data_9FON
# 
_entry.id   9FON 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9FON         pdb_00009fon 10.2210/pdb9fon/pdb 
WWPDB D_1292139341 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FON 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aengus.mac-sweeney@idorsia.com 
_pdbx_contact_author.name_first         Aengus 
_pdbx_contact_author.name_last          'Mac Sweeney' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7250-9541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wicki, M.'       1 ? 
'Mac Sweeney, A.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Structure-Activity Relationship, cellular potency optimization of novel heme-binding Imidazo[5,1-b]thiazoles, imidazo[1,5-a]pyridines and pyrazines as potent IDO inhibitors devoid of Cyp inhibition
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cren, S.'            1 ? 
primary 'Kimmerlin, T.'       2 ? 
primary 'Pothier, J.'         3 ? 
primary 'Boss, C.'            4 ? 
primary 'Lotz-Jenne, C.'      5 ? 
primary 'Mac Sweeney, A.'     6 ? 
primary 'Pouzol, L.'          7 ? 
primary 'Chavanton-Arpel, A.' 8 ? 
# 
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 'Tryptophan 2,3-dioxygenase'                                                           43304.668 2   1.13.11.11 
? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                      616.487   2   ?          
? ? ? 
3 non-polymer syn '(~{R})-(7-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' 325.752   2   ?          
? ? ? 
4 water       nat water                                                                                  18.015    108 ?          
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'TDO,Protein vermilion,Tryptamin 2,3-dioxygenase,Tryptophan oxygenase,TO,TRPO,Tryptophan pyrrolase,Tryptophanase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRV
VLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKD
PSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVR
RGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSD
RYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSVLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRV
VLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKD
PSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVR
RGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSD
RYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSVLEHHHHHH
;
_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 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEM   
3 '(~{R})-(7-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' A1IER 
4 water                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   LYS n 
1 4   ILE n 
1 5   TYR n 
1 6   GLY n 
1 7   GLU n 
1 8   TYR n 
1 9   LEU n 
1 10  MET n 
1 11  LEU n 
1 12  ASP n 
1 13  LYS n 
1 14  LEU n 
1 15  LEU n 
1 16  ASP n 
1 17  ALA n 
1 18  GLN n 
1 19  CYS n 
1 20  MET n 
1 21  LEU n 
1 22  SER n 
1 23  GLU n 
1 24  GLU n 
1 25  ASP n 
1 26  LYS n 
1 27  ARG n 
1 28  PRO n 
1 29  VAL n 
1 30  HIS n 
1 31  ASP n 
1 32  GLU n 
1 33  HIS n 
1 34  LEU n 
1 35  PHE n 
1 36  ILE n 
1 37  ILE n 
1 38  THR n 
1 39  HIS n 
1 40  GLN n 
1 41  ALA n 
1 42  TYR n 
1 43  GLU n 
1 44  LEU n 
1 45  TRP n 
1 46  PHE n 
1 47  LYS n 
1 48  GLN n 
1 49  ILE n 
1 50  ILE n 
1 51  PHE n 
1 52  GLU n 
1 53  PHE n 
1 54  ASP n 
1 55  SER n 
1 56  ILE n 
1 57  ARG n 
1 58  ASP n 
1 59  MET n 
1 60  LEU n 
1 61  ASP n 
1 62  ALA n 
1 63  GLU n 
1 64  VAL n 
1 65  ILE n 
1 66  ASP n 
1 67  GLU n 
1 68  THR n 
1 69  LYS n 
1 70  THR n 
1 71  LEU n 
1 72  GLU n 
1 73  ILE n 
1 74  VAL n 
1 75  LYS n 
1 76  ARG n 
1 77  LEU n 
1 78  ASN n 
1 79  ARG n 
1 80  VAL n 
1 81  VAL n 
1 82  LEU n 
1 83  ILE n 
1 84  LEU n 
1 85  LYS n 
1 86  LEU n 
1 87  LEU n 
1 88  VAL n 
1 89  ASP n 
1 90  GLN n 
1 91  VAL n 
1 92  PRO n 
1 93  ILE n 
1 94  LEU n 
1 95  GLU n 
1 96  THR n 
1 97  MET n 
1 98  THR n 
1 99  PRO n 
1 100 LEU n 
1 101 ASP n 
1 102 PHE n 
1 103 MET n 
1 104 ASP n 
1 105 PHE n 
1 106 ARG n 
1 107 LYS n 
1 108 TYR n 
1 109 LEU n 
1 110 ALA n 
1 111 PRO n 
1 112 ALA n 
1 113 SER n 
1 114 GLY n 
1 115 PHE n 
1 116 GLN n 
1 117 SER n 
1 118 LEU n 
1 119 GLN n 
1 120 PHE n 
1 121 ARG n 
1 122 LEU n 
1 123 ILE n 
1 124 GLU n 
1 125 ASN n 
1 126 LYS n 
1 127 LEU n 
1 128 GLY n 
1 129 VAL n 
1 130 LEU n 
1 131 THR n 
1 132 GLU n 
1 133 GLN n 
1 134 ARG n 
1 135 VAL n 
1 136 ARG n 
1 137 TYR n 
1 138 ASN n 
1 139 GLN n 
1 140 LYS n 
1 141 TYR n 
1 142 SER n 
1 143 ASP n 
1 144 VAL n 
1 145 PHE n 
1 146 SER n 
1 147 ASP n 
1 148 GLU n 
1 149 GLU n 
1 150 ALA n 
1 151 ARG n 
1 152 ASN n 
1 153 SER n 
1 154 ILE n 
1 155 ARG n 
1 156 ASN n 
1 157 SER n 
1 158 GLU n 
1 159 LYS n 
1 160 ASP n 
1 161 PRO n 
1 162 SER n 
1 163 LEU n 
1 164 LEU n 
1 165 GLU n 
1 166 LEU n 
1 167 VAL n 
1 168 GLN n 
1 169 ARG n 
1 170 TRP n 
1 171 LEU n 
1 172 GLU n 
1 173 ARG n 
1 174 THR n 
1 175 PRO n 
1 176 GLY n 
1 177 LEU n 
1 178 GLU n 
1 179 GLU n 
1 180 SER n 
1 181 GLY n 
1 182 PHE n 
1 183 ASN n 
1 184 PHE n 
1 185 TRP n 
1 186 ALA n 
1 187 LYS n 
1 188 PHE n 
1 189 GLN n 
1 190 GLU n 
1 191 SER n 
1 192 VAL n 
1 193 ASP n 
1 194 ARG n 
1 195 PHE n 
1 196 LEU n 
1 197 GLU n 
1 198 ALA n 
1 199 GLN n 
1 200 VAL n 
1 201 GLN n 
1 202 SER n 
1 203 ALA n 
1 204 MET n 
1 205 GLU n 
1 206 GLU n 
1 207 PRO n 
1 208 VAL n 
1 209 GLU n 
1 210 LYS n 
1 211 ALA n 
1 212 LYS n 
1 213 ASN n 
1 214 TYR n 
1 215 ARG n 
1 216 LEU n 
1 217 MET n 
1 218 ASP n 
1 219 ILE n 
1 220 GLU n 
1 221 LYS n 
1 222 ARG n 
1 223 ARG n 
1 224 GLU n 
1 225 VAL n 
1 226 TYR n 
1 227 ARG n 
1 228 SER n 
1 229 ILE n 
1 230 PHE n 
1 231 ASP n 
1 232 PRO n 
1 233 ALA n 
1 234 VAL n 
1 235 HIS n 
1 236 ASP n 
1 237 ALA n 
1 238 LEU n 
1 239 VAL n 
1 240 ARG n 
1 241 ARG n 
1 242 GLY n 
1 243 ASP n 
1 244 ARG n 
1 245 ARG n 
1 246 PHE n 
1 247 SER n 
1 248 HIS n 
1 249 ARG n 
1 250 ALA n 
1 251 LEU n 
1 252 GLN n 
1 253 GLY n 
1 254 ALA n 
1 255 ILE n 
1 256 MET n 
1 257 ILE n 
1 258 THR n 
1 259 PHE n 
1 260 TYR n 
1 261 ARG n 
1 262 ASP n 
1 263 GLU n 
1 264 PRO n 
1 265 ARG n 
1 266 PHE n 
1 267 SER n 
1 268 GLN n 
1 269 PRO n 
1 270 HIS n 
1 271 GLN n 
1 272 LEU n 
1 273 LEU n 
1 274 THR n 
1 275 LEU n 
1 276 LEU n 
1 277 MET n 
1 278 ASP n 
1 279 ILE n 
1 280 ASP n 
1 281 SER n 
1 282 LEU n 
1 283 ILE n 
1 284 THR n 
1 285 LYS n 
1 286 TRP n 
1 287 ARG n 
1 288 TYR n 
1 289 ASN n 
1 290 HIS n 
1 291 VAL n 
1 292 ILE n 
1 293 MET n 
1 294 VAL n 
1 295 GLN n 
1 296 ARG n 
1 297 MET n 
1 298 ILE n 
1 299 GLY n 
1 300 SER n 
1 301 GLN n 
1 302 GLN n 
1 303 LEU n 
1 304 GLY n 
1 305 THR n 
1 306 GLY n 
1 307 GLY n 
1 308 SER n 
1 309 SER n 
1 310 GLY n 
1 311 TYR n 
1 312 GLN n 
1 313 TYR n 
1 314 LEU n 
1 315 ARG n 
1 316 SER n 
1 317 THR n 
1 318 LEU n 
1 319 SER n 
1 320 ASP n 
1 321 ARG n 
1 322 TYR n 
1 323 LYS n 
1 324 VAL n 
1 325 PHE n 
1 326 LEU n 
1 327 ASP n 
1 328 LEU n 
1 329 PHE n 
1 330 ASN n 
1 331 LEU n 
1 332 SER n 
1 333 THR n 
1 334 PHE n 
1 335 LEU n 
1 336 ILE n 
1 337 PRO n 
1 338 ARG n 
1 339 GLU n 
1 340 ALA n 
1 341 ILE n 
1 342 PRO n 
1 343 PRO n 
1 344 LEU n 
1 345 ASP n 
1 346 GLU n 
1 347 THR n 
1 348 ILE n 
1 349 ARG n 
1 350 LYS n 
1 351 LYS n 
1 352 LEU n 
1 353 ILE n 
1 354 ASN n 
1 355 LYS n 
1 356 SER n 
1 357 VAL n 
1 358 LEU n 
1 359 GLU n 
1 360 HIS n 
1 361 HIS n 
1 362 HIS n 
1 363 HIS n 
1 364 HIS n 
1 365 HIS 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                   365 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'v, CG5163' 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_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 
A1IER non-polymer         . '(~{R})-(7-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' ?    
'C16 H12 Cl N5 O'  325.752 
ALA   'L-peptide linking' y ALANINE                                                                                ?    
'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ?    
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ?    
'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ?    
'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ?    
'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                              ?    
'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ?    
'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ?    
'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                              ?    
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                  ?    'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ?    
'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                ?    
'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                                 ?    
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                             ?    
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ?    
'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                                ?    
'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                                 ?    
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                              ?    
'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                             ?    
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                               ?    
'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                                 ?    
'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   23  ?   ?   ?   A . n 
A 1 2   GLY 2   24  ?   ?   ?   A . n 
A 1 3   LYS 3   25  25  LYS LYS A . n 
A 1 4   ILE 4   26  26  ILE ILE A . n 
A 1 5   TYR 5   27  27  TYR TYR A . n 
A 1 6   GLY 6   28  28  GLY GLY A . n 
A 1 7   GLU 7   29  29  GLU GLU A . n 
A 1 8   TYR 8   30  30  TYR TYR A . n 
A 1 9   LEU 9   31  31  LEU LEU A . n 
A 1 10  MET 10  32  32  MET MET A . n 
A 1 11  LEU 11  33  33  LEU LEU A . n 
A 1 12  ASP 12  34  34  ASP ASP A . n 
A 1 13  LYS 13  35  35  LYS LYS A . n 
A 1 14  LEU 14  36  36  LEU LEU A . n 
A 1 15  LEU 15  37  37  LEU LEU A . n 
A 1 16  ASP 16  38  38  ASP ASP A . n 
A 1 17  ALA 17  39  39  ALA ALA A . n 
A 1 18  GLN 18  40  40  GLN GLN A . n 
A 1 19  CYS 19  41  41  CYS CYS A . n 
A 1 20  MET 20  42  42  MET MET A . n 
A 1 21  LEU 21  43  43  LEU LEU A . n 
A 1 22  SER 22  44  44  SER SER A . n 
A 1 23  GLU 23  45  45  GLU GLU A . n 
A 1 24  GLU 24  46  46  GLU GLU A . n 
A 1 25  ASP 25  47  47  ASP ASP A . n 
A 1 26  LYS 26  48  48  LYS LYS A . n 
A 1 27  ARG 27  49  49  ARG ARG A . n 
A 1 28  PRO 28  50  50  PRO PRO A . n 
A 1 29  VAL 29  51  51  VAL VAL A . n 
A 1 30  HIS 30  52  52  HIS HIS A . n 
A 1 31  ASP 31  53  53  ASP ASP A . n 
A 1 32  GLU 32  54  54  GLU GLU A . n 
A 1 33  HIS 33  55  55  HIS HIS A . n 
A 1 34  LEU 34  56  56  LEU LEU A . n 
A 1 35  PHE 35  57  57  PHE PHE A . n 
A 1 36  ILE 36  58  58  ILE ILE A . n 
A 1 37  ILE 37  59  59  ILE ILE A . n 
A 1 38  THR 38  60  60  THR THR A . n 
A 1 39  HIS 39  61  61  HIS HIS A . n 
A 1 40  GLN 40  62  62  GLN GLN A . n 
A 1 41  ALA 41  63  63  ALA ALA A . n 
A 1 42  TYR 42  64  64  TYR TYR A . n 
A 1 43  GLU 43  65  65  GLU GLU A . n 
A 1 44  LEU 44  66  66  LEU LEU A . n 
A 1 45  TRP 45  67  67  TRP TRP A . n 
A 1 46  PHE 46  68  68  PHE PHE A . n 
A 1 47  LYS 47  69  69  LYS LYS A . n 
A 1 48  GLN 48  70  70  GLN GLN A . n 
A 1 49  ILE 49  71  71  ILE ILE A . n 
A 1 50  ILE 50  72  72  ILE ILE A . n 
A 1 51  PHE 51  73  73  PHE PHE A . n 
A 1 52  GLU 52  74  74  GLU GLU A . n 
A 1 53  PHE 53  75  75  PHE PHE A . n 
A 1 54  ASP 54  76  76  ASP ASP A . n 
A 1 55  SER 55  77  77  SER SER A . n 
A 1 56  ILE 56  78  78  ILE ILE A . n 
A 1 57  ARG 57  79  79  ARG ARG A . n 
A 1 58  ASP 58  80  80  ASP ASP A . n 
A 1 59  MET 59  81  81  MET MET A . n 
A 1 60  LEU 60  82  82  LEU LEU A . n 
A 1 61  ASP 61  83  83  ASP ASP A . n 
A 1 62  ALA 62  84  84  ALA ALA A . n 
A 1 63  GLU 63  85  85  GLU GLU A . n 
A 1 64  VAL 64  86  86  VAL VAL A . n 
A 1 65  ILE 65  87  87  ILE ILE A . n 
A 1 66  ASP 66  88  88  ASP ASP A . n 
A 1 67  GLU 67  89  89  GLU GLU A . n 
A 1 68  THR 68  90  90  THR THR A . n 
A 1 69  LYS 69  91  91  LYS LYS A . n 
A 1 70  THR 70  92  92  THR THR A . n 
A 1 71  LEU 71  93  93  LEU LEU A . n 
A 1 72  GLU 72  94  94  GLU GLU A . n 
A 1 73  ILE 73  95  95  ILE ILE A . n 
A 1 74  VAL 74  96  96  VAL VAL A . n 
A 1 75  LYS 75  97  97  LYS LYS A . n 
A 1 76  ARG 76  98  98  ARG ARG A . n 
A 1 77  LEU 77  99  99  LEU LEU A . n 
A 1 78  ASN 78  100 100 ASN ASN A . n 
A 1 79  ARG 79  101 101 ARG ARG A . n 
A 1 80  VAL 80  102 102 VAL VAL A . n 
A 1 81  VAL 81  103 103 VAL VAL A . n 
A 1 82  LEU 82  104 104 LEU LEU A . n 
A 1 83  ILE 83  105 105 ILE ILE A . n 
A 1 84  LEU 84  106 106 LEU LEU A . n 
A 1 85  LYS 85  107 107 LYS LYS A . n 
A 1 86  LEU 86  108 108 LEU LEU A . n 
A 1 87  LEU 87  109 109 LEU LEU A . n 
A 1 88  VAL 88  110 110 VAL VAL A . n 
A 1 89  ASP 89  111 111 ASP ASP A . n 
A 1 90  GLN 90  112 112 GLN GLN A . n 
A 1 91  VAL 91  113 113 VAL VAL A . n 
A 1 92  PRO 92  114 114 PRO PRO A . n 
A 1 93  ILE 93  115 115 ILE ILE A . n 
A 1 94  LEU 94  116 116 LEU LEU A . n 
A 1 95  GLU 95  117 117 GLU GLU A . n 
A 1 96  THR 96  118 118 THR THR A . n 
A 1 97  MET 97  119 119 MET MET A . n 
A 1 98  THR 98  120 120 THR THR A . n 
A 1 99  PRO 99  121 121 PRO PRO A . n 
A 1 100 LEU 100 122 122 LEU LEU A . n 
A 1 101 ASP 101 123 123 ASP ASP A . n 
A 1 102 PHE 102 124 124 PHE PHE A . n 
A 1 103 MET 103 125 125 MET MET A . n 
A 1 104 ASP 104 126 126 ASP ASP A . n 
A 1 105 PHE 105 127 127 PHE PHE A . n 
A 1 106 ARG 106 128 128 ARG ARG A . n 
A 1 107 LYS 107 129 129 LYS LYS A . n 
A 1 108 TYR 108 130 130 TYR TYR A . n 
A 1 109 LEU 109 131 131 LEU LEU A . n 
A 1 110 ALA 110 132 132 ALA ALA A . n 
A 1 111 PRO 111 133 133 PRO PRO A . n 
A 1 112 ALA 112 134 134 ALA ALA A . n 
A 1 113 SER 113 135 135 SER SER A . n 
A 1 114 GLY 114 136 136 GLY GLY A . n 
A 1 115 PHE 115 137 137 PHE PHE A . n 
A 1 116 GLN 116 138 138 GLN GLN A . n 
A 1 117 SER 117 139 139 SER SER A . n 
A 1 118 LEU 118 140 140 LEU LEU A . n 
A 1 119 GLN 119 141 141 GLN GLN A . n 
A 1 120 PHE 120 142 142 PHE PHE A . n 
A 1 121 ARG 121 143 143 ARG ARG A . n 
A 1 122 LEU 122 144 144 LEU LEU A . n 
A 1 123 ILE 123 145 145 ILE ILE A . n 
A 1 124 GLU 124 146 146 GLU GLU A . n 
A 1 125 ASN 125 147 147 ASN ASN A . n 
A 1 126 LYS 126 148 148 LYS LYS A . n 
A 1 127 LEU 127 149 149 LEU LEU A . n 
A 1 128 GLY 128 150 150 GLY GLY A . n 
A 1 129 VAL 129 151 151 VAL VAL A . n 
A 1 130 LEU 130 152 152 LEU LEU A . n 
A 1 131 THR 131 153 153 THR THR A . n 
A 1 132 GLU 132 154 154 GLU GLU A . n 
A 1 133 GLN 133 155 155 GLN GLN A . n 
A 1 134 ARG 134 156 156 ARG ARG A . n 
A 1 135 VAL 135 157 157 VAL VAL A . n 
A 1 136 ARG 136 158 158 ARG ARG A . n 
A 1 137 TYR 137 159 ?   ?   ?   A . n 
A 1 138 ASN 138 160 ?   ?   ?   A . n 
A 1 139 GLN 139 161 161 GLN GLN A . n 
A 1 140 LYS 140 162 162 LYS LYS A . n 
A 1 141 TYR 141 163 163 TYR TYR A . n 
A 1 142 SER 142 164 164 SER SER A . n 
A 1 143 ASP 143 165 165 ASP ASP A . n 
A 1 144 VAL 144 166 166 VAL VAL A . n 
A 1 145 PHE 145 167 167 PHE PHE A . n 
A 1 146 SER 146 168 168 SER SER A . n 
A 1 147 ASP 147 169 169 ASP ASP A . n 
A 1 148 GLU 148 170 170 GLU GLU A . n 
A 1 149 GLU 149 171 171 GLU GLU A . n 
A 1 150 ALA 150 172 172 ALA ALA A . n 
A 1 151 ARG 151 173 173 ARG ARG A . n 
A 1 152 ASN 152 174 174 ASN ASN A . n 
A 1 153 SER 153 175 175 SER SER A . n 
A 1 154 ILE 154 176 176 ILE ILE A . n 
A 1 155 ARG 155 177 177 ARG ARG A . n 
A 1 156 ASN 156 178 178 ASN ASN A . n 
A 1 157 SER 157 179 179 SER SER A . n 
A 1 158 GLU 158 180 180 GLU GLU A . n 
A 1 159 LYS 159 181 181 LYS LYS A . n 
A 1 160 ASP 160 182 182 ASP ASP A . n 
A 1 161 PRO 161 183 183 PRO PRO A . n 
A 1 162 SER 162 184 184 SER SER A . n 
A 1 163 LEU 163 185 185 LEU LEU A . n 
A 1 164 LEU 164 186 186 LEU LEU A . n 
A 1 165 GLU 165 187 187 GLU GLU A . n 
A 1 166 LEU 166 188 188 LEU LEU A . n 
A 1 167 VAL 167 189 189 VAL VAL A . n 
A 1 168 GLN 168 190 190 GLN GLN A . n 
A 1 169 ARG 169 191 191 ARG ARG A . n 
A 1 170 TRP 170 192 192 TRP TRP A . n 
A 1 171 LEU 171 193 193 LEU LEU A . n 
A 1 172 GLU 172 194 194 GLU GLU A . n 
A 1 173 ARG 173 195 195 ARG ARG A . n 
A 1 174 THR 174 196 196 THR THR A . n 
A 1 175 PRO 175 197 197 PRO PRO A . n 
A 1 176 GLY 176 198 198 GLY GLY A . n 
A 1 177 LEU 177 199 199 LEU LEU A . n 
A 1 178 GLU 178 200 200 GLU GLU A . n 
A 1 179 GLU 179 201 201 GLU GLU A . n 
A 1 180 SER 180 202 202 SER SER A . n 
A 1 181 GLY 181 203 203 GLY GLY A . n 
A 1 182 PHE 182 204 204 PHE PHE A . n 
A 1 183 ASN 183 205 205 ASN ASN A . n 
A 1 184 PHE 184 206 206 PHE PHE A . n 
A 1 185 TRP 185 207 207 TRP TRP A . n 
A 1 186 ALA 186 208 208 ALA ALA A . n 
A 1 187 LYS 187 209 209 LYS LYS A . n 
A 1 188 PHE 188 210 210 PHE PHE A . n 
A 1 189 GLN 189 211 211 GLN GLN A . n 
A 1 190 GLU 190 212 212 GLU GLU A . n 
A 1 191 SER 191 213 213 SER SER A . n 
A 1 192 VAL 192 214 214 VAL VAL A . n 
A 1 193 ASP 193 215 215 ASP ASP A . n 
A 1 194 ARG 194 216 216 ARG ARG A . n 
A 1 195 PHE 195 217 217 PHE PHE A . n 
A 1 196 LEU 196 218 218 LEU LEU A . n 
A 1 197 GLU 197 219 219 GLU GLU A . n 
A 1 198 ALA 198 220 220 ALA ALA A . n 
A 1 199 GLN 199 221 221 GLN GLN A . n 
A 1 200 VAL 200 222 222 VAL VAL A . n 
A 1 201 GLN 201 223 223 GLN GLN A . n 
A 1 202 SER 202 224 224 SER SER A . n 
A 1 203 ALA 203 225 225 ALA ALA A . n 
A 1 204 MET 204 226 226 MET MET A . n 
A 1 205 GLU 205 227 227 GLU GLU A . n 
A 1 206 GLU 206 228 228 GLU GLU A . n 
A 1 207 PRO 207 229 229 PRO PRO A . n 
A 1 208 VAL 208 230 230 VAL VAL A . n 
A 1 209 GLU 209 231 231 GLU GLU A . n 
A 1 210 LYS 210 232 232 LYS LYS A . n 
A 1 211 ALA 211 233 233 ALA ALA A . n 
A 1 212 LYS 212 234 234 LYS LYS A . n 
A 1 213 ASN 213 235 235 ASN ASN A . n 
A 1 214 TYR 214 236 236 TYR TYR A . n 
A 1 215 ARG 215 237 237 ARG ARG A . n 
A 1 216 LEU 216 238 238 LEU LEU A . n 
A 1 217 MET 217 239 239 MET MET A . n 
A 1 218 ASP 218 240 240 ASP ASP A . n 
A 1 219 ILE 219 241 241 ILE ILE A . n 
A 1 220 GLU 220 242 242 GLU GLU A . n 
A 1 221 LYS 221 243 243 LYS LYS A . n 
A 1 222 ARG 222 244 244 ARG ARG A . n 
A 1 223 ARG 223 245 245 ARG ARG A . n 
A 1 224 GLU 224 246 246 GLU GLU A . n 
A 1 225 VAL 225 247 247 VAL VAL A . n 
A 1 226 TYR 226 248 248 TYR TYR A . n 
A 1 227 ARG 227 249 249 ARG ARG A . n 
A 1 228 SER 228 250 250 SER SER A . n 
A 1 229 ILE 229 251 251 ILE ILE A . n 
A 1 230 PHE 230 252 252 PHE PHE A . n 
A 1 231 ASP 231 253 253 ASP ASP A . n 
A 1 232 PRO 232 254 254 PRO PRO A . n 
A 1 233 ALA 233 255 255 ALA ALA A . n 
A 1 234 VAL 234 256 256 VAL VAL A . n 
A 1 235 HIS 235 257 257 HIS HIS A . n 
A 1 236 ASP 236 258 258 ASP ASP A . n 
A 1 237 ALA 237 259 259 ALA ALA A . n 
A 1 238 LEU 238 260 260 LEU LEU A . n 
A 1 239 VAL 239 261 261 VAL VAL A . n 
A 1 240 ARG 240 262 262 ARG ARG A . n 
A 1 241 ARG 241 263 263 ARG ARG A . n 
A 1 242 GLY 242 264 264 GLY GLY A . n 
A 1 243 ASP 243 265 265 ASP ASP A . n 
A 1 244 ARG 244 266 266 ARG ARG A . n 
A 1 245 ARG 245 267 267 ARG ARG A . n 
A 1 246 PHE 246 268 268 PHE PHE A . n 
A 1 247 SER 247 269 269 SER SER A . n 
A 1 248 HIS 248 270 270 HIS HIS A . n 
A 1 249 ARG 249 271 271 ARG ARG A . n 
A 1 250 ALA 250 272 272 ALA ALA A . n 
A 1 251 LEU 251 273 273 LEU LEU A . n 
A 1 252 GLN 252 274 274 GLN GLN A . n 
A 1 253 GLY 253 275 275 GLY GLY A . n 
A 1 254 ALA 254 276 276 ALA ALA A . n 
A 1 255 ILE 255 277 277 ILE ILE A . n 
A 1 256 MET 256 278 278 MET MET A . n 
A 1 257 ILE 257 279 279 ILE ILE A . n 
A 1 258 THR 258 280 280 THR THR A . n 
A 1 259 PHE 259 281 281 PHE PHE A . n 
A 1 260 TYR 260 282 282 TYR TYR A . n 
A 1 261 ARG 261 283 283 ARG ARG A . n 
A 1 262 ASP 262 284 284 ASP ASP A . n 
A 1 263 GLU 263 285 285 GLU GLU A . n 
A 1 264 PRO 264 286 286 PRO PRO A . n 
A 1 265 ARG 265 287 287 ARG ARG A . n 
A 1 266 PHE 266 288 288 PHE PHE A . n 
A 1 267 SER 267 289 289 SER SER A . n 
A 1 268 GLN 268 290 290 GLN GLN A . n 
A 1 269 PRO 269 291 291 PRO PRO A . n 
A 1 270 HIS 270 292 292 HIS HIS A . n 
A 1 271 GLN 271 293 293 GLN GLN A . n 
A 1 272 LEU 272 294 294 LEU LEU A . n 
A 1 273 LEU 273 295 295 LEU LEU A . n 
A 1 274 THR 274 296 296 THR THR A . n 
A 1 275 LEU 275 297 297 LEU LEU A . n 
A 1 276 LEU 276 298 298 LEU LEU A . n 
A 1 277 MET 277 299 299 MET MET A . n 
A 1 278 ASP 278 300 300 ASP ASP A . n 
A 1 279 ILE 279 301 301 ILE ILE A . n 
A 1 280 ASP 280 302 302 ASP ASP A . n 
A 1 281 SER 281 303 303 SER SER A . n 
A 1 282 LEU 282 304 304 LEU LEU A . n 
A 1 283 ILE 283 305 305 ILE ILE A . n 
A 1 284 THR 284 306 306 THR THR A . n 
A 1 285 LYS 285 307 307 LYS LYS A . n 
A 1 286 TRP 286 308 308 TRP TRP A . n 
A 1 287 ARG 287 309 309 ARG ARG A . n 
A 1 288 TYR 288 310 310 TYR TYR A . n 
A 1 289 ASN 289 311 311 ASN ASN A . n 
A 1 290 HIS 290 312 312 HIS HIS A . n 
A 1 291 VAL 291 313 313 VAL VAL A . n 
A 1 292 ILE 292 314 314 ILE ILE A . n 
A 1 293 MET 293 315 315 MET MET A . n 
A 1 294 VAL 294 316 316 VAL VAL A . n 
A 1 295 GLN 295 317 317 GLN GLN A . n 
A 1 296 ARG 296 318 318 ARG ARG A . n 
A 1 297 MET 297 319 319 MET MET A . n 
A 1 298 ILE 298 320 320 ILE ILE A . n 
A 1 299 GLY 299 321 321 GLY GLY A . n 
A 1 300 SER 300 322 322 SER SER A . n 
A 1 301 GLN 301 323 323 GLN GLN A . n 
A 1 302 GLN 302 324 324 GLN GLN A . n 
A 1 303 LEU 303 325 325 LEU LEU A . n 
A 1 304 GLY 304 326 326 GLY GLY A . n 
A 1 305 THR 305 327 327 THR THR A . n 
A 1 306 GLY 306 328 328 GLY GLY A . n 
A 1 307 GLY 307 329 329 GLY GLY A . n 
A 1 308 SER 308 330 330 SER SER A . n 
A 1 309 SER 309 331 331 SER SER A . n 
A 1 310 GLY 310 332 332 GLY GLY A . n 
A 1 311 TYR 311 333 333 TYR TYR A . n 
A 1 312 GLN 312 334 334 GLN GLN A . n 
A 1 313 TYR 313 335 335 TYR TYR A . n 
A 1 314 LEU 314 336 336 LEU LEU A . n 
A 1 315 ARG 315 337 337 ARG ARG A . n 
A 1 316 SER 316 338 338 SER SER A . n 
A 1 317 THR 317 339 339 THR THR A . n 
A 1 318 LEU 318 340 340 LEU LEU A . n 
A 1 319 SER 319 341 341 SER SER A . n 
A 1 320 ASP 320 342 342 ASP ASP A . n 
A 1 321 ARG 321 343 343 ARG ARG A . n 
A 1 322 TYR 322 344 344 TYR TYR A . n 
A 1 323 LYS 323 345 345 LYS LYS A . n 
A 1 324 VAL 324 346 346 VAL VAL A . n 
A 1 325 PHE 325 347 347 PHE PHE A . n 
A 1 326 LEU 326 348 348 LEU LEU A . n 
A 1 327 ASP 327 349 349 ASP ASP A . n 
A 1 328 LEU 328 350 350 LEU LEU A . n 
A 1 329 PHE 329 351 351 PHE PHE A . n 
A 1 330 ASN 330 352 352 ASN ASN A . n 
A 1 331 LEU 331 353 353 LEU LEU A . n 
A 1 332 SER 332 354 354 SER SER A . n 
A 1 333 THR 333 355 355 THR THR A . n 
A 1 334 PHE 334 356 356 PHE PHE A . n 
A 1 335 LEU 335 357 357 LEU LEU A . n 
A 1 336 ILE 336 358 358 ILE ILE A . n 
A 1 337 PRO 337 359 359 PRO PRO A . n 
A 1 338 ARG 338 360 360 ARG ARG A . n 
A 1 339 GLU 339 361 361 GLU GLU A . n 
A 1 340 ALA 340 362 362 ALA ALA A . n 
A 1 341 ILE 341 363 363 ILE ILE A . n 
A 1 342 PRO 342 364 364 PRO PRO A . n 
A 1 343 PRO 343 365 365 PRO PRO A . n 
A 1 344 LEU 344 366 366 LEU LEU A . n 
A 1 345 ASP 345 367 ?   ?   ?   A . n 
A 1 346 GLU 346 368 ?   ?   ?   A . n 
A 1 347 THR 347 369 ?   ?   ?   A . n 
A 1 348 ILE 348 370 ?   ?   ?   A . n 
A 1 349 ARG 349 371 ?   ?   ?   A . n 
A 1 350 LYS 350 372 ?   ?   ?   A . n 
A 1 351 LYS 351 373 ?   ?   ?   A . n 
A 1 352 LEU 352 374 ?   ?   ?   A . n 
A 1 353 ILE 353 375 ?   ?   ?   A . n 
A 1 354 ASN 354 376 ?   ?   ?   A . n 
A 1 355 LYS 355 377 ?   ?   ?   A . n 
A 1 356 SER 356 378 ?   ?   ?   A . n 
A 1 357 VAL 357 379 ?   ?   ?   A . n 
A 1 358 LEU 358 380 ?   ?   ?   A . n 
A 1 359 GLU 359 381 ?   ?   ?   A . n 
A 1 360 HIS 360 382 ?   ?   ?   A . n 
A 1 361 HIS 361 383 ?   ?   ?   A . n 
A 1 362 HIS 362 384 ?   ?   ?   A . n 
A 1 363 HIS 363 385 ?   ?   ?   A . n 
A 1 364 HIS 364 386 ?   ?   ?   A . n 
A 1 365 HIS 365 387 ?   ?   ?   A . n 
B 1 1   MET 1   23  ?   ?   ?   B . n 
B 1 2   GLY 2   24  ?   ?   ?   B . n 
B 1 3   LYS 3   25  25  LYS LYS B . n 
B 1 4   ILE 4   26  26  ILE ILE B . n 
B 1 5   TYR 5   27  27  TYR TYR B . n 
B 1 6   GLY 6   28  28  GLY GLY B . n 
B 1 7   GLU 7   29  29  GLU GLU B . n 
B 1 8   TYR 8   30  30  TYR TYR B . n 
B 1 9   LEU 9   31  31  LEU LEU B . n 
B 1 10  MET 10  32  32  MET MET B . n 
B 1 11  LEU 11  33  33  LEU LEU B . n 
B 1 12  ASP 12  34  34  ASP ASP B . n 
B 1 13  LYS 13  35  35  LYS LYS B . n 
B 1 14  LEU 14  36  36  LEU LEU B . n 
B 1 15  LEU 15  37  37  LEU LEU B . n 
B 1 16  ASP 16  38  38  ASP ASP B . n 
B 1 17  ALA 17  39  39  ALA ALA B . n 
B 1 18  GLN 18  40  40  GLN GLN B . n 
B 1 19  CYS 19  41  41  CYS CYS B . n 
B 1 20  MET 20  42  42  MET MET B . n 
B 1 21  LEU 21  43  43  LEU LEU B . n 
B 1 22  SER 22  44  44  SER SER B . n 
B 1 23  GLU 23  45  45  GLU GLU B . n 
B 1 24  GLU 24  46  46  GLU GLU B . n 
B 1 25  ASP 25  47  47  ASP ASP B . n 
B 1 26  LYS 26  48  48  LYS LYS B . n 
B 1 27  ARG 27  49  49  ARG ARG B . n 
B 1 28  PRO 28  50  50  PRO PRO B . n 
B 1 29  VAL 29  51  51  VAL VAL B . n 
B 1 30  HIS 30  52  52  HIS HIS B . n 
B 1 31  ASP 31  53  53  ASP ASP B . n 
B 1 32  GLU 32  54  54  GLU GLU B . n 
B 1 33  HIS 33  55  55  HIS HIS B . n 
B 1 34  LEU 34  56  56  LEU LEU B . n 
B 1 35  PHE 35  57  57  PHE PHE B . n 
B 1 36  ILE 36  58  58  ILE ILE B . n 
B 1 37  ILE 37  59  59  ILE ILE B . n 
B 1 38  THR 38  60  60  THR THR B . n 
B 1 39  HIS 39  61  61  HIS HIS B . n 
B 1 40  GLN 40  62  62  GLN GLN B . n 
B 1 41  ALA 41  63  63  ALA ALA B . n 
B 1 42  TYR 42  64  64  TYR TYR B . n 
B 1 43  GLU 43  65  65  GLU GLU B . n 
B 1 44  LEU 44  66  66  LEU LEU B . n 
B 1 45  TRP 45  67  67  TRP TRP B . n 
B 1 46  PHE 46  68  68  PHE PHE B . n 
B 1 47  LYS 47  69  69  LYS LYS B . n 
B 1 48  GLN 48  70  70  GLN GLN B . n 
B 1 49  ILE 49  71  71  ILE ILE B . n 
B 1 50  ILE 50  72  72  ILE ILE B . n 
B 1 51  PHE 51  73  73  PHE PHE B . n 
B 1 52  GLU 52  74  74  GLU GLU B . n 
B 1 53  PHE 53  75  75  PHE PHE B . n 
B 1 54  ASP 54  76  76  ASP ASP B . n 
B 1 55  SER 55  77  77  SER SER B . n 
B 1 56  ILE 56  78  78  ILE ILE B . n 
B 1 57  ARG 57  79  79  ARG ARG B . n 
B 1 58  ASP 58  80  80  ASP ASP B . n 
B 1 59  MET 59  81  81  MET MET B . n 
B 1 60  LEU 60  82  82  LEU LEU B . n 
B 1 61  ASP 61  83  83  ASP ASP B . n 
B 1 62  ALA 62  84  84  ALA ALA B . n 
B 1 63  GLU 63  85  85  GLU GLU B . n 
B 1 64  VAL 64  86  86  VAL VAL B . n 
B 1 65  ILE 65  87  87  ILE ILE B . n 
B 1 66  ASP 66  88  88  ASP ASP B . n 
B 1 67  GLU 67  89  89  GLU GLU B . n 
B 1 68  THR 68  90  90  THR THR B . n 
B 1 69  LYS 69  91  91  LYS LYS B . n 
B 1 70  THR 70  92  92  THR THR B . n 
B 1 71  LEU 71  93  93  LEU LEU B . n 
B 1 72  GLU 72  94  94  GLU GLU B . n 
B 1 73  ILE 73  95  95  ILE ILE B . n 
B 1 74  VAL 74  96  96  VAL VAL B . n 
B 1 75  LYS 75  97  97  LYS LYS B . n 
B 1 76  ARG 76  98  98  ARG ARG B . n 
B 1 77  LEU 77  99  99  LEU LEU B . n 
B 1 78  ASN 78  100 100 ASN ASN B . n 
B 1 79  ARG 79  101 101 ARG ARG B . n 
B 1 80  VAL 80  102 102 VAL VAL B . n 
B 1 81  VAL 81  103 103 VAL VAL B . n 
B 1 82  LEU 82  104 104 LEU LEU B . n 
B 1 83  ILE 83  105 105 ILE ILE B . n 
B 1 84  LEU 84  106 106 LEU LEU B . n 
B 1 85  LYS 85  107 107 LYS LYS B . n 
B 1 86  LEU 86  108 108 LEU LEU B . n 
B 1 87  LEU 87  109 109 LEU LEU B . n 
B 1 88  VAL 88  110 110 VAL VAL B . n 
B 1 89  ASP 89  111 111 ASP ASP B . n 
B 1 90  GLN 90  112 112 GLN GLN B . n 
B 1 91  VAL 91  113 113 VAL VAL B . n 
B 1 92  PRO 92  114 114 PRO PRO B . n 
B 1 93  ILE 93  115 115 ILE ILE B . n 
B 1 94  LEU 94  116 116 LEU LEU B . n 
B 1 95  GLU 95  117 117 GLU GLU B . n 
B 1 96  THR 96  118 118 THR THR B . n 
B 1 97  MET 97  119 119 MET MET B . n 
B 1 98  THR 98  120 120 THR THR B . n 
B 1 99  PRO 99  121 121 PRO PRO B . n 
B 1 100 LEU 100 122 122 LEU LEU B . n 
B 1 101 ASP 101 123 123 ASP ASP B . n 
B 1 102 PHE 102 124 124 PHE PHE B . n 
B 1 103 MET 103 125 125 MET MET B . n 
B 1 104 ASP 104 126 126 ASP ASP B . n 
B 1 105 PHE 105 127 127 PHE PHE B . n 
B 1 106 ARG 106 128 128 ARG ARG B . n 
B 1 107 LYS 107 129 129 LYS LYS B . n 
B 1 108 TYR 108 130 130 TYR TYR B . n 
B 1 109 LEU 109 131 131 LEU LEU B . n 
B 1 110 ALA 110 132 132 ALA ALA B . n 
B 1 111 PRO 111 133 133 PRO PRO B . n 
B 1 112 ALA 112 134 134 ALA ALA B . n 
B 1 113 SER 113 135 135 SER SER B . n 
B 1 114 GLY 114 136 136 GLY GLY B . n 
B 1 115 PHE 115 137 137 PHE PHE B . n 
B 1 116 GLN 116 138 138 GLN GLN B . n 
B 1 117 SER 117 139 139 SER SER B . n 
B 1 118 LEU 118 140 140 LEU LEU B . n 
B 1 119 GLN 119 141 141 GLN GLN B . n 
B 1 120 PHE 120 142 142 PHE PHE B . n 
B 1 121 ARG 121 143 143 ARG ARG B . n 
B 1 122 LEU 122 144 144 LEU LEU B . n 
B 1 123 ILE 123 145 145 ILE ILE B . n 
B 1 124 GLU 124 146 146 GLU GLU B . n 
B 1 125 ASN 125 147 147 ASN ASN B . n 
B 1 126 LYS 126 148 148 LYS LYS B . n 
B 1 127 LEU 127 149 149 LEU LEU B . n 
B 1 128 GLY 128 150 150 GLY GLY B . n 
B 1 129 VAL 129 151 151 VAL VAL B . n 
B 1 130 LEU 130 152 152 LEU LEU B . n 
B 1 131 THR 131 153 153 THR THR B . n 
B 1 132 GLU 132 154 154 GLU GLU B . n 
B 1 133 GLN 133 155 155 GLN GLN B . n 
B 1 134 ARG 134 156 156 ARG ARG B . n 
B 1 135 VAL 135 157 157 VAL VAL B . n 
B 1 136 ARG 136 158 158 ARG ARG B . n 
B 1 137 TYR 137 159 159 TYR TYR B . n 
B 1 138 ASN 138 160 160 ASN ASN B . n 
B 1 139 GLN 139 161 161 GLN GLN B . n 
B 1 140 LYS 140 162 162 LYS LYS B . n 
B 1 141 TYR 141 163 163 TYR TYR B . n 
B 1 142 SER 142 164 164 SER SER B . n 
B 1 143 ASP 143 165 165 ASP ASP B . n 
B 1 144 VAL 144 166 166 VAL VAL B . n 
B 1 145 PHE 145 167 167 PHE PHE B . n 
B 1 146 SER 146 168 168 SER SER B . n 
B 1 147 ASP 147 169 169 ASP ASP B . n 
B 1 148 GLU 148 170 170 GLU GLU B . n 
B 1 149 GLU 149 171 171 GLU GLU B . n 
B 1 150 ALA 150 172 172 ALA ALA B . n 
B 1 151 ARG 151 173 173 ARG ARG B . n 
B 1 152 ASN 152 174 174 ASN ASN B . n 
B 1 153 SER 153 175 175 SER SER B . n 
B 1 154 ILE 154 176 176 ILE ILE B . n 
B 1 155 ARG 155 177 177 ARG ARG B . n 
B 1 156 ASN 156 178 178 ASN ASN B . n 
B 1 157 SER 157 179 179 SER SER B . n 
B 1 158 GLU 158 180 180 GLU GLU B . n 
B 1 159 LYS 159 181 181 LYS LYS B . n 
B 1 160 ASP 160 182 182 ASP ASP B . n 
B 1 161 PRO 161 183 183 PRO PRO B . n 
B 1 162 SER 162 184 184 SER SER B . n 
B 1 163 LEU 163 185 185 LEU LEU B . n 
B 1 164 LEU 164 186 186 LEU LEU B . n 
B 1 165 GLU 165 187 187 GLU GLU B . n 
B 1 166 LEU 166 188 188 LEU LEU B . n 
B 1 167 VAL 167 189 189 VAL VAL B . n 
B 1 168 GLN 168 190 190 GLN GLN B . n 
B 1 169 ARG 169 191 191 ARG ARG B . n 
B 1 170 TRP 170 192 192 TRP TRP B . n 
B 1 171 LEU 171 193 193 LEU LEU B . n 
B 1 172 GLU 172 194 194 GLU GLU B . n 
B 1 173 ARG 173 195 195 ARG ARG B . n 
B 1 174 THR 174 196 196 THR THR B . n 
B 1 175 PRO 175 197 197 PRO PRO B . n 
B 1 176 GLY 176 198 198 GLY GLY B . n 
B 1 177 LEU 177 199 199 LEU LEU B . n 
B 1 178 GLU 178 200 200 GLU GLU B . n 
B 1 179 GLU 179 201 201 GLU GLU B . n 
B 1 180 SER 180 202 202 SER SER B . n 
B 1 181 GLY 181 203 203 GLY GLY B . n 
B 1 182 PHE 182 204 204 PHE PHE B . n 
B 1 183 ASN 183 205 205 ASN ASN B . n 
B 1 184 PHE 184 206 206 PHE PHE B . n 
B 1 185 TRP 185 207 207 TRP TRP B . n 
B 1 186 ALA 186 208 208 ALA ALA B . n 
B 1 187 LYS 187 209 209 LYS LYS B . n 
B 1 188 PHE 188 210 210 PHE PHE B . n 
B 1 189 GLN 189 211 211 GLN GLN B . n 
B 1 190 GLU 190 212 212 GLU GLU B . n 
B 1 191 SER 191 213 213 SER SER B . n 
B 1 192 VAL 192 214 214 VAL VAL B . n 
B 1 193 ASP 193 215 215 ASP ASP B . n 
B 1 194 ARG 194 216 216 ARG ARG B . n 
B 1 195 PHE 195 217 217 PHE PHE B . n 
B 1 196 LEU 196 218 218 LEU LEU B . n 
B 1 197 GLU 197 219 219 GLU GLU B . n 
B 1 198 ALA 198 220 220 ALA ALA B . n 
B 1 199 GLN 199 221 221 GLN GLN B . n 
B 1 200 VAL 200 222 222 VAL VAL B . n 
B 1 201 GLN 201 223 223 GLN GLN B . n 
B 1 202 SER 202 224 224 SER SER B . n 
B 1 203 ALA 203 225 225 ALA ALA B . n 
B 1 204 MET 204 226 226 MET MET B . n 
B 1 205 GLU 205 227 227 GLU GLU B . n 
B 1 206 GLU 206 228 228 GLU GLU B . n 
B 1 207 PRO 207 229 229 PRO PRO B . n 
B 1 208 VAL 208 230 230 VAL VAL B . n 
B 1 209 GLU 209 231 231 GLU GLU B . n 
B 1 210 LYS 210 232 232 LYS LYS B . n 
B 1 211 ALA 211 233 233 ALA ALA B . n 
B 1 212 LYS 212 234 234 LYS LYS B . n 
B 1 213 ASN 213 235 235 ASN ASN B . n 
B 1 214 TYR 214 236 236 TYR TYR B . n 
B 1 215 ARG 215 237 237 ARG ARG B . n 
B 1 216 LEU 216 238 238 LEU LEU B . n 
B 1 217 MET 217 239 239 MET MET B . n 
B 1 218 ASP 218 240 240 ASP ASP B . n 
B 1 219 ILE 219 241 241 ILE ILE B . n 
B 1 220 GLU 220 242 242 GLU GLU B . n 
B 1 221 LYS 221 243 243 LYS LYS B . n 
B 1 222 ARG 222 244 244 ARG ARG B . n 
B 1 223 ARG 223 245 245 ARG ARG B . n 
B 1 224 GLU 224 246 246 GLU GLU B . n 
B 1 225 VAL 225 247 247 VAL VAL B . n 
B 1 226 TYR 226 248 248 TYR TYR B . n 
B 1 227 ARG 227 249 249 ARG ARG B . n 
B 1 228 SER 228 250 250 SER SER B . n 
B 1 229 ILE 229 251 251 ILE ILE B . n 
B 1 230 PHE 230 252 252 PHE PHE B . n 
B 1 231 ASP 231 253 253 ASP ASP B . n 
B 1 232 PRO 232 254 254 PRO PRO B . n 
B 1 233 ALA 233 255 255 ALA ALA B . n 
B 1 234 VAL 234 256 256 VAL VAL B . n 
B 1 235 HIS 235 257 257 HIS HIS B . n 
B 1 236 ASP 236 258 258 ASP ASP B . n 
B 1 237 ALA 237 259 259 ALA ALA B . n 
B 1 238 LEU 238 260 260 LEU LEU B . n 
B 1 239 VAL 239 261 261 VAL VAL B . n 
B 1 240 ARG 240 262 262 ARG ARG B . n 
B 1 241 ARG 241 263 263 ARG ARG B . n 
B 1 242 GLY 242 264 264 GLY GLY B . n 
B 1 243 ASP 243 265 265 ASP ASP B . n 
B 1 244 ARG 244 266 266 ARG ARG B . n 
B 1 245 ARG 245 267 267 ARG ARG B . n 
B 1 246 PHE 246 268 268 PHE PHE B . n 
B 1 247 SER 247 269 269 SER SER B . n 
B 1 248 HIS 248 270 270 HIS HIS B . n 
B 1 249 ARG 249 271 271 ARG ARG B . n 
B 1 250 ALA 250 272 272 ALA ALA B . n 
B 1 251 LEU 251 273 273 LEU LEU B . n 
B 1 252 GLN 252 274 274 GLN GLN B . n 
B 1 253 GLY 253 275 275 GLY GLY B . n 
B 1 254 ALA 254 276 276 ALA ALA B . n 
B 1 255 ILE 255 277 277 ILE ILE B . n 
B 1 256 MET 256 278 278 MET MET B . n 
B 1 257 ILE 257 279 279 ILE ILE B . n 
B 1 258 THR 258 280 280 THR THR B . n 
B 1 259 PHE 259 281 281 PHE PHE B . n 
B 1 260 TYR 260 282 282 TYR TYR B . n 
B 1 261 ARG 261 283 283 ARG ARG B . n 
B 1 262 ASP 262 284 284 ASP ASP B . n 
B 1 263 GLU 263 285 285 GLU GLU B . n 
B 1 264 PRO 264 286 286 PRO PRO B . n 
B 1 265 ARG 265 287 287 ARG ARG B . n 
B 1 266 PHE 266 288 288 PHE PHE B . n 
B 1 267 SER 267 289 289 SER SER B . n 
B 1 268 GLN 268 290 290 GLN GLN B . n 
B 1 269 PRO 269 291 291 PRO PRO B . n 
B 1 270 HIS 270 292 292 HIS HIS B . n 
B 1 271 GLN 271 293 293 GLN GLN B . n 
B 1 272 LEU 272 294 294 LEU LEU B . n 
B 1 273 LEU 273 295 295 LEU LEU B . n 
B 1 274 THR 274 296 296 THR THR B . n 
B 1 275 LEU 275 297 297 LEU LEU B . n 
B 1 276 LEU 276 298 298 LEU LEU B . n 
B 1 277 MET 277 299 299 MET MET B . n 
B 1 278 ASP 278 300 300 ASP ASP B . n 
B 1 279 ILE 279 301 301 ILE ILE B . n 
B 1 280 ASP 280 302 302 ASP ASP B . n 
B 1 281 SER 281 303 303 SER SER B . n 
B 1 282 LEU 282 304 304 LEU LEU B . n 
B 1 283 ILE 283 305 305 ILE ILE B . n 
B 1 284 THR 284 306 306 THR THR B . n 
B 1 285 LYS 285 307 307 LYS LYS B . n 
B 1 286 TRP 286 308 308 TRP TRP B . n 
B 1 287 ARG 287 309 309 ARG ARG B . n 
B 1 288 TYR 288 310 310 TYR TYR B . n 
B 1 289 ASN 289 311 311 ASN ASN B . n 
B 1 290 HIS 290 312 312 HIS HIS B . n 
B 1 291 VAL 291 313 313 VAL VAL B . n 
B 1 292 ILE 292 314 314 ILE ILE B . n 
B 1 293 MET 293 315 315 MET MET B . n 
B 1 294 VAL 294 316 316 VAL VAL B . n 
B 1 295 GLN 295 317 317 GLN GLN B . n 
B 1 296 ARG 296 318 318 ARG ARG B . n 
B 1 297 MET 297 319 319 MET MET B . n 
B 1 298 ILE 298 320 320 ILE ILE B . n 
B 1 299 GLY 299 321 321 GLY GLY B . n 
B 1 300 SER 300 322 322 SER SER B . n 
B 1 301 GLN 301 323 323 GLN GLN B . n 
B 1 302 GLN 302 324 324 GLN GLN B . n 
B 1 303 LEU 303 325 325 LEU LEU B . n 
B 1 304 GLY 304 326 326 GLY GLY B . n 
B 1 305 THR 305 327 327 THR THR B . n 
B 1 306 GLY 306 328 328 GLY GLY B . n 
B 1 307 GLY 307 329 329 GLY GLY B . n 
B 1 308 SER 308 330 330 SER SER B . n 
B 1 309 SER 309 331 331 SER SER B . n 
B 1 310 GLY 310 332 332 GLY GLY B . n 
B 1 311 TYR 311 333 333 TYR TYR B . n 
B 1 312 GLN 312 334 334 GLN GLN B . n 
B 1 313 TYR 313 335 335 TYR TYR B . n 
B 1 314 LEU 314 336 336 LEU LEU B . n 
B 1 315 ARG 315 337 337 ARG ARG B . n 
B 1 316 SER 316 338 338 SER SER B . n 
B 1 317 THR 317 339 339 THR THR B . n 
B 1 318 LEU 318 340 340 LEU LEU B . n 
B 1 319 SER 319 341 341 SER SER B . n 
B 1 320 ASP 320 342 342 ASP ASP B . n 
B 1 321 ARG 321 343 343 ARG ARG B . n 
B 1 322 TYR 322 344 344 TYR TYR B . n 
B 1 323 LYS 323 345 345 LYS LYS B . n 
B 1 324 VAL 324 346 346 VAL VAL B . n 
B 1 325 PHE 325 347 347 PHE PHE B . n 
B 1 326 LEU 326 348 348 LEU LEU B . n 
B 1 327 ASP 327 349 349 ASP ASP B . n 
B 1 328 LEU 328 350 350 LEU LEU B . n 
B 1 329 PHE 329 351 351 PHE PHE B . n 
B 1 330 ASN 330 352 352 ASN ASN B . n 
B 1 331 LEU 331 353 353 LEU LEU B . n 
B 1 332 SER 332 354 354 SER SER B . n 
B 1 333 THR 333 355 355 THR THR B . n 
B 1 334 PHE 334 356 356 PHE PHE B . n 
B 1 335 LEU 335 357 357 LEU LEU B . n 
B 1 336 ILE 336 358 358 ILE ILE B . n 
B 1 337 PRO 337 359 359 PRO PRO B . n 
B 1 338 ARG 338 360 360 ARG ARG B . n 
B 1 339 GLU 339 361 361 GLU GLU B . n 
B 1 340 ALA 340 362 362 ALA ALA B . n 
B 1 341 ILE 341 363 363 ILE ILE B . n 
B 1 342 PRO 342 364 364 PRO PRO B . n 
B 1 343 PRO 343 365 365 PRO PRO B . n 
B 1 344 LEU 344 366 366 LEU LEU B . n 
B 1 345 ASP 345 367 367 ASP ASP B . n 
B 1 346 GLU 346 368 368 GLU GLU B . n 
B 1 347 THR 347 369 ?   ?   ?   B . n 
B 1 348 ILE 348 370 ?   ?   ?   B . n 
B 1 349 ARG 349 371 ?   ?   ?   B . n 
B 1 350 LYS 350 372 ?   ?   ?   B . n 
B 1 351 LYS 351 373 ?   ?   ?   B . n 
B 1 352 LEU 352 374 ?   ?   ?   B . n 
B 1 353 ILE 353 375 ?   ?   ?   B . n 
B 1 354 ASN 354 376 ?   ?   ?   B . n 
B 1 355 LYS 355 377 ?   ?   ?   B . n 
B 1 356 SER 356 378 ?   ?   ?   B . n 
B 1 357 VAL 357 379 ?   ?   ?   B . n 
B 1 358 LEU 358 380 ?   ?   ?   B . n 
B 1 359 GLU 359 381 ?   ?   ?   B . n 
B 1 360 HIS 360 382 ?   ?   ?   B . n 
B 1 361 HIS 361 383 ?   ?   ?   B . n 
B 1 362 HIS 362 384 ?   ?   ?   B . n 
B 1 363 HIS 363 385 ?   ?   ?   B . n 
B 1 364 HIS 364 386 ?   ?   ?   B . n 
B 1 365 HIS 365 387 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IER 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IER 
_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 HEM   1  401 401 HEM   HEM A . 
