data_9G66
# 
_entry.id   9G66 
# 
_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   9G66         pdb_00009g66 10.2210/pdb9g66/pdb 
WWPDB D_1292138750 ?            ?                   
# 
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                        9G66 
_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 . 8osw unspecified 
PDB . 8clz unspecified 
PDB . 8cly unspecified 
PDB . 8ori unspecified 
PDB . 8col 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' 39570.867 2   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL              62.068    22  ? ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'     106.120   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                    92.094    1   ? ? ? ? 
5 non-polymer syn ASPARAGINE                  132.118   2   ? ? ? ? 
6 non-polymer syn 'CADMIUM ION'               112.411   2   ? ? ? ? 
7 water       nat water                       18.015    635 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GIDPFTMTPSEDFVVTDRGGIVENSHRVHAAVVDAKGRLLYALGNPTRMTLARSAAKPAQALAILETEGVAGYGFDDADI
ALMCASHSSEDRHIARTRAMLSKIKAEEADLRCGGHPSLSEMVNRSWIKQDFIPTAVCSNCSGKHVGMLAGARAIGAGTD
GYHLPDHPMQGRVKRTVAELCDLDAGDVEWGTDGCNLPTPAFPLDRLGRIYAKLASAADGSDAGEGQSTR(CSO)AALAH
IFRAMARHPEMVAGEGRYCTMLMRAFDGALVGKLGADASYAIGVRASDATRQLGTDGALGISVKIEDGNLEMLYAVVTEL
LERLGIGSPDVRSQLASFHHPQRVNTMGVTTGGVSFPFKLRGSKSNVDDPRLAAVAR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GIDPFTMTPSEDFVVTDRGGIVENSHRVHAAVVDAKGRLLYALGNPTRMTLARSAAKPAQALAILETEGVAGYGFDDADI
ALMCASHSSEDRHIARTRAMLSKIKAEEADLRCGGHPSLSEMVNRSWIKQDFIPTAVCSNCSGKHVGMLAGARAIGAGTD
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 'DI(HYDROXYETHYL)ETHER' PEG 
4 GLYCEROL                GOL 
5 ASPARAGINE              ASN 
6 'CADMIUM ION'           CD  
7 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 LYS 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 CSO 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 
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE       ?                               'C3 H7 N O3 S'   137.158 
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  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
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 LYS 144 138 138 LYS LYS 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 CSO 231 225 225 CSO CSO 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  -4  ILE ILE 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 LYS 144 138 138 LYS LYS 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 CSO 231 225 225 CSO CSO 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 359 353 353 SER SER 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 363 357 357 VAL VAL 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   401 664 EDO EDO A . 
D  2 EDO 1   402 665 EDO EDO A . 
E  2 EDO 1   403 666 EDO EDO A . 
F  3 PEG 1   404 667 PEG PEG A . 
G  2 EDO 1   405 668 EDO EDO A . 
H  2 EDO 1   406 669 EDO EDO A . 
I  2 EDO 1   407 670 EDO EDO A . 
J  2 EDO 1   408 671 EDO EDO A . 
K  4 GOL 1   409 672 GOL GOL A . 
L  2 EDO 1   410 673 EDO EDO A . 
M  2 EDO 1   411 674 EDO EDO A . 
N  2 EDO 1   412 675 EDO EDO A . 
O  5 ASN 1   413 676 ASN ASN A . 
P  2 EDO 1   414 701 EDO EDO A . 
Q  2 EDO 1   415 702 EDO EDO A . 
R  2 EDO 1   416 703 EDO EDO A . 
S  2 EDO 1   417 710 EDO EDO A . 
T  6 CD  1   418 1   CD  CD  A . 
U  2 EDO 1   401 368 EDO EDO B . 
V  2 EDO 1   402 369 EDO EDO B . 
W  2 EDO 1   403 370 EDO EDO B . 
X  2 EDO 1   404 371 EDO EDO B . 
Y  2 EDO 1   405 372 EDO EDO B . 
Z  2 EDO 1   406 373 EDO EDO B . 
AA 3 PEG 1   407 374 PEG PEG B . 
BA 2 EDO 1   408 375 EDO EDO B . 
CA 5 ASN 1   409 376 ASN ASN B . 
DA 6 CD  1   410 377 CD  CD  B . 
EA 2 EDO 1   411 709 EDO EDO B . 
FA 7 HOH 1   501 587 HOH HOH A . 
FA 7 HOH 2   502 548 HOH HOH A . 
FA 7 HOH 3   503 606 HOH HOH A . 
FA 7 HOH 4   504 549 HOH HOH A . 
FA 7 HOH 5   505 654 HOH HOH A . 
FA 7 HOH 6   506 594 HOH HOH A . 
FA 7 HOH 7   507 478 HOH HOH A . 
FA 7 HOH 8   508 533 HOH HOH A . 
FA 7 HOH 9   509 638 HOH HOH A . 
FA 7 HOH 10  510 474 HOH HOH A . 
FA 7 HOH 11  511 611 HOH HOH A . 
FA 7 HOH 12  512 433 HOH HOH A . 
FA 7 HOH 13  513 432 HOH HOH A . 
FA 7 HOH 14  514 536 HOH HOH A . 
FA 7 HOH 15  515 427 HOH HOH A . 
FA 7 HOH 16  516 517 HOH HOH A . 
FA 7 HOH 17  517 468 HOH HOH A . 
FA 7 HOH 18  518 499 HOH HOH A . 
FA 7 HOH 19  519 614 HOH HOH A . 
FA 7 HOH 20  520 531 HOH HOH A . 
FA 7 HOH 21  521 444 HOH HOH A . 
FA 7 HOH 22  522 446 HOH HOH A . 
FA 7 HOH 23  523 424 HOH HOH A . 
FA 7 HOH 24  524 640 HOH HOH A . 
FA 7 HOH 25  525 376 HOH HOH A . 
FA 7 HOH 26  526 482 HOH HOH A . 
FA 7 HOH 27  527 448 HOH HOH A . 
FA 7 HOH 28  528 584 HOH HOH A . 
FA 7 HOH 29  529 382 HOH HOH A . 
FA 7 HOH 30  530 373 HOH HOH A . 
FA 7 HOH 31  531 381 HOH HOH A . 
FA 7 HOH 32  532 513 HOH HOH A . 
FA 7 HOH 33  533 503 HOH HOH A . 
FA 7 HOH 34  534 421 HOH HOH A . 
FA 7 HOH 35  535 447 HOH HOH A . 
FA 7 HOH 36  536 477 HOH HOH A . 
FA 7 HOH 37  537 503 HOH HOH A . 
FA 7 HOH 38  538 408 HOH HOH A . 
FA 7 HOH 39  539 526 HOH HOH A . 
FA 7 HOH 40  540 569 HOH HOH A . 
FA 7 HOH 41  541 409 HOH HOH A . 
FA 7 HOH 42  542 524 HOH HOH A . 
FA 7 HOH 43  543 406 HOH HOH A . 
FA 7 HOH 44  544 440 HOH HOH A . 
FA 7 HOH 45  545 371 HOH HOH A . 
FA 7 HOH 46  546 423 HOH HOH A . 
FA 7 HOH 47  547 509 HOH HOH A . 
FA 7 HOH 48  548 443 HOH HOH A . 
FA 7 HOH 49  549 369 HOH HOH A . 
FA 7 HOH 50  550 451 HOH HOH A . 
FA 7 HOH 51  551 601 HOH HOH A . 
FA 7 HOH 52  552 395 HOH HOH A . 
FA 7 HOH 53  553 384 HOH HOH A . 
FA 7 HOH 54  554 617 HOH HOH A . 
FA 7 HOH 55  555 535 HOH HOH A . 
FA 7 HOH 56  556 491 HOH HOH A . 
FA 7 HOH 57  557 643 HOH HOH A . 
FA 7 HOH 58  558 428 HOH HOH A . 
FA 7 HOH 59  559 13  HOH HOH A . 
FA 7 HOH 60  560 553 HOH HOH A . 
FA 7 HOH 61  561 460 HOH HOH A . 
FA 7 HOH 62  562 497 HOH HOH A . 
FA 7 HOH 63  563 566 HOH HOH A . 
FA 7 HOH 64  564 415 HOH HOH A . 
FA 7 HOH 65  565 429 HOH HOH A . 
FA 7 HOH 66  566 413 HOH HOH A . 
FA 7 HOH 67  567 445 HOH HOH A . 
FA 7 HOH 68  568 639 HOH HOH A . 
FA 7 HOH 69  569 484 HOH HOH A . 
FA 7 HOH 70  570 510 HOH HOH A . 
FA 7 HOH 71  571 591 HOH HOH A . 
FA 7 HOH 72  572 516 HOH HOH A . 
FA 7 HOH 73  573 368 HOH HOH A . 
FA 7 HOH 74  574 485 HOH HOH A . 
FA 7 HOH 75  575 482 HOH HOH A . 
FA 7 HOH 76  576 436 HOH HOH A . 
FA 7 HOH 77  577 642 HOH HOH A . 
FA 7 HOH 78  578 452 HOH HOH A . 
FA 7 HOH 79  579 403 HOH HOH A . 
FA 7 HOH 80  580 412 HOH HOH A . 
FA 7 HOH 81  581 470 HOH HOH A . 
FA 7 HOH 82  582 457 HOH HOH A . 
FA 7 HOH 83  583 577 HOH HOH A . 
FA 7 HOH 84  584 624 HOH HOH A . 
FA 7 HOH 85  585 466 HOH HOH A . 
FA 7 HOH 86  586 456 HOH HOH A . 
FA 7 HOH 87  587 590 HOH HOH A . 
FA 7 HOH 88  588 411 HOH HOH A . 
FA 7 HOH 89  589 390 HOH HOH A . 
FA 7 HOH 90  590 556 HOH HOH A . 
FA 7 HOH 91  591 438 HOH HOH A . 
FA 7 HOH 92  592 506 HOH HOH A . 
FA 7 HOH 93  593 488 HOH HOH A . 
FA 7 HOH 94  594 529 HOH HOH A . 
FA 7 HOH 95  595 450 HOH HOH A . 
FA 7 HOH 96  596 461 HOH HOH A . 
FA 7 HOH 97  597 465 HOH HOH A . 
FA 7 HOH 98  598 655 HOH HOH A . 
FA 7 HOH 99  599 607 HOH HOH A . 
FA 7 HOH 100 600 374 HOH HOH A . 
FA 7 HOH 101 601 647 HOH HOH A . 
FA 7 HOH 102 602 397 HOH HOH A . 
FA 7 HOH 103 603 575 HOH HOH A . 
FA 7 HOH 104 604 494 HOH HOH A . 
FA 7 HOH 105 605 627 HOH HOH A . 
FA 7 HOH 106 606 543 HOH HOH A . 
FA 7 HOH 107 607 378 HOH HOH A . 
FA 7 HOH 108 608 394 HOH HOH A . 
FA 7 HOH 109 609 490 HOH HOH A . 
FA 7 HOH 110 610 479 HOH HOH A . 
FA 7 HOH 111 611 375 HOH HOH A . 
FA 7 HOH 112 612 370 HOH HOH A . 
FA 7 HOH 113 613 380 HOH HOH A . 
FA 7 HOH 114 614 372 HOH HOH A . 
FA 7 HOH 115 615 393 HOH HOH A . 
FA 7 HOH 116 616 578 HOH HOH A . 
FA 7 HOH 117 617 379 HOH HOH A . 
FA 7 HOH 118 618 402 HOH HOH A . 
FA 7 HOH 119 619 453 HOH HOH A . 
FA 7 HOH 120 620 454 HOH HOH A . 
FA 7 HOH 121 621 559 HOH HOH A . 
FA 7 HOH 122 622 405 HOH HOH A . 
FA 7 HOH 123 623 657 HOH HOH A . 
FA 7 HOH 124 624 419 HOH HOH A . 
FA 7 HOH 125 625 659 HOH HOH A . 
FA 7 HOH 126 626 476 HOH HOH A . 
FA 7 HOH 127 627 579 HOH HOH A . 
FA 7 HOH 128 628 609 HOH HOH A . 
FA 7 HOH 129 629 521 HOH HOH A . 
FA 7 HOH 130 630 552 HOH HOH A . 
FA 7 HOH 131 631 661 HOH HOH A . 
FA 7 HOH 132 632 416 HOH HOH A . 
FA 7 HOH 133 633 558 HOH HOH A . 
FA 7 HOH 134 634 628 HOH HOH A . 
FA 7 HOH 135 635 515 HOH HOH A . 
FA 7 HOH 136 636 16  HOH HOH A . 
FA 7 HOH 137 637 504 HOH HOH A . 
FA 7 HOH 138 638 502 HOH HOH A . 
FA 7 HOH 139 639 520 HOH HOH A . 
FA 7 HOH 140 640 430 HOH HOH A . 
FA 7 HOH 141 641 418 HOH HOH A . 
FA 7 HOH 142 642 492 HOH HOH A . 
FA 7 HOH 143 643 463 HOH HOH A . 
FA 7 HOH 144 644 401 HOH HOH A . 
FA 7 HOH 145 645 459 HOH HOH A . 
FA 7 HOH 146 646 396 HOH HOH A . 
FA 7 HOH 147 647 428 HOH HOH A . 
FA 7 HOH 148 648 537 HOH HOH A . 
FA 7 HOH 149 649 495 HOH HOH A . 
FA 7 HOH 150 650 422 HOH HOH A . 
FA 7 HOH 151 651 572 HOH HOH A . 
FA 7 HOH 152 652 464 HOH HOH A . 
FA 7 HOH 153 653 392 HOH HOH A . 
FA 7 HOH 154 654 508 HOH HOH A . 
FA 7 HOH 155 655 496 HOH HOH A . 
FA 7 HOH 156 656 449 HOH HOH A . 
FA 7 HOH 157 657 632 HOH HOH A . 
FA 7 HOH 158 658 383 HOH HOH A . 
FA 7 HOH 159 659 588 HOH HOH A . 
FA 7 HOH 160 660 441 HOH HOH A . 
FA 7 HOH 161 661 467 HOH HOH A . 
FA 7 HOH 162 662 489 HOH HOH A . 
FA 7 HOH 163 663 414 HOH HOH A . 
FA 7 HOH 164 664 391 HOH HOH A . 
FA 7 HOH 165 665 473 HOH HOH A . 
FA 7 HOH 166 666 598 HOH HOH A . 
FA 7 HOH 167 667 648 HOH HOH A . 
FA 7 HOH 168 668 407 HOH HOH A . 
FA 7 HOH 169 669 564 HOH HOH A . 
FA 7 HOH 170 670 530 HOH HOH A . 
FA 7 HOH 171 671 420 HOH HOH A . 
FA 7 HOH 172 672 399 HOH HOH A . 
FA 7 HOH 173 673 507 HOH HOH A . 
FA 7 HOH 174 674 648 HOH HOH A . 
FA 7 HOH 175 675 620 HOH HOH A . 
FA 7 HOH 176 676 528 HOH HOH A . 
FA 7 HOH 177 677 377 HOH HOH A . 
FA 7 HOH 178 678 417 HOH HOH A . 
FA 7 HOH 179 679 385 HOH HOH A . 
FA 7 HOH 180 680 613 HOH HOH A . 
FA 7 HOH 181 681 600 HOH HOH A . 
FA 7 HOH 182 682 400 HOH HOH A . 
FA 7 HOH 183 683 637 HOH HOH A . 
FA 7 HOH 184 684 567 HOH HOH A . 
FA 7 HOH 185 685 573 HOH HOH A . 
FA 7 HOH 186 686 636 HOH HOH A . 
FA 7 HOH 187 687 500 HOH HOH A . 
FA 7 HOH 188 688 493 HOH HOH A . 
FA 7 HOH 189 689 410 HOH HOH A . 
FA 7 HOH 190 690 649 HOH HOH A . 
FA 7 HOH 191 691 615 HOH HOH A . 
FA 7 HOH 192 692 523 HOH HOH A . 
FA 7 HOH 193 693 595 HOH HOH A . 
FA 7 HOH 194 694 398 HOH HOH A . 
FA 7 HOH 195 695 483 HOH HOH A . 
FA 7 HOH 196 696 486 HOH HOH A . 
FA 7 HOH 197 697 604 HOH HOH A . 
FA 7 HOH 198 698 387 HOH HOH A . 
FA 7 HOH 199 699 455 HOH HOH A . 
FA 7 HOH 200 700 540 HOH HOH A . 
FA 7 HOH 201 701 539 HOH HOH A . 
FA 7 HOH 202 702 404 HOH HOH A . 
FA 7 HOH 203 703 17  HOH HOH A . 
FA 7 HOH 204 704 8   HOH HOH A . 
FA 7 HOH 205 705 519 HOH HOH A . 
FA 7 HOH 206 706 481 HOH HOH A . 
FA 7 HOH 207 707 389 HOH HOH A . 
FA 7 HOH 208 708 574 HOH HOH A . 
FA 7 HOH 209 709 635 HOH HOH A . 
FA 7 HOH 210 710 514 HOH HOH A . 
FA 7 HOH 211 711 439 HOH HOH A . 
FA 7 HOH 212 712 653 HOH HOH A . 
FA 7 HOH 213 713 583 HOH HOH A . 
FA 7 HOH 214 714 631 HOH HOH A . 
FA 7 HOH 215 715 518 HOH HOH A . 
FA 7 HOH 216 716 442 HOH HOH A . 
FA 7 HOH 217 717 386 HOH HOH A . 
FA 7 HOH 218 718 527 HOH HOH A . 
FA 7 HOH 219 719 586 HOH HOH A . 
FA 7 HOH 220 720 557 HOH HOH A . 
FA 7 HOH 221 721 565 HOH HOH A . 
FA 7 HOH 222 722 554 HOH HOH A . 
FA 7 HOH 223 723 498 HOH HOH A . 
FA 7 HOH 224 724 608 HOH HOH A . 
FA 7 HOH 225 725 388 HOH HOH A . 
FA 7 HOH 226 726 471 HOH HOH A . 
FA 7 HOH 227 727 511 HOH HOH A . 
FA 7 HOH 228 728 458 HOH HOH A . 
FA 7 HOH 229 729 599 HOH HOH A . 
FA 7 HOH 230 730 623 HOH HOH A . 
FA 7 HOH 231 731 541 HOH HOH A . 
FA 7 HOH 232 732 562 HOH HOH A . 
FA 7 HOH 233 733 544 HOH HOH A . 
FA 7 HOH 234 734 462 HOH HOH A . 
FA 7 HOH 235 735 596 HOH HOH A . 
FA 7 HOH 236 736 644 HOH HOH A . 
FA 7 HOH 237 737 550 HOH HOH A . 
FA 7 HOH 238 738 576 HOH HOH A . 
FA 7 HOH 239 739 603 HOH HOH A . 
FA 7 HOH 240 740 501 HOH HOH A . 
FA 7 HOH 241 741 12  HOH HOH A . 
FA 7 HOH 242 742 534 HOH HOH A . 
FA 7 HOH 243 743 472 HOH HOH A . 
FA 7 HOH 244 744 538 HOH HOH A . 
FA 7 HOH 245 745 6   HOH HOH A . 
FA 7 HOH 246 746 660 HOH HOH A . 
FA 7 HOH 247 747 645 HOH HOH A . 
FA 7 HOH 248 748 633 HOH HOH A . 
FA 7 HOH 249 749 426 HOH HOH A . 
FA 7 HOH 250 750 658 HOH HOH A . 
FA 7 HOH 251 751 652 HOH HOH A . 
FA 7 HOH 252 752 469 HOH HOH A . 
FA 7 HOH 253 753 589 HOH HOH A . 
FA 7 HOH 254 754 7   HOH HOH A . 
FA 7 HOH 255 755 612 HOH HOH A . 
FA 7 HOH 256 756 622 HOH HOH A . 
FA 7 HOH 257 757 651 HOH HOH A . 
FA 7 HOH 258 758 592 HOH HOH A . 
FA 7 HOH 259 759 650 HOH HOH A . 
FA 7 HOH 260 760 585 HOH HOH A . 
FA 7 HOH 261 761 568 HOH HOH A . 
FA 7 HOH 262 762 431 HOH HOH A . 
FA 7 HOH 263 763 602 HOH HOH A . 
FA 7 HOH 264 764 551 HOH HOH A . 
FA 7 HOH 265 765 4   HOH HOH A . 
FA 7 HOH 266 766 581 HOH HOH A . 
FA 7 HOH 267 767 621 HOH HOH A . 
FA 7 HOH 268 768 434 HOH HOH A . 
FA 7 HOH 269 769 561 HOH HOH A . 
FA 7 HOH 270 770 547 HOH HOH A . 
FA 7 HOH 271 771 3   HOH HOH A . 
FA 7 HOH 272 772 545 HOH HOH A . 
FA 7 HOH 273 773 487 HOH HOH A . 
FA 7 HOH 274 774 563 HOH HOH A . 
FA 7 HOH 275 775 532 HOH HOH A . 
FA 7 HOH 276 776 475 HOH HOH A . 
FA 7 HOH 277 777 634 HOH HOH A . 
FA 7 HOH 278 778 593 HOH HOH A . 
FA 7 HOH 279 779 505 HOH HOH A . 
FA 7 HOH 280 780 605 HOH HOH A . 
FA 7 HOH 281 781 571 HOH HOH A . 
FA 7 HOH 282 782 546 HOH HOH A . 
FA 7 HOH 283 783 597 HOH HOH A . 
FA 7 HOH 284 784 525 HOH HOH A . 
FA 7 HOH 285 785 616 HOH HOH A . 
FA 7 HOH 286 786 626 HOH HOH A . 
FA 7 HOH 287 787 522 HOH HOH A . 
FA 7 HOH 288 788 662 HOH HOH A . 
FA 7 HOH 289 789 555 HOH HOH A . 
FA 7 HOH 290 790 435 HOH HOH A . 
FA 7 HOH 291 791 610 HOH HOH A . 
FA 7 HOH 292 792 480 HOH HOH A . 
FA 7 HOH 293 793 560 HOH HOH A . 
FA 7 HOH 294 794 619 HOH HOH A . 
FA 7 HOH 295 795 425 HOH HOH A . 
FA 7 HOH 296 796 542 HOH HOH A . 
FA 7 HOH 297 797 570 HOH HOH A . 
FA 7 HOH 298 798 580 HOH HOH A . 
FA 7 HOH 299 799 646 HOH HOH A . 
FA 7 HOH 300 800 15  HOH HOH A . 
FA 7 HOH 301 801 582 HOH HOH A . 
FA 7 HOH 302 802 641 HOH HOH A . 
FA 7 HOH 303 803 656 HOH HOH A . 
FA 7 HOH 304 804 14  HOH HOH A . 
FA 7 HOH 305 805 573 HOH HOH A . 
FA 7 HOH 306 806 512 HOH HOH A . 
FA 7 HOH 307 807 629 HOH HOH A . 
FA 7 HOH 308 808 618 HOH HOH A . 
GA 7 HOH 1   501 619 HOH HOH B . 
GA 7 HOH 2   502 610 HOH HOH B . 
GA 7 HOH 3   503 653 HOH HOH B . 
GA 7 HOH 4   504 616 HOH HOH B . 
GA 7 HOH 5   505 515 HOH HOH B . 
GA 7 HOH 6   506 621 HOH HOH B . 
GA 7 HOH 7   507 663 HOH HOH B . 
GA 7 HOH 8   508 554 HOH HOH B . 
GA 7 HOH 9   509 651 HOH HOH B . 
GA 7 HOH 10  510 560 HOH HOH B . 
GA 7 HOH 11  511 412 HOH HOH B . 
GA 7 HOH 12  512 431 HOH HOH B . 
GA 7 HOH 13  513 400 HOH HOH B . 
GA 7 HOH 14  514 408 HOH HOH B . 
GA 7 HOH 15  515 524 HOH HOH B . 
GA 7 HOH 16  516 459 HOH HOH B . 
GA 7 HOH 17  517 631 HOH HOH B . 
GA 7 HOH 18  518 632 HOH HOH B . 
GA 7 HOH 19  519 701 HOH HOH B . 
GA 7 HOH 20  520 521 HOH HOH B . 
GA 7 HOH 21  521 437 HOH HOH B . 
GA 7 HOH 22  522 588 HOH HOH B . 
GA 7 HOH 23  523 424 HOH HOH B . 
GA 7 HOH 24  524 383 HOH HOH B . 
GA 7 HOH 25  525 626 HOH HOH B . 
GA 7 HOH 26  526 538 HOH HOH B . 
GA 7 HOH 27  527 670 HOH HOH B . 
GA 7 HOH 28  528 700 HOH HOH B . 
GA 7 HOH 29  529 504 HOH HOH B . 
GA 7 HOH 30  530 615 HOH HOH B . 
GA 7 HOH 31  531 489 HOH HOH B . 
GA 7 HOH 32  532 552 HOH HOH B . 
GA 7 HOH 33  533 571 HOH HOH B . 
GA 7 HOH 34  534 622 HOH HOH B . 
GA 7 HOH 35  535 671 HOH HOH B . 
GA 7 HOH 36  536 448 HOH HOH B . 
GA 7 HOH 37  537 501 HOH HOH B . 
GA 7 HOH 38  538 404 HOH HOH B . 
GA 7 HOH 39  539 397 HOH HOH B . 
GA 7 HOH 40  540 454 HOH HOH B . 
GA 7 HOH 41  541 387 HOH HOH B . 
GA 7 HOH 42  542 535 HOH HOH B . 
GA 7 HOH 43  543 476 HOH HOH B . 
GA 7 HOH 44  544 613 HOH HOH B . 
GA 7 HOH 45  545 458 HOH HOH B . 
GA 7 HOH 46  546 443 HOH HOH B . 
GA 7 HOH 47  547 683 HOH HOH B . 
GA 7 HOH 48  548 593 HOH HOH B . 
GA 7 HOH 49  549 594 HOH HOH B . 
GA 7 HOH 50  550 436 HOH HOH B . 
GA 7 HOH 51  551 487 HOH HOH B . 
GA 7 HOH 52  552 542 HOH HOH B . 
GA 7 HOH 53  553 675 HOH HOH B . 
GA 7 HOH 54  554 695 HOH HOH B . 
GA 7 HOH 55  555 399 HOH HOH B . 
GA 7 HOH 56  556 493 HOH HOH B . 
GA 7 HOH 57  557 492 HOH HOH B . 
GA 7 HOH 58  558 579 HOH HOH B . 
GA 7 HOH 59  559 390 HOH HOH B . 
GA 7 HOH 60  560 457 HOH HOH B . 
GA 7 HOH 61  561 419 HOH HOH B . 
GA 7 HOH 62  562 471 HOH HOH B . 
GA 7 HOH 63  563 550 HOH HOH B . 
GA 7 HOH 64  564 565 HOH HOH B . 
GA 7 HOH 65  565 378 HOH HOH B . 
GA 7 HOH 66  566 402 HOH HOH B . 
GA 7 HOH 67  567 568 HOH HOH B . 
GA 7 HOH 68  568 475 HOH HOH B . 
GA 7 HOH 69  569 583 HOH HOH B . 
GA 7 HOH 70  570 543 HOH HOH B . 
GA 7 HOH 71  571 541 HOH HOH B . 
GA 7 HOH 72  572 381 HOH HOH B . 
GA 7 HOH 73  573 418 HOH HOH B . 
GA 7 HOH 74  574 536 HOH HOH B . 
GA 7 HOH 75  575 433 HOH HOH B . 
GA 7 HOH 76  576 665 HOH HOH B . 
GA 7 HOH 77  577 379 HOH HOH B . 
GA 7 HOH 78  578 446 HOH HOH B . 
GA 7 HOH 79  579 527 HOH HOH B . 
GA 7 HOH 80  580 618 HOH HOH B . 
GA 7 HOH 81  581 401 HOH HOH B . 
GA 7 HOH 82  582 411 HOH HOH B . 
GA 7 HOH 83  583 625 HOH HOH B . 
GA 7 HOH 84  584 510 HOH HOH B . 
GA 7 HOH 85  585 380 HOH HOH B . 
GA 7 HOH 86  586 393 HOH HOH B . 
GA 7 HOH 87  587 517 HOH HOH B . 
GA 7 HOH 88  588 484 HOH HOH B . 
GA 7 HOH 89  589 647 HOH HOH B . 
GA 7 HOH 90  590 455 HOH HOH B . 
GA 7 HOH 91  591 435 HOH HOH B . 
GA 7 HOH 92  592 575 HOH HOH B . 
GA 7 HOH 93  593 601 HOH HOH B . 
GA 7 HOH 94  594 441 HOH HOH B . 
GA 7 HOH 95  595 617 HOH HOH B . 
GA 7 HOH 96  596 440 HOH HOH B . 
GA 7 HOH 97  597 429 HOH HOH B . 
GA 7 HOH 98  598 415 HOH HOH B . 
GA 7 HOH 99  599 519 HOH HOH B . 
GA 7 HOH 100 600 434 HOH HOH B . 
GA 7 HOH 101 601 447 HOH HOH B . 
GA 7 HOH 102 602 545 HOH HOH B . 
GA 7 HOH 103 603 386 HOH HOH B . 
GA 7 HOH 104 604 417 HOH HOH B . 
GA 7 HOH 105 605 453 HOH HOH B . 
GA 7 HOH 106 606 385 HOH HOH B . 
GA 7 HOH 107 607 620 HOH HOH B . 
GA 7 HOH 108 608 505 HOH HOH B . 
GA 7 HOH 109 609 444 HOH HOH B . 
GA 7 HOH 110 610 439 HOH HOH B . 
GA 7 HOH 111 611 405 HOH HOH B . 
GA 7 HOH 112 612 640 HOH HOH B . 
GA 7 HOH 113 613 423 HOH HOH B . 
GA 7 HOH 114 614 465 HOH HOH B . 
GA 7 HOH 115 615 432 HOH HOH B . 
GA 7 HOH 116 616 566 HOH HOH B . 
GA 7 HOH 117 617 496 HOH HOH B . 
GA 7 HOH 118 618 394 HOH HOH B . 
GA 7 HOH 119 619 19  HOH HOH B . 
GA 7 HOH 120 620 430 HOH HOH B . 
GA 7 HOH 121 621 461 HOH HOH B . 
GA 7 HOH 122 622 513 HOH HOH B . 
GA 7 HOH 123 623 410 HOH HOH B . 
GA 7 HOH 124 624 414 HOH HOH B . 
GA 7 HOH 125 625 534 HOH HOH B . 
GA 7 HOH 126 626 584 HOH HOH B . 
GA 7 HOH 127 627 642 HOH HOH B . 
GA 7 HOH 128 628 472 HOH HOH B . 
GA 7 HOH 129 629 452 HOH HOH B . 
GA 7 HOH 130 630 474 HOH HOH B . 
GA 7 HOH 131 631 650 HOH HOH B . 
GA 7 HOH 132 632 10  HOH HOH B . 
GA 7 HOH 133 633 481 HOH HOH B . 
GA 7 HOH 134 634 468 HOH HOH B . 
GA 7 HOH 135 635 567 HOH HOH B . 
GA 7 HOH 136 636 687 HOH HOH B . 
GA 7 HOH 137 637 676 HOH HOH B . 
GA 7 HOH 138 638 477 HOH HOH B . 
GA 7 HOH 139 639 416 HOH HOH B . 
GA 7 HOH 140 640 480 HOH HOH B . 
GA 7 HOH 141 641 388 HOH HOH B . 
GA 7 HOH 142 642 391 HOH HOH B . 
GA 7 HOH 143 643 704 HOH HOH B . 
GA 7 HOH 144 644 664 HOH HOH B . 
GA 7 HOH 145 645 646 HOH HOH B . 
GA 7 HOH 146 646 526 HOH HOH B . 
GA 7 HOH 147 647 403 HOH HOH B . 
GA 7 HOH 148 648 520 HOH HOH B . 
GA 7 HOH 149 649 462 HOH HOH B . 
GA 7 HOH 150 650 406 HOH HOH B . 
GA 7 HOH 151 651 382 HOH HOH B . 
GA 7 HOH 152 652 680 HOH HOH B . 
GA 7 HOH 153 653 488 HOH HOH B . 
GA 7 HOH 154 654 495 HOH HOH B . 
GA 7 HOH 155 655 508 HOH HOH B . 
GA 7 HOH 156 656 528 HOH HOH B . 
GA 7 HOH 157 657 686 HOH HOH B . 
GA 7 HOH 158 658 509 HOH HOH B . 
GA 7 HOH 159 659 598 HOH HOH B . 
GA 7 HOH 160 660 548 HOH HOH B . 
GA 7 HOH 161 661 689 HOH HOH B . 
GA 7 HOH 162 662 395 HOH HOH B . 
GA 7 HOH 163 663 466 HOH HOH B . 
GA 7 HOH 164 664 673 HOH HOH B . 
GA 7 HOH 165 665 469 HOH HOH B . 
GA 7 HOH 166 666 641 HOH HOH B . 
GA 7 HOH 167 667 557 HOH HOH B . 
GA 7 HOH 168 668 392 HOH HOH B . 
GA 7 HOH 169 669 421 HOH HOH B . 
GA 7 HOH 170 670 407 HOH HOH B . 
GA 7 HOH 171 671 512 HOH HOH B . 
GA 7 HOH 172 672 494 HOH HOH B . 
GA 7 HOH 173 673 586 HOH HOH B . 
GA 7 HOH 174 674 547 HOH HOH B . 
GA 7 HOH 175 675 587 HOH HOH B . 
GA 7 HOH 176 676 451 HOH HOH B . 
GA 7 HOH 177 677 531 HOH HOH B . 
GA 7 HOH 178 678 635 HOH HOH B . 
GA 7 HOH 179 679 389 HOH HOH B . 
GA 7 HOH 180 680 652 HOH HOH B . 
GA 7 HOH 181 681 483 HOH HOH B . 
GA 7 HOH 182 682 486 HOH HOH B . 
GA 7 HOH 183 683 558 HOH HOH B . 
GA 7 HOH 184 684 580 HOH HOH B . 
GA 7 HOH 185 685 572 HOH HOH B . 
GA 7 HOH 186 686 551 HOH HOH B . 
GA 7 HOH 187 687 422 HOH HOH B . 
GA 7 HOH 188 688 427 HOH HOH B . 
GA 7 HOH 189 689 570 HOH HOH B . 
GA 7 HOH 190 690 574 HOH HOH B . 
GA 7 HOH 191 691 437 HOH HOH B . 
GA 7 HOH 192 692 540 HOH HOH B . 
GA 7 HOH 193 693 398 HOH HOH B . 
GA 7 HOH 194 694 525 HOH HOH B . 
GA 7 HOH 195 695 498 HOH HOH B . 
GA 7 HOH 196 696 643 HOH HOH B . 
GA 7 HOH 197 697 500 HOH HOH B . 
GA 7 HOH 198 698 409 HOH HOH B . 
GA 7 HOH 199 699 425 HOH HOH B . 
GA 7 HOH 200 700 612 HOH HOH B . 
GA 7 HOH 201 701 672 HOH HOH B . 
GA 7 HOH 202 702 456 HOH HOH B . 
GA 7 HOH 203 703 532 HOH HOH B . 
GA 7 HOH 204 704 460 HOH HOH B . 
GA 7 HOH 205 705 516 HOH HOH B . 
GA 7 HOH 206 706 562 HOH HOH B . 
GA 7 HOH 207 707 420 HOH HOH B . 
GA 7 HOH 208 708 592 HOH HOH B . 
GA 7 HOH 209 709 426 HOH HOH B . 
GA 7 HOH 210 710 589 HOH HOH B . 
GA 7 HOH 211 711 602 HOH HOH B . 
GA 7 HOH 212 712 511 HOH HOH B . 
GA 7 HOH 213 713 596 HOH HOH B . 
GA 7 HOH 214 714 628 HOH HOH B . 
GA 7 HOH 215 715 467 HOH HOH B . 
GA 7 HOH 216 716 702 HOH HOH B . 
GA 7 HOH 217 717 396 HOH HOH B . 
GA 7 HOH 218 718 384 HOH HOH B . 
GA 7 HOH 219 719 413 HOH HOH B . 
GA 7 HOH 220 720 514 HOH HOH B . 
GA 7 HOH 221 721 563 HOH HOH B . 
GA 7 HOH 222 722 605 HOH HOH B . 
GA 7 HOH 223 723 678 HOH HOH B . 
GA 7 HOH 224 724 479 HOH HOH B . 
GA 7 HOH 225 725 539 HOH HOH B . 
GA 7 HOH 226 726 529 HOH HOH B . 
GA 7 HOH 227 727 649 HOH HOH B . 
GA 7 HOH 228 728 445 HOH HOH B . 
GA 7 HOH 229 729 703 HOH HOH B . 
GA 7 HOH 230 730 629 HOH HOH B . 
GA 7 HOH 231 731 553 HOH HOH B . 
GA 7 HOH 232 732 657 HOH HOH B . 
GA 7 HOH 233 733 502 HOH HOH B . 
GA 7 HOH 234 734 582 HOH HOH B . 
GA 7 HOH 235 735 490 HOH HOH B . 
GA 7 HOH 236 736 546 HOH HOH B . 
GA 7 HOH 237 737 639 HOH HOH B . 
GA 7 HOH 238 738 464 HOH HOH B . 
GA 7 HOH 239 739 561 HOH HOH B . 
GA 7 HOH 240 740 614 HOH HOH B . 
GA 7 HOH 241 741 499 HOH HOH B . 
GA 7 HOH 242 742 699 HOH HOH B . 
GA 7 HOH 243 743 438 HOH HOH B . 
GA 7 HOH 244 744 609 HOH HOH B . 
GA 7 HOH 245 745 636 HOH HOH B . 
GA 7 HOH 246 746 637 HOH HOH B . 
GA 7 HOH 247 747 577 HOH HOH B . 
GA 7 HOH 248 748 692 HOH HOH B . 
GA 7 HOH 249 749 581 HOH HOH B . 
GA 7 HOH 250 750 591 HOH HOH B . 
GA 7 HOH 251 751 533 HOH HOH B . 
GA 7 HOH 252 752 595 HOH HOH B . 
GA 7 HOH 253 753 18  HOH HOH B . 
GA 7 HOH 254 754 668 HOH HOH B . 
GA 7 HOH 255 755 507 HOH HOH B . 
GA 7 HOH 256 756 638 HOH HOH B . 
GA 7 HOH 257 757 450 HOH HOH B . 
GA 7 HOH 258 758 656 HOH HOH B . 
GA 7 HOH 259 759 705 HOH HOH B . 
GA 7 HOH 260 760 611 HOH HOH B . 
GA 7 HOH 261 761 633 HOH HOH B . 
GA 7 HOH 262 762 530 HOH HOH B . 
GA 7 HOH 263 763 682 HOH HOH B . 
GA 7 HOH 264 764 658 HOH HOH B . 
GA 7 HOH 265 765 522 HOH HOH B . 
GA 7 HOH 266 766 463 HOH HOH B . 
GA 7 HOH 267 767 645 HOH HOH B . 
GA 7 HOH 268 768 559 HOH HOH B . 
GA 7 HOH 269 769 693 HOH HOH B . 
GA 7 HOH 270 770 549 HOH HOH B . 
GA 7 HOH 271 771 555 HOH HOH B . 
GA 7 HOH 272 772 597 HOH HOH B . 
GA 7 HOH 273 773 544 HOH HOH B . 
GA 7 HOH 274 774 706 HOH HOH B . 
GA 7 HOH 275 775 667 HOH HOH B . 
GA 7 HOH 276 776 697 HOH HOH B . 
GA 7 HOH 277 777 478 HOH HOH B . 
GA 7 HOH 278 778 666 HOH HOH B . 
GA 7 HOH 279 779 473 HOH HOH B . 
GA 7 HOH 280 780 681 HOH HOH B . 
GA 7 HOH 281 781 644 HOH HOH B . 
GA 7 HOH 282 782 599 HOH HOH B . 
GA 7 HOH 283 783 523 HOH HOH B . 
GA 7 HOH 284 784 11  HOH HOH B . 
GA 7 HOH 285 785 491 HOH HOH B . 
GA 7 HOH 286 786 590 HOH HOH B . 
GA 7 HOH 287 787 518 HOH HOH B . 
GA 7 HOH 288 788 679 HOH HOH B . 
GA 7 HOH 289 789 624 HOH HOH B . 
GA 7 HOH 290 790 485 HOH HOH B . 
GA 7 HOH 291 791 662 HOH HOH B . 
GA 7 HOH 292 792 661 HOH HOH B . 
GA 7 HOH 293 793 684 HOH HOH B . 
GA 7 HOH 294 794 470 HOH HOH B . 
GA 7 HOH 295 795 600 HOH HOH B . 
GA 7 HOH 296 796 604 HOH HOH B . 
GA 7 HOH 297 797 608 HOH HOH B . 
GA 7 HOH 298 798 537 HOH HOH B . 
GA 7 HOH 299 799 630 HOH HOH B . 
GA 7 HOH 300 800 685 HOH HOH B . 
GA 7 HOH 301 801 688 HOH HOH B . 
GA 7 HOH 302 802 449 HOH HOH B . 
GA 7 HOH 303 803 578 HOH HOH B . 
GA 7 HOH 304 804 576 HOH HOH B . 
GA 7 HOH 305 805 660 HOH HOH B . 
GA 7 HOH 306 806 506 HOH HOH B . 
GA 7 HOH 307 807 556 HOH HOH B . 
GA 7 HOH 308 808 627 HOH HOH B . 
GA 7 HOH 309 809 694 HOH HOH B . 
GA 7 HOH 310 810 442 HOH HOH B . 
GA 7 HOH 311 811 698 HOH HOH B . 
GA 7 HOH 312 812 564 HOH HOH B . 
GA 7 HOH 313 813 497 HOH HOH B . 
GA 7 HOH 314 814 603 HOH HOH B . 
GA 7 HOH 315 815 654 HOH HOH B . 
GA 7 HOH 316 816 606 HOH HOH B . 
GA 7 HOH 317 817 623 HOH HOH B . 
GA 7 HOH 318 818 634 HOH HOH B . 
GA 7 HOH 319 819 607 HOH HOH B . 
GA 7 HOH 320 820 669 HOH HOH B . 
GA 7 HOH 321 821 677 HOH HOH B . 
GA 7 HOH 322 822 659 HOH HOH B . 
GA 7 HOH 323 823 655 HOH HOH B . 
GA 7 HOH 324 824 9   HOH HOH B . 
GA 7 HOH 325 825 707 HOH HOH B . 
GA 7 HOH 326 826 690 HOH HOH B . 
GA 7 HOH 327 827 708 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                     9G66 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.964 
_cell.length_a_esd                 ? 
_cell.length_b                     91.329 
_cell.length_b_esd                 ? 
_cell.length_c                     106.061 
_cell.length_c_esd                 ? 
_cell.volume                       755194.003 
_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                         9G66 
_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                   9G66 
_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             2.47 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.22 
_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              ? 
_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    '20% PEG 8000, 0.2 M Li2SO4, 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         2023-09-26 
_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   0.9763 
_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        0.9763 
_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                          22.03 
_reflns.entry_id                                       9G66 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.79 
_reflns.d_resolution_low                               106.06 
_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                                     71415 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.3 
_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                                0.122 
_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                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.111 
_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                                    1.79 
_reflns_shell.d_res_low                                     1.90 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11263 
_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                               1.037 
_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                                  0.798 
_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                                  0.945 
_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                               25.37 
_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                                 9G66 
_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                            1.79 
_refine.ls_d_res_low                             45.66 
_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                     71329 
_refine.ls_number_reflns_R_free                  997 
_refine.ls_number_reflns_R_work                  70332 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.35 
_refine.ls_percent_reflns_R_free                 1.40 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1743 
_refine.ls_R_factor_R_free                       0.2210 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1737 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.6781 
_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                            0.1980 
_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                       1.79 
_refine_hist.d_res_low                        45.66 
_refine_hist.number_atoms_solvent             635 
_refine_hist.number_atoms_total               6101 
_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        5338 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         128 
_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' ? 0.0101  ? 5654 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0732  ? 7615 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0644  ? 845  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0112  ? 1008 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.5047 ? 2115 ? 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' 1.79 1.89  . . 138 9739  97.70 . . . . 0.2393 . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 1.89 2.00  . . 142 10006 99.77 . . . . 0.2140 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 2.00 2.16  . . 142 9990  99.73 . . . . 0.1899 . . . . . . . . . . . 0.2281 
'X-RAY DIFFRACTION' 2.16 2.38  . . 142 9985  99.67 . . . . 0.1837 . . . . . . . . . . . 0.2376 
'X-RAY DIFFRACTION' 2.38 2.72  . . 141 10030 99.33 . . . . 0.1816 . . . . . . . . . . . 0.2656 
'X-RAY DIFFRACTION' 2.72 3.43  . . 144 10147 99.68 . . . . 0.1698 . . . . . . . . . . . 0.2168 
'X-RAY DIFFRACTION' 3.43 45.66 . . 148 10435 99.54 . . . . 0.1489 . . . . . . . . . . . 0.1806 
# 
_struct.entry_id                     9G66 
_struct.title                        'Crystal structure of WT Rhizobium etli L-asparaginase ReAV 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        9G66 
_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 3 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 2 ? 
J  N N 2 ? 
K  N N 4 ? 
L  N N 2 ? 
M  N N 2 ? 
N  N N 2 ? 
O  N N 5 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 6 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 2 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 2 ? 
CA N N 5 ? 
DA N N 6 ? 
EA N N 2 ? 
FA N N 7 ? 
GA N N 7 ? 
# 
_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 9G66 A 7 ? 373 ? Q2K0Z2 1 ? 367 ? 1 367 
2 1 9G66 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 9G66 GLY A 1 ? UNP Q2K0Z2 ? ? 'expression tag' -5 1  
1 9G66 ILE A 2 ? UNP Q2K0Z2 ? ? 'expression tag' -4 2  
1 9G66 ASP A 3 ? UNP Q2K0Z2 ? ? 'expression tag' -3 3  
1 9G66 PRO A 4 ? UNP Q2K0Z2 ? ? 'expression tag' -2 4  
1 9G66 PHE A 5 ? UNP Q2K0Z2 ? ? 'expression tag' -1 5  
1 9G66 THR A 6 ? UNP Q2K0Z2 ? ? 'expression tag' 0  6  
2 9G66 GLY B 1 ? UNP Q2K0Z2 ? ? 'expression tag' -5 7  
2 9G66 ILE B 2 ? UNP Q2K0Z2 ? ? 'expression tag' -4 8  
2 9G66 ASP B 3 ? UNP Q2K0Z2 ? ? 'expression tag' -3 9  
2 9G66 PRO B 4 ? UNP Q2K0Z2 ? ? 'expression tag' -2 10 
2 9G66 PHE B 5 ? UNP Q2K0Z2 ? ? 'expression tag' -1 11 
2 9G66 THR B 6 ? UNP Q2K0Z2 ? ? 'expression tag' 0  12 
# 
_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)' 8390  ? 
1 MORE         54    ? 
1 'SSA (A^2)'  26280 ? 
# 
_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,Y,Z,AA,BA,CA,DA,EA,FA,GA 
# 
_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 ? GLY B 156 ? CYS B 135 GLY B 150 1 ? 16 
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 ? GLY B 224 ? LEU B 198 GLY B 218 1 ? 21 
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 
covale1 covale both ? A  ARG 230 C  ? ? ? 1_555 A  CSO 231 N  ? ? A ARG 224 A CSO 225 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale2 covale both ? A  CSO 231 C  ? ? ? 1_555 A  ALA 232 N  ? ? A CSO 225 A ALA 226 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale3 covale both ? B  ARG 230 C  ? ? ? 1_555 B  CSO 231 N  ? ? B ARG 224 B CSO 225 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale4 covale both ? B  CSO 231 C  ? ? ? 1_555 B  ALA 232 N  ? ? B CSO 225 B ALA 226 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
metalc1 metalc ?    ? A  CYS 141 SG ? ? ? 1_555 T  CD  .   CD ? ? A CYS 135 A CD  418 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc2 metalc ?    ? A  LYS 144 NZ ? ? ? 1_555 T  CD  .   CD ? ? A LYS 138 A CD  418 1_555 ? ? ? ? ? ? ? 2.521 ? ? 
metalc3 metalc ?    ? A  CYS 195 SG ? ? ? 1_555 T  CD  .   CD ? ? A CYS 189 A CD  418 1_555 ? ? ? ? ? ? ? 2.592 ? ? 
metalc4 metalc ?    ? O  ASN .   N  A ? ? 1_555 T  CD  .   CD ? ? A ASN 413 A CD  418 1_555 ? ? ? ? ? ? ? 2.653 ? ? 
metalc5 metalc ?    ? B  CYS 141 SG ? ? ? 1_555 DA CD  .   CD ? ? B CYS 135 B CD  410 1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc6 metalc ?    ? B  LYS 144 NZ ? ? ? 1_555 DA CD  .   CD ? ? B LYS 138 B CD  410 1_555 ? ? ? ? ? ? ? 2.505 ? ? 
metalc7 metalc ?    ? B  CYS 195 SG ? ? ? 1_555 DA CD  .   CD ? ? B CYS 189 B CD  410 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc8 metalc ?    ? CA ASN .   N  A ? ? 1_555 DA CD  .   CD ? ? B ASN 409 B CD  410 1_555 ? ? ? ? ? ? ? 2.685 ? ? 
metalc9 metalc ?    ? DA CD  .   CD ? ? ? 1_555 GA HOH .   O  B ? B CD  410 B HOH 577 1_555 ? ? ? ? ? ? ? 2.521 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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  SG ? A  CYS 141 ? A CYS 135 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 NZ ? A  LYS 144 ? A LYS 138 ? 1_555 113.3 ? 
2  SG ? A  CYS 141 ? A CYS 135 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 SG ? A  CYS 195 ? A CYS 189 ? 1_555 115.9 ? 
3  NZ ? A  LYS 144 ? A LYS 138 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 SG ? A  CYS 195 ? A CYS 189 ? 1_555 96.4  ? 
4  SG ? A  CYS 141 ? A CYS 135 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 N  A O  ASN .   ? A ASN 413 ? 1_555 93.5  ? 
5  NZ ? A  LYS 144 ? A LYS 138 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 N  A O  ASN .   ? A ASN 413 ? 1_555 104.6 ? 
6  SG ? A  CYS 195 ? A CYS 189 ? 1_555 CD ? T  CD . ? A CD 418 ? 1_555 N  A O  ASN .   ? A ASN 413 ? 1_555 133.2 ? 
7  SG ? B  CYS 141 ? B CYS 135 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 NZ ? B  LYS 144 ? B LYS 138 ? 1_555 113.3 ? 
8  SG ? B  CYS 141 ? B CYS 135 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 SG ? B  CYS 195 ? B CYS 189 ? 1_555 112.0 ? 
9  NZ ? B  LYS 144 ? B LYS 138 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 SG ? B  CYS 195 ? B CYS 189 ? 1_555 98.9  ? 
10 SG ? B  CYS 141 ? B CYS 135 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 N  A CA ASN .   ? B ASN 409 ? 1_555 92.2  ? 
11 NZ ? B  LYS 144 ? B LYS 138 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 N  A CA ASN .   ? B ASN 409 ? 1_555 104.1 ? 
12 SG ? B  CYS 195 ? B CYS 189 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 N  A CA ASN .   ? B ASN 409 ? 1_555 136.3 ? 
13 SG ? B  CYS 141 ? B CYS 135 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 O  B GA HOH .   ? B HOH 577 ? 1_555 103.0 ? 
14 NZ ? B  LYS 144 ? B LYS 138 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 O  B GA HOH .   ? B HOH 577 ? 1_555 84.2  ? 
15 SG ? B  CYS 195 ? B CYS 189 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 O  B GA HOH .   ? B HOH 577 ? 1_555 139.9 ? 
16 N  A CA ASN .   ? B ASN 409 ? 1_555 CD ? DA CD . ? B CD 410 ? 1_555 O  B GA HOH .   ? B HOH 577 ? 1_555 20.1  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CSO A 231 ? . . . . CSO A 225 ? 1_555 . . . . . . . CYS 1 CSO Hydroxylation 'Named protein modification' 
2 CSO B 231 ? . . . . CSO B 225 ? 1_555 . . . . . . . CYS 1 CSO Hydroxylation 'Named protein modification' 
# 
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                   9G66 
_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   Y 
# 
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  ? ? -98.25  -74.39  
2 1 ARG A 47  ? ? 52.96   -133.52 
3 1 SER A 80  ? ? -111.98 79.97   
4 1 ALA A 243 ? ? -148.61 -85.87  
5 1 GLU B 17  ? ? -94.28  -75.78  
6 1 ARG B 47  ? ? 51.84   -137.92 
7 1 SER B 80  ? ? -111.97 78.72   
8 1 ASN B 190 ? ? 80.80   18.07   
9 1 ALA B 243 ? ? -139.69 -83.14  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSO 231 A CSO 225 ? CYS 'modified residue' 
2 B CSO 231 B CSO 225 ? CYS 'modified residue' 
# 
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 29.777 0.955   35.267 0.127086210712 0.172024668057 0.164897413789 -0.0123844913199   
0.000115514577601  0.0335443141157   2.40690487324  3.79450647431 0.950530262141 -2.45361765185  0.465808081146   -0.652542704261 
-0.0998334222689  0.0156111660974  0.0840440135688  -0.164345850161  0.088512596918    -0.108936291476  0.220196066667   
0.022845288906   0.11267105009    
'X-RAY DIFFRACTION' 2  ? refined 35.196 -14.996 9.005  0.225008313615 0.181116278858 0.186208720463 0.0407272501821    
0.0445059987929    0.0120442811111   1.98516395454  1.92427937544 1.21334206068  -0.867775962633 0.642589847474   -0.620781829054 
0.0245512012888   -0.0271370467985 0.0045170977587  0.0973248251656  -0.14383592818    0.0246277357296  -0.181487870274  
0.129771615066   0.077447972414   
'X-RAY DIFFRACTION' 3  ? refined 38.269 -17.038 27.330 0.189917670355 0.216628538217 0.186570829155 0.0834719807398    
0.0148361798508    0.0591642670261   1.96121411484  1.50330783069 1.13634298472  0.320500998558  0.676769429588   0.510767129028  
0.0240351922692   -0.080248522907  0.0421310618363  -0.0893896579845 -0.102648075159   -0.121114971624  0.121499199979   
0.316841849067   0.20687215785    
'X-RAY DIFFRACTION' 4  ? refined 51.865 -11.953 21.165 0.197458168511 0.56303038634  0.368580199361 0.117075205251     
0.0317866442543    0.0120141177101   1.79266347616  6.50744515437 0.108592021927 0.196583611922  0.393016962657   0.262170158656  
-0.0934456336087  0.00459216513614 0.0634442183958  -0.390209914759  -0.0652379697817  -0.934625837483  0.0679850495665  
0.161213962645   0.850180726726   
'X-RAY DIFFRACTION' 5  ? refined 37.212 5.102   24.819 0.124302766278 0.185914492522 0.216936050261 -0.0140316818181   
-0.00192486966708  0.0219295065599   1.23674402076  1.32184143641 1.21230470748  -0.366493167176 -0.0927804314823 -0.296085755454 
0.00889890604124  -0.0207313921792 0.0173132539167  -0.0356249162995 0.134254819662    -0.156066756607  -0.0151985060144 
-0.0453476303453 0.223767428804   
'X-RAY DIFFRACTION' 6  ? refined 28.941 -10.780 17.630 0.264069866233 0.199090962633 0.250654505369 0.103231491408     
0.0355218382024    0.0145785389552   9.04046040553  7.92937914674 1.99988951048  3.58255183965   4.34417815097    3.37386534193   
-0.0916845884929  -0.374721648362  0.409520286016   0.415430831327   0.929798490409    0.351810995403   0.319344220493   
0.372355326816   0.163908180219   
'X-RAY DIFFRACTION' 7  ? refined 13.637 -8.123  38.713 0.269873328962 0.173629245186 0.259837764097 -0.00248362059066  
0.00563501061387   -0.00242519989668 3.68443953275  1.35029965668 2.74280289831  -1.36193465647  -2.79762039745   1.78653034913   
-0.227883329722   -0.121653171316  0.277249859276   -0.152336701241  -0.251130636046   0.0167050497608  0.521830759243   
0.430288048513   -0.0308024294585 
'X-RAY DIFFRACTION' 8  ? refined 2.745  12.316  27.570 0.147290181352 0.130082813158 0.173241833299 0.00107936349221   
-0.00111110899781  -0.0179761677051  0.880543162643 1.82289889929 0.538954766807 -0.838345073021 0.461232382395   -0.827067464845 
0.0314618078328   -0.0209764231275 -0.018350680037  -0.011288269837  0.00721074296336  0.115319237035   0.0342191147883  
-0.0725191128569 -0.0411708825236 
'X-RAY DIFFRACTION' 9  ? refined 3.732  17.841  6.522  0.265006656333 0.201082663774 0.154621114576 0.0715754438579    
0.0250495846682    0.0141227238426   2.38938823663  1.98578844635 1.00063952663  -0.468254584208 -0.145719067696  0.0995995527813 
0.143417633553    -0.145452244947  -0.0001419600193 0.233853299949   -0.00984243305636 -0.107021690231  -0.379220945994  
-0.0621946584151 0.0393607804653  
'X-RAY DIFFRACTION' 10 ? refined 9.660  16.039  6.404  0.27545045415  0.180760535193 0.206595747269 0.0534749978064    
0.0354551710757    0.0289676795574   3.71435423417  3.69823671663 2.55984313388  -1.88602778805  -1.54707129595   2.12784450522   
0.324649138951    -0.199494864759  -0.0980427244604 0.249272550861   -0.128350178551   -0.335564670584  -0.595147855986  
-0.0499300052126 0.0641558620234  
'X-RAY DIFFRACTION' 11 ? refined 3.865  30.095  21.136 0.14904465919  0.133921311207 0.225937941598 0.0153207646441    
-0.00395809742312  -0.00839447755605 3.29976241653  6.42865576346 5.79045220846  -0.540861965208 -1.29295602973   -2.08098109555  
0.156755940774    0.105774969632   -0.251589758103  0.131615279782   0.543750867838    -0.139374212576  -0.229563416553  
-0.367138962529  0.0216630747898  
'X-RAY DIFFRACTION' 12 ? refined -3.291 17.353  26.174 0.161591396007 0.119213955845 0.187581003949 0.0307874085404    
0.0123664037509    0.0112858118771   2.76532337158  1.37295967687 1.57454392961  -0.115820966019 -0.149750017525  -0.108396024375 
0.0333676529921   0.00662751483012 -0.0356721811235 0.00507040343114 0.0553529625001   0.171753916199   0.010044834297   
-0.0474045499543 -0.164900586353  
'X-RAY DIFFRACTION' 13 ? refined -4.091 4.013   21.806 0.136477966035 0.109149584749 0.216739845687 0.0031636355902    
-0.0194953650016   -0.0140782066381  2.13081696363  1.60687176469 2.24560913587  -0.143417071826 -0.729063929667  -0.673225721223 
0.0243831576579   0.0339911014235  -0.040149257125  0.137961273829   -0.0768840199946  0.240570624986   -0.182002939383  
0.105547126264   -0.253489568076  
'X-RAY DIFFRACTION' 14 ? refined 3.186  -2.466  25.503 0.150088970025 0.126536314914 0.200466574751 -0.000145502640132 
-0.0144262546398   -0.0115008905218  1.41880862832  2.48638969155 2.77855904334  -0.816907979875 -1.05773071565   -0.192998598495 
-0.0190339684088  -0.0619237466325 0.0542111546705  0.163185185729   -0.28403537935    0.293196785089   -0.0983951632544 
0.248223263904   -0.310460763701  
'X-RAY DIFFRACTION' 15 ? refined 10.083 -7.514  33.385 0.163397259929 0.135651639302 0.244851149533 -0.0120231361551   
-0.000899182758992 0.0206412310042   2.18484940877  3.05097301122 6.69891688819  -2.10427294821  -2.94476398547   4.01177621392   
-0.00103369010303 -0.0414314756676 0.131165181848   -0.0788278209965 -0.04449150550    0.00500823801557 0.114087586231   
0.0503893634128  -0.110950414178  
'X-RAY DIFFRACTION' 16 ? refined 10.543 14.628  17.986 0.148695884263 0.417091508031 0.219585588289 -0.04344561142     
0.315709636885     -0.0900162906268  1.58708854119  1.99993306574 6.6881780897   3.36858598828   -2.80833502076   -3.73943347301  
-0.00925619136096 -0.0323137033161 0.125110161335   -0.0441685831203 -0.07386540344    -0.0117844843584 0.0277057653921  
0.0455921085042  -0.0454919749273 
# 
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 46  '( CHAIN A AND RESID 2:46 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  A 47  A 161 '( CHAIN A AND RESID 47:161 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  A 162 A 217 '( CHAIN A AND RESID 162:217 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  A 218 A 237 '( CHAIN A AND RESID 218:237 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  A 238 A 352 '( CHAIN A AND RESID 238:352 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  A 413 A 413 '( CHAIN A AND RESID 413:413 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  B -4  B 14  '( CHAIN B AND RESID -4:14 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  B 15  B 70  '( CHAIN B AND RESID 15:70 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  B 71  B 114 '( CHAIN B AND RESID 71:114 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 B 115 B 149 '( CHAIN B AND RESID 115:149 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 B 150 B 174 '( CHAIN B AND RESID 150:174 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 B 175 B 237 '( CHAIN B AND RESID 175:237 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 B 238 B 288 '( CHAIN B AND RESID 238:288 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 B 289 B 329 '( CHAIN B AND RESID 289:329 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 B 330 B 367 '( CHAIN B AND RESID 330:367 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 B 409 B 409 '( CHAIN B AND RESID 409:409 )' ? ? ? ? ? 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 808 ? 5.82 . 
2 1 O ? B HOH 826 ? 5.83 . 
3 1 O ? B HOH 827 ? 6.08 . 
# 
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 LYS 354 ? B LYS 360 
25 1 Y 1 B SER 355 ? B SER 361 
26 1 Y 1 B ASN 356 ? B ASN 362 
# 
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  
CSO N    N  N N 75  
CSO CA   C  N R 76  
CSO CB   C  N N 77  
CSO SG   S  N N 78  
CSO C    C  N N 79  
CSO O    O  N N 80  
CSO OXT  O  N N 81  
CSO OD   O  N N 82  
CSO H    H  N N 83  
CSO H2   H  N N 84  
CSO HA   H  N N 85  
CSO HB2  H  N N 86  
CSO HB3  H  N N 87  
CSO HXT  H  N N 88  
CSO HD   H  N N 89  
CYS N    N  N N 90  
CYS CA   C  N R 91  
CYS C    C  N N 92  
CYS O    O  N N 93  
CYS CB   C  N N 94  
CYS SG   S  N N 95  
CYS OXT  O  N N 96  
CYS H    H  N N 97  
CYS H2   H  N N 98  
CYS HA   H  N N 99  
CYS HB2  H  N N 100 
CYS HB3  H  N N 101 
CYS HG   H  N N 102 
CYS HXT  H  N N 103 
EDO C1   C  N N 104 
EDO O1   O  N N 105 
EDO C2   C  N N 106 
EDO O2   O  N N 107 
EDO H11  H  N N 108 
EDO H12  H  N N 109 
EDO HO1  H  N N 110 
EDO H21  H  N N 111 
EDO H22  H  N N 112 
EDO HO2  H  N N 113 
GLN N    N  N N 114 
GLN CA   C  N S 115 
GLN C    C  N N 116 
GLN O    O  N N 117 
GLN CB   C  N N 118 
GLN CG   C  N N 119 
GLN CD   C  N N 120 
GLN OE1  O  N N 121 
GLN NE2  N  N N 122 
GLN OXT  O  N N 123 
GLN H    H  N N 124 
GLN H2   H  N N 125 
GLN HA   H  N N 126 
GLN HB2  H  N N 127 
GLN HB3  H  N N 128 
GLN HG2  H  N N 129 
GLN HG3  H  N N 130 
GLN HE21 H  N N 131 
GLN HE22 H  N N 132 
GLN HXT  H  N N 133 
GLU N    N  N N 134 
GLU CA   C  N S 135 
GLU C    C  N N 136 
GLU O    O  N N 137 
GLU CB   C  N N 138 
GLU CG   C  N N 139 
GLU CD   C  N N 140 
GLU OE1  O  N N 141 
GLU OE2  O  N N 142 
GLU OXT  O  N N 143 
GLU H    H  N N 144 
GLU H2   H  N N 145 
GLU HA   H  N N 146 
GLU HB2  H  N N 147 
GLU HB3  H  N N 148 
GLU HG2  H  N N 149 
GLU HG3  H  N N 150 
GLU HE2  H  N N 151 
GLU HXT  H  N N 152 
GLY N    N  N N 153 
GLY CA   C  N N 154 
GLY C    C  N N 155 
GLY O    O  N N 156 
GLY OXT  O  N N 157 
GLY H    H  N N 158 
GLY H2   H  N N 159 
GLY HA2  H  N N 160 
GLY HA3  H  N N 161 
GLY HXT  H  N N 162 
GOL C1   C  N N 163 
GOL O1   O  N N 164 
GOL C2   C  N N 165 
GOL O2   O  N N 166 
GOL C3   C  N N 167 
GOL O3   O  N N 168 
GOL H11  H  N N 169 
GOL H12  H  N N 170 
GOL HO1  H  N N 171 
GOL H2   H  N N 172 
GOL HO2  H  N N 173 
GOL H31  H  N N 174 
GOL H32  H  N N 175 
GOL HO3  H  N N 176 
HIS N    N  N N 177 
HIS CA   C  N S 178 
HIS C    C  N N 179 
HIS O    O  N N 180 
HIS CB   C  N N 181 
HIS CG   C  Y N 182 
HIS ND1  N  Y N 183 
HIS CD2  C  Y N 184 
HIS CE1  C  Y N 185 
HIS NE2  N  Y N 186 
HIS OXT  O  N N 187 
HIS H    H  N N 188 
HIS H2   H  N N 189 
HIS HA   H  N N 190 
HIS HB2  H  N N 191 
HIS HB3  H  N N 192 
HIS HD1  H  N N 193 
HIS HD2  H  N N 194 
HIS HE1  H  N N 195 
HIS HE2  H  N N 196 
HIS HXT  H  N N 197 
HOH O    O  N N 198 
HOH H1   H  N N 199 
HOH H2   H  N N 200 
ILE N    N  N N 201 
ILE CA   C  N S 202 
ILE C    C  N N 203 
ILE O    O  N N 204 
ILE CB   C  N S 205 
ILE CG1  C  N N 206 
ILE CG2  C  N N 207 
ILE CD1  C  N N 208 
ILE OXT  O  N N 209 
ILE H    H  N N 210 
ILE H2   H  N N 211 
ILE HA   H  N N 212 
ILE HB   H  N N 213 
ILE HG12 H  N N 214 
ILE HG13 H  N N 215 
ILE HG21 H  N N 216 
ILE HG22 H  N N 217 
ILE HG23 H  N N 218 
ILE HD11 H  N N 219 
ILE HD12 H  N N 220 
ILE HD13 H  N N 221 
ILE HXT  H  N N 222 
LEU N    N  N N 223 
LEU CA   C  N S 224 
LEU C    C  N N 225 
LEU O    O  N N 226 
LEU CB   C  N N 227 
LEU CG   C  N N 228 
LEU CD1  C  N N 229 
LEU CD2  C  N N 230 
LEU OXT  O  N N 231 
LEU H    H  N N 232 
LEU H2   H  N N 233 
LEU HA   H  N N 234 
LEU HB2  H  N N 235 
LEU HB3  H  N N 236 
LEU HG   H  N N 237 
LEU HD11 H  N N 238 
LEU HD12 H  N N 239 
LEU HD13 H  N N 240 
LEU HD21 H  N N 241 
LEU HD22 H  N N 242 
LEU HD23 H  N N 243 
LEU HXT  H  N N 244 
LYS N    N  N N 245 
LYS CA   C  N S 246 
LYS C    C  N N 247 
LYS O    O  N N 248 
LYS CB   C  N N 249 
LYS CG   C  N N 250 
LYS CD   C  N N 251 
LYS CE   C  N N 252 
LYS NZ   N  N N 253 
LYS OXT  O  N N 254 
LYS H    H  N N 255 
LYS H2   H  N N 256 
LYS HA   H  N N 257 
LYS HB2  H  N N 258 
LYS HB3  H  N N 259 
LYS HG2  H  N N 260 
LYS HG3  H  N N 261 
LYS HD2  H  N N 262 
LYS HD3  H  N N 263 
LYS HE2  H  N N 264 
LYS HE3  H  N N 265 
LYS HZ1  H  N N 266 
LYS HZ2  H  N N 267 
LYS HZ3  H  N N 268 
LYS HXT  H  N N 269 
MET N    N  N N 270 
MET CA   C  N S 271 
MET C    C  N N 272 
MET O    O  N N 273 
MET CB   C  N N 274 
MET CG   C  N N 275 
MET SD   S  N N 276 
MET CE   C  N N 277 
MET OXT  O  N N 278 
MET H    H  N N 279 
MET H2   H  N N 280 
MET HA   H  N N 281 
MET HB2  H  N N 282 
MET HB3  H  N N 283 
MET HG2  H  N N 284 
MET HG3  H  N N 285 
MET HE1  H  N N 286 
MET HE2  H  N N 287 
MET HE3  H  N N 288 
MET HXT  H  N N 289 
PEG C1   C  N N 290 
PEG O1   O  N N 291 
PEG C2   C  N N 292 
PEG O2   O  N N 293 
PEG C3   C  N N 294 
PEG C4   C  N N 295 
PEG O4   O  N N 296 
PEG H11  H  N N 297 
PEG H12  H  N N 298 
PEG HO1  H  N N 299 
PEG H21  H  N N 300 
PEG H22  H  N N 301 
PEG H31  H  N N 302 
PEG H32  H  N N 303 
PEG H41  H  N N 304 
PEG H42  H  N N 305 
PEG HO4  H  N N 306 
PHE N    N  N N 307 
PHE CA   C  N S 308 
PHE C    C  N N 309 
PHE O    O  N N 310 
PHE CB   C  N N 311 
PHE CG   C  Y N 312 
PHE CD1  C  Y N 313 
PHE CD2  C  Y N 314 
PHE CE1  C  Y N 315 
PHE CE2  C  Y N 316 
PHE CZ   C  Y N 317 
PHE OXT  O  N N 318 
PHE H    H  N N 319 
PHE H2   H  N N 320 
PHE HA   H  N N 321 
PHE HB2  H  N N 322 
PHE HB3  H  N N 323 
PHE HD1  H  N N 324 
PHE HD2  H  N N 325 
PHE HE1  H  N N 326 
PHE HE2  H  N N 327 
PHE HZ   H  N N 328 
PHE HXT  H  N N 329 
PRO N    N  N N 330 
PRO CA   C  N S 331 
PRO C    C  N N 332 
PRO O    O  N N 333 
PRO CB   C  N N 334 
PRO CG   C  N N 335 
PRO CD   C  N N 336 
PRO OXT  O  N N 337 
PRO H    H  N N 338 
PRO HA   H  N N 339 
PRO HB2  H  N N 340 
PRO HB3  H  N N 341 
PRO HG2  H  N N 342 
PRO HG3  H  N N 343 
PRO HD2  H  N N 344 
PRO HD3  H  N N 345 
PRO HXT  H  N N 346 
SER N    N  N N 347 
SER CA   C  N S 348 
SER C    C  N N 349 
SER O    O  N N 350 
SER CB   C  N N 351 
SER OG   O  N N 352 
SER OXT  O  N N 353 
SER H    H  N N 354 
SER H2   H  N N 355 
SER HA   H  N N 356 
SER HB2  H  N N 357 
SER HB3  H  N N 358 
SER HG   H  N N 359 
SER HXT  H  N N 360 
THR N    N  N N 361 
THR CA   C  N S 362 
THR C    C  N N 363 
THR O    O  N N 364 
THR CB   C  N R 365 
THR OG1  O  N N 366 
THR CG2  C  N N 367 
THR OXT  O  N N 368 
THR H    H  N N 369 
THR H2   H  N N 370 
THR HA   H  N N 371 
THR HB   H  N N 372 
THR HG1  H  N N 373 
THR HG21 H  N N 374 
THR HG22 H  N N 375 
THR HG23 H  N N 376 
THR HXT  H  N N 377 
TRP N    N  N N 378 
TRP CA   C  N S 379 
TRP C    C  N N 380 
TRP O    O  N N 381 
TRP CB   C  N N 382 
TRP CG   C  Y N 383 
TRP CD1  C  Y N 384 
TRP CD2  C  Y N 385 
TRP NE1  N  Y N 386 
TRP CE2  C  Y N 387 
TRP CE3  C  Y N 388 
TRP CZ2  C  Y N 389 
TRP CZ3  C  Y N 390 
TRP CH2  C  Y N 391 
TRP OXT  O  N N 392 
TRP H    H  N N 393 
TRP H2   H  N N 394 
TRP HA   H  N N 395 
TRP HB2  H  N N 396 
TRP HB3  H  N N 397 
TRP HD1  H  N N 398 
TRP HE1  H  N N 399 
TRP HE3  H  N N 400 
TRP HZ2  H  N N 401 
TRP HZ3  H  N N 402 
TRP HH2  H  N N 403 
TRP HXT  H  N N 404 
TYR N    N  N N 405 
TYR CA   C  N S 406 
TYR C    C  N N 407 
TYR O    O  N N 408 
TYR CB   C  N N 409 
TYR CG   C  Y N 410 
TYR CD1  C  Y N 411 
TYR CD2  C  Y N 412 
TYR CE1  C  Y N 413 
TYR CE2  C  Y N 414 
TYR CZ   C  Y N 415 
TYR OH   O  N N 416 
TYR OXT  O  N N 417 
TYR H    H  N N 418 
TYR H2   H  N N 419 
TYR HA   H  N N 420 
TYR HB2  H  N N 421 
TYR HB3  H  N N 422 
TYR HD1  H  N N 423 
TYR HD2  H  N N 424 
TYR HE1  H  N N 425 
TYR HE2  H  N N 426 
TYR HH   H  N N 427 
TYR HXT  H  N N 428 
VAL N    N  N N 429 
VAL CA   C  N S 430 
VAL C    C  N N 431 
VAL O    O  N N 432 
VAL CB   C  N N 433 
VAL CG1  C  N N 434 
VAL CG2  C  N N 435 
VAL OXT  O  N N 436 
VAL H    H  N N 437 
VAL H2   H  N N 438 
VAL HA   H  N N 439 
VAL HB   H  N N 440 
VAL HG11 H  N N 441 
VAL HG12 H  N N 442 
VAL HG13 H  N N 443 
VAL HG21 H  N N 444 
VAL HG22 H  N N 445 
VAL HG23 H  N N 446 
VAL HXT  H  N N 447 
# 
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  
CSO N   CA   sing N N 70  
CSO N   H    sing N N 71  
CSO N   H2   sing N N 72  
CSO CA  CB   sing N N 73  
CSO CA  C    sing N N 74  
CSO CA  HA   sing N N 75  
CSO CB  SG   sing N N 76  
CSO CB  HB2  sing N N 77  
CSO CB  HB3  sing N N 78  
CSO SG  OD   sing N N 79  
CSO C   O    doub N N 80  
CSO C   OXT  sing N N 81  
CSO OXT HXT  sing N N 82  
CSO OD  HD   sing N N 83  
CYS N   CA   sing N N 84  
CYS N   H    sing N N 85  
CYS N   H2   sing N N 86  
CYS CA  C    sing N N 87  
CYS CA  CB   sing N N 88  
CYS CA  HA   sing N N 89  
CYS C   O    doub N N 90  
CYS C   OXT  sing N N 91  
CYS CB  SG   sing N N 92  
CYS CB  HB2  sing N N 93  
CYS CB  HB3  sing N N 94  
CYS SG  HG   sing N N 95  
CYS OXT HXT  sing N N 96  
EDO C1  O1   sing N N 97  
EDO C1  C2   sing N N 98  
EDO C1  H11  sing N N 99  
EDO C1  H12  sing N N 100 
EDO O1  HO1  sing N N 101 
EDO C2  O2   sing N N 102 
EDO C2  H21  sing N N 103 
EDO C2  H22  sing N N 104 
EDO O2  HO2  sing N N 105 
GLN N   CA   sing N N 106 
GLN N   H    sing N N 107 
GLN N   H2   sing N N 108 
GLN CA  C    sing N N 109 
GLN CA  CB   sing N N 110 
GLN CA  HA   sing N N 111 
GLN C   O    doub N N 112 
GLN C   OXT  sing N N 113 
GLN CB  CG   sing N N 114 
GLN CB  HB2  sing N N 115 
GLN CB  HB3  sing N N 116 
GLN CG  CD   sing N N 117 
GLN CG  HG2  sing N N 118 
GLN CG  HG3  sing N N 119 
GLN CD  OE1  doub N N 120 
GLN CD  NE2  sing N N 121 
GLN NE2 HE21 sing N N 122 
GLN NE2 HE22 sing N N 123 
GLN OXT HXT  sing N N 124 
GLU N   CA   sing N N 125 
GLU N   H    sing N N 126 
GLU N   H2   sing N N 127 
GLU CA  C    sing N N 128 
GLU CA  CB   sing N N 129 
GLU CA  HA   sing N N 130 
GLU C   O    doub N N 131 
GLU C   OXT  sing N N 132 
GLU CB  CG   sing N N 133 
GLU CB  HB2  sing N N 134 
GLU CB  HB3  sing N N 135 
GLU CG  CD   sing N N 136 
GLU CG  HG2  sing N N 137 
GLU CG  HG3  sing N N 138 
GLU CD  OE1  doub N N 139 
GLU CD  OE2  sing N N 140 
GLU OE2 HE2  sing N N 141 
GLU OXT HXT  sing N N 142 
GLY N   CA   sing N N 143 
GLY N   H    sing N N 144 
GLY N   H2   sing N N 145 
GLY CA  C    sing N N 146 
GLY CA  HA2  sing N N 147 
GLY CA  HA3  sing N N 148 
GLY C   O    doub N N 149 
GLY C   OXT  sing N N 150 
GLY OXT HXT  sing N N 151 
GOL C1  O1   sing N N 152 
GOL C1  C2   sing N N 153 
GOL C1  H11  sing N N 154 
GOL C1  H12  sing N N 155 
GOL O1  HO1  sing N N 156 
GOL C2  O2   sing N N 157 
GOL C2  C3   sing N N 158 
GOL C2  H2   sing N N 159 
GOL O2  HO2  sing N N 160 
GOL C3  O3   sing N N 161 
GOL C3  H31  sing N N 162 
GOL C3  H32  sing N N 163 
GOL O3  HO3  sing N N 164 
HIS N   CA   sing N N 165 
HIS N   H    sing N N 166 
HIS N   H2   sing N N 167 
HIS CA  C    sing N N 168 
HIS CA  CB   sing N N 169 
HIS CA  HA   sing N N 170 
HIS C   O    doub N N 171 
HIS C   OXT  sing N N 172 
HIS CB  CG   sing N N 173 
HIS CB  HB2  sing N N 174 
HIS CB  HB3  sing N N 175 
HIS CG  ND1  sing Y N 176 
HIS CG  CD2  doub Y N 177 
HIS ND1 CE1  doub Y N 178 
HIS ND1 HD1  sing N N 179 
HIS CD2 NE2  sing Y N 180 
HIS CD2 HD2  sing N N 181 
HIS CE1 NE2  sing Y N 182 
HIS CE1 HE1  sing N N 183 
HIS NE2 HE2  sing N N 184 
HIS OXT HXT  sing N N 185 
HOH O   H1   sing N N 186 
HOH O   H2   sing N N 187 
ILE N   CA   sing N N 188 
ILE N   H    sing N N 189 
ILE N   H2   sing N N 190 
ILE CA  C    sing N N 191 
ILE CA  CB   sing N N 192 
ILE CA  HA   sing N N 193 
ILE C   O    doub N N 194 
ILE C   OXT  sing N N 195 
ILE CB  CG1  sing N N 196 
ILE CB  CG2  sing N N 197 
ILE CB  HB   sing N N 198 
ILE CG1 CD1  sing N N 199 
ILE CG1 HG12 sing N N 200 
ILE CG1 HG13 sing N N 201 
ILE CG2 HG21 sing N N 202 
ILE CG2 HG22 sing N N 203 
ILE CG2 HG23 sing N N 204 
ILE CD1 HD11 sing N N 205 
ILE CD1 HD12 sing N N 206 
ILE CD1 HD13 sing N N 207 
ILE OXT HXT  sing N N 208 
LEU N   CA   sing N N 209 
LEU N   H    sing N N 210 
LEU N   H2   sing N N 211 
LEU CA  C    sing N N 212 
LEU CA  CB   sing N N 213 
LEU CA  HA   sing N N 214 
LEU C   O    doub N N 215 
LEU C   OXT  sing N N 216 
LEU CB  CG   sing N N 217 
LEU CB  HB2  sing N N 218 
LEU CB  HB3  sing N N 219 
LEU CG  CD1  sing N N 220 
LEU CG  CD2  sing N N 221 
LEU CG  HG   sing N N 222 
LEU CD1 HD11 sing N N 223 
LEU CD1 HD12 sing N N 224 
LEU CD1 HD13 sing N N 225 
LEU CD2 HD21 sing N N 226 
LEU CD2 HD22 sing N N 227 
LEU CD2 HD23 sing N N 228 
LEU OXT HXT  sing N N 229 
LYS N   CA   sing N N 230 
LYS N   H    sing N N 231 
LYS N   H2   sing N N 232 
LYS CA  C    sing N N 233 
LYS CA  CB   sing N N 234 
LYS CA  HA   sing N N 235 
LYS C   O    doub N N 236 
LYS C   OXT  sing N N 237 
LYS CB  CG   sing N N 238 
LYS CB  HB2  sing N N 239 
LYS CB  HB3  sing N N 240 
LYS CG  CD   sing N N 241 
LYS CG  HG2  sing N N 242 
LYS CG  HG3  sing N N 243 
LYS CD  CE   sing N N 244 
LYS CD  HD2  sing N N 245 
LYS CD  HD3  sing N N 246 
LYS CE  NZ   sing N N 247 
LYS CE  HE2  sing N N 248 
LYS CE  HE3  sing N N 249 
LYS NZ  HZ1  sing N N 250 
LYS NZ  HZ2  sing N N 251 
LYS NZ  HZ3  sing N N 252 
LYS OXT HXT  sing N N 253 
MET N   CA   sing N N 254 
MET N   H    sing N N 255 
MET N   H2   sing N N 256 
MET CA  C    sing N N 257 
MET CA  CB   sing N N 258 
MET CA  HA   sing N N 259 
MET C   O    doub N N 260 
MET C   OXT  sing N N 261 
MET CB  CG   sing N N 262 
MET CB  HB2  sing N N 263 
MET CB  HB3  sing N N 264 
MET CG  SD   sing N N 265 
MET CG  HG2  sing N N 266 
MET CG  HG3  sing N N 267 
MET SD  CE   sing N N 268 
MET CE  HE1  sing N N 269 
MET CE  HE2  sing N N 270 
MET CE  HE3  sing N N 271 
MET OXT HXT  sing N N 272 
PEG C1  O1   sing N N 273 
PEG C1  C2   sing N N 274 
PEG C1  H11  sing N N 275 
PEG C1  H12  sing N N 276 
PEG O1  HO1  sing N N 277 
PEG C2  O2   sing N N 278 
PEG C2  H21  sing N N 279 
PEG C2  H22  sing N N 280 
PEG O2  C3   sing N N 281 
PEG C3  C4   sing N N 282 
PEG C3  H31  sing N N 283 
PEG C3  H32  sing N N 284 
PEG C4  O4   sing N N 285 
PEG C4  H41  sing N N 286 
PEG C4  H42  sing N N 287 
PEG O4  HO4  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_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       10.18150/HGLASL 
_pdbx_related_exp_data_set.metadata_reference   10.18150/HGLASL 
_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                    9G66 
_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]   0.012826 
_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]   0.010949 
_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]   0.009429 
_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.
;
? 
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   ? 26.99100  -2.66800  47.84600 1.000 61.60000  ? 2   THR A N   1 
ATOM   2    C  CA  . THR A  1 8   ? 28.33200  -2.08500  47.82800 1.000 62.78000  ? 2   THR A CA  1 
ATOM   3    C  C   . THR A  1 8   ? 28.70800  -1.41800  46.47500 1.000 57.17000  ? 2   THR A C   1 
ATOM   4    O  O   . THR A  1 8   ? 29.22600  -0.29700  46.49700 1.000 57.77000  ? 2   THR A O   1 
ATOM   5    C  CB  . THR A  1 8   ? 29.41600  -3.14700  48.25800 1.000 65.58000  ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A  1 8   ? 30.59800  -3.03700  47.44700 1.000 64.81000  ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A  1 8   ? 28.86000  -4.58400  48.22600 1.000 61.63000  ? 2   THR A CG2 1 
ATOM   8    N  N   . PRO A  1 9   ? 28.44200  -2.05600  45.32200 1.000 53.27000  ? 3   PRO A N   1 
ATOM   9    C  CA  . PRO A  1 9   ? 28.67900  -1.37100  44.03900 1.000 47.77000  ? 3   PRO A CA  1 
ATOM   10   C  C   . PRO A  1 9   ? 28.00800  -0.00100  43.97500 1.000 43.57000  ? 3   PRO A C   1 
ATOM   11   O  O   . PRO A  1 9   ? 26.87400  0.18100   44.41900 1.000 46.87000  ? 3   PRO A O   1 
ATOM   12   C  CB  . PRO A  1 9   ? 28.08200  -2.34000  43.01100 1.000 39.32000  ? 3   PRO A CB  1 
ATOM   13   C  CG  . PRO A  1 9   ? 28.34200  -3.66300  43.60800 1.000 48.64000  ? 3   PRO A CG  1 
ATOM   14   C  CD  . PRO A  1 9   ? 28.05500  -3.46100  45.08600 1.000 57.21000  ? 3   PRO A CD  1 
ATOM   15   N  N   . SER A  1 10  ? 28.72500  0.97400   43.41800 1.000 39.82000  ? 4   SER A N   1 
ATOM   16   C  CA  . SER A  1 10  ? 28.22300  2.33400   43.39500 1.000 36.16000  ? 4   SER A CA  1 
ATOM   17   C  C   . SER A  1 10  ? 27.12800  2.49900   42.33800 1.000 38.00000  ? 4   SER A C   1 
ATOM   18   O  O   . SER A  1 10  ? 26.91600  1.64600   41.46500 1.000 31.07000  ? 4   SER A O   1 
ATOM   19   C  CB  . SER A  1 10  ? 29.35700  3.32300   43.13600 1.000 39.01000  ? 4   SER A CB  1 
ATOM   20   O  OG  . SER A  1 10  ? 30.11300  3.53900   44.31600 1.000 46.00000  ? 4   SER A OG  1 
ATOM   21   N  N   . GLU A  1 11  ? 26.43700  3.64000   42.42000 1.000 31.41000  ? 5   GLU A N   1 
ATOM   22   C  CA  . GLU A  1 11  ? 25.42000  4.00000   41.44200 1.000 30.32000  ? 5   GLU A CA  1 
ATOM   23   C  C   . GLU A  1 11  ? 26.08900  4.87100   40.39600 1.000 30.12000  ? 5   GLU A C   1 
ATOM   24   O  O   . GLU A  1 11  ? 26.10000  6.09800   40.49300 1.000 26.83000  ? 5   GLU A O   1 
ATOM   25   C  CB  . GLU A  1 11  ? 24.26100  4.70400   42.13000 1.000 35.88000  ? 5   GLU A CB  1 
ATOM   26   C  CG  . GLU A  1 11  ? 23.55600  3.77800   43.11000 1.000 39.87000  ? 5   GLU A CG  1 
ATOM   27   C  CD  . GLU A  1 11  ? 22.77000  2.68300   42.39200 1.000 42.45000  ? 5   GLU A CD  1 
ATOM   28   O  OE1 . GLU A  1 11  ? 21.79700  3.04100   41.68000 1.000 48.07000  ? 5   GLU A OE1 1 
ATOM   29   O  OE2 . GLU A  1 11  ? 23.12200  1.48400   42.53200 1.000 35.56000  ? 5   GLU A OE2 1 
ATOM   30   N  N   . ASP A  1 12  ? 26.65700  4.23100   39.37700 1.000 20.60000  ? 6   ASP A N   1 
ATOM   31   C  CA  . ASP A  1 12  ? 27.51100  4.90800   38.41200 1.000 21.51000  ? 6   ASP A CA  1 
ATOM   32   C  C   . ASP A  1 12  ? 26.78000  5.03200   37.07800 1.000 19.85000  ? 6   ASP A C   1 
ATOM   33   O  O   . ASP A  1 12  ? 26.46700  4.02200   36.44400 1.000 20.67000  ? 6   ASP A O   1 
ATOM   34   C  CB  . ASP A  1 12  ? 28.83900  4.15600   38.25900 1.000 23.16000  ? 6   ASP A CB  1 
ATOM   35   C  CG  . ASP A  1 12  ? 29.73400  4.31400   39.47900 1.000 24.29000  ? 6   ASP A CG  1 
ATOM   36   O  OD1 . ASP A  1 12  ? 29.74900  5.43200   40.00500 1.000 27.27000  ? 6   ASP A OD1 1 
ATOM   37   O  OD2 . ASP A  1 12  ? 30.39600  3.34800   39.92900 1.000 21.32000  ? 6   ASP A OD2 1 
ATOM   38   N  N   . PHE A  1 13  ? 26.50400  6.27300   36.65300 1.000 19.57000  ? 7   PHE A N   1 
ATOM   39   C  CA  . PHE A  1 13  ? 25.74900  6.51500   35.42900 1.000 18.58000  ? 7   PHE A CA  1 
ATOM   40   C  C   . PHE A  1 13  ? 26.48100  7.44500   34.47300 1.000 19.19000  ? 7   PHE A C   1 
ATOM   41   O  O   . PHE A  1 13  ? 27.24000  8.32300   34.88000 1.000 19.22000  ? 7   PHE A O   1 
ATOM   42   C  CB  . PHE A  1 13  ? 24.35600  7.15100   35.72200 1.000 21.40000  ? 7   PHE A CB  1 
ATOM   43   C  CG  . PHE A  1 13  ? 23.45300  6.23600   36.45600 1.000 21.30000  ? 7   PHE A CG  1 
ATOM   44   C  CD1 . PHE A  1 13  ? 23.58100  6.07000   37.82000 1.000 26.01000  ? 7   PHE A CD1 1 
ATOM   45   C  CD2 . PHE A  1 13  ? 22.50300  5.48300   35.77100 1.000 25.59000  ? 7   PHE A CD2 1 
ATOM   46   C  CE1 . PHE A  1 13  ? 22.74200  5.17500   38.51500 1.000 30.33000  ? 7   PHE A CE1 1 
ATOM   47   C  CE2 . PHE A  1 13  ? 21.66200  4.58200   36.45400 1.000 25.61000  ? 7   PHE A CE2 1 
ATOM   48   C  CZ  . PHE A  1 13  ? 21.79000  4.42800   37.82100 1.000 29.65000  ? 7   PHE A CZ  1 
ATOM   49   N  N   . VAL A  1 14  ? 26.21000  7.25900   33.19900 1.000 17.29000  ? 8   VAL A N   1 
ATOM   50   C  CA  . VAL A  1 14  ? 26.40900  8.30300   32.20300 1.000 15.92000  ? 8   VAL A CA  1 
ATOM   51   C  C   . VAL A  1 14  ? 25.02400  8.83200   31.84400 1.000 16.92000  ? 8   VAL A C   1 
ATOM   52   O  O   . VAL A  1 14  ? 24.07000  8.06400   31.72900 1.000 16.33000  ? 8   VAL A O   1 
ATOM   53   C  CB  . VAL A  1 14  ? 27.16300  7.78100   30.96500 1.000 18.21000  ? 8   VAL A CB  1 
ATOM   54   C  CG1 . VAL A  1 14  ? 26.46900  6.55300   30.38000 1.000 18.95000  ? 8   VAL A CG1 1 
ATOM   55   C  CG2 . VAL A  1 14  ? 27.29200  8.86100   29.93200 1.000 20.34000  ? 8   VAL A CG2 1 
ATOM   56   N  N   . VAL A  1 15  ? 24.91300  10.13800  31.68800 1.000 14.67000  ? 9   VAL A N   1 
ATOM   57   C  CA  . VAL A  1 15  ? 23.62200  10.82500  31.63400 1.000 18.12000  ? 9   VAL A CA  1 
ATOM   58   C  C   . VAL A  1 15  ? 23.61500  11.75900  30.42800 1.000 19.85000  ? 9   VAL A C   1 
ATOM   59   O  O   . VAL A  1 15  ? 24.55600  12.53800  30.23000 1.000 20.00000  ? 9   VAL A O   1 
ATOM   60   C  CB  . VAL A  1 15  ? 23.35700  11.62000  32.92500 1.000 19.15000  ? 9   VAL A CB  1 
ATOM   61   C  CG1 . VAL A  1 15  ? 22.02500  12.39100  32.81800 1.000 20.96000  ? 9   VAL A CG1 1 
ATOM   62   C  CG2 . VAL A  1 15  ? 23.33700  10.68100  34.12300 1.000 16.39000  ? 9   VAL A CG2 1 
ATOM   63   N  N   . THR A  1 16  ? 22.55500  11.70100  29.62500 1.000 17.10000  ? 10  THR A N   1 
ATOM   64   C  CA  . THR A  1 16  ? 22.42600  12.65300  28.53000 1.000 17.03000  ? 10  THR A CA  1 
ATOM   65   C  C   . THR A  1 16  ? 21.35100  13.67200  28.87100 1.000 17.84000  ? 10  THR A C   1 
ATOM   66   O  O   . THR A  1 16  ? 20.40200  13.38200  29.60600 1.000 19.14000  ? 10  THR A O   1 
ATOM   67   C  CB  . THR A  1 16  ? 22.10600  11.95500  27.20400 1.000 19.12000  ? 10  THR A CB  1 
ATOM   68   O  OG1 . THR A  1 16  ? 20.78900  11.38100  27.26200 1.000 19.13000  ? 10  THR A OG1 1 
ATOM   69   C  CG2 . THR A  1 16  ? 23.14500  10.86100  26.90100 1.000 19.39000  ? 10  THR A CG2 1 
ATOM   70   N  N   . ASP A  1 17  ? 21.49900  14.87200  28.33800 1.000 15.55000  ? 11  ASP A N   1 
ATOM   71   C  CA  . ASP A  1 17  ? 20.58100  15.93600  28.71200 1.000 16.89000  ? 11  ASP A CA  1 
ATOM   72   C  C   . ASP A  1 17  ? 20.16500  16.68400  27.46900 1.000 17.33000  ? 11  ASP A C   1 
ATOM   73   O  O   . ASP A  1 17  ? 20.86500  16.69600  26.46000 1.000 17.68000  ? 11  ASP A O   1 
ATOM   74   C  CB  . ASP A  1 17  ? 21.18200  16.94500  29.71500 1.000 18.02000  ? 11  ASP A CB  1 
ATOM   75   C  CG  . ASP A  1 17  ? 22.24300  17.84600  29.08400 1.000 22.52000  ? 11  ASP A CG  1 
ATOM   76   O  OD1 . ASP A  1 17  ? 23.41200  17.39500  28.95300 1.000 21.50000  ? 11  ASP A OD1 1 
ATOM   77   O  OD2 . ASP A  1 17  ? 21.93000  19.00900  28.68900 1.000 21.99000  ? 11  ASP A OD2 1 
ATOM   78   N  N   . ARG A  1 18  ? 19.03300  17.36000  27.58500 1.000 16.23000  ? 12  ARG A N   1 
ATOM   79   C  CA  . ARG A  1 18  ? 18.55900  18.29100  26.57600 1.000 17.22000  ? 12  ARG A CA  1 
ATOM   80   C  C   . ARG A  1 18  ? 18.37700  19.62100  27.29300 1.000 18.59000  ? 12  ARG A C   1 
ATOM   81   O  O   . ARG A  1 18  ? 17.48500  19.75600  28.13700 1.000 18.70000  ? 12  ARG A O   1 
ATOM   82   C  CB  . ARG A  1 18  ? 17.25200  17.78000  25.96600 1.000 15.91000  ? 12  ARG A CB  1 
ATOM   83   C  CG  . ARG A  1 18  ? 16.67600  18.61100  24.77900 1.000 19.92000  ? 12  ARG A CG  1 
ATOM   84   C  CD  . ARG A  1 18  ? 15.50300  17.82300  24.12000 1.000 18.65000  ? 12  ARG A CD  1 
ATOM   85   N  NE  . ARG A  1 18  ? 15.98200  16.57600  23.52300 1.000 16.03000  ? 12  ARG A NE  1 
ATOM   86   C  CZ  . ARG A  1 18  ? 16.43700  16.47100  22.28000 1.000 18.59000  ? 12  ARG A CZ  1 
ATOM   87   N  NH1 . ARG A  1 18  ? 16.40000  17.50500  21.44800 1.000 19.54000  ? 12  ARG A NH1 1 
ATOM   88   N  NH2 . ARG A  1 18  ? 16.98600  15.31400  21.87500 1.000 18.60000  ? 12  ARG A NH2 1 
ATOM   89   N  N   . GLY A  1 19  ? 19.23600  20.58200  27.00400 1.000 19.44000  ? 13  GLY A N   1 
ATOM   90   C  CA  . GLY A  1 19  ? 19.11400  21.86900  27.68600 1.000 22.19000  ? 13  GLY A CA  1 
ATOM   91   C  C   . GLY A  1 19  ? 19.24600  21.75700  29.19100 1.000 19.17000  ? 13  GLY A C   1 
ATOM   92   O  O   . GLY A  1 19  ? 18.62100  22.52900  29.92200 1.000 19.85000  ? 13  GLY A O   1 
ATOM   93   N  N   . GLY A  1 20  ? 20.02700  20.80300  29.67600 1.000 20.59000  ? 14  GLY A N   1 
ATOM   94   C  CA  . GLY A  1 20  ? 20.19700  20.62500  31.10400 1.000 22.49000  ? 14  GLY A CA  1 
ATOM   95   C  C   . GLY A  1 20  ? 19.19100  19.69500  31.73200 1.000 21.32000  ? 14  GLY A C   1 
ATOM   96   O  O   . GLY A  1 20  ? 19.37300  19.28600  32.88900 1.000 21.83000  ? 14  GLY A O   1 
ATOM   97   N  N   . ILE A  1 21  ? 18.14300  19.33000  30.99700 1.000 16.51000  ? 15  ILE A N   1 
ATOM   98   C  CA  . ILE A  1 21  ? 17.10400  18.44700  31.49100 1.000 19.76000  ? 15  ILE A CA  1 
ATOM   99   C  C   . ILE A  1 21  ? 17.50300  17.01200  31.17300 1.000 17.45000  ? 15  ILE A C   1 
ATOM   100  O  O   . ILE A  1 21  ? 17.85100  16.69700  30.02900 1.000 17.20000  ? 15  ILE A O   1 
ATOM   101  C  CB  . ILE A  1 21  ? 15.75300  18.80100  30.84000 1.000 15.89000  ? 15  ILE A CB  1 
ATOM   102  C  CG1 . ILE A  1 21  ? 15.46700  20.29600  31.00800 1.000 17.25000  ? 15  ILE A CG1 1 
ATOM   103  C  CG2 . ILE A  1 21  ? 14.67300  17.86200  31.37000 1.000 16.53000  ? 15  ILE A CG2 1 
ATOM   104  C  CD1 . ILE A  1 21  ? 14.35800  20.81000  30.04900 1.000 18.66000  ? 15  ILE A CD1 1 
ATOM   105  N  N   . VAL A  1 22  ? 17.45000  16.13200  32.17700 1.000 17.15000  ? 16  VAL A N   1 
ATOM   106  C  CA  . VAL A  1 22  ? 17.83200  14.73700  31.95500 1.000 17.07000  ? 16  VAL A CA  1 
ATOM   107  C  C   . VAL A  1 22  ? 16.98000  14.10600  30.86500 1.000 16.38000  ? 16  VAL A C   1 
ATOM   108  O  O   . VAL A  1 22  ? 15.75300  14.11700  30.92800 1.000 19.34000  ? 16  VAL A O   1 
ATOM   109  C  CB  . VAL A  1 22  ? 17.73300  13.93500  33.26200 1.000 15.75000  ? 16  VAL A CB  1 
ATOM   110  C  CG1 . VAL A  1 22  ? 18.01600  12.47400  32.97400 1.000 21.17000  ? 16  VAL A CG1 1 
ATOM   111  C  CG2 . VAL A  1 22  ? 18.79000  14.46500  34.25400 1.000 19.70000  ? 16  VAL A CG2 1 
ATOM   112  N  N   . GLU A  1 23  ? 17.63700  13.50800  29.88100 1.000 15.18000  ? 17  GLU A N   1 
ATOM   113  C  CA  . GLU A  1 23  ? 16.95000  12.75700  28.84200 1.000 16.56000  ? 17  GLU A CA  1 
ATOM   114  C  C   . GLU A  1 23  ? 16.99700  11.26800  29.18300 1.000 17.24000  ? 17  GLU A C   1 
ATOM   115  O  O   . GLU A  1 23  ? 15.98100  10.69100  29.61400 1.000 15.48000  ? 17  GLU A O   1 
ATOM   116  C  CB  . GLU A  1 23  ? 17.59400  13.07000  27.47900 1.000 16.32000  ? 17  GLU A CB  1 
ATOM   117  C  CG  . GLU A  1 23  ? 16.91600  12.40600  26.29600 1.000 16.06000  ? 17  GLU A CG  1 
ATOM   118  C  CD  . GLU A  1 23  ? 15.97500  13.34400  25.56900 1.000 18.95000  ? 17  GLU A CD  1 
ATOM   119  O  OE1 . GLU A  1 23  ? 16.50600  14.31500  24.95200 1.000 18.31000  ? 17  GLU A OE1 1 
ATOM   120  O  OE2 . GLU A  1 23  ? 14.72700  13.10500  25.65400 1.000 18.85000  ? 17  GLU A OE2 1 
ATOM   121  N  N   . ASN A  1 24  ? 18.16800  10.64000  29.00700 1.000 15.95000  ? 18  ASN A N   1 
ATOM   122  C  CA  . ASN A  1 24  ? 18.38200  9.22700   29.32300 1.000 15.40000  ? 18  ASN A CA  1 
ATOM   123  C  C   . ASN A  1 24  ? 19.50000  9.10000   30.34900 1.000 18.15000  ? 18  ASN A C   1 
ATOM   124  O  O   . ASN A  1 24  ? 20.38100  9.96600   30.44900 1.000 17.54000  ? 18  ASN A O   1 
ATOM   125  C  CB  . ASN A  1 24  ? 18.76400  8.39600   28.07500 1.000 14.96000  ? 18  ASN A CB  1 
ATOM   126  C  CG  . ASN A  1 24  ? 17.77400  8.58600   26.93200 1.000 15.84000  ? 18  ASN A CG  1 
ATOM   127  O  OD1 . ASN A  1 24  ? 16.57800  8.63300   27.15700 1.000 14.99000  ? 18  ASN A OD1 1 
ATOM   128  N  ND2 . ASN A  1 24  ? 18.27300  8.68900   25.71000 1.000 18.04000  ? 18  ASN A ND2 1 
ATOM   129  N  N   . SER A  1 25  ? 19.47700  8.01700   31.11400 1.000 15.47000  ? 19  SER A N   1 
ATOM   130  C  CA  . SER A  1 25  ? 20.64600  7.69000   31.91000 1.000 15.50000  ? 19  SER A CA  1 
ATOM   131  C  C   . SER A  1 25  ? 20.93200  6.20600   31.76000 1.000 16.07000  ? 19  SER A C   1 
ATOM   132  O  O   . SER A  1 25  ? 20.01200  5.39200   31.54100 1.000 16.31000  ? 19  SER A O   1 
ATOM   133  C  CB  . SER A  1 25  ? 20.47000  8.08500   33.37000 1.000 15.63000  ? 19  SER A CB  1 
ATOM   134  O  OG  . SER A  1 25  ? 19.46100  7.34700   34.00500 1.000 18.89000  ? 19  SER A OG  1 
ATOM   135  N  N   . HIS A  1 26  ? 22.21900  5.86600   31.88000 1.000 16.14000  ? 20  HIS A N   1 
ATOM   136  C  CA  . HIS A  1 26  ? 22.72300  4.52900   31.55000 1.000 17.29000  ? 20  HIS A CA  1 
ATOM   137  C  C   . HIS A  1 26  ? 23.67100  4.06900   32.65100 1.000 15.57000  ? 20  HIS A C   1 
ATOM   138  O  O   . HIS A  1 26  ? 24.59700  4.80300   33.01700 1.000 17.09000  ? 20  HIS A O   1 
ATOM   139  C  CB  . HIS A  1 26  ? 23.48100  4.53800   30.21400 1.000 16.92000  ? 20  HIS A CB  1 
ATOM   140  C  CG  . HIS A  1 26  ? 22.74000  5.18800   29.09200 1.000 15.62000  ? 20  HIS A CG  1 
ATOM   141  N  ND1 . HIS A  1 26  ? 22.09200  4.46200   28.11600 1.000 14.28000  ? 20  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A  1 26  ? 22.59700  6.50000   28.75200 1.000 14.59000  ? 20  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A  1 26  ? 21.55200  5.30000   27.24200 1.000 17.59000  ? 20  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A  1 26  ? 21.83400  6.54300   27.61000 1.000 17.05000  ? 20  HIS A NE2 1 
ATOM   145  N  N   . ARG A  1 27  ? 23.41800  2.87800   33.20200 1.000 15.91000  ? 21  ARG A N   1 
ATOM   146  C  CA  . ARG A  1 27  ? 24.25400  2.36800   34.27600 1.000 17.29000  ? 21  ARG A CA  1 
ATOM   147  C  C   . ARG A  1 27  ? 25.54300  1.80900   33.68500 1.000 15.38000  ? 21  ARG A C   1 
ATOM   148  O  O   . ARG A  1 27  ? 25.51400  1.16600   32.64400 1.000 16.81000  ? 21  ARG A O   1 
ATOM   149  C  CB  . ARG A  1 27  ? 23.50200  1.27700   35.04400 1.000 19.35000  ? 21  ARG A CB  1 
ATOM   150  C  CG  . ARG A  1 27  ? 24.29900  0.73800   36.22700 1.000 25.04000  ? 21  ARG A CG  1 
ATOM   151  C  CD  . ARG A  1 27  ? 23.51400  -0.28800  37.05200 1.000 27.35000  ? 21  ARG A CD  1 
ATOM   152  N  NE  . ARG A  1 27  ? 22.35300  0.33100   37.69000 1.000 33.85000  ? 21  ARG A NE  1 
ATOM   153  C  CZ  . ARG A  1 27  ? 22.37300  0.92000   38.87800 1.000 32.59000  ? 21  ARG A CZ  1 
ATOM   154  N  NH1 . ARG A  1 27  ? 23.48800  1.00400   39.59100 1.000 34.07000  ? 21  ARG A NH1 1 
ATOM   155  N  NH2 . ARG A  1 27  ? 21.24800  1.44300   39.36300 1.000 28.02000  ? 21  ARG A NH2 1 
ATOM   156  N  N   . VAL A  1 28  ? 26.67800  2.06100   34.34500 1.000 13.24000  ? 22  VAL A N   1 
ATOM   157  C  CA  . VAL A  1 28  ? 28.00200  1.72300   33.81600 1.000 14.75000  ? 22  VAL A CA  1 
ATOM   158  C  C   . VAL A  1 28  ? 28.64500  0.76900   34.79000 1.000 17.64000  ? 22  VAL A C   1 
ATOM   159  O  O   . VAL A  1 28  ? 28.67400  1.04400   35.99400 1.000 18.38000  ? 22  VAL A O   1 
ATOM   160  C  CB  . VAL A  1 28  ? 28.91000  2.95700   33.65300 1.000 16.93000  ? 22  VAL A CB  1 
ATOM   161  C  CG1 . VAL A  1 28  ? 30.32100  2.53000   33.18700 1.000 19.09000  ? 22  VAL A CG1 1 
ATOM   162  C  CG2 . VAL A  1 28  ? 28.28800  3.96200   32.68700 1.000 19.27000  ? 22  VAL A CG2 1 
ATOM   163  N  N   . HIS A  1 29  ? 29.14300  -0.34800  34.26900 1.000 13.98000  ? 23  HIS A N   1 
ATOM   164  C  CA  . HIS A  1 29  ? 30.01400  -1.25600  35.00300 1.000 16.35000  ? 23  HIS A CA  1 
ATOM   165  C  C   . HIS A  1 29  ? 31.39400  -1.28100  34.36700 1.000 14.91000  ? 23  HIS A C   1 
ATOM   166  O  O   . HIS A  1 29  ? 31.52100  -1.31700  33.14100 1.000 14.86000  ? 23  HIS A O   1 
ATOM   167  C  CB  . HIS A  1 29  ? 29.42800  -2.64800  34.98500 1.000 14.41000  ? 23  HIS A CB  1 
ATOM   168  C  CG  . HIS A  1 29  ? 28.01100  -2.67300  35.40800 1.000 14.13000  ? 23  HIS A CG  1 
ATOM   169  N  ND1 . HIS A  1 29  ? 27.63900  -2.65900  36.73300 1.000 16.06000  ? 23  HIS A ND1 1 
ATOM   170  C  CD2 . HIS A  1 29  ? 26.86600  -2.78500  34.68800 1.000 14.89000  ? 23  HIS A CD2 1 
ATOM   171  C  CE1 . HIS A  1 29  ? 26.32100  -2.75000  36.81400 1.000 21.38000  ? 23  HIS A CE1 1 
ATOM   172  N  NE2 . HIS A  1 29  ? 25.82800  -2.82600  35.58800 1.000 18.77000  ? 23  HIS A NE2 1 
ATOM   173  N  N   . ALA A  1 30  ? 32.42800  -1.25200  35.19400 1.000 17.20000  ? 24  ALA A N   1 
ATOM   174  C  CA  . ALA A  1 30  ? 33.78200  -1.25700  34.64500 1.000 17.40000  ? 24  ALA A CA  1 
ATOM   175  C  C   . ALA A  1 30  ? 34.72600  -1.90100  35.64100 1.000 17.80000  ? 24  ALA A C   1 
ATOM   176  O  O   . ALA A  1 30  ? 34.53100  -1.79300  36.84900 1.000 17.73000  ? 24  ALA A O   1 
ATOM   177  C  CB  . ALA A  1 30  ? 34.27000  0.15600   34.30900 1.000 16.49000  ? 24  ALA A CB  1 
ATOM   178  N  N   . ALA A  1 31  ? 35.73400  -2.59900  35.10900 1.000 17.00000  ? 25  ALA A N   1 
ATOM   179  C  CA  . ALA A  1 31  ? 36.79900  -3.22300  35.89000 1.000 18.43000  ? 25  ALA A CA  1 
ATOM   180  C  C   . ALA A  1 31  ? 38.12700  -2.78200  35.29100 1.000 19.12000  ? 25  ALA A C   1 
ATOM   181  O  O   . ALA A  1 31  ? 38.28600  -2.77200  34.06600 1.000 18.40000  ? 25  ALA A O   1 
ATOM   182  C  CB  . ALA A  1 31  ? 36.69600  -4.75700  35.87400 1.000 16.81000  ? 25  ALA A CB  1 
ATOM   183  N  N   . VAL A  1 32  ? 39.04700  -2.35100  36.14300 1.000 19.67000  ? 26  VAL A N   1 
ATOM   184  C  CA  . VAL A  1 32  ? 40.42900  -2.09800  35.75500 1.000 21.71000  ? 26  VAL A CA  1 
ATOM   185  C  C   . VAL A  1 32  ? 41.28100  -3.04400  36.59800 1.000 20.26000  ? 26  VAL A C   1 
ATOM   186  O  O   . VAL A  1 32  ? 41.24700  -2.98800  37.83500 1.000 23.06000  ? 26  VAL A O   1 
ATOM   187  C  CB  . VAL A  1 32  ? 40.83600  -0.62100  35.95700 1.000 20.61000  ? 26  VAL A CB  1 
ATOM   188  C  CG1 . VAL A  1 32  ? 42.23100  -0.36000  35.42400 1.000 22.02000  ? 26  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A  1 32  ? 39.86600  0.33800   35.25600 1.000 22.96000  ? 26  VAL A CG2 1 
ATOM   190  N  N   . VAL A  1 33  ? 42.04600  -3.91800  35.93800 1.000 21.80000  ? 27  VAL A N   1 
ATOM   191  C  CA  . VAL A  1 33  ? 42.73500  -5.00700  36.61900 1.000 22.11000  ? 27  VAL A CA  1 
ATOM   192  C  C   . VAL A  1 33  ? 44.19800  -5.01300  36.20800 1.000 23.86000  ? 27  VAL A C   1 
ATOM   193  O  O   . VAL A  1 33  ? 44.57200  -4.49700  35.15200 1.000 23.40000  ? 27  VAL A O   1 
ATOM   194  C  CB  . VAL A  1 33  ? 42.11400  -6.37900  36.32000 1.000 20.56000  ? 27  VAL A CB  1 
ATOM   195  C  CG1 . VAL A  1 33  ? 40.61600  -6.37700  36.69000 1.000 23.94000  ? 27  VAL A CG1 1 
ATOM   196  C  CG2 . VAL A  1 33  ? 42.34300  -6.77300  34.85300 1.000 19.74000  ? 27  VAL A CG2 1 
ATOM   197  N  N   . ASP A  1 34  ? 45.02900  -5.60000  37.06300 1.000 24.82000  ? 28  ASP A N   1 
ATOM   198  C  CA  . ASP A  1 34  ? 46.44200  -5.72100  36.72700 1.000 26.64000  ? 28  ASP A CA  1 
ATOM   199  C  C   . ASP A  1 34  ? 46.63200  -7.01300  35.92500 1.000 26.16000  ? 28  ASP A C   1 
ATOM   200  O  O   . ASP A  1 34  ? 45.66300  -7.65600  35.53600 1.000 26.61000  ? 28  ASP A O   1 
ATOM   201  C  CB  . ASP A  1 34  ? 47.31000  -5.63100  37.98900 1.000 27.87000  ? 28  ASP A CB  1 
ATOM   202  C  CG  . ASP A  1 34  ? 47.22700  -6.85700  38.89500 1.000 29.27000  ? 28  ASP A CG  1 
ATOM   203  O  OD1 . ASP A  1 34  ? 46.59200  -7.88800  38.54500 1.000 29.47000  ? 28  ASP A OD1 1 
ATOM   204  O  OD2 . ASP A  1 34  ? 47.84700  -6.78400  39.99500 1.000 30.53000  ? 28  ASP A OD2 1 
ATOM   205  N  N   . ALA A  1 35  ? 47.88400  -7.40100  35.67000 1.000 28.08000  ? 29  ALA A N   1 
ATOM   206  C  CA  . ALA A  1 35  ? 48.20100  -8.55700  34.82500 1.000 24.39000  ? 29  ALA A CA  1 
ATOM   207  C  C   . ALA A  1 35  ? 47.77600  -9.89500  35.43200 1.000 30.87000  ? 29  ALA A C   1 
ATOM   208  O  O   . ALA A  1 35  ? 47.57000  -10.86700 34.69000 1.000 31.62000  ? 29  ALA A O   1 
ATOM   209  C  CB  . ALA A  1 35  ? 49.70700  -8.55100  34.51300 1.000 28.98000  ? 29  ALA A CB  1 
ATOM   210  N  N   . LYS A  1 36  ? 47.64900  -9.98600  36.74900 1.000 27.58000  ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A  1 36  ? 47.12000  -11.18700 37.38200 1.000 26.08000  ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A  1 36  ? 45.59700  -11.14300 37.54800 1.000 28.50000  ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A  1 36  ? 45.01200  -12.10700 38.05400 1.000 27.81000  ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A  1 36  ? 47.77500  -11.38100 38.75100 1.000 27.75000  ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A  1 36  ? 49.30700  -11.37100 38.73800 1.000 34.07000  ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A  1 36  ? 49.89700  -12.75900 38.56100 1.000 38.26000  ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A  1 36  ? 51.43200  -12.72600 38.54100 1.000 47.04000  ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A  1 36  ? 52.02900  -12.44100 39.87800 1.000 48.23000  ? 30  LYS A NZ  1 
ATOM   219  N  N   . GLY A  1 37  ? 44.94600  -10.05800 37.13400 1.000 27.60000  ? 31  GLY A N   1 
ATOM   220  C  CA  . GLY A  1 37  ? 43.52600  -9.89900  37.32300 1.000 24.12000  ? 31  GLY A CA  1 
ATOM   221  C  C   . GLY A  1 37  ? 43.12100  -9.21400  38.60300 1.000 26.38000  ? 31  GLY A C   1 
ATOM   222  O  O   . GLY A  1 37  ? 41.91500  -9.10400  38.87300 1.000 25.61000  ? 31  GLY A O   1 
ATOM   223  N  N   . ARG A  1 38  ? 44.07600  -8.72700  39.39000 1.000 24.96000  ? 32  ARG A N   1 
ATOM   224  C  CA  . ARG A  1 38  ? 43.72800  -8.04600  40.62300 1.000 26.32000  ? 32  ARG A CA  1 
ATOM   225  C  C   . ARG A  1 38  ? 42.96400  -6.77100  40.31100 1.000 26.50000  ? 32  ARG A C   1 
ATOM   226  O  O   . ARG A  1 38  ? 43.32800  -6.00500  39.41700 1.000 28.30000  ? 32  ARG A O   1 
ATOM   227  C  CB  . ARG A  1 38  ? 44.97900  -7.72300  41.43200 1.000 28.09000  ? 32  ARG A CB  1 
ATOM   228  C  CG  . ARG A  1 38  ? 44.69800  -7.10300  42.78700 1.000 37.17000  ? 32  ARG A CG  1 
ATOM   229  C  CD  . ARG A  1 38  ? 45.99000  -6.76100  43.53000 1.000 43.94000  ? 32  ARG A CD  1 
ATOM   230  N  NE  . ARG A  1 38  ? 46.62200  -5.54800  43.01000 1.000 52.80000  ? 32  ARG A NE  1 
ATOM   231  C  CZ  . ARG A  1 38  ? 47.79700  -5.07300  43.41400 1.000 57.73000  ? 32  ARG A CZ  1 
ATOM   232  N  NH1 . ARG A  1 38  ? 48.52500  -5.70600  44.32400 1.000 59.68000  ? 32  ARG A NH1 1 
ATOM   233  N  NH2 . ARG A  1 38  ? 48.25100  -3.93100  42.89300 1.000 57.64000  ? 32  ARG A NH2 1 
ATOM   234  N  N   . LEU A  1 39  ? 41.89100  -6.54200  41.04000 1.000 23.08000  ? 33  LEU A N   1 
ATOM   235  C  CA  . LEU A  1 39  ? 41.05100  -5.39800  40.74300 1.000 26.53000  ? 33  LEU A CA  1 
ATOM   236  C  C   . LEU A  1 39  ? 41.73200  -4.12500  41.24400 1.000 27.47000  ? 33  LEU A C   1 
ATOM   237  O  O   . LEU A  1 39  ? 42.06600  -4.01900  42.42600 1.000 25.92000  ? 33  LEU A O   1 
ATOM   238  C  CB  . LEU A  1 39  ? 39.68000  -5.59300  41.38800 1.000 29.06000  ? 33  LEU A CB  1 
ATOM   239  C  CG  . LEU A  1 39  ? 38.60400  -4.65400  40.91100 1.000 32.36000  ? 33  LEU A CG  1 
ATOM   240  C  CD1 . LEU A  1 39  ? 38.41800  -4.84800  39.41700 1.000 26.31000  ? 33  LEU A CD1 1 
ATOM   241  C  CD2 . LEU A  1 39  ? 37.29100  -4.88200  41.70200 1.000 34.74000  ? 33  LEU A CD2 1 
ATOM   242  N  N   . LEU A  1 40  ? 41.95200  -3.16300  40.35600 1.000 20.97000  ? 34  LEU A N   1 
ATOM   243  C  CA  . LEU A  1 40  ? 42.57100  -1.90800  40.78100 1.000 28.17000  ? 34  LEU A CA  1 
ATOM   244  C  C   . LEU A  1 40  ? 41.56900  -0.76200  40.91100 1.000 26.42000  ? 34  LEU A C   1 
ATOM   245  O  O   . LEU A  1 40  ? 41.63800  -0.01000  41.88000 1.000 26.41000  ? 34  LEU A O   1 
ATOM   246  C  CB  . LEU A  1 40  ? 43.68800  -1.49000  39.81600 1.000 23.45000  ? 34  LEU A CB  1 
ATOM   247  C  CG  . LEU A  1 40  ? 44.70800  -2.57600  39.48800 1.000 24.77000  ? 34  LEU A CG  1 
ATOM   248  C  CD1 . LEU A  1 40  ? 45.65800  -2.08300  38.40700 1.000 28.38000  ? 34  LEU A CD1 1 
ATOM   249  C  CD2 . LEU A  1 40  ? 45.48000  -2.93800  40.73000 1.000 32.53000  ? 34  LEU A CD2 1 
ATOM   250  N  N   . TYR A  1 41  ? 40.66700  -0.60200  39.94300 1.000 21.34000  ? 35  TYR A N   1 
ATOM   251  C  CA  . TYR A  1 41  ? 39.60900  0.40000   39.99800 1.000 26.89000  ? 35  TYR A CA  1 
ATOM   252  C  C   . TYR A  1 41  ? 38.31300  -0.20400  39.48600 1.000 21.12000  ? 35  TYR A C   1 
ATOM   253  O  O   . TYR A  1 41  ? 38.32000  -1.18800  38.75300 1.000 21.65000  ? 35  TYR A O   1 
ATOM   254  C  CB  . TYR A  1 41  ? 39.95100  1.64100   39.17200 1.000 21.50000  ? 35  TYR A CB  1 
ATOM   255  C  CG  . TYR A  1 41  ? 41.26600  2.22900   39.59600 1.000 28.10000  ? 35  TYR A CG  1 
ATOM   256  C  CD1 . TYR A  1 41  ? 41.33200  3.15000   40.62100 1.000 29.44000  ? 35  TYR A CD1 1 
ATOM   257  C  CD2 . TYR A  1 41  ? 42.44600  1.81800   39.00000 1.000 29.29000  ? 35  TYR A CD2 1 
ATOM   258  C  CE1 . TYR A  1 41  ? 42.52400  3.66100   41.03100 1.000 31.97000  ? 35  TYR A CE1 1 
ATOM   259  C  CE2 . TYR A  1 41  ? 43.64200  2.31900   39.38800 1.000 27.89000  ? 35  TYR A CE2 1 
ATOM   260  C  CZ  . TYR A  1 41  ? 43.69000  3.25500   40.40100 1.000 31.63000  ? 35  TYR A CZ  1 
ATOM   261  O  OH  . TYR A  1 41  ? 44.91200  3.75100   40.80000 1.000 36.04000  ? 35  TYR A OH  1 
ATOM   262  N  N   . ALA A  1 42  ? 37.18900  0.42600   39.83100 1.000 21.98000  ? 36  ALA A N   1 
ATOM   263  C  CA  . ALA A  1 42  ? 35.92100  -0.11000  39.36200 1.000 20.90000  ? 36  ALA A CA  1 
ATOM   264  C  C   . ALA A  1 42  ? 34.87700  0.98200   39.21200 1.000 22.73000  ? 36  ALA A C   1 
ATOM   265  O  O   . ALA A  1 42  ? 34.91300  2.01500   39.90200 1.000 18.76000  ? 36  ALA A O   1 
ATOM   266  C  CB  . ALA A  1 42  ? 35.37400  -1.18600  40.31200 1.000 22.82000  ? 36  ALA A CB  1 
ATOM   267  N  N   . LEU A  1 43  ? 33.92800  0.71300   38.30600 1.000 19.21000  ? 37  LEU A N   1 
ATOM   268  C  CA  . LEU A  1 43  ? 32.64200  1.39200   38.24200 1.000 19.55000  ? 37  LEU A CA  1 
ATOM   269  C  C   . LEU A  1 43  ? 31.53900  0.34600   38.34300 1.000 20.52000  ? 37  LEU A C   1 
ATOM   270  O  O   . LEU A  1 43  ? 31.69000  -0.79500  37.86400 1.000 16.43000  ? 37  LEU A O   1 
ATOM   271  C  CB  . LEU A  1 43  ? 32.45900  2.18400   36.94700 1.000 18.14000  ? 37  LEU A CB  1 
ATOM   272  C  CG  . LEU A  1 43  ? 33.34700  3.40000   36.67800 1.000 19.53000  ? 37  LEU A CG  1 
ATOM   273  C  CD1 . LEU A  1 43  ? 32.94100  4.03300   35.36500 1.000 19.73000  ? 37  LEU A CD1 1 
ATOM   274  C  CD2 . LEU A  1 43  ? 33.25200  4.40500   37.85400 1.000 19.93000  ? 37  LEU A CD2 1 
ATOM   275  N  N   . GLY A  1 44  ? 30.43700  0.72000   39.00800 1.000 19.43000  ? 38  GLY A N   1 
ATOM   276  C  CA  . GLY A  1 44  ? 29.30000  -0.18800  39.09000 1.000 20.36000  ? 38  GLY A CA  1 
ATOM   277  C  C   . GLY A  1 44  ? 29.67000  -1.48400  39.78200 1.000 22.64000  ? 38  GLY A C   1 
ATOM   278  O  O   . GLY A  1 44  ? 30.34200  -1.49700  40.82400 1.000 22.90000  ? 38  GLY A O   1 
ATOM   279  N  N   . ASN A  1 45  ? 29.23000  -2.60200  39.19300 1.000 16.61000  ? 39  ASN A N   1 
ATOM   280  C  CA  . ASN A  1 45  ? 29.54800  -3.94000  39.69100 1.000 20.65000  ? 39  ASN A CA  1 
ATOM   281  C  C   . ASN A  1 45  ? 30.65500  -4.51500  38.83300 1.000 20.79000  ? 39  ASN A C   1 
ATOM   282  O  O   . ASN A  1 45  ? 30.37600  -4.99500  37.72100 1.000 17.57000  ? 39  ASN A O   1 
ATOM   283  C  CB  . ASN A  1 45  ? 28.31300  -4.85000  39.63700 1.000 19.04000  ? 39  ASN A CB  1 
ATOM   284  C  CG  . ASN A  1 45  ? 28.61600  -6.26800  40.12400 1.000 24.12000  ? 39  ASN A CG  1 
ATOM   285  O  OD1 . ASN A  1 45  ? 29.72500  -6.54900  40.58400 1.000 22.15000  ? 39  ASN A OD1 1 
ATOM   286  N  ND2 . ASN A  1 45  ? 27.61900  -7.15300  40.05600 1.000 21.67000  ? 39  ASN A ND2 1 
ATOM   287  N  N   . PRO A  1 46  ? 31.91900  -4.49900  39.27900 1.000 18.38000  ? 40  PRO A N   1 
ATOM   288  C  CA  . PRO A  1 46  ? 32.99700  -4.95200  38.39500 1.000 19.50000  ? 40  PRO A CA  1 
ATOM   289  C  C   . PRO A  1 46  ? 32.99500  -6.45100  38.14900 1.000 18.22000  ? 40  PRO A C   1 
ATOM   290  O  O   . PRO A  1 46  ? 33.79000  -6.89000  37.31600 1.000 20.26000  ? 40  PRO A O   1 
ATOM   291  C  CB  . PRO A  1 46  ? 34.28200  -4.51700  39.13500 1.000 19.42000  ? 40  PRO A CB  1 
ATOM   292  C  CG  . PRO A  1 46  ? 33.87400  -4.38000  40.55400 1.000 20.23000  ? 40  PRO A CG  1 
ATOM   293  C  CD  . PRO A  1 46  ? 32.44400  -3.90700  40.52200 1.000 19.47000  ? 40  PRO A CD  1 
ATOM   294  N  N   . THR A  1 47  ? 32.16900  -7.24000  38.85200 1.000 17.54000  ? 41  THR A N   1 
ATOM   295  C  CA  . THR A  1 47  ? 32.09700  -8.68400  38.63000 1.000 17.87000  ? 41  THR A CA  1 
ATOM   296  C  C   . THR A  1 47  ? 30.76800  -9.11200  38.02400 1.000 19.37000  ? 41  THR A C   1 
ATOM   297  O  O   . THR A  1 47  ? 30.39900  -10.30100 38.08800 1.000 22.11000  ? 41  THR A O   1 
ATOM   298  C  CB  . THR A  1 47  ? 32.35000  -9.45300  39.92700 1.000 20.36000  ? 41  THR A CB  1 
ATOM   299  O  OG1 . THR A  1 47  ? 31.32000  -9.16700  40.88000 1.000 21.23000  ? 41  THR A OG1 1 
ATOM   300  C  CG2 . THR A  1 47  ? 33.71700  -9.08900  40.50700 1.000 20.12000  ? 41  THR A CG2 1 
ATOM   301  N  N   . ARG A  1 48  ? 30.02400  -8.16200  37.47100 1.000 18.19000  ? 42  ARG A N   1 
ATOM   302  C  CA  . ARG A  1 48  ? 28.76400  -8.46000  36.81200 1.000 18.85000  ? 42  ARG A CA  1 
ATOM   303  C  C   . ARG A  1 48  ? 28.93200  -9.58500  35.80300 1.000 19.90000  ? 42  ARG A C   1 
ATOM   304  O  O   . ARG A  1 48  ? 29.79500  -9.51300  34.92200 1.000 18.08000  ? 42  ARG A O   1 
ATOM   305  C  CB  . ARG A  1 48  ? 28.25600  -7.20400  36.08500 1.000 18.39000  ? 42  ARG A CB  1 
ATOM   306  C  CG  . ARG A  1 48  ? 26.94700  -7.42400  35.30000 1.000 19.02000  ? 42  ARG A CG  1 
ATOM   307  C  CD  . ARG A  1 48  ? 26.81500  -6.43400  34.16700 1.000 16.98000  ? 42  ARG A CD  1 
ATOM   308  N  NE  . ARG A  1 48  ? 25.49400  -6.40200  33.53000 1.000 15.79000  ? 42  ARG A NE  1 
ATOM   309  C  CZ  . ARG A  1 48  ? 25.18400  -7.04900  32.41500 1.000 17.89000  ? 42  ARG A CZ  1 
ATOM   310  N  NH1 . ARG A  1 48  ? 26.07100  -7.84300  31.80300 1.000 16.66000  ? 42  ARG A NH1 1 
ATOM   311  N  NH2 . ARG A  1 48  ? 23.94900  -6.93100  31.91600 1.000 16.41000  ? 42  ARG A NH2 1 
ATOM   312  N  N   . MET A  1 49  ? 28.11300  -10.62600 35.94700 1.000 17.45000  ? 43  MET A N   1 
ATOM   313  C  CA  A MET A  1 49  ? 28.07700  -11.68700 34.94800 0.500 20.34000  ? 43  MET A CA  1 
ATOM   314  C  CA  B MET A  1 49  ? 28.06700  -11.68900 34.95300 0.500 20.33000  ? 43  MET A CA  1 
ATOM   315  C  C   . MET A  1 49  ? 27.71100  -11.09500 33.59300 1.000 20.97000  ? 43  MET A C   1 
ATOM   316  O  O   . MET A  1 49  ? 26.65200  -10.46900 33.44500 1.000 17.43000  ? 43  MET A O   1 
ATOM   317  C  CB  A MET A  1 49  ? 27.06300  -12.75600 35.34700 0.500 20.48000  ? 43  MET A CB  1 
ATOM   318  C  CB  B MET A  1 49  ? 27.03200  -12.72800 35.37700 0.500 20.48000  ? 43  MET A CB  1 
ATOM   319  C  CG  A MET A  1 49  ? 26.91300  -13.87000 34.31600 0.500 21.92000  ? 43  MET A CG  1 
ATOM   320  C  CG  B MET A  1 49  ? 27.17600  -14.08300 34.71900 0.500 21.95000  ? 43  MET A CG  1 
ATOM   321  S  SD  A MET A  1 49  ? 28.47500  -14.73000 34.09000 0.500 22.06000  ? 43  MET A SD  1 
ATOM   322  S  SD  B MET A  1 49  ? 28.77900  -14.81200 35.07200 0.500 23.54000  ? 43  MET A SD  1 
ATOM   323  C  CE  A MET A  1 49  ? 28.35900  -15.89800 35.44000 0.500 21.97000  ? 43  MET A CE  1 
ATOM   324  C  CE  B MET A  1 49  ? 28.62000  -16.26400 34.06600 0.500 22.54000  ? 43  MET A CE  1 
ATOM   325  N  N   . THR A  1 50  ? 28.56200  -11.32600 32.59600 1.000 17.23000  ? 44  THR A N   1 
ATOM   326  C  CA  . THR A  1 50  ? 28.46900  -10.59500 31.33400 1.000 15.99000  ? 44  THR A CA  1 
ATOM   327  C  C   . THR A  1 50  ? 28.83000  -11.46400 30.13400 1.000 18.81000  ? 44  THR A C   1 
ATOM   328  O  O   . THR A  1 50  ? 29.91800  -12.06500 30.08700 1.000 17.17000  ? 44  THR A O   1 
ATOM   329  C  CB  . THR A  1 50  ? 29.38600  -9.36100  31.39700 1.000 19.13000  ? 44  THR A CB  1 
ATOM   330  O  OG1 . THR A  1 50  ? 28.97100  -8.52100  32.49400 1.000 16.52000  ? 44  THR A OG1 1 
ATOM   331  C  CG2 . THR A  1 50  ? 29.34700  -8.55100  30.08600 1.000 16.86000  ? 44  THR A CG2 1 
ATOM   332  N  N   . LEU A  1 51  ? 27.94700  -11.45400 29.13700 1.000 17.39000  ? 45  LEU A N   1 
ATOM   333  C  CA  . LEU A  1 51  ? 28.24800  -12.02700 27.83700 1.000 17.57000  ? 45  LEU A CA  1 
ATOM   334  C  C   . LEU A  1 51  ? 29.31300  -11.19500 27.14300 1.000 17.00000  ? 45  LEU A C   1 
ATOM   335  O  O   . LEU A  1 51  ? 29.08700  -10.01900 26.80500 1.000 17.94000  ? 45  LEU A O   1 
ATOM   336  C  CB  . LEU A  1 51  ? 27.00200  -12.08000 26.96900 1.000 18.60000  ? 45  LEU A CB  1 
ATOM   337  C  CG  . LEU A  1 51  ? 25.91100  -13.03700 27.43800 1.000 19.75000  ? 45  LEU A CG  1 
ATOM   338  C  CD1 . LEU A  1 51  ? 24.52300  -12.49100 27.03100 1.000 20.33000  ? 45  LEU A CD1 1 
ATOM   339  C  CD2 . LEU A  1 51  ? 26.16900  -14.43800 26.85600 1.000 21.28000  ? 45  LEU A CD2 1 
ATOM   340  N  N   . ALA A  1 52  ? 30.48000  -11.81300 26.92600 1.000 17.31000  ? 46  ALA A N   1 
ATOM   341  C  CA  . ALA A  1 52  ? 31.59500  -11.09700 26.31500 1.000 21.06000  ? 46  ALA A CA  1 
ATOM   342  C  C   . ALA A  1 52  ? 31.36700  -10.86200 24.83200 1.000 24.31000  ? 46  ALA A C   1 
ATOM   343  O  O   . ALA A  1 52  ? 31.92600  -9.91100  24.26100 1.000 19.04000  ? 46  ALA A O   1 
ATOM   344  C  CB  . ALA A  1 52  ? 32.89400  -11.88600 26.54000 1.000 17.68000  ? 46  ALA A CB  1 
ATOM   345  N  N   . ARG A  1 53  ? 30.57900  -11.72300 24.18300 1.000 19.69000  ? 47  ARG A N   1 
ATOM   346  C  CA  . ARG A  1 53  ? 30.24600  -11.59200 22.76000 1.000 19.24000  ? 47  ARG A CA  1 
ATOM   347  C  C   . ARG A  1 53  ? 31.55600  -11.46500 21.98500 1.000 19.77000  ? 47  ARG A C   1 
ATOM   348  O  O   . ARG A  1 53  ? 32.51200  -12.17700 22.31500 1.000 18.04000  ? 47  ARG A O   1 
ATOM   349  C  CB  . ARG A  1 53  ? 29.24600  -10.43400 22.58200 1.000 18.95000  ? 47  ARG A CB  1 
ATOM   350  C  CG  . ARG A  1 53  ? 28.01300  -10.50400 23.48400 1.000 21.65000  ? 47  ARG A CG  1 
ATOM   351  C  CD  . ARG A  1 53  ? 27.01200  -11.63400 23.10100 1.000 21.25000  ? 47  ARG A CD  1 
ATOM   352  N  NE  . ARG A  1 53  ? 26.52800  -11.46800 21.73500 1.000 20.24000  ? 47  ARG A NE  1 
ATOM   353  C  CZ  . ARG A  1 53  ? 25.64400  -10.56000 21.34100 1.000 19.59000  ? 47  ARG A CZ  1 
ATOM   354  N  NH1 . ARG A  1 53  ? 25.04400  -9.74200  22.19900 1.000 20.48000  ? 47  ARG A NH1 1 
ATOM   355  N  NH2 . ARG A  1 53  ? 25.35200  -10.46400 20.05400 1.000 20.24000  ? 47  ARG A NH2 1 
ATOM   356  N  N   . SER A  1 54  ? 31.68900  -10.51800 21.04500 1.000 18.69000  ? 48  SER A N   1 
ATOM   357  C  CA  A SER A  1 54  ? 32.92700  -10.42900 20.27000 0.300 19.84000  ? 48  SER A CA  1 
ATOM   358  C  CA  B SER A  1 54  ? 32.91300  -10.38200 20.25800 0.700 19.83000  ? 48  SER A CA  1 
ATOM   359  C  C   . SER A  1 54  ? 34.12000  -9.94700  21.07100 1.000 20.42000  ? 48  SER A C   1 
ATOM   360  O  O   . SER A  1 54  ? 35.24100  -9.99600  20.55100 1.000 20.61000  ? 48  SER A O   1 
ATOM   361  C  CB  A SER A  1 54  ? 32.77300  -9.48200  19.10400 0.300 21.29000  ? 48  SER A CB  1 
ATOM   362  C  CB  B SER A  1 54  ? 32.70300  -9.37500  19.14600 0.700 21.34000  ? 48  SER A CB  1 
ATOM   363  O  OG  A SER A  1 54  ? 32.03900  -8.34600  19.53000 0.300 21.09000  ? 48  SER A OG  1 
ATOM   364  O  OG  B SER A  1 54  ? 32.09800  -9.99600  18.05100 0.700 24.09000  ? 48  SER A OG  1 
ATOM   365  N  N   . ALA A  1 55  ? 33.92200  -9.45400  22.28400 1.000 19.14000  ? 49  ALA A N   1 
ATOM   366  C  CA  . ALA A  1 55  ? 35.10300  -9.13900  23.07500 1.000 18.42000  ? 49  ALA A CA  1 
ATOM   367  C  C   . ALA A  1 55  ? 35.87400  -10.38400 23.43000 1.000 21.44000  ? 49  ALA A C   1 
ATOM   368  O  O   . ALA A  1 55  ? 37.04500  -10.28500 23.83200 1.000 19.50000  ? 49  ALA A O   1 
ATOM   369  C  CB  . ALA A  1 55  ? 34.73400  -8.38800  24.35200 1.000 19.68000  ? 49  ALA A CB  1 
ATOM   370  N  N   . ALA A  1 56  ? 35.25300  -11.55500 23.28300 1.000 18.80000  ? 50  ALA A N   1 
ATOM   371  C  CA  . ALA A  1 56  ? 35.98300  -12.79400 23.50900 1.000 20.32000  ? 50  ALA A CA  1 
ATOM   372  C  C   . ALA A  1 56  ? 36.80400  -13.23400 22.30500 1.000 20.26000  ? 50  ALA A C   1 
ATOM   373  O  O   . ALA A  1 56  ? 37.50900  -14.23800 22.40400 1.000 22.40000  ? 50  ALA A O   1 
ATOM   374  C  CB  . ALA A  1 56  ? 35.02100  -13.91900 23.90600 1.000 18.77000  ? 50  ALA A CB  1 
ATOM   375  N  N   . LYS A  1 57  ? 36.72900  -12.56000 21.16500 1.000 17.14000  ? 51  LYS A N   1 
ATOM   376  C  CA  . LYS A  1 57  ? 37.40100  -13.10100 19.98100 1.000 16.42000  ? 51  LYS A CA  1 
ATOM   377  C  C   . LYS A  1 57  ? 38.92000  -13.27000 20.11800 1.000 17.85000  ? 51  LYS A C   1 
ATOM   378  O  O   . LYS A  1 57  ? 39.45000  -14.22200 19.51800 1.000 19.91000  ? 51  LYS A O   1 
ATOM   379  C  CB  . LYS A  1 57  ? 37.05300  -12.25600 18.75200 1.000 19.88000  ? 51  LYS A CB  1 
ATOM   380  C  CG  . LYS A  1 57  ? 35.73500  -12.62000 18.12700 1.000 21.82000  ? 51  LYS A CG  1 
ATOM   381  C  CD  . LYS A  1 57  ? 35.24500  -11.51200 17.20500 1.000 20.73000  ? 51  LYS A CD  1 
ATOM   382  C  CE  . LYS A  1 57  ? 33.94500  -11.89900 16.50700 1.000 21.42000  ? 51  LYS A CE  1 
ATOM   383  N  NZ  . LYS A  1 57  ? 33.25600  -10.68400 15.87500 1.000 25.21000  ? 51  LYS A NZ  1 
ATOM   384  N  N   . PRO A  1 58  ? 39.66700  -12.45900 20.86500 1.000 22.35000  ? 52  PRO A N   1 
ATOM   385  C  CA  . PRO A  1 58  ? 41.09200  -12.81600 21.03500 1.000 24.01000  ? 52  PRO A CA  1 
ATOM   386  C  C   . PRO A  1 58  ? 41.29300  -14.16100 21.71700 1.000 21.65000  ? 52  PRO A C   1 
ATOM   387  O  O   . PRO A  1 58  ? 42.21800  -14.88900 21.36200 1.000 19.06000  ? 52  PRO A O   1 
ATOM   388  C  CB  . PRO A  1 58  ? 41.66300  -11.66700 21.86900 1.000 21.48000  ? 52  PRO A CB  1 
ATOM   389  C  CG  . PRO A  1 58  ? 40.84000  -10.48100 21.44700 1.000 19.78000  ? 52  PRO A CG  1 
ATOM   390  C  CD  . PRO A  1 58  ? 39.40200  -11.07100 21.28100 1.000 22.72000  ? 52  PRO A CD  1 
ATOM   391  N  N   . ALA A  1 59  ? 40.46700  -14.51800 22.70200 1.000 20.74000  ? 53  ALA A N   1 
ATOM   392  C  CA  . ALA A  1 59  ? 40.58500  -15.84600 23.30100 1.000 20.77000  ? 53  ALA A CA  1 
ATOM   393  C  C   . ALA A  1 59  ? 40.23100  -16.93000 22.29500 1.000 19.35000  ? 53  ALA A C   1 
ATOM   394  O  O   . ALA A  1 59  ? 40.82300  -18.02400 22.30000 1.000 21.52000  ? 53  ALA A O   1 
ATOM   395  C  CB  . ALA A  1 59  ? 39.66500  -15.95600 24.52600 1.000 21.57000  ? 53  ALA A CB  1 
ATOM   396  N  N   . GLN A  1 60  ? 39.22300  -16.67900 21.46000 1.000 20.41000  ? 54  GLN A N   1 
ATOM   397  C  CA  . GLN A  1 60  ? 38.89500  -17.67200 20.45100 1.000 20.02000  ? 54  GLN A CA  1 
ATOM   398  C  C   . GLN A  1 60  ? 40.00400  -17.77600 19.41700 1.000 23.13000  ? 54  GLN A C   1 
ATOM   399  O  O   . GLN A  1 60  ? 40.30500  -18.88200 18.94100 1.000 20.37000  ? 54  GLN A O   1 
ATOM   400  C  CB  . GLN A  1 60  ? 37.55300  -17.34000 19.79800 1.000 20.00000  ? 54  GLN A CB  1 
ATOM   401  C  CG  . GLN A  1 60  ? 36.37600  -17.59500 20.74200 1.000 20.45000  ? 54  GLN A CG  1 
ATOM   402  C  CD  . GLN A  1 60  ? 35.14600  -16.81300 20.35100 1.000 20.51000  ? 54  GLN A CD  1 
ATOM   403  O  OE1 . GLN A  1 60  ? 35.23800  -15.62800 20.05000 1.000 20.74000  ? 54  GLN A OE1 1 
ATOM   404  N  NE2 . GLN A  1 60  ? 33.99100  -17.46800 20.36300 1.000 21.08000  ? 54  GLN A NE2 1 
ATOM   405  N  N   . ALA A  1 61  ? 40.64600  -16.63900 19.08100 1.000 19.72000  ? 55  ALA A N   1 
ATOM   406  C  CA  . ALA A  1 61  ? 41.80400  -16.68700 18.18800 1.000 21.39000  ? 55  ALA A CA  1 
ATOM   407  C  C   . ALA A  1 61  ? 42.95300  -17.47400 18.80700 1.000 22.73000  ? 55  ALA A C   1 
ATOM   408  O  O   . ALA A  1 61  ? 43.70900  -18.14900 18.09300 1.000 24.52000  ? 55  ALA A O   1 
ATOM   409  C  CB  . ALA A  1 61  ? 42.27200  -15.27600 17.82800 1.000 18.65000  ? 55  ALA A CB  1 
ATOM   410  N  N   . LEU A  1 62  ? 43.12000  -17.38600 20.12400 1.000 22.27000  ? 56  LEU A N   1 
ATOM   411  C  CA  . LEU A  1 62  ? 44.17300  -18.17400 20.74600 1.000 23.57000  ? 56  LEU A CA  1 
ATOM   412  C  C   . LEU A  1 62  ? 43.87600  -19.65700 20.59400 1.000 24.24000  ? 56  LEU A C   1 
ATOM   413  O  O   . LEU A  1 62  ? 44.76100  -20.43100 20.22000 1.000 22.26000  ? 56  LEU A O   1 
ATOM   414  C  CB  . LEU A  1 62  ? 44.34200  -17.80000 22.21300 1.000 22.47000  ? 56  LEU A CB  1 
ATOM   415  C  CG  . LEU A  1 62  ? 45.32300  -18.66600 23.01300 1.000 25.07000  ? 56  LEU A CG  1 
ATOM   416  C  CD1 . LEU A  1 62  ? 46.70800  -18.45600 22.47100 1.000 24.98000  ? 56  LEU A CD1 1 
ATOM   417  C  CD2 . LEU A  1 62  ? 45.28200  -18.34300 24.49300 1.000 23.30000  ? 56  LEU A CD2 1 
ATOM   418  N  N   . ALA A  1 63  ? 42.61900  -20.06700 20.83000 1.000 21.63000  ? 57  ALA A N   1 
ATOM   419  C  CA  . ALA A  1 63  ? 42.26700  -21.46600 20.63900 1.000 21.73000  ? 57  ALA A CA  1 
ATOM   420  C  C   . ALA A  1 63  ? 42.53100  -21.91200 19.20500 1.000 23.54000  ? 57  ALA A C   1 
ATOM   421  O  O   . ALA A  1 63  ? 42.96500  -23.05000 18.96600 1.000 23.03000  ? 57  ALA A O   1 
ATOM   422  C  CB  . ALA A  1 63  ? 40.80700  -21.70500 21.02700 1.000 22.15000  ? 57  ALA A CB  1 
ATOM   423  N  N   . ILE A  1 64  ? 42.27000  -21.03500 18.23700 1.000 20.04000  ? 58  ILE A N   1 
ATOM   424  C  CA  . ILE A  1 64  ? 42.56000  -21.35700 16.84100 1.000 22.71000  ? 58  ILE A CA  1 
ATOM   425  C  C   . ILE A  1 64  ? 44.06500  -21.52600 16.63100 1.000 22.61000  ? 58  ILE A C   1 
ATOM   426  O  O   . ILE A  1 64  ? 44.51900  -22.52200 16.05900 1.000 23.80000  ? 58  ILE A O   1 
ATOM   427  C  CB  . ILE A  1 64  ? 41.99100  -20.26700 15.92100 1.000 19.86000  ? 58  ILE A CB  1 
ATOM   428  C  CG1 . ILE A  1 64  ? 40.45900  -20.25500 15.97900 1.000 18.54000  ? 58  ILE A CG1 1 
ATOM   429  C  CG2 . ILE A  1 64  ? 42.49800  -20.43000 14.49100 1.000 19.21000  ? 58  ILE A CG2 1 
ATOM   430  C  CD1 . ILE A  1 64  ? 39.89200  -18.93000 15.43500 1.000 18.38000  ? 58  ILE A CD1 1 
ATOM   431  N  N   . LEU A  1 65  ? 44.86300  -20.55000 17.08800 1.000 18.57000  ? 59  LEU A N   1 
ATOM   432  C  CA  . LEU A  1 65  ? 46.29300  -20.58900 16.81400 1.000 23.31000  ? 59  LEU A CA  1 
ATOM   433  C  C   . LEU A  1 65  ? 46.99500  -21.71400 17.57000 1.000 24.73000  ? 59  LEU A C   1 
ATOM   434  O  O   . LEU A  1 65  ? 48.07300  -22.17500 17.14300 1.000 28.70000  ? 59  LEU A O   1 
ATOM   435  C  CB  . LEU A  1 65  ? 46.91500  -19.23400 17.15200 1.000 23.44000  ? 59  LEU A CB  1 
ATOM   436  C  CG  . LEU A  1 65  ? 46.48200  -18.11100 16.21200 1.000 24.99000  ? 59  LEU A CG  1 
ATOM   437  C  CD1 . LEU A  1 65  ? 46.92900  -16.77400 16.77300 1.000 27.40000  ? 59  LEU A CD1 1 
ATOM   438  C  CD2 . LEU A  1 65  ? 47.02100  -18.31800 14.79200 1.000 28.01000  ? 59  LEU A CD2 1 
ATOM   439  N  N   . GLU A  1 66  ? 46.42000  -22.19100 18.66900 1.000 23.46000  ? 60  GLU A N   1 
ATOM   440  C  CA  . GLU A  1 66  ? 47.03800  -23.29000 19.40400 1.000 28.54000  ? 60  GLU A CA  1 
ATOM   441  C  C   . GLU A  1 66  ? 46.65100  -24.65900 18.87000 1.000 28.44000  ? 60  GLU A C   1 
ATOM   442  O  O   . GLU A  1 66  ? 47.17300  -25.68100 19.34900 1.000 23.78000  ? 60  GLU A O   1 
ATOM   443  C  CB  . GLU A  1 66  ? 46.67600  -23.20100 20.88300 1.000 27.47000  ? 60  GLU A CB  1 
ATOM   444  C  CG  . GLU A  1 66  ? 47.33900  -22.04200 21.57000 1.000 28.22000  ? 60  GLU A CG  1 
ATOM   445  C  CD  . GLU A  1 66  ? 47.08100  -22.05700 23.05500 1.000 30.64000  ? 60  GLU A CD  1 
ATOM   446  O  OE1 . GLU A  1 66  ? 45.93700  -22.40500 23.44300 1.000 32.30000  ? 60  GLU A OE1 1 
ATOM   447  O  OE2 . GLU A  1 66  ? 48.02700  -21.73900 23.82400 1.000 34.10000  ? 60  GLU A OE2 1 
ATOM   448  N  N   . THR A  1 67  ? 45.77800  -24.71000 17.87800 1.000 22.33000  ? 61  THR A N   1 
ATOM   449  C  CA  . THR A  1 67  ? 45.37800  -25.99400 17.31100 1.000 22.77000  ? 61  THR A CA  1 
ATOM   450  C  C   . THR A  1 67  ? 46.49600  -26.57000 16.44100 1.000 25.10000  ? 61  THR A C   1 
ATOM   451  O  O   . THR A  1 67  ? 47.08700  -25.86100 15.61900 1.000 25.22000  ? 61  THR A O   1 
ATOM   452  C  CB  . THR A  1 67  ? 44.09900  -25.81100 16.50100 1.000 22.03000  ? 61  THR A CB  1 
ATOM   453  O  OG1 . THR A  1 67  ? 43.05300  -25.37700 17.38900 1.000 26.54000  ? 61  THR A OG1 1 
ATOM   454  C  CG2 . THR A  1 67  ? 43.71300  -27.13000 15.84500 1.000 21.63000  ? 61  THR A CG2 1 
ATOM   455  N  N   . GLU A  1 68  ? 46.79800  -27.85100 16.65400 1.000 25.14000  ? 62  GLU A N   1 
ATOM   456  C  CA  . GLU A  1 68  ? 47.83200  -28.55300 15.90200 1.000 27.26000  ? 62  GLU A CA  1 
ATOM   457  C  C   . GLU A  1 68  ? 47.60800  -28.41600 14.40000 1.000 27.61000  ? 62  GLU A C   1 
ATOM   458  O  O   . GLU A  1 68  ? 46.52200  -28.70000 13.89700 1.000 27.54000  ? 62  GLU A O   1 
ATOM   459  C  CB  . GLU A  1 68  ? 47.81600  -30.03700 16.28700 1.000 28.55000  ? 62  GLU A CB  1 
ATOM   460  C  CG  . GLU A  1 68  ? 48.16100  -30.34100 17.72900 1.000 25.23000  ? 62  GLU A CG  1 
ATOM   461  C  CD  . GLU A  1 68  ? 47.00400  -30.18600 18.72400 1.000 24.73000  ? 62  GLU A CD  1 
ATOM   462  O  OE1 . GLU A  1 68  ? 45.99600  -29.45100 18.43700 1.000 26.26000  ? 62  GLU A OE1 1 
ATOM   463  O  OE2 . GLU A  1 68  ? 47.14200  -30.75500 19.84100 1.000 25.34000  ? 62  GLU A OE2 1 
ATOM   464  N  N   . GLY A  1 69  ? 48.65200  -28.02200 13.68200 1.000 25.39000  ? 63  GLY A N   1 
ATOM   465  C  CA  . GLY A  1 69  ? 48.61000  -27.92200 12.24100 1.000 27.41000  ? 63  GLY A CA  1 
ATOM   466  C  C   . GLY A  1 69  ? 48.19700  -26.56500 11.68700 1.000 27.79000  ? 63  GLY A C   1 
ATOM   467  O  O   . GLY A  1 69  ? 48.46100  -26.29300 10.51400 1.000 30.64000  ? 63  GLY A O   1 
ATOM   468  N  N   . VAL A  1 70  ? 47.54900  -25.70600 12.48200 1.000 22.81000  ? 64  VAL A N   1 
ATOM   469  C  CA  . VAL A  1 70  ? 47.11100  -24.42200 11.93600 1.000 26.17000  ? 64  VAL A CA  1 
ATOM   470  C  C   . VAL A  1 70  ? 48.28700  -23.57100 11.44300 1.000 24.47000  ? 64  VAL A C   1 
ATOM   471  O  O   . VAL A  1 70  ? 48.15200  -22.81800 10.47200 1.000 26.75000  ? 64  VAL A O   1 
ATOM   472  C  CB  . VAL A  1 70  ? 46.26000  -23.67000 12.97700 1.000 23.92000  ? 64  VAL A CB  1 
ATOM   473  C  CG1 . VAL A  1 70  ? 46.03600  -22.20300 12.53700 1.000 23.80000  ? 64  VAL A CG1 1 
ATOM   474  C  CG2 . VAL A  1 70  ? 44.90100  -24.37400 13.15200 1.000 25.48000  ? 64  VAL A CG2 1 
ATOM   475  N  N   . ALA A  1 71  ? 49.45100  -23.68200 12.07900 1.000 30.51000  ? 65  ALA A N   1 
ATOM   476  C  CA  . ALA A  1 71  ? 50.62700  -22.94500 11.62100 1.000 27.60000  ? 65  ALA A CA  1 
ATOM   477  C  C   . ALA A  1 71  ? 50.94300  -23.21300 10.15200 1.000 28.35000  ? 65  ALA A C   1 
ATOM   478  O  O   . ALA A  1 71  ? 51.48700  -22.34200 9.46100  1.000 31.60000  ? 65  ALA A O   1 
ATOM   479  C  CB  . ALA A  1 71  ? 51.82800  -23.30200 12.49300 1.000 30.63000  ? 65  ALA A CB  1 
ATOM   480  N  N   . GLY A  1 72  ? 50.60400  -24.39800 9.64800  1.000 31.00000  ? 66  GLY A N   1 
ATOM   481  C  CA  . GLY A  1 72  ? 50.91800  -24.72500 8.27000  1.000 30.15000  ? 66  GLY A CA  1 
ATOM   482  C  C   . GLY A  1 72  ? 50.13900  -23.94400 7.23000  1.000 31.02000  ? 66  GLY A C   1 
ATOM   483  O  O   . GLY A  1 72  ? 50.52600  -23.94800 6.05900  1.000 30.27000  ? 66  GLY A O   1 
ATOM   484  N  N   . TYR A  1 73  ? 49.03300  -23.30900 7.60900  1.000 29.51000  ? 67  TYR A N   1 
ATOM   485  C  CA  . TYR A  1 73  ? 48.26300  -22.57600 6.61600  1.000 27.27000  ? 67  TYR A CA  1 
ATOM   486  C  C   . TYR A  1 73  ? 48.87600  -21.22300 6.26500  1.000 29.56000  ? 67  TYR A C   1 
ATOM   487  O  O   . TYR A  1 73  ? 48.46200  -20.61500 5.27500  1.000 30.01000  ? 67  TYR A O   1 
ATOM   488  C  CB  . TYR A  1 73  ? 46.82300  -22.37300 7.09700  1.000 29.22000  ? 67  TYR A CB  1 
ATOM   489  C  CG  . TYR A  1 73  ? 46.04400  -23.67000 7.21200  1.000 29.30000  ? 67  TYR A CG  1 
ATOM   490  C  CD1 . TYR A  1 73  ? 46.00100  -24.56800 6.15000  1.000 30.88000  ? 67  TYR A CD1 1 
ATOM   491  C  CD2 . TYR A  1 73  ? 45.34700  -23.99400 8.38200  1.000 25.99000  ? 67  TYR A CD2 1 
ATOM   492  C  CE1 . TYR A  1 73  ? 45.30000  -25.76300 6.25300  1.000 36.24000  ? 67  TYR A CE1 1 
ATOM   493  C  CE2 . TYR A  1 73  ? 44.63300  -25.17800 8.48200  1.000 27.99000  ? 67  TYR A CE2 1 
ATOM   494  C  CZ  . TYR A  1 73  ? 44.61500  -26.05600 7.42200  1.000 33.63000  ? 67  TYR A CZ  1 
ATOM   495  O  OH  . TYR A  1 73  ? 43.92400  -27.24700 7.53100  1.000 40.24000  ? 67  TYR A OH  1 
ATOM   496  N  N   . GLY A  1 74  ? 49.83300  -20.73700 7.04400  1.000 24.62000  ? 68  GLY A N   1 
ATOM   497  C  CA  . GLY A  1 74  ? 50.44900  -19.45000 6.74200  1.000 31.56000  ? 68  GLY A CA  1 
ATOM   498  C  C   . GLY A  1 74  ? 49.56100  -18.22600 6.90200  1.000 29.60000  ? 68  GLY A C   1 
ATOM   499  O  O   . GLY A  1 74  ? 49.68000  -17.27900 6.11700  1.000 29.24000  ? 68  GLY A O   1 
ATOM   500  N  N   . PHE A  1 75  ? 48.68400  -18.20500 7.90700  1.000 25.56000  ? 69  PHE A N   1 
ATOM   501  C  CA  . PHE A  1 75  ? 47.99300  -16.96200 8.23000  1.000 26.66000  ? 69  PHE A CA  1 
ATOM   502  C  C   . PHE A  1 75  ? 49.00300  -15.90600 8.66700  1.000 27.75000  ? 69  PHE A C   1 
ATOM   503  O  O   . PHE A  1 75  ? 49.96700  -16.21600 9.37000  1.000 29.94000  ? 69  PHE A O   1 
ATOM   504  C  CB  . PHE A  1 75  ? 46.96700  -17.18400 9.34100  1.000 27.98000  ? 69  PHE A CB  1 
ATOM   505  C  CG  . PHE A  1 75  ? 45.84800  -18.12800 8.97500  1.000 28.60000  ? 69  PHE A CG  1 
ATOM   506  C  CD1 . PHE A  1 75  ? 44.99900  -17.84000 7.91400  1.000 24.80000  ? 69  PHE A CD1 1 
ATOM   507  C  CD2 . PHE A  1 75  ? 45.61000  -19.27900 9.72600  1.000 22.38000  ? 69  PHE A CD2 1 
ATOM   508  C  CE1 . PHE A  1 75  ? 43.94300  -18.68900 7.59400  1.000 25.52000  ? 69  PHE A CE1 1 
ATOM   509  C  CE2 . PHE A  1 75  ? 44.53600  -20.11900 9.41600  1.000 23.54000  ? 69  PHE A CE2 1 
ATOM   510  C  CZ  . PHE A  1 75  ? 43.71800  -19.83400 8.34100  1.000 23.24000  ? 69  PHE A CZ  1 
ATOM   511  N  N   . ASP A  1 76  ? 48.81500  -14.66000 8.20700  1.000 24.32000  ? 70  ASP A N   1 
ATOM   512  C  CA  . ASP A  1 76  ? 49.72200  -13.56300 8.56400  1.000 25.69000  ? 70  ASP A CA  1 
ATOM   513  C  C   . ASP A  1 76  ? 49.06900  -12.63500 9.59500  1.000 22.23000  ? 70  ASP A C   1 
ATOM   514  O  O   . ASP A  1 76  ? 47.98700  -12.90900 10.10600 1.000 25.46000  ? 70  ASP A O   1 
ATOM   515  C  CB  . ASP A  1 76  ? 50.18700  -12.79500 7.32100  1.000 27.75000  ? 70  ASP A CB  1 
ATOM   516  C  CG  . ASP A  1 76  ? 49.07500  -12.13100 6.56600  1.000 28.48000  ? 70  ASP A CG  1 
ATOM   517  O  OD1 . ASP A  1 76  ? 47.91500  -12.05800 7.05800  1.000 27.42000  ? 70  ASP A OD1 1 
ATOM   518  O  OD2 . ASP A  1 76  ? 49.37200  -11.64900 5.45100  1.000 29.06000  ? 70  ASP A OD2 1 
ATOM   519  N  N   . ASP A  1 77  ? 49.78400  -11.56100 9.95400  1.000 25.27000  ? 71  ASP A N   1 
ATOM   520  C  CA  . ASP A  1 77  ? 49.29000  -10.68800 11.01900 1.000 25.50000  ? 71  ASP A CA  1 
ATOM   521  C  C   . ASP A  1 77  ? 47.90900  -10.13200 10.68800 1.000 24.93000  ? 71  ASP A C   1 
ATOM   522  O  O   . ASP A  1 77  ? 47.00900  -10.12600 11.54200 1.000 22.44000  ? 71  ASP A O   1 
ATOM   523  C  CB  . ASP A  1 77  ? 50.27000  -9.54800  11.26600 1.000 28.58000  ? 71  ASP A CB  1 
ATOM   524  C  CG  . ASP A  1 77  ? 51.56600  -10.01000 11.94100 1.000 34.12000  ? 71  ASP A CG  1 
ATOM   525  O  OD1 . ASP A  1 77  ? 51.66700  -11.18600 12.34300 1.000 29.96000  ? 71  ASP A OD1 1 
ATOM   526  O  OD2 . ASP A  1 77  ? 52.48900  -9.17900  12.05100 1.000 43.97000  ? 71  ASP A OD2 1 
ATOM   527  N  N   . ALA A  1 78  ? 47.71300  -9.67300  9.44800  1.000 23.35000  ? 72  ALA A N   1 
ATOM   528  C  CA  . ALA A  1 78  ? 46.40000  -9.13600  9.08000  1.000 24.00000  ? 72  ALA A CA  1 
ATOM   529  C  C   . ALA A  1 78  ? 45.30600  -10.20600 9.14300  1.000 23.74000  ? 72  ALA A C   1 
ATOM   530  O  O   . ALA A  1 78  ? 44.17100  -9.91500  9.55500  1.000 21.79000  ? 72  ALA A O   1 
ATOM   531  C  CB  . ALA A  1 78  ? 46.46100  -8.52300  7.69300  1.000 25.43000  ? 72  ALA A CB  1 
ATOM   532  N  N   . ASP A  1 79  ? 45.61800  -11.43300 8.70800  1.000 23.22000  ? 73  ASP A N   1 
ATOM   533  C  CA  . ASP A  1 79  ? 44.68000  -12.54100 8.85500  1.000 22.04000  ? 73  ASP A CA  1 
ATOM   534  C  C   . ASP A  1 79  ? 44.28400  -12.73100 10.31700 1.000 22.70000  ? 73  ASP A C   1 
ATOM   535  O  O   . ASP A  1 79  ? 43.10900  -12.92000 10.63700 1.000 23.42000  ? 73  ASP A O   1 
ATOM   536  C  CB  . ASP A  1 79  ? 45.29000  -13.83300 8.31900  1.000 23.48000  ? 73  ASP A CB  1 
ATOM   537  C  CG  . ASP A  1 79  ? 45.53100  -13.82000 6.82200  1.000 25.16000  ? 73  ASP A CG  1 
ATOM   538  O  OD1 . ASP A  1 79  ? 44.86300  -13.03500 6.10300  1.000 23.23000  ? 73  ASP A OD1 1 
ATOM   539  O  OD2 . ASP A  1 79  ? 46.38900  -14.64600 6.37400  1.000 26.31000  ? 73  ASP A OD2 1 
ATOM   540  N  N   . ILE A  1 80  ? 45.26600  -12.73400 11.21700 1.000 23.33000  ? 74  ILE A N   1 
ATOM   541  C  CA  . ILE A  1 80  ? 44.94000  -12.93900 12.62000 1.000 22.35000  ? 74  ILE A CA  1 
ATOM   542  C  C   . ILE A  1 80  ? 44.06700  -11.80100 13.13300 1.000 22.97000  ? 74  ILE A C   1 
ATOM   543  O  O   . ILE A  1 80  ? 43.08400  -12.02800 13.85700 1.000 18.02000  ? 74  ILE A O   1 
ATOM   544  C  CB  . ILE A  1 80  ? 46.22600  -13.10400 13.44200 1.000 24.68000  ? 74  ILE A CB  1 
ATOM   545  C  CG1 . ILE A  1 80  ? 46.90300  -14.41500 13.03300 1.000 26.46000  ? 74  ILE A CG1 1 
ATOM   546  C  CG2 . ILE A  1 80  ? 45.89900  -13.11600 14.93300 1.000 22.49000  ? 74  ILE A CG2 1 
ATOM   547  C  CD1 . ILE A  1 80  ? 48.40200  -14.46300 13.36200 1.000 28.94000  ? 74  ILE A CD1 1 
ATOM   548  N  N   . ALA A  1 81  ? 44.41600  -10.55800 12.76100 1.000 21.19000  ? 75  ALA A N   1 
ATOM   549  C  CA  . ALA A  1 81  ? 43.58200  -9.41200  13.08900 1.000 21.85000  ? 75  ALA A CA  1 
ATOM   550  C  C   . ALA A  1 81  ? 42.14100  -9.64800  12.67200 1.000 21.09000  ? 75  ALA A C   1 
ATOM   551  O  O   . ALA A  1 81  ? 41.21200  -9.30400  13.41000 1.000 19.84000  ? 75  ALA A O   1 
ATOM   552  C  CB  . ALA A  1 81  ? 44.12800  -8.15700  12.41500 1.000 19.21000  ? 75  ALA A CB  1 
ATOM   553  N  N   . LEU A  1 82  ? 41.93000  -10.20800 11.48600 1.000 19.96000  ? 76  LEU A N   1 
ATOM   554  C  CA  . LEU A  1 82  ? 40.56000  -10.47300 11.06300 1.000 20.93000  ? 76  LEU A CA  1 
ATOM   555  C  C   . LEU A  1 82  ? 39.90500  -11.55500 11.92900 1.000 19.91000  ? 76  LEU A C   1 
ATOM   556  O  O   . LEU A  1 82  ? 38.70400  -11.48800 12.21300 1.000 21.34000  ? 76  LEU A O   1 
ATOM   557  C  CB  . LEU A  1 82  ? 40.51800  -10.87400 9.59500  1.000 22.60000  ? 76  LEU A CB  1 
ATOM   558  C  CG  . LEU A  1 82  ? 39.10600  -10.69400 9.00700  1.000 20.87000  ? 76  LEU A CG  1 
ATOM   559  C  CD1 . LEU A  1 82  ? 38.83200  -9.22900  8.76800  1.000 19.40000  ? 76  LEU A CD1 1 
ATOM   560  C  CD2 . LEU A  1 82  ? 38.94700  -11.53900 7.73900  1.000 19.94000  ? 76  LEU A CD2 1 
ATOM   561  N  N   . MET A  1 83  ? 40.66500  -12.56100 12.35200 1.000 18.98000  ? 77  MET A N   1 
ATOM   562  C  CA  . MET A  1 83  ? 40.13900  -13.51200 13.33100 1.000 19.84000  ? 77  MET A CA  1 
ATOM   563  C  C   . MET A  1 83  ? 39.61700  -12.79000 14.55900 1.000 21.87000  ? 77  MET A C   1 
ATOM   564  O  O   . MET A  1 83  ? 38.59200  -13.17900 15.13300 1.000 20.80000  ? 77  MET A O   1 
ATOM   565  C  CB  . MET A  1 83  ? 41.23100  -14.51300 13.74400 1.000 18.08000  ? 77  MET A CB  1 
ATOM   566  C  CG  . MET A  1 83  ? 41.65400  -15.42300 12.65400 1.000 16.75000  ? 77  MET A CG  1 
ATOM   567  S  SD  . MET A  1 83  ? 42.78000  -16.68300 13.32900 1.000 26.90000  ? 77  MET A SD  1 
ATOM   568  C  CE  . MET A  1 83  ? 43.29000  -17.48400 11.81800 1.000 25.94000  ? 77  MET A CE  1 
ATOM   569  N  N   . CYS A  1 84  ? 40.31600  -11.74100 14.98200 1.000 20.70000  ? 78  CYS A N   1 
ATOM   570  C  CA  . CYS A  1 84  ? 39.98700  -10.97700 16.17900 1.000 19.38000  ? 78  CYS A CA  1 
ATOM   571  C  C   . CYS A  1 84  ? 38.94800  -9.88800  15.94100 1.000 19.87000  ? 78  CYS A C   1 
ATOM   572  O  O   . CYS A  1 84  ? 38.76200  -9.04600  16.82800 1.000 22.46000  ? 78  CYS A O   1 
ATOM   573  C  CB  . CYS A  1 84  ? 41.25000  -10.32400 16.74800 1.000 21.97000  ? 78  CYS A CB  1 
ATOM   574  S  SG  . CYS A  1 84  ? 42.45500  -11.57000 17.35000 1.000 22.64000  ? 78  CYS A SG  1 
ATOM   575  N  N   . ALA A  1 85  ? 38.27500  -9.87200  14.79800 1.000 22.94000  ? 79  ALA A N   1 
ATOM   576  C  CA  . ALA A  1 85  ? 37.56800  -8.68100  14.33500 1.000 20.82000  ? 79  ALA A CA  1 
ATOM   577  C  C   . ALA A  1 85  ? 36.06400  -8.76600  14.54700 1.000 22.19000  ? 79  ALA A C   1 
ATOM   578  O  O   . ALA A  1 85  ? 35.47300  -9.83900  14.44200 1.000 20.80000  ? 79  ALA A O   1 
ATOM   579  C  CB  . ALA A  1 85  ? 37.80300  -8.46300  12.85000 1.000 19.32000  ? 79  ALA A CB  1 
ATOM   580  N  N   . SER A  1 86  ? 35.44100  -7.60100  14.75400 1.000 20.91000  ? 80  SER A N   1 
ATOM   581  C  CA  . SER A  1 86  ? 34.03100  -7.38100  14.39700 1.000 22.08000  ? 80  SER A CA  1 
ATOM   582  C  C   . SER A  1 86  ? 34.04100  -6.38300  13.24800 1.000 18.37000  ? 80  SER A C   1 
ATOM   583  O  O   . SER A  1 86  ? 33.84300  -5.19000  13.44300 1.000 20.46000  ? 80  SER A O   1 
ATOM   584  C  CB  . SER A  1 86  ? 33.22800  -6.87100  15.56300 1.000 21.84000  ? 80  SER A CB  1 
ATOM   585  O  OG  . SER A  1 86  ? 33.21200  -7.84800  16.59300 1.000 20.11000  ? 80  SER A OG  1 
ATOM   586  N  N   . HIS A  1 87  ? 34.30700  -6.87100  12.04800 1.000 17.63000  ? 81  HIS A N   1 
ATOM   587  C  CA  . HIS A  1 87  ? 34.61700  -5.90800  11.01700 1.000 19.32000  ? 81  HIS A CA  1 
ATOM   588  C  C   . HIS A  1 87  ? 33.33300  -5.35000  10.42900 1.000 19.40000  ? 81  HIS A C   1 
ATOM   589  O  O   . HIS A  1 87  ? 32.23200  -5.85700  10.68600 1.000 15.71000  ? 81  HIS A O   1 
ATOM   590  C  CB  . HIS A  1 87  ? 35.53100  -6.51500  9.94100  1.000 20.41000  ? 81  HIS A CB  1 
ATOM   591  C  CG  . HIS A  1 87  ? 34.94100  -7.67700  9.20600  1.000 19.31000  ? 81  HIS A CG  1 
ATOM   592  N  ND1 . HIS A  1 87  ? 33.88000  -7.54400  8.33400  1.000 19.59000  ? 81  HIS A ND1 1 
ATOM   593  C  CD2 . HIS A  1 87  ? 35.27800  -8.99400  9.19300  1.000 19.25000  ? 81  HIS A CD2 1 
ATOM   594  C  CE1 . HIS A  1 87  ? 33.58400  -8.72500  7.82200  1.000 18.99000  ? 81  HIS A CE1 1 
ATOM   595  N  NE2 . HIS A  1 87  ? 34.42500  -9.61900  8.31900  1.000 16.81000  ? 81  HIS A NE2 1 
ATOM   596  N  N   . SER A  1 88  ? 33.49400  -4.22800  9.71100  1.000 18.70000  ? 82  SER A N   1 
ATOM   597  C  CA  . SER A  1 88  ? 32.43200  -3.48000  9.06000  1.000 19.61000  ? 82  SER A CA  1 
ATOM   598  C  C   . SER A  1 88  ? 32.00600  -4.08000  7.72800  1.000 19.06000  ? 82  SER A C   1 
ATOM   599  O  O   . SER A  1 88  ? 31.15700  -3.48300  7.05800  1.000 19.26000  ? 82  SER A O   1 
ATOM   600  C  CB  . SER A  1 88  ? 32.87800  -2.03100  8.85000  1.000 20.66000  ? 82  SER A CB  1 
ATOM   601  O  OG  . SER A  1 88  ? 32.99000  -1.35700  10.09200 1.000 20.35000  ? 82  SER A OG  1 
ATOM   602  N  N   . SER A  1 89  ? 32.52500  -5.25200  7.33800  1.000 17.96000  ? 83  SER A N   1 
ATOM   603  C  CA  . SER A  1 89  ? 32.16100  -5.84000  6.04700  1.000 17.78000  ? 83  SER A CA  1 
ATOM   604  C  C   . SER A  1 89  ? 32.51000  -4.89900  4.89100  1.000 23.75000  ? 83  SER A C   1 
ATOM   605  O  O   . SER A  1 89  ? 31.78200  -4.81700  3.89500  1.000 20.20000  ? 83  SER A O   1 
ATOM   606  C  CB  . SER A  1 89  ? 30.66600  -6.19200  5.98000  1.000 19.37000  ? 83  SER A CB  1 
ATOM   607  O  OG  . SER A  1 89  ? 30.22400  -6.90200  7.14300  1.000 22.20000  ? 83  SER A OG  1 
ATOM   608  N  N   . GLU A  1 90  ? 33.59000  -4.14100  5.02900  1.000 17.08000  ? 84  GLU A N   1 
ATOM   609  C  CA  . GLU A  1 90  ? 34.11300  -3.42900  3.88400  1.000 18.89000  ? 84  GLU A CA  1 
ATOM   610  C  C   . GLU A  1 90  ? 34.60900  -4.42200  2.84700  1.000 21.51000  ? 84  GLU A C   1 
ATOM   611  O  O   . GLU A  1 90  ? 34.94700  -5.55500  3.16600  1.000 21.09000  ? 84  GLU A O   1 
ATOM   612  C  CB  . GLU A  1 90  ? 35.22900  -2.48100  4.33500  1.000 21.75000  ? 84  GLU A CB  1 
ATOM   613  C  CG  . GLU A  1 90  ? 34.67400  -1.42600  5.32100  1.000 18.62000  ? 84  GLU A CG  1 
ATOM   614  C  CD  . GLU A  1 90  ? 35.75800  -0.70400  6.09100  1.000 23.14000  ? 84  GLU A CD  1 
ATOM   615  O  OE1 . GLU A  1 90  ? 36.95400  -1.00800  5.85700  1.000 23.65000  ? 84  GLU A OE1 1 
ATOM   616  O  OE2 . GLU A  1 90  ? 35.40700  0.20600   6.89400  1.000 23.68000  ? 84  GLU A OE2 1 
ATOM   617  N  N   . ASP A  1 91  ? 34.65200  -3.99100  1.58200  1.000 22.60000  ? 85  ASP A N   1 
ATOM   618  C  CA  . ASP A  1 91  ? 35.13600  -4.88800  0.52700  1.000 21.56000  ? 85  ASP A CA  1 
ATOM   619  C  C   . ASP A  1 91  ? 36.45700  -5.55900  0.91200  1.000 25.92000  ? 85  ASP A C   1 
ATOM   620  O  O   . ASP A  1 91  ? 36.65400  -6.75300  0.64300  1.000 24.35000  ? 85  ASP A O   1 
ATOM   621  C  CB  . ASP A  1 91  ? 35.26700  -4.13700  -0.79600 1.000 23.92000  ? 85  ASP A CB  1 
ATOM   622  C  CG  . ASP A  1 91  ? 33.91200  -3.84200  -1.42400 1.000 22.36000  ? 85  ASP A CG  1 
ATOM   623  O  OD1 . ASP A  1 91  ? 32.87300  -4.19800  -0.81400 1.000 22.73000  ? 85  ASP A OD1 1 
ATOM   624  O  OD2 . ASP A  1 91  ? 33.87200  -3.27700  -2.52800 1.000 27.34000  ? 85  ASP A OD2 1 
ATOM   625  N  N   . ARG A  1 92  ? 37.36200  -4.82000  1.57700  1.000 24.33000  ? 86  ARG A N   1 
ATOM   626  C  CA  . ARG A  1 92  ? 38.65500  -5.40800  1.93700  1.000 21.87000  ? 86  ARG A CA  1 
ATOM   627  C  C   . ARG A  1 92  ? 38.51700  -6.49600  2.99100  1.000 21.62000  ? 86  ARG A C   1 
ATOM   628  O  O   . ARG A  1 92  ? 39.34000  -7.42000  3.01600  1.000 21.19000  ? 86  ARG A O   1 
ATOM   629  C  CB  . ARG A  1 92  ? 39.64300  -4.34900  2.43200  1.000 23.32000  ? 86  ARG A CB  1 
ATOM   630  C  CG  . ARG A  1 92  ? 39.14600  -3.52800  3.62000  1.000 22.80000  ? 86  ARG A CG  1 
ATOM   631  C  CD  . ARG A  1 92  ? 40.12200  -2.41600  4.01000  1.000 24.01000  ? 86  ARG A CD  1 
ATOM   632  N  NE  . ARG A  1 92  ? 39.52400  -1.55500  5.02700  1.000 22.61000  ? 86  ARG A NE  1 
ATOM   633  C  CZ  . ARG A  1 92  ? 40.09500  -0.47900  5.55000  1.000 23.17000  ? 86  ARG A CZ  1 
ATOM   634  N  NH1 . ARG A  1 92  ? 41.30500  -0.09500  5.19200  1.000 24.71000  ? 86  ARG A NH1 1 
ATOM   635  N  NH2 . ARG A  1 92  ? 39.44500  0.21400   6.47800  1.000 22.74000  ? 86  ARG A NH2 1 
ATOM   636  N  N   . HIS A  1 93  ? 37.51000  -6.40100  3.87400  1.000 21.99000  ? 87  HIS A N   1 
ATOM   637  C  CA  . HIS A  1 93  ? 37.28800  -7.48200  4.82700  1.000 19.80000  ? 87  HIS A CA  1 
ATOM   638  C  C   . HIS A  1 93  ? 36.76500  -8.71300  4.10800  1.000 21.87000  ? 87  HIS A C   1 
ATOM   639  O  O   . HIS A  1 93  ? 37.17500  -9.83600  4.41000  1.000 21.29000  ? 87  HIS A O   1 
ATOM   640  C  CB  . HIS A  1 93  ? 36.30000  -7.06800  5.92200  1.000 20.52000  ? 87  HIS A CB  1 
ATOM   641  C  CG  . HIS A  1 93  ? 36.72300  -5.87500  6.71700  1.000 20.31000  ? 87  HIS A CG  1 
ATOM   642  N  ND1 . HIS A  1 93  ? 35.95300  -4.72900  6.80000  1.000 21.01000  ? 87  HIS A ND1 1 
ATOM   643  C  CD2 . HIS A  1 93  ? 37.81700  -5.65200  7.49200  1.000 20.15000  ? 87  HIS A CD2 1 
ATOM   644  C  CE1 . HIS A  1 93  ? 36.55600  -3.85200  7.58400  1.000 21.49000  ? 87  HIS A CE1 1 
ATOM   645  N  NE2 . HIS A  1 93  ? 37.69500  -4.37800  8.00400  1.000 19.80000  ? 87  HIS A NE2 1 
ATOM   646  N  N   . ILE A  1 94  ? 35.85100  -8.52400  3.14600  1.000 20.81000  ? 88  ILE A N   1 
ATOM   647  C  CA  . ILE A  1 94  ? 35.36100  -9.67800  2.38900  1.000 20.96000  ? 88  ILE A CA  1 
ATOM   648  C  C   . ILE A  1 94  ? 36.51300  -10.31100 1.61300  1.000 21.61000  ? 88  ILE A C   1 
ATOM   649  O  O   . ILE A  1 94  ? 36.67800  -11.53900 1.60400  1.000 22.16000  ? 88  ILE A O   1 
ATOM   650  C  CB  . ILE A  1 94  ? 34.19600  -9.26200  1.46700  1.000 22.20000  ? 88  ILE A CB  1 
ATOM   651  C  CG1 . ILE A  1 94  ? 32.86400  -9.27400  2.20700  1.000 27.03000  ? 88  ILE A CG1 1 
ATOM   652  C  CG2 . ILE A  1 94  ? 34.08700  -10.17800 0.27100  1.000 24.41000  ? 88  ILE A CG2 1 
ATOM   653  C  CD1 . ILE A  1 94  ? 32.74800  -8.29000  3.31400  1.000 22.24000  ? 88  ILE A CD1 1 
ATOM   654  N  N   . ALA A  1 95  ? 37.34600  -9.47500  0.97300  1.000 23.41000  ? 89  ALA A N   1 
ATOM   655  C  CA  . ALA A  1 95  ? 38.47200  -9.98300  0.19600  1.000 23.45000  ? 89  ALA A CA  1 
ATOM   656  C  C   . ALA A  1 95  ? 39.43300  -10.78200 1.06900  1.000 24.87000  ? 89  ALA A C   1 
ATOM   657  O  O   . ALA A  1 95  ? 39.89200  -11.85300 0.66200  1.000 24.91000  ? 89  ALA A O   1 
ATOM   658  C  CB  . ALA A  1 95  ? 39.21100  -8.84100  -0.51600 1.000 21.73000  ? 89  ALA A CB  1 
ATOM   659  N  N   . ARG A  1 96  ? 39.72100  -10.30400 2.28600  1.000 22.75000  ? 90  ARG A N   1 
ATOM   660  C  CA  . ARG A  1 96  ? 40.62400  -11.07500 3.14600  1.000 23.64000  ? 90  ARG A CA  1 
ATOM   661  C  C   . ARG A  1 96  ? 39.97300  -12.36700 3.61700  1.000 22.14000  ? 90  ARG A C   1 
ATOM   662  O  O   . ARG A  1 96  ? 40.65600  -13.39400 3.77900  1.000 23.62000  ? 90  ARG A O   1 
ATOM   663  C  CB  . ARG A  1 96  ? 41.08800  -10.23700 4.34600  1.000 22.20000  ? 90  ARG A CB  1 
ATOM   664  C  CG  . ARG A  1 96  ? 42.15100  -10.96200 5.20600  1.000 23.58000  ? 90  ARG A CG  1 
ATOM   665  C  CD  . ARG A  1 96  ? 42.81700  -10.01700 6.18400  1.000 21.38000  ? 90  ARG A CD  1 
ATOM   666  N  NE  . ARG A  1 96  ? 43.63600  -9.05700  5.44900  1.000 28.09000  ? 90  ARG A NE  1 
ATOM   667  C  CZ  . ARG A  1 96  ? 44.82800  -9.33200  4.93300  1.000 30.09000  ? 90  ARG A CZ  1 
ATOM   668  N  NH1 . ARG A  1 96  ? 45.37400  -10.53100 5.05100  1.000 24.72000  ? 90  ARG A NH1 1 
ATOM   669  N  NH2 . ARG A  1 96  ? 45.49800  -8.37300  4.30000  1.000 28.62000  ? 90  ARG A NH2 1 
ATOM   670  N  N   . THR A  1 97  ? 38.65900  -12.34100 3.84000  1.000 21.54000  ? 91  THR A N   1 
ATOM   671  C  CA  . THR A  1 97  ? 37.94800  -13.55700 4.22200  1.000 19.47000  ? 91  THR A CA  1 
ATOM   672  C  C   . THR A  1 97  ? 38.12800  -14.62900 3.16100  1.000 23.56000  ? 91  THR A C   1 
ATOM   673  O  O   . THR A  1 97  ? 38.46300  -15.78200 3.47500  1.000 20.01000  ? 91  THR A O   1 
ATOM   674  C  CB  . THR A  1 97  ? 36.46600  -13.25200 4.44300  1.000 20.59000  ? 91  THR A CB  1 
ATOM   675  O  OG1 . THR A  1 97  ? 36.34500  -12.30600 5.51400  1.000 21.59000  ? 91  THR A OG1 1 
ATOM   676  C  CG2 . THR A  1 97  ? 35.70200  -14.53800 4.79000  1.000 21.65000  ? 91  THR A CG2 1 
ATOM   677  N  N   . ARG A  1 98  ? 37.96000  -14.24100 1.89100  1.000 23.44000  ? 92  ARG A N   1 
ATOM   678  C  CA  . ARG A  1 98  ? 38.13800  -15.16000 0.77600  1.000 22.22000  ? 92  ARG A CA  1 
ATOM   679  C  C   . ARG A  1 98  ? 39.58800  -15.60300 0.66000  1.000 24.32000  ? 92  ARG A C   1 
ATOM   680  O  O   . ARG A  1 98  ? 39.86500  -16.76400 0.34100  1.000 24.74000  ? 92  ARG A O   1 
ATOM   681  C  CB  . ARG A  1 98  ? 37.67000  -14.48600 -0.51500 1.000 26.89000  ? 92  ARG A CB  1 
ATOM   682  C  CG  . ARG A  1 98  ? 36.16200  -14.20800 -0.52000 1.000 26.19000  ? 92  ARG A CG  1 
ATOM   683  C  CD  . ARG A  1 98  ? 35.65800  -13.63900 -1.83800 1.000 30.52000  ? 92  ARG A CD  1 
ATOM   684  N  NE  . ARG A  1 98  ? 34.19700  -13.71800 -1.88800 1.000 32.35000  ? 92  ARG A NE  1 
ATOM   685  C  CZ  . ARG A  1 98  ? 33.41000  -12.82200 -2.46500 1.000 37.29000  ? 92  ARG A CZ  1 
ATOM   686  N  NH1 . ARG A  1 98  ? 33.91000  -11.74300 -3.05500 1.000 38.62000  ? 92  ARG A NH1 1 
ATOM   687  N  NH2 . ARG A  1 98  ? 32.08500  -13.01000 -2.44600 1.000 30.56000  ? 92  ARG A NH2 1 
ATOM   688  N  N   . ALA A  1 99  ? 40.53100  -14.69200 0.92000  1.000 23.94000  ? 93  ALA A N   1 
ATOM   689  C  CA  . ALA A  1 99  ? 41.94200  -15.05500 0.84700  1.000 24.11000  ? 93  ALA A CA  1 
ATOM   690  C  C   . ALA A  1 99  ? 42.29700  -16.05700 1.93300  1.000 27.05000  ? 93  ALA A C   1 
ATOM   691  O  O   . ALA A  1 99  ? 43.10900  -16.96200 1.70800  1.000 25.45000  ? 93  ALA A O   1 
ATOM   692  C  CB  . ALA A  1 99  ? 42.82300  -13.81000 0.95400  1.000 26.95000  ? 93  ALA A CB  1 
ATOM   693  N  N   . MET A  1 100 ? 41.67200  -15.93600 3.10400  1.000 21.15000  ? 94  MET A N   1 
ATOM   694  C  CA  . MET A  1 100 ? 41.89900  -16.91800 4.16500  1.000 23.93000  ? 94  MET A CA  1 
ATOM   695  C  C   . MET A  1 100 ? 41.24200  -18.26100 3.83800  1.000 25.42000  ? 94  MET A C   1 
ATOM   696  O  O   . MET A  1 100 ? 41.81500  -19.32000 4.11800  1.000 28.47000  ? 94  MET A O   1 
ATOM   697  C  CB  . MET A  1 100 ? 41.40300  -16.35600 5.49500  1.000 23.90000  ? 94  MET A CB  1 
ATOM   698  C  CG  . MET A  1 100 ? 42.20700  -15.16800 5.99100  1.000 23.77000  ? 94  MET A CG  1 
ATOM   699  S  SD  . MET A  1 100 ? 41.45300  -14.40500 7.43000  1.000 23.82000  ? 94  MET A SD  1 
ATOM   700  C  CE  . MET A  1 100 ? 41.70900  -15.70900 8.63300  1.000 17.23000  ? 94  MET A CE  1 
ATOM   701  N  N   . LEU A  1 101 ? 40.04900  -18.23800 3.23200  1.000 23.87000  ? 95  LEU A N   1 
ATOM   702  C  CA  . LEU A  1 101 ? 39.40300  -19.47200 2.78200  1.000 24.74000  ? 95  LEU A CA  1 
ATOM   703  C  C   . LEU A  1 101 ? 40.27300  -20.22800 1.79600  1.000 26.14000  ? 95  LEU A C   1 
ATOM   704  O  O   . LEU A  1 101 ? 40.33900  -21.46500 1.83000  1.000 24.99000  ? 95  LEU A O   1 
ATOM   705  C  CB  . LEU A  1 101 ? 38.04300  -19.16100 2.13300  1.000 21.69000  ? 95  LEU A CB  1 
ATOM   706  C  CG  . LEU A  1 101 ? 36.93300  -18.82400 3.13600  1.000 20.67000  ? 95  LEU A CG  1 
ATOM   707  C  CD1 . LEU A  1 101 ? 35.71100  -18.31100 2.40900  1.000 26.56000  ? 95  LEU A CD1 1 
ATOM   708  C  CD2 . LEU A  1 101 ? 36.57700  -20.05700 3.96200  1.000 24.58000  ? 95  LEU A CD2 1 
ATOM   709  N  N   . SER A  1 102 ? 40.92800  -19.50600 0.88500  1.000 27.69000  ? 96  SER A N   1 
ATOM   710  C  CA  . SER A  1 102 ? 41.78200  -20.18200 -0.08500 1.000 25.92000  ? 96  SER A CA  1 
ATOM   711  C  C   . SER A  1 102 ? 42.99900  -20.80600 0.58500  1.000 26.06000  ? 96  SER A C   1 
ATOM   712  O  O   . SER A  1 102 ? 43.49100  -21.84300 0.13000  1.000 27.87000  ? 96  SER A O   1 
ATOM   713  C  CB  . SER A  1 102 ? 42.22800  -19.20800 -1.16700 1.000 30.33000  ? 96  SER A CB  1 
ATOM   714  O  OG  . SER A  1 102 ? 41.10600  -18.69300 -1.84200 1.000 35.01000  ? 96  SER A OG  1 
ATOM   715  N  N   . LYS A  1 103 ? 43.50800  -20.17900 1.64500  1.000 25.44000  ? 97  LYS A N   1 
ATOM   716  C  CA  . LYS A  1 103 ? 44.66500  -20.73400 2.33600  1.000 29.06000  ? 97  LYS A CA  1 
ATOM   717  C  C   . LYS A  1 103 ? 44.36400  -22.10700 2.91800  1.000 28.92000  ? 97  LYS A C   1 
ATOM   718  O  O   . LYS A  1 103 ? 45.26600  -22.94000 3.03300  1.000 28.20000  ? 97  LYS A O   1 
ATOM   719  C  CB  . LYS A  1 103 ? 45.13200  -19.78400 3.44500  1.000 27.85000  ? 97  LYS A CB  1 
ATOM   720  C  CG  . LYS A  1 103 ? 45.84100  -18.53800 2.92400  1.000 30.24000  ? 97  LYS A CG  1 
ATOM   721  C  CD  . LYS A  1 103 ? 46.35100  -17.66400 4.05900  1.000 30.62000  ? 97  LYS A CD  1 
ATOM   722  C  CE  . LYS A  1 103 ? 47.22200  -16.52500 3.51400  1.000 30.54000  ? 97  LYS A CE  1 
ATOM   723  N  NZ  . LYS A  1 103 ? 47.66800  -15.60100 4.58200  1.000 28.06000  ? 97  LYS A NZ  1 
ATOM   724  N  N   . ILE A  1 104 ? 43.12300  -22.35200 3.33200  1.000 26.41000  ? 98  ILE A N   1 
ATOM   725  C  CA  . ILE A  1 104 ? 42.75500  -23.65600 3.87300  1.000 26.85000  ? 98  ILE A CA  1 
ATOM   726  C  C   . ILE A  1 104 ? 41.96100  -24.47600 2.87300  1.000 31.01000  ? 98  ILE A C   1 
ATOM   727  O  O   . ILE A  1 104 ? 41.36400  -25.49200 3.24900  1.000 27.94000  ? 98  ILE A O   1 
ATOM   728  C  CB  . ILE A  1 104 ? 41.97800  -23.52800 5.19100  1.000 25.91000  ? 98  ILE A CB  1 
ATOM   729  C  CG1 . ILE A  1 104 ? 40.66700  -22.74300 4.99000  1.000 29.73000  ? 98  ILE A CG1 1 
ATOM   730  C  CG2 . ILE A  1 104 ? 42.83100  -22.84300 6.22800  1.000 28.91000  ? 98  ILE A CG2 1 
ATOM   731  C  CD1 . ILE A  1 104 ? 39.72600  -22.83400 6.19100  1.000 22.81000  ? 98  ILE A CD1 1 
ATOM   732  N  N   . LYS A  1 105 ? 41.91700  -24.04300 1.61100  1.000 27.36000  ? 99  LYS A N   1 
ATOM   733  C  CA  . LYS A  1 105 ? 41.24100  -24.77300 0.53900  1.000 27.97000  ? 99  LYS A CA  1 
ATOM   734  C  C   . LYS A  1 105 ? 39.77000  -25.03700 0.87800  1.000 32.04000  ? 99  LYS A C   1 
ATOM   735  O  O   . LYS A  1 105 ? 39.25100  -26.13700 0.67000  1.000 31.61000  ? 99  LYS A O   1 
ATOM   736  C  CB  . LYS A  1 105 ? 41.97700  -26.07900 0.22000  1.000 31.75000  ? 99  LYS A CB  1 
ATOM   737  C  CG  . LYS A  1 105 ? 43.44300  -25.89400 -0.14900 1.000 33.74000  ? 99  LYS A CG  1 
ATOM   738  C  CD  . LYS A  1 105 ? 44.05300  -27.21200 -0.66400 1.000 38.02000  ? 99  LYS A CD  1 
ATOM   739  C  CE  . LYS A  1 105 ? 45.55000  -27.08700 -0.92300 1.000 41.83000  ? 99  LYS A CE  1 
ATOM   740  N  NZ  . LYS A  1 105 ? 46.13900  -28.41200 -1.31300 1.000 47.85000  ? 99  LYS A NZ  1 
ATOM   741  N  N   . ALA A  1 106 ? 39.10400  -24.02300 1.41600  1.000 28.91000  ? 100 ALA A N   1 
ATOM   742  C  CA  . ALA A  1 106 ? 37.68100  -24.04800 1.73100  1.000 28.62000  ? 100 ALA A CA  1 
ATOM   743  C  C   . ALA A  1 106 ? 36.93700  -23.06600 0.83600  1.000 28.34000  ? 100 ALA A C   1 
ATOM   744  O  O   . ALA A  1 106 ? 37.52300  -22.31800 0.05000  1.000 29.64000  ? 100 ALA A O   1 
ATOM   745  C  CB  . ALA A  1 106 ? 37.45000  -23.72000 3.20300  1.000 26.63000  ? 100 ALA A CB  1 
ATOM   746  N  N   . GLU A  1 107 ? 35.62100  -23.04500 0.96600  1.000 25.70000  ? 101 GLU A N   1 
ATOM   747  C  CA  . GLU A  1 107 ? 34.83800  -22.10200 0.19600  1.000 29.23000  ? 101 GLU A CA  1 
ATOM   748  C  C   . GLU A  1 107 ? 33.76800  -21.50900 1.09600  1.000 27.75000  ? 101 GLU A C   1 
ATOM   749  O  O   . GLU A  1 107 ? 33.54700  -21.97500 2.21600  1.000 25.95000  ? 101 GLU A O   1 
ATOM   750  C  CB  . GLU A  1 107 ? 34.25200  -22.74900 -1.05000 1.000 31.14000  ? 101 GLU A CB  1 
ATOM   751  C  CG  . GLU A  1 107 ? 33.39100  -23.94400 -0.80600 1.000 37.57000  ? 101 GLU A CG  1 
ATOM   752  C  CD  . GLU A  1 107 ? 33.30700  -24.80300 -2.05000 1.000 51.42000  ? 101 GLU A CD  1 
ATOM   753  O  OE1 . GLU A  1 107 ? 34.15900  -24.59500 -2.94900 1.000 57.24000  ? 101 GLU A OE1 1 
ATOM   754  O  OE2 . GLU A  1 107 ? 32.41200  -25.68200 -2.12800 1.000 61.18000  ? 101 GLU A OE2 1 
ATOM   755  N  N   . GLU A  1 108 ? 33.14600  -20.42900 0.60900  1.000 25.48000  ? 102 GLU A N   1 
ATOM   756  C  CA  A GLU A  1 108 ? 32.14500  -19.73400 1.40900  0.500 25.64000  ? 102 GLU A CA  1 
ATOM   757  C  CA  B GLU A  1 108 ? 32.11900  -19.72800 1.38000  0.500 25.65000  ? 102 GLU A CA  1 
ATOM   758  C  C   . GLU A  1 108 ? 31.05000  -20.68100 1.90600  1.000 25.58000  ? 102 GLU A C   1 
ATOM   759  O  O   . GLU A  1 108 ? 30.55100  -20.52100 3.02100  1.000 25.15000  ? 102 GLU A O   1 
ATOM   760  C  CB  A GLU A  1 108 ? 31.56300  -18.58200 0.58900  0.500 25.86000  ? 102 GLU A CB  1 
ATOM   761  C  CB  B GLU A  1 108 ? 31.46400  -18.64200 0.52100  0.500 25.86000  ? 102 GLU A CB  1 
ATOM   762  C  CG  A GLU A  1 108 ? 32.63400  -17.59100 0.07700  0.500 24.34000  ? 102 GLU A CG  1 
ATOM   763  C  CG  B GLU A  1 108 ? 30.24800  -18.04200 1.19900  0.500 25.80000  ? 102 GLU A CG  1 
ATOM   764  C  CD  A GLU A  1 108 ? 32.03800  -16.44800 -0.71900 0.500 25.21000  ? 102 GLU A CD  1 
ATOM   765  C  CD  B GLU A  1 108 ? 29.67100  -16.81400 0.51300  0.500 24.56000  ? 102 GLU A CD  1 
ATOM   766  O  OE1 A GLU A  1 108 ? 30.80400  -16.28300 -0.65100 0.500 25.31000  ? 102 GLU A OE1 1 
ATOM   767  O  OE1 B GLU A  1 108 ? 29.59000  -16.77200 -0.73400 0.500 26.22000  ? 102 GLU A OE1 1 
ATOM   768  O  OE2 A GLU A  1 108 ? 32.78700  -15.72900 -1.41800 0.500 23.52000  ? 102 GLU A OE2 1 
ATOM   769  O  OE2 B GLU A  1 108 ? 29.28500  -15.89900 1.24900  0.500 19.97000  ? 102 GLU A OE2 1 
ATOM   770  N  N   . ALA A  1 109 ? 30.68700  -21.68400 1.11600  1.000 24.00000  ? 103 ALA A N   1 
ATOM   771  C  CA  . ALA A  1 109 ? 29.63900  -22.62000 1.53200  1.000 27.29000  ? 103 ALA A CA  1 
ATOM   772  C  C   . ALA A  1 109 ? 30.01400  -23.42800 2.77300  1.000 26.72000  ? 103 ALA A C   1 
ATOM   773  O  O   . ALA A  1 109 ? 29.12700  -23.99700 3.41800  1.000 29.56000  ? 103 ALA A O   1 
ATOM   774  C  CB  . ALA A  1 109 ? 29.30100  -23.58800 0.40200  1.000 26.41000  ? 103 ALA A CB  1 
ATOM   775  N  N   . ASP A  1 110 ? 31.29500  -23.49500 3.11900  1.000 24.78000  ? 104 ASP A N   1 
ATOM   776  C  CA  . ASP A  1 110 ? 31.69800  -24.14200 4.35400  1.000 28.04000  ? 104 ASP A CA  1 
ATOM   777  C  C   . ASP A  1 110 ? 31.49800  -23.27500 5.59300  1.000 26.47000  ? 104 ASP A C   1 
ATOM   778  O  O   . ASP A  1 110 ? 31.45300  -23.82800 6.69700  1.000 26.14000  ? 104 ASP A O   1 
ATOM   779  C  CB  . ASP A  1 110 ? 33.16600  -24.57500 4.27600  1.000 25.20000  ? 104 ASP A CB  1 
ATOM   780  C  CG  . ASP A  1 110 ? 33.43100  -25.53200 3.12500  1.000 31.09000  ? 104 ASP A CG  1 
ATOM   781  O  OD1 . ASP A  1 110 ? 32.61600  -26.46900 2.90600  1.000 33.37000  ? 104 ASP A OD1 1 
ATOM   782  O  OD2 . ASP A  1 110 ? 34.47200  -25.33800 2.44700  1.000 30.46000  ? 104 ASP A OD2 1 
ATOM   783  N  N   . LEU A  1 111 ? 31.39700  -21.95000 5.45300  1.000 22.90000  ? 105 LEU A N   1 
ATOM   784  C  CA  . LEU A  1 111 ? 31.12200  -21.10000 6.60600  1.000 20.70000  ? 105 LEU A CA  1 
ATOM   785  C  C   . LEU A  1 111 ? 29.76800  -21.43800 7.22500  1.000 25.55000  ? 105 LEU A C   1 
ATOM   786  O  O   . LEU A  1 111 ? 28.79700  -21.71900 6.52000  1.000 23.54000  ? 105 LEU A O   1 
ATOM   787  C  CB  . LEU A  1 111 ? 31.12500  -19.62600 6.18400  1.000 22.91000  ? 105 LEU A CB  1 
ATOM   788  C  CG  . LEU A  1 111 ? 32.47700  -19.10300 5.70000  1.000 25.68000  ? 105 LEU A CG  1 
ATOM   789  C  CD1 . LEU A  1 111 ? 32.27000  -17.72700 5.09100  1.000 21.13000  ? 105 LEU A CD1 1 
ATOM   790  C  CD2 . LEU A  1 111 ? 33.49100  -19.09700 6.84800  1.000 23.32000  ? 105 LEU A CD2 1 
ATOM   791  N  N   . ARG A  1 112 ? 29.69100  -21.36500 8.55400  1.000 21.20000  ? 106 ARG A N   1 
ATOM   792  C  CA  . ARG A  1 112 ? 28.45100  -21.59200 9.27600  1.000 21.40000  ? 106 ARG A CA  1 
ATOM   793  C  C   . ARG A  1 112 ? 27.92800  -20.33400 9.96700  1.000 21.98000  ? 106 ARG A C   1 
ATOM   794  O  O   . ARG A  1 112 ? 27.03600  -20.43200 10.81700 1.000 23.19000  ? 106 ARG A O   1 
ATOM   795  C  CB  . ARG A  1 112 ? 28.63300  -22.71400 10.30100 1.000 24.71000  ? 106 ARG A CB  1 
ATOM   796  C  CG  . ARG A  1 112 ? 28.95800  -24.08700 9.67500  1.000 28.62000  ? 106 ARG A CG  1 
ATOM   797  C  CD  . ARG A  1 112 ? 27.75100  -24.61700 8.89100  1.000 29.84000  ? 106 ARG A CD  1 
ATOM   798  N  NE  . ARG A  1 112 ? 28.09000  -25.80900 8.11600  1.000 31.29000  ? 106 ARG A NE  1 
ATOM   799  C  CZ  . ARG A  1 112 ? 28.29600  -25.81600 6.80400  1.000 32.94000  ? 106 ARG A CZ  1 
ATOM   800  N  NH1 . ARG A  1 112 ? 28.21300  -24.70100 6.08500  1.000 31.39000  ? 106 ARG A NH1 1 
ATOM   801  N  NH2 . ARG A  1 112 ? 28.56000  -26.97600 6.19200  1.000 32.16000  ? 106 ARG A NH2 1 
ATOM   802  N  N   . CYS A  1 113 ? 28.46100  -19.16800 9.62900  1.000 22.74000  ? 107 CYS A N   1 
ATOM   803  C  CA  . CYS A  1 113 ? 27.92300  -17.87500 10.04100 1.000 20.93000  ? 107 CYS A CA  1 
ATOM   804  C  C   . CYS A  1 113 ? 27.03100  -17.33000 8.92700  1.000 21.15000  ? 107 CYS A C   1 
ATOM   805  O  O   . CYS A  1 113 ? 27.12200  -17.75600 7.77500  1.000 21.32000  ? 107 CYS A O   1 
ATOM   806  C  CB  . CYS A  1 113 ? 29.06500  -16.87800 10.33600 1.000 20.14000  ? 107 CYS A CB  1 
ATOM   807  S  SG  . CYS A  1 113 ? 30.36700  -16.78000 9.06500  1.000 23.21000  ? 107 CYS A SG  1 
ATOM   808  N  N   . GLY A  1 114 ? 26.16200  -16.38700 9.27800  1.000 21.86000  ? 108 GLY A N   1 
ATOM   809  C  CA  . GLY A  1 114 ? 25.25600  -15.78500 8.30900  1.000 25.08000  ? 108 GLY A CA  1 
ATOM   810  C  C   . GLY A  1 114 ? 25.48700  -14.30000 8.09300  1.000 23.00000  ? 108 GLY A C   1 
ATOM   811  O  O   . GLY A  1 114 ? 26.12000  -13.64000 8.92200  1.000 20.26000  ? 108 GLY A O   1 
ATOM   812  N  N   . GLY A  1 115 ? 25.00600  -13.76100 6.98000  1.000 21.85000  ? 109 GLY A N   1 
ATOM   813  C  CA  . GLY A  1 115 ? 25.13900  -12.33500 6.72900  1.000 21.61000  ? 109 GLY A CA  1 
ATOM   814  C  C   . GLY A  1 115 ? 24.18200  -11.49700 7.55100  1.000 23.18000  ? 109 GLY A C   1 
ATOM   815  O  O   . GLY A  1 115 ? 23.21600  -12.01000 8.12400  1.000 21.87000  ? 109 GLY A O   1 
ATOM   816  N  N   . HIS A  1 116 ? 24.44600  -10.18600 7.59100  1.000 22.44000  ? 110 HIS A N   1 
ATOM   817  C  CA  . HIS A  1 116 ? 23.66400  -9.26000  8.40700  1.000 18.98000  ? 110 HIS A CA  1 
ATOM   818  C  C   . HIS A  1 116 ? 23.93900  -7.84100  7.93200  1.000 23.37000  ? 110 HIS A C   1 
ATOM   819  O  O   . HIS A  1 116 ? 24.98100  -7.58600  7.30900  1.000 21.19000  ? 110 HIS A O   1 
ATOM   820  C  CB  . HIS A  1 116 ? 24.03100  -9.39900  9.88700  1.000 22.70000  ? 110 HIS A CB  1 
ATOM   821  C  CG  . HIS A  1 116 ? 25.49900  -9.26800  10.14000 1.000 21.89000  ? 110 HIS A CG  1 
ATOM   822  N  ND1 . HIS A  1 116 ? 26.13300  -8.04500  10.19700 1.000 24.13000  ? 110 HIS A ND1 1 
ATOM   823  C  CD2 . HIS A  1 116 ? 26.46400  -10.20100 10.32200 1.000 23.94000  ? 110 HIS A CD2 1 
ATOM   824  C  CE1 . HIS A  1 116 ? 27.42900  -8.23000  10.41700 1.000 18.80000  ? 110 HIS A CE1 1 
ATOM   825  N  NE2 . HIS A  1 116 ? 27.65500  -9.52800  10.49800 1.000 20.89000  ? 110 HIS A NE2 1 
ATOM   826  N  N   . PRO A  1 117 ? 23.04600  -6.88500  8.23300  1.000 21.84000  ? 111 PRO A N   1 
ATOM   827  C  CA  . PRO A  1 117 ? 23.35200  -5.48900  7.90900  1.000 22.56000  ? 111 PRO A CA  1 
ATOM   828  C  C   . PRO A  1 117 ? 24.69800  -5.10300  8.50300  1.000 19.90000  ? 111 PRO A C   1 
ATOM   829  O  O   . PRO A  1 117 ? 25.06700  -5.53700  9.60000  1.000 18.90000  ? 111 PRO A O   1 
ATOM   830  C  CB  . PRO A  1 117 ? 22.19300  -4.70500  8.54400  1.000 20.66000  ? 111 PRO A CB  1 
ATOM   831  C  CG  . PRO A  1 117 ? 21.08400  -5.69100  8.67200  1.000 24.56000  ? 111 PRO A CG  1 
ATOM   832  C  CD  . PRO A  1 117 ? 21.74200  -7.01000  8.92100  1.000 18.71000  ? 111 PRO A CD  1 
ATOM   833  N  N   . SER A  1 118 ? 25.44300  -4.29500  7.76000  1.000 21.21000  ? 112 SER A N   1 
ATOM   834  C  CA  . SER A  1 118 ? 26.81300  -3.99700  8.15300  1.000 21.76000  ? 112 SER A CA  1 
ATOM   835  C  C   . SER A  1 118 ? 26.85900  -3.21400  9.46100  1.000 21.72000  ? 112 SER A C   1 
ATOM   836  O  O   . SER A  1 118 ? 25.95300  -2.42800  9.77700  1.000 21.33000  ? 112 SER A O   1 
ATOM   837  C  CB  . SER A  1 118 ? 27.53200  -3.20100  7.06300  1.000 17.56000  ? 112 SER A CB  1 
ATOM   838  O  OG  . SER A  1 118 ? 28.77700  -2.74700  7.57500  1.000 22.74000  ? 112 SER A OG  1 
ATOM   839  N  N   . LEU A  1 119 ? 27.93900  -3.42900  10.22400 1.000 19.50000  ? 113 LEU A N   1 
ATOM   840  C  CA  . LEU A  1 119 ? 28.12500  -2.68300  11.46300 1.000 19.52000  ? 113 LEU A CA  1 
ATOM   841  C  C   . LEU A  1 119 ? 28.44600  -1.21400  11.19700 1.000 25.52000  ? 113 LEU A C   1 
ATOM   842  O  O   . LEU A  1 119 ? 28.35600  -0.39600  12.11900 1.000 24.96000  ? 113 LEU A O   1 
ATOM   843  C  CB  . LEU A  1 119 ? 29.23000  -3.33200  12.31800 1.000 20.79000  ? 113 LEU A CB  1 
ATOM   844  C  CG  . LEU A  1 119 ? 29.05900  -4.77800  12.78000 1.000 20.92000  ? 113 LEU A CG  1 
ATOM   845  C  CD1 . LEU A  1 119 ? 30.05200  -5.24100  13.87800 1.000 17.80000  ? 113 LEU A CD1 1 
ATOM   846  C  CD2 . LEU A  1 119 ? 27.64200  -5.07600  13.23300 1.000 21.48000  ? 113 LEU A CD2 1 
ATOM   847  N  N   . SER A  1 120 ? 28.83000  -0.87600  9.96400  1.000 21.90000  ? 114 SER A N   1 
ATOM   848  C  CA  . SER A  1 120 ? 29.00200  0.49500   9.51200  1.000 21.08000  ? 114 SER A CA  1 
ATOM   849  C  C   . SER A  1 120 ? 27.74000  0.94100   8.79700  1.000 22.78000  ? 114 SER A C   1 
ATOM   850  O  O   . SER A  1 120 ? 27.34000  0.33200   7.79700  1.000 21.44000  ? 114 SER A O   1 
ATOM   851  C  CB  . SER A  1 120 ? 30.19300  0.60500   8.56300  1.000 23.71000  ? 114 SER A CB  1 
ATOM   852  O  OG  . SER A  1 120 ? 30.11900  1.83100   7.84500  1.000 20.58000  ? 114 SER A OG  1 
ATOM   853  N  N   . GLU A  1 121 ? 27.10300  2.00700   9.30200  1.000 26.57000  ? 115 GLU A N   1 
ATOM   854  C  CA  A GLU A  1 121 ? 25.90000  2.53400   8.65500  0.500 25.28000  ? 115 GLU A CA  1 
ATOM   855  C  CA  B GLU A  1 121 ? 25.88700  2.41000   8.61600  0.500 25.27000  ? 115 GLU A CA  1 
ATOM   856  C  C   . GLU A  1 121 ? 26.21100  2.94600   7.22600  1.000 23.54000  ? 115 GLU A C   1 
ATOM   857  O  O   . GLU A  1 121 ? 25.41900  2.74100   6.30000  1.000 21.36000  ? 115 GLU A O   1 
ATOM   858  C  CB  A GLU A  1 121 ? 25.35900  3.72400   9.45100  0.500 27.84000  ? 115 GLU A CB  1 
ATOM   859  C  CB  B GLU A  1 121 ? 25.09000  3.38000   9.48500  0.500 28.38000  ? 115 GLU A CB  1 
ATOM   860  C  CG  A GLU A  1 121 ? 24.79300  3.37700   10.83600 0.500 29.55000  ? 115 GLU A CG  1 
ATOM   861  C  CG  B GLU A  1 121 ? 24.51700  2.67700   10.76000 0.500 27.28000  ? 115 GLU A CG  1 
ATOM   862  C  CD  A GLU A  1 121 ? 25.85500  3.24500   11.93100 0.500 31.36000  ? 115 GLU A CD  1 
ATOM   863  C  CD  B GLU A  1 121 ? 23.90600  1.28800   10.49200 0.500 28.64000  ? 115 GLU A CD  1 
ATOM   864  O  OE1 A GLU A  1 121 ? 27.05600  3.51800   11.68200 0.500 29.72000  ? 115 GLU A OE1 1 
ATOM   865  O  OE1 B GLU A  1 121 ? 22.76700  1.22100   9.96200  0.500 27.86000  ? 115 GLU A OE1 1 
ATOM   866  O  OE2 A GLU A  1 121 ? 25.47300  2.86200   13.05600 0.500 33.05000  ? 115 GLU A OE2 1 
ATOM   867  O  OE2 B GLU A  1 121 ? 24.57000  0.25400   10.80600 0.500 28.12000  ? 115 GLU A OE2 1 
ATOM   868  N  N   . MET A  1 122 ? 27.39700  3.50400   7.02600  1.000 24.46000  ? 116 MET A N   1 
ATOM   869  C  CA  . MET A  1 122 ? 27.77500  3.95500   5.69400  1.000 24.56000  ? 116 MET A CA  1 
ATOM   870  C  C   . MET A  1 122 ? 27.89700  2.78700   4.72300  1.000 22.56000  ? 116 MET A C   1 
ATOM   871  O  O   . MET A  1 122 ? 27.43000  2.88400   3.58400  1.000 22.73000  ? 116 MET A O   1 
ATOM   872  C  CB  . MET A  1 122 ? 29.08700  4.73200   5.75800  1.000 25.79000  ? 116 MET A CB  1 
ATOM   873  C  CG  . MET A  1 122 ? 29.53400  5.26600   4.42300  1.000 29.00000  ? 116 MET A CG  1 
ATOM   874  S  SD  . MET A  1 122 ? 30.98600  6.33600   4.60500  1.000 31.91000  ? 116 MET A SD  1 
ATOM   875  C  CE  . MET A  1 122 ? 30.35200  7.57000   5.74900  1.000 30.26000  ? 116 MET A CE  1 
ATOM   876  N  N   . VAL A  1 123 ? 28.54800  1.69200   5.14200  1.000 20.73000  ? 117 VAL A N   1 
ATOM   877  C  CA  . VAL A  1 123 ? 28.61100  0.49400   4.30100  1.000 23.00000  ? 117 VAL A CA  1 
ATOM   878  C  C   . VAL A  1 123 ? 27.21300  -0.00700  4.01300  1.000 21.44000  ? 117 VAL A C   1 
ATOM   879  O  O   . VAL A  1 123 ? 26.86500  -0.33200  2.87200  1.000 22.32000  ? 117 VAL A O   1 
ATOM   880  C  CB  . VAL A  1 123 ? 29.45200  -0.61600  4.96200  1.000 21.71000  ? 117 VAL A CB  1 
ATOM   881  C  CG1 . VAL A  1 123 ? 29.31500  -1.94500  4.14300  1.000 20.71000  ? 117 VAL A CG1 1 
ATOM   882  C  CG2 . VAL A  1 123 ? 30.90400  -0.19400  5.13400  1.000 20.56000  ? 117 VAL A CG2 1 
ATOM   883  N  N   . ASN A  1 124 ? 26.39200  -0.09200  5.05700  1.000 22.87000  ? 118 ASN A N   1 
ATOM   884  C  CA  . ASN A  1 124 ? 25.03400  -0.57100  4.87300  1.000 20.65000  ? 118 ASN A CA  1 
