C CD  . ARG B 112 ? 0.53110 0.48740 0.65040 -0.08760 0.16380  -0.12950 106 ARG B CD  
3477 N NE  . ARG B 112 ? 0.60920 0.54880 0.72420 -0.08910 0.17550  -0.14170 106 ARG B NE  
3478 C CZ  . ARG B 112 ? 0.57820 0.50490 0.66500 -0.10100 0.18460  -0.15330 106 ARG B CZ  
3479 N NH1 . ARG B 112 ? 0.57760 0.50670 0.63900 -0.11220 0.18520  -0.15430 106 ARG B NH1 
3480 N NH2 . ARG B 112 ? 0.64050 0.55090 0.72360 -0.10230 0.19330  -0.16410 106 ARG B NH2 
3481 N N   . CYS B 113 ? 0.38850 0.37260 0.45560 -0.10780 0.11940  -0.09560 107 CYS B N   
3482 C CA  . CYS B 113 ? 0.42550 0.42150 0.49570 -0.10900 0.11340  -0.08730 107 CYS B CA  
3483 C C   . CYS B 113 ? 0.45700 0.45440 0.51540 -0.11790 0.12550  -0.09240 107 CYS B C   
3484 O O   . CYS B 113 ? 0.45430 0.44180 0.49490 -0.12500 0.13580  -0.10130 107 CYS B O   
3485 C CB  . CYS B 113 ? 0.46080 0.45400 0.51440 -0.11280 0.09720  -0.07810 107 CYS B CB  
3486 S SG  . CYS B 113 ? 0.43900 0.41710 0.45480 -0.12590 0.09530  -0.08110 107 CYS B SG  
3487 N N   . GLY B 114 ? 0.42590 0.43530 0.49370 -0.11810 0.12470  -0.08690 108 GLY B N   
3488 C CA  . GLY B 114 ? 0.42350 0.43640 0.48550 -0.12540 0.13780  -0.09130 108 GLY B CA  
3489 C C   . GLY B 114 ? 0.41510 0.42990 0.46040 -0.13390 0.13060  -0.08350 108 GLY B C   
3490 O O   . GLY B 114 ? 0.38380 0.40130 0.43130 -0.13170 0.11650  -0.07420 108 GLY B O   
3491 N N   . GLY B 115 ? 0.41130 0.42430 0.44040 -0.14380 0.14160  -0.08730 109 GLY B N   
3492 C CA  . GLY B 115 ? 0.39510 0.40900 0.40830 -0.15190 0.13600  -0.07950 109 GLY B CA  
3493 C C   . GLY B 115 ? 0.40700 0.43370 0.44220 -0.14460 0.13050  -0.07260 109 GLY B C   
3494 O O   . GLY B 115 ? 0.39470 0.43190 0.45710 -0.13610 0.13490  -0.07490 109 GLY B O   
3495 N N   . HIS B 116 ? 0.35880 0.38430 0.38190 -0.14820 0.12060  -0.06350 110 HIS B N   
3496 C CA  . HIS B 116 ? 0.40550 0.44120 0.44520 -0.14340 0.11520  -0.05700 110 HIS B CA  
3497 C C   . HIS B 116 ? 0.37580 0.40610 0.39500 -0.15090 0.11020  -0.04970 110 HIS B C   
3498 O O   . HIS B 116 ? 0.39170 0.41120 0.38630 -0.15780 0.10680  -0.04760 110 HIS B O   
3499 C CB  . HIS B 116 ? 0.31230 0.35280 0.36980 -0.13410 0.10220  -0.05150 110 HIS B CB  
3500 C CG  . HIS B 116 ? 0.37630 0.40660 0.41790 -0.13530 0.09000  -0.04610 110 HIS B CG  
3501 N ND1 . HIS B 116 ? 0.40280 0.42740 0.42880 -0.13930 0.08140  -0.03810 110 HIS B ND1 
3502 C CD2 . HIS B 116 ? 0.36190 0.38640 0.40120 -0.13290 0.08530  -0.04750 110 HIS B CD2 
3503 C CE1 . HIS B 116 ? 0.37490 0.39150 0.39080 -0.13870 0.07160  -0.03440 110 HIS B CE1 
3504 N NE2 . HIS B 116 ? 0.38190 0.39820 0.40490 -0.13510 0.07340  -0.04010 110 HIS B NE2 
3505 N N   . PRO B 117 ? 0.38750 0.42480 0.41690 -0.14960 0.10870  -0.04490 111 PRO B N   
3506 C CA  . PRO B 117 ? 0.37390 0.40540 0.38680 -0.15560 0.10300  -0.03690 111 PRO B CA  
3507 C C   . PRO B 117 ? 0.39620 0.42000 0.40080 -0.15390 0.08850  -0.02930 111 PRO B C   
3508 O O   . PRO B 117 ? 0.41880 0.44540 0.43760 -0.14600 0.08070  -0.02810 111 PRO B O   
3509 C CB  . PRO B 117 ? 0.38720 0.42900 0.41950 -0.15240 0.10310  -0.03390 111 PRO B CB  
3510 C CG  . PRO B 117 ? 0.38920 0.44140 0.44010 -0.14890 0.11420  -0.04210 111 PRO B CG  
3511 C CD  . PRO B 117 ? 0.35760 0.40850 0.41310 -0.14400 0.11410  -0.04730 111 PRO B CD  
3512 N N   . SER B 118 ? 0.38400 0.39810 0.36530 -0.16110 0.08500  -0.02390 112 SER B N   
3513 C CA  . SER B 118 ? 0.41150 0.41800 0.38490 -0.15950 0.07170  -0.01640 112 SER B CA  
3514 C C   . SER B 118 ? 0.42070 0.43090 0.41320 -0.15100 0.06250  -0.01070 112 SER B C   
3515 O O   . SER B 118 ? 0.41670 0.43270 0.42130 -0.14980 0.06480  -0.00970 112 SER B O   
3516 C CB  . SER B 118 ? 0.43410 0.43150 0.38280 -0.16830 0.06890  -0.00950 112 SER B CB  
3517 O OG  . SER B 118 ? 0.44780 0.43940 0.39380 -0.16520 0.05570  -0.00130 112 SER B OG  
3518 N N   . LEU B 119 ? 0.35810 0.36450 0.35280 -0.14550 0.05200  -0.00720 113 LEU B N   
3519 C CA  . LEU B 119 ? 0.40120 0.40850 0.41000 -0.13840 0.04330  -0.00170 113 LEU B CA  
3520 C C   . LEU B 119 ? 0.37790 0.37820 0.37820 -0.14170 0.03910  0.00660  113 LEU B C   
3521 O O   . LEU B 119 ? 0.41900 0.41880 0.43070 -0.13670 0.03380  0.01040  113 LEU B O   
3522 C CB  . LEU B 119 ? 0.33000 0.33550 0.34460 -0.13100 0.03470  -0.00110 113 LEU B CB  
3523 C CG  . LEU B 119 ? 0.38120 0.39300 0.40720 -0.12620 0.03710  -0.00800 113 LEU B CG  
3524 C CD1 . LEU B 119 ? 0.34120 0.35060 0.37240 -0.11900 0.02800  -0.00610 113 LEU B CD1 
3525 C CD2 . LEU B 119 ? 0.39250 0.41540 0.43730 -0.12290 0.04160  -0.01150 113 LEU B CD2 
3526 N N   . SER B 120 ? 0.42420 0.41880 0.40460 -0.15030 0.04160  0.00950  114 SER B N   
3527 C CA  . SER B 120 ? 0.46220 0.45020 0.43430 -0.15410 0.03820  0.01820  114 SER B CA  
3528 C C   . SER B 120 ? 0.43410 0.42460 0.40260 -0.16070 0.04740  0.01750  114 SER B C   
3529 O O   . SER B 120 ? 0.47470 0.46690 0.43150 -0.16700 0.05560  0.01260  114 SER B O   
3530 C CB  . SER B 120 ? 0.45260 0.43240 0.40360 -0.15940 0.03230  0.02420  114 SER B CB  
3531 O OG  . SER B 120 ? 0.45700 0.43190 0.39570 -0.16620 0.03250  0.03180  114 SER B OG  
3532 N N   . GLU B 121 ? 0.46650 0.45690 0.44530 -0.15950 0.04680  0.02180  115 GLU B N   
3533 C CA  . GLU B 121 ? 0.48530 0.47770 0.46130 -0.16590 0.05510  0.02220  115 GLU B CA  
3534 C C   . GLU B 121 ? 0.49790 0.48350 0.44880 -0.17530 0.05700  0.02680  115 GLU B C   
3535 O O   . GLU B 121 ? 0.50880 0.49700 0.45060 -0.18200 0.06650  0.02340  115 GLU B O   
3536 C CB  . GLU B 121 ? 0.61010 0.60150 0.60050 -0.16340 0.05280  0.02710  115 GLU B CB  
3537 C CG  . GLU B 121 ? 0.71340 0.71500 0.72490 -0.15920 0.05630  0.02090  115 GLU B CG  
3538 C CD  . GLU B 121 ? 0.80090 0.81120 0.81140 -0.16350 0.06700  0.01430  115 GLU B CD  
3539 O OE1 . GLU B 121 ? 0.83190 0.84130 0.83490 -0.17050 0.07350  0.01640  115 GLU B OE1 
3540 O OE2 . GLU B 121 ? 0.76280 0.78040 0.78020 -0.15990 0.06920  0.00720  115 GLU B OE2 
3541 N N   . MET B 122 ? 0.52470 0.50210 0.46430 -0.17610 0.04810  0.03470  116 MET B N   
3542 C CA  . MET B 122 ? 0.52770 0.49890 0.44260 -0.18540 0.04770  0.04080  116 MET B CA  
3543 C C   . MET B 122 ? 0.53050 0.50320 0.42720 -0.19180 0.05340  0.03330  116 MET B C   
3544 O O   . MET B 122 ? 0.51090 0.48240 0.38990 -0.20070 0.06000  0.03290  116 MET B O   
3545 C CB  . MET B 122 ? 0.55270 0.51620 0.46260 -0.18380 0.03540  0.05120  116 MET B CB  
3546 C CG  . MET B 122 ? 0.70180 0.65920 0.60710 -0.18760 0.03330  0.06240  116 MET B CG  
3547 S SD  . MET B 122 ? 0.89600 0.85540 0.81980 -0.18620 0.04160  0.06200  116 MET B SD  
3548 C CE  . MET B 122 ? 0.69280 0.64930 0.59430 -0.19820 0.04770  0.06780  116 MET B CE  
3549 N N   . VAL B 123 ? 0.47230 0.44730 0.37330 -0.18740 0.05170  0.02670  117 VAL B N   
3550 C CA  . VAL B 123 ? 0.50780 0.48340 0.39330 -0.19330 0.05840  0.01810  117 VAL B CA  
3551 C C   . VAL B 123 ? 0.48920 0.47150 0.38090 -0.19490 0.07290  0.00850  117 VAL B C   
3552 O O   . VAL B 123 ? 0.51240 0.49360 0.38650 -0.20330 0.08190  0.00380  117 VAL B O   
3553 C CB  . VAL B 123 ? 0.45650 0.43270 0.34850 -0.18750 0.05360  0.01340  117 VAL B CB  
3554 C CG1 . VAL B 123 ? 0.41690 0.39300 0.29500 -0.19350 0.06240  0.00270  117 VAL B CG1 
3555 C CG2 . VAL B 123 ? 0.43070 0.40090 0.31760 -0.18570 0.03920  0.02310  117 VAL B CG2 
3556 N N   . ASN B 124 ? 0.46800 0.45790 0.38540 -0.18690 0.07520  0.00550  118 ASN B N   
3557 C CA  . ASN B 124 ? 0.47450 0.47260 0.40220 -0.18730 0.08810  -0.00270 118 ASN B CA  
3558 C C   . ASN B 124 ? 0.51890 0.51550 0.43430 -0.19560 0.09510  0.00020  118 ASN B C   
3559 O O   . ASN B 124 ? 0.48680 0.48570 0.39480 -0.20080 0.10700  -0.00710 118 ASN B O   
3560 C CB  . ASN B 124 ? 0.44840 0.45520 0.40540 -0.17780 0.08640  -0.00380 118 ASN B CB  
3561 C CG  . ASN B 124 ? 0.52240 0.53890 0.49400 -0.17500 0.09670  -0.01390 118 ASN B CG  
3562 O OD1 . ASN B 124 ? 0.50690 0.52340 0.47640 -0.17380 0.09960  -0.02080 118 ASN B OD1 
3563 N ND2 . ASN B 124 ? 0.53470 0.55940 0.52100 -0.17450 0.10310  -0.01520 118 ASN B ND2 
3564 N N   . ARG B 125 ? 0.50330 0.49550 0.41710 -0.19670 0.08830  0.01060  119 ARG B N   
3565 C CA  . ARG B 125 ? 0.49980 0.48980 0.40190 -0.20460 0.09370  0.01510  119 ARG B CA  
3566 C C   . ARG B 125 ? 0.55410 0.53860 0.42660 -0.21470 0.09830  0.01330  119 ARG B C   
3567 O O   . ARG B 125 ? 0.53320 0.51950 0.39740 -0.22110 0.10950  0.00930  119 ARG B O   
3568 C CB  . ARG B 125 ? 0.56280 0.54690 0.46740 -0.20340 0.08380  0.02750  119 ARG B CB  
3569 C CG  . ARG B 125 ? 0.68100 0.66140 0.57570 -0.21070 0.08710  0.03500  119 ARG B CG  
3570 C CD  . ARG B 125 ? 0.74270 0.71820 0.64970 -0.20640 0.07800  0.04550  119 ARG B CD  
3571 N NE  . ARG B 125 ? 0.75110 0.73070 0.68280 -0.19640 0.07360  0.04200  119 ARG B NE  
3572 C CZ  . ARG B 125 ? 0.76050 0.74690 0.71380 -0.19260 0.07770  0.03830  119 ARG B CZ  
3573 N NH1 . ARG B 125 ? 0.73800 0.72830 0.69370 -0.19760 0.08650  0.03780  119 ARG B NH1 
3574 N NH2 . ARG B 125 ? 0.72960 0.71950 0.70240 -0.18410 0.07240  0.03530  119 ARG B NH2 
3575 N N   . SER B 126 ? 0.51590 0.49400 0.37200 -0.21660 0.08970  0.01590  120 SER B N   
3576 C CA  . SER B 126 ? 0.53190 0.50470 0.35860 -0.22690 0.09280  0.01350  120 SER B CA  
3577 C C   . SER B 126 ? 0.61430 0.59110 0.44010 -0.22850 0.10650  -0.00130 120 SER B C   
3578 O O   . SER B 126 ? 0.64250 0.61780 0.45110 -0.23680 0.11640  -0.00610 120 SER B O   
3579 C CB  . SER B 126 ? 0.64290 0.60920 0.45520 -0.22830 0.07930  0.01950  120 SER B CB  
3580 O OG  . SER B 126 ? 0.77510 0.73810 0.56340 -0.23670 0.08320  0.01240  120 SER B OG  
3581 N N   . TRP B 127 ? 0.55780 0.53940 0.40280 -0.22020 0.10780  -0.00880 121 TRP B N   
3582 C CA  . TRP B 127 ? 0.51700 0.50250 0.36600 -0.22000 0.12150  -0.02280 121 TRP B CA  
3583 C C   . TRP B 127 ? 0.56710 0.55890 0.42500 -0.22120 0.13510  -0.02740 121 TRP B C   
3584 O O   . TRP B 127 ? 0.56140 0.55250 0.40900 -0.22660 0.14770  -0.03680 121 TRP B O   
3585 C CB  . TRP B 127 ? 0.49580 0.48680 0.36970 -0.20930 0.11950  -0.02780 121 TRP B CB  
3586 C CG  . TRP B 127 ? 0.52010 0.50520 0.38530 -0.20860 0.10980  -0.02680 121 TRP B CG  
3587 C CD1 . TRP B 127 ? 0.51740 0.49360 0.35550 -0.21670 0.10220  -0.02200 121 TRP B CD1 
3588 C CD2 . TRP B 127 ? 0.49180 0.48010 0.37610 -0.19960 0.10610  -0.03040 121 TRP B CD2 
3589 N NE1 . TRP B 127 ? 0.46430 0.43790 0.30380 -0.21330 0.09430  -0.02260 121 TRP B NE1 
3590 C CE2 . TRP B 127 ? 0.48930 0.46980 0.35690 -0.20270 0.09680  -0.02780 121 TRP B CE2 
3591 C CE3 . TRP B 127 ? 0.41420 0.41170 0.32850 -0.18930 0.10910  -0.03500 121 TRP B CE3 
3592 C CZ2 . TRP B 127 ? 0.45940 0.44040 0.33970 -0.19580 0.09120  -0.03000 121 TRP B CZ2 
3593 C CZ3 . TRP B 127 ? 0.45520 0.45310 0.38110 -0.18240 0.10320  -0.03700 121 TRP B CZ3 
3594 C CH2 . TRP B 127 ? 0.43000 0.41930 0.33900 -0.18560 0.09470  -0.03460 121 TRP B CH2 
3595 N N   . ILE B 128 ? 0.52380 0.52170 0.40180 -0.21630 0.13290  -0.02120 122 ILE B N   
3596 C CA  . ILE B 128 ? 0.53300 0.53830 0.42270 -0.21720 0.14480  -0.02460 122 ILE B CA  
3597 C C   . ILE B 128 ? 0.59950 0.59900 0.46330 -0.22850 0.15130  -0.02290 122 ILE B C   
3598 O O   . ILE B 128 ? 0.64350 0.64620 0.50620 -0.23190 0.16520  -0.03090 122 ILE B O   
3599 C CB  . ILE B 128 ? 0.46200 0.47390 0.37610 -0.21090 0.13910  -0.01720 122 ILE B CB  
3600 C CG1 . ILE B 128 ? 0.47740 0.49690 0.41830 -0.20000 0.13490  -0.02090 122 ILE B CG1 
3601 C CG2 . ILE B 128 ? 0.45360 0.47190 0.37590 -0.21400 0.14980  -0.01810 122 ILE B CG2 
3602 C CD1 . ILE B 128 ? 0.50550 0.52950 0.46740 -0.19410 0.12590  -0.01340 122 ILE B CD1 
3603 N N   . LYS B 129 ? 0.60010 0.59120 0.44330 -0.23420 0.14120  -0.01220 123 LYS B N   
3604 C CA  . LYS B 129 ? 0.57910 0.56500 0.39740 -0.24510 0.14590  -0.00900 123 LYS B CA  
3605 C C   . LYS B 129 ? 0.71890 0.70100 0.51510 -0.25250 0.15550  -0.02000 123 LYS B C   
3606 O O   . LYS B 129 ? 0.73130 0.71260 0.51440 -0.26020 0.16610  -0.02310 123 LYS B O   
3607 C CB  . LYS B 129 ? 0.58670 0.56470 0.38890 -0.24900 0.13170  0.00540  123 LYS B CB  
3608 C CG  . LYS B 129 ? 0.71870 0.69540 0.51580 -0.25440 0.13340  0.01490  123 LYS B CG  
3609 C CD  . LYS B 129 ? 0.67430 0.64590 0.47350 -0.25210 0.11870  0.02980  123 LYS B CD  
3610 C CE  . LYS B 129 ? 0.57760 0.55190 0.40090 -0.24080 0.11040  0.02940  123 LYS B CE  
3611 N NZ  . LYS B 129 ? 0.68560 0.65670 0.52130 -0.23650 0.10020  0.04200  123 LYS B NZ  
3612 N N   . GLN B 130 ? 0.68190 0.66110 0.47420 -0.25050 0.15250  -0.02640 124 GLN B N   
3613 C CA  . GLN B 130 ? 0.71760 0.69170 0.48910 -0.25760 0.16100  -0.03770 124 GLN B CA  
3614 C C   . GLN B 130 ? 0.71760 0.69720 0.50850 -0.25180 0.17580  -0.05270 124 GLN B C   
3615 O O   . GLN B 130 ? 0.78420 0.75870 0.56160 -0.25630 0.18380  -0.06360 124 GLN B O   
3616 C CB  . GLN B 130 ? 0.69720 0.66380 0.45090 -0.26030 0.14880  -0.03570 124 GLN B CB  
3617 C CG  . GLN B 130 ? 0.75870 0.72180 0.50310 -0.26210 0.13180  -0.01940 124 GLN B CG  
3618 C CD  . GLN B 130 ? 0.94640 0.90470 0.68190 -0.26180 0.11840  -0.01640 124 GLN B CD  
3619 O OE1 . GLN B 130 ? 0.93680 0.89320 0.66870 -0.26220 0.12230  -0.02700 124 GLN B OE1 
3620 N NE2 . GLN B 130 ? 0.95280 0.90900 0.68640 -0.26090 0.10270  -0.00190 124 GLN B NE2 
3621 N N   . ASP B 131 ? 0.72600 0.71580 0.54920 -0.24190 0.17910  -0.05320 125 ASP B N   
3622 C CA  . ASP B 131 ? 0.72380 0.72040 0.57080 -0.23440 0.19130  -0.06560 125 ASP B CA  
3623 C C   . ASP B 131 ? 0.74640 0.73870 0.59280 -0.23090 0.18920  -0.07300 125 ASP B C   
3624 O O   . ASP B 131 ? 0.72460 0.71690 0.57740 -0.22910 0.20120  -0.08530 125 ASP B O   
3625 C CB  . ASP B 131 ? 0.74690 0.74380 0.58860 -0.23980 0.20880  -0.07540 125 ASP B CB  
3626 C CG  . ASP B 131 ? 0.79940 0.80320 0.64960 -0.24130 0.21330  -0.06940 125 ASP B CG  
3627 O OD1 . ASP B 131 ? 0.79580 0.81090 0.67720 -0.23270 0.21500  -0.06850 125 ASP B OD1 
3628 O OD2 . ASP B 131 ? 0.78670 0.78480 0.61210 -0.25160 0.21450  -0.06520 125 ASP B OD2 
3629 N N   . PHE B 132 ? 0.65240 0.64080 0.49250 -0.22980 0.17410  -0.06520 126 PHE B N   
3630 C CA  . PHE B 132 ? 0.68220 0.66620 0.52080 -0.22720 0.17080  -0.07070 126 PHE B CA  
3631 C C   . PHE B 132 ? 0.65130 0.64460 0.52520 -0.21420 0.17310  -0.07510 126 PHE B C   
3632 O O   . PHE B 132 ? 0.62210 0.62380 0.51860 -0.20670 0.16640  -0.06780 126 PHE B O   
3633 C CB  . PHE B 132 ? 0.62460 0.60260 0.44710 -0.22990 0.15330  -0.05980 126 PHE B CB  
3634 C CG  . PHE B 132 ? 0.61830 0.59200 0.43900 -0.22780 0.14880  -0.06430 126 PHE B CG  
3635 C CD1 . PHE B 132 ? 0.64220 0.60830 0.44480 -0.23440 0.15710  -0.07560 126 PHE B CD1 
3636 C CD2 . PHE B 132 ? 0.61310 0.58940 0.44980 -0.21970 0.13630  -0.05730 126 PHE B CD2 
3637 C CE1 . PHE B 132 ? 0.57300 0.53470 0.37380 -0.23310 0.15330  -0.07970 126 PHE B CE1 
3638 C CE2 . PHE B 132 ? 0.59690 0.56930 0.43260 -0.21810 0.13220  -0.06080 126 PHE B CE2 
3639 C CZ  . PHE B 132 ? 0.65410 0.61940 0.47190 -0.22490 0.14090  -0.07190 126 PHE B CZ  
3640 N N   . ILE B 133 ? 0.64570 0.63710 0.52490 -0.21170 0.18230  -0.08700 127 ILE B N   
3641 C CA  . ILE B 133 ? 0.57720 0.57680 0.48980 -0.19930 0.18430  -0.09110 127 ILE B CA  
3642 C C   . ILE B 133 ? 0.54060 0.53480 0.44910 -0.19740 0.17450  -0.09010 127 ILE B C   
3643 O O   . ILE B 133 ? 0.54750 0.53190 0.43640 -0.20330 0.17850  -0.09750 127 ILE B O   
3644 C CB  . ILE B 133 ? 0.62490 0.62640 0.55130 -0.19610 0.20190  -0.10440 127 ILE B CB  
3645 C CG1 . ILE B 133 ? 0.65470 0.66710 0.60090 -0.19290 0.20930  -0.10330 127 ILE B CG1 
3646 C CG2 . ILE B 133 ? 0.62630 0.63070 0.57790 -0.18530 0.20310  -0.11010 127 ILE B CG2 
3647 C CD1 . ILE B 133 ? 0.74340 0.75330 0.66750 -0.20310 0.21040  -0.09840 127 ILE B CD1 
3648 N N   . PRO B 134 ? 0.51980 0.51950 0.44500 -0.19000 0.16140  -0.08130 128 PRO B N   
3649 C CA  . PRO B 134 ? 0.49460 0.48910 0.41690 -0.18830 0.15150  -0.07960 128 PRO B CA  
3650 C C   . PRO B 134 ? 0.50750 0.50100 0.44260 -0.18350 0.16130  -0.09120 128 PRO B C   
3651 O O   . PRO B 134 ? 0.46580 0.46660 0.42510 -0.17610 0.17200  -0.09780 128 PRO B O   
3652 C CB  . PRO B 134 ? 0.46580 0.46800 0.41000 -0.17920 0.13740  -0.06900 128 PRO B CB  
3653 C CG  . PRO B 134 ? 0.40820 0.42080 0.36990 -0.17570 0.14180  -0.06690 128 PRO B CG  
3654 C CD  . PRO B 134 ? 0.46500 0.47420 0.40840 -0.18460 0.15390  -0.07160 128 PRO B CD  
3655 N N   . THR B 135 ? 0.47850 0.46280 0.39820 -0.18770 0.15710  -0.09320 129 THR B N   
3656 C CA  . THR B 135 ? 0.50050 0.48010 0.42860 -0.18250 0.16400  -0.10400 129 THR B CA  
3657 C C   . THR B 135 ? 0.48630 0.46470 0.42640 -0.17310 0.14730  -0.09810 129 THR B C   
3658 O O   . THR B 135 ? 0.41100 0.39240 0.35260 -0.17150 0.13250  -0.08660 129 THR B O   
3659 C CB  . THR B 135 ? 0.45340 0.41990 0.34930 -0.19390 0.17260  -0.11390 129 THR B CB  
3660 O OG1 . THR B 135 ? 0.52180 0.47980 0.39160 -0.20060 0.15700  -0.10720 129 THR B OG1 
3661 C CG2 . THR B 135 ? 0.51420 0.48020 0.39320 -0.20290 0.18340  -0.11710 129 THR B CG2 
3662 N N   . ALA B 136 ? 0.47540 0.44830 0.42390 -0.16710 0.15070  -0.10630 130 ALA B N   
3663 C CA  . ALA B 136 ? 0.43560 0.40790 0.39850 -0.15730 0.13690  -0.10140 130 ALA B CA  
3664 C C   . ALA B 136 ? 0.41060 0.37730 0.35220 -0.16280 0.11970  -0.09200 130 ALA B C   
3665 O O   . ALA B 136 ? 0.43120 0.40210 0.38540 -0.15600 0.10600  -0.08270 130 ALA B O   
3666 C CB  . ALA B 136 ? 0.39910 0.36320 0.36800 -0.15290 0.14410  -0.11220 130 ALA B CB  
3667 N N   . VAL B 137 ? 0.45200 0.40950 0.36140 -0.17540 0.12030  -0.09410 131 VAL B N   
3668 C CA  . VAL B 137 ? 0.45140 0.40360 0.34020 -0.18140 0.10410  -0.08510 131 VAL B CA  
3669 C C   . VAL B 137 ? 0.49240 0.45140 0.38300 -0.18170 0.09370  -0.07150 131 VAL B C   
3670 O O   . VAL B 137 ? 0.50830 0.46510 0.39130 -0.18300 0.07880  -0.06180 131 VAL B O   
3671 C CB  . VAL B 137 ? 0.50160 0.44350 0.35530 -0.19590 0.10860  -0.09140 131 VAL B CB  
3672 C CG1 . VAL B 137 ? 0.49050 0.43440 0.32620 -0.20620 0.11650  -0.09000 131 VAL B CG1 
3673 C CG2 . VAL B 137 ? 0.53600 0.47160 0.37160 -0.20100 0.09220  -0.08490 131 VAL B CG2 
3674 N N   . CYS B 138 ? 0.43990 0.40720 0.34280 -0.18020 0.10150  -0.07050 132 CYS B N   
3675 C CA  . CYS B 138 ? 0.44170 0.41470 0.34800 -0.18080 0.09350  -0.05860 132 CYS B CA  
3676 C C   . CYS B 138 ? 0.44200 0.42300 0.37770 -0.16860 0.08560  -0.05320 132 CYS B C   
3677 O O   . CYS B 138 ? 0.45980 0.44370 0.39830 -0.16640 0.07600  -0.04310 132 CYS B O   
3678 C CB  . CYS B 138 ? 0.42080 0.39870 0.32440 -0.18700 0.10630  -0.06020 132 CYS B CB  
3679 S SG  . CYS B 138 ? 0.53070 0.49980 0.39630 -0.20330 0.11670  -0.06550 132 CYS B SG  
3680 N N   . SER B 139 ? 0.39590 0.38030 0.35310 -0.15870 0.08910  -0.05960 133 SER B N   
3681 C CA  . SER B 139 ? 0.38860 0.38110 0.37260 -0.14750 0.08190  -0.05510 133 SER B CA  
3682 C C   . SER B 139 ? 0.40120 0.39090 0.38050 -0.14560 0.06540  -0.04450 133 SER B C   
3683 O O   . SER B 139 ? 0.37270 0.35410 0.33560 -0.14930 0.05840  -0.04270 133 SER B O   
3684 C CB  . SER B 139 ? 0.41430 0.40730 0.41560 -0.13820 0.08480  -0.06190 133 SER B CB  
3685 O OG  . SER B 139 ? 0.39130 0.39020 0.41310 -0.12840 0.07480  -0.05610 133 SER B OG  
3686 N N   . ASN B 140 ? 0.34940 0.34640 0.34390 -0.13840 0.05900  -0.03760 134 ASN B N   
3687 C CA  . ASN B 140 ? 0.33160 0.32630 0.32540 -0.13370 0.04460  -0.02810 134 ASN B CA  
3688 C C   . ASN B 140 ? 0.33110 0.32300 0.33070 -0.12750 0.03770  -0.02850 134 ASN B C   
3689 O O   . ASN B 140 ? 0.33390 0.32220 0.32940 -0.12480 0.02680  -0.02150 134 ASN B O   
3690 C CB  . ASN B 140 ? 0.34120 0.34370 0.35140 -0.12740 0.04110  -0.02280 134 ASN B CB  
3691 C CG  . ASN B 140 ? 0.39740 0.40840 0.43130 -0.11830 0.04120  -0.02550 134 ASN B CG  
3692 O OD1 . ASN B 140 ? 0.47600 0.48700 0.51750 -0.11150 0.03230  -0.02160 134 ASN B OD1 
3693 N ND2 . ASN B 140 ? 0.37250 0.39140 0.41870 -0.11820 0.05120  -0.03150 134 ASN B ND2 
3694 N N   . CYS B 141 ? 0.32860 0.32170 0.33820 -0.12510 0.04450  -0.03650 135 CYS B N   
3695 C CA  . CYS B 141 ? 0.36430 0.35460 0.38100 -0.11900 0.03910  -0.03740 135 CYS B CA  
3696 C C   . CYS B 141 ? 0.36320 0.34400 0.36530 -0.12510 0.04340  -0.04440 135 CYS B C   
3697 O O   . CYS B 141 ? 0.37560 0.35360 0.38560 -0.12020 0.04310  -0.04790 135 CYS B O   
3698 C CB  . CYS B 141 ? 0.38150 0.38020 0.42380 -0.11060 0.04270  -0.04030 135 CYS B CB  
3699 S SG  . CYS B 141 ? 0.40930 0.42020 0.46830 -0.10440 0.03810  -0.03350 135 CYS B SG  
3700 N N   . SER B 142 ? 0.32770 0.30310 0.30800 -0.13580 0.04750  -0.04650 136 SER B N   
3701 C CA  . SER B 142 ? 0.37260 0.33900 0.33650 -0.14170 0.05290  -0.05460 136 SER B CA  
3702 C C   . SER B 142 ? 0.38650 0.34650 0.34340 -0.14130 0.04190  -0.05170 136 SER B C   
3703 O O   . SER B 142 ? 0.38760 0.34110 0.34250 -0.14170 0.04550  -0.05930 136 SER B O   
3704 C CB  . SER B 142 ? 0.43150 0.39440 0.37060 -0.15400 0.05820  -0.05590 136 SER B CB  
3705 O OG  . SER B 142 ? 0.41020 0.37170 0.33540 -0.15930 0.04620  -0.04520 136 SER B OG  
3706 N N   . GLY B 143 ? 0.36590 0.32760 0.31960 -0.13890 0.02870  -0.04050 137 GLY B N   
3707 C CA  . GLY B 143 ? 0.35170 0.30930 0.30120 -0.13670 0.01840  -0.03680 137 GLY B CA  
3708 C C   . GLY B 143 ? 0.34270 0.30180 0.31300 -0.12600 0.01680  -0.03800 137 GLY B C   
3709 O O   . GLY B 143 ? 0.32120 0.27560 0.28990 -0.12490 0.01340  -0.03970 137 GLY B O   
3710 N N   . HIS B 144 ? 0.36770 0.33360 0.35770 -0.11860 0.01890  -0.03690 138 HIS B N   
3711 C CA  . HIS B 144 ? 0.32330 0.29080 0.33250 -0.10960 0.01820  -0.03810 138 HIS B CA  
3712 C C   . HIS B 144 ? 0.34260 0.30520 0.35560 -0.11090 0.02940  -0.04910 138 HIS B C   
3713 O O   . HIS B 144 ? 0.35280 0.31090 0.37180 -0.10690 0.02790  -0.05090 138 HIS B O   
3714 C CB  . HIS B 144 ? 0.33940 0.31640 0.36700 -0.10280 0.01760  -0.03390 138 HIS B CB  
3715 C CG  . HIS B 144 ? 0.38990 0.36960 0.43590 -0.09420 0.01530  -0.03300 138 HIS B CG  
3716 N ND1 . HIS B 144 ? 0.41280 0.39200 0.46150 -0.08910 0.00510  -0.02610 138 HIS B ND1 
3717 C CD2 . HIS B 144 ? 0.45420 0.43710 0.51770 -0.08980 0.02220  -0.03790 138 HIS B CD2 