D 3 A1IER 1  402 402 A1IER LIG A . 
E 2 HEM   1  401 401 HEM   HEM B . 
F 3 A1IER 1  402 402 A1IER LIG B . 
G 4 HOH   1  501 114 HOH   HOH A . 
G 4 HOH   2  502 43  HOH   HOH A . 
G 4 HOH   3  503 55  HOH   HOH A . 
G 4 HOH   4  504 115 HOH   HOH A . 
G 4 HOH   5  505 12  HOH   HOH A . 
G 4 HOH   6  506 119 HOH   HOH A . 
G 4 HOH   7  507 3   HOH   HOH A . 
G 4 HOH   8  508 56  HOH   HOH A . 
G 4 HOH   9  509 65  HOH   HOH A . 
G 4 HOH   10 510 87  HOH   HOH A . 
G 4 HOH   11 511 120 HOH   HOH A . 
G 4 HOH   12 512 41  HOH   HOH A . 
G 4 HOH   13 513 10  HOH   HOH A . 
G 4 HOH   14 514 22  HOH   HOH A . 
G 4 HOH   15 515 19  HOH   HOH A . 
G 4 HOH   16 516 83  HOH   HOH A . 
G 4 HOH   17 517 13  HOH   HOH A . 
G 4 HOH   18 518 39  HOH   HOH A . 
G 4 HOH   19 519 89  HOH   HOH A . 
G 4 HOH   20 520 97  HOH   HOH A . 
G 4 HOH   21 521 118 HOH   HOH A . 
G 4 HOH   22 522 116 HOH   HOH A . 
G 4 HOH   23 523 92  HOH   HOH A . 
G 4 HOH   24 524 117 HOH   HOH A . 
G 4 HOH   25 525 45  HOH   HOH A . 
G 4 HOH   26 526 49  HOH   HOH A . 
G 4 HOH   27 527 18  HOH   HOH A . 
G 4 HOH   28 528 86  HOH   HOH A . 
G 4 HOH   29 529 75  HOH   HOH A . 
G 4 HOH   30 530 14  HOH   HOH A . 
G 4 HOH   31 531 32  HOH   HOH A . 
G 4 HOH   32 532 24  HOH   HOH A . 
G 4 HOH   33 533 107 HOH   HOH A . 
G 4 HOH   34 534 15  HOH   HOH A . 
G 4 HOH   35 535 29  HOH   HOH A . 
G 4 HOH   36 536 37  HOH   HOH A . 
G 4 HOH   37 537 121 HOH   HOH A . 
G 4 HOH   38 538 74  HOH   HOH A . 
G 4 HOH   39 539 71  HOH   HOH A . 
G 4 HOH   40 540 17  HOH   HOH A . 
G 4 HOH   41 541 31  HOH   HOH A . 
G 4 HOH   42 542 108 HOH   HOH A . 
G 4 HOH   43 543 36  HOH   HOH A . 
G 4 HOH   44 544 66  HOH   HOH A . 
G 4 HOH   45 545 6   HOH   HOH A . 
G 4 HOH   46 546 69  HOH   HOH A . 
G 4 HOH   47 547 101 HOH   HOH A . 
G 4 HOH   48 548 109 HOH   HOH A . 
G 4 HOH   49 549 106 HOH   HOH A . 
G 4 HOH   50 550 99  HOH   HOH A . 
H 4 HOH   1  501 122 HOH   HOH B . 
H 4 HOH   2  502 7   HOH   HOH B . 
H 4 HOH   3  503 46  HOH   HOH B . 
H 4 HOH   4  504 11  HOH   HOH B . 
H 4 HOH   5  505 80  HOH   HOH B . 
H 4 HOH   6  506 57  HOH   HOH B . 
H 4 HOH   7  507 77  HOH   HOH B . 
H 4 HOH   8  508 91  HOH   HOH B . 
H 4 HOH   9  509 50  HOH   HOH B . 
H 4 HOH   10 510 105 HOH   HOH B . 
H 4 HOH   11 511 48  HOH   HOH B . 
H 4 HOH   12 512 73  HOH   HOH B . 
H 4 HOH   13 513 16  HOH   HOH B . 
H 4 HOH   14 514 4   HOH   HOH B . 
H 4 HOH   15 515 59  HOH   HOH B . 
H 4 HOH   16 516 40  HOH   HOH B . 
H 4 HOH   17 517 30  HOH   HOH B . 
H 4 HOH   18 518 90  HOH   HOH B . 
H 4 HOH   19 519 9   HOH   HOH B . 
H 4 HOH   20 520 2   HOH   HOH B . 
H 4 HOH   21 521 78  HOH   HOH B . 
H 4 HOH   22 522 1   HOH   HOH B . 
H 4 HOH   23 523 20  HOH   HOH B . 
H 4 HOH   24 524 98  HOH   HOH B . 
H 4 HOH   25 525 125 HOH   HOH B . 
H 4 HOH   26 526 34  HOH   HOH B . 
H 4 HOH   27 527 5   HOH   HOH B . 
H 4 HOH   28 528 27  HOH   HOH B . 
H 4 HOH   29 529 28  HOH   HOH B . 
H 4 HOH   30 530 25  HOH   HOH B . 
H 4 HOH   31 531 111 HOH   HOH B . 
H 4 HOH   32 532 63  HOH   HOH B . 
H 4 HOH   33 533 104 HOH   HOH B . 
H 4 HOH   34 534 72  HOH   HOH B . 
H 4 HOH   35 535 64  HOH   HOH B . 
H 4 HOH   36 536 23  HOH   HOH B . 
H 4 HOH   37 537 44  HOH   HOH B . 
H 4 HOH   38 538 8   HOH   HOH B . 
H 4 HOH   39 539 76  HOH   HOH B . 
H 4 HOH   40 540 53  HOH   HOH B . 
H 4 HOH   41 541 100 HOH   HOH B . 
H 4 HOH   42 542 52  HOH   HOH B . 
H 4 HOH   43 543 79  HOH   HOH B . 
H 4 HOH   44 544 95  HOH   HOH B . 
H 4 HOH   45 545 54  HOH   HOH B . 
H 4 HOH   46 546 51  HOH   HOH B . 
H 4 HOH   47 547 81  HOH   HOH B . 
H 4 HOH   48 548 84  HOH   HOH B . 
H 4 HOH   49 549 67  HOH   HOH B . 
H 4 HOH   50 550 35  HOH   HOH B . 
H 4 HOH   51 551 102 HOH   HOH B . 
H 4 HOH   52 552 88  HOH   HOH B . 
H 4 HOH   53 553 124 HOH   HOH B . 
H 4 HOH   54 554 103 HOH   HOH B . 
H 4 HOH   55 555 123 HOH   HOH B . 
H 4 HOH   56 556 38  HOH   HOH B . 
H 4 HOH   57 557 68  HOH   HOH B . 
H 4 HOH   58 558 82  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 25  ? CG  ? A LYS 3   CG  
2   1 Y 1 A LYS 25  ? CD  ? A LYS 3   CD  
3   1 Y 1 A LYS 25  ? CE  ? A LYS 3   CE  
4   1 Y 1 A LYS 25  ? NZ  ? A LYS 3   NZ  
5   1 Y 1 A GLU 46  ? OE1 ? A GLU 24  OE1 
6   1 Y 1 A GLU 46  ? OE2 ? A GLU 24  OE2 
7   1 Y 1 A LYS 48  ? CG  ? A LYS 26  CG  
8   1 Y 1 A LYS 48  ? CD  ? A LYS 26  CD  
9   1 Y 1 A LYS 48  ? CE  ? A LYS 26  CE  
10  1 Y 1 A LYS 48  ? NZ  ? A LYS 26  NZ  
11  1 Y 1 A ARG 49  ? CG  ? A ARG 27  CG  
12  1 Y 1 A ARG 49  ? CD  ? A ARG 27  CD  
13  1 Y 1 A ARG 49  ? NE  ? A ARG 27  NE  
14  1 Y 1 A ARG 49  ? CZ  ? A ARG 27  CZ  
15  1 Y 1 A ARG 49  ? NH1 ? A ARG 27  NH1 
16  1 Y 1 A ARG 49  ? NH2 ? A ARG 27  NH2 
17  1 Y 1 A ILE 58  ? CD1 ? A ILE 36  CD1 
18  1 Y 1 A GLU 85  ? CG  ? A GLU 63  CG  
19  1 Y 1 A GLU 85  ? CD  ? A GLU 63  CD  
20  1 Y 1 A GLU 85  ? OE1 ? A GLU 63  OE1 
21  1 Y 1 A GLU 85  ? OE2 ? A GLU 63  OE2 
22  1 Y 1 A VAL 86  ? CG1 ? A VAL 64  CG1 
23  1 Y 1 A VAL 86  ? CG2 ? A VAL 64  CG2 
24  1 Y 1 A ILE 87  ? CD1 ? A ILE 65  CD1 
25  1 Y 1 A LYS 91  ? CG  ? A LYS 69  CG  
26  1 Y 1 A LYS 91  ? CD  ? A LYS 69  CD  
27  1 Y 1 A LYS 91  ? CE  ? A LYS 69  CE  
28  1 Y 1 A LYS 91  ? NZ  ? A LYS 69  NZ  
29  1 Y 1 A LYS 129 ? CG  ? A LYS 107 CG  
30  1 Y 1 A LYS 129 ? CD  ? A LYS 107 CD  
31  1 Y 1 A LYS 129 ? CE  ? A LYS 107 CE  
32  1 Y 1 A LYS 129 ? NZ  ? A LYS 107 NZ  
33  1 Y 1 A LEU 152 ? CG  ? A LEU 130 CG  
34  1 Y 1 A LEU 152 ? CD1 ? A LEU 130 CD1 
35  1 Y 1 A LEU 152 ? CD2 ? A LEU 130 CD2 
36  1 Y 1 A GLU 154 ? CG  ? A GLU 132 CG  
37  1 Y 1 A GLU 154 ? CD  ? A GLU 132 CD  
38  1 Y 1 A GLU 154 ? OE1 ? A GLU 132 OE1 
39  1 Y 1 A GLU 154 ? OE2 ? A GLU 132 OE2 
40  1 Y 1 A VAL 157 ? CG1 ? A VAL 135 CG1 
41  1 Y 1 A VAL 157 ? CG2 ? A VAL 135 CG2 
42  1 Y 1 A ARG 158 ? CG  ? A ARG 136 CG  
43  1 Y 1 A ARG 158 ? CD  ? A ARG 136 CD  
44  1 Y 1 A ARG 158 ? NE  ? A ARG 136 NE  
45  1 Y 1 A ARG 158 ? CZ  ? A ARG 136 CZ  
46  1 Y 1 A ARG 158 ? NH1 ? A ARG 136 NH1 
47  1 Y 1 A ARG 158 ? NH2 ? A ARG 136 NH2 
48  1 Y 1 A LYS 162 ? CE  ? A LYS 140 CE  
49  1 Y 1 A LYS 162 ? NZ  ? A LYS 140 NZ  
50  1 Y 1 A SER 168 ? OG  ? A SER 146 OG  
51  1 Y 1 A GLU 171 ? CG  ? A GLU 149 CG  
52  1 Y 1 A GLU 171 ? CD  ? A GLU 149 CD  
53  1 Y 1 A GLU 171 ? OE1 ? A GLU 149 OE1 
54  1 Y 1 A GLU 171 ? OE2 ? A GLU 149 OE2 
55  1 Y 1 A ILE 176 ? CD1 ? A ILE 154 CD1 
56  1 Y 1 A LYS 181 ? CE  ? A LYS 159 CE  
57  1 Y 1 A LYS 181 ? NZ  ? A LYS 159 NZ  
58  1 Y 1 A ARG 195 ? NE  ? A ARG 173 NE  
59  1 Y 1 A ARG 195 ? CZ  ? A ARG 173 CZ  
60  1 Y 1 A ARG 195 ? NH1 ? A ARG 173 NH1 
61  1 Y 1 A ARG 195 ? NH2 ? A ARG 173 NH2 
62  1 Y 1 A GLU 200 ? CD  ? A GLU 178 CD  
63  1 Y 1 A GLU 200 ? OE1 ? A GLU 178 OE1 
64  1 Y 1 A GLU 200 ? OE2 ? A GLU 178 OE2 
65  1 Y 1 A SER 202 ? OG  ? A SER 180 OG  
66  1 Y 1 A GLU 212 ? CG  ? A GLU 190 CG  
67  1 Y 1 A GLU 212 ? CD  ? A GLU 190 CD  
68  1 Y 1 A GLU 212 ? OE1 ? A GLU 190 OE1 
69  1 Y 1 A GLU 212 ? OE2 ? A GLU 190 OE2 
70  1 Y 1 A ARG 216 ? CG  ? A ARG 194 CG  
71  1 Y 1 A ARG 216 ? CD  ? A ARG 194 CD  
72  1 Y 1 A ARG 216 ? NE  ? A ARG 194 NE  
73  1 Y 1 A ARG 216 ? CZ  ? A ARG 194 CZ  
74  1 Y 1 A ARG 216 ? NH1 ? A ARG 194 NH1 
75  1 Y 1 A ARG 216 ? NH2 ? A ARG 194 NH2 
76  1 Y 1 A GLN 223 ? CD  ? A GLN 201 CD  
77  1 Y 1 A GLN 223 ? OE1 ? A GLN 201 OE1 
78  1 Y 1 A GLN 223 ? NE2 ? A GLN 201 NE2 
79  1 Y 1 A GLU 227 ? CD  ? A GLU 205 CD  
80  1 Y 1 A GLU 227 ? OE1 ? A GLU 205 OE1 
81  1 Y 1 A GLU 227 ? OE2 ? A GLU 205 OE2 
82  1 Y 1 A VAL 230 ? CG1 ? A VAL 208 CG1 
83  1 Y 1 A VAL 230 ? CG2 ? A VAL 208 CG2 
84  1 Y 1 A LYS 234 ? CE  ? A LYS 212 CE  
85  1 Y 1 A LYS 234 ? NZ  ? A LYS 212 NZ  
86  1 Y 1 A ARG 263 ? NE  ? A ARG 241 NE  
87  1 Y 1 A ARG 263 ? CZ  ? A ARG 241 CZ  
88  1 Y 1 A ARG 263 ? NH1 ? A ARG 241 NH1 
89  1 Y 1 A ARG 263 ? NH2 ? A ARG 241 NH2 
90  1 Y 1 A ARG 287 ? CG  ? A ARG 265 CG  
91  1 Y 1 A ARG 287 ? CD  ? A ARG 265 CD  
92  1 Y 1 A ARG 287 ? NE  ? A ARG 265 NE  
93  1 Y 1 A ARG 287 ? CZ  ? A ARG 265 CZ  
94  1 Y 1 A ARG 287 ? NH1 ? A ARG 265 NH1 
95  1 Y 1 A ARG 287 ? NH2 ? A ARG 265 NH2 
96  1 Y 1 A SER 322 ? OG  ? A SER 300 OG  
97  1 Y 1 A LEU 325 ? CG  ? A LEU 303 CG  
98  1 Y 1 A LEU 325 ? CD1 ? A LEU 303 CD1 
99  1 Y 1 A LEU 325 ? CD2 ? A LEU 303 CD2 
100 1 Y 1 A ARG 343 ? CG  ? A ARG 321 CG  
101 1 Y 1 A ARG 343 ? CD  ? A ARG 321 CD  
102 1 Y 1 A ARG 343 ? NE  ? A ARG 321 NE  
103 1 Y 1 A ARG 343 ? CZ  ? A ARG 321 CZ  
104 1 Y 1 A ARG 343 ? NH1 ? A ARG 321 NH1 
105 1 Y 1 A ARG 343 ? NH2 ? A ARG 321 NH2 
106 1 Y 1 A GLU 361 ? CG  ? A GLU 339 CG  
107 1 Y 1 A GLU 361 ? CD  ? A GLU 339 CD  
108 1 Y 1 A GLU 361 ? OE1 ? A GLU 339 OE1 
109 1 Y 1 A GLU 361 ? OE2 ? A GLU 339 OE2 
110 1 Y 1 B LYS 25  ? CG  ? B LYS 3   CG  
111 1 Y 1 B LYS 25  ? CD  ? B LYS 3   CD  
112 1 Y 1 B LYS 25  ? CE  ? B LYS 3   CE  
113 1 Y 1 B LYS 25  ? NZ  ? B LYS 3   NZ  
114 1 Y 1 B ILE 26  ? CD1 ? B ILE 4   CD1 
115 1 Y 1 B GLU 29  ? CG  ? B GLU 7   CG  
116 1 Y 1 B GLU 29  ? CD  ? B GLU 7   CD  
117 1 Y 1 B GLU 29  ? OE1 ? B GLU 7   OE1 
118 1 Y 1 B GLU 29  ? OE2 ? B GLU 7   OE2 
119 1 Y 1 B LYS 35  ? CE  ? B LYS 13  CE  
120 1 Y 1 B LYS 35  ? NZ  ? B LYS 13  NZ  
121 1 Y 1 B ARG 49  ? CZ  ? B ARG 27  CZ  
122 1 Y 1 B ARG 49  ? NH1 ? B ARG 27  NH1 
123 1 Y 1 B ARG 49  ? NH2 ? B ARG 27  NH2 
124 1 Y 1 B GLU 85  ? CG  ? B GLU 63  CG  
125 1 Y 1 B GLU 85  ? CD  ? B GLU 63  CD  
126 1 Y 1 B GLU 85  ? OE1 ? B GLU 63  OE1 
127 1 Y 1 B GLU 85  ? OE2 ? B GLU 63  OE2 
128 1 Y 1 B VAL 86  ? CG1 ? B VAL 64  CG1 
129 1 Y 1 B VAL 86  ? CG2 ? B VAL 64  CG2 
130 1 Y 1 B LYS 91  ? CG  ? B LYS 69  CG  
131 1 Y 1 B LYS 91  ? CD  ? B LYS 69  CD  
132 1 Y 1 B LYS 91  ? CE  ? B LYS 69  CE  
133 1 Y 1 B LYS 91  ? NZ  ? B LYS 69  NZ  
134 1 Y 1 B LYS 97  ? CE  ? B LYS 75  CE  
135 1 Y 1 B LYS 97  ? NZ  ? B LYS 75  NZ  
136 1 Y 1 B LYS 129 ? CD  ? B LYS 107 CD  
137 1 Y 1 B LYS 129 ? CE  ? B LYS 107 CE  
138 1 Y 1 B LYS 129 ? NZ  ? B LYS 107 NZ  
139 1 Y 1 B LEU 152 ? CG  ? B LEU 130 CG  
140 1 Y 1 B LEU 152 ? CD1 ? B LEU 130 CD1 
141 1 Y 1 B LEU 152 ? CD2 ? B LEU 130 CD2 
142 1 Y 1 B GLU 154 ? CG  ? B GLU 132 CG  
143 1 Y 1 B GLU 154 ? CD  ? B GLU 132 CD  
144 1 Y 1 B GLU 154 ? OE1 ? B GLU 132 OE1 
145 1 Y 1 B GLU 154 ? OE2 ? B GLU 132 OE2 
146 1 Y 1 B SER 168 ? OG  ? B SER 146 OG  
147 1 Y 1 B GLU 170 ? CG  ? B GLU 148 CG  
148 1 Y 1 B GLU 170 ? CD  ? B GLU 148 CD  
149 1 Y 1 B GLU 170 ? OE1 ? B GLU 148 OE1 
150 1 Y 1 B GLU 170 ? OE2 ? B GLU 148 OE2 
151 1 Y 1 B GLU 171 ? CG  ? B GLU 149 CG  
152 1 Y 1 B GLU 171 ? CD  ? B GLU 149 CD  
153 1 Y 1 B GLU 171 ? OE1 ? B GLU 149 OE1 
154 1 Y 1 B GLU 171 ? OE2 ? B GLU 149 OE2 
155 1 Y 1 B LYS 181 ? CG  ? B LYS 159 CG  
156 1 Y 1 B LYS 181 ? CD  ? B LYS 159 CD  
157 1 Y 1 B LYS 181 ? CE  ? B LYS 159 CE  
158 1 Y 1 B LYS 181 ? NZ  ? B LYS 159 NZ  
159 1 Y 1 B GLU 187 ? CD  ? B GLU 165 CD  
160 1 Y 1 B GLU 187 ? OE1 ? B GLU 165 OE1 
161 1 Y 1 B GLU 187 ? OE2 ? B GLU 165 OE2 
162 1 Y 1 B ARG 191 ? CD  ? B ARG 169 CD  
163 1 Y 1 B ARG 191 ? NE  ? B ARG 169 NE  
164 1 Y 1 B ARG 191 ? CZ  ? B ARG 169 CZ  
165 1 Y 1 B ARG 191 ? NH1 ? B ARG 169 NH1 
166 1 Y 1 B ARG 191 ? NH2 ? B ARG 169 NH2 
167 1 Y 1 B ARG 195 ? NE  ? B ARG 173 NE  
168 1 Y 1 B ARG 195 ? CZ  ? B ARG 173 CZ  
169 1 Y 1 B ARG 195 ? NH1 ? B ARG 173 NH1 
170 1 Y 1 B ARG 195 ? NH2 ? B ARG 173 NH2 
171 1 Y 1 B GLU 200 ? CG  ? B GLU 178 CG  
172 1 Y 1 B GLU 200 ? CD  ? B GLU 178 CD  
173 1 Y 1 B GLU 200 ? OE1 ? B GLU 178 OE1 
174 1 Y 1 B GLU 200 ? OE2 ? B GLU 178 OE2 
175 1 Y 1 B GLU 201 ? CG  ? B GLU 179 CG  
176 1 Y 1 B GLU 201 ? CD  ? B GLU 179 CD  
177 1 Y 1 B GLU 201 ? OE1 ? B GLU 179 OE1 
178 1 Y 1 B GLU 201 ? OE2 ? B GLU 179 OE2 
179 1 Y 1 B SER 202 ? OG  ? B SER 180 OG  
180 1 Y 1 B ASN 205 ? CG  ? B ASN 183 CG  
181 1 Y 1 B ASN 205 ? OD1 ? B ASN 183 OD1 
182 1 Y 1 B ASN 205 ? ND2 ? B ASN 183 ND2 
183 1 Y 1 B LYS 209 ? CG  ? B LYS 187 CG  
184 1 Y 1 B LYS 209 ? CD  ? B LYS 187 CD  
185 1 Y 1 B LYS 209 ? CE  ? B LYS 187 CE  
186 1 Y 1 B LYS 209 ? NZ  ? B LYS 187 NZ  
187 1 Y 1 B GLU 212 ? CD  ? B GLU 190 CD  
188 1 Y 1 B GLU 212 ? OE1 ? B GLU 190 OE1 
189 1 Y 1 B GLU 212 ? OE2 ? B GLU 190 OE2 
190 1 Y 1 B ARG 216 ? CG  ? B ARG 194 CG  
191 1 Y 1 B ARG 216 ? CD  ? B ARG 194 CD  
192 1 Y 1 B ARG 216 ? NE  ? B ARG 194 NE  
193 1 Y 1 B ARG 216 ? CZ  ? B ARG 194 CZ  
194 1 Y 1 B ARG 216 ? NH1 ? B ARG 194 NH1 
195 1 Y 1 B ARG 216 ? NH2 ? B ARG 194 NH2 
196 1 Y 1 B LEU 218 ? CG  ? B LEU 196 CG  
197 1 Y 1 B LEU 218 ? CD1 ? B LEU 196 CD1 
198 1 Y 1 B LEU 218 ? CD2 ? B LEU 196 CD2 
199 1 Y 1 B GLU 219 ? CG  ? B GLU 197 CG  
200 1 Y 1 B GLU 219 ? CD  ? B GLU 197 CD  
201 1 Y 1 B GLU 219 ? OE1 ? B GLU 197 OE1 
202 1 Y 1 B GLU 219 ? OE2 ? B GLU 197 OE2 
203 1 Y 1 B VAL 222 ? CG1 ? B VAL 200 CG1 
204 1 Y 1 B VAL 222 ? CG2 ? B VAL 200 CG2 
205 1 Y 1 B GLN 223 ? CG  ? B GLN 201 CG  
206 1 Y 1 B GLN 223 ? CD  ? B GLN 201 CD  
207 1 Y 1 B GLN 223 ? OE1 ? B GLN 201 OE1 
208 1 Y 1 B GLN 223 ? NE2 ? B GLN 201 NE2 
209 1 Y 1 B SER 224 ? OG  ? B SER 202 OG  
210 1 Y 1 B MET 226 ? SD  ? B MET 204 SD  
211 1 Y 1 B MET 226 ? CE  ? B MET 204 CE  
212 1 Y 1 B GLU 227 ? CG  ? B GLU 205 CG  
213 1 Y 1 B GLU 227 ? CD  ? B GLU 205 CD  
214 1 Y 1 B GLU 227 ? OE1 ? B GLU 205 OE1 
215 1 Y 1 B GLU 227 ? OE2 ? B GLU 205 OE2 
216 1 Y 1 B GLU 228 ? CG  ? B GLU 206 CG  
217 1 Y 1 B GLU 228 ? CD  ? B GLU 206 CD  
218 1 Y 1 B GLU 228 ? OE1 ? B GLU 206 OE1 
219 1 Y 1 B GLU 228 ? OE2 ? B GLU 206 OE2 
220 1 Y 1 B VAL 230 ? CG1 ? B VAL 208 CG1 
221 1 Y 1 B VAL 230 ? CG2 ? B VAL 208 CG2 
222 1 Y 1 B GLU 231 ? CG  ? B GLU 209 CG  
223 1 Y 1 B GLU 231 ? CD  ? B GLU 209 CD  
224 1 Y 1 B GLU 231 ? OE1 ? B GLU 209 OE1 
225 1 Y 1 B GLU 231 ? OE2 ? B GLU 209 OE2 
226 1 Y 1 B LYS 232 ? CG  ? B LYS 210 CG  
227 1 Y 1 B LYS 232 ? CD  ? B LYS 210 CD  
228 1 Y 1 B LYS 232 ? CE  ? B LYS 210 CE  
229 1 Y 1 B LYS 232 ? NZ  ? B LYS 210 NZ  
230 1 Y 1 B LYS 234 ? CG  ? B LYS 212 CG  
231 1 Y 1 B LYS 234 ? CD  ? B LYS 212 CD  
232 1 Y 1 B LYS 234 ? CE  ? B LYS 212 CE  
233 1 Y 1 B LYS 234 ? NZ  ? B LYS 212 NZ  
234 1 Y 1 B ASN 235 ? CG  ? B ASN 213 CG  
235 1 Y 1 B ASN 235 ? OD1 ? B ASN 213 OD1 
236 1 Y 1 B ASN 235 ? ND2 ? B ASN 213 ND2 
237 1 Y 1 B LEU 238 ? CG  ? B LEU 216 CG  
238 1 Y 1 B LEU 238 ? CD1 ? B LEU 216 CD1 
239 1 Y 1 B LEU 238 ? CD2 ? B LEU 216 CD2 
240 1 Y 1 B GLU 242 ? CG  ? B GLU 220 CG  
241 1 Y 1 B GLU 242 ? CD  ? B GLU 220 CD  
242 1 Y 1 B GLU 242 ? OE1 ? B GLU 220 OE1 
243 1 Y 1 B GLU 242 ? OE2 ? B GLU 220 OE2 
244 1 Y 1 B ARG 245 ? CG  ? B ARG 223 CG  
245 1 Y 1 B ARG 245 ? CD  ? B ARG 223 CD  
246 1 Y 1 B ARG 245 ? NE  ? B ARG 223 NE  
247 1 Y 1 B ARG 245 ? CZ  ? B ARG 223 CZ  
248 1 Y 1 B ARG 245 ? NH1 ? B ARG 223 NH1 
249 1 Y 1 B ARG 245 ? NH2 ? B ARG 223 NH2 
250 1 Y 1 B GLU 246 ? CD  ? B GLU 224 CD  
251 1 Y 1 B GLU 246 ? OE1 ? B GLU 224 OE1 
252 1 Y 1 B GLU 246 ? OE2 ? B GLU 224 OE2 
253 1 Y 1 B ARG 249 ? CG  ? B ARG 227 CG  
254 1 Y 1 B ARG 249 ? CD  ? B ARG 227 CD  
255 1 Y 1 B ARG 249 ? NE  ? B ARG 227 NE  
256 1 Y 1 B ARG 249 ? CZ  ? B ARG 227 CZ  
257 1 Y 1 B ARG 249 ? NH1 ? B ARG 227 NH1 
258 1 Y 1 B ARG 249 ? NH2 ? B ARG 227 NH2 
259 1 Y 1 B VAL 256 ? CG1 ? B VAL 234 CG1 
260 1 Y 1 B VAL 256 ? CG2 ? B VAL 234 CG2 
261 1 Y 1 B LEU 260 ? CD1 ? B LEU 238 CD1 
262 1 Y 1 B LEU 260 ? CD2 ? B LEU 238 CD2 
263 1 Y 1 B ARG 262 ? CG  ? B ARG 240 CG  
264 1 Y 1 B ARG 262 ? CD  ? B ARG 240 CD  
265 1 Y 1 B ARG 262 ? NE  ? B ARG 240 NE  
266 1 Y 1 B ARG 262 ? CZ  ? B ARG 240 CZ  
267 1 Y 1 B ARG 262 ? NH1 ? B ARG 240 NH1 
268 1 Y 1 B ARG 262 ? NH2 ? B ARG 240 NH2 
269 1 Y 1 B ARG 263 ? CD  ? B ARG 241 CD  
270 1 Y 1 B ARG 263 ? NE  ? B ARG 241 NE  
271 1 Y 1 B ARG 263 ? CZ  ? B ARG 241 CZ  
272 1 Y 1 B ARG 263 ? NH1 ? B ARG 241 NH1 
273 1 Y 1 B ARG 263 ? NH2 ? B ARG 241 NH2 
274 1 Y 1 B ARG 271 ? CG  ? B ARG 249 CG  
275 1 Y 1 B ARG 271 ? CD  ? B ARG 249 CD  
276 1 Y 1 B ARG 271 ? NE  ? B ARG 249 NE  
277 1 Y 1 B ARG 271 ? CZ  ? B ARG 249 CZ  
278 1 Y 1 B ARG 271 ? NH1 ? B ARG 249 NH1 
279 1 Y 1 B ARG 271 ? NH2 ? B ARG 249 NH2 
280 1 Y 1 B ARG 287 ? CG  ? B ARG 265 CG  
281 1 Y 1 B ARG 287 ? CD  ? B ARG 265 CD  
282 1 Y 1 B ARG 287 ? NE  ? B ARG 265 NE  
283 1 Y 1 B ARG 287 ? CZ  ? B ARG 265 CZ  
284 1 Y 1 B ARG 287 ? NH1 ? B ARG 265 NH1 
285 1 Y 1 B ARG 287 ? NH2 ? B ARG 265 NH2 
286 1 Y 1 B ARG 337 ? NE  ? B ARG 315 NE  
287 1 Y 1 B ARG 337 ? CZ  ? B ARG 315 CZ  
288 1 Y 1 B ARG 337 ? NH1 ? B ARG 315 NH1 
289 1 Y 1 B ARG 337 ? NH2 ? B ARG 315 NH2 
290 1 Y 1 B GLU 361 ? CG  ? B GLU 339 CG  
291 1 Y 1 B GLU 361 ? CD  ? B GLU 339 CD  
292 1 Y 1 B GLU 361 ? OE1 ? B GLU 339 OE1 
293 1 Y 1 B GLU 361 ? OE2 ? B GLU 339 OE2 
294 1 Y 1 B GLU 368 ? CG  ? B GLU 346 CG  
295 1 Y 1 B GLU 368 ? CD  ? B GLU 346 CD  
296 1 Y 1 B GLU 368 ? OE1 ? B GLU 346 OE1 
297 1 Y 1 B GLU 368 ? OE2 ? B GLU 346 OE2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FON 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     119.543 
_cell.length_a_esd                 ? 
_cell.length_b                     119.543 
_cell.length_b_esd                 ? 
_cell.length_c                     101.804 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9FON 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FON 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.27 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Morpheus screen I, condition B12' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-03-28 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0007 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0007 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FON 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.12 
_reflns.d_resolution_low                               103.5 
_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                                     42135 
_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                           95.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.110 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.099 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.12 
_reflns_shell.d_res_low                                     2.240 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2107 
_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                               1.538 
_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                                  0.657 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          59.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.388 
_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]                            0.3372 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.3372 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.6744 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               46.77 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.939 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_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                                 9FON 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.121 
_refine.ls_d_res_low                             39.13 
_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                     42126 
_refine.ls_number_reflns_R_free                  2097 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2326 
_refine.ls_R_factor_R_free                       0.2565 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2314 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.207 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.203 
_refine.pdbx_overall_SU_R_Blow_DPI               0.267 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.275 
_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_analyze.entry_id                        9FON 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.33 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.121 
_refine_hist.d_res_low                        39.13 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               5644 
_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        5404 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         132 
_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' ? 0.008 ? 5681 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.8   ? 7719 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1956 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1026 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 5681 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 733  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4504 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.65  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 16.3  ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.121 
_refine_ls_shell.d_res_low                        2.19 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             32 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               18.67 
_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                  0.2943 
_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                  0.3216 
# 
_struct.entry_id                     9FON 
_struct.title                        'Cocrystal structure of Drosophila melangaster TDO with Compound 128' 
_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        9FON 
_struct_keywords.text            'Inhibitor, heme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    T23O_DROME 
_struct_ref.pdbx_db_accession          P20351 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVV
LILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDP
SLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRR
GDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDR
YKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSV
;
_struct_ref.pdbx_align_begin           24 
# 
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 9FON A 2 ? 357 ? P20351 24 ? 379 ? 24 379 
2 1 9FON B 2 ? 357 ? P20351 24 ? 379 ? 24 379 
# 
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 9FON MET A 1   ? UNP P20351 ? ? 'initiating methionine' 23  1  
1 9FON LEU A 358 ? UNP P20351 ? ? 'expression tag'        380 2  
1 9FON GLU A 359 ? UNP P20351 ? ? 'expression tag'        381 3  
1 9FON HIS A 360 ? UNP P20351 ? ? 'expression tag'        382 4  
1 9FON HIS A 361 ? UNP P20351 ? ? 'expression tag'        383 5  
1 9FON HIS A 362 ? UNP P20351 ? ? 'expression tag'        384 6  
1 9FON HIS A 363 ? UNP P20351 ? ? 'expression tag'        385 7  
1 9FON HIS A 364 ? UNP P20351 ? ? 'expression tag'        386 8  
1 9FON HIS A 365 ? UNP P20351 ? ? 'expression tag'        387 9  
2 9FON MET B 1   ? UNP P20351 ? ? 'initiating methionine' 23  10 
2 9FON LEU B 358 ? UNP P20351 ? ? 'expression tag'        380 11 
2 9FON GLU B 359 ? UNP P20351 ? ? 'expression tag'        381 12 
2 9FON HIS B 360 ? UNP P20351 ? ? 'expression tag'        382 13 
2 9FON HIS B 361 ? UNP P20351 ? ? 'expression tag'        383 14 
2 9FON HIS B 362 ? UNP P20351 ? ? 'expression tag'        384 15 
2 9FON HIS B 363 ? UNP P20351 ? ? 'expression tag'        385 16 
2 9FON HIS B 364 ? UNP P20351 ? ? 'expression tag'        386 17 
2 9FON HIS B 365 ? UNP P20351 ? ? 'expression tag'        387 18 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 25580 ? 
1 MORE         -218  ? 
1 'SSA (A^2)'  51370 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z              1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 6_765 -x+2,-x+y+1,-z+2/3 -0.5000000000 -0.8660254038 0.0000000000 179.3145000000 -0.8660254038 
0.5000000000 0.0000000000 103.5272748446 0.0000000000 0.0000000000 -1.0000000000 67.8693333333 
# 
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 ILE A 4   ? LEU A 9   ? ILE A 26  LEU A 31  1 ? 6  
HELX_P HELX_P2  AA2 MET A 10  ? LEU A 15  ? MET A 32  LEU A 37  1 ? 6  
HELX_P HELX_P3  AA3 MET A 20  ? ASP A 25  ? MET A 42  ASP A 47  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 31  ? ASP A 61  ? ASP A 53  ASP A 83  1 ? 31 
HELX_P HELX_P5  AA5 ASP A 66  ? GLN A 90  ? ASP A 88  GLN A 112 1 ? 25 
HELX_P HELX_P6  AA6 GLN A 90  ? GLU A 95  ? GLN A 112 GLU A 117 1 ? 6  
HELX_P HELX_P7  AA7 THR A 98  ? LYS A 107 ? THR A 120 LYS A 129 1 ? 10 
HELX_P HELX_P8  AA8 SER A 113 ? GLN A 116 ? SER A 135 GLN A 138 5 ? 4  
HELX_P HELX_P9  AA9 SER A 117 ? GLY A 128 ? SER A 139 GLY A 150 1 ? 12 
HELX_P HELX_P10 AB1 LEU A 130 ? ARG A 134 ? LEU A 152 ARG A 156 5 ? 5  
HELX_P HELX_P11 AB2 LYS A 140 ? PHE A 145 ? LYS A 162 PHE A 167 5 ? 6  
HELX_P HELX_P12 AB3 ASP A 147 ? ASP A 160 ? ASP A 169 ASP A 182 1 ? 14 
HELX_P HELX_P13 AB4 SER A 162 ? ARG A 173 ? SER A 184 ARG A 195 1 ? 12 
HELX_P HELX_P14 AB5 ASN A 183 ? GLU A 205 ? ASN A 205 GLU A 227 1 ? 23 
HELX_P HELX_P15 AB6 VAL A 208 ? ASP A 231 ? VAL A 230 ASP A 253 1 ? 24 
HELX_P HELX_P16 AB7 ASP A 231 ? ARG A 241 ? ASP A 253 ARG A 263 1 ? 11 
HELX_P HELX_P17 AB8 SER A 247 ? TYR A 260 ? SER A 269 TYR A 282 1 ? 14 
HELX_P HELX_P18 AB9 GLU A 263 ? GLY A 299 ? GLU A 285 GLY A 321 1 ? 37 
HELX_P HELX_P19 AC1 SER A 308 ? THR A 317 ? SER A 330 THR A 339 1 ? 10 
HELX_P HELX_P20 AC2 LEU A 318 ? LYS A 323 ? LEU A 340 LYS A 345 5 ? 6  
HELX_P HELX_P21 AC3 PHE A 325 ? ASN A 330 ? PHE A 347 ASN A 352 1 ? 6  
HELX_P HELX_P22 AC4 LEU A 331 ? LEU A 335 ? LEU A 353 LEU A 357 5 ? 5  
HELX_P HELX_P23 AC5 PRO A 337 ? ILE A 341 ? PRO A 359 ILE A 363 5 ? 5  
HELX_P HELX_P24 AC6 ILE B 4   ? LEU B 9   ? ILE B 26  LEU B 31  1 ? 6  
HELX_P HELX_P25 AC7 MET B 10  ? LEU B 15  ? MET B 32  LEU B 37  1 ? 6  
HELX_P HELX_P26 AC8 MET B 20  ? ASP B 25  ? MET B 42  ASP B 47  1 ? 6  
HELX_P HELX_P27 AC9 HIS B 30  ? ASP B 61  ? HIS B 52  ASP B 83  1 ? 32 
HELX_P HELX_P28 AD1 ASP B 66  ? GLN B 90  ? ASP B 88  GLN B 112 1 ? 25 
HELX_P HELX_P29 AD2 GLN B 90  ? GLU B 95  ? GLN B 112 GLU B 117 1 ? 6  
HELX_P HELX_P30 AD3 THR B 98  ? LYS B 107 ? THR B 120 LYS B 129 1 ? 10 
HELX_P HELX_P31 AD4 SER B 113 ? GLN B 116 ? SER B 135 GLN B 138 5 ? 4  
HELX_P HELX_P32 AD5 SER B 117 ? GLY B 128 ? SER B 139 GLY B 150 1 ? 12 
HELX_P HELX_P33 AD6 LEU B 130 ? ARG B 134 ? LEU B 152 ARG B 156 5 ? 5  
HELX_P HELX_P34 AD7 LYS B 140 ? PHE B 145 ? LYS B 162 PHE B 167 5 ? 6  
HELX_P HELX_P35 AD8 ASP B 147 ? ASP B 160 ? ASP B 169 ASP B 182 1 ? 14 
HELX_P HELX_P36 AD9 SER B 162 ? ARG B 173 ? SER B 184 ARG B 195 1 ? 12 
HELX_P HELX_P37 AE1 ASN B 183 ? GLU B 205 ? ASN B 205 GLU B 227 1 ? 23 
HELX_P HELX_P38 AE2 VAL B 208 ? ASP B 231 ? VAL B 230 ASP B 253 1 ? 24 
HELX_P HELX_P39 AE3 ASP B 231 ? ARG B 241 ? ASP B 253 ARG B 263 1 ? 11 
HELX_P HELX_P40 AE4 SER B 247 ? TYR B 260 ? SER B 269 TYR B 282 1 ? 14 
HELX_P HELX_P41 AE5 GLU B 263 ? GLY B 299 ? GLU B 285 GLY B 321 1 ? 37 
HELX_P HELX_P42 AE6 SER B 308 ? THR B 317 ? SER B 330 THR B 339 1 ? 10 
HELX_P HELX_P43 AE7 LEU B 318 ? LYS B 323 ? LEU B 340 LYS B 345 5 ? 6  
HELX_P HELX_P44 AE8 PHE B 325 ? ASN B 330 ? PHE B 347 ASN B 352 1 ? 6  
HELX_P HELX_P45 AE9 LEU B 331 ? LEU B 335 ? LEU B 353 LEU B 357 5 ? 5  
HELX_P HELX_P46 AF1 PRO B 337 ? ILE B 341 ? PRO B 359 ILE B 363 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 290 NE2 ? ? ? 1_555 C HEM   . FE  ? ? A HIS 312 A HEM   401 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1IER . N21 ? ? A HEM 401 A A1IER 402 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc3 metalc ? ? B HIS 290 NE2 ? ? ? 1_555 E HEM   . FE  ? ? B HIS 312 B HEM   401 1_555 ? ? ? ? ? ? ? 2.132 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1IER . N21 ? ? B HEM 401 B A1IER 402 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NA  ? C HEM   . ? A HEM   401 ? 1_555 92.4  ? 
2  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB  ? C HEM   . ? A HEM   401 ? 1_555 95.9  ? 
3  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB  ? C HEM   . ? A HEM   401 ? 1_555 90.0  ? 
4  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC  ? C HEM   . ? A HEM   401 ? 1_555 88.5  ? 
5  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC  ? C HEM   . ? A HEM   401 ? 1_555 178.7 ? 
6  NB  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC  ? C HEM   . ? A HEM   401 ? 1_555 89.1  ? 
7  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND  ? C HEM   . ? A HEM   401 ? 1_555 88.4  ? 
8  NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND  ? C HEM   . ? A HEM   401 ? 1_555 90.5  ? 
9  NB  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND  ? C HEM   . ? A HEM   401 ? 1_555 175.6 ? 
10 NC  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND  ? C HEM   . ? A HEM   401 ? 1_555 90.4  ? 
11 NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 N21 ? D A1IER . ? A A1IER 402 ? 1_555 174.6 ? 
12 NA  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 N21 ? D A1IER . ? A A1IER 402 ? 1_555 91.0  ? 
13 NB  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 N21 ? D A1IER . ? A A1IER 402 ? 1_555 88.3  ? 
14 NC  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 N21 ? D A1IER . ? A A1IER 402 ? 1_555 88.2  ? 
15 ND  ? C HEM .   ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 N21 ? D A1IER . ? A A1IER 402 ? 1_555 87.3  ? 
16 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NA  ? E HEM   . ? B HEM   401 ? 1_555 93.3  ? 
17 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NB  ? E HEM   . ? B HEM   401 ? 1_555 97.0  ? 
18 NA  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NB  ? E HEM   . ? B HEM   401 ? 1_555 90.7  ? 
19 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NC  ? E HEM   . ? B HEM   401 ? 1_555 88.7  ? 
20 NA  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NC  ? E HEM   . ? B HEM   401 ? 1_555 178.0 ? 
21 NB  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 NC  ? E HEM   . ? B HEM   401 ? 1_555 88.8  ? 
22 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 ND  ? E HEM   . ? B HEM   401 ? 1_555 88.1  ? 
23 NA  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 ND  ? E HEM   . ? B HEM   401 ? 1_555 91.4  ? 
24 NB  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 ND  ? E HEM   . ? B HEM   401 ? 1_555 174.4 ? 
25 NC  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 ND  ? E HEM   . ? B HEM   401 ? 1_555 88.9  ? 
26 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 N21 ? F A1IER . ? B A1IER 402 ? 1_555 173.7 ? 