ATOM   885  C  C   . ASN A  1 124 ? 24.26000  0.28300   3.87900  1.000 21.23000  ? 118 ASN A C   1 
ATOM   886  O  O   . ASN A  1 124 ? 23.51800  -0.25100  3.04900  1.000 23.02000  ? 118 ASN A O   1 
ATOM   887  C  CB  . ASN A  1 124 ? 24.28500  -0.63100  6.20300  1.000 23.37000  ? 118 ASN A CB  1 
ATOM   888  C  CG  . ASN A  1 124 ? 23.25000  -1.72600  6.18300  1.000 24.81000  ? 118 ASN A CG  1 
ATOM   889  O  OD1 . ASN A  1 124 ? 23.55800  -2.84800  5.76100  1.000 22.86000  ? 118 ASN A OD1 1 
ATOM   890  N  ND2 . ASN A  1 124 ? 22.00600  -1.40700  6.53700  1.000 24.87000  ? 118 ASN A ND2 1 
ATOM   891  N  N   . ARG A  1 125 ? 24.38000  1.61000   3.95900  1.000 22.78000  ? 119 ARG A N   1 
ATOM   892  C  CA  . ARG A  1 125 ? 23.68300  2.45900   2.98400  1.000 21.94000  ? 119 ARG A CA  1 
ATOM   893  C  C   . ARG A  1 125 ? 24.15800  2.16500   1.56300  1.000 23.18000  ? 119 ARG A C   1 
ATOM   894  O  O   . ARG A  1 125 ? 23.36300  2.12100   0.61900  1.000 20.93000  ? 119 ARG A O   1 
ATOM   895  C  CB  . ARG A  1 125 ? 23.90500  3.94500   3.31100  1.000 24.49000  ? 119 ARG A CB  1 
ATOM   896  C  CG  . ARG A  1 125 ? 23.18300  4.45400   4.58200  1.000 27.26000  ? 119 ARG A CG  1 
ATOM   897  C  CD  . ARG A  1 125 ? 23.11200  5.99900   4.61000  1.000 29.26000  ? 119 ARG A CD  1 
ATOM   898  N  NE  . ARG A  1 125 ? 24.43600  6.61400   4.66500  1.000 33.41000  ? 119 ARG A NE  1 
ATOM   899  C  CZ  . ARG A  1 125 ? 25.13400  6.77400   5.78200  1.000 31.71000  ? 119 ARG A CZ  1 
ATOM   900  N  NH1 . ARG A  1 125 ? 24.66700  6.36400   6.95400  1.000 32.22000  ? 119 ARG A NH1 1 
ATOM   901  N  NH2 . ARG A  1 125 ? 26.33500  7.34700   5.72300  1.000 31.39000  ? 119 ARG A NH2 1 
ATOM   902  N  N   . SER A  1 126 ? 25.46300  1.98300   1.39000  1.000 23.48000  ? 120 SER A N   1 
ATOM   903  C  CA  . SER A  1 126 ? 25.97700  1.55800   0.09200  1.000 22.90000  ? 120 SER A CA  1 
ATOM   904  C  C   . SER A  1 126 ? 25.38000  0.20700   -0.34000 1.000 20.34000  ? 120 SER A C   1 
ATOM   905  O  O   . SER A  1 126 ? 25.02300  0.01900   -1.51100 1.000 21.07000  ? 120 SER A O   1 
ATOM   906  C  CB  . SER A  1 126 ? 27.50600  1.47900   0.16600  1.000 25.04000  ? 120 SER A CB  1 
ATOM   907  O  OG  . SER A  1 126 ? 28.02700  1.05400   -1.06800 1.000 26.97000  ? 120 SER A OG  1 
ATOM   908  N  N   . TRP A  1 127 ? 25.24600  -0.73600  0.58800  1.000 19.57000  ? 121 TRP A N   1 
ATOM   909  C  CA  . TRP A  1 127 ? 24.61900  -2.01200  0.24700  1.000 21.95000  ? 121 TRP A CA  1 
ATOM   910  C  C   . TRP A  1 127 ? 23.16200  -1.81400  -0.15300 1.000 20.75000  ? 121 TRP A C   1 
ATOM   911  O  O   . TRP A  1 127 ? 22.69900  -2.37900  -1.13900 1.000 20.87000  ? 121 TRP A O   1 
ATOM   912  C  CB  . TRP A  1 127 ? 24.68800  -2.97000  1.42400  1.000 18.80000  ? 121 TRP A CB  1 
ATOM   913  C  CG  . TRP A  1 127 ? 26.02100  -3.53300  1.70300  1.000 21.78000  ? 121 TRP A CG  1 
ATOM   914  C  CD1 . TRP A  1 127 ? 27.20600  -3.30800  1.00300  1.000 21.41000  ? 121 TRP A CD1 1 
ATOM   915  C  CD2 . TRP A  1 127 ? 26.33700  -4.44900  2.73900  1.000 19.61000  ? 121 TRP A CD2 1 
ATOM   916  N  NE1 . TRP A  1 127 ? 28.22700  -4.03300  1.56800  1.000 22.08000  ? 121 TRP A NE1 1 
ATOM   917  C  CE2 . TRP A  1 127 ? 27.72100  -4.74400  2.63200  1.000 21.96000  ? 121 TRP A CE2 1 
ATOM   918  C  CE3 . TRP A  1 127 ? 25.58600  -5.06500  3.75700  1.000 20.27000  ? 121 TRP A CE3 1 
ATOM   919  C  CZ2 . TRP A  1 127 ? 28.36300  -5.62800  3.50100  1.000 20.82000  ? 121 TRP A CZ2 1 
ATOM   920  C  CZ3 . TRP A  1 127 ? 26.24200  -5.94300  4.61500  1.000 18.99000  ? 121 TRP A CZ3 1 
ATOM   921  C  CH2 . TRP A  1 127 ? 27.61000  -6.19700  4.48600  1.000 17.28000  ? 121 TRP A CH2 1 
ATOM   922  N  N   . ILE A  1 128 ? 22.42300  -1.01400  0.62300  1.000 20.89000  ? 122 ILE A N   1 
ATOM   923  C  CA  . ILE A  1 128 ? 21.01100  -0.79800  0.32000  1.000 22.20000  ? 122 ILE A CA  1 
ATOM   924  C  C   . ILE A  1 128 ? 20.85700  -0.16700  -1.05400 1.000 21.80000  ? 122 ILE A C   1 
ATOM   925  O  O   . ILE A  1 128 ? 19.96600  -0.53400  -1.83400 1.000 23.04000  ? 122 ILE A O   1 
ATOM   926  C  CB  . ILE A  1 128 ? 20.36200  0.07200   1.41200  1.000 24.06000  ? 122 ILE A CB  1 
ATOM   927  C  CG1 . ILE A  1 128 ? 20.16300  -0.73100  2.70100  1.000 24.11000  ? 122 ILE A CG1 1 
ATOM   928  C  CG2 . ILE A  1 128 ? 19.06200  0.60500   0.92000  1.000 22.67000  ? 122 ILE A CG2 1 
ATOM   929  C  CD1 . ILE A  1 128 ? 19.88600  0.15000   3.92500  1.000 23.78000  ? 122 ILE A CD1 1 
ATOM   930  N  N   . LYS A  1 129 ? 21.72500  0.78300   -1.38300 1.000 21.93000  ? 123 LYS A N   1 
ATOM   931  C  CA  . LYS A  1 129 ? 21.61600  1.42600   -2.68300 1.000 22.98000  ? 123 LYS A CA  1 
ATOM   932  C  C   . LYS A  1 129 ? 21.75600  0.41600   -3.81700 1.000 23.51000  ? 123 LYS A C   1 
ATOM   933  O  O   . LYS A  1 129 ? 21.16000  0.60200   -4.88300 1.000 24.57000  ? 123 LYS A O   1 
ATOM   934  C  CB  . LYS A  1 129 ? 22.66400  2.54600   -2.81500 1.000 23.17000  ? 123 LYS A CB  1 
ATOM   935  C  CG  . LYS A  1 129 ? 22.72800  3.15600   -4.18500 1.000 24.39000  ? 123 LYS A CG  1 
ATOM   936  C  CD  . LYS A  1 129 ? 23.69800  4.35500   -4.22300 1.000 24.76000  ? 123 LYS A CD  1 
ATOM   937  C  CE  . LYS A  1 129 ? 23.75900  4.97600   -5.63100 1.000 29.66000  ? 123 LYS A CE  1 
ATOM   938  N  NZ  . LYS A  1 129 ? 24.70100  6.13600   -5.70400 1.000 27.93000  ? 123 LYS A NZ  1 
ATOM   939  N  N   . GLN A  1 130 ? 22.51800  -0.65800  -3.60900 1.000 22.93000  ? 124 GLN A N   1 
ATOM   940  C  CA  . GLN A  1 130 ? 22.83600  -1.57700  -4.69200 1.000 23.58000  ? 124 GLN A CA  1 
ATOM   941  C  C   . GLN A  1 130 ? 22.07400  -2.88100  -4.56900 1.000 23.57000  ? 124 GLN A C   1 
ATOM   942  O  O   . GLN A  1 130 ? 22.40800  -3.84900  -5.25500 1.000 24.55000  ? 124 GLN A O   1 
ATOM   943  C  CB  . GLN A  1 130 ? 24.34600  -1.82500  -4.73800 1.000 23.27000  ? 124 GLN A CB  1 
ATOM   944  C  CG  . GLN A  1 130 ? 25.13200  -0.49400  -4.83200 1.000 23.48000  ? 124 GLN A CG  1 
ATOM   945  C  CD  . GLN A  1 130 ? 26.63600  -0.68700  -4.64100 1.000 25.01000  ? 124 GLN A CD  1 
ATOM   946  O  OE1 . GLN A  1 130 ? 27.33600  -1.10400  -5.57400 1.000 24.13000  ? 124 GLN A OE1 1 
ATOM   947  N  NE2 . GLN A  1 130 ? 27.13700  -0.37700  -3.43800 1.000 22.19000  ? 124 GLN A NE2 1 
ATOM   948  N  N   . ASP A  1 131 ? 21.06200  -2.92500  -3.70100 1.000 24.40000  ? 125 ASP A N   1 
ATOM   949  C  CA  . ASP A  1 131 ? 20.24600  -4.12400  -3.50400 1.000 24.45000  ? 125 ASP A CA  1 
ATOM   950  C  C   . ASP A  1 131 ? 21.08200  -5.33400  -3.08800 1.000 26.05000  ? 125 ASP A C   1 
ATOM   951  O  O   . ASP A  1 131 ? 20.76300  -6.48100  -3.44400 1.000 25.34000  ? 125 ASP A O   1 
ATOM   952  C  CB  . ASP A  1 131 ? 19.44000  -4.43100  -4.76500 1.000 26.39000  ? 125 ASP A CB  1 
ATOM   953  C  CG  . ASP A  1 131 ? 18.42500  -3.34200  -5.08500 1.000 33.84000  ? 125 ASP A CG  1 
ATOM   954  O  OD1 . ASP A  1 131 ? 17.68600  -2.94100  -4.16400 1.000 35.88000  ? 125 ASP A OD1 1 
ATOM   955  O  OD2 . ASP A  1 131 ? 18.38100  -2.87700  -6.24600 1.000 39.45000  ? 125 ASP A OD2 1 
ATOM   956  N  N   . PHE A  1 132 ? 22.15200  -5.11400  -2.33400 1.000 22.48000  ? 126 PHE A N   1 
ATOM   957  C  CA  . PHE A  1 132 ? 23.04700  -6.21800  -1.98300 1.000 23.43000  ? 126 PHE A CA  1 
ATOM   958  C  C   . PHE A  1 132 ? 22.51800  -6.99700  -0.78500 1.000 23.68000  ? 126 PHE A C   1 
ATOM   959  O  O   . PHE A  1 132 ? 22.22300  -6.41200  0.26200  1.000 23.10000  ? 126 PHE A O   1 
ATOM   960  C  CB  . PHE A  1 132 ? 24.44100  -5.68800  -1.66000 1.000 23.40000  ? 126 PHE A CB  1 
ATOM   961  C  CG  . PHE A  1 132 ? 25.40300  -6.76900  -1.24300 1.000 22.59000  ? 126 PHE A CG  1 
ATOM   962  C  CD1 . PHE A  1 132 ? 25.80000  -7.72600  -2.16300 1.000 23.53000  ? 126 PHE A CD1 1 
ATOM   963  C  CD2 . PHE A  1 132 ? 25.88300  -6.84700  0.06900  1.000 22.74000  ? 126 PHE A CD2 1 
ATOM   964  C  CE1 . PHE A  1 132 ? 26.67400  -8.74400  -1.79300 1.000 22.88000  ? 126 PHE A CE1 1 
ATOM   965  C  CE2 . PHE A  1 132 ? 26.76100  -7.86400  0.44300  1.000 22.54000  ? 126 PHE A CE2 1 
ATOM   966  C  CZ  . PHE A  1 132 ? 27.15700  -8.80000  -0.50300 1.000 20.76000  ? 126 PHE A CZ  1 
ATOM   967  N  N   . ILE A  1 133 ? 22.41600  -8.31700  -0.92700 1.000 23.03000  ? 127 ILE A N   1 
ATOM   968  C  CA  . ILE A  1 133 ? 22.03800  -9.20300  0.17200  1.000 24.78000  ? 127 ILE A CA  1 
ATOM   969  C  C   . ILE A  1 133 ? 23.32400  -9.77900  0.76300  1.000 22.38000  ? 127 ILE A C   1 
ATOM   970  O  O   . ILE A  1 133 ? 24.00400  -10.54900 0.07800  1.000 25.61000  ? 127 ILE A O   1 
ATOM   971  C  CB  . ILE A  1 133 ? 21.10900  -10.32600 -0.30000 1.000 23.76000  ? 127 ILE A CB  1 
ATOM   972  C  CG1 . ILE A  1 133 ? 19.85200  -9.74900  -0.95000 1.000 28.60000  ? 127 ILE A CG1 1 
ATOM   973  C  CG2 . ILE A  1 133 ? 20.72100  -11.23700 0.87800  1.000 29.25000  ? 127 ILE A CG2 1 
ATOM   974  C  CD1 . ILE A  1 133 ? 19.26000  -10.70400 -1.97300 1.000 32.60000  ? 127 ILE A CD1 1 
ATOM   975  N  N   . PRO A  1 134 ? 23.69000  -9.44100  1.99700  1.000 21.72000  ? 128 PRO A N   1 
ATOM   976  C  CA  . PRO A  1 134 ? 24.90800  -10.01600 2.58100  1.000 21.94000  ? 128 PRO A CA  1 
ATOM   977  C  C   . PRO A  1 134 ? 24.79200  -11.52500 2.78900  1.000 27.11000  ? 128 PRO A C   1 
ATOM   978  O  O   . PRO A  1 134 ? 23.72300  -12.06600 3.10700  1.000 22.94000  ? 128 PRO A O   1 
ATOM   979  C  CB  . PRO A  1 134 ? 25.04700  -9.27800  3.92100  1.000 23.84000  ? 128 PRO A CB  1 
ATOM   980  C  CG  . PRO A  1 134 ? 23.67300  -8.79200  4.23700  1.000 24.94000  ? 128 PRO A CG  1 
ATOM   981  C  CD  . PRO A  1 134 ? 23.04200  -8.48500  2.91200  1.000 24.11000  ? 128 PRO A CD  1 
ATOM   982  N  N   . THR A  1 135 ? 25.92200  -12.20100 2.59900  1.000 25.27000  ? 129 THR A N   1 
ATOM   983  C  CA  . THR A  1 135 ? 26.02000  -13.65300 2.71900  1.000 22.42000  ? 129 THR A CA  1 
ATOM   984  C  C   . THR A  1 135 ? 27.02700  -13.99600 3.81700  1.000 21.02000  ? 129 THR A C   1 
ATOM   985  O  O   . THR A  1 135 ? 27.57100  -13.11400 4.47700  1.000 22.76000  ? 129 THR A O   1 
ATOM   986  C  CB  . THR A  1 135 ? 26.40800  -14.27600 1.37400  1.000 24.35000  ? 129 THR A CB  1 
ATOM   987  O  OG1 . THR A  1 135 ? 27.71900  -13.86300 1.00300  1.000 25.90000  ? 129 THR A OG1 1 
ATOM   988  C  CG2 . THR A  1 135 ? 25.47700  -13.83600 0.28400  1.000 27.42000  ? 129 THR A CG2 1 
ATOM   989  N  N   . ALA A  1 136 ? 27.29500  -15.29200 4.00000  1.000 23.06000  ? 130 ALA A N   1 
ATOM   990  C  CA  . ALA A  1 136 ? 28.19500  -15.72000 5.07900  1.000 25.91000  ? 130 ALA A CA  1 
ATOM   991  C  C   . ALA A  1 136 ? 29.53100  -14.97500 5.06200  1.000 21.12000  ? 130 ALA A C   1 
ATOM   992  O  O   . ALA A  1 136 ? 30.02600  -14.51900 6.10900  1.000 19.46000  ? 130 ALA A O   1 
ATOM   993  C  CB  . ALA A  1 136 ? 28.42700  -17.22100 4.97900  1.000 22.13000  ? 130 ALA A CB  1 
ATOM   994  N  N   . VAL A  1 137 ? 30.11500  -14.80200 3.87500  1.000 19.35000  ? 131 VAL A N   1 
ATOM   995  C  CA  . VAL A  1 137 ? 31.44400  -14.20200 3.78100  1.000 21.42000  ? 131 VAL A CA  1 
ATOM   996  C  C   . VAL A  1 137 ? 31.47100  -12.75200 4.25300  1.000 21.69000  ? 131 VAL A C   1 
ATOM   997  O  O   . VAL A  1 137 ? 32.55600  -12.20100 4.51100  1.000 22.84000  ? 131 VAL A O   1 
ATOM   998  C  CB  . VAL A  1 137 ? 31.92600  -14.33600 2.32100  1.000 25.08000  ? 131 VAL A CB  1 
ATOM   999  C  CG1 . VAL A  1 137 ? 31.34100  -13.21100 1.45500  1.000 21.46000  ? 131 VAL A CG1 1 
ATOM   1000 C  CG2 . VAL A  1 137 ? 33.42600  -14.42000 2.24100  1.000 25.96000  ? 131 VAL A CG2 1 
ATOM   1001 N  N   . CYS A  1 138 ? 30.30300  -12.12200 4.38500  1.000 22.32000  ? 132 CYS A N   1 
ATOM   1002 C  CA  . CYS A  1 138 ? 30.19400  -10.75000 4.88200  1.000 21.44000  ? 132 CYS A CA  1 
ATOM   1003 C  C   . CYS A  1 138 ? 30.03900  -10.66800 6.39000  1.000 21.34000  ? 132 CYS A C   1 
ATOM   1004 O  O   . CYS A  1 138 ? 30.06500  -9.56500  6.93000  1.000 21.87000  ? 132 CYS A O   1 
ATOM   1005 C  CB  . CYS A  1 138 ? 28.98800  -10.04600 4.26400  1.000 19.62000  ? 132 CYS A CB  1 
ATOM   1006 S  SG  . CYS A  1 138 ? 28.96900  -10.10000 2.47400  1.000 24.27000  ? 132 CYS A SG  1 
ATOM   1007 N  N   . SER A  1 139 ? 29.86900  -11.79100 7.07900  1.000 20.07000  ? 133 SER A N   1 
ATOM   1008 C  CA  . SER A  1 139 ? 29.67500  -11.74100 8.52100  1.000 19.99000  ? 133 SER A CA  1 
ATOM   1009 C  C   . SER A  1 139 ? 30.79700  -10.97300 9.19400  1.000 18.85000  ? 133 SER A C   1 
ATOM   1010 O  O   . SER A  1 139 ? 31.96500  -11.16900 8.87400  1.000 18.99000  ? 133 SER A O   1 
ATOM   1011 C  CB  . SER A  1 139 ? 29.64200  -13.15100 9.10900  1.000 23.34000  ? 133 SER A CB  1 
ATOM   1012 O  OG  . SER A  1 139 ? 29.80400  -13.02600 10.50900 1.000 26.01000  ? 133 SER A OG  1 
ATOM   1013 N  N   . ASN A  1 140 ? 30.44300  -10.12500 10.17100 1.000 17.04000  ? 134 ASN A N   1 
ATOM   1014 C  CA  . ASN A  1 140 ? 31.48300  -9.44000  10.93200 1.000 20.49000  ? 134 ASN A CA  1 
ATOM   1015 C  C   . ASN A  1 140 ? 32.39100  -10.43900 11.65400 1.000 18.88000  ? 134 ASN A C   1 
ATOM   1016 O  O   . ASN A  1 140 ? 33.50800  -10.08500 12.06200 1.000 19.92000  ? 134 ASN A O   1 
ATOM   1017 C  CB  . ASN A  1 140 ? 30.84600  -8.44900  11.92300 1.000 19.15000  ? 134 ASN A CB  1 
ATOM   1018 C  CG  . ASN A  1 140 ? 30.37200  -9.13100  13.20000 1.000 21.96000  ? 134 ASN A CG  1 
ATOM   1019 O  OD1 . ASN A  1 140 ? 31.03000  -9.04800  14.25300 1.000 22.43000  ? 134 ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A  1 140 ? 29.27400  -9.85400  13.10100 1.000 18.95000  ? 134 ASN A ND2 1 
ATOM   1021 N  N   . CYS A  1 141 ? 31.94300  -11.68200 11.79600 1.000 16.29000  ? 135 CYS A N   1 
ATOM   1022 C  CA  . CYS A  1 141 ? 32.70300  -12.71600 12.46400 1.000 18.93000  ? 135 CYS A CA  1 
ATOM   1023 C  C   . CYS A  1 141 ? 33.38000  -13.64700 11.45600 1.000 18.59000  ? 135 CYS A C   1 
ATOM   1024 O  O   . CYS A  1 141 ? 33.80200  -14.75000 11.82400 1.000 19.42000  ? 135 CYS A O   1 
ATOM   1025 C  CB  . CYS A  1 141 ? 31.76900  -13.48600 13.39800 1.000 21.82000  ? 135 CYS A CB  1 
ATOM   1026 S  SG  . CYS A  1 141 ? 31.03100  -12.42500 14.65500 1.000 20.11000  ? 135 CYS A SG  1 
ATOM   1027 N  N   . SER A  1 142 ? 33.45700  -13.24200 10.18700 1.000 18.22000  ? 136 SER A N   1 
ATOM   1028 C  CA  . SER A  1 142 ? 33.89900  -14.18300 9.15400  1.000 16.68000  ? 136 SER A CA  1 
ATOM   1029 C  C   . SER A  1 142 ? 35.32900  -14.64200 9.40000  1.000 22.16000  ? 136 SER A C   1 
ATOM   1030 O  O   . SER A  1 142 ? 35.67000  -15.79200 9.10600  1.000 21.11000  ? 136 SER A O   1 
ATOM   1031 C  CB  . SER A  1 142 ? 33.79900  -13.55700 7.76600  1.000 18.29000  ? 136 SER A CB  1 
ATOM   1032 O  OG  . SER A  1 142 ? 34.60300  -12.37800 7.66200  1.000 21.56000  ? 136 SER A OG  1 
ATOM   1033 N  N   . GLY A  1 143 ? 36.17500  -13.77100 9.95400  1.000 21.32000  ? 137 GLY A N   1 
ATOM   1034 C  CA  . GLY A  1 143 ? 37.54800  -14.19100 10.21600 1.000 21.13000  ? 137 GLY A CA  1 
ATOM   1035 C  C   . GLY A  1 143 ? 37.63600  -15.26100 11.28900 1.000 20.20000  ? 137 GLY A C   1 
ATOM   1036 O  O   . GLY A  1 143 ? 38.42500  -16.19800 11.17600 1.000 20.95000  ? 137 GLY A O   1 
ATOM   1037 N  N   . LYS A  1 144 ? 36.87100  -15.09700 12.37000 1.000 18.44000  ? 138 LYS A N   1 
ATOM   1038 C  CA  . LYS A  1 144 ? 36.80600  -16.11200 13.41700 1.000 22.47000  ? 138 LYS A CA  1 
ATOM   1039 C  C   . LYS A  1 144 ? 36.33000  -17.44200 12.84700 1.000 21.72000  ? 138 LYS A C   1 
ATOM   1040 O  O   . LYS A  1 144 ? 36.88800  -18.50500 13.15000 1.000 18.83000  ? 138 LYS A O   1 
ATOM   1041 C  CB  . LYS A  1 144 ? 35.86700  -15.63900 14.52600 1.000 19.75000  ? 138 LYS A CB  1 
ATOM   1042 C  CG  . LYS A  1 144 ? 35.52000  -16.74100 15.49700 1.000 19.83000  ? 138 LYS A CG  1 
ATOM   1043 C  CD  . LYS A  1 144 ? 34.68800  -16.19800 16.64000 1.000 20.51000  ? 138 LYS A CD  1 
ATOM   1044 C  CE  . LYS A  1 144 ? 33.36800  -15.61500 16.15000 1.000 20.66000  ? 138 LYS A CE  1 
ATOM   1045 N  NZ  . LYS A  1 144 ? 32.50500  -15.31700 17.31800 1.000 17.68000  ? 138 LYS A NZ  1 
ATOM   1046 N  N   . HIS A  1 145 ? 35.32700  -17.39000 11.96900 1.000 19.80000  ? 139 HIS A N   1 
ATOM   1047 C  CA  . HIS A  1 145 ? 34.79300  -18.62400 11.39900 1.000 21.18000  ? 139 HIS A CA  1 
ATOM   1048 C  C   . HIS A  1 145 ? 35.78600  -19.30700 10.47100 1.000 23.82000  ? 139 HIS A C   1 
ATOM   1049 O  O   . HIS A  1 145 ? 35.87100  -20.54300 10.46400 1.000 20.70000  ? 139 HIS A O   1 
ATOM   1050 C  CB  . HIS A  1 145 ? 33.48000  -18.32400 10.69700 1.000 16.99000  ? 139 HIS A CB  1 
ATOM   1051 C  CG  . HIS A  1 145 ? 32.33500  -18.25900 11.66000 1.000 18.67000  ? 139 HIS A CG  1 
ATOM   1052 N  ND1 . HIS A  1 145 ? 31.47500  -19.31100 11.84800 1.000 17.06000  ? 139 HIS A ND1 1 
ATOM   1053 C  CD2 . HIS A  1 145 ? 31.98300  -17.31500 12.56600 1.000 20.36000  ? 139 HIS A CD2 1 
ATOM   1054 C  CE1 . HIS A  1 145 ? 30.60900  -19.01300 12.80400 1.000 18.13000  ? 139 HIS A CE1 1 
ATOM   1055 N  NE2 . HIS A  1 145 ? 30.90200  -17.80400 13.26200 1.000 22.52000  ? 139 HIS A NE2 1 
ATOM   1056 N  N   . VAL A  1 146 ? 36.52900  -18.54300 9.66800  1.000 20.15000  ? 140 VAL A N   1 
ATOM   1057 C  CA  . VAL A  1 146 ? 37.54400  -19.19600 8.83900  1.000 20.85000  ? 140 VAL A CA  1 
ATOM   1058 C  C   . VAL A  1 146 ? 38.59200  -19.85300 9.72600  1.000 21.64000  ? 140 VAL A C   1 
ATOM   1059 O  O   . VAL A  1 146 ? 39.03200  -20.97700 9.46200  1.000 21.13000  ? 140 VAL A O   1 
ATOM   1060 C  CB  . VAL A  1 146 ? 38.19800  -18.21100 7.85700  1.000 21.51000  ? 140 VAL A CB  1 
ATOM   1061 C  CG1 . VAL A  1 146 ? 39.36400  -18.92200 7.12100  1.000 20.49000  ? 140 VAL A CG1 1 
ATOM   1062 C  CG2 . VAL A  1 146 ? 37.17300  -17.67600 6.84600  1.000 20.63000  ? 140 VAL A CG2 1 
ATOM   1063 N  N   . GLY A  1 147 ? 39.00300  -19.16300 10.79600 1.000 20.75000  ? 141 GLY A N   1 
ATOM   1064 C  CA  . GLY A  1 147 ? 39.95400  -19.76500 11.72200 1.000 21.63000  ? 141 GLY A CA  1 
ATOM   1065 C  C   . GLY A  1 147 ? 39.43400  -21.05400 12.34400 1.000 22.18000  ? 141 GLY A C   1 
ATOM   1066 O  O   . GLY A  1 147 ? 40.16600  -22.03400 12.47400 1.000 21.08000  ? 141 GLY A O   1 
ATOM   1067 N  N   . MET A  1 148 ? 38.16600  -21.07700 12.72900 1.000 19.44000  ? 142 MET A N   1 
ATOM   1068 C  CA  A MET A  1 148 ? 37.63300  -22.30100 13.30900 0.600 20.58000  ? 142 MET A CA  1 
ATOM   1069 C  CA  B MET A  1 148 ? 37.57700  -22.29000 13.30000 0.400 20.59000  ? 142 MET A CA  1 
ATOM   1070 C  C   . MET A  1 148 ? 37.50100  -23.40000 12.26300 1.000 21.64000  ? 142 MET A C   1 
ATOM   1071 O  O   . MET A  1 148 ? 37.76600  -24.56500 12.56600 1.000 23.72000  ? 142 MET A O   1 
ATOM   1072 C  CB  A MET A  1 148 ? 36.31100  -22.01300 14.00100 0.600 21.11000  ? 142 MET A CB  1 
ATOM   1073 C  CB  B MET A  1 148 ? 36.17700  -22.00500 13.84600 0.400 21.12000  ? 142 MET A CB  1 
ATOM   1074 C  CG  A MET A  1 148 ? 36.53700  -21.23600 15.27300 0.600 22.02000  ? 142 MET A CG  1 
ATOM   1075 C  CG  B MET A  1 148 ? 36.11000  -20.98000 14.94700 0.400 22.22000  ? 142 MET A CG  1 
ATOM   1076 S  SD  A MET A  1 148 ? 35.01000  -20.91900 16.14300 0.600 19.36000  ? 142 MET A SD  1 
ATOM   1077 S  SD  B MET A  1 148 ? 36.59200  -21.57000 16.57700 0.400 23.38000  ? 142 MET A SD  1 
ATOM   1078 C  CE  A MET A  1 148 ? 35.53500  -19.76900 17.40900 0.600 19.49000  ? 142 MET A CE  1 
ATOM   1079 C  CE  B MET A  1 148 ? 36.48100  -20.02200 17.46900 0.400 21.69000  ? 142 MET A CE  1 
ATOM   1080 N  N   . LEU A  1 149 ? 37.12600  -23.05100 11.03200 1.000 20.67000  ? 143 LEU A N   1 
ATOM   1081 C  CA  . LEU A  1 149 ? 37.20400  -24.01500 9.93800  1.000 19.57000  ? 143 LEU A CA  1 
ATOM   1082 C  C   . LEU A  1 149 ? 38.61200  -24.55400 9.80800  1.000 22.46000  ? 143 LEU A C   1 
ATOM   1083 O  O   . LEU A  1 149 ? 38.82600  -25.76900 9.64900  1.000 25.07000  ? 143 LEU A O   1 
ATOM   1084 C  CB  . LEU A  1 149 ? 36.81000  -23.34900 8.61900  1.000 24.61000  ? 143 LEU A CB  1 
ATOM   1085 C  CG  . LEU A  1 149 ? 35.39000  -23.47200 8.08000  1.000 31.74000  ? 143 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A  1 149 ? 35.24400  -22.59300 6.82700  1.000 26.41000  ? 143 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A  1 149 ? 35.10100  -24.94700 7.77700  1.000 31.15000  ? 143 LEU A CD2 1 
ATOM   1088 N  N   . ALA A  1 150 ? 39.59300  -23.64900 9.85300  1.000 23.63000  ? 144 ALA A N   1 
ATOM   1089 C  CA  . ALA A  1 150 ? 40.98400  -24.04400 9.69400  1.000 22.60000  ? 144 ALA A CA  1 
ATOM   1090 C  C   . ALA A  1 150 ? 41.37900  -25.03100 10.77600 1.000 23.95000  ? 144 ALA A C   1 
ATOM   1091 O  O   . ALA A  1 150 ? 41.97800  -26.06900 10.49400 1.000 25.90000  ? 144 ALA A O   1 
ATOM   1092 C  CB  . ALA A  1 150 ? 41.89400  -22.81700 9.72900  1.000 23.20000  ? 144 ALA A CB  1 
ATOM   1093 N  N   . GLY A  1 151 ? 41.03100  -24.72700 12.02600 1.000 25.25000  ? 145 GLY A N   1 
ATOM   1094 C  CA  . GLY A  1 151 ? 41.39900  -25.61700 13.11100 1.000 22.38000  ? 145 GLY A CA  1 
ATOM   1095 C  C   . GLY A  1 151 ? 40.73700  -26.97300 12.99300 1.000 24.94000  ? 145 GLY A C   1 
ATOM   1096 O  O   . GLY A  1 151 ? 41.35600  -27.99500 13.27800 1.000 25.09000  ? 145 GLY A O   1 
ATOM   1097 N  N   . ALA A  1 152 ? 39.45900  -26.99900 12.59400 1.000 21.94000  ? 146 ALA A N   1 
ATOM   1098 C  CA  . ALA A  1 152 ? 38.77900  -28.27600 12.39000 1.000 22.20000  ? 146 ALA A CA  1 
ATOM   1099 C  C   . ALA A  1 152 ? 39.47600  -29.10700 11.32400 1.000 24.69000  ? 146 ALA A C   1 
ATOM   1100 O  O   . ALA A  1 152 ? 39.69100  -30.31100 11.50000 1.000 24.28000  ? 146 ALA A O   1 
ATOM   1101 C  CB  . ALA A  1 152 ? 37.31500  -28.04800 12.00100 1.000 22.13000  ? 146 ALA A CB  1 
ATOM   1102 N  N   . ARG A  1 153 ? 39.81700  -28.47900 10.19600 1.000 26.84000  ? 147 ARG A N   1 
ATOM   1103 C  CA  . ARG A  1 153 ? 40.49700  -29.18700 9.11700  1.000 26.54000  ? 147 ARG A CA  1 
ATOM   1104 C  C   . ARG A  1 153 ? 41.88300  -29.65300 9.55700  1.000 26.82000  ? 147 ARG A C   1 
ATOM   1105 O  O   . ARG A  1 153 ? 42.29900  -30.77500 9.24400  1.000 27.10000  ? 147 ARG A O   1 
ATOM   1106 C  CB  . ARG A  1 153 ? 40.56900  -28.27300 7.88100  1.000 26.64000  ? 147 ARG A CB  1 
ATOM   1107 C  CG  . ARG A  1 153 ? 41.18700  -28.90800 6.64400  1.000 33.67000  ? 147 ARG A CG  1 
ATOM   1108 C  CD  . ARG A  1 153 ? 40.68300  -28.30300 5.33300  1.000 37.57000  ? 147 ARG A CD  1 
ATOM   1109 N  NE  . ARG A  1 153 ? 39.33900  -28.75200 4.96000  1.000 37.55000  ? 147 ARG A NE  1 
ATOM   1110 C  CZ  . ARG A  1 153 ? 38.62900  -28.22200 3.97200  1.000 40.35000  ? 147 ARG A CZ  1 
ATOM   1111 N  NH1 . ARG A  1 153 ? 39.09600  -27.21300 3.25200  1.000 41.18000  ? 147 ARG A NH1 1 
ATOM   1112 N  NH2 . ARG A  1 153 ? 37.40700  -28.68900 3.72000  1.000 36.90000  ? 147 ARG A NH2 1 
ATOM   1113 N  N   . ALA A  1 154 ? 42.57800  -28.82600 10.34200 1.000 26.92000  ? 148 ALA A N   1 
ATOM   1114 C  CA  . ALA A  1 154 ? 43.96100  -29.09600 10.73800 1.000 24.83000  ? 148 ALA A CA  1 
ATOM   1115 C  C   . ALA A  1 154 ? 44.09600  -30.38600 11.53600 1.000 32.07000  ? 148 ALA A C   1 
ATOM   1116 O  O   . ALA A  1 154 ? 45.06800  -31.13100 11.36800 1.000 31.12000  ? 148 ALA A O   1 
ATOM   1117 C  CB  . ALA A  1 154 ? 44.50100  -27.92000 11.55300 1.000 29.28000  ? 148 ALA A CB  1 
ATOM   1118 N  N   . ILE A  1 155 ? 43.16200  -30.65900 12.44100 1.000 29.20000  ? 149 ILE A N   1 
ATOM   1119 C  CA  . ILE A  1 155 ? 43.26000  -31.88400 13.21900 1.000 32.65000  ? 149 ILE A CA  1 
ATOM   1120 C  C   . ILE A  1 155 ? 42.43100  -33.00700 12.60500 1.000 32.00000  ? 149 ILE A C   1 
ATOM   1121 O  O   . ILE A  1 155 ? 42.28600  -34.07400 13.21200 1.000 31.50000  ? 149 ILE A O   1 
ATOM   1122 C  CB  . ILE A  1 155 ? 42.86400  -31.66300 14.68400 1.000 31.52000  ? 149 ILE A CB  1 
ATOM   1123 C  CG1 . ILE A  1 155 ? 41.43600  -31.13800 14.76700 1.000 24.66000  ? 149 ILE A CG1 1 
ATOM   1124 C  CG2 . ILE A  1 155 ? 43.88600  -30.76000 15.39200 1.000 29.73000  ? 149 ILE A CG2 1 
ATOM   1125 C  CD1 . ILE A  1 155 ? 40.85900  -31.26900 16.14600 1.000 28.45000  ? 149 ILE A CD1 1 
ATOM   1126 N  N   . GLY A  1 156 ? 41.87800  -32.78900 11.41700 1.000 28.06000  ? 150 GLY A N   1 
ATOM   1127 C  CA  . GLY A  1 156 ? 41.16600  -33.85500 10.75200 1.000 33.60000  ? 150 GLY A CA  1 
ATOM   1128 C  C   . GLY A  1 156 ? 39.79800  -34.10200 11.31800 1.000 32.03000  ? 150 GLY A C   1 
ATOM   1129 O  O   . GLY A  1 156 ? 39.24000  -35.18200 11.10800 1.000 32.23000  ? 150 GLY A O   1 
ATOM   1130 N  N   . ALA A  1 157 ? 39.26100  -33.14500 12.06800 1.000 30.78000  ? 151 ALA A N   1 
ATOM   1131 C  CA  . ALA A  1 157 ? 37.85700  -33.19300 12.42500 1.000 34.37000  ? 151 ALA A CA  1 
ATOM   1132 C  C   . ALA A  1 157 ? 36.99900  -32.90000 11.19400 1.000 34.25000  ? 151 ALA A C   1 
ATOM   1133 O  O   . ALA A  1 157 ? 37.45600  -32.32800 10.19300 1.000 32.85000  ? 151 ALA A O   1 
ATOM   1134 C  CB  . ALA A  1 157 ? 37.54500  -32.18400 13.53000 1.000 27.82000  ? 151 ALA A CB  1 
ATOM   1135 N  N   . GLY A  1 158 ? 35.74900  -33.33400 11.25900 1.000 34.32000  ? 152 GLY A N   1 
ATOM   1136 C  CA  . GLY A  1 158 ? 34.79900  -32.85300 10.27700 1.000 37.50000  ? 152 GLY A CA  1 
ATOM   1137 C  C   . GLY A  1 158 ? 34.78600  -31.33900 10.26500 1.000 32.18000  ? 152 GLY A C   1 
ATOM   1138 O  O   . GLY A  1 158 ? 35.07200  -30.70700 11.28500 1.000 32.80000  ? 152 GLY A O   1 
ATOM   1139 N  N   . THR A  1 159 ? 34.48600  -30.74300 9.11300  1.000 34.67000  ? 153 THR A N   1 
ATOM   1140 C  CA  . THR A  1 159 ? 34.25300  -29.31200 9.03900  1.000 31.88000  ? 153 THR A CA  1 
ATOM   1141 C  C   . THR A  1 159 ? 32.77900  -28.93600 9.09600  1.000 29.01000  ? 153 THR A C   1 
ATOM   1142 O  O   . THR A  1 159 ? 32.47900  -27.78300 9.40600  1.000 28.25000  ? 153 THR A O   1 
ATOM   1143 C  CB  . THR A  1 159 ? 34.85700  -28.72200 7.75800  1.000 32.97000  ? 153 THR A CB  1 
ATOM   1144 O  OG1 . THR A  1 159 ? 34.34000  -29.40800 6.60800  1.000 34.24000  ? 153 THR A OG1 1 
ATOM   1145 C  CG2 . THR A  1 159 ? 36.36700  -28.86400 7.78700  1.000 35.71000  ? 153 THR A CG2 1 
ATOM   1146 N  N   . ASP A  1 160 ? 31.85600  -29.87200 8.81800  1.000 30.21000  ? 154 ASP A N   1 
ATOM   1147 C  CA  . ASP A  1 160 ? 30.45200  -29.49200 8.67300  1.000 34.30000  ? 154 ASP A CA  1 
ATOM   1148 C  C   . ASP A  1 160 ? 29.90700  -28.84000 9.94600  1.000 30.28000  ? 154 ASP A C   1 
ATOM   1149 O  O   . ASP A  1 160 ? 29.13400  -27.87100 9.87600  1.000 33.14000  ? 154 ASP A O   1 
ATOM   1150 C  CB  . ASP A  1 160 ? 29.62100  -30.71400 8.27700  1.000 33.07000  ? 154 ASP A CB  1 
ATOM   1151 C  CG  . ASP A  1 160 ? 28.11600  -30.41400 8.21500  1.000 40.95000  ? 154 ASP A CG  1 
ATOM   1152 O  OD1 . ASP A  1 160 ? 27.69800  -29.42400 7.56000  1.000 41.73000  ? 154 ASP A OD1 1 
ATOM   1153 O  OD2 . ASP A  1 160 ? 27.33600  -31.18600 8.81600  1.000 47.29000  ? 154 ASP A OD2 1 
ATOM   1154 N  N   . GLY A  1 161 ? 30.31100  -29.34200 11.11400 1.000 30.73000  ? 155 GLY A N   1 
ATOM   1155 C  CA  . GLY A  1 161 ? 29.80400  -28.82900 12.37400 1.000 30.94000  ? 155 GLY A CA  1 
ATOM   1156 C  C   . GLY A  1 161 ? 30.84000  -28.24100 13.31100 1.000 27.08000  ? 155 GLY A C   1 
ATOM   1157 O  O   . GLY A  1 161 ? 30.72100  -28.40500 14.52800 1.000 25.75000  ? 155 GLY A O   1 
ATOM   1158 N  N   . TYR A  1 162 ? 31.86200  -27.57900 12.75000 1.000 24.25000  ? 156 TYR A N   1 
ATOM   1159 C  CA  . TYR A  1 162 ? 32.91100  -26.92400 13.53900 1.000 23.96000  ? 156 TYR A CA  1 
ATOM   1160 C  C   . TYR A  1 162 ? 32.34400  -25.94500 14.55200 1.000 24.03000  ? 156 TYR A C   1 
ATOM   1161 O  O   . TYR A  1 162 ? 33.02800  -25.61600 15.52600 1.000 24.48000  ? 156 TYR A O   1 
ATOM   1162 C  CB  . TYR A  1 162 ? 33.90500  -26.15800 12.63500 1.000 25.18000  ? 156 TYR A CB  1 
ATOM   1163 C  CG  . TYR A  1 162 ? 33.35800  -24.87900 12.00100 1.000 22.36000  ? 156 TYR A CG  1 
ATOM   1164 C  CD1 . TYR A  1 162 ? 33.26900  -23.68100 12.72300 1.000 23.76000  ? 156 TYR A CD1 1 
ATOM   1165 C  CD2 . TYR A  1 162 ? 32.94700  -24.86300 10.67800 1.000 24.91000  ? 156 TYR A CD2 1 
ATOM   1166 C  CE1 . TYR A  1 162 ? 32.76800  -22.52200 12.14400 1.000 22.92000  ? 156 TYR A CE1 1 
ATOM   1167 C  CE2 . TYR A  1 162 ? 32.43700  -23.70400 10.08900 1.000 22.22000  ? 156 TYR A CE2 1 
ATOM   1168 C  CZ  . TYR A  1 162 ? 32.35100  -22.54000 10.82900 1.000 22.29000  ? 156 TYR A CZ  1 
ATOM   1169 O  OH  . TYR A  1 162 ? 31.81500  -21.41100 10.24400 1.000 22.07000  ? 156 TYR A OH  1 
ATOM   1170 N  N   . HIS A  1 163 ? 31.11900  -25.46400 14.33100 1.000 22.89000  ? 157 HIS A N   1 
ATOM   1171 C  CA  . HIS A  1 163 ? 30.48500  -24.45700 15.17200 1.000 24.75000  ? 157 HIS A CA  1 
ATOM   1172 C  C   . HIS A  1 163 ? 29.66700  -25.05500 16.30000 1.000 24.77000  ? 157 HIS A C   1 
ATOM   1173 O  O   . HIS A  1 163 ? 29.20900  -24.30200 17.16800 1.000 28.15000  ? 157 HIS A O   1 
ATOM   1174 C  CB  . HIS A  1 163 ? 29.56900  -23.55300 14.32900 1.000 22.80000  ? 157 HIS A CB  1 
ATOM   1175 C  CG  . HIS A  1 163 ? 28.41500  -24.28100 13.71800 1.000 27.16000  ? 157 HIS A CG  1 
ATOM   1176 N  ND1 . HIS A  1 163 ? 28.58400  -25.33100 12.84200 1.000 23.72000  ? 157 HIS A ND1 1 
ATOM   1177 C  CD2 . HIS A  1 163 ? 27.07400  -24.11000 13.85000 1.000 29.48000  ? 157 HIS A CD2 1 
ATOM   1178 C  CE1 . HIS A  1 163 ? 27.39800  -25.77900 12.46300 1.000 28.24000  ? 157 HIS A CE1 1 
ATOM   1179 N  NE2 . HIS A  1 163 ? 26.46300  -25.05800 13.06200 1.000 27.35000  ? 157 HIS A NE2 1 
ATOM   1180 N  N   . LEU A  1 164 ? 29.47300  -26.36000 16.29700 1.000 24.28000  ? 158 LEU A N   1 
ATOM   1181 C  CA  . LEU A  1 164 ? 28.60800  -27.07900 17.22900 1.000 25.96000  ? 158 LEU A CA  1 
ATOM   1182 C  C   . LEU A  1 164 ? 29.32900  -27.31600 18.55400 1.000 33.13000  ? 158 LEU A C   1 
ATOM   1183 O  O   . LEU A  1 164 ? 30.51200  -27.67100 18.55800 1.000 28.24000  ? 158 LEU A O   1 
ATOM   1184 C  CB  . LEU A  1 164 ? 28.18700  -28.41900 16.64300 1.000 28.15000  ? 158 LEU A CB  1 
ATOM   1185 C  CG  . LEU A  1 164 ? 27.33400  -28.41400 15.36700 1.000 31.36000  ? 158 LEU A CG  1 
ATOM   1186 C  CD1 . LEU A  1 164 ? 27.11700  -29.84200 14.86200 1.000 29.85000  ? 158 LEU A CD1 1 
ATOM   1187 C  CD2 . LEU A  1 164 ? 26.02000  -27.71100 15.62600 1.000 30.26000  ? 158 LEU A CD2 1 
ATOM   1188 N  N   . PRO A  1 165 ? 28.62500  -27.16700 19.68400 1.000 30.18000  ? 159 PRO A N   1 
ATOM   1189 C  CA  . PRO A  1 165 ? 29.28200  -27.32000 20.99700 1.000 33.77000  ? 159 PRO A CA  1 
ATOM   1190 C  C   . PRO A  1 165 ? 30.05000  -28.61900 21.19300 1.000 34.64000  ? 159 PRO A C   1 
ATOM   1191 O  O   . PRO A  1 165 ? 31.09100  -28.59600 21.86200 1.000 41.11000  ? 159 PRO A O   1 
ATOM   1192 C  CB  . PRO A  1 165 ? 28.10900  -27.21200 21.97700 1.000 31.75000  ? 159 PRO A CB  1 
ATOM   1193 C  CG  . PRO A  1 165 ? 27.10100  -26.39200 21.25200 1.000 31.95000  ? 159 PRO A CG  1 
ATOM   1194 C  CD  . PRO A  1 165 ? 27.20400  -26.80400 19.81300 1.000 29.12000  ? 159 PRO A CD  1 
ATOM   1195 N  N   . ASP A  1 166 ? 29.56700  -29.75500 20.66500 1.000 36.66000  ? 160 ASP A N   1 
ATOM   1196 C  CA  . ASP A  1 166 ? 30.23300  -31.05600 20.82000 1.000 35.14000  ? 160 ASP A CA  1 
ATOM   1197 C  C   . ASP A  1 166 ? 31.34300  -31.27900 19.79600 1.000 34.40000  ? 160 ASP A C   1 
ATOM   1198 O  O   . ASP A  1 166 ? 31.81300  -32.40800 19.64900 1.000 30.59000  ? 160 ASP A O   1 
ATOM   1199 C  CB  . ASP A  1 166 ? 29.22100  -32.19700 20.69900 1.000 36.81000  ? 160 ASP A CB  1 
ATOM   1200 C  CG  . ASP A  1 166 ? 28.23000  -32.25000 21.86600 1.000 50.20000  ? 160 ASP A CG  1 
ATOM   1201 O  OD1 . ASP A  1 166 ? 28.62100  -32.68700 22.96900 1.000 45.67000  ? 160 ASP A OD1 1 
ATOM   1202 O  OD2 . ASP A  1 166 ? 27.04300  -31.86900 21.67600 1.000 51.40000  ? 160 ASP A OD2 1 
ATOM   1203 N  N   . HIS A  1 167 ? 31.75100  -30.24600 19.07400 1.000 30.73000  ? 161 HIS A N   1 
ATOM   1204 C  CA  . HIS A  1 167 ? 32.84100  -30.41300 18.12200 1.000 29.18000  ? 161 HIS A CA  1 
ATOM   1205 C  C   . HIS A  1 167 ? 34.17900  -30.14200 18.81800 1.000 26.51000  ? 161 HIS A C   1 
ATOM   1206 O  O   . HIS A  1 167 ? 34.27000  -29.22900 19.64800 1.000 26.18000  ? 161 HIS A O   1 
ATOM   1207 C  CB  . HIS A  1 167 ? 32.64900  -29.45900 16.94100 1.000 26.40000  ? 161 HIS A CB  1 
ATOM   1208 C  CG  . HIS A  1 167 ? 33.60800  -29.68200 15.81700 1.000 27.39000  ? 161 HIS A CG  1 
ATOM   1209 N  ND1 . HIS A  1 167 ? 34.90400  -29.22300 15.85200 1.000 25.88000  ? 161 HIS A ND1 1 
ATOM   1210 C  CD2 . HIS A  1 167 ? 33.45500  -30.29100 14.61700 1.000 30.86000  ? 161 HIS A CD2 1 
ATOM   1211 C  CE1 . HIS A  1 167 ? 35.52100  -29.56300 14.73300 1.000 31.48000  ? 161 HIS A CE1 1 
ATOM   1212 N  NE2 . HIS A  1 167 ? 34.66300  -30.21300 13.96500 1.000 30.89000  ? 161 HIS A NE2 1 
ATOM   1213 N  N   . PRO A  1 168 ? 35.23700  -30.91500 18.53600 1.000 26.19000  ? 162 PRO A N   1 
ATOM   1214 C  CA  . PRO A  1 168 ? 36.53600  -30.63700 19.18600 1.000 24.60000  ? 162 PRO A CA  1 
ATOM   1215 C  C   . PRO A  1 168 ? 36.97900  -29.17800 19.12900 1.000 24.54000  ? 162 PRO A C   1 
ATOM   1216 O  O   . PRO A  1 168 ? 37.65200  -28.71600 20.05400 1.000 24.52000  ? 162 PRO A O   1 
ATOM   1217 C  CB  . PRO A  1 168 ? 37.51700  -31.51900 18.40700 1.000 26.94000  ? 162 PRO A CB  1 
ATOM   1218 C  CG  . PRO A  1 168 ? 36.69300  -32.56800 17.75800 1.000 27.39000  ? 162 PRO A CG  1 
ATOM   1219 C  CD  . PRO A  1 168 ? 35.34000  -31.96900 17.51000 1.000 25.24000  ? 162 PRO A CD  1 
ATOM   1220 N  N   . MET A  1 169 ? 36.66000  -28.44400 18.06400 1.000 22.52000  ? 163 MET A N   1 
ATOM   1221 C  CA  A MET A  1 169 ? 37.08600  -27.04900 18.01200 0.500 22.81000  ? 163 MET A CA  1 
ATOM   1222 C  CA  B MET A  1 169 ? 37.09000  -27.05000 18.00600 0.500 22.82000  ? 163 MET A CA  1 
ATOM   1223 C  C   . MET A  1 169 ? 36.41100  -26.22500 19.09400 1.000 24.08000  ? 163 MET A C   1 
ATOM   1224 O  O   . MET A  1 169 ? 37.05400  -25.37700 19.71900 1.000 22.29000  ? 163 MET A O   1 
ATOM   1225 C  CB  A MET A  1 169 ? 36.82100  -26.45100 16.63000 0.500 24.73000  ? 163 MET A CB  1 
ATOM   1226 C  CB  B MET A  1 169 ? 36.82800  -26.47100 16.61300 0.500 24.73000  ? 163 MET A CB  1 
ATOM   1227 C  CG  A MET A  1 169 ? 37.28400  -24.99700 16.48100 0.500 23.77000  ? 163 MET A CG  1 
ATOM   1228 C  CG  B MET A  1 169 ? 37.70600  -25.27100 16.23200 0.500 24.04000  ? 163 MET A CG  1 
ATOM   1229 S  SD  A MET A  1 169 ? 39.07200  -24.74600 16.27100 0.500 24.46000  ? 163 MET A SD  1 
ATOM   1230 S  SD  B MET A  1 169 ? 39.49500  -25.54900 16.37700 0.500 27.48000  ? 163 MET A SD  1 
ATOM   1231 C  CE  A MET A  1 169 ? 39.64200  -26.43100 15.99600 0.500 22.61000  ? 163 MET A CE  1 
ATOM   1232 C  CE  B MET A  1 169 ? 39.88300  -24.43200 17.72000 0.500 21.65000  ? 163 MET A CE  1 
ATOM   1233 N  N   . GLN A  1 170 ? 35.11400  -26.47300 19.35900 1.000 20.93000  ? 164 GLN A N   1 
ATOM   1234 C  CA  . GLN A  1 170 ? 34.46600  -25.72000 20.42700 1.000 22.66000  ? 164 GLN A CA  1 
ATOM   1235 C  C   . GLN A  1 170 ? 34.90500  -26.18800 21.81000 1.000 22.47000  ? 164 GLN A C   1 
ATOM   1236 O  O   . GLN A  1 170 ? 34.94300  -25.37400 22.74600 1.000 23.72000  ? 164 GLN A O   1 
ATOM   1237 C  CB  . GLN A  1 170 ? 32.94400  -25.81600 20.30300 1.000 23.85000  ? 164 GLN A CB  1 
ATOM   1238 C  CG  . GLN A  1 170 ? 32.42500  -25.22800 19.02000 1.000 21.91000  ? 164 GLN A CG  1 
ATOM   1239 C  CD  . GLN A  1 170 ? 33.06400  -23.91800 18.71500 1.000 23.77000  ? 164 GLN A CD  1 
ATOM   1240 O  OE1 . GLN A  1 170 ? 33.10400  -23.02500 19.56100 1.000 20.23000  ? 164 GLN A OE1 1 
ATOM   1241 N  NE2 . GLN A  1 170 ? 33.60500  -23.79200 17.51100 1.000 24.64000  ? 164 GLN A NE2 1 
ATOM   1242 N  N   . GLY A  1 171 ? 35.17500  -27.48600 21.96900 1.000 24.81000  ? 165 GLY A N   1 
ATOM   1243 C  CA  . GLY A  1 171 ? 35.83800  -27.96600 23.18000 1.000 21.24000  ? 165 GLY A CA  1 
ATOM   1244 C  C   . GLY A  1 171 ? 37.11800  -27.20700 23.47000 1.000 28.73000  ? 165 GLY A C   1 
ATOM   1245 O  O   . GLY A  1 171 ? 37.35000  -26.75200 24.59500 1.000 27.48000  ? 165 GLY A O   1 
ATOM   1246 N  N   . ARG A  1 172 ? 37.96600  -27.03900 22.44500 1.000 25.79000  ? 166 ARG A N   1 
ATOM   1247 C  CA  . ARG A  1 172 ? 39.17400  -26.23300 22.60400 1.000 22.17000  ? 166 ARG A CA  1 
ATOM   1248 C  C   . ARG A  1 172 ? 38.83300  -24.78900 22.96700 1.000 25.42000  ? 166 ARG A C   1 
ATOM   1249 O  O   . ARG A  1 172 ? 39.46900  -24.20000 23.85300 1.000 26.57000  ? 166 ARG A O   1 
ATOM   1250 C  CB  . ARG A  1 172 ? 40.02400  -26.28100 21.32700 1.000 24.14000  ? 166 ARG A CB  1 
ATOM   1251 C  CG  . ARG A  1 172 ? 40.92000  -27.52000 21.20200 1.000 22.98000  ? 166 ARG A CG  1 
ATOM   1252 C  CD  . ARG A  1 172 ? 40.89900  -28.10100 19.80000 1.000 25.10000  ? 166 ARG A CD  1 
ATOM   1253 N  NE  . ARG A  1 172 ? 41.56900  -29.40100 19.76400 1.000 28.55000  ? 166 ARG A NE  1 
ATOM   1254 C  CZ  . ARG A  1 172 ? 42.87100  -29.53100 19.56200 1.000 26.20000  ? 166 ARG A CZ  1 
ATOM   1255 N  NH1 . ARG A  1 172 ? 43.63500  -28.47300 19.34900 1.000 28.68000  ? 166 ARG A NH1 1 
ATOM   1256 N  NH2 . ARG A  1 172 ? 43.42000  -30.75000 19.57300 1.000 27.77000  ? 166 ARG A NH2 1 
ATOM   1257 N  N   . VAL A  1 173 ? 37.83800  -24.19900 22.29600 1.000 22.03000  ? 167 VAL A N   1 
ATOM   1258 C  CA  . VAL A  1 173 ? 37.46000  -22.80900 22.57700 1.000 22.13000  ? 167 VAL A CA  1 
ATOM   1259 C  C   . VAL A  1 173 ? 36.98400  -22.67500 24.01400 1.000 23.56000  ? 167 VAL A C   1 
ATOM   1260 O  O   . VAL A  1 173 ? 37.41300  -21.78100 24.75000 1.000 23.60000  ? 167 VAL A O   1 
ATOM   1261 C  CB  . VAL A  1 173 ? 36.37600  -22.33700 21.59400 1.000 19.40000  ? 167 VAL A CB  1 
ATOM   1262 C  CG1 . VAL A  1 173 ? 35.61100  -21.10200 22.13900 1.000 20.71000  ? 167 VAL A CG1 1 
ATOM   1263 C  CG2 . VAL A  1 173 ? 36.96300  -22.12000 20.20100 1.000 21.86000  ? 167 VAL A CG2 1 
ATOM   1264 N  N   . LYS A  1 174 ? 36.10500  -23.58500 24.43800 1.000 23.29000  ? 168 LYS A N   1 
ATOM   1265 C  CA  . LYS A  1 174 ? 35.57200  -23.53400 25.79600 1.000 25.62000  ? 168 LYS A CA  1 
ATOM   1266 C  C   . LYS A  1 174 ? 36.69200  -23.60700 26.82500 1.000 26.37000  ? 168 LYS A C   1 
ATOM   1267 O  O   . LYS A  1 174 ? 36.75700  -22.79900 27.76500 1.000 23.78000  ? 168 LYS A O   1 
ATOM   1268 C  CB  . LYS A  1 174 ? 34.58200  -24.67400 25.99900 1.000 26.13000  ? 168 LYS A CB  1 
ATOM   1269 C  CG  . LYS A  1 174 ? 33.25000  -24.47000 25.28300 1.000 29.57000  ? 168 LYS A CG  1 
ATOM   1270 C  CD  . LYS A  1 174 ? 32.20200  -25.45900 25.82100 1.000 29.53000  ? 168 LYS A CD  1 
ATOM   1271 C  CE  . LYS A  1 174 ? 30.79500  -25.13400 25.31700 1.000 33.92000  ? 168 LYS A CE  1 
ATOM   1272 N  NZ  . LYS A  1 174 ? 30.78300  -25.07700 23.83400 1.000 30.22000  ? 168 LYS A NZ  1 
ATOM   1273 N  N   . ARG A  1 175 ? 37.60600  -24.55300 26.62500 1.000 23.72000  ? 169 ARG A N   1 
ATOM   1274 C  CA  A ARG A  1 175 ? 38.73000  -24.73500 27.53400 0.700 26.28000  ? 169 ARG A CA  1 
ATOM   1275 C  CA  B ARG A  1 175 ? 38.72000  -24.73600 27.54300 0.300 26.28000  ? 169 ARG A CA  1 
ATOM   1276 C  C   . ARG A  1 175 ? 39.62800  -23.51000 27.56800 1.000 27.33000  ? 169 ARG A C   1 
ATOM   1277 O  O   . ARG A  1 175 ? 40.09600  -23.10200 28.63700 1.000 28.67000  ? 169 ARG A O   1 
ATOM   1278 C  CB  A ARG A  1 175 ? 39.53500  -25.96300 27.10800 0.700 26.99000  ? 169 ARG A CB  1 
ATOM   1279 C  CB  B ARG A  1 175 ? 39.49400  -25.99800 27.14700 0.300 26.99000  ? 169 ARG A CB  1 
ATOM   1280 C  CG  A ARG A  1 175 ? 39.47100  -27.08500 28.06200 0.700 27.66000  ? 169 ARG A CG  1 
ATOM   1281 C  CG  B ARG A  1 175 ? 40.80600  -26.18800 27.86400 0.300 26.34000  ? 169 ARG A CG  1 
ATOM   1282 C  CD  A ARG A  1 175 ? 40.61800  -28.03900 27.80300 0.700 27.45000  ? 169 ARG A CD  1 
ATOM   1283 C  CD  B ARG A  1 175 ? 41.48200  -27.49100 27.46800 0.300 27.02000  ? 169 ARG A CD  1 
ATOM   1284 N  NE  A ARG A  1 175 ? 40.87900  -28.25000 26.38300 0.700 28.96000  ? 169 ARG A NE  1 
ATOM   1285 N  NE  B ARG A  1 175 ? 42.00200  -27.48000 26.10500 0.300 26.61000  ? 169 ARG A NE  1 
ATOM   1286 C  CZ  A ARG A  1 175 ? 40.17100  -29.05700 25.60300 0.700 26.95000  ? 169 ARG A CZ  1 
ATOM   1287 C  CZ  B ARG A  1 175 ? 43.16700  -26.95300 25.75400 0.300 26.67000  ? 169 ARG A CZ  1 
ATOM   1288 N  NH1 A ARG A  1 175 ? 39.04200  -29.59800 26.01800 0.700 28.40000  ? 169 ARG A NH1 1 
ATOM   1289 N  NH1 B ARG A  1 175 ? 43.92100  -26.30600 26.62600 0.300 27.65000  ? 169 ARG A NH1 1 
ATOM   1290 N  NH2 A ARG A  1 175 ? 40.62500  -29.34700 24.38400 0.700 25.80000  ? 169 ARG A NH2 1 
ATOM   1291 N  NH2 B ARG A  1 175 ? 43.58700  -27.08600 24.50000 0.300 24.53000  ? 169 ARG A NH2 1 
ATOM   1292 N  N   . THR A  1 176 ? 39.88200  -22.91100 26.40100 1.000 25.05000  ? 170 THR A N   1 
ATOM   1293 C  CA  . THR A  1 176 ? 40.79700  -21.78200 26.32200 1.000 24.74000  ? 170 THR A CA  1 
ATOM   1294 C  C   . THR A  1 176 ? 40.21200  -20.54900 27.00400 1.000 25.29000  ? 170 THR A C   1 
ATOM   1295 O  O   . THR A  1 176 ? 40.90800  -19.85300 27.74600 1.000 23.94000  ? 170 THR A O   1 
ATOM   1296 C  CB  . THR A  1 176 ? 41.13500  -21.51700 24.85500 1.000 25.95000  ? 170 THR A CB  1 
ATOM   1297 O  OG1 . THR A  1 176 ? 41.68000  -22.73000 24.29200 1.000 29.51000  ? 170 THR A OG1 1 
ATOM   1298 C  CG2 . THR A  1 176 ? 42.21100  -20.45500 24.74600 1.000 26.05000  ? 170 THR A CG2 1 
ATOM   1299 N  N   . VAL A  1 177 ? 38.91200  -20.30700 26.82700 1.000 23.59000  ? 171 VAL A N   1 
ATOM   1300 C  CA  . VAL A  1 177 ? 38.27000  -19.19700 27.52700 1.000 25.42000  ? 171 VAL A CA  1 
ATOM   1301 C  C   . VAL A  1 177 ? 38.37500  -19.36100 29.04800 1.000 24.10000  ? 171 VAL A C   1 
ATOM   1302 O  O   . VAL A  1 177 ? 38.77900  -18.43800 29.75900 1.000 24.48000  ? 171 VAL A O   1 
ATOM   1303 C  CB  . VAL A  1 177 ? 36.81900  -19.06700 27.05500 1.000 21.73000  ? 171 VAL A CB  1 
ATOM   1304 C  CG1 . VAL A  1 177 ? 36.08800  -18.01100 27.88900 1.000 17.40000  ? 171 VAL A CG1 1 
ATOM   1305 C  CG2 . VAL A  1 177 ? 36.83100  -18.70200 25.58000 1.000 24.50000  ? 171 VAL A CG2 1 
ATOM   1306 N  N   . ALA A  1 178 ? 38.01700  -20.53000 29.58000 1.000 22.95000  ? 172 ALA A N   1 
ATOM   1307 C  CA  . ALA A  1 178 ? 38.06400  -20.69000 31.03200 1.000 23.91000  ? 172 ALA A CA  1 
ATOM   1308 C  C   . ALA A  1 178 ? 39.48300  -20.49600 31.57200 1.000 26.99000  ? 172 ALA A C   1 
ATOM   1309 O  O   . ALA A  1 178 ? 39.68200  -19.87300 32.62800 1.000 25.38000  ? 172 ALA A O   1 
ATOM   1310 C  CB  . ALA A  1 178 ? 37.53300  -22.06700 31.43000 1.000 25.34000  ? 172 ALA A CB  1 
ATOM   1311 N  N   . GLU A  1 179 ? 40.47900  -21.01200 30.85100 1.000 24.10000  ? 173 GLU A N   1 
ATOM   1312 C  CA  . GLU A  1 179 ? 41.87600  -20.89600 31.26700 1.000 24.33000  ? 173 GLU A CA  1 
ATOM   1313 C  C   . GLU A  1 179 ? 42.33500  -19.43700 31.28700 1.000 26.89000  ? 173 GLU A C   1 
ATOM   1314 O  O   . GLU A  1 179 ? 42.96200  -18.99400 32.25600 1.000 25.99000  ? 173 GLU A O   1 
ATOM   1315 C  CB  . GLU A  1 179 ? 42.76600  -21.74800 30.34600 1.000 29.60000  ? 173 GLU A CB  1 
ATOM   1316 C  CG  . GLU A  1 179 ? 42.51600  -23.24700 30.53800 1.000 27.07000  ? 173 GLU A CG  1 
ATOM   1317 C  CD  . GLU A  1 179 ? 43.22000  -24.16100 29.53000 1.000 29.92000  ? 173 GLU A CD  1 
ATOM   1318 O  OE1 . GLU A  1 179 ? 43.83700  -23.68400 28.55100 1.000 36.41000  ? 173 GLU A OE1 1 
ATOM   1319 O  OE2 . GLU A  1 179 ? 43.11500  -25.37900 29.71300 1.000 33.32000  ? 173 GLU A OE2 1 
ATOM   1320 N  N   . LEU A  1 180 ? 42.01100  -18.66200 30.24100 1.000 23.05000  ? 174 LEU A N   1 
ATOM   1321 C  CA  . LEU A  1 180 ? 42.44800  -17.27000 30.25200 1.000 23.47000  ? 174 LEU A CA  1 
ATOM   1322 C  C   . LEU A  1 180 ? 41.74500  -16.48200 31.34800 1.000 21.02000  ? 174 LEU A C   1 
ATOM   1323 O  O   . LEU A  1 180 ? 42.33700  -15.55500 31.91400 1.000 23.66000  ? 174 LEU A O   1 
ATOM   1324 C  CB  . LEU A  1 180 ? 42.22400  -16.60600 28.89500 1.000 21.68000  ? 174 LEU A CB  1 
ATOM   1325 C  CG  . LEU A  1 180 ? 43.14300  -17.04700 27.75200 1.000 22.73000  ? 174 LEU A CG  1 
ATOM   1326 C  CD1 . LEU A  1 180 ? 42.60900  -16.50000 26.43200 1.000 23.10000  ? 174 LEU A CD1 1 
ATOM   1327 C  CD2 . LEU A  1 180 ? 44.58500  -16.61600 27.99200 1.000 22.99000  ? 174 LEU A CD2 1 
ATOM   1328 N  N   . CYS A  1 181 ? 40.50000  -16.83700 31.66500 1.000 22.23000  ? 175 CYS A N   1 
ATOM   1329 C  CA  . CYS A  1 181 ? 39.76800  -16.23100 32.77500 1.000 19.72000  ? 175 CYS A CA  1 
ATOM   1330 C  C   . CYS A  1 181 ? 40.23600  -16.71000 34.13900 1.000 25.99000  ? 175 CYS A C   1 
ATOM   1331 O  O   . CYS A  1 181 ? 39.83600  -16.11900 35.15300 1.000 26.81000  ? 175 CYS A O   1 
ATOM   1332 C  CB  . CYS A  1 181 ? 38.27300  -16.53600 32.64500 1.000 20.69000  ? 175 CYS A CB  1 
ATOM   1333 S  SG  . CYS A  1 181 ? 37.55700  -15.63500 31.28100 1.000 21.64000  ? 175 CYS A SG  1 
ATOM   1334 N  N   . ASP A  1 182 ? 41.05300  -17.76600 34.18700 1.000 26.37000  ? 176 ASP A N   1 
ATOM   1335 C  CA  . ASP A  1 182 ? 41.38200  -18.46400 35.42700 1.000 25.55000  ? 176 ASP A CA  1 
ATOM   1336 C  C   . ASP A  1 182 ? 40.12000  -18.87900 36.17100 1.000 26.66000  ? 176 ASP A C   1 
ATOM   1337 O  O   . ASP A  1 182 ? 39.97900  -18.64300 37.36700 1.000 26.43000  ? 176 ASP A O   1 
ATOM   1338 C  CB  . ASP A  1 182 ? 42.28000  -17.61600 36.32900 1.000 26.32000  ? 176 ASP A CB  1 
ATOM   1339 C  CG  . ASP A  1 182 ? 43.58300  -17.22900 35.65300 1.000 29.06000  ? 176 ASP A CG  1 
ATOM   1340 O  OD1 . ASP A  1 182 ? 44.16700  -18.07300 34.94200 1.000 31.07000  ? 176 ASP A OD1 1 
ATOM   1341 O  OD2 . ASP A  1 182 ? 44.02500  -16.08400 35.84000 1.000 28.94000  ? 176 ASP A OD2 1 
ATOM   1342 N  N   . LEU A  1 183 ? 39.20500  -19.52700 35.45300 1.000 24.66000  ? 177 LEU A N   1 
ATOM   1343 C  CA  . LEU A  1 183 ? 37.94700  -19.99200 36.01700 1.000 23.01000  ? 177 LEU A CA  1 
ATOM   1344 C  C   . LEU A  1 183 ? 37.77400  -21.47300 35.72400 1.000 29.21000  ? 177 LEU A C   1 
ATOM   1345 O  O   . LEU A  1 183 ? 38.27600  -21.97800 34.71900 1.000 27.98000  ? 177 LEU A O   1 
ATOM   1346 C  CB  . LEU A  1 183 ? 36.75200  -19.23000 35.41700 1.000 28.12000  ? 177 LEU A CB  1 
ATOM   1347 C  CG  . LEU A  1 183 ? 36.59000  -17.74900 35.74900 1.000 25.82000  ? 177 LEU A CG  1 
ATOM   1348 C  CD1 . LEU A  1 183 ? 35.61200  -17.10200 34.75700 1.000 21.39000  ? 177 LEU A CD1 1 
ATOM   1349 C  CD2 . LEU A  1 183 ? 36.13900  -17.59300 37.22000 1.000 28.18000  ? 177 LEU A CD2 1 
ATOM   1350 N  N   . ASP A  1 184 ? 37.03000  -22.16300 36.58100 1.000 25.59000  ? 178 ASP A N   1 
ATOM   1351 C  CA  . ASP A  1 184 ? 36.66800  -23.53000 36.24300 1.000 32.21000  ? 178 ASP A CA  1 
ATOM   1352 C  C   . ASP A  1 184 ? 35.59900  -23.51600 35.16200 1.000 29.29000  ? 178 ASP A C   1 
ATOM   1353 O  O   . ASP A  1 184 ? 34.87400  -22.53300 34.99300 1.000 26.71000  ? 178 ASP A O   1 
ATOM   1354 C  CB  . ASP A  1 184 ? 36.18000  -24.29000 37.46900 1.000 31.73000  ? 178 ASP A CB  1 
ATOM   1355 C  CG  . ASP A  1 184 ? 37.23900  -24.38700 38.53200 1.000 41.89000  ? 178 ASP A CG  1 
ATOM   1356 O  OD1 . ASP A  1 184 ? 38.39700  -24.74000 38.20400 1.000 45.43000  ? 178 ASP A OD1 1 
ATOM   1357 O  OD2 . ASP A  1 184 ? 36.91800  -24.08300 39.69200 1.000 43.33000  ? 178 ASP A OD2 1 
ATOM   1358 N  N   . ALA A  1 185 ? 35.55500  -24.60400 34.39700 1.000 25.97000  ? 179 ALA A N   1 
ATOM   1359 C  CA  . ALA A  1 185 ? 34.56700  -24.83700 33.34800 1.000 28.08000  ? 179 ALA A CA  1 
ATOM   1360 C  C   . ALA A  1 185 ? 33.17800  -24.40500 33.79400 1.000 28.13000  ? 179 ALA A C   1 
ATOM   1361 O  O   . ALA A  1 185 ? 32.45500  -23.72900 33.05000 1.000 28.81000  ? 179 ALA A O   1 
ATOM   1362 C  CB  . ALA A  1 185 ? 34.56100  -26.33600 32.95900 1.000 25.28000  ? 179 ALA A CB  1 
ATOM   1363 N  N   . GLY A  1 186 ? 32.81300  -24.77000 35.01900 1.000 27.26000  ? 180 GLY A N   1 
ATOM   1364 C  CA  . GLY A  1 186 ? 31.47300  -24.53400 35.50400 1.000 30.38000  ? 180 GLY A CA  1 
ATOM   1365 C  C   . GLY A  1 186 ? 31.14300  -23.08500 35.80100 1.000 31.68000  ? 180 GLY A C   1 
ATOM   1366 O  O   . GLY A  1 186 ? 29.96400  -22.77500 36.00100 1.000 33.36000  ? 180 GLY A O   1 
ATOM   1367 N  N   . ASP A  1 187 ? 32.13600  -22.19300 35.84200 1.000 28.95000  ? 181 ASP A N   1 
ATOM   1368 C  CA  . ASP A  1 187 ? 31.88700  -20.78300 36.12000 1.000 28.08000  ? 181 ASP A CA  1 
ATOM   1369 C  C   . ASP A  1 187 ? 31.86100  -19.92000 34.87400 1.000 25.01000  ? 181 ASP A C   1 
ATOM   1370 O  O   . ASP A  1 187 ? 31.79400  -18.69700 34.99600 1.000 27.04000  ? 181 ASP A O   1 
ATOM   1371 C  CB  . ASP A  1 187 ? 32.92100  -20.22600 37.08800 1.000 27.04000  ? 181 ASP A CB  1 
ATOM   1372 C  CG  . ASP A  1 187 ? 32.85800  -20.90000 38.43500 1.000 32.76000  ? 181 ASP A CG  1 
ATOM   1373 O  OD1 . ASP A  1 187 ? 31.75600  -21.35100 38.81400 1.000 37.92000  ? 181 ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A  1 187 ? 33.90200  -20.98700 39.10500 1.000 42.69000  ? 181 ASP A OD2 1 
ATOM   1375 N  N   . VAL A  1 188 ? 31.93800  -20.51900 33.69300 1.000 23.19000  ? 182 VAL A N   1 
ATOM   1376 C  CA  . VAL A  1 188 ? 31.67900  -19.83500 32.43200 1.000 22.42000  ? 182 VAL A CA  1 
ATOM   1377 C  C   . VAL A  1 188 ? 30.35700  -20.36000 31.89600 1.000 23.31000  ? 182 VAL A C   1 
ATOM   1378 O  O   . VAL A  1 188 ? 30.17600  -21.57800 31.79400 1.000 23.44000  ? 182 VAL A O   1 
ATOM   1379 C  CB  . VAL A  1 188 ? 32.81300  -20.07000 31.41900 1.000 20.89000  ? 182 VAL A CB  1 
ATOM   1380 C  CG1 . VAL A  1 188 ? 32.48400  -19.43000 30.07100 1.000 21.33000  ? 182 VAL A CG1 1 
ATOM   1381 C  CG2 . VAL A  1 188 ? 34.15200  -19.55300 31.95900 1.000 26.59000  ? 182 VAL A CG2 1 
ATOM   1382 N  N   . GLU A  1 189 ? 29.42300  -19.45900 31.56500 1.000 19.50000  ? 183 GLU A N   1 
ATOM   1383 C  CA  . GLU A  1 189 ? 28.15900  -19.90500 30.98900 1.000 21.06000  ? 183 GLU A CA  1 
ATOM   1384 C  C   . GLU A  1 189 ? 28.17100  -19.66700 29.49100 1.000 19.52000  ? 183 GLU A C   1 
ATOM   1385 O  O   . GLU A  1 189 ? 28.96200  -18.88400 28.99000 1.000 20.69000  ? 183 GLU A O   1 
ATOM   1386 C  CB  . GLU A  1 189 ? 26.97300  -19.19700 31.65800 1.000 22.59000  ? 183 GLU A CB  1 
ATOM   1387 C  CG  . GLU A  1 189 ? 26.92700  -19.55100 33.12800 1.000 23.53000  ? 183 GLU A CG  1 
ATOM   1388 C  CD  . GLU A  1 189 ? 25.98800  -18.69400 33.92600 1.000 36.06000  ? 183 GLU A CD  1 
ATOM   1389 O  OE1 . GLU A  1 189 ? 25.15400  -17.98800 33.31400 1.000 34.43000  ? 183 GLU A OE1 1 
ATOM   1390 O  OE2 . GLU A  1 189 ? 26.08400  -18.72700 35.17600 1.000 38.75000  ? 183 GLU A OE2 1 
ATOM   1391 N  N   . TRP A  1 190 ? 27.32700  -20.39500 28.75600 1.000 19.67000  ? 184 TRP A N   1 
ATOM   1392 C  CA  . TRP A  1 190 ? 27.43600  -20.34400 27.30100 1.000 23.92000  ? 184 TRP A CA  1 
ATOM   1393 C  C   . TRP A  1 190 ? 26.05600  -20.18900 26.70800 1.000 18.97000  ? 184 TRP A C   1 
ATOM   1394 O  O   . TRP A  1 190 ? 25.14200  -20.90600 27.09800 1.000 19.15000  ? 184 TRP A O   1 
ATOM   1395 C  CB  . TRP A  1 190 ? 28.12400  -21.61000 26.72400 1.000 23.17000  ? 184 TRP A CB  1 
ATOM   1396 C  CG  . TRP A  1 190 ? 29.56200  -21.71500 27.19100 1.000 22.53000  ? 184 TRP A CG  1 
ATOM   1397 C  CD1 . TRP A  1 190 ? 29.98300  -22.20100 28.38000 1.000 21.58000  ? 184 TRP A CD1 1 
ATOM   1398 C  CD2 . TRP A  1 190 ? 30.73400  -21.25800 26.50300 1.000 21.51000  ? 184 TRP A CD2 1 
ATOM   1399 N  NE1 . TRP A  1 190 ? 31.34000  -22.09500 28.48000 1.000 22.89000  ? 184 TRP A NE1 1 
ATOM   1400 C  CE2 . TRP A  1 190 ? 31.82900  -21.51100 27.34100 1.000 23.07000  ? 184 TRP A CE2 1 
ATOM   1401 C  CE3 . TRP A  1 190 ? 30.96200  -20.65500 25.26500 1.000 23.37000  ? 184 TRP A CE3 1 
ATOM   1402 C  CZ2 . TRP A  1 190 ? 33.14000  -21.20700 26.97500 1.000 22.41000  ? 184 TRP A CZ2 1 
ATOM   1403 C  CZ3 . TRP A  1 190 ? 32.27400  -20.34600 24.90100 1.000 22.57000  ? 184 TRP A CZ3 1 
ATOM   1404 C  CH2 . TRP A  1 190 ? 33.34000  -20.62900 25.75400 1.000 22.31000  ? 184 TRP A CH2 1 
ATOM   1405 N  N   . GLY A  1 191 ? 25.90600  -19.25300 25.78400 1.000 17.65000  ? 185 GLY A N   1 
ATOM   1406 C  CA  . GLY A  1 191 ? 24.72900  -19.23100 24.95100 1.000 19.48000  ? 185 GLY A CA  1 
ATOM   1407 C  C   . GLY A  1 191 ? 25.14600  -19.27900 23.49500 1.000 22.09000  ? 185 GLY A C   1 
ATOM   1408 O  O   . GLY A  1 191 ? 26.27300  -19.66600 23.18300 1.000 21.16000  ? 185 GLY A O   1 
ATOM   1409 N  N   . THR A  1 192 ? 24.27000  -18.84400 22.60300 1.000 19.28000  ? 186 THR A N   1 
ATOM   1410 C  CA  . THR A  1 192 ? 24.51600  -18.87700 21.16900 1.000 21.91000  ? 186 THR A CA  1 
ATOM   1411 C  C   . THR A  1 192 ? 24.61800  -17.45700 20.61100 1.000 19.09000  ? 186 THR A C   1 
ATOM   1412 O  O   . THR A  1 192 ? 23.72900  -16.62600 20.83800 1.000 18.73000  ? 186 THR A O   1 
ATOM   1413 C  CB  . THR A  1 192 ? 23.38700  -19.63900 20.47500 1.000 25.39000  ? 186 THR A CB  1 
ATOM   1414 O  OG1 . THR A  1 192 ? 23.36700  -20.99400 20.96800 1.000 26.53000  ? 186 THR A OG1 1 
ATOM   1415 C  CG2 . THR A  1 192 ? 23.58100  -19.63400 18.96400 1.000 21.77000  ? 186 THR A CG2 1 
ATOM   1416 N  N   . ASP A  1 193 ? 25.68800  -17.18700 19.85800 1.000 21.07000  ? 187 ASP A N   1 
ATOM   1417 C  CA  . ASP A  1 193 ? 25.96600  -15.85200 19.34300 1.000 19.82000  ? 187 ASP A CA  1 
ATOM   1418 C  C   . ASP A  1 193 ? 25.10900  -15.54600 18.10700 1.000 21.40000  ? 187 ASP A C   1 
ATOM   1419 O  O   . ASP A  1 193 ? 24.42200  -16.41100 17.55100 1.000 20.20000  ? 187 ASP A O   1 
ATOM   1420 C  CB  . ASP A  1 193 ? 27.45700  -15.72200 18.99300 1.000 21.86000  ? 187 ASP A CB  1 
ATOM   1421 C  CG  . ASP A  1 193 ? 28.13300  -14.49800 19.66500 1.000 21.25000  ? 187 ASP A CG  1 
ATOM   1422 O  OD1 . ASP A  1 193 ? 27.38700  -13.58500 20.00200 1.000 25.88000  ? 187 ASP A OD1 1 
ATOM   1423 O  OD2 . ASP A  1 193 ? 29.40600  -14.46000 19.85300 1.000 24.88000  ? 187 ASP A OD2 1 
ATOM   1424 N  N   . GLY A  1 194 ? 25.20800  -14.30200 17.63600 1.000 18.57000  ? 188 GLY A N   1 
ATOM   1425 C  CA  . GLY A  1 194 ? 24.53200  -13.94400 16.39800 1.000 18.89000  ? 188 GLY A CA  1 
ATOM   1426 C  C   . GLY A  1 194 ? 25.08600  -14.66200 15.17800 1.000 18.89000  ? 188 GLY A C   1 
ATOM   1427 O  O   . GLY A  1 194 ? 24.37100  -14.85800 14.19200 1.000 19.15000  ? 188 GLY A O   1 
ATOM   1428 N  N   . CYS A  1 195 ? 26.36500  -15.05400 15.22600 1.000 19.46000  ? 189 CYS A N   1 
ATOM   1429 C  CA  . CYS A  1 195 ? 26.99600  -15.81400 14.14900 1.000 19.88000  ? 189 CYS A CA  1 
ATOM   1430 C  C   . CYS A  1 195 ? 26.77700  -17.30700 14.29800 1.000 18.90000  ? 189 CYS A C   1 
ATOM   1431 O  O   . CYS A  1 195 ? 27.33500  -18.08000 13.51100 1.000 22.09000  ? 189 CYS A O   1 
ATOM   1432 C  CB  . CYS A  1 195 ? 28.49000  -15.54900 14.12300 1.000 21.21000  ? 189 CYS A CB  1 
ATOM   1433 S  SG  . CYS A  1 195 ? 29.22400  -16.23200 15.60500 1.000 20.62000  ? 189 CYS A SG  1 
ATOM   1434 N  N   . ASN A  1 196 ? 26.04700  -17.71500 15.33800 1.000 17.83000  ? 190 ASN A N   1 
ATOM   1435 C  CA  . ASN A  1 196 ? 25.61200  -19.09100 15.62300 1.000 19.89000  ? 190 ASN A CA  1 
ATOM   1436 C  C   . ASN A  1 196 ? 26.71000  -19.96300 16.24400 1.000 22.76000  ? 190 ASN A C   1 
ATOM   1437 O  O   . ASN A  1 196 ? 26.57300  -21.20500 16.25700 1.000 21.39000  ? 190 ASN A O   1 
ATOM   1438 C  CB  . ASN A  1 196 ? 25.03200  -19.76300 14.37000 1.000 21.96000  ? 190 ASN A CB  1 
ATOM   1439 C  CG  . ASN A  1 196 ? 23.96200  -20.81800 14.69300 1.000 20.33000  ? 190 ASN A CG  1 
ATOM   1440 O  OD1 . ASN A  1 196 ? 23.19900  -20.68400 15.64900 1.000 21.83000  ? 190 ASN A OD1 1 
ATOM   1441 N  ND2 . ASN A  1 196 ? 23.92200  -21.87100 13.89500 1.000 21.88000  ? 190 ASN A ND2 1 
ATOM   1442 N  N   . LEU A  1 197 ? 27.80800  -19.36400 16.78700 1.000 18.20000  ? 191 LEU A N   1 
ATOM   1443 C  CA  . LEU A  1 197 ? 28.78600  -20.07300 17.62400 1.000 20.19000  ? 191 LEU A CA  1 
ATOM   1444 C  C   . LEU A  1 197 ? 28.38500  -20.03300 19.09000 1.000 22.11000  ? 191 LEU A C   1 
ATOM   1445 O  O   . LEU A  1 197 ? 27.69700  -19.10100 19.52700 1.000 19.97000  ? 191 LEU A O   1 
ATOM   1446 C  CB  . LEU A  1 197 ? 30.16600  -19.42300 17.50800 1.000 16.28000  ? 191 LEU A CB  1 
ATOM   1447 C  CG  . LEU A  1 197 ? 30.89500  -19.73100 16.22600 1.000 18.54000  ? 191 LEU A CG  1 
ATOM   1448 C  CD1 . LEU A  1 197 ? 32.07500  -18.81200 16.10200 1.000 20.39000  ? 191 LEU A CD1 1 
ATOM   1449 C  CD2 . LEU A  1 197 ? 31.35200  -21.21500 16.27100 1.000 16.70000  ? 191 LEU A CD2 1 
ATOM   1450 N  N   . PRO A  1 198 ? 28.85200  -20.98900 19.89800 1.000 19.34000  ? 192 PRO A N   1 
ATOM   1451 C  CA  . PRO A  1 198 ? 28.78000  -20.80200 21.35200 1.000 18.54000  ? 192 PRO A CA  1 
ATOM   1452 C  C   . PRO A  1 198 ? 29.52000  -19.53000 21.73500 1.000 20.09000  ? 192 PRO A C   1 
ATOM   1453 O  O   . PRO A  1 198 ? 30.52800  -19.17300 21.12000 1.000 19.28000  ? 192 PRO A O   1 
ATOM   1454 C  CB  . PRO A  1 198 ? 29.48100  -22.03900 21.92200 1.000 22.77000  ? 192 PRO A CB  1 
ATOM   1455 C  CG  . PRO A  1 198 ? 29.53200  -23.07300 20.81700 1.000 22.54000  ? 192 PRO A CG  1 
ATOM   1456 C  CD  . PRO A  1 198 ? 29.54600  -22.24200 19.51200 1.000 21.35000  ? 192 PRO A CD  1 
ATOM   1457 N  N   . THR A  1 199 ? 29.00300  -18.84100 22.75200 1.000 19.11000  ? 193 THR A N   1 
ATOM   1458 C  CA  . THR A  1 199 ? 29.54100  -17.54700 23.15600 1.000 20.40000  ? 193 THR A CA  1 
ATOM   1459 C  C   . THR A  1 199 ? 29.46500  -17.48300 24.67400 1.000 20.20000  ? 193 THR A C   1 
ATOM   1460 O  O   . THR A  1 199 ? 28.48500  -17.96400 25.27100 1.000 22.26000  ? 193 THR A O   1 
ATOM   1461 C  CB  . THR A  1 199 ? 28.78300  -16.36000 22.49700 1.000 19.82000  ? 193 THR A CB  1 
ATOM   1462 O  OG1 . THR A  1 199 ? 29.50700  -15.13800 22.70800 1.000 24.13000  ? 193 THR A OG1 1 
ATOM   1463 C  CG2 . THR A  1 199 ? 27.34100  -16.24300 22.99800 1.000 20.64000  ? 193 THR A CG2 1 
ATOM   1464 N  N   . PRO A  1 200 ? 30.51900  -17.00300 25.32700 1.000 18.40000  ? 194 PRO A N   1 
ATOM   1465 C  CA  . PRO A  1 200 ? 30.62300  -17.16700 26.77700 1.000 17.82000  ? 194 PRO A CA  1 
ATOM   1466 C  C   . PRO A  1 200 ? 30.19700  -15.96400 27.59400 1.000 19.92000  ? 194 PRO A C   1 
ATOM   1467 O  O   . PRO A  1 200 ? 30.30700  -14.80500 27.16600 1.000 15.95000  ? 194 PRO A O   1 
ATOM   1468 C  CB  . PRO A  1 200 ? 32.12300  -17.40700 26.97700 1.000 19.83000  ? 194 PRO A CB  1 
ATOM   1469 C  CG  . PRO A  1 200 ? 32.71700  -16.44800 25.95700 1.000 22.22000  ? 194 PRO A CG  1 
ATOM   1470 C  CD  . PRO A  1 200 ? 31.80600  -16.58800 24.73300 1.000 17.66000  ? 194 PRO A CD  1 
ATOM   1471 N  N   . ALA A  1 201 ? 29.81900  -16.24400 28.82600 1.000 17.43000  ? 195 ALA A N   1 
ATOM   1472 C  CA  . ALA A  1 201 ? 29.55700  -15.21200 29.81500 1.000 18.92000  ? 195 ALA A CA  1 
ATOM   1473 C  C   . ALA A  1 201 ? 30.35500  -15.53300 31.06300 1.000 21.28000  ? 195 ALA A C   1 
ATOM   1474 O  O   . ALA A  1 201 ? 30.37000  -16.68500 31.51400 1.000 19.60000  ? 195 ALA A O   1 
ATOM   1475 C  CB  . ALA A  1 201 ? 28.07500  -15.12600 30.17700 1.000 19.17000  ? 195 ALA A CB  1 
ATOM   1476 N  N   . PHE A  1 202 ? 30.97800  -14.50600 31.63600 1.000 18.40000  ? 196 PHE A N   1 
ATOM   1477 C  CA  . PHE A  1 202 ? 31.76300  -14.65200 32.85200 1.000 20.67000  ? 196 PHE A CA  1 
ATOM   1478 C  C   . PHE A  1 202 ? 31.82700  -13.28600 33.52900 1.000 20.16000  ? 196 PHE A C   1 
ATOM   1479 O  O   . PHE A  1 202 ? 31.31400  -12.29100 32.97900 1.000 20.36000  ? 196 PHE A O   1 
ATOM   1480 C  CB  . PHE A  1 202 ? 33.16100  -15.22400 32.54700 1.000 16.42000  ? 196 PHE A CB  1 
ATOM   1481 C  CG  . PHE A  1 202 ? 33.79900  -14.65500 31.32600 1.000 20.59000  ? 196 PHE A CG  1 
ATOM   1482 C  CD1 . PHE A  1 202 ? 34.46100  -13.44300 31.38700 1.000 18.45000  ? 196 PHE A CD1 1 
ATOM   1483 C  CD2 . PHE A  1 202 ? 33.77900  -15.34700 30.12300 1.000 19.68000  ? 196 PHE A CD2 1 
ATOM   1484 C  CE1 . PHE A  1 202 ? 35.03600  -12.89600 30.26900 1.000 18.12000  ? 196 PHE A CE1 1 
ATOM   1485 C  CE2 . PHE A  1 202 ? 34.40000  -14.82900 28.98500 1.000 17.85000  ? 196 PHE A CE2 1 
ATOM   1486 C  CZ  . PHE A  1 202 ? 35.02600  -13.58000 29.05700 1.000 19.58000  ? 196 PHE A CZ  1 
ATOM   1487 N  N   . PRO A  1 203 ? 32.31800  -13.21900 34.77300 1.000 19.30000  ? 197 PRO A N   1 
ATOM   1488 C  CA  . PRO A  1 203 ? 32.37500  -11.91700 35.46100 1.000 17.73000  ? 197 PRO A CA  1 
ATOM   1489 C  C   . PRO A  1 203 ? 33.15200  -10.88400 34.64900 1.000 17.44000  ? 197 PRO A C   1 
ATOM   1490 O  O   . PRO A  1 203 ? 34.14100  -11.19900 33.99000 1.000 17.59000  ? 197 PRO A O   1 
ATOM   1491 C  CB  . PRO A  1 203 ? 33.07500  -12.24900 36.77800 1.000 21.40000  ? 197 PRO A CB  1 
ATOM   1492 C  CG  . PRO A  1 203 ? 32.60100  -13.65400 37.06600 1.000 21.23000  ? 197 PRO A CG  1 
ATOM   1493 C  CD  . PRO A  1 203 ? 32.63400  -14.32300 35.71000 1.000 21.35000  ? 197 PRO A CD  1 
ATOM   1494 N  N   . LEU A  1 204 ? 32.66300  -9.63900  34.67600 1.000 19.05000  ? 198 LEU A N   1 
ATOM   1495 C  CA  . LEU A  1 204 ? 33.23500  -8.59000  33.83200 1.000 18.79000  ? 198 LEU A CA  1 
ATOM   1496 C  C   . LEU A  1 204 ? 34.73000  -8.41300  34.07900 1.000 19.57000  ? 198 LEU A C   1 
ATOM   1497 O  O   . LEU A  1 204 ? 35.50300  -8.21900  33.13100 1.000 18.30000  ? 198 LEU A O   1 
ATOM   1498 C  CB  . LEU A  1 204 ? 32.48000  -7.27500  34.06900 1.000 17.75000  ? 198 LEU A CB  1 
ATOM   1499 C  CG  . LEU A  1 204 ? 32.84500  -6.08500  33.19200 1.000 18.78000  ? 198 LEU A CG  1 
ATOM   1500 C  CD1 . LEU A  1 204 ? 32.59800  -6.44000  31.75300 1.000 19.81000  ? 198 LEU A CD1 1 
ATOM   1501 C  CD2 . LEU A  1 204 ? 32.02000  -4.87900  33.61800 1.000 16.63000  ? 198 LEU A CD2 1 
ATOM   1502 N  N   . ASP A  1 205 ? 35.16700  -8.50600  35.33700 1.000 18.22000  ? 199 ASP A N   1 
ATOM   1503 C  CA  . ASP A  1 205 ? 36.58900  -8.32400  35.60700 1.000 18.93000  ? 199 ASP A CA  1 
ATOM   1504 C  C   . ASP A  1 205 ? 37.45400  -9.34200  34.86100 1.000 22.03000  ? 199 ASP A C   1 
ATOM   1505 O  O   . ASP A  1 205 ? 38.58500  -9.02600  34.46200 1.000 20.93000  ? 199 ASP A O   1 
ATOM   1506 C  CB  . ASP A  1 205 ? 36.84100  -8.40200  37.11200 1.000 19.13000  ? 199 ASP A CB  1 
ATOM   1507 C  CG  . ASP A  1 205 ? 36.57700  -9.78500  37.67000 1.000 23.29000  ? 199 ASP A CG  1 
ATOM   1508 O  OD1 . ASP A  1 205 ? 35.39700  -10.24600 37.61900 1.000 21.96000  ? 199 ASP A OD1 1 
ATOM   1509 O  OD2 . ASP A  1 205 ? 37.55600  -10.39700 38.15400 1.000 20.86000  ? 199 ASP A OD2 1 
ATOM   1510 N  N   . ARG A  1 206 ? 36.94200  -10.55900 34.66000 1.000 19.55000  ? 200 ARG A N   1 
ATOM   1511 C  CA  . ARG A  1 206 ? 37.70000  -11.58000 33.94800 1.000 21.95000  ? 200 ARG A CA  1 
ATOM   1512 C  C   . ARG A  1 206 ? 37.87700  -11.22800 32.48500 1.000 18.06000  ? 200 ARG A C   1 
ATOM   1513 O  O   . ARG A  1 206 ? 38.81100  -11.72000 31.84300 1.000 21.79000  ? 200 ARG A O   1 
ATOM   1514 C  CB  . ARG A  1 206 ? 37.00400  -12.93600 34.09800 1.000 21.27000  ? 200 ARG A CB  1 
ATOM   1515 C  CG  . ARG A  1 206 ? 36.73100  -13.33800 35.54900 1.000 22.64000  ? 200 ARG A CG  1 
ATOM   1516 C  CD  . ARG A  1 206 ? 38.07000  -13.47500 36.35400 1.000 24.31000  ? 200 ARG A CD  1 
ATOM   1517 N  NE  . ARG A  1 206 ? 37.83700  -13.74300 37.77300 1.000 30.09000  ? 200 ARG A NE  1 
ATOM   1518 C  CZ  . ARG A  1 206 ? 38.26900  -14.81100 38.43900 1.000 29.65000  ? 200 ARG A CZ  1 
ATOM   1519 N  NH1 . ARG A  1 206 ? 39.02000  -15.73300 37.86200 1.000 28.53000  ? 200 ARG A NH1 1 
ATOM   1520 N  NH2 . ARG A  1 206 ? 37.96300  -14.94200 39.72600 1.000 32.50000  ? 200 ARG A NH2 1 
ATOM   1521 N  N   . LEU A  1 207 ? 36.96100  -10.43800 31.91100 1.000 16.74000  ? 201 LEU A N   1 
ATOM   1522 C  CA  . LEU A  1 207 ? 37.20100  -9.94300  30.56600 1.000 15.75000  ? 201 LEU A CA  1 
ATOM   1523 C  C   . LEU A  1 207 ? 38.39400  -8.99600  30.56600 1.000 19.47000  ? 201 LEU A C   1 
ATOM   1524 O  O   . LEU A  1 207 ? 39.28800  -9.11100  29.71600 1.000 17.59000  ? 201 LEU A O   1 
ATOM   1525 C  CB  . LEU A  1 207 ? 35.94400  -9.25100  29.99600 1.000 22.31000  ? 201 LEU A CB  1 
ATOM   1526 C  CG  . LEU A  1 207 ? 36.04500  -8.69700  28.56900 1.000 21.54000  ? 201 LEU A CG  1 
ATOM   1527 C  CD1 . LEU A  1 207 ? 36.43100  -9.82500  27.55200 1.000 22.70000  ? 201 LEU A CD1 1 
ATOM   1528 C  CD2 . LEU A  1 207 ? 34.78000  -7.90900  28.08500 1.000 17.56000  ? 201 LEU A CD2 1 
ATOM   1529 N  N   . GLY A  1 208 ? 38.46000  -8.09400  31.55300 1.000 18.95000  ? 202 GLY A N   1 
ATOM   1530 C  CA  . GLY A  1 208 ? 39.63300  -7.24500  31.68500 1.000 20.04000  ? 202 GLY A CA  1 
ATOM   1531 C  C   . GLY A  1 208 ? 40.89000  -8.05100  31.94600 1.000 23.28000  ? 202 GLY A C   1 
ATOM   1532 O  O   . GLY A  1 208 ? 41.98900  -7.66700  31.51800 1.000 25.65000  ? 202 GLY A O   1 
ATOM   1533 N  N   . ARG A  1 209 ? 40.74500  -9.19900  32.61400 1.000 19.52000  ? 203 ARG A N   1 
ATOM   1534 C  CA  . ARG A  1 209 ? 41.90800  -10.04900 32.87100 1.000 22.73000  ? 203 ARG A CA  1 
ATOM   1535 C  C   . ARG A  1 209 ? 42.48600  -10.60700 31.57700 1.000 21.86000  ? 203 ARG A C   1 
ATOM   1536 O  O   . ARG A  1 209 ? 43.71900  -10.62000 31.39400 1.000 20.45000  ? 203 ARG A O   1 
ATOM   1537 C  CB  . ARG A  1 209 ? 41.52100  -11.18100 33.82100 1.000 21.39000  ? 203 ARG A CB  1 
ATOM   1538 C  CG  . ARG A  1 209 ? 42.65900  -12.05600 34.25100 1.000 21.36000  ? 203 ARG A CG  1 
ATOM   1539 C  CD  . ARG A  1 209 ? 42.22500  -13.20900 35.15700 1.000 23.24000  ? 203 ARG A CD  1 
ATOM   1540 N  NE  . ARG A  1 209 ? 41.67200  -12.75600 36.42600 1.000 26.80000  ? 203 ARG A NE  1 
ATOM   1541 C  CZ  . ARG A  1 209 ? 41.82000  -13.39500 37.58000 1.000 27.08000  ? 203 ARG A CZ  1 
ATOM   1542 N  NH1 . ARG A  1 209 ? 42.54500  -14.50600 37.67400 1.000 25.41000  ? 203 ARG A NH1 1 
ATOM   1543 N  NH2 . ARG A  1 209 ? 41.23400  -12.90900 38.67100 1.000 24.43000  ? 203 ARG A NH2 1 
ATOM   1544 N  N   . ILE A  1 210 ? 41.61700  -11.03200 30.65200 1.000 20.73000  ? 204 ILE A N   1 
ATOM   1545 C  CA  . ILE A  1 210 ? 42.08300  -11.54400 29.36600 1.000 21.62000  ? 204 ILE A CA  1 
ATOM   1546 C  C   . ILE A  1 210 ? 42.93400  -10.50100 28.66200 1.000 20.57000  ? 204 ILE A C   1 
ATOM   1547 O  O   . ILE A  1 210 ? 44.04600  -10.78600 28.19200 1.000 22.24000  ? 204 ILE A O   1 
ATOM   1548 C  CB  . ILE A  1 210 ? 40.89100  -11.97300 28.49600 1.000 21.99000  ? 204 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A  1 210 ? 40.25700  -13.23800 29.08200 1.000 22.80000  ? 204 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A  1 210 ? 41.34500  -12.25300 27.07300 1.000 21.67000  ? 204 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A  1 210 ? 38.96000  -13.60600 28.41200 1.000 22.81000  ? 204 ILE A CD1 1 
ATOM   1552 N  N   . TYR A  1 211 ? 42.43300  -9.26000  28.61500 1.000 22.26000  ? 205 TYR A N   1 
ATOM   1553 C  CA  . TYR A  1 211 ? 43.13000  -8.21000  27.89200 1.000 20.68000  ? 205 TYR A CA  1 
ATOM   1554 C  C   . TYR A  1 211 ? 44.38500  -7.74600  28.62200 1.000 20.07000  ? 205 TYR A C   1 
ATOM   1555 O  O   . TYR A  1 211 ? 45.35000  -7.35000  27.97700 1.000 22.50000  ? 205 TYR A O   1 
ATOM   1556 C  CB  . TYR A  1 211 ? 42.14200  -7.06800  27.60000 1.000 20.13000  ? 205 TYR A CB  1 
ATOM   1557 C  CG  . TYR A  1 211 ? 41.26800  -7.45500  26.44200 1.000 22.38000  ? 205 TYR A CG  1 
ATOM   1558 C  CD1 . TYR A  1 211 ? 40.31400  -8.49100  26.56100 1.000 20.89000  ? 205 TYR A CD1 1 
ATOM   1559 C  CD2 . TYR A  1 211 ? 41.41200  -6.82200  25.20700 1.000 19.83000  ? 205 TYR A CD2 1 
ATOM   1560 C  CE1 . TYR A  1 211 ? 39.50600  -8.87600  25.48000 1.000 18.25000  ? 205 TYR A CE1 1 
ATOM   1561 C  CE2 . TYR A  1 211 ? 40.60400  -7.18900  24.12500 1.000 19.86000  ? 205 TYR A CE2 1 
ATOM   1562 C  CZ  . TYR A  1 211 ? 39.66200  -8.21400  24.26700 1.000 19.31000  ? 205 TYR A CZ  1 
ATOM   1563 O  OH  . TYR A  1 211 ? 38.90100  -8.56500  23.16700 1.000 19.77000  ? 205 TYR A OH  1 
ATOM   1564 N  N   . ALA A  1 212 ? 44.42300  -7.83600  29.95300 1.000 19.71000  ? 206 ALA A N   1 
ATOM   1565 C  CA  . ALA A  1 212 ? 45.67000  -7.53600  30.65900 1.000 23.16000  ? 206 ALA A CA  1 
ATOM   1566 C  C   . ALA A  1 212 ? 46.73200  -8.59600  30.35600 1.000 25.92000  ? 206 ALA A C   1 
ATOM   1567 O  O   . ALA A  1 212 ? 47.94600  -8.29500  30.28600 1.000 23.14000  ? 206 ALA A O   1 
ATOM   1568 C  CB  . ALA A  1 212 ? 45.39900  -7.43800  32.15900 1.000 23.27000  ? 206 ALA A CB  1 
ATOM   1569 N  N   . LYS A  1 213 ? 46.28200  -9.83800  30.14700 1.000 22.76000  ? 207 LYS A N   1 
ATOM   1570 C  CA  . LYS A  1 213 ? 47.17900  -10.92100 29.77200 1.000 22.54000  ? 207 LYS A CA  1 
ATOM   1571 C  C   . LYS A  1 213 ? 47.67100  -10.77100 28.33400 1.000 24.30000  ? 207 LYS A C   1 
ATOM   1572 O  O   . LYS A  1 213 ? 48.81600  -11.13100 28.02600 1.000 25.47000  ? 207 LYS A O   1 
ATOM   1573 C  CB  . LYS A  1 213 ? 46.47200  -12.26000 29.96400 1.000 20.84000  ? 207 LYS A CB  1 
ATOM   1574 C  CG  . LYS A  1 213 ? 46.28600  -12.68100 31.41800 1.000 25.44000  ? 207 LYS A CG  1 
ATOM   1575 C  CD  . LYS A  1 213 ? 45.57600  -14.02900 31.51500 1.000 26.93000  ? 207 LYS A CD  1 
ATOM   1576 C  CE  . LYS A  1 213 ? 45.57500  -14.56500 32.93300 1.000 24.93000  ? 207 LYS A CE  1 
ATOM   1577 N  NZ  . LYS A  1 213 ? 44.94400  -15.91400 32.98100 1.000 28.20000  ? 207 LYS A NZ  1 
ATOM   1578 N  N   . LEU A  1 214 ? 46.81500  -10.28900 27.42800 1.000 23.00000  ? 208 LEU A N   1 
ATOM   1579 C  CA  . LEU A  1 214 ? 47.27600  -9.93300  26.08400 1.000 25.30000  ? 208 LEU A CA  1 
ATOM   1580 C  C   . LEU A  1 214 ? 48.39900  -8.90300  26.13600 1.000 23.18000  ? 208 LEU A C   1 
ATOM   1581 O  O   . LEU A  1 214 ? 49.42500  -9.03700  25.46300 1.000 25.76000  ? 208 LEU A O   1 
ATOM   1582 C  CB  . LEU A  1 214 ? 46.09800  -9.39200  25.25700 1.000 22.30000  ? 208 LEU A CB  1 
ATOM   1583 C  CG  . LEU A  1 214 ? 45.15400  -10.44300 24.65800 1.000 24.22000  ? 208 LEU A CG  1 
ATOM   1584 C  CD1 . LEU A  1 214 ? 43.91800  -9.80200  24.06500 1.000 21.75000  ? 208 LEU A CD1 1 
ATOM   1585 C  CD2 . LEU A  1 214 ? 45.89700  -11.27100 23.59400 1.000 27.54000  ? 208 LEU A CD2 1 
ATOM   1586 N  N   . ALA A  1 215 ? 48.21000  -7.84600  26.90800 1.000 24.87000  ? 209 ALA A N   1 
ATOM   1587 C  CA  . ALA A  1 215 ? 49.18800  -6.77200  26.90800 1.000 25.65000  ? 209 ALA A CA  1 
ATOM   1588 C  C   . ALA A  1 215 ? 50.44200  -7.14800  27.68100 1.000 27.50000  ? 209 ALA A C   1 
ATOM   1589 O  O   . ALA A  1 215 ? 51.54700  -6.68200  27.35300 1.000 27.62000  ? 209 ALA A O   1 
ATOM   1590 C  CB  . ALA A  1 215 ? 48.57000  -5.51900  27.50700 1.000 23.14000  ? 209 ALA A CB  1 
ATOM   1591 N  N   . SER A  1 216 ? 50.28000  -7.96300  28.72000 1.000 23.12000  ? 210 SER A N   1 
ATOM   1592 C  CA  . SER A  1 216 ? 51.43400  -8.43600  29.46000 1.000 26.57000  ? 210 SER A CA  1 
ATOM   1593 C  C   . SER A  1 216 ? 52.28800  -9.34500  28.58500 1.000 28.32000  ? 210 SER A C   1 
ATOM   1594 O  O   . SER A  1 216 ? 53.52100  -9.24200  28.59200 1.000 26.45000  ? 210 SER A O   1 
ATOM   1595 C  CB  . SER A  1 216 ? 50.96400  -9.14300  30.72900 1.000 25.61000  ? 210 SER A CB  1 
ATOM   1596 O  OG  . SER A  1 216 ? 52.06200  -9.66200  31.45600 1.000 26.82000  ? 210 SER A OG  1 
ATOM   1597 N  N   . ALA A  1 217 ? 51.64700  -10.18200 27.76400 1.000 26.09000  ? 211 ALA A N   1 
ATOM   1598 C  CA  . ALA A  1 217 ? 52.39500  -11.02100 26.83100 1.000 29.98000  ? 211 ALA A CA  1 
ATOM   1599 C  C   . ALA A  1 217 ? 53.18300  -10.18800 25.82300 1.000 30.90000  ? 211 ALA A C   1 
ATOM   1600 O  O   . ALA A  1 217 ? 54.34500  -10.49300 25.53600 1.000 33.40000  ? 211 ALA A O   1 
ATOM   1601 C  CB  . ALA A  1 217 ? 51.44700  -11.98100 26.10800 1.000 29.51000  ? 211 ALA A CB  1 
ATOM   1602 N  N   . ALA A  1 218 ? 52.55700  -9.15400  25.25500 1.000 28.39000  ? 212 ALA A N   1 
ATOM   1603 C  CA  . ALA A  1 218 ? 53.26700  -8.23500  24.37100 1.000 29.04000  ? 212 ALA A CA  1 
ATOM   1604 C  C   . ALA A  1 218 ? 54.47000  -7.62800  25.07600 1.000 32.85000  ? 212 ALA A C   1 
ATOM   1605 O  O   . ALA A  1 218 ? 55.55300  -7.51800  24.49000 1.000 36.02000  ? 212 ALA A O   1 
ATOM   1606 C  CB  . ALA A  1 218 ? 52.30900  -7.14400  23.88200 1.000 29.82000  ? 212 ALA A CB  1 
ATOM   1607 N  N   . ASP A  1 219 ? 54.30800  -7.25800  26.34700 1.000 28.26000  ? 213 ASP A N   1 
ATOM   1608 C  CA  . ASP A  1 219 ? 55.40300  -6.68600  27.12500 1.000 32.65000  ? 213 ASP A CA  1 
ATOM   1609 C  C   . ASP A  1 219 ? 56.55300  -7.67900  27.26700 1.000 37.97000  ? 213 ASP A C   1 
ATOM   1610 O  O   . ASP A  1 219 ? 57.73200  -7.32400  27.08600 1.000 36.64000  ? 213 ASP A O   1 
ATOM   1611 C  CB  . ASP A  1 219 ? 54.88400  -6.26800  28.50400 1.000 31.28000  ? 213 ASP A CB  1 
ATOM   1612 C  CG  . ASP A  1 219 ? 54.21200  -4.88700  28.50400 1.000 32.07000  ? 213 ASP A CG  1 
ATOM   1613 O  OD1 . ASP A  1 219 ? 54.38300  -4.10200  27.54200 1.000 33.93000  ? 213 ASP A OD1 1 
ATOM   1614 O  OD2 . ASP A  1 219 ? 53.54100  -4.57000  29.50200 1.000 28.93000  ? 213 ASP A OD2 1 
ATOM   1615 N  N   . GLY A  1 220 ? 56.22600  -8.93300  27.60400 1.000 38.96000  ? 214 GLY A N   1 
ATOM   1616 C  CA  . GLY A  1 220 ? 57.25700  -9.94200  27.79000 1.000 44.01000  ? 214 GLY A CA  1 
ATOM   1617 C  C   . GLY A  1 220 ? 57.98100  -10.28300 26.50300 1.000 50.09000  ? 214 GLY A C   1 
ATOM   1618 O  O   . GLY A  1 220 ? 59.19700  -10.49300 26.50200 1.000 51.49000  ? 214 GLY A O   1 
ATOM   1619 N  N   . SER A  1 221 ? 57.24800  -10.32000 25.38900 1.000 43.89000  ? 215 SER A N   1 
ATOM   1620 C  CA  . SER A  1 221 ? 57.85900  -10.53400 24.08000 1.000 43.10000  ? 215 SER A CA  1 
ATOM   1621 C  C   . SER A  1 221 ? 58.78100  -9.38100  23.70100 1.000 46.13000  ? 215 SER A C   1 
ATOM   1622 O  O   . SER A  1 221 ? 59.87100  -9.59800  23.17000 1.000 46.79000  ? 215 SER A O   1 
ATOM   1623 C  CB  . SER A  1 221 ? 56.76600  -10.71700 23.03000 1.000 42.94000  ? 215 SER A CB  1 
ATOM   1624 O  OG  . SER A  1 221 ? 57.33300  -10.77300 21.73800 1.000 52.18000  ? 215 SER A OG  1 
ATOM   1625 N  N   . ASP A  1 222 ? 58.35300  -8.14600  23.95700 1.000 53.73000  ? 216 ASP A N   1 
ATOM   1626 C  CA  . ASP A  1 222 ? 59.22000  -6.99300  23.74600 1.000 56.81000  ? 216 ASP A CA  1 
ATOM   1627 C  C   . ASP A  1 222 ? 60.49600  -7.09600  24.57200 1.000 57.80000  ? 216 ASP A C   1 
ATOM   1628 O  O   . ASP A  1 222 ? 61.55600  -6.61600  24.14900 1.000 60.21000  ? 216 ASP A O   1 
ATOM   1629 C  CB  . ASP A  1 222 ? 58.45800  -5.72100  24.11600 1.000 56.02000  ? 216 ASP A CB  1 
ATOM   1630 C  CG  . ASP A  1 222 ? 58.65800  -4.60000  23.13000 1.000 58.72000  ? 216 ASP A CG  1 
ATOM   1631 O  OD1 . ASP A  1 222 ? 58.06200  -4.65600  22.02800 1.000 62.45000  ? 216 ASP A OD1 1 
ATOM   1632 O  OD2 . ASP A  1 222 ? 59.38900  -3.64500  23.47500 1.000 63.14000  ? 216 ASP A OD2 1 
ATOM   1633 N  N   . ALA A  1 223 ? 60.40700  -7.71400  25.75000 1.000 49.61000  ? 217 ALA A N   1 
ATOM   1634 C  CA  . ALA A  1 223 ? 61.50500  -7.80300  26.70200 1.000 58.78000  ? 217 ALA A CA  1 
ATOM   1635 C  C   . ALA A  1 223 ? 62.37500  -9.05600  26.52300 1.000 59.45000  ? 217 ALA A C   1 
ATOM   1636 O  O   . ALA A  1 223 ? 63.35600  -9.21900  27.25500 1.000 62.48000  ? 217 ALA A O   1 
ATOM   1637 C  CB  . ALA A  1 223 ? 60.93800  -7.73900  28.12800 1.000 48.12000  ? 217 ALA A CB  1 
ATOM   1638 N  N   . GLY A  1 224 ? 62.04400  -9.94400  25.57900 1.000 59.56000  ? 218 GLY A N   1 
ATOM   1639 C  CA  . GLY A  1 224 ? 62.87800  -11.09400 25.26300 1.000 62.70000  ? 218 GLY A CA  1 
ATOM   1640 C  C   . GLY A  1 224 ? 63.03200  -12.12300 26.36800 1.000 78.10000  ? 218 GLY A C   1 
ATOM   1641 O  O   . GLY A  1 224 ? 64.13500  -12.35000 26.87700 1.000 68.59000  ? 218 GLY A O   1 
ATOM   1642 N  N   . GLU A  1 225 ? 61.93900  -12.78100 26.73300 1.000 97.89000  ? 219 GLU A N   1 
ATOM   1643 C  CA  . GLU A  1 225 ? 61.92900  -13.65500 27.89400 1.000 100.47000 ? 219 GLU A CA  1 
ATOM   1644 C  C   . GLU A  1 225 ? 61.67000  -15.09800 27.48900 1.000 101.07000 ? 219 GLU A C   1 
ATOM   1645 O  O   . GLU A  1 225 ? 61.19400  -15.38400 26.38500 1.000 100.91000 ? 219 GLU A O   1 
ATOM   1646 C  CB  . GLU A  1 225 ? 60.86000  -13.21300 28.89800 1.000 92.80000  ? 219 GLU A CB  1 
ATOM   1647 C  CG  . GLU A  1 225 ? 61.05600  -11.80700 29.41700 1.000 91.16000  ? 219 GLU A CG  1 
ATOM   1648 C  CD  . GLU A  1 225 ? 59.77400  -11.21700 29.94800 1.000 96.05000  ? 219 GLU A CD  1 
ATOM   1649 O  OE1 . GLU A  1 225 ? 58.75000  -11.93300 29.93400 1.000 99.86000  ? 219 GLU A OE1 1 
ATOM   1650 O  OE2 . GLU A  1 225 ? 59.78800  -10.04100 30.37200 1.000 96.13000  ? 219 GLU A OE2 1 
ATOM   1651 N  N   . GLY A  1 226 ? 61.97900  -16.01000 28.41300 1.000 86.20000  ? 220 GLY A N   1 
ATOM   1652 C  CA  . GLY A  1 226 ? 61.51700  -17.37900 28.29900 1.000 80.15000  ? 220 GLY A CA  1 
ATOM   1653 C  C   . GLY A  1 226 ? 60.00000  -17.42900 28.33100 1.000 79.77000  ? 220 GLY A C   1 
ATOM   1654 O  O   . GLY A  1 226 ? 59.40600  -17.98000 29.26400 1.000 82.04000  ? 220 GLY A O   1 
ATOM   1655 N  N   . GLN A  1 227 ? 59.36400  -16.83800 27.32000 1.000 74.26000  ? 221 GLN A N   1 
ATOM   1656 C  CA  . GLN A  1 227 ? 57.91200  -16.81500 27.25400 1.000 64.28000  ? 221 GLN A CA  1 
ATOM   1657 C  C   . GLN A  1 227 ? 57.37600  -18.19600 26.91800 1.000 57.84000  ? 221 GLN A C   1 
ATOM   1658 O  O   . GLN A  1 227 ? 57.85600  -18.85100 25.98700 1.000 58.55000  ? 221 GLN A O   1 
ATOM   1659 C  CB  . GLN A  1 227 ? 57.43600  -15.81000 26.20700 1.000 57.91000  ? 221 GLN A CB  1 
ATOM   1660 C  CG  . GLN A  1 227 ? 56.94200  -14.51700 26.78900 1.000 56.33000  ? 221 GLN A CG  1 
ATOM   1661 C  CD  . GLN A  1 227 ? 56.25800  -13.63300 25.76000 1.000 50.14000  ? 221 GLN A CD  1 
ATOM   1662 O  OE1 . GLN A  1 227 ? 56.45000  -13.78800 24.54100 1.000 48.47000  ? 221 GLN A OE1 1 
ATOM   1663 N  NE2 . GLN A  1 227 ? 55.46300  -12.69000 26.24600 1.000 40.23000  ? 221 GLN A NE2 1 
ATOM   1664 N  N   . SER A  1 228 ? 56.37300  -18.63400 27.67600 1.000 54.50000  ? 222 SER A N   1 
ATOM   1665 C  CA  . SER A  1 228 ? 55.62400  -19.82200 27.30700 1.000 44.82000  ? 222 SER A CA  1 
ATOM   1666 C  C   . SER A  1 228 ? 55.11800  -19.67300 25.88000 1.000 43.22000  ? 222 SER A C   1 
ATOM   1667 O  O   . SER A  1 228 ? 54.99000  -18.55300 25.36800 1.000 40.74000  ? 222 SER A O   1 
ATOM   1668 C  CB  . SER A  1 228 ? 54.46600  -20.01800 28.27400 1.000 43.56000  ? 222 SER A CB  1 
ATOM   1669 O  OG  . SER A  1 228 ? 53.56800  -18.91500 28.17100 1.000 47.50000  ? 222 SER A OG  1 
ATOM   1670 N  N   . THR A  1 229 ? 54.85500  -20.80300 25.21600 1.000 41.08000  ? 223 THR A N   1 
ATOM   1671 C  CA  . THR A  1 229 ? 54.30500  -20.70600 23.87100 1.000 38.77000  ? 223 THR A CA  1 
ATOM   1672 C  C   . THR A  1 229 ? 52.98800  -19.97100 23.89700 1.000 36.40000  ? 223 THR A C   1 
ATOM   1673 O  O   . THR A  1 229 ? 52.66300  -19.24200 22.95500 1.000 36.81000  ? 223 THR A O   1 
ATOM   1674 C  CB  . THR A  1 229 ? 54.06800  -22.07500 23.24800 1.000 38.55000  ? 223 THR A CB  1 
ATOM   1675 O  OG1 . THR A  1 229 ? 53.12200  -22.79300 24.03800 1.000 38.13000  ? 223 THR A OG1 1 
ATOM   1676 C  CG2 . THR A  1 229 ? 55.36400  -22.85800 23.14300 1.000 41.44000  ? 223 THR A CG2 1 
ATOM   1677 N  N   . ARG A  1 230 ? 52.21000  -20.16300 24.95300 1.000 35.70000  ? 224 ARG A N   1 
ATOM   1678 C  CA  . ARG A  1 230 ? 50.90700  -19.50600 25.01100 1.000 34.38000  ? 224 ARG A CA  1 
ATOM   1679 C  C   . ARG A  1 230 ? 51.07600  -17.99800 25.11300 1.000 34.71000  ? 224 ARG A C   1 
ATOM   1680 O  O   . ARG A  1 230 ? 50.32200  -17.25200 24.46900 1.000 32.46000  ? 224 ARG A O   1 
ATOM   1681 C  CB  . ARG A  1 230 ? 50.06400  -20.01800 26.17200 1.000 33.86000  ? 224 ARG A CB  1 
ATOM   1682 C  CG  . ARG A  1 230 ? 48.81500  -19.14000 26.39800 1.000 31.71000  ? 224 ARG A CG  1 
ATOM   1683 C  CD  . ARG A  1 230 ? 47.73900  -19.86000 27.17000 1.000 34.60000  ? 224 ARG A CD  1 
ATOM   1684 N  NE  . ARG A  1 230 ? 47.13000  -20.93700 26.39900 1.000 35.33000  ? 224 ARG A NE  1 
ATOM   1685 C  CZ  . ARG A  1 230 ? 46.12600  -21.68600 26.83400 1.000 36.43000  ? 224 ARG A CZ  1 
ATOM   1686 N  NH1 . ARG A  1 230 ? 45.62500  -21.53200 28.04900 1.000 39.06000  ? 224 ARG A NH1 1 
ATOM   1687 N  NH2 . ARG A  1 230 ? 45.60200  -22.60600 26.02700 1.000 35.46000  ? 224 ARG A NH2 1 
HETATM 1688 N  N   . CSO A  1 231 ? 52.04400  -17.54000 25.90900 1.000 35.25000  ? 225 CSO A N   1 
HETATM 1689 C  CA  . CSO A  1 231 ? 52.29100  -16.10300 25.99200 1.000 39.14000  ? 225 CSO A CA  1 
HETATM 1690 C  CB  . CSO A  1 231 ? 53.30800  -15.75700 27.08600 1.000 43.74000  ? 225 CSO A CB  1 
HETATM 1691 S  SG  . CSO A  1 231 ? 52.57000  -15.74600 28.74600 1.000 49.85000  ? 225 CSO A SG  1 
HETATM 1692 C  C   . CSO A  1 231 ? 52.77900  -15.58200 24.64400 1.000 37.60000  ? 225 CSO A C   1 
HETATM 1693 O  O   . CSO A  1 231 ? 52.41100  -14.49700 24.23200 1.000 35.49000  ? 225 CSO A O   1 
HETATM 1694 O  OD  . CSO A  1 231 ? 53.81500  -15.62100 30.02400 1.000 58.06000  ? 225 CSO A OD  1 
ATOM   1695 N  N   . ALA A  1 232 ? 53.62600  -16.35500 23.96800 1.000 36.09000  ? 226 ALA A N   1 
ATOM   1696 C  CA  . ALA A  1 232 ? 54.06500  -15.99700 22.62000 1.000 35.46000  ? 226 ALA A CA  1 
ATOM   1697 C  C   . ALA A  1 232 ? 52.87100  -15.77800 21.68800 1.000 32.69000  ? 226 ALA A C   1 
ATOM   1698 O  O   . ALA A  1 232 ? 52.80500  -14.76800 20.97300 1.000 31.94000  ? 226 ALA A O   1 
ATOM   1699 C  CB  . ALA A  1 232 ? 54.99800  -17.07500 22.05900 1.000 39.35000  ? 226 ALA A CB  1 
ATOM   1700 N  N   . ALA A  1 233 ? 51.92200  -16.72100 21.70600 1.000 32.79000  ? 227 ALA A N   1 
ATOM   1701 C  CA  . ALA A  1 233 ? 50.72600  -16.58200 20.87800 1.000 31.28000  ? 227 ALA A CA  1 
ATOM   1702 C  C   . ALA A  1 233 ? 49.86900  -15.40500 21.32500 1.000 31.02000  ? 227 ALA A C   1 
ATOM   1703 O  O   . ALA A  1 233 ? 49.23900  -14.75400 20.48800 1.000 29.27000  ? 227 ALA A O   1 
ATOM   1704 C  CB  . ALA A  1 233 ? 49.88700  -17.85800 20.90400 1.000 30.70000  ? 227 ALA A CB  1 
ATOM   1705 N  N   . LEU A  1 234 ? 49.75400  -15.16700 22.63800 1.000 31.11000  ? 228 LEU A N   1 
ATOM   1706 C  CA  . LEU A  1 234 ? 48.99700  -13.99200 23.07300 1.000 31.24000  ? 228 LEU A CA  1 
ATOM   1707 C  C   . LEU A  1 234 ? 49.67200  -12.73300 22.56600 1.000 29.38000  ? 228 LEU A C   1 
ATOM   1708 O  O   . LEU A  1 234 ? 49.01600  -11.83700 22.02600 1.000 27.95000  ? 228 LEU A O   1 
ATOM   1709 C  CB  . LEU A  1 234 ? 48.87000  -13.95200 24.59600 1.000 28.06000  ? 228 LEU A CB  1 
ATOM   1710 C  CG  . LEU A  1 234 ? 47.91200  -14.99100 25.16300 1.000 32.59000  ? 228 LEU A CG  1 
ATOM   1711 C  CD1 . LEU A  1 234 ? 48.08600  -15.14200 26.65200 1.000 29.57000  ? 228 LEU A CD1 1 
ATOM   1712 C  CD2 . LEU A  1 234 ? 46.49100  -14.55600 24.80600 1.000 26.60000  ? 228 LEU A CD2 1 
ATOM   1713 N  N   . ALA A  1 235 ? 50.99800  -12.68000 22.69600 1.000 29.39000  ? 229 ALA A N   1 
ATOM   1714 C  CA  . ALA A  1 235 ? 51.77300  -11.57000 22.16300 1.000 29.97000  ? 229 ALA A CA  1 
ATOM   1715 C  C   . ALA A  1 235 ? 51.54400  -11.38800 20.66800 1.000 28.89000  ? 229 ALA A C   1 
ATOM   1716 O  O   . ALA A  1 235 ? 51.46100  -10.25400 20.18400 1.000 30.02000  ? 229 ALA A O   1 
ATOM   1717 C  CB  . ALA A  1 235 ? 53.25600  -11.79900 22.45600 1.000 32.71000  ? 229 ALA A CB  1 
ATOM   1718 N  N   . HIS A  1 236 ? 51.46300  -12.48600 19.91300 1.000 28.75000  ? 230 HIS A N   1 
ATOM   1719 C  CA  . HIS A  1 236 ? 51.22500  -12.37500 18.47700 1.000 28.11000  ? 230 HIS A CA  1 
ATOM   1720 C  C   . HIS A  1 236 ? 49.84700  -11.78600 18.20400 1.000 27.26000  ? 230 HIS A C   1 
ATOM   1721 O  O   . HIS A  1 236 ? 49.67600  -10.94600 17.30900 1.000 27.69000  ? 230 HIS A O   1 
ATOM   1722 C  CB  . HIS A  1 236 ? 51.34000  -13.74900 17.82300 1.000 28.59000  ? 230 HIS A CB  1 
ATOM   1723 C  CG  . HIS A  1 236 ? 51.43100  -13.70600 16.33100 1.000 30.94000  ? 230 HIS A CG  1 
ATOM   1724 N  ND1 . HIS A  1 236 ? 51.55800  -14.84400 15.56200 1.000 37.61000  ? 230 HIS A ND1 1 
ATOM   1725 C  CD2 . HIS A  1 236 ? 51.42400  -12.66400 15.46400 1.000 30.52000  ? 230 HIS A CD2 1 
ATOM   1726 C  CE1 . HIS A  1 236 ? 51.62900  -14.50400 14.28600 1.000 37.67000  ? 230 HIS A CE1 1 
ATOM   1727 N  NE2 . HIS A  1 236 ? 51.54100  -13.18800 14.19900 1.000 34.06000  ? 230 HIS A NE2 1 
ATOM   1728 N  N   . ILE A  1 237 ? 48.85100  -12.23000 18.95900 1.000 24.66000  ? 231 ILE A N   1 
ATOM   1729 C  CA  . ILE A  1 237 ? 47.50500  -11.70100 18.79700 1.000 24.47000  ? 231 ILE A CA  1 
ATOM   1730 C  C   . ILE A  1 237 ? 47.47900  -10.20300 19.08300 1.000 25.26000  ? 231 ILE A C   1 
ATOM   1731 O  O   . ILE A  1 237 ? 46.88000  -9.42700  18.32900 1.000 21.75000  ? 231 ILE A O   1 
ATOM   1732 C  CB  . ILE A  1 237 ? 46.53500  -12.47600 19.69900 1.000 22.45000  ? 231 ILE A CB  1 
ATOM   1733 C  CG1 . ILE A  1 237 ? 46.40200  -13.91700 19.18200 1.000 22.12000  ? 231 ILE A CG1 1 
ATOM   1734 C  CG2 . ILE A  1 237 ? 45.18600  -11.73900 19.82500 1.000 20.59000  ? 231 ILE A CG2 1 
ATOM   1735 C  CD1 . ILE A  1 237 ? 45.75200  -14.85600 20.18000 1.000 25.35000  ? 231 ILE A CD1 1 
ATOM   1736 N  N   . PHE A  1 238 ? 48.14100  -9.77300  20.16600 1.000 23.62000  ? 232 PHE A N   1 
ATOM   1737 C  CA  . PHE A  1 238 ? 48.20900  -8.34600  20.46700 1.000 23.65000  ? 232 PHE A CA  1 
ATOM   1738 C  C   . PHE A  1 238 ? 48.84400  -7.58300  19.31400 1.000 25.56000  ? 232 PHE A C   1 
ATOM   1739 O  O   . PHE A  1 238 ? 48.27400  -6.59700  18.82500 1.000 23.72000  ? 232 PHE A O   1 
ATOM   1740 C  CB  . PHE A  1 238 ? 48.96100  -8.10000  21.77800 1.000 25.15000  ? 232 PHE A CB  1 
ATOM   1741 C  CG  . PHE A  1 238 ? 49.03900  -6.64300  22.17700 1.000 25.37000  ? 232 PHE A CG  1 
ATOM   1742 C  CD1 . PHE A  1 238 ? 49.90900  -5.76800  21.52500 1.000 26.20000  ? 232 PHE A CD1 1 
ATOM   1743 C  CD2 . PHE A  1 238 ? 48.25000  -6.15100  23.20800 1.000 24.99000  ? 232 PHE A CD2 1 
ATOM   1744 C  CE1 . PHE A  1 238 ? 49.98800  -4.44800  21.87400 1.000 26.48000  ? 232 PHE A CE1 1 
ATOM   1745 C  CE2 . PHE A  1 238 ? 48.31200  -4.81700  23.57500 1.000 25.31000  ? 232 PHE A CE2 1 
ATOM   1746 C  CZ  . PHE A  1 238 ? 49.18500  -3.95300  22.90400 1.000 25.99000  ? 232 PHE A CZ  1 
ATOM   1747 N  N   . ARG A  1 239 ? 50.03700  -8.01300  18.87600 1.000 25.73000  ? 233 ARG A N   1 
ATOM   1748 C  CA  . ARG A  1 239 ? 50.71700  -7.33300  17.77500 1.000 26.66000  ? 233 ARG A CA  1 
ATOM   1749 C  C   . ARG A  1 239 ? 49.84500  -7.27400  16.52400 1.000 27.74000  ? 233 ARG A C   1 
ATOM   1750 O  O   . ARG A  1 239 ? 49.81600  -6.25200  15.82100 1.000 28.14000  ? 233 ARG A O   1 
ATOM   1751 C  CB  . ARG A  1 239 ? 52.04000  -8.03100  17.45000 1.000 28.84000  ? 233 ARG A CB  1 
ATOM   1752 C  CG  . ARG A  1 239 ? 52.81800  -7.33200  16.31000 1.000 36.29000  ? 233 ARG A CG  1 
ATOM   1753 C  CD  . ARG A  1 239 ? 54.11500  -8.04100  15.87200 1.000 43.11000  ? 233 ARG A CD  1 
ATOM   1754 N  NE  . ARG A  1 239 ? 53.84500  -9.22200  15.05400 1.000 48.34000  ? 233 ARG A NE  1 
ATOM   1755 C  CZ  . ARG A  1 239 ? 54.76800  -10.00700 14.50600 1.000 54.17000  ? 233 ARG A CZ  1 
ATOM   1756 N  NH1 . ARG A  1 239 ? 56.06800  -9.77400  14.66200 1.000 63.44000  ? 233 ARG A NH1 1 
ATOM   1757 N  NH2 . ARG A  1 239 ? 54.38200  -11.05500 13.77600 1.000 48.65000  ? 233 ARG A NH2 1 
ATOM   1758 N  N   . ALA A  1 240 ? 49.13600  -8.36100  16.21900 1.000 26.29000  ? 234 ALA A N   1 
ATOM   1759 C  CA  . ALA A  1 240 ? 48.34600  -8.38400  14.99600 1.000 25.55000  ? 234 ALA A CA  1 
ATOM   1760 C  C   . ALA A  1 240 ? 47.20300  -7.38100  15.05800 1.000 25.31000  ? 234 ALA A C   1 
ATOM   1761 O  O   . ALA A  1 240 ? 46.94400  -6.66800  14.08200 1.000 25.94000  ? 234 ALA A O   1 
ATOM   1762 C  CB  . ALA A  1 240 ? 47.79500  -9.78700  14.73900 1.000 25.32000  ? 234 ALA A CB  1 
ATOM   1763 N  N   . MET A  1 241 ? 46.50500  -7.31900  16.19200 1.000 23.98000  ? 235 MET A N   1 
ATOM   1764 C  CA  . MET A  1 241 ? 45.41600  -6.36100  16.33100 1.000 22.90000  ? 235 MET A CA  1 
ATOM   1765 C  C   . MET A  1 241 ? 45.92200  -4.92000  16.20400 1.000 22.65000  ? 235 MET A C   1 
ATOM   1766 O  O   . MET A  1 241 ? 45.33800  -4.11100  15.47100 1.000 23.41000  ? 235 MET A O   1 
ATOM   1767 C  CB  . MET A  1 241 ? 44.69500  -6.57500  17.66500 1.000 20.46000  ? 235 MET A CB  1 
ATOM   1768 C  CG  . MET A  1 241 ? 43.89700  -7.86400  17.75900 1.000 18.75000  ? 235 MET A CG  1 
ATOM   1769 S  SD  . MET A  1 241 ? 43.19200  -8.07500  19.40500 1.000 23.31000  ? 235 MET A SD  1 
ATOM   1770 C  CE  . MET A  1 241 ? 41.80100  -6.91200  19.38500 1.000 17.56000  ? 235 MET A CE  1 
ATOM   1771 N  N   . ALA A  1 242 ? 47.03400  -4.59100  16.88300 1.000 21.86000  ? 236 ALA A N   1 
ATOM   1772 C  CA  . ALA A  1 242 ? 47.53100  -3.22000  16.87600 1.000 22.53000  ? 236 ALA A CA  1 
ATOM   1773 C  C   . ALA A  1 242 ? 48.17600  -2.85700  15.54300 1.000 25.17000  ? 236 ALA A C   1 
ATOM   1774 O  O   . ALA A  1 242 ? 48.15300  -1.69300  15.13600 1.000 24.74000  ? 236 ALA A O   1 
ATOM   1775 C  CB  . ALA A  1 242 ? 48.52300  -3.01800  18.01500 1.000 23.67000  ? 236 ALA A CB  1 
ATOM   1776 N  N   . ARG A  1 243 ? 48.72900  -3.82900  14.83700 1.000 26.91000  ? 237 ARG A N   1 
ATOM   1777 C  CA  A ARG A  1 243 ? 49.32100  -3.49400  13.55600 0.400 26.27000  ? 237 ARG A CA  1 
ATOM   1778 C  CA  B ARG A  1 243 ? 49.32900  -3.58100  13.53300 0.600 26.29000  ? 237 ARG A CA  1 
ATOM   1779 C  C   . ARG A  1 243 ? 48.27600  -3.37800  12.45300 1.000 25.52000  ? 237 ARG A C   1 
ATOM   1780 O  O   . ARG A  1 243 ? 48.47600  -2.59400  11.51900 1.000 26.56000  ? 237 ARG A O   1 
ATOM   1781 C  CB  A ARG A  1 243 ? 50.40900  -4.51200  13.20000 0.400 27.82000  ? 237 ARG A CB  1 
ATOM   1782 C  CB  B ARG A  1 243 ? 50.24900  -4.75400  13.15700 0.600 27.59000  ? 237 ARG A CB  1 
ATOM   1783 C  CG  A ARG A  1 243 ? 51.63400  -4.39900  14.11600 0.400 29.20000  ? 237 ARG A CG  1 
ATOM   1784 C  CG  B ARG A  1 243 ? 51.36200  -4.40900  12.19100 0.600 30.05000  ? 237 ARG A CG  1 
ATOM   1785 C  CD  A ARG A  1 243 ? 52.27500  -3.00900  14.02000 0.400 30.95000  ? 237 ARG A CD  1 
ATOM   1786 C  CD  B ARG A  1 243 ? 52.48800  -5.44700  12.20300 0.600 31.92000  ? 237 ARG A CD  1 
ATOM   1787 N  NE  A ARG A  1 243 ? 52.59400  -2.42900  15.32200 0.400 31.84000  ? 237 ARG A NE  1 
ATOM   1788 N  NE  B ARG A  1 243 ? 52.23400  -6.52600  11.25500 0.600 33.47000  ? 237 ARG A NE  1 
ATOM   1789 C  CZ  A ARG A  1 243 ? 52.08200  -1.29800  15.79500 0.400 32.94000  ? 237 ARG A CZ  1 
ATOM   1790 C  CZ  B ARG A  1 243 ? 52.43000  -6.42900  9.94900  0.600 35.21000  ? 237 ARG A CZ  1 
ATOM   1791 N  NH1 A ARG A  1 243 ? 51.20200  -0.59100  15.10700 0.400 30.84000  ? 237 ARG A NH1 1 
ATOM   1792 N  NH1 B ARG A  1 243 ? 52.94300  -5.33200  9.40500  0.600 37.73000  ? 237 ARG A NH1 1 
ATOM   1793 N  NH2 A ARG A  1 243 ? 52.48100  -0.85300  16.98100 0.400 35.13000  ? 237 ARG A NH2 1 
ATOM   1794 N  NH2 B ARG A  1 243 ? 52.09700  -7.45100  9.16700  0.600 34.24000  ? 237 ARG A NH2 1 
ATOM   1795 N  N   . HIS A  1 244 ? 47.14900  -4.08100  12.55400 1.000 24.89000  ? 238 HIS A N   1 
ATOM   1796 C  CA  . HIS A  1 244 ? 46.09800  -4.00300  11.54300 1.000 24.19000  ? 238 HIS A CA  1 
ATOM   1797 C  C   . HIS A  1 244 ? 44.76200  -3.66500  12.18300 1.000 25.20000  ? 238 HIS A C   1 
ATOM   1798 O  O   . HIS A  1 244 ? 43.79900  -4.42100  12.06100 1.000 20.45000  ? 238 HIS A O   1 
ATOM   1799 C  CB  . HIS A  1 244 ? 46.02200  -5.31200  10.76800 1.000 22.76000  ? 238 HIS A CB  1 
ATOM   1800 C  CG  . HIS A  1 244 ? 47.33500  -5.70800  10.17700 1.000 25.96000  ? 238 HIS A CG  1 
ATOM   1801 N  ND1 . HIS A  1 244 ? 47.80300  -5.18700  8.99000  1.000 28.24000  ? 238 HIS A ND1 1 
ATOM   1802 C  CD2 . HIS A  1 244 ? 48.29200  -6.55000  10.62300 1.000 27.61000  ? 238 HIS A CD2 1 
ATOM   1803 C  CE1 . HIS A  1 244 ? 48.98900  -5.70200  8.72400  1.000 30.17000  ? 238 HIS A CE1 1 
ATOM   1804 N  NE2 . HIS A  1 244 ? 49.30700  -6.54000  9.69500  1.000 29.55000  ? 238 HIS A NE2 1 
ATOM   1805 N  N   . PRO A  1 245 ? 44.66100  -2.52000  12.86700 1.000 21.58000  ? 239 PRO A N   1 
ATOM   1806 C  CA  . PRO A  1 245 ? 43.40600  -2.21700  13.56000 1.000 19.42000  ? 239 PRO A CA  1 
ATOM   1807 C  C   . PRO A  1 245 ? 42.25500  -2.00600  12.60300 1.000 24.09000  ? 239 PRO A C   1 
ATOM   1808 O  O   . PRO A  1 245 ? 41.09500  -2.07200  13.03300 1.000 19.60000  ? 239 PRO A O   1 
ATOM   1809 C  CB  . PRO A  1 245 ? 43.73700  -0.94200  14.34300 1.000 23.96000  ? 239 PRO A CB  1 
ATOM   1810 C  CG  . PRO A  1 245 ? 44.76600  -0.25100  13.48000 1.000 21.99000  ? 239 PRO A CG  1 
ATOM   1811 C  CD  . PRO A  1 245 ? 45.61700  -1.39600  12.94300 1.000 27.18000  ? 239 PRO A CD  1 
ATOM   1812 N  N   . GLU A  1 246 ? 42.53100  -1.78300  11.31700 1.000 20.97000  ? 240 GLU A N   1 
ATOM   1813 C  CA  . GLU A  1 246 ? 41.44700  -1.55900  10.32300 1.000 22.39000  ? 240 GLU A CA  1 
ATOM   1814 C  C   . GLU A  1 246 ? 40.77300  -2.89000  10.01900 1.000 22.58000  ? 240 GLU A C   1 
ATOM   1815 O  O   . GLU A  1 246 ? 39.61700  -2.87800  9.62400  1.000 20.06000  ? 240 GLU A O   1 
ATOM   1816 C  CB  . GLU A  1 246 ? 41.95700  -0.92700  9.03100  1.000 24.46000  ? 240 GLU A CB  1 
ATOM   1817 C  CG  . GLU A  1 246 ? 42.85000  -1.84400  8.23000  1.000 28.90000  ? 240 GLU A CG  1 
ATOM   1818 C  CD  . GLU A  1 246 ? 44.30700  -1.85600  8.65300  1.000 34.96000  ? 240 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A  1 246 ? 44.61500  -1.40000  9.76500  1.000 34.88000  ? 240 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A  1 246 ? 45.13100  -2.30400  7.85300  1.000 39.33000  ? 240 GLU A OE2 1 
ATOM   1821 N  N   . MET A  1 247 ? 41.51200  -3.98800  10.18600 1.000 22.81000  ? 241 MET A N   1 
ATOM   1822 C  CA  . MET A  1 247 ? 40.89900  -5.29500  10.02500 1.000 20.48000  ? 241 MET A CA  1 
ATOM   1823 C  C   . MET A  1 247 ? 40.01700  -5.62000  11.21700 1.000 22.04000  ? 241 MET A C   1 
ATOM   1824 O  O   . MET A  1 247 ? 39.01100  -6.31400  11.06900 1.000 21.08000  ? 241 MET A O   1 
ATOM   1825 C  CB  . MET A  1 247 ? 41.96000  -6.37400  9.85800  1.000 21.38000  ? 241 MET A CB  1 
ATOM   1826 C  CG  . MET A  1 247 ? 42.74700  -6.29800  8.54400  1.000 23.56000  ? 241 MET A CG  1 
ATOM   1827 S  SD  . MET A  1 247 ? 41.68700  -6.58300  7.10400  1.000 24.34000  ? 241 MET A SD  1 
ATOM   1828 C  CE  . MET A  1 247 ? 41.38100  -4.92600  6.48000  1.000 23.24000  ? 241 MET A CE  1 
ATOM   1829 N  N   . VAL A  1 248 ? 40.37400  -5.11700  12.39900 1.000 21.73000  ? 242 VAL A N   1 
ATOM   1830 C  CA  . VAL A  1 248 ? 39.61600  -5.43400  13.60300 1.000 18.51000  ? 242 VAL A CA  1 
ATOM   1831 C  C   . VAL A  1 248 ? 38.25800  -4.75500  13.59000 1.000 20.58000  ? 242 VAL A C   1 
ATOM   1832 O  O   . VAL A  1 248 ? 37.31800  -5.22900  14.24000 1.000 19.24000  ? 242 VAL A O   1 
ATOM   1833 C  CB  . VAL A  1 248 ? 40.46100  -5.06800  14.84400 1.000 18.18000  ? 242 VAL A CB  1 
ATOM   1834 C  CG1 . VAL A  1 248 ? 39.67700  -5.32800  16.11400 1.000 16.91000  ? 242 VAL A CG1 1 
ATOM   1835 C  CG2 . VAL A  1 248 ? 41.72900  -5.94300  14.86500 1.000 20.73000  ? 242 VAL A CG2 1 
ATOM   1836 N  N   . ALA A  1 249 ? 38.10300  -3.67800  12.82700 1.000 19.37000  ? 243 ALA A N   1 
ATOM   1837 C  CA  . ALA A  1 249 ? 36.80300  -3.02400  12.77000 1.000 20.49000  ? 243 ALA A CA  1 
ATOM   1838 C  C   . ALA A  1 249 ? 36.61600  -2.40600  11.39400 1.000 20.63000  ? 243 ALA A C   1 
ATOM   1839 O  O   . ALA A  1 249 ? 36.04800  -3.05400  10.50800 1.000 19.54000  ? 243 ALA A O   1 
ATOM   1840 C  CB  . ALA A  1 249 ? 36.67100  -1.99500  13.89800 1.000 17.67000  ? 243 ALA A CB  1 
ATOM   1841 N  N   . GLY A  1 250 ? 37.09900  -1.18700  11.18800 1.000 17.54000  ? 244 GLY A N   1 
ATOM   1842 C  CA  . GLY A  1 250 ? 36.99600  -0.58400  9.87200  1.000 19.87000  ? 244 GLY A CA  1 
ATOM   1843 C  C   . GLY A  1 250 ? 37.14100  0.92000   9.94800  1.000 19.30000  ? 244 GLY A C   1 
ATOM   1844 O  O   . GLY A  1 250 ? 37.41100  1.49300   11.01100 1.000 19.37000  ? 244 GLY A O   1 
ATOM   1845 N  N   . GLU A  1 251 ? 37.00700  1.54500   8.78200  1.000 19.89000  ? 245 GLU A N   1 
ATOM   1846 C  CA  . GLU A  1 251 ? 37.13800  2.99900   8.71300  1.000 23.36000  ? 245 GLU A CA  1 
ATOM   1847 C  C   . GLU A  1 251 ? 36.11100  3.65500   9.63400  1.000 20.91000  ? 245 GLU A C   1 
ATOM   1848 O  O   . GLU A  1 251 ? 34.94500  3.27500   9.64800  1.000 18.70000  ? 245 GLU A O   1 
ATOM   1849 C  CB  . GLU A  1 251 ? 36.95300  3.45900   7.26000  1.000 27.92000  ? 245 GLU A CB  1 
ATOM   1850 C  CG  . GLU A  1 251 ? 37.05300  4.96200   7.00400  1.000 32.44000  ? 245 GLU A CG  1 
ATOM   1851 C  CD  . GLU A  1 251 ? 38.50100  5.47500   7.03000  1.000 35.76000  ? 245 GLU A CD  1 
ATOM   1852 O  OE1 . GLU A  1 251 ? 39.44900  4.67600   6.78500  1.000 35.71000  ? 245 GLU A OE1 1 
ATOM   1853 O  OE2 . GLU A  1 251 ? 38.67100  6.69100   7.30400  1.000 45.93000  ? 245 GLU A OE2 1 
ATOM   1854 N  N   . GLY A  1 252 ? 36.54100  4.64900   10.40500 1.000 23.84000  ? 246 GLY A N   1 
ATOM   1855 C  CA  . GLY A  1 252 ? 35.62100  5.38500   11.25300 1.000 21.66000  ? 246 GLY A CA  1 
ATOM   1856 C  C   . GLY A  1 252 ? 35.19000  4.68200   12.52700 1.000 22.18000  ? 246 GLY A C   1 
ATOM   1857 O  O   . GLY A  1 252 ? 34.51800  5.31600   13.36000 1.000 18.17000  ? 246 GLY A O   1 
ATOM   1858 N  N   . ARG A  1 253 ? 35.55900  3.40800   12.71900 1.000 16.19000  ? 247 ARG A N   1 
ATOM   1859 C  CA  . ARG A  1 253 ? 35.07200  2.62800   13.85500 1.000 16.98000  ? 247 ARG A CA  1 
ATOM   1860 C  C   . ARG A  1 253 ? 35.89600  2.94500   15.10100 1.000 19.60000  ? 247 ARG A C   1 
ATOM   1861 O  O   . ARG A  1 253 ? 37.11200  3.13000   15.02600 1.000 17.49000  ? 247 ARG A O   1 
ATOM   1862 C  CB  . ARG A  1 253 ? 35.16800  1.11600   13.55700 1.000 18.21000  ? 247 ARG A CB  1 
ATOM   1863 C  CG  . ARG A  1 253 ? 34.24000  0.63200   12.44400 1.000 17.10000  ? 247 ARG A CG  1 
ATOM   1864 C  CD  . ARG A  1 253 ? 32.86200  0.31400   13.03300 1.000 17.56000  ? 247 ARG A CD  1 
ATOM   1865 N  NE  . ARG A  1 253 ? 32.93300  -0.65000  14.13600 1.000 18.36000  ? 247 ARG A NE  1 
ATOM   1866 C  CZ  . ARG A  1 253 ? 33.02400  -1.96600  13.99100 1.000 18.54000  ? 247 ARG A CZ  1 
ATOM   1867 N  NH1 . ARG A  1 253 ? 33.02600  -2.53300  12.78900 1.000 18.18000  ? 247 ARG A NH1 1 
ATOM   1868 N  NH2 . ARG A  1 253 ? 33.13900  -2.73700  15.07600 1.000 19.09000  ? 247 ARG A NH2 1 
ATOM   1869 N  N   . TYR A  1 254 ? 35.24000  2.92900   16.27000 1.000 18.28000  ? 248 TYR A N   1 
ATOM   1870 C  CA  . TYR A  1 254 ? 35.97700  3.24400   17.50100 1.000 17.23000  ? 248 TYR A CA  1 
ATOM   1871 C  C   . TYR A  1 254 ? 37.24000  2.40000   17.68000 1.000 19.76000  ? 248 TYR A C   1 
ATOM   1872 O  O   . TYR A  1 254 ? 38.29300  2.93500   18.04400 1.000 19.55000  ? 248 TYR A O   1 
ATOM   1873 C  CB  . TYR A  1 254 ? 35.09100  3.06200   18.72000 1.000 17.32000  ? 248 TYR A CB  1 
ATOM   1874 C  CG  . TYR A  1 254 ? 35.72200  3.56800   19.99400 1.000 16.08000  ? 248 TYR A CG  1 
ATOM   1875 C  CD1 . TYR A  1 254 ? 35.72700  4.93500   20.28800 1.000 19.13000  ? 248 TYR A CD1 1 
ATOM   1876 C  CD2 . TYR A  1 254 ? 36.30200  2.70200   20.90100 1.000 17.26000  ? 248 TYR A CD2 1 
ATOM   1877 C  CE1 . TYR A  1 254 ? 36.31400  5.42300   21.45700 1.000 17.74000  ? 248 TYR A CE1 1 
ATOM   1878 C  CE2 . TYR A  1 254 ? 36.87200  3.16300   22.09000 1.000 18.25000  ? 248 TYR A CE2 1 
ATOM   1879 C  CZ  . TYR A  1 254 ? 36.87500  4.54100   22.35200 1.000 18.64000  ? 248 TYR A CZ  1 
ATOM   1880 O  OH  . TYR A  1 254 ? 37.41400  4.99500   23.51600 1.000 16.24000  ? 248 TYR A OH  1 
ATOM   1881 N  N   . CYS A  1 255 ? 37.14400  1.06500   17.49800 1.000 18.29000  ? 249 CYS A N   1 
ATOM   1882 C  CA  . CYS A  1 255 ? 38.30900  0.20700   17.78300 1.000 19.77000  ? 249 CYS A CA  1 
ATOM   1883 C  C   . CYS A  1 255 ? 39.48300  0.58800   16.89700 1.000 23.68000  ? 249 CYS A C   1 
ATOM   1884 O  O   . CYS A  1 255 ? 40.64600  0.56600   17.33200 1.000 22.29000  ? 249 CYS A O   1 
ATOM   1885 C  CB  . CYS A  1 255 ? 37.98300  -1.27600  17.57300 1.000 18.06000  ? 249 CYS A CB  1 
ATOM   1886 S  SG  . CYS A  1 255 ? 36.48400  -1.89200  18.41300 1.000 23.13000  ? 249 CYS A SG  1 
ATOM   1887 N  N   . THR A  1 256 ? 39.19400  0.91700   15.64400 1.000 21.14000  ? 250 THR A N   1 
ATOM   1888 C  CA  . THR A  1 256 ? 40.26200  1.22300   14.69700 1.000 20.97000  ? 250 THR A CA  1 
ATOM   1889 C  C   . THR A  1 256 ? 40.89800  2.56700   15.02600 1.000 22.98000  ? 250 THR A C   1 
ATOM   1890 O  O   . THR A  1 256 ? 42.13500  2.69600   15.06900 1.000 22.39000  ? 250 THR A O   1 
ATOM   1891 C  CB  . THR A  1 256 ? 39.68700  1.19000   13.27600 1.000 19.63000  ? 250 THR A CB  1 
ATOM   1892 O  OG1 . THR A  1 256 ? 39.26500  -0.14700  12.99000 1.000 19.22000  ? 250 THR A OG1 1 
ATOM   1893 C  CG2 . THR A  1 256 ? 40.73000  1.61700   12.23800 1.000 20.33000  ? 250 THR A CG2 1 
ATOM   1894 N  N   . MET A  1 257 ? 40.06500  3.56500   15.32200 1.000 23.94000  ? 251 MET A N   1 
ATOM   1895 C  CA  . MET A  1 257 ? 40.59600  4.88100   15.63800 1.000 22.49000  ? 251 MET A CA  1 
ATOM   1896 C  C   . MET A  1 257 ? 41.30800  4.87300   16.97900 1.000 22.39000  ? 251 MET A C   1 
ATOM   1897 O  O   . MET A  1 257 ? 42.32300  5.55300   17.14100 1.000 22.87000  ? 251 MET A O   1 
ATOM   1898 C  CB  . MET A  1 257 ? 39.46500  5.91300   15.60200 1.000 24.67000  ? 251 MET A CB  1 
ATOM   1899 C  CG  . MET A  1 257 ? 38.79000  5.96800   14.23400 1.000 22.40000  ? 251 MET A CG  1 
ATOM   1900 S  SD  . MET A  1 257 ? 37.46900  7.20200   14.16200 1.000 26.59000  ? 251 MET A SD  1 
ATOM   1901 C  CE  . MET A  1 257 ? 38.31100  8.72000   14.68500 1.000 31.26000  ? 251 MET A CE  1 
ATOM   1902 N  N   . LEU A  1 258 ? 40.77700  4.13500   17.95600 1.000 18.93000  ? 252 LEU A N   1 
ATOM   1903 C  CA  . LEU A  1 258 ? 41.45200  3.98800   19.23700 1.000 21.12000  ? 252 LEU A CA  1 
ATOM   1904 C  C   . LEU A  1 258 ? 42.84400  3.40100   19.04500 1.000 23.71000  ? 252 LEU A C   1 
ATOM   1905 O  O   . LEU A  1 258 ? 43.84800  3.97700   19.48800 1.000 21.81000  ? 252 LEU A O   1 
ATOM   1906 C  CB  . LEU A  1 258 ? 40.62900  3.09600   20.17100 1.000 22.68000  ? 252 LEU A CB  1 
ATOM   1907 C  CG  . LEU A  1 258 ? 41.28900  2.69400   21.49800 1.000 21.39000  ? 252 LEU A CG  1 
ATOM   1908 C  CD1 . LEU A  1 258 ? 41.38500  3.91000   22.41000 1.000 23.09000  ? 252 LEU A CD1 1 
ATOM   1909 C  CD2 . LEU A  1 258 ? 40.47100  1.57800   22.15000 1.000 17.94000  ? 252 LEU A CD2 1 
ATOM   1910 N  N   . MET A  1 259 ? 42.92900  2.24900   18.37600 1.000 22.56000  ? 253 MET A N   1 
ATOM   1911 C  CA  . MET A  1 259 ? 44.23400  1.60400   18.27900 1.000 22.53000  ? 253 MET A CA  1 
ATOM   1912 C  C   . MET A  1 259 ? 45.18200  2.39300   17.38700 1.000 22.53000  ? 253 MET A C   1 
ATOM   1913 O  O   . MET A  1 259 ? 46.38200  2.45800   17.67000 1.000 24.27000  ? 253 MET A O   1 
ATOM   1914 C  CB  . MET A  1 259 ? 44.07700  0.16600   17.79200 1.000 21.84000  ? 253 MET A CB  1 
ATOM   1915 C  CG  . MET A  1 259 ? 43.56700  -0.75400  18.89900 1.000 22.08000  ? 253 MET A CG  1 
ATOM   1916 S  SD  . MET A  1 259 ? 43.52900  -2.49600  18.47100 1.000 21.48000  ? 253 MET A SD  1 
ATOM   1917 C  CE  . MET A  1 259 ? 42.15100  -2.52400  17.31500 1.000 22.69000  ? 253 MET A CE  1 
ATOM   1918 N  N   . ARG A  1 260 ? 44.67300  3.04000   16.34100 1.000 26.14000  ? 254 ARG A N   1 
ATOM   1919 C  CA  . ARG A  1 260 ? 45.56000  3.88300   15.54400 1.000 25.28000  ? 254 ARG A CA  1 
ATOM   1920 C  C   . ARG A  1 260 ? 46.10900  5.03700   16.36900 1.000 21.31000  ? 254 ARG A C   1 
ATOM   1921 O  O   . ARG A  1 260 ? 47.29100  5.38200   16.26000 1.000 27.65000  ? 254 ARG A O   1 
ATOM   1922 C  CB  . ARG A  1 260 ? 44.82600  4.39700   14.30800 1.000 28.97000  ? 254 ARG A CB  1 
ATOM   1923 C  CG  . ARG A  1 260 ? 45.12000  3.53100   13.11800 1.000 32.46000  ? 254 ARG A CG  1 
ATOM   1924 C  CD  . ARG A  1 260 ? 44.21100  3.75900   11.94400 1.000 36.15000  ? 254 ARG A CD  1 
ATOM   1925 N  NE  . ARG A  1 260 ? 44.46400  2.71300   10.96000 1.000 46.62000  ? 254 ARG A NE  1 
ATOM   1926 C  CZ  . ARG A  1 260 ? 43.73800  2.49700   9.87200  1.000 43.84000  ? 254 ARG A CZ  1 
ATOM   1927 N  NH1 . ARG A  1 260 ? 42.71500  3.28600   9.55100  1.000 39.57000  ? 254 ARG A NH1 1 
ATOM   1928 N  NH2 . ARG A  1 260 ? 44.04000  1.45700   9.09400  1.000 43.42000  ? 254 ARG A NH2 1 
ATOM   1929 N  N   . ALA A  1 261 ? 45.26900  5.63300   17.20100 1.000 23.02000  ? 255 ALA A N   1 
ATOM   1930 C  CA  . ALA A  1 261 ? 45.68000  6.74600   18.04000 1.000 25.06000  ? 255 ALA A CA  1 
ATOM   1931 C  C   . ALA A  1 261 ? 46.79600  6.32900   18.97700 1.000 26.56000  ? 255 ALA A C   1 
ATOM   1932 O  O   . ALA A  1 261 ? 47.76100  7.07200   19.18000 1.000 25.93000  ? 255 ALA A O   1 
ATOM   1933 C  CB  . ALA A  1 261 ? 44.47400  7.24300   18.83600 1.000 27.91000  ? 255 ALA A CB  1 
ATOM   1934 N  N   . PHE A  1 262 ? 46.69100  5.12800   19.54300 1.000 24.11000  ? 256 PHE A N   1 
ATOM   1935 C  CA  . PHE A  1 262 ? 47.65000  4.68600   20.54100 1.000 26.01000  ? 256 PHE A CA  1 
ATOM   1936 C  C   . PHE A  1 262 ? 48.86500  3.97600   19.94800 1.000 25.71000  ? 256 PHE A C   1 
ATOM   1937 O  O   . PHE A  1 262 ? 49.79800  3.65700   20.69800 1.000 25.30000  ? 256 PHE A O   1 
ATOM   1938 C  CB  . PHE A  1 262 ? 46.94500  3.80400   21.57400 1.000 23.39000  ? 256 PHE A CB  1 
ATOM   1939 C  CG  . PHE A  1 262 ? 46.25100  4.60400   22.62900 1.000 22.50000  ? 256 PHE A CG  1 
ATOM   1940 C  CD1 . PHE A  1 262 ? 46.92700  4.97700   23.77800 1.000 22.73000  ? 256 PHE A CD1 1 
ATOM   1941 C  CD2 . PHE A  1 262 ? 44.92600  4.99800   22.47000 1.000 25.32000  ? 256 PHE A CD2 1 
ATOM   1942 C  CE1 . PHE A  1 262 ? 46.30300  5.73600   24.75600 1.000 24.78000  ? 256 PHE A CE1 1 
ATOM   1943 C  CE2 . PHE A  1 262 ? 44.29600  5.77200   23.44400 1.000 24.81000  ? 256 PHE A CE2 1 
ATOM   1944 C  CZ  . PHE A  1 262 ? 44.98800  6.13400   24.59400 1.000 26.55000  ? 256 PHE A CZ  1 
ATOM   1945 N  N   . ASP A  1 263 ? 48.86300  3.73700   18.63600 1.000 26.36000  ? 257 ASP A N   1 
ATOM   1946 C  CA  . ASP A  1 263 ? 50.03800  3.33100   17.86400 1.000 25.22000  ? 257 ASP A CA  1 
ATOM   1947 C  C   . ASP A  1 263 ? 50.85700  2.24600   18.58000 1.000 29.93000  ? 257 ASP A C   1 
ATOM   1948 O  O   . ASP A  1 263 ? 52.08600  2.30400   18.66500 1.000 30.78000  ? 257 ASP A O   1 
ATOM   1949 C  CB  . ASP A  1 263 ? 50.89200  4.55400   17.53400 1.000 33.58000  ? 257 ASP A CB  1 
ATOM   1950 C  CG  . ASP A  1 263 ? 51.90200  4.28900   16.42400 1.000 37.93000  ? 257 ASP A CG  1 
ATOM   1951 O  OD1 . ASP A  1 263 ? 51.55900  3.55000   15.47600 1.000 40.55000  ? 257 ASP A OD1 1 
ATOM   1952 O  OD2 . ASP A  1 263 ? 53.03000  4.84400   16.49200 1.000 36.79000  ? 257 ASP A OD2 1 
ATOM   1953 N  N   . GLY A  1 264 ? 50.15100  1.24000   19.10500 1.000 26.96000  ? 258 GLY A N   1 
ATOM   1954 C  CA  . GLY A  1 264 ? 50.76000  0.07500   19.70700 1.000 27.75000  ? 258 GLY A CA  1 
ATOM   1955 C  C   . GLY A  1 264 ? 50.74200  0.02000   21.22400 1.000 28.86000  ? 258 GLY A C   1 
ATOM   1956 O  O   . GLY A  1 264 ? 51.09400  -1.02600  21.79000 1.000 25.50000  ? 258 GLY A O   1 
ATOM   1957 N  N   . ALA A  1 265 ? 50.36200  1.10600   21.90200 1.000 23.72000  ? 259 ALA A N   1 
ATOM   1958 C  CA  . ALA A  1 265 ? 50.36700  1.09600   23.36100 1.000 24.26000  ? 259 ALA A CA  1 
ATOM   1959 C  C   . ALA A  1 265 ? 49.22500  0.26300   23.95500 1.000 27.62000  ? 259 ALA A C   1 
ATOM   1960 O  O   . ALA A  1 265 ? 49.29800  -0.12400  25.12700 1.000 23.70000  ? 259 ALA A O   1 
ATOM   1961 C  CB  . ALA A  1 265 ? 50.29400  2.53000   23.88300 1.000 27.49000  ? 259 ALA A CB  1 
ATOM   1962 N  N   . LEU A  1 266 ? 48.18300  -0.03600  23.18100 1.000 24.47000  ? 260 LEU A N   1 
ATOM   1963 C  CA  . LEU A  1 266 ? 47.07200  -0.80800  23.70800 1.000 24.17000  ? 260 LEU A CA  1 
ATOM   1964 C  C   . LEU A  1 266 ? 46.35800  -1.46300  22.53800 1.000 23.79000  ? 260 LEU A C   1 
ATOM   1965 O  O   . LEU A  1 266 ? 46.58100  -1.10600  21.37700 1.000 23.94000  ? 260 LEU A O   1 
ATOM   1966 C  CB  . LEU A  1 266 ? 46.12100  0.07500   24.53900 1.000 22.67000  ? 260 LEU A CB  1 
ATOM   1967 C  CG  . LEU A  1 266 ? 45.52700  1.35400   23.93900 1.000 22.99000  ? 260 LEU A CG  1 
ATOM   1968 C  CD1 . LEU A  1 266 ? 44.37800  1.05900   22.99200 1.000 22.25000  ? 260 LEU A CD1 1 
ATOM   1969 C  CD2 . LEU A  1 266 ? 45.09800  2.27600   25.05700 1.000 21.18000  ? 260 LEU A CD2 1 
ATOM   1970 N  N   . VAL A  1 267 ? 45.52000  -2.44700  22.85700 1.000 21.56000  ? 261 VAL A N   1 
ATOM   1971 C  CA  . VAL A  1 267 ? 44.50400  -2.92600  21.93200 1.000 21.10000  ? 261 VAL A CA  1 
ATOM   1972 C  C   . VAL A  1 267 ? 43.16400  -2.74700  22.60500 1.000 21.07000  ? 261 VAL A C   1 
ATOM   1973 O  O   . VAL A  1 267 ? 43.06000  -2.75200  23.83500 1.000 20.45000  ? 261 VAL A O   1 
ATOM   1974 C  CB  . VAL A  1 267 ? 44.70300  -4.39200  21.50400 1.000 20.13000  ? 261 VAL A CB  1 
ATOM   1975 C  CG1 . VAL A  1 267 ? 46.05100  -4.52800  20.73400 1.000 20.72000  ? 261 VAL A CG1 1 
ATOM   1976 C  CG2 . VAL A  1 267 ? 44.70000  -5.32700  22.71700 1.000 19.50000  ? 261 VAL A CG2 1 
ATOM   1977 N  N   . GLY A  1 268 ? 42.13600  -2.58400  21.78800 1.000 22.36000  ? 262 GLY A N   1 
ATOM   1978 C  CA  . GLY A  1 268 ? 40.77600  -2.47100  22.28900 1.000 19.66000  ? 262 GLY A CA  1 
ATOM   1979 C  C   . GLY A  1 268 ? 39.82400  -3.19600  21.36200 1.000 18.08000  ? 262 GLY A C   1 
ATOM   1980 O  O   . GLY A  1 268 ? 40.08000  -3.34200  20.16800 1.000 21.27000  ? 262 GLY A O   1 
ATOM   1981 N  N   . LYS A  1 269 ? 38.75100  -3.71800  21.93700 1.000 16.67000  ? 263 LYS A N   1 
ATOM   1982 C  CA  . LYS A  1 269 ? 37.82200  -4.55900  21.17400 1.000 18.41000  ? 263 LYS A CA  1 
ATOM   1983 C  C   . LYS A  1 269 ? 36.39100  -4.38500  21.67100 1.000 16.74000  ? 263 LYS A C   1 
ATOM   1984 O  O   . LYS A  1 269 ? 36.14400  -4.45300  22.87800 1.000 16.00000  ? 263 LYS A O   1 
ATOM   1985 C  CB  . LYS A  1 269 ? 38.22500  -6.04000  21.27200 1.000 17.20000  ? 263 LYS A CB  1 
ATOM   1986 C  CG  . LYS A  1 269 ? 37.34300  -6.98100  20.49300 1.000 17.97000  ? 263 LYS A CG  1 
ATOM   1987 C  CD  . LYS A  1 269 ? 37.60200  -6.94700  18.99600 1.000 17.93000  ? 263 LYS A CD  1 
ATOM   1988 C  CE  . LYS A  1 269 ? 36.46400  -7.63400  18.24100 1.000 20.42000  ? 263 LYS A CE  1 
ATOM   1989 N  NZ  . LYS A  1 269 ? 35.22400  -6.76200  18.29000 1.000 20.01000  ? 263 LYS A NZ  1 
ATOM   1990 N  N   . LEU A  1 270 ? 35.46600  -4.17800  20.73200 1.000 15.61000  ? 264 LEU A N   1 
ATOM   1991 C  CA  . LEU A  1 270 ? 34.02800  -4.10500  21.02600 1.000 15.92000  ? 264 LEU A CA  1 
ATOM   1992 C  C   . LEU A  1 270 ? 33.39900  -5.48400  21.25900 1.000 17.12000  ? 264 LEU A C   1 
ATOM   1993 O  O   . LEU A  1 270 ? 33.69200  -6.44200  20.54800 1.000 17.68000  ? 264 LEU A O   1 
ATOM   1994 C  CB  . LEU A  1 270 ? 33.31000  -3.44600  19.85300 1.000 14.37000  ? 264 LEU A CB  1 
ATOM   1995 C  CG  . LEU A  1 270 ? 31.79400  -3.41700  19.85500 1.000 16.50000  ? 264 LEU A CG  1 
ATOM   1996 C  CD1 . LEU A  1 270 ? 31.31000  -2.45900  20.95400 1.000 16.02000  ? 264 LEU A CD1 1 
ATOM   1997 C  CD2 . LEU A  1 270 ? 31.32900  -2.93400  18.48500 1.000 15.55000  ? 264 LEU A CD2 1 
ATOM   1998 N  N   . GLY A  1 271 ? 32.46100  -5.54300  22.19900 1.000 18.90000  ? 265 GLY A N   1 
ATOM   1999 C  CA  . GLY A  1 271 ? 31.51100  -6.63000  22.30400 1.000 18.77000  ? 265 GLY A CA  1 
ATOM   2000 C  C   . GLY A  1 271 ? 30.10800  -6.10500  22.02800 1.000 17.24000  ? 265 GLY A C   1 
ATOM   2001 O  O   . GLY A  1 271 ? 29.70000  -5.06300  22.55600 1.000 17.85000  ? 265 GLY A O   1 
ATOM   2002 N  N   . ALA A  1 272 ? 29.39400  -6.83000  21.18400 1.000 18.34000  ? 266 ALA A N   1 
ATOM   2003 C  CA  . ALA A  1 272 ? 28.00400  -6.52400  20.91200 1.000 19.29000  ? 266 ALA A CA  1 
ATOM   2004 C  C   . ALA A  1 272 ? 27.22500  -6.35000  22.20500 1.000 19.83000  ? 266 ALA A C   1 
ATOM   2005 O  O   . ALA A  1 272 ? 27.51900  -6.98800  23.22100 1.000 16.71000  ? 266 ALA A O   1 
ATOM   2006 C  CB  . ALA A  1 272 ? 27.39100  -7.63300  20.06900 1.000 18.70000  ? 266 ALA A CB  1 
ATOM   2007 N  N   . ASP A  1 273 ? 26.20500  -5.48500  22.12300 1.000 21.55000  ? 267 ASP A N   1 
ATOM   2008 C  CA  . ASP A  1 273 ? 25.37300  -5.05300  23.24600 1.000 18.66000  ? 267 ASP A CA  1 
ATOM   2009 C  C   . ASP A  1 273 ? 26.19900  -4.31100  24.29300 1.000 19.03000  ? 267 ASP A C   1 
ATOM   2010 O  O   . ASP A  1 273 ? 25.90400  -4.36200  25.48700 1.000 16.40000  ? 267 ASP A O   1 
ATOM   2011 C  CB  . ASP A  1 273 ? 24.58000  -6.22800  23.82600 1.000 17.48000  ? 267 ASP A CB  1 
ATOM   2012 C  CG  . ASP A  1 273 ? 23.36100  -6.54900  22.97600 1.000 19.97000  ? 267 ASP A CG  1 
ATOM   2013 O  OD1 . ASP A  1 273 ? 22.53700  -5.61300  22.72700 1.000 19.32000  ? 267 ASP A OD1 1 
ATOM   2014 O  OD2 . ASP A  1 273 ? 23.24200  -7.68500  22.50400 1.000 23.64000  ? 267 ASP A OD2 1 
ATOM   2015 N  N   . ALA A  1 274 ? 27.21100  -3.58700  23.79800 1.000 16.07000  ? 268 ALA A N   1 
ATOM   2016 C  CA  . ALA A  1 274 ? 27.92700  -2.52400  24.51600 1.000 15.31000  ? 268 ALA A CA  1 
ATOM   2017 C  C   . ALA A  1 274 ? 28.80200  -3.03400  25.66200 1.000 17.53000  ? 268 ALA A C   1 
ATOM   2018 O  O   . ALA A  1 274 ? 28.72600  -2.55400  26.80300 1.000 17.86000  ? 268 ALA A O   1 
ATOM   2019 C  CB  . ALA A  1 274 ? 26.96200  -1.44500  25.00200 1.000 17.47000  ? 268 ALA A CB  1 
ATOM   2020 N  N   . SER A  1 275 ? 29.64300  -4.01200  25.36200 1.000 17.95000  ? 269 SER A N   1 
ATOM   2021 C  CA  A SER A  1 275 ? 30.79500  -4.32300  26.19400 0.700 18.23000  ? 269 SER A CA  1 
ATOM   2022 C  CA  B SER A  1 275 ? 30.78700  -4.28900  26.21100 0.300 18.16000  ? 269 SER A CA  1 
ATOM   2023 C  C   . SER A  1 275 ? 32.03500  -3.81900  25.47800 1.000 14.86000  ? 269 SER A C   1 
ATOM   2024 O  O   . SER A  1 275 ? 32.03200  -3.67300  24.26200 1.000 15.02000  ? 269 SER A O   1 
ATOM   2025 C  CB  A SER A  1 275 ? 30.92800  -5.82200  26.47000 0.700 15.79000  ? 269 SER A CB  1 
ATOM   2026 C  CB  B SER A  1 275 ? 30.88000  -5.77700  26.57700 0.300 15.94000  ? 269 SER A CB  1 
ATOM   2027 O  OG  A SER A  1 275 ? 29.97000  -6.21400  27.41300 0.700 16.99000  ? 269 SER A OG  1 
ATOM   2028 O  OG  B SER A  1 275 ? 30.85500  -6.59100  25.42400 0.300 14.86000  ? 269 SER A OG  1 
ATOM   2029 N  N   . TYR A  1 276 ? 33.09400  -3.51700  26.24400 1.000 18.93000  ? 270 TYR A N   1 
ATOM   2030 C  CA  . TYR A  1 276 ? 34.36300  -3.09700  25.65000 1.000 16.78000  ? 270 TYR A CA  1 
ATOM   2031 C  C   . TYR A  1 276 ? 35.50700  -3.65300  26.48900 1.000 17.16000  ? 270 TYR A C   1 
ATOM   2032 O  O   . TYR A  1 276 ? 35.38300  -3.75200  27.70900 1.000 17.30000  ? 270 TYR A O   1 
ATOM   2033 C  CB  . TYR A  1 276 ? 34.50400  -1.54500  25.52700 1.000 16.85000  ? 270 TYR A CB  1 
ATOM   2034 C  CG  . TYR A  1 276 ? 35.39000  -1.20800  24.34700 1.000 15.94000  ? 270 TYR A CG  1 
ATOM   2035 C  CD1 . TYR A  1 276 ? 34.87400  -1.26400  23.04700 1.000 13.48000  ? 270 TYR A CD1 1 
ATOM   2036 C  CD2 . TYR A  1 276 ? 36.76700  -0.93300  24.51300 1.000 17.28000  ? 270 TYR A CD2 1 
ATOM   2037 C  CE1 . TYR A  1 276 ? 35.67800  -1.06900  21.95500 1.000 16.00000  ? 270 TYR A CE1 1 
ATOM   2038 C  CE2 . TYR A  1 276 ? 37.58300  -0.71300  23.40900 1.000 17.45000  ? 270 TYR A CE2 1 
ATOM   2039 C  CZ  . TYR A  1 276 ? 37.02800  -0.78200  22.13700 1.000 18.36000  ? 270 TYR A CZ  1 
ATOM   2040 O  OH  . TYR A  1 276 ? 37.82000  -0.57200  21.02900 1.000 20.11000  ? 270 TYR A OH  1 
ATOM   2041 N  N   . ALA A  1 277 ? 36.61400  -4.04800  25.83700 1.000 14.51000  ? 271 ALA A N   1 
ATOM   2042 C  CA  . ALA A  1 277 ? 37.79600  -4.46000  26.58100 1.000 16.13000  ? 271 ALA A CA  1 
ATOM   2043 C  C   . ALA A  1 277 ? 39.03500  -3.78900  25.99600 1.000 17.37000  ? 271 ALA A C   1 
ATOM   2044 O  O   . ALA A  1 277 ? 39.15400  -3.66200  24.76900 1.000 17.11000  ? 271 ALA A O   1 
ATOM   2045 C  CB  . ALA A  1 277 ? 37.93200  -5.98300  26.57000 1.000 17.87000  ? 271 ALA A CB  1 
ATOM   2046 N  N   . ILE A  1 278 ? 39.95400  -3.35100  26.86900 1.000 19.00000  ? 272 ILE A N   1 
ATOM   2047 C  CA  . ILE A  1 278 ? 41.23200  -2.76200  26.45200 1.000 18.30000  ? 272 ILE A CA  1 
ATOM   2048 C  C   . ILE A  1 278 ? 42.37800  -3.46000  27.19200 1.000 19.18000  ? 272 ILE A C   1 
ATOM   2049 O  O   . ILE A  1 278 ? 42.29700  -3.68900  28.40200 1.000 20.29000  ? 272 ILE A O   1 
ATOM   2050 C  CB  . ILE A  1 278 ? 41.26100  -1.23700  26.70400 1.000 19.06000  ? 272 ILE A CB  1 
ATOM   2051 C  CG1 . ILE A  1 278 ? 40.21100  -0.55000  25.82900 1.000 20.13000  ? 272 ILE A CG1 1 
ATOM   2052 C  CG2 . ILE A  1 278 ? 42.67100  -0.64000  26.40700 1.000 19.26000  ? 272 ILE A CG2 1 
ATOM   2053 C  CD1 . ILE A  1 278 ? 40.01300  0.91000   26.16200 1.000 18.64000  ? 272 ILE A CD1 1 
ATOM   2054 N  N   . GLY A  1 279 ? 43.43300  -3.81600  26.46700 1.000 20.06000  ? 273 GLY A N   1 
ATOM   2055 C  CA  . GLY A  1 279 ? 44.64600  -4.31400  27.11000 1.000 21.98000  ? 273 GLY A CA  1 
ATOM   2056 C  C   . GLY A  1 279 ? 45.73000  -3.27400  26.94200 1.000 22.82000  ? 273 GLY A C   1 
ATOM   2057 O  O   . GLY A  1 279 ? 45.99000  -2.87600  25.80700 1.000 21.55000  ? 273 GLY A O   1 
ATOM   2058 N  N   . VAL A  1 280 ? 46.34100  -2.80200  28.03400 1.000 21.83000  ? 274 VAL A N   1 
ATOM   2059 C  CA  . VAL A  1 280 ? 47.25000  -1.65600  28.00900 1.000 20.17000  ? 274 VAL A CA  1 
ATOM   2060 C  C   . VAL A  1 280 ? 48.65400  -2.13200  28.37500 1.000 24.61000  ? 274 VAL A C   1 
ATOM   2061 O  O   . VAL A  1 280 ? 48.87900  -2.64300  29.47900 1.000 22.84000  ? 274 VAL A O   1 
ATOM   2062 C  CB  . VAL A  1 280 ? 46.79900  -0.53100  28.96400 1.000 23.64000  ? 274 VAL A CB  1 
ATOM   2063 C  CG1 . VAL A  1 280 ? 47.79200  0.66700   28.89100 1.000 21.02000  ? 274 VAL A CG1 1 
ATOM   2064 C  CG2 . VAL A  1 280 ? 45.36100  -0.06000  28.65300 1.000 21.33000  ? 274 VAL A CG2 1 
ATOM   2065 N  N   . ARG A  1 281 ? 49.60600  -1.93400  27.47200 1.000 22.67000  ? 275 ARG A N   1 
ATOM   2066 C  CA  . ARG A  1 281 ? 51.00000  -2.26700  27.78200 1.000 25.80000  ? 275 ARG A CA  1 
ATOM   2067 C  C   . ARG A  1 281 ? 51.53000  -1.38000  28.90500 1.000 23.84000  ? 275 ARG A C   1 
ATOM   2068 O  O   . ARG A  1 281 ? 51.07700  -0.24900  29.09400 1.000 26.33000  ? 275 ARG A O   1 
ATOM   2069 C  CB  . ARG A  1 281 ? 51.86800  -2.12900  26.53400 1.000 26.13000  ? 275 ARG A CB  1 
ATOM   2070 C  CG  . ARG A  1 281 ? 51.57300  -3.19200  25.48500 1.000 26.85000  ? 275 ARG A CG  1 
ATOM   2071 C  CD  . ARG A  1 281 ? 52.57400  -3.14800  24.34500 1.000 26.51000  ? 275 ARG A CD  1 
ATOM   2072 N  NE  . ARG A  1 281 ? 53.89500  -3.53800  24.82000 1.000 31.21000  ? 275 ARG A NE  1 
ATOM   2073 C  CZ  . ARG A  1 281 ? 54.98600  -3.52800  24.07500 1.000 34.54000  ? 275 ARG A CZ  1 
ATOM   2074 N  NH1 . ARG A  1 281 ? 54.93600  -3.24900  22.78300 1.000 32.64000  ? 275 ARG A NH1 1 
ATOM   2075 N  NH2 . ARG A  1 281 ? 56.15900  -3.77400  24.64700 1.000 36.18000  ? 275 ARG A NH2 1 
ATOM   2076 N  N   . ALA A  1 282 ? 52.47600  -1.91700  29.68100 1.000 29.34000  ? 276 ALA A N   1 
ATOM   2077 C  CA  . ALA A  1 282 ? 53.01700  -1.15300  30.79600 1.000 28.50000  ? 276 ALA A CA  1 
ATOM   2078 C  C   . ALA A  1 282 ? 53.59400  0.15800   30.29000 1.000 31.86000  ? 276 ALA A C   1 
ATOM   2079 O  O   . ALA A  1 282 ? 54.30000  0.19300   29.27900 1.000 30.72000  ? 276 ALA A O   1 
ATOM   2080 C  CB  . ALA A  1 282 ? 54.09300  -1.94700  31.53500 1.000 25.73000  ? 276 ALA A CB  1 
ATOM   2081 N  N   . SER A  1 283 ? 53.30000  1.23700   31.01000 1.000 27.02000  ? 277 SER A N   1 
ATOM   2082 C  CA  . SER A  1 283 ? 53.69700  2.57400   30.59700 1.000 30.82000  ? 277 SER A CA  1 
ATOM   2083 C  C   . SER A  1 283 ? 53.84900  3.43900   31.83700 1.000 30.00000  ? 277 SER A C   1 
ATOM   2084 O  O   . SER A  1 283 ? 53.59100  2.99200   32.95600 1.000 30.74000  ? 277 SER A O   1 
ATOM   2085 C  CB  . SER A  1 283 ? 52.64700  3.18400   29.67300 1.000 31.23000  ? 277 SER A CB  1 
ATOM   2086 O  OG  . SER A  1 283 ? 51.48100  3.44000   30.43900 1.000 28.21000  ? 277 SER A OG  1 
ATOM   2087 N  N   . ASP A  1 284 ? 54.24100  4.70200   31.62800 1.000 30.69000  ? 278 ASP A N   1 
ATOM   2088 C  CA  . ASP A  1 284 ? 54.24600  5.64500   32.73900 1.000 30.58000  ? 278 ASP A CA  1 
ATOM   2089 C  C   . ASP A  1 284 ? 52.84900  5.76300   33.34000 1.000 29.27000  ? 278 ASP A C   1 
ATOM   2090 O  O   . ASP A  1 284 ? 52.70100  5.95500   34.55200 1.000 29.82000  ? 278 ASP A O   1 
ATOM   2091 C  CB  . ASP A  1 284 ? 54.73100  7.03100   32.28800 1.000 28.90000  ? 278 ASP A CB  1 
ATOM   2092 C  CG  . ASP A  1 284 ? 56.21900  7.09500   31.96200 1.000 36.43000  ? 278 ASP A CG  1 
ATOM   2093 O  OD1 . ASP A  1 284 ? 56.99400  6.16200   32.27700 1.000 33.19000  ? 278 ASP A OD1 1 
ATOM   2094 O  OD2 . ASP A  1 284 ? 56.60300  8.13000   31.37500 1.000 34.95000  ? 278 ASP A OD2 1 
ATOM   2095 N  N   . ALA A  1 285 ? 51.81500  5.62100   32.51100 1.000 28.81000  ? 279 ALA A N   1 
ATOM   2096 C  CA  . ALA A  1 285 ? 50.44500  5.75600   32.99300 1.000 26.43000  ? 279 ALA A CA  1 
ATOM   2097 C  C   . ALA A  1 285 ? 50.05800  4.58500   33.89700 1.000 29.17000  ? 279 ALA A C   1 
ATOM   2098 O  O   . ALA A  1 285 ? 49.48200  4.78000   34.97300 1.000 30.59000  ? 279 ALA A O   1 
ATOM   2099 C  CB  . ALA A  1 285 ? 49.49600  5.85400   31.79900 1.000 22.70000  ? 279 ALA A CB  1 
ATOM   2100 N  N   . THR A  1 286 ? 50.35500  3.35900   33.47100 1.000 26.02000  ? 280 THR A N   1 
ATOM   2101 C  CA  . THR A  1 286 ? 50.03400  2.19800   34.29700 1.000 24.86000  ? 280 THR A CA  1 
ATOM   2102 C  C   . THR A  1 286 ? 50.81300  2.23700   35.60400 1.000 28.83000  ? 280 THR A C   1 
ATOM   2103 O  O   . THR A  1 286 ? 50.28300  1.89700   36.67000 1.000 25.26000  ? 280 THR A O   1 
ATOM   2104 C  CB  . THR A  1 286 ? 50.30100  0.90100   33.52000 1.000 27.90000  ? 280 THR A CB  1 
ATOM   2105 O  OG1 . THR A  1 286 ? 51.69100  0.75700   33.21300 1.000 27.30000  ? 280 THR A OG1 1 
ATOM   2106 C  CG2 . THR A  1 286 ? 49.48100  0.86700   32.20900 1.000 30.16000  ? 280 THR A CG2 1 
ATOM   2107 N  N   . ARG A  1 287 ? 52.07500  2.67700   35.54300 1.000 29.17000  ? 281 ARG A N   1 
ATOM   2108 C  CA  . ARG A  1 287 ? 52.88300  2.76800   36.75400 1.000 27.73000  ? 281 ARG A CA  1 
ATOM   2109 C  C   . ARG A  1 287 ? 52.29200  3.77900   37.72500 1.000 31.06000  ? 281 ARG A C   1 
ATOM   2110 O  O   . ARG A  1 287 ? 52.25800  3.54200   38.94000 1.000 30.38000  ? 281 ARG A O   1 
ATOM   2111 C  CB  . ARG A  1 287 ? 54.32300  3.13700   36.38900 1.000 28.50000  ? 281 ARG A CB  1 
ATOM   2112 C  CG  . ARG A  1 287 ? 55.08400  1.97500   35.75800 1.000 29.40000  ? 281 ARG A CG  1 
ATOM   2113 C  CD  . ARG A  1 287 ? 56.61200  2.25900   35.53600 1.000 30.38000  ? 281 ARG A CD  1 
ATOM   2114 N  NE  . ARG A  1 287 ? 56.86700  3.00700   34.30800 1.000 30.29000  ? 281 ARG A NE  1 
ATOM   2115 C  CZ  . ARG A  1 287 ? 56.85600  2.46500   33.09500 1.000 33.08000  ? 281 ARG A CZ  1 
ATOM   2116 N  NH1 . ARG A  1 287 ? 56.68900  1.16300   32.92500 1.000 29.17000  ? 281 ARG A NH1 1 
ATOM   2117 N  NH2 . ARG A  1 287 ? 56.99500  3.25000   32.02200 1.000 29.62000  ? 281 ARG A NH2 1 
ATOM   2118 N  N   . GLN A  1 288 ? 51.81200  4.90800   37.20200 1.000 26.89000  ? 282 GLN A N   1 
ATOM   2119 C  CA  . GLN A  1 288 ? 51.19000  5.92100   38.05000 1.000 32.74000  ? 282 GLN A CA  1 
ATOM   2120 C  C   . GLN A  1 288 ? 49.90900  5.41000   38.68400 1.000 30.52000  ? 282 GLN A C   1 
ATOM   2121 O  O   . GLN A  1 288 ? 49.56100  5.81700   39.79900 1.000 32.40000  ? 282 GLN A O   1 
ATOM   2122 C  CB  . GLN A  1 288 ? 50.90000  7.17000   37.23600 1.000 33.72000  ? 282 GLN A CB  1 
ATOM   2123 C  CG  . GLN A  1 288 ? 50.29300  8.29000   38.02800 1.000 47.20000  ? 282 GLN A CG  1 
ATOM   2124 C  CD  . GLN A  1 288 ? 50.17300  9.53600   37.19400 1.000 55.25000  ? 282 GLN A CD  1 
ATOM   2125 O  OE1 . GLN A  1 288 ? 51.16200  9.99300   36.61200 1.000 60.32000  ? 282 GLN A OE1 1 
ATOM   2126 N  NE2 . GLN A  1 288 ? 48.95800  10.08300  37.10300 1.000 56.35000  ? 282 GLN A NE2 1 
ATOM   2127 N  N   . LEU A  1 289 ? 49.21700  4.50500   38.00400 1.000 26.82000  ? 283 LEU A N   1 
ATOM   2128 C  CA  . LEU A  1 289 ? 48.00100  3.88500   38.51500 1.000 30.63000  ? 283 LEU A CA  1 
ATOM   2129 C  C   . LEU A  1 289 ? 48.28200  2.82900   39.57800 1.000 31.92000  ? 283 LEU A C   1 
ATOM   2130 O  O   . LEU A  1 289 ? 47.33400  2.27200   40.14100 1.000 30.00000  ? 283 LEU A O   1 
ATOM   2131 C  CB  . LEU A  1 289 ? 47.21600  3.25800   37.36200 1.000 27.70000  ? 283 LEU A CB  1 
ATOM   2132 C  CG  . LEU A  1 289 ? 46.59000  4.23600   36.36600 1.000 25.04000  ? 283 LEU A CG  1 
ATOM   2133 C  CD1 . LEU A  1 289 ? 46.08300  3.49300   35.13900 1.000 23.85000  ? 283 LEU A CD1 1 
ATOM   2134 C  CD2 . LEU A  1 289 ? 45.44700  4.95500   37.03800 1.000 23.58000  ? 283 LEU A CD2 1 
ATOM   2135 N  N   . GLY A  1 290 ? 49.54500  2.52000   39.84000 1.000 28.95000  ? 284 GLY A N   1 
ATOM   2136 C  CA  . GLY A  1 290 ? 49.91200  1.66800   40.95300 1.000 35.80000  ? 284 GLY A CA  1 
ATOM   2137 C  C   . GLY A  1 290 ? 50.27100  0.22700   40.64400 1.000 34.68000  ? 284 GLY A C   1 
ATOM   2138 O  O   . GLY A  1 290 ? 50.35100  -0.57500  41.57600 1.000 38.35000  ? 284 GLY A O   1 
ATOM   2139 N  N   . THR A  1 291 ? 50.49600  -0.13100  39.38400 1.000 31.81000  ? 285 THR A N   1 
ATOM   2140 C  CA  . THR A  1 291 ? 50.85200  -1.49500  39.03300 1.000 31.21000  ? 285 THR A CA  1 
ATOM   2141 C  C   . THR A  1 291 ? 52.18100  -1.51200  38.27800 1.000 33.13000  ? 285 THR A C   1 
ATOM   2142 O  O   . THR A  1 291 ? 52.51100  -0.57500  37.54000 1.000 28.70000  ? 285 THR A O   1 
ATOM   2143 C  CB  . THR A  1 291 ? 49.74800  -2.15000  38.20900 1.000 31.50000  ? 285 THR A CB  1 
ATOM   2144 O  OG1 . THR A  1 291 ? 50.11300  -3.50000  37.90600 1.000 34.29000  ? 285 THR A OG1 1 
ATOM   2145 C  CG2 . THR A  1 291 ? 49.51900  -1.36400  36.93500 1.000 28.00000  ? 285 THR A CG2 1 
ATOM   2146 N  N   . ASP A  1 292 ? 52.95600  -2.57700  38.48700 1.000 28.85000  ? 286 ASP A N   1 
ATOM   2147 C  CA  . ASP A  1 292 ? 54.26100  -2.69500  37.85300 1.000 30.87000  ? 286 ASP A CA  1 
ATOM   2148 C  C   . ASP A  1 292 ? 54.19400  -3.37200  36.48900 1.000 28.84000  ? 286 ASP A C   1 
ATOM   2149 O  O   . ASP A  1 292 ? 55.23800  -3.54200  35.84600 1.000 35.65000  ? 286 ASP A O   1 
ATOM   2150 C  CB  . ASP A  1 292 ? 55.25200  -3.43500  38.78200 1.000 32.40000  ? 286 ASP A CB  1 
ATOM   2151 C  CG  . ASP A  1 292 ? 54.76400  -4.84700  39.20200 1.000 41.80000  ? 286 ASP A CG  1 
ATOM   2152 O  OD1 . ASP A  1 292 ? 53.69700  -5.30600  38.72500 1.000 44.43000  ? 286 ASP A OD1 1 
ATOM   2153 O  OD2 . ASP A  1 292 ? 55.45600  -5.49800  40.03000 1.000 47.58000  ? 286 ASP A OD2 1 
ATOM   2154 N  N   . GLY A  1 293 ? 53.00500  -3.76200  36.03300 1.000 29.33000  ? 287 GLY A N   1 
ATOM   2155 C  CA  . GLY A  1 293 ? 52.89600  -4.45900  34.76700 1.000 29.10000  ? 287 GLY A CA  1 
ATOM   2156 C  C   . GLY A  1 293 ? 51.81900  -3.90600  33.85000 1.000 25.30000  ? 287 GLY A C   1 
ATOM   2157 O  O   . GLY A  1 293 ? 51.45000  -2.72500  33.93700 1.000 26.75000  ? 287 GLY A O   1 
ATOM   2158 N  N   . ALA A  1 294 ? 51.29500  -4.76100  32.97300 1.000 23.59000  ? 288 ALA A N   1 
ATOM   2159 C  CA  . ALA A  1 294 ? 50.24100  -4.35300  32.05800 1.000 22.37000  ? 288 ALA A CA  1 
ATOM   2160 C  C   . ALA A  1 294 ? 48.90600  -4.25700  32.79800 1.000 23.88000  ? 288 ALA A C   1 
ATOM   2161 O  O   . ALA A  1 294 ? 48.76300  -4.69300  33.94600 1.000 23.68000  ? 288 ALA A O   1 
ATOM   2162 C  CB  . ALA A  1 294 ? 50.17300  -5.32400  30.88600 1.000 23.56000  ? 288 ALA A CB  1 
ATOM   2163 N  N   . LEU A  1 295 ? 47.92000  -3.67900  32.12300 1.000 22.55000  ? 289 LEU A N   1 
ATOM   2164 C  CA  . LEU A  1 295 ? 46.63900  -3.34900  32.72500 1.000 22.12000  ? 289 LEU A CA  1 
ATOM   2165 C  C   . LEU A  1 295 ? 45.53300  -3.79900  31.78300 1.000 22.93000  ? 289 LEU A C   1 
ATOM   2166 O  O   . LEU A  1 295 ? 45.70300  -3.77500  30.56100 1.000 22.72000  ? 289 LEU A O   1 
ATOM   2167 C  CB  . LEU A  1 295 ? 46.60000  -1.83700  32.96300 1.000 28.89000  ? 289 LEU A CB  1 
ATOM   2168 C  CG  . LEU A  1 295 ? 45.44000  -1.05700  33.53100 1.000 31.56000  ? 289 LEU A CG  1 
ATOM   2169 C  CD1 . LEU A  1 295 ? 46.07200  -0.21100  34.59600 1.000 33.53000  ? 289 LEU A CD1 1 
ATOM   2170 C  CD2 . LEU A  1 295 ? 44.90800  -0.18900  32.42600 1.000 29.47000  ? 289 LEU A CD2 1 
ATOM   2171 N  N   . GLY A  1 296 ? 44.40900  -4.23100  32.34700 1.000 22.30000  ? 290 GLY A N   1 
ATOM   2172 C  CA  . GLY A  1 296 ? 43.21100  -4.53300  31.56600 1.000 24.09000  ? 290 GLY A CA  1 
ATOM   2173 C  C   . GLY A  1 296 ? 42.02000  -3.69500  31.99900 1.000 20.87000  ? 290 GLY A C   1 
ATOM   2174 O  O   . GLY A  1 296 ? 41.84800  -3.42300  33.19200 1.000 21.60000  ? 290 GLY A O   1 
ATOM   2175 N  N   . ILE A  1 297 ? 41.19800  -3.28300  31.02300 1.000 17.76000  ? 291 ILE A N   1 
ATOM   2176 C  CA  . ILE A  1 297 ? 39.97500  -2.51200  31.26300 1.000 17.99000  ? 291 ILE A CA  1 
ATOM   2177 C  C   . ILE A  1 297 ? 38.81500  -3.22000  30.59000 1.000 19.40000  ? 291 ILE A C   1 
ATOM   2178 O  O   . ILE A  1 297 ? 38.91600  -3.58200  29.41400 1.000 17.54000  ? 291 ILE A O   1 
ATOM   2179 C  CB  . ILE A  1 297 ? 40.06700  -1.06100  30.71800 1.000 17.03000  ? 291 ILE A CB  1 
ATOM   2180 C  CG1 . ILE A  1 297 ? 41.26400  -0.32000  31.32600 1.000 16.74000  ? 291 ILE A CG1 1 
ATOM   2181 C  CG2 . ILE A  1 297 ? 38.71500  -0.30800  30.93400 1.000 15.57000  ? 291 ILE A CG2 1 
ATOM   2182 C  CD1 . ILE A  1 297 ? 41.71000  0.87000   30.48900 1.000 21.29000  ? 291 ILE A CD1 1 
ATOM   2183 N  N   . SER A  1 298 ? 37.70900  -3.40700  31.32300 1.000 17.87000  ? 292 SER A N   1 
ATOM   2184 C  CA  . SER A  1 298 ? 36.48600  -3.93300  30.71700 1.000 15.68000  ? 292 SER A CA  1 
ATOM   2185 C  C   . SER A  1 298 ? 35.30100  -3.11900  31.20500 1.000 18.69000  ? 292 SER A C   1 
ATOM   2186 O  O   . SER A  1 298 ? 35.29600  -2.62200  32.33500 1.000 16.48000  ? 292 SER A O   1 
ATOM   2187 C  CB  . SER A  1 298 ? 36.26100  -5.42300  31.01300 1.000 17.02000  ? 292 SER A CB  1 
ATOM   2188 O  OG  . SER A  1 298 ? 36.30500  -5.70200  32.39900 1.000 16.53000  ? 292 SER A OG  1 
ATOM   2189 N  N   . VAL A  1 299 ? 34.33600  -2.92700  30.30800 1.000 18.25000  ? 293 VAL A N   1 
ATOM   2190 C  CA  . VAL A  1 299 ? 33.24300  -1.97300  30.50200 1.000 17.25000  ? 293 VAL A CA  1 
ATOM   2191 C  C   . VAL A  1 299 ? 31.97400  -2.61400  29.94900 1.000 16.41000  ? 293 VAL A C   1 
ATOM   2192 O  O   . VAL A  1 299 ? 32.00900  -3.26200  28.89500 1.000 15.36000  ? 293 VAL A O   1 
ATOM   2193 C  CB  . VAL A  1 299 ? 33.49700  -0.61000  29.80400 1.000 14.15000  ? 293 VAL A CB  1 
ATOM   2194 C  CG1 . VAL A  1 299 ? 32.27000  0.33000   29.99800 1.000 15.43000  ? 293 VAL A CG1 1 
ATOM   2195 C  CG2 . VAL A  1 299 ? 34.72200  0.08700   30.36800 1.000 17.51000  ? 293 VAL A CG2 1 
ATOM   2196 N  N   . LYS A  1 300 ? 30.86400  -2.45800  30.66700 1.000 13.18000  ? 294 LYS A N   1 
ATOM   2197 C  CA  . LYS A  1 300 ? 29.54900  -2.85700  30.13700 1.000 13.10000  ? 294 LYS A CA  1 
ATOM   2198 C  C   . LYS A  1 300 ? 28.55300  -1.74200  30.44100 1.000 19.15000  ? 294 LYS A C   1 
ATOM   2199 O  O   . LYS A  1 300 ? 28.49300  -1.26700  31.58200 1.000 17.54000  ? 294 LYS A O   1 
ATOM   2200 C  CB  . LYS A  1 300 ? 29.10200  -4.20900  30.75500 1.000 15.68000  ? 294 LYS A CB  1 
ATOM   2201 C  CG  . LYS A  1 300 ? 27.59800  -4.57400  30.59300 1.000 14.83000  ? 294 LYS A CG  1 
ATOM   2202 C  CD  . LYS A  1 300 ? 27.16900  -4.81700  29.15700 1.000 17.17000  ? 294 LYS A CD  1 
ATOM   2203 C  CE  . LYS A  1 300 ? 25.62900  -5.13300  29.14100 1.000 17.61000  ? 294 LYS A CE  1 
ATOM   2204 N  NZ  . LYS A  1 300 ? 25.17100  -5.60200  27.80200 1.000 21.80000  ? 294 LYS A NZ  1 
ATOM   2205 N  N   . ILE A  1 301 ? 27.83000  -1.26900  29.41600 1.000 16.64000  ? 295 ILE A N   1 
ATOM   2206 C  CA  . ILE A  1 301 ? 26.66300  -0.40800  29.62100 1.000 13.99000  ? 295 ILE A CA  1 
ATOM   2207 C  C   . ILE A  1 301 ? 25.46600  -1.32900  29.83800 1.000 17.78000  ? 295 ILE A C   1 
ATOM   2208 O  O   . ILE A  1 301 ? 25.18000  -2.18900  28.99100 1.000 14.12000  ? 295 ILE A O   1 
ATOM   2209 C  CB  . ILE A  1 301 ? 26.43400  0.54400   28.43200 1.000 19.00000  ? 295 ILE A CB  1 
ATOM   2210 C  CG1 . ILE A  1 301 ? 27.68600  1.38300   28.14000 1.000 16.25000  ? 295 ILE A CG1 1 
ATOM   2211 C  CG2 . ILE A  1 301 ? 25.25700  1.51600   28.70900 1.000 12.77000  ? 295 ILE A CG2 1 
ATOM   2212 C  CD1 . ILE A  1 301 ? 28.24600  2.13600   29.34500 1.000 19.26000  ? 295 ILE A CD1 1 
ATOM   2213 N  N   . GLU A  1 302 ? 24.81000  -1.19200  31.00100 1.000 15.92000  ? 296 GLU A N   1 
ATOM   2214 C  CA  . GLU A  1 302 ? 23.77100  -2.14200  31.42000 1.000 15.93000  ? 296 GLU A CA  1 
ATOM   2215 C  C   . GLU A  1 302 ? 22.67700  -2.31400  30.37900 1.000 17.72000  ? 296 GLU A C   1 
ATOM   2216 O  O   . GLU A  1 302 ? 22.17800  -3.43000  30.16600 1.000 15.52000  ? 296 GLU A O   1 
ATOM   2217 C  CB  . GLU A  1 302 ? 23.14600  -1.68800  32.73400 1.000 16.35000  ? 296 GLU A CB  1 
ATOM   2218 C  CG  . GLU A  1 302 ? 22.13400  -2.68500  33.29300 1.000 14.96000  ? 296 GLU A CG  1 
ATOM   2219 C  CD  . GLU A  1 302 ? 22.75400  -4.06700  33.55400 1.000 19.41000  ? 296 GLU A CD  1 
ATOM   2220 O  OE1 . GLU A  1 302 ? 23.89600  -4.14300  34.07700 1.000 17.19000  ? 296 GLU A OE1 1 
ATOM   2221 O  OE2 . GLU A  1 302 ? 22.10500  -5.08100  33.21500 1.000 18.31000  ? 296 GLU A OE2 1 
ATOM   2222 N  N   . ASP A  1 303 ? 22.28800  -1.22900  29.73000 1.000 15.92000  ? 297 ASP A N   1 
ATOM   2223 C  CA  . ASP A  1 303 ? 21.17800  -1.25000  28.78900 1.000 16.49000  ? 297 ASP A CA  1 
ATOM   2224 C  C   . ASP A  1 303 ? 21.62000  -1.45800  27.34600 1.000 18.66000  ? 297 ASP A C   1 
ATOM   2225 O  O   . ASP A  1 303 ? 20.76200  -1.53100  26.45500 1.000 17.45000  ? 297 ASP A O   1 
ATOM   2226 C  CB  . ASP A  1 303 ? 20.40700  0.06400   28.87800 1.000 16.51000  ? 297 ASP A CB  1 
ATOM   2227 C  CG  . ASP A  1 303 ? 21.33800  1.24800   28.69600 1.000 16.57000  ? 297 ASP A CG  1 
ATOM   2228 O  OD1 . ASP A  1 303 ? 21.58500  1.66000   27.53200 1.000 17.54000  ? 297 ASP A OD1 1 
ATOM   2229 O  OD2 . ASP A  1 303 ? 21.89500  1.68700   29.71400 1.000 15.02000  ? 297 ASP A OD2 1 
ATOM   2230 N  N   . GLY A  1 304 ? 22.92600  -1.51600  27.08100 1.000 15.75000  ? 298 GLY A N   1 
ATOM   2231 C  CA  . GLY A  1 304 ? 23.36200  -1.94000  25.76800 1.000 17.19000  ? 298 GLY A CA  1 
ATOM   2232 C  C   . GLY A  1 304 ? 23.61800  -0.82900  24.78000 1.000 18.86000  ? 298 GLY A C   1 
ATOM   2233 O  O   . GLY A  1 304 ? 23.75400  -1.10800  23.57900 1.000 19.01000  ? 298 GLY A O   1 
ATOM   2234 N  N   . ASN A  1 305 ? 23.69600  0.41400   25.23200 1.000 16.78000  ? 299 ASN A N   1 
ATOM   2235 C  CA  . ASN A  1 305 ? 23.81500  1.53400   24.30600 1.000 17.84000  ? 299 ASN A CA  1 
ATOM   2236 C  C   . ASN A  1 305 ? 25.27900  1.70100   23.88500 1.000 16.90000  ? 299 ASN A C   1 
ATOM   2237 O  O   . ASN A  1 305 ? 26.14700  1.93900   24.73400 1.000 17.67000  ? 299 ASN A O   1 
ATOM   2238 C  CB  . ASN A  1 305 ? 23.29800  2.80600   24.97000 1.000 17.38000  ? 299 ASN A CB  1 
ATOM   2239 C  CG  . ASN A  1 305 ? 23.17700  3.94000   24.00600 1.000 18.88000  ? 299 ASN A CG  1 
ATOM   2240 O  OD1 . ASN A  1 305 ? 24.16800  4.44300   23.52600 1.000 16.69000  ? 299 ASN A OD1 1 
ATOM   2241 N  ND2 . ASN A  1 305 ? 21.94300  4.37200   23.73500 1.000 20.09000  ? 299 ASN A ND2 1 
ATOM   2242 N  N   . LEU A  1 306 ? 25.54700  1.59600   22.57800 1.000 13.86000  ? 300 LEU A N   1 
ATOM   2243 C  CA  . LEU A  1 306 ? 26.92900  1.68500   22.08400 1.000 16.40000  ? 300 LEU A CA  1 
ATOM   2244 C  C   . LEU A  1 306 ? 27.46600  3.11600   22.13800 1.000 18.35000  ? 300 LEU A C   1 
ATOM   2245 O  O   . LEU A  1 306 ? 28.65400  3.34700   22.43700 1.000 15.03000  ? 300 LEU A O   1 
ATOM   2246 C  CB  . LEU A  1 306 ? 26.98200  1.20800   20.64100 1.000 22.09000  ? 300 LEU A CB  1 
ATOM   2247 C  CG  . LEU A  1 306 ? 27.46100  -0.21300  20.42600 1.000 31.76000  ? 300 LEU A CG  1 
ATOM   2248 C  CD1 . LEU A  1 306 ? 27.07600  -0.67100  19.01300 1.000 29.77000  ? 300 LEU A CD1 1 
ATOM   2249 C  CD2 . LEU A  1 306 ? 28.95900  -0.13700  20.60500 1.000 26.43000  ? 300 LEU A CD2 1 
ATOM   2250 N  N   . GLU A  1 307 ? 26.63600  4.08600   21.75500 1.000 18.23000  ? 301 GLU A N   1 
ATOM   2251 C  CA  . GLU A  1 307 ? 27.12500  5.45800   21.78000 1.000 16.95000  ? 301 GLU A CA  1 
ATOM   2252 C  C   . GLU A  1 307 ? 27.61500  5.82100   23.17500 1.000 15.66000  ? 301 GLU A C   1 
ATOM   2253 O  O   . GLU A  1 307 ? 28.69200  6.40800   23.33500 1.000 17.49000  ? 301 GLU A O   1 
ATOM   2254 C  CB  . GLU A  1 307 ? 26.02900  6.40400   21.31300 1.000 18.73000  ? 301 GLU A CB  1 
ATOM   2255 C  CG  . GLU A  1 307 ? 26.44900  7.85700   21.29000 1.000 18.78000  ? 301 GLU A CG  1 
ATOM   2256 C  CD  . GLU A  1 307 ? 25.30100  8.79700   20.91600 1.000 25.04000  ? 301 GLU A CD  1 
ATOM   2257 O  OE1 . GLU A  1 307 ? 24.21600  8.66400   21.50400 1.000 27.15000  ? 301 GLU A OE1 1 
ATOM   2258 O  OE2 . GLU A  1 307 ? 25.48100  9.65300   20.03800 1.000 22.47000  ? 301 GLU A OE2 1 
ATOM   2259 N  N   . MET A  1 308 ? 26.83600  5.46200   24.20600 1.000 16.30000  ? 302 MET A N   1 
ATOM   2260 C  CA  . MET A  1 308 ? 27.26900  5.72500   25.57100 1.000 15.34000  ? 302 MET A CA  1 
ATOM   2261 C  C   . MET A  1 308 ? 28.50000  4.91200   25.93900 1.000 17.98000  ? 302 MET A C   1 
ATOM   2262 O  O   . MET A  1 308 ? 29.34100  5.40900   26.69200 1.000 17.51000  ? 302 MET A O   1 
ATOM   2263 C  CB  . MET A  1 308 ? 26.13500  5.42800   26.53500 1.000 18.33000  ? 302 MET A CB  1 
ATOM   2264 C  CG  . MET A  1 308 ? 24.93900  6.33800   26.33800 1.000 15.96000  ? 302 MET A CG  1 
ATOM   2265 S  SD  . MET A  1 308 ? 25.33200  8.06100   26.67200 1.000 20.00000  ? 302 MET A SD  1 
ATOM   2266 C  CE  . MET A  1 308 ? 25.63800  8.73200   25.04500 1.000 20.46000  ? 302 MET A CE  1 
ATOM   2267 N  N   . LEU A  1 309 ? 28.62100  3.67000   25.42900 1.000 12.36000  ? 303 LEU A N   1 
ATOM   2268 C  CA  . LEU A  1 309 ? 29.81900  2.86900   25.70800 1.000 16.02000  ? 303 LEU A CA  1 
ATOM   2269 C  C   . LEU A  1 309 ? 31.08300  3.61700   25.29500 1.000 16.73000  ? 303 LEU A C   1 
ATOM   2270 O  O   . LEU A  1 309 ? 32.01100  3.81700   26.09600 1.000 16.13000  ? 303 LEU A O   1 
ATOM   2271 C  CB  . LEU A  1 309 ? 29.73900  1.51400   24.98700 1.000 13.92000  ? 303 LEU A CB  1 
ATOM   2272 C  CG  . LEU A  1 309 ? 31.03700  0.66700   25.10100 1.000 14.96000  ? 303 LEU A CG  1 
ATOM   2273 C  CD1 . LEU A  1 309 ? 31.24100  0.16100   26.53900 1.000 16.17000  ? 303 LEU A CD1 1 
ATOM   2274 C  CD2 . LEU A  1 309 ? 31.01700  -0.49600  24.09400 1.000 13.13000  ? 303 LEU A CD2 1 
ATOM   2275 N  N   . TYR A  1 310 ? 31.12400  4.07700   24.04700 1.000 17.60000  ? 304 TYR A N   1 
ATOM   2276 C  CA  . TYR A  1 310 ? 32.31800  4.72400   23.54000 1.000 16.10000  ? 304 TYR A CA  1 
ATOM   2277 C  C   . TYR A  1 310 ? 32.64400  6.01200   24.29900 1.000 17.32000  ? 304 TYR A C   1 
ATOM   2278 O  O   . TYR A  1 310 ? 33.81900  6.31700   24.54300 1.000 18.43000  ? 304 TYR A O   1 
ATOM   2279 C  CB  . TYR A  1 310 ? 32.13700  5.03700   22.06300 1.000 18.47000  ? 304 TYR A CB  1 
ATOM   2280 C  CG  . TYR A  1 310 ? 32.07100  3.82000   21.19800 1.000 15.75000  ? 304 TYR A CG  1 
ATOM   2281 C  CD1 . TYR A  1 310 ? 32.86700  2.70300   21.45800 1.000 17.21000  ? 304 TYR A CD1 1 
ATOM   2282 C  CD2 . TYR A  1 310 ? 31.19700  3.77600   20.11500 1.000 20.14000  ? 304 TYR A CD2 1 
ATOM   2283 C  CE1 . TYR A  1 310 ? 32.78400  1.57500   20.63700 1.000 17.40000  ? 304 TYR A CE1 1 
ATOM   2284 C  CE2 . TYR A  1 310 ? 31.11300  2.66600   19.30900 1.000 20.17000  ? 304 TYR A CE2 1 
ATOM   2285 C  CZ  . TYR A  1 310 ? 31.92600  1.57700   19.56100 1.000 18.66000  ? 304 TYR A CZ  1 
ATOM   2286 O  OH  . TYR A  1 310 ? 31.83100  0.50700   18.72300 1.000 24.27000  ? 304 TYR A OH  1 
ATOM   2287 N  N   . ALA A  1 311 ? 31.61600  6.79600   24.63700 1.000 16.38000  ? 305 ALA A N   1 
ATOM   2288 C  CA  . ALA A  1 311 ? 31.78700  7.97900   25.46700 1.000 17.13000  ? 305 ALA A CA  1 
ATOM   2289 C  C   . ALA A  1 311 ? 32.41500  7.62900   26.80200 1.000 15.80000  ? 305 ALA A C   1 
ATOM   2290 O  O   . ALA A  1 311 ? 33.39300  8.26500   27.22600 1.000 15.05000  ? 305 ALA A O   1 
ATOM   2291 C  CB  . ALA A  1 311 ? 30.42200  8.67100   25.67500 1.000 15.82000  ? 305 ALA A CB  1 
ATOM   2292 N  N   . VAL A  1 312 ? 31.84900  6.62400   27.48100 1.000 13.85000  ? 306 VAL A N   1 
ATOM   2293 C  CA  . VAL A  1 312 ? 32.33900  6.20200   28.79400 1.000 16.31000  ? 306 VAL A CA  1 
ATOM   2294 C  C   . VAL A  1 312 ? 33.78600  5.72000   28.71000 1.000 17.15000  ? 306 VAL A C   1 
ATOM   2295 O  O   . VAL A  1 312 ? 34.61800  6.04000   29.56500 1.000 16.27000  ? 306 VAL A O   1 
ATOM   2296 C  CB  . VAL A  1 312 ? 31.43700  5.09900   29.36700 1.000 16.95000  ? 306 VAL A CB  1 
ATOM   2297 C  CG1 . VAL A  1 312 ? 32.13100  4.42000   30.54200 1.000 17.85000  ? 306 VAL A CG1 1 
ATOM   2298 C  CG2 . VAL A  1 312 ? 30.09100  5.68200   29.78800 1.000 19.85000  ? 306 VAL A CG2 1 
ATOM   2299 N  N   . VAL A  1 313 ? 34.06200  4.83500   27.75500 1.000 16.43000  ? 307 VAL A N   1 
ATOM   2300 C  CA  . VAL A  1 313 ? 35.41200  4.29300   27.61000 1.000 18.20000  ? 307 VAL A CA  1 
ATOM   2301 C  C   . VAL A  1 313 ? 36.42300  5.41700   27.41200 1.000 17.45000  ? 307 VAL A C   1 
ATOM   2302 O  O   . VAL A  1 313 ? 37.49400  5.42000   28.03500 1.000 17.49000  ? 307 VAL A O   1 
ATOM   2303 C  CB  . VAL A  1 313 ? 35.46600  3.27500   26.45300 1.000 13.74000  ? 307 VAL A CB  1 
ATOM   2304 C  CG1 . VAL A  1 313 ? 36.93800  2.89800   26.12500 1.000 18.23000  ? 307 VAL A CG1 1 
ATOM   2305 C  CG2 . VAL A  1 313 ? 34.58600  2.04400   26.78000 1.000 17.43000  ? 307 VAL A CG2 1 
ATOM   2306 N  N   . THR A  1 314 ? 36.08800  6.41100   26.57900 1.000 15.97000  ? 308 THR A N   1 
ATOM   2307 C  CA  . THR A  1 314 ? 37.04900  7.49300   26.36200 1.000 15.93000  ? 308 THR A CA  1 
ATOM   2308 C  C   . THR A  1 314 ? 37.18200  8.36500   27.60600 1.000 17.65000  ? 308 THR A C   1 
ATOM   2309 O  O   . THR A  1 314 ? 38.28300  8.84300   27.92300 1.000 19.47000  ? 308 THR A O   1 
ATOM   2310 C  CB  . THR A  1 314 ? 36.65300  8.34900   25.15200 1.000 16.50000  ? 308 THR A CB  1 
ATOM   2311 O  OG1 . THR A  1 314 ? 36.30200  7.50600   24.05000 1.000 17.61000  ? 308 THR A OG1 1 
ATOM   2312 C  CG2 . THR A  1 314 ? 37.83500  9.18100   24.73300 1.000 19.17000  ? 308 THR A CG2 1 
ATOM   2313 N  N   . GLU A  1 315 ? 36.07400  8.58800   28.33000 1.000 17.21000  ? 309 GLU A N   1 
ATOM   2314 C  CA  . GLU A  1 315 ? 36.18300  9.31600   29.59300 1.000 20.31000  ? 309 GLU A CA  1 
ATOM   2315 C  C   . GLU A  1 315 ? 37.05500  8.55100   30.58800 1.000 16.63000  ? 309 GLU A C   1 
ATOM   2316 O  O   . GLU A  1 315 ? 37.83400  9.14700   31.34500 1.000 18.99000  ? 309 GLU A O   1 
ATOM   2317 C  CB  . GLU A  1 315 ? 34.78700  9.58500   30.17300 1.000 18.54000  ? 309 GLU A CB  1 
ATOM   2318 C  CG  . GLU A  1 315 ? 34.77400  10.28600  31.56600 1.000 17.59000  ? 309 GLU A CG  1 
ATOM   2319 C  CD  . GLU A  1 315 ? 35.13800  11.76500  31.55200 1.000 21.74000  ? 309 GLU A CD  1 
ATOM   2320 O  OE1 . GLU A  1 315 ? 35.30200  12.35100  30.45600 1.000 21.41000  ? 309 GLU A OE1 1 
ATOM   2321 O  OE2 . GLU A  1 315 ? 35.26200  12.35000  32.66600 1.000 22.89000  ? 309 GLU A OE2 1 
ATOM   2322 N  N   . LEU A  1 316 ? 36.96200  7.23700   30.57000 1.000 16.63000  ? 310 LEU A N   1 
ATOM   2323 C  CA  . LEU A  1 316 ? 37.72000  6.40700   31.50300 1.000 18.97000  ? 310 LEU A CA  1 
ATOM   2324 C  C   . LEU A  1 316 ? 39.20000  6.50300   31.21800 1.000 18.91000  ? 310 LEU A C   1 
ATOM   2325 O  O   . LEU A  1 316 ? 40.01500  6.62500   32.14400 1.000 17.02000  ? 310 LEU A O   1 
ATOM   2326 C  CB  . LEU A  1 316 ? 37.26400  4.96100   31.37000 1.000 20.12000  ? 310 LEU A CB  1 
ATOM   2327 C  CG  . LEU A  1 316 ? 37.18100  3.95700   32.51700 1.000 33.05000  ? 310 LEU A CG  1 
ATOM   2328 C  CD1 . LEU A  1 316 ? 37.23000  4.64300   33.87300 1.000 30.93000  ? 310 LEU A CD1 1 
ATOM   2329 C  CD2 . LEU A  1 316 ? 35.86600  3.13400   32.35600 1.000 25.71000  ? 310 LEU A CD2 1 
ATOM   2330 N  N   . LEU A  1 317 ? 39.55400  6.43700   29.93400 1.000 18.62000  ? 311 LEU A N   1 
ATOM   2331 C  CA  . LEU A  1 317 ? 40.93300  6.62700   29.53400 1.000 21.19000  ? 311 LEU A CA  1 
ATOM   2332 C  C   . LEU A  1 317 ? 41.45000  7.96500   30.02400 1.000 23.42000  ? 311 LEU A C   1 
ATOM   2333 O  O   . LEU A  1 317 ? 42.57700  8.04700   30.51400 1.000 24.65000  ? 311 LEU A O   1 
ATOM   2334 C  CB  . LEU A  1 317 ? 41.05600  6.51400   28.01600 1.000 19.52000  ? 311 LEU A CB  1 
ATOM   2335 C  CG  . LEU A  1 317 ? 40.82200  5.08000   27.50300 1.000 21.94000  ? 311 LEU A CG  1 
ATOM   2336 C  CD1 . LEU A  1 317 ? 40.96400  4.99400   25.98600 1.000 21.41000  ? 311 LEU A CD1 1 
ATOM   2337 C  CD2 . LEU A  1 317 ? 41.72700  4.04600   28.19000 1.000 20.38000  ? 311 LEU A CD2 1 
ATOM   2338 N  N   . GLU A  1 318 ? 40.63600  9.02800   29.90100 1.000 19.06000  ? 312 GLU A N   1 
ATOM   2339 C  CA  . GLU A  1 318 ? 41.03800  10.33000  30.43900 1.000 21.56000  ? 312 GLU A CA  1 
ATOM   2340 C  C   . GLU A  1 318 ? 41.21100  10.27900  31.95300 1.000 22.50000  ? 312 GLU A C   1 
ATOM   2341 O  O   . GLU A  1 318 ? 42.22000  10.75900  32.47700 1.000 23.15000  ? 312 GLU A O   1 
ATOM   2342 C  CB  . GLU A  1 318 ? 40.03800  11.41600  30.07200 1.000 23.58000  ? 312 GLU A CB  1 
ATOM   2343 C  CG  . GLU A  1 318 ? 40.59000  12.83000  30.48000 1.000 21.36000  ? 312 GLU A CG  1 
ATOM   2344 C  CD  . GLU A  1 318 ? 39.79500  13.93400  29.85000 1.000 29.23000  ? 312 GLU A CD  1 
ATOM   2345 O  OE1 . GLU A  1 318 ? 38.62900  14.09800  30.23400 1.000 29.33000  ? 312 GLU A OE1 1 
ATOM   2346 O  OE2 . GLU A  1 318 ? 40.33900  14.63500  28.97400 1.000 37.72000  ? 312 GLU A OE2 1 
ATOM   2347 N  N   . ARG A  1 319 ? 40.25800  9.67300   32.67500 1.000 20.31000  ? 313 ARG A N   1 
ATOM   2348 C  CA  . ARG A  1 319 ? 40.39600  9.60700   34.13200 1.000 24.47000  ? 313 ARG A CA  1 
ATOM   2349 C  C   . ARG A  1 319 ? 41.65300  8.84900   34.53900 1.000 22.14000  ? 313 ARG A C   1 
ATOM   2350 O  O   . ARG A  1 319 ? 42.34200  9.23700   35.48900 1.000 25.16000  ? 313 ARG A O   1 
ATOM   2351 C  CB  . ARG A  1 319 ? 39.18500  8.93400   34.77400 1.000 23.06000  ? 313 ARG A CB  1 
ATOM   2352 C  CG  . ARG A  1 319 ? 37.81500  9.49400   34.41500 1.000 25.12000  ? 313 ARG A CG  1 
ATOM   2353 C  CD  . ARG A  1 319 ? 37.34700  10.53100  35.39100 1.000 24.40000  ? 313 ARG A CD  1 
ATOM   2354 N  NE  . ARG A  1 319 ? 36.02600  11.00500  35.00500 1.000 23.06000  ? 313 ARG A NE  1 
ATOM   2355 C  CZ  . ARG A  1 319 ? 34.91700  10.83300  35.70800 1.000 21.39000  ? 313 ARG A CZ  1 
ATOM   2356 N  NH1 . ARG A  1 319 ? 34.92800  10.23800  36.88600 1.000 22.88000  ? 313 ARG A NH1 1 
ATOM   2357 N  NH2 . ARG A  1 319 ? 33.77600  11.32800  35.24600 1.000 21.41000  ? 313 ARG A NH2 1 
ATOM   2358 N  N   . LEU A  1 320 ? 41.96400  7.77000   33.82900 1.000 18.88000  ? 314 LEU A N   1 
ATOM   2359 C  CA  . LEU A  1 320 ? 43.12400  6.92300   34.10900 1.000 21.64000  ? 314 LEU A CA  1 
ATOM   2360 C  C   . LEU A  1 320 ? 44.43100  7.52000   33.61900 1.000 24.01000  ? 314 LEU A C   1 
ATOM   2361 O  O   . LEU A  1 320 ? 45.50800  6.97200   33.90600 1.000 22.16000  ? 314 LEU A O   1 