3718 C CE1 . HIS B 144 ? 0.43770 0.41930 0.50160 -0.08290 0.00560  -0.02650 138 HIS B CE1 
3719 N NE2 . HIS B 144 ? 0.43050 0.41450 0.50470 -0.08260 0.01550  -0.03330 138 HIS B NE2 
3720 N N   . HIS B 145 ? 0.32290 0.28580 0.33380 -0.11540 0.04130  -0.05650 139 HIS B N   
3721 C CA  . HIS B 145 ? 0.32940 0.28690 0.34390 -0.11440 0.05290  -0.06700 139 HIS B CA  
3722 C C   . HIS B 145 ? 0.36310 0.30840 0.35810 -0.12230 0.05260  -0.07270 139 HIS B C   
3723 O O   . HIS B 145 ? 0.35790 0.29640 0.35890 -0.11960 0.05810  -0.07960 139 HIS B O   
3724 C CB  . HIS B 145 ? 0.36260 0.32380 0.37760 -0.11670 0.06610  -0.07310 139 HIS B CB  
3725 C CG  . HIS B 145 ? 0.38200 0.35510 0.42310 -0.10730 0.06940  -0.07060 139 HIS B CG  
3726 N ND1 . HIS B 145 ? 0.40260 0.37780 0.46290 -0.10070 0.08040  -0.07690 139 HIS B ND1 
3727 C CD2 . HIS B 145 ? 0.35210 0.33580 0.40410 -0.10350 0.06250  -0.06220 139 HIS B CD2 
3728 C CE1 . HIS B 145 ? 0.38620 0.37430 0.46800 -0.09350 0.07950  -0.07190 139 HIS B CE1 
3729 N NE2 . HIS B 145 ? 0.37550 0.36850 0.45180 -0.09550 0.06880  -0.06350 139 HIS B NE2 
3730 N N   . VAL B 146 ? 0.31170 0.25440 0.28360 -0.13080 0.04560  -0.06880 140 VAL B N   
3731 C CA  . VAL B 146 ? 0.36180 0.29550 0.31560 -0.13650 0.04360  -0.07270 140 VAL B CA  
3732 C C   . VAL B 146 ? 0.38120 0.31430 0.34540 -0.12880 0.03310  -0.06710 140 VAL B C   
3733 O O   . VAL B 146 ? 0.37640 0.30220 0.33800 -0.12930 0.03490  -0.07260 140 VAL B O   
3734 C CB  . VAL B 146 ? 0.34520 0.27800 0.27210 -0.14740 0.03820  -0.06870 140 VAL B CB  
3735 C CG1 . VAL B 146 ? 0.39140 0.31700 0.30120 -0.15290 0.03410  -0.07100 140 VAL B CG1 
3736 C CG2 . VAL B 146 ? 0.38380 0.31540 0.29840 -0.15640 0.05050  -0.07590 140 VAL B CG2 
3737 N N   . GLY B 147 ? 0.35570 0.29630 0.33190 -0.12180 0.02280  -0.05630 141 GLY B N   
3738 C CA  . GLY B 147 ? 0.29610 0.23690 0.28460 -0.11420 0.01430  -0.05120 141 GLY B CA  
3739 C C   . GLY B 147 ? 0.35490 0.29210 0.36010 -0.10820 0.02160  -0.05730 141 GLY B C   
3740 O O   . GLY B 147 ? 0.29540 0.22690 0.30200 -0.10670 0.01950  -0.05870 141 GLY B O   
3741 N N   . MET B 148 ? 0.34730 0.28810 0.36710 -0.10450 0.03040  -0.06080 142 MET B N   
3742 C CA  . MET B 148 ? 0.32800 0.26590 0.36730 -0.09800 0.03820  -0.06600 142 MET B CA  
3743 C C   . MET B 148 ? 0.35980 0.28610 0.39080 -0.10220 0.04780  -0.07710 142 MET B C   
3744 O O   . MET B 148 ? 0.38770 0.30800 0.42810 -0.09760 0.04920  -0.07910 142 MET B O   
3745 C CB  . MET B 148 ? 0.28490 0.23180 0.34250 -0.09200 0.04550  -0.06630 142 MET B CB  
3746 C CG  . MET B 148 ? 0.34490 0.30360 0.41410 -0.08600 0.03650  -0.05580 142 MET B CG  
3747 S SD  . MET B 148 ? 0.40530 0.36460 0.49170 -0.07660 0.02870  -0.04900 142 MET B SD  
3748 C CE  . MET B 148 ? 0.44620 0.41370 0.52810 -0.07680 0.01570  -0.03820 142 MET B CE  
3749 N N   . LEU B 149 ? 0.35080 0.27360 0.36370 -0.11130 0.05510  -0.08450 143 LEU B N   
3750 C CA  . LEU B 149 ? 0.37400 0.28540 0.37470 -0.11660 0.06410  -0.09540 143 LEU B CA  
3751 C C   . LEU B 149 ? 0.40840 0.31470 0.39720 -0.11890 0.05390  -0.09230 143 LEU B C   
3752 O O   . LEU B 149 ? 0.38600 0.28380 0.37700 -0.11800 0.05860  -0.09840 143 LEU B O   
3753 C CB  . LEU B 149 ? 0.36790 0.27750 0.34700 -0.12740 0.07210  -0.10240 143 LEU B CB  
3754 C CG  . LEU B 149 ? 0.44330 0.35430 0.43280 -0.12720 0.08770  -0.11060 143 LEU B CG  
3755 C CD1 . LEU B 149 ? 0.45080 0.36170 0.41510 -0.13920 0.09230  -0.11430 143 LEU B CD1 
3756 C CD2 . LEU B 149 ? 0.42290 0.32490 0.42440 -0.12320 0.10200  -0.12200 143 LEU B CD2 
3757 N N   . ALA B 150 ? 0.37250 0.28430 0.35020 -0.12180 0.04030  -0.08270 144 ALA B N   
3758 C CA  . ALA B 150 ? 0.38650 0.29540 0.35620 -0.12390 0.03010  -0.07900 144 ALA B CA  
3759 C C   . ALA B 150 ? 0.36450 0.27150 0.35410 -0.11490 0.02720  -0.07630 144 ALA B C   
3760 O O   . ALA B 150 ? 0.40840 0.30800 0.39610 -0.11620 0.02790  -0.08040 144 ALA B O   
3761 C CB  . ALA B 150 ? 0.39860 0.31520 0.35930 -0.12640 0.01680  -0.06810 144 ALA B CB  
3762 N N   . GLY B 151 ? 0.37200 0.28560 0.38040 -0.10630 0.02470  -0.06960 145 GLY B N   
3763 C CA  . GLY B 151 ? 0.40730 0.31940 0.43370 -0.09820 0.02230  -0.06610 145 GLY B CA  
3764 C C   . GLY B 151 ? 0.39520 0.29820 0.43070 -0.09560 0.03430  -0.07530 145 GLY B C   
3765 O O   . GLY B 151 ? 0.34530 0.24210 0.38510 -0.09370 0.03280  -0.07540 145 GLY B O   
3766 N N   . ALA B 152 ? 0.36790 0.27000 0.40850 -0.09520 0.04690  -0.08290 146 ALA B N   
3767 C CA  . ALA B 152 ? 0.40180 0.29490 0.45360 -0.09180 0.05980  -0.09190 146 ALA B CA  
3768 C C   . ALA B 152 ? 0.43570 0.31810 0.47060 -0.09900 0.06210  -0.09940 146 ALA B C   
3769 O O   . ALA B 152 ? 0.45850 0.33330 0.50260 -0.09540 0.06540  -0.10180 146 ALA B O   
3770 C CB  . ALA B 152 ? 0.41020 0.30470 0.46960 -0.09120 0.07360  -0.09950 146 ALA B CB  
3771 N N   . ARG B 153 ? 0.39880 0.28080 0.40890 -0.10940 0.05990  -0.10250 147 ARG B N   
3772 C CA  . ARG B 153 ? 0.41520 0.28800 0.40840 -0.11730 0.06190  -0.10990 147 ARG B CA  
3773 C C   . ARG B 153 ? 0.43360 0.30500 0.42770 -0.11660 0.04950  -0.10330 147 ARG B C   
3774 O O   . ARG B 153 ? 0.45380 0.31610 0.44750 -0.11810 0.05270  -0.10870 147 ARG B O   
3775 C CB  . ARG B 153 ? 0.40740 0.28130 0.37340 -0.12920 0.06160  -0.11330 147 ARG B CB  
3776 C CG  . ARG B 153 ? 0.56400 0.43560 0.52530 -0.13250 0.07760  -0.12360 147 ARG B CG  
3777 C CD  . ARG B 153 ? 0.60590 0.46840 0.54570 -0.14310 0.08630  -0.13480 147 ARG B CD  
3778 N NE  . ARG B 153 ? 0.71640 0.57550 0.65720 -0.14440 0.10440  -0.14560 147 ARG B NE  
3779 C CZ  . ARG B 153 ? 0.72320 0.58380 0.64400 -0.15380 0.11040  -0.14990 147 ARG B CZ  
3780 N NH1 . ARG B 153 ? 0.69430 0.55920 0.59120 -0.16310 0.09950  -0.14400 147 ARG B NH1 
3781 N NH2 . ARG B 153 ? 0.69060 0.54860 0.61640 -0.15380 0.12800  -0.15980 147 ARG B NH2 
3782 N N   . ALA B 154 ? 0.40070 0.28110 0.39770 -0.11420 0.03590  -0.09160 148 ALA B N   
3783 C CA  . ALA B 154 ? 0.41520 0.29580 0.41340 -0.11420 0.02390  -0.08500 148 ALA B CA  
3784 C C   . ALA B 154 ? 0.40920 0.28330 0.42480 -0.10720 0.02690  -0.08500 148 ALA B C   
3785 O O   . ALA B 154 ? 0.44690 0.31510 0.46040 -0.10990 0.02350  -0.08610 148 ALA B O   
3786 C CB  . ALA B 154 ? 0.37400 0.26610 0.37640 -0.11120 0.01100  -0.07260 148 ALA B CB  
3787 N N   . ILE B 155 ? 0.35050 0.22560 0.38410 -0.09840 0.03370  -0.08390 149 ILE B N   
3788 C CA  . ILE B 155 ? 0.38690 0.25700 0.43820 -0.09090 0.03620  -0.08190 149 ILE B CA  
3789 C C   . ILE B 155 ? 0.40730 0.26700 0.46500 -0.08960 0.05080  -0.09250 149 ILE B C   
3790 O O   . ILE B 155 ? 0.42040 0.27510 0.49410 -0.08310 0.05410  -0.09110 149 ILE B O   
3791 C CB  . ILE B 155 ? 0.42340 0.30220 0.49370 -0.08110 0.03360  -0.07230 149 ILE B CB  
3792 C CG1 . ILE B 155 ? 0.35720 0.24100 0.43560 -0.07770 0.04220  -0.07550 149 ILE B CG1 
3793 C CG2 . ILE B 155 ? 0.35220 0.23990 0.41750 -0.08190 0.01920  -0.06110 149 ILE B CG2 
3794 C CD1 . ILE B 155 ? 0.36770 0.26120 0.46610 -0.06830 0.03960  -0.06630 149 ILE B CD1 
3795 N N   . GLY B 156 ? 0.44820 0.30430 0.49350 -0.09580 0.06000  -0.10290 150 GLY B N   
3796 C CA  . GLY B 156 ? 0.44290 0.28890 0.49370 -0.09520 0.07500  -0.11380 150 GLY B CA  
3797 C C   . GLY B 156 ? 0.49260 0.34070 0.56710 -0.08520 0.08620  -0.11450 150 GLY B C   
3798 O O   . GLY B 156 ? 0.45320 0.29360 0.54120 -0.08100 0.09740  -0.11990 150 GLY B O   
3799 N N   . ALA B 157 ? 0.53530 0.39410 0.61690 -0.08130 0.08330  -0.10860 151 ALA B N   
3800 C CA  . ALA B 157 ? 0.59500 0.45800 0.70190 -0.07160 0.09230  -0.10770 151 ALA B CA  
3801 C C   . ALA B 157 ? 0.67930 0.54010 0.78490 -0.07430 0.10760  -0.11910 151 ALA B C   
3802 O O   . ALA B 157 ? 0.69840 0.55900 0.82720 -0.06630 0.11870  -0.12120 151 ALA B O   
3803 C CB  . ALA B 157 ? 0.45150 0.32740 0.56650 -0.06730 0.08270  -0.09720 151 ALA B CB  
3804 N N   . GLY B 158 ? 0.61290 0.47290 0.69240 -0.08540 0.10830  -0.12560 152 GLY B N   
3805 C CA  . GLY B 158 ? 0.58890 0.44790 0.66530 -0.08880 0.12300  -0.13590 152 GLY B CA  
3806 C C   . GLY B 158 ? 0.63640 0.50630 0.71310 -0.08930 0.12130  -0.13280 152 GLY B C   
3807 O O   . GLY B 158 ? 0.52820 0.40660 0.62180 -0.08190 0.11360  -0.12320 152 GLY B O   
3808 N N   . THR B 159 ? 0.61860 0.48820 0.67590 -0.09850 0.12870  -0.14070 153 THR B N   
3809 C CA  . THR B 159 ? 0.64300 0.52220 0.69550 -0.10150 0.12650  -0.13800 153 THR B CA  
3810 C C   . THR B 159 ? 0.60740 0.49180 0.68640 -0.09370 0.13880  -0.14080 153 THR B C   
3811 O O   . THR B 159 ? 0.57140 0.46910 0.65740 -0.09070 0.13290  -0.13260 153 THR B O   
3812 C CB  . THR B 159 ? 0.65250 0.52960 0.67190 -0.11540 0.12860  -0.14410 153 THR B CB  
3813 O OG1 . THR B 159 ? 0.68680 0.55610 0.70270 -0.11870 0.14600  -0.15670 153 THR B OG1 
3814 C CG2 . THR B 159 ? 0.61390 0.48810 0.61000 -0.12240 0.11430  -0.13920 153 THR B CG2 
3815 N N   . ASP B 160 ? 0.59880 0.47800 0.69350 -0.08860 0.15410  -0.14860 154 ASP B N   
3816 C CA  . ASP B 160 ? 0.63860 0.52470 0.76420 -0.07840 0.16490  -0.14920 154 ASP B CA  
3817 C C   . ASP B 160 ? 0.63480 0.53380 0.78510 -0.06640 0.15160  -0.13380 154 ASP B C   
3818 O O   . ASP B 160 ? 0.63350 0.52700 0.79230 -0.06160 0.14420  -0.12860 154 ASP B O   
3819 C CB  . ASP B 160 ? 0.65930 0.53980 0.80250 -0.07270 0.18010  -0.15570 154 ASP B CB  
3820 C CG  . ASP B 160 ? 0.81740 0.68870 0.93540 -0.08440 0.19150  -0.16780 154 ASP B CG  
3821 O OD1 . ASP B 160 ? 0.69660 0.57110 0.80210 -0.09140 0.19970  -0.17380 154 ASP B OD1 
3822 O OD2 . ASP B 160 ? 0.94390 0.80460 1.05440 -0.08700 0.19220  -0.17120 154 ASP B OD2 
3823 N N   . GLY B 161 ? 0.52220 0.43890 0.68270 -0.06240 0.14830  -0.12590 155 GLY B N   
3824 C CA  . GLY B 161 ? 0.43510 0.36600 0.61910 -0.05150 0.13680  -0.11160 155 GLY B CA  
3825 C C   . GLY B 161 ? 0.41240 0.34710 0.58350 -0.05350 0.11800  -0.10080 155 GLY B C   
3826 O O   . GLY B 161 ? 0.37220 0.31600 0.56150 -0.04480 0.10880  -0.08970 155 GLY B O   
3827 N N   . TYR B 162 ? 0.42690 0.35530 0.56760 -0.06490 0.11200  -0.10330 156 TYR B N   
3828 C CA  . TYR B 162 ? 0.43270 0.36520 0.56300 -0.06650 0.09490  -0.09290 156 TYR B CA  
3829 C C   . TYR B 162 ? 0.39680 0.34700 0.53950 -0.06080 0.08660  -0.08190 156 TYR B C   
3830 O O   . TYR B 162 ? 0.38920 0.34420 0.53360 -0.05800 0.07390  -0.07220 156 TYR B O   
3831 C CB  . TYR B 162 ? 0.44090 0.36710 0.53880 -0.07970 0.09030  -0.09640 156 TYR B CB  
3832 C CG  . TYR B 162 ? 0.35820 0.29240 0.44290 -0.08610 0.09220  -0.09690 156 TYR B CG  
3833 C CD1 . TYR B 162 ? 0.45830 0.38840 0.53460 -0.09180 0.10640  -0.10760 156 TYR B CD1 
3834 C CD2 . TYR B 162 ? 0.42240 0.36740 0.50320 -0.08660 0.08060  -0.08690 156 TYR B CD2 
3835 C CE1 . TYR B 162 ? 0.41170 0.34890 0.47570 -0.09820 0.10860  -0.10760 156 TYR B CE1 
3836 C CE2 . TYR B 162 ? 0.40090 0.35220 0.47060 -0.09260 0.08260  -0.08680 156 TYR B CE2 
3837 C CZ  . TYR B 162 ? 0.43700 0.38470 0.49810 -0.09850 0.09630  -0.09680 156 TYR B CZ  
3838 O OH  . TYR B 162 ? 0.42340 0.37720 0.47290 -0.10490 0.09850  -0.09610 156 TYR B OH  
3839 N N   . HIS B 163 ? 0.32940 0.28940 0.48090 -0.05960 0.09420  -0.08350 157 HIS B N   
3840 C CA  . HIS B 163 ? 0.40130 0.37810 0.56280 -0.05610 0.08730  -0.07460 157 HIS B CA  
3841 C C   . HIS B 163 ? 0.41620 0.40380 0.60880 -0.04420 0.08620  -0.06770 157 HIS B C   
3842 O O   . HIS B 163 ? 0.36850 0.37090 0.57070 -0.04140 0.07950  -0.06000 157 HIS B O   
3843 C CB  . HIS B 163 ? 0.36870 0.35140 0.52440 -0.06180 0.09600  -0.07970 157 HIS B CB  
3844 C CG  . HIS B 163 ? 0.43420 0.41690 0.60700 -0.05810 0.11230  -0.08780 157 HIS B CG  
3845 N ND1 . HIS B 163 ? 0.40520 0.37360 0.57790 -0.05790 0.12270  -0.09710 157 HIS B ND1 
3846 C CD2 . HIS B 163 ? 0.40000 0.39520 0.59210 -0.05450 0.12060  -0.08830 157 HIS B CD2 
3847 C CE1 . HIS B 163 ? 0.37270 0.34430 0.56430 -0.05370 0.13730  -0.10310 157 HIS B CE1 
3848 N NE2 . HIS B 163 ? 0.43640 0.42480 0.64060 -0.05150 0.13620  -0.09760 157 HIS B NE2 
3849 N N   . LEU B 164 ? 0.34820 0.32890 0.55690 -0.03750 0.09230  -0.06980 158 LEU B N   
3850 C CA  . LEU B 164 ? 0.39910 0.38960 0.63900 -0.02590 0.09180  -0.06260 158 LEU B CA  
3851 C C   . LEU B 164 ? 0.41490 0.40540 0.65750 -0.02140 0.07850  -0.05220 158 LEU B C   
3852 O O   . LEU B 164 ? 0.41320 0.39060 0.64030 -0.02510 0.07500  -0.05390 158 LEU B O   
3853 C CB  . LEU B 164 ? 0.40790 0.39010 0.66600 -0.02050 0.10660  -0.06980 158 LEU B CB  
3854 C CG  . LEU B 164 ? 0.44000 0.41940 0.69490 -0.02530 0.12270  -0.08210 158 LEU B CG  
3855 C CD1 . LEU B 164 ? 0.42550 0.39570 0.70150 -0.01870 0.13740  -0.08890 158 LEU B CD1 
3856 C CD2 . LEU B 164 ? 0.35640 0.35450 0.62030 -0.02540 0.12380  -0.07930 158 LEU B CD2 
3857 N N   . PRO B 165 ? 0.40070 0.40580 0.66290 -0.01390 0.07110  -0.04160 159 PRO B N   
3858 C CA  . PRO B 165 ? 0.39960 0.40510 0.66240 -0.01030 0.05860  -0.03140 159 PRO B CA  
3859 C C   . PRO B 165 ? 0.42910 0.42020 0.69750 -0.00620 0.06110  -0.03150 159 PRO B C   
3860 O O   . PRO B 165 ? 0.39170 0.37780 0.65080 -0.00710 0.05220  -0.02630 159 PRO B O   
3861 C CB  . PRO B 165 ? 0.46400 0.48860 0.74920 -0.00310 0.05290  -0.02110 159 PRO B CB  
3862 C CG  . PRO B 165 ? 0.34980 0.38560 0.63700 -0.00640 0.05800  -0.02540 159 PRO B CG  
3863 C CD  . PRO B 165 ? 0.37290 0.39620 0.65370 -0.01020 0.07240  -0.03810 159 PRO B CD  
3864 N N   . ASP B 166 ? 0.51260 0.49630 0.79670 -0.00190 0.07340  -0.03730 160 ASP B N   
3865 C CA  . ASP B 166 ? 0.51000 0.47850 0.80010 0.00160  0.07610  -0.03750 160 ASP B CA  
3866 C C   . ASP B 166 ? 0.46840 0.41890 0.73270 -0.00780 0.07800  -0.04700 160 ASP B C   
3867 O O   . ASP B 166 ? 0.47030 0.40790 0.73610 -0.00660 0.07810  -0.04670 160 ASP B O   
3868 C CB  . ASP B 166 ? 0.55110 0.51600 0.86840 0.00970  0.08960  -0.04080 160 ASP B CB  
3869 C CG  . ASP B 166 ? 0.68870 0.64950 1.00220 0.00510  0.10460  -0.05500 160 ASP B CG  
3870 O OD1 . ASP B 166 ? 0.64840 0.62090 0.95380 0.00060  0.10410  -0.05680 160 ASP B OD1 
3871 O OD2 . ASP B 166 ? 0.68150 0.62690 1.00040 0.00580  0.11780  -0.06450 160 ASP B OD2 
3872 N N   . HIS B 167 ? 0.37320 0.32290 0.61450 -0.01740 0.07900  -0.05460 161 HIS B N   
3873 C CA  . HIS B 167 ? 0.34960 0.28380 0.56610 -0.02720 0.07990  -0.06320 161 HIS B CA  
3874 C C   . HIS B 167 ? 0.35000 0.28320 0.55530 -0.02930 0.06600  -0.05510 161 HIS B C   
3875 O O   . HIS B 167 ? 0.34780 0.29390 0.55520 -0.02670 0.05570  -0.04520 161 HIS B O   
3876 C CB  . HIS B 167 ? 0.36960 0.30520 0.56480 -0.03680 0.08340  -0.07130 161 HIS B CB  
3877 C CG  . HIS B 167 ? 0.41040 0.33040 0.58030 -0.04770 0.08580  -0.08110 161 HIS B CG  
3878 N ND1 . HIS B 167 ? 0.36540 0.28280 0.51540 -0.05460 0.07420  -0.07780 161 HIS B ND1 
3879 C CD2 . HIS B 167 ? 0.38140 0.28810 0.54290 -0.05340 0.09840  -0.09420 161 HIS B CD2 
3880 C CE1 . HIS B 167 ? 0.37050 0.27460 0.50080 -0.06430 0.07840  -0.08770 161 HIS B CE1 
3881 N NE2 . HIS B 167 ? 0.44670 0.34390 0.58200 -0.06410 0.09300  -0.09810 161 HIS B NE2 
3882 N N   . PRO B 168 ? 0.37200 0.29020 0.56640 -0.03420 0.06580  -0.05930 162 PRO B N   
3883 C CA  . PRO B 168 ? 0.33550 0.25360 0.52040 -0.03650 0.05310  -0.05160 162 PRO B CA  
3884 C C   . PRO B 168 ? 0.32630 0.25350 0.49280 -0.04280 0.04360  -0.04860 162 PRO B C   
3885 O O   . PRO B 168 ? 0.29710 0.23030 0.46270 -0.04140 0.03310  -0.03940 162 PRO B O   
3886 C CB  . PRO B 168 ? 0.32020 0.22490 0.49100 -0.04110 0.05520  -0.05760 162 PRO B CB  
3887 C CG  . PRO B 168 ? 0.30000 0.19610 0.47090 -0.04310 0.06930  -0.06990 162 PRO B CG  
3888 C CD  . PRO B 168 ? 0.29530 0.19740 0.49060 -0.03570 0.07710  -0.06950 162 PRO B CD  
3889 N N   . MET B 169 ? 0.29590 0.22340 0.44710 -0.05000 0.04730  -0.05580 163 MET B N   
3890 C CA  . MET B 169 ? 0.33080 0.26690 0.46700 -0.05520 0.03840  -0.05160 163 MET B CA  
3891 C C   . MET B 169 ? 0.33090 0.28240 0.47960 -0.04830 0.03340  -0.04260 163 MET B C   
3892 O O   . MET B 169 ? 0.27270 0.23050 0.41560 -0.04940 0.02360  -0.03570 163 MET B O   
3893 C CB  . MET B 169 ? 0.31680 0.25050 0.43460 -0.06430 0.04360  -0.06000 163 MET B CB  
3894 C CG  . MET B 169 ? 0.35370 0.27490 0.45130 -0.07220 0.04400  -0.06650 163 MET B CG  
3895 S SD  . MET B 169 ? 0.43550 0.35790 0.52120 -0.07330 0.02810  -0.05640 163 MET B SD  
3896 C CE  . MET B 169 ? 0.25490 0.18950 0.33240 -0.07590 0.01950  -0.04900 163 MET B CE  
3897 N N   . GLN B 170 ? 0.28150 0.23960 0.44840 -0.04150 0.03990  -0.04260 164 GLN B N   
3898 C CA  . GLN B 170 ? 0.30610 0.27990 0.48460 -0.03610 0.03440  -0.03420 164 GLN B CA  
3899 C C   . GLN B 170 ? 0.27890 0.25590 0.46820 -0.02960 0.02640  -0.02430 164 GLN B C   
3900 O O   . GLN B 170 ? 0.29600 0.28300 0.48470 -0.02870 0.01800  -0.01710 164 GLN B O   
3901 C CB  . GLN B 170 ? 0.33750 0.31960 0.53320 -0.03140 0.04310  -0.03650 164 GLN B CB  
3902 C CG  . GLN B 170 ? 0.35440 0.33490 0.53870 -0.03840 0.05200  -0.04600 164 GLN B CG  
3903 C CD  . GLN B 170 ? 0.39360 0.37750 0.55730 -0.04650 0.04560  -0.04510 164 GLN B CD  
3904 O OE1 . GLN B 170 ? 0.34530 0.33780 0.50930 -0.04540 0.03610  -0.03740 164 GLN B OE1 
3905 N NE2 . GLN B 170 ? 0.41880 0.39510 0.56420 -0.05500 0.05100  -0.05290 164 GLN B NE2 
3906 N N   . GLY B 171 ? 0.29800 0.26560 0.49590 -0.02590 0.02910  -0.02410 165 GLY B N   
3907 C CA  . GLY B 171 ? 0.24610 0.21460 0.44980 -0.02160 0.02130  -0.01480 165 GLY B CA  
3908 C C   . GLY B 171 ? 0.26600 0.23360 0.45220 -0.02740 0.01240  -0.01220 165 GLY B C   
3909 O O   . GLY B 171 ? 0.27460 0.24990 0.46220 -0.02510 0.00460  -0.00390 165 GLY B O   
3910 N N   . ARG B 172 ? 0.23910 0.19740 0.40880 -0.03530 0.01350  -0.01910 166 ARG B N   
3911 C CA  . ARG B 172 ? 0.24150 0.20030 0.39510 -0.03980 0.00500  -0.01570 166 ARG B CA  
3912 C C   . ARG B 172 ? 0.23470 0.20480 0.38300 -0.04110 -0.00010 -0.01240 166 ARG B C   
3913 O O   . ARG B 172 ? 0.25110 0.22660 0.39420 -0.03950 -0.00710 -0.00590 166 ARG B O   
3914 C CB  . ARG B 172 ? 0.25120 0.20030 0.38510 -0.04690 0.00620  -0.02230 166 ARG B CB  
3915 C CG  . ARG B 172 ? 0.26200 0.20090 0.39570 -0.04630 0.00760  -0.02350 166 ARG B CG  
3916 C CD  . ARG B 172 ? 0.28310 0.21200 0.40160 -0.05390 0.01160  -0.03240 166 ARG B CD  
3917 N NE  . ARG B 172 ? 0.29290 0.21250 0.41010 -0.05420 0.01210  -0.03330 166 ARG B NE  
3918 C CZ  . ARG B 172 ? 0.31210 0.22950 0.41550 -0.05890 0.00550  -0.03110 166 ARG B CZ  
3919 N NH1 . ARG B 172 ? 0.28900 0.21180 0.37850 -0.06370 -0.00160 -0.02800 166 ARG B NH1 
3920 N NH2 . ARG B 172 ? 0.24900 0.15880 0.35400 -0.05870 0.00620  -0.03140 166 ARG B NH2 
3921 N N   . VAL B 173 ? 0.21680 0.19090 0.36490 -0.04350 0.00430  -0.01700 167 VAL B N   
3922 C CA  . VAL B 173 ? 0.20000 0.18430 0.34400 -0.04500 0.00020  -0.01410 167 VAL B CA  
3923 C C   . VAL B 173 ? 0.21320 0.20840 0.36970 -0.03860 -0.00440 -0.00640 167 VAL B C   
3924 O O   . VAL B 173 ? 0.21880 0.21910 0.36780 -0.03890 -0.01060 -0.00190 167 VAL B O   
3925 C CB  . VAL B 173 ? 0.24820 0.23530 0.39020 -0.04790 0.00710  -0.02010 167 VAL B CB  
3926 C CG1 . VAL B 173 ? 0.22530 0.22400 0.36770 -0.04840 0.00380  -0.01680 167 VAL B CG1 
3927 C CG2 . VAL B 173 ? 0.27860 0.25580 0.40300 -0.05620 0.00990  -0.02680 167 VAL B CG2 
3928 N N   . LYS B 174 ? 0.23080 0.22990 0.40350 -0.03210 -0.00100 -0.00470 168 LYS B N   
3929 C CA  . LYS B 174 ? 0.23610 0.24710 0.42000 -0.02690 -0.00610 0.00310  168 LYS B CA  
3930 C C   . LYS B 174 ? 0.23430 0.24350 0.41420 -0.02620 -0.01300 0.00950  168 LYS B C   
3931 O O   . LYS B 174 ? 0.22610 0.24350 0.40350 -0.02640 -0.01880 0.01410  168 LYS B O   
3932 C CB  . LYS B 174 ? 0.27550 0.29090 0.47940 -0.01970 -0.00180 0.00520  168 LYS B CB  
3933 C CG  . LYS B 174 ? 0.31990 0.34310 0.53230 -0.01940 0.00410  0.00100  168 LYS B CG  
3934 C CD  . LYS B 174 ? 0.38490 0.41640 0.62130 -0.01120 0.00660  0.00560  168 LYS B CD  
3935 C CE  . LYS B 174 ? 0.39740 0.43760 0.64460 -0.01090 0.01350  0.00110  168 LYS B CE  
3936 N NZ  . LYS B 174 ? 0.39290 0.42230 0.62960 -0.01610 0.02320  -0.00990 168 LYS B NZ  
3937 N N   . ARG B 175 ? 0.22290 0.22120 0.40190 -0.02570 -0.01200 0.00940  169 ARG B N   
3938 C CA  A ARG B 175 ? 0.23360 0.22970 0.40900 -0.02550 -0.01750 0.01520  169 ARG B CA  
3939 C CA  B ARG B 175 ? 0.23360 0.22970 0.40900 -0.02550 -0.01750 0.01520  169 ARG B CA  
3940 C C   . ARG B 175 ? 0.23650 0.23370 0.39300 -0.02920 -0.02140 0.01430  169 ARG B C   
3941 O O   . ARG B 175 ? 0.21430 0.21640 0.36700 -0.02790 -0.02580 0.01920  169 ARG B O   
3942 C CB  A ARG B 175 ? 0.24100 0.22440 0.41750 -0.02560 -0.01490 0.01400  169 ARG B CB  
3943 C CB  B ARG B 175 ? 0.24090 0.22430 0.41780 -0.02540 -0.01470 0.01390  169 ARG B CB  
3944 C CG  A ARG B 175 ? 0.25350 0.23620 0.44370 -0.01920 -0.01460 0.02070  169 ARG B CG  
3945 C CG  B ARG B 175 ? 0.27080 0.25220 0.44120 -0.02440 -0.01890 0.01910  169 ARG B CG  
3946 C CD  A ARG B 175 ? 0.24450 0.21610 0.43130 -0.01990 -0.01390 0.02080  169 ARG B CD  
3947 C CD  B ARG B 175 ? 0.25580 0.22660 0.42730 -0.02350 -0.01560 0.01750  169 ARG B CD  
3948 N NE  A ARG B 175 ? 0.25320 0.21590 0.42810 -0.02410 -0.00960 0.01150  169 ARG B NE  
3949 N NE  B ARG B 175 ? 0.28360 0.24640 0.44340 -0.02820 -0.01180 0.00870  169 ARG B NE  
3950 C CZ  A ARG B 175 ? 0.27590 0.23100 0.45690 -0.02420 -0.00260 0.00510  169 ARG B CZ  
3951 C CZ  B ARG B 175 ? 0.28440 0.24620 0.42660 -0.03290 -0.01430 0.00610  169 ARG B CZ  
3952 N NH1 A ARG B 175 ? 0.24680 0.20220 0.44750 -0.01910 0.00170  0.00690  169 ARG B NH1 
3953 N NH1 B ARG B 175 ? 0.27350 0.24160 0.40840 -0.03270 -0.01930 0.01040  169 ARG B NH1 
3954 N NH2 A ARG B 175 ? 0.27070 0.21740 0.43790 -0.02950 0.00050  -0.00290 169 ARG B NH2 
3955 N NH2 B ARG B 175 ? 0.26250 0.21640 0.39480 -0.03810 -0.01140 -0.00080 169 ARG B NH2 
3956 N N   . THR B 176 ? 0.21240 0.20460 0.35540 -0.03340 -0.01920 0.00820  170 THR B N   
3957 C CA  . THR B 176 ? 0.23690 0.22900 0.36230 -0.03580 -0.02200 0.00820  170 THR B CA  
3958 C C   . THR B 176 ? 0.20810 0.20830 0.33070 -0.03550 -0.02400 0.00980  170 THR B C   
3959 O O   . THR B 176 ? 0.22010 0.22130 0.33430 -0.03500 -0.02650 0.01200  170 THR B O   