27 NA  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 N21 ? F A1IER . ? B A1IER 402 ? 1_555 90.9  ? 
28 NB  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 N21 ? F A1IER . ? B A1IER 402 ? 1_555 87.7  ? 
29 NC  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 N21 ? F A1IER . ? B A1IER 402 ? 1_555 87.1  ? 
30 ND  ? E HEM .   ? B HEM 401 ? 1_555 FE ? E HEM . ? B HEM 401 ? 1_555 N21 ? F A1IER . ? B A1IER 402 ? 1_555 87.1  ? 
# 
_pdbx_entry_details.entry_id                   9FON 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 132 ? ? 33.15   -89.02 
2 1 PHE A 347 ? ? -99.91  47.67  
3 1 ALA B 132 ? ? 34.57   -87.96 
4 1 ASN B 160 ? ? -149.31 -78.42 
5 1 PHE B 347 ? ? -98.73  48.43  
# 
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 MET 23  ? A MET 1   
2  1 Y 1 A GLY 24  ? A GLY 2   
3  1 Y 1 A TYR 159 ? A TYR 137 
4  1 Y 1 A ASN 160 ? A ASN 138 
5  1 Y 1 A ASP 367 ? A ASP 345 
6  1 Y 1 A GLU 368 ? A GLU 346 
7  1 Y 1 A THR 369 ? A THR 347 
8  1 Y 1 A ILE 370 ? A ILE 348 
9  1 Y 1 A ARG 371 ? A ARG 349 
10 1 Y 1 A LYS 372 ? A LYS 350 
11 1 Y 1 A LYS 373 ? A LYS 351 
12 1 Y 1 A LEU 374 ? A LEU 352 
13 1 Y 1 A ILE 375 ? A ILE 353 
14 1 Y 1 A ASN 376 ? A ASN 354 
15 1 Y 1 A LYS 377 ? A LYS 355 
16 1 Y 1 A SER 378 ? A SER 356 
17 1 Y 1 A VAL 379 ? A VAL 357 
18 1 Y 1 A LEU 380 ? A LEU 358 
19 1 Y 1 A GLU 381 ? A GLU 359 
20 1 Y 1 A HIS 382 ? A HIS 360 
21 1 Y 1 A HIS 383 ? A HIS 361 
22 1 Y 1 A HIS 384 ? A HIS 362 
23 1 Y 1 A HIS 385 ? A HIS 363 
24 1 Y 1 A HIS 386 ? A HIS 364 
25 1 Y 1 A HIS 387 ? A HIS 365 
26 1 Y 1 B MET 23  ? B MET 1   
27 1 Y 1 B GLY 24  ? B GLY 2   
28 1 Y 1 B THR 369 ? B THR 347 
29 1 Y 1 B ILE 370 ? B ILE 348 
30 1 Y 1 B ARG 371 ? B ARG 349 
31 1 Y 1 B LYS 372 ? B LYS 350 
32 1 Y 1 B LYS 373 ? B LYS 351 
33 1 Y 1 B LEU 374 ? B LEU 352 
34 1 Y 1 B ILE 375 ? B ILE 353 
35 1 Y 1 B ASN 376 ? B ASN 354 
36 1 Y 1 B LYS 377 ? B LYS 355 
37 1 Y 1 B SER 378 ? B SER 356 
38 1 Y 1 B VAL 379 ? B VAL 357 
39 1 Y 1 B LEU 380 ? B LEU 358 
40 1 Y 1 B GLU 381 ? B GLU 359 
41 1 Y 1 B HIS 382 ? B HIS 360 
42 1 Y 1 B HIS 383 ? B HIS 361 
43 1 Y 1 B HIS 384 ? B HIS 362 
44 1 Y 1 B HIS 385 ? B HIS 363 
45 1 Y 1 B HIS 386 ? B HIS 364 
46 1 Y 1 B HIS 387 ? B HIS 365 
# 
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 
A1IER C4   C  Y N 1   
A1IER C6   C  Y N 2   
A1IER C7   C  Y N 3   
A1IER C8   C  Y N 4   
A1IER C10  C  Y N 5   
A1IER N12  N  Y N 6   
A1IER C15  C  Y N 7   
A1IER C20  C  Y N 8   
A1IER C22  C  Y N 9   
A1IER O1   O  N N 10  
A1IER C2   C  N R 11  
A1IER C3   C  Y N 12  
A1IER N5   N  Y N 13  
A1IER C9   C  Y N 14  
A1IER C11  C  Y N 15  
A1IER N13  N  Y N 16  
A1IER C14  C  Y N 17  
A1IER C16  C  Y N 18  
A1IER CL17 CL N N 19  
A1IER C18  C  Y N 20  
A1IER C19  C  Y N 21  
A1IER N21  N  Y N 22  
A1IER N23  N  Y N 23  
A1IER H4   H  N N 24  
A1IER H7   H  N N 25  
A1IER H8   H  N N 26  
A1IER H10  H  N N 27  
A1IER H15  H  N N 28  
A1IER H20  H  N N 29  
A1IER H22  H  N N 30  
A1IER H1   H  N N 31  
A1IER H2   H  N N 32  
A1IER H9   H  N N 33  
A1IER H11  H  N N 34  
A1IER H18  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HEM   CHA  C  N N 172 
HEM   CHB  C  N N 173 
HEM   CHC  C  N N 174 
HEM   CHD  C  N N 175 
HEM   C1A  C  Y N 176 
HEM   C2A  C  Y N 177 
HEM   C3A  C  Y N 178 
HEM   C4A  C  Y N 179 
HEM   CMA  C  N N 180 
HEM   CAA  C  N N 181 
HEM   CBA  C  N N 182 
HEM   CGA  C  N N 183 
HEM   O1A  O  N N 184 
HEM   O2A  O  N N 185 
HEM   C1B  C  N N 186 
HEM   C2B  C  N N 187 
HEM   C3B  C  N N 188 
HEM   C4B  C  N N 189 
HEM   CMB  C  N N 190 
HEM   CAB  C  N N 191 
HEM   CBB  C  N N 192 
HEM   C1C  C  Y N 193 
HEM   C2C  C  Y N 194 
HEM   C3C  C  Y N 195 
HEM   C4C  C  Y N 196 
HEM   CMC  C  N N 197 
HEM   CAC  C  N N 198 
HEM   CBC  C  N N 199 
HEM   C1D  C  N N 200 
HEM   C2D  C  N N 201 
HEM   C3D  C  N N 202 
HEM   C4D  C  N N 203 
HEM   CMD  C  N N 204 
HEM   CAD  C  N N 205 
HEM   CBD  C  N N 206 
HEM   CGD  C  N N 207 
HEM   O1D  O  N N 208 
HEM   O2D  O  N N 209 
HEM   NA   N  Y N 210 
HEM   NB   N  N N 211 
HEM   NC   N  Y N 212 
HEM   ND   N  N N 213 
HEM   FE   FE N N 214 
HEM   HHB  H  N N 215 
HEM   HHC  H  N N 216 
HEM   HHD  H  N N 217 
HEM   HMA  H  N N 218 
HEM   HMAA H  N N 219 
HEM   HMAB H  N N 220 
HEM   HAA  H  N N 221 
HEM   HAAA H  N N 222 
HEM   HBA  H  N N 223 
HEM   HBAA H  N N 224 
HEM   HMB  H  N N 225 
HEM   HMBA H  N N 226 
HEM   HMBB H  N N 227 
HEM   HAB  H  N N 228 
HEM   HBB  H  N N 229 
HEM   HBBA H  N N 230 
HEM   HMC  H  N N 231 
HEM   HMCA H  N N 232 
HEM   HMCB H  N N 233 
HEM   HAC  H  N N 234 
HEM   HBC  H  N N 235 
HEM   HBCA H  N N 236 
HEM   HMD  H  N N 237 
HEM   HMDA H  N N 238 
HEM   HMDB H  N N 239 
HEM   HAD  H  N N 240 
HEM   HADA H  N N 241 
HEM   HBD  H  N N 242 
HEM   HBDA H  N N 243 
HEM   H2A  H  N N 244 
HEM   H2D  H  N N 245 
HEM   HHA  H  N N 246 
HIS   N    N  N N 247 
HIS   CA   C  N S 248 
HIS   C    C  N N 249 
HIS   O    O  N N 250 
HIS   CB   C  N N 251 
HIS   CG   C  Y N 252 
HIS   ND1  N  Y N 253 
HIS   CD2  C  Y N 254 
HIS   CE1  C  Y N 255 
HIS   NE2  N  Y N 256 
HIS   OXT  O  N N 257 
HIS   H    H  N N 258 
HIS   H2   H  N N 259 
HIS   HA   H  N N 260 
HIS   HB2  H  N N 261 
HIS   HB3  H  N N 262 
HIS   HD1  H  N N 263 
HIS   HD2  H  N N 264 
HIS   HE1  H  N N 265 
HIS   HE2  H  N N 266 
HIS   HXT  H  N N 267 
HOH   O    O  N N 268 
HOH   H1   H  N N 269 
HOH   H2   H  N N 270 
ILE   N    N  N N 271 
ILE   CA   C  N S 272 
ILE   C    C  N N 273 
ILE   O    O  N N 274 
ILE   CB   C  N S 275 
ILE   CG1  C  N N 276 
ILE   CG2  C  N N 277 
ILE   CD1  C  N N 278 
ILE   OXT  O  N N 279 
ILE   H    H  N N 280 
ILE   H2   H  N N 281 
ILE   HA   H  N N 282 
ILE   HB   H  N N 283 
ILE   HG12 H  N N 284 
ILE   HG13 H  N N 285 
ILE   HG21 H  N N 286 
ILE   HG22 H  N N 287 
ILE   HG23 H  N N 288 
ILE   HD11 H  N N 289 
ILE   HD12 H  N N 290 
ILE   HD13 H  N N 291 
ILE   HXT  H  N N 292 
LEU   N    N  N N 293 
LEU   CA   C  N S 294 
LEU   C    C  N N 295 
LEU   O    O  N N 296 
LEU   CB   C  N N 297 
LEU   CG   C  N N 298 
LEU   CD1  C  N N 299 
LEU   CD2  C  N N 300 
LEU   OXT  O  N N 301 
LEU   H    H  N N 302 
LEU   H2   H  N N 303 
LEU   HA   H  N N 304 
LEU   HB2  H  N N 305 
LEU   HB3  H  N N 306 
LEU   HG   H  N N 307 
LEU   HD11 H  N N 308 
LEU   HD12 H  N N 309 
LEU   HD13 H  N N 310 
LEU   HD21 H  N N 311 
LEU   HD22 H  N N 312 
LEU   HD23 H  N N 313 
LEU   HXT  H  N N 314 
LYS   N    N  N N 315 
LYS   CA   C  N S 316 
LYS   C    C  N N 317 
LYS   O    O  N N 318 
LYS   CB   C  N N 319 
LYS   CG   C  N N 320 
LYS   CD   C  N N 321 
LYS   CE   C  N N 322 
LYS   NZ   N  N N 323 
LYS   OXT  O  N N 324 
LYS   H    H  N N 325 
LYS   H2   H  N N 326 
LYS   HA   H  N N 327 
LYS   HB2  H  N N 328 
LYS   HB3  H  N N 329 
LYS   HG2  H  N N 330 
LYS   HG3  H  N N 331 
LYS   HD2  H  N N 332 
LYS   HD3  H  N N 333 
LYS   HE2  H  N N 334 
LYS   HE3  H  N N 335 
LYS   HZ1  H  N N 336 
LYS   HZ2  H  N N 337 
LYS   HZ3  H  N N 338 
LYS   HXT  H  N N 339 
MET   N    N  N N 340 
MET   CA   C  N S 341 
MET   C    C  N N 342 
MET   O    O  N N 343 
MET   CB   C  N N 344 
MET   CG   C  N N 345 
MET   SD   S  N N 346 
MET   CE   C  N N 347 
MET   OXT  O  N N 348 
MET   H    H  N N 349 
MET   H2   H  N N 350 
MET   HA   H  N N 351 
MET   HB2  H  N N 352 
MET   HB3  H  N N 353 
MET   HG2  H  N N 354 
MET   HG3  H  N N 355 
MET   HE1  H  N N 356 
MET   HE2  H  N N 357 
MET   HE3  H  N N 358 
MET   HXT  H  N N 359 
PHE   N    N  N N 360 
PHE   CA   C  N S 361 
PHE   C    C  N N 362 
PHE   O    O  N N 363 
PHE   CB   C  N N 364 
PHE   CG   C  Y N 365 
PHE   CD1  C  Y N 366 
PHE   CD2  C  Y N 367 
PHE   CE1  C  Y N 368 
PHE   CE2  C  Y N 369 
PHE   CZ   C  Y N 370 
PHE   OXT  O  N N 371 
PHE   H    H  N N 372 
PHE   H2   H  N N 373 
PHE   HA   H  N N 374 
PHE   HB2  H  N N 375 
PHE   HB3  H  N N 376 
PHE   HD1  H  N N 377 
PHE   HD2  H  N N 378 
PHE   HE1  H  N N 379 
PHE   HE2  H  N N 380 
PHE   HZ   H  N N 381 
PHE   HXT  H  N N 382 
PRO   N    N  N N 383 
PRO   CA   C  N S 384 
PRO   C    C  N N 385 
PRO   O    O  N N 386 
PRO   CB   C  N N 387 
PRO   CG   C  N N 388 
PRO   CD   C  N N 389 
PRO   OXT  O  N N 390 
PRO   H    H  N N 391 
PRO   HA   H  N N 392 
PRO   HB2  H  N N 393 
PRO   HB3  H  N N 394 
PRO   HG2  H  N N 395 
PRO   HG3  H  N N 396 
PRO   HD2  H  N N 397 
PRO   HD3  H  N N 398 
PRO   HXT  H  N N 399 
SER   N    N  N N 400 
SER   CA   C  N S 401 
SER   C    C  N N 402 
SER   O    O  N N 403 
SER   CB   C  N N 404 
SER   OG   O  N N 405 
SER   OXT  O  N N 406 
SER   H    H  N N 407 
SER   H2   H  N N 408 
SER   HA   H  N N 409 
SER   HB2  H  N N 410 
SER   HB3  H  N N 411 
SER   HG   H  N N 412 
SER   HXT  H  N N 413 
THR   N    N  N N 414 
THR   CA   C  N S 415 
THR   C    C  N N 416 
THR   O    O  N N 417 
THR   CB   C  N R 418 
THR   OG1  O  N N 419 
THR   CG2  C  N N 420 
THR   OXT  O  N N 421 
THR   H    H  N N 422 
THR   H2   H  N N 423 
THR   HA   H  N N 424 
THR   HB   H  N N 425 
THR   HG1  H  N N 426 
THR   HG21 H  N N 427 
THR   HG22 H  N N 428 
THR   HG23 H  N N 429 
THR   HXT  H  N N 430 
TRP   N    N  N N 431 
TRP   CA   C  N S 432 
TRP   C    C  N N 433 
TRP   O    O  N N 434 
TRP   CB   C  N N 435 
TRP   CG   C  Y N 436 
TRP   CD1  C  Y N 437 
TRP   CD2  C  Y N 438 
TRP   NE1  N  Y N 439 
TRP   CE2  C  Y N 440 
TRP   CE3  C  Y N 441 
TRP   CZ2  C  Y N 442 
TRP   CZ3  C  Y N 443 
TRP   CH2  C  Y N 444 
TRP   OXT  O  N N 445 
TRP   H    H  N N 446 
TRP   H2   H  N N 447 
TRP   HA   H  N N 448 
TRP   HB2  H  N N 449 
TRP   HB3  H  N N 450 
TRP   HD1  H  N N 451 
TRP   HE1  H  N N 452 
TRP   HE3  H  N N 453 
TRP   HZ2  H  N N 454 
TRP   HZ3  H  N N 455 
TRP   HH2  H  N N 456 
TRP   HXT  H  N N 457 
TYR   N    N  N N 458 
TYR   CA   C  N S 459 
TYR   C    C  N N 460 
TYR   O    O  N N 461 
TYR   CB   C  N N 462 
TYR   CG   C  Y N 463 
TYR   CD1  C  Y N 464 
TYR   CD2  C  Y N 465 
TYR   CE1  C  Y N 466 
TYR   CE2  C  Y N 467 
TYR   CZ   C  Y N 468 
TYR   OH   O  N N 469 
TYR   OXT  O  N N 470 
TYR   H    H  N N 471 
TYR   H2   H  N N 472 
TYR   HA   H  N N 473 
TYR   HB2  H  N N 474 
TYR   HB3  H  N N 475 
TYR   HD1  H  N N 476 
TYR   HD2  H  N N 477 
TYR   HE1  H  N N 478 
TYR   HE2  H  N N 479 
TYR   HH   H  N N 480 
TYR   HXT  H  N N 481 
VAL   N    N  N N 482 
VAL   CA   C  N S 483 
VAL   C    C  N N 484 
VAL   O    O  N N 485 
VAL   CB   C  N N 486 
VAL   CG1  C  N N 487 
VAL   CG2  C  N N 488 
VAL   OXT  O  N N 489 
VAL   H    H  N N 490 
VAL   H2   H  N N 491 
VAL   HA   H  N N 492 
VAL   HB   H  N N 493 
VAL   HG11 H  N N 494 
VAL   HG12 H  N N 495 
VAL   HG13 H  N N 496 
VAL   HG21 H  N N 497 
VAL   HG22 H  N N 498 
VAL   HG23 H  N N 499 
VAL   HXT  H  N N 500 
# 
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 
A1IER O1  C2   sing N N 1   
A1IER C2  C3   sing N N 2   
A1IER C3  C4   doub Y N 3   
A1IER C4  N5   sing Y N 4   
A1IER N5  C6   sing N N 5   
A1IER C6  C7   doub Y N 6   
A1IER C7  C8   sing Y N 7   
A1IER C8  C9   doub Y N 8   
A1IER C9  C10  sing Y N 9   
A1IER C10 C11  doub Y N 10  
A1IER N5  N12  sing Y N 11  
A1IER N12 N13  doub Y N 12  
A1IER C2  C14  sing N N 13  
A1IER C14 C15  doub Y N 14  
A1IER C15 C16  sing Y N 15  
A1IER C16 CL17 sing N N 16  
A1IER C16 C18  doub Y N 17  
A1IER C18 C19  sing Y N 18  
A1IER C19 C20  doub Y N 19  
A1IER C20 N21  sing Y N 20  
A1IER N21 C22  doub Y N 21  
A1IER C22 N23  sing Y N 22  
A1IER N13 C3   sing Y N 23  
A1IER N23 C14  sing Y N 24  
A1IER C11 C6   sing Y N 25  
A1IER N23 C19  sing Y N 26  
A1IER C4  H4   sing N N 27  
A1IER C7  H7   sing N N 28  
A1IER C8  H8   sing N N 29  
A1IER C10 H10  sing N N 30  
A1IER C15 H15  sing N N 31  
A1IER C20 H20  sing N N 32  
A1IER C22 H22  sing N N 33  
A1IER O1  H1   sing N N 34  
A1IER C2  H2   sing N N 35  
A1IER C9  H9   sing N N 36  
A1IER C11 H11  sing N N 37  
A1IER C18 H18  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HEM   CHA C1A  sing N N 167 
HEM   CHA C4D  doub N N 168 
HEM   CHA HHA  sing N N 169 
HEM   CHB C4A  sing N N 170 
HEM   CHB C1B  doub N N 171 
HEM   CHB HHB  sing N N 172 
HEM   CHC C4B  sing N N 173 
HEM   CHC C1C  doub N N 174 
HEM   CHC HHC  sing N N 175 
HEM   CHD C4C  doub N N 176 
HEM   CHD C1D  sing N N 177 
HEM   CHD HHD  sing N N 178 
HEM   C1A C2A  doub Y N 179 
HEM   C1A NA   sing Y N 180 
HEM   C2A C3A  sing Y N 181 
HEM   C2A CAA  sing N N 182 
HEM   C3A C4A  doub Y N 183 
HEM   C3A CMA  sing N N 184 
HEM   C4A NA   sing Y N 185 
HEM   CMA HMA  sing N N 186 
HEM   CMA HMAA sing N N 187 
HEM   CMA HMAB sing N N 188 
HEM   CAA CBA  sing N N 189 
HEM   CAA HAA  sing N N 190 
HEM   CAA HAAA sing N N 191 
HEM   CBA CGA  sing N N 192 
HEM   CBA HBA  sing N N 193 
HEM   CBA HBAA sing N N 194 
HEM   CGA O1A  doub N N 195 
HEM   CGA O2A  sing N N 196 
HEM   C1B C2B  sing N N 197 
HEM   C1B NB   sing N N 198 
HEM   C2B C3B  doub N N 199 
HEM   C2B CMB  sing N N 200 
HEM   C3B C4B  sing N N 201 
HEM   C3B CAB  sing N N 202 
HEM   C4B NB   doub N N 203 
HEM   CMB HMB  sing N N 204 
HEM   CMB HMBA sing N N 205 
HEM   CMB HMBB sing N N 206 
HEM   CAB CBB  doub N N 207 
HEM   CAB HAB  sing N N 208 
HEM   CBB HBB  sing N N 209 
HEM   CBB HBBA sing N N 210 
HEM   C1C C2C  sing Y N 211 
HEM   C1C NC   sing Y N 212 
HEM   C2C C3C  doub Y N 213 
HEM   C2C CMC  sing N N 214 
HEM   C3C C4C  sing Y N 215 
HEM   C3C CAC  sing N N 216 
HEM   C4C NC   sing Y N 217 
HEM   CMC HMC  sing N N 218 
HEM   CMC HMCA sing N N 219 
HEM   CMC HMCB sing N N 220 
HEM   CAC CBC  doub N N 221 
HEM   CAC HAC  sing N N 222 
HEM   CBC HBC  sing N N 223 
HEM   CBC HBCA sing N N 224 
HEM   C1D C2D  sing N N 225 
HEM   C1D ND   doub N N 226 
HEM   C2D C3D  doub N N 227 
HEM   C2D CMD  sing N N 228 
HEM   C3D C4D  sing N N 229 
HEM   C3D CAD  sing N N 230 
HEM   C4D ND   sing N N 231 
HEM   CMD HMD  sing N N 232 
HEM   CMD HMDA sing N N 233 
HEM   CMD HMDB sing N N 234 
HEM   CAD CBD  sing N N 235 
HEM   CAD HAD  sing N N 236 
HEM   CAD HADA sing N N 237 
HEM   CBD CGD  sing N N 238 
HEM   CBD HBD  sing N N 239 
HEM   CBD HBDA sing N N 240 
HEM   CGD O1D  doub N N 241 
HEM   CGD O2D  sing N N 242 
HEM   O2A H2A  sing N N 243 
HEM   O2D H2D  sing N N 244 
HEM   FE  NA   sing N N 245 
HEM   FE  NB   sing N N 246 
HEM   FE  NC   sing N N 247 
HEM   FE  ND   sing N N 248 
HIS   N   CA   sing N N 249 
HIS   N   H    sing N N 250 
HIS   N   H2   sing N N 251 
HIS   CA  C    sing N N 252 
HIS   CA  CB   sing N N 253 
HIS   CA  HA   sing N N 254 
HIS   C   O    doub N N 255 
HIS   C   OXT  sing N N 256 
HIS   CB  CG   sing N N 257 
HIS   CB  HB2  sing N N 258 
HIS   CB  HB3  sing N N 259 
HIS   CG  ND1  sing Y N 260 
HIS   CG  CD2  doub Y N 261 
HIS   ND1 CE1  doub Y N 262 
HIS   ND1 HD1  sing N N 263 
HIS   CD2 NE2  sing Y N 264 
HIS   CD2 HD2  sing N N 265 
HIS   CE1 NE2  sing Y N 266 
HIS   CE1 HE1  sing N N 267 
HIS   NE2 HE2  sing N N 268 
HIS   OXT HXT  sing N N 269 
HOH   O   H1   sing N N 270 
HOH   O   H2   sing N N 271 
ILE   N   CA   sing N N 272 
ILE   N   H    sing N N 273 
ILE   N   H2   sing N N 274 
ILE   CA  C    sing N N 275 
ILE   CA  CB   sing N N 276 
ILE   CA  HA   sing N N 277 
ILE   C   O    doub N N 278 
ILE   C   OXT  sing N N 279 
ILE   CB  CG1  sing N N 280 
ILE   CB  CG2  sing N N 281 
ILE   CB  HB   sing N N 282 
ILE   CG1 CD1  sing N N 283 
ILE   CG1 HG12 sing N N 284 
ILE   CG1 HG13 sing N N 285 
ILE   CG2 HG21 sing N N 286 
ILE   CG2 HG22 sing N N 287 
ILE   CG2 HG23 sing N N 288 
ILE   CD1 HD11 sing N N 289 
ILE   CD1 HD12 sing N N 290 
ILE   CD1 HD13 sing N N 291 
ILE   OXT HXT  sing N N 292 
LEU   N   CA   sing N N 293 
LEU   N   H    sing N N 294 
LEU   N   H2   sing N N 295 
LEU   CA  C    sing N N 296 
LEU   CA  CB   sing N N 297 
LEU   CA  HA   sing N N 298 
LEU   C   O    doub N N 299 
LEU   C   OXT  sing N N 300 
LEU   CB  CG   sing N N 301 
LEU   CB  HB2  sing N N 302 
LEU   CB  HB3  sing N N 303 
LEU   CG  CD1  sing N N 304 
LEU   CG  CD2  sing N N 305 
LEU   CG  HG   sing N N 306 
LEU   CD1 HD11 sing N N 307 
LEU   CD1 HD12 sing N N 308 
LEU   CD1 HD13 sing N N 309 
LEU   CD2 HD21 sing N N 310 
LEU   CD2 HD22 sing N N 311 
LEU   CD2 HD23 sing N N 312 
LEU   OXT HXT  sing N N 313 
LYS   N   CA   sing N N 314 
LYS   N   H    sing N N 315 
LYS   N   H2   sing N N 316 
LYS   CA  C    sing N N 317 
LYS   CA  CB   sing N N 318 
LYS   CA  HA   sing N N 319 
LYS   C   O    doub N N 320 
LYS   C   OXT  sing N N 321 
LYS   CB  CG   sing N N 322 
LYS   CB  HB2  sing N N 323 
LYS   CB  HB3  sing N N 324 
LYS   CG  CD   sing N N 325 
LYS   CG  HG2  sing N N 326 
LYS   CG  HG3  sing N N 327 
LYS   CD  CE   sing N N 328 
LYS   CD  HD2  sing N N 329 
LYS   CD  HD3  sing N N 330 
LYS   CE  NZ   sing N N 331 
LYS   CE  HE2  sing N N 332 
LYS   CE  HE3  sing N N 333 
LYS   NZ  HZ1  sing N N 334 
LYS   NZ  HZ2  sing N N 335 
LYS   NZ  HZ3  sing N N 336 
LYS   OXT HXT  sing N N 337 
MET   N   CA   sing N N 338 
MET   N   H    sing N N 339 
MET   N   H2   sing N N 340 
MET   CA  C    sing N N 341 
MET   CA  CB   sing N N 342 
MET   CA  HA   sing N N 343 
MET   C   O    doub N N 344 
MET   C   OXT  sing N N 345 
MET   CB  CG   sing N N 346 
MET   CB  HB2  sing N N 347 
MET   CB  HB3  sing N N 348 
MET   CG  SD   sing N N 349 
MET   CG  HG2  sing N N 350 
MET   CG  HG3  sing N N 351 
MET   SD  CE   sing N N 352 
MET   CE  HE1  sing N N 353 
MET   CE  HE2  sing N N 354 
MET   CE  HE3  sing N N 355 
MET   OXT HXT  sing N N 356 
PHE   N   CA   sing N N 357 
PHE   N   H    sing N N 358 
PHE   N   H2   sing N N 359 
PHE   CA  C    sing N N 360 
PHE   CA  CB   sing N N 361 
PHE   CA  HA   sing N N 362 
PHE   C   O    doub N N 363 
PHE   C   OXT  sing N N 364 
PHE   CB  CG   sing N N 365 
PHE   CB  HB2  sing N N 366 
PHE   CB  HB3  sing N N 367 
PHE   CG  CD1  doub Y N 368 
PHE   CG  CD2  sing Y N 369 
PHE   CD1 CE1  sing Y N 370 
PHE   CD1 HD1  sing N N 371 
PHE   CD2 CE2  doub Y N 372 
PHE   CD2 HD2  sing N N 373 
PHE   CE1 CZ   doub Y N 374 
PHE   CE1 HE1  sing N N 375 
PHE   CE2 CZ   sing Y N 376 
PHE   CE2 HE2  sing N N 377 
PHE   CZ  HZ   sing N N 378 
PHE   OXT HXT  sing N N 379 
PRO   N   CA   sing N N 380 
PRO   N   CD   sing N N 381 
PRO   N   H    sing N N 382 
PRO   CA  C    sing N N 383 
PRO   CA  CB   sing N N 384 
PRO   CA  HA   sing N N 385 
PRO   C   O    doub N N 386 
PRO   C   OXT  sing N N 387 
PRO   CB  CG   sing N N 388 
PRO   CB  HB2  sing N N 389 
PRO   CB  HB3  sing N N 390 
PRO   CG  CD   sing N N 391 
PRO   CG  HG2  sing N N 392 
PRO   CG  HG3  sing N N 393 
PRO   CD  HD2  sing N N 394 
PRO   CD  HD3  sing N N 395 
PRO   OXT HXT  sing N N 396 
SER   N   CA   sing N N 397 
SER   N   H    sing N N 398 
SER   N   H2   sing N N 399 
SER   CA  C    sing N N 400 
SER   CA  CB   sing N N 401 
SER   CA  HA   sing N N 402 
SER   C   O    doub N N 403 
SER   C   OXT  sing N N 404 
SER   CB  OG   sing N N 405 
SER   CB  HB2  sing N N 406 
SER   CB  HB3  sing N N 407 
SER   OG  HG   sing N N 408 
SER   OXT HXT  sing N N 409 
THR   N   CA   sing N N 410 
THR   N   H    sing N N 411 
THR   N   H2   sing N N 412 
THR   CA  C    sing N N 413 
THR   CA  CB   sing N N 414 
THR   CA  HA   sing N N 415 
THR   C   O    doub N N 416 
THR   C   OXT  sing N N 417 
THR   CB  OG1  sing N N 418 
THR   CB  CG2  sing N N 419 
THR   CB  HB   sing N N 420 
THR   OG1 HG1  sing N N 421 
THR   CG2 HG21 sing N N 422 
THR   CG2 HG22 sing N N 423 
THR   CG2 HG23 sing N N 424 
THR   OXT HXT  sing N N 425 
TRP   N   CA   sing N N 426 
TRP   N   H    sing N N 427 
TRP   N   H2   sing N N 428 
TRP   CA  C    sing N N 429 
TRP   CA  CB   sing N N 430 
TRP   CA  HA   sing N N 431 
TRP   C   O    doub N N 432 
TRP   C   OXT  sing N N 433 
TRP   CB  CG   sing N N 434 
TRP   CB  HB2  sing N N 435 
TRP   CB  HB3  sing N N 436 
TRP   CG  CD1  doub Y N 437 
TRP   CG  CD2  sing Y N 438 
TRP   CD1 NE1  sing Y N 439 
TRP   CD1 HD1  sing N N 440 
TRP   CD2 CE2  doub Y N 441 
TRP   CD2 CE3  sing Y N 442 
TRP   NE1 CE2  sing Y N 443 
TRP   NE1 HE1  sing N N 444 
TRP   CE2 CZ2  sing Y N 445 
TRP   CE3 CZ3  doub Y N 446 
TRP   CE3 HE3  sing N N 447 
TRP   CZ2 CH2  doub Y N 448 
TRP   CZ2 HZ2  sing N N 449 
TRP   CZ3 CH2  sing Y N 450 
TRP   CZ3 HZ3  sing N N 451 
TRP   CH2 HH2  sing N N 452 
TRP   OXT HXT  sing N N 453 
TYR   N   CA   sing N N 454 
TYR   N   H    sing N N 455 
TYR   N   H2   sing N N 456 
TYR   CA  C    sing N N 457 
TYR   CA  CB   sing N N 458 
TYR   CA  HA   sing N N 459 
TYR   C   O    doub N N 460 
TYR   C   OXT  sing N N 461 
TYR   CB  CG   sing N N 462 
TYR   CB  HB2  sing N N 463 
TYR   CB  HB3  sing N N 464 
TYR   CG  CD1  doub Y N 465 
TYR   CG  CD2  sing Y N 466 
TYR   CD1 CE1  sing Y N 467 
TYR   CD1 HD1  sing N N 468 
TYR   CD2 CE2  doub Y N 469 
TYR   CD2 HD2  sing N N 470 
TYR   CE1 CZ   doub Y N 471 
TYR   CE1 HE1  sing N N 472 
TYR   CE2 CZ   sing Y N 473 
TYR   CE2 HE2  sing N N 474 
TYR   CZ  OH   sing N N 475 
TYR   OH  HH   sing N N 476 
TYR   OXT HXT  sing N N 477 
VAL   N   CA   sing N N 478 
VAL   N   H    sing N N 479 
VAL   N   H2   sing N N 480 
VAL   CA  C    sing N N 481 
VAL   CA  CB   sing N N 482 
VAL   CA  HA   sing N N 483 
VAL   C   O    doub N N 484 
VAL   C   OXT  sing N N 485 
VAL   CB  CG1  sing N N 486 
VAL   CB  CG2  sing N N 487 
VAL   CB  HB   sing N N 488 
VAL   CG1 HG11 sing N N 489 
VAL   CG1 HG12 sing N N 490 
VAL   CG1 HG13 sing N N 491 
VAL   CG2 HG21 sing N N 492 
VAL   CG2 HG22 sing N N 493 
VAL   CG2 HG23 sing N N 494 
VAL   OXT HXT  sing N N 495 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Internal structure' 
# 
_atom_sites.entry_id                    9FON 
_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]   0.008365 
_atom_sites.fract_transf_matrix[1][2]   0.004830 
_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]   0.009659 
_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]   0.009823 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
FE 
N  
O  
S  
# 
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    . LYS   A 1 3   ? 115.986 73.59   27.835  1   42.01 ? 25  LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 3   ? 116.55  73.429  29.171  1   41.95 ? 25  LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 3   ? 115.568 73.92   30.236  1   41.54 ? 25  LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 3   ? 115.164 73.119  31.077  1   42.65 ? 25  LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 3   ? 117.958 74.05   29.288  1   44.13 ? 25  LYS   A CB   1 
ATOM   6    N  N    . ILE   A 1 4   ? 115.147 75.187  30.194  1   39.91 ? 26  ILE   A N    1 
ATOM   7    C  CA   . ILE   A 1 4   ? 114.136 75.677  31.131  1   39.31 ? 26  ILE   A CA   1 
ATOM   8    C  C    . ILE   A 1 4   ? 112.71  75.331  30.619  1   38.9  ? 26  ILE   A C    1 
ATOM   9    O  O    . ILE   A 1 4   ? 112.574 74.898  29.486  1   39.69 ? 26  ILE   A O    1 
ATOM   10   C  CB   . ILE   A 1 4   ? 114.325 77.168  31.509  1   39.8  ? 26  ILE   A CB   1 
ATOM   11   C  CG1  . ILE   A 1 4   ? 114.007 78.106  30.339  1   40.78 ? 26  ILE   A CG1  1 
ATOM   12   C  CG2  . ILE   A 1 4   ? 115.734 77.407  32.042  1   40.06 ? 26  ILE   A CG2  1 
ATOM   13   C  CD1  . ILE   A 1 4   ? 113.916 79.568  30.764  1   41.66 ? 26  ILE   A CD1  1 
ATOM   14   N  N    . TYR   A 1 5   ? 111.666 75.487  31.455  1   37.45 ? 27  TYR   A N    1 
ATOM   15   C  CA   . TYR   A 1 5   ? 110.282 75.11   31.148  1   36.58 ? 27  TYR   A CA   1 
ATOM   16   C  C    . TYR   A 1 5   ? 109.792 75.557  29.754  1   37.59 ? 27  TYR   A C    1 
ATOM   17   O  O    . TYR   A 1 5   ? 109.432 74.703  28.925  1   38.11 ? 27  TYR   A O    1 
ATOM   18   C  CB   . TYR   A 1 5   ? 109.357 75.594  32.267  1   35.2  ? 27  TYR   A CB   1 
ATOM   19   C  CG   . TYR   A 1 5   ? 107.897 75.214  32.138  1   34.77 ? 27  TYR   A CG   1 
ATOM   20   C  CD1  . TYR   A 1 5   ? 107.4   74.072  32.752  1   34.39 ? 27  TYR   A CD1  1 
ATOM   21   C  CD2  . TYR   A 1 5   ? 106.984 76.076  31.54   1   34.93 ? 27  TYR   A CD2  1 
ATOM   22   C  CE1  . TYR   A 1 5   ? 106.046 73.748  32.694  1   34.47 ? 27  TYR   A CE1  1 
ATOM   23   C  CE2  . TYR   A 1 5   ? 105.635 75.755  31.458  1   35.28 ? 27  TYR   A CE2  1 
ATOM   24   C  CZ   . TYR   A 1 5   ? 105.161 74.597  32.058  1   34.92 ? 27  TYR   A CZ   1 
ATOM   25   O  OH   . TYR   A 1 5   ? 103.823 74.275  31.989  1   34.05 ? 27  TYR   A OH   1 
ATOM   26   N  N    . GLY   A 1 6   ? 109.823 76.867  29.495  1   37.24 ? 28  GLY   A N    1 
ATOM   27   C  CA   . GLY   A 1 6   ? 109.402 77.435  28.227  1   36.78 ? 28  GLY   A CA   1 
ATOM   28   C  C    . GLY   A 1 6   ? 110.193 76.943  27.034  1   37.07 ? 28  GLY   A C    1 
ATOM   29   O  O    . GLY   A 1 6   ? 109.63  76.751  25.959  1   37.84 ? 28  GLY   A O    1 
ATOM   30   N  N    . GLU   A 1 7   ? 111.486 76.707  27.203  1   36.86 ? 29  GLU   A N    1 
ATOM   31   C  CA   . GLU   A 1 7   ? 112.344 76.227  26.116  1   37.14 ? 29  GLU   A CA   1 
ATOM   32   C  C    . GLU   A 1 7   ? 112.107 74.738  25.828  1   36.61 ? 29  GLU   A C    1 
ATOM   33   O  O    . GLU   A 1 7   ? 112.044 74.336  24.663  1   37.1  ? 29  GLU   A O    1 
ATOM   34   C  CB   . GLU   A 1 7   ? 113.836 76.463  26.458  1   40.18 ? 29  GLU   A CB   1 
ATOM   35   C  CG   . GLU   A 1 7   ? 114.22  77.925  26.595  1   46.59 ? 29  GLU   A CG   1 
ATOM   36   C  CD   . GLU   A 1 7   ? 115.661 78.174  27.014  1   57.41 ? 29  GLU   A CD   1 
ATOM   37   O  OE1  . GLU   A 1 7   ? 116.053 79.364  27.084  1   59.7  ? 29  GLU   A OE1  1 
ATOM   38   O  OE2  . GLU   A 1 7   ? 116.401 77.191  27.266  1   60.22 ? 29  GLU   A OE2  1 
ATOM   39   N  N    . TYR   A 1 8   ? 111.956 73.929  26.884  1   35    ? 30  TYR   A N    1 
ATOM   40   C  CA   . TYR   A 1 8   ? 111.691 72.504  26.775  1   34.37 ? 30  TYR   A CA   1 
ATOM   41   C  C    . TYR   A 1 8   ? 110.354 72.272  26.047  1   34.24 ? 30  TYR   A C    1 
ATOM   42   O  O    . TYR   A 1 8   ? 110.252 71.36   25.222  1   34.77 ? 30  TYR   A O    1 
ATOM   43   C  CB   . TYR   A 1 8   ? 111.653 71.868  28.186  1   33.97 ? 30  TYR   A CB   1 
ATOM   44   C  CG   . TYR   A 1 8   ? 111.217 70.421  28.178  1   33.95 ? 30  TYR   A CG   1 
ATOM   45   C  CD1  . TYR   A 1 8   ? 112.061 69.428  27.721  1   34.59 ? 30  TYR   A CD1  1 
ATOM   46   C  CD2  . TYR   A 1 8   ? 109.95  70.051  28.612  1   34.44 ? 30  TYR   A CD2  1 
ATOM   47   C  CE1  . TYR   A 1 8   ? 111.652 68.105  27.666  1   35.4  ? 30  TYR   A CE1  1 
ATOM   48   C  CE2  . TYR   A 1 8   ? 109.535 68.728  28.583  1   34.71 ? 30  TYR   A CE2  1 
ATOM   49   C  CZ   . TYR   A 1 8   ? 110.394 67.757  28.119  1   35.55 ? 30  TYR   A CZ   1 
ATOM   50   O  OH   . TYR   A 1 8   ? 110     66.453  28.07   1   36.36 ? 30  TYR   A OH   1 
ATOM   51   N  N    . LEU   A 1 9   ? 109.336 73.085  26.364  1   33.44 ? 31  LEU   A N    1 
ATOM   52   C  CA   . LEU   A 1 9   ? 108.014 72.972  25.732  1   32.58 ? 31  LEU   A CA   1 
ATOM   53   C  C    . LEU   A 1 9   ? 107.856 73.811  24.459  1   33.11 ? 31  LEU   A C    1 
ATOM   54   O  O    . LEU   A 1 9   ? 106.774 73.822  23.873  1   32.55 ? 31  LEU   A O    1 
ATOM   55   C  CB   . LEU   A 1 9   ? 106.927 73.345  26.73   1   31.8  ? 31  LEU   A CB   1 
ATOM   56   C  CG   . LEU   A 1 9   ? 106.82  72.41   27.941  1   33.03 ? 31  LEU   A CG   1 
ATOM   57   C  CD1  . LEU   A 1 9   ? 105.865 72.968  28.963  1   32.82 ? 31  LEU   A CD1  1 
ATOM   58   C  CD2  . LEU   A 1 9   ? 106.428 70.986  27.504  1   33.44 ? 31  LEU   A CD2  1 
ATOM   59   N  N    . MET   A 1 10  ? 108.914 74.557  24.065  1   33.64 ? 32  MET   A N    1 
ATOM   60   C  CA   . MET   A 1 10  ? 108.958 75.419  22.892  1   34.84 ? 32  MET   A CA   1 
ATOM   61   C  C    . MET   A 1 10  ? 107.777 76.353  22.827  1   36.09 ? 32  MET   A C    1 
ATOM   62   O  O    . MET   A 1 10  ? 107.121 76.455  21.784  1   36.58 ? 32  MET   A O    1 
ATOM   63   C  CB   . MET   A 1 10  ? 109.128 74.593  21.603  1   35.91 ? 32  MET   A CB   1 
ATOM   64   C  CG   . MET   A 1 10  ? 110.318 73.679  21.675  1   39.24 ? 32  MET   A CG   1 
ATOM   65   S  SD   . MET   A 1 10  ? 110.606 72.777  20.157  1   47.01 ? 32  MET   A SD   1 
ATOM   66   C  CE   . MET   A 1 10  ? 111.15  74.086  19.141  1   48.45 ? 32  MET   A CE   1 
ATOM   67   N  N    . LEU   A 1 11  ? 107.473 77.002  23.961  1   36.5  ? 33  LEU   A N    1 
ATOM   68   C  CA   . LEU   A 1 11  ? 106.369 77.946  24.053  1   37.5  ? 33  LEU   A CA   1 
ATOM   69   C  C    . LEU   A 1 11  ? 106.575 79.178  23.177  1   39.94 ? 33  LEU   A C    1 
ATOM   70   O  O    . LEU   A 1 11  ? 105.61  79.873  22.886  1   39.87 ? 33  LEU   A O    1 
ATOM   71   C  CB   . LEU   A 1 11  ? 106.097 78.334  25.51   1   37.34 ? 33  LEU   A CB   1 
ATOM   72   C  CG   . LEU   A 1 11  ? 105.87  77.157  26.48   1   38.29 ? 33  LEU   A CG   1 
ATOM   73   C  CD1  . LEU   A 1 11  ? 105.606 77.657  27.871  1   38.58 ? 33  LEU   A CD1  1 
ATOM   74   C  CD2  . LEU   A 1 11  ? 104.7   76.28   26.033  1   38.57 ? 33  LEU   A CD2  1 
ATOM   75   N  N    . ASP   A 1 12  ? 107.824 79.446  22.738  1   42.18 ? 34  ASP   A N    1 
ATOM   76   C  CA   . ASP   A 1 12  ? 108.172 80.528  21.816  1   44.48 ? 34  ASP   A CA   1 
ATOM   77   C  C    . ASP   A 1 12  ? 107.409 80.282  20.506  1   44.5  ? 34  ASP   A C    1 
ATOM   78   O  O    . ASP   A 1 12  ? 106.742 81.172  20.009  1   44.77 ? 34  ASP   A O    1 
ATOM   79   C  CB   . ASP   A 1 12  ? 109.719 80.568  21.565  1   48.7  ? 34  ASP   A CB   1 
ATOM   80   C  CG   . ASP   A 1 12  ? 110.328 79.376  20.802  1   58.23 ? 34  ASP   A CG   1 
ATOM   81   O  OD1  . ASP   A 1 12  ? 110.334 78.247  21.356  1   58.94 ? 34  ASP   A OD1  1 
ATOM   82   O  OD2  . ASP   A 1 12  ? 110.826 79.583  19.654  1   62.71 ? 34  ASP   A OD2  1 
ATOM   83   N  N    . LYS   A 1 13  ? 107.442 79.03   20.027  1   44.06 ? 35  LYS   A N    1 
ATOM   84   C  CA   . LYS   A 1 13  ? 106.806 78.509  18.833  1   43.67 ? 35  LYS   A CA   1 
ATOM   85   C  C    . LYS   A 1 13  ? 105.3   78.244  19.117  1   42.98 ? 35  LYS   A C    1 
ATOM   86   O  O    . LYS   A 1 13  ? 104.448 78.803  18.425  1   43.2  ? 35  LYS   A O    1 
ATOM   87   C  CB   . LYS   A 1 13  ? 107.548 77.214  18.456  1   45.66 ? 35  LYS   A CB   1 
ATOM   88   C  CG   . LYS   A 1 13  ? 107.603 76.89   16.996  1   51.7  ? 35  LYS   A CG   1 
ATOM   89   C  CD   . LYS   A 1 13  ? 108.313 75.563  16.773  1   58.01 ? 35  LYS   A CD   1 
ATOM   90   C  CE   . LYS   A 1 13  ? 109.727 75.717  16.282  1   63.56 ? 35  LYS   A CE   1 
ATOM   91   N  NZ   . LYS   A 1 13  ? 110.308 74.4    15.89   1   67.49 ? 35  LYS   A NZ   1 
ATOM   92   N  N    . LEU   A 1 14  ? 104.974 77.443  20.164  1   41.88 ? 36  LEU   A N    1 
ATOM   93   C  CA   . LEU   A 1 14  ? 103.6   77.075  20.516  1   41.69 ? 36  LEU   A CA   1 
ATOM   94   C  C    . LEU   A 1 14  ? 102.674 78.247  20.777  1   41.46 ? 36  LEU   A C    1 
ATOM   95   O  O    . LEU   A 1 14  ? 101.522 78.235  20.337  1   41.14 ? 36  LEU   A O    1 
ATOM   96   C  CB   . LEU   A 1 14  ? 103.567 76.123  21.731  1   41.55 ? 36  LEU   A CB   1 
ATOM   97   C  CG   . LEU   A 1 14  ? 102.205 75.463  22.002  1   41.55 ? 36  LEU   A CG   1 
ATOM   98   C  CD1  . LEU   A 1 14  ? 102.1   74.126  21.266  1   41.65 ? 36  LEU   A CD1  1 
ATOM   99   C  CD2  . LEU   A 1 14  ? 101.965 75.289  23.501  1   41.61 ? 36  LEU   A CD2  1 
ATOM   100  N  N    . LEU   A 1 15  ? 103.16  79.241  21.523  1   41.5  ? 37  LEU   A N    1 
ATOM   101  C  CA   . LEU   A 1 15  ? 102.354 80.397  21.895  1   41.95 ? 37  LEU   A CA   1 
ATOM   102  C  C    . LEU   A 1 15  ? 102.481 81.597  20.964  1   42.72 ? 37  LEU   A C    1 
ATOM   103  O  O    . LEU   A 1 15  ? 101.999 82.679  21.294  1   42.07 ? 37  LEU   A O    1 
ATOM   104  C  CB   . LEU   A 1 15  ? 102.605 80.805  23.339  1   42.14 ? 37  LEU   A CB   1 
ATOM   105  C  CG   . LEU   A 1 15  ? 102.345 79.694  24.373  1   43.23 ? 37  LEU   A CG   1 
ATOM   106  C  CD1  . LEU   A 1 15  ? 102.651 80.187  25.758  1   43.35 ? 37  LEU   A CD1  1 
ATOM   107  C  CD2  . LEU   A 1 15  ? 100.903 79.182  24.308  1   43.55 ? 37  LEU   A CD2  1 
ATOM   108  N  N    . ASP   A 1 16  ? 103.064 81.394  19.781  1   43.97 ? 38  ASP   A N    1 
ATOM   109  C  CA   . ASP   A 1 16  ? 103.093 82.396  18.716  1   45.35 ? 38  ASP   A CA   1 
ATOM   110  C  C    . ASP   A 1 16  ? 102.369 81.826  17.454  1   45.98 ? 38  ASP   A C    1 
ATOM   111  O  O    . ASP   A 1 16  ? 102.651 82.237  16.33   1   46.97 ? 38  ASP   A O    1 
ATOM   112  C  CB   . ASP   A 1 16  ? 104.535 82.824  18.389  1   47.69 ? 38  ASP   A CB   1 
ATOM   113  C  CG   . ASP   A 1 16  ? 104.618 84.073  17.522  1   53.61 ? 38  ASP   A CG   1 
ATOM   114  O  OD1  . ASP   A 1 16  ? 103.861 85.046  17.801  1   53.73 ? 38  ASP   A OD1  1 
ATOM   115  O  OD2  . ASP   A 1 16  ? 105.418 84.07   16.55   1   56.25 ? 38  ASP   A OD2  1 
ATOM   116  N  N    . ALA   A 1 17  ? 101.452 80.864  17.643  1   45.06 ? 39  ALA   A N    1 
ATOM   117  C  CA   . ALA   A 1 17  ? 100.699 80.261  16.557  1   44.18 ? 39  ALA   A CA   1 
ATOM   118  C  C    . ALA   A 1 17  ? 99.229  80.68   16.591  1   44.28 ? 39  ALA   A C    1 
ATOM   119  O  O    . ALA   A 1 17  ? 98.422  80.058  15.917  1   44.73 ? 39  ALA   A O    1 
ATOM   120  C  CB   . ALA   A 1 17  ? 100.818 78.746  16.624  1   43.82 ? 39  ALA   A CB   1 
ATOM   121  N  N    . GLN   A 1 18  ? 98.871  81.74   17.332  1   44.03 ? 40  GLN   A N    1 
ATOM   122  C  CA   . GLN   A 1 18  ? 97.496  82.19   17.425  1   44.91 ? 40  GLN   A CA   1 
ATOM   123  C  C    . GLN   A 1 18  ? 97.325  83.504  16.67   1   47.39 ? 40  GLN   A C    1 
ATOM   124  O  O    . GLN   A 1 18  ? 97.832  84.545  17.09   1   48.37 ? 40  GLN   A O    1 
ATOM   125  C  CB   . GLN   A 1 18  ? 97.052  82.293  18.89   1   44.88 ? 40  GLN   A CB   1 
ATOM   126  C  CG   . GLN   A 1 18  ? 97.043  80.937  19.635  1   44.76 ? 40  GLN   A CG   1 
ATOM   127  C  CD   . GLN   A 1 18  ? 98.436  80.464  19.956  1   45.47 ? 40  GLN   A CD   1 
ATOM   128  O  OE1  . GLN   A 1 18  ? 99.3    81.251  20.335  1   45.37 ? 40  GLN   A OE1  1 
ATOM   129  N  NE2  . GLN   A 1 18  ? 98.706  79.179  19.777  1   45.62 ? 40  GLN   A NE2  1 
ATOM   130  N  N    . CYS   A 1 19  ? 96.654  83.446  15.523  1   48.23 ? 41  CYS   A N    1 
ATOM   131  C  CA   . CYS   A 1 19  ? 96.478  84.617  14.667  1   49.27 ? 41  CYS   A CA   1 
ATOM   132  C  C    . CYS   A 1 19  ? 95.003  84.825  14.314  1   48.88 ? 41  CYS   A C    1 
ATOM   133  O  O    . CYS   A 1 19  ? 94.486  84.154  13.425  1   48.91 ? 41  CYS   A O    1 
ATOM   134  C  CB   . CYS   A 1 19  ? 97.341  84.476  13.412  1   51.46 ? 41  CYS   A CB   1 
ATOM   135  S  SG   . CYS   A 1 19  ? 97.202  85.854  12.244  1   59.1  ? 41  CYS   A SG   1 
ATOM   136  N  N    . MET   A 1 20  ? 94.33   85.754  14.999  1   48.74 ? 42  MET   A N    1 
ATOM   137  C  CA   . MET   A 1 20  ? 92.933  86.051  14.71   1   49.62 ? 42  MET   A CA   1 
ATOM   138  C  C    . MET   A 1 20  ? 92.819  86.905  13.44   1   50.69 ? 42  MET   A C    1 
ATOM   139  O  O    . MET   A 1 20  ? 93.287  88.042  13.427  1   50.51 ? 42  MET   A O    1 
ATOM   140  C  CB   . MET   A 1 20  ? 92.285  86.794  15.878  1   49.8  ? 42  MET   A CB   1 
ATOM   141  C  CG   . MET   A 1 20  ? 92.091  85.934  17.101  1   50.76 ? 42  MET   A CG   1 
ATOM   142  S  SD   . MET   A 1 20  ? 91.966  86.947  18.577  1   52.75 ? 42  MET   A SD   1 
ATOM   143  C  CE   . MET   A 1 20  ? 90.471  87.809  18.26   1   52.98 ? 42  MET   A CE   1 
ATOM   144  N  N    . LEU   A 1 21  ? 92.182  86.362  12.397  1   51.22 ? 43  LEU   A N    1 
ATOM   145  C  CA   . LEU   A 1 21  ? 91.982  87.055  11.136  1   52.27 ? 43  LEU   A CA   1 
ATOM   146  C  C    . LEU   A 1 21  ? 91.039  88.233  11.271  1   54.27 ? 43  LEU   A C    1 
ATOM   147  O  O    . LEU   A 1 21  ? 91.28   89.251  10.626  1   55.15 ? 43  LEU   A O    1 
ATOM   148  C  CB   . LEU   A 1 21  ? 91.566  86.105  10.002  1   51.59 ? 43  LEU   A CB   1 
ATOM   149  C  CG   . LEU   A 1 21  ? 92.64   85.089  9.591   1   52.24 ? 43  LEU   A CG   1 
ATOM   150  C  CD1  . LEU   A 1 21  ? 92.153  84.2    8.452   1   52.7  ? 43  LEU   A CD1  1 
ATOM   151  C  CD2  . LEU   A 1 21  ? 93.965  85.764  9.236   1   52.29 ? 43  LEU   A CD2  1 
ATOM   152  N  N    . SER   A 1 22  ? 90.034  88.153  12.149  1   54.93 ? 44  SER   A N    1 
ATOM   153  C  CA   . SER   A 1 22  ? 89.15   89.295  12.382  1   56.4  ? 44  SER   A CA   1 