ATOM   2362 C  CB  . LEU A  1 320 ? 42.91400  5.54900   33.46200 1.000 18.86000  ? 314 LEU A CB  1 
ATOM   2363 C  CG  . LEU A  1 320 ? 41.72800  4.76100   34.02100 1.000 21.83000  ? 314 LEU A CG  1 
ATOM   2364 C  CD1 . LEU A  1 320 ? 41.48600  3.54900   33.13700 1.000 18.50000  ? 314 LEU A CD1 1 
ATOM   2365 C  CD2 . LEU A  1 320 ? 41.97900  4.32300   35.47000 1.000 22.36000  ? 314 LEU A CD2 1 
ATOM   2366 N  N   . GLY A  1 321 ? 44.37100  8.60700   32.86900 1.000 23.15000  ? 315 GLY A N   1 
ATOM   2367 C  CA  . GLY A  1 321 ? 45.56900  9.20900   32.34000 1.000 27.19000  ? 315 GLY A CA  1 
ATOM   2368 C  C   . GLY A  1 321 ? 46.23500  8.41800   31.24300 1.000 27.34000  ? 315 GLY A C   1 
ATOM   2369 O  O   . GLY A  1 321 ? 47.43200  8.57000   31.02800 1.000 30.10000  ? 315 GLY A O   1 
ATOM   2370 N  N   . ILE A  1 322 ? 45.49200  7.59100   30.52300 1.000 28.51000  ? 316 ILE A N   1 
ATOM   2371 C  CA  . ILE A  1 322 ? 46.08600  6.71800   29.51600 1.000 28.79000  ? 316 ILE A CA  1 
ATOM   2372 C  C   . ILE A  1 322 ? 46.13400  7.46400   28.18400 1.000 30.62000  ? 316 ILE A C   1 
ATOM   2373 O  O   . ILE A  1 322 ? 45.10100  7.89200   27.65900 1.000 31.98000  ? 316 ILE A O   1 
ATOM   2374 C  CB  . ILE A  1 322 ? 45.30800  5.40100   29.43000 1.000 26.46000  ? 316 ILE A CB  1 
ATOM   2375 C  CG1 . ILE A  1 322 ? 45.64400  4.56600   30.67500 1.000 26.46000  ? 316 ILE A CG1 1 
ATOM   2376 C  CG2 . ILE A  1 322 ? 45.60400  4.66800   28.13700 1.000 26.12000  ? 316 ILE A CG2 1 
ATOM   2377 C  CD1 . ILE A  1 322 ? 44.66700  3.49400   30.97400 1.000 25.73000  ? 316 ILE A CD1 1 
ATOM   2378 N  N   . GLY A  1 323 ? 47.33500  7.63600   27.64800 1.000 30.76000  ? 317 GLY A N   1 
ATOM   2379 C  CA  . GLY A  1 323 ? 47.54300  8.47300   26.48300 1.000 33.17000  ? 317 GLY A CA  1 
ATOM   2380 C  C   . GLY A  1 323 ? 47.75400  9.93300   26.85400 1.000 37.42000  ? 317 GLY A C   1 
ATOM   2381 O  O   . GLY A  1 323 ? 47.46300  10.37300  27.96300 1.000 41.55000  ? 317 GLY A O   1 
ATOM   2382 N  N   . SER A  1 324 ? 48.27600  10.69600  25.90100 1.000 38.94000  ? 318 SER A N   1 
ATOM   2383 C  CA  . SER A  1 324 ? 48.34400  12.14500  26.07200 1.000 37.83000  ? 318 SER A CA  1 
ATOM   2384 C  C   . SER A  1 324 ? 46.99700  12.79300  25.74900 1.000 41.85000  ? 318 SER A C   1 
ATOM   2385 O  O   . SER A  1 324 ? 46.18100  12.21900  25.03000 1.000 39.79000  ? 318 SER A O   1 
ATOM   2386 C  CB  . SER A  1 324 ? 49.40600  12.72800  25.15900 1.000 40.68000  ? 318 SER A CB  1 
ATOM   2387 O  OG  . SER A  1 324 ? 49.04700  12.46200  23.82100 1.000 38.27000  ? 318 SER A OG  1 
ATOM   2388 N  N   . PRO A  1 325 ? 46.74400  14.00400  26.25600 1.000 47.05000  ? 319 PRO A N   1 
ATOM   2389 C  CA  . PRO A  1 325 ? 45.57900  14.77000  25.76400 1.000 48.65000  ? 319 PRO A CA  1 
ATOM   2390 C  C   . PRO A  1 325 ? 45.48100  14.84100  24.24100 1.000 45.94000  ? 319 PRO A C   1 
ATOM   2391 O  O   . PRO A  1 325 ? 44.38200  14.70100  23.68700 1.000 40.03000  ? 319 PRO A O   1 
ATOM   2392 C  CB  . PRO A  1 325 ? 45.80100  16.15400  26.39200 1.000 48.53000  ? 319 PRO A CB  1 
ATOM   2393 C  CG  . PRO A  1 325 ? 46.47800  15.83400  27.68800 1.000 47.67000  ? 319 PRO A CG  1 
ATOM   2394 C  CD  . PRO A  1 325 ? 47.39700  14.67000  27.39700 1.000 46.38000  ? 319 PRO A CD  1 
ATOM   2395 N  N   . ASP A  1 326 ? 46.61100  15.02400  23.54600 1.000 41.12000  ? 320 ASP A N   1 
ATOM   2396 C  CA  . ASP A  1 326 ? 46.56800  15.08800  22.08600 1.000 41.97000  ? 320 ASP A CA  1 
ATOM   2397 C  C   . ASP A  1 326 ? 46.14400  13.74600  21.48100 1.000 37.83000  ? 320 ASP A C   1 
ATOM   2398 O  O   . ASP A  1 326 ? 45.31000  13.70900  20.56400 1.000 35.45000  ? 320 ASP A O   1 
ATOM   2399 C  CB  . ASP A  1 326 ? 47.92800  15.55300  21.54000 1.000 41.81000  ? 320 ASP A CB  1 
ATOM   2400 C  CG  . ASP A  1 326 ? 48.16100  17.06600  21.72100 1.000 49.46000  ? 320 ASP A CG  1 
ATOM   2401 O  OD1 . ASP A  1 326 ? 47.21500  17.87100  21.52100 1.000 45.44000  ? 320 ASP A OD1 1 
ATOM   2402 O  OD2 . ASP A  1 326 ? 49.30900  17.46000  22.05400 1.000 56.22000  ? 320 ASP A OD2 1 
ATOM   2403 N  N   . VAL A  1 327 ? 46.67500  12.63400  21.99900 1.000 34.19000  ? 321 VAL A N   1 
ATOM   2404 C  CA  . VAL A  1 327 ? 46.27700  11.31600  21.50200 1.000 31.57000  ? 321 VAL A CA  1 
ATOM   2405 C  C   . VAL A  1 327 ? 44.78400  11.09000  21.71900 1.000 33.52000  ? 321 VAL A C   1 
ATOM   2406 O  O   . VAL A  1 327 ? 44.04300  10.76700  20.78500 1.000 30.78000  ? 321 VAL A O   1 
ATOM   2407 C  CB  . VAL A  1 327 ? 47.10500  10.20800  22.17600 1.000 31.32000  ? 321 VAL A CB  1 
ATOM   2408 C  CG1 . VAL A  1 327 ? 46.47900  8.85600   21.91900 1.000 30.32000  ? 321 VAL A CG1 1 
ATOM   2409 C  CG2 . VAL A  1 327 ? 48.56400  10.24500  21.67100 1.000 36.78000  ? 321 VAL A CG2 1 
ATOM   2410 N  N   . ARG A  1 328 ? 44.31600  11.28000  22.95200 1.000 29.20000  ? 322 ARG A N   1 
ATOM   2411 C  CA  . ARG A  1 328 ? 42.89700  11.08300  23.21600 1.000 31.94000  ? 322 ARG A CA  1 
ATOM   2412 C  C   . ARG A  1 328 ? 42.00800  12.01700  22.39100 1.000 32.45000  ? 322 ARG A C   1 
ATOM   2413 O  O   . ARG A  1 328 ? 40.87900  11.64000  22.06000 1.000 32.19000  ? 322 ARG A O   1 
ATOM   2414 C  CB  . ARG A  1 328 ? 42.61100  11.23700  24.71400 1.000 37.23000  ? 322 ARG A CB  1 
ATOM   2415 C  CG  . ARG A  1 328 ? 43.10300  10.05200  25.56900 1.000 35.19000  ? 322 ARG A CG  1 
ATOM   2416 C  CD  . ARG A  1 328 ? 42.66000  10.19300  27.02100 1.000 31.43000  ? 322 ARG A CD  1 
ATOM   2417 N  NE  . ARG A  1 328 ? 42.95600  11.52200  27.52800 1.000 34.44000  ? 322 ARG A NE  1 
ATOM   2418 C  CZ  . ARG A  1 328 ? 44.02500  11.80200  28.25600 1.000 37.86000  ? 322 ARG A CZ  1 
ATOM   2419 N  NH1 . ARG A  1 328 ? 44.83300  10.84200  28.67900 1.000 36.02000  ? 322 ARG A NH1 1 
ATOM   2420 N  NH2 . ARG A  1 328 ? 44.29500  13.07200  28.56400 1.000 37.20000  ? 322 ARG A NH2 1 
ATOM   2421 N  N   . SER A  1 329 ? 42.48500  13.21100  22.02800 1.000 33.12000  ? 323 SER A N   1 
ATOM   2422 C  CA  . SER A  1 329 ? 41.62300  14.14900  21.31400 1.000 33.62000  ? 323 SER A CA  1 
ATOM   2423 C  C   . SER A  1 329 ? 41.22200  13.63300  19.93800 1.000 32.09000  ? 323 SER A C   1 
ATOM   2424 O  O   . SER A  1 329 ? 40.25200  14.13900  19.36600 1.000 28.49000  ? 323 SER A O   1 
ATOM   2425 C  CB  . SER A  1 329 ? 42.29400  15.51900  21.18100 1.000 34.84000  ? 323 SER A CB  1 
ATOM   2426 O  OG  . SER A  1 329 ? 43.34600  15.49300  20.23100 1.000 37.22000  ? 323 SER A OG  1 
ATOM   2427 N  N   . GLN A  1 330 ? 41.94100  12.64700  19.39600 1.000 25.35000  ? 324 GLN A N   1 
ATOM   2428 C  CA  . GLN A  1 330 ? 41.49100  11.92200  18.20000 1.000 28.28000  ? 324 GLN A CA  1 
ATOM   2429 C  C   . GLN A  1 330 ? 40.15000  11.21200  18.39200 1.000 27.15000  ? 324 GLN A C   1 
ATOM   2430 O  O   . GLN A  1 330 ? 39.48300  10.86800  17.40500 1.000 27.52000  ? 324 GLN A O   1 
ATOM   2431 C  CB  . GLN A  1 330 ? 42.54300  10.89000  17.79100 1.000 27.80000  ? 324 GLN A CB  1 
ATOM   2432 C  CG  . GLN A  1 330 ? 43.88600  11.52100  17.46300 1.000 23.71000  ? 324 GLN A CG  1 
ATOM   2433 C  CD  . GLN A  1 330 ? 44.92900  10.55400  16.92600 1.000 31.58000  ? 324 GLN A CD  1 
ATOM   2434 O  OE1 . GLN A  1 330 ? 44.61700  9.51300   16.33000 1.000 31.70000  ? 324 GLN A OE1 1 
ATOM   2435 N  NE2 . GLN A  1 330 ? 46.19300  10.88900  17.15800 1.000 30.26000  ? 324 GLN A NE2 1 
ATOM   2436 N  N   . LEU A  1 331 ? 39.72900  10.98300  19.62700 1.000 24.68000  ? 325 LEU A N   1 
ATOM   2437 C  CA  . LEU A  1 331 ? 38.45500  10.31900  19.86900 1.000 25.95000  ? 325 LEU A CA  1 
ATOM   2438 C  C   . LEU A  1 331 ? 37.38600  11.27800  20.37600 1.000 23.51000  ? 325 LEU A C   1 
ATOM   2439 O  O   . LEU A  1 331 ? 36.35900  10.83000  20.92100 1.000 18.74000  ? 325 LEU A O   1 
ATOM   2440 C  CB  . LEU A  1 331 ? 38.66200  9.16400   20.84700 1.000 25.51000  ? 325 LEU A CB  1 
ATOM   2441 C  CG  . LEU A  1 331 ? 39.75700  8.15700   20.46500 1.000 23.75000  ? 325 LEU A CG  1 
ATOM   2442 C  CD1 . LEU A  1 331 ? 39.91500  7.12100   21.57000 1.000 24.20000  ? 325 LEU A CD1 1 
ATOM   2443 C  CD2 . LEU A  1 331 ? 39.45300  7.43800   19.13500 1.000 26.12000  ? 325 LEU A CD2 1 
ATOM   2444 N  N   . ALA A  1 332 ? 37.60900  12.59100  20.17800 1.000 27.18000  ? 326 ALA A N   1 
ATOM   2445 C  CA  . ALA A  1 332 ? 36.72300  13.61100  20.73200 1.000 25.12000  ? 326 ALA A CA  1 
ATOM   2446 C  C   . ALA A  1 332 ? 35.27400  13.39500  20.30300 1.000 24.43000  ? 326 ALA A C   1 
ATOM   2447 O  O   . ALA A  1 332 ? 34.35000  13.64600  21.08100 1.000 24.55000  ? 326 ALA A O   1 
ATOM   2448 C  CB  . ALA A  1 332 ? 37.19800  15.00900  20.31700 1.000 26.08000  ? 326 ALA A CB  1 
ATOM   2449 N  N   . SER A  1 333 ? 35.05800  12.93000  19.07000 1.000 22.53000  ? 327 SER A N   1 
ATOM   2450 C  CA  . SER A  1 333 ? 33.70200  12.78800  18.57100 1.000 22.65000  ? 327 SER A CA  1 
ATOM   2451 C  C   . SER A  1 333 ? 32.97100  11.62700  19.24300 1.000 24.05000  ? 327 SER A C   1 
ATOM   2452 O  O   . SER A  1 333 ? 31.73300  11.61900  19.28700 1.000 20.66000  ? 327 SER A O   1 
ATOM   2453 C  CB  . SER A  1 333 ? 33.74200  12.58900  17.06300 1.000 27.38000  ? 327 SER A CB  1 
ATOM   2454 O  OG  . SER A  1 333 ? 34.19300  11.26600  16.80100 1.000 32.00000  ? 327 SER A OG  1 
ATOM   2455 N  N   . PHE A  1 334 ? 33.71500  10.64500  19.75900 1.000 23.07000  ? 328 PHE A N   1 
ATOM   2456 C  CA  . PHE A  1 334 ? 33.10000  9.59000   20.55800 1.000 21.81000  ? 328 PHE A CA  1 
ATOM   2457 C  C   . PHE A  1 334 ? 32.95000  10.00000  22.01100 1.000 19.86000  ? 328 PHE A C   1 
ATOM   2458 O  O   . PHE A  1 334 ? 31.99800  9.58700   22.67900 1.000 18.71000  ? 328 PHE A O   1 
ATOM   2459 C  CB  . PHE A  1 334 ? 33.95100  8.32600   20.50200 1.000 21.04000  ? 328 PHE A CB  1 
ATOM   2460 C  CG  . PHE A  1 334 ? 33.98500  7.66300   19.16000 1.000 19.77000  ? 328 PHE A CG  1 
ATOM   2461 C  CD1 . PHE A  1 334 ? 32.96600  6.79500   18.77400 1.000 24.44000  ? 328 PHE A CD1 1 
ATOM   2462 C  CD2 . PHE A  1 334 ? 35.04900  7.86800   18.30500 1.000 22.99000  ? 328 PHE A CD2 1 
ATOM   2463 C  CE1 . PHE A  1 334 ? 33.01500  6.15300   17.55200 1.000 24.97000  ? 328 PHE A CE1 1 
ATOM   2464 C  CE2 . PHE A  1 334 ? 35.11200  7.22400   17.08100 1.000 22.44000  ? 328 PHE A CE2 1 
ATOM   2465 C  CZ  . PHE A  1 334 ? 34.10100  6.36700   16.70200 1.000 21.13000  ? 328 PHE A CZ  1 
ATOM   2466 N  N   . HIS A  1 335 ? 33.91900  10.75300  22.52800 1.000 21.23000  ? 329 HIS A N   1 
ATOM   2467 C  CA  . HIS A  1 335 ? 33.92700  11.10000  23.94500 1.000 21.40000  ? 329 HIS A CA  1 
ATOM   2468 C  C   . HIS A  1 335 ? 32.72800  11.97400  24.32000 1.000 21.93000  ? 329 HIS A C   1 
ATOM   2469 O  O   . HIS A  1 335 ? 32.08000  11.74900  25.35300 1.000 18.05000  ? 329 HIS A O   1 
ATOM   2470 C  CB  . HIS A  1 335 ? 35.24200  11.80600  24.26200 1.000 23.10000  ? 329 HIS A CB  1 
ATOM   2471 C  CG  . HIS A  1 335 ? 35.45900  12.08900  25.70900 1.000 23.06000  ? 329 HIS A CG  1 
ATOM   2472 N  ND1 . HIS A  1 335 ? 36.51300  12.85900  26.14600 1.000 23.94000  ? 329 HIS A ND1 1 
ATOM   2473 C  CD2 . HIS A  1 335 ? 34.80700  11.67900  26.82200 1.000 23.67000  ? 329 HIS A CD2 1 
ATOM   2474 C  CE1 . HIS A  1 335 ? 36.47700  12.94900  27.46200 1.000 27.08000  ? 329 HIS A CE1 1 
ATOM   2475 N  NE2 . HIS A  1 335 ? 35.44600  12.25100  27.89900 1.000 18.76000  ? 329 HIS A NE2 1 
ATOM   2476 N  N   . HIS A  1 336 ? 32.43300  12.99100  23.50500 1.000 19.81000  ? 330 HIS A N   1 
ATOM   2477 C  CA  . HIS A  1 336 ? 31.26800  13.85800  23.69100 1.000 22.06000  ? 330 HIS A CA  1 
ATOM   2478 C  C   . HIS A  1 336 ? 30.43800  13.83700  22.41600 1.000 22.30000  ? 330 HIS A C   1 
ATOM   2479 O  O   . HIS A  1 336 ? 30.62000  14.69300  21.53000 1.000 25.52000  ? 330 HIS A O   1 
ATOM   2480 C  CB  . HIS A  1 336 ? 31.70200  15.27700  24.07000 1.000 21.04000  ? 330 HIS A CB  1 
ATOM   2481 C  CG  . HIS A  1 336 ? 32.46800  15.30400  25.35000 1.000 25.13000  ? 330 HIS A CG  1 
ATOM   2482 N  ND1 . HIS A  1 336 ? 33.84300  15.23200  25.39600 1.000 29.94000  ? 330 HIS A ND1 1 
ATOM   2483 C  CD2 . HIS A  1 336 ? 32.04400  15.27800  26.63700 1.000 28.06000  ? 330 HIS A CD2 1 
ATOM   2484 C  CE1 . HIS A  1 336 ? 34.23800  15.21800  26.65600 1.000 27.90000  ? 330 HIS A CE1 1 
ATOM   2485 N  NE2 . HIS A  1 336 ? 33.16700  15.24000  27.42900 1.000 25.94000  ? 330 HIS A NE2 1 
ATOM   2486 N  N   . PRO A  1 337 ? 29.52200  12.88000  22.28700 1.000 20.43000  ? 331 PRO A N   1 
ATOM   2487 C  CA  . PRO A  1 337 ? 28.80500  12.70200  21.02200 1.000 23.34000  ? 331 PRO A CA  1 
ATOM   2488 C  C   . PRO A  1 337 ? 28.02500  13.95800  20.66100 1.000 25.74000  ? 331 PRO A C   1 
ATOM   2489 O  O   . PRO A  1 337 ? 27.58300  14.70700  21.52900 1.000 27.31000  ? 331 PRO A O   1 
ATOM   2490 C  CB  . PRO A  1 337 ? 27.85700  11.52100  21.29500 1.000 27.28000  ? 331 PRO A CB  1 
ATOM   2491 C  CG  . PRO A  1 337 ? 28.24100  10.91200  22.56600 1.000 23.40000  ? 331 PRO A CG  1 
ATOM   2492 C  CD  . PRO A  1 337 ? 29.24500  11.82400  23.27300 1.000 19.38000  ? 331 PRO A CD  1 
ATOM   2493 N  N   . GLN A  1 338 ? 27.87600  14.17900  19.36100 1.000 28.08000  ? 332 GLN A N   1 
ATOM   2494 C  CA  . GLN A  1 338 ? 27.17300  15.34800  18.85800 1.000 27.66000  ? 332 GLN A CA  1 
ATOM   2495 C  C   . GLN A  1 338 ? 25.71300  15.32300  19.30800 1.000 24.89000  ? 332 GLN A C   1 
ATOM   2496 O  O   . GLN A  1 338 ? 25.06800  14.28100  19.28800 1.000 24.82000  ? 332 GLN A O   1 
ATOM   2497 C  CB  . GLN A  1 338 ? 27.23800  15.37300  17.33400 1.000 30.33000  ? 332 GLN A CB  1 
ATOM   2498 C  CG  . GLN A  1 338 ? 28.61600  15.22000  16.74000 1.000 39.46000  ? 332 GLN A CG  1 
ATOM   2499 C  CD  . GLN A  1 338 ? 29.58400  16.29500  17.19200 1.000 50.26000  ? 332 GLN A CD  1 
ATOM   2500 O  OE1 . GLN A  1 338 ? 29.19800  17.46600  17.36600 1.000 48.92000  ? 332 GLN A OE1 1 
ATOM   2501 N  NE2 . GLN A  1 338 ? 30.86300  15.90700  17.38600 1.000 48.37000  ? 332 GLN A NE2 1 
ATOM   2502 N  N   . ARG A  1 339 ? 25.19400  16.47900  19.71000 1.000 25.78000  ? 333 ARG A N   1 
ATOM   2503 C  CA  . ARG A  1 339 ? 23.78700  16.63200  20.09900 1.000 28.26000  ? 333 ARG A CA  1 
ATOM   2504 C  C   . ARG A  1 339 ? 23.27000  17.86400  19.39900 1.000 26.77000  ? 333 ARG A C   1 
ATOM   2505 O  O   . ARG A  1 339 ? 23.04000  18.90100  20.03400 1.000 31.69000  ? 333 ARG A O   1 
ATOM   2506 C  CB  . ARG A  1 339 ? 23.61800  16.75000  21.60500 1.000 27.75000  ? 333 ARG A CB  1 
ATOM   2507 C  CG  . ARG A  1 339 ? 23.72400  15.40200  22.32300 1.000 19.95000  ? 333 ARG A CG  1 
ATOM   2508 C  CD  . ARG A  1 339 ? 22.59300  14.47500  21.95500 1.000 26.07000  ? 333 ARG A CD  1 
ATOM   2509 N  NE  . ARG A  1 339 ? 22.67400  13.21700  22.69300 1.000 27.68000  ? 333 ARG A NE  1 
ATOM   2510 C  CZ  . ARG A  1 339 ? 23.37200  12.15500  22.30900 1.000 26.42000  ? 333 ARG A CZ  1 
ATOM   2511 N  NH1 . ARG A  1 339 ? 24.13500  12.18000  21.22600 1.000 27.38000  ? 333 ARG A NH1 1 
ATOM   2512 N  NH2 . ARG A  1 339 ? 23.28200  11.03100  23.01600 1.000 26.10000  ? 333 ARG A NH2 1 
ATOM   2513 N  N   . VAL A  1 340 ? 23.14700  17.78500  18.08000 1.000 26.99000  ? 334 VAL A N   1 
ATOM   2514 C  CA  . VAL A  1 340 ? 22.69800  18.94100  17.31100 1.000 29.65000  ? 334 VAL A CA  1 
ATOM   2515 C  C   . VAL A  1 340 ? 21.49700  18.51800  16.48800 1.000 29.63000  ? 334 VAL A C   1 
ATOM   2516 O  O   . VAL A  1 340 ? 21.42600  17.37200  16.02400 1.000 26.43000  ? 334 VAL A O   1 
ATOM   2517 C  CB  . VAL A  1 340 ? 23.79700  19.54500  16.40600 1.000 34.05000  ? 334 VAL A CB  1 
ATOM   2518 C  CG1 . VAL A  1 340 ? 25.19700  19.30600  16.97800 1.000 30.02000  ? 334 VAL A CG1 1 
ATOM   2519 C  CG2 . VAL A  1 340 ? 23.65700  19.08100  14.95700 1.000 36.66000  ? 334 VAL A CG2 1 
ATOM   2520 N  N   . ASN A  1 341 ? 20.54900  19.44400  16.31900 1.000 26.22000  ? 335 ASN A N   1 
ATOM   2521 C  CA  . ASN A  1 341 ? 19.24400  19.07400  15.79000 1.000 26.08000  ? 335 ASN A CA  1 
ATOM   2522 C  C   . ASN A  1 341 ? 19.25000  19.25700  14.27500 1.000 27.30000  ? 335 ASN A C   1 
ATOM   2523 O  O   . ASN A  1 341 ? 20.28000  19.58500  13.67700 1.000 20.73000  ? 335 ASN A O   1 
ATOM   2524 C  CB  . ASN A  1 341 ? 18.12900  19.84500  16.52000 1.000 25.21000  ? 335 ASN A CB  1 
ATOM   2525 C  CG  . ASN A  1 341 ? 18.12100  21.34600  16.25200 1.000 23.43000  ? 335 ASN A CG  1 
ATOM   2526 O  OD1 . ASN A  1 341 ? 18.78800  21.86000  15.35400 1.000 28.48000  ? 335 ASN A OD1 1 
ATOM   2527 N  ND2 . ASN A  1 341 ? 17.32800  22.07200  17.04100 1.000 24.09000  ? 335 ASN A ND2 1 
ATOM   2528 N  N   . THR A  1 342 ? 18.08900  19.05700  13.64100 1.000 22.05000  ? 336 THR A N   1 
ATOM   2529 C  CA  . THR A  1 342 ? 17.94200  19.17200  12.19000 1.000 22.68000  ? 336 THR A CA  1 
ATOM   2530 C  C   . THR A  1 342 ? 18.20900  20.56900  11.66100 1.000 24.63000  ? 336 THR A C   1 
ATOM   2531 O  O   . THR A  1 342 ? 18.25900  20.76300  10.43700 1.000 23.52000  ? 336 THR A O   1 
ATOM   2532 C  CB  . THR A  1 342 ? 16.53000  18.75200  11.77100 1.000 23.23000  ? 336 THR A CB  1 
ATOM   2533 O  OG1 . THR A  1 342 ? 15.56500  19.61300  12.40200 1.000 23.00000  ? 336 THR A OG1 1 
ATOM   2534 C  CG2 . THR A  1 342 ? 16.29100  17.26800  12.15400 1.000 22.39000  ? 336 THR A CG2 1 
ATOM   2535 N  N   . MET A  1 343 ? 18.33900  21.56000  12.53300 1.000 24.57000  ? 337 MET A N   1 
ATOM   2536 C  CA  . MET A  1 343 ? 18.65000  22.90300  12.09300 1.000 26.49000  ? 337 MET A CA  1 
ATOM   2537 C  C   . MET A  1 343 ? 20.03200  23.33700  12.55800 1.000 27.85000  ? 337 MET A C   1 
ATOM   2538 O  O   . MET A  1 343 ? 20.34500  24.52900  12.51200 1.000 27.49000  ? 337 MET A O   1 
ATOM   2539 C  CB  . MET A  1 343 ? 17.56500  23.86800  12.57300 1.000 27.10000  ? 337 MET A CB  1 
ATOM   2540 C  CG  . MET A  1 343 ? 16.20400  23.49900  12.01300 1.000 26.59000  ? 337 MET A CG  1 
ATOM   2541 S  SD  . MET A  1 343 ? 16.12200  23.67400  10.20700 1.000 28.63000  ? 337 MET A SD  1 
ATOM   2542 C  CE  . MET A  1 343 ? 16.08100  25.46500  10.02400 1.000 27.79000  ? 337 MET A CE  1 
ATOM   2543 N  N   . GLY A  1 344 ? 20.84600  22.38800  13.00400 1.000 26.91000  ? 338 GLY A N   1 
ATOM   2544 C  CA  . GLY A  1 344 ? 22.21200  22.62000  13.40900 1.000 31.24000  ? 338 GLY A CA  1 
ATOM   2545 C  C   . GLY A  1 344 ? 22.39300  23.26500  14.76200 1.000 32.86000  ? 338 GLY A C   1 
ATOM   2546 O  O   . GLY A  1 344 ? 23.47500  23.77900  15.03500 1.000 27.51000  ? 338 GLY A O   1 
ATOM   2547 N  N   . VAL A  1 345 ? 21.37700  23.27400  15.61200 1.000 28.27000  ? 339 VAL A N   1 
ATOM   2548 C  CA  . VAL A  1 345 ? 21.45900  23.90600  16.92800 1.000 27.16000  ? 339 VAL A CA  1 
ATOM   2549 C  C   . VAL A  1 345 ? 21.84200  22.83200  17.94100 1.000 27.27000  ? 339 VAL A C   1 
ATOM   2550 O  O   . VAL A  1 345 ? 21.28600  21.73100  17.91000 1.000 23.34000  ? 339 VAL A O   1 
ATOM   2551 C  CB  . VAL A  1 345 ? 20.11500  24.55700  17.30800 1.000 25.19000  ? 339 VAL A CB  1 
ATOM   2552 C  CG1 . VAL A  1 345 ? 20.16700  25.12400  18.71900 1.000 28.08000  ? 339 VAL A CG1 1 
ATOM   2553 C  CG2 . VAL A  1 345 ? 19.67800  25.63500  16.29300 1.000 26.41000  ? 339 VAL A CG2 1 
ATOM   2554 N  N   . THR A  1 346 ? 22.78500  23.13800  18.83800 1.000 27.41000  ? 340 THR A N   1 
ATOM   2555 C  CA  . THR A  1 346 ? 23.14600  22.17200  19.88200 1.000 27.23000  ? 340 THR A CA  1 
ATOM   2556 C  C   . THR A  1 346 ? 22.03200  22.13200  20.91300 1.000 24.79000  ? 340 THR A C   1 
ATOM   2557 O  O   . THR A  1 346 ? 21.70500  23.16900  21.50300 1.000 24.99000  ? 340 THR A O   1 
ATOM   2558 C  CB  . THR A  1 346 ? 24.45400  22.56500  20.57400 1.000 31.36000  ? 340 THR A CB  1 
ATOM   2559 O  OG1 . THR A  1 346 ? 25.46500  22.82700  19.59600 1.000 36.78000  ? 340 THR A OG1 1 
ATOM   2560 C  CG2 . THR A  1 346 ? 24.91400  21.43800  21.51100 1.000 27.77000  ? 340 THR A CG2 1 
ATOM   2561 N  N   . THR A  1 347 ? 21.48300  20.94700  21.15500 1.000 25.00000  ? 341 THR A N   1 
ATOM   2562 C  CA  . THR A  1 347 ? 20.34800  20.78200  22.05300 1.000 25.21000  ? 341 THR A CA  1 
ATOM   2563 C  C   . THR A  1 347 ? 20.71800  20.18300  23.40200 1.000 25.47000  ? 341 THR A C   1 
ATOM   2564 O  O   . THR A  1 347 ? 19.88600  20.21000  24.32400 1.000 20.89000  ? 341 THR A O   1 
ATOM   2565 C  CB  . THR A  1 347 ? 19.27300  19.88000  21.41500 1.000 21.61000  ? 341 THR A CB  1 
ATOM   2566 O  OG1 . THR A  1 347 ? 19.80600  18.59300  21.18900 1.000 27.67000  ? 341 THR A OG1 1 
ATOM   2567 C  CG2 . THR A  1 347 ? 18.78600  20.42500  20.10200 1.000 28.18000  ? 341 THR A CG2 1 
ATOM   2568 N  N   . GLY A  1 348 ? 21.91700  19.62700  23.54900 1.000 19.90000  ? 342 GLY A N   1 
ATOM   2569 C  CA  . GLY A  1 348 ? 22.24100  19.03800  24.82800 1.000 18.60000  ? 342 GLY A CA  1 
ATOM   2570 C  C   . GLY A  1 348 ? 23.62800  18.42800  24.82600 1.000 23.34000  ? 342 GLY A C   1 
ATOM   2571 O  O   . GLY A  1 348 ? 24.48400  18.85100  24.04900 1.000 24.26000  ? 342 GLY A O   1 
ATOM   2572 N  N   . GLY A  1 349 ? 23.85500  17.44600  25.68400 1.000 19.58000  ? 343 GLY A N   1 
ATOM   2573 C  CA  . GLY A  1 349 ? 25.17400  16.87000  25.81700 1.000 20.44000  ? 343 GLY A CA  1 
ATOM   2574 C  C   . GLY A  1 349 ? 25.14000  15.63300  26.68500 1.000 22.27000  ? 343 GLY A C   1 
ATOM   2575 O  O   . GLY A  1 349 ? 24.08000  15.12200  27.04700 1.000 18.26000  ? 343 GLY A O   1 
ATOM   2576 N  N   . VAL A  1 350 ? 26.33400  15.16900  27.02400 1.000 21.47000  ? 344 VAL A N   1 
ATOM   2577 C  CA  A VAL A  1 350 ? 26.52400  13.96200  27.81100 0.700 19.53000  ? 344 VAL A CA  1 
ATOM   2578 C  CA  B VAL A  1 350 ? 26.53100  13.96000  27.81000 0.300 19.58000  ? 344 VAL A CA  1 
ATOM   2579 C  C   . VAL A  1 350 ? 27.38600  14.32100  29.01700 1.000 22.55000  ? 344 VAL A C   1 
ATOM   2580 O  O   . VAL A  1 350 ? 28.26700  15.18100  28.92400 1.000 23.87000  ? 344 VAL A O   1 
ATOM   2581 C  CB  A VAL A  1 350 ? 27.16600  12.87000  26.94000 0.700 21.50000  ? 344 VAL A CB  1 
ATOM   2582 C  CB  B VAL A  1 350 ? 27.18500  12.85200  26.96000 0.300 21.46000  ? 344 VAL A CB  1 
ATOM   2583 C  CG1 A VAL A  1 350 ? 27.51700  11.60700  27.77000 0.700 18.13000  ? 344 VAL A CG1 1 
ATOM   2584 C  CG1 B VAL A  1 350 ? 26.33100  12.58200  25.72200 0.300 23.28000  ? 344 VAL A CG1 1 
ATOM   2585 C  CG2 A VAL A  1 350 ? 26.21400  12.55400  25.77000 0.700 23.34000  ? 344 VAL A CG2 1 
ATOM   2586 C  CG2 B VAL A  1 350 ? 28.62100  13.22600  26.56400 0.300 19.98000  ? 344 VAL A CG2 1 
ATOM   2587 N  N   . SER A  1 351 ? 27.09000  13.70500  30.16200 1.000 19.25000  ? 345 SER A N   1 
ATOM   2588 C  CA  . SER A  1 351 ? 27.78600  13.97200  31.41300 1.000 18.22000  ? 345 SER A CA  1 
ATOM   2589 C  C   . SER A  1 351 ? 28.16900  12.65300  32.06000 1.000 20.94000  ? 345 SER A C   1 
ATOM   2590 O  O   . SER A  1 351 ? 27.54000  11.60800  31.83100 1.000 17.83000  ? 345 SER A O   1 
ATOM   2591 C  CB  . SER A  1 351 ? 26.93900  14.77000  32.42100 1.000 17.60000  ? 345 SER A CB  1 
ATOM   2592 O  OG  . SER A  1 351 ? 26.38300  15.93100  31.84700 1.000 25.58000  ? 345 SER A OG  1 
ATOM   2593 N  N   . PHE A  1 352 ? 29.19900  12.71000  32.89400 1.000 19.31000  ? 346 PHE A N   1 
ATOM   2594 C  CA  . PHE A  1 352 ? 29.74900  11.50800  33.52000 1.000 18.03000  ? 346 PHE A CA  1 
ATOM   2595 C  C   . PHE A  1 352 ? 29.80200  11.65500  35.03400 1.000 22.24000  ? 346 PHE A C   1 
ATOM   2596 O  O   . PHE A  1 352 ? 30.89700  11.76200  35.61700 1.000 20.77000  ? 346 PHE A O   1 
ATOM   2597 C  CB  . PHE A  1 352 ? 31.15700  11.21600  32.98600 1.000 16.98000  ? 346 PHE A CB  1 
ATOM   2598 C  CG  . PHE A  1 352 ? 31.23600  11.15600  31.48900 1.000 17.13000  ? 346 PHE A CG  1 
ATOM   2599 C  CD1 . PHE A  1 352 ? 30.80600  10.03900  30.78900 1.000 17.19000  ? 346 PHE A CD1 1 
ATOM   2600 C  CD2 . PHE A  1 352 ? 31.75200  12.22300  30.77800 1.000 20.49000  ? 346 PHE A CD2 1 
ATOM   2601 C  CE1 . PHE A  1 352 ? 30.87400  10.01500  29.40400 1.000 18.07000  ? 346 PHE A CE1 1 
ATOM   2602 C  CE2 . PHE A  1 352 ? 31.83000  12.19000  29.40200 1.000 21.12000  ? 346 PHE A CE2 1 
ATOM   2603 C  CZ  . PHE A  1 352 ? 31.39400  11.11700  28.71700 1.000 15.51000  ? 346 PHE A CZ  1 
ATOM   2604 N  N   . PRO A  1 353 ? 28.65600  11.59100  35.71300 1.000 20.98000  ? 347 PRO A N   1 
ATOM   2605 C  CA  . PRO A  1 353 ? 28.65900  11.83300  37.16300 1.000 21.65000  ? 347 PRO A CA  1 
ATOM   2606 C  C   . PRO A  1 353 ? 29.26300  10.68200  37.96000 1.000 24.50000  ? 347 PRO A C   1 
ATOM   2607 O  O   . PRO A  1 353 ? 29.22600  10.68700  39.18800 1.000 32.07000  ? 347 PRO A O   1 
ATOM   2608 C  CB  . PRO A  1 353 ? 27.17300  12.03200  37.48600 1.000 24.90000  ? 347 PRO A CB  1 
ATOM   2609 C  CG  . PRO A  1 353 ? 26.43700  11.31000  36.37600 1.000 19.28000  ? 347 PRO A CG  1 
ATOM   2610 C  CD  . PRO A  1 353 ? 27.28000  11.52900  35.15800 1.000 17.99000  ? 347 PRO A CD  1 
ATOM   2611 N  N   . PHE A  1 354 ? 29.83100  9.69500   37.29000 1.000 27.52000  ? 348 PHE A N   1 
ATOM   2612 C  CA  . PHE A  1 354 ? 30.40000  8.59400   38.06000 1.000 25.29000  ? 348 PHE A CA  1 
ATOM   2613 C  C   . PHE A  1 354 ? 31.76600  8.97700   38.65300 1.000 28.33000  ? 348 PHE A C   1 
ATOM   2614 O  O   . PHE A  1 354 ? 32.38600  9.99800   38.29900 1.000 24.99000  ? 348 PHE A O   1 
ATOM   2615 C  CB  . PHE A  1 354 ? 30.48200  7.34500   37.20200 1.000 21.12000  ? 348 PHE A CB  1 
ATOM   2616 C  CG  . PHE A  1 354 ? 31.31700  7.47600   35.95600 1.000 25.41000  ? 348 PHE A CG  1 
ATOM   2617 C  CD1 . PHE A  1 354 ? 32.68000  7.58300   36.03000 1.000 19.59000  ? 348 PHE A CD1 1 
ATOM   2618 C  CD2 . PHE A  1 354 ? 30.72500  7.43400   34.70300 1.000 21.78000  ? 348 PHE A CD2 1 
ATOM   2619 C  CE1 . PHE A  1 354 ? 33.44600  7.67700   34.88200 1.000 24.92000  ? 348 PHE A CE1 1 
ATOM   2620 C  CE2 . PHE A  1 354 ? 31.48900  7.49200   33.57000 1.000 21.56000  ? 348 PHE A CE2 1 
ATOM   2621 C  CZ  . PHE A  1 354 ? 32.83100  7.63600   33.65000 1.000 23.22000  ? 348 PHE A CZ  1 
ATOM   2622 N  N   . LYS A  1 355 ? 32.23600  8.15700   39.59300 1.000 25.30000  ? 349 LYS A N   1 
ATOM   2623 C  CA  . LYS A  1 355 ? 33.56500  8.35300   40.17000 1.000 27.03000  ? 349 LYS A CA  1 
ATOM   2624 C  C   . LYS A  1 355 ? 34.22600  6.99300   40.29800 1.000 24.34000  ? 349 LYS A C   1 
ATOM   2625 O  O   . LYS A  1 355 ? 33.65500  6.08600   40.91300 1.000 23.82000  ? 349 LYS A O   1 
ATOM   2626 C  CB  . LYS A  1 355 ? 33.50000  9.05300   41.53500 1.000 30.76000  ? 349 LYS A CB  1 
ATOM   2627 C  CG  . LYS A  1 355 ? 32.77200  10.41200  41.51000 1.000 33.73000  ? 349 LYS A CG  1 
ATOM   2628 C  CD  . LYS A  1 355 ? 32.25100  10.81600  42.88300 1.000 35.38000  ? 349 LYS A CD  1 
ATOM   2629 C  CE  . LYS A  1 355 ? 33.38200  11.15900  43.85300 1.000 35.41000  ? 349 LYS A CE  1 
ATOM   2630 N  NZ  . LYS A  1 355 ? 33.04500  12.37500  44.66800 1.000 41.33000  ? 349 LYS A NZ  1 
ATOM   2631 N  N   . LEU A  1 356 ? 35.41100  6.85500   39.69700 1.000 25.26000  ? 350 LEU A N   1 
ATOM   2632 C  CA  . LEU A  1 356 ? 36.19600  5.63400   39.81100 1.000 25.51000  ? 350 LEU A CA  1 
ATOM   2633 C  C   . LEU A  1 356 ? 36.49200  5.34600   41.26300 1.000 27.13000  ? 350 LEU A C   1 
ATOM   2634 O  O   . LEU A  1 356 ? 37.01900  6.19700   41.97200 1.000 28.48000  ? 350 LEU A O   1 
ATOM   2635 C  CB  . LEU A  1 356 ? 37.51800  5.78700   39.05800 1.000 22.80000  ? 350 LEU A CB  1 
ATOM   2636 C  CG  . LEU A  1 356 ? 37.53200  5.37000   37.60300 1.000 29.79000  ? 350 LEU A CG  1 
ATOM   2637 C  CD1 . LEU A  1 356 ? 38.92700  5.53800   37.01700 1.000 30.61000  ? 350 LEU A CD1 1 
ATOM   2638 C  CD2 . LEU A  1 356 ? 37.12100  3.92200   37.55800 1.000 23.78000  ? 350 LEU A CD2 1 
ATOM   2639 N  N   . ARG A  1 357 ? 36.16500  4.15800   41.73100 1.000 24.33000  ? 351 ARG A N   1 
ATOM   2640 C  CA  . ARG A  1 357 ? 36.60400  3.82200   43.07200 1.000 27.03000  ? 351 ARG A CA  1 
ATOM   2641 C  C   . ARG A  1 357 ? 37.87300  2.99200   42.98600 1.000 27.94000  ? 351 ARG A C   1 
ATOM   2642 O  O   . ARG A  1 357 ? 38.01300  2.12900   42.11400 1.000 27.13000  ? 351 ARG A O   1 
ATOM   2643 C  CB  . ARG A  1 357 ? 35.51700  3.11800   43.89100 1.000 31.58000  ? 351 ARG A CB  1 
ATOM   2644 C  CG  . ARG A  1 357 ? 34.89100  1.93600   43.28300 1.000 31.50000  ? 351 ARG A CG  1 
ATOM   2645 C  CD  . ARG A  1 357 ? 33.64000  1.55500   44.10800 1.000 39.77000  ? 351 ARG A CD  1 
ATOM   2646 N  NE  . ARG A  1 357 ? 33.25900  0.16900   43.87400 1.000 39.02000  ? 351 ARG A NE  1 
ATOM   2647 C  CZ  . ARG A  1 357 ? 32.39200  -0.22900  42.94900 1.000 32.47000  ? 351 ARG A CZ  1 
ATOM   2648 N  NH1 . ARG A  1 357 ? 31.69600  0.64300   42.22700 1.000 28.69000  ? 351 ARG A NH1 1 
ATOM   2649 N  NH2 . ARG A  1 357 ? 32.22800  -1.53300  42.73800 1.000 34.69000  ? 351 ARG A NH2 1 
ATOM   2650 N  N   . GLY A  1 358 ? 38.82200  3.30900   43.86200 1.000 26.58000  ? 352 GLY A N   1 
ATOM   2651 C  CA  . GLY A  1 358 ? 40.09100  2.61700   43.89100 1.000 30.98000  ? 352 GLY A CA  1 
ATOM   2652 C  C   . GLY A  1 358 ? 39.96500  1.32100   44.66100 1.000 38.51000  ? 352 GLY A C   1 
ATOM   2653 O  O   . GLY A  1 358 ? 39.33700  1.28000   45.72200 1.000 40.35000  ? 352 GLY A O   1 
ATOM   2654 N  N   . ILE B  1 2   ? 15.78700  -14.21900 44.95000 1.000 63.38000  ? -4  ILE B N   1 
ATOM   2655 C  CA  . ILE B  1 2   ? 15.53000  -13.11600 45.85800 1.000 58.77000  ? -4  ILE B CA  1 
ATOM   2656 C  C   . ILE B  1 2   ? 14.19800  -13.31600 46.58900 1.000 58.57000  ? -4  ILE B C   1 
ATOM   2657 O  O   . ILE B  1 2   ? 13.74000  -14.45200 46.78700 1.000 54.75000  ? -4  ILE B O   1 
ATOM   2658 C  CB  . ILE B  1 2   ? 15.56800  -11.75800 45.10900 1.000 65.54000  ? -4  ILE B CB  1 
ATOM   2659 C  CG1 . ILE B  1 2   ? 14.75900  -11.82700 43.81300 1.000 59.93000  ? -4  ILE B CG1 1 
ATOM   2660 C  CG2 . ILE B  1 2   ? 17.01400  -11.34200 44.81000 1.000 68.91000  ? -4  ILE B CG2 1 
ATOM   2661 C  CD1 . ILE B  1 2   ? 13.34700  -11.39400 43.95100 1.000 51.34000  ? -4  ILE B CD1 1 
ATOM   2662 N  N   . ASP B  1 3   ? 13.57600  -12.20500 46.97300 1.000 41.96000  ? -3  ASP B N   1 
ATOM   2663 C  CA  . ASP B  1 3   ? 12.46200  -12.21300 47.92000 1.000 39.01000  ? -3  ASP B CA  1 
ATOM   2664 C  C   . ASP B  1 3   ? 11.24000  -11.51900 47.32900 1.000 36.33000  ? -3  ASP B C   1 
ATOM   2665 O  O   . ASP B  1 3   ? 11.27400  -10.28700 47.14000 1.000 31.86000  ? -3  ASP B O   1 
ATOM   2666 C  CB  . ASP B  1 3   ? 12.90600  -11.52000 49.20700 1.000 36.80000  ? -3  ASP B CB  1 
ATOM   2667 C  CG  . ASP B  1 3   ? 11.89700  -11.65300 50.33400 1.000 40.51000  ? -3  ASP B CG  1 
ATOM   2668 O  OD1 . ASP B  1 3   ? 10.75300  -12.11500 50.08900 1.000 35.09000  ? -3  ASP B OD1 1 
ATOM   2669 O  OD2 . ASP B  1 3   ? 12.26400  -11.30300 51.48300 1.000 38.82000  ? -3  ASP B OD2 1 
ATOM   2670 N  N   . PRO B  1 4   ? 10.13800  -12.23500 47.04800 1.000 33.74000  ? -2  PRO B N   1 
ATOM   2671 C  CA  . PRO B  1 4   ? 8.94300   -11.57100 46.47900 1.000 30.00000  ? -2  PRO B CA  1 
ATOM   2672 C  C   . PRO B  1 4   ? 8.29700   -10.58500 47.42600 1.000 29.37000  ? -2  PRO B C   1 
ATOM   2673 O  O   . PRO B  1 4   ? 7.44300   -9.79500  47.00200 1.000 29.90000  ? -2  PRO B O   1 
ATOM   2674 C  CB  . PRO B  1 4   ? 7.98000   -12.74400 46.19000 1.000 30.46000  ? -2  PRO B CB  1 
ATOM   2675 C  CG  . PRO B  1 4   ? 8.81800   -13.98700 46.31800 1.000 34.81000  ? -2  PRO B CG  1 
ATOM   2676 C  CD  . PRO B  1 4   ? 9.87000   -13.65300 47.33900 1.000 37.51000  ? -2  PRO B CD  1 
ATOM   2677 N  N   . PHE B  1 5   ? 8.64800   -10.61400 48.70200 1.000 30.39000  ? -1  PHE B N   1 
ATOM   2678 C  CA  . PHE B  1 5   ? 7.95800   -9.78600  49.67600 1.000 30.58000  ? -1  PHE B CA  1 
ATOM   2679 C  C   . PHE B  1 5   ? 8.72900   -8.51600  50.01500 1.000 29.61000  ? -1  PHE B C   1 
ATOM   2680 O  O   . PHE B  1 5   ? 8.30800   -7.76700  50.90400 1.000 29.93000  ? -1  PHE B O   1 
ATOM   2681 C  CB  . PHE B  1 5   ? 7.66200   -10.62300 50.91100 1.000 33.32000  ? -1  PHE B CB  1 
ATOM   2682 C  CG  . PHE B  1 5   ? 6.89600   -11.88400 50.58300 1.000 34.66000  ? -1  PHE B CG  1 
ATOM   2683 C  CD1 . PHE B  1 5   ? 5.55200   -11.81600 50.24300 1.000 34.22000  ? -1  PHE B CD1 1 
ATOM   2684 C  CD2 . PHE B  1 5   ? 7.53300   -13.11000 50.53800 1.000 36.73000  ? -1  PHE B CD2 1 
ATOM   2685 C  CE1 . PHE B  1 5   ? 4.83100   -12.97900 49.90300 1.000 35.75000  ? -1  PHE B CE1 1 
ATOM   2686 C  CE2 . PHE B  1 5   ? 6.82800   -14.26600 50.20100 1.000 37.99000  ? -1  PHE B CE2 1 
ATOM   2687 C  CZ  . PHE B  1 5   ? 5.47000   -14.19200 49.88900 1.000 37.65000  ? -1  PHE B CZ  1 
ATOM   2688 N  N   . THR B  1 6   ? 9.82600   -8.23900  49.30100 1.000 28.55000  ? 0   THR B N   1 
ATOM   2689 C  CA  . THR B  1 6   ? 10.57100  -6.99500  49.48400 1.000 28.96000  ? 0   THR B CA  1 
ATOM   2690 C  C   . THR B  1 6   ? 10.83200  -6.29900  48.15300 1.000 25.80000  ? 0   THR B C   1 
ATOM   2691 O  O   . THR B  1 6   ? 11.82300  -5.56100  48.02400 1.000 27.67000  ? 0   THR B O   1 
ATOM   2692 C  CB  . THR B  1 6   ? 11.90500  -7.24600  50.20000 1.000 30.91000  ? 0   THR B CB  1 
ATOM   2693 O  OG1 . THR B  1 6   ? 12.76500  -8.02800  49.35100 1.000 30.06000  ? 0   THR B OG1 1 
ATOM   2694 C  CG2 . THR B  1 6   ? 11.69000  -7.96300  51.52900 1.000 32.19000  ? 0   THR B CG2 1 
ATOM   2695 N  N   . MET B  1 7   ? 9.97200   -6.53800  47.15300 1.000 24.74000  ? 1   MET B N   1 
ATOM   2696 C  CA  . MET B  1 7   ? 10.14000  -5.97100  45.81800 1.000 22.68000  ? 1   MET B CA  1 
ATOM   2697 C  C   . MET B  1 7   ? 9.90300   -4.46100  45.85200 1.000 26.20000  ? 1   MET B C   1 
ATOM   2698 O  O   . MET B  1 7   ? 9.09500   -3.95600  46.63800 1.000 22.37000  ? 1   MET B O   1 
ATOM   2699 C  CB  . MET B  1 7   ? 9.16500   -6.59900  44.82100 1.000 24.33000  ? 1   MET B CB  1 
ATOM   2700 C  CG  . MET B  1 7   ? 9.32200   -8.10900  44.60100 1.000 30.89000  ? 1   MET B CG  1 
ATOM   2701 S  SD  . MET B  1 7   ? 11.02900  -8.57300  44.21400 1.000 30.66000  ? 1   MET B SD  1 
ATOM   2702 C  CE  . MET B  1 7   ? 11.37200  -7.78800  42.64000 1.000 28.34000  ? 1   MET B CE  1 
ATOM   2703 N  N   . THR B  1 8   ? 10.60500  -3.73300  44.99100 1.000 20.73000  ? 2   THR B N   1 
ATOM   2704 C  CA  . THR B  1 8   ? 10.59400  -2.27700  45.08800 1.000 20.31000  ? 2   THR B CA  1 
ATOM   2705 C  C   . THR B  1 8   ? 10.53500  -1.66400  43.69700 1.000 19.10000  ? 2   THR B C   1 
ATOM   2706 O  O   . THR B  1 8   ? 10.90000  -2.31000  42.70700 1.000 19.66000  ? 2   THR B O   1 
ATOM   2707 C  CB  . THR B  1 8   ? 11.84600  -1.76400  45.81500 1.000 22.53000  ? 2   THR B CB  1 
ATOM   2708 O  OG1 . THR B  1 8   ? 13.00000  -2.07100  45.01900 1.000 21.76000  ? 2   THR B OG1 1 
ATOM   2709 C  CG2 . THR B  1 8   ? 11.98100  -2.37900  47.22500 1.000 22.73000  ? 2   THR B CG2 1 
ATOM   2710 N  N   . PRO B  1 9   ? 10.09600  -0.41100  43.58800 1.000 20.67000  ? 3   PRO B N   1 
ATOM   2711 C  CA  . PRO B  1 9   ? 10.09400  0.25000   42.26400 1.000 18.09000  ? 3   PRO B CA  1 
ATOM   2712 C  C   . PRO B  1 9   ? 11.45600  0.26600   41.59100 1.000 19.65000  ? 3   PRO B C   1 
ATOM   2713 O  O   . PRO B  1 9   ? 11.53800  0.25100   40.35200 1.000 17.31000  ? 3   PRO B O   1 
ATOM   2714 C  CB  . PRO B  1 9   ? 9.62000   1.67100   42.59500 1.000 21.34000  ? 3   PRO B CB  1 
ATOM   2715 C  CG  . PRO B  1 9   ? 8.71400   1.46500   43.80600 1.000 20.88000  ? 3   PRO B CG  1 
ATOM   2716 C  CD  . PRO B  1 9   ? 9.45100   0.41800   44.62200 1.000 20.77000  ? 3   PRO B CD  1 
ATOM   2717 N  N   . SER B  1 10  ? 12.52800  0.30100   42.37700 1.000 18.70000  ? 4   SER B N   1 
ATOM   2718 C  CA  . SER B  1 10  ? 13.88500  0.30200   41.82300 1.000 18.53000  ? 4   SER B CA  1 
ATOM   2719 C  C   . SER B  1 10  ? 14.20700  -0.99600  41.08700 1.000 23.04000  ? 4   SER B C   1 
ATOM   2720 O  O   . SER B  1 10  ? 15.20300  -1.05300  40.35100 1.000 19.59000  ? 4   SER B O   1 
ATOM   2721 C  CB  . SER B  1 10  ? 14.88600  0.55400   42.94300 1.000 24.19000  ? 4   SER B CB  1 
ATOM   2722 O  OG  . SER B  1 10  ? 14.99300  -0.56000  43.80900 1.000 22.73000  ? 4   SER B OG  1 
ATOM   2723 N  N   . GLU B  1 11  ? 13.36700  -2.01800  41.24500 1.000 17.94000  ? 5   GLU B N   1 
ATOM   2724 C  CA  . GLU B  1 11  ? 13.52700  -3.31800  40.60700 1.000 20.71000  ? 5   GLU B CA  1 
ATOM   2725 C  C   . GLU B  1 11  ? 12.57800  -3.51100  39.43200 1.000 17.03000  ? 5   GLU B C   1 
ATOM   2726 O  O   . GLU B  1 11  ? 12.42100  -4.64300  38.97100 1.000 17.09000  ? 5   GLU B O   1 
ATOM   2727 C  CB  . GLU B  1 11  ? 13.31400  -4.43900  41.64100 1.000 20.07000  ? 5   GLU B CB  1 
ATOM   2728 C  CG  . GLU B  1 11  ? 14.47200  -4.52900  42.65000 1.000 24.27000  ? 5   GLU B CG  1 
ATOM   2729 C  CD  . GLU B  1 11  ? 14.09800  -5.18900  43.97200 1.000 24.83000  ? 5   GLU B CD  1 
ATOM   2730 O  OE1 . GLU B  1 11  ? 13.13100  -4.72000  44.61300 1.000 27.44000  ? 5   GLU B OE1 1 
ATOM   2731 O  OE2 . GLU B  1 11  ? 14.78900  -6.16000  44.37700 1.000 28.51000  ? 5   GLU B OE2 1 
ATOM   2732 N  N   . ASP B  1 12  ? 11.94000  -2.43500  38.94800 1.000 17.26000  ? 6   ASP B N   1 
ATOM   2733 C  CA  . ASP B  1 12  ? 11.04600  -2.52300  37.78500 1.000 17.19000  ? 6   ASP B CA  1 
ATOM   2734 C  C   . ASP B  1 12  ? 11.86400  -2.48900  36.49200 1.000 18.03000  ? 6   ASP B C   1 
ATOM   2735 O  O   . ASP B  1 12  ? 12.28700  -1.43100  36.04500 1.000 18.36000  ? 6   ASP B O   1 
ATOM   2736 C  CB  . ASP B  1 12  ? 10.01700  -1.40800  37.82800 1.000 18.30000  ? 6   ASP B CB  1 
ATOM   2737 C  CG  . ASP B  1 12  ? 8.89200   -1.69400  38.83000 1.000 19.02000  ? 6   ASP B CG  1 
ATOM   2738 O  OD1 . ASP B  1 12  ? 8.64900   -2.87600  39.08100 1.000 19.62000  ? 6   ASP B OD1 1 
ATOM   2739 O  OD2 . ASP B  1 12  ? 8.28300   -0.72800  39.36500 1.000 17.76000  ? 6   ASP B OD2 1 
ATOM   2740 N  N   . PHE B  1 13  ? 12.07700  -3.66300  35.87900 1.000 18.19000  ? 7   PHE B N   1 
ATOM   2741 C  CA  . PHE B  1 13  ? 12.95100  -3.82100  34.72100 1.000 17.57000  ? 7   PHE B CA  1 
ATOM   2742 C  C   . PHE B  1 13  ? 12.24500  -4.53600  33.57400 1.000 16.24000  ? 7   PHE B C   1 
ATOM   2743 O  O   . PHE B  1 13  ? 11.36100  -5.37100  33.78500 1.000 18.94000  ? 7   PHE B O   1 
ATOM   2744 C  CB  . PHE B  1 13  ? 14.21200  -4.65700  35.04200 1.000 16.25000  ? 7   PHE B CB  1 
ATOM   2745 C  CG  . PHE B  1 13  ? 15.25900  -3.92200  35.81800 1.000 17.33000  ? 7   PHE B CG  1 
ATOM   2746 C  CD1 . PHE B  1 13  ? 16.21300  -3.17800  35.16000 1.000 18.11000  ? 7   PHE B CD1 1 
ATOM   2747 C  CD2 . PHE B  1 13  ? 15.30400  -4.00300  37.20900 1.000 19.18000  ? 7   PHE B CD2 1 
ATOM   2748 C  CE1 . PHE B  1 13  ? 17.22100  -2.52500  35.87100 1.000 19.26000  ? 7   PHE B CE1 1 
ATOM   2749 C  CE2 . PHE B  1 13  ? 16.29500  -3.34700  37.93400 1.000 19.83000  ? 7   PHE B CE2 1 
ATOM   2750 C  CZ  . PHE B  1 13  ? 17.26100  -2.60000  37.25200 1.000 23.55000  ? 7   PHE B CZ  1 
ATOM   2751 N  N   . VAL B  1 14  ? 12.71400  -4.26700  32.35600 1.000 17.41000  ? 8   VAL B N   1 
ATOM   2752 C  CA  . VAL B  1 14  ? 12.53000  -5.17200  31.22700 1.000 16.01000  ? 8   VAL B CA  1 
ATOM   2753 C  C   . VAL B  1 14  ? 13.92000  -5.65100  30.81700 1.000 18.18000  ? 8   VAL B C   1 
ATOM   2754 O  O   . VAL B  1 14  ? 14.87800  -4.86500  30.79700 1.000 15.84000  ? 8   VAL B O   1 
ATOM   2755 C  CB  . VAL B  1 14  ? 11.74800  -4.51700  30.05400 1.000 16.98000  ? 8   VAL B CB  1 
ATOM   2756 C  CG1 . VAL B  1 14  ? 12.36300  -3.19700  29.60300 1.000 18.69000  ? 8   VAL B CG1 1 
ATOM   2757 C  CG2 . VAL B  1 14  ? 11.64500  -5.47100  28.86000 1.000 16.76000  ? 8   VAL B CG2 1 
ATOM   2758 N  N   . VAL B  1 15  ? 14.04400  -6.95600  30.55000 1.000 15.61000  ? 9   VAL B N   1 
ATOM   2759 C  CA  . VAL B  1 15  ? 15.34700  -7.62600  30.49100 1.000 16.41000  ? 9   VAL B CA  1 
ATOM   2760 C  C   . VAL B  1 15  ? 15.40300  -8.50500  29.24800 1.000 20.21000  ? 9   VAL B C   1 
ATOM   2761 O  O   . VAL B  1 15  ? 14.45800  -9.24500  28.97200 1.000 20.61000  ? 9   VAL B O   1 
ATOM   2762 C  CB  . VAL B  1 15  ? 15.57200  -8.48500  31.75100 1.000 18.07000  ? 9   VAL B CB  1 
ATOM   2763 C  CG1 . VAL B  1 15  ? 16.84500  -9.37300  31.59400 1.000 18.00000  ? 9   VAL B CG1 1 
ATOM   2764 C  CG2 . VAL B  1 15  ? 15.60900  -7.60500  33.01500 1.000 18.73000  ? 9   VAL B CG2 1 
ATOM   2765 N  N   . THR B  1 16  ? 16.50800  -8.44700  28.51000 1.000 18.45000  ? 10  THR B N   1 
ATOM   2766 C  CA  . THR B  1 16  ? 16.71800  -9.38400  27.42000 1.000 18.71000  ? 10  THR B CA  1 
ATOM   2767 C  C   . THR B  1 16  ? 17.75200  -10.41600 27.83100 1.000 17.10000  ? 10  THR B C   1 
ATOM   2768 O  O   . THR B  1 16  ? 18.66600  -10.13800 28.62200 1.000 18.33000  ? 10  THR B O   1 
ATOM   2769 C  CB  . THR B  1 16  ? 17.11300  -8.67600  26.12200 1.000 18.26000  ? 10  THR B CB  1 
ATOM   2770 O  OG1 . THR B  1 16  ? 18.33000  -7.93400  26.29600 1.000 20.02000  ? 10  THR B OG1 1 
ATOM   2771 C  CG2 . THR B  1 16  ? 15.97700  -7.69300  25.68300 1.000 20.89000  ? 10  THR B CG2 1 
ATOM   2772 N  N   . ASP B  1 17  ? 17.60400  -11.62600 27.30500 1.000 17.29000  ? 11  ASP B N   1 
ATOM   2773 C  CA  . ASP B  1 17  ? 18.52900  -12.69700 27.65000 1.000 18.47000  ? 11  ASP B CA  1 
ATOM   2774 C  C   . ASP B  1 17  ? 19.02200  -13.37400 26.38400 1.000 18.99000  ? 11  ASP B C   1 
ATOM   2775 O  O   . ASP B  1 17  ? 18.39000  -13.30900 25.32500 1.000 20.41000  ? 11  ASP B O   1 
ATOM   2776 C  CB  . ASP B  1 17  ? 17.89200  -13.76800 28.57300 1.000 20.32000  ? 11  ASP B CB  1 
ATOM   2777 C  CG  . ASP B  1 17  ? 16.81800  -14.61700 27.86800 1.000 21.56000  ? 11  ASP B CG  1 
ATOM   2778 O  OD1 . ASP B  1 17  ? 15.63700  -14.18000 27.79000 1.000 23.39000  ? 11  ASP B OD1 1 
ATOM   2779 O  OD2 . ASP B  1 17  ? 17.13500  -15.71800 27.36500 1.000 22.23000  ? 11  ASP B OD2 1 
ATOM   2780 N  N   . ARG B  1 18  ? 20.14600  -14.05000 26.52800 1.000 20.14000  ? 12  ARG B N   1 
ATOM   2781 C  CA  . ARG B  1 18  ? 20.67000  -14.95200 25.50600 1.000 19.26000  ? 12  ARG B CA  1 
ATOM   2782 C  C   . ARG B  1 18  ? 20.80000  -16.30800 26.18000 1.000 19.44000  ? 12  ARG B C   1 
ATOM   2783 O  O   . ARG B  1 18  ? 21.67700  -16.49100 27.02900 1.000 20.91000  ? 12  ARG B O   1 
ATOM   2784 C  CB  . ARG B  1 18  ? 22.00400  -14.44200 24.96800 1.000 22.40000  ? 12  ARG B CB  1 
ATOM   2785 C  CG  . ARG B  1 18  ? 22.62700  -15.23800 23.82000 1.000 21.81000  ? 12  ARG B CG  1 
ATOM   2786 C  CD  . ARG B  1 18  ? 23.86600  -14.46800 23.29800 1.000 19.50000  ? 12  ARG B CD  1 
ATOM   2787 N  NE  . ARG B  1 18  ? 23.48700  -13.13100 22.82700 1.000 23.23000  ? 12  ARG B NE  1 
ATOM   2788 C  CZ  . ARG B  1 18  ? 23.03200  -12.87000 21.60800 1.000 24.79000  ? 12  ARG B CZ  1 
ATOM   2789 N  NH1 . ARG B  1 18  ? 22.96000  -13.81900 20.68200 1.000 17.59000  ? 12  ARG B NH1 1 
ATOM   2790 N  NH2 . ARG B  1 18  ? 22.61700  -11.63200 21.31400 1.000 21.32000  ? 12  ARG B NH2 1 
ATOM   2791 N  N   . GLY B  1 19  ? 19.91100  -17.24500 25.83500 1.000 20.04000  ? 13  GLY B N   1 
ATOM   2792 C  CA  . GLY B  1 19  ? 19.95400  -18.54800 26.47600 1.000 25.65000  ? 13  GLY B CA  1 
ATOM   2793 C  C   . GLY B  1 19  ? 19.77200  -18.47900 27.97300 1.000 21.96000  ? 13  GLY B C   1 
ATOM   2794 O  O   . GLY B  1 19  ? 20.34600  -19.29300 28.70900 1.000 25.05000  ? 13  GLY B O   1 
ATOM   2795 N  N   . GLY B  1 20  ? 19.01900  -17.50900 28.44400 1.000 22.85000  ? 14  GLY B N   1 
ATOM   2796 C  CA  . GLY B  1 20  ? 18.76900  -17.34600 29.85400 1.000 23.78000  ? 14  GLY B CA  1 
ATOM   2797 C  C   . GLY B  1 20  ? 19.79300  -16.51400 30.56900 1.000 23.60000  ? 14  GLY B C   1 
ATOM   2798 O  O   . GLY B  1 20  ? 19.59600  -16.20800 31.74700 1.000 24.16000  ? 14  GLY B O   1 
ATOM   2799 N  N   . ILE B  1 21  ? 20.87900  -16.14800 29.89600 1.000 17.21000  ? 15  ILE B N   1 
ATOM   2800 C  CA  . ILE B  1 21  ? 21.91900  -15.30100 30.47400 1.000 21.77000  ? 15  ILE B CA  1 
ATOM   2801 C  C   . ILE B  1 21  ? 21.53700  -13.85700 30.21500 1.000 17.92000  ? 15  ILE B C   1 
ATOM   2802 O  O   . ILE B  1 21  ? 21.21800  -13.50300 29.07900 1.000 16.17000  ? 15  ILE B O   1 
ATOM   2803 C  CB  . ILE B  1 21  ? 23.28800  -15.61600 29.85100 1.000 18.86000  ? 15  ILE B CB  1 
ATOM   2804 C  CG1 . ILE B  1 21  ? 23.59000  -17.10700 29.99800 1.000 18.81000  ? 15  ILE B CG1 1 
ATOM   2805 C  CG2 . ILE B  1 21  ? 24.40000  -14.79100 30.51000 1.000 17.08000  ? 15  ILE B CG2 1 
ATOM   2806 C  CD1 . ILE B  1 21  ? 24.62300  -17.58600 29.04700 1.000 18.77000  ? 15  ILE B CD1 1 
ATOM   2807 N  N   . VAL B  1 22  ? 21.57900  -13.02000 31.25400 1.000 16.48000  ? 16  VAL B N   1 
ATOM   2808 C  CA  . VAL B  1 22  ? 21.17100  -11.61700 31.07600 1.000 18.43000  ? 16  VAL B CA  1 
ATOM   2809 C  C   . VAL B  1 22  ? 22.08200  -10.90700 30.07300 1.000 18.18000  ? 16  VAL B C   1 
ATOM   2810 O  O   . VAL B  1 22  ? 23.31500  -10.89700 30.20300 1.000 17.03000  ? 16  VAL B O   1 
ATOM   2811 C  CB  . VAL B  1 22  ? 21.14100  -10.87200 32.41800 1.000 17.80000  ? 16  VAL B CB  1 
ATOM   2812 C  CG1 . VAL B  1 22  ? 20.88100  -9.35600  32.17700 1.000 19.24000  ? 16  VAL B CG1 1 
ATOM   2813 C  CG2 . VAL B  1 22  ? 20.05100  -11.43100 33.31100 1.000 21.68000  ? 16  VAL B CG2 1 
ATOM   2814 N  N   . GLU B  1 23  ? 21.46100  -10.29100 29.06600 1.000 16.49000  ? 17  GLU B N   1 
ATOM   2815 C  CA  . GLU B  1 23  ? 22.18300  -9.47900  28.10300 1.000 16.45000  ? 17  GLU B CA  1 
ATOM   2816 C  C   . GLU B  1 23  ? 22.12300  -8.02900  28.58000 1.000 18.43000  ? 17  GLU B C   1 
ATOM   2817 O  O   . GLU B  1 23  ? 23.10800  -7.50600  29.12200 1.000 15.66000  ? 17  GLU B O   1 
ATOM   2818 C  CB  . GLU B  1 23  ? 21.59100  -9.62400  26.69800 1.000 17.66000  ? 17  GLU B CB  1 
ATOM   2819 C  CG  . GLU B  1 23  ? 22.40900  -8.91700  25.63000 1.000 22.19000  ? 17  GLU B CG  1 
ATOM   2820 C  CD  . GLU B  1 23  ? 23.37900  -9.84800  24.92600 1.000 19.35000  ? 17  GLU B CD  1 
ATOM   2821 O  OE1 . GLU B  1 23  ? 22.88400  -10.73800 24.18900 1.000 20.57000  ? 17  GLU B OE1 1 
ATOM   2822 O  OE2 . GLU B  1 23  ? 24.63200  -9.68900  25.08700 1.000 19.83000  ? 17  GLU B OE2 1 
ATOM   2823 N  N   . ASN B  1 24  ? 20.96500  -7.38700  28.40000 1.000 15.94000  ? 18  ASN B N   1 
ATOM   2824 C  CA  . ASN B  1 24  ? 20.74200  -6.00900  28.81200 1.000 14.02000  ? 18  ASN B CA  1 
ATOM   2825 C  C   . ASN B  1 24  ? 19.58700  -5.93400  29.79800 1.000 15.25000  ? 18  ASN B C   1 
ATOM   2826 O  O   . ASN B  1 24  ? 18.65800  -6.74600  29.73800 1.000 17.10000  ? 18  ASN B O   1 
ATOM   2827 C  CB  . ASN B  1 24  ? 20.38800  -5.11300  27.62700 1.000 17.48000  ? 18  ASN B CB  1 
ATOM   2828 C  CG  . ASN B  1 24  ? 21.39200  -5.21300  26.50600 1.000 18.96000  ? 18  ASN B CG  1 
ATOM   2829 O  OD1 . ASN B  1 24  ? 22.60000  -5.28200  26.74200 1.000 15.29000  ? 18  ASN B OD1 1 
ATOM   2830 N  ND2 . ASN B  1 24  ? 20.89200  -5.21700  25.26500 1.000 21.32000  ? 18  ASN B ND2 1 
ATOM   2831 N  N   . SER B  1 25  ? 19.58600  -4.89600  30.65000 1.000 12.47000  ? 19  SER B N   1 
ATOM   2832 C  CA  . SER B  1 25  ? 18.38100  -4.61400  31.42800 1.000 15.15000  ? 19  SER B CA  1 
ATOM   2833 C  C   . SER B  1 25  ? 18.09200  -3.12400  31.35500 1.000 15.64000  ? 19  SER B C   1 
ATOM   2834 O  O   . SER B  1 25  ? 19.01000  -2.31000  31.21000 1.000 14.61000  ? 19  SER B O   1 
ATOM   2835 C  CB  . SER B  1 25  ? 18.49600  -5.08700  32.88900 1.000 19.37000  ? 19  SER B CB  1 
ATOM   2836 O  OG  . SER B  1 25  ? 19.43300  -4.35300  33.63000 1.000 17.16000  ? 19  SER B OG  1 
ATOM   2837 N  N   . HIS B  1 26  ? 16.80400  -2.78500  31.46900 1.000 14.06000  ? 20  HIS B N   1 
ATOM   2838 C  CA  . HIS B  1 26  ? 16.31000  -1.42800  31.22300 1.000 14.31000  ? 20  HIS B CA  1 
ATOM   2839 C  C   . HIS B  1 26  ? 15.29600  -1.08200  32.31200 1.000 12.71000  ? 20  HIS B C   1 
ATOM   2840 O  O   . HIS B  1 26  ? 14.32600  -1.83000  32.50800 1.000 14.68000  ? 20  HIS B O   1 
ATOM   2841 C  CB  . HIS B  1 26  ? 15.61600  -1.33100  29.84900 1.000 14.56000  ? 20  HIS B CB  1 
ATOM   2842 C  CG  . HIS B  1 26  ? 16.40100  -1.91100  28.70700 1.000 15.28000  ? 20  HIS B CG  1 
ATOM   2843 N  ND1 . HIS B  1 26  ? 17.03400  -1.12000  27.77600 1.000 13.12000  ? 20  HIS B ND1 1 
ATOM   2844 C  CD2 . HIS B  1 26  ? 16.61300  -3.19600  28.31400 1.000 14.14000  ? 20  HIS B CD2 1 
ATOM   2845 C  CE1 . HIS B  1 26  ? 17.64500  -1.88200  26.88400 1.000 17.06000  ? 20  HIS B CE1 1 
ATOM   2846 N  NE2 . HIS B  1 26  ? 17.39700  -3.15100  27.18200 1.000 15.44000  ? 20  HIS B NE2 1 
ATOM   2847 N  N   . ARG B  1 27  ? 15.48900  0.05600   32.98300 1.000 14.84000  ? 21  ARG B N   1 
ATOM   2848 C  CA  . ARG B  1 27  ? 14.54400  0.48900   34.00900 1.000 14.46000  ? 21  ARG B CA  1 
ATOM   2849 C  C   . ARG B  1 27  ? 13.28700  1.08700   33.37800 1.000 15.85000  ? 21  ARG B C   1 
ATOM   2850 O  O   . ARG B  1 27  ? 13.36600  1.83900   32.40600 1.000 15.24000  ? 21  ARG B O   1 
ATOM   2851 C  CB  . ARG B  1 27  ? 15.19600  1.54400   34.91900 1.000 16.51000  ? 21  ARG B CB  1 
ATOM   2852 C  CG  . ARG B  1 27  ? 16.03000  0.95300   36.06500 1.000 16.64000  ? 21  ARG B CG  1 
ATOM   2853 C  CD  . ARG B  1 27  ? 15.16000  0.03900   36.95800 1.000 18.21000  ? 21  ARG B CD  1 
ATOM   2854 N  NE  . ARG B  1 27  ? 13.83300  0.63000   37.15100 1.000 19.16000  ? 21  ARG B NE  1 
ATOM   2855 C  CZ  . ARG B  1 27  ? 13.57900  1.70500   37.88400 1.000 20.55000  ? 21  ARG B CZ  1 
ATOM   2856 N  NH1 . ARG B  1 27  ? 14.52400  2.28900   38.61100 1.000 15.82000  ? 21  ARG B NH1 1 
ATOM   2857 N  NH2 . ARG B  1 27  ? 12.34600  2.21900   37.87000 1.000 19.82000  ? 21  ARG B NH2 1 
ATOM   2858 N  N   . VAL B  1 28  ? 12.13600  0.76800   33.96500 1.000 15.90000  ? 22  VAL B N   1 
ATOM   2859 C  CA  . VAL B  1 28  ? 10.83000  1.18400   33.46900 1.000 16.84000  ? 22  VAL B CA  1 
ATOM   2860 C  C   . VAL B  1 28  ? 10.23000  2.14300   34.47900 1.000 15.26000  ? 22  VAL B C   1 
ATOM   2861 O  O   . VAL B  1 28  ? 10.22600  1.86900   35.68800 1.000 14.65000  ? 22  VAL B O   1 
ATOM   2862 C  CB  . VAL B  1 28  ? 9.87300   -0.00600  33.24100 1.000 14.61000  ? 22  VAL B CB  1 
ATOM   2863 C  CG1 . VAL B  1 28  ? 8.50100   0.46600   32.70100 1.000 15.20000  ? 22  VAL B CG1 1 
ATOM   2864 C  CG2 . VAL B  1 28  ? 10.46400  -1.02100  32.25000 1.000 18.91000  ? 22  VAL B CG2 1 
ATOM   2865 N  N   . HIS B  1 29  ? 9.63600   3.21300   33.96900 1.000 13.29000  ? 23  HIS B N   1 
ATOM   2866 C  CA  . HIS B  1 29  ? 8.77400   4.09600   34.73800 1.000 14.52000  ? 23  HIS B CA  1 
ATOM   2867 C  C   . HIS B  1 29  ? 7.42200   4.16000   34.05200 1.000 17.08000  ? 23  HIS B C   1 
ATOM   2868 O  O   . HIS B  1 29  ? 7.35400   4.24400   32.82200 1.000 15.32000  ? 23  HIS B O   1 
ATOM   2869 C  CB  . HIS B  1 29  ? 9.37100   5.49600   34.79900 1.000 15.06000  ? 23  HIS B CB  1 
ATOM   2870 C  CG  . HIS B  1 29  ? 10.78400  5.52500   35.28200 1.000 16.47000  ? 23  HIS B CG  1 
ATOM   2871 N  ND1 . HIS B  1 29  ? 11.10900  5.45100   36.62000 1.000 16.62000  ? 23  HIS B ND1 1 
ATOM   2872 C  CD2 . HIS B  1 29  ? 11.96100  5.66400   34.61500 1.000 17.32000  ? 23  HIS B CD2 1 
ATOM   2873 C  CE1 . HIS B  1 29  ? 12.42400  5.50500   36.75900 1.000 17.63000  ? 23  HIS B CE1 1 
ATOM   2874 N  NE2 . HIS B  1 29  ? 12.96400  5.64700   35.55900 1.000 16.34000  ? 23  HIS B NE2 1 
ATOM   2875 N  N   . ALA B  1 30  ? 6.34700   4.11800   34.83300 1.000 15.66000  ? 24  ALA B N   1 
ATOM   2876 C  CA  . ALA B  1 30  ? 5.02400   4.25200   34.23400 1.000 13.56000  ? 24  ALA B CA  1 
ATOM   2877 C  C   . ALA B  1 30  ? 4.04500   4.84900   35.22300 1.000 16.45000  ? 24  ALA B C   1 
ATOM   2878 O  O   . ALA B  1 30  ? 4.15300   4.65100   36.43600 1.000 17.20000  ? 24  ALA B O   1 
ATOM   2879 C  CB  . ALA B  1 30  ? 4.45000   2.89800   33.75000 1.000 12.01000  ? 24  ALA B CB  1 
ATOM   2880 N  N   . ALA B  1 31  ? 3.02900   5.51100   34.66900 1.000 15.73000  ? 25  ALA B N   1 
ATOM   2881 C  CA  . ALA B  1 31  ? 1.94100   6.07300   35.44600 1.000 18.16000  ? 25  ALA B CA  1 
ATOM   2882 C  C   . ALA B  1 31  ? 0.63800   5.75300   34.74000 1.000 17.13000  ? 25  ALA B C   1 
ATOM   2883 O  O   . ALA B  1 31  ? 0.56100   5.84300   33.51400 1.000 16.80000  ? 25  ALA B O   1 
ATOM   2884 C  CB  . ALA B  1 31  ? 2.09000   7.59900   35.58300 1.000 16.00000  ? 25  ALA B CB  1 
ATOM   2885 N  N   . VAL B  1 32  ? -0.36000  5.34500   35.52000 1.000 16.52000  ? 26  VAL B N   1 
ATOM   2886 C  CA  . VAL B  1 32  ? -1.71900  5.14100   35.04700 1.000 14.43000  ? 26  VAL B CA  1 
ATOM   2887 C  C   . VAL B  1 32  ? -2.58500  6.04100   35.92000 1.000 17.69000  ? 26  VAL B C   1 
ATOM   2888 O  O   . VAL B  1 32  ? -2.58600  5.89900   37.14700 1.000 18.88000  ? 26  VAL B O   1 
ATOM   2889 C  CB  . VAL B  1 32  ? -2.15500  3.67000   35.13900 1.000 14.77000  ? 26  VAL B CB  1 
ATOM   2890 C  CG1 . VAL B  1 32  ? -3.54700  3.52500   34.59400 1.000 21.12000  ? 26  VAL B CG1 1 
ATOM   2891 C  CG2 . VAL B  1 32  ? -1.15800  2.74000   34.39800 1.000 16.12000  ? 26  VAL B CG2 1 
ATOM   2892 N  N   . VAL B  1 33  ? -3.29600  6.97900   35.30200 1.000 15.96000  ? 27  VAL B N   1 
ATOM   2893 C  CA  . VAL B  1 33  ? -4.01700  7.98800   36.06900 1.000 16.85000  ? 27  VAL B CA  1 
ATOM   2894 C  C   . VAL B  1 33  ? -5.44700  8.07000   35.58200 1.000 18.40000  ? 27  VAL B C   1 
ATOM   2895 O  O   . VAL B  1 33  ? -5.76600  7.68700   34.45600 1.000 17.99000  ? 27  VAL B O   1 
ATOM   2896 C  CB  . VAL B  1 33  ? -3.37600  9.38400   35.96200 1.000 16.85000  ? 27  VAL B CB  1 
ATOM   2897 C  CG1 . VAL B  1 33  ? -1.88400  9.31700   36.36400 1.000 15.39000  ? 27  VAL B CG1 1 
ATOM   2898 C  CG2 . VAL B  1 33  ? -3.51400  9.92000   34.52900 1.000 17.14000  ? 27  VAL B CG2 1 
ATOM   2899 N  N   . ASP B  1 34  ? -6.30200  8.65800   36.42800 1.000 17.77000  ? 28  ASP B N   1 
ATOM   2900 C  CA  . ASP B  1 34  ? -7.67400  8.88800   36.01000 1.000 18.88000  ? 28  ASP B CA  1 
ATOM   2901 C  C   . ASP B  1 34  ? -7.79400  10.26300  35.33100 1.000 25.72000  ? 28  ASP B C   1 
ATOM   2902 O  O   . ASP B  1 34  ? -6.80400  10.98300  35.12600 1.000 20.63000  ? 28  ASP B O   1 
ATOM   2903 C  CB  . ASP B  1 34  ? -8.62200  8.71100   37.20000 1.000 24.60000  ? 28  ASP B CB  1 
ATOM   2904 C  CG  . ASP B  1 34  ? -8.63400  9.91300   38.17800 1.000 26.76000  ? 28  ASP B CG  1 
ATOM   2905 O  OD1 . ASP B  1 34  ? -7.98900  10.97600  37.94400 1.000 22.82000  ? 28  ASP B OD1 1 
ATOM   2906 O  OD2 . ASP B  1 34  ? -9.31300  9.77100   39.21900 1.000 26.94000  ? 28  ASP B OD2 1 
ATOM   2907 N  N   . ALA B  1 35  ? -9.03800  10.64400  34.99000 1.000 23.12000  ? 29  ALA B N   1 
ATOM   2908 C  CA  . ALA B  1 35  ? -9.24400  11.85600  34.19600 1.000 23.56000  ? 29  ALA B CA  1 
ATOM   2909 C  C   . ALA B  1 35  ? -8.89600  13.14700  34.94600 1.000 25.91000  ? 29  ALA B C   1 
ATOM   2910 O  O   . ALA B  1 35  ? -8.77000  14.20000  34.31100 1.000 24.88000  ? 29  ALA B O   1 
ATOM   2911 C  CB  . ALA B  1 35  ? -10.69800 11.91900  33.72200 1.000 25.69000  ? 29  ALA B CB  1 
ATOM   2912 N  N   . LYS B  1 36  ? -8.77600  13.09600  36.27200 1.000 25.41000  ? 30  LYS B N   1 
ATOM   2913 C  CA  . LYS B  1 36  ? -8.33900  14.21000  37.10100 1.000 24.31000  ? 30  LYS B CA  1 
ATOM   2914 C  C   . LYS B  1 36  ? -6.85200  14.12600  37.45100 1.000 27.92000  ? 30  LYS B C   1 
ATOM   2915 O  O   . LYS B  1 36  ? -6.32900  14.98600  38.17300 1.000 27.78000  ? 30  LYS B O   1 
ATOM   2916 C  CB  . LYS B  1 36  ? -9.18500  14.25300  38.37600 1.000 28.15000  ? 30  LYS B CB  1 
ATOM   2917 C  CG  . LYS B  1 36  ? -10.62400 14.71200  38.09200 1.000 30.91000  ? 30  LYS B CG  1 
ATOM   2918 C  CD  . LYS B  1 36  ? -11.25600 15.41600  39.30800 1.000 41.32000  ? 30  LYS B CD  1 
ATOM   2919 C  CE  . LYS B  1 36  ? -12.44200 16.34900  38.93500 1.000 49.06000  ? 30  LYS B CE  1 
ATOM   2920 N  NZ  . LYS B  1 36  ? -12.02000 17.73600  38.51000 1.000 45.56000  ? 30  LYS B NZ  1 
ATOM   2921 N  N   . GLY B  1 37  ? -6.17000  13.12000  36.95200 1.000 22.65000  ? 31  GLY B N   1 
ATOM   2922 C  CA  . GLY B  1 37  ? -4.76700  12.92400  37.23700 1.000 21.90000  ? 31  GLY B CA  1 
ATOM   2923 C  C   . GLY B  1 37  ? -4.45800  12.08900  38.45200 1.000 22.90000  ? 31  GLY B C   1 
ATOM   2924 O  O   . GLY B  1 37  ? -3.27300  11.86500  38.73400 1.000 21.96000  ? 31  GLY B O   1 
ATOM   2925 N  N   . ARG B  1 38  ? -5.46900  11.62400  39.18800 1.000 20.95000  ? 32  ARG B N   1 
ATOM   2926 C  CA  . ARG B  1 38  ? -5.20300  10.77100  40.33600 1.000 20.44000  ? 32  ARG B CA  1 
ATOM   2927 C  C   . ARG B  1 38  ? -4.41000  9.53700   39.91200 1.000 22.94000  ? 32  ARG B C   1 
ATOM   2928 O  O   . ARG B  1 38  ? -4.73900  8.87000   38.93000 1.000 22.69000  ? 32  ARG B O   1 
ATOM   2929 C  CB  . ARG B  1 38  ? -6.50700  10.34200  41.00300 1.000 28.72000  ? 32  ARG B CB  1 
ATOM   2930 C  CG  . ARG B  1 38  ? -6.31500  9.25600   42.05400 1.000 32.68000  ? 32  ARG B CG  1 
ATOM   2931 C  CD  . ARG B  1 38  ? -7.57600  9.05400   42.88200 1.000 39.82000  ? 32  ARG B CD  1 
ATOM   2932 N  NE  . ARG B  1 38  ? -8.60600  8.32400   42.15100 1.000 42.76000  ? 32  ARG B NE  1 
ATOM   2933 C  CZ  . ARG B  1 38  ? -8.85900  7.02600   42.29900 1.000 47.66000  ? 32  ARG B CZ  1 
ATOM   2934 N  NH1 . ARG B  1 38  ? -8.13600  6.26600   43.11500 1.000 46.88000  ? 32  ARG B NH1 1 
ATOM   2935 N  NH2 . ARG B  1 38  ? -9.86200  6.47600   41.61000 1.000 44.26000  ? 32  ARG B NH2 1 
ATOM   2936 N  N   . LEU B  1 39  ? -3.37800  9.21200   40.67200 1.000 23.60000  ? 33  LEU B N   1 
ATOM   2937 C  CA  . LEU B  1 39  ? -2.51300  8.10300   40.30800 1.000 22.65000  ? 33  LEU B CA  1 
ATOM   2938 C  C   . LEU B  1 39  ? -3.16200  6.78400   40.71700 1.000 23.24000  ? 33  LEU B C   1 
ATOM   2939 O  O   . LEU B  1 39  ? -3.45100  6.58000   41.89900 1.000 26.69000  ? 33  LEU B O   1 
ATOM   2940 C  CB  . LEU B  1 39  ? -1.15700  8.26200   40.98300 1.000 22.12000  ? 33  LEU B CB  1 
ATOM   2941 C  CG  . LEU B  1 39  ? -0.15500  7.17200   40.59800 1.000 21.81000  ? 33  LEU B CG  1 
ATOM   2942 C  CD1 . LEU B  1 39  ? 0.27600   7.35400   39.13000 1.000 19.15000  ? 33  LEU B CD1 1 
ATOM   2943 C  CD2 . LEU B  1 39  ? 1.04200   7.20300   41.51400 1.000 25.38000  ? 33  LEU B CD2 1 
ATOM   2944 N  N   . LEU B  1 40  ? -3.38100  5.88700   39.75100 1.000 18.92000  ? 34  LEU B N   1 
ATOM   2945 C  CA  . LEU B  1 40  ? -4.03400  4.60300   40.00300 1.000 24.19000  ? 34  LEU B CA  1 
ATOM   2946 C  C   . LEU B  1 40  ? -3.03200  3.46000   40.13100 1.000 23.21000  ? 34  LEU B C   1 
ATOM   2947 O  O   . LEU B  1 40  ? -3.11200  2.67300   41.07000 1.000 23.09000  ? 34  LEU B O   1 
ATOM   2948 C  CB  . LEU B  1 40  ? -5.03600  4.27600   38.88200 1.000 19.30000  ? 34  LEU B CB  1 
ATOM   2949 C  CG  . LEU B  1 40  ? -6.14400  5.29700   38.64700 1.000 26.32000  ? 34  LEU B CG  1 
ATOM   2950 C  CD1 . LEU B  1 40  ? -7.06000  4.84300   37.50100 1.000 27.68000  ? 34  LEU B CD1 1 
ATOM   2951 C  CD2 . LEU B  1 40  ? -6.97300  5.48500   39.91400 1.000 27.48000  ? 34  LEU B CD2 1 
ATOM   2952 N  N   . TYR B  1 41  ? -2.09700  3.35700   39.19000 1.000 19.17000  ? 35  TYR B N   1 
ATOM   2953 C  CA  . TYR B  1 41  ? -1.09300  2.31300   39.17800 1.000 20.05000  ? 35  TYR B CA  1 
ATOM   2954 C  C   . TYR B  1 41  ? 0.22700   2.93700   38.76400 1.000 17.81000  ? 35  TYR B C   1 
ATOM   2955 O  O   . TYR B  1 41  ? 0.25200   3.97700   38.11700 1.000 16.50000  ? 35  TYR B O   1 
ATOM   2956 C  CB  . TYR B  1 41  ? -1.44300  1.16600   38.21400 1.000 19.49000  ? 35  TYR B CB  1 
ATOM   2957 C  CG  . TYR B  1 41  ? -2.74700  0.56900   38.55400 1.000 20.92000  ? 35  TYR B CG  1 
ATOM   2958 C  CD1 . TYR B  1 41  ? -3.91600  1.12900   38.05600 1.000 19.58000  ? 35  TYR B CD1 1 
ATOM   2959 C  CD2 . TYR B  1 41  ? -2.83700  -0.53000  39.40700 1.000 27.37000  ? 35  TYR B CD2 1 
ATOM   2960 C  CE1 . TYR B  1 41  ? -5.14900  0.60500   38.40300 1.000 25.61000  ? 35  TYR B CE1 1 
ATOM   2961 C  CE2 . TYR B  1 41  ? -4.09000  -1.08600  39.74900 1.000 25.31000  ? 35  TYR B CE2 1 
ATOM   2962 C  CZ  . TYR B  1 41  ? -5.22200  -0.51300  39.23200 1.000 27.63000  ? 35  TYR B CZ  1 
ATOM   2963 O  OH  . TYR B  1 41  ? -6.46000  -1.00000  39.56600 1.000 25.83000  ? 35  TYR B OH  1 
ATOM   2964 N  N   . ALA B  1 42  ? 1.32500   2.26800   39.10100 1.000 19.20000  ? 36  ALA B N   1 
ATOM   2965 C  CA  . ALA B  1 42  ? 2.63200   2.82800   38.77000 1.000 16.36000  ? 36  ALA B CA  1 
ATOM   2966 C  C   . ALA B  1 42  ? 3.67500   1.72900   38.57300 1.000 15.66000  ? 36  ALA B C   1 
ATOM   2967 O  O   . ALA B  1 42  ? 3.55300   0.61300   39.10100 1.000 17.05000  ? 36  ALA B O   1 
ATOM   2968 C  CB  . ALA B  1 42  ? 3.09900   3.77700   39.86000 1.000 17.12000  ? 36  ALA B CB  1 
ATOM   2969 N  N   . LEU B  1 43  ? 4.68100   2.06100   37.78300 1.000 15.73000  ? 37  LEU B N   1 
ATOM   2970 C  CA  . LEU B  1 43  ? 5.94600   1.35800   37.75900 1.000 15.88000  ? 37  LEU B CA  1 
ATOM   2971 C  C   . LEU B  1 43  ? 7.06400   2.36000   37.99800 1.000 15.73000  ? 37  LEU B C   1 
ATOM   2972 O  O   . LEU B  1 43  ? 6.98100   3.52400   37.57500 1.000 14.70000  ? 37  LEU B O   1 
ATOM   2973 C  CB  . LEU B  1 43  ? 6.18500   0.65700   36.42100 1.000 14.85000  ? 37  LEU B CB  1 
ATOM   2974 C  CG  . LEU B  1 43  ? 5.19300   -0.44100  36.00500 1.000 17.31000  ? 37  LEU B CG  1 
ATOM   2975 C  CD1 . LEU B  1 43  ? 5.44400   -0.87800  34.55900 1.000 15.56000  ? 37  LEU B CD1 1 
ATOM   2976 C  CD2 . LEU B  1 43  ? 5.26200   -1.59200  36.97300 1.000 17.19000  ? 37  LEU B CD2 1 
ATOM   2977 N  N   . GLY B  1 44  ? 8.11600   1.90200   38.66600 1.000 15.39000  ? 38  GLY B N   1 
ATOM   2978 C  CA  . GLY B  1 44  ? 9.29600   2.77400   38.83000 1.000 15.29000  ? 38  GLY B CA  1 
ATOM   2979 C  C   . GLY B  1 44  ? 8.91500   4.06300   39.52800 1.000 17.60000  ? 38  GLY B C   1 
ATOM   2980 O  O   . GLY B  1 44  ? 8.22800   4.04200   40.55200 1.000 18.07000  ? 38  GLY B O   1 
ATOM   2981 N  N   . ASN B  1 45  ? 9.34600   5.22100   38.97000 1.000 15.99000  ? 39  ASN B N   1 
ATOM   2982 C  CA  . ASN B  1 45  ? 8.99700   6.52300   39.52800 1.000 16.76000  ? 39  ASN B CA  1 
ATOM   2983 C  C   . ASN B  1 45  ? 7.93800   7.17300   38.65300 1.000 17.24000  ? 39  ASN B C   1 
ATOM   2984 O  O   . ASN B  1 45  ? 8.27000   7.71700   37.59900 1.000 14.32000  ? 39  ASN B O   1 
ATOM   2985 C  CB  . ASN B  1 45  ? 10.23300  7.41700   39.62100 1.000 18.53000  ? 39  ASN B CB  1 
ATOM   2986 C  CG  . ASN B  1 45  ? 9.91200   8.83000   40.11000 1.000 20.25000  ? 39  ASN B CG  1 
ATOM   2987 O  OD1 . ASN B  1 45  ? 8.79200   9.15200   40.54900 1.000 19.33000  ? 39  ASN B OD1 1 
ATOM   2988 N  ND2 . ASN B  1 45  ? 10.90900  9.67800   40.03000 1.000 17.57000  ? 39  ASN B ND2 1 
ATOM   2989 N  N   . PRO B  1 46  ? 6.65900   7.14300   39.03900 1.000 16.30000  ? 40  PRO B N   1 
ATOM   2990 C  CA  . PRO B  1 46  ? 5.61300   7.65900   38.15400 1.000 15.52000  ? 40  PRO B CA  1 
ATOM   2991 C  C   . PRO B  1 46  ? 5.63500   9.17200   38.01000 1.000 15.05000  ? 40  PRO B C   1 
ATOM   2992 O  O   . PRO B  1 46  ? 4.90400   9.66700   37.15200 1.000 15.79000  ? 40  PRO B O   1 
ATOM   2993 C  CB  . PRO B  1 46  ? 4.31300   7.18000   38.82600 1.000 15.20000  ? 40  PRO B CB  1 
ATOM   2994 C  CG  . PRO B  1 46  ? 4.66900   7.05000   40.27400 1.000 15.36000  ? 40  PRO B CG  1 
ATOM   2995 C  CD  . PRO B  1 46  ? 6.10000   6.47900   40.23200 1.000 14.74000  ? 40  PRO B CD  1 
ATOM   2996 N  N   . THR B  1 47  ? 6.42900   9.90300   38.81600 1.000 16.33000  ? 41  THR B N   1 
ATOM   2997 C  CA  . THR B  1 47  ? 6.52600   11.36200  38.71800 1.000 15.72000  ? 41  THR B CA  1 
ATOM   2998 C  C   . THR B  1 47  ? 7.89100   11.81600  38.19400 1.000 15.12000  ? 41  THR B C   1 
ATOM   2999 O  O   . THR B  1 47  ? 8.26000   12.99000  38.33900 1.000 18.90000  ? 41  THR B O   1 
ATOM   3000 C  CB  . THR B  1 47  ? 6.22700   12.02500  40.06200 1.000 17.25000  ? 41  THR B CB  1 
ATOM   3001 O  OG1 . THR B  1 47  ? 7.21600   11.64900  41.03600 1.000 22.24000  ? 41  THR B OG1 1 
ATOM   3002 C  CG2 . THR B  1 47  ? 4.81200   11.69200  40.56000 1.000 16.15000  ? 41  THR B CG2 1 
ATOM   3003 N  N   . ARG B  1 48  ? 8.63300   10.90700  37.57600 1.000 16.65000  ? 42  ARG B N   1 
ATOM   3004 C  CA  . ARG B  1 48  ? 9.93500   11.24000  37.01800 1.000 16.05000  ? 42  ARG B CA  1 
ATOM   3005 C  C   . ARG B  1 48  ? 9.80900   12.42500  36.08800 1.000 16.36000  ? 42  ARG B C   1 
ATOM   3006 O  O   . ARG B  1 48  ? 8.99100   12.40800  35.17400 1.000 17.52000  ? 42  ARG B O   1 
ATOM   3007 C  CB  . ARG B  1 48  ? 10.50500  10.05500  36.24800 1.000 16.75000  ? 42  ARG B CB  1 
ATOM   3008 C  CG  . ARG B  1 48  ? 11.80100  10.38300  35.46300 1.000 16.26000  ? 42  ARG B CG  1 
ATOM   3009 C  CD  . ARG B  1 48  ? 12.05500  9.28400   34.44400 1.000 15.06000  ? 42  ARG B CD  1 
ATOM   3010 N  NE  . ARG B  1 48  ? 13.40800  9.34800   33.89200 1.000 17.29000  ? 42  ARG B NE  1 
ATOM   3011 C  CZ  . ARG B  1 48  ? 13.76000  10.03900  32.82100 1.000 13.89000  ? 42  ARG B CZ  1 
ATOM   3012 N  NH1 . ARG B  1 48  ? 12.92000  10.87300  32.22900 1.000 14.56000  ? 42  ARG B NH1 1 
ATOM   3013 N  NH2 . ARG B  1 48  ? 14.99000  9.89200   32.32700 1.000 13.92000  ? 42  ARG B NH2 1 
ATOM   3014 N  N   . MET B  1 49  ? 10.61600  13.46000  36.34200 1.000 14.41000  ? 43  MET B N   1 
ATOM   3015 C  CA  A MET B  1 49  ? 10.70000  14.57100  35.40400 0.500 16.67000  ? 43  MET B CA  1 
ATOM   3016 C  CA  B MET B  1 49  ? 10.72800  14.57200  35.41400 0.500 16.63000  ? 43  MET B CA  1 
ATOM   3017 C  C   . MET B  1 49  ? 11.13800  14.05100  34.04500 1.000 17.29000  ? 43  MET B C   1 
ATOM   3018 O  O   . MET B  1 49  ? 12.21400  13.46800  33.90600 1.000 16.96000  ? 43  MET B O   1 
ATOM   3019 C  CB  A MET B  1 49  ? 11.67200  15.63100  35.91200 0.500 19.66000  ? 43  MET B CB  1 
ATOM   3020 C  CB  B MET B  1 49  ? 11.76100  15.55400  35.95100 0.500 19.67000  ? 43  MET B CB  1 
ATOM   3021 C  CG  A MET B  1 49  ? 11.90400  16.77200  34.92200 0.500 17.70000  ? 43  MET B CG  1 
ATOM   3022 C  CG  B MET B  1 49  ? 11.73000  16.90000  35.29900 0.500 18.40000  ? 43  MET B CG  1 
ATOM   3023 S  SD  A MET B  1 49  ? 10.42700  17.78900  34.71100 0.500 20.02000  ? 43  MET B SD  1 
ATOM   3024 S  SD  B MET B  1 49  ? 10.12300  17.64900  35.61300 0.500 18.41000  ? 43  MET B SD  1 
ATOM   3025 C  CE  A MET B  1 49  ? 10.53800  18.83700  36.15600 0.500 20.07000  ? 43  MET B CE  1 
ATOM   3026 C  CE  B MET B  1 49  ? 10.39400  19.22700  34.80900 0.500 17.62000  ? 43  MET B CE  1 
ATOM   3027 N  N   . THR B  1 50  ? 10.29700  14.26100  33.02800 1.000 15.83000  ? 44  THR B N   1 
ATOM   3028 C  CA  . THR B  1 50  ? 10.49800  13.57600  31.75000 1.000 13.75000  ? 44  THR B CA  1 
ATOM   3029 C  C   . THR B  1 50  ? 10.23300  14.51400  30.58200 1.000 14.62000  ? 44  THR B C   1 
ATOM   3030 O  O   . THR B  1 50  ? 9.22200   15.22300  30.56100 1.000 13.88000  ? 44  THR B O   1 
ATOM   3031 C  CB  . THR B  1 50  ? 9.60200   12.33300  31.65200 1.000 15.72000  ? 44  THR B CB  1 
ATOM   3032 O  OG1 . THR B  1 50  ? 9.90700   11.43600  32.74400 1.000 14.14000  ? 44  THR B OG1 1 
ATOM   3033 C  CG2 . THR B  1 50  ? 9.78800   11.62000  30.29500 1.000 16.03000  ? 44  THR B CG2 1 
ATOM   3034 N  N   . LEU B  1 51  ? 11.14500  14.51900  29.61900 1.000 15.33000  ? 45  LEU B N   1 
ATOM   3035 C  CA  . LEU B  1 51  ? 10.94700  15.27300  28.38800 1.000 13.89000  ? 45  LEU B CA  1 
ATOM   3036 C  C   . LEU B  1 51  ? 9.87200   14.55300  27.58600 1.000 16.85000  ? 45  LEU B C   1 
ATOM   3037 O  O   . LEU B  1 51  ? 10.10000  13.43800  27.12700 1.000 16.59000  ? 45  LEU B O   1 
ATOM   3038 C  CB  . LEU B  1 51  ? 12.26100  15.34800  27.60200 1.000 13.60000  ? 45  LEU B CB  1 
ATOM   3039 C  CG  . LEU B  1 51  ? 13.23600  16.35500  28.20800 1.000 17.91000  ? 45  LEU B CG  1 
ATOM   3040 C  CD1 . LEU B  1 51  ? 14.67900  15.82800  28.05700 1.000 16.83000  ? 45  LEU B CD1 1 
ATOM   3041 C  CD2 . LEU B  1 51  ? 13.06200  17.70300  27.54700 1.000 17.07000  ? 45  LEU B CD2 1 
ATOM   3042 N  N   . ALA B  1 52  ? 8.71100   15.18400  27.39600 1.000 14.89000  ? 46  ALA B N   1 
ATOM   3043 C  CA  . ALA B  1 52  ? 7.61700   14.55800  26.64700 1.000 17.53000  ? 46  ALA B CA  1 
ATOM   3044 C  C   . ALA B  1 52  ? 7.95800   14.35500  25.16900 1.000 15.78000  ? 46  ALA B C   1 
ATOM   3045 O  O   . ALA B  1 52  ? 7.40900   13.45900  24.51500 1.000 15.12000  ? 46  ALA B O   1 
ATOM   3046 C  CB  . ALA B  1 52  ? 6.35200   15.44700  26.75500 1.000 13.33000  ? 46  ALA B CB  1 
ATOM   3047 N  N   . ARG B  1 53  ? 8.78400   15.22100  24.60500 1.000 17.05000  ? 47  ARG B N   1 
ATOM   3048 C  CA  . ARG B  1 53  ? 9.13700   15.14900  23.19500 1.000 17.42000  ? 47  ARG B CA  1 
ATOM   3049 C  C   . ARG B  1 53  ? 7.86400   15.07900  22.35300 1.000 18.70000  ? 47  ARG B C   1 
ATOM   3050 O  O   . ARG B  1 53  ? 6.89000   15.75900  22.68300 1.000 18.43000  ? 47  ARG B O   1 
ATOM   3051 C  CB  . ARG B  1 53  ? 10.08300  13.98000  22.95800 1.000 16.23000  ? 47  ARG B CB  1 
ATOM   3052 C  CG  . ARG B  1 53  ? 11.32600  14.04500  23.86600 1.000 16.57000  ? 47  ARG B CG  1 
ATOM   3053 C  CD  . ARG B  1 53  ? 12.29100  15.22700  23.59800 1.000 17.73000  ? 47  ARG B CD  1 
ATOM   3054 N  NE  . ARG B  1 53  ? 12.90200  15.17600  22.26600 1.000 19.12000  ? 47  ARG B NE  1 
ATOM   3055 C  CZ  . ARG B  1 53  ? 13.80200  14.27700  21.88000 1.000 20.27000  ? 47  ARG B CZ  1 
ATOM   3056 N  NH1 . ARG B  1 53  ? 14.31400  13.38300  22.73000 1.000 19.29000  ? 47  ARG B NH1 1 
ATOM   3057 N  NH2 . ARG B  1 53  ? 14.19400  14.25700  20.60300 1.000 19.62000  ? 47  ARG B NH2 1 
ATOM   3058 N  N   . SER B  1 54  ? 7.80900   14.24100  21.31800 1.000 18.34000  ? 48  SER B N   1 
ATOM   3059 C  CA  . SER B  1 54  ? 6.62800   14.27000  20.45900 1.000 19.60000  ? 48  SER B CA  1 
ATOM   3060 C  C   . SER B  1 54  ? 5.34300   13.84700  21.15100 1.000 19.30000  ? 48  SER B C   1 
ATOM   3061 O  O   . SER B  1 54  ? 4.25800   14.04100  20.57700 1.000 19.13000  ? 48  SER B O   1 
ATOM   3062 C  CB  . SER B  1 54  ? 6.81200   13.36100  19.27600 1.000 22.07000  ? 48  SER B CB  1 
ATOM   3063 O  OG  . SER B  1 54  ? 7.51100   14.06900  18.28400 1.000 24.14000  ? 48  SER B OG  1 
ATOM   3064 N  N   . ALA B  1 55  ? 5.43400   13.20400  22.32200 1.000 16.13000  ? 49  ALA B N   1 
ATOM   3065 C  CA  . ALA B  1 55  ? 4.21500   12.87200  23.03900 1.000 16.61000  ? 49  ALA B CA  1 
ATOM   3066 C  C   . ALA B  1 55  ? 3.48700   14.12000  23.52000 1.000 18.89000  ? 49  ALA B C   1 
ATOM   3067 O  O   . ALA B  1 55  ? 2.30000   14.02300  23.89000 1.000 21.68000  ? 49  ALA B O   1 
ATOM   3068 C  CB  . ALA B  1 55  ? 4.51000   11.91000  24.20700 1.000 16.45000  ? 49  ALA B CB  1 
ATOM   3069 N  N   . ALA B  1 56  ? 4.12800   15.29500  23.46000 1.000 19.09000  ? 50  ALA B N   1 
ATOM   3070 C  CA  . ALA B  1 56  ? 3.43900   16.53900  23.77400 1.000 18.02000  ? 50  ALA B CA  1 
ATOM   3071 C  C   . ALA B  1 56  ? 2.61400   17.05200  22.60500 1.000 17.55000  ? 50  ALA B C   1 
ATOM   3072 O  O   . ALA B  1 56  ? 1.88900   18.03100  22.77800 1.000 19.98000  ? 50  ALA B O   1 
ATOM   3073 C  CB  . ALA B  1 56  ? 4.42400   17.63600  24.20300 1.000 15.93000  ? 50  ALA B CB  1 
ATOM   3074 N  N   . LYS B  1 57  ? 2.74600   16.45700  21.42200 1.000 17.95000  ? 51  LYS B N   1 
ATOM   3075 C  CA  . LYS B  1 57  ? 2.14300   17.05200  20.22800 1.000 16.12000  ? 51  LYS B CA  1 
ATOM   3076 C  C   . LYS B  1 57  ? 0.63800   17.28400  20.32800 1.000 16.39000  ? 51  LYS B C   1 
ATOM   3077 O  O   . LYS B  1 57  ? 0.17400   18.29200  19.76400 1.000 18.40000  ? 51  LYS B O   1 
ATOM   3078 C  CB  . LYS B  1 57  ? 2.46200   16.21000  18.98100 1.000 17.37000  ? 51  LYS B CB  1 
ATOM   3079 C  CG  . LYS B  1 57  ? 3.83600   16.50200  18.39800 1.000 19.70000  ? 51  LYS B CG  1 
ATOM   3080 C  CD  . LYS B  1 57  ? 4.24700   15.49900  17.32500 1.000 21.17000  ? 51  LYS B CD  1 
ATOM   3081 C  CE  . LYS B  1 57  ? 5.71400   15.86200  16.89300 1.000 21.89000  ? 51  LYS B CE  1 
ATOM   3082 N  NZ  . LYS B  1 57  ? 6.39500   14.88300  15.98500 1.000 21.91000  ? 51  LYS B NZ  1 
ATOM   3083 N  N   . PRO B  1 58  ? -0.18300  16.43200  20.95500 1.000 18.23000  ? 52  PRO B N   1 
ATOM   3084 C  CA  . PRO B  1 58  ? -1.60900  16.80600  21.06200 1.000 16.56000  ? 52  PRO B CA  1 
ATOM   3085 C  C   . PRO B  1 58  ? -1.82400  18.07300  21.86300 1.000 17.66000  ? 52  PRO B C   1 
ATOM   3086 O  O   . PRO B  1 58  ? -2.78500  18.80800  21.59600 1.000 16.64000  ? 52  PRO B O   1 
ATOM   3087 C  CB  . PRO B  1 58  ? -2.25500  15.59200  21.74400 1.000 19.26000  ? 52  PRO B CB  1 
ATOM   3088 C  CG  . PRO B  1 58  ? -1.41900  14.44600  21.26300 1.000 15.85000  ? 52  PRO B CG  1 
ATOM   3089 C  CD  . PRO B  1 58  ? 0.00200   15.01300  21.34200 1.000 17.48000  ? 52  PRO B CD  1 
ATOM   3090 N  N   . ALA B  1 59  ? -0.94800  18.36200  22.82600 1.000 17.33000  ? 53  ALA B N   1 
ATOM   3091 C  CA  . ALA B  1 59  ? -1.05800  19.62700  23.54600 1.000 17.22000  ? 53  ALA B CA  1 
ATOM   3092 C  C   . ALA B  1 59  ? -0.68600  20.78600  22.64100 1.000 16.77000  ? 53  ALA B C   1 
ATOM   3093 O  O   . ALA B  1 59  ? -1.32000  21.83800  22.68400 1.000 18.45000  ? 53  ALA B O   1 
ATOM   3094 C  CB  . ALA B  1 59  ? -0.16100  19.63400  24.78800 1.000 20.91000  ? 53  ALA B CB  1 
ATOM   3095 N  N   . GLN B  1 60  ? 0.36600   20.61800  21.84300 1.000 16.03000  ? 54  GLN B N   1 
ATOM   3096 C  CA  . GLN B  1 60  ? 0.73300   21.65700  20.89100 1.000 17.47000  ? 54  GLN B CA  1 
ATOM   3097 C  C   . GLN B  1 60  ? -0.36900  21.85700  19.86500 1.000 19.69000  ? 54  GLN B C   1 
ATOM   3098 O  O   . GLN B  1 60  ? -0.68100  22.99100  19.49600 1.000 17.93000  ? 54  GLN B O   1 
ATOM   3099 C  CB  . GLN B  1 60  ? 2.05500   21.29700  20.22400 1.000 19.97000  ? 54  GLN B CB  1 
ATOM   3100 C  CG  . GLN B  1 60  ? 3.18800   21.45800  21.20900 1.000 17.62000  ? 54  GLN B CG  1 
ATOM   3101 C  CD  . GLN B  1 60  ? 4.43000   20.68000  20.86500 1.000 21.28000  ? 54  GLN B CD  1 
ATOM   3102 O  OE1 . GLN B  1 60  ? 4.38200   19.45500  20.69300 1.000 17.77000  ? 54  GLN B OE1 1 
ATOM   3103 N  NE2 . GLN B  1 60  ? 5.57300   21.39200  20.79500 1.000 18.80000  ? 54  GLN B NE2 1 
ATOM   3104 N  N   . ALA B  1 61  ? -0.97300  20.76100  19.40600 1.000 18.53000  ? 55  ALA B N   1 
ATOM   3105 C  CA  . ALA B  1 61  ? -2.08400  20.84300  18.47000 1.000 16.56000  ? 55  ALA B CA  1 
ATOM   3106 C  C   . ALA B  1 61  ? -3.25900  21.57400  19.08400 1.000 16.20000  ? 55  ALA B C   1 
ATOM   3107 O  O   . ALA B  1 61  ? -3.93800  22.33800  18.40000 1.000 17.21000  ? 55  ALA B O   1 
ATOM   3108 C  CB  . ALA B  1 61  ? -2.50300  19.43200  18.01500 1.000 16.94000  ? 55  ALA B CB  1 
ATOM   3109 N  N   . LEU B  1 62  ? -3.50800  21.38000  20.38000 1.000 18.51000  ? 56  LEU B N   1 
ATOM   3110 C  CA  . LEU B  1 62  ? -4.58400  22.14300  21.02000 1.000 19.67000  ? 56  LEU B CA  1 
ATOM   3111 C  C   . LEU B  1 62  ? -4.29100  23.63800  20.98100 1.000 20.17000  ? 56  LEU B C   1 
ATOM   3112 O  O   . LEU B  1 62  ? -5.17400  24.45300  20.70400 1.000 16.91000  ? 56  LEU B O   1 
ATOM   3113 C  CB  . LEU B  1 62  ? -4.77800  21.67900  22.46300 1.000 17.87000  ? 56  LEU B CB  1 
ATOM   3114 C  CG  . LEU B  1 62  ? -5.85000  22.37400  23.30400 1.000 18.91000  ? 56  LEU B CG  1 
ATOM   3115 C  CD1 . LEU B  1 62  ? -7.21200  22.22100  22.62400 1.000 17.74000  ? 56  LEU B CD1 1 
ATOM   3116 C  CD2 . LEU B  1 62  ? -5.88700  21.88300  24.77400 1.000 18.27000  ? 56  LEU B CD2 1 
ATOM   3117 N  N   . ALA B  1 63  ? -3.03500  24.01800  21.22700 1.000 16.62000  ? 57  ALA B N   1 
ATOM   3118 C  CA  . ALA B  1 63  ? -2.68800  25.43700  21.20200 1.000 16.15000  ? 57  ALA B CA  1 
ATOM   3119 C  C   . ALA B  1 63  ? -2.88800  26.01600  19.80800 1.000 17.26000  ? 57  ALA B C   1 
ATOM   3120 O  O   . ALA B  1 63  ? -3.44700  27.12400  19.65000 1.000 18.66000  ? 57  ALA B O   1 
ATOM   3121 C  CB  . ALA B  1 63  ? -1.24700  25.61800  21.68900 1.000 14.30000  ? 57  ALA B CB  1 
ATOM   3122 N  N   . ILE B  1 64  ? -2.48500  25.26400  18.77800 1.000 15.78000  ? 58  ILE B N   1 
ATOM   3123 C  CA  . ILE B  1 64  ? -2.77700  25.64500  17.40000 1.000 17.45000  ? 58  ILE B CA  1 
ATOM   3124 C  C   . ILE B  1 64  ? -4.27800  25.82400  17.18300 1.000 17.80000  ? 58  ILE B C   1 
ATOM   3125 O  O   . ILE B  1 64  ? -4.71200  26.84900  16.64900 1.000 19.34000  ? 58  ILE B O   1 
ATOM   3126 C  CB  . ILE B  1 64  ? -2.21100  24.61400  16.41800 1.000 19.83000  ? 58  ILE B CB  1 
ATOM   3127 C  CG1 . ILE B  1 64  ? -0.68000  24.60300  16.50200 1.000 18.94000  ? 58  ILE B CG1 1 
ATOM   3128 C  CG2 . ILE B  1 64  ? -2.72300  24.92700  14.99300 1.000 17.02000  ? 58  ILE B CG2 1 
ATOM   3129 C  CD1 . ILE B  1 64  ? -0.06500  23.28900  15.97800 1.000 16.99000  ? 58  ILE B CD1 1 
ATOM   3130 N  N   . LEU B  1 65  ? -5.08200  24.80800  17.53600 1.000 16.01000  ? 59  LEU B N   1 
ATOM   3131 C  CA  . LEU B  1 65  ? -6.51000  24.84500  17.20800 1.000 18.99000  ? 59  LEU B CA  1 
ATOM   3132 C  C   . LEU B  1 65  ? -7.26700  25.88100  18.02900 1.000 21.84000  ? 59  LEU B C   1 
ATOM   3133 O  O   . LEU B  1 65  ? -8.32900  26.35100  17.59700 1.000 21.77000  ? 59  LEU B O   1 
ATOM   3134 C  CB  . LEU B  1 65  ? -7.16000  23.46100  17.40100 1.000 16.90000  ? 59  LEU B CB  1 
ATOM   3135 C  CG  . LEU B  1 65  ? -6.67200  22.38700  16.43600 1.000 17.34000  ? 59  LEU B CG  1 
ATOM   3136 C  CD1 . LEU B  1 65  ? -7.28900  21.07400  16.85600 1.000 24.53000  ? 59  LEU B CD1 1 
ATOM   3137 C  CD2 . LEU B  1 65  ? -7.05000  22.72200  15.00300 1.000 23.13000  ? 59  LEU B CD2 1 
ATOM   3138 N  N   . GLU B  1 66  ? -6.75200  26.25500  19.18600 1.000 20.26000  ? 60  GLU B N   1 
ATOM   3139 C  CA  . GLU B  1 66  ? -7.34300  27.32400  19.96500 1.000 20.93000  ? 60  GLU B CA  1 
ATOM   3140 C  C   . GLU B  1 66  ? -6.83700  28.70100  19.56700 1.000 22.16000  ? 60  GLU B C   1 
ATOM   3141 O  O   . GLU B  1 66  ? -7.20200  29.70000  20.20800 1.000 23.27000  ? 60  GLU B O   1 
ATOM   3142 C  CB  . GLU B  1 66  ? -7.08400  27.10600  21.45600 1.000 22.32000  ? 60  GLU B CB  1 
ATOM   3143 C  CG  . GLU B  1 66  ? -7.85700  25.90500  22.04700 1.000 17.36000  ? 60  GLU B CG  1 
ATOM   3144 C  CD  . GLU B  1 66  ? -7.60900  25.79900  23.54500 1.000 24.87000  ? 60  GLU B CD  1 
ATOM   3145 O  OE1 . GLU B  1 66  ? -6.50700  26.18300  24.00100 1.000 27.80000  ? 60  GLU B OE1 1 
ATOM   3146 O  OE2 . GLU B  1 66  ? -8.50300  25.35600  24.28000 1.000 24.69000  ? 60  GLU B OE2 1 
ATOM   3147 N  N   . THR B  1 67  ? -6.00900  28.79700  18.54100 1.000 20.53000  ? 61  THR B N   1 
ATOM   3148 C  CA  . THR B  1 67  ? -5.56200  30.11800  18.10300 1.000 19.02000  ? 61  THR B CA  1 
ATOM   3149 C  C   . THR B  1 67  ? -6.63600  30.74200  17.23200 1.000 20.89000  ? 61  THR B C   1 
ATOM   3150 O  O   . THR B  1 67  ? -7.06700  30.13800  16.24400 1.000 19.22000  ? 61  THR B O   1 
ATOM   3151 C  CB  . THR B  1 67  ? -4.25200  30.01900  17.34400 1.000 20.09000  ? 61  THR B CB  1 
ATOM   3152 O  OG1 . THR B  1 67  ? -3.26300  29.49100  18.23400 1.000 18.12000  ? 61  THR B OG1 1 
ATOM   3153 C  CG2 . THR B  1 67  ? -3.84900  31.41700  16.86200 1.000 17.90000  ? 61  THR B CG2 1 
ATOM   3154 N  N   . GLU B  1 68  ? -7.08700  31.94000  17.62000 1.000 18.37000  ? 62  GLU B N   1 
ATOM   3155 C  CA  . GLU B  1 68  ? -8.22100  32.58500  16.96800 1.000 20.61000  ? 62  GLU B CA  1 
ATOM   3156 C  C   . GLU B  1 68  ? -7.92300  32.81000  15.49500 1.000 23.69000  ? 62  GLU B C   1 
ATOM   3157 O  O   . GLU B  1 68  ? -6.92400  33.45000  15.15000 1.000 20.86000  ? 62  GLU B O   1 
ATOM   3158 C  CB  . GLU B  1 68  ? -8.51700  33.92200  17.65600 1.000 18.96000  ? 62  GLU B CB  1 
ATOM   3159 C  CG  . GLU B  1 68  ? -9.01300  33.75800  19.06500 1.000 18.26000  ? 62  GLU B CG  1 
ATOM   3160 C  CD  . GLU B  1 68  ? -7.90400  33.70100  20.09400 1.000 21.71000  ? 62  GLU B CD  1 
ATOM   3161 O  OE1 . GLU B  1 68  ? -6.75500  33.37300  19.73300 1.000 20.51000  ? 62  GLU B OE1 1 
ATOM   3162 O  OE2 . GLU B  1 68  ? -8.19800  33.97600  21.27500 1.000 20.12000  ? 62  GLU B OE2 1 
ATOM   3163 N  N   . GLY B  1 69  ? -8.80000  32.30600  14.63700 1.000 21.83000  ? 63  GLY B N   1 
ATOM   3164 C  CA  . GLY B  1 69  ? -8.65300  32.46700  13.21300 1.000 24.24000  ? 63  GLY B CA  1 
ATOM   3165 C  C   . GLY B  1 69  ? -8.18700  31.22500  12.49200 1.000 24.24000  ? 63  GLY B C   1 
ATOM   3166 O  O   . GLY B  1 69  ? -8.32700  31.15100  11.26400 1.000 24.45000  ? 63  GLY B O   1 
ATOM   3167 N  N   . VAL B  1 70  ? -7.66400  30.23300  13.21700 1.000 18.71000  ? 64  VAL B N   1 
ATOM   3168 C  CA  . VAL B  1 70  ? -7.16500  29.03600  12.54200 1.000 22.17000  ? 64  VAL B CA  1 
ATOM   3169 C  C   . VAL B  1 70  ? -8.29600  28.23900  11.91900 1.000 21.59000  ? 64  VAL B C   1 
ATOM   3170 O  O   . VAL B  1 70  ? -8.11600  27.63200  10.85900 1.000 23.13000  ? 64  VAL B O   1 
ATOM   3171 C  CB  . VAL B  1 70  ? -6.34900  28.18700  13.52500 1.000 20.57000  ? 64  VAL B CB  1 
ATOM   3172 C  CG1 . VAL B  1 70  ? -6.12400  26.75400  12.96800 1.000 18.68000  ? 64  VAL B CG1 1 
ATOM   3173 C  CG2 . VAL B  1 70  ? -5.00700  28.87700  13.78100 1.000 20.19000  ? 64  VAL B CG2 1 
ATOM   3174 N  N   . ALA B  1 71  ? -9.47900  28.22900  12.54900 1.000 18.91000  ? 65  ALA B N   1 
ATOM   3175 C  CA  . ALA B  1 71  ? -10.57900 27.43300  12.03400 1.000 24.75000  ? 65  ALA B CA  1 
ATOM   3176 C  C   . ALA B  1 71  ? -10.90100 27.79800  10.59200 1.000 24.48000  ? 65  ALA B C   1 
ATOM   3177 O  O   . ALA B  1 71  ? -11.37800 26.95100  9.83200  1.000 25.63000  ? 65  ALA B O   1 
ATOM   3178 C  CB  . ALA B  1 71  ? -11.81400 27.60400  12.92800 1.000 24.39000  ? 65  ALA B CB  1 
ATOM   3179 N  N   . GLY B  1 72  ? -10.61000 29.03300  10.18500 1.000 23.44000  ? 66  GLY B N   1 
ATOM   3180 C  CA  . GLY B  1 72  ? -10.93100 29.47100  8.83600  1.000 26.36000  ? 66  GLY B CA  1 
ATOM   3181 C  C   . GLY B  1 72  ? -10.13000 28.78600  7.74100  1.000 26.29000  ? 66  GLY B C   1 
ATOM   3182 O  O   . GLY B  1 72  ? -10.55500 28.79700  6.58100  1.000 25.45000  ? 66  GLY B O   1 
ATOM   3183 N  N   . TYR B  1 73  ? -8.98100  28.19600  8.07400  1.000 23.42000  ? 67  TYR B N   1 
ATOM   3184 C  CA  . TYR B  1 73  ? -8.17200  27.54000  7.04700  1.000 22.22000  ? 67  TYR B CA  1 
ATOM   3185 C  C   . TYR B  1 73  ? -8.79400  26.24200  6.54400  1.000 24.56000  ? 67  TYR B C   1 
ATOM   3186 O  O   . TYR B  1 73  ? -8.36600  25.73000  5.50500  1.000 26.46000  ? 67  TYR B O   1 
ATOM   3187 C  CB  . TYR B  1 73  ? -6.77200  27.25800  7.58400  1.000 23.75000  ? 67  TYR B CB  1 
ATOM   3188 C  CG  . TYR B  1 73  ? -6.00200  28.52200  7.87600  1.000 23.56000  ? 67  TYR B CG  1 
ATOM   3189 C  CD1 . TYR B  1 73  ? -5.77000  29.44200  6.86900  1.000 24.56000  ? 67  TYR B CD1 1 
ATOM   3190 C  CD2 . TYR B  1 73  ? -5.49400  28.78300  9.14800  1.000 24.45000  ? 67  TYR B CD2 1 
ATOM   3191 C  CE1 . TYR B  1 73  ? -5.08500  30.60100  7.10800  1.000 30.03000  ? 67  TYR B CE1 1 
ATOM   3192 C  CE2 . TYR B  1 73  ? -4.78400  29.94900  9.39200  1.000 21.18000  ? 67  TYR B CE2 1 
ATOM   3193 C  CZ  . TYR B  1 73  ? -4.59600  30.84600  8.36800  1.000 26.18000  ? 67  TYR B CZ  1 
ATOM   3194 O  OH  . TYR B  1 73  ? -3.90400  32.01000  8.57700  1.000 32.97000  ? 67  TYR B OH  1 
ATOM   3195 N  N   . GLY B  1 74  ? -9.75800  25.68200  7.26800  1.000 25.10000  ? 68  GLY B N   1 
ATOM   3196 C  CA  . GLY B  1 74  ? -10.37100 24.43000  6.85000  1.000 22.26000  ? 68  GLY B CA  1 
ATOM   3197 C  C   . GLY B  1 74  ? -9.44700  23.22900  6.93900  1.000 23.53000  ? 68  GLY B C   1 
ATOM   3198 O  O   . GLY B  1 74  ? -9.49100  22.34700  6.06900  1.000 24.97000  ? 68  GLY B O   1 
ATOM   3199 N  N   . PHE B  1 75  ? -8.57800  23.19200  7.94600  1.000 23.78000  ? 69  PHE B N   1 
ATOM   3200 C  CA  . PHE B  1 75  ? -7.86100  21.96500  8.25100  1.000 22.17000  ? 69  PHE B CA  1 
ATOM   3201 C  C   . PHE B  1 75  ? -8.88900  20.89300  8.57400  1.000 23.61000  ? 69  PHE B C   1 
ATOM   3202 O  O   . PHE B  1 75  ? -9.89200  21.17000  9.24000  1.000 26.86000  ? 69  PHE B O   1 
ATOM   3203 C  CB  . PHE B  1 75  ? -6.91900  22.17100  9.43700  1.000 24.67000  ? 69  PHE B CB  1 
ATOM   3204 C  CG  . PHE B  1 75  ? -5.74200  23.05000  9.13300  1.000 25.01000  ? 69  PHE B CG  1 
ATOM   3205 C  CD1 . PHE B  1 75  ? -4.94700  22.81500  8.01900  1.000 20.87000  ? 69  PHE B CD1 1 
ATOM   3206 C  CD2 . PHE B  1 75  ? -5.42600  24.12000  9.96400  1.000 21.76000  ? 69  PHE B CD2 1 
ATOM   3207 C  CE1 . PHE B  1 75  ? -3.84200  23.65000  7.74100  1.000 22.72000  ? 69  PHE B CE1 1 
ATOM   3208 C  CE2 . PHE B  1 75  ? -4.33300  24.94300  9.69500  1.000 20.92000  ? 69  PHE B CE2 1 
ATOM   3209 C  CZ  . PHE B  1 75  ? -3.52700  24.69600  8.59400  1.000 22.06000  ? 69  PHE B CZ  1 
ATOM   3210 N  N   . ASP B  1 76  ? -8.69200  19.69400  8.03400  1.000 20.07000  ? 70  ASP B N   1 
ATOM   3211 C  CA  . ASP B  1 76  ? -9.62500  18.60900  8.28500  1.000 20.28000  ? 70  ASP B CA  1 
ATOM   3212 C  C   . ASP B  1 76  ? -9.04000  17.63100  9.29600  1.000 19.65000  ? 70  ASP B C   1 
ATOM   3213 O  O   . ASP B  1 76  ? -7.93600  17.83700  9.81100  1.000 21.30000  ? 70  ASP B O   1 
ATOM   3214 C  CB  . ASP B  1 76  ? -10.03200 17.91600  6.98500  1.000 24.33000  ? 70  ASP B CB  1 
ATOM   3215 C  CG  . ASP B  1 76  ? -8.89200  17.23600  6.25300  1.000 27.72000  ? 70  ASP B CG  1 
ATOM   3216 O  OD1 . ASP B  1 76  ? -7.76600  17.04400  6.80000  1.000 24.61000  ? 70  ASP B OD1 1 
ATOM   3217 O  OD2 . ASP B  1 76  ? -9.17000  16.88000  5.08000  1.000 29.33000  ? 70  ASP B OD2 1 
ATOM   3218 N  N   . ASP B  1 77  ? -9.80200  16.56600  9.58800  1.000 22.85000  ? 71  ASP B N   1 
ATOM   3219 C  CA  . ASP B  1 77  ? -9.39300  15.59600  10.60400 1.000 19.85000  ? 71  ASP B CA  1 
ATOM   3220 C  C   . ASP B  1 77  ? -8.00800  15.03100  10.29900 1.000 19.54000  ? 71  ASP B C   1 
ATOM   3221 O  O   . ASP B  1 77  ? -7.22300  14.80100  11.21500 1.000 16.42000  ? 71  ASP B O   1 
ATOM   3222 C  CB  . ASP B  1 77  ? -10.38900 14.42800  10.71300 1.000 22.86000  ? 71  ASP B CB  1 
ATOM   3223 C  CG  . ASP B  1 77  ? -11.68400 14.77600  11.50700 1.000 26.00000  ? 71  ASP B CG  1 
ATOM   3224 O  OD1 . ASP B  1 77  ? -11.85800 15.89300  11.99000 1.000 25.20000  ? 71  ASP B OD1 1 
ATOM   3225 O  OD2 . ASP B  1 77  ? -12.53300 13.88300  11.64900 1.000 33.40000  ? 71  ASP B OD2 1 
ATOM   3226 N  N   . ALA B  1 78  ? -7.72300  14.74300  9.02700  1.000 21.15000  ? 72  ALA B N   1 
ATOM   3227 C  CA  . ALA B  1 78  ? -6.44800  14.11300  8.70300  1.000 22.20000  ? 72  ALA B CA  1 
ATOM   3228 C  C   . ALA B  1 78  ? -5.30100  15.10100  8.85600  1.000 22.19000  ? 72  ALA B C   1 
ATOM   3229 O  O   . ALA B  1 78  ? -4.20200  14.71200  9.26600  1.000 18.09000  ? 72  ALA B O   1 
ATOM   3230 C  CB  . ALA B  1 78  ? -6.48700  13.52700  7.29600  1.000 22.41000  ? 72  ALA B CB  1 
ATOM   3231 N  N   . ASP B  1 79  ? -5.54100  16.37300  8.51100  1.000 20.74000  ? 73  ASP B N   1 
ATOM   3232 C  CA  . ASP B  1 79  ? -4.62200  17.47000  8.81900  1.000 22.82000  ? 73  ASP B CA  1 
ATOM   3233 C  C   . ASP B  1 79  ? -4.29500  17.55000  10.30800 1.000 21.82000  ? 73  ASP B C   1 
ATOM   3234 O  O   . ASP B  1 79  ? -3.13300  17.70700  10.68600 1.000 18.57000  ? 73  ASP B O   1 
ATOM   3235 C  CB  . ASP B  1 79  ? -5.20900  18.81000  8.36100  1.000 21.86000  ? 73  ASP B CB  1 
ATOM   3236 C  CG  . ASP B  1 79  ? -5.36800  18.91500  6.85000  1.000 22.83000  ? 73  ASP B CG  1 
ATOM   3237 O  OD1 . ASP B  1 79  ? -4.70200  18.18700  6.08600  1.000 23.32000  ? 73  ASP B OD1 1 
ATOM   3238 O  OD2 . ASP B  1 79  ? -6.17700  19.74800  6.41000  1.000 24.01000  ? 73  ASP B OD2 1 
ATOM   3239 N  N   . ILE B  1 80  ? -5.32000  17.53900  11.17100 1.000 18.95000  ? 74  ILE B N   1 
ATOM   3240 C  CA  . ILE B  1 80  ? -5.07800  17.58400  12.61400 1.000 18.74000  ? 74  ILE B CA  1 
ATOM   3241 C  C   . ILE B  1 80  ? -4.28100  16.35600  13.07600 1.000 20.33000  ? 74  ILE B C   1 
ATOM   3242 O  O   . ILE B  1 80  ? -3.37800  16.45900  13.93400 1.000 16.56000  ? 74  ILE B O   1 
ATOM   3243 C  CB  . ILE B  1 80  ? -6.42500  17.72200  13.35100 1.000 16.84000  ? 74  ILE B CB  1 
ATOM   3244 C  CG1 . ILE B  1 80  ? -7.08200  19.05000  12.93300 1.000 20.14000  ? 74  ILE B CG1 1 
ATOM   3245 C  CG2 . ILE B  1 80  ? -6.23600  17.60300  14.86800 1.000 19.50000  ? 74  ILE B CG2 1 
ATOM   3246 C  CD1 . ILE B  1 80  ? -8.57600  19.21300  13.33900 1.000 22.12000  ? 74  ILE B CD1 1 
ATOM   3247 N  N   . ALA B  1 81  ? -4.58600  15.17100  12.51900 1.000 18.03000  ? 75  ALA B N   1 
ATOM   3248 C  CA  . ALA B  1 81  ? -3.80500  14.00000  12.89500 1.000 20.05000  ? 75  ALA B CA  1 
ATOM   3249 C  C   . ALA B  1 81  ? -2.34200  14.20500  12.51800 1.000 18.76000  ? 75  ALA B C   1 
ATOM   3250 O  O   . ALA B  1 81  ? -1.43900  13.83100  13.27100 1.000 17.47000  ? 75  ALA B O   1 
ATOM   3251 C  CB  . ALA B  1 81  ? -4.36800  12.72100  12.25200 1.000 17.10000  ? 75  ALA B CB  1 
ATOM   3252 N  N   . LEU B  1 82  ? -2.08300  14.87200  11.39500 1.000 17.53000  ? 76  LEU B N   1 
ATOM   3253 C  CA  . LEU B  1 82  ? -0.68900  15.15000  11.05600 1.000 18.26000  ? 76  LEU B CA  1 
ATOM   3254 C  C   . LEU B  1 82  ? -0.06000  16.14900  12.03100 1.000 17.70000  ? 76  LEU B C   1 
ATOM   3255 O  O   . LEU B  1 82  ? 1.13300   16.06500  12.32200 1.000 20.04000  ? 76  LEU B O   1 
ATOM   3256 C  CB  . LEU B  1 82  ? -0.57400  15.67600  9.62100  1.000 18.98000  ? 76  LEU B CB  1 
ATOM   3257 C  CG  . LEU B  1 82  ? 0.82800   15.52800  8.98800  1.000 16.61000  ? 76  LEU B CG  1 
ATOM   3258 C  CD1 . LEU B  1 82  ? 1.05500   14.05800  8.63700  1.000 19.78000  ? 76  LEU B CD1 1 
ATOM   3259 C  CD2 . LEU B  1 82  ? 0.95800   16.36200  7.70800  1.000 18.35000  ? 76  LEU B CD2 1 
ATOM   3260 N  N   . MET B  1 83  ? -0.82700  17.13900  12.51400 1.000 16.25000  ? 77  MET B N   1 
ATOM   3261 C  CA  . MET B  1 83  ? -0.29800  18.02800  13.54800 1.000 16.33000  ? 77  MET B CA  1 
ATOM   3262 C  C   . MET B  1 83  ? 0.10800   17.26100  14.79000 1.000 18.13000  ? 77  MET B C   1 
ATOM   3263 O  O   . MET B  1 83  ? 1.07700   17.63700  15.46800 1.000 19.16000  ? 77  MET B O   1 
ATOM   3264 C  CB  . MET B  1 83  ? -1.33000  19.10100  13.93800 1.000 15.90000  ? 77  MET B CB  1 
ATOM   3265 C  CG  . MET B  1 83  ? -1.75500  20.00000  12.83500 1.000 16.29000  ? 77  MET B CG  1 
ATOM   3266 S  SD  . MET B  1 83  ? -2.94400  21.16700  13.58600 1.000 21.63000  ? 77  MET B SD  1 
ATOM   3267 C  CE  . MET B  1 83  ? -3.49600  22.01400  12.11500 1.000 21.20000  ? 77  MET B CE  1 
ATOM   3268 N  N   . CYS B  1 84  ? -0.59500  16.17400  15.08800 1.000 18.32000  ? 78  CYS B N   1 
ATOM   3269 C  CA  . CYS B  1 84  ? -0.29700  15.26500  16.19600 1.000 19.32000  ? 78  CYS B CA  1 
ATOM   3270 C  C   . CYS B  1 84  ? 0.74500   14.18900  15.88100 1.000 17.21000  ? 78  CYS B C   1 
ATOM   3271 O  O   . CYS B  1 84  ? 0.88300   13.25300  16.68000 1.000 21.70000  ? 78  CYS B O   1 
ATOM   3272 C  CB  . CYS B  1 84  ? -1.58400  14.57500  16.63000 1.000 18.04000  ? 78  CYS B CB  1 
ATOM   3273 S  SG  . CYS B  1 84  ? -2.82000  15.78600  17.22000 1.000 20.21000  ? 78  CYS B SG  1 
ATOM   3274 N  N   . ALA B  1 85  ? 1.40800   14.24500  14.73400 1.000 16.67000  ? 79  ALA B N   1 
ATOM   3275 C  CA  . ALA B  1 85  ? 2.16500   13.11300  14.21400 1.000 17.74000  ? 79  ALA B CA  1 
ATOM   3276 C  C   . ALA B  1 85  ? 3.67100   13.17800  14.47500 1.000 20.88000  ? 79  ALA B C   1 
ATOM   3277 O  O   . ALA B  1 85  ? 4.27200   14.25300  14.51600 1.000 22.17000  ? 79  ALA B O   1 
ATOM   3278 C  CB  . ALA B  1 85  ? 1.95000   13.00100  12.70600 1.000 18.57000  ? 79  ALA B CB  1 
ATOM   3279 N  N   . SER B  1 86  ? 4.28700   11.99400  14.60400 1.000 21.04000  ? 80  SER B N   1 
ATOM   3280 C  CA  . SER B  1 86  ? 5.71400   11.77500  14.29500 1.000 18.59000  ? 80  SER B CA  1 
ATOM   3281 C  C   . SER B  1 86  ? 5.72700   10.87500  13.06300 1.000 19.11000  ? 80  SER B C   1 
ATOM   3282 O  O   . SER B  1 86  ? 5.87200   9.65900   13.16400 1.000 20.00000  ? 80  SER B O   1 
ATOM   3283 C  CB  . SER B  1 86  ? 6.50000   11.12900  15.46900 1.000 18.22000  ? 80  SER B CB  1 
ATOM   3284 O  OG  . SER B  1 86  ? 6.39700   11.93200  16.62700 1.000 21.10000  ? 80  SER B OG  1 
ATOM   3285 N  N   . HIS B  1 87  ? 5.49500   11.46600  11.89700 1.000 18.32000  ? 81  HIS B N   1 
ATOM   3286 C  CA  . HIS B  1 87  ? 5.17100   10.58300  10.79300 1.000 20.82000  ? 81  HIS B CA  1 
ATOM   3287 C  C   . HIS B  1 87  ? 6.43800   10.00100  10.18200 1.000 20.33000  ? 81  HIS B C   1 
ATOM   3288 O  O   . HIS B  1 87  ? 7.56500   10.43900  10.45600 1.000 18.90000  ? 81  HIS B O   1 
ATOM   3289 C  CB  . HIS B  1 87  ? 4.32700   11.30700  9.74100  1.000 20.81000  ? 81  HIS B CB  1 
ATOM   3290 C  CG  . HIS B  1 87  ? 4.99200   12.50700  9.12800  1.000 19.17000  ? 81  HIS B CG  1 
ATOM   3291 N  ND1 . HIS B  1 87  ? 6.10200   12.41000  8.31300  1.000 18.62000  ? 81  HIS B ND1 1 
ATOM   3292 C  CD2 . HIS B  1 87  ? 4.68400   13.83000  9.18500  1.000 18.11000  ? 81  HIS B CD2 1 
ATOM   3293 C  CE1 . HIS B  1 87  ? 6.46200   13.62100  7.91000  1.000 17.43000  ? 81  HIS B CE1 1 
ATOM   3294 N  NE2 . HIS B  1 87  ? 5.61400   14.49900  8.42200  1.000 16.43000  ? 81  HIS B NE2 1 
ATOM   3295 N  N   . SER B  1 88  ? 6.22700   9.03000   9.31100  1.000 17.50000  ? 82  SER B N   1 
ATOM   3296 C  CA  . SER B  1 88  ? 7.30100   8.26200   8.69100  1.000 20.37000  ? 82  SER B CA  1 
ATOM   3297 C  C   . SER B  1 88  ? 7.85600   8.92300   7.43900  1.000 20.94000  ? 82  SER B C   1 
ATOM   3298 O  O   . SER B  1 88  ? 8.68900   8.31900   6.75000  1.000 22.94000  ? 82  SER B O   1 
ATOM   3299 C  CB  . SER B  1 88  ? 6.79800   6.87600   8.35800  1.000 18.59000  ? 82  SER B CB  1 
ATOM   3300 O  OG  . SER B  1 88  ? 6.78200   6.06300   9.52100  1.000 19.93000  ? 82  SER B OG  1 
ATOM   3301 N  N   . SER B  1 89  ? 7.40600   10.13100  7.12200  1.000 17.87000  ? 83  SER B N   1 
ATOM   3302 C  CA  . SER B  1 89  ? 7.83200   10.81000  5.90100  1.000 18.97000  ? 83  SER B CA  1 
ATOM   3303 C  C   . SER B  1 89  ? 7.45200   10.00700  4.66800  1.000 20.51000  ? 83  SER B C   1 
ATOM   3304 O  O   . SER B  1 89  ? 8.15000   10.03600  3.65500  1.000 20.98000  ? 83  SER B O   1 
ATOM   3305 C  CB  . SER B  1 89  ? 9.34200   11.08100  5.90800  1.000 20.92000  ? 83  SER B CB  1 
ATOM   3306 O  OG  . SER B  1 89  ? 9.72100   11.67200  7.14000  1.000 20.38000  ? 83  SER B OG  1 
ATOM   3307 N  N   . GLU B  1 90  ? 6.36000   9.25900   4.73600  1.000 19.36000  ? 84  GLU B N   1 
ATOM   3308 C  CA  . GLU B  1 90  ? 5.88400   8.61000   3.52600  1.000 20.40000  ? 84  GLU B CA  1 
ATOM   3309 C  C   . GLU B  1 90  ? 5.38200   9.67800   2.56300  1.000 23.02000  ? 84  GLU B C   1 
ATOM   3310 O  O   . GLU B  1 90  ? 5.11800   10.82200  2.94700  1.000 21.95000  ? 84  GLU B O   1 
ATOM   3311 C  CB  . GLU B  1 90  ? 4.78300   7.58400   3.85800  1.000 20.96000  ? 84  GLU B CB  1 
ATOM   3312 C  CG  . GLU B  1 90  ? 5.27400   6.53400   4.88000  1.000 22.00000  ? 84  GLU B CG  1 
ATOM   3313 C  CD  . GLU B  1 90  ? 4.15600   5.64200   5.47700  1.000 23.72000  ? 84  GLU B CD  1 
ATOM   3314 O  OE1 . GLU B  1 90  ? 2.98300   5.90200   5.18400  1.000 27.81000  ? 84  GLU B OE1 1 
ATOM   3315 O  OE2 . GLU B  1 90  ? 4.46100   4.66100   6.21400  1.000 28.75000  ? 84  GLU B OE2 1 
ATOM   3316 N  N   . ASP B  1 91  ? 5.29700   9.31400   1.28500  1.000 23.00000  ? 85  ASP B N   1 
ATOM   3317 C  CA  . ASP B  1 91  ? 4.87500   10.29800  0.29600  1.000 25.43000  ? 85  ASP B CA  1 
ATOM   3318 C  C   . ASP B  1 91  ? 3.54700   10.96600  0.68300  1.000 28.27000  ? 85  ASP B C   1 
ATOM   3319 O  O   . ASP B  1 91  ? 3.40100   12.17900  0.52500  1.000 23.12000  ? 85  ASP B O   1 
ATOM   3320 C  CB  . ASP B  1 91  ? 4.80300   9.64800   -1.08700 1.000 27.01000  ? 85  ASP B CB  1 
ATOM   3321 C  CG  . ASP B  1 91  ? 6.17400   9.47400   -1.71700 1.000 30.68000  ? 85  ASP B CG  1 
ATOM   3322 O  OD1 . ASP B  1 91  ? 7.20100   9.89700   -1.10900 1.000 30.67000  ? 85  ASP B OD1 1 
ATOM   3323 O  OD2 . ASP B  1 91  ? 6.22100   8.92400   -2.83400 1.000 36.95000  ? 85  ASP B OD2 1 
ATOM   3324 N  N   . ARG B  1 92  ? 2.58700   10.21200  1.23900  1.000 23.27000  ? 86  ARG B N   1 
ATOM   3325 C  CA  . ARG B  1 92  ? 1.32200   10.84200  1.62600  1.000 26.69000  ? 86  ARG B CA  1 
ATOM   3326 C  C   . ARG B  1 92  ? 1.51100   11.87300  2.72900  1.000 24.93000  ? 86  ARG B C   1 
ATOM   3327 O  O   . ARG B  1 92  ? 0.77700   12.87200  2.78000  1.000 23.98000  ? 86  ARG B O   1 
ATOM   3328 C  CB  . ARG B  1 92  ? 0.30100   9.80100   2.08200  1.000 25.35000  ? 86  ARG B CB  1 
ATOM   3329 C  CG  . ARG B  1 92  ? 0.84800   8.82400   3.13600  1.000 24.87000  ? 86  ARG B CG  1 
ATOM   3330 C  CD  . ARG B  1 92  ? -0.18600  7.75600   3.50700  1.000 22.89000  ? 86  ARG B CD  1 
ATOM   3331 N  NE  . ARG B  1 92  ? 0.40300   6.73700   4.37300  1.000 27.05000  ? 86  ARG B NE  1 
ATOM   3332 C  CZ  . ARG B  1 92  ? -0.26400  5.71700   4.89600  1.000 25.51000  ? 86  ARG B CZ  1 
ATOM   3333 N  NH1 . ARG B  1 92  ? -1.55600  5.53500   4.65700  1.000 24.01000  ? 86  ARG B NH1 1 
ATOM   3334 N  NH2 . ARG B  1 92  ? 0.37000   4.88700   5.71000  1.000 27.17000  ? 86  ARG B NH2 1 
ATOM   3335 N  N   . HIS B  1 93  ? 2.48900   11.66300  3.61400  1.000 21.81000  ? 87  HIS B N   1 
ATOM   3336 C  CA  . HIS B  1 93  ? 2.72300   12.64000  4.67200  1.000 22.15000  ? 87  HIS B CA  1 
ATOM   3337 C  C   . HIS B  1 93  ? 3.32200   13.91400  4.11300  1.000 24.48000  ? 87  HIS B C   1 
ATOM   3338 O  O   . HIS B  1 93  ? 2.99900   15.01000  4.55800  1.000 24.20000  ? 87  HIS B O   1 
ATOM   3339 C  CB  . HIS B  1 93  ? 3.66300   12.06800  5.72100  1.000 20.50000  ? 87  HIS B CB  1 
ATOM   3340 C  CG  . HIS B  1 93  ? 3.11500   10.88000  6.43000  1.000 22.78000  ? 87  HIS B CG  1 
ATOM   3341 N  ND1 . HIS B  1 93  ? 3.77100   9.67400   6.45700  1.000 20.54000  ? 87  HIS B ND1 1 
ATOM   3342 C  CD2 . HIS B  1 93  ? 1.97800   10.71200  7.14600  1.000 20.50000  ? 87  HIS B CD2 1 
ATOM   3343 C  CE1 . HIS B  1 93  ? 3.06700   8.80900   7.16400  1.000 25.80000  ? 87  HIS B CE1 1 
ATOM   3344 N  NE2 . HIS B  1 93  ? 1.97700   9.41700   7.59900  1.000 19.20000  ? 87  HIS B NE2 1 
ATOM   3345 N  N   . ILE B  1 94  ? 4.26700   13.77500  3.20400  1.000 22.30000  ? 88  ILE B N   1 
ATOM   3346 C  CA  . ILE B  1 94  ? 4.82200   14.94300  2.54800  1.000 21.51000  ? 88  ILE B CA  1 
ATOM   3347 C  C   . ILE B  1 94  ? 3.73600   15.67500  1.77100  1.000 21.78000  ? 88  ILE B C   1 
ATOM   3348 O  O   . ILE B  1 94  ? 3.63400   16.90200  1.82800  1.000 22.01000  ? 88  ILE B O   1 
ATOM   3349 C  CB  . ILE B  1 94  ? 5.98500   14.52000  1.64500  1.000 22.04000  ? 88  ILE B CB  1 
ATOM   3350 C  CG1 . ILE B  1 94  ? 7.10300   13.87500  2.50200  1.000 23.16000  ? 88  ILE B CG1 1 
ATOM   3351 C  CG2 . ILE B  1 94  ? 6.44000   15.70100  0.79100  1.000 22.85000  ? 88  ILE B CG2 1 
ATOM   3352 C  CD1 . ILE B  1 94  ? 8.25200   13.23800  1.70700  1.000 26.35000  ? 88  ILE B CD1 1 
ATOM   3353 N  N   . ALA B  1 95  ? 2.91100   14.93200  1.03400  1.000 22.89000  ? 89  ALA B N   1 
ATOM   3354 C  CA  . ALA B  1 95  ? 1.85200   15.55200  0.23800  1.000 24.89000  ? 89  ALA B CA  1 
ATOM   3355 C  C   . ALA B  1 95  ? 0.85700   16.30400  1.11800  1.000 21.87000  ? 89  ALA B C   1 
ATOM   3356 O  O   . ALA B  1 95  ? 0.43900   17.43400  0.78400  1.000 24.19000  ? 89  ALA B O   1 
ATOM   3357 C  CB  . ALA B  1 95  ? 1.13200   14.48500  -0.58500 1.000 26.18000  ? 89  ALA B CB  1 
ATOM   3358 N  N   . ARG B  1 96  ? 0.45800   15.70100  2.24700  1.000 21.25000  ? 90  ARG B N   1 
ATOM   3359 C  CA  . ARG B  1 96  ? -0.46600  16.41000  3.12700  1.000 21.80000  ? 90  ARG B CA  1 
ATOM   3360 C  C   . ARG B  1 96  ? 0.17900   17.64400  3.73700  1.000 19.32000  ? 90  ARG B C   1 
ATOM   3361 O  O   . ARG B  1 96  ? -0.51200  18.63700  3.98000  1.000 23.02000  ? 90  ARG B O   1 
ATOM   3362 C  CB  . ARG B  1 96  ? -1.00300  15.48800  4.23100  1.000 20.71000  ? 90  ARG B CB  1 
ATOM   3363 C  CG  . ARG B  1 96  ? -2.13700  16.15900  5.06900  1.000 23.80000  ? 90  ARG B CG  1 
ATOM   3364 C  CD  . ARG B  1 96  ? -2.87200  15.16600  5.94600  1.000 20.64000  ? 90  ARG B CD  1 
ATOM   3365 N  NE  . ARG B  1 96  ? -3.62700  14.20500  5.14700  1.000 22.92000  ? 90  ARG B NE  1 
ATOM   3366 C  CZ  . ARG B  1 96  ? -4.79300  14.48100  4.57000  1.000 25.45000  ? 90  ARG B CZ  1 
ATOM   3367 N  NH1 . ARG B  1 96  ? -5.37300  15.66300  4.72000  1.000 24.80000  ? 90  ARG B NH1 1 
ATOM   3368 N  NH2 . ARG B  1 96  ? -5.40800  13.53600  3.85500  1.000 25.16000  ? 90  ARG B NH2 1 
ATOM   3369 N  N   . THR B  1 97  ? 1.49300   17.60100  4.00000  1.000 21.66000  ? 91  THR B N   1 
ATOM   3370 C  CA  . THR B  1 97  ? 2.20500   18.78600  4.48300  1.000 18.13000  ? 91  THR B CA  1 
ATOM   3371 C  C   . THR B  1 97  ? 2.11400   19.92000  3.46000  1.000 20.75000  ? 91  THR B C   1 
ATOM   3372 O  O   . THR B  1 97  ? 1.78900   21.06100  3.80700  1.000 20.65000  ? 91  THR B O   1 
ATOM   3373 C  CB  . THR B  1 97  ? 3.66900   18.43200  4.79000  1.000 18.93000  ? 91  THR B CB  1 
ATOM   3374 O  OG1 . THR B  1 97  ? 3.70700   17.40200  5.79100  1.000 19.11000  ? 91  THR B OG1 1 
ATOM   3375 C  CG2 . THR B  1 97  ? 4.44200   19.65600  5.29900  1.000 18.68000  ? 91  THR B CG2 1 
ATOM   3376 N  N   . ARG B  1 98  ? 2.32800   19.59900  2.18100  1.000 21.70000  ? 92  ARG B N   1 
ATOM   3377 C  CA  . ARG B  1 98  ? 2.18900   20.59400  1.12300  1.000 21.29000  ? 92  ARG B CA  1 
ATOM   3378 C  C   . ARG B  1 98  ? 0.75000   21.09200  0.99700  1.000 25.46000  ? 92  ARG B C   1 
ATOM   3379 O  O   . ARG B  1 98  ? 0.51000   22.28100  0.73700  1.000 28.46000  ? 92  ARG B O   1 
ATOM   3380 C  CB  . ARG B  1 98  ? 2.66600   19.99600  -0.19100 1.000 22.39000  ? 92  ARG B CB  1 
ATOM   3381 C  CG  . ARG B  1 98  ? 4.16800   19.76300  -0.17000 1.000 22.41000  ? 92  ARG B CG  1 
ATOM   3382 C  CD  . ARG B  1 98  ? 4.67700   19.22800  -1.48300 1.000 27.69000  ? 92  ARG B CD  1 
ATOM   3383 N  NE  . ARG B  1 98  ? 6.13700   19.20700  -1.51100 1.000 30.83000  ? 92  ARG B NE  1 
ATOM   3384 C  CZ  . ARG B  1 98  ? 6.85100   18.20700  -2.01400 1.000 38.15000  ? 92  ARG B CZ  1 
ATOM   3385 N  NH1 . ARG B  1 98  ? 6.26700   17.10500  -2.47300 1.000 34.78000  ? 92  ARG B NH1 1 
ATOM   3386 N  NH2 . ARG B  1 98  ? 8.18400   18.31000  -2.05200 1.000 32.91000  ? 92  ARG B NH2 1 
ATOM   3387 N  N   . ALA B  1 99  ? -0.22300  20.19600  1.14200  1.000 22.90000  ? 93  ALA B N   1 
ATOM   3388 C  CA  . ALA B  1 99  ? -1.61800  20.62100  1.06300  1.000 25.08000  ? 93  ALA B CA  1 
ATOM   3389 C  C   . ALA B  1 99  ? -1.95400  21.60700  2.17700  1.000 24.21000  ? 93  ALA B C   1 
ATOM   3390 O  O   . ALA B  1 99  ? -2.66800  22.59900  1.95800  1.000 24.68000  ? 93  ALA B O   1 
ATOM   3391 C  CB  . ALA B  1 99  ? -2.53800  19.40100  1.13500  1.000 22.99000  ? 93  ALA B CB  1 
ATOM   3392 N  N   . MET B  1 100 ? -1.45100  21.34800  3.38000  1.000 23.35000  ? 94  MET B N   1 
ATOM   3393 C  CA  . MET B  1 100 ? -1.69500  22.23600  4.51600  1.000 23.75000  ? 94  MET B CA  1 
ATOM   3394 C  C   . MET B  1 100 ? -0.99300  23.57900  4.32100  1.000 22.40000  ? 94  MET B C   1 
ATOM   3395 O  O   . MET B  1 100 ? -1.52800  24.63200  4.67700  1.000 21.67000  ? 94  MET B O   1 
ATOM   3396 C  CB  . MET B  1 100 ? -1.22000  21.54400  5.79700  1.000 20.81000  ? 94  MET B CB  1 
ATOM   3397 C  CG  . MET B  1 100 ? -2.05000  20.32700  6.18300  1.000 22.58000  ? 94  MET B CG  1 
ATOM   3398 S  SD  . MET B  1 100 ? -1.43900  19.43200  7.61500  1.000 23.01000  ? 94  MET B SD  1 
ATOM   3399 C  CE  . MET B  1 100 ? -1.61300  20.64400  8.93100  1.000 19.10000  ? 94  MET B CE  1 
ATOM   3400 N  N   . LEU B  1 101 ? 0.22400   23.55100  3.78400  1.000 22.85000  ? 95  LEU B N   1 
ATOM   3401 C  CA  . LEU B  1 101 ? 0.89600   24.78900  3.43000  1.000 22.68000  ? 95  LEU B CA  1 
ATOM   3402 C  C   . LEU B  1 101 ? 0.07100   25.57500  2.42200  1.000 24.85000  ? 95  LEU B C   1 
ATOM   3403 O  O   . LEU B  1 101 ? -0.05600  26.80200  2.52800  1.000 25.38000  ? 95  LEU B O   1 
ATOM   3404 C  CB  . LEU B  1 101 ? 2.28000   24.47200  2.87100  1.000 22.85000  ? 95  LEU B CB  1 
ATOM   3405 C  CG  . LEU B  1 101 ? 3.35600   24.11600  3.89600  1.000 22.87000  ? 95  LEU B CG  1 
ATOM   3406 C  CD1 . LEU B  1 101 ? 4.58000   23.59600  3.15100  1.000 23.16000  ? 95  LEU B CD1 1 
ATOM   3407 C  CD2 . LEU B  1 101 ? 3.75100   25.34400  4.74900  1.000 20.61000  ? 95  LEU B CD2 1 
ATOM   3408 N  N   . SER B  1 102 ? -0.53500  24.88500  1.45300  1.000 24.45000  ? 96  SER B N   1 
ATOM   3409 C  CA  . SER B  1 102 ? -1.34100  25.61500  0.47600  1.000 26.28000  ? 96  SER B CA  1 
ATOM   3410 C  C   . SER B  1 102 ? -2.55600  26.25400  1.13200  1.000 25.85000  ? 96  SER B C   1 
ATOM   3411 O  O   . SER B  1 102 ? -2.96600  27.36100  0.75300  1.000 25.37000  ? 96  SER B O   1 
ATOM   3412 C  CB  . SER B  1 102 ? -1.76600  24.69000  -0.66400 1.000 32.24000  ? 96  SER B CB  1 
ATOM   3413 O  OG  . SER B  1 102 ? -0.63100  24.20500  -1.36500 1.000 34.88000  ? 96  SER B OG  1 
ATOM   3414 N  N   . LYS B  1 103 ? -3.14400  25.57800  2.12500  1.000 24.41000  ? 97  LYS B N   1 
ATOM   3415 C  CA  . LYS B  1 103 ? -4.33600  26.12400  2.76900  1.000 23.46000  ? 97  LYS B CA  1 
ATOM   3416 C  C   . LYS B  1 103 ? -4.05000  27.43900  3.48300  1.000 25.28000  ? 97  LYS B C   1 
ATOM   3417 O  O   . LYS B  1 103 ? -4.93700  28.29900  3.57200  1.000 27.07000  ? 97  LYS B O   1 
ATOM   3418 C  CB  . LYS B  1 103 ? -4.92800  25.12500  3.76500  1.000 24.67000  ? 97  LYS B CB  1 
ATOM   3419 C  CG  . LYS B  1 103 ? -5.61500  23.92700  3.11100  1.000 23.81000  ? 97  LYS B CG  1 
ATOM   3420 C  CD  . LYS B  1 103 ? -6.31500  23.04800  4.15400  1.000 24.91000  ? 97  LYS B CD  1 
ATOM   3421 C  CE  . LYS B  1 103 ? -7.05900  21.90500  3.47500  1.000 25.45000  ? 97  LYS B CE  1 
ATOM   3422 N  NZ  . LYS B  1 103 ? -7.59000  20.85500  4.41500  1.000 25.21000  ? 97  LYS B NZ  1 
ATOM   3423 N  N   . ILE B  1 104 ? -2.84300  27.61900  4.01200  1.000 22.01000  ? 98  ILE B N   1 
ATOM   3424 C  CA  . ILE B  1 104 ? -2.48800  28.86200  4.68000  1.000 22.42000  ? 98  ILE B CA  1 
ATOM   3425 C  C   . ILE B  1 104 ? -1.66100  29.76500  3.78300  1.000 26.09000  ? 98  ILE B C   1 
ATOM   3426 O  O   . ILE B  1 104 ? -1.13100  30.76500  4.25000  1.000 25.40000  ? 98  ILE B O   1 
ATOM   3427 C  CB  . ILE B  1 104 ? -1.77400  28.61100  6.02500  1.000 24.60000  ? 98  ILE B CB  1 
ATOM   3428 C  CG1 . ILE B  1 104 ? -0.32500  28.12100  5.83900  1.000 24.36000  ? 98  ILE B CG1 1 
ATOM   3429 C  CG2 . ILE B  1 104 ? -2.59100  27.61400  6.87900  1.000 20.97000  ? 98  ILE B CG2 1 
ATOM   3430 C  CD1 . ILE B  1 104 ? 0.48200   28.10900  7.13500  1.000 20.91000  ? 98  ILE B CD1 1 
ATOM   3431 N  N   . LYS B  1 105 ? -1.56300  29.45300  2.49900  1.000 24.29000  ? 99  LYS B N   1 
ATOM   3432 C  CA  . LYS B  1 105 ? -0.78300  30.25300  1.55000  1.000 26.80000  ? 99  LYS B CA  1 
ATOM   3433 C  C   . LYS B  1 105 ? 0.65600   30.50100  2.04000  1.000 30.16000  ? 99  LYS B C   1 
ATOM   3434 O  O   . LYS B  1 105 ? 1.16000   31.62300  2.02200  1.000 31.65000  ? 99  LYS B O   1 
ATOM   3435 C  CB  . LYS B  1 105 ? -1.50500  31.57300  1.23600  1.000 30.45000  ? 99  LYS B CB  1 
ATOM   3436 C  CG  . LYS B  1 105 ? -2.85100  31.36300  0.57300  1.000 29.15000  ? 99  LYS B CG  1 
ATOM   3437 C  CD  . LYS B  1 105 ? -3.45700  32.65500  0.01100  1.000 31.97000  ? 99  LYS B CD  1 
ATOM   3438 C  CE  . LYS B  1 105 ? -4.82200  32.36600  -0.60500 1.000 30.94000  ? 99  LYS B CE  1 
ATOM   3439 N  NZ  . LYS B  1 105 ? -5.49600  33.57900  -1.19600 1.000 33.51000  ? 99  LYS B NZ  1 
ATOM   3440 N  N   . ALA B  1 106 ? 1.33300   29.42800  2.46400  1.000 28.84000  ? 100 ALA B N   1 
ATOM   3441 C  CA  . ALA B  1 106 ? 2.73900   29.47700  2.86400  1.000 26.09000  ? 100 ALA B CA  1 
ATOM   3442 C  C   . ALA B  1 106 ? 3.55500   28.52000  1.99200  1.000 29.50000  ? 100 ALA B C   1 
ATOM   3443 O  O   . ALA B  1 106 ? 3.01600   27.76400  1.18600  1.000 26.89000  ? 100 ALA B O   1 
ATOM   3444 C  CB  . ALA B  1 106 ? 2.90500   29.13300  4.35100  1.000 26.13000  ? 100 ALA B CB  1 
ATOM   3445 N  N   . GLU B  1 107 ? 4.86900   28.54500  2.18300  1.000 28.95000  ? 101 GLU B N   1 
ATOM   3446 C  CA  . GLU B  1 107 ? 5.81900   27.79600  1.36700  1.000 31.61000  ? 101 GLU B CA  1 
ATOM   3447 C  C   . GLU B  1 107 ? 6.67800   26.89600  2.24800  1.000 30.09000  ? 101 GLU B C   1 
ATOM   3448 O  O   . GLU B  1 107 ? 6.84800   27.15700  3.43900  1.000 27.00000  ? 101 GLU B O   1 
ATOM   3449 C  CB  . GLU B  1 107 ? 6.74000   28.74400  0.59400  1.000 31.89000  ? 101 GLU B CB  1 
ATOM   3450 C  CG  . GLU B  1 107 ? 6.06200   29.94800  0.03600  1.000 42.14000  ? 101 GLU B CG  1 
ATOM   3451 C  CD  . GLU B  1 107 ? 5.61200   29.74300  -1.38500 1.000 50.52000  ? 101 GLU B CD  1 
ATOM   3452 O  OE1 . GLU B  1 107 ? 5.09400   28.64600  -1.70100 1.000 49.68000  ? 101 GLU B OE1 1 
ATOM   3453 O  OE2 . GLU B  1 107 ? 5.78200   30.68000  -2.18800 1.000 60.21000  ? 101 GLU B OE2 1 
ATOM   3454 N  N   . GLU B  1 108 ? 7.27100   25.85300  1.64500  1.000 26.44000  ? 102 GLU B N   1 
ATOM   3455 C  CA  . GLU B  1 108 ? 8.22800   25.03700  2.38700  1.000 24.84000  ? 102 GLU B CA  1 
ATOM   3456 C  C   . GLU B  1 108 ? 9.33800   25.89700  2.98400  1.000 26.01000  ? 102 GLU B C   1 
ATOM   3457 O  O   . GLU B  1 108 ? 9.77100   25.66500  4.11500  1.000 28.67000  ? 102 GLU B O   1 
ATOM   3458 C  CB  . GLU B  1 108 ? 8.82200   23.95100  1.48400  1.000 27.93000  ? 102 GLU B CB  1 
ATOM   3459 C  CG  . GLU B  1 108 ? 7.77300   23.10000  0.80700  1.000 31.08000  ? 102 GLU B CG  1 
ATOM   3460 C  CD  . GLU B  1 108 ? 8.35500   21.94400  0.01000  1.000 35.55000  ? 102 GLU B CD  1 
ATOM   3461 O  OE1 . GLU B  1 108 ? 9.60200   21.68100  0.09100  1.000 27.69000  ? 102 GLU B OE1 1 
ATOM   3462 O  OE2 . GLU B  1 108 ? 7.53800   21.31900  -0.71300 1.000 33.07000  ? 102 GLU B OE2 1 
ATOM   3463 N  N   . ALA B  1 109 ? 9.80700   26.90000  2.24500  1.000 27.01000  ? 103 ALA B N   1 
ATOM   3464 C  CA  . ALA B  1 109 ? 10.82200  27.80700  2.78200  1.000 26.11000  ? 103 ALA B CA  1 
ATOM   3465 C  C   . ALA B  1 109 ? 10.39600  28.46900  4.09300  1.000 25.51000  ? 103 ALA B C   1 
ATOM   3466 O  O   . ALA B  1 109 ? 11.25500  28.94100  4.84100  1.000 25.88000  ? 103 ALA B O   1 
ATOM   3467 C  CB  . ALA B  1 109 ? 11.16400  28.89000  1.75500  1.000 26.61000  ? 103 ALA B CB  1 
ATOM   3468 N  N   . ASP B  1 110 ? 9.10500   28.51000  4.40000  1.000 23.67000  ? 104 ASP B N   1 
ATOM   3469 C  CA  . ASP B  1 110 ? 8.65400   29.09400  5.65700  1.000 28.05000  ? 104 ASP B CA  1 
ATOM   3470 C  C   . ASP B  1 110 ? 8.79400   28.14500  6.84200  1.000 23.93000  ? 104 ASP B C   1 
ATOM   3471 O  O   . ASP B  1 110 ? 8.71200   28.60600  7.98600  1.000 22.28000  ? 104 ASP B O   1 
ATOM   3472 C  CB  . ASP B  1 110 ? 7.18400   29.55900  5.54500  1.000 25.43000  ? 104 ASP B CB  1 
ATOM   3473 C  CG  . ASP B  1 110 ? 6.98900   30.62500  4.48600  1.000 30.04000  ? 104 ASP B CG  1 
ATOM   3474 O  OD1 . ASP B  1 110 ? 7.76100   31.60400  4.50600  1.000 33.18000  ? 104 ASP B OD1 1 
ATOM   3475 O  OD2 . ASP B  1 110 ? 6.08600   30.48000  3.62600  1.000 28.38000  ? 104 ASP B OD2 1 
ATOM   3476 N  N   . LEU B  1 111 ? 9.00900   26.84800  6.60200  1.000 24.53000  ? 105 LEU B N   1 
ATOM   3477 C  CA  . LEU B  1 111 ? 9.17900   25.89400  7.69500  1.000 22.04000  ? 105 LEU B CA  1 
ATOM   3478 C  C   . LEU B  1 111 ? 10.48500  26.18700  8.40700  1.000 26.00000  ? 105 LEU B C   1 
ATOM   3479 O  O   . LEU B  1 111 ? 11.47700  26.55900  7.77400  1.000 27.98000  ? 105 LEU B O   1 
ATOM   3480 C  CB  . LEU B  1 111 ? 9.18200   24.44900  7.16500  1.000 23.55000  ? 105 LEU B CB  1 
ATOM   3481 C  CG  . LEU B  1 111 ? 7.84300   23.98300  6.61500  1.000 23.76000  ? 105 LEU B CG  1 
ATOM   3482 C  CD1 . LEU B  1 111 ? 7.95100   22.63700  5.91600  1.000 27.31000  ? 105 LEU B CD1 1 
ATOM   3483 C  CD2 . LEU B  1 111 ? 6.76700   23.96800  7.73900  1.000 22.06000  ? 105 LEU B CD2 1 
ATOM   3484 N  N   . ARG B  1 112 ? 10.49000  26.02800  9.72800  1.000 24.18000  ? 106 ARG B N   1 
ATOM   3485 C  CA  . ARG B  1 112 ? 11.71100  26.23100  10.50100 1.000 25.11000  ? 106 ARG B CA  1 
ATOM   3486 C  C   . ARG B  1 112 ? 12.23200  24.92700  11.11100 1.000 24.99000  ? 106 ARG B C   1 
ATOM   3487 O  O   . ARG B  1 112 ? 13.14000  24.95700  11.95200 1.000 22.74000  ? 106 ARG B O   1 
ATOM   3488 C  CB  . ARG B  1 112 ? 11.46800  27.29800  11.56900 1.000 25.07000  ? 106 ARG B CB  1 
ATOM   3489 C  CG  . ARG B  1 112 ? 11.28600  28.69400  10.95700 1.000 27.31000  ? 106 ARG B CG  1 
ATOM   3490 C  CD  . ARG B  1 112 ? 12.58300  29.20900  10.29700 1.000 32.62000  ? 106 ARG B CD  1 
ATOM   3491 N  NE  . ARG B  1 112 ? 12.35100  30.46100  9.57800  1.000 35.40000  ? 106 ARG B NE  1 
ATOM   3492 C  CZ  . ARG B  1 112 ? 12.01700  30.53500  8.29600  1.000 33.48000  ? 106 ARG B CZ  1 
ATOM   3493 N  NH1 . ARG B  1 112 ? 11.89100  29.44600  7.55200  1.000 29.67000  ? 106 ARG B NH1 1 
ATOM   3494 N  NH2 . ARG B  1 112 ? 11.80600  31.73000  7.74700  1.000 36.90000  ? 106 ARG B NH2 1 
ATOM   3495 N  N   . CYS B  1 113 ? 11.66700  23.79300  10.70300 1.000 19.49000  ? 107 CYS B N   1 
ATOM   3496 C  CA  . CYS B  1 113 ? 12.15200  22.45000  11.00400 1.000 21.41000  ? 107 CYS B CA  1 
ATOM   3497 C  C   . CYS B  1 113 ? 13.00000  21.96500  9.84300  1.000 25.56000  ? 107 CYS B C   1 
ATOM   3498 O  O   . CYS B  1 113 ? 12.93700  22.51400  8.73800  1.000 23.26000  ? 107 CYS B O   1 
ATOM   3499 C  CB  . CYS B  1 113 ? 10.97800  21.49200  11.23100 1.000 20.50000  ? 107 CYS B CB  1 
ATOM   3500 S  SG  . CYS B  1 113 ? 9.77400   21.43400  9.85300  1.000 21.68000  ? 107 CYS B SG  1 
ATOM   3501 N  N   . GLY B  1 114 ? 13.81200  20.93300  10.09900 1.000 25.19000  ? 108 GLY B N   1 
ATOM   3502 C  CA  . GLY B  1 114 ? 14.75000  20.45500  9.10900  1.000 22.42000  ? 108 GLY B CA  1 
ATOM   3503 C  C   . GLY B  1 114 ? 14.56800  18.96900  8.86600  1.000 23.56000  ? 108 GLY B C   1 
ATOM   3504 O  O   . GLY B  1 114 ? 13.96700  18.26000  9.66800  1.000 19.37000  ? 108 GLY B O   1 
ATOM   3505 N  N   . GLY B  1 115 ? 15.11900  18.49700  7.73400  1.000 24.29000  ? 109 GLY B N   1 
ATOM   3506 C  CA  . GLY B  1 115 ? 14.93600  17.10500  7.35000  1.000 23.09000  ? 109 GLY B CA  1 
ATOM   3507 C  C   . GLY B  1 115 ? 15.78600  16.16300  8.18100  1.000 22.53000  ? 109 GLY B C   1 
ATOM   3508 O  O   . GLY B  1 115 ? 16.70600  16.59300  8.86700  1.000 22.86000  ? 109 GLY B O   1 
ATOM   3509 N  N   . HIS B  1 116 ? 15.48700  14.86100  8.09100  1.000 22.86000  ? 110 HIS B N   1 
ATOM   3510 C  CA  . HIS B  1 116 ? 16.23000  13.84800  8.83600  1.000 20.59000  ? 110 HIS B CA  1 
ATOM   3511 C  C   . HIS B  1 116 ? 15.95400  12.48500  8.21200  1.000 24.61000  ? 110 HIS B C   1 
ATOM   3512 O  O   . HIS B  1 116 ? 14.98200  12.33500  7.46400  1.000 23.72000  ? 110 HIS B O   1 
ATOM   3513 C  CB  . HIS B  1 116 ? 15.81600  13.84800  10.30600 1.000 19.84000  ? 110 HIS B CB  1 
ATOM   3514 C  CG  . HIS B  1 116 ? 14.33900  13.68800  10.49000 1.000 22.80000  ? 110 HIS B CG  1 
ATOM   3515 N  ND1 . HIS B  1 116 ? 13.69700  12.48100  10.32500 1.000 24.67000  ? 110 HIS B ND1 1 
ATOM   3516 C  CD2 . HIS B  1 116 ? 13.37200  14.59500  10.76500 1.000 22.96000  ? 110 HIS B CD2 1 
ATOM   3517 C  CE1 . HIS B  1 116 ? 12.39400  12.64600  10.51400 1.000 20.73000  ? 110 HIS B CE1 1 
ATOM   3518 N  NE2 . HIS B  1 116 ? 12.17600  13.92100  10.78900 1.000 21.67000  ? 110 HIS B NE2 1 
ATOM   3519 N  N   . PRO B  1 117 ? 16.77400  11.46300  8.52000  1.000 24.53000  ? 111 PRO B N   1 
ATOM   3520 C  CA  . PRO B  1 117 ? 16.46400  10.11300  8.03800  1.000 24.35000  ? 111 PRO B CA  1 
ATOM   3521 C  C   . PRO B  1 117 ? 15.07900  9.70200   8.49700  1.000 23.25000  ? 111 PRO B C   1 
ATOM   3522 O  O   . PRO B  1 117 ? 14.66400  10.00400  9.61400  1.000 23.80000  ? 111 PRO B O   1 
ATOM   3523 C  CB  . PRO B  1 117 ? 17.56400  9.24400   8.66900  1.000 24.47000  ? 111 PRO B CB  1 
ATOM   3524 C  CG  . PRO B  1 117 ? 18.71500  10.17800  8.78500  1.000 26.60000  ? 111 PRO B CG  1 
ATOM   3525 C  CD  . PRO B  1 117 ? 18.07000  11.49100  9.22000  1.000 22.20000  ? 111 PRO B CD  1 
ATOM   3526 N  N   . SER B  1 118 ? 14.34800  9.04200   7.61000  1.000 24.04000  ? 112 SER B N   1 
ATOM   3527 C  CA  . SER B  1 118 ? 12.97200  8.70000   7.93000  1.000 20.33000  ? 112 SER B CA  1 
ATOM   3528 C  C   . SER B  1 118 ? 12.91300  7.82400   9.16600  1.000 25.47000  ? 112 SER B C   1 
ATOM   3529 O  O   . SER B  1 118 ? 13.84200  7.05800   9.45600  1.000 23.26000  ? 112 SER B O   1 
ATOM   3530 C  CB  . SER B  1 118 ? 12.30600  7.97700   6.76800  1.000 24.91000  ? 112 SER B CB  1 
ATOM   3531 O  OG  . SER B  1 118 ? 11.07800  7.42700   7.20400  1.000 24.56000  ? 112 SER B OG  1 
ATOM   3532 N  N   . LEU B  1 119 ? 11.80900  7.95600   9.90400  1.000 23.92000  ? 113 LEU B N   1 
ATOM   3533 C  CA  . LEU B  1 119 ? 11.53200  7.08600   11.03900 1.000 24.79000  ? 113 LEU B CA  1 
ATOM   3534 C  C   . LEU B  1 119 ? 11.12900  5.68700   10.62000 1.000 26.67000  ? 113 LEU B C   1 
ATOM   3535 O  O   . LEU B  1 119 ? 11.05500  4.80600   11.48200 1.000 28.86000  ? 113 LEU B O   1 
ATOM   3536 C  CB  . LEU B  1 119 ? 10.41500  7.66100   11.89700 1.000 25.30000  ? 113 LEU B CB  1 
ATOM   3537 C  CG  . LEU B  1 119 ? 10.69300  8.94200   12.65200 1.000 23.30000  ? 113 LEU B CG  1 
ATOM   3538 C  CD1 . LEU B  1 119 ? 9.46000   9.27100   13.51000 1.000 22.78000  ? 113 LEU B CD1 1 
ATOM   3539 C  CD2 . LEU B  1 119 ? 11.92100  8.74000   13.48700 1.000 29.12000  ? 113 LEU B CD2 1 
ATOM   3540 N  N   . SER B  1 120 ? 10.86900  5.48000   9.33600  1.000 22.17000  ? 114 SER B N   1 
ATOM   3541 C  CA  . SER B  1 120 ? 10.55300  4.18500   8.76900  1.000 27.76000  ? 114 SER B CA  1 
ATOM   3542 C  C   . SER B  1 120 ? 11.77600  3.67700   8.02300  1.000 25.14000  ? 114 SER B C   1 
ATOM   3543 O  O   . SER B  1 120 ? 12.34900  4.40400   7.20000  1.000 24.29000  ? 114 SER B O   1 
ATOM   3544 C  CB  . SER B  1 120 ? 9.36000   4.29500   7.82200  1.000 26.26000  ? 114 SER B CB  1 
ATOM   3545 O  OG  . SER B  1 120 ? 9.32800   3.19200   6.94200  1.000 26.28000  ? 114 SER B OG  1 
ATOM   3546 N  N   . GLU B  1 121 ? 12.18700  2.44300   8.32300  1.000 27.67000  ? 115 GLU B N   1 
ATOM   3547 C  CA  . GLU B  1 121 ? 13.32900  1.89400   7.61000  1.000 30.75000  ? 115 GLU B CA  1 
ATOM   3548 C  C   . GLU B  1 121 ? 13.00500  1.68000   6.14000  1.000 33.99000  ? 115 GLU B C   1 
ATOM   3549 O  O   . GLU B  1 121 ? 13.87400  1.85700   5.28500  1.000 33.08000  ? 115 GLU B O   1 
ATOM   3550 C  CB  . GLU B  1 121 ? 13.77600  0.59400   8.26400  1.000 39.90000  ? 115 GLU B CB  1 
ATOM   3551 C  CG  . GLU B  1 121 ? 15.24500  0.32900   8.07400  1.000 50.13000  ? 115 GLU B CG  1 
ATOM   3552 C  CD  . GLU B  1 121 ? 15.99600  0.26900   9.38900  1.000 65.69000  ? 115 GLU B CD  1 
ATOM   3553 O  OE1 . GLU B  1 121 ? 15.88100  -0.77600  10.08600 1.000 67.02000  ? 115 GLU B OE1 1 
ATOM   3554 O  OE2 . GLU B  1 121 ? 16.68800  1.26800   9.72100  1.000 64.43000  ? 115 GLU B OE2 1 
ATOM   3555 N  N   . MET B  1 122 ? 11.74700  1.37800   5.81900  1.000 31.98000  ? 116 MET B N   1 
ATOM   3556 C  CA  . MET B  1 122 ? 11.39900  1.11300   4.42700  1.000 32.14000  ? 116 MET B CA  1 
ATOM   3557 C  C   . MET B  1 122 ? 11.38800  2.39300   3.61000  1.000 30.76000  ? 116 MET B C   1 
ATOM   3558 O  O   . MET B  1 122 ? 11.78600  2.39200   2.44200  1.000 31.93000  ? 116 MET B O   1 
ATOM   3559 C  CB  . MET B  1 122 ? 10.04000  0.40700   4.34100  1.000 34.13000  ? 116 MET B CB  1 
ATOM   3560 C  CG  . MET B  1 122 ? 10.11500  -1.13600  4.53900  1.000 46.87000  ? 116 MET B CG  1 
ATOM   3561 S  SD  . MET B  1 122 ? 11.51300  -1.99600  3.73900  1.000 58.76000  ? 116 MET B SD  1 
ATOM   3562 C  CE  . MET B  1 122 ? 10.66800  -3.38000  2.96200  1.000 56.85000  ? 116 MET B CE  1 
ATOM   3563 N  N   . VAL B  1 123 ? 10.93000  3.49400   4.20200  1.000 29.68000  ? 117 VAL B N   1 
ATOM   3564 C  CA  . VAL B  1 123 ? 11.02800  4.78300   3.52300  1.000 26.28000  ? 117 VAL B CA  1 
ATOM   3565 C  C   . VAL B  1 123 ? 12.48300  5.17100   3.38700  1.000 28.60000  ? 117 VAL B C   1 
ATOM   3566 O  O   . VAL B  1 123 ? 12.93900  5.57600   2.30700  1.000 31.28000  ? 117 VAL B O   1 
ATOM   3567 C  CB  . VAL B  1 123 ? 10.22100  5.85700   4.27100  1.000 27.40000  ? 117 VAL B CB  1 
ATOM   3568 C  CG1 . VAL B  1 123 ? 10.45000  7.24300   3.64100  1.000 23.80000  ? 117 VAL B CG1 1 
ATOM   3569 C  CG2 . VAL B  1 123 ? 8.74300   5.48300   4.28600  1.000 30.19000  ? 117 VAL B CG2 1 
ATOM   3570 N  N   . ASN B  1 124 ? 13.25000  5.00900   4.46500  1.000 25.95000  ? 118 ASN B N   1 
ATOM   3571 C  CA  . ASN B  1 124 ? 14.64000  5.42300   4.40400  1.000 29.31000  ? 118 ASN B CA  1 
ATOM   3572 C  C   . ASN B  1 124 ? 15.40000  4.64800   3.33900  1.000 30.78000  ? 118 ASN B C   1 
ATOM   3573 O  O   . ASN B  1 124 ? 16.27100  5.20900   2.66000  1.000 30.62000  ? 118 ASN B O   1 
ATOM   3574 C  CB  . ASN B  1 124 ? 15.30800  5.25800   5.76000  1.000 29.27000  ? 118 ASN B CB  1 
ATOM   3575 C  CG  . ASN B  1 124 ? 16.36800  6.29200   5.97400  1.000 34.51000  ? 118 ASN B CG  1 
ATOM   3576 O  OD1 . ASN B  1 124 ? 16.12700  7.49700   5.79700  1.000 27.28000  ? 118 ASN B OD1 1 
ATOM   3577 N  ND2 . ASN B  1 124 ? 17.57000  5.84000   6.27300  1.000 30.18000  ? 118 ASN B ND2 1 
ATOM   3578 N  N   . ARG B  1 125 ? 15.08900  3.35800   3.17000  1.000 29.13000  ? 119 ARG B N   1 
ATOM   3579 C  CA  . ARG B  1 125 ? 15.74600  2.59400   2.11100  1.000 30.93000  ? 119 ARG B CA  1 
ATOM   3580 C  C   . ARG B  1 125 ? 15.44200  3.17000   0.73600  1.000 31.26000  ? 119 ARG B C   1 
ATOM   3581 O  O   . ARG B  1 125 ? 16.32500  3.24500   -0.12500 1.000 33.43000  ? 119 ARG B O   1 
ATOM   3582 C  CB  . ARG B  1 125 ? 15.31700  1.14900   2.17000  1.000 33.77000  ? 119 ARG B CB  1 
ATOM   3583 C  CG  . ARG B  1 125 ? 15.70900  0.49400   3.43600  1.000 36.89000  ? 119 ARG B CG  1 
ATOM   3584 C  CD  . ARG B  1 125 ? 15.45900  -1.00300  3.31500  1.000 41.54000  ? 119 ARG B CD  1 
ATOM   3585 N  NE  . ARG B  1 125 ? 15.22700  -1.63500  4.60600  1.000 52.59000  ? 119 ARG B NE  1 
ATOM   3586 C  CZ  . ARG B  1 125 ? 16.14500  -1.77700  5.55300  1.000 54.66000  ? 119 ARG B CZ  1 
ATOM   3587 N  NH1 . ARG B  1 125 ? 17.35600  -1.26200  5.42600  1.000 51.82000  ? 119 ARG B NH1 1 
ATOM   3588 N  NH2 . ARG B  1 125 ? 15.83600  -2.44700  6.66200  1.000 59.84000  ? 119 ARG B NH2 1 
ATOM   3589 N  N   . SER B  1 126 ? 14.18800  3.53500   0.49000  1.000 30.67000  ? 120 SER B N   1 
ATOM   3590 C  CA  A SER B  1 126 ? 13.85800  4.18700   -0.77400 0.400 32.70000  ? 120 SER B CA  1 
ATOM   3591 C  CA  B SER B  1 126 ? 13.86200  4.18500   -0.77400 0.600 32.72000  ? 120 SER B CA  1 
ATOM   3592 C  C   . SER B  1 126 ? 14.69100  5.44700   -0.97400 1.000 31.20000  ? 120 SER B C   1 
ATOM   3593 O  O   . SER B  1 126 ? 15.24300  5.67200   -2.05700 1.000 39.43000  ? 120 SER B O   1 
ATOM   3594 C  CB  A SER B  1 126 ? 12.36900  4.52100   -0.82700 0.400 31.37000  ? 120 SER B CB  1 
ATOM   3595 C  CB  B SER B  1 126 ? 12.37600  4.51500   -0.83800 0.600 31.36000  ? 120 SER B CB  1 
ATOM   3596 O  OG  A SER B  1 126 ? 12.09900  5.73000   -0.14400 0.400 29.95000  ? 120 SER B OG  1 
ATOM   3597 O  OG  B SER B  1 126 ? 12.05900  5.03400   -2.11400 0.600 38.69000  ? 120 SER B OG  1 
ATOM   3598 N  N   . TRP B  1 127 ? 14.80700  6.27000   0.06400  1.000 29.03000  ? 121 TRP B N   1 
ATOM   3599 C  CA  . TRP B  1 127 ? 15.58500  7.49400   -0.04600 1.000 29.87000  ? 121 TRP B CA  1 
ATOM   3600 C  C   . TRP B  1 127 ? 17.04700  7.19800   -0.35400 1.000 30.30000  ? 121 TRP B C   1 
ATOM   3601 O  O   . TRP B  1 127 ? 17.66800  7.89400   -1.17000 1.000 31.23000  ? 121 TRP B O   1 
ATOM   3602 C  CB  . TRP B  1 127 ? 15.47300  8.27500   1.25000  1.000 29.43000  ? 121 TRP B CB  1 
ATOM   3603 C  CG  . TRP B  1 127 ? 14.11100  8.86700   1.51900  1.000 28.74000  ? 121 TRP B CG  1 
ATOM   3604 C  CD1 . TRP B  1 127 ? 12.97800  8.77500   0.74600  1.000 26.09000  ? 121 TRP B CD1 1 
ATOM   3605 C  CD2 . TRP B  1 127 ? 13.76100  9.65600   2.65500  1.000 28.30000  ? 121 TRP B CD2 1 
ATOM   3606 N  NE1 . TRP B  1 127 ? 11.92500  9.48100   1.34700  1.000 27.93000  ? 121 TRP B NE1 1 
ATOM   3607 C  CE2 . TRP B  1 127 ? 12.39300  10.03800  2.51100  1.000 23.50000  ? 121 TRP B CE2 1 
ATOM   3608 C  CE3 . TRP B  1 127 ? 14.46900  10.08500  3.78000  1.000 25.45000  ? 121 TRP B CE3 1 
ATOM   3609 C  CZ2 . TRP B  1 127 ? 11.73700  10.80900  3.45100  1.000 25.32000  ? 121 TRP B CZ2 1 
ATOM   3610 C  CZ3 . TRP B  1 127 ? 13.80000  10.88400  4.71600  1.000 24.19000  ? 121 TRP B CZ3 1 
ATOM   3611 C  CH2 . TRP B  1 127 ? 12.45100  11.22600  4.53800  1.000 24.34000  ? 121 TRP B CH2 1 
ATOM   3612 N  N   . ILE B  1 128 ? 17.61700  6.18700   0.32000  1.000 30.44000  ? 122 ILE B N   1 
ATOM   3613 C  CA  . ILE B  1 128 ? 19.03200  5.86500   0.14900  1.000 31.90000  ? 122 ILE B CA  1 
ATOM   3614 C  C   . ILE B  1 128 ? 19.30500  5.47000   -1.28800 1.000 33.82000  ? 122 ILE B C   1 
ATOM   3615 O  O   . ILE B  1 128 ? 20.31800  5.87200   -1.88300 1.000 35.16000  ? 122 ILE B O   1 
ATOM   3616 C  CB  . ILE B  1 128 ? 19.44700  4.75400   1.12700  1.000 32.16000  ? 122 ILE B CB  1 
ATOM   3617 C  CG1 . ILE B  1 128 ? 19.49100  5.30700   2.54800  1.000 30.80000  ? 122 ILE B CG1 1 
ATOM   3618 C  CG2 . ILE B  1 128 ? 20.79100  4.14400   0.72400  1.000 34.17000  ? 122 ILE B CG2 1 
ATOM   3619 C  CD1 . ILE B  1 128 ? 19.46000  4.21800   3.63400  1.000 31.05000  ? 122 ILE B CD1 1 
ATOM   3620 N  N   . LYS B  1 129 ? 18.40800  4.67800   -1.87100 1.000 34.29000  ? 123 LYS B N   1 
ATOM   3621 C  CA  . LYS B  1 129 ? 18.60600  4.24000   -3.24600 1.000 36.40000  ? 123 LYS B CA  1 
ATOM   3622 C  C   . LYS B  1 129 ? 18.67900  5.41200   -4.21200 1.000 37.09000  ? 123 LYS B C   1 
ATOM   3623 O  O   . LYS B  1 129 ? 19.39100  5.33300   -5.22300 1.000 39.16000  ? 123 LYS B O   1 
ATOM   3624 C  CB  . LYS B  1 129 ? 17.48300  3.29700   -3.66800 1.000 36.97000  ? 123 LYS B CB  1 
ATOM   3625 C  CG  . LYS B  1 129 ? 17.55300  1.93600   -3.02000 1.000 37.33000  ? 123 LYS B CG  1 
ATOM   3626 C  CD  . LYS B  1 129 ? 16.51100  1.06000   -3.63200 1.000 38.51000  ? 123 LYS B CD  1 
ATOM   3627 C  CE  . LYS B  1 129 ? 16.33800  -0.23000  -2.87600 1.000 39.88000  ? 123 LYS B CE  1 
ATOM   3628 N  NZ  . LYS B  1 129 ? 15.92600  -1.31800  -3.82300 1.000 48.82000  ? 123 LYS B NZ  1 
ATOM   3629 N  N   . GLN B  1 130 ? 17.94100  6.48600   -3.93300 1.000 35.69000  ? 124 GLN B N   1 
ATOM   3630 C  CA  . GLN B  1 130 ? 17.88000  7.63600   -4.82300 1.000 40.48000  ? 124 GLN B CA  1 
ATOM   3631 C  C   . GLN B  1 130 ? 18.83000  8.75100   -4.40700 1.000 39.14000  ? 124 GLN B C   1 
ATOM   3632 O  O   . GLN B  1 130 ? 18.81700  9.82000   -5.02500 1.000 43.90000  ? 124 GLN B O   1 
ATOM   3633 C  CB  . GLN B  1 130 ? 16.45200  8.16700   -4.90400 1.000 43.08000  ? 124 GLN B CB  1 
ATOM   3634 C  CG  . GLN B  1 130 ? 15.41800  7.10900   -5.29400 1.000 46.94000  ? 124 GLN B CG  1 
ATOM   3635 C  CD  . GLN B  1 130 ? 13.96400  7.54500   -5.04000 1.000 60.67000  ? 124 GLN B CD  1 
ATOM   3636 O  OE1 . GLN B  1 130 ? 13.69800  8.58800   -4.42700 1.000 54.88000  ? 124 GLN B OE1 1 
ATOM   3637 N  NE2 . GLN B  1 130 ? 13.01700  6.73100   -5.51100 1.000 68.43000  ? 124 GLN B NE2 1 
ATOM   3638 N  N   . ASP B  1 131 ? 19.66400  8.52700   -3.38600 1.000 37.53000  ? 125 ASP B N   1 
ATOM   3639 C  CA  . ASP B  1 131 ? 20.57600  9.55700   -2.87500 1.000 37.10000  ? 125 ASP B CA  1 
ATOM   3640 C  C   . ASP B  1 131 ? 19.80700  10.82000  -2.48300 1.000 38.54000  ? 125 ASP B C   1 
ATOM   3641 O  O   . ASP B  1 131 ? 20.31600  11.93600  -2.60700 1.000 35.98000  ? 125 ASP B O   1 
ATOM   3642 C  CB  . ASP B  1 131 ? 21.68700  9.87700   -3.89000 1.000 39.23000  ? 125 ASP B CB  1 
ATOM   3643 C  CG  . ASP B  1 131 ? 22.82800  8.84600   -3.88100 1.000 39.62000  ? 125 ASP B CG  1 
ATOM   3644 O  OD1 . ASP B  1 131 ? 23.49300  8.66800   -2.83000 1.000 39.05000  ? 125 ASP B OD1 1 
ATOM   3645 O  OD2 . ASP B  1 131 ? 23.09100  8.23100   -4.94200 1.000 41.53000  ? 125 ASP B OD2 1 
ATOM   3646 N  N   . PHE B  1 132 ? 18.57100  10.63900  -2.01200 1.000 32.46000  ? 126 PHE B N   1 
ATOM   3647 C  CA  . PHE B  1 132 ? 17.70200  11.74700  -1.63300 1.000 34.56000  ? 126 PHE B CA  1 
ATOM   3648 C  C   . PHE B  1 132 ? 18.10100  12.34100  -0.28600 1.000 34.60000  ? 126 PHE B C   1 
ATOM   3649 O  O   . PHE B  1 132 ? 18.31300  11.61700  0.69900  1.000 34.84000  ? 126 PHE B O   1 
ATOM   3650 C  CB  . PHE B  1 132 ? 16.25100  11.27800  -1.58500 1.000 29.97000  ? 126 PHE B CB  1 
ATOM   3651 C  CG  . PHE B  1 132 ? 15.27200  12.32500  -1.10900 1.000 32.13000  ? 126 PHE B CG  1 
ATOM   3652 C  CD1 . PHE B  1 132 ? 14.95400  13.41200  -1.90700 1.000 33.04000  ? 126 PHE B CD1 1 
ATOM   3653 C  CD2 . PHE B  1 132 ? 14.62500  12.18900  0.11200  1.000 27.53000  ? 126 PHE B CD2 1 
ATOM   3654 C  CE1 . PHE B  1 132 ? 14.02900  14.34700  -1.48300 1.000 33.26000  ? 126 PHE B CE1 1 
ATOM   3655 C  CE2 . PHE B  1 132 ? 13.70700  13.12800  0.54500  1.000 32.38000  ? 126 PHE B CE2 1 
ATOM   3656 C  CZ  . PHE B  1 132 ? 13.40200  14.20700  -0.25200 1.000 30.87000  ? 126 PHE B CZ  1 
ATOM   3657 N  N   . ILE B  1 133 ? 18.20600  13.66600  -0.25900 1.000 30.69000  ? 127 ILE B N   1 
ATOM   3658 C  CA  . ILE B  1 133 ? 18.46700  14.43000  0.95500  1.000 29.19000  ? 127 ILE B CA  1 
ATOM   3659 C  C   . ILE B  1 133 ? 17.12900  14.97900  1.45000  1.000 30.78000  ? 127 ILE B C   1 
ATOM   3660 O  O   . ILE B  1 133 ? 16.56500  15.89600  0.81700  1.000 30.74000  ? 127 ILE B O   1 
ATOM   3661 C  CB  . ILE B  1 133 ? 19.47700  15.55400  0.69700  1.000 32.07000  ? 127 ILE B CB  1 
ATOM   3662 C  CG1 . ILE B  1 133 ? 20.82300  14.95900  0.26000  1.000 38.83000  ? 127 ILE B CG1 1 
ATOM   3663 C  CG2 . ILE B  1 133 ? 19.62400  16.41200  1.94700  1.000 35.11000  ? 127 ILE B CG2 1 
ATOM   3664 C  CD1 . ILE B  1 133 ? 21.83000  15.98400  -0.22800 1.000 44.21000  ? 127 ILE B CD1 1 
ATOM   3665 N  N   . PRO B  1 134 ? 16.57800  14.45400  2.53600  1.000 28.51000  ? 128 PRO B N   1 
ATOM   3666 C  CA  . PRO B  1 134 ? 15.31400  14.99400  3.04100  1.000 27.58000  ? 128 PRO B CA  1 
ATOM   3667 C  C   . PRO B  1 134 ? 15.46300  16.45500  3.42700  1.000 26.44000  ? 128 PRO B C   1 
ATOM   3668 O  O   . PRO B  1 134 ? 16.52900  16.90000  3.85400  1.000 24.94000  ? 128 PRO B O   1 
ATOM   3669 C  CB  . PRO B  1 134 ? 15.01000  14.12200  4.26400  1.000 26.89000  ? 128 PRO B CB  1 
ATOM   3670 C  CG  . PRO B  1 134 ? 16.30500  13.50900  4.64200  1.000 23.20000  ? 128 PRO B CG  1 
ATOM   3671 C  CD  . PRO B  1 134 ? 17.14100  13.41300  3.40800  1.000 26.29000  ? 128 PRO B CD  1 
ATOM   3672 N  N   . THR B  1 135 ? 14.36000  17.19400  3.29400  1.000 27.15000  ? 129 THR B N   1 
ATOM   3673 C  CA  . THR B  1 135 ? 14.29900  18.63500  3.54100  1.000 25.44000  ? 129 THR B CA  1 
ATOM   3674 C  C   . THR B  1 135 ? 13.21700  18.93400  4.57500  1.000 22.63000  ? 129 THR B C   1 
ATOM   3675 O  O   . THR B  1 135 ? 12.58000  18.02600  5.12400  1.000 22.34000  ? 129 THR B O   1 
ATOM   3676 C  CB  . THR B  1 135 ? 14.02300  19.41500  2.24700  1.000 29.92000  ? 129 THR B CB  1 
ATOM   3677 O  OG1 . THR B  1 135 ? 12.72400  19.06700  1.75400  1.000 27.47000  ? 129 THR B OG1 1 
ATOM   3678 C  CG2 . THR B  1 135 ? 15.06400  19.07200  1.18100  1.000 29.03000  ? 129 THR B CG2 1 
ATOM   3679 N  N   . ALA B  1 136 ? 12.98900  20.23000  4.80400  1.000 24.90000  ? 130 ALA B N   1 
ATOM   3680 C  CA  . ALA B  1 136 ? 12.05400  20.65200  5.84600  1.000 26.46000  ? 130 ALA B CA  1 
ATOM   3681 C  C   . ALA B  1 136 ? 10.70300  19.96200  5.72200  1.000 20.49000  ? 130 ALA B C   1 
ATOM   3682 O  O   . ALA B  1 136 ? 10.12000  19.53600  6.72400  1.000 19.96000  ? 130 ALA B O   1 
ATOM   3683 C  CB  . ALA B  1 136 ? 11.86200  22.15900  5.79800  1.000 22.81000  ? 130 ALA B CB  1 
ATOM   3684 N  N   . VAL B  1 137 ? 10.17400  19.86500  4.50000  1.000 22.90000  ? 131 VAL B N   1 
ATOM   3685 C  CA  . VAL B  1 137 ? 8.83600   19.32300  4.31600  1.000 20.97000  ? 131 VAL B CA  1 
ATOM   3686 C  C   . VAL B  1 137 ? 8.75400   17.84800  4.68400  1.000 21.77000  ? 131 VAL B C   1 
ATOM   3687 O  O   . VAL B  1 137 ? 7.65300   17.33200  4.90700  1.000 23.45000  ? 131 VAL B O   1 
ATOM   3688 C  CB  . VAL B  1 137 ? 8.36300   19.57500  2.87200  1.000 22.63000  ? 131 VAL B CB  1 
ATOM   3689 C  CG1 . VAL B  1 137 ? 8.96500   18.55100  1.91000  1.000 26.17000  ? 131 VAL B CG1 1 
ATOM   3690 C  CG2 . VAL B  1 137 ? 6.85000   19.59300  2.79100  1.000 22.53000  ? 131 VAL B CG2 1 
ATOM   3691 N  N   . CYS B  1 138 ? 9.89400   17.17700  4.82100  1.000 20.05000  ? 132 CYS B N   1 
ATOM   3692 C  CA  . CYS B  1 138 ? 9.93400   15.77900  5.19400  1.000 21.05000  ? 132 CYS B CA  1 
ATOM   3693 C  C   . CYS B  1 138 ? 9.96900   15.53800  6.69100  1.000 20.09000  ? 132 CYS B C   1 
ATOM   3694 O  O   . CYS B  1 138 ? 9.93700   14.36300  7.10300  1.000 21.97000  ? 132 CYS B O   1 
ATOM   3695 C  CB  . CYS B  1 138 ? 11.18500  15.10700  4.57100  1.000 22.15000  ? 132 CYS B CB  1 
ATOM   3696 S  SG  . CYS B  1 138 ? 11.30100  15.25900  2.76800  1.000 28.36000  ? 132 CYS B SG  1 
ATOM   3697 N  N   . SER B  1 139 ? 10.09000  16.59100  7.50400  1.000 18.40000  ? 133 SER B N   1 
ATOM   3698 C  CA  . SER B  1 139 ? 10.26600  16.40600  8.93600  1.000 18.49000  ? 133 SER B CA  1 
ATOM   3699 C  C   . SER B  1 139 ? 9.10300   15.61800  9.51100  1.000 20.92000  ? 133 SER B C   1 
ATOM   3700 O  O   . SER B  1 139 ? 7.94700   15.89200  9.17700  1.000 20.87000  ? 133 SER B O   1 
ATOM   3701 C  CB  . SER B  1 139 ? 10.35900  17.75300  9.62300  1.000 18.53000  ? 133 SER B CB  1 
ATOM   3702 O  OG  . SER B  1 139 ? 10.12200  17.64100  11.00000 1.000 21.18000  ? 133 SER B OG  1 
ATOM   3703 N  N   . ASN B  1 140 ? 9.40300   14.64800  10.39200 1.000 18.18000  ? 134 ASN B N   1 
ATOM   3704 C  CA  . ASN B  1 140 ? 8.32300   13.97200  11.09800 1.000 17.28000  ? 134 ASN B CA  1 
ATOM   3705 C  C   . ASN B  1 140 ? 7.41100   14.94000  11.85300 1.000 19.80000  ? 134 ASN B C   1 
ATOM   3706 O  O   . ASN B  1 140 ? 6.30300   14.55400  12.22400 1.000 17.88000  ? 134 ASN B O   1 
ATOM   3707 C  CB  . ASN B  1 140 ? 8.86300   12.93900  12.07700 1.000 19.68000  ? 134 ASN B CB  1 
ATOM   3708 C  CG  . ASN B  1 140 ? 9.35800   13.55300  13.37800 1.000 23.16000  ? 134 ASN B CG  1 
ATOM   3709 O  OD1 . ASN B  1 140 ? 8.71800   13.41000  14.44300 1.000 23.89000  ? 134 ASN B OD1 1 
ATOM   3710 N  ND2 . ASN B  1 140 ? 10.51000  14.17500  13.32100 1.000 20.64000  ? 134 ASN B ND2 1 
ATOM   3711 N  N   . CYS B  1 141 ? 7.85700   16.17700  12.09800 1.000 17.81000  ? 135 CYS B N   1 
ATOM   3712 C  CA  . CYS B  1 141 ? 7.07500   17.17700  12.80200 1.000 20.31000  ? 135 CYS B CA  1 
ATOM   3713 C  C   . CYS B  1 141 ? 6.48200   18.20000  11.85800 1.000 18.22000  ? 135 CYS B C   1 
ATOM   3714 O  O   . CYS B  1 141 ? 6.06000   19.27600  12.30700 1.000 18.55000  ? 135 CYS B O   1 
ATOM   3715 C  CB  . CYS B  1 141 ? 7.95300   17.88100  13.84200 1.000 21.18000  ? 135 CYS B CB  1 
ATOM   3716 S  SG  . CYS B  1 141 ? 8.70600   16.70900  14.98300 1.000 21.13000  ? 135 CYS B SG  1 
ATOM   3717 N  N   . SER B  1 142 ? 6.46400   17.91100  10.55500 1.000 18.34000  ? 136 SER B N   1 
ATOM   3718 C  CA  . SER B  1 142 ? 6.10800   18.96000  9.60200  1.000 19.74000  ? 136 SER B CA  1 
ATOM   3719 C  C   . SER B  1 142 ? 4.67000   19.41900  9.80600  1.000 18.27000  ? 136 SER B C   1 
ATOM   3720 O  O   . SER B  1 142 ? 4.36700   20.58900  9.59900  1.000 20.23000  ? 136 SER B O   1 
ATOM   3721 C  CB  . SER B  1 142 ? 6.28800   18.47700  8.16500  1.000 21.39000  ? 136 SER B CB  1 
ATOM   3722 O  OG  . SER B  1 142 ? 5.46700   17.33900  7.92600  1.000 21.66000  ? 136 SER B OG  1 
ATOM   3723 N  N   . GLY B  1 143 ? 3.77600   18.51400  10.21700 1.000 17.76000  ? 137 GLY B N   1 
ATOM   3724 C  CA  . GLY B  1 143 ? 2.38600   18.92700  10.42700 1.000 18.57000  ? 137 GLY B CA  1 
ATOM   3725 C  C   . GLY B  1 143 ? 2.24400   19.89700  11.58400 1.000 18.71000  ? 137 GLY B C   1 
ATOM   3726 O  O   . GLY B  1 143 ? 1.46900   20.85800  11.51500 1.000 22.10000  ? 137 GLY B O   1 
ATOM   3727 N  N   . LYS B  1 144 ? 2.97400   19.64100  12.66800 1.000 18.76000  ? 138 LYS B N   1 
ATOM   3728 C  CA  . LYS B  1 144 ? 3.01500   20.55400  13.79600 1.000 17.79000  ? 138 LYS B CA  1 
ATOM   3729 C  C   . LYS B  1 144 ? 3.52500   21.92400  13.37000 1.000 21.01000  ? 138 LYS B C   1 
ATOM   3730 O  O   . LYS B  1 144 ? 2.95200   22.96200  13.73700 1.000 18.40000  ? 138 LYS B O   1 
ATOM   3731 C  CB  . LYS B  1 144 ? 3.89600   19.94200  14.89500 1.000 18.11000  ? 138 LYS B CB  1 
ATOM   3732 C  CG  . LYS B  1 144 ? 4.21000   20.89300  16.00900 1.000 20.99000  ? 138 LYS B CG  1 
ATOM   3733 C  CD  . LYS B  1 144 ? 4.96900   20.18900  17.10700 1.000 19.63000  ? 138 LYS B CD  1 
ATOM   3734 C  CE  . LYS B  1 144 ? 6.28100   19.60700  16.61000 1.000 18.75000  ? 138 LYS B CE  1 
ATOM   3735 N  NZ  . LYS B  1 144 ? 7.00500   19.24700  17.84800 1.000 19.19000  ? 138 LYS B NZ  1 
ATOM   3736 N  N   . HIS B  1 145 ? 4.60800   21.95100  12.58500 1.000 18.20000  ? 139 HIS B N   1 
ATOM   3737 C  CA  . HIS B  1 145 ? 5.16000   23.24000  12.17100 1.000 19.13000  ? 139 HIS B CA  1 
ATOM   3738 C  C   . HIS B  1 145 ? 4.20800   23.99400  11.25500 1.000 18.59000  ? 139 HIS B C   1 
ATOM   3739 O  O   . HIS B  1 145 ? 4.11000   25.22800  11.33900 1.000 18.67000  ? 139 HIS B O   1 
ATOM   3740 C  CB  . HIS B  1 145 ? 6.52400   23.01900  11.51600 1.000 18.72000  ? 139 HIS B CB  1 
ATOM   3741 C  CG  . HIS B  1 145 ? 7.60900   22.80700  12.52000 1.000 19.66000  ? 139 HIS B CG  1 
ATOM   3742 N  ND1 . HIS B  1 145 ? 8.50800   23.79800  12.84200 1.000 17.46000  ? 139 HIS B ND1 1 
ATOM   3743 C  CD2 . HIS B  1 145 ? 7.88200   21.76000  13.34500 1.000 17.83000  ? 139 HIS B CD2 1 
ATOM   3744 C  CE1 . HIS B  1 145 ? 9.31400   23.36400  13.79500 1.000 19.36000  ? 139 HIS B CE1 1 
ATOM   3745 N  NE2 . HIS B  1 145 ? 8.96600   22.12800  14.10800 1.000 19.46000  ? 139 HIS B NE2 1 
ATOM   3746 N  N   . VAL B  1 146 ? 3.49300   23.29300  10.37700 1.000 16.01000  ? 140 VAL B N   1 
ATOM   3747 C  CA  . VAL B  1 146 ? 2.53200   24.02100  9.54700  1.000 18.65000  ? 140 VAL B CA  1 
ATOM   3748 C  C   . VAL B  1 146 ? 1.43400   24.60900  10.42600 1.000 17.90000  ? 140 VAL B C   1 
ATOM   3749 O  O   . VAL B  1 146 ? 0.98200   25.74500  10.20400 1.000 19.31000  ? 140 VAL B O   1 
ATOM   3750 C  CB  . VAL B  1 146 ? 1.95500   23.13100  8.43700  1.000 17.22000  ? 140 VAL B CB  1 
ATOM   3751 C  CG1 . VAL B  1 146 ? 0.84400   23.85400  7.69200  1.000 18.44000  ? 140 VAL B CG1 1 
ATOM   3752 C  CG2 . VAL B  1 146 ? 3.05500   22.78700  7.43700  1.000 17.63000  ? 140 VAL B CG2 1 
ATOM   3753 N  N   . GLY B  1 147 ? 1.01000   23.85900  11.44800 1.000 15.77000  ? 141 GLY B N   1 
ATOM   3754 C  CA  . GLY B  1 147 ? -0.00300  24.38000  12.35100 1.000 18.79000  ? 141 GLY B CA  1 
ATOM   3755 C  C   . GLY B  1 147 ? 0.46800   25.63000  13.06000 1.000 18.37000  ? 141 GLY B C   1 
ATOM   3756 O  O   . GLY B  1 147 ? -0.30000  26.56600  13.26100 1.000 17.27000  ? 141 GLY B O   1 
ATOM   3757 N  N   . MET B  1 148 ? 1.73300   25.65000  13.47200 1.000 19.03000  ? 142 MET B N   1 
ATOM   3758 C  CA  A MET B  1 148 ? 2.30200   26.80400  14.16900 0.500 18.52000  ? 142 MET B CA  1 
ATOM   3759 C  CA  B MET B  1 148 ? 2.23400   26.82200  14.17900 0.500 18.51000  ? 142 MET B CA  1 
ATOM   3760 C  C   . MET B  1 148 ? 2.41000   28.00600  13.24100 1.000 19.94000  ? 142 MET B C   1 
ATOM   3761 O  O   . MET B  1 148 ? 2.17700   29.14400  13.65400 1.000 22.30000  ? 142 MET B O   1 
ATOM   3762 C  CB  A MET B  1 148 ? 3.68100   26.44100  14.72300 0.500 18.57000  ? 142 MET B CB  1 
ATOM   3763 C  CB  B MET B  1 148 ? 3.53500   26.48600  14.89800 0.500 18.64000  ? 142 MET B CB  1 
ATOM   3764 C  CG  A MET B  1 148 ? 3.67300   25.29200  15.71200 0.500 20.93000  ? 142 MET B CG  1 
ATOM   3765 C  CG  B MET B  1 148 ? 3.28200   25.88100  16.26700 0.500 21.35000  ? 142 MET B CG  1 
ATOM   3766 S  SD  A MET B  1 148 ? 3.10600   25.84100  17.33400 0.500 24.55000  ? 142 MET B SD  1 
ATOM   3767 S  SD  B MET B  1 148 ? 4.72700   25.02100  16.87700 0.500 19.45000  ? 142 MET B SD  1 
ATOM   3768 C  CE  A MET B  1 148 ? 2.73200   24.26100  18.09600 0.500 18.24000  ? 142 MET B CE  1 
ATOM   3769 C  CE  B MET B  1 148 ? 4.10800   24.20200  18.34100 0.500 15.65000  ? 142 MET B CE  1 
ATOM   3770 N  N   . LEU B  1 149 ? 2.77400   27.75900  11.98800 1.000 18.22000  ? 143 LEU B N   1 
ATOM   3771 C  CA  . LEU B  1 149 ? 2.74000   28.80100  10.97000 1.000 19.12000  ? 143 LEU B CA  1 
ATOM   3772 C  C   . LEU B  1 149 ? 1.33600   29.35300  10.79600 1.000 20.87000  ? 143 LEU B C   1 
ATOM   3773 O  O   . LEU B  1 149 ? 1.14100   30.56900  10.62500 1.000 18.59000  ? 143 LEU B O   1 
ATOM   3774 C  CB  . LEU B  1 149 ? 3.21600   28.20900  9.64500  1.000 20.47000  ? 143 LEU B CB  1 
ATOM   3775 C  CG  . LEU B  1 149 ? 4.71800   28.23900  9.43200  1.000 23.32000  ? 143 LEU B CG  1 
ATOM   3776 C  CD1 . LEU B  1 149 ? 5.07700   27.45800  8.18200  1.000 26.40000  ? 143 LEU B CD1 1 
ATOM   3777 C  CD2 . LEU B  1 149 ? 5.18400   29.69400  9.29600  1.000 24.24000  ? 143 LEU B CD2 1 
ATOM   3778 N  N   . ALA B  1 150 ? 0.36200   28.44600  10.73800 1.000 19.21000  ? 144 ALA B N   1 
ATOM   3779 C  CA  . ALA B  1 150 ? -1.03000  28.82700  10.58300 1.000 20.23000  ? 144 ALA B CA  1 
ATOM   3780 C  C   . ALA B  1 150 ? -1.45700  29.72000  11.73000 1.000 19.94000  ? 144 ALA B C   1 
ATOM   3781 O  O   . ALA B  1 150 ? -2.02500  30.78400  11.51300 1.000 18.20000  ? 144 ALA B O   1 
ATOM   3782 C  CB  . ALA B  1 150 ? -1.91300  27.57600  10.49800 1.000 18.15000  ? 144 ALA B CB  1 
ATOM   3783 N  N   . GLY B  1 151 ? -1.16900  29.31000  12.96600 1.000 17.49000  ? 145 GLY B N   1 
ATOM   3784 C  CA  . GLY B  1 151 ? -1.50500  30.15800  14.10500 1.000 21.70000  ? 145 GLY B CA  1 
ATOM   3785 C  C   . GLY B  1 151 ? -0.82400  31.51000  14.05900 1.000 23.22000  ? 145 GLY B C   1 
ATOM   3786 O  O   . GLY B  1 151 ? -1.46400  32.54700  14.27300 1.000 21.12000  ? 145 GLY B O   1 
ATOM   3787 N  N   . ALA B  1 152 ? 0.48200   31.52300  13.77800 1.000 19.68000  ? 146 ALA B N   1 
ATOM   3788 C  CA  . ALA B  1 152 ? 1.17500   32.81000  13.64300 1.000 21.52000  ? 146 ALA B CA  1 
ATOM   3789 C  C   . ALA B  1 152 ? 0.49500   33.71900  12.61700 1.000 23.15000  ? 146 ALA B C   1 
ATOM   3790 O  O   . ALA B  1 152 ? 0.30500   34.91900  12.86000 1.000 21.65000  ? 146 ALA B O   1 
ATOM   3791 C  CB  . ALA B  1 152 ? 2.65700   32.59000  13.26300 1.000 19.98000  ? 146 ALA B CB  1 
ATOM   3792 N  N   . ARG B  1 153 ? 0.11000   33.16700  11.46700 1.000 21.02000  ? 147 ARG B N   1 
ATOM   3793 C  CA  . ARG B  1 153 ? -0.50600  33.98900  10.42900 1.000 23.41000  ? 147 ARG B CA  1 
ATOM   3794 C  C   . ARG B  1 153 ? -1.85400  34.53800  10.88700 1.000 23.16000  ? 147 ARG B C   1 
ATOM   3795 O  O   . ARG B  1 153 ? -2.17400  35.71000  10.65500 1.000 25.75000  ? 147 ARG B O   1 
ATOM   3796 C  CB  . ARG B  1 153 ? -0.68500  33.15700  9.15800  1.000 25.47000  ? 147 ARG B CB  1 
ATOM   3797 C  CG  . ARG B  1 153 ? 0.56600   33.03200  8.32400  1.000 30.02000  ? 147 ARG B CG  1 
ATOM   3798 C  CD  . ARG B  1 153 ? 0.53400   33.96500  7.11700  1.000 33.55000  ? 147 ARG B CD  1 
ATOM   3799 N  NE  . ARG B  1 153 ? 1.82000   34.01500  6.41900  1.000 46.32000  ? 147 ARG B NE  1 
ATOM   3800 C  CZ  . ARG B  1 153 ? 2.08600   33.38200  5.28300  1.000 42.18000  ? 147 ARG B CZ  1 
ATOM   3801 N  NH1 . ARG B  1 153 ? 1.19500   32.59200  4.70800  1.000 41.02000  ? 147 ARG B NH1 1 
ATOM   3802 N  NH2 . ARG B  1 153 ? 3.27000   33.56200  4.69600  1.000 39.55000  ? 147 ARG B NH2 1 
ATOM   3803 N  N   . ALA B  1 154 ? -2.63800  33.69000  11.54300 1.000 23.52000  ? 148 ALA B N   1 
ATOM   3804 C  CA  . ALA B  1 154 ? -4.02700  33.99800  11.86700 1.000 21.65000  ? 148 ALA B CA  1 
ATOM   3805 C  C   . ALA B  1 154 ? -4.12300  35.15900  12.83000 1.000 23.23000  ? 148 ALA B C   1 
ATOM   3806 O  O   . ALA B  1 154 ? -5.09900  35.91700  12.78800 1.000 24.87000  ? 148 ALA B O   1 
ATOM   3807 C  CB  . ALA B  1 154 ? -4.69700  32.77100  12.48600 1.000 24.10000  ? 148 ALA B CB  1 
ATOM   3808 N  N   . ILE B  1 155 ? -3.12100  35.31200  13.70100 1.000 23.84000  ? 149 ILE B N   1 
ATOM   3809 C  CA  . ILE B  1 155 ? -3.15100  36.36000  14.70200 1.000 24.21000  ? 149 ILE B CA  1 
ATOM   3810 C  C   . ILE B  1 155 ? -2.36100  37.58200  14.27900 1.000 26.92000  ? 149 ILE B C   1 
ATOM   3811 O  O   . ILE B  1 155 ? -2.38500  38.60000  14.99500 1.000 24.60000  ? 149 ILE B O   1 
ATOM   3812 C  CB  . ILE B  1 155 ? -2.66200  35.85000  16.07500 1.000 23.66000  ? 149 ILE B CB  1 
ATOM   3813 C  CG1 . ILE B  1 155 ? -1.24100  35.30600  16.02500 1.000 24.26000  ? 149 ILE B CG1 1 
ATOM   3814 C  CG2 . ILE B  1 155 ? -3.66600  34.83000  16.65600 1.000 24.47000  ? 149 ILE B CG2 1 
ATOM   3815 C  CD1 . ILE B  1 155 ? -0.73300  34.94200  17.43200 1.000 25.54000  ? 149 ILE B CD1 1 
ATOM   3816 N  N   . GLY B  1 156 ? -1.71300  37.53100  13.11300 1.000 32.13000  ? 150 GLY B N   1 
ATOM   3817 C  CA  . GLY B  1 156 ? -1.01400  38.67000  12.56900 1.000 34.16000  ? 150 GLY B CA  1 
ATOM   3818 C  C   . GLY B  1 156 ? 0.37200   38.82900  13.13000 1.000 32.58000  ? 150 GLY B C   1 
ATOM   3819 O  O   . GLY B  1 156 ? 0.93500   39.92600  13.06700 1.000 34.42000  ? 150 GLY B O   1 
ATOM   3820 N  N   . ALA B  1 157 ? 0.93300   37.75000  13.67200 1.000 35.75000  ? 151 ALA B N   1 
ATOM   3821 C  CA  . ALA B  1 157 ? 2.17200   37.80300  14.43400 1.000 40.94000  ? 151 ALA B CA  1 
ATOM   3822 C  C   . ALA B  1 157 ? 3.41000   37.84600  13.55800 1.000 43.59000  ? 151 ALA B C   1 
ATOM   3823 O  O   . ALA B  1 157 ? 4.46700   38.30400  14.01200 1.000 45.98000  ? 151 ALA B O   1 
ATOM   3824 C  CB  . ALA B  1 157 ? 2.26800   36.59400  15.35900 1.000 25.96000  ? 151 ALA B CB  1 
ATOM   3825 N  N   . GLY B  1 158 ? 3.32000   37.38300  12.32700 1.000 35.13000  ? 152 GLY B N   1 
ATOM   3826 C  CA  . GLY B  1 158 ? 4.54400   37.34600  11.56300 1.000 43.23000  ? 152 GLY B CA  1 
ATOM   3827 C  C   . GLY B  1 158 ? 5.09600   35.94900  11.70100 1.000 33.76000  ? 152 GLY B C   1 
ATOM   3828 O  O   . GLY B  1 158 ? 5.03800   35.35500  12.77800 1.000 29.70000  ? 152 GLY B O   1 
ATOM   3829 N  N   . THR B  1 159 ? 5.60200   35.41000  10.60200 1.000 32.51000  ? 153 THR B N   1 
ATOM   3830 C  CA  . THR B  1 159 ? 5.93500   34.00200  10.53600 1.000 35.67000  ? 153 THR B CA  1 
ATOM   3831 C  C   . THR B  1 159 ? 7.41200   33.69900  10.73800 1.000 34.16000  ? 153 THR B C   1 
ATOM   3832 O  O   . THR B  1 159 ? 7.73400   32.55000  11.03500 1.000 31.16000  ? 153 THR B O   1 
ATOM   3833 C  CB  . THR B  1 159 ? 5.51400   33.42900  9.17900  1.000 35.64000  ? 153 THR B CB  1 
ATOM   3834 O  OG1 . THR B  1 159 ? 6.02300   34.28500  8.14600  1.000 37.16000  ? 153 THR B OG1 1 
ATOM   3835 C  CG2 . THR B  1 159 ? 4.01200   33.38000  9.07600  1.000 36.24000  ? 153 THR B CG2 1 
ATOM   3836 N  N   . ASP B  1 160 ? 8.32000   34.67100  10.60100 1.000 31.10000  ? 154 ASP B N   1 
ATOM   3837 C  CA  . ASP B  1 160 ? 9.72700   34.29300  10.42900 1.000 36.81000  ? 154 ASP B CA  1 
ATOM   3838 C  C   . ASP B  1 160 ? 10.30200  33.59600  11.66200 1.000 37.87000  ? 154 ASP B C   1 
ATOM   3839 O  O   . ASP B  1 160 ? 11.16600  32.71300  11.52600 1.000 38.71000  ? 154 ASP B O   1 