3960 C CB  . THR B 176 ? 0.23130 0.21730 0.34480 -0.04120 -0.01960 0.00260  170 THR B CB  
3961 O OG1 . THR B 176 ? 0.24660 0.22440 0.36160 -0.04210 -0.01740 0.00020  170 THR B OG1 
3962 C CG2 . THR B 176 ? 0.21370 0.19980 0.31240 -0.04320 -0.02240 0.00380  170 THR B CG2 
3963 N N   . VAL B 177 ? 0.22110 0.22700 0.35080 -0.03610 -0.02210 0.00790  171 VAL B N   
3964 C CA  . VAL B 177 ? 0.20320 0.21690 0.33000 -0.03640 -0.02360 0.00880  171 VAL B CA  
3965 C C   . VAL B 177 ? 0.21880 0.23780 0.34960 -0.03320 -0.02750 0.01410  171 VAL B C   
3966 O O   . VAL B 177 ? 0.23550 0.25550 0.35680 -0.03380 -0.02930 0.01490  171 VAL B O   
3967 C CB  . VAL B 177 ? 0.20430 0.22440 0.34040 -0.03760 -0.02050 0.00600  171 VAL B CB  
3968 C CG1 . VAL B 177 ? 0.20340 0.23280 0.33810 -0.03760 -0.02270 0.00750  171 VAL B CG1 
3969 C CG2 . VAL B 177 ? 0.20020 0.21480 0.32760 -0.04250 -0.01670 0.00070  171 VAL B CG2 
3970 N N   . ALA B 178 ? 0.21450 0.23670 0.35990 -0.03000 -0.02850 0.01800  172 ALA B N   
3971 C CA  . ALA B 178 ? 0.23510 0.26300 0.38330 -0.02780 -0.03260 0.02400  172 ALA B CA  
3972 C C   . ALA B 178 ? 0.22770 0.24930 0.36580 -0.02810 -0.03420 0.02590  172 ALA B C   
3973 O O   . ALA B 178 ? 0.24810 0.27340 0.38090 -0.02870 -0.03650 0.02830  172 ALA B O   
3974 C CB  . ALA B 178 ? 0.16460 0.19720 0.33150 -0.02390 -0.03340 0.02940  172 ALA B CB  
3975 N N   . GLU B 179 ? 0.18910 0.20180 0.32490 -0.02820 -0.03250 0.02460  173 GLU B N   
3976 C CA  . GLU B 179 ? 0.21080 0.21890 0.33850 -0.02810 -0.03350 0.02620  173 GLU B CA  
3977 C C   . GLU B 179 ? 0.26090 0.26910 0.37590 -0.02990 -0.03310 0.02340  173 GLU B C   
3978 O O   . GLU B 179 ? 0.27350 0.28270 0.38510 -0.02990 -0.03410 0.02550  173 GLU B O   
3979 C CB  . GLU B 179 ? 0.22470 0.22480 0.35160 -0.02810 -0.03180 0.02450  173 GLU B CB  
3980 C CG  . GLU B 179 ? 0.22470 0.22260 0.36490 -0.02600 -0.03150 0.02810  173 GLU B CG  
3981 C CD  . GLU B 179 ? 0.30490 0.29430 0.44320 -0.02680 -0.02890 0.02460  173 GLU B CD  
3982 O OE1 . GLU B 179 ? 0.31560 0.30190 0.44230 -0.02970 -0.02800 0.01980  173 GLU B OE1 
3983 O OE2 . GLU B 179 ? 0.39590 0.38170 0.54410 -0.02490 -0.02780 0.02700  173 GLU B OE2 
3984 N N   . LEU B 180 ? 0.20720 0.21390 0.31610 -0.03180 -0.03120 0.01890  174 LEU B N   
3985 C CA  . LEU B 180 ? 0.21510 0.22160 0.31450 -0.03330 -0.03070 0.01710  174 LEU B CA  
3986 C C   . LEU B 180 ? 0.23180 0.24410 0.33120 -0.03390 -0.03130 0.01740  174 LEU B C   
3987 O O   . LEU B 180 ? 0.25220 0.26380 0.34650 -0.03460 -0.03090 0.01690  174 LEU B O   
3988 C CB  . LEU B 180 ? 0.18330 0.18790 0.27690 -0.03600 -0.02880 0.01330  174 LEU B CB  
3989 C CG  . LEU B 180 ? 0.27160 0.27040 0.36130 -0.03710 -0.02840 0.01250  174 LEU B CG  
3990 C CD1 . LEU B 180 ? 0.23690 0.23470 0.32130 -0.04100 -0.02660 0.00900  174 LEU B CD1 
3991 C CD2 . LEU B 180 ? 0.24120 0.23770 0.32690 -0.03600 -0.02970 0.01470  174 LEU B CD2 
3992 N N   . CYS B 181 ? 0.20870 0.22730 0.31460 -0.03400 -0.03220 0.01780  175 CYS B N   
3993 C CA  . CYS B 181 ? 0.20850 0.23420 0.31410 -0.03530 -0.03350 0.01810  175 CYS B CA  
3994 C C   . CYS B 181 ? 0.20980 0.23810 0.31730 -0.03490 -0.03610 0.02240  175 CYS B C   
3995 O O   . CYS B 181 ? 0.22590 0.25950 0.33060 -0.03720 -0.03720 0.02200  175 CYS B O   
3996 C CB  . CYS B 181 ? 0.19840 0.23230 0.31160 -0.03540 -0.03430 0.01800  175 CYS B CB  
3997 S SG  . CYS B 181 ? 0.23040 0.26430 0.34210 -0.03770 -0.03090 0.01270  175 CYS B SG  
3998 N N   . ASP B 182 ? 0.24760 0.25190 0.35580 -0.05810 0.04020  0.04200  176 ASP B N   
3999 C CA  . ASP B 182 ? 0.29400 0.29470 0.39480 -0.06280 0.04430  0.04860  176 ASP B CA  
4000 C C   . ASP B 182 ? 0.29740 0.28650 0.38810 -0.06010 0.04230  0.05610  176 ASP B C   
4001 O O   . ASP B 182 ? 0.30700 0.29720 0.38770 -0.06160 0.04480  0.06140  176 ASP B O   
4002 C CB  . ASP B 182 ? 0.28580 0.30070 0.38630 -0.06500 0.04980  0.04740  176 ASP B CB  
4003 C CG  . ASP B 182 ? 0.32280 0.34980 0.43450 -0.06670 0.05020  0.04040  176 ASP B CG  
4004 O OD1 . ASP B 182 ? 0.33780 0.36140 0.45390 -0.07040 0.04810  0.03890  176 ASP B OD1 
4005 O OD2 . ASP B 182 ? 0.31100 0.35070 0.42760 -0.06410 0.05210  0.03640  176 ASP B OD2 
4006 N N   . LEU B 183 ? 0.27470 0.25300 0.36690 -0.05600 0.03730  0.05570  177 LEU B N   
4007 C CA  . LEU B 183 ? 0.29650 0.26450 0.38130 -0.05170 0.03340  0.06170  177 LEU B CA  
4008 C C   . LEU B 183 ? 0.33370 0.28540 0.42200 -0.05400 0.03180  0.06650  177 LEU B C   
4009 O O   . LEU B 183 ? 0.30360 0.25200 0.39940 -0.05640 0.03220  0.06110  177 LEU B O   
4010 C CB  . LEU B 183 ? 0.27890 0.24900 0.36500 -0.04360 0.02890  0.05640  177 LEU B CB  
4011 C CG  . LEU B 183 ? 0.30380 0.28680 0.38550 -0.04030 0.02940  0.05270  177 LEU B CG  
4012 C CD1 . LEU B 183 ? 0.25920 0.24250 0.34350 -0.03360 0.02510  0.04760  177 LEU B CD1 
4013 C CD2 . LEU B 183 ? 0.30410 0.28830 0.37390 -0.04110 0.03020  0.05930  177 LEU B CD2 
4014 N N   . ASP B 184 ? 0.29540 0.23700 0.37660 -0.05300 0.02920  0.07570  178 ASP B N   
4015 C CA  . ASP B 184 ? 0.37720 0.30230 0.46190 -0.05190 0.02580  0.07870  178 ASP B CA  
4016 C C   . ASP B 184 ? 0.36300 0.28420 0.45850 -0.04460 0.02210  0.07250  178 ASP B C   
4017 O O   . ASP B 184 ? 0.29770 0.22830 0.39240 -0.03910 0.02040  0.06790  178 ASP B O   
4018 C CB  . ASP B 184 ? 0.41540 0.33090 0.48970 -0.05170 0.02250  0.09050  178 ASP B CB  
4019 C CG  . ASP B 184 ? 0.49370 0.41120 0.55580 -0.06010 0.02700  0.09630  178 ASP B CG  
4020 O OD1 . ASP B 184 ? 0.53880 0.45470 0.60280 -0.06650 0.03130  0.09320  178 ASP B OD1 
4021 O OD2 . ASP B 184 ? 0.59980 0.52100 0.64970 -0.06090 0.02640  0.10360  178 ASP B OD2 
4022 N N   . ALA B 185 ? 0.35630 0.26550 0.45850 -0.04390 0.02080  0.06960  179 ALA B N   
4023 C CA  . ALA B 185 ? 0.35040 0.25570 0.46320 -0.03750 0.01860  0.06210  179 ALA B CA  
4024 C C   . ALA B 185 ? 0.32350 0.22930 0.43730 -0.02950 0.01390  0.06610  179 ALA B C   
4025 O O   . ALA B 185 ? 0.29860 0.21240 0.41590 -0.02440 0.01320  0.05800  179 ALA B O   
4026 C CB  . ALA B 185 ? 0.32540 0.21610 0.44420 -0.03790 0.01800  0.05990  179 ALA B CB  
4027 N N   . GLY B 186 ? 0.36390 0.26340 0.47180 -0.02800 0.01000  0.07730  180 GLY B N   
4028 C CA  . GLY B 186 ? 0.32680 0.22830 0.43570 -0.02020 0.00410  0.08060  180 GLY B CA  
4029 C C   . GLY B 186 ? 0.39280 0.31150 0.49290 -0.01870 0.00420  0.07730  180 GLY B C   
4030 O O   . GLY B 186 ? 0.38040 0.30330 0.48220 -0.01230 -0.00040 0.07740  180 GLY B O   
4031 N N   . ASP B 187 ? 0.32790 0.25670 0.42020 -0.02430 0.00930  0.07410  181 ASP B N   
4032 C CA  . ASP B 187 ? 0.32660 0.27060 0.41210 -0.02300 0.01000  0.06990  181 ASP B CA  
4033 C C   . ASP B 187 ? 0.29710 0.24900 0.38960 -0.02080 0.01200  0.05800  181 ASP B C   
4034 O O   . ASP B 187 ? 0.31580 0.27890 0.40400 -0.01930 0.01240  0.05420  181 ASP B O   
4035 C CB  . ASP B 187 ? 0.37980 0.33060 0.45420 -0.02980 0.01440  0.07300  181 ASP B CB  
4036 C CG  . ASP B 187 ? 0.41380 0.36090 0.47590 -0.03200 0.01200  0.08460  181 ASP B CG  
4037 O OD1 . ASP B 187 ? 0.51870 0.46450 0.57830 -0.02710 0.00590  0.08870  181 ASP B OD1 
4038 O OD2 . ASP B 187 ? 0.49760 0.44390 0.55230 -0.03920 0.01620  0.08950  181 ASP B OD2 
4039 N N   . VAL B 188 ? 0.28670 0.23240 0.38890 -0.02110 0.01340  0.05220  182 VAL B N   
4040 C CA  . VAL B 188 ? 0.22890 0.18050 0.33660 -0.01930 0.01460  0.04160  182 VAL B CA  
4041 C C   . VAL B 188 ? 0.31630 0.26160 0.43340 -0.01330 0.01220  0.03870  182 VAL B C   
4042 O O   . VAL B 188 ? 0.29820 0.23120 0.42270 -0.01280 0.01160  0.04050  182 VAL B O   
4043 C CB  . VAL B 188 ? 0.25250 0.20350 0.36330 -0.02510 0.01830  0.03570  182 VAL B CB  
4044 C CG1 . VAL B 188 ? 0.22650 0.18450 0.33970 -0.02420 0.01900  0.02560  182 VAL B CG1 
4045 C CG2 . VAL B 188 ? 0.23900 0.19680 0.34400 -0.03070 0.02070  0.03910  182 VAL B CG2 
4046 N N   . GLU B 189 ? 0.25980 0.21340 0.37800 -0.00900 0.01110  0.03400  183 GLU B N   
4047 C CA  . GLU B 189 ? 0.28500 0.23570 0.41420 -0.00340 0.00990  0.02920  183 GLU B CA  
4048 C C   . GLU B 189 ? 0.21410 0.16790 0.34680 -0.00540 0.01420  0.01760  183 GLU B C   
4049 O O   . GLU B 189 ? 0.24010 0.20110 0.36540 -0.00980 0.01630  0.01420  183 GLU B O   
4050 C CB  . GLU B 189 ? 0.29190 0.25070 0.42070 0.00190  0.00600  0.03160  183 GLU B CB  
4051 C CG  . GLU B 189 ? 0.35430 0.30860 0.48030 0.00400  0.00050  0.04320  183 GLU B CG  
4052 C CD  . GLU B 189 ? 0.50580 0.47050 0.62780 0.00720  -0.00370 0.04550  183 GLU B CD  
4053 O OE1 . GLU B 189 ? 0.51550 0.48730 0.64480 0.01070  -0.00370 0.03860  183 GLU B OE1 
4054 O OE2 . GLU B 189 ? 0.57900 0.54550 0.69000 0.00540  -0.00660 0.05360  183 GLU B OE2 
4055 N N   . TRP B 190 ? 0.24850 0.19690 0.39280 -0.00220 0.01540  0.01130  184 TRP B N   
4056 C CA  . TRP B 190 ? 0.19240 0.14210 0.33910 -0.00530 0.02020  -0.00040 184 TRP B CA  
4057 C C   . TRP B 190 ? 0.26740 0.22170 0.42310 -0.00050 0.02170  -0.00790 184 TRP B C   
4058 O O   . TRP B 190 ? 0.25710 0.20650 0.42540 0.00570  0.02000  -0.00680 184 TRP B O   
4059 C CB  . TRP B 190 ? 0.22540 0.16230 0.37790 -0.00850 0.02260  -0.00360 184 TRP B CB  
4060 C CG  . TRP B 190 ? 0.20530 0.13960 0.34960 -0.01470 0.02210  0.00230  184 TRP B CG  
4061 C CD1 . TRP B 190 ? 0.25250 0.18030 0.39540 -0.01490 0.01950  0.01300  184 TRP B CD1 
4062 C CD2 . TRP B 190 ? 0.24690 0.18680 0.38330 -0.02200 0.02400  -0.00180 184 TRP B CD2 
4063 N NE1 . TRP B 190 ? 0.26270 0.19230 0.39840 -0.02190 0.02080  0.01500  184 TRP B NE1 
4064 C CE2 . TRP B 190 ? 0.25960 0.19690 0.39240 -0.02600 0.02300  0.00600  184 TRP B CE2 
4065 C CE3 . TRP B 190 ? 0.26310 0.21050 0.39520 -0.02590 0.02620  -0.01080 184 TRP B CE3 
4066 C CZ2 . TRP B 190 ? 0.26960 0.21240 0.39720 -0.03300 0.02400  0.00450  184 TRP B CZ2 
4067 C CZ3 . TRP B 190 ? 0.22670 0.17860 0.35220 -0.03280 0.02600  -0.01130 184 TRP B CZ3 
4068 C CH2 . TRP B 190 ? 0.25360 0.20370 0.37830 -0.03590 0.02490  -0.00410 184 TRP B CH2 
4069 N N   . GLY B 191 ? 0.25870 0.22250 0.40880 -0.00360 0.02490  -0.01540 185 GLY B N   
4070 C CA  . GLY B 191 ? 0.25840 0.22760 0.41640 -0.00110 0.02830  -0.02460 185 GLY B CA  
4071 C C   . GLY B 191 ? 0.26330 0.23160 0.41860 -0.00720 0.03420  -0.03590 185 GLY B C   
4072 O O   . GLY B 191 ? 0.26060 0.22210 0.41140 -0.01210 0.03480  -0.03650 185 GLY B O   
4073 N N   . THR B 192 ? 0.25880 0.23420 0.41640 -0.00780 0.03890  -0.04520 186 THR B N   
4074 C CA  . THR B 192 ? 0.24990 0.22550 0.40240 -0.01470 0.04500  -0.05680 186 THR B CA  
4075 C C   . THR B 192 ? 0.27630 0.26290 0.41400 -0.02030 0.04580  -0.05760 186 THR B C   
4076 O O   . THR B 192 ? 0.25140 0.24630 0.39060 -0.01770 0.04580  -0.05640 186 THR B O   
4077 C CB  . THR B 192 ? 0.24010 0.21420 0.40780 -0.01170 0.05130  -0.06850 186 THR B CB  
4078 O OG1 . THR B 192 ? 0.28210 0.24370 0.46450 -0.00640 0.05020  -0.06760 186 THR B OG1 
4079 C CG2 . THR B 192 ? 0.28640 0.26240 0.44540 -0.02040 0.05860  -0.08160 186 THR B CG2 
4080 N N   . ASP B 193 ? 0.27300 0.25950 0.39690 -0.02840 0.04600  -0.05930 187 ASP B N   
4081 C CA  . ASP B 193 ? 0.27090 0.26580 0.37960 -0.03400 0.04490  -0.05730 187 ASP B CA  
4082 C C   . ASP B 193 ? 0.26600 0.26670 0.37050 -0.03890 0.05140  -0.06760 187 ASP B C   
4083 O O   . ASP B 193 ? 0.27730 0.27590 0.39020 -0.03870 0.05750  -0.07800 187 ASP B O   
4084 C CB  . ASP B 193 ? 0.31310 0.30630 0.41000 -0.04050 0.04130  -0.05420 187 ASP B CB  
4085 C CG  . ASP B 193 ? 0.36550 0.36460 0.45310 -0.04120 0.03580  -0.04460 187 ASP B CG  
4086 O OD1 . ASP B 193 ? 0.32740 0.33200 0.41340 -0.03920 0.03600  -0.04250 187 ASP B OD1 
4087 O OD2 . ASP B 193 ? 0.34930 0.34750 0.43250 -0.04370 0.03140  -0.03940 187 ASP B OD2 
4088 N N   . GLY B 194 ? 0.28120 0.28890 0.37200 -0.04400 0.05030  -0.06490 188 GLY B N   
4089 C CA  . GLY B 194 ? 0.34260 0.35570 0.42510 -0.05090 0.05660  -0.07380 188 GLY B CA  
4090 C C   . GLY B 194 ? 0.35650 0.36650 0.43060 -0.05900 0.06010  -0.08300 188 GLY B C   
4091 O O   . GLY B 194 ? 0.32170 0.33470 0.39390 -0.06370 0.06790  -0.09420 188 GLY B O   
4092 N N   . CYS B 195 ? 0.31150 0.31650 0.38050 -0.06150 0.05490  -0.07930 189 CYS B N   
4093 C CA  . CYS B 195 ? 0.38910 0.39090 0.45000 -0.06980 0.05720  -0.08820 189 CYS B CA  
4094 C C   . CYS B 195 ? 0.36270 0.35580 0.43860 -0.06640 0.06160  -0.09680 189 CYS B C   
4095 O O   . CYS B 195 ? 0.35810 0.34720 0.42890 -0.07330 0.06340  -0.10480 189 CYS B O   
4096 C CB  . CYS B 195 ? 0.39310 0.39470 0.44260 -0.07490 0.04900  -0.08050 189 CYS B CB  
4097 S SG  . CYS B 195 ? 0.37460 0.36970 0.43810 -0.06710 0.04280  -0.07100 189 CYS B SG  
4098 N N   . ASN B 196 ? 0.33410 0.32370 0.42840 -0.05620 0.06240  -0.09460 190 ASN B N   
4099 C CA  . ASN B 196 ? 0.29340 0.27390 0.40530 -0.05110 0.06660  -0.10180 190 ASN B CA  
4100 C C   . ASN B 196 ? 0.34430 0.31400 0.46100 -0.05000 0.06170  -0.09660 190 ASN B C   
4101 O O   . ASN B 196 ? 0.40450 0.36420 0.53280 -0.04860 0.06520  -0.10390 190 ASN B O   
4102 C CB  . ASN B 196 ? 0.35350 0.33370 0.46470 -0.05710 0.07590  -0.11860 190 ASN B CB  
4103 C CG  . ASN B 196 ? 0.39840 0.37370 0.53180 -0.04910 0.08190  -0.12660 190 ASN B CG  
4104 O OD1 . ASN B 196 ? 0.37070 0.34580 0.51960 -0.03920 0.07960  -0.12040 190 ASN B OD1 
4105 N ND2 . ASN B 196 ? 0.43090 0.40560 0.56560 -0.05220 0.08770  -0.13660 190 ASN B ND2 
4106 N N   . LEU B 197 ? 0.31650 0.28780 0.42580 -0.05050 0.05410  -0.08420 191 LEU B N   
4107 C CA  . LEU B 197 ? 0.33400 0.29720 0.44800 -0.04930 0.04940  -0.07710 191 LEU B CA  
4108 C C   . LEU B 197 ? 0.31290 0.27460 0.43640 -0.04000 0.04550  -0.06550 191 LEU B C   
4109 O O   . LEU B 197 ? 0.25100 0.22040 0.37310 -0.03590 0.04430  -0.06070 191 LEU B O   
4110 C CB  . LEU B 197 ? 0.31740 0.28540 0.41770 -0.05660 0.04390  -0.07160 191 LEU B CB  
4111 C CG  . LEU B 197 ? 0.40890 0.37750 0.49870 -0.06730 0.04500  -0.08070 191 LEU B CG  
4112 C CD1 . LEU B 197 ? 0.41410 0.39110 0.49200 -0.07220 0.03790  -0.07250 191 LEU B CD1 
4113 C CD2 . LEU B 197 ? 0.36500 0.32190 0.46350 -0.06960 0.04680  -0.08630 191 LEU B CD2 
4114 N N   . PRO B 198 ? 0.28890 0.24090 0.42060 -0.03740 0.04330  -0.06010 192 PRO B N   
4115 C CA  . PRO B 198 ? 0.28930 0.24090 0.42560 -0.03040 0.03880  -0.04760 192 PRO B CA  
4116 C C   . PRO B 198 ? 0.24530 0.20700 0.36950 -0.03250 0.03460  -0.03960 192 PRO B C   
4117 O O   . PRO B 198 ? 0.25900 0.22440 0.37420 -0.03920 0.03340  -0.04040 192 PRO B O   
4118 C CB  . PRO B 198 ? 0.34030 0.27890 0.48390 -0.03040 0.03750  -0.04360 192 PRO B CB  
4119 C CG  . PRO B 198 ? 0.33510 0.26500 0.48430 -0.03440 0.04270  -0.05660 192 PRO B CG  
4120 C CD  . PRO B 198 ? 0.29910 0.23950 0.43550 -0.04160 0.04480  -0.06490 192 PRO B CD  
4121 N N   . THR B 199 ? 0.27080 0.23760 0.39570 -0.02660 0.03210  -0.03240 193 THR B N   
4122 C CA  . THR B 199 ? 0.26290 0.23820 0.37820 -0.02780 0.02860  -0.02530 193 THR B CA  
4123 C C   . THR B 199 ? 0.26920 0.24330 0.38720 -0.02260 0.02540  -0.01510 193 THR B C   
4124 O O   . THR B 199 ? 0.22240 0.19410 0.34740 -0.01680 0.02500  -0.01330 193 THR B O   
4125 C CB  . THR B 199 ? 0.24520 0.22980 0.35420 -0.02820 0.02950  -0.02840 193 THR B CB  
4126 O OG1 . THR B 199 ? 0.23290 0.22420 0.33340 -0.02990 0.02610  -0.02230 193 THR B OG1 
4127 C CG2 . THR B 199 ? 0.25140 0.23820 0.36820 -0.02140 0.03060  -0.02880 193 THR B CG2 
4128 N N   . PRO B 200 ? 0.22710 0.20380 0.34000 -0.02480 0.02310  -0.00860 194 PRO B N   
4129 C CA  . PRO B 200 ? 0.23080 0.20540 0.34480 -0.02140 0.02100  0.00050  194 PRO B CA  
4130 C C   . PRO B 200 ? 0.21600 0.19850 0.32530 -0.01790 0.01920  0.00470  194 PRO B C   
4131 O O   . PRO B 200 ? 0.20810 0.19820 0.31250 -0.01900 0.01910  0.00240  194 PRO B O   
4132 C CB  . PRO B 200 ? 0.21740 0.19140 0.32900 -0.02680 0.02100  0.00360  194 PRO B CB  
4133 C CG  . PRO B 200 ? 0.18810 0.17050 0.29460 -0.03090 0.02070  -0.00110 194 PRO B CG  
4134 C CD  . PRO B 200 ? 0.20890 0.18960 0.31610 -0.03110 0.02250  -0.00960 194 PRO B CD  
4135 N N   . ALA B 201 ? 0.19290 0.17310 0.30340 -0.01410 0.01730  0.01130  195 ALA B N   
4136 C CA  . ALA B 201 ? 0.17630 0.16340 0.28130 -0.01190 0.01540  0.01560  195 ALA B CA  
4137 C C   . ALA B 201 ? 0.21160 0.19670 0.31240 -0.01330 0.01490  0.02330  195 ALA B C   
4138 O O   . ALA B 201 ? 0.20410 0.18110 0.30760 -0.01360 0.01440  0.02740  195 ALA B O   
4139 C CB  . ALA B 201 ? 0.19880 0.18730 0.30750 -0.00650 0.01320  0.01590  195 ALA B CB  
4140 N N   . PHE B 202 ? 0.19990 0.19220 0.29440 -0.01460 0.01540  0.02490  196 PHE B N   
4141 C CA  . PHE B 202 ? 0.18610 0.17830 0.27560 -0.01670 0.01610  0.03120  196 PHE B CA  
4142 C C   . PHE B 202 ? 0.18590 0.18680 0.26930 -0.01620 0.01660  0.03080  196 PHE B C   
4143 O O   . PHE B 202 ? 0.20040 0.20600 0.28440 -0.01440 0.01610  0.02620  196 PHE B O   
4144 C CB  . PHE B 202 ? 0.19830 0.18840 0.29010 -0.02180 0.01880  0.03160  196 PHE B CB  
4145 C CG  . PHE B 202 ? 0.20090 0.19580 0.29610 -0.02390 0.01970  0.02530  196 PHE B CG  
4146 C CD1 . PHE B 202 ? 0.18530 0.18930 0.27910 -0.02430 0.02030  0.02370  196 PHE B CD1 
4147 C CD2 . PHE B 202 ? 0.18620 0.17630 0.28630 -0.02580 0.01960  0.02100  196 PHE B CD2 
4148 C CE1 . PHE B 202 ? 0.18500 0.19340 0.28200 -0.02630 0.01960  0.01940  196 PHE B CE1 
4149 C CE2 . PHE B 202 ? 0.19760 0.19270 0.29890 -0.02870 0.01940  0.01580  196 PHE B CE2 
4150 C CZ  . PHE B 202 ? 0.18540 0.18970 0.28510 -0.02890 0.01880  0.01580  196 PHE B CZ  
4151 N N   . PRO B 203 ? 0.19030 0.19310 0.26750 -0.01800 0.01810  0.03530  197 PRO B N   
4152 C CA  . PRO B 203 ? 0.18050 0.19100 0.25230 -0.01760 0.01930  0.03340  197 PRO B CA  
4153 C C   . PRO B 203 ? 0.17220 0.18840 0.24870 -0.01820 0.02140  0.02800  197 PRO B C   
4154 O O   . PRO B 203 ? 0.16530 0.18180 0.24710 -0.02060 0.02300  0.02730  197 PRO B O   
4155 C CB  . PRO B 203 ? 0.16940 0.18070 0.23380 -0.02110 0.02190  0.03850  197 PRO B CB  
4156 C CG  . PRO B 203 ? 0.21350 0.21580 0.27690 -0.02170 0.01930  0.04530  197 PRO B CG  
4157 C CD  . PRO B 203 ? 0.21250 0.20960 0.28610 -0.02080 0.01860  0.04240  197 PRO B CD  
4158 N N   . LEU B 204 ? 0.19800 0.21840 0.27310 -0.01600 0.02080  0.02440  198 LEU B N   
4159 C CA  . LEU B 204 ? 0.16370 0.18770 0.24380 -0.01560 0.02120  0.02020  198 LEU B CA  
4160 C C   . LEU B 204 ? 0.17200 0.20040 0.25640 -0.01770 0.02440  0.02010  198 LEU B C   
4161 O O   . LEU B 204 ? 0.17830 0.20880 0.26940 -0.01840 0.02360  0.01850  198 LEU B O   
4162 C CB  . LEU B 204 ? 0.13330 0.15950 0.21080 -0.01340 0.02030  0.01720  198 LEU B CB  
4163 C CG  . LEU B 204 ? 0.13350 0.16190 0.21540 -0.01270 0.02000  0.01400  198 LEU B CG  
4164 C CD1 . LEU B 204 ? 0.12380 0.14980 0.20840 -0.01350 0.01740  0.01350  198 LEU B CD1 
4165 C CD2 . LEU B 204 ? 0.14930 0.17850 0.22840 -0.01110 0.01980  0.01120  198 LEU B CD2 
4166 N N   . ASP B 205 ? 0.20460 0.23560 0.28550 -0.01920 0.02800  0.02150  199 ASP B N   
4167 C CA  . ASP B 205 ? 0.19470 0.23190 0.28180 -0.02110 0.03210  0.02030  199 ASP B CA  
4168 C C   . ASP B 205 ? 0.16950 0.20610 0.26300 -0.02430 0.03210  0.02230  199 ASP B C   
4169 O O   . ASP B 205 ? 0.17290 0.21580 0.27580 -0.02550 0.03360  0.02050  199 ASP B O   
4170 C CB  . ASP B 205 ? 0.21280 0.25320 0.29350 -0.02330 0.03730  0.02090  199 ASP B CB  
4171 C CG  . ASP B 205 ? 0.25640 0.29170 0.32910 -0.02690 0.03760  0.02700  199 ASP B CG  
4172 O OD1 . ASP B 205 ? 0.28050 0.30960 0.34720 -0.02530 0.03320  0.03000  199 ASP B OD1 
4173 O OD2 . ASP B 205 ? 0.27510 0.31230 0.34860 -0.03130 0.04180  0.02930  199 ASP B OD2 
4174 N N   . ARG B 206 ? 0.15990 0.18930 0.24980 -0.02590 0.03040  0.02580  200 ARG B N   
4175 C CA  . ARG B 206 ? 0.17600 0.20380 0.27210 -0.02960 0.03050  0.02680  200 ARG B CA  
4176 C C   . ARG B 206 ? 0.17870 0.20740 0.28120 -0.02900 0.02670  0.02320  200 ARG B C   
4177 O O   . ARG B 206 ? 0.18400 0.21490 0.29330 -0.03260 0.02660  0.02260  200 ARG B O   
4178 C CB  . ARG B 206 ? 0.20380 0.22190 0.29530 -0.03130 0.02970  0.03120  200 ARG B CB  
4179 C CG  . ARG B 206 ? 0.20440 0.22070 0.28710 -0.03250 0.03210  0.03630  200 ARG B CG  
4180 C CD  . ARG B 206 ? 0.23700 0.25910 0.32100 -0.03760 0.03770  0.03750  200 ARG B CD  
4181 N NE  . ARG B 206 ? 0.30030 0.32160 0.37320 -0.03980 0.04050  0.04220  200 ARG B NE  
4182 C CZ  . ARG B 206 ? 0.31280 0.32990 0.38090 -0.04530 0.04320  0.04830  200 ARG B CZ  
4183 N NH1 . ARG B 206 ? 0.25170 0.26350 0.32630 -0.04900 0.04340  0.05040  200 ARG B NH1 
4184 N NH2 . ARG B 206 ? 0.33480 0.35270 0.39060 -0.04800 0.04590  0.05230  200 ARG B NH2 
4185 N N   . LEU B 207 ? 0.14600 0.17350 0.24580 -0.02550 0.02360  0.02100  201 LEU B N   
4186 C CA  . LEU B 207 ? 0.15670 0.18630 0.26040 -0.02560 0.02010  0.01820  201 LEU B CA  
4187 C C   . LEU B 207 ? 0.17030 0.20860 0.28180 -0.02540 0.02010  0.01750  201 LEU B C   
4188 O O   . LEU B 207 ? 0.16270 0.20480 0.28070 -0.02780 0.01770  0.01690  201 LEU B O   
4189 C CB  . LEU B 207 ? 0.14760 0.17440 0.24600 -0.02250 0.01770  0.01640  201 LEU B CB  
4190 C CG  . LEU B 207 ? 0.12980 0.15750 0.22900 -0.02390 0.01410  0.01430  201 LEU B CG  
4191 C CD1 . LEU B 207 ? 0.15850 0.18380 0.25880 -0.02830 0.01300  0.01290  201 LEU B CD1 
4192 C CD2 . LEU B 207 ? 0.13810 0.16300 0.23150 -0.02190 0.01300  0.01280  201 LEU B CD2 
4193 N N   . GLY B 208 ? 0.16970 0.21150 0.28160 -0.02260 0.02270  0.01710  202 GLY B N   
4194 C CA  . GLY B 208 ? 0.16620 0.21660 0.28870 -0.02180 0.02380  0.01590  202 GLY B CA  
4195 C C   . GLY B 208 ? 0.15460 0.21060 0.28510 -0.02590 0.02640  0.01660  202 GLY B C   
4196 O O   . GLY B 208 ? 0.15760 0.22120 0.29980 -0.02640 0.02460  0.01570  202 GLY B O   
4197 N N   . ARG B 209 ? 0.16210 0.21420 0.28690 -0.02930 0.02990  0.01860  203 ARG B N   
4198 C CA  . ARG B 209 ? 0.16140 0.21850 0.29330 -0.03420 0.03340  0.01950  203 ARG B CA  
4199 C C   . ARG B 209 ? 0.17300 0.23060 0.31150 -0.03760 0.02880  0.01910  203 ARG B C   
4200 O O   . ARG B 209 ? 0.17250 0.23880 0.32190 -0.04010 0.02890  0.01800  203 ARG B O   
4201 C CB  . ARG B 209 ? 0.15550 0.20630 0.27810 -0.03750 0.03770  0.02300  203 ARG B CB  