ATOM   154  C  C    . SER   A 1 22  ? 89.942  90.462  13.024  1   58.95 ? 44  SER   A C    1 
ATOM   155  O  O    . SER   A 1 22  ? 89.636  91.62   12.758  1   59.39 ? 44  SER   A O    1 
ATOM   156  C  CB   . SER   A 1 22  ? 87.968  88.9    13.26   1   56.65 ? 44  SER   A CB   1 
ATOM   157  O  OG   . SER   A 1 22  ? 88.386  88.577  14.575  1   58    ? 44  SER   A OG   1 
ATOM   158  N  N    . GLU   A 1 23  ? 90.961  90.159  13.856  1   60.25 ? 45  GLU   A N    1 
ATOM   159  C  CA   . GLU   A 1 23  ? 91.808  91.176  14.469  1   61.88 ? 45  GLU   A CA   1 
ATOM   160  C  C    . GLU   A 1 23  ? 92.71   91.802  13.379  1   63.17 ? 45  GLU   A C    1 
ATOM   161  O  O    . GLU   A 1 23  ? 92.858  93.026  13.337  1   63.54 ? 45  GLU   A O    1 
ATOM   162  C  CB   . GLU   A 1 23  ? 92.655  90.572  15.606  1   64.31 ? 45  GLU   A CB   1 
ATOM   163  C  CG   . GLU   A 1 23  ? 93.648  91.548  16.222  1   68.96 ? 45  GLU   A CG   1 
ATOM   164  C  CD   . GLU   A 1 23  ? 94.793  90.908  16.984  1   75.27 ? 45  GLU   A CD   1 
ATOM   165  O  OE1  . GLU   A 1 23  ? 95.96   91.315  16.774  1   76.41 ? 45  GLU   A OE1  1 
ATOM   166  O  OE2  . GLU   A 1 23  ? 94.522  89.993  17.794  1   77.54 ? 45  GLU   A OE2  1 
ATOM   167  N  N    . GLU   A 1 24  ? 93.247  90.971  12.462  1   63.6  ? 46  GLU   A N    1 
ATOM   168  C  CA   . GLU   A 1 24  ? 94.07   91.428  11.339  1   64.66 ? 46  GLU   A CA   1 
ATOM   169  C  C    . GLU   A 1 24  ? 93.284  92.393  10.429  1   66.03 ? 46  GLU   A C    1 
ATOM   170  O  O    . GLU   A 1 24  ? 93.861  93.329  9.888   1   66.58 ? 46  GLU   A O    1 
ATOM   171  C  CB   . GLU   A 1 24  ? 94.572  90.238  10.514  1   66.05 ? 46  GLU   A CB   1 
ATOM   172  C  CG   . GLU   A 1 24  ? 95.928  89.717  10.941  1   69.81 ? 46  GLU   A CG   1 
ATOM   173  C  CD   . GLU   A 1 24  ? 96.731  89.148  9.79    1   74.5  ? 46  GLU   A CD   1 
ATOM   174  N  N    . ASP   A 1 25  ? 91.968  92.173  10.282  1   66.17 ? 47  ASP   A N    1 
ATOM   175  C  CA   . ASP   A 1 25  ? 91.094  93.026  9.48    1   66.52 ? 47  ASP   A CA   1 
ATOM   176  C  C    . ASP   A 1 25  ? 90.528  94.225  10.274  1   67    ? 47  ASP   A C    1 
ATOM   177  O  O    . ASP   A 1 25  ? 89.561  94.847  9.832   1   67.48 ? 47  ASP   A O    1 
ATOM   178  C  CB   . ASP   A 1 25  ? 89.956  92.186  8.884   1   67.64 ? 47  ASP   A CB   1 
ATOM   179  C  CG   . ASP   A 1 25  ? 89.29   92.799  7.674   1   70.17 ? 47  ASP   A CG   1 
ATOM   180  O  OD1  . ASP   A 1 25  ? 90.016  93.259  6.77    1   70.73 ? 47  ASP   A OD1  1 
ATOM   181  O  OD2  . ASP   A 1 25  ? 88.044  92.82   7.633   1   71.55 ? 47  ASP   A OD2  1 
ATOM   182  N  N    . LYS   A 1 26  ? 91.135  94.549  11.436  1   66.72 ? 48  LYS   A N    1 
ATOM   183  C  CA   . LYS   A 1 26  ? 90.777  95.658  12.316  1   66.96 ? 48  LYS   A CA   1 
ATOM   184  C  C    . LYS   A 1 26  ? 89.327  95.639  12.791  1   66.84 ? 48  LYS   A C    1 
ATOM   185  O  O    . LYS   A 1 26  ? 88.769  96.695  13.075  1   67.3  ? 48  LYS   A O    1 
ATOM   186  C  CB   . LYS   A 1 26  ? 91.133  97.015  11.692  1   68.94 ? 48  LYS   A CB   1 
ATOM   187  N  N    . ARG   A 1 27  ? 88.722  94.448  12.904  1   66.07 ? 49  ARG   A N    1 
ATOM   188  C  CA   . ARG   A 1 27  ? 87.369  94.285  13.456  1   65.43 ? 49  ARG   A CA   1 
ATOM   189  C  C    . ARG   A 1 27  ? 87.382  92.994  14.294  1   64.07 ? 49  ARG   A C    1 
ATOM   190  O  O    . ARG   A 1 27  ? 86.795  91.985  13.899  1   64.18 ? 49  ARG   A O    1 
ATOM   191  C  CB   . ARG   A 1 27  ? 86.317  94.211  12.339  1   66.66 ? 49  ARG   A CB   1 
ATOM   192  N  N    . PRO   A 1 28  ? 88.133  92.987  15.412  1   62.39 ? 50  PRO   A N    1 
ATOM   193  C  CA   . PRO   A 1 28  ? 88.281  91.746  16.178  1   60.67 ? 50  PRO   A CA   1 
ATOM   194  C  C    . PRO   A 1 28  ? 87.014  91.207  16.814  1   58.24 ? 50  PRO   A C    1 
ATOM   195  O  O    . PRO   A 1 28  ? 86.186  91.959  17.32   1   57.95 ? 50  PRO   A O    1 
ATOM   196  C  CB   . PRO   A 1 28  ? 89.344  92.099  17.225  1   61.96 ? 50  PRO   A CB   1 
ATOM   197  C  CG   . PRO   A 1 28  ? 89.233  93.579  17.391  1   63.01 ? 50  PRO   A CG   1 
ATOM   198  C  CD   . PRO   A 1 28  ? 88.923  94.084  16.009  1   61.82 ? 50  PRO   A CD   1 
ATOM   199  N  N    . VAL   A 1 29  ? 86.867  89.881  16.756  1   56.5  ? 51  VAL   A N    1 
ATOM   200  C  CA   . VAL   A 1 29  ? 85.772  89.164  17.394  1   55.19 ? 51  VAL   A CA   1 
ATOM   201  C  C    . VAL   A 1 29  ? 86.43   88.345  18.493  1   52.91 ? 51  VAL   A C    1 
ATOM   202  O  O    . VAL   A 1 29  ? 87.236  87.461  18.197  1   52.71 ? 51  VAL   A O    1 
ATOM   203  C  CB   . VAL   A 1 29  ? 84.996  88.27   16.414  1   56.1  ? 51  VAL   A CB   1 
ATOM   204  C  CG1  . VAL   A 1 29  ? 83.854  87.569  17.132  1   56.54 ? 51  VAL   A CG1  1 
ATOM   205  C  CG2  . VAL   A 1 29  ? 84.473  89.091  15.245  1   56.74 ? 51  VAL   A CG2  1 
ATOM   206  N  N    . HIS   A 1 30  ? 86.139  88.684  19.756  1   50.93 ? 52  HIS   A N    1 
ATOM   207  C  CA   . HIS   A 1 30  ? 86.75   88.042  20.92   1   49.33 ? 52  HIS   A CA   1 
ATOM   208  C  C    . HIS   A 1 30  ? 86.754  86.499  20.863  1   46.85 ? 52  HIS   A C    1 
ATOM   209  O  O    . HIS   A 1 30  ? 87.786  85.877  21.131  1   46.63 ? 52  HIS   A O    1 
ATOM   210  C  CB   . HIS   A 1 30  ? 86.102  88.55   22.22   1   50.12 ? 52  HIS   A CB   1 
ATOM   211  C  CG   . HIS   A 1 30  ? 86.699  87.954  23.459  1   53.1  ? 52  HIS   A CG   1 
ATOM   212  N  ND1  . HIS   A 1 30  ? 86.178  86.799  24.035  1   55.21 ? 52  HIS   A ND1  1 
ATOM   213  C  CD2  . HIS   A 1 30  ? 87.752  88.372  24.195  1   54.01 ? 52  HIS   A CD2  1 
ATOM   214  C  CE1  . HIS   A 1 30  ? 86.944  86.551  25.083  1   55.51 ? 52  HIS   A CE1  1 
ATOM   215  N  NE2  . HIS   A 1 30  ? 87.918  87.457  25.205  1   55.23 ? 52  HIS   A NE2  1 
ATOM   216  N  N    . ASP   A 1 31  ? 85.63   85.893  20.461  1   44.65 ? 53  ASP   A N    1 
ATOM   217  C  CA   . ASP   A 1 31  ? 85.522  84.441  20.435  1   42.91 ? 53  ASP   A CA   1 
ATOM   218  C  C    . ASP   A 1 31  ? 86.326  83.741  19.364  1   42.71 ? 53  ASP   A C    1 
ATOM   219  O  O    . ASP   A 1 31  ? 86.442  82.516  19.444  1   43.38 ? 53  ASP   A O    1 
ATOM   220  C  CB   . ASP   A 1 31  ? 84.064  83.986  20.378  1   41.67 ? 53  ASP   A CB   1 
ATOM   221  C  CG   . ASP   A 1 31  ? 83.289  84.269  21.643  1   40.86 ? 53  ASP   A CG   1 
ATOM   222  O  OD1  . ASP   A 1 31  ? 83.86   84.88   22.575  1   40.43 ? 53  ASP   A OD1  1 
ATOM   223  O  OD2  . ASP   A 1 31  ? 82.109  83.907  21.7    1   42.99 ? 53  ASP   A OD2  1 
ATOM   224  N  N    . GLU   A 1 32  ? 86.922  84.47   18.406  1   41.48 ? 54  GLU   A N    1 
ATOM   225  C  CA   . GLU   A 1 32  ? 87.772  83.817  17.414  1   40.84 ? 54  GLU   A CA   1 
ATOM   226  C  C    . GLU   A 1 32  ? 89.011  83.189  18.094  1   40.61 ? 54  GLU   A C    1 
ATOM   227  O  O    . GLU   A 1 32  ? 89.516  82.157  17.648  1   41.15 ? 54  GLU   A O    1 
ATOM   228  C  CB   . GLU   A 1 32  ? 88.196  84.79   16.318  1   42.11 ? 54  GLU   A CB   1 
ATOM   229  C  CG   . GLU   A 1 32  ? 88.972  84.065  15.24   1   45.18 ? 54  GLU   A CG   1 
ATOM   230  C  CD   . GLU   A 1 32  ? 89.485  84.909  14.097  1   49.72 ? 54  GLU   A CD   1 
ATOM   231  O  OE1  . GLU   A 1 32  ? 89.288  86.145  14.121  1   48.93 ? 54  GLU   A OE1  1 
ATOM   232  O  OE2  . GLU   A 1 32  ? 90.124  84.331  13.189  1   51.04 ? 54  GLU   A OE2  1 
ATOM   233  N  N    . HIS   A 1 33  ? 89.477  83.803  19.199  1   39.55 ? 55  HIS   A N    1 
ATOM   234  C  CA   . HIS   A 1 33  ? 90.587  83.294  19.999  1   38.71 ? 55  HIS   A CA   1 
ATOM   235  C  C    . HIS   A 1 33  ? 90.237  81.894  20.533  1   36.47 ? 55  HIS   A C    1 
ATOM   236  O  O    . HIS   A 1 33  ? 91.039  80.984  20.389  1   36.06 ? 55  HIS   A O    1 
ATOM   237  C  CB   . HIS   A 1 33  ? 90.874  84.26   21.161  1   39.74 ? 55  HIS   A CB   1 
ATOM   238  C  CG   . HIS   A 1 33  ? 92.23   84.086  21.761  1   41.99 ? 55  HIS   A CG   1 
ATOM   239  N  ND1  . HIS   A 1 33  ? 92.48   83.1    22.682  1   43.82 ? 55  HIS   A ND1  1 
ATOM   240  C  CD2  . HIS   A 1 33  ? 93.374  84.774  21.537  1   43.08 ? 55  HIS   A CD2  1 
ATOM   241  C  CE1  . HIS   A 1 33  ? 93.758  83.212  22.998  1   44.1  ? 55  HIS   A CE1  1 
ATOM   242  N  NE2  . HIS   A 1 33  ? 94.334  84.215  22.348  1   43.99 ? 55  HIS   A NE2  1 
ATOM   243  N  N    . LEU   A 1 34  ? 89.029  81.728  21.096  1   35.9  ? 56  LEU   A N    1 
ATOM   244  C  CA   . LEU   A 1 34  ? 88.529  80.448  21.599  1   36.59 ? 56  LEU   A CA   1 
ATOM   245  C  C    . LEU   A 1 34  ? 88.449  79.438  20.462  1   37.33 ? 56  LEU   A C    1 
ATOM   246  O  O    . LEU   A 1 34  ? 88.896  78.296  20.626  1   38.16 ? 56  LEU   A O    1 
ATOM   247  C  CB   . LEU   A 1 34  ? 87.144  80.604  22.257  1   36.77 ? 56  LEU   A CB   1 
ATOM   248  C  CG   . LEU   A 1 34  ? 86.556  79.298  22.802  1   37.76 ? 56  LEU   A CG   1 
ATOM   249  C  CD1  . LEU   A 1 34  ? 87.429  78.742  23.941  1   38.56 ? 56  LEU   A CD1  1 
ATOM   250  C  CD2  . LEU   A 1 34  ? 85.126  79.471  23.232  1   37.38 ? 56  LEU   A CD2  1 
ATOM   251  N  N    . PHE   A 1 35  ? 87.933  79.869  19.294  1   36.63 ? 57  PHE   A N    1 
ATOM   252  C  CA   . PHE   A 1 35  ? 87.83   79.034  18.097  1   36.65 ? 57  PHE   A CA   1 
ATOM   253  C  C    . PHE   A 1 35  ? 89.21   78.465  17.706  1   36.76 ? 57  PHE   A C    1 
ATOM   254  O  O    . PHE   A 1 35  ? 89.331  77.275  17.431  1   37.54 ? 57  PHE   A O    1 
ATOM   255  C  CB   . PHE   A 1 35  ? 87.183  79.829  16.92   1   36.08 ? 57  PHE   A CB   1 
ATOM   256  C  CG   . PHE   A 1 35  ? 86.93   79.029  15.661  1   36.15 ? 57  PHE   A CG   1 
ATOM   257  C  CD1  . PHE   A 1 35  ? 85.775  78.27   15.518  1   36.38 ? 57  PHE   A CD1  1 
ATOM   258  C  CD2  . PHE   A 1 35  ? 87.848  79.02   14.628  1   36.82 ? 57  PHE   A CD2  1 
ATOM   259  C  CE1  . PHE   A 1 35  ? 85.549  77.53   14.367  1   36.54 ? 57  PHE   A CE1  1 
ATOM   260  C  CE2  . PHE   A 1 35  ? 87.613  78.28   13.478  1   37.38 ? 57  PHE   A CE2  1 
ATOM   261  C  CZ   . PHE   A 1 35  ? 86.461  77.549  13.353  1   36.76 ? 57  PHE   A CZ   1 
ATOM   262  N  N    . ILE   A 1 36  ? 90.244  79.297  17.716  1   36.08 ? 58  ILE   A N    1 
ATOM   263  C  CA   . ILE   A 1 36  ? 91.602  78.865  17.365  1   35.52 ? 58  ILE   A CA   1 
ATOM   264  C  C    . ILE   A 1 36  ? 92.178  77.932  18.436  1   35.22 ? 58  ILE   A C    1 
ATOM   265  O  O    . ILE   A 1 36  ? 92.677  76.86   18.098  1   35.47 ? 58  ILE   A O    1 
ATOM   266  C  CB   . ILE   A 1 36  ? 92.522  80.098  17.117  1   35.81 ? 58  ILE   A CB   1 
ATOM   267  C  CG1  . ILE   A 1 36  ? 92.089  80.905  15.868  1   37.06 ? 58  ILE   A CG1  1 
ATOM   268  C  CG2  . ILE   A 1 36  ? 93.999  79.716  17.044  1   36.17 ? 58  ILE   A CG2  1 
ATOM   269  N  N    . ILE   A 1 37  ? 92.132  78.35   19.72   1   34.42 ? 59  ILE   A N    1 
ATOM   270  C  CA   . ILE   A 1 37  ? 92.685  77.562  20.827  1   33.91 ? 59  ILE   A CA   1 
ATOM   271  C  C    . ILE   A 1 37  ? 92.046  76.155  20.922  1   32.76 ? 59  ILE   A C    1 
ATOM   272  O  O    . ILE   A 1 37  ? 92.773  75.178  21.084  1   32.32 ? 59  ILE   A O    1 
ATOM   273  C  CB   . ILE   A 1 37  ? 92.604  78.356  22.169  1   34.08 ? 59  ILE   A CB   1 
ATOM   274  C  CG1  . ILE   A 1 37  ? 93.626  79.529  22.2    1   34.38 ? 59  ILE   A CG1  1 
ATOM   275  C  CG2  . ILE   A 1 37  ? 92.764  77.438  23.399  1   34.01 ? 59  ILE   A CG2  1 
ATOM   276  C  CD1  . ILE   A 1 37  ? 95.138  79.098  22.32   1   35.18 ? 59  ILE   A CD1  1 
ATOM   277  N  N    . THR   A 1 38  ? 90.705  76.058  20.772  1   32.15 ? 60  THR   A N    1 
ATOM   278  C  CA   . THR   A 1 38  ? 89.987  74.782  20.825  1   32.19 ? 60  THR   A CA   1 
ATOM   279  C  C    . THR   A 1 38  ? 90.493  73.836  19.759  1   31.99 ? 60  THR   A C    1 
ATOM   280  O  O    . THR   A 1 38  ? 90.813  72.69   20.069  1   32.09 ? 60  THR   A O    1 
ATOM   281  C  CB   . THR   A 1 38  ? 88.457  74.968  20.695  1   33.18 ? 60  THR   A CB   1 
ATOM   282  O  OG1  . THR   A 1 38  ? 87.989  75.903  21.659  1   32.36 ? 60  THR   A OG1  1 
ATOM   283  C  CG2  . THR   A 1 38  ? 87.701  73.643  20.862  1   34.14 ? 60  THR   A CG2  1 
ATOM   284  N  N    . HIS   A 1 39  ? 90.626  74.33   18.511  1   31.32 ? 61  HIS   A N    1 
ATOM   285  C  CA   . HIS   A 1 39  ? 91.125  73.524  17.408  1   31.5  ? 61  HIS   A CA   1 
ATOM   286  C  C    . HIS   A 1 39  ? 92.553  73.105  17.629  1   31.59 ? 61  HIS   A C    1 
ATOM   287  O  O    . HIS   A 1 39  ? 92.891  71.941  17.397  1   32.96 ? 61  HIS   A O    1 
ATOM   288  C  CB   . HIS   A 1 39  ? 91.01   74.284  16.083  1   33.06 ? 61  HIS   A CB   1 
ATOM   289  C  CG   . HIS   A 1 39  ? 89.649  74.207  15.471  1   35.19 ? 61  HIS   A CG   1 
ATOM   290  N  ND1  . HIS   A 1 39  ? 88.625  75.036  15.892  1   36.64 ? 61  HIS   A ND1  1 
ATOM   291  C  CD2  . HIS   A 1 39  ? 89.178  73.37   14.517  1   36.39 ? 61  HIS   A CD2  1 
ATOM   292  C  CE1  . HIS   A 1 39  ? 87.575  74.703  15.162  1   37.72 ? 61  HIS   A CE1  1 
ATOM   293  N  NE2  . HIS   A 1 39  ? 87.862  73.716  14.311  1   37.86 ? 61  HIS   A NE2  1 
ATOM   294  N  N    . GLN   A 1 40  ? 93.389  74.014  18.127  1   30.39 ? 62  GLN   A N    1 
ATOM   295  C  CA   . GLN   A 1 40  ? 94.788  73.705  18.381  1   29.87 ? 62  GLN   A CA   1 
ATOM   296  C  C    . GLN   A 1 40  ? 94.946  72.638  19.474  1   29.33 ? 62  GLN   A C    1 
ATOM   297  O  O    . GLN   A 1 40  ? 95.791  71.766  19.336  1   30.25 ? 62  GLN   A O    1 
ATOM   298  C  CB   . GLN   A 1 40  ? 95.552  74.99   18.704  1   31.39 ? 62  GLN   A CB   1 
ATOM   299  C  CG   . GLN   A 1 40  ? 95.756  75.85   17.459  1   34.4  ? 62  GLN   A CG   1 
ATOM   300  C  CD   . GLN   A 1 40  ? 96.487  77.14   17.786  1   37.35 ? 62  GLN   A CD   1 
ATOM   301  O  OE1  . GLN   A 1 40  ? 96.389  77.69   18.881  1   37.33 ? 62  GLN   A OE1  1 
ATOM   302  N  NE2  . GLN   A 1 40  ? 97.232  77.649  16.833  1   38.07 ? 62  GLN   A NE2  1 
ATOM   303  N  N    . ALA   A 1 41  ? 94.083  72.649  20.494  1   28.41 ? 63  ALA   A N    1 
ATOM   304  C  CA   . ALA   A 1 41  ? 94.09   71.654  21.556  1   28.86 ? 63  ALA   A CA   1 
ATOM   305  C  C    . ALA   A 1 41  ? 93.665  70.298  20.974  1   29.31 ? 63  ALA   A C    1 
ATOM   306  O  O    . ALA   A 1 41  ? 94.322  69.288  21.255  1   30.1  ? 63  ALA   A O    1 
ATOM   307  C  CB   . ALA   A 1 41  ? 93.148  72.08   22.669  1   28.99 ? 63  ALA   A CB   1 
ATOM   308  N  N    . TYR   A 1 42  ? 92.643  70.277  20.07   1   28.35 ? 64  TYR   A N    1 
ATOM   309  C  CA   . TYR   A 1 42  ? 92.263  69.052  19.343  1   27.89 ? 64  TYR   A CA   1 
ATOM   310  C  C    . TYR   A 1 42  ? 93.47   68.51   18.567  1   27.43 ? 64  TYR   A C    1 
ATOM   311  O  O    . TYR   A 1 42  ? 93.804  67.341  18.721  1   27.53 ? 64  TYR   A O    1 
ATOM   312  C  CB   . TYR   A 1 42  ? 91.122  69.322  18.316  1   27.78 ? 64  TYR   A CB   1 
ATOM   313  C  CG   . TYR   A 1 42  ? 89.731  69.101  18.863  1   27.27 ? 64  TYR   A CG   1 
ATOM   314  C  CD1  . TYR   A 1 42  ? 89.228  67.818  19.044  1   27.71 ? 64  TYR   A CD1  1 
ATOM   315  C  CD2  . TYR   A 1 42  ? 88.929  70.171  19.221  1   27.33 ? 64  TYR   A CD2  1 
ATOM   316  C  CE1  . TYR   A 1 42  ? 87.975  67.609  19.599  1   28.14 ? 64  TYR   A CE1  1 
ATOM   317  C  CE2  . TYR   A 1 42  ? 87.677  69.975  19.775  1   28.27 ? 64  TYR   A CE2  1 
ATOM   318  C  CZ   . TYR   A 1 42  ? 87.201  68.694  19.958  1   29.4  ? 64  TYR   A CZ   1 
ATOM   319  O  OH   . TYR   A 1 42  ? 85.967  68.511  20.514  1   31.65 ? 64  TYR   A OH   1 
ATOM   320  N  N    . GLU   A 1 43  ? 94.157  69.368  17.788  1   26.96 ? 65  GLU   A N    1 
ATOM   321  C  CA   . GLU   A 1 43  ? 95.286  68.931  16.969  1   27.87 ? 65  GLU   A CA   1 
ATOM   322  C  C    . GLU   A 1 43  ? 96.472  68.426  17.777  1   28.98 ? 65  GLU   A C    1 
ATOM   323  O  O    . GLU   A 1 43  ? 97.151  67.489  17.329  1   29.56 ? 65  GLU   A O    1 
ATOM   324  C  CB   . GLU   A 1 43  ? 95.698  70.029  15.976  1   30.06 ? 65  GLU   A CB   1 
ATOM   325  C  CG   . GLU   A 1 43  ? 94.622  70.321  14.938  1   31.43 ? 65  GLU   A CG   1 
ATOM   326  C  CD   . GLU   A 1 43  ? 94.392  69.22   13.917  1   33.89 ? 65  GLU   A CD   1 
ATOM   327  O  OE1  . GLU   A 1 43  ? 95.345  68.46   13.623  1   34.76 ? 65  GLU   A OE1  1 
ATOM   328  O  OE2  . GLU   A 1 43  ? 93.251  69.114  13.411  1   35.9  ? 65  GLU   A OE2  1 
ATOM   329  N  N    . LEU   A 1 44  ? 96.717  68.996  18.993  1   28.7  ? 66  LEU   A N    1 
ATOM   330  C  CA   . LEU   A 1 44  ? 97.802  68.473  19.837  1   27.94 ? 66  LEU   A CA   1 
ATOM   331  C  C    . LEU   A 1 44  ? 97.447  67.042  20.272  1   27.56 ? 66  LEU   A C    1 
ATOM   332  O  O    . LEU   A 1 44  ? 98.279  66.142  20.173  1   28.45 ? 66  LEU   A O    1 
ATOM   333  C  CB   . LEU   A 1 44  ? 98.013  69.338  21.087  1   27.62 ? 66  LEU   A CB   1 
ATOM   334  C  CG   . LEU   A 1 44  ? 98.698  70.691  20.911  1   28.52 ? 66  LEU   A CG   1 
ATOM   335  C  CD1  . LEU   A 1 44  ? 98.857  71.377  22.267  1   28.91 ? 66  LEU   A CD1  1 
ATOM   336  C  CD2  . LEU   A 1 44  ? 100.085 70.539  20.205  1   27.78 ? 66  LEU   A CD2  1 
ATOM   337  N  N    . TRP   A 1 45  ? 96.211  66.828  20.711  1   26.64 ? 67  TRP   A N    1 
ATOM   338  C  CA   . TRP   A 1 45  ? 95.745  65.506  21.137  1   26.84 ? 67  TRP   A CA   1 
ATOM   339  C  C    . TRP   A 1 45  ? 95.625  64.511  19.989  1   27.55 ? 67  TRP   A C    1 
ATOM   340  O  O    . TRP   A 1 45  ? 95.913  63.345  20.202  1   28.43 ? 67  TRP   A O    1 
ATOM   341  C  CB   . TRP   A 1 45  ? 94.44   65.6    21.946  1   26.11 ? 67  TRP   A CB   1 
ATOM   342  C  CG   . TRP   A 1 45  ? 94.627  66.261  23.286  1   25.47 ? 67  TRP   A CG   1 
ATOM   343  C  CD1  . TRP   A 1 45  ? 94.099  67.448  23.694  1   25.94 ? 67  TRP   A CD1  1 
ATOM   344  C  CD2  . TRP   A 1 45  ? 95.419  65.776  24.382  1   24.9  ? 67  TRP   A CD2  1 
ATOM   345  N  NE1  . TRP   A 1 45  ? 94.502  67.731  24.976  1   25.84 ? 67  TRP   A NE1  1 
ATOM   346  C  CE2  . TRP   A 1 45  ? 95.336  66.734  25.414  1   25.61 ? 67  TRP   A CE2  1 
ATOM   347  C  CE3  . TRP   A 1 45  ? 96.226  64.643  24.575  1   25.43 ? 67  TRP   A CE3  1 
ATOM   348  C  CZ2  . TRP   A 1 45  ? 95.981  66.566  26.648  1   25.84 ? 67  TRP   A CZ2  1 
ATOM   349  C  CZ3  . TRP   A 1 45  ? 96.857  64.473  25.801  1   26.31 ? 67  TRP   A CZ3  1 
ATOM   350  C  CH2  . TRP   A 1 45  ? 96.751  65.437  26.81   1   26.03 ? 67  TRP   A CH2  1 
ATOM   351  N  N    . PHE   A 1 46  ? 95.294  64.968  18.755  1   27.31 ? 68  PHE   A N    1 
ATOM   352  C  CA   . PHE   A 1 46  ? 95.278  64.116  17.554  1   27.75 ? 68  PHE   A CA   1 
ATOM   353  C  C    . PHE   A 1 46  ? 96.7    63.601  17.314  1   28.31 ? 68  PHE   A C    1 
ATOM   354  O  O    . PHE   A 1 46  ? 96.885  62.418  17.042  1   28.99 ? 68  PHE   A O    1 
ATOM   355  C  CB   . PHE   A 1 46  ? 94.823  64.908  16.297  1   27.74 ? 68  PHE   A CB   1 
ATOM   356  C  CG   . PHE   A 1 46  ? 93.35   65.224  16.171  1   28.47 ? 68  PHE   A CG   1 
ATOM   357  C  CD1  . PHE   A 1 46  ? 92.423  64.661  17.039  1   29.32 ? 68  PHE   A CD1  1 
ATOM   358  C  CD2  . PHE   A 1 46  ? 92.899  66.118  15.216  1   28.9  ? 68  PHE   A CD2  1 
ATOM   359  C  CE1  . PHE   A 1 46  ? 91.075  64.97   16.932  1   30.07 ? 68  PHE   A CE1  1 
ATOM   360  C  CE2  . PHE   A 1 46  ? 91.552  66.43   15.114  1   29.54 ? 68  PHE   A CE2  1 
ATOM   361  C  CZ   . PHE   A 1 46  ? 90.649  65.858  15.97   1   29.79 ? 68  PHE   A CZ   1 
ATOM   362  N  N    . LYS   A 1 47  ? 97.717  64.474  17.488  1   28.07 ? 69  LYS   A N    1 
ATOM   363  C  CA   . LYS   A 1 47  ? 99.112  64.069  17.339  1   28.4  ? 69  LYS   A CA   1 
ATOM   364  C  C    . LYS   A 1 47  ? 99.486  63      18.369  1   28.52 ? 69  LYS   A C    1 
ATOM   365  O  O    . LYS   A 1 47  ? 100.188 62.05   18.039  1   29.6  ? 69  LYS   A O    1 
ATOM   366  C  CB   . LYS   A 1 47  ? 100.059 65.293  17.376  1   29.67 ? 69  LYS   A CB   1 
ATOM   367  C  CG   . LYS   A 1 47  ? 101.502 64.944  17.016  1   33.44 ? 69  LYS   A CG   1 
ATOM   368  C  CD   . LYS   A 1 47  ? 102.409 66.17   16.885  1   36.37 ? 69  LYS   A CD   1 
ATOM   369  C  CE   . LYS   A 1 47  ? 103.828 65.696  16.649  1   40.5  ? 69  LYS   A CE   1 
ATOM   370  N  NZ   . LYS   A 1 47  ? 104.782 66.808  16.398  1   42.9  ? 69  LYS   A NZ   1 
ATOM   371  N  N    . GLN   A 1 48  ? 98.967  63.113  19.593  1   27.56 ? 70  GLN   A N    1 
ATOM   372  C  CA   . GLN   A 1 48  ? 99.205  62.114  20.64   1   26.71 ? 70  GLN   A CA   1 
ATOM   373  C  C    . GLN   A 1 48  ? 98.508  60.787  20.311  1   26.25 ? 70  GLN   A C    1 
ATOM   374  O  O    . GLN   A 1 48  ? 99.105  59.727  20.446  1   26.47 ? 70  GLN   A O    1 
ATOM   375  C  CB   . GLN   A 1 48  ? 98.733  62.623  22.014  1   26.79 ? 70  GLN   A CB   1 
ATOM   376  C  CG   . GLN   A 1 48  ? 99.118  61.665  23.154  1   27.09 ? 70  GLN   A CG   1 
ATOM   377  C  CD   . GLN   A 1 48  ? 100.616 61.605  23.308  1   27.45 ? 70  GLN   A CD   1 
ATOM   378  O  OE1  . GLN   A 1 48  ? 101.297 62.627  23.18   1   28.71 ? 70  GLN   A OE1  1 
ATOM   379  N  NE2  . GLN   A 1 48  ? 101.16  60.425  23.571  1   25.03 ? 70  GLN   A NE2  1 
ATOM   380  N  N    . ILE   A 1 49  ? 97.259  60.839  19.857  1   25.73 ? 71  ILE   A N    1 
ATOM   381  C  CA   . ILE   A 1 49  ? 96.517  59.635  19.457  1   26.04 ? 71  ILE   A CA   1 
ATOM   382  C  C    . ILE   A 1 49  ? 97.229  58.929  18.312  1   26.9  ? 71  ILE   A C    1 
ATOM   383  O  O    . ILE   A 1 49  ? 97.377  57.719  18.356  1   27.74 ? 71  ILE   A O    1 
ATOM   384  C  CB   . ILE   A 1 49  ? 95.047  59.977  19.095  1   25.54 ? 71  ILE   A CB   1 
ATOM   385  C  CG1  . ILE   A 1 49  ? 94.272  60.484  20.335  1   25.69 ? 71  ILE   A CG1  1 
ATOM   386  C  CG2  . ILE   A 1 49  ? 94.353  58.806  18.418  1   25.69 ? 71  ILE   A CG2  1 
ATOM   387  C  CD1  . ILE   A 1 49  ? 92.877  61.053  20.049  1   26.39 ? 71  ILE   A CD1  1 
ATOM   388  N  N    . ILE   A 1 50  ? 97.736  59.675  17.328  1   26.97 ? 72  ILE   A N    1 
ATOM   389  C  CA   . ILE   A 1 50  ? 98.461  59.077  16.198  1   26.83 ? 72  ILE   A CA   1 
ATOM   390  C  C    . ILE   A 1 50  ? 99.737  58.408  16.707  1   27.39 ? 72  ILE   A C    1 
ATOM   391  O  O    . ILE   A 1 50  ? 99.996  57.243  16.398  1   27.58 ? 72  ILE   A O    1 
ATOM   392  C  CB   . ILE   A 1 50  ? 98.703  60.134  15.089  1   26.79 ? 72  ILE   A CB   1 
ATOM   393  C  CG1  . ILE   A 1 50  ? 97.361  60.536  14.457  1   26.57 ? 72  ILE   A CG1  1 
ATOM   394  C  CG2  . ILE   A 1 50  ? 99.688  59.615  14.026  1   27.23 ? 72  ILE   A CG2  1 
ATOM   395  C  CD1  . ILE   A 1 50  ? 97.396  61.692  13.567  1   26.64 ? 72  ILE   A CD1  1 
ATOM   396  N  N    . PHE   A 1 51  ? 100.46  59.093  17.604  1   27.62 ? 73  PHE   A N    1 
ATOM   397  C  CA   . PHE   A 1 51  ? 101.664 58.543  18.224  1   28.17 ? 73  PHE   A CA   1 
ATOM   398  C  C    . PHE   A 1 51  ? 101.382 57.235  18.97   1   28.24 ? 73  PHE   A C    1 
ATOM   399  O  O    . PHE   A 1 51  ? 102.132 56.27   18.828  1   29.2  ? 73  PHE   A O    1 
ATOM   400  C  CB   . PHE   A 1 51  ? 102.28  59.588  19.161  1   28.83 ? 73  PHE   A CB   1 
ATOM   401  C  CG   . PHE   A 1 51  ? 103.703 59.297  19.578  1   29.76 ? 73  PHE   A CG   1 
ATOM   402  C  CD1  . PHE   A 1 51  ? 104.748 59.417  18.673  1   30.63 ? 73  PHE   A CD1  1 
ATOM   403  C  CD2  . PHE   A 1 51  ? 103.995 58.9    20.871  1   30.32 ? 73  PHE   A CD2  1 
ATOM   404  C  CE1  . PHE   A 1 51  ? 106.065 59.15   19.065  1   31.66 ? 73  PHE   A CE1  1 
ATOM   405  C  CE2  . PHE   A 1 51  ? 105.311 58.656  21.263  1   31.07 ? 73  PHE   A CE2  1 
ATOM   406  C  CZ   . PHE   A 1 51  ? 106.337 58.77   20.359  1   31.01 ? 73  PHE   A CZ   1 
ATOM   407  N  N    . GLU   A 1 52  ? 100.298 57.19   19.752  1   27.37 ? 74  GLU   A N    1 
ATOM   408  C  CA   . GLU   A 1 52  ? 99.913  55.974  20.469  1   26.93 ? 74  GLU   A CA   1 
ATOM   409  C  C    . GLU   A 1 52  ? 99.499  54.876  19.492  1   27.3  ? 74  GLU   A C    1 
ATOM   410  O  O    . GLU   A 1 52  ? 99.945  53.75   19.639  1   28.21 ? 74  GLU   A O    1 
ATOM   411  C  CB   . GLU   A 1 52  ? 98.779  56.246  21.465  1   26.94 ? 74  GLU   A CB   1 
ATOM   412  C  CG   . GLU   A 1 52  ? 99.11   57.291  22.523  1   29.48 ? 74  GLU   A CG   1 
ATOM   413  C  CD   . GLU   A 1 52  ? 100.206 56.937  23.514  1   29.7  ? 74  GLU   A CD   1 
ATOM   414  O  OE1  . GLU   A 1 52  ? 100.557 55.746  23.626  1   27.34 ? 74  GLU   A OE1  1 
ATOM   415  O  OE2  . GLU   A 1 52  ? 100.717 57.859  24.185  1   33    ? 74  GLU   A OE2  1 
ATOM   416  N  N    . PHE   A 1 53  ? 98.671  55.202  18.492  1   26.94 ? 75  PHE   A N    1 
ATOM   417  C  CA   . PHE   A 1 53  ? 98.198  54.249  17.484  1   27.37 ? 75  PHE   A CA   1 
ATOM   418  C  C    . PHE   A 1 53  ? 99.36   53.61   16.729  1   27.7  ? 75  PHE   A C    1 
ATOM   419  O  O    . PHE   A 1 53  ? 99.402  52.391  16.636  1   28.2  ? 75  PHE   A O    1 
ATOM   420  C  CB   . PHE   A 1 53  ? 97.232  54.925  16.482  1   27.44 ? 75  PHE   A CB   1 
ATOM   421  C  CG   . PHE   A 1 53  ? 95.77   55.012  16.882  1   28.17 ? 75  PHE   A CG   1 
ATOM   422  C  CD1  . PHE   A 1 53  ? 95.353  54.622  18.139  1   28.98 ? 75  PHE   A CD1  1 
ATOM   423  C  CD2  . PHE   A 1 53  ? 94.809  55.445  15.976  1   28.74 ? 75  PHE   A CD2  1 
ATOM   424  C  CE1  . PHE   A 1 53  ? 93.999  54.677  18.485  1   30.17 ? 75  PHE   A CE1  1 
ATOM   425  C  CE2  . PHE   A 1 53  ? 93.468  55.503  16.323  1   29.14 ? 75  PHE   A CE2  1 
ATOM   426  C  CZ   . PHE   A 1 53  ? 93.067  55.123  17.574  1   29.57 ? 75  PHE   A CZ   1 
ATOM   427  N  N    . ASP   A 1 54  ? 100.332 54.407  16.247  1   27.37 ? 76  ASP   A N    1 
ATOM   428  C  CA   . ASP   A 1 54  ? 101.484 53.872  15.523  1   27.8  ? 76  ASP   A CA   1 
ATOM   429  C  C    . ASP   A 1 54  ? 102.295 52.92   16.356  1   28.27 ? 76  ASP   A C    1 
ATOM   430  O  O    . ASP   A 1 54  ? 102.709 51.881  15.846  1   28.33 ? 76  ASP   A O    1 
ATOM   431  C  CB   . ASP   A 1 54  ? 102.364 54.998  14.959  1   29.72 ? 76  ASP   A CB   1 
ATOM   432  C  CG   . ASP   A 1 54  ? 101.743 55.721  13.775  1   36.96 ? 76  ASP   A CG   1 
ATOM   433  O  OD1  . ASP   A 1 54  ? 100.791 55.166  13.164  1   37.36 ? 76  ASP   A OD1  1 
ATOM   434  O  OD2  . ASP   A 1 54  ? 102.197 56.838  13.461  1   41.12 ? 76  ASP   A OD2  1 
ATOM   435  N  N    . SER   A 1 55  ? 102.473 53.222  17.659  1   28.35 ? 77  SER   A N    1 
ATOM   436  C  CA   . SER   A 1 55  ? 103.213 52.354  18.563  1   28.41 ? 77  SER   A CA   1 
ATOM   437  C  C    . SER   A 1 55  ? 102.455 51.052  18.837  1   28.74 ? 77  SER   A C    1 
ATOM   438  O  O    . SER   A 1 55  ? 103.073 50.001  18.973  1   29.39 ? 77  SER   A O    1 
ATOM   439  C  CB   . SER   A 1 55  ? 103.578 53.093  19.851  1   30.59 ? 77  SER   A CB   1 
ATOM   440  O  OG   . SER   A 1 55  ? 102.567 53.059  20.849  1   33.87 ? 77  SER   A OG   1 
ATOM   441  N  N    . ILE   A 1 56  ? 101.124 51.104  18.886  1   28.04 ? 78  ILE   A N    1 
ATOM   442  C  CA   . ILE   A 1 56  ? 100.295 49.908  19.089  1   27.96 ? 78  ILE   A CA   1 
ATOM   443  C  C    . ILE   A 1 56  ? 100.299 49.056  17.811  1   29.35 ? 78  ILE   A C    1 
ATOM   444  O  O    . ILE   A 1 56  ? 100.372 47.84   17.897  1   29.98 ? 78  ILE   A O    1 
ATOM   445  C  CB   . ILE   A 1 56  ? 98.848  50.315  19.523  1   27.05 ? 78  ILE   A CB   1 
ATOM   446  C  CG1  . ILE   A 1 56  ? 98.862  50.99   20.902  1   26.57 ? 78  ILE   A CG1  1 
ATOM   447  C  CG2  . ILE   A 1 56  ? 97.875  49.121  19.475  1   26.9  ? 78  ILE   A CG2  1 
ATOM   448  C  CD1  . ILE   A 1 56  ? 97.598  51.74   21.228  1   27.01 ? 78  ILE   A CD1  1 
ATOM   449  N  N    . ARG   A 1 57  ? 100.287 49.696  16.631  1   30.48 ? 79  ARG   A N    1 
ATOM   450  C  CA   . ARG   A 1 57  ? 100.364 49.002  15.357  1   32.81 ? 79  ARG   A CA   1 
ATOM   451  C  C    . ARG   A 1 57  ? 101.691 48.268  15.23   1   33.77 ? 79  ARG   A C    1 
ATOM   452  O  O    . ARG   A 1 57  ? 101.698 47.126  14.772  1   34.39 ? 79  ARG   A O    1 
ATOM   453  C  CB   . ARG   A 1 57  ? 100.164 49.959  14.179  1   35.59 ? 79  ARG   A CB   1 
ATOM   454  C  CG   . ARG   A 1 57  ? 98.716  50.489  14.02   1   41.71 ? 79  ARG   A CG   1 
ATOM   455  C  CD   . ARG   A 1 57  ? 98.467  51.315  12.751  1   47.1  ? 79  ARG   A CD   1 
ATOM   456  N  NE   . ARG   A 1 57  ? 99.611  52.173  12.419  1   53.58 ? 79  ARG   A NE   1 
ATOM   457  C  CZ   . ARG   A 1 57  ? 100.493 51.91   11.456  1   56.78 ? 79  ARG   A CZ   1 
ATOM   458  N  NH1  . ARG   A 1 57  ? 100.331 50.852  10.669  1   56.49 ? 79  ARG   A NH1  1 
ATOM   459  N  NH2  . ARG   A 1 57  ? 101.526 52.717  11.256  1   57.13 ? 79  ARG   A NH2  1 
ATOM   460  N  N    . ASP   A 1 58  ? 102.8   48.886  15.682  1   33.53 ? 80  ASP   A N    1 
ATOM   461  C  CA   . ASP   A 1 58  ? 104.111 48.233  15.65   1   34.44 ? 80  ASP   A CA   1 
ATOM   462  C  C    . ASP   A 1 58  ? 104.151 47.012  16.562  1   34.87 ? 80  ASP   A C    1 
ATOM   463  O  O    . ASP   A 1 58  ? 104.717 45.986  16.189  1   34.62 ? 80  ASP   A O    1 
ATOM   464  C  CB   . ASP   A 1 58  ? 105.25  49.217  16.007  1   36.2  ? 80  ASP   A CB   1 
ATOM   465  C  CG   . ASP   A 1 58  ? 105.408 50.338  14.999  1   43.66 ? 80  ASP   A CG   1 
ATOM   466  O  OD1  . ASP   A 1 58  ? 104.972 50.163  13.84   1   45.2  ? 80  ASP   A OD1  1 
ATOM   467  O  OD2  . ASP   A 1 58  ? 105.926 51.41   15.379  1   47.13 ? 80  ASP   A OD2  1 
ATOM   468  N  N    . MET   A 1 59  ? 103.541 47.108  17.753  1   35.21 ? 81  MET   A N    1 
ATOM   469  C  CA   . MET   A 1 59  ? 103.524 45.984  18.69   1   35.74 ? 81  MET   A CA   1 
ATOM   470  C  C    . MET   A 1 59  ? 102.63  44.841  18.179  1   36.83 ? 81  MET   A C    1 
ATOM   471  O  O    . MET   A 1 59  ? 102.932 43.67   18.428  1   36.81 ? 81  MET   A O    1 
ATOM   472  C  CB   . MET   A 1 59  ? 103.074 46.44   20.085  1   36.15 ? 81  MET   A CB   1 
ATOM   473  C  CG   . MET   A 1 59  ? 104.06  47.366  20.778  1   37.04 ? 81  MET   A CG   1 
ATOM   474  S  SD   . MET   A 1 59  ? 103.583 47.661  22.496  1   39.03 ? 81  MET   A SD   1 
ATOM   475  C  CE   . MET   A 1 59  ? 102.585 49.111  22.34   1   31.86 ? 81  MET   A CE   1 
ATOM   476  N  N    . LEU   A 1 60  ? 101.538 45.18   17.467  1   37.63 ? 82  LEU   A N    1 
ATOM   477  C  CA   . LEU   A 1 60  ? 100.615 44.199  16.873  1   39.27 ? 82  LEU   A CA   1 
ATOM   478  C  C    . LEU   A 1 60  ? 101.159 43.583  15.559  1   42.15 ? 82  LEU   A C    1 
ATOM   479  O  O    . LEU   A 1 60  ? 100.74  42.503  15.171  1   42.4  ? 82  LEU   A O    1 
ATOM   480  C  CB   . LEU   A 1 60  ? 99.241  44.834  16.616  1   38.42 ? 82  LEU   A CB   1 
ATOM   481  C  CG   . LEU   A 1 60  ? 98.369  45.081  17.848  1   38.68 ? 82  LEU   A CG   1 
ATOM   482  C  CD1  . LEU   A 1 60  ? 97.08   45.759  17.455  1   38.95 ? 82  LEU   A CD1  1 
ATOM   483  C  CD2  . LEU   A 1 60  ? 98.076  43.776  18.588  1   38.41 ? 82  LEU   A CD2  1 
ATOM   484  N  N    . ASP   A 1 61  ? 102.086 44.265  14.88   1   44.34 ? 83  ASP   A N    1 
ATOM   485  C  CA   . ASP   A 1 61  ? 102.673 43.758  13.636  1   46.8  ? 83  ASP   A CA   1 
ATOM   486  C  C    . ASP   A 1 61  ? 103.869 42.872  13.97   1   49.4  ? 83  ASP   A C    1 
ATOM   487  O  O    . ASP   A 1 61  ? 105.005 43.166  13.607  1   50.38 ? 83  ASP   A O    1 
ATOM   488  C  CB   . ASP   A 1 61  ? 103.098 44.92   12.71   1   47.92 ? 83  ASP   A CB   1 
ATOM   489  C  CG   . ASP   A 1 61  ? 103.11  44.588  11.231  1   51.52 ? 83  ASP   A CG   1 
ATOM   490  O  OD1  . ASP   A 1 61  ? 102.812 43.43   10.881  1   51.67 ? 83  ASP   A OD1  1 
ATOM   491  O  OD2  . ASP   A 1 61  ? 103.402 45.495  10.422  1   54    ? 83  ASP   A OD2  1 
ATOM   492  N  N    . ALA   A 1 62  ? 103.611 41.794  14.681  1   50.75 ? 84  ALA   A N    1 
ATOM   493  C  CA   . ALA   A 1 62  ? 104.638 40.85   15.091  1   52.52 ? 84  ALA   A CA   1 
ATOM   494  C  C    . ALA   A 1 62  ? 104.011 39.462  15.233  1   54.42 ? 84  ALA   A C    1 
ATOM   495  O  O    . ALA   A 1 62  ? 102.816 39.353  15.54   1   54.93 ? 84  ALA   A O    1 
ATOM   496  C  CB   . ALA   A 1 62  ? 105.247 41.289  16.414  1   52.68 ? 84  ALA   A CB   1 
ATOM   497  N  N    . GLU   A 1 63  ? 104.799 38.396  14.982  1   55.17 ? 85  GLU   A N    1 
ATOM   498  C  CA   . GLU   A 1 63  ? 104.273 37.034  15.112  1   55.92 ? 85  GLU   A CA   1 
ATOM   499  C  C    . GLU   A 1 63  ? 104.029 36.701  16.593  1   55.67 ? 85  GLU   A C    1 
ATOM   500  O  O    . GLU   A 1 63  ? 102.998 36.103  16.931  1   56.09 ? 85  GLU   A O    1 
ATOM   501  C  CB   . GLU   A 1 63  ? 105.213 36.002  14.457  1   58.36 ? 85  GLU   A CB   1 
ATOM   502  N  N    . VAL   A 1 64  ? 104.946 37.142  17.475  1   54.53 ? 86  VAL   A N    1 
ATOM   503  C  CA   . VAL   A 1 64  ? 104.816 36.906  18.908  1   54.11 ? 86  VAL   A CA   1 
ATOM   504  C  C    . VAL   A 1 64  ? 104.21  38.089  19.7    1   53.16 ? 86  VAL   A C    1 
ATOM   505  O  O    . VAL   A 1 64  ? 104.881 39.11   19.879  1   53.82 ? 86  VAL   A O    1 
ATOM   506  C  CB   . VAL   A 1 64  ? 106.182 36.496  19.5    1   55.13 ? 86  VAL   A CB   1 
ATOM   507  N  N    . ILE   A 1 65  ? 102.966 37.939  20.215  1   51.54 ? 87  ILE   A N    1 
ATOM   508  C  CA   . ILE   A 1 65  ? 102.346 38.972  21.065  1   50.39 ? 87  ILE   A CA   1 
ATOM   509  C  C    . ILE   A 1 65  ? 102.246 38.432  22.514  1   48.91 ? 87  ILE   A C    1 
ATOM   510  O  O    . ILE   A 1 65  ? 101.294 37.733  22.862  1   49.12 ? 87  ILE   A O    1 
ATOM   511  C  CB   . ILE   A 1 65  ? 101.006 39.516  20.488  1   50.79 ? 87  ILE   A CB   1 
ATOM   512  C  CG1  . ILE   A 1 65  ? 101.207 40.09   19.073  1   52    ? 87  ILE   A CG1  1 
ATOM   513  C  CG2  . ILE   A 1 65  ? 100.392 40.579  21.394  1   51.24 ? 87  ILE   A CG2  1 
ATOM   514  N  N    . ASP   A 1 66  ? 103.281 38.679  23.332  1   47.32 ? 88  ASP   A N    1 
ATOM   515  C  CA   . ASP   A 1 66  ? 103.318 38.155  24.7    1   46.04 ? 88  ASP   A CA   1 
ATOM   516  C  C    . ASP   A 1 66  ? 102.432 38.967  25.681  1   44.04 ? 88  ASP   A C    1 
ATOM   517  O  O    . ASP   A 1 66  ? 101.861 39.997  25.302  1   43.36 ? 88  ASP   A O    1 
ATOM   518  C  CB   . ASP   A 1 66  ? 104.779 37.997  25.207  1   48.25 ? 88  ASP   A CB   1 
ATOM   519  C  CG   . ASP   A 1 66  ? 105.597 39.267  25.414  1   54.57 ? 88  ASP   A CG   1 
ATOM   520  O  OD1  . ASP   A 1 66  ? 105.003 40.363  25.464  1   55.01 ? 88  ASP   A OD1  1 
ATOM   521  O  OD2  . ASP   A 1 66  ? 106.83  39.159  25.551  1   58.34 ? 88  ASP   A OD2  1 
ATOM   522  N  N    . GLU   A 1 67  ? 102.305 38.488  26.931  1   42.71 ? 89  GLU   A N    1 
ATOM   523  C  CA   . GLU   A 1 67  ? 101.505 39.157  27.935  1   42.14 ? 89  GLU   A CA   1 
ATOM   524  C  C    . GLU   A 1 67  ? 102.071 40.519  28.334  1   40.58 ? 89  GLU   A C    1 
ATOM   525  O  O    . GLU   A 1 67  ? 101.314 41.373  28.763  1   40.74 ? 89  GLU   A O    1 
ATOM   526  C  CB   . GLU   A 1 67  ? 101.381 38.284  29.178  1   45.37 ? 89  GLU   A CB   1 
ATOM   527  C  CG   . GLU   A 1 67  ? 100.607 37.004  28.977  1   53.26 ? 89  GLU   A CG   1 
ATOM   528  C  CD   . GLU   A 1 67  ? 100.446 36.223  30.272  1   63.67 ? 89  GLU   A CD   1 
ATOM   529  O  OE1  . GLU   A 1 67  ? 99.349  36.293  30.878  1   65.17 ? 89  GLU   A OE1  1 
ATOM   530  O  OE2  . GLU   A 1 67  ? 101.427 35.569  30.7    1   66.77 ? 89  GLU   A OE2  1 
ATOM   531  N  N    . THR   A 1 68  ? 103.391 40.717  28.218  1   39.25 ? 90  THR   A N    1 
ATOM   532  C  CA   . THR   A 1 68  ? 104.036 41.963  28.598  1   38.13 ? 90  THR   A CA   1 
ATOM   533  C  C    . THR   A 1 68  ? 103.67  43.065  27.597  1   36.72 ? 90  THR   A C    1 
ATOM   534  O  O    . THR   A 1 68  ? 103.338 44.181  28      1   36.31 ? 90  THR   A O    1 
ATOM   535  C  CB   . THR   A 1 68  ? 105.563 41.733  28.783  1   39.1  ? 90  THR   A CB   1 
ATOM   536  O  OG1  . THR   A 1 68  ? 105.769 40.726  29.764  1   39.99 ? 90  THR   A OG1  1 
ATOM   537  C  CG2  . THR   A 1 68  ? 106.297 42.976  29.232  1   38.86 ? 90  THR   A CG2  1 
ATOM   538  N  N    . LYS   A 1 69  ? 103.698 42.735  26.309  1   35.73 ? 91  LYS   A N    1 
ATOM   539  C  CA   . LYS   A 1 69  ? 103.34  43.654  25.235  1   35.94 ? 91  LYS   A CA   1 