ATOM   3840 C  CB  . ASP B  1 160 ? 10.59200  35.50500  10.05100 1.000 44.49000  ? 154 ASP B CB  1 
ATOM   3841 C  CG  . ASP B  1 160 ? 12.08200  35.12700  9.85000  1.000 55.03000  ? 154 ASP B CG  1 
ATOM   3842 O  OD1 . ASP B  1 160 ? 12.38500  34.20400  9.05500  1.000 54.99000  ? 154 ASP B OD1 1 
ATOM   3843 O  OD2 . ASP B  1 160 ? 12.96200  35.75200  10.48500 1.000 66.15000  ? 154 ASP B OD2 1 
ATOM   3844 N  N   . GLY B  1 161 ? 9.85500   33.96400  12.86100 1.000 31.81000  ? 155 GLY B N   1 
ATOM   3845 C  CA  . GLY B  1 161 ? 10.35800  33.28400  14.04200 1.000 26.64000  ? 155 GLY B CA  1 
ATOM   3846 C  C   . GLY B  1 161 ? 9.27000   32.59500  14.83700 1.000 24.14000  ? 155 GLY B C   1 
ATOM   3847 O  O   . GLY B  1 161 ? 9.29000   32.64100  16.07400 1.000 22.67000  ? 155 GLY B O   1 
ATOM   3848 N  N   . TYR B  1 162 ? 8.31400   31.94300  14.15400 1.000 23.34000  ? 156 TYR B N   1 
ATOM   3849 C  CA  . TYR B  1 162 ? 7.19800   31.32400  14.87100 1.000 20.60000  ? 156 TYR B CA  1 
ATOM   3850 C  C   . TYR B  1 162 ? 7.66400   30.27400  15.85800 1.000 20.91000  ? 156 TYR B C   1 
ATOM   3851 O  O   . TYR B  1 162 ? 6.90900   29.90800  16.76200 1.000 19.11000  ? 156 TYR B O   1 
ATOM   3852 C  CB  . TYR B  1 162 ? 6.21600   30.65900  13.91100 1.000 23.66000  ? 156 TYR B CB  1 
ATOM   3853 C  CG  . TYR B  1 162 ? 6.74500   29.39400  13.23700 1.000 21.79000  ? 156 TYR B CG  1 
ATOM   3854 C  CD1 . TYR B  1 162 ? 6.64700   28.12200  13.85000 1.000 21.64000  ? 156 TYR B CD1 1 
ATOM   3855 C  CD2 . TYR B  1 162 ? 7.32100   29.46000  11.98900 1.000 24.34000  ? 156 TYR B CD2 1 
ATOM   3856 C  CE1 . TYR B  1 162 ? 7.13500   26.98000  13.22400 1.000 20.73000  ? 156 TYR B CE1 1 
ATOM   3857 C  CE2 . TYR B  1 162 ? 7.82200   28.29100  11.34800 1.000 24.68000  ? 156 TYR B CE2 1 
ATOM   3858 C  CZ  . TYR B  1 162 ? 7.70700   27.07300  11.98800 1.000 23.20000  ? 156 TYR B CZ  1 
ATOM   3859 O  OH  . TYR B  1 162 ? 8.18100   25.96900  11.35200 1.000 24.67000  ? 156 TYR B OH  1 
ATOM   3860 N  N   . HIS B  1 163 ? 8.85700   29.74800  15.66500 1.000 21.99000  ? 157 HIS B N   1 
ATOM   3861 C  CA  . HIS B  1 163 ? 9.39100   28.66600  16.46700 1.000 22.66000  ? 157 HIS B CA  1 
ATOM   3862 C  C   . HIS B  1 163 ? 10.16700  29.15800  17.67900 1.000 23.39000  ? 157 HIS B C   1 
ATOM   3863 O  O   . HIS B  1 163 ? 10.63500  28.33200  18.47100 1.000 24.36000  ? 157 HIS B O   1 
ATOM   3864 C  CB  . HIS B  1 163 ? 10.32300  27.80100  15.60500 1.000 23.17000  ? 157 HIS B CB  1 
ATOM   3865 C  CG  . HIS B  1 163 ? 11.50900  28.54800  15.09600 1.000 26.15000  ? 157 HIS B CG  1 
ATOM   3866 N  ND1 . HIS B  1 163 ? 11.39600  29.72200  14.37900 1.000 24.58000  ? 157 HIS B ND1 1 
ATOM   3867 C  CD2 . HIS B  1 163 ? 12.83700  28.29400  15.19200 1.000 27.70000  ? 157 HIS B CD2 1 
ATOM   3868 C  CE1 . HIS B  1 163 ? 12.59800  30.16400  14.06300 1.000 27.17000  ? 157 HIS B CE1 1 
ATOM   3869 N  NE2 . HIS B  1 163 ? 13.49200  29.32100  14.54900 1.000 27.65000  ? 157 HIS B NE2 1 
ATOM   3870 N  N   . LEU B  1 164 ? 10.31300  30.50000  17.84800 1.000 20.24000  ? 158 LEU B N   1 
ATOM   3871 C  CA  . LEU B  1 164 ? 11.16100  31.02500  18.90500 1.000 26.65000  ? 158 LEU B CA  1 
ATOM   3872 C  C   . LEU B  1 164 ? 10.36700  31.18300  20.19500 1.000 26.61000  ? 158 LEU B C   1 
ATOM   3873 O  O   . LEU B  1 164 ? 9.18100   31.52000  20.16000 1.000 26.80000  ? 158 LEU B O   1 
ATOM   3874 C  CB  . LEU B  1 164 ? 11.75100  32.38000  18.48700 1.000 29.05000  ? 158 LEU B CB  1 
ATOM   3875 C  CG  . LEU B  1 164 ? 12.60200  32.30500  17.21500 1.000 31.40000  ? 158 LEU B CG  1 
ATOM   3876 C  CD1 . LEU B  1 164 ? 13.16500  33.68100  16.80500 1.000 33.09000  ? 158 LEU B CD1 1 
ATOM   3877 C  CD2 . LEU B  1 164 ? 13.75700  31.25800  17.33800 1.000 27.68000  ? 158 LEU B CD2 1 
ATOM   3878 N  N   . PRO B  1 165 ? 10.98800  30.98400  21.36100 1.000 28.58000  ? 159 PRO B N   1 
ATOM   3879 C  CA  . PRO B  1 165 ? 10.21200  31.07100  22.61400 1.000 28.07000  ? 159 PRO B CA  1 
ATOM   3880 C  C   . PRO B  1 165 ? 9.50200   32.40700  22.82800 1.000 27.43000  ? 159 PRO B C   1 
ATOM   3881 O  O   . PRO B  1 165 ? 8.41900   32.42300  23.42100 1.000 33.92000  ? 159 PRO B O   1 
ATOM   3882 C  CB  . PRO B  1 165 ? 11.26900  30.80900  23.69600 1.000 37.26000  ? 159 PRO B CB  1 
ATOM   3883 C  CG  . PRO B  1 165 ? 12.35800  30.04900  22.99300 1.000 33.27000  ? 159 PRO B CG  1 
ATOM   3884 C  CD  . PRO B  1 165 ? 12.39600  30.60500  21.60000 1.000 30.43000  ? 159 PRO B CD  1 
ATOM   3885 N  N   . ASP B  1 166 ? 10.05500  33.53400  22.35800 1.000 31.68000  ? 160 ASP B N   1 
ATOM   3886 C  CA  . ASP B  1 166 ? 9.37500   34.80800  22.59000 1.000 30.07000  ? 160 ASP B CA  1 
ATOM   3887 C  C   . ASP B  1 166 ? 8.21400   35.05900  21.62000 1.000 28.50000  ? 160 ASP B C   1 
ATOM   3888 O  O   . ASP B  1 166 ? 7.50300   36.05300  21.77600 1.000 29.49000  ? 160 ASP B O   1 
ATOM   3889 C  CB  . ASP B  1 166 ? 10.36600  35.96000  22.52700 1.000 34.42000  ? 160 ASP B CB  1 
ATOM   3890 C  CG  . ASP B  1 166 ? 10.88600  36.21800  21.11400 1.000 48.34000  ? 160 ASP B CG  1 
ATOM   3891 O  OD1 . ASP B  1 166 ? 11.44200  35.27700  20.50200 1.000 47.19000  ? 160 ASP B OD1 1 
ATOM   3892 O  OD2 . ASP B  1 166 ? 10.76000  37.36800  20.61700 1.000 54.54000  ? 160 ASP B OD2 1 
ATOM   3893 N  N   . HIS B  1 167 ? 8.00900   34.20600  20.62800 1.000 24.66000  ? 161 HIS B N   1 
ATOM   3894 C  CA  . HIS B  1 167 ? 6.89000   34.37700  19.70800 1.000 24.89000  ? 161 HIS B CA  1 
ATOM   3895 C  C   . HIS B  1 167 ? 5.56800   34.04800  20.40500 1.000 20.34000  ? 161 HIS B C   1 
ATOM   3896 O  O   . HIS B  1 167 ? 5.50400   33.11100  21.20800 1.000 22.17000  ? 161 HIS B O   1 
ATOM   3897 C  CB  . HIS B  1 167 ? 7.08900   33.46400  18.50000 1.000 23.10000  ? 161 HIS B CB  1 
ATOM   3898 C  CG  . HIS B  1 167 ? 6.19000   33.77900  17.34600 1.000 21.79000  ? 161 HIS B CG  1 
ATOM   3899 N  ND1 . HIS B  1 167 ? 4.87200   33.40300  17.31500 1.000 20.79000  ? 161 HIS B ND1 1 
ATOM   3900 C  CD2 . HIS B  1 167 ? 6.43200   34.41200  16.17400 1.000 22.48000  ? 161 HIS B CD2 1 
ATOM   3901 C  CE1 . HIS B  1 167 ? 4.33200   33.79800  16.17300 1.000 24.26000  ? 161 HIS B CE1 1 
ATOM   3902 N  NE2 . HIS B  1 167 ? 5.26500   34.40000  15.45900 1.000 25.20000  ? 161 HIS B NE2 1 
ATOM   3903 N  N   . PRO B  1 168 ? 4.48300   34.77800  20.11600 1.000 21.85000  ? 162 PRO B N   1 
ATOM   3904 C  CA  . PRO B  1 168 ? 3.20600   34.43500  20.78700 1.000 18.90000  ? 162 PRO B CA  1 
ATOM   3905 C  C   . PRO B  1 168 ? 2.74600   33.00100  20.58900 1.000 18.31000  ? 162 PRO B C   1 
ATOM   3906 O  O   . PRO B  1 168 ? 2.02800   32.48700  21.45500 1.000 18.33000  ? 162 PRO B O   1 
ATOM   3907 C  CB  . PRO B  1 168 ? 2.19800   35.41600  20.16900 1.000 20.87000  ? 162 PRO B CB  1 
ATOM   3908 C  CG  . PRO B  1 168 ? 2.86600   35.93900  18.90000 1.000 21.41000  ? 162 PRO B CG  1 
ATOM   3909 C  CD  . PRO B  1 168 ? 4.33300   35.92600  19.20200 1.000 21.40000  ? 162 PRO B CD  1 
ATOM   3910 N  N   . MET B  1 169 ? 3.00900   32.37300  19.44500 1.000 16.33000  ? 163 MET B N   1 
ATOM   3911 C  CA  A MET B  1 169 ? 2.59900   30.97700  19.29200 0.600 19.43000  ? 163 MET B CA  1 
ATOM   3912 C  CA  B MET B  1 169 ? 2.58900   30.98400  19.30600 0.400 19.43000  ? 163 MET B CA  1 
ATOM   3913 C  C   . MET B  1 169 ? 3.28300   30.09900  20.32800 1.000 20.57000  ? 163 MET B C   1 
ATOM   3914 O  O   . MET B  1 169 ? 2.68100   29.15000  20.84400 1.000 19.37000  ? 163 MET B O   1 
ATOM   3915 C  CB  A MET B  1 169 ? 2.88900   30.46900  17.87600 0.600 18.13000  ? 163 MET B CB  1 
ATOM   3916 C  CB  B MET B  1 169 ? 2.83400   30.47600  17.88600 0.400 18.16000  ? 163 MET B CB  1 
ATOM   3917 C  CG  A MET B  1 169 ? 1.88400   30.95800  16.84500 0.600 20.71000  ? 163 MET B CG  1 
ATOM   3918 C  CG  B MET B  1 169 ? 1.57500   30.53000  17.03900 0.400 21.43000  ? 163 MET B CG  1 
ATOM   3919 S  SD  A MET B  1 169 ? 0.16200   30.72800  17.38000 0.600 19.62000  ? 163 MET B SD  1 
ATOM   3920 S  SD  B MET B  1 169 ? 0.59300   28.99800  17.01700 0.400 20.46000  ? 163 MET B SD  1 
ATOM   3921 C  CE  A MET B  1 169 ? 0.04100   28.95300  17.53900 0.600 20.27000  ? 163 MET B CE  1 
ATOM   3922 C  CE  B MET B  1 169 ? 0.16600   28.70200  18.73800 0.400 18.32000  ? 163 MET B CE  1 
ATOM   3923 N  N   . GLN B  1 170 ? 4.53800   30.39700  20.64700 1.000 19.65000  ? 164 GLN B N   1 
ATOM   3924 C  CA  . GLN B  1 170 ? 5.22100   29.59700  21.65600 1.000 17.99000  ? 164 GLN B CA  1 
ATOM   3925 C  C   . GLN B  1 170 ? 4.80400   29.98300  23.07000 1.000 20.49000  ? 164 GLN B C   1 
ATOM   3926 O  O   . GLN B  1 170 ? 4.76300   29.11700  23.94400 1.000 20.64000  ? 164 GLN B O   1 
ATOM   3927 C  CB  . GLN B  1 170 ? 6.74500   29.71600  21.48600 1.000 19.56000  ? 164 GLN B CB  1 
ATOM   3928 C  CG  . GLN B  1 170 ? 7.24100   29.15700  20.13600 1.000 21.10000  ? 164 GLN B CG  1 
ATOM   3929 C  CD  . GLN B  1 170 ? 6.61500   27.81200  19.77700 1.000 19.55000  ? 164 GLN B CD  1 
ATOM   3930 O  OE1 . GLN B  1 170 ? 6.48200   26.94700  20.62600 1.000 18.59000  ? 164 GLN B OE1 1 
ATOM   3931 N  NE2 . GLN B  1 170 ? 6.19600   27.65300  18.53100 1.000 20.59000  ? 164 GLN B NE2 1 
ATOM   3932 N  N   . GLY B  1 171 ? 4.51500   31.26400  23.33900 1.000 19.14000  ? 165 GLY B N   1 
ATOM   3933 C  CA  . GLY B  1 171 ? 3.85300   31.58100  24.59800 1.000 18.58000  ? 165 GLY B CA  1 
ATOM   3934 C  C   . GLY B  1 171 ? 2.55100   30.80600  24.75900 1.000 20.03000  ? 165 GLY B C   1 
ATOM   3935 O  O   . GLY B  1 171 ? 2.21800   30.33900  25.85500 1.000 18.84000  ? 165 GLY B O   1 
ATOM   3936 N  N   . ARG B  1 172 ? 1.78300   30.68200  23.67600 1.000 17.36000  ? 166 ARG B N   1 
ATOM   3937 C  CA  . ARG B  1 172 ? 0.52400   29.95200  23.77100 1.000 19.93000  ? 166 ARG B CA  1 
ATOM   3938 C  C   . ARG B  1 172 ? 0.77600   28.47900  24.05700 1.000 17.67000  ? 166 ARG B C   1 
ATOM   3939 O  O   . ARG B  1 172 ? 0.10200   27.87500  24.90700 1.000 17.55000  ? 166 ARG B O   1 
ATOM   3940 C  CB  . ARG B  1 172 ? -0.28000  30.13400  22.48800 1.000 20.10000  ? 166 ARG B CB  1 
ATOM   3941 C  CG  . ARG B  1 172 ? -0.96700  31.48600  22.40600 1.000 20.08000  ? 166 ARG B CG  1 
ATOM   3942 C  CD  . ARG B  1 172 ? -1.43500  31.78500  21.00500 1.000 19.50000  ? 166 ARG B CD  1 
ATOM   3943 N  NE  . ARG B  1 172 ? -2.25900  32.98900  20.97900 1.000 19.82000  ? 166 ARG B NE  1 
ATOM   3944 C  CZ  . ARG B  1 172 ? -3.58700  32.97900  20.94100 1.000 21.86000  ? 166 ARG B CZ  1 
ATOM   3945 N  NH1 . ARG B  1 172 ? -4.27300  31.82900  20.86700 1.000 21.62000  ? 166 ARG B NH1 1 
ATOM   3946 N  NH2 . ARG B  1 172 ? -4.24300  34.13700  21.00100 1.000 22.97000  ? 166 ARG B NH2 1 
ATOM   3947 N  N   . VAL B  1 173 ? 1.77000   27.89300  23.37800 1.000 15.65000  ? 167 VAL B N   1 
ATOM   3948 C  CA  . VAL B  1 173 ? 2.12600   26.49800  23.62500 1.000 17.93000  ? 167 VAL B CA  1 
ATOM   3949 C  C   . VAL B  1 173 ? 2.50100   26.29800  25.09200 1.000 18.87000  ? 167 VAL B C   1 
ATOM   3950 O  O   . VAL B  1 173 ? 2.01500   25.36900  25.75900 1.000 18.69000  ? 167 VAL B O   1 
ATOM   3951 C  CB  . VAL B  1 173 ? 3.28000   26.06900  22.69200 1.000 18.40000  ? 167 VAL B CB  1 
ATOM   3952 C  CG1 . VAL B  1 173 ? 3.84800   24.75000  23.11500 1.000 16.83000  ? 167 VAL B CG1 1 
ATOM   3953 C  CG2 . VAL B  1 173 ? 2.80500   25.95700  21.26700 1.000 18.96000  ? 167 VAL B CG2 1 
ATOM   3954 N  N   . LYS B  1 174 ? 3.38000   27.16700  25.61300 1.000 18.42000  ? 168 LYS B N   1 
ATOM   3955 C  CA  . LYS B  1 174 ? 3.87100   26.98700  26.97500 1.000 18.64000  ? 168 LYS B CA  1 
ATOM   3956 C  C   . LYS B  1 174 ? 2.71700   27.07400  27.96800 1.000 20.49000  ? 168 LYS B C   1 
ATOM   3957 O  O   . LYS B  1 174 ? 2.58900   26.23800  28.86900 1.000 17.45000  ? 168 LYS B O   1 
ATOM   3958 C  CB  . LYS B  1 174 ? 4.97000   28.00600  27.30000 1.000 22.35000  ? 168 LYS B CB  1 
ATOM   3959 C  CG  . LYS B  1 174 ? 6.30700   27.72000  26.59500 1.000 23.51000  ? 168 LYS B CG  1 
ATOM   3960 C  CD  . LYS B  1 174 ? 7.43100   28.65600  27.09600 1.000 29.66000  ? 168 LYS B CD  1 
ATOM   3961 C  CE  . LYS B  1 174 ? 8.79300   28.44100  26.37800 1.000 32.70000  ? 168 LYS B CE  1 
ATOM   3962 N  NZ  . LYS B  1 174 ? 8.69600   28.40600  24.86000 1.000 28.15000  ? 168 LYS B NZ  1 
ATOM   3963 N  N   . ARG B  1 175 ? 1.85000   28.06500  27.80000 1.000 15.60000  ? 169 ARG B N   1 
ATOM   3964 C  CA  A ARG B  1 175 ? 0.70500   28.18100  28.69400 0.500 17.72000  ? 169 ARG B CA  1 
ATOM   3965 C  CA  B ARG B  1 175 ? 0.70100   28.18100  28.69200 0.500 17.72000  ? 169 ARG B CA  1 
ATOM   3966 C  C   . ARG B  1 175 ? -0.19500  26.95600  28.58200 1.000 19.73000  ? 169 ARG B C   1 
ATOM   3967 O  O   . ARG B  1 175 ? -0.67100  26.42800  29.60000 1.000 18.31000  ? 169 ARG B O   1 
ATOM   3968 C  CB  A ARG B  1 175 ? -0.05400  29.46800  28.38200 0.500 20.03000  ? 169 ARG B CB  1 
ATOM   3969 C  CB  B ARG B  1 175 ? -0.08200  29.45400  28.37900 0.500 20.04000  ? 169 ARG B CB  1 
ATOM   3970 C  CG  A ARG B  1 175 ? -1.05900  29.85900  29.43000 0.500 23.72000  ? 169 ARG B CG  1 
ATOM   3971 C  CG  B ARG B  1 175 ? -1.49800  29.42600  28.91500 0.500 22.11000  ? 169 ARG B CG  1 
ATOM   3972 C  CD  A ARG B  1 175 ? -1.44300  31.33300  29.30400 0.500 24.04000  ? 169 ARG B CD  1 
ATOM   3973 C  CD  B ARG B  1 175 ? -2.19100  30.77600  28.75100 0.500 23.62000  ? 169 ARG B CD  1 
ATOM   3974 N  NE  A ARG B  1 175 ? -1.84800  31.70200  27.95500 0.500 23.66000  ? 169 ARG B NE  1 
ATOM   3975 N  NE  B ARG B  1 175 ? -2.48900  31.09000  27.36100 0.500 23.37000  ? 169 ARG B NE  1 
ATOM   3976 C  CZ  A ARG B  1 175 ? -1.14600  32.49000  27.15600 0.500 22.12000  ? 169 ARG B CZ  1 
ATOM   3977 C  CZ  B ARG B  1 175 ? -3.46600  30.52100  26.66800 0.500 25.26000  ? 169 ARG B CZ  1 
ATOM   3978 N  NH1 A ARG B  1 175 ? 0.04800   32.93600  27.50400 0.500 23.22000  ? 169 ARG B NH1 1 
ATOM   3979 N  NH1 B ARG B  1 175 ? -4.18400  29.53000  27.17700 0.500 23.28000  ? 169 ARG B NH1 1 
ATOM   3980 N  NH2 A ARG B  1 175 ? -1.66700  32.86100  25.99100 0.500 21.52000  ? 169 ARG B NH2 1 
ATOM   3981 N  NH2 B ARG B  1 175 ? -3.74200  30.96900  25.44400 0.500 25.53000  ? 169 ARG B NH2 1 
ATOM   3982 N  N   . THR B  1 176 ? -0.41500  26.46900  27.35500 1.000 16.55000  ? 170 THR B N   1 
ATOM   3983 C  CA  . THR B  1 176 ? -1.37200  25.38000  27.16400 1.000 19.21000  ? 170 THR B CA  1 
ATOM   3984 C  C   . THR B  1 176 ? -0.86300  24.07200  27.76800 1.000 17.41000  ? 170 THR B C   1 
ATOM   3985 O  O   . THR B  1 176 ? -1.64400  23.31500  28.36300 1.000 18.52000  ? 170 THR B O   1 
ATOM   3986 C  CB  . THR B  1 176 ? -1.66700  25.18600  25.68600 1.000 21.03000  ? 170 THR B CB  1 
ATOM   3987 O  OG1 . THR B  1 176 ? -2.14500  26.40100  25.14200 1.000 22.03000  ? 170 THR B OG1 1 
ATOM   3988 C  CG2 . THR B  1 176 ? -2.73200  24.11700  25.46800 1.000 19.27000  ? 170 THR B CG2 1 
ATOM   3989 N  N   . VAL B  1 177 ? 0.43000   23.78800  27.61900 1.000 19.30000  ? 171 VAL B N   1 
ATOM   3990 C  CA  . VAL B  1 177 ? 1.00500   22.58800  28.22400 1.000 16.05000  ? 171 VAL B CA  1 
ATOM   3991 C  C   . VAL B  1 177 ? 0.83000   22.62700  29.72900 1.000 16.17000  ? 171 VAL B C   1 
ATOM   3992 O  O   . VAL B  1 177 ? 0.36300   21.65900  30.34600 1.000 18.72000  ? 171 VAL B O   1 
ATOM   3993 C  CB  . VAL B  1 177 ? 2.49400   22.45700  27.84900 1.000 18.31000  ? 171 VAL B CB  1 
ATOM   3994 C  CG1 . VAL B  1 177 ? 3.14900   21.33100  28.70700 1.000 16.03000  ? 171 VAL B CG1 1 
ATOM   3995 C  CG2 . VAL B  1 177 ? 2.64000   22.19700  26.34700 1.000 17.67000  ? 171 VAL B CG2 1 
ATOM   3996 N  N   . ALA B  1 178 ? 1.19900   23.74700  30.34800 1.000 17.33000  ? 172 ALA B N   1 
ATOM   3997 C  CA  . ALA B  1 178 ? 1.08600   23.82500  31.80200 1.000 22.10000  ? 172 ALA B CA  1 
ATOM   3998 C  C   . ALA B  1 178 ? -0.36300  23.66500  32.24300 1.000 21.33000  ? 172 ALA B C   1 
ATOM   3999 O  O   . ALA B  1 178 ? -0.65300  23.00900  33.25700 1.000 20.22000  ? 172 ALA B O   1 
ATOM   4000 C  CB  . ALA B  1 178 ? 1.64100   25.14600  32.31800 1.000 21.34000  ? 172 ALA B CB  1 
ATOM   4001 N  N   . GLU B  1 179 ? -1.28100  24.22300  31.47300 1.000 18.03000  ? 173 GLU B N   1 
ATOM   4002 C  CA  . GLU B  1 179 ? -2.69000  24.15900  31.85100 1.000 19.08000  ? 173 GLU B CA  1 
ATOM   4003 C  C   . GLU B  1 179 ? -3.20100  22.72300  31.78900 1.000 20.55000  ? 173 GLU B C   1 
ATOM   4004 O  O   . GLU B  1 179 ? -3.85300  22.24300  32.72700 1.000 22.94000  ? 173 GLU B O   1 
ATOM   4005 C  CB  . GLU B  1 179 ? -3.51600  25.09900  30.96200 1.000 19.76000  ? 173 GLU B CB  1 
ATOM   4006 C  CG  . GLU B  1 179 ? -3.41100  26.58100  31.41300 1.000 22.28000  ? 173 GLU B CG  1 
ATOM   4007 C  CD  . GLU B  1 179 ? -4.04900  27.56000  30.44200 1.000 27.86000  ? 173 GLU B CD  1 
ATOM   4008 O  OE1 . GLU B  1 179 ? -4.49300  27.12500  29.36400 1.000 25.19000  ? 173 GLU B OE1 1 
ATOM   4009 O  OE2 . GLU B  1 179 ? -4.14100  28.76900  30.78300 1.000 26.32000  ? 173 GLU B OE2 1 
ATOM   4010 N  N   . LEU B  1 180 ? -2.87500  22.00200  30.71200 1.000 17.77000  ? 174 LEU B N   1 
ATOM   4011 C  CA  . LEU B  1 180 ? -3.31500  20.61500  30.61500 1.000 18.58000  ? 174 LEU B CA  1 
ATOM   4012 C  C   . LEU B  1 180 ? -2.68200  19.75800  31.69300 1.000 18.28000  ? 174 LEU B C   1 
ATOM   4013 O  O   . LEU B  1 180 ? -3.32100  18.82000  32.17900 1.000 20.68000  ? 174 LEU B O   1 
ATOM   4014 C  CB  . LEU B  1 180 ? -3.01900  20.04300  29.23200 1.000 16.67000  ? 174 LEU B CB  1 
ATOM   4015 C  CG  . LEU B  1 180 ? -3.80000  20.64400  28.08000 1.000 19.86000  ? 174 LEU B CG  1 
ATOM   4016 C  CD1 . LEU B  1 180 ? -3.16000  20.17600  26.79900 1.000 21.20000  ? 174 LEU B CD1 1 
ATOM   4017 C  CD2 . LEU B  1 180 ? -5.30400  20.18900  28.17700 1.000 17.79000  ? 174 LEU B CD2 1 
ATOM   4018 N  N   . CYS B  1 181 ? -1.42000  20.04700  32.08200 1.000 18.47000  ? 175 CYS B N   1 
ATOM   4019 C  CA  . CYS B  1 181 ? -0.77100  19.27800  33.15100 1.000 16.20000  ? 175 CYS B CA  1 
ATOM   4020 C  C   . CYS B  1 181 ? -1.25900  19.67800  34.53200 1.000 19.68000  ? 175 CYS B C   1 
ATOM   4021 O  O   . CYS B  1 181 ? -0.87600  19.03400  35.51400 1.000 18.82000  ? 175 CYS B O   1 
ATOM   4022 C  CB  . CYS B  1 181 ? 0.75500   19.47800  33.14100 1.000 17.86000  ? 175 CYS B CB  1 
ATOM   4023 S  SG  . CYS B  1 181 ? 1.58100   18.85000  31.71100 1.000 17.93000  ? 175 CYS B SG  1 
ATOM   4024 N  N   . ASP B  1 182 ? -2.04200  20.74800  34.61500 1.000 21.01000  ? 176 ASP B N   1 
ATOM   4025 C  CA  . ASP B  1 182 ? -2.41800  21.39300  35.87500 1.000 21.31000  ? 176 ASP B CA  1 
ATOM   4026 C  C   . ASP B  1 182 ? -1.18800  21.73100  36.71700 1.000 21.54000  ? 176 ASP B C   1 
ATOM   4027 O  O   . ASP B  1 182 ? -1.14300  21.49900  37.92700 1.000 22.94000  ? 176 ASP B O   1 
ATOM   4028 C  CB  . ASP B  1 182 ? -3.41100  20.53200  36.65700 1.000 20.88000  ? 176 ASP B CB  1 
ATOM   4029 C  CG  . ASP B  1 182 ? -4.66300  20.23900  35.86500 1.000 25.25000  ? 176 ASP B CG  1 
ATOM   4030 O  OD1 . ASP B  1 182 ? -5.17200  21.18500  35.21700 1.000 27.60000  ? 176 ASP B OD1 1 
ATOM   4031 O  OD2 . ASP B  1 182 ? -5.13300  19.06500  35.88700 1.000 23.70000  ? 176 ASP B OD2 1 
ATOM   4032 N  N   . LEU B  1 183 ? -0.20200  22.34900  36.06800 1.000 21.67000  ? 177 LEU B N   1 
ATOM   4033 C  CA  . LEU B  1 183 ? 1.03600   22.75200  36.70900 1.000 22.42000  ? 177 LEU B CA  1 
ATOM   4034 C  C   . LEU B  1 183 ? 1.22700   24.25100  36.59000 1.000 22.52000  ? 177 LEU B C   1 
ATOM   4035 O  O   . LEU B  1 183 ? 0.80400   24.86500  35.61700 1.000 22.13000  ? 177 LEU B O   1 
ATOM   4036 C  CB  . LEU B  1 183 ? 2.24100   22.08600  36.07400 1.000 21.44000  ? 177 LEU B CB  1 
ATOM   4037 C  CG  . LEU B  1 183 ? 2.27100   20.58100  36.29000 1.000 21.32000  ? 177 LEU B CG  1 
ATOM   4038 C  CD1 . LEU B  1 183 ? 3.40500   20.05800  35.44600 1.000 19.87000  ? 177 LEU B CD1 1 
ATOM   4039 C  CD2 . LEU B  1 183 ? 2.49700   20.28900  37.77400 1.000 24.48000  ? 177 LEU B CD2 1 
ATOM   4040 N  N   . ASP B  1 184 ? 1.90900   24.81600  37.56700 1.000 21.25000  ? 178 ASP B N   1 
ATOM   4041 C  CA  . ASP B  1 184 ? 2.41400   26.17300  37.41300 1.000 24.11000  ? 178 ASP B CA  1 
ATOM   4042 C  C   . ASP B  1 184 ? 3.53300   26.19700  36.38000 1.000 23.54000  ? 178 ASP B C   1 
ATOM   4043 O  O   . ASP B  1 184 ? 4.20300   25.18400  36.13600 1.000 20.14000  ? 178 ASP B O   1 
ATOM   4044 C  CB  . ASP B  1 184 ? 2.91400   26.70300  38.75100 1.000 24.49000  ? 178 ASP B CB  1 
ATOM   4045 C  CG  . ASP B  1 184 ? 1.79900   26.81800  39.78500 1.000 34.31000  ? 178 ASP B CG  1 
ATOM   4046 O  OD1 . ASP B  1 184 ? 0.66000   27.23200  39.43900 1.000 36.80000  ? 178 ASP B OD1 1 
ATOM   4047 O  OD2 . ASP B  1 184 ? 2.06800   26.48500  40.95700 1.000 39.71000  ? 178 ASP B OD2 1 
ATOM   4048 N  N   . ALA B  1 185 ? 3.71500   27.37100  35.76000 1.000 21.36000  ? 179 ALA B N   1 
ATOM   4049 C  CA  . ALA B  1 185 ? 4.69200   27.51600  34.68600 1.000 19.06000  ? 179 ALA B CA  1 
ATOM   4050 C  C   . ALA B  1 185 ? 6.07000   27.03600  35.13000 1.000 18.90000  ? 179 ALA B C   1 
ATOM   4051 O  O   . ALA B  1 185 ? 6.80100   26.41800  34.35400 1.000 19.00000  ? 179 ALA B O   1 
ATOM   4052 C  CB  . ALA B  1 185 ? 4.77800   28.98600  34.24900 1.000 22.98000  ? 179 ALA B CB  1 
ATOM   4053 N  N   . GLY B  1 186 ? 6.43400   27.31500  36.37700 1.000 20.21000  ? 180 GLY B N   1 
ATOM   4054 C  CA  . GLY B  1 186 ? 7.75300   26.99000  36.85800 1.000 22.29000  ? 180 GLY B CA  1 
ATOM   4055 C  C   . GLY B  1 186 ? 7.97600   25.52600  37.08000 1.000 23.89000  ? 180 GLY B C   1 
ATOM   4056 O  O   . GLY B  1 186 ? 9.12500   25.12200  37.26900 1.000 23.61000  ? 180 GLY B O   1 
ATOM   4057 N  N   . ASP B  1 187 ? 6.91700   24.72400  37.06000 1.000 21.40000  ? 181 ASP B N   1 
ATOM   4058 C  CA  . ASP B  1 187 ? 7.06000   23.27700  37.20400 1.000 20.89000  ? 181 ASP B CA  1 
ATOM   4059 C  C   . ASP B  1 187 ? 7.14200   22.54800  35.85900 1.000 20.11000  ? 181 ASP B C   1 
ATOM   4060 O  O   . ASP B  1 187 ? 7.27900   21.31200  35.83400 1.000 21.36000  ? 181 ASP B O   1 
ATOM   4061 C  CB  . ASP B  1 187 ? 5.90800   22.75100  38.05800 1.000 22.93000  ? 181 ASP B CB  1 
ATOM   4062 C  CG  . ASP B  1 187 ? 6.06100   23.11800  39.53600 1.000 25.56000  ? 181 ASP B CG  1 
ATOM   4063 O  OD1 . ASP B  1 187 ? 7.20400   23.29200  40.00800 1.000 34.96000  ? 181 ASP B OD1 1 
ATOM   4064 O  OD2 . ASP B  1 187 ? 5.04700   23.23100  40.24300 1.000 34.48000  ? 181 ASP B OD2 1 
ATOM   4065 N  N   . VAL B  1 188 ? 7.09800   23.28400  34.75500 1.000 17.42000  ? 182 VAL B N   1 
ATOM   4066 C  CA  . VAL B  1 188 ? 7.40500   22.78400  33.42100 1.000 17.27000  ? 182 VAL B CA  1 
ATOM   4067 C  C   . VAL B  1 188 ? 8.71700   23.39700  32.96400 1.000 20.18000  ? 182 VAL B C   1 
ATOM   4068 O  O   . VAL B  1 188 ? 8.86000   24.63800  32.95900 1.000 18.76000  ? 182 VAL B O   1 
ATOM   4069 C  CB  . VAL B  1 188 ? 6.31000   23.13400  32.40900 1.000 18.99000  ? 182 VAL B CB  1 
ATOM   4070 C  CG1 . VAL B  1 188 ? 6.67200   22.55500  31.03700 1.000 16.61000  ? 182 VAL B CG1 1 
ATOM   4071 C  CG2 . VAL B  1 188 ? 4.95800   22.66600  32.90000 1.000 18.08000  ? 182 VAL B CG2 1 
ATOM   4072 N  N   . GLU B  1 189 ? 9.66600   22.53100  32.57000 1.000 19.07000  ? 183 GLU B N   1 
ATOM   4073 C  CA  A GLU B  1 189 ? 10.94400  22.96100  32.02500 0.600 20.44000  ? 183 GLU B CA  1 
ATOM   4074 C  CA  B GLU B  1 189 ? 10.96100  22.92500  32.02700 0.400 20.45000  ? 183 GLU B CA  1 
ATOM   4075 C  C   . GLU B  1 189 ? 10.95500  22.80800  30.50700 1.000 18.74000  ? 183 GLU B C   1 
ATOM   4076 O  O   . GLU B  1 189 ? 10.20300  22.01400  29.92700 1.000 18.89000  ? 183 GLU B O   1 
ATOM   4077 C  CB  A GLU B  1 189 ? 12.09400  22.18500  32.69000 0.600 22.54000  ? 183 GLU B CB  1 
ATOM   4078 C  CB  B GLU B  1 189 ? 12.09500  22.06500  32.60600 0.400 22.46000  ? 183 GLU B CB  1 
ATOM   4079 C  CG  A GLU B  1 189 ? 12.27700  22.64200  34.14400 0.600 22.72000  ? 183 GLU B CG  1 
ATOM   4080 C  CG  B GLU B  1 189 ? 12.33200  22.23000  34.10700 0.400 22.75000  ? 183 GLU B CG  1 
ATOM   4081 C  CD  A GLU B  1 189 ? 13.22700  21.79800  34.96000 0.600 25.57000  ? 183 GLU B CD  1 
ATOM   4082 C  CD  B GLU B  1 189 ? 12.87500  23.60400  34.49800 0.400 25.09000  ? 183 GLU B CD  1 
ATOM   4083 O  OE1 A GLU B  1 189 ? 14.10600  21.11200  34.37500 0.600 25.37000  ? 183 GLU B OE1 1 
ATOM   4084 O  OE1 B GLU B  1 189 ? 13.50200  24.29800  33.65200 0.400 23.39000  ? 183 GLU B OE1 1 
ATOM   4085 O  OE2 A GLU B  1 189 ? 13.08600  21.82000  36.20600 0.600 26.95000  ? 183 GLU B OE2 1 
ATOM   4086 O  OE2 B GLU B  1 189 ? 12.66700  23.99500  35.66900 0.400 25.95000  ? 183 GLU B OE2 1 
ATOM   4087 N  N   . TRP B  1 190 ? 11.80200  23.61100  29.85600 1.000 16.69000  ? 184 TRP B N   1 
ATOM   4088 C  CA  . TRP B  1 190 ? 11.80800  23.66700  28.40100 1.000 16.89000  ? 184 TRP B CA  1 
ATOM   4089 C  C   . TRP B  1 190 ? 13.21600  23.52600  27.86400 1.000 18.64000  ? 184 TRP B C   1 
ATOM   4090 O  O   . TRP B  1 190 ? 14.13000  24.18500  28.34900 1.000 22.68000  ? 184 TRP B O   1 
ATOM   4091 C  CB  . TRP B  1 190 ? 11.19100  25.00300  27.93000 1.000 18.28000  ? 184 TRP B CB  1 
ATOM   4092 C  CG  . TRP B  1 190 ? 9.77300   25.07000  28.34000 1.000 19.04000  ? 184 TRP B CG  1 
ATOM   4093 C  CD1 . TRP B  1 190 ? 9.28200   25.46400  29.55100 1.000 19.22000  ? 184 TRP B CD1 1 
ATOM   4094 C  CD2 . TRP B  1 190 ? 8.66000   24.66600  27.56000 1.000 17.63000  ? 184 TRP B CD2 1 
ATOM   4095 N  NE1 . TRP B  1 190 ? 7.90900   25.33000  29.57500 1.000 20.19000  ? 184 TRP B NE1 1 
ATOM   4096 C  CE2 . TRP B  1 190 ? 7.50200   24.84000  28.36300 1.000 20.40000  ? 184 TRP B CE2 1 
ATOM   4097 C  CE3 . TRP B  1 190 ? 8.51900   24.15600  26.27000 1.000 19.53000  ? 184 TRP B CE3 1 
ATOM   4098 C  CZ2 . TRP B  1 190 ? 6.21600   24.55600  27.89700 1.000 18.58000  ? 184 TRP B CZ2 1 
ATOM   4099 C  CZ3 . TRP B  1 190 ? 7.21100   23.83900  25.81600 1.000 18.61000  ? 184 TRP B CZ3 1 
ATOM   4100 C  CH2 . TRP B  1 190 ? 6.09700   24.04900  26.62700 1.000 16.14000  ? 184 TRP B CH2 1 
ATOM   4101 N  N   . GLY B  1 191 ? 13.37800  22.68200  26.85800 1.000 15.85000  ? 185 GLY B N   1 
ATOM   4102 C  CA  . GLY B  1 191 ? 14.58700  22.63300  26.05700 1.000 19.81000  ? 185 GLY B CA  1 
ATOM   4103 C  C   . GLY B  1 191 ? 14.22500  22.81300  24.59800 1.000 21.03000  ? 185 GLY B C   1 
ATOM   4104 O  O   . GLY B  1 191 ? 13.14300  23.30500  24.30600 1.000 20.63000  ? 185 GLY B O   1 
ATOM   4105 N  N   . THR B  1 192 ? 15.10000  22.41900  23.67900 1.000 18.09000  ? 186 THR B N   1 
ATOM   4106 C  CA  . THR B  1 192 ? 14.86600  22.54300  22.24600 1.000 19.60000  ? 186 THR B CA  1 
ATOM   4107 C  C   . THR B  1 192 ? 14.82700  21.14600  21.61900 1.000 20.89000  ? 186 THR B C   1 
ATOM   4108 O  O   . THR B  1 192 ? 15.68600  20.30900  21.91800 1.000 18.71000  ? 186 THR B O   1 
ATOM   4109 C  CB  . THR B  1 192 ? 15.96800  23.40800  21.61200 1.000 19.55000  ? 186 THR B CB  1 
ATOM   4110 O  OG1 . THR B  1 192 ? 15.87900  24.74700  22.15200 1.000 24.43000  ? 186 THR B OG1 1 
ATOM   4111 C  CG2 . THR B  1 192 ? 15.81300  23.43100  20.11100 1.000 19.97000  ? 186 THR B CG2 1 
ATOM   4112 N  N   . ASP B  1 193 ? 13.79800  20.88500  20.79500 1.000 21.62000  ? 187 ASP B N   1 
ATOM   4113 C  CA  . ASP B  1 193 ? 13.51100  19.60100  20.16800 1.000 17.91000  ? 187 ASP B CA  1 
ATOM   4114 C  C   . ASP B  1 193 ? 14.36500  19.39500  18.91700 1.000 20.01000  ? 187 ASP B C   1 
ATOM   4115 O  O   . ASP B  1 193 ? 15.02400  20.31200  18.42500 1.000 21.25000  ? 187 ASP B O   1 
ATOM   4116 C  CB  . ASP B  1 193 ? 12.01500  19.52000  19.81100 1.000 18.94000  ? 187 ASP B CB  1 
ATOM   4117 C  CG  . ASP B  1 193 ? 11.32700  18.27500  20.38100 1.000 25.84000  ? 187 ASP B CG  1 
ATOM   4118 O  OD1 . ASP B  1 193 ? 12.04800  17.29700  20.60300 1.000 24.61000  ? 187 ASP B OD1 1 
ATOM   4119 O  OD2 . ASP B  1 193 ? 10.06100  18.28600  20.59900 1.000 26.06000  ? 187 ASP B OD2 1 
ATOM   4120 N  N   . GLY B  1 194 ? 14.36000  18.15700  18.39300 1.000 18.79000  ? 188 GLY B N   1 
ATOM   4121 C  CA  . GLY B  1 194 ? 15.05400  17.90600  17.13000 1.000 22.82000  ? 188 GLY B CA  1 
ATOM   4122 C  C   . GLY B  1 194 ? 14.53600  18.74700  15.96800 1.000 19.47000  ? 188 GLY B C   1 
ATOM   4123 O  O   . GLY B  1 194 ? 15.28400  19.07700  15.04400 1.000 18.59000  ? 188 GLY B O   1 
ATOM   4124 N  N   . CYS B  1 195 ? 13.25300  19.13800  16.01400 1.000 17.52000  ? 189 CYS B N   1 
ATOM   4125 C  CA  . CYS B  1 195 ? 12.64800  19.94700  14.96400 1.000 19.50000  ? 189 CYS B CA  1 
ATOM   4126 C  C   . CYS B  1 195 ? 12.86500  21.44400  15.17800 1.000 22.93000  ? 189 CYS B C   1 
ATOM   4127 O  O   . CYS B  1 195 ? 12.40000  22.26400  14.36300 1.000 21.33000  ? 189 CYS B O   1 
ATOM   4128 C  CB  . CYS B  1 195 ? 11.15500  19.65200  14.89700 1.000 17.03000  ? 189 CYS B CB  1 
ATOM   4129 S  SG  . CYS B  1 195 ? 10.34800  20.28000  16.34300 1.000 20.42000  ? 189 CYS B SG  1 
ATOM   4130 N  N   . ASN B  1 196 ? 13.56100  21.80000  16.26000 1.000 18.20000  ? 190 ASN B N   1 
ATOM   4131 C  CA  . ASN B  1 196 ? 13.99100  23.14900  16.60500 1.000 18.44000  ? 190 ASN B CA  1 
ATOM   4132 C  C   . ASN B  1 196 ? 12.90700  24.00600  17.25800 1.000 19.99000  ? 190 ASN B C   1 
ATOM   4133 O  O   . ASN B  1 196 ? 13.05100  25.26300  17.30300 1.000 22.29000  ? 190 ASN B O   1 
ATOM   4134 C  CB  . ASN B  1 196 ? 14.56100  23.90700  15.41200 1.000 23.99000  ? 190 ASN B CB  1 
ATOM   4135 C  CG  . ASN B  1 196 ? 15.61800  24.87400  15.81900 1.000 24.61000  ? 190 ASN B CG  1 
ATOM   4136 O  OD1 . ASN B  1 196 ? 16.26900  24.68500  16.84100 1.000 26.31000  ? 190 ASN B OD1 1 
ATOM   4137 N  ND2 . ASN B  1 196 ? 15.81900  25.92500  15.02000 1.000 27.58000  ? 190 ASN B ND2 1 
ATOM   4138 N  N   . LEU B  1 197 ? 11.84000  23.39800  17.78500 1.000 17.13000  ? 191 LEU B N   1 
ATOM   4139 C  CA  . LEU B  1 197 ? 10.85000  24.06700  18.63100 1.000 17.54000  ? 191 LEU B CA  1 
ATOM   4140 C  C   . LEU B  1 197 ? 11.16700  23.86500  20.10200 1.000 17.71000  ? 191 LEU B C   1 
ATOM   4141 O  O   . LEU B  1 197 ? 11.82300  22.90300  20.48500 1.000 19.38000  ? 191 LEU B O   1 
ATOM   4142 C  CB  . LEU B  1 197 ? 9.44600   23.49200  18.37900 1.000 16.33000  ? 191 LEU B CB  1 
ATOM   4143 C  CG  . LEU B  1 197 ? 8.73300   23.89100  17.09500 1.000 19.85000  ? 191 LEU B CG  1 
ATOM   4144 C  CD1 . LEU B  1 197 ? 7.51600   22.99500  17.01300 1.000 17.90000  ? 191 LEU B CD1 1 
ATOM   4145 C  CD2 . LEU B  1 197 ? 8.31100   25.36600  17.15900 1.000 22.27000  ? 191 LEU B CD2 1 
ATOM   4146 N  N   . PRO B  1 198 ? 10.66800  24.73800  20.96500 1.000 19.88000  ? 192 PRO B N   1 
ATOM   4147 C  CA  . PRO B  1 198 ? 10.69800  24.44100  22.39900 1.000 19.51000  ? 192 PRO B CA  1 
ATOM   4148 C  C   . PRO B  1 198 ? 9.96400   23.13800  22.68800 1.000 18.39000  ? 192 PRO B C   1 
ATOM   4149 O  O   . PRO B  1 198 ? 8.95900   22.81800  22.05300 1.000 16.08000  ? 192 PRO B O   1 
ATOM   4150 C  CB  . PRO B  1 198 ? 9.98200   25.65500  23.02400 1.000 21.11000  ? 192 PRO B CB  1 
ATOM   4151 C  CG  . PRO B  1 198 ? 10.08400  26.76700  21.96700 1.000 22.19000  ? 192 PRO B CG  1 
ATOM   4152 C  CD  . PRO B  1 198 ? 10.02900  26.02800  20.65800 1.000 19.40000  ? 192 PRO B CD  1 
ATOM   4153 N  N   . THR B  1 199 ? 10.47300  22.37800  23.65900 1.000 18.15000  ? 193 THR B N   1 
ATOM   4154 C  CA  . THR B  1 199 ? 9.85700   21.11700  23.99700 1.000 16.93000  ? 193 THR B CA  1 
ATOM   4155 C  C   . THR B  1 199 ? 9.80000   20.97400  25.51500 1.000 18.59000  ? 193 THR B C   1 
ATOM   4156 O  O   . THR B  1 199 ? 10.72400  21.37000  26.20900 1.000 17.24000  ? 193 THR B O   1 
ATOM   4157 C  CB  . THR B  1 199 ? 10.58500  19.93100  23.32100 1.000 15.79000  ? 193 THR B CB  1 
ATOM   4158 O  OG1 . THR B  1 199 ? 9.79200   18.73400  23.46900 1.000 18.00000  ? 193 THR B OG1 1 
ATOM   4159 C  CG2 . THR B  1 199 ? 12.05200  19.71000  23.86200 1.000 16.02000  ? 193 THR B CG2 1 
ATOM   4160 N  N   . PRO B  1 200 ? 8.68600   20.50700  26.06500 1.000 18.37000  ? 194 PRO B N   1 
ATOM   4161 C  CA  . PRO B  1 200 ? 8.51100   20.50300  27.52400 1.000 18.23000  ? 194 PRO B CA  1 
ATOM   4162 C  C   . PRO B  1 200 ? 8.96800   19.23200  28.23600 1.000 16.16000  ? 194 PRO B C   1 
ATOM   4163 O  O   . PRO B  1 200 ? 8.95000   18.11900  27.70200 1.000 15.13000  ? 194 PRO B O   1 
ATOM   4164 C  CB  . PRO B  1 200 ? 6.97900   20.65600  27.66000 1.000 17.68000  ? 194 PRO B CB  1 
ATOM   4165 C  CG  . PRO B  1 200 ? 6.49300   19.84200  26.54600 1.000 13.99000  ? 194 PRO B CG  1 
ATOM   4166 C  CD  . PRO B  1 200 ? 7.41700   20.23400  25.37000 1.000 16.79000  ? 194 PRO B CD  1 
ATOM   4167 N  N   . ALA B  1 201 ? 9.32900   19.42300  29.50000 1.000 16.09000  ? 195 ALA B N   1 
ATOM   4168 C  CA  . ALA B  1 201 ? 9.53100   18.34700  30.46000 1.000 13.17000  ? 195 ALA B CA  1 
ATOM   4169 C  C   . ALA B  1 201 ? 8.69100   18.61300  31.69300 1.000 15.33000  ? 195 ALA B C   1 
ATOM   4170 O  O   . ALA B  1 201 ? 8.65400   19.73700  32.20900 1.000 17.42000  ? 195 ALA B O   1 
ATOM   4171 C  CB  . ALA B  1 201 ? 10.99900  18.19400  30.89400 1.000 16.23000  ? 195 ALA B CB  1 
ATOM   4172 N  N   . PHE B  1 202 ? 8.05800   17.56000  32.18700 1.000 15.34000  ? 196 PHE B N   1 
ATOM   4173 C  CA  . PHE B  1 202 ? 7.22600   17.65600  33.37300 1.000 15.56000  ? 196 PHE B CA  1 
ATOM   4174 C  C   . PHE B  1 202 ? 7.10200   16.25800  33.95600 1.000 16.80000  ? 196 PHE B C   1 
ATOM   4175 O  O   . PHE B  1 202 ? 7.59100   15.29100  33.36100 1.000 16.98000  ? 196 PHE B O   1 
ATOM   4176 C  CB  . PHE B  1 202 ? 5.85800   18.29800  33.04200 1.000 17.75000  ? 196 PHE B CB  1 
ATOM   4177 C  CG  . PHE B  1 202 ? 5.22800   17.80100  31.75600 1.000 17.48000  ? 196 PHE B CG  1 
ATOM   4178 C  CD1 . PHE B  1 202 ? 4.58100   16.56200  31.71200 1.000 16.67000  ? 196 PHE B CD1 1 
ATOM   4179 C  CD2 . PHE B  1 202 ? 5.27000   18.57100  30.59600 1.000 17.64000  ? 196 PHE B CD2 1 
ATOM   4180 C  CE1 . PHE B  1 202 ? 3.98600   16.08600  30.53000 1.000 15.09000  ? 196 PHE B CE1 1 
ATOM   4181 C  CE2 . PHE B  1 202 ? 4.67600   18.10900  29.40000 1.000 18.08000  ? 196 PHE B CE2 1 
ATOM   4182 C  CZ  . PHE B  1 202 ? 4.01500   16.87100  29.36800 1.000 15.72000  ? 196 PHE B CZ  1 
ATOM   4183 N  N   . PRO B  1 203 ? 6.54700   16.12400  35.15800 1.000 16.64000  ? 197 PRO B N   1 
ATOM   4184 C  CA  . PRO B  1 203 ? 6.45500   14.79400  35.76400 1.000 15.67000  ? 197 PRO B CA  1 
ATOM   4185 C  C   . PRO B  1 203 ? 5.69000   13.82100  34.86800 1.000 14.76000  ? 197 PRO B C   1 
ATOM   4186 O  O   . PRO B  1 203 ? 4.69300   14.18000  34.22600 1.000 15.22000  ? 197 PRO B O   1 
ATOM   4187 C  CB  . PRO B  1 203 ? 5.72500   15.06800  37.08000 1.000 19.86000  ? 197 PRO B CB  1 
ATOM   4188 C  CG  . PRO B  1 203 ? 6.15200   16.44200  37.45000 1.000 18.53000  ? 197 PRO B CG  1 
ATOM   4189 C  CD  . PRO B  1 203 ? 6.24500   17.19000  36.14400 1.000 19.41000  ? 197 PRO B CD  1 
ATOM   4190 N  N   . LEU B  1 204 ? 6.19000   12.58000  34.82600 1.000 18.97000  ? 198 LEU B N   1 
ATOM   4191 C  CA  . LEU B  1 204 ? 5.67700   11.58300  33.89400 1.000 15.79000  ? 198 LEU B CA  1 
ATOM   4192 C  C   . LEU B  1 204 ? 4.17600   11.42200  34.05100 1.000 15.67000  ? 198 LEU B C   1 
ATOM   4193 O  O   . LEU B  1 204 ? 3.45600   11.29900  33.05500 1.000 16.50000  ? 198 LEU B O   1 
ATOM   4194 C  CB  . LEU B  1 204 ? 6.38500   10.22900  34.09500 1.000 14.87000  ? 198 LEU B CB  1 
ATOM   4195 C  CG  . LEU B  1 204 ? 6.03000   9.07500   33.14900 1.000 14.66000  ? 198 LEU B CG  1 
ATOM   4196 C  CD1 . LEU B  1 204 ? 6.28400   9.47200   31.68300 1.000 16.33000  ? 198 LEU B CD1 1 
ATOM   4197 C  CD2 . LEU B  1 204 ? 6.77200   7.79900   33.54600 1.000 18.65000  ? 198 LEU B CD2 1 
ATOM   4198 N  N   . ASP B  1 205 ? 3.67600   11.43600  35.29100 1.000 16.51000  ? 199 ASP B N   1 
ATOM   4199 C  CA  . ASP B  1 205 ? 2.23200   11.24700  35.47300 1.000 16.08000  ? 199 ASP B CA  1 
ATOM   4200 C  C   . ASP B  1 205 ? 1.43200   12.33700  34.76400 1.000 19.51000  ? 199 ASP B C   1 
ATOM   4201 O  O   . ASP B  1 205 ? 0.31200   12.08000  34.29900 1.000 17.41000  ? 199 ASP B O   1 
ATOM   4202 C  CB  . ASP B  1 205 ? 1.84100   11.20500  36.95200 1.000 17.51000  ? 199 ASP B CB  1 
ATOM   4203 C  CG  . ASP B  1 205 ? 2.07800   12.55300  37.67100 1.000 23.82000  ? 199 ASP B CG  1 
ATOM   4204 O  OD1 . ASP B  1 205 ? 3.23200   12.97500  37.74100 1.000 18.05000  ? 199 ASP B OD1 1 
ATOM   4205 O  OD2 . ASP B  1 205 ? 1.11300   13.17600  38.18100 1.000 22.53000  ? 199 ASP B OD2 1 
ATOM   4206 N  N   . ARG B  1 206 ? 1.98700   13.54400  34.64600 1.000 14.54000  ? 200 ARG B N   1 
ATOM   4207 C  CA  . ARG B  1 206 ? 1.22400   14.60300  34.00000 1.000 16.33000  ? 200 ARG B CA  1 
ATOM   4208 C  C   . ARG B  1 206 ? 1.10000   14.37100  32.50600 1.000 16.91000  ? 200 ARG B C   1 
ATOM   4209 O  O   . ARG B  1 206 ? 0.12800   14.83500  31.91100 1.000 18.50000  ? 200 ARG B O   1 
ATOM   4210 C  CB  . ARG B  1 206 ? 1.83300   15.98600  34.29500 1.000 18.76000  ? 200 ARG B CB  1 
ATOM   4211 C  CG  . ARG B  1 206 ? 2.01100   16.26800  35.77800 1.000 16.97000  ? 200 ARG B CG  1 
ATOM   4212 C  CD  . ARG B  1 206 ? 0.67300   16.28200  36.52800 1.000 19.11000  ? 200 ARG B CD  1 
ATOM   4213 N  NE  . ARG B  1 206 ? 0.83400   16.34800  37.97700 1.000 21.77000  ? 200 ARG B NE  1 
ATOM   4214 C  CZ  . ARG B  1 206 ? 0.36500   17.32400  38.75600 1.000 26.05000  ? 200 ARG B CZ  1 
ATOM   4215 N  NH1 . ARG B  1 206 ? -0.27000  18.38100  38.25700 1.000 23.32000  ? 200 ARG B NH1 1 
ATOM   4216 N  NH2 . ARG B  1 206 ? 0.51700   17.22700  40.07000 1.000 28.25000  ? 200 ARG B NH2 1 
ATOM   4217 N  N   . LEU B  1 207 ? 2.01600   13.59800  31.90000 1.000 15.54000  ? 201 LEU B N   1 
ATOM   4218 C  CA  . LEU B  1 207 ? 1.80300   13.16300  30.52500 1.000 16.45000  ? 201 LEU B CA  1 
ATOM   4219 C  C   . LEU B  1 207 ? 0.59300   12.23200  30.42700 1.000 13.85000  ? 201 LEU B C   1 
ATOM   4220 O  O   . LEU B  1 207 ? -0.20200  12.33000  29.48800 1.000 16.11000  ? 201 LEU B O   1 
ATOM   4221 C  CB  . LEU B  1 207 ? 3.05500   12.46200  29.99600 1.000 16.94000  ? 201 LEU B CB  1 
ATOM   4222 C  CG  . LEU B  1 207 ? 3.04900   12.07000  28.52000 1.000 16.85000  ? 201 LEU B CG  1 
ATOM   4223 C  CD1 . LEU B  1 207 ? 2.88200   13.29800  27.63300 1.000 16.42000  ? 201 LEU B CD1 1 
ATOM   4224 C  CD2 . LEU B  1 207 ? 4.32300   11.34600  28.15900 1.000 13.81000  ? 201 LEU B CD2 1 
ATOM   4225 N  N   . GLY B  1 208 ? 0.45100   11.30700  31.36900 1.000 15.65000  ? 202 GLY B N   1 
ATOM   4226 C  CA  . GLY B  1 208 ? -0.73800  10.47100  31.36400 1.000 16.28000  ? 202 GLY B CA  1 
ATOM   4227 C  C   . GLY B  1 208 ? -1.99000  11.30200  31.58100 1.000 17.59000  ? 202 GLY B C   1 
ATOM   4228 O  O   . GLY B  1 208 ? -3.03000  11.04700  30.96700 1.000 15.68000  ? 202 GLY B O   1 
ATOM   4229 N  N   . ARG B  1 209 ? -1.89200  12.31800  32.44000 1.000 15.63000  ? 203 ARG B N   1 
ATOM   4230 C  CA  . ARG B  1 209 ? -3.01800  13.21500  32.69100 1.000 16.74000  ? 203 ARG B CA  1 
ATOM   4231 C  C   . ARG B  1 209 ? -3.48400  13.91200  31.41200 1.000 18.48000  ? 203 ARG B C   1 
ATOM   4232 O  O   . ARG B  1 209 ? -4.69000  14.04000  31.17300 1.000 17.24000  ? 203 ARG B O   1 
ATOM   4233 C  CB  . ARG B  1 209 ? -2.63400  14.24400  33.75700 1.000 15.29000  ? 203 ARG B CB  1 
ATOM   4234 C  CG  . ARG B  1 209 ? -3.83500  15.09400  34.19300 1.000 22.59000  ? 203 ARG B CG  1 
ATOM   4235 C  CD  . ARG B  1 209 ? -3.44600  16.23700  35.12700 1.000 19.90000  ? 203 ARG B CD  1 
ATOM   4236 N  NE  . ARG B  1 209 ? -2.89800  15.73900  36.39000 1.000 21.02000  ? 203 ARG B NE  1 
ATOM   4237 C  CZ  . ARG B  1 209 ? -3.12300  16.30600  37.56800 1.000 24.56000  ? 203 ARG B CZ  1 
ATOM   4238 N  NH1 . ARG B  1 209 ? -3.92200  17.35400  37.68800 1.000 23.61000  ? 203 ARG B NH1 1 
ATOM   4239 N  NH2 . ARG B  1 209 ? -2.55400  15.79600  38.65800 1.000 23.37000  ? 203 ARG B NH2 1 
ATOM   4240 N  N   . ILE B  1 210 ? -2.55100  14.33100  30.55400 1.000 16.52000  ? 204 ILE B N   1 
ATOM   4241 C  CA  . ILE B  1 210 ? -2.94600  14.97400  29.30300 1.000 16.98000  ? 204 ILE B CA  1 
ATOM   4242 C  C   . ILE B  1 210 ? -3.74800  14.00000  28.45700 1.000 16.80000  ? 204 ILE B C   1 
ATOM   4243 O  O   . ILE B  1 210 ? -4.77700  14.35100  27.86200 1.000 15.69000  ? 204 ILE B O   1 
ATOM   4244 C  CB  . ILE B  1 210 ? -1.71300  15.47700  28.53400 1.000 18.14000  ? 204 ILE B CB  1 
ATOM   4245 C  CG1 . ILE B  1 210 ? -1.03000  16.67300  29.22900 1.000 16.52000  ? 204 ILE B CG1 1 
ATOM   4246 C  CG2 . ILE B  1 210 ? -2.12700  15.90100  27.15000 1.000 20.42000  ? 204 ILE B CG2 1 
ATOM   4247 C  CD1 . ILE B  1 210 ? 0.40300   16.93400  28.65700 1.000 12.55000  ? 204 ILE B CD1 1 
ATOM   4248 N  N   . TYR B  1 211 ? -3.31600  12.74400  28.41500 1.000 15.26000  ? 205 TYR B N   1 
ATOM   4249 C  CA  . TYR B  1 211 ? -4.01400  11.82500  27.54000 1.000 16.71000  ? 205 TYR B CA  1 
ATOM   4250 C  C   . TYR B  1 211 ? -5.31800  11.34300  28.17400 1.000 15.50000  ? 205 TYR B C   1 
ATOM   4251 O  O   . TYR B  1 211 ? -6.29100  11.12300  27.46100 1.000 19.05000  ? 205 TYR B O   1 
ATOM   4252 C  CB  . TYR B  1 211 ? -3.07000  10.68500  27.17300 1.000 15.87000  ? 205 TYR B CB  1 
ATOM   4253 C  CG  . TYR B  1 211 ? -2.09700  11.14100  26.09900 1.000 16.56000  ? 205 TYR B CG  1 
ATOM   4254 C  CD1 . TYR B  1 211 ? -1.09800  12.06300  26.37500 1.000 14.89000  ? 205 TYR B CD1 1 
ATOM   4255 C  CD2 . TYR B  1 211 ? -2.21600  10.65900  24.80400 1.000 16.22000  ? 205 TYR B CD2 1 
ATOM   4256 C  CE1 . TYR B  1 211 ? -0.20000  12.49000  25.35900 1.000 13.82000  ? 205 TYR B CE1 1 
ATOM   4257 C  CE2 . TYR B  1 211 ? -1.37300  11.08000  23.80500 1.000 16.31000  ? 205 TYR B CE2 1 
ATOM   4258 C  CZ  . TYR B  1 211 ? -0.37600  11.98900  24.08200 1.000 15.93000  ? 205 TYR B CZ  1 
ATOM   4259 O  OH  . TYR B  1 211 ? 0.43300   12.32400  23.02200 1.000 15.50000  ? 205 TYR B OH  1 
ATOM   4260 N  N   . ALA B  1 212 ? -5.35600  11.23000  29.50200 1.000 15.56000  ? 206 ALA B N   1 
ATOM   4261 C  CA  . ALA B  1 212 ? -6.62100  11.00000  30.18900 1.000 16.67000  ? 206 ALA B CA  1 
ATOM   4262 C  C   . ALA B  1 212 ? -7.64900  12.05700  29.80200 1.000 19.07000  ? 206 ALA B C   1 
ATOM   4263 O  O   . ALA B  1 212 ? -8.82300  11.72800  29.55800 1.000 19.09000  ? 206 ALA B O   1 
ATOM   4264 C  CB  . ALA B  1 212 ? -6.40800  10.99100  31.69900 1.000 17.35000  ? 206 ALA B CB  1 
ATOM   4265 N  N   . LYS B  1 213 ? -7.22400  13.32400  29.73400 1.000 16.46000  ? 207 LYS B N   1 
ATOM   4266 C  CA  . LYS B  1 213 ? -8.12100  14.41700  29.38600 1.000 17.61000  ? 207 LYS B CA  1 
ATOM   4267 C  C   . LYS B  1 213 ? -8.56700  14.33300  27.93300 1.000 19.59000  ? 207 LYS B C   1 
ATOM   4268 O  O   . LYS B  1 213 ? -9.73000  14.63400  27.62300 1.000 19.74000  ? 207 LYS B O   1 
ATOM   4269 C  CB  . LYS B  1 213 ? -7.44300  15.75900  29.66700 1.000 15.83000  ? 207 LYS B CB  1 
ATOM   4270 C  CG  . LYS B  1 213 ? -7.31100  16.09900  31.16100 1.000 17.70000  ? 207 LYS B CG  1 
ATOM   4271 C  CD  . LYS B  1 213 ? -6.65500  17.45500  31.37400 1.000 17.49000  ? 207 LYS B CD  1 
ATOM   4272 C  CE  . LYS B  1 213 ? -6.58300  17.86700  32.85300 1.000 22.43000  ? 207 LYS B CE  1 
ATOM   4273 N  NZ  . LYS B  1 213 ? -5.81800  19.18000  33.02300 1.000 22.37000  ? 207 LYS B NZ  1 
ATOM   4274 N  N   . LEU B  1 214 ? -7.66400  13.94300  27.02700 1.000 15.01000  ? 208 LEU B N   1 
ATOM   4275 C  CA  . LEU B  1 214 ? -8.05700  13.73400  25.63300 1.000 17.66000  ? 208 LEU B CA  1 
ATOM   4276 C  C   . LEU B  1 214 ? -9.15900  12.69600  25.55400 1.000 21.96000  ? 208 LEU B C   1 
ATOM   4277 O  O   . LEU B  1 214 ? -10.18700 12.90100  24.90800 1.000 21.23000  ? 208 LEU B O   1 
ATOM   4278 C  CB  . LEU B  1 214 ? -6.86400  13.26500  24.79700 1.000 17.40000  ? 208 LEU B CB  1 
ATOM   4279 C  CG  . LEU B  1 214 ? -5.87800  14.24200  24.19700 1.000 20.51000  ? 208 LEU B CG  1 
ATOM   4280 C  CD1 . LEU B  1 214 ? -4.72000  13.48200  23.53800 1.000 19.72000  ? 208 LEU B CD1 1 
ATOM   4281 C  CD2 . LEU B  1 214 ? -6.59500  15.16400  23.16100 1.000 18.47000  ? 208 LEU B CD2 1 
ATOM   4282 N  N   . ALA B  1 215 ? -8.95600  11.56400  26.21500 1.000 16.39000  ? 209 ALA B N   1 
ATOM   4283 C  CA  . ALA B  1 215 ? -9.94600  10.49600  26.15200 1.000 18.78000  ? 209 ALA B CA  1 
ATOM   4284 C  C   . ALA B  1 215 ? -11.23300 10.90500  26.85700 1.000 21.24000  ? 209 ALA B C   1 
ATOM   4285 O  O   . ALA B  1 215 ? -12.34300 10.55800  26.39900 1.000 18.69000  ? 209 ALA B O   1 
ATOM   4286 C  CB  . ALA B  1 215 ? -9.35400  9.21600   26.76200 1.000 17.95000  ? 209 ALA B CB  1 
ATOM   4287 N  N   . SER B  1 216 ? -11.10100 11.68200  27.94300 1.000 19.09000  ? 210 SER B N   1 
ATOM   4288 C  CA  . SER B  1 216 ? -12.28700 12.11200  28.69000 1.000 21.57000  ? 210 SER B CA  1 
ATOM   4289 C  C   . SER B  1 216 ? -13.13200 13.04100  27.84500 1.000 18.88000  ? 210 SER B C   1 
ATOM   4290 O  O   . SER B  1 216 ? -14.36700 12.95600  27.84900 1.000 22.19000  ? 210 SER B O   1 
ATOM   4291 C  CB  . SER B  1 216 ? -11.86500 12.81400  29.97300 1.000 20.03000  ? 210 SER B CB  1 
ATOM   4292 O  OG  . SER B  1 216 ? -12.98200 13.11500  30.76400 1.000 23.20000  ? 210 SER B OG  1 
ATOM   4293 N  N   . ALA B  1 217 ? -12.47600 13.91500  27.08900 1.000 18.64000  ? 211 ALA B N   1 
ATOM   4294 C  CA  . ALA B  1 217 ? -13.18700 14.83600  26.20200 1.000 19.20000  ? 211 ALA B CA  1 
ATOM   4295 C  C   . ALA B  1 217 ? -13.90800 14.08600  25.08800 1.000 19.61000  ? 211 ALA B C   1 
ATOM   4296 O  O   . ALA B  1 217 ? -15.01700 14.45700  24.69900 1.000 24.40000  ? 211 ALA B O   1 
ATOM   4297 C  CB  . ALA B  1 217 ? -12.19900 15.83100  25.61400 1.000 21.65000  ? 211 ALA B CB  1 
ATOM   4298 N  N   . ALA B  1 218 ? -13.28100 13.04600  24.54100 1.000 22.10000  ? 212 ALA B N   1 
ATOM   4299 C  CA  . ALA B  1 218 ? -13.95900 12.25400  23.51900 1.000 21.34000  ? 212 ALA B CA  1 
ATOM   4300 C  C   . ALA B  1 218 ? -15.19000 11.58100  24.08700 1.000 23.61000  ? 212 ALA B C   1 
ATOM   4301 O  O   . ALA B  1 218 ? -16.22200 11.48100  23.40900 1.000 23.16000  ? 212 ALA B O   1 
ATOM   4302 C  CB  . ALA B  1 218 ? -13.00900 11.20800  22.93600 1.000 21.65000  ? 212 ALA B CB  1 
ATOM   4303 N  N   . ASP B  1 219 ? -15.09200 11.09300  25.32400 1.000 21.35000  ? 213 ASP B N   1 
ATOM   4304 C  CA  . ASP B  1 219 ? -16.25100 10.51800  25.99900 1.000 21.54000  ? 213 ASP B CA  1 
ATOM   4305 C  C   . ASP B  1 219 ? -17.37800 11.54100  26.13300 1.000 24.30000  ? 213 ASP B C   1 
ATOM   4306 O  O   . ASP B  1 219 ? -18.54600 11.24400  25.84200 1.000 26.84000  ? 213 ASP B O   1 
ATOM   4307 C  CB  . ASP B  1 219 ? -15.83100 9.99000   27.37100 1.000 21.95000  ? 213 ASP B CB  1 
ATOM   4308 C  CG  . ASP B  1 219 ? -15.20100 8.58400   27.30400 1.000 25.32000  ? 213 ASP B CG  1 
ATOM   4309 O  OD1 . ASP B  1 219 ? -15.31700 7.91700   26.25700 1.000 24.76000  ? 213 ASP B OD1 1 
ATOM   4310 O  OD2 . ASP B  1 219 ? -14.59700 8.14100   28.30700 1.000 23.47000  ? 213 ASP B OD2 1 
ATOM   4311 N  N   . GLY B  1 220 ? -17.05300 12.75300  26.57600 1.000 24.48000  ? 214 GLY B N   1 
ATOM   4312 C  CA  . GLY B  1 220 ? -18.10100 13.75300  26.73500 1.000 22.32000  ? 214 GLY B CA  1 
ATOM   4313 C  C   . GLY B  1 220 ? -18.73400 14.11700  25.40400 1.000 28.15000  ? 214 GLY B C   1 
ATOM   4314 O  O   . GLY B  1 220 ? -19.95900 14.29000  25.30600 1.000 28.06000  ? 214 GLY B O   1 
ATOM   4315 N  N   . SER B  1 221 ? -17.90700 14.21500  24.35800 1.000 24.71000  ? 215 SER B N   1 
ATOM   4316 C  CA  . SER B  1 221 ? -18.39700 14.56800  23.03200 1.000 29.86000  ? 215 SER B CA  1 
ATOM   4317 C  C   . SER B  1 221 ? -19.36600 13.51800  22.51900 1.000 28.40000  ? 215 SER B C   1 
ATOM   4318 O  O   . SER B  1 221 ? -20.49400 13.83400  22.09400 1.000 25.58000  ? 215 SER B O   1 
ATOM   4319 C  CB  . SER B  1 221 ? -17.21300 14.71200  22.06500 1.000 24.61000  ? 215 SER B CB  1 
ATOM   4320 O  OG  . SER B  1 221 ? -17.68300 15.04700  20.75700 1.000 27.40000  ? 215 SER B OG  1 
ATOM   4321 N  N   . ASP B  1 222 ? -18.93000 12.25600  22.55400 1.000 29.44000  ? 216 ASP B N   1 
ATOM   4322 C  CA  . ASP B  1 222 ? -19.72800 11.14400  22.06400 1.000 30.38000  ? 216 ASP B CA  1 
ATOM   4323 C  C   . ASP B  1 222 ? -21.05100 11.03100  22.80700 1.000 28.50000  ? 216 ASP B C   1 
ATOM   4324 O  O   . ASP B  1 222 ? -22.06600 10.62500  22.22200 1.000 29.65000  ? 216 ASP B O   1 
ATOM   4325 C  CB  . ASP B  1 222 ? -18.90100 9.86200   22.20100 1.000 30.80000  ? 216 ASP B CB  1 
ATOM   4326 C  CG  . ASP B  1 222 ? -19.41700 8.74100   21.34800 1.000 37.42000  ? 216 ASP B CG  1 
ATOM   4327 O  OD1 . ASP B  1 222 ? -20.10600 9.01100   20.34000 1.000 49.47000  ? 216 ASP B OD1 1 
ATOM   4328 O  OD2 . ASP B  1 222 ? -19.16100 7.57800   21.70500 1.000 35.46000  ? 216 ASP B OD2 1 
ATOM   4329 N  N   . ALA B  1 223 ? -21.06100 11.37900  24.09200 1.000 26.94000  ? 217 ALA B N   1 
ATOM   4330 C  CA  . ALA B  1 223 ? -22.27400 11.30800  24.89800 1.000 30.81000  ? 217 ALA B CA  1 
ATOM   4331 C  C   . ALA B  1 223 ? -23.18500 12.52200  24.71200 1.000 30.86000  ? 217 ALA B C   1 
ATOM   4332 O  O   . ALA B  1 223 ? -24.32500 12.51600  25.20500 1.000 30.11000  ? 217 ALA B O   1 
ATOM   4333 C  CB  . ALA B  1 223 ? -21.90600 11.15500  26.37500 1.000 27.83000  ? 217 ALA B CB  1 
ATOM   4334 N  N   . GLY B  1 224 ? -22.72400 13.55200  24.01000 1.000 32.33000  ? 218 GLY B N   1 
ATOM   4335 C  CA  . GLY B  1 224 ? -23.57000 14.69500  23.73500 1.000 31.10000  ? 218 GLY B CA  1 
ATOM   4336 C  C   . GLY B  1 224 ? -23.60100 15.74000  24.82300 1.000 32.14000  ? 218 GLY B C   1 
ATOM   4337 O  O   . GLY B  1 224 ? -24.51000 16.57200  24.83500 1.000 35.32000  ? 218 GLY B O   1 
ATOM   4338 N  N   . GLU B  1 225 ? -22.62900 15.73600  25.72500 1.000 31.94000  ? 219 GLU B N   1 
ATOM   4339 C  CA  . GLU B  1 225 ? -22.58300 16.72100  26.79600 1.000 33.06000  ? 219 GLU B CA  1 
ATOM   4340 C  C   . GLU B  1 225 ? -22.16700 18.08600  26.26500 1.000 35.16000  ? 219 GLU B C   1 
ATOM   4341 O  O   . GLU B  1 225 ? -21.30100 18.18900  25.38900 1.000 31.44000  ? 219 GLU B O   1 
ATOM   4342 C  CB  . GLU B  1 225 ? -21.57700 16.29200  27.86000 1.000 34.26000  ? 219 GLU B CB  1 
ATOM   4343 C  CG  . GLU B  1 225 ? -21.73100 14.89000  28.39800 1.000 35.31000  ? 219 GLU B CG  1 
ATOM   4344 C  CD  . GLU B  1 225 ? -20.53200 14.49300  29.25900 1.000 35.57000  ? 219 GLU B CD  1 
ATOM   4345 O  OE1 . GLU B  1 225 ? -19.58800 15.31300  29.41000 1.000 37.89000  ? 219 GLU B OE1 1 
ATOM   4346 O  OE2 . GLU B  1 225 ? -20.54200 13.37000  29.78400 1.000 35.44000  ? 219 GLU B OE2 1 
ATOM   4347 N  N   . GLY B  1 226 ? -22.75100 19.14100  26.82800 1.000 33.57000  ? 220 GLY B N   1 
ATOM   4348 C  CA  . GLY B  1 226 ? -22.25300 20.47600  26.54300 1.000 35.37000  ? 220 GLY B CA  1 
ATOM   4349 C  C   . GLY B  1 226 ? -20.80900 20.58400  26.99200 1.000 29.76000  ? 220 GLY B C   1 
ATOM   4350 O  O   . GLY B  1 226 ? -20.47600 20.16100  28.10100 1.000 31.54000  ? 220 GLY B O   1 
ATOM   4351 N  N   . GLN B  1 227 ? -19.92500 21.09400  26.13500 1.000 30.15000  ? 221 GLN B N   1 
ATOM   4352 C  CA  . GLN B  1 227 ? -18.50000 21.11500  26.42900 1.000 23.60000  ? 221 GLN B CA  1 
ATOM   4353 C  C   . GLN B  1 227 ? -17.95700 22.52500  26.26800 1.000 29.12000  ? 221 GLN B C   1 
ATOM   4354 O  O   . GLN B  1 227 ? -18.44800 23.31400  25.45100 1.000 26.95000  ? 221 GLN B O   1 
ATOM   4355 C  CB  . GLN B  1 227 ? -17.71600 20.15300  25.50700 1.000 27.90000  ? 221 GLN B CB  1 
ATOM   4356 C  CG  . GLN B  1 227 ? -17.85400 18.66400  25.88200 1.000 27.56000  ? 221 GLN B CG  1 
ATOM   4357 C  CD  . GLN B  1 227 ? -17.00300 17.77400  24.99500 1.000 27.18000  ? 221 GLN B CD  1 
ATOM   4358 O  OE1 . GLN B  1 227 ? -17.00000 17.95600  23.78500 1.000 26.59000  ? 221 GLN B OE1 1 
ATOM   4359 N  NE2 . GLN B  1 227 ? -16.27600 16.81200  25.59100 1.000 21.14000  ? 221 GLN B NE2 1 
ATOM   4360 N  N   . SER B  1 228 ? -16.96700 22.84500  27.09400 1.000 24.47000  ? 222 SER B N   1 
ATOM   4361 C  CA  . SER B  1 228 ? -16.18000 24.04500  26.88000 1.000 25.18000  ? 222 SER B CA  1 
ATOM   4362 C  C   . SER B  1 228 ? -15.51500 23.99600  25.50900 1.000 24.21000  ? 222 SER B C   1 
ATOM   4363 O  O   . SER B  1 228 ? -15.35700 22.92800  24.90400 1.000 28.08000  ? 222 SER B O   1 
ATOM   4364 C  CB  . SER B  1 228 ? -15.11000 24.17100  27.95300 1.000 26.58000  ? 222 SER B CB  1 
ATOM   4365 O  OG  . SER B  1 228 ? -14.08200 23.21800  27.72700 1.000 30.70000  ? 222 SER B OG  1 
ATOM   4366 N  N   . THR B  1 229 ? -15.10300 25.17000  25.02000 1.000 28.23000  ? 223 THR B N   1 
ATOM   4367 C  CA  . THR B  1 229 ? -14.36200 25.18000  23.76400 1.000 26.66000  ? 223 THR B CA  1 
ATOM   4368 C  C   . THR B  1 229 ? -13.10800 24.32100  23.86200 1.000 25.85000  ? 223 THR B C   1 
ATOM   4369 O  O   . THR B  1 229 ? -12.72300 23.69100  22.87700 1.000 22.46000  ? 223 THR B O   1 
ATOM   4370 C  CB  . THR B  1 229 ? -14.01300 26.61900  23.33000 1.000 28.88000  ? 223 THR B CB  1 
ATOM   4371 O  OG1 . THR B  1 229 ? -13.20100 27.26300  24.31700 1.000 31.87000  ? 223 THR B OG1 1 
ATOM   4372 C  CG2 . THR B  1 229 ? -15.27800 27.45000  23.07800 1.000 27.21000  ? 223 THR B CG2 1 
ATOM   4373 N  N   . ARG B  1 230 ? -12.46300 24.27300  25.02600 1.000 21.32000  ? 224 ARG B N   1 
ATOM   4374 C  CA  . ARG B  1 230 ? -11.25600 23.46700  25.15000 1.000 20.96000  ? 224 ARG B CA  1 
ATOM   4375 C  C   . ARG B  1 230 ? -11.56000 21.96200  25.11900 1.000 20.52000  ? 224 ARG B C   1 
ATOM   4376 O  O   . ARG B  1 230 ? -10.87800 21.20500  24.44200 1.000 18.35000  ? 224 ARG B O   1 
ATOM   4377 C  CB  . ARG B  1 230 ? -10.48300 23.78800  26.42000 1.000 23.76000  ? 224 ARG B CB  1 
ATOM   4378 C  CG  . ARG B  1 230 ? -9.32600  22.79400  26.61400 1.000 20.28000  ? 224 ARG B CG  1 
ATOM   4379 C  CD  . ARG B  1 230 ? -8.25500  23.34000  27.52300 1.000 22.61000  ? 224 ARG B CD  1 
ATOM   4380 N  NE  . ARG B  1 230 ? -7.57300  24.47900  26.92500 1.000 25.74000  ? 224 ARG B NE  1 
ATOM   4381 C  CZ  . ARG B  1 230 ? -6.61900  25.16800  27.53300 1.000 27.63000  ? 224 ARG B CZ  1 
ATOM   4382 N  NH1 . ARG B  1 230 ? -6.25500  24.89600  28.76800 1.000 23.91000  ? 224 ARG B NH1 1 
ATOM   4383 N  NH2 . ARG B  1 230 ? -6.02200  26.16200  26.88700 1.000 27.47000  ? 224 ARG B NH2 1 
HETATM 4384 N  N   . CSO B  1 231 ? -12.58200 21.53500  25.85600 1.000 22.96000  ? 225 CSO B N   1 
HETATM 4385 C  CA  . CSO B  1 231 ? -12.95000 20.12800  25.83500 1.000 21.45000  ? 225 CSO B CA  1 
HETATM 4386 C  CB  . CSO B  1 231 ? -14.03700 19.85500  26.88000 1.000 23.36000  ? 225 CSO B CB  1 
HETATM 4387 S  SG  . CSO B  1 231 ? -13.17600 19.76300  28.48800 1.000 33.58000  ? 225 CSO B SG  1 
HETATM 4388 C  C   . CSO B  1 231 ? -13.37600 19.71100  24.43200 1.000 20.97000  ? 225 CSO B C   1 
HETATM 4389 O  O   . CSO B  1 231 ? -13.03600 18.62600  23.98000 1.000 21.98000  ? 225 CSO B O   1 
HETATM 4390 O  OD  . CSO B  1 231 ? -14.29000 19.83000  29.91500 1.000 29.00000  ? 225 CSO B OD  1 
ATOM   4391 N  N   . ALA B  1 232 ? -14.07200 20.59200  23.72100 1.000 20.97000  ? 226 ALA B N   1 
ATOM   4392 C  CA  . ALA B  1 232 ? -14.52300 20.26300  22.36200 1.000 24.60000  ? 226 ALA B CA  1 
ATOM   4393 C  C   . ALA B  1 232 ? -13.30200 20.06500  21.46300 1.000 21.21000  ? 226 ALA B C   1 
ATOM   4394 O  O   . ALA B  1 232 ? -13.25800 19.18600  20.60000 1.000 20.60000  ? 226 ALA B O   1 
ATOM   4395 C  CB  . ALA B  1 232 ? -15.42000 21.37100  21.81000 1.000 23.85000  ? 226 ALA B CB  1 
ATOM   4396 N  N   . ALA B  1 233 ? -12.29500 20.90500  21.66400 1.000 22.27000  ? 227 ALA B N   1 
ATOM   4397 C  CA  . ALA B  1 233 ? -11.09200 20.78700  20.85200 1.000 18.79000  ? 227 ALA B CA  1 
ATOM   4398 C  C   . ALA B  1 233 ? -10.29800 19.52900  21.19900 1.000 22.25000  ? 227 ALA B C   1 
ATOM   4399 O  O   . ALA B  1 233 ? -9.71600  18.89800  20.31000 1.000 21.58000  ? 227 ALA B O   1 
ATOM   4400 C  CB  . ALA B  1 233 ? -10.21900 22.02400  21.02800 1.000 21.52000  ? 227 ALA B CB  1 
ATOM   4401 N  N   . LEU B  1 234 ? -10.22600 19.16900  22.48700 1.000 17.77000  ? 228 LEU B N   1 
ATOM   4402 C  CA  . LEU B  1 234 ? -9.53500  17.93200  22.86100 1.000 18.48000  ? 228 LEU B CA  1 
ATOM   4403 C  C   . LEU B  1 234 ? -10.24900 16.72800  22.27400 1.000 21.71000  ? 228 LEU B C   1 
ATOM   4404 O  O   . LEU B  1 234 ? -9.61100  15.75300  21.83800 1.000 16.69000  ? 228 LEU B O   1 
ATOM   4405 C  CB  . LEU B  1 234 ? -9.45800  17.80300  24.38800 1.000 17.82000  ? 228 LEU B CB  1 
ATOM   4406 C  CG  . LEU B  1 234 ? -8.49400  18.74300  25.11200 1.000 20.86000  ? 228 LEU B CG  1 
ATOM   4407 C  CD1 . LEU B  1 234 ? -8.83500  18.70200  26.60100 1.000 24.55000  ? 228 LEU B CD1 1 
ATOM   4408 C  CD2 . LEU B  1 234 ? -7.04700  18.29000  24.83300 1.000 15.77000  ? 228 LEU B CD2 1 
ATOM   4409 N  N   . ALA B  1 235 ? -11.59000 16.78400  22.23100 1.000 18.57000  ? 229 ALA B N   1 
ATOM   4410 C  CA  . ALA B  1 235 ? -12.33700 15.67100  21.66900 1.000 18.92000  ? 229 ALA B CA  1 
ATOM   4411 C  C   . ALA B  1 235 ? -12.07000 15.54400  20.17500 1.000 18.97000  ? 229 ALA B C   1 
ATOM   4412 O  O   . ALA B  1 235 ? -11.97500 14.43100  19.64100 1.000 18.72000  ? 229 ALA B O   1 
ATOM   4413 C  CB  . ALA B  1 235 ? -13.84300 15.85100  21.94700 1.000 20.37000  ? 229 ALA B CB  1 
ATOM   4414 N  N   . HIS B  1 236 ? -11.92600 16.66900  19.49300 1.000 18.32000  ? 230 HIS B N   1 
ATOM   4415 C  CA  . HIS B  1 236 ? -11.61100 16.65500  18.07000 1.000 19.68000  ? 230 HIS B CA  1 
ATOM   4416 C  C   . HIS B  1 236 ? -10.22200 16.05600  17.82600 1.000 21.65000  ? 230 HIS B C   1 
ATOM   4417 O  O   . HIS B  1 236 ? -10.00400 15.32500  16.85100 1.000 21.04000  ? 230 HIS B O   1 
ATOM   4418 C  CB  . HIS B  1 236 ? -11.69400 18.09800  17.56400 1.000 21.70000  ? 230 HIS B CB  1 
ATOM   4419 C  CG  . HIS B  1 236 ? -11.74000 18.23700  16.08000 1.000 22.85000  ? 230 HIS B CG  1 
ATOM   4420 N  ND1 . HIS B  1 236 ? -11.81800 19.46400  15.45900 1.000 26.36000  ? 230 HIS B ND1 1 
ATOM   4421 C  CD2 . HIS B  1 236 ? -11.72000 17.31400  15.09000 1.000 27.10000  ? 230 HIS B CD2 1 
ATOM   4422 C  CE1 . HIS B  1 236 ? -11.86700 19.29200  14.14900 1.000 28.78000  ? 230 HIS B CE1 1 
ATOM   4423 N  NE2 . HIS B  1 236 ? -11.79700 17.99600  13.89900 1.000 26.02000  ? 230 HIS B NE2 1 
ATOM   4424 N  N   . ILE B  1 237 ? -9.26100  16.38700  18.68500 1.000 18.53000  ? 231 ILE B N   1 
ATOM   4425 C  CA  . ILE B  1 237 ? -7.91200  15.84700  18.53500 1.000 19.88000  ? 231 ILE B CA  1 
ATOM   4426 C  C   . ILE B  1 237 ? -7.92500  14.33800  18.71300 1.000 18.15000  ? 231 ILE B C   1 
ATOM   4427 O  O   . ILE B  1 237 ? -7.32800  13.59700  17.92300 1.000 18.39000  ? 231 ILE B O   1 
ATOM   4428 C  CB  . ILE B  1 237 ? -6.94900  16.52400  19.52500 1.000 20.55000  ? 231 ILE B CB  1 
ATOM   4429 C  CG1 . ILE B  1 237 ? -6.69100  17.96900  19.09000 1.000 20.08000  ? 231 ILE B CG1 1 
ATOM   4430 C  CG2 . ILE B  1 237 ? -5.59300  15.76400  19.55500 1.000 16.47000  ? 231 ILE B CG2 1 
ATOM   4431 C  CD1 . ILE B  1 237 ? -6.11100  18.86600  20.20000 1.000 21.60000  ? 231 ILE B CD1 1 
ATOM   4432 N  N   . PHE B  1 238 ? -8.62100  13.85800  19.74700 1.000 18.81000  ? 232 PHE B N   1 
ATOM   4433 C  CA  . PHE B  1 238 ? -8.74500  12.41300  19.92900 1.000 19.58000  ? 232 PHE B CA  1 
ATOM   4434 C  C   . PHE B  1 238 ? -9.34700  11.76300  18.69200 1.000 22.33000  ? 232 PHE B C   1 
ATOM   4435 O  O   . PHE B  1 238 ? -8.78800  10.81400  18.14000 1.000 17.98000  ? 232 PHE B O   1 
ATOM   4436 C  CB  . PHE B  1 238 ? -9.60100  12.11600  21.15800 1.000 19.38000  ? 232 PHE B CB  1 
ATOM   4437 C  CG  . PHE B  1 238 ? -9.67000  10.65400  21.50200 1.000 20.50000  ? 232 PHE B CG  1 
ATOM   4438 C  CD1 . PHE B  1 238 ? -10.45100 9.78700   20.76000 1.000 21.31000  ? 232 PHE B CD1 1 
ATOM   4439 C  CD2 . PHE B  1 238 ? -8.98100  10.15800  22.59300 1.000 19.10000  ? 232 PHE B CD2 1 
ATOM   4440 C  CE1 . PHE B  1 238 ? -10.52000 8.44100   21.06500 1.000 19.02000  ? 232 PHE B CE1 1 
ATOM   4441 C  CE2 . PHE B  1 238 ? -9.04300  8.79100   22.91100 1.000 17.16000  ? 232 PHE B CE2 1 
ATOM   4442 C  CZ  . PHE B  1 238 ? -9.83000  7.94200   22.15100 1.000 20.49000  ? 232 PHE B CZ  1 
ATOM   4443 N  N   . ARG B  1 239 ? -10.50100 12.27200  18.25800 1.000 18.52000  ? 233 ARG B N   1 
ATOM   4444 C  CA  A ARG B  1 239 ? -11.16800 11.78800  17.05300 0.500 21.53000  ? 233 ARG B CA  1 
ATOM   4445 C  CA  B ARG B  1 239 ? -11.16200 11.77000  17.05600 0.500 21.53000  ? 233 ARG B CA  1 
ATOM   4446 C  C   . ARG B  1 239 ? -10.22300 11.74100  15.85300 1.000 20.45000  ? 233 ARG B C   1 
ATOM   4447 O  O   . ARG B  1 239 ? -10.14600 10.73500  15.13500 1.000 21.72000  ? 233 ARG B O   1 
ATOM   4448 C  CB  A ARG B  1 239 ? -12.36100 12.71100  16.79400 0.500 22.51000  ? 233 ARG B CB  1 
ATOM   4449 C  CB  B ARG B  1 239 ? -12.38900 12.63600  16.76100 0.500 22.52000  ? 233 ARG B CB  1 
ATOM   4450 C  CG  A ARG B  1 239 ? -13.19600 12.47300  15.57300 0.500 28.97000  ? 233 ARG B CG  1 
ATOM   4451 C  CG  B ARG B  1 239 ? -12.91700 12.54800  15.34400 0.500 28.75000  ? 233 ARG B CG  1 
ATOM   4452 C  CD  A ARG B  1 239 ? -14.33700 13.50600  15.58500 0.500 26.95000  ? 233 ARG B CD  1 
ATOM   4453 C  CD  B ARG B  1 239 ? -13.66700 13.83900  14.95800 0.500 27.64000  ? 233 ARG B CD  1 
ATOM   4454 N  NE  A ARG B  1 239 ? -14.98400 13.51400  16.89400 0.500 27.72000  ? 233 ARG B NE  1 
ATOM   4455 N  NE  B ARG B  1 239 ? -14.44000 13.71200  13.73200 0.500 28.40000  ? 233 ARG B NE  1 
ATOM   4456 C  CZ  A ARG B  1 239 ? -15.19000 14.57700  17.66600 0.500 27.03000  ? 233 ARG B CZ  1 
ATOM   4457 C  CZ  B ARG B  1 239 ? -14.88400 14.73500  13.01300 0.500 33.67000  ? 233 ARG B CZ  1 
ATOM   4458 N  NH1 A ARG B  1 239 ? -14.90000 15.80800  17.26300 0.500 21.94000  ? 233 ARG B NH1 1 
ATOM   4459 N  NH1 B ARG B  1 239 ? -14.52800 15.98100  13.28800 0.500 29.27000  ? 233 ARG B NH1 1 
ATOM   4460 N  NH2 A ARG B  1 239 ? -15.72100 14.39800  18.87300 0.500 24.30000  ? 233 ARG B NH2 1 
ATOM   4461 N  NH2 B ARG B  1 239 ? -15.70300 14.50200  11.98600 0.500 37.08000  ? 233 ARG B NH2 1 
ATOM   4462 N  N   . ALA B  1 240 ? -9.51700  12.83800  15.60300 1.000 19.40000  ? 234 ALA B N   1 
ATOM   4463 C  CA  . ALA B  1 240 ? -8.62700  12.91200  14.45000 1.000 19.71000  ? 234 ALA B CA  1 
ATOM   4464 C  C   . ALA B  1 240 ? -7.53700  11.83600  14.50900 1.000 19.34000  ? 234 ALA B C   1 
ATOM   4465 O  O   . ALA B  1 240 ? -7.27100  11.14200  13.51600 1.000 20.25000  ? 234 ALA B O   1 
ATOM   4466 C  CB  . ALA B  1 240 ? -8.00000  14.30600  14.37000 1.000 19.13000  ? 234 ALA B CB  1 
ATOM   4467 N  N   . MET B  1 241 ? -6.88400  11.69900  15.65800 1.000 18.17000  ? 235 MET B N   1 
ATOM   4468 C  CA  . MET B  1 241 ? -5.82100  10.70300  15.77400 1.000 17.93000  ? 235 MET B CA  1 
ATOM   4469 C  C   . MET B  1 241 ? -6.36600  9.29100   15.55700 1.000 19.14000  ? 235 MET B C   1 
ATOM   4470 O  O   . MET B  1 241 ? -5.76200  8.47700   14.83400 1.000 19.64000  ? 235 MET B O   1 
ATOM   4471 C  CB  . MET B  1 241 ? -5.15700  10.82900  17.14000 1.000 16.68000  ? 235 MET B CB  1 
ATOM   4472 C  CG  . MET B  1 241 ? -4.43500  12.16300  17.36600 1.000 15.81000  ? 235 MET B CG  1 
ATOM   4473 S  SD  . MET B  1 241 ? -3.67900  12.19400  19.01800 1.000 18.32000  ? 235 MET B SD  1 
ATOM   4474 C  CE  . MET B  1 241 ? -2.30600  11.06700  18.85600 1.000 14.62000  ? 235 MET B CE  1 
ATOM   4475 N  N   . ALA B  1 242 ? -7.51400  8.98300   16.16700 1.000 19.29000  ? 236 ALA B N   1 
ATOM   4476 C  CA  . ALA B  1 242 ? -8.04300  7.63200   16.08500 1.000 20.42000  ? 236 ALA B CA  1 
ATOM   4477 C  C   . ALA B  1 242 ? -8.58200  7.33200   14.70400 1.000 21.93000  ? 236 ALA B C   1 
ATOM   4478 O  O   . ALA B  1 242 ? -8.53600  6.18500   14.25300 1.000 24.11000  ? 236 ALA B O   1 
ATOM   4479 C  CB  . ALA B  1 242 ? -9.11900  7.41600   17.14400 1.000 22.87000  ? 236 ALA B CB  1 
ATOM   4480 N  N   . ARG B  1 243 ? -9.10000  8.33200   14.01500 1.000 22.21000  ? 237 ARG B N   1 
ATOM   4481 C  CA  . ARG B  1 243 ? -9.62600  8.06200   12.69300 1.000 23.86000  ? 237 ARG B CA  1 
ATOM   4482 C  C   . ARG B  1 243 ? -8.54700  8.03400   11.62100 1.000 24.22000  ? 237 ARG B C   1 
ATOM   4483 O  O   . ARG B  1 243 ? -8.75300  7.42800   10.57000 1.000 25.79000  ? 237 ARG B O   1 
ATOM   4484 C  CB  . ARG B  1 243 ? -10.69600 9.09800   12.35800 1.000 24.69000  ? 237 ARG B CB  1 
ATOM   4485 C  CG  . ARG B  1 243 ? -12.07800 8.58700   12.70700 1.000 36.18000  ? 237 ARG B CG  1 
ATOM   4486 C  CD  . ARG B  1 243 ? -12.76600 9.52100   13.66600 1.000 37.10000  ? 237 ARG B CD  1 
ATOM   4487 N  NE  . ARG B  1 243 ? -14.02900 10.04700  13.16400 1.000 43.26000  ? 237 ARG B NE  1 
ATOM   4488 C  CZ  . ARG B  1 243 ? -14.15500 10.85900  12.11900 1.000 46.24000  ? 237 ARG B CZ  1 
ATOM   4489 N  NH1 . ARG B  1 243 ? -13.13000 11.12900  11.31500 1.000 39.32000  ? 237 ARG B NH1 1 
ATOM   4490 N  NH2 . ARG B  1 243 ? -15.34000 11.41200  11.86900 1.000 43.10000  ? 237 ARG B NH2 1 
ATOM   4491 N  N   . HIS B  1 244 ? -7.41700  8.68400   11.83900 1.000 19.85000  ? 238 HIS B N   1 
ATOM   4492 C  CA  . HIS B  1 244 ? -6.34600  8.73200   10.84500 1.000 20.77000  ? 238 HIS B CA  1 
ATOM   4493 C  C   . HIS B  1 244 ? -5.03100  8.33400   11.48100 1.000 20.21000  ? 238 HIS B C   1 
ATOM   4494 O  O   . HIS B  1 244 ? -4.06000  9.10000   11.46800 1.000 18.70000  ? 238 HIS B O   1 
ATOM   4495 C  CB  . HIS B  1 244 ? -6.26200  10.12300  10.23300 1.000 20.50000  ? 238 HIS B CB  1 
ATOM   4496 C  CG  . HIS B  1 244 ? -7.54500  10.54700  9.60300  1.000 22.33000  ? 238 HIS B CG  1 
ATOM   4497 N  ND1 . HIS B  1 244 ? -7.89000  10.18600  8.32400  1.000 25.15000  ? 238 HIS B ND1 1 
ATOM   4498 C  CD2 . HIS B  1 244 ? -8.60300  11.21900  10.10300 1.000 22.64000  ? 238 HIS B CD2 1 
ATOM   4499 C  CE1 . HIS B  1 244 ? -9.08100  10.67400  8.03800  1.000 25.11000  ? 238 HIS B CE1 1 
ATOM   4500 N  NE2 . HIS B  1 244 ? -9.53500  11.30400  9.10100  1.000 24.49000  ? 238 HIS B NE2 1 
ATOM   4501 N  N   . PRO B  1 245 ? -4.96200  7.13000   12.05100 1.000 18.43000  ? 239 PRO B N   1 
ATOM   4502 C  CA  . PRO B  1 245 ? -3.76200  6.75400   12.79200 1.000 16.61000  ? 239 PRO B CA  1 
ATOM   4503 C  C   . PRO B  1 245 ? -2.55900  6.66400   11.88700 1.000 18.15000  ? 239 PRO B C   1 
ATOM   4504 O  O   . PRO B  1 245 ? -1.43500  6.80100   12.36200 1.000 20.22000  ? 239 PRO B O   1 
ATOM   4505 C  CB  . PRO B  1 245 ? -4.13400  5.37900   13.39000 1.000 21.68000  ? 239 PRO B CB  1 
ATOM   4506 C  CG  . PRO B  1 245 ? -5.17800  4.83900   12.48000 1.000 19.05000  ? 239 PRO B CG  1 
ATOM   4507 C  CD  . PRO B  1 245 ? -5.97200  6.04800   12.05300 1.000 19.80000  ? 239 PRO B CD  1 
ATOM   4508 N  N   . GLU B  1 246 ? -2.76700  6.45200   10.58800 1.000 19.35000  ? 240 GLU B N   1 
ATOM   4509 C  CA  . GLU B  1 246 ? -1.63100  6.34800   9.67800  1.000 20.40000  ? 240 GLU B CA  1 
ATOM   4510 C  C   . GLU B  1 246 ? -1.00200  7.71100   9.42500  1.000 18.51000  ? 240 GLU B C   1 
ATOM   4511 O  O   . GLU B  1 246 ? 0.18100   7.77400   9.06100  1.000 18.81000  ? 240 GLU B O   1 
ATOM   4512 C  CB  . GLU B  1 246 ? -2.04700  5.67500   8.36500  1.000 24.12000  ? 240 GLU B CB  1 
ATOM   4513 C  CG  . GLU B  1 246 ? -2.96200  6.51400   7.45300  1.000 27.12000  ? 240 GLU B CG  1 
ATOM   4514 C  CD  . GLU B  1 246 ? -4.34600  6.84400   8.06600  1.000 29.37000  ? 240 GLU B CD  1 
ATOM   4515 O  OE1 . GLU B  1 246 ? -4.87700  6.04200   8.89100  1.000 31.27000  ? 240 GLU B OE1 1 
ATOM   4516 O  OE2 . GLU B  1 246 ? -4.90400  7.91200   7.69700  1.000 32.44000  ? 240 GLU B OE2 1 
ATOM   4517 N  N   . MET B  1 247 ? -1.75300  8.80600   9.64500  1.000 20.49000  ? 241 MET B N   1 
ATOM   4518 C  CA  . MET B  1 247 ? -1.11400  10.11700  9.60900  1.000 18.23000  ? 241 MET B CA  1 
ATOM   4519 C  C   . MET B  1 247 ? -0.24000  10.33300  10.82400 1.000 17.71000  ? 241 MET B C   1 
ATOM   4520 O  O   . MET B  1 247 ? 0.76100   11.05700  10.73800 1.000 20.61000  ? 241 MET B O   1 
ATOM   4521 C  CB  . MET B  1 247 ? -2.13500  11.25200  9.54700  1.000 18.93000  ? 241 MET B CB  1 
ATOM   4522 C  CG  . MET B  1 247 ? -2.93800  11.33500  8.23300  1.000 20.94000  ? 241 MET B CG  1 
ATOM   4523 S  SD  . MET B  1 247 ? -1.82200  11.72900  6.88600  1.000 22.12000  ? 241 MET B SD  1 
ATOM   4524 C  CE  . MET B  1 247 ? -1.46900  10.11800  6.16100  1.000 22.71000  ? 241 MET B CE  1 
ATOM   4525 N  N   . VAL B  1 248 ? -0.63100  9.76900   11.97000 1.000 16.36000  ? 242 VAL B N   1 
ATOM   4526 C  CA  . VAL B  1 248 ? 0.09600   10.00100  13.21300 1.000 15.36000  ? 242 VAL B CA  1 
ATOM   4527 C  C   . VAL B  1 248 ? 1.45100   9.30900   13.20300 1.000 18.62000  ? 242 VAL B C   1 
ATOM   4528 O  O   . VAL B  1 248 ? 2.37300   9.76800   13.88600 1.000 18.41000  ? 242 VAL B O   1 
ATOM   4529 C  CB  . VAL B  1 248 ? -0.74200  9.55800   14.42800 1.000 14.26000  ? 242 VAL B CB  1 
ATOM   4530 C  CG1 . VAL B  1 248 ? 0.03000   9.77500   15.73100 1.000 16.09000  ? 242 VAL B CG1 1 
ATOM   4531 C  CG2 . VAL B  1 248 ? -2.01300  10.36900  14.47200 1.000 16.15000  ? 242 VAL B CG2 1 
ATOM   4532 N  N   . ALA B  1 249 ? 1.59200   8.18600   12.47000 1.000 16.16000  ? 243 ALA B N   1 
ATOM   4533 C  CA  . ALA B  1 249 ? 2.88800   7.53000   12.33500 1.000 18.07000  ? 243 ALA B CA  1 
ATOM   4534 C  C   . ALA B  1 249 ? 3.08700   7.03800   10.90300 1.000 19.52000  ? 243 ALA B C   1 
ATOM   4535 O  O   . ALA B  1 249 ? 3.68000   7.73300   10.07600 1.000 18.54000  ? 243 ALA B O   1 
ATOM   4536 C  CB  . ALA B  1 249 ? 2.98800   6.35800   13.33100 1.000 14.24000  ? 243 ALA B CB  1 
ATOM   4537 N  N   . GLY B  1 250 ? 2.55700   5.87200   10.56900 1.000 16.47000  ? 244 GLY B N   1 
ATOM   4538 C  CA  . GLY B  1 250 ? 2.67600   5.37300   9.21300  1.000 18.53000  ? 244 GLY B CA  1 
ATOM   4539 C  C   . GLY B  1 250 ? 2.61100   3.86000   9.21100  1.000 18.03000  ? 244 GLY B C   1 
ATOM   4540 O  O   . GLY B  1 250 ? 2.38100   3.24800   10.25000 1.000 18.32000  ? 244 GLY B O   1 
ATOM   4541 N  N   . GLU B  1 251 ? 2.83900   3.27200   8.02600  1.000 19.37000  ? 245 GLU B N   1 
ATOM   4542 C  CA  . GLU B  1 251 ? 2.69100   1.82100   7.88500  1.000 23.51000  ? 245 GLU B CA  1 
ATOM   4543 C  C   . GLU B  1 251 ? 3.72200   1.10200   8.73300  1.000 20.42000  ? 245 GLU B C   1 
ATOM   4544 O  O   . GLU B  1 251 ? 4.89000   1.47800   8.77300  1.000 19.09000  ? 245 GLU B O   1 
ATOM   4545 C  CB  . GLU B  1 251 ? 2.81700   1.38000   6.42400  1.000 28.02000  ? 245 GLU B CB  1 
ATOM   4546 C  CG  . GLU B  1 251 ? 1.57900   1.77100   5.54500  1.000 37.47000  ? 245 GLU B CG  1 
ATOM   4547 C  CD  . GLU B  1 251 ? 0.20700   1.30900   6.11500  1.000 40.11000  ? 245 GLU B CD  1 
ATOM   4548 O  OE1 . GLU B  1 251 ? 0.04800   0.09400   6.38900  1.000 48.72000  ? 245 GLU B OE1 1 
ATOM   4549 O  OE2 . GLU B  1 251 ? -0.70200  2.16200   6.29000  1.000 31.80000  ? 245 GLU B OE2 1 
ATOM   4550 N  N   . GLY B  1 252 ? 3.28300   0.03800   9.41300  1.000 22.41000  ? 246 GLY B N   1 
ATOM   4551 C  CA  . GLY B  1 252 ? 4.18500   -0.71900  10.24200 1.000 18.90000  ? 246 GLY B CA  1 
ATOM   4552 C  C   . GLY B  1 252 ? 4.56300   -0.08500  11.56100 1.000 18.77000  ? 246 GLY B C   1 
ATOM   4553 O  O   . GLY B  1 252 ? 5.21400   -0.75800  12.37400 1.000 20.31000  ? 246 GLY B O   1 
ATOM   4554 N  N   . ARG B  1 253 ? 4.21100   1.19100   11.79700 1.000 16.51000  ? 247 ARG B N   1 
ATOM   4555 C  CA  . ARG B  1 253 ? 4.60800   1.86200   13.01800 1.000 15.24000  ? 247 ARG B CA  1 
ATOM   4556 C  C   . ARG B  1 253 ? 3.70800   1.48400   14.18800 1.000 18.38000  ? 247 ARG B C   1 
ATOM   4557 O  O   . ARG B  1 253 ? 2.49000   1.33400   14.04200 1.000 18.15000  ? 247 ARG B O   1 
ATOM   4558 C  CB  . ARG B  1 253 ? 4.54100   3.38600   12.83100 1.000 18.15000  ? 247 ARG B CB  1 
ATOM   4559 C  CG  . ARG B  1 253 ? 5.46100   3.92200   11.74900 1.000 20.16000  ? 247 ARG B CG  1 
ATOM   4560 C  CD  . ARG B  1 253 ? 6.86000   4.17000   12.33800 1.000 20.32000  ? 247 ARG B CD  1 
ATOM   4561 N  NE  . ARG B  1 253 ? 6.78400   5.07900   13.48000 1.000 18.84000  ? 247 ARG B NE  1 
ATOM   4562 C  CZ  . ARG B  1 253 ? 6.65700   6.39700   13.39300 1.000 17.62000  ? 247 ARG B CZ  1 
ATOM   4563 N  NH1 . ARG B  1 253 ? 6.61300   7.01200   12.21700 1.000 18.62000  ? 247 ARG B NH1 1 
ATOM   4564 N  NH2 . ARG B  1 253 ? 6.54300   7.11500   14.51500 1.000 16.45000  ? 247 ARG B NH2 1 
ATOM   4565 N  N   . TYR B  1 254 ? 4.30400   1.44000   15.38000 1.000 13.82000  ? 248 TYR B N   1 
ATOM   4566 C  CA  . TYR B  1 254 ? 3.55000   1.05600   16.57200 1.000 18.17000  ? 248 TYR B CA  1 
ATOM   4567 C  C   . TYR B  1 254 ? 2.29100   1.87900   16.76900 1.000 19.69000  ? 248 TYR B C   1 
ATOM   4568 O  O   . TYR B  1 254 ? 1.20700   1.31500   16.98200 1.000 18.39000  ? 248 TYR B O   1 
ATOM   4569 C  CB  . TYR B  1 254 ? 4.41800   1.18100   17.82000 1.000 16.63000  ? 248 TYR B CB  1 
ATOM   4570 C  CG  . TYR B  1 254 ? 3.76200   0.59500   19.05000 1.000 18.98000  ? 248 TYR B CG  1 
ATOM   4571 C  CD1 . TYR B  1 254 ? 3.77900   -0.78500  19.27100 1.000 17.36000  ? 248 TYR B CD1 1 
ATOM   4572 C  CD2 . TYR B  1 254 ? 3.10300   1.41000   19.98700 1.000 16.95000  ? 248 TYR B CD2 1 
ATOM   4573 C  CE1 . TYR B  1 254 ? 3.17700   -1.35200  20.38800 1.000 17.70000  ? 248 TYR B CE1 1 
ATOM   4574 C  CE2 . TYR B  1 254 ? 2.49300   0.86900   21.10500 1.000 17.09000  ? 248 TYR B CE2 1 
ATOM   4575 C  CZ  . TYR B  1 254 ? 2.56000   -0.52400  21.32100 1.000 16.17000  ? 248 TYR B CZ  1 
ATOM   4576 O  OH  . TYR B  1 254 ? 1.98900   -1.09900  22.43300 1.000 17.63000  ? 248 TYR B OH  1 
ATOM   4577 N  N   . CYS B  1 255 ? 2.41800   3.22500   16.78600 1.000 16.67000  ? 249 CYS B N   1 
ATOM   4578 C  CA  . CYS B  1 255 ? 1.24100   4.04600   17.07500 1.000 18.77000  ? 249 CYS B CA  1 
ATOM   4579 C  C   . CYS B  1 255 ? 0.08700   3.71300   16.13000 1.000 20.86000  ? 249 CYS B C   1 
ATOM   4580 O  O   . CYS B  1 255 ? -1.06500  3.65600   16.55300 1.000 17.05000  ? 249 CYS B O   1 
ATOM   4581 C  CB  . CYS B  1 255 ? 1.54800   5.53300   16.96100 1.000 17.17000  ? 249 CYS B CB  1 
ATOM   4582 S  SG  . CYS B  1 255 ? 3.03600   6.04600   17.87000 1.000 21.41000  ? 249 CYS B SG  1 
ATOM   4583 N  N   . THR B  1 256 ? 0.38000   3.55600   14.84400 1.000 18.91000  ? 250 THR B N   1 
ATOM   4584 C  CA  . THR B  1 256 ? -0.65000  3.27000   13.84400 1.000 16.90000  ? 250 THR B CA  1 
ATOM   4585 C  C   . THR B  1 256 ? -1.28900  1.91000   14.07000 1.000 22.07000  ? 250 THR B C   1 
ATOM   4586 O  O   . THR B  1 256 ? -2.52000  1.77100   14.04600 1.000 20.85000  ? 250 THR B O   1 
ATOM   4587 C  CB  . THR B  1 256 ? -0.03700  3.34600   12.44400 1.000 16.01000  ? 250 THR B CB  1 
ATOM   4588 O  OG1 . THR B  1 256 ? 0.42000   4.68300   12.19600 1.000 20.47000  ? 250 THR B OG1 1 
ATOM   4589 C  CG2 . THR B  1 256 ? -1.06000  2.94000   11.40100 1.000 17.34000  ? 250 THR B CG2 1 
ATOM   4590 N  N   . MET B  1 257 ? -0.46400  0.88100   14.27100 1.000 20.26000  ? 251 MET B N   1 
ATOM   4591 C  CA  . MET B  1 257 ? -0.99800  -0.44700  14.48300 1.000 19.94000  ? 251 MET B CA  1 
ATOM   4592 C  C   . MET B  1 257 ? -1.77600  -0.52300  15.78800 1.000 21.64000  ? 251 MET B C   1 
ATOM   4593 O  O   . MET B  1 257 ? -2.85500  -1.12100  15.83700 1.000 21.39000  ? 251 MET B O   1 
ATOM   4594 C  CB  . MET B  1 257 ? 0.14500   -1.46000  14.43000 1.000 16.58000  ? 251 MET B CB  1 
ATOM   4595 C  CG  . MET B  1 257 ? 0.83300   -1.45000  13.07300 1.000 18.48000  ? 251 MET B CG  1 
ATOM   4596 S  SD  . MET B  1 257 ? 2.20900   -2.62600  12.95600 1.000 25.31000  ? 251 MET B SD  1 
ATOM   4597 C  CE  . MET B  1 257 ? 1.32400   -4.19800  13.14400 1.000 28.25000  ? 251 MET B CE  1 
ATOM   4598 N  N   . LEU B  1 258 ? -1.27700  0.13200   16.83000 1.000 19.93000  ? 252 LEU B N   1 
ATOM   4599 C  CA  . LEU B  1 258 ? -1.98800  0.17900   18.10300 1.000 17.61000  ? 252 LEU B CA  1 
ATOM   4600 C  C   . LEU B  1 258 ? -3.35700  0.85100   17.94100 1.000 22.34000  ? 252 LEU B C   1 
ATOM   4601 O  O   . LEU B  1 258 ? -4.39500  0.29400   18.33300 1.000 21.72000  ? 252 LEU B O   1 
ATOM   4602 C  CB  . LEU B  1 258 ? -1.12500  0.93000   19.12200 1.000 17.78000  ? 252 LEU B CB  1 
ATOM   4603 C  CG  . LEU B  1 258 ? -1.86600  1.38500   20.38400 1.000 18.85000  ? 252 LEU B CG  1 
ATOM   4604 C  CD1 . LEU B  1 258 ? -1.95800  0.18200   21.31800 1.000 17.19000  ? 252 LEU B CD1 1 
ATOM   4605 C  CD2 . LEU B  1 258 ? -1.21500  2.60900   21.08500 1.000 20.28000  ? 252 LEU B CD2 1 
ATOM   4606 N  N   . MET B  1 259 ? -3.38900  2.02100   17.31400 1.000 18.53000  ? 253 MET B N   1 
ATOM   4607 C  CA  . MET B  1 259 ? -4.67900  2.71300   17.20700 1.000 17.90000  ? 253 MET B CA  1 
ATOM   4608 C  C   . MET B  1 259 ? -5.61500  2.02900   16.22400 1.000 21.18000  ? 253 MET B C   1 
ATOM   4609 O  O   . MET B  1 259 ? -6.82900  2.00600   16.45400 1.000 23.19000  ? 253 MET B O   1 
ATOM   4610 C  CB  . MET B  1 259 ? -4.46200  4.18200   16.85000 1.000 18.21000  ? 253 MET B CB  1 
ATOM   4611 C  CG  . MET B  1 259 ? -3.99800  4.96900   18.05100 1.000 17.12000  ? 253 MET B CG  1 
ATOM   4612 S  SD  . MET B  1 259 ? -3.97400  6.73500   17.68900 1.000 17.73000  ? 253 MET B SD  1 
ATOM   4613 C  CE  . MET B  1 259 ? -2.58400  6.81600   16.53100 1.000 15.56000  ? 253 MET B CE  1 
ATOM   4614 N  N   . ARG B  1 260 ? -5.09300  1.40600   15.16900 1.000 24.36000  ? 254 ARG B N   1 
ATOM   4615 C  CA  . ARG B  1 260 ? -5.96500  0.62100   14.29500 1.000 22.79000  ? 254 ARG B CA  1 
ATOM   4616 C  C   . ARG B  1 260 ? -6.57400  -0.55400  15.04400 1.000 24.48000  ? 254 ARG B C   1 
ATOM   4617 O  O   . ARG B  1 260 ? -7.78800  -0.78400  14.97800 1.000 22.83000  ? 254 ARG B O   1 
ATOM   4618 C  CB  . ARG B  1 260 ? -5.21000  0.10800   13.07900 1.000 26.63000  ? 254 ARG B CB  1 
ATOM   4619 C  CG  . ARG B  1 260 ? -5.16800  1.08500   11.95000 1.000 30.62000  ? 254 ARG B CG  1 
ATOM   4620 C  CD  . ARG B  1 260 ? -4.83600  0.41800   10.61900 1.000 37.86000  ? 254 ARG B CD  1 
ATOM   4621 N  NE  . ARG B  1 260 ? -4.76500  1.43300   9.57500  1.000 43.76000  ? 254 ARG B NE  1 
ATOM   4622 C  CZ  . ARG B  1 260 ? -3.71600  1.68200   8.79900  1.000 38.90000  ? 254 ARG B CZ  1 
ATOM   4623 N  NH1 . ARG B  1 260 ? -2.62600  0.92400   8.83100  1.000 34.75000  ? 254 ARG B NH1 1 
ATOM   4624 N  NH2 . ARG B  1 260 ? -3.77700  2.70200   7.94700  1.000 39.94000  ? 254 ARG B NH2 1 
ATOM   4625 N  N   . ALA B  1 261 ? -5.73600  -1.28700  15.78800 1.000 26.75000  ? 255 ALA B N   1 
ATOM   4626 C  CA  . ALA B  1 261 ? -6.18300  -2.46000  16.53900 1.000 24.93000  ? 255 ALA B CA  1 
ATOM   4627 C  C   . ALA B  1 261 ? -7.34100  -2.12200  17.45500 1.000 23.61000  ? 255 ALA B C   1 
ATOM   4628 O  O   . ALA B  1 261 ? -8.32700  -2.88000  17.54700 1.000 24.30000  ? 255 ALA B O   1 
ATOM   4629 C  CB  . ALA B  1 261 ? -5.02100  -2.99800  17.37500 1.000 24.24000  ? 255 ALA B CB  1 
ATOM   4630 N  N   . PHE B  1 262 ? -7.24300  -0.97800  18.14000 1.000 21.05000  ? 256 PHE B N   1 
ATOM   4631 C  CA  . PHE B  1 262 ? -8.22500  -0.61000  19.14800 1.000 25.06000  ? 256 PHE B CA  1 
ATOM   4632 C  C   . PHE B  1 262 ? -9.41200  0.15500   18.58000 1.000 27.03000  ? 256 PHE B C   1 
ATOM   4633 O  O   . PHE B  1 262 ? -10.39700 0.35500   19.29900 1.000 25.73000  ? 256 PHE B O   1 
ATOM   4634 C  CB  . PHE B  1 262 ? -7.55900  0.20700   20.26100 1.000 22.23000  ? 256 PHE B CB  1 
ATOM   4635 C  CG  . PHE B  1 262 ? -6.89200  -0.64100  21.30100 1.000 20.62000  ? 256 PHE B CG  1 
ATOM   4636 C  CD1 . PHE B  1 262 ? -7.60200  -1.11200  22.39700 1.000 22.38000  ? 256 PHE B CD1 1 
ATOM   4637 C  CD2 . PHE B  1 262 ? -5.54300  -0.95300  21.19400 1.000 19.52000  ? 256 PHE B CD2 1 
ATOM   4638 C  CE1 . PHE B  1 262 ? -6.96200  -1.93500  23.36100 1.000 25.55000  ? 256 PHE B CE1 1 
ATOM   4639 C  CE2 . PHE B  1 262 ? -4.90600  -1.79100  22.13700 1.000 21.04000  ? 256 PHE B CE2 1 
ATOM   4640 C  CZ  . PHE B  1 262 ? -5.61300  -2.25300  23.22500 1.000 24.31000  ? 256 PHE B CZ  1 
ATOM   4641 N  N   . ASP B  1 263 ? -9.34300  0.58600   17.32400 1.000 24.19000  ? 257 ASP B N   1 
ATOM   4642 C  CA  . ASP B  1 263 ? -10.54300 0.96800   16.56800 1.000 23.92000  ? 257 ASP B CA  1 
ATOM   4643 C  C   . ASP B  1 263 ? -11.38900 2.01900   17.30700 1.000 26.83000  ? 257 ASP B C   1 
ATOM   4644 O  O   . ASP B  1 263 ? -12.61200 1.91600   17.40200 1.000 28.13000  ? 257 ASP B O   1 
ATOM   4645 C  CB  . ASP B  1 263 ? -11.37400 -0.27000  16.23400 1.000 25.53000  ? 257 ASP B CB  1 
ATOM   4646 C  CG  . ASP B  1 263 ? -12.40500 -0.01200  15.15400 1.000 30.27000  ? 257 ASP B CG  1 
ATOM   4647 O  OD1 . ASP B  1 263 ? -12.20000 0.91600   14.32700 1.000 34.53000  ? 257 ASP B OD1 1 
ATOM   4648 O  OD2 . ASP B  1 263 ? -13.42700 -0.72100  15.14300 1.000 33.43000  ? 257 ASP B OD2 1 
ATOM   4649 N  N   . GLY B  1 264 ? -10.72600 3.03800   17.84400 1.000 23.67000  ? 258 GLY B N   1 
ATOM   4650 C  CA  . GLY B  1 264 ? -11.39000 4.13400   18.50600 1.000 26.20000  ? 258 GLY B CA  1 
ATOM   4651 C  C   . GLY B  1 264 ? -11.39900 4.06600   20.01500 1.000 24.17000  ? 258 GLY B C   1 
ATOM   4652 O  O   . GLY B  1 264 ? -11.79200 5.05300   20.65200 1.000 26.08000  ? 258 GLY B O   1 
ATOM   4653 N  N   . ALA B  1 265 ? -10.98000 2.94700   20.60600 1.000 23.32000  ? 259 ALA B N   1 
ATOM   4654 C  CA  . ALA B  1 265 ? -11.03900 2.78300   22.05300 1.000 21.69000  ? 259 ALA B CA  1 
ATOM   4655 C  C   . ALA B  1 265 ? -9.96500  3.56800   22.79200 1.000 22.86000  ? 259 ALA B C   1 
ATOM   4656 O  O   . ALA B  1 265 ? -10.11800 3.82500   23.99500 1.000 22.38000  ? 259 ALA B O   1 
ATOM   4657 C  CB  . ALA B  1 265 ? -10.91000 1.32100   22.41900 1.000 24.12000  ? 259 ALA B CB  1 
ATOM   4658 N  N   . LEU B  1 266 ? -8.87700  3.92900   22.11300 1.000 19.20000  ? 260 LEU B N   1 
ATOM   4659 C  CA  . LEU B  1 266 ? -7.80900  4.70000   22.73600 1.000 17.49000  ? 260 LEU B CA  1 
ATOM   4660 C  C   . LEU B  1 266 ? -7.02100  5.41900   21.65100 1.000 20.08000  ? 260 LEU B C   1 
ATOM   4661 O  O   . LEU B  1 266 ? -7.12400  5.07400   20.47100 1.000 20.78000  ? 260 LEU B O   1 
ATOM   4662 C  CB  . LEU B  1 266 ? -6.89800  3.79100   23.56800 1.000 16.11000  ? 260 LEU B CB  1 
ATOM   4663 C  CG  . LEU B  1 266 ? -6.28900  2.53200   22.92300 1.000 16.20000  ? 260 LEU B CG  1 
ATOM   4664 C  CD1 . LEU B  1 266 ? -5.14000  2.85700   21.97100 1.000 16.66000  ? 260 LEU B CD1 1 
ATOM   4665 C  CD2 . LEU B  1 266 ? -5.77400  1.52000   23.99000 1.000 14.48000  ? 260 LEU B CD2 1 
ATOM   4666 N  N   . VAL B  1 267 ? -6.24400  6.43900   22.05800 1.000 16.02000  ? 261 VAL B N   1 
ATOM   4667 C  CA  . VAL B  1 267 ? -5.17300  6.96800   21.21000 1.000 17.79000  ? 261 VAL B CA  1 
ATOM   4668 C  C   . VAL B  1 267 ? -3.82700  6.75400   21.88700 1.000 16.69000  ? 261 VAL B C   1 
ATOM   4669 O  O   . VAL B  1 267 ? -3.71400  6.69100   23.11200 1.000 16.04000  ? 261 VAL B O   1 
ATOM   4670 C  CB  . VAL B  1 267 ? -5.35700  8.46200   20.85300 1.000 16.71000  ? 261 VAL B CB  1 
ATOM   4671 C  CG1 . VAL B  1 267 ? -6.56400  8.64300   19.93100 1.000 17.71000  ? 261 VAL B CG1 1 
ATOM   4672 C  CG2 . VAL B  1 267 ? -5.43600  9.32100   22.11500 1.000 19.78000  ? 261 VAL B CG2 1 
ATOM   4673 N  N   . GLY B  1 268 ? -2.78900  6.66700   21.07700 1.000 15.97000  ? 262 GLY B N   1 
ATOM   4674 C  CA  . GLY B  1 268 ? -1.45400  6.44300   21.59300 1.000 17.93000  ? 262 GLY B CA  1 
ATOM   4675 C  C   . GLY B  1 268 ? -0.44900  7.22300   20.78200 1.000 16.58000  ? 262 GLY B C   1 
ATOM   4676 O  O   . GLY B  1 268 ? -0.64700  7.48300   19.60000 1.000 15.46000  ? 262 GLY B O   1 
ATOM   4677 N  N   . LYS B  1 269 ? 0.63700   7.59500   21.43500 1.000 12.24000  ? 263 LYS B N   1 
ATOM   4678 C  CA  . LYS B  1 269 ? 1.61200   8.45700   20.78000 1.000 14.51000  ? 263 LYS B CA  1 
ATOM   4679 C  C   . LYS B  1 269 ? 3.00100   8.26000   21.36400 1.000 16.60000  ? 263 LYS B C   1 
ATOM   4680 O  O   . LYS B  1 269 ? 3.19200   8.28400   22.58500 1.000 15.89000  ? 263 LYS B O   1 
ATOM   4681 C  CB  . LYS B  1 269 ? 1.19800   9.93300   20.93400 1.000 14.57000  ? 263 LYS B CB  1 
ATOM   4682 C  CG  . LYS B  1 269 ? 2.11800   10.90100  20.27300 1.000 19.75000  ? 263 LYS B CG  1 
ATOM   4683 C  CD  . LYS B  1 269 ? 2.00900   10.89400  18.74800 1.000 21.79000  ? 263 LYS B CD  1 
ATOM   4684 C  CE  . LYS B  1 269 ? 3.13100   11.76700  18.13000 1.000 21.88000  ? 263 LYS B CE  1 
ATOM   4685 N  NZ  . LYS B  1 269 ? 4.34600   10.87800  18.08700 1.000 19.51000  ? 263 LYS B NZ  1 
ATOM   4686 N  N   . LEU B  1 270 ? 3.96900   8.14400   20.46600 1.000 14.88000  ? 264 LEU B N   1 
ATOM   4687 C  CA  . LEU B  1 270 ? 5.37100   7.99500   20.82100 1.000 15.77000  ? 264 LEU B CA  1 
ATOM   4688 C  C   . LEU B  1 270 ? 5.99900   9.34000   21.14600 1.000 12.61000  ? 264 LEU B C   1 
ATOM   4689 O  O   . LEU B  1 270 ? 5.73800   10.32500  20.46500 1.000 15.07000  ? 264 LEU B O   1 
ATOM   4690 C  CB  . LEU B  1 270 ? 6.09500   7.37300   19.62800 1.000 12.12000  ? 264 LEU B CB  1 
ATOM   4691 C  CG  . LEU B  1 270 ? 7.61400   7.34500   19.67800 1.000 11.57000  ? 264 LEU B CG  1 
ATOM   4692 C  CD1 . LEU B  1 270 ? 8.04500   6.35600   20.72300 1.000 13.94000  ? 264 LEU B CD1 1 
ATOM   4693 C  CD2 . LEU B  1 270 ? 8.14200   6.97000   18.26700 1.000 18.11000  ? 264 LEU B CD2 1 
ATOM   4694 N  N   . GLY B  1 271 ? 6.91500   9.37000   22.12700 1.000 15.45000  ? 265 GLY B N   1 
ATOM   4695 C  CA  . GLY B  1 271 ? 7.85600   10.47900  22.28100 1.000 18.94000  ? 265 GLY B CA  1 
ATOM   4696 C  C   . GLY B  1 271 ? 9.27900   9.98300   22.06600 1.000 16.81000  ? 265 GLY B C   1 
ATOM   4697 O  O   . GLY B  1 271 ? 9.63200   8.90400   22.52000 1.000 16.60000  ? 265 GLY B O   1 
ATOM   4698 N  N   . ALA B  1 272 ? 10.09000  10.78200  21.36700 1.000 16.14000  ? 266 ALA B N   1 
ATOM   4699 C  CA  . ALA B  1 272 ? 11.47600  10.38000  21.13700 1.000 16.22000  ? 266 ALA B CA  1 
ATOM   4700 C  C   . ALA B  1 272 ? 12.17000  10.08300  22.45400 1.000 17.12000  ? 266 ALA B C   1 
ATOM   4701 O  O   . ALA B  1 272 ? 11.82300  10.64400  23.50800 1.000 17.49000  ? 266 ALA B O   1 
ATOM   4702 C  CB  . ALA B  1 272 ? 12.24500  11.46800  20.38600 1.000 20.69000  ? 266 ALA B CB  1 
ATOM   4703 N  N   . ASP B  1 273 ? 13.17600  9.20100   22.36100 1.000 19.67000  ? 267 ASP B N   1 
ATOM   4704 C  CA  . ASP B  1 273 ? 13.95000  8.68800   23.49200 1.000 17.60000  ? 267 ASP B CA  1 
ATOM   4705 C  C   . ASP B  1 273 ? 13.09300  7.88800   24.45800 1.000 15.26000  ? 267 ASP B C   1 
ATOM   4706 O  O   . ASP B  1 273 ? 13.31900  7.90900   25.67200 1.000 16.86000  ? 267 ASP B O   1 
ATOM   4707 C  CB  . ASP B  1 273 ? 14.72000  9.79600   24.19300 1.000 15.88000  ? 267 ASP B CB  1 
ATOM   4708 C  CG  . ASP B  1 273 ? 15.96200  10.16000  23.41500 1.000 21.02000  ? 267 ASP B CG  1 
ATOM   4709 O  OD1 . ASP B  1 273 ? 16.79500  9.25800   23.18900 1.000 20.58000  ? 267 ASP B OD1 1 
ATOM   4710 O  OD2 . ASP B  1 273 ? 16.09900  11.31000  22.97600 1.000 23.07000  ? 267 ASP B OD2 1 
ATOM   4711 N  N   . ALA B  1 274 ? 12.11600  7.16700   23.88000 1.000 13.90000  ? 268 ALA B N   1 
ATOM   4712 C  CA  . ALA B  1 274 ? 11.35400  6.08800   24.52200 1.000 18.79000  ? 268 ALA B CA  1 
ATOM   4713 C  C   . ALA B  1 274 ? 10.42200  6.57200   25.63800 1.000 18.30000  ? 268 ALA B C   1 
ATOM   4714 O  O   . ALA B  1 274 ? 10.44400  6.05900   26.75800 1.000 17.26000  ? 268 ALA B O   1 
ATOM   4715 C  CB  . ALA B  1 274 ? 12.28900  4.99100   25.03100 1.000 17.64000  ? 268 ALA B CB  1 
ATOM   4716 N  N   . SER B  1 275 ? 9.55900   7.52400   25.31200 1.000 17.17000  ? 269 SER B N   1 
ATOM   4717 C  CA  . SER B  1 275 ? 8.37200   7.79000   26.10500 1.000 17.89000  ? 269 SER B CA  1 
ATOM   4718 C  C   . SER B  1 275 ? 7.17000   7.37300   25.27800 1.000 15.76000  ? 269 SER B C   1 
ATOM   4719 O  O   . SER B  1 275 ? 7.25100   7.31700   24.04600 1.000 15.76000  ? 269 SER B O   1 
ATOM   4720 C  CB  . SER B  1 275 ? 8.27300   9.28700   26.49800 1.000 16.79000  ? 269 SER B CB  1 
ATOM   4721 O  OG  . SER B  1 275 ? 9.29700   9.54700   27.46200 1.000 21.00000  ? 269 SER B OG  1 
ATOM   4722 N  N   . TYR B  1 276 ? 6.06800   7.04100   25.97200 1.000 14.67000  ? 270 TYR B N   1 
ATOM   4723 C  CA  . TYR B  1 276 ? 4.82100   6.67800   25.31400 1.000 16.99000  ? 270 TYR B CA  1 
ATOM   4724 C  C   . TYR B  1 276 ? 3.64700   7.18200   26.14300 1.000 17.64000  ? 270 TYR B C   1 
ATOM   4725 O  O   . TYR B  1 276 ? 3.70000   7.15500   27.37800 1.000 15.51000  ? 270 TYR B O   1 
ATOM   4726 C  CB  . TYR B  1 276 ? 4.67900   5.14200   25.11100 1.000 12.66000  ? 270 TYR B CB  1 
ATOM   4727 C  CG  . TYR B  1 276 ? 3.89800   4.91300   23.86200 1.000 17.56000  ? 270 TYR B CG  1 
ATOM   4728 C  CD1 . TYR B  1 276 ? 4.52100   4.99400   22.61000 1.000 14.63000  ? 270 TYR B CD1 1 
ATOM   4729 C  CD2 . TYR B  1 276 ? 2.50800   4.74300   23.91300 1.000 15.22000  ? 270 TYR B CD2 1 
ATOM   4730 C  CE1 . TYR B  1 276 ? 3.78100   4.84400   21.43500 1.000 16.79000  ? 270 TYR B CE1 1 
ATOM   4731 C  CE2 . TYR B  1 276 ? 1.77400   4.59000   22.75100 1.000 17.74000  ? 270 TYR B CE2 1 
ATOM   4732 C  CZ  . TYR B  1 276 ? 2.40100   4.66300   21.51800 1.000 19.93000  ? 270 TYR B CZ  1 
ATOM   4733 O  OH  . TYR B  1 276 ? 1.63100   4.53200   20.37300 1.000 19.71000  ? 270 TYR B OH  1 
ATOM   4734 N  N   . ALA B  1 277 ? 2.58600   7.62800   25.45900 1.000 15.89000  ? 271 ALA B N   1 
ATOM   4735 C  CA  . ALA B  1 277 ? 1.38200   8.07300   26.14000 1.000 17.85000  ? 271 ALA B CA  1 
ATOM   4736 C  C   . ALA B  1 277 ? 0.14400   7.48700   25.46900 1.000 15.61000  ? 271 ALA B C   1 
ATOM   4737 O  O   . ALA B  1 277 ? 0.06600   7.40400   24.23400 1.000 14.25000  ? 271 ALA B O   1 
ATOM   4738 C  CB  . ALA B  1 277 ? 1.30200   9.61800   26.17600 1.000 17.09000  ? 271 ALA B CB  1 
ATOM   4739 N  N   . ILE B  1 278 ? -0.83300  7.10600   26.28700 1.000 16.68000  ? 272 ILE B N   1 
ATOM   4740 C  CA  . ILE B  1 278 ? -2.07500  6.50300   25.79100 1.000 16.40000  ? 272 ILE B CA  1 
ATOM   4741 C  C   . ILE B  1 278 ? -3.24100  7.07600   26.56900 1.000 15.26000  ? 272 ILE B C   1 
ATOM   4742 O  O   . ILE B  1 278 ? -3.17800  7.16900   27.79800 1.000 17.68000  ? 272 ILE B O   1 
ATOM   4743 C  CB  . ILE B  1 278 ? -2.07100  4.95700   25.92300 1.000 14.47000  ? 272 ILE B CB  1 
ATOM   4744 C  CG1 . ILE B  1 278 ? -1.03100  4.37600   24.98400 1.000 17.45000  ? 272 ILE B CG1 1 
ATOM   4745 C  CG2 . ILE B  1 278 ? -3.44500  4.41400   25.59800 1.000 14.42000  ? 272 ILE B CG2 1 
ATOM   4746 C  CD1 . ILE B  1 278 ? -0.81700  2.89200   25.15200 1.000 16.28000  ? 272 ILE B CD1 1 
ATOM   4747 N  N   . GLY B  1 279 ? -4.29600  7.47700   25.85800 1.000 13.71000  ? 273 GLY B N   1 
ATOM   4748 C  CA  . GLY B  1 279 ? -5.53300  7.94100   26.47800 1.000 15.00000  ? 273 GLY B CA  1 
ATOM   4749 C  C   . GLY B  1 279 ? -6.63700  6.95500   26.12900 1.000 17.07000  ? 273 GLY B C   1 
ATOM   4750 O  O   . GLY B  1 279 ? -6.86900  6.66600   24.95100 1.000 17.10000  ? 273 GLY B O   1 
ATOM   4751 N  N   . VAL B  1 280 ? -7.29900  6.44000   27.16200 1.000 17.67000  ? 274 VAL B N   1 
ATOM   4752 C  CA  . VAL B  1 280 ? -8.18600  5.28300   27.05100 1.000 18.37000  ? 274 VAL B CA  1 
ATOM   4753 C  C   . VAL B  1 280 ? -9.61700  5.74100   27.36800 1.000 21.85000  ? 274 VAL B C   1 
ATOM   4754 O  O   . VAL B  1 280 ? -9.89000  6.20400   28.48000 1.000 18.25000  ? 274 VAL B O   1 
ATOM   4755 C  CB  . VAL B  1 280 ? -7.77100  4.16300   28.01100 1.000 17.74000  ? 274 VAL B CB  1 
ATOM   4756 C  CG1 . VAL B  1 280 ? -8.77600  3.01900   27.91500 1.000 19.68000  ? 274 VAL B CG1 1 
ATOM   4757 C  CG2 . VAL B  1 280 ? -6.36100  3.68300   27.71500 1.000 16.45000  ? 274 VAL B CG2 1 
ATOM   4758 N  N   . ARG B  1 281 ? -10.53400 5.58400   26.41400 1.000 18.64000  ? 275 ARG B N   1 
ATOM   4759 C  CA  . ARG B  1 281 ? -11.91600 5.95700   26.70400 1.000 20.07000  ? 275 ARG B CA  1 
ATOM   4760 C  C   . ARG B  1 281 ? -12.48200 5.03400   27.76900 1.000 19.32000  ? 275 ARG B C   1 
ATOM   4761 O  O   . ARG B  1 281 ? -12.02400 3.90100   27.94100 1.000 21.34000  ? 275 ARG B O   1 
ATOM   4762 C  CB  . ARG B  1 281 ? -12.79200 5.90100   25.44400 1.000 21.51000  ? 275 ARG B CB  1 
ATOM   4763 C  CG  . ARG B  1 281 ? -12.38600 6.97100   24.42000 1.000 21.04000  ? 275 ARG B CG  1 
ATOM   4764 C  CD  . ARG B  1 281 ? -13.38100 7.03300   23.25400 1.000 23.64000  ? 275 ARG B CD  1 
ATOM   4765 N  NE  . ARG B  1 281 ? -14.72200 7.38700   23.70800 1.000 26.89000  ? 275 ARG B NE  1 
ATOM   4766 C  CZ  . ARG B  1 281 ? -15.81700 7.27800   22.96500 1.000 27.08000  ? 275 ARG B CZ  1 
ATOM   4767 N  NH1 . ARG B  1 281 ? -15.76000 6.87400   21.70600 1.000 26.77000  ? 275 ARG B NH1 1 
ATOM   4768 N  NH2 . ARG B  1 281 ? -17.00000 7.58600   23.49600 1.000 25.52000  ? 275 ARG B NH2 1 
ATOM   4769 N  N   . ALA B  1 282 ? -13.50900 5.52200   28.46900 1.000 20.93000  ? 276 ALA B N   1 
ATOM   4770 C  CA  . ALA B  1 282 ? -14.09700 4.72500   29.52700 1.000 23.43000  ? 276 ALA B CA  1 
ATOM   4771 C  C   . ALA B  1 282 ? -14.64100 3.40900   28.96800 1.000 23.78000  ? 276 ALA B C   1 
ATOM   4772 O  O   . ALA B  1 282 ? -15.24100 3.35000   27.88800 1.000 25.61000  ? 276 ALA B O   1 
ATOM   4773 C  CB  . ALA B  1 282 ? -15.21100 5.50600   30.22800 1.000 22.57000  ? 276 ALA B CB  1 
ATOM   4774 N  N   . SER B  1 283 ? -14.53100 2.36600   29.75600 1.000 23.39000  ? 277 SER B N   1 
ATOM   4775 C  CA  . SER B  1 283 ? -14.87700 1.05100   29.23600 1.000 24.49000  ? 277 SER B CA  1 
ATOM   4776 C  C   . SER B  1 283 ? -15.03500 0.10500   30.41300 1.000 26.50000  ? 277 SER B C   1 
ATOM   4777 O  O   . SER B  1 283 ? -14.79000 0.48500   31.56000 1.000 24.06000  ? 277 SER B O   1 
ATOM   4778 C  CB  . SER B  1 283 ? -13.78900 0.55400   28.29800 1.000 25.64000  ? 277 SER B CB  1 
ATOM   4779 O  OG  . SER B  1 283 ? -12.61900 0.31500   29.05600 1.000 23.85000  ? 277 SER B OG  1 
ATOM   4780 N  N   . ASP B  1 284 ? -15.45500 -1.13800  30.12800 1.000 28.07000  ? 278 ASP B N   1 
ATOM   4781 C  CA  A ASP B  1 284 ? -15.43400 -2.15900  31.16600 0.600 27.83000  ? 278 ASP B CA  1 
ATOM   4782 C  CA  B ASP B  1 284 ? -15.44700 -2.13000  31.19600 0.400 27.87000  ? 278 ASP B CA  1 
ATOM   4783 C  C   . ASP B  1 284 ? -14.04300 -2.28000  31.76500 1.000 26.17000  ? 278 ASP B C   1 
ATOM   4784 O  O   . ASP B  1 284 ? -13.88300 -2.40400  32.98000 1.000 25.33000  ? 278 ASP B O   1 
ATOM   4785 C  CB  A ASP B  1 284 ? -15.87600 -3.49500  30.58900 0.600 33.04000  ? 278 ASP B CB  1 
ATOM   4786 C  CB  B ASP B  1 284 ? -16.01200 -3.48600  30.73500 0.400 33.03000  ? 278 ASP B CB  1 
ATOM   4787 C  CG  A ASP B  1 284 ? -17.00900 -4.07900  31.34900 0.600 35.58000  ? 278 ASP B CG  1 
ATOM   4788 C  CG  B ASP B  1 284 ? -15.16400 -4.18200  29.67400 0.400 33.01000  ? 278 ASP B CG  1 
ATOM   4789 O  OD1 A ASP B  1 284 ? -16.79300 -4.43900  32.52300 0.600 36.30000  ? 278 ASP B OD1 1 
ATOM   4790 O  OD1 B ASP B  1 284 ? -14.04500 -4.67800  29.97700 0.400 36.14000  ? 278 ASP B OD1 1 
ATOM   4791 O  OD2 A ASP B  1 284 ? -18.11800 -4.12200  30.79000 0.600 41.65000  ? 278 ASP B OD2 1 
ATOM   4792 O  OD2 B ASP B  1 284 ? -15.64600 -4.27300  28.52600 0.400 38.12000  ? 278 ASP B OD2 1 
ATOM   4793 N  N   . ALA B  1 285 ? -13.01900 -2.20500  30.90900 1.000 25.42000  ? 279 ALA B N   1 
ATOM   4794 C  CA  . ALA B  1 285 ? -11.63100 -2.34000  31.36500 1.000 25.41000  ? 279 ALA B CA  1 
ATOM   4795 C  C   . ALA B  1 285 ? -11.23900 -1.22800  32.34100 1.000 25.92000  ? 279 ALA B C   1 
ATOM   4796 O  O   . ALA B  1 285 ? -10.67600 -1.51200  33.40800 1.000 24.65000  ? 279 ALA B O   1 
ATOM   4797 C  CB  . ALA B  1 285 ? -10.68500 -2.37300  30.16100 1.000 21.63000  ? 279 ALA B CB  1 
ATOM   4798 N  N   . THR B  1 286 ? -11.53700 0.04700   32.00300 1.000 23.53000  ? 280 THR B N   1 
ATOM   4799 C  CA  . THR B  1 286 ? -11.23500 1.14200   32.92600 1.000 20.40000  ? 280 THR B CA  1 
ATOM   4800 C  C   . THR B  1 286 ? -12.02500 0.99900   34.22600 1.000 23.25000  ? 280 THR B C   1 
ATOM   4801 O  O   . THR B  1 286 ? -11.51000 1.29900   35.31100 1.000 21.92000  ? 280 THR B O   1 
ATOM   4802 C  CB  . THR B  1 286 ? -11.50500 2.52000   32.29000 1.000 24.50000  ? 280 THR B CB  1 
ATOM   4803 O  OG1 . THR B  1 286 ? -12.87300 2.67600   31.94500 1.000 25.80000  ? 280 THR B OG1 1 
ATOM   4804 C  CG2 . THR B  1 286 ? -10.64500 2.75900   31.03400 1.000 26.50000  ? 280 THR B CG2 1 
ATOM   4805 N  N   . ARG B  1 287 ? -13.28400 0.55800   34.14500 1.000 22.05000  ? 281 ARG B N   1 
ATOM   4806 C  CA  . ARG B  1 287 ? -14.06300 0.39900   35.37900 1.000 21.84000  ? 281 ARG B CA  1 
ATOM   4807 C  C   . ARG B  1 287 ? -13.47500 -0.68900  36.27900 1.000 27.11000  ? 281 ARG B C   1 
ATOM   4808 O  O   . ARG B  1 287 ? -13.40500 -0.51200  37.50100 1.000 27.66000  ? 281 ARG B O   1 
ATOM   4809 C  CB  . ARG B  1 287 ? -15.53100 0.10800   35.06700 1.000 24.65000  ? 281 ARG B CB  1 
ATOM   4810 C  CG  . ARG B  1 287 ? -16.21600 1.26300   34.40500 1.000 21.91000  ? 281 ARG B CG  1 
ATOM   4811 C  CD  . ARG B  1 287 ? -17.76200 1.06400   34.30500 1.000 23.65000  ? 281 ARG B CD  1 
ATOM   4812 N  NE  . ARG B  1 287 ? -18.08800 0.19900   33.17900 1.000 26.98000  ? 281 ARG B NE  1 
ATOM   4813 C  CZ  . ARG B  1 287 ? -18.08400 0.58100   31.90600 1.000 28.39000  ? 281 ARG B CZ  1 
ATOM   4814 N  NH1 . ARG B  1 287 ? -17.89700 1.83300   31.56400 1.000 23.98000  ? 281 ARG B NH1 1 
ATOM   4815 N  NH2 . ARG B  1 287 ? -18.34700 -0.31400  30.95500 1.000 36.64000  ? 281 ARG B NH2 1 
ATOM   4816 N  N   . GLN B  1 288 ? -13.07600 -1.83200  35.70000 1.000 25.39000  ? 282 GLN B N   1 
ATOM   4817 C  CA  . GLN B  1 288 ? -12.42800 -2.87900  36.49400 1.000 27.68000  ? 282 GLN B CA  1 
ATOM   4818 C  C   . GLN B  1 288 ? -11.13200 -2.38700  37.12900 1.000 24.27000  ? 282 GLN B C   1 
ATOM   4819 O  O   . GLN B  1 288 ? -10.74500 -2.87300  38.19400 1.000 28.41000  ? 282 GLN B O   1 
ATOM   4820 C  CB  . GLN B  1 288 ? -12.13400 -4.12000  35.63900 1.000 28.21000  ? 282 GLN B CB  1 
ATOM   4821 C  CG  . GLN B  1 288 ? -13.38400 -4.87300  35.20600 1.000 35.89000  ? 282 GLN B CG  1 
ATOM   4822 C  CD  . GLN B  1 288 ? -13.06100 -6.05500  34.32600 1.000 43.46000  ? 282 GLN B CD  1 
ATOM   4823 O  OE1 . GLN B  1 288 ? -11.96300 -6.61800  34.41000 1.000 51.56000  ? 282 GLN B OE1 1 
ATOM   4824 N  NE2 . GLN B  1 288 ? -14.00300 -6.43100  33.46200 1.000 47.62000  ? 282 GLN B NE2 1 
ATOM   4825 N  N   . LEU B  1 289 ? -10.45500 -1.43400  36.50700 1.000 23.61000  ? 283 LEU B N   1 
ATOM   4826 C  CA  . LEU B  1 289 ? -9.25400  -0.84900  37.10300 1.000 23.48000  ? 283 LEU B CA  1 
ATOM   4827 C  C   . LEU B  1 289 ? -9.57300  0.14900   38.21000 1.000 29.31000  ? 283 LEU B C   1 
ATOM   4828 O  O   . LEU B  1 289 ? -8.64200  0.66900   38.84600 1.000 27.17000  ? 283 LEU B O   1 
ATOM   4829 C  CB  . LEU B  1 289 ? -8.43100  -0.12500  36.03400 1.000 20.49000  ? 283 LEU B CB  1 
ATOM   4830 C  CG  . LEU B  1 289 ? -7.76100  -1.07000  35.03200 1.000 22.65000  ? 283 LEU B CG  1 
ATOM   4831 C  CD1 . LEU B  1 289 ? -7.22500  -0.30000  33.83900 1.000 23.49000  ? 283 LEU B CD1 1 
ATOM   4832 C  CD2 . LEU B  1 289 ? -6.65500  -1.92300  35.71500 1.000 19.38000  ? 283 LEU B CD2 1 
ATOM   4833 N  N   . GLY B  1 290 ? -10.84800 0.47700   38.40600 1.000 26.91000  ? 284 GLY B N   1 
ATOM   4834 C  CA  . GLY B  1 290 ? -11.27300 1.27000   39.53800 1.000 29.05000  ? 284 GLY B CA  1 
ATOM   4835 C  C   . GLY B  1 290 ? -11.55300 2.74100   39.30200 1.000 30.77000  ? 284 GLY B C   1 
ATOM   4836 O  O   . GLY B  1 290 ? -11.56200 3.50300   40.27500 1.000 31.86000  ? 284 GLY B O   1 
ATOM   4837 N  N   . THR B  1 291 ? -11.78300 3.17800   38.06300 1.000 26.81000  ? 285 THR B N   1 
ATOM   4838 C  CA  . THR B  1 291 ? -12.19500 4.55500   37.84400 1.000 26.54000  ? 285 THR B CA  1 
ATOM   4839 C  C   . THR B  1 291 ? -13.49300 4.59200   37.04200 1.000 25.13000  ? 285 THR B C   1 
ATOM   4840 O  O   . THR B  1 291 ? -13.82200 3.66300   36.29100 1.000 25.85000  ? 285 THR B O   1 
ATOM   4841 C  CB  . THR B  1 291 ? -11.09800 5.41300   37.16600 1.000 23.67000  ? 285 THR B CB  1 
ATOM   4842 O  OG1 . THR B  1 291 ? -11.56500 6.75900   37.09200 1.000 29.65000  ? 285 THR B OG1 1 
ATOM   4843 C  CG2 . THR B  1 291 ? -10.78500 4.90400   35.78000 1.000 24.99000  ? 285 THR B CG2 1 
ATOM   4844 N  N   . ASP B  1 292 ? -14.28100 5.62600   37.29000 1.000 24.09000  ? 286 ASP B N   1 
ATOM   4845 C  CA  . ASP B  1 292 ? -15.55900 5.78000   36.60700 1.000 24.25000  ? 286 ASP B CA  1 
ATOM   4846 C  C   . ASP B  1 292 ? -15.46900 6.61000   35.33300 1.000 28.20000  ? 286 ASP B C   1 
ATOM   4847 O  O   . ASP B  1 292 ? -16.49400 6.81900   34.69000 1.000 29.75000  ? 286 ASP B O   1 
ATOM   4848 C  CB  . ASP B  1 292 ? -16.61200 6.39700   37.54300 1.000 29.17000  ? 286 ASP B CB  1 
ATOM   4849 C  CG  . ASP B  1 292 ? -16.18700 7.73700   38.12100 1.000 32.87000  ? 286 ASP B CG  1 
ATOM   4850 O  OD1 . ASP B  1 292 ? -15.09800 8.25700   37.77300 1.000 36.35000  ? 286 ASP B OD1 1 
ATOM   4851 O  OD2 . ASP B  1 292 ? -16.95100 8.26600   38.94900 1.000 37.90000  ? 286 ASP B OD2 1 
ATOM   4852 N  N   . GLY B  1 293 ? -14.28800 7.07700   34.93800 1.000 25.58000  ? 287 GLY B N   1 
ATOM   4853 C  CA  . GLY B  1 293 ? -14.15200 7.78700   33.68800 1.000 23.65000  ? 287 GLY B CA  1 
ATOM   4854 C  C   . GLY B  1 293 ? -13.03500 7.20900   32.82400 1.000 23.10000  ? 287 GLY B C   1 
ATOM   4855 O  O   . GLY B  1 293 ? -12.72600 6.00700   32.85900 1.000 19.15000  ? 287 GLY B O   1 
ATOM   4856 N  N   . ALA B  1 294 ? -12.45000 8.09400   32.01600 1.000 20.92000  ? 288 ALA B N   1 
ATOM   4857 C  CA  . ALA B  1 294 ? -11.35000 7.74900   31.13800 1.000 19.00000  ? 288 ALA B CA  1 
ATOM   4858 C  C   . ALA B  1 294 ? -10.05600 7.61900   31.93600 1.000 17.70000  ? 288 ALA B C   1 
ATOM   4859 O  O   . ALA B  1 294 ? -9.99100  7.95200   33.12200 1.000 21.59000  ? 288 ALA B O   1 
ATOM   4860 C  CB  . ALA B  1 294 ? -11.20400 8.77800   30.01700 1.000 19.43000  ? 288 ALA B CB  1 
ATOM   4861 N  N   . LEU B  1 295 ? -9.03100  7.10800   31.26300 1.000 21.14000  ? 289 LEU B N   1 
ATOM   4862 C  CA  . LEU B  1 295 ? -7.76500  6.74000   31.87600 1.000 19.46000  ? 289 LEU B CA  1 
ATOM   4863 C  C   . LEU B  1 295 ? -6.63100  7.22900   30.99000 1.000 20.37000  ? 289 LEU B C   1 
ATOM   4864 O  O   . LEU B  1 295 ? -6.77400  7.31100   29.76500 1.000 19.37000  ? 289 LEU B O   1 
ATOM   4865 C  CB  . LEU B  1 295 ? -7.75200  5.21800   32.05200 1.000 23.62000  ? 289 LEU B CB  1 
ATOM   4866 C  CG  . LEU B  1 295 ? -6.80100  4.44600   32.89000 1.000 25.18000  ? 289 LEU B CG  1 
ATOM   4867 C  CD1 . LEU B  1 295 ? -7.64600  3.42600   33.61100 1.000 26.49000  ? 289 LEU B CD1 1 
ATOM   4868 C  CD2 . LEU B  1 295 ? -5.88100  3.81500   31.89900 1.000 27.00000  ? 289 LEU B CD2 1 
ATOM   4869 N  N   . GLY B  1 296 ? -5.50300  7.57200   31.60400 1.000 18.27000  ? 290 GLY B N   1 
ATOM   4870 C  CA  . GLY B  1 296 ? -4.30300  7.89000   30.85200 1.000 19.16000  ? 290 GLY B CA  1 
ATOM   4871 C  C   . GLY B  1 296 ? -3.13900  7.05300   31.32900 1.000 14.92000  ? 290 GLY B C   1 
ATOM   4872 O  O   . GLY B  1 296 ? -3.05700  6.68900   32.49900 1.000 18.01000  ? 290 GLY B O   1 
ATOM   4873 N  N   . ILE B  1 297 ? -2.24000  6.71800   30.39300 1.000 16.32000  ? 291 ILE B N   1 
ATOM   4874 C  CA  . ILE B  1 297 ? -1.04600  5.91900   30.66800 1.000 18.64000  ? 291 ILE B CA  1 
ATOM   4875 C  C   . ILE B  1 297 ? 0.18300   6.64000   30.11500 1.000 17.82000  ? 291 ILE B C   1 
ATOM   4876 O  O   . ILE B  1 297 ? 0.16700   7.10100   28.97400 1.000 16.04000  ? 291 ILE B O   1 
ATOM   4877 C  CB  . ILE B  1 297 ? -1.13900  4.51600   30.02600 1.000 15.51000  ? 291 ILE B CB  1 
ATOM   4878 C  CG1 . ILE B  1 297 ? -2.39900  3.75500   30.47800 1.000 17.11000  ? 291 ILE B CG1 1 
ATOM   4879 C  CG2 . ILE B  1 297 ? 0.13700   3.70000   30.27800 1.000 13.23000  ? 291 ILE B CG2 1 
ATOM   4880 C  CD1 . ILE B  1 297 ? -2.65700  2.51700   29.59600 1.000 18.61000  ? 291 ILE B CD1 1 
ATOM   4881 N  N   . SER B  1 298 ? 1.25700   6.70200   30.89500 1.000 17.74000  ? 292 SER B N   1 
ATOM   4882 C  CA  . SER B  1 298 ? 2.52000   7.22500   30.36700 1.000 14.12000  ? 292 SER B CA  1 
ATOM   4883 C  C   . SER B  1 298 ? 3.66400   6.32600   30.81400 1.000 18.50000  ? 292 SER B C   1 
ATOM   4884 O  O   . SER B  1 298 ? 3.60600   5.69900   31.87600 1.000 16.54000  ? 292 SER B O   1 
ATOM   4885 C  CB  . SER B  1 298 ? 2.76100   8.68100   30.77700 1.000 17.45000  ? 292 SER B CB  1 
ATOM   4886 O  OG  . SER B  1 298 ? 2.61700   8.83800   32.17200 1.000 16.84000  ? 292 SER B OG  1 
ATOM   4887 N  N   . VAL B  1 299 ? 4.66400   6.18100   29.94000 1.000 16.47000  ? 293 VAL B N   1 
ATOM   4888 C  CA  . VAL B  1 299 ? 5.73900   5.19800   30.11100 1.000 15.16000  ? 293 VAL B CA  1 
ATOM   4889 C  C   . VAL B  1 299 ? 7.02800   5.87600   29.67000 1.000 15.03000  ? 293 VAL B C   1 
ATOM   4890 O  O   . VAL B  1 299 ? 7.03400   6.63600   28.70500 1.000 14.72000  ? 293 VAL B O   1 
ATOM   4891 C  CB  . VAL B  1 299 ? 5.51400   3.91200   29.28700 1.000 14.34000  ? 293 VAL B CB  1 
ATOM   4892 C  CG1 . VAL B  1 299 ? 6.70200   2.95100   29.44200 1.000 17.16000  ? 293 VAL B CG1 1 
ATOM   4893 C  CG2 . VAL B  1 299 ? 4.18000   3.15400   29.72400 1.000 12.89000  ? 293 VAL B CG2 1 
ATOM   4894 N  N   . LYS B  1 300 ? 8.11400   5.62700   30.38900 1.000 17.31000  ? 294 LYS B N   1 
ATOM   4895 C  CA  . LYS B  1 300 ? 9.43200   6.09800   29.95100 1.000 15.89000  ? 294 LYS B CA  1 
ATOM   4896 C  C   . LYS B  1 300 ? 10.41100  4.97700   30.22200 1.000 14.78000  ? 294 LYS B C   1 
ATOM   4897 O  O   . LYS B  1 300 ? 10.40500  4.42100   31.32200 1.000 14.98000  ? 294 LYS B O   1 
ATOM   4898 C  CB  . LYS B  1 300 ? 9.82400   7.39300   30.69500 1.000 13.23000  ? 294 LYS B CB  1 
ATOM   4899 C  CG  . LYS B  1 300 ? 11.34800  7.66800   30.71200 1.000 16.21000  ? 294 LYS B CG  1 
ATOM   4900 C  CD  . LYS B  1 300 ? 11.92700  8.06500   29.35600 1.000 15.74000  ? 294 LYS B CD  1 
ATOM   4901 C  CE  . LYS B  1 300 ? 13.47400  8.40200   29.48600 1.000 14.42000  ? 294 LYS B CE  1 
ATOM   4902 N  NZ  . LYS B  1 300 ? 13.94200  9.04500   28.22000 1.000 16.48000  ? 294 LYS B NZ  1 
ATOM   4903 N  N   . ILE B  1 301 ? 11.21900  4.61200   29.22600 1.000 13.81000  ? 295 ILE B N   1 
ATOM   4904 C  CA  . ILE B  1 301 ? 12.33900  3.71000   29.46000 1.000 14.53000  ? 295 ILE B CA  1 
ATOM   4905 C  C   . ILE B  1 301 ? 13.54400  4.58400   29.78500 1.000 14.79000  ? 295 ILE B C   1 
ATOM   4906 O  O   . ILE B  1 301 ? 13.92200  5.41500   28.97300 1.000 13.27000  ? 295 ILE B O   1 
ATOM   4907 C  CB  . ILE B  1 301 ? 12.61500  2.81900   28.23700 1.000 15.90000  ? 295 ILE B CB  1 
ATOM   4908 C  CG1 . ILE B  1 301 ? 11.35400  2.08800   27.76100 1.000 16.41000  ? 295 ILE B CG1 1 
ATOM   4909 C  CG2 . ILE B  1 301 ? 13.75100  1.85000   28.53000 1.000 13.95000  ? 295 ILE B CG2 1 
ATOM   4910 C  CD1 . ILE B  1 301 ? 10.84100  0.98300   28.72400 1.000 16.10000  ? 295 ILE B CD1 1 
ATOM   4911 N  N   . GLU B  1 302 ? 14.13000  4.39700   30.96400 1.000 13.15000  ? 296 GLU B N   1 
ATOM   4912 C  CA  . GLU B  1 302 ? 15.15200  5.30400   31.48000 1.000 13.90000  ? 296 GLU B CA  1 
ATOM   4913 C  C   . GLU B  1 302 ? 16.30800  5.53600   30.50300 1.000 15.74000  ? 296 GLU B C   1 
ATOM   4914 O  O   . GLU B  1 302 ? 16.80800  6.65600   30.39100 1.000 15.85000  ? 296 GLU B O   1 
ATOM   4915 C  CB  . GLU B  1 302 ? 15.69900  4.75800   32.79600 1.000 14.41000  ? 296 GLU B CB  1 
ATOM   4916 C  CG  . GLU B  1 302 ? 16.76200  5.66300   33.43700 1.000 18.44000  ? 296 GLU B CG  1 
ATOM   4917 C  CD  . GLU B  1 302 ? 16.20300  7.03200   33.80500 1.000 19.17000  ? 296 GLU B CD  1 
ATOM   4918 O  OE1 . GLU B  1 302 ? 15.01400  7.13500   34.19100 1.000 18.40000  ? 296 GLU B OE1 1 
ATOM   4919 O  OE2 . GLU B  1 302 ? 16.94100  8.03400   33.70700 1.000 18.15000  ? 296 GLU B OE2 1 
ATOM   4920 N  N   . ASP B  1 303 ? 16.78200  4.48200   29.84800 1.000 16.66000  ? 297 ASP B N   1 
ATOM   4921 C  CA  . ASP B  1 303 ? 17.93100  4.54200   28.94100 1.000 16.36000  ? 297 ASP B CA  1 
ATOM   4922 C  C   . ASP B  1 303 ? 17.52600  4.85900   27.50300 1.000 16.19000  ? 297 ASP B C   1 
ATOM   4923 O  O   . ASP B  1 303 ? 18.40600  4.95900   26.63400 1.000 16.62000  ? 297 ASP B O   1 
ATOM   4924 C  CB  . ASP B  1 303 ? 18.68300  3.20800   28.97700 1.000 17.37000  ? 297 ASP B CB  1 
ATOM   4925 C  CG  . ASP B  1 303 ? 17.73200  2.02200   28.67400 1.000 16.93000  ? 297 ASP B CG  1 
ATOM   4926 O  OD1 . ASP B  1 303 ? 17.50400  1.73400   27.48300 1.000 16.78000  ? 297 ASP B OD1 1 
ATOM   4927 O  OD2 . ASP B  1 303 ? 17.17300  1.45200   29.63700 1.000 15.46000  ? 297 ASP B OD2 1 
ATOM   4928 N  N   . GLY B  1 304 ? 16.21800  5.01700   27.22800 1.000 14.19000  ? 298 GLY B N   1 
ATOM   4929 C  CA  . GLY B  1 304 ? 15.79300  5.46900   25.91300 1.000 15.91000  ? 298 GLY B CA  1 
ATOM   4930 C  C   . GLY B  1 304 ? 15.62900  4.43000   24.81000 1.000 17.26000  ? 298 GLY B C   1 
ATOM   4931 O  O   . GLY B  1 304 ? 15.50700  4.82800   23.63900 1.000 15.77000  ? 298 GLY B O   1 
ATOM   4932 N  N   . ASN B  1 305 ? 15.58300  3.12500   25.12900 1.000 14.08000  ? 299 ASN B N   1 
ATOM   4933 C  CA  . ASN B  1 305 ? 15.49600  2.08600   24.10800 1.000 16.52000  ? 299 ASN B CA  1 
ATOM   4934 C  C   . ASN B  1 305 ? 14.06300  1.93000   23.59100 1.000 17.71000  ? 299 ASN B C   1 
ATOM   4935 O  O   . ASN B  1 305 ? 13.15200  1.57000   24.34500 1.000 16.04000  ? 299 ASN B O   1 
ATOM   4936 C  CB  . ASN B  1 305 ? 16.01500  0.76000   24.68600 1.000 16.45000  ? 299 ASN B CB  1 
ATOM   4937 C  CG  . ASN B  1 305 ? 16.13300  -0.32700  23.64700 1.000 19.12000  ? 299 ASN B CG  1 
ATOM   4938 O  OD1 . ASN B  1 305 ? 15.14300  -0.80000  23.14400 1.000 17.45000  ? 299 ASN B OD1 1 
ATOM   4939 N  ND2 . ASN B  1 305 ? 17.35300  -0.72800  23.32500 1.000 21.57000  ? 299 ASN B ND2 1 
ATOM   4940 N  N   . LEU B  1 306 ? 13.88700  2.18000   22.29900 1.000 16.15000  ? 300 LEU B N   1 
ATOM   4941 C  CA  . LEU B  1 306 ? 12.56300  2.18200   21.67600 1.000 18.07000  ? 300 LEU B CA  1 
ATOM   4942 C  C   . LEU B  1 306 ? 11.97400  0.76700   21.58300 1.000 19.12000  ? 300 LEU B C   1 
ATOM   4943 O  O   . LEU B  1 306 ? 10.77500  0.55600   21.83400 1.000 16.01000  ? 300 LEU B O   1 
ATOM   4944 C  CB  . LEU B  1 306 ? 12.70300  2.78800   20.28300 1.000 19.44000  ? 300 LEU B CB  1 
ATOM   4945 C  CG  . LEU B  1 306 ? 11.44500  2.85200   19.44300 1.000 24.33000  ? 300 LEU B CG  1 
ATOM   4946 C  CD1 . LEU B  1 306 ? 10.52300  3.89600   20.06700 1.000 27.00000  ? 300 LEU B CD1 1 
ATOM   4947 C  CD2 . LEU B  1 306 ? 11.78800  3.21800   17.98800 1.000 31.48000  ? 300 LEU B CD2 1 
ATOM   4948 N  N   . GLU B  1 307 ? 12.78700  -0.21300  21.17500 1.000 16.06000  ? 301 GLU B N   1 
ATOM   4949 C  CA  . GLU B  1 307 ? 12.30000  -1.58100  21.10800 1.000 18.00000  ? 301 GLU B CA  1 
ATOM   4950 C  C   . GLU B  1 307 ? 11.75200  -2.03900  22.45400 1.000 19.36000  ? 301 GLU B C   1 
ATOM   4951 O  O   . GLU B  1 307 ? 10.67400  -2.65300  22.52800 1.000 18.55000  ? 301 GLU B O   1 
ATOM   4952 C  CB  . GLU B  1 307 ? 13.41100  -2.50100  20.64500 1.000 18.34000  ? 301 GLU B CB  1 
ATOM   4953 C  CG  . GLU B  1 307 ? 12.98400  -3.98500  20.52900 1.000 23.09000  ? 301 GLU B CG  1 
ATOM   4954 C  CD  . GLU B  1 307 ? 14.13700  -4.89800  20.15400 1.000 22.29000  ? 301 GLU B CD  1 
ATOM   4955 O  OE1 . GLU B  1 307 ? 15.20000  -4.79000  20.79900 1.000 20.88000  ? 301 GLU B OE1 1 
ATOM   4956 O  OE2 . GLU B  1 307 ? 13.99200  -5.72200  19.21900 1.000 22.26000  ? 301 GLU B OE2 1 
ATOM   4957 N  N   . MET B  1 308 ? 12.46200  -1.71500  23.53600 1.000 15.73000  ? 302 MET B N   1 
ATOM   4958 C  CA  . MET B  1 308 ? 11.97500  -2.07700  24.85600 1.000 14.12000  ? 302 MET B CA  1 
ATOM   4959 C  C   . MET B  1 308 ? 10.70200  -1.30000  25.22200 1.000 14.69000  ? 302 MET B C   1 
ATOM   4960 O  O   . MET B  1 308 ? 9.81700   -1.85400  25.87800 1.000 16.16000  ? 302 MET B O   1 
ATOM   4961 C  CB  . MET B  1 308 ? 13.08000  -1.84600  25.88600 1.000 18.09000  ? 302 MET B CB  1 
ATOM   4962 C  CG  . MET B  1 308 ? 14.29100  -2.82700  25.74200 1.000 15.30000  ? 302 MET B CG  1 
ATOM   4963 S  SD  . MET B  1 308 ? 13.87600  -4.58500  25.90300 1.000 18.47000  ? 302 MET B SD  1 
ATOM   4964 C  CE  . MET B  1 308 ? 13.72900  -4.99000  24.15700 1.000 18.62000  ? 302 MET B CE  1 
ATOM   4965 N  N   . LEU B  1 309 ? 10.61600  -0.01700  24.84800 1.000 15.99000  ? 303 LEU B N   1 
ATOM   4966 C  CA  . LEU B  1 309 ? 9.39400   0.75500   25.10700 1.000 14.30000  ? 303 LEU B CA  1 
ATOM   4967 C  C   . LEU B  1 309 ? 8.17200   0.01800   24.56600 1.000 14.52000  ? 303 LEU B C   1 
ATOM   4968 O  O   . LEU B  1 309 ? 7.22300   -0.24000  25.30100 1.000 15.29000  ? 303 LEU B O   1 
ATOM   4969 C  CB  . LEU B  1 309 ? 9.48900   2.14800   24.49200 1.000 15.58000  ? 303 LEU B CB  1 
ATOM   4970 C  CG  . LEU B  1 309 ? 8.18400   2.98000   24.60200 1.000 15.37000  ? 303 LEU B CG  1 
ATOM   4971 C  CD1 . LEU B  1 309 ? 8.01900   3.54800   26.02700 1.000 11.02000  ? 303 LEU B CD1 1 
ATOM   4972 C  CD2 . LEU B  1 309 ? 8.24200   4.04400   23.54800 1.000 11.90000  ? 303 LEU B CD2 1 
ATOM   4973 N  N   . TYR B  1 310 ? 8.18100   -0.31100  23.27100 1.000 15.02000  ? 304 TYR B N   1 
ATOM   4974 C  CA  . TYR B  1 310 ? 7.02100   -0.94800  22.65000 1.000 12.47000  ? 304 TYR B CA  1 
ATOM   4975 C  C   . TYR B  1 310 ? 6.67600   -2.28400  23.31600 1.000 15.54000  ? 304 TYR B C   1 
ATOM   4976 O  O   . TYR B  1 310 ? 5.49400   -2.61100  23.48300 1.000 18.20000  ? 304 TYR B O   1 
ATOM   4977 C  CB  . TYR B  1 310 ? 7.27600   -1.18800  21.17300 1.000 18.71000  ? 304 TYR B CB  1 
ATOM   4978 C  CG  . TYR B  1 310 ? 7.42700   0.04800   20.38400 1.000 17.71000  ? 304 TYR B CG  1 
ATOM   4979 C  CD1 . TYR B  1 310 ? 6.63000   1.17600   20.66800 1.000 18.40000  ? 304 TYR B CD1 1 
ATOM   4980 C  CD2 . TYR B  1 310 ? 8.33500   0.12300   19.34400 1.000 16.96000  ? 304 TYR B CD2 1 
ATOM   4981 C  CE1 . TYR B  1 310 ? 6.72800   2.32000   19.94200 1.000 19.77000  ? 304 TYR B CE1 1 
ATOM   4982 C  CE2 . TYR B  1 310 ? 8.43100   1.30600   18.58900 1.000 21.05000  ? 304 TYR B CE2 1 
ATOM   4983 C  CZ  . TYR B  1 310 ? 7.62700   2.38500   18.91000 1.000 22.61000  ? 304 TYR B CZ  1 
ATOM   4984 O  OH  . TYR B  1 310 ? 7.67700   3.57100   18.20700 1.000 20.87000  ? 304 TYR B OH  1 
ATOM   4985 N  N   . ALA B  1 311 ? 7.67900   -3.05900  23.71200 1.000 15.67000  ? 305 ALA B N   1 
ATOM   4986 C  CA  . ALA B  1 311 ? 7.40500   -4.31900  24.42100 1.000 16.76000  ? 305 ALA B CA  1 
ATOM   4987 C  C   . ALA B  1 311 ? 6.74700   -4.04200  25.76700 1.000 17.71000  ? 305 ALA B C   1 
ATOM   4988 O  O   . ALA B  1 311 ? 5.75500   -4.69800  26.13700 1.000 17.97000  ? 305 ALA B O   1 
ATOM   4989 C  CB  . ALA B  1 311 ? 8.69500   -5.11500  24.61000 1.000 14.93000  ? 305 ALA B CB  1 
ATOM   4990 N  N   . VAL B  1 312 ? 7.26200   -3.04100  26.49200 1.000 15.04000  ? 306 VAL B N   1 
ATOM   4991 C  CA  . VAL B  1 312 ? 6.74700   -2.74100  27.82000 1.000 13.03000  ? 306 VAL B CA  1 
ATOM   4992 C  C   . VAL B  1 312 ? 5.31800   -2.22100  27.72600 1.000 14.95000  ? 306 VAL B C   1 
ATOM   4993 O  O   . VAL B  1 312 ? 4.46200   -2.58000  28.54100 1.000 14.92000  ? 306 VAL B O   1 
ATOM   4994 C  CB  . VAL B  1 312 ? 7.67300   -1.73400  28.52800 1.000 15.75000  ? 306 VAL B CB  1 
ATOM   4995 C  CG1 . VAL B  1 312 ? 6.95100   -1.01700  29.68200 1.000 15.01000  ? 306 VAL B CG1 1 
ATOM   4996 C  CG2 . VAL B  1 312 ? 8.96700   -2.41100  28.97500 1.000 11.43000  ? 306 VAL B CG2 1 
ATOM   4997 N  N   . VAL B  1 313 ? 5.07400   -1.28500  26.79000 1.000 14.19000  ? 307 VAL B N   1 
ATOM   4998 C  CA  . VAL B  1 313 ? 3.74600   -0.68900  26.64600 1.000 16.52000  ? 307 VAL B CA  1 
ATOM   4999 C  C   . VAL B  1 313 ? 2.73900   -1.77700  26.32300 1.000 19.42000  ? 307 VAL B C   1 
ATOM   5000 O  O   . VAL B  1 313 ? 1.64400   -1.79900  26.89200 1.000 17.43000  ? 307 VAL B O   1 
ATOM   5001 C  CB  . VAL B  1 313 ? 3.75500   0.45500   25.59300 1.000 13.44000  ? 307 VAL B CB  1 
ATOM   5002 C  CG1 . VAL B  1 313 ? 2.31500   0.90400   25.15600 1.000 11.86000  ? 307 VAL B CG1 1 
ATOM   5003 C  CG2 . VAL B  1 313 ? 4.56200   1.69600   26.07000 1.000 14.42000  ? 307 VAL B CG2 1 
ATOM   5004 N  N   . THR B  1 314 ? 3.13800   -2.76700  25.48700 1.000 14.76000  ? 308 THR B N   1 
ATOM   5005 C  CA  . THR B  1 314 ? 2.19200   -3.81900  25.12000 1.000 17.61000  ? 308 THR B CA  1 
ATOM   5006 C  C   . THR B  1 314 ? 1.96100   -4.75100  26.30000 1.000 16.82000  ? 308 THR B C   1 
ATOM   5007 O  O   . THR B  1 314 ? 0.83600   -5.20900  26.53100 1.000 15.51000  ? 308 THR B O   1 
ATOM   5008 C  CB  . THR B  1 314 ? 2.66700   -4.61000  23.88700 1.000 15.27000  ? 308 THR B CB  1 
ATOM   5009 O  OG1 . THR B  1 314 ? 3.01300   -3.67800  22.84200 1.000 16.68000  ? 308 THR B OG1 1 
ATOM   5010 C  CG2 . THR B  1 314 ? 1.47900   -5.50900  23.37900 1.000 20.57000  ? 308 THR B CG2 1 
ATOM   5011 N  N   . GLU B  1 315 ? 3.01800   -5.02100  27.06500 1.000 15.37000  ? 309 GLU B N   1 
ATOM   5012 C  CA  . GLU B  1 315 ? 2.87400   -5.82100  28.27300 1.000 17.15000  ? 309 GLU B CA  1 
ATOM   5013 C  C   . GLU B  1 315 ? 1.97600   -5.10100  29.28000 1.000 15.65000  ? 309 GLU B C   1 
ATOM   5014 O  O   . GLU B  1 315 ? 1.11900   -5.71500  29.92600 1.000 16.65000  ? 309 GLU B O   1 
ATOM   5015 C  CB  . GLU B  1 315 ? 4.26800   -6.11700  28.85800 1.000 15.95000  ? 309 GLU B CB  1 
ATOM   5016 C  CG  . GLU B  1 315 ? 4.25500   -6.81800  30.21800 1.000 15.41000  ? 309 GLU B CG  1 
ATOM   5017 C  CD  . GLU B  1 315 ? 3.75000   -8.23100  30.18600 1.000 17.94000  ? 309 GLU B CD  1 
ATOM   5018 O  OE1 . GLU B  1 315 ? 3.62500   -8.82900  29.09300 1.000 18.59000  ? 309 GLU B OE1 1 
ATOM   5019 O  OE2 . GLU B  1 315 ? 3.50300   -8.78100  31.28500 1.000 20.65000  ? 309 GLU B OE2 1 
ATOM   5020 N  N   . LEU B  1 316 ? 2.11800   -3.79200  29.37800 1.000 15.75000  ? 310 LEU B N   1 
ATOM   5021 C  CA  . LEU B  1 316 ? 1.34000   -3.04600  30.35000 1.000 14.90000  ? 310 LEU B CA  1 
ATOM   5022 C  C   . LEU B  1 316 ? -0.14300  -3.09000  30.01700 1.000 16.40000  ? 310 LEU B C   1 
ATOM   5023 O  O   . LEU B  1 316 ? -0.97700  -3.20000  30.92200 1.000 15.41000  ? 310 LEU B O   1 
ATOM   5024 C  CB  . LEU B  1 316 ? 1.86400   -1.60600  30.40900 1.000 13.52000  ? 310 LEU B CB  1 
ATOM   5025 C  CG  . LEU B  1 316 ? 1.26800   -0.68000  31.45400 1.000 19.31000  ? 310 LEU B CG  1 
ATOM   5026 C  CD1 . LEU B  1 316 ? 1.25700   -1.28500  32.84400 1.000 18.17000  ? 310 LEU B CD1 1 
ATOM   5027 C  CD2 . LEU B  1 316 ? 2.12200   0.65000   31.44800 1.000 18.14000  ? 310 LEU B CD2 1 
ATOM   5028 N  N   . LEU B  1 317 ? -0.48600  -3.00800  28.72800 1.000 14.86000  ? 311 LEU B N   1 
ATOM   5029 C  CA  . LEU B  1 317 ? -1.88600  -3.11100  28.32200 1.000 18.98000  ? 311 LEU B CA  1 
ATOM   5030 C  C   . LEU B  1 317 ? -2.45200  -4.46900  28.67000 1.000 18.89000  ? 311 LEU B C   1 
ATOM   5031 O  O   . LEU B  1 317 ? -3.58500  -4.58100  29.13300 1.000 18.72000  ? 311 LEU B O   1 
ATOM   5032 C  CB  . LEU B  1 317 ? -2.00500  -2.85300  26.82500 1.000 19.00000  ? 311 LEU B CB  1 
ATOM   5033 C  CG  . LEU B  1 317 ? -1.70600  -1.39200  26.46400 1.000 20.61000  ? 311 LEU B CG  1 
ATOM   5034 C  CD1 . LEU B  1 317 ? -1.60300  -1.23800  24.94800 1.000 24.09000  ? 311 LEU B CD1 1 
ATOM   5035 C  CD2 . LEU B  1 317 ? -2.76700  -0.49300  27.02700 1.000 23.96000  ? 311 LEU B CD2 1 
ATOM   5036 N  N   . GLU B  1 318 ? -1.66800  -5.51300  28.46000 1.000 17.53000  ? 312 GLU B N   1 
ATOM   5037 C  CA  . GLU B  1 318 ? -2.12400  -6.82700  28.86600 1.000 20.78000  ? 312 GLU B CA  1 
ATOM   5038 C  C   . GLU B  1 318 ? -2.36200  -6.88800  30.37400 1.000 19.12000  ? 312 GLU B C   1 
ATOM   5039 O  O   . GLU B  1 318 ? -3.35800  -7.46300  30.83000 1.000 20.64000  ? 312 GLU B O   1 
ATOM   5040 C  CB  . GLU B  1 318 ? -1.10900  -7.87300  28.41900 1.000 19.17000  ? 312 GLU B CB  1 
ATOM   5041 C  CG  . GLU B  1 318 ? -1.60600  -9.27600  28.66200 1.000 23.60000  ? 312 GLU B CG  1 
ATOM   5042 C  CD  . GLU B  1 318 ? -0.68600  -10.36400 28.08000 1.000 28.85000  ? 312 GLU B CD  1 
ATOM   5043 O  OE1 . GLU B  1 318 ? 0.35500   -10.71200 28.69900 1.000 26.83000  ? 312 GLU B OE1 1 
ATOM   5044 O  OE2 . GLU B  1 318 ? -1.02200  -10.88600 26.99800 1.000 35.06000  ? 312 GLU B OE2 1 
ATOM   5045 N  N   . ARG B  1 319 ? -1.45900  -6.29600  31.16500 1.000 19.19000  ? 313 ARG B N   1 
ATOM   5046 C  CA  . ARG B  1 319 ? -1.60800  -6.34800  32.61400 1.000 19.90000  ? 313 ARG B CA  1 
ATOM   5047 C  C   . ARG B  1 319 ? -2.80000  -5.53500  33.09000 1.000 19.31000  ? 313 ARG B C   1 
ATOM   5048 O  O   . ARG B  1 319 ? -3.39400  -5.84600  34.12300 1.000 19.57000  ? 313 ARG B O   1 
ATOM   5049 C  CB  . ARG B  1 319 ? -0.33900  -5.84400  33.28000 1.000 19.22000  ? 313 ARG B CB  1 
ATOM   5050 C  CG  . ARG B  1 319 ? 0.84800   -6.78800  32.96800 1.000 23.46000  ? 313 ARG B CG  1 
ATOM   5051 C  CD  . ARG B  1 319 ? 1.79700   -6.86400  34.11200 1.000 24.85000  ? 313 ARG B CD  1 
ATOM   5052 N  NE  . ARG B  1 319 ? 3.04600   -7.50800  33.73000 1.000 20.32000  ? 313 ARG B NE  1 
ATOM   5053 C  CZ  . ARG B  1 319 ? 4.12600   -7.48500  34.49900 1.000 20.14000  ? 313 ARG B CZ  1 
ATOM   5054 N  NH1 . ARG B  1 319 ? 4.11300   -6.88400  35.67400 1.000 19.53000  ? 313 ARG B NH1 1 
ATOM   5055 N  NH2 . ARG B  1 319 ? 5.24000   -8.07600  34.07600 1.000 19.33000  ? 313 ARG B NH2 1 
ATOM   5056 N  N   . LEU B  1 320 ? -3.14800  -4.50300  32.36400 1.000 18.67000  ? 314 LEU B N   1 
ATOM   5057 C  CA  . LEU B  1 320 ? -4.29800  -3.67100  32.71700 1.000 21.24000  ? 314 LEU B CA  1 
ATOM   5058 C  C   . LEU B  1 320 ? -5.60000  -4.21300  32.15500 1.000 22.60000  ? 314 LEU B C   1 
ATOM   5059 O  O   . LEU B  1 320 ? -6.66700  -3.64200  32.41800 1.000 21.55000  ? 314 LEU B O   1 
ATOM   5060 C  CB  . LEU B  1 320 ? -4.06300  -2.23800  32.23000 1.000 18.18000  ? 314 LEU B CB  1 
ATOM   5061 C  CG  . LEU B  1 320 ? -2.82700  -1.53700  32.83000 1.000 20.47000  ? 314 LEU B CG  1 
ATOM   5062 C  CD1 . LEU B  1 320 ? -2.47200  -0.26000  32.07200 1.000 18.82000  ? 314 LEU B CD1 1 
ATOM   5063 C  CD2 . LEU B  1 320 ? -3.00800  -1.21100  34.31400 1.000 21.20000  ? 314 LEU B CD2 1 
ATOM   5064 N  N   . GLY B  1 321 ? -5.53800  -5.29400  31.39400 1.000 21.35000  ? 315 GLY B N   1 
ATOM   5065 C  CA  . GLY B  1 321 ? -6.72300  -5.84400  30.79800 1.000 23.33000  ? 315 GLY B CA  1 
ATOM   5066 C  C   . GLY B  1 321 ? -7.36600  -4.94000  29.77700 1.000 23.62000  ? 315 GLY B C   1 
ATOM   5067 O  O   . GLY B  1 321 ? -8.59000  -4.99800  29.58200 1.000 25.48000  ? 315 GLY B O   1 
ATOM   5068 N  N   . ILE B  1 322 ? -6.57100  -4.13100  29.09700 1.000 24.76000  ? 316 ILE B N   1 
ATOM   5069 C  CA  . ILE B  1 322 ? -7.06600  -3.22900  28.06900 1.000 26.59000  ? 316 ILE B CA  1 
ATOM   5070 C  C   . ILE B  1 322 ? -6.90500  -3.91400  26.72100 1.000 29.72000  ? 316 ILE B C   1 
ATOM   5071 O  O   . ILE B  1 322 ? -5.78700  -4.23100  26.30200 1.000 31.13000  ? 316 ILE B O   1 
ATOM   5072 C  CB  . ILE B  1 322 ? -6.34600  -1.87700  28.13500 1.000 24.55000  ? 316 ILE B CB  1 
ATOM   5073 C  CG1 . ILE B  1 322 ? -6.75600  -1.22300  29.45600 1.000 25.66000  ? 316 ILE B CG1 1 
ATOM   5074 C  CG2 . ILE B  1 322 ? -6.72700  -0.97000  26.94800 1.000 22.60000  ? 316 ILE B CG2 1 
ATOM   5075 C  CD1 . ILE B  1 322 ? -5.95700  -0.06300  29.82800 1.000 22.45000  ? 316 ILE B CD1 1 
ATOM   5076 N  N   . GLY B  1 323 ? -8.02000  -4.13300  26.04800 1.000 37.86000  ? 317 GLY B N   1 
ATOM   5077 C  CA  . GLY B  1 323 ? -8.03500  -4.85400  24.79600 1.000 38.96000  ? 317 GLY B CA  1 
ATOM   5078 C  C   . GLY B  1 323 ? -8.56000  -6.25700  24.98800 1.000 45.29000  ? 317 GLY B C   1 
ATOM   5079 O  O   . GLY B  1 323 ? -8.96300  -6.67100  26.07800 1.000 43.97000  ? 317 GLY B O   1 
ATOM   5080 N  N   . SER B  1 324 ? -8.57300  -6.97700  23.89300 1.000 42.54000  ? 318 SER B N   1 
ATOM   5081 C  CA  . SER B  1 324 ? -8.72100  -8.41700  23.89500 1.000 48.58000  ? 318 SER B CA  1 
ATOM   5082 C  C   . SER B  1 324 ? -7.38700  -9.05300  23.53200 1.000 51.63000  ? 318 SER B C   1 
ATOM   5083 O  O   . SER B  1 324 ? -6.51500  -8.38900  22.95600 1.000 45.49000  ? 318 SER B O   1 
ATOM   5084 C  CB  . SER B  1 324 ? -9.78700  -8.83800  22.88500 1.000 48.43000  ? 318 SER B CB  1 
ATOM   5085 O  OG  . SER B  1 324 ? -9.58100  -8.15800  21.66400 1.000 53.49000  ? 318 SER B OG  1 
ATOM   5086 N  N   . PRO B  1 325 ? -7.17000  -10.33100 23.87600 1.000 60.94000  ? 319 PRO B N   1 
ATOM   5087 C  CA  . PRO B  1 325 ? -6.01300  -11.03500 23.29900 1.000 58.40000  ? 319 PRO B CA  1 
ATOM   5088 C  C   . PRO B  1 325 ? -5.98500  -10.94900 21.78500 1.000 58.05000  ? 319 PRO B C   1 
ATOM   5089 O  O   . PRO B  1 325 ? -4.89600  -10.91800 21.19500 1.000 59.11000  ? 319 PRO B O   1 
ATOM   5090 C  CB  . PRO B  1 325 ? -6.19400  -12.47600 23.79500 1.000 55.34000  ? 319 PRO B CB  1 
ATOM   5091 C  CG  . PRO B  1 325 ? -6.90700  -12.32000 25.09300 1.000 57.43000  ? 319 PRO B CG  1 
ATOM   5092 C  CD  . PRO B  1 325 ? -7.84300  -11.14200 24.90800 1.000 58.15000  ? 319 PRO B CD  1 
ATOM   5093 N  N   . ASP B  1 326 ? -7.16000  -10.85700 21.14500 1.000 48.10000  ? 320 ASP B N   1 
ATOM   5094 C  CA  . ASP B  1 326 ? -7.22900  -10.73200 19.69300 1.000 46.10000  ? 320 ASP B CA  1 
ATOM   5095 C  C   . ASP B  1 326 ? -6.81500  -9.34200  19.22900 1.000 49.79000  ? 320 ASP B C   1 
ATOM   5096 O  O   . ASP B  1 326 ? -6.12400  -9.20200  18.21300 1.000 47.24000  ? 320 ASP B O   1 
ATOM   5097 C  CB  . ASP B  1 326 ? -8.64100  -11.05000 19.22400 1.000 56.20000  ? 320 ASP B CB  1 
ATOM   5098 C  CG  . ASP B  1 326 ? -9.29300  -12.13000 20.06100 1.000 57.07000  ? 320 ASP B CG  1 
ATOM   5099 O  OD1 . ASP B  1 326 ? -9.41000  -11.94900 21.30000 1.000 55.79000  ? 320 ASP B OD1 1 
ATOM   5100 O  OD2 . ASP B  1 326 ? -9.68500  -13.16400 19.48100 1.000 65.71000  ? 320 ASP B OD2 1 
ATOM   5101 N  N   . VAL B  1 327 ? -7.23900  -8.30400  19.95300 1.000 48.95000  ? 321 VAL B N   1 
ATOM   5102 C  CA  . VAL B  1 327 ? -6.85400  -6.94200  19.58900 1.000 45.68000  ? 321 VAL B CA  1 
ATOM   5103 C  C   . VAL B  1 327 ? -5.36400  -6.74600  19.79700 1.000 41.56000  ? 321 VAL B C   1 
ATOM   5104 O  O   . VAL B  1 327 ? -4.64800  -6.26100  18.91300 1.000 40.53000  ? 321 VAL B O   1 
ATOM   5105 C  CB  . VAL B  1 327 ? -7.66700  -5.90900  20.39600 1.000 41.35000  ? 321 VAL B CB  1 
ATOM   5106 C  CG1 . VAL B  1 327 ? -6.89800  -4.56800  20.44200 1.000 34.75000  ? 321 VAL B CG1 1 
ATOM   5107 C  CG2 . VAL B  1 327 ? -9.06200  -5.74100  19.81400 1.000 45.32000  ? 321 VAL B CG2 1 
ATOM   5108 N  N   . ARG B  1 328 ? -4.87500  -7.11000  20.98000 1.000 44.60000  ? 322 ARG B N   1 
ATOM   5109 C  CA  . ARG B  1 328 ? -3.47000  -6.89800  21.29300 1.000 41.95000  ? 322 ARG B CA  1 
ATOM   5110 C  C   . ARG B  1 328 ? -2.54600  -7.82000  20.49800 1.000 40.97000  ? 322 ARG B C   1 
ATOM   5111 O  O   . ARG B  1 328 ? -1.35300  -7.51600  20.38800 1.000 39.40000  ? 322 ARG B O   1 
ATOM   5112 C  CB  . ARG B  1 328 ? -3.24800  -7.05600  22.80800 1.000 35.57000  ? 322 ARG B CB  1 
ATOM   5113 C  CG  . ARG B  1 328 ? -3.85200  -5.90100  23.66700 1.000 37.48000  ? 322 ARG B CG  1 
ATOM   5114 C  CD  . ARG B  1 328 ? -3.63000  -6.08600  25.18500 1.000 28.34000  ? 322 ARG B CD  1 
ATOM   5115 N  NE  . ARG B  1 328 ? -3.88900  -7.45700  25.62900 1.000 37.68000  ? 322 ARG B NE  1 
ATOM   5116 C  CZ  . ARG B  1 328 ? -4.94500  -7.84400  26.34200 1.000 39.10000  ? 322 ARG B CZ  1 
ATOM   5117 N  NH1 . ARG B  1 328 ? -5.82200  -6.97000  26.82200 1.000 32.60000  ? 322 ARG B NH1 1 
ATOM   5118 N  NH2 . ARG B  1 328 ? -5.12100  -9.14100  26.58700 1.000 35.55000  ? 322 ARG B NH2 1 
ATOM   5119 N  N   . SER B  1 329 ? -3.05500  -8.92200  19.92900 1.000 41.43000  ? 323 SER B N   1 
ATOM   5120 C  CA  . SER B  1 329 ? -2.18300  -9.82700  19.17700 1.000 40.25000  ? 323 SER B CA  1 
ATOM   5121 C  C   . SER B  1 329 ? -1.71400  -9.25100  17.83600 1.000 40.08000  ? 323 SER B C   1 
ATOM   5122 O  O   . SER B  1 329 ? -0.75500  -9.76800  17.24400 1.000 35.72000  ? 323 SER B O   1 
ATOM   5123 C  CB  . SER B  1 329 ? -2.87900  -11.14700 18.92000 1.000 38.66000  ? 323 SER B CB  1 
ATOM   5124 O  OG  . SER B  1 329 ? -3.70800  -11.04600 17.77700 1.000 48.30000  ? 323 SER B OG  1 
ATOM   5125 N  N   . GLN B  1 330 ? -2.37400  -8.21400  17.32400 1.000 33.97000  ? 324 GLN B N   1 
ATOM   5126 C  CA  . GLN B  1 330 ? -1.81800  -7.46100  16.20700 1.000 33.34000  ? 324 GLN B CA  1 
ATOM   5127 C  C   . GLN B  1 330 ? -0.49100  -6.80500  16.58400 1.000 29.14000  ? 324 GLN B C   1 
ATOM   5128 O  O   . GLN B  1 330 ? 0.28600   -6.43200  15.70100 1.000 30.00000  ? 324 GLN B O   1 
ATOM   5129 C  CB  . GLN B  1 330 ? -2.85500  -6.42200  15.75100 1.000 36.97000  ? 324 GLN B CB  1 
ATOM   5130 C  CG  . GLN B  1 330 ? -4.28700  -7.00500  15.76300 1.000 33.89000  ? 324 GLN B CG  1 
ATOM   5131 C  CD  . GLN B  1 330 ? -5.33900  -6.05100  15.20500 1.000 43.00000  ? 324 GLN B CD  1 
ATOM   5132 O  OE1 . GLN B  1 330 ? -5.00900  -5.04300  14.57500 1.000 40.56000  ? 324 GLN B OE1 1 
ATOM   5133 N  NE2 . GLN B  1 330 ? -6.62000  -6.37200  15.42500 1.000 42.46000  ? 324 GLN B NE2 1 
ATOM   5134 N  N   . LEU B  1 331 ? -0.20700  -6.68700  17.87500 1.000 24.92000  ? 325 LEU B N   1 
ATOM   5135 C  CA  . LEU B  1 331 ? 1.01900   -6.08400  18.37200 1.000 26.01000  ? 325 LEU B CA  1 
ATOM   5136 C  C   . LEU B  1 331 ? 2.02900   -7.11400  18.84100 1.000 24.80000  ? 325 LEU B C   1 
ATOM   5137 O  O   . LEU B  1 331 ? 2.98200   -6.73400  19.53200 1.000 19.35000  ? 325 LEU B O   1 
ATOM   5138 C  CB  . LEU B  1 331 ? 0.71200   -5.14400  19.52800 1.000 23.89000  ? 325 LEU B CB  1 
ATOM   5139 C  CG  . LEU B  1 331 ? -0.30500  -4.06900  19.19700 1.000 23.58000  ? 325 LEU B CG  1 
ATOM   5140 C  CD1 . LEU B  1 331 ? -0.49100  -3.25300  20.43000 1.000 18.47000  ? 325 LEU B CD1 1 
ATOM   5141 C  CD2 . LEU B  1 331 ? 0.17200   -3.22600  18.04400 1.000 23.01000  ? 325 LEU B CD2 1 
ATOM   5142 N  N   . ALA B  1 332 ? 1.80900   -8.40300  18.51700 1.000 25.91000  ? 326 ALA B N   1 
ATOM   5143 C  CA  . ALA B  1 332 ? 2.62900   -9.47300  19.07900 1.000 26.44000  ? 326 ALA B CA  1 
ATOM   5144 C  C   . ALA B  1 332 ? 4.10600   -9.30200  18.72900 1.000 25.78000  ? 326 ALA B C   1 
ATOM   5145 O  O   . ALA B  1 332 ? 4.97700   -9.67700  19.51800 1.000 24.26000  ? 326 ALA B O   1 
ATOM   5146 C  CB  . ALA B  1 332 ? 2.11100   -10.84300 18.60600 1.000 27.34000  ? 326 ALA B CB  1 
ATOM   5147 N  N   . SER B  1 333 ? 4.40800   -8.80100  17.52900 1.000 23.96000  ? 327 SER B N   1 
ATOM   5148 C  CA  . SER B  1 333 ? 5.80700   -8.62800  17.14400 1.000 24.32000  ? 327 SER B CA  1 
ATOM   5149 C  C   . SER B  1 333 ? 6.49700   -7.58200  17.99700 1.000 25.08000  ? 327 SER B C   1 
ATOM   5150 O  O   . SER B  1 333 ? 7.72100   -7.61500  18.13700 1.000 22.29000  ? 327 SER B O   1 
ATOM   5151 C  CB  . SER B  1 333 ? 5.92800   -8.22000  15.67800 1.000 26.26000  ? 327 SER B CB  1 
ATOM   5152 O  OG  . SER B  1 333 ? 5.43000   -6.90100  15.51100 1.000 28.81000  ? 327 SER B OG  1 
ATOM   5153 N  N   . PHE B  1 334 ? 5.74200   -6.60500  18.51900 1.000 19.29000  ? 328 PHE B N   1 
ATOM   5154 C  CA  . PHE B  1 334 ? 6.31600   -5.62400  19.43800 1.000 19.73000  ? 328 PHE B CA  1 
ATOM   5155 C  C   . PHE B  1 334 ? 6.40400   -6.15800  20.85900 1.000 19.66000  ? 328 PHE B C   1 
ATOM   5156 O  O   . PHE B  1 334 ? 7.36100   -5.86200  21.58300 1.000 18.77000  ? 328 PHE B O   1 
ATOM   5157 C  CB  . PHE B  1 334 ? 5.46400   -4.34500  19.43700 1.000 20.22000  ? 328 PHE B CB  1 
ATOM   5158 C  CG  . PHE B  1 334 ? 5.46200   -3.61100  18.13200 1.000 18.34000  ? 328 PHE B CG  1 
ATOM   5159 C  CD1 . PHE B  1 334 ? 6.51400   -2.78000  17.78600 1.000 22.79000  ? 328 PHE B CD1 1 
ATOM   5160 C  CD2 . PHE B  1 334 ? 4.39800   -3.73900  17.25900 1.000 21.72000  ? 328 PHE B CD2 1 
ATOM   5161 C  CE1 . PHE B  1 334 ? 6.50700   -2.10000  16.57700 1.000 21.22000  ? 328 PHE B CE1 1 
ATOM   5162 C  CE2 . PHE B  1 334 ? 4.38500   -3.07300  16.06900 1.000 22.08000  ? 328 PHE B CE2 1 
ATOM   5163 C  CZ  . PHE B  1 334 ? 5.44200   -2.23500  15.73200 1.000 22.53000  ? 328 PHE B CZ  1 
ATOM   5164 N  N   . HIS B  1 335 ? 5.40100   -6.93600  21.26700 1.000 17.86000  ? 329 HIS B N   1 
ATOM   5165 C  CA  . HIS B  1 335 ? 5.29500   -7.42700  22.63600 1.000 18.54000  ? 329 HIS B CA  1 
ATOM   5166 C  C   . HIS B  1 335 ? 6.47400   -8.33100  23.01500 1.000 19.07000  ? 329 HIS B C   1 
ATOM   5167 O  O   . HIS B  1 335 ? 7.06500   -8.18100  24.09700 1.000 17.91000  ? 329 HIS B O   1 
ATOM   5168 C  CB  . HIS B  1 335 ? 3.98000   -8.19800  22.77900 1.000 23.09000  ? 329 HIS B CB  1 
ATOM   5169 C  CG  . HIS B  1 335 ? 3.62600   -8.52400  24.18900 1.000 21.94000  ? 329 HIS B CG  1 
ATOM   5170 N  ND1 . HIS B  1 335 ? 2.52900   -9.28300  24.52000 1.000 24.65000  ? 329 HIS B ND1 1 
ATOM   5171 C  CD2 . HIS B  1 335 ? 4.20900   -8.16800  25.35800 1.000 20.61000  ? 329 HIS B CD2 1 
ATOM   5172 C  CE1 . HIS B  1 335 ? 2.46900   -9.41100  25.83500 1.000 27.07000  ? 329 HIS B CE1 1 
ATOM   5173 N  NE2 . HIS B  1 335 ? 3.48900   -8.76000  26.36400 1.000 17.18000  ? 329 HIS B NE2 1 
ATOM   5174 N  N   . HIS B  1 336 ? 6.83800   -9.25700  22.13100 1.000 19.83000  ? 330 HIS B N   1 
ATOM   5175 C  CA  . HIS B  1 336 ? 7.95400   -10.17700 22.34300 1.000 21.42000  ? 330 HIS B CA  1 
ATOM   5176 C  C   . HIS B  1 336 ? 8.87200   -10.08200 21.12700 1.000 23.28000  ? 330 HIS B C   1 
ATOM   5177 O  O   . HIS B  1 336 ? 8.71000   -10.81700 20.14500 1.000 20.89000  ? 330 HIS B O   1 
ATOM   5178 C  CB  . HIS B  1 336 ? 7.44900   -11.60100 22.61400 1.000 22.18000  ? 330 HIS B CB  1 
ATOM   5179 C  CG  . HIS B  1 336 ? 6.44000   -11.65900 23.72200 1.000 22.26000  ? 330 HIS B CG  1 
ATOM   5180 N  ND1 . HIS B  1 336 ? 5.08200   -11.68600 23.48900 1.000 28.17000  ? 330 HIS B ND1 1 
ATOM   5181 C  CD2 . HIS B  1 336 ? 6.59000   -11.61600 25.06800 1.000 20.67000  ? 330 HIS B CD2 1 
ATOM   5182 C  CE1 . HIS B  1 336 ? 4.43800   -11.69300 24.64700 1.000 26.56000  ? 330 HIS B CE1 1 
ATOM   5183 N  NE2 . HIS B  1 336 ? 5.33300   -11.63400 25.61900 1.000 25.86000  ? 330 HIS B NE2 1 
ATOM   5184 N  N   . PRO B  1 337 ? 9.82300   -9.14200  21.15200 1.000 25.18000  ? 331 PRO B N   1 
ATOM   5185 C  CA  . PRO B  1 337 ? 10.68800  -8.89000  19.98800 1.000 26.39000  ? 331 PRO B CA  1 
ATOM   5186 C  C   . PRO B  1 337 ? 11.44500  -10.13900 19.55400 1.000 22.72000  ? 331 PRO B C   1 
ATOM   5187 O  O   . PRO B  1 337 ? 11.91900  -10.91200 20.38300 1.000 25.01000  ? 331 PRO B O   1 
ATOM   5188 C  CB  . PRO B  1 337 ? 11.66300  -7.83000  20.50900 1.000 23.12000  ? 331 PRO B CB  1 
ATOM   5189 C  CG  . PRO B  1 337 ? 10.89400  -7.09100  21.56000 1.000 24.22000  ? 331 PRO B CG  1 
ATOM   5190 C  CD  . PRO B  1 337 ? 9.97000   -8.11900  22.19800 1.000 17.92000  ? 331 PRO B CD  1 
ATOM   5191 N  N   . GLN B  1 338 ? 11.55900  -10.31300 18.24000 1.000 25.93000  ? 332 GLN B N   1 
ATOM   5192 C  CA  . GLN B  1 338 ? 12.29500  -11.43500 17.68800 1.000 25.34000  ? 332 GLN B CA  1 
ATOM   5193 C  C   . GLN B  1 338 ? 13.74500  -11.34900 18.13000 1.000 25.36000  ? 332 GLN B C   1 
ATOM   5194 O  O   . GLN B  1 338 ? 14.32700  -10.26300 18.17000 1.000 23.22000  ? 332 GLN B O   1 
ATOM   5195 C  CB  . GLN B  1 338 ? 12.22600  -11.41700 16.16400 1.000 27.84000  ? 332 GLN B CB  1 
ATOM   5196 C  CG  . GLN B  1 338 ? 10.83700  -11.61800 15.58800 1.000 38.39000  ? 332 GLN B CG  1 
ATOM   5197 C  CD  . GLN B  1 338 ? 10.34600  -13.04500 15.74200 1.000 41.97000  ? 332 GLN B CD  1 
ATOM   5198 O  OE1 . GLN B  1 338 ? 9.40000   -13.30300 16.48800 1.000 47.20000  ? 332 GLN B OE1 1 
ATOM   5199 N  NE2 . GLN B  1 338 ? 10.99200  -13.98200 15.04100 1.000 34.74000  ? 332 GLN B NE2 1 
ATOM   5200 N  N   . ARG B  1 339 ? 14.29500  -12.48400 18.50200 1.000 21.34000  ? 333 ARG B N   1 
ATOM   5201 C  CA  . ARG B  1 339 ? 15.72600  -12.64100 18.79700 1.000 23.66000  ? 333 ARG B CA  1 
ATOM   5202 C  C   . ARG B  1 339 ? 16.28900  -13.79000 17.95300 1.000 26.63000  ? 333 ARG B C   1 
ATOM   5203 O  O   . ARG B  1 339 ? 16.63700  -14.85500 18.47800 1.000 23.11000  ? 333 ARG B O   1 
ATOM   5204 C  CB  . ARG B  1 339 ? 15.93500  -12.88800 20.28600 1.000 25.65000  ? 333 ARG B CB  1 
ATOM   5205 C  CG  . ARG B  1 339 ? 15.80300  -11.63600 21.12300 1.000 21.80000  ? 333 ARG B CG  1 
ATOM   5206 C  CD  . ARG B  1 339 ? 16.82500  -10.62400 20.70000 1.000 22.69000  ? 333 ARG B CD  1 
ATOM   5207 N  NE  . ARG B  1 339 ? 16.76600  -9.40900  21.51300 1.000 25.39000  ? 333 ARG B NE  1 
ATOM   5208 C  CZ  . ARG B  1 339 ? 16.07600  -8.31600  21.21300 1.000 25.49000  ? 333 ARG B CZ  1 
ATOM   5209 N  NH1 . ARG B  1 339 ? 15.35800  -8.23100  20.10800 1.000 24.47000  ? 333 ARG B NH1 1 
ATOM   5210 N  NH2 . ARG B  1 339 ? 16.14600  -7.26200  22.02200 1.000 24.25000  ? 333 ARG B NH2 1 
ATOM   5211 N  N   . VAL B  1 340 ? 16.37400  -13.57800 16.63800 1.000 24.41000  ? 334 VAL B N   1 
ATOM   5212 C  CA  . VAL B  1 340 ? 16.78400  -14.62000 15.68500 1.000 22.45000  ? 334 VAL B CA  1 
ATOM   5213 C  C   . VAL B  1 340 ? 18.13600  -14.22700 15.09400 1.000 24.90000  ? 334 VAL B C   1 
ATOM   5214 O  O   . VAL B  1 340 ? 18.30600  -13.09300 14.61800 1.000 23.29000  ? 334 VAL B O   1 
ATOM   5215 C  CB  . VAL B  1 340 ? 15.72900  -14.78600 14.57900 1.000 25.62000  ? 334 VAL B CB  1 
ATOM   5216 C  CG1 . VAL B  1 340 ? 16.17400  -15.78200 13.57100 1.000 24.19000  ? 334 VAL B CG1 1 
ATOM   5217 C  CG2 . VAL B  1 340 ? 14.33600  -15.19000 15.16600 1.000 30.38000  ? 334 VAL B CG2 1 
ATOM   5218 N  N   . ASN B  1 341 ? 19.10400  -15.15100 15.13000 1.000 24.69000  ? 335 ASN B N   1 
ATOM   5219 C  CA  . ASN B  1 341 ? 20.46700  -14.82000 14.72900 1.000 19.97000  ? 335 ASN B CA  1 
ATOM   5220 C  C   . ASN B  1 341 ? 20.58600  -14.92600 13.21200 1.000 20.90000  ? 335 ASN B C   1 
ATOM   5221 O  O   . ASN B  1 341 ? 19.60000  -15.10300 12.49800 1.000 18.71000  ? 335 ASN B O   1 
ATOM   5222 C  CB  . ASN B  1 341 ? 21.47300  -15.68100 15.49600 1.000 18.49000  ? 335 ASN B CB  1 
ATOM   5223 C  CG  . ASN B  1 341 ? 21.48800  -17.18700 15.08800 1.000 20.32000  ? 335 ASN B CG  1 
ATOM   5224 O  OD1 . ASN B  1 341 ? 20.88400  -17.63100 14.10500 1.000 22.43000  ? 335 ASN B OD1 1 
ATOM   5225 N  ND2 . ASN B  1 341 ? 22.20900  -17.96100 15.86800 1.000 21.06000  ? 335 ASN B ND2 1 
ATOM   5226 N  N   . THR B  1 342 ? 21.79900  -14.82800 12.69000 1.000 21.01000  ? 336 THR B N   1 
ATOM   5227 C  CA  . THR B  1 342 ? 21.97800  -14.77800 11.24800 1.000 21.05000  ? 336 THR B CA  1 
ATOM   5228 C  C   . THR B  1 342 ? 21.75900  -16.13100 10.58100 1.000 23.19000  ? 336 THR B C   1 
ATOM   5229 O  O   . THR B  1 342 ? 21.73000  -16.19800 9.34900  1.000 24.36000  ? 336 THR B O   1 
ATOM   5230 C  CB  . THR B  1 342 ? 23.38000  -14.27000 10.91800 1.000 20.86000  ? 336 THR B CB  1 
ATOM   5231 O  OG1 . THR B  1 342 ? 24.33200  -15.19600 11.45300 1.000 20.56000  ? 336 THR B OG1 1 
ATOM   5232 C  CG2 . THR B  1 342 ? 23.64300  -12.84400 11.50900 1.000 22.49000  ? 336 THR B CG2 1 
ATOM   5233 N  N   . MET B  1 343 ? 21.60000  -17.20800 11.35000 1.000 19.42000  ? 337 MET B N   1 
ATOM   5234 C  CA  . MET B  1 343 ? 21.33700  -18.51500 10.77900 1.000 24.32000  ? 337 MET B CA  1 
ATOM   5235 C  C   . MET B  1 343 ? 19.93900  -19.00900 11.12500 1.000 26.17000  ? 337 MET B C   1 
ATOM   5236 O  O   . MET B  1 343 ? 19.67100  -20.20900 11.01200 1.000 22.59000  ? 337 MET B O   1 
ATOM   5237 C  CB  . MET B  1 343 ? 22.39300  -19.53400 11.22700 1.000 22.95000  ? 337 MET B CB  1 
ATOM   5238 C  CG  . MET B  1 343 ? 23.82600  -19.21800 10.75900 1.000 22.09000  ? 337 MET B CG  1 
ATOM   5239 S  SD  . MET B  1 343 ? 23.92400  -19.11500 8.95100  1.000 27.45000  ? 337 MET B SD  1 
ATOM   5240 C  CE  . MET B  1 343 ? 23.87600  -20.87200 8.53800  1.000 26.99000  ? 337 MET B CE  1 
ATOM   5241 N  N   . GLY B  1 344 ? 19.05700  -18.10700 11.55200 1.000 23.83000  ? 338 GLY B N   1 
ATOM   5242 C  CA  . GLY B  1 344 ? 17.64700  -18.41800 11.75400 1.000 26.73000  ? 338 GLY B CA  1 
ATOM   5243 C  C   . GLY B  1 344 ? 17.32200  -19.03500 13.09200 1.000 25.91000  ? 338 GLY B C   1 
ATOM   5244 O  O   . GLY B  1 344 ? 16.19100  -19.50600 13.29400 1.000 26.19000  ? 338 GLY B O   1 
ATOM   5245 N  N   . VAL B  1 345 ? 18.27800  -19.04400 14.00800 1.000 22.08000  ? 339 VAL B N   1 
ATOM   5246 C  CA  . VAL B  1 345 ? 18.14300  -19.67100 15.31500 1.000 26.77000  ? 339 VAL B CA  1 
ATOM   5247 C  C   . VAL B  1 345 ? 17.76500  -18.61200 16.34100 1.000 24.49000  ? 339 VAL B C   1 
ATOM   5248 O  O   . VAL B  1 345 ? 18.42000  -17.56100 16.44000 1.000 21.02000  ? 339 VAL B O   1 
ATOM   5249 C  CB  . VAL B  1 345 ? 19.44900  -20.37800 15.72400 1.000 23.78000  ? 339 VAL B CB  1 
ATOM   5250 C  CG1 . VAL B  1 345 ? 19.30300  -21.03900 17.08300 1.000 26.04000  ? 339 VAL B CG1 1 
ATOM   5251 C  CG2 . VAL B  1 345 ? 19.84600  -21.39400 14.67600 1.000 26.71000  ? 339 VAL B CG2 1 
ATOM   5252 N  N   . THR B  1 346 ? 16.73700  -18.90600 17.13200 1.000 23.94000  ? 340 THR B N   1 
ATOM   5253 C  CA  . THR B  1 346 ? 16.35800  -18.00000 18.21400 1.000 24.11000  ? 340 THR B CA  1 
ATOM   5254 C  C   . THR B  1 346 ? 17.34100  -18.13000 19.37200 1.000 22.08000  ? 340 THR B C   1 
ATOM   5255 O  O   . THR B  1 346 ? 17.59000  -19.23300 19.85400 1.000 23.70000  ? 340 THR B O   1 
ATOM   5256 C  CB  . THR B  1 346 ? 14.94800  -18.31100 18.67700 1.000 24.51000  ? 340 THR B CB  1 
ATOM   5257 O  OG1 . THR B  1 346 ? 14.05800  -18.01800 17.59300 1.000 27.47000  ? 340 THR B OG1 1 
ATOM   5258 C  CG2 . THR B  1 346 ? 14.59600  -17.44300 19.89400 1.000 22.97000  ? 340 THR B CG2 1 
ATOM   5259 N  N   . THR B  1 347 ? 17.90300  -17.00600 19.81100 1.000 20.69000  ? 341 THR B N   1 
ATOM   5260 C  CA  . THR B  1 347 ? 18.96300  -17.02700 20.80900 1.000 19.51000  ? 341 THR B CA  1 
ATOM   5261 C  C   . THR B  1 347 ? 18.51900  -16.58500 22.19400 1.000 19.77000  ? 341 THR B C   1 
ATOM   5262 O  O   . THR B  1 347 ? 19.29900  -16.71900 23.14400 1.000 21.14000  ? 341 THR B O   1 
ATOM   5263 C  CB  . THR B  1 347 ? 20.12800  -16.14400 20.36600 1.000 22.38000  ? 341 THR B CB  1 
ATOM   5264 O  OG1 . THR B  1 347 ? 19.64200  -14.82600 20.09500 1.000 22.58000  ? 341 THR B OG1 1 
ATOM   5265 C  CG2 . THR B  1 347 ? 20.78200  -16.74500 19.11400 1.000 24.97000  ? 341 THR B CG2 1 
ATOM   5266 N  N   . GLY B  1 348 ? 17.30900  -16.04600 22.33600 1.000 23.18000  ? 342 GLY B N   1 
ATOM   5267 C  CA  . GLY B  1 348 ? 16.90500  -15.48500 23.61000 1.000 20.43000  ? 342 GLY B CA  1 
ATOM   5268 C  C   . GLY B  1 348 ? 15.58900  -14.75200 23.45400 1.000 20.26000  ? 342 GLY B C   1 
ATOM   5269 O  O   . GLY B  1 348 ? 14.85700  -14.95700 22.48300 1.000 20.95000  ? 342 GLY B O   1 
ATOM   5270 N  N   . GLY B  1 349 ? 15.30300  -13.89500 24.41800 1.000 21.48000  ? 343 GLY B N   1 
ATOM   5271 C  CA  . GLY B  1 349 ? 14.03300  -13.20700 24.36400 1.000 23.36000  ? 343 GLY B CA  1 
ATOM   5272 C  C   . GLY B  1 349 ? 13.97100  -12.09400 25.37700 1.000 20.77000  ? 343 GLY B C   1 
ATOM   5273 O  O   . GLY B  1 349 ? 14.97600  -11.71900 25.98000 1.000 20.22000  ? 343 GLY B O   1 
ATOM   5274 N  N   . VAL B  1 350 ? 12.75600  -11.58500 25.55600 1.000 21.17000  ? 344 VAL B N   1 
ATOM   5275 C  CA  A VAL B  1 350 ? 12.46500  -10.44100 26.41800 0.500 20.00000  ? 344 VAL B CA  1 
ATOM   5276 C  CA  B VAL B  1 350 ? 12.48600  -10.44800 26.42800 0.500 20.00000  ? 344 VAL B CA  1 
ATOM   5277 C  C   . VAL B  1 350 ? 11.61700  -10.91500 27.58800 1.000 20.20000  ? 344 VAL B C   1 
ATOM   5278 O  O   . VAL B  1 350 ? 10.71200  -11.73600 27.41100 1.000 23.62000  ? 344 VAL B O   1 
ATOM   5279 C  CB  A VAL B  1 350 ? 11.74000  -9.31700  25.64800 0.500 19.88000  ? 344 VAL B CB  1 
ATOM   5280 C  CB  B VAL B  1 350 ? 11.81600  -9.30500  25.64300 0.500 19.87000  ? 344 VAL B CB  1 
ATOM   5281 C  CG1 A VAL B  1 350 ? 10.28400  -9.70200  25.29900 0.500 21.50000  ? 344 VAL B CG1 1 
ATOM   5282 C  CG1 B VAL B  1 350 ? 11.33100  -8.22200  26.58200 0.500 16.28000  ? 344 VAL B CG1 1 
ATOM   5283 C  CG2 A VAL B  1 350 ? 11.75200  -8.05800  26.45400 0.500 16.58000  ? 344 VAL B CG2 1 
ATOM   5284 C  CG2 B VAL B  1 350 ? 12.79300  -8.73400  24.60100 0.500 19.68000  ? 344 VAL B CG2 1 
ATOM   5285 N  N   . SER B  1 351 ? 11.91500  -10.41800 28.78900 1.000 18.17000  ? 345 SER B N   1 
ATOM   5286 C  CA  A SER B  1 351 ? 11.07800  -10.68800 29.94900 0.500 18.20000  ? 345 SER B CA  1 
ATOM   5287 C  CA  B SER B  1 351 ? 11.14600  -10.69900 29.99800 0.500 18.22000  ? 345 SER B CA  1 
ATOM   5288 C  C   . SER B  1 351 ? 10.79000  -9.38500  30.68300 1.000 18.72000  ? 345 SER B C   1 
ATOM   5289 O  O   . SER B  1 351 ? 11.45800  -8.37300  30.48800 1.000 14.87000  ? 345 SER B O   1 
ATOM   5290 C  CB  A SER B  1 351 ? 11.72500  -11.68800 30.90600 0.500 20.50000  ? 345 SER B CB  1 
ATOM   5291 C  CB  B SER B  1 351 ? 11.92600  -11.57100 30.99100 0.500 20.37000  ? 345 SER B CB  1 
ATOM   5292 O  OG  A SER B  1 351 ? 13.01800  -11.25400 31.25000 0.500 20.30000  ? 345 SER B OG  1 
ATOM   5293 O  OG  B SER B  1 351 ? 12.31200  -12.79400 30.40200 0.500 19.41000  ? 345 SER B OG  1 
ATOM   5294 N  N   . PHE B  1 352 ? 9.77700   -9.44600  31.54500 1.000 16.85000  ? 346 PHE B N   1 
ATOM   5295 C  CA  . PHE B  1 352 ? 9.19200   -8.28000  32.18600 1.000 17.82000  ? 346 PHE B CA  1 
ATOM   5296 C  C   . PHE B  1 352 ? 9.16400   -8.42500  33.70300 1.000 19.09000  ? 346 PHE B C   1 
ATOM   5297 O  O   . PHE B  1 352 ? 8.08200   -8.46100  34.30700 1.000 19.02000  ? 346 PHE B O   1 
ATOM   5298 C  CB  . PHE B  1 352 ? 7.77400   -8.08300  31.63600 1.000 16.22000  ? 346 PHE B CB  1 
ATOM   5299 C  CG  . PHE B  1 352 ? 7.73700   -7.88500  30.14900 1.000 16.66000  ? 346 PHE B CG  1 
ATOM   5300 C  CD1 . PHE B  1 352 ? 8.19400   -6.68400  29.57700 1.000 16.99000  ? 346 PHE B CD1 1 
ATOM   5301 C  CD2 . PHE B  1 352 ? 7.24000   -8.89100  29.31500 1.000 17.35000  ? 346 PHE B CD2 1 
ATOM   5302 C  CE1 . PHE B  1 352 ? 8.15600   -6.50900  28.20400 1.000 18.04000  ? 346 PHE B CE1 1 
ATOM   5303 C  CE2 . PHE B  1 352 ? 7.19500   -8.72100  27.94200 1.000 16.71000  ? 346 PHE B CE2 1 
ATOM   5304 C  CZ  . PHE B  1 352 ? 7.67100   -7.54900  27.38100 1.000 16.15000  ? 346 PHE B CZ  1 
ATOM   5305 N  N   . PRO B  1 353 ? 10.34300  -8.47500  34.36500 1.000 17.39000  ? 347 PRO B N   1 
ATOM   5306 C  CA  . PRO B  1 353 ? 10.36900  -8.41900  35.84800 1.000 18.94000  ? 347 PRO B CA  1 
ATOM   5307 C  C   . PRO B  1 353 ? 10.12300  -7.00500  36.37800 1.000 17.07000  ? 347 PRO B C   1 
ATOM   5308 O  O   . PRO B  1 353 ? 10.98900  -6.29500  36.94300 1.000 16.80000  ? 347 PRO B O   1 
ATOM   5309 C  CB  . PRO B  1 353 ? 11.77300  -8.94700  36.17500 1.000 17.79000  ? 347 PRO B CB  1 
ATOM   5310 C  CG  . PRO B  1 353 ? 12.60200  -8.53700  34.99600 1.000 23.24000  ? 347 PRO B CG  1 
ATOM   5311 C  CD  . PRO B  1 353 ? 11.70000  -8.52300  33.78600 1.000 16.89000  ? 347 PRO B CD  1 
ATOM   5312 N  N   . PHE B  1 354 ? 8.89400   -6.57000  36.20900 1.000 18.61000  ? 348 PHE B N   1 
ATOM   5313 C  CA  . PHE B  1 354 ? 8.39400   -5.41600  36.91300 1.000 19.42000  ? 348 PHE B CA  1 
ATOM   5314 C  C   . PHE B  1 354 ? 7.04900   -5.79400  37.52000 1.000 18.29000  ? 348 PHE B C   1 
ATOM   5315 O  O   . PHE B  1 354 ? 6.42500   -6.79600  37.15300 1.000 20.77000  ? 348 PHE B O   1 
ATOM   5316 C  CB  . PHE B  1 354 ? 8.28000   -4.18300  36.00200 1.000 19.85000  ? 348 PHE B CB  1 
ATOM   5317 C  CG  . PHE B  1 354 ? 7.39400   -4.34900  34.76000 1.000 18.94000  ? 348 PHE B CG  1 
ATOM   5318 C  CD1 . PHE B  1 354 ? 6.00800   -4.36400  34.84400 1.000 17.64000  ? 348 PHE B CD1 1 