4202 C CG  . ARG B 209 ? 0.21010 0.26540 0.33940 -0.04380 0.04220  0.02430  203 ARG B CG  
4203 C CD  . ARG B 209 ? 0.21050 0.25760 0.32960 -0.04830 0.04600  0.02950  203 ARG B CD  
4204 N NE  . ARG B 209 ? 0.21280 0.25910 0.32060 -0.04640 0.04910  0.03110  203 ARG B NE  
4205 C CZ  . ARG B 209 ? 0.27050 0.31570 0.37040 -0.05100 0.05430  0.03520  203 ARG B CZ  
4206 N NH1 . ARG B 209 ? 0.23060 0.27440 0.33280 -0.05790 0.05760  0.03860  203 ARG B NH1 
4207 N NH2 . ARG B 209 ? 0.27100 0.31660 0.35950 -0.04960 0.05640  0.03570  203 ARG B NH2 
4208 N N   . ILE B 210 ? 0.15960 0.20860 0.29110 -0.03760 0.02460  0.01900  204 ILE B N   
4209 C CA  . ILE B 210 ? 0.19050 0.23970 0.32590 -0.04150 0.02020  0.01750  204 ILE B CA  
4210 C C   . ILE B 210 ? 0.16280 0.22200 0.30730 -0.04040 0.01550  0.01620  204 ILE B C   
4211 O O   . ILE B 210 ? 0.17000 0.23590 0.32330 -0.04450 0.01310  0.01540  204 ILE B O   
4212 C CB  . ILE B 210 ? 0.16160 0.20040 0.28720 -0.04110 0.01750  0.01620  204 ILE B CB  
4213 C CG1 . ILE B 210 ? 0.19120 0.21980 0.31130 -0.04190 0.02100  0.01800  204 ILE B CG1 
4214 C CG2 . ILE B 210 ? 0.17010 0.20980 0.29780 -0.04560 0.01300  0.01340  204 ILE B CG2 
4215 C CD1 . ILE B 210 ? 0.16290 0.18280 0.27560 -0.03930 0.01920  0.01630  204 ILE B CD1 
4216 N N   . TYR B 211 ? 0.16100 0.22140 0.30410 -0.03510 0.01370  0.01630  205 TYR B N   
4217 C CA  . TYR B 211 ? 0.14220 0.21050 0.29420 -0.03370 0.00800  0.01630  205 TYR B CA  
4218 C C   . TYR B 211 ? 0.13260 0.21250 0.30050 -0.03220 0.01040  0.01600  205 TYR B C   
4219 O O   . TYR B 211 ? 0.15120 0.23940 0.32980 -0.03260 0.00540  0.01610  205 TYR B O   
4220 C CB  . TYR B 211 ? 0.11880 0.18230 0.26360 -0.02900 0.00500  0.01690  205 TYR B CB  
4221 C CG  . TYR B 211 ? 0.13710 0.19330 0.27010 -0.03190 0.00110  0.01660  205 TYR B CG  
4222 C CD1 . TYR B 211 ? 0.13420 0.18220 0.25770 -0.03340 0.00460  0.01510  205 TYR B CD1 
4223 C CD2 . TYR B 211 ? 0.13280 0.19070 0.26460 -0.03320 -0.00600 0.01770  205 TYR B CD2 
4224 C CE1 . TYR B 211 ? 0.13960 0.18180 0.25380 -0.03600 0.00230  0.01330  205 TYR B CE1 
4225 C CE2 . TYR B 211 ? 0.16060 0.21250 0.28020 -0.03680 -0.00830 0.01640  205 TYR B CE2 
4226 C CZ  . TYR B 211 ? 0.16580 0.21020 0.27730 -0.03810 -0.00350 0.01350  205 TYR B CZ  
4227 O OH  . TYR B 211 ? 0.20580 0.24500 0.30670 -0.04160 -0.00440 0.01070  205 TYR B OH  
4228 N N   . ALA B 212 ? 0.14140 0.22220 0.30990 -0.03080 0.01800  0.01520  206 ALA B N   
4229 C CA  . ALA B 212 ? 0.13590 0.22670 0.31520 -0.03010 0.02140  0.01320  206 ALA B CA  
4230 C C   . ALA B 212 ? 0.18580 0.28110 0.36890 -0.03600 0.02080  0.01300  206 ALA B C   
4231 O O   . ALA B 212 ? 0.16470 0.27060 0.36020 -0.03570 0.01980  0.01150  206 ALA B O   
4232 C CB  . ALA B 212 ? 0.13860 0.22920 0.31420 -0.02900 0.03040  0.01180  206 ALA B CB  
4233 N N   . LYS B 213 ? 0.13570 0.22320 0.30940 -0.04120 0.02140  0.01410  207 LYS B N   
4234 C CA  . LYS B 213 ? 0.16310 0.25400 0.34040 -0.04740 0.02070  0.01350  207 LYS B CA  
4235 C C   . LYS B 213 ? 0.16920 0.26470 0.35220 -0.04890 0.01200  0.01270  207 LYS B C   
4236 O O   . LYS B 213 ? 0.21070 0.31490 0.40240 -0.05250 0.01020  0.01140  207 LYS B O   
4237 C CB  . LYS B 213 ? 0.16240 0.24190 0.32870 -0.05240 0.02390  0.01480  207 LYS B CB  
4238 C CG  . LYS B 213 ? 0.20250 0.27850 0.36300 -0.05290 0.03170  0.01680  207 LYS B CG  
4239 C CD  . LYS B 213 ? 0.22270 0.28590 0.37350 -0.05750 0.03320  0.01940  207 LYS B CD  
4240 C CE  . LYS B 213 ? 0.21580 0.27620 0.36050 -0.05990 0.04050  0.02280  207 LYS B CE  
4241 N NZ  . LYS B 213 ? 0.25170 0.29750 0.38720 -0.06310 0.04090  0.02660  207 LYS B NZ  
4242 N N   . LEU B 214 ? 0.13740 0.22770 0.31490 -0.04720 0.00640  0.01350  208 LEU B N   
4243 C CA  . LEU B 214 ? 0.17580 0.27090 0.35690 -0.04930 -0.00260 0.01340  208 LEU B CA  
4244 C C   . LEU B 214 ? 0.15500 0.26270 0.35060 -0.04540 -0.00660 0.01410  208 LEU B C   
4245 O O   . LEU B 214 ? 0.17220 0.28870 0.37570 -0.04850 -0.01170 0.01350  208 LEU B O   
4246 C CB  . LEU B 214 ? 0.16090 0.24850 0.33250 -0.04820 -0.00730 0.01470  208 LEU B CB  
4247 C CG  . LEU B 214 ? 0.18620 0.26320 0.34500 -0.05350 -0.00700 0.01270  208 LEU B CG  
4248 C CD1 . LEU B 214 ? 0.18530 0.25440 0.33060 -0.05000 -0.00920 0.01320  208 LEU B CD1 
4249 C CD2 . LEU B 214 ? 0.21450 0.29570 0.37430 -0.06100 -0.01290 0.01030  208 LEU B CD2 
4250 N N   . ALA B 215 ? 0.17520 0.28380 0.37520 -0.03840 -0.00450 0.01510  209 ALA B N   
4251 C CA  . ALA B 215 ? 0.14830 0.26720 0.36350 -0.03330 -0.00810 0.01560  209 ALA B CA  
4252 C C   . ALA B 215 ? 0.16470 0.29410 0.39150 -0.03450 -0.00310 0.01270  209 ALA B C   
4253 O O   . ALA B 215 ? 0.19000 0.33020 0.43040 -0.03350 -0.00800 0.01260  209 ALA B O   
4254 C CB  . ALA B 215 ? 0.14510 0.26010 0.36140 -0.02580 -0.00600 0.01630  209 ALA B CB  
4255 N N   . SER B 216 ? 0.16320 0.28990 0.38450 -0.03730 0.00630  0.01080  210 SER B N   
4256 C CA  . SER B 216 ? 0.17380 0.31050 0.40460 -0.04010 0.01180  0.00840  210 SER B CA  
4257 C C   . SER B 216 ? 0.14840 0.29130 0.38350 -0.04690 0.00690  0.00810  210 SER B C   
4258 O O   . SER B 216 ? 0.17680 0.33250 0.42600 -0.04750 0.00610  0.00660  210 SER B O   
4259 C CB  . SER B 216 ? 0.14200 0.27270 0.36260 -0.04300 0.02200  0.00780  210 SER B CB  
4260 O OG  . SER B 216 ? 0.21380 0.35470 0.44310 -0.04580 0.02790  0.00580  210 SER B OG  
4261 N N   . ALA B 217 ? 0.17190 0.30590 0.39510 -0.05220 0.00390  0.00890  211 ALA B N   
4262 C CA  . ALA B 217 ? 0.16810 0.30690 0.39400 -0.05950 -0.00120 0.00780  211 ALA B CA  
4263 C C   . ALA B 217 ? 0.21290 0.36230 0.44970 -0.05720 -0.01160 0.00840  211 ALA B C   
4264 O O   . ALA B 217 ? 0.22580 0.38680 0.47300 -0.06110 -0.01490 0.00690  211 ALA B O   
4265 C CB  . ALA B 217 ? 0.18850 0.31390 0.39880 -0.06490 -0.00230 0.00760  211 ALA B CB  
4266 N N   . ALA B 218 ? 0.19590 0.34160 0.43030 -0.05140 -0.01720 0.01100  212 ALA B N   
4267 C CA  . ALA B 218 ? 0.14500 0.29950 0.38940 -0.04830 -0.02780 0.01320  212 ALA B CA  
4268 C C   . ALA B 218 ? 0.18670 0.35470 0.45060 -0.04360 -0.02630 0.01230  212 ALA B C   
4269 O O   . ALA B 218 ? 0.20410 0.38380 0.47960 -0.04490 -0.03330 0.01250  212 ALA B O   
4270 C CB  . ALA B 218 ? 0.16010 0.30630 0.39770 -0.04260 -0.03280 0.01730  212 ALA B CB  
4271 N N   . ASP B 219 ? 0.18740 0.35460 0.45540 -0.03860 -0.01690 0.01070  213 ASP B N   
4272 C CA  . ASP B 219 ? 0.16510 0.34540 0.45200 -0.03470 -0.01400 0.00860  213 ASP B CA  
4273 C C   . ASP B 219 ? 0.17350 0.36520 0.46770 -0.04210 -0.01120 0.00580  213 ASP B C   
4274 O O   . ASP B 219 ? 0.18700 0.39290 0.49850 -0.04100 -0.01450 0.00490  213 ASP B O   
4275 C CB  . ASP B 219 ? 0.17000 0.34670 0.45720 -0.02940 -0.00340 0.00630  213 ASP B CB  
4276 C CG  . ASP B 219 ? 0.22170 0.39040 0.50790 -0.02100 -0.00640 0.00820  213 ASP B CG  
4277 O OD1 . ASP B 219 ? 0.24420 0.41350 0.53560 -0.01770 -0.01700 0.01180  213 ASP B OD1 
4278 O OD2 . ASP B 219 ? 0.16270 0.32470 0.44290 -0.01820 0.00180  0.00630  213 ASP B OD2 
4279 N N   . GLY B 220 ? 0.17780 0.36350 0.45990 -0.04970 -0.00500 0.00470  214 GLY B N   
4280 C CA  . GLY B 220 ? 0.19490 0.39050 0.48370 -0.05750 -0.00210 0.00260  214 GLY B CA  
4281 C C   . GLY B 220 ? 0.32470 0.52870 0.61940 -0.06210 -0.01270 0.00260  214 GLY B C   
4282 O O   . GLY B 220 ? 0.32500 0.54380 0.63430 -0.06520 -0.01380 0.00090  214 GLY B O   
4283 N N   . SER B 221 ? 0.23340 0.42870 0.51670 -0.06290 -0.02090 0.00430  215 SER B N   
4284 C CA  . SER B 221 ? 0.26850 0.47090 0.55420 -0.06820 -0.03150 0.00390  215 SER B CA  
4285 C C   . SER B 221 ? 0.32280 0.53920 0.62620 -0.06190 -0.04030 0.00580  215 SER B C   
4286 O O   . SER B 221 ? 0.26860 0.49960 0.58460 -0.06570 -0.04480 0.00420  215 SER B O   
4287 C CB  . SER B 221 ? 0.24530 0.43420 0.51250 -0.07080 -0.03720 0.00490  215 SER B CB  
4288 O OG  . SER B 221 ? 0.34210 0.53820 0.61080 -0.07510 -0.04870 0.00460  215 SER B OG  
4289 N N   . ASP B 222 ? 0.27470 0.48670 0.57990 -0.05230 -0.04270 0.00920  216 ASP B N   
4290 C CA  . ASP B 222 ? 0.33350 0.55600 0.65550 -0.04510 -0.05130 0.01200  216 ASP B CA  
4291 C C   . ASP B 222 ? 0.28180 0.52080 0.62560 -0.04350 -0.04660 0.00890  216 ASP B C   
4292 O O   . ASP B 222 ? 0.31360 0.56590 0.67370 -0.04130 -0.05490 0.01000  216 ASP B O   
4293 C CB  . ASP B 222 ? 0.30190 0.51390 0.62150 -0.03530 -0.05200 0.01590  216 ASP B CB  
4294 C CG  . ASP B 222 ? 0.35460 0.56970 0.68200 -0.02960 -0.06560 0.02160  216 ASP B CG  
4295 O OD1 . ASP B 222 ? 0.43730 0.66150 0.76820 -0.03380 -0.07560 0.02300  216 ASP B OD1 
4296 O OD2 . ASP B 222 ? 0.44380 0.65180 0.77360 -0.02120 -0.06650 0.02480  216 ASP B OD2 
4297 N N   . ALA B 223 ? 0.31920 0.55780 0.66350 -0.04490 -0.03350 0.00520  217 ALA B N   
4298 C CA  . ALA B 223 ? 0.32620 0.58000 0.68970 -0.04430 -0.02690 0.00190  217 ALA B CA  
4299 C C   . ALA B 223 ? 0.39880 0.66550 0.76830 -0.05440 -0.02750 -0.00030 217 ALA B C   
4300 O O   . ALA B 223 ? 0.38180 0.66330 0.76870 -0.05500 -0.02280 -0.00280 217 ALA B O   
4301 C CB  . ALA B 223 ? 0.34910 0.59650 0.70770 -0.04280 -0.01250 -0.00070 217 ALA B CB  
4302 N N   . GLY B 224 ? 0.36450 0.62630 0.72050 -0.06280 -0.03300 0.00000  218 GLY B N   
4303 C CA  . GLY B 224 ? 0.40470 0.67760 0.76570 -0.07330 -0.03340 -0.00260 218 GLY B CA  
4304 C C   . GLY B 224 ? 0.47200 0.74090 0.82660 -0.08080 -0.02080 -0.00440 218 GLY B C   
4305 O O   . GLY B 224 ? 0.47340 0.75280 0.83520 -0.08940 -0.01960 -0.00610 218 GLY B O   
4306 N N   . GLU B 225 ? 0.54130 0.79490 0.88220 -0.07810 -0.01200 -0.00350 219 GLU B N   
4307 C CA  . GLU B 225 ? 0.57810 0.82580 0.91130 -0.08480 -0.00050 -0.00390 219 GLU B CA  
4308 C C   . GLU B 225 ? 0.58700 0.82360 0.90450 -0.09520 -0.00210 -0.00370 219 GLU B C   
4309 O O   . GLU B 225 ? 0.58140 0.80680 0.88580 -0.09520 -0.00820 -0.00350 219 GLU B O   
4310 C CB  . GLU B 225 ? 0.55860 0.79340 0.88110 -0.07850 0.00820  -0.00290 219 GLU B CB  
4311 C CG  . GLU B 225 ? 0.54410 0.78640 0.88000 -0.06760 0.00970  -0.00380 219 GLU B CG  
4312 C CD  . GLU B 225 ? 0.60410 0.83330 0.92770 -0.06230 0.01790  -0.00350 219 GLU B CD  
4313 O OE1 . GLU B 225 ? 0.59550 0.80880 0.89980 -0.06510 0.01960  -0.00170 219 GLU B OE1 
4314 O OE2 . GLU B 225 ? 0.67300 0.90820 1.00710 -0.05540 0.02260  -0.00550 219 GLU B OE2 
4315 N N   . GLY B 226 ? 0.49180 0.73120 0.81110 -0.10440 0.00360  -0.00380 220 GLY B N   
4316 C CA  . GLY B 226 ? 0.43250 0.65710 0.73590 -0.11380 0.00450  -0.00300 220 GLY B CA  
4317 C C   . GLY B 226 ? 0.42650 0.63010 0.71060 -0.11020 0.00940  -0.00110 220 GLY B C   
4318 O O   . GLY B 226 ? 0.40920 0.61020 0.69190 -0.10440 0.01670  0.00030  220 GLY B O   
4319 N N   . GLN B 227 ? 0.39730 0.58630 0.66670 -0.11380 0.00520  -0.00140 221 GLN B N   
4320 C CA  . GLN B 227 ? 0.37390 0.54350 0.62600 -0.10970 0.00800  0.00020  221 GLN B CA  
4321 C C   . GLN B 227 ? 0.33860 0.49140 0.57750 -0.11790 0.00930  0.00070  221 GLN B C   
4322 O O   . GLN B 227 ? 0.29650 0.45090 0.53700 -0.12590 0.00450  -0.00110 221 GLN B O   
4323 C CB  . GLN B 227 ? 0.30580 0.47330 0.55370 -0.10280 0.00050  -0.00100 221 GLN B CB  
4324 C CG  . GLN B 227 ? 0.34850 0.52650 0.60720 -0.09240 -0.00060 -0.00020 221 GLN B CG  
4325 C CD  . GLN B 227 ? 0.35220 0.52350 0.60400 -0.08550 -0.00720 0.00060  221 GLN B CD  
4326 O OE1 . GLN B 227 ? 0.33080 0.50200 0.57930 -0.08820 -0.01570 -0.00060 221 GLN B OE1 
4327 N NE2 . GLN B 227 ? 0.27360 0.43920 0.52240 -0.07720 -0.00320 0.00270  221 GLN B NE2 
4328 N N   . SER B 228 ? 0.31370 0.45020 0.54000 -0.11570 0.01560  0.00330  222 SER B N   
4329 C CA  . SER B 228 ? 0.30070 0.41860 0.51460 -0.12110 0.01590  0.00370  222 SER B CA  
4330 C C   . SER B 228 ? 0.32410 0.43650 0.53150 -0.12090 0.00800  0.00030  222 SER B C   
4331 O O   . SER B 228 ? 0.29780 0.41810 0.50720 -0.11550 0.00320  -0.00130 222 SER B O   
4332 C CB  . SER B 228 ? 0.31850 0.42060 0.52060 -0.11730 0.02280  0.00730  222 SER B CB  
4333 O OG  . SER B 228 ? 0.35810 0.45860 0.55550 -0.10830 0.02150  0.00700  222 SER B OG  
4334 N N   . THR B 229 ? 0.29170 0.38990 0.49150 -0.12690 0.00670  -0.00090 223 THR B N   
4335 C CA  . THR B 229 ? 0.27580 0.36720 0.46760 -0.12690 0.00020  -0.00440 223 THR B CA  
4336 C C   . THR B 229 ? 0.29570 0.38080 0.47920 -0.11780 0.00130  -0.00390 223 THR B C   
4337 O O   . THR B 229 ? 0.29950 0.38810 0.48030 -0.11590 -0.00460 -0.00620 223 THR B O   
4338 C CB  . THR B 229 ? 0.32660 0.40050 0.51190 -0.13310 0.00020  -0.00650 223 THR B CB  
4339 O OG1 . THR B 229 ? 0.32640 0.38480 0.50550 -0.13090 0.00800  -0.00360 223 THR B OG1 
4340 C CG2 . THR B 229 ? 0.26260 0.34290 0.45730 -0.14260 -0.00300 -0.00780 223 THR B CG2 
4341 N N   . ARG B 230 ? 0.25670 0.33300 0.43600 -0.11260 0.00840  -0.00030 224 ARG B N   
4342 C CA  . ARG B 230 ? 0.28880 0.35860 0.46090 -0.10430 0.00920  0.00060  224 ARG B CA  
4343 C C   . ARG B 230 ? 0.26950 0.35440 0.44860 -0.09790 0.00650  0.00130  224 ARG B C   
4344 O O   . ARG B 230 ? 0.21850 0.30280 0.39390 -0.09370 0.00230  0.00040  224 ARG B O   
4345 C CB  . ARG B 230 ? 0.26930 0.32680 0.43520 -0.10070 0.01650  0.00480  224 ARG B CB  
4346 C CG  . ARG B 230 ? 0.22770 0.28180 0.38820 -0.09200 0.01690  0.00620  224 ARG B CG  
4347 C CD  . ARG B 230 ? 0.30540 0.34370 0.45730 -0.08940 0.02180  0.00940  224 ARG B CD  
4348 N NE  . ARG B 230 ? 0.30670 0.32990 0.45280 -0.09230 0.02080  0.00680  224 ARG B NE  
4349 C CZ  . ARG B 230 ? 0.36580 0.37360 0.50590 -0.09030 0.02400  0.00940  224 ARG B CZ  
4350 N NH1 . ARG B 230 ? 0.31320 0.31880 0.45050 -0.08630 0.02790  0.01510  224 ARG B NH1 
4351 N NH2 . ARG B 230 ? 0.31550 0.30980 0.45270 -0.09260 0.02320  0.00600  224 ARG B NH2 
4352 N N   . CYS B 231 ? 0.27730 0.37510 0.46700 -0.09710 0.00900  0.00290  225 CYS B N   
4353 C CA  . CYS B 231 ? 0.24480 0.35620 0.44350 -0.09030 0.00620  0.00330  225 CYS B CA  
4354 C C   . CYS B 231 ? 0.21860 0.33950 0.42230 -0.09190 -0.00340 0.00060  225 CYS B C   
4355 O O   . CYS B 231 ? 0.20040 0.32420 0.40490 -0.08590 -0.00830 0.00140  225 CYS B O   
4356 C CB  . CYS B 231 ? 0.28070 0.40440 0.49110 -0.08960 0.01130  0.00450  225 CYS B CB  
4357 S SG  . CYS B 231 ? 0.49400 0.60970 0.69740 -0.08490 0.02160  0.00800  225 CYS B SG  
4358 N N   . ALA B 232 ? 0.23330 0.35840 0.43950 -0.10050 -0.00660 -0.00230 226 ALA B N   
4359 C CA  . ALA B 232 ? 0.22380 0.35760 0.43250 -0.10310 -0.01620 -0.00540 226 ALA B CA  
4360 C C   . ALA B 232 ? 0.25650 0.37900 0.45180 -0.10200 -0.01990 -0.00680 226 ALA B C   
4361 O O   . ALA B 232 ? 0.23040 0.35850 0.42670 -0.09850 -0.02750 -0.00640 226 ALA B O   
4362 C CB  . ALA B 232 ? 0.22470 0.36370 0.43620 -0.11390 -0.01840 -0.00910 226 ALA B CB  
4363 N N   . ALA B 233 ? 0.23850 0.34420 0.42110 -0.10430 -0.01510 -0.00730 227 ALA B N   
4364 C CA  . ALA B 233 ? 0.23920 0.33450 0.40940 -0.10390 -0.01760 -0.00930 227 ALA B CA  
4365 C C   . ALA B 233 ? 0.25080 0.34490 0.41980 -0.09420 -0.01760 -0.00530 227 ALA B C   
4366 O O   . ALA B 233 ? 0.19700 0.29000 0.35980 -0.09310 -0.02310 -0.00570 227 ALA B O   
4367 C CB  . ALA B 233 ? 0.22070 0.29780 0.38060 -0.10740 -0.01280 -0.01030 227 ALA B CB  
4368 N N   . LEU B 234 ? 0.20250 0.29640 0.37610 -0.08780 -0.01160 -0.00120 228 LEU B N   
4369 C CA  . LEU B 234 ? 0.21630 0.31020 0.38970 -0.07910 -0.01180 0.00250  228 LEU B CA  
4370 C C   . LEU B 234 ? 0.17550 0.28290 0.35820 -0.07570 -0.01980 0.00450  228 LEU B C   
4371 O O   . LEU B 234 ? 0.15820 0.26420 0.33720 -0.07110 -0.02400 0.00720  228 LEU B O   
4372 C CB  . LEU B 234 ? 0.21580 0.30730 0.39180 -0.07410 -0.00330 0.00530  228 LEU B CB  
4373 C CG  . LEU B 234 ? 0.21600 0.29220 0.38160 -0.07460 0.00340  0.00560  228 LEU B CG  
4374 C CD1 . LEU B 234 ? 0.24390 0.32120 0.41260 -0.07210 0.01080  0.00850  228 LEU B CD1 
4375 C CD2 . LEU B 234 ? 0.13840 0.20540 0.29480 -0.07040 0.00250  0.00600  228 LEU B CD2 
4376 N N   . ALA B 235 ? 0.16110 0.28140 0.35600 -0.07760 -0.02210 0.00380  229 ALA B N   
4377 C CA  . ALA B 235 ? 0.16240 0.29510 0.36740 -0.07370 -0.03070 0.00630  229 ALA B CA  
4378 C C   . ALA B 235 ? 0.19830 0.33030 0.39460 -0.07770 -0.04090 0.00620  229 ALA B C   
4379 O O   . ALA B 235 ? 0.22330 0.35750 0.41910 -0.07330 -0.04840 0.01050  229 ALA B O   
4380 C CB  . ALA B 235 ? 0.15150 0.29900 0.37280 -0.07520 -0.03060 0.00500  229 ALA B CB  
4381 N N   . HIS B 236 ? 0.20150 0.32890 0.38920 -0.08640 -0.04110 0.00120  230 HIS B N   
4382 C CA  . HIS B 236 ? 0.22770 0.35270 0.40330 -0.09140 -0.04960 -0.00010 230 HIS B CA  
4383 C C   . HIS B 236 ? 0.22930 0.34340 0.39040 -0.08860 -0.04970 0.00250  230 HIS B C   
4384 O O   . HIS B 236 ? 0.27240 0.38780 0.42480 -0.08940 -0.05820 0.00550  230 HIS B O   
4385 C CB  . HIS B 236 ? 0.29410 0.41410 0.46410 -0.10100 -0.04730 -0.00790 230 HIS B CB  
4386 C CG  . HIS B 236 ? 0.34780 0.46850 0.50690 -0.10720 -0.05650 -0.01050 230 HIS B CG  
4387 N ND1 . HIS B 236 ? 0.38680 0.50340 0.54180 -0.11550 -0.05640 -0.01790 230 HIS B ND1 
4388 C CD2 . HIS B 236 ? 0.36980 0.49420 0.51990 -0.10660 -0.06630 -0.00620 230 HIS B CD2 
4389 C CE1 . HIS B 236 ? 0.39680 0.51530 0.53920 -0.11990 -0.06530 -0.01860 230 HIS B CE1 
4390 N NE2 . HIS B 236 ? 0.44750 0.57080 0.58590 -0.11500 -0.07140 -0.01120 230 HIS B NE2 
4391 N N   . ILE B 237 ? 0.21130 0.31450 0.36850 -0.08610 -0.04050 0.00180  231 ILE B N   
4392 C CA  . ILE B 237 ? 0.21640 0.31050 0.36160 -0.08340 -0.04000 0.00400  231 ILE B CA  
4393 C C   . ILE B 237 ? 0.20720 0.30700 0.35810 -0.07570 -0.04480 0.01110  231 ILE B C   
4394 O O   . ILE B 237 ? 0.21000 0.30760 0.35020 -0.07560 -0.05060 0.01410  231 ILE B O   
4395 C CB  . ILE B 237 ? 0.19980 0.28180 0.34220 -0.08120 -0.02940 0.00200  231 ILE B CB  
4396 C CG1 . ILE B 237 ? 0.24890 0.32200 0.38350 -0.08890 -0.02590 -0.00500 231 ILE B CG1 
4397 C CG2 . ILE B 237 ? 0.18600 0.25900 0.31570 -0.07510 -0.02700 0.00350  231 ILE B CG2 
4398 C CD1 . ILE B 237 ? 0.26780 0.33010 0.40430 -0.08660 -0.01600 -0.00630 231 ILE B CD1 
4399 N N   . PHE B 238 ? 0.18950 0.29520 0.35540 -0.06900 -0.04130 0.01330  232 PHE B N   
4400 C CA  . PHE B 238 ? 0.15810 0.26840 0.33170 -0.06120 -0.04540 0.01910  232 PHE B CA  
4401 C C   . PHE B 238 ? 0.21750 0.33480 0.39070 -0.06290 -0.05800 0.02300  232 PHE B C   
4402 O O   . PHE B 238 ? 0.21760 0.33210 0.38490 -0.06060 -0.06400 0.02820  232 PHE B O   
4403 C CB  . PHE B 238 ? 0.16920 0.28650 0.35970 -0.05490 -0.03970 0.01900  232 PHE B CB  
4404 C CG  . PHE B 238 ? 0.17050 0.29020 0.36990 -0.04600 -0.04210 0.02340  232 PHE B CG  
4405 C CD1 . PHE B 238 ? 0.24340 0.37040 0.45050 -0.04370 -0.05220 0.02750  232 PHE B CD1 
4406 C CD2 . PHE B 238 ? 0.13320 0.24690 0.33270 -0.04020 -0.03430 0.02340  232 PHE B CD2 
4407 C CE1 . PHE B 238 ? 0.19160 0.31870 0.40760 -0.03530 -0.05420 0.03150  232 PHE B CE1 
4408 C CE2 . PHE B 238 ? 0.14310 0.25780 0.35090 -0.03240 -0.03610 0.02640  232 PHE B CE2 
4409 C CZ  . PHE B 238 ? 0.12270 0.24350 0.33940 -0.02980 -0.04600 0.03040  232 PHE B CZ  
4410 N N   . ARG B 239 ? 0.21750 0.34400 0.39710 -0.06690 -0.06240 0.02110  233 ARG B N   
4411 C CA  . ARG B 239 ? 0.21970 0.35360 0.39940 -0.06810 -0.07490 0.02540  233 ARG B CA  
4412 C C   . ARG B 239 ? 0.25060 0.37730 0.40800 -0.07490 -0.08110 0.02660  233 ARG B C   
4413 O O   . ARG B 239 ? 0.23390 0.36090 0.38610 -0.07350 -0.09030 0.03340  233 ARG B O   
4414 C CB  . ARG B 239 ? 0.24760 0.39310 0.43780 -0.07230 -0.07770 0.02180  233 ARG B CB  
4415 C CG  . ARG B 239 ? 0.40500 0.55610 0.58870 -0.07720 -0.09040 0.02430  233 ARG B CG  
4416 C CD  . ARG B 239 ? 0.51900 0.68380 0.71760 -0.07960 -0.09360 0.02140  233 ARG B CD  
4417 N NE  . ARG B 239 ? 0.56480 0.73050 0.75210 -0.09020 -0.09720 0.01590  233 ARG B NE  
4418 C CZ  . ARG B 239 ? 0.67330 0.84520 0.85520 -0.09440 -0.10900 0.01820  233 ARG B CZ  
4419 N NH1 . ARG B 239 ? 0.63760 0.81390 0.82270 -0.08900 -0.11910 0.02690  233 ARG B NH1 
4420 N NH2 . ARG B 239 ? 0.71670 0.88960 0.89000 -0.10420 -0.11080 0.01150  233 ARG B NH2 
4421 N N   . ALA B 240 ? 0.21960 0.33900 0.36290 -0.08250 -0.07580 0.02000  234 ALA B N   
4422 C CA  . ALA B 240 ? 0.22050 0.33290 0.34070 -0.08970 -0.07950 0.01920  234 ALA B CA  
4423 C C   . ALA B 240 ? 0.25030 0.35570 0.36210 -0.08590 -0.07980 0.02490  234 ALA B C   
4424 O O   . ALA B 240 ? 0.22570 0.32970 0.32270 -0.08920 -0.08740 0.02930  234 ALA B O   
4425 C CB  . ALA B 240 ? 0.23710 0.34120 0.34660 -0.09670 -0.07100 0.00960  234 ALA B CB  
4426 N N   . MET B 241 ? 0.21270 0.31090 0.32960 -0.07800 -0.06950 0.02400  235 MET B N   
4427 C CA  . MET B 241 ? 0.19010 0.27920 0.29730 -0.07250 -0.06700 0.02770  235 MET B CA  
4428 C C   . MET B 241 ? 0.23230 0.32620 0.34750 -0.06750 -0.07670 0.03710  235 MET B C   
4429 O O   . MET B 241 ? 0.26740 0.35570 0.36900 -0.06830 -0.08110 0.04200  235 MET B O   
4430 C CB  . MET B 241 ? 0.22500 0.30730 0.33780 -0.06540 -0.05510 0.02470  235 MET B CB  
4431 C CG  . MET B 241 ? 0.22150 0.29600 0.32490 -0.06930 -0.04600 0.01680  235 MET B CG  
4432 S SD  . MET B 241 ? 0.23440 0.30180 0.34430 -0.06130 -0.03390 0.01490  235 MET B SD  
4433 C CE  . MET B 241 ? 0.17930 0.23850 0.27800 -0.05610 -0.03220 0.01780  235 MET B CE  
4434 N N   . ALA B 242 ? 0.20120 0.30540 0.33950 -0.06240 -0.08000 0.03970  236 ALA B N   
4435 C CA  . ALA B 242 ? 0.24670 0.35470 0.39690 -0.05570 -0.08840 0.04810  236 ALA B CA  
4436 C C   . ALA B 242 ? 0.25650 0.36880 0.39920 -0.06080 -0.10240 0.05440  236 ALA B C   
4437 O O   . ALA B 242 ? 0.29150 0.40090 0.43370 -0.05710 -0.11010 0.06280  236 ALA B O   
4438 C CB  . ALA B 242 ? 0.21490 0.33140 0.39080 -0.04770 -0.08500 0.04690  236 ALA B CB  
4439 N N   . ARG B 243 ? 0.23960 0.35690 0.37470 -0.06890 -0.10500 0.05020  237 ARG B N   
4440 C CA  . ARG B 243 ? 0.23670 0.35710 0.36150 -0.07370 -0.11730 0.05560  237 ARG B CA  
4441 C C   . ARG B 243 ? 0.28320 0.39530 0.37910 -0.08280 -0.11990 0.05710  237 ARG B C   
4442 O O   . ARG B 243 ? 0.32760 0.43920 0.41200 -0.08580 -0.13000 0.06440  237 ARG B O   
4443 C CB  . ARG B 243 ? 0.30670 0.43760 0.43720 -0.07850 -0.11960 0.05020  237 ARG B CB  