ATOM   540  C  C    . LYS   A 1 69  ? 101.826 43.927  25.219  1   35.25 ? 91  LYS   A C    1 
ATOM   541  O  O    . LYS   A 1 69  ? 101.419 45.045  24.923  1   35.8  ? 91  LYS   A O    1 
ATOM   542  C  CB   . LYS   A 1 69  ? 103.805 43.108  23.859  1   38.06 ? 91  LYS   A CB   1 
ATOM   543  N  N    . THR   A 1 70  ? 101.009 42.927  25.581  1   34.21 ? 92  THR   A N    1 
ATOM   544  C  CA   . THR   A 1 70  ? 99.549  43.027  25.648  1   33.95 ? 92  THR   A CA   1 
ATOM   545  C  C    . THR   A 1 70  ? 99.147  44.045  26.711  1   32.69 ? 92  THR   A C    1 
ATOM   546  O  O    . THR   A 1 70  ? 98.281  44.886  26.456  1   32.58 ? 92  THR   A O    1 
ATOM   547  C  CB   . THR   A 1 70  ? 98.945  41.638  25.904  1   35.29 ? 92  THR   A CB   1 
ATOM   548  O  OG1  . THR   A 1 70  ? 99.346  40.784  24.83   1   37.17 ? 92  THR   A OG1  1 
ATOM   549  C  CG2  . THR   A 1 70  ? 97.44   41.665  25.996  1   34.55 ? 92  THR   A CG2  1 
ATOM   550  N  N    . LEU   A 1 71  ? 99.812  43.996  27.881  1   31.3  ? 93  LEU   A N    1 
ATOM   551  C  CA   . LEU   A 1 71  ? 99.593  44.943  28.968  1   31.23 ? 93  LEU   A CA   1 
ATOM   552  C  C    . LEU   A 1 71  ? 99.908  46.37   28.521  1   30.86 ? 93  LEU   A C    1 
ATOM   553  O  O    . LEU   A 1 71  ? 99.227  47.303  28.923  1   31.73 ? 93  LEU   A O    1 
ATOM   554  C  CB   . LEU   A 1 71  ? 100.495 44.594  30.155  1   31.57 ? 93  LEU   A CB   1 
ATOM   555  C  CG   . LEU   A 1 71  ? 100.045 43.438  31.008  1   34.23 ? 93  LEU   A CG   1 
ATOM   556  C  CD1  . LEU   A 1 71  ? 101.062 43.134  32.091  1   34.52 ? 93  LEU   A CD1  1 
ATOM   557  C  CD2  . LEU   A 1 71  ? 98.69   43.744  31.655  1   35.69 ? 93  LEU   A CD2  1 
ATOM   558  N  N    . GLU   A 1 72  ? 100.949 46.538  27.707  1   29.76 ? 94  GLU   A N    1 
ATOM   559  C  CA   . GLU   A 1 72  ? 101.371 47.844  27.217  1   28.91 ? 94  GLU   A CA   1 
ATOM   560  C  C    . GLU   A 1 72  ? 100.397 48.383  26.186  1   28.65 ? 94  GLU   A C    1 
ATOM   561  O  O    . GLU   A 1 72  ? 100.178 49.589  26.121  1   29.47 ? 94  GLU   A O    1 
ATOM   562  C  CB   . GLU   A 1 72  ? 102.799 47.75   26.644  1   29.48 ? 94  GLU   A CB   1 
ATOM   563  C  CG   . GLU   A 1 72  ? 103.462 49.094  26.422  1   33.64 ? 94  GLU   A CG   1 
ATOM   564  C  CD   . GLU   A 1 72  ? 103.87  49.872  27.661  1   39.08 ? 94  GLU   A CD   1 
ATOM   565  O  OE1  . GLU   A 1 72  ? 103.84  49.311  28.781  1   41.16 ? 94  GLU   A OE1  1 
ATOM   566  O  OE2  . GLU   A 1 72  ? 104.218 51.061  27.507  1   41.58 ? 94  GLU   A OE2  1 
ATOM   567  N  N    . ILE   A 1 73  ? 99.831  47.498  25.354  1   27.9  ? 95  ILE   A N    1 
ATOM   568  C  CA   . ILE   A 1 73  ? 98.836  47.897  24.364  1   27.78 ? 95  ILE   A CA   1 
ATOM   569  C  C    . ILE   A 1 73  ? 97.564  48.343  25.11   1   26.56 ? 95  ILE   A C    1 
ATOM   570  O  O    . ILE   A 1 73  ? 97.022  49.389  24.794  1   27    ? 95  ILE   A O    1 
ATOM   571  C  CB   . ILE   A 1 73  ? 98.548  46.723  23.387  1   28.12 ? 95  ILE   A CB   1 
ATOM   572  C  CG1  . ILE   A 1 73  ? 99.773  46.437  22.493  1   29.31 ? 95  ILE   A CG1  1 
ATOM   573  C  CG2  . ILE   A 1 73  ? 97.336  47.026  22.526  1   28.28 ? 95  ILE   A CG2  1 
ATOM   574  C  CD1  . ILE   A 1 73  ? 99.685  45.074  21.704  1   30.04 ? 95  ILE   A CD1  1 
ATOM   575  N  N    . VAL   A 1 74  ? 97.113  47.56   26.113  1   25.5  ? 96  VAL   A N    1 
ATOM   576  C  CA   . VAL   A 1 74  ? 95.934  47.867  26.937  1   25.08 ? 96  VAL   A CA   1 
ATOM   577  C  C    . VAL   A 1 74  ? 96.124  49.228  27.636  1   25.13 ? 96  VAL   A C    1 
ATOM   578  O  O    . VAL   A 1 74  ? 95.209  50.053  27.616  1   25.46 ? 96  VAL   A O    1 
ATOM   579  C  CB   . VAL   A 1 74  ? 95.636  46.707  27.928  1   24.95 ? 96  VAL   A CB   1 
ATOM   580  C  CG1  . VAL   A 1 74  ? 94.717  47.142  29.057  1   24.32 ? 96  VAL   A CG1  1 
ATOM   581  C  CG2  . VAL   A 1 74  ? 95.056  45.503  27.182  1   25.58 ? 96  VAL   A CG2  1 
ATOM   582  N  N    . LYS   A 1 75  ? 97.335  49.494  28.162  1   24.32 ? 97  LYS   A N    1 
ATOM   583  C  CA   . LYS   A 1 75  ? 97.625  50.779  28.785  1   24.49 ? 97  LYS   A CA   1 
ATOM   584  C  C    . LYS   A 1 75  ? 97.461  51.936  27.804  1   23.63 ? 97  LYS   A C    1 
ATOM   585  O  O    . LYS   A 1 75  ? 96.862  52.945  28.152  1   22.76 ? 97  LYS   A O    1 
ATOM   586  C  CB   . LYS   A 1 75  ? 99.045  50.795  29.411  1   26.5  ? 97  LYS   A CB   1 
ATOM   587  C  CG   . LYS   A 1 75  ? 99.485  52.181  29.932  1   29.96 ? 97  LYS   A CG   1 
ATOM   588  C  CD   . LYS   A 1 75  ? 100.771 52.087  30.721  1   34.23 ? 97  LYS   A CD   1 
ATOM   589  C  CE   . LYS   A 1 75  ? 101.927 51.812  29.823  1   37.73 ? 97  LYS   A CE   1 
ATOM   590  N  NZ   . LYS   A 1 75  ? 103.11  51.351  30.595  1   37.56 ? 97  LYS   A NZ   1 
ATOM   591  N  N    . ARG   A 1 76  ? 98.009  51.803  26.588  1   23.97 ? 98  ARG   A N    1 
ATOM   592  C  CA   . ARG   A 1 76  ? 97.961  52.9    25.611  1   24.14 ? 98  ARG   A CA   1 
ATOM   593  C  C    . ARG   A 1 76  ? 96.59   53.061  24.965  1   23.99 ? 98  ARG   A C    1 
ATOM   594  O  O    . ARG   A 1 76  ? 96.188  54.189  24.672  1   24.02 ? 98  ARG   A O    1 
ATOM   595  C  CB   . ARG   A 1 76  ? 99.083  52.776  24.583  1   25.39 ? 98  ARG   A CB   1 
ATOM   596  C  CG   . ARG   A 1 76  ? 100.45  52.69   25.274  1   27.72 ? 98  ARG   A CG   1 
ATOM   597  C  CD   . ARG   A 1 76  ? 101.604 52.643  24.284  1   28.98 ? 98  ARG   A CD   1 
ATOM   598  N  NE   . ARG   A 1 76  ? 102.885 52.468  24.969  1   30.46 ? 98  ARG   A NE   1 
ATOM   599  C  CZ   . ARG   A 1 76  ? 104.047 52.268  24.349  1   32.02 ? 98  ARG   A CZ   1 
ATOM   600  N  NH1  . ARG   A 1 76  ? 104.103 52.23   23.028  1   32.1  ? 98  ARG   A NH1  1 
ATOM   601  N  NH2  . ARG   A 1 76  ? 105.164 52.133  25.049  1   30.6  ? 98  ARG   A NH2  1 
ATOM   602  N  N    . LEU   A 1 77  ? 95.834  51.963  24.811  1   23.83 ? 99  LEU   A N    1 
ATOM   603  C  CA   . LEU   A 1 77  ? 94.458  52.059  24.293  1   23.46 ? 99  LEU   A CA   1 
ATOM   604  C  C    . LEU   A 1 77  ? 93.608  52.781  25.346  1   22.6  ? 99  LEU   A C    1 
ATOM   605  O  O    . LEU   A 1 77  ? 92.824  53.643  24.986  1   22.69 ? 99  LEU   A O    1 
ATOM   606  C  CB   . LEU   A 1 77  ? 93.862  50.673  23.999  1   23.34 ? 99  LEU   A CB   1 
ATOM   607  C  CG   . LEU   A 1 77  ? 94.354  49.962  22.756  1   24.06 ? 99  LEU   A CG   1 
ATOM   608  C  CD1  . LEU   A 1 77  ? 93.837  48.494  22.725  1   24.6  ? 99  LEU   A CD1  1 
ATOM   609  C  CD2  . LEU   A 1 77  ? 93.94   50.713  21.499  1   23.56 ? 99  LEU   A CD2  1 
ATOM   610  N  N    . ASN   A 1 78  ? 93.811  52.466  26.643  1   22.17 ? 100 ASN   A N    1 
ATOM   611  C  CA   . ASN   A 1 78  ? 93.095  53.109  27.738  1   22.94 ? 100 ASN   A CA   1 
ATOM   612  C  C    . ASN   A 1 78  ? 93.395  54.617  27.775  1   23.96 ? 100 ASN   A C    1 
ATOM   613  O  O    . ASN   A 1 78  ? 92.492  55.427  28.013  1   24.48 ? 100 ASN   A O    1 
ATOM   614  C  CB   . ASN   A 1 78  ? 93.408  52.439  29.086  1   22.55 ? 100 ASN   A CB   1 
ATOM   615  C  CG   . ASN   A 1 78  ? 92.648  53.094  30.203  1   26.47 ? 100 ASN   A CG   1 
ATOM   616  O  OD1  . ASN   A 1 78  ? 91.439  52.93   30.33   1   29.07 ? 100 ASN   A OD1  1 
ATOM   617  N  ND2  . ASN   A 1 78  ? 93.324  53.913  30.994  1   25.21 ? 100 ASN   A ND2  1 
ATOM   618  N  N    . ARG   A 1 79  ? 94.646  54.982  27.507  1   23.74 ? 101 ARG   A N    1 
ATOM   619  C  CA   . ARG   A 1 79  ? 95.086  56.369  27.433  1   24.18 ? 101 ARG   A CA   1 
ATOM   620  C  C    . ARG   A 1 79  ? 94.369  57.076  26.296  1   24.21 ? 101 ARG   A C    1 
ATOM   621  O  O    . ARG   A 1 79  ? 93.892  58.184  26.497  1   25.19 ? 101 ARG   A O    1 
ATOM   622  C  CB   . ARG   A 1 79  ? 96.597  56.402  27.207  1   25.1  ? 101 ARG   A CB   1 
ATOM   623  C  CG   . ARG   A 1 79  ? 97.185  57.788  27.039  1   25.69 ? 101 ARG   A CG   1 
ATOM   624  C  CD   . ARG   A 1 79  ? 98.653  57.663  26.755  1   24.42 ? 101 ARG   A CD   1 
ATOM   625  N  NE   . ARG   A 1 79  ? 99.34   57.058  27.889  1   25.74 ? 101 ARG   A NE   1 
ATOM   626  C  CZ   . ARG   A 1 79  ? 100.626 56.728  27.901  1   25.98 ? 101 ARG   A CZ   1 
ATOM   627  N  NH1  . ARG   A 1 79  ? 101.378 56.903  26.813  1   25.7  ? 101 ARG   A NH1  1 
ATOM   628  N  NH2  . ARG   A 1 79  ? 101.168 56.215  28.988  1   23.03 ? 101 ARG   A NH2  1 
ATOM   629  N  N    . VAL   A 1 80  ? 94.239  56.426  25.119  1   23.86 ? 102 VAL   A N    1 
ATOM   630  C  CA   . VAL   A 1 80  ? 93.502  56.99   23.98   1   23.6  ? 102 VAL   A CA   1 
ATOM   631  C  C    . VAL   A 1 80  ? 92.022  57.18   24.352  1   23.27 ? 102 VAL   A C    1 
ATOM   632  O  O    . VAL   A 1 80  ? 91.455  58.194  24.013  1   24.11 ? 102 VAL   A O    1 
ATOM   633  C  CB   . VAL   A 1 80  ? 93.681  56.148  22.686  1   24.4  ? 102 VAL   A CB   1 
ATOM   634  C  CG1  . VAL   A 1 80  ? 92.687  56.577  21.599  1   23.95 ? 102 VAL   A CG1  1 
ATOM   635  C  CG2  . VAL   A 1 80  ? 95.12   56.243  22.171  1   25.45 ? 102 VAL   A CG2  1 
ATOM   636  N  N    . VAL   A 1 81  ? 91.417  56.245  25.101  1   22.92 ? 103 VAL   A N    1 
ATOM   637  C  CA   . VAL   A 1 81  ? 90.034  56.359  25.595  1   22.8  ? 103 VAL   A CA   1 
ATOM   638  C  C    . VAL   A 1 81  ? 89.9    57.634  26.468  1   23.99 ? 103 VAL   A C    1 
ATOM   639  O  O    . VAL   A 1 81  ? 88.978  58.418  26.26   1   25.35 ? 103 VAL   A O    1 
ATOM   640  C  CB   . VAL   A 1 81  ? 89.612  55.084  26.379  1   22.24 ? 103 VAL   A CB   1 
ATOM   641  C  CG1  . VAL   A 1 81  ? 88.365  55.329  27.234  1   22.2  ? 103 VAL   A CG1  1 
ATOM   642  C  CG2  . VAL   A 1 81  ? 89.404  53.898  25.44   1   21.88 ? 103 VAL   A CG2  1 
ATOM   643  N  N    . LEU   A 1 82  ? 90.844  57.866  27.398  1   22.76 ? 104 LEU   A N    1 
ATOM   644  C  CA   . LEU   A 1 82  ? 90.817  59.057  28.243  1   22.89 ? 104 LEU   A CA   1 
ATOM   645  C  C    . LEU   A 1 82  ? 90.963  60.325  27.408  1   23.68 ? 104 LEU   A C    1 
ATOM   646  O  O    . LEU   A 1 82  ? 90.268  61.314  27.674  1   24.91 ? 104 LEU   A O    1 
ATOM   647  C  CB   . LEU   A 1 82  ? 91.926  59      29.323  1   22.33 ? 104 LEU   A CB   1 
ATOM   648  C  CG   . LEU   A 1 82  ? 91.806  57.842  30.339  1   23.98 ? 104 LEU   A CG   1 
ATOM   649  C  CD1  . LEU   A 1 82  ? 92.963  57.863  31.343  1   23.86 ? 104 LEU   A CD1  1 
ATOM   650  C  CD2  . LEU   A 1 82  ? 90.466  57.919  31.124  1   24.57 ? 104 LEU   A CD2  1 
ATOM   651  N  N    . ILE   A 1 83  ? 91.847  60.308  26.414  1   23.38 ? 105 ILE   A N    1 
ATOM   652  C  CA   . ILE   A 1 83  ? 92.048  61.472  25.536  1   24.42 ? 105 ILE   A CA   1 
ATOM   653  C  C    . ILE   A 1 83  ? 90.778  61.752  24.722  1   26.85 ? 105 ILE   A C    1 
ATOM   654  O  O    . ILE   A 1 83  ? 90.389  62.911  24.591  1   28.21 ? 105 ILE   A O    1 
ATOM   655  C  CB   . ILE   A 1 83  ? 93.287  61.285  24.61   1   23.18 ? 105 ILE   A CB   1 
ATOM   656  C  CG1  . ILE   A 1 83  ? 94.569  61.214  25.425  1   22.86 ? 105 ILE   A CG1  1 
ATOM   657  C  CG2  . ILE   A 1 83  ? 93.38   62.388  23.551  1   22.85 ? 105 ILE   A CG2  1 
ATOM   658  C  CD1  . ILE   A 1 83  ? 95.847  60.739  24.575  1   22.86 ? 105 ILE   A CD1  1 
ATOM   659  N  N    . LEU   A 1 84  ? 90.113  60.694  24.207  1   26.96 ? 106 LEU   A N    1 
ATOM   660  C  CA   . LEU   A 1 84  ? 88.874  60.843  23.437  1   27.23 ? 106 LEU   A CA   1 
ATOM   661  C  C    . LEU   A 1 84  ? 87.722  61.384  24.304  1   27.45 ? 106 LEU   A C    1 
ATOM   662  O  O    . LEU   A 1 84  ? 86.935  62.204  23.813  1   28.28 ? 106 LEU   A O    1 
ATOM   663  C  CB   . LEU   A 1 84  ? 88.484  59.527  22.724  1   26.98 ? 106 LEU   A CB   1 
ATOM   664  C  CG   . LEU   A 1 84  ? 89.313  59.186  21.456  1   26.84 ? 106 LEU   A CG   1 
ATOM   665  C  CD1  . LEU   A 1 84  ? 89.036  57.754  20.959  1   26.16 ? 106 LEU   A CD1  1 
ATOM   666  C  CD2  . LEU   A 1 84  ? 89.074  60.203  20.34   1   26.79 ? 106 LEU   A CD2  1 
ATOM   667  N  N    . LYS   A 1 85  ? 87.64   60.982  25.589  1   26.58 ? 107 LYS   A N    1 
ATOM   668  C  CA   . LYS   A 1 85  ? 86.603  61.54   26.473  1   27.48 ? 107 LYS   A CA   1 
ATOM   669  C  C    . LYS   A 1 85  ? 86.841  63.028  26.694  1   27.48 ? 107 LYS   A C    1 
ATOM   670  O  O    . LYS   A 1 85  ? 85.895  63.799  26.726  1   27.51 ? 107 LYS   A O    1 
ATOM   671  C  CB   . LYS   A 1 85  ? 86.53   60.819  27.83   1   29.7  ? 107 LYS   A CB   1 
ATOM   672  C  CG   . LYS   A 1 85  ? 86.07   59.376  27.733  1   35.23 ? 107 LYS   A CG   1 
ATOM   673  C  CD   . LYS   A 1 85  ? 86.219  58.661  29.063  1   40.88 ? 107 LYS   A CD   1 
ATOM   674  C  CE   . LYS   A 1 85  ? 85.245  57.513  29.171  1   46    ? 107 LYS   A CE   1 
ATOM   675  N  NZ   . LYS   A 1 85  ? 85.299  56.883  30.515  1   49.34 ? 107 LYS   A NZ   1 
ATOM   676  N  N    . LEU   A 1 86  ? 88.107  63.434  26.81   1   27.65 ? 108 LEU   A N    1 
ATOM   677  C  CA   . LEU   A 1 86  ? 88.488  64.825  26.961  1   27.78 ? 108 LEU   A CA   1 
ATOM   678  C  C    . LEU   A 1 86  ? 88.111  65.621  25.711  1   28.18 ? 108 LEU   A C    1 
ATOM   679  O  O    . LEU   A 1 86  ? 87.599  66.729  25.83   1   28.47 ? 108 LEU   A O    1 
ATOM   680  C  CB   . LEU   A 1 86  ? 89.999  64.919  27.199  1   27.59 ? 108 LEU   A CB   1 
ATOM   681  C  CG   . LEU   A 1 86  ? 90.502  66.287  27.665  1   28.22 ? 108 LEU   A CG   1 
ATOM   682  C  CD1  . LEU   A 1 86  ? 90.426  66.389  29.177  1   27.41 ? 108 LEU   A CD1  1 
ATOM   683  C  CD2  . LEU   A 1 86  ? 91.941  66.503  27.225  1   28.34 ? 108 LEU   A CD2  1 
ATOM   684  N  N    . LEU   A 1 87  ? 88.336  65.054  24.517  1   28.19 ? 109 LEU   A N    1 
ATOM   685  C  CA   . LEU   A 1 87  ? 88.005  65.71   23.243  1   28.72 ? 109 LEU   A CA   1 
ATOM   686  C  C    . LEU   A 1 87  ? 86.511  65.863  23.047  1   29.78 ? 109 LEU   A C    1 
ATOM   687  O  O    . LEU   A 1 87  ? 86.063  66.87   22.521  1   30.2  ? 109 LEU   A O    1 
ATOM   688  C  CB   . LEU   A 1 87  ? 88.658  64.995  22.055  1   28.64 ? 109 LEU   A CB   1 
ATOM   689  C  CG   . LEU   A 1 87  ? 90.202  65.005  22.045  1   30.4  ? 109 LEU   A CG   1 
ATOM   690  C  CD1  . LEU   A 1 87  ? 90.753  64.304  20.823  1   30.47 ? 109 LEU   A CD1  1 
ATOM   691  C  CD2  . LEU   A 1 87  ? 90.754  66.415  22.125  1   31.84 ? 109 LEU   A CD2  1 
ATOM   692  N  N    . VAL   A 1 88  ? 85.725  64.916  23.54   1   30.59 ? 110 VAL   A N    1 
ATOM   693  C  CA   . VAL   A 1 88  ? 84.262  65.018  23.505  1   31.14 ? 110 VAL   A CA   1 
ATOM   694  C  C    . VAL   A 1 88  ? 83.84   66.195  24.412  1   32.24 ? 110 VAL   A C    1 
ATOM   695  O  O    . VAL   A 1 88  ? 82.999  66.995  24.011  1   33.62 ? 110 VAL   A O    1 
ATOM   696  C  CB   . VAL   A 1 88  ? 83.594  63.662  23.901  1   31.02 ? 110 VAL   A CB   1 
ATOM   697  C  CG1  . VAL   A 1 88  ? 82.126  63.837  24.263  1   31.34 ? 110 VAL   A CG1  1 
ATOM   698  C  CG2  . VAL   A 1 88  ? 83.751  62.638  22.787  1   30.96 ? 110 VAL   A CG2  1 
ATOM   699  N  N    . ASP   A 1 89  ? 84.493  66.365  25.585  1   31.54 ? 111 ASP   A N    1 
ATOM   700  C  CA   . ASP   A 1 89  ? 84.207  67.465  26.52   1   31.11 ? 111 ASP   A CA   1 
ATOM   701  C  C    . ASP   A 1 89  ? 84.675  68.851  26.041  1   30.85 ? 111 ASP   A C    1 
ATOM   702  O  O    . ASP   A 1 89  ? 84.307  69.846  26.645  1   31.2  ? 111 ASP   A O    1 
ATOM   703  C  CB   . ASP   A 1 89  ? 84.793  67.18   27.906  1   33    ? 111 ASP   A CB   1 
ATOM   704  C  CG   . ASP   A 1 89  ? 84.059  66.135  28.713  1   39.45 ? 111 ASP   A CG   1 
ATOM   705  O  OD1  . ASP   A 1 89  ? 82.969  65.679  28.261  1   40.71 ? 111 ASP   A OD1  1 
ATOM   706  O  OD2  . ASP   A 1 89  ? 84.561  65.767  29.793  1   42.49 ? 111 ASP   A OD2  1 
ATOM   707  N  N    . GLN   A 1 90  ? 85.486  68.925  24.987  1   30.29 ? 112 GLN   A N    1 
ATOM   708  C  CA   . GLN   A 1 90  ? 85.902  70.201  24.418  1   30.52 ? 112 GLN   A CA   1 
ATOM   709  C  C    . GLN   A 1 90  ? 84.792  70.833  23.576  1   32.36 ? 112 GLN   A C    1 
ATOM   710  O  O    . GLN   A 1 90  ? 84.847  72.044  23.329  1   33.32 ? 112 GLN   A O    1 
ATOM   711  C  CB   . GLN   A 1 90  ? 87.191  70.064  23.603  1   30.19 ? 112 GLN   A CB   1 
ATOM   712  C  CG   . GLN   A 1 90  ? 88.391  69.842  24.508  1   31.41 ? 112 GLN   A CG   1 
ATOM   713  C  CD   . GLN   A 1 90  ? 89.703  69.805  23.779  1   33.15 ? 112 GLN   A CD   1 
ATOM   714  O  OE1  . GLN   A 1 90  ? 89.801  70.088  22.57   1   33.99 ? 112 GLN   A OE1  1 
ATOM   715  N  NE2  . GLN   A 1 90  ? 90.745  69.457  24.508  1   31.32 ? 112 GLN   A NE2  1 
ATOM   716  N  N    . VAL   A 1 91  ? 83.794  70.045  23.132  1   32.27 ? 113 VAL   A N    1 
ATOM   717  C  CA   . VAL   A 1 91  ? 82.692  70.583  22.344  1   33.08 ? 113 VAL   A CA   1 
ATOM   718  C  C    . VAL   A 1 91  ? 81.845  71.585  23.179  1   33.93 ? 113 VAL   A C    1 
ATOM   719  O  O    . VAL   A 1 91  ? 81.692  72.713  22.72   1   34.22 ? 113 VAL   A O    1 
ATOM   720  C  CB   . VAL   A 1 91  ? 81.851  69.473  21.659  1   33.49 ? 113 VAL   A CB   1 
ATOM   721  C  CG1  . VAL   A 1 91  ? 80.615  70.056  20.99   1   34.1  ? 113 VAL   A CG1  1 
ATOM   722  C  CG2  . VAL   A 1 91  ? 82.697  68.707  20.651  1   33.41 ? 113 VAL   A CG2  1 
ATOM   723  N  N    . PRO   A 1 92  ? 81.369  71.268  24.416  1   33.48 ? 114 PRO   A N    1 
ATOM   724  C  CA   . PRO   A 1 92  ? 80.609  72.269  25.179  1   33.51 ? 114 PRO   A CA   1 
ATOM   725  C  C    . PRO   A 1 92  ? 81.35   73.577  25.443  1   34.49 ? 114 PRO   A C    1 
ATOM   726  O  O    . PRO   A 1 92  ? 80.71   74.597  25.658  1   34.25 ? 114 PRO   A O    1 
ATOM   727  C  CB   . PRO   A 1 92  ? 80.244  71.534  26.475  1   33.82 ? 114 PRO   A CB   1 
ATOM   728  C  CG   . PRO   A 1 92  ? 80.241  70.09   26.091  1   34    ? 114 PRO   A CG   1 
ATOM   729  C  CD   . PRO   A 1 92  ? 81.397  69.975  25.13   1   32.7  ? 114 PRO   A CD   1 
ATOM   730  N  N    . ILE   A 1 93  ? 82.683  73.556  25.422  1   35.45 ? 115 ILE   A N    1 
ATOM   731  C  CA   . ILE   A 1 93  ? 83.486  74.774  25.605  1   36.26 ? 115 ILE   A CA   1 
ATOM   732  C  C    . ILE   A 1 93  ? 83.316  75.661  24.359  1   36.76 ? 115 ILE   A C    1 
ATOM   733  O  O    . ILE   A 1 93  ? 83.069  76.841  24.509  1   37.33 ? 115 ILE   A O    1 
ATOM   734  C  CB   . ILE   A 1 93  ? 84.987  74.448  25.862  1   36.31 ? 115 ILE   A CB   1 
ATOM   735  C  CG1  . ILE   A 1 93  ? 85.182  73.729  27.223  1   36.77 ? 115 ILE   A CG1  1 
ATOM   736  C  CG2  . ILE   A 1 93  ? 85.848  75.71   25.765  1   36.47 ? 115 ILE   A CG2  1 
ATOM   737  C  CD1  . ILE   A 1 93  ? 86.584  73.163  27.46   1   37.25 ? 115 ILE   A CD1  1 
ATOM   738  N  N    . LEU   A 1 94  ? 83.469  75.113  23.14   1   36.49 ? 116 LEU   A N    1 
ATOM   739  C  CA   . LEU   A 1 94  ? 83.286  75.92   21.925  1   36.51 ? 116 LEU   A CA   1 
ATOM   740  C  C    . LEU   A 1 94  ? 81.815  76.364  21.735  1   36.47 ? 116 LEU   A C    1 
ATOM   741  O  O    . LEU   A 1 94  ? 81.566  77.444  21.209  1   36.4  ? 116 LEU   A O    1 
ATOM   742  C  CB   . LEU   A 1 94  ? 83.858  75.243  20.666  1   36.44 ? 116 LEU   A CB   1 
ATOM   743  C  CG   . LEU   A 1 94  ? 83.954  76.133  19.399  1   36.93 ? 116 LEU   A CG   1 
ATOM   744  C  CD1  . LEU   A 1 94  ? 84.699  77.436  19.679  1   36.76 ? 116 LEU   A CD1  1 
ATOM   745  C  CD2  . LEU   A 1 94  ? 84.588  75.383  18.257  1   37.47 ? 116 LEU   A CD2  1 
ATOM   746  N  N    . GLU   A 1 95  ? 80.859  75.582  22.249  1   36.61 ? 117 GLU   A N    1 
ATOM   747  C  CA   . GLU   A 1 95  ? 79.426  75.91   22.207  1   37.38 ? 117 GLU   A CA   1 
ATOM   748  C  C    . GLU   A 1 95  ? 79.048  77.163  23.018  1   38.09 ? 117 GLU   A C    1 
ATOM   749  O  O    . GLU   A 1 95  ? 77.947  77.686  22.863  1   38.31 ? 117 GLU   A O    1 
ATOM   750  C  CB   . GLU   A 1 95  ? 78.572  74.72   22.659  1   39.12 ? 117 GLU   A CB   1 
ATOM   751  C  CG   . GLU   A 1 95  ? 78.601  73.577  21.662  1   43.13 ? 117 GLU   A CG   1 
ATOM   752  C  CD   . GLU   A 1 95  ? 77.772  72.383  22.077  1   46.95 ? 117 GLU   A CD   1 
ATOM   753  O  OE1  . GLU   A 1 95  ? 77.791  72.019  23.274  1   48.63 ? 117 GLU   A OE1  1 
ATOM   754  O  OE2  . GLU   A 1 95  ? 77.107  71.8    21.197  1   48.73 ? 117 GLU   A OE2  1 
ATOM   755  N  N    . THR   A 1 96  ? 79.951  77.629  23.877  1   38.01 ? 118 THR   A N    1 
ATOM   756  C  CA   . THR   A 1 96  ? 79.8    78.833  24.68   1   38.85 ? 118 THR   A CA   1 
ATOM   757  C  C    . THR   A 1 96  ? 79.893  80.109  23.764  1   39.68 ? 118 THR   A C    1 
ATOM   758  O  O    . THR   A 1 96  ? 79.495  81.186  24.183  1   40.64 ? 118 THR   A O    1 
ATOM   759  C  CB   . THR   A 1 96  ? 80.837  78.699  25.796  1   40.53 ? 118 THR   A CB   1 
ATOM   760  O  OG1  . THR   A 1 96  ? 80.266  78.916  27.066  1   43.59 ? 118 THR   A OG1  1 
ATOM   761  C  CG2  . THR   A 1 96  ? 82.024  79.512  25.595  1   39.86 ? 118 THR   A CG2  1 
ATOM   762  N  N    . MET   A 1 97  ? 80.405  79.965  22.518  1   39.34 ? 119 MET   A N    1 
ATOM   763  C  CA   . MET   A 1 97  ? 80.459  81.007  21.505  1   39.53 ? 119 MET   A CA   1 
ATOM   764  C  C    . MET   A 1 97  ? 79.067  81.073  20.865  1   39.91 ? 119 MET   A C    1 
ATOM   765  O  O    . MET   A 1 97  ? 78.543  80.05   20.445  1   39.61 ? 119 MET   A O    1 
ATOM   766  C  CB   . MET   A 1 97  ? 81.504  80.668  20.431  1   39.57 ? 119 MET   A CB   1 
ATOM   767  C  CG   . MET   A 1 97  ? 81.407  81.542  19.18   1   40.94 ? 119 MET   A CG   1 
ATOM   768  S  SD   . MET   A 1 97  ? 82.75   81.284  18.007  1   44.28 ? 119 MET   A SD   1 
ATOM   769  C  CE   . MET   A 1 97  ? 82.456  79.575  17.486  1   39.72 ? 119 MET   A CE   1 
ATOM   770  N  N    . THR   A 1 98  ? 78.481  82.26   20.796  1   40.35 ? 120 THR   A N    1 
ATOM   771  C  CA   . THR   A 1 98  ? 77.157  82.426  20.212  1   41.18 ? 120 THR   A CA   1 
ATOM   772  C  C    . THR   A 1 98  ? 77.197  82.366  18.678  1   42.16 ? 120 THR   A C    1 
ATOM   773  O  O    . THR   A 1 98  ? 78.171  82.808  18.053  1   42.59 ? 120 THR   A O    1 
ATOM   774  C  CB   . THR   A 1 98  ? 76.548  83.754  20.663  1   41.72 ? 120 THR   A CB   1 
ATOM   775  O  OG1  . THR   A 1 98  ? 77.36   84.791  20.144  1   42.77 ? 120 THR   A OG1  1 
ATOM   776  C  CG2  . THR   A 1 98  ? 76.417  83.867  22.176  1   41.87 ? 120 THR   A CG2  1 
ATOM   777  N  N    . PRO   A 1 99  ? 76.104  81.892  18.062  1   42.42 ? 121 PRO   A N    1 
ATOM   778  C  CA   . PRO   A 1 99  ? 76.044  81.877  16.59   1   43.22 ? 121 PRO   A CA   1 
ATOM   779  C  C    . PRO   A 1 99  ? 76.306  83.248  15.94   1   44.63 ? 121 PRO   A C    1 
ATOM   780  O  O    . PRO   A 1 99  ? 76.968  83.299  14.899  1   45.15 ? 121 PRO   A O    1 
ATOM   781  C  CB   . PRO   A 1 99  ? 74.625  81.376  16.29   1   43.5  ? 121 PRO   A CB   1 
ATOM   782  C  CG   . PRO   A 1 99  ? 74.181  80.66   17.519  1   43.79 ? 121 PRO   A CG   1 
ATOM   783  C  CD   . PRO   A 1 99  ? 74.875  81.336  18.672  1   42.18 ? 121 PRO   A CD   1 
ATOM   784  N  N    . LEU   A 1 100 ? 75.83   84.356  16.558  1   45.1  ? 122 LEU   A N    1 
ATOM   785  C  CA   . LEU   A 1 100 ? 76.045  85.7    16.007  1   46.07 ? 122 LEU   A CA   1 
ATOM   786  C  C    . LEU   A 1 100 ? 77.494  86.145  16.049  1   46.74 ? 122 LEU   A C    1 
ATOM   787  O  O    . LEU   A 1 100 ? 77.923  86.863  15.146  1   47.23 ? 122 LEU   A O    1 
ATOM   788  C  CB   . LEU   A 1 100 ? 75.149  86.736  16.682  1   46.55 ? 122 LEU   A CB   1 
ATOM   789  C  CG   . LEU   A 1 100 ? 73.704  86.717  16.206  1   48.31 ? 122 LEU   A CG   1 
ATOM   790  C  CD1  . LEU   A 1 100 ? 72.797  87.494  17.156  1   48.71 ? 122 LEU   A CD1  1 
ATOM   791  C  CD2  . LEU   A 1 100 ? 73.599  87.184  14.754  1   48.79 ? 122 LEU   A CD2  1 
ATOM   792  N  N    . ASP   A 1 101 ? 78.262  85.719  17.071  1   46.38 ? 123 ASP   A N    1 
ATOM   793  C  CA   . ASP   A 1 101 ? 79.684  86.07   17.145  1   46.34 ? 123 ASP   A CA   1 
ATOM   794  C  C    . ASP   A 1 101 ? 80.467  85.268  16.125  1   45.22 ? 123 ASP   A C    1 
ATOM   795  O  O    . ASP   A 1 101 ? 81.358  85.809  15.485  1   44.87 ? 123 ASP   A O    1 
ATOM   796  C  CB   . ASP   A 1 101 ? 80.253  85.859  18.565  1   49.47 ? 123 ASP   A CB   1 
ATOM   797  C  CG   . ASP   A 1 101 ? 79.898  86.95   19.561  1   55.45 ? 123 ASP   A CG   1 
ATOM   798  O  OD1  . ASP   A 1 101 ? 79.365  87.995  19.133  1   55.98 ? 123 ASP   A OD1  1 
ATOM   799  O  OD2  . ASP   A 1 101 ? 80.164  86.761  20.767  1   58.75 ? 123 ASP   A OD2  1 
ATOM   800  N  N    . PHE   A 1 102 ? 80.13   83.978  15.952  1   45.1  ? 124 PHE   A N    1 
ATOM   801  C  CA   . PHE   A 1 102 ? 80.77   83.124  14.947  1   44.9  ? 124 PHE   A CA   1 
ATOM   802  C  C    . PHE   A 1 102 ? 80.494  83.682  13.548  1   46.82 ? 124 PHE   A C    1 
ATOM   803  O  O    . PHE   A 1 102 ? 81.386  83.656  12.697  1   47.1  ? 124 PHE   A O    1 
ATOM   804  C  CB   . PHE   A 1 102 ? 80.286  81.663  15.05   1   43.18 ? 124 PHE   A CB   1 
ATOM   805  C  CG   . PHE   A 1 102 ? 80.95   80.75   14.043  1   42.28 ? 124 PHE   A CG   1 
ATOM   806  C  CD1  . PHE   A 1 102 ? 82.326  80.626  13.995  1   42.36 ? 124 PHE   A CD1  1 
ATOM   807  C  CD2  . PHE   A 1 102 ? 80.195  80      13.161  1   42.44 ? 124 PHE   A CD2  1 
ATOM   808  C  CE1  . PHE   A 1 102 ? 82.929  79.777  13.086  1   42.78 ? 124 PHE   A CE1  1 
ATOM   809  C  CE2  . PHE   A 1 102 ? 80.804  79.157  12.244  1   42.56 ? 124 PHE   A CE2  1 
ATOM   810  C  CZ   . PHE   A 1 102 ? 82.163  79.054  12.21   1   42.49 ? 124 PHE   A CZ   1 
ATOM   811  N  N    . MET   A 1 103 ? 79.286  84.241  13.322  1   48.03 ? 125 MET   A N    1 
ATOM   812  C  CA   . MET   A 1 103 ? 78.917  84.865  12.042  1   49.62 ? 125 MET   A CA   1 
ATOM   813  C  C    . MET   A 1 103 ? 79.833  86.059  11.699  1   49.93 ? 125 MET   A C    1 
ATOM   814  O  O    . MET   A 1 103 ? 80.144  86.28   10.528  1   50.45 ? 125 MET   A O    1 
ATOM   815  C  CB   . MET   A 1 103 ? 77.446  85.323  12.076  1   51.3  ? 125 MET   A CB   1 
ATOM   816  C  CG   . MET   A 1 103 ? 76.787  85.355  10.701  1   54.54 ? 125 MET   A CG   1 
ATOM   817  S  SD   . MET   A 1 103 ? 75.006  85.588  10.836  1   60.18 ? 125 MET   A SD   1 
ATOM   818  C  CE   . MET   A 1 103 ? 74.411  83.97   10.508  1   54.95 ? 125 MET   A CE   1 
ATOM   819  N  N    . ASP   A 1 104 ? 80.308  86.794  12.717  1   49.62 ? 126 ASP   A N    1 
ATOM   820  C  CA   . ASP   A 1 104 ? 81.181  87.948  12.494  1   49.73 ? 126 ASP   A CA   1 
ATOM   821  C  C    . ASP   A 1 104 ? 82.613  87.598  12.098  1   49.64 ? 126 ASP   A C    1 
ATOM   822  O  O    . ASP   A 1 104 ? 83.34   88.506  11.697  1   50.2  ? 126 ASP   A O    1 
ATOM   823  C  CB   . ASP   A 1 104 ? 81.172  88.91   13.69   1   51.6  ? 126 ASP   A CB   1 
ATOM   824  C  CG   . ASP   A 1 104 ? 79.873  89.686  13.871  1   56.88 ? 126 ASP   A CG   1 
ATOM   825  O  OD1  . ASP   A 1 104 ? 79.018  89.645  12.954  1   57.58 ? 126 ASP   A OD1  1 
ATOM   826  O  OD2  . ASP   A 1 104 ? 79.706  90.328  14.935  1   59.68 ? 126 ASP   A OD2  1 
ATOM   827  N  N    . PHE   A 1 105 ? 83.031  86.314  12.171  1   49.05 ? 127 PHE   A N    1 
ATOM   828  C  CA   . PHE   A 1 105 ? 84.379  85.959  11.717  1   49.32 ? 127 PHE   A CA   1 
ATOM   829  C  C    . PHE   A 1 105 ? 84.41   84.745  10.78   1   49.91 ? 127 PHE   A C    1 
ATOM   830  O  O    . PHE   A 1 105 ? 85.455  84.478  10.191  1   49.47 ? 127 PHE   A O    1 
ATOM   831  C  CB   . PHE   A 1 105 ? 85.384  85.794  12.881  1   49.13 ? 127 PHE   A CB   1 
ATOM   832  C  CG   . PHE   A 1 105 ? 85.258  84.549  13.732  1   49.69 ? 127 PHE   A CG   1 
ATOM   833  C  CD1  . PHE   A 1 105 ? 84.544  84.571  14.915  1   50.47 ? 127 PHE   A CD1  1 
ATOM   834  C  CD2  . PHE   A 1 105 ? 85.919  83.377  13.385  1   50.38 ? 127 PHE   A CD2  1 
ATOM   835  C  CE1  . PHE   A 1 105 ? 84.457  83.434  15.713  1   51.08 ? 127 PHE   A CE1  1 
ATOM   836  C  CE2  . PHE   A 1 105 ? 85.826  82.242  14.182  1   50.71 ? 127 PHE   A CE2  1 
ATOM   837  C  CZ   . PHE   A 1 105 ? 85.102  82.282  15.342  1   50.59 ? 127 PHE   A CZ   1 
ATOM   838  N  N    . ARG   A 1 106 ? 83.295  84.008  10.635  1   51.01 ? 128 ARG   A N    1 
ATOM   839  C  CA   . ARG   A 1 106 ? 83.278  82.812  9.787   1   53.16 ? 128 ARG   A CA   1 
ATOM   840  C  C    . ARG   A 1 106 ? 83.622  83.098  8.33    1   54.71 ? 128 ARG   A C    1 
ATOM   841  O  O    . ARG   A 1 106 ? 84.181  82.227  7.665   1   54.95 ? 128 ARG   A O    1 
ATOM   842  C  CB   . ARG   A 1 106 ? 81.965  82.027  9.905   1   55.3  ? 128 ARG   A CB   1 
ATOM   843  C  CG   . ARG   A 1 106 ? 80.767  82.827  9.452   1   60.39 ? 128 ARG   A CG   1 
ATOM   844  C  CD   . ARG   A 1 106 ? 79.45   82.224  9.904   1   64.88 ? 128 ARG   A CD   1 
ATOM   845  N  NE   . ARG   A 1 106 ? 78.42   82.462  8.891   1   68.67 ? 128 ARG   A NE   1 
ATOM   846  C  CZ   . ARG   A 1 106 ? 77.144  82.108  9.009   1   70.89 ? 128 ARG   A CZ   1 
ATOM   847  N  NH1  . ARG   A 1 106 ? 76.715  81.504  10.111  1   70.54 ? 128 ARG   A NH1  1 
ATOM   848  N  NH2  . ARG   A 1 106 ? 76.288  82.346  8.022   1   70.46 ? 128 ARG   A NH2  1 
ATOM   849  N  N    . LYS   A 1 107 ? 83.363  84.331  7.852   1   55.59 ? 129 LYS   A N    1 
ATOM   850  C  CA   . LYS   A 1 107 ? 83.693  84.748  6.486   1   56.48 ? 129 LYS   A CA   1 
ATOM   851  C  C    . LYS   A 1 107 ? 85.204  84.718  6.205   1   57.09 ? 129 LYS   A C    1 
ATOM   852  O  O    . LYS   A 1 107 ? 85.588  84.515  5.055   1   57.42 ? 129 LYS   A O    1 
ATOM   853  C  CB   . LYS   A 1 107 ? 83.104  86.139  6.173   1   58.29 ? 129 LYS   A CB   1 
ATOM   854  N  N    . TYR   A 1 108 ? 86.059  84.912  7.239   1   57.19 ? 130 TYR   A N    1 
ATOM   855  C  CA   . TYR   A 1 108 ? 87.524  84.856  7.07    1   57.7  ? 130 TYR   A CA   1 
ATOM   856  C  C    . TYR   A 1 108 ? 88.041  83.421  6.957   1   57.65 ? 130 TYR   A C    1 
ATOM   857  O  O    . TYR   A 1 108 ? 89.182  83.222  6.541   1   57.13 ? 130 TYR   A O    1 
ATOM   858  C  CB   . TYR   A 1 108 ? 88.267  85.537  8.231   1   58.22 ? 130 TYR   A CB   1 
ATOM   859  C  CG   . TYR   A 1 108 ? 87.868  86.972  8.482   1   59.74 ? 130 TYR   A CG   1 
ATOM   860  C  CD1  . TYR   A 1 108 ? 88.376  88.005  7.705   1   60.94 ? 130 TYR   A CD1  1 
ATOM   861  C  CD2  . TYR   A 1 108 ? 87.019  87.304  9.527   1   61.06 ? 130 TYR   A CD2  1 
ATOM   862  C  CE1  . TYR   A 1 108 ? 88.012  89.332  7.936   1   61.82 ? 130 TYR   A CE1  1 
ATOM   863  C  CE2  . TYR   A 1 108 ? 86.637  88.619  9.76    1   62.26 ? 130 TYR   A CE2  1 
ATOM   864  C  CZ   . TYR   A 1 108 ? 87.142  89.635  8.969   1   63    ? 130 TYR   A CZ   1 
ATOM   865  O  OH   . TYR   A 1 108 ? 86.753  90.933  9.229   1   64.58 ? 130 TYR   A OH   1 
ATOM   866  N  N    . LEU   A 1 109 ? 87.247  82.43   7.411   1   58.22 ? 131 LEU   A N    1 
ATOM   867  C  CA   . LEU   A 1 109 ? 87.63   81.016  7.363   1   59.33 ? 131 LEU   A CA   1 
ATOM   868  C  C    . LEU   A 1 109 ? 87.782  80.592  5.912   1   60.65 ? 131 LEU   A C    1 
ATOM   869  O  O    . LEU   A 1 109 ? 88.771  79.954  5.573   1   60.84 ? 131 LEU   A O    1 
ATOM   870  C  CB   . LEU   A 1 109 ? 86.622  80.121  8.119   1   59.19 ? 131 LEU   A CB   1 
ATOM   871  C  CG   . LEU   A 1 109 ? 86.577  80.303  9.643   1   60.14 ? 131 LEU   A CG   1 
ATOM   872  C  CD1  . LEU   A 1 109 ? 85.45   79.528  10.279  1   60.68 ? 131 LEU   A CD1  1 
ATOM   873  C  CD2  . LEU   A 1 109 ? 87.917  80.113  10.288  1   60.6  ? 131 LEU   A CD2  1 
ATOM   874  N  N    . ALA   A 1 110 ? 86.822  81.031  5.063   1   61.2  ? 132 ALA   A N    1 
ATOM   875  C  CA   . ALA   A 1 110 ? 86.708  80.926  3.614   1   61.97 ? 132 ALA   A CA   1 
ATOM   876  C  C    . ALA   A 1 110 ? 87.302  79.644  3.005   1   62.06 ? 132 ALA   A C    1 
ATOM   877  O  O    . ALA   A 1 110 ? 86.529  78.687  2.875   1   63.07 ? 132 ALA   A O    1 
ATOM   878  C  CB   . ALA   A 1 110 ? 87.276  82.177  2.953   1   62.38 ? 132 ALA   A CB   1 
ATOM   879  N  N    . PRO   A 1 111 ? 88.604  79.547  2.613   1   60.73 ? 133 PRO   A N    1 
ATOM   880  C  CA   . PRO   A 1 111 ? 89.078  78.269  2.035   1   60.11 ? 133 PRO   A CA   1 
ATOM   881  C  C    . PRO   A 1 111 ? 89.295  77.142  3.062   1   59.23 ? 133 PRO   A C    1 
ATOM   882  O  O    . PRO   A 1 111 ? 89.392  75.981  2.668   1   59.37 ? 133 PRO   A O    1 
ATOM   883  C  CB   . PRO   A 1 111 ? 90.357  78.646  1.279   1   60.63 ? 133 PRO   A CB   1 
ATOM   884  C  CG   . PRO   A 1 111 ? 90.748  79.992  1.786   1   61.14 ? 133 PRO   A CG   1 
ATOM   885  C  CD   . PRO   A 1 111 ? 89.688  80.549  2.681   1   59.6  ? 133 PRO   A CD   1 
ATOM   886  N  N    . ALA   A 1 112 ? 89.363  77.475  4.364   1   58.17 ? 134 ALA   A N    1 
ATOM   887  C  CA   . ALA   A 1 112 ? 89.548  76.472  5.416   1   57.68 ? 134 ALA   A CA   1 
ATOM   888  C  C    . ALA   A 1 112 ? 88.327  75.58   5.56    1   56.93 ? 134 ALA   A C    1 
ATOM   889  O  O    . ALA   A 1 112 ? 87.192  76.044  5.461   1   57.02 ? 134 ALA   A O    1 
ATOM   890  C  CB   . ALA   A 1 112 ? 89.853  77.135  6.75    1   57.67 ? 134 ALA   A CB   1 
ATOM   891  N  N    . SER   A 1 113 ? 88.564  74.297  5.791   1   56.12 ? 135 SER   A N    1 
ATOM   892  C  CA   . SER   A 1 113 ? 87.497  73.329  5.976   1   55.88 ? 135 SER   A CA   1 
ATOM   893  C  C    . SER   A 1 113 ? 87.922  72.272  6.987   1   55.03 ? 135 SER   A C    1 
ATOM   894  O  O    . SER   A 1 113 ? 89.098  71.908  7.037   1   54.69 ? 135 SER   A O    1 
ATOM   895  C  CB   . SER   A 1 113 ? 87.151  72.656  4.652   1   57.25 ? 135 SER   A CB   1 
ATOM   896  O  OG   . SER   A 1 113 ? 86.217  71.601  4.821   1   59.52 ? 135 SER   A OG   1 
ATOM   897  N  N    . GLY   A 1 114 ? 86.954  71.744  7.735   1   54.5  ? 136 GLY   A N    1 
ATOM   898  C  CA   . GLY   A 1 114 ? 87.195  70.648  8.667   1   54.82 ? 136 GLY   A CA   1 
ATOM   899  C  C    . GLY   A 1 114 ? 87.726  69.409  7.964   1   54.67 ? 136 GLY   A C    1 
ATOM   900  O  O    . GLY   A 1 114 ? 88.45   68.61   8.566   1   54.98 ? 136 GLY   A O    1 
ATOM   901  N  N    . PHE   A 1 115 ? 87.399  69.268  6.654   1   53.76 ? 137 PHE   A N    1 
ATOM   902  C  CA   . PHE   A 1 115 ? 87.87   68.203  5.766   1   53.42 ? 137 PHE   A CA   1 
ATOM   903  C  C    . PHE   A 1 115 ? 89.401  68.265  5.586   1   51.51 ? 137 PHE   A C    1 
ATOM   904  O  O    . PHE   A 1 115 ? 90.008  67.246  5.273   1   51.6  ? 137 PHE   A O    1 
ATOM   905  C  CB   . PHE   A 1 115 ? 87.19   68.32   4.383   1   54.53 ? 137 PHE   A CB   1 
ATOM   906  C  CG   . PHE   A 1 115 ? 85.688  68.11   4.366   1   56.49 ? 137 PHE   A CG   1 
ATOM   907  C  CD1  . PHE   A 1 115 ? 85.066  67.337  5.337   1   57.63 ? 137 PHE   A CD1  1 
ATOM   908  C  CD2  . PHE   A 1 115 ? 84.91   68.624  3.34    1   57.77 ? 137 PHE   A CD2  1 
ATOM   909  C  CE1  . PHE   A 1 115 ? 83.692  67.122  5.305   1   58.59 ? 137 PHE   A CE1  1 
ATOM   910  C  CE2  . PHE   A 1 115 ? 83.536  68.397  3.305   1   58.57 ? 137 PHE   A CE2  1 
ATOM   911  C  CZ   . PHE   A 1 115 ? 82.937  67.64   4.284   1   58.51 ? 137 PHE   A CZ   1 
ATOM   912  N  N    . GLN   A 1 116 ? 90.023  69.458  5.772   1   49.9  ? 138 GLN   A N    1 
ATOM   913  C  CA   . GLN   A 1 116 ? 91.472  69.666  5.643   1   48.49 ? 138 GLN   A CA   1 
ATOM   914  C  C    . GLN   A 1 116 ? 92.288  69.291  6.896   1   45.92 ? 138 GLN   A C    1 
ATOM   915  O  O    . GLN   A 1 116 ? 93.485  69.598  6.945   1   45.89 ? 138 GLN   A O    1 
ATOM   916  C  CB   . GLN   A 1 116 ? 91.796  71.106  5.208   1   50.1  ? 138 GLN   A CB   1 
ATOM   917  C  CG   . GLN   A 1 116 ? 91.241  71.469  3.844   1   54.67 ? 138 GLN   A CG   1 
ATOM   918  C  CD   . GLN   A 1 116 ? 91.178  72.96   3.615   1   60.55 ? 138 GLN   A CD   1 
ATOM   919  O  OE1  . GLN   A 1 116 ? 91.232  73.774  4.551   1   62.22 ? 138 GLN   A OE1  1 
ATOM   920  N  NE2  . GLN   A 1 116 ? 91.032  73.358  2.361   1   60.93 ? 138 GLN   A NE2  1 
ATOM   921  N  N    . SER   A 1 117 ? 91.664  68.631  7.902   1   43.51 ? 139 SER   A N    1 
ATOM   922  C  CA   . SER   A 1 117 ? 92.434  68.161  9.063   1   40.92 ? 139 SER   A CA   1 
ATOM   923  C  C    . SER   A 1 117 ? 93.068  66.841  8.662   1   38.91 ? 139 SER   A C    1 
ATOM   924  O  O    . SER   A 1 117 ? 92.389  65.811  8.658   1   39.16 ? 139 SER   A O    1 
ATOM   925  C  CB   . SER   A 1 117 ? 91.555  67.946  10.292  1   40.1  ? 139 SER   A CB   1 