ATOM   5319 C  CD2 . PHE B  1 354 ? 7.97300   -4.34000  33.48600 1.000 20.74000  ? 348 PHE B CD2 1 
ATOM   5320 C  CE1 . PHE B  1 354 ? 5.22900   -4.45400  33.69600 1.000 18.11000  ? 348 PHE B CE1 1 
ATOM   5321 C  CE2 . PHE B  1 354 ? 7.19500   -4.42000  32.34500 1.000 15.97000  ? 348 PHE B CE2 1 
ATOM   5322 C  CZ  . PHE B  1 354 ? 5.83100   -4.48300  32.43900 1.000 16.38000  ? 348 PHE B CZ  1 
ATOM   5323 N  N   . LYS B  1 355 ? 6.60500   -4.98200  38.46300 1.000 15.99000  ? 349 LYS B N   1 
ATOM   5324 C  CA  . LYS B  1 355 ? 5.45000   -5.35200  39.26500 1.000 19.25000  ? 349 LYS B CA  1 
ATOM   5325 C  C   . LYS B  1 355 ? 4.59600   -4.10400  39.42100 1.000 17.97000  ? 349 LYS B C   1 
ATOM   5326 O  O   . LYS B  1 355 ? 4.99200   -3.10500  40.03300 1.000 16.68000  ? 349 LYS B O   1 
ATOM   5327 C  CB  . LYS B  1 355 ? 5.88800   -5.95400  40.59900 1.000 20.30000  ? 349 LYS B CB  1 
ATOM   5328 C  CG  . LYS B  1 355 ? 4.79900   -6.11200  41.61800 1.000 24.68000  ? 349 LYS B CG  1 
ATOM   5329 C  CD  . LYS B  1 355 ? 5.21400   -7.17300  42.63000 1.000 26.68000  ? 349 LYS B CD  1 
ATOM   5330 C  CE  . LYS B  1 355 ? 4.11100   -7.43500  43.62700 1.000 32.34000  ? 349 LYS B CE  1 
ATOM   5331 N  NZ  . LYS B  1 355 ? 4.61400   -8.13500  44.83500 1.000 32.55000  ? 349 LYS B NZ  1 
ATOM   5332 N  N   . LEU B  1 356 ? 3.42300   -4.15200  38.82800 1.000 22.16000  ? 350 LEU B N   1 
ATOM   5333 C  CA  . LEU B  1 356 ? 2.52600   -3.02700  38.91300 1.000 19.45000  ? 350 LEU B CA  1 
ATOM   5334 C  C   . LEU B  1 356 ? 2.13800   -2.79700  40.36700 1.000 24.13000  ? 350 LEU B C   1 
ATOM   5335 O  O   . LEU B  1 356 ? 1.87300   -3.74400  41.10700 1.000 23.57000  ? 350 LEU B O   1 
ATOM   5336 C  CB  . LEU B  1 356 ? 1.30300   -3.32600  38.06300 1.000 19.86000  ? 350 LEU B CB  1 
ATOM   5337 C  CG  . LEU B  1 356 ? 0.45900   -2.17500  37.56700 1.000 28.66000  ? 350 LEU B CG  1 
ATOM   5338 C  CD1 . LEU B  1 356 ? 1.29000   -1.30000  36.64900 1.000 20.03000  ? 350 LEU B CD1 1 
ATOM   5339 C  CD2 . LEU B  1 356 ? -0.73500  -2.80400  36.84200 1.000 29.13000  ? 350 LEU B CD2 1 
ATOM   5340 N  N   . ARG B  1 357 ? 2.11800   -1.54700  40.79900 1.000 18.52000  ? 351 ARG B N   1 
ATOM   5341 C  CA  . ARG B  1 357 ? 1.62000   -1.27500  42.14400 1.000 21.53000  ? 351 ARG B CA  1 
ATOM   5342 C  C   . ARG B  1 357 ? 0.43900   -0.31600  42.07600 1.000 27.81000  ? 351 ARG B C   1 
ATOM   5343 O  O   . ARG B  1 357 ? 0.40600   0.58200   41.23300 1.000 21.00000  ? 351 ARG B O   1 
ATOM   5344 C  CB  . ARG B  1 357 ? 2.70800   -0.74600  43.05000 1.000 24.44000  ? 351 ARG B CB  1 
ATOM   5345 C  CG  . ARG B  1 357 ? 3.39900   0.50300   42.58500 1.000 22.03000  ? 351 ARG B CG  1 
ATOM   5346 C  CD  . ARG B  1 357 ? 4.58800   0.80100   43.46800 1.000 24.43000  ? 351 ARG B CD  1 
ATOM   5347 N  NE  . ARG B  1 357 ? 5.03400   2.18700   43.34800 1.000 19.76000  ? 351 ARG B NE  1 
ATOM   5348 C  CZ  . ARG B  1 357 ? 5.87100   2.62700   42.41200 1.000 21.99000  ? 351 ARG B CZ  1 
ATOM   5349 N  NH1 . ARG B  1 357 ? 6.31000   1.83400   41.45000 1.000 21.70000  ? 351 ARG B NH1 1 
ATOM   5350 N  NH2 . ARG B  1 357 ? 6.29500   3.88900   42.46200 1.000 19.44000  ? 351 ARG B NH2 1 
ATOM   5351 N  N   . GLY B  1 358 ? -0.54600  -0.54600  42.94400 1.000 27.45000  ? 352 GLY B N   1 
ATOM   5352 C  CA  . GLY B  1 358 ? -1.76400  0.25400   42.96900 1.000 33.88000  ? 352 GLY B CA  1 
ATOM   5353 C  C   . GLY B  1 358 ? -2.94400  -0.45900  43.60900 1.000 54.39000  ? 352 GLY B C   1 
ATOM   5354 O  O   . GLY B  1 358 ? -3.51700  0.05500   44.57800 1.000 68.96000  ? 352 GLY B O   1 
ATOM   5355 N  N   . SER B  1 359 ? -3.33700  -1.61300  43.04900 1.000 59.08000  ? 353 SER B N   1 
ATOM   5356 C  CA  . SER B  1 359 ? -4.26700  -2.59300  43.66300 1.000 60.85000  ? 353 SER B CA  1 
ATOM   5357 C  C   . SER B  1 359 ? -4.56400  -3.73800  42.69200 1.000 62.38000  ? 353 SER B C   1 
ATOM   5358 O  O   . SER B  1 359 ? -4.16700  -4.88600  42.91200 1.000 64.48000  ? 353 SER B O   1 
ATOM   5359 C  CB  . SER B  1 359 ? -5.59200  -1.96500  44.09600 1.000 64.32000  ? 353 SER B CB  1 
ATOM   5360 O  OG  . SER B  1 359 ? -6.42200  -2.94200  44.71600 1.000 65.30000  ? 353 SER B OG  1 
ATOM   5361 N  N   . VAL B  1 363 ? -2.29800  -4.46500  49.24000 1.000 58.44000  ? 357 VAL B N   1 
ATOM   5362 C  CA  . VAL B  1 363 ? -2.03100  -5.86800  48.93200 1.000 55.81000  ? 357 VAL B CA  1 
ATOM   5363 C  C   . VAL B  1 363 ? -0.76800  -6.37700  49.68300 1.000 53.09000  ? 357 VAL B C   1 
ATOM   5364 O  O   . VAL B  1 363 ? -0.72300  -7.53100  50.11400 1.000 46.79000  ? 357 VAL B O   1 
ATOM   5365 C  CB  . VAL B  1 363 ? -1.93400  -6.07400  47.38600 1.000 53.43000  ? 357 VAL B CB  1 
ATOM   5366 C  CG1 . VAL B  1 363 ? -3.09200  -5.37100  46.69200 1.000 59.52000  ? 357 VAL B CG1 1 
ATOM   5367 C  CG2 . VAL B  1 363 ? -0.63100  -5.54300  46.83100 1.000 53.16000  ? 357 VAL B CG2 1 
ATOM   5368 N  N   . ASP B  1 364 ? 0.22700   -5.50500  49.87700 1.000 48.79000  ? 358 ASP B N   1 
ATOM   5369 C  CA  . ASP B  1 364 ? 1.48500   -5.83200  50.54700 1.000 41.67000  ? 358 ASP B CA  1 
ATOM   5370 C  C   . ASP B  1 364 ? 1.45700   -5.41000  52.02300 1.000 39.99000  ? 358 ASP B C   1 
ATOM   5371 O  O   . ASP B  1 364 ? 0.57700   -4.66700  52.46900 1.000 37.51000  ? 358 ASP B O   1 
ATOM   5372 C  CB  . ASP B  1 364 ? 2.66400   -5.15000  49.84000 1.000 41.88000  ? 358 ASP B CB  1 
ATOM   5373 C  CG  . ASP B  1 364 ? 2.84000   -5.61100  48.40400 1.000 40.76000  ? 358 ASP B CG  1 
ATOM   5374 O  OD1 . ASP B  1 364 ? 2.90000   -6.83800  48.17200 1.000 46.97000  ? 358 ASP B OD1 1 
ATOM   5375 O  OD2 . ASP B  1 364 ? 2.92000   -4.74300  47.50900 1.000 45.72000  ? 358 ASP B OD2 1 
ATOM   5376 N  N   . ASP B  1 365 ? 2.44700   -5.89000  52.78100 1.000 29.77000  ? 359 ASP B N   1 
ATOM   5377 C  CA  . ASP B  1 365 ? 2.59400   -5.45900  54.16900 1.000 32.64000  ? 359 ASP B CA  1 
ATOM   5378 C  C   . ASP B  1 365 ? 2.67500   -3.93300  54.20700 1.000 28.91000  ? 359 ASP B C   1 
ATOM   5379 O  O   . ASP B  1 365 ? 3.40200   -3.34400  53.39300 1.000 28.36000  ? 359 ASP B O   1 
ATOM   5380 C  CB  . ASP B  1 365 ? 3.85800   -6.07000  54.79400 1.000 32.48000  ? 359 ASP B CB  1 
ATOM   5381 C  CG  . ASP B  1 365 ? 3.84200   -6.03300  56.31600 1.000 36.91000  ? 359 ASP B CG  1 
ATOM   5382 O  OD1 . ASP B  1 365 ? 3.85800   -4.92800  56.87500 1.000 34.23000  ? 359 ASP B OD1 1 
ATOM   5383 O  OD2 . ASP B  1 365 ? 3.81100   -7.11400  56.97700 1.000 38.14000  ? 359 ASP B OD2 1 
ATOM   5384 N  N   . PRO B  1 366 ? 1.95600   -3.25800  55.11400 1.000 29.48000  ? 360 PRO B N   1 
ATOM   5385 C  CA  . PRO B  1 366 ? 2.12100   -1.78900  55.21300 1.000 28.04000  ? 360 PRO B CA  1 
ATOM   5386 C  C   . PRO B  1 366 ? 3.56400   -1.37900  55.45900 1.000 27.99000  ? 360 PRO B C   1 
ATOM   5387 O  O   . PRO B  1 366 ? 3.91800   -0.22100  55.20600 1.000 26.84000  ? 360 PRO B O   1 
ATOM   5388 C  CB  . PRO B  1 366 ? 1.22200   -1.39800  56.39400 1.000 29.32000  ? 360 PRO B CB  1 
ATOM   5389 C  CG  . PRO B  1 366 ? 0.26300   -2.52900  56.55300 1.000 31.81000  ? 360 PRO B CG  1 
ATOM   5390 C  CD  . PRO B  1 366 ? 0.96900   -3.77300  56.07500 1.000 31.71000  ? 360 PRO B CD  1 
ATOM   5391 N  N   . ARG B  1 367 ? 4.41700   -2.30500  55.92300 1.000 29.65000  ? 361 ARG B N   1 
ATOM   5392 C  CA  . ARG B  1 367 ? 5.80700   -1.99200  56.23300 1.000 30.33000  ? 361 ARG B CA  1 
ATOM   5393 C  C   . ARG B  1 367 ? 6.72900   -2.09700  55.02900 1.000 30.58000  ? 361 ARG B C   1 
ATOM   5394 O  O   . ARG B  1 367 ? 7.94700   -1.93300  55.18400 1.000 30.02000  ? 361 ARG B O   1 
ATOM   5395 C  CB  . ARG B  1 367 ? 6.31300   -2.89400  57.36300 1.000 33.35000  ? 361 ARG B CB  1 
ATOM   5396 C  CG  . ARG B  1 367 ? 5.66500   -2.54000  58.69500 1.000 34.90000  ? 361 ARG B CG  1 
ATOM   5397 C  CD  . ARG B  1 367 ? 5.96600   -3.55800  59.75700 1.000 38.33000  ? 361 ARG B CD  1 
ATOM   5398 N  NE  . ARG B  1 367 ? 5.47300   -4.86600  59.34600 1.000 39.14000  ? 361 ARG B NE  1 
ATOM   5399 C  CZ  . ARG B  1 367 ? 5.52500   -5.95300  60.09600 1.000 42.48000  ? 361 ARG B CZ  1 
ATOM   5400 N  NH1 . ARG B  1 367 ? 6.03600   -5.92500  61.31700 1.000 45.36000  ? 361 ARG B NH1 1 
ATOM   5401 N  NH2 . ARG B  1 367 ? 5.08500   -7.10600  59.59600 1.000 43.32000  ? 361 ARG B NH2 1 
ATOM   5402 N  N   . LEU B  1 368 ? 6.19700   -2.38500  53.84500 1.000 27.36000  ? 362 LEU B N   1 
ATOM   5403 C  CA  . LEU B  1 368 ? 6.99300   -2.35400  52.62400 1.000 27.57000  ? 362 LEU B CA  1 
ATOM   5404 C  C   . LEU B  1 368 ? 6.91400   -0.94300  52.04600 1.000 26.26000  ? 362 LEU B C   1 
ATOM   5405 O  O   . LEU B  1 368 ? 5.84600   -0.50800  51.62000 1.000 25.78000  ? 362 LEU B O   1 
ATOM   5406 C  CB  . LEU B  1 368 ? 6.48600   -3.38800  51.61800 1.000 28.95000  ? 362 LEU B CB  1 
ATOM   5407 C  CG  . LEU B  1 368 ? 7.17500   -3.35800  50.24600 1.000 33.01000  ? 362 LEU B CG  1 
ATOM   5408 C  CD1 . LEU B  1 368 ? 8.65900   -3.81700  50.32700 1.000 25.50000  ? 362 LEU B CD1 1 
ATOM   5409 C  CD2 . LEU B  1 368 ? 6.36400   -4.19800  49.22500 1.000 34.34000  ? 362 LEU B CD2 1 
ATOM   5410 N  N   . ALA B  1 369 ? 8.03200   -0.22000  52.03700 1.000 26.50000  ? 363 ALA B N   1 
ATOM   5411 C  CA  . ALA B  1 369 ? 8.04100   1.11500   51.43800 1.000 25.48000  ? 363 ALA B CA  1 
ATOM   5412 C  C   . ALA B  1 369 ? 8.16300   1.02500   49.92000 1.000 23.13000  ? 363 ALA B C   1 
ATOM   5413 O  O   . ALA B  1 369 ? 8.92700   0.21100   49.38500 1.000 25.44000  ? 363 ALA B O   1 
ATOM   5414 C  CB  . ALA B  1 369 ? 9.19100   1.95000   52.00600 1.000 25.48000  ? 363 ALA B CB  1 
ATOM   5415 N  N   . ALA B  1 370 ? 7.39500   1.85300   49.22000 1.000 23.56000  ? 364 ALA B N   1 
ATOM   5416 C  CA  . ALA B  1 370 ? 7.44100   1.93000   47.76200 1.000 23.57000  ? 364 ALA B CA  1 
ATOM   5417 C  C   . ALA B  1 370 ? 8.10600   3.26000   47.40700 1.000 24.63000  ? 364 ALA B C   1 
ATOM   5418 O  O   . ALA B  1 370 ? 7.44900   4.26100   47.10000 1.000 24.72000  ? 364 ALA B O   1 
ATOM   5419 C  CB  . ALA B  1 370 ? 6.00800   1.79800   47.12200 1.000 24.79000  ? 364 ALA B CB  1 
ATOM   5420 N  N   . VAL B  1 371 ? 9.43400   3.25600   47.44000 1.000 23.09000  ? 365 VAL B N   1 
ATOM   5421 C  CA  . VAL B  1 371 ? 10.23100  4.44300   47.15200 1.000 25.87000  ? 365 VAL B CA  1 
ATOM   5422 C  C   . VAL B  1 371 ? 10.30100  4.63900   45.64000 1.000 28.40000  ? 365 VAL B C   1 
ATOM   5423 O  O   . VAL B  1 371 ? 11.00600  3.89600   44.94500 1.000 24.59000  ? 365 VAL B O   1 
ATOM   5424 C  CB  . VAL B  1 371 ? 11.63500  4.32000   47.75700 1.000 25.23000  ? 365 VAL B CB  1 
ATOM   5425 C  CG1 . VAL B  1 371 ? 12.44300  5.63100   47.52000 1.000 27.22000  ? 365 VAL B CG1 1 
ATOM   5426 C  CG2 . VAL B  1 371 ? 11.50900  4.00500   49.24900 1.000 26.01000  ? 365 VAL B CG2 1 
ATOM   5427 N  N   . ALA B  1 372 ? 9.63700   5.68800   45.13400 1.000 24.94000  ? 366 ALA B N   1 
ATOM   5428 C  CA  . ALA B  1 372 ? 9.66600   5.95700   43.69500 1.000 24.77000  ? 366 ALA B CA  1 
ATOM   5429 C  C   . ALA B  1 372 ? 11.10800  6.13100   43.22200 1.000 26.77000  ? 366 ALA B C   1 
ATOM   5430 O  O   . ALA B  1 372 ? 11.83200  6.98300   43.73000 1.000 30.69000  ? 366 ALA B O   1 
ATOM   5431 C  CB  . ALA B  1 372 ? 8.84900   7.21500   43.36900 1.000 26.88000  ? 366 ALA B CB  1 
ATOM   5432 N  N   . ARG B  1 373 ? 11.53600  5.31000   42.26300 1.000 27.68000  ? 367 ARG B N   1 
ATOM   5433 C  CA  . ARG B  1 373 ? 12.91800  5.39500   41.76600 1.000 27.96000  ? 367 ARG B CA  1 
ATOM   5434 C  C   . ARG B  1 373 ? 13.00400  4.73700   40.39000 1.000 24.75000  ? 367 ARG B C   1 
ATOM   5435 O  O   . ARG B  1 373 ? 12.11000  3.92600   40.03600 1.000 24.48000  ? 367 ARG B O   1 
ATOM   5436 C  CB  . ARG B  1 373 ? 13.88500  4.71900   42.75500 1.000 28.99000  ? 367 ARG B CB  1 
ATOM   5437 C  CG  . ARG B  1 373 ? 15.29400  5.20800   42.70700 1.000 41.20000  ? 367 ARG B CG  1 
ATOM   5438 C  CD  . ARG B  1 373 ? 15.92300  5.09600   44.07400 1.000 43.46000  ? 367 ARG B CD  1 
ATOM   5439 N  NE  . ARG B  1 373 ? 15.27400  5.93300   45.07900 1.000 40.78000  ? 367 ARG B NE  1 
ATOM   5440 C  CZ  . ARG B  1 373 ? 15.93100  6.62200   46.00700 1.000 40.08000  ? 367 ARG B CZ  1 
ATOM   5441 N  NH1 . ARG B  1 373 ? 17.25400  6.61900   46.06500 1.000 51.31000  ? 367 ARG B NH1 1 
ATOM   5442 N  NH2 . ARG B  1 373 ? 15.24700  7.33500   46.89600 1.000 40.77000  ? 367 ARG B NH2 1 
ATOM   5443 O  OXT . ARG B  1 373 ? 13.96900  4.96800   39.64200 1.000 25.60000  ? 367 ARG B OXT 1 
HETATM 5444 C  C1  . EDO C  2 .   ? 35.79600  -38.97900 14.20200 1.000 38.92000  ? 401 EDO A C1  1 
HETATM 5445 O  O1  . EDO C  2 .   ? 36.91900  -38.43300 13.48300 1.000 41.20000  ? 401 EDO A O1  1 
HETATM 5446 C  C2  . EDO C  2 .   ? 34.64900  -37.98200 14.17200 1.000 36.20000  ? 401 EDO A C2  1 
HETATM 5447 O  O2  . EDO C  2 .   ? 34.44600  -37.60900 12.80600 1.000 38.46000  ? 401 EDO A O2  1 
HETATM 5448 C  C1  . EDO D  2 .   ? 25.82400  -28.61900 9.91800  1.000 41.27000  ? 402 EDO A C1  1 
HETATM 5449 O  O1  . EDO D  2 .   ? 26.34600  -28.69000 11.25000 1.000 42.48000  ? 402 EDO A O1  1 
HETATM 5450 C  C2  . EDO D  2 .   ? 25.14000  -27.28300 9.67700  1.000 43.03000  ? 402 EDO A C2  1 
HETATM 5451 O  O2  . EDO D  2 .   ? 24.19300  -26.98400 10.71700 1.000 47.66000  ? 402 EDO A O2  1 
HETATM 5452 C  C1  . EDO E  2 .   ? 24.97200  -6.77400  38.65000 0.900 29.68000  ? 403 EDO A C1  1 
HETATM 5453 O  O1  . EDO E  2 .   ? 25.03100  -5.42800  39.11100 0.900 33.26000  ? 403 EDO A O1  1 
HETATM 5454 C  C2  . EDO E  2 .   ? 23.69300  -6.88900  37.83400 0.900 33.59000  ? 403 EDO A C2  1 
HETATM 5455 O  O2  . EDO E  2 .   ? 23.78000  -5.92000  36.78600 0.900 34.93000  ? 403 EDO A O2  1 
HETATM 5456 C  C1  . PEG F  3 .   ? 26.86500  7.42600   8.82900  1.000 33.52000  ? 404 PEG A C1  1 
HETATM 5457 O  O1  . PEG F  3 .   ? 26.21700  6.73900   9.88600  1.000 35.09000  ? 404 PEG A O1  1 
HETATM 5458 C  C2  . PEG F  3 .   ? 28.32100  7.15300   8.83200  1.000 28.67000  ? 404 PEG A C2  1 
HETATM 5459 O  O2  . PEG F  3 .   ? 28.68900  6.88200   10.18200 1.000 41.87000  ? 404 PEG A O2  1 
HETATM 5460 C  C3  . PEG F  3 .   ? 29.71000  5.90600   10.32700 1.000 34.49000  ? 404 PEG A C3  1 
HETATM 5461 C  C4  . PEG F  3 .   ? 29.33600  4.65800   9.58000  1.000 28.59000  ? 404 PEG A C4  1 
HETATM 5462 O  O4  . PEG F  3 .   ? 30.54500  3.97100   9.23600  1.000 28.44000  ? 404 PEG A O4  1 
HETATM 5463 C  C1  . EDO G  2 .   ? 45.44000  -4.91900  5.68200  1.000 37.84000  ? 405 EDO A C1  1 
HETATM 5464 O  O1  . EDO G  2 .   ? 45.61600  -4.56900  7.02900  1.000 38.18000  ? 405 EDO A O1  1 
HETATM 5465 C  C2  . EDO G  2 .   ? 46.67100  -4.86000  4.85900  1.000 37.69000  ? 405 EDO A C2  1 
HETATM 5466 O  O2  . EDO G  2 .   ? 47.84200  -5.22000  5.55300  1.000 37.41000  ? 405 EDO A O2  1 
HETATM 5467 C  C1  . EDO H  2 .   ? 19.72000  16.61100  18.91800 1.000 35.17000  ? 406 EDO A C1  1 
HETATM 5468 O  O1  . EDO H  2 .   ? 19.90400  15.41400  19.71200 1.000 37.00000  ? 406 EDO A O1  1 
HETATM 5469 C  C2  . EDO H  2 .   ? 18.23600  16.96200  18.85600 1.000 26.18000  ? 406 EDO A C2  1 
HETATM 5470 O  O2  . EDO H  2 .   ? 17.48800  15.74000  18.75900 1.000 37.88000  ? 406 EDO A O2  1 
HETATM 5471 C  C1  . EDO I  2 .   ? 50.87600  -17.50700 12.29600 1.000 34.90000  ? 407 EDO A C1  1 
HETATM 5472 O  O1  . EDO I  2 .   ? 50.77900  -18.09000 10.99100 1.000 39.80000  ? 407 EDO A O1  1 
HETATM 5473 C  C2  . EDO I  2 .   ? 50.75900  -18.62200 13.33200 1.000 38.62000  ? 407 EDO A C2  1 
HETATM 5474 O  O2  . EDO I  2 .   ? 49.73900  -19.52800 12.88200 1.000 38.34000  ? 407 EDO A O2  1 
HETATM 5475 C  C1  . EDO J  2 .   ? 30.14200  -6.74700  -0.31500 1.000 28.83000  ? 408 EDO A C1  1 
HETATM 5476 O  O1  . EDO J  2 .   ? 31.37300  -7.46100  -0.42100 1.000 34.89000  ? 408 EDO A O1  1 
HETATM 5477 C  C2  . EDO J  2 .   ? 29.69300  -6.34200  -1.71500 1.000 28.77000  ? 408 EDO A C2  1 
HETATM 5478 O  O2  . EDO J  2 .   ? 30.77200  -5.63400  -2.33700 1.000 35.04000  ? 408 EDO A O2  1 
HETATM 5479 C  C1  . GOL K  4 .   ? 46.42700  -19.12100 32.83400 1.000 38.52000  ? 409 GOL A C1  1 
HETATM 5480 O  O1  . GOL K  4 .   ? 45.43400  -20.10800 32.95200 1.000 41.68000  ? 409 GOL A O1  1 
HETATM 5481 C  C2  . GOL K  4 .   ? 46.32200  -18.57000 31.37200 1.000 41.45000  ? 409 GOL A C2  1 
HETATM 5482 O  O2  . GOL K  4 .   ? 46.72700  -17.22300 31.25400 1.000 43.09000  ? 409 GOL A O2  1 
HETATM 5483 C  C3  . GOL K  4 .   ? 47.21900  -19.52200 30.56900 1.000 38.94000  ? 409 GOL A C3  1 
HETATM 5484 O  O3  . GOL K  4 .   ? 46.54200  -20.73800 30.54400 1.000 40.03000  ? 409 GOL A O3  1 
HETATM 5485 C  C1  . EDO L  2 .   ? 38.85200  -2.99800  44.46500 1.000 42.02000  ? 410 EDO A C1  1 
HETATM 5486 O  O1  . EDO L  2 .   ? 39.92500  -2.04900  44.32700 1.000 42.73000  ? 410 EDO A O1  1 
HETATM 5487 C  C2  . EDO L  2 .   ? 37.54000  -2.26300  44.24600 1.000 41.92000  ? 410 EDO A C2  1 
HETATM 5488 O  O2  . EDO L  2 .   ? 37.79400  -1.28900  43.22600 1.000 35.75000  ? 410 EDO A O2  1 
HETATM 5489 C  C1  . EDO M  2 .   ? 25.76900  -8.59200  13.80900 1.000 31.68000  ? 411 EDO A C1  1 
HETATM 5490 O  O1  . EDO M  2 .   ? 26.15700  -8.85200  15.17300 1.000 40.11000  ? 411 EDO A O1  1 
HETATM 5491 C  C2  . EDO M  2 .   ? 24.47000  -9.34900  13.50000 1.000 34.30000  ? 411 EDO A C2  1 
HETATM 5492 O  O2  . EDO M  2 .   ? 24.42400  -10.57900 14.23000 1.000 31.98000  ? 411 EDO A O2  1 
HETATM 5493 C  C1  . EDO N  2 .   ? 38.51000  12.68000  23.58800 1.000 29.14000  ? 412 EDO A C1  1 
HETATM 5494 O  O1  . EDO N  2 .   ? 39.39200  11.78900  24.27300 1.000 38.21000  ? 412 EDO A O1  1 
HETATM 5495 C  C2  . EDO N  2 .   ? 38.59500  14.06000  24.20600 1.000 33.30000  ? 412 EDO A C2  1 
HETATM 5496 O  O2  . EDO N  2 .   ? 37.36000  14.73400  23.96000 1.000 34.29000  ? 412 EDO A O2  1 
HETATM 5497 N  N   A ASN O  5 .   ? 29.93100  -12.26900 18.24400 0.700 24.36000  ? 413 ASN A N   1 
HETATM 5498 C  CA  A ASN O  5 .   ? 28.85900  -11.30800 17.89400 0.700 22.66000  ? 413 ASN A CA  1 
HETATM 5499 C  C   A ASN O  5 .   ? 27.74200  -11.98700 17.15000 0.700 21.36000  ? 413 ASN A C   1 
HETATM 5500 O  O   A ASN O  5 .   ? 27.95200  -12.94100 16.40600 0.700 22.10000  ? 413 ASN A O   1 
HETATM 5501 C  CB  A ASN O  5 .   ? 29.43000  -10.16600 17.07400 0.700 24.48000  ? 413 ASN A CB  1 
HETATM 5502 C  CG  A ASN O  5 .   ? 29.91900  -9.09700  17.93800 0.700 26.21000  ? 413 ASN A CG  1 
HETATM 5503 O  OD1 A ASN O  5 .   ? 29.84300  -9.23500  19.17300 0.700 20.26000  ? 413 ASN A OD1 1 
HETATM 5504 N  ND2 A ASN O  5 .   ? 30.56000  -8.07900  17.35300 0.700 27.73000  ? 413 ASN A ND2 1 
HETATM 5505 O  OXT A ASN O  5 .   ? 26.60500  -11.65000 17.36300 0.700 26.75000  ? 413 ASN A OXT 1 
HETATM 5506 C  C1  . EDO P  2 .   ? 54.94300  -10.51900 19.49600 1.000 35.94000  ? 414 EDO A C1  1 
HETATM 5507 O  O1  . EDO P  2 .   ? 54.99000  -9.12100  19.83700 1.000 45.64000  ? 414 EDO A O1  1 
HETATM 5508 C  C2  . EDO P  2 .   ? 54.76800  -10.65800 17.99000 1.000 36.95000  ? 414 EDO A C2  1 
HETATM 5509 O  O2  . EDO P  2 .   ? 54.48600  -12.00700 17.63100 1.000 39.99000  ? 414 EDO A O2  1 
HETATM 5510 C  C1  . EDO Q  2 .   ? 43.12900  -14.86000 41.19100 1.000 44.28000  ? 415 EDO A C1  1 
HETATM 5511 O  O1  . EDO Q  2 .   ? 41.98500  -14.01800 40.99300 1.000 46.60000  ? 415 EDO A O1  1 
HETATM 5512 C  C2  . EDO Q  2 .   ? 42.86500  -16.19800 40.50200 1.000 43.02000  ? 415 EDO A C2  1 
HETATM 5513 O  O2  . EDO Q  2 .   ? 41.47600  -16.53700 40.64500 1.000 47.27000  ? 415 EDO A O2  1 
HETATM 5514 C  C1  . EDO R  2 .   ? 38.07900  -18.43000 40.29300 1.000 34.96000  ? 416 EDO A C1  1 
HETATM 5515 O  O1  . EDO R  2 .   ? 38.97200  -17.36700 40.69700 1.000 41.89000  ? 416 EDO A O1  1 
HETATM 5516 C  C2  . EDO R  2 .   ? 38.85000  -19.73900 40.12900 1.000 40.95000  ? 416 EDO A C2  1 
HETATM 5517 O  O2  . EDO R  2 .   ? 40.23700  -19.47500 39.82600 1.000 47.58000  ? 416 EDO A O2  1 
HETATM 5518 C  C1  . EDO S  2 .   ? 21.17900  -21.58200 24.57100 1.000 34.32000  ? 417 EDO A C1  1 
HETATM 5519 O  O1  . EDO S  2 .   ? 22.22300  -21.33000 23.60000 1.000 35.15000  ? 417 EDO A O1  1 
HETATM 5520 C  C2  . EDO S  2 .   ? 19.80800  -21.64500 23.88800 1.000 34.62000  ? 417 EDO A C2  1 
HETATM 5521 O  O2  . EDO S  2 .   ? 19.49700  -20.39800 23.24300 1.000 27.19000  ? 417 EDO A O2  1 
HETATM 5522 CD CD  . CD  T  6 .   ? 30.47900  -14.11500 16.41900 1.000 25.40000  ? 418 CD  A CD  1 
HETATM 5523 C  C1  . EDO U  2 .   ? 21.32300  -13.27000 17.97700 1.000 25.02000  ? 401 EDO B C1  1 
HETATM 5524 O  O1  . EDO U  2 .   ? 19.95600  -12.82900 17.98100 1.000 34.33000  ? 401 EDO B O1  1 
HETATM 5525 C  C2  . EDO U  2 .   ? 22.19600  -12.02000 18.09000 1.000 28.83000  ? 401 EDO B C2  1 
HETATM 5526 O  O2  . EDO U  2 .   ? 21.59900  -11.15500 19.05800 1.000 40.33000  ? 401 EDO B O2  1 
HETATM 5527 C  C1  . EDO V  2 .   ? 13.87200  13.09300  14.82800 1.000 30.18000  ? 402 EDO B C1  1 
HETATM 5528 O  O1  . EDO V  2 .   ? 13.41800  12.10500  13.90600 1.000 39.07000  ? 402 EDO B O1  1 
HETATM 5529 C  C2  . EDO V  2 .   ? 15.09300  13.80300  14.23400 1.000 30.10000  ? 402 EDO B C2  1 
HETATM 5530 O  O2  . EDO V  2 .   ? 15.24000  15.02900  14.93400 1.000 33.35000  ? 402 EDO B O2  1 
HETATM 5531 C  C1  . EDO W  2 .   ? 2.38800   25.19700  -1.31500 1.000 37.91000  ? 403 EDO B C1  1 
HETATM 5532 O  O1  . EDO W  2 .   ? 3.57000   25.99900  -1.23700 1.000 44.63000  ? 403 EDO B O1  1 
HETATM 5533 C  C2  . EDO W  2 .   ? 2.71400   23.77000  -0.87600 1.000 24.99000  ? 403 EDO B C2  1 
HETATM 5534 O  O2  . EDO W  2 .   ? 3.92500   23.31800  -1.52400 1.000 43.98000  ? 403 EDO B O2  1 
HETATM 5535 C  C1  . EDO X  2 .   ? 5.39700   37.75700  7.49400  1.000 46.15000  ? 404 EDO B C1  1 
HETATM 5536 O  O1  . EDO X  2 .   ? 4.05900   37.84000  8.01200  1.000 49.99000  ? 404 EDO B O1  1 
HETATM 5537 C  C2  . EDO X  2 .   ? 6.39600   38.36200  8.47900  1.000 50.47000  ? 404 EDO B C2  1 
HETATM 5538 O  O2  . EDO X  2 .   ? 7.05000   37.32400  9.22100  1.000 40.23000  ? 404 EDO B O2  1 
HETATM 5539 C  C1  . EDO Y  2 .   ? 18.23900  -6.49000  36.31200 1.000 36.85000  ? 405 EDO B C1  1 
HETATM 5540 O  O1  . EDO Y  2 .   ? 17.53200  -6.96400  37.46300 1.000 41.86000  ? 405 EDO B O1  1 
HETATM 5541 C  C2  . EDO Y  2 .   ? 18.84600  -7.69600  35.60500 1.000 37.03000  ? 405 EDO B C2  1 
HETATM 5542 O  O2  . EDO Y  2 .   ? 20.18000  -7.96700  36.09700 1.000 41.23000  ? 405 EDO B O2  1 
HETATM 5543 C  C1  . EDO Z  2 .   ? -4.32200  17.80000  41.17900 1.000 39.99000  ? 406 EDO B C1  1 
HETATM 5544 O  O1  . EDO Z  2 .   ? -3.33000  16.75600  41.13400 1.000 41.04000  ? 406 EDO B O1  1 
HETATM 5545 C  C2  . EDO Z  2 .   ? -3.62600  19.12200  41.49600 1.000 41.52000  ? 406 EDO B C2  1 
HETATM 5546 O  O2  . EDO Z  2 .   ? -2.70800  19.47100  40.45100 1.000 41.32000  ? 406 EDO B O2  1 
HETATM 5547 C  C1  . PEG AA 3 .   ? -6.78500  21.95900  31.12300 0.900 30.79000  ? 407 PEG B C1  1 
HETATM 5548 O  O1  . PEG AA 3 .   ? -7.55200  20.84400  31.54300 0.900 31.51000  ? 407 PEG B O1  1 
HETATM 5549 C  C2  . PEG AA 3 .   ? -7.58100  23.23900  31.12200 0.900 22.69000  ? 407 PEG B C2  1 
HETATM 5550 O  O2  . PEG AA 3 .   ? -7.62000  23.82300  32.43400 0.900 37.57000  ? 407 PEG B O2  1 
HETATM 5551 C  C3  . PEG AA 3 .   ? -6.71100  23.28200  33.39900 0.900 26.26000  ? 407 PEG B C3  1 
HETATM 5552 C  C4  . PEG AA 3 .   ? -5.86800  24.38300  33.98800 0.900 37.49000  ? 407 PEG B C4  1 
HETATM 5553 O  O4  . PEG AA 3 .   ? -4.81200  23.90900  34.83500 0.900 30.85000  ? 407 PEG B O4  1 
HETATM 5554 C  C1  . EDO BA 2 .   ? 17.41400  -4.37800  24.11100 0.800 23.14000  ? 408 EDO B C1  1 
HETATM 5555 O  O1  . EDO BA 2 .   ? 17.91200  -5.06700  25.26900 0.800 20.12000  ? 408 EDO B O1  1 
HETATM 5556 C  C2  . EDO BA 2 .   ? 18.54700  -4.07300  23.13600 0.800 27.99000  ? 408 EDO B C2  1 
HETATM 5557 O  O2  . EDO BA 2 .   ? 19.10300  -5.29200  22.62200 0.800 36.36000  ? 408 EDO B O2  1 
HETATM 5558 N  N   A ASN CA 5 .   ? 9.51400   16.09700  18.58800 0.700 24.50000  ? 409 ASN B N   1 
HETATM 5559 C  CA  A ASN CA 5 .   ? 10.64900  15.20800  18.24300 0.700 25.68000  ? 409 ASN B CA  1 
HETATM 5560 C  C   A ASN CA 5 .   ? 11.61300  15.91200  17.35500 0.700 24.06000  ? 409 ASN B C   1 
HETATM 5561 O  O   A ASN CA 5 .   ? 11.87100  17.08400  17.50600 0.700 25.29000  ? 409 ASN B O   1 
HETATM 5562 C  CB  A ASN CA 5 .   ? 10.19300  13.92800  17.53400 0.700 25.02000  ? 409 ASN B CB  1 
HETATM 5563 C  CG  A ASN CA 5 .   ? 9.74000   12.88800  18.51100 0.700 26.91000  ? 409 ASN B CG  1 
HETATM 5564 O  OD1 A ASN CA 5 .   ? 9.76000   13.15700  19.71700 0.700 24.42000  ? 409 ASN B OD1 1 
HETATM 5565 N  ND2 A ASN CA 5 .   ? 9.19000   11.75000  18.01500 0.700 27.31000  ? 409 ASN B ND2 1 
HETATM 5566 O  OXT A ASN CA 5 .   ? 12.06700  15.31200  16.41200 0.700 24.44000  ? 409 ASN B OXT 1 
HETATM 5567 CD CD  . CD  DA 6 .   ? 9.10100   18.19700  16.96600 1.000 25.23000  ? 410 CD  B CD  1 
HETATM 5568 C  C1  . EDO EA 2 .   ? -7.31700  3.08300   9.91600  1.000 41.88000  ? 411 EDO B C1  1 
HETATM 5569 O  O1  . EDO EA 2 .   ? -6.64900  4.02900   9.06400  1.000 41.68000  ? 411 EDO B O1  1 
HETATM 5570 C  C2  . EDO EA 2 .   ? -8.62600  3.65300   10.46200 1.000 40.44000  ? 411 EDO B C2  1 
HETATM 5571 O  O2  . EDO EA 2 .   ? -8.82300  3.16900   11.80700 1.000 37.19000  ? 411 EDO B O2  1 
HETATM 5572 O  O   . HOH FA 7 .   ? 40.53600  2.83900   7.51900  1.000 36.01000  ? 501 HOH A O   1 
HETATM 5573 O  O   . HOH FA 7 .   ? 29.52000  -6.07400  17.70000 0.700 27.69000  ? 502 HOH A O   1 
HETATM 5574 O  O   . HOH FA 7 .   ? 36.18600  -20.74500 38.87100 1.000 37.86000  ? 503 HOH A O   1 
HETATM 5575 O  O   . HOH FA 7 .   ? 42.10200  -27.08300 31.09000 1.000 35.59000  ? 504 HOH A O   1 
HETATM 5576 O  O   . HOH FA 7 .   ? 25.06200  -16.92300 36.41700 1.000 40.20000  ? 505 HOH A O   1 
HETATM 5577 O  O   . HOH FA 7 .   ? 54.24600  -0.49100  18.60100 1.000 39.47000  ? 506 HOH A O   1 
HETATM 5578 O  O   . HOH FA 7 .   ? 30.30000  -12.45100 39.25000 1.000 29.62000  ? 507 HOH A O   1 
HETATM 5579 O  O   . HOH FA 7 .   ? 51.66900  -11.29300 4.63500  1.000 32.40000  ? 508 HOH A O   1 
HETATM 5580 O  O   . HOH FA 7 .   ? 19.33600  -8.16100  -4.57100 1.000 39.37000  ? 509 HOH A O   1 
HETATM 5581 O  O   . HOH FA 7 .   ? 23.60500  -16.24600 34.15500 1.000 30.66000  ? 510 HOH A O   1 
HETATM 5582 O  O   . HOH FA 7 .   ? 46.11500  8.72700   14.51800 1.000 37.73000  ? 511 HOH A O   1 
HETATM 5583 O  O   . HOH FA 7 .   ? 54.39300  -5.72000  31.55600 1.000 26.86000  ? 512 HOH A O   1 
HETATM 5584 O  O   . HOH FA 7 .   ? 50.11300  -5.26000  36.10800 1.000 26.15000  ? 513 HOH A O   1 
HETATM 5585 O  O   . HOH FA 7 .   ? 49.64100  -21.22000 14.74600 1.000 32.94000  ? 514 HOH A O   1 
HETATM 5586 O  O   . HOH FA 7 .   ? 50.57900  1.35300   27.21400 1.000 25.73000  ? 515 HOH A O   1 
HETATM 5587 O  O   . HOH FA 7 .   ? 20.23200  -0.70400  24.12400 1.000 31.21000  ? 516 HOH A O   1 
HETATM 5588 O  O   . HOH FA 7 .   ? 48.36800  -9.66200  4.24900  1.000 29.44000  ? 517 HOH A O   1 
HETATM 5589 O  O   . HOH FA 7 .   ? 37.13900  8.50200   43.01300 1.000 30.70000  ? 518 HOH A O   1 
HETATM 5590 O  O   . HOH FA 7 .   ? 47.45000  -1.69900  8.67000  1.000 38.00000  ? 519 HOH A O   1 
HETATM 5591 O  O   . HOH FA 7 .   ? 38.88200  -32.59700 8.11300  1.000 33.25000  ? 520 HOH A O   1 
HETATM 5592 O  O   . HOH FA 7 .   ? 23.98300  -11.76300 -2.15200 1.000 28.17000  ? 521 HOH A O   1 
HETATM 5593 O  O   . HOH FA 7 .   ? 33.00100  -7.67200  -2.36000 1.000 27.52000  ? 522 HOH A O   1 
HETATM 5594 O  O   . HOH FA 7 .   ? 53.04200  -0.65500  34.84800 1.000 25.76000  ? 523 HOH A O   1 
HETATM 5595 O  O   . HOH FA 7 .   ? 39.60600  -28.62300 0.22200  1.000 41.32000  ? 524 HOH A O   1 
HETATM 5596 O  O   . HOH FA 7 .   ? 13.50300  11.75300  27.44200 1.000 19.38000  ? 525 HOH A O   1 
HETATM 5597 O  O   . HOH FA 7 .   ? 38.55800  -36.62600 14.24700 1.000 31.00000  ? 526 HOH A O   1 
HETATM 5598 O  O   . HOH FA 7 .   ? 25.92900  -19.49800 6.33200  1.000 28.74000  ? 527 HOH A O   1 
HETATM 5599 O  O   . HOH FA 7 .   ? 23.03900  -3.49900  37.15400 1.000 35.49000  ? 528 HOH A O   1 
HETATM 5600 O  O   . HOH FA 7 .   ? 33.80300  0.87900   8.77400  1.000 20.11000  ? 529 HOH A O   1 
HETATM 5601 O  O   . HOH FA 7 .   ? 29.06700  -13.98100 24.95500 1.000 17.85000  ? 530 HOH A O   1 
HETATM 5602 O  O   . HOH FA 7 .   ? 24.20000  15.38700  30.61400 1.000 19.64000  ? 531 HOH A O   1 
HETATM 5603 O  O   . HOH FA 7 .   ? 29.54800  -14.56200 -2.08500 1.000 31.17000  ? 532 HOH A O   1 
HETATM 5604 O  O   . HOH FA 7 .   ? 53.39900  -19.55700 20.51300 1.000 31.66000  ? 533 HOH A O   1 
HETATM 5605 O  O   . HOH FA 7 .   ? 18.98600  14.32700  24.27500 1.000 25.76000  ? 534 HOH A O   1 
HETATM 5606 O  O   . HOH FA 7 .   ? 32.36300  3.19200   41.58500 1.000 27.78000  ? 535 HOH A O   1 
HETATM 5607 O  O   . HOH FA 7 .   ? 53.00800  -2.63100  21.13500 1.000 30.54000  ? 536 HOH A O   1 
HETATM 5608 O  O   . HOH FA 7 .   ? 19.86700  -20.59500 20.69300 1.000 30.05000  ? 537 HOH A O   1 
HETATM 5609 O  O   . HOH FA 7 .   ? 59.50900  6.03800   31.68900 1.000 24.10000  ? 538 HOH A O   1 
HETATM 5610 O  O   . HOH FA 7 .   ? 33.74500  -32.84600 21.31300 1.000 33.17000  ? 539 HOH A O   1 
HETATM 5611 O  O   . HOH FA 7 .   ? 43.61900  -21.13400 34.48400 1.000 34.17000  ? 540 HOH A O   1 
HETATM 5612 O  O   . HOH FA 7 .   ? 49.55900  3.57900   28.71100 1.000 25.42000  ? 541 HOH A O   1 
HETATM 5613 O  O   . HOH FA 7 .   ? 36.07800  -10.39400 -2.61900 1.000 32.50000  ? 542 HOH A O   1 
HETATM 5614 O  O   . HOH FA 7 .   ? 19.66300  1.86500   25.80600 1.000 23.79000  ? 543 HOH A O   1 
HETATM 5615 O  O   . HOH FA 7 .   ? 35.14800  15.80500  23.11700 1.000 27.69000  ? 544 HOH A O   1 
HETATM 5616 O  O   . HOH FA 7 .   ? 19.45700  3.50700   33.25900 1.000 17.21000  ? 545 HOH A O   1 
HETATM 5617 O  O   . HOH FA 7 .   ? 33.74000  7.81000   13.27800 1.000 26.10000  ? 546 HOH A O   1 
HETATM 5618 O  O   . HOH FA 7 .   ? 23.75300  20.69000  27.85200 1.000 31.46000  ? 547 HOH A O   1 
HETATM 5619 O  O   . HOH FA 7 .   ? 22.47700  -2.93800  22.18300 1.000 26.51000  ? 548 HOH A O   1 
HETATM 5620 O  O   . HOH FA 7 .   ? 27.45900  -13.86200 11.36700 1.000 16.56000  ? 549 HOH A O   1 
HETATM 5621 O  O   . HOH FA 7 .   ? 56.80900  1.38800   30.16800 1.000 28.24000  ? 550 HOH A O   1 
HETATM 5622 O  O   . HOH FA 7 .   ? 46.25700  -14.94100 36.65500 1.000 36.35000  ? 551 HOH A O   1 
HETATM 5623 O  O   . HOH FA 7 .   ? 45.92400  -29.55700 21.85300 1.000 22.88000  ? 552 HOH A O   1 
HETATM 5624 O  O   . HOH FA 7 .   ? 33.18200  -13.97800 19.88500 1.000 21.37000  ? 553 HOH A O   1 
HETATM 5625 O  O   . HOH FA 7 .   ? 49.39800  -4.69400  40.44600 1.000 38.61000  ? 554 HOH A O   1 
HETATM 5626 O  O   . HOH FA 7 .   ? 25.59700  18.79100  29.45900 1.000 32.48000  ? 555 HOH A O   1 
HETATM 5627 O  O   . HOH FA 7 .   ? 37.72300  13.73500  32.69200 1.000 30.15000  ? 556 HOH A O   1 
HETATM 5628 O  O   . HOH FA 7 .   ? 51.12900  13.24300  22.38400 1.000 40.79000  ? 557 HOH A O   1 
HETATM 5629 O  O   . HOH FA 7 .   ? 31.46200  -26.41700 7.26600  1.000 27.17000  ? 558 HOH A O   1 
HETATM 5630 O  O   . HOH FA 7 .   ? 32.22600  -3.21500  49.53200 1.000 53.25000  ? 559 HOH A O   1 
HETATM 5631 O  O   . HOH FA 7 .   ? 24.14100  -10.10100 16.82400 1.000 34.18000  ? 560 HOH A O   1 
HETATM 5632 O  O   . HOH FA 7 .   ? 32.48400  3.56700   11.00700 1.000 29.22000  ? 561 HOH A O   1 
HETATM 5633 O  O   . HOH FA 7 .   ? 39.02900  5.58400   10.33300 1.000 31.93000  ? 562 HOH A O   1 
HETATM 5634 O  O   . HOH FA 7 .   ? 37.06800  11.93500  17.08200 1.000 34.13000  ? 563 HOH A O   1 
HETATM 5635 O  O   . HOH FA 7 .   ? 47.93800  7.15500   34.97500 1.000 24.84000  ? 564 HOH A O   1 
HETATM 5636 O  O   . HOH FA 7 .   ? 17.02900  24.42400  28.93900 1.000 25.63000  ? 565 HOH A O   1 
HETATM 5637 O  O   . HOH FA 7 .   ? 26.73500  -23.48800 17.75400 1.000 25.89000  ? 566 HOH A O   1 
HETATM 5638 O  O   . HOH FA 7 .   ? 26.37200  -10.59500 37.97900 1.000 28.25000  ? 567 HOH A O   1 
HETATM 5639 O  O   . HOH FA 7 .   ? 48.93000  4.62000   14.28400 1.000 38.23000  ? 568 HOH A O   1 
HETATM 5640 O  O   . HOH FA 7 .   ? 27.38200  9.88500   18.16500 1.000 30.55000  ? 569 HOH A O   1 
HETATM 5641 O  O   . HOH FA 7 .   ? 55.60800  -1.72800  27.77000 1.000 31.86000  ? 570 HOH A O   1 
HETATM 5642 O  O   . HOH FA 7 .   ? 18.50700  21.85400  7.99800  1.000 36.93000  ? 571 HOH A O   1 
HETATM 5643 O  O   . HOH FA 7 .   ? 35.97500  -1.72200  -3.14900 1.000 31.26000  ? 572 HOH A O   1 
HETATM 5644 O  O   . HOH FA 7 .   ? 21.30400  1.45500   32.34000 1.000 15.60000  ? 573 HOH A O   1 
HETATM 5645 O  O   . HOH FA 7 .   ? 21.63600  -14.05600 7.37100  1.000 29.92000  ? 574 HOH A O   1 
HETATM 5646 O  O   . HOH FA 7 .   ? 22.06500  -11.87500 14.39800 1.000 29.53000  ? 575 HOH A O   1 
HETATM 5647 O  O   . HOH FA 7 .   ? 25.23200  -22.39700 11.59700 1.000 27.16000  ? 576 HOH A O   1 
HETATM 5648 O  O   . HOH FA 7 .   ? 57.64500  -13.41200 21.26600 1.000 40.70000  ? 577 HOH A O   1 
HETATM 5649 O  O   . HOH FA 7 .   ? 31.30000  -17.02700 37.05800 1.000 28.84000  ? 578 HOH A O   1 
HETATM 5650 O  O   . HOH FA 7 .   ? 31.26100  -4.01200  1.37200  1.000 23.09000  ? 579 HOH A O   1 
HETATM 5651 O  O   . HOH FA 7 .   ? 35.41700  -12.36800 39.28900 1.000 24.66000  ? 580 HOH A O   1 
HETATM 5652 O  O   . HOH FA 7 .   ? 30.48100  0.41600   16.38400 1.000 29.74000  ? 581 HOH A O   1 
HETATM 5653 O  O   . HOH FA 7 .   ? 48.76800  -20.20600 10.14400 1.000 29.08000  ? 582 HOH A O   1 
HETATM 5654 O  O   . HOH FA 7 .   ? 36.22100  -27.30600 1.72100  1.000 37.69000  ? 583 HOH A O   1 
HETATM 5655 O  O   . HOH FA 7 .   ? 31.60200  -31.66900 11.60400 1.000 37.97000  ? 584 HOH A O   1 
HETATM 5656 O  O   . HOH FA 7 .   ? 23.84600  -25.47100 13.61500 1.000 28.45000  ? 585 HOH A O   1 
HETATM 5657 O  O   . HOH FA 7 .   ? 28.30700  -12.36300 -1.17600 1.000 29.12000  ? 586 HOH A O   1 
HETATM 5658 O  O   . HOH FA 7 .   ? 25.77200  -6.55300  16.55600 1.000 37.67000  ? 587 HOH A O   1 
HETATM 5659 O  O   . HOH FA 7 .   ? 47.47300  0.77600   19.63800 1.000 24.77000  ? 588 HOH A O   1 
HETATM 5660 O  O   . HOH FA 7 .   ? 40.12500  -10.47000 37.27400 1.000 22.07000  ? 589 HOH A O   1 
HETATM 5661 O  O   . HOH FA 7 .   ? 32.57100  9.35500   15.75300 1.000 34.57000  ? 590 HOH A O   1 
HETATM 5662 O  O   . HOH FA 7 .   ? 22.91700  -9.37100  -3.38100 1.000 26.35000  ? 591 HOH A O   1 
HETATM 5663 O  O   . HOH FA 7 .   ? 55.23400  -13.66000 19.65400 1.000 31.32000  ? 592 HOH A O   1 
HETATM 5664 O  O   . HOH FA 7 .   ? 25.78600  23.34500  16.94700 1.000 30.98000  ? 593 HOH A O   1 
HETATM 5665 O  O   . HOH FA 7 .   ? 48.51800  9.00400   17.42100 1.000 32.37000  ? 594 HOH A O   1 
HETATM 5666 O  O   . HOH FA 7 .   ? 52.48600  -7.44300  32.97500 1.000 27.40000  ? 595 HOH A O   1 
HETATM 5667 O  O   . HOH FA 7 .   ? 23.65400  -15.35500 5.23500  1.000 28.56000  ? 596 HOH A O   1 
HETATM 5668 O  O   . HOH FA 7 .   ? 40.55400  -12.11800 -1.96700 1.000 29.81000  ? 597 HOH A O   1 
HETATM 5669 O  O   . HOH FA 7 .   ? 42.03500  14.93100  25.05500 1.000 41.45000  ? 598 HOH A O   1 
HETATM 5670 O  O   . HOH FA 7 .   ? 39.67600  -22.67000 -1.58600 1.000 37.30000  ? 599 HOH A O   1 
HETATM 5671 O  O   . HOH FA 7 .   ? 30.12800  7.94600   21.56100 1.000 17.95000  ? 600 HOH A O   1 
HETATM 5672 O  O   . HOH FA 7 .   ? 34.93100  -34.51200 13.58000 1.000 40.45000  ? 601 HOH A O   1 
HETATM 5673 O  O   . HOH FA 7 .   ? 21.29400  8.31600   25.60700 1.000 21.94000  ? 602 HOH A O   1 
HETATM 5674 O  O   . HOH FA 7 .   ? 48.35900  -13.25200 3.36600  1.000 35.69000  ? 603 HOH A O   1 
HETATM 5675 O  O   . HOH FA 7 .   ? 49.16600  -7.60300  5.34700  1.000 31.62000  ? 604 HOH A O   1 
HETATM 5676 O  O   . HOH FA 7 .   ? 42.60100  2.20100   5.92300  1.000 40.68000  ? 605 HOH A O   1 
HETATM 5677 O  O   . HOH FA 7 .   ? 55.40900  4.99900   29.17100 1.000 32.73000  ? 606 HOH A O   1 
HETATM 5678 O  O   . HOH FA 7 .   ? 29.72700  -5.68300  9.59000  1.000 19.74000  ? 607 HOH A O   1 
HETATM 5679 O  O   . HOH FA 7 .   ? 35.95300  -11.41300 11.33700 1.000 21.87000  ? 608 HOH A O   1 
HETATM 5680 O  O   . HOH FA 7 .   ? 54.75200  6.82100   36.15400 1.000 31.63000  ? 609 HOH A O   1 
HETATM 5681 O  O   . HOH FA 7 .   ? 20.75100  11.24800  24.51900 1.000 29.67000  ? 610 HOH A O   1 
HETATM 5682 O  O   . HOH FA 7 .   ? 21.64700  -18.39200 23.30000 1.000 19.09000  ? 611 HOH A O   1 
HETATM 5683 O  O   . HOH FA 7 .   ? 13.49600  12.74000  30.14400 1.000 16.51000  ? 612 HOH A O   1 
HETATM 5684 O  O   . HOH FA 7 .   ? 17.81900  22.01000  24.64300 1.000 19.76000  ? 613 HOH A O   1 
HETATM 5685 O  O   . HOH FA 7 .   ? 28.03800  -7.52800  25.87700 1.000 18.08000  ? 614 HOH A O   1 
HETATM 5686 O  O   . HOH FA 7 .   ? 27.17600  -9.19100  6.83000  1.000 22.31000  ? 615 HOH A O   1 
HETATM 5687 O  O   . HOH FA 7 .   ? 26.43000  -23.43100 3.59700  1.000 37.60000  ? 616 HOH A O   1 
HETATM 5688 O  O   B HOH FA 7 .   ? 30.81600  -12.47800 18.54200 0.300 20.55000  ? 617 HOH A O   1 
HETATM 5689 O  O   . HOH FA 7 .   ? 34.39800  14.91400  29.95500 1.000 23.84000  ? 618 HOH A O   1 
HETATM 5690 O  O   . HOH FA 7 .   ? 42.59100  7.70600   15.42900 1.000 28.43000  ? 619 HOH A O   1 
HETATM 5691 O  O   . HOH FA 7 .   ? 19.11400  1.17500   37.62700 1.000 28.26000  ? 620 HOH A O   1 
HETATM 5692 O  O   . HOH FA 7 .   ? 43.99500  0.63200   43.17400 1.000 35.10000  ? 621 HOH A O   1 
HETATM 5693 O  O   . HOH FA 7 .   ? 21.88400  -4.62300  4.45900  1.000 23.58000  ? 622 HOH A O   1 
HETATM 5694 O  O   . HOH FA 7 .   ? 26.84100  5.08200   44.74900 1.000 43.09000  ? 623 HOH A O   1 
HETATM 5695 O  O   . HOH FA 7 .   ? 41.79300  -7.40800  1.73000  1.000 26.23000  ? 624 HOH A O   1 
HETATM 5696 O  O   . HOH FA 7 .   ? 20.69400  0.18400   42.82600 1.000 43.02000  ? 625 HOH A O   1 
HETATM 5697 O  O   . HOH FA 7 .   ? 21.68000  -22.70000 19.58000 1.000 30.09000  ? 626 HOH A O   1 
HETATM 5698 O  O   . HOH FA 7 .   ? 29.56400  12.49300  17.79700 1.000 35.70000  ? 627 HOH A O   1 
HETATM 5699 O  O   . HOH FA 7 .   ? 50.53600  -22.64200 23.04800 1.000 38.12000  ? 628 HOH A O   1 
HETATM 5700 O  O   . HOH FA 7 .   ? 26.16700  7.11300   2.55500  1.000 32.61000  ? 629 HOH A O   1 
HETATM 5701 O  O   . HOH FA 7 .   ? 22.16300  -14.30700 2.58700  1.000 35.00000  ? 630 HOH A O   1 
HETATM 5702 O  O   . HOH FA 7 .   ? 48.58900  16.57000  24.75800 1.000 46.60000  ? 631 HOH A O   1 
HETATM 5703 O  O   . HOH FA 7 .   ? 32.82400  -23.67500 30.28400 1.000 24.29000  ? 632 HOH A O   1 
HETATM 5704 O  O   . HOH FA 7 .   ? 23.11200  -8.41000  19.80900 1.000 33.46000  ? 633 HOH A O   1 
HETATM 5705 O  O   . HOH FA 7 .   ? 34.89800  -4.67700  -4.72600 1.000 36.99000  ? 634 HOH A O   1 
HETATM 5706 O  O   . HOH FA 7 .   ? 26.98400  -30.18800 19.43300 1.000 32.57000  ? 635 HOH A O   1 
HETATM 5707 O  O   . HOH FA 7 .   ? 29.21700  2.12700   12.99200 1.000 35.11000  ? 636 HOH A O   1 
HETATM 5708 O  O   . HOH FA 7 .   ? 32.21100  -27.99500 5.44900  1.000 32.36000  ? 637 HOH A O   1 
HETATM 5709 O  O   . HOH FA 7 .   ? 21.32600  -11.49800 4.45400  1.000 31.09000  ? 638 HOH A O   1 
HETATM 5710 O  O   . HOH FA 7 .   ? 20.94900  -11.35700 9.64700  1.000 32.34000  ? 639 HOH A O   1 
HETATM 5711 O  O   . HOH FA 7 .   ? 22.43000  -22.96000 17.10600 1.000 26.12000  ? 640 HOH A O   1 
HETATM 5712 O  O   . HOH FA 7 .   ? 41.27100  10.64300  37.67500 1.000 25.39000  ? 641 HOH A O   1 
HETATM 5713 O  O   . HOH FA 7 .   ? 28.59800  -9.87500  40.81800 1.000 30.32000  ? 642 HOH A O   1 
HETATM 5714 O  O   . HOH FA 7 .   ? 45.11500  -16.82600 -0.26500 1.000 30.32000  ? 643 HOH A O   1 
HETATM 5715 O  O   . HOH FA 7 .   ? 26.67300  8.19800   38.70400 1.000 22.32000  ? 644 HOH A O   1 
HETATM 5716 O  O   . HOH FA 7 .   ? 27.63700  -20.72200 4.15300  1.000 28.95000  ? 645 HOH A O   1 
HETATM 5717 O  O   . HOH FA 7 .   ? 20.05400  16.79500  23.35200 1.000 22.60000  ? 646 HOH A O   1 
HETATM 5718 O  O   . HOH FA 7 .   ? 17.23600  -19.03800 24.25800 1.000 22.79000  ? 647 HOH A O   1 
HETATM 5719 O  O   . HOH FA 7 .   ? 36.82400  -36.49900 10.45600 1.000 33.79000  ? 648 HOH A O   1 
HETATM 5720 O  O   . HOH FA 7 .   ? 17.93500  -2.41500  -1.25200 1.000 31.29000  ? 649 HOH A O   1 
HETATM 5721 O  O   . HOH FA 7 .   ? 35.74400  -7.70800  -1.86000 1.000 26.63000  ? 650 HOH A O   1 
HETATM 5722 O  O   . HOH FA 7 .   ? 26.04600  -22.46100 30.20700 1.000 34.93000  ? 651 HOH A O   1 
HETATM 5723 O  O   . HOH FA 7 .   ? 26.05400  -0.56000  39.90900 1.000 29.06000  ? 652 HOH A O   1 
HETATM 5724 O  O   . HOH FA 7 .   ? 26.69300  1.49500   37.98100 1.000 20.82000  ? 653 HOH A O   1 
HETATM 5725 O  O   . HOH FA 7 .   ? 41.29000  -8.10800  43.33400 1.000 32.45000  ? 654 HOH A O   1 
HETATM 5726 O  O   . HOH FA 7 .   ? 52.34800  -11.03600 8.84500  1.000 31.37000  ? 655 HOH A O   1 
HETATM 5727 O  O   . HOH FA 7 .   ? 32.43500  2.84300   15.81300 1.000 27.51000  ? 656 HOH A O   1 
HETATM 5728 O  O   . HOH FA 7 .   ? 28.31500  -33.57300 10.02100 1.000 40.70000  ? 657 HOH A O   1 
HETATM 5729 O  O   . HOH FA 7 .   ? 26.72700  -12.09100 13.48500 1.000 20.44000  ? 658 HOH A O   1 
HETATM 5730 O  O   . HOH FA 7 .   ? 46.26700  19.70100  23.49600 1.000 35.90000  ? 659 HOH A O   1 
HETATM 5731 O  O   . HOH FA 7 .   ? 41.05000  -36.45000 14.20400 1.000 27.03000  ? 660 HOH A O   1 
HETATM 5732 O  O   . HOH FA 7 .   ? 25.42600  -4.48400  19.56300 1.000 30.65000  ? 661 HOH A O   1 
HETATM 5733 O  O   . HOH FA 7 .   ? 28.04700  15.53900  24.22300 1.000 29.97000  ? 662 HOH A O   1 
HETATM 5734 O  O   . HOH FA 7 .   ? 43.31100  -25.24600 20.76200 1.000 24.22000  ? 663 HOH A O   1 
HETATM 5735 O  O   . HOH FA 7 .   ? 32.92000  -20.15900 19.89900 1.000 22.12000  ? 664 HOH A O   1 
HETATM 5736 O  O   . HOH FA 7 .   ? 47.99800  1.17800   15.68500 1.000 29.89000  ? 665 HOH A O   1 
HETATM 5737 O  O   . HOH FA 7 .   ? 22.26700  5.15600   7.94900  1.000 37.89000  ? 666 HOH A O   1 
HETATM 5738 O  O   . HOH FA 7 .   ? 52.12200  -22.25600 4.38300  1.000 41.96000  ? 667 HOH A O   1 
HETATM 5739 O  O   . HOH FA 7 .   ? 36.13200  -12.55800 13.79300 1.000 24.08000  ? 668 HOH A O   1 
HETATM 5740 O  O   . HOH FA 7 .   ? 27.60200  20.92100  19.41000 1.000 36.19000  ? 669 HOH A O   1 
HETATM 5741 O  O   . HOH FA 7 .   ? 56.06000  -1.10800  34.56700 1.000 32.19000  ? 670 HOH A O   1 
HETATM 5742 O  O   . HOH FA 7 .   ? 38.40900  -15.37100 16.99100 1.000 25.13000  ? 671 HOH A O   1 
HETATM 5743 O  O   . HOH FA 7 .   ? 27.04600  5.02200   1.69200  1.000 24.19000  ? 672 HOH A O   1 
HETATM 5744 O  O   . HOH FA 7 .   ? 45.60100  -13.27200 3.32800  1.000 30.97000  ? 673 HOH A O   1 
HETATM 5745 O  O   . HOH FA 7 .   ? 19.67500  -3.06500  6.14700  1.000 38.40000  ? 674 HOH A O   1 
HETATM 5746 O  O   . HOH FA 7 .   ? 33.91300  -26.80300 36.76500 1.000 37.54000  ? 675 HOH A O   1 
HETATM 5747 O  O   . HOH FA 7 .   ? 43.75200  -24.25000 22.95400 1.000 32.41000  ? 676 HOH A O   1 
HETATM 5748 O  O   . HOH FA 7 .   ? 31.14100  -16.77300 19.59400 1.000 19.44000  ? 677 HOH A O   1 
HETATM 5749 O  O   . HOH FA 7 .   ? 34.00400  -0.51800  17.09300 1.000 24.93000  ? 678 HOH A O   1 
HETATM 5750 O  O   . HOH FA 7 .   ? 35.67400  -4.35000  16.73200 1.000 21.69000  ? 679 HOH A O   1 
HETATM 5751 O  O   . HOH FA 7 .   ? 53.78200  1.80400   40.70800 1.000 37.80000  ? 680 HOH A O   1 
HETATM 5752 O  O   . HOH FA 7 .   ? 58.19800  -4.46800  27.42300 1.000 39.02000  ? 681 HOH A O   1 
HETATM 5753 O  O   . HOH FA 7 .   ? 30.96600  -21.43200 -1.77300 1.000 22.95000  ? 682 HOH A O   1 
HETATM 5754 O  O   . HOH FA 7 .   ? 45.98100  -26.55200 28.67200 1.000 39.62000  ? 683 HOH A O   1 
HETATM 5755 O  O   . HOH FA 7 .   ? 25.56100  -17.35800 2.89500  1.000 34.59000  ? 684 HOH A O   1 
HETATM 5756 O  O   . HOH FA 7 .   ? 22.62500  9.51600   19.21400 1.000 35.80000  ? 685 HOH A O   1 
HETATM 5757 O  O   . HOH FA 7 .   ? 51.89500  -17.46500 16.80300 1.000 43.14000  ? 686 HOH A O   1 
HETATM 5758 O  O   . HOH FA 7 .   ? 21.00500  -4.22400  1.76900  1.000 31.46000  ? 687 HOH A O   1 
HETATM 5759 O  O   . HOH FA 7 .   ? 39.92200  6.13800   42.31900 1.000 31.63000  ? 688 HOH A O   1 
HETATM 5760 O  O   . HOH FA 7 .   ? 15.61800  16.63200  34.40900 1.000 24.50000  ? 689 HOH A O   1 
HETATM 5761 O  O   . HOH FA 7 .   ? 46.87000  1.14300   10.37400 1.000 40.06000  ? 690 HOH A O   1 
HETATM 5762 O  O   . HOH FA 7 .   ? 24.59000  -2.77100  40.27000 1.000 38.61000  ? 691 HOH A O   1 
HETATM 5763 O  O   . HOH FA 7 .   ? 33.74600  -19.67400 -2.16100 1.000 32.49000  ? 692 HOH A O   1 
HETATM 5764 O  O   . HOH FA 7 .   ? 48.13900  -28.04000 8.17200  1.000 38.68000  ? 693 HOH A O   1 
HETATM 5765 O  O   . HOH FA 7 .   ? 32.52800  -10.77300 30.50700 1.000 22.80000  ? 694 HOH A O   1 
HETATM 5766 O  O   . HOH FA 7 .   ? 17.82100  22.82600  32.74100 1.000 29.30000  ? 695 HOH A O   1 
HETATM 5767 O  O   . HOH FA 7 .   ? 50.14500  -13.19900 29.66700 1.000 30.44000  ? 696 HOH A O   1 
HETATM 5768 O  O   . HOH FA 7 .   ? 49.83700  -25.01700 14.93800 1.000 37.75000  ? 697 HOH A O   1 
HETATM 5769 O  O   . HOH FA 7 .   ? 23.23300  1.12800   20.79700 1.000 20.83000  ? 698 HOH A O   1 
HETATM 5770 O  O   . HOH FA 7 .   ? 21.86800  -23.94000 13.37900 1.000 28.19000  ? 699 HOH A O   1 
HETATM 5771 O  O   . HOH FA 7 .   ? 37.72700  -12.15300 40.69600 1.000 34.73000  ? 700 HOH A O   1 
HETATM 5772 O  O   . HOH FA 7 .   ? 23.78700  -5.96800  12.24200 1.000 33.32000  ? 701 HOH A O   1 
HETATM 5773 O  O   . HOH FA 7 .   ? 35.49600  -24.37100 29.94700 1.000 23.69000  ? 702 HOH A O   1 
HETATM 5774 O  O   . HOH FA 7 .   ? 49.09000  -15.55700 30.56700 1.000 39.49000  ? 703 HOH A O   1 
HETATM 5775 O  O   . HOH FA 7 .   ? 49.95000  -19.19000 3.12300  1.000 40.43000  ? 704 HOH A O   1 
HETATM 5776 O  O   . HOH FA 7 .   ? 47.20400  -30.63500 9.34800  1.000 31.73000  ? 705 HOH A O   1 
HETATM 5777 O  O   . HOH FA 7 .   ? 57.04700  5.70400   35.57200 1.000 31.29000  ? 706 HOH A O   1 
HETATM 5778 O  O   . HOH FA 7 .   ? 23.98700  4.01300   20.37000 1.000 21.51000  ? 707 HOH A O   1 
HETATM 5779 O  O   . HOH FA 7 .   ? 37.94900  5.35200   45.86700 1.000 34.93000  ? 708 HOH A O   1 
HETATM 5780 O  O   . HOH FA 7 .   ? 42.01500  0.06600   46.31900 1.000 41.47000  ? 709 HOH A O   1 
HETATM 5781 O  O   . HOH FA 7 .   ? 50.10500  -8.93900  7.48300  1.000 31.95000  ? 710 HOH A O   1 
HETATM 5782 O  O   . HOH FA 7 .   ? 49.90300  6.11000   28.04000 1.000 26.90000  ? 711 HOH A O   1 
HETATM 5783 O  O   . HOH FA 7 .   ? 50.39100  9.10100   24.46300 1.000 42.24000  ? 712 HOH A O   1 
HETATM 5784 O  O   . HOH FA 7 .   ? 29.62200  -24.52400 31.47700 1.000 35.71000  ? 713 HOH A O   1 
HETATM 5785 O  O   . HOH FA 7 .   ? 40.92400  -23.28100 34.07900 1.000 39.50000  ? 714 HOH A O   1 
HETATM 5786 O  O   . HOH FA 7 .   ? 52.04500  6.69500   29.69800 1.000 32.70000  ? 715 HOH A O   1 
HETATM 5787 O  O   . HOH FA 7 .   ? 26.98100  3.41300   -2.64500 1.000 27.37000  ? 716 HOH A O   1 
HETATM 5788 O  O   . HOH FA 7 .   ? 37.20900  -1.80500  1.36200  1.000 21.58000  ? 717 HOH A O   1 
HETATM 5789 O  O   . HOH FA 7 .   ? 35.79600  -28.12400 26.83400 1.000 32.29000  ? 718 HOH A O   1 
HETATM 5790 O  O   . HOH FA 7 .   ? 32.37600  -32.70700 7.81600  1.000 38.92000  ? 719 HOH A O   1 
HETATM 5791 O  O   . HOH FA 7 .   ? 27.81200  -24.53200 24.32600 1.000 35.17000  ? 720 HOH A O   1 
HETATM 5792 O  O   . HOH FA 7 .   ? 24.43000  -24.27500 9.26500  1.000 36.18000  ? 721 HOH A O   1 
HETATM 5793 O  O   . HOH FA 7 .   ? 49.08200  9.51400   33.47300 1.000 34.30000  ? 722 HOH A O   1 
HETATM 5794 O  O   . HOH FA 7 .   ? 25.73000  -22.87800 20.22000 1.000 31.11000  ? 723 HOH A O   1 
HETATM 5795 O  O   . HOH FA 7 .   ? 29.01100  -27.17600 3.11100  1.000 38.48000  ? 724 HOH A O   1 
HETATM 5796 O  O   . HOH FA 7 .   ? 20.06300  -0.63200  35.80200 1.000 21.31000  ? 725 HOH A O   1 
HETATM 5797 O  O   . HOH FA 7 .   ? 26.40400  -22.78700 23.07700 1.000 30.18000  ? 726 HOH A O   1 
HETATM 5798 O  O   . HOH FA 7 .   ? 43.29600  -6.20900  3.74700  1.000 32.43000  ? 727 HOH A O   1 
HETATM 5799 O  O   . HOH FA 7 .   ? 22.47700  6.10700   20.96300 1.000 28.57000  ? 728 HOH A O   1 
HETATM 5800 O  O   . HOH FA 7 .   ? 43.70000  -1.88900  4.21200  1.000 37.07000  ? 729 HOH A O   1 
HETATM 5801 O  O   . HOH FA 7 .   ? 45.92300  -25.98900 2.55600  1.000 38.49000  ? 730 HOH A O   1 
HETATM 5802 O  O   . HOH FA 7 .   ? 58.66500  8.75800   29.06800 1.000 32.86000  ? 731 HOH A O   1 
HETATM 5803 O  O   . HOH FA 7 .   ? 28.46600  17.53300  26.81800 1.000 34.93000  ? 732 HOH A O   1 
HETATM 5804 O  O   . HOH FA 7 .   ? 47.58600  -31.83100 13.15800 1.000 33.13000  ? 733 HOH A O   1 
HETATM 5805 O  O   . HOH FA 7 .   ? 23.92900  -9.52200  34.80400 1.000 29.64000  ? 734 HOH A O   1 
HETATM 5806 O  O   . HOH FA 7 .   ? 37.75000  -18.26500 -1.52200 1.000 35.81000  ? 735 HOH A O   1 
HETATM 5807 O  O   . HOH FA 7 .   ? 27.96100  18.12600  30.13800 1.000 39.01000  ? 736 HOH A O   1 
HETATM 5808 O  O   . HOH FA 7 .   ? 56.04100  -22.92600 27.44000 1.000 35.24000  ? 737 HOH A O   1 
HETATM 5809 O  O   . HOH FA 7 .   ? 58.61000  5.16000   29.52000 1.000 36.09000  ? 738 HOH A O   1 
HETATM 5810 O  O   . HOH FA 7 .   ? 23.42200  7.20800   1.52200  1.000 36.66000  ? 739 HOH A O   1 
HETATM 5811 O  O   . HOH FA 7 .   ? 38.78600  -4.96600  -1.47400 1.000 32.07000  ? 740 HOH A O   1 
HETATM 5812 O  O   . HOH FA 7 .   ? 25.40600  -22.87300 6.47600  1.000 40.95000  ? 741 HOH A O   1 
HETATM 5813 O  O   . HOH FA 7 .   ? 23.21900  15.82600  33.13700 1.000 33.43000  ? 742 HOH A O   1 
HETATM 5814 O  O   . HOH FA 7 .   ? 42.84700  -9.88800  0.95400  1.000 30.13000  ? 743 HOH A O   1 
HETATM 5815 O  O   . HOH FA 7 .   ? 45.07000  -11.14700 1.69100  1.000 34.04000  ? 744 HOH A O   1 
HETATM 5816 O  O   . HOH FA 7 .   ? 51.73200  -26.66500 14.35000 1.000 40.74000  ? 745 HOH A O   1 
HETATM 5817 O  O   . HOH FA 7 .   ? 48.69300  -25.93100 3.92400  1.000 42.75000  ? 746 HOH A O   1 
HETATM 5818 O  O   . HOH FA 7 .   ? 49.21600  -27.14400 6.08900  1.000 40.78000  ? 747 HOH A O   1 
HETATM 5819 O  O   . HOH FA 7 .   ? 41.29300  -15.06700 -2.45200 1.000 38.99000  ? 748 HOH A O   1 
HETATM 5820 O  O   . HOH FA 7 .   ? 25.47700  4.68700   -0.80800 1.000 25.90000  ? 749 HOH A O   1 
HETATM 5821 O  O   . HOH FA 7 .   ? 37.37600  -31.49400 5.85300  1.000 43.92000  ? 750 HOH A O   1 
HETATM 5822 O  O   . HOH FA 7 .   ? 58.76400  -21.35600 28.44800 1.000 42.70000  ? 751 HOH A O   1 
HETATM 5823 O  O   . HOH FA 7 .   ? 31.30100  3.85400   13.48200 1.000 30.60000  ? 752 HOH A O   1 
HETATM 5824 O  O   . HOH FA 7 .   ? 51.70700  -29.76000 14.11200 1.000 36.03000  ? 753 HOH A O   1 
HETATM 5825 O  O   . HOH FA 7 .   ? 26.878    18.015    34.704   1.000 39.43000  ? 754 HOH A O   1 
HETATM 5826 O  O   . HOH FA 7 .   ? 27.52300  -19.13900 1.70400  1.000 39.60000  ? 755 HOH A O   1 
HETATM 5827 O  O   . HOH FA 7 .   ? 30.25000  -31.94000 15.08600 1.000 38.15000  ? 756 HOH A O   1 
HETATM 5828 O  O   . HOH FA 7 .   ? 28.38000  -32.12900 12.40000 1.000 42.13000  ? 757 HOH A O   1 
HETATM 5829 O  O   . HOH FA 7 .   ? 19.98500  -1.89800  40.02600 1.000 35.53000  ? 758 HOH A O   1 
HETATM 5830 O  O   . HOH FA 7 .   ? 39.33000  -15.96300 -3.53900 1.000 39.78000  ? 759 HOH A O   1 
HETATM 5831 O  O   . HOH FA 7 .   ? 49.80600  -31.35500 12.60000 1.000 35.24000  ? 760 HOH A O   1 
HETATM 5832 O  O   . HOH FA 7 .   ? 55.31500  3.10900   27.25900 1.000 36.72000  ? 761 HOH A O   1 
HETATM 5833 O  O   . HOH FA 7 .   ? 21.04400  -9.38300  6.31400  1.000 26.46000  ? 762 HOH A O   1 
HETATM 5834 O  O   . HOH FA 7 .   ? 46.20600  -19.06400 -0.67800 1.000 37.35000  ? 763 HOH A O   1 
HETATM 5835 O  O   . HOH FA 7 .   ? 53.84000  0.14100   24.14600 1.000 33.60000  ? 764 HOH A O   1 
HETATM 5836 O  O   . HOH FA 7 .   ? 21.169    -2.768    -8.777   1.000 34.21000  ? 765 HOH A O   1 
HETATM 5837 O  O   . HOH FA 7 .   ? 25.62800  4.09500   18.10200 1.000 36.57000  ? 766 HOH A O   1 
HETATM 5838 O  O   . HOH FA 7 .   ? 18.30300  5.64800   37.21300 1.000 37.82000  ? 767 HOH A O   1 
HETATM 5839 O  O   . HOH FA 7 .   ? 18.82100  2.94800   22.04400 1.000 25.97000  ? 768 HOH A O   1 
HETATM 5840 O  O   . HOH FA 7 .   ? 42.63700  -10.41400 -1.66000 1.000 34.24000  ? 769 HOH A O   1 
HETATM 5841 O  O   . HOH FA 7 .   ? 19.53400  -7.76200  2.72200  1.000 33.12000  ? 770 HOH A O   1 
HETATM 5842 O  O   . HOH FA 7 .   ? 52.14100  9.07900   30.73300 1.000 37.55000  ? 771 HOH A O   1 
HETATM 5843 O  O   . HOH FA 7 .   ? 53.07900  2.30300   26.22500 1.000 33.93000  ? 772 HOH A O   1 
HETATM 5844 O  O   . HOH FA 7 .   ? 28.27500  5.38200   18.38000 1.000 31.77000  ? 773 HOH A O   1 
HETATM 5845 O  O   . HOH FA 7 .   ? 20.62600  -10.22800 -4.91500 1.000 35.33000  ? 774 HOH A O   1 
HETATM 5846 O  O   . HOH FA 7 .   ? 50.25900  6.16500   25.29600 1.000 32.76000  ? 775 HOH A O   1 
HETATM 5847 O  O   . HOH FA 7 .   ? 20.48800  -6.88800  5.06700  1.000 29.98000  ? 776 HOH A O   1 
HETATM 5848 O  O   . HOH FA 7 .   ? 18.42800  4.75900   40.07900 1.000 38.30000  ? 777 HOH A O   1 
HETATM 5849 O  O   . HOH FA 7 .   ? 42.837    18.527    24.058   1.000 35.96000  ? 778 HOH A O   1 
HETATM 5850 O  O   . HOH FA 7 .   ? 24.35500  -24.80700 16.79700 1.000 30.28000  ? 779 HOH A O   1 
HETATM 5851 O  O   . HOH FA 7 .   ? 43.81200  -15.55600 -2.24700 1.000 36.97000  ? 780 HOH A O   1 
HETATM 5852 O  O   . HOH FA 7 .   ? 23.48900  -25.17200 20.80300 1.000 36.18000  ? 781 HOH A O   1 
HETATM 5853 O  O   . HOH FA 7 .   ? 26.351    15.687    36.077   1.000 34.29000  ? 782 HOH A O   1 
HETATM 5854 O  O   . HOH FA 7 .   ? 21.52100  -7.92000  12.64600 1.000 36.96000  ? 783 HOH A O   1 
HETATM 5855 O  O   . HOH FA 7 .   ? 32.81000  -13.12400 40.44900 1.000 31.40000  ? 784 HOH A O   1 
HETATM 5856 O  O   . HOH FA 7 .   ? 37.94400  -6.49100  -3.40900 1.000 39.13000  ? 785 HOH A O   1 
HETATM 5857 O  O   . HOH FA 7 .   ? 21.48200  8.88700   2.56400  1.000 40.93000  ? 786 HOH A O   1 
HETATM 5858 O  O   . HOH FA 7 .   ? 53.54200  -8.22600  35.28400 1.000 33.29000  ? 787 HOH A O   1 
HETATM 5859 O  O   . HOH FA 7 .   ? 26.47600  7.97400   44.44000 1.000 46.43000  ? 788 HOH A O   1 
HETATM 5860 O  O   . HOH FA 7 .   ? 24.24000  9.59600   38.54300 1.000 33.38000  ? 789 HOH A O   1 
HETATM 5861 O  O   . HOH FA 7 .   ? 29.46900  7.81700   18.97900 1.000 26.72000  ? 790 HOH A O   1 
HETATM 5862 O  O   . HOH FA 7 .   ? 19.57800  4.38200   19.94100 1.000 37.54000  ? 791 HOH A O   1 
HETATM 5863 O  O   . HOH FA 7 .   ? 41.54500  -5.66300  -0.47000 1.000 30.98000  ? 792 HOH A O   1 
HETATM 5864 O  O   . HOH FA 7 .   ? 26.62700  -12.14000 -3.21300 1.000 34.89000  ? 793 HOH A O   1 
HETATM 5865 O  O   . HOH FA 7 .   ? 33.04200  -16.55400 39.32400 1.000 39.78000  ? 794 HOH A O   1 
HETATM 5866 O  O   . HOH FA 7 .   ? 18.65000  3.32600   36.01200 1.000 25.68000  ? 795 HOH A O   1 
HETATM 5867 O  O   . HOH FA 7 .   ? 19.20300  -9.77500  8.27500  1.000 33.01000  ? 796 HOH A O   1 
HETATM 5868 O  O   . HOH FA 7 .   ? 38.56100  -11.15400 -3.68700 1.000 35.78000  ? 797 HOH A O   1 
HETATM 5869 O  O   . HOH FA 7 .   ? 20.84200  -9.72300  11.41500 1.000 34.69000  ? 798 HOH A O   1 
HETATM 5870 O  O   . HOH FA 7 .   ? 30.39700  8.17200   16.39700 1.000 39.53000  ? 799 HOH A O   1 
HETATM 5871 O  O   . HOH FA 7 .   ? 26.16500  -2.21300  15.86000 1.000 41.24000  ? 800 HOH A O   1 
HETATM 5872 O  O   . HOH FA 7 .   ? 38.49500  -2.20400  -2.16100 1.000 36.03000  ? 801 HOH A O   1 
HETATM 5873 O  O   . HOH FA 7 .   ? 42.09600  7.25000   12.75400 1.000 40.00000  ? 802 HOH A O   1 
HETATM 5874 O  O   . HOH FA 7 .   ? 37.77800  -13.22700 -5.31900 1.000 43.47000  ? 803 HOH A O   1 
HETATM 5875 O  O   . HOH FA 7 .   ? 26.87400  -4.32100  17.36900 1.000 44.43000  ? 804 HOH A O   1 
HETATM 5876 O  O   . HOH FA 7 .   ? 19.91300  -24.62400 16.49200 1.000 34.10000  ? 805 HOH A O   1 
HETATM 5877 O  O   . HOH FA 7 .   ? 23.52700  -26.65800 18.73500 1.000 32.79000  ? 806 HOH A O   1 
HETATM 5878 O  O   . HOH FA 7 .   ? 52.87700  4.92100   25.29700 1.000 38.26000  ? 807 HOH A O   1 
HETATM 5879 O  O   . HOH FA 7 .   ? 41.67800  -7.76600  -3.07100 1.000 38.76000  ? 808 HOH A O   1 
HETATM 5880 O  O   . HOH GA 7 .   ? 10.76400  10.76100  16.68500 0.700 28.75000  ? 501 HOH B O   1 
HETATM 5881 O  O   . HOH GA 7 .   ? -5.84500  9.29600   6.12600  1.000 37.31000  ? 502 HOH B O   1 
HETATM 5882 O  O   . HOH GA 7 .   ? 13.06000  33.99700  21.53400 1.000 37.55000  ? 503 HOH B O   1 
HETATM 5883 O  O   . HOH GA 7 .   ? 4.67500   -7.96200  49.17600 1.000 36.47000  ? 504 HOH B O   1 
HETATM 5884 O  O   . HOH GA 7 .   ? -16.35900 20.78600  29.43700 1.000 29.86000  ? 505 HOH B O   1 
HETATM 5885 O  O   . HOH GA 7 .   ? -0.50400  19.96400  41.02300 1.000 36.51000  ? 506 HOH B O   1 
HETATM 5886 O  O   . HOH GA 7 .   ? -6.11800  -3.58100  13.07400 1.000 38.73000  ? 507 HOH B O   1 
HETATM 5887 O  O   . HOH GA 7 .   ? 15.24500  19.22600  35.29700 1.000 31.02000  ? 508 HOH B O   1 
HETATM 5888 O  O   . HOH GA 7 .   ? -12.35500 11.98200  9.19800  1.000 37.50000  ? 509 HOH B O   1 
HETATM 5889 O  O   . HOH GA 7 .   ? 16.70700  17.02700  -1.31400 1.000 32.89000  ? 510 HOH B O   1 
HETATM 5890 O  O   . HOH GA 7 .   ? 5.97900   3.91900   7.98300  1.000 22.09000  ? 511 HOH B O   1 
HETATM 5891 O  O   . HOH GA 7 .   ? -11.32500 8.45300   35.31400 1.000 23.93000  ? 512 HOH B O   1 
HETATM 5892 O  O   . HOH GA 7 .   ? -14.32700 3.87100   33.56800 1.000 20.00000  ? 513 HOH B O   1 
HETATM 5893 O  O   . HOH GA 7 .   ? -4.35500  27.44700  23.81800 1.000 20.80000  ? 514 HOH B O   1 
HETATM 5894 O  O   . HOH GA 7 .   ? 10.55500  19.86900  -1.35800 1.000 30.43000  ? 515 HOH B O   1 
HETATM 5895 O  O   . HOH GA 7 .   ? 13.17900  25.57200  31.51500 1.000 26.73000  ? 516 HOH B O   1 
HETATM 5896 O  O   . HOH GA 7 .   ? 2.94400   -7.06000  15.21100 1.000 36.48000  ? 517 HOH B O   1 
HETATM 5897 O  O   . HOH GA 7 .   ? 11.13400  -11.68300 53.69600 1.000 38.88000  ? 518 HOH B O   1 
HETATM 5898 O  O   . HOH GA 7 .   ? -26.53600 15.89900  23.49300 1.000 42.12000  ? 519 HOH B O   1 
HETATM 5899 O  O   . HOH GA 7 .   ? -18.35200 2.29500   29.12000 1.000 31.87000  ? 520 HOH B O   1 
HETATM 5900 O  O   . HOH GA 7 .   ? 22.39100  -7.27000  35.08700 1.000 26.80000  ? 521 HOH B O   1 
HETATM 5901 O  O   . HOH GA 7 .   ? 3.62800   -0.98000  50.48800 1.000 34.26000  ? 522 HOH B O   1 
HETATM 5902 O  O   . HOH GA 7 .   ? 3.29600   14.85900  39.44000 1.000 22.86000  ? 523 HOH B O   1 
HETATM 5903 O  O   . HOH GA 7 .   ? 10.24900  17.36300  25.65100 1.000 17.51000  ? 524 HOH B O   1 
HETATM 5904 O  O   . HOH GA 7 .   ? 8.58100   36.12900  13.29000 1.000 36.62000  ? 525 HOH B O   1 
HETATM 5905 O  O   . HOH GA 7 .   ? 18.53700  -7.57400  23.64600 1.000 30.38000  ? 526 HOH B O   1 
HETATM 5906 O  O   . HOH GA 7 .   ? 14.38800  -19.96800 11.52900 1.000 38.91000  ? 527 HOH B O   1 
HETATM 5907 O  O   . HOH GA 7 .   ? 5.35500   40.67300  14.44100 1.000 44.58000  ? 528 HOH B O   1 
HETATM 5908 O  O   . HOH GA 7 .   ? 12.43400  -14.90000 21.64000 1.000 29.76000  ? 529 HOH B O   1 
HETATM 5909 O  O   . HOH GA 7 .   ? 15.30400  14.29400  17.39600 1.000 35.46000  ? 530 HOH B O   1 
HETATM 5910 O  O   . HOH GA 7 .   ? -11.13700 7.73000   39.43400 1.000 30.16000  ? 531 HOH B O   1 
HETATM 5911 O  O   . HOH GA 7 .   ? 6.43700   -9.83900  44.21400 1.000 33.07000  ? 532 HOH B O   1 
HETATM 5912 O  O   . HOH GA 7 .   ? -18.58800 19.12500  22.13000 1.000 33.05000  ? 533 HOH B O   1 
HETATM 5913 O  O   . HOH GA 7 .   ? -8.70400  33.33100  9.94300  1.000 36.07000  ? 534 HOH B O   1 
HETATM 5914 O  O   . HOH GA 7 .   ? 3.97200   -12.67000 21.37700 1.000 37.37000  ? 535 HOH B O   1 
HETATM 5915 O  O   . HOH GA 7 .   ? 11.16000  21.33500  2.12000  1.000 26.80000  ? 536 HOH B O   1 
HETATM 5916 O  O   . HOH GA 7 .   ? 2.47000   23.22900  40.39700 1.000 29.20000  ? 537 HOH B O   1 
HETATM 5917 O  O   . HOH GA 7 .   ? -6.68800  33.12600  23.18900 1.000 20.11000  ? 538 HOH B O   1 
HETATM 5918 O  O   . HOH GA 7 .   ? 6.35100   -0.87900  41.08000 1.000 19.11000  ? 539 HOH B O   1 
HETATM 5919 O  O   . HOH GA 7 .   ? 7.83500   19.84100  37.89000 1.000 26.57000  ? 540 HOH B O   1 
HETATM 5920 O  O   . HOH GA 7 .   ? 25.76300  -8.33900  26.98400 1.000 18.30000  ? 541 HOH B O   1 
HETATM 5921 O  O   . HOH GA 7 .   ? 21.69800  -21.30000 27.78900 1.000 31.96000  ? 542 HOH B O   1 
HETATM 5922 O  O   . HOH GA 7 .   ? 12.05000  -5.87200  17.50900 1.000 27.90000  ? 543 HOH B O   1 
HETATM 5923 O  O   . HOH GA 7 .   ? -5.77200  14.66600  40.68900 1.000 35.25000  ? 544 HOH B O   1 
HETATM 5924 O  O   . HOH GA 7 .   ? -13.56100 24.08500  20.44900 1.000 26.96000  ? 545 HOH B O   1 
HETATM 5925 O  O   . HOH GA 7 .   ? 5.50500   1.42400   53.96500 1.000 24.96000  ? 546 HOH B O   1 
HETATM 5926 O  O   . HOH GA 7 .   ? 11.56700  8.98900   45.36500 1.000 40.24000  ? 547 HOH B O   1 
HETATM 5927 O  O   . HOH GA 7 .   ? -10.69700 26.80100  23.77700 1.000 34.72000  ? 548 HOH B O   1 
HETATM 5928 O  O   . HOH GA 7 .   ? -18.15400 23.94300  22.93700 1.000 33.84000  ? 549 HOH B O   1 
HETATM 5929 O  O   . HOH GA 7 .   ? -15.33800 9.26300   30.54300 1.000 24.97000  ? 550 HOH B O   1 
HETATM 5930 O  O   . HOH GA 7 .   ? -7.99800  14.96500  3.75000  1.000 29.64000  ? 551 HOH B O   1 
HETATM 5931 O  O   . HOH GA 7 .   ? -7.49200  27.82200  3.31900  1.000 33.15000  ? 552 HOH B O   1 
HETATM 5932 O  O   . HOH GA 7 .   ? -9.07700  24.83700  3.14500  1.000 38.25000  ? 553 HOH B O   1 
HETATM 5933 O  O   . HOH GA 7 .   ? 17.39000  -6.32800  44.09200 1.000 40.78000  ? 554 HOH B O   1 
HETATM 5934 O  O   . HOH GA 7 .   ? 12.54300  1.77000   44.96800 1.000 20.13000  ? 555 HOH B O   1 
HETATM 5935 O  O   . HOH GA 7 .   ? -12.73000 24.76600  10.36600 1.000 28.91000  ? 556 HOH B O   1 
HETATM 5936 O  O   . HOH GA 7 .   ? 7.17800   -7.24500  47.56600 1.000 29.64000  ? 557 HOH B O   1 
HETATM 5937 O  O   . HOH GA 7 .   ? 18.70300  16.28400  5.19400  1.000 32.96000  ? 558 HOH B O   1 
HETATM 5938 O  O   . HOH GA 7 .   ? -11.52300 2.38800   25.84800 1.000 18.66000  ? 559 HOH B O   1 
HETATM 5939 O  O   . HOH GA 7 .   ? 5.90300   -3.28300  12.07700 1.000 27.57000  ? 560 HOH B O   1 
HETATM 5940 O  O   . HOH GA 7 .   ? -9.14300  -3.95900  33.26400 1.000 22.94000  ? 561 HOH B O   1 
HETATM 5941 O  O   . HOH GA 7 .   ? 17.12200  6.70600   22.61100 1.000 27.34000  ? 562 HOH B O   1 
HETATM 5942 O  O   . HOH GA 7 .   ? -9.64800  30.44200  20.86300 1.000 32.05000  ? 563 HOH B O   1 
HETATM 5943 O  O   . HOH GA 7 .   ? 8.34300   15.18400  39.80400 1.000 33.84000  ? 564 HOH B O   1 
HETATM 5944 O  O   . HOH GA 7 .   ? 19.37200  -0.40200  32.99900 1.000 13.73000  ? 565 HOH B O   1 
HETATM 5945 O  O   . HOH GA 7 .   ? 6.44500   17.81100  20.49600 1.000 19.30000  ? 566 HOH B O   1 
HETATM 5946 O  O   . HOH GA 7 .   ? 12.14300  17.83000  -0.51200 1.000 33.01000  ? 567 HOH B O   1 
HETATM 5947 O  O   . HOH GA 7 .   ? 19.23900  4.22500   24.22900 1.000 26.85000  ? 568 HOH B O   1 
HETATM 5948 O  O   . HOH GA 7 .   ? 1.09000   28.38200  -0.52700 1.000 34.26000  ? 569 HOH B O   1 
HETATM 5949 O  O   . HOH GA 7 .   ? 8.19900   -12.54700 27.65100 1.000 31.57000  ? 570 HOH B O   1 
HETATM 5950 O  O   . HOH GA 7 .   ? -12.97400 -3.23100  28.03000 1.000 31.93000  ? 571 HOH B O   1 
HETATM 5951 O  O   . HOH GA 7 .   ? 17.66900  1.57700   32.24100 1.000 15.94000  ? 572 HOH B O   1 
HETATM 5952 O  O   . HOH GA 7 .   ? 5.24400   36.47700  23.10300 1.000 22.49000  ? 573 HOH B O   1 
HETATM 5953 O  O   . HOH GA 7 .   ? -6.62300  30.48100  22.67900 1.000 31.31000  ? 574 HOH B O   1 
HETATM 5954 O  O   . HOH GA 7 .   ? 16.49300  10.00400  35.43100 1.000 23.45000  ? 575 HOH B O   1 
HETATM 5955 O  O   . HOH GA 7 .   ? 4.80700   32.48000  2.42800  1.000 39.20000  ? 576 HOH B O   1 
HETATM 5956 O  O   B HOH GA 7 .   ? 8.83000   16.62400  18.91700 0.300 15.97000  ? 577 HOH B O   1 
HETATM 5957 O  O   . HOH GA 7 .   ? -13.59800 6.72300   19.62000 1.000 26.97000  ? 578 HOH B O   1 
HETATM 5958 O  O   . HOH GA 7 .   ? 14.50200  27.05700  12.87500 1.000 30.34000  ? 579 HOH B O   1 
HETATM 5959 O  O   . HOH GA 7 .   ? -11.66400 16.50300  4.21100  1.000 36.48000  ? 580 HOH B O   1 
HETATM 5960 O  O   . HOH GA 7 .   ? 3.66700   16.82600  14.15400 1.000 19.89000  ? 581 HOH B O   1 
HETATM 5961 O  O   . HOH GA 7 .   ? -10.58600 0.16700   27.33300 1.000 21.56000  ? 582 HOH B O   1 
HETATM 5962 O  O   . HOH GA 7 .   ? 8.21800   33.12300  7.16400  1.000 36.54000  ? 583 HOH B O   1 
HETATM 5963 O  O   . HOH GA 7 .   ? -8.27100  18.45700  3.12100  1.000 31.54000  ? 584 HOH B O   1 
HETATM 5964 O  O   . HOH GA 7 .   ? 11.17200  10.98900  26.22100 1.000 15.81000  ? 585 HOH B O   1 
HETATM 5965 O  O   . HOH GA 7 .   ? 10.05600  10.37600  9.45700  1.000 18.67000  ? 586 HOH B O   1 
HETATM 5966 O  O   . HOH GA 7 .   ? 5.85200   5.19100   45.15700 1.000 29.90000  ? 587 HOH B O   1 
HETATM 5967 O  O   . HOH GA 7 .   ? -17.15900 3.92900   33.06800 1.000 28.69000  ? 588 HOH B O   1 
HETATM 5968 O  O   . HOH GA 7 .   ? -17.78500 17.65300  20.12400 1.000 37.11000  ? 589 HOH B O   1 
HETATM 5969 O  O   . HOH GA 7 .   ? -0.13100  17.95200  -1.78800 1.000 26.18000  ? 590 HOH B O   1 
HETATM 5970 O  O   . HOH GA 7 .   ? -7.25000  35.72700  11.18600 1.000 25.21000  ? 591 HOH B O   1 
HETATM 5971 O  O   . HOH GA 7 .   ? 8.91000   31.13800  8.87300  1.000 34.74000  ? 592 HOH B O   1 
HETATM 5972 O  O   . HOH GA 7 .   ? 24.29400  10.28600  -0.83300 1.000 35.24000  ? 593 HOH B O   1 
HETATM 5973 O  O   . HOH GA 7 .   ? -8.12600  3.22200   18.55900 1.000 25.05000  ? 594 HOH B O   1 
HETATM 5974 O  O   . HOH GA 7 .   ? -2.38200  29.71700  32.60500 1.000 34.96000  ? 595 HOH B O   1 
HETATM 5975 O  O   . HOH GA 7 .   ? -15.39100 18.29100  19.18600 1.000 25.64000  ? 596 HOH B O   1 
HETATM 5976 O  O   . HOH GA 7 .   ? -16.42100 5.44700   26.46900 1.000 23.17000  ? 597 HOH B O   1 
HETATM 5977 O  O   . HOH GA 7 .   ? 12.54400  18.23100  12.07500 1.000 22.00000  ? 598 HOH B O   1 
HETATM 5978 O  O   . HOH GA 7 .   ? -8.43100  3.52100   14.77100 1.000 30.58000  ? 599 HOH B O   1 
HETATM 5979 O  O   . HOH GA 7 .   ? 14.05200  15.20800  32.91600 1.000 24.25000  ? 600 HOH B O   1 
HETATM 5980 O  O   . HOH GA 7 .   ? 13.78100  -6.97600  38.66000 1.000 26.22000  ? 601 HOH B O   1 
HETATM 5981 O  O   . HOH GA 7 .   ? 21.42400  -17.55000 7.00900  1.000 31.66000  ? 602 HOH B O   1 
HETATM 5982 O  O   . HOH GA 7 .   ? 25.60600  -9.59400  29.53100 1.000 18.26000  ? 603 HOH B O   1 
HETATM 5983 O  O   . HOH GA 7 .   ? -8.75200  25.03600  10.32600 1.000 22.82000  ? 604 HOH B O   1 
HETATM 5984 O  O   . HOH GA 7 .   ? 2.66800   7.51200   0.86200  1.000 26.36000  ? 605 HOH B O   1 
HETATM 5985 O  O   . HOH GA 7 .   ? 6.52200   26.88400  31.68100 1.000 18.43000  ? 606 HOH B O   1 
HETATM 5986 O  O   . HOH GA 7 .   ? -15.05500 0.92400   39.14000 1.000 35.44000  ? 607 HOH B O   1 
HETATM 5987 O  O   . HOH GA 7 .   ? 12.64000  -14.65100 18.29300 1.000 29.55000  ? 608 HOH B O   1 
HETATM 5988 O  O   . HOH GA 7 .   ? 1.26100   19.64900  17.31100 1.000 26.17000  ? 609 HOH B O   1 
HETATM 5989 O  O   . HOH GA 7 .   ? 20.30900  -10.83400 23.27000 1.000 24.67000  ? 610 HOH B O   1 
HETATM 5990 O  O   . HOH GA 7 .   ? 14.70000  -12.04100 29.23800 1.000 20.78000  ? 611 HOH B O   1 
HETATM 5991 O  O   . HOH GA 7 .   ? -0.22600  27.17500  34.56700 1.000 38.55000  ? 612 HOH B O   1 
HETATM 5992 O  O   . HOH GA 7 .   ? 12.84100  14.01700  7.15100  1.000 22.85000  ? 613 HOH B O   1 
HETATM 5993 O  O   . HOH GA 7 .   ? 5.27300   -5.83700  46.17800 1.000 28.16000  ? 614 HOH B O   1 
HETATM 5994 O  O   . HOH GA 7 .   ? -1.04500  35.35800  21.65000 1.000 23.13000  ? 615 HOH B O   1 
HETATM 5995 O  O   . HOH GA 7 .   ? -16.16800 1.47100   26.11300 1.000 34.47000  ? 616 HOH B O   1 
HETATM 5996 O  O   . HOH GA 7 .   ? 14.06100  24.62900  7.39300  1.000 30.47000  ? 617 HOH B O   1 
HETATM 5997 O  O   . HOH GA 7 .   ? -13.49200 10.79900  32.15800 1.000 18.43000  ? 618 HOH B O   1 
HETATM 5998 O  O   . HOH GA 7 .   ? -14.70900 17.55700  31.41800 1.000 45.45000  ? 619 HOH B O   1 
HETATM 5999 O  O   . HOH GA 7 .   ? 24.80800  -12.13300 32.16400 1.000 24.08000  ? 620 HOH B O   1 
HETATM 6000 O  O   . HOH GA 7 .   ? 7.92100   -1.41200  47.39000 1.000 26.86000  ? 621 HOH B O   1 
HETATM 6001 O  O   . HOH GA 7 .   ? 10.23000  26.95800  33.57500 1.000 29.82000  ? 622 HOH B O   1 
HETATM 6002 O  O   . HOH GA 7 .   ? 13.09700  27.27700  19.19900 1.000 21.07000  ? 623 HOH B O   1 
HETATM 6003 O  O   . HOH GA 7 .   ? 3.82500   16.04800  11.47200 1.000 21.41000  ? 624 HOH B O   1 
HETATM 6004 O  O   . HOH GA 7 .   ? 14.02900  -18.98900 15.00000 1.000 31.33000  ? 625 HOH B O   1 
HETATM 6005 O  O   . HOH GA 7 .   ? 13.44500  -8.83500  46.20500 1.000 34.41000  ? 626 HOH B O   1 
HETATM 6006 O  O   . HOH GA 7 .   ? 21.01100  7.84300   -6.74300 1.000 38.02000  ? 627 HOH B O   1 
HETATM 6007 O  O   . HOH GA 7 .   ? -3.06600  -3.13300  13.93100 1.000 27.65000  ? 628 HOH B O   1 
HETATM 6008 O  O   . HOH GA 7 .   ? 12.16700  13.41800  38.65000 1.000 26.18000  ? 629 HOH B O   1 
HETATM 6009 O  O   . HOH GA 7 .   ? -4.58100  22.45300  -0.05600 1.000 28.31000  ? 630 HOH B O   1 
HETATM 6010 O  O   . HOH GA 7 .   ? -15.91000 -1.94100  27.03000 1.000 37.57000  ? 631 HOH B O   1 
HETATM 6011 O  O   . HOH GA 7 .   ? -5.23900  18.70000  3.40200  1.000 35.50000  ? 632 HOH B O   1 
HETATM 6012 O  O   . HOH GA 7 .   ? 14.09400  8.22400   19.91800 1.000 29.00000  ? 633 HOH B O   1 
HETATM 6013 O  O   . HOH GA 7 .   ? 15.91800  -18.03700 26.40300 1.000 28.84000  ? 634 HOH B O   1 
HETATM 6014 O  O   . HOH GA 7 .   ? -6.05300  -6.40400  34.77200 1.000 32.33000  ? 635 HOH B O   1 
HETATM 6015 O  O   . HOH GA 7 .   ? 14.83900  -8.78700  43.42300 1.000 40.04000  ? 636 HOH B O   1 
HETATM 6016 O  O   . HOH GA 7 .   ? 15.57300  8.39400   11.71400 1.000 38.71000  ? 637 HOH B O   1 
HETATM 6017 O  O   . HOH GA 7 .   ? 9.97500   -8.44600  16.69800 1.000 29.03000  ? 638 HOH B O   1 
HETATM 6018 O  O   . HOH GA 7 .   ? 12.98900  16.39900  13.98300 1.000 22.37000  ? 639 HOH B O   1 
HETATM 6019 O  O   . HOH GA 7 .   ? 9.70200   26.98800  -0.55600 1.000 29.16000  ? 640 HOH B O   1 
HETATM 6020 O  O   . HOH GA 7 .   ? 6.72500   24.11200  20.95700 1.000 18.73000  ? 641 HOH B O   1 
HETATM 6021 O  O   . HOH GA 7 .   ? -3.64400  29.07800  21.65400 1.000 18.92000  ? 642 HOH B O   1 
HETATM 6022 O  O   . HOH GA 7 .   ? 14.07400  -17.18200 46.22900 1.000 44.67000  ? 643 HOH B O   1 
HETATM 6023 O  O   . HOH GA 7 .   ? 10.49600  32.13200  4.85300  1.000 38.90000  ? 644 HOH B O   1 
HETATM 6024 O  O   . HOH GA 7 .   ? -21.16000 17.90400  22.59400 1.000 37.72000  ? 645 HOH B O   1 
HETATM 6025 O  O   . HOH GA 7 .   ? 18.67200  9.18100   2.06000  1.000 32.43000  ? 646 HOH B O   1 
HETATM 6026 O  O   . HOH GA 7 .   ? 9.17300   -4.20100  41.50700 1.000 20.90000  ? 647 HOH B O   1 
HETATM 6027 O  O   . HOH GA 7 .   ? -8.40600  6.92000   7.82400  1.000 30.83000  ? 648 HOH B O   1 
HETATM 6028 O  O   . HOH GA 7 .   ? 8.97200   3.70900   15.71100 1.000 26.83000  ? 649 HOH B O   1 
HETATM 6029 O  O   . HOH GA 7 .   ? -1.43700  13.40300  37.00900 1.000 20.44000  ? 650 HOH B O   1 
HETATM 6030 O  O   . HOH GA 7 .   ? 9.22500   -4.03000  20.52100 1.000 17.44000  ? 651 HOH B O   1 
HETATM 6031 O  O   . HOH GA 7 .   ? 11.63700  4.82000   14.24500 1.000 40.36000  ? 652 HOH B O   1 
HETATM 6032 O  O   . HOH GA 7 .   ? 9.09100   9.50300   0.95200  1.000 28.80000  ? 653 HOH B O   1 
HETATM 6033 O  O   . HOH GA 7 .   ? 11.05400  -11.86500 22.89800 1.000 29.59000  ? 654 HOH B O   1 
HETATM 6034 O  O   . HOH GA 7 .   ? 16.89300  26.90100  18.49000 1.000 29.68000  ? 655 HOH B O   1 
HETATM 6035 O  O   . HOH GA 7 .   ? -10.59300 30.13300  14.95300 1.000 31.86000  ? 656 HOH B O   1 
HETATM 6036 O  O   . HOH GA 7 .   ? 6.25200   22.99000  42.79800 1.000 37.54000  ? 657 HOH B O   1 
HETATM 6037 O  O   . HOH GA 7 .   ? 9.97400   12.32200  41.04300 1.000 29.82000  ? 658 HOH B O   1 
HETATM 6038 O  O   . HOH GA 7 .   ? -19.11900 7.90200   34.65700 1.000 33.83000  ? 659 HOH B O   1 
HETATM 6039 O  O   . HOH GA 7 .   ? 3.24500   3.47600   45.13900 1.000 31.57000  ? 660 HOH B O   1 
HETATM 6040 O  O   . HOH GA 7 .   ? 7.53600   -6.59200  53.37700 1.000 39.88000  ? 661 HOH B O   1 
HETATM 6041 O  O   . HOH GA 7 .   ? 8.41500   20.64400  20.29600 1.000 18.79000  ? 662 HOH B O   1 
HETATM 6042 O  O   . HOH GA 7 .   ? 0.73700   -1.22000  9.20000  1.000 28.06000  ? 663 HOH B O   1 
HETATM 6043 O  O   . HOH GA 7 .   ? -6.30800  30.57800  30.37300 1.000 38.67000  ? 664 HOH B O   1 
HETATM 6044 O  O   . HOH GA 7 .   ? 3.30500   31.55600  28.19800 1.000 28.03000  ? 665 HOH B O   1 
HETATM 6045 O  O   . HOH GA 7 .   ? 14.53800  26.99700  28.05800 1.000 36.24000  ? 666 HOH B O   1 
HETATM 6046 O  O   . HOH GA 7 .   ? 8.01400   37.82400  19.58500 1.000 32.57000  ? 667 HOH B O   1 
HETATM 6047 O  O   . HOH GA 7 .   ? 3.87700   27.45000  31.12200 1.000 19.15000  ? 668 HOH B O   1 
HETATM 6048 O  O   . HOH GA 7 .   ? 7.15200   1.55200   15.08100 1.000 22.76000  ? 669 HOH B O   1 
HETATM 6049 O  O   . HOH GA 7 .   ? -7.411    36.274    15.152   1.000 21.08000  ? 670 HOH B O   1 
HETATM 6050 O  O   . HOH GA 7 .   ? 1.77000   -10.98700 22.34300 1.000 29.95000  ? 671 HOH B O   1 
HETATM 6051 O  O   . HOH GA 7 .   ? 16.58900  20.46500  6.25500  1.000 30.15000  ? 672 HOH B O   1 
HETATM 6052 O  O   . HOH GA 7 .   ? 16.45500  12.53900  20.19000 1.000 33.94000  ? 673 HOH B O   1 
HETATM 6053 O  O   . HOH GA 7 .   ? 18.02300  9.16800   4.43700  1.000 31.79000  ? 674 HOH B O   1 
HETATM 6054 O  O   . HOH GA 7 .   ? 2.91600   -3.95300  43.77600 1.000 34.50000  ? 675 HOH B O   1 
HETATM 6055 O  O   . HOH GA 7 .   ? 15.54900  -21.52200 17.17200 1.000 27.81000  ? 676 HOH B O   1 
HETATM 6056 O  O   . HOH GA 7 .   ? -5.60700  1.94500   42.29900 1.000 31.95000  ? 677 HOH B O   1 
HETATM 6057 O  O   . HOH GA 7 .   ? 20.90500  -16.39700 34.30800 1.000 37.35000  ? 678 HOH B O   1 
HETATM 6058 O  O   . HOH GA 7 .   ? 4.59300   -11.45700 28.41000 1.000 17.91000  ? 679 HOH B O   1 
HETATM 6059 O  O   . HOH GA 7 .   ? 6.86200   25.58400  -1.19800 1.000 38.74000  ? 680 HOH B O   1 
HETATM 6060 O  O   . HOH GA 7 .   ? 23.05600  6.40600   -1.09000 1.000 30.34000  ? 681 HOH B O   1 
HETATM 6061 O  O   . HOH GA 7 .   ? 13.55300  9.31200   38.92800 1.000 27.80000  ? 682 HOH B O   1 
HETATM 6062 O  O   . HOH GA 7 .   ? -11.80300 22.02100  16.80500 1.000 32.30000  ? 683 HOH B O   1 
HETATM 6063 O  O   . HOH GA 7 .   ? 9.64700   -13.55100 19.97500 1.000 33.88000  ? 684 HOH B O   1 
HETATM 6064 O  O   . HOH GA 7 .   ? 13.85300  26.81200  21.90500 1.000 33.28000  ? 685 HOH B O   1 
HETATM 6065 O  O   . HOH GA 7 .   ? 12.59300  25.54600  5.29200  1.000 31.97000  ? 686 HOH B O   1 
HETATM 6066 O  O   . HOH GA 7 .   ? 19.38800  -13.08200 22.40900 1.000 22.04000  ? 687 HOH B O   1 
HETATM 6067 O  O   . HOH GA 7 .   ? 23.17000  -13.60000 33.62300 1.000 22.96000  ? 688 HOH B O   1 
HETATM 6068 O  O   . HOH GA 7 .   ? 15.76400  -11.08600 15.24700 1.000 33.39000  ? 689 HOH B O   1 
HETATM 6069 O  O   . HOH GA 7 .   ? -2.07200  32.89200  6.01500  1.000 33.58000  ? 690 HOH B O   1 
HETATM 6070 O  O   . HOH GA 7 .   ? 8.31200   7.60500   46.90500 1.000 24.63000  ? 691 HOH B O   1 
HETATM 6071 O  O   . HOH GA 7 .   ? 1.87100   29.61400  36.13000 1.000 32.28000  ? 692 HOH B O   1 
HETATM 6072 O  O   . HOH GA 7 .   ? 16.22500  2.80800   20.65000 1.000 18.73000  ? 693 HOH B O   1 
HETATM 6073 O  O   . HOH GA 7 .   ? -7.67300  17.98900  36.87400 1.000 31.23000  ? 694 HOH B O   1 
HETATM 6074 O  O   . HOH GA 7 .   ? 14.56800  -11.52800 33.72800 1.000 30.82000  ? 695 HOH B O   1 
HETATM 6075 O  O   . HOH GA 7 .   ? 18.29100  15.31100  -2.69300 1.000 37.79000  ? 696 HOH B O   1 
HETATM 6076 O  O   . HOH GA 7 .   ? -1.81000  12.74300  1.38000  1.000 30.86000  ? 697 HOH B O   1 
HETATM 6077 O  O   . HOH GA 7 .   ? 5.67100   4.89000   16.49700 1.000 21.19000  ? 698 HOH B O   1 
HETATM 6078 O  O   . HOH GA 7 .   ? -11.14100 16.72600  29.14700 1.000 23.30000  ? 699 HOH B O   1 
HETATM 6079 O  O   . HOH GA 7 .   ? 5.71600   6.53200   0.38800  1.000 35.60000  ? 700 HOH B O   1 
HETATM 6080 O  O   . HOH GA 7 .   ? 13.68200  19.26800  37.56700 1.000 37.30000  ? 701 HOH B O   1 
HETATM 6081 O  O   . HOH GA 7 .   ? -19.17200 8.35400   25.84000 1.000 25.60000  ? 702 HOH B O   1 
HETATM 6082 O  O   . HOH GA 7 .   ? 17.81100  28.11000  14.94500 1.000 31.11000  ? 703 HOH B O   1 
HETATM 6083 O  O   . HOH GA 7 .   ? 9.17700   -4.32600  53.95500 1.000 27.02000  ? 704 HOH B O   1 
HETATM 6084 O  O   . HOH GA 7 .   ? -12.38200 26.29900  27.18900 1.000 31.00000  ? 705 HOH B O   1 
HETATM 6085 O  O   . HOH GA 7 .   ? -16.32200 12.67000  30.06600 1.000 32.25000  ? 706 HOH B O   1 
HETATM 6086 O  O   . HOH GA 7 .   ? 17.11200  1.07300   39.52100 1.000 22.67000  ? 707 HOH B O   1 
HETATM 6087 O  O   . HOH GA 7 .   ? -7.86700  2.08900   41.34500 1.000 33.06000  ? 708 HOH B O   1 
HETATM 6088 O  O   . HOH GA 7 .   ? 6.57300   13.86400  30.72200 1.000 23.43000  ? 709 HOH B O   1 
HETATM 6089 O  O   . HOH GA 7 .   ? 17.89200  2.90500   6.70300  1.000 36.70000  ? 710 HOH B O   1 
HETATM 6090 O  O   . HOH GA 7 .   ? -9.65800  29.09600  3.75100  1.000 36.35000  ? 711 HOH B O   1 
HETATM 6091 O  O   . HOH GA 7 .   ? -12.36700 15.81200  8.26200  1.000 31.21000  ? 712 HOH B O   1 
HETATM 6092 O  O   . HOH GA 7 .   ? -2.83900  10.76700  43.16300 1.000 33.53000  ? 713 HOH B O   1 
HETATM 6093 O  O   . HOH GA 7 .   ? -9.94500  19.42500  30.43700 1.000 36.95000  ? 714 HOH B O   1 
HETATM 6094 O  O   . HOH GA 7 .   ? 6.05900   34.04100  24.33700 1.000 28.65000  ? 715 HOH B O   1 
HETATM 6095 O  O   . HOH GA 7 .   ? 0.94300   34.60600  1.72800  1.000 42.84000  ? 716 HOH B O   1 
HETATM 6096 O  O   . HOH GA 7 .   ? 3.85700   8.55300   16.24600 1.000 19.41000  ? 717 HOH B O   1 
HETATM 6097 O  O   . HOH GA 7 .   ? 10.07300  -6.31100  39.84900 1.000 17.88000  ? 718 HOH B O   1 
HETATM 6098 O  O   . HOH GA 7 .   ? 15.50500  -0.05400  19.88500 1.000 21.21000  ? 719 HOH B O   1 
HETATM 6099 O  O   . HOH GA 7 .   ? -9.30900  25.58400  14.84700 1.000 30.12000  ? 720 HOH B O   1 
HETATM 6100 O  O   . HOH GA 7 .   ? 5.46500   29.42000  38.31300 1.000 33.38000  ? 721 HOH B O   1 
HETATM 6101 O  O   . HOH GA 7 .   ? 7.77700   1.15100   9.59800  1.000 33.71000  ? 722 HOH B O   1 
HETATM 6102 O  O   . HOH GA 7 .   ? 14.16600  28.06400  4.98600  1.000 40.38000  ? 723 HOH B O   1 
HETATM 6103 O  O   . HOH GA 7 .   ? -3.17600  11.50700  3.32100  1.000 28.50000  ? 724 HOH B O   1 
HETATM 6104 O  O   . HOH GA 7 .   ? 11.22200  -14.74400 27.12800 1.000 31.09000  ? 725 HOH B O   1 
HETATM 6105 O  O   . HOH GA 7 .   ? 19.26900  15.82700  10.36200 1.000 32.23000  ? 726 HOH B O   1 
HETATM 6106 O  O   . HOH GA 7 .   ? 23.09300  13.15200  -2.15800 1.000 39.73000  ? 727 HOH B O   1 
HETATM 6107 O  O   . HOH GA 7 .   ? -10.01000 13.89000  7.15400  1.000 26.23000  ? 728 HOH B O   1 
HETATM 6108 O  O   . HOH GA 7 .   ? 0.22600   -2.41300  45.27300 1.000 43.78000  ? 729 HOH B O   1 
HETATM 6109 O  O   . HOH GA 7 .   ? 17.73700  -2.31400  41.57900 1.000 37.70000  ? 730 HOH B O   1 
HETATM 6110 O  O   . HOH GA 7 .   ? 15.73700  5.32700   37.08200 1.000 31.42000  ? 731 HOH B O   1 
HETATM 6111 O  O   . HOH GA 7 .   ? -2.23100  25.69700  35.02700 1.000 36.77000  ? 732 HOH B O   1 
HETATM 6112 O  O   . HOH GA 7 .   ? 17.10000  -2.06000  20.47600 1.000 30.10000  ? 733 HOH B O   1 
HETATM 6113 O  O   . HOH GA 7 .   ? 20.43000  -3.11500  36.36400 1.000 34.26000  ? 734 HOH B O   1 
HETATM 6114 O  O   . HOH GA 7 .   ? -16.12500 16.46100  28.73300 1.000 30.41000  ? 735 HOH B O   1 
HETATM 6115 O  O   . HOH GA 7 .   ? -9.48000  27.50300  26.40300 1.000 30.62000  ? 736 HOH B O   1 
HETATM 6116 O  O   . HOH GA 7 .   ? 15.08400  22.48900  4.01900  1.000 36.52000  ? 737 HOH B O   1 
HETATM 6117 O  O   . HOH GA 7 .   ? 14.79700  12.45000  35.46400 1.000 27.51000  ? 738 HOH B O   1 
HETATM 6118 O  O   . HOH GA 7 .   ? 14.55600  27.43800  7.73100  1.000 33.68000  ? 739 HOH B O   1 
HETATM 6119 O  O   . HOH GA 7 .   ? -10.99400 -2.35200  20.96700 1.000 36.38000  ? 740 HOH B O   1 
HETATM 6120 O  O   . HOH GA 7 .   ? 13.15000  26.55400  24.43200 1.000 30.60000  ? 741 HOH B O   1 
HETATM 6121 O  O   . HOH GA 7 .   ? 5.11800   -7.47600  51.73700 1.000 42.77000  ? 742 HOH B O   1 
HETATM 6122 O  O   . HOH GA 7 .   ? -10.77200 -2.35900  26.48400 1.000 25.56000  ? 743 HOH B O   1 
HETATM 6123 O  O   . HOH GA 7 .   ? -20.57900 -3.18700  32.79000 1.000 36.01000  ? 744 HOH B O   1 
HETATM 6124 O  O   . HOH GA 7 .   ? 10.41700  15.91400  -1.59300 1.000 35.92000  ? 745 HOH B O   1 
HETATM 6125 O  O   . HOH GA 7 .   ? -14.66500 2.72800   19.91000 1.000 37.71000  ? 746 HOH B O   1 
HETATM 6126 O  O   . HOH GA 7 .   ? 11.79400  27.83100  26.01700 1.000 33.16000  ? 747 HOH B O   1 
HETATM 6127 O  O   . HOH GA 7 .   ? -12.81700 10.45900  36.59800 1.000 41.20000  ? 748 HOH B O   1 
HETATM 6128 O  O   . HOH GA 7 .   ? -5.42000  24.96300  -0.30000 1.000 33.16000  ? 749 HOH B O   1 
HETATM 6129 O  O   . HOH GA 7 .   ? 14.97000  8.07000   37.49400 1.000 33.73000  ? 750 HOH B O   1 
HETATM 6130 O  O   . HOH GA 7 .   ? 0.60300   3.77200   42.59300 1.000 31.23000  ? 751 HOH B O   1 
HETATM 6131 O  O   . HOH GA 7 .   ? -4.98800  16.84000  1.47400  1.000 35.40000  ? 752 HOH B O   1 
HETATM 6132 O  O   . HOH GA 7 .   ? 0.94300   37.29700  9.48200  1.000 45.90000  ? 753 HOH B O   1 
HETATM 6133 O  O   . HOH GA 7 .   ? 1.87000   13.66900  41.55600 1.000 37.82000  ? 754 HOH B O   1 
HETATM 6134 O  O   . HOH GA 7 .   ? -2.58400  15.39900  0.54500  1.000 29.96000  ? 755 HOH B O   1 
HETATM 6135 O  O   . HOH GA 7 .   ? 12.58600  24.05200  2.78600  1.000 37.23000  ? 756 HOH B O   1 
HETATM 6136 O  O   . HOH GA 7 .   ? 19.00100  13.80300  7.00300  1.000 26.23000  ? 757 HOH B O   1 
HETATM 6137 O  O   . HOH GA 7 .   ? -1.41100  4.49600   43.95900 1.000 38.79000  ? 758 HOH B O   1 
HETATM 6138 O  O   . HOH GA 7 .   ? 1.02700   10.65400  -1.94700 1.000 37.56000  ? 759 HOH B O   1 
HETATM 6139 O  O   . HOH GA 7 .   ? 8.40500   -4.90300  15.65400 1.000 34.91000  ? 760 HOH B O   1 
HETATM 6140 O  O   . HOH GA 7 .   ? -13.76000 22.01800  18.45500 1.000 35.77000  ? 761 HOH B O   1 
HETATM 6141 O  O   . HOH GA 7 .   ? -7.39700  10.50500  4.78100  1.000 31.82000  ? 762 HOH B O   1 
HETATM 6142 O  O   . HOH GA 7 .   ? 9.52400   1.55700   11.60400 1.000 38.85000  ? 763 HOH B O   1 
HETATM 6143 O  O   . HOH GA 7 .   ? -10.28000 23.13100  12.22900 1.000 37.60000  ? 764 HOH B O   1 
HETATM 6144 O  O   . HOH GA 7 .   ? -12.27200 33.26300  15.07000 1.000 30.83000  ? 765 HOH B O   1 
HETATM 6145 O  O   . HOH GA 7 .   ? 7.32600   -2.73100  43.22000 1.000 27.51000  ? 766 HOH B O   1 
HETATM 6146 O  O   . HOH GA 7 .   ? 16.17200  -12.83200 32.13700 1.000 37.91000  ? 767 HOH B O   1 
HETATM 6147 O  O   . HOH GA 7 .   ? 13.67100  -17.38400 24.93400 1.000 31.46000  ? 768 HOH B O   1 
HETATM 6148 O  O   . HOH GA 7 .   ? -11.026   33.546    10.726   1.000 40.86000  ? 769 HOH B O   1 
HETATM 6149 O  O   . HOH GA 7 .   ? -14.68300 3.44600   22.47900 1.000 32.15000  ? 770 HOH B O   1 
HETATM 6150 O  O   . HOH GA 7 .   ? -17.55200 8.45700   31.57300 1.000 33.20000  ? 771 HOH B O   1 
HETATM 6151 O  O   . HOH GA 7 .   ? -0.53300  20.68500  -2.49900 1.000 35.38000  ? 772 HOH B O   1 
HETATM 6152 O  O   . HOH GA 7 .   ? 14.06800  -0.34300  17.71400 1.000 32.60000  ? 773 HOH B O   1 
HETATM 6153 O  O   . HOH GA 7 .   ? 9.28400   29.67700  -1.50000 1.000 46.09000  ? 774 HOH B O   1 
HETATM 6154 O  O   . HOH GA 7 .   ? -11.38500 27.54700  21.07800 1.000 38.97000  ? 775 HOH B O   1 
HETATM 6155 O  O   . HOH GA 7 .   ? -3.01600  21.42300  -2.39300 1.000 44.38000  ? 776 HOH B O   1 
HETATM 6156 O  O   . HOH GA 7 .   ? 20.54200  0.79600   21.88600 1.000 28.92000  ? 777 HOH B O   1 
HETATM 6157 O  O   . HOH GA 7 .   ? -9.51100  17.78500  35.49900 1.000 38.78000  ? 778 HOH B O   1 
HETATM 6158 O  O   . HOH GA 7 .   ? -13.90700 1.74900   24.63900 1.000 28.30000  ? 779 HOH B O   1 
HETATM 6159 O  O   . HOH GA 7 .   ? 3.78400   -2.67300  6.70900  1.000 40.45000  ? 780 HOH B O   1 
HETATM 6160 O  O   . HOH GA 7 .   ? 11.46100  -0.90600  17.60400 1.000 36.40000  ? 781 HOH B O   1 
HETATM 6161 O  O   . HOH GA 7 .   ? 3.79500   30.18300  30.44400 1.000 34.69000  ? 782 HOH B O   1 
HETATM 6162 O  O   . HOH GA 7 .   ? 19.46600  11.59500  5.67000  1.000 31.22000  ? 783 HOH B O   1 
HETATM 6163 O  O   . HOH GA 7 .   ? 18.26100  -4.85600  40.69300 1.000 36.24000  ? 784 HOH B O   1 
HETATM 6164 O  O   . HOH GA 7 .   ? 5.30800   -3.46500  44.63700 1.000 31.29000  ? 785 HOH B O   1 
HETATM 6165 O  O   . HOH GA 7 .   ? -2.15300  16.20400  -1.97900 1.000 34.08000  ? 786 HOH B O   1 
HETATM 6166 O  O   . HOH GA 7 .   ? -8.41900  -5.24500  35.61600 1.000 30.48000  ? 787 HOH B O   1 
HETATM 6167 O  O   . HOH GA 7 .   ? -15.76800 20.55800  17.80800 1.000 37.74000  ? 788 HOH B O   1 
HETATM 6168 O  O   . HOH GA 7 .   ? 5.94500   -2.44500  7.66400  1.000 37.36000  ? 789 HOH B O   1 
HETATM 6169 O  O   . HOH GA 7 .   ? -11.38700 35.08300  13.24800 1.000 29.92000  ? 790 HOH B O   1 
HETATM 6170 O  O   . HOH GA 7 .   ? 15.95100  23.33200  6.16600  1.000 37.14000  ? 791 HOH B O   1 
HETATM 6171 O  O   . HOH GA 7 .   ? 20.80800  15.88700  -3.35000 1.000 39.04000  ? 792 HOH B O   1 
HETATM 6172 O  O   . HOH GA 7 .   ? -2.72100  25.27600  38.04400 1.000 40.17000  ? 793 HOH B O   1 
HETATM 6173 O  O   . HOH GA 7 .   ? 9.90800   -4.18500  18.02900 1.000 26.75000  ? 794 HOH B O   1 
HETATM 6174 O  O   . HOH GA 7 .   ? -9.28700  12.75500  4.93100  1.000 35.34000  ? 795 HOH B O   1 
HETATM 6175 O  O   . HOH GA 7 .   ? 14.07900  12.14700  38.10500 1.000 33.97000  ? 796 HOH B O   1 
HETATM 6176 O  O   . HOH GA 7 .   ? -13.62400 9.65200   19.03400 1.000 34.38000  ? 797 HOH B O   1 
HETATM 6177 O  O   . HOH GA 7 .   ? -10.97200 -2.39500  23.70500 1.000 33.02000  ? 798 HOH B O   1 
HETATM 6178 O  O   . HOH GA 7 .   ? -11.45200 24.28000  15.77000 1.000 36.18000  ? 799 HOH B O   1 
HETATM 6179 O  O   . HOH GA 7 .   ? 2.19200   17.11800  -3.39400 1.000 40.26000  ? 800 HOH B O   1 
HETATM 6180 O  O   . HOH GA 7 .   ? -7.740    -15.961   21.918   1.000 42.92000  ? 801 HOH B O   1 
HETATM 6181 O  O   . HOH GA 7 .   ? -9.209    36.712    13.180   1.000 26.61000  ? 802 HOH B O   1 
HETATM 6182 O  O   . HOH GA 7 .   ? 12.019    -12.608   35.114   1.000 33.88000  ? 803 HOH B O   1 
HETATM 6183 O  O   . HOH GA 7 .   ? 11.393    -14.979   33.894   1.000 34.16000  ? 804 HOH B O   1 
HETATM 6184 O  O   . HOH GA 7 .   ? 14.38300  17.79700  -2.25900 1.000 39.51000  ? 805 HOH B O   1 
HETATM 6185 O  O   . HOH GA 7 .   ? 5.73800   19.06000  39.96000 1.000 29.57000  ? 806 HOH B O   1 
HETATM 6186 O  O   . HOH GA 7 .   ? -2.56200  -2.58100  11.30600 1.000 31.81000  ? 807 HOH B O   1 
HETATM 6187 O  O   . HOH GA 7 .   ? 15.70800  -10.49700 35.69900 1.000 35.96000  ? 808 HOH B O   1 
HETATM 6188 O  O   . HOH GA 7 .   ? 14.85600  6.61300   13.66800 1.000 41.50000  ? 809 HOH B O   1 
HETATM 6189 O  O   . HOH GA 7 .   ? 5.83600   15.79000  40.82000 1.000 25.23000  ? 810 HOH B O   1 
HETATM 6190 O  O   . HOH GA 7 .   ? -4.19400  28.24500  35.35500 1.000 43.67000  ? 811 HOH B O   1 
HETATM 6191 O  O   . HOH GA 7 .   ? 5.65100   -1.20600  46.29200 1.000 33.35000  ? 812 HOH B O   1 
HETATM 6192 O  O   . HOH GA 7 .   ? -1.46400  11.66100  -1.10500 1.000 30.20000  ? 813 HOH B O   1 
HETATM 6193 O  O   . HOH GA 7 .   ? 15.57800  15.09000  36.70100 1.000 36.04000  ? 814 HOH B O   1 
HETATM 6194 O  O   . HOH GA 7 .   ? -8.11100  25.50200  0.80200  1.000 38.05000  ? 815 HOH B O   1 
HETATM 6195 O  O   . HOH GA 7 .   ? 14.22400  15.52000  38.69000 1.000 34.01000  ? 816 HOH B O   1 
HETATM 6196 O  O   . HOH GA 7 .   ? 10.71800  0.83900   15.74400 1.000 35.86000  ? 817 HOH B O   1 
HETATM 6197 O  O   . HOH GA 7 .   ? 13.92000  -8.94800  40.39500 1.000 35.42000  ? 818 HOH B O   1 
HETATM 6198 O  O   . HOH GA 7 .   ? 15.90500  4.47600   18.61700 1.000 36.51000  ? 819 HOH B O   1 
HETATM 6199 O  O   . HOH GA 7 .   ? 19.75000  -0.17200  19.13500 1.000 37.69000  ? 820 HOH B O   1 
HETATM 6200 O  O   . HOH GA 7 .   ? -0.33500  10.58000  44.22500 1.000 40.49000  ? 821 HOH B O   1 
HETATM 6201 O  O   . HOH GA 7 .   ? 1.72000   10.92800  42.49000 1.000 38.84000  ? 822 HOH B O   1 
HETATM 6202 O  O   . HOH GA 7 .   ? 3.45000   9.71300   43.52700 1.000 38.21000  ? 823 HOH B O   1 
HETATM 6203 O  O   . HOH GA 7 .   ? -3.67200  9.20800   2.06400  1.000 40.39000  ? 824 HOH B O   1 
HETATM 6204 O  O   . HOH GA 7 .   ? 1.03200   13.63900  -4.34300 1.000 54.32000  ? 825 HOH B O   1 
HETATM 6205 O  O   . HOH GA 7 .   ? 14.24400  2.20200   16.07400 1.000 41.84000  ? 826 HOH B O   1 
HETATM 6206 O  O   . HOH GA 7 .   ? -1.29700  13.34700  -3.37300 1.000 46.57000  ? 827 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   ? 0.86430 0.83050 0.64580 0.13480  0.06930  0.08380  2   THR A N   
2    C CA  . THR A  8   ? 0.88380 0.84770 0.65370 0.13320  0.03890  0.06370  2   THR A CA  
3    C C   . THR A  8   ? 0.79480 0.77140 0.60620 0.10620  0.02300  0.05080  2   THR A C   
4    O O   . THR A  8   ? 0.80500 0.77850 0.61140 0.10580  0.00220  0.03420  2   THR A O   
5    C CB  . THR A  8   ? 0.92460 0.88590 0.68120 0.14080  0.03250  0.06760  2   THR A CB  
6    O OG1 . THR A  8   ? 0.90300 0.87360 0.68560 0.12330  0.00980  0.05500  2   THR A OG1 
7    C CG2 . THR A  8   ? 0.86930 0.83330 0.63910 0.14050  0.05880  0.09070  2   THR A CG2 
8    N N   . PRO A  9   ? 0.72820 0.71680 0.57920 0.08600  0.03190  0.05820  3   PRO A N   
9    C CA  . PRO A  9   ? 0.64410 0.64280 0.52800 0.06520  0.02020  0.04810  3   PRO A CA  
10   C C   . PRO A  9   ? 0.59200 0.58860 0.47470 0.06440  0.01700  0.03920  3   PRO A C   
11   O O   . PRO A  9   ? 0.63860 0.63090 0.51140 0.07260  0.03180  0.04520  3   PRO A O   
12   C CB  . PRO A  9   ? 0.52360 0.53040 0.44000 0.05120  0.03410  0.05890  3   PRO A CB  
13   C CG  . PRO A  9   ? 0.64610 0.64920 0.55300 0.05990  0.04290  0.07070  3   PRO A CG  
14   C CD  . PRO A  9   ? 0.77120 0.76320 0.63910 0.08250  0.04990  0.07510  3   PRO A CD  
15   N N   . SER A  10  ? 0.53930 0.53890 0.43490 0.05500  -0.00160 0.02610  4   SER A N   
16   C CA  . SER A  10  ? 0.49460 0.49010 0.38910 0.05480  -0.00740 0.01660  4   SER A CA  
17   C C   . SER A  10  ? 0.50670 0.50990 0.42700 0.04160  0.00590  0.02180  4   SER A C   
18   O O   . SER A  10  ? 0.40880 0.42030 0.35140 0.03100  0.01470  0.03000  4   SER A O   
19   C CB  . SER A  10  ? 0.52650 0.52220 0.43370 0.04850  -0.03150 0.00280  4   SER A CB  
20   O OG  . SER A  10  ? 0.62790 0.61190 0.50790 0.06460  -0.04880 -0.00670 4   SER A OG  
21   N N   . GLU A  11  ? 0.42600 0.42470 0.34250 0.04370  0.00470  0.01550  5   GLU A N   
22   C CA  . GLU A  11  ? 0.40230 0.40730 0.34260 0.03270  0.01370  0.01830  5   GLU A CA  
23   C C   . GLU A  11  ? 0.39100 0.40030 0.35310 0.01920  -0.00050 0.01000  5   GLU A C   
24   O O   . GLU A  11  ? 0.35160 0.35550 0.31210 0.02010  -0.01010 0.00100  5   GLU A O   
25   C CB  . GLU A  11  ? 0.48020 0.47840 0.40460 0.04420  0.02290  0.01810  5   GLU A CB  
26   C CG  . GLU A  11  ? 0.53750 0.53280 0.44440 0.05930  0.04230  0.03130  5   GLU A CG  
27   C CD  . GLU A  11  ? 0.55580 0.56180 0.49530 0.04890  0.05840  0.04550  5   GLU A CD  
28   O OE1 . GLU A  11  ? 0.61690 0.62860 0.58100 0.04090  0.06370  0.04680  5   GLU A OE1 
29   O OE2 . GLU A  11  ? 0.46710 0.47470 0.40930 0.04920  0.06380  0.05450  5   GLU A OE2 
30   N N   . ASP A  12  ? 0.26050 0.27870 0.24350 0.00830  -0.00100 0.01430  6   ASP A N   
31   C CA  . ASP A  12  ? 0.26360 0.28650 0.26710 -0.00160 -0.01130 0.01060  6   ASP A CA  
32   C C   . ASP A  12  ? 0.23510 0.26290 0.25620 -0.00980 -0.00410 0.01420  6   ASP A C   
33   O O   . ASP A  12  ? 0.24240 0.27400 0.26910 -0.01210 0.00320  0.02000  6   ASP A O   
34   C CB  . ASP A  12  ? 0.28030 0.30880 0.29090 -0.00350 -0.01700 0.01340  6   ASP A CB  
35   C CG  . ASP A  12  ? 0.30100 0.32390 0.29790 0.00480  -0.03050 0.00710  6   ASP A CG  
36   O OD1 . ASP A  12  ? 0.34260 0.35800 0.33560 0.00820  -0.04170 -0.00210 6   ASP A OD1 
37   O OD2 . ASP A  12  ? 0.26550 0.28970 0.25480 0.00940  -0.03160 0.01020  6   ASP A OD2 
38   N N   . PHE A  13  ? 0.22950 0.25550 0.25860 -0.01290 -0.00780 0.00990  7   PHE A N   
39   C CA  . PHE A  13  ? 0.21190 0.24070 0.25340 -0.01780 -0.00240 0.01240  7   PHE A CA  
40   C C   . PHE A  13  ? 0.21380 0.24450 0.27100 -0.02260 -0.00750 0.01320  7   PHE A C   
41   O O   . PHE A  13  ? 0.21240 0.24100 0.27680 -0.02370 -0.01610 0.01000  7   PHE A O   
42   C CB  . PHE A  13  ? 0.25050 0.27510 0.28770 -0.01500 0.00220  0.00940  7   PHE A CB  
43   C CG  . PHE A  13  ? 0.25170 0.27620 0.28140 -0.00980 0.01190  0.01320  7   PHE A CG  
44   C CD1 . PHE A  13  ? 0.31930 0.33910 0.32970 -0.00070 0.01380  0.01290  7   PHE A CD1 
45   C CD2 . PHE A  13  ? 0.30000 0.32840 0.34370 -0.01240 0.01870  0.01800  7   PHE A CD2 
46   C CE1 . PHE A  13  ? 0.37560 0.39570 0.38120 0.00600  0.02700  0.02070  7   PHE A CE1 
47   C CE2 . PHE A  13  ? 0.29910 0.32840 0.34560 -0.00830 0.02930  0.02450  7   PHE A CE2 
48   C CZ  . PHE A  13  ? 0.35760 0.38340 0.38550 0.00100  0.03560  0.02760  7   PHE A CZ  
49   N N   . VAL A  14  ? 0.18670 0.22010 0.25030 -0.02400 -0.00240 0.01780  8   VAL A N   
50   C CA  . VAL A  14  ? 0.16550 0.19870 0.24080 -0.02540 -0.00260 0.02070  8   VAL A CA  
51   C C   . VAL A  14  ? 0.18080 0.20980 0.25240 -0.02410 -0.00040 0.01730  8   VAL A C   
52   O O   . VAL A  14  ? 0.17530 0.20410 0.24120 -0.02220 0.00230  0.01590  8   VAL A O   
53   C CB  . VAL A  14  ? 0.19150 0.22920 0.27120 -0.02290 0.00230  0.02940  8   VAL A CB  
54   C CG1 . VAL A  14  ? 0.20570 0.24190 0.27240 -0.01840 0.00510  0.02860  8   VAL A CG1 
55   C CG2 . VAL A  14  ? 0.21560 0.25210 0.30500 -0.02130 0.00560  0.03560  8   VAL A CG2 
56   N N   . VAL A  15  ? 0.15110 0.17640 0.22990 -0.02520 -0.00250 0.01640  9   VAL A N   
57   C CA  . VAL A  15  ? 0.19720 0.21800 0.27310 -0.02360 -0.00180 0.01200  9   VAL A CA  
58   C C   . VAL A  15  ? 0.21750 0.23580 0.30090 -0.02240 -0.00040 0.01680  9   VAL A C   
59   O O   . VAL A  15  ? 0.21540 0.23290 0.31160 -0.02440 -0.00130 0.02180  9   VAL A O   
60   C CB  . VAL A  15  ? 0.21350 0.22860 0.28570 -0.02320 -0.00630 0.00440  9   VAL A CB  
61   C CG1 . VAL A  15  ? 0.23820 0.24930 0.30900 -0.02050 -0.00410 0.00100  9   VAL A CG1 
62   C CG2 . VAL A  15  ? 0.18260 0.19860 0.24170 -0.02030 -0.00540 0.00170  9   VAL A CG2 
63   N N   . THR A  16  ? 0.18490 0.20170 0.26320 -0.01820 0.00130  0.01610  10  THR A N   
64   C CA  . THR A  16  ? 0.18460 0.19720 0.26520 -0.01410 0.00290  0.02090  10  THR A CA  
65   C C   . THR A  16  ? 0.19560 0.20350 0.27870 -0.01430 0.00070  0.01510  10  THR A C   
66   O O   . THR A  16  ? 0.21250 0.22160 0.29330 -0.01480 -0.00050 0.00830  10  THR A O   
67   C CB  . THR A  16  ? 0.21540 0.22680 0.28440 -0.00520 0.00400  0.02380  10  THR A CB  
68   O OG1 . THR A  16  ? 0.21650 0.22760 0.28280 -0.00370 -0.00120 0.01540  10  THR A OG1 
69   C CG2 . THR A  16  ? 0.21940 0.23440 0.28300 -0.00280 0.00660  0.02880  10  THR A CG2 
70   N N   . ASP A  17  ? 0.16630 0.16880 0.25580 -0.01290 0.00160  0.01950  11  ASP A N   
71   C CA  . ASP A  17  ? 0.18430 0.18100 0.27650 -0.01260 -0.00090 0.01390  11  ASP A CA  
72   C C   . ASP A  17  ? 0.19180 0.18360 0.28310 -0.00590 0.00130  0.01980  11  ASP A C   
73   O O   . ASP A  17  ? 0.19690 0.18780 0.28720 -0.00130 0.00620  0.03020  11  ASP A O   
74   C CB  . ASP A  17  ? 0.19690 0.18770 0.29990 -0.01770 -0.00540 0.01060  11  ASP A CB  
75   C CG  . ASP A  17  ? 0.24900 0.23580 0.37060 -0.01970 -0.00440 0.02060  11  ASP A CG  
76   O OD1 . ASP A  17  ? 0.23110 0.22290 0.36270 -0.02260 -0.00260 0.02780  11  ASP A OD1 
77   O OD2 . ASP A  17  ? 0.24220 0.22120 0.37210 -0.01800 -0.00420 0.02310  11  ASP A OD2 
78   N N   . ARG A  18  ? 0.17920 0.16710 0.27020 -0.00360 -0.00100 0.01410  12  ARG A N   
79   C CA  . ARG A  18  ? 0.19430 0.17560 0.28440 0.00350  0.00000  0.01880  12  ARG A CA  
80   C C   . ARG A  18  ? 0.21070 0.18450 0.31140 0.00020  -0.00180 0.01550  12  ARG A C   
81   O O   . ARG A  18  ? 0.21240 0.18620 0.31190 -0.00020 -0.00480 0.00590  12  ARG A O   
82   C CB  . ARG A  18  ? 0.18000 0.16320 0.26120 0.01110  -0.00410 0.01360  12  ARG A CB  
83   C CG  . ARG A  18  ? 0.23560 0.21110 0.31020 0.02210  -0.00500 0.01780  12  ARG A CG  
84   C CD  . ARG A  18  ? 0.22110 0.19870 0.28880 0.03060  -0.01390 0.01060  12  ARG A CD  
85   N NE  . ARG A  18  ? 0.19140 0.17050 0.24730 0.03500  -0.01670 0.01100  12  ARG A NE  
86   C CZ  . ARG A  18  ? 0.23310 0.20470 0.26850 0.04860  -0.01640 0.01740  12  ARG A CZ  
87   N NH1 . ARG A  18  ? 0.25150 0.21420 0.27660 0.05950  -0.01300 0.02510  12  ARG A NH1 
88   N NH2 . ARG A  18  ? 0.23730 0.20920 0.26040 0.05320  -0.01840 0.01710  12  ARG A NH2 
89   N N   . GLY A  19  ? 0.21960 0.18640 0.33280 -0.00120 0.00030  0.02390  13  GLY A N   
90   C CA  . GLY A  19  ? 0.25370 0.21020 0.37920 -0.00410 -0.00430 0.01930  13  GLY A CA  
91   C C   . GLY A  19  ? 0.21580 0.17110 0.34140 -0.00940 -0.01200 0.00650  13  GLY A C   
92   O O   . GLY A  19  ? 0.22790 0.17470 0.35160 -0.00720 -0.01710 -0.00290 13  GLY A O   
93   N N   . GLY A  20  ? 0.23190 0.19410 0.35620 -0.01380 -0.01300 0.00560  14  GLY A N   
94   C CA  . GLY A  20  ? 0.25890 0.21840 0.37730 -0.01530 -0.02070 -0.00620 14  GLY A CA  
95   C C   . GLY A  20  ? 0.24850 0.21480 0.34670 -0.01060 -0.01680 -0.01270 14  GLY A C   
96   O O   . GLY A  20  ? 0.25890 0.22410 0.34650 -0.00900 -0.02000 -0.01990 14  GLY A O   
97   N N   . ILE A  21  ? 0.18650 0.15950 0.28110 -0.00720 -0.01030 -0.00950 15  ILE A N   
98   C CA  . ILE A  21  ? 0.22780 0.20880 0.31430 -0.00350 -0.00550 -0.01280 15  ILE A CA  
99   C C   . ILE A  21  ? 0.19540 0.18660 0.28110 -0.00680 -0.00290 -0.00830 15  ILE A C   
100  O O   . ILE A  21  ? 0.19040 0.18400 0.27900 -0.00790 -0.00310 -0.00240 15  ILE A O   
101  C CB  . ILE A  21  ? 0.17650 0.15940 0.26770 0.00160  -0.00310 -0.01250 15  ILE A CB  
102  C CG1 . ILE A  21  ? 0.19740 0.16850 0.28940 0.00520  -0.00590 -0.01620 15  ILE A CG1 
103  C CG2 . ILE A  21  ? 0.18050 0.17350 0.27400 0.00470  0.00270  -0.01360 15  ILE A CG2 
104  C CD1 . ILE A  21  ? 0.21300 0.18480 0.31120 0.01020  -0.00510 -0.01420 15  ILE A CD1 
105  N N   . VAL A  22  ? 0.19210 0.18780 0.27160 -0.00630 0.00010  -0.01040 16  VAL A N   
106  C CA  . VAL A  22  ? 0.18820 0.19220 0.26820 -0.00940 0.00220  -0.00630 16  VAL A CA  
107  C C   . VAL A  22  ? 0.17450 0.18440 0.26370 -0.00840 0.00250  -0.00370 16  VAL A C   
108  O O   . VAL A  22  ? 0.20790 0.22090 0.30610 -0.00530 0.00440  -0.00500 16  VAL A O   
109  C CB  . VAL A  22  ? 0.17300 0.17990 0.24530 -0.00700 0.00720  -0.00730 16  VAL A CB  
110  C CG1 . VAL A  22  ? 0.23790 0.25250 0.31400 -0.01030 0.00930  -0.00260 16  VAL A CG1 
111  C CG2 . VAL A  22  ? 0.23030 0.22870 0.28950 -0.00580 0.00180  -0.01220 16  VAL A CG2 
112  N N   . GLU A  23  ? 0.15950 0.17030 0.24710 -0.00950 -0.00040 -0.00030 17  GLU A N   
113  C CA  . GLU A  23  ? 0.17460 0.18760 0.26700 -0.00610 -0.00450 -0.00050 17  GLU A CA  
114  C C   . GLU A  23  ? 0.17980 0.19830 0.27700 -0.00860 -0.00420 -0.00030 17  GLU A C   
115  O O   . GLU A  23  ? 0.15060 0.17400 0.26350 -0.00900 -0.00320 -0.00130 17  GLU A O   
116  C CB  . GLU A  23  ? 0.17690 0.18420 0.25880 -0.00090 -0.00780 0.00310  17  GLU A CB  
117  C CG  . GLU A  23  ? 0.17520 0.18020 0.25470 0.00720  -0.01610 0.00020  17  GLU A CG  
118  C CD  . GLU A  23  ? 0.21340 0.21350 0.29310 0.01440  -0.02090 -0.00190 17  GLU A CD  
119  O OE1 . GLU A  23  ? 0.21120 0.20500 0.27930 0.01940  -0.01750 0.00380  17  GLU A OE1 
120  O OE2 . GLU A  23  ? 0.20590 0.20920 0.30110 0.01500  -0.02730 -0.00790 17  GLU A OE2 
121  N N   . ASN A  24  ? 0.16680 0.18480 0.25440 -0.00990 -0.00410 0.00250  18  ASN A N   
122  C CA  . ASN A  24  ? 0.15760 0.17910 0.24820 -0.01190 -0.00390 0.00320  18  ASN A CA  
123  C C   . ASN A  24  ? 0.19460 0.21800 0.27720 -0.01580 0.00150  0.00620  18  ASN A C   
124  O O   . ASN A  24  ? 0.18980 0.21100 0.26590 -0.01690 0.00190  0.00740  18  ASN A O   
125  C CB  . ASN A  24  ? 0.15570 0.17330 0.23960 -0.00680 -0.01090 0.00260  18  ASN A CB  
126  C CG  . ASN A  24  ? 0.16770 0.18020 0.25410 0.00060  -0.02060 -0.00230 18  ASN A CG  
127  O OD1 . ASN A  24  ? 0.15000 0.16490 0.25460 -0.00070 -0.02380 -0.00590 18  ASN A OD1 
128  N ND2 . ASN A  24  ? 0.20420 0.20920 0.27210 0.01020  -0.02500 -0.00200 18  ASN A ND2 
129  N N   . SER A  25  ? 0.15850 0.18520 0.24430 -0.01750 0.00480  0.00770  19  SER A N   
130  C CA  . SER A  25  ? 0.16200 0.18940 0.23760 -0.01910 0.00720  0.01000  19  SER A CA  
131  C C   . SER A  25  ? 0.16780 0.19700 0.24570 -0.01940 0.00710  0.01260  19  SER A C   
132  O O   . SER A  25  ? 0.16630 0.19590 0.25760 -0.01920 0.00660  0.01260  19  SER A O   
133  C CB  . SER A  25  ? 0.16590 0.19280 0.23530 -0.01750 0.01230  0.00940  19  SER A CB  
134  O OG  . SER A  25  ? 0.20360 0.23330 0.28070 -0.01510 0.01990  0.01280  19  SER A OG  
135  N N   . HIS A  26  ? 0.17160 0.20140 0.24040 -0.02000 0.00660  0.01480  20  HIS A N   
136  C CA  . HIS A  26  ? 0.18620 0.21620 0.25450 -0.01920 0.00560  0.01700  20  HIS A CA  
137  C C   . HIS A  26  ? 0.16610 0.19840 0.22720 -0.01990 0.00860  0.02010  20  HIS A C   
138  O O   . HIS A  26  ? 0.18670 0.22020 0.24250 -0.02050 0.00680  0.01990  20  HIS A O   
139  C CB  . HIS A  26  ? 0.18420 0.21220 0.24630 -0.01540 0.00180  0.01770  20  HIS A CB  
140  C CG  . HIS A  26  ? 0.16920 0.19300 0.23110 -0.01120 -0.00200 0.01480  20  HIS A CG  
141  N ND1 . HIS A  26  ? 0.15450 0.17220 0.21590 -0.00520 -0.00920 0.01060  20  HIS A ND1 
142  C CD2 . HIS A  26  ? 0.15670 0.17970 0.21790 -0.01040 -0.00120 0.01520  20  HIS A CD2 
143  C CE1 . HIS A  26  ? 0.19890 0.21270 0.25660 0.00000  -0.01280 0.00820  20  HIS A CE1 
144  N NE2 . HIS A  26  ? 0.19090 0.20820 0.24870 -0.00350 -0.00670 0.01200  20  HIS A NE2 
145  N N   . ARG A  27  ? 0.16960 0.20180 0.23330 -0.01930 0.01200  0.02300  21  ARG A N   
146  C CA  . ARG A  27  ? 0.19000 0.22320 0.24390 -0.01770 0.01470  0.02630  21  ARG A CA  
147  C C   . ARG A  27  ? 0.16650 0.20110 0.21690 -0.01750 0.01050  0.02750  21  ARG A C   
148  O O   . ARG A  27  ? 0.18370 0.21660 0.23830 -0.01670 0.00850  0.02740  21  ARG A O   
149  C CB  . ARG A  27  ? 0.21470 0.24660 0.27410 -0.01560 0.02240  0.03200  21  ARG A CB  
150  C CG  . ARG A  27  ? 0.29200 0.32320 0.33630 -0.01080 0.02600  0.03630  21  ARG A CG  
151  C CD  . ARG A  27  ? 0.31980 0.34930 0.37010 -0.00680 0.03760  0.04570  21  ARG A CD  
152  N NE  . ARG A  27  ? 0.40120 0.43080 0.45430 -0.00280 0.04700  0.04890  21  ARG A NE  
153  C CZ  . ARG A  27  ? 0.39370 0.42040 0.42420 0.00700  0.05280  0.05020  21  ARG A CZ  
154  N NH1 . ARG A  27  ? 0.42240 0.44540 0.42680 0.01320  0.04720  0.04720  21  ARG A NH1 
155  N NH2 . ARG A  27  ? 0.33480 0.36160 0.36830 0.01250  0.06320  0.05410  21  ARG A NH2 
156  N N   . VAL A  28  ? 0.14090 0.17800 0.18420 -0.01670 0.00820  0.02810  22  VAL A N   
157  C CA  . VAL A  28  ? 0.15810 0.19900 0.20310 -0.01620 0.00530  0.03080  22  VAL A CA  
158  C C   . VAL A  28  ? 0.19700 0.23840 0.23500 -0.01340 0.00520  0.03330  22  VAL A C   
159  O O   . VAL A  28  ? 0.20990 0.24950 0.23890 -0.01090 0.00360  0.03160  22  VAL A O   
160  C CB  . VAL A  28  ? 0.18170 0.22680 0.23470 -0.01820 0.00070  0.03050  22  VAL A CB  
161  C CG1 . VAL A  28  ? 0.20430 0.25590 0.26530 -0.01670 0.00020  0.03630  22  VAL A CG1 
162  C CG2 . VAL A  28  ? 0.20980 0.25350 0.26870 -0.01970 0.00210  0.02970  22  VAL A CG2 
163  N N   . HIS A  29  ? 0.15020 0.19200 0.18900 -0.01150 0.00650  0.03680  23  HIS A N   
164  C CA  . HIS A  29  ? 0.18170 0.22470 0.21500 -0.00820 0.00590  0.04010  23  HIS A CA  
165  C C   . HIS A  29  ? 0.15880 0.20870 0.19910 -0.00690 0.00300  0.04290  23  HIS A C   
166  O O   . HIS A  29  ? 0.15630 0.20710 0.20100 -0.00560 0.00550  0.04470  23  HIS A O   
167  C CB  . HIS A  29  ? 0.15950 0.19650 0.19140 -0.00620 0.01060  0.04330  23  HIS A CB  
168  C CG  . HIS A  29  ? 0.15660 0.18880 0.19170 -0.00750 0.01580  0.04370  23  HIS A CG  
169  N ND1 . HIS A  29  ? 0.18440 0.21480 0.21100 -0.00390 0.02140  0.04730  23  HIS A ND1 
170  C CD2 . HIS A  29  ? 0.16320 0.19170 0.21080 -0.01030 0.01670  0.04210  23  HIS A CD2 
171  C CE1 . HIS A  29  ? 0.24930 0.27700 0.28620 -0.00500 0.02830  0.05000  23  HIS A CE1 
172  N NE2 . HIS A  29  ? 0.21120 0.23810 0.26390 -0.01000 0.02420  0.04620  23  HIS A NE2 
173  N N   . ALA A  30  ? 0.18590 0.24030 0.22720 -0.00540 -0.00230 0.04380  24  ALA A N   
174  C CA  . ALA A  30  ? 0.18070 0.24410 0.23640 -0.00410 -0.00410 0.04840  24  ALA A CA  
175  C C   . ALA A  30  ? 0.18550 0.25150 0.23920 -0.00040 -0.01010 0.04930  24  ALA A C   
176  O O   . ALA A  30  ? 0.19030 0.25150 0.23210 0.00160  -0.01630 0.04490  24  ALA A O   
177  C CB  . ALA A  30  ? 0.16010 0.23010 0.23610 -0.00830 -0.00770 0.04890  24  ALA A CB  
178  N N   . ALA A  31  ? 0.17020 0.24270 0.23280 0.00310  -0.00800 0.05550  25  ALA A N   
179  C CA  . ALA A  31  ? 0.18610 0.26300 0.25110 0.00740  -0.01440 0.05720  25  ALA A CA  
180  C C   . ALA A  31  ? 0.18020 0.27100 0.27520 0.00730  -0.01600 0.06360  25  ALA A C   
181  O O   . ALA A  31  ? 0.16670 0.26190 0.27060 0.00880  -0.00550 0.07050  25  ALA A O   
182  C CB  . ALA A  31  ? 0.17290 0.24380 0.22180 0.01320  -0.00830 0.06060  25  ALA A CB  
183  N N   . VAL A  32  ? 0.17930 0.27660 0.29140 0.00700  -0.02920 0.06160  26  VAL A N   
184  C CA  . VAL A  32  ? 0.18760 0.30020 0.33720 0.00720  -0.03170 0.06940  26  VAL A CA  
185  C C   . VAL A  32  ? 0.16920 0.28430 0.31630 0.01360  -0.04060 0.06900  26  VAL A C   
186  O O   . VAL A  32  ? 0.21120 0.31960 0.34540 0.01580  -0.05590 0.05980  26  VAL A O   
187  C CB  . VAL A  32  ? 0.15990 0.27850 0.34460 0.00020  -0.04350 0.06720  26  VAL A CB  
188  C CG1 . VAL A  32  ? 0.15520 0.29170 0.38970 -0.00020 -0.04290 0.07920  26  VAL A CG1 
189  C CG2 . VAL A  32  ? 0.19220 0.30570 0.37460 -0.00530 -0.03530 0.06680  26  VAL A CG2 
190  N N   . VAL A  33  ? 0.18290 0.30640 0.33920 0.01900  -0.03120 0.07890  27  VAL A N   
191  C CA  . VAL A  33  ? 0.18890 0.31320 0.33790 0.02630  -0.03700 0.07930  27  VAL A CA  
192  C C   . VAL A  33  ? 0.19090 0.33390 0.38180 0.02910  -0.03740 0.08960  27  VAL A C   
193  O O   . VAL A  33  ? 0.17200 0.32600 0.39120 0.02780  -0.02570 0.10000  27  VAL A O   
194  C CB  . VAL A  33  ? 0.18460 0.29760 0.29900 0.03240  -0.02460 0.08110  27  VAL A CB  
195  C CG1 . VAL A  33  ? 0.24370 0.34000 0.32600 0.02920  -0.02260 0.07360  27  VAL A CG1 
196  C CG2 . VAL A  33  ? 0.17040 0.28800 0.29150 0.03670  -0.00810 0.09060  27  VAL A CG2 
197  N N   . ASP A  34  ? 0.20020 0.34680 0.39610 0.03440  -0.04990 0.08800  28  ASP A N   
198  C CA  . ASP A  34  ? 0.20220 0.36810 0.44210 0.03790  -0.05030 0.09880  28  ASP A CA  
199  C C   . ASP A  34  ? 0.20140 0.36770 0.42470 0.04760  -0.03150 0.10850  28  ASP A C   
200  O O   . ASP A  34  ? 0.22540 0.37670 0.40900 0.04990  -0.02030 0.10610  28  ASP A O   
201  C CB  . ASP A  34  ? 0.21000 0.38030 0.46850 0.04000  -0.07630 0.09140  28  ASP A CB  
202  C CG  . ASP A  34  ? 0.24550 0.40400 0.46270 0.04990  -0.08230 0.08590  28  ASP A CG  
203  O OD1 . ASP A  34  ? 0.26360 0.41180 0.44410 0.05430  -0.06590 0.08910  28  ASP A OD1 
204  O OD2 . ASP A  34  ? 0.25910 0.41780 0.48290 0.05460  -0.10560 0.07810  28  ASP A OD2 
205  N N   . ALA A  35  ? 0.20940 0.39200 0.46540 0.05410  -0.02910 0.11930  29  ALA A N   
206  C CA  . ALA A  35  ? 0.16720 0.35010 0.40960 0.06570  -0.01100 0.12890  29  ALA A CA  
207  C C   . ALA A  35  ? 0.26940 0.43570 0.46770 0.07220  -0.01450 0.12170  29  ALA A C   
208  O O   . ALA A  35  ? 0.28970 0.44750 0.46400 0.08100  -0.00040 0.12540  29  ALA A O   
209  C CB  . ALA A  35  ? 0.20910 0.40420 0.48760 0.06720  -0.00650 0.13740  29  ALA A CB  
210  N N   . LYS A  36  ? 0.23420 0.39370 0.42000 0.06990  -0.03290 0.11190  30  LYS A N   
211  C CA  . LYS A  36  ? 0.23520 0.37690 0.37890 0.07600  -0.03380 0.10720  30  LYS A CA  
212  C C   . LYS A  36  ? 0.28500 0.40660 0.39140 0.07050  -0.03000 0.09950  30  LYS A C   
213  O O   . LYS A  36  ? 0.29170 0.39770 0.36730 0.07480  -0.02830 0.09780  30  LYS A O   
214  C CB  . LYS A  36  ? 0.25560 0.39860 0.40020 0.08090  -0.05390 0.10260  30  LYS A CB  
215  C CG  . LYS A  36  ? 0.31370 0.47800 0.50270 0.08580  -0.06200 0.10930  30  LYS A CG  
216  C CD  . LYS A  36  ? 0.36990 0.53390 0.54990 0.09770  -0.05410 0.11680  30  LYS A CD  
217  C CE  . LYS A  36  ? 0.46210 0.64250 0.68270 0.09970  -0.05970 0.11940  30  LYS A CE  
218  N NZ  . LYS A  36  ? 0.47370 0.65560 0.70320 0.10150  -0.08660 0.10950  30  LYS A NZ  
219  N N   . GLY A  37  ? 0.27130 0.39360 0.38380 0.06150  -0.02770 0.09640  31  GLY A N   
220  C CA  . GLY A  37  ? 0.24220 0.34830 0.32600 0.05620  -0.02480 0.08960  31  GLY A CA  
221  C C   . GLY A  37  ? 0.27620 0.37680 0.34910 0.05360  -0.03860 0.08130  31  GLY A C   
222  O O   . GLY A  37  ? 0.27880 0.36630 0.32800 0.05070  -0.03460 0.07720  31  GLY A O   
223  N N   . ARG A  38  ? 0.24960 0.35900 0.33960 0.05610  -0.05570 0.07830  32  ARG A N   
224  C CA  . ARG A  38  ? 0.27510 0.37600 0.34900 0.05780  -0.07160 0.06820  32  ARG A CA  
225  C C   . ARG A  38  ? 0.27560 0.37530 0.35600 0.04800  -0.07130 0.06270  32  ARG A C   
226  O O   . ARG A  38  ? 0.28280 0.39480 0.39750 0.04000  -0.06900 0.06560  32  ARG A O   
227  C CB  . ARG A  38  ? 0.28750 0.39700 0.38270 0.06350  -0.09500 0.06350  32  ARG A CB  
228  C CG  . ARG A  38  ? 0.41510 0.51170 0.48570 0.07070  -0.11540 0.05070  32  ARG A CG  
229  C CD  . ARG A  38  ? 0.49000 0.59380 0.58560 0.07750  -0.14390 0.04340  32  ARG A CD  
230  N NE  . ARG A  38  ? 0.57900 0.69750 0.72980 0.06620  -0.15580 0.04070  32  ARG A NE  
231  C CZ  . ARG A  38  ? 0.62780 0.75340 0.81220 0.06580  -0.17450 0.03430  32  ARG A CZ  
232  N NH1 . ARG A  38  ? 0.65860 0.78010 0.82890 0.07710  -0.18720 0.02970  32  ARG A NH1 
233  N NH2 . ARG A  38  ? 0.60860 0.74220 0.83910 0.05290  -0.17660 0.03280  32  ARG A NH2 
234  N N   . LEU A  39  ? 0.24800 0.33290 0.29590 0.05000  -0.07170 0.05640  33  LEU A N   
235  C CA  . LEU A  39  ? 0.29160 0.37390 0.34240 0.04160  -0.07010 0.05130  33  LEU A CA  
236  C C   . LEU A  39  ? 0.29420 0.38110 0.36840 0.04020  -0.09240 0.04180  33  LEU A C   
237  O O   . LEU A  39  ? 0.28210 0.36150 0.34130 0.05020  -0.11120 0.03320  33  LEU A O   
238  C CB  . LEU A  39  ? 0.34260 0.40820 0.35360 0.04580  -0.06180 0.04910  33  LEU A CB  
239  C CG  . LEU A  39  ? 0.38500 0.44760 0.39690 0.03730  -0.05510 0.04590  33  LEU A CG  
240  C CD1 . LEU A  39  ? 0.29910 0.36930 0.33130 0.02770  -0.04060 0.05270  33  LEU A CD1 
241  C CD2 . LEU A  39  ? 0.43210 0.47960 0.40820 0.04380  -0.04620 0.04570  33  LEU A CD2 
242  N N   . LEU A  40  ? 0.19600 0.29340 0.30730 0.02940  -0.09150 0.04350  34  LEU A N   
243  C CA  . LEU A  40  ? 0.27580 0.37650 0.41800 0.02650  -0.11400 0.03470  34  LEU A CA  
244  C C   . LEU A  40  ? 0.26090 0.35070 0.39230 0.02210  -0.11650 0.02600  34  LEU A C   
245  O O   . LEU A  40  ? 0.26570 0.34590 0.39190 0.02710  -0.13870 0.01270  34  LEU A O   
246  C CB  . LEU A  40  ? 0.18940 0.31020 0.39160 0.01830  -0.11310 0.04470  34  LEU A CB  
247  C CG  . LEU A  40  ? 0.19640 0.33040 0.41450 0.02300  -0.10700 0.05570  34  LEU A CG  
248  C CD1 . LEU A  40  ? 0.21520 0.36990 0.49330 0.01630  -0.09940 0.06940  34  LEU A CD1 
249  C CD2 . LEU A  40  ? 0.29660 0.42810 0.51140 0.03250  -0.13140 0.04690  34  LEU A CD2 
250  N N   . TYR A  41  ? 0.19770 0.28790 0.32540 0.01450  -0.09600 0.03230  35  TYR A N   
251  C CA  . TYR A  41  ? 0.27530 0.35550 0.39080 0.01090  -0.09560 0.02520  35  TYR A CA  
252  C C   . TYR A  41  ? 0.21450 0.28880 0.29930 0.01010  -0.07320 0.03030  35  TYR A C   
253  O O   . TYR A  41  ? 0.22020 0.29940 0.30330 0.00970  -0.05830 0.03970  35  TYR A O   
254  C CB  . TYR A  41  ? 0.18910 0.27810 0.34990 0.00000  -0.09800 0.02760  35  TYR A CB  
255  C CG  . TYR A  41  ? 0.25570 0.35190 0.46020 -0.00090 -0.12110 0.02410  35  TYR A CG  
256  C CD1 . TYR A  41  ? 0.27610 0.36070 0.48180 0.00210  -0.14750 0.00810  35  TYR A CD1 
257  C CD2 . TYR A  41  ? 0.25120 0.36510 0.49670 -0.00320 -0.11780 0.03620  35  TYR A CD2 
258  C CE1 . TYR A  41  ? 0.29670 0.38130 0.53670 0.00140  -0.16580 0.00290  35  TYR A CE1 
259  C CE2 . TYR A  41  ? 0.22030 0.33660 0.50280 -0.00450 -0.13440 0.03280  35  TYR A CE2 
260  C CZ  . TYR A  41  ? 0.27450 0.37420 0.55320 -0.00300 -0.15750 0.01560  35  TYR A CZ  
261  O OH  . TYR A  41  ? 0.32020 0.41650 0.63250 -0.00410 -0.17260 0.01150  35  TYR A OH  
262  N N   . ALA A  42  ? 0.23610 0.29930 0.29960 0.01040  -0.07190 0.02370  36  ALA A N   
263  C CA  . ALA A  42  ? 0.23110 0.28950 0.27340 0.00920  -0.05250 0.02860  36  ALA A CA  
264  C C   . ALA A  42  ? 0.25730 0.30980 0.29650 0.00510  -0.05040 0.02360  36  ALA A C   
265  O O   . ALA A  42  ? 0.20940 0.25590 0.24760 0.00740  -0.06430 0.01410  36  ALA A O   
266  C CB  . ALA A  42  ? 0.27030 0.31900 0.27750 0.01960  -0.04690 0.02990  36  ALA A CB  
267  N N   . LEU A  43  ? 0.21320 0.26620 0.25060 0.00040  -0.03470 0.02890  37  LEU A N   
268  C CA  . LEU A  43  ? 0.22280 0.26920 0.25100 -0.00140 -0.02910 0.02560  37  LEU A CA  
269  C C   . LEU A  43  ? 0.24260 0.28400 0.25310 0.00180  -0.01530 0.03040  37  LEU A C   
270  O O   . LEU A  43  ? 0.18920 0.23290 0.20210 0.00140  -0.00870 0.03670  37  LEU A O   
271  C CB  . LEU A  43  ? 0.19600 0.24760 0.24570 -0.00980 -0.02500 0.02760  37  LEU A CB  
272  C CG  . LEU A  43  ? 0.20290 0.25940 0.27970 -0.01450 -0.03510 0.02610  37  LEU A CG  
273  C CD1 . LEU A  43  ? 0.19970 0.25920 0.29090 -0.01980 -0.02600 0.03130  37  LEU A CD1 
274  C CD2 . LEU A  43  ? 0.21320 0.26060 0.28360 -0.01160 -0.05040 0.01470  37  LEU A CD2 
275  N N   . GLY A  44  ? 0.23640 0.27030 0.23160 0.00580  -0.01090 0.02810  38  GLY A N   
276  C CA  . GLY A  44  ? 0.25150 0.28200 0.24020 0.00790  0.00340  0.03500  38  GLY A CA  
277  C C   . GLY A  44  ? 0.28500 0.31300 0.26210 0.01520  0.00770  0.04190  38  GLY A C   
278  O O   . GLY A  44  ? 0.29590 0.32010 0.25430 0.02480  0.00120  0.04020  38  GLY A O   
279  N N   . ASN A  45  ? 0.20490 0.23320 0.19320 0.01170  0.01690  0.04920  39  ASN A N   
280  C CA  . ASN A  45  ? 0.25900 0.28420 0.24130 0.01750  0.02200  0.05730  39  ASN A CA  
281  C C   . ASN A  45  ? 0.25570 0.28580 0.24820 0.01340  0.01520  0.05620  39  ASN A C   
282  O O   . ASN A  45  ? 0.20980 0.24030 0.21760 0.00770  0.01720  0.05670  39  ASN A O   
283  C CB  . ASN A  45  ? 0.23610 0.25680 0.23030 0.01670  0.03600  0.06670  39  ASN A CB  
284  C CG  . ASN A  45  ? 0.30290 0.31890 0.29480 0.02250  0.04220  0.07680  39  ASN A CG  
285  O OD1 . ASN A  45  ? 0.28300 0.29910 0.25930 0.02850  0.03640  0.07630  39  ASN A OD1 
286  N ND2 . ASN A  45  ? 0.26700 0.27860 0.27790 0.02100  0.05350  0.08640  39  ASN A ND2 
287  N N   . PRO A  46  ? 0.22670 0.26010 0.21170 0.01790  0.00630  0.05440  40  PRO A N   
288  C CA  . PRO A  46  ? 0.23430 0.27430 0.23240 0.01500  0.00180  0.05490  40  PRO A CA  
289  C C   . PRO A  46  ? 0.21930 0.25490 0.21800 0.01750  0.00820  0.06160  40  PRO A C   
290  O O   . PRO A  46  ? 0.24100 0.28060 0.24820 0.01710  0.00600  0.06210  40  PRO A O   
291  C CB  . PRO A  46  ? 0.23260 0.27770 0.22760 0.01980  -0.01060 0.05170  40  PRO A CB  
292  C CG  . PRO A  46  ? 0.25400 0.29030 0.22430 0.02930  -0.01220 0.05030  40  PRO A CG  
293  C CD  . PRO A  46  ? 0.24750 0.27850 0.21370 0.02680  -0.00240 0.05040  40  PRO A CD  
294  N N   . THR A  47  ? 0.21600 0.24290 0.20750 0.02130  0.01680  0.06790  41  THR A N   
295  C CA  . THR A  47  ? 0.22050 0.24080 0.21760 0.02300  0.02220  0.07460  41  THR A CA  
296  C C   . THR A  47  ? 0.23590 0.24930 0.25060 0.01740  0.02860  0.07640  41  THR A C   
297  O O   . THR A  47  ? 0.27030 0.27540 0.29460 0.01880  0.03360  0.08330  41  THR A O   
298  C CB  . THR A  47  ? 0.25920 0.27410 0.24030 0.03320  0.02710  0.08340  41  THR A CB  
299  O OG1 . THR A  47  ? 0.27490 0.28470 0.24710 0.03770  0.03700  0.08920  41  THR A OG1 
300  C CG2 . THR A  47  ? 0.25910 0.28000 0.22530 0.03990  0.01630  0.07960  41  THR A CG2 
301  N N   . ARG A  48  ? 0.21750 0.23360 0.23990 0.01140  0.02730  0.07060  42  ARG A N   
302  C CA  . ARG A  48  ? 0.22090 0.23120 0.26420 0.00610  0.02950  0.07030  42  ARG A CA  
303  C C   . ARG A  48  ? 0.23290 0.23530 0.28770 0.00600  0.02340  0.06780  42  ARG A C   
304  O O   . ARG A  48  ? 0.21210 0.21620 0.25870 0.00820  0.01610  0.06150  42  ARG A O   
305  C CB  . ARG A  48  ? 0.21240 0.22740 0.25910 0.00090  0.02510  0.06190  42  ARG A CB  
306  C CG  . ARG A  48  ? 0.21440 0.22360 0.28460 -0.00390 0.02350  0.05940  42  ARG A CG  
307  C CD  . ARG A  48  ? 0.18820 0.19980 0.25700 -0.00620 0.01540  0.04930  42  ARG A CD  
308  N NE  . ARG A  48  ? 0.16770 0.17450 0.25780 -0.00970 0.01140  0.04540  42  ARG A NE  
309  C CZ  . ARG A  48  ? 0.19400 0.19140 0.29440 -0.00820 0.00030  0.03830  42  ARG A CZ  
310  N NH1 . ARG A  48  ? 0.18440 0.17520 0.27350 -0.00220 -0.00590 0.03510  42  ARG A NH1 
311  N NH2 . ARG A  48  ? 0.16920 0.16250 0.29200 -0.01100 -0.00610 0.03370  42  ARG A NH2 
312  N N   . MET A  49  ? 0.19820 0.19130 0.27360 0.00500  0.02680  0.07360  43  MET A N   
313  C CA  A MET A  49  ? 0.23390 0.21550 0.32320 0.00550  0.01730  0.06850  43  MET A CA  
314  C CA  B MET A  49  ? 0.23390 0.21540 0.32340 0.00540  0.01730  0.06860  43  MET A CA  
315  C C   . MET A  49  ? 0.24200 0.22150 0.33330 0.00420  0.00530  0.05520  43  MET A C   
316  O O   . MET A  49  ? 0.19180 0.17260 0.29770 -0.00090 0.00450  0.05290  43  MET A O   
317  C CB  A MET A  49  ? 0.22850 0.19980 0.35000 0.00280  0.02140  0.07720  43  MET A CB  
318  C CB  B MET A  49  ? 0.22820 0.19990 0.35010 0.00260  0.02190  0.07750  43  MET A CB  
319  C CG  A MET A  49  ? 0.24560 0.20130 0.38600 0.00360  0.00720  0.06940  43  MET A CG  
320  C CG  B MET A  49  ? 0.24700 0.20340 0.38370 0.00480  0.01180  0.07420  43  MET A CG  
321  S SD  A MET A  49  ? 0.25800 0.20850 0.37160 0.01300  0.00320  0.06740  43  MET A SD  
322  S SD  B MET A  49  ? 0.27690 0.23270 0.38480 0.01370  0.01400  0.07790  43  MET A SD  
323  C CE  A MET A  49  ? 0.25290 0.19810 0.38370 0.01330  0.01680  0.08600  43  MET A CE  
324  C CE  B MET A  49  ? 0.26450 0.19880 0.39320 0.01660  -0.00090 0.07030  43  MET A CE  
325  N N   . THR A  50  ? 0.20120 0.17660 0.27690 0.01090  -0.00330 0.04740  44  THR A N   
326  C CA  . THR A  50  ? 0.18910 0.16320 0.25510 0.01450  -0.01210 0.03650  44  THR A CA  
327  C C   . THR A  50  ? 0.23300 0.19200 0.28960 0.02570  -0.02410 0.02740  44  THR A C   
328  O O   . THR A  50  ? 0.21730 0.17550 0.25950 0.03310  -0.02200 0.02990  44  THR A O   
329  C CB  . THR A  50  ? 0.23050 0.21980 0.27670 0.01530  -0.00540 0.03880  44  THR A CB  
330  O OG1 . THR A  50  ? 0.19210 0.19160 0.24400 0.00720  0.00240  0.04430  44  THR A OG1 
331  C CG2 . THR A  50  ? 0.20590 0.19400 0.24070 0.02110  -0.01090 0.03110  44  THR A CG2 
332  N N   . LEU A  51  ? 0.21720 0.16400 0.27940 0.02900  -0.03750 0.01620  45  LEU A N   
333  C CA  . LEU A  51  ? 0.23130 0.16130 0.27490 0.04450  -0.05130 0.00450  45  LEU A CA  
334  C C   . LEU A  51  ? 0.23260 0.17100 0.24250 0.05590  -0.04380 0.00600  45  LEU A C   
335  O O   . LEU A  51  ? 0.24400 0.19040 0.24720 0.05520  -0.04060 0.00600  45  LEU A O   
336  C CB  . LEU A  51  ? 0.24550 0.15970 0.30160 0.04720  -0.07030 -0.00940 45  LEU A CB  
337  C CG  . LEU A  51  ? 0.24910 0.15260 0.34860 0.03750  -0.08060 -0.01110 45  LEU A CG  
338  C CD1 . LEU A  51  ? 0.24930 0.14960 0.37350 0.03270  -0.09330 -0.01950 45  LEU A CD1 
339  C CD2 . LEU A  51  ? 0.27660 0.15660 0.37540 0.04860  -0.09710 -0.02080 45  LEU A CD2 
340  N N   . ALA A  52  ? 0.24310 0.17980 0.23480 0.06710  -0.03990 0.00900  46  ALA A N   
341  C CA  . ALA A  52  ? 0.29570 0.24230 0.26230 0.07880  -0.02920 0.01470  46  ALA A CA  
342  C C   . ALA A  52  ? 0.35050 0.28260 0.29050 0.09810  -0.03730 0.00530  46  ALA A C   
343  O O   . ALA A  52  ? 0.28620 0.22750 0.20980 0.10660  -0.02650 0.01190  46  ALA A O   
344  C CB  . ALA A  52  ? 0.25430 0.20430 0.21310 0.08630  -0.02180 0.02200  46  ALA A CB  
345  N N   . ARG A  53  ? 0.27180 0.29170 0.18470 0.10160  0.06640  0.04290  47  ARG A N   
346  C CA  . ARG A  53  ? 0.26150 0.27730 0.19200 0.09080  0.06450  0.04080  47  ARG A CA  
347  C C   . ARG A  53  ? 0.27120 0.27610 0.20380 0.08320  0.05550  0.03350  47  ARG A C   
348  O O   . ARG A  53  ? 0.25040 0.25400 0.18090 0.08260  0.05370  0.03550  47  ARG A O   
349  C CB  . ARG A  53  ? 0.25750 0.27510 0.18740 0.09500  0.06530  0.03610  47  ARG A CB  
350  C CG  . ARG A  53  ? 0.28800 0.31920 0.21540 0.10510  0.07560  0.04390  47  ARG A CG  
351  C CD  . ARG A  53  ? 0.27210 0.31420 0.22090 0.09870  0.08400  0.05800  47  ARG A CD  
352  N NE  . ARG A  53  ? 0.25480 0.29320 0.22110 0.08860  0.08000  0.05570  47  ARG A NE  
353  C CZ  . ARG A  53  ? 0.24390 0.28530 0.21510 0.09090  0.08000  0.05260  47  ARG A CZ  
354  N NH1 . ARG A  53  ? 0.25610 0.30470 0.21750 0.10340  0.08490  0.05140  47  ARG A NH1 
355  N NH2 . ARG A  53  ? 0.24910 0.28570 0.23410 0.08150  0.07470  0.05040  47  ARG A NH2 
356  N N   . SER A  54  ? 0.25840 0.25670 0.19500 0.07850  0.04980  0.02590  48  SER A N   
357  C CA  A SER A  54  ? 0.27410 0.26490 0.21490 0.07150  0.04320  0.02150  48  SER A CA  
358  C CA  B SER A  54  ? 0.27390 0.26470 0.21470 0.07160  0.04300  0.02130  48  SER A CA  
359  C C   . SER A  54  ? 0.28570 0.27300 0.21720 0.07550  0.03580  0.01610  48  SER A C   
360  O O   . SER A  54  ? 0.28700 0.27100 0.22490 0.07000  0.03100  0.01450  48  SER A O   
361  C CB  A SER A  54  ? 0.29200 0.27760 0.23920 0.06610  0.03950  0.01680  48  SER A CB  
362  C CB  B SER A  54  ? 0.29290 0.27840 0.23950 0.06660  0.03930  0.01640  48  SER A CB  
363  O OG  A SER A  54  ? 0.29190 0.27640 0.23290 0.07210  0.03790  0.01240  48  SER A OG  
364  O OG  B SER A  54  ? 0.32380 0.31050 0.28080 0.06030  0.04300  0.02050  48  SER A OG  
365  N N   . ALA A  55  ? 0.27410 0.26220 0.19100 0.08520  0.03410  0.01300  49  ALA A N   
366  C CA  . ALA A  55  ? 0.26920 0.25330 0.17730 0.08880  0.02490  0.00770  49  ALA A CA  
367  C C   . ALA A  55  ? 0.30560 0.29400 0.21510 0.08800  0.02660  0.01430  49  ALA A C   
368  O O   . ALA A  55  ? 0.28240 0.26840 0.19020 0.08860  0.01800  0.01110  49  ALA A O   
369  C CB  . ALA A  55  ? 0.29250 0.27510 0.18040 0.10150  0.02160  0.00150  49  ALA A CB  
370  N N   . ALA A  56  ? 0.26840 0.26270 0.18310 0.08660  0.03630  0.02390  50  ALA A N   
371  C CA  . ALA A  56  ? 0.28570 0.28230 0.20410 0.08550  0.03770  0.03070  50  ALA A CA  
372  C C   . ALA A  56  ? 0.28060 0.27400 0.21500 0.07620  0.03610  0.03050  50  ALA A C   
373  O O   . ALA A  56  ? 0.30600 0.30030 0.24480 0.07580  0.03660  0.03520  50  ALA A O   
374  C CB  . ALA A  56  ? 0.26370 0.26670 0.18290 0.08780  0.04790  0.04210  50  ALA A CB  
375  N N   . LYS A  57  ? 0.23960 0.22960 0.18220 0.06990  0.03490  0.02580  51  LYS A N   
376  C CA  . LYS A  57  ? 0.22670 0.21500 0.18200 0.06310  0.03580  0.02670  51  LYS A CA  
377  C C   . LYS A  57  ? 0.24290 0.23240 0.20300 0.06300  0.03060  0.02620  51  LYS A C   
378  O O   . LYS A  57  ? 0.26600 0.25600 0.23440 0.06100  0.03370  0.02930  51  LYS A O   
379  C CB  . LYS A  57  ? 0.26980 0.25500 0.23050 0.05750  0.03550  0.02280  51  LYS A CB  
380  C CG  . LYS A  57  ? 0.29400 0.27860 0.25660 0.05530  0.04110  0.02520  51  LYS A CG  
381  C CD  . LYS A  57  ? 0.28050 0.26250 0.24470 0.05200  0.03930  0.02120  51  LYS A CD  
382  C CE  . LYS A  57  ? 0.28810 0.26990 0.25580 0.04960  0.04320  0.02350  51  LYS A CE  
383  N NZ  . LYS A  57  ? 0.33680 0.31670 0.30430 0.04820  0.04090  0.02030  51  LYS A NZ  
384  N N   . PRO A  58  ? 0.30090 0.29090 0.25750 0.06560  0.02230  0.02220  52  PRO A N   
385  C CA  . PRO A  58  ? 0.31810 0.31140 0.28290 0.06550  0.01730  0.02350  52  PRO A CA  
386  C C   . PRO A  58  ? 0.28830 0.28410 0.25030 0.07020  0.02030  0.02970  52  PRO A C   
387  O O   . PRO A  58  ? 0.25100 0.24950 0.22370 0.06930  0.02070  0.03260  52  PRO A O   
388  C CB  . PRO A  58  ? 0.28780 0.27990 0.24860 0.06770  0.00550  0.01760  52  PRO A CB  
389  C CG  . PRO A  58  ? 0.26900 0.25570 0.22690 0.06540  0.00460  0.01240  52  PRO A CG  
390  C CD  . PRO A  58  ? 0.30900 0.29560 0.25860 0.06730  0.01550  0.01550  52  PRO A CD  
391  N N   . ALA A  59  ? 0.28130 0.27700 0.22980 0.07600  0.02270  0.03270  53  ALA A N   
392  C CA  . ALA A  59  ? 0.28150 0.27900 0.22860 0.08000  0.02620  0.04090  53  ALA A CA  
393  C C   . ALA A  59  ? 0.26050 0.25530 0.21930 0.07540  0.03410  0.04550  53  ALA A C   
394  O O   . ALA A  59  ? 0.28600 0.28020 0.25140 0.07660  0.03510  0.05040  53  ALA A O   
395  C CB  . ALA A  59  ? 0.29660 0.29610 0.22690 0.08740  0.02890  0.04530  53  ALA A CB  
396  N N   . GLN A  60  ? 0.27410 0.26620 0.23520 0.07080  0.03880  0.04370  54  GLN A N   
397  C CA  . GLN A  60  ? 0.26740 0.25490 0.23850 0.06670  0.04390  0.04610  54  GLN A CA  
398  C C   . GLN A  60  ? 0.30420 0.29030 0.28430 0.06440  0.04250  0.04200  54  GLN A C   
399  O O   . GLN A  60  ? 0.26840 0.25050 0.25510 0.06490  0.04470  0.04400  54  GLN A O   
400  C CB  . GLN A  60  ? 0.26770 0.25300 0.23930 0.06260  0.04750  0.04490  54  GLN A CB  
401  C CG  . GLN A  60  ? 0.27370 0.26240 0.24110 0.06530  0.05150  0.05220  54  GLN A CG  
402  C CD  . GLN A  60  ? 0.27400 0.26420 0.24110 0.06290  0.05360  0.05010  54  GLN A CD  
403  O OE1 . GLN A  60  ? 0.27830 0.26870 0.24100 0.06250  0.05060  0.04280  54  GLN A OE1 
404  N NE2 . GLN A  60  ? 0.27840 0.27010 0.25270 0.06120  0.05830  0.05720  54  GLN A NE2 
405  N N   . ALA A  61  ? 0.25950 0.24910 0.24070 0.06270  0.03880  0.03670  55  ALA A N   
406  C CA  . ALA A  61  ? 0.27650 0.26860 0.26780 0.06160  0.03880  0.03510  55  ALA A CA  
407  C C   . ALA A  61  ? 0.29010 0.28590 0.28740 0.06620  0.03660  0.03870  55  ALA A C   
408  O O   . ALA A  61  ? 0.30960 0.30630 0.31570 0.06760  0.03950  0.03920  55  ALA A O   
409  C CB  . ALA A  61  ? 0.23920 0.23550 0.23400 0.05820  0.03500  0.03150  55  ALA A CB  
410  N N   . LEU A  62  ? 0.28530 0.28370 0.27710 0.06970  0.03130  0.04100  56  LEU A N   
411  C CA  . LEU A  62  ? 0.29880 0.30070 0.29610 0.07450  0.02830  0.04510  56  LEU A CA  
412  C C   . LEU A  62  ? 0.30870 0.30450 0.30770 0.07710  0.03390  0.05010  56  LEU A C   
413  O O   . LEU A  62  ? 0.28010 0.27670 0.28920 0.07990  0.03480  0.05160  56  LEU A O   
414  C CB  . LEU A  62  ? 0.28720 0.29210 0.27460 0.07880  0.02040  0.04640  56  LEU A CB  
415  C CG  . LEU A  62  ? 0.31770 0.32610 0.30870 0.08470  0.01600  0.05190  56  LEU A CG  
416  C CD1 . LEU A  62  ? 0.30800 0.32390 0.31700 0.08360  0.01210  0.05040  56  LEU A CD1 
417  C CD2 . LEU A  62  ? 0.29990 0.30990 0.27560 0.09030  0.00820  0.05320  56  LEU A CD2 
418  N N   . ALA A  63  ? 0.28020 0.26990 0.27160 0.07630  0.03760  0.05310  57  ALA A N   
419  C CA  . ALA A  63  ? 0.28250 0.26440 0.27860 0.07740  0.04160  0.05820  57  ALA A CA  
420  C C   . ALA A  63  ? 0.30460 0.28070 0.30920 0.07580  0.04450  0.05280  57  ALA A C   
421  O O   . ALA A  63  ? 0.29790 0.26800 0.30920 0.07920  0.04530  0.05460  57  ALA A O   
422  C CB  . ALA A  63  ? 0.29090 0.26890 0.28170 0.07520  0.04500  0.06330  57  ALA A CB  
423  N N   . ILE A  64  ? 0.26040 0.23750 0.26340 0.07160  0.04600  0.04620  58  ILE A N   
424  C CA  . ILE A  64  ? 0.29440 0.26710 0.30150 0.07180  0.04900  0.04070  58  ILE A CA  
425  C C   . ILE A  64  ? 0.28810 0.26770 0.30340 0.07700  0.04950  0.04050  58  ILE A C   
426  O O   . ILE A  64  ? 0.30340 0.27780 0.32310 0.08190  0.05180  0.03920  58  ILE A O   
427  C CB  . ILE A  64  ? 0.25940 0.23340 0.26160 0.06690  0.05040  0.03530  58  ILE A CB  
428  C CG1 . ILE A  64  ? 0.24670 0.21410 0.24360 0.06240  0.05020  0.03560  58  ILE A CG1 
429  C CG2 . ILE A  64  ? 0.25150 0.22380 0.25470 0.06890  0.05400  0.03010  58  ILE A CG2 
430  C CD1 . ILE A  64  ? 0.24530 0.21610 0.23720 0.05800  0.05010  0.03180  58  ILE A CD1 
431  N N   . LEU A  65  ? 0.23170 0.22320 0.25080 0.07640  0.04670  0.04160  59  LEU A N   
432  C CA  . LEU A  65  ? 0.28440 0.28580 0.31570 0.08050  0.04720  0.04250  59  LEU A CA  
433  C C   . LEU A  65  ? 0.30030 0.30140 0.33800 0.08710  0.04510  0.04710  59  LEU A C   
434  O O   . LEU A  65  ? 0.34480 0.35170 0.39380 0.09270  0.04740  0.04790  59  LEU A O   
435  C CB  . LEU A  65  ? 0.27990 0.29350 0.31740 0.07670  0.04250  0.04330  59  LEU A CB  
436  C CG  . LEU A  65  ? 0.29980 0.31460 0.33490 0.07090  0.04520  0.04000  59  LEU A CG  
437  C CD1 . LEU A  65  ? 0.32560 0.34850 0.36700 0.06640  0.03790  0.04080  59  LEU A CD1 
438  C CD2 . LEU A  65  ? 0.33490 0.35370 0.37570 0.07340  0.05340  0.03940  59  LEU A CD2 
439  N N   . GLU A  66  ? 0.28830 0.28360 0.31950 0.08760  0.04140  0.05130  60  GLU A N   
440  C CA  . GLU A  66  ? 0.35120 0.34520 0.38790 0.09410  0.03900  0.05710  60  GLU A CA  
441  C C   . GLU A  66  ? 0.35420 0.33410 0.39220 0.09740  0.04290  0.05730  60  GLU A C   
442  O O   . GLU A  66  ? 0.29430 0.27080 0.33830 0.10350  0.04120  0.06220  60  GLU A O   
443  C CB  . GLU A  66  ? 0.34030 0.33510 0.36830 0.09440  0.03330  0.06330  60  GLU A CB  
444  C CG  . GLU A  66  ? 0.34590 0.35270 0.37360 0.09360  0.02610  0.06230  60  GLU A CG  
445  C CD  . GLU A  66  ? 0.38060 0.38770 0.39600 0.09670  0.01990  0.06760  60  GLU A CD  
446  O OE1 . GLU A  66  ? 0.40780 0.40780 0.41160 0.09630  0.02360  0.07120  60  GLU A OE1 
447  O OE2 . GLU A  66  ? 0.42080 0.43600 0.43870 0.10010  0.01130  0.06880  60  GLU A OE2 
448  N N   . THR A  67  ? 0.28170 0.25220 0.31470 0.09400  0.04680  0.05170  61  THR A N   
449  C CA  . THR A  67  ? 0.29190 0.24650 0.32650 0.09690  0.04820  0.05010  61  THR A CA  
450  C C   . THR A  67  ? 0.31920 0.27370 0.36080 0.10550  0.05110  0.04530  61  THR A C   
451  O O   . THR A  67  ? 0.31730 0.28160 0.35940 0.10680  0.05510  0.04050  61  THR A O   
452  C CB  . THR A  67  ? 0.28830 0.23320 0.31550 0.09070  0.04940  0.04460  61  THR A CB  
453  O OG1 . THR A  67  ? 0.34640 0.29280 0.36920 0.08420  0.04770  0.05050  61  THR A OG1 
454  C CG2 . THR A  67  ? 0.28870 0.21480 0.31830 0.09360  0.04830  0.04130  61  THR A CG2 
455  N N   . GLU A  68  ? 0.32120 0.26510 0.36890 0.11200  0.04940  0.04770  62  GLU A N   
456  C CA  . GLU A  68  ? 0.34630 0.28870 0.40070 0.12260  0.05230  0.04310  62  GLU A CA  
457  C C   . GLU A  68  ? 0.35540 0.29220 0.40160 0.12450  0.05710  0.03180  62  GLU A C   
458  O O   . GLU A  68  ? 0.36250 0.28360 0.40030 0.12060  0.05510  0.02670  62  GLU A O   
459  C CB  . GLU A  68  ? 0.36640 0.29160 0.42680 0.12840  0.04850  0.04620  62  GLU A CB  
460  C CG  . GLU A  68  ? 0.32030 0.25040 0.38790 0.12900  0.04410  0.05850  62  GLU A CG  
461  C CD  . GLU A  68  ? 0.31710 0.24380 0.37880 0.11990  0.04080  0.06700  62  GLU A CD  
462  O OE1 . GLU A  68  ? 0.33930 0.26600 0.39240 0.11150  0.04220  0.06380  62  GLU A OE1 
463  O OE2 . GLU A  68  ? 0.32380 0.24970 0.38940 0.12200  0.03720  0.07790  62  GLU A OE2 
464  N N   . GLY A  69  ? 0.32170 0.27200 0.37100 0.13130  0.06330  0.02880  63  GLY A N   
465  C CA  . GLY A  69  ? 0.35170 0.29880 0.39100 0.13610  0.06910  0.01910  63  GLY A CA  
466  C C   . GLY A  69  ? 0.35550 0.31350 0.38680 0.12820  0.07240  0.01790  63  GLY A C   
467  O O   . GLY A  69  ? 0.39290 0.35460 0.41680 0.13350  0.07900  0.01250  63  GLY A O   
468  N N   . VAL A  70  ? 0.29090 0.25360 0.32220 0.11670  0.06830  0.02310  64  VAL A N   
469  C CA  . VAL A  70  ? 0.33310 0.30390 0.35740 0.10960  0.07060  0.02190  64  VAL A CA  
470  C C   . VAL A  70  ? 0.30190 0.29340 0.33430 0.11270  0.07740  0.02500  64  VAL A C   
471  O O   . VAL A  70  ? 0.33150 0.32790 0.35700 0.11150  0.08230  0.02300  64  VAL A O   
472  C CB  . VAL A  70  ? 0.30440 0.27640 0.32800 0.09850  0.06470  0.02660  64  VAL A CB  
473  C CG1 . VAL A  70  ? 0.30070 0.28290 0.32060 0.09180  0.06650  0.02650  64  VAL A CG1 
474  C CG2 . VAL A  70  ? 0.33270 0.28640 0.34890 0.09460  0.06010  0.02440  64  VAL A CG2 
475  N N   . ALA A  71  ? 0.36860 0.37330 0.41730 0.11670  0.07770  0.03120  65  ALA A N   
476  C CA  . ALA A  71  ? 0.32020 0.34660 0.38210 0.11950  0.08410  0.03600  65  ALA A CA  
477  C C   . ALA A  71  ? 0.33150 0.35960 0.38610 0.12940  0.09490  0.03160  65  ALA A C   
478  O O   . ALA A  71  ? 0.36530 0.41010 0.42520 0.12940  0.10210  0.03600  65  ALA A O   
479  C CB  . ALA A  71  ? 0.34750 0.38640 0.42970 0.12410  0.08180  0.04280  65  ALA A CB  
480  N N   . GLY A  72  ? 0.37500 0.38560 0.41710 0.13830  0.09590  0.02330  66  GLY A N   
481  C CA  . GLY A  72  ? 0.36800 0.37860 0.39900 0.15040  0.10550  0.01740  66  GLY A CA  
482  C C   . GLY A  72  ? 0.38590 0.39410 0.39860 0.14660  0.10860  0.01360  66  GLY A C   
483  O O   . GLY A  72  ? 0.37800 0.39140 0.38070 0.15690  0.11810  0.01100  66  GLY A O   
484  N N   . TYR A  73  ? 0.37150 0.37170 0.37820 0.13350  0.10100  0.01340  67  TYR A N   
485  C CA  . TYR A  73  ? 0.34970 0.34710 0.33930 0.13030  0.10300  0.01020  67  TYR A CA  
486  C C   . TYR A  73  ? 0.36840 0.38840 0.36650 0.12650  0.11030  0.02000  67  TYR A C   
487  O O   . TYR A  73  ? 0.37850 0.39920 0.36260 0.12640  0.11410  0.01910  67  TYR A O   
488  C CB  . TYR A  73  ? 0.38210 0.36390 0.36410 0.11840  0.09250  0.00690  67  TYR A CB  
489  C CG  . TYR A  73  ? 0.39360 0.35200 0.36760 0.12100  0.08510  -0.00200 67  TYR A CG  
490  C CD1 . TYR A  73  ? 0.42320 0.36800 0.38190 0.13230  0.08630  -0.01230 67  TYR A CD1 
491  C CD2 . TYR A  73  ? 0.35210 0.30160 0.33380 0.11260  0.07660  0.00040  67  TYR A CD2 
492  C CE1 . TYR A  73  ? 0.50050 0.42170 0.45480 0.13390  0.07750  -0.02050 67  TYR A CE1 
493  C CE2 . TYR A  73  ? 0.38560 0.31410 0.36400 0.11390  0.06960  -0.00550 67  TYR A CE2 
494  C CZ  . TYR A  73  ? 0.46600 0.37970 0.43220 0.12390  0.06930  -0.01610 67  TYR A CZ  
495  O OH  . TYR A  73  ? 0.55750 0.44830 0.52320 0.12440  0.06040  -0.02200 67  TYR A OH  
496  N N   . GLY A  74  ? 0.29200 0.32990 0.31340 0.12310  0.11110  0.02980  68  GLY A N   
497  C CA  . GLY A  74  ? 0.36860 0.42760 0.40290 0.11830  0.11670  0.04040  68  GLY A CA  
498  C C   . GLY A  74  ? 0.34600 0.40190 0.37690 0.10490  0.11050  0.04250  68  GLY A C   
499  O O   . GLY A  74  ? 0.33800 0.40410 0.36890 0.10290  0.11630  0.04870  68  GLY A O   
500  N N   . PHE A  75  ? 0.30010 0.34280 0.32840 0.09640  0.09940  0.03850  69  PHE A N   
501  C CA  . PHE A  75  ? 0.31400 0.35600 0.34300 0.08470  0.09340  0.04110  69  PHE A CA  
502  C C   . PHE A  75  ? 0.31380 0.37390 0.36650 0.07910  0.09260  0.05150  69  PHE A C   
503  O O   . PHE A  75  ? 0.33250 0.40220 0.40270 0.08110  0.09110  0.05510  69  PHE A O   
504  C CB  . PHE A  75  ? 0.33760 0.36480 0.36090 0.07870  0.08290  0.03580  69  PHE A CB  
505  C CG  . PHE A  75  ? 0.35770 0.36680 0.36230 0.08150  0.08160  0.02710  69  PHE A CG  
506  C CD1 . PHE A  75  ? 0.31720 0.31920 0.30600 0.08100  0.08310  0.02320  69  PHE A CD1 
507  C CD2 . PHE A  75  ? 0.28260 0.28110 0.28670 0.08410  0.07740  0.02360  69  PHE A CD2 
508  C CE1 . PHE A  75  ? 0.33670 0.32170 0.31110 0.08260  0.07950  0.01500  69  PHE A CE1 
509  C CE2 . PHE A  75  ? 0.30750 0.28870 0.29850 0.08500  0.07450  0.01660  69  PHE A CE2 
510  C CZ  . PHE A  75  ? 0.31050 0.28500 0.28740 0.08420  0.07500  0.01180  69  PHE A CZ  
511  N N   . ASP A  76  ? 0.26800 0.33300 0.32320 0.07230  0.09300  0.05670  70  ASP A N   
512  C CA  . ASP A  76  ? 0.27170 0.35220 0.35220 0.06550  0.09050  0.06700  70  ASP A CA  
513  C C   . ASP A  76  ? 0.23020 0.30160 0.31280 0.05510  0.07720  0.06450  70  ASP A C   
514  O O   . ASP A  76  ? 0.28200 0.33780 0.34760 0.05410  0.07150  0.05600  70  ASP A O   
515  C CB  . ASP A  76  ? 0.29110 0.38540 0.37780 0.06580  0.10070  0.07720  70  ASP A CB  
516  C CG  . ASP A  76  ? 0.31040 0.39400 0.37780 0.06240  0.10110  0.07540  70  ASP A CG  
517  O OD1 . ASP A  76  ? 0.30740 0.37400 0.36040 0.05810  0.09240  0.06670  70  ASP A OD1 
518  O OD2 . ASP A  76  ? 0.31430 0.40810 0.38180 0.06450  0.11070  0.08400  70  ASP A OD2 
519  N N   . ASP A  77  ? 0.25780 0.33930 0.36300 0.04800  0.07170  0.07220  71  ASP A N   
520  C CA  . ASP A  77  ? 0.26330 0.33520 0.37030 0.04000  0.05760  0.06840  71  ASP A CA  
521  C C   . ASP A  77  ? 0.26790 0.32490 0.35460 0.03690  0.05630  0.06320  71  ASP A C   
522  O O   . ASP A  77  ? 0.24490 0.28890 0.31890 0.03580  0.04850  0.05510  71  ASP A O   
523  C CB  . ASP A  77  ? 0.28890 0.37220 0.42470 0.03240  0.05070  0.07740  71  ASP A CB  
524  C CG  . ASP A  77  ? 0.34680 0.44410 0.50560 0.03430  0.04720  0.08150  71  ASP A CG  
525  O OD1 . ASP A  77  ? 0.29700 0.39350 0.44760 0.04170  0.04930  0.07680  71  ASP A OD1 
526  O OD2 . ASP A  77  ? 0.45820 0.56720 0.64520 0.02810  0.04160  0.09010  71  ASP A OD2 
527  N N   . ALA A  78  ? 0.24810 0.30780 0.33140 0.03630  0.06440  0.06850  72  ALA A N   
528  C CA  . ALA A  78  ? 0.26680 0.31320 0.33210 0.03380  0.06250  0.06410  72  ALA A CA  
529  C C   . ALA A  78  ? 0.27540 0.30950 0.31710 0.03900  0.06380  0.05380  72  ALA A C   
530  O O   . ALA A  78  ? 0.25830 0.28050 0.28890 0.03650  0.05780  0.04790  72  ALA A O   
531  C CB  . ALA A  78  ? 0.28280 0.33530 0.34790 0.03330  0.07100  0.07290  72  ALA A CB  
532  N N   . ASP A  79  ? 0.27010 0.30670 0.30540 0.04650  0.07130  0.05200  73  ASP A N   
533  C CA  . ASP A  79  ? 0.26520 0.28940 0.28270 0.05060  0.07080  0.04290  73  ASP A CA  
534  C C   . ASP A  79  ? 0.27540 0.29300 0.29430 0.04820  0.06210  0.03860  73  ASP A C   
535  O O   . ASP A  79  ? 0.29180 0.29880 0.29910 0.04720  0.05870  0.03340  73  ASP A O   
536  C CB  . ASP A  79  ? 0.28380 0.31060 0.29770 0.05960  0.07840  0.04140  73  ASP A CB  
537  C CG  . ASP A  79  ? 0.30630 0.33810 0.31170 0.06500  0.08810  0.04400  73  ASP A CG  
538  O OD1 . ASP A  79  ? 0.28580 0.31480 0.28220 0.06200  0.08820  0.04530  73  ASP A OD1 
539  O OD2 . ASP A  79  ? 0.31820 0.35660 0.32470 0.07380  0.09570  0.04460  73  ASP A OD2 
540  N N   . ILE A  80  ? 0.27600 0.30120 0.30940 0.04810  0.05850  0.04140  74  ILE A N   
541  C CA  . ILE A  80  ? 0.26600 0.28560 0.29750 0.04760  0.05050  0.03770  74  ILE A CA  
542  C C   . ILE A  80  ? 0.27770 0.29070 0.30440 0.04250  0.04330  0.03520  74  ILE A C   
543  O O   . ILE A  80  ? 0.22140 0.22630 0.23680 0.04340  0.04030  0.03090  74  ILE A O   
544  C CB  . ILE A  80  ? 0.28700 0.31620 0.33440 0.04900  0.04650  0.04120  74  ILE A CB  
545  C CG1 . ILE A  80  ? 0.30720 0.34090 0.35720 0.05610  0.05390  0.04260  74  ILE A CG1 
546  C CG2 . ILE A  80  ? 0.26280 0.28640 0.30530 0.04910  0.03700  0.03780  74  ILE A CG2 
547  C CD1 . ILE A  80  ? 0.32670 0.37500 0.39790 0.05800  0.05270  0.04850  74  ILE A CD1 
548  N N   . ALA A  81  ? 0.25070 0.26740 0.28710 0.03750  0.04070  0.03860  75  ALA A N   
549  C CA  . ALA A  81  ? 0.26310 0.27190 0.29510 0.03360  0.03390  0.03570  75  ALA A CA  
550  C C   . ALA A  81  ? 0.26210 0.26210 0.27720 0.03480  0.03740  0.03170  75  ALA A C   
551  O O   . ALA A  81  ? 0.25110 0.24410 0.25840 0.03510  0.03270  0.02730  75  ALA A O   
552  C CB  . ALA A  81  ? 0.22350 0.23650 0.26970 0.02790  0.03220  0.04170  75  ALA A CB  
553  N N   . LEU A  82  ? 0.24940 0.25000 0.25910 0.03610  0.04520  0.03320  76  LEU A N   
554  C CA  . LEU A  82  ? 0.26890 0.26140 0.26480 0.03680  0.04660  0.02930  76  LEU A CA  
555  C C   . LEU A  82  ? 0.25970 0.24750 0.24930 0.03970  0.04590  0.02530  76  LEU A C   
556  O O   . LEU A  82  ? 0.28180 0.26420 0.26490 0.03930  0.04400  0.02280  76  LEU A O   
557  C CB  . LEU A  82  ? 0.29210 0.28500 0.28150 0.03850  0.05320  0.03060  76  LEU A CB  
558  C CG  . LEU A  82  ? 0.27670 0.26170 0.25470 0.03760  0.05170  0.02760  76  LEU A CG  
559  C CD1 . LEU A  82  ? 0.25720 0.24200 0.23810 0.03350  0.04850  0.03080  76  LEU A CD1 
560  C CD2 . LEU A  82  ? 0.26940 0.25190 0.23620 0.04140  0.05630  0.02580  76  LEU A CD2 
561  N N   . MET A  83  ? 0.24600 0.23650 0.23880 0.04300  0.04760  0.02590  77  MET A N   
562  C CA  . MET A  83  ? 0.25950 0.24610 0.24840 0.04550  0.04650  0.02450  77  MET A CA  
563  C C   . MET A  83  ? 0.28610 0.27220 0.27260 0.04510  0.04130  0.02370  77  MET A C   
564  O O   . MET A  83  ? 0.27560 0.25850 0.25640 0.04630  0.04160  0.02340  77  MET A O   
565  C CB  . MET A  83  ? 0.23400 0.22420 0.22870 0.04940  0.04790  0.02640  77  MET A CB  
566  C CG  . MET A  83  ? 0.21740 0.20670 0.21220 0.05240  0.05340  0.02590  77  MET A CG  
567  S SD  . MET A  83  ? 0.34250 0.33470 0.34490 0.05830  0.05430  0.02810  77  MET A SD  
568  C CE  . MET A  83  ? 0.33150 0.32230 0.33200 0.06370  0.06150  0.02570  77  MET A CE  
569  N N   . CYS A  84  ? 0.26860 0.25790 0.26000 0.04380  0.03620  0.02360  78  CYS A N   
570  C CA  . CYS A  84  ? 0.25400 0.24140 0.24090 0.04530  0.02970  0.02100  78  CYS A CA  
571  C C   . CYS A  84  ? 0.26330 0.24590 0.24560 0.04370  0.02800  0.01820  78  CYS A C   
572  O O   . CYS A  84  ? 0.29840 0.27830 0.27670 0.04590  0.02180  0.01470  78  CYS A O   
573  C CB  . CYS A  84  ? 0.28270 0.27370 0.27820 0.04480  0.02210  0.02080  78  CYS A CB  
574  S SG  . CYS A  84  ? 0.28710 0.28480 0.28840 0.04840  0.02230  0.02410  78  CYS A SG  
575  N N   . ALA A  85  ? 0.30290 0.28380 0.28480 0.04100  0.03230  0.01910  79  ALA A N   
576  C CA  . ALA A  85  ? 0.27770 0.25460 0.25870 0.03890  0.02980  0.01770  79  ALA A CA  
577  C C   . ALA A  85  ? 0.29830 0.27280 0.27210 0.04120  0.03150  0.01600  79  ALA A C   
578  O O   . ALA A  85  ? 0.28080 0.25660 0.25280 0.04200  0.03590  0.01750  79  ALA A O   
579  C CB  . ALA A  85  ? 0.25720 0.23480 0.24210 0.03500  0.03280  0.02090  79  ALA A CB  
580  N N   . SER A  86  ? 0.28380 0.25480 0.25600 0.04220  0.02750  0.01340  80  SER A N   
581  C CA  . SER A  86  ? 0.29970 0.26960 0.26950 0.04310  0.02920  0.01330  80  SER A CA  
582  C C   . SER A  86  ? 0.25280 0.21880 0.22630 0.03920  0.02650  0.01420  80  SER A C   
583  O O   . SER A  86  ? 0.28050 0.24180 0.25490 0.04020  0.02160  0.01220  80  SER A O   
584  C CB  . SER A  86  ? 0.29860 0.26820 0.26310 0.04950  0.02780  0.01010  80  SER A CB  
585  O OG  . SER A  86  ? 0.27660 0.25100 0.23660 0.05370  0.03140  0.01140  80  SER A OG  
586  N N   . HIS A  87  ? 0.24260 0.20990 0.21730 0.03550  0.02960  0.01750  81  HIS A N   
587  C CA  . HIS A  87  ? 0.26390 0.22870 0.24140 0.03210  0.02770  0.02050  81  HIS A CA  
588  C C   . HIS A  87  ? 0.26680 0.22850 0.24190 0.03260  0.02600  0.02060  81  HIS A C   
589  O O   . HIS A  87  ? 0.22030 0.18330 0.19320 0.03490  0.02700  0.01860  81  HIS A O   
590  C CB  . HIS A  87  ? 0.27640 0.24500 0.25410 0.02990  0.03230  0.02470  81  HIS A CB  
591  C CG  . HIS A  87  ? 0.26490 0.23370 0.23500 0.03110  0.03610  0.02360  81  HIS A CG  
592  N ND1 . HIS A  87  ? 0.27120 0.23720 0.23610 0.03090  0.03470  0.02350  81  HIS A ND1 
593  C CD2 . HIS A  87  ? 0.26450 0.23480 0.23220 0.03270  0.03970  0.02220  81  HIS A CD2 
594  C CE1 . HIS A  87  ? 0.26570 0.23090 0.22510 0.03200  0.03640  0.02140  81  HIS A CE1 
595  N NE2 . HIS A  87  ? 0.23690 0.20400 0.19790 0.03320  0.03960  0.02040  81  HIS A NE2 
596  N N   . SER A  88  ? 0.25820 0.21640 0.23610 0.03030  0.02300  0.02390  82  SER A N   
597  C CA  . SER A  88  ? 0.27130 0.22580 0.24810 0.03080  0.02020  0.02520  82  SER A CA  
598  C C   . SER A  88  ? 0.26580 0.22240 0.23610 0.02970  0.02260  0.02820  82  SER A C   
599  O O   . SER A  88  ? 0.26950 0.22360 0.23860 0.03010  0.01950  0.03010  82  SER A O   
600  C CB  . SER A  88  ? 0.28440 0.23300 0.26780 0.02870  0.01520  0.02870  82  SER A CB  
601  O OG  . SER A  88  ? 0.28060 0.22410 0.26830 0.03110  0.01000  0.02350  82  SER A OG  
602  N N   . SER A  89  ? 0.25220 0.21240 0.21760 0.02930  0.02710  0.02790  83  SER A N   
603  C CA  . SER A  89  ? 0.25310 0.21310 0.20920 0.02970  0.02790  0.02890  83  SER A CA  
604  C C   . SER A  89  ? 0.33040 0.28960 0.28250 0.02900  0.02780  0.03570  83  SER A C   
605  O O   . SER A  89  ? 0.28880 0.24610 0.23270 0.03010  0.02520  0.03700  83  SER A O   
606  C CB  . SER A  89  ? 0.27390 0.23260 0.22940 0.03070  0.02360  0.02560  83  SER A CB  
607  O OG  . SER A  89  ? 0.30690 0.26780 0.26890 0.03130  0.02440  0.02200  83  SER A OG  
608  N N   . GLU A  90  ? 0.24300 0.20370 0.20210 0.02700  0.02980  0.04120  84  GLU A N   
609  C CA  . GLU A  90  ? 0.26630 0.22850 0.22280 0.02620  0.03190  0.05040  84  GLU A CA  
610  C C   . GLU A  90  ? 0.30230 0.26940 0.24540 0.02950  0.03840  0.05150  84  GLU A C   
611  O O   . GLU A  90  ? 0.29730 0.26630 0.23770 0.03150  0.04150  0.04580  84  GLU A O   
612  C CB  . GLU A  90  ? 0.29700 0.26080 0.26880 0.02230  0.03220  0.05710  84  GLU A CB  
613  C CG  . GLU A  90  ? 0.25650 0.21230 0.23880 0.02060  0.02390  0.05400  84  GLU A CG  
614  C CD  . GLU A  90  ? 0.30860 0.26350 0.30700 0.01670  0.02100  0.05650  84  GLU A CD  
615  O OE1 . GLU A  90  ? 0.31040 0.27320 0.31490 0.01460  0.02600  0.06230  84  GLU A OE1 
616  O OE2 . GLU A  90  ? 0.31590 0.26230 0.32170 0.01640  0.01300  0.05280  84  GLU A OE2 
617  N N   . ASP A  91  ? 0.31890 0.28730 0.25230 0.03130  0.04050  0.05900  85  ASP A N   
618  C CA  . ASP A  91  ? 0.31000 0.28260 0.22650 0.03690  0.04700  0.05950  85  ASP A CA  
619  C C   . ASP A  91  ? 0.36060 0.34090 0.28350 0.03800  0.05510  0.05990  85  ASP A C   
620  O O   . ASP A  91  ? 0.34430 0.32490 0.25590 0.04330  0.05850  0.05350  85  ASP A O   
621  C CB  . ASP A  91  ? 0.34260 0.31800 0.24840 0.03950  0.05000  0.07060  85  ASP A CB  
622  C CG  . ASP A  91  ? 0.32930 0.29730 0.22300 0.04090  0.04150  0.06850  85  ASP A CG  
623  O OD1 . ASP A  91  ? 0.33510 0.29690 0.23170 0.03940  0.03360  0.05870  85  ASP A OD1 
624  O OD2 . ASP A  91  ? 0.39590 0.36510 0.27770 0.04380  0.04270  0.07730  85  ASP A OD2 
625  N N   . ARG A  92  ? 0.33220 0.31780 0.27450 0.03330  0.05700  0.06700  86  ARG A N   
626  C CA  . ARG A  92  ? 0.29510 0.28980 0.24630 0.03430  0.06410  0.06860  86  ARG A CA  
627  C C   . ARG A  92  ? 0.29260 0.28370 0.24520 0.03510  0.06140  0.05690  86  ARG A C   
628  O O   . ARG A  92  ? 0.28540 0.28210 0.23770 0.03900  0.06730  0.05540  86  ARG A O   
629  C CB  . ARG A  92  ? 0.30330 0.30450 0.27820 0.02810  0.06430  0.07900  86  ARG A CB  
630  C CG  . ARG A  92  ? 0.29520 0.28750 0.28370 0.02190  0.05360  0.07480  86  ARG A CG  
631  C CD  . ARG A  92  ? 0.30130 0.29730 0.31370 0.01540  0.05110  0.08460  86  ARG A CD  
632  N NE  . ARG A  92  ? 0.28460 0.26900 0.30550 0.01140  0.03950  0.07890  86  ARG A NE  
633  C CZ  . ARG A  92  ? 0.28580 0.26750 0.32690 0.00560  0.03260  0.08380  86  ARG A CZ  
634  N NH1 . ARG A  92  ? 0.29590 0.28740 0.35550 0.00130  0.03590  0.09630  86  ARG A NH1 
635  N NH2 . ARG A  92  ? 0.28360 0.25270 0.32760 0.00440  0.02170  0.07590  86  ARG A NH2 
636  N N   . HIS A  93  ? 0.29930 0.28200 0.25410 0.03220  0.05330  0.04970  87  HIS A N   
637  C CA  . HIS A  93  ? 0.27240 0.25230 0.22750 0.03340  0.05160  0.04060  87  HIS A CA  
638  C C   . HIS A  93  ? 0.30530 0.28110 0.24460 0.03830  0.05280  0.03430  87  HIS A C   
639  O O   . HIS A  93  ? 0.29820 0.27400 0.23660 0.04130  0.05520  0.02980  87  HIS A O   
640  C CB  . HIS A  93  ? 0.28170 0.25560 0.24230 0.03040  0.04420  0.03600  87  HIS A CB  
641  C CG  . HIS A  93  ? 0.27440 0.24870 0.24840 0.02670  0.04050  0.03930  87  HIS A CG  