4444 C CG  . ARG B 243 ? 0.39600 0.53680 0.55470 -0.07030 -0.11760 0.04930  237 ARG B CG  
4445 C CD  . ARG B 243 ? 0.55570 0.70900 0.72210 -0.07430 -0.12430 0.04720  237 ARG B CD  
4446 N NE  . ARG B 243 ? 0.67810 0.84140 0.87080 -0.06780 -0.11950 0.04420  237 ARG B NE  
4447 C CZ  . ARG B 243 ? 0.69960 0.86920 0.91170 -0.05880 -0.12330 0.04920  237 ARG B CZ  
4448 N NH1 . ARG B 243 ? 0.71080 0.87720 0.92060 -0.05480 -0.13300 0.05840  237 ARG B NH1 
4449 N NH2 . ARG B 243 ? 0.61070 0.78960 0.84490 -0.05410 -0.11670 0.04470  237 ARG B NH2 
4450 N N   . HIS B 244 ? 0.23900 0.34410 0.32240 -0.08740 -0.11050 0.05010  238 HIS B N   
4451 C CA  . HIS B 244 ? 0.28810 0.38520 0.34310 -0.09640 -0.11010 0.04900  238 HIS B CA  
4452 C C   . HIS B 244 ? 0.24690 0.33140 0.29520 -0.09110 -0.09810 0.04700  238 HIS B C   
4453 O O   . HIS B 244 ? 0.26000 0.33770 0.29450 -0.09530 -0.08820 0.03860  238 HIS B O   
4454 C CB  . HIS B 244 ? 0.29150 0.38960 0.33360 -0.10650 -0.10610 0.03840  238 HIS B CB  
4455 C CG  . HIS B 244 ? 0.29040 0.39780 0.33700 -0.10910 -0.11430 0.03870  238 HIS B CG  
4456 N ND1 . HIS B 244 ? 0.34670 0.45630 0.37860 -0.11450 -0.12490 0.04470  238 HIS B ND1 
4457 C CD2 . HIS B 244 ? 0.28040 0.39580 0.34510 -0.10730 -0.11360 0.03410  238 HIS B CD2 
4458 C CE1 . HIS B 244 ? 0.31050 0.42960 0.35180 -0.11580 -0.13070 0.04330  238 HIS B CE1 
4459 N NE2 . HIS B 244 ? 0.31260 0.43560 0.37410 -0.11160 -0.12390 0.03670  238 HIS B NE2 
4460 N N   . PRO B 245 ? 0.25130 0.33230 0.30980 -0.08190 -0.09900 0.05440  239 PRO B N   
4461 C CA  . PRO B 245 ? 0.24440 0.31430 0.29840 -0.07690 -0.08770 0.05200  239 PRO B CA  
4462 C C   . PRO B 245 ? 0.24890 0.31040 0.27700 -0.08420 -0.08540 0.05180  239 PRO B C   
4463 O O   . PRO B 245 ? 0.28410 0.33790 0.30670 -0.08230 -0.07480 0.04710  239 PRO B O   
4464 C CB  . PRO B 245 ? 0.28220 0.35120 0.35330 -0.06660 -0.09130 0.06020  239 PRO B CB  
4465 C CG  . PRO B 245 ? 0.28330 0.35840 0.35620 -0.06900 -0.10700 0.07010  239 PRO B CG  
4466 C CD  . PRO B 245 ? 0.28810 0.37410 0.36050 -0.07660 -0.11130 0.06560  239 PRO B CD  
4467 N N   . GLU B 246 ? 0.25970 0.32310 0.27150 -0.09290 -0.09490 0.05670  240 GLU B N   
4468 C CA  . GLU B 246 ? 0.28070 0.33690 0.26650 -0.10130 -0.09120 0.05560  240 GLU B CA  
4469 C C   . GLU B 246 ? 0.31390 0.37020 0.28800 -0.10860 -0.08150 0.04230  240 GLU B C   
4470 O O   . GLU B 246 ? 0.27110 0.32150 0.22790 -0.11380 -0.07380 0.03780  240 GLU B O   
4471 C CB  . GLU B 246 ? 0.38500 0.44270 0.35430 -0.10940 -0.10480 0.06590  240 GLU B CB  
4472 C CG  . GLU B 246 ? 0.46130 0.52960 0.42630 -0.11790 -0.11400 0.06400  240 GLU B CG  
4473 C CD  . GLU B 246 ? 0.46670 0.54510 0.45820 -0.11080 -0.12400 0.06880  240 GLU B CD  
4474 O OE1 . GLU B 246 ? 0.53630 0.61320 0.54630 -0.10020 -0.12710 0.07680  240 GLU B OE1 
4475 O OE2 . GLU B 246 ? 0.50540 0.59170 0.49940 -0.11470 -0.12630 0.06350  240 GLU B OE2 
4476 N N   . MET B 247 ? 0.28440 0.34740 0.26850 -0.10960 -0.08170 0.03580  241 MET B N   
4477 C CA  . MET B 247 ? 0.29990 0.36080 0.27760 -0.11450 -0.07110 0.02240  241 MET B CA  
4478 C C   . MET B 247 ? 0.26620 0.32080 0.25550 -0.10570 -0.05850 0.01700  241 MET B C   
4479 O O   . MET B 247 ? 0.25340 0.30300 0.23460 -0.10840 -0.04840 0.00770  241 MET B O   
4480 C CB  . MET B 247 ? 0.24540 0.31400 0.23110 -0.11860 -0.07500 0.01720  241 MET B CB  
4481 C CG  . MET B 247 ? 0.30640 0.38230 0.27810 -0.12950 -0.08730 0.02020  241 MET B CG  
4482 S SD  . MET B 247 ? 0.34180 0.41290 0.28030 -0.14350 -0.08200 0.01170  241 MET B SD  
4483 C CE  . MET B 247 ? 0.32270 0.39260 0.24250 -0.14680 -0.09210 0.02640  241 MET B CE  
4484 N N   . VAL B 248 ? 0.26200 0.31690 0.27020 -0.09520 -0.05900 0.02260  242 VAL B N   
4485 C CA  . VAL B 248 ? 0.25190 0.30140 0.27030 -0.08710 -0.04830 0.01850  242 VAL B CA  
4486 C C   . VAL B 248 ? 0.27780 0.32010 0.28510 -0.08630 -0.04250 0.01890  242 VAL B C   
4487 O O   . VAL B 248 ? 0.27150 0.30940 0.28030 -0.08350 -0.03270 0.01240  242 VAL B O   
4488 C CB  . VAL B 248 ? 0.19270 0.24540 0.23270 -0.07740 -0.05020 0.02370  242 VAL B CB  
4489 C CG1 . VAL B 248 ? 0.17540 0.22260 0.22320 -0.06960 -0.03990 0.02030  242 VAL B CG1 
4490 C CG2 . VAL B 248 ? 0.20770 0.26850 0.25990 -0.07910 -0.05390 0.02160  242 VAL B CG2 
4491 N N   . ALA B 249 ? 0.26860 0.30960 0.26520 -0.08900 -0.04860 0.02670  243 ALA B N   
4492 C CA  . ALA B 249 ? 0.23360 0.26800 0.21940 -0.08970 -0.04270 0.02690  243 ALA B CA  
4493 C C   . ALA B 249 ? 0.30210 0.33570 0.26600 -0.10000 -0.04780 0.03120  243 ALA B C   
4494 O O   . ALA B 249 ? 0.30770 0.34150 0.25600 -0.10870 -0.04270 0.02370  243 ALA B O   
4495 C CB  . ALA B 249 ? 0.22530 0.25590 0.22370 -0.08020 -0.04250 0.03330  243 ALA B CB  
4496 N N   . GLY B 250 ? 0.26750 0.29980 0.22970 -0.09950 -0.05760 0.04300  244 GLY B N   
4497 C CA  . GLY B 250 ? 0.31410 0.34550 0.25410 -0.11010 -0.06410 0.04920  244 GLY B CA  
4498 C C   . GLY B 250 ? 0.34950 0.37490 0.29020 -0.10700 -0.07170 0.06270  244 GLY B C   
4499 O O   . GLY B 250 ? 0.30740 0.33020 0.26690 -0.09660 -0.07210 0.06630  244 GLY B O   
4500 N N   . GLU B 251 ? 0.37370 0.39650 0.29290 -0.11680 -0.07780 0.07020  245 GLU B N   
4501 C CA  . GLU B 251 ? 0.43310 0.44880 0.35350 -0.11410 -0.08680 0.08470  245 GLU B CA  
4502 C C   . GLU B 251 ? 0.37830 0.38520 0.30410 -0.10890 -0.07740 0.08410  245 GLU B C   
4503 O O   . GLU B 251 ? 0.32620 0.33200 0.24370 -0.11250 -0.06520 0.07500  245 GLU B O   
4504 C CB  . GLU B 251 ? 0.48140 0.49530 0.37580 -0.12660 -0.09620 0.09450  245 GLU B CB  
4505 C CG  . GLU B 251 ? 0.58000 0.59240 0.48140 -0.12330 -0.11390 0.11110  245 GLU B CG  
4506 C CD  . GLU B 251 ? 0.66800 0.69190 0.58460 -0.11970 -0.12510 0.11180  245 GLU B CD  
4507 O OE1 . GLU B 251 ? 0.59390 0.62690 0.50740 -0.12410 -0.12200 0.10120  245 GLU B OE1 
4508 O OE2 . GLU B 251 ? 0.72180 0.74550 0.65490 -0.11240 -0.13740 0.12300  245 GLU B OE2 
4509 N N   . GLY B 252 ? 0.34430 0.34550 0.28640 -0.09980 -0.08290 0.09270  246 GLY B N   
4510 C CA  . GLY B 252 ? 0.32950 0.32240 0.27860 -0.09460 -0.07490 0.09180  246 GLY B CA  
4511 C C   . GLY B 252 ? 0.34730 0.34340 0.31270 -0.08650 -0.06360 0.07970  246 GLY B C   
4512 O O   . GLY B 252 ? 0.31790 0.30800 0.29040 -0.08180 -0.05770 0.07870  246 GLY B O   
4513 N N   . ARG B 253 ? 0.26200 0.26700 0.23280 -0.08510 -0.06060 0.07080  247 ARG B N   
4514 C CA  . ARG B 253 ? 0.27540 0.28320 0.25990 -0.07820 -0.05030 0.06020  247 ARG B CA  
4515 C C   . ARG B 253 ? 0.25840 0.26710 0.26610 -0.06680 -0.05310 0.06210  247 ARG B C   
4516 O O   . ARG B 253 ? 0.26150 0.27390 0.27800 -0.06430 -0.06230 0.06770  247 ARG B O   
4517 C CB  . ARG B 253 ? 0.25960 0.27480 0.24020 -0.08200 -0.04590 0.05040  247 ARG B CB  
4518 C CG  . ARG B 253 ? 0.30230 0.31760 0.26150 -0.09310 -0.04070 0.04530  247 ARG B CG  
4519 C CD  . ARG B 253 ? 0.29570 0.30930 0.25570 -0.09190 -0.02790 0.03620  247 ARG B CD  
4520 N NE  . ARG B 253 ? 0.30030 0.31670 0.27770 -0.08350 -0.02290 0.02900  247 ARG B NE  
4521 C CZ  . ARG B 253 ? 0.34060 0.36130 0.31960 -0.08460 -0.01920 0.02050  247 ARG B CZ  
4522 N NH1 . ARG B 253 ? 0.27870 0.30180 0.24330 -0.09390 -0.01920 0.01640  247 ARG B NH1 
4523 N NH2 . ARG B 253 ? 0.26650 0.28840 0.26130 -0.07680 -0.01550 0.01600  247 ARG B NH2 
4524 N N   . TYR B 254 ? 0.24560 0.25250 0.26360 -0.06030 -0.04480 0.05640  248 TYR B N   
4525 C CA  . TYR B 254 ? 0.25260 0.26010 0.29110 -0.05030 -0.04560 0.05700  248 TYR B CA  
4526 C C   . TYR B 254 ? 0.23190 0.24840 0.28250 -0.04720 -0.04880 0.05530  248 TYR B C   
4527 O O   . TYR B 254 ? 0.25020 0.26880 0.31500 -0.04200 -0.05530 0.06030  248 TYR B O   
4528 C CB  . TYR B 254 ? 0.26350 0.26880 0.30770 -0.04560 -0.03560 0.04990  248 TYR B CB  
4529 C CG  . TYR B 254 ? 0.24190 0.24740 0.30480 -0.03630 -0.03520 0.04960  248 TYR B CG  
4530 C CD1 . TYR B 254 ? 0.24540 0.24380 0.31470 -0.03260 -0.03830 0.05470  248 TYR B CD1 
4531 C CD2 . TYR B 254 ? 0.22040 0.23290 0.29440 -0.03170 -0.03150 0.04400  248 TYR B CD2 
4532 C CE1 . TYR B 254 ? 0.22070 0.21940 0.30720 -0.02450 -0.03700 0.05300  248 TYR B CE1 
4533 C CE2 . TYR B 254 ? 0.20850 0.22200 0.29860 -0.02410 -0.03010 0.04300  248 TYR B CE2 
4534 C CZ  . TYR B 254 ? 0.19380 0.20070 0.29020 -0.02040 -0.03260 0.04690  248 TYR B CZ  
4535 O OH  . TYR B 254 ? 0.20820 0.21570 0.32070 -0.01310 -0.03050 0.04460  248 TYR B OH  
4536 N N   . CYS B 255 ? 0.21340 0.23530 0.26020 -0.05040 -0.04420 0.04790  249 CYS B N   
4537 C CA  . CYS B 255 ? 0.22020 0.25040 0.27900 -0.04840 -0.04650 0.04600  249 CYS B CA  
4538 C C   . CYS B 255 ? 0.20260 0.23750 0.26270 -0.05110 -0.05820 0.05320  249 CYS B C   
4539 O O   . CYS B 255 ? 0.20110 0.24260 0.27820 -0.04640 -0.06270 0.05510  249 CYS B O   
4540 C CB  . CYS B 255 ? 0.18620 0.21940 0.23880 -0.05290 -0.04050 0.03760  249 CYS B CB  
4541 S SG  . CYS B 255 ? 0.30150 0.32960 0.34980 -0.05140 -0.02840 0.02960  249 CYS B SG  
4542 N N   . THR B 256 ? 0.24210 0.27470 0.28420 -0.05930 -0.06340 0.05710  250 THR B N   
4543 C CA  . THR B 256 ? 0.22480 0.26190 0.26550 -0.06300 -0.07620 0.06510  250 THR B CA  
4544 C C   . THR B 256 ? 0.26820 0.30280 0.32290 -0.05580 -0.08420 0.07490  250 THR B C   
4545 O O   . THR B 256 ? 0.27950 0.32120 0.34870 -0.05270 -0.09340 0.07960  250 THR B O   
4546 C CB  . THR B 256 ? 0.23450 0.26860 0.24940 -0.07430 -0.07890 0.06710  250 THR B CB  
4547 O OG1 . THR B 256 ? 0.25440 0.29140 0.25930 -0.08040 -0.07110 0.05630  250 THR B OG1 
4548 C CG2 . THR B 256 ? 0.30770 0.34610 0.31820 -0.07900 -0.09320 0.07640  250 THR B CG2 
4549 N N   . MET B 257 ? 0.30810 0.33250 0.36040 -0.05290 -0.08080 0.07770  251 MET B N   
4550 C CA  . MET B 257 ? 0.22540 0.24510 0.29120 -0.04620 -0.08820 0.08680  251 MET B CA  
4551 C C   . MET B 257 ? 0.26460 0.28910 0.35690 -0.03530 -0.08500 0.08270  251 MET B C   
4552 O O   . MET B 257 ? 0.26480 0.29210 0.37510 -0.02940 -0.09310 0.08860  251 MET B O   
4553 C CB  . MET B 257 ? 0.29730 0.30370 0.35200 -0.04750 -0.08480 0.09030  251 MET B CB  
4554 C CG  . MET B 257 ? 0.23340 0.23530 0.26170 -0.05910 -0.08910 0.09630  251 MET B CG  
4555 S SD  . MET B 257 ? 0.39530 0.38200 0.41060 -0.06220 -0.08460 0.10060  251 MET B SD  
4556 C CE  . MET B 257 ? 0.36390 0.34250 0.39930 -0.05310 -0.09570 0.11270  251 MET B CE  
4557 N N   . LEU B 258 ? 0.24420 0.27010 0.33960 -0.03280 -0.07320 0.07270  252 LEU B N   
4558 C CA  . LEU B 258 ? 0.20320 0.23490 0.32100 -0.02420 -0.06880 0.06790  252 LEU B CA  
4559 C C   . LEU B 258 ? 0.24250 0.28720 0.37460 -0.02350 -0.07480 0.06830  252 LEU B C   
4560 O O   . LEU B 258 ? 0.25000 0.29950 0.40350 -0.01660 -0.07910 0.07090  252 LEU B O   
4561 C CB  . LEU B 258 ? 0.25260 0.28360 0.36640 -0.02380 -0.05600 0.05810  252 LEU B CB  
4562 C CG  . LEU B 258 ? 0.22790 0.26600 0.35970 -0.01750 -0.04980 0.05200  252 LEU B CG  
4563 C CD1 . LEU B 258 ? 0.20160 0.23470 0.34630 -0.00990 -0.04800 0.05240  252 LEU B CD1 
4564 C CD2 . LEU B 258 ? 0.23400 0.27270 0.35770 -0.01980 -0.03980 0.04410  252 LEU B CD2 
4565 N N   . MET B 259 ? 0.22370 0.27460 0.34560 -0.03080 -0.07510 0.06520  253 MET B N   
4566 C CA  . MET B 259 ? 0.22050 0.28430 0.35590 -0.03140 -0.08080 0.06500  253 MET B CA  
4567 C C   . MET B 259 ? 0.23630 0.30410 0.37750 -0.03170 -0.09560 0.07500  253 MET B C   
4568 O O   . MET B 259 ? 0.28610 0.36500 0.44870 -0.02780 -0.10110 0.07630  253 MET B O   
4569 C CB  . MET B 259 ? 0.15770 0.22550 0.28010 -0.03980 -0.07770 0.05890  253 MET B CB  
4570 C CG  . MET B 259 ? 0.21550 0.28100 0.33770 -0.03820 -0.06430 0.04980  253 MET B CG  
4571 S SD  . MET B 259 ? 0.22220 0.29160 0.33550 -0.04660 -0.06020 0.04210  253 MET B SD  
4572 C CE  . MET B 259 ? 0.17670 0.23560 0.26260 -0.05370 -0.05770 0.04050  253 MET B CE  
4573 N N   . ARG B 260 ? 0.26920 0.32900 0.39260 -0.03650 -0.10270 0.08260  254 ARG B N   
4574 C CA  . ARG B 260 ? 0.30510 0.36820 0.43550 -0.03590 -0.11820 0.09370  254 ARG B CA  
4575 C C   . ARG B 260 ? 0.31120 0.37260 0.46750 -0.02420 -0.12040 0.09780  254 ARG B C   
4576 O O   . ARG B 260 ? 0.33240 0.39980 0.50470 -0.01980 -0.12540 0.09940  254 ARG B O   
4577 C CB  . ARG B 260 ? 0.29350 0.34720 0.39780 -0.04420 -0.12550 0.10230  254 ARG B CB  
4578 C CG  . ARG B 260 ? 0.39490 0.45350 0.47650 -0.05640 -0.12700 0.09920  254 ARG B CG  
4579 C CD  . ARG B 260 ? 0.49890 0.55730 0.56460 -0.06440 -0.14210 0.11070  254 ARG B CD  
4580 N NE  . ARG B 260 ? 0.63690 0.68470 0.67170 -0.07390 -0.13850 0.11190  254 ARG B NE  
4581 C CZ  . ARG B 260 ? 0.60980 0.66000 0.62030 -0.08590 -0.13720 0.10740  254 ARG B CZ  
4582 N NH1 . ARG B 260 ? 0.51690 0.57890 0.52910 -0.09040 -0.13920 0.10090  254 ARG B NH1 
4583 N NH2 . ARG B 260 ? 0.55460 0.59540 0.53880 -0.09420 -0.13320 0.10870  254 ARG B NH2 
4584 N N   . ALA B 261 ? 0.30020 0.35040 0.45650 -0.01920 -0.11100 0.09500  255 ALA B N   
4585 C CA  . ALA B 261 ? 0.28070 0.32720 0.46040 -0.00850 -0.11180 0.09750  255 ALA B CA  
4586 C C   . ALA B 261 ? 0.31110 0.36940 0.51510 -0.00180 -0.10620 0.08930  255 ALA B C   
4587 O O   . ALA B 261 ? 0.30630 0.36500 0.52710 0.00470  -0.10880 0.09050  255 ALA B O   
4588 C CB  . ALA B 261 ? 0.28930 0.32230 0.46250 -0.00590 -0.10090 0.09330  255 ALA B CB  
4589 N N   . PHE B 262 ? 0.26680 0.33450 0.47240 -0.00380 -0.09820 0.08090  256 PHE B N   
4590 C CA  . PHE B 262 ? 0.27580 0.35370 0.50160 0.00150  -0.09070 0.07260  256 PHE B CA  
4591 C C   . PHE B 262 ? 0.27420 0.36460 0.50470 -0.00190 -0.09640 0.07260  256 PHE B C   
4592 O O   . PHE B 262 ? 0.25530 0.35480 0.50330 0.00230  -0.09170 0.06690  256 PHE B O   
4593 C CB  . PHE B 262 ? 0.27870 0.35920 0.50350 0.00090  -0.07760 0.06340  256 PHE B CB  
4594 C CG  . PHE B 262 ? 0.24500 0.31530 0.47120 0.00660  -0.06880 0.05980  256 PHE B CG  
4595 C CD1 . PHE B 262 ? 0.19370 0.24990 0.39780 0.00350  -0.06610 0.06080  256 PHE B CD1 
4596 C CD2 . PHE B 262 ? 0.23360 0.30650 0.47830 0.01400  -0.06120 0.05350  256 PHE B CD2 
4597 C CE1 . PHE B 262 ? 0.25580 0.30280 0.46050 0.00800  -0.05790 0.05680  256 PHE B CE1 
4598 C CE2 . PHE B 262 ? 0.22890 0.29300 0.47510 0.01870  -0.05350 0.04950  256 PHE B CE2 
4599 C CZ  . PHE B 262 ? 0.26220 0.31330 0.48850 0.01560  -0.05220 0.05130  256 PHE B CZ  
4600 N N   . ASP B 263 ? 0.27890 0.37020 0.49330 -0.01000 -0.10580 0.07810  257 ASP B N   
4601 C CA  . ASP B 263 ? 0.29930 0.40090 0.51780 -0.01290 -0.11410 0.08000  257 ASP B CA  
4602 C C   . ASP B 263 ? 0.27560 0.39030 0.50780 -0.01270 -0.10670 0.07090  257 ASP B C   
4603 O O   . ASP B 263 ? 0.29780 0.42140 0.54840 -0.00820 -0.10830 0.06970  257 ASP B O   
4604 C CB  . ASP B 263 ? 0.32230 0.42190 0.55310 -0.00670 -0.12310 0.08720  257 ASP B CB  
4605 C CG  . ASP B 263 ? 0.38370 0.49310 0.61560 -0.01060 -0.13410 0.09110  257 ASP B CG  
4606 O OD1 . ASP B 263 ? 0.41490 0.52770 0.62910 -0.02020 -0.13790 0.09130  257 ASP B OD1 
4607 O OD2 . ASP B 263 ? 0.39150 0.50590 0.64280 -0.00420 -0.13860 0.09310  257 ASP B OD2 
4608 N N   . GLY B 264 ? 0.27860 0.39410 0.50180 -0.01780 -0.09820 0.06430  258 GLY B N   
4609 C CA  . GLY B 264 ? 0.24250 0.36830 0.47480 -0.01940 -0.09070 0.05630  258 GLY B CA  
4610 C C   . GLY B 264 ? 0.24780 0.37320 0.49100 -0.01360 -0.07720 0.04940  258 GLY B C   
4611 O O   . GLY B 264 ? 0.27100 0.40250 0.51670 -0.01650 -0.06930 0.04290  258 GLY B O   
4612 N N   . ALA B 265 ? 0.18320 0.30130 0.43210 -0.00610 -0.07420 0.05060  259 ALA B N   
4613 C CA  . ALA B 265 ? 0.18160 0.29990 0.44010 -0.00090 -0.06140 0.04340  259 ALA B CA  
4614 C C   . ALA B 265 ? 0.23820 0.35150 0.48350 -0.00480 -0.05140 0.03890  259 ALA B C   
4615 O O   . ALA B 265 ? 0.18630 0.30170 0.43620 -0.00300 -0.04040 0.03250  259 ALA B O   
4616 C CB  . ALA B 265 ? 0.17770 0.28870 0.44530 0.00760  -0.06100 0.04490  259 ALA B CB  
4617 N N   . LEU B 266 ? 0.16440 0.27140 0.39270 -0.01040 -0.05490 0.04190  260 LEU B N   
4618 C CA  . LEU B 266 ? 0.14230 0.24290 0.35680 -0.01380 -0.04550 0.03760  260 LEU B CA  
4619 C C   . LEU B 266 ? 0.15730 0.25090 0.34880 -0.02140 -0.04950 0.03930  260 LEU B C   
4620 O O   . LEU B 266 ? 0.18660 0.28020 0.37330 -0.02410 -0.05990 0.04480  260 LEU B O   
4621 C CB  . LEU B 266 ? 0.14740 0.23760 0.35770 -0.00800 -0.03890 0.03620  260 LEU B CB  
4622 C CG  . LEU B 266 ? 0.20730 0.28700 0.41100 -0.00500 -0.04480 0.04160  260 LEU B CG  
4623 C CD1 . LEU B 266 ? 0.16490 0.23450 0.34320 -0.01150 -0.04770 0.04440  260 LEU B CD1 
4624 C CD2 . LEU B 266 ? 0.18870 0.26200 0.39700 0.00150  -0.03730 0.03820  260 LEU B CD2 
4625 N N   . VAL B 267 ? 0.12230 0.20990 0.29970 -0.02510 -0.04130 0.03460  261 VAL B N   
4626 C CA  . VAL B 267 ? 0.11610 0.19510 0.27160 -0.03120 -0.04230 0.03440  261 VAL B CA  
4627 C C   . VAL B 267 ? 0.17890 0.24710 0.32280 -0.02870 -0.03410 0.03190  261 VAL B C   
4628 O O   . VAL B 267 ? 0.18120 0.24920 0.33140 -0.02450 -0.02650 0.02900  261 VAL B O   
4629 C CB  . VAL B 267 ? 0.17660 0.25840 0.32660 -0.03890 -0.04120 0.03030  261 VAL B CB  
4630 C CG1 . VAL B 267 ? 0.16750 0.26060 0.32720 -0.04290 -0.05060 0.03250  261 VAL B CG1 
4631 C CG2 . VAL B 267 ? 0.15590 0.23810 0.31150 -0.03800 -0.03130 0.02560  261 VAL B CG2 
4632 N N   . GLY B 268 ? 0.16800 0.22820 0.29490 -0.03190 -0.03580 0.03300  262 GLY B N   
4633 C CA  . GLY B 268 ? 0.14290 0.19410 0.25930 -0.03030 -0.02880 0.03060  262 GLY B CA  
4634 C C   . GLY B 268 ? 0.17820 0.22460 0.27780 -0.03680 -0.02760 0.02780  262 GLY B C   
4635 O O   . GLY B 268 ? 0.24640 0.29450 0.33890 -0.04260 -0.03320 0.02900  262 GLY B O   
4636 N N   . LYS B 269 ? 0.15840 0.19930 0.25180 -0.03580 -0.02020 0.02380  263 LYS B N   
4637 C CA  . LYS B 269 ? 0.16590 0.20290 0.24660 -0.04100 -0.01750 0.01970  263 LYS B CA  
4638 C C   . LYS B 269 ? 0.18530 0.21650 0.26100 -0.03840 -0.01140 0.01740  263 LYS B C   
4639 O O   . LYS B 269 ? 0.19230 0.22290 0.27440 -0.03330 -0.00730 0.01670  263 LYS B O   
4640 C CB  . LYS B 269 ? 0.20970 0.24860 0.29360 -0.04380 -0.01480 0.01530  263 LYS B CB  
4641 C CG  . LYS B 269 ? 0.17960 0.21370 0.25290 -0.04850 -0.01120 0.00960  263 LYS B CG  
4642 C CD  . LYS B 269 ? 0.24690 0.28200 0.30850 -0.05570 -0.01620 0.00940  263 LYS B CD  
4643 C CE  . LYS B 269 ? 0.20840 0.23900 0.25900 -0.06050 -0.01110 0.00230  263 LYS B CE  
4644 N NZ  . LYS B 269 ? 0.23320 0.26050 0.27650 -0.05930 -0.00780 0.00230  263 LYS B NZ  
4645 N N   . LEU B 270 ? 0.17350 0.20120 0.23740 -0.04230 -0.01100 0.01610  264 LEU B N   
4646 C CA  . LEU B 270 ? 0.18050 0.20430 0.23990 -0.04120 -0.00540 0.01310  264 LEU B CA  
4647 C C   . LEU B 270 ? 0.16760 0.19040 0.22750 -0.04140 0.00030  0.00680  264 LEU B C   
4648 O O   . LEU B 270 ? 0.21150 0.23460 0.26890 -0.04560 0.00040  0.00340  264 LEU B O   
4649 C CB  . LEU B 270 ? 0.23870 0.26050 0.28590 -0.04660 -0.00660 0.01390  264 LEU B CB  
4650 C CG  . LEU B 270 ? 0.24880 0.26820 0.29090 -0.04740 -0.00060 0.00970  264 LEU B CG  
4651 C CD1 . LEU B 270 ? 0.21570 0.23330 0.26350 -0.04200 0.00040  0.01210  264 LEU B CD1 
4652 C CD2 . LEU B 270 ? 0.25540 0.27390 0.28370 -0.05510 -0.00130 0.00990  264 LEU B CD2 
4653 N N   . GLY B 271 ? 0.20080 0.22190 0.26410 -0.03710 0.00460  0.00520  265 GLY B N   
4654 C CA  . GLY B 271 ? 0.15400 0.17330 0.21760 -0.03700 0.00950  -0.00030 265 GLY B CA  
4655 C C   . GLY B 271 ? 0.20520 0.22440 0.26490 -0.03750 0.01240  -0.00280 265 GLY B C   
4656 O O   . GLY B 271 ? 0.18770 0.20720 0.24730 -0.03550 0.01170  0.00020  265 GLY B O   
4657 N N   . ALA B 272 ? 0.16790 0.18690 0.22550 -0.04030 0.01630  -0.00880 266 ALA B N   
4658 C CA  . ALA B 272 ? 0.21410 0.23460 0.26960 -0.04130 0.02000  -0.01200 266 ALA B CA  
4659 C C   . ALA B 272 ? 0.21680 0.23830 0.28070 -0.03510 0.02080  -0.01080 266 ALA B C   
4660 O O   . ALA B 272 ? 0.20040 0.22070 0.27100 -0.03030 0.01980  -0.00920 266 ALA B O   
4661 C CB  . ALA B 272 ? 0.25820 0.27930 0.31320 -0.04470 0.02530  -0.02030 266 ALA B CB  
4662 N N   . ASP B 273 ? 0.22640 0.25010 0.28880 -0.03610 0.02240  -0.01150 267 ASP B N   
4663 C CA  . ASP B 273 ? 0.21000 0.23550 0.27870 -0.03150 0.02220  -0.01040 267 ASP B CA  
4664 C C   . ASP B 273 ? 0.19620 0.21970 0.26520 -0.02830 0.01830  -0.00460 267 ASP B C   
4665 O O   . ASP B 273 ? 0.17430 0.19890 0.24830 -0.02390 0.01760  -0.00380 267 ASP B O   
4666 C CB  . ASP B 273 ? 0.20770 0.23530 0.28640 -0.02700 0.02410  -0.01390 267 ASP B CB  
4667 C CG  . ASP B 273 ? 0.26010 0.29150 0.34190 -0.02940 0.02900  -0.02080 267 ASP B CG  
4668 O OD1 . ASP B 273 ? 0.23530 0.27060 0.31570 -0.03220 0.03100  -0.02230 267 ASP B OD1 
4669 O OD2 . ASP B 273 ? 0.28950 0.32020 0.37560 -0.02900 0.03160  -0.02540 267 ASP B OD2 
4670 N N   . ALA B 274 ? 0.16500 0.18610 0.22860 -0.03070 0.01560  -0.00100 268 ALA B N   
4671 C CA  . ALA B 274 ? 0.19560 0.21490 0.26000 -0.02850 0.01260  0.00350  268 ALA B CA  
4672 C C   . ALA B 274 ? 0.16250 0.18220 0.23250 -0.02390 0.01170  0.00500  268 ALA B C   
4673 O O   . ALA B 274 ? 0.17970 0.19990 0.25250 -0.02070 0.01180  0.00550  268 ALA B O   
4674 C CB  . ALA B 274 ? 0.16690 0.18600 0.23160 -0.02820 0.01350  0.00300  268 ALA B CB  
4675 N N   . SER B 275 ? 0.16740 0.18730 0.23830 -0.02450 0.01100  0.00540  269 SER B N   
4676 C CA  A SER B 275 ? 0.14140 0.16210 0.21710 -0.02190 0.01000  0.00770  269 SER B CA  
4677 C CA  B SER B 275 ? 0.13680 0.15750 0.21250 -0.02190 0.01000  0.00780  269 SER B CA  
4678 C C   . SER B 275 ? 0.15600 0.17730 0.23200 -0.02390 0.00660  0.01050  269 SER B C   
4679 O O   . SER B 275 ? 0.15680 0.17750 0.22770 -0.02800 0.00460  0.01070  269 SER B O   
4680 C CB  A SER B 275 ? 0.15190 0.17230 0.23030 -0.02120 0.01170  0.00660  269 SER B CB  
4681 C CB  B SER B 275 ? 0.15120 0.17170 0.22980 -0.02100 0.01170  0.00670  269 SER B CB  
4682 O OG  A SER B 275 ? 0.14710 0.16730 0.22660 -0.01850 0.01350  0.00550  269 SER B OG  
4683 O OG  B SER B 275 ? 0.14760 0.16720 0.22510 -0.02450 0.01140  0.00500  269 SER B OG  
4684 N N   . TYR B 276 ? 0.12770 0.15100 0.20990 -0.02130 0.00570  0.01260  270 TYR B N   