ATOM   926  O  OG   . SER   A 1 117 ? 92.272  67.268  11.312  1   39.37 ? 139 SER   A OG   1 
ATOM   927  N  N    . LEU   A 1 118 ? 94.355  66.871  8.318   1   36.65 ? 140 LEU   A N    1 
ATOM   928  C  CA   . LEU   A 1 118 ? 95.09   65.682  7.942   1   36.36 ? 140 LEU   A CA   1 
ATOM   929  C  C    . LEU   A 1 118 ? 95.123  64.674  9.098   1   36.36 ? 140 LEU   A C    1 
ATOM   930  O  O    . LEU   A 1 118 ? 94.91   63.472  8.887   1   37.43 ? 140 LEU   A O    1 
ATOM   931  C  CB   . LEU   A 1 118 ? 96.517  66.097  7.514   1   36.7  ? 140 LEU   A CB   1 
ATOM   932  C  CG   . LEU   A 1 118 ? 97.569  64.994  7.363   1   38.57 ? 140 LEU   A CG   1 
ATOM   933  C  CD1  . LEU   A 1 118 ? 97.195  64.02   6.241   1   38.98 ? 140 LEU   A CD1  1 
ATOM   934  C  CD2  . LEU   A 1 118 ? 98.958  65.597  7.112   1   38.97 ? 140 LEU   A CD2  1 
ATOM   935  N  N    . GLN   A 1 119 ? 95.354  65.166  10.322  1   34.94 ? 141 GLN   A N    1 
ATOM   936  C  CA   . GLN   A 1 119 ? 95.444  64.304  11.491  1   34.24 ? 141 GLN   A CA   1 
ATOM   937  C  C    . GLN   A 1 119 ? 94.151  63.567  11.792  1   33.94 ? 141 GLN   A C    1 
ATOM   938  O  O    . GLN   A 1 119 ? 94.223  62.401  12.151  1   34.02 ? 141 GLN   A O    1 
ATOM   939  C  CB   . GLN   A 1 119 ? 95.957  65.081  12.715  1   34.04 ? 141 GLN   A CB   1 
ATOM   940  C  CG   . GLN   A 1 119 ? 97.422  65.49   12.566  1   33.01 ? 141 GLN   A CG   1 
ATOM   941  C  CD   . GLN   A 1 119 ? 98.032  65.861  13.891  1   32.04 ? 141 GLN   A CD   1 
ATOM   942  O  OE1  . GLN   A 1 119 ? 98.995  65.23   14.328  1   32.61 ? 141 GLN   A OE1  1 
ATOM   943  N  NE2  . GLN   A 1 119 ? 97.483  66.88   14.557  1   30.01 ? 141 GLN   A NE2  1 
ATOM   944  N  N    . PHE   A 1 120 ? 92.982  64.192  11.583  1   34.24 ? 142 PHE   A N    1 
ATOM   945  C  CA   . PHE   A 1 120 ? 91.712  63.483  11.801  1   35.55 ? 142 PHE   A CA   1 
ATOM   946  C  C    . PHE   A 1 120 ? 91.561  62.304  10.807  1   36.08 ? 142 PHE   A C    1 
ATOM   947  O  O    . PHE   A 1 120 ? 91.171  61.201  11.213  1   36.44 ? 142 PHE   A O    1 
ATOM   948  C  CB   . PHE   A 1 120 ? 90.505  64.43   11.761  1   36.03 ? 142 PHE   A CB   1 
ATOM   949  C  CG   . PHE   A 1 120 ? 89.2    63.745  12.088  1   37.26 ? 142 PHE   A CG   1 
ATOM   950  C  CD1  . PHE   A 1 120 ? 88.845  63.486  13.401  1   38.25 ? 142 PHE   A CD1  1 
ATOM   951  C  CD2  . PHE   A 1 120 ? 88.325  63.361  11.079  1   37.9  ? 142 PHE   A CD2  1 
ATOM   952  C  CE1  . PHE   A 1 120 ? 87.649  62.843  13.699  1   38.91 ? 142 PHE   A CE1  1 
ATOM   953  C  CE2  . PHE   A 1 120 ? 87.121  62.739  11.384  1   38.4  ? 142 PHE   A CE2  1 
ATOM   954  C  CZ   . PHE   A 1 120 ? 86.799  62.466  12.689  1   38.34 ? 142 PHE   A CZ   1 
ATOM   955  N  N    . ARG   A 1 121 ? 91.937  62.517  9.53    1   35.48 ? 143 ARG   A N    1 
ATOM   956  C  CA   . ARG   A 1 121 ? 91.888  61.453  8.53    1   35.17 ? 143 ARG   A CA   1 
ATOM   957  C  C    . ARG   A 1 121 ? 92.849  60.343  8.893   1   35.05 ? 143 ARG   A C    1 
ATOM   958  O  O    . ARG   A 1 121 ? 92.483  59.17   8.811   1   35.55 ? 143 ARG   A O    1 
ATOM   959  C  CB   . ARG   A 1 121 ? 92.209  62.001  7.12    1   36.08 ? 143 ARG   A CB   1 
ATOM   960  C  CG   . ARG   A 1 121 ? 91.214  63.042  6.608   1   38.64 ? 143 ARG   A CG   1 
ATOM   961  C  CD   . ARG   A 1 121 ? 89.783  62.525  6.649   1   40.41 ? 143 ARG   A CD   1 
ATOM   962  N  NE   . ARG   A 1 121 ? 88.817  63.505  6.149   1   41.5  ? 143 ARG   A NE   1 
ATOM   963  C  CZ   . ARG   A 1 121 ? 87.542  63.551  6.517   1   42.33 ? 143 ARG   A CZ   1 
ATOM   964  N  NH1  . ARG   A 1 121 ? 87.072  62.698  7.417   1   40.63 ? 143 ARG   A NH1  1 
ATOM   965  N  NH2  . ARG   A 1 121 ? 86.734  64.471  6.011   1   43.64 ? 143 ARG   A NH2  1 
ATOM   966  N  N    . LEU   A 1 122 ? 94.082  60.705  9.317   1   34.24 ? 144 LEU   A N    1 
ATOM   967  C  CA   . LEU   A 1 122 ? 95.092  59.73   9.731   1   33.25 ? 144 LEU   A CA   1 
ATOM   968  C  C    . LEU   A 1 122 ? 94.589  58.865  10.885  1   32.12 ? 144 LEU   A C    1 
ATOM   969  O  O    . LEU   A 1 122 ? 94.815  57.661  10.861  1   33.31 ? 144 LEU   A O    1 
ATOM   970  C  CB   . LEU   A 1 122 ? 96.41   60.429  10.109  1   33.63 ? 144 LEU   A CB   1 
ATOM   971  C  CG   . LEU   A 1 122 ? 97.169  61.097  8.96    1   35.28 ? 144 LEU   A CG   1 
ATOM   972  C  CD1  . LEU   A 1 122 ? 98.411  61.846  9.477   1   35.56 ? 144 LEU   A CD1  1 
ATOM   973  C  CD2  . LEU   A 1 122 ? 97.597  60.064  7.92    1   35.46 ? 144 LEU   A CD2  1 
ATOM   974  N  N    . ILE   A 1 123 ? 93.886  59.447  11.874  1   30.19 ? 145 ILE   A N    1 
ATOM   975  C  CA   . ILE   A 1 123 ? 93.31   58.68   12.988  1   29.1  ? 145 ILE   A CA   1 
ATOM   976  C  C    . ILE   A 1 123 ? 92.249  57.69   12.461  1   29.13 ? 145 ILE   A C    1 
ATOM   977  O  O    . ILE   A 1 123 ? 92.274  56.515  12.822  1   29.3  ? 145 ILE   A O    1 
ATOM   978  C  CB   . ILE   A 1 123 ? 92.725  59.63   14.06   1   28.6  ? 145 ILE   A CB   1 
ATOM   979  C  CG1  . ILE   A 1 123 ? 93.848  60.4    14.79   1   28.55 ? 145 ILE   A CG1  1 
ATOM   980  C  CG2  . ILE   A 1 123 ? 91.797  58.894  15.057  1   28.72 ? 145 ILE   A CG2  1 
ATOM   981  C  CD1  . ILE   A 1 123 ? 93.343  61.507  15.692  1   28.53 ? 145 ILE   A CD1  1 
ATOM   982  N  N    . GLU   A 1 124 ? 91.326  58.163  11.604  1   28.96 ? 146 GLU   A N    1 
ATOM   983  C  CA   . GLU   A 1 124 ? 90.294  57.3    11.003  1   29.78 ? 146 GLU   A CA   1 
ATOM   984  C  C    . GLU   A 1 124 ? 90.912  56.111  10.238  1   30.63 ? 146 GLU   A C    1 
ATOM   985  O  O    . GLU   A 1 124 ? 90.496  54.967  10.424  1   30.82 ? 146 GLU   A O    1 
ATOM   986  C  CB   . GLU   A 1 124 ? 89.423  58.103  10.024  1   30.38 ? 146 GLU   A CB   1 
ATOM   987  C  CG   . GLU   A 1 124 ? 88.454  59.066  10.673  1   32.32 ? 146 GLU   A CG   1 
ATOM   988  C  CD   . GLU   A 1 124 ? 87.608  59.796  9.648   1   36.35 ? 146 GLU   A CD   1 
ATOM   989  O  OE1  . GLU   A 1 124 ? 88.19   60.395  8.716   1   38.15 ? 146 GLU   A OE1  1 
ATOM   990  O  OE2  . GLU   A 1 124 ? 86.364  59.779  9.775   1   38.07 ? 146 GLU   A OE2  1 
ATOM   991  N  N    . ASN   A 1 125 ? 91.905  56.386  9.387   1   30.76 ? 147 ASN   A N    1 
ATOM   992  C  CA   . ASN   A 1 125 ? 92.536  55.342  8.587   1   31.41 ? 147 ASN   A CA   1 
ATOM   993  C  C    . ASN   A 1 125 ? 93.368  54.411  9.421   1   32.53 ? 147 ASN   A C    1 
ATOM   994  O  O    . ASN   A 1 125 ? 93.26   53.203  9.243   1   33.69 ? 147 ASN   A O    1 
ATOM   995  C  CB   . ASN   A 1 125 ? 93.347  55.94   7.444   1   31.55 ? 147 ASN   A CB   1 
ATOM   996  C  CG   . ASN   A 1 125 ? 92.509  56.711  6.447   1   34.54 ? 147 ASN   A CG   1 
ATOM   997  O  OD1  . ASN   A 1 125 ? 91.264  56.67   6.475   1   36.28 ? 147 ASN   A OD1  1 
ATOM   998  N  ND2  . ASN   A 1 125 ? 93.174  57.456  5.558   1   33.98 ? 147 ASN   A ND2  1 
ATOM   999  N  N    . LYS   A 1 126 ? 94.16   54.945  10.372  1   31.88 ? 148 LYS   A N    1 
ATOM   1000 C  CA   . LYS   A 1 126 ? 94.965  54.092  11.239  1   31.58 ? 148 LYS   A CA   1 
ATOM   1001 C  C    . LYS   A 1 126 ? 94.101  53.205  12.126  1   31.78 ? 148 LYS   A C    1 
ATOM   1002 O  O    . LYS   A 1 126 ? 94.511  52.09   12.437  1   32.18 ? 148 LYS   A O    1 
ATOM   1003 C  CB   . LYS   A 1 126 ? 95.989  54.916  12.043  1   32.14 ? 148 LYS   A CB   1 
ATOM   1004 C  CG   . LYS   A 1 126 ? 97.074  55.529  11.132  1   32.4  ? 148 LYS   A CG   1 
ATOM   1005 C  CD   . LYS   A 1 126 ? 97.849  56.642  11.81   1   32.33 ? 148 LYS   A CD   1 
ATOM   1006 C  CE   . LYS   A 1 126 ? 98.961  57.194  10.944  1   32.81 ? 148 LYS   A CE   1 
ATOM   1007 N  NZ   . LYS   A 1 126 ? 100.01  56.154  10.727  1   33.83 ? 148 LYS   A NZ   1 
ATOM   1008 N  N    . LEU   A 1 127 ? 92.904  53.672  12.521  1   31.64 ? 149 LEU   A N    1 
ATOM   1009 C  CA   . LEU   A 1 127 ? 91.989  52.834  13.306  1   32.04 ? 149 LEU   A CA   1 
ATOM   1010 C  C    . LEU   A 1 127 ? 91.408  51.755  12.372  1   32.96 ? 149 LEU   A C    1 
ATOM   1011 O  O    . LEU   A 1 127 ? 91.407  50.571  12.719  1   32.7  ? 149 LEU   A O    1 
ATOM   1012 C  CB   . LEU   A 1 127 ? 90.868  53.666  13.948  1   31.79 ? 149 LEU   A CB   1 
ATOM   1013 C  CG   . LEU   A 1 127 ? 89.873  52.871  14.809  1   32.58 ? 149 LEU   A CG   1 
ATOM   1014 C  CD1  . LEU   A 1 127 ? 90.55   52.273  16.02   1   32.3  ? 149 LEU   A CD1  1 
ATOM   1015 C  CD2  . LEU   A 1 127 ? 88.691  53.735  15.218  1   33.18 ? 149 LEU   A CD2  1 
ATOM   1016 N  N    . GLY   A 1 128 ? 91.004  52.156  11.173  1   34.41 ? 150 GLY   A N    1 
ATOM   1017 C  CA   . GLY   A 1 128 ? 90.536  51.2    10.183  1   37.05 ? 150 GLY   A CA   1 
ATOM   1018 C  C    . GLY   A 1 128 ? 89.32   51.556  9.365   1   40.08 ? 150 GLY   A C    1 
ATOM   1019 O  O    . GLY   A 1 128 ? 88.686  50.655  8.826   1   40.65 ? 150 GLY   A O    1 
ATOM   1020 N  N    . VAL   A 1 129 ? 88.993  52.847  9.224   1   42.32 ? 151 VAL   A N    1 
ATOM   1021 C  CA   . VAL   A 1 129 ? 87.857  53.254  8.396   1   44.96 ? 151 VAL   A CA   1 
ATOM   1022 C  C    . VAL   A 1 129 ? 88.175  52.94   6.929   1   48.74 ? 151 VAL   A C    1 
ATOM   1023 O  O    . VAL   A 1 129 ? 89.166  53.442  6.387   1   49.06 ? 151 VAL   A O    1 
ATOM   1024 C  CB   . VAL   A 1 129 ? 87.467  54.731  8.599   1   45.15 ? 151 VAL   A CB   1 
ATOM   1025 C  CG1  . VAL   A 1 129 ? 86.429  55.16   7.572   1   45.64 ? 151 VAL   A CG1  1 
ATOM   1026 C  CG2  . VAL   A 1 129 ? 86.949  54.966  10.007  1   45.24 ? 151 VAL   A CG2  1 
ATOM   1027 N  N    . LEU   A 1 130 ? 87.369  52.059  6.301   1   51.21 ? 152 LEU   A N    1 
ATOM   1028 C  CA   . LEU   A 1 130 ? 87.605  51.692  4.902   1   53.53 ? 152 LEU   A CA   1 
ATOM   1029 C  C    . LEU   A 1 130 ? 87.16   52.817  3.971   1   54.86 ? 152 LEU   A C    1 
ATOM   1030 O  O    . LEU   A 1 130 ? 86.089  53.399  4.185   1   54.56 ? 152 LEU   A O    1 
ATOM   1031 C  CB   . LEU   A 1 130 ? 86.894  50.376  4.565   1   54.13 ? 152 LEU   A CB   1 
ATOM   1032 N  N    . THR   A 1 131 ? 87.999  53.151  2.968   1   56.31 ? 153 THR   A N    1 
ATOM   1033 C  CA   . THR   A 1 131 ? 87.71   54.222  2.007   1   58.45 ? 153 THR   A CA   1 
ATOM   1034 C  C    . THR   A 1 131 ? 86.398  53.967  1.23    1   59.77 ? 153 THR   A C    1 
ATOM   1035 O  O    . THR   A 1 131 ? 85.63   54.903  0.981   1   59.53 ? 153 THR   A O    1 
ATOM   1036 C  CB   . THR   A 1 131 ? 88.917  54.446  1.093   1   60.78 ? 153 THR   A CB   1 
ATOM   1037 O  OG1  . THR   A 1 131 ? 90.063  54.743  1.895   1   62.43 ? 153 THR   A OG1  1 
ATOM   1038 C  CG2  . THR   A 1 131 ? 88.691  55.568  0.086   1   61.69 ? 153 THR   A CG2  1 
ATOM   1039 N  N    . GLU   A 1 132 ? 86.128  52.684  0.907   1   60.72 ? 154 GLU   A N    1 
ATOM   1040 C  CA   . GLU   A 1 132 ? 84.933  52.243  0.191   1   62.21 ? 154 GLU   A CA   1 
ATOM   1041 C  C    . GLU   A 1 132 ? 83.653  52.428  1.017   1   63.92 ? 154 GLU   A C    1 
ATOM   1042 O  O    . GLU   A 1 132 ? 82.587  52.642  0.443   1   64.36 ? 154 GLU   A O    1 
ATOM   1043 C  CB   . GLU   A 1 132 ? 85.083  50.778  -0.25   1   64.13 ? 154 GLU   A CB   1 
ATOM   1044 N  N    . GLN   A 1 133 ? 83.749  52.36   2.355   1   64.66 ? 155 GLN   A N    1 
ATOM   1045 C  CA   . GLN   A 1 133 ? 82.581  52.544  3.221   1   65.75 ? 155 GLN   A CA   1 
ATOM   1046 C  C    . GLN   A 1 133 ? 82.242  54.014  3.527   1   65.56 ? 155 GLN   A C    1 
ATOM   1047 O  O    . GLN   A 1 133 ? 81.215  54.279  4.15    1   65.59 ? 155 GLN   A O    1 
ATOM   1048 C  CB   . GLN   A 1 133 ? 82.722  51.741  4.519   1   68.78 ? 155 GLN   A CB   1 
ATOM   1049 C  CG   . GLN   A 1 133 ? 82.589  50.243  4.305   1   74.6  ? 155 GLN   A CG   1 
ATOM   1050 C  CD   . GLN   A 1 133 ? 83.305  49.426  5.348   1   82.75 ? 155 GLN   A CD   1 
ATOM   1051 O  OE1  . GLN   A 1 133 ? 84.094  49.929  6.165   1   86.08 ? 155 GLN   A OE1  1 
ATOM   1052 N  NE2  . GLN   A 1 133 ? 83.043  48.13   5.349   1   83.97 ? 155 GLN   A NE2  1 
ATOM   1053 N  N    . ARG   A 1 134 ? 83.073  54.963  3.073   1   65.33 ? 156 ARG   A N    1 
ATOM   1054 C  CA   . ARG   A 1 134 ? 82.827  56.38   3.309   1   65.91 ? 156 ARG   A CA   1 
ATOM   1055 C  C    . ARG   A 1 134 ? 81.699  56.91   2.422   1   67.91 ? 156 ARG   A C    1 
ATOM   1056 O  O    . ARG   A 1 134 ? 81.593  56.512  1.262   1   68.16 ? 156 ARG   A O    1 
ATOM   1057 C  CB   . ARG   A 1 134 ? 84.099  57.213  3.048   1   65.07 ? 156 ARG   A CB   1 
ATOM   1058 C  CG   . ARG   A 1 134 ? 85.263  56.962  4.001   1   63.4  ? 156 ARG   A CG   1 
ATOM   1059 C  CD   . ARG   A 1 134 ? 86.433  57.859  3.652   1   61.61 ? 156 ARG   A CD   1 
ATOM   1060 N  NE   . ARG   A 1 134 ? 87.547  57.704  4.585   1   60.2  ? 156 ARG   A NE   1 
ATOM   1061 C  CZ   . ARG   A 1 134 ? 87.744  58.467  5.656   1   58.81 ? 156 ARG   A CZ   1 
ATOM   1062 N  NH1  . ARG   A 1 134 ? 86.896  59.45   5.946   1   57.72 ? 156 ARG   A NH1  1 
ATOM   1063 N  NH2  . ARG   A 1 134 ? 88.782  58.249  6.449   1   56.9  ? 156 ARG   A NH2  1 
ATOM   1064 N  N    . VAL   A 1 135 ? 80.88   57.833  2.958   1   69.08 ? 157 VAL   A N    1 
ATOM   1065 C  CA   . VAL   A 1 135 ? 79.805  58.466  2.195   1   70.57 ? 157 VAL   A CA   1 
ATOM   1066 C  C    . VAL   A 1 135 ? 80.43   59.596  1.386   1   72.35 ? 157 VAL   A C    1 
ATOM   1067 O  O    . VAL   A 1 135 ? 81.058  60.479  1.966   1   72.77 ? 157 VAL   A O    1 
ATOM   1068 C  CB   . VAL   A 1 135 ? 78.643  58.968  3.086   1   71.04 ? 157 VAL   A CB   1 
ATOM   1069 N  N    . ARG   A 1 136 ? 80.318  59.537  0.045   1   73.17 ? 158 ARG   A N    1 
ATOM   1070 C  CA   . ARG   A 1 136 ? 80.924  60.53   -0.839  1   74.11 ? 158 ARG   A CA   1 
ATOM   1071 C  C    . ARG   A 1 136 ? 79.911  61.128  -1.8    1   74.75 ? 158 ARG   A C    1 
ATOM   1072 O  O    . ARG   A 1 136 ? 80.217  62.125  -2.453  1   75.13 ? 158 ARG   A O    1 
ATOM   1073 C  CB   . ARG   A 1 136 ? 82.092  59.912  -1.622  1   75.31 ? 158 ARG   A CB   1 
ATOM   1074 N  N    . GLN   A 1 139 ? 83.502  64.851  -4.334  1   68.84 ? 161 GLN   A N    1 
ATOM   1075 C  CA   . GLN   A 1 139 ? 84.941  64.916  -4.083  1   69.43 ? 161 GLN   A CA   1 
ATOM   1076 C  C    . GLN   A 1 139 ? 85.367  63.82   -3.108  1   69.07 ? 161 GLN   A C    1 
ATOM   1077 O  O    . GLN   A 1 139 ? 84.731  63.642  -2.07   1   69.53 ? 161 GLN   A O    1 
ATOM   1078 C  CB   . GLN   A 1 139 ? 85.322  66.307  -3.532  1   71.76 ? 161 GLN   A CB   1 
ATOM   1079 C  CG   . GLN   A 1 139 ? 86.822  66.573  -3.381  1   76.32 ? 161 GLN   A CG   1 
ATOM   1080 C  CD   . GLN   A 1 139 ? 87.125  68.041  -3.143  1   82.11 ? 161 GLN   A CD   1 
ATOM   1081 O  OE1  . GLN   A 1 139 ? 88.038  68.621  -3.748  1   83.95 ? 161 GLN   A OE1  1 
ATOM   1082 N  NE2  . GLN   A 1 139 ? 86.366  68.68   -2.262  1   83.18 ? 161 GLN   A NE2  1 
ATOM   1083 N  N    . LYS   A 1 140 ? 86.425  63.076  -3.45   1   68.14 ? 162 LYS   A N    1 
ATOM   1084 C  CA   . LYS   A 1 140 ? 86.985  62.051  -2.571  1   67.6  ? 162 LYS   A CA   1 
ATOM   1085 C  C    . LYS   A 1 140 ? 87.627  62.778  -1.366  1   66.99 ? 162 LYS   A C    1 
ATOM   1086 O  O    . LYS   A 1 140 ? 88.162  63.882  -1.522  1   66.97 ? 162 LYS   A O    1 
ATOM   1087 C  CB   . LYS   A 1 140 ? 88.041  61.213  -3.321  1   68.79 ? 162 LYS   A CB   1 
ATOM   1088 C  CG   . LYS   A 1 140 ? 88.432  59.937  -2.587  1   71.77 ? 162 LYS   A CG   1 
ATOM   1089 C  CD   . LYS   A 1 140 ? 89.445  59.113  -3.358  1   75.32 ? 162 LYS   A CD   1 
ATOM   1090 N  N    . TYR   A 1 141 ? 87.555  62.178  -0.169  1   66.12 ? 163 TYR   A N    1 
ATOM   1091 C  CA   . TYR   A 1 141 ? 88.088  62.805  1.044   1   65.75 ? 163 TYR   A CA   1 
ATOM   1092 C  C    . TYR   A 1 141 ? 89.583  63.235  0.914   1   66.76 ? 163 TYR   A C    1 
ATOM   1093 O  O    . TYR   A 1 141 ? 89.965  64.301  1.408   1   66.99 ? 163 TYR   A O    1 
ATOM   1094 C  CB   . TYR   A 1 141 ? 87.837  61.906  2.282   1   64.45 ? 163 TYR   A CB   1 
ATOM   1095 C  CG   . TYR   A 1 141 ? 88.899  60.859  2.526   1   63.77 ? 163 TYR   A CG   1 
ATOM   1096 C  CD1  . TYR   A 1 141 ? 88.955  59.703  1.759   1   64.02 ? 163 TYR   A CD1  1 
ATOM   1097 C  CD2  . TYR   A 1 141 ? 89.874  61.046  3.494   1   63.88 ? 163 TYR   A CD2  1 
ATOM   1098 C  CE1  . TYR   A 1 141 ? 89.947  58.751  1.965   1   64.55 ? 163 TYR   A CE1  1 
ATOM   1099 C  CE2  . TYR   A 1 141 ? 90.872  60.107  3.704   1   64.35 ? 163 TYR   A CE2  1 
ATOM   1100 C  CZ   . TYR   A 1 141 ? 90.908  58.961  2.938   1   65.06 ? 163 TYR   A CZ   1 
ATOM   1101 O  OH   . TYR   A 1 141 ? 91.899  58.042  3.165   1   65.77 ? 163 TYR   A OH   1 
ATOM   1102 N  N    . SER   A 1 142 ? 90.395  62.425  0.218   1   67.17 ? 164 SER   A N    1 
ATOM   1103 C  CA   . SER   A 1 142 ? 91.82   62.677  0.022   1   68.31 ? 164 SER   A CA   1 
ATOM   1104 C  C    . SER   A 1 142 ? 92.128  63.787  -0.985  1   69.65 ? 164 SER   A C    1 
ATOM   1105 O  O    . SER   A 1 142 ? 93.221  64.361  -0.947  1   69.82 ? 164 SER   A O    1 
ATOM   1106 C  CB   . SER   A 1 142 ? 92.558  61.389  -0.344  1   69.35 ? 164 SER   A CB   1 
ATOM   1107 O  OG   . SER   A 1 142 ? 91.791  60.476  -1.116  1   71.2  ? 164 SER   A OG   1 
ATOM   1108 N  N    . ASP   A 1 143 ? 91.165  64.097  -1.875  1   70.32 ? 165 ASP   A N    1 
ATOM   1109 C  CA   . ASP   A 1 143 ? 91.299  65.147  -2.892  1   71.3  ? 165 ASP   A CA   1 
ATOM   1110 C  C    . ASP   A 1 143 ? 91.409  66.558  -2.309  1   70.76 ? 165 ASP   A C    1 
ATOM   1111 O  O    . ASP   A 1 143 ? 91.925  67.465  -2.964  1   70.86 ? 165 ASP   A O    1 
ATOM   1112 C  CB   . ASP   A 1 143 ? 90.134  65.079  -3.887  1   74.55 ? 165 ASP   A CB   1 
ATOM   1113 C  CG   . ASP   A 1 143 ? 90.47   64.3    -5.138  1   82.09 ? 165 ASP   A CG   1 
ATOM   1114 O  OD1  . ASP   A 1 143 ? 91.279  63.344  -5.044  1   83.64 ? 165 ASP   A OD1  1 
ATOM   1115 O  OD2  . ASP   A 1 143 ? 89.936  64.65   -6.218  1   85.02 ? 165 ASP   A OD2  1 
ATOM   1116 N  N    . VAL   A 1 144 ? 90.908  66.734  -1.089  1   69.87 ? 166 VAL   A N    1 
ATOM   1117 C  CA   . VAL   A 1 144 ? 90.926  67.968  -0.324  1   69.36 ? 166 VAL   A CA   1 
ATOM   1118 C  C    . VAL   A 1 144 ? 92.386  68.442  -0.02   1   68.36 ? 166 VAL   A C    1 
ATOM   1119 O  O    . VAL   A 1 144 ? 92.634  69.639  0.137   1   68.25 ? 166 VAL   A O    1 
ATOM   1120 C  CB   . VAL   A 1 144 ? 90.072  67.677  0.939   1   70.31 ? 166 VAL   A CB   1 
ATOM   1121 C  CG1  . VAL   A 1 144 ? 90.461  68.537  2.131   1   70.77 ? 166 VAL   A CG1  1 
ATOM   1122 C  CG2  . VAL   A 1 144 ? 88.584  67.795  0.625   1   70.93 ? 166 VAL   A CG2  1 
ATOM   1123 N  N    . PHE   A 1 145 ? 93.349  67.508  -0.001  1   67.55 ? 167 PHE   A N    1 
ATOM   1124 C  CA   . PHE   A 1 145 ? 94.748  67.807  0.294   1   67.46 ? 167 PHE   A CA   1 
ATOM   1125 C  C    . PHE   A 1 145 ? 95.593  68.024  -0.961  1   68.27 ? 167 PHE   A C    1 
ATOM   1126 O  O    . PHE   A 1 145 ? 95.773  67.094  -1.737  1   68.42 ? 167 PHE   A O    1 
ATOM   1127 C  CB   . PHE   A 1 145 ? 95.359  66.697  1.171   1   66.65 ? 167 PHE   A CB   1 
ATOM   1128 C  CG   . PHE   A 1 145 ? 94.588  66.449  2.451   1   66.33 ? 167 PHE   A CG   1 
ATOM   1129 C  CD1  . PHE   A 1 145 ? 94.823  67.215  3.583   1   66.52 ? 167 PHE   A CD1  1 
ATOM   1130 C  CD2  . PHE   A 1 145 ? 93.604  65.474  2.511   1   66.43 ? 167 PHE   A CD2  1 
ATOM   1131 C  CE1  . PHE   A 1 145 ? 94.087  67.012  4.743   1   66.67 ? 167 PHE   A CE1  1 
ATOM   1132 C  CE2  . PHE   A 1 145 ? 92.874  65.274  3.676   1   66.57 ? 167 PHE   A CE2  1 
ATOM   1133 C  CZ   . PHE   A 1 145 ? 93.133  66.031  4.786   1   66.19 ? 167 PHE   A CZ   1 
ATOM   1134 N  N    . SER   A 1 146 ? 96.129  69.246  -1.142  1   68.56 ? 168 SER   A N    1 
ATOM   1135 C  CA   . SER   A 1 146 ? 96.969  69.611  -2.29   1   69.16 ? 168 SER   A CA   1 
ATOM   1136 C  C    . SER   A 1 146 ? 98.475  69.426  -2.02   1   69.76 ? 168 SER   A C    1 
ATOM   1137 O  O    . SER   A 1 146 ? 99.253  69.299  -2.964  1   70.36 ? 168 SER   A O    1 
ATOM   1138 C  CB   . SER   A 1 146 ? 96.704  71.053  -2.71   1   70.1  ? 168 SER   A CB   1 
ATOM   1139 N  N    . ASP   A 1 147 ? 98.888  69.422  -0.745  1   69.38 ? 169 ASP   A N    1 
ATOM   1140 C  CA   . ASP   A 1 147 ? 100.293 69.255  -0.348  1   69.11 ? 169 ASP   A CA   1 
ATOM   1141 C  C    . ASP   A 1 147 ? 100.762 67.815  -0.597  1   67.91 ? 169 ASP   A C    1 
ATOM   1142 O  O    . ASP   A 1 147 ? 100.045 66.874  -0.263  1   68.09 ? 169 ASP   A O    1 
ATOM   1143 C  CB   . ASP   A 1 147 ? 100.465 69.638  1.134   1   71.47 ? 169 ASP   A CB   1 
ATOM   1144 C  CG   . ASP   A 1 147 ? 101.867 69.463  1.687   1   77.32 ? 169 ASP   A CG   1 
ATOM   1145 O  OD1  . ASP   A 1 147 ? 102.697 70.384  1.505   1   77.77 ? 169 ASP   A OD1  1 
ATOM   1146 O  OD2  . ASP   A 1 147 ? 102.13  68.414  2.319   1   80.51 ? 169 ASP   A OD2  1 
ATOM   1147 N  N    . GLU   A 1 148 ? 101.955 67.643  -1.19   1   66.47 ? 170 GLU   A N    1 
ATOM   1148 C  CA   . GLU   A 1 148 ? 102.47  66.316  -1.515  1   65.3  ? 170 GLU   A CA   1 
ATOM   1149 C  C    . GLU   A 1 148 ? 102.738 65.44   -0.294  1   63.62 ? 170 GLU   A C    1 
ATOM   1150 O  O    . GLU   A 1 148 ? 102.437 64.248  -0.333  1   63.72 ? 170 GLU   A O    1 
ATOM   1151 C  CB   . GLU   A 1 148 ? 103.707 66.407  -2.414  1   67.37 ? 170 GLU   A CB   1 
ATOM   1152 C  CG   . GLU   A 1 148 ? 103.578 65.554  -3.664  1   71.96 ? 170 GLU   A CG   1 
ATOM   1153 C  CD   . GLU   A 1 148 ? 104.198 64.175  -3.548  1   78.13 ? 170 GLU   A CD   1 
ATOM   1154 O  OE1  . GLU   A 1 148 ? 105.383 64.091  -3.149  1   78.97 ? 170 GLU   A OE1  1 
ATOM   1155 O  OE2  . GLU   A 1 148 ? 103.506 63.18   -3.87   1   79.83 ? 170 GLU   A OE2  1 
ATOM   1156 N  N    . GLU   A 1 149 ? 103.288 66.016  0.786   1   61.89 ? 171 GLU   A N    1 
ATOM   1157 C  CA   . GLU   A 1 149 ? 103.551 65.246  2.003   1   60.58 ? 171 GLU   A CA   1 
ATOM   1158 C  C    . GLU   A 1 149 ? 102.229 64.832  2.675   1   58.95 ? 171 GLU   A C    1 
ATOM   1159 O  O    . GLU   A 1 149 ? 102.14  63.723  3.199   1   59.09 ? 171 GLU   A O    1 
ATOM   1160 C  CB   . GLU   A 1 149 ? 104.465 66.017  2.969   1   62.21 ? 171 GLU   A CB   1 
ATOM   1161 N  N    . ALA   A 1 150 ? 101.188 65.693  2.604   1   57.26 ? 172 ALA   A N    1 
ATOM   1162 C  CA   . ALA   A 1 150 ? 99.863  65.374  3.137   1   55.97 ? 172 ALA   A CA   1 
ATOM   1163 C  C    . ALA   A 1 150 ? 99.256  64.194  2.357   1   54.93 ? 172 ALA   A C    1 
ATOM   1164 O  O    . ALA   A 1 150 ? 98.816  63.228  2.982   1   54.89 ? 172 ALA   A O    1 
ATOM   1165 C  CB   . ALA   A 1 150 ? 98.949  66.59   3.066   1   55.72 ? 172 ALA   A CB   1 
ATOM   1166 N  N    . ARG   A 1 151 ? 99.305  64.236  0.997   1   53.93 ? 173 ARG   A N    1 
ATOM   1167 C  CA   . ARG   A 1 151 ? 98.799  63.167  0.118   1   53.14 ? 173 ARG   A CA   1 
ATOM   1168 C  C    . ARG   A 1 151 ? 99.543  61.862  0.366   1   50.7  ? 173 ARG   A C    1 
ATOM   1169 O  O    . ARG   A 1 151 ? 98.936  60.794  0.378   1   49.97 ? 173 ARG   A O    1 
ATOM   1170 C  CB   . ARG   A 1 151 ? 98.963  63.555  -1.36   1   55.73 ? 173 ARG   A CB   1 
ATOM   1171 C  CG   . ARG   A 1 151 ? 98.08   64.697  -1.81   1   61.03 ? 173 ARG   A CG   1 
ATOM   1172 C  CD   . ARG   A 1 151 ? 98.14   64.829  -3.319  1   66.22 ? 173 ARG   A CD   1 
ATOM   1173 N  NE   . ARG   A 1 151 ? 97.11   65.725  -3.841  1   71.41 ? 173 ARG   A NE   1 
ATOM   1174 C  CZ   . ARG   A 1 151 ? 96.685  65.731  -5.102  1   75.26 ? 173 ARG   A CZ   1 
ATOM   1175 N  NH1  . ARG   A 1 151 ? 97.18   64.866  -5.982  1   75.63 ? 173 ARG   A NH1  1 
ATOM   1176 N  NH2  . ARG   A 1 151 ? 95.744  66.586  -5.487  1   75.3  ? 173 ARG   A NH2  1 
ATOM   1177 N  N    . ASN   A 1 152 ? 100.866 61.957  0.58    1   49.39 ? 174 ASN   A N    1 
ATOM   1178 C  CA   . ASN   A 1 152 ? 101.7   60.789  0.859   1   48.57 ? 174 ASN   A CA   1 
ATOM   1179 C  C    . ASN   A 1 152 ? 101.269 60.162  2.165   1   46.37 ? 174 ASN   A C    1 
ATOM   1180 O  O    . ASN   A 1 152 ? 101.076 58.962  2.211   1   46.23 ? 174 ASN   A O    1 
ATOM   1181 C  CB   . ASN   A 1 152 ? 103.185 61.161  0.923   1   50.64 ? 174 ASN   A CB   1 
ATOM   1182 C  CG   . ASN   A 1 152 ? 103.892 61.203  -0.406  1   55.06 ? 174 ASN   A CG   1 
ATOM   1183 O  OD1  . ASN   A 1 152 ? 103.488 60.562  -1.383  1   56.26 ? 174 ASN   A OD1  1 
ATOM   1184 N  ND2  . ASN   A 1 152 ? 104.966 61.98   -0.462  1   56.08 ? 174 ASN   A ND2  1 
ATOM   1185 N  N    . SER   A 1 153 ? 101.051 60.983  3.204   1   44.89 ? 175 SER   A N    1 
ATOM   1186 C  CA   . SER   A 1 153 ? 100.631 60.529  4.532   1   43.96 ? 175 SER   A CA   1 
ATOM   1187 C  C    . SER   A 1 153 ? 99.289  59.814  4.462   1   42.11 ? 175 SER   A C    1 
ATOM   1188 O  O    . SER   A 1 153 ? 99.19   58.695  4.963   1   41.78 ? 175 SER   A O    1 
ATOM   1189 C  CB   . SER   A 1 153 ? 100.579 61.702  5.51    1   45.99 ? 175 SER   A CB   1 
ATOM   1190 O  OG   . SER   A 1 153 ? 101.868 62.256  5.73    1   49.06 ? 175 SER   A OG   1 
ATOM   1191 N  N    . ILE   A 1 154 ? 98.289  60.417  3.783   1   40.98 ? 176 ILE   A N    1 
ATOM   1192 C  CA   . ILE   A 1 154 ? 96.969  59.813  3.592   1   41.22 ? 176 ILE   A CA   1 
ATOM   1193 C  C    . ILE   A 1 154 ? 97.086  58.467  2.866   1   41.5  ? 176 ILE   A C    1 
ATOM   1194 O  O    . ILE   A 1 154 ? 96.568  57.456  3.342   1   41.23 ? 176 ILE   A O    1 
ATOM   1195 C  CB   . ILE   A 1 154 ? 96.005  60.792  2.861   1   41.52 ? 176 ILE   A CB   1 
ATOM   1196 C  CG1  . ILE   A 1 154 ? 95.555  61.9    3.805   1   42.51 ? 176 ILE   A CG1  1 
ATOM   1197 C  CG2  . ILE   A 1 154 ? 94.784  60.077  2.261   1   41.32 ? 176 ILE   A CG2  1 
ATOM   1198 N  N    . ARG   A 1 155 ? 97.81   58.442  1.744   1   41.61 ? 177 ARG   A N    1 
ATOM   1199 C  CA   . ARG   A 1 155 ? 98.004  57.22   0.967   1   42.25 ? 177 ARG   A CA   1 
ATOM   1200 C  C    . ARG   A 1 155 ? 98.657  56.117  1.824   1   41.7  ? 177 ARG   A C    1 
ATOM   1201 O  O    . ARG   A 1 155 ? 98.191  54.977  1.828   1   42.28 ? 177 ARG   A O    1 
ATOM   1202 C  CB   . ARG   A 1 155 ? 98.88   57.555  -0.26   1   44.86 ? 177 ARG   A CB   1 
ATOM   1203 C  CG   . ARG   A 1 155 ? 98.496  56.851  -1.552  1   49.54 ? 177 ARG   A CG   1 
ATOM   1204 C  CD   . ARG   A 1 155 ? 99.52   57.131  -2.653  1   53.64 ? 177 ARG   A CD   1 
ATOM   1205 N  NE   . ARG   A 1 155 ? 100.833 56.602  -2.286  1   57.74 ? 177 ARG   A NE   1 
ATOM   1206 C  CZ   . ARG   A 1 155 ? 101.89  57.345  -1.97   1   60.38 ? 177 ARG   A CZ   1 
ATOM   1207 N  NH1  . ARG   A 1 155 ? 103.028 56.769  -1.611  1   59.85 ? 177 ARG   A NH1  1 
ATOM   1208 N  NH2  . ARG   A 1 155 ? 101.809 58.671  -1.997  1   60.55 ? 177 ARG   A NH2  1 
ATOM   1209 N  N    . ASN   A 1 156 ? 99.692  56.474  2.597   1   40.78 ? 178 ASN   A N    1 
ATOM   1210 C  CA   . ASN   A 1 156 ? 100.362 55.518  3.469   1   40.96 ? 178 ASN   A CA   1 
ATOM   1211 C  C    . ASN   A 1 156 ? 99.415  54.997  4.547   1   39.64 ? 178 ASN   A C    1 
ATOM   1212 O  O    . ASN   A 1 156 ? 99.399  53.799  4.788   1   39.51 ? 178 ASN   A O    1 
ATOM   1213 C  CB   . ASN   A 1 156 ? 101.606 56.136  4.1     1   43.71 ? 178 ASN   A CB   1 
ATOM   1214 C  CG   . ASN   A 1 156 ? 102.689 56.501  3.105   1   48.66 ? 178 ASN   A CG   1 
ATOM   1215 O  OD1  . ASN   A 1 156 ? 102.776 55.93   2.013   1   50.49 ? 178 ASN   A OD1  1 
ATOM   1216 N  ND2  . ASN   A 1 156 ? 103.526 57.478  3.459   1   49.27 ? 178 ASN   A ND2  1 
ATOM   1217 N  N    . SER   A 1 157 ? 98.59   55.873  5.162   1   38.74 ? 179 SER   A N    1 
ATOM   1218 C  CA   . SER   A 1 157 ? 97.645  55.435  6.194   1   38.78 ? 179 SER   A CA   1 
ATOM   1219 C  C    . SER   A 1 157 ? 96.595  54.463  5.656   1   39.79 ? 179 SER   A C    1 
ATOM   1220 O  O    . SER   A 1 157 ? 96.141  53.606  6.408   1   40.5  ? 179 SER   A O    1 
ATOM   1221 C  CB   . SER   A 1 157 ? 96.992  56.614  6.906   1   38.51 ? 179 SER   A CB   1 
ATOM   1222 O  OG   . SER   A 1 157 ? 96.151  57.386  6.064   1   39.29 ? 179 SER   A OG   1 
ATOM   1223 N  N    . GLU   A 1 158 ? 96.257  54.551  4.351   1   39.83 ? 180 GLU   A N    1 
ATOM   1224 C  CA   . GLU   A 1 158 ? 95.304  53.63   3.728   1   40.73 ? 180 GLU   A CA   1 
ATOM   1225 C  C    . GLU   A 1 158 ? 95.954  52.271  3.442   1   41.11 ? 180 GLU   A C    1 
ATOM   1226 O  O    . GLU   A 1 158 ? 95.337  51.236  3.682   1   41.55 ? 180 GLU   A O    1 
ATOM   1227 C  CB   . GLU   A 1 158 ? 94.79   54.195  2.394   1   43.07 ? 180 GLU   A CB   1 
ATOM   1228 C  CG   . GLU   A 1 158 ? 94.038  55.501  2.47    1   48.32 ? 180 GLU   A CG   1 
ATOM   1229 C  CD   . GLU   A 1 158 ? 93.668  56.048  1.103   1   57.21 ? 180 GLU   A CD   1 
ATOM   1230 O  OE1  . GLU   A 1 158 ? 94.374  55.729  0.117   1   60.48 ? 180 GLU   A OE1  1 
ATOM   1231 O  OE2  . GLU   A 1 158 ? 92.668  56.796  1.017   1   58.89 ? 180 GLU   A OE2  1 
ATOM   1232 N  N    . LYS   A 1 159 ? 97.187  52.27   2.9     1   40.8  ? 181 LYS   A N    1 
ATOM   1233 C  CA   . LYS   A 1 159 ? 97.877  51.033  2.514   1   40.61 ? 181 LYS   A CA   1 
ATOM   1234 C  C    . LYS   A 1 159 ? 98.528  50.286  3.661   1   39.64 ? 181 LYS   A C    1 
ATOM   1235 O  O    . LYS   A 1 159 ? 98.631  49.06   3.595   1   39.77 ? 181 LYS   A O    1 
ATOM   1236 C  CB   . LYS   A 1 159 ? 98.908  51.302  1.398   1   42.82 ? 181 LYS   A CB   1 
ATOM   1237 C  CG   . LYS   A 1 159 ? 98.315  51.209  -0.003  1   47.58 ? 181 LYS   A CG   1 
ATOM   1238 C  CD   . LYS   A 1 159 ? 97.728  52.526  -0.499  1   52.2  ? 181 LYS   A CD   1 
ATOM   1239 N  N    . ASP   A 1 160 ? 99.021  51.002  4.69    1   38.51 ? 182 ASP   A N    1 
ATOM   1240 C  CA   . ASP   A 1 160 ? 99.629  50.334  5.847   1   38.08 ? 182 ASP   A CA   1 
ATOM   1241 C  C    . ASP   A 1 160 ? 98.527  49.59   6.609   1   37.18 ? 182 ASP   A C    1 
ATOM   1242 O  O    . ASP   A 1 160 ? 97.395  50.065  6.645   1   37.15 ? 182 ASP   A O    1 
ATOM   1243 C  CB   . ASP   A 1 160 ? 100.252 51.366  6.801   1   40.07 ? 182 ASP   A CB   1 
ATOM   1244 C  CG   . ASP   A 1 160 ? 101.42  52.165  6.254   1   44.03 ? 182 ASP   A CG   1 
ATOM   1245 O  OD1  . ASP   A 1 160 ? 102.054 51.701  5.286   1   44.28 ? 182 ASP   A OD1  1 
ATOM   1246 O  OD2  . ASP   A 1 160 ? 101.685 53.261  6.79    1   45.97 ? 182 ASP   A OD2  1 
ATOM   1247 N  N    . PRO   A 1 161 ? 98.821  48.436  7.23    1   36.72 ? 183 PRO   A N    1 
ATOM   1248 C  CA   . PRO   A 1 161 ? 97.78   47.739  7.998   1   36.11 ? 183 PRO   A CA   1 
ATOM   1249 C  C    . PRO   A 1 161 ? 97.225  48.61   9.137   1   36.67 ? 183 PRO   A C    1 
ATOM   1250 O  O    . PRO   A 1 161 ? 97.969  49.214  9.919   1   37.41 ? 183 PRO   A O    1 
ATOM   1251 C  CB   . PRO   A 1 161 ? 98.481  46.481  8.519   1   36.37 ? 183 PRO   A CB   1 
ATOM   1252 C  CG   . PRO   A 1 161 ? 99.932  46.758  8.413   1   37.55 ? 183 PRO   A CG   1 
ATOM   1253 C  CD   . PRO   A 1 161 ? 100.11  47.714  7.271   1   36.4  ? 183 PRO   A CD   1 
ATOM   1254 N  N    . SER   A 1 162 ? 95.906  48.741  9.163   1   35.36 ? 184 SER   A N    1 
ATOM   1255 C  CA   . SER   A 1 162 ? 95.192  49.499  10.171  1   34.77 ? 184 SER   A CA   1 
ATOM   1256 C  C    . SER   A 1 162 ? 95.102  48.668  11.464  1   34.4  ? 184 SER   A C    1 
ATOM   1257 O  O    . SER   A 1 162 ? 95.459  47.483  11.474  1   35.52 ? 184 SER   A O    1 
ATOM   1258 C  CB   . SER   A 1 162 ? 93.786  49.815  9.66    1   35.14 ? 184 SER   A CB   1 
ATOM   1259 O  OG   . SER   A 1 162 ? 92.993  48.639  9.579   1   37.06 ? 184 SER   A OG   1 
ATOM   1260 N  N    . LEU   A 1 163 ? 94.602  49.266  12.555  1   32.51 ? 185 LEU   A N    1 
ATOM   1261 C  CA   . LEU   A 1 163 ? 94.386  48.528  13.793  1   31.71 ? 185 LEU   A CA   1 
ATOM   1262 C  C    . LEU   A 1 163 ? 93.344  47.417  13.552  1   31.7  ? 185 LEU   A C    1 
ATOM   1263 O  O    . LEU   A 1 163 ? 93.482  46.332  14.091  1   31.34 ? 185 LEU   A O    1 
ATOM   1264 C  CB   . LEU   A 1 163 ? 93.93   49.471  14.912  1   31.6  ? 185 LEU   A CB   1 
ATOM   1265 C  CG   . LEU   A 1 163 ? 95.047  50.257  15.603  1   32.66 ? 185 LEU   A CG   1 
ATOM   1266 C  CD1  . LEU   A 1 163 ? 94.488  51.273  16.576  1   32.79 ? 185 LEU   A CD1  1 
ATOM   1267 C  CD2  . LEU   A 1 163 ? 96.095  49.328  16.228  1   33.01 ? 185 LEU   A CD2  1 
ATOM   1268 N  N    . LEU   A 1 164 ? 92.335  47.677  12.693  1   31.98 ? 186 LEU   A N    1 
ATOM   1269 C  CA   . LEU   A 1 164 ? 91.328  46.678  12.319  1   32.34 ? 186 LEU   A CA   1 
ATOM   1270 C  C    . LEU   A 1 164 ? 91.995  45.433  11.703  1   33.25 ? 186 LEU   A C    1 
ATOM   1271 O  O    . LEU   A 1 164 ? 91.702  44.317  12.137  1   33.25 ? 186 LEU   A O    1 
ATOM   1272 C  CB   . LEU   A 1 164 ? 90.318  47.297  11.329  1   31.44 ? 186 LEU   A CB   1 
ATOM   1273 C  CG   . LEU   A 1 164 ? 89.307  46.335  10.691  1   31.31 ? 186 LEU   A CG   1 
ATOM   1274 C  CD1  . LEU   A 1 164 ? 88.441  45.639  11.764  1   31.12 ? 186 LEU   A CD1  1 
ATOM   1275 C  CD2  . LEU   A 1 164 ? 88.456  47.061  9.632   1   30.64 ? 186 LEU   A CD2  1 
ATOM   1276 N  N    . GLU   A 1 165 ? 92.893  45.63   10.708  1   33.64 ? 187 GLU   A N    1 
ATOM   1277 C  CA   . GLU   A 1 165 ? 93.573  44.512  10.058  1   34.59 ? 187 GLU   A CA   1 
ATOM   1278 C  C    . GLU   A 1 165 ? 94.492  43.794  11.025  1   34.52 ? 187 GLU   A C    1 
ATOM   1279 O  O    . GLU   A 1 165 ? 94.458  42.577  11.096  1   34.62 ? 187 GLU   A O    1 
ATOM   1280 C  CB   . GLU   A 1 165 ? 94.391  44.993  8.842   1   38.59 ? 187 GLU   A CB   1 
ATOM   1281 C  CG   . GLU   A 1 165 ? 93.599  45.769  7.806   1   46.12 ? 187 GLU   A CG   1 
ATOM   1282 C  CD   . GLU   A 1 165 ? 94.484  46.478  6.794   1   55.11 ? 187 GLU   A CD   1 
ATOM   1283 O  OE1  . GLU   A 1 165 ? 94.315  47.709  6.622   1   54.55 ? 187 GLU   A OE1  1 
ATOM   1284 O  OE2  . GLU   A 1 165 ? 95.387  45.819  6.223   1   59.42 ? 187 GLU   A OE2  1 
ATOM   1285 N  N    . LEU   A 1 166 ? 95.315  44.539  11.778  1   34.7  ? 188 LEU   A N    1 
ATOM   1286 C  CA   . LEU   A 1 166 ? 96.253  43.938  12.718  1   35.08 ? 188 LEU   A CA   1 
ATOM   1287 C  C    . LEU   A 1 166 ? 95.574  43.158  13.844  1   35.06 ? 188 LEU   A C    1 
ATOM   1288 O  O    . LEU   A 1 166 ? 96.051  42.088  14.222  1   35.28 ? 188 LEU   A O    1 
ATOM   1289 C  CB   . LEU   A 1 166 ? 97.183  45.018  13.277  1   35.79 ? 188 LEU   A CB   1 
ATOM   1290 C  CG   . LEU   A 1 166 ? 98.102  45.624  12.239  1   37.63 ? 188 LEU   A CG   1 
ATOM   1291 C  CD1  . LEU   A 1 166 ? 98.783  46.838  12.774  1   38.12 ? 188 LEU   A CD1  1 
ATOM   1292 C  CD2  . LEU   A 1 166 ? 99.136  44.618  11.778  1   38.44 ? 188 LEU   A CD2  1 
ATOM   1293 N  N    . VAL   A 1 167 ? 94.463  43.678  14.377  1   34.25 ? 189 VAL   A N    1 
ATOM   1294 C  CA   . VAL   A 1 167 ? 93.731  42.989  15.448  1   33.82 ? 189 VAL   A CA   1 
ATOM   1295 C  C    . VAL   A 1 167 ? 93.162  41.664  14.935  1   33.72 ? 189 VAL   A C    1 
ATOM   1296 O  O    . VAL   A 1 167 ? 93.181  40.666  15.666  1   33.95 ? 189 VAL   A O    1 
ATOM   1297 C  CB   . VAL   A 1 167 ? 92.667  43.917  16.095  1   34.22 ? 189 VAL   A CB   1 
ATOM   1298 C  CG1  . VAL   A 1 167 ? 91.622  43.132  16.886  1   34.95 ? 189 VAL   A CG1  1 
ATOM   1299 C  CG2  . VAL   A 1 167 ? 93.344  44.949  16.987  1   34.46 ? 189 VAL   A CG2  1 
ATOM   1300 N  N    . GLN   A 1 168 ? 92.692  41.646  13.673  1   33.36 ? 190 GLN   A N    1 
ATOM   1301 C  CA   . GLN   A 1 168 ? 92.185  40.435  13.033  1   34.25 ? 190 GLN   A CA   1 
ATOM   1302 C  C    . GLN   A 1 168 ? 93.276  39.362  12.902  1   35.45 ? 190 GLN   A C    1 
ATOM   1303 O  O    . GLN   A 1 168 ? 93.029  38.233  13.298  1   35.75 ? 190 GLN   A O    1 
ATOM   1304 C  CB   . GLN   A 1 168 ? 91.614  40.762  11.651  1   35.33 ? 190 GLN   A CB   1 
ATOM   1305 C  CG   . GLN   A 1 168 ? 90.194  41.268  11.684  1   36.92 ? 190 GLN   A CG   1 
ATOM   1306 C  CD   . GLN   A 1 168 ? 89.771  41.612  10.308  1   39.82 ? 190 GLN   A CD   1 
ATOM   1307 O  OE1  . GLN   A 1 168 ? 89.824  42.767  9.889   1   40.09 ? 190 GLN   A OE1  1 
ATOM   1308 N  NE2  . GLN   A 1 168 ? 89.387  40.594  9.556   1   41.66 ? 190 GLN   A NE2  1 
ATOM   1309 N  N    . ARG   A 1 169 ? 94.502  39.715  12.426  1   36.02 ? 191 ARG   A N    1 
ATOM   1310 C  CA   . ARG   A 1 169 ? 95.608  38.742  12.312  1   36.62 ? 191 ARG   A CA   1 
ATOM   1311 C  C    . ARG   A 1 169 ? 95.933  38.145  13.671  1   37.26 ? 191 ARG   A C    1 