642  N ND1 . HIS A  93  ? 0.28430 0.25310 0.26080 0.02490  0.03480  0.04010  87  HIS A ND1 
643  C CD2 . HIS A  93  ? 0.26700 0.24530 0.25330 0.02490  0.04010  0.04120  87  HIS A CD2 
644  C CE1 . HIS A  93  ? 0.28670 0.25440 0.27540 0.02220  0.03060  0.04150  87  HIS A CE1 
645  N NE2 . HIS A  93  ? 0.26110 0.23480 0.25630 0.02180  0.03330  0.04230  87  HIS A NE2 
646  N N   . ILE A  94  ? 0.29760 0.26870 0.22450 0.03960  0.04980  0.03350  88  ILE A N   
647  C CA  . ILE A  94  ? 0.30660 0.27190 0.21790 0.04440  0.04850  0.02630  88  ILE A CA  
648  C C   . ILE A  94  ? 0.31670 0.28630 0.21820 0.05130  0.05670  0.02720  88  ILE A C   
649  O O   . ILE A  94  ? 0.32690 0.29230 0.22260 0.05570  0.05720  0.01990  88  ILE A O   
650  C CB  . ILE A  94  ? 0.32790 0.28780 0.22770 0.04480  0.04200  0.02560  88  ILE A CB  
651  C CG1 . ILE A  94  ? 0.38770 0.34270 0.29650 0.04040  0.03350  0.02120  88  ILE A CG1 
652  C CG2 . ILE A  94  ? 0.36460 0.31930 0.24360 0.05170  0.04100  0.01980  88  ILE A CG2 
653  C CD1 . ILE A  94  ? 0.32060 0.27900 0.24550 0.03580  0.03310  0.02520  88  ILE A CD1 
654  N N   . ALA A  95  ? 0.33660 0.31510 0.23750 0.05260  0.06360  0.03700  89  ALA A N   
655  C CA  . ALA A  95  ? 0.33760 0.32350 0.22980 0.06060  0.07360  0.03970  89  ALA A CA  
656  C C   . ALA A  95  ? 0.34990 0.34030 0.25500 0.06160  0.07780  0.03750  89  ALA A C   
657  O O   . ALA A  95  ? 0.35400 0.34360 0.24900 0.06990  0.08220  0.03210  89  ALA A O   
658  C CB  . ALA A  95  ? 0.31110 0.30870 0.20590 0.06070  0.08130  0.05410  89  ALA A CB  
659  N N   . ARG A  96  ? 0.31470 0.30870 0.24100 0.05440  0.07560  0.04060  90  ARG A N   
660  C CA  . ARG A  96  ? 0.32060 0.31890 0.25880 0.05570  0.07840  0.03890  90  ARG A CA  
661  C C   . ARG A  96  ? 0.30750 0.29450 0.23920 0.05800  0.07340  0.02760  90  ARG A C   
662  O O   . ARG A  96  ? 0.32580 0.31350 0.25830 0.06340  0.07690  0.02440  90  ARG A O   
663  C CB  . ARG A  96  ? 0.29310 0.29700 0.25350 0.04810  0.07520  0.04420  90  ARG A CB  
664  C CG  . ARG A  96  ? 0.30410 0.31440 0.27760 0.04990  0.07750  0.04390  90  ARG A CG  
665  C CD  . ARG A  96  ? 0.26670 0.28390 0.26160 0.04320  0.07360  0.05000  90  ARG A CD  
666  N NE  . ARG A  96  ? 0.34440 0.37300 0.35000 0.04140  0.07880  0.06160  90  ARG A NE  
667  C CZ  . ARG A  96  ? 0.36220 0.40490 0.37630 0.04570  0.08790  0.06900  90  ARG A CZ  
668  N NH1 . ARG A  96  ? 0.29370 0.33960 0.30590 0.05280  0.09250  0.06480  90  ARG A NH1 
669  N NH2 . ARG A  96  ? 0.33540 0.38970 0.36210 0.04300  0.09280  0.08190  90  ARG A NH2 
670  N N   . THR A  97  ? 0.30470 0.28160 0.23200 0.05400  0.06530  0.02250  91  THR A N   
671  C CA  . THR A  97  ? 0.28310 0.24940 0.20720 0.05510  0.06010  0.01380  91  THR A CA  
672  C C   . THR A  97  ? 0.34250 0.30230 0.25040 0.06360  0.06180  0.00720  91  THR A C   
673  O O   . THR A  97  ? 0.29880 0.25360 0.20800 0.06750  0.06200  0.00220  91  THR A O   
674  C CB  . THR A  97  ? 0.29980 0.25890 0.22380 0.04960  0.05170  0.01130  91  THR A CB  
675  O OG1 . THR A  97  ? 0.30630 0.27060 0.24360 0.04380  0.05050  0.01600  91  THR A OG1 
676  C CG2 . THR A  97  ? 0.31630 0.26540 0.24080 0.04970  0.04610  0.00430  91  THR A CG2 
677  N N   . ARG A  98  ? 0.34660 0.30600 0.23810 0.06770  0.06290  0.00720  92  ARG A N   
678  C CA  . ARG A  98  ? 0.34020 0.29270 0.21140 0.07800  0.06410  -0.00020 92  ARG A CA  
679  C C   . ARG A  98  ? 0.36350 0.32490 0.23560 0.08630  0.07520  0.00210  92  ARG A C   
680  O O   . ARG A  98  ? 0.37470 0.32830 0.23720 0.09510  0.07550  -0.00640 92  ARG A O   
681  C CB  . ARG A  98  ? 0.40610 0.35810 0.25760 0.08120  0.06320  0.00090  92  ARG A CB  
682  C CG  . ARG A  98  ? 0.40080 0.34330 0.25120 0.07440  0.05090  -0.00270 92  ARG A CG  
683  C CD  . ARG A  98  ? 0.46330 0.40400 0.29230 0.07860  0.04820  -0.00220 92  ARG A CD  
684  N NE  . ARG A  98  ? 0.49010 0.42030 0.31860 0.07360  0.03440  -0.00820 92  ARG A NE  
685  C CZ  . ARG A  98  ? 0.55470 0.48540 0.37690 0.07150  0.02910  -0.00450 92  ARG A CZ  
686  N NH1 . ARG A  98  ? 0.57070 0.51080 0.38580 0.07370  0.03650  0.00570  92  ARG A NH1 
687  N NH2 . ARG A  98  ? 0.47110 0.39340 0.29650 0.06710  0.01600  -0.01000 92  ARG A NH2 
688  N N   . ALA A  99  ? 0.34890 0.32660 0.23430 0.08400  0.08370  0.01360  93  ALA A N   
689  C CA  . ALA A  99  ? 0.34520 0.33480 0.23630 0.09170  0.09450  0.01770  93  ALA A CA  
690  C C   . ALA A  99  ? 0.37920 0.36490 0.28370 0.09160  0.09220  0.01300  93  ALA A C   
691  O O   . ALA A  99  ? 0.35940 0.34650 0.26130 0.10140  0.09790  0.00990  93  ALA A O   
692  C CB  . ALA A  99  ? 0.36930 0.37760 0.27720 0.08720  0.10220  0.03260  93  ALA A CB  
693  N N   . MET A  100 ? 0.30170 0.28240 0.21950 0.08180  0.08400  0.01250  94  MET A N   
694  C CA  . MET A  100 ? 0.33480 0.31090 0.26360 0.08180  0.08120  0.00900  94  MET A CA  
695  C C   . MET A  100 ? 0.36370 0.32210 0.28010 0.08710  0.07570  -0.00220 94  MET A C   
696  O O   . MET A  100 ? 0.40250 0.35700 0.32220 0.09310  0.07680  -0.00570 94  MET A O   
697  C CB  . MET A  100 ? 0.32920 0.30610 0.27300 0.07120  0.07490  0.01260  94  MET A CB  
698  C CG  . MET A  100 ? 0.31750 0.30930 0.27640 0.06650  0.07780  0.02220  94  MET A CG  
699  S SD  . MET A  100 ? 0.31530 0.30500 0.28480 0.05650  0.06910  0.02360  94  MET A SD  
700  C CE  . MET A  100 ? 0.23100 0.21670 0.20690 0.05900  0.06680  0.02090  94  MET A CE  
701  N N   . LEU A  101 ? 0.35220 0.29910 0.25560 0.08490  0.06850  -0.00800 95  LEU A N   
702  C CA  . LEU A  101 ? 0.37310 0.30160 0.26540 0.08950  0.06110  -0.01930 95  LEU A CA  
703  C C   . LEU A  101 ? 0.39700 0.32240 0.27360 0.10370  0.06660  -0.02580 95  LEU A C   
704  O O   . LEU A  101 ? 0.38780 0.29960 0.26230 0.10960  0.06270  -0.03410 95  LEU A O   
705  C CB  . LEU A  101 ? 0.34120 0.26030 0.22260 0.08520  0.05170  -0.02370 95  LEU A CB  
706  C CG  . LEU A  101 ? 0.32320 0.24130 0.22070 0.07300  0.04440  -0.01990 95  LEU A CG  
707  C CD1 . LEU A  101 ? 0.40250 0.31550 0.29110 0.06940  0.03640  -0.02250 95  LEU A CD1 
708  C CD2 . LEU A  101 ? 0.37250 0.27940 0.28200 0.07090  0.03840  -0.02310 95  LEU A CD2 
709  N N   . SER A  102 ? 0.41650 0.35410 0.28150 0.11010  0.07600  -0.02170 96  SER A N   
710  C CA  . SER A  102 ? 0.40000 0.33700 0.24800 0.12590  0.08330  -0.02730 96  SER A CA  
711  C C   . SER A  102 ? 0.39400 0.33870 0.25760 0.13130  0.09090  -0.02450 96  SER A C   
712  O O   . SER A  102 ? 0.42290 0.35980 0.27630 0.14440  0.09300  -0.03300 96  SER A O   
713  C CB  . SER A  102 ? 0.45580 0.40740 0.28930 0.13170  0.09350  -0.02040 96  SER A CB  
714  O OG  . SER A  102 ? 0.52310 0.46660 0.34040 0.12800  0.08560  -0.02340 96  SER A OG  
715  N N   . LYS A  103 ? 0.37300 0.33260 0.26090 0.12250  0.09430  -0.01320 97  LYS A N   
716  C CA  . LYS A  103 ? 0.41050 0.37860 0.31510 0.12720  0.10020  -0.00970 97  LYS A CA  
717  C C   . LYS A  103 ? 0.41420 0.36350 0.32100 0.12950  0.09190  -0.01880 97  LYS A C   
718  O O   . LYS A  103 ? 0.40320 0.35340 0.31490 0.13930  0.09630  -0.02050 97  LYS A O   
719  C CB  . LYS A  103 ? 0.38110 0.36620 0.31080 0.11610  0.10160  0.00300  97  LYS A CB  
720  C CG  . LYS A  103 ? 0.40260 0.40870 0.33750 0.11530  0.11120  0.01440  97  LYS A CG  
721  C CD  . LYS A  103 ? 0.39410 0.41410 0.35520 0.10450  0.10980  0.02520  97  LYS A CD  
722  C CE  . LYS A  103 ? 0.38250 0.42390 0.35410 0.10390  0.11920  0.03800  97  LYS A CE  
723  N NZ  . LYS A  103 ? 0.33870 0.39110 0.33630 0.09270  0.11490  0.04730  97  LYS A NZ  
724  N N   . ILE A  104 ? 0.38800 0.32120 0.29420 0.12050  0.08010  -0.02350 98  ILE A N   
725  C CA  . ILE A  104 ? 0.39830 0.31280 0.30900 0.12140  0.07160  -0.03030 98  ILE A CA  
726  C C   . ILE A  104 ? 0.46500 0.35710 0.35620 0.12730  0.06320  -0.04400 98  ILE A C   
727  O O   . ILE A  104 ? 0.43070 0.30400 0.32700 0.12530  0.05310  -0.04970 98  ILE A O   
728  C CB  . ILE A  104 ? 0.38120 0.29400 0.30930 0.10760  0.06430  -0.02400 98  ILE A CB  
729  C CG1 . ILE A  104 ? 0.43220 0.34220 0.35510 0.09740  0.05810  -0.02400 98  ILE A CG1 
730  C CG2 . ILE A  104 ? 0.40710 0.33910 0.35220 0.10360  0.07040  -0.01260 98  ILE A CG2 
731  C CD1 . ILE A  104 ? 0.34080 0.24710 0.27890 0.08610  0.05100  -0.01900 98  ILE A CD1 
732  N N   . LYS A  105 ? 0.42570 0.31890 0.29500 0.13430  0.06610  -0.04910 99  LYS A N   
733  C CA  . LYS A  105 ? 0.44820 0.31980 0.29480 0.14190  0.05680  -0.06390 99  LYS A CA  
734  C C   . LYS A  105 ? 0.50330 0.35780 0.35610 0.12940  0.04080  -0.06760 99  LYS A C   
735  O O   . LYS A  105 ? 0.50660 0.33830 0.35610 0.13210  0.02900  -0.07870 99  LYS A O   
736  C CB  . LYS A  105 ? 0.50300 0.36100 0.34220 0.15750  0.05730  -0.07450 99  LYS A CB  
737  C CG  . LYS A  105 ? 0.52340 0.40020 0.35830 0.17160  0.07410  -0.07030 99  LYS A CG  
738  C CD  . LYS A  105 ? 0.58480 0.44850 0.41130 0.18590  0.07240  -0.08170 99  LYS A CD  
739  C CE  . LYS A  105 ? 0.62310 0.51130 0.45500 0.19470  0.08740  -0.07380 99  LYS A CE  
740  N NZ  . LYS A  105 ? 0.70470 0.58110 0.53230 0.20670  0.08480  -0.08410 99  LYS A NZ  
741  N N   . ALA A  106 ? 0.45620 0.32200 0.32020 0.11590  0.04020  -0.05790 100 ALA A N   
742  C CA  . ALA A  106 ? 0.45310 0.30870 0.32560 0.10380  0.02720  -0.05860 100 ALA A CA  
743  C C   . ALA A  106 ? 0.45340 0.31260 0.31090 0.10140  0.02420  -0.05950 100 ALA A C   
744  O O   . ALA A  106 ? 0.47170 0.34170 0.31270 0.10820  0.03280  -0.05810 100 ALA A O   
745  C CB  . ALA A  106 ? 0.41590 0.28180 0.31430 0.09140  0.02890  -0.04620 100 ALA A CB  
746  N N   . GLU A  107 ? 0.42000 0.27140 0.28510 0.09150  0.01220  -0.06050 101 GLU A N   
747  C CA  . GLU A  107 ? 0.46740 0.32240 0.32070 0.08870  0.00810  -0.06050 101 GLU A CA  
748  C C   . GLU A  107 ? 0.43900 0.30090 0.31450 0.07450  0.00380  -0.05150 101 GLU A C   
749  O O   . GLU A  107 ? 0.40900 0.27070 0.30630 0.06760  0.00290  -0.04660 101 GLU A O   
750  C CB  . GLU A  107 ? 0.50510 0.34080 0.33700 0.09560  -0.00510 -0.07490 101 GLU A CB  
751  C CG  . GLU A  107 ? 0.58930 0.40440 0.43390 0.09090  -0.02120 -0.08270 101 GLU A CG  
752  C CD  . GLU A  107 ? 0.78050 0.57340 0.59990 0.10240  -0.03320 -0.10010 101 GLU A CD  
753  O OE1 . GLU A  107 ? 0.86260 0.65800 0.65410 0.11630  -0.02510 -0.10530 101 GLU A OE1 
754  O OE2 . GLU A  107 ? 0.90780 0.68110 0.73560 0.09810  -0.05080 -0.10830 101 GLU A OE2 
755  N N   . GLU A  108 ? 0.40990 0.27920 0.27910 0.07120  0.00230  -0.04850 102 GLU A N   
756  C CA  A GLU A  108 ? 0.40260 0.28020 0.29160 0.05960  -0.00050 -0.04000 102 GLU A CA  
757  C CA  B GLU A  108 ? 0.40280 0.28020 0.29150 0.05960  -0.00080 -0.04010 102 GLU A CA  
758  C C   . GLU A  108 ? 0.39900 0.26590 0.30690 0.05240  -0.01260 -0.04190 102 GLU A C   
759  O O   . GLU A  108 ? 0.38350 0.25850 0.31340 0.04430  -0.01080 -0.03300 102 GLU A O   
760  C CB  A GLU A  108 ? 0.40720 0.29060 0.28470 0.05900  -0.00290 -0.03830 102 GLU A CB  
761  C CB  B GLU A  108 ? 0.40780 0.28980 0.28480 0.05890  -0.00430 -0.03920 102 GLU A CB  
762  C CG  A GLU A  108 ? 0.38940 0.28430 0.25100 0.06530  0.00950  -0.03360 102 GLU A CG  
763  C CG  B GLU A  108 ? 0.39810 0.28670 0.29540 0.04860  -0.00930 -0.03230 102 GLU A CG  
764  C CD  A GLU A  108 ? 0.40240 0.30210 0.25340 0.06460  0.00680  -0.03030 102 GLU A CD  
765  C CD  B GLU A  108 ? 0.38310 0.27820 0.27200 0.04780  -0.01150 -0.02920 102 GLU A CD  
766  O OE1 A GLU A  108 ? 0.40170 0.29860 0.26140 0.05820  -0.00360 -0.03060 102 GLU A OE1 
767  O OE1 B GLU A  108 ? 0.41340 0.30200 0.28090 0.05370  -0.01720 -0.03530 102 GLU A OE1 
768  O OE2 A GLU A  108 ? 0.38370 0.29060 0.21920 0.07050  0.01490  -0.02640 102 GLU A OE2 
769  O OE2 B GLU A  108 ? 0.31640 0.22280 0.21960 0.04220  -0.00780 -0.02070 102 GLU A OE2 
770  N N   . ALA A  109 ? 0.38770 0.23640 0.28800 0.05560  -0.02500 -0.05300 103 ALA A N   
771  C CA  . ALA A  109 ? 0.42570 0.26340 0.34800 0.04760  -0.03800 -0.05380 103 ALA A CA  
772  C C   . ALA A  109 ? 0.41150 0.24890 0.35470 0.04430  -0.03280 -0.04730 103 ALA A C   
773  O O   . ALA A  109 ? 0.44030 0.27480 0.40800 0.03570  -0.03990 -0.04210 103 ALA A O   
774  C CB  . ALA A  109 ? 0.42650 0.24160 0.33560 0.05250  -0.05450 -0.06880 103 ALA A CB  
775  N N   . ASP A  110 ? 0.38820 0.22960 0.32380 0.05100  -0.02070 -0.04610 104 ASP A N   
776  C CA  . ASP A  110 ? 0.42260 0.26580 0.37690 0.04850  -0.01530 -0.03840 104 ASP A CA  
777  C C   . ASP A  110 ? 0.39100 0.25390 0.36070 0.04150  -0.00590 -0.02430 104 ASP A C   
778  O O   . ASP A  110 ? 0.38040 0.24500 0.36780 0.03780  -0.00370 -0.01620 104 ASP A O   
779  C CB  . ASP A  110 ? 0.39180 0.23220 0.33350 0.05910  -0.00690 -0.04250 104 ASP A CB  
780  C CG  . ASP A  110 ? 0.47900 0.29870 0.40380 0.06870  -0.01540 -0.05750 104 ASP A CG  
781  O OD1 . ASP A  110 ? 0.51130 0.31240 0.44400 0.06550  -0.02980 -0.06350 104 ASP A OD1 
782  O OD2 . ASP A  110 ? 0.47710 0.29910 0.38100 0.08000  -0.00760 -0.06310 104 ASP A OD2 
783  N N   . LEU A  111 ? 0.34350 0.22050 0.30600 0.04060  -0.00060 -0.02130 105 LEU A N   
784  C CA  . LEU A  111 ? 0.30590 0.19940 0.28120 0.03530  0.00660  -0.00990 105 LEU A CA  
785  C C   . LEU A  111 ? 0.35970 0.25420 0.35680 0.02710  0.00070  -0.00320 105 LEU A C   
786  O O   . LEU A  111 ? 0.33520 0.22230 0.33690 0.02360  -0.01010 -0.00710 105 LEU A O   
787  C CB  . LEU A  111 ? 0.33380 0.23860 0.29810 0.03580  0.01070  -0.00910 105 LEU A CB  
788  C CG  . LEU A  111 ? 0.37340 0.28190 0.32060 0.04280  0.01860  -0.01160 105 LEU A CG  
789  C CD1 . LEU A  111 ? 0.31610 0.23250 0.25430 0.04230  0.02000  -0.01020 105 LEU A CD1 
790  C CD2 . LEU A  111 ? 0.33840 0.25510 0.29270 0.04400  0.02750  -0.00560 105 LEU A CD2 
791  N N   . ARG A  112 ? 0.29650 0.20170 0.30730 0.02450  0.00770  0.00740  106 ARG A N   
792  C CA  . ARG A  112 ? 0.28970 0.20060 0.32270 0.01770  0.00530  0.01690  106 ARG A CA  
793  C C   . ARG A  112 ? 0.29020 0.21900 0.32600 0.01680  0.01240  0.02420  106 ARG A C   
794  O O   . ARG A  112 ? 0.29650 0.23450 0.35010 0.01330  0.01450  0.03430  106 ARG A O   
795  C CB  . ARG A  112 ? 0.32770 0.23600 0.37540 0.01650  0.00770  0.02510  106 ARG A CB  
796  C CG  . ARG A  112 ? 0.38330 0.27110 0.43290 0.01700  -0.00130 0.01830  106 ARG A CG  
797  C CD  . ARG A  112 ? 0.39760 0.27520 0.46090 0.01060  -0.01530 0.01520  106 ARG A CD  
798  N NE  . ARG A  112 ? 0.42450 0.27920 0.48510 0.01250  -0.02620 0.00490  106 ARG A NE  
799  C CZ  . ARG A  112 ? 0.45620 0.29760 0.49780 0.01720  -0.03470 -0.01020 106 ARG A CZ  
800  N NH1 . ARG A  112 ? 0.43960 0.28900 0.46390 0.01960  -0.03330 -0.01540 106 ARG A NH1 
801  N NH2 . ARG A  112 ? 0.45460 0.27360 0.49380 0.02020  -0.04530 -0.02020 106 ARG A NH2 
802  N N   . CYS A  113 ? 0.30370 0.23750 0.32300 0.02060  0.01630  0.01980  107 CYS A N   
803  C CA  . CYS A  113 ? 0.27610 0.22310 0.29600 0.02060  0.02040  0.02390  107 CYS A CA  
804  C C   . CYS A  113 ? 0.27960 0.22510 0.29880 0.01830  0.01260  0.01970  107 CYS A C   
805  O O   . CYS A  113 ? 0.28810 0.22240 0.29950 0.01820  0.00490  0.01210  107 CYS A O   
806  C CB  . CYS A  113 ? 0.26960 0.22120 0.27430 0.02540  0.02750  0.02200  107 CYS A CB  
807  S SG  . CYS A  113 ? 0.31780 0.26060 0.30340 0.02900  0.02650  0.01290  107 CYS A SG  
808  N N   . GLY A  114 ? 0.28250 0.23920 0.30890 0.01770  0.01430  0.02450  108 GLY A N   
809  C CA  . GLY A  114 ? 0.32290 0.27990 0.35030 0.01590  0.00660  0.02190  108 GLY A CA  
810  C C   . GLY A  114 ? 0.29900 0.26080 0.31400 0.01950  0.00980  0.02040  108 GLY A C   
811  O O   . GLY A  114 ? 0.26420 0.23120 0.27430 0.02280  0.01780  0.02250  108 GLY A O   
812  N N   . GLY A  115 ? 0.28720 0.24610 0.29680 0.01910  0.00250  0.01700  109 GLY A N   
813  C CA  . GLY A  115 ? 0.28610 0.24860 0.28630 0.02220  0.00460  0.01710  109 GLY A CA  
814  C C   . GLY A  115 ? 0.29760 0.27150 0.31160 0.02310  0.00720  0.02290  109 GLY A C   
815  O O   . GLY A  115 ? 0.27250 0.25380 0.30480 0.02130  0.00690  0.02760  109 GLY A O   
816  N N   . HIS A  116 ? 0.29020 0.26570 0.29660 0.02660  0.00980  0.02290  110 HIS A N   
817  C CA  . HIS A  116 ? 0.24010 0.22480 0.25640 0.03000  0.01290  0.02680  110 HIS A CA  
818  C C   . HIS A  116 ? 0.30010 0.28120 0.30670 0.03280  0.01130  0.02530  110 HIS A C   
819  O O   . HIS A  116 ? 0.27970 0.25310 0.27240 0.03210  0.01100  0.02300  110 HIS A O   
820  C CB  . HIS A  116 ? 0.28450 0.27490 0.30320 0.03320  0.02180  0.02890  110 HIS A CB  
821  C CG  . HIS A  116 ? 0.28130 0.26500 0.28550 0.03420  0.02530  0.02550  110 HIS A CG  
822  N ND1 . HIS A  116 ? 0.31370 0.29400 0.30910 0.03710  0.02560  0.02320  110 HIS A ND1 
823  C CD2 . HIS A  116 ? 0.31020 0.29010 0.30940 0.03260  0.02770  0.02440  110 HIS A CD2 
824  C CE1 . HIS A  116 ? 0.25040 0.22640 0.23750 0.03660  0.02800  0.02130  110 HIS A CE1 
825  N NE2 . HIS A  116 ? 0.27620 0.25240 0.26490 0.03450  0.02970  0.02190  110 HIS A NE2 
826  N N   . PRO A  117 ? 0.27620 0.26280 0.29080 0.03650  0.01070  0.02750  111 PRO A N   
827  C CA  . PRO A  117 ? 0.28970 0.27090 0.29660 0.03950  0.00890  0.02670  111 PRO A CA  
828  C C   . PRO A  117 ? 0.26130 0.23670 0.25790 0.04050  0.01350  0.02430  111 PRO A C   
829  O O   . PRO A  117 ? 0.24740 0.22580 0.24470 0.04220  0.01900  0.02320  111 PRO A O   
830  C CB  . PRO A  117 ? 0.25890 0.24790 0.27820 0.04520  0.00940  0.02870  111 PRO A CB  
831  C CG  . PRO A  117 ? 0.29920 0.29930 0.33460 0.04360  0.00920  0.03230  111 PRO A CG  
832  C CD  . PRO A  117 ? 0.22640 0.22520 0.25930 0.03890  0.01230  0.03170  111 PRO A CD  
833  N N   . SER A  118 ? 0.28340 0.25110 0.27150 0.03940  0.01090  0.02440  112 SER A N   
834  C CA  . SER A  118 ? 0.29410 0.25690 0.27570 0.03870  0.01380  0.02330  112 SER A CA  
835  C C   . SER A  118 ? 0.29280 0.25490 0.27750 0.04360  0.01500  0.02050  112 SER A C   
836  O O   . SER A  118 ? 0.28610 0.24870 0.27570 0.04840  0.01300  0.02000  112 SER A O   
837  C CB  . SER A  118 ? 0.24510 0.20140 0.22060 0.03630  0.01110  0.02660  112 SER A CB  
838  O OG  . SER A  118 ? 0.31210 0.26500 0.28700 0.03540  0.01300  0.02650  112 SER A OG  
839  N N   . LEU A  119 ? 0.26640 0.22700 0.24760 0.04340  0.01760  0.01830  113 LEU A N   
840  C CA  . LEU A  119 ? 0.26760 0.22550 0.24840 0.04880  0.01690  0.01420  113 LEU A CA  
841  C C   . LEU A  119 ? 0.34660 0.29440 0.32860 0.04920  0.01050  0.01350  113 LEU A C   
842  O O   . LEU A  119 ? 0.34140 0.28410 0.32290 0.05510  0.00740  0.00850  113 LEU A O   
843  C CB  . LEU A  119 ? 0.28490 0.24360 0.26150 0.04840  0.01940  0.01200  113 LEU A CB  
844  C CG  . LEU A  119 ? 0.28400 0.25100 0.25990 0.04850  0.02540  0.01330  113 LEU A CG  
845  C CD1 . LEU A  119 ? 0.24590 0.21350 0.21700 0.05040  0.02700  0.01120  113 LEU A CD1 
846  C CD2 . LEU A  119 ? 0.28700 0.26180 0.26730 0.05310  0.02870  0.01480  113 LEU A CD2 
847  N N   . SER A  120 ? 0.30150 0.24580 0.28480 0.04360  0.00810  0.01860  114 SER A N   
848  C CA  . SER A  120 ? 0.29300 0.22770 0.28020 0.04300  0.00200  0.02100  114 SER A CA  
849  C C   . SER A  120 ? 0.31380 0.24870 0.30300 0.04550  -0.00040 0.02360  114 SER A C   
850  O O   . SER A  120 ? 0.29600 0.23610 0.28270 0.04280  0.00110  0.02780  114 SER A O   
851  C CB  . SER A  120 ? 0.32660 0.25960 0.31470 0.03580  0.00210  0.02790  114 SER A CB  
852  O OG  . SER A  120 ? 0.28790 0.21310 0.28100 0.03450  -0.00320 0.03350  114 SER A OG  
853  N N   . GLU A  121 ? 0.36260 0.29110 0.35590 0.05150  -0.00500 0.02050  115 GLU A N   
854  C CA  A GLU A  121 ? 0.34480 0.27360 0.34220 0.05470  -0.00800 0.02340  115 GLU A CA  
855  C CA  B GLU A  121 ? 0.34450 0.27430 0.34150 0.05440  -0.00750 0.02360  115 GLU A CA  
856  C C   . GLU A  121 ? 0.32430 0.24890 0.32110 0.04890  -0.01130 0.03220  115 GLU A C   
857  O O   . GLU A  121 ? 0.29560 0.22460 0.29150 0.04870  -0.01240 0.03650  115 GLU A O   
858  C CB  A GLU A  121 ? 0.37850 0.29890 0.38030 0.06330  -0.01270 0.01820  115 GLU A CB  
859  C CB  B GLU A  121 ? 0.38400 0.30890 0.38550 0.06390  -0.01070 0.01810  115 GLU A CB  
860  C CG  A GLU A  121 ? 0.39880 0.32540 0.39860 0.07240  -0.00830 0.01020  115 GLU A CG  
861  C CG  B GLU A  121 ? 0.36730 0.30210 0.36710 0.07130  -0.00450 0.01170  115 GLU A CG  
862  C CD  A GLU A  121 ? 0.42560 0.34760 0.41850 0.07310  -0.00780 0.00360  115 GLU A CD  
863  C CD  B GLU A  121 ? 0.37870 0.32900 0.38040 0.06830  0.00190  0.01550  115 GLU A CD  
864  O OE1 A GLU A  121 ? 0.40770 0.32120 0.40050 0.06630  -0.01200 0.00480  115 GLU A OE1 
865  O OE1 B GLU A  121 ? 0.36380 0.32130 0.37320 0.06980  0.00130  0.01910  115 GLU A OE1 
866  O OE2 A GLU A  121 ? 0.44660 0.37460 0.43470 0.08100  -0.00330 -0.00190 115 GLU A OE2 
867  O OE2 B GLU A  121 ? 0.37220 0.32690 0.36930 0.06420  0.00650  0.01500  115 GLU A OE2 
868  N N   . MET A  122 ? 0.33820 0.25510 0.33590 0.04410  -0.01300 0.03580  116 MET A N   
869  C CA  . MET A  122 ? 0.34070 0.25480 0.33770 0.03920  -0.01470 0.04640  116 MET A CA  
870  C C   . MET A  122 ? 0.31540 0.23950 0.30210 0.03600  -0.00920 0.05020  116 MET A C   
871  O O   . MET A  122 ? 0.31910 0.24420 0.30040 0.03600  -0.01090 0.05650  116 MET A O   
872  C CB  . MET A  122 ? 0.35660 0.26270 0.36050 0.03420  -0.01680 0.05120  116 MET A CB  
873  C CG  . MET A  122 ? 0.39750 0.30210 0.40210 0.02950  -0.01700 0.06490  116 MET A CG  
874  S SD  . MET A  122 ? 0.43220 0.32760 0.45280 0.02280  -0.02070 0.07270  116 MET A SD  
875  C CE  . MET A  122 ? 0.41360 0.29150 0.44450 0.02800  -0.03240 0.06300  116 MET A CE  
876  N N   . VAL A  123 ? 0.29160 0.22200 0.27420 0.03410  -0.00340 0.04610  117 VAL A N   
877  C CA  . VAL A  123 ? 0.32140 0.25920 0.29330 0.03250  0.00100  0.04720  117 VAL A CA  
878  C C   . VAL A  123 ? 0.30120 0.24260 0.27090 0.03550  -0.00210 0.04420  117 VAL A C   
879  O O   . VAL A  123 ? 0.31480 0.25770 0.27570 0.03540  -0.00410 0.04730  117 VAL A O   
880  C CB  . VAL A  123 ? 0.30400 0.24680 0.27420 0.03100  0.00700  0.04240  117 VAL A CB  
881  C CG1 . VAL A  123 ? 0.29320 0.24130 0.25220 0.03090  0.01000  0.04130  117 VAL A CG1 
882  C CG2 . VAL A  123 ? 0.28840 0.22980 0.26310 0.02760  0.00950  0.04650  117 VAL A CG2 
883  N N   . ASN A  124 ? 0.31570 0.25940 0.29360 0.03870  -0.00290 0.03820  118 ASN A N   
884  C CA  . ASN A  124 ? 0.28460 0.23410 0.26580 0.04100  -0.00580 0.03670  118 ASN A CA  
885  C C   . ASN A  124 ? 0.29280 0.23960 0.27430 0.04270  -0.01270 0.04190  118 ASN A C   
886  O O   . ASN A  124 ? 0.31510 0.26560 0.29380 0.04240  -0.01690 0.04290  118 ASN A O   
887  C CB  . ASN A  124 ? 0.31390 0.26850 0.30570 0.04550  -0.00380 0.03180  118 ASN A CB  
888  C CG  . ASN A  124 ? 0.32690 0.29130 0.32470 0.04530  -0.00380 0.03100  118 ASN A CG  
889  O OD1 . ASN A  124 ? 0.30320 0.26920 0.29600 0.04110  -0.00300 0.03030  118 ASN A OD1 
890  N ND2 . ASN A  124 ? 0.32140 0.29230 0.33140 0.04990  -0.00560 0.03160  118 ASN A ND2 
891  N N   . ARG A  125 ? 0.31350 0.25290 0.29910 0.04470  -0.01540 0.04520  119 ARG A N   
892  C CA  . ARG A  125 ? 0.30390 0.23990 0.28990 0.04670  -0.02230 0.05160  119 ARG A CA  
893  C C   . ARG A  125 ? 0.32460 0.26010 0.29600 0.04340  -0.02330 0.05830  119 ARG A C   
894  O O   . ARG A  125 ? 0.29710 0.23440 0.26390 0.04490  -0.02930 0.06130  119 ARG A O   
895  C CB  . ARG A  125 ? 0.33730 0.26270 0.33060 0.04900  -0.02540 0.05450  119 ARG A CB  
896  C CG  . ARG A  125 ? 0.36870 0.29310 0.37380 0.05590  -0.02630 0.04730  119 ARG A CG  
897  C CD  . ARG A  125 ? 0.39610 0.30730 0.40830 0.05970  -0.03270 0.05010  119 ARG A CD  
898  N NE  . ARG A  125 ? 0.45260 0.35250 0.46410 0.05480  -0.03320 0.05300  119 ARG A NE  
899  C CZ  . ARG A  125 ? 0.43220 0.32650 0.44630 0.05530  -0.03220 0.04580  119 ARG A CZ  
900  N NH1 . ARG A  125 ? 0.43700 0.33590 0.45120 0.06140  -0.02940 0.03540  119 ARG A NH1 
901  N NH2 . ARG A  125 ? 0.43030 0.31510 0.44750 0.04960  -0.03430 0.04990  119 ARG A NH2 
902  N N   . SER A  126 ? 0.33150 0.26530 0.29530 0.03970  -0.01750 0.06090  120 SER A N   
903  C CA  . SER A  126 ? 0.32920 0.26450 0.27660 0.03850  -0.01610 0.06670  120 SER A CA  
904  C C   . SER A  126 ? 0.29820 0.23880 0.23570 0.03950  -0.01800 0.06000  120 SER A C   
905  O O   . SER A  126 ? 0.31200 0.25260 0.23580 0.04140  -0.02270 0.06270  120 SER A O   
906  C CB  . SER A  126 ? 0.35720 0.29260 0.30170 0.03510  -0.00790 0.07030  120 SER A CB  
907  O OG  . SER A  126 ? 0.38630 0.32470 0.31350 0.03590  -0.00460 0.07620  120 SER A OG  
908  N N   . TRP A  127 ? 0.28500 0.22950 0.22920 0.03830  -0.01550 0.05140  121 TRP A N   
909  C CA  . TRP A  127 ? 0.31570 0.26350 0.25480 0.03840  -0.01900 0.04520  121 TRP A CA  
910  C C   . TRP A  127 ? 0.29770 0.24750 0.24320 0.04020  -0.02920 0.04540  121 TRP A C   
911  O O   . TRP A  127 ? 0.30290 0.25210 0.23810 0.04100  -0.03640 0.04410  121 TRP A O   
912  C CB  . TRP A  127 ? 0.27120 0.22280 0.22020 0.03650  -0.01440 0.03820  121 TRP A CB  
913  C CG  . TRP A  127 ? 0.31150 0.26220 0.25370 0.03500  -0.00630 0.03670  121 TRP A CG  
914  C CD1 . TRP A  127 ? 0.31170 0.26030 0.24140 0.03510  -0.00160 0.04110  121 TRP A CD1 
915  C CD2 . TRP A  127 ? 0.28100 0.23440 0.22970 0.03350  -0.00140 0.03150  121 TRP A CD2 
916  N NE1 . TRP A  127 ? 0.31980 0.26990 0.24920 0.03390  0.00550  0.03820  121 TRP A NE1 
917  C CE2 . TRP A  127 ? 0.31400 0.26620 0.25410 0.03300  0.00530  0.03210  121 TRP A CE2 
918  C CE3 . TRP A  127 ? 0.28350 0.24140 0.24530 0.03310  -0.00140 0.02770  121 TRP A CE3 
919  C CZ2 . TRP A  127 ? 0.29790 0.25190 0.24140 0.03200  0.01060  0.02810  121 TRP A CZ2 
920  C CZ3 . TRP A  127 ? 0.26610 0.22540 0.22990 0.03200  0.00450  0.02470  121 TRP A CZ3 
921  C CH2 . TRP A  127 ? 0.24840 0.20520 0.20290 0.03150  0.00980  0.02450  121 TRP A CH2 
922  N N   . ILE A  128 ? 0.29310 0.24510 0.25560 0.04190  -0.03050 0.04660  122 ILE A N   
923  C CA  . ILE A  128 ? 0.30490 0.26110 0.27760 0.04420  -0.03970 0.04760  122 ILE A CA  
924  C C   . ILE A  128 ? 0.30570 0.25720 0.26520 0.04610  -0.04750 0.05390  122 ILE A C   
925  O O   . ILE A  128 ? 0.32130 0.27520 0.27890 0.04700  -0.05750 0.05340  122 ILE A O   
926  C CB  . ILE A  128 ? 0.32080 0.28040 0.31290 0.04780  -0.03790 0.04820  122 ILE A CB  
927  C CG1 . ILE A  128 ? 0.31460 0.28210 0.31950 0.04730  -0.03140 0.04270  122 ILE A CG1 
928  C CG2 . ILE A  128 ? 0.29850 0.26200 0.30080 0.05130  -0.04730 0.05160  122 ILE A CG2 
929  C CD1 . ILE A  128 ? 0.30560 0.27500 0.32300 0.05290  -0.02670 0.04200  122 ILE A CD1 
930  N N   . LYS A  129 ? 0.31260 0.25750 0.26310 0.04680  -0.04380 0.06060  123 LYS A N   
931  C CA  . LYS A  129 ? 0.33180 0.27270 0.26870 0.04930  -0.05020 0.06890  123 LYS A CA  
932  C C   . LYS A  129 ? 0.34580 0.28710 0.26040 0.04980  -0.05380 0.06660  123 LYS A C   
933  O O   . LYS A  129 ? 0.36340 0.30350 0.26680 0.05300  -0.06320 0.07030  123 LYS A O   
934  C CB  . LYS A  129 ? 0.33760 0.27190 0.27080 0.04890  -0.04420 0.07860  123 LYS A CB  
935  C CG  . LYS A  129 ? 0.35950 0.29050 0.27650 0.05150  -0.04850 0.08970  123 LYS A CG  
936  C CD  . LYS A  129 ? 0.36530 0.29010 0.28520 0.05010  -0.04290 0.10180  123 LYS A CD  
937  C CE  . LYS A  129 ? 0.43380 0.35630 0.33700 0.05320  -0.04610 0.11580  123 LYS A CE  
938  N NZ  . LYS A  129 ? 0.41150 0.32850 0.32120 0.05080  -0.04080 0.13010  123 LYS A NZ  
939  N N   . GLN A  130 ? 0.34080 0.28270 0.24760 0.04760  -0.04740 0.06010  124 GLN A N   
940  C CA  . GLN A  130 ? 0.35800 0.29790 0.24020 0.04980  -0.04990 0.05690  124 GLN A CA  
941  C C   . GLN A  130 ? 0.35620 0.29710 0.24230 0.04850  -0.05780 0.04550  124 GLN A C   
942  O O   . GLN A  130 ? 0.37620 0.31340 0.24320 0.05040  -0.06010 0.03950  124 GLN A O   
943  C CB  . GLN A  130 ? 0.35880 0.29780 0.22780 0.04990  -0.03720 0.05860  124 GLN A CB  
944  C CG  . GLN A  130 ? 0.36100 0.29960 0.23140 0.04980  -0.02990 0.07180  124 GLN A CG  
945  C CD  . GLN A  130 ? 0.38120 0.32180 0.24730 0.04850  -0.01680 0.07470  124 GLN A CD  
946  O OE1 . GLN A  130 ? 0.37660 0.31880 0.22130 0.05250  -0.01210 0.07750  124 GLN A OE1 
947  N NE2 . GLN A  130 ? 0.33860 0.28000 0.22480 0.04380  -0.01100 0.07420  124 GLN A NE2 
948  N N   . ASP A  131 ? 0.35660 0.30250 0.26810 0.04560  -0.06210 0.04300  125 ASP A N   
949  C CA  . ASP A  131 ? 0.35290 0.30110 0.27500 0.04290  -0.07010 0.03460  125 ASP A CA  
950  C C   . ASP A  131 ? 0.37580 0.32120 0.29290 0.04050  -0.06330 0.02730  125 ASP A C   
951  O O   . ASP A  131 ? 0.36890 0.31080 0.28290 0.03940  -0.07150 0.01970  125 ASP A O   
952  C CB  . ASP A  131 ? 0.38260 0.32760 0.29260 0.04530  -0.08640 0.03220  125 ASP A CB  
953  C CG  . ASP A  131 ? 0.47230 0.42140 0.39210 0.04760  -0.09490 0.03950  125 ASP A CG  
954  O OD1 . ASP A  131 ? 0.48610 0.44340 0.43370 0.04580  -0.09370 0.04210  125 ASP A OD1 
955  O OD2 . ASP A  131 ? 0.55160 0.49640 0.45080 0.05210  -0.10230 0.04320  125 ASP A OD2 
956  N N   . PHE A  132 ? 0.33030 0.27630 0.24760 0.03980  -0.04970 0.02920  126 PHE A N   
957  C CA  . PHE A  132 ? 0.34510 0.28840 0.25680 0.03850  -0.04300 0.02310  126 PHE A CA  
958  C C   . PHE A  132 ? 0.33890 0.28670 0.27410 0.03400  -0.04220 0.01960  126 PHE A C   
959  O O   . PHE A  132 ? 0.32330 0.27790 0.27670 0.03290  -0.03710 0.02340  126 PHE A O   
960  C CB  . PHE A  132 ? 0.34710 0.29040 0.25150 0.03940  -0.02960 0.02750  126 PHE A CB  
961  C CG  . PHE A  132 ? 0.33860 0.28040 0.23910 0.03870  -0.02230 0.02200  126 PHE A CG  
962  C CD1 . PHE A  132 ? 0.35910 0.29500 0.23980 0.04220  -0.02470 0.01620  126 PHE A CD1 
963  C CD2 . PHE A  132 ? 0.33420 0.27980 0.24990 0.03580  -0.01390 0.02220  126 PHE A CD2 
964  C CE1 . PHE A  132 ? 0.35260 0.28630 0.23040 0.04260  -0.01840 0.01090  126 PHE A CE1 
965  C CE2 . PHE A  132 ? 0.33320 0.27740 0.24590 0.03570  -0.00790 0.01780  126 PHE A CE2 
966  C CZ  . PHE A  132 ? 0.31860 0.25690 0.21330 0.03900  -0.01000 0.01240  126 PHE A CZ  
967  N N   . ILE A  133 ? 0.33230 0.27610 0.26670 0.03230  -0.04710 0.01260  127 ILE A N   
968  C CA  . ILE A  133 ? 0.34580 0.29350 0.30220 0.02790  -0.04550 0.01090  127 ILE A CA  
969  C C   . ILE A  133 ? 0.31870 0.26340 0.26810 0.02810  -0.03420 0.00870  127 ILE A C   
970  O O   . ILE A  133 ? 0.36830 0.30440 0.30040 0.03020  -0.03560 0.00290  127 ILE A O   
971  C CB  . ILE A  133 ? 0.33150 0.27540 0.29600 0.02480  -0.05950 0.00560  127 ILE A CB  
972  C CG1 . ILE A  133 ? 0.38890 0.33660 0.36120 0.02470  -0.07230 0.00800  127 ILE A CG1 
973  C CG2 . ILE A  133 ? 0.39060 0.33970 0.38110 0.01950  -0.05670 0.00690  127 ILE A CG2 
974  C CD1 . ILE A  133 ? 0.44410 0.38300 0.41160 0.02360  -0.08980 0.00040  127 ILE A CD1 
975  N N   . PRO A  134 ? 0.30430 0.25550 0.26530 0.02720  -0.02380 0.01270  128 PRO A N   
976  C CA  . PRO A  134 ? 0.30970 0.25860 0.26530 0.02760  -0.01440 0.01090  128 PRO A CA  
977  C C   . PRO A  134 ? 0.37460 0.31920 0.33640 0.02520  -0.01750 0.00630  128 PRO A C   
978  O O   . PRO A  134 ? 0.31490 0.26210 0.29470 0.02150  -0.02370 0.00710  128 PRO A O   
979  C CB  . PRO A  134 ? 0.32700 0.28390 0.29510 0.02740  -0.00560 0.01580  128 PRO A CB  
980  C CG  . PRO A  134 ? 0.33290 0.29690 0.31770 0.02680  -0.01010 0.01910  128 PRO A CG  
981  C CD  . PRO A  134 ? 0.32590 0.28640 0.30370 0.02720  -0.02040 0.01840  128 PRO A CD  
982  N N   . THR A  135 ? 0.35790 0.29600 0.30640 0.02740  -0.01330 0.00220  129 THR A N   
983  C CA  . THR A  135 ? 0.32310 0.25380 0.27500 0.02620  -0.01630 -0.00280 129 THR A CA  
984  C C   . THR A  135 ? 0.30300 0.23650 0.25910 0.02670  -0.00530 -0.00060 129 THR A C   
985  O O   . THR A  135 ? 0.32240 0.26340 0.27910 0.02750  0.00320  0.00410  129 THR A O   
986  C CB  . THR A  135 ? 0.35900 0.27740 0.28900 0.03070  -0.02310 -0.01150 129 THR A CB  
987  O OG1 . THR A  135 ? 0.38470 0.30360 0.29560 0.03640  -0.01350 -0.01140 129 THR A OG1 
988  C CG2 . THR A  135 ? 0.40100 0.31700 0.32380 0.03130  -0.03470 -0.01360 129 THR A CG2 
989  N N   . ALA A  136 ? 0.33040 0.25650 0.28940 0.02630  -0.00680 -0.00420 130 ALA A N   
990  C CA  . ALA A  136 ? 0.36380 0.29260 0.32800 0.02690  0.00240  -0.00140 130 ALA A CA  
991  C C   . ALA A  136 ? 0.30630 0.23900 0.25700 0.03130  0.01180  -0.00060 130 ALA A C   
992  O O   . ALA A  136 ? 0.28060 0.22100 0.23770 0.03100  0.01910  0.00440  130 ALA A O   
993  C CB  . ALA A  136 ? 0.31930 0.23650 0.28500 0.02740  -0.00170 -0.00640 130 ALA A CB  
994  N N   . VAL A  137 ? 0.29140 0.21980 0.22390 0.03580  0.01140  -0.00470 131 VAL A N   
995  C CA  . VAL A  137 ? 0.31890 0.25250 0.24230 0.03970  0.02070  -0.00230 131 VAL A CA  
996  C C   . VAL A  137 ? 0.31730 0.26040 0.24620 0.03720  0.02460  0.00480  131 VAL A C   
997  O O   . VAL A  137 ? 0.33020 0.27880 0.25880 0.03840  0.03150  0.00850  131 VAL A O   
998  C CB  . VAL A  137 ? 0.37420 0.30250 0.27620 0.04610  0.02020  -0.00680 131 VAL A CB  
999  C CG1 . VAL A  137 ? 0.33050 0.26110 0.22380 0.04590  0.01690  -0.00400 131 VAL A CG1 
1000 C CG2 . VAL A  137 ? 0.38600 0.31870 0.28160 0.05150  0.03040  -0.00530 131 VAL A CG2 
1001 N N   . CYS A  138 ? 0.32250 0.26720 0.25830 0.03390  0.01940  0.00660  132 CYS A N   
1002 C CA  . CYS A  138 ? 0.30730 0.25840 0.24890 0.03240  0.02150  0.01200  132 CYS A CA  
1003 C C   . CYS A  138 ? 0.29970 0.25590 0.25520 0.03080  0.02430  0.01410  132 CYS A C   
1004 O O   . CYS A  138 ? 0.30400 0.26380 0.26320 0.03090  0.02570  0.01690  132 CYS A O   
1005 C CB  . CYS A  138 ? 0.28430 0.23510 0.22620 0.03140  0.01470  0.01300  132 CYS A CB  
1006 S SG  . CYS A  138 ? 0.35180 0.29650 0.27390 0.03450  0.00950  0.01070  132 CYS A SG  
1007 N N   . SER A  139 ? 0.28160 0.23730 0.24380 0.03020  0.02490  0.01290  133 SER A N   
1008 C CA  . SER A  139 ? 0.27520 0.23660 0.24780 0.03010  0.02820  0.01600  133 SER A CA  
1009 C C   . SER A  139 ? 0.26080 0.22500 0.23050 0.03200  0.03270  0.01700  133 SER A C   
1010 O O   . SER A  139 ? 0.26480 0.22760 0.22920 0.03280  0.03500  0.01630  133 SER A O   
1011 C CB  . SER A  139 ? 0.31590 0.27590 0.29500 0.02950  0.02920  0.01640  133 SER A CB  
1012 O OG  . SER A  139 ? 0.34590 0.31220 0.33020 0.03110  0.03400  0.02010  133 SER A OG  
1013 N N   . ASN A  140 ? 0.23510 0.20340 0.20900 0.03340  0.03330  0.01860  134 ASN A N   
1014 C CA  . ASN A  140 ? 0.27900 0.24840 0.25110 0.03510  0.03490  0.01840  134 ASN A CA  
1015 C C   . ASN A  140 ? 0.25820 0.22880 0.23040 0.03620  0.03800  0.01860  134 ASN A C   
1016 O O   . ASN A  140 ? 0.27140 0.24280 0.24280 0.03700  0.03830  0.01840  134 ASN A O   
1017 C CB  . ASN A  140 ? 0.26060 0.23230 0.23480 0.03830  0.03390  0.01800  134 ASN A CB  
1018 C CG  . ASN A  140 ? 0.29380 0.27060 0.27000 0.04180  0.03730  0.01940  134 ASN A CG  
1019 O OD1 . ASN A  140 ? 0.30060 0.27840 0.27310 0.04520  0.03820  0.01850  134 ASN A OD1 
1020 N ND2 . ASN A  140 ? 0.25230 0.23280 0.23490 0.04110  0.03870  0.02230  134 ASN A ND2 
1021 N N   . CYS A  141 ? 0.22440 0.19500 0.19950 0.03590  0.03940  0.01970  135 CYS A N   
1022 C CA  . CYS A  141 ? 0.25750 0.22830 0.23350 0.03730  0.04200  0.02090  135 CYS A CA  
1023 C C   . CYS A  141 ? 0.25560 0.22120 0.22950 0.03660  0.04220  0.01890  135 CYS A C   
1024 O O   . CYS A  141 ? 0.26590 0.22980 0.24210 0.03780  0.04360  0.01970  135 CYS A O   
1025 C CB  . CYS A  141 ? 0.29100 0.26480 0.27310 0.03810  0.04370  0.02500  135 CYS A CB  
1026 S SG  . CYS A  141 ? 0.26710 0.24850 0.24830 0.04240  0.04540  0.02710  135 CYS A SG  
1027 N N   . SER A  142 ? 0.25360 0.21640 0.22220 0.03560  0.04080  0.01640  136 SER A N   
1028 C CA  . SER A  142 ? 0.23780 0.19490 0.20110 0.03700  0.04090  0.01320  136 SER A CA  
1029 C C   . SER A  142 ? 0.30650 0.26560 0.26980 0.04020  0.04510  0.01360  136 SER A C   
1030 O O   . SER A  142 ? 0.29540 0.24940 0.25730 0.04290  0.04570  0.01120  136 SER A O   
1031 C CB  . SER A  142 ? 0.26190 0.21710 0.21610 0.03720  0.03950  0.01120  136 SER A CB  
1032 O OG  . SER A  142 ? 0.30160 0.26270 0.25480 0.03730  0.04250  0.01450  136 SER A OG  
1033 N N   . GLY A  143 ? 0.29260 0.25870 0.25890 0.04030  0.04710  0.01650  137 GLY A N   
1034 C CA  . GLY A  143 ? 0.28770 0.25770 0.25740 0.04320  0.05040  0.01770  137 GLY A CA  
1035 C C   . GLY A  143 ? 0.27490 0.24350 0.24900 0.04500  0.05010  0.01850  137 GLY A C   
1036 O O   . GLY A  143 ? 0.28450 0.25190 0.25980 0.04860  0.05220  0.01810  137 GLY A O   
1037 N N   . LYS A  144 ? 0.25170 0.22090 0.22790 0.04350  0.04800  0.02040  138 LYS A N   
1038 C CA  . LYS A  144 ? 0.30190 0.27020 0.28160 0.04540  0.04830  0.02330  138 LYS A CA  
1039 C C   . LYS A  144 ? 0.29470 0.25450 0.27610 0.04540  0.04810  0.02240  138 LYS A C   
1040 O O   . LYS A  144 ? 0.25810 0.21460 0.24270 0.04810  0.04870  0.02370  138 LYS A O   
1041 C CB  . LYS A  144 ? 0.26640 0.23810 0.24590 0.04500  0.04750  0.02630  138 LYS A CB  
1042 C CG  . LYS A  144 ? 0.26630 0.23760 0.24930 0.04670  0.04890  0.03180  138 LYS A CG  
1043 C CD  . LYS A  144 ? 0.27370 0.25110 0.25450 0.04840  0.05000  0.03570  138 LYS A CD  
1044 C CE  . LYS A  144 ? 0.27470 0.25290 0.25750 0.04570  0.05010  0.03500  138 LYS A CE  
1045 N NZ  . LYS A  144 ? 0.23490 0.22040 0.21640 0.04920  0.05310  0.04000  138 LYS A NZ  
1046 N N   . HIS A  145 ? 0.27250 0.22740 0.25230 0.04260  0.04590  0.01960  139 HIS A N   
1047 C CA  . HIS A  145 ? 0.29250 0.23710 0.27490 0.04200  0.04290  0.01750  139 HIS A CA  
1048 C C   . HIS A  145 ? 0.33030 0.26810 0.30680 0.04670  0.04340  0.01190  139 HIS A C   
1049 O O   . HIS A  145 ? 0.29260 0.22120 0.27260 0.04860  0.04140  0.01060  139 HIS A O   
1050 C CB  . HIS A  145 ? 0.24040 0.18200 0.22320 0.03790  0.03850  0.01560  139 HIS A CB  
1051 C CG  . HIS A  145 ? 0.25630 0.20320 0.24980 0.03440  0.03820  0.02230  139 HIS A CG  
1052 N ND1 . HIS A  145 ? 0.23350 0.17550 0.23890 0.03140  0.03500  0.02590  139 HIS A ND1 
1053 C CD2 . HIS A  145 ? 0.27400 0.23110 0.26860 0.03450  0.04140  0.02680  139 HIS A CD2 
1054 C CE1 . HIS A  145 ? 0.24100 0.19230 0.25540 0.02970  0.03770  0.03380  139 HIS A CE1 
1055 N NE2 . HIS A  145 ? 0.29640 0.25660 0.30260 0.03240  0.04170  0.03360  139 HIS A NE2 
1056 N N   . VAL A  146 ? 0.28510 0.22720 0.25320 0.04920  0.04620  0.00900  140 VAL A N   
1057 C CA  . VAL A  146 ? 0.29730 0.23560 0.25940 0.05570  0.04870  0.00450  140 VAL A CA  
1058 C C   . VAL A  146 ? 0.30370 0.24500 0.27350 0.05940  0.05170  0.00780  140 VAL A C   
1059 O O   . VAL A  146 ? 0.30000 0.23330 0.26960 0.06480  0.05160  0.00450  140 VAL A O   
1060 C CB  . VAL A  146 ? 0.30600 0.25180 0.25940 0.05820  0.05310  0.00380  140 VAL A CB  
1061 C CG1 . VAL A  146 ? 0.29510 0.24020 0.24300 0.06710  0.05810  0.00050  140 VAL A CG1 
1062 C CG2 . VAL A  146 ? 0.29970 0.24110 0.24310 0.05590  0.04940  0.00040  140 VAL A CG2 
1063 N N   . GLY A  147 ? 0.28670 0.23860 0.26310 0.05730  0.05330  0.01380  141 GLY A N   
1064 C CA  . GLY A  147 ? 0.29420 0.24950 0.27800 0.06090  0.05460  0.01750  141 GLY A CA  
1065 C C   . GLY A  147 ? 0.30290 0.24830 0.29130 0.06130  0.05180  0.01920  141 GLY A C   
1066 O O   . GLY A  147 ? 0.28910 0.23050 0.28120 0.06640  0.05230  0.01940  141 GLY A O   
1067 N N   . MET A  148 ? 0.26890 0.21060 0.25890 0.05610  0.04890  0.02150  142 MET A N   
1068 C CA  A MET A  148 ? 0.28390 0.21670 0.28150 0.05560  0.04640  0.02560  142 MET A CA  
1069 C CA  B MET A  148 ? 0.28400 0.21680 0.28170 0.05530  0.04630  0.02560  142 MET A CA  
1070 C C   . MET A  148 ? 0.30250 0.21980 0.30010 0.05760  0.04270  0.01890  142 MET A C   
1071 O O   . MET A  148 ? 0.32970 0.23800 0.33380 0.06030  0.04090  0.02070  142 MET A O   
1072 C CB  A MET A  148 ? 0.28810 0.22390 0.29020 0.04980  0.04530  0.03170  142 MET A CB  
1073 C CB  B MET A  148 ? 0.28860 0.22340 0.29060 0.04930  0.04490  0.03090  142 MET A CB  
1074 C CG  A MET A  148 ? 0.29590 0.24430 0.29630 0.05080  0.04840  0.03800  142 MET A CG  
1075 C CG  B MET A  148 ? 0.29880 0.24680 0.29860 0.04890  0.04790  0.03640  142 MET A CG  
1076 S SD  A MET A  148 ? 0.25900 0.21320 0.26340 0.04690  0.04960  0.04600  142 MET A SD  
1077 S SD  B MET A  148 ? 0.31080 0.26370 0.31370 0.05280  0.04990  0.04650  142 MET A SD  
1078 C CE  A MET A  148 ? 0.25960 0.22670 0.25440 0.05120  0.05210  0.04840  142 MET A CE  
1079 C CE  B MET A  148 ? 0.28810 0.25420 0.28180 0.05370  0.05140  0.04730  142 MET A CE  
1080 N N   . LEU A  149 ? 0.29440 0.20730 0.28370 0.05710  0.04070  0.01100  143 LEU A N   
1081 C CA  . LEU A  149 ? 0.28730 0.18470 0.27170 0.06150  0.03640  0.00190  143 LEU A CA  
1082 C C   . LEU A  149 ? 0.32500 0.22180 0.30670 0.07090  0.04070  -0.00070 143 LEU A C   
1083 O O   . LEU A  149 ? 0.36190 0.24460 0.34610 0.07570  0.03730  -0.00430 143 LEU A O   
1084 C CB  . LEU A  149 ? 0.35610 0.25180 0.32710 0.06180  0.03470  -0.00620 143 LEU A CB  
1085 C CG  . LEU A  149 ? 0.44930 0.33540 0.42120 0.05590  0.02580  -0.00960 143 LEU A CG  
1086 C CD1 . LEU A  149 ? 0.38670 0.27460 0.34210 0.05770  0.02530  -0.01640 143 LEU A CD1 
1087 C CD2 . LEU A  149 ? 0.44700 0.31290 0.42360 0.05750  0.01700  -0.01520 143 LEU A CD2 
1088 N N   . ALA A  150 ? 0.33590 0.24800 0.31410 0.07370  0.04780  0.00140  144 ALA A N   
1089 C CA  . ALA A  150 ? 0.32150 0.23730 0.29980 0.08300  0.05290  0.00020  144 ALA A CA  
1090 C C   . ALA A  150 ? 0.33590 0.24790 0.32610 0.08490  0.05130  0.00560  144 ALA A C   
1091 O O   . ALA A  150 ? 0.36340 0.26610 0.35470 0.09290  0.05100  0.00180  144 ALA A O   
1092 C CB  . ALA A  150 ? 0.32260 0.25770 0.30130 0.08330  0.05960  0.00440  144 ALA A CB  
1093 N N   . GLY A  151 ? 0.34760 0.26620 0.34560 0.07870  0.05020  0.01460  145 GLY A N   
1094 C CA  . GLY A  151 ? 0.30870 0.22490 0.31670 0.08090  0.04880  0.02150  145 GLY A CA  
1095 C C   . GLY A  151 ? 0.34600 0.24260 0.35900 0.08110  0.04330  0.02040  145 GLY A C   
1096 O O   . GLY A  151 ? 0.34830 0.23730 0.36760 0.08700  0.04220  0.02200  145 GLY A O   
1097 N N   . ALA A  152 ? 0.31110 0.19890 0.32350 0.07440  0.03880  0.01830  146 ALA A N   
1098 C CA  . ALA A  152 ? 0.31860 0.18620 0.33880 0.07330  0.03150  0.01690  146 ALA A CA  
1099 C C   . ALA A  152 ? 0.35720 0.20960 0.37120 0.08290  0.02890  0.00490  146 ALA A C   
1100 O O   . ALA A  152 ? 0.35450 0.19160 0.37650 0.08680  0.02460  0.00510  146 ALA A O   
1101 C CB  . ALA A  152 ? 0.31860 0.18130 0.34100 0.06420  0.02600  0.01590  146 ALA A CB  
1102 N N   . ARG A  153 ? 0.38840 0.24400 0.38730 0.08760  0.03170  -0.00540 147 ARG A N   
1103 C CA  . ARG A  153 ? 0.39220 0.23500 0.38120 0.09920  0.03080  -0.01760 147 ARG A CA  
1104 C C   . ARG A  153 ? 0.39230 0.24040 0.38620 0.10920  0.03680  -0.01480 147 ARG A C   
1105 O O   . ARG A  153 ? 0.40100 0.23290 0.39560 0.11830  0.03350  -0.02100 147 ARG A O   
1106 C CB  . ARG A  153 ? 0.39740 0.24690 0.36770 0.10260  0.03450  -0.02650 147 ARG A CB  
1107 C CG  . ARG A  153 ? 0.49580 0.33310 0.45050 0.11660  0.03460  -0.04010 147 ARG A CG  
1108 C CD  . ARG A  153 ? 0.55280 0.38800 0.48680 0.11840  0.03320  -0.04970 147 ARG A CD  
1109 N NE  . ARG A  153 ? 0.55960 0.37490 0.49220 0.11180  0.01950  -0.05640 147 ARG A NE  
1110 C CZ  . ARG A  153 ? 0.60130 0.41370 0.51810 0.11070  0.01500  -0.06360 147 ARG A CZ  
1111 N NH1 . ARG A  153 ? 0.61220 0.43990 0.51240 0.11560  0.02410  -0.06410 147 ARG A NH1 
1112 N NH2 . ARG A  153 ? 0.56250 0.35720 0.48220 0.10400  0.00070  -0.06900 147 ARG A NH2 
1113 N N   . ALA A  154 ? 0.38460 0.25460 0.38360 0.10770  0.04410  -0.00540 148 ALA A N   
1114 C CA  . ALA A  154 ? 0.35290 0.23220 0.35830 0.11690  0.04960  -0.00190 148 ALA A CA  
1115 C C   . ALA A  154 ? 0.44500 0.31060 0.46280 0.11980  0.04450  0.00260  148 ALA A C   
1116 O O   . ALA A  154 ? 0.43330 0.29510 0.45410 0.13120  0.04620  -0.00020 148 ALA A O   
1117 C CB  . ALA A  154 ? 0.39940 0.30310 0.41010 0.11220  0.05500  0.00780  148 ALA A CB  
1118 N N   . ILE A  155 ? 0.40800 0.26740 0.43410 0.11040  0.03900  0.01110  149 ILE A N   
1119 C CA  . ILE A  155 ? 0.45180 0.29820 0.49080 0.11270  0.03420  0.01780  149 ILE A CA  
1120 C C   . ILE A  155 ? 0.45190 0.27050 0.49350 0.11220  0.02510  0.01100  149 ILE A C   
1121 O O   . ILE A  155 ? 0.44600 0.25030 0.50070 0.11210  0.01950  0.01760  149 ILE A O   
1122 C CB  . ILE A  155 ? 0.43110 0.28760 0.47900 0.10450  0.03410  0.03380  149 ILE A CB  
1123 C CG1 . ILE A  155 ? 0.34450 0.20110 0.39130 0.09250  0.03210  0.03670  149 ILE A CG1 
1124 C CG2 . ILE A  155 ? 0.40100 0.28110 0.44740 0.10720  0.04010  0.03950  149 ILE A CG2 
1125 C CD1 . ILE A  155 ? 0.38770 0.24950 0.44370 0.08630  0.03190  0.05290  149 ILE A CD1 
1126 N N   . GLY A  156 ? 0.40870 0.21890 0.43870 0.11180  0.02230  -0.00180 150 GLY A N   
1127 C CA  . GLY A  156 ? 0.48750 0.26960 0.51950 0.11220  0.01120  -0.01060 150 GLY A CA  
1128 C C   . GLY A  156 ? 0.46540 0.23970 0.51200 0.09810  0.00340  -0.00150 150 GLY A C   
1129 O O   . GLY A  156 ? 0.47270 0.22270 0.52930 0.09670  -0.00760 -0.00430 150 GLY A O   
1130 N N   . ALA A  157 ? 0.44170 0.23630 0.49140 0.08820  0.00860  0.01000  151 ALA A N   
1131 C CA  . ALA A  157 ? 0.48400 0.27530 0.54660 0.07540  0.00290  0.01820  151 ALA A CA  
1132 C C   . ALA A  157 ? 0.48810 0.27060 0.54270 0.07180  -0.00430 0.00500  151 ALA A C   
1133 O O   . ALA A  157 ? 0.47610 0.26090 0.51120 0.07850  -0.00200 -0.00820 151 ALA A O   
1134 C CB  . ALA A  157 ? 0.39180 0.20820 0.45690 0.06830  0.01140  0.03280  151 ALA A CB  
1135 N N   . GLY A  158 ? 0.48710 0.25930 0.55760 0.06150  -0.01350 0.00960  152 GLY A N   
1136 C CA  . GLY A  158 ? 0.53040 0.29930 0.59520 0.05630  -0.02050 0.00000  152 GLY A CA  
1137 C C   . GLY A  158 ? 0.45930 0.25330 0.51020 0.05480  -0.01030 0.00120  152 GLY A C   
1138 O O   . GLY A  158 ? 0.45980 0.27360 0.51280 0.05330  0.00000  0.01310  152 GLY A O   
1139 N N   . THR A  159 ? 0.49650 0.28880 0.53180 0.05590  -0.01390 -0.01150 153 THR A N   
1140 C CA  . THR A  159 ? 0.45750 0.27110 0.48280 0.05280  -0.00650 -0.00960 153 THR A CA  
1141 C C   . THR A  159 ? 0.41550 0.23310 0.45360 0.04140  -0.01240 -0.00410 153 THR A C   
1142 O O   . THR A  159 ? 0.40050 0.23720 0.43580 0.03790  -0.00540 0.00150  153 THR A O   
1143 C CB  . THR A  159 ? 0.47990 0.29300 0.47970 0.06160  -0.00490 -0.02410 153 THR A CB  
1144 O OG1 . THR A  159 ? 0.50550 0.29670 0.49870 0.06380  -0.01810 -0.03780 153 THR A OG1 
1145 C CG2 . THR A  159 ? 0.51690 0.33340 0.50640 0.07320  0.00420  -0.02670 153 THR A CG2 
1146 N N   . ASP A  160 ? 0.43120 0.23140 0.48520 0.03550  -0.02570 -0.00540 154 ASP A N   
1147 C CA  . ASP A  160 ? 0.47700 0.28190 0.54440 0.02510  -0.03250 -0.00150 154 ASP A CA  
1148 C C   . ASP A  160 ? 0.41300 0.24130 0.49610 0.01820  -0.02220 0.01700  154 ASP A C   
1149 O O   . ASP A  160 ? 0.44430 0.28690 0.52810 0.01380  -0.02040 0.01960  154 ASP A O   
1150 C CB  . ASP A  160 ? 0.46250 0.24440 0.54950 0.01920  -0.04980 -0.00430 154 ASP A CB  
1151 C CG  . ASP A  160 ? 0.55310 0.34180 0.66100 0.00740  -0.05780 0.00220  154 ASP A CG  
1152 O OD1 . ASP A  160 ? 0.56400 0.36200 0.65960 0.00720  -0.05850 -0.00360 154 ASP A OD1 
1153 O OD2 . ASP A  160 ? 0.62430 0.40950 0.76300 -0.00170 -0.06370 0.01440  154 ASP A OD2 
1154 N N   . GLY A  161 ? 0.41370 0.24610 0.50780 0.01850  -0.01510 0.02970  155 GLY A N   
1155 C CA  . GLY A  161 ? 0.40510 0.25890 0.51150 0.01390  -0.00500 0.04730  155 GLY A CA  
1156 C C   . GLY A  161 ? 0.35600 0.22440 0.44830 0.02080  0.00830  0.05240  155 GLY A C   
1157 O O   . GLY A  161 ? 0.33240 0.21110 0.43490 0.01980  0.01510  0.06770  155 GLY A O   
1158 N N   . TYR A  162 ? 0.32740 0.19710 0.39690 0.02810  0.01160  0.04050  156 TYR A N   
1159 C CA  . TYR A  162 ? 0.32330 0.20670 0.38040 0.03430  0.02200  0.04380  156 TYR A CA  
1160 C C   . TYR A  162 ? 0.31700 0.22060 0.37560 0.03180  0.02960  0.05450  156 TYR A C   
1161 O O   . TYR A  162 ? 0.32140 0.23520 0.37370 0.03610  0.03650  0.06030  156 TYR A O   
1162 C CB  . TYR A  162 ? 0.34520 0.22990 0.38150 0.04070  0.02400  0.03040  156 TYR A CB  
1163 C CG  . TYR A  162 ? 0.30960 0.20340 0.33670 0.03810  0.02470  0.02540  156 TYR A CG  
1164 C CD1 . TYR A  162 ? 0.32270 0.23390 0.34620 0.03730  0.03150  0.03100  156 TYR A CD1 
1165 C CD2 . TYR A  162 ? 0.34730 0.23120 0.36800 0.03750  0.01760  0.01460  156 TYR A CD2 
1166 C CE1 . TYR A  162 ? 0.31220 0.23020 0.32860 0.03520  0.03140  0.02690  156 TYR A CE1 
1167 C CE2 . TYR A  162 ? 0.31330 0.20520 0.32580 0.03540  0.01780  0.01120  156 TYR A CE2 
1168 C CZ  . TYR A  162 ? 0.30880 0.21760 0.32040 0.03410  0.02490  0.01780  156 TYR A CZ  
1169 O OH  . TYR A  162 ? 0.30610 0.22140 0.31120 0.03220  0.02430  0.01480  156 TYR A OH  
1170 N N   . HIS A  163 ? 0.29810 0.20720 0.36430 0.02580  0.02780  0.05650  157 HIS A N   
1171 C CA  . HIS A  163 ? 0.31540 0.24330 0.38180 0.02490  0.03510  0.06490  157 HIS A CA  
1172 C C   . HIS A  163 ? 0.30700 0.24250 0.39180 0.02200  0.03900  0.08210  157 HIS A C   
1173 O O   . HIS A  163 ? 0.34470 0.29680 0.42790 0.02380  0.04670  0.09020  157 HIS A O   
1174 C CB  . HIS A  163 ? 0.28950 0.22140 0.35530 0.02120  0.03190  0.05880  157 HIS A CB  
1175 C CG  . HIS A  163 ? 0.34080 0.26500 0.42630 0.01370  0.02300  0.06050  157 HIS A CG  
1176 N ND1 . HIS A  163 ? 0.30240 0.20700 0.39190 0.01190  0.01280  0.05300  157 HIS A ND1 
1177 C CD2 . HIS A  163 ? 0.36100 0.29430 0.46460 0.00790  0.02190  0.06860  157 HIS A CD2 
1178 C CE1 . HIS A  163 ? 0.35420 0.25490 0.46380 0.00440  0.00420  0.05600  157 HIS A CE1 
1179 N NE2 . HIS A  163 ? 0.33330 0.25250 0.45340 0.00150  0.00990  0.06630  157 HIS A NE2 
1180 N N   . LEU A  164 ? 0.29890 0.22250 0.40090 0.01820  0.03390  0.08810  158 LEU A N   
1181 C CA  . LEU A  164 ? 0.31060 0.24050 0.43530 0.01400  0.03690  0.10700  158 LEU A CA  
1182 C C   . LEU A  164 ? 0.40130 0.33850 0.51920 0.02040  0.04590  0.11870  158 LEU A C   
1183 O O   . LEU A  164 ? 0.34640 0.27420 0.45260 0.02560  0.04450  0.11290  158 LEU A O   
1184 C CB  . LEU A  164 ? 0.33690 0.24810 0.48460 0.00680  0.02590  0.10860  158 LEU A CB  
1185 C CG  . LEU A  164 ? 0.37730 0.27900 0.53510 -0.00020 0.01390  0.09830  158 LEU A CG  
1186 C CD1 . LEU A  164 ? 0.35880 0.23780 0.53760 -0.00610 0.00060  0.09830  158 LEU A CD1 
1187 C CD2 . LEU A  164 ? 0.35210 0.27310 0.52460 -0.00540 0.01760  0.10800  158 LEU A CD2 
1188 N N   . PRO A  165 ? 0.35560 0.31020 0.48080 0.02110  0.05500  0.13570  159 PRO A N   
1189 C CA  . PRO A  165 ? 0.40200 0.36460 0.51660 0.02870  0.06330  0.14720  159 PRO A CA  
1190 C C   . PRO A  165 ? 0.41570 0.36330 0.53720 0.02920  0.05930  0.15260  159 PRO A C   
1191 O O   . PRO A  165 ? 0.50270 0.45160 0.60770 0.03700  0.06220  0.15290  159 PRO A O   
1192 C CB  . PRO A  165 ? 0.36570 0.34790 0.49270 0.02830  0.07320  0.16680  159 PRO A CB  
1193 C CG  . PRO A  165 ? 0.36370 0.35280 0.49760 0.02370  0.07190  0.16030  159 PRO A CG  
1194 C CD  . PRO A  165 ? 0.33170 0.30070 0.47390 0.01620  0.05850  0.14550  159 PRO A CD  
1195 N N   . ASP A  166 ? 0.43790 0.37070 0.58420 0.02140  0.05160  0.15700  160 ASP A N   
1196 C CA  . ASP A  166 ? 0.42140 0.33710 0.57680 0.02190  0.04670  0.16240  160 ASP A CA  
1197 C C   . ASP A  166 ? 0.42250 0.31860 0.56580 0.02530  0.03780  0.14180  160 ASP A C   
1198 O O   . ASP A  166 ? 0.37720 0.25510 0.53010 0.02570  0.03130  0.14270  160 ASP A O   
1199 C CB  . ASP A  166 ? 0.43430 0.34050 0.62390 0.01190  0.04080  0.17610  160 ASP A CB  
1200 C CG  . ASP A  166 ? 0.59150 0.51920 0.79680 0.00950  0.05130  0.20080  160 ASP A CG  
1201 O OD1 . ASP A  166 ? 0.53290 0.46930 0.73290 0.01470  0.05740  0.21220  160 ASP A OD1 
1202 O OD2 . ASP A  166 ? 0.59740 0.53740 0.81800 0.00310  0.05250  0.20490  160 ASP A OD2 
1203 N N   . HIS A  167 ? 0.38170 0.28090 0.50520 0.02830  0.03750  0.12420  161 HIS A N   
1204 C CA  . HIS A  167 ? 0.37120 0.25520 0.48250 0.03310  0.03140  0.10640  161 HIS A CA  
1205 C C   . HIS A  167 ? 0.34070 0.23180 0.43480 0.04260  0.03700  0.10620  161 HIS A C   
1206 O O   . HIS A  167 ? 0.33450 0.24360 0.41690 0.04560  0.04440  0.11110  161 HIS A O   
1207 C CB  . HIS A  167 ? 0.33950 0.22410 0.43930 0.03170  0.02860  0.08930  161 HIS A CB  
1208 C CG  . HIS A  167 ? 0.36100 0.23050 0.44910 0.03690  0.02290  0.07180  161 HIS A CG  
1209 N ND1 . HIS A  167 ? 0.34590 0.22060 0.41690 0.04530  0.02760  0.06520  161 HIS A ND1 
1210 C CD2 . HIS A  167 ? 0.41060 0.26070 0.50120 0.03590  0.01310  0.05950  161 HIS A CD2 
1211 C CE1 . HIS A  167 ? 0.42370 0.28460 0.48790 0.04970  0.02270  0.05090  161 HIS A CE1 
1212 N NE2 . HIS A  167 ? 0.41840 0.26330 0.49200 0.04480  0.01380  0.04640  161 HIS A NE2 
1213 N N   . PRO A  168 ? 0.39840 0.23390 0.36270 0.14000  0.01420  -0.00520 162 PRO A N   
1214 C CA  . PRO A  168 ? 0.37240 0.22030 0.34200 0.14820  0.01330  0.00130  162 PRO A CA  
1215 C C   . PRO A  168 ? 0.36140 0.23930 0.33150 0.14530  0.01870  0.00490  162 PRO A C   
1216 O O   . PRO A  168 ? 0.35760 0.24370 0.33040 0.14600  0.01730  0.01400  162 PRO A O   
1217 C CB  . PRO A  168 ? 0.39960 0.24690 0.37720 0.16400  0.01140  -0.01040 162 PRO A CB  
1218 C CG  . PRO A  168 ? 0.41350 0.23800 0.38930 0.16380  0.00880  -0.02020 162 PRO A CG  
1219 C CD  . PRO A  168 ? 0.38910 0.21360 0.35630 0.14920  0.01220  -0.01920 162 PRO A CD  
1220 N N   . MET A  169 ? 0.33130 0.22520 0.29900 0.14200  0.02380  -0.00180 163 MET A N   
1221 C CA  A MET A  169 ? 0.32580 0.24610 0.29490 0.13840  0.02790  0.00280  163 MET A CA  
1222 C CA  B MET A  169 ? 0.32580 0.24620 0.29490 0.13850  0.02790  0.00280  163 MET A CA  
1223 C C   . MET A  169 ? 0.34270 0.26230 0.30970 0.12680  0.02700  0.01360  163 MET A C   
1224 O O   . MET A  169 ? 0.31380 0.24850 0.28470 0.12610  0.02740  0.02050  163 MET A O   
1225 C CB  A MET A  169 ? 0.34650 0.28160 0.31150 0.13620  0.03240  -0.00490 163 MET A CB  
1226 C CB  B MET A  169 ? 0.34650 0.28160 0.31150 0.13640  0.03240  -0.00520 163 MET A CB  
1227 C CG  A MET A  169 ? 0.32510 0.28610 0.29190 0.13180  0.03600  0.00070  163 MET A CG  
1228 C CG  B MET A  169 ? 0.32720 0.29100 0.29530 0.13650  0.03690  -0.00230 163 MET A CG  
1229 S SD  A MET A  169 ? 0.32220 0.30880 0.29850 0.14230  0.04000  0.00010  163 MET A SD  
1230 S SD  B MET A  169 ? 0.36130 0.34180 0.34100 0.14990  0.03890  -0.00360 163 MET A SD  
1231 C CE  A MET A  169 ? 0.30200 0.27500 0.28210 0.15710  0.03850  -0.01130 163 MET A CE  
1232 C CE  B MET A  169 ? 0.28190 0.27260 0.26790 0.14390  0.03680  0.01050  163 MET A CE  
1233 N N   . GLN A  170 ? 0.31010 0.21310 0.27210 0.11750  0.02580  0.01420  164 GLN A N   
1234 C CA  . GLN A  170 ? 0.33200 0.23630 0.29290 0.10670  0.02580  0.02260  164 GLN A CA  
1235 C C   . GLN A  170 ? 0.33320 0.22790 0.29260 0.10760  0.02270  0.03180  164 GLN A C   
1236 O O   . GLN A  170 ? 0.34610 0.25000 0.30520 0.10210  0.02300  0.03870  164 GLN A O   
1237 C CB  . GLN A  170 ? 0.35170 0.24450 0.30980 0.09600  0.02620  0.01960  164 GLN A CB  
1238 C CG  . GLN A  170 ? 0.32370 0.22630 0.28240 0.09410  0.02740  0.01180  164 GLN A CG  
1239 C CD  . GLN A  170 ? 0.33860 0.26450 0.30010 0.09480  0.02900  0.01420  164 GLN A CD  
1240 O OE1 . GLN A  170 ? 0.28950 0.22450 0.25450 0.08990  0.02920  0.02060  164 GLN A OE1 
1241 N NE2 . GLN A  170 ? 0.34670 0.28300 0.30650 0.10040  0.03030  0.00900  164 GLN A NE2 
1242 N N   . GLY A  171 ? 0.36990 0.24490 0.32790 0.11400  0.01900  0.03180  165 GLY A N   
1243 C CA  . GLY A  171 ? 0.32830 0.19430 0.28430 0.11710  0.01420  0.04140  165 GLY A CA  
1244 C C   . GLY A  171 ? 0.41410 0.30150 0.37590 0.12410  0.01340  0.04460  165 GLY A C   
1245 O O   . GLY A  171 ? 0.39780 0.28950 0.35680 0.12050  0.01140  0.05330  165 GLY A O   
1246 N N   . ARG A  172 ? 0.36900 0.27170 0.33920 0.13370  0.01540  0.03690  166 ARG A N   
1247 C CA  . ARG A  172 ? 0.31260 0.23890 0.29090 0.13930  0.01550  0.03900  166 ARG A CA  
1248 C C   . ARG A  172 ? 0.34830 0.29180 0.32580 0.12880  0.01860  0.04340  166 ARG A C   
1249 O O   . ARG A  172 ? 0.35840 0.31240 0.33880 0.12860  0.01610  0.04970  166 ARG A O   
1250 C CB  . ARG A  172 ? 0.32930 0.27130 0.31650 0.14940  0.01910  0.02900  166 ARG A CB  
1251 C CG  . ARG A  172 ? 0.31510 0.24820 0.30960 0.16380  0.01480  0.02410  166 ARG A CG  
1252 C CD  . ARG A  172 ? 0.34100 0.27490 0.33760 0.16990  0.01880  0.01040  166 ARG A CD  
1253 N NE  . ARG A  172 ? 0.38540 0.30840 0.39110 0.17850  0.01300  0.00410  166 ARG A NE  
1254 C CZ  . ARG A  172 ? 0.34500 0.28540 0.36490 0.18640  0.01250  -0.00100 166 ARG A CZ  
1255 N NH1 . ARG A  172 ? 0.36490 0.33420 0.39060 0.18600  0.01770  -0.00050 166 ARG A NH1 
1256 N NH2 . ARG A  172 ? 0.36530 0.29410 0.39580 0.19430  0.00650  -0.00680 166 ARG A NH2 
1257 N N   . VAL A  173 ? 0.30540 0.25160 0.28000 0.12030  0.02280  0.03960  167 VAL A N   
1258 C CA  . VAL A  173 ? 0.30110 0.26230 0.27730 0.11090  0.02460  0.04260  167 VAL A CA  
1259 C C   . VAL A  173 ? 0.32330 0.27730 0.29450 0.10370  0.02220  0.04940  167 VAL A C   
1260 O O   . VAL A  173 ? 0.31840 0.28560 0.29280 0.10140  0.02090  0.05350  167 VAL A O   
1261 C CB  . VAL A  173 ? 0.26680 0.22880 0.24130 0.10380  0.02770  0.03710  167 VAL A CB  
1262 C CG1 . VAL A  173 ? 0.28020 0.25000 0.25680 0.09300  0.02770  0.03970  167 VAL A CG1 
1263 C CG2 . VAL A  173 ? 0.29270 0.26800 0.27010 0.10920  0.03050  0.03160  167 VAL A CG2 
1264 N N   . LYS A  174 ? 0.32950 0.26270 0.29250 0.09960  0.02160  0.05050  168 LYS A N   
1265 C CA  . LYS A  174 ? 0.36370 0.29040 0.31940 0.09120  0.02050  0.05710  168 LYS A CA  
1266 C C   . LYS A  174 ? 0.37280 0.30270 0.32670 0.09660  0.01560  0.06460  168 LYS A C   
1267 O O   . LYS A  174 ? 0.33690 0.27730 0.28910 0.09150  0.01490  0.06820  168 LYS A O   
1268 C CB  . LYS A  174 ? 0.38080 0.28380 0.32810 0.08600  0.02090  0.05800  168 LYS A CB  
1269 C CG  . LYS A  174 ? 0.42420 0.32550 0.37370 0.07770  0.02520  0.05080  168 LYS A CG  
1270 C CD  . LYS A  174 ? 0.43330 0.31340 0.37540 0.06920  0.02600  0.05330  168 LYS A CD  
1271 C CE  . LYS A  174 ? 0.48690 0.36850 0.43340 0.05940  0.03010  0.04590  168 LYS A CE  
1272 N NZ  . LYS A  174 ? 0.43700 0.32130 0.39000 0.06530  0.02940  0.03710  168 LYS A NZ  
1273 N N   . ARG A  175 ? 0.34140 0.26310 0.29680 0.10760  0.01140  0.06590  169 ARG A N   
1274 C CA  A ARG A  175 ? 0.37310 0.29680 0.32840 0.11440  0.00480  0.07280  169 ARG A CA  
1275 C CA  B ARG A  175 ? 0.37320 0.29680 0.32850 0.11420  0.00480  0.07290  169 ARG A CA  
1276 C C   . ARG A  175 ? 0.37430 0.32450 0.33980 0.11670  0.00480  0.07180  169 ARG A C   
1277 O O   . ARG A  175 ? 0.38980 0.34640 0.35300 0.11550  0.00040  0.07750  169 ARG A O   
1278 C CB  A ARG A  175 ? 0.38490 0.29600 0.34460 0.12740  -0.00020 0.07190  169 ARG A CB  
1279 C CB  B ARG A  175 ? 0.38540 0.29540 0.34450 0.12700  -0.00030 0.07220  169 ARG A CB  
1280 C CG  A ARG A  175 ? 0.40510 0.29150 0.35440 0.12780  -0.00740 0.08080  169 ARG A CG  
1281 C CG  B ARG A  175 ? 0.37430 0.28870 0.33790 0.13680  -0.00850 0.07770  169 ARG A CG  
1282 C CD  A ARG A  175 ? 0.40120 0.28150 0.36040 0.14220  -0.01500 0.07920  169 ARG A CD  
1283 C CD  B ARG A  175 ? 0.38500 0.28590 0.35580 0.14740  -0.01450 0.07450  169 ARG A CD  
1284 N NE  A ARG A  175 ? 0.41370 0.30110 0.38570 0.15000  -0.01070 0.06670  169 ARG A NE  
1285 N NE  B ARG A  175 ? 0.37030 0.28510 0.35580 0.15520  -0.00990 0.06230  169 ARG A NE  
1286 C CZ  A ARG A  175 ? 0.39460 0.26450 0.36480 0.15070  -0.00860 0.06090  169 ARG A CZ  
1287 C CZ  B ARG A  175 ? 0.35800 0.29720 0.35810 0.16100  -0.00950 0.05730  169 ARG A CZ  
1288 N NH1 A ARG A  175 ? 0.42510 0.27130 0.38280 0.14190  -0.00890 0.06620  169 ARG A NH1 
1289 N NH1 B ARG A  175 ? 0.36460 0.31770 0.36850 0.15990  -0.01380 0.06260  169 ARG A NH1 
1290 N NH2 A ARG A  175 ? 0.37350 0.25140 0.35530 0.15890  -0.00620 0.04870  169 ARG A NH2 
1291 N NH2 B ARG A  175 ? 0.32350 0.27400 0.33450 0.16740  -0.00450 0.04630  169 ARG A NH2 
1292 N N   . THR A  176 ? 0.33650 0.30240 0.31300 0.11940  0.00930  0.06470  170 THR A N   
1293 C CA  . THR A  176 ? 0.32040 0.31110 0.30850 0.12110  0.00940  0.06420  170 THR A CA  
1294 C C   . THR A  176 ? 0.32480 0.32480 0.31130 0.11000  0.01020  0.06590  170 THR A C   
1295 O O   . THR A  176 ? 0.30180 0.31480 0.29300 0.11000  0.00650  0.06880  170 THR A O   
1296 C CB  . THR A  176 ? 0.32810 0.33190 0.32580 0.12500  0.01470  0.05730  170 THR A CB  
1297 O OG1 . THR A  176 ? 0.37530 0.37080 0.37510 0.13620  0.01400  0.05360  170 THR A OG1 
1298 C CG2 . THR A  176 ? 0.31640 0.34590 0.32750 0.12660  0.01490  0.05780  170 THR A CG2 
1299 N N   . VAL A  177 ? 0.30750 0.30040 0.28830 0.10070  0.01410  0.06340  171 VAL A N   
1300 C CA  . VAL A  177 ? 0.32800 0.32890 0.30870 0.09080  0.01460  0.06310  171 VAL A CA  
1301 C C   . VAL A  177 ? 0.31580 0.31290 0.28700 0.08830  0.01070  0.06850  171 VAL A C   
1302 O O   . VAL A  177 ? 0.31480 0.32560 0.28980 0.08610  0.00800  0.06890  171 VAL A O   
1303 C CB  . VAL A  177 ? 0.28470 0.27820 0.26280 0.08240  0.01910  0.05840  171 VAL A CB  
1304 C CG1 . VAL A  177 ? 0.22670 0.22800 0.20620 0.07280  0.01950  0.05640  171 VAL A CG1 
1305 C CG2 . VAL A  177 ? 0.31490 0.31480 0.30110 0.08460  0.02150  0.05390  171 VAL A CG2 
1306 N N   . ALA A  178 ? 0.31200 0.29010 0.27010 0.08810  0.00970  0.07290  172 ALA A N   
1307 C CA  . ALA A  178 ? 0.32970 0.30380 0.27520 0.08430  0.00590  0.07920  172 ALA A CA  
1308 C C   . ALA A  178 ? 0.36370 0.34840 0.31330 0.09240  -0.00170 0.08320  172 ALA A C   
1309 O O   . ALA A  178 ? 0.34190 0.33560 0.28700 0.08860  -0.00490 0.08500  172 ALA A O   
1310 C CB  . ALA A  178 ? 0.36090 0.31060 0.29120 0.08250  0.00530  0.08530  172 ALA A CB  
1311 N N   . GLU A  179 ? 0.32370 0.30890 0.28300 0.10380  -0.00460 0.08350  173 GLU A N   
1312 C CA  . GLU A  179 ? 0.32030 0.31690 0.28730 0.11260  -0.01220 0.08640  173 GLU A CA  
1313 C C   . GLU A  179 ? 0.34010 0.36150 0.32000 0.10980  -0.01180 0.08230  173 GLU A C   
1314 O O   . GLU A  179 ? 0.32570 0.35630 0.30540 0.10990  -0.01820 0.08490  173 GLU A O   
1315 C CB  . GLU A  179 ? 0.38420 0.37850 0.36220 0.12550  -0.01390 0.08490  173 GLU A CB  
1316 C CG  . GLU A  179 ? 0.36470 0.33230 0.33150 0.12970  -0.01770 0.08970  173 GLU A CG  
1317 C CD  . GLU A  179 ? 0.39770 0.36180 0.37720 0.13980  -0.01860 0.08370  173 GLU A CD  
1318 O OE1 . GLU A  179 ? 0.46850 0.45120 0.46360 0.14390  -0.01440 0.07590  173 GLU A OE1 
1319 O OE2 . GLU A  179 ? 0.45000 0.39220 0.42360 0.14260  -0.02350 0.08650  173 GLU A OE2 
1320 N N   . LEU A  180 ? 0.28440 0.31610 0.27530 0.10670  -0.00530 0.07630  174 LEU A N   
1321 C CA  . LEU A  180 ? 0.27810 0.33120 0.28240 0.10340  -0.00590 0.07340  174 LEU A CA  
1322 C C   . LEU A  180 ? 0.24900 0.30370 0.24600 0.09380  -0.00730 0.07230  174 LEU A C   
1323 O O   . LEU A  180 ? 0.27480 0.34450 0.27980 0.09240  -0.01170 0.07120  174 LEU A O   
1324 C CB  . LEU A  180 ? 0.24870 0.31040 0.26470 0.10120  0.00040  0.06880  174 LEU A CB  
1325 C CG  . LEU A  180 ? 0.25630 0.32500 0.28250 0.11000  0.00270  0.06800  174 LEU A CG  
1326 C CD1 . LEU A  180 ? 0.25800 0.33100 0.28860 0.10560  0.00930  0.06450  174 LEU A CD1 
1327 C CD2 . LEU A  180 ? 0.24800 0.33640 0.28930 0.11540  -0.00170 0.06930  174 LEU A CD2 
1328 N N   . CYS A  181 ? 0.27360 0.31440 0.25660 0.08690  -0.00350 0.07170  175 CYS A N   
1329 C CA  . CYS A  181 ? 0.24390 0.28690 0.21860 0.07780  -0.00360 0.06930  175 CYS A CA  
1330 C C   . CYS A  181 ? 0.32930 0.36910 0.28890 0.07860  -0.00980 0.07500  175 CYS A C   
1331 O O   . CYS A  181 ? 0.34030 0.38600 0.29250 0.07150  -0.01040 0.07230  175 CYS A O   
1332 C CB  . CYS A  181 ? 0.26300 0.29400 0.22890 0.06980  0.00350  0.06630  175 CYS A CB  
1333 S SG  . CYS A  181 ? 0.26730 0.30460 0.25020 0.06680  0.00850  0.05850  175 CYS A SG  
1334 N N   . ASP A  182 ? 0.33870 0.36940 0.29360 0.08710  -0.01480 0.08240  176 ASP A N   
1335 C CA  . ASP A  182 ? 0.33720 0.35930 0.27420 0.08780  -0.02190 0.09020  176 ASP A CA  
1336 C C   . ASP A  182 ? 0.36280 0.37170 0.27830 0.07700  -0.01710 0.09240  176 ASP A C   
1337 O O   . ASP A  182 ? 0.36380 0.37600 0.26450 0.07090  -0.01950 0.09400  176 ASP A O   
1338 C CB  . ASP A  182 ? 0.34010 0.37950 0.28040 0.08880  -0.02980 0.08940  176 ASP A CB  
1339 C CG  . ASP A  182 ? 0.36220 0.41660 0.32550 0.09850  -0.03450 0.08770  176 ASP A CG  
1340 O OD1 . ASP A  182 ? 0.38750 0.43560 0.35740 0.10780  -0.03570 0.09090  176 ASP A OD1 
1341 O OD2 . ASP A  182 ? 0.35030 0.42320 0.32600 0.09670  -0.03690 0.08250  176 ASP A OD2 
1342 N N   . LEU A  183 ? 0.34300 0.33770 0.25640 0.07420  -0.01000 0.09200  177 LEU A N   
1343 C CA  . LEU A  183 ? 0.33190 0.31460 0.22780 0.06310  -0.00410 0.09380  177 LEU A CA  
1344 C C   . LEU A  183 ? 0.42180 0.37970 0.30840 0.06550  -0.00480 0.10220  177 LEU A C   
1345 O O   . LEU A  183 ? 0.40440 0.35610 0.30260 0.07510  -0.00660 0.10190  177 LEU A O   
1346 C CB  . LEU A  183 ? 0.39080 0.38100 0.29650 0.05520  0.00560  0.08320  177 LEU A CB  
1347 C CG  . LEU A  183 ? 0.35130 0.36320 0.26670 0.05070  0.00700  0.07340  177 LEU A CG  
1348 C CD1 . LEU A  183 ? 0.28830 0.30490 0.21950 0.04690  0.01380  0.06350  177 LEU A CD1 
1349 C CD2 . LEU A  183 ? 0.38590 0.40210 0.28290 0.04130  0.00800  0.07340  177 LEU A CD2 
1350 N N   . ASP A  184 ? 0.38740 0.33150 0.25340 0.05620  -0.00300 0.10910  178 ASP A N   
1351 C CA  . ASP A  184 ? 0.48210 0.40070 0.34100 0.05630  -0.00310 0.11640  178 ASP A CA  
1352 C C   . ASP A  184 ? 0.44210 0.35850 0.31240 0.05220  0.00620  0.10770  178 ASP A C   
1353 O O   . ASP A  184 ? 0.40160 0.33380 0.27960 0.04570  0.01340  0.09800  178 ASP A O   
1354 C CB  . ASP A  184 ? 0.48980 0.39330 0.32270 0.04590  -0.00410 0.12800  178 ASP A CB  
1355 C CG  . ASP A  184 ? 0.62290 0.52660 0.44220 0.05030  -0.01520 0.13770  178 ASP A CG  
1356 O OD1 . ASP A  184 ? 0.66600 0.56560 0.49440 0.06390  -0.02530 0.14090  178 ASP A OD1 
1357 O OD2 . ASP A  184 ? 0.64550 0.55520 0.44570 0.04020  -0.01410 0.14120  178 ASP A OD2 
1358 N N   . ALA A  185 ? 0.40580 0.30220 0.27860 0.05690  0.00490  0.11030  179 ALA A N   
1359 C CA  . ALA A  185 ? 0.43160 0.32190 0.31350 0.05350  0.01190  0.10300  179 ALA A CA  
1360 C C   . ALA A  185 ? 0.43200 0.32790 0.30880 0.03820  0.02120  0.09900  179 ALA A C   
1361 O O   . ALA A  185 ? 0.43260 0.33950 0.32260 0.03530  0.02710  0.08840  179 ALA A O   
1362 C CB  . ALA A  185 ? 0.40670 0.26900 0.28480 0.05720  0.00800  0.10910  179 ALA A CB  
1363 N N   . GLY A  186 ? 0.42930 0.31920 0.28730 0.02810  0.02210  0.10750  180 GLY A N   
1364 C CA  . GLY A  186 ? 0.46870 0.36400 0.32160 0.01260  0.03200  0.10380  180 GLY A CA  
1365 C C   . GLY A  186 ? 0.47340 0.39620 0.33400 0.00860  0.03720  0.09250  180 GLY A C   
1366 O O   . GLY A  186 ? 0.49140 0.42210 0.35390 -0.00280 0.04610  0.08570  180 GLY A O   
1367 N N   . ASP A  187 ? 0.43180 0.36950 0.29880 0.01750  0.03180  0.08960  181 ASP A N   
1368 C CA  . ASP A  187 ? 0.40940 0.37170 0.28570 0.01440  0.03520  0.07830  181 ASP A CA  
1369 C C   . ASP A  187 ? 0.35910 0.33160 0.25950 0.02080  0.03530  0.06760  181 ASP A C   
1370 O O   . ASP A  187 ? 0.37490 0.36620 0.28620 0.01990  0.03590  0.05850  181 ASP A O   
1371 C CB  . ASP A  187 ? 0.39540 0.36880 0.26330 0.01790  0.02880  0.08140  181 ASP A CB  
1372 C CG  . ASP A  187 ? 0.47920 0.44530 0.32030 0.00980  0.02850  0.09170  181 ASP A CG  
1373 O OD1 . ASP A  187 ? 0.54950 0.51070 0.38050 -0.00230 0.03670  0.09240  181 ASP A OD1 
1374 O OD2 . ASP A  187 ? 0.60880 0.57440 0.43890 0.01510  0.01990  0.09940  181 ASP A OD2 
1375 N N   . VAL A  188 ? 0.33740 0.29780 0.24600 0.02700  0.03400  0.06850  182 VAL A N   
1376 C CA  . VAL A  188 ? 0.31870 0.28650 0.24680 0.03070  0.03490  0.05930  182 VAL A CA  
1377 C C   . VAL A  188 ? 0.33200 0.29070 0.26310 0.02350  0.04070  0.05490  182 VAL A C   
1378 O O   . VAL A  188 ? 0.34280 0.28280 0.26490 0.02250  0.04110  0.06090  182 VAL A O   
1379 C CB  . VAL A  188 ? 0.29840 0.26240 0.23310 0.04340  0.02920  0.06220  182 VAL A CB  
1380 C CG1 . VAL A  188 ? 0.29620 0.26680 0.24750 0.04580  0.03020  0.05400  182 VAL A CG1 
1381 C CG2 . VAL A  188 ? 0.36690 0.34180 0.30160 0.05030  0.02310  0.06620  182 VAL A CG2 
1382 N N   . GLU A  189 ? 0.27500 0.24610 0.21990 0.01850  0.04430  0.04420  183 GLU A N   
1383 C CA  . GLU A  189 ? 0.29500 0.25930 0.24580 0.01200  0.04890  0.03880  183 GLU A CA  
1384 C C   . GLU A  189 ? 0.27140 0.23440 0.23580 0.01900  0.04530  0.03400  183 GLU A C   
1385 O O   . GLU A  189 ? 0.28090 0.25280 0.25240 0.02640  0.04080  0.03320  183 GLU A O   
1386 C CB  . GLU A  189 ? 0.30720 0.28610 0.26500 0.00110  0.05520  0.02940  183 GLU A CB  
1387 C CG  . GLU A  189 ? 0.32450 0.30460 0.26480 -0.00710 0.05990  0.03460  183 GLU A CG  
1388 C CD  . GLU A  189 ? 0.47450 0.47410 0.42130 -0.01660 0.06650  0.02370  183 GLU A CD  
1389 O OE1 . GLU A  189 ? 0.44380 0.45340 0.41090 -0.01770 0.06770  0.01170  183 GLU A OE1 
1390 O OE2 . GLU A  189 ? 0.51170 0.51720 0.44330 -0.02280 0.07010  0.02660  183 GLU A OE2 
1391 N N   . TRP A  190 ? 0.27620 0.22790 0.24350 0.01620  0.04700  0.03120  184 TRP A N   
1392 C CA  . TRP A  190 ? 0.32820 0.27690 0.30400 0.02320  0.04290  0.02760  184 TRP A CA  
1393 C C   . TRP A  190 ? 0.26100 0.21110 0.24880 0.01670  0.04450  0.01820  184 TRP A C   
1394 O O   . TRP A  190 ? 0.26620 0.20910 0.25240 0.00830  0.04880  0.01690  184 TRP A O   
1395 C CB  . TRP A  190 ? 0.32790 0.25830 0.29410 0.03040  0.04060  0.03350  184 TRP A CB  
1396 C CG  . TRP A  190 ? 0.32250 0.25320 0.28050 0.03870  0.03760  0.04180  184 TRP A CG  
1397 C CD1 . TRP A  190 ? 0.31620 0.24140 0.26230 0.03700  0.03770  0.04990  184 TRP A CD1 
1398 C CD2 . TRP A  190 ? 0.30560 0.24430 0.26740 0.04920  0.03370  0.04260  184 TRP A CD2 
1399 N NE1 . TRP A  190 ? 0.33240 0.26130 0.27620 0.04660  0.03320  0.05510  184 TRP A NE1 
1400 C CE2 . TRP A  190 ? 0.32800 0.26610 0.28230 0.05400  0.03140  0.05030  184 TRP A CE2 
1401 C CE3 . TRP A  190 ? 0.32350 0.27040 0.29390 0.05420  0.03200  0.03790  184 TRP A CE3 
1402 C CZ2 . TRP A  190 ? 0.31560 0.26240 0.27360 0.06400  0.02790  0.05240  184 TRP A CZ2 
1403 C CZ3 . TRP A  190 ? 0.31000 0.26550 0.28200 0.06320  0.02950  0.04080  184 TRP A CZ3 
1404 C CH2 . TRP A  190 ? 0.30820 0.26420 0.27540 0.06810  0.02770  0.04740  184 TRP A CH2 
1405 N N   . GLY A  191 ? 0.23700 0.19640 0.23720 0.01990  0.04040  0.01210  185 GLY A N   
1406 C CA  . GLY A  191 ? 0.25680 0.21510 0.26830 0.01610  0.03920  0.00370  185 GLY A CA  
1407 C C   . GLY A  191 ? 0.29170 0.24500 0.30270 0.02400  0.03340  0.00360  185 GLY A C   
1408 O O   . GLY A  191 ? 0.28490 0.23330 0.28580 0.03160  0.03230  0.00970  185 GLY A O   
1409 N N   . THR A  192 ? 0.25150 0.20760 0.27350 0.02230  0.02930  -0.00370 186 THR A N   
1410 C CA  . THR A  192 ? 0.28690 0.23910 0.30650 0.02830  0.02360  -0.00450 186 THR A CA  
1411 C C   . THR A  192 ? 0.24400 0.20880 0.27270 0.03020  0.01740  -0.00530 186 THR A C   
1412 O O   . THR A  192 ? 0.23170 0.20450 0.27540 0.02550  0.01470  -0.01110 186 THR A O   
1413 C CB  . THR A  192 ? 0.33310 0.27560 0.35600 0.02460  0.02200  -0.01170 186 THR A CB  
1414 O OG1 . THR A  192 ? 0.35510 0.28340 0.36950 0.02250  0.02710  -0.00970 186 THR A OG1 
1415 C CG2 . THR A  192 ? 0.28980 0.22930 0.30820 0.03040  0.01550  -0.01340 186 THR A CG2 
1416 N N   . ASP A  193 ? 0.27100 0.23770 0.29190 0.03680  0.01470  0.00030  187 ASP A N   
1417 C CA  . ASP A  193 ? 0.24930 0.22660 0.27710 0.03780  0.00870  0.00240  187 ASP A CA  
1418 C C   . ASP A  193 ? 0.26870 0.24400 0.30050 0.03660  0.00100  -0.00200 187 ASP A C   
1419 O O   . ASP A  193 ? 0.25760 0.22410 0.28580 0.03590  0.00050  -0.00710 187 ASP A O   
1420 C CB  . ASP A  193 ? 0.27710 0.25860 0.29480 0.04400  0.00970  0.01070  187 ASP A CB  
1421 C CG  . ASP A  193 ? 0.26260 0.25620 0.28860 0.04340  0.00830  0.01530  187 ASP A CG  
1422 O OD1 . ASP A  193 ? 0.31520 0.31340 0.35490 0.03910  0.00420  0.01150  187 ASP A OD1 
1423 O OD2 . ASP A  193 ? 0.30850 0.30750 0.32920 0.04750  0.01080  0.02170  187 ASP A OD2 
1424 N N   . GLY A  194 ? 0.22810 0.21070 0.26680 0.03640  -0.00620 0.00070  188 GLY A N   
1425 C CA  . GLY A  194 ? 0.23260 0.21280 0.27250 0.03570  -0.01530 -0.00120 188 GLY A CA  
1426 C C   . GLY A  194 ? 0.24070 0.21580 0.26140 0.03950  -0.01510 0.00170  188 GLY A C   
1427 O O   . GLY A  194 ? 0.24660 0.21690 0.26420 0.03880  -0.02130 -0.00220 188 GLY A O   
1428 N N   . CYS A  195 ? 0.25110 0.22860 0.25950 0.04390  -0.00830 0.00750  189 CYS A N   
1429 C CA  . CYS A  195 ? 0.26320 0.23820 0.25390 0.04830  -0.00620 0.00830  189 CYS A CA  
1430 C C   . CYS A  195 ? 0.25640 0.22050 0.24100 0.05100  -0.00090 0.00150  189 CYS A C   
1431 O O   . CYS A  195 ? 0.30220 0.26370 0.27320 0.05580  0.00160  -0.00010 189 CYS A O   
1432 C CB  . CYS A  195 ? 0.27920 0.26390 0.26290 0.05210  -0.00110 0.01640  189 CYS A CB  
1433 S SG  . CYS A  195 ? 0.27080 0.25480 0.25810 0.05550  0.00760  0.01710  189 CYS A SG  
1434 N N   . ASN A  196 ? 0.24160 0.19970 0.23600 0.04770  0.00140  -0.00240 190 ASN A N   
1435 C CA  . ASN A  196 ? 0.27300 0.21830 0.26460 0.04780  0.00520  -0.00820 190 ASN A CA  
1436 C C   . ASN A  196 ? 0.31350 0.25450 0.29690 0.05320  0.01240  -0.00430 190 ASN A C   
1437 O O   . ASN A  196 ? 0.30210 0.23000 0.28080 0.05480  0.01460  -0.00820 190 ASN A O   
1438 C CB  . ASN A  196 ? 0.30420 0.24150 0.28860 0.04880  0.00080  -0.01550 190 ASN A CB  
1439 C CG  . ASN A  196 ? 0.28610 0.21030 0.27610 0.04470  0.00130  -0.02320 190 ASN A CG  
1440 O OD1 . ASN A  196 ? 0.30080 0.22520 0.30340 0.03840  0.00290  -0.02420 190 ASN A OD1 
1441 N ND2 . ASN A  196 ? 0.31220 0.22600 0.29320 0.04780  0.00040  -0.02920 190 ASN A ND2 
1442 N N   . LEU A  197 ? 0.25250 0.20340 0.23570 0.05620  0.01520  0.00310  191 LEU A N   
1443 C CA  . LEU A  197 ? 0.28010 0.22790 0.25900 0.06090  0.02050  0.00730  191 LEU A CA  
1444 C C   . LEU A  197 ? 0.30300 0.24870 0.28820 0.05550  0.02280  0.00960  191 LEU A C   
1445 O O   . LEU A  197 ? 0.27040 0.22340 0.26510 0.04930  0.02120  0.00880  191 LEU A O   
1446 C CB  . LEU A  197 ? 0.22670 0.18820 0.20380 0.06630  0.02180  0.01350  191 LEU A CB  
1447 C CG  . LEU A  197 ? 0.25700 0.22220 0.22520 0.07260  0.02250  0.01170  191 LEU A CG  
1448 C CD1 . LEU A  197 ? 0.27430 0.25660 0.24380 0.07490  0.02390  0.01820  191 LEU A CD1 
1449 C CD2 . LEU A  197 ? 0.23970 0.19300 0.20180 0.07990  0.02560  0.00780  191 LEU A CD2 
1450 N N   . PRO A  198 ? 0.27270 0.20930 0.25270 0.05790  0.02610  0.01270  192 PRO A N   
1451 C CA  . PRO A  198 ? 0.26130 0.19940 0.24350 0.05310  0.02860  0.01720  192 PRO A CA  
1452 C C   . PRO A  198 ? 0.27370 0.22880 0.26080 0.05420  0.02770  0.02120  192 PRO A C   
1453 O O   . PRO A  198 ? 0.26110 0.22410 0.24730 0.06040  0.02650  0.02380  192 PRO A O   
1454 C CB  . PRO A  198 ? 0.32240 0.24740 0.29550 0.05770  0.03030  0.02190  192 PRO A CB  
1455 C CG  . PRO A  198 ? 0.32500 0.23770 0.29380 0.06340  0.02900  0.01720  192 PRO A CG  
1456 C CD  . PRO A  198 ? 0.30500 0.22990 0.27650 0.06560  0.02700  0.01240  192 PRO A CD  
1457 N N   . THR A  199 ? 0.25710 0.21870 0.25030 0.04750  0.02850  0.02100  193 THR A N   
1458 C CA  . THR A  199 ? 0.26580 0.24290 0.26620 0.04750  0.02660  0.02300  193 THR A CA  
1459 C C   . THR A  199 ? 0.26290 0.24260 0.26220 0.04310  0.02930  0.02450  193 THR A C   
1460 O O   . THR A  199 ? 0.29130 0.26510 0.28930 0.03640  0.03270  0.02140  193 THR A O   
1461 C CB  . THR A  199 ? 0.25160 0.23700 0.26460 0.04380  0.02240  0.01800  193 THR A CB  
1462 O OG1 . THR A  199 ? 0.29940 0.29790 0.31960 0.04470  0.01940  0.02090  193 THR A OG1 
1463 C CG2 . THR A  199 ? 0.25940 0.24400 0.28100 0.03590  0.02320  0.01040  193 THR A CG2 
1464 N N   . PRO A  200 ? 0.23750 0.22580 0.23580 0.04620  0.02830  0.02920  194 PRO A N   
1465 C CA  . PRO A  200 ? 0.23190 0.22110 0.22400 0.04300  0.03050  0.03160  194 PRO A CA  
1466 C C   . PRO A  200 ? 0.25080 0.25390 0.25210 0.03720  0.03020  0.02640  194 PRO A C   
1467 O O   . PRO A  200 ? 0.19280 0.20650 0.20680 0.03800  0.02640  0.02320  194 PRO A O   
1468 C CB  . PRO A  200 ? 0.25880 0.24960 0.24510 0.05100  0.02820  0.03920  194 PRO A CB  
1469 C CG  . PRO A  200 ? 0.28170 0.28380 0.27890 0.05510  0.02500  0.03830  194 PRO A CG  
1470 C CD  . PRO A  200 ? 0.22500 0.22100 0.22500 0.05360  0.02550  0.03370  194 PRO A CD  
1471 N N   . ALA A  201 ? 0.22160 0.22480 0.21570 0.03150  0.03390  0.02600  195 ALA A N   
1472 C CA  . ALA A  201 ? 0.23370 0.25120 0.23390 0.02660  0.03420  0.02010  195 ALA A CA  
1473 C C   . ALA A  201 ? 0.26810 0.28690 0.25370 0.02680  0.03460  0.02620  195 ALA A C   
1474 O O   . ALA A  201 ? 0.25590 0.26290 0.22570 0.02530  0.03740  0.03290  195 ALA A O   
1475 C CB  . ALA A  201 ? 0.23390 0.25450 0.24000 0.01760  0.03940  0.01070  195 ALA A CB  
1476 N N   . PHE A  202 ? 0.22520 0.25760 0.21620 0.02810  0.03100  0.02390  196 PHE A N   
1477 C CA  . PHE A  202 ? 0.25730 0.29310 0.23490 0.02840  0.02980  0.02870  196 PHE A CA  
1478 C C   . PHE A  202 ? 0.24160 0.29490 0.22970 0.02620  0.02720  0.01980  196 PHE A C   
1479 O O   . PHE A  202 ? 0.23540 0.29600 0.24220 0.02530  0.02580  0.01110  196 PHE A O   
1480 C CB  . PHE A  202 ? 0.20760 0.23720 0.17910 0.03750  0.02460  0.03930  196 PHE A CB  
1481 C CG  . PHE A  202 ? 0.25380 0.28770 0.24080 0.04420  0.02080  0.03920  196 PHE A CG  
1482 C CD1 . PHE A  202 ? 0.21770 0.26580 0.21750 0.04580  0.01600  0.03650  196 PHE A CD1 
1483 C CD2 . PHE A  202 ? 0.24550 0.26900 0.23330 0.04830  0.02190  0.04210  196 PHE A CD2 
1484 C CE1 . PHE A  202 ? 0.20760 0.26010 0.22070 0.05010  0.01310  0.03770  196 PHE A CE1 
1485 C CE2 . PHE A  202 ? 0.21660 0.24560 0.21610 0.05350  0.01930  0.04260  196 PHE A CE2 
1486 C CZ  . PHE A  202 ? 0.22950 0.27320 0.24150 0.05390  0.01510  0.04110  196 PHE A CZ  
1487 N N   . PRO A  203 ? 0.23240 0.29210 0.20870 0.02470  0.02610  0.02090  197 PRO A N   
1488 C CA  . PRO A  203 ? 0.20350 0.28000 0.19010 0.02270  0.02320  0.01050  197 PRO A CA  
1489 C C   . PRO A  203 ? 0.19110 0.27360 0.19820 0.02880  0.01560  0.00940  197 PRO A C   
1490 O O   . PRO A  203 ? 0.19430 0.27210 0.20180 0.03520  0.01180  0.01860  197 PRO A O   
1491 C CB  . PRO A  203 ? 0.25560 0.33540 0.22220 0.02190  0.02150  0.01510  197 PRO A CB  
1492 C CG  . PRO A  203 ? 0.26540 0.33100 0.21030 0.01780  0.02750  0.02380  197 PRO A CG  
1493 C CD  . PRO A  203 ? 0.26930 0.32070 0.22110 0.02300  0.02750  0.03020  197 PRO A CD  
1494 N N   . LEU A  204 ? 0.20160 0.29480 0.22720 0.02630  0.01350  -0.00250 198 LEU A N   
1495 C CA  . LEU A  204 ? 0.19010 0.28710 0.23660 0.03010  0.00600  -0.00310 198 LEU A CA  
1496 C C   . LEU A  204 ? 0.19880 0.30070 0.24400 0.03490  -0.00020 0.00400  198 LEU A C   
1497 O O   . LEU A  204 ? 0.17990 0.28070 0.23460 0.03900  -0.00400 0.01090  198 LEU A O   
1498 C CB  . LEU A  204 ? 0.16700 0.27390 0.23360 0.02660  0.00320  -0.01780 198 LEU A CB  
1499 C CG  . LEU A  204 ? 0.17160 0.28030 0.26180 0.02880  -0.00540 -0.01860 198 LEU A CG  
1500 C CD1 . LEU A  204 ? 0.18720 0.28510 0.28060 0.03040  -0.00490 -0.01080 198 LEU A CD1 
1501 C CD2 . LEU A  204 ? 0.13500 0.25190 0.24500 0.02570  -0.00890 -0.03470 198 LEU A CD2 
1502 N N   . ASP A  205 ? 0.18360 0.29190 0.21680 0.03410  -0.00140 0.00260  199 ASP A N   
1503 C CA  . ASP A  205 ? 0.19050 0.30460 0.22440 0.03870  -0.00850 0.00850  199 ASP A CA  
1504 C C   . ASP A  205 ? 0.23470 0.34040 0.26200 0.04510  -0.00840 0.02210  199 ASP A C   
1505 O O   . ASP A  205 ? 0.21530 0.32670 0.25310 0.04960  -0.01370 0.02680  199 ASP A O   
1506 C CB  . ASP A  205 ? 0.19580 0.31700 0.21400 0.03680  -0.01030 0.00510  199 ASP A CB  
1507 C CG  . ASP A  205 ? 0.26070 0.37210 0.25190 0.03570  -0.00490 0.01290  199 ASP A CG  
1508 O OD1 . ASP A  205 ? 0.24840 0.35350 0.23250 0.03060  0.00320  0.01020  199 ASP A OD1 
1509 O OD2 . ASP A  205 ? 0.23490 0.34460 0.21320 0.03970  -0.00950 0.02170  199 ASP A OD2 
1510 N N   . ARG A  206 ? 0.21270 0.30570 0.22430 0.04540  -0.00240 0.02770  200 ARG A N   
1511 C CA  . ARG A  206 ? 0.24780 0.33200 0.25420 0.05220  -0.00240 0.03850  200 ARG A CA  
1512 C C   . ARG A  206 ? 0.19300 0.27760 0.21570 0.05500  -0.00200 0.03980  200 ARG A C   
1513 O O   . ARG A  206 ? 0.23990 0.32390 0.26430 0.06140  -0.00300 0.04670  200 ARG A O   
1514 C CB  . ARG A  206 ? 0.25090 0.31960 0.23780 0.05110  0.00330  0.04310  200 ARG A CB  
1515 C CG  . ARG A  206 ? 0.27510 0.34260 0.24230 0.04630  0.00370  0.04350  200 ARG A CG  
1516 C CD  . ARG A  206 ? 0.29700 0.36930 0.25720 0.05170  -0.00460 0.04980  200 ARG A CD  
1517 N NE  . ARG A  206 ? 0.37730 0.44970 0.31630 0.04640  -0.00520 0.05040  200 ARG A NE  
1518 C CZ  . ARG A  206 ? 0.38200 0.44400 0.30060 0.04830  -0.00850 0.06080  200 ARG A CZ  
1519 N NH1 . ARG A  206 ? 0.37140 0.42220 0.29030 0.05660  -0.01220 0.07050  200 ARG A NH1 
1520 N NH2 . ARG A  206 ? 0.42470 0.48810 0.32210 0.04160  -0.00860 0.06130  200 ARG A NH2 
1521 N N   . LEU A  207 ? 0.17210 0.25760 0.20640 0.05030  -0.00040 0.03330  201 LEU A N   
1522 C CA  . LEU A  207 ? 0.15440 0.24130 0.20290 0.05190  -0.00150 0.03560  201 LEU A CA  
1523 C C   . LEU A  207 ? 0.19230 0.29230 0.25530 0.05330  -0.00760 0.03740  201 LEU A C   
1524 O O   . LEU A  207 ? 0.16570 0.26900 0.23370 0.05710  -0.00780 0.04390  201 LEU A O   
1525 C CB  . LEU A  207 ? 0.23520 0.31910 0.29340 0.04650  -0.00070 0.02870  201 LEU A CB  
1526 C CG  . LEU A  207 ? 0.22140 0.30520 0.29170 0.04680  -0.00270 0.03200  201 LEU A CG  
1527 C CD1 . LEU A  207 ? 0.24200 0.31880 0.30160 0.05170  0.00180  0.03970  201 LEU A CD1 
1528 C CD2 . LEU A  207 ? 0.16850 0.24880 0.25010 0.04180  -0.00470 0.02510  201 LEU A CD2 
1529 N N   . GLY A  208 ? 0.18060 0.28910 0.25040 0.05010  -0.01240 0.03110  202 GLY A N   
1530 C CA  . GLY A  208 ? 0.18540 0.30630 0.26950 0.05100  -0.01900 0.03250  202 GLY A CA  
1531 C C   . GLY A  208 ? 0.22730 0.35250 0.30460 0.05730  -0.02000 0.03980  202 GLY A C   
1532 O O   . GLY A  208 ? 0.24970 0.38480 0.34010 0.05930  -0.02320 0.04400  202 GLY A O   
1533 N N   . ARG A  209 ? 0.18870 0.30630 0.24660 0.06040  -0.01760 0.04190  203 ARG A N   
1534 C CA  . ARG A  209 ? 0.23060 0.35040 0.28280 0.06760  -0.02010 0.04890  203 ARG A CA  
1535 C C   . ARG A  209 ? 0.21780 0.33690 0.27590 0.07310  -0.01650 0.05500  203 ARG A C   
1536 O O   . ARG A  209 ? 0.19310 0.32290 0.26120 0.07810  -0.01960 0.05860  203 ARG A O   
1537 C CB  . ARG A  209 ? 0.22500 0.33350 0.25400 0.06890  -0.01910 0.05100  203 ARG A CB  
1538 C CG  . ARG A  209 ? 0.22680 0.33550 0.24950 0.07680  -0.02420 0.05810  203 ARG A CG  
1539 C CD  . ARG A  209 ? 0.26360 0.35790 0.26160 0.07700  -0.02420 0.06240  203 ARG A CD  
1540 N NE  . ARG A  209 ? 0.31180 0.40880 0.29760 0.07000  -0.02590 0.05780  203 ARG A NE  
1541 C CZ  . ARG A  209 ? 0.32380 0.41600 0.28930 0.06990  -0.03020 0.06230  203 ARG A CZ  
1542 N NH1 . ARG A  209 ? 0.30860 0.39150 0.26540 0.07720  -0.03490 0.07200  203 ARG A NH1 
1543 N NH2 . ARG A  209 ? 0.29260 0.38940 0.24610 0.06240  -0.03020 0.05660  203 ARG A NH2 
1544 N N   . ILE A  210 ? 0.20880 0.31690 0.26180 0.07210  -0.01010 0.05530  204 ILE A N   
1545 C CA  . ILE A  210 ? 0.21870 0.32690 0.27570 0.07690  -0.00610 0.05950  204 ILE A CA  
1546 C C   . ILE A  210 ? 0.19370 0.31800 0.26990 0.07530  -0.00760 0.06080  204 ILE A C   
1547 O O   . ILE A  210 ? 0.20900 0.34340 0.29260 0.08060  -0.00690 0.06420  204 ILE A O   
1548 C CB  . ILE A  210 ? 0.23070 0.32530 0.27960 0.07450  -0.00010 0.05800  204 ILE A CB  
1549 C CG1 . ILE A  210 ? 0.25240 0.33100 0.28310 0.07660  0.00200  0.05840  204 ILE A CG1 
1550 C CG2 . ILE A  210 ? 0.22420 0.32160 0.27750 0.07820  0.00400  0.06080  204 ILE A CG2 
1551 C CD1 . ILE A  210 ? 0.25910 0.32460 0.28310 0.07290  0.00710  0.05570  204 ILE A CD1 
1552 N N   . TYR A  211 ? 0.21070 0.33830 0.29680 0.06760  -0.01000 0.05780  205 TYR A N   
1553 C CA  . TYR A  211 ? 0.18030 0.32080 0.28450 0.06400  -0.01180 0.06040  205 TYR A CA  
1554 C C   . TYR A  211 ? 0.16310 0.31910 0.28030 0.06530  -0.01750 0.06100  205 TYR A C   
1555 O O   . TYR A  211 ? 0.18510 0.35380 0.31590 0.06450  -0.01710 0.06490  205 TYR A O   
1556 C CB  . TYR A  211 ? 0.17250 0.30830 0.28400 0.05570  -0.01420 0.05740  205 TYR A CB  
1557 C CG  . TYR A  211 ? 0.20720 0.33250 0.31060 0.05490  -0.00910 0.05910  205 TYR A CG  
1558 C CD1 . TYR A  211 ? 0.19840 0.31010 0.28540 0.05760  -0.00490 0.05600  205 TYR A CD1 
1559 C CD2 . TYR A  211 ? 0.17130 0.30000 0.28230 0.05080  -0.00870 0.06430  205 TYR A CD2 
1560 C CE1 . TYR A  211 ? 0.17040 0.27260 0.25040 0.05690  -0.00110 0.05670  205 TYR A CE1 
1561 C CE2 . TYR A  211 ? 0.17800 0.29710 0.27960 0.05000  -0.00490 0.06560  205 TYR A CE2 
1562 C CZ  . TYR A  211 ? 0.18030 0.28640 0.26710 0.05350  -0.00140 0.06120  205 TYR A CZ  
1563 O OH  . TYR A  211 ? 0.19170 0.28920 0.27030 0.05270  0.00130  0.06190  205 TYR A OH  
1564 N N   . ALA A  212 ? 0.16030 0.31590 0.27260 0.06670  -0.02260 0.05710  206 ALA A N   
1565 C CA  . ALA A  212 ? 0.19530 0.36570 0.31900 0.06900  -0.02910 0.05740  206 ALA A CA  
1566 C C   . ALA A  212 ? 0.23030 0.40320 0.35120 0.07630  -0.02660 0.06100  206 ALA A C   
1567 O O   . ALA A  212 ? 0.18710 0.37110 0.32110 0.07600  -0.02900 0.06070  206 ALA A O   
1568 C CB  . ALA A  212 ? 0.20030 0.36850 0.31530 0.06840  -0.03550 0.05170  206 ALA A CB  
1569 N N   . LYS A  213 ? 0.19930 0.36100 0.30450 0.08280  -0.02200 0.06340  207 LYS A N   
1570 C CA  . LYS A  213 ? 0.19730 0.35870 0.30060 0.09010  -0.01980 0.06500  207 LYS A CA  
1571 C C   . LYS A  213 ? 0.21330 0.38300 0.32720 0.08890  -0.01280 0.06590  207 LYS A C   
1572 O O   . LYS A  213 ? 0.22190 0.40130 0.34460 0.09300  -0.01210 0.06530  207 LYS A O   
1573 C CB  . LYS A  213 ? 0.18780 0.33240 0.27180 0.09680  -0.01780 0.06700  207 LYS A CB  
1574 C CG  . LYS A  213 ? 0.25250 0.39060 0.32350 0.09960  -0.02500 0.06850  207 LYS A CG  
1575 C CD  . LYS A  213 ? 0.28510 0.40230 0.33570 0.10340  -0.02240 0.07110  207 LYS A CD  
1576 C CE  . LYS A  213 ? 0.26790 0.37660 0.30260 0.10470  -0.02970 0.07390  207 LYS A CE  
1577 N NZ  . LYS A  213 ? 0.32290 0.40980 0.33880 0.10750  -0.02760 0.07790  207 LYS A NZ  
1578 N N   . LEU A  214 ? 0.19790 0.36510 0.31100 0.08390  -0.00770 0.06730  208 LEU A N   
1579 C CA  . LEU A  214 ? 0.22000 0.39860 0.34280 0.08130  -0.00160 0.06990  208 LEU A CA  
1580 C C   . LEU A  214 ? 0.18100 0.37690 0.32280 0.07580  -0.00460 0.07060  208 LEU A C   
1581 O O   . LEU A  214 ? 0.20570 0.41600 0.35710 0.07730  -0.00050 0.07160  208 LEU A O   
1582 C CB  . LEU A  214 ? 0.18500 0.35780 0.30440 0.07570  0.00150  0.07260  208 LEU A CB  
1583 C CG  . LEU A  214 ? 0.22070 0.37750 0.32210 0.07970  0.00700  0.07120  208 LEU A CG  
1584 C CD1 . LEU A  214 ? 0.19480 0.34060 0.29080 0.07160  0.00740  0.07130  208 LEU A CD1 
1585 C CD2 . LEU A  214 ? 0.25990 0.42530 0.36110 0.08620  0.01430  0.07170  208 LEU A CD2 
1586 N N   . ALA A  215 ? 0.20020 0.39590 0.34890 0.06930  -0.01160 0.06930  209 ALA A N   
1587 C CA  . ALA A  215 ? 0.19880 0.40920 0.36660 0.06290  -0.01490 0.07000  209 ALA A CA  
1588 C C   . ALA A  215 ? 0.21660 0.43640 0.39180 0.06800  -0.01910 0.06640  209 ALA A C   
1589 O O   . ALA A  215 ? 0.20730 0.44290 0.39910 0.06520  -0.01870 0.06700  209 ALA A O   
1590 C CB  . ALA A  215 ? 0.16650 0.37220 0.34060 0.05480  -0.02220 0.06800  209 ALA A CB  
1591 N N   . SER A  216 ? 0.16810 0.37870 0.33170 0.07500  -0.02360 0.06320  210 SER A N   
1592 C CA  . SER A  216 ? 0.20730 0.42530 0.37710 0.08090  -0.02910 0.06040  210 SER A CA  
1593 C C   . SER A  216 ? 0.22520 0.45110 0.39980 0.08740  -0.02280 0.06100  210 SER A C   
1594 O O   . SER A  216 ? 0.19090 0.43190 0.38220 0.08870  -0.02470 0.05890  210 SER A O   
1595 C CB  . SER A  216 ? 0.20460 0.41010 0.35840 0.08650  -0.03580 0.05920  210 SER A CB  
1596 O OG  . SER A  216 ? 0.21630 0.42730 0.37540 0.09270  -0.04270 0.05760  210 SER A OG  
1597 N N   . ALA A  217 ? 0.20380 0.42140 0.36610 0.09130  -0.01510 0.06280  211 ALA A N   
1598 C CA  . ALA A  217 ? 0.24840 0.47480 0.41590 0.09780  -0.00840 0.06160  211 ALA A CA  
1599 C C   . ALA A  217 ? 0.24680 0.49490 0.43230 0.09150  -0.00220 0.06290  211 ALA A C   
1600 O O   . ALA A  217 ? 0.26840 0.53230 0.46820 0.09530  -0.00030 0.05990  211 ALA A O   
1601 C CB  . ALA A  217 ? 0.25260 0.46540 0.40310 0.10250  -0.00160 0.06230  211 ALA A CB  
1602 N N   . ALA A  218 ? 0.21440 0.46400 0.40020 0.08170  0.00090  0.06780  212 ALA A N   
1603 C CA  . ALA A  218 ? 0.21040 0.48030 0.41280 0.07350  0.00590  0.07140  212 ALA A CA  
1604 C C   . ALA A  218 ? 0.24750 0.53100 0.46970 0.07090  -0.00040 0.06850  212 ALA A C   
1605 O O   . ALA A  218 ? 0.27560 0.57920 0.51380 0.06950  0.00450  0.06810  212 ALA A O   
1606 C CB  . ALA A  218 ? 0.22270 0.48780 0.42250 0.06270  0.00660  0.07830  212 ALA A CB  
1607 N N   . ASP A  219 ? 0.19270 0.46660 0.41450 0.07050  -0.01100 0.06570  213 ASP A N   
1608 C CA  . ASP A  219 ? 0.23810 0.52410 0.47840 0.06870  -0.01860 0.06190  213 ASP A CA  
1609 C C   . ASP A  219 ? 0.29890 0.59560 0.54820 0.07850  -0.01890 0.05690  213 ASP A C   
1610 O O   . ASP A  219 ? 0.26830 0.58480 0.53890 0.07650  -0.01850 0.05470  213 ASP A O   
1611 C CB  . ASP A  219 ? 0.22720 0.49990 0.46130 0.06800  -0.03010 0.05860  213 ASP A CB  
1612 C CG  . ASP A  219 ? 0.23740 0.50620 0.47490 0.05680  -0.03260 0.06060  213 ASP A CG  
1613 O OD1 . ASP A  219 ? 0.25440 0.53200 0.50280 0.04820  -0.02760 0.06580  213 ASP A OD1 
1614 O OD2 . ASP A  219 ? 0.20380 0.46120 0.43400 0.05630  -0.04030 0.05700  213 ASP A OD2 
1615 N N   . GLY A  220 ? 0.32060 0.60420 0.55540 0.08900  -0.02020 0.05490  214 GLY A N   
1616 C CA  . GLY A  220 ? 0.37910 0.66990 0.62330 0.09930  -0.02240 0.05000  214 GLY A CA  
1617 C C   . GLY A  220 ? 0.44570 0.75470 0.70260 0.10090  -0.01130 0.04830  214 GLY A C   
1618 O O   . GLY A  220 ? 0.45100 0.77690 0.72850 0.10470  -0.01230 0.04340  214 GLY A O   
1619 N N   . SER A  221 ? 0.37160 0.67880 0.61730 0.09790  -0.00050 0.05190  215 SER A N   
1620 C CA  . SER A  221 ? 0.35190 0.67830 0.60720 0.09790  0.01160  0.05020  215 SER A CA  
1621 C C   . SER A  221 ? 0.37500 0.72550 0.65210 0.08730  0.01480  0.05190  215 SER A C   
1622 O O   . SER A  221 ? 0.37040 0.74200 0.66540 0.08890  0.02060  0.04720  215 SER A O   
1623 C CB  . SER A  221 ? 0.35920 0.67740 0.59510 0.09590  0.02110  0.05440  215 SER A CB  
1624 O OG  . SER A  221 ? 0.46700 0.80550 0.71020 0.09390  0.03330  0.05310  215 SER A OG  
1625 N N   . ASP A  222 ? 0.47240 0.81980 0.74940 0.07600  0.01110  0.05820  216 ASP A N   
1626 C CA  . ASP A  222 ? 0.49760 0.86500 0.79610 0.06500  0.01220  0.06040  216 ASP A CA  
1627 C C   . ASP A  222 ? 0.49830 0.87860 0.81900 0.06960  0.00480  0.05250  216 ASP A C   
1628 O O   . ASP A  222 ? 0.51390 0.91710 0.85670 0.06400  0.00910  0.05110  216 ASP A O   
1629 C CB  . ASP A  222 ? 0.49250 0.84870 0.78720 0.05360  0.00600  0.06720  216 ASP A CB  
1630 C CG  . ASP A  222 ? 0.51880 0.88870 0.82340 0.03910  0.01280  0.07550  216 ASP A CG  
1631 O OD1 . ASP A  222 ? 0.57020 0.93970 0.86300 0.03530  0.02210  0.08220  216 ASP A OD1 
1632 O OD2 . ASP A  222 ? 0.56510 0.94520 0.88870 0.03100  0.00820  0.07570  216 ASP A OD2 
1633 N N   . ALA A  223 ? 0.40110 0.76720 0.71660 0.07920  -0.00640 0.04770  217 ALA A N   
1634 C CA  . ALA A  223 ? 0.50760 0.88280 0.84280 0.08410  -0.01650 0.04080  217 ALA A CA  
1635 C C   . ALA A  223 ? 0.50940 0.89360 0.85600 0.09640  -0.01480 0.03410  217 ALA A C   
1636 O O   . ALA A  223 ? 0.53850 0.93100 0.90450 0.10140  -0.02370 0.02870  217 ALA A O   
1637 C CB  . ALA A  223 ? 0.38360 0.73840 0.70620 0.08700  -0.03090 0.04020  217 ALA A CB  
1638 N N   . GLY A  224 ? 0.34240 0.96220 0.95830 0.10920  -0.13160 0.02600  218 GLY A N   
1639 C CA  . GLY A  224 ? 0.36610 1.01560 1.00070 0.12900  -0.11810 0.03240  218 GLY A CA  
1640 C C   . GLY A  224 ? 0.56700 1.21100 1.18940 0.14410  -0.15370 0.04250  218 GLY A C   
1641 O O   . GLY A  224 ? 0.42300 1.09540 1.08750 0.15340  -0.17800 0.03800  218 GLY A O   
1642 N N   . GLU A  225 ? 0.84780 1.43800 1.43370 0.14790  -0.16690 0.04060  219 GLU A N   
1643 C CA  . GLU A  225 ? 0.89530 1.47230 1.44990 0.15950  -0.20350 0.05360  219 GLU A CA  
1644 C C   . GLU A  225 ? 0.91090 1.46950 1.45980 0.17810  -0.18790 0.05480  219 GLU A C   
1645 O O   . GLU A  225 ? 0.91320 1.46650 1.45430 0.18070  -0.14630 0.04790  219 GLU A O   
1646 C CB  . GLU A  225 ? 0.83860 1.38890 1.29830 0.15530  -0.22490 0.04840  219 GLU A CB  
1647 C CG  . GLU A  225 ? 0.81570 1.37560 1.27250 0.13710  -0.24510 0.04050  219 GLU A CG  
1648 C CD  . GLU A  225 ? 0.91750 1.44950 1.28250 0.13050  -0.24560 0.02960  219 GLU A CD  
1649 O OE1 . GLU A  225 ? 0.99300 1.50320 1.29820 0.14050  -0.22890 0.03300  219 GLU A OE1 
1650 O OE2 . GLU A  225 ? 0.92170 1.45430 1.27650 0.11480  -0.26000 0.01960  219 GLU A OE2 
1651 N N   . GLY A  226 ? 0.72990 1.27590 1.26930 0.18780  -0.21860 0.06950  220 GLY A N   
1652 C CA  . GLY A  226 ? 0.66880 1.19210 1.18430 0.20510  -0.21070 0.07310  220 GLY A CA  
1653 C C   . GLY A  226 ? 0.70580 1.20120 1.12410 0.20480  -0.18960 0.07530  220 GLY A C   
1654 O O   . GLY A  226 ? 0.76470 1.23250 1.12010 0.21080  -0.20770 0.08580  220 GLY A O   
1655 N N   . GLN A  227 ? 0.63840 1.13750 1.04540 0.19700  -0.15140 0.06580  221 GLN A N   
1656 C CA  . GLN A  227 ? 0.54680 1.02010 0.87530 0.19620  -0.13140 0.06670  221 GLN A CA  
1657 C C   . GLN A  227 ? 0.48130 0.92770 0.78870 0.20940  -0.11340 0.07540  221 GLN A C   
1658 O O   . GLN A  227 ? 0.47490 0.92410 0.82560 0.21390  -0.09350 0.07330  221 GLN A O   
1659 C CB  . GLN A  227 ? 0.46350 0.94450 0.79230 0.18310  -0.09990 0.05490  221 GLN A CB  
1660 C CG  . GLN A  227 ? 0.45290 0.93910 0.74840 0.16950  -0.11300 0.04720  221 GLN A CG  
1661 C CD  . GLN A  227 ? 0.37710 0.86290 0.66510 0.15660  -0.08230 0.03690  221 GLN A CD  
1662 O OE1 . GLN A  227 ? 0.34700 0.83180 0.66280 0.15540  -0.05320 0.03480  221 GLN A OE1 
1663 N NE2 . GLN A  227 ? 0.26610 0.74850 0.51400 0.14600  -0.08960 0.02980  221 GLN A NE2 
1664 N N   . SER A  228 ? 0.47100 0.88840 0.71130 0.21470  -0.11900 0.08380  222 SER A N   
1665 C CA  . SER A  228 ? 0.36670 0.75410 0.58230 0.22410  -0.09810 0.09080  222 SER A CA  
1666 C C   . SER A  228 ? 0.34580 0.72750 0.56870 0.21870  -0.06060 0.08140  222 SER A C   
1667 O O   . SER A  228 ? 0.30900 0.70350 0.53550 0.20760  -0.05010 0.07150  222 SER A O   
1668 C CB  . SER A  228 ? 0.38580 0.74170 0.52740 0.22760  -0.10330 0.09930  222 SER A CB  
1669 O OG  . SER A  228 ? 0.44720 0.80210 0.55550 0.21860  -0.09110 0.09100  222 SER A OG  
1670 N N   . THR A  229 ? 0.32640 0.68490 0.54970 0.22500  -0.04270 0.08370  223 THR A N   
1671 C CA  . THR A  229 ? 0.30470 0.64630 0.52220 0.21870  -0.01190 0.07480  223 THR A CA  
1672 C C   . THR A  229 ? 0.29780 0.61970 0.46570 0.21140  -0.00360 0.07230  223 THR A C   
1673 O O   . THR A  229 ? 0.30570 0.62230 0.47080 0.20170  0.01290  0.06310  223 THR A O   
1674 C CB  . THR A  229 ? 0.31210 0.62520 0.52740 0.22520  0.00110  0.07660  223 THR A CB  
1675 O OG1 . THR A  229 ? 0.32900 0.61580 0.50380 0.23020  -0.00560 0.08620  223 THR A OG1 
1676 C CG2 . THR A  229 ? 0.32380 0.65600 0.59480 0.23330  -0.00530 0.07660  223 THR A CG2 
1677 N N   . ARG A  230 ? 0.30650 0.61430 0.43580 0.21620  -0.01440 0.08030  224 ARG A N   
1678 C CA  . ARG A  230 ? 0.30950 0.59720 0.39940 0.21070  -0.00480 0.07700  224 ARG A CA  
1679 C C   . ARG A  230 ? 0.30230 0.61840 0.39800 0.20070  -0.01080 0.06790  224 ARG A C   
1680 O O   . ARG A  230 ? 0.28030 0.58570 0.36730 0.19130  0.00310  0.05900  224 ARG A O   
1681 C CB  . ARG A  230 ? 0.32410 0.58950 0.37280 0.21950  -0.01100 0.08790  224 ARG A CB  
1682 C CG  . ARG A  230 ? 0.31250 0.56270 0.32950 0.21560  -0.00210 0.08380  224 ARG A CG  
1683 C CD  . ARG A  230 ? 0.37500 0.58620 0.35360 0.22220  0.00530  0.09360  224 ARG A CD  
1684 N NE  . ARG A  230 ? 0.39100 0.57200 0.37950 0.22240  0.02170  0.09460  224 ARG A NE  
1685 C CZ  . ARG A  230 ? 0.42320 0.56960 0.39140 0.22660  0.03230  0.10210  224 ARG A CZ  
1686 N NH1 . ARG A  230 ? 0.47290 0.60640 0.40460 0.23640  0.03250  0.11290  224 ARG A NH1 
1687 N NH2 . ARG A  230 ? 0.41510 0.53560 0.39650 0.21950  0.04210  0.09900  224 ARG A NH2 
1688 N N   . CSO A  231 ? 0.29300 0.64180 0.40460 0.20050  -0.03420 0.06890  225 CSO A N   
1689 C CA  . CSO A  231 ? 0.33200 0.70340 0.45170 0.18450  -0.04170 0.05720  225 CSO A CA  
1690 C CB  . CSO A  231 ? 0.37810 0.77530 0.50860 0.18380  -0.07490 0.05880  225 CSO A CB  
1691 S SG  . CSO A  231 ? 0.49290 0.85450 0.54650 0.18190  -0.09490 0.06320  225 CSO A SG  
1692 C C   . CSO A  231 ? 0.29250 0.68130 0.45480 0.17660  -0.02330 0.04840  225 CSO A C   
1693 O O   . CSO A  231 ? 0.26820 0.65480 0.42550 0.16030  -0.01550 0.03780  225 CSO A O   
1694 O OD  . CSO A  231 ? 0.59000 0.97010 0.64600 0.18520  -0.14170 0.06760  225 CSO A OD  
1695 N N   . ALA A  232 ? 0.26140 0.65160 0.45820 0.18180  -0.01470 0.05110  226 ALA A N   
1696 C CA  . ALA A  232 ? 0.24320 0.63540 0.46860 0.17350  0.00830  0.04320  226 ALA A CA  
1697 C C   . ALA A  232 ? 0.23280 0.58930 0.42010 0.16710  0.02920  0.03840  226 ALA A C   
1698 O O   . ALA A  232 ? 0.22140 0.58030 0.41180 0.15420  0.04020  0.03020  226 ALA A O   
1699 C CB  . ALA A  232 ? 0.28030 0.67260 0.54230 0.18290  0.01710  0.04610  226 ALA A CB  
1700 N N   . ALA A  233 ? 0.25740 0.57780 0.41050 0.17520  0.03270  0.04360  227 ALA A N   
1701 C CA  . ALA A  233 ? 0.26250 0.54290 0.38310 0.16920  0.04630  0.03900  227 ALA A CA  
1702 C C   . ALA A  233 ? 0.26410 0.54650 0.36810 0.15920  0.04130  0.03310  227 ALA A C   
1703 O O   . ALA A  233 ? 0.25230 0.51430 0.34550 0.14940  0.05080  0.02580  227 ALA A O   
1704 C CB  . ALA A  233 ? 0.27640 0.51780 0.37230 0.17790  0.04760  0.04530  227 ALA A CB  
1705 N N   . LEU A  234 ? 0.26250 0.56060 0.35880 0.16020  0.02570  0.03530  228 LEU A N   
1706 C CA  . LEU A  234 ? 0.27490 0.56100 0.35100 0.14120  0.02110  0.02570  228 LEU A CA  
1707 C C   . LEU A  234 ? 0.23570 0.54550 0.33500 0.12430  0.02010  0.01590  228 LEU A C   
1708 O O   . LEU A  234 ? 0.22650 0.51770 0.31770 0.10860  0.02560  0.00710  228 LEU A O   
1709 C CB  . LEU A  234 ? 0.24140 0.53010 0.29470 0.14160  0.00570  0.02830  228 LEU A CB  
1710 C CG  . LEU A  234 ? 0.31990 0.57520 0.34310 0.15380  0.01140  0.03730  228 LEU A CG  
1711 C CD1 . LEU A  234 ? 0.29120 0.54750 0.28500 0.15720  -0.00330 0.04300  228 LEU A CD1 
1712 C CD2 . LEU A  234 ? 0.26120 0.47850 0.27090 0.14280  0.02560  0.02930  228 LEU A CD2 
1713 N N   . ALA A  235 ? 0.21110 0.56090 0.34480 0.12760  0.01270  0.01800  229 ALA A N   
1714 C CA  . ALA A  235 ? 0.19960 0.57450 0.36480 0.11280  0.01460  0.01020  229 ALA A CA  
1715 C C   . ALA A  235 ? 0.19360 0.54680 0.35720 0.10690  0.03810  0.00730  229 ALA A C   
1716 O O   . ALA A  235 ? 0.20820 0.55840 0.37380 0.08880  0.04160  -0.00040 229 ALA A O   
1717 C CB  . ALA A  235 ? 0.20290 0.62250 0.41750 0.12100  0.00510  0.01430  229 ALA A CB  
1718 N N   . HIS A  236 ? 0.20050 0.53480 0.35710 0.12170  0.05340  0.01330  230 HIS A N   
1719 C CA  . HIS A  236 ? 0.20760 0.51100 0.34950 0.11680  0.07440  0.01040  230 HIS A CA  
1720 C C   . HIS A  236 ? 0.22440 0.48370 0.32790 0.10370  0.07000  0.00480  230 HIS A C   
1721 O O   . HIS A  236 ? 0.24020 0.47930 0.33260 0.08880  0.07680  -0.00050 230 HIS A O   
1722 C CB  . HIS A  236 ? 0.22330 0.50500 0.35800 0.13420  0.08770  0.01620  230 HIS A CB  
1723 C CG  . HIS A  236 ? 0.26860 0.52050 0.38660 0.13130  0.11120  0.01300  230 HIS A CG  
1724 N ND1 . HIS A  236 ? 0.36710 0.58980 0.47220 0.14210  0.12330  0.01470  230 HIS A ND1 
1725 C CD2 . HIS A  236 ? 0.27240 0.51010 0.37710 0.11540  0.12280  0.00770  230 HIS A CD2 
1726 C CE1 . HIS A  236 ? 0.38520 0.57950 0.46660 0.13650  0.14440  0.01070  230 HIS A CE1 
1727 N NE2 . HIS A  236 ? 0.33780 0.53960 0.41690 0.12090  0.14560  0.00750  230 HIS A NE2 
1728 N N   . ILE A  237 ? 0.20330 0.44490 0.28880 0.10920  0.05910  0.00640  231 ILE A N   
1729 C CA  . ILE A  237 ? 0.22220 0.42320 0.28420 0.09750  0.05420  0.00050  231 ILE A CA  
1730 C C   . ILE A  237 ? 0.22540 0.43880 0.29570 0.07550  0.04610  -0.00860 231 ILE A C   
1731 O O   . ILE A  237 ? 0.19380 0.37830 0.25450 0.06090  0.04570  -0.01450 231 ILE A O   
1732 C CB  . ILE A  237 ? 0.20600 0.39010 0.25700 0.10780  0.04840  0.00420  231 ILE A CB  
1733 C CG1 . ILE A  237 ? 0.21110 0.37450 0.25480 0.12820  0.05600  0.01250  231 ILE A CG1 
1734 C CG2 . ILE A  237 ? 0.19670 0.34690 0.23880 0.09340  0.04300  -0.00380 231 ILE A CG2 
1735 C CD1 . ILE A  237 ? 0.25630 0.41160 0.29540 0.14140  0.05300  0.01960  231 ILE A CD1 
1736 N N   . PHE A  238 ? 0.18530 0.43900 0.27320 0.07280  0.03680  -0.01010 232 PHE A N   
1737 C CA  . PHE A  238 ? 0.17730 0.44510 0.27630 0.05240  0.02820  -0.01980 232 PHE A CA  
1738 C C   . PHE A  238 ? 0.19550 0.46730 0.30840 0.04030  0.03670  -0.02190 232 PHE A C   
1739 O O   . PHE A  238 ? 0.18120 0.43160 0.28840 0.02300  0.03480  -0.02840 232 PHE A O   
1740 C CB  . PHE A  238 ? 0.17810 0.48610 0.29120 0.05330  0.01400  -0.02120 232 PHE A CB  
1741 C CG  . PHE A  238 ? 0.17210 0.49450 0.29730 0.03290  0.00310  -0.03270 232 PHE A CG  
1742 C CD1 . PHE A  238 ? 0.16470 0.51030 0.32060 0.02100  0.00450  -0.03560 232 PHE A CD1 
1743 C CD2 . PHE A  238 ? 0.17710 0.48800 0.28420 0.02560  -0.00610 -0.04100 232 PHE A CD2 
1744 C CE1 . PHE A  238 ? 0.15890 0.51770 0.32970 0.00260  -0.00630 -0.04600 232 PHE A CE1 
1745 C CE2 . PHE A  238 ? 0.17350 0.49610 0.29230 0.00720  -0.01610 -0.05300 232 PHE A CE2 
1746 C CZ  . PHE A  238 ? 0.16240 0.51020 0.31470 -0.00440 -0.01820 -0.05550 232 PHE A CZ  
1747 N N   . ARG A  239 ? 0.18220 0.47960 0.31590 0.04870  0.04750  -0.01610 233 ARG A N   
1748 C CA  . ARG A  239 ? 0.18940 0.48820 0.33550 0.03740  0.06210  -0.01700 233 ARG A CA  
1749 C C   . ARG A  239 ? 0.23500 0.47760 0.34120 0.03120  0.07170  -0.01710 233 ARG A C   
1750 O O   . ARG A  239 ? 0.24700 0.47430 0.34800 0.01350  0.07490  -0.02040 233 ARG A O   
1751 C CB  . ARG A  239 ? 0.19680 0.52530 0.37380 0.05040  0.07830  -0.01070 233 ARG A CB  
1752 C CG  . ARG A  239 ? 0.28650 0.61470 0.47760 0.03830  0.10080  -0.01120 233 ARG A CG  
1753 C CD  . ARG A  239 ? 0.35200 0.70580 0.58020 0.05090  0.12420  -0.00610 233 ARG A CD  
1754 N NE  . ARG A  239 ? 0.44180 0.75930 0.63550 0.06630  0.14300  -0.00190 233 ARG A NE  
1755 C CZ  . ARG A  239 ? 0.50500 0.83180 0.72120 0.07900  0.16830  0.00140  233 ARG A CZ  
1756 N NH1 . ARG A  239 ? 0.59000 0.95460 0.86580 0.07570  0.17530  -0.00070 233 ARG A NH1 
1757 N NH2 . ARG A  239 ? 0.46250 0.74750 0.63850 0.09140  0.18150  0.00280  233 ARG A NH2 
1758 N N   . ALA A  240 ? 0.23800 0.44580 0.31510 0.04540  0.07410  -0.01340 234 ALA A N   
1759 C CA  . ALA A  240 ? 0.26190 0.41030 0.29840 0.04090  0.07840  -0.01370 234 ALA A CA  
1760 C C   . ALA A  240 ? 0.27180 0.39130 0.29870 0.02310  0.06010  -0.02030 234 ALA A C   
1761 O O   . ALA A  240 ? 0.29910 0.38220 0.30420 0.00880  0.05960  -0.02180 234 ALA A O   
1762 C CB  . ALA A  240 ? 0.27720 0.39450 0.29020 0.06070  0.08060  -0.00930 234 ALA A CB  
1763 N N   . MET A  241 ? 0.24600 0.37730 0.28780 0.02340  0.04580  -0.02420 235 MET A N   
1764 C CA  . MET A  241 ? 0.24030 0.34650 0.28330 0.00670  0.03050  -0.03210 235 MET A CA  
1765 C C   . MET A  241 ? 0.22580 0.35030 0.28440 -0.01440 0.02760  -0.03730 235 MET A C   
1766 O O   . MET A  241 ? 0.25070 0.33950 0.29940 -0.03000 0.01970  -0.04040 235 MET A O   
1767 C CB  . MET A  241 ? 0.20070 0.31850 0.25830 0.01140  0.02290  -0.03610 235 MET A CB  
1768 C CG  . MET A  241 ? 0.19210 0.28210 0.23820 0.02900  0.02460  -0.03120 235 MET A CG  
1769 S SD  . MET A  241 ? 0.24120 0.34420 0.30010 0.03340  0.02330  -0.03460 235 MET A SD  
1770 C CE  . MET A  241 ? 0.17450 0.24200 0.25060 0.01270  0.01360  -0.04730 235 MET A CE  
1771 N N   . ALA A  242 ? 0.18900 0.36720 0.27430 -0.01510 0.03170  -0.03780 236 ALA A N   
1772 C CA  . ALA A  242 ? 0.18310 0.38220 0.29070 -0.03490 0.02790  -0.04320 236 ALA A CA  
1773 C C   . ALA A  242 ? 0.22530 0.40860 0.32250 -0.04320 0.04220  -0.03770 236 ALA A C   
1774 O O   . ALA A  242 ? 0.22080 0.39570 0.32340 -0.06250 0.03820  -0.04070 236 ALA A O   
1775 C CB  . ALA A  242 ? 0.16650 0.42420 0.30850 -0.03240 0.02420  -0.04580 236 ALA A CB  
1776 N N   . ARG A  243 ? 0.25600 0.43070 0.33580 -0.02930 0.06050  -0.02970 237 ARG A N   
1777 C CA  A ARG A  243 ? 0.26150 0.41340 0.32310 -0.03750 0.07950  -0.02480 237 ARG A CA  
1778 C CA  B ARG A  243 ? 0.26260 0.41360 0.32270 -0.03620 0.08040  -0.02440 237 ARG A CA  
1779 C C   . ARG A  243 ? 0.29430 0.37320 0.30230 -0.04520 0.07320  -0.02360 237 ARG A C   
1780 O O   . ARG A  243 ? 0.32370 0.37440 0.31110 -0.06060 0.08020  -0.02110 237 ARG A O   
1781 C CB  A ARG A  243 ? 0.27370 0.44330 0.33990 -0.02070 0.10570  -0.01830 237 ARG A CB  
1782 C CB  B ARG A  243 ? 0.27600 0.43800 0.33440 -0.01730 0.10520  -0.01790 237 ARG A CB  
1783 C CG  A ARG A  243 ? 0.24710 0.48690 0.37530 -0.01690 0.10960  -0.01880 237 ARG A CG  
1784 C CG  B ARG A  243 ? 0.30610 0.46880 0.36700 -0.02410 0.13470  -0.01360 237 ARG A CG  
1785 C CD  A ARG A  243 ? 0.25090 0.51320 0.41190 -0.03780 0.11210  -0.02130 237 ARG A CD  
1786 C CD  B ARG A  243 ? 0.30990 0.50500 0.39790 -0.00540 0.15940  -0.00960 237 ARG A CD  
1787 N NE  A ARG A  243 ? 0.22790 0.54310 0.43880 -0.04150 0.09070  -0.02750 237 ARG A NE  
1788 N NE  B ARG A  243 ? 0.36300 0.50890 0.39970 0.00790  0.17640  -0.00630 237 ARG A NE  
1789 C CZ  A ARG A  243 ? 0.23850 0.55610 0.45690 -0.05840 0.07070  -0.03490 237 ARG A CZ  
1790 C CZ  B ARG A  243 ? 0.41640 0.51360 0.40770 0.00190  0.20200  -0.00370 237 ARG A CZ  
1791 N NH1 A ARG A  243 ? 0.23760 0.51030 0.42380 -0.07360 0.06710  -0.03640 237 ARG A NH1 
1792 N NH1 B ARG A  243 ? 0.44880 0.54200 0.44260 -0.01710 0.21710  -0.00240 237 ARG A NH1 
1793 N NH2 A ARG A  243 ? 0.23740 0.60070 0.49680 -0.06010 0.05210  -0.04140 237 ARG A NH2 
1794 N NH2 B ARG A  243 ? 0.43830 0.48580 0.37690 0.01500  0.21280  -0.00250 237 ARG A NH2 
1795 N N   . HIS A  244 ? 0.26280 0.36910 0.31370 0.07860  0.08170  0.04470  238 HIS A N   
1796 C CA  . HIS A  244 ? 0.26820 0.35560 0.29550 0.07810  0.08070  0.04080  238 HIS A CA  
1797 C C   . HIS A  244 ? 0.28600 0.36120 0.31030 0.06850  0.06910  0.03720  238 HIS A C   
1798 O O   . HIS A  244 ? 0.23690 0.29410 0.24580 0.07000  0.06360  0.03080  238 HIS A O   
1799 C CB  . HIS A  244 ? 0.26200 0.33410 0.26860 0.08990  0.08410  0.03460  238 HIS A CB  
1800 C CG  . HIS A  244 ? 0.29770 0.38170 0.30700 0.10100  0.09640  0.03800  238 HIS A CG  
1801 N ND1 . HIS A  244 ? 0.32730 0.41690 0.32870 0.10470  0.10670  0.04200  238 HIS A ND1 
1802 C CD2 . HIS A  244 ? 0.31210 0.40480 0.33210 0.10970  0.10060  0.03870  238 HIS A CD2 
1803 C CE1 . HIS A  244 ? 0.34580 0.44730 0.35320 0.11530  0.11730  0.04480  238 HIS A CE1 
1804 N NE2 . HIS A  244 ? 0.33340 0.43700 0.35240 0.11870  0.11360  0.04270  238 HIS A NE2 
1805 N N   . PRO A  245 ? 0.23210 0.31660 0.27140 0.05840  0.06540  0.04110  239 PRO A N   
1806 C CA  . PRO A  245 ? 0.20890 0.28280 0.24640 0.05030  0.05520  0.03790  239 PRO A CA  
1807 C C   . PRO A  245 ? 0.27950 0.33780 0.29800 0.04910  0.05280  0.03530  239 PRO A C   
1808 O O   . PRO A  245 ? 0.22760 0.27510 0.24190 0.04450  0.04450  0.03160  239 PRO A O   
1809 C CB  . PRO A  245 ? 0.25530 0.34300 0.31220 0.04100  0.05370  0.04270  239 PRO A CB  
1810 C CG  . PRO A  245 ? 0.22410 0.32450 0.28680 0.04210  0.06340  0.04910  239 PRO A CG  
1811 C CD  . PRO A  245 ? 0.29040 0.39410 0.34820 0.05360  0.07070  0.04860  239 PRO A CD  
1812 N N   . GLU A  246 ? 0.24410 0.30190 0.25090 0.05310  0.05980  0.03770  240 GLU A N   
1813 C CA  . GLU A  246 ? 0.27330 0.31690 0.26070 0.05250  0.05640  0.03530  240 GLU A CA  
1814 C C   . GLU A  246 ? 0.28710 0.31430 0.25650 0.05830  0.05220  0.02700  240 GLU A C   
1815 O O   . GLU A  246 ? 0.26370 0.27850 0.22000 0.05590  0.04540  0.02340  240 GLU A O   
1816 C CB  . GLU A  246 ? 0.30150 0.34870 0.27920 0.05560  0.06510  0.04080  240 GLU A CB  
1817 C CG  . GLU A  246 ? 0.36200 0.40900 0.32690 0.06690  0.07410  0.03930  240 GLU A CG  
1818 C CD  . GLU A  246 ? 0.42700 0.49120 0.41030 0.07070  0.08260  0.04340  240 GLU A CD  
1819 O OE1 . GLU A  246 ? 0.41410 0.49070 0.42030 0.06400  0.08050  0.04670  240 GLU A OE1 
1820 O OE2 . GLU A  246 ? 0.48460 0.55060 0.45920 0.08090  0.09160  0.04310  240 GLU A OE2 
1821 N N   . MET A  247 ? 0.29020 0.31710 0.25940 0.06590  0.05590  0.02400  241 MET A N   
1822 C CA  . MET A  247 ? 0.27150 0.28070 0.22590 0.07050  0.05120  0.01560  241 MET A CA  
1823 C C   . MET A  247 ? 0.29000 0.29360 0.25390 0.06370  0.04150  0.01290  241 MET A C   
1824 O O   . MET A  247 ? 0.28670 0.27450 0.23970 0.06270  0.03460  0.00680  241 MET A O   
1825 C CB  . MET A  247 ? 0.28380 0.29300 0.23560 0.08140  0.05870  0.01360  241 MET A CB  
1826 C CG  . MET A  247 ? 0.31520 0.32710 0.25300 0.09030  0.06940  0.01500  241 MET A CG  
1827 S SD  . MET A  247 ? 0.34300 0.33370 0.24810 0.09290  0.06550  0.00740  241 MET A SD  
1828 C CE  . MET A  247 ? 0.32600 0.32660 0.23040 0.08600  0.06650  0.01550  241 MET A CE  
1829 N N   . VAL A  248 ? 0.27510 0.29150 0.25920 0.05890  0.04080  0.01760  242 VAL A N   
1830 C CA  . VAL A  248 ? 0.23280 0.24500 0.22540 0.05350  0.03290  0.01590  242 VAL A CA  
1831 C C   . VAL A  248 ? 0.26200 0.26800 0.25190 0.04530  0.02550  0.01500  242 VAL A C   
1832 O O   . VAL A  248 ? 0.24720 0.24520 0.23850 0.04160  0.01880  0.01220  242 VAL A O   
1833 C CB  . VAL A  248 ? 0.21660 0.24500 0.22930 0.05160  0.03430  0.02080  242 VAL A CB  
1834 C CG1 . VAL A  248 ? 0.19950 0.22390 0.21920 0.04660  0.02690  0.01970  242 VAL A CG1 
1835 C CG2 . VAL A  248 ? 0.24590 0.28010 0.26180 0.06110  0.04070  0.02150  242 VAL A CG2 
1836 N N   . ALA A  249 ? 0.24670 0.25640 0.23280 0.04270  0.02690  0.01780  243 ALA A N   
1837 C CA  . ALA A  249 ? 0.26330 0.26780 0.24730 0.03600  0.01990  0.01750  243 ALA A CA  
1838 C C   . ALA A  249 ? 0.27070 0.27270 0.24050 0.03760  0.02160  0.01880  243 ALA A C   
1839 O O   . ALA A  249 ? 0.26630 0.25680 0.21930 0.04070  0.01850  0.01390  243 ALA A O   
1840 C CB  . ALA A  249 ? 0.21870 0.23270 0.21990 0.02890  0.01810  0.02170  243 ALA A CB  
1841 N N   . GLY A  250 ? 0.22650 0.23820 0.20190 0.03560  0.02640  0.02520  244 GLY A N   
1842 C CA  . GLY A  250 ? 0.26140 0.27100 0.22260 0.03790  0.02900  0.02800  244 GLY A CA  
1843 C C   . GLY A  250 ? 0.24800 0.26590 0.21930 0.03280  0.03190  0.03580  244 GLY A C   
1844 O O   . GLY A  250 ? 0.24040 0.26590 0.22980 0.02740  0.03190  0.03820  244 GLY A O   
1845 N N   . GLU A  251 ? 0.26060 0.27630 0.21900 0.03480  0.03450  0.03970  245 GLU A N   
1846 C CA  . GLU A  251 ? 0.29980 0.32120 0.26650 0.03040  0.03790  0.04800  245 GLU A CA  
1847 C C   . GLU A  251 ? 0.26580 0.28480 0.24390 0.02340  0.03000  0.04770  245 GLU A C   
1848 O O   . GLU A  251 ? 0.24230 0.25380 0.21420 0.02300  0.02170  0.04340  245 GLU A O   
1849 C CB  . GLU A  251 ? 0.36530 0.38240 0.31290 0.03470  0.04090  0.05260  245 GLU A CB  
1850 C CG  . GLU A  251 ? 0.41950 0.44000 0.37320 0.03090  0.04510  0.06240  245 GLU A CG  
1851 C CD  . GLU A  251 ? 0.45360 0.48540 0.41960 0.03010  0.05680  0.06930  245 GLU A CD  
1852 O OE1 . GLU A  251 ? 0.45200 0.48940 0.41540 0.03530  0.06330  0.06780  245 GLU A OE1 
1853 O OE2 . GLU A  251 ? 0.57700 0.61190 0.55610 0.02410  0.05930  0.07630  245 GLU A OE2 
1854 N N   . GLY A  252 ? 0.29500 0.32060 0.29040 0.01770  0.03250  0.05210  246 GLY A N   
1855 C CA  . GLY A  252 ? 0.26510 0.28780 0.27020 0.01200  0.02640  0.05190  246 GLY A CA  
1856 C C   . GLY A  252 ? 0.26870 0.29140 0.28260 0.00970  0.02040  0.04550  246 GLY A C   
1857 O O   . GLY A  252 ? 0.21530 0.23670 0.23820 0.00530  0.01650  0.04530  246 GLY A O   
1858 N N   . ARG A  253 ? 0.19360 0.21710 0.20460 0.01310  0.02020  0.04060  247 ARG A N   
1859 C CA  . ARG A  253 ? 0.20190 0.22400 0.21920 0.01160  0.01470  0.03540  247 ARG A CA  
1860 C C   . ARG A  253 ? 0.22690 0.25780 0.26000 0.00820  0.01670  0.03600  247 ARG A C   
1861 O O   . ARG A  253 ? 0.19550 0.23470 0.23420 0.00880  0.02240  0.03870  247 ARG A O   
1862 C CB  . ARG A  253 ? 0.22230 0.23980 0.22990 0.01680  0.01390  0.03030  247 ARG A CB  
1863 C CG  . ARG A  253 ? 0.21710 0.22460 0.20810 0.01950  0.00960  0.02750  247 ARG A CG  
1864 C CD  . ARG A  253 ? 0.22380 0.22570 0.21790 0.01580  0.00110  0.02420  247 ARG A CD  
1865 N NE  . ARG A  253 ? 0.23150 0.23290 0.23340 0.01510  -0.00020 0.02080  247 ARG A NE  
1866 C CZ  . ARG A  253 ? 0.23830 0.23290 0.23340 0.01840  -0.00120 0.01620  247 ARG A CZ  
1867 N NH1 . ARG A  253 ? 0.24140 0.22850 0.22090 0.02250  -0.00160 0.01290  247 ARG A NH1 
1868 N NH2 . ARG A  253 ? 0.24250 0.23690 0.24570 0.01790  -0.00170 0.01470  247 ARG A NH2 
1869 N N   . TYR A  254 ? 0.20800 0.23790 0.24840 0.00500  0.01180  0.03350  248 TYR A N   
1870 C CA  . TYR A  254 ? 0.18780 0.22560 0.24120 0.00190  0.01250  0.03350  248 TYR A CA  
1871 C C   . TYR A  254 ? 0.21610 0.26200 0.27270 0.00540  0.01580  0.03310  248 TYR A C   
1872 O O   . TYR A  254 ? 0.20660 0.26250 0.27360 0.00330  0.01860  0.03520  248 TYR A O   
1873 C CB  . TYR A  254 ? 0.18860 0.22370 0.24570 -0.00020 0.00740  0.03040  248 TYR A CB  
1874 C CG  . TYR A  254 ? 0.16690 0.20920 0.23480 -0.00350 0.00700  0.02990  248 TYR A CG  
1875 C CD1 . TYR A  254 ? 0.20330 0.24610 0.27750 -0.00830 0.00720  0.03100  248 TYR A CD1 
1876 C CD2 . TYR A  254 ? 0.17910 0.22670 0.25020 -0.00160 0.00610  0.02820  248 TYR A CD2 
1877 C CE1 . TYR A  254 ? 0.18090 0.22930 0.26370 -0.01170 0.00590  0.02920  248 TYR A CE1 
1878 C CE2 . TYR A  254 ? 0.18630 0.24110 0.26590 -0.00440 0.00460  0.02720  248 TYR A CE2 
1879 C CZ  . TYR A  254 ? 0.18930 0.24440 0.27440 -0.00980 0.00420  0.02730  248 TYR A CZ  
1880 O OH  . TYR A  254 ? 0.15470 0.21570 0.24670 -0.01290 0.00180  0.02510  248 TYR A OH  
1881 N N   . CYS A  255 ? 0.20140 0.24320 0.25050 0.01060  0.01510  0.03040  249 CYS A N   
1882 C CA  . CYS A  255 ? 0.21640 0.26550 0.26940 0.01510  0.01820  0.03020  249 CYS A CA  
1883 C C   . CYS A  255 ? 0.26230 0.32010 0.31740 0.01730  0.02520  0.03390  249 CYS A C   
1884 O O   . CYS A  255 ? 0.23690 0.30700 0.30290 0.01820  0.02820  0.03580  249 CYS A O   
1885 C CB  . CYS A  255 ? 0.20100 0.24110 0.24420 0.02090  0.01700  0.02670  249 CYS A CB  
1886 S SG  . CYS A  255 ? 0.26980 0.29860 0.31040 0.01820  0.00970  0.02340  249 CYS A SG  
1887 N N   . THR A  256 ? 0.23540 0.28770 0.28010 0.01850  0.02810  0.03530  250 THR A N   
1888 C CA  . THR A  256 ? 0.23060 0.29070 0.27540 0.02140  0.03620  0.03960  250 THR A CA  
1889 C C   . THR A  256 ? 0.24750 0.31820 0.30750 0.01470  0.03860  0.04470  250 THR A C   
1890 O O   . THR A  256 ? 0.23170 0.31570 0.30320 0.01520  0.04400  0.04810  250 THR A O   
1891 C CB  . THR A  256 ? 0.22320 0.27320 0.24960 0.02500  0.03810  0.03980  250 THR A CB  
1892 O OG1 . THR A  256 ? 0.22570 0.26580 0.23890 0.03100  0.03570  0.03410  250 THR A OG1 
1893 C CG2 . THR A  256 ? 0.22980 0.28770 0.25480 0.02820  0.04780  0.04550  250 THR A CG2 
1894 N N   . MET A  257 ? 0.26090 0.32600 0.32260 0.00830  0.03450  0.04510  251 MET A N   
1895 C CA  . MET A  257 ? 0.23560 0.30760 0.31120 0.00130  0.03630  0.04930  251 MET A CA  
1896 C C   . MET A  257 ? 0.22550 0.30800 0.31710 -0.00230 0.03330  0.04720  251 MET A C   
1897 O O   . MET A  257 ? 0.22310 0.31680 0.32890 -0.00650 0.03630  0.05050  251 MET A O   
1898 C CB  . MET A  257 ? 0.26800 0.32920 0.34020 -0.00330 0.03280  0.04980  251 MET A CB  
1899 C CG  . MET A  257 ? 0.24760 0.29980 0.30370 0.00060  0.03490  0.05260  251 MET A CG  
1900 S SD  . MET A  257 ? 0.30540 0.34620 0.35880 -0.00360 0.03070  0.05450  251 MET A SD  
1901 C CE  . MET A  257 ? 0.35700 0.40240 0.42820 -0.01180 0.03440  0.05910  251 MET A CE  
1902 N N   . LEU A  258 ? 0.18340 0.26280 0.27300 -0.00100 0.02720  0.04210  252 LEU A N   
1903 C CA  . LEU A  258 ? 0.20380 0.29330 0.30560 -0.00300 0.02380  0.04020  252 LEU A CA  
1904 C C   . LEU A  258 ? 0.22880 0.33300 0.33920 0.00100  0.02830  0.04280  252 LEU A C   
1905 O O   . LEU A  258 ? 0.19500 0.31280 0.32100 -0.00320 0.02870  0.04480  252 LEU A O   
1906 C CB  . LEU A  258 ? 0.22790 0.31080 0.32320 -0.00040 0.01780  0.03550  252 LEU A CB  
1907 C CG  . LEU A  258 ? 0.20520 0.29810 0.30950 -0.00030 0.01390  0.03380  252 LEU A CG  
1908 C CD1 . LEU A  258 ? 0.22250 0.31900 0.33590 -0.00810 0.01000  0.03240  252 LEU A CD1 
1909 C CD2 . LEU A  258 ? 0.16710 0.25200 0.26240 0.00410  0.01020  0.03090  252 LEU A CD2 
1910 N N   . MET A  259 ? 0.21810 0.32010 0.31920 0.00940  0.03180  0.04260  253 MET A N   
1911 C CA  . MET A  259 ? 0.21000 0.32630 0.31970 0.01480  0.03640  0.04510  253 MET A CA  
1912 C C   . MET A  259 ? 0.20330 0.33070 0.32200 0.01300  0.04430  0.05090  253 MET A C   
1913 O O   . MET A  259 ? 0.21410 0.35890 0.34920 0.01280  0.04680  0.05400  253 MET A O   
1914 C CB  . MET A  259 ? 0.20820 0.31700 0.30470 0.02480  0.03860  0.04290  253 MET A CB  
1915 C CG  . MET A  259 ? 0.21400 0.31700 0.30780 0.02690  0.03180  0.03890  253 MET A CG  
1916 S SD  . MET A  259 ? 0.21400 0.30710 0.29500 0.03840  0.03420  0.03640  253 MET A SD  
1917 C CE  . MET A  259 ? 0.24290 0.31560 0.30370 0.03760  0.03380  0.03290  253 MET A CE  
1918 N N   . ARG A  260 ? 0.25510 0.37360 0.36440 0.01140  0.04830  0.05330  254 ARG A N   
1919 C CA  . ARG A  260 ? 0.23780 0.36660 0.35630 0.00890  0.05650  0.06010  254 ARG A CA  
1920 C C   . ARG A  260 ? 0.17700 0.31630 0.31640 -0.00150 0.05370  0.06220  254 ARG A C   
1921 O O   . ARG A  260 ? 0.24610 0.40190 0.40240 -0.00370 0.05880  0.06720  254 ARG A O   
1922 C CB  . ARG A  260 ? 0.29400 0.41010 0.39670 0.00950  0.06070  0.06280  254 ARG A CB  
1923 C CG  . ARG A  260 ? 0.34310 0.45830 0.43170 0.01960  0.06850  0.06420  254 ARG A CG  
1924 C CD  . ARG A  260 ? 0.40190 0.50240 0.46940 0.02190  0.07030  0.06510  254 ARG A CD  
1925 N NE  . ARG A  260 ? 0.54060 0.63870 0.59200 0.03270  0.07640  0.06400  254 ARG A NE  
1926 C CZ  . ARG A  260 ? 0.51740 0.60250 0.54600 0.03760  0.07730  0.06280  254 ARG A CZ  
1927 N NH1 . ARG A  260 ? 0.46960 0.54420 0.48960 0.03310  0.07290  0.06390  254 ARG A NH1 
1928 N NH2 . ARG A  260 ? 0.51800 0.60030 0.53160 0.04780  0.08240  0.06020  254 ARG A NH2 
1929 N N   . ALA A  261 ? 0.20210 0.33190 0.34060 -0.00800 0.04570  0.05810  255 ALA A N   
1930 C CA  . ALA A  261 ? 0.22010 0.35630 0.37590 -0.01820 0.04190  0.05830  255 ALA A CA  
1931 C C   . ALA A  261 ? 0.22720 0.38200 0.39990 -0.01870 0.03880  0.05720  255 ALA A C   
1932 O O   . ALA A  261 ? 0.20830 0.37670 0.40020 -0.02560 0.03960  0.06020  255 ALA A O   
1933 C CB  . ALA A  261 ? 0.26370 0.38480 0.41200 -0.02250 0.03380  0.05270  255 ALA A CB  
1934 N N   . PHE A  262 ? 0.19790 0.35380 0.36450 -0.01140 0.03510  0.05340  256 PHE A N   
1935 C CA  . PHE A  262 ? 0.21140 0.38450 0.39260 -0.01080 0.03070  0.05240  256 PHE A CA  
1936 C C   . PHE A  262 ? 0.19830 0.38900 0.38960 -0.00390 0.03800  0.05760  256 PHE A C   
1937 O O   . PHE A  262 ? 0.18220 0.39040 0.38860 -0.00310 0.03460  0.05800  256 PHE A O   
1938 C CB  . PHE A  262 ? 0.18430 0.34980 0.35450 -0.00640 0.02300  0.04670  256 PHE A CB  
1939 C CG  . PHE A  262 ? 0.17610 0.33380 0.34500 -0.01420 0.01470  0.04180  256 PHE A CG  
1940 C CD1 . PHE A  262 ? 0.17050 0.34060 0.35240 -0.01920 0.00770  0.03960  256 PHE A CD1 
1941 C CD2 . PHE A  262 ? 0.22290 0.36160 0.37760 -0.01600 0.01390  0.03920  256 PHE A CD2 
1942 C CE1 . PHE A  262 ? 0.20030 0.36210 0.37890 -0.02570 0.00030  0.03420  256 PHE A CE1 
1943 C CE2 . PHE A  262 ? 0.21940 0.35080 0.37260 -0.02220 0.00730  0.03460  256 PHE A CE2 
1944 C CZ  . PHE A  262 ? 0.23410 0.37630 0.39840 -0.02690 0.00070  0.03170  256 PHE A CZ  
1945 N N   . ASP A  263 ? 0.21070 0.39730 0.39350 0.00170  0.04760  0.06140  257 ASP A N   
1946 C CA  . ASP A  263 ? 0.18730 0.39060 0.38010 0.00780  0.05720  0.06740  257 ASP A CA  
1947 C C   . ASP A  263 ? 0.23890 0.45730 0.44120 0.01550  0.05490  0.06680  257 ASP A C   
1948 O O   . ASP A  263 ? 0.23520 0.47610 0.45840 0.01570  0.05780  0.07140  257 ASP A O   
1949 C CB  . ASP A  263 ? 0.28170 0.49940 0.49490 -0.00140 0.06190  0.07380  257 ASP A CB  
1950 C CG  . ASP A  263 ? 0.32960 0.56180 0.54990 0.00510  0.07490  0.08150  257 ASP A CG  
1951 O OD1 . ASP A  263 ? 0.37240 0.59460 0.57360 0.01510  0.08180  0.08160  257 ASP A OD1 
1952 O OD2 . ASP A  263 ? 0.29980 0.55330 0.54490 -0.00020 0.07810  0.08720  257 ASP A OD2 
1953 N N   . GLY A  264 ? 0.21040 0.41640 0.39770 0.02190  0.04950  0.06150  258 GLY A N   
1954 C CA  . GLY A  264 ? 0.21570 0.43130 0.40760 0.03110  0.04770  0.06130  258 GLY A CA  
1955 C C   . GLY A  264 ? 0.22570 0.44630 0.42440 0.02770  0.03620  0.05820  258 GLY A C   
1956 O O   . GLY A  264 ? 0.18120 0.40690 0.38070 0.03620  0.03390  0.05820  258 GLY A O   
1957 N N   . ALA A  265 ? 0.15980 0.37870 0.36260 0.01620  0.02900  0.05570  259 ALA A N   
1958 C CA  . ALA A  265 ? 0.16350 0.38740 0.37070 0.01320  0.01800  0.05240  259 ALA A CA  
1959 C C   . ALA A  265 ? 0.21920 0.42410 0.40610 0.01820  0.01350  0.04800  259 ALA A C   
1960 O O   . ALA A  265 ? 0.16790 0.37710 0.35550 0.01970  0.00590  0.04650  259 ALA A O   
1961 C CB  . ALA A  265 ? 0.20090 0.42670 0.41700 -0.00030 0.01210  0.05000  259 ALA A CB  
1962 N N   . LEU A  266 ? 0.19200 0.37670 0.36110 0.02070  0.01780  0.04650  260 LEU A N   
1963 C CA  . LEU A  266 ? 0.19960 0.36680 0.35180 0.02430  0.01390  0.04300  260 LEU A CA  
1964 C C   . LEU A  266 ? 0.20570 0.35600 0.34230 0.02980  0.02040  0.04250  260 LEU A C   
1965 O O   . LEU A  266 ? 0.20740 0.35810 0.34400 0.02970  0.02720  0.04430  260 LEU A O   
1966 C CB  . LEU A  266 ? 0.18530 0.34360 0.33260 0.01540  0.00710  0.03890  260 LEU A CB  
1967 C CG  . LEU A  266 ? 0.19240 0.34270 0.33830 0.00660  0.00870  0.03770  260 LEU A CG  
1968 C CD1 . LEU A  266 ? 0.19470 0.32620 0.32450 0.00910  0.01270  0.03690  260 LEU A CD1 
1969 C CD2 . LEU A  266 ? 0.16970 0.31800 0.31690 -0.00130 0.00120  0.03390  260 LEU A CD2 
1970 N N   . VAL A  267 ? 0.18660 0.32230 0.31000 0.03450  0.01820  0.04020  261 VAL A N   
1971 C CA  . VAL A  267 ? 0.19270 0.30910 0.29990 0.03680  0.02130  0.03790  261 VAL A CA  
1972 C C   . VAL A  267 ? 0.19970 0.30260 0.29840 0.03160  0.01540  0.03480  261 VAL A C   
1973 O O   . VAL A  267 ? 0.18970 0.29570 0.29150 0.02990  0.01000  0.03460  261 VAL A O   
1974 C CB  . VAL A  267 ? 0.18540 0.29470 0.28490 0.04770  0.02500  0.03780  261 VAL A CB  
1975 C CG1 . VAL A  267 ? 0.18520 0.30890 0.29330 0.05410  0.03250  0.04120  261 VAL A CG1 
1976 C CG2 . VAL A  267 ? 0.17740 0.28590 0.27760 0.05200  0.02030  0.03840  261 VAL A CG2 
1977 N N   . GLY A  268 ? 0.22430 0.31300 0.31210 0.02930  0.01650  0.03280  262 GLY A N   
1978 C CA  . GLY A  268 ? 0.19670 0.27300 0.27730 0.02500  0.01180  0.03030  262 GLY A CA  
1979 C C   . GLY A  268 ? 0.18630 0.24650 0.25410 0.02740  0.01290  0.02810  262 GLY A C   
1980 O O   . GLY A  268 ? 0.22960 0.28700 0.29180 0.03050  0.01710  0.02780  262 GLY A O   
1981 N N   . LYS A  269 ? 0.17380 0.22330 0.23650 0.02630  0.00920  0.02660  263 LYS A N   
1982 C CA  . LYS A  269 ? 0.20450 0.23860 0.25640 0.02800  0.00880  0.02400  263 LYS A CA  
1983 C C   . LYS A  269 ? 0.18660 0.21270 0.23690 0.02250  0.00440  0.02300  263 LYS A C   
1984 O O   . LYS A  269 ? 0.17500 0.20330 0.22970 0.02110  0.00230  0.02440  263 LYS A O   
1985 C CB  . LYS A  269 ? 0.19250 0.22020 0.24080 0.03530  0.01010  0.02370  263 LYS A CB  
1986 C CG  . LYS A  269 ? 0.21170 0.22200 0.24910 0.03650  0.00920  0.02010  263 LYS A CG  
1987 C CD  . LYS A  269 ? 0.21560 0.22180 0.24370 0.03950  0.01230  0.01730  263 LYS A CD  
1988 C CE  . LYS A  269 ? 0.25690 0.24560 0.27350 0.03820  0.00880  0.01250  263 LYS A CE  
1989 N NZ  . LYS A  269 ? 0.25110 0.23960 0.26940 0.02990  0.00390  0.01250  263 LYS A NZ  
1990 N N   . LEU A  270 ? 0.17700 0.19490 0.22110 0.01990  0.00310  0.02100  264 LEU A N   
1991 C CA  . LEU A  270 ? 0.18340 0.19440 0.22720 0.01510  -0.00100 0.02030  264 LEU A CA  
1992 C C   . LEU A  270 ? 0.20320 0.20310 0.24410 0.01640  -0.00280 0.01910  264 LEU A C   
1993 O O   . LEU A  270 ? 0.21540 0.20700 0.24950 0.02030  -0.00210 0.01680  264 LEU A O   
1994 C CB  . LEU A  270 ? 0.16660 0.17390 0.20540 0.01250  -0.00250 0.01890  264 LEU A CB  
1995 C CG  . LEU A  270 ? 0.19550 0.19680 0.23460 0.00820  -0.00710 0.01820  264 LEU A CG  
1996 C CD1 . LEU A  270 ? 0.18410 0.19210 0.23220 0.00450  -0.00740 0.02070  264 LEU A CD1 
1997 C CD2 . LEU A  270 ? 0.18700 0.18500 0.21900 0.00750  -0.00890 0.01690  264 LEU A CD2 
1998 N N   . GLY A  271 ? 0.22450 0.22320 0.27030 0.01280  -0.00500 0.02070  265 GLY A N   
1999 C CA  . GLY A  271 ? 0.22690 0.21460 0.27190 0.01150  -0.00720 0.02020  265 GLY A CA  
2000 C C   . GLY A  271 ? 0.20690 0.19330 0.25480 0.00560  -0.01070 0.01970  265 GLY A C   
2001 O O   . GLY A  271 ? 0.21020 0.20460 0.26350 0.00300  -0.01060 0.02170  265 GLY A O   
2002 N N   . ALA A  272 ? 0.22530 0.20180 0.26980 0.00390  -0.01420 0.01680  266 ALA A N   
2003 C CA  . ALA A  272 ? 0.23590 0.21190 0.28500 -0.00170 -0.01850 0.01660  266 ALA A CA  
2004 C C   . ALA A  272 ? 0.23740 0.21880 0.29720 -0.00470 -0.01730 0.02110  266 ALA A C   
2005 O O   . ALA A  272 ? 0.19760 0.17780 0.25960 -0.00320 -0.01440 0.02380  266 ALA A O   
2006 C CB  . ALA A  272 ? 0.23390 0.19740 0.27900 -0.00360 -0.02320 0.01260  266 ALA A CB  
2007 N N   . ASP A  273 ? 0.25520 0.24250 0.32120 -0.00830 -0.01940 0.02210  267 ASP A N   
2008 C CA  . ASP A  273 ? 0.21290 0.20720 0.28890 -0.01040 -0.01750 0.02630  267 ASP A CA  
2009 C C   . ASP A  273 ? 0.21570 0.21670 0.29050 -0.00720 -0.01270 0.02830  267 ASP A C   
2010 O O   . ASP A  273 ? 0.18000 0.18430 0.25900 -0.00710 -0.00960 0.03160  267 ASP A O   
2011 C CB  . ASP A  273 ? 0.19730 0.18660 0.28020 -0.01350 -0.01760 0.02880  267 ASP A CB  
2012 C CG  . ASP A  273 ? 0.22770 0.21450 0.31680 -0.01870 -0.02340 0.02740  267 ASP A CG  
2013 O OD1 . ASP A  273 ? 0.21460 0.20960 0.30980 -0.02050 -0.02540 0.02830  267 ASP A OD1 
2014 O OD2 . ASP A  273 ? 0.27790 0.25460 0.36570 -0.02100 -0.02650 0.02520  267 ASP A OD2 
2015 N N   . ALA A  274 ? 0.17950 0.18290 0.24840 -0.00480 -0.01220 0.02610  268 ALA A N   
2016 C CA  . ALA A  274 ? 0.16740 0.17810 0.23610 -0.00320 -0.00930 0.02670  268 ALA A CA  
2017 C C   . ALA A  274 ? 0.19540 0.20820 0.26260 -0.00040 -0.00670 0.02810  268 ALA A C   
2018 O O   . ALA A  274 ? 0.19730 0.21490 0.26610 0.00000  -0.00490 0.02950  268 ALA A O   
2019 C CB  . ALA A  274 ? 0.19140 0.20670 0.26580 -0.00500 -0.00880 0.02800  268 ALA A CB  
2020 N N   . SER A  275 ? 0.20320 0.21220 0.26650 0.00230  -0.00660 0.02760  269 SER A N   
2021 C CA  A SER A  275 ? 0.20610 0.21920 0.26760 0.00620  -0.00480 0.02880  269 SER A CA  
2022 C CA  B SER A  275 ? 0.20510 0.21830 0.26660 0.00610  -0.00480 0.02880  269 SER A CA  
2023 C C   . SER A  275 ? 0.16240 0.18020 0.22210 0.00800  -0.00450 0.02670  269 SER A C   
2024 O O   . SER A  275 ? 0.16620 0.18100 0.22360 0.00750  -0.00500 0.02470  269 SER A O   
2025 C CB  A SER A  275 ? 0.17820 0.18410 0.23790 0.00920  -0.00420 0.03090  269 SER A CB  
2026 C CB  B SER A  275 ? 0.17980 0.18610 0.23970 0.00900  -0.00410 0.03110  269 SER A CB  
2027 O OG  A SER A  275 ? 0.19310 0.19680 0.25550 0.00760  -0.00330 0.03430  269 SER A OG  
2028 O OG  B SER A  275 ? 0.17020 0.16720 0.22730 0.00950  -0.00520 0.02880  269 SER A OG  
2029 N N   . TYR A  276 ? 0.21070 0.23690 0.27160 0.01010  -0.00380 0.02740  270 TYR A N   
2030 C CA  . TYR A  276 ? 0.18090 0.21390 0.24290 0.01170  -0.00300 0.02640  270 TYR A CA  
2031 C C   . TYR A  276 ? 0.18260 0.22290 0.24630 0.01610  -0.00290 0.02820  270 TYR A C   
2032 O O   . TYR A  276 ? 0.18370 0.22660 0.24720 0.01670  -0.00410 0.02970  270 TYR A O   
2033 C CB  . TYR A  276 ? 0.17850 0.21790 0.24410 0.00740  -0.00330 0.02500  270 TYR A CB  
2034 C CG  . TYR A  276 ? 0.16550 0.20810 0.23190 0.00790  -0.00140 0.02470  270 TYR A CG  
2035 C CD1 . TYR A  276 ? 0.13840 0.17380 0.20010 0.00780  -0.00050 0.02410  270 TYR A CD1 
2036 C CD2 . TYR A  276 ? 0.17710 0.23060 0.24900 0.00900  -0.00040 0.02540  270 TYR A CD2 
2037 C CE1 . TYR A  276 ? 0.16980 0.20780 0.23030 0.00930  0.00230  0.02440  270 TYR A CE1 
2038 C CE2 . TYR A  276 ? 0.17750 0.23470 0.25090 0.00990  0.00280  0.02610  270 TYR A CE2 
2039 C CZ  . TYR A  276 ? 0.19390 0.24290 0.26060 0.01040  0.00460  0.02570  270 TYR A CZ  
2040 O OH  . TYR A  276 ? 0.21510 0.26760 0.28130 0.01210  0.00860  0.02700  270 TYR A OH  
2041 N N   . ALA A  277 ? 0.14750 0.19160 0.21230 0.02010  -0.00120 0.02830  271 ALA A N   
2042 C CA  . ALA A  277 ? 0.16360 0.21740 0.23200 0.02470  -0.00150 0.03050  271 ALA A CA  
2043 C C   . ALA A  277 ? 0.17290 0.23890 0.24810 0.02490  -0.00020 0.03020  271 ALA A C   
2044 O O   . ALA A  277 ? 0.17080 0.23430 0.24500 0.02500  0.00290  0.02930  271 ALA A O   
2045 C CB  . ALA A  277 ? 0.18940 0.23560 0.25400 0.03150  -0.00010 0.03260  271 ALA A CB  
2046 N N   . ILE A  278 ? 0.18660 0.26640 0.26880 0.02480  -0.00260 0.03120  272 ILE A N   
2047 C CA  . ILE A  278 ? 0.16960 0.26380 0.26180 0.02440  -0.00150 0.03170  272 ILE A CA  
2048 C C   . ILE A  278 ? 0.17460 0.28130 0.27290 0.03050  -0.00320 0.03460  272 ILE A C   
2049 O O   . ILE A  278 ? 0.18850 0.29750 0.28500 0.03160  -0.00750 0.03530  272 ILE A O   
2050 C CB  . ILE A  278 ? 0.17530 0.27560 0.27320 0.01610  -0.00400 0.02960  272 ILE A CB  
2051 C CG1 . ILE A  278 ? 0.19450 0.28300 0.28720 0.01140  -0.00170 0.02790  272 ILE A CG1 
2052 C CG2 . ILE A  278 ? 0.16780 0.28480 0.27900 0.01460  -0.00320 0.03090  272 ILE A CG2 
2053 C CD1 . ILE A  278 ? 0.17390 0.26400 0.27050 0.00380  -0.00400 0.02570  272 ILE A CD1 
2054 N N   . GLY A  279 ? 0.18060 0.29590 0.28570 0.03530  0.00050  0.03660  273 GLY A N   
2055 C CA  . GLY A  279 ? 0.19660 0.32770 0.31080 0.04120  -0.00130 0.03980  273 GLY A CA  
2056 C C   . GLY A  279 ? 0.19580 0.34600 0.32520 0.03660  -0.00190 0.04020  273 GLY A C   
2057 O O   . GLY A  279 ? 0.17810 0.32950 0.31120 0.03510  0.00360  0.04050  273 GLY A O   
2058 N N   . VAL A  280 ? 0.17550 0.34030 0.31340 0.03380  -0.00860 0.04040  274 VAL A N   
2059 C CA  . VAL A  280 ? 0.14360 0.32570 0.29720 0.02670  -0.01070 0.03990  274 VAL A CA  
2060 C C   . VAL A  280 ? 0.18730 0.39170 0.35590 0.03240  -0.01280 0.04390  274 VAL A C   
2061 O O   . VAL A  280 ? 0.16320 0.37370 0.33070 0.03650  -0.01910 0.04480  274 VAL A O   
2062 C CB  . VAL A  280 ? 0.18830 0.36940 0.34040 0.01720  -0.01800 0.03530  274 VAL A CB  
2063 C CG1 . VAL A  280 ? 0.14360 0.34140 0.31360 0.00860  -0.02050 0.03460  274 VAL A CG1 
2064 C CG2 . VAL A  280 ? 0.17070 0.33060 0.30900 0.01260  -0.01580 0.03190  274 VAL A CG2 
2065 N N   . ARG A  281 ? 0.15350 0.37120 0.33650 0.03280  -0.00740 0.04680  275 ARG A N   
2066 C CA  . ARG A  281 ? 0.17890 0.42140 0.38010 0.03770  -0.00930 0.05110  275 ARG A CA  
2067 C C   . ARG A  281 ? 0.14470 0.40350 0.35750 0.02940  -0.02000 0.04910  275 ARG A C   
2068 O O   . ARG A  281 ? 0.17850 0.43190 0.39010 0.01840  -0.02340 0.04460  275 ARG A O   
2069 C CB  . ARG A  281 ? 0.17450 0.42870 0.38970 0.03930  0.00000  0.05500  275 ARG A CB  
2070 C CG  . ARG A  281 ? 0.19220 0.43260 0.39540 0.05000  0.00990  0.05670  275 ARG A CG  
2071 C CD  . ARG A  281 ? 0.17850 0.43330 0.39550 0.05360  0.01970  0.06110  275 ARG A CD  
2072 N NE  . ARG A  281 ? 0.22270 0.50350 0.45980 0.05970  0.01800  0.06600  275 ARG A NE  
2073 C CZ  . ARG A  281 ? 0.25260 0.55260 0.50700 0.06370  0.02580  0.07100  275 ARG A CZ  
2074 N NH1 . ARG A  281 ? 0.23130 0.52600 0.48270 0.06350  0.03670  0.07210  275 ARG A NH1 
2075 N NH2 . ARG A  281 ? 0.26300 0.58040 0.53130 0.06620  0.02180  0.07300  275 ARG A NH2 
2076 N N   . ALA A  282 ? 0.20440 0.48260 0.42790 0.03530  -0.02580 0.05220  276 ALA A N   
2077 C CA  . ALA A  282 ? 0.18490 0.47940 0.41860 0.02780  -0.03750 0.04970  276 ALA A CA  
2078 C C   . ALA A  282 ? 0.21720 0.52350 0.46960 0.01540  -0.03730 0.04820  276 ALA A C   
2079 O O   . ALA A  282 ? 0.19400 0.51140 0.46180 0.01630  -0.02930 0.05270  276 ALA A O   
2080 C CB  . ALA A  282 ? 0.13840 0.45560 0.38360 0.03680  -0.04360 0.05440  276 ALA A CB  
2081 N N   . SER A  283 ? 0.15740 0.46080 0.40830 0.00410  -0.04570 0.04200  277 SER A N   
2082 C CA  . SER A  283 ? 0.19810 0.50790 0.46510 -0.00930 -0.04600 0.03990  277 SER A CA  
2083 C C   . SER A  283 ? 0.18500 0.50030 0.45450 -0.01880 -0.05970 0.03310  277 SER A C   
2084 O O   . SER A  283 ? 0.19930 0.51290 0.45570 -0.01430 -0.06810 0.03020  277 SER A O   
2085 C CB  . SER A  283 ? 0.21530 0.50110 0.47020 -0.01420 -0.03730 0.03800  277 SER A CB  
2086 O OG  . SER A  283 ? 0.19090 0.45610 0.42480 -0.01640 -0.04240 0.03150  277 SER A OG  
2087 N N   . ASP A  284 ? 0.18700 0.50720 0.47180 -0.03220 -0.06170 0.03030  278 ASP A N   
2088 C CA  . ASP A  284 ? 0.18590 0.50600 0.47010 -0.04240 -0.07460 0.02190  278 ASP A CA  
2089 C C   . ASP A  284 ? 0.18820 0.48080 0.44310 -0.04130 -0.07620 0.01520  278 ASP A C   
2090 O O   . ASP A  284 ? 0.19900 0.49040 0.44370 -0.04280 -0.08720 0.00870  278 ASP A O   
2091 C CB  . ASP A  284 ? 0.15850 0.47950 0.46010 -0.05710 -0.07420 0.01900  278 ASP A CB  
2092 C CG  . ASP A  284 ? 0.23920 0.58070 0.56410 -0.05840 -0.07270 0.02150  278 ASP A CG  
2093 O OD1 . ASP A  284 ? 0.19100 0.54870 0.52130 -0.04920 -0.07500 0.02460  278 ASP A OD1 
2094 O OD2 . ASP A  284 ? 0.21650 0.55710 0.55450 -0.06910 -0.06890 0.02060  278 ASP A OD2 
2095 N N   . ALA A  285 ? 0.19420 0.46550 0.43510 -0.03800 -0.06540 0.01690  279 ALA A N   
2096 C CA  . ALA A  285 ? 0.18070 0.42700 0.39630 -0.03690 -0.06560 0.01130  279 ALA A CA  
2097 C C   . ALA A  285 ? 0.22170 0.46670 0.42010 -0.02560 -0.06900 0.01210  279 ALA A C   
2098 O O   . ALA A  285 ? 0.24770 0.48420 0.43040 -0.02590 -0.07580 0.00630  279 ALA A O   
2099 C CB  . ALA A  285 ? 0.14260 0.36950 0.35040 -0.03620 -0.05360 0.01390  279 ALA A CB  
2100 N N   . THR A  286 ? 0.17870 0.43090 0.37910 -0.01510 -0.06390 0.01940  280 THR A N   
2101 C CA  . THR A  286 ? 0.16970 0.41990 0.35490 -0.00420 -0.06650 0.02150  280 THR A CA  
2102 C C   . THR A  286 ? 0.21320 0.48090 0.40140 -0.00420 -0.07940 0.01920  280 THR A C   
2103 O O   . THR A  286 ? 0.17620 0.43730 0.34620 0.00030  -0.08460 0.01720  280 THR A O   
2104 C CB  . THR A  286 ? 0.20590 0.45970 0.39440 0.00700  -0.05830 0.02970  280 THR A CB  
2105 O OG1 . THR A  286 ? 0.18240 0.46100 0.39360 0.00830  -0.05940 0.03410  280 THR A OG1 
2106 C CG2 . THR A  286 ? 0.24240 0.47800 0.42550 0.00700  -0.04640 0.03090  280 THR A CG2 
2107 N N   . ARG A  287 ? 0.20210 0.49280 0.41320 -0.00940 -0.08490 0.01970  281 ARG A N   
2108 C CA  . ARG A  287 ? 0.17620 0.48560 0.39170 -0.01020 -0.09890 0.01710  281 ARG A CA  
2109 C C   . ARG A  287 ? 0.22730 0.52480 0.42800 -0.01860 -0.10760 0.00690  281 ARG A C   
2110 O O   . ARG A  287 ? 0.22240 0.52260 0.40930 -0.01480 -0.11720 0.00400  281 ARG A O   
2111 C CB  . ARG A  287 ? 0.16630 0.50370 0.41280 -0.01570 -0.10280 0.01960  281 ARG A CB  
2112 C CG  . ARG A  287 ? 0.17050 0.51890 0.42780 -0.00400 -0.09530 0.02880  281 ARG A CG  
2113 C CD  . ARG A  287 ? 0.16760 0.53580 0.45090 -0.00740 -0.09740 0.02950  281 ARG A CD  
2114 N NE  . ARG A  287 ? 0.16080 0.52940 0.46070 -0.01570 -0.08790 0.03030  281 ARG A NE  
2115 C CZ  . ARG A  287 ? 0.19560 0.56210 0.49930 -0.00970 -0.07420 0.03710  281 ARG A CZ  
2116 N NH1 . ARG A  287 ? 0.14980 0.51400 0.44430 0.00440  -0.06870 0.04300  281 ARG A NH1 
2117 N NH2 . ARG A  287 ? 0.14830 0.51330 0.46390 -0.01780 -0.06570 0.03780  281 ARG A NH2 
2118 N N   . GLN A  288 ? 0.17880 0.46210 0.38080 -0.02930 -0.10410 0.00140  282 GLN A N   
2119 C CA  . GLN A  288 ? 0.26270 0.53160 0.44990 -0.03680 -0.11100 -0.00910 282 GLN A CA  
2120 C C   . GLN A  288 ? 0.25110 0.49970 0.40880 -0.02840 -0.10810 -0.01040 282 GLN A C   
2121 O O   . GLN A  288 ? 0.28250 0.52490 0.42370 -0.02950 -0.11600 -0.01780 282 GLN A O   
2122 C CB  . GLN A  288 ? 0.27670 0.53260 0.47200 -0.04870 -0.10600 -0.01320 282 GLN A CB  
2123 C CG  . GLN A  288 ? 0.45760 0.69680 0.63880 -0.05640 -0.11240 -0.02450 282 GLN A CG  
2124 C CD  . GLN A  288 ? 0.55970 0.78740 0.75230 -0.06810 -0.10780 -0.02750 282 GLN A CD  
2125 O OE1 . GLN A  288 ? 0.61070 0.85280 0.82820 -0.07640 -0.10880 -0.02530 282 GLN A OE1 
2126 N NE2 . GLN A  288 ? 0.58770 0.79000 0.76330 -0.06860 -0.10200 -0.03160 282 GLN A NE2 
2127 N N   . LEU A  289 ? 0.20980 0.44850 0.36080 -0.02000 -0.09680 -0.00330 283 LEU A N   
2128 C CA  . LEU A  289 ? 0.27210 0.49320 0.39850 -0.01200 -0.09270 -0.00260 283 LEU A CA  
2129 C C   . LEU A  289 ? 0.28870 0.51950 0.40450 -0.00170 -0.09870 0.00120  283 LEU A C   
2130 O O   . LEU A  289 ? 0.27560 0.49340 0.37100 0.00510  -0.09560 0.00260  283 LEU A O   
2131 C CB  . LEU A  289 ? 0.23990 0.44770 0.36500 -0.00750 -0.07950 0.00360  283 LEU A CB  
2132 C CG  . LEU A  289 ? 0.20970 0.40310 0.33860 -0.01560 -0.07260 0.00060  283 LEU A CG  
2133 C CD1 . LEU A  289 ? 0.19700 0.38230 0.32710 -0.01070 -0.06130 0.00730  283 LEU A CD1 
2134 C CD2 . LEU A  289 ? 0.20340 0.37850 0.31420 -0.01820 -0.07320 -0.00630 283 LEU A CD2 
2135 N N   . GLY A  290 ? 0.23860 0.49260 0.36870 -0.00010 -0.10660 0.00390  284 GLY A N   
2136 C CA  . GLY A  290 ? 0.32510 0.59000 0.44530 0.00920  -0.11440 0.00720  284 GLY A CA  
2137 C C   . GLY A  290 ? 0.30680 0.57950 0.43150 0.02150  -0.10950 0.01850  284 GLY A C   
2138 O O   . GLY A  290 ? 0.35580 0.63290 0.46850 0.03080  -0.11420 0.02260  284 GLY A O   
2139 N N   . THR A  291 ? 0.26480 0.53850 0.40540 0.02240  -0.10020 0.02360  285 THR A N   
2140 C CA  . THR A  291 ? 0.25400 0.53310 0.39880 0.03450  -0.09490 0.03350  285 THR A CA  
2141 C C   . THR A  291 ? 0.26140 0.56360 0.43370 0.03410  -0.09530 0.03710  285 THR A C   
2142 O O   . THR A  291 ? 0.19850 0.50560 0.38660 0.02410  -0.09380 0.03340  285 THR A O   
2143 C CB  . THR A  291 ? 0.26890 0.52470 0.40320 0.03860  -0.08180 0.03680  285 THR A CB  
2144 O OG1 . THR A  291 ? 0.30230 0.56110 0.43960 0.05060  -0.07700 0.04570  285 THR A OG1 
2145 C CG2 . THR A  291 ? 0.22350 0.47230 0.36810 0.02980  -0.07430 0.03330  285 THR A CG2 
2146 N N   . ASP A  292 ? 0.20010 0.51710 0.37890 0.04550  -0.09690 0.04490  286 ASP A N   
2147 C CA  . ASP A  292 ? 0.21170 0.54670 0.41470 0.04630  -0.09570 0.04810  286 ASP A CA  
2148 C C   . ASP A  292 ? 0.18550 0.51460 0.39570 0.05220  -0.08170 0.05370  286 ASP A C   
2149 O O   . ASP A  292 ? 0.26190 0.60260 0.49010 0.05390  -0.07800 0.05630  286 ASP A O   
2150 C CB  . ASP A  292 ? 0.22660 0.57350 0.43100 0.05480  -0.10340 0.05190  286 ASP A CB  
2151 C CG  . ASP A  292 ? 0.35580 0.69060 0.54200 0.06920  -0.09960 0.05930  286 ASP A CG  
2152 O OD1 . ASP A  292 ? 0.39880 0.71620 0.57290 0.07300  -0.09080 0.06160  286 ASP A OD1 
2153 O OD2 . ASP A  292 ? 0.42700 0.76930 0.61160 0.07670  -0.10570 0.06310  286 ASP A OD2 
2154 N N   . GLY A  293 ? 0.20450 0.51120 0.39870 0.05490  -0.07320 0.05430  287 GLY A N   
2155 C CA  . GLY A  293 ? 0.20360 0.50100 0.40090 0.06080  -0.06050 0.05830  287 GLY A CA  
2156 C C   . GLY A  293 ? 0.16620 0.44100 0.35420 0.05300  -0.05210 0.05360  287 GLY A C   
2157 O O   . GLY A  293 ? 0.18570 0.45740 0.37310 0.04130  -0.05510 0.04730  287 GLY A O   
2158 N N   . ALA A  294 ? 0.15260 0.41090 0.33290 0.05980  -0.04190 0.05630  288 ALA A N   
2159 C CA  . ALA A  294 ? 0.14730 0.38450 0.31810 0.05360  -0.03440 0.05230  288 ALA A CA  
2160 C C   . ALA A  294 ? 0.17980 0.39700 0.33040 0.05040  -0.03700 0.04880  288 ALA A C   
2161 O O   . ALA A  294 ? 0.18030 0.39760 0.32200 0.05450  -0.04280 0.05030  288 ALA A O   
2162 C CB  . ALA A  294 ? 0.16640 0.39330 0.33540 0.06200  -0.02380 0.05560  288 ALA A CB  
2163 N N   . LEU A  295 ? 0.17090 0.37150 0.31440 0.04340  -0.03220 0.04480  289 LEU A N   
2164 C CA  . LEU A  295 ? 0.17650 0.36020 0.30380 0.03900  -0.03390 0.04110  289 LEU A CA  
2165 C C   . LEU A  295 ? 0.19700 0.35960 0.31460 0.03980  -0.02570 0.04110  289 LEU A C   
2166 O O   . LEU A  295 ? 0.19310 0.35390 0.31620 0.03950  -0.01980 0.04120  289 LEU A O   
2167 C CB  . LEU A  295 ? 0.25950 0.44750 0.39090 0.02760  -0.03850 0.03500  289 LEU A CB  
2168 C CG  . LEU A  295 ? 0.30230 0.47610 0.42060 0.02120  -0.04040 0.02980  289 LEU A CG  
2169 C CD1 . LEU A  295 ? 0.32170 0.50870 0.44350 0.01640  -0.05000 0.02570  289 LEU A CD1 
2170 C CD2 . LEU A  295 ? 0.27810 0.44230 0.39920 0.01400  -0.03500 0.02690  289 LEU A CD2 
2171 N N   . GLY A  296 ? 0.19900 0.34620 0.30220 0.04110  -0.02550 0.04120  290 GLY A N   
2172 C CA  . GLY A  296 ? 0.23110 0.35860 0.32570 0.04000  -0.01940 0.04040  290 GLY A CA  
2173 C C   . GLY A  296 ? 0.19620 0.31400 0.28270 0.03280  -0.02060 0.03650  290 GLY A C   
2174 O O   . GLY A  296 ? 0.20640 0.32700 0.28730 0.03220  -0.02510 0.03590  290 GLY A O   
2175 N N   . ILE A  297 ? 0.16110 0.26780 0.24600 0.02820  -0.01650 0.03410  291 ILE A N   
2176 C CA  . ILE A  297 ? 0.16940 0.26630 0.24780 0.02240  -0.01650 0.03090  291 ILE A CA  
2177 C C   . ILE A  297 ? 0.19440 0.27570 0.26680 0.02340  -0.01200 0.03220  291 ILE A C   
2178 O O   . ILE A  297 ? 0.17160 0.24870 0.24610 0.02440  -0.00880 0.03240  291 ILE A O   
2179 C CB  . ILE A  297 ? 0.15430 0.25400 0.23870 0.01460  -0.01700 0.02660  291 ILE A CB  
2180 C CG1 . ILE A  297 ? 0.14270 0.25800 0.23530 0.01200  -0.02220 0.02480  291 ILE A CG1 
2181 C CG2 . ILE A  297 ? 0.14200 0.23030 0.21950 0.01000  -0.01640 0.02370  291 ILE A CG2 
2182 C CD1 . ILE A  297 ? 0.19570 0.31500 0.29810 0.00500  -0.02130 0.02240  291 ILE A CD1 
2183 N N   . SER A  298 ? 0.18040 0.25330 0.24540 0.02300  -0.01180 0.03290  292 SER A N   
2184 C CA  . SER A  298 ? 0.15830 0.21750 0.21990 0.02210  -0.00830 0.03370  292 SER A CA  
2185 C C   . SER A  298 ? 0.19880 0.25390 0.25740 0.01760  -0.00810 0.03200  292 SER A C   
2186 O O   . SER A  298 ? 0.17040 0.23010 0.22550 0.01750  -0.00990 0.03140  292 SER A O   
2187 C CB  . SER A  298 ? 0.17900 0.23070 0.23680 0.02760  -0.00660 0.03840  292 SER A CB  
2188 O OG  . SER A  298 ? 0.17330 0.22850 0.22650 0.03070  -0.00790 0.04180  292 SER A OG  
2189 N N   . VAL A  299 ? 0.19550 0.24260 0.25530 0.01430  -0.00620 0.03090  293 VAL A N   
2190 C CA  . VAL A  299 ? 0.18390 0.22830 0.24320 0.01020  -0.00560 0.02900  293 VAL A CA  
2191 C C   . VAL A  299 ? 0.17620 0.21130 0.23610 0.00920  -0.00360 0.03100  293 VAL A C   
2192 O O   . VAL A  299 ? 0.16410 0.19420 0.22520 0.00930  -0.00360 0.03100  293 VAL A O   
2193 C CB  . VAL A  299 ? 0.14260 0.18960 0.20560 0.00610  -0.00660 0.02510  293 VAL A CB  
2194 C CG1 . VAL A  299 ? 0.16040 0.20300 0.22290 0.00310  -0.00550 0.02370  293 VAL A CG1 
2195 C CG2 . VAL A  299 ? 0.18150 0.23790 0.24600 0.00550  -0.00920 0.02290  293 VAL A CG2 
2196 N N   . LYS A  300 ? 0.13610 0.16930 0.19540 0.00820  -0.00200 0.03240  294 LYS A N   
2197 C CA  . LYS A  300 ? 0.13600 0.16270 0.19900 0.00590  -0.00060 0.03410  294 LYS A CA  
2198 C C   . LYS A  300 ? 0.21130 0.23990 0.27650 0.00380  0.00070  0.03310  294 LYS A C   
2199 O O   . LYS A  300 ? 0.19100 0.22290 0.25260 0.00540  0.00240  0.03320  294 LYS A O   
2200 C CB  . LYS A  300 ? 0.17040 0.19260 0.23290 0.00760  0.00140  0.03920  294 LYS A CB  
2201 C CG  . LYS A  300 ? 0.15910 0.17680 0.22770 0.00430  0.00310  0.04190  294 LYS A CG  
2202 C CD  . LYS A  300 ? 0.18900 0.20130 0.26220 0.00090  0.00020  0.03960  294 LYS A CD  
2203 C CE  . LYS A  300 ? 0.19220 0.20280 0.27400 -0.00310 0.00110  0.04260  294 LYS A CE  
2204 N NZ  . LYS A  300 ? 0.24610 0.25060 0.33170 -0.00670 -0.00310 0.04020  294 LYS A NZ  
2205 N N   . ILE A  301 ? 0.17850 0.20490 0.24860 0.00090  -0.00020 0.03190  295 ILE A N   
2206 C CA  . ILE A  301 ? 0.14330 0.17100 0.21740 -0.00020 0.00140  0.03210  295 ILE A CA  
2207 C C   . ILE A  301 ? 0.18980 0.21620 0.26950 -0.00110 0.00330  0.03650  295 ILE A C   
2208 O O   . ILE A  301 ? 0.14350 0.16610 0.22690 -0.00330 0.00110  0.03750  295 ILE A O   
2209 C CB  . ILE A  301 ? 0.20600 0.23270 0.28330 -0.00230 -0.00070 0.02980  295 ILE A CB  
2210 C CG1 . ILE A  301 ? 0.17220 0.19970 0.24550 -0.00230 -0.00200 0.02640  295 ILE A CG1 
2211 C CG2 . ILE A  301 ? 0.12490 0.15320 0.20700 -0.00210 0.00130  0.03040  295 ILE A CG2 
2212 C CD1 . ILE A  301 ? 0.21070 0.24100 0.28020 -0.00120 -0.00080 0.02420  295 ILE A CD1 
2213 N N   . GLU A  302 ? 0.16500 0.19460 0.24510 0.00060  0.00760  0.03920  296 GLU A N   
2214 C CA  . GLU A  302 ? 0.16310 0.19270 0.24940 -0.00030 0.01070  0.04480  296 GLU A CA  
2215 C C   . GLU A  302 ? 0.18200 0.21140 0.27990 -0.00430 0.00840  0.04580  296 GLU A C   
2216 O O   . GLU A  302 ? 0.15300 0.17970 0.25700 -0.00720 0.00790  0.04910  296 GLU A O   
2217 C CB  . GLU A  302 ? 0.16730 0.20170 0.25230 0.00280  0.01670  0.04740  296 GLU A CB  
2218 C CG  . GLU A  302 ? 0.14690 0.18250 0.23890 0.00200  0.02130  0.05470  296 GLU A CG  
2219 C CD  . GLU A  302 ? 0.20630 0.23650 0.29450 0.00190  0.02110  0.05830  296 GLU A CD  
2220 O OE1 . GLU A  302 ? 0.18260 0.21140 0.25930 0.00550  0.02030  0.05690  296 GLU A OE1 
2221 O OE2 . GLU A  302 ? 0.19050 0.21750 0.28770 -0.00170 0.02140  0.06260  296 GLU A OE2 
2222 N N   . ASP A  303 ? 0.15720 0.18920 0.25840 -0.00470 0.00670  0.04320  297 ASP A N   
2223 C CA  . ASP A  303 ? 0.16000 0.19410 0.27250 -0.00800 0.00370  0.04440  297 ASP A CA  
2224 C C   . ASP A  303 ? 0.18990 0.21910 0.30000 -0.01040 -0.00290 0.04090  297 ASP A C   
2225 O O   . ASP A  303 ? 0.17160 0.20210 0.28940 -0.01320 -0.00700 0.04130  297 ASP A O   
2226 C CB  . ASP A  303 ? 0.15670 0.19650 0.27410 -0.00580 0.00570  0.04440  297 ASP A CB  
2227 C CG  . ASP A  303 ? 0.16140 0.19840 0.26960 -0.00340 0.00490  0.03970  297 ASP A CG  
2228 O OD1 . ASP A  303 ? 0.17470 0.20940 0.28210 -0.00460 0.00030  0.03760  297 ASP A OD1 
2229 O OD2 . ASP A  303 ? 0.14440 0.18100 0.24520 -0.00050 0.00850  0.03820  297 ASP A OD2 
2230 N N   . GLY A  304 ? 0.15810 0.18250 0.25780 -0.00910 -0.00410 0.03760  298 GLY A N   
2231 C CA  . GLY A  304 ? 0.17930 0.19850 0.27540 -0.01060 -0.00920 0.03470  298 GLY A CA  
2232 C C   . GLY A  304 ? 0.20120 0.22120 0.29400 -0.00990 -0.01160 0.03220  298 GLY A C   
2233 O O   . GLY A  304 ? 0.20560 0.22190 0.29490 -0.01090 -0.01580 0.03030  298 GLY A O   
2234 N N   . ASN A  305 ? 0.17380 0.19730 0.26660 -0.00810 -0.00900 0.03220  299 ASN A N   
2235 C CA  . ASN A  305 ? 0.18780 0.21120 0.27870 -0.00750 -0.01080 0.03110  299 ASN A CA  
2236 C C   . ASN A  305 ? 0.17990 0.20040 0.26200 -0.00680 -0.01050 0.02870  299 ASN A C   
2237 O O   . ASN A  305 ? 0.19000 0.21160 0.26970 -0.00590 -0.00770 0.02770  299 ASN A O   
2238 C CB  . ASN A  305 ? 0.17960 0.20600 0.27460 -0.00570 -0.00780 0.03200  299 ASN A CB  
2239 C CG  . ASN A  305 ? 0.19920 0.22420 0.29380 -0.00500 -0.00950 0.03230  299 ASN A CG  
2240 O OD1 . ASN A  305 ? 0.17460 0.19650 0.26300 -0.00500 -0.00950 0.03090  299 ASN A OD1 
2241 N ND2 . ASN A  305 ? 0.21090 0.23920 0.31330 -0.00400 -0.01070 0.03480  299 ASN A ND2 
2242 N N   . LEU A  306 ? 0.14370 0.16140 0.22130 -0.00710 -0.01350 0.02800  300 LEU A N   
2243 C CA  . LEU A  306 ? 0.17880 0.19510 0.24910 -0.00610 -0.01220 0.02650  300 LEU A CA  
2244 C C   . LEU A  306 ? 0.20290 0.22070 0.27360 -0.00600 -0.00990 0.02700  300 LEU A C   
2245 O O   . LEU A  306 ? 0.16080 0.18030 0.22990 -0.00600 -0.00760 0.02610  300 LEU A O   
2246 C CB  . LEU A  306 ? 0.25440 0.26690 0.31820 -0.00560 -0.01520 0.02570  300 LEU A CB  
2247 C CG  . LEU A  306 ? 0.37990 0.38830 0.43860 -0.00480 -0.01600 0.02350  300 LEU A CG  
2248 C CD1 . LEU A  306 ? 0.35880 0.36210 0.41030 -0.00460 -0.02030 0.02180  300 LEU A CD1 