4685 C CA  . TYR B 276 ? 0.16590 0.19140 0.25210 -0.02210 0.00170  0.01550  270 TYR B CA  
4686 C C   . TYR B 276 ? 0.15990 0.18980 0.25490 -0.02020 0.00290  0.01580  270 TYR B C   
4687 O O   . TYR B 276 ? 0.16830 0.19870 0.26560 -0.01750 0.00660  0.01480  270 TYR B O   
4688 C CB  . TYR B 276 ? 0.14360 0.16730 0.23130 -0.02060 -0.00130 0.01830  270 TYR B CB  
4689 C CG  . TYR B 276 ? 0.14970 0.17450 0.23740 -0.02340 -0.00730 0.02210  270 TYR B CG  
4690 C CD1 . TYR B 276 ? 0.17140 0.19380 0.24840 -0.02870 -0.00960 0.02290  270 TYR B CD1 
4691 C CD2 . TYR B 276 ? 0.14870 0.17810 0.24700 -0.02140 -0.01080 0.02450  270 TYR B CD2 
4692 C CE1 . TYR B 276 ? 0.17340 0.19700 0.24800 -0.03220 -0.01600 0.02680  270 TYR B CE1 
4693 C CE2 . TYR B 276 ? 0.15000 0.18150 0.24860 -0.02410 -0.01780 0.02850  270 TYR B CE2 
4694 C CZ  . TYR B 276 ? 0.22500 0.25330 0.31050 -0.02990 -0.02070 0.03000  270 TYR B CZ  
4695 O OH  . TYR B 276 ? 0.21940 0.25000 0.30260 -0.03370 -0.02850 0.03450  270 TYR B OH  
4696 N N   . ALA B 277 ? 0.14180 0.17530 0.24120 -0.02250 -0.00050 0.01720  271 ALA B N   
4697 C CA  . ALA B 277 ? 0.11140 0.15050 0.22070 -0.02160 0.00090  0.01740  271 ALA B CA  
4698 C C   . ALA B 277 ? 0.13930 0.18420 0.25770 -0.02170 -0.00450 0.01990  271 ALA B C   
4699 O O   . ALA B 277 ? 0.14340 0.18790 0.25780 -0.02470 -0.01020 0.02180  271 ALA B O   
4700 C CB  . ALA B 277 ? 0.14400 0.18270 0.25170 -0.02510 0.00310  0.01580  271 ALA B CB  
4701 N N   . ILE B 278 ? 0.14160 0.19240 0.27240 -0.01840 -0.00280 0.01990  272 ILE B N   
4702 C CA  . ILE B 278 ? 0.09890 0.15680 0.24330 -0.01700 -0.00780 0.02210  272 ILE B CA  
4703 C C   . ILE B 278 ? 0.14290 0.20990 0.30010 -0.01710 -0.00400 0.02030  272 ILE B C   
4704 O O   . ILE B 278 ? 0.12300 0.19040 0.28130 -0.01560 0.00330  0.01770  272 ILE B O   
4705 C CB  . ILE B 278 ? 0.12760 0.18350 0.27800 -0.01150 -0.00930 0.02350  272 ILE B CB  
4706 C CG1 . ILE B 278 ? 0.14560 0.19290 0.28350 -0.01280 -0.01370 0.02630  272 ILE B CG1 
4707 C CG2 . ILE B 278 ? 0.11760 0.18150 0.28570 -0.00880 -0.01480 0.02590  272 ILE B CG2 
4708 C CD1 . ILE B 278 ? 0.18830 0.23080 0.33080 -0.00810 -0.01500 0.02780  272 ILE B CD1 
4709 N N   . GLY B 279 ? 0.13690 0.21140 0.30270 -0.02000 -0.00900 0.02170  273 GLY B N   
4710 C CA  . GLY B 279 ? 0.11080 0.19570 0.29170 -0.02070 -0.00600 0.02000  273 GLY B CA  
4711 C C   . GLY B 279 ? 0.15180 0.24590 0.35110 -0.01670 -0.01150 0.02170  273 GLY B C   
4712 O O   . GLY B 279 ? 0.13790 0.23300 0.33800 -0.01750 -0.02090 0.02550  273 GLY B O   
4713 N N   . VAL B 280 ? 0.16460 0.26420 0.37650 -0.01220 -0.00570 0.01880  274 VAL B N   
4714 C CA  . VAL B 280 ? 0.14490 0.24940 0.37210 -0.00610 -0.00920 0.01910  274 VAL B CA  
4715 C C   . VAL B 280 ? 0.13550 0.25100 0.37430 -0.00700 -0.00680 0.01620  274 VAL B C   
4716 O O   . VAL B 280 ? 0.12810 0.24630 0.36600 -0.00840 0.00270  0.01180  274 VAL B O   
4717 C CB  . VAL B 280 ? 0.09330 0.19310 0.32320 0.00010  -0.00330 0.01620  274 VAL B CB  
4718 C CG1 . VAL B 280 ? 0.14500 0.24880 0.39210 0.00660  -0.00590 0.01540  274 VAL B CG1 
4719 C CG2 . VAL B 280 ? 0.12930 0.21750 0.34560 0.00040  -0.00510 0.01860  274 VAL B CG2 
4720 N N   . ARG B 281 ? 0.13500 0.25740 0.38380 -0.00680 -0.01550 0.01890  275 ARG B N   
4721 C CA  . ARG B 281 ? 0.10830 0.24270 0.37030 -0.00760 -0.01340 0.01590  275 ARG B CA  
4722 C C   . ARG B 281 ? 0.12990 0.26770 0.40490 -0.00100 -0.00680 0.01160  275 ARG B C   
4723 O O   . ARG B 281 ? 0.14570 0.27710 0.42340 0.00510  -0.00750 0.01190  275 ARG B O   
4724 C CB  . ARG B 281 ? 0.15980 0.30150 0.43050 -0.00850 -0.02510 0.01980  275 ARG B CB  
4725 C CG  . ARG B 281 ? 0.20240 0.34280 0.46020 -0.01690 -0.03090 0.02220  275 ARG B CG  
4726 C CD  . ARG B 281 ? 0.20130 0.35060 0.46720 -0.01860 -0.04240 0.02540  275 ARG B CD  
4727 N NE  . ARG B 281 ? 0.22380 0.38650 0.50630 -0.01830 -0.03980 0.02190  275 ARG B NE  
4728 C CZ  . ARG B 281 ? 0.27510 0.44850 0.56920 -0.01880 -0.04860 0.02370  275 ARG B CZ  
4729 N NH1 . ARG B 281 ? 0.27220 0.44390 0.56140 -0.01990 -0.06100 0.02930  275 ARG B NH1 
4730 N NH2 . ARG B 281 ? 0.23980 0.42640 0.55030 -0.01850 -0.04490 0.01990  275 ARG B NH2 
4731 N N   . ALA B 282 ? 0.14530 0.29320 0.42870 -0.00270 0.00000  0.00710  276 ALA B N   
4732 C CA  . ALA B 282 ? 0.16640 0.31870 0.46200 0.00250  0.00740  0.00180  276 ALA B CA  
4733 C C   . ALA B 282 ? 0.14900 0.30340 0.46190 0.01010  0.00000  0.00320  276 ALA B C   
4734 O O   . ALA B 282 ? 0.21570 0.37560 0.53720 0.01020  -0.01000 0.00740  276 ALA B O   
4735 C CB  . ALA B 282 ? 0.12740 0.29200 0.42980 -0.00180 0.01510  -0.00240 276 ALA B CB  
4736 N N   . SER B 283 ? 0.15820 0.30790 0.47630 0.01620  0.00490  -0.00050 277 SER B N   
4737 C CA  . SER B 283 ? 0.20050 0.34750 0.53280 0.02380  -0.00190 0.00130  277 SER B CA  
4738 C C   . SER B 283 ? 0.21560 0.36090 0.55600 0.02900  0.00790  -0.00640 277 SER B C   
4739 O O   . SER B 283 ? 0.18420 0.32970 0.51610 0.02620  0.01920  -0.01240 277 SER B O   
4740 C CB  . SER B 283 ? 0.14890 0.28270 0.47020 0.02480  -0.01090 0.00830  277 SER B CB  
4741 O OG  . SER B 283 ? 0.15000 0.27330 0.45820 0.02490  -0.00370 0.00540  277 SER B OG  
4742 N N   . ASP B 284 ? 0.20350 0.34670 0.55990 0.03610  0.00330  -0.00610 278 ASP B N   
4743 C CA  . ASP B 284 ? 0.18300 0.32220 0.54620 0.04090  0.01210  -0.01390 278 ASP B CA  
4744 C C   . ASP B 284 ? 0.20810 0.33460 0.55200 0.03920  0.01760  -0.01580 278 ASP B C   
4745 O O   . ASP B 284 ? 0.21220 0.33860 0.55270 0.03860  0.02890  -0.02400 278 ASP B O   
4746 C CB  . ASP B 284 ? 0.19080 0.32600 0.57260 0.04880  0.00500  -0.01210 278 ASP B CB  
4747 C CG  . ASP B 284 ? 0.33900 0.48800 0.74300 0.05150  0.00050  -0.01160 278 ASP B CG  
4748 O OD1 . ASP B 284 ? 0.34070 0.50380 0.74940 0.04800  0.00620  -0.01550 278 ASP B OD1 
4749 O OD2 . ASP B 284 ? 0.44200 0.58760 0.85950 0.05720  -0.00910 -0.00670 278 ASP B OD2 
4750 N N   . ALA B 285 ? 0.15420 0.27070 0.48490 0.03770  0.00980  -0.00850 279 ALA B N   
4751 C CA  . ALA B 285 ? 0.17980 0.28490 0.49320 0.03610  0.01430  -0.00990 279 ALA B CA  
4752 C C   . ALA B 285 ? 0.20320 0.31270 0.50180 0.02990  0.02440  -0.01430 279 ALA B C   
4753 O O   . ALA B 285 ? 0.17940 0.28490 0.47030 0.02940  0.03340  -0.02070 279 ALA B O   
4754 C CB  . ALA B 285 ? 0.19480 0.29030 0.49800 0.03520  0.00380  -0.00070 279 ALA B CB  
4755 N N   . THR B 286 ? 0.17880 0.29610 0.47250 0.02450  0.02300  -0.01100 280 THR B N   
4756 C CA  . THR B 286 ? 0.17040 0.29070 0.44990 0.01820  0.03210  -0.01410 280 THR B CA  
4757 C C   . THR B 286 ? 0.16300 0.29110 0.44870 0.01820  0.04340  -0.02250 280 THR B C   
4758 O O   . THR B 286 ? 0.16550 0.29210 0.43840 0.01460  0.05250  -0.02670 280 THR B O   
4759 C CB  . THR B 286 ? 0.20510 0.33150 0.47990 0.01210  0.02840  -0.00910 280 THR B CB  
4760 O OG1 . THR B 286 ? 0.19260 0.33040 0.48410 0.01280  0.02540  -0.00910 280 THR B OG1 
4761 C CG2 . THR B 286 ? 0.16540 0.28400 0.43070 0.01060  0.01850  -0.00170 280 THR B CG2 
4762 N N   . ARG B 287 ? 0.17710 0.31390 0.48230 0.02170  0.04280  -0.02500 281 ARG B N   
4763 C CA  A ARG B 287 ? 0.18260 0.32780 0.49490 0.02130  0.05400  -0.03350 281 ARG B CA  
4764 C CA  B ARG B 287 ? 0.18330 0.32850 0.49570 0.02140  0.05390  -0.03350 281 ARG B CA  
4765 C C   . ARG B 287 ? 0.22890 0.36620 0.53850 0.02460  0.06080  -0.04070 281 ARG B C   
4766 O O   . ARG B 287 ? 0.26980 0.40980 0.57150 0.02110  0.07170  -0.04740 281 ARG B O   
4767 C CB  A ARG B 287 ? 0.17540 0.33230 0.51170 0.02490  0.05150  -0.03480 281 ARG B CB  
4768 C CB  B ARG B 287 ? 0.17620 0.33290 0.51250 0.02500  0.05120  -0.03460 281 ARG B CB  
4769 C CG  A ARG B 287 ? 0.14590 0.31360 0.48550 0.02020  0.04720  -0.02990 281 ARG B CG  
4770 C CG  B ARG B 287 ? 0.19720 0.36800 0.53840 0.02030  0.06030  -0.03930 281 ARG B CG  
4771 C CD  A ARG B 287 ? 0.15800 0.33910 0.52300 0.02380  0.04480  -0.03170 281 ARG B CD  
4772 C CD  B ARG B 287 ? 0.16840 0.35220 0.53260 0.02270  0.05510  -0.03820 281 ARG B CD  
4773 N NE  A ARG B 287 ? 0.16920 0.34770 0.54670 0.02970  0.03170  -0.02580 281 ARG B NE  
4774 N NE  B ARG B 287 ? 0.15800 0.34210 0.52120 0.02110  0.04290  -0.02930 281 ARG B NE  
4775 C CZ  A ARG B 287 ? 0.16640 0.34650 0.54200 0.02730  0.02080  -0.01810 281 ARG B CZ  
4776 C CZ  B ARG B 287 ? 0.16690 0.34900 0.54170 0.02660  0.03120  -0.02440 281 ARG B CZ  
4777 N NH1 A ARG B 287 ? 0.14560 0.32930 0.50860 0.01950  0.02150  -0.01570 281 ARG B NH1 
4778 N NH1 B ARG B 287 ? 0.15970 0.33920 0.55000 0.03440  0.02940  -0.02670 281 ARG B NH1 
4779 N NH2 A ARG B 287 ? 0.16870 0.34650 0.55500 0.03250  0.00880  -0.01250 281 ARG B NH2 
4780 N NH2 B ARG B 287 ? 0.15980 0.34220 0.53010 0.02360  0.02070  -0.01670 281 ARG B NH2 
4781 N N   . GLN B 288 ? 0.17880 0.30640 0.49470 0.03070  0.05450  -0.03960 282 GLN B N   
4782 C CA  . GLN B 288 ? 0.25220 0.37080 0.56470 0.03320  0.06040  -0.04650 282 GLN B CA  
4783 C C   . GLN B 288 ? 0.22040 0.33280 0.50910 0.02780  0.06550  -0.04740 282 GLN B C   
4784 O O   . GLN B 288 ? 0.22450 0.33390 0.50670 0.02700  0.07390  -0.05530 282 GLN B O   
4785 C CB  . GLN B 288 ? 0.22200 0.32940 0.54380 0.03980  0.05160  -0.04340 282 GLN B CB  
4786 C CG  . GLN B 288 ? 0.39710 0.50710 0.74300 0.04640  0.05020  -0.04660 282 GLN B CG  
4787 C CD  . GLN B 288 ? 0.44140 0.54090 0.79550 0.05180  0.03820  -0.03920 282 GLN B CD  
4788 O OE1 . GLN B 288 ? 0.46110 0.56490 0.83060 0.05530  0.02960  -0.03370 282 GLN B OE1 
4789 N NE2 . GLN B 288 ? 0.51570 0.60120 0.85870 0.05210  0.03720  -0.03860 282 GLN B NE2 
4790 N N   . LEU B 289 ? 0.19590 0.30650 0.47150 0.02390  0.06030  -0.03960 283 LEU B N   
4791 C CA  . LEU B 289 ? 0.25730 0.36290 0.51130 0.01890  0.06430  -0.03940 283 LEU B CA  
4792 C C   . LEU B 289 ? 0.30940 0.42320 0.55280 0.01220  0.07390  -0.04260 283 LEU B C   
4793 O O   . LEU B 289 ? 0.31410 0.42440 0.53910 0.00750  0.07750  -0.04210 283 LEU B O   
4794 C CB  . LEU B 289 ? 0.20210 0.30280 0.44720 0.01700  0.05530  -0.02990 283 LEU B CB  
4795 C CG  . LEU B 289 ? 0.16080 0.25130 0.41000 0.02190  0.04620  -0.02560 283 LEU B CG  
4796 C CD1 . LEU B 289 ? 0.16570 0.25430 0.40830 0.01930  0.03720  -0.01620 283 LEU B CD1 
4797 C CD2 . LEU B 289 ? 0.17880 0.25970 0.41920 0.02280  0.05040  -0.03050 283 LEU B CD2 
4798 N N   . GLY B 290 ? 0.23820 0.36280 0.49280 0.01140  0.07760  -0.04490 284 GLY B N   
4799 C CA  . GLY B 290 ? 0.27880 0.41110 0.52420 0.00490  0.08750  -0.04830 284 GLY B CA  
4800 C C   . GLY B 290 ? 0.33480 0.47280 0.57400 -0.00140 0.08630  -0.04150 284 GLY B C   
4801 O O   . GLY B 290 ? 0.38040 0.52060 0.60530 -0.00810 0.09360  -0.04190 284 GLY B O   
4802 N N   . THR B 291 ? 0.30230 0.44190 0.55080 -0.00010 0.07720  -0.03510 285 THR B N   
4803 C CA  . THR B 291 ? 0.25640 0.40140 0.50100 -0.00650 0.07610  -0.02970 285 THR B CA  
4804 C C   . THR B 291 ? 0.24070 0.39530 0.50550 -0.00440 0.07070  -0.02850 285 THR B C   
4805 O O   . THR B 291 ? 0.21000 0.36380 0.48880 0.00220  0.06370  -0.02840 285 THR B O   
4806 C CB  . THR B 291 ? 0.28230 0.41810 0.51180 -0.00960 0.06980  -0.02230 285 THR B CB  
4807 O OG1 . THR B 291 ? 0.30400 0.44360 0.52890 -0.01650 0.07000  -0.01780 285 THR B OG1 
4808 C CG2 . THR B 291 ? 0.25850 0.38880 0.49500 -0.00440 0.05860  -0.01830 285 THR B CG2 
4809 N N   . ASP B 292 ? 0.26760 0.43110 0.53380 -0.01040 0.07390  -0.02740 286 ASP B N   
4810 C CA  . ASP B 292 ? 0.23930 0.41410 0.52450 -0.00980 0.06970  -0.02680 286 ASP B CA  
4811 C C   . ASP B 292 ? 0.23860 0.41170 0.52230 -0.01240 0.05930  -0.01960 286 ASP B C   
4812 O O   . ASP B 292 ? 0.22830 0.41090 0.52660 -0.01260 0.05450  -0.01870 286 ASP B O   
4813 C CB  . ASP B 292 ? 0.28830 0.47510 0.57750 -0.01560 0.07950  -0.03020 286 ASP B CB  
4814 C CG  . ASP B 292 ? 0.40410 0.58660 0.67190 -0.02470 0.08560  -0.02700 286 ASP B CG  
4815 O OD1 . ASP B 292 ? 0.47920 0.65010 0.73030 -0.02620 0.08220  -0.02240 286 ASP B OD1 
4816 O OD2 . ASP B 292 ? 0.50690 0.69770 0.77510 -0.03060 0.09370  -0.02850 286 ASP B OD2 
4817 N N   . GLY B 293 ? 0.19840 0.36000 0.46510 -0.01460 0.05560  -0.01500 287 GLY B N   
4818 C CA  . GLY B 293 ? 0.21110 0.37020 0.47500 -0.01770 0.04650  -0.00930 287 GLY B CA  
4819 C C   . GLY B 293 ? 0.26780 0.41590 0.52570 -0.01350 0.03820  -0.00590 287 GLY B C   
4820 O O   . GLY B 293 ? 0.21100 0.35550 0.47340 -0.00680 0.03700  -0.00760 287 GLY B O   
4821 N N   . ALA B 294 ? 0.19500 0.33710 0.44240 -0.01790 0.03270  -0.00130 288 ALA B N   
4822 C CA  . ALA B 294 ? 0.17330 0.30540 0.41380 -0.01530 0.02500  0.00240  288 ALA B CA  
4823 C C   . ALA B 294 ? 0.17020 0.29200 0.39610 -0.01450 0.03020  0.00200  288 ALA B C   
4824 O O   . ALA B 294 ? 0.16050 0.28220 0.37960 -0.01670 0.03910  -0.00060 288 ALA B O   
4825 C CB  . ALA B 294 ? 0.15940 0.28940 0.39390 -0.02090 0.01790  0.00640  288 ALA B CB  
4826 N N   . LEU B 295 ? 0.14070 0.25400 0.36080 -0.01200 0.02430  0.00480  289 LEU B N   
4827 C CA  . LEU B 295 ? 0.12590 0.23030 0.33440 -0.01050 0.02810  0.00430  289 LEU B CA  
4828 C C   . LEU B 295 ? 0.14350 0.23940 0.34070 -0.01300 0.02250  0.00870  289 LEU B C   
4829 O O   . LEU B 295 ? 0.18920 0.28550 0.38970 -0.01360 0.01420  0.01180  289 LEU B O   
4830 C CB  . LEU B 295 ? 0.18030 0.28370 0.39740 -0.00350 0.02770  0.00170  289 LEU B CB  
4831 C CG  . LEU B 295 ? 0.21890 0.31540 0.42930 -0.00060 0.03220  -0.00110 289 LEU B CG  
4832 C CD1 . LEU B 295 ? 0.26230 0.36330 0.48360 0.00360  0.03780  -0.00730 289 LEU B CD1 
4833 C CD2 . LEU B 295 ? 0.23490 0.32450 0.44620 0.00260  0.02370  0.00280  289 LEU B CD2 
4834 N N   . GLY B 296 ? 0.13900 0.22760 0.32260 -0.01460 0.02670  0.00890  290 GLY B N   
4835 C CA  . GLY B 296 ? 0.11430 0.19190 0.28210 -0.01560 0.02160  0.01170  290 GLY B CA  
4836 C C   . GLY B 296 ? 0.12450 0.19420 0.28200 -0.01210 0.02290  0.01060  290 GLY B C   
4837 O O   . GLY B 296 ? 0.15480 0.22540 0.31060 -0.01090 0.02930  0.00760  290 GLY B O   
4838 N N   . ILE B 297 ? 0.12290 0.18570 0.27350 -0.01110 0.01690  0.01250  291 ILE B N   
4839 C CA  . ILE B 297 ? 0.12240 0.17750 0.26340 -0.00870 0.01740  0.01150  291 ILE B CA  
4840 C C   . ILE B 297 ? 0.13810 0.18610 0.26540 -0.01140 0.01480  0.01330  291 ILE B C   
4841 O O   . ILE B 297 ? 0.13860 0.18580 0.26480 -0.01380 0.01010  0.01540  291 ILE B O   
4842 C CB  . ILE B 297 ? 0.13020 0.18390 0.27860 -0.00470 0.01310  0.01180  291 ILE B CB  
4843 C CG1 . ILE B 297 ? 0.12590 0.18750 0.29220 -0.00120 0.01510  0.00960  291 ILE B CG1 
4844 C CG2 . ILE B 297 ? 0.12680 0.17220 0.26560 -0.00310 0.01410  0.01030  291 ILE B CG2 
4845 C CD1 . ILE B 297 ? 0.17160 0.23090 0.34710 0.00280  0.00890  0.01170  291 ILE B CD1 
4846 N N   . SER B 298 ? 0.13770 0.18100 0.25500 -0.01120 0.01770  0.01220  292 SER B N   
4847 C CA  . SER B 298 ? 0.11340 0.15080 0.22060 -0.01280 0.01560  0.01310  292 SER B CA  
4848 C C   . SER B 298 ? 0.14500 0.17850 0.24590 -0.01100 0.01620  0.01140  292 SER B C   
4849 O O   . SER B 298 ? 0.13750 0.17230 0.23860 -0.00930 0.01950  0.00930  292 SER B O   
4850 C CB  . SER B 298 ? 0.13480 0.17100 0.23770 -0.01530 0.01750  0.01400  292 SER B CB  
4851 O OG  . SER B 298 ? 0.14900 0.18680 0.25020 -0.01470 0.02190  0.01370  292 SER B OG  
4852 N N   . VAL B 299 ? 0.11870 0.14820 0.21430 -0.01190 0.01340  0.01170  293 VAL B N   
4853 C CA  . VAL B 299 ? 0.14630 0.17260 0.23760 -0.01100 0.01330  0.01020  293 VAL B CA  
4854 C C   . VAL B 299 ? 0.12770 0.15190 0.21270 -0.01280 0.01280  0.00980  293 VAL B C   
4855 O O   . VAL B 299 ? 0.12890 0.15260 0.21290 -0.01490 0.01150  0.01040  293 VAL B O   
4856 C CB  . VAL B 299 ? 0.10870 0.13250 0.20310 -0.01060 0.01040  0.01110  293 VAL B CB  
4857 C CG1 . VAL B 299 ? 0.14280 0.16250 0.23270 -0.01070 0.01090  0.00920  293 VAL B CG1 
4858 C CG2 . VAL B 299 ? 0.14310 0.16950 0.24770 -0.00770 0.01080  0.01110  293 VAL B CG2 
4859 N N   . LYS B 300 ? 0.15580 0.17950 0.23730 -0.01210 0.01380  0.00790  294 LYS B N   
4860 C CA  . LYS B 300 ? 0.15350 0.17650 0.23180 -0.01330 0.01330  0.00680  294 LYS B CA  
4861 C C   . LYS B 300 ? 0.14200 0.16450 0.21850 -0.01360 0.01340  0.00470  294 LYS B C   
4862 O O   . LYS B 300 ? 0.12510 0.14840 0.20110 -0.01230 0.01420  0.00340  294 LYS B O   
4863 C CB  . LYS B 300 ? 0.13060 0.15470 0.20870 -0.01220 0.01390  0.00720  294 LYS B CB  
4864 C CG  . LYS B 300 ? 0.13510 0.16020 0.21320 -0.01200 0.01340  0.00530  294 LYS B CG  
4865 C CD  . LYS B 300 ? 0.14550 0.16980 0.22490 -0.01390 0.01390  0.00350  294 LYS B CD  
4866 C CE  . LYS B 300 ? 0.13280 0.15970 0.21560 -0.01290 0.01410  0.00100  294 LYS B CE  
4867 N NZ  . LYS B 300 ? 0.18620 0.21340 0.27100 -0.01500 0.01610  -0.00260 294 LYS B NZ  
4868 N N   . ILE B 301 ? 0.13000 0.15140 0.20510 -0.01600 0.01290  0.00380  295 ILE B N   
4869 C CA  . ILE B 301 ? 0.12840 0.14980 0.20250 -0.01730 0.01320  0.00150  295 ILE B CA  
4870 C C   . ILE B 301 ? 0.13570 0.16170 0.21110 -0.01700 0.01360  -0.00050 295 ILE B C   
4871 O O   . ILE B 301 ? 0.13240 0.15940 0.20900 -0.01770 0.01430  -0.00100 295 ILE B O   
4872 C CB  . ILE B 301 ? 0.11810 0.13600 0.18990 -0.02110 0.01290  0.00220  295 ILE B CB  
4873 C CG1 . ILE B 301 ? 0.15660 0.16990 0.22890 -0.02070 0.01100  0.00560  295 ILE B CG1 
4874 C CG2 . ILE B 301 ? 0.12020 0.13840 0.19160 -0.02360 0.01380  -0.00040 295 ILE B CG2 
4875 C CD1 . ILE B 301 ? 0.16880 0.18020 0.24490 -0.01760 0.01120  0.00480  295 ILE B CD1 
4876 N N   . GLU B 302 ? 0.13970 0.16860 0.21550 -0.01570 0.01300  -0.00200 296 GLU B N   
4877 C CA  . GLU B 302 ? 0.16830 0.20220 0.24720 -0.01420 0.01180  -0.00280 296 GLU B CA  
4878 C C   . GLU B 302 ? 0.15790 0.19470 0.24120 -0.01590 0.01290  -0.00530 296 GLU B C   
4879 O O   . GLU B 302 ? 0.13890 0.17800 0.22710 -0.01410 0.01290  -0.00570 296 GLU B O   
4880 C CB  . GLU B 302 ? 0.17320 0.21070 0.25090 -0.01400 0.01000  -0.00410 296 GLU B CB  
4881 C CG  . GLU B 302 ? 0.19590 0.23920 0.27750 -0.01190 0.00700  -0.00360 296 GLU B CG  
4882 C CD  . GLU B 302 ? 0.26720 0.30870 0.34880 -0.00880 0.00600  0.00070  296 GLU B CD  
4883 O OE1 . GLU B 302 ? 0.21220 0.25000 0.28850 -0.00870 0.00700  0.00310  296 GLU B OE1 
4884 O OE2 . GLU B 302 ? 0.22070 0.26420 0.30880 -0.00660 0.00440  0.00150  296 GLU B OE2 
4885 N N   . ASP B 303 ? 0.12610 0.16260 0.20830 -0.01970 0.01440  -0.00730 297 ASP B N   
4886 C CA  . ASP B 303 ? 0.14100 0.18180 0.22730 -0.02260 0.01660  -0.01070 297 ASP B CA  
4887 C C   . ASP B 303 ? 0.15280 0.19070 0.23600 -0.02550 0.01940  -0.01070 297 ASP B C   
4888 O O   . ASP B 303 ? 0.14940 0.19100 0.23460 -0.02890 0.02250  -0.01410 297 ASP B O   
4889 C CB  . ASP B 303 ? 0.17490 0.21650 0.26040 -0.02680 0.01720  -0.01260 297 ASP B CB  
4890 C CG  . ASP B 303 ? 0.17590 0.20900 0.25440 -0.02900 0.01710  -0.00990 297 ASP B CG  
4891 O OD1 . ASP B 303 ? 0.17370 0.20380 0.25080 -0.02670 0.01530  -0.00900 297 ASP B OD1 
4892 O OD2 . ASP B 303 ? 0.15240 0.18180 0.22710 -0.03310 0.01880  -0.00870 297 ASP B OD2 
4893 N N   . GLY B 304 ? 0.14750 0.17980 0.22560 -0.02500 0.01850  -0.00740 298 GLY B N   
4894 C CA  . GLY B 304 ? 0.20550 0.23570 0.27970 -0.02800 0.02000  -0.00740 298 GLY B CA  
4895 C C   . GLY B 304 ? 0.20830 0.23460 0.27460 -0.03360 0.02030  -0.00550 298 GLY B C   
4896 O O   . GLY B 304 ? 0.20140 0.22720 0.26270 -0.03750 0.02170  -0.00600 298 GLY B O   
4897 N N   . ASN B 305 ? 0.16720 0.19020 0.23180 -0.03450 0.01880  -0.00310 299 ASN B N   
4898 C CA  . ASN B 305 ? 0.20310 0.22100 0.26060 -0.04010 0.01850  0.00000  299 ASN B CA  
4899 C C   . ASN B 305 ? 0.19780 0.21010 0.25110 -0.03950 0.01450  0.00540  299 ASN B C   
4900 O O   . ASN B 305 ? 0.17380 0.18350 0.23110 -0.03510 0.01180  0.00770  299 ASN B O   
4901 C CB  . ASN B 305 ? 0.19480 0.21000 0.25370 -0.04120 0.01830  0.00020  299 ASN B CB  
4902 C CG  . ASN B 305 ? 0.22960 0.23870 0.28130 -0.04790 0.01830  0.00380  299 ASN B CG  
4903 O OD1 . ASN B 305 ? 0.19430 0.19650 0.24220 -0.04800 0.01490  0.00920  299 ASN B OD1 
4904 N ND2 . ASN B 305 ? 0.24370 0.25560 0.29410 -0.05370 0.02210  0.00110  299 ASN B ND2 
4905 N N   . LEU B 306 ? 0.18880 0.20020 0.23440 -0.04450 0.01420  0.00720  300 LEU B N   
4906 C CA  . LEU B 306 ? 0.21500 0.22290 0.25730 -0.04450 0.00940  0.01240  300 LEU B CA  
4907 C C   . LEU B 306 ? 0.20260 0.20330 0.24400 -0.04470 0.00500  0.01890  300 LEU B C   
4908 O O   . LEU B 306 ? 0.19970 0.19840 0.24570 -0.04080 0.00070  0.02250  300 LEU B O   
4909 C CB  . LEU B 306 ? 0.22910 0.23840 0.26140 -0.05100 0.00980  0.01220  300 LEU B CB  
4910 C CG  . LEU B 306 ? 0.42450 0.43920 0.45840 -0.05060 0.01320  0.00600  300 LEU B CG  
4911 C CD1 . LEU B 306 ? 0.44390 0.45920 0.46600 -0.05830 0.01360  0.00520  300 LEU B CD1 
4912 C CD2 . LEU B 306 ? 0.32270 0.33790 0.36460 -0.04430 0.01030  0.00690  300 LEU B CD2 
4913 N N   . GLU B 307 ? 0.21100 0.20750 0.24720 -0.04980 0.00610  0.02050  301 GLU B N   
4914 C CA  . GLU B 307 ? 0.20070 0.18820 0.23720 -0.04970 0.00180  0.02690  301 GLU B CA  
4915 C C   . GLU B 307 ? 0.20830 0.19420 0.25690 -0.04200 0.00110  0.02530  301 GLU B C   
4916 O O   . GLU B 307 ? 0.22400 0.20520 0.27780 -0.03830 -0.00340 0.02970  301 GLU B O   
4917 C CB  . GLU B 307 ? 0.22870 0.21150 0.25880 -0.05670 0.00430  0.02800  301 GLU B CB  
4918 C CG  . GLU B 307 ? 0.28840 0.25940 0.31750 -0.05810 -0.00050 0.03600  301 GLU B CG  
4919 C CD  . GLU B 307 ? 0.31940 0.28520 0.34380 -0.06510 0.00300  0.03620  301 GLU B CD  
4920 O OE1 . GLU B 307 ? 0.34550 0.31680 0.37460 -0.06520 0.00850  0.02870  301 GLU B OE1 
4921 O OE2 . GLU B 307 ? 0.32240 0.27880 0.33900 -0.07080 -0.00010 0.04410  301 GLU B OE2 
4922 N N   . MET B 308 ? 0.15830 0.14880 0.21160 -0.03960 0.00540  0.01880  302 MET B N   
4923 C CA  . MET B 308 ? 0.16500 0.15510 0.22730 -0.03330 0.00550  0.01620  302 MET B CA  
4924 C C   . MET B 308 ? 0.17100 0.16500 0.23840 -0.02800 0.00390  0.01660  302 MET B C   
4925 O O   . MET B 308 ? 0.14640 0.13850 0.22110 -0.02330 0.00320  0.01640  302 MET B O   
4926 C CB  . MET B 308 ? 0.15180 0.14700 0.21590 -0.03300 0.00960  0.00970  302 MET B CB  