ATOM   1312 O  O    . ARG   A 1 169 ? 96.136  36.941  13.771  1   37.99 ? 191 ARG   A O    1 
ATOM   1313 C  CB   . ARG   A 1 169 ? 96.885  39.351  11.683  1   37.92 ? 191 ARG   A CB   1 
ATOM   1314 C  CG   . ARG   A 1 169 ? 96.687  40.217  10.441  1   41.93 ? 191 ARG   A CG   1 
ATOM   1315 C  CD   . ARG   A 1 169 ? 96.401  39.507  9.121   1   46.03 ? 191 ARG   A CD   1 
ATOM   1316 N  NE   . ARG   A 1 169 ? 95.011  39.058  8.964   1   49.06 ? 191 ARG   A NE   1 
ATOM   1317 C  CZ   . ARG   A 1 169 ? 94.014  39.815  8.508   1   51.36 ? 191 ARG   A CZ   1 
ATOM   1318 N  NH1  . ARG   A 1 169 ? 94.228  41.085  8.181   1   49.81 ? 191 ARG   A NH1  1 
ATOM   1319 N  NH2  . ARG   A 1 169 ? 92.791  39.31   8.386   1   51.95 ? 191 ARG   A NH2  1 
ATOM   1320 N  N    . TRP   A 1 170 ? 95.944  38.979  14.725  1   36.69 ? 192 TRP   A N    1 
ATOM   1321 C  CA   . TRP   A 1 170 ? 96.202  38.556  16.095  1   36.43 ? 192 TRP   A CA   1 
ATOM   1322 C  C    . TRP   A 1 170 ? 95.103  37.613  16.585  1   36.97 ? 192 TRP   A C    1 
ATOM   1323 O  O    . TRP   A 1 170 ? 95.4    36.62   17.247  1   37.1  ? 192 TRP   A O    1 
ATOM   1324 C  CB   . TRP   A 1 170 ? 96.332  39.801  17.01   1   36.06 ? 192 TRP   A CB   1 
ATOM   1325 C  CG   . TRP   A 1 170 ? 96.244  39.534  18.494  1   36.01 ? 192 TRP   A CG   1 
ATOM   1326 C  CD1  . TRP   A 1 170 ? 97.195  38.965  19.288  1   36.72 ? 192 TRP   A CD1  1 
ATOM   1327 C  CD2  . TRP   A 1 170 ? 95.15   39.88   19.363  1   35.83 ? 192 TRP   A CD2  1 
ATOM   1328 N  NE1  . TRP   A 1 170 ? 96.74   38.888  20.593  1   36.96 ? 192 TRP   A NE1  1 
ATOM   1329 C  CE2  . TRP   A 1 170 ? 95.509  39.484  20.671  1   36.42 ? 192 TRP   A CE2  1 
ATOM   1330 C  CE3  . TRP   A 1 170 ? 93.914  40.508  19.165  1   35.77 ? 192 TRP   A CE3  1 
ATOM   1331 C  CZ2  . TRP   A 1 170 ? 94.684  39.703  21.765  1   36.46 ? 192 TRP   A CZ2  1 
ATOM   1332 C  CZ3  . TRP   A 1 170 ? 93.085  40.693  20.245  1   36.31 ? 192 TRP   A CZ3  1 
ATOM   1333 C  CH2  . TRP   A 1 170 ? 93.465  40.283  21.527  1   36.53 ? 192 TRP   A CH2  1 
ATOM   1334 N  N    . LEU   A 1 171 ? 93.837  37.913  16.255  1   37.44 ? 193 LEU   A N    1 
ATOM   1335 C  CA   . LEU   A 1 171 ? 92.697  37.089  16.647  1   38.1  ? 193 LEU   A CA   1 
ATOM   1336 C  C    . LEU   A 1 171 ? 92.7    35.737  15.931  1   38.97 ? 193 LEU   A C    1 
ATOM   1337 O  O    . LEU   A 1 171 ? 92.265  34.746  16.509  1   39.03 ? 193 LEU   A O    1 
ATOM   1338 C  CB   . LEU   A 1 171 ? 91.374  37.815  16.36   1   38.16 ? 193 LEU   A CB   1 
ATOM   1339 C  CG   . LEU   A 1 171 ? 90.946  38.892  17.361  1   38.94 ? 193 LEU   A CG   1 
ATOM   1340 C  CD1  . LEU   A 1 171 ? 89.693  39.627  16.876  1   38.96 ? 193 LEU   A CD1  1 
ATOM   1341 C  CD2  . LEU   A 1 171 ? 90.728  38.305  18.716  1   39.17 ? 193 LEU   A CD2  1 
ATOM   1342 N  N    . GLU   A 1 172 ? 93.154  35.701  14.677  1   39.91 ? 194 GLU   A N    1 
ATOM   1343 C  CA   . GLU   A 1 172 ? 93.219  34.478  13.863  1   41.83 ? 194 GLU   A CA   1 
ATOM   1344 C  C    . GLU   A 1 172 ? 94.194  33.461  14.482  1   44.49 ? 194 GLU   A C    1 
ATOM   1345 O  O    . GLU   A 1 172 ? 93.907  32.265  14.535  1   44.95 ? 194 GLU   A O    1 
ATOM   1346 C  CB   . GLU   A 1 172 ? 93.658  34.825  12.436  1   42.37 ? 194 GLU   A CB   1 
ATOM   1347 C  CG   . GLU   A 1 172 ? 92.551  35.45   11.603  1   45.14 ? 194 GLU   A CG   1 
ATOM   1348 C  CD   . GLU   A 1 172 ? 93.012  36.211  10.376  1   50.7  ? 194 GLU   A CD   1 
ATOM   1349 O  OE1  . GLU   A 1 172 ? 94.234  36.244  10.108  1   51.36 ? 194 GLU   A OE1  1 
ATOM   1350 O  OE2  . GLU   A 1 172 ? 92.146  36.792  9.686   1   54.24 ? 194 GLU   A OE2  1 
ATOM   1351 N  N    . ARG   A 1 173 ? 95.317  33.963  15.011  1   45.47 ? 195 ARG   A N    1 
ATOM   1352 C  CA   . ARG   A 1 173 ? 96.35   33.167  15.65   1   46.68 ? 195 ARG   A CA   1 
ATOM   1353 C  C    . ARG   A 1 173 ? 96.057  32.912  17.129  1   48.76 ? 195 ARG   A C    1 
ATOM   1354 O  O    . ARG   A 1 173 ? 96.988  32.596  17.866  1   49.67 ? 195 ARG   A O    1 
ATOM   1355 C  CB   . ARG   A 1 173 ? 97.712  33.875  15.512  1   47.2  ? 195 ARG   A CB   1 
ATOM   1356 C  CG   . ARG   A 1 173 ? 98.047  34.272  14.076  1   48.69 ? 195 ARG   A CG   1 
ATOM   1357 C  CD   . ARG   A 1 173 ? 99.174  35.28   14.033  1   51.4  ? 195 ARG   A CD   1 
ATOM   1358 N  N    . THR   A 1 174 ? 94.798  33.031  17.574  1   49.45 ? 196 THR   A N    1 
ATOM   1359 C  CA   . THR   A 1 174 ? 94.458  32.805  18.976  1   50.83 ? 196 THR   A CA   1 
ATOM   1360 C  C    . THR   A 1 174 ? 94.715  31.368  19.386  1   52.85 ? 196 THR   A C    1 
ATOM   1361 O  O    . THR   A 1 174 ? 94.123  30.446  18.827  1   53.34 ? 196 THR   A O    1 
ATOM   1362 C  CB   . THR   A 1 174 ? 92.987  33.184  19.274  1   51.31 ? 196 THR   A CB   1 
ATOM   1363 O  OG1  . THR   A 1 174 ? 92.773  34.566  19.013  1   51.79 ? 196 THR   A OG1  1 
ATOM   1364 C  CG2  . THR   A 1 174 ? 92.584  32.879  20.707  1   51.49 ? 196 THR   A CG2  1 
ATOM   1365 N  N    . PRO   A 1 175 ? 95.592  31.152  20.378  1   53.89 ? 197 PRO   A N    1 
ATOM   1366 C  CA   . PRO   A 1 175 ? 95.801  29.78   20.872  1   54.33 ? 197 PRO   A CA   1 
ATOM   1367 C  C    . PRO   A 1 175 ? 94.518  29.333  21.589  1   54.59 ? 197 PRO   A C    1 
ATOM   1368 O  O    . PRO   A 1 175 ? 93.996  30.011  22.496  1   54.97 ? 197 PRO   A O    1 
ATOM   1369 C  CB   . PRO   A 1 175 ? 96.999  29.908  21.823  1   55.03 ? 197 PRO   A CB   1 
ATOM   1370 C  CG   . PRO   A 1 175 ? 97.521  31.333  21.645  1   55.46 ? 197 PRO   A CG   1 
ATOM   1371 C  CD   . PRO   A 1 175 ? 96.36   32.14   21.157  1   53.72 ? 197 PRO   A CD   1 
ATOM   1372 N  N    . GLY   A 1 176 ? 93.997  28.223  21.123  1   53.78 ? 198 GLY   A N    1 
ATOM   1373 C  CA   . GLY   A 1 176 ? 92.743  27.679  21.601  1   53.7  ? 198 GLY   A CA   1 
ATOM   1374 C  C    . GLY   A 1 176 ? 91.87   27.277  20.431  1   53.88 ? 198 GLY   A C    1 
ATOM   1375 O  O    . GLY   A 1 176 ? 91.106  26.321  20.527  1   54.25 ? 198 GLY   A O    1 
ATOM   1376 N  N    . LEU   A 1 177 ? 91.968  28.014  19.317  1   53.76 ? 199 LEU   A N    1 
ATOM   1377 C  CA   . LEU   A 1 177 ? 91.25   27.73   18.081  1   54.51 ? 199 LEU   A CA   1 
ATOM   1378 C  C    . LEU   A 1 177 ? 91.902  26.567  17.302  1   56.38 ? 199 LEU   A C    1 
ATOM   1379 O  O    . LEU   A 1 177 ? 91.225  25.944  16.47   1   56.73 ? 199 LEU   A O    1 
ATOM   1380 C  CB   . LEU   A 1 177 ? 91.241  28.973  17.169  1   53.73 ? 199 LEU   A CB   1 
ATOM   1381 C  CG   . LEU   A 1 177 ? 90.404  30.173  17.589  1   53.33 ? 199 LEU   A CG   1 
ATOM   1382 C  CD1  . LEU   A 1 177 ? 90.493  31.242  16.54   1   53.5  ? 199 LEU   A CD1  1 
ATOM   1383 C  CD2  . LEU   A 1 177 ? 88.954  29.781  17.832  1   53.12 ? 199 LEU   A CD2  1 
ATOM   1384 N  N    . GLU   A 1 178 ? 93.224  26.314  17.528  1   56.84 ? 200 GLU   A N    1 
ATOM   1385 C  CA   . GLU   A 1 178 ? 94.005  25.269  16.865  1   57.47 ? 200 GLU   A CA   1 
ATOM   1386 C  C    . GLU   A 1 178 ? 93.29   23.92   16.902  1   57.78 ? 200 GLU   A C    1 
ATOM   1387 O  O    . GLU   A 1 178 ? 92.941  23.427  17.973  1   57.77 ? 200 GLU   A O    1 
ATOM   1388 C  CB   . GLU   A 1 178 ? 95.407  25.172  17.489  1   59.38 ? 200 GLU   A CB   1 
ATOM   1389 C  CG   . GLU   A 1 178 ? 96.308  26.33   17.101  1   63.37 ? 200 GLU   A CG   1 
ATOM   1390 N  N    . GLU   A 1 179 ? 93.022  23.357  15.729  1   58.06 ? 201 GLU   A N    1 
ATOM   1391 C  CA   . GLU   A 1 179 ? 92.308  22.087  15.621  1   59.06 ? 201 GLU   A CA   1 
ATOM   1392 C  C    . GLU   A 1 179 ? 93.102  20.915  16.244  1   59.54 ? 201 GLU   A C    1 
ATOM   1393 O  O    . GLU   A 1 179 ? 92.504  19.986  16.788  1   59.67 ? 201 GLU   A O    1 
ATOM   1394 C  CB   . GLU   A 1 179 ? 91.89   21.838  14.169  1   61.3  ? 201 GLU   A CB   1 
ATOM   1395 C  CG   . GLU   A 1 179 ? 90.92   22.895  13.649  1   66.29 ? 201 GLU   A CG   1 
ATOM   1396 C  CD   . GLU   A 1 179 ? 91.478  24.203  13.098  1   72.61 ? 201 GLU   A CD   1 
ATOM   1397 O  OE1  . GLU   A 1 179 ? 90.672  25.017  12.591  1   72.94 ? 201 GLU   A OE1  1 
ATOM   1398 O  OE2  . GLU   A 1 179 ? 92.712  24.416  13.162  1   74.61 ? 201 GLU   A OE2  1 
ATOM   1399 N  N    . SER   A 1 180 ? 94.446  21.023  16.252  1   59.45 ? 202 SER   A N    1 
ATOM   1400 C  CA   . SER   A 1 180 ? 95.36   20.073  16.893  1   59.45 ? 202 SER   A CA   1 
ATOM   1401 C  C    . SER   A 1 180 ? 95.315  20.203  18.427  1   58.78 ? 202 SER   A C    1 
ATOM   1402 O  O    . SER   A 1 180 ? 95.475  19.21   19.14   1   59    ? 202 SER   A O    1 
ATOM   1403 C  CB   . SER   A 1 180 ? 96.79   20.325  16.416  1   60.96 ? 202 SER   A CB   1 
ATOM   1404 N  N    . GLY   A 1 181 ? 95.129  21.429  18.918  1   57.71 ? 203 GLY   A N    1 
ATOM   1405 C  CA   . GLY   A 1 181 ? 95.084  21.723  20.345  1   56.71 ? 203 GLY   A CA   1 
ATOM   1406 C  C    . GLY   A 1 181 ? 93.708  21.692  20.981  1   55.38 ? 203 GLY   A C    1 
ATOM   1407 O  O    . GLY   A 1 181 ? 93.021  20.664  20.958  1   55.4  ? 203 GLY   A O    1 
ATOM   1408 N  N    . PHE   A 1 182 ? 93.311  22.827  21.589  1   53.85 ? 204 PHE   A N    1 
ATOM   1409 C  CA   . PHE   A 1 182 ? 92.046  22.96   22.307  1   52.31 ? 204 PHE   A CA   1 
ATOM   1410 C  C    . PHE   A 1 182 ? 90.831  22.779  21.399  1   51.41 ? 204 PHE   A C    1 
ATOM   1411 O  O    . PHE   A 1 182 ? 89.806  22.289  21.858  1   51.04 ? 204 PHE   A O    1 
ATOM   1412 C  CB   . PHE   A 1 182 ? 91.984  24.278  23.102  1   51.39 ? 204 PHE   A CB   1 
ATOM   1413 C  CG   . PHE   A 1 182 ? 90.797  24.356  24.034  1   51.03 ? 204 PHE   A CG   1 
ATOM   1414 C  CD1  . PHE   A 1 182 ? 90.758  23.605  25.192  1   51.26 ? 204 PHE   A CD1  1 
ATOM   1415 C  CD2  . PHE   A 1 182 ? 89.703  25.153  23.73   1   51.2  ? 204 PHE   A CD2  1 
ATOM   1416 C  CE1  . PHE   A 1 182 ? 89.65   23.643  26.023  1   51.73 ? 204 PHE   A CE1  1 
ATOM   1417 C  CE2  . PHE   A 1 182 ? 88.603  25.201  24.574  1   51.65 ? 204 PHE   A CE2  1 
ATOM   1418 C  CZ   . PHE   A 1 182 ? 88.586  24.452  25.719  1   51.46 ? 204 PHE   A CZ   1 
ATOM   1419 N  N    . ASN   A 1 183 ? 90.95   23.146  20.114  1   51.09 ? 205 ASN   A N    1 
ATOM   1420 C  CA   . ASN   A 1 183 ? 89.896  22.966  19.115  1   51.24 ? 205 ASN   A CA   1 
ATOM   1421 C  C    . ASN   A 1 183 ? 88.541  23.542  19.583  1   50.75 ? 205 ASN   A C    1 
ATOM   1422 O  O    . ASN   A 1 183 ? 87.539  22.822  19.651  1   51.62 ? 205 ASN   A O    1 
ATOM   1423 C  CB   . ASN   A 1 183 ? 89.812  21.482  18.751  1   52.7  ? 205 ASN   A CB   1 
ATOM   1424 C  CG   . ASN   A 1 183 ? 88.816  21.147  17.697  1   56.61 ? 205 ASN   A CG   1 
ATOM   1425 O  OD1  . ASN   A 1 183 ? 88.737  21.802  16.648  1   58.61 ? 205 ASN   A OD1  1 
ATOM   1426 N  ND2  . ASN   A 1 183 ? 88.02   20.13   17.984  1   56.75 ? 205 ASN   A ND2  1 
ATOM   1427 N  N    . PHE   A 1 184 ? 88.536  24.841  19.947  1   49.03 ? 206 PHE   A N    1 
ATOM   1428 C  CA   . PHE   A 1 184 ? 87.36   25.517  20.486  1   47.56 ? 206 PHE   A CA   1 
ATOM   1429 C  C    . PHE   A 1 184 ? 86.152  25.509  19.558  1   47.25 ? 206 PHE   A C    1 
ATOM   1430 O  O    . PHE   A 1 184 ? 85.044  25.251  20.029  1   47.11 ? 206 PHE   A O    1 
ATOM   1431 C  CB   . PHE   A 1 184 ? 87.696  26.971  20.94   1   46.42 ? 206 PHE   A CB   1 
ATOM   1432 C  CG   . PHE   A 1 184 ? 86.486  27.822  21.273  1   45.46 ? 206 PHE   A CG   1 
ATOM   1433 C  CD1  . PHE   A 1 184 ? 85.804  27.647  22.464  1   45.55 ? 206 PHE   A CD1  1 
ATOM   1434 C  CD2  . PHE   A 1 184 ? 85.985  28.735  20.356  1   45.47 ? 206 PHE   A CD2  1 
ATOM   1435 C  CE1  . PHE   A 1 184 ? 84.664  28.387  22.745  1   45.96 ? 206 PHE   A CE1  1 
ATOM   1436 C  CE2  . PHE   A 1 184 ? 84.846  29.471  20.637  1   45.93 ? 206 PHE   A CE2  1 
ATOM   1437 C  CZ   . PHE   A 1 184 ? 84.189  29.289  21.828  1   45.67 ? 206 PHE   A CZ   1 
ATOM   1438 N  N    . TRP   A 1 185 ? 86.334  25.871  18.282  1   47.15 ? 207 TRP   A N    1 
ATOM   1439 C  CA   . TRP   A 1 185 ? 85.2    26.001  17.369  1   48.27 ? 207 TRP   A CA   1 
ATOM   1440 C  C    . TRP   A 1 185 ? 84.328  24.753  17.267  1   49.73 ? 207 TRP   A C    1 
ATOM   1441 O  O    . TRP   A 1 185 ? 83.105  24.87   17.326  1   50.04 ? 207 TRP   A O    1 
ATOM   1442 C  CB   . TRP   A 1 185 ? 85.637  26.48   15.98   1   47.97 ? 207 TRP   A CB   1 
ATOM   1443 C  CG   . TRP   A 1 185 ? 84.57   27.212  15.214  1   48.79 ? 207 TRP   A CG   1 
ATOM   1444 C  CD1  . TRP   A 1 185 ? 84.052  26.864  14.003  1   49.64 ? 207 TRP   A CD1  1 
ATOM   1445 C  CD2  . TRP   A 1 185 ? 83.919  28.437  15.592  1   49.06 ? 207 TRP   A CD2  1 
ATOM   1446 N  NE1  . TRP   A 1 185 ? 83.125  27.794  13.599  1   49.97 ? 207 TRP   A NE1  1 
ATOM   1447 C  CE2  . TRP   A 1 185 ? 83.017  28.767  14.561  1   49.9  ? 207 TRP   A CE2  1 
ATOM   1448 C  CE3  . TRP   A 1 185 ? 84.011  29.288  16.705  1   49.51 ? 207 TRP   A CE3  1 
ATOM   1449 C  CZ2  . TRP   A 1 185 ? 82.219  29.914  14.605  1   50.53 ? 207 TRP   A CZ2  1 
ATOM   1450 C  CZ3  . TRP   A 1 185 ? 83.229  30.428  16.74   1   50.13 ? 207 TRP   A CZ3  1 
ATOM   1451 C  CH2  . TRP   A 1 185 ? 82.335  30.724  15.708  1   50.3  ? 207 TRP   A CH2  1 
ATOM   1452 N  N    . ALA   A 1 186 ? 84.942  23.567  17.161  1   50.27 ? 208 ALA   A N    1 
ATOM   1453 C  CA   . ALA   A 1 186 ? 84.186  22.32   17.058  1   50.82 ? 208 ALA   A CA   1 
ATOM   1454 C  C    . ALA   A 1 186 ? 83.472  22.006  18.357  1   51.13 ? 208 ALA   A C    1 
ATOM   1455 O  O    . ALA   A 1 186 ? 82.29   21.66   18.324  1   52.17 ? 208 ALA   A O    1 
ATOM   1456 C  CB   . ALA   A 1 186 ? 85.102  21.173  16.662  1   51.11 ? 208 ALA   A CB   1 
ATOM   1457 N  N    . LYS   A 1 187 ? 84.153  22.181  19.508  1   50.31 ? 209 LYS   A N    1 
ATOM   1458 C  CA   . LYS   A 1 187 ? 83.539  21.93   20.816  1   49.92 ? 209 LYS   A CA   1 
ATOM   1459 C  C    . LYS   A 1 187 ? 82.331  22.845  21.035  1   49.87 ? 209 LYS   A C    1 
ATOM   1460 O  O    . LYS   A 1 187 ? 81.308  22.409  21.572  1   51.03 ? 209 LYS   A O    1 
ATOM   1461 C  CB   . LYS   A 1 187 ? 84.546  22.154  21.948  1   51.02 ? 209 LYS   A CB   1 
ATOM   1462 C  CG   . LYS   A 1 187 ? 85.771  21.278  21.901  1   54.18 ? 209 LYS   A CG   1 
ATOM   1463 C  CD   . LYS   A 1 187 ? 86.64   21.558  23.113  1   57.5  ? 209 LYS   A CD   1 
ATOM   1464 C  CE   . LYS   A 1 187 ? 87.779  20.585  23.229  1   60.61 ? 209 LYS   A CE   1 
ATOM   1465 N  NZ   . LYS   A 1 187 ? 88.832  21.103  24.143  1   62.68 ? 209 LYS   A NZ   1 
ATOM   1466 N  N    . PHE   A 1 188 ? 82.46   24.115  20.616  1   48.18 ? 210 PHE   A N    1 
ATOM   1467 C  CA   . PHE   A 1 188 ? 81.43   25.14   20.721  1   46.44 ? 210 PHE   A CA   1 
ATOM   1468 C  C    . PHE   A 1 188 ? 80.19   24.694  19.936  1   46.41 ? 210 PHE   A C    1 
ATOM   1469 O  O    . PHE   A 1 188 ? 79.098  24.714  20.497  1   46.12 ? 210 PHE   A O    1 
ATOM   1470 C  CB   . PHE   A 1 188 ? 82.01   26.495  20.243  1   44.75 ? 210 PHE   A CB   1 
ATOM   1471 C  CG   . PHE   A 1 188 ? 81.084  27.684  20.125  1   43.47 ? 210 PHE   A CG   1 
ATOM   1472 C  CD1  . PHE   A 1 188 ? 80.02   27.847  20.996  1   43.06 ? 210 PHE   A CD1  1 
ATOM   1473 C  CD2  . PHE   A 1 188 ? 81.311  28.665  19.177  1   43.25 ? 210 PHE   A CD2  1 
ATOM   1474 C  CE1  . PHE   A 1 188 ? 79.153  28.919  20.855  1   43.47 ? 210 PHE   A CE1  1 
ATOM   1475 C  CE2  . PHE   A 1 188 ? 80.461  29.751  19.06   1   43.27 ? 210 PHE   A CE2  1 
ATOM   1476 C  CZ   . PHE   A 1 188 ? 79.391  29.875  19.902  1   43.04 ? 210 PHE   A CZ   1 
ATOM   1477 N  N    . GLN   A 1 189 ? 80.366  24.191  18.695  1   46.68 ? 211 GLN   A N    1 
ATOM   1478 C  CA   . GLN   A 1 189 ? 79.242  23.691  17.884  1   47.49 ? 211 GLN   A CA   1 
ATOM   1479 C  C    . GLN   A 1 189 ? 78.492  22.55   18.566  1   47.6  ? 211 GLN   A C    1 
ATOM   1480 O  O    . GLN   A 1 189 ? 77.259  22.565  18.603  1   47.55 ? 211 GLN   A O    1 
ATOM   1481 C  CB   . GLN   A 1 189 ? 79.695  23.273  16.478  1   49.69 ? 211 GLN   A CB   1 
ATOM   1482 C  CG   . GLN   A 1 189 ? 80.44   24.382  15.768  1   54.76 ? 211 GLN   A CG   1 
ATOM   1483 C  CD   . GLN   A 1 189 ? 80.741  24.088  14.322  1   60.04 ? 211 GLN   A CD   1 
ATOM   1484 O  OE1  . GLN   A 1 189 ? 81.895  24.178  13.876  1   61.38 ? 211 GLN   A OE1  1 
ATOM   1485 N  NE2  . GLN   A 1 189 ? 79.708  23.747  13.558  1   60.55 ? 211 GLN   A NE2  1 
ATOM   1486 N  N    . GLU   A 1 190 ? 79.235  21.6    19.157  1   47.72 ? 212 GLU   A N    1 
ATOM   1487 C  CA   . GLU   A 1 190 ? 78.65   20.466  19.872  1   48.15 ? 212 GLU   A CA   1 
ATOM   1488 C  C    . GLU   A 1 190 ? 77.901  20.941  21.111  1   48.45 ? 212 GLU   A C    1 
ATOM   1489 O  O    . GLU   A 1 190 ? 76.804  20.457  21.386  1   48.65 ? 212 GLU   A O    1 
ATOM   1490 C  CB   . GLU   A 1 190 ? 79.74   19.449  20.254  1   50.35 ? 212 GLU   A CB   1 
ATOM   1491 N  N    . SER   A 1 191 ? 78.482  21.915  21.849  1   48.25 ? 213 SER   A N    1 
ATOM   1492 C  CA   . SER   A 1 191 ? 77.866  22.493  23.048  1   47.87 ? 213 SER   A CA   1 
ATOM   1493 C  C    . SER   A 1 191 ? 76.572  23.18   22.696  1   47.13 ? 213 SER   A C    1 
ATOM   1494 O  O    . SER   A 1 191 ? 75.614  23.078  23.449  1   47.4  ? 213 SER   A O    1 
ATOM   1495 C  CB   . SER   A 1 191 ? 78.806  23.488  23.721  1   49.83 ? 213 SER   A CB   1 
ATOM   1496 O  OG   . SER   A 1 191 ? 79.814  22.834  24.474  1   52.85 ? 213 SER   A OG   1 
ATOM   1497 N  N    . VAL   A 1 192 ? 76.531  23.883  21.558  1   46.38 ? 214 VAL   A N    1 
ATOM   1498 C  CA   . VAL   A 1 192 ? 75.316  24.55   21.101  1   46.37 ? 214 VAL   A CA   1 
ATOM   1499 C  C    . VAL   A 1 192 ? 74.223  23.511  20.795  1   46.78 ? 214 VAL   A C    1 
ATOM   1500 O  O    . VAL   A 1 192 ? 73.083  23.69   21.208  1   46.74 ? 214 VAL   A O    1 
ATOM   1501 C  CB   . VAL   A 1 192 ? 75.595  25.481  19.897  1   46.24 ? 214 VAL   A CB   1 
ATOM   1502 C  CG1  . VAL   A 1 192 ? 74.3    25.9    19.21   1   46.31 ? 214 VAL   A CG1  1 
ATOM   1503 C  CG2  . VAL   A 1 192 ? 76.399  26.704  20.336  1   46.24 ? 214 VAL   A CG2  1 
ATOM   1504 N  N    . ASP   A 1 193 ? 74.575  22.412  20.111  1   47.12 ? 215 ASP   A N    1 
ATOM   1505 C  CA   . ASP   A 1 193 ? 73.606  21.348  19.813  1   47.78 ? 215 ASP   A CA   1 
ATOM   1506 C  C    . ASP   A 1 193 ? 73.087  20.73   21.096  1   47.51 ? 215 ASP   A C    1 
ATOM   1507 O  O    . ASP   A 1 193 ? 71.88   20.693  21.287  1   48.2  ? 215 ASP   A O    1 
ATOM   1508 C  CB   . ASP   A 1 193 ? 74.214  20.272  18.906  1   50.49 ? 215 ASP   A CB   1 
ATOM   1509 C  CG   . ASP   A 1 193 ? 74.471  20.744  17.491  1   57.99 ? 215 ASP   A CG   1 
ATOM   1510 O  OD1  . ASP   A 1 193 ? 73.685  21.594  16.992  1   59.79 ? 215 ASP   A OD1  1 
ATOM   1511 O  OD2  . ASP   A 1 193 ? 75.458  20.268  16.875  1   60.7  ? 215 ASP   A OD2  1 
ATOM   1512 N  N    . ARG   A 1 194 ? 73.978  20.359  22.025  1   46.46 ? 216 ARG   A N    1 
ATOM   1513 C  CA   . ARG   A 1 194 ? 73.574  19.776  23.294  1   46.19 ? 216 ARG   A CA   1 
ATOM   1514 C  C    . ARG   A 1 194 ? 72.694  20.721  24.096  1   45.91 ? 216 ARG   A C    1 
ATOM   1515 O  O    . ARG   A 1 194 ? 71.645  20.313  24.593  1   46.52 ? 216 ARG   A O    1 
ATOM   1516 C  CB   . ARG   A 1 194 ? 74.807  19.33   24.106  1   47.59 ? 216 ARG   A CB   1 
ATOM   1517 N  N    . PHE   A 1 195 ? 73.09   22.002  24.177  1   45.04 ? 217 PHE   A N    1 
ATOM   1518 C  CA   . PHE   A 1 195 ? 72.35   23.036  24.902  1   44.19 ? 217 PHE   A CA   1 
ATOM   1519 C  C    . PHE   A 1 195 ? 70.96   23.277  24.285  1   44.62 ? 217 PHE   A C    1 
ATOM   1520 O  O    . PHE   A 1 195 ? 69.969  23.274  25      1   44.08 ? 217 PHE   A O    1 
ATOM   1521 C  CB   . PHE   A 1 195 ? 73.179  24.344  24.981  1   43.06 ? 217 PHE   A CB   1 
ATOM   1522 C  CG   . PHE   A 1 195 ? 72.423  25.52   25.546  1   42.29 ? 217 PHE   A CG   1 
ATOM   1523 C  CD1  . PHE   A 1 195 ? 72.155  25.605  26.9    1   42    ? 217 PHE   A CD1  1 
ATOM   1524 C  CD2  . PHE   A 1 195 ? 71.939  26.518  24.713  1   42.45 ? 217 PHE   A CD2  1 
ATOM   1525 C  CE1  . PHE   A 1 195 ? 71.415  26.66   27.411  1   42.18 ? 217 PHE   A CE1  1 
ATOM   1526 C  CE2  . PHE   A 1 195 ? 71.21   27.579  25.232  1   42.48 ? 217 PHE   A CE2  1 
ATOM   1527 C  CZ   . PHE   A 1 195 ? 70.961  27.646  26.577  1   41.99 ? 217 PHE   A CZ   1 
ATOM   1528 N  N    . LEU   A 1 196 ? 70.89   23.479  22.972  1   45.93 ? 218 LEU   A N    1 
ATOM   1529 C  CA   . LEU   A 1 196 ? 69.62   23.712  22.287  1   48.21 ? 218 LEU   A CA   1 
ATOM   1530 C  C    . LEU   A 1 196 ? 68.686  22.483  22.31   1   49.68 ? 218 LEU   A C    1 
ATOM   1531 O  O    . LEU   A 1 196 ? 67.476  22.658  22.479  1   49.82 ? 218 LEU   A O    1 
ATOM   1532 C  CB   . LEU   A 1 196 ? 69.838  24.239  20.846  1   48.57 ? 218 LEU   A CB   1 
ATOM   1533 C  CG   . LEU   A 1 196 ? 70.392  25.682  20.721  1   49.46 ? 218 LEU   A CG   1 
ATOM   1534 C  CD1  . LEU   A 1 196 ? 70.522  26.096  19.266  1   49.88 ? 218 LEU   A CD1  1 
ATOM   1535 C  CD2  . LEU   A 1 196 ? 69.529  26.679  21.462  1   49.56 ? 218 LEU   A CD2  1 
ATOM   1536 N  N    . GLU   A 1 197 ? 69.248  21.252  22.229  1   50.48 ? 219 GLU   A N    1 
ATOM   1537 C  CA   . GLU   A 1 197 ? 68.463  19.999  22.295  1   51.83 ? 219 GLU   A CA   1 
ATOM   1538 C  C    . GLU   A 1 197 ? 67.776  19.903  23.656  1   52.4  ? 219 GLU   A C    1 
ATOM   1539 O  O    . GLU   A 1 197 ? 66.595  19.565  23.733  1   52.79 ? 219 GLU   A O    1 
ATOM   1540 C  CB   . GLU   A 1 197 ? 69.353  18.752  22.066  1   54.85 ? 219 GLU   A CB   1 
ATOM   1541 C  CG   . GLU   A 1 197 ? 69.75   18.491  20.619  1   61    ? 219 GLU   A CG   1 
ATOM   1542 C  CD   . GLU   A 1 197 ? 71.05   17.719  20.434  1   69.25 ? 219 GLU   A CD   1 
ATOM   1543 O  OE1  . GLU   A 1 197 ? 71.567  17.167  21.434  1   70.36 ? 219 GLU   A OE1  1 
ATOM   1544 O  OE2  . GLU   A 1 197 ? 71.567  17.691  19.292  1   71.81 ? 219 GLU   A OE2  1 
ATOM   1545 N  N    . ALA   A 1 198 ? 68.507  20.257  24.725  1   52.46 ? 220 ALA   A N    1 
ATOM   1546 C  CA   . ALA   A 1 198 ? 67.978  20.281  26.083  1   53.04 ? 220 ALA   A CA   1 
ATOM   1547 C  C    . ALA   A 1 198 ? 66.902  21.352  26.225  1   53.96 ? 220 ALA   A C    1 
ATOM   1548 O  O    . ALA   A 1 198 ? 65.921  21.139  26.928  1   54.77 ? 220 ALA   A O    1 
ATOM   1549 C  CB   . ALA   A 1 198 ? 69.103  20.536  27.073  1   53.07 ? 220 ALA   A CB   1 
ATOM   1550 N  N    . GLN   A 1 199 ? 67.075  22.505  25.555  1   54.07 ? 221 GLN   A N    1 
ATOM   1551 C  CA   . GLN   A 1 199 ? 66.091  23.586  25.591  1   54.45 ? 221 GLN   A CA   1 
ATOM   1552 C  C    . GLN   A 1 199 ? 64.779  23.116  24.948  1   55.21 ? 221 GLN   A C    1 
ATOM   1553 O  O    . GLN   A 1 199 ? 63.706  23.466  25.443  1   54.94 ? 221 GLN   A O    1 
ATOM   1554 C  CB   . GLN   A 1 199 ? 66.615  24.85   24.878  1   54.93 ? 221 GLN   A CB   1 
ATOM   1555 C  CG   . GLN   A 1 199 ? 67.696  25.623  25.631  1   56.41 ? 221 GLN   A CG   1 
ATOM   1556 C  CD   . GLN   A 1 199 ? 67.242  26.056  26.994  1   59.92 ? 221 GLN   A CD   1 
ATOM   1557 O  OE1  . GLN   A 1 199 ? 67.852  25.699  28.012  1   62.09 ? 221 GLN   A OE1  1 
ATOM   1558 N  NE2  . GLN   A 1 199 ? 66.156  26.827  27.048  1   59.24 ? 221 GLN   A NE2  1 
ATOM   1559 N  N    . VAL   A 1 200 ? 64.865  22.329  23.849  1   55.86 ? 222 VAL   A N    1 
ATOM   1560 C  CA   . VAL   A 1 200 ? 63.688  21.782  23.17   1   57.06 ? 222 VAL   A CA   1 
ATOM   1561 C  C    . VAL   A 1 200 ? 62.947  20.789  24.084  1   57.67 ? 222 VAL   A C    1 
ATOM   1562 O  O    . VAL   A 1 200 ? 61.73   20.893  24.235  1   57.84 ? 222 VAL   A O    1 
ATOM   1563 C  CB   . VAL   A 1 200 ? 64.049  21.157  21.802  1   58.4  ? 222 VAL   A CB   1 
ATOM   1564 C  CG1  . VAL   A 1 200 ? 62.881  20.344  21.233  1   59.05 ? 222 VAL   A CG1  1 
ATOM   1565 C  CG2  . VAL   A 1 200 ? 64.473  22.237  20.817  1   59.15 ? 222 VAL   A CG2  1 
ATOM   1566 N  N    . GLN   A 1 201 ? 63.692  19.891  24.75   1   57.81 ? 223 GLN   A N    1 
ATOM   1567 C  CA   . GLN   A 1 201 ? 63.127  18.915  25.683  1   58.53 ? 223 GLN   A CA   1 
ATOM   1568 C  C    . GLN   A 1 201 ? 62.462  19.592  26.882  1   59.05 ? 223 GLN   A C    1 
ATOM   1569 O  O    . GLN   A 1 201 ? 61.425  19.132  27.352  1   59.5  ? 223 GLN   A O    1 
ATOM   1570 C  CB   . GLN   A 1 201 ? 64.201  17.915  26.145  1   60.1  ? 223 GLN   A CB   1 
ATOM   1571 C  CG   . GLN   A 1 201 ? 64.674  16.982  25.036  1   62.97 ? 223 GLN   A CG   1 
ATOM   1572 N  N    . SER   A 1 202 ? 63.03   20.702  27.35   1   59.1  ? 224 SER   A N    1 
ATOM   1573 C  CA   . SER   A 1 202 ? 62.474  21.454  28.472  1   59.54 ? 224 SER   A CA   1 
ATOM   1574 C  C    . SER   A 1 202 ? 61.222  22.239  28.053  1   60.28 ? 224 SER   A C    1 
ATOM   1575 O  O    . SER   A 1 202 ? 60.294  22.381  28.848  1   60.35 ? 224 SER   A O    1 
ATOM   1576 C  CB   . SER   A 1 202 ? 63.531  22.392  29.052  1   60.26 ? 224 SER   A CB   1 
ATOM   1577 O  OG   . SER   A 1 202 ? 62.975  23.343  29.947  1   62.25 ? 224 SER   A OG   1 
ATOM   1578 N  N    . ALA   A 1 203 ? 61.205  22.754  26.812  1   60.71 ? 225 ALA   A N    1 
ATOM   1579 C  CA   . ALA   A 1 203 ? 60.082  23.526  26.269  1   61.35 ? 225 ALA   A CA   1 
ATOM   1580 C  C    . ALA   A 1 203 ? 58.821  22.673  26.128  1   61.89 ? 225 ALA   A C    1 
ATOM   1581 O  O    . ALA   A 1 203 ? 57.72   23.185  26.289  1   61.68 ? 225 ALA   A O    1 
ATOM   1582 C  CB   . ALA   A 1 203 ? 60.457  24.13   24.918  1   61.24 ? 225 ALA   A CB   1 
ATOM   1583 N  N    . MET   A 1 204 ? 58.983  21.382  25.826  1   62.53 ? 226 MET   A N    1 
ATOM   1584 C  CA   . MET   A 1 204 ? 57.866  20.455  25.67   1   63.77 ? 226 MET   A CA   1 
ATOM   1585 C  C    . MET   A 1 204 ? 57.079  20.26   26.976  1   65.24 ? 226 MET   A C    1 
ATOM   1586 O  O    . MET   A 1 204 ? 55.857  20.098  26.949  1   65.96 ? 226 MET   A O    1 
ATOM   1587 C  CB   . MET   A 1 204 ? 58.357  19.102  25.114  1   63.94 ? 226 MET   A CB   1 
ATOM   1588 C  CG   . MET   A 1 204 ? 58.985  19.187  23.724  1   65.72 ? 226 MET   A CG   1 
ATOM   1589 S  SD   . MET   A 1 204 ? 57.99   20.044  22.463  1   71.5  ? 226 MET   A SD   1 
ATOM   1590 C  CE   . MET   A 1 204 ? 58.873  19.562  20.947  1   67.99 ? 226 MET   A CE   1 
ATOM   1591 N  N    . GLU   A 1 205 ? 57.76   20.339  28.115  1   65.62 ? 227 GLU   A N    1 
ATOM   1592 C  CA   . GLU   A 1 205 ? 57.124  20.139  29.412  1   66.65 ? 227 GLU   A CA   1 
ATOM   1593 C  C    . GLU   A 1 205 ? 56.313  21.354  29.933  1   67.42 ? 227 GLU   A C    1 
ATOM   1594 O  O    . GLU   A 1 205 ? 55.7    21.268  31.003  1   67.36 ? 227 GLU   A O    1 
ATOM   1595 C  CB   . GLU   A 1 205 ? 58.181  19.692  30.437  1   69    ? 227 GLU   A CB   1 
ATOM   1596 C  CG   . GLU   A 1 205 ? 58.955  18.459  29.988  1   73.11 ? 227 GLU   A CG   1 
ATOM   1597 N  N    . GLU   A 1 206 ? 56.296  22.471  29.186  1   67.77 ? 228 GLU   A N    1 
ATOM   1598 C  CA   . GLU   A 1 206 ? 55.576  23.683  29.593  1   68.47 ? 228 GLU   A CA   1 
ATOM   1599 C  C    . GLU   A 1 206 ? 54.063  23.458  29.779  1   68.83 ? 228 GLU   A C    1 
ATOM   1600 O  O    . GLU   A 1 206 ? 53.422  22.78   28.969  1   69.15 ? 228 GLU   A O    1 
ATOM   1601 C  CB   . GLU   A 1 206 ? 55.84   24.818  28.596  1   71.01 ? 228 GLU   A CB   1 
ATOM   1602 C  CG   . GLU   A 1 206 ? 57.245  25.389  28.682  1   76.25 ? 228 GLU   A CG   1 
ATOM   1603 C  CD   . GLU   A 1 206 ? 57.444  26.44   29.759  1   83.52 ? 228 GLU   A CD   1 
ATOM   1604 O  OE1  . GLU   A 1 206 ? 56.434  26.921  30.323  1   85.22 ? 228 GLU   A OE1  1 
ATOM   1605 O  OE2  . GLU   A 1 206 ? 58.614  26.793  30.03   1   85.65 ? 228 GLU   A OE2  1 
ATOM   1606 N  N    . PRO   A 1 207 ? 53.481  24.002  30.863  1   68.46 ? 229 PRO   A N    1 
ATOM   1607 C  CA   . PRO   A 1 207 ? 52.048  23.782  31.108  1   68.28 ? 229 PRO   A CA   1 
ATOM   1608 C  C    . PRO   A 1 207 ? 51.16   24.536  30.121  1   68.09 ? 229 PRO   A C    1 
ATOM   1609 O  O    . PRO   A 1 207 ? 50.289  23.924  29.502  1   68.56 ? 229 PRO   A O    1 
ATOM   1610 C  CB   . PRO   A 1 207 ? 51.848  24.239  32.567  1   68.9  ? 229 PRO   A CB   1 
ATOM   1611 C  CG   . PRO   A 1 207 ? 53.224  24.513  33.108  1   69.27 ? 229 PRO   A CG   1 
ATOM   1612 C  CD   . PRO   A 1 207 ? 54.093  24.811  31.931  1   67.82 ? 229 PRO   A CD   1 
ATOM   1613 N  N    . VAL   A 1 208 ? 51.395  25.846  29.944  1   67.09 ? 230 VAL   A N    1 
ATOM   1614 C  CA   . VAL   A 1 208 ? 50.614  26.626  28.992  1   66.64 ? 230 VAL   A CA   1 
ATOM   1615 C  C    . VAL   A 1 208 ? 51.129  26.349  27.58   1   65.74 ? 230 VAL   A C    1 
ATOM   1616 O  O    . VAL   A 1 208 ? 52.341  26.314  27.368  1   66.03 ? 230 VAL   A O    1 
ATOM   1617 C  CB   . VAL   A 1 208 ? 50.644  28.131  29.331  1   67.59 ? 230 VAL   A CB   1 
ATOM   1618 N  N    . GLU   A 1 209 ? 50.219  26.109  26.619  1   64.35 ? 231 GLU   A N    1 
ATOM   1619 C  CA   . GLU   A 1 209 ? 50.627  25.808  25.247  1   63.14 ? 231 GLU   A CA   1 
ATOM   1620 C  C    . GLU   A 1 209 ? 51.183  27.035  24.501  1   61.22 ? 231 GLU   A C    1 
ATOM   1621 O  O    . GLU   A 1 209 ? 52.04   26.886  23.636  1   61.29 ? 231 GLU   A O    1 
ATOM   1622 C  CB   . GLU   A 1 209 ? 49.498  25.128  24.465  1   65.42 ? 231 GLU   A CB   1 
ATOM   1623 C  CG   . GLU   A 1 209 ? 49.797  23.674  24.142  1   70.5  ? 231 GLU   A CG   1 
ATOM   1624 C  CD   . GLU   A 1 209 ? 50.282  23.447  22.722  1   77.12 ? 231 GLU   A CD   1 
ATOM   1625 O  OE1  . GLU   A 1 209 ? 49.911  24.251  21.835  1   78.66 ? 231 GLU   A OE1  1 
ATOM   1626 O  OE2  . GLU   A 1 209 ? 51.024  22.464  22.494  1   78.55 ? 231 GLU   A OE2  1 
ATOM   1627 N  N    . LYS   A 1 210 ? 50.729  28.234  24.857  1   59.36 ? 232 LYS   A N    1 
ATOM   1628 C  CA   . LYS   A 1 210 ? 51.229  29.464  24.254  1   58.54 ? 232 LYS   A CA   1 
ATOM   1629 C  C    . LYS   A 1 210 ? 52.708  29.691  24.668  1   57.49 ? 232 LYS   A C    1 
ATOM   1630 O  O    . LYS   A 1 210 ? 53.511  30.144  23.856  1   57.43 ? 232 LYS   A O    1 
ATOM   1631 C  CB   . LYS   A 1 210 ? 50.348  30.648  24.684  1   60.25 ? 232 LYS   A CB   1 
ATOM   1632 C  CG   . LYS   A 1 210 ? 50.707  31.963  24.022  1   64.61 ? 232 LYS   A CG   1 
ATOM   1633 C  CD   . LYS   A 1 210 ? 49.838  33.101  24.533  1   69.07 ? 232 LYS   A CD   1 
ATOM   1634 C  CE   . LYS   A 1 210 ? 50.144  34.386  23.815  1   73.22 ? 232 LYS   A CE   1 
ATOM   1635 N  NZ   . LYS   A 1 210 ? 49.283  35.499  24.291  1   76.25 ? 232 LYS   A NZ   1 
ATOM   1636 N  N    . ALA   A 1 211 ? 53.067  29.337  25.919  1   56.33 ? 233 ALA   A N    1 
ATOM   1637 C  CA   . ALA   A 1 211 ? 54.437  29.443  26.435  1   55.41 ? 233 ALA   A CA   1 
ATOM   1638 C  C    . ALA   A 1 211 ? 55.36   28.377  25.812  1   53.66 ? 233 ALA   A C    1 
ATOM   1639 O  O    . ALA   A 1 211 ? 56.536  28.647  25.582  1   53.69 ? 233 ALA   A O    1 
ATOM   1640 C  CB   . ALA   A 1 211 ? 54.443  29.312  27.951  1   55.68 ? 233 ALA   A CB   1 
ATOM   1641 N  N    . LYS   A 1 212 ? 54.835  27.178  25.542  1   52.09 ? 234 LYS   A N    1 
ATOM   1642 C  CA   . LYS   A 1 212 ? 55.608  26.107  24.908  1   51.78 ? 234 LYS   A CA   1 
ATOM   1643 C  C    . LYS   A 1 212 ? 56      26.505  23.474  1   51.64 ? 234 LYS   A C    1 
ATOM   1644 O  O    . LYS   A 1 212 ? 57.117  26.241  23.028  1   51.61 ? 234 LYS   A O    1 
ATOM   1645 C  CB   . LYS   A 1 212 ? 54.779  24.805  24.884  1   53.3  ? 234 LYS   A CB   1 
ATOM   1646 C  CG   . LYS   A 1 212 ? 55.367  23.673  24.034  1   56.11 ? 234 LYS   A CG   1 
ATOM   1647 C  CD   . LYS   A 1 212 ? 54.29   22.728  23.522  1   59.74 ? 234 LYS   A CD   1 
ATOM   1648 N  N    . ASN   A 1 213 ? 55.07   27.148  22.758  1   51.21 ? 235 ASN   A N    1 
ATOM   1649 C  CA   . ASN   A 1 213 ? 55.286  27.572  21.385  1   50.94 ? 235 ASN   A CA   1 
ATOM   1650 C  C    . ASN   A 1 213 ? 56.234  28.752  21.289  1   50.14 ? 235 ASN   A C    1 
ATOM   1651 O  O    . ASN   A 1 213 ? 57.031  28.799  20.356  1   50.5  ? 235 ASN   A O    1 
ATOM   1652 C  CB   . ASN   A 1 213 ? 53.952  27.863  20.696  1   52.32 ? 235 ASN   A CB   1 
ATOM   1653 C  CG   . ASN   A 1 213 ? 53.078  26.637  20.518  1   55.31 ? 235 ASN   A CG   1 
ATOM   1654 O  OD1  . ASN   A 1 213 ? 53.554  25.513  20.255  1   55.28 ? 235 ASN   A OD1  1 
ATOM   1655 N  ND2  . ASN   A 1 213 ? 51.772  26.842  20.672  1   56.2  ? 235 ASN   A ND2  1 
ATOM   1656 N  N    . TYR   A 1 214 ? 56.186  29.689  22.252  1   49.51 ? 236 TYR   A N    1 
ATOM   1657 C  CA   . TYR   A 1 214 ? 57.108  30.838  22.253  1   49.38 ? 236 TYR   A CA   1 
ATOM   1658 C  C    . TYR   A 1 214 ? 58.549  30.365  22.382  1   48.24 ? 236 TYR   A C    1 
ATOM   1659 O  O    . TYR   A 1 214 ? 59.411  30.844  21.655  1   48.24 ? 236 TYR   A O    1 
ATOM   1660 C  CB   . TYR   A 1 214 ? 56.784  31.836  23.369  1   50.11 ? 236 TYR   A CB   1 
ATOM   1661 C  CG   . TYR   A 1 214 ? 57.589  33.116  23.279  1   51.92 ? 236 TYR   A CG   1 
ATOM   1662 C  CD1  . TYR   A 1 214 ? 58.801  33.25   23.945  1   53.15 ? 236 TYR   A CD1  1 
ATOM   1663 C  CD2  . TYR   A 1 214 ? 57.127  34.2    22.546  1   53.4  ? 236 TYR   A CD2  1 
ATOM   1664 C  CE1  . TYR   A 1 214 ? 59.552  34.417  23.849  1   54.4  ? 236 TYR   A CE1  1 
ATOM   1665 C  CE2  . TYR   A 1 214 ? 57.862  35.378  22.457  1   54.48 ? 236 TYR   A CE2  1 
ATOM   1666 C  CZ   . TYR   A 1 214 ? 59.075  35.482  23.109  1   55.54 ? 236 TYR   A CZ   1 
ATOM   1667 O  OH   . TYR   A 1 214 ? 59.796  36.65   23.02   1   57.88 ? 236 TYR   A OH   1 
ATOM   1668 N  N    . ARG   A 1 215 ? 58.797  29.392  23.268  1   47.28 ? 237 ARG   A N    1 
ATOM   1669 C  CA   . ARG   A 1 215 ? 60.117  28.807  23.481  1   46.63 ? 237 ARG   A CA   1 
ATOM   1670 C  C    . ARG   A 1 215 ? 60.601  28.049  22.272  1   46.45 ? 237 ARG   A C    1 
ATOM   1671 O  O    . ARG   A 1 215 ? 61.763  28.192  21.921  1   46.94 ? 237 ARG   A O    1 
ATOM   1672 C  CB   . ARG   A 1 215 ? 60.134  27.915  24.717  1   47.14 ? 237 ARG   A CB   1 
ATOM   1673 C  CG   . ARG   A 1 215 ? 60.026  28.712  26.007  1   49.16 ? 237 ARG   A CG   1 
ATOM   1674 C  CD   . ARG   A 1 215 ? 60.258  27.85   27.222  1   51.65 ? 237 ARG   A CD   1 
ATOM   1675 N  NE   . ARG   A 1 215 ? 61.527  27.124  27.163  1   53.32 ? 237 ARG   A NE   1 
ATOM   1676 C  CZ   . ARG   A 1 215 ? 61.955  26.286  28.104  1   54.57 ? 237 ARG   A CZ   1 
ATOM   1677 N  NH1  . ARG   A 1 215 ? 61.216  26.057  29.185  1   52.41 ? 237 ARG   A NH1  1 
ATOM   1678 N  NH2  . ARG   A 1 215 ? 63.122  25.671  27.97   1   54.8  ? 237 ARG   A NH2  1 
ATOM   1679 N  N    . LEU   A 1 216 ? 59.729  27.281  21.597  1   45.87 ? 238 LEU   A N    1 
ATOM   1680 C  CA   . LEU   A 1 216 ? 60.132  26.57   20.375  1   45.72 ? 238 LEU   A CA   1 
ATOM   1681 C  C    . LEU   A 1 216 ? 60.452  27.576  19.244  1   44.28 ? 238 LEU   A C    1 
ATOM   1682 O  O    . LEU   A 1 216 ? 61.372  27.354  18.46   1   43.82 ? 238 LEU   A O    1 
ATOM   1683 C  CB   . LEU   A 1 216 ? 59.038  25.589  19.917  1   46.63 ? 238 LEU   A CB   1 
ATOM   1684 C  CG   . LEU   A 1 216 ? 58.718  24.412  20.848  1   48.84 ? 238 LEU   A CG   1 
ATOM   1685 C  CD1  . LEU   A 1 216 ? 57.637  23.525  20.23   1   49.48 ? 238 LEU   A CD1  1 
ATOM   1686 C  CD2  . LEU   A 1 216 ? 59.983  23.592  21.207  1   48.96 ? 238 LEU   A CD2  1 
ATOM   1687 N  N    . MET   A 1 217 ? 59.704  28.688  19.189  1   43.46 ? 239 MET   A N    1 
ATOM   1688 C  CA   . MET   A 1 217 ? 59.948  29.736  18.207  1   43.87 ? 239 MET   A CA   1 
ATOM   1689 C  C    . MET   A 1 217 ? 61.307  30.41   18.518  1   43.99 ? 239 MET   A C    1 
ATOM   1690 O  O    . MET   A 1 217 ? 62.106  30.653  17.615  1   44.08 ? 239 MET   A O    1 
ATOM   1691 C  CB   . MET   A 1 217 ? 58.788  30.76   18.228  1   44.12 ? 239 MET   A CB   1 
ATOM   1692 C  CG   . MET   A 1 217 ? 59.011  31.971  17.33   1   45.43 ? 239 MET   A CG   1 
ATOM   1693 S  SD   . MET   A 1 217 ? 60.024  33.3    18.076  1   46.32 ? 239 MET   A SD   1 
ATOM   1694 C  CE   . MET   A 1 217 ? 59.014  33.747  19.424  1   37.49 ? 239 MET   A CE   1 
ATOM   1695 N  N    . ASP   A 1 218 ? 61.569  30.674  19.805  1   43.62 ? 240 ASP   A N    1 
ATOM   1696 C  CA   . ASP   A 1 218 ? 62.815  31.284  20.245  1   43.69 ? 240 ASP   A CA   1 
ATOM   1697 C  C    . ASP   A 1 218 ? 64.014  30.401  19.959  1   43.36 ? 240 ASP   A C    1 
ATOM   1698 O  O    . ASP   A 1 218 ? 65.037  30.911  19.493  1   43.79 ? 240 ASP   A O    1 