2249 C CD2 . LEU A  306 ? 0.31280 0.32330 0.36810 -0.00260 -0.01200 0.02310  300 LEU A CD2 
2250 N N   . GLU A  307 ? 0.20080 0.21790 0.27410 -0.00600 -0.01070 0.02870  301 GLU A N   
2251 C CA  . GLU A  307 ? 0.18470 0.20080 0.25850 -0.00620 -0.00820 0.02940  301 GLU A CA  
2252 C C   . GLU A  307 ? 0.16710 0.18460 0.24350 -0.00690 -0.00560 0.02710  301 GLU A C   
2253 O O   . GLU A  307 ? 0.19040 0.20800 0.26610 -0.00840 -0.00400 0.02590  301 GLU A O   
2254 C CB  . GLU A  307 ? 0.20690 0.22110 0.28380 -0.00510 -0.00930 0.03200  301 GLU A CB  
2255 C CG  . GLU A  307 ? 0.20850 0.21900 0.28600 -0.00530 -0.00660 0.03310  301 GLU A CG  
2256 C CD  . GLU A  307 ? 0.28750 0.29550 0.36850 -0.00280 -0.00740 0.03630  301 GLU A CD  
2257 O OE1 . GLU A  307 ? 0.31150 0.32200 0.39810 -0.00120 -0.00800 0.03630  301 GLU A OE1 
2258 O OE2 . GLU A  307 ? 0.25710 0.26100 0.33580 -0.00220 -0.00700 0.03950  301 GLU A OE2 
2259 N N   . MET A  308 ? 0.17360 0.19260 0.25290 -0.00610 -0.00520 0.02640  302 MET A N   
2260 C CA  . MET A  308 ? 0.16130 0.18140 0.24020 -0.00600 -0.00310 0.02390  302 MET A CA  
2261 C C   . MET A  308 ? 0.19470 0.21800 0.27030 -0.00660 -0.00350 0.02240  302 MET A C   
2262 O O   . MET A  308 ? 0.18860 0.21340 0.26320 -0.00740 -0.00300 0.02000  302 MET A O   
2263 C CB  . MET A  308 ? 0.19770 0.21940 0.27930 -0.00410 -0.00160 0.02450  302 MET A CB  
2264 C CG  . MET A  308 ? 0.16660 0.18670 0.25310 -0.00240 -0.00070 0.02600  302 MET A CG  
2265 S SD  . MET A  308 ? 0.22040 0.23440 0.30510 -0.00190 0.00140  0.02310  302 MET A SD  
2266 C CE  . MET A  308 ? 0.22720 0.23740 0.31260 -0.00340 -0.00070 0.02580  302 MET A CE  
2267 N N   . LEU A  309 ? 0.12370 0.14800 0.19790 -0.00600 -0.00460 0.02370  303 LEU A N   
2268 C CA  . LEU A  309 ? 0.16990 0.19720 0.24160 -0.00530 -0.00470 0.02300  303 LEU A CA  
2269 C C   . LEU A  309 ? 0.17790 0.20790 0.25000 -0.00670 -0.00430 0.02200  303 LEU A C   
2270 O O   . LEU A  309 ? 0.16840 0.20290 0.24140 -0.00720 -0.00440 0.02040  303 LEU A O   
2271 C CB  . LEU A  309 ? 0.14470 0.16980 0.21430 -0.00400 -0.00570 0.02420  303 LEU A CB  
2272 C CG  . LEU A  309 ? 0.15790 0.18570 0.22500 -0.00190 -0.00520 0.02380  303 LEU A CG  
2273 C CD1 . LEU A  309 ? 0.17210 0.20300 0.23920 -0.00030 -0.00480 0.02430  303 LEU A CD1 
2274 C CD2 . LEU A  309 ? 0.13740 0.16030 0.20100 -0.00020 -0.00580 0.02400  303 LEU A CD2 
2275 N N   . TYR A  310 ? 0.18970 0.21740 0.26150 -0.00750 -0.00390 0.02330  304 TYR A N   
2276 C CA  . TYR A  310 ? 0.16920 0.19990 0.24260 -0.00910 -0.00250 0.02360  304 TYR A CA  
2277 C C   . TYR A  310 ? 0.18300 0.21420 0.26080 -0.01230 -0.00230 0.02190  304 TYR A C   
2278 O O   . TYR A  310 ? 0.19410 0.23060 0.27560 -0.01450 -0.00210 0.02110  304 TYR A O   
2279 C CB  . TYR A  310 ? 0.20130 0.22850 0.27200 -0.00890 -0.00140 0.02620  304 TYR A CB  
2280 C CG  . TYR A  310 ? 0.16920 0.19530 0.23400 -0.00590 -0.00190 0.02670  304 TYR A CG  
2281 C CD1 . TYR A  310 ? 0.18690 0.21630 0.25060 -0.00360 -0.00140 0.02560  304 TYR A CD1 
2282 C CD2 . TYR A  310 ? 0.22820 0.24920 0.28780 -0.00490 -0.00340 0.02790  304 TYR A CD2 
2283 C CE1 . TYR A  310 ? 0.19280 0.21850 0.24990 -0.00050 -0.00170 0.02510  304 TYR A CE1 
2284 C CE2 . TYR A  310 ? 0.23180 0.25010 0.28440 -0.00230 -0.00460 0.02700  304 TYR A CE2 
2285 C CZ  . TYR A  310 ? 0.21270 0.23250 0.26380 -0.00020 -0.00340 0.02530  304 TYR A CZ  
2286 O OH  . TYR A  310 ? 0.28810 0.30280 0.33120 0.00260  -0.00450 0.02370  304 TYR A OH  
2287 N N   . ALA A  311 ? 0.17300 0.19850 0.25080 -0.01270 -0.00240 0.02120  305 ALA A N   
2288 C CA  . ALA A  311 ? 0.18260 0.20570 0.26280 -0.01520 -0.00240 0.01830  305 ALA A CA  
2289 C C   . ALA A  311 ? 0.16420 0.19240 0.24370 -0.01550 -0.00420 0.01460  305 ALA A C   
2290 O O   . ALA A  311 ? 0.15290 0.18360 0.23540 -0.01890 -0.00540 0.01200  305 ALA A O   
2291 C CB  . ALA A  311 ? 0.16850 0.18440 0.24810 -0.01360 -0.00170 0.01820  305 ALA A CB  
2292 N N   . VAL A  312 ? 0.14010 0.17020 0.21590 -0.01210 -0.00460 0.01460  306 VAL A N   
2293 C CA  . VAL A  312 ? 0.17070 0.20560 0.24350 -0.01120 -0.00630 0.01200  306 VAL A CA  
2294 C C   . VAL A  312 ? 0.17750 0.22090 0.25320 -0.01210 -0.00820 0.01220  306 VAL A C   
2295 O O   . VAL A  312 ? 0.16450 0.21290 0.24080 -0.01370 -0.01090 0.00910  306 VAL A O   
2296 C CB  . VAL A  312 ? 0.18010 0.21500 0.24880 -0.00710 -0.00530 0.01390  306 VAL A CB  
2297 C CG1 . VAL A  312 ? 0.19100 0.23180 0.25560 -0.00520 -0.00700 0.01300  306 VAL A CG1 
2298 C CG2 . VAL A  312 ? 0.21910 0.24850 0.28650 -0.00580 -0.00310 0.01340  306 VAL A CG2 
2299 N N   . VAL A  313 ? 0.16720 0.21290 0.24430 -0.01050 -0.00700 0.01560  307 VAL A N   
2300 C CA  . VAL A  313 ? 0.18530 0.24000 0.26600 -0.01000 -0.00780 0.01650  307 VAL A CA  
2301 C C   . VAL A  313 ? 0.17190 0.23120 0.25990 -0.01500 -0.00850 0.01520  307 VAL A C   
2302 O O   . VAL A  313 ? 0.16780 0.23650 0.26040 -0.01620 -0.01110 0.01390  307 VAL A O   
2303 C CB  . VAL A  313 ? 0.12940 0.18340 0.20910 -0.00690 -0.00550 0.01990  307 VAL A CB  
2304 C CG1 . VAL A  313 ? 0.18120 0.24520 0.26630 -0.00580 -0.00490 0.02120  307 VAL A CG1 
2305 C CG2 . VAL A  313 ? 0.17970 0.22890 0.25380 -0.00290 -0.00550 0.02100  307 VAL A CG2 
2306 N N   . THR A  314 ? 0.15460 0.20770 0.24460 -0.01820 -0.00640 0.01590  308 THR A N   
2307 C CA  . THR A  314 ? 0.15020 0.20660 0.24850 -0.02370 -0.00640 0.01540  308 THR A CA  
2308 C C   . THR A  314 ? 0.17190 0.22730 0.27130 -0.02750 -0.01040 0.00990  308 THR A C   
2309 O O   . THR A  314 ? 0.19000 0.25270 0.29720 -0.03210 -0.01290 0.00820  308 THR A O   
2310 C CB  . THR A  314 ? 0.15960 0.20830 0.25900 -0.02580 -0.00270 0.01850  308 THR A CB  
2311 O OG1 . THR A  314 ? 0.17550 0.22330 0.27020 -0.02140 0.00010  0.02250  308 THR A OG1 
2312 C CG2 . THR A  314 ? 0.18820 0.24220 0.29780 -0.03130 -0.00140 0.02010  308 THR A CG2 
2313 N N   . GLU A  315 ? 0.17180 0.21850 0.26350 -0.02570 -0.01100 0.00700  309 GLU A N   
2314 C CA  . GLU A  315 ? 0.21250 0.25720 0.30190 -0.02810 -0.01480 0.00070  309 GLU A CA  
2315 C C   . GLU A  315 ? 0.16240 0.21860 0.25090 -0.02690 -0.01930 -0.00120 309 GLU A C   
2316 O O   . GLU A  315 ? 0.19010 0.25020 0.28110 -0.03100 -0.02410 -0.00600 309 GLU A O   
2317 C CB  . GLU A  315 ? 0.19660 0.23070 0.27700 -0.02470 -0.01330 -0.00150 309 GLU A CB  
2318 C CG  . GLU A  315 ? 0.18800 0.21820 0.26220 -0.02560 -0.01660 -0.00890 309 GLU A CG  
2319 C CD  . GLU A  315 ? 0.24190 0.26390 0.32010 -0.03170 -0.01800 -0.01370 309 GLU A CD  
2320 O OE1 . GLU A  315 ? 0.23630 0.25460 0.32260 -0.03530 -0.01570 -0.01030 309 GLU A OE1 
2321 O OE2 . GLU A  315 ? 0.25970 0.27790 0.33210 -0.03300 -0.02160 -0.02110 309 GLU A OE2 
2322 N N   . LEU A  316 ? 0.16160 0.22330 0.24700 -0.02150 -0.01840 0.00250  310 LEU A N   
2323 C CA  . LEU A  316 ? 0.18820 0.26050 0.27190 -0.01880 -0.02240 0.00210  310 LEU A CA  
2324 C C   . LEU A  316 ? 0.17930 0.26440 0.27460 -0.02220 -0.02520 0.00270  310 LEU A C   
2325 O O   . LEU A  316 ? 0.15200 0.24590 0.24900 -0.02370 -0.03100 -0.00050 310 LEU A O   
2326 C CB  . LEU A  316 ? 0.20420 0.27720 0.28310 -0.01210 -0.01980 0.00700  310 LEU A CB  
2327 C CG  . LEU A  316 ? 0.36950 0.44590 0.44030 -0.00660 -0.02170 0.00790  310 LEU A CG  
2328 C CD1 . LEU A  316 ? 0.34470 0.42180 0.40850 -0.00770 -0.02620 0.00260  310 LEU A CD1 
2329 C CD2 . LEU A  316 ? 0.28160 0.34910 0.34600 -0.00250 -0.01710 0.01150  310 LEU A CD2 
2330 N N   . LEU A  317 ? 0.17230 0.25930 0.27570 -0.02330 -0.02110 0.00690  311 LEU A N   
2331 C CA  . LEU A  317 ? 0.19610 0.29610 0.31280 -0.02680 -0.02220 0.00850  311 LEU A CA  
2332 C C   . LEU A  317 ? 0.22170 0.32260 0.34550 -0.03510 -0.02650 0.00360  311 LEU A C   
2333 O O   . LEU A  317 ? 0.22980 0.34400 0.36290 -0.03820 -0.03150 0.00220  311 LEU A O   
2334 C CB  . LEU A  317 ? 0.17350 0.27290 0.29540 -0.02630 -0.01560 0.01380  311 LEU A CB  
2335 C CG  . LEU A  317 ? 0.20600 0.30580 0.32200 -0.01820 -0.01220 0.01780  311 LEU A CG  
2336 C CD1 . LEU A  317 ? 0.19890 0.29750 0.31730 -0.01730 -0.00580 0.02220  311 LEU A CD1 
2337 C CD2 . LEU A  317 ? 0.18090 0.29370 0.29980 -0.01350 -0.01510 0.01890  311 LEU A CD2 
2338 N N   . GLU A  318 ? 0.17250 0.25900 0.29250 -0.03890 -0.02510 0.00070  312 GLU A N   
2339 C CA  . GLU A  318 ? 0.20350 0.28710 0.32870 -0.04700 -0.02950 -0.00500 312 GLU A CA  
2340 C C   . GLU A  318 ? 0.21650 0.30340 0.33480 -0.04670 -0.03730 -0.01200 312 GLU A C   
2341 O O   . GLU A  318 ? 0.21900 0.31470 0.34580 -0.05260 -0.04370 -0.01580 312 GLU A O   
2342 C CB  . GLU A  318 ? 0.23660 0.30200 0.35740 -0.04940 -0.02600 -0.00660 312 GLU A CB  
2343 C CG  . GLU A  318 ? 0.20770 0.26810 0.33580 -0.05880 -0.03010 -0.01250 312 GLU A CG  
2344 C CD  . GLU A  318 ? 0.31380 0.35620 0.44070 -0.06120 -0.02540 -0.01210 312 GLU A CD  
2345 O OE1 . GLU A  318 ? 0.32320 0.35300 0.43800 -0.05660 -0.02420 -0.01490 312 GLU A OE1 
2346 O OE2 . GLU A  318 ? 0.41760 0.45920 0.55630 -0.06730 -0.02270 -0.00830 312 GLU A OE2 
2347 N N   . ARG A  319 ? 0.19580 0.27690 0.29900 -0.03980 -0.03710 -0.01330 313 ARG A N   
2348 C CA  . ARG A  319 ? 0.25060 0.33460 0.34450 -0.03840 -0.04400 -0.01950 313 ARG A CA  
2349 C C   . ARG A  319 ? 0.21250 0.31560 0.31320 -0.03770 -0.05000 -0.01790 313 ARG A C   
2350 O O   . ARG A  319 ? 0.24850 0.35820 0.34920 -0.04110 -0.05820 -0.02370 313 ARG A O   
2351 C CB  . ARG A  319 ? 0.24100 0.31720 0.31810 -0.03030 -0.04120 -0.01910 313 ARG A CB  
2352 C CG  . ARG A  319 ? 0.27470 0.33440 0.34550 -0.02900 -0.03490 -0.01950 313 ARG A CG  
2353 C CD  . ARG A  319 ? 0.27240 0.32120 0.33330 -0.03040 -0.03720 -0.02790 313 ARG A CD  
2354 N NE  . ARG A  319 ? 0.26170 0.29620 0.31830 -0.02790 -0.03050 -0.02730 313 ARG A NE  
2355 C CZ  . ARG A  319 ? 0.24690 0.27490 0.29100 -0.02160 -0.02730 -0.02830 313 ARG A CZ  
2356 N NH1 . ARG A  319 ? 0.26800 0.30070 0.30040 -0.01720 -0.02970 -0.03030 313 ARG A NH1 
2357 N NH2 . ARG A  319 ? 0.25100 0.26790 0.29450 -0.01960 -0.02140 -0.02710 313 ARG A NH2 
2358 N N   . LEU A  320 ? 0.16630 0.27840 0.27280 -0.03300 -0.04620 -0.01030 314 LEU A N   
2359 C CA  . LEU A  320 ? 0.19240 0.32330 0.30660 -0.03040 -0.05060 -0.00730 314 LEU A CA  
2360 C C   . LEU A  320 ? 0.21120 0.35590 0.34530 -0.03790 -0.05350 -0.00700 314 LEU A C   
2361 O O   . LEU A  320 ? 0.17860 0.34140 0.32200 -0.03640 -0.05810 -0.00490 314 LEU A O   
2362 C CB  . LEU A  320 ? 0.15710 0.28990 0.26960 -0.02190 -0.04450 0.00050  314 LEU A CB  
2363 C CG  . LEU A  320 ? 0.20410 0.32600 0.29950 -0.01470 -0.04200 0.00160  314 LEU A CG  
2364 C CD1 . LEU A  320 ? 0.16220 0.28280 0.25800 -0.00830 -0.03560 0.00860  314 LEU A CD1 
2365 C CD2 . LEU A  320 ? 0.21160 0.34020 0.29760 -0.01060 -0.04880 -0.00020 314 LEU A CD2 
2366 N N   . GLY A  321 ? 0.20020 0.33730 0.34210 -0.04560 -0.05040 -0.00820 315 GLY A N   
2367 C CA  . GLY A  321 ? 0.24030 0.39010 0.40280 -0.05350 -0.05180 -0.00680 315 GLY A CA  
2368 C C   . GLY A  321 ? 0.23390 0.39650 0.40850 -0.04970 -0.04530 0.00190  315 GLY A C   
2369 O O   . GLY A  321 ? 0.25700 0.43680 0.45000 -0.05400 -0.04710 0.00430  315 GLY A O   
2370 N N   . ILE A  322 ? 0.25450 0.40930 0.41960 -0.04190 -0.03770 0.00670  316 ILE A N   
2371 C CA  . ILE A  322 ? 0.25180 0.41710 0.42500 -0.03660 -0.03130 0.01410  316 ILE A CA  
2372 C C   . ILE A  322 ? 0.27380 0.43470 0.45500 -0.04150 -0.02360 0.01790  316 ILE A C   
2373 O O   . ILE A  322 ? 0.30010 0.44370 0.47120 -0.04210 -0.01940 0.01750  316 ILE A O   
2374 C CB  . ILE A  322 ? 0.22970 0.38770 0.38800 -0.02590 -0.02780 0.01670  316 ILE A CB  
2375 C CG1 . ILE A  322 ? 0.22780 0.39520 0.38220 -0.02050 -0.03470 0.01550  316 ILE A CG1 
2376 C CG2 . ILE A  322 ? 0.22300 0.38430 0.38520 -0.02060 -0.01940 0.02310  316 ILE A CG2 
2377 C CD1 . ILE A  322 ? 0.22790 0.38410 0.36560 -0.01200 -0.03290 0.01670  316 ILE A CD1 
2378 N N   . GLY A  323 ? 0.26390 0.44120 0.46360 -0.04480 -0.02150 0.02210  317 GLY A N   
2379 C CA  . GLY A  323 ? 0.29220 0.46720 0.50110 -0.05050 -0.01430 0.02640  317 GLY A CA  
2380 C C   . GLY A  323 ? 0.34370 0.51540 0.56270 -0.06290 -0.01860 0.02260  317 GLY A C   
2381 O O   . GLY A  323 ? 0.39960 0.56560 0.61370 -0.06660 -0.02700 0.01520  317 GLY A O   
2382 N N   . SER A  324 ? 0.35760 0.53190 0.59020 -0.06920 -0.01240 0.02790  318 SER A N   
2383 C CA  . SER A  324 ? 0.34330 0.50950 0.58460 -0.08130 -0.01500 0.02500  318 SER A CA  
2384 C C   . SER A  324 ? 0.40850 0.54870 0.63300 -0.08100 -0.01180 0.02330  318 SER A C   
2385 O O   . SER A  324 ? 0.39000 0.52160 0.60040 -0.07280 -0.00570 0.02680  318 SER A O   
2386 C CB  . SER A  324 ? 0.36790 0.54650 0.63140 -0.08840 -0.00870 0.03270  318 SER A CB  
2387 O OG  . SER A  324 ? 0.34140 0.51440 0.59800 -0.08240 0.00280  0.04070  318 SER A OG  
2388 N N   . PRO A  325 ? 0.47820 0.60540 0.70410 -0.08980 -0.01610 0.01790  319 PRO A N   
2389 C CA  . PRO A  325 ? 0.51050 0.61390 0.72420 -0.08970 -0.01160 0.01820  319 PRO A CA  
2390 C C   . PRO A  325 ? 0.47670 0.57740 0.69140 -0.08740 -0.00070 0.02850  319 PRO A C   
2391 O O   . PRO A  325 ? 0.41170 0.49860 0.61080 -0.08080 0.00340  0.03040  319 PRO A O   
2392 C CB  . PRO A  325 ? 0.50930 0.60300 0.73150 -0.10130 -0.01700 0.01220  319 PRO A CB  
2393 C CG  . PRO A  325 ? 0.49260 0.59960 0.71930 -0.10380 -0.02770 0.00420  319 PRO A CG  
2394 C CD  . PRO A  325 ? 0.46470 0.59660 0.70090 -0.09910 -0.02630 0.01010  319 PRO A CD  
2395 N N   . ASP A  326 ? 0.40490 0.51980 0.63760 -0.09240 0.00410  0.03550  320 ASP A N   
2396 C CA  . ASP A  326 ? 0.41660 0.52940 0.64850 -0.08960 0.01520  0.04580  320 ASP A CA  
2397 C C   . ASP A  326 ? 0.36780 0.48470 0.58480 -0.07690 0.01950  0.04870  320 ASP A C   
2398 O O   . ASP A  326 ? 0.34640 0.45120 0.54950 -0.07140 0.02510  0.05270  320 ASP A O   
2399 C CB  . ASP A  326 ? 0.40130 0.53030 0.65690 -0.09770 0.02030  0.05320  320 ASP A CB  
2400 C CG  . ASP A  326 ? 0.49710 0.61570 0.76630 -0.11100 0.01880  0.05280  320 ASP A CG  
2401 O OD1 . ASP A  326 ? 0.45740 0.55330 0.71570 -0.11190 0.02010  0.05240  320 ASP A OD1 
2402 O OD2 . ASP A  326 ? 0.57280 0.70420 0.85920 -0.11920 0.01620  0.05180  320 ASP A OD2 
2403 N N   . VAL A  327 ? 0.31570 0.44850 0.53480 -0.07190 0.01620  0.04630  321 VAL A N   
2404 C CA  . VAL A  327 ? 0.28680 0.42130 0.49160 -0.06000 0.01960  0.04790  321 VAL A CA  
2405 C C   . VAL A  327 ? 0.32480 0.44020 0.50850 -0.05480 0.01670  0.04330  321 VAL A C   
2406 O O   . VAL A  327 ? 0.29750 0.40390 0.46810 -0.04880 0.02160  0.04650  321 VAL A O   
2407 C CB  . VAL A  327 ? 0.27510 0.42850 0.48660 -0.05560 0.01590  0.04600  321 VAL A CB  
2408 C CG1 . VAL A  327 ? 0.26940 0.41910 0.46370 -0.04370 0.01750  0.04550  321 VAL A CG1 
2409 C CG2 . VAL A  327 ? 0.32990 0.50490 0.56270 -0.05830 0.02110  0.05260  321 VAL A CG2 
2410 N N   . ARG A  328 ? 0.27300 0.38280 0.45360 -0.05710 0.00850  0.03560  322 ARG A N   
2411 C CA  . ARG A  328 ? 0.31900 0.41260 0.48190 -0.05220 0.00630  0.03180  322 ARG A CA  
2412 C C   . ARG A  328 ? 0.33320 0.41010 0.48980 -0.05360 0.01050  0.03480  322 ARG A C   
2413 O O   . ARG A  328 ? 0.33790 0.40460 0.48070 -0.04760 0.01140  0.03490  322 ARG A O   
2414 C CB  . ARG A  328 ? 0.38770 0.47860 0.54830 -0.05440 -0.00210 0.02340  322 ARG A CB  
2415 C CG  . ARG A  328 ? 0.35740 0.46190 0.51770 -0.04960 -0.00680 0.02090  322 ARG A CG  
2416 C CD  . ARG A  328 ? 0.31360 0.41350 0.46720 -0.05050 -0.01460 0.01300  322 ARG A CD  
2417 N NE  . ARG A  328 ? 0.35070 0.44630 0.51170 -0.05980 -0.01850 0.00850  322 ARG A NE  
2418 C CZ  . ARG A  328 ? 0.38600 0.49370 0.55870 -0.06570 -0.02470 0.00520  322 ARG A CZ  
2419 N NH1 . ARG A  328 ? 0.35530 0.48070 0.53270 -0.06230 -0.02800 0.00600  322 ARG A NH1 
2420 N NH2 . ARG A  328 ? 0.37710 0.47890 0.55730 -0.07520 -0.02800 0.00090  322 ARG A NH2 
2421 N N   . SER A  329 ? 0.33910 0.41310 0.50630 -0.06140 0.01310  0.03790  323 SER A N   
2422 C CA  . SER A  329 ? 0.35320 0.41020 0.51420 -0.06210 0.01680  0.04130  323 SER A CA  
2423 C C   . SER A  329 ? 0.33760 0.39320 0.48850 -0.05500 0.02350  0.04870  323 SER A C   
2424 O O   . SER A  329 ? 0.29960 0.34140 0.44140 -0.05290 0.02530  0.05130  323 SER A O   
2425 C CB  . SER A  329 ? 0.36510 0.41840 0.54030 -0.07220 0.01880  0.04400  323 SER A CB  
2426 O OG  . SER A  329 ? 0.38750 0.45300 0.57370 -0.07440 0.02560  0.05240  323 SER A OG  
2427 N N   . GLN A  330 ? 0.24730 0.31670 0.39920 -0.05090 0.02700  0.05190  324 GLN A N   
2428 C CA  . GLN A  330 ? 0.28950 0.35700 0.42790 -0.04270 0.03200  0.05660  324 GLN A CA  
2429 C C   . GLN A  330 ? 0.28380 0.34160 0.40620 -0.03610 0.02750  0.05200  324 GLN A C   
2430 O O   . GLN A  330 ? 0.29470 0.34670 0.40450 -0.03050 0.02990  0.05510  324 GLN A O   
2431 C CB  . GLN A  330 ? 0.27690 0.36050 0.41880 -0.03860 0.03610  0.05900  324 GLN A CB  
2432 C CG  . GLN A  330 ? 0.21510 0.31120 0.37460 -0.04460 0.04190  0.06500  324 GLN A CG  
2433 C CD  . GLN A  330 ? 0.30780 0.42080 0.47150 -0.03920 0.04770  0.06860  324 GLN A CD  
2434 O OE1 . GLN A  330 ? 0.31440 0.42620 0.46390 -0.03000 0.05000  0.06840  324 GLN A OE1 
2435 N NE2 . GLN A  330 ? 0.27880 0.40790 0.46300 -0.04500 0.04990  0.07160  324 GLN A NE2 
2436 N N   . LEU A  331 ? 0.25290 0.30920 0.37550 -0.03670 0.02090  0.04500  325 LEU A N   
2437 C CA  . LEU A  331 ? 0.27580 0.32430 0.38580 -0.03120 0.01720  0.04140  325 LEU A CA  
2438 C C   . LEU A  331 ? 0.24990 0.28550 0.35780 -0.03330 0.01430  0.03900  325 LEU A C   
2439 O O   . LEU A  331 ? 0.19330 0.22430 0.29440 -0.02990 0.01070  0.03530  325 LEU A O   
2440 C CB  . LEU A  331 ? 0.26770 0.32410 0.37760 -0.02840 0.01310  0.03630  325 LEU A CB  
2441 C CG  . LEU A  331 ? 0.24010 0.30930 0.35300 -0.02510 0.01600  0.03830  325 LEU A CG  
2442 C CD1 . LEU A  331 ? 0.24370 0.31900 0.35670 -0.02220 0.01140  0.03380  325 LEU A CD1 
2443 C CD2 . LEU A  331 ? 0.27490 0.34090 0.37660 -0.01880 0.02030  0.04180  325 LEU A CD2 
2444 N N   . ALA A  332 ? 0.29620 0.32580 0.41060 -0.03870 0.01640  0.04160  326 ALA A N   
2445 C CA  . ALA A  332 ? 0.27490 0.29120 0.38830 -0.04060 0.01410  0.03900  326 ALA A CA  
2446 C C   . ALA A  332 ? 0.27260 0.28070 0.37500 -0.03410 0.01350  0.04020  326 ALA A C   
2447 O O   . ALA A  332 ? 0.27720 0.27830 0.37730 -0.03270 0.01060  0.03600  326 ALA A O   
2448 C CB  . ALA A  332 ? 0.28670 0.29580 0.40820 -0.04680 0.01760  0.04310  326 ALA A CB  
2449 N N   . SER A  333 ? 0.25050 0.25970 0.34600 -0.02990 0.01610  0.04580  327 SER A N   
2450 C CA  . SER A  333 ? 0.25720 0.25980 0.34360 -0.02430 0.01440  0.04730  327 SER A CA  
2451 C C   . SER A  333 ? 0.27510 0.28130 0.35730 -0.02070 0.01000  0.04200  327 SER A C   
2452 O O   . SER A  333 ? 0.23490 0.23640 0.31360 -0.01740 0.00760  0.04160  327 SER A O   
2453 C CB  . SER A  333 ? 0.31950 0.32260 0.39810 -0.02100 0.01750  0.05420  327 SER A CB  
2454 O OG  . SER A  333 ? 0.37660 0.38860 0.45050 -0.01830 0.01730  0.05240  327 SER A OG  
2455 N N   . PHE A  334 ? 0.25920 0.27430 0.34290 -0.02110 0.00930  0.03860  328 PHE A N   
2456 C CA  . PHE A  334 ? 0.24340 0.26100 0.32430 -0.01830 0.00570  0.03410  328 PHE A CA  
2457 C C   . PHE A  334 ? 0.21760 0.23400 0.30290 -0.02040 0.00360  0.02910  328 PHE A C   
2458 O O   . PHE A  334 ? 0.20450 0.21930 0.28720 -0.01790 0.00150  0.02670  328 PHE A O   
2459 C CB  . PHE A  334 ? 0.23120 0.25750 0.31080 -0.01670 0.00590  0.03310  328 PHE A CB  
2460 C CG  . PHE A  334 ? 0.21750 0.24410 0.28960 -0.01320 0.00770  0.03640  328 PHE A CG  
2461 C CD1 . PHE A  334 ? 0.28040 0.30340 0.34480 -0.00940 0.00490  0.03540  328 PHE A CD1 
2462 C CD2 . PHE A  334 ? 0.25680 0.28740 0.32950 -0.01360 0.01220  0.04010  328 PHE A CD2 
2463 C CE1 . PHE A  334 ? 0.29050 0.31260 0.34590 -0.00610 0.00570  0.03710  328 PHE A CE1 
2464 C CE2 . PHE A  334 ? 0.25290 0.28340 0.31630 -0.00930 0.01430  0.04240  328 PHE A CE2 
2465 C CZ  . PHE A  334 ? 0.24120 0.26670 0.29490 -0.00550 0.01070  0.04040  328 PHE A CZ  
2466 N N   . HIS A  335 ? 0.23240 0.25010 0.32410 -0.02520 0.00410  0.02740  329 HIS A N   
2467 C CA  . HIS A  335 ? 0.23420 0.25090 0.32790 -0.02720 0.00150  0.02160  329 HIS A CA  
2468 C C   . HIS A  335 ? 0.24550 0.25100 0.33680 -0.02580 0.00150  0.02000  329 HIS A C   
2469 O O   . HIS A  335 ? 0.19770 0.20230 0.28590 -0.02340 0.00000  0.01590  329 HIS A O   
2470 C CB  . HIS A  335 ? 0.25190 0.27210 0.35380 -0.03350 0.00120  0.02000  329 HIS A CB  
2471 C CG  . HIS A  335 ? 0.25100 0.27140 0.35370 -0.03580 -0.00280 0.01300  329 HIS A CG  
2472 N ND1 . HIS A  335 ? 0.25890 0.28120 0.36940 -0.04250 -0.00470 0.01000  329 HIS A ND1 
2473 C CD2 . HIS A  335 ? 0.26130 0.28060 0.35740 -0.03250 -0.00520 0.00830  329 HIS A CD2 
2474 C CE1 . HIS A  335 ? 0.30010 0.32170 0.40730 -0.04300 -0.00900 0.00310  329 HIS A CE1 
2475 N NE2 . HIS A  335 ? 0.19840 0.21810 0.29630 -0.03660 -0.00880 0.00220  329 HIS A NE2 
2476 N N   . HIS A  336 ? 0.22090 0.21800 0.31370 -0.02650 0.00380  0.02370  330 HIS A N   
2477 C CA  . HIS A  336 ? 0.25360 0.23970 0.34480 -0.02390 0.00440  0.02340  330 HIS A CA  
2478 C C   . HIS A  336 ? 0.25820 0.24210 0.34700 -0.01990 0.00570  0.03020  330 HIS A C   
2479 O O   . HIS A  336 ? 0.30050 0.27830 0.39070 -0.02110 0.00790  0.03510  330 HIS A O   
2480 C CB  . HIS A  336 ? 0.24270 0.21840 0.33820 -0.02840 0.00530  0.02100  330 HIS A CB  
2481 C CG  . HIS A  336 ? 0.29330 0.27140 0.39000 -0.03240 0.00260  0.01330  330 HIS A CG  
2482 N ND1 . HIS A  336 ? 0.34990 0.33530 0.45240 -0.03860 0.00120  0.01240  330 HIS A ND1 
2483 C CD2 . HIS A  336 ? 0.33260 0.30870 0.42480 -0.03050 0.00060  0.00640  330 HIS A CD2 
2484 C CE1 . HIS A  336 ? 0.32360 0.31100 0.42530 -0.04070 -0.00250 0.00490  330 HIS A CE1 
2485 N NE2 . HIS A  336 ? 0.30340 0.28450 0.39750 -0.03570 -0.00270 0.00110  330 HIS A NE2 
2486 N N   . PRO A  337 ? 0.23410 0.22280 0.31950 -0.01540 0.00400  0.03090  331 PRO A N   
2487 C CA  . PRO A  337 ? 0.27200 0.26050 0.35440 -0.01200 0.00360  0.03680  331 PRO A CA  
2488 C C   . PRO A  337 ? 0.30500 0.28410 0.38900 -0.00960 0.00480  0.04050  331 PRO A C   
2489 O O   . PRO A  337 ? 0.32600 0.29870 0.41290 -0.00880 0.00570  0.03750  331 PRO A O   
2490 C CB  . PRO A  337 ? 0.32020 0.31500 0.40110 -0.00860 0.00070  0.03530  331 PRO A CB  
2491 C CG  . PRO A  337 ? 0.26940 0.26840 0.35130 -0.01010 0.00050  0.02990  331 PRO A CG  
2492 C CD  . PRO A  337 ? 0.21900 0.21430 0.30320 -0.01400 0.00210  0.02660  331 PRO A CD  
2493 N N   . GLN A  338 ? 0.33630 0.31370 0.41700 -0.00780 0.00500  0.04700  332 GLN A N   
2494 C CA  . GLN A  338 ? 0.33360 0.30190 0.41530 -0.00470 0.00610  0.05210  332 GLN A CA  
2495 C C   . GLN A  338 ? 0.29740 0.26640 0.38190 0.00070  0.00380  0.05130  332 GLN A C   
2496 O O   . GLN A  338 ? 0.29370 0.27170 0.37770 0.00250  0.00050  0.05040  332 GLN A O   
2497 C CB  . GLN A  338 ? 0.36950 0.33810 0.44500 -0.00290 0.00600  0.05990  332 GLN A CB  
2498 C CG  . GLN A  338 ? 0.48540 0.45600 0.55790 -0.00710 0.00920  0.06180  332 GLN A CG  
2499 C CD  . GLN A  338 ? 0.62250 0.58560 0.70150 -0.01260 0.01360  0.06180  332 GLN A CD  
2500 O OE1 . GLN A  338 ? 0.60810 0.56010 0.69060 -0.01210 0.01510  0.06380  332 GLN A OE1 
2501 N NE2 . GLN A  338 ? 0.59570 0.56490 0.67730 -0.01780 0.01550  0.05960  332 GLN A NE2 
2502 N N   . ARG A  339 ? 0.31060 0.27010 0.39890 0.00320  0.00600  0.05190  333 ARG A N   
2503 C CA  . ARG A  339 ? 0.34030 0.30070 0.43290 0.00950  0.00510  0.05220  333 ARG A CA  
2504 C C   . ARG A  339 ? 0.32420 0.27480 0.41810 0.01410  0.00640  0.05900  333 ARG A C   
2505 O O   . ARG A  339 ? 0.38910 0.32870 0.48610 0.01630  0.00970  0.05750  333 ARG A O   
2506 C CB  . ARG A  339 ? 0.33350 0.29190 0.42920 0.00960  0.00730  0.04490  333 ARG A CB  
2507 C CG  . ARG A  339 ? 0.23110 0.20100 0.32600 0.00740  0.00560  0.04000  333 ARG A CG  
2508 C CD  . ARG A  339 ? 0.30380 0.28470 0.40200 0.01090  0.00250  0.04310  333 ARG A CD  
2509 N NE  . ARG A  339 ? 0.32120 0.31120 0.41930 0.00870  0.00160  0.03900  333 ARG A NE  
2510 C CZ  . ARG A  339 ? 0.30480 0.30000 0.39890 0.00480  -0.00090 0.03840  333 ARG A CZ  
2511 N NH1 . ARG A  339 ? 0.31920 0.31260 0.40860 0.00260  -0.00230 0.04090  333 ARG A NH1 
2512 N NH2 . ARG A  339 ? 0.29830 0.30050 0.39310 0.00370  -0.00150 0.03560  333 ARG A NH2 
2513 N N   . VAL A  340 ? 0.32760 0.28050 0.41750 0.01590  0.00410  0.06630  334 VAL A N   
2514 C CA  . VAL A  340 ? 0.36440 0.30790 0.45430 0.02090  0.00520  0.07430  334 VAL A CA  
2515 C C   . VAL A  340 ? 0.36070 0.31400 0.45090 0.02730  -0.00020 0.07990  334 VAL A C   
2516 O O   . VAL A  340 ? 0.31750 0.28250 0.40410 0.02580  -0.00490 0.07900  334 VAL A O   
2517 C CB  . VAL A  340 ? 0.42490 0.35980 0.50900 0.01720  0.00820  0.07990  334 VAL A CB  
2518 C CG1 . VAL A  340 ? 0.37420 0.30820 0.45810 0.00860  0.01110  0.07390  334 VAL A CG1 
2519 C CG2 . VAL A  340 ? 0.45850 0.40020 0.53430 0.01990  0.00480  0.08760  334 VAL A CG2 
2520 N N   . ASN A  341 ? 0.31780 0.26610 0.41250 0.03450  0.00000  0.08540  335 ASN A N   
2521 C CA  . ASN A  341 ? 0.31080 0.27090 0.40940 0.04100  -0.00590 0.08980  335 ASN A CA  
2522 C C   . ASN A  341 ? 0.32910 0.28920 0.41900 0.04380  -0.00970 0.09900  335 ASN A C   
2523 O O   . ASN A  341 ? 0.25180 0.20340 0.33260 0.04050  -0.00670 0.10190  335 ASN A O   
2524 C CB  . ASN A  341 ? 0.29670 0.25470 0.40650 0.04850  -0.00370 0.09060  335 ASN A CB  
2525 C CG  . ASN A  341 ? 0.27980 0.22100 0.38940 0.05400  0.00060  0.09690  335 ASN A CG  
2526 O OD1 . ASN A  341 ? 0.34950 0.28160 0.45110 0.05280  0.00140  0.10280  335 ASN A OD1 
2527 N ND2 . ASN A  341 ? 0.28690 0.22320 0.40520 0.06060  0.00420  0.09600  335 ASN A ND2 
2528 N N   . THR A  342 ? 0.25820 0.22860 0.35100 0.05000  -0.01630 0.10400  336 THR A N   
2529 C CA  . THR A  342 ? 0.26900 0.24110 0.35190 0.05380  -0.02150 0.11270  336 THR A CA  
2530 C C   . THR A  342 ? 0.30020 0.25690 0.37880 0.05850  -0.01660 0.12200  336 THR A C   
2531 O O   . THR A  342 ? 0.29000 0.24600 0.35780 0.06170  -0.01950 0.13030  336 THR A O   
2532 C CB  . THR A  342 ? 0.26850 0.25600 0.35810 0.05970  -0.03060 0.11580  336 THR A CB  
2533 O OG1 . THR A  342 ? 0.26120 0.24770 0.36490 0.06690  -0.02840 0.11870  336 THR A OG1 
2534 C CG2 . THR A  342 ? 0.25170 0.25370 0.34510 0.05390  -0.03590 0.10730  336 THR A CG2 
2535 N N   . MET A  343 ? 0.30130 0.24480 0.38750 0.05930  -0.00940 0.12100  337 MET A N   
2536 C CA  . MET A  343 ? 0.33250 0.25860 0.41550 0.06290  -0.00420 0.12950  337 MET A CA  
2537 C C   . MET A  343 ? 0.35550 0.26690 0.43580 0.05450  0.00380  0.12570  337 MET A C   
2538 O O   . MET A  343 ? 0.35660 0.25050 0.43750 0.05580  0.00950  0.13090  337 MET A O   
2539 C CB  . MET A  343 ? 0.33840 0.25870 0.43250 0.07230  -0.00280 0.13270  337 MET A CB  
2540 C CG  . MET A  343 ? 0.32480 0.26190 0.42370 0.08080  -0.01120 0.13800  337 MET A CG  
2541 S SD  . MET A  343 ? 0.35450 0.29380 0.43940 0.08600  -0.01740 0.15170  337 MET A SD  
2542 C CE  . MET A  343 ? 0.35150 0.26820 0.43630 0.09370  -0.01000 0.16140  337 MET A CE  
2543 N N   . GLY A  344 ? 0.34200 0.26020 0.42040 0.04590  0.00390  0.11710  338 GLY A N   
2544 C CA  . GLY A  344 ? 0.40040 0.30900 0.47750 0.03710  0.01010  0.11320  338 GLY A CA  
2545 C C   . GLY A  344 ? 0.42180 0.31910 0.50780 0.03440  0.01460  0.10540  338 GLY A C   
2546 O O   . GLY A  344 ? 0.35750 0.24390 0.44380 0.02740  0.01940  0.10350  338 GLY A O   
2547 N N   . VAL A  345 ? 0.36050 0.26010 0.45360 0.03960  0.01330  0.10070  339 VAL A N   
2548 C CA  . VAL A  345 ? 0.34830 0.23640 0.44740 0.03840  0.01770  0.09250  339 VAL A CA  
2549 C C   . VAL A  345 ? 0.34560 0.24480 0.44550 0.03230  0.01630  0.08140  339 VAL A C   
2550 O O   . VAL A  345 ? 0.29020 0.20600 0.39050 0.03370  0.01200  0.08010  339 VAL A O   
2551 C CB  . VAL A  345 ? 0.32230 0.20660 0.42810 0.04910  0.01830  0.09420  339 VAL A CB  
2552 C CG1 . VAL A  345 ? 0.36170 0.23390 0.47120 0.04870  0.02300  0.08430  339 VAL A CG1 
2553 C CG2 . VAL A  345 ? 0.34180 0.21480 0.44700 0.05660  0.01930  0.10630  339 VAL A CG2 
2554 N N   . THR A  346 ? 0.35050 0.24040 0.45050 0.02540  0.01960  0.07370  340 THR A N   
2555 C CA  . THR A  346 ? 0.34490 0.24480 0.44490 0.02050  0.01830  0.06350  340 THR A CA  
2556 C C   . THR A  346 ? 0.31200 0.21410 0.41580 0.02720  0.01890  0.05840  340 THR A C   
2557 O O   . THR A  346 ? 0.31880 0.20650 0.42440 0.03110  0.02250  0.05610  340 THR A O   
2558 C CB  . THR A  346 ? 0.40070 0.29100 0.50000 0.01160  0.02050  0.05660  340 THR A CB  
2559 O OG1 . THR A  346 ? 0.47090 0.35780 0.56890 0.00580  0.02160  0.06280  340 THR A OG1 
2560 C CG2 . THR A  346 ? 0.35150 0.25440 0.44940 0.00690  0.01830  0.04770  340 THR A CG2 
2561 N N   . THR A  347 ? 0.30850 0.22770 0.41360 0.02840  0.01590  0.05650  341 THR A N   
2562 C CA  . THR A  347 ? 0.30780 0.23240 0.41780 0.03500  0.01720  0.05330  341 THR A CA  
2563 C C   . THR A  347 ? 0.31070 0.23870 0.41830 0.03140  0.01860  0.04350  341 THR A C   
2564 O O   . THR A  347 ? 0.25110 0.18100 0.36140 0.03710  0.02150  0.04020  341 THR A O   
2565 C CB  . THR A  347 ? 0.25440 0.19680 0.36970 0.03930  0.01290  0.05920  341 THR A CB  
2566 O OG1 . THR A  347 ? 0.32820 0.28280 0.44040 0.03280  0.00900  0.05750  341 THR A OG1 
2567 C CG2 . THR A  347 ? 0.33760 0.27870 0.45440 0.04410  0.01040  0.06910  341 THR A CG2 
2568 N N   . GLY A  348 ? 0.24120 0.17100 0.34380 0.02300  0.01700  0.03930  342 GLY A N   
2569 C CA  . GLY A  348 ? 0.22460 0.15820 0.32400 0.02040  0.01770  0.03080  342 GLY A CA  
2570 C C   . GLY A  348 ? 0.28490 0.22190 0.38010 0.01150  0.01510  0.02760  342 GLY A C   
2571 O O   . GLY A  348 ? 0.29850 0.23000 0.39320 0.00680  0.01450  0.03040  342 GLY A O   
2572 N N   . GLY A  349 ? 0.23510 0.18140 0.32760 0.00960  0.01420  0.02270  343 GLY A N   
2573 C CA  . GLY A  349 ? 0.24570 0.19600 0.33510 0.00220  0.01180  0.01940  343 GLY A CA  
2574 C C   . GLY A  349 ? 0.26580 0.22780 0.35260 0.00220  0.01070  0.01600  343 GLY A C   
2575 O O   . GLY A  349 ? 0.21260 0.18050 0.30080 0.00720  0.01200  0.01710  343 GLY A O   
2576 N N   . VAL A  350 ? 0.25550 0.22090 0.33930 -0.00340 0.00860  0.01240  344 VAL A N   
2577 C CA  A VAL A  350 ? 0.22860 0.20440 0.30920 -0.00360 0.00730  0.00990  344 VAL A CA  
2578 C CA  B VAL A  350 ? 0.22920 0.20500 0.30980 -0.00370 0.00730  0.00990  344 VAL A CA  
2579 C C   . VAL A  350 ? 0.26990 0.24210 0.34500 -0.00640 0.00640  0.00210  344 VAL A C   
2580 O O   . VAL A  350 ? 0.28870 0.25380 0.36460 -0.01110 0.00520  -0.00080 344 VAL A O   
2581 C CB  A VAL A  350 ? 0.24990 0.23520 0.33190 -0.00670 0.00470  0.01390  344 VAL A CB  
2582 C CB  B VAL A  350 ? 0.24940 0.23480 0.33130 -0.00680 0.00470  0.01380  344 VAL A CB  
2583 C CG1 A VAL A  350 ? 0.20520 0.19980 0.28390 -0.00700 0.00340  0.01170  344 VAL A CG1 
2584 C CG1 B VAL A  350 ? 0.27050 0.25820 0.35590 -0.00430 0.00450  0.02050  344 VAL A CG1 
2585 C CG2 A VAL A  350 ? 0.27120 0.25910 0.35670 -0.00380 0.00460  0.02050  344 VAL A CG2 
2586 C CG2 B VAL A  350 ? 0.23070 0.21490 0.31360 -0.01280 0.00320  0.01290  344 VAL A CG2 
2587 N N   . SER A  351 ? 0.22830 0.20510 0.29790 -0.00350 0.00700  -0.00130 345 SER A N   
2588 C CA  . SER A  351 ? 0.21860 0.19290 0.28060 -0.00490 0.00540  -0.00910 345 SER A CA  
2589 C C   . SER A  351 ? 0.25060 0.23660 0.30830 -0.00470 0.00360  -0.00890 345 SER A C   
2590 O O   . SER A  351 ? 0.20800 0.20170 0.26770 -0.00190 0.00520  -0.00340 345 SER A O   
2591 C CB  . SER A  351 ? 0.21620 0.18100 0.27140 0.00050  0.00900  -0.01440 345 SER A CB  
2592 O OG  . SER A  351 ? 0.31980 0.27290 0.37910 0.00210  0.01150  -0.01370 345 SER A OG  
2593 N N   . PHE A  352 ? 0.23140 0.21860 0.28360 -0.00770 -0.00010 -0.01470 346 PHE A N   
2594 C CA  . PHE A  352 ? 0.21290 0.21120 0.26090 -0.00730 -0.00250 -0.01410 346 PHE A CA  
2595 C C   . PHE A  352 ? 0.27090 0.26780 0.30640 -0.00450 -0.00350 -0.02070 346 PHE A C   
2596 O O   . PHE A  352 ? 0.25270 0.25210 0.28440 -0.00800 -0.00890 -0.02580 346 PHE A O   
2597 C CB  . PHE A  352 ? 0.19530 0.20060 0.24910 -0.01320 -0.00740 -0.01340 346 PHE A CB  
2598 C CG  . PHE A  352 ? 0.19370 0.19980 0.25750 -0.01560 -0.00620 -0.00740 346 PHE A CG  
2599 C CD1 . PHE A  352 ? 0.19160 0.20370 0.25780 -0.01310 -0.00450 -0.00100 346 PHE A CD1 
2600 C CD2 . PHE A  352 ? 0.23610 0.23630 0.30600 -0.02050 -0.00670 -0.00810 346 PHE A CD2 
2601 C CE1 . PHE A  352 ? 0.20060 0.21270 0.27330 -0.01470 -0.00370 0.00380  346 PHE A CE1 
2602 C CE2 . PHE A  352 ? 0.24150 0.24230 0.31850 -0.02210 -0.00500 -0.00210 346 PHE A CE2 
2603 C CZ  . PHE A  352 ? 0.16840 0.17520 0.24580 -0.01890 -0.00370 0.00350  346 PHE A CZ  
2604 N N   . PRO A  353 ? 0.25800 0.25220 0.28680 0.00190  0.00160  -0.02060 347 PRO A N   
2605 C CA  . PRO A  353 ? 0.27240 0.26390 0.28650 0.00550  0.00150  -0.02730 347 PRO A CA  
2606 C C   . PRO A  353 ? 0.30740 0.30960 0.31400 0.00670  -0.00140 -0.02590 347 PRO A C   
2607 O O   . PRO A  353 ? 0.40810 0.40980 0.40060 0.01060  -0.00130 -0.03020 347 PRO A O   
2608 C CB  . PRO A  353 ? 0.31590 0.30290 0.32710 0.01290  0.00960  -0.02560 347 PRO A CB  
2609 C CG  . PRO A  353 ? 0.23820 0.23150 0.26290 0.01310  0.01270  -0.01590 347 PRO A CG  
2610 C CD  . PRO A  353 ? 0.21870 0.21150 0.25340 0.00630  0.00780  -0.01480 347 PRO A CD  
2611 N N   . PHE A  354 ? 0.33980 0.35140 0.35460 0.00400  -0.00380 -0.01980 348 PHE A N   
2612 C CA  . PHE A  354 ? 0.31070 0.33170 0.31860 0.00610  -0.00630 -0.01760 348 PHE A CA  
2613 C C   . PHE A  354 ? 0.34980 0.37380 0.35280 0.00240  -0.01460 -0.02450 348 PHE A C   
2614 O O   . PHE A  354 ? 0.30730 0.32680 0.31520 -0.00330 -0.01850 -0.03030 348 PHE A O   
2615 C CB  . PHE A  354 ? 0.25210 0.28070 0.26970 0.00560  -0.00560 -0.00900 348 PHE A CB  
2616 C CG  . PHE A  354 ? 0.30160 0.33220 0.33150 -0.00020 -0.00900 -0.00810 348 PHE A CG  
2617 C CD1 . PHE A  354 ? 0.22540 0.26180 0.25720 -0.00400 -0.01530 -0.01110 348 PHE A CD1 
2618 C CD2 . PHE A  354 ? 0.25330 0.28130 0.29320 -0.00150 -0.00590 -0.00370 348 PHE A CD2 
2619 C CE1 . PHE A  354 ? 0.28800 0.32730 0.33160 -0.00870 -0.01700 -0.00940 348 PHE A CE1 
2620 C CE2 . PHE A  354 ? 0.24670 0.27670 0.29580 -0.00580 -0.00820 -0.00230 348 PHE A CE2 
2621 C CZ  . PHE A  354 ? 0.26520 0.30070 0.31630 -0.00940 -0.01300 -0.00490 348 PHE A CZ  
2622 N N   . LYS A  355 ? 0.31200 0.34390 0.30550 0.00570  -0.01750 -0.02360 349 LYS A N   
2623 C CA  . LYS A  355 ? 0.33310 0.37100 0.32300 0.00250  -0.02650 -0.02920 349 LYS A CA  
2624 C C   . LYS A  355 ? 0.29440 0.34500 0.28550 0.00510  -0.02900 -0.02210 349 LYS A C   
2625 O O   . LYS A  355 ? 0.29020 0.34260 0.27230 0.01150  -0.02510 -0.01680 349 LYS A O   
2626 C CB  . LYS A  355 ? 0.38820 0.42080 0.35970 0.00520  -0.02930 -0.03810 349 LYS A CB  
2627 C CG  . LYS A  355 ? 0.43180 0.44950 0.40030 0.00410  -0.02600 -0.04570 349 LYS A CG  
2628 C CD  . LYS A  355 ? 0.46220 0.47300 0.40900 0.01030  -0.02470 -0.05260 349 LYS A CD  
2629 C CE  . LYS A  355 ? 0.46560 0.47910 0.40060 0.00780  -0.03550 -0.06190 349 LYS A CE  
2630 N NZ  . LYS A  355 ? 0.55090 0.54960 0.46980 0.00920  -0.03610 -0.07420 349 LYS A NZ  
2631 N N   . LEU A  356 ? 0.29920 0.35850 0.30220 0.00040  -0.03480 -0.02150 350 LEU A N   
2632 C CA  . LEU A  356 ? 0.29750 0.36910 0.30260 0.00340  -0.03780 -0.01530 350 LEU A CA  
2633 C C   . LEU A  356 ? 0.32190 0.39840 0.31070 0.00830  -0.04260 -0.01730 350 LEU A C   
2634 O O   . LEU A  356 ? 0.34090 0.41800 0.32310 0.00570  -0.04950 -0.02580 350 LEU A O   
2635 C CB  . LEU A  356 ? 0.25480 0.33600 0.27540 -0.00240 -0.04350 -0.01580 350 LEU A CB  
2636 C CG  . LEU A  356 ? 0.33820 0.42000 0.37390 -0.00420 -0.03870 -0.00980 350 LEU A CG  
2637 C CD1 . LEU A  356 ? 0.33980 0.43310 0.39000 -0.00910 -0.04380 -0.01010 350 LEU A CD1 
2638 C CD2 . LEU A  356 ? 0.26260 0.34590 0.29520 0.00270  -0.03440 -0.00140 350 LEU A CD2 
2639 N N   . ARG A  357 ? 0.28790 0.36740 0.26920 0.01530  -0.03940 -0.00960 351 ARG A N   
2640 C CA  . ARG A  357 ? 0.32530 0.41100 0.29070 0.02060  -0.04470 -0.01030 351 ARG A CA  
2641 C C   . ARG A  357 ? 0.32950 0.42940 0.30280 0.02170  -0.05140 -0.00580 351 ARG A C   
2642 O O   . ARG A  357 ? 0.31420 0.41670 0.29980 0.02250  -0.04800 0.00170  351 ARG A O   
2643 C CB  . ARG A  357 ? 0.38990 0.47050 0.33960 0.02850  -0.03720 -0.00450 351 ARG A CB  
2644 C CG  . ARG A  357 ? 0.38700 0.46580 0.34410 0.03150  -0.02930 0.00640  351 ARG A CG  
2645 C CD  . ARG A  357 ? 0.49850 0.57100 0.44150 0.03770  -0.02060 0.01120  351 ARG A CD  
2646 N NE  . ARG A  357 ? 0.48750 0.55990 0.43500 0.04130  -0.01490 0.02280  351 ARG A NE  
2647 C CZ  . ARG A  357 ? 0.40240 0.46910 0.36230 0.03900  -0.00790 0.02760  351 ARG A CZ  
2648 N NH1 . ARG A  357 ? 0.35380 0.41490 0.32160 0.03430  -0.00490 0.02280  351 ARG A NH1 
2649 N NH2 . ARG A  357 ? 0.42930 0.49530 0.39360 0.04160  -0.00420 0.03730  351 ARG A NH2 
2650 N N   . GLY A  358 ? 0.31140 0.42050 0.27790 0.02160  -0.06150 -0.01090 352 GLY A N   
2651 C CA  . GLY A  358 ? 0.35920 0.48400 0.33380 0.02320  -0.06900 -0.00690 352 GLY A CA  
2652 C C   . GLY A  358 ? 0.45760 0.58580 0.41980 0.03330  -0.06730 0.00250  352 GLY A C   
2653 O O   . GLY A  358 ? 0.48930 0.61250 0.43130 0.03840  -0.06590 0.00230  352 GLY A O   
2654 N N   . ILE B  2   ? 0.97180 0.68320 0.75310 0.08870  0.08410  0.10450  -4  ILE B N   
2655 C CA  . ILE B  2   ? 0.90910 0.64640 0.67760 0.08910  0.06610  0.09830  -4  ILE B CA  
2656 C C   . ILE B  2   ? 0.92250 0.63100 0.67170 0.07900  0.09170  0.09690  -4  ILE B C   
2657 O O   . ILE B  2   ? 0.89510 0.55830 0.62690 0.08140  0.12550  0.10820  -4  ILE B O   
2658 C CB  . ILE B  2   ? 0.96720 0.74870 0.77420 0.07130  0.03860  0.07610  -4  ILE B CB  
2659 C CG1 . ILE B  2   ? 0.88520 0.66360 0.72820 0.04690  0.04910  0.06070  -4  ILE B CG1 
2660 C CG2 . ILE B  2   ? 0.99500 0.80920 0.81390 0.08490  0.01170  0.07720  -4  ILE B CG2 
2661 C CD1 . ILE B  2   ? 0.77520 0.55200 0.62340 0.02760  0.06010  0.04580  -4  ILE B CD1 
2662 N N   . ASP B  3   ? 0.70230 0.43530 0.45650 0.06670  0.07830  0.08200  -3  ASP B N   
2663 C CA  . ASP B  3   ? 0.67950 0.39230 0.41030 0.06090  0.09720  0.08100  -3  ASP B CA  
2664 C C   . ASP B  3   ? 0.63060 0.35580 0.39390 0.03140  0.09910  0.05600  -3  ASP B C   
2665 O O   . ASP B  3   ? 0.55490 0.31750 0.33800 0.02410  0.07400  0.04220  -3  ASP B O   
2666 C CB  . ASP B  3   ? 0.65450 0.38980 0.35400 0.07950  0.07870  0.08740  -3  ASP B CB  
2667 C CG  . ASP B  3   ? 0.72020 0.43190 0.38710 0.07890  0.09970  0.09110  -3  ASP B CG  
2668 O OD1 . ASP B  3   ? 0.65940 0.33990 0.33380 0.05970  0.12760  0.08460  -3  ASP B OD1 
2669 O OD2 . ASP B  3   ? 0.70430 0.43210 0.33860 0.09820  0.08890  0.09880  -3  ASP B OD2 
2670 N N   . PRO B  4   ? 0.60490 0.30170 0.37540 0.01460  0.12980  0.04790  -2  PRO B N   
2671 C CA  . PRO B  4   ? 0.54050 0.25740 0.34210 -0.01070 0.13040  0.02160  -2  PRO B CA  
2672 C C   . PRO B  4   ? 0.53230 0.26250 0.32110 -0.01430 0.12200  0.01500  -2  PRO B C   
2673 O O   . PRO B  4   ? 0.52260 0.27700 0.33660 -0.03080 0.11620  -0.00540 -2  PRO B O   
2674 C CB  . PRO B  4   ? 0.55530 0.23830 0.36390 -0.02580 0.17000  0.01270  -2  PRO B CB  
2675 C CG  . PRO B  4   ? 0.63030 0.27390 0.41840 -0.00930 0.18910  0.03540  -2  PRO B CG  
2676 C CD  . PRO B  4   ? 0.67670 0.32210 0.42660 0.01870  0.16870  0.06060  -2  PRO B CD  
2677 N N   . PHE B  5   ? 0.56250 0.27990 0.31210 0.00230  0.12200  0.03140  -1  PHE B N   
2678 C CA  . PHE B  5   ? 0.56610 0.29380 0.30190 -0.00210 0.11800  0.02400  -1  PHE B CA  
2679 C C   . PHE B  5   ? 0.53910 0.30790 0.27780 0.00640  0.08340  0.02100  -1  PHE B C   
2680 O O   . PHE B  5   ? 0.54310 0.32400 0.27010 0.00450  0.07810  0.01450  -1  PHE B O   
2681 C CB  . PHE B  5   ? 0.62920 0.31750 0.31930 0.00950  0.14490  0.04080  -1  PHE B CB  
2682 C CG  . PHE B  5   ? 0.66090 0.30370 0.35230 -0.00140 0.18570  0.04110  -1  PHE B CG  
2683 C CD1 . PHE B  5   ? 0.64780 0.28860 0.36390 -0.02810 0.20370  0.01690  -1  PHE B CD1 
2684 C CD2 . PHE B  5   ? 0.70570 0.31110 0.37860 0.01450  0.20690  0.06240  -1  PHE B CD2 
2685 C CE1 . PHE B  5   ? 0.67700 0.28000 0.40140 -0.04160 0.24450  0.01030  -1  PHE B CE1 
2686 C CE2 . PHE B  5   ? 0.73400 0.29560 0.41380 0.00180  0.24930  0.05900  -1  PHE B CE2 
2687 C CZ  . PHE B  5   ? 0.72050 0.28220 0.42770 -0.02780 0.26850  0.03100  -1  PHE B CZ  
2688 N N   . THR B  6   ? 0.51200 0.30320 0.26950 0.01370  0.06200  0.02280  0   THR B N   
2689 C CA  . THR B  6   ? 0.49980 0.33110 0.26930 0.01780  0.03310  0.01450  0   THR B CA  
2690 C C   . THR B  6   ? 0.43790 0.29110 0.25110 0.00710  0.01930  0.00280  0   THR B C   
2691 O O   . THR B  6   ? 0.44800 0.32820 0.27520 0.01290  -0.00080 -0.00090 0   THR B O   
2692 C CB  . THR B  6   ? 0.52900 0.37230 0.27310 0.04290  0.01980  0.02800  0   THR B CB  
2693 O OG1 . THR B  6   ? 0.51830 0.35360 0.27040 0.05180  0.01910  0.03910  0   THR B OG1 
2694 C CG2 . THR B  6   ? 0.56860 0.39120 0.26320 0.05980  0.03480  0.04360  0   THR B CG2 
2695 N N   . MET B  7   ? 0.42020 0.26450 0.25520 -0.00730 0.03170  -0.00430 1   MET B N   
2696 C CA  . MET B  7   ? 0.37490 0.23970 0.24700 -0.01370 0.02160  -0.01290 1   MET B CA  
2697 C C   . MET B  7   ? 0.40470 0.29510 0.29550 -0.01950 0.00890  -0.02580 1   MET B C   
2698 O O   . MET B  7   ? 0.35890 0.24990 0.24110 -0.02550 0.01290  -0.03340 1   MET B O   
2699 C CB  . MET B  7   ? 0.39260 0.25020 0.28150 -0.02560 0.03840  -0.02070 1   MET B CB  
2700 C CG  . MET B  7   ? 0.48840 0.31800 0.36710 -0.02340 0.05690  -0.01180 1   MET B CG  
2701 S SD  . MET B  7   ? 0.48630 0.31500 0.36350 -0.00620 0.04330  0.00550  1   MET B SD  
2702 C CE  . MET B  7   ? 0.43210 0.29410 0.35050 -0.01100 0.02680  -0.00470 1   MET B CE  
2703 N N   . THR B  8   ? 0.32060 0.22970 0.23750 -0.01760 -0.00360 -0.02820 2   THR B N   
2704 C CA  . THR B  8   ? 0.30290 0.23110 0.23780 -0.02100 -0.01170 -0.03870 2   THR B CA  
2705 C C   . THR B  8   ? 0.27370 0.21300 0.23920 -0.02190 -0.01210 -0.04110 2   THR B C   
2706 O O   . THR B  8   ? 0.27840 0.21690 0.25180 -0.01830 -0.01190 -0.03490 2   THR B O   
2707 C CB  . THR B  8   ? 0.32700 0.26880 0.26030 -0.01430 -0.02530 -0.04040 2   THR B CB  
2708 O OG1 . THR B  8   ? 0.31130 0.25800 0.25730 -0.00730 -0.03280 -0.03420 2   THR B OG1 
2709 C CG2 . THR B  8   ? 0.34280 0.28020 0.24070 -0.00740 -0.02620 -0.03640 2   THR B CG2 
2710 N N   . PRO B  9   ? 0.28460 0.23430 0.26670 -0.02470 -0.01110 -0.04930 3   PRO B N   
2711 C CA  . PRO B  9   ? 0.24020 0.19950 0.24770 -0.02020 -0.00900 -0.04800 3   PRO B CA  
2712 C C   . PRO B  9   ? 0.25460 0.21620 0.27570 -0.01430 -0.01560 -0.04150 3   PRO B C   
2713 O O   . PRO B  9   ? 0.21870 0.18540 0.25360 -0.00850 -0.01320 -0.03620 3   PRO B O   
2714 C CB  . PRO B  9   ? 0.27570 0.23970 0.29520 -0.02200 -0.00440 -0.05590 3   PRO B CB  
2715 C CG  . PRO B  9   ? 0.27800 0.23770 0.27770 -0.02990 -0.00200 -0.06340 3   PRO B CG  
2716 C CD  . PRO B  9   ? 0.28680 0.23840 0.26400 -0.03050 -0.00860 -0.05910 3   PRO B CD  
2717 N N   . SER B  10  ? 0.24360 0.20570 0.26130 -0.01460 -0.02380 -0.04350 4   SER B N   
2718 C CA  . SER B  10  ? 0.23470 0.20210 0.26730 -0.01000 -0.03020 -0.04070 4   SER B CA  
2719 C C   . SER B  10  ? 0.29600 0.25820 0.32120 -0.00470 -0.03280 -0.02950 4   SER B C   
2720 O O   . SER B  10  ? 0.24620 0.21250 0.28570 -0.00050 -0.03660 -0.02600 4   SER B O   
2721 C CB  . SER B  10  ? 0.30350 0.28180 0.33380 -0.01060 -0.03930 -0.05010 4   SER B CB  
2722 O OG  . SER B  10  ? 0.29570 0.27180 0.29620 -0.00570 -0.04600 -0.04490 4   SER B OG  
2723 N N   . GLU B  11  ? 0.24120 0.19350 0.24700 -0.00600 -0.02800 -0.02550 5   GLU B N   
2724 C CA  . GLU B  11  ? 0.28080 0.22520 0.28100 -0.00320 -0.02550 -0.01750 5   GLU B CA  
2725 C C   . GLU B  11  ? 0.22810 0.17880 0.24030 -0.00560 -0.01660 -0.02010 5   GLU B C   
2726 O O   . GLU B  11  ? 0.23150 0.17710 0.24070 -0.00660 -0.01050 -0.01860 5   GLU B O   
2727 C CB  . GLU B  11  ? 0.28830 0.21500 0.25930 -0.00270 -0.02090 -0.01280 5   GLU B CB  
2728 C CG  . GLU B  11  ? 0.34610 0.27400 0.30190 0.00670  -0.03160 -0.00800 5   GLU B CG  
2729 C CD  . GLU B  11  ? 0.36960 0.28270 0.29100 0.01080  -0.02590 -0.00300 5   GLU B CD  
2730 O OE1 . GLU B  11  ? 0.40590 0.31730 0.31950 0.00360  -0.02050 -0.00970 5   GLU B OE1 
2731 O OE2 . GLU B  11  ? 0.42650 0.32930 0.32730 0.02320  -0.02580 0.00880  5   GLU B OE2 
2732 N N   . ASP B  12  ? 0.22190 0.18600 0.24800 -0.00500 -0.01420 -0.02520 6   ASP B N   
2733 C CA  . ASP B  12  ? 0.21170 0.19280 0.24880 -0.00240 -0.00750 -0.02910 6   ASP B CA  
2734 C C   . ASP B  12  ? 0.21340 0.20510 0.26660 0.00630  -0.01050 -0.02250 6   ASP B C   
2735 O O   . ASP B  12  ? 0.21220 0.20820 0.27710 0.01370  -0.01110 -0.01780 6   ASP B O   
2736 C CB  . ASP B  12  ? 0.22040 0.21310 0.26190 -0.00030 -0.00300 -0.03500 6   ASP B CB  
2737 C CG  . ASP B  12  ? 0.23580 0.22390 0.26320 -0.00990 0.00260  -0.04490 6   ASP B CG  
2738 O OD1 . ASP B  12  ? 0.24930 0.22930 0.26670 -0.01720 0.00750  -0.04840 6   ASP B OD1 
2739 O OD2 . ASP B  12  ? 0.21920 0.20930 0.24640 -0.01030 0.00460  -0.04910 6   ASP B OD2 
2740 N N   . PHE B  13  ? 0.21440 0.20830 0.26870 0.00530  -0.00930 -0.02260 7   PHE B N   
2741 C CA  . PHE B  13  ? 0.19890 0.20180 0.26670 0.01250  -0.01250 -0.01660 7   PHE B CA  
2742 C C   . PHE B  13  ? 0.17120 0.19840 0.24750 0.01420  -0.00640 -0.02500 7   PHE B C   
2743 O O   . PHE B  13  ? 0.20540 0.23610 0.27800 0.00570  0.00130  -0.03700 7   PHE B O   
2744 C CB  . PHE B  13  ? 0.18950 0.17440 0.25350 0.01050  -0.01810 -0.00970 7   PHE B CB  
2745 C CG  . PHE B  13  ? 0.20690 0.18150 0.27000 0.01220  -0.02660 -0.00460 7   PHE B CG  
2746 C CD1 . PHE B  13  ? 0.20920 0.18960 0.28930 0.01750  -0.02990 -0.00090 7   PHE B CD1 
2747 C CD2 . PHE B  13  ? 0.24010 0.20210 0.28630 0.00860  -0.02970 -0.00560 7   PHE B CD2 
2748 C CE1 . PHE B  13  ? 0.22360 0.19980 0.30850 0.01680  -0.03580 -0.00230 7   PHE B CE1 
2749 C CE2 . PHE B  13  ? 0.24770 0.21010 0.29580 0.01030  -0.03820 -0.00630 7   PHE B CE2 
2750 C CZ  . PHE B  13  ? 0.28460 0.25540 0.35470 0.01320  -0.04100 -0.00670 7   PHE B CZ  
2751 N N   . VAL B  14  ? 0.17590 0.22090 0.26460 0.02470  -0.00820 -0.02050 8   VAL B N   
2752 C CA  . VAL B  14  ? 0.14670 0.21620 0.24530 0.02620  -0.00480 -0.02870 8   VAL B CA  
2753 C C   . VAL B  14  ? 0.17650 0.23320 0.28110 0.02700  -0.00960 -0.01910 8   VAL B C   
2754 O O   . VAL B  14  ? 0.14980 0.19540 0.25680 0.03320  -0.01480 -0.00680 8   VAL B O   
2755 C CB  . VAL B  14  ? 0.14270 0.25370 0.24880 0.04150  -0.00240 -0.03340 8   VAL B CB  
2756 C CG1 . VAL B  14  ? 0.16520 0.27290 0.27210 0.05800  -0.00400 -0.01590 8   VAL B CG1 
2757 C CG2 . VAL B  14  ? 0.12480 0.26910 0.24290 0.04340  0.00010  -0.04550 8   VAL B CG2 
2758 N N   . VAL B  15  ? 0.14260 0.19910 0.25140 0.01960  -0.00550 -0.02640 9   VAL B N   
2759 C CA  . VAL B  15  ? 0.15820 0.19560 0.26980 0.01860  -0.00920 -0.01760 9   VAL B CA  
2760 C C   . VAL B  15  ? 0.19380 0.25360 0.32060 0.01860  -0.00420 -0.02660 9   VAL B C   
2761 O O   . VAL B  15  ? 0.19120 0.26810 0.32380 0.01150  0.00600  -0.04390 9   VAL B O   
2762 C CB  . VAL B  15  ? 0.19530 0.19860 0.29250 0.01020  -0.00610 -0.01480 9   VAL B CB  
2763 C CG1 . VAL B  15  ? 0.19870 0.18620 0.29890 0.01210  -0.00820 -0.00660 9   VAL B CG1 
2764 C CG2 . VAL B  15  ? 0.21440 0.20100 0.29620 0.01110  -0.01260 -0.00760 9   VAL B CG2 
2765 N N   . THR B  16  ? 0.16790 0.22970 0.30340 0.02520  -0.01000 -0.01790 10  THR B N   
2766 C CA  . THR B  16  ? 0.16010 0.24070 0.31030 0.02410  -0.00540 -0.02660 10  THR B CA  
2767 C C   . THR B  16  ? 0.14970 0.19970 0.30020 0.01840  -0.00450 -0.02080 10  THR B C   
2768 O O   . THR B  16  ? 0.17690 0.20090 0.31850 0.02130  -0.01240 -0.00680 10  THR B O   
2769 C CB  . THR B  16  ? 0.14140 0.25110 0.30110 0.03760  -0.00980 -0.02220 10  THR B CB  
2770 O OG1 . THR B  16  ? 0.17150 0.25930 0.32990 0.04340  -0.01720 -0.00470 10  THR B OG1 
2771 C CG2 . THR B  16  ? 0.16500 0.30790 0.32090 0.04890  -0.00820 -0.02630 10  THR B CG2 
2772 N N   . ASP B  17  ? 0.14640 0.20220 0.30840 0.01120  0.00640  -0.03330 11  ASP B N   
2773 C CA  . ASP B  17  ? 0.17160 0.19650 0.33360 0.00820  0.01090  -0.02680 11  ASP B CA  
2774 C C   . ASP B  17  ? 0.16460 0.20930 0.34750 0.00770  0.01450  -0.03500 11  ASP B C   
2775 O O   . ASP B  17  ? 0.16470 0.24910 0.36170 0.00680  0.01760  -0.05100 11  ASP B O   
2776 C CB  . ASP B  17  ? 0.20760 0.20320 0.36120 -0.00190 0.02890  -0.03260 11  ASP B CB  
2777 C CG  . ASP B  17  ? 0.20980 0.22720 0.38230 -0.01490 0.04860  -0.05920 11  ASP B CG  
2778 O OD1 . ASP B  17  ? 0.22330 0.26720 0.39830 -0.01960 0.05150  -0.07480 11  ASP B OD1 
2779 O OD2 . ASP B  17  ? 0.21500 0.22710 0.40260 -0.02080 0.06230  -0.06750 11  ASP B OD2 
2780 N N   . ARG B  18  ? 0.18710 0.20700 0.37120 0.00970  0.01410  -0.02490 12  ARG B N   
2781 C CA  . ARG B  18  ? 0.16590 0.19610 0.36990 0.00730  0.02090  -0.03300 12  ARG B CA  
2782 C C   . ARG B  18  ? 0.18170 0.17370 0.38330 0.00150  0.03880  -0.03260 12  ARG B C   
2783 O O   . ARG B  18  ? 0.21620 0.17520 0.40310 0.01010  0.03450  -0.01390 12  ARG B O   
2784 C CB  . ARG B  18  ? 0.20230 0.23740 0.41150 0.01740  0.00560  -0.01990 12  ARG B CB  
2785 C CG  . ARG B  18  ? 0.18310 0.23240 0.41340 0.01590  0.01060  -0.02770 12  ARG B CG  
2786 C CD  . ARG B  18  ? 0.14990 0.20660 0.38440 0.02600  -0.00480 -0.01500 12  ARG B CD  
2787 N NE  . ARG B  18  ? 0.18970 0.27190 0.42090 0.03230  -0.01240 -0.01290 12  ARG B NE  
2788 C CZ  . ARG B  18  ? 0.20180 0.31440 0.42560 0.03350  -0.00900 -0.02040 12  ARG B CZ  
2789 N NH1 . ARG B  18  ? 0.10240 0.23190 0.33400 0.02840  -0.00160 -0.03340 12  ARG B NH1 
2790 N NH2 . ARG B  18  ? 0.15950 0.28540 0.36530 0.04150  -0.01180 -0.01360 12  ARG B NH2 
2791 N N   . GLY B  19  ? 0.18260 0.18020 0.39870 -0.01160 0.06090  -0.05400 13  GLY B N   
2792 C CA  . GLY B  19  ? 0.26870 0.22300 0.48290 -0.01700 0.08520  -0.05310 13  GLY B CA  
2793 C C   . GLY B  19  ? 0.24580 0.15850 0.43020 -0.01160 0.08880  -0.03530 13  GLY B C   
2794 O O   . GLY B  19  ? 0.30380 0.17330 0.47480 -0.00430 0.10100  -0.01960 13  GLY B O   
2795 N N   . GLY B  20  ? 0.25690 0.18260 0.42890 -0.01240 0.07860  -0.03620 14  GLY B N   
2796 C CA  . GLY B  20  ? 0.28940 0.18150 0.43270 -0.00760 0.08080  -0.02140 14  GLY B CA  
2797 C C   . GLY B  20  ? 0.29650 0.18160 0.41870 0.00930  0.05590  0.00230  14  GLY B C   
2798 O O   . GLY B  20  ? 0.31820 0.18410 0.41580 0.01480  0.05400  0.01330  14  GLY B O   
2799 N N   . ILE B  21  ? 0.21250 0.18030 0.26120 0.02170  -0.01840 0.00800  15  ILE B N   
2800 C CA  . ILE B  21  ? 0.26330 0.24360 0.32040 0.01810  -0.01110 0.01610  15  ILE B CA  
2801 C C   . ILE B  21  ? 0.21410 0.19850 0.26810 0.01640  -0.00840 0.01600  15  ILE B C   
2802 O O   . ILE B  21  ? 0.19800 0.17610 0.24030 0.02410  -0.00700 0.01260  15  ILE B O   
2803 C CB  . ILE B  21  ? 0.22670 0.20750 0.28250 0.02770  -0.00400 0.02180  15  ILE B CB  
2804 C CG1 . ILE B  21  ? 0.22760 0.20230 0.28460 0.03070  -0.00720 0.02090  15  ILE B CG1 
2805 C CG2 . ILE B  21  ? 0.19520 0.18920 0.26460 0.02280  0.00170  0.03180  15  ILE B CG2 
2806 C CD1 . ILE B  21  ? 0.23100 0.20120 0.28100 0.04420  -0.00060 0.02400  15  ILE B CD1 
2807 N N   . VAL B  22  ? 0.18990 0.18330 0.25290 0.00690  -0.00820 0.01960  16  VAL B N   
2808 C CA  . VAL B  22  ? 0.21450 0.21090 0.27500 0.00480  -0.00640 0.01930  16  VAL B CA  
2809 C C   . VAL B  22  ? 0.21130 0.20980 0.26960 0.01260  0.00070  0.02420  16  VAL B C   
2810 O O   . VAL B  22  ? 0.19190 0.19640 0.25890 0.01390  0.00500  0.03210  16  VAL B O   
2811 C CB  . VAL B  22  ? 0.20150 0.20470 0.27000 -0.00550 -0.00820 0.02210  16  VAL B CB  
2812 C CG1 . VAL B  22  ? 0.21980 0.22530 0.28590 -0.00680 -0.00640 0.02210  16  VAL B CG1 
2813 C CG2 . VAL B  22  ? 0.25110 0.25250 0.32020 -0.01140 -0.01330 0.01810  16  VAL B CG2 
2814 N N   . GLU B  23  ? 0.19490 0.18900 0.24270 0.01800  0.00210  0.02040  17  GLU B N   
2815 C CA  . GLU B  23  ? 0.19440 0.19090 0.23970 0.02570  0.00960  0.02600  17  GLU B CA  
2816 C C   . GLU B  23  ? 0.21440 0.21830 0.26760 0.01820  0.01000  0.02920  17  GLU B C   
2817 O O   . GLU B  23  ? 0.17210 0.18410 0.23860 0.01420  0.01210  0.03740  17  GLU B O   
2818 C CB  . GLU B  23  ? 0.21930 0.20530 0.24650 0.03720  0.01060  0.02040  17  GLU B CB  
2819 C CG  . GLU B  23  ? 0.27730 0.26550 0.30030 0.04760  0.02020  0.02750  17  GLU B CG  
2820 C CD  . GLU B  23  ? 0.24450 0.22890 0.26170 0.06030  0.02650  0.03170  17  GLU B CD  
2821 O OE1 . GLU B  23  ? 0.27050 0.24140 0.26980 0.06940  0.02340  0.02410  17  GLU B OE1 
2822 O OE2 . GLU B  23  ? 0.24290 0.23710 0.27340 0.06180  0.03420  0.04290  17  GLU B OE2 
2823 N N   . ASN B  24  ? 0.18640 0.18680 0.23220 0.01610  0.00690  0.02290  18  ASN B N   
2824 C CA  . ASN B  24  ? 0.15900 0.16410 0.20970 0.00970  0.00650  0.02440  18  ASN B CA  
2825 C C   . ASN B  24  ? 0.17540 0.17880 0.22540 0.00120  0.00010  0.01800  18  ASN B C   
2826 O O   . ASN B  24  ? 0.20240 0.20050 0.24680 0.00180  -0.00340 0.01190  18  ASN B O   
2827 C CB  . ASN B  24  ? 0.20620 0.20920 0.24870 0.01630  0.01020  0.02390  18  ASN B CB  
2828 C CG  . ASN B  24  ? 0.22550 0.22920 0.26570 0.02740  0.01820  0.03080  18  ASN B CG  
2829 O OD1 . ASN B  24  ? 0.17280 0.18330 0.22490 0.02780  0.02240  0.03980  18  ASN B OD1 
2830 N ND2 . ASN B  24  ? 0.26300 0.25940 0.28770 0.03740  0.02050  0.02720  18  ASN B ND2 
2831 N N   . SER B  25  ? 0.13710 0.14410 0.19250 -0.00590 -0.00140 0.01980  19  SER B N   
2832 C CA  . SER B  25  ? 0.17290 0.17780 0.22500 -0.01150 -0.00550 0.01430  19  SER B CA  
2833 C C   . SER B  25  ? 0.17940 0.18470 0.23030 -0.01320 -0.00510 0.01430  19  SER B C   
2834 O O   . SER B  25  ? 0.16350 0.17170 0.22010 -0.01330 -0.00360 0.01980  19  SER B O   
2835 C CB  . SER B  25  ? 0.22460 0.23060 0.28070 -0.01810 -0.00890 0.01510  19  SER B CB  
2836 O OG  . SER B  25  ? 0.19410 0.20230 0.25570 -0.02220 -0.01040 0.02000  19  SER B OG  
2837 N N   . HIS B  26  ? 0.16210 0.16470 0.20750 -0.01450 -0.00670 0.00880  20  HIS B N   
2838 C CA  . HIS B  26  ? 0.16640 0.16830 0.20920 -0.01480 -0.00620 0.00770  20  HIS B CA  
2839 C C   . HIS B  26  ? 0.14760 0.14770 0.18770 -0.01930 -0.00860 0.00430  20  HIS B C   
2840 O O   . HIS B  26  ? 0.17320 0.17250 0.21210 -0.01940 -0.00920 0.00120  20  HIS B O   
2841 C CB  . HIS B  26  ? 0.17220 0.17180 0.20920 -0.00870 -0.00450 0.00470  20  HIS B CB  
2842 C CG  . HIS B  26  ? 0.18220 0.18120 0.21700 -0.00140 -0.00140 0.00720  20  HIS B CG  
2843 N ND1 . HIS B  26  ? 0.15460 0.15510 0.18890 0.00350  0.00300  0.01170  20  HIS B ND1 
2844 C CD2 . HIS B  26  ? 0.16960 0.16600 0.20170 0.00290  -0.00160 0.00620  20  HIS B CD2 
2845 C CE1 . HIS B  26  ? 0.20630 0.20540 0.23650 0.01140  0.00640  0.01380  20  HIS B CE1 
2846 N NE2 . HIS B  26  ? 0.18770 0.18340 0.21560 0.01130  0.00310  0.00990  20  HIS B NE2 
2847 N N   . ARG B  27  ? 0.17520 0.17400 0.21450 -0.02240 -0.00990 0.00520  21  ARG B N   
2848 C CA  . ARG B  27  ? 0.17340 0.16900 0.20700 -0.02460 -0.01110 0.00220  21  ARG B CA  
2849 C C   . ARG B  27  ? 0.19220 0.18720 0.22290 -0.02220 -0.00920 -0.00130 21  ARG B C   
2850 O O   . ARG B  27  ? 0.18430 0.17930 0.21540 -0.02010 -0.00840 -0.00130 21  ARG B O   
2851 C CB  . ARG B  27  ? 0.20160 0.19290 0.23280 -0.02750 -0.01480 0.00360  21  ARG B CB  
2852 C CG  . ARG B  27  ? 0.20390 0.19350 0.23500 -0.03050 -0.01840 0.00600  21  ARG B CG  
2853 C CD  . ARG B  27  ? 0.22580 0.21490 0.25110 -0.03010 -0.01670 0.00410  21  ARG B CD  
2854 N NE  . ARG B  27  ? 0.24090 0.22770 0.25920 -0.02790 -0.01390 0.00080  21  ARG B NE  
2855 C CZ  . ARG B  27  ? 0.26410 0.24400 0.27260 -0.02720 -0.01550 -0.00100 21  ARG B CZ  
2856 N NH1 . ARG B  27  ? 0.20820 0.18110 0.21170 -0.02890 -0.02160 -0.00040 21  ARG B NH1 
2857 N NH2 . ARG B  27  ? 0.25680 0.23570 0.26060 -0.02430 -0.01180 -0.00330 21  ARG B NH2 
2858 N N   . VAL B  28  ? 0.19350 0.18810 0.22230 -0.02220 -0.00820 -0.00330 22  VAL B N   
2859 C CA  . VAL B  28  ? 0.20540 0.20010 0.23420 -0.02010 -0.00670 -0.00580 22  VAL B CA  
2860 C C   . VAL B  28  ? 0.18850 0.18010 0.21110 -0.02020 -0.00520 -0.00640 22  VAL B C   
2861 O O   . VAL B  28  ? 0.18270 0.17270 0.20130 -0.02090 -0.00460 -0.00520 22  VAL B O   
2862 C CB  . VAL B  28  ? 0.17420 0.17150 0.20930 -0.01940 -0.00680 -0.00610 22  VAL B CB  
2863 C CG1 . VAL B  28  ? 0.18070 0.17830 0.21860 -0.01750 -0.00630 -0.00770 22  VAL B CG1 
2864 C CG2 . VAL B  28  ? 0.22770 0.22500 0.26570 -0.01790 -0.00920 -0.00650 22  VAL B CG2 
2865 N N   . HIS B  29  ? 0.16460 0.15480 0.18550 -0.01860 -0.00450 -0.00820 23  HIS B N   
2866 C CA  . HIS B  29  ? 0.18330 0.17020 0.19830 -0.01690 -0.00230 -0.00920 23  HIS B CA  
2867 C C   . HIS B  29  ? 0.21260 0.20280 0.23340 -0.01470 0.00010  -0.00970 23  HIS B C   
2868 O O   . HIS B  29  ? 0.18830 0.18010 0.21350 -0.01430 -0.00160 -0.01090 23  HIS B O   
2869 C CB  . HIS B  29  ? 0.19450 0.17520 0.20260 -0.01710 -0.00470 -0.01060 23  HIS B CB  
2870 C CG  . HIS B  29  ? 0.21410 0.19130 0.22020 -0.01990 -0.00910 -0.00930 23  HIS B CG  
2871 N ND1 . HIS B  29  ? 0.22100 0.19220 0.21840 -0.02020 -0.01120 -0.00930 23  HIS B ND1 
2872 C CD2 . HIS B  29  ? 0.22240 0.20100 0.23450 -0.02200 -0.01220 -0.00710 23  HIS B CD2 
2873 C CE1 . HIS B  29  ? 0.23390 0.20270 0.23320 -0.02330 -0.01670 -0.00760 23  HIS B CE1 
2874 N NE2 . HIS B  29  ? 0.21240 0.18640 0.22210 -0.02450 -0.01680 -0.00560 23  HIS B NE2 
2875 N N   . ALA B  30  ? 0.19410 0.18530 0.21540 -0.01270 0.00400  -0.00820 24  ALA B N   
2876 C CA  . ALA B  30  ? 0.16350 0.15830 0.19340 -0.01070 0.00580  -0.00750 24  ALA B CA  
2877 C C   . ALA B  30  ? 0.20140 0.19540 0.22810 -0.00690 0.01170  -0.00540 24  ALA B C   
2878 O O   . ALA B  30  ? 0.21410 0.20600 0.23350 -0.00520 0.01520  -0.00330 24  ALA B O   
2879 C CB  . ALA B  30  ? 0.13730 0.13780 0.18120 -0.01190 0.00400  -0.00520 24  ALA B CB  
2880 N N   . ALA B  31  ? 0.19000 0.18560 0.22200 -0.00480 0.01320  -0.00530 25  ALA B N   
2881 C CA  . ALA B  31  ? 0.22090 0.21680 0.25230 0.00010  0.02000  -0.00220 25  ALA B CA  
2882 C C   . ALA B  31  ? 0.19910 0.20260 0.24900 0.00050  0.02060  0.00160  25  ALA B C   
2883 O O   . ALA B  31  ? 0.19250 0.19680 0.24890 -0.00170 0.01500  -0.00100 25  ALA B O   
2884 C CB  . ALA B  31  ? 0.20100 0.18870 0.21820 0.00310  0.02060  -0.00620 25  ALA B CB  
2885 N N   . VAL B  32  ? 0.18650 0.19540 0.24570 0.00370  0.02720  0.00850  26  VAL B N   
2886 C CA  . VAL B  32  ? 0.15050 0.16710 0.23060 0.00460  0.02830  0.01410  26  VAL B CA  
2887 C C   . VAL B  32  ? 0.19300 0.20970 0.26940 0.01180  0.03840  0.01850  26  VAL B C   
2888 O O   . VAL B  32  ? 0.21100 0.22700 0.27920 0.01650  0.04630  0.02260  26  VAL B O   
2889 C CB  . VAL B  32  ? 0.14560 0.16980 0.24580 0.00200  0.02690  0.02090  26  VAL B CB  
2890 C CG1 . VAL B  32  ? 0.21540 0.24700 0.34030 0.00230  0.02590  0.02730  26  VAL B CG1 
2891 C CG2 . VAL B  32  ? 0.16370 0.18540 0.26320 -0.00380 0.01720  0.01580  26  VAL B CG2 
2892 N N   . VAL B  33  ? 0.16970 0.18660 0.25020 0.01380  0.03850  0.01770  27  VAL B N   
2893 C CA  . VAL B  33  ? 0.18390 0.19890 0.25750 0.02170  0.04820  0.02070  27  VAL B CA  
2894 C C   . VAL B  33  ? 0.19260 0.21670 0.29000 0.02350  0.05060  0.02800  27  VAL B C   
2895 O O   . VAL B  33  ? 0.18010 0.20860 0.29500 0.01810  0.04220  0.02780  27  VAL B O   
2896 C CB  . VAL B  33  ? 0.19500 0.19870 0.24640 0.02360  0.04640  0.01210  27  VAL B CB  
2897 C CG1 . VAL B  33  ? 0.18640 0.18100 0.21760 0.02080  0.04170  0.00550  27  VAL B CG1 
2898 C CG2 . VAL B  33  ? 0.19560 0.20010 0.25540 0.01940  0.03870  0.00800  27  VAL B CG2 
2899 N N   . ASP B  34  ? 0.18440 0.20990 0.28100 0.03200  0.06200  0.03440  28  ASP B N   
2900 C CA  . ASP B  34  ? 0.18750 0.22190 0.30790 0.03450  0.06520  0.04230  28  ASP B CA  
2901 C C   . ASP B  34  ? 0.27920 0.30740 0.39070 0.03600  0.06270  0.03570  28  ASP B C   
2902 O O   . ASP B  34  ? 0.22570 0.24320 0.31480 0.03450  0.05800  0.02550  28  ASP B O   
2903 C CB  . ASP B  34  ? 0.25500 0.29620 0.38340 0.04370  0.07990  0.05500  28  ASP B CB  
2904 C CG  . ASP B  34  ? 0.29460 0.32610 0.39600 0.05510  0.09110  0.05320  28  ASP B CG  
2905 O OD1 . ASP B  34  ? 0.25640 0.27580 0.33500 0.05540  0.08670  0.04220  28  ASP B OD1 
2906 O OD2 . ASP B  34  ? 0.29500 0.33050 0.39800 0.06470  0.10460  0.06360  28  ASP B OD2 
2907 N N   . ALA B  35  ? 0.23720 0.27260 0.36870 0.03910  0.06600  0.04270  29  ALA B N   
2908 C CA  . ALA B  35  ? 0.24580 0.27650 0.37300 0.03980  0.06250  0.03720  29  ALA B CA  
2909 C C   . ALA B  35  ? 0.28880 0.30780 0.38790 0.04760  0.06980  0.03190  29  ALA B C   
2910 O O   . ALA B  35  ? 0.28050 0.29320 0.37170 0.04730  0.06550  0.02550  29  ALA B O   
2911 C CB  . ALA B  35  ? 0.25920 0.30070 0.41610 0.04150  0.06420  0.04690  29  ALA B CB  
2912 N N   . LYS B  36  ? 0.28890 0.30400 0.37270 0.05530  0.08000  0.03460  30  LYS B N   
2913 C CA  . LYS B  36  ? 0.29010 0.29050 0.34330 0.06350  0.08490  0.02860  30  LYS B CA  
2914 C C   . LYS B  36  ? 0.34810 0.33640 0.37620 0.05970  0.07780  0.01880  30  LYS B C   
2915 O O   . LYS B  36  ? 0.36040 0.33380 0.36150 0.06570  0.07890  0.01280  30  LYS B O   
2916 C CB  . LYS B  36  ? 0.33970 0.34100 0.38860 0.07670  0.10070  0.03800  30  LYS B CB  
2917 C CG  . LYS B  36  ? 0.36410 0.37510 0.43510 0.08260  0.10870  0.04750  30  LYS B CG  
2918 C CD  . LYS B  36  ? 0.50380 0.50840 0.55790 0.09910  0.12470  0.05290  30  LYS B CD  
2919 C CE  . LYS B  36  ? 0.59580 0.60460 0.66370 0.10580  0.13110  0.05830  30  LYS B CE  
2920 N NZ  . LYS B  36  ? 0.56360 0.55720 0.61040 0.10640  0.12430  0.04590  30  LYS B NZ  
2921 N N   . GLY B  37  ? 0.27680 0.27020 0.31340 0.05010  0.06990  0.01740  31  GLY B N   
2922 C CA  . GLY B  37  ? 0.27680 0.26100 0.29430 0.04590  0.06320  0.00980  31  GLY B CA  
2923 C C   . GLY B  37  ? 0.29330 0.27600 0.30080 0.04940  0.06870  0.01340  31  GLY B C   
2924 O O   . GLY B  37  ? 0.28880 0.26400 0.28150 0.04580  0.06250  0.00760  31  GLY B O   
2925 N N   . ARG B  38  ? 0.26320 0.25340 0.27950 0.05680  0.08020  0.02350  32  ARG B N   
2926 C CA  . ARG B  38  ? 0.25990 0.24950 0.26720 0.06070  0.08620  0.02810  32  ARG B CA  
2927 C C   . ARG B  38  ? 0.28580 0.28160 0.30430 0.04990  0.07770  0.02710  32  ARG B C   
2928 O O   . ARG B  38  ? 0.27050 0.27740 0.31440 0.04230  0.07270  0.02980  32  ARG B O   
2929 C CB  . ARG B  38  ? 0.35640 0.35660 0.37840 0.06970  0.10060  0.04200  32  ARG B CB  
2930 C CG  . ARG B  38  ? 0.40670 0.40960 0.42530 0.07290  0.10710  0.04910  32  ARG B CG  
2931 C CD  . ARG B  38  ? 0.49080 0.50250 0.51990 0.08490  0.12400  0.06420  32  ARG B CD  
2932 N NE  . ARG B  38  ? 0.50760 0.53850 0.57860 0.07960  0.12520  0.07560  32  ARG B NE  
2933 C CZ  . ARG B  38  ? 0.55750 0.60110 0.65240 0.07590  0.12700  0.08620  32  ARG B CZ  
2934 N NH1 . ARG B  38  ? 0.55320 0.59350 0.63450 0.07660  0.12850  0.08680  32  ARG B NH1 
2935 N NH2 . ARG B  38  ? 0.49590 0.55530 0.63040 0.07130  0.12630  0.09670  32  ARG B NH2 
2936 N N   . LEU B  39  ? 0.30360 0.29090 0.30230 0.04980  0.07540  0.02340  33  LEU B N   
2937 C CA  . LEU B  39  ? 0.28730 0.27900 0.29420 0.04020  0.06740  0.02190  33  LEU B CA  
2938 C C   . LEU B  39  ? 0.28400 0.28830 0.31060 0.04070  0.07400  0.03310  33  LEU B C   
2939 O O   . LEU B  39  ? 0.33120 0.33430 0.34840 0.04910  0.08390  0.03960  33  LEU B O   
2940 C CB  . LEU B  39  ? 0.29400 0.27210 0.27460 0.03970  0.06190  0.01440  33  LEU B CB  
2941 C CG  . LEU B  39  ? 0.28610 0.26830 0.27440 0.03010  0.05370  0.01270  33  LEU B CG  
2942 C CD1 . LEU B  39  ? 0.24740 0.23260 0.24770 0.02130  0.04390  0.00700  33  LEU B CD1 
2943 C CD2 . LEU B  39  ? 0.34330 0.31330 0.30780 0.03100  0.04980  0.00810  33  LEU B CD2 
2944 N N   . LEU B  40  ? 0.21680 0.23210 0.26980 0.03230  0.06810  0.03570  34  LEU B N   
2945 C CA  . LEU B  40  ? 0.27160 0.29910 0.34850 0.03140  0.07210  0.04690  34  LEU B CA  
2946 C C   . LEU B  40  ? 0.25970 0.28690 0.33530 0.02510  0.06590  0.04510  34  LEU B C   
2947 O O   . LEU B  40  ? 0.25640 0.28710 0.33380 0.02810  0.07240  0.05280  34  LEU B O   
2948 C CB  . LEU B  40  ? 0.19530 0.23370 0.30440 0.02660  0.06770  0.05170  34  LEU B CB  
2949 C CG  . LEU B  40  ? 0.28090 0.32180 0.39720 0.03210  0.07320  0.05510  34  LEU B CG  
2950 C CD1 . LEU B  40  ? 0.28360 0.33450 0.43340 0.02630  0.06600  0.05970  34  LEU B CD1 
2951 C CD2 . LEU B  40  ? 0.29490 0.33930 0.40980 0.04360  0.08940  0.06640  34  LEU B CD2 
2952 N N   . TYR B  41  ? 0.21070 0.23400 0.28370 0.01700  0.05420  0.03570  35  TYR B N   
2953 C CA  . TYR B  41  ? 0.22230 0.24490 0.29450 0.01110  0.04790  0.03350  35  TYR B CA  
2954 C C   . TYR B  41  ? 0.20390 0.21660 0.25610 0.00780  0.04020  0.02230  35  TYR B C   
2955 O O   . TYR B  41  ? 0.19070 0.19910 0.23700 0.00790  0.03760  0.01670  35  TYR B O   
2956 C CB  . TYR B  41  ? 0.20370 0.23450 0.30260 0.00450  0.04050  0.03630  35  TYR B CB  
2957 C CG  . TYR B  41  ? 0.20990 0.25120 0.33370 0.00680  0.04650  0.04860  35  TYR B CG  
2958 C CD1 . TYR B  41  ? 0.18610 0.23230 0.32560 0.00880  0.04820  0.05260  35  TYR B CD1 
2959 C CD2 . TYR B  41  ? 0.28650 0.33340 0.42000 0.00740  0.05090  0.05760  35  TYR B CD2 
2960 C CE1 . TYR B  41  ? 0.24990 0.30700 0.41620 0.01130  0.05420  0.06610  35  TYR B CE1 
2961 C CE2 . TYR B  41  ? 0.24770 0.30570 0.40840 0.00980  0.05730  0.07160  35  TYR B CE2 
2962 C CZ  . TYR B  41  ? 0.26970 0.33290 0.44740 0.01160  0.05870  0.07580  35  TYR B CZ  
2963 O OH  . TYR B  41  ? 0.23280 0.30800 0.44050 0.01420  0.06510  0.09110  35  TYR B OH  
2964 N N   . ALA B  42  ? 0.22520 0.23480 0.26940 0.00460  0.03650  0.02010  36  ALA B N   
2965 C CA  . ALA B  42  ? 0.19730 0.19850 0.22580 0.00140  0.02950  0.01140  36  ALA B CA  
2966 C C   . ALA B  42  ? 0.18700 0.18930 0.21880 -0.00420 0.02350  0.01040  36  ALA B C   
2967 O O   . ALA B  42  ? 0.20050 0.20730 0.24000 -0.00470 0.02550  0.01570  36  ALA B O   
2968 C CB  . ALA B  42  ? 0.21850 0.20900 0.22300 0.00650  0.03210  0.00890  36  ALA B CB  
2969 N N   . LEU B  43  ? 0.19080 0.18920 0.21780 -0.00790 0.01680  0.00430  37  LEU B N   
2970 C CA  . LEU B  43  ? 0.19390 0.19090 0.21860 -0.01180 0.01180  0.00280  37  LEU B CA  
2971 C C   . LEU B  43  ? 0.19980 0.18850 0.20920 -0.01220 0.00840  -0.00150 37  LEU B C   
2972 O O   . LEU B  43  ? 0.18960 0.17450 0.19430 -0.01110 0.00750  -0.00470 37  LEU B O   
2973 C CB  . LEU B  43  ? 0.17550 0.17640 0.21240 -0.01530 0.00660  0.00110  37  LEU B CB  
2974 C CG  . LEU B  43  ? 0.19880 0.20590 0.25290 -0.01590 0.00610  0.00460  37  LEU B CG  
2975 C CD1 . LEU B  43  ? 0.17490 0.18130 0.23500 -0.01760 -0.00070 0.00100  37  LEU B CD1 
2976 C CD2 . LEU B  43  ? 0.19470 0.20470 0.25360 -0.01670 0.00800  0.00980  37  LEU B CD2 
2977 N N   . GLY B  44  ? 0.19860 0.18420 0.20200 -0.01400 0.00570  -0.00120 38  GLY B N   
2978 C CA  . GLY B  44  ? 0.20340 0.18110 0.19640 -0.01540 0.00010  -0.00430 38  GLY B CA  
2979 C C   . GLY B  44  ? 0.24070 0.20900 0.21890 -0.01120 0.00070  -0.00670 38  GLY B C   
2980 O O   . GLY B  44  ? 0.25110 0.21600 0.21950 -0.00620 0.00540  -0.00510 38  GLY B O   
2981 N N   . ASN B  45  ? 0.22270 0.18600 0.19870 -0.01230 -0.00370 -0.00990 39  ASN B N   
2982 C CA  . ASN B  45  ? 0.24080 0.19350 0.20270 -0.00800 -0.00440 -0.01290 39  ASN B CA  
2983 C C   . ASN B  45  ? 0.24340 0.20030 0.21150 -0.00610 -0.00010 -0.01380 39  ASN B C   
2984 O O   . ASN B  45  ? 0.20320 0.16200 0.17900 -0.00900 -0.00320 -0.01500 39  ASN B O   
2985 C CB  . ASN B  45  ? 0.26830 0.21100 0.22490 -0.01090 -0.01410 -0.01540 39  ASN B CB  
2986 C CG  . ASN B  45  ? 0.29940 0.22870 0.24120 -0.00650 -0.01690 -0.01940 39  ASN B CG  
2987 O OD1 . ASN B  45  ? 0.29200 0.21830 0.22400 -0.00010 -0.01060 -0.02040 39  ASN B OD1 
2988 N ND2 . ASN B  45  ? 0.26840 0.18940 0.20970 -0.00960 -0.02650 -0.02090 39  ASN B ND2 
2989 N N   . PRO B  46  ? 0.23150 0.19020 0.19760 -0.00080 0.00740  -0.01220 40  PRO B N   
2990 C CA  . PRO B  46  ? 0.21700 0.18090 0.19200 0.00060  0.01110  -0.01220 40  PRO B CA  
2991 C C   . PRO B  46  ? 0.21700 0.17180 0.18310 0.00270  0.00840  -0.01620 40  PRO B C   
2992 O O   . PRO B  46  ? 0.22230 0.18120 0.19630 0.00330  0.01040  -0.01640 40  PRO B O   
2993 C CB  . PRO B  46  ? 0.21080 0.17920 0.18750 0.00620  0.02010  -0.00760 40  PRO B CB  
2994 C CG  . PRO B  46  ? 0.22170 0.18140 0.18050 0.01060  0.02160  -0.00700 40  PRO B CG  
2995 C CD  . PRO B  46  ? 0.21450 0.17260 0.17310 0.00410  0.01350  -0.00870 40  PRO B CD  
2996 N N   . THR B  47  ? 0.24280 0.18440 0.19310 0.00390  0.00290  -0.01940 41  THR B N   
2997 C CA  . THR B  47  ? 0.24140 0.17230 0.18350 0.00560  -0.00150 -0.02330 41  THR B CA  
2998 C C   . THR B  47  ? 0.23340 0.16070 0.18050 -0.00080 -0.01160 -0.02450 41  THR B C   
2999 O O   . THR B  47  ? 0.28740 0.20320 0.22750 -0.00020 -0.01810 -0.02740 41  THR B O   
3000 C CB  . THR B  47  ? 0.27370 0.18900 0.19270 0.01360  -0.00120 -0.02610 41  THR B CB  
3001 O OG1 . THR B  47  ? 0.34400 0.25010 0.25090 0.01300  -0.00760 -0.02710 41  THR B OG1 
3002 C CG2 . THR B  47  ? 0.25950 0.17920 0.17510 0.02150  0.01080  -0.02290 41  THR B CG2 
3003 N N   . ARG B  48  ? 0.24510 0.18210 0.20530 -0.00640 -0.01280 -0.02160 42  ARG B N   
3004 C CA  . ARG B  48  ? 0.23500 0.17130 0.20360 -0.01190 -0.02050 -0.02030 42  ARG B CA  
3005 C C   . ARG B  48  ? 0.23720 0.17270 0.21160 -0.01220 -0.02200 -0.02070 42  ARG B C   
3006 O O   . ARG B  48  ? 0.24710 0.19070 0.22810 -0.01090 -0.01620 -0.02020 42  ARG B O   
3007 C CB  . ARG B  48  ? 0.23510 0.18390 0.21760 -0.01590 -0.01860 -0.01640 42  ARG B CB  
3008 C CG  . ARG B  48  ? 0.22410 0.17510 0.21870 -0.02040 -0.02400 -0.01290 42  ARG B CG  
3009 C CD  . ARG B  48  ? 0.20090 0.16420 0.20700 -0.02150 -0.01950 -0.00940 42  ARG B CD  
3010 N NE  . ARG B  48  ? 0.22440 0.19060 0.24180 -0.02460 -0.02280 -0.00420 42  ARG B NE  
3011 C CZ  . ARG B  48  ? 0.17730 0.14670 0.20360 -0.02440 -0.02230 -0.00070 42  ARG B CZ  
3012 N NH1 . ARG B  48  ? 0.18680 0.15540 0.21110 -0.02200 -0.02010 -0.00270 42  ARG B NH1 
3013 N NH2 . ARG B  48  ? 0.17210 0.14620 0.21050 -0.02620 -0.02340 0.00600  42  ARG B NH2 
3014 N N   . MET B  49  ? 0.21670 0.14170 0.18920 -0.01390 -0.03070 -0.02130 43  MET B N   
3015 C CA  A MET B  49  ? 0.24230 0.16720 0.22360 -0.01500 -0.03280 -0.02010 43  MET B CA  
3016 C CA  B MET B  49  ? 0.24190 0.16670 0.22330 -0.01510 -0.03300 -0.02010 43  MET B CA  
3017 C C   . MET B  49  ? 0.23970 0.17900 0.23810 -0.01800 -0.02900 -0.01470 43  MET B C   
3018 O O   . MET B  49  ? 0.23120 0.17480 0.23830 -0.02150 -0.03130 -0.01040 43  MET B O   
3019 C CB  A MET B  49  ? 0.28510 0.19640 0.26550 -0.01740 -0.04460 -0.02020 43  MET B CB  
3020 C CB  B MET B  49  ? 0.28510 0.19650 0.26580 -0.01780 -0.04500 -0.02000 43  MET B CB  
3021 C CG  A MET B  49  ? 0.25580 0.16780 0.24890 -0.01930 -0.04740 -0.01720 43  MET B CG  
3022 C CG  B MET B  49  ? 0.26820 0.17560 0.25540 -0.01810 -0.04850 -0.01930 43  MET B CG  
3023 S SD  A MET B  49  ? 0.29000 0.19720 0.27340 -0.01350 -0.04260 -0.02230 43  MET B SD  
3024 S SD  B MET B  49  ? 0.27660 0.17620 0.24680 -0.01070 -0.04320 -0.02610 43  MET B SD  
3025 C CE  A MET B  49  ? 0.30510 0.18810 0.26950 -0.01050 -0.05390 -0.02860 43  MET B CE  
3026 C CE  B MET B  49  ? 0.26470 0.15920 0.24560 -0.01250 -0.04960 -0.02420 43  MET B CE  
3027 N N   . THR B  50  ? 0.21770 0.16360 0.22000 -0.01580 -0.02300 -0.01460 44  THR B N   
3028 C CA  . THR B  50  ? 0.18380 0.14170 0.19690 -0.01620 -0.01840 -0.01050 44  THR B CA  
3029 C C   . THR B  50  ? 0.19210 0.15230 0.21100 -0.01470 -0.01700 -0.00850 44  THR B C   
3030 O O   . THR B  50  ? 0.18550 0.14230 0.19960 -0.01220 -0.01570 -0.01180 44  THR B O   
3031 C CB  . THR B  50  ? 0.20750 0.17210 0.21780 -0.01410 -0.01260 -0.01250 44  THR B CB  
3032 O OG1 . THR B  50  ? 0.18950 0.15260 0.19520 -0.01550 -0.01360 -0.01330 44  THR B OG1 
3033 C CG2 . THR B  50  ? 0.20580 0.17960 0.22370 -0.01320 -0.00940 -0.00950 44  THR B CG2 
3034 N N   . LEU B  51  ? 0.19580 0.16180 0.22500 -0.01550 -0.01640 -0.00240 45  LEU B N   
3035 C CA  . LEU B  51  ? 0.17480 0.14400 0.20910 -0.01310 -0.01390 0.00080  45  LEU B CA  
3036 C C   . LEU B  51  ? 0.21230 0.18670 0.24130 -0.00900 -0.00850 -0.00210 45  LEU B C   
3037 O O   . LEU B  51  ? 0.20730 0.18680 0.23610 -0.00760 -0.00590 -0.00100 45  LEU B O   
3038 C CB  . LEU B  51  ? 0.16510 0.13970 0.21170 -0.01360 -0.01330 0.00990  45  LEU B CB  
3039 C CG  . LEU B  51  ? 0.21830 0.18740 0.27500 -0.01810 -0.02050 0.01440  45  LEU B CG  
3040 C CD1 . LEU B  51  ? 0.19810 0.17330 0.26820 -0.02000 -0.02060 0.02330  45  LEU B CD1 
3041 C CD2 . LEU B  51  ? 0.20620 0.17340 0.26890 -0.01720 -0.02130 0.01760  45  LEU B CD2 
3042 N N   . ALA B  52  ? 0.18950 0.16160 0.21470 -0.00690 -0.00770 -0.00570 46  ALA B N   
3043 C CA  . ALA B  52  ? 0.22270 0.19870 0.24490 -0.00340 -0.00470 -0.00820 46  ALA B CA  
3044 C C   . ALA B  52  ? 0.19860 0.17880 0.22200 0.00030  -0.00260 -0.00430 46  ALA B C   
3045 O O   . ALA B  52  ? 0.19080 0.17290 0.21060 0.00340  -0.00190 -0.00620 46  ALA B O   
3046 C CB  . ALA B  52  ? 0.17110 0.14390 0.19130 -0.00180 -0.00460 -0.01150 46  ALA B CB  
3047 N N   . ARG B  53  ? 0.21300 0.19360 0.24110 0.00090  -0.00200 0.00150  47  ARG B N   
3048 C CA  . ARG B  53  ? 0.21690 0.20080 0.24430 0.00620  0.00130  0.00650  47  ARG B CA  
3049 C C   . ARG B  53  ? 0.23590 0.21850 0.25590 0.01070  0.00120  0.00240  47  ARG B C   
3050 O O   . ARG B  53  ? 0.23310 0.21330 0.25370 0.00930  -0.00060 -0.00130 47  ARG B O   
3051 C CB  . ARG B  53  ? 0.20090 0.18830 0.22750 0.00810  0.00370  0.00960  47  ARG B CB  
3052 C CG  . ARG B  53  ? 0.20140 0.19030 0.23770 0.00300  0.00270  0.01420  47  ARG B CG  
3053 C CD  . ARG B  53  ? 0.21160 0.20200 0.26000 0.00210  0.00310  0.02330  47  ARG B CD  
3054 N NE  . ARG B  53  ? 0.22700 0.22250 0.27690 0.00900  0.00960  0.03190  47  ARG B NE  
3055 C CZ  . ARG B  53  ? 0.23980 0.23980 0.29060 0.01270  0.01410  0.03730  47  ARG B CZ  
3056 N NH1 . ARG B  53  ? 0.22630 0.22710 0.27940 0.00900  0.01220  0.03570  47  ARG B NH1 
3057 N NH2 . ARG B  53  ? 0.23140 0.23460 0.27960 0.02130  0.02110  0.04480  47  ARG B NH2 
3058 N N   . SER B  54  ? 0.23380 0.21670 0.24640 0.01640  0.00240  0.00250  48  SER B N   
3059 C CA  . SER B  54  ? 0.25290 0.23290 0.25880 0.02070  0.00010  -0.00110 48  SER B CA  
3060 C C   . SER B  54  ? 0.24890 0.22770 0.25660 0.01750  -0.00400 -0.00780 48  SER B C   
3061 O O   . SER B  54  ? 0.24800 0.22480 0.25410 0.01980  -0.00690 -0.01030 48  SER B O   
3062 C CB  . SER B  54  ? 0.28880 0.26630 0.28350 0.02840  0.00030  -0.00070 48  SER B CB  
3063 O OG  . SER B  54  ? 0.31590 0.29400 0.30730 0.03430  0.00480  0.00630  48  SER B OG  
3064 N N   . ALA B  55  ? 0.20690 0.18730 0.21870 0.01270  -0.00430 -0.01000 49  ALA B N   
3065 C CA  . ALA B  55  ? 0.21170 0.19210 0.22740 0.01020  -0.00660 -0.01420 49  ALA B CA  
3066 C C   . ALA B  55  ? 0.23950 0.21920 0.25910 0.00880  -0.00560 -0.01460 49  ALA B C   
3067 O O   . ALA B  55  ? 0.27320 0.25360 0.29710 0.00850  -0.00650 -0.01670 49  ALA B O   
3068 C CB  . ALA B  55  ? 0.20820 0.19040 0.22640 0.00630  -0.00610 -0.01530 49  ALA B CB  
3069 N N   . ALA B  56  ? 0.24260 0.22090 0.26200 0.00860  -0.00400 -0.01200 50  ALA B N   
3070 C CA  . ALA B  56  ? 0.22900 0.20500 0.25080 0.00830  -0.00380 -0.01270 50  ALA B CA  
3071 C C   . ALA B  56  ? 0.22300 0.19890 0.24480 0.01210  -0.00490 -0.01230 50  ALA B C   
3072 O O   . ALA B  56  ? 0.25350 0.22770 0.27790 0.01240  -0.00470 -0.01290 50  ALA B O   
3073 C CB  . ALA B  56  ? 0.20320 0.17600 0.22610 0.00620  -0.00350 -0.01010 50  ALA B CB  
3074 N N   . LYS B  57  ? 0.22940 0.20580 0.24690 0.01580  -0.00640 -0.01120 51  LYS B N   
3075 C CA  . LYS B  57  ? 0.20760 0.18230 0.22260 0.02020  -0.00810 -0.01020 51  LYS B CA  
3076 C C   . LYS B  57  ? 0.20930 0.18380 0.22970 0.02020  -0.01090 -0.01300 51  LYS B C   
3077 O O   . LYS B  57  ? 0.23490 0.20810 0.25610 0.02220  -0.01130 -0.01170 51  LYS B O   
3078 C CB  . LYS B  57  ? 0.22730 0.20010 0.23280 0.02580  -0.01000 -0.00950 51  LYS B CB  
3079 C CG  . LYS B  57  ? 0.25830 0.23160 0.25870 0.02900  -0.00540 -0.00360 51  LYS B CG  
3080 C CD  . LYS B  57  ? 0.28210 0.25230 0.26990 0.03620  -0.00600 -0.00310 51  LYS B CD  
3081 C CE  . LYS B  57  ? 0.29100 0.26370 0.27700 0.03970  0.00110  0.00520  51  LYS B CE  
3082 N NZ  . LYS B  57  ? 0.29660 0.26640 0.26920 0.04810  0.00310  0.00710  51  LYS B NZ  
3083 N N   . PRO B  58  ? 0.23010 0.20630 0.25610 0.01820  -0.01280 -0.01570 52  PRO B N   
3084 C CA  . PRO B  58  ? 0.20570 0.18300 0.24060 0.01860  -0.01450 -0.01620 52  PRO B CA  
3085 C C   . PRO B  58  ? 0.21860 0.19580 0.25670 0.01770  -0.00980 -0.01550 52  PRO B C   
3086 O O   . PRO B  58  ? 0.20400 0.18120 0.24730 0.01940  -0.01040 -0.01490 52  PRO B O   
3087 C CB  . PRO B  58  ? 0.23610 0.21650 0.27910 0.01640  -0.01610 -0.01710 52  PRO B CB  
3088 C CG  . PRO B  58  ? 0.19600 0.17460 0.23170 0.01680  -0.01930 -0.01830 52  PRO B CG  
3089 C CD  . PRO B  58  ? 0.22000 0.19750 0.24640 0.01660  -0.01440 -0.01720 52  PRO B CD  
3090 N N   . ALA B  59  ? 0.21590 0.19180 0.25060 0.01540  -0.00590 -0.01570 53  ALA B N   
3091 C CA  . ALA B  59  ? 0.21580 0.18820 0.25040 0.01550  -0.00310 -0.01590 53  ALA B CA  
3092 C C   . ALA B  59  ? 0.21150 0.18120 0.24450 0.01690  -0.00430 -0.01390 53  ALA B C   
3093 O O   . ALA B  59  ? 0.23270 0.20000 0.26820 0.01840  -0.00370 -0.01390 53  ALA B O   
3094 C CB  . ALA B  59  ? 0.26520 0.23430 0.29490 0.01310  -0.00110 -0.01710 53  ALA B CB  
3095 N N   . GLN B  60  ? 0.20320 0.17330 0.23260 0.01680  -0.00530 -0.01140 54  GLN B N   
3096 C CA  . GLN B  60  ? 0.22210 0.19070 0.25120 0.01880  -0.00560 -0.00770 54  GLN B CA  
3097 C C   . GLN B  60  ? 0.24980 0.21900 0.27950 0.02260  -0.00760 -0.00760 54  GLN B C   
3098 O O   . GLN B  60  ? 0.22740 0.19470 0.25930 0.02400  -0.00760 -0.00580 54  GLN B O   
3099 C CB  . GLN B  60  ? 0.25430 0.22440 0.28010 0.01940  -0.00460 -0.00330 54  GLN B CB  
3100 C CG  . GLN B  60  ? 0.22400 0.19290 0.25260 0.01510  -0.00380 -0.00200 54  GLN B CG  
3101 C CD  . GLN B  60  ? 0.26960 0.24170 0.29710 0.01520  -0.00230 0.00220  54  GLN B CD  
3102 O OE1 . GLN B  60  ? 0.22620 0.20040 0.24870 0.01650  -0.00200 0.00010  54  GLN B OE1 
3103 N NE2 . GLN B  60  ? 0.23620 0.20830 0.26970 0.01390  -0.00150 0.00860  54  GLN B NE2 
3104 N N   . ALA B  61  ? 0.23500 0.20600 0.26320 0.02420  -0.01050 -0.00950 55  ALA B N   
3105 C CA  . ALA B  61  ? 0.20990 0.18020 0.23930 0.02760  -0.01470 -0.00970 55  ALA B CA  
3106 C C   . ALA B  61  ? 0.20160 0.17290 0.24090 0.02670  -0.01410 -0.01050 55  ALA B C   
3107 O O   . ALA B  61  ? 0.21400 0.18420 0.25560 0.02920  -0.01600 -0.00920 55  ALA B O   
3108 C CB  . ALA B  61  ? 0.21540 0.18550 0.24270 0.02880  -0.02020 -0.01200 55  ALA B CB  
3109 N N   . LEU B  62  ? 0.22870 0.20160 0.27320 0.02410  -0.01080 -0.01210 56  LEU B N   
3110 C CA  . LEU B  62  ? 0.24050 0.21370 0.29300 0.02510  -0.00840 -0.01200 56  LEU B CA  
3111 C C   . LEU B  62  ? 0.24920 0.21790 0.29920 0.02620  -0.00650 -0.01120 56  LEU B C   
3112 O O   . LEU B  62  ? 0.20640 0.17460 0.26160 0.02850  -0.00670 -0.01020 56  LEU B O   
3113 C CB  . LEU B  62  ? 0.21640 0.19110 0.27150 0.02380  -0.00370 -0.01320 56  LEU B CB  
3114 C CG  . LEU B  62  ? 0.22740 0.20210 0.28900 0.02670  0.00100  -0.01240 56  LEU B CG  
3115 C CD1 . LEU B  62  ? 0.20620 0.18620 0.28150 0.02850  -0.00160 -0.00940 56  LEU B CD1 
3116 C CD2 . LEU B  62  ? 0.21980 0.19460 0.27980 0.02720  0.00680  -0.01290 56  LEU B CD2 
3117 N N   . ALA B  63  ? 0.20760 0.17270 0.25100 0.02430  -0.00550 -0.01110 57  ALA B N   
3118 C CA  . ALA B  63  ? 0.20360 0.16340 0.24660 0.02480  -0.00520 -0.00980 57  ALA B CA  
3119 C C   . ALA B  63  ? 0.21680 0.17760 0.26130 0.02730  -0.00740 -0.00620 57  ALA B C   
3120 O O   . ALA B  63  ? 0.23430 0.19240 0.28240 0.02900  -0.00750 -0.00530 57  ALA B O   
3121 C CB  . ALA B  63  ? 0.18280 0.13880 0.22190 0.02170  -0.00540 -0.00900 57  ALA B CB  
3122 N N   . ILE B  64  ? 0.19850 0.16230 0.23900 0.02830  -0.00920 -0.00420 58  ILE B N   
3123 C CA  . ILE B  64  ? 0.22010 0.18390 0.25880 0.03230  -0.01150 -0.00100 58  ILE B CA  
3124 C C   . ILE B  64  ? 0.22240 0.18680 0.26700 0.03420  -0.01430 -0.00250 58  ILE B C   
3125 O O   . ILE B  64  ? 0.24160 0.20440 0.28880 0.03640  -0.01510 -0.00030 58  ILE B O   
3126 C CB  . ILE B  64  ? 0.25300 0.21780 0.28250 0.03500  -0.01320 0.00040  58  ILE B CB  
3127 C CG1 . ILE B  64  ? 0.24280 0.20810 0.26890 0.03390  -0.00930 0.00420  58  ILE B CG1 
3128 C CG2 . ILE B  64  ? 0.21990 0.18260 0.24410 0.04070  -0.01660 0.00290  58  ILE B CG2 
3129 C CD1 . ILE B  64  ? 0.22090 0.18710 0.23760 0.03640  -0.00950 0.00430  58  ILE B CD1 
3130 N N   . LEU B  65  ? 0.19750 0.16460 0.24610 0.03350  -0.01640 -0.00530 59  LEU B N   
3131 C CA  . LEU B  65  ? 0.23180 0.20040 0.28930 0.03530  -0.02020 -0.00520 59  LEU B CA  
3132 C C   . LEU B  65  ? 0.26460 0.23360 0.33150 0.03550  -0.01600 -0.00480 59  LEU B C   
3133 O O   . LEU B  65  ? 0.26080 0.23070 0.33570 0.03770  -0.01840 -0.00310 59  LEU B O   
3134 C CB  . LEU B  65  ? 0.20240 0.17420 0.26570 0.03420  -0.02410 -0.00680 59  LEU B CB  
3135 C CG  . LEU B  65  ? 0.21220 0.18130 0.26550 0.03550  -0.03050 -0.00800 59  LEU B CG  
3136 C CD1 . LEU B  65  ? 0.29960 0.27130 0.36130 0.03340  -0.03460 -0.00950 59  LEU B CD1 
3137 C CD2 . LEU B  65  ? 0.28890 0.25350 0.33630 0.04010  -0.03740 -0.00670 59  LEU B CD2 
3138 N N   . GLU B  66  ? 0.24590 0.21300 0.31080 0.03400  -0.01040 -0.00630 60  GLU B N   
3139 C CA  . GLU B  66  ? 0.25380 0.21830 0.32320 0.03590  -0.00640 -0.00640 60  GLU B CA  
3140 C C   . GLU B  66  ? 0.27240 0.23110 0.33840 0.03670  -0.00680 -0.00530 60  GLU B C   
3141 O O   . GLU B  66  ? 0.28760 0.24150 0.35520 0.03870  -0.00410 -0.00600 60  GLU B O   
3142 C CB  . GLU B  66  ? 0.27320 0.23550 0.33930 0.03530  -0.00110 -0.00910 60  GLU B CB  
3143 C CG  . GLU B  66  ? 0.20590 0.17470 0.27910 0.03550  0.00110  -0.00860 60  GLU B CG  
3144 C CD  . GLU B  66  ? 0.30410 0.26960 0.37130 0.03650  0.00720  -0.01070 60  GLU B CD  
3145 O OE1 . GLU B  66  ? 0.34740 0.30570 0.40310 0.03510  0.00700  -0.01360 60  GLU B OE1 
3146 O OE2 . GLU B  66  ? 0.29810 0.26770 0.37220 0.03920  0.01200  -0.00890 60  GLU B OE2 
3147 N N   . THR B  67  ? 0.25350 0.21180 0.31480 0.03590  -0.00970 -0.00290 61  THR B N   
3148 C CA  . THR B  67  ? 0.23600 0.18960 0.29700 0.03670  -0.01010 -0.00010 61  THR B CA  
3149 C C   . THR B  67  ? 0.25750 0.21220 0.32410 0.04010  -0.01220 0.00220  61  THR B C   
3150 O O   . THR B  67  ? 0.23540 0.19350 0.30140 0.04180  -0.01570 0.00360  61  THR B O   
3151 C CB  . THR B  67  ? 0.25120 0.20510 0.30690 0.03560  -0.01090 0.00380  61  THR B CB  
3152 O OG1 . THR B  67  ? 0.22760 0.18060 0.28020 0.03210  -0.00940 0.00200  61  THR B OG1 
3153 C CG2 . THR B  67  ? 0.22380 0.17380 0.28270 0.03640  -0.01120 0.00850  61  THR B CG2 
3154 N N   . GLU B  68  ? 0.22550 0.17580 0.29670 0.04160  -0.01090 0.00220  62  GLU B N   
3155 C CA  . GLU B  68  ? 0.25110 0.20240 0.32950 0.04490  -0.01250 0.00440  62  GLU B CA  
3156 C C   . GLU B  68  ? 0.29070 0.24300 0.36630 0.04630  -0.01630 0.00900  62  GLU B C   
3157 O O   . GLU B  68  ? 0.25700 0.20640 0.32910 0.04570  -0.01580 0.01220  62  GLU B O   
3158 C CB  . GLU B  68  ? 0.23120 0.17590 0.31310 0.04680  -0.01010 0.00370  62  GLU B CB  
3159 C CG  . GLU B  68  ? 0.22310 0.16550 0.30520 0.04820  -0.00550 -0.00050 62  GLU B CG  
3160 C CD  . GLU B  68  ? 0.27220 0.20780 0.34490 0.04590  -0.00440 -0.00410 62  GLU B CD  
3161 O OE1 . GLU B  68  ? 0.25810 0.19420 0.32680 0.04200  -0.00690 -0.00300 62  GLU B OE1 
3162 O OE2 . GLU B  68  ? 0.25530 0.18470 0.32440 0.04880  -0.00100 -0.00760 62  GLU B OE2 
3163 N N   . GLY B  69  ? 0.26540 0.22110 0.34280 0.04860  -0.02050 0.01000  63  GLY B N   
3164 C CA  . GLY B  69  ? 0.29820 0.25310 0.36960 0.05160  -0.02460 0.01400  63  GLY B CA  
3165 C C   . GLY B  69  ? 0.30170 0.25740 0.36190 0.05270  -0.02800 0.01360  63  GLY B C   
3166 O O   . GLY B  69  ? 0.30760 0.26130 0.36030 0.05710  -0.03260 0.01620  63  GLY B O   
3167 N N   . VAL B  70  ? 0.23190 0.18940 0.28960 0.04970  -0.02610 0.01030  64  VAL B N   
3168 C CA  . VAL B  70  ? 0.27980 0.23670 0.32570 0.05140  -0.02930 0.00960  64  VAL B CA  
3169 C C   . VAL B  70  ? 0.27260 0.22860 0.31920 0.05370  -0.03800 0.00760  64  VAL B C   
3170 O O   . VAL B  70  ? 0.29780 0.24950 0.33140 0.05810  -0.04350 0.00780  64  VAL B O   
3171 C CB  . VAL B  70  ? 0.25940 0.21840 0.30380 0.04740  -0.02540 0.00670  64  VAL B CB  
3172 C CG1 . VAL B  70  ? 0.23930 0.19730 0.27330 0.04930  -0.02970 0.00470  64  VAL B CG1 
3173 C CG2 . VAL B  70  ? 0.25570 0.21410 0.29740 0.04600  -0.01930 0.01010  64  VAL B CG2 
3174 N N   . ALA B  71  ? 0.23250 0.19160 0.29440 0.05140  -0.03990 0.00610  65  ALA B N   
3175 C CA  . ALA B  71  ? 0.30470 0.26340 0.37220 0.05260  -0.04970 0.00510  65  ALA B CA  
3176 C C   . ALA B  71  ? 0.30630 0.25890 0.36500 0.05800  -0.05780 0.00720  65  ALA B C   
3177 O O   . ALA B  71  ? 0.32390 0.27180 0.37810 0.06040  -0.06850 0.00570  65  ALA B O   
3178 C CB  . ALA B  71  ? 0.29100 0.25550 0.38030 0.05000  -0.04870 0.00590  65  ALA B CB  
3179 N N   . GLY B  72  ? 0.29470 0.24610 0.34970 0.06040  -0.05360 0.01070  66  GLY B N   
3180 C CA  . GLY B  72  ? 0.33660 0.28220 0.38260 0.06630  -0.06050 0.01340  66  GLY B CA  
3181 C C   . GLY B  72  ? 0.34620 0.28440 0.36840 0.07240  -0.06430 0.01330  66  GLY B C   
3182 O O   . GLY B  72  ? 0.34170 0.27250 0.35290 0.07850  -0.07290 0.01420  66  GLY B O   
3183 N N   . TYR B  73  ? 0.31280 0.25170 0.32540 0.07170  -0.05810 0.01230  67  TYR B N   
3184 C CA  . TYR B  73  ? 0.30810 0.23950 0.29670 0.07910  -0.06010 0.01290  67  TYR B CA  
3185 C C   . TYR B  73  ? 0.34330 0.26670 0.32320 0.08190  -0.07300 0.00740  67  TYR B C   
3186 O O   . TYR B  73  ? 0.37840 0.29210 0.33480 0.09040  -0.07730 0.00710  67  TYR B O   
3187 C CB  . TYR B  73  ? 0.32780 0.26310 0.31150 0.07760  -0.04960 0.01420  67  TYR B CB  
3188 C CG  . TYR B  73  ? 0.32130 0.26200 0.31190 0.07590  -0.03900 0.02070  67  TYR B CG  
3189 C CD1 . TYR B  73  ? 0.33730 0.27540 0.32020 0.08230  -0.03700 0.02760  67  TYR B CD1 
3190 C CD2 . TYR B  73  ? 0.32580 0.27290 0.33040 0.06830  -0.03190 0.02020  67  TYR B CD2 
3191 C CE1 . TYR B  73  ? 0.40210 0.34480 0.39410 0.08040  -0.02860 0.03430  67  TYR B CE1 
3192 C CE2 . TYR B  73  ? 0.28100 0.23100 0.29280 0.06660  -0.02470 0.02610  67  TYR B CE2 
3193 C CZ  . TYR B  73  ? 0.34660 0.29470 0.35350 0.07220  -0.02320 0.03340  67  TYR B CZ  
3194 O OH  . TYR B  73  ? 0.42840 0.37920 0.44510 0.07030  -0.01710 0.04010  67  TYR B OH  
3195 N N   . GLY B  74  ? 0.34300 0.26960 0.34090 0.07570  -0.07940 0.00350  68  GLY B N   
3196 C CA  . GLY B  74  ? 0.31120 0.22970 0.30480 0.07730  -0.09350 -0.00120 68  GLY B CA  
3197 C C   . GLY B  74  ? 0.33350 0.24820 0.31240 0.07880  -0.09270 -0.00480 68  GLY B C   
3198 O O   . GLY B  74  ? 0.36190 0.26420 0.32280 0.08510  -0.10390 -0.00830 68  GLY B O   
3199 N N   . PHE B  75  ? 0.33190 0.25530 0.31640 0.07380  -0.08040 -0.00420 69  PHE B N   
3200 C CA  . PHE B  75  ? 0.31490 0.23640 0.29120 0.07340  -0.08010 -0.00780 69  PHE B CA  
3201 C C   . PHE B  75  ? 0.32940 0.24890 0.31890 0.06930  -0.09240 -0.01210 69  PHE B C   
3202 O O   . PHE B  75  ? 0.36010 0.28700 0.37360 0.06320  -0.09400 -0.01080 69  PHE B O   
3203 C CB  . PHE B  75  ? 0.34010 0.27220 0.32490 0.06730  -0.06590 -0.00610 69  PHE B CB  
3204 C CG  . PHE B  75  ? 0.34750 0.28110 0.32150 0.07090  -0.05490 -0.00090 69  PHE B CG  
3205 C CD1 . PHE B  75  ? 0.30540 0.23140 0.25600 0.08040  -0.05440 0.00120  69  PHE B CD1 
3206 C CD2 . PHE B  75  ? 0.29890 0.24100 0.28670 0.06560  -0.04510 0.00270  69  PHE B CD2 
3207 C CE1 . PHE B  75  ? 0.32980 0.25900 0.27440 0.08390  -0.04320 0.00850  69  PHE B CE1 
3208 C CE2 . PHE B  75  ? 0.28970 0.23350 0.27180 0.06820  -0.03610 0.00880  69  PHE B CE2 
3209 C CZ  . PHE B  75  ? 0.31250 0.25110 0.27470 0.07700  -0.03460 0.01240  69  PHE B CZ  
3210 N N   . ASP B  76  ? 0.29310 0.20210 0.26750 0.07350  -0.10180 -0.01640 70  ASP B N   
3211 C CA  . ASP B  76  ? 0.29200 0.19810 0.28040 0.06950  -0.11540 -0.01980 70  ASP B CA  
3212 C C   . ASP B  76  ? 0.28000 0.19170 0.27470 0.06420  -0.10990 -0.02160 70  ASP B C   
3213 O O   . ASP B  76  ? 0.30110 0.21880 0.28940 0.06350  -0.09610 -0.02050 70  ASP B O   
3214 C CB  . ASP B  76  ? 0.35580 0.24340 0.32510 0.07760  -0.13380 -0.02400 70  ASP B CB  
3215 C CG  . ASP B  76  ? 0.41410 0.28920 0.35010 0.08710  -0.13340 -0.02750 70  ASP B CG  
3216 O OD1 . ASP B  76  ? 0.37440 0.25570 0.30490 0.08630  -0.11990 -0.02680 70  ASP B OD1 
3217 O OD2 . ASP B  76  ? 0.44750 0.30500 0.36190 0.09620  -0.14770 -0.03100 70  ASP B OD2 
3218 N N   . ASP B  77  ? 0.29550 0.28380 0.28880 0.06670  -0.04710 -0.02300 71  ASP B N   
3219 C CA  . ASP B  77  ? 0.25280 0.24410 0.25710 0.05900  -0.04020 -0.02030 71  ASP B CA  
3220 C C   . ASP B  77  ? 0.25700 0.23890 0.24660 0.05830  -0.03700 -0.01850 71  ASP B C   
3221 O O   . ASP B  77  ? 0.21700 0.19950 0.20730 0.05400  -0.02920 -0.01310 71  ASP B O   
3222 C CB  . ASP B  77  ? 0.28050 0.27910 0.30920 0.05480  -0.04480 -0.02480 71  ASP B CB  
3223 C CG  . ASP B  77  ? 0.30850 0.32020 0.35940 0.05280  -0.04330 -0.02440 71  ASP B CG  
3224 O OD1 . ASP B  77  ? 0.29850 0.31350 0.34570 0.05520  -0.03900 -0.02180 71  ASP B OD1 
3225 O OD2 . ASP B  77  ? 0.39190 0.41070 0.46640 0.04860  -0.04600 -0.02720 71  ASP B OD2 
3226 N N   . ALA B  78  ? 0.28400 0.25860 0.26110 0.06310  -0.04310 -0.02340 72  ALA B N   
3227 C CA  . ALA B  78  ? 0.30360 0.27030 0.26940 0.06300  -0.03920 -0.02270 72  ALA B CA  
3228 C C   . ALA B  78  ? 0.31040 0.27280 0.25990 0.06440  -0.03110 -0.01580 72  ALA B C   
3229 O O   . ALA B  78  ? 0.25940 0.22000 0.20780 0.06170  -0.02470 -0.01230 72  ALA B O   
3230 C CB  . ALA B  78  ? 0.31170 0.27240 0.26730 0.06830  -0.04730 -0.03120 72  ALA B CB  
3231 N N   . ASP B  79  ? 0.29600 0.25690 0.23520 0.06860  -0.03160 -0.01390 73  ASP B N   
3232 C CA  . ASP B  79  ? 0.32670 0.28390 0.25640 0.06860  -0.02360 -0.00740 73  ASP B CA  
3233 C C   . ASP B  79  ? 0.30800 0.27150 0.24940 0.06190  -0.01730 -0.00400 73  ASP B C   
3234 O O   . ASP B  79  ? 0.26870 0.23060 0.20630 0.05950  -0.01110 -0.00040 73  ASP B O   
3235 C CB  . ASP B  79  ? 0.31800 0.27220 0.24050 0.07390  -0.02570 -0.00560 73  ASP B CB  
3236 C CG  . ASP B  79  ? 0.33820 0.28580 0.24320 0.08200  -0.03160 -0.00680 73  ASP B CG  
3237 O OD1 . ASP B  79  ? 0.34960 0.29310 0.24320 0.08370  -0.03140 -0.00870 73  ASP B OD1 
3238 O OD2 . ASP B  79  ? 0.35460 0.30130 0.25650 0.08740  -0.03670 -0.00580 73  ASP B OD2 
3239 N N   . ILE B  80  ? 0.26440 0.23600 0.21970 0.05920  -0.01850 -0.00520 74  ILE B N   
3240 C CA  . ILE B  80  ? 0.25680 0.23550 0.21980 0.05360  -0.01250 -0.00220 74  ILE B CA  
3241 C C   . ILE B  80  ? 0.27500 0.25550 0.24180 0.04960  -0.01030 0.00070  74  ILE B C   
3242 O O   . ILE B  80  ? 0.22700 0.21020 0.19200 0.04660  -0.00550 0.00450  74  ILE B O   
3243 C CB  . ILE B  80  ? 0.22500 0.21300 0.20190 0.05250  -0.01310 -0.00400 74  ILE B CB  
3244 C CG1 . ILE B  80  ? 0.26840 0.25410 0.24270 0.05760  -0.01500 -0.00640 74  ILE B CG1 
3245 C CG2 . ILE B  80  ? 0.25410 0.25070 0.23610 0.04730  -0.00640 -0.00090 74  ILE B CG2 
3246 C CD1 . ILE B  80  ? 0.28500 0.28020 0.27550 0.05840  -0.01680 -0.00950 74  ILE B CD1 
3247 N N   . ALA B  81  ? 0.24440 0.22320 0.21750 0.04980  -0.01430 -0.00150 75  ALA B N   
3248 C CA  . ALA B  81  ? 0.26830 0.24680 0.24660 0.04690  -0.01210 0.00180  75  ALA B CA  
3249 C C   . ALA B  81  ? 0.25780 0.23090 0.22430 0.04870  -0.00890 0.00360  75  ALA B C   
3250 O O   . ALA B  81  ? 0.23950 0.21550 0.20890 0.04620  -0.00540 0.00850  75  ALA B O   
3251 C CB  . ALA B  81  ? 0.22850 0.20380 0.21760 0.04690  -0.01720 -0.00250 75  ALA B CB  
3252 N N   . LEU B  82  ? 0.24870 0.21510 0.20240 0.05330  -0.00970 0.00070  76  LEU B N   
3253 C CA  . LEU B  82  ? 0.26210 0.22470 0.20710 0.05460  -0.00480 0.00320  76  LEU B CA  
3254 C C   . LEU B  82  ? 0.25320 0.22050 0.19870 0.05120  -0.00020 0.00740  76  LEU B C   
3255 O O   . LEU B  82  ? 0.28190 0.25090 0.22880 0.04980  0.00350  0.01040  76  LEU B O   
3256 C CB  . LEU B  82  ? 0.27910 0.23350 0.20870 0.06050  -0.00510 0.00050  76  LEU B CB  
3257 C CG  . LEU B  82  ? 0.25270 0.20310 0.17520 0.06270  0.00110  0.00220  76  LEU B CG  
3258 C CD1 . LEU B  82  ? 0.29190 0.24060 0.21910 0.06420  -0.00040 -0.00190 76  LEU B CD1 
3259 C CD2 . LEU B  82  ? 0.28330 0.22630 0.18780 0.06860  0.00330  0.00250  76  LEU B CD2 
3260 N N   . MET B  83  ? 0.23410 0.20380 0.17950 0.05030  -0.00080 0.00670  77  MET B N   
3261 C CA  . MET B  83  ? 0.23300 0.20740 0.18000 0.04680  0.00260  0.00830  77  MET B CA  
3262 C C   . MET B  83  ? 0.25030 0.23400 0.20440 0.04260  0.00310  0.01110  77  MET B C   
3263 O O   . MET B  83  ? 0.26190 0.24990 0.21640 0.04010  0.00490  0.01250  77  MET B O   
3264 C CB  . MET B  83  ? 0.22720 0.20250 0.17460 0.04710  0.00210  0.00560  77  MET B CB  
3265 C CG  . MET B  83  ? 0.23720 0.20350 0.17800 0.05190  0.00110  0.00450  77  MET B CG  
3266 S SD  . MET B  83  ? 0.30220 0.27130 0.24850 0.05230  0.00090  0.00100  77  MET B SD  
3267 C CE  . MET B  83  ? 0.30290 0.26070 0.24190 0.05980  -0.00200 0.00200  77  MET B CE  
3268 N N   . CYS B  84  ? 0.24970 0.23660 0.21000 0.04200  0.00110  0.01240  78  CYS B N   
3269 C CA  . CYS B  84  ? 0.25770 0.25230 0.22420 0.03910  0.00170  0.01760  78  CYS B CA  
3270 C C   . CYS B  84  ? 0.23030 0.22260 0.20090 0.04000  0.00150  0.02120  78  CYS B C   
3271 O O   . CYS B  84  ? 0.28340 0.28040 0.26070 0.03850  0.00140  0.02700  78  CYS B O   
3272 C CB  . CYS B  84  ? 0.23750 0.23580 0.21200 0.03770  0.00110  0.01890  78  CYS B CB  
3273 S SG  . CYS B  84  ? 0.26360 0.26770 0.23650 0.03720  0.00280  0.01480  78  CYS B SG  
3274 N N   . ALA B  85  ? 0.22710 0.21200 0.19440 0.04300  0.00200  0.01860  79  ALA B N   
3275 C CA  . ALA B  85  ? 0.24020 0.22130 0.21270 0.04520  0.00230  0.01990  79  ALA B CA  
3276 C C   . ALA B  85  ? 0.27760 0.26290 0.25270 0.04530  0.00480  0.02330  79  ALA B C   
3277 O O   . ALA B  85  ? 0.29450 0.28230 0.26570 0.04430  0.00680  0.02260  79  ALA B O   
3278 C CB  . ALA B  85  ? 0.25600 0.22720 0.22230 0.04950  0.00200  0.01370  79  ALA B CB  
3279 N N   . SER B  86  ? 0.27630 0.26210 0.26100 0.04680  0.00460  0.02700  80  SER B N   
3280 C CA  . SER B  86  ? 0.24290 0.23030 0.23320 0.04920  0.00740  0.02830  80  SER B CA  
3281 C C   . SER B  86  ? 0.25240 0.22960 0.24390 0.05400  0.00920  0.02370  80  SER B C   
3282 O O   . SER B  86  ? 0.26090 0.23570 0.26310 0.05590  0.00820  0.02550  80  SER B O   
3283 C CB  . SER B  86  ? 0.23130 0.22810 0.23290 0.04860  0.00510  0.03620  80  SER B CB  
3284 O OG  . SER B  86  ? 0.26580 0.27250 0.26320 0.04460  0.00250  0.03870  80  SER B OG  
3285 N N   . HIS B  87  ? 0.24860 0.21910 0.22830 0.05630  0.01160  0.01760  81  HIS B N   
3286 C CA  . HIS B  87  ? 0.28420 0.24520 0.26170 0.06080  0.01140  0.01100  81  HIS B CA  
3287 C C   . HIS B  87  ? 0.27680 0.23650 0.25920 0.06550  0.01700  0.00990  81  HIS B C   
3288 O O   . HIS B  87  ? 0.25470 0.22130 0.24210 0.06530  0.02140  0.01430  81  HIS B O   
3289 C CB  . HIS B  87  ? 0.29180 0.24650 0.25230 0.06280  0.01050  0.00470  81  HIS B CB  
3290 C CG  . HIS B  87  ? 0.27500 0.22980 0.22340 0.06450  0.01640  0.00590  81  HIS B CG  
3291 N ND1 . HIS B  87  ? 0.26970 0.22280 0.21520 0.06860  0.02370  0.00520  81  HIS B ND1 
3292 C CD2 . HIS B  87  ? 0.26430 0.21970 0.20410 0.06260  0.01710  0.00820  81  HIS B CD2 
3293 C CE1 . HIS B  87  ? 0.25770 0.21080 0.19380 0.06870  0.02910  0.00820  81  HIS B CE1 
3294 N NE2 . HIS B  87  ? 0.24600 0.19960 0.17870 0.06510  0.02480  0.00990  81  HIS B NE2 
3295 N N   . SER B  88  ? 0.24390 0.19500 0.22610 0.07000  0.01670  0.00270  82  SER B N   
3296 C CA  . SER B  88  ? 0.27890 0.22760 0.26730 0.07560  0.02230  -0.00030 82  SER B CA  
3297 C C   . SER B  88  ? 0.29240 0.23900 0.26440 0.08040  0.02990  -0.00500 82  SER B C   
3298 O O   . SER B  88  ? 0.31740 0.26200 0.29210 0.08610  0.03620  -0.00920 82  SER B O   
3299 C CB  . SER B  88  ? 0.25680 0.19610 0.25340 0.07830  0.01860  -0.00740 82  SER B CB  
3300 O OG  . SER B  88  ? 0.26630 0.20770 0.28310 0.07530  0.01510  0.00010  82  SER B OG  
3301 N N   . SER B  89  ? 0.25890 0.20580 0.21440 0.07880  0.03030  -0.00390 83  SER B N   
3302 C CA  . SER B  89  ? 0.27990 0.22390 0.21720 0.08370  0.03820  -0.00620 83  SER B CA  
3303 C C   . SER B  89  ? 0.30690 0.24190 0.23040 0.09080  0.03770  -0.01730 83  SER B C   
3304 O O   . SER B  89  ? 0.31730 0.25050 0.22920 0.09690  0.04650  -0.02040 83  SER B O   
3305 C CB  . SER B  89  ? 0.29890 0.24990 0.24590 0.08460  0.04900  -0.00090 83  SER B CB  
3306 O OG  . SER B  89  ? 0.28390 0.24420 0.24640 0.07780  0.04720  0.00730  83  SER B OG  
3307 N N   . GLU B  90  ? 0.29350 0.22330 0.21870 0.09010  0.02780  -0.02410 84  GLU B N   
3308 C CA  . GLU B  90  ? 0.31440 0.23590 0.22500 0.09660  0.02520  -0.03700 84  GLU B CA  
3309 C C   . GLU B  90  ? 0.35750 0.27730 0.23990 0.10010  0.02510  -0.03770 84  GLU B C   
3310 O O   . GLU B  90  ? 0.34420 0.26750 0.22240 0.09640  0.02490  -0.02880 84  GLU B O   
3311 C CB  . GLU B  90  ? 0.31860 0.23540 0.24220 0.09390  0.01380  -0.04450 84  GLU B CB  
3312 C CG  . GLU B  90  ? 0.32220 0.23960 0.27430 0.09070  0.01450  -0.04080 84  GLU B CG  
3313 C CD  . GLU B  90  ? 0.33940 0.25280 0.30910 0.08590  0.00460  -0.04380 84  GLU B CD  
3314 O OE1 . GLU B  90  ? 0.39410 0.30630 0.35630 0.08420  -0.00320 -0.04900 84  GLU B OE1 
3315 O OE2 . GLU B  90  ? 0.39600 0.30760 0.38870 0.08410  0.00490  -0.04040 84  GLU B OE2 
3316 N N   . ASP B  91  ? 0.36590 0.28000 0.22800 0.10790  0.02560  -0.04840 85  ASP B N   
3317 C CA  . ASP B  91  ? 0.40720 0.31970 0.23940 0.11280  0.02550  -0.04760 85  ASP B CA  
3318 C C   . ASP B  91  ? 0.44320 0.35660 0.27430 0.10870  0.01350  -0.04480 85  ASP B C   
3319 O O   . ASP B  91  ? 0.38210 0.29650 0.19980 0.10920  0.01550  -0.03600 85  ASP B O   
3320 C CB  . ASP B  91  ? 0.43690 0.34370 0.24570 0.12230  0.02490  -0.06170 85  ASP B CB  
3321 C CG  . ASP B  91  ? 0.48590 0.39290 0.28710 0.12850  0.04080  -0.06170 85  ASP B CG  
3322 O OD1 . ASP B  91  ? 0.47900 0.39130 0.29510 0.12500  0.05200  -0.05020 85  ASP B OD1 
3323 O OD2 . ASP B  91  ? 0.57350 0.47630 0.35410 0.13700  0.04200  -0.07410 85  ASP B OD2 
3324 N N   . ARG B  92  ? 0.37420 0.28760 0.22230 0.10440  0.00200  -0.05150 86  ARG B N   
3325 C CA  . ARG B  92  ? 0.41600 0.33200 0.26600 0.10080  -0.00840 -0.04900 86  ARG B CA  
3326 C C   . ARG B  92  ? 0.38850 0.30970 0.24910 0.09450  -0.00360 -0.03500 86  ARG B C   
3327 O O   . ARG B  92  ? 0.37800 0.30080 0.23210 0.09410  -0.00760 -0.03040 86  ARG B O   
3328 C CB  . ARG B  92  ? 0.39210 0.30820 0.26290 0.09650  -0.01980 -0.05800 86  ARG B CB  
3329 C CG  . ARG B  92  ? 0.37670 0.29310 0.27520 0.09060  -0.01580 -0.05570 86  ARG B CG  
3330 C CD  . ARG B  92  ? 0.34480 0.25970 0.26510 0.08620  -0.02590 -0.06370 86  ARG B CD  
3331 N NE  . ARG B  92  ? 0.39000 0.30320 0.33470 0.08220  -0.02150 -0.06050 86  ARG B NE  
3332 C CZ  . ARG B  92  ? 0.36320 0.27400 0.33210 0.07740  -0.02700 -0.06380 86  ARG B CZ  
3333 N NH1 . ARG B  92  ? 0.34210 0.25320 0.31710 0.07510  -0.03740 -0.07190 86  ARG B NH1 
3334 N NH2 . ARG B  92  ? 0.37810 0.28690 0.36750 0.07470  -0.02200 -0.05790 86  ARG B NH2 
3335 N N   . HIS B  93  ? 0.34240 0.26670 0.21960 0.09000  0.00420  -0.02880 87  HIS B N   
3336 C CA  . HIS B  93  ? 0.34180 0.27160 0.22830 0.08410  0.00790  -0.01760 87  HIS B CA  
3337 C C   . HIS B  93  ? 0.37720 0.30570 0.24740 0.08680  0.01590  -0.01050 87  HIS B C   
3338 O O   . HIS B  93  ? 0.37310 0.30300 0.24340 0.08390  0.01560  -0.00400 87  HIS B O   
3339 C CB  . HIS B  93  ? 0.31230 0.24700 0.21970 0.07940  0.01260  -0.01310 87  HIS B CB  
3340 C CG  . HIS B  93  ? 0.33490 0.27020 0.26050 0.07620  0.00610  -0.01660 87  HIS B CG  
3341 N ND1 . HIS B  93  ? 0.30320 0.23650 0.24080 0.07750  0.00820  -0.01950 87  HIS B ND1 
3342 C CD2 . HIS B  93  ? 0.30200 0.23940 0.23770 0.07160  -0.00140 -0.01660 87  HIS B CD2 
3343 C CE1 . HIS B  93  ? 0.36440 0.29740 0.31870 0.07370  0.00210  -0.02030 87  HIS B CE1 
3344 N NE2 . HIS B  93  ? 0.28000 0.21620 0.23340 0.06980  -0.00330 -0.01850 87  HIS B NE2 
3345 N N   . ILE B  94  ? 0.35420 0.28010 0.21280 0.09210  0.02460  -0.01110 88  ILE B N   
3346 C CA  . ILE B  94  ? 0.35020 0.27400 0.19310 0.09500  0.03380  -0.00320 88  ILE B CA  
3347 C C   . ILE B  94  ? 0.36260 0.28120 0.18370 0.09980  0.02740  -0.00300 88  ILE B C   
3348 O O   . ILE B  94  ? 0.36750 0.28440 0.18430 0.09890  0.03000  0.00600  88  ILE B O   
3349 C CB  . ILE B  94  ? 0.36020 0.28290 0.19420 0.10060  0.04550  -0.00450 88  ILE B CB  
3350 C CG1 . ILE B  94  ? 0.36360 0.29290 0.22340 0.09620  0.05130  -0.00350 88  ILE B CG1 
3351 C CG2 . ILE B  94  ? 0.37790 0.29750 0.19280 0.10440  0.05610  0.00470  88  ILE B CG2 
3352 C CD1 . ILE B  94  ? 0.40480 0.33470 0.26190 0.10210  0.06290  -0.00660 88  ILE B CD1 
3353 N N   . ALA B  95  ? 0.38160 0.29770 0.19030 0.10510  0.01810  -0.01320 89  ALA B N   
3354 C CA  . ALA B  95  ? 0.41510 0.32790 0.20280 0.11090  0.00990  -0.01360 89  ALA B CA  
3355 C C   . ALA B  95  ? 0.37150 0.28680 0.17280 0.10590  0.00200  -0.00920 89  ALA B C   
3356 O O   . ALA B  95  ? 0.40560 0.31810 0.19530 0.10910  0.00130  -0.00180 89  ALA B O   
3357 C CB  . ALA B  95  ? 0.43560 0.34720 0.21210 0.11660  -0.00100 -0.02810 89  ALA B CB  
3358 N N   . ARG B  96  ? 0.35370 0.27410 0.17980 0.09860  -0.00330 -0.01310 90  ARG B N   
3359 C CA  . ARG B  96  ? 0.35510 0.27900 0.19420 0.09430  -0.00900 -0.00950 90  ARG B CA  
3360 C C   . ARG B  96  ? 0.32260 0.24580 0.16580 0.09080  0.00020  0.00150  90  ARG B C   
3361 O O   . ARG B  96  ? 0.36920 0.29180 0.21350 0.09080  -0.00260 0.00550  90  ARG B O   
3362 C CB  . ARG B  96  ? 0.33100 0.26110 0.19470 0.08730  -0.01460 -0.01470 90  ARG B CB  
3363 C CG  . ARG B  96  ? 0.36420 0.29930 0.24060 0.08390  -0.02030 -0.01260 90  ARG B CG  
3364 C CD  . ARG B  96  ? 0.31480 0.25630 0.21320 0.07820  -0.02590 -0.01770 90  ARG B CD  
3365 N NE  . ARG B  96  ? 0.34400 0.28480 0.24220 0.08120  -0.03550 -0.02780 90  ARG B NE  
3366 C CZ  . ARG B  96  ? 0.37630 0.31910 0.27170 0.08500  -0.04570 -0.03250 90  ARG B CZ  
3367 N NH1 . ARG B  96  ? 0.36800 0.31310 0.26130 0.08680  -0.04690 -0.02710 90  ARG B NH1 
3368 N NH2 . ARG B  96  ? 0.37200 0.31490 0.26900 0.08720  -0.05550 -0.04350 90  ARG B NH2 
3369 N N   . THR B  97  ? 0.35050 0.27400 0.19840 0.08780  0.01090  0.00550  91  THR B N   
3370 C CA  . THR B  97  ? 0.30420 0.22690 0.15750 0.08410  0.01950  0.01470  91  THR B CA  
3371 C C   . THR B  97  ? 0.34660 0.26110 0.18080 0.09010  0.02320  0.02190  91  THR B C   
3372 O O   . THR B  97  ? 0.34500 0.25640 0.18320 0.08870  0.02350  0.02760  91  THR B O   
3373 C CB  . THR B  97  ? 0.30990 0.23600 0.17310 0.08050  0.02940  0.01680  91  THR B CB  
3374 O OG1 . THR B  97  ? 0.30400 0.23730 0.18480 0.07560  0.02510  0.01190  91  THR B OG1 
3375 C CG2 . THR B  97  ? 0.30370 0.22970 0.17630 0.07560  0.03750  0.02480  91  THR B CG2 
3376 N N   . ARG B  98  ? 0.36720 0.27760 0.17970 0.09770  0.02570  0.02170  92  ARG B N   
3377 C CA  . ARG B  98  ? 0.37200 0.27440 0.16240 0.10490  0.02900  0.03020  92  ARG B CA  
3378 C C   . ARG B  98  ? 0.42740 0.32790 0.21210 0.10900  0.01640  0.02960  92  ARG B C   
3379 O O   . ARG B  98  ? 0.46960 0.36360 0.24810 0.11200  0.01830  0.03930  92  ARG B O   
3380 C CB  . ARG B  98  ? 0.39510 0.29520 0.16030 0.11310  0.03370  0.02860  92  ARG B CB  
3381 C CG  . ARG B  98  ? 0.39250 0.29440 0.16440 0.11010  0.04900  0.03170  92  ARG B CG  
3382 C CD  . ARG B  98  ? 0.46880 0.36870 0.21480 0.11900  0.05600  0.02990  92  ARG B CD  
3383 N NE  . ARG B  98  ? 0.50480 0.40720 0.25920 0.11660  0.07280  0.03490  92  ARG B NE  
3384 C CZ  . ARG B  98  ? 0.59820 0.50380 0.34760 0.12040  0.07910  0.02790  92  ARG B CZ  
3385 N NH1 . ARG B  98  ? 0.55970 0.46530 0.29660 0.12580  0.06960  0.01440  92  ARG B NH1 
3386 N NH2 . ARG B  98  ? 0.52730 0.43630 0.28680 0.11850  0.09540  0.03370  92  ARG B NH2 
3387 N N   . ALA B  99  ? 0.39190 0.29790 0.18050 0.10960  0.00360  0.01880  93  ALA B N   
3388 C CA  . ALA B  99  ? 0.41950 0.32620 0.20730 0.11330  -0.00890 0.01740  93  ALA B CA  
3389 C C   . ALA B  99  ? 0.40150 0.30860 0.20990 0.10780  -0.00780 0.02250  93  ALA B C   
3390 O O   . ALA B  99  ? 0.40980 0.31300 0.21480 0.11240  -0.01150 0.02800  93  ALA B O   
3391 C CB  . ALA B  99  ? 0.38820 0.30220 0.18310 0.11300  -0.02200 0.00400  93  ALA B CB  
3392 N N   . MET B  100 ? 0.38190 0.29370 0.21140 0.09860  -0.00300 0.02020  94  MET B N   
3393 C CA  . MET B  100 ? 0.38050 0.29340 0.22840 0.09310  -0.00150 0.02280  94  MET B CA  
3394 C C   . MET B  100 ? 0.36780 0.27130 0.21220 0.09370  0.00820  0.03320  94  MET B C   
3395 O O   . MET B  100 ? 0.35730 0.25700 0.20900 0.09410  0.00730  0.03650  94  MET B O   
3396 C CB  . MET B  100 ? 0.33420 0.25530 0.20140 0.08400  0.00100  0.01790  94  MET B CB  
3397 C CG  . MET B  100 ? 0.35090 0.28030 0.22680 0.08230  -0.00770 0.00930  94  MET B CG  
3398 S SD  . MET B  100 ? 0.34710 0.28530 0.24210 0.07300  -0.00430 0.00660  94  MET B SD  
3399 C CE  . MET B  100 ? 0.29220 0.23340 0.20000 0.06800  -0.00120 0.00890  94  MET B CE  
3400 N N   . LEU B  101 ? 0.37760 0.27720 0.21350 0.09340  0.01830  0.03850  95  LEU B N   
3401 C CA  . LEU B  101 ? 0.37960 0.26940 0.21280 0.09410  0.02850  0.04970  95  LEU B CA  
3402 C C   . LEU B  101 ? 0.41590 0.29670 0.23140 0.10380  0.02480  0.05740  95  LEU B C   
3403 O O   . LEU B  101 ? 0.42370 0.29590 0.24490 0.10430  0.02800  0.06520  95  LEU B O   
3404 C CB  . LEU B  101 ? 0.38410 0.27320 0.21090 0.09310  0.04050  0.05400  95  LEU B CB  
3405 C CG  . LEU B  101 ? 0.37470 0.27120 0.22320 0.08340  0.04640  0.05030  95  LEU B CG  
3406 C CD1 . LEU B  101 ? 0.38020 0.27790 0.22170 0.08460  0.05730  0.05350  95  LEU B CD1 
3407 C CD2 . LEU B  101 ? 0.34040 0.23360 0.20890 0.07630  0.05140  0.05420  95  LEU B CD2 
3408 N N   . SER B  102 ? 0.41720 0.29980 0.21180 0.11200  0.01700  0.05470  96  SER B N   
3409 C CA  . SER B  102 ? 0.44900 0.32440 0.22500 0.12250  0.01160  0.06260  96  SER B CA  
3410 C C   . SER B  102 ? 0.43800 0.31410 0.23010 0.12310  0.00180  0.06070  96  SER B C   
3411 O O   . SER B  102 ? 0.43620 0.30340 0.22430 0.12920  0.00150  0.07070  96  SER B O   
3412 C CB  . SER B  102 ? 0.53200 0.41100 0.28190 0.13130  0.00300  0.05760  96  SER B CB  
3413 O OG  . SER B  102 ? 0.57160 0.44900 0.30460 0.13230  0.01390  0.05980  96  SER B OG  
3414 N N   . LYS B  103 ? 0.40990 0.29650 0.22110 0.11730  -0.00550 0.04860  97  LYS B N   
3415 C CA  . LYS B  103 ? 0.39130 0.28080 0.21920 0.11820  -0.01380 0.04580  97  LYS B CA  
3416 C C   . LYS B  103 ? 0.41210 0.29310 0.25520 0.11480  -0.00540 0.05210  97  LYS B C   
3417 O O   . LYS B  103 ? 0.43340 0.31090 0.28400 0.11970  -0.01000 0.05450  97  LYS B O   
3418 C CB  . LYS B  103 ? 0.39600 0.29890 0.24240 0.11180  -0.02030 0.03280  97  LYS B CB  
3419 C CG  . LYS B  103 ? 0.38520 0.29620 0.22340 0.11560  -0.03180 0.02480  97  LYS B CG  
3420 C CD  . LYS B  103 ? 0.38720 0.31070 0.24830 0.10890  -0.03720 0.01390  97  LYS B CD  
3421 C CE  . LYS B  103 ? 0.39300 0.32370 0.25020 0.11210  -0.04940 0.00510  97  LYS B CE  
3422 N NZ  . LYS B  103 ? 0.37850 0.32040 0.25890 0.10450  -0.05270 -0.00420 97  LYS B NZ  
3423 N N   . ILE B  104 ? 0.36940 0.24730 0.21960 0.10670  0.00620  0.05370  98  ILE B N   
3424 C CA  . ILE B  104 ? 0.37220 0.24140 0.23840 0.10270  0.01380  0.05780  98  ILE B CA  
3425 C C   . ILE B  104 ? 0.42680 0.28150 0.28290 0.10560  0.02400  0.07210  98  ILE B C   
3426 O O   . ILE B  104 ? 0.41610 0.26200 0.28710 0.10100  0.03200  0.07580  98  ILE B O   
3427 C CB  . ILE B  104 ? 0.39100 0.26740 0.27640 0.09110  0.01860  0.04900  98  ILE B CB  
3428 C CG1 . ILE B  104 ? 0.38890 0.26630 0.27050 0.08550  0.02760  0.05160  98  ILE B CG1 
3429 C CG2 . ILE B  104 ? 0.33750 0.22860 0.23070 0.08860  0.00990  0.03710  98  ILE B CG2 
3430 C CD1 . ILE B  104 ? 0.33650 0.22020 0.23790 0.07480  0.03170  0.04460  98  ILE B CD1 
3431 N N   . LYS B  105 ? 0.41330 0.26500 0.24450 0.11340  0.02410  0.08000  99  LYS B N   
3432 C CA  . LYS B  105 ? 0.45390 0.29210 0.27240 0.11700  0.03540  0.09590  99  LYS B CA  
3433 C C   . LYS B  105 ? 0.49200 0.32790 0.32580 0.10650  0.05000  0.09790  99  LYS B C   
3434 O O   . LYS B  105 ? 0.51160 0.33530 0.35560 0.10440  0.05960  0.10780  99  LYS B O   
3435 C CB  . LYS B  105 ? 0.50410 0.32870 0.32420 0.12440  0.03390  0.10700  99  LYS B CB  
3436 C CG  . LYS B  105 ? 0.49180 0.31970 0.29600 0.13640  0.01920  0.10690  99  LYS B CG  
3437 C CD  . LYS B  105 ? 0.53110 0.34770 0.33590 0.14380  0.01800  0.11940  99  LYS B CD  
3438 C CE  . LYS B  105 ? 0.51810 0.34440 0.31310 0.15300  0.00130  0.11570  99  LYS B CE  
3439 N NZ  . LYS B  105 ? 0.55210 0.37090 0.35020 0.15950  -0.00160 0.12680  99  LYS B NZ  
3440 N N   . ALA B  106 ? 0.47010 0.31800 0.30750 0.09990  0.05130  0.08840  100 ALA B N   
3441 C CA  . ALA B  106 ? 0.43000 0.27930 0.28210 0.09050  0.06360  0.08940  100 ALA B CA  
3442 C C   . ALA B  106 ? 0.47720 0.33180 0.31170 0.09290  0.07010  0.09170  100 ALA B C   
3443 O O   . ALA B  106 ? 0.45120 0.30840 0.26200 0.10110  0.06420  0.09020  100 ALA B O   
3444 C CB  . ALA B  106 ? 0.41870 0.27880 0.29550 0.08030  0.05930  0.07570  100 ALA B CB  
3445 N N   . GLU B  107 ? 0.46510 0.32200 0.31310 0.08580  0.08220  0.09390  101 GLU B N   
3446 C CA  . GLU B  107 ? 0.50140 0.36290 0.33680 0.08790  0.09190  0.09710  101 GLU B CA  
3447 C C   . GLU B  107 ? 0.47090 0.34610 0.32630 0.07950  0.09250  0.08640  101 GLU B C   
3448 O O   . GLU B  107 ? 0.42200 0.30150 0.30230 0.07080  0.08910  0.08030  101 GLU B O   
3449 C CB  . GLU B  107 ? 0.50840 0.36020 0.34330 0.08810  0.10920  0.11320  101 GLU B CB  
3450 C CG  . GLU B  107 ? 0.64670 0.48280 0.47180 0.09390  0.11020  0.12630  101 GLU B CG  
3451 C CD  . GLU B  107 ? 0.76700 0.59830 0.55400 0.10700  0.11100  0.13570  101 GLU B CD  
3452 O OE1 . GLU B  107 ? 0.76030 0.60000 0.52740 0.11290  0.10120  0.12590  101 GLU B OE1 
3453 O OE2 . GLU B  107 ? 0.89280 0.71750 0.67730 0.10910  0.11830  0.14730  101 GLU B OE2 
3454 N N   . GLU B  108 ? 0.42610 0.30810 0.27020 0.08280  0.09710  0.08440  102 GLU B N   
3455 C CA  . GLU B  108 ? 0.39480 0.28950 0.25960 0.07590  0.09910  0.07660  102 GLU B CA  
3456 C C   . GLU B  108 ? 0.39950 0.29570 0.29310 0.06650  0.10900  0.08140  102 GLU B C   
3457 O O   . GLU B  108 ? 0.42190 0.32790 0.33940 0.05860  0.10450  0.07380  102 GLU B O   
3458 C CB  . GLU B  108 ? 0.43730 0.33700 0.28700 0.08200  0.10570  0.07520  102 GLU B CB  
3459 C CG  . GLU B  108 ? 0.48710 0.38500 0.30900 0.09120  0.09560  0.06870  102 GLU B CG  
3460 C CD  . GLU B  108 ? 0.54650 0.44930 0.35510 0.09710  0.10130  0.06390  102 GLU B CD  
3461 O OE1 . GLU B  108 ? 0.43960 0.34900 0.26340 0.09400  0.11310  0.06510  102 GLU B OE1 
3462 O OE2 . GLU B  108 ? 0.52420 0.42440 0.30800 0.10520  0.09350  0.05810  102 GLU B OE2 
3463 N N   . ALA B  109 ? 0.41580 0.30270 0.30800 0.06710  0.12220  0.09430  103 ALA B N   
3464 C CA  . ALA B  109 ? 0.39380 0.28110 0.31720 0.05720  0.13150  0.09870  103 ALA B CA  
3465 C C   . ALA B  109 ? 0.37910 0.26580 0.32450 0.04920  0.12060  0.09080  103 ALA B C   
3466 O O   . ALA B  109 ? 0.37230 0.26390 0.34720 0.03970  0.12370  0.08850  103 ALA B O   
3467 C CB  . ALA B  109 ? 0.40630 0.28050 0.32430 0.05940  0.14730  0.11560  103 ALA B CB  
3468 N N   . ASP B  110 ? 0.36160 0.24340 0.29430 0.05290  0.10780  0.08580  104 ASP B N   
3469 C CA  . ASP B  110 ? 0.41090 0.29280 0.36210 0.04640  0.09830  0.07710  104 ASP B CA  
3470 C C   . ASP B  110 ? 0.34960 0.24770 0.31190 0.04140  0.08820  0.06350  104 ASP B C   
3471 O O   . ASP B  110 ? 0.32200 0.22310 0.30150 0.03490  0.08200  0.05550  104 ASP B O   
3472 C CB  . ASP B  110 ? 0.38640 0.25780 0.32210 0.05290  0.08960  0.07730  104 ASP B CB  
3473 C CG  . ASP B  110 ? 0.45370 0.30800 0.37980 0.05840  0.09820  0.09210  104 ASP B CG  
3474 O OD1 . ASP B  110 ? 0.48960 0.33640 0.43460 0.05260  0.10840  0.09870  104 ASP B OD1 
3475 O OD2 . ASP B  110 ? 0.44310 0.29150 0.34350 0.06850  0.09460  0.09740  104 ASP B OD2 
3476 N N   . LEU B  111 ? 0.35710 0.26510 0.30960 0.04470  0.08670  0.06090  105 LEU B N   
3477 C CA  . LEU B  111 ? 0.31730 0.23990 0.28020 0.04080  0.07780  0.05060  105 LEU B CA  
3478 C C   . LEU B  111 ? 0.35500 0.28700 0.34580 0.03200  0.08170  0.04870  105 LEU B C   
3479 O O   . LEU B  111 ? 0.37720 0.30820 0.37780 0.03030  0.09350  0.05570  105 LEU B O   
3480 C CB  . LEU B  111 ? 0.33910 0.26800 0.28770 0.04690  0.07650  0.04910  105 LEU B CB  
3481 C CG  . LEU B  111 ? 0.35200 0.27460 0.27620 0.05470  0.06940  0.04770  105 LEU B CG  
3482 C CD1 . LEU B  111 ? 0.40000 0.32650 0.31120 0.06070  0.06950  0.04550  105 LEU B CD1 
3483 C CD2 . LEU B  111 ? 0.32820 0.25370 0.25620 0.05230  0.05690  0.04010  105 LEU B CD2 
3484 N N   . ARG B  112 ? 0.32420 0.26630 0.32810 0.02650  0.07180  0.03950  106 ARG B N   
3485 C CA  . ARG B  112 ? 0.32310 0.27690 0.35390 0.01840  0.07230  0.03590  106 ARG B CA  
3486 C C   . ARG B  112 ? 0.31450 0.28490 0.35020 0.01870  0.06600  0.03160  106 ARG B C   
3487 O O   . ARG B  112 ? 0.27450 0.25770 0.33190 0.01270  0.06260  0.02730  106 ARG B O   
3488 C CB  . ARG B  112 ? 0.31870 0.27100 0.36270 0.01160  0.06590  0.02810  106 ARG B CB  
3489 C CG  . ARG B  112 ? 0.35150 0.28670 0.39950 0.01030  0.07410  0.03340  106 ARG B CG  
3490 C CD  . ARG B  112 ? 0.41200 0.34650 0.48080 0.00560  0.08710  0.04110  106 ARG B CD  
3491 N NE  . ARG B  112 ? 0.45290 0.36880 0.52340 0.00540  0.09650  0.04940  106 ARG B NE  
3492 C CZ  . ARG B  112 ? 0.43900 0.34270 0.49020 0.01280  0.10610  0.06230  106 ARG B CZ  
3493 N NH1 . ARG B  112 ? 0.39680 0.30500 0.42570 0.02060  0.10780  0.06650  106 ARG B NH1 
3494 N NH2 . ARG B  112 ? 0.48710 0.37350 0.54130 0.01270  0.11400  0.07110  106 ARG B NH2 
3495 N N   . CYS B  113 ? 0.25100 0.22130 0.26810 0.02580  0.06380  0.03270  107 CYS B N   
3496 C CA  . CYS B  113 ? 0.27000 0.25260 0.29080 0.02790  0.06010  0.03110  107 CYS B CA  
3497 C C   . CYS B  113 ? 0.32220 0.30480 0.34430 0.03220  0.07170  0.03670  107 CYS B C   
3498 O O   . CYS B  113 ? 0.29990 0.27200 0.31190 0.03490  0.08180  0.04230  107 CYS B O   
3499 C CB  . CYS B  113 ? 0.26520 0.24590 0.26760 0.03280  0.05150  0.02830  107 CYS B CB  
3500 S SG  . CYS B  113 ? 0.29470 0.25930 0.26970 0.04080  0.05500  0.03130  107 CYS B SG  
3501 N N   . GLY B  114 ? 0.30940 0.30420 0.34350 0.03340  0.07070  0.03560  108 GLY B N   
3502 C CA  . GLY B  114 ? 0.27170 0.26910 0.31110 0.03750  0.08260  0.03960  108 GLY B CA  
3503 C C   . GLY B  114 ? 0.28870 0.28760 0.31880 0.04490  0.07990  0.03740  108 GLY B C   
3504 O O   . GLY B  114 ? 0.23580 0.23700 0.26300 0.04530  0.06840  0.03380  108 GLY B O   
3505 N N   . GLY B  115 ? 0.29970 0.29700 0.32610 0.05100  0.09160  0.03950  109 GLY B N   
3506 C CA  . GLY B  115 ? 0.28770 0.28400 0.30540 0.05870  0.09010  0.03580  109 GLY B CA  
3507 C C   . GLY B  115 ? 0.26780 0.27790 0.31010 0.05860  0.08540  0.03430  109 GLY B C   
3508 O O   . GLY B  115 ? 0.25980 0.28240 0.32650 0.05330  0.08510  0.03620  109 GLY B O   
3509 N N   . HIS B  116 ? 0.27450 0.28220 0.31190 0.06470  0.08140  0.03060  110 HIS B N   
3510 C CA  . HIS B  116 ? 0.23440 0.25340 0.29460 0.06630  0.07660  0.03050  110 HIS B CA  
3511 C C   . HIS B  116 ? 0.29040 0.30190 0.34300 0.07490  0.07770  0.02600  110 HIS B C   
3512 O O   . HIS B  116 ? 0.29140 0.28970 0.32020 0.07800  0.07800  0.02190  110 HIS B O   
3513 C CB  . HIS B  116 ? 0.22070 0.24580 0.28730 0.06090  0.06180  0.03180  110 HIS B CB  
3514 C CG  . HIS B  116 ? 0.26950 0.28300 0.31390 0.06060  0.05390  0.02970  110 HIS B CG  
3515 N ND1 . HIS B  116 ? 0.29790 0.30400 0.33560 0.06570  0.05030  0.02730  110 HIS B ND1 
3516 C CD2 . HIS B  116 ? 0.27810 0.28610 0.30810 0.05590  0.04970  0.02920  110 HIS B CD2 
3517 C CE1 . HIS B  116 ? 0.25630 0.25420 0.27730 0.06360  0.04400  0.02580  110 HIS B CE1 
3518 N NE2 . HIS B  116 ? 0.26940 0.26870 0.28510 0.05810  0.04360  0.02690  110 HIS B NE2 
3519 N N   . PRO B  117 ? 0.27950 0.29890 0.35350 0.07900  0.07720  0.02610  111 PRO B N   
3520 C CA  . PRO B  117 ? 0.28170 0.29220 0.35150 0.08680  0.07710  0.02080  111 PRO B CA  
3521 C C   . PRO B  117 ? 0.27620 0.27610 0.33100 0.08500  0.06530  0.01910  111 PRO B C   
3522 O O   . PRO B  117 ? 0.28080 0.28510 0.33850 0.07910  0.05540  0.02380  111 PRO B O   
3523 C CB  . PRO B  117 ? 0.26890 0.29150 0.36940 0.09030  0.07570  0.02370  111 PRO B CB  
3524 C CG  . PRO B  117 ? 0.28470 0.32260 0.40330 0.08670  0.08220  0.02790  111 PRO B CG  
3525 C CD  . PRO B  117 ? 0.23400 0.27090 0.33880 0.07750  0.07730  0.03030  111 PRO B CD  
3526 N N   . SER B  118 ? 0.29600 0.28260 0.33480 0.09000  0.06660  0.01180  112 SER B N   
3527 C CA  . SER B  118 ? 0.25620 0.23320 0.28290 0.08770  0.05610  0.00950  112 SER B CA  
3528 C C   . SER B  118 ? 0.31400 0.29440 0.35950 0.08610  0.04690  0.01470  112 SER B C   
3529 O O   . SER B  118 ? 0.27720 0.26300 0.34340 0.09000  0.04830  0.01720  112 SER B O   
3530 C CB  . SER B  118 ? 0.32400 0.28730 0.33500 0.09380  0.05780  -0.00100 112 SER B CB  
3531 O OG  . SER B  118 ? 0.32310 0.27880 0.33140 0.09120  0.04720  -0.00310 112 SER B OG  
3532 N N   . LEU B  119 ? 0.29750 0.27520 0.33600 0.08080  0.03800  0.01720  113 LEU B N   
3533 C CA  . LEU B  119 ? 0.30360 0.28260 0.35570 0.07940  0.02990  0.02330  113 LEU B CA  
3534 C C   . LEU B  119 ? 0.32920 0.29600 0.38800 0.08420  0.02900  0.01850  113 LEU B C   
3535 O O   . LEU B  119 ? 0.35210 0.31860 0.42580 0.08420  0.02400  0.02510  113 LEU B O   
3536 C CB  . LEU B  119 ? 0.31310 0.29320 0.35510 0.07260  0.02270  0.02710  113 LEU B CB  
3537 C CG  . LEU B  119 ? 0.28510 0.27690 0.32330 0.06720  0.02130  0.03170  113 LEU B CG  
3538 C CD1 . LEU B  119 ? 0.28170 0.27330 0.31050 0.06180  0.01490  0.03420  113 LEU B CD1 
3539 C CD2 . LEU B  119 ? 0.34840 0.35320 0.40490 0.06800  0.01970  0.03850  113 LEU B CD2 
3540 N N   . SER B  120 ? 0.27920 0.23580 0.32720 0.08830  0.03340  0.00740  114 SER B N   
3541 C CA  . SER B  120 ? 0.35210 0.29600 0.40680 0.09320  0.03290  -0.00080 114 SER B CA  
3542 C C   . SER B  120 ? 0.31570 0.25980 0.37970 0.10140  0.04170  -0.00590 114 SER B C   
3543 O O   . SER B  120 ? 0.30760 0.25570 0.35960 0.10400  0.04990  -0.00970 114 SER B O   
3544 C CB  . SER B  120 ? 0.34320 0.27650 0.37800 0.09270  0.03040  -0.01230 114 SER B CB  
3545 O OG  . SER B  120 ? 0.34600 0.26770 0.38480 0.09880  0.03160  -0.02440 114 SER B OG  
3546 N N   . GLU B  121 ? 0.39400 0.18340 0.47400 0.09330  0.01810  0.01620  115 GLU B N   
3547 C CA  . GLU B  121 ? 0.43000 0.21920 0.51930 0.10730  0.02090  0.00740  115 GLU B CA  
3548 C C   . GLU B  121 ? 0.47190 0.25860 0.56080 0.10420  0.02390  -0.01810 115 GLU B C   
3549 O O   . GLU B  121 ? 0.45700 0.25610 0.54370 0.11270  0.02670  -0.02840 115 GLU B O   
3550 C CB  . GLU B  121 ? 0.55060 0.31170 0.65350 0.12020  0.02520  0.01840  115 GLU B CB  
3551 C CG  . GLU B  121 ? 0.67330 0.44530 0.78630 0.13940  0.02440  0.01710  115 GLU B CG  
3552 C CD  . GLU B  121 ? 0.86870 0.64600 0.98100 0.15580  0.01810  0.03870  115 GLU B CD  
3553 O OE1 . GLU B  121 ? 0.89620 0.64830 1.00200 0.16090  0.01790  0.04980  115 GLU B OE1 
3554 O OE2 . GLU B  121 ? 0.84090 0.65470 0.95240 0.15900  0.01050  0.04020  115 GLU B OE2 
3555 N N   . MET B  122 ? 0.45000 0.22420 0.54070 0.09270  0.02340  -0.03080 116 MET B N   
3556 C CA  . MET B  122 ? 0.45240 0.22740 0.54150 0.09310  0.02300  -0.05930 116 MET B CA  
3557 C C   . MET B  122 ? 0.43570 0.23690 0.49630 0.09460  0.01860  -0.06560 116 MET B C   
3558 O O   . MET B  122 ? 0.45270 0.25930 0.50100 0.10380  0.02100  -0.08210 116 MET B O   
3559 C CB  . MET B  122 ? 0.47710 0.23630 0.58340 0.08090  0.02240  -0.07650 116 MET B CB  
3560 C CG  . MET B  122 ? 0.63970 0.36430 0.77690 0.08180  0.03280  -0.08150 116 MET B CG  
3561 S SD  . MET B  122 ? 0.79130 0.50910 0.93210 0.09990  0.03770  -0.09000 116 MET B SD  
3562 C CE  . MET B  122 ? 0.76550 0.46860 0.92610 0.09030  0.04130  -0.11950 116 MET B CE  
3563 N N   . VAL B  123 ? 0.42170 0.23690 0.46920 0.08690  0.01420  -0.05210 117 VAL B N   
3564 C CA  . VAL B  123 ? 0.38180 0.21600 0.40080 0.09020  0.01370  -0.05310 117 VAL B CA  
3565 C C   . VAL B  123 ? 0.40910 0.25190 0.42580 0.09900  0.02370  -0.04430 117 VAL B C   
3566 O O   . VAL B  123 ? 0.44790 0.29530 0.44530 0.10730  0.03120  -0.05310 117 VAL B O   
3567 C CB  . VAL B  123 ? 0.39530 0.24030 0.40530 0.08000  0.00790  -0.04080 117 VAL B CB  
3568 C CG1 . VAL B  123 ? 0.35490 0.21360 0.33550 0.08480  0.01120  -0.03780 117 VAL B CG1 
3569 C CG2 . VAL B  123 ? 0.42970 0.27040 0.44700 0.07120  -0.00080 -0.05440 117 VAL B CG2 
3570 N N   . ASN B  124 ? 0.36790 0.21340 0.40470 0.09890  0.02470  -0.02860 118 ASN B N   
3571 C CA  . ASN B  124 ? 0.40310 0.26350 0.44690 0.10640  0.03340  -0.02470 118 ASN B CA  
3572 C C   . ASN B  124 ? 0.42250 0.27670 0.47040 0.11780  0.04210  -0.03990 118 ASN B C   
3573 O O   . ASN B  124 ? 0.41820 0.28390 0.46140 0.12280  0.05450  -0.04420 118 ASN B O   
3574 C CB  . ASN B  124 ? 0.39230 0.26110 0.45870 0.10860  0.02870  -0.00980 118 ASN B CB  
3575 C CG  . ASN B  124 ? 0.44660 0.34250 0.52230 0.10970  0.03440  -0.00710 118 ASN B CG  
3576 O OD1 . ASN B  124 ? 0.35580 0.26190 0.41890 0.10130  0.03910  -0.00590 118 ASN B OD1 
3577 N ND2 . ASN B  124 ? 0.37950 0.28720 0.48010 0.12080  0.03540  -0.00890 118 ASN B ND2 
3578 N N   . ARG B  125 ? 0.40450 0.23930 0.46300 0.12150  0.03860  -0.04940 119 ARG B N   
3579 C CA  . ARG B  125 ? 0.42810 0.25690 0.49040 0.13280  0.04670  -0.06700 119 ARG B CA  
3580 C C   . ARG B  125 ? 0.44150 0.27460 0.47150 0.13560  0.05250  -0.08250 119 ARG B C   
3581 O O   . ARG B  125 ? 0.46970 0.30790 0.49280 0.14510  0.06540  -0.09080 119 ARG B O   
3582 C CB  . ARG B  125 ? 0.46600 0.27010 0.54690 0.13470  0.04280  -0.07660 119 ARG B CB  
3583 C CG  . ARG B  125 ? 0.50110 0.29430 0.60620 0.13780  0.04030  -0.05870 119 ARG B CG  
3584 C CD  . ARG B  125 ? 0.56390 0.32570 0.68880 0.14190  0.04270  -0.06910 119 ARG B CD  
3585 N NE  . ARG B  125 ? 0.70710 0.44790 0.84320 0.14120  0.04090  -0.04830 119 ARG B NE  
3586 C CZ  . ARG B  125 ? 0.73100 0.47540 0.87060 0.15310  0.03840  -0.02860 119 ARG B CZ  
3587 N NH1 . ARG B  125 ? 0.68430 0.45470 0.82970 0.16530  0.03790  -0.02890 119 ARG B NH1 
3588 N NH2 . ARG B  125 ? 0.80440 0.52750 0.94160 0.15340  0.03660  -0.00990 119 ARG B NH2 
3589 N N   . SER B  126 ? 0.44200 0.27270 0.45060 0.12970  0.04360  -0.08770 120 SER B N   
3590 C CA  A SER B  126 ? 0.47940 0.31450 0.44870 0.13750  0.04710  -0.10020 120 SER B CA  
3591 C CA  B SER B  126 ? 0.47960 0.31470 0.44890 0.13750  0.04710  -0.10010 120 SER B CA  
3592 C C   . SER B  126 ? 0.46370 0.30850 0.41310 0.14040  0.06300  -0.08550 120 SER B C   
3593 O O   . SER B  126 ? 0.57650 0.42030 0.50130 0.15190  0.07760  -0.09290 120 SER B O   
3594 C CB  A SER B  126 ? 0.46780 0.30390 0.42020 0.13260  0.03200  -0.10690 120 SER B CB  
3595 C CB  B SER B  126 ? 0.46760 0.30380 0.42000 0.13270  0.03210  -0.10700 120 SER B CB  
3596 O OG  A SER B  126 ? 0.45050 0.29460 0.39270 0.12490  0.03120  -0.08660 120 SER B OG  
3597 O OG  B SER B  126 ? 0.57370 0.41340 0.48300 0.14650  0.03300  -0.12050 120 SER B OG  
3598 N N   . TRP B  127 ? 0.42960 0.28280 0.39070 0.12990  0.06290  -0.06590 121 TRP B N   
3599 C CA  . TRP B  127 ? 0.44060 0.30230 0.39200 0.12950  0.08070  -0.05430 121 TRP B CA  
3600 C C   . TRP B  127 ? 0.43700 0.30490 0.40920 0.13540  0.09880  -0.05860 121 TRP B C   
3601 O O   . TRP B  127 ? 0.45500 0.32230 0.40930 0.14030  0.12090  -0.05880 121 TRP B O   
3602 C CB  . TRP B  127 ? 0.42520 0.29790 0.39500 0.11640  0.07500  -0.03750 121 TRP B CB  
3603 C CG  . TRP B  127 ? 0.42470 0.29390 0.37340 0.11030  0.06190  -0.03230 121 TRP B CG  
3604 C CD1 . TRP B  127 ? 0.40430 0.26460 0.32250 0.11610  0.05280  -0.04250 121 TRP B CD1 
3605 C CD2 . TRP B  127 ? 0.41260 0.29090 0.37200 0.09860  0.05570  -0.01870 121 TRP B CD2 
3606 N NE1 . TRP B  127 ? 0.42870 0.29220 0.34020 0.10830  0.04160  -0.03520 121 TRP B NE1 
3607 C CE2 . TRP B  127 ? 0.36160 0.23460 0.29670 0.09700  0.04440  -0.01980 121 TRP B CE2 
3608 C CE3 . TRP B  127 ? 0.36180 0.25540 0.35000 0.09070  0.05740  -0.00850 121 TRP B CE3 
3609 C CZ2 . TRP B  127 ? 0.38110 0.26080 0.32000 0.08680  0.03720  -0.00930 121 TRP B CZ2 
3610 C CZ3 . TRP B  127 ? 0.34320 0.24380 0.33210 0.08070  0.04940  0.00120  121 TRP B CZ3 
3611 C CH2 . TRP B  127 ? 0.35620 0.24840 0.32040 0.07840  0.04050  0.00160  121 TRP B CH2 
3612 N N   . ILE B  128 ? 0.42440 0.29710 0.43500 0.13600  0.09140  -0.06130 122 ILE B N   
3613 C CA  . ILE B  128 ? 0.42990 0.31370 0.46850 0.14280  0.10600  -0.06750 122 ILE B CA  
3614 C C   . ILE B  128 ? 0.46520 0.33880 0.48100 0.15440  0.12120  -0.08330 122 ILE B C   
3615 O O   . ILE B  128 ? 0.47860 0.35980 0.49740 0.15840  0.14450  -0.08710 122 ILE B O   
3616 C CB  . ILE B  128 ? 0.41890 0.30610 0.49690 0.14640  0.09180  -0.06700 122 ILE B CB  
3617 C CG1 . ILE B  128 ? 0.38980 0.29280 0.48780 0.13890  0.08070  -0.05160 122 ILE B CG1 
3618 C CG2 . ILE B  128 ? 0.43180 0.32860 0.53780 0.15800  0.10420  -0.07910 122 ILE B CG2 
3619 C CD1 . ILE B  128 ? 0.38760 0.28480 0.50750 0.14520  0.06320  -0.04510 122 ILE B CD1 
3620 N N   . LYS B  129 ? 0.48350 0.34130 0.47800 0.15990  0.10950  -0.09520 123 LYS B N   
3621 C CA  . LYS B  129 ? 0.52120 0.37120 0.49060 0.17340  0.12130  -0.11370 123 LYS B CA  
3622 C C   . LYS B  129 ? 0.54620 0.39400 0.46910 0.17890  0.14200  -0.10950 123 LYS B C   
3623 O O   . LYS B  129 ? 0.57590 0.42570 0.48610 0.18610  0.15930  -0.11780 123 LYS B O   
3624 C CB  . LYS B  129 ? 0.53700 0.37420 0.49340 0.17750  0.10260  -0.13150 123 LYS B CB  
3625 C CG  . LYS B  129 ? 0.52950 0.35940 0.52960 0.17560  0.09090  -0.13880 123 LYS B CG  
3626 C CD  . LYS B  129 ? 0.55140 0.36920 0.54280 0.17860  0.07810  -0.16240 123 LYS B CD  
3627 C CE  . LYS B  129 ? 0.55920 0.36190 0.59420 0.17360  0.06880  -0.16690 123 LYS B CE  
3628 N NZ  . LYS B  129 ? 0.67580 0.47050 0.70880 0.17520  0.06660  -0.19160 123 LYS B NZ  
3629 N N   . GLN B  130 ? 0.53710 0.38290 0.43600 0.17260  0.13840  -0.09470 124 GLN B N   
3630 C CA  . GLN B  130 ? 0.61680 0.45460 0.46650 0.17910  0.15780  -0.08660 124 GLN B CA  
3631 C C   . GLN B  130 ? 0.59160 0.43550 0.46010 0.16810  0.18240  -0.06950 124 GLN B C   
3632 O O   . GLN B  130 ? 0.66610 0.50120 0.50050 0.16800  0.19860  -0.05720 124 GLN B O   
3633 C CB  . GLN B  130 ? 0.66630 0.49550 0.47500 0.18300  0.14020  -0.08300 124 GLN B CB  
3634 C CG  . GLN B  130 ? 0.71820 0.54760 0.51760 0.19060  0.11340  -0.10510 124 GLN B CG  
3635 C CD  . GLN B  130 ? 0.89860 0.72860 0.67790 0.18990  0.09050  -0.10450 124 GLN B CD  
3636 O OE1 . GLN B  130 ? 0.82650 0.65650 0.60210 0.18190  0.09190  -0.08500 124 GLN B OE1 
3637 N NE2 . GLN B  130 ? 0.99710 0.83180 0.77120 0.19600  0.06840  -0.12790 124 GLN B NE2 
3638 N N   . ASP B  131 ? 0.54680 0.40690 0.47210 0.15820  0.18370  -0.06910 125 ASP B N   
3639 C CA  . ASP B  131 ? 0.52700 0.39990 0.48260 0.14600  0.20470  -0.05930 125 ASP B CA  
3640 C C   . ASP B  131 ? 0.55550 0.41990 0.48920 0.13810  0.20540  -0.04290 125 ASP B C   
3641 O O   . ASP B  131 ? 0.52270 0.38620 0.45840 0.12920  0.22800  -0.03380 125 ASP B O   
3642 C CB  . ASP B  131 ? 0.55390 0.42930 0.50720 0.14470  0.23220  -0.06180 125 ASP B CB  
3643 C CG  . ASP B  131 ? 0.53710 0.43250 0.53570 0.14720  0.23340  -0.07810 125 ASP B CG  
3644 O OD1 . ASP B  131 ? 0.50350 0.42220 0.55780 0.14100  0.22700  -0.08210 125 ASP B OD1 
3645 O OD2 . ASP B  131 ? 0.57000 0.45980 0.54840 0.15690  0.23990  -0.08780 125 ASP B OD2 
3646 N N   . PHE B  132 ? 0.48490 0.34580 0.40280 0.13690  0.17590  -0.03890 126 PHE B N   
3647 C CA  . PHE B  132 ? 0.52080 0.37470 0.41750 0.13070  0.17170  -0.02480 126 PHE B CA  
3648 C C   . PHE B  132 ? 0.49860 0.37250 0.44360 0.11320  0.16890  -0.01820 126 PHE B C   
3649 O O   . PHE B  132 ? 0.48200 0.37500 0.46680 0.10770  0.14960  -0.02250 126 PHE B O   
3650 C CB  . PHE B  132 ? 0.47340 0.32150 0.34370 0.13520  0.14110  -0.02720 126 PHE B CB  
3651 C CG  . PHE B  132 ? 0.50790 0.35210 0.36080 0.12970  0.13310  -0.01470 126 PHE B CG  
3652 C CD1 . PHE B  132 ? 0.54160 0.36670 0.34700 0.13950  0.14980  -0.00520 126 PHE B CD1 
3653 C CD2 . PHE B  132 ? 0.43620 0.29320 0.31660 0.11700  0.10950  -0.01190 126 PHE B CD2 
3654 C CE1 . PHE B  132 ? 0.55090 0.37150 0.34120 0.13660  0.14150  0.00540  126 PHE B CE1 
3655 C CE2 . PHE B  132 ? 0.50310 0.35790 0.36930 0.11230  0.10220  -0.00230 126 PHE B CE2 
3656 C CZ  . PHE B  132 ? 0.50420 0.34160 0.32730 0.12210  0.11710  0.00560  126 PHE B CZ  
3657 N N   . ILE B  133 ? 0.45300 0.32080 0.39210 0.10660  0.18920  -0.00820 127 ILE B N   
3658 C CA  . ILE B  133 ? 0.41380 0.30060 0.39480 0.09030  0.18730  -0.00480 127 ILE B CA  
3659 C C   . ILE B  133 ? 0.44510 0.32380 0.40070 0.08730  0.16780  0.00580  127 ILE B C   
3660 O O   . ILE B  133 ? 0.46570 0.32130 0.38100 0.09200  0.18110  0.01560  127 ILE B O   
3661 C CB  . ILE B  133 ? 0.44430 0.32940 0.44500 0.08250  0.22560  -0.00440 127 ILE B CB  
3662 C CG1 . ILE B  133 ? 0.51430 0.41320 0.54780 0.08360  0.24250  -0.01770 127 ILE B CG1 
3663 C CG2 . ILE B  133 ? 0.46100 0.36750 0.50560 0.06570  0.22140  -0.00520 127 ILE B CG2 
3664 C CD1 . ILE B  133 ? 0.57870 0.47320 0.62800 0.07040  0.27130  -0.01680 127 ILE B CD1 
3665 N N   . PRO B  134 ? 0.40450 0.29950 0.37940 0.08150  0.13820  0.00500  128 PRO B N   
3666 C CA  . PRO B  134 ? 0.40090 0.29080 0.35630 0.07760  0.12180  0.01320  128 PRO B CA  
3667 C C   . PRO B  134 ? 0.38360 0.27350 0.34750 0.06780  0.13830  0.02000  128 PRO B C   
3668 O O   . PRO B  134 ? 0.34630 0.25160 0.34970 0.05870  0.15370  0.01510  128 PRO B O   
3669 C CB  . PRO B  134 ? 0.37650 0.28530 0.35970 0.07180  0.09410  0.01100  128 PRO B CB  
3670 C CG  . PRO B  134 ? 0.31040 0.23790 0.33340 0.07180  0.09770  0.00360  128 PRO B CG  
3671 C CD  . PRO B  134 ? 0.35510 0.27300 0.37100 0.07950  0.12130  -0.00250 128 PRO B CD  
3672 N N   . THR B  135 ? 0.40900 0.28310 0.33950 0.07010  0.13430  0.02870  129 THR B N   
3673 C CA  . THR B  135 ? 0.38980 0.25580 0.32120 0.06290  0.15100  0.03630  129 THR B CA  
3674 C C   . THR B  135 ? 0.34940 0.22590 0.28460 0.05600  0.12680  0.03880  129 THR B C   
3675 O O   . THR B  135 ? 0.34010 0.22980 0.27900 0.05560  0.10020  0.03530  129 THR B O   
3676 C CB  . THR B  135 ? 0.47590 0.30560 0.35550 0.07720  0.17500  0.04700  129 THR B CB  
3677 O OG1 . THR B  135 ? 0.46360 0.28300 0.29710 0.09250  0.15280  0.04940  129 THR B OG1 
3678 C CG2 . THR B  135 ? 0.47150 0.28920 0.34230 0.08520  0.20190  0.04500  129 THR B CG2 
3679 N N   . ALA B  136 ? 0.38160 0.24900 0.31560 0.05080  0.13950  0.04480  130 ALA B N   
3680 C CA  . ALA B  136 ? 0.39480 0.27400 0.33660 0.04320  0.12000  0.04570  130 ALA B CA  
3681 C C   . ALA B  136 ? 0.32970 0.20700 0.24190 0.05230  0.09330  0.04670  130 ALA B C   
3682 O O   . ALA B  136 ? 0.31100 0.20730 0.24020 0.04460  0.07180  0.04320  130 ALA B O   
3683 C CB  . ALA B  136 ? 0.35690 0.21770 0.29210 0.04080  0.13990  0.05260  130 ALA B CB  
3684 N N   . VAL B  137 ? 0.38230 0.23750 0.25030 0.06950  0.09550  0.04970  131 VAL B N   
3685 C CA  . VAL B  137 ? 0.36470 0.22210 0.21000 0.07860  0.07020  0.04510  131 VAL B CA  
3686 C C   . VAL B  137 ? 0.36190 0.23680 0.22830 0.07340  0.05080  0.03470  131 VAL B C   
3687 O O   . VAL B  137 ? 0.38090 0.26350 0.24650 0.07360  0.03040  0.02770  131 VAL B O   
3688 C CB  . VAL B  137 ? 0.41180 0.24510 0.20310 0.10260  0.07540  0.04730  131 VAL B CB  
3689 C CG1 . VAL B  137 ? 0.46260 0.29160 0.24000 0.11270  0.07910  0.04040  131 VAL B CG1 
3690 C CG2 . VAL B  137 ? 0.41530 0.25380 0.18690 0.11290  0.05080  0.04100  131 VAL B CG2 
3691 N N   . CYS B  138 ? 0.33040 0.21150 0.22000 0.06830  0.05830  0.03280  132 CYS B N   
3692 C CA  . CYS B  138 ? 0.33280 0.22470 0.24240 0.06510  0.04350  0.02530  132 CYS B CA  
3693 C C   . CYS B  138 ? 0.30320 0.21330 0.24680 0.05140  0.03310  0.02800  132 CYS B C   
3694 O O   . CYS B  138 ? 0.32100 0.23480 0.27880 0.05000  0.02260  0.02500  132 CYS B O   
3695 C CB  . CYS B  138 ? 0.34540 0.23440 0.26190 0.07040  0.05640  0.02160  132 CYS B CB  
3696 S SG  . CYS B  138 ? 0.44710 0.31330 0.31730 0.08960  0.07220  0.01860  132 CYS B SG  
3697 N N   . SER B  139 ? 0.27460 0.19440 0.23020 0.04300  0.03720  0.03320  133 SER B N   
3698 C CA  . SER B  139 ? 0.25990 0.19940 0.24320 0.03340  0.02770  0.03470  133 SER B CA  
3699 C C   . SER B  139 ? 0.29200 0.23110 0.27190 0.03090  0.01110  0.03550  133 SER B C   
3700 O O   . SER B  139 ? 0.29880 0.23130 0.26280 0.03110  0.00600  0.03350  133 SER B O   
3701 C CB  . SER B  139 ? 0.25330 0.20350 0.24730 0.02540  0.03380  0.03610  133 SER B CB  
3702 O OG  . SER B  139 ? 0.27540 0.24420 0.28520 0.01870  0.02100  0.03680  133 SER B OG  
3703 N N   . ASN B  140 ? 0.24970 0.19550 0.24540 0.02960  0.00400  0.03820  134 ASN B N   
3704 C CA  . ASN B  140 ? 0.23970 0.18200 0.23490 0.02500  -0.00570 0.04090  134 ASN B CA  
3705 C C   . ASN B  140 ? 0.26930 0.22110 0.26190 0.01680  -0.00900 0.04280  134 ASN B C   
3706 O O   . ASN B  140 ? 0.24640 0.19470 0.23830 0.01180  -0.01390 0.04250  134 ASN B O   
3707 C CB  . ASN B  140 ? 0.26570 0.20930 0.27260 0.02770  -0.00910 0.04810  134 ASN B CB  
3708 C CG  . ASN B  140 ? 0.30060 0.26480 0.31440 0.02690  -0.01230 0.05380  134 ASN B CG  
3709 O OD1 . ASN B  140 ? 0.31070 0.27660 0.32030 0.02390  -0.01650 0.06080  134 ASN B OD1 
3710 N ND2 . ASN B  140 ? 0.25910 0.24000 0.28510 0.03020  -0.00950 0.04890  134 ASN B ND2 
3711 N N   . CYS B  141 ? 0.23910 0.20290 0.23450 0.01460  -0.00460 0.04300  135 CYS B N   
3712 C CA  . CYS B  141 ? 0.26800 0.24110 0.26270 0.00760  -0.00680 0.04320  135 CYS B CA  
3713 C C   . CYS B  141 ? 0.24930 0.21290 0.23000 0.00960  -0.00200 0.03980  135 CYS B C   
3714 O O   . CYS B  141 ? 0.25100 0.22080 0.23290 0.00530  -0.00070 0.03930  135 CYS B O   
3715 C CB  . CYS B  141 ? 0.26690 0.26070 0.27740 0.00440  -0.00540 0.04280  135 CYS B CB  
3716 S SG  . CYS B  141 ? 0.25930 0.26530 0.27830 0.00980  -0.01370 0.04780  135 CYS B SG  
3717 N N   . SER B  142 ? 0.26140 0.20930 0.22620 0.01850  0.00090  0.03730  136 SER B N   
3718 C CA  . SER B  142 ? 0.29030 0.22580 0.23400 0.02620  0.00750  0.03690  136 SER B CA  
3719 C C   . SER B  142 ? 0.27280 0.21160 0.20970 0.02630  -0.00280 0.03340  136 SER B C   
3720 O O   . SER B  142 ? 0.30340 0.23620 0.22910 0.03060  0.00230  0.03550  136 SER B O   
3721 C CB  . SER B  142 ? 0.32430 0.24330 0.24490 0.03990  0.01100  0.03420  136 SER B CB  
3722 O OG  . SER B  142 ? 0.32740 0.24840 0.24700 0.04230  -0.00350 0.02520  136 SER B OG  
3723 N N   . GLY B  143 ? 0.26040 0.20770 0.20670 0.02170  -0.01530 0.02730  137 GLY B N   
3724 C CA  . GLY B  143 ? 0.26790 0.22280 0.21470 0.02100  -0.02440 0.02040  137 GLY B CA  
3725 C C   . GLY B  143 ? 0.26250 0.22810 0.22040 0.01160  -0.02140 0.02500  137 GLY B C   
3726 O O   . GLY B  143 ? 0.30680 0.27390 0.25910 0.01550  -0.02340 0.02210  137 GLY B O   
3727 N N   . LYS B  144 ? 0.25520 0.22960 0.22810 0.00150  -0.01770 0.03090  138 LYS B N   
3728 C CA  . LYS B  144 ? 0.23510 0.22270 0.21800 -0.00620 -0.01510 0.03250  138 LYS B CA  
3729 C C   . LYS B  144 ? 0.27940 0.26030 0.25840 -0.00250 -0.00540 0.03300  138 LYS B C   
3730 O O   . LYS B  144 ? 0.24460 0.22880 0.22590 -0.00420 -0.00410 0.03040  138 LYS B O   
3731 C CB  . LYS B  144 ? 0.23140 0.23080 0.22590 -0.01190 -0.01480 0.03720  138 LYS B CB  
3732 C CG  . LYS B  144 ? 0.25860 0.27560 0.26310 -0.01730 -0.01320 0.03510  138 LYS B CG  
3733 C CD  . LYS B  144 ? 0.23490 0.26620 0.24460 -0.01750 -0.01680 0.03840  138 LYS B CD  
3734 C CE  . LYS B  144 ? 0.22290 0.25190 0.23770 -0.01120 -0.01530 0.03990  138 LYS B CE  
3735 N NZ  . LYS B  144 ? 0.22020 0.26920 0.23990 -0.00760 -0.02150 0.04050  138 LYS B NZ  
3736 N N   . HIS B  145 ? 0.24920 0.21830 0.22390 0.00250  0.00450  0.03610  139 HIS B N   
3737 C CA  . HIS B  145 ? 0.26540 0.22260 0.23900 0.00460  0.02030  0.03740  139 HIS B CA  
3738 C C   . HIS B  145 ? 0.27380 0.21060 0.22180 0.01690  0.02220  0.04010  139 HIS B C   
3739 O O   . HIS B  145 ? 0.27770 0.20540 0.22630 0.01750  0.03260  0.04130  139 HIS B O   
3740 C CB  . HIS B  145 ? 0.26180 0.21060 0.23890 0.00650  0.03410  0.03950  139 HIS B CB  
3741 C CG  . HIS B  145 ? 0.25540 0.22780 0.26390 -0.00360 0.03440  0.03360  139 HIS B CG  
3742 N ND1 . HIS B  145 ? 0.21690 0.19590 0.25050 -0.01070 0.04890  0.02670  139 HIS B ND1 
3743 C CD2 . HIS B  145 ? 0.22190 0.21410 0.24140 -0.00600 0.02120  0.03200  139 HIS B CD2 
3744 C CE1 . HIS B  145 ? 0.22280 0.23010 0.28260 -0.01590 0.04150  0.01830  139 HIS B CE1 
3745 N NE2 . HIS B  145 ? 0.22590 0.23960 0.27370 -0.01140 0.02470  0.02350  139 HIS B NE2 
3746 N N   . VAL B  146 ? 0.25090 0.18070 0.17670 0.02890  0.01190  0.03930  140 VAL B N   
3747 C CA  . VAL B  146 ? 0.29830 0.21310 0.19720 0.04570  0.00960  0.03990  140 VAL B CA  
3748 C C   . VAL B  146 ? 0.27940 0.20890 0.19190 0.04080  0.00010  0.03400  140 VAL B C   
3749 O O   . VAL B  146 ? 0.30530 0.22220 0.20610 0.05060  0.00500  0.03650  140 VAL B O   
3750 C CB  . VAL B  146 ? 0.28930 0.20060 0.16420 0.06170  -0.00320 0.03430  140 VAL B CB  
3751 C CG1 . VAL B  146 ? 0.31690 0.21980 0.16400 0.08320  -0.01120 0.03160  140 VAL B CG1 
3752 C CG2 . VAL B  146 ? 0.30750 0.19980 0.16250 0.06990  0.01000  0.04080  140 VAL B CG2 
3753 N N   . GLY B  147 ? 0.23620 0.19020 0.17270 0.02660  -0.01110 0.02690  141 GLY B N   
3754 C CA  . GLY B  147 ? 0.26430 0.23410 0.21540 0.02070  -0.01750 0.02040  141 GLY B CA  
3755 C C   . GLY B  147 ? 0.25640 0.22420 0.21750 0.01430  -0.00530 0.02340  141 GLY B C   
3756 O O   . GLY B  147 ? 0.24200 0.20980 0.20430 0.01810  -0.00580 0.01990  141 GLY B O   
3757 N N   . MET B  148 ? 0.26050 0.22920 0.23340 0.00470  0.00540  0.02680  142 MET B N   
3758 C CA  A MET B  148 ? 0.24760 0.21810 0.23810 -0.00320 0.01770  0.02410  142 MET B CA  
3759 C CA  B MET B  148 ? 0.24760 0.21820 0.23770 -0.00300 0.01720  0.02400  142 MET B CA  
3760 C C   . MET B  148 ? 0.28030 0.22000 0.25740 0.00770  0.03410  0.02970  142 MET B C   
3761 O O   . MET B  148 ? 0.30820 0.24350 0.29560 0.00570  0.04210  0.02610  142 MET B O   
3762 C CB  A MET B  148 ? 0.23730 0.22070 0.24760 -0.01380 0.02330  0.02190  142 MET B CB  
3763 C CB  B MET B  148 ? 0.23670 0.22310 0.24840 -0.01480 0.02170  0.02080  142 MET B CB  
3764 C CG  A MET B  148 ? 0.25630 0.26520 0.27400 -0.02060 0.00910  0.01970  142 MET B CG  
3765 C CG  B MET B  148 ? 0.25700 0.27310 0.28110 -0.02390 0.00880  0.01510  142 MET B CG  
3766 S SD  A MET B  148 ? 0.28790 0.32390 0.32100 -0.03000 0.00310  0.01000  142 MET B SD  
3767 S SD  B MET B  148 ? 0.22190 0.25680 0.26020 -0.02830 0.00690  0.01350  142 MET B SD  
3768 C CE  A MET B  148 ? 0.20600 0.25630 0.23070 -0.03150 -0.00950 0.01540  142 MET B CE  
3769 C CE  B MET B  148 ? 0.16670 0.22610 0.20190 -0.03170 -0.00730 0.01320  142 MET B CE  
3770 N N   . LEU B  149 ? 0.27480 0.19030 0.22710 0.02040  0.04140  0.03890  143 LEU B N   
3771 C CA  . LEU B  149 ? 0.30670 0.18560 0.23410 0.03630  0.05870  0.04850  143 LEU B CA  
3772 C C   . LEU B  149 ? 0.33670 0.21040 0.24580 0.05190  0.04710  0.04810  143 LEU B C   
3773 O O   . LEU B  149 ? 0.31830 0.16780 0.22010 0.06060  0.06090  0.05310  143 LEU B O   
3774 C CB  . LEU B  149 ? 0.34180 0.19890 0.23710 0.05090  0.06490  0.05820  143 LEU B CB  
3775 C CG  . LEU B  149 ? 0.37710 0.22350 0.28550 0.04160  0.08890  0.06180  143 LEU B CG  
3776 C CD1 . LEU B  149 ? 0.43260 0.26250 0.30800 0.05620  0.09210  0.06940  143 LEU B CD1 
3777 C CD2 . LEU B  149 ? 0.39730 0.21290 0.31080 0.04110  0.11940  0.06760  143 LEU B CD2 
3778 N N   . ALA B  150 ? 0.31090 0.20530 0.21350 0.05730  0.02320  0.04120  144 ALA B N   
3779 C CA  . ALA B  150 ? 0.32620 0.22450 0.21810 0.07270  0.00840  0.03570  144 ALA B CA  
3780 C C   . ALA B  150 ? 0.30940 0.21950 0.22870 0.06130  0.01070  0.02910  144 ALA B C   
3781 O O   . ALA B  150 ? 0.29630 0.18990 0.20550 0.07560  0.01470  0.03120  144 ALA B O   
3782 C CB  . ALA B  150 ? 0.28930 0.21530 0.18480 0.07400  -0.01570 0.02320  144 ALA B CB  
3783 N N   . GLY B  151 ? 0.25860 0.19600 0.21000 0.03770  0.00860  0.02140  145 GLY B N   
3784 C CA  . GLY B  151 ? 0.29930 0.24990 0.27530 0.02700  0.01140  0.01300  145 GLY B CA  
3785 C C   . GLY B  151 ? 0.32580 0.25030 0.30600 0.02760  0.03320  0.01710  145 GLY B C   
3786 O O   . GLY B  151 ? 0.30040 0.21720 0.28490 0.03350  0.03680  0.01360  145 GLY B O   
3787 N N   . ALA B  152 ? 0.28480 0.19480 0.26800 0.02100  0.05000  0.02300  146 ALA B N   
3788 C CA  . ALA B  152 ? 0.31460 0.19560 0.30730 0.01990  0.07630  0.02550  146 ALA B CA  
3789 C C   . ALA B  152 ? 0.36000 0.19960 0.32010 0.04470  0.08600  0.03830  146 ALA B C   
3790 O O   . ALA B  152 ? 0.34380 0.16480 0.31410 0.04650  0.10020  0.03670  146 ALA B O   
3791 C CB  . ALA B  152 ? 0.29590 0.16630 0.29710 0.01110  0.09530  0.02920  146 ALA B CB  
3792 N N   . ARG B  153 ? 0.35160 0.17610 0.27100 0.06640  0.07800  0.05010  147 ARG B N   
3793 C CA  . ARG B  153 ? 0.40850 0.19290 0.28800 0.09640  0.08540  0.06370  147 ARG B CA  
3794 C C   . ARG B  153 ? 0.39960 0.19650 0.28370 0.10690  0.06860  0.05480  147 ARG B C   
3795 O O   . ARG B  153 ? 0.44710 0.21150 0.31990 0.12280  0.08220  0.06190  147 ARG B O   
3796 C CB  . ARG B  153 ? 0.45320 0.22800 0.28660 0.11990  0.07460  0.07330  147 ARG B CB  
3797 C CG  . ARG B  153 ? 0.52160 0.27730 0.34180 0.11620  0.09770  0.08300  147 ARG B CG  
3798 C CD  . ARG B  153 ? 0.58800 0.31490 0.37190 0.13690  0.11510  0.09250  147 ARG B CD  
3799 N NE  . ARG B  153 ? 0.75710 0.46640 0.53650 0.13180  0.14300  0.09870  147 ARG B NE  
3800 C CZ  . ARG B  153 ? 0.71710 0.42150 0.46400 0.14620  0.14310  0.10180  147 ARG B CZ  
3801 N NH1 . ARG B  153 ? 0.70730 0.42590 0.42520 0.16460  0.11570  0.09720  147 ARG B NH1 
3802 N NH2 . ARG B  153 ? 0.69030 0.37570 0.43680 0.14280  0.17200  0.10670  147 ARG B NH2 
3803 N N   . ALA B  154 ? 0.38300 0.22520 0.28540 0.09810  0.04140  0.03930  148 ALA B N   
3804 C CA  . ALA B  154 ? 0.35120 0.21190 0.25930 0.10940  0.02280  0.02790  148 ALA B CA  
3805 C C   . ALA B  154 ? 0.36270 0.22040 0.29940 0.09920  0.03540  0.02160  148 ALA B C   
3806 O O   . ALA B  154 ? 0.38660 0.23890 0.31960 0.11700  0.03010  0.01820  148 ALA B O   
3807 C CB  . ALA B  154 ? 0.35860 0.26830 0.28870 0.09560  -0.00180 0.01140  148 ALA B CB  
3808 N N   . ILE B  155 ? 0.35840 0.22200 0.32550 0.07220  0.05090  0.01720  149 ILE B N   
3809 C CA  . ILE B  155 ? 0.35160 0.21770 0.35060 0.06010  0.06210  0.00590  149 ILE B CA  
3810 C C   . ILE B  155 ? 0.40230 0.22000 0.40070 0.06400  0.09360  0.01550  149 ILE B C   
3811 O O   . ILE B  155 ? 0.36510 0.17810 0.39160 0.05600  0.10610  0.00490  149 ILE B O   
3812 C CB  . ILE B  155 ? 0.31800 0.22680 0.35410 0.03010  0.05730  -0.01090 149 ILE B CB  
3813 C CG1 . ILE B  155 ? 0.32350 0.23210 0.36610 0.01500  0.06760  -0.00730 149 ILE B CG1 
3814 C CG2 . ILE B  155 ? 0.31320 0.26430 0.35210 0.02660  0.03180  -0.02020 149 ILE B CG2 
3815 C CD1 . ILE B  155 ? 0.31460 0.26530 0.39030 -0.00900 0.06170  -0.02500 149 ILE B CD1 
3816 N N   . GLY B  156 ? 0.45340 0.32790 0.43940 0.12190  0.01440  0.19040  150 GLY B N   
3817 C CA  . GLY B  156 ? 0.50080 0.32970 0.46740 0.12370  0.03910  0.19840  150 GLY B CA  
3818 C C   . GLY B  156 ? 0.49010 0.28660 0.46110 0.10640  0.06540  0.18000  150 GLY B C   
3819 O O   . GLY B  156 ? 0.52650 0.28550 0.49580 0.10340  0.08880  0.18120  150 GLY B O   
3820 N N   . ALA B  157 ? 0.52270 0.33410 0.50140 0.09320  0.06090  0.16340  151 ALA B N   
3821 C CA  . ALA B  157 ? 0.58850 0.38230 0.58470 0.07280  0.07990  0.14080  151 ALA B CA  
3822 C C   . ALA B  157 ? 0.63430 0.41040 0.61170 0.05870  0.09820  0.14420  151 ALA B C   
3823 O O   . ALA B  157 ? 0.66260 0.42260 0.66190 0.04010  0.11730  0.13200  151 ALA B O   
3824 C CB  . ALA B  157 ? 0.37940 0.21310 0.39410 0.06100  0.06260  0.11360  151 ALA B CB  
3825 N N   . GLY B  158 ? 0.53960 0.31860 0.47660 0.06590  0.09320  0.16090  152 GLY B N   
3826 C CA  . GLY B  158 ? 0.65330 0.41660 0.57260 0.05460  0.11690  0.16390  152 GLY B CA  
3827 C C   . GLY B  158 ? 0.52250 0.31930 0.44090 0.04470  0.10750  0.14220  152 GLY B C   
3828 O O   . GLY B  158 ? 0.45100 0.27580 0.40170 0.03740  0.09300  0.11970  152 GLY B O   
3829 N N   . THR B  159 ? 0.52400 0.31240 0.39890 0.04720  0.11780  0.15020  153 THR B N   
3830 C CA  . THR B  159 ? 0.56280 0.37170 0.42090 0.04450  0.10940  0.13260  153 THR B CA  
3831 C C   . THR B  159 ? 0.52990 0.35040 0.41770 0.03390  0.13730  0.12240  153 THR B C   
3832 O O   . THR B  159 ? 0.48450 0.32550 0.37390 0.03320  0.13100  0.10530  153 THR B O   
3833 C CB  . THR B  159 ? 0.59620 0.38270 0.37520 0.05620  0.10220  0.14500  153 THR B CB  
3834 O OG1 . THR B  159 ? 0.63590 0.39060 0.38550 0.06190  0.13050  0.16730  153 THR B OG1 
3835 C CG2 . THR B  159 ? 0.60850 0.40130 0.36710 0.06370  0.06400  0.15260  153 THR B CG2 
3836 N N   . ASP B  160 ? 0.48530 0.29530 0.40110 0.02550  0.16820  0.13420  154 ASP B N   
3837 C CA  . ASP B  160 ? 0.54400 0.37070 0.48400 0.01870  0.19790  0.13280  154 ASP B CA  
3838 C C   . ASP B  160 ? 0.52230 0.39470 0.52170 0.00790  0.18590  0.10900  154 ASP B C   
3839 O O   . ASP B  160 ? 0.52280 0.41730 0.53090 0.01200  0.20000  0.10500  154 ASP B O   
3840 C CB  . ASP B  160 ? 0.63530 0.45050 0.60450 0.00770  0.22880  0.14890  154 ASP B CB  
3841 C CG  . ASP B  160 ? 0.74560 0.59230 0.75310 0.00210  0.25490  0.14740  154 ASP B CG  
3842 O OD1 . ASP B  160 ? 0.75830 0.60410 0.72690 0.01870  0.26720  0.14920  154 ASP B OD1 
3843 O OD2 . ASP B  160 ? 0.85520 0.72710 0.93090 -0.01820 0.26070  0.14400  154 ASP B OD2 
3844 N N   . GLY B  161 ? 0.42910 0.31390 0.46580 -0.00270 0.16200  0.09450  155 GLY B N   
3845 C CA  . GLY B  161 ? 0.33460 0.26010 0.41760 -0.01130 0.14750  0.07340  155 GLY B CA  
3846 C C   . GLY B  161 ? 0.30620 0.23740 0.37350 -0.00420 0.11450  0.05700  155 GLY B C   
3847 O O   . GLY B  161 ? 0.26990 0.21970 0.37170 -0.01360 0.09840  0.04130  155 GLY B O   
3848 N N   . TYR B  162 ? 0.31940 0.23440 0.33310 0.01060  0.10350  0.06090  156 TYR B N   
3849 C CA  . TYR B  162 ? 0.28480 0.20780 0.29010 0.01460  0.07380  0.04910  156 TYR B CA  
3850 C C   . TYR B  162 ? 0.27110 0.22280 0.30040 0.01210  0.06440  0.03080  156 TYR B C   
3851 O O   . TYR B  162 ? 0.24340 0.20450 0.27830 0.01210  0.04380  0.02060  156 TYR B O   
3852 C CB  . TYR B  162 ? 0.34840 0.25430 0.29630 0.02510  0.06040  0.05620  156 TYR B CB  
3853 C CG  . TYR B  162 ? 0.34010 0.23840 0.24930 0.03020  0.06680  0.05070  156 TYR B CG  
3854 C CD1 . TYR B  162 ? 0.33500 0.24430 0.24310 0.03030  0.05280  0.03430  156 TYR B CD1 
3855 C CD2 . TYR B  162 ? 0.39480 0.26750 0.26250 0.03700  0.09000  0.06250  156 TYR B CD2 