4927 C CG  . MET B 308 ? 0.18510 0.17720 0.24690 -0.03840 0.01140  0.00840  302 MET B CG  
4928 S SD  . MET B 308 ? 0.22960 0.20890 0.29410 -0.03880 0.00940  0.01120  302 MET B SD  
4929 C CE  . MET B 308 ? 0.20390 0.17500 0.26050 -0.04450 0.00600  0.02030  302 MET B CE  
4930 N N   . LEU B 309 ? 0.15190 0.15160 0.21640 -0.02880 0.00420  0.01630  303 LEU B N   
4931 C CA  . LEU B 309 ? 0.16520 0.16850 0.23450 -0.02490 0.00270  0.01690  303 LEU B CA  
4932 C C   . LEU B 309 ? 0.15180 0.15180 0.22520 -0.02370 -0.00230 0.02230  303 LEU B C   
4933 O O   . LEU B 309 ? 0.15450 0.15600 0.23690 -0.01890 -0.00290 0.02220  303 LEU B O   
4934 C CB  . LEU B 309 ? 0.16330 0.17150 0.22840 -0.02730 0.00360  0.01560  303 LEU B CB  
4935 C CG  . LEU B 309 ? 0.16700 0.17870 0.23680 -0.02490 0.00190  0.01650  303 LEU B CG  
4936 C CD1 . LEU B 309 ? 0.10420 0.11880 0.18040 -0.02010 0.00500  0.01350  303 LEU B CD1 
4937 C CD2 . LEU B 309 ? 0.13990 0.15410 0.20440 -0.02880 0.00200  0.01540  303 LEU B CD2 
4938 N N   . TYR B 310 ? 0.18120 0.17740 0.24790 -0.02820 -0.00610 0.02730  304 TYR B N   
4939 C CA  . TYR B 310 ? 0.17720 0.17070 0.24810 -0.02700 -0.01270 0.03380  304 TYR B CA  
4940 C C   . TYR B 310 ? 0.18230 0.16930 0.26290 -0.02240 -0.01380 0.03510  304 TYR B C   
4941 O O   . TYR B 310 ? 0.21500 0.20260 0.30680 -0.01760 -0.01720 0.03730  304 TYR B O   
4942 C CB  . TYR B 310 ? 0.18640 0.17640 0.24550 -0.03390 -0.01710 0.03970  304 TYR B CB  
4943 C CG  . TYR B 310 ? 0.22880 0.22480 0.27820 -0.03910 -0.01610 0.03760  304 TYR B CG  
4944 C CD1 . TYR B 310 ? 0.24340 0.24640 0.29790 -0.03660 -0.01550 0.03420  304 TYR B CD1 
4945 C CD2 . TYR B 310 ? 0.23220 0.22640 0.26720 -0.04710 -0.01520 0.03860  304 TYR B CD2 
4946 C CE1 . TYR B 310 ? 0.22700 0.23430 0.27340 -0.04150 -0.01440 0.03140  304 TYR B CE1 
4947 C CE2 . TYR B 310 ? 0.25300 0.25260 0.27930 -0.05210 -0.01340 0.03500  304 TYR B CE2 
4948 C CZ  . TYR B 310 ? 0.26710 0.27270 0.29970 -0.04900 -0.01320 0.03130  304 TYR B CZ  
4949 O OH  . TYR B 310 ? 0.33430 0.34410 0.35970 -0.05370 -0.01130 0.02700  304 TYR B OH  
4950 N N   . ALA B 311 ? 0.16280 0.14380 0.24070 -0.02380 -0.01060 0.03310  305 ALA B N   
4951 C CA  . ALA B 311 ? 0.16150 0.13540 0.24900 -0.01970 -0.01040 0.03240  305 ALA B CA  
4952 C C   . ALA B 311 ? 0.19960 0.17920 0.29830 -0.01320 -0.00690 0.02620  305 ALA B C   
4953 O O   . ALA B 311 ? 0.17990 0.15750 0.29080 -0.00800 -0.00860 0.02680  305 ALA B O   
4954 C CB  . ALA B 311 ? 0.16500 0.13260 0.24690 -0.02370 -0.00680 0.02980  305 ALA B CB  
4955 N N   . VAL B 312 ? 0.14230 0.12910 0.23700 -0.01360 -0.00190 0.02050  306 VAL B N   
4956 C CA  . VAL B 312 ? 0.14390 0.13640 0.24560 -0.00910 0.00220  0.01470  306 VAL B CA  
4957 C C   . VAL B 312 ? 0.16600 0.16440 0.27620 -0.00570 0.00040  0.01670  306 VAL B C   
4958 O O   . VAL B 312 ? 0.13250 0.13270 0.25360 -0.00130 0.00240  0.01380  306 VAL B O   
4959 C CB  . VAL B 312 ? 0.16540 0.16360 0.25940 -0.01110 0.00640  0.01030  306 VAL B CB  
4960 C CG1 . VAL B 312 ? 0.15510 0.16000 0.25340 -0.00770 0.01000  0.00630  306 VAL B CG1 
4961 C CG2 . VAL B 312 ? 0.17790 0.17220 0.26720 -0.01370 0.00840  0.00700  306 VAL B CG2 
4962 N N   . VAL B 313 ? 0.15780 0.16010 0.26390 -0.00830 -0.00280 0.02060  307 VAL B N   
4963 C CA  . VAL B 313 ? 0.14890 0.15770 0.26380 -0.00600 -0.00500 0.02240  307 VAL B CA  
4964 C C   . VAL B 313 ? 0.16930 0.17530 0.29700 -0.00200 -0.00960 0.02580  307 VAL B C   
4965 O O   . VAL B 313 ? 0.18350 0.19510 0.32470 0.00230  -0.00860 0.02400  307 VAL B O   
4966 C CB  . VAL B 313 ? 0.14630 0.15870 0.25380 -0.01040 -0.00850 0.02570  307 VAL B CB  
4967 C CG1 . VAL B 313 ? 0.11880 0.13830 0.23690 -0.00870 -0.01190 0.02770  307 VAL B CG1 
4968 C CG2 . VAL B 313 ? 0.14590 0.16130 0.24480 -0.01300 -0.00370 0.02160  307 VAL B CG2 
4969 N N   . THR B 314 ? 0.14940 0.14700 0.27390 -0.00360 -0.01460 0.03110  308 THR B N   
4970 C CA  . THR B 314 ? 0.20800 0.20140 0.34580 0.00070  -0.02030 0.03580  308 THR B CA  
4971 C C   . THR B 314 ? 0.19100 0.18130 0.34190 0.00650  -0.01540 0.02990  308 THR B C   
4972 O O   . THR B 314 ? 0.16800 0.16100 0.33630 0.01230  -0.01680 0.02960  308 THR B O   
4973 C CB  . THR B 314 ? 0.18190 0.16510 0.31120 -0.00330 -0.02710 0.04400  308 THR B CB  
4974 O OG1 . THR B 314 ? 0.19530 0.18200 0.31020 -0.00980 -0.03030 0.04790  308 THR B OG1 
4975 C CG2 . THR B 314 ? 0.19670 0.17630 0.34040 0.00130  -0.03520 0.05100  308 THR B CG2 
4976 N N   . GLU B 315 ? 0.16470 0.15010 0.30820 0.00490  -0.00940 0.02430  309 GLU B N   
4977 C CA  . GLU B 315 ? 0.17380 0.15660 0.32750 0.00940  -0.00380 0.01690  309 GLU B CA  
4978 C C   . GLU B 315 ? 0.17600 0.17020 0.33760 0.01250  0.00180  0.01060  309 GLU B C   
4979 O O   . GLU B 315 ? 0.18190 0.17700 0.35820 0.01760  0.00510  0.00560  309 GLU B O   
4980 C CB  . GLU B 315 ? 0.17660 0.15340 0.31840 0.00540  0.00070  0.01220  309 GLU B CB  
4981 C CG  . GLU B 315 ? 0.16840 0.14370 0.31610 0.00800  0.00770  0.00250  309 GLU B CG  
4982 C CD  . GLU B 315 ? 0.20940 0.17380 0.37070 0.01210  0.00650  0.00180  309 GLU B CD  
4983 O OE1 . GLU B 315 ? 0.21970 0.17660 0.38470 0.01250  -0.00070 0.01050  309 GLU B OE1 
4984 O OE2 . GLU B 315 ? 0.21210 0.17490 0.38070 0.01470  0.01250  -0.00730 309 GLU B OE2 
4985 N N   . LEU B 316 ? 0.17840 0.18110 0.33090 0.00930  0.00330  0.01060  310 LEU B N   
4986 C CA  . LEU B 316 ? 0.17370 0.18700 0.33170 0.01090  0.00890  0.00560  310 LEU B CA  
4987 C C   . LEU B 316 ? 0.13740 0.15720 0.31320 0.01500  0.00610  0.00780  310 LEU B C   
4988 O O   . LEU B 316 ? 0.15260 0.17850 0.34110 0.01850  0.01150  0.00210  310 LEU B O   
4989 C CB  . LEU B 316 ? 0.17450 0.19300 0.31840 0.00620  0.01040  0.00630  310 LEU B CB  
4990 C CG  . LEU B 316 ? 0.23340 0.26110 0.37840 0.00600  0.01650  0.00220  310 LEU B CG  
4991 C CD1 . LEU B 316 ? 0.19230 0.22040 0.33930 0.00770  0.02380  -0.00560 310 LEU B CD1 
4992 C CD2 . LEU B 316 ? 0.25090 0.27980 0.38110 0.00160  0.01700  0.00360  310 LEU B CD2 
4993 N N   . LEU B 317 ? 0.16020 0.17980 0.33770 0.01430  -0.00230 0.01560  311 LEU B N   
4994 C CA  . LEU B 317 ? 0.20370 0.23040 0.39990 0.01830  -0.00660 0.01830  311 LEU B CA  
4995 C C   . LEU B 317 ? 0.17910 0.20180 0.39410 0.02520  -0.00630 0.01590  311 LEU B C   
4996 O O   . LEU B 317 ? 0.17080 0.20200 0.40530 0.02990  -0.00410 0.01240  311 LEU B O   
4997 C CB  . LEU B 317 ? 0.19500 0.22110 0.38700 0.01540  -0.01710 0.02770  311 LEU B CB  
4998 C CG  . LEU B 317 ? 0.19550 0.22730 0.37350 0.00910  -0.01740 0.02890  311 LEU B CG  
4999 C CD1 . LEU B 317 ? 0.23260 0.26220 0.40330 0.00520  -0.02740 0.03720  311 LEU B CD1 
5000 C CD2 . LEU B 317 ? 0.21950 0.26400 0.40880 0.00990  -0.01420 0.02550  311 LEU B CD2 
5001 N N   . GLU B 318 ? 0.14170 0.15110 0.35230 0.02560  -0.00820 0.01740  312 GLU B N   
5002 C CA  . GLU B 318 ? 0.18340 0.18660 0.41200 0.03220  -0.00700 0.01400  312 GLU B CA  
5003 C C   . GLU B 318 ? 0.16910 0.17750 0.40410 0.03450  0.00470  0.00160  312 GLU B C   
5004 O O   . GLU B 318 ? 0.16270 0.17470 0.41630 0.03970  0.00750  -0.00320 312 GLU B O   
5005 C CB  . GLU B 318 ? 0.18880 0.17530 0.40950 0.03090  -0.01040 0.01750  312 GLU B CB  
5006 C CG  . GLU B 318 ? 0.23620 0.21330 0.47690 0.03790  -0.00950 0.01410  312 GLU B CG  
5007 C CD  . GLU B 318 ? 0.36670 0.32600 0.59990 0.03580  -0.01380 0.01910  312 GLU B CD  
5008 O OE1 . GLU B 318 ? 0.34880 0.30080 0.57130 0.03240  -0.00770 0.01290  312 GLU B OE1 
5009 O OE2 . GLU B 318 ? 0.42570 0.37970 0.66030 0.03580  -0.02340 0.02920  312 GLU B OE2 
5010 N N   . ARG B 319 ? 0.15630 0.16500 0.37300 0.02940  0.01160  -0.00370 313 ARG B N   
5011 C CA  . ARG B 319 ? 0.17010 0.18340 0.39010 0.03050  0.02240  -0.01520 313 ARG B CA  
5012 C C   . ARG B 319 ? 0.20920 0.23780 0.44040 0.03180  0.02720  -0.01840 313 ARG B C   
5013 O O   . ARG B 319 ? 0.18960 0.22240 0.43020 0.03410  0.03500  -0.02730 313 ARG B O   
5014 C CB  . ARG B 319 ? 0.22130 0.23240 0.41920 0.02440  0.02730  -0.01920 313 ARG B CB  
5015 C CG  . ARG B 319 ? 0.23820 0.23510 0.42930 0.02320  0.02560  -0.01980 313 ARG B CG  
5016 C CD  . ARG B 319 ? 0.25530 0.25190 0.42960 0.01830  0.03110  -0.02600 313 ARG B CD  
5017 N NE  . ARG B 319 ? 0.24310 0.22800 0.40860 0.01530  0.02770  -0.02430 313 ARG B NE  
5018 C CZ  . ARG B 319 ? 0.26190 0.24520 0.41420 0.01070  0.03110  -0.02970 313 ARG B CZ  
5019 N NH1 . ARG B 319 ? 0.22920 0.22070 0.37470 0.00890  0.03750  -0.03680 313 ARG B NH1 
5020 N NH2 . ARG B 319 ? 0.24060 0.21440 0.38610 0.00740  0.02780  -0.02770 313 ARG B NH2 
5021 N N   . LEU B 320 ? 0.15550 0.19180 0.38320 0.02920  0.02270  -0.01170 314 LEU B N   
5022 C CA  . LEU B 320 ? 0.18990 0.24080 0.42860 0.02950  0.02670  -0.01400 314 LEU B CA  
5023 C C   . LEU B 320 ? 0.15910 0.21260 0.41500 0.03370  0.02120  -0.01170 314 LEU B C   
5024 O O   . LEU B 320 ? 0.18540 0.24960 0.44810 0.03320  0.02410  -0.01400 314 LEU B O   
5025 C CB  . LEU B 320 ? 0.19240 0.24870 0.41710 0.02350  0.02420  -0.00840 314 LEU B CB  
5026 C CG  . LEU B 320 ? 0.16520 0.21790 0.36570 0.01750  0.02830  -0.00950 314 LEU B CG  
5027 C CD1 . LEU B 320 ? 0.11920 0.17300 0.30810 0.01280  0.02280  -0.00230 314 LEU B CD1 
5028 C CD2 . LEU B 320 ? 0.16410 0.22350 0.36160 0.01560  0.03910  -0.01720 314 LEU B CD2 
5029 N N   . GLY B 321 ? 0.16960 0.23210 0.39130 0.00300  0.04840  0.04230  315 GLY B N   
5030 C CA  . GLY B 321 ? 0.18280 0.27410 0.44120 0.00900  0.05010  0.05470  315 GLY B CA  
5031 C C   . GLY B 321 ? 0.25360 0.36390 0.51750 -0.00280 0.03460  0.06860  315 GLY B C   
5032 O O   . GLY B 321 ? 0.15910 0.30170 0.45170 -0.00310 0.03560  0.08030  315 GLY B O   
5033 N N   . ILE B 322 ? 0.21290 0.30500 0.45030 -0.01270 0.02050  0.06730  316 ILE B N   
5034 C CA  . ILE B 322 ? 0.21690 0.32250 0.45260 -0.02730 0.00600  0.07730  316 ILE B CA  
5035 C C   . ILE B 322 ? 0.31240 0.42640 0.56070 -0.02280 -0.00420 0.08630  316 ILE B C   
5036 O O   . ILE B 322 ? 0.27540 0.36770 0.50960 -0.01700 -0.00730 0.08100  316 ILE B O   
5037 C CB  . ILE B 322 ? 0.20290 0.28200 0.40130 -0.04120 -0.00180 0.06990  316 ILE B CB  
5038 C CG1 . ILE B 322 ? 0.24020 0.31540 0.42930 -0.04600 0.00830  0.06500  316 ILE B CG1 
5039 C CG2 . ILE B 322 ? 0.17650 0.26450 0.36990 -0.05780 -0.01680 0.07790  316 ILE B CG2 
5040 C CD1 . ILE B 322 ? 0.31220 0.35610 0.46410 -0.05670 0.00310  0.05840  316 ILE B CD1 
5041 N N   . GLY B 323 ? 0.41070 0.55920 0.68620 -0.02600 -0.00970 0.10120  317 GLY B N   
5042 C CA  . GLY B 323 ? 0.42940 0.59170 0.72090 -0.02080 -0.01900 0.11330  317 GLY B CA  
5043 C C   . GLY B 323 ? 0.46920 0.64010 0.79360 0.00050  -0.00750 0.11880  317 GLY B C   
5044 O O   . GLY B 323 ? 0.50480 0.66860 0.83750 0.01140  0.00870  0.11060  317 GLY B O   
5045 N N   . SER B 324 ? 0.47420 0.65940 0.81610 0.00590  -0.01570 0.13290  318 SER B N   
5046 C CA  . SER B 324 ? 0.42370 0.60520 0.78540 0.02540  -0.00590 0.13770  318 SER B CA  
5047 C C   . SER B 324 ? 0.45540 0.60590 0.80300 0.03190  -0.00640 0.13210  318 SER B C   
5048 O O   . SER B 324 ? 0.42020 0.55840 0.74310 0.02160  -0.01710 0.12800  318 SER B O   
5049 C CB  . SER B 324 ? 0.39110 0.59920 0.76750 0.02560  -0.01400 0.15620  318 SER B CB  
5050 O OG  . SER B 324 ? 0.42880 0.64150 0.78860 0.01240  -0.03190 0.16390  318 SER B OG  
5051 N N   . PRO B 325 ? 0.57220 0.70440 0.92670 0.04670  0.00600  0.12930  319 PRO B N   
5052 C CA  . PRO B 325 ? 0.58470 0.68920 0.92420 0.04970  0.00450  0.12580  319 PRO B CA  
5053 C C   . PRO B 325 ? 0.55390 0.66920 0.88620 0.04140  -0.01230 0.13990  319 PRO B C   
5054 O O   . PRO B 325 ? 0.55860 0.65710 0.87110 0.03700  -0.01830 0.13580  319 PRO B O   
5055 C CB  . PRO B 325 ? 0.60250 0.69370 0.95500 0.06360  0.01890  0.12460  319 PRO B CB  
5056 C CG  . PRO B 325 ? 0.57330 0.67360 0.93950 0.06930  0.03230  0.11770  319 PRO B CG  
5057 C CD  . PRO B 325 ? 0.54020 0.67450 0.91400 0.05960  0.02240  0.12710  319 PRO B CD  
5058 N N   . ASP B 326 ? 0.40680 0.55160 0.75290 0.03800  -0.02010 0.15610  320 ASP B N   
5059 C CA  . ASP B 326 ? 0.39350 0.55190 0.73220 0.02910  -0.03540 0.17050  320 ASP B CA  
5060 C C   . ASP B 326 ? 0.42100 0.58790 0.73740 0.01140  -0.05020 0.16760  320 ASP B C   
5061 O O   . ASP B 326 ? 0.44340 0.60510 0.74030 0.00370  -0.06030 0.16950  320 ASP B O   
5062 C CB  . ASP B 326 ? 0.43650 0.62370 0.79830 0.03220  -0.03730 0.18830  320 ASP B CB  
5063 C CG  . ASP B 326 ? 0.59820 0.77930 0.98460 0.05000  -0.02030 0.18730  320 ASP B CG  
5064 O OD1 . ASP B 326 ? 0.51770 0.70670 0.91500 0.05350  -0.01150 0.18070  320 ASP B OD1 
5065 O OD2 . ASP B 326 ? 0.65670 0.82390 1.05010 0.05990  -0.01500 0.19190  320 ASP B OD2 
5066 N N   . VAL B 327 ? 0.40820 0.58740 0.72550 0.00330  -0.05110 0.16220  321 VAL B N   
5067 C CA  . VAL B 327 ? 0.39730 0.57650 0.69050 -0.01510 -0.06310 0.15480  321 VAL B CA  
5068 C C   . VAL B 327 ? 0.37340 0.51260 0.63450 -0.01350 -0.05830 0.13670  321 VAL B C   
5069 O O   . VAL B 327 ? 0.38140 0.51100 0.61680 -0.02160 -0.06690 0.13420  321 VAL B O   
5070 C CB  . VAL B 327 ? 0.36400 0.55370 0.65900 -0.02480 -0.06020 0.14880  321 VAL B CB  
5071 C CG1 . VAL B 327 ? 0.35800 0.52130 0.61030 -0.04150 -0.06450 0.13170  321 VAL B CG1 
5072 C CG2 . VAL B 327 ? 0.33720 0.56080 0.64500 -0.03230 -0.06680 0.16330  321 VAL B CG2 
5073 N N   . ARG B 328 ? 0.37280 0.49000 0.63490 -0.00270 -0.04370 0.12390  322 ARG B N   
5074 C CA  . ARG B 328 ? 0.40040 0.48350 0.63260 -0.00210 -0.03940 0.10700  322 ARG B CA  
5075 C C   . ARG B 328 ? 0.44600 0.51880 0.67560 0.00410  -0.04110 0.11090  322 ARG B C   
5076 O O   . ARG B 328 ? 0.39590 0.44840 0.59870 0.00080  -0.04180 0.09990  322 ARG B O   
5077 C CB  . ARG B 328 ? 0.36100 0.42710 0.59440 0.00580  -0.02450 0.09350  322 ARG B CB  
5078 C CG  . ARG B 328 ? 0.34980 0.42300 0.57960 -0.00250 -0.02230 0.08870  322 ARG B CG  
5079 C CD  . ARG B 328 ? 0.30010 0.35570 0.52410 0.00350  -0.00830 0.07490  322 ARG B CD  
5080 N NE  . ARG B 328 ? 0.37250 0.43000 0.62210 0.01830  0.00410  0.07620  322 ARG B NE  
5081 C CZ  . ARG B 328 ? 0.39650 0.47020 0.67030 0.02430  0.01460  0.07880  322 ARG B CZ  
5082 N NH1 . ARG B 328 ? 0.32620 0.41740 0.60160 0.01550  0.01450  0.08060  322 ARG B NH1 
5083 N NH2 . ARG B 328 ? 0.39890 0.47050 0.69590 0.03920  0.02660  0.07960  322 ARG B NH2 
5084 N N   . SER B 329 ? 0.38040 0.46720 0.63790 0.01320  -0.04150 0.12730  323 SER B N   
5085 C CA  . SER B 329 ? 0.36240 0.43810 0.61560 0.01700  -0.04340 0.13260  323 SER B CA  
5086 C C   . SER B 329 ? 0.35390 0.43660 0.58180 0.00340  -0.05720 0.13610  323 SER B C   
5087 O O   . SER B 329 ? 0.37160 0.44310 0.58700 0.00350  -0.05820 0.13650  323 SER B O   
5088 C CB  . SER B 329 ? 0.33930 0.42260 0.61540 0.02540  -0.03820 0.14560  323 SER B CB  
5089 O OG  . SER B 329 ? 0.42980 0.54260 0.71400 0.01900  -0.04880 0.16180  323 SER B OG  
5090 N N   . GLN B 330 ? 0.39150 0.49250 0.61020 -0.00940 -0.06720 0.13810  324 GLN B N   
5091 C CA  . GLN B 330 ? 0.31260 0.41590 0.50110 -0.02370 -0.07840 0.13640  324 GLN B CA  
5092 C C   . GLN B 330 ? 0.32610 0.40000 0.48230 -0.02570 -0.07290 0.11560  324 GLN B C   
5093 O O   . GLN B 330 ? 0.36080 0.43160 0.49250 -0.03300 -0.07800 0.11260  324 GLN B O   
5094 C CB  . GLN B 330 ? 0.30440 0.43050 0.48910 -0.03890 -0.08930 0.14040  324 GLN B CB  
5095 C CG  . GLN B 330 ? 0.36030 0.52230 0.58190 -0.03590 -0.09510 0.16350  324 GLN B CG  
5096 C CD  . GLN B 330 ? 0.50050 0.68640 0.71730 -0.05270 -0.10430 0.16720  324 GLN B CD  
5097 O OE1 . GLN B 330 ? 0.51920 0.70450 0.70650 -0.07080 -0.11430 0.16020  324 GLN B OE1 
5098 N NE2 . GLN B 330 ? 0.42490 0.63000 0.66860 -0.04730 -0.09980 0.17720  324 GLN B NE2 
5099 N N   . LEU B 331 ? 0.30240 0.35670 0.45890 -0.01830 -0.06200 0.10200  325 LEU B N   
5100 C CA  . LEU B 331 ? 0.31830 0.34790 0.44820 -0.01840 -0.05690 0.08410  325 LEU B CA  
5101 C C   . LEU B 331 ? 0.27810 0.29350 0.41280 -0.00780 -0.04800 0.08020  325 LEU B C   
5102 O O   . LEU B 331 ? 0.26350 0.26180 0.38240 -0.00590 -0.04260 0.06630  325 LEU B O   
5103 C CB  . LEU B 331 ? 0.29790 0.31700 0.42090 -0.02040 -0.05280 0.07240  325 LEU B CB  
5104 C CG  . LEU B 331 ? 0.28030 0.31250 0.39920 -0.03350 -0.06140 0.07630  325 LEU B CG  
5105 C CD1 . LEU B 331 ? 0.26250 0.28360 0.37650 -0.03600 -0.05660 0.06710  325 LEU B CD1 
5106 C CD2 . LEU B 331 ? 0.28190 0.30920 0.37140 -0.04450 -0.06950 0.07160  325 LEU B CD2 
5107 N N   . ALA B 332 ? 0.31200 0.33430 0.46860 -0.00170 -0.04690 0.09320  326 ALA B N   
5108 C CA  . ALA B 332 ? 0.27410 0.28080 0.43770 0.00660  -0.03790 0.09000  326 ALA B CA  
5109 C C   . ALA B 332 ? 0.26270 0.25970 0.40330 0.00300  -0.03790 0.08180  326 ALA B C   
5110 O O   . ALA B 332 ? 0.27770 0.26060 0.41580 0.00650  -0.03030 0.07210  326 ALA B O   
5111 C CB  . ALA B 332 ? 0.32160 0.33540 0.51200 0.01290  -0.03780 0.10800  326 ALA B CB  
5112 N N   . SER B 333 ? 0.26010 0.26670 0.38370 -0.00460 -0.04580 0.08540  327 SER B N   
5113 C CA  . SER B 333 ? 0.31640 0.31710 0.41950 -0.00700 -0.04410 0.07720  327 SER B CA  
5114 C C   . SER B 333 ? 0.29290 0.28120 0.37930 -0.00550 -0.03960 0.05910  327 SER B C   
5115 O O   . SER B 333 ? 0.29390 0.27640 0.37210 -0.00330 -0.03490 0.05130  327 SER B O   
5116 C CB  . SER B 333 ? 0.32300 0.33750 0.40940 -0.01580 -0.05210 0.08380  327 SER B CB  
5117 O OG  . SER B 333 ? 0.42300 0.44180 0.49650 -0.02220 -0.05800 0.07950  327 SER B OG  
5118 N N   . PHE B 334 ? 0.30260 0.28790 0.38510 -0.00670 -0.04110 0.05380  328 PHE B N   
5119 C CA  . PHE B 334 ? 0.27850 0.25040 0.34740 -0.00410 -0.03700 0.03950  328 PHE B CA  
5120 C C   . PHE B 334 ? 0.24920 0.21350 0.33100 0.00210  -0.02980 0.03540  328 PHE B C   
5121 O O   . PHE B 334 ? 0.26910 0.22530 0.34160 0.00530  -0.02590 0.02590  328 PHE B O   
5122 C CB  . PHE B 334 ? 0.28630 0.25490 0.34450 -0.00970 -0.04130 0.03620  328 PHE B CB  
5123 C CG  . PHE B 334 ? 0.28170 0.25320 0.32020 -0.01780 -0.04760 0.03560  328 PHE B CG  
5124 C CD1 . PHE B 334 ? 0.28660 0.24730 0.30250 -0.01660 -0.04530 0.02440  328 PHE B CD1 
5125 C CD2 . PHE B 334 ? 0.30010 0.28640 0.34270 -0.02670 -0.05550 0.04590  328 PHE B CD2 
5126 C CE1 . PHE B 334 ? 0.33800 0.29930 0.33270 -0.02460 -0.04950 0.02130  328 PHE B CE1 
5127 C CE2 . PHE B 334 ? 0.31010 0.29930 0.33080 -0.03680 -0.06160 0.04380  328 PHE B CE2 
5128 C CZ  . PHE B 334 ? 0.30280 0.27770 0.29820 -0.03600 -0.05790 0.03030  328 PHE B CZ  
5129 N N   . HIS B 335 ? 0.22800 0.19610 0.33090 0.00410  -0.02760 0.04250  329 HIS B N   
5130 C CA  . HIS B 335 ? 0.23630 0.19650 0.34900 0.00900  -0.01930 0.03660  329 HIS B CA  
5131 C C   . HIS B 335 ? 0.28070 0.23340 0.39300 0.01130  -0.01400 0.03150  329 HIS B C   
5132 O O   . HIS B 335 ? 0.24190 0.18740 0.34760 0.01230  -0.00930 0.02140  329 HIS B O   
5133 C CB  . HIS B 335 ? 0.23610 0.20330 0.37330 0.01200  -0.01670 0.04560  329 HIS B CB  
5134 C CG  . HIS B 335 ? 0.24770 0.20800 0.39320 0.01630  -0.00680 0.03820  329 HIS B CG  
5135 N ND1 . HIS B 335 ? 0.30500 0.27010 0.47450 0.02170  -0.00070 0.04390  329 HIS B ND1 
5136 C CD2 . HIS B 335 ? 0.26970 0.22060 0.40230 0.01590  -0.00170 0.02590  329 HIS B CD2 
5137 C CE1 . HIS B 335 ? 0.30710 0.26460 0.47640 0.02400  0.00900  0.03360  329 HIS B CE1 
5138 N NE2 . HIS B 335 ? 0.25340 0.20290 0.39950 0.01960  0.00780  0.02310  329 HIS B NE2 
5139 N N   . HIS B 336 ? 0.26680 0.22220 0.38520 0.01050  -0.01540 0.03910  330 HIS B N   
5140 C CA  . HIS B 336 ? 0.29890 0.24740 0.41880 0.01000  -0.01060 0.03580  330 HIS B CA  
5141 C C   . HIS B 336 ? 0.28040 0.23710 0.39000 0.00600  -0.01540 0.04020  330 HIS B C   
5142 O O   . HIS B 336 ? 0.30840 0.26880 0.42580 0.00410  -0.01750 0.05190  330 HIS B O   
5143 C CB  . HIS B 336 ? 0.29860 0.23850 0.43960 0.01290  -0.00480 0.04190  330 HIS B CB  
5144 C CG  . HIS B 336 ? 0.34100 0.27410 0.49180 0.01760  0.00250  0.03580  330 HIS B CG  
5145 N ND1 . HIS B 336 ? 0.38820 0.32650 0.55720 0.02300  0.00350  0.04440  330 HIS B ND1 
5146 C CD2 . HIS B 336 ? 0.32170 0.24650 0.46570 0.01720  0.00920  0.02220  330 HIS B CD2 
5147 C CE1 . HIS B 336 ? 0.36190 0.29530 0.53480 0.02610  0.01190  0.03540  330 HIS B CE1 
5148 N NE2 . HIS B 336 ? 0.33140 0.25500 0.48830 0.02230  0.01530  0.02180  330 HIS B NE2 
5149 N N   . PRO B 337 ? 0.27960 0.24040 0.37170 0.00510  -0.01680 0.03190  331 PRO B N   
5150 C CA  . PRO B 337 ? 0.32890 0.29990 0.41000 0.00210  -0.01970 0.03460  331 PRO B CA  
5151 C C   . PRO B 337 ? 0.32020 0.29360 0.40900 -0.00210 -0.01730 0.04060  331 PRO B C   
5152 O O   . PRO B 337 ? 0.32250 0.28890 0.41830 -0.00320 -0.01260 0.03640  331 PRO B O   
5153 C CB  . PRO B 337 ? 0.30530 0.27810 0.37160 0.00510  -0.01850 0.02300  331 PRO B CB  
5154 C CG  . PRO B 337 ? 0.30110 0.26410 0.36650 0.00870  -0.01810 0.01700  331 PRO B CG  
5155 C CD  . PRO B 337 ? 0.27610 0.23280 0.35800 0.00800  -0.01580 0.02110  331 PRO B CD  
5156 N N   . GLN B 338 ? 0.37790 0.36110 0.46360 -0.00620 -0.02050 0.05070  332 GLN B N   
5157 C CA  . GLN B 338 ? 0.37950 0.36690 0.46940 -0.01210 -0.01870 0.05840  332 GLN B CA  
5158 C C   . GLN B 338 ? 0.34390 0.33700 0.42820 -0.01410 -0.01440 0.04850  332 GLN B C   
5159 O O   . GLN B 338 ? 0.35680 0.36010 0.42850 -0.01100 -0.01430 0.04030  332 GLN B O   
5160 C CB  . GLN B 338 ? 0.36230 0.36430 0.44250 -0.01670 -0.02310 0.06900  332 GLN B CB  
5161 C CG  . GLN B 338 ? 0.48260 0.48510 0.56950 -0.01710 -0.02930 0.08290  332 GLN B CG  
5162 C CD  . GLN B 338 ? 0.62330 0.61550 0.73130 -0.01700 -0.02800 0.09650  332 GLN B CD  
5163 O OE1 . GLN B 338 ? 0.64570 0.62440 0.76930 -0.01100 -0.02550 0.09520  332 GLN B OE1 
5164 N NE2 . GLN B 338 ? 0.64180 0.63900 0.75010 -0.02360 -0.02870 0.10980  332 GLN B NE2 
5165 N N   . ARG B 339 ? 0.33740 0.32400 0.43150 -0.01940 -0.01070 0.04940  333 ARG B N   
5166 C CA  . ARG B 339 ? 0.32990 0.32820 0.42060 -0.02480 -0.00780 0.04320  333 ARG B CA  
5167 C C   . ARG B 339 ? 0.35440 0.35550 0.45040 -0.03540 -0.00640 0.05450  333 ARG B C   
5168 O O   . ARG B 339 ? 0.33430 0.32210 0.43940 -0.04250 -0.00340 0.05500  333 ARG B O   
5169 C CB  . ARG B 339 ? 0.38420 0.37380 0.47820 -0.02490 -0.00510 0.03150  333 ARG B CB  
5170 C CG  . ARG B 339 ? 0.32700 0.32010 0.41280 -0.01590 -0.00660 0.02130  333 ARG B CG  
5171 C CD  . ARG B 339 ? 0.37270 0.38760 0.44920 -0.01250 -0.00750 0.01910  333 ARG B CD  
5172 N NE  . ARG B 339 ? 0.37670 0.39210 0.44560 -0.00320 -0.00870 0.01090  333 ARG B NE  
5173 C CZ  . ARG B 339 ? 0.39530 0.40440 0.45580 0.00430  -0.01050 0.00990  333 ARG B CZ  
5174 N NH1 . ARG B 339 ? 0.31810 0.32210 0.37640 0.00300  -0.01220 0.01600  333 ARG B NH1 
5175 N NH2 . ARG B 339 ? 0.35130 0.35930 0.40500 0.01220  -0.01110 0.00350  333 ARG B NH2 
5176 N N   . VAL B 340 ? 0.33480 0.35240 0.42340 -0.03760 -0.00800 0.06310  334 VAL B N   
5177 C CA  . VAL B 340 ? 0.34800 0.36930 0.43970 -0.04810 -0.00740 0.07760  334 VAL B CA  
5178 C C   . VAL B 340 ? 0.36110 0.41090 0.44330 -0.05350 -0.00480 0.07670  334 VAL B C   
5179 O O   . VAL B 340 ? 0.34240 0.40810 0.41210 -0.04730 -0.00500 0.07190  334 VAL B O   
5180 C CB  . VAL B 340 ? 0.39390 0.41050 0.48570 -0.04670 -0.01210 0.09300  334 VAL B CB  
5181 C CG1 . VAL B 340 ? 0.35530 0.37890 0.44720 -0.05770 -0.01200 0.10980  334 VAL B CG1 
5182 C CG2 . VAL B 340 ? 0.38990 0.38120 0.49660 -0.04030 -0.01330 0.09590  334 VAL B CG2 
5183 N N   . ASN B 341 ? 0.34260 0.39850 0.43060 -0.06540 -0.00160 0.08090  335 ASN B N   
5184 C CA  . ASN B 341 ? 0.27090 0.35840 0.35370 -0.07020 0.00210  0.07890  335 ASN B CA  
5185 C C   . ASN B 341 ? 0.29850 0.40180 0.37130 -0.07510 0.00260  0.09200  335 ASN B C   
5186 O O   . ASN B 341 ? 0.33420 0.42540 0.40300 -0.07390 -0.00140 0.10210  335 ASN B O   
5187 C CB  . ASN B 341 ? 0.26390 0.35550 0.35690 -0.08310 0.00480  0.07760  335 ASN B CB  
5188 C CG  . ASN B 341 ? 0.30180 0.38000 0.40080 -0.09870 0.00540  0.09290  335 ASN B CG  
5189 O OD1 . ASN B 341 ? 0.33310 0.40240 0.42920 -0.09950 0.00370  0.10730  335 ASN B OD1 
5190 N ND2 . ASN B 341 ? 0.29740 0.37500 0.40420 -0.11270 0.00760  0.09090  335 ASN B ND2 
5191 N N   . THR B 342 ? 0.25430 0.38770 0.32320 -0.08140 0.00770  0.09300  336 THR B N   
5192 C CA  . THR B 342 ? 0.35110 0.50370 0.40660 -0.08590 0.00960  0.10310  336 THR B CA  
5193 C C   . THR B 342 ? 0.38520 0.52930 0.44340 -0.10070 0.00740  0.12420  336 THR B C   
5194 O O   . THR B 342 ? 0.31460 0.47360 0.36000 -0.10600 0.00780  0.13550  336 THR B O   
5195 C CB  . THR B 342 ? 0.32940 0.52000 0.38100 -0.08700 0.01770  0.09710  336 THR B CB  
5196 O OG1 . THR B 342 ? 0.27340 0.47590 0.33870 -0.10080 0.02040  0.10230  336 THR B OG1 
5197 C CG2 . THR B 342 ? 0.30550 0.50310 0.35590 -0.07000 0.02010  0.07810  336 THR B CG2 
5198 N N   . MET B 343 ? 0.38340 0.50280 0.45650 -0.10770 0.00570  0.12990  337 MET B N   
5199 C CA  . MET B 343 ? 0.35740 0.46130 0.43510 -0.12010 0.00370  0.15100  337 MET B CA  
5200 C C   . MET B 343 ? 0.36850 0.43550 0.45530 -0.11240 -0.00180 0.15680  337 MET B C   
5201 O O   . MET B 343 ? 0.36030 0.40410 0.45690 -0.12000 -0.00260 0.17200  337 MET B O   
5202 C CB  . MET B 343 ? 0.29980 0.40340 0.38740 -0.13700 0.00800  0.15470  337 MET B CB  
5203 C CG  . MET B 343 ? 0.35130 0.49750 0.43330 -0.14540 0.01400  0.15180  337 MET B CG  
5204 S SD  . MET B 343 ? 0.37010 0.54340 0.43570 -0.15400 0.01590  0.17160  337 MET B SD  
5205 C CE  . MET B 343 ? 0.35390 0.50150 0.42560 -0.16840 0.01420  0.18560  337 MET B CE  
5206 N N   . GLY B 344 ? 0.36640 0.42720 0.45170 -0.09740 -0.00470 0.14460  338 GLY B N   
5207 C CA  . GLY B 344 ? 0.40480 0.43820 0.49950 -0.08840 -0.00940 0.15020  338 GLY B CA  
5208 C C   . GLY B 344 ? 0.41340 0.41500 0.52450 -0.08720 -0.00670 0.14410  338 GLY B C   
5209 O O   . GLY B 344 ? 0.43540 0.41220 0.55820 -0.08110 -0.00850 0.15280  338 GLY B O   
5210 N N   . VAL B 345 ? 0.39070 0.39340 0.50310 -0.09290 -0.00200 0.12960  339 VAL B N   
5211 C CA  . VAL B 345 ? 0.45600 0.42920 0.57950 -0.09310 0.00130  0.11940  339 VAL B CA  
5212 C C   . VAL B 345 ? 0.36650 0.34030 0.48780 -0.07990 0.00070  0.10080  339 VAL B C   
5213 O O   . VAL B 345 ? 0.27880 0.27800 0.39070 -0.07640 -0.00010 0.09030  339 VAL B O   
5214 C CB  . VAL B 345 ? 0.37610 0.35140 0.50050 -0.11010 0.00560  0.11430  339 VAL B CB  
5215 C CG1 . VAL B 345 ? 0.37290 0.31470 0.50530 -0.11290 0.00930  0.10300  339 VAL B CG1 
5216 C CG2 . VAL B 345 ? 0.36720 0.34470 0.49230 -0.12450 0.00620  0.13400  339 VAL B CG2 
5217 N N   . THR B 346 ? 0.37800 0.32370 0.50870 -0.07200 0.00190  0.09720  340 THR B N   
5218 C CA  . THR B 346 ? 0.31330 0.25740 0.44190 -0.06190 0.00230  0.07990  340 THR B CA  
5219 C C   . THR B 346 ? 0.32860 0.27440 0.45370 -0.07070 0.00570  0.06400  340 THR B C   
5220 O O   . THR B 346 ? 0.37160 0.29660 0.50190 -0.08090 0.00990  0.06200  340 THR B O   
5221 C CB  . THR B 346 ? 0.40600 0.32230 0.54640 -0.05190 0.00430  0.08060  340 THR B CB  
5222 O OG1 . THR B 346 ? 0.40510 0.32810 0.54890 -0.04300 -0.00080 0.09490  340 THR B OG1 
5223 C CG2 . THR B 346 ? 0.33390 0.24820 0.47090 -0.04470 0.00620  0.06200  340 THR B CG2 
5224 N N   . THR B 347 ? 0.29060 0.26040 0.40680 -0.06690 0.00370  0.05280  341 THR B N   
5225 C CA  . THR B 347 ? 0.27420 0.25470 0.38740 -0.07530 0.00490  0.04030  341 THR B CA  
5226 C C   . THR B 347 ? 0.24660 0.21890 0.35670 -0.06860 0.00520  0.02550  341 THR B C   
5227 O O   . THR B 347 ? 0.25470 0.23330 0.36170 -0.07700 0.00550  0.01530  341 THR B O   
5228 C CB  . THR B 347 ? 0.24980 0.26830 0.35750 -0.07620 0.00280  0.04080  341 THR B CB  
5229 O OG1 . THR B 347 ? 0.26390 0.29310 0.36510 -0.06100 0.00040  0.03980  341 THR B OG1 
5230 C CG2 . THR B 347 ? 0.29300 0.32320 0.40260 -0.08690 0.00390  0.05430  341 THR B CG2 
5231 N N   . GLY B 348 ? 0.30220 0.26230 0.41250 -0.05530 0.00480  0.02470  342 GLY B N   
5232 C CA  . GLY B 348 ? 0.23210 0.18540 0.33840 -0.05000 0.00580  0.01170  342 GLY B CA  
5233 C C   . GLY B 348 ? 0.27070 0.21640 0.37830 -0.03610 0.00490  0.01400  342 GLY B C   
5234 O O   . GLY B 348 ? 0.28990 0.23000 0.40400 -0.03190 0.00410  0.02540  342 GLY B O   
5235 N N   . GLY B 349 ? 0.24570 0.19370 0.34670 -0.03020 0.00440  0.00450  343 GLY B N   
5236 C CA  . GLY B 349 ? 0.25880 0.20140 0.36080 -0.01910 0.00350  0.00630  343 GLY B CA  
5237 C C   . GLY B 349 ? 0.28370 0.23230 0.37580 -0.01420 0.00220  -0.00270 343 GLY B C   
5238 O O   . GLY B 349 ? 0.28640 0.24730 0.37060 -0.01730 0.00050  -0.00880 343 GLY B O   
5239 N N   . VAL B 350 ? 0.24860 0.18930 0.34240 -0.00700 0.00280  -0.00220 344 VAL B N   
5240 C CA  A VAL B 350 ? 0.23700 0.18060 0.32140 -0.00250 0.00160  -0.00810 344 VAL B CA  
5241 C CA  B VAL B 350 ? 0.23700 0.18060 0.32150 -0.00250 0.00160  -0.00810 344 VAL B CA  
5242 C C   . VAL B 350 ? 0.25230 0.18270 0.33980 -0.00320 0.00820  -0.01490 344 VAL B C   
5243 O O   . VAL B 350 ? 0.28700 0.20530 0.38700 -0.00200 0.01330  -0.01250 344 VAL B O   
5244 C CB  A VAL B 350 ? 0.25670 0.20360 0.33840 0.00440  -0.00290 -0.00220 344 VAL B CB  
5245 C CB  B VAL B 350 ? 0.25650 0.20330 0.33880 0.00430  -0.00290 -0.00180 344 VAL B CB  
5246 C CG1 A VAL B 350 ? 0.25830 0.19670 0.35200 0.00690  -0.00100 0.00360  344 VAL B CG1 
5247 C CG1 B VAL B 350 ? 0.21330 0.15900 0.28610 0.00800  -0.00380 -0.00650 344 VAL B CG1 
5248 C CG2 A VAL B 350 ? 0.21560 0.16520 0.28470 0.00800  -0.00520 -0.00710 344 VAL B CG2 
5249 C CG2 B VAL B 350 ? 0.25570 0.21430 0.33240 0.00480  -0.00740 0.00260  344 VAL B CG2 
5250 N N   . SER B 351 ? 0.22650 0.16000 0.30300 -0.00480 0.00870  -0.02300 345 SER B N   
5251 C CA  . SER B 351 ? 0.20350 0.12650 0.27980 -0.00560 0.01600  -0.03030 345 SER B CA  
5252 C C   . SER B 351 ? 0.24750 0.17720 0.31180 -0.00290 0.01340  -0.03150 345 SER B C   
5253 O O   . SER B 351 ? 0.24280 0.18280 0.29830 -0.00080 0.00630  -0.02820 345 SER B O   
5254 C CB  . SER B 351 ? 0.29200 0.20760 0.36460 -0.01500 0.02170  -0.04100 345 SER B CB  
5255 O OG  . SER B 351 ? 0.34740 0.27750 0.40760 -0.02150 0.01590  -0.04410 345 SER B OG  
5256 N N   . PHE B 352 ? 0.21950 0.14290 0.28400 -0.00260 0.02020  -0.03590 346 PHE B N   
5257 C CA  . PHE B 352 ? 0.22080 0.14860 0.27620 -0.00050 0.01880  -0.03420 346 PHE B CA  
5258 C C   . PHE B 352 ? 0.26600 0.19380 0.30890 -0.00640 0.02480  -0.04370 346 PHE B C   
5259 O O   . PHE B 352 ? 0.26680 0.19140 0.31180 -0.00590 0.03260  -0.04630 346 PHE B O   
5260 C CB  . PHE B 352 ? 0.24420 0.16930 0.31270 0.00470  0.02120  -0.02770 346 PHE B CB  
5261 C CG  . PHE B 352 ? 0.18780 0.11470 0.26560 0.00850  0.01470  -0.01830 346 PHE B CG  
5262 C CD1 . PHE B 352 ? 0.20000 0.13080 0.26790 0.00980  0.00610  -0.01360 346 PHE B CD1 
5263 C CD2 . PHE B 352 ? 0.22950 0.15320 0.32500 0.01080  0.01750  -0.01400 346 PHE B CD2 
5264 C CE1 . PHE B 352 ? 0.21600 0.14880 0.28910 0.01170  0.00080  -0.00660 346 PHE B CE1 
5265 C CE2 . PHE B 352 ? 0.21370 0.14160 0.31570 0.01280  0.01080  -0.00420 346 PHE B CE2 
5266 C CZ  . PHE B 352 ? 0.18880 0.12190 0.27820 0.01240  0.00260  -0.00150 346 PHE B CZ  
5267 N N   . PRO B 353 ? 0.26820 0.20260 0.29790 -0.01300 0.02150  -0.04890 347 PRO B N   
5268 C CA  . PRO B 353 ? 0.29520 0.23240 0.30880 -0.02060 0.02600  -0.05760 347 PRO B CA  
5269 C C   . PRO B 353 ? 0.32430 0.26940 0.32610 -0.01840 0.02140  -0.05060 347 PRO B C   
5270 O O   . PRO B 353 ? 0.35590 0.31250 0.34410 -0.02080 0.01370  -0.04740 347 PRO B O   
5271 C CB  . PRO B 353 ? 0.24640 0.19210 0.25100 -0.02960 0.02120  -0.06300 347 PRO B CB  
5272 C CG  . PRO B 353 ? 0.27220 0.22740 0.28350 -0.02330 0.01110  -0.05240 347 PRO B CG  
5273 C CD  . PRO B 353 ? 0.24150 0.18560 0.26950 -0.01430 0.01300  -0.04610 347 PRO B CD  
5274 N N   . PHE B 354 ? 0.28980 0.22970 0.29840 -0.01350 0.02520  -0.04590 348 PHE B N   
5275 C CA  . PHE B 354 ? 0.29340 0.23710 0.29010 -0.01420 0.02380  -0.04030 348 PHE B CA  
5276 C C   . PHE B 354 ? 0.34400 0.28530 0.34520 -0.01610 0.03590  -0.04480 348 PHE B C   
5277 O O   . PHE B 354 ? 0.32500 0.26080 0.34220 -0.01350 0.04440  -0.05010 348 PHE B O   
5278 C CB  . PHE B 354 ? 0.29120 0.23250 0.29000 -0.00750 0.01470  -0.02790 348 PHE B CB  
5279 C CG  . PHE B 354 ? 0.28770 0.22280 0.30460 -0.00250 0.01530  -0.02410 348 PHE B CG  
5280 C CD1 . PHE B 354 ? 0.27050 0.20490 0.29750 -0.00320 0.02220  -0.02290 348 PHE B CD1 
5281 C CD2 . PHE B 354 ? 0.28710 0.22030 0.31010 0.00240  0.00850  -0.02050 348 PHE B CD2 
5282 C CE1 . PHE B 354 ? 0.24830 0.18140 0.29210 0.00030  0.02090  -0.01740 348 PHE B CE1 
5283 C CE2 . PHE B 354 ? 0.29230 0.22210 0.32890 0.00530  0.00770  -0.01600 348 PHE B CE2 
5284 C CZ  . PHE B 354 ? 0.25220 0.18260 0.29960 0.00390  0.01310  -0.01400 348 PHE B CZ  
5285 N N   . LYS B 355 ? 0.31740 0.26390 0.30500 -0.02030 0.03750  -0.04210 349 LYS B N   
5286 C CA  . LYS B 355 ? 0.31700 0.26580 0.30610 -0.02340 0.05070  -0.04740 349 LYS B CA  
5287 C C   . LYS B 355 ? 0.30430 0.25680 0.29140 -0.02410 0.04840  -0.03550 349 LYS B C   
5288 O O   . LYS B 355 ? 0.30960 0.26450 0.27830 -0.02820 0.04180  -0.02850 349 LYS B O   
5289 C CB  . LYS B 355 ? 0.34990 0.30330 0.31860 -0.03260 0.05750  -0.05920 349 LYS B CB  
5290 C CG  . LYS B 355 ? 0.39400 0.34850 0.36420 -0.03510 0.07460  -0.06950 349 LYS B CG  
5291 C CD  . LYS B 355 ? 0.45490 0.41080 0.40220 -0.04560 0.08070  -0.08430 349 LYS B CD  
5292 C CE  . LYS B 355 ? 0.45860 0.41720 0.40130 -0.04900 0.09890  -0.09520 349 LYS B CE  
5293 N NZ  . LYS B 355 ? 0.62260 0.58200 0.53760 -0.06170 0.10520  -0.11170 349 LYS B NZ  
5294 N N   . LEU B 356 ? 0.31210 0.26550 0.31900 -0.02040 0.05320  -0.03170 350 LEU B N   
5295 C CA  . LEU B 356 ? 0.30300 0.26050 0.30900 -0.02380 0.05160  -0.02090 350 LEU B CA  
5296 C C   . LEU B 356 ? 0.35810 0.32440 0.34760 -0.03210 0.06040  -0.02320 350 LEU B C   
5297 O O   . LEU B 356 ? 0.32850 0.30070 0.31840 -0.03320 0.07350  -0.03460 350 LEU B O   
5298 C CB  . LEU B 356 ? 0.35500 0.31810 0.38760 -0.02010 0.05610  -0.01730 350 LEU B CB  
5299 C CG  . LEU B 356 ? 0.36070 0.32520 0.39840 -0.02360 0.04900  -0.00460 350 LEU B CG  
5300 C CD1 . LEU B 356 ? 0.27970 0.22910 0.30490 -0.02310 0.03410  0.00140  350 LEU B CD1 
5301 C CD2 . LEU B 356 ? 0.38130 0.35580 0.44840 -0.01890 0.05250  -0.00240 350 LEU B CD2 
5302 N N   . ARG B 357 ? 0.27960 0.24560 0.25310 -0.03810 0.05440  -0.01250 351 ARG B N   
5303 C CA  . ARG B 357 ? 0.33890 0.31570 0.29620 -0.04730 0.06330  -0.01270 351 ARG B CA  
5304 C C   . ARG B 357 ? 0.34950 0.33060 0.31150 -0.05310 0.06450  -0.00050 351 ARG B C   
5305 O O   . ARG B 357 ? 0.33510 0.30550 0.30020 -0.05270 0.05380  0.01030  351 ARG B O   
5306 C CB  . ARG B 357 ? 0.36310 0.33890 0.29170 -0.05230 0.05580  -0.01040 351 ARG B CB  
5307 C CG  . ARG B 357 ? 0.40430 0.36990 0.32190 -0.05250 0.04170  0.00640  351 ARG B CG  
5308 C CD  . ARG B 357 ? 0.43980 0.40740 0.33470 -0.05370 0.03250  0.00980  351 ARG B CD  
5309 N NE  . ARG B 357 ? 0.43130 0.38780 0.31590 -0.05210 0.02050  0.02740  351 ARG B NE  
5310 C CZ  . ARG B 357 ? 0.42450 0.36780 0.31540 -0.04200 0.00950  0.03290  351 ARG B CZ  
5311 N NH1 . ARG B 357 ? 0.35410 0.29570 0.26060 -0.03390 0.00800  0.02340  351 ARG B NH1 
5312 N NH2 . ARG B 357 ? 0.43240 0.36290 0.31310 -0.03980 0.00070  0.04860  351 ARG B NH2 
5313 N N   . GLY B 358 ? 0.34610 0.34300 0.30910 -0.05920 0.07870  -0.00320 352 GLY B N   
5314 C CA  . GLY B 358 ? 0.34640 0.35240 0.31290 -0.06780 0.08170  0.00860  352 GLY B CA  
5315 C C   . GLY B 358 ? 0.54880 0.55670 0.48590 -0.07960 0.08130  0.01700  352 GLY B C   
5316 O O   . GLY B 358 ? 0.71470 0.72890 0.65000 -0.08960 0.08340  0.02850  352 GLY B O   
5317 N N   . ASP B 364 ? 0.98780 1.01990 0.83870 -0.09260 0.16590  -0.11170 358 ASP B N   
5318 C CA  . ASP B 364 ? 0.97890 1.01390 0.79610 -0.10520 0.14980  -0.10700 358 ASP B CA  
5319 C C   . ASP B 364 ? 0.95110 1.00430 0.73200 -0.12150 0.15890  -0.11040 358 ASP B C   
5320 O O   . ASP B 364 ? 0.96610 1.03290 0.74780 -0.12380 0.16850  -0.10240 358 ASP B O   
5321 C CB  . ASP B 364 ? 1.06140 1.09590 0.88440 -0.10200 0.12690  -0.08140 358 ASP B CB  
5322 C CG  . ASP B 364 ? 1.04020 1.05830 0.88790 -0.08960 0.11410  -0.07900 358 ASP B CG  
5323 O OD1 . ASP B 364 ? 1.06060 1.06900 0.91040 -0.08820 0.11690  -0.09510 358 ASP B OD1 
5324 O OD2 . ASP B 364 ? 1.04360 1.05760 0.90680 -0.08260 0.10170  -0.06130 358 ASP B OD2 
5325 N N   . ASP B 365 ? 0.91700 0.97190 0.66770 -0.13340 0.15440  -0.12100 359 ASP B N   
5326 C CA  . ASP B 365 ? 0.82310 0.89540 0.54400 -0.14740 0.15180  -0.11650 359 ASP B CA  
5327 C C   . ASP B 365 ? 0.81140 0.89670 0.52000 -0.15220 0.13800  -0.08870 359 ASP B C   
5328 O O   . ASP B 365 ? 0.77340 0.85270 0.48770 -0.14750 0.12030  -0.07410 359 ASP B O   
5329 C CB  . ASP B 365 ? 0.77320 0.84530 0.47250 -0.15790 0.14150  -0.12690 359 ASP B CB  
5330 C CG  . ASP B 365 ? 0.84000 0.92870 0.51070 -0.17250 0.14360  -0.12900 359 ASP B CG  
5331 O OD1 . ASP B 365 ? 0.83200 0.93710 0.48970 -0.17790 0.14030  -0.11150 359 ASP B OD1 
5332 O OD2 . ASP B 365 ? 0.79820 0.88280 0.45870 -0.17970 0.14880  -0.14790 359 ASP B OD2 
5333 N N   . PRO B 366 ? 0.79140 0.89160 0.48890 -0.15910 0.14320  -0.07860 360 PRO B N   
5334 C CA  . PRO B 366 ? 0.74440 0.85270 0.42980 -0.16430 0.12830  -0.04970 360 PRO B CA  
5335 C C   . PRO B 366 ? 0.70620 0.81660 0.37250 -0.16850 0.10490  -0.03700 360 PRO B C   
5336 O O   . PRO B 366 ? 0.63770 0.74590 0.30250 -0.16660 0.08980  -0.01220 360 PRO B O   
5337 C CB  . PRO B 366 ? 0.66320 0.78810 0.33490 -0.17370 0.13790  -0.04620 360 PRO B CB  
5338 C CG  . PRO B 366 ? 0.72370 0.84860 0.41030 -0.16890 0.16120  -0.07010 360 PRO B CG  
5339 C CD  . PRO B 366 ? 0.78490 0.89370 0.48130 -0.16180 0.16280  -0.09190 360 PRO B CD  
5340 N N   . ARG B 367 ? 0.72250 0.83660 0.37690 -0.17380 0.10120  -0.05260 361 ARG B N   
5341 C CA  . ARG B 367 ? 0.66550 0.78750 0.30630 -0.17780 0.07930  -0.04120 361 ARG B CA  
5342 C C   . ARG B 367 ? 0.67500 0.78590 0.33070 -0.16800 0.06750  -0.03990 361 ARG B C   
5343 O O   . ARG B 367 ? 0.65160 0.77160 0.30090 -0.16910 0.04860  -0.02850 361 ARG B O   
5344 C CB  . ARG B 367 ? 0.64790 0.78160 0.27040 -0.19040 0.08030  -0.05760 361 ARG B CB  
5345 C CG  . ARG B 367 ? 0.65660 0.80580 0.25810 -0.20200 0.08670  -0.05390 361 ARG B CG  
5346 C CD  . ARG B 367 ? 0.69110 0.84770 0.27550 -0.21490 0.09260  -0.07550 361 ARG B CD  
5347 N NE  . ARG B 367 ? 0.68970 0.82870 0.28680 -0.21070 0.11170  -0.10380 361 ARG B NE  
5348 C CZ  . ARG B 367 ? 0.74130 0.87920 0.32640 -0.22010 0.12330  -0.12650 361 ARG B CZ  
5349 N NH1 . ARG B 367 ? 0.76080 0.91650 0.31890 -0.23640 0.11790  -0.12620 361 ARG B NH1 
5350 N NH2 . ARG B 367 ? 0.77340 0.89100 0.37440 -0.21280 0.14060  -0.14950 361 ARG B NH2 
5351 N N   . LEU B 368 ? 0.67180 0.76440 0.35240 -0.15670 0.07690  -0.04970 362 LEU B N   
5352 C CA  . LEU B 368 ? 0.68640 0.76570 0.39410 -0.14230 0.06270  -0.04450 362 LEU B CA  
5353 C C   . LEU B 368 ? 0.70020 0.77280 0.42230 -0.13120 0.04980  -0.01720 362 LEU B C   
5354 O O   . LEU B 368 ? 0.71320 0.77470 0.45300 -0.12460 0.05750  -0.01260 362 LEU B O   
5355 C CB  . LEU B 368 ? 0.73260 0.79310 0.46930 -0.13210 0.07520  -0.06430 362 LEU B CB  
5356 C CG  . LEU B 368 ? 0.79810 0.84470 0.56410 -0.11730 0.06260  -0.05900 362 LEU B CG  
5357 C CD1 . LEU B 368 ? 0.68600 0.74090 0.44220 -0.12230 0.04840  -0.06150 362 LEU B CD1 
5358 C CD2 . LEU B 368 ? 0.80460 0.83280 0.60090 -0.10630 0.07550  -0.07320 362 LEU B CD2 
5359 N N   . ALA B 369 ? 0.68660 0.76620 0.40170 -0.12930 0.03030  0.00100  363 ALA B N   
5360 C CA  . ALA B 369 ? 0.63220 0.70080 0.35930 -0.11780 0.01800  0.02630  363 ALA B CA  
5361 C C   . ALA B 369 ? 0.63860 0.68720 0.39910 -0.10070 0.01420  0.02400  363 ALA B C   
5362 O O   . ALA B 369 ? 0.58680 0.63730 0.35690 -0.09620 0.00940  0.01400  363 ALA B O   
5363 C CB  . ALA B 369 ? 0.58480 0.66870 0.29380 -0.11970 -0.00040 0.04730  363 ALA B CB  
5364 N N   . ALA B 370 ? 0.61820 0.64850 0.39470 -0.09280 0.01610  0.03360  364 ALA B N   
5365 C CA  . ALA B 370 ? 0.59330 0.60450 0.39790 -0.07790 0.01190  0.03350  364 ALA B CA  
5366 C C   . ALA B 370 ? 0.63720 0.63760 0.44220 -0.06850 -0.00320 0.05580  364 ALA B C   
5367 O O   . ALA B 370 ? 0.55690 0.54000 0.36540 -0.06610 -0.00380 0.06850  364 ALA B O   
5368 C CB  . ALA B 370 ? 0.58980 0.58900 0.41250 -0.07670 0.02440  0.02720  364 ALA B CB  
5369 N N   . VAL B 371 ? 0.57650 0.58720 0.37860 -0.06320 -0.01520 0.06050  365 VAL B N   
5370 C CA  . VAL B 371 ? 0.56670 0.56950 0.37070 -0.05140 -0.02900 0.08150  365 VAL B CA  
5371 C C   . VAL B 371 ? 0.61180 0.59290 0.44070 -0.03620 -0.03030 0.07810  365 VAL B C   
5372 O O   . VAL B 371 ? 0.58250 0.56990 0.42510 -0.03010 -0.03170 0.06680  365 VAL B O   
5373 C CB  . VAL B 371 ? 0.54740 0.57560 0.34160 -0.05090 -0.04120 0.08890  365 VAL B CB  
5374 C CG1 . VAL B 371 ? 0.58210 0.60260 0.37960 -0.03630 -0.05440 0.11350  365 VAL B CG1 
5375 C CG2 . VAL B 371 ? 0.52720 0.57970 0.29350 -0.06930 -0.03920 0.08840  365 VAL B CG2 
5376 N N   . ALA B 372 ? 0.53860 0.49380 0.37170 -0.03170 -0.02950 0.08770  366 ALA B N   
5377 C CA  . ALA B 372 ? 0.53100 0.46380 0.38330 -0.01900 -0.03070 0.08480  366 ALA B CA  
5378 C C   . ALA B 372 ? 0.55230 0.48980 0.41230 -0.00390 -0.04070 0.08950  366 ALA B C   
5379 O O   . ALA B 372 ? 0.62820 0.56340 0.48150 0.00360  -0.04910 0.10710  366 ALA B O   
5380 C CB  . ALA B 372 ? 0.47110 0.37430 0.32060 -0.01900 -0.03040 0.09700  366 ALA B CB  
5381 N N   . ARG B 373 ? 0.53990 0.48580 0.41500 0.00080  -0.03940 0.07520  367 ARG B N   
5382 C CA  . ARG B 373 ? 0.56070 0.51660 0.44600 0.01450  -0.04730 0.07820  367 ARG B CA  
5383 C C   . ARG B 373 ? 0.51770 0.46490 0.42130 0.02090  -0.04320 0.06440  367 ARG B C   
5384 O O   . ARG B 373 ? 0.38130 0.32250 0.28920 0.01270  -0.03520 0.05160  367 ARG B O   
5385 C CB  . ARG B 373 ? 0.46900 0.46000 0.34960 0.00850  -0.05230 0.07640  367 ARG B CB  
5386 C CG  . ARG B 373 ? 0.58910 0.59580 0.45170 0.00380  -0.05960 0.09260  367 ARG B CG  
5387 C CD  . ARG B 373 ? 0.64230 0.66360 0.51170 0.01850  -0.07150 0.10900  367 ARG B CD  
5388 N NE  . ARG B 373 ? 0.68290 0.72390 0.53430 0.01230  -0.07980 0.12630  367 ARG B NE  
5389 C CZ  . ARG B 373 ? 0.70960 0.73400 0.54720 0.01190  -0.08100 0.14300  367 ARG B CZ  
5390 N NH1 . ARG B 373 ? 0.81170 0.79840 0.65210 0.01730  -0.07490 0.14470  367 ARG B NH1 
5391 N NH2 . ARG B 373 ? 0.62210 0.66860 0.44130 0.00380  -0.08870 0.15870  367 ARG B NH2 
5392 O OXT . ARG B 373 ? 0.44100 0.39050 0.35520 0.03420  -0.04760 0.06660  367 ARG B OXT 
5409 N N   . ASN G .   ? 0.43600 0.39280 0.37210 -0.15330 0.05160  0.13990  505 ASN A N   
5410 C CA  . ASN G .   ? 0.41350 0.38480 0.46760 -0.14710 0.06890  0.15190  505 ASN A CA  
5411 C C   . ASN G .   ? 0.39540 0.36780 0.44370 -0.15000 0.07850  0.13080  505 ASN A C   
5412 O O   . ASN G .   ? 0.37640 0.35200 0.36740 -0.16150 0.06490  0.08680  505 ASN A O   
5413 C CB  . ASN G .   ? 0.37620 0.37000 0.55580 -0.15610 0.04800  0.12930  505 ASN A CB  
5414 C CG  . ASN G .   ? 0.39160 0.39040 0.61090 -0.15120 0.04670  0.16690  505 ASN A CG  
5415 O OD1 . ASN G .   ? 0.43350 0.41840 0.58900 -0.14070 0.06020  0.21220  505 ASN A OD1 
5416 N ND2 . ASN G .   ? 0.36860 0.38130 0.68370 -0.15550 0.03110  0.14770  505 ASN A ND2 
5417 O OXT . ASN G .   ? 0.40240 0.37440 0.50520 -0.13760 0.09850  0.15920  505 ASN A OXT 
5456 N N   . ASN S .   ? 0.28550 0.55390 0.62270 -0.10030 -0.04340 -0.19800 408 ASN B N   
5457 C CA  . ASN S .   ? 0.28720 0.53250 0.68780 -0.09830 -0.05990 -0.18660 408 ASN B CA  
5458 C C   . ASN S .   ? 0.26690 0.50720 0.63480 -0.10100 -0.06640 -0.13900 408 ASN B C   
5459 O O   . ASN S .   ? 0.27370 0.50920 0.67110 -0.10670 -0.07980 -0.14130 408 ASN B O   
5460 C CB  . ASN S .   ? 0.28820 0.51570 0.78610 -0.08210 -0.05750 -0.17220 408 ASN B CB  
5461 C CG  . ASN S .   ? 0.31920 0.54650 0.86090 -0.07470 -0.05910 -0.22880 408 ASN B CG  
5462 O OD1 . ASN S .   ? 0.34130 0.58260 0.85760 -0.08280 -0.06590 -0.28090 408 ASN B OD1 
5463 N ND2 . ASN S .   ? 0.32860 0.54180 0.92880 -0.05210 -0.05400 -0.22030 408 ASN B ND2 
5464 O OXT . ASN S .   ? 0.24580 0.49190 0.56140 -0.09580 -0.06050 -0.10180 408 ASN B OXT 
# 