3856 C CE1 . TYR B  162 ? 0.34350 0.23420 0.21010 0.03760  0.06250  0.02880  156 TYR B CE1 
3857 C CE2 . TYR B  162 ? 0.42010 0.27530 0.24250 0.04530  0.10130  0.05630  156 TYR B CE2 
3858 C CZ  . TYR B  162 ? 0.39870 0.26130 0.22150 0.04560  0.08680  0.03870  156 TYR B CZ  
3859 O OH  . TYR B  162 ? 0.44320 0.27790 0.21630 0.05600  0.10100  0.03240  156 TYR B OH  
3860 N N   . HIS B  163 ? 0.27590 0.24150 0.31820 0.01290  0.08110  0.02970  157 HIS B N   
3861 C CA  . HIS B  163 ? 0.26900 0.26110 0.33100 0.01590  0.07430  0.01710  157 HIS B CA  
3862 C C   . HIS B  163 ? 0.24710 0.27280 0.36880 0.00330  0.06910  0.00960  157 HIS B C   
3863 O O   . HIS B  163 ? 0.24410 0.29600 0.38530 0.00680  0.06010  0.00130  157 HIS B O   
3864 C CB  . HIS B  163 ? 0.28090 0.27200 0.32750 0.02850  0.09790  0.02270  157 HIS B CB  
3865 C CG  . HIS B  163 ? 0.30210 0.30780 0.38370 0.02480  0.12730  0.03610  157 HIS B CG  
3866 N ND1 . HIS B  163 ? 0.29140 0.27670 0.36600 0.01700  0.14100  0.04940  157 HIS B ND1 
3867 C CD2 . HIS B  163 ? 0.29400 0.33550 0.42290 0.02770  0.14740  0.04160  157 HIS B CD2 
3868 C CE1 . HIS B  163 ? 0.30400 0.30920 0.41930 0.01220  0.16940  0.06150  157 HIS B CE1 
3869 N NE2 . HIS B  163 ? 0.28440 0.32860 0.43770 0.01830  0.17330  0.05750  157 HIS B NE2 
3870 N N   . LEU B  164 ? 0.20040 0.22140 0.34740 -0.01210 0.07300  0.01250  158 LEU B N   
3871 C CA  . LEU B  164 ? 0.25510 0.30340 0.45410 -0.02980 0.06580  0.00390  158 LEU B CA  
3872 C C   . LEU B  164 ? 0.25960 0.30040 0.45110 -0.03400 0.04050  -0.01270 158 LEU B C   
3873 O O   . LEU B  164 ? 0.28260 0.29300 0.44250 -0.02780 0.03650  -0.01280 158 LEU B O   
3874 C CB  . LEU B  164 ? 0.28020 0.31770 0.50600 -0.04870 0.08330  0.01320  158 LEU B CB  
3875 C CG  . LEU B  164 ? 0.30440 0.34960 0.53910 -0.04440 0.11500  0.03290  158 LEU B CG  
3876 C CD1 . LEU B  164 ? 0.32100 0.35220 0.58420 -0.06590 0.13540  0.04510  158 LEU B CD1 
3877 C CD2 . LEU B  164 ? 0.22710 0.32400 0.50060 -0.03750 0.12100  0.03490  158 LEU B CD2 
3878 N N   . PRO B  165 ? 0.26590 0.33460 0.48520 -0.04310 0.02370  -0.02510 159 PRO B N   
3879 C CA  . PRO B  165 ? 0.27060 0.32570 0.47030 -0.04410 0.00290  -0.04090 159 PRO B CA  
3880 C C   . PRO B  165 ? 0.28210 0.29390 0.46610 -0.05330 0.00590  -0.04590 159 PRO B C   
3881 O O   . PRO B  165 ? 0.38140 0.37120 0.53610 -0.04330 -0.00010 -0.05210 159 PRO B O   
3882 C CB  . PRO B  165 ? 0.36400 0.45630 0.59540 -0.05570 -0.01590 -0.05090 159 PRO B CB  
3883 C CG  . PRO B  165 ? 0.28740 0.42210 0.55470 -0.04940 -0.00540 -0.03740 159 PRO B CG  
3884 C CD  . PRO B  165 ? 0.25700 0.37400 0.52540 -0.05020 0.02240  -0.02290 159 PRO B CD  
3885 N N   . ASP B  166 ? 0.33510 0.33070 0.53790 -0.07050 0.01870  -0.04150 160 ASP B N   
3886 C CA  . ASP B  166 ? 0.33880 0.28240 0.52150 -0.07630 0.02450  -0.04600 160 ASP B CA  
3887 C C   . ASP B  166 ? 0.33800 0.25250 0.49240 -0.05520 0.04010  -0.02880 160 ASP B C   
3888 O O   . ASP B  166 ? 0.37090 0.24170 0.50780 -0.05200 0.04770  -0.02850 160 ASP B O   
3889 C CB  . ASP B  166 ? 0.38950 0.31770 0.60040 -0.10570 0.03200  -0.04780 160 ASP B CB  
3890 C CG  . ASP B  166 ? 0.55780 0.49030 0.78880 -0.10760 0.05690  -0.02480 160 ASP B CG  
3891 O OD1 . ASP B  166 ? 0.52270 0.49870 0.77170 -0.09950 0.06150  -0.01420 160 ASP B OD1 
3892 O OD2 . ASP B  166 ? 0.65330 0.54070 0.87820 -0.11580 0.07480  -0.01630 160 ASP B OD2 
3893 N N   . HIS B  167 ? 0.28510 0.21990 0.43200 -0.04020 0.04430  -0.01420 161 HIS B N   
3894 C CA  . HIS B  167 ? 0.30450 0.21810 0.42310 -0.02180 0.05140  0.00310  161 HIS B CA  
3895 C C   . HIS B  167 ? 0.25250 0.16530 0.35490 -0.00630 0.03840  -0.00100 161 HIS B C   
3896 O O   . HIS B  167 ? 0.26750 0.20370 0.37120 -0.00530 0.02470  -0.01320 161 HIS B O   
3897 C CB  . HIS B  167 ? 0.28040 0.21180 0.38560 -0.01340 0.05570  0.01630  161 HIS B CB  
3898 C CG  . HIS B  167 ? 0.28190 0.19100 0.35510 0.00070  0.06100  0.03660  161 HIS B CG  
3899 N ND1 . HIS B  167 ? 0.27480 0.18660 0.32860 0.01500  0.04540  0.04170  161 HIS B ND1 
3900 C CD2 . HIS B  167 ? 0.30320 0.19010 0.36080 0.00270  0.07880  0.05560  161 HIS B CD2 
3901 C CE1 . HIS B  167 ? 0.33290 0.22790 0.36080 0.02510  0.04890  0.06250  161 HIS B CE1 
3902 N NE2 . HIS B  167 ? 0.35230 0.22850 0.37670 0.01910  0.07000  0.07110  161 HIS B NE2 
3903 N N   . PRO B  168 ? 0.28410 0.17250 0.37380 0.00780  0.04410  0.01210  162 PRO B N   
3904 C CA  . PRO B  168 ? 0.24540 0.14250 0.33030 0.02370  0.03500  0.01200  162 PRO B CA  
3905 C C   . PRO B  168 ? 0.22660 0.16100 0.30800 0.02790  0.01860  0.01420  162 PRO B C   
3906 O O   . PRO B  168 ? 0.22120 0.16940 0.30610 0.03370  0.01150  0.00910  162 PRO B O   
3907 C CB  . PRO B  168 ? 0.27980 0.15380 0.35940 0.04160  0.04510  0.03390  162 PRO B CB  
3908 C CG  . PRO B  168 ? 0.29530 0.15200 0.36630 0.03640  0.05520  0.04840  162 PRO B CG  
3909 C CD  . PRO B  168 ? 0.29230 0.14660 0.37440 0.01270  0.06060  0.03090  162 PRO B CD  
3910 N N   . MET B  169 ? 0.20210 0.14680 0.27150 0.02600  0.01450  0.02330  163 MET B N   
3911 C CA  A MET B  169 ? 0.23700 0.20540 0.29600 0.02640  -0.00140 0.02200  163 MET B CA  
3912 C CA  B MET B  169 ? 0.23690 0.20530 0.29610 0.02650  -0.00140 0.02190  163 MET B CA  
3913 C C   . MET B  169 ? 0.24420 0.22620 0.31120 0.01960  -0.00520 0.00320  163 MET B C   
3914 O O   . MET B  169 ? 0.22510 0.22090 0.29000 0.02120  -0.01600 -0.00010 163 MET B O   
3915 C CB  A MET B  169 ? 0.23150 0.19500 0.26220 0.02520  -0.00290 0.03110  163 MET B CB  
3916 C CB  B MET B  169 ? 0.23170 0.19560 0.26260 0.02550  -0.00340 0.03150  163 MET B CB  
3917 C CG  A MET B  169 ? 0.27210 0.22930 0.28550 0.03360  -0.00980 0.05250  163 MET B CG  
3918 C CG  B MET B  169 ? 0.27780 0.24390 0.29260 0.03280  -0.01740 0.05020  163 MET B CG  
3919 S SD  A MET B  169 ? 0.24220 0.22730 0.27600 0.04070  -0.03020 0.06220  163 MET B SD  
3920 S SD  B MET B  169 ? 0.26200 0.24990 0.26550 0.02650  -0.04400 0.04780  163 MET B SD  
3921 C CE  A MET B  169 ? 0.24940 0.25050 0.27030 0.02750  -0.04880 0.04880  163 MET B CE  
3922 C CE  B MET B  169 ? 0.21460 0.22430 0.25720 0.02660  -0.04360 0.03680  163 MET B CE  
3923 N N   . GLN B  170 ? 0.22920 0.20940 0.30790 0.01130  0.00270  -0.00700 164 GLN B N   
3924 C CA  . GLN B  170 ? 0.19940 0.19690 0.28700 0.00730  -0.00430 -0.02160 164 GLN B CA  
3925 C C   . GLN B  170 ? 0.23150 0.22480 0.32240 0.00740  -0.00920 -0.03250 164 GLN B C   
3926 O O   . GLN B  170 ? 0.23080 0.23620 0.31720 0.00980  -0.01790 -0.03990 164 GLN B O   
3927 C CB  . GLN B  170 ? 0.20930 0.21770 0.31640 -0.00190 0.00270  -0.02540 164 GLN B CB  
3928 C CG  . GLN B  170 ? 0.23170 0.24150 0.32870 0.00250  0.01390  -0.01470 164 GLN B CG  
3929 C CD  . GLN B  170 ? 0.22300 0.23010 0.28960 0.01230  0.00650  -0.01370 164 GLN B CD  
3930 O OE1 . GLN B  170 ? 0.20770 0.22440 0.27440 0.01500  -0.00380 -0.02140 164 GLN B OE1 
3931 N NE2 . GLN B  170 ? 0.25270 0.24150 0.28790 0.01610  0.01060  -0.00400 164 GLN B NE2 
3932 N N   . GLY B  171 ? 0.22180 0.19130 0.31400 0.00630  -0.00130 -0.03360 165 GLY B N   
3933 C CA  . GLY B  171 ? 0.22270 0.17850 0.30480 0.01180  -0.00140 -0.04290 165 GLY B CA  
3934 C C   . GLY B  171 ? 0.23780 0.20760 0.31550 0.02610  -0.00310 -0.03300 165 GLY B C   
3935 O O   . GLY B  171 ? 0.22500 0.19750 0.29330 0.03040  -0.00490 -0.04000 165 GLY B O   
3936 N N   . ARG B  172 ? 0.19870 0.17800 0.28280 0.03220  -0.00320 -0.01520 166 ARG B N   
3937 C CA  . ARG B  172 ? 0.22260 0.22240 0.31240 0.04050  -0.00780 -0.00350 166 ARG B CA  
3938 C C   . ARG B  172 ? 0.19080 0.20700 0.27370 0.03330  -0.01900 -0.00970 166 ARG B C   
3939 O O   . ARG B  172 ? 0.18550 0.21110 0.27020 0.03680  -0.01860 -0.00870 166 ARG B O   
3940 C CB  . ARG B  172 ? 0.21870 0.22870 0.31650 0.04480  -0.01250 0.01730  166 ARG B CB  
3941 C CG  . ARG B  172 ? 0.21910 0.21600 0.32790 0.05990  0.00050  0.03050  166 ARG B CG  
3942 C CD  . ARG B  172 ? 0.20880 0.21290 0.31940 0.06420  -0.00700 0.05220  166 ARG B CD  
3943 N NE  . ARG B  172 ? 0.21080 0.20610 0.33630 0.08440  0.00580  0.07020  166 ARG B NE  
3944 C CZ  . ARG B  172 ? 0.21840 0.24440 0.36790 0.09730  0.00180  0.08990  166 ARG B CZ  
3945 N NH1 . ARG B  172 ? 0.19790 0.26410 0.35940 0.08700  -0.01670 0.09370  166 ARG B NH1 
3946 N NH2 . ARG B  172 ? 0.23520 0.24900 0.38860 0.11300  0.01690  0.10000  166 ARG B NH2 
3947 N N   . VAL B  173 ? 0.16820 0.18440 0.24220 0.02520  -0.02490 -0.01460 167 VAL B N   
3948 C CA  . VAL B  173 ? 0.19830 0.22100 0.26190 0.02190  -0.03220 -0.01990 167 VAL B CA  
3949 C C   . VAL B  173 ? 0.21060 0.23440 0.27200 0.02480  -0.03140 -0.03080 167 VAL B C   
3950 O O   . VAL B  173 ? 0.20950 0.23660 0.26380 0.02700  -0.03360 -0.02910 167 VAL B O   
3951 C CB  . VAL B  173 ? 0.20890 0.22720 0.26290 0.01850  -0.03180 -0.02290 167 VAL B CB  
3952 C CG1 . VAL B  173 ? 0.19200 0.21140 0.23590 0.02040  -0.03490 -0.02870 167 VAL B CG1 
3953 C CG2 . VAL B  173 ? 0.22400 0.23390 0.26260 0.01610  -0.03450 -0.01280 167 VAL B CG2 
3954 N N   . LYS B  174 ? 0.20570 0.22420 0.26990 0.02290  -0.02930 -0.04140 168 LYS B N   
3955 C CA  . LYS B  174 ? 0.21210 0.23030 0.26560 0.02400  -0.03410 -0.05270 168 LYS B CA  
3956 C C   . LYS B  174 ? 0.24390 0.25170 0.28290 0.03240  -0.02710 -0.05130 168 LYS B C   
3957 O O   . LYS B  174 ? 0.21010 0.21960 0.23320 0.03720  -0.02910 -0.05170 168 LYS B O   
3958 C CB  . LYS B  174 ? 0.25890 0.27240 0.31800 0.01460  -0.03790 -0.06530 168 LYS B CB  
3959 C CG  . LYS B  174 ? 0.25890 0.29390 0.34040 0.00750  -0.04290 -0.06450 168 LYS B CG  
3960 C CD  . LYS B  174 ? 0.33070 0.36960 0.42680 -0.00750 -0.05080 -0.07600 168 LYS B CD  
3961 C CE  . LYS B  174 ? 0.34620 0.41710 0.47890 -0.01430 -0.05200 -0.07060 168 LYS B CE  
3962 N NZ  . LYS B  174 ? 0.28670 0.35470 0.42820 -0.01060 -0.03390 -0.05730 168 LYS B NZ  
3963 N N   . ARG B  175 ? 0.18400 0.18030 0.22830 0.03700  -0.01550 -0.04660 169 ARG B N   
3964 C CA  A ARG B  175 ? 0.21620 0.20530 0.25170 0.04910  -0.00230 -0.04180 169 ARG B CA  
3965 C CA  B ARG B  175 ? 0.21620 0.20530 0.25180 0.04920  -0.00220 -0.04170 169 ARG B CA  
3966 C C   . ARG B  175 ? 0.22990 0.24210 0.27740 0.05090  -0.00250 -0.02630 169 ARG B C   
3967 O O   . ARG B  175 ? 0.21670 0.22750 0.25140 0.05730  0.00550  -0.02400 169 ARG B O   
3968 C CB  A ARG B  175 ? 0.24700 0.22150 0.29260 0.05830  0.01310  -0.03540 169 ARG B CB  
3969 C CB  B ARG B  175 ? 0.24680 0.22180 0.29280 0.05850  0.01320  -0.03500 169 ARG B CB  
3970 C CG  A ARG B  175 ? 0.30260 0.26250 0.33610 0.07550  0.03400  -0.03240 169 ARG B CG  
3971 C CG  B ARG B  175 ? 0.26800 0.25000 0.32230 0.07520  0.03120  -0.02040 169 ARG B CG  
3972 C CD  A ARG B  175 ? 0.31720 0.24650 0.34970 0.08770  0.05200  -0.03150 169 ARG B CD  
3973 C CD  B ARG B  175 ? 0.29050 0.25380 0.35310 0.09110  0.05050  -0.01290 169 ARG B CD  
3974 N NE  A ARG B  175 ? 0.29470 0.24210 0.36230 0.08950  0.04960  -0.01300 169 ARG B NE  
3975 N NE  B ARG B  175 ? 0.27050 0.25260 0.36500 0.09030  0.04350  0.00400  169 ARG B NE  
3976 C CZ  A ARG B  175 ? 0.28160 0.21020 0.34880 0.08180  0.04540  -0.01670 169 ARG B CZ  
3977 C CZ  B ARG B  175 ? 0.26910 0.29230 0.39840 0.09250  0.03740  0.02680  169 ARG B CZ  
3978 N NH1 A ARG B  175 ? 0.31360 0.21170 0.35700 0.06710  0.04070  -0.03840 169 ARG B NH1 
3979 N NH1 B ARG B  175 ? 0.22970 0.28140 0.37340 0.09190  0.03800  0.03540  169 ARG B NH1 
3980 N NH2 A ARG B  175 ? 0.26140 0.20310 0.35320 0.08800  0.04540  0.00380  169 ARG B NH2 
3981 N NH2 B ARG B  175 ? 0.26190 0.29710 0.41120 0.09400  0.02950  0.04250  169 ARG B NH2 
3982 N N   . THR B  176 ? 0.17740 0.20660 0.24480 0.04330  -0.01160 -0.01570 170 THR B N   
3983 C CA  . THR B  176 ? 0.20060 0.24830 0.28110 0.03890  -0.01450 -0.00130 170 THR B CA  
3984 C C   . THR B  176 ? 0.18690 0.22750 0.24690 0.03460  -0.01890 -0.00650 170 THR B C   
3985 O O   . THR B  176 ? 0.19830 0.24410 0.26120 0.03400  -0.01280 0.00320  170 THR B O   
3986 C CB  . THR B  176 ? 0.21500 0.27440 0.30960 0.02880  -0.02790 0.00800  170 THR B CB  
3987 O OG1 . THR B  176 ? 0.21980 0.28530 0.33180 0.03620  -0.02390 0.01670  170 THR B OG1 
3988 C CG2 . THR B  176 ? 0.18160 0.25910 0.29150 0.01780  -0.03540 0.02200  170 THR B CG2 
3989 N N   . VAL B  177 ? 0.22010 0.25030 0.26300 0.03290  -0.02740 -0.01860 171 VAL B N   
3990 C CA  . VAL B  177 ? 0.18840 0.21020 0.21130 0.03440  -0.03050 -0.02100 171 VAL B CA  
3991 C C   . VAL B  177 ? 0.19780 0.21380 0.20270 0.04390  -0.02240 -0.02190 171 VAL B C   
3992 O O   . VAL B  177 ? 0.23580 0.24600 0.22960 0.04570  -0.01690 -0.01310 171 VAL B O   
3993 C CB  . VAL B  177 ? 0.21980 0.23970 0.23630 0.03600  -0.03890 -0.03070 171 VAL B CB  
3994 C CG1 . VAL B  177 ? 0.19980 0.21290 0.19650 0.04440  -0.04160 -0.03030 171 VAL B CG1 
3995 C CG2 . VAL B  177 ? 0.21090 0.22770 0.23270 0.02920  -0.04160 -0.02860 171 VAL B CG2 
3996 N N   . ALA B  178 ? 0.21730 0.22840 0.21280 0.04930  -0.02060 -0.03260 172 ALA B N   
3997 C CA  . ALA B  178 ? 0.29330 0.29010 0.25650 0.05910  -0.01340 -0.03600 172 ALA B CA  
3998 C C   . ALA B  178 ? 0.28220 0.27890 0.24950 0.06520  0.00780  -0.02120 172 ALA B C   
3999 O O   . ALA B  178 ? 0.27980 0.26670 0.22180 0.07240  0.01750  -0.01500 172 ALA B O   
4000 C CB  . ALA B  178 ? 0.29450 0.27630 0.23980 0.06020  -0.01580 -0.05310 172 ALA B CB  
4001 N N   . GLU B  179 ? 0.22420 0.23490 0.22600 0.06320  0.01590  -0.01220 173 GLU B N   
4002 C CA  . GLU B  179 ? 0.22750 0.24970 0.24780 0.06990  0.03750  0.00580  173 GLU B CA  
4003 C C   . GLU B  179 ? 0.23750 0.27230 0.27100 0.05940  0.03660  0.02150  173 GLU B C   
4004 O O   . GLU B  179 ? 0.27110 0.30360 0.29710 0.06520  0.05550  0.03330  173 GLU B O   
4005 C CB  . GLU B  179 ? 0.21550 0.25760 0.27750 0.07190  0.04260  0.01560  173 GLU B CB  
4006 C CG  . GLU B  179 ? 0.26170 0.27910 0.30560 0.08810  0.05720  0.00490  173 GLU B CG  
4007 C CD  . GLU B  179 ? 0.31490 0.34660 0.39700 0.09360  0.06110  0.01600  173 GLU B CD  
4008 O OE1 . GLU B  179 ? 0.25730 0.32200 0.37780 0.08330  0.04720  0.03080  173 GLU B OE1 
4009 O OE2 . GLU B  179 ? 0.30860 0.31410 0.37730 0.10910  0.07810  0.01050  173 GLU B OE2 
4010 N N   . LEU B  180 ? 0.19590 0.23670 0.24270 0.04340  0.01690  0.02130  174 LEU B N   
4011 C CA  . LEU B  180 ? 0.20430 0.24470 0.25690 0.02980  0.01520  0.03340  174 LEU B CA  
4012 C C   . LEU B  180 ? 0.22340 0.23670 0.23460 0.03760  0.02100  0.03140  174 LEU B C   
4013 O O   . LEU B  180 ? 0.25550 0.26320 0.26690 0.03230  0.03250  0.04620  174 LEU B O   
4014 C CB  . LEU B  180 ? 0.17840 0.21670 0.23840 0.01210  -0.00630 0.02970  174 LEU B CB  
4015 C CG  . LEU B  180 ? 0.19750 0.26280 0.29440 0.00160  -0.01640 0.03670  174 LEU B CG  
4016 C CD1 . LEU B  180 ? 0.22540 0.27430 0.30570 -0.01120 -0.03670 0.02710  174 LEU B CD1 
4017 C CD2 . LEU B  180 ? 0.14740 0.24190 0.28650 -0.01210 -0.01130 0.05920  174 LEU B CD2 
4018 N N   . CYS B  181 ? 0.24910 0.20140 0.25140 0.03200  0.02820  -0.00960 175 CYS B N   
4019 C CA  . CYS B  181 ? 0.22150 0.18040 0.21350 0.02920  0.02750  -0.00930 175 CYS B CA  
4020 C C   . CYS B  181 ? 0.26520 0.23220 0.25030 0.03060  0.03230  -0.01530 175 CYS B C   
4021 O O   . CYS B  181 ? 0.25490 0.23030 0.22980 0.02890  0.03210  -0.01360 175 CYS B O   
4022 C CB  . CYS B  181 ? 0.24530 0.20030 0.23300 0.02630  0.02290  -0.01190 175 CYS B CB  
4023 S SG  . CYS B  181 ? 0.24630 0.19570 0.23940 0.02480  0.01830  -0.00540 175 CYS B SG  
4024 N N   . ASP B  182 ? 0.28110 0.24600 0.27110 0.03440  0.03680  -0.02220 176 ASP B N   
4025 C CA  . ASP B  182 ? 0.28510 0.25660 0.26820 0.03670  0.04220  -0.03190 176 ASP B CA  
4026 C C   . ASP B  182 ? 0.29200 0.26380 0.26280 0.03340  0.03890  -0.04020 176 ASP B C   
4027 O O   . ASP B  182 ? 0.31000 0.29380 0.26790 0.03300  0.04070  -0.04360 176 ASP B O   
4028 C CB  . ASP B  182 ? 0.27570 0.26270 0.25510 0.03770  0.04770  -0.02650 176 ASP B CB  
4029 C CG  . ASP B  182 ? 0.32540 0.31470 0.31940 0.04010  0.05040  -0.01960 176 ASP B CG  
4030 O OD1 . ASP B  182 ? 0.35370 0.33650 0.35860 0.04450  0.05150  -0.02370 176 ASP B OD1 
4031 O OD2 . ASP B  182 ? 0.30230 0.30000 0.29810 0.03740  0.05110  -0.00960 176 ASP B OD2 
4032 N N   . LEU B  183 ? 0.29610 0.25610 0.27140 0.03080  0.03400  -0.04340 177 LEU B N   
4033 C CA  . LEU B  183 ? 0.30780 0.26850 0.27560 0.02640  0.02960  -0.05190 177 LEU B CA  
4034 C C   . LEU B  183 ? 0.31120 0.25840 0.28620 0.02610  0.03060  -0.06480 177 LEU B C   
4035 O O   . LEU B  183 ? 0.30620 0.24050 0.29410 0.02850  0.03250  -0.06250 177 LEU B O   
4036 C CB  . LEU B  183 ? 0.29500 0.25510 0.26440 0.02220  0.02270  -0.04390 177 LEU B CB  
4037 C CG  . LEU B  183 ? 0.29190 0.26310 0.25500 0.02240  0.02100  -0.03200 177 LEU B CG  
4038 C CD1 . LEU B  183 ? 0.27270 0.24090 0.24120 0.01990  0.01530  -0.02550 177 LEU B CD1 
4039 C CD2 . LEU B  183 ? 0.33200 0.31820 0.27990 0.02190  0.02040  -0.03510 177 LEU B CD2 
4040 N N   . ASP B  184 ? 0.29660 0.24700 0.26380 0.02280  0.02860  -0.07790 178 ASP B N   
4041 C CA  . ASP B  184 ? 0.33480 0.27020 0.31110 0.01990  0.02790  -0.09040 178 ASP B CA  
4042 C C   . ASP B  184 ? 0.32670 0.25440 0.31320 0.01410  0.02240  -0.08310 178 ASP B C   
4043 O O   . ASP B  184 ? 0.28160 0.21910 0.26460 0.01180  0.01780  -0.07290 178 ASP B O   
4044 C CB  . ASP B  184 ? 0.34090 0.28370 0.30590 0.01650  0.02620  -0.10830 178 ASP B CB  
4045 C CG  . ASP B  184 ? 0.46610 0.41740 0.42020 0.02270  0.03340  -0.11750 178 ASP B CG  
4046 O OD1 . ASP B  184 ? 0.49750 0.44050 0.46040 0.02950  0.04070  -0.11740 178 ASP B OD1 
4047 O OD2 . ASP B  184 ? 0.53450 0.50310 0.47110 0.02120  0.03170  -0.12430 178 ASP B OD2 
4048 N N   . ALA B  185 ? 0.30040 0.21020 0.30090 0.01230  0.02350  -0.08760 179 ALA B N   
4049 C CA  . ALA B  185 ? 0.26990 0.17250 0.28170 0.00690  0.02010  -0.07940 179 ALA B CA  
4050 C C   . ALA B  185 ? 0.26500 0.18100 0.27220 -0.00060 0.01310  -0.08140 179 ALA B C   
4051 O O   . ALA B  185 ? 0.26340 0.18400 0.27450 -0.00290 0.01030  -0.07020 179 ALA B O   
4052 C CB  . ALA B  185 ? 0.32140 0.20280 0.34890 0.00470  0.02260  -0.08560 179 ALA B CB  
4053 N N   . GLY B  186 ? 0.28160 0.20560 0.28060 -0.00410 0.01020  -0.09600 180 GLY B N   
4054 C CA  . GLY B  186 ? 0.30390 0.24270 0.30020 -0.01120 0.00250  -0.09890 180 GLY B CA  
4055 C C   . GLY B  186 ? 0.32150 0.27960 0.30660 -0.00820 -0.00100 -0.08710 180 GLY B C   
4056 O O   . GLY B  186 ? 0.31320 0.28470 0.29900 -0.01270 -0.00770 -0.08560 180 GLY B O   
4057 N N   . ASP B  187 ? 0.29210 0.25200 0.26880 -0.00080 0.00330  -0.07840 181 ASP B N   
4058 C CA  . ASP B  187 ? 0.28360 0.25820 0.25200 0.00230  0.00070  -0.06560 181 ASP B CA  
4059 C C   . ASP B  187 ? 0.27240 0.24120 0.25050 0.00430  0.00160  -0.05090 181 ASP B C   
4060 O O   . ASP B  187 ? 0.28670 0.26430 0.26080 0.00700  -0.00020 -0.04030 181 ASP B O   
4061 C CB  . ASP B  187 ? 0.31180 0.29350 0.26610 0.00780  0.00500  -0.06460 181 ASP B CB  
4062 C CG  . ASP B  187 ? 0.34550 0.34070 0.28500 0.00620  0.00290  -0.07760 181 ASP B CG  
4063 O OD1 . ASP B  187 ? 0.46180 0.46680 0.39950 0.00110  -0.00450 -0.08360 181 ASP B OD1 
4064 O OD2 . ASP B  187 ? 0.46070 0.45910 0.39020 0.01010  0.00860  -0.08230 181 ASP B OD2 
4065 N N   . VAL B  188 ? 0.23900 0.19340 0.22940 0.00300  0.00440  -0.05020 182 VAL B N   
4066 C CA  . VAL B  188 ? 0.23550 0.18620 0.23440 0.00380  0.00480  -0.03870 182 VAL B CA  
4067 C C   . VAL B  188 ? 0.26860 0.21950 0.27860 -0.00270 0.00210  -0.04050 182 VAL B C   
4068 O O   . VAL B  188 ? 0.25130 0.19250 0.26880 -0.00730 0.00320  -0.04820 182 VAL B O   
4069 C CB  . VAL B  188 ? 0.26020 0.19740 0.26400 0.00770  0.01020  -0.03400 182 VAL B CB  
4070 C CG1 . VAL B  188 ? 0.22840 0.16490 0.23780 0.00850  0.01020  -0.02320 182 VAL B CG1 
4071 C CG2 . VAL B  188 ? 0.25070 0.18950 0.24690 0.01320  0.01330  -0.03330 182 VAL B CG2 
4072 N N   . GLU B  189 ? 0.25010 0.21150 0.26290 -0.00300 -0.00090 -0.03330 183 GLU B N   
4073 C CA  A GLU B  189 ? 0.26190 0.22730 0.28740 -0.00890 -0.00260 -0.03300 183 GLU B CA  
4074 C CA  B GLU B  189 ? 0.26190 0.22770 0.28730 -0.00880 -0.00270 -0.03280 183 GLU B CA  
4075 C C   . GLU B  189 ? 0.24010 0.19950 0.27240 -0.00700 0.00200  -0.02290 183 GLU B C   
4076 O O   . GLU B  189 ? 0.24480 0.20140 0.27130 -0.00090 0.00430  -0.01630 183 GLU B O   
4077 C CB  A GLU B  189 ? 0.28200 0.26700 0.30760 -0.01000 -0.00900 -0.03270 183 GLU B CB  
4078 C CB  B GLU B  189 ? 0.28070 0.26610 0.30640 -0.00940 -0.00890 -0.03150 183 GLU B CB  
4079 C CG  A GLU B  189 ? 0.28360 0.27690 0.30290 -0.01390 -0.01450 -0.04420 183 GLU B CG  
4080 C CG  B GLU B  189 ? 0.28330 0.27980 0.30140 -0.01200 -0.01500 -0.04100 183 GLU B CG  
4081 C CD  A GLU B  189 ? 0.31320 0.32860 0.32990 -0.01330 -0.02210 -0.04260 183 GLU B CD  
4082 C CD  B GLU B  189 ? 0.31090 0.30560 0.33700 -0.02130 -0.01720 -0.05390 183 GLU B CD  
4083 O OE1 A GLU B  189 ? 0.30440 0.32920 0.33040 -0.01170 -0.02360 -0.03450 183 GLU B OE1 
4084 O OE1 B GLU B  189 ? 0.28600 0.27540 0.32750 -0.02710 -0.01530 -0.05320 183 GLU B OE1 
4085 O OE2 A GLU B  189 ? 0.33150 0.35600 0.33660 -0.01360 -0.02650 -0.04940 183 GLU B OE2 
4086 O OE2 B GLU B  189 ? 0.32340 0.32210 0.34040 -0.02330 -0.02050 -0.06520 183 GLU B OE2 
4087 N N   . TRP B  190 ? 0.21030 0.16850 0.25520 -0.01310 0.00340  -0.02220 184 TRP B N   
4088 C CA  . TRP B  190 ? 0.21270 0.16630 0.26270 -0.01190 0.00860  -0.01240 184 TRP B CA  
4089 C C   . TRP B  190 ? 0.22670 0.19370 0.28790 -0.01610 0.00880  -0.00870 184 TRP B C   
4090 O O   . TRP B  190 ? 0.27240 0.24490 0.34440 -0.02380 0.00640  -0.01360 184 TRP B O   
4091 C CB  . TRP B  190 ? 0.23440 0.17030 0.28970 -0.01450 0.01280  -0.01190 184 TRP B CB  
4092 C CG  . TRP B  190 ? 0.25070 0.17600 0.29680 -0.00870 0.01340  -0.01480 184 TRP B CG  
4093 C CD1 . TRP B  190 ? 0.25560 0.17680 0.29790 -0.00900 0.01160  -0.02550 184 TRP B CD1 
4094 C CD2 . TRP B  190 ? 0.23660 0.15710 0.27630 -0.00160 0.01610  -0.00750 184 TRP B CD2 
4095 N NE1 . TRP B  190 ? 0.27250 0.18690 0.30760 -0.00200 0.01390  -0.02450 184 TRP B NE1 
4096 C CE2 . TRP B  190 ? 0.27560 0.18970 0.30990 0.00230  0.01610  -0.01340 184 TRP B CE2 
4097 C CE3 . TRP B  190 ? 0.26040 0.18350 0.29820 0.00190  0.01830  0.00250  184 TRP B CE3 
4098 C CZ2 . TRP B  190 ? 0.25530 0.16580 0.28510 0.00900  0.01790  -0.00860 184 TRP B CZ2 
4099 C CZ3 . TRP B  190 ? 0.25220 0.17140 0.28340 0.00850  0.01910  0.00630  184 TRP B CZ3 
4100 C CH2 . TRP B  190 ? 0.22380 0.13710 0.25250 0.01170  0.01870  0.00110  184 TRP B CH2 
4101 N N   . GLY B  191 ? 0.18980 0.16300 0.24940 -0.01110 0.01180  -0.00080 185 GLY B N   
4102 C CA  . GLY B  191 ? 0.23210 0.21790 0.30290 -0.01390 0.01470  0.00420  185 GLY B CA  
4103 C C   . GLY B  191 ? 0.25000 0.23060 0.31850 -0.01170 0.02160  0.01300  185 GLY B C   
4104 O O   . GLY B  191 ? 0.25200 0.21810 0.31370 -0.01010 0.02310  0.01520  185 GLY B O   
4105 N N   . THR B  192 ? 0.20660 0.20050 0.28010 -0.01110 0.02590  0.01840  186 THR B N   
4106 C CA  . THR B  192 ? 0.22750 0.22070 0.29660 -0.00880 0.03270  0.02700  186 THR B CA  
4107 C C   . THR B  192 ? 0.24380 0.24620 0.30370 0.00010  0.03390  0.02640  186 THR B C   
4108 O O   . THR B  192 ? 0.21000 0.22540 0.27550 0.00260  0.03280  0.02300  186 THR B O   
4109 C CB  . THR B  192 ? 0.21900 0.22110 0.30260 -0.01660 0.03860  0.03390  186 THR B CB  
4110 O OG1 . THR B  192 ? 0.28200 0.27100 0.37520 -0.02540 0.03750  0.03370  186 THR B OG1 
4111 C CG2 . THR B  192 ? 0.22560 0.23120 0.30210 -0.01360 0.04620  0.04400  186 THR B CG2 
4112 N N   . ASP B  193 ? 0.25990 0.25540 0.30640 0.00530  0.03550  0.02900  187 ASP B N   
4113 C CA  . ASP B  193 ? 0.21450 0.21490 0.25090 0.01330  0.03600  0.02610  187 ASP B CA  
4114 C C   . ASP B  193 ? 0.23600 0.25160 0.27260 0.01490  0.04320  0.02980  187 ASP B C   
4115 O O   . ASP B  193 ? 0.24730 0.26940 0.29070 0.00960  0.04850  0.03710  187 ASP B O   
4116 C CB  . ASP B  193 ? 0.23600 0.22460 0.25910 0.01670  0.03370  0.02640  187 ASP B CB  
4117 C CG  . ASP B  193 ? 0.32680 0.31080 0.34440 0.02180  0.02880  0.01900  187 ASP B CG  
4118 O OD1 . ASP B  193 ? 0.30780 0.29830 0.32910 0.02490  0.02870  0.01470  187 ASP B OD1 
4119 O OD2 . ASP B  193 ? 0.33500 0.30890 0.34620 0.02280  0.02550  0.01820  187 ASP B OD2 
4120 N N   . GLY B  194 ? 0.22090 0.24230 0.25060 0.02230  0.04420  0.02430  188 GLY B N   
4121 C CA  . GLY B  194 ? 0.26760 0.30470 0.29470 0.02520  0.05200  0.02590  188 GLY B CA  
4122 C C   . GLY B  194 ? 0.22860 0.26670 0.24440 0.02320  0.05630  0.03450  188 GLY B C   
4123 O O   . GLY B  194 ? 0.21250 0.26530 0.22860 0.02230  0.06420  0.04050  188 GLY B O   
4124 N N   . CYS B  195 ? 0.21160 0.23580 0.21820 0.02280  0.05140  0.03670  189 CYS B N   
4125 C CA  . CYS B  195 ? 0.24000 0.26500 0.23600 0.02210  0.05400  0.04670  189 CYS B CA  
4126 C C   . CYS B  195 ? 0.28200 0.30080 0.28840 0.01480  0.05630  0.05890  189 CYS B C   
4127 O O   . CYS B  195 ? 0.26410 0.28210 0.26410 0.01420  0.05860  0.07040  189 CYS B O   
4128 C CB  . CYS B  195 ? 0.21600 0.23100 0.20010 0.02580  0.04720  0.04360  189 CYS B CB  
4129 S SG  . CYS B  195 ? 0.26230 0.25750 0.25600 0.02250  0.04040  0.04320  189 CYS B SG  
4130 N N   . ASN B  196 ? 0.21810 0.23270 0.24080 0.00930  0.05520  0.05650  190 ASN B N   
4131 C CA  . ASN B  196 ? 0.21860 0.22670 0.25550 0.00080  0.05740  0.06480  190 ASN B CA  
4132 C C   . ASN B  196 ? 0.24480 0.23190 0.28270 -0.00070 0.05230  0.06610  190 ASN B C   
4133 O O   . ASN B  196 ? 0.27350 0.25150 0.32210 -0.00710 0.05470  0.07440  190 ASN B O   
4134 C CB  . ASN B  196 ? 0.28510 0.30330 0.32300 -0.00260 0.06630  0.07910  190 ASN B CB  
4135 C CG  . ASN B  196 ? 0.28580 0.30470 0.34450 -0.01280 0.07020  0.08440  190 ASN B CG  
4136 O OD1 . ASN B  196 ? 0.30250 0.32290 0.37430 -0.01650 0.06680  0.07520  190 ASN B OD1 
4137 N ND2 . ASN B  196 ? 0.32200 0.34090 0.38500 -0.01790 0.07700  0.09990  190 ASN B ND2 
4138 N N   . LEU B  197 ? 0.21420 0.19310 0.24350 0.00470  0.04580  0.05820  191 LEU B N   
4139 C CA  . LEU B  197 ? 0.22440 0.18560 0.25640 0.00420  0.04120  0.05640  191 LEU B CA  
4140 C C   . LEU B  197 ? 0.22530 0.18230 0.26520 0.00120  0.03690  0.04500  191 LEU B C   
4141 O O   . LEU B  197 ? 0.24300 0.21020 0.28310 0.00210  0.03550  0.03830  191 LEU B O   
4142 C CB  . LEU B  197 ? 0.21460 0.17240 0.23340 0.01170  0.03700  0.05460  191 LEU B CB  
4143 C CG  . LEU B  197 ? 0.26150 0.22160 0.27130 0.01540  0.03850  0.06590  191 LEU B CG  
4144 C CD1 . LEU B  197 ? 0.23980 0.20140 0.23880 0.02170  0.03290  0.06000  191 LEU B CD1 
4145 C CD2 . LEU B  197 ? 0.29390 0.23970 0.31260 0.01350  0.03970  0.07600  191 LEU B CD2 
4146 N N   . PRO B  198 ? 0.25560 0.19810 0.30150 -0.00140 0.03460  0.04230  192 PRO B N   
4147 C CA  . PRO B  198 ? 0.25100 0.19110 0.29920 -0.00270 0.02970  0.03050  192 PRO B CA  
4148 C C   . PRO B  198 ? 0.23940 0.18340 0.27600 0.00420  0.02600  0.02530  192 PRO B C   
4149 O O   . PRO B  198 ? 0.21360 0.15560 0.24180 0.00950  0.02590  0.02840  192 PRO B O   
4150 C CB  . PRO B  198 ? 0.27510 0.19780 0.32900 -0.00480 0.02910  0.02860  192 PRO B CB  
4151 C CG  . PRO B  198 ? 0.28880 0.20440 0.34980 -0.00730 0.03430  0.04080  192 PRO B CG  
4152 C CD  . PRO B  198 ? 0.25290 0.18080 0.30350 -0.00240 0.03660  0.05000  192 PRO B CD  
4153 N N   . THR B  199 ? 0.23390 0.18450 0.27120 0.00380  0.02260  0.01790  193 THR B N   
4154 C CA  . THR B  199 ? 0.22070 0.17360 0.24910 0.00950  0.01960  0.01440  193 THR B CA  
4155 C C   . THR B  199 ? 0.24190 0.19400 0.27040 0.00840  0.01550  0.00740  193 THR B C   
4156 O O   . THR B  199 ? 0.22110 0.17790 0.25610 0.00370  0.01380  0.00400  193 THR B O   
4157 C CB  . THR B  199 ? 0.20290 0.16730 0.22990 0.01280  0.02060  0.01530  193 THR B CB  
4158 O OG1 . THR B  199 ? 0.23380 0.19660 0.25350 0.01810  0.01820  0.01260  193 THR B OG1 
4159 C CG2 . THR B  199 ? 0.19860 0.17490 0.23530 0.01020  0.01990  0.01320  193 THR B CG2 
4160 N N   . PRO B  200 ? 0.24310 0.19050 0.26440 0.01190  0.01370  0.00530  194 PRO B N   
4161 C CA  . PRO B  200 ? 0.24200 0.18970 0.26100 0.01100  0.01080  -0.00060 194 PRO B CA  
4162 C C   . PRO B  200 ? 0.21360 0.17070 0.22970 0.01320  0.00750  -0.00080 194 PRO B C   
4163 O O   . PRO B  200 ? 0.20020 0.15950 0.21500 0.01710  0.00760  0.00280  194 PRO B O   
4164 C CB  . PRO B  200 ? 0.23940 0.17900 0.25340 0.01420  0.01210  -0.00100 194 PRO B CB  
4165 C CG  . PRO B  200 ? 0.19310 0.13340 0.20490 0.01780  0.01290  0.00430  194 PRO B CG  
4166 C CD  . PRO B  200 ? 0.22660 0.16890 0.24250 0.01620  0.01480  0.00820  194 PRO B CD  
4167 N N   . ALA B  201 ? 0.21150 0.17370 0.22610 0.01090  0.00430  -0.00520 195 ALA B N   
4168 C CA  . ALA B  201 ? 0.17320 0.14400 0.18310 0.01360  0.00070  -0.00390 195 ALA B CA  
4169 C C   . ALA B  201 ? 0.20380 0.17400 0.20480 0.01330  0.00010  -0.00780 195 ALA B C   
4170 O O   . ALA B  201 ? 0.23090 0.19940 0.23140 0.00950  0.00010  -0.01530 195 ALA B O   
4171 C CB  . ALA B  201 ? 0.20540 0.18990 0.22130 0.01180  -0.00360 -0.00440 195 ALA B CB  
4172 N N   . PHE B  202 ? 0.20530 0.17730 0.20010 0.01700  0.00000  -0.00310 196 PHE B N   
4173 C CA  . PHE B  202 ? 0.21050 0.18510 0.19570 0.01730  0.00060  -0.00520 196 PHE B CA  
4174 C C   . PHE B  202 ? 0.22570 0.20610 0.20640 0.02070  -0.00060 0.00360  196 PHE B C   
4175 O O   . PHE B  202 ? 0.22640 0.20570 0.21290 0.02320  -0.00190 0.01000  196 PHE B O   
4176 C CB  . PHE B  202 ? 0.24160 0.20640 0.22640 0.01790  0.00580  -0.00800 196 PHE B CB  
4177 C CG  . PHE B  202 ? 0.23890 0.19590 0.22940 0.02000  0.00810  -0.00260 196 PHE B CG  
4178 C CD1 . PHE B  202 ? 0.22870 0.18610 0.21850 0.02220  0.00870  0.00390  196 PHE B CD1 
4179 C CD2 . PHE B  202 ? 0.24120 0.19100 0.23810 0.01930  0.00940  -0.00380 196 PHE B CD2 
4180 C CE1 . PHE B  202 ? 0.20890 0.16040 0.20390 0.02340  0.00980  0.00670  196 PHE B CE1 
4181 C CE2 . PHE B  202 ? 0.24710 0.19270 0.24710 0.02140  0.01060  0.00060  196 PHE B CE2 
4182 C CZ  . PHE B  202 ? 0.21720 0.16390 0.21610 0.02320  0.01050  0.00460  196 PHE B CZ  
4183 N N   . PRO B  203 ? 0.22480 0.21180 0.19550 0.02110  -0.00010 0.00440  197 PRO B N   
4184 C CA  . PRO B  203 ? 0.21200 0.20430 0.17900 0.02410  -0.00100 0.01550  197 PRO B CA  
4185 C C   . PRO B  203 ? 0.20170 0.18280 0.17630 0.02580  0.00240  0.02250  197 PRO B C   
4186 O O   . PRO B  203 ? 0.20920 0.18260 0.18670 0.02480  0.00640  0.01920  197 PRO B O   
4187 C CB  . PRO B  203 ? 0.26640 0.26770 0.22030 0.02360  0.00120  0.01440  197 PRO B CB  
4188 C CG  . PRO B  203 ? 0.24960 0.25510 0.19930 0.02070  -0.00050 0.00090  197 PRO B CG  
4189 C CD  . PRO B  203 ? 0.26110 0.25340 0.22290 0.01900  0.00070  -0.00500 197 PRO B CD  
4190 N N   . LEU B  204 ? 0.25380 0.23430 0.23270 0.02870  0.00020  0.03170  198 LEU B N   
4191 C CA  . LEU B  204 ? 0.21450 0.18310 0.20250 0.02980  0.00240  0.03610  198 LEU B CA  
4192 C C   . LEU B  204 ? 0.21450 0.17950 0.20140 0.02750  0.00720  0.03820  198 LEU B C   
4193 O O   . LEU B  204 ? 0.22550 0.18200 0.21940 0.02620  0.00910  0.03540  198 LEU B O   
4194 C CB  . LEU B  204 ? 0.20140 0.16880 0.19480 0.03390  -0.00020 0.04620  198 LEU B CB  
4195 C CG  . LEU B  204 ? 0.19970 0.15290 0.20430 0.03520  0.00160  0.04900  198 LEU B CG  
4196 C CD1 . LEU B  204 ? 0.22100 0.16830 0.23120 0.03510  0.00190  0.03870  198 LEU B CD1 
4197 C CD2 . LEU B  204 ? 0.24880 0.19970 0.25990 0.04030  -0.00070 0.05960  198 LEU B CD2 
4198 N N   . ASP B  205 ? 0.22520 0.19880 0.20350 0.02680  0.00920  0.04300  199 ASP B N   
4199 C CA  . ASP B  205 ? 0.21960 0.19240 0.19900 0.02440  0.01480  0.04580  199 ASP B CA  
4200 C C   . ASP B  205 ? 0.26280 0.23350 0.24490 0.02300  0.01730  0.03540  199 ASP B C   
4201 O O   . ASP B  205 ? 0.23480 0.20250 0.22430 0.02130  0.02050  0.03640  199 ASP B O   
4202 C CB  . ASP B  205 ? 0.23710 0.22290 0.20520 0.02420  0.01790  0.05230  199 ASP B CB  
4203 C CG  . ASP B  205 ? 0.31760 0.31430 0.27300 0.02470  0.01780  0.04180  199 ASP B CG  
4204 O OD1 . ASP B  205 ? 0.24490 0.24430 0.19660 0.02560  0.01230  0.03710  199 ASP B OD1 
4205 O OD2 . ASP B  205 ? 0.30090 0.30400 0.25130 0.02400  0.02330  0.03760  199 ASP B OD2 
4206 N N   . ARG B  206 ? 0.20080 0.17290 0.17870 0.02370  0.01570  0.02590  200 ARG B N   
4207 C CA  . ARG B  206 ? 0.22340 0.19220 0.20500 0.02340  0.01830  0.01790  200 ARG B CA  
4208 C C   . ARG B  206 ? 0.23050 0.19020 0.22200 0.02330  0.01660  0.01750  200 ARG B C   
4209 O O   . ARG B  206 ? 0.24940 0.20770 0.24590 0.02330  0.01860  0.01500  200 ARG B O   
4210 C CB  . ARG B  206 ? 0.25540 0.22570 0.23180 0.02360  0.01740  0.00820  200 ARG B CB  
4211 C CG  . ARG B  206 ? 0.23300 0.21420 0.19750 0.02360  0.01820  0.00580  200 ARG B CG  
4212 C CD  . ARG B  206 ? 0.25910 0.24720 0.22000 0.02460  0.02480  0.00660  200 ARG B CD  
4213 N NE  . ARG B  206 ? 0.29310 0.29440 0.23960 0.02480  0.02600  0.00550  200 ARG B NE  
4214 C CZ  . ARG B  206 ? 0.34770 0.35550 0.28680 0.02590  0.03020  -0.00470 200 ARG B CZ  
4215 N NH1 . ARG B  206 ? 0.31300 0.31350 0.25950 0.02750  0.03360  -0.01430 200 ARG B NH1 
4216 N NH2 . ARG B  206 ? 0.37580 0.39820 0.29950 0.02620  0.03110  -0.00510 200 ARG B NH2 
4217 N N   . LEU B  207 ? 0.21360 0.16870 0.20790 0.02360  0.01310  0.02000  201 LEU B N   
4218 C CA  . LEU B  207 ? 0.22510 0.17330 0.22680 0.02350  0.01200  0.01900  201 LEU B CA  
4219 C C   . LEU B  207 ? 0.19050 0.13720 0.19850 0.02150  0.01360  0.02270  201 LEU B C   
4220 O O   . LEU B  207 ? 0.21770 0.16320 0.23110 0.02050  0.01330  0.01980  201 LEU B O   
4221 C CB  . LEU B  207 ? 0.23170 0.17640 0.23540 0.02510  0.00910  0.01960  201 LEU B CB  
4222 C CG  . LEU B  207 ? 0.23080 0.16990 0.23960 0.02560  0.00810  0.01620  201 LEU B CG  
4223 C CD1 . LEU B  207 ? 0.22540 0.16590 0.23240 0.02540  0.00850  0.01160  201 LEU B CD1 
4224 C CD2 . LEU B  207 ? 0.19210 0.12920 0.20340 0.02840  0.00650  0.01620  201 LEU B CD2 
4225 N N   . GLY B  208 ? 0.21280 0.16060 0.22110 0.02050  0.01490  0.02990  202 GLY B N   
4226 C CA  . GLY B  208 ? 0.21830 0.16530 0.23510 0.01700  0.01710  0.03420  202 GLY B CA  
4227 C C   . GLY B  208 ? 0.23160 0.18730 0.24960 0.01580  0.02070  0.03220  202 GLY B C   
4228 O O   . GLY B  208 ? 0.20370 0.16050 0.23140 0.01310  0.02100  0.03140  202 GLY B O   
4229 N N   . ARG B  209 ? 0.20730 0.17020 0.21650 0.01810  0.02330  0.03030  203 ARG B N   
4230 C CA  . ARG B  209 ? 0.21800 0.18920 0.22910 0.01880  0.02760  0.02710  203 ARG B CA  
4231 C C   . ARG B  209 ? 0.23830 0.20700 0.25670 0.02010  0.02530  0.02130  203 ARG B C   
4232 O O   . ARG B  209 ? 0.21740 0.19260 0.24490 0.01970  0.02720  0.02140  203 ARG B O   
4233 C CB  . ARG B  209 ? 0.20150 0.17840 0.20110 0.02170  0.03030  0.02290  203 ARG B CB  
4234 C CG  . ARG B  209 ? 0.29010 0.27610 0.29230 0.02360  0.03630  0.01910  203 ARG B CG  
4235 C CD  . ARG B  209 ? 0.25850 0.24810 0.24960 0.02680  0.03880  0.01110  203 ARG B CD  
4236 N NE  . ARG B  209 ? 0.27450 0.27170 0.25250 0.02570  0.03990  0.01470  203 ARG B NE  
4237 C CZ  . ARG B  209 ? 0.31920 0.32710 0.28680 0.02750  0.04480  0.01000  203 ARG B CZ  
4238 N NH1 . ARG B  209 ? 0.30520 0.31610 0.27560 0.03090  0.05000  0.00090  203 ARG B NH1 
4239 N NH2 . ARG B  209 ? 0.30580 0.32250 0.25970 0.02650  0.04470  0.01460  203 ARG B NH2 
4240 N N   . ILE B  210 ? 0.21700 0.17820 0.23240 0.02170  0.02110  0.01730  204 ILE B N   
4241 C CA  . ILE B  210 ? 0.22150 0.18150 0.24210 0.02320  0.01870  0.01400  204 ILE B CA  
4242 C C   . ILE B  210 ? 0.21560 0.17760 0.24520 0.02030  0.01620  0.01560  204 ILE B C   
4243 O O   . ILE B  210 ? 0.19680 0.16520 0.23400 0.02090  0.01530  0.01480  204 ILE B O   
4244 C CB  . ILE B  210 ? 0.24030 0.19320 0.25560 0.02470  0.01560  0.01140  204 ILE B CB  
4245 C CG1 . ILE B  210 ? 0.22230 0.17340 0.23190 0.02650  0.01750  0.00820  204 ILE B CG1 
4246 C CG2 . ILE B  210 ? 0.26790 0.22090 0.28710 0.02610  0.01300  0.01050  204 ILE B CG2 
4247 C CD1 . ILE B  210 ? 0.17500 0.12070 0.18100 0.02610  0.01490  0.00690  204 ILE B CD1 
4248 N N   . TYR B  211 ? 0.19760 0.15440 0.22790 0.01710  0.01450  0.01740  205 TYR B N   
4249 C CA  . TYR B  211 ? 0.21280 0.16980 0.25240 0.01340  0.01150  0.01630  205 TYR B CA  
4250 C C   . TYR B  211 ? 0.19110 0.15600 0.24170 0.00920  0.01440  0.02030  205 TYR B C   
4251 O O   . TYR B  211 ? 0.23060 0.20170 0.29140 0.00630  0.01180  0.01830  205 TYR B O   
4252 C CB  . TYR B  211 ? 0.20600 0.15240 0.24450 0.01200  0.00900  0.01520  205 TYR B CB  
4253 C CG  . TYR B  211 ? 0.21820 0.16140 0.24940 0.01550  0.00600  0.00980  205 TYR B CG  
4254 C CD1 . TYR B  211 ? 0.20010 0.14280 0.22280 0.01930  0.00730  0.01040  205 TYR B CD1 
4255 C CD2 . TYR B  211 ? 0.21360 0.15600 0.24660 0.01440  0.00210  0.00380  205 TYR B CD2 
4256 C CE1 . TYR B  211 ? 0.18880 0.13010 0.20610 0.02170  0.00560  0.00690  205 TYR B CE1 
4257 C CE2 . TYR B  211 ? 0.21740 0.15950 0.24260 0.01770  0.00050  -0.00020 205 TYR B CE2 
4258 C CZ  . TYR B  211 ? 0.21520 0.15680 0.23320 0.02130  0.00270  0.00220  205 TYR B CZ  
4259 O OH  . TYR B  211 ? 0.21140 0.15420 0.22320 0.02370  0.00190  -0.00080 205 TYR B OH  
4260 N N   . ALA B  212 ? 0.19180 0.15910 0.24030 0.00880  0.01970  0.02620  206 ALA B N   
4261 C CA  . ALA B  212 ? 0.19890 0.17730 0.25740 0.00540  0.02450  0.03090  206 ALA B CA  
4262 C C   . ALA B  212 ? 0.22300 0.21370 0.28790 0.00830  0.02500  0.02720  206 ALA B C   
4263 O O   . ALA B  212 ? 0.21500 0.21590 0.29440 0.00460  0.02520  0.02830  206 ALA B O   
4264 C CB  . ALA B  212 ? 0.20880 0.19090 0.25950 0.00620  0.03100  0.03760  206 ALA B CB  
4265 N N   . LYS B  213 ? 0.19310 0.18280 0.24940 0.01470  0.02510  0.02310  207 LYS B N   
4266 C CA  . LYS B  213 ? 0.20230 0.20150 0.26550 0.01930  0.02580  0.02050  207 LYS B CA  
4267 C C   . LYS B  213 ? 0.22380 0.22560 0.29510 0.01870  0.01870  0.01860  207 LYS B C   
4268 O O   . LYS B  213 ? 0.21700 0.23210 0.30100 0.01980  0.01820  0.01910  207 LYS B O   
4269 C CB  . LYS B  213 ? 0.18490 0.17850 0.23800 0.02600  0.02770  0.01660  207 LYS B CB  
4270 C CG  . LYS B  213 ? 0.21010 0.20650 0.25580 0.02760  0.03490  0.01590  207 LYS B CG  
4271 C CD  . LYS B  213 ? 0.21250 0.20180 0.25020 0.03310  0.03600  0.00960  207 LYS B CD  
4272 C CE  . LYS B  213 ? 0.27640 0.27030 0.30550 0.03480  0.04280  0.00590  207 LYS B CE  
4273 N NZ  . LYS B  213 ? 0.28110 0.26560 0.30340 0.03880  0.04280  -0.00260 207 LYS B NZ  
4274 N N   . LEU B  214 ? 0.17140 0.16320 0.23560 0.01730  0.01300  0.01630  208 LEU B N   
4275 C CA  . LEU B  214 ? 0.20200 0.19820 0.27090 0.01610  0.00580  0.01360  208 LEU B CA  
4276 C C   . LEU B  214 ? 0.24820 0.25400 0.33210 0.00920  0.00400  0.01360  208 LEU B C   
4277 O O   . LEU B  214 ? 0.23070 0.25040 0.32540 0.00910  0.00010  0.01280  208 LEU B O   
4278 C CB  . LEU B  214 ? 0.20620 0.19090 0.26420 0.01530  0.00170  0.01000  208 LEU B CB  
4279 C CG  . LEU B  214 ? 0.25140 0.23040 0.29760 0.02070  0.00070  0.00950  208 LEU B CG  
4280 C CD1 . LEU B  214 ? 0.24720 0.21730 0.28470 0.01910  -0.00170 0.00570  208 LEU B CD1 
4281 C CD2 . LEU B  214 ? 0.22130 0.21040 0.27010 0.02480  -0.00330 0.01080  208 LEU B CD2 
4282 N N   . ALA B  215 ? 0.17910 0.17820 0.26540 0.00310  0.00660  0.01510  209 ALA B N   
4283 C CA  . ALA B  215 ? 0.20160 0.20760 0.30440 -0.00530 0.00530  0.01540  209 ALA B CA  
4284 C C   . ALA B  215 ? 0.22220 0.24610 0.33890 -0.00570 0.01020  0.02020  209 ALA B C   
4285 O O   . ALA B  215 ? 0.17950 0.21750 0.31320 -0.01070 0.00690  0.01910  209 ALA B O   
4286 C CB  . ALA B  215 ? 0.19580 0.18750 0.29870 -0.01120 0.00780  0.01800  209 ALA B CB  
4287 N N   . SER B  216 ? 0.19650 0.22210 0.30680 -0.00010 0.01790  0.02440  210 SER B N   
4288 C CA  . SER B  216 ? 0.21760 0.26150 0.34060 0.00090  0.02440  0.02810  210 SER B CA  
4289 C C   . SER B  216 ? 0.17540 0.23360 0.30820 0.00640  0.02020  0.02520  210 SER B C   
4290 O O   . SER B  216 ? 0.20470 0.28200 0.35630 0.00420  0.02100  0.02700  210 SER B O   
4291 C CB  . SER B  216 ? 0.20270 0.24480 0.31350 0.00680  0.03330  0.03050  210 SER B CB  
4292 O OG  . SER B  216 ? 0.23280 0.29340 0.35530 0.00790  0.04110  0.03350  210 SER B OG  
4293 N N   . ALA B  217 ? 0.17880 0.22910 0.30020 0.01340  0.01540  0.02190  211 ALA B N   
4294 C CA  . ALA B  217 ? 0.17910 0.24170 0.30870 0.01980  0.01050  0.02130  211 ALA B CA  
4295 C C   . ALA B  217 ? 0.17610 0.25110 0.31790 0.01350  0.00120  0.01940  211 ALA B C   
4296 O O   . ALA B  217 ? 0.22480 0.31960 0.38260 0.01590  -0.00180 0.02080  211 ALA B O   
4297 C CB  . ALA B  217 ? 0.21980 0.26900 0.33380 0.02730  0.00780  0.02000  211 ALA B CB  
4298 N N   . ALA B  218 ? 0.21340 0.27760 0.34860 0.00600  -0.00390 0.01540  212 ALA B N   
4299 C CA  . ALA B  218 ? 0.19620 0.27190 0.34270 -0.00120 -0.01320 0.01100  212 ALA B CA  
4300 C C   . ALA B  218 ? 0.21170 0.30370 0.38170 -0.00920 -0.01080 0.01300  212 ALA B C   
4301 O O   . ALA B  218 ? 0.19380 0.30610 0.38020 -0.01220 -0.01760 0.01110  212 ALA B O   
4302 C CB  . ALA B  218 ? 0.20950 0.26820 0.34490 -0.00760 -0.01760 0.00430  212 ALA B CB  
4303 N N   . ASP B  219 ? 0.18450 0.26970 0.35680 -0.01310 -0.00120 0.01750  213 ASP B N   
4304 C CA  . ASP B  219 ? 0.17380 0.27570 0.36900 -0.02070 0.00360  0.02180  213 ASP B CA  
4305 C C   . ASP B  219 ? 0.19530 0.32270 0.40520 -0.01360 0.00590  0.02490  213 ASP B C   
4306 O O   . ASP B  219 ? 0.21230 0.36210 0.44540 -0.01900 0.00270  0.02500  213 ASP B O   
4307 C CB  . ASP B  219 ? 0.18430 0.27490 0.37490 -0.02390 0.01470  0.02860  213 ASP B CB  
4308 C CG  . ASP B  219 ? 0.23380 0.30500 0.42310 -0.03430 0.01260  0.02780  213 ASP B CG  
4309 O OD1 . ASP B  219 ? 0.22510 0.29410 0.42140 -0.04080 0.00340  0.02040  213 ASP B OD1 
4310 O OD2 . ASP B  219 ? 0.21730 0.27580 0.39880 -0.03550 0.02020  0.03450  213 ASP B OD2 
4311 N N   . GLY B  220 ? 0.20230 0.32690 0.40080 -0.00130 0.01130  0.02680  214 GLY B N   
4312 C CA  . GLY B  220 ? 0.16250 0.30950 0.37620 0.00720  0.01440  0.02930  214 GLY B CA  
4313 C C   . GLY B  220 ? 0.22740 0.39030 0.45200 0.01020  0.00240  0.02740  214 GLY B C   
4314 O O   . GLY B  220 ? 0.20950 0.39880 0.45760 0.01110  0.00140  0.02950  214 GLY B O   
4315 N N   . SER B  221 ? 0.19400 0.34310 0.40180 0.01170  -0.00690 0.02390  215 SER B N   
4316 C CA  . SER B  221 ? 0.25230 0.41680 0.46560 0.01490  -0.01920 0.02290  215 SER B CA  
4317 C C   . SER B  221 ? 0.21990 0.40540 0.45380 0.00310  -0.02710 0.01940  215 SER B C   
4318 O O   . SER B  221 ? 0.16820 0.38130 0.42240 0.00540  -0.03270 0.02140  215 SER B O   
4319 C CB  . SER B  221 ? 0.20040 0.34590 0.38890 0.01720  -0.02610 0.01990  215 SER B CB  
4320 O OG  . SER B  221 ? 0.22900 0.39160 0.42030 0.02060  -0.03820 0.02010  215 SER B OG  
4321 N N   . ASP B  222 ? 0.23870 0.41100 0.46890 -0.00970 -0.02800 0.01400  216 ASP B N   
4322 C CA  . ASP B  222 ? 0.23910 0.42650 0.48880 -0.02330 -0.03580 0.00850  216 ASP B CA  
4323 C C   . ASP B  222 ? 0.19650 0.40960 0.47660 -0.02750 -0.03040 0.01370  216 ASP B C   
4324 O O   . ASP B  222 ? 0.19540 0.43330 0.49790 -0.03490 -0.03890 0.01060  216 ASP B O   
4325 C CB  . ASP B  222 ? 0.25570 0.41800 0.49650 -0.03490 -0.03470 0.00260  216 ASP B CB  
4326 C CG  . ASP B  222 ? 0.33210 0.50280 0.58710 -0.04870 -0.04550 -0.00720 216 ASP B CG  
4327 O OD1 . ASP B  222 ? 0.47450 0.66820 0.73690 -0.04810 -0.05710 -0.01170 216 ASP B OD1 
4328 O OD2 . ASP B  222 ? 0.31100 0.46550 0.57070 -0.06020 -0.04270 -0.01040 216 ASP B OD2 
4329 N N   . ALA B  223 ? 0.17760 0.38720 0.45900 -0.02330 -0.01620 0.02100  217 ALA B N   
4330 C CA  . ALA B  223 ? 0.20870 0.44390 0.51810 -0.02640 -0.00840 0.02670  217 ALA B CA  
4331 C C   . ALA B  223 ? 0.19540 0.45800 0.51920 -0.01330 -0.00920 0.03020  217 ALA B C   
4332 O O   . ALA B  223 ? 0.16760 0.45770 0.51870 -0.01490 -0.00400 0.03420  217 ALA B O   
4333 C CB  . ALA B  223 ? 0.17730 0.39980 0.48020 -0.02690 0.00790  0.03310  217 ALA B CB  
4334 N N   . GLY B  224 ? 0.22130 0.47770 0.52940 -0.00010 -0.01520 0.02950  218 GLY B N   
4335 C CA  . GLY B  224 ? 0.19270 0.47310 0.51580 0.01350  -0.01720 0.03380  218 GLY B CA  
4336 C C   . GLY B  224 ? 0.20700 0.48460 0.52960 0.02690  -0.00270 0.03830  218 GLY B C   
4337 O O   . GLY B  224 ? 0.23290 0.53360 0.57530 0.03790  -0.00140 0.04200  218 GLY B O   
4338 N N   . GLU B  225 ? 0.22060 0.47140 0.52170 0.02700  0.00780  0.03730  219 GLU B N   
4339 C CA  . GLU B  225 ? 0.23710 0.48400 0.53490 0.03920  0.02140  0.03880  219 GLU B CA  
4340 C C   . GLU B  225 ? 0.27090 0.50640 0.55850 0.05520  0.01810  0.03900  219 GLU B C   
4341 O O   . GLU B  225 ? 0.23610 0.45320 0.50520 0.05530  0.00890  0.03820  219 GLU B O   
4342 C CB  . GLU B  225 ? 0.26810 0.49020 0.54340 0.03400  0.03160  0.03720  219 GLU B CB  
4343 C CG  . GLU B  225 ? 0.27840 0.50400 0.55940 0.01790  0.03520  0.03910  219 GLU B CG  
4344 C CD  . GLU B  225 ? 0.29940 0.49780 0.55420 0.01420  0.04230  0.03900  219 GLU B CD  
4345 O OE1 . GLU B  225 ? 0.34280 0.52130 0.57570 0.02340  0.04370  0.03590  219 GLU B OE1 
4346 O OE2 . GLU B  225 ? 0.29710 0.49470 0.55470 0.00210  0.04610  0.04250  219 GLU B OE2 
4347 N N   . GLY B  226 ? 0.24350 0.48890 0.54320 0.06880  0.02660  0.04020  220 GLY B N   
4348 C CA  . GLY B  226 ? 0.27510 0.50360 0.56510 0.08390  0.02610  0.04050  220 GLY B CA  
4349 C C   . GLY B  226 ? 0.22590 0.41960 0.48520 0.08170  0.03030  0.03600  220 GLY B C   
4350 O O   . GLY B  226 ? 0.25380 0.44070 0.50400 0.07630  0.04040  0.03220  220 GLY B O   
4351 N N   . GLN B  227 ? 0.24310 0.41640 0.48630 0.08520  0.02240  0.03730  221 GLN B N   
4352 C CA  . GLN B  227 ? 0.17940 0.32200 0.39530 0.08160  0.02470  0.03330  221 GLN B CA  
4353 C C   . GLN B  227 ? 0.25780 0.38140 0.46740 0.09420  0.02610  0.03380  221 GLN B C   
4354 O O   . GLN B  227 ? 0.22410 0.35410 0.44550 0.10400  0.02070  0.03980  221 GLN B O   
4355 C CB  . GLN B  227 ? 0.24200 0.37560 0.44250 0.07020  0.01420  0.03390  221 GLN B CB  
4356 C CG  . GLN B  227 ? 0.23490 0.37560 0.43660 0.05580  0.01470  0.03160  221 GLN B CG  
4357 C CD  . GLN B  227 ? 0.23930 0.36790 0.42570 0.04620  0.00520  0.02990  221 GLN B CD  
4358 O OE1 . GLN B  227 ? 0.23100 0.36320 0.41600 0.04810  -0.00500 0.03140  221 GLN B OE1 
4359 N NE2 . GLN B  227 ? 0.17110 0.28620 0.34590 0.03660  0.00880  0.02710  221 GLN B NE2 
4360 N N   . SER B  228 ? 0.21220 0.31310 0.40450 0.09370  0.03350  0.02780  222 SER B N   
4361 C CA  . SER B  228 ? 0.23170 0.30930 0.41560 0.10190  0.03380  0.02740  222 SER B CA  
4362 C C   . SER B  228 ? 0.22550 0.29460 0.39970 0.09920  0.02250  0.03450  222 SER B C   
4363 O O   . SER B  228 ? 0.27440 0.35040 0.44200 0.08950  0.01530  0.03610  222 SER B O   
4364 C CB  . SER B  228 ? 0.26260 0.31930 0.42820 0.09830  0.04160  0.01860  222 SER B CB  
4365 O OG  . SER B  228 ? 0.32410 0.37150 0.47100 0.08640  0.03680  0.01870  222 SER B OG  
4366 N N   . THR B  229 ? 0.28200 0.33530 0.45540 0.10790  0.02140  0.03860  223 THR B N   
4367 C CA  . THR B  229 ? 0.26870 0.31390 0.43020 0.10530  0.01230  0.04630  223 THR B CA  
4368 C C   . THR B  229 ? 0.27020 0.30240 0.40970 0.09300  0.01160  0.04120  223 THR B C   
4369 O O   . THR B  229 ? 0.22940 0.26480 0.35930 0.08740  0.00380  0.04490  223 THR B O   
4370 C CB  . THR B  229 ? 0.30180 0.32920 0.46620 0.11580  0.01300  0.05300  223 THR B CB  
4371 O OG1 . THR B  229 ? 0.34970 0.35330 0.50800 0.11580  0.02190  0.04460  223 THR B OG1 
4372 C CG2 . THR B  229 ? 0.26810 0.30920 0.45640 0.12980  0.01230  0.06020  223 THR B CG2 
4373 N N   . ARG B  230 ? 0.21990 0.23890 0.35120 0.08930  0.01960  0.03250  224 ARG B N   
4374 C CA  . ARG B  230 ? 0.22540 0.23340 0.33780 0.07890  0.01860  0.02860  224 ARG B CA  
4375 C C   . ARG B  230 ? 0.21550 0.23780 0.32620 0.06960  0.01530  0.02720  224 ARG B C   
4376 O O   . ARG B  230 ? 0.19280 0.21200 0.29250 0.06300  0.00980  0.02790  224 ARG B O   
4377 C CB  . ARG B  230 ? 0.26860 0.26150 0.37260 0.07730  0.02670  0.02000  224 ARG B CB  
4378 C CG  . ARG B  230 ? 0.23250 0.21860 0.31940 0.06700  0.02520  0.01700  224 ARG B CG  
4379 C CD  . ARG B  230 ? 0.27080 0.24060 0.34770 0.06570  0.03010  0.01020  224 ARG B CD  
4380 N NE  . ARG B  230 ? 0.31580 0.26990 0.39250 0.06900  0.02900  0.01230  224 ARG B NE  
4381 C CZ  . ARG B  230 ? 0.34660 0.28540 0.41770 0.06760  0.03220  0.00610  224 ARG B CZ  
4382 N NH1 . ARG B  230 ? 0.30210 0.24070 0.36560 0.06410  0.03620  -0.00300 224 ARG B NH1 
4383 N NH2 . ARG B  230 ? 0.34860 0.27290 0.42210 0.06940  0.03120  0.00970  224 ARG B NH2 
4384 N N   . CSO B  231 ? 0.23730 0.27500 0.36000 0.06930  0.01930  0.02520  225 CSO B N   
4385 C CA  . CSO B  231 ? 0.21340 0.26370 0.33810 0.05970  0.01650  0.02470  225 CSO B CA  
4386 C CB  . CSO B  231 ? 0.22710 0.29390 0.36640 0.05960  0.02390  0.02340  225 CSO B CB  
4387 S SG  . CSO B  231 ? 0.36630 0.41950 0.49010 0.05690  0.03450  0.01770  225 CSO B SG  
4388 C C   . CSO B  231 ? 0.20170 0.26370 0.33130 0.05780  0.00580  0.02870  225 CSO B C   
4389 O O   . CSO B  231 ? 0.21670 0.27850 0.33990 0.04910  0.00080  0.02670  225 CSO B O   
4390 O OD  . CSO B  231 ? 0.29820 0.36970 0.43390 0.05980  0.04670  0.01570  225 CSO B OD  
4391 N N   . ALA B  232 ? 0.19490 0.26670 0.33520 0.06660  0.00190  0.03390  226 ALA B N   
4392 C CA  . ALA B  232 ? 0.23480 0.32150 0.37850 0.06550  -0.00940 0.03790  226 ALA B CA  
4393 C C   . ALA B  232 ? 0.20360 0.27590 0.32620 0.06190  -0.01460 0.03790  226 ALA B C   
4394 O O   . ALA B  232 ? 0.19520 0.27500 0.31250 0.05540  -0.02240 0.03570  226 ALA B O   
4395 C CB  . ALA B  232 ? 0.21590 0.31590 0.37440 0.07750  -0.01260 0.04570  226 ALA B CB  
4396 N N   . ALA B  233 ? 0.22760 0.27980 0.33890 0.06600  -0.00980 0.03950  227 ALA B N   
4397 C CA  . ALA B  233 ? 0.19370 0.23390 0.28650 0.06290  -0.01310 0.04020  227 ALA B CA  
4398 C C   . ALA B  233 ? 0.24360 0.27620 0.32550 0.05270  -0.01200 0.03220  227 ALA B C   
4399 O O   . ALA B  233 ? 0.23890 0.27130 0.30950 0.04840  -0.01710 0.03040  227 ALA B O   
4400 C CB  . ALA B  233 ? 0.23660 0.25770 0.32350 0.06870  -0.00790 0.04440  227 ALA B CB  
4401 N N   . LEU B  234 ? 0.18800 0.21450 0.27260 0.04950  -0.00500 0.02760  228 LEU B N   
4402 C CA  . LEU B  234 ? 0.20200 0.22160 0.27850 0.04070  -0.00420 0.02200  228 LEU B CA  
4403 C C   . LEU B  234 ? 0.23640 0.26900 0.31950 0.03400  -0.01050 0.01900  228 LEU B C   
4404 O O   . LEU B  234 ? 0.17740 0.20430 0.25240 0.02800  -0.01350 0.01450  228 LEU B O   
4405 C CB  . LEU B  234 ? 0.19500 0.20880 0.27320 0.03910  0.00420  0.01970  228 LEU B CB  
4406 C CG  . LEU B  234 ? 0.24140 0.24040 0.31050 0.04300  0.00990  0.01890  228 LEU B CG  
4407 C CD1 . LEU B  234 ? 0.28660 0.28730 0.35890 0.04270  0.01760  0.01650  228 LEU B CD1 
4408 C CD2 . LEU B  234 ? 0.18620 0.17230 0.24080 0.03890  0.00830  0.01720  228 LEU B CD2 
4409 N N   . ALA B  235 ? 0.18520 0.23590 0.28470 0.03500  -0.01260 0.02080  229 ALA B N   
4410 C CA  . ALA B  235 ? 0.18190 0.24640 0.29050 0.02730  -0.01940 0.01700  229 ALA B CA  
4411 C C   . ALA B  235 ? 0.18430 0.25330 0.28320 0.02710  -0.02920 0.01490  229 ALA B C   
4412 O O   . ALA B  235 ? 0.18150 0.25150 0.27840 0.01920  -0.03430 0.00770  229 ALA B O   
4413 C CB  . ALA B  235 ? 0.18550 0.27210 0.31640 0.02840  -0.01970 0.01990  229 ALA B CB  
4414 N N   . HIS B  236 ? 0.17730 0.24870 0.27000 0.03570  -0.03150 0.02100  230 HIS B N   
4415 C CA  . HIS B  236 ? 0.19670 0.27430 0.27690 0.03650  -0.03990 0.02070  230 HIS B CA  
4416 C C   . HIS B  236 ? 0.23350 0.29390 0.29510 0.03240  -0.03790 0.01490  230 HIS B C   
4417 O O   . HIS B  236 ? 0.22710 0.29260 0.27980 0.02850  -0.04410 0.00830  230 HIS B O   
4418 C CB  . HIS B  236 ? 0.22160 0.30290 0.29990 0.04740  -0.04080 0.03200  230 HIS B CB  
4419 C CG  . HIS B  236 ? 0.23480 0.33040 0.30280 0.04980  -0.05040 0.03520  230 HIS B CG  
4420 N ND1 . HIS B  236 ? 0.27860 0.37880 0.34430 0.05960  -0.05220 0.04780  230 HIS B ND1 
4421 C CD2 . HIS B  236 ? 0.28810 0.39480 0.34680 0.04390  -0.05850 0.02750  230 HIS B CD2 
4422 C CE1 . HIS B  236 ? 0.30790 0.42370 0.36200 0.05980  -0.06130 0.04920  230 HIS B CE1 
4423 N NE2 . HIS B  236 ? 0.27300 0.39350 0.32200 0.05030  -0.06530 0.03570  230 HIS B NE2 
4424 N N   . ILE B  237 ? 0.20220 0.24370 0.25800 0.03380  -0.02940 0.01650  231 ILE B N   
4425 C CA  . ILE B  237 ? 0.22910 0.25620 0.27020 0.03090  -0.02690 0.01170  231 ILE B CA  
4426 C C   . ILE B  237 ? 0.20710 0.23150 0.25110 0.02250  -0.02830 0.00190  231 ILE B C   
4427 O O   . ILE B  237 ? 0.21390 0.23630 0.24840 0.01980  -0.03140 -0.00520 231 ILE B O   
4428 C CB  . ILE B  237 ? 0.24440 0.25470 0.28160 0.03360  -0.01840 0.01540  231 ILE B CB  
4429 C CG1 . ILE B  237 ? 0.24030 0.24940 0.27350 0.04090  -0.01730 0.02430  231 ILE B CG1 
4430 C CG2 . ILE B  237 ? 0.20070 0.19830 0.22680 0.03000  -0.01590 0.01000  231 ILE B CG2 
4431 C CD1 . ILE B  237 ? 0.26370 0.25820 0.29860 0.04340  -0.00960 0.02700  231 ILE B CD1 
4432 N N   . PHE B  238 ? 0.21070 0.23510 0.26880 0.01850  -0.02560 0.00150  232 PHE B N   
4433 C CA  . PHE B  238 ? 0.21970 0.24030 0.28400 0.00990  -0.02680 -0.00610 232 PHE B CA  
4434 C C   . PHE B  238 ? 0.24970 0.28310 0.31590 0.00550  -0.03630 -0.01420 232 PHE B C   
4435 O O   . PHE B  238 ? 0.19890 0.22520 0.25910 0.00150  -0.03870 -0.02350 232 PHE B O   
4436 C CB  . PHE B  238 ? 0.21090 0.23390 0.29170 0.00610  -0.02230 -0.00260 232 PHE B CB  
4437 C CG  . PHE B  238 ? 0.22460 0.24040 0.31370 -0.00320 -0.02200 -0.00760 232 PHE B CG  
4438 C CD1 . PHE B  238 ? 0.22840 0.25300 0.32820 -0.01060 -0.02910 -0.01500 232 PHE B CD1 
4439 C CD2 . PHE B  238 ? 0.21260 0.21310 0.30010 -0.00460 -0.01500 -0.00450 232 PHE B CD2 
4440 C CE1 . PHE B  238 ? 0.19920 0.21430 0.30920 -0.01980 -0.02860 -0.01960 232 PHE B CE1 
4441 C CE2 . PHE B  238 ? 0.18780 0.17950 0.28460 -0.01270 -0.01450 -0.00700 232 PHE B CE2 
4442 C CZ  . PHE B  238 ? 0.22400 0.22170 0.33300 -0.02060 -0.02090 -0.01460 232 PHE B CZ  
4443 N N   . ARG B  239 ? 0.19170 0.24510 0.26710 0.00670  -0.04190 -0.01150 233 ARG B N   
4444 C CA  A ARG B  239 ? 0.22350 0.29390 0.30050 0.00280  -0.05260 -0.01920 233 ARG B CA  
4445 C CA  B ARG B  239 ? 0.22360 0.29380 0.30060 0.00270  -0.05260 -0.01940 233 ARG B CA  
4446 C C   . ARG B  239 ? 0.21790 0.28600 0.27340 0.00530  -0.05640 -0.02510 233 ARG B C   
4447 O O   . ARG B  239 ? 0.23470 0.30390 0.28680 -0.00070 -0.06170 -0.03780 233 ARG B O   
4448 C CB  A ARG B  239 ? 0.22450 0.31830 0.31240 0.00740  -0.05760 -0.01160 233 ARG B CB  
4449 C CB  B ARG B  239 ? 0.22440 0.31870 0.31260 0.00680  -0.05810 -0.01230 233 ARG B CB  
4450 C CG  A ARG B  239 ? 0.29760 0.41540 0.38800 0.00480  -0.07020 -0.01710 233 ARG B CG  
4451 C CG  B ARG B  239 ? 0.29750 0.41340 0.38150 0.00610  -0.07050 -0.01740 233 ARG B CG  
4452 C CD  A ARG B  239 ? 0.25980 0.39990 0.36440 0.01170  -0.07340 -0.00620 233 ARG B CD  
4453 C CD  B ARG B  239 ? 0.27530 0.41150 0.36330 0.01580  -0.07460 -0.00520 233 ARG B CD  
4454 N NE  A ARG B  239 ? 0.26300 0.40170 0.38860 0.01000  -0.06580 -0.00190 233 ARG B NE  
4455 N NE  B ARG B  239 ? 0.27600 0.43900 0.36410 0.01470  -0.08800 -0.00870 233 ARG B NE  
4456 C CZ  A ARG B  239 ? 0.25240 0.39020 0.38440 0.01890  -0.05850 0.00860  233 ARG B CZ  
4457 C CZ  B ARG B  239 ? 0.33730 0.51930 0.42290 0.02390  -0.09410 0.00190  233 ARG B CZ  
4458 N NH1 A ARG B  239 ? 0.19120 0.32860 0.31380 0.03030  -0.05850 0.01760  233 ARG B NH1 
4459 N NH1 B ARG B  239 ? 0.28580 0.45930 0.36720 0.03500  -0.08770 0.01620  233 ARG B NH1 
4460 N NH2 A ARG B  239 ? 0.21240 0.34970 0.36130 0.01630  -0.05070 0.01020  233 ARG B NH2 
4461 N NH2 B ARG B  239 ? 0.37040 0.58050 0.45800 0.02190  -0.10750 -0.00200 233 ARG B NH2 
4462 N N   . ALA B  240 ? 0.21010 0.27570 0.25150 0.01400  -0.05320 -0.01640 234 ALA B N   
4463 C CA  . ALA B  240 ? 0.22050 0.28720 0.24120 0.01690  -0.05540 -0.01960 234 ALA B CA  
4464 C C   . ALA B  240 ? 0.22410 0.27350 0.23720 0.01290  -0.05130 -0.03090 234 ALA B C   
4465 O O   . ALA B  240 ? 0.23760 0.29150 0.24030 0.01070  -0.05570 -0.04240 234 ALA B O   
4466 C CB  . ALA B  240 ? 0.21750 0.28150 0.22800 0.02600  -0.05070 -0.00590 234 ALA B CB  
4467 N N   . MET B  241 ? 0.21410 0.24460 0.23200 0.01260  -0.04290 -0.02800 235 MET B N   
4468 C CA  . MET B  241 ? 0.21800 0.23220 0.23100 0.01030  -0.03890 -0.03690 235 MET B CA  
4469 C C   . MET B  241 ? 0.23070 0.24350 0.25310 0.00220  -0.04380 -0.05070 235 MET B C   
4470 O O   . MET B  241 ? 0.24110 0.24930 0.25570 0.00110  -0.04500 -0.06310 235 MET B O   
4471 C CB  . MET B  241 ? 0.20610 0.20350 0.22430 0.01160  -0.03030 -0.02970 235 MET B CB  
4472 C CG  . MET B  241 ? 0.19830 0.19430 0.20810 0.01840  -0.02530 -0.01880 235 MET B CG  
4473 S SD  . MET B  241 ? 0.23390 0.21290 0.24930 0.01870  -0.01690 -0.01320 235 MET B SD  
4474 C CE  . MET B  241 ? 0.19300 0.15980 0.20280 0.01830  -0.01440 -0.02120 235 MET B CE  
4475 N N   . ALA B  242 ? 0.22520 0.24210 0.26570 -0.00380 -0.04620 -0.04940 236 ALA B N   
4476 C CA  . ALA B  242 ? 0.23660 0.24960 0.28980 -0.01320 -0.05020 -0.06160 236 ALA B CA  
4477 C C   . ALA B  242 ? 0.25180 0.28150 0.30000 -0.01640 -0.06050 -0.07470 236 ALA B C   
4478 O O   . ALA B  242 ? 0.28050 0.30370 0.33170 -0.02270 -0.06380 -0.09000 236 ALA B O   
4479 C CB  . ALA B  242 ? 0.25960 0.27440 0.33500 -0.01950 -0.04900 -0.05510 236 ALA B CB  
4480 N N   . ARG B  243 ? 0.25050 0.30200 0.29130 -0.01190 -0.06600 -0.06920 237 ARG B N   
4481 C CA  . ARG B  243 ? 0.26720 0.33820 0.30130 -0.01480 -0.07700 -0.08120 237 ARG B CA  
4482 C C   . ARG B  243 ? 0.28030 0.35070 0.28930 -0.00960 -0.07670 -0.08950 237 ARG B C   
4483 O O   . ARG B  243 ? 0.29900 0.38060 0.30040 -0.01330 -0.08460 -0.10500 237 ARG B O   
4484 C CB  . ARG B  243 ? 0.26760 0.36520 0.30520 -0.01160 -0.08400 -0.07070 237 ARG B CB  
4485 C CG  . ARG B  243 ? 0.40060 0.51050 0.46350 -0.02070 -0.09040 -0.07390 237 ARG B CG  
4486 C CD  . ARG B  243 ? 0.40520 0.52120 0.48330 -0.01650 -0.08620 -0.05670 237 ARG B CD  
4487 N NE  . ARG B  243 ? 0.46950 0.61580 0.55840 -0.01590 -0.09600 -0.05280 237 ARG B NE  
4488 C CZ  . ARG B  243 ? 0.50510 0.67150 0.58030 -0.00840 -0.10370 -0.04850 237 ARG B CZ  
4489 N NH1 . ARG B  243 ? 0.42800 0.58910 0.47680 -0.00270 -0.10310 -0.04960 237 ARG B NH1 
4490 N NH2 . ARG B  243 ? 0.45160 0.64560 0.54060 -0.00630 -0.11190 -0.04180 237 ARG B NH2 
4491 N N   . HIS B  244 ? 0.22820 0.27450 0.25150 0.03450  -0.07130 0.02360  238 HIS B N   
4492 C CA  . HIS B  244 ? 0.25290 0.28570 0.25040 0.03700  -0.06860 0.02210  238 HIS B CA  
4493 C C   . HIS B  244 ? 0.25570 0.26420 0.24810 0.03420  -0.05740 0.01360  238 HIS B C   
4494 O O   . HIS B  244 ? 0.24220 0.23820 0.23000 0.04030  -0.04730 0.01840  238 HIS B O   
4495 C CB  . HIS B  244 ? 0.24960 0.28540 0.24400 0.04970  -0.06440 0.03730  238 HIS B CB  
4496 C CG  . HIS B  244 ? 0.26180 0.32450 0.26230 0.05470  -0.07530 0.04820  238 HIS B CG  
4497 N ND1 . HIS B  244 ? 0.29870 0.37670 0.28020 0.05320  -0.08740 0.04880  238 HIS B ND1 
4498 C CD2 . HIS B  244 ? 0.25220 0.33170 0.27610 0.06090  -0.07650 0.05870  238 HIS B CD2 
4499 C CE1 . HIS B  244 ? 0.28490 0.39020 0.27890 0.05840  -0.09650 0.06050  238 HIS B CE1 
4500 N NE2 . HIS B  244 ? 0.26770 0.37430 0.28840 0.06390  -0.08950 0.06720  238 HIS B NE2 
4501 N N   . PRO B  245 ? 0.23450 0.23670 0.22900 0.02470  -0.05880 0.00190  239 PRO B N   
4502 C CA  . PRO B  245 ? 0.21840 0.20110 0.21160 0.02340  -0.04830 -0.00410 239 PRO B CA  
4503 C C   . PRO B  245 ? 0.24950 0.21970 0.22040 0.02650  -0.04310 -0.00620 239 PRO B C   
4504 O O   . PRO B  245 ? 0.27940 0.23770 0.25110 0.02860  -0.03310 -0.00630 239 PRO B O   
4505 C CB  . PRO B  245 ? 0.28170 0.26170 0.28020 0.01330  -0.05220 -0.01460 239 PRO B CB  
4506 C CG  . PRO B  245 ? 0.24630 0.23910 0.23830 0.00730  -0.06520 -0.01790 239 PRO B CG  
4507 C CD  . PRO B  245 ? 0.24680 0.25970 0.24580 0.01450  -0.06990 -0.00560 239 PRO B CD  
4508 N N   . GLU B  246 ? 0.26990 0.24450 0.22080 0.02690  -0.04970 -0.00730 240 GLU B N   
4509 C CA  . GLU B  246 ? 0.29480 0.25790 0.22260 0.03090  -0.04340 -0.00900 240 GLU B CA  
4510 C C   . GLU B  246 ? 0.27060 0.23390 0.19890 0.04000  -0.03490 0.00400  240 GLU B C   
4511 O O   . GLU B  246 ? 0.28140 0.23470 0.19860 0.04350  -0.02540 0.00470  240 GLU B O   
4512 C CB  . GLU B  246 ? 0.34910 0.31590 0.25150 0.02820  -0.05270 -0.01560 240 GLU B CB  
4513 C CG  . GLU B  246 ? 0.38240 0.36920 0.27900 0.03230  -0.06220 -0.00550 240 GLU B CG  
4514 C CD  . GLU B  246 ? 0.39610 0.40250 0.31730 0.02960  -0.07200 0.00000  240 GLU B CD  
4515 O OE1 . GLU B  246 ? 0.41510 0.42180 0.35110 0.02060  -0.07590 -0.00820 240 GLU B OE1 
4516 O OE2 . GLU B  246 ? 0.42820 0.45020 0.35420 0.03730  -0.07490 0.01370  240 GLU B OE2 
4517 N N   . MET B  247 ? 0.28740 0.26120 0.22990 0.04420  -0.03690 0.01510  241 MET B N   
4518 C CA  . MET B  247 ? 0.25920 0.22800 0.20550 0.05170  -0.02690 0.02710  241 MET B CA  
4519 C C   . MET B  247 ? 0.25140 0.20820 0.21330 0.04910  -0.01660 0.02470  241 MET B C   
4520 O O   . MET B  247 ? 0.29110 0.23970 0.25220 0.05170  -0.00670 0.03040  241 MET B O   
4521 C CB  . MET B  247 ? 0.26070 0.24040 0.21800 0.05820  -0.03000 0.04000  241 MET B CB  
4522 C CG  . MET B  247 ? 0.28590 0.28200 0.22770 0.06300  -0.04010 0.04710  241 MET B CG  
4523 S SD  . MET B  247 ? 0.31250 0.30110 0.22690 0.06920  -0.03260 0.05420  241 MET B SD  
4524 C CE  . MET B  247 ? 0.32930 0.31650 0.21710 0.06170  -0.03880 0.03700  241 MET B CE  
4525 N N   . VAL B  248 ? 0.22920 0.18640 0.20600 0.04350  -0.01910 0.01730  242 VAL B N   
4526 C CA  . VAL B  248 ? 0.21450 0.16340 0.20550 0.04080  -0.01090 0.01510  242 VAL B CA  
4527 C C   . VAL B  248 ? 0.26100 0.20210 0.24450 0.03840  -0.00480 0.00960  242 VAL B C   
4528 O O   . VAL B  248 ? 0.25710 0.19350 0.24900 0.03710  0.00290  0.01090  242 VAL B O   
4529 C CB  . VAL B  248 ? 0.19380 0.14710 0.20080 0.03650  -0.01490 0.00980  242 VAL B CB  
4530 C CG1 . VAL B  248 ? 0.21560 0.16170 0.23390 0.03350  -0.00730 0.00700  242 VAL B CG1 
4531 C CG2 . VAL B  248 ? 0.21130 0.17400 0.22850 0.04070  -0.01870 0.01690  242 VAL B CG2 
4532 N N   . ALA B  249 ? 0.23540 0.17530 0.20330 0.03760  -0.00790 0.00320  243 ALA B N   
4533 C CA  . ALA B  249 ? 0.26450 0.19730 0.22480 0.03810  -0.00050 -0.00050 243 ALA B CA  
4534 C C   . ALA B  249 ? 0.29190 0.22210 0.22770 0.04170  -0.00080 -0.00240 243 ALA B C   
4535 O O   . ALA B  249 ? 0.28240 0.21320 0.20880 0.04660  0.00500  0.00490  243 ALA B O   
4536 C CB  . ALA B  249 ? 0.21460 0.14370 0.18270 0.03370  -0.00120 -0.00910 243 ALA B CB  
4537 N N   . GLY B  250 ? 0.25830 0.18510 0.18250 0.03880  -0.00720 -0.01230 244 GLY B N   
4538 C CA  . GLY B  250 ? 0.29460 0.21760 0.19190 0.04140  -0.00790 -0.01640 244 GLY B CA  
4539 C C   . GLY B  250 ? 0.29550 0.20670 0.18280 0.03720  -0.00990 -0.03030 244 GLY B C   
4540 O O   . GLY B  250 ? 0.29530 0.20280 0.19810 0.03240  -0.01120 -0.03460 244 GLY B O   
4541 N N   . GLU B  251 ? 0.32430 0.22790 0.18400 0.03950  -0.00890 -0.03700 245 GLU B N   
4542 C CA  . GLU B  251 ? 0.38640 0.27420 0.23280 0.03480  -0.01060 -0.05190 245 GLU B CA  
4543 C C   . GLU B  251 ? 0.34800 0.22300 0.20500 0.03800  0.00110  -0.05390 245 GLU B C   
4544 O O   . GLU B  251 ? 0.32970 0.20590 0.18980 0.04600  0.01260  -0.04690 245 GLU B O   
4545 C CB  . GLU B  251 ? 0.45790 0.33790 0.26890 0.03720  -0.01040 -0.06000 245 GLU B CB  
4546 C CG  . GLU B  251 ? 0.57750 0.47160 0.37470 0.03200  -0.02570 -0.06070 245 GLU B CG  
4547 C CD  . GLU B  251 ? 0.60410 0.50430 0.41580 0.01960  -0.04050 -0.06680 245 GLU B CD  
4548 O OE1 . GLU B  251 ? 0.71950 0.60340 0.52840 0.01200  -0.04140 -0.08020 245 GLU B OE1 
4549 O OE2 . GLU B  251 ? 0.48690 0.40770 0.31360 0.01780  -0.05000 -0.05740 245 GLU B OE2 
4550 N N   . GLY B  252 ? 0.37470 0.23850 0.23840 0.03160  -0.00170 -0.06250 246 GLY B N   
4551 C CA  . GLY B  252 ? 0.33060 0.18280 0.20460 0.03560  0.00890  -0.06290 246 GLY B CA  
4552 C C   . GLY B  252 ? 0.31510 0.18030 0.21790 0.03700  0.01160  -0.05180 246 GLY B C   
4553 O O   . GLY B  252 ? 0.33340 0.19200 0.24650 0.03990  0.01870  -0.05100 246 GLY B O   
4554 N N   . ARG B  253 ? 0.27650 0.15910 0.19150 0.03550  0.00680  -0.04310 247 ARG B N   
4555 C CA  . ARG B  253 ? 0.24890 0.14240 0.18790 0.03580  0.00960  -0.03430 247 ARG B CA  
4556 C C   . ARG B  253 ? 0.28270 0.17750 0.23810 0.02900  0.00330  -0.03600 247 ARG B C   
4557 O O   . ARG B  253 ? 0.27990 0.17560 0.23420 0.02270  -0.00580 -0.04000 247 ARG B O   
4558 C CB  . ARG B  253 ? 0.27940 0.18640 0.22380 0.03660  0.00820  -0.02530 247 ARG B CB  
4559 C CG  . ARG B  253 ? 0.30920 0.21700 0.23990 0.04320  0.01560  -0.02070 247 ARG B CG  
4560 C CD  . ARG B  253 ? 0.30520 0.21780 0.24900 0.04680  0.02620  -0.01440 247 ARG B CD  
4561 N NE  . ARG B  253 ? 0.27590 0.19810 0.24160 0.04220  0.02420  -0.00880 247 ARG B NE  
4562 C CZ  . ARG B  253 ? 0.25690 0.18480 0.22800 0.04070  0.02390  -0.00200 247 ARG B CZ  
4563 N NH1 . ARG B  253 ? 0.27410 0.20150 0.23190 0.04400  0.02550  0.00250  247 ARG B NH1 
4564 N NH2 . ARG B  253 ? 0.23440 0.16730 0.22330 0.03590  0.02250  0.00040  247 ARG B NH2 
4565 N N   . TYR B  254 ? 0.21830 0.11690 0.19010 0.03010  0.00810  -0.03160 248 TYR B N   
4566 C CA  . TYR B  254 ? 0.26780 0.16810 0.25420 0.02470  0.00400  -0.03180 248 TYR B CA  
4567 C C   . TYR B  254 ? 0.28100 0.19170 0.27530 0.01930  -0.00440 -0.03050 248 TYR B C   
4568 O O   . TYR B  254 ? 0.26380 0.17340 0.26170 0.01330  -0.01030 -0.03400 248 TYR B O   
4569 C CB  . TYR B  254 ? 0.24090 0.14860 0.24220 0.02730  0.00950  -0.02560 248 TYR B CB  
4570 C CG  . TYR B  254 ? 0.26660 0.17490 0.27980 0.02310  0.00720  -0.02520 248 TYR B CG  
4571 C CD1 . TYR B  254 ? 0.25090 0.14620 0.26230 0.02350  0.01000  -0.02770 248 TYR B CD1 
4572 C CD2 . TYR B  254 ? 0.23280 0.15300 0.25840 0.01920  0.00350  -0.02210 248 TYR B CD2 
4573 C CE1 . TYR B  254 ? 0.25170 0.14710 0.27390 0.01980  0.00900  -0.02560 248 TYR B CE1 
4574 C CE2 . TYR B  254 ? 0.23080 0.15260 0.26610 0.01590  0.00250  -0.02090 248 TYR B CE2 
4575 C CZ  . TYR B  254 ? 0.22330 0.13360 0.25740 0.01610  0.00530  -0.02190 248 TYR B CZ  
4576 O OH  . TYR B  254 ? 0.23820 0.14970 0.28190 0.01310  0.00550  -0.01890 248 TYR B OH  
4577 N N   . CYS B  255 ? 0.23780 0.15870 0.23700 0.02130  -0.00400 -0.02450 249 CYS B N   
4578 C CA  . CYS B  255 ? 0.25820 0.18840 0.26670 0.01840  -0.01010 -0.02190 249 CYS B CA  
4579 C C   . CYS B  255 ? 0.28670 0.21840 0.28750 0.01530  -0.01870 -0.02540 249 CYS B C   
4580 O O   . CYS B  255 ? 0.23250 0.17180 0.24370 0.01110  -0.02450 -0.02530 249 CYS B O   
4581 C CB  . CYS B  255 ? 0.23500 0.17080 0.24640 0.02190  -0.00730 -0.01540 249 CYS B CB  
4582 S SG  . CYS B  255 ? 0.28600 0.22220 0.30510 0.02290  0.00160  -0.01230 249 CYS B SG  
4583 N N   . THR B  256 ? 0.26970 0.19660 0.25230 0.01740  -0.01960 -0.02790 250 THR B N   
4584 C CA  . THR B  256 ? 0.24650 0.17700 0.21870 0.01370  -0.02930 -0.03170 250 THR B CA  
4585 C C   . THR B  256 ? 0.31390 0.23780 0.28670 0.00520  -0.03400 -0.04070 250 THR B C   
4586 O O   . THR B  256 ? 0.29290 0.22680 0.27260 -0.00150 -0.04330 -0.04190 250 THR B O   
4587 C CB  . THR B  256 ? 0.24490 0.17030 0.19330 0.01820  -0.02790 -0.03320 250 THR B CB  
4588 O OG1 . THR B  256 ? 0.29870 0.23080 0.24830 0.02510  -0.02360 -0.02310 250 THR B OG1 
4589 C CG2 . THR B  256 ? 0.26490 0.19500 0.19910 0.01320  -0.03920 -0.03880 250 THR B CG2 
4590 N N   . MET B  257 ? 0.29880 0.20580 0.26520 0.00530  -0.02730 -0.04650 251 MET B N   
4591 C CA  . MET B  257 ? 0.29850 0.19410 0.26490 -0.00290 -0.03000 -0.05480 251 MET B CA  
4592 C C   . MET B  257 ? 0.30930 0.21350 0.29940 -0.00810 -0.03160 -0.05050 251 MET B C   
4593 O O   . MET B  257 ? 0.30340 0.20990 0.29950 -0.01770 -0.03860 -0.05430 251 MET B O   
4594 C CB  . MET B  257 ? 0.26720 0.14090 0.22210 0.00120  -0.02000 -0.06000 251 MET B CB  
4595 C CG  . MET B  257 ? 0.30240 0.16770 0.23200 0.00660  -0.01730 -0.06500 251 MET B CG  
4596 S SD  . MET B  257 ? 0.40200 0.24150 0.31830 0.01430  -0.00310 -0.07040 251 MET B SD  
4597 C CE  . MET B  257 ? 0.44760 0.26470 0.36130 0.00290  -0.00660 -0.08240 251 MET B CE  
4598 N N   . LEU B  258 ? 0.28100 0.19170 0.28450 -0.00250 -0.02550 -0.04250 252 LEU B N   
4599 C CA  . LEU B  258 ? 0.24180 0.16190 0.26540 -0.00600 -0.02580 -0.03780 252 LEU B CA  
4600 C C   . LEU B  258 ? 0.29230 0.23050 0.32610 -0.01000 -0.03440 -0.03520 252 LEU B C   
4601 O O   . LEU B  258 ? 0.27860 0.22260 0.32410 -0.01780 -0.03870 -0.03590 252 LEU B O   
4602 C CB  . LEU B  258 ? 0.23980 0.16450 0.27130 0.00090  -0.01830 -0.03110 252 LEU B CB  
4603 C CG  . LEU B  258 ? 0.24330 0.18050 0.29240 -0.00070 -0.01810 -0.02590 252 LEU B CG  
4604 C CD1 . LEU B  258 ? 0.22230 0.15310 0.27790 -0.00450 -0.01490 -0.02580 252 LEU B CD1 
4605 C CD2 . LEU B  258 ? 0.25780 0.20180 0.31080 0.00510  -0.01320 -0.02100 252 LEU B CD2 
4606 N N   . MET B  259 ? 0.24200 0.19000 0.27220 -0.00460 -0.03670 -0.03130 253 MET B N   
4607 C CA  . MET B  259 ? 0.22370 0.19090 0.26570 -0.00590 -0.04390 -0.02650 253 MET B CA  
4608 C C   . MET B  259 ? 0.26480 0.23820 0.30190 -0.01430 -0.05500 -0.03160 253 MET B C   
4609 O O   . MET B  259 ? 0.27930 0.26960 0.33210 -0.01960 -0.06140 -0.02900 253 MET B O   
4610 C CB  . MET B  259 ? 0.22580 0.19990 0.26620 0.00330  -0.04210 -0.01920 253 MET B CB  
4611 C CG  . MET B  259 ? 0.20900 0.18150 0.26010 0.00840  -0.03310 -0.01460 253 MET B CG  
4612 S SD  . MET B  259 ? 0.21470 0.19210 0.26670 0.01780  -0.03020 -0.00600 253 MET B SD  
4613 C CE  . MET B  259 ? 0.19870 0.16340 0.22920 0.02070  -0.02740 -0.00740 253 MET B CE  
4614 N N   . ARG B  260 ? 0.31640 0.27710 0.33210 -0.01640 -0.05740 -0.03950 254 ARG B N   
4615 C CA  . ARG B  260 ? 0.29750 0.26210 0.30620 -0.02700 -0.06860 -0.04710 254 ARG B CA  
4616 C C   . ARG B  260 ? 0.31630 0.27570 0.33810 -0.03880 -0.06960 -0.05220 254 ARG B C   
4617 O O   . ARG B  260 ? 0.28570 0.26170 0.32000 -0.04860 -0.07910 -0.05230 254 ARG B O   
4618 C CB  . ARG B  260 ? 0.36150 0.30920 0.34100 -0.02690 -0.06910 -0.05670 254 ARG B CB  
4619 C CG  . ARG B  260 ? 0.41300 0.37260 0.37790 -0.01990 -0.07370 -0.05230 254 ARG B CG  
4620 C CD  . ARG B  260 ? 0.51900 0.46650 0.45310 -0.02300 -0.07750 -0.06350 254 ARG B CD  
4621 N NE  . ARG B  260 ? 0.59420 0.55490 0.51380 -0.01490 -0.08100 -0.05680 254 ARG B NE  
4622 C CZ  . ARG B  260 ? 0.54390 0.49350 0.44060 -0.00640 -0.07380 -0.05700 254 ARG B CZ  
4623 N NH1 . ARG B  260 ? 0.50370 0.42900 0.38770 -0.00450 -0.06320 -0.06500 254 ARG B NH1 
4624 N NH2 . ARG B  260 ? 0.55560 0.51960 0.44240 0.00110  -0.07680 -0.04780 254 ARG B NH2 
4625 N N   . ALA B  261 ? 0.35250 0.29060 0.37330 -0.03780 -0.05940 -0.05480 255 ALA B N   
4626 C CA  . ALA B  261 ? 0.32870 0.25760 0.36090 -0.04810 -0.05800 -0.05810 255 ALA B CA  
4627 C C   . ALA B  261 ? 0.29530 0.24730 0.35450 -0.05230 -0.06080 -0.04970 255 ALA B C   
4628 O O   . ALA B  261 ? 0.29860 0.25550 0.36930 -0.06530 -0.06630 -0.05220 255 ALA B O   
4629 C CB  . ALA B  261 ? 0.32790 0.23530 0.35770 -0.04170 -0.04500 -0.05700 255 ALA B CB  
4630 N N   . PHE B  262 ? 0.25470 0.22080 0.32440 -0.04200 -0.05630 -0.03980 256 PHE B N   
4631 C CA  . PHE B  262 ? 0.29050 0.27670 0.38480 -0.04310 -0.05560 -0.03130 256 PHE B CA  
4632 C C   . PHE B  262 ? 0.30250 0.31650 0.40800 -0.04410 -0.06540 -0.02670 256 PHE B C   
4633 O O   . PHE B  262 ? 0.27220 0.30560 0.40000 -0.04580 -0.06520 -0.01970 256 PHE B O   
4634 C CB  . PHE B  262 ? 0.25340 0.23910 0.35220 -0.03170 -0.04490 -0.02420 256 PHE B CB  
4635 C CG  . PHE B  262 ? 0.23820 0.20800 0.33720 -0.03240 -0.03590 -0.02430 256 PHE B CG  
4636 C CD1 . PHE B  262 ? 0.25250 0.22910 0.36860 -0.03710 -0.03230 -0.01940 256 PHE B CD1 
4637 C CD2 . PHE B  262 ? 0.23620 0.18630 0.31920 -0.02740 -0.03040 -0.02770 256 PHE B CD2 
4638 C CE1 . PHE B  262 ? 0.29770 0.25990 0.41290 -0.03680 -0.02370 -0.01760 256 PHE B CE1 
4639 C CE2 . PHE B  262 ? 0.25960 0.19670 0.34330 -0.02670 -0.02230 -0.02600 256 PHE B CE2 
4640 C CZ  . PHE B  262 ? 0.29390 0.23680 0.39290 -0.03110 -0.01920 -0.02060 256 PHE B CZ  
4641 N N   . ASP B  263 ? 0.27010 0.28790 0.36110 -0.04210 -0.07320 -0.02920 257 ASP B N   
4642 C CA  . ASP B  263 ? 0.25450 0.30000 0.35440 -0.04580 -0.08560 -0.02570 257 ASP B CA  
4643 C C   . ASP B  263 ? 0.27470 0.34550 0.39930 -0.03760 -0.08300 -0.01270 257 ASP B C   
4644 O O   . ASP B  263 ? 0.27570 0.37190 0.42110 -0.04370 -0.08950 -0.00800 257 ASP B O   
4645 C CB  . ASP B  263 ? 0.27180 0.32150 0.37660 -0.06370 -0.09540 -0.03340 257 ASP B CB  
4646 C CG  . ASP B  263 ? 0.32160 0.39970 0.42900 -0.06930 -0.11120 -0.03230 257 ASP B CG  
4647 O OD1 . ASP B  263 ? 0.37700 0.46330 0.47190 -0.05900 -0.11480 -0.02830 257 ASP B OD1 
4648 O OD2 . ASP B  263 ? 0.35120 0.44490 0.47390 -0.08420 -0.11990 -0.03450 257 ASP B OD2 
4649 N N   . GLY B  264 ? 0.23760 0.30140 0.36030 -0.02400 -0.07280 -0.00710 258 GLY B N   
4650 C CA  . GLY B  264 ? 0.25740 0.33910 0.39890 -0.01410 -0.06790 0.00390  258 GLY B CA  
4651 C C   . GLY B  264 ? 0.22850 0.30620 0.38340 -0.01260 -0.05650 0.00600  258 GLY B C   
4652 O O   . GLY B  264 ? 0.24560 0.33300 0.41240 -0.00260 -0.04970 0.01360  258 GLY B O   
4653 N N   . ALA B  265 ? 0.22370 0.28660 0.37570 -0.02140 -0.05330 -0.00020 259 ALA B N   
4654 C CA  . ALA B  265 ? 0.19980 0.26120 0.36320 -0.02050 -0.04290 0.00280  259 ALA B CA  
4655 C C   . ALA B  265 ? 0.22350 0.26920 0.37570 -0.00990 -0.03230 0.00270  259 ALA B C   
4656 O O   . ALA B  265 ? 0.21380 0.26230 0.37410 -0.00620 -0.02350 0.00620  259 ALA B O   
4657 C CB  . ALA B  265 ? 0.23440 0.28420 0.39780 -0.03250 -0.04250 -0.00200 259 ALA B CB  
4658 N N   . LEU B  266 ? 0.18860 0.21880 0.32210 -0.00590 -0.03290 -0.00150 260 LEU B N   
4659 C CA  . LEU B  266 ? 0.17450 0.19160 0.29850 0.00190  -0.02410 -0.00200 260 LEU B CA  
4660 C C   . LEU B  266 ? 0.21510 0.22350 0.32430 0.00670  -0.02640 -0.00340 260 LEU B C   
4661 O O   . LEU B  266 ? 0.22590 0.23550 0.32810 0.00380  -0.03420 -0.00510 260 LEU B O   
4662 C CB  . LEU B  266 ? 0.16380 0.16700 0.28120 -0.00190 -0.01900 -0.00580 260 LEU B CB  
4663 C CG  . LEU B  266 ? 0.17290 0.16290 0.27990 -0.00860 -0.02280 -0.01120 260 LEU B CG  
4664 C CD1 . LEU B  266 ? 0.18850 0.16630 0.27810 -0.00460 -0.02370 -0.01490 260 LEU B CD1 
4665 C CD2 . LEU B  266 ? 0.15400 0.13480 0.26120 -0.01130 -0.01670 -0.01110 260 LEU B CD2 
4666 N N   . VAL B  267 ? 0.16850 0.16820 0.27220 0.01350  -0.01920 -0.00270 261 VAL B N   
4667 C CA  . VAL B  267 ? 0.19960 0.18770 0.28870 0.01660  -0.01880 -0.00400 261 VAL B CA  
4668 C C   . VAL B  267 ? 0.19260 0.16800 0.27370 0.01520  -0.01290 -0.00810 261 VAL B C   
4669 O O   . VAL B  267 ? 0.18280 0.15820 0.26850 0.01440  -0.00800 -0.00900 261 VAL B O   
4670 C CB  . VAL B  267 ? 0.18530 0.17400 0.27540 0.02490  -0.01590 0.00170  261 VAL B CB  
4671 C CG1 . VAL B  267 ? 0.19050 0.19490 0.28730 0.02770  -0.02330 0.00780  261 VAL B CG1 
4672 C CG2 . VAL B  267 ? 0.22280 0.20850 0.32020 0.02880  -0.00700 0.00220  261 VAL B CG2 
4673 N N   . GLY B  268 ? 0.19050 0.15710 0.25930 0.01550  -0.01320 -0.00990 262 GLY B N   
4674 C CA  . GLY B  268 ? 0.21990 0.17850 0.28300 0.01460  -0.00820 -0.01240 262 GLY B CA  
4675 C C   . GLY B  268 ? 0.20770 0.16030 0.26210 0.01740  -0.00570 -0.01120 262 GLY B C   
4676 O O   . GLY B  268 ? 0.19580 0.14780 0.24380 0.01980  -0.00850 -0.00920 262 GLY B O   
4677 N N   . LYS B  269 ? 0.15370 0.10340 0.20790 0.01670  -0.00060 -0.01180 263 LYS B N   
4678 C CA  . LYS B  269 ? 0.18570 0.13090 0.23480 0.01810  0.00300  -0.00970 263 LYS B CA  
4679 C C   . LYS B  269 ? 0.21170 0.15800 0.26110 0.01540  0.00680  -0.01090 263 LYS B C   
4680 O O   . LYS B  269 ? 0.19960 0.14980 0.25430 0.01250  0.00780  -0.01290 263 LYS B O   
4681 C CB  . LYS B  269 ? 0.18620 0.12790 0.23940 0.01970  0.00600  -0.00720 263 LYS B CB  
4682 C CG  . LYS B  269 ? 0.25530 0.19050 0.30470 0.02000  0.01060  -0.00390 263 LYS B CG  
4683 C CD  . LYS B  269 ? 0.28430 0.21850 0.32500 0.02450  0.00890  0.00130  263 LYS B CD  
4684 C CE  . LYS B  269 ? 0.28860 0.21690 0.32600 0.02420  0.01530  0.00590  263 LYS B CE  
4685 N NZ  . LYS B  269 ? 0.25800 0.19070 0.29260 0.02150  0.01670  0.00350  263 LYS B NZ  
4686 N N   . LEU B  270 ? 0.19230 0.13730 0.23600 0.01680  0.00890  -0.00890 264 LEU B N   
4687 C CA  . LEU B  270 ? 0.20100 0.15110 0.24720 0.01510  0.01270  -0.00810 264 LEU B CA  
4688 C C   . LEU B  270 ? 0.15890 0.10970 0.21040 0.01060  0.01620  -0.00690 264 LEU B C   
4689 O O   . LEU B  270 ? 0.19320 0.13680 0.24260 0.01120  0.01820  -0.00440 264 LEU B O   
4690 C CB  . LEU B  270 ? 0.15780 0.10660 0.19610 0.01940  0.01520  -0.00590 264 LEU B CB  
4691 C CG  . LEU B  270 ? 0.14670 0.10350 0.18930 0.01930  0.02050  -0.00270 264 LEU B CG  
4692 C CD1 . LEU B  270 ? 0.17220 0.13680 0.22080 0.01960  0.01980  -0.00330 264 LEU B CD1 
4693 C CD2 . LEU B  270 ? 0.23410 0.18740 0.26640 0.02520  0.02490  -0.00010 264 LEU B CD2 
4694 N N   . GLY B  271 ? 0.18980 0.14950 0.24780 0.00580  0.01700  -0.00800 265 GLY B N   
4695 C CA  . GLY B  271 ? 0.23160 0.19340 0.29480 -0.00080 0.02030  -0.00730 265 GLY B CA  
4696 C C   . GLY B  271 ? 0.19840 0.17390 0.26650 -0.00140 0.02250  -0.00310 265 GLY B C   
4697 O O   . GLY B  271 ? 0.19160 0.17750 0.26160 0.00150  0.02080  -0.00240 265 GLY B O   
4698 N N   . ALA B  272 ? 0.18850 0.16470 0.26000 -0.00460 0.02710  0.00090  266 ALA B N   
4699 C CA  . ALA B  272 ? 0.18150 0.17410 0.26060 -0.00480 0.03030  0.00620  266 ALA B CA  
4700 C C   . ALA B  272 ? 0.18360 0.19450 0.27240 -0.01050 0.02630  0.00450  266 ALA B C   
4701 O O   . ALA B  272 ? 0.18830 0.19820 0.27790 -0.01800 0.02220  -0.00150 266 ALA B O   
4702 C CB  . ALA B  272 ? 0.23660 0.22890 0.32080 -0.01010 0.03640  0.01120  266 ALA B CB  
4703 N N   . ASP B  273 ? 0.20790 0.23640 0.30330 -0.00590 0.02800  0.01030  267 ASP B N   
4704 C CA  . ASP B  273 ? 0.17070 0.22190 0.27610 -0.00820 0.02400  0.01190  267 ASP B CA  
4705 C C   . ASP B  273 ? 0.14440 0.19230 0.24330 -0.00450 0.01870  0.00820  267 ASP B C   
4706 O O   . ASP B  273 ? 0.15860 0.22050 0.26140 -0.00980 0.01350  0.00680  267 ASP B O   
4707 C CB  . ASP B  273 ? 0.14050 0.20610 0.25680 -0.02260 0.02120  0.01020  267 ASP B CB  
4708 C CG  . ASP B  273 ? 0.19650 0.27670 0.32560 -0.02540 0.02670  0.01780  267 ASP B CG  
4709 O OD1 . ASP B  273 ? 0.18200 0.28100 0.31910 -0.01730 0.02940  0.02590  267 ASP B OD1 
4710 O OD2 . ASP B  273 ? 0.22410 0.29640 0.35590 -0.03460 0.02980  0.01680  267 ASP B OD2 
4711 N N   . ALA B  274 ? 0.13660 0.16650 0.22500 0.00420  0.02020  0.00700  268 ALA B N   
4712 C CA  . ALA B  274 ? 0.20170 0.22730 0.28510 0.00980  0.01760  0.00600  268 ALA B CA  
4713 C C   . ALA B  274 ? 0.19760 0.21980 0.27780 0.00350  0.01260  0.00000  268 ALA B C   
4714 O O   . ALA B  274 ? 0.18060 0.21320 0.26200 0.00350  0.00960  0.00110  268 ALA B O   
4715 C CB  . ALA B  274 ? 0.17890 0.22190 0.26940 0.01620  0.01840  0.01330  268 ALA B CB  
4716 N N   . SER B  275 ? 0.18990 0.19730 0.26520 -0.00040 0.01260  -0.00540 269 SER B N   
4717 C CA  . SER B  275 ? 0.20320 0.20270 0.27390 -0.00240 0.01020  -0.01080 269 SER B CA  
4718 C C   . SER B  275 ? 0.18310 0.16740 0.24850 0.00340  0.01080  -0.01120 269 SER B C   
4719 O O   . SER B  275 ? 0.18610 0.16360 0.24910 0.00680  0.01270  -0.00930 269 SER B O   
4720 C CB  . SER B  275 ? 0.19100 0.18560 0.26120 -0.01100 0.01040  -0.01670 269 SER B CB  
4721 O OG  . SER B  275 ? 0.23770 0.24860 0.31170 -0.01850 0.00790  -0.01810 269 SER B OG  
4722 N N   . TYR B  276 ? 0.17090 0.15200 0.23460 0.00420  0.00910  -0.01330 270 TYR B N   
4723 C CA  . TYR B  276 ? 0.20460 0.17510 0.26580 0.00780  0.00840  -0.01370 270 TYR B CA  
4724 C C   . TYR B  276 ? 0.21310 0.18200 0.27530 0.00630  0.00800  -0.01670 270 TYR B C   
4725 O O   . TYR B  276 ? 0.18370 0.15940 0.24620 0.00420  0.00830  -0.01780 270 TYR B O   
4726 C CB  . TYR B  276 ? 0.15050 0.11960 0.21080 0.01180  0.00780  -0.01120 270 TYR B CB  
4727 C CG  . TYR B  276 ? 0.21740 0.17620 0.27350 0.01370  0.00640  -0.01250 270 TYR B CG  
4728 C CD1 . TYR B  276 ? 0.18380 0.13800 0.23420 0.01620  0.00770  -0.01200 270 TYR B CD1 
4729 C CD2 . TYR B  276 ? 0.18820 0.14410 0.24610 0.01260  0.00360  -0.01390 270 TYR B CD2 
4730 C CE1 . TYR B  276 ? 0.21600 0.16230 0.25960 0.01750  0.00540  -0.01370 270 TYR B CE1 
4731 C CE2 . TYR B  276 ? 0.22330 0.17340 0.27740 0.01310  0.00060  -0.01520 270 TYR B CE2 
4732 C CZ  . TYR B  276 ? 0.25550 0.20050 0.30110 0.01550  0.00100  -0.01550 270 TYR B CZ  
4733 O OH  . TYR B  276 ? 0.25620 0.19720 0.29540 0.01570  -0.00310 -0.01710 270 TYR B OH  
4734 N N   . ALA B  277 ? 0.19330 0.15490 0.25580 0.00820  0.00770  -0.01710 271 ALA B N   
4735 C CA  . ALA B  277 ? 0.21710 0.17850 0.28270 0.00880  0.00870  -0.01860 271 ALA B CA  
4736 C C   . ALA B  277 ? 0.18750 0.14890 0.25680 0.01150  0.00590  -0.01620 271 ALA B C   
4737 O O   . ALA B  277 ? 0.17210 0.13020 0.23930 0.01290  0.00320  -0.01470 271 ALA B O   
4738 C CB  . ALA B  277 ? 0.21010 0.16430 0.27480 0.00850  0.01230  -0.02110 271 ALA B CB  
4739 N N   . ILE B  278 ? 0.19740 0.16430 0.27210 0.01150  0.00640  -0.01560 272 ILE B N   
4740 C CA  . ILE B  278 ? 0.19020 0.16090 0.27180 0.01200  0.00320  -0.01310 272 ILE B CA  
4741 C C   . ILE B  278 ? 0.17090 0.14820 0.26050 0.01420  0.00660  -0.01180 272 ILE B C   
4742 O O   . ILE B  278 ? 0.20110 0.18070 0.28990 0.01410  0.01120  -0.01290 272 ILE B O   
4743 C CB  . ILE B  278 ? 0.16520 0.13680 0.24780 0.00860  0.00110  -0.01200 272 ILE B CB  
4744 C CG1 . ILE B  278 ? 0.20840 0.17200 0.28270 0.00840  -0.00090 -0.01340 272 ILE B CG1 
4745 C CG2 . ILE B  278 ? 0.15960 0.13680 0.25150 0.00640  -0.00220 -0.01010 272 ILE B CG2 
4746 C CD1 . ILE B  278 ? 0.19520 0.15450 0.26900 0.00640  -0.00080 -0.01260 272 ILE B CD1 
4747 N N   . GLY B  279 ? 0.14740 0.12920 0.24430 0.01700  0.00450  -0.00890 273 GLY B N   
4748 C CA  . GLY B  279 ? 0.15710 0.14800 0.26490 0.02080  0.00830  -0.00600 273 GLY B CA  
4749 C C   . GLY B  279 ? 0.17490 0.17900 0.29480 0.01760  0.00310  -0.00190 273 GLY B C   
4750 O O   . GLY B  279 ? 0.17410 0.18070 0.29500 0.01570  -0.00430 -0.00080 273 GLY B O   
4751 N N   . VAL B  280 ? 0.17660 0.18950 0.30510 0.01610  0.00710  0.00030  274 VAL B N   
4752 C CA  . VAL B  280 ? 0.17770 0.20190 0.31850 0.00980  0.00300  0.00380  274 VAL B CA  
4753 C C   . VAL B  280 ? 0.20960 0.25230 0.36830 0.01360  0.00610  0.00990  274 VAL B C   
4754 O O   . VAL B  280 ? 0.16210 0.20810 0.32310 0.01860  0.01530  0.01140  274 VAL B O   
4755 C CB  . VAL B  280 ? 0.17190 0.19210 0.31000 0.00460  0.00630  0.00380  274 VAL B CB  
4756 C CG1 . VAL B  280 ? 0.18840 0.21830 0.34120 -0.00320 0.00340  0.00790  274 VAL B CG1 
4757 C CG2 . VAL B  280 ? 0.16590 0.17030 0.28870 0.00270  0.00410  -0.00050 274 VAL B CG2 
4758 N N   . ARG B  281 ? 0.16020 0.21670 0.33140 0.01140  -0.00150 0.01360  275 ARG B N   
4759 C CA  . ARG B  281 ? 0.16390 0.24270 0.35580 0.01540  0.00130  0.02120  275 ARG B CA  
4760 C C   . ARG B  281 ? 0.14750 0.23570 0.35090 0.00950  0.00660  0.02450  275 ARG B C   
4761 O O   . ARG B  281 ? 0.17750 0.25710 0.37600 0.00030  0.00460  0.02200  275 ARG B O   
4762 C CB  . ARG B  281 ? 0.17190 0.26870 0.37650 0.01290  -0.00980 0.02550  275 ARG B CB  
4763 C CG  . ARG B  281 ? 0.17160 0.26200 0.36580 0.02120  -0.01330 0.02540  275 ARG B CG  
4764 C CD  . ARG B  281 ? 0.19250 0.30610 0.39970 0.02070  -0.02440 0.03180  275 ARG B CD  
4765 N NE  . ARG B  281 ? 0.21620 0.35680 0.44860 0.02620  -0.02090 0.04160  275 ARG B NE  
4766 C CZ  . ARG B  281 ? 0.20290 0.37250 0.45360 0.02440  -0.03050 0.04910  275 ARG B CZ  
4767 N NH1 . ARG B  281 ? 0.19960 0.37410 0.44360 0.01700  -0.04470 0.04700  275 ARG B NH1 
4768 N NH2 . ARG B  281 ? 0.16580 0.36200 0.44190 0.03030  -0.02550 0.05910  275 ARG B NH2 
4769 N N   . ALA B  282 ? 0.15660 0.26260 0.37600 0.01590  0.01440  0.03120  276 ALA B N   
4770 C CA  . ALA B  282 ? 0.18080 0.29750 0.41170 0.01130  0.02130  0.03600  276 ALA B CA  
4771 C C   . ALA B  282 ? 0.17700 0.30410 0.42250 -0.00340 0.01210  0.03860  276 ALA B C   
4772 O O   . ALA B  282 ? 0.19190 0.33230 0.44880 -0.00790 0.00160  0.03990  276 ALA B O   
4773 C CB  . ALA B  282 ? 0.15760 0.29470 0.40530 0.02160  0.03190  0.04370  276 ALA B CB  
4774 N N   . SER B  283 ? 0.17340 0.29590 0.41940 -0.01110 0.01660  0.04010  277 SER B N   
4775 C CA  . SER B  283 ? 0.18320 0.30760 0.43970 -0.02670 0.00880  0.04070  277 SER B CA  
4776 C C   . SER B  283 ? 0.20700 0.33060 0.46930 -0.03210 0.01840  0.04670  277 SER B C   
4777 O O   . SER B  283 ? 0.17900 0.30110 0.43400 -0.02310 0.03000  0.04980  277 SER B O   
4778 C CB  . SER B  283 ? 0.21260 0.31240 0.44920 -0.03210 -0.00050 0.03110  277 SER B CB  
4779 O OG  . SER B  283 ? 0.20350 0.28150 0.42090 -0.02830 0.00650  0.02850  277 SER B OG  
4780 N N   . ASP B  284 ? 0.22270 0.34660 0.49720 -0.04730 0.01400  0.04840  278 ASP B N   
4781 C CA  A ASP B  284 ? 0.22100 0.33820 0.49840 -0.05290 0.02350  0.05490  278 ASP B CA  
4782 C CA  B ASP B  284 ? 0.22120 0.33890 0.49870 -0.05260 0.02380  0.05510  278 ASP B CA  
4783 C C   . ASP B  284 ? 0.21760 0.30860 0.46820 -0.04560 0.02880  0.05160  278 ASP B C   
4784 O O   . ASP B  284 ? 0.20830 0.29930 0.45470 -0.04060 0.04000  0.05830  278 ASP B O   
4785 C CB  A ASP B  284 ? 0.28410 0.39670 0.57460 -0.07160 0.01700  0.05480  278 ASP B CB  
4786 C CB  B ASP B  284 ? 0.28190 0.39780 0.57530 -0.07140 0.01850  0.05650  278 ASP B CB  
4787 C CG  A ASP B  284 ? 0.30500 0.43400 0.61270 -0.07770 0.02400  0.06460  278 ASP B CG  
4788 C CG  B ASP B  284 ? 0.29640 0.38450 0.57320 -0.07940 0.00830  0.04530  278 ASP B CG  
4789 O OD1 A ASP B  284 ? 0.31740 0.44050 0.62120 -0.07400 0.03630  0.07210  278 ASP B OD1 
4790 O OD1 B ASP B  284 ? 0.35170 0.41270 0.60860 -0.07610 0.01260  0.04280  278 ASP B OD1 
4791 O OD2 A ASP B  284 ? 0.37040 0.51920 0.69290 -0.08510 0.01730  0.06490  278 ASP B OD2 
4792 O OD2 B ASP B  284 ? 0.35660 0.45130 0.64040 -0.08890 -0.00390 0.03930  278 ASP B OD2 
4793 N N   . ALA B  285 ? 0.22080 0.29200 0.45280 -0.04440 0.02080  0.04190  279 ALA B N   
4794 C CA  . ALA B  285 ? 0.23580 0.28520 0.44450 -0.03770 0.02460  0.03920  279 ALA B CA  
4795 C C   . ALA B  285 ? 0.24370 0.29960 0.44130 -0.02450 0.03220  0.04030  279 ALA B C   
4796 O O   . ALA B  285 ? 0.23270 0.28370 0.42010 -0.02060 0.03980  0.04460  279 ALA B O   
4797 C CB  . ALA B  285 ? 0.19920 0.22990 0.39270 -0.03840 0.01510  0.02900  279 ALA B CB  
4798 N N   . THR B  286 ? 0.20980 0.27610 0.40830 -0.01750 0.03030  0.03640  280 THR B N   
4799 C CA  . THR B  286 ? 0.17300 0.24220 0.36010 -0.00610 0.03830  0.03560  280 THR B CA  
4800 C C   . THR B  286 ? 0.20140 0.28530 0.39660 -0.00380 0.05010  0.04430  280 THR B C   
4801 O O   . THR B  286 ? 0.19060 0.27190 0.37050 0.00260  0.05790  0.04450  280 THR B O   
4802 C CB  . THR B  286 ? 0.22270 0.29720 0.41080 0.00130  0.03580  0.03070  280 THR B CB  
4803 O OG1 . THR B  286 ? 0.22480 0.31980 0.43580 0.00050  0.03540  0.03640  280 THR B OG1 
4804 C CG2 . THR B  286 ? 0.25650 0.31650 0.43390 0.00020  0.02540  0.02300  280 THR B CG2 
4805 N N   . ARG B  287 ? 0.17250 0.27380 0.39150 -0.00930 0.05160  0.05190  281 ARG B N   
4806 C CA  . ARG B  287 ? 0.16160 0.27860 0.38960 -0.00690 0.06450  0.06170  281 ARG B CA  
4807 C C   . ARG B  287 ? 0.23510 0.34190 0.45300 -0.01060 0.07000  0.06750  281 ARG B C   
4808 O O   . ARG B  287 ? 0.24400 0.35540 0.45160 -0.00370 0.08080  0.07200  281 ARG B O   
4809 C CB  . ARG B  287 ? 0.17880 0.31970 0.43810 -0.01320 0.06500  0.06990  281 ARG B CB  
4810 C CG  . ARG B  287 ? 0.13520 0.29150 0.40570 -0.00610 0.06210  0.06770  281 ARG B CG  
4811 C CD  . ARG B  287 ? 0.13750 0.32290 0.43820 -0.01030 0.06330  0.07740  281 ARG B CD  
4812 N NE  . ARG B  287 ? 0.17450 0.36210 0.48840 -0.02560 0.04930  0.07640  281 ARG B NE  
4813 C CZ  . ARG B  287 ? 0.19020 0.38040 0.50790 -0.02740 0.03640  0.07090  281 ARG B CZ  
4814 N NH1 . ARG B  287 ? 0.13530 0.32770 0.44820 -0.01430 0.03610  0.06790  281 ARG B NH1 
4815 N NH2 . ARG B  287 ? 0.29230 0.48250 0.61750 -0.04270 0.02390  0.06840  281 ARG B NH2 
4816 N N   . GLN B  288 ? 0.21750 0.31000 0.43730 -0.02080 0.06330  0.06800  282 GLN B N   
4817 C CA  . GLN B  288 ? 0.25380 0.33400 0.46380 -0.02250 0.06890  0.07500  282 GLN B CA  
4818 C C   . GLN B  288 ? 0.22310 0.29370 0.40550 -0.01220 0.07020  0.07100  282 GLN B C   
4819 O O   . GLN B  288 ? 0.27910 0.34910 0.45130 -0.00900 0.07770  0.07900  282 GLN B O   
4820 C CB  . GLN B  288 ? 0.26510 0.32650 0.48020 -0.03390 0.06190  0.07450  282 GLN B CB  
4821 C CG  . GLN B  288 ? 0.35050 0.42050 0.59270 -0.04770 0.06120  0.07960  282 GLN B CG  
4822 C CD  . GLN B  288 ? 0.45360 0.50030 0.69730 -0.05970 0.05450  0.07610  282 GLN B CD  
4823 O OE1 . GLN B  288 ? 0.56950 0.59340 0.79620 -0.05650 0.05540  0.07540  282 GLN B OE1 
4824 N NE2 . GLN B  288 ? 0.49760 0.55030 0.76140 -0.07350 0.04770  0.07360  282 GLN B NE2 
4825 N N   . LEU B  289 ? 0.22060 0.28530 0.39110 -0.00750 0.06290  0.05950  283 LEU B N   
4826 C CA  . LEU B  289 ? 0.22900 0.28780 0.37540 0.00050  0.06330  0.05470  283 LEU B CA  
4827 C C   . LEU B  289 ? 0.30170 0.37330 0.43870 0.00850  0.07210  0.05400  283 LEU B C   
4828 O O   . LEU B  289 ? 0.28260 0.35120 0.39830 0.01370  0.07260  0.04930  283 LEU B O   
4829 C CB  . LEU B  289 ? 0.19750 0.24540 0.33570 0.00150  0.05340  0.04280  283 LEU B CB  
4830 C CG  . LEU B  289 ? 0.22970 0.26190 0.36900 -0.00410 0.04560  0.04170  283 LEU B CG  
4831 C CD1 . LEU B  289 ? 0.24440 0.26910 0.37890 -0.00330 0.03690  0.03110  283 LEU B CD1 
4832 C CD2 . LEU B  289 ? 0.19520 0.21930 0.32190 -0.00180 0.04800  0.04750  283 LEU B CD2 
4833 N N   . GLY B  290 ? 0.26140 0.34730 0.41360 0.00960  0.07900  0.05760  284 GLY B N   
4834 C CA  . GLY B  290 ? 0.28780 0.38490 0.43110 0.01800  0.09030  0.05800  284 GLY B CA  
4835 C C   . GLY B  290 ? 0.31030 0.40820 0.45040 0.02530  0.09170  0.04780  284 GLY B C   
4836 O O   . GLY B  290 ? 0.32860 0.42890 0.45300 0.03290  0.10080  0.04430  284 GLY B O   
4837 N N   . THR B  291 ? 0.25700 0.35180 0.41000 0.02380  0.08380  0.04310  285 THR B N   
4838 C CA  . THR B  291 ? 0.25320 0.34880 0.40630 0.03230  0.08710  0.03630  285 THR B CA  
4839 C C   . THR B  291 ? 0.22050 0.33190 0.40260 0.03220  0.08640  0.04280  285 THR B C   
4840 O O   . THR B  291 ? 0.22170 0.33910 0.42140 0.02300  0.07850  0.04830  285 THR B O   
4841 C CB  . THR B  291 ? 0.22860 0.30530 0.36550 0.03330  0.07900  0.02420  285 THR B CB  
4842 O OG1 . THR B  291 ? 0.30510 0.37990 0.44160 0.04250  0.08490  0.01890  285 THR B OG1 
4843 C CG2 . THR B  291 ? 0.24380 0.31510 0.39070 0.02610  0.06580  0.02410  285 THR B CG2 
4844 N N   . ASP B  292 ? 0.20270 0.32250 0.39020 0.04270  0.09560  0.04260  286 ASP B N   
4845 C CA  . ASP B  292 ? 0.18810 0.32820 0.40500 0.04480  0.09560  0.05040  286 ASP B CA  
4846 C C   . ASP B  292 ? 0.23880 0.37290 0.45980 0.04790  0.08630  0.04570  286 ASP B C   
4847 O O   . ASP B  292 ? 0.24410 0.39710 0.48900 0.05070  0.08480  0.05280  286 ASP B O   
4848 C CB  . ASP B  292 ? 0.24360 0.39840 0.46640 0.05600  0.11130  0.05540  286 ASP B CB  
4849 C CG  . ASP B  292 ? 0.30430 0.44160 0.50290 0.06860  0.12070  0.04490  286 ASP B CG  
4850 O OD1 . ASP B  292 ? 0.36170 0.47730 0.54210 0.06840  0.11540  0.03420  286 ASP B OD1 
4851 O OD2 . ASP B  292 ? 0.36810 0.50990 0.56220 0.07680  0.13160  0.04600  286 ASP B OD2 
4852 N N   . GLY B  293 ? 0.22060 0.33120 0.41990 0.04760  0.08000  0.03540  287 GLY B N   
4853 C CA  . GLY B  293 ? 0.19740 0.30180 0.39960 0.05000  0.07140  0.03250  287 GLY B CA  
4854 C C   . GLY B  293 ? 0.19910 0.28850 0.39010 0.03990  0.05780  0.02700  287 GLY B C   
4855 O O   . GLY B  293 ? 0.14890 0.23870 0.33990 0.02970  0.05250  0.02850  287 GLY B O   
4856 N N   . ALA B  294 ? 0.17920 0.25460 0.36120 0.04370  0.05340  0.02150  288 ALA B N   
4857 C CA  . ALA B  294 ? 0.16360 0.22460 0.33380 0.03640  0.04230  0.01630  288 ALA B CA  
4858 C C   . ALA B  294 ? 0.16000 0.20430 0.30820 0.03330  0.04460  0.00880  288 ALA B C   
4859 O O   . ALA B  294 ? 0.21290 0.25540 0.35210 0.03690  0.05390  0.00640  288 ALA B O   
4860 C CB  . ALA B  294 ? 0.17190 0.22550 0.34080 0.04190  0.03810  0.01490  288 ALA B CB  
4861 N N   . LEU B  295 ? 0.15650 0.32150 0.32500 0.08810  0.05330  0.05400  289 LEU B N   
4862 C CA  . LEU B  295 ? 0.15780 0.28300 0.29860 0.07820  0.05480  0.05050  289 LEU B CA  
4863 C C   . LEU B  295 ? 0.18430 0.29000 0.29950 0.07980  0.04330  0.04560  289 LEU B C   
4864 O O   . LEU B  295 ? 0.16280 0.28720 0.28590 0.08250  0.03150  0.04240  289 LEU B O   
4865 C CB  . LEU B  295 ? 0.20140 0.33340 0.36260 0.05900  0.05260  0.04580  289 LEU B CB  
4866 C CG  . LEU B  295 ? 0.23760 0.33820 0.38100 0.04840  0.05680  0.04430  289 LEU B CG  
4867 C CD1 . LEU B  295 ? 0.24150 0.35440 0.41050 0.03890  0.06770  0.04710  289 LEU B CD1 
4868 C CD2 . LEU B  295 ? 0.26370 0.35920 0.40290 0.03870  0.04170  0.03570  289 LEU B CD2 
4869 N N   . GLY B  296 ? 0.18020 0.24920 0.26460 0.07850  0.04690  0.04490  290 GLY B N   
4870 C CA  . GLY B  296 ? 0.20460 0.25490 0.26830 0.07680  0.03770  0.04010  290 GLY B CA  
4871 C C   . GLY B  296 ? 0.16090 0.19110 0.21470 0.06340  0.03480  0.03570  290 GLY B C   
4872 O O   . GLY B  296 ? 0.20580 0.22390 0.25440 0.05970  0.04220  0.03760  290 GLY B O   
4873 N N   . ILE B  297 ? 0.18080 0.20800 0.23120 0.05770  0.02430  0.03030  291 ILE B N   
4874 C CA  . ILE B  297 ? 0.21820 0.22930 0.26070 0.04710  0.02060  0.02660  291 ILE B CA  
4875 C C   . ILE B  297 ? 0.21990 0.21400 0.24330 0.04850  0.01650  0.02440  291 ILE B C   
4876 O O   . ILE B  297 ? 0.19560 0.19550 0.21840 0.05340  0.01230  0.02350  291 ILE B O   
4877 C CB  . ILE B  297 ? 0.16760 0.19280 0.22880 0.03720  0.01350  0.02210  291 ILE B CB  
4878 C CG1 . ILE B  297 ? 0.17390 0.21760 0.25870 0.03290  0.01840  0.02350  291 ILE B CG1 
4879 C CG2 . ILE B  297 ? 0.14790 0.15540 0.19940 0.02940  0.01110  0.01960  291 ILE B CG2 
4880 C CD1 . ILE B  297 ? 0.18160 0.23990 0.28560 0.02210  0.01050  0.01690  291 ILE B CD1 
4881 N N   . SER B  298 ? 0.23020 0.20490 0.23880 0.04400  0.01760  0.02370  292 SER B N   
4882 C CA  . SER B  298 ? 0.19260 0.15480 0.18920 0.04220  0.01380  0.02110  292 SER B CA  
4883 C C   . SER B  298 ? 0.24980 0.20700 0.24600 0.03390  0.00930  0.01890  292 SER B C   
4884 O O   . SER B  298 ? 0.22630 0.18070 0.22150 0.03140  0.01100  0.02010  292 SER B O   
4885 C CB  . SER B  298 ? 0.24750 0.19080 0.22480 0.04660  0.01980  0.02200  292 SER B CB  
4886 O OG  . SER B  298 ? 0.24720 0.17900 0.21370 0.04610  0.02470  0.02280  292 SER B OG  
4887 N N   . VAL B  299 ? 0.22380 0.18100 0.22110 0.03110  0.00460  0.01660  293 VAL B N   
4888 C CA  . VAL B  299 ? 0.20610 0.16320 0.20670 0.02560  0.00020  0.01540  293 VAL B CA  
4889 C C   . VAL B  299 ? 0.20770 0.15950 0.20370 0.02360  -0.00130 0.01400  293 VAL B C   
4890 O O   . VAL B  299 ? 0.20520 0.15510 0.19890 0.02620  0.00070  0.01380  293 VAL B O   
4891 C CB  . VAL B  299 ? 0.18870 0.15500 0.20120 0.02440  -0.00260 0.01410  293 VAL B CB  
4892 C CG1 . VAL B  299 ? 0.22500 0.18840 0.23860 0.02150  -0.00510 0.01410  293 VAL B CG1 
4893 C CG2 . VAL B  299 ? 0.16500 0.13800 0.18680 0.02330  -0.00020 0.01490  293 VAL B CG2 
4894 N N   . LYS B  300 ? 0.23750 0.18780 0.23250 0.01940  -0.00440 0.01360  294 LYS B N   
4895 C CA  . LYS B  300 ? 0.21850 0.16930 0.21580 0.01570  -0.00590 0.01220  294 LYS B CA  
4896 C C   . LYS B  300 ? 0.19860 0.15850 0.20430 0.01470  -0.01070 0.01320  294 LYS B C   
4897 O O   . LYS B  300 ? 0.20240 0.16240 0.20440 0.01510  -0.01370 0.01420  294 LYS B O   
4898 C CB  . LYS B  300 ? 0.19160 0.13230 0.17880 0.01090  -0.00500 0.00970  294 LYS B CB  
4899 C CG  . LYS B  300 ? 0.22520 0.17110 0.21960 0.00350  -0.00850 0.00740  294 LYS B CG  
4900 C CD  . LYS B  300 ? 0.21610 0.16320 0.21880 0.00260  -0.00340 0.00830  294 LYS B CD  
4901 C CE  . LYS B  300 ? 0.19230 0.14820 0.20730 -0.00670 -0.00570 0.00610  294 LYS B CE  
4902 N NZ  . LYS B  300 ? 0.21790 0.16990 0.23820 -0.00800 0.00340  0.00770  294 LYS B NZ  
4903 N N   . ILE B  301 ? 0.18130 0.14740 0.19620 0.01530  -0.01030 0.01380  295 ILE B N   
4904 C CA  . ILE B  301 ? 0.18420 0.16000 0.20780 0.01610  -0.01380 0.01570  295 ILE B CA  
4905 C C   . ILE B  301 ? 0.18290 0.16630 0.21270 0.01010  -0.01640 0.01430  295 ILE B C   
4906 O O   . ILE B  301 ? 0.16260 0.14500 0.19650 0.00690  -0.01200 0.01330  295 ILE B O   
4907 C CB  . ILE B  301 ? 0.19870 0.17670 0.22860 0.02080  -0.01050 0.01710  295 ILE B CB  
4908 C CG1 . ILE B  301 ? 0.20970 0.17990 0.23400 0.02360  -0.00880 0.01590  295 ILE B CG1 
4909 C CG2 . ILE B  301 ? 0.16810 0.15540 0.20640 0.02430  -0.01250 0.02040  295 ILE B CG2 
4910 C CD1 . ILE B  301 ? 0.20750 0.17440 0.22980 0.02450  -0.01000 0.01740  295 ILE B CD1 
4911 N N   . GLU B  302 ? 0.15950 0.15040 0.18970 0.00860  -0.02350 0.01420  296 GLU B N   
4912 C CA  . GLU B  302 ? 0.16420 0.16390 0.20020 0.00040  -0.02860 0.01070  296 GLU B CA  
4913 C C   . GLU B  302 ? 0.17630 0.18960 0.23210 -0.00310 -0.02550 0.01150  296 GLU B C   
4914 O O   . GLU B  302 ? 0.17600 0.18940 0.23700 -0.01290 -0.02400 0.00770  296 GLU B O   
4915 C CB  . GLU B  302 ? 0.16770 0.17830 0.20150 0.00210  -0.03890 0.01100  296 GLU B CB  
4916 C CG  . GLU B  302 ? 0.21230 0.23560 0.25270 -0.00810 -0.04750 0.00540  296 GLU B CG  
4917 C CD  . GLU B  302 ? 0.23320 0.23710 0.25800 -0.01780 -0.04580 -0.00170 296 GLU B CD  
4918 O OE1 . GLU B  302 ? 0.23690 0.22100 0.24140 -0.01360 -0.04200 -0.00160 296 GLU B OE1 
4919 O OE2 . GLU B  302 ? 0.21640 0.22370 0.24950 -0.02970 -0.04700 -0.00730 296 GLU B OE2 
4920 N N   . ASP B  303 ? 0.18100 0.20440 0.24760 0.00470  -0.02320 0.01640  297 ASP B N   
4921 C CA  . ASP B  303 ? 0.16570 0.20380 0.25220 0.00390  -0.01840 0.01870  297 ASP B CA  
4922 C C   . ASP B  303 ? 0.16960 0.19360 0.25190 0.00590  -0.00660 0.01980  297 ASP B C   
4923 O O   . ASP B  303 ? 0.16760 0.20000 0.26380 0.00610  0.00050  0.02250  297 ASP B O   
4924 C CB  . ASP B  303 ? 0.16950 0.22370 0.26690 0.01420  -0.02040 0.02440  297 ASP B CB  
4925 C CG  . ASP B  303 ? 0.17470 0.21200 0.25660 0.02480  -0.01690 0.02710  297 ASP B CG  
4926 O OD1 . ASP B  303 ? 0.17680 0.20460 0.25610 0.02890  -0.00840 0.02800  297 ASP B OD1 
4927 O OD2 . ASP B  303 ? 0.16160 0.19340 0.23240 0.02780  -0.02220 0.02750  297 ASP B OD2 
4928 N N   . GLY B  304 ? 0.15700 0.16150 0.22070 0.00830  -0.00420 0.01830  298 GLY B N   
4929 C CA  . GLY B  304 ? 0.18550 0.17730 0.24190 0.01120  0.00520  0.01900  298 GLY B CA  
4930 C C   . GLY B  304 ? 0.20490 0.19350 0.25740 0.02120  0.00940  0.02140  298 GLY B C   
4931 O O   . GLY B  304 ? 0.19150 0.17100 0.23690 0.02470  0.01710  0.02230  298 GLY B O   
4932 N N   . ASN B  305 ? 0.16310 0.15530 0.21640 0.02650  0.00520  0.02220  299 ASN B N   
4933 C CA  . ASN B  305 ? 0.19830 0.18370 0.24560 0.03500  0.00960  0.02310  299 ASN B CA  
4934 C C   . ASN B  305 ? 0.22370 0.19490 0.25430 0.03660  0.00810  0.01900  299 ASN B C   
4935 O O   . ASN B  305 ? 0.20440 0.17340 0.23180 0.03420  0.00250  0.01690  299 ASN B O   
4936 C CB  . ASN B  305 ? 0.19370 0.18480 0.24670 0.04010  0.00730  0.02570  299 ASN B CB  
4937 C CG  . ASN B  305 ? 0.23340 0.21410 0.27890 0.04900  0.01360  0.02630  299 ASN B CG  
4938 O OD1 . ASN B  305 ? 0.22200 0.18780 0.25310 0.04990  0.01320  0.02210  299 ASN B OD1 
4939 N ND2 . ASN B  305 ? 0.25830 0.24750 0.31390 0.05570  0.01960  0.03120  299 ASN B ND2 
4940 N N   . LEU B  306 ? 0.21000 0.17290 0.23050 0.04110  0.01310  0.01820  300 LEU B N   
4941 C CA  . LEU B  306 ? 0.24220 0.19630 0.24800 0.04310  0.01000  0.01390  300 LEU B CA  
4942 C C   . LEU B  306 ? 0.25880 0.20770 0.25990 0.04430  0.00590  0.00960  300 LEU B C   
4943 O O   . LEU B  306 ? 0.22030 0.16900 0.21900 0.04100  0.00000  0.00560  300 LEU B O   
4944 C CB  . LEU B  306 ? 0.26640 0.21270 0.25950 0.04970  0.01640  0.01470  300 LEU B CB  
4945 C CG  . LEU B  306 ? 0.33600 0.27620 0.31220 0.05430  0.01190  0.01040  300 LEU B CG  
4946 C CD1 . LEU B  306 ? 0.36790 0.31230 0.34550 0.05150  0.00840  0.01100  300 LEU B CD1 
4947 C CD2 . LEU B  306 ? 0.43590 0.36570 0.39460 0.06380  0.01910  0.01200  300 LEU B CD2 
4948 N N   . GLU B  307 ? 0.22210 0.16590 0.22200 0.04880  0.01020  0.01040  301 GLU B N   
4949 C CA  . GLU B  307 ? 0.25250 0.18580 0.24580 0.04900  0.00830  0.00590  301 GLU B CA  
4950 C C   . GLU B  307 ? 0.26570 0.20220 0.26780 0.04270  0.00390  0.00620  301 GLU B C   
4951 O O   . GLU B  307 ? 0.25850 0.18900 0.25720 0.03800  0.00040  0.00090  301 GLU B O   
4952 C CB  . GLU B  307 ? 0.26050 0.18560 0.25070 0.05660  0.01590  0.00840  301 GLU B CB  
4953 C CG  . GLU B  307 ? 0.33010 0.23740 0.30970 0.05700  0.01630  0.00320  301 GLU B CG  
4954 C CD  . GLU B  307 ? 0.32510 0.22180 0.30000 0.06700  0.02590  0.00690  301 GLU B CD  
4955 O OE1 . GLU B  307 ? 0.29820 0.20760 0.28750 0.07180  0.02970  0.01530  301 GLU B OE1 
4956 O OE2 . GLU B  307 ? 0.33770 0.21390 0.29420 0.07070  0.02950  0.00130  301 GLU B OE2 
4957 N N   . MET B  308 ? 0.21260 0.15900 0.22600 0.04220  0.00410  0.01200  302 MET B N   
4958 C CA  . MET B  308 ? 0.19050 0.13800 0.20810 0.03810  0.00090  0.01330  302 MET B CA  
4959 C C   . MET B  308 ? 0.19650 0.14750 0.21410 0.03180  -0.00340 0.01030  302 MET B C   
4960 O O   . MET B  308 ? 0.21610 0.16360 0.23420 0.02800  -0.00420 0.00920  302 MET B O   
4961 C CB  . MET B  308 ? 0.23400 0.19270 0.26060 0.04030  0.00030  0.01960  302 MET B CB  
4962 C CG  . MET B  308 ? 0.19790 0.15630 0.22720 0.04910  0.00480  0.02430  302 MET B CG  
4963 S SD  . MET B  308 ? 0.24880 0.18590 0.26720 0.05360  0.00940  0.02440  302 MET B SD  
4964 C CE  . MET B  308 ? 0.25940 0.18130 0.26690 0.05560  0.01470  0.01810  302 MET B CE  
4965 N N   . LEU B  309 ? 0.21100 0.16820 0.22820 0.03130  -0.00430 0.01000  303 LEU B N   
4966 C CA  . LEU B  309 ? 0.18890 0.14920 0.20520 0.02820  -0.00710 0.00820  303 LEU B CA  
4967 C C   . LEU B  309 ? 0.19260 0.15150 0.20770 0.02640  -0.00960 0.00300  303 LEU B C   
4968 O O   . LEU B  309 ? 0.19970 0.16130 0.22010 0.02220  -0.01060 0.00240  303 LEU B O   
4969 C CB  . LEU B  309 ? 0.20590 0.16810 0.21810 0.03040  -0.00570 0.00890  303 LEU B CB  
4970 C CG  . LEU B  309 ? 0.20320 0.16820 0.21270 0.03070  -0.00740 0.00790  303 LEU B CG  
4971 C CD1 . LEU B  309 ? 0.14720 0.11250 0.15900 0.02730  -0.00670 0.01030  303 LEU B CD1 
4972 C CD2 . LEU B  309 ? 0.16310 0.12530 0.16370 0.03630  -0.00470 0.00880  303 LEU B CD2 
4973 N N   . TYR B  310 ? 0.20260 0.15760 0.21060 0.02920  -0.01050 -0.00110 304 TYR B N   
4974 C CA  . TYR B  310 ? 0.17040 0.12620 0.17720 0.02600  -0.01530 -0.00820 304 TYR B CA  
4975 C C   . TYR B  310 ? 0.20950 0.15850 0.22240 0.01880  -0.01410 -0.01050 304 TYR B C   
4976 O O   . TYR B  310 ? 0.23870 0.19350 0.25940 0.01210  -0.01710 -0.01470 304 TYR B O   
4977 C CB  . TYR B  310 ? 0.25630 0.20520 0.24940 0.03080  -0.01680 -0.01300 304 TYR B CB  
4978 C CG  . TYR B  310 ? 0.24530 0.19800 0.22950 0.03860  -0.01670 -0.01060 304 TYR B CG  
4979 C CD1 . TYR B  310 ? 0.24890 0.21310 0.23700 0.04000  -0.01910 -0.00810 304 TYR B CD1 
4980 C CD2 . TYR B  310 ? 0.24370 0.18650 0.21400 0.04600  -0.01230 -0.00980 304 TYR B CD2 
4981 C CE1 . TYR B  310 ? 0.27010 0.23380 0.24730 0.04840  -0.01720 -0.00490 304 TYR B CE1 
4982 C CE2 . TYR B  310 ? 0.29890 0.24220 0.25870 0.05390  -0.01000 -0.00640 304 TYR B CE2 
4983 C CZ  . TYR B  310 ? 0.31440 0.26720 0.27740 0.05490  -0.01260 -0.00400 304 TYR B CZ  
4984 O OH  . TYR B  310 ? 0.29770 0.24730 0.24810 0.06390  -0.00870 0.00040  304 TYR B OH  
4985 N N   . ALA B  311 ? 0.21600 0.15310 0.22620 0.02060  -0.00870 -0.00730 305 ALA B N   
4986 C CA  . ALA B  311 ? 0.23280 0.15850 0.24560 0.01540  -0.00500 -0.00780 305 ALA B CA  
4987 C C   . ALA B  311 ? 0.23920 0.17200 0.26170 0.01140  -0.00370 -0.00330 305 ALA B C   
4988 O O   . ALA B  311 ? 0.24120 0.17140 0.27020 0.00370  -0.00180 -0.00590 305 ALA B O   
4989 C CB  . ALA B  311 ? 0.21640 0.12820 0.22260 0.02210  0.00130  -0.00310 305 ALA B CB  
4990 N N   . VAL B  312 ? 0.20230 0.14350 0.22570 0.01580  -0.00400 0.00290  306 VAL B N   
4991 C CA  . VAL B  312 ? 0.17440 0.11900 0.20180 0.01390  -0.00200 0.00740  306 VAL B CA  
4992 C C   . VAL B  312 ? 0.19230 0.14790 0.22800 0.00910  -0.00360 0.00420  306 VAL B C   
4993 O O   . VAL B  312 ? 0.18970 0.14530 0.23180 0.00480  0.00070  0.00570  306 VAL B O   
4994 C CB  . VAL B  312 ? 0.20860 0.15800 0.23200 0.01900  -0.00340 0.01260  306 VAL B CB  
4995 C CG1 . VAL B  312 ? 0.19820 0.15090 0.22130 0.01770  -0.00220 0.01530  306 VAL B CG1 
4996 C CG2 . VAL B  312 ? 0.15700 0.10070 0.17640 0.02410  -0.00210 0.01710  306 VAL B CG2 
4997 N N   . VAL B  313 ? 0.17910 0.14510 0.21490 0.01140  -0.00860 0.00120  307 VAL B N   
4998 C CA  . VAL B  313 ? 0.20090 0.18140 0.24540 0.00980  -0.01070 -0.00070 307 VAL B CA  
4999 C C   . VAL B  313 ? 0.23230 0.21700 0.28850 0.00130  -0.01190 -0.00660 307 VAL B C   
5000 O O   . VAL B  313 ? 0.19910 0.19440 0.26870 -0.00310 -0.00950 -0.00600 307 VAL B O   
5001 C CB  . VAL B  313 ? 0.16120 0.14960 0.19990 0.01660  -0.01550 -0.00200 307 VAL B CB  
5002 C CG1 . VAL B  313 ? 0.13160 0.13890 0.18000 0.01750  -0.01970 -0.00440 307 VAL B CG1 
5003 C CG2 . VAL B  313 ? 0.17830 0.16170 0.20800 0.02240  -0.01240 0.00360  307 VAL B CG2 
5004 N N   . THR B  314 ? 0.17840 0.15280 0.22960 -0.00200 -0.01400 -0.01260 308 THR B N   
5005 C CA  . THR B  314 ? 0.21060 0.18640 0.27200 -0.01280 -0.01560 -0.02040 308 THR B CA  
5006 C C   . THR B  314 ? 0.20200 0.16640 0.27060 -0.02000 -0.00580 -0.01690 308 THR B C   
5007 O O   . THR B  314 ? 0.17720 0.14970 0.26240 -0.03010 -0.00380 -0.02000 308 THR B O   
5008 C CB  . THR B  314 ? 0.18930 0.15210 0.23860 -0.01430 -0.01990 -0.02900 308 THR B CB  
5009 O OG1 . THR B  314 ? 0.20840 0.17860 0.24670 -0.00500 -0.02690 -0.03020 308 THR B OG1 
5010 C CG2 . THR B  314 ? 0.25070 0.21890 0.31190 -0.02800 -0.02460 -0.04020 308 THR B CG2 
5011 N N   . GLU B  315 ? 0.19350 0.14010 0.25030 -0.01430 0.00100  -0.00980 309 GLU B N   
5012 C CA  . GLU B  315 ? 0.22010 0.15310 0.27850 -0.01770 0.01160  -0.00420 309 GLU B CA  
5013 C C   . GLU B  315 ? 0.19270 0.13990 0.26200 -0.01820 0.01540  0.00120  309 GLU B C   
5014 O O   . GLU B  315 ? 0.20260 0.14750 0.28250 -0.02570 0.02380  0.00260  309 GLU B O   
5015 C CB  . GLU B  315 ? 0.21630 0.13170 0.25800 -0.00790 0.01580  0.00320  309 GLU B CB  
5016 C CG  . GLU B  315 ? 0.21610 0.11600 0.25350 -0.00680 0.02680  0.01130  309 GLU B CG  
5017 C CD  . GLU B  315 ? 0.25420 0.13390 0.29350 -0.01570 0.03620  0.00880  309 GLU B CD  
5018 O OE1 . GLU B  315 ? 0.26380 0.13760 0.30480 -0.02260 0.03350  -0.00030 309 GLU B OE1 
5019 O OE2 . GLU B  315 ? 0.29400 0.16020 0.33050 -0.01570 0.04740  0.01590  309 GLU B OE2 
5020 N N   . LEU B  316 ? 0.19060 0.15090 0.25700 -0.01040 0.01080  0.00410  310 LEU B N   
5021 C CA  . LEU B  316 ? 0.17470 0.14470 0.24690 -0.00850 0.01570  0.00960  310 LEU B CA  
5022 C C   . LEU B  316 ? 0.17950 0.16940 0.27440 -0.01620 0.01610  0.00570  310 LEU B C   
5023 O O   . LEU B  316 ? 0.16230 0.15590 0.26750 -0.01890 0.02550  0.01030  310 LEU B O   
5024 C CB  . LEU B  316 ? 0.15900 0.13450 0.22040 0.00110  0.01110  0.01220  310 LEU B CB  
5025 C CG  . LEU B  316 ? 0.23140 0.21090 0.29130 0.00570  0.01680  0.01790  310 LEU B CG  
5026 C CD1 . LEU B  316 ? 0.22400 0.18930 0.27720 0.00580  0.02690  0.02420  310 LEU B CD1 
5027 C CD2 . LEU B  316 ? 0.22290 0.19940 0.26690 0.01370  0.01220  0.01890  310 LEU B CD2 
5028 N N   . LEU B  317 ? 0.15230 0.15690 0.25540 -0.01920 0.00610  -0.00240 311 LEU B N   
5029 C CA  . LEU B  317 ? 0.18790 0.21720 0.31590 -0.02710 0.00360  -0.00720 311 LEU B CA  
5030 C C   . LEU B  317 ? 0.18410 0.20670 0.32680 -0.04180 0.01130  -0.01020 311 LEU B C   
5031 O O   . LEU B  317 ? 0.16880 0.20790 0.33450 -0.04860 0.01730  -0.00890 311 LEU B O   
5032 C CB  . LEU B  317 ? 0.18310 0.22720 0.31170 -0.02640 -0.01060 -0.01610 311 LEU B CB  
5033 C CG  . LEU B  317 ? 0.20460 0.25710 0.32130 -0.01160 -0.01580 -0.01210 311 LEU B CG  
5034 C CD1 . LEU B  317 ? 0.24850 0.30860 0.35810 -0.00870 -0.02870 -0.01980 311 LEU B CD1 
5035 C CD2 . LEU B  317 ? 0.23490 0.30920 0.36620 -0.00630 -0.01220 -0.00630 311 LEU B CD2 
5036 N N   . GLU B  318 ? 0.17980 0.17680 0.30960 -0.04650 0.01290  -0.01350 312 GLU B N   
5037 C CA  . GLU B  318 ? 0.22230 0.20520 0.36220 -0.06030 0.02320  -0.01550 312 GLU B CA  
5038 C C   . GLU B  318 ? 0.20370 0.17780 0.34510 -0.05810 0.03940  -0.00390 312 GLU B C   
5039 O O   . GLU B  318 ? 0.21460 0.19320 0.37650 -0.06960 0.04950  -0.00350 312 GLU B O   
5040 C CB  . GLU B  318 ? 0.21890 0.17040 0.33890 -0.06200 0.02400  -0.01960 312 GLU B CB  
5041 C CG  . GLU B  318 ? 0.27880 0.21080 0.40700 -0.07750 0.03520  -0.02330 312 GLU B CG  
5042 C CD  . GLU B  318 ? 0.36390 0.26170 0.47070 -0.07870 0.03680  -0.02860 312 GLU B CD  
5043 O OE1 . GLU B  318 ? 0.35410 0.22570 0.43960 -0.06770 0.04540  -0.01960 312 GLU B OE1 
5044 O OE2 . GLU B  318 ? 0.44130 0.33870 0.55190 -0.09010 0.02930  -0.04190 312 GLU B OE2 
5045 N N   . ARG B  319 ? 0.21600 0.17780 0.33550 -0.04380 0.04220  0.00550  313 ARG B N   
5046 C CA  . ARG B  319 ? 0.23060 0.18090 0.34480 -0.03960 0.05700  0.01650  313 ARG B CA  
5047 C C   . ARG B  319 ? 0.20860 0.18330 0.34170 -0.03940 0.06160  0.02000  313 ARG B C   
5048 O O   . ARG B  319 ? 0.21230 0.18100 0.35010 -0.04100 0.07690  0.02730  313 ARG B O   
5049 C CB  . ARG B  319 ? 0.23680 0.17120 0.32210 -0.02450 0.05550  0.02370  313 ARG B CB  
5050 C CG  . ARG B  319 ? 0.30410 0.21480 0.37250 -0.02250 0.05400  0.02270  313 ARG B CG  
5051 C CD  . ARG B  319 ? 0.33590 0.22780 0.38040 -0.01030 0.05930  0.03270  313 ARG B CD  
5052 N NE  . ARG B  319 ? 0.28870 0.16500 0.31850 -0.00460 0.05560  0.03260  313 ARG B NE  
5053 C CZ  . ARG B  319 ? 0.29630 0.16260 0.30620 0.00820  0.05520  0.04010  313 ARG B CZ  
5054 N NH1 . ARG B  319 ? 0.29210 0.15910 0.29090 0.01540  0.05750  0.04710  313 ARG B NH1 
5055 N NH2 . ARG B  319 ? 0.29260 0.14880 0.29280 0.01440  0.05220  0.04050  313 ARG B NH2 
5056 N N   . LEU B  320 ? 0.18880 0.18950 0.33120 -0.03590 0.05030  0.01600  314 LEU B N   
5057 C CA  . LEU B  320 ? 0.20660 0.23280 0.36770 -0.03320 0.05470  0.01970  314 LEU B CA  
5058 C C   . LEU B  320 ? 0.20230 0.25590 0.40030 -0.04750 0.05480  0.01370  314 LEU B C   
5059 O O   . LEU B  320 ? 0.17300 0.25290 0.39290 -0.04570 0.05950  0.01730  314 LEU B O   
5060 C CB  . LEU B  320 ? 0.16630 0.20620 0.31820 -0.02030 0.04380  0.01950  314 LEU B CB  
5061 C CG  . LEU B  320 ? 0.21430 0.23060 0.33300 -0.00820 0.04340  0.02440  314 LEU B CG  
5062 C CD1 . LEU B  320 ? 0.19340 0.21870 0.30310 0.00120  0.03250  0.02210  314 LEU B CD1 
5063 C CD2 . LEU B  320 ? 0.23150 0.23540 0.33840 -0.00120 0.05740  0.03390  314 LEU B CD2 
5064 N N   . GLY B  321 ? 0.18570 0.23410 0.39150 -0.06150 0.04990  0.00440  315 GLY B N   
5065 C CA  . GLY B  321 ? 0.19000 0.26520 0.43130 -0.07790 0.04740  -0.00380 315 GLY B CA  
5066 C C   . GLY B  321 ? 0.17460 0.28960 0.43300 -0.07400 0.03090  -0.00970 315 GLY B C   
5067 O O   . GLY B  321 ? 0.17480 0.32460 0.46880 -0.08290 0.02990  -0.01290 315 GLY B O   
5068 N N   . ILE B  322 ? 0.19810 0.30980 0.43270 -0.06070 0.01810  -0.01110 316 ILE B N   
5069 C CA  . ILE B  322 ? 0.20740 0.35210 0.45100 -0.05340 0.00260  -0.01550 316 ILE B CA  
5070 C C   . ILE B  322 ? 0.24670 0.39340 0.48900 -0.06330 -0.01340 -0.02970 316 ILE B C   
5071 O O   . ILE B  322 ? 0.28370 0.40110 0.49810 -0.06160 -0.01680 -0.03290 316 ILE B O   
5072 C CB  . ILE B  322 ? 0.19300 0.33000 0.40970 -0.03280 0.00070  -0.00780 316 ILE B CB  
5073 C CG1 . ILE B  322 ? 0.20590 0.34330 0.42570 -0.02440 0.01630  0.00430  316 ILE B CG1 
5074 C CG2 . ILE B  322 ? 0.15830 0.32300 0.37750 -0.02290 -0.01480 -0.01160 316 ILE B CG2 
5075 C CD1 . ILE B  322 ? 0.18100 0.30060 0.37140 -0.00770 0.01830  0.01130  316 ILE B CD1 
5076 N N   . GLY B  323 ? 0.32800 0.51020 0.60020 -0.07320 -0.02330 -0.03820 317 GLY B N   
5077 C CA  . GLY B  323 ? 0.34110 0.52660 0.61270 -0.08470 -0.03930 -0.05370 317 GLY B CA  
5078 C C   . GLY B  323 ? 0.41560 0.59590 0.70950 -0.10980 -0.03370 -0.06270 317 GLY B C   
5079 O O   . GLY B  323 ? 0.39430 0.57030 0.70620 -0.11800 -0.01640 -0.05590 317 GLY B O   
5080 N N   . SER B  324 ? 0.38270 0.56110 0.67270 -0.12180 -0.04760 -0.07820 318 SER B N   
5081 C CA  . SER B  324 ? 0.46850 0.62120 0.75600 -0.14220 -0.04170 -0.08500 318 SER B CA  
5082 C C   . SER B  324 ? 0.53480 0.63990 0.78690 -0.14160 -0.04000 -0.09100 318 SER B C   
5083 O O   . SER B  324 ? 0.46780 0.56590 0.69480 -0.12570 -0.04830 -0.09080 318 SER B O   
5084 C CB  . SER B  324 ? 0.45350 0.63290 0.75370 -0.15490 -0.05840 -0.09580 318 SER B CB  
5085 O OG  . SER B  324 ? 0.51780 0.71240 0.80210 -0.14330 -0.07880 -0.10280 318 SER B OG  
5086 N N   . PRO B  325 ? 0.66850 0.73650 0.91060 -0.15470 -0.02760 -0.09240 319 PRO B N   
5087 C CA  . PRO B  325 ? 0.66280 0.68690 0.86930 -0.15330 -0.02770 -0.09910 319 PRO B CA  
5088 C C   . PRO B  325 ? 0.66060 0.69300 0.85190 -0.15280 -0.04880 -0.11350 319 PRO B C   
5089 O O   . PRO B  325 ? 0.69260 0.69940 0.85370 -0.14290 -0.05170 -0.11740 319 PRO B O   
5090 C CB  . PRO B  325 ? 0.63620 0.62730 0.83930 -0.16830 -0.01310 -0.09870 319 PRO B CB  
5091 C CG  . PRO B  325 ? 0.64900 0.65490 0.87830 -0.17060 0.00190  -0.08610 319 PRO B CG  
5092 C CD  . PRO B  325 ? 0.63010 0.69020 0.88900 -0.16730 -0.01030 -0.08560 319 PRO B CD  
5093 N N   . ASP B  326 ? 0.51630 0.58480 0.72670 -0.16140 -0.06360 -0.12030 320 ASP B N   
5094 C CA  . ASP B  326 ? 0.49350 0.57140 0.68660 -0.15940 -0.08480 -0.13280 320 ASP B CA  
5095 C C   . ASP B  326 ? 0.53580 0.63630 0.71990 -0.13730 -0.09570 -0.12960 320 ASP B C   
5096 O O   . ASP B  326 ? 0.51850 0.60500 0.67150 -0.12780 -0.10570 -0.13660 320 ASP B O   
5097 C CB  . ASP B  326 ? 0.60230 0.71310 0.81990 -0.17480 -0.09750 -0.13950 320 ASP B CB  
5098 C CG  . ASP B  326 ? 0.60940 0.70970 0.84920 -0.19520 -0.08370 -0.13790 320 ASP B CG  
5099 O OD1 . ASP B  326 ? 0.58560 0.68930 0.84470 -0.19390 -0.06640 -0.12540 320 ASP B OD1 
5100 O OD2 . ASP B  326 ? 0.72470 0.81120 0.96080 -0.21220 -0.08970 -0.14900 320 ASP B OD2 
5101 N N   . VAL B  327 ? 0.50590 0.63920 0.71470 -0.12760 -0.09290 -0.11830 321 VAL B N   
5102 C CA  . VAL B  327 ? 0.46160 0.61350 0.66070 -0.10480 -0.10180 -0.11330 321 VAL B CA  
5103 C C   . VAL B  327 ? 0.43580 0.54510 0.59790 -0.08970 -0.09010 -0.10350 321 VAL B C   
5104 O O   . VAL B  327 ? 0.43620 0.53550 0.56830 -0.07520 -0.09740 -0.10410 321 VAL B O   
5105 C CB  . VAL B  327 ? 0.38370 0.57430 0.61300 -0.09610 -0.09790 -0.10020 321 VAL B CB  
5106 C CG1 . VAL B  327 ? 0.31060 0.49520 0.51460 -0.06940 -0.09510 -0.08590 321 VAL B CG1 
5107 C CG2 . VAL B  327 ? 0.41290 0.64600 0.66310 -0.09970 -0.11120 -0.10220 321 VAL B CG2 
5108 N N   . ARG B  328 ? 0.48190 0.56680 0.64600 -0.09240 -0.07140 -0.09370 322 ARG B N   
5109 C CA  . ARG B  328 ? 0.46970 0.52040 0.60380 -0.07810 -0.06090 -0.08350 322 ARG B CA  
5110 C C   . ARG B  328 ? 0.47930 0.49350 0.58400 -0.08030 -0.06150 -0.09250 322 ARG B C   
5111 O O   . ARG B  328 ? 0.47500 0.46780 0.55420 -0.06590 -0.05670 -0.08570 322 ARG B O   
5112 C CB  . ARG B  328 ? 0.39050 0.42750 0.53360 -0.07910 -0.04240 -0.07070 322 ARG B CB  
5113 C CG  . ARG B  328 ? 0.39890 0.46440 0.56070 -0.07030 -0.03890 -0.05880 322 ARG B CG  
5114 C CD  . ARG B  328 ? 0.28740 0.33660 0.45280 -0.07040 -0.02060 -0.04660 322 ARG B CD  
5115 N NE  . ARG B  328 ? 0.40890 0.43930 0.58360 -0.08760 -0.01040 -0.05070 322 ARG B NE  
5116 C CZ  . ARG B  328 ? 0.41300 0.45650 0.61610 -0.10010 -0.00170 -0.04950 322 ARG B CZ  
5117 N NH1 . ARG B  328 ? 0.31240 0.38850 0.53780 -0.09590 -0.00070 -0.04300 322 ARG B NH1 
5118 N NH2 . ARG B  328 ? 0.37350 0.39500 0.58230 -0.11690 0.00820  -0.05430 322 ARG B NH2 
5119 N N   . SER B  329 ? 0.48660 0.49310 0.59430 -0.09800 -0.06670 -0.10800 323 SER B N   
5120 C CA  . SER B  329 ? 0.49540 0.46250 0.57150 -0.09910 -0.06530 -0.11680 323 SER B CA  
5121 C C   . SER B  329 ? 0.50230 0.47070 0.55000 -0.08490 -0.07880 -0.12220 323 SER B C   
5122 O O   . SER B  329 ? 0.46870 0.40300 0.48550 -0.07930 -0.07490 -0.12560 323 SER B O   
5123 C CB  . SER B  329 ? 0.47690 0.43100 0.56090 -0.12310 -0.06670 -0.13340 323 SER B CB  
5124 O OG  . SER B  329 ? 0.59090 0.56940 0.67480 -0.12870 -0.08640 -0.14620 323 SER B OG  
5125 N N   . GLN B  330 ? 0.40970 0.41530 0.46550 -0.07750 -0.09320 -0.12240 324 GLN B N   
5126 C CA  . GLN B  330 ? 0.41190 0.41680 0.43800 -0.05930 -0.10210 -0.12250 324 GLN B CA  
5127 C C   . GLN B  330 ? 0.37130 0.35640 0.37970 -0.04100 -0.08820 -0.10650 324 GLN B C   
5128 O O   . GLN B  330 ? 0.39610 0.36810 0.37570 -0.02690 -0.08950 -0.10570 324 GLN B O   
5129 C CB  . GLN B  330 ? 0.43820 0.48810 0.47840 -0.05290 -0.11840 -0.12310 324 GLN B CB  
5130 C CG  . GLN B  330 ? 0.37800 0.45890 0.45070 -0.07350 -0.13070 -0.13620 324 GLN B CG  
5131 C CD  . GLN B  330 ? 0.47400 0.60090 0.55880 -0.06490 -0.14650 -0.13450 324 GLN B CD  
5132 O OE1 . GLN B  330 ? 0.44820 0.58110 0.51200 -0.04380 -0.15230 -0.12910 324 GLN B OE1 
5133 N NE2 . GLN B  330 ? 0.44660 0.60350 0.56320 -0.07980 -0.15100 -0.13620 324 GLN B NE2 
5134 N N   . LEU B  331 ? 0.31320 0.29570 0.33790 -0.04160 -0.07460 -0.09410 325 LEU B N   
5135 C CA  . LEU B  331 ? 0.33580 0.30380 0.34880 -0.02700 -0.06270 -0.07980 325 LEU B CA  
5136 C C   . LEU B  331 ? 0.33540 0.26890 0.33800 -0.02930 -0.04930 -0.07760 325 LEU B C   
5137 O O   . LEU B  331 ? 0.26960 0.19560 0.26980 -0.01980 -0.03930 -0.06540 325 LEU B O   
5138 C CB  . LEU B  331 ? 0.29480 0.28350 0.32940 -0.02370 -0.05780 -0.06730 325 LEU B CB  
5139 C CG  . LEU B  331 ? 0.27560 0.29850 0.32170 -0.01860 -0.06860 -0.06700 325 LEU B CG  
5140 C CD1 . LEU B  331 ? 0.20120 0.23620 0.26420 -0.01500 -0.06040 -0.05460 325 LEU B CD1 
5141 C CD2 . LEU B  331 ? 0.27680 0.29910 0.29830 -0.00300 -0.07480 -0.06640 325 LEU B CD2 
5142 N N   . ALA B  332 ? 0.35810 0.27110 0.35510 -0.04180 -0.04890 -0.08930 326 ALA B N   
5143 C CA  . ALA B  332 ? 0.37930 0.25790 0.36740 -0.04350 -0.03440 -0.08630 326 ALA B CA  
5144 C C   . ALA B  332 ? 0.38530 0.24470 0.34950 -0.02590 -0.02700 -0.07870 326 ALA B C   
5145 O O   . ALA B  332 ? 0.37190 0.21510 0.33470 -0.02040 -0.01450 -0.06890 326 ALA B O   
5146 C CB  . ALA B  332 ? 0.40060 0.25590 0.38230 -0.05990 -0.03490 -0.10190 326 ALA B CB  
5147 N N   . SER B  333 ? 0.36830 0.22900 0.31320 -0.01650 -0.03390 -0.08290 327 SER B N   
5148 C CA  . SER B  333 ? 0.38490 0.22930 0.30990 -0.00020 -0.02500 -0.07520 327 SER B CA  
5149 C C   . SER B  333 ? 0.38410 0.24560 0.32310 0.00950  -0.01950 -0.05930 327 SER B C   
5150 O O   . SER B  333 ? 0.35450 0.20520 0.28700 0.02010  -0.00960 -0.05070 327 SER B O   
5151 C CB  . SER B  333 ? 0.41860 0.26060 0.31870 0.00860  -0.03200 -0.08200 327 SER B CB  
5152 O OG  . SER B  333 ? 0.43820 0.30990 0.34670 0.01330  -0.04110 -0.07820 327 SER B OG  
5153 N N   . PHE B  334 ? 0.29550 0.18440 0.25310 0.00650  -0.02610 -0.05580 328 PHE B N   
5154 C CA  . PHE B  334 ? 0.29250 0.19480 0.26220 0.01330  -0.02120 -0.04260 328 PHE B CA  
5155 C C   . PHE B  334 ? 0.28810 0.18670 0.27210 0.00800  -0.01410 -0.03630 328 PHE B C   
5156 O O   . PHE B  334 ? 0.27600 0.17460 0.26260 0.01500  -0.00780 -0.02630 328 PHE B O   
5157 C CB  . PHE B  334 ? 0.28670 0.21510 0.26640 0.01400  -0.02930 -0.04110 328 PHE B CB  
5158 C CG  . PHE B  334 ? 0.26710 0.19940 0.23020 0.02300  -0.03510 -0.04400 328 PHE B CG  
5159 C CD1 . PHE B  334 ? 0.32830 0.25650 0.28100 0.03480  -0.02870 -0.03600 328 PHE B CD1 
5160 C CD2 . PHE B  334 ? 0.30870 0.24980 0.26690 0.01980  -0.04670 -0.05440 328 PHE B CD2 
5161 C CE1 . PHE B  334 ? 0.31450 0.24300 0.24880 0.04450  -0.03180 -0.03740 328 PHE B CE1 
5162 C CE2 . PHE B  334 ? 0.31880 0.26230 0.25770 0.03040  -0.05230 -0.05640 328 PHE B CE2 
5163 C CZ  . PHE B  334 ? 0.33170 0.26710 0.25720 0.04350  -0.04370 -0.04710 328 PHE B CZ  
5164 N N   . HIS B  335 ? 0.26290 0.15930 0.25640 -0.00430 -0.01510 -0.04210 329 HIS B N   
5165 C CA  . HIS B  335 ? 0.26920 0.16100 0.27440 -0.00910 -0.00720 -0.03560 329 HIS B CA  
5166 C C   . HIS B  335 ? 0.28810 0.15480 0.28160 -0.00220 0.00350  -0.02980 329 HIS B C   
5167 O O   . HIS B  335 ? 0.27170 0.13980 0.26910 0.00370  0.00900  -0.01920 329 HIS B O   
5168 C CB  . HIS B  335 ? 0.32290 0.21430 0.34010 -0.02490 -0.00840 -0.04410 329 HIS B CB  
5169 C CG  . HIS B  335 ? 0.30460 0.19400 0.33490 -0.02990 0.00060  -0.03660 329 HIS B CG  
5170 N ND1 . HIS B  335 ? 0.33510 0.22220 0.37910 -0.04490 0.00390  -0.04190 329 HIS B ND1 
5171 C CD2 . HIS B  335 ? 0.28760 0.17710 0.31850 -0.02180 0.00730  -0.02430 329 HIS B CD2 
5172 C CE1 . HIS B  335 ? 0.36500 0.24790 0.41560 -0.04460 0.01420  -0.03200 329 HIS B CE1 
5173 N NE2 . HIS B  335 ? 0.24270 0.12650 0.28350 -0.03010 0.01550  -0.02150 329 HIS B NE2 
5174 N N   . HIS B  336 ? 0.19760 0.28850 0.26720 0.08640  -0.03100 -0.04490 330 HIS B N   
5175 C CA  . HIS B  336 ? 0.22080 0.28690 0.30640 0.05770  -0.02300 -0.03260 330 HIS B CA  
5176 C C   . HIS B  336 ? 0.26000 0.30100 0.32350 0.07040  -0.02190 -0.02220 330 HIS B C   
5177 O O   . HIS B  336 ? 0.22020 0.28310 0.29050 0.07580  -0.02640 -0.03420 330 HIS B O   
5178 C CB  . HIS B  336 ? 0.20840 0.30480 0.32940 0.03290  -0.01990 -0.05160 330 HIS B CB  
5179 C CG  . HIS B  336 ? 0.19590 0.31530 0.33480 0.01970  -0.01590 -0.06550 330 HIS B CG  
5180 N ND1 . HIS B  336 ? 0.24590 0.42170 0.40280 0.02610  -0.02000 -0.09710 330 HIS B ND1 
5181 C CD2 . HIS B  336 ? 0.18290 0.27950 0.32290 0.00280  -0.00780 -0.05440 330 HIS B CD2 
5182 C CE1 . HIS B  336 ? 0.21810 0.40260 0.38860 0.00940  -0.01200 -0.10470 330 HIS B CE1 
5183 N NE2 . HIS B  336 ? 0.23080 0.36360 0.38800 -0.00360 -0.00460 -0.07670 330 HIS B NE2 
5184 N N   . PRO B  337 ? 0.30840 0.30350 0.34480 0.07430  -0.01300 -0.00280 331 PRO B N   
5185 C CA  . PRO B  337 ? 0.34310 0.30710 0.35250 0.08560  -0.00580 0.00620  331 PRO B CA  
5186 C C   . PRO B  337 ? 0.28510 0.25870 0.31950 0.06820  -0.00680 0.00440  331 PRO B C   
5187 O O   . PRO B  337 ? 0.30300 0.28210 0.36540 0.04450  -0.00650 0.00530  331 PRO B O   
5188 C CB  . PRO B  337 ? 0.32420 0.24020 0.31400 0.07660  0.01080  0.02110  331 PRO B CB  
5189 C CG  . PRO B  337 ? 0.33800 0.25700 0.32510 0.07950  0.00880  0.02040  331 PRO B CG  
5190 C CD  . PRO B  337 ? 0.22830 0.19870 0.25400 0.07010  -0.00630 0.00720  331 PRO B CD  
5191 N N   . GLN B  338 ? 0.33210 0.30380 0.34950 0.08460  -0.00750 0.00200  332 GLN B N   
5192 C CA  . GLN B  338 ? 0.31620 0.29410 0.35270 0.07140  -0.00770 0.00020  332 GLN B CA  
5193 C C   . GLN B  338 ? 0.32430 0.27310 0.36600 0.05160  0.00380  0.01250  332 GLN B C   
5194 O O   . GLN B  338 ? 0.31550 0.23190 0.33480 0.05290  0.01710  0.02080  332 GLN B O   
5195 C CB  . GLN B  338 ? 0.35710 0.33350 0.36720 0.09620  -0.00910 -0.00340 332 GLN B CB  
5196 C CG  . GLN B  338 ? 0.47600 0.49770 0.48490 0.12070  -0.02390 -0.02440 332 GLN B CG  
5197 C CD  . GLN B  338 ? 0.48990 0.55890 0.54580 0.09920  -0.03130 -0.04580 332 GLN B CD  
5198 O OE1 . GLN B  338 ? 0.53670 0.63920 0.61750 0.08940  -0.03520 -0.06210 332 GLN B OE1 
5199 N NE2 . GLN B  338 ? 0.39540 0.46300 0.46140 0.09010  -0.02960 -0.04740 332 GLN B NE2 
5200 N N   . ARG B  339 ? 0.26000 0.22120 0.32960 0.03430  0.00060  0.01010  333 ARG B N   
5201 C CA  . ARG B  339 ? 0.29020 0.23980 0.36910 0.02100  0.00730  0.01470  333 ARG B CA  
5202 C C   . ARG B  339 ? 0.32260 0.27900 0.41020 0.02040  0.00480  0.01120  333 ARG B C   
5203 O O   . ARG B  339 ? 0.27040 0.23400 0.37360 0.01310  0.00050  0.00920  333 ARG B O   
5204 C CB  . ARG B  339 ? 0.30740 0.26390 0.40330 0.00930  0.00400  0.01510  333 ARG B CB  
5205 C CG  . ARG B  339 ? 0.26370 0.21180 0.35280 0.00710  0.00900  0.01770  333 ARG B CG  
5206 C CD  . ARG B  339 ? 0.28440 0.21420 0.36350 0.00290  0.02420  0.01680  333 ARG B CD  
5207 N NE  . ARG B  339 ? 0.32540 0.24240 0.39700 -0.00240 0.03330  0.01650  333 ARG B NE  
5208 C CZ  . ARG B  339 ? 0.34630 0.23480 0.38750 0.00720  0.04300  0.02180  333 ARG B CZ  
5209 N NH1 . ARG B  339 ? 0.34770 0.22140 0.36070 0.02720  0.04280  0.02700  333 ARG B NH1 
5210 N NH2 . ARG B  339 ? 0.33770 0.21120 0.37250 -0.00020 0.05360  0.02010  333 ARG B NH2 
5211 N N   . VAL B  340 ? 0.30270 0.25140 0.37330 0.03140  0.00890  0.01100  334 VAL B N   
5212 C CA  . VAL B  340 ? 0.27330 0.22950 0.35020 0.03280  0.00630  0.00660  334 VAL B CA  
5213 C C   . VAL B  340 ? 0.31230 0.25200 0.38200 0.02960  0.01910  0.00940  334 VAL B C   
5214 O O   . VAL B  340 ? 0.30900 0.22330 0.35240 0.03450  0.03350  0.01350  334 VAL B O   
5215 C CB  . VAL B  340 ? 0.31380 0.28210 0.37750 0.05020  0.00000  -0.00080 334 VAL B CB  
5216 C CG1 . VAL B  340 ? 0.29160 0.26670 0.36070 0.05130  -0.00150 -0.00630 334 VAL B CG1 
5217 C CG2 . VAL B  340 ? 0.35960 0.35620 0.43860 0.04890  -0.00980 -0.01290 334 VAL B CG2 
5218 N N   . ASN B  341 ? 0.29940 0.25020 0.38860 0.02190  0.01720  0.00530  335 ASN B N   
5219 C CA  . ASN B  341 ? 0.24010 0.18710 0.33170 0.01500  0.03020  0.00120  335 ASN B CA  
5220 C C   . ASN B  341 ? 0.26230 0.19660 0.33510 0.02370  0.03730  0.00190  335 ASN B C   
5221 O O   . ASN B  341 ? 0.24150 0.17220 0.29720 0.03830  0.03060  0.00480  335 ASN B O   
5222 C CB  . ASN B  341 ? 0.20430 0.17580 0.32260 0.00970  0.02290  -0.00710 335 ASN B CB  
5223 C CG  . ASN B  341 ? 0.22380 0.20180 0.34640 0.01810  0.01170  -0.00760 335 ASN B CG  
5224 O OD1 . ASN B  341 ? 0.25610 0.22670 0.36920 0.02330  0.01040  -0.00550 335 ASN B OD1 
5225 N ND2 . ASN B  341 ? 0.22530 0.21630 0.35850 0.02220  0.00460  -0.01250 335 ASN B ND2 
5226 N N   . THR B  342 ? 0.26320 0.19560 0.33960 0.01600  0.05110  -0.00440 336 THR B N   
5227 C CA  . THR B  342 ? 0.27840 0.19140 0.33020 0.02440  0.06240  -0.00280 336 THR B CA  
5228 C C   . THR B  342 ? 0.29600 0.22800 0.35700 0.03460  0.04560  -0.00460 336 THR B C   
5229 O O   . THR B  342 ? 0.32210 0.24200 0.36140 0.04570  0.05080  -0.00350 336 THR B O   
5230 C CB  . THR B  342 ? 0.27710 0.18310 0.33260 0.00810  0.08730  -0.01310 336 THR B CB  
5231 O OG1 . THR B  342 ? 0.24520 0.19390 0.34190 -0.00020 0.07620  -0.02670 336 THR B OG1 
5232 C CG2 . THR B  342 ? 0.30960 0.19070 0.35410 -0.00790 0.11230  -0.01650 336 THR B CG2 
5233 N N   . MET B  343 ? 0.23190 0.18720 0.31880 0.03220  0.02840  -0.00770 337 MET B N   
5234 C CA  . MET B  343 ? 0.28870 0.25390 0.38140 0.03870  0.01740  -0.01150 337 MET B CA  
5235 C C   . MET B  343 ? 0.30980 0.28070 0.40400 0.04120  0.00620  -0.01320 337 MET B C   
5236 O O   . MET B  343 ? 0.25970 0.23600 0.36270 0.03990  0.00080  -0.01990 337 MET B O   
5237 C CB  . MET B  343 ? 0.26080 0.23800 0.37300 0.03560  0.01330  -0.01690 337 MET B CB  
5238 C CG  . MET B  343 ? 0.24450 0.23100 0.36370 0.03220  0.02420  -0.02420 337 MET B CG  
5239 S SD  . MET B  343 ? 0.32360 0.29680 0.42260 0.03770  0.03530  -0.02410 337 MET B SD  
5240 C CE  . MET B  343 ? 0.31130 0.29480 0.41920 0.04690  0.02030  -0.02850 337 MET B CE  
5241 N N   . GLY B  344 ? 0.28350 0.25260 0.36910 0.04340  0.00570  -0.01010 338 GLY B N   
5242 C CA  . GLY B  344 ? 0.31400 0.29810 0.40360 0.04550  -0.00280 -0.01810 338 GLY B CA  
5243 C C   . GLY B  344 ? 0.29790 0.28210 0.40450 0.03120  -0.00450 -0.01930 338 GLY B C   
5244 O O   . GLY B  344 ? 0.29450 0.29160 0.40910 0.02640  -0.00660 -0.03110 338 GLY B O   
5245 N N   . VAL B  345 ? 0.25230 0.22420 0.36260 0.02550  -0.00200 -0.01080 339 VAL B N   
5246 C CA  . VAL B  345 ? 0.31340 0.27570 0.42790 0.01850  -0.00190 -0.00920 339 VAL B CA  
5247 C C   . VAL B  345 ? 0.28420 0.24800 0.39840 0.01580  -0.00250 -0.00370 339 VAL B C   
5248 O O   . VAL B  345 ? 0.23990 0.20580 0.35290 0.01740  -0.00100 0.00100  339 VAL B O   
5249 C CB  . VAL B  345 ? 0.27950 0.23220 0.39200 0.02360  -0.00200 -0.00600 339 VAL B CB  
5250 C CG1 . VAL B  345 ? 0.31860 0.25070 0.42010 0.02470  -0.00040 -0.00230 339 VAL B CG1 
5251 C CG2 . VAL B  345 ? 0.31840 0.26750 0.42910 0.02760  -0.00090 -0.01120 339 VAL B CG2 
5252 N N   . THR B  346 ? 0.27780 0.23860 0.39310 0.00900  -0.00130 -0.00660 340 THR B N   
5253 C CA  . THR B  346 ? 0.28000 0.24150 0.39460 0.00660  -0.00200 -0.00150 340 THR B CA  
5254 C C   . THR B  346 ? 0.25970 0.20930 0.36980 0.00900  -0.00240 0.00590  340 THR B C   
5255 O O   . THR B  346 ? 0.28990 0.22090 0.38960 0.01190  0.00030  0.00690  340 THR B O   
5256 C CB  . THR B  346 ? 0.28240 0.24800 0.40080 -0.00230 0.00140  -0.01040 340 THR B CB  
5257 O OG1 . THR B  346 ? 0.30910 0.30100 0.43370 0.00180  -0.00230 -0.02340 340 THR B OG1 
5258 C CG2 . THR B  346 ? 0.26390 0.22830 0.38040 -0.00420 0.00090  -0.00440 340 THR B CG2 
5259 N N   . THR B  347 ? 0.23780 0.19660 0.35150 0.01030  -0.00430 0.00880  341 THR B N   
5260 C CA  . THR B  347 ? 0.22140 0.18460 0.33540 0.01620  -0.00740 0.00830  341 THR B CA  
5261 C C   . THR B  347 ? 0.22720 0.18760 0.33650 0.01570  -0.00880 0.01140  341 THR B C   
5262 O O   . THR B  347 ? 0.24370 0.21050 0.34910 0.02590  -0.01350 0.00890  341 THR B O   
5263 C CB  . THR B  347 ? 0.24660 0.23000 0.37370 0.01420  -0.00510 0.00060  341 THR B CB  
5264 O OG1 . THR B  347 ? 0.25080 0.22990 0.37720 0.00500  0.00280  0.00220  341 THR B OG1 
5265 C CG2 . THR B  347 ? 0.27760 0.26380 0.40740 0.01690  -0.00320 -0.00320 341 THR B CG2 
5266 N N   . GLY B  348 ? 0.27210 0.22790 0.38080 0.00750  -0.00600 0.01430  342 GLY B N   
5267 C CA  . GLY B  348 ? 0.23870 0.19350 0.34410 0.00630  -0.00670 0.01680  342 GLY B CA  
5268 C C   . GLY B  348 ? 0.23510 0.19200 0.34270 -0.00100 -0.00420 0.01690  342 GLY B C   
5269 O O   . GLY B  348 ? 0.24170 0.20290 0.35150 -0.00230 -0.00310 0.01280  342 GLY B O   
5270 N N   . GLY B  349 ? 0.25010 0.20910 0.35680 -0.00250 -0.00460 0.01860  343 GLY B N   
5271 C CA  . GLY B  349 ? 0.27240 0.23630 0.37900 -0.00480 -0.00340 0.01700  343 GLY B CA  
5272 C C   . GLY B  349 ? 0.24040 0.20430 0.34450 -0.00530 -0.00340 0.01950  343 GLY B C   
5273 O O   . GLY B  349 ? 0.23260 0.19700 0.33850 -0.00570 -0.00370 0.01950  343 GLY B O   
5274 N N   . VAL B  350 ? 0.24430 0.21360 0.34640 -0.00470 -0.00320 0.01730  344 VAL B N   
5275 C CA  A VAL B  350 ? 0.23150 0.19930 0.32900 -0.00390 -0.00250 0.01910  344 VAL B CA  
5276 C CA  B VAL B  350 ? 0.23150 0.19920 0.32910 -0.00400 -0.00250 0.01920  344 VAL B CA  
5277 C C   . VAL B  350 ? 0.23170 0.20380 0.33190 -0.00950 -0.00230 0.01740  344 VAL B C   
5278 O O   . VAL B  350 ? 0.27090 0.25050 0.37610 -0.01440 0.00060  0.01030  344 VAL B O   
5279 C CB  A VAL B  350 ? 0.23480 0.20130 0.31910 0.00770  -0.00130 0.01780  344 VAL B CB  
5280 C CB  B VAL B  350 ? 0.23510 0.20060 0.31930 0.00740  -0.00100 0.01810  344 VAL B CB  
5281 C CG1 A VAL B  350 ? 0.24580 0.23680 0.33430 0.01460  -0.00640 0.00730  344 VAL B CG1 
5282 C CG1 B VAL B  350 ? 0.19370 0.15480 0.27030 0.00930  0.00070  0.01930  344 VAL B CG1 
5283 C CG2 A VAL B  350 ? 0.20050 0.15480 0.27480 0.00840  0.00310  0.02080  344 VAL B CG2 
5284 C CG2 B VAL B  350 ? 0.24390 0.18940 0.31460 0.01170  0.00640  0.02160  344 VAL B CG2 
5285 N N   . SER B  351 ? 0.20880 0.17610 0.30530 -0.01070 -0.00240 0.02090  345 SER B N   
5286 C CA  A SER B  351 ? 0.21090 0.17680 0.30390 -0.01480 0.00060  0.02040  345 SER B CA  
5287 C CA  B SER B  351 ? 0.21150 0.17670 0.30410 -0.01470 0.00050  0.02070  345 SER B CA  
5288 C C   . SER B  351 ? 0.21660 0.18700 0.30780 -0.01260 -0.00110 0.02060  345 SER B C   
5289 O O   . SER B  351 ? 0.16900 0.13710 0.25910 -0.00970 -0.00190 0.02120  345 SER B O   
5290 C CB  A SER B  351 ? 0.25050 0.19840 0.33000 -0.01320 0.00320  0.02540  345 SER B CB  
5291 C CB  B SER B  351 ? 0.24880 0.19730 0.32790 -0.01170 0.00180  0.02600  345 SER B CB  
5292 O OG  A SER B  351 ? 0.24660 0.19960 0.32520 -0.00470 -0.00430 0.02650  345 SER B OG  
5293 O OG  B SER B  351 ? 0.24290 0.17840 0.31620 -0.01070 0.00510  0.02710  345 SER B OG  
5294 N N   . PHE B  352 ? 0.19220 0.16590 0.28190 -0.01630 0.00230  0.01810  346 PHE B N   
5295 C CA  . PHE B  352 ? 0.20310 0.18310 0.29100 -0.01340 0.00110  0.01660  346 PHE B CA  
5296 C C   . PHE B  352 ? 0.22430 0.19690 0.30440 -0.01660 0.00390  0.01940  346 PHE B C   
5297 O O   . PHE B  352 ? 0.22160 0.19940 0.30150 -0.02110 0.00930  0.01490  346 PHE B O   
5298 C CB  . PHE B  352 ? 0.17350 0.17490 0.26790 -0.01060 0.00150  0.00570  346 PHE B CB  
5299 C CG  . PHE B  352 ? 0.17660 0.18600 0.27050 0.00060  -0.00290 0.00200  346 PHE B CG  
5300 C CD1 . PHE B  352 ? 0.19210 0.18500 0.26840 0.01470  -0.00410 0.00830  346 PHE B CD1 
5301 C CD2 . PHE B  352 ? 0.17480 0.20340 0.28090 -0.00260 -0.00240 -0.00930 346 PHE B CD2 
5302 C CE1 . PHE B  352 ? 0.20970 0.20120 0.27430 0.02990  -0.00570 0.00670  346 PHE B CE1 
5303 C CE2 . PHE B  352 ? 0.16470 0.20320 0.26690 0.01210  -0.00800 -0.01390 346 PHE B CE2 
5304 C CZ  . PHE B  352 ? 0.17250 0.19030 0.25080 0.03050  -0.01010 -0.00410 346 PHE B CZ  
5305 N N   . PRO B  353 ? 0.20780 0.17230 0.28040 -0.01210 0.00030  0.02370  347 PRO B N   
5306 C CA  . PRO B  353 ? 0.23380 0.19300 0.29270 -0.00800 0.00060  0.02540  347 PRO B CA  
5307 C C   . PRO B  353 ? 0.20450 0.17490 0.26920 -0.00860 -0.00190 0.02120  347 PRO B C   
5308 O O   . PRO B  353 ? 0.19790 0.17610 0.26430 -0.00550 -0.00640 0.01610  347 PRO B O   
5309 C CB  . PRO B  353 ? 0.22280 0.18090 0.27230 0.00400  -0.00590 0.02560  347 PRO B CB  
5310 C CG  . PRO B  353 ? 0.28060 0.25270 0.34970 0.00040  -0.00990 0.02000  347 PRO B CG  
5311 C CD  . PRO B  353 ? 0.19920 0.16630 0.27630 -0.00830 -0.00470 0.02280  347 PRO B CD  
5312 N N   . PHE B  354 ? 0.22140 0.19590 0.28980 -0.01230 0.00180  0.01950  348 PHE B N   
5313 C CA  . PHE B  354 ? 0.23060 0.20970 0.29730 -0.01060 0.00160  0.01660  348 PHE B CA  
5314 C C   . PHE B  354 ? 0.21500 0.20000 0.28010 -0.01440 0.00760  0.01380  348 PHE B C   
5315 O O   . PHE B  354 ? 0.24430 0.23170 0.31330 -0.02130 0.01450  0.01030  348 PHE B O   
5316 C CB  . PHE B  354 ? 0.23680 0.21370 0.30380 -0.00590 0.00180  0.01410  348 PHE B CB  
5317 C CG  . PHE B  354 ? 0.22250 0.20680 0.29050 0.00090  0.00140  0.01170  348 PHE B CG  
5318 C CD1 . PHE B  354 ? 0.19780 0.20320 0.26940 0.00560  0.00070  0.00350  348 PHE B CD1 
5319 C CD2 . PHE B  354 ? 0.24950 0.22440 0.31410 0.00530  0.00170  0.01380  348 PHE B CD2 
5320 C CE1 . PHE B  354 ? 0.19650 0.22110 0.27040 0.01710  -0.00250 -0.00560 348 PHE B CE1 
5321 C CE2 . PHE B  354 ? 0.18700 0.17190 0.24800 0.01760  -0.00070 0.00940  348 PHE B CE2 
5322 C CZ  . PHE B  354 ? 0.18090 0.19420 0.24730 0.02510  -0.00420 -0.00170 348 PHE B CZ  
5323 N N   . LYS B  355 ? 0.18600 0.17450 0.24700 -0.01240 0.00770  0.01190  349 LYS B N   
5324 C CA  . LYS B  355 ? 0.22610 0.22020 0.28500 -0.01820 0.01630  0.00720  349 LYS B CA  
5325 C C   . LYS B  355 ? 0.20270 0.21380 0.26620 -0.01190 0.01310  0.00010  349 LYS B C   
5326 O O   . LYS B  355 ? 0.19120 0.19520 0.24710 -0.00620 0.00910  0.00290  349 LYS B O   
5327 C CB  . LYS B  355 ? 0.25370 0.22650 0.29120 -0.01810 0.02200  0.01420  349 LYS B CB  
5328 C CG  . LYS B  355 ? 0.31290 0.28320 0.34180 -0.02470 0.03500  0.01010  349 LYS B CG  
5329 C CD  . LYS B  355 ? 0.36240 0.29530 0.35600 -0.02180 0.04720  0.01950  349 LYS B CD  
5330 C CE  . LYS B  355 ? 0.44320 0.36350 0.42200 -0.03160 0.06760  0.01530  349 LYS B CE  
5331 N NZ  . LYS B  355 ? 0.47780 0.35200 0.40690 -0.01910 0.07870  0.02770  349 LYS B NZ  
5332 N N   . LEU B  356 ? 0.24330 0.27980 0.31910 -0.01120 0.01500  -0.01260 350 LEU B N   
5333 C CA  . LEU B  356 ? 0.20250 0.25820 0.27830 0.00160  0.01080  -0.02140 350 LEU B CA  
5334 C C   . LEU B  356 ? 0.26380 0.31810 0.33510 -0.00440 0.01660  -0.02190 350 LEU B C   
5335 O O   . LEU B  356 ? 0.25740 0.30880 0.32950 -0.01960 0.02840  -0.02390 350 LEU B O   
5336 C CB  . LEU B  356 ? 0.18790 0.28570 0.28100 0.00630  0.01020  -0.04230 350 LEU B CB  
5337 C CG  . LEU B  356 ? 0.29330 0.41560 0.38020 0.03370  0.00040  -0.05370 350 LEU B CG  
5338 C CD1 . LEU B  356 ? 0.20460 0.29200 0.26420 0.05500  -0.00630 -0.03880 350 LEU B CD1 
5339 C CD2 . LEU B  356 ? 0.27110 0.45240 0.38330 0.03650  -0.00070 -0.08320 350 LEU B CD2 
5340 N N   . ARG B  357 ? 0.19800 0.24700 0.25870 0.00770  0.01150  -0.02000 351 ARG B N   
5341 C CA  . ARG B  357 ? 0.23630 0.28860 0.29330 0.00380  0.01620  -0.02260 351 ARG B CA  
5342 C C   . ARG B  357 ? 0.30650 0.38470 0.36540 0.01880  0.01300  -0.03590 351 ARG B C   
5343 O O   . ARG B  357 ? 0.22510 0.29950 0.27310 0.03920  0.00580  -0.03630 351 ARG B O   
5344 C CB  . ARG B  357 ? 0.28690 0.31260 0.32920 0.00370  0.01390  -0.01150 351 ARG B CB  
5345 C CG  . ARG B  357 ? 0.26500 0.27350 0.29870 0.01340  0.00920  -0.00920 351 ARG B CG  
5346 C CD  . ARG B  357 ? 0.30150 0.29650 0.33030 0.00760  0.00850  -0.00720 351 ARG B CD  
5347 N NE  . ARG B  357 ? 0.25140 0.22780 0.27150 0.01070  0.01200  -0.01170 351 ARG B NE  
5348 C CZ  . ARG B  357 ? 0.28770 0.24340 0.30430 0.00840  0.01730  -0.01240 351 ARG B CZ  
5349 N NH1 . ARG B  357 ? 0.28140 0.23800 0.30500 0.00590  0.01550  -0.00790 351 ARG B NH1 
5350 N NH2 . ARG B  357 ? 0.26840 0.19770 0.27230 0.00640  0.02820  -0.01920 351 ARG B NH2 
5351 N N   . GLY B  358 ? 0.29120 0.39290 0.35900 0.01120  0.02060  -0.04790 352 GLY B N   
5352 C CA  . GLY B  358 ? 0.35900 0.49630 0.43200 0.02700  0.01710  -0.06570 352 GLY B CA  
5353 C C   . GLY B  358 ? 0.59820 0.77520 0.69330 0.01000  0.03050  -0.08780 352 GLY B C   
5354 O O   . GLY B  358 ? 0.78050 0.96640 0.87310 0.01110  0.03420  -0.09350 352 GLY B O   
5355 N N   . SER B  359 ? 0.64210 0.84340 0.75920 -0.00740 0.04060  -0.10350 353 SER B N   
5356 C CA  . SER B  359 ? 0.64970 0.87550 0.78680 -0.03620 0.06490  -0.12660 353 SER B CA  
5357 C C   . SER B  359 ? 0.65220 0.90350 0.81420 -0.05390 0.07560  -0.14730 353 SER B C   
5358 O O   . SER B  359 ? 0.69360 0.90790 0.84820 -0.08000 0.09690  -0.14070 353 SER B O   
5359 C CB  . SER B  359 ? 0.66870 0.95050 0.82450 -0.03010 0.06630  -0.15580 353 SER B CB  
5360 O OG  . SER B  359 ? 0.66840 0.96920 0.84360 -0.06440 0.09660  -0.18090 353 SER B OG  
5361 N N   . VAL B  363 ? 0.74460 0.74420 0.73150 -0.07330 0.13650  -0.04920 357 VAL B N   
5362 C CA  . VAL B  363 ? 0.73190 0.68970 0.69890 -0.08790 0.16000  -0.04500 357 VAL B CA  
5363 C C   . VAL B  363 ? 0.73880 0.63060 0.64770 -0.06820 0.15990  -0.01600 357 VAL B C   
5364 O O   . VAL B  363 ? 0.69340 0.52630 0.55810 -0.07500 0.19050  -0.00900 357 VAL B O   
5365 C CB  . VAL B  363 ? 0.67850 0.66870 0.68280 -0.09240 0.14730  -0.05460 357 VAL B CB  
5366 C CG1 . VAL B  363 ? 0.71410 0.77810 0.76930 -0.09750 0.13910  -0.08470 357 VAL B CG1 
5367 C CG2 . VAL B  363 ? 0.67770 0.66330 0.67890 -0.06800 0.11470  -0.03390 357 VAL B CG2 
5368 N N   . ASP B  364 ? 0.68230 0.58360 0.58780 -0.04200 0.12790  -0.00260 358 ASP B N   
5369 C CA  . ASP B  364 ? 0.62160 0.48210 0.47960 -0.01630 0.12000  0.01710  358 ASP B CA  
5370 C C   . ASP B  364 ? 0.61750 0.46250 0.43950 -0.00060 0.12240  0.02190  358 ASP B C   
5371 O O   . ASP B  364 ? 0.57180 0.44150 0.41190 -0.01010 0.12550  0.01160  358 ASP B O   
5372 C CB  . ASP B  364 ? 0.60630 0.49670 0.48840 -0.00030 0.08560  0.02010  358 ASP B CB  
5373 C CG  . ASP B  364 ? 0.57970 0.47970 0.48930 -0.01120 0.08260  0.01800  358 ASP B CG  
5374 O OD1 . ASP B  364 ? 0.67830 0.54190 0.56460 -0.01610 0.10100  0.02340  358 ASP B OD1 
5375 O OD2 . ASP B  364 ? 0.61670 0.55470 0.56560 -0.01330 0.06410  0.01120  358 ASP B OD2 
5376 N N   . ASP B  365 ? 0.51890 0.32530 0.28680 0.02790  0.11940  0.03610  359 ASP B N   
5377 C CA  . ASP B  365 ? 0.57140 0.36770 0.30130 0.05050  0.11650  0.03960  359 ASP B CA  
5378 C C   . ASP B  365 ? 0.48690 0.34550 0.26610 0.05040  0.08760  0.02700  359 ASP B C   
5379 O O   . ASP B  365 ? 0.45510 0.35000 0.27260 0.05130  0.06330  0.02130  359 ASP B O   
5380 C CB  . ASP B  365 ? 0.60080 0.36370 0.26960 0.09180  0.10720  0.05170  359 ASP B CB  
5381 C CG  . ASP B  365 ? 0.68730 0.42060 0.29440 0.11980  0.11430  0.05710  359 ASP B CG  
5382 O OD1 . ASP B  365 ? 0.63040 0.40840 0.26180 0.12430  0.09490  0.04660  359 ASP B OD1 
5383 O OD2 . ASP B  365 ? 0.75430 0.41320 0.28180 0.13920  0.14190  0.07200  359 ASP B OD2 
5384 N N   . PRO B  366 ? 0.49220 0.35910 0.26880 0.04820  0.09280  0.02170  360 PRO B N   
5385 C CA  . PRO B  366 ? 0.44450 0.36120 0.25960 0.05060  0.06760  0.00970  360 PRO B CA  
5386 C C   . PRO B  366 ? 0.43920 0.37450 0.24970 0.07520  0.04120  0.00590  360 PRO B C   
5387 O O   . PRO B  366 ? 0.39960 0.37270 0.24770 0.07110  0.02350  -0.00730 360 PRO B O   
5388 C CB  . PRO B  366 ? 0.46870 0.38010 0.26530 0.05040  0.08070  0.00680  360 PRO B CB  
5389 C CG  . PRO B  366 ? 0.52380 0.39290 0.29180 0.03500  0.11680  0.01240  360 PRO B CG  
5390 C CD  . PRO B  366 ? 0.54680 0.37450 0.28340 0.04190  0.12510  0.02490  360 PRO B CD  
5391 N N   . ARG B  367 ? 0.48460 0.39410 0.24780 0.10170  0.04010  0.01370  361 ARG B N   
5392 C CA  . ARG B  367 ? 0.48370 0.42450 0.24400 0.12900  0.01380  0.00200  361 ARG B CA  
5393 C C   . ARG B  367 ? 0.46770 0.43160 0.26260 0.12370  0.00000  -0.00390 361 ARG B C   
5394 O O   . ARG B  367 ? 0.44820 0.44600 0.24620 0.14440  -0.02030 -0.01920 361 ARG B O   
5395 C CB  . ARG B  367 ? 0.55790 0.46570 0.24340 0.17100  0.01610  0.00990  361 ARG B CB  
5396 C CG  . ARG B  367 ? 0.59360 0.48800 0.24430 0.18180  0.02490  0.01070  361 ARG B CG  
5397 C CD  . ARG B  367 ? 0.68480 0.52680 0.24470 0.22620  0.03480  0.02370  361 ARG B CD  
5398 N NE  . ARG B  367 ? 0.73480 0.50220 0.25030 0.21980  0.06710  0.04640  361 ARG B NE  
5399 C CZ  . ARG B  367 ? 0.82730 0.52390 0.26280 0.25050  0.08750  0.06210  361 ARG B CZ  
5400 N NH1 . ARG B  367 ? 0.87440 0.57130 0.27780 0.29150  0.07510  0.05780  361 ARG B NH1 
5401 N NH2 . ARG B  367 ? 0.86690 0.49780 0.28130 0.23470  0.11890  0.07670  361 ARG B NH2 
5402 N N   . LEU B  368 ? 0.42210 0.37380 0.24360 0.09780  0.01060  0.00430  362 LEU B N   
5403 C CA  . LEU B  368 ? 0.40590 0.37900 0.26280 0.08980  -0.00100 -0.00140 362 LEU B CA  
5404 C C   . LEU B  368 ? 0.36070 0.36790 0.26900 0.06820  -0.00830 -0.01580 362 LEU B C   
5405 O O   . LEU B  368 ? 0.35110 0.35200 0.27650 0.04970  0.00150  -0.01190 362 LEU B O   
5406 C CB  . LEU B  368 ? 0.43470 0.37580 0.28950 0.07570  0.01460  0.01330  362 LEU B CB  
5407 C CG  . LEU B  368 ? 0.46750 0.42780 0.35880 0.06570  0.00460  0.00910  362 LEU B CG  
5408 C CD1 . LEU B  368 ? 0.37250 0.34620 0.25010 0.09100  -0.01130 0.00270  362 LEU B CD1 
5409 C CD2 . LEU B  368 ? 0.49090 0.42620 0.38770 0.04690  0.02120  0.01990  362 LEU B CD2 
5410 N N   . ALA B  369 ? 0.34500 0.38720 0.27480 0.07190  -0.02290 -0.03570 363 ALA B N   
5411 C CA  . ALA B  369 ? 0.31380 0.37210 0.28220 0.05020  -0.02210 -0.04950 363 ALA B CA  
5412 C C   . ALA B  369 ? 0.27970 0.32880 0.27050 0.03440  -0.01770 -0.04450 363 ALA B C   
5413 O O   . ALA B  369 ? 0.30750 0.36040 0.29890 0.03950  -0.02250 -0.04330 363 ALA B O   
5414 C CB  . ALA B  369 ? 0.29520 0.39290 0.27980 0.05350  -0.03220 -0.07930 363 ALA B CB  
5415 N N   . ALA B  370 ? 0.28520 0.32060 0.28930 0.01960  -0.00890 -0.04160 364 ALA B N   
5416 C CA  . ALA B  370 ? 0.28490 0.30770 0.30310 0.00900  -0.00380 -0.03720 364 ALA B CA  
5417 C C   . ALA B  370 ? 0.29470 0.31500 0.32610 -0.00270 0.00310  -0.05460 364 ALA B C   
5418 O O   . ALA B  370 ? 0.30530 0.30310 0.33090 -0.00640 0.01310  -0.05380 364 ALA B O   
5419 C CB  . ALA B  370 ? 0.30700 0.31390 0.32120 0.00800  0.00280  -0.02300 364 ALA B CB  
5420 N N   . VAL B  371 ? 0.26300 0.30510 0.30910 -0.00770 0.00040  -0.07340 365 VAL B N   
5421 C CA  . VAL B  371 ? 0.29400 0.33410 0.35500 -0.02570 0.01390  -0.09740 365 VAL B CA  
5422 C C   . VAL B  371 ? 0.33780 0.34340 0.39770 -0.03640 0.02830  -0.08950 365 VAL B C   
5423 O O   . VAL B  371 ? 0.28210 0.29890 0.35320 -0.03840 0.02480  -0.08980 365 VAL B O   
5424 C CB  . VAL B  371 ? 0.26190 0.35160 0.34520 -0.02830 0.00660  -0.12910 365 VAL B CB  
5425 C CG1 . VAL B  371 ? 0.28070 0.36960 0.38400 -0.05560 0.02850  -0.16270 365 VAL B CG1 
5426 C CG2 . VAL B  371 ? 0.26430 0.38600 0.33800 -0.00810 -0.01020 -0.13410 365 VAL B CG2 
5427 N N   . ALA B  372 ? 0.31520 0.27600 0.35640 -0.04020 0.04560  -0.08390 366 ALA B N   
5428 C CA  . ALA B  372 ? 0.33180 0.25040 0.35910 -0.04380 0.06150  -0.07530 366 ALA B CA  
5429 C C   . ALA B  372 ? 0.34940 0.27250 0.39540 -0.06620 0.07630  -0.09860 366 ALA B C   
5430 O O   . ALA B  372 ? 0.39440 0.32080 0.45080 -0.08530 0.09210  -0.12660 366 ALA B O   
5431 C CB  . ALA B  372 ? 0.38930 0.25140 0.38080 -0.03760 0.08080  -0.06920 366 ALA B CB  
5432 N N   . ARG B  373 ? 0.35690 0.28460 0.41020 -0.06600 0.07260  -0.09130 367 ARG B N   
5433 C CA  . ARG B  373 ? 0.34970 0.28830 0.42440 -0.08810 0.08720  -0.11640 367 ARG B CA  
5434 C C   . ARG B  373 ? 0.31820 0.23670 0.38530 -0.08420 0.08890  -0.09930 367 ARG B C   
5435 O O   . ARG B  373 ? 0.31950 0.23570 0.37490 -0.06350 0.07140  -0.07210 367 ARG B O   
5436 C CB  . ARG B  373 ? 0.32570 0.33830 0.43760 -0.08950 0.06750  -0.14190 367 ARG B CB  
5437 C CG  . ARG B  373 ? 0.46020 0.50240 0.60300 -0.11600 0.08490  -0.18470 367 ARG B CG  
5438 C CD  . ARG B  373 ? 0.45500 0.57010 0.62620 -0.11170 0.06700  -0.21730 367 ARG B CD  
5439 N NE  . ARG B  373 ? 0.42830 0.53290 0.58820 -0.11130 0.06990  -0.22030 367 ARG B NE  
5440 C CZ  . ARG B  373 ? 0.39740 0.54480 0.58070 -0.12340 0.07520  -0.26020 367 ARG B CZ  
5441 N NH1 . ARG B  373 ? 0.50910 0.71540 0.72500 -0.12830 0.08060  -0.29010 367 ARG B NH1 
5442 N NH2 . ARG B  373 ? 0.41510 0.54860 0.58550 -0.12240 0.07680  -0.26130 367 ARG B NH2 
5443 O OXT . ARG B  373 ? 0.32980 0.23830 0.40470 -0.10310 0.10880  -0.11550 367 ARG B OXT 
5497 N N   A ASN O  .   ? 0.37220 0.27370 0.27960 0.11080  0.04140  0.00860  413 ASN A N   
5498 C CA  A ASN O  .   ? 0.32660 0.24710 0.28730 0.10260  0.04230  0.00570  413 ASN A CA  
5499 C C   A ASN O  .   ? 0.31040 0.23490 0.26630 0.10150  0.04980  -0.00450 413 ASN A C   
5500 O O   A ASN O  .   ? 0.32760 0.26070 0.25130 0.11080  0.05050  0.00010  413 ASN A O   
5501 C CB  A ASN O  .   ? 0.31870 0.27880 0.33270 0.10610  0.02350  0.03600  413 ASN A CB  
5502 C CG  A ASN O  .   ? 0.32960 0.28330 0.38290 0.10310  0.01340  0.03620  413 ASN A CG  
5503 O OD1 A ASN O  .   ? 0.27210 0.19390 0.30390 0.09820  0.02240  0.00990  413 ASN A OD1 
5504 N ND2 A ASN O  .   ? 0.32230 0.30570 0.42560 0.10320  -0.00640 0.06710  413 ASN A ND2 
5505 O OXT A ASN O  .   ? 0.36940 0.28830 0.35880 0.09150  0.05520  -0.02460 413 ASN A OXT 
5558 N N   A ASN CA .   ? 0.25520 0.38840 0.28720 -0.01730 0.15580  -0.04150 409 ASN B N   
5559 C CA  A ASN CA .   ? 0.26980 0.40250 0.30320 -0.01920 0.15350  -0.04200 409 ASN B CA  
5560 C C   A ASN CA .   ? 0.24990 0.38190 0.28250 -0.01920 0.15230  -0.04230 409 ASN B C   
5561 O O   A ASN CA .   ? 0.26790 0.39730 0.29550 -0.02070 0.15270  -0.04330 409 ASN B O   
5562 C CB  A ASN CA .   ? 0.26180 0.39330 0.29570 -0.02060 0.15450  -0.04270 409 ASN B CB  
5563 C CG  A ASN CA .   ? 0.28630 0.41740 0.31870 -0.02180 0.15580  -0.04230 409 ASN B CG  
5564 O OD1 A ASN CA .   ? 0.25340 0.38730 0.28700 -0.02140 0.15490  -0.04120 409 ASN B OD1 
5565 N ND2 A ASN CA .   ? 0.29520 0.42080 0.32160 -0.02650 0.15880  -0.04430 409 ASN B ND2 
5566 O OXT A ASN CA .   ? 0.25410 0.38600 0.28870 -0.01880 0.15250  -0.04240 409 ASN B OXT 
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