ATOM   1699 C  CB   . ASP   A 1 218 ? 62.761  31.67   21.726  1   45.56 ? 240 ASP   A CB   1 
ATOM   1700 C  CG   . ASP   A 1 218 ? 64.018  32.38   22.182  1   49.19 ? 240 ASP   A CG   1 
ATOM   1701 O  OD1  . ASP   A 1 218 ? 64.33   33.445  21.622  1   49.71 ? 240 ASP   A OD1  1 
ATOM   1702 O  OD2  . ASP   A 1 218 ? 64.707  31.852  23.083  1   51.23 ? 240 ASP   A OD2  1 
ATOM   1703 N  N    . ILE   A 1 219 ? 63.894  29.083  20.194  1   42.63 ? 241 ILE   A N    1 
ATOM   1704 C  CA   . ILE   A 1 219 ? 64.97   28.129  19.916  1   42.35 ? 241 ILE   A CA   1 
ATOM   1705 C  C    . ILE   A 1 219 ? 65.318  28.124  18.417  1   42.18 ? 241 ILE   A C    1 
ATOM   1706 O  O    . ILE   A 1 219 ? 66.496  28.031  18.062  1   42.55 ? 241 ILE   A O    1 
ATOM   1707 C  CB   . ILE   A 1 219 ? 64.611  26.72   20.452  1   43.13 ? 241 ILE   A CB   1 
ATOM   1708 C  CG1  . ILE   A 1 219 ? 64.514  26.727  21.981  1   44    ? 241 ILE   A CG1  1 
ATOM   1709 C  CG2  . ILE   A 1 219 ? 65.614  25.659  19.971  1   43.58 ? 241 ILE   A CG2  1 
ATOM   1710 C  CD1  . ILE   A 1 219 ? 63.8    25.567  22.538  1   44.98 ? 241 ILE   A CD1  1 
ATOM   1711 N  N    . GLU   A 1 220 ? 64.309  28.291  17.541  1   41.51 ? 242 GLU   A N    1 
ATOM   1712 C  CA   . GLU   A 1 220 ? 64.564  28.376  16.109  1   41.61 ? 242 GLU   A CA   1 
ATOM   1713 C  C    . GLU   A 1 220 ? 65.334  29.674  15.761  1   40.46 ? 242 GLU   A C    1 
ATOM   1714 O  O    . GLU   A 1 220 ? 66.277  29.624  14.972  1   40.37 ? 242 GLU   A O    1 
ATOM   1715 C  CB   . GLU   A 1 220 ? 63.269  28.237  15.289  1   44.37 ? 242 GLU   A CB   1 
ATOM   1716 C  CG   . GLU   A 1 220 ? 63.517  28.3    13.787  1   49.39 ? 242 GLU   A CG   1 
ATOM   1717 C  CD   . GLU   A 1 220 ? 64.502  27.3    13.194  1   56.3  ? 242 GLU   A CD   1 
ATOM   1718 O  OE1  . GLU   A 1 220 ? 64.699  26.217  13.794  1   57.29 ? 242 GLU   A OE1  1 
ATOM   1719 O  OE2  . GLU   A 1 220 ? 65.061  27.597  12.109  1   58.38 ? 242 GLU   A OE2  1 
ATOM   1720 N  N    . LYS   A 1 221 ? 64.999  30.807  16.424  1   39.28 ? 243 LYS   A N    1 
ATOM   1721 C  CA   . LYS   A 1 221 ? 65.732  32.074  16.264  1   38.64 ? 243 LYS   A CA   1 
ATOM   1722 C  C    . LYS   A 1 221 ? 67.212  31.87   16.631  1   38.32 ? 243 LYS   A C    1 
ATOM   1723 O  O    . LYS   A 1 221 ? 68.089  32.308  15.882  1   38.21 ? 243 LYS   A O    1 
ATOM   1724 C  CB   . LYS   A 1 221 ? 65.129  33.188  17.132  1   39.8  ? 243 LYS   A CB   1 
ATOM   1725 C  CG   . LYS   A 1 221 ? 63.765  33.71   16.675  1   43.63 ? 243 LYS   A CG   1 
ATOM   1726 C  CD   . LYS   A 1 221 ? 63.774  34.255  15.263  1   48.44 ? 243 LYS   A CD   1 
ATOM   1727 C  CE   . LYS   A 1 221 ? 62.721  35.311  15.014  1   53.25 ? 243 LYS   A CE   1 
ATOM   1728 N  NZ   . LYS   A 1 221 ? 61.344  34.843  15.292  1   56.19 ? 243 LYS   A NZ   1 
ATOM   1729 N  N    . ARG   A 1 222 ? 67.479  31.122  17.728  1   37.78 ? 244 ARG   A N    1 
ATOM   1730 C  CA   . ARG   A 1 222 ? 68.835  30.764  18.164  1   37.87 ? 244 ARG   A CA   1 
ATOM   1731 C  C    . ARG   A 1 222 ? 69.567  29.945  17.111  1   39.47 ? 244 ARG   A C    1 
ATOM   1732 O  O    . ARG   A 1 222 ? 70.717  30.242  16.806  1   40.25 ? 244 ARG   A O    1 
ATOM   1733 C  CB   . ARG   A 1 222 ? 68.823  29.993  19.506  1   37.44 ? 244 ARG   A CB   1 
ATOM   1734 C  CG   . ARG   A 1 222 ? 68.254  30.764  20.697  1   37.51 ? 244 ARG   A CG   1 
ATOM   1735 C  CD   . ARG   A 1 222 ? 68.912  32.126  20.887  1   37.44 ? 244 ARG   A CD   1 
ATOM   1736 N  NE   . ARG   A 1 222 ? 70.347  32.013  21.161  1   37.59 ? 244 ARG   A NE   1 
ATOM   1737 C  CZ   . ARG   A 1 222 ? 71.249  32.951  20.872  1   35.9  ? 244 ARG   A CZ   1 
ATOM   1738 N  NH1  . ARG   A 1 222 ? 70.881  34.075  20.265  1   32.7  ? 244 ARG   A NH1  1 
ATOM   1739 N  NH2  . ARG   A 1 222 ? 72.528  32.758  21.16   1   34.58 ? 244 ARG   A NH2  1 
ATOM   1740 N  N    . ARG   A 1 223 ? 68.899  28.954  16.51   1   40    ? 245 ARG   A N    1 
ATOM   1741 C  CA   . ARG   A 1 223 ? 69.502  28.121  15.46   1   40.76 ? 245 ARG   A CA   1 
ATOM   1742 C  C    . ARG   A 1 223 ? 69.91   28.954  14.253  1   40.68 ? 245 ARG   A C    1 
ATOM   1743 O  O    . ARG   A 1 223 ? 70.956  28.691  13.652  1   40.8  ? 245 ARG   A O    1 
ATOM   1744 C  CB   . ARG   A 1 223 ? 68.529  27.009  15.024  1   43.03 ? 245 ARG   A CB   1 
ATOM   1745 C  CG   . ARG   A 1 223 ? 68.189  26.03   16.123  1   47.13 ? 245 ARG   A CG   1 
ATOM   1746 C  CD   . ARG   A 1 223 ? 69.079  24.818  16.064  1   53.05 ? 245 ARG   A CD   1 
ATOM   1747 N  NE   . ARG   A 1 223 ? 68.586  23.752  16.941  1   58.28 ? 245 ARG   A NE   1 
ATOM   1748 C  CZ   . ARG   A 1 223 ? 69.351  22.807  17.476  1   60.67 ? 245 ARG   A CZ   1 
ATOM   1749 N  NH1  . ARG   A 1 223 ? 70.659  22.787  17.238  1   59.92 ? 245 ARG   A NH1  1 
ATOM   1750 N  NH2  . ARG   A 1 223 ? 68.818  21.883  18.269  1   61.33 ? 245 ARG   A NH2  1 
ATOM   1751 N  N    . GLU   A 1 224 ? 69.09   29.951  13.887  1   40.65 ? 246 GLU   A N    1 
ATOM   1752 C  CA   . GLU   A 1 224 ? 69.398  30.847  12.772  1   41.33 ? 246 GLU   A CA   1 
ATOM   1753 C  C    . GLU   A 1 224 ? 70.612  31.751  13.139  1   41.18 ? 246 GLU   A C    1 
ATOM   1754 O  O    . GLU   A 1 224 ? 71.458  32.025  12.282  1   42.13 ? 246 GLU   A O    1 
ATOM   1755 C  CB   . GLU   A 1 224 ? 68.173  31.69   12.404  1   45.88 ? 246 GLU   A CB   1 
ATOM   1756 C  CG   . GLU   A 1 224 ? 68.221  32.196  10.967  1   55.61 ? 246 GLU   A CG   1 
ATOM   1757 C  CD   . GLU   A 1 224 ? 68.14   31.109  9.911   1   64.24 ? 246 GLU   A CD   1 
ATOM   1758 O  OE1  . GLU   A 1 224 ? 68.888  31.183  8.907   1   66.41 ? 246 GLU   A OE1  1 
ATOM   1759 O  OE2  . GLU   A 1 224 ? 67.333  30.172  10.098  1   66.67 ? 246 GLU   A OE2  1 
ATOM   1760 N  N    . VAL   A 1 225 ? 70.732  32.152  14.425  1   39.51 ? 247 VAL   A N    1 
ATOM   1761 C  CA   . VAL   A 1 225 ? 71.881  32.924  14.909  1   38.57 ? 247 VAL   A CA   1 
ATOM   1762 C  C    . VAL   A 1 225 ? 73.154  32.085  14.751  1   37.7  ? 247 VAL   A C    1 
ATOM   1763 O  O    . VAL   A 1 225 ? 74.155  32.568  14.221  1   37.33 ? 247 VAL   A O    1 
ATOM   1764 C  CB   . VAL   A 1 225 ? 71.671  33.399  16.386  1   38.57 ? 247 VAL   A CB   1 
ATOM   1765 C  CG1  . VAL   A 1 225 ? 72.985  33.812  17.049  1   39.05 ? 247 VAL   A CG1  1 
ATOM   1766 C  CG2  . VAL   A 1 225 ? 70.673  34.535  16.446  1   38.29 ? 247 VAL   A CG2  1 
ATOM   1767 N  N    . TYR   A 1 226 ? 73.1    30.819  15.176  1   37.57 ? 248 TYR   A N    1 
ATOM   1768 C  CA   . TYR   A 1 226 ? 74.258  29.942  15.094  1   38.31 ? 248 TYR   A CA   1 
ATOM   1769 C  C    . TYR   A 1 226 ? 74.603  29.534  13.667  1   40.14 ? 248 TYR   A C    1 
ATOM   1770 O  O    . TYR   A 1 226 ? 75.781  29.321  13.384  1   40.86 ? 248 TYR   A O    1 
ATOM   1771 C  CB   . TYR   A 1 226 ? 74.112  28.745  16.028  1   37.98 ? 248 TYR   A CB   1 
ATOM   1772 C  CG   . TYR   A 1 226 ? 74.235  29.202  17.463  1   38.76 ? 248 TYR   A CG   1 
ATOM   1773 C  CD1  . TYR   A 1 226 ? 75.42   29.757  17.938  1   39.37 ? 248 TYR   A CD1  1 
ATOM   1774 C  CD2  . TYR   A 1 226 ? 73.134  29.212  18.305  1   39.53 ? 248 TYR   A CD2  1 
ATOM   1775 C  CE1  . TYR   A 1 226 ? 75.524  30.232  19.241  1   39.71 ? 248 TYR   A CE1  1 
ATOM   1776 C  CE2  . TYR   A 1 226 ? 73.222  29.702  19.603  1   40.25 ? 248 TYR   A CE2  1 
ATOM   1777 C  CZ   . TYR   A 1 226 ? 74.422  30.206  20.07   1   40.2  ? 248 TYR   A CZ   1 
ATOM   1778 O  OH   . TYR   A 1 226 ? 74.497  30.683  21.356  1   40.44 ? 248 TYR   A OH   1 
ATOM   1779 N  N    . ARG   A 1 227 ? 73.623  29.503  12.745  1   40.42 ? 249 ARG   A N    1 
ATOM   1780 C  CA   . ARG   A 1 227 ? 73.918  29.226  11.339  1   40.86 ? 249 ARG   A CA   1 
ATOM   1781 C  C    . ARG   A 1 227 ? 74.763  30.382  10.764  1   40.59 ? 249 ARG   A C    1 
ATOM   1782 O  O    . ARG   A 1 227 ? 75.65   30.148  9.952   1   40.73 ? 249 ARG   A O    1 
ATOM   1783 C  CB   . ARG   A 1 227 ? 72.612  29.11   10.522  1   43.22 ? 249 ARG   A CB   1 
ATOM   1784 C  CG   . ARG   A 1 227 ? 72.08   27.688  10.343  1   47.27 ? 249 ARG   A CG   1 
ATOM   1785 C  CD   . ARG   A 1 227 ? 70.602  27.667  9.95    1   50.44 ? 249 ARG   A CD   1 
ATOM   1786 N  NE   . ARG   A 1 227 ? 69.894  26.588  10.641  1   53.72 ? 249 ARG   A NE   1 
ATOM   1787 C  CZ   . ARG   A 1 227 ? 68.679  26.697  11.169  1   56.15 ? 249 ARG   A CZ   1 
ATOM   1788 N  NH1  . ARG   A 1 227 ? 68.003  27.832  11.069  1   54.84 ? 249 ARG   A NH1  1 
ATOM   1789 N  NH2  . ARG   A 1 227 ? 68.122  25.663  11.785  1   57.69 ? 249 ARG   A NH2  1 
ATOM   1790 N  N    . SER   A 1 228 ? 74.495  31.634  11.187  1   40.06 ? 250 SER   A N    1 
ATOM   1791 C  CA   . SER   A 1 228 ? 75.243  32.81   10.72   1   39.78 ? 250 SER   A CA   1 
ATOM   1792 C  C    . SER   A 1 228 ? 76.73   32.788  11.086  1   39.51 ? 250 SER   A C    1 
ATOM   1793 O  O    . SER   A 1 228 ? 77.506  33.529  10.489  1   39.81 ? 250 SER   A O    1 
ATOM   1794 C  CB   . SER   A 1 228 ? 74.596  34.103  11.211  1   40.76 ? 250 SER   A CB   1 
ATOM   1795 O  OG   . SER   A 1 228 ? 74.859  34.335  12.586  1   42.42 ? 250 SER   A OG   1 
ATOM   1796 N  N    . ILE   A 1 229 ? 77.131  31.943  12.049  1   39.26 ? 251 ILE   A N    1 
ATOM   1797 C  CA   . ILE   A 1 229 ? 78.533  31.828  12.44   1   39.76 ? 251 ILE   A CA   1 
ATOM   1798 C  C    . ILE   A 1 229 ? 79.117  30.439  12.12   1   41.54 ? 251 ILE   A C    1 
ATOM   1799 O  O    . ILE   A 1 229 ? 80.308  30.328  11.858  1   41.61 ? 251 ILE   A O    1 
ATOM   1800 C  CB   . ILE   A 1 229 ? 78.782  32.241  13.924  1   38.73 ? 251 ILE   A CB   1 
ATOM   1801 C  CG1  . ILE   A 1 229 ? 77.947  31.416  14.893  1   39.05 ? 251 ILE   A CG1  1 
ATOM   1802 C  CG2  . ILE   A 1 229 ? 78.535  33.712  14.117  1   38.71 ? 251 ILE   A CG2  1 
ATOM   1803 C  CD1  . ILE   A 1 229 ? 78.455  31.461  16.363  1   40.38 ? 251 ILE   A CD1  1 
ATOM   1804 N  N    . PHE   A 1 230 ? 78.297  29.381  12.167  1   42.53 ? 252 PHE   A N    1 
ATOM   1805 C  CA   . PHE   A 1 230 ? 78.796  28.034  11.887  1   43.75 ? 252 PHE   A CA   1 
ATOM   1806 C  C    . PHE   A 1 230 ? 78.822  27.707  10.378  1   45.11 ? 252 PHE   A C    1 
ATOM   1807 O  O    . PHE   A 1 230 ? 79.502  26.769  9.981   1   45.23 ? 252 PHE   A O    1 
ATOM   1808 C  CB   . PHE   A 1 230 ? 78.06   26.974  12.708  1   43.36 ? 252 PHE   A CB   1 
ATOM   1809 C  CG   . PHE   A 1 230 ? 78.254  27.121  14.205  1   43.49 ? 252 PHE   A CG   1 
ATOM   1810 C  CD1  . PHE   A 1 230 ? 79.438  27.631  14.724  1   44.07 ? 252 PHE   A CD1  1 
ATOM   1811 C  CD2  . PHE   A 1 230 ? 77.259  26.743  15.091  1   43.64 ? 252 PHE   A CD2  1 
ATOM   1812 C  CE1  . PHE   A 1 230 ? 79.615  27.763  16.101  1   44.27 ? 252 PHE   A CE1  1 
ATOM   1813 C  CE2  . PHE   A 1 230 ? 77.443  26.873  16.468  1   44.06 ? 252 PHE   A CE2  1 
ATOM   1814 C  CZ   . PHE   A 1 230 ? 78.626  27.361  16.963  1   43.86 ? 252 PHE   A CZ   1 
ATOM   1815 N  N    . ASP   A 1 231 ? 78.139  28.513  9.538   1   45.64 ? 253 ASP   A N    1 
ATOM   1816 C  CA   . ASP   A 1 231 ? 78.17   28.341  8.09    1   46.21 ? 253 ASP   A CA   1 
ATOM   1817 C  C    . ASP   A 1 231 ? 79.008  29.479  7.532   1   46.31 ? 253 ASP   A C    1 
ATOM   1818 O  O    . ASP   A 1 231 ? 78.508  30.599  7.387   1   46.69 ? 253 ASP   A O    1 
ATOM   1819 C  CB   . ASP   A 1 231 ? 76.753  28.36   7.486   1   48.34 ? 253 ASP   A CB   1 
ATOM   1820 C  CG   . ASP   A 1 231 ? 76.691  28.145  5.977   1   53.72 ? 253 ASP   A CG   1 
ATOM   1821 O  OD1  . ASP   A 1 231 ? 77.764  28.066  5.339   1   54.25 ? 253 ASP   A OD1  1 
ATOM   1822 O  OD2  . ASP   A 1 231 ? 75.568  28.05   5.437   1   56.73 ? 253 ASP   A OD2  1 
ATOM   1823 N  N    . PRO   A 1 232 ? 80.276  29.186  7.177   1   45.81 ? 254 PRO   A N    1 
ATOM   1824 C  CA   . PRO   A 1 232 ? 81.155  30.228  6.633   1   45.38 ? 254 PRO   A CA   1 
ATOM   1825 C  C    . PRO   A 1 232 ? 80.596  31.043  5.48    1   45.76 ? 254 PRO   A C    1 
ATOM   1826 O  O    . PRO   A 1 232 ? 80.984  32.197  5.329   1   46.79 ? 254 PRO   A O    1 
ATOM   1827 C  CB   . PRO   A 1 232 ? 82.395  29.448  6.206   1   45.86 ? 254 PRO   A CB   1 
ATOM   1828 C  CG   . PRO   A 1 232 ? 82.423  28.263  7.114   1   46.43 ? 254 PRO   A CG   1 
ATOM   1829 C  CD   . PRO   A 1 232 ? 80.981  27.892  7.296   1   45.23 ? 254 PRO   A CD   1 
ATOM   1830 N  N    . ALA   A 1 233 ? 79.703  30.471  4.671   1   45.07 ? 255 ALA   A N    1 
ATOM   1831 C  CA   . ALA   A 1 233 ? 79.108  31.185  3.547   1   44.82 ? 255 ALA   A CA   1 
ATOM   1832 C  C    . ALA   A 1 233 ? 78.135  32.26   4.023   1   44.18 ? 255 ALA   A C    1 
ATOM   1833 O  O    . ALA   A 1 233 ? 78.055  33.332  3.414   1   44.05 ? 255 ALA   A O    1 
ATOM   1834 C  CB   . ALA   A 1 233 ? 78.406  30.209  2.613   1   45.13 ? 255 ALA   A CB   1 
ATOM   1835 N  N    . VAL   A 1 234 ? 77.398  31.987  5.11    1   43.7  ? 256 VAL   A N    1 
ATOM   1836 C  CA   . VAL   A 1 234 ? 76.479  32.98   5.668   1   43.76 ? 256 VAL   A CA   1 
ATOM   1837 C  C    . VAL   A 1 234 ? 77.294  34.141  6.283   1   44.18 ? 256 VAL   A C    1 
ATOM   1838 O  O    . VAL   A 1 234 ? 76.924  35.304  6.121   1   44.12 ? 256 VAL   A O    1 
ATOM   1839 C  CB   . VAL   A 1 234 ? 75.467  32.363  6.663   1   44.05 ? 256 VAL   A CB   1 
ATOM   1840 C  CG1  . VAL   A 1 234 ? 74.59   33.443  7.289   1   44.38 ? 256 VAL   A CG1  1 
ATOM   1841 C  CG2  . VAL   A 1 234 ? 74.601  31.318  5.972   1   43.89 ? 256 VAL   A CG2  1 
ATOM   1842 N  N    . HIS   A 1 235 ? 78.445  33.832  6.911   1   44.38 ? 257 HIS   A N    1 
ATOM   1843 C  CA   . HIS   A 1 235 ? 79.321  34.869  7.444   1   45.11 ? 257 HIS   A CA   1 
ATOM   1844 C  C    . HIS   A 1 235 ? 79.875  35.718  6.293   1   45.87 ? 257 HIS   A C    1 
ATOM   1845 O  O    . HIS   A 1 235 ? 79.879  36.939  6.391   1   45.9  ? 257 HIS   A O    1 
ATOM   1846 C  CB   . HIS   A 1 235 ? 80.478  34.265  8.262   1   45.56 ? 257 HIS   A CB   1 
ATOM   1847 C  CG   . HIS   A 1 235 ? 81.496  35.286  8.68    1   47.5  ? 257 HIS   A CG   1 
ATOM   1848 N  ND1  . HIS   A 1 235 ? 81.373  35.983  9.874   1   48.75 ? 257 HIS   A ND1  1 
ATOM   1849 C  CD2  . HIS   A 1 235 ? 82.593  35.734  8.022   1   48.34 ? 257 HIS   A CD2  1 
ATOM   1850 C  CE1  . HIS   A 1 235 ? 82.397  36.818  9.903   1   49.15 ? 257 HIS   A CE1  1 
ATOM   1851 N  NE2  . HIS   A 1 235 ? 83.162  36.697  8.813   1   49.32 ? 257 HIS   A NE2  1 
ATOM   1852 N  N    . ASP   A 1 236 ? 80.326  35.071  5.204   1   46.51 ? 258 ASP   A N    1 
ATOM   1853 C  CA   . ASP   A 1 236 ? 80.899  35.75   4.041   1   47.66 ? 258 ASP   A CA   1 
ATOM   1854 C  C    . ASP   A 1 236 ? 79.919  36.672  3.353   1   47.88 ? 258 ASP   A C    1 
ATOM   1855 O  O    . ASP   A 1 236 ? 80.312  37.737  2.886   1   48.26 ? 258 ASP   A O    1 
ATOM   1856 C  CB   . ASP   A 1 236 ? 81.479  34.74   3.048   1   50.68 ? 258 ASP   A CB   1 
ATOM   1857 C  CG   . ASP   A 1 236 ? 82.726  34.048  3.555   1   57.19 ? 258 ASP   A CG   1 
ATOM   1858 O  OD1  . ASP   A 1 236 ? 83.562  34.723  4.195   1   58.38 ? 258 ASP   A OD1  1 
ATOM   1859 O  OD2  . ASP   A 1 236 ? 82.867  32.832  3.313   1   60.15 ? 258 ASP   A OD2  1 
ATOM   1860 N  N    . ALA   A 1 237 ? 78.643  36.297  3.319   1   47.77 ? 259 ALA   A N    1 
ATOM   1861 C  CA   . ALA   A 1 237 ? 77.613  37.136  2.713   1   48.4  ? 259 ALA   A CA   1 
ATOM   1862 C  C    . ALA   A 1 237 ? 77.382  38.39   3.56    1   48.71 ? 259 ALA   A C    1 
ATOM   1863 O  O    . ALA   A 1 237 ? 77.248  39.491  3.012   1   48.85 ? 259 ALA   A O    1 
ATOM   1864 C  CB   . ALA   A 1 237 ? 76.32   36.351  2.571   1   48.56 ? 259 ALA   A CB   1 
ATOM   1865 N  N    . LEU   A 1 238 ? 77.381  38.228  4.902   1   48.59 ? 260 LEU   A N    1 
ATOM   1866 C  CA   . LEU   A 1 238 ? 77.225  39.332  5.848   1   48.75 ? 260 LEU   A CA   1 
ATOM   1867 C  C    . LEU   A 1 238 ? 78.407  40.298  5.724   1   49.56 ? 260 LEU   A C    1 
ATOM   1868 O  O    . LEU   A 1 238 ? 78.211  41.511  5.8     1   49.58 ? 260 LEU   A O    1 
ATOM   1869 C  CB   . LEU   A 1 238 ? 77.12   38.792  7.275   1   48.58 ? 260 LEU   A CB   1 
ATOM   1870 C  CG   . LEU   A 1 238 ? 75.84   38.068  7.583   1   49.77 ? 260 LEU   A CG   1 
ATOM   1871 C  CD1  . LEU   A 1 238 ? 75.926  37.351  8.898   1   50.41 ? 260 LEU   A CD1  1 
ATOM   1872 C  CD2  . LEU   A 1 238 ? 74.676  39.027  7.597   1   50.47 ? 260 LEU   A CD2  1 
ATOM   1873 N  N    . VAL   A 1 239 ? 79.624  39.764  5.495   1   49.9  ? 261 VAL   A N    1 
ATOM   1874 C  CA   . VAL   A 1 239 ? 80.82   40.578  5.296   1   51    ? 261 VAL   A CA   1 
ATOM   1875 C  C    . VAL   A 1 239 ? 80.686  41.408  3.997   1   52.39 ? 261 VAL   A C    1 
ATOM   1876 O  O    . VAL   A 1 239 ? 80.988  42.602  3.986   1   52.64 ? 261 VAL   A O    1 
ATOM   1877 C  CB   . VAL   A 1 239 ? 82.113  39.71   5.32    1   51.28 ? 261 VAL   A CB   1 
ATOM   1878 C  CG1  . VAL   A 1 239 ? 83.33   40.508  4.845   1   51.61 ? 261 VAL   A CG1  1 
ATOM   1879 C  CG2  . VAL   A 1 239 ? 82.36   39.13   6.716   1   51.27 ? 261 VAL   A CG2  1 
ATOM   1880 N  N    . ARG   A 1 240 ? 80.167  40.788  2.932   1   53.23 ? 262 ARG   A N    1 
ATOM   1881 C  CA   . ARG   A 1 240 ? 79.957  41.438  1.636   1   54.34 ? 262 ARG   A CA   1 
ATOM   1882 C  C    . ARG   A 1 240 ? 78.962  42.591  1.706   1   54.7  ? 262 ARG   A C    1 
ATOM   1883 O  O    . ARG   A 1 240 ? 79.201  43.628  1.088   1   55.03 ? 262 ARG   A O    1 
ATOM   1884 C  CB   . ARG   A 1 240 ? 79.516  40.415  0.581   1   56.4  ? 262 ARG   A CB   1 
ATOM   1885 C  CG   . ARG   A 1 240 ? 80.667  39.546  0.111   1   60.82 ? 262 ARG   A CG   1 
ATOM   1886 C  CD   . ARG   A 1 240 ? 80.29   38.664  -1.058  1   64.97 ? 262 ARG   A CD   1 
ATOM   1887 N  NE   . ARG   A 1 240 ? 80.16   37.264  -0.652  1   68.44 ? 262 ARG   A NE   1 
ATOM   1888 C  CZ   . ARG   A 1 240 ? 79.004  36.61   -0.588  1   71.01 ? 262 ARG   A CZ   1 
ATOM   1889 N  NH1  . ARG   A 1 240 ? 77.868  37.219  -0.917  1   71.09 ? 262 ARG   A NH1  1 
ATOM   1890 N  NH2  . ARG   A 1 240 ? 78.975  35.339  -0.197  1   70.29 ? 262 ARG   A NH2  1 
ATOM   1891 N  N    . ARG   A 1 241 ? 77.861  42.435  2.469   1   54.48 ? 263 ARG   A N    1 
ATOM   1892 C  CA   . ARG   A 1 241 ? 76.876  43.516  2.577   1   54.72 ? 263 ARG   A CA   1 
ATOM   1893 C  C    . ARG   A 1 241 ? 77.203  44.572  3.657   1   54.8  ? 263 ARG   A C    1 
ATOM   1894 O  O    . ARG   A 1 241 ? 76.374  45.445  3.929   1   55.44 ? 263 ARG   A O    1 
ATOM   1895 C  CB   . ARG   A 1 241 ? 75.445  42.979  2.745   1   55.84 ? 263 ARG   A CB   1 
ATOM   1896 C  CG   . ARG   A 1 241 ? 75.179  42.228  4.023   1   58.76 ? 263 ARG   A CG   1 
ATOM   1897 C  CD   . ARG   A 1 241 ? 73.713  41.832  4.093   1   61.71 ? 263 ARG   A CD   1 
ATOM   1898 N  N    . GLY   A 1 242 ? 78.399  44.505  4.239   1   53.98 ? 264 GLY   A N    1 
ATOM   1899 C  CA   . GLY   A 1 242 ? 78.845  45.467  5.234   1   53.48 ? 264 GLY   A CA   1 
ATOM   1900 C  C    . GLY   A 1 242 ? 78.367  45.228  6.647   1   52.74 ? 264 GLY   A C    1 
ATOM   1901 O  O    . GLY   A 1 242 ? 78.688  46.017  7.538   1   53.16 ? 264 GLY   A O    1 
ATOM   1902 N  N    . ASP   A 1 243 ? 77.599  44.151  6.878   1   51.49 ? 265 ASP   A N    1 
ATOM   1903 C  CA   . ASP   A 1 243 ? 77.096  43.841  8.222   1   50.95 ? 265 ASP   A CA   1 
ATOM   1904 C  C    . ASP   A 1 243 ? 78.207  43.366  9.169   1   49.24 ? 265 ASP   A C    1 
ATOM   1905 O  O    . ASP   A 1 243 ? 78.075  43.509  10.38   1   49.6  ? 265 ASP   A O    1 
ATOM   1906 C  CB   . ASP   A 1 243 ? 75.963  42.798  8.163   1   53.63 ? 265 ASP   A CB   1 
ATOM   1907 C  CG   . ASP   A 1 243 ? 74.688  43.272  7.488   1   59.7  ? 265 ASP   A CG   1 
ATOM   1908 O  OD1  . ASP   A 1 243 ? 74.685  44.409  6.939   1   60.12 ? 265 ASP   A OD1  1 
ATOM   1909 O  OD2  . ASP   A 1 243 ? 73.694  42.505  7.493   1   62.85 ? 265 ASP   A OD2  1 
ATOM   1910 N  N    . ARG   A 1 244 ? 79.272  42.763  8.615   1   47.22 ? 266 ARG   A N    1 
ATOM   1911 C  CA   . ARG   A 1 244 ? 80.447  42.283  9.333   1   45.77 ? 266 ARG   A CA   1 
ATOM   1912 C  C    . ARG   A 1 244 ? 81.718  42.738  8.584   1   45.73 ? 266 ARG   A C    1 
ATOM   1913 O  O    . ARG   A 1 244 ? 81.668  42.998  7.383   1   46.26 ? 266 ARG   A O    1 
ATOM   1914 C  CB   . ARG   A 1 244 ? 80.418  40.755  9.465   1   44.73 ? 266 ARG   A CB   1 
ATOM   1915 C  CG   . ARG   A 1 244 ? 79.383  40.254  10.455  1   43.56 ? 266 ARG   A CG   1 
ATOM   1916 C  CD   . ARG   A 1 244 ? 79.473  38.757  10.683  1   42.09 ? 266 ARG   A CD   1 
ATOM   1917 N  NE   . ARG   A 1 244 ? 78.318  38.265  11.429  1   41.84 ? 266 ARG   A NE   1 
ATOM   1918 C  CZ   . ARG   A 1 244 ? 78.043  36.981  11.639  1   41.75 ? 266 ARG   A CZ   1 
ATOM   1919 N  NH1  . ARG   A 1 244 ? 78.844  36.037  11.162  1   40.44 ? 266 ARG   A NH1  1 
ATOM   1920 N  NH2  . ARG   A 1 244 ? 76.958  36.63   12.318  1   40.34 ? 266 ARG   A NH2  1 
ATOM   1921 N  N    . ARG   A 1 245 ? 82.839  42.866  9.295   1   44.87 ? 267 ARG   A N    1 
ATOM   1922 C  CA   . ARG   A 1 245 ? 84.136  43.283  8.736   1   44.5  ? 267 ARG   A CA   1 
ATOM   1923 C  C    . ARG   A 1 245 ? 85.232  42.233  8.963   1   43.02 ? 267 ARG   A C    1 
ATOM   1924 O  O    . ARG   A 1 245 ? 86.225  42.206  8.237   1   43.88 ? 267 ARG   A O    1 
ATOM   1925 C  CB   . ARG   A 1 245 ? 84.604  44.584  9.398   1   47.01 ? 267 ARG   A CB   1 
ATOM   1926 C  CG   . ARG   A 1 245 ? 84.025  45.827  8.785   1   52.05 ? 267 ARG   A CG   1 
ATOM   1927 C  CD   . ARG   A 1 245 ? 83.587  46.772  9.867   1   56.61 ? 267 ARG   A CD   1 
ATOM   1928 N  NE   . ARG   A 1 245 ? 83.126  48.067  9.358   1   60.87 ? 267 ARG   A NE   1 
ATOM   1929 C  CZ   . ARG   A 1 245 ? 81.911  48.292  8.866   1   64.79 ? 267 ARG   A CZ   1 
ATOM   1930 N  NH1  . ARG   A 1 245 ? 81.041  47.298  8.746   1   66.41 ? 267 ARG   A NH1  1 
ATOM   1931 N  NH2  . ARG   A 1 245 ? 81.566  49.503  8.468   1   65.48 ? 267 ARG   A NH2  1 
ATOM   1932 N  N    . PHE   A 1 246 ? 85.086  41.428  10.006  1   40.86 ? 268 PHE   A N    1 
ATOM   1933 C  CA   . PHE   A 1 246 ? 86.05   40.433  10.422  1   39.84 ? 268 PHE   A CA   1 
ATOM   1934 C  C    . PHE   A 1 246 ? 86.071  39.217  9.537   1   40.36 ? 268 PHE   A C    1 
ATOM   1935 O  O    . PHE   A 1 246 ? 85.026  38.767  9.062   1   40.27 ? 268 PHE   A O    1 
ATOM   1936 C  CB   . PHE   A 1 246 ? 85.734  39.942  11.845  1   38.45 ? 268 PHE   A CB   1 
ATOM   1937 C  CG   . PHE   A 1 246 ? 86.239  40.774  12.99   1   38.23 ? 268 PHE   A CG   1 
ATOM   1938 C  CD1  . PHE   A 1 246 ? 86.667  42.075  12.789  1   38.86 ? 268 PHE   A CD1  1 
ATOM   1939 C  CD2  . PHE   A 1 246 ? 86.26   40.267  14.274  1   38.7  ? 268 PHE   A CD2  1 
ATOM   1940 C  CE1  . PHE   A 1 246 ? 87.113  42.846  13.851  1   39.35 ? 268 PHE   A CE1  1 
ATOM   1941 C  CE2  . PHE   A 1 246 ? 86.711  41.037  15.33   1   39.16 ? 268 PHE   A CE2  1 
ATOM   1942 C  CZ   . PHE   A 1 246 ? 87.127  42.321  15.114  1   39.09 ? 268 PHE   A CZ   1 
ATOM   1943 N  N    . SER   A 1 247 ? 87.261  38.599  9.427   1   39.86 ? 269 SER   A N    1 
ATOM   1944 C  CA   . SER   A 1 247 ? 87.388  37.326  8.748   1   39.94 ? 269 SER   A CA   1 
ATOM   1945 C  C    . SER   A 1 247 ? 86.709  36.286  9.653   1   40.15 ? 269 SER   A C    1 
ATOM   1946 O  O    . SER   A 1 247 ? 86.602  36.492  10.875  1   40.7  ? 269 SER   A O    1 
ATOM   1947 C  CB   . SER   A 1 247 ? 88.857  36.963  8.546   1   40.7  ? 269 SER   A CB   1 
ATOM   1948 O  OG   . SER   A 1 247 ? 89.49   36.504  9.733   1   41.31 ? 269 SER   A OG   1 
ATOM   1949 N  N    . HIS   A 1 248 ? 86.258  35.177  9.073   1   39.12 ? 270 HIS   A N    1 
ATOM   1950 C  CA   . HIS   A 1 248 ? 85.592  34.133  9.828   1   38.52 ? 270 HIS   A CA   1 
ATOM   1951 C  C    . HIS   A 1 248 ? 86.431  33.625  11.01   1   37.58 ? 270 HIS   A C    1 
ATOM   1952 O  O    . HIS   A 1 248 ? 85.889  33.372  12.092  1   37.64 ? 270 HIS   A O    1 
ATOM   1953 C  CB   . HIS   A 1 248 ? 85.165  32.978  8.896   1   39.17 ? 270 HIS   A CB   1 
ATOM   1954 C  CG   . HIS   A 1 248 ? 84.198  32.04   9.552   1   42.29 ? 270 HIS   A CG   1 
ATOM   1955 N  ND1  . HIS   A 1 248 ? 84.551  30.737  9.871   1   44.91 ? 270 HIS   A ND1  1 
ATOM   1956 C  CD2  . HIS   A 1 248 ? 82.945  32.274  10.004  1   43.13 ? 270 HIS   A CD2  1 
ATOM   1957 C  CE1  . HIS   A 1 248 ? 83.487  30.213  10.458  1   45.07 ? 270 HIS   A CE1  1 
ATOM   1958 N  NE2  . HIS   A 1 248 ? 82.498  31.099  10.557  1   44.46 ? 270 HIS   A NE2  1 
ATOM   1959 N  N    . ARG   A 1 249 ? 87.749  33.511  10.812  1   36.64 ? 271 ARG   A N    1 
ATOM   1960 C  CA   . ARG   A 1 249 ? 88.635  33.043  11.873  1   36.29 ? 271 ARG   A CA   1 
ATOM   1961 C  C    . ARG   A 1 249 ? 88.886  34.121  12.947  1   35.92 ? 271 ARG   A C    1 
ATOM   1962 O  O    . ARG   A 1 249 ? 88.949  33.795  14.125  1   36.35 ? 271 ARG   A O    1 
ATOM   1963 C  CB   . ARG   A 1 249 ? 89.946  32.48   11.308  1   36.67 ? 271 ARG   A CB   1 
ATOM   1964 C  CG   . ARG   A 1 249 ? 90.671  31.666  12.361  1   38.67 ? 271 ARG   A CG   1 
ATOM   1965 C  CD   . ARG   A 1 249 ? 92.008  31.131  11.886  1   41.46 ? 271 ARG   A CD   1 
ATOM   1966 N  NE   . ARG   A 1 249 ? 92.569  30.178  12.851  1   44.41 ? 271 ARG   A NE   1 
ATOM   1967 C  CZ   . ARG   A 1 249 ? 92.268  28.882  12.883  1   47.36 ? 271 ARG   A CZ   1 
ATOM   1968 N  NH1  . ARG   A 1 249 ? 91.409  28.369  12.005  1   47.69 ? 271 ARG   A NH1  1 
ATOM   1969 N  NH2  . ARG   A 1 249 ? 92.821  28.089  13.791  1   46.83 ? 271 ARG   A NH2  1 
ATOM   1970 N  N    . ALA   A 1 250 ? 88.968  35.406  12.554  1   35.52 ? 272 ALA   A N    1 
ATOM   1971 C  CA   . ALA   A 1 250 ? 89.119  36.506  13.534  1   35.35 ? 272 ALA   A CA   1 
ATOM   1972 C  C    . ALA   A 1 250 ? 87.865  36.552  14.436  1   35.29 ? 272 ALA   A C    1 
ATOM   1973 O  O    . ALA   A 1 250 ? 87.991  36.701  15.652  1   35.37 ? 272 ALA   A O    1 
ATOM   1974 C  CB   . ALA   A 1 250 ? 89.284  37.837  12.823  1   34.52 ? 272 ALA   A CB   1 
ATOM   1975 N  N    . LEU   A 1 251 ? 86.67   36.357  13.837  1   34.74 ? 273 LEU   A N    1 
ATOM   1976 C  CA   . LEU   A 1 251 ? 85.419  36.331  14.571  1   35.41 ? 273 LEU   A CA   1 
ATOM   1977 C  C    . LEU   A 1 251 ? 85.385  35.179  15.585  1   35.73 ? 273 LEU   A C    1 
ATOM   1978 O  O    . LEU   A 1 251 ? 84.93   35.377  16.716  1   36.25 ? 273 LEU   A O    1 
ATOM   1979 C  CB   . LEU   A 1 251 ? 84.212  36.271  13.617  1   35.74 ? 273 LEU   A CB   1 
ATOM   1980 C  CG   . LEU   A 1 251 ? 82.86   36.292  14.338  1   37.6  ? 273 LEU   A CG   1 
ATOM   1981 C  CD1  . LEU   A 1 251 ? 82.635  37.622  15.008  1   38.21 ? 273 LEU   A CD1  1 
ATOM   1982 C  CD2  . LEU   A 1 251 ? 81.712  36.021  13.385  1   38.78 ? 273 LEU   A CD2  1 
ATOM   1983 N  N    . GLN   A 1 252 ? 85.908  33.991  15.206  1   35.25 ? 274 GLN   A N    1 
ATOM   1984 C  CA   . GLN   A 1 252 ? 85.974  32.821  16.095  1   35.18 ? 274 GLN   A CA   1 
ATOM   1985 C  C    . GLN   A 1 252 ? 86.833  33.139  17.323  1   34.14 ? 274 GLN   A C    1 
ATOM   1986 O  O    . GLN   A 1 252 ? 86.476  32.773  18.431  1   33.71 ? 274 GLN   A O    1 
ATOM   1987 C  CB   . GLN   A 1 252 ? 86.585  31.595  15.368  1   37.08 ? 274 GLN   A CB   1 
ATOM   1988 C  CG   . GLN   A 1 252 ? 85.796  31.074  14.175  1   39.76 ? 274 GLN   A CG   1 
ATOM   1989 C  CD   . GLN   A 1 252 ? 86.465  29.918  13.448  1   43.44 ? 274 GLN   A CD   1 
ATOM   1990 O  OE1  . GLN   A 1 252 ? 86.032  29.545  12.358  1   45.78 ? 274 GLN   A OE1  1 
ATOM   1991 N  NE2  . GLN   A 1 252 ? 87.533  29.343  13.99   1   42.59 ? 274 GLN   A NE2  1 
ATOM   1992 N  N    . GLY   A 1 253 ? 87.975  33.785  17.098  1   34.07 ? 275 GLY   A N    1 
ATOM   1993 C  CA   . GLY   A 1 253 ? 88.878  34.163  18.176  1   34.15 ? 275 GLY   A CA   1 
ATOM   1994 C  C    . GLY   A 1 253 ? 88.257  35.185  19.116  1   33.25 ? 275 GLY   A C    1 
ATOM   1995 O  O    . GLY   A 1 253 ? 88.356  35.056  20.328  1   32.86 ? 275 GLY   A O    1 
ATOM   1996 N  N    . ALA   A 1 254 ? 87.567  36.187  18.564  1   33.07 ? 276 ALA   A N    1 
ATOM   1997 C  CA   . ALA   A 1 254 ? 86.911  37.218  19.369  1   32.81 ? 276 ALA   A CA   1 
ATOM   1998 C  C    . ALA   A 1 254 ? 85.82   36.6    20.236  1   33.16 ? 276 ALA   A C    1 
ATOM   1999 O  O    . ALA   A 1 254 ? 85.692  36.973  21.403  1   33.39 ? 276 ALA   A O    1 
ATOM   2000 C  CB   . ALA   A 1 254 ? 86.331  38.293  18.462  1   32.39 ? 276 ALA   A CB   1 
ATOM   2001 N  N    . ILE   A 1 255 ? 85.064  35.63   19.689  1   32.68 ? 277 ILE   A N    1 
ATOM   2002 C  CA   . ILE   A 1 255 ? 84.016  34.922  20.43   1   32.59 ? 277 ILE   A CA   1 
ATOM   2003 C  C    . ILE   A 1 255 ? 84.606  34.115  21.579  1   32.64 ? 277 ILE   A C    1 
ATOM   2004 O  O    . ILE   A 1 255 ? 84.113  34.174  22.706  1   32.7  ? 277 ILE   A O    1 
ATOM   2005 C  CB   . ILE   A 1 255 ? 83.133  34.054  19.478  1   32.85 ? 277 ILE   A CB   1 
ATOM   2006 C  CG1  . ILE   A 1 255 ? 82.285  34.95   18.562  1   33.74 ? 277 ILE   A CG1  1 
ATOM   2007 C  CG2  . ILE   A 1 255 ? 82.231  33.1    20.261  1   33.06 ? 277 ILE   A CG2  1 
ATOM   2008 C  CD1  . ILE   A 1 255 ? 81.649  34.206  17.344  1   34.93 ? 277 ILE   A CD1  1 
ATOM   2009 N  N    . MET   A 1 256 ? 85.695  33.397  21.311  1   32.65 ? 278 MET   A N    1 
ATOM   2010 C  CA   . MET   A 1 256 ? 86.377  32.599  22.321  1   32.52 ? 278 MET   A CA   1 
ATOM   2011 C  C    . MET   A 1 256 ? 86.904  33.491  23.446  1   32.4  ? 278 MET   A C    1 
ATOM   2012 O  O    . MET   A 1 256 ? 86.77   33.151  24.624  1   32.76 ? 278 MET   A O    1 
ATOM   2013 C  CB   . MET   A 1 256 ? 87.534  31.832  21.675  1   33.94 ? 278 MET   A CB   1 
ATOM   2014 C  CG   . MET   A 1 256 ? 88.079  30.758  22.573  1   37.32 ? 278 MET   A CG   1 
ATOM   2015 S  SD   . MET   A 1 256 ? 89.608  29.985  21.991  1   45.62 ? 278 MET   A SD   1 
ATOM   2016 C  CE   . MET   A 1 256 ? 89.871  28.886  23.372  1   41.95 ? 278 MET   A CE   1 
ATOM   2017 N  N    . ILE   A 1 257 ? 87.462  34.657  23.097  1   31.56 ? 279 ILE   A N    1 
ATOM   2018 C  CA   . ILE   A 1 257 ? 87.952  35.596  24.105  1   31.7  ? 279 ILE   A CA   1 
ATOM   2019 C  C    . ILE   A 1 257 ? 86.829  36.036  25.064  1   31.42 ? 279 ILE   A C    1 
ATOM   2020 O  O    . ILE   A 1 257 ? 87.021  35.985  26.274  1   31.43 ? 279 ILE   A O    1 
ATOM   2021 C  CB   . ILE   A 1 257 ? 88.699  36.785  23.429  1   32.17 ? 279 ILE   A CB   1 
ATOM   2022 C  CG1  . ILE   A 1 257 ? 90.054  36.305  22.859  1   32.58 ? 279 ILE   A CG1  1 
ATOM   2023 C  CG2  . ILE   A 1 257 ? 88.9    37.937  24.42   1   32.71 ? 279 ILE   A CG2  1 
ATOM   2024 C  CD1  . ILE   A 1 257 ? 90.881  37.345  22.173  1   33.24 ? 279 ILE   A CD1  1 
ATOM   2025 N  N    . THR   A 1 258 ? 85.631  36.363  24.534  1   31.58 ? 280 THR   A N    1 
ATOM   2026 C  CA   . THR   A 1 258 ? 84.487  36.781  25.365  1   31.99 ? 280 THR   A CA   1 
ATOM   2027 C  C    . THR   A 1 258 ? 83.952  35.67   26.267  1   33.81 ? 280 THR   A C    1 
ATOM   2028 O  O    . THR   A 1 258 ? 83.422  35.942  27.344  1   33.67 ? 280 THR   A O    1 
ATOM   2029 C  CB   . THR   A 1 258 ? 83.352  37.381  24.522  1   31.46 ? 280 THR   A CB   1 
ATOM   2030 O  OG1  . THR   A 1 258 ? 82.749  36.37   23.717  1   31.24 ? 280 THR   A OG1  1 
ATOM   2031 C  CG2  . THR   A 1 258 ? 83.792  38.55   23.689  1   31.2  ? 280 THR   A CG2  1 
ATOM   2032 N  N    . PHE   A 1 259 ? 84.063  34.418  25.816  1   34.95 ? 281 PHE   A N    1 
ATOM   2033 C  CA   . PHE   A 1 259 ? 83.592  33.269  26.582  1   35.34 ? 281 PHE   A CA   1 
ATOM   2034 C  C    . PHE   A 1 259 ? 84.487  33.015  27.809  1   35.25 ? 281 PHE   A C    1 
ATOM   2035 O  O    . PHE   A 1 259 ? 83.99   32.647  28.878  1   34.75 ? 281 PHE   A O    1 
ATOM   2036 C  CB   . PHE   A 1 259 ? 83.597  32.016  25.69   1   35.62 ? 281 PHE   A CB   1 
ATOM   2037 C  CG   . PHE   A 1 259 ? 82.371  31.786  24.832  1   36.73 ? 281 PHE   A CG   1 
ATOM   2038 C  CD1  . PHE   A 1 259 ? 81.617  32.849  24.37   1   37.63 ? 281 PHE   A CD1  1 
ATOM   2039 C  CD2  . PHE   A 1 259 ? 81.992  30.505  24.467  1   37.91 ? 281 PHE   A CD2  1 
ATOM   2040 C  CE1  . PHE   A 1 259 ? 80.514  32.636  23.551  1   38.37 ? 281 PHE   A CE1  1 
ATOM   2041 C  CE2  . PHE   A 1 259 ? 80.868  30.293  23.674  1   38.62 ? 281 PHE   A CE2  1 
ATOM   2042 C  CZ   . PHE   A 1 259 ? 80.138  31.359  23.225  1   38.44 ? 281 PHE   A CZ   1 
ATOM   2043 N  N    . TYR   A 1 260 ? 85.799  33.218  27.658  1   35.56 ? 282 TYR   A N    1 
ATOM   2044 C  CA   . TYR   A 1 260 ? 86.731  32.928  28.748  1   36.58 ? 282 TYR   A CA   1 
ATOM   2045 C  C    . TYR   A 1 260 ? 87.334  34.163  29.423  1   36.98 ? 282 TYR   A C    1 
ATOM   2046 O  O    . TYR   A 1 260 ? 88.326  34.035  30.129  1   37.07 ? 282 TYR   A O    1 
ATOM   2047 C  CB   . TYR   A 1 260 ? 87.836  31.985  28.255  1   36.84 ? 282 TYR   A CB   1 
ATOM   2048 C  CG   . TYR   A 1 260 ? 87.287  30.69   27.695  1   37.94 ? 282 TYR   A CG   1 
ATOM   2049 C  CD1  . TYR   A 1 260 ? 86.764  29.712  28.533  1   39.19 ? 282 TYR   A CD1  1 
ATOM   2050 C  CD2  . TYR   A 1 260 ? 87.225  30.473  26.33   1   38.94 ? 282 TYR   A CD2  1 
ATOM   2051 C  CE1  . TYR   A 1 260 ? 86.221  28.538  28.021  1   40.45 ? 282 TYR   A CE1  1 
ATOM   2052 C  CE2  . TYR   A 1 260 ? 86.67   29.315  25.804  1   40.39 ? 282 TYR   A CE2  1 
ATOM   2053 C  CZ   . TYR   A 1 260 ? 86.185  28.339  26.652  1   41.41 ? 282 TYR   A CZ   1 
ATOM   2054 O  OH   . TYR   A 1 260 ? 85.681  27.18   26.122  1   42.65 ? 282 TYR   A OH   1 
ATOM   2055 N  N    . ARG   A 1 261 ? 86.716  35.339  29.247  1   36.42 ? 283 ARG   A N    1 
ATOM   2056 C  CA   . ARG   A 1 261 ? 87.214  36.603  29.802  1   36.06 ? 283 ARG   A CA   1 
ATOM   2057 C  C    . ARG   A 1 261 ? 87.522  36.581  31.318  1   36.43 ? 283 ARG   A C    1 
ATOM   2058 O  O    . ARG   A 1 261 ? 88.411  37.306  31.742  1   36.68 ? 283 ARG   A O    1 
ATOM   2059 C  CB   . ARG   A 1 261 ? 86.257  37.745  29.468  1   35.45 ? 283 ARG   A CB   1 
ATOM   2060 C  CG   . ARG   A 1 261 ? 84.876  37.509  30.007  1   36.54 ? 283 ARG   A CG   1 
ATOM   2061 C  CD   . ARG   A 1 261 ? 83.981  38.663  29.686  1   39.39 ? 283 ARG   A CD   1 
ATOM   2062 N  NE   . ARG   A 1 261 ? 84.293  39.801  30.534  1   42.8  ? 283 ARG   A NE   1 
ATOM   2063 C  CZ   . ARG   A 1 261 ? 83.7    40.988  30.45   1   45.05 ? 283 ARG   A CZ   1 
ATOM   2064 N  NH1  . ARG   A 1 261 ? 82.746  41.201  29.545  1   44.04 ? 283 ARG   A NH1  1 
ATOM   2065 N  NH2  . ARG   A 1 261 ? 84.06   41.973  31.262  1   44.51 ? 283 ARG   A NH2  1 
ATOM   2066 N  N    . ASP   A 1 262 ? 86.801  35.78   32.121  1   36.47 ? 284 ASP   A N    1 
ATOM   2067 C  CA   . ASP   A 1 262 ? 87.048  35.672  33.565  1   37.15 ? 284 ASP   A CA   1 
ATOM   2068 C  C    . ASP   A 1 262 ? 88.332  34.892  33.892  1   37.71 ? 284 ASP   A C    1 
ATOM   2069 O  O    . ASP   A 1 262 ? 88.748  34.899  35.049  1   38.46 ? 284 ASP   A O    1 
ATOM   2070 C  CB   . ASP   A 1 262 ? 85.884  34.96   34.269  1   39.06 ? 284 ASP   A CB   1 
ATOM   2071 C  CG   . ASP   A 1 262 ? 84.633  35.801  34.477  1   44.4  ? 284 ASP   A CG   1 
ATOM   2072 O  OD1  . ASP   A 1 262 ? 84.613  36.963  34.024  1   43.91 ? 284 ASP   A OD1  1 
ATOM   2073 O  OD2  . ASP   A 1 262 ? 83.668  35.29   35.101  1   48.66 ? 284 ASP   A OD2  1 
ATOM   2074 N  N    . GLU   A 1 263 ? 88.907  34.174  32.917  1   37.31 ? 285 GLU   A N    1 
ATOM   2075 C  CA   . GLU   A 1 263 ? 90.117  33.384  33.086  1   38.02 ? 285 GLU   A CA   1 
ATOM   2076 C  C    . GLU   A 1 263 ? 91.326  34.267  32.96   1   38.08 ? 285 GLU   A C    1 
ATOM   2077 O  O    . GLU   A 1 263 ? 91.419  35.036  32.004  1   38.03 ? 285 GLU   A O    1 
ATOM   2078 C  CB   . GLU   A 1 263 ? 90.207  32.273  32.025  1   41.05 ? 285 GLU   A CB   1 
ATOM   2079 C  CG   . GLU   A 1 263 ? 89.049  31.297  32.098  1   48.51 ? 285 GLU   A CG   1 
ATOM   2080 C  CD   . GLU   A 1 263 ? 89.009  30.529  33.404  1   59.75 ? 285 GLU   A CD   1 
ATOM   2081 O  OE1  . GLU   A 1 263 ? 90.093  30.123  33.885  1   62.08 ? 285 GLU   A OE1  1 
ATOM   2082 O  OE2  . GLU   A 1 263 ? 87.895  30.343  33.951  1   62.89 ? 285 GLU   A OE2  1 
ATOM   2083 N  N    . PRO   A 1 264 ? 92.281  34.14   33.895  1   37.83 ? 286 PRO   A N    1 
ATOM   2084 C  CA   . PRO   A 1 264 ? 93.492  34.977  33.842  1   37.7  ? 286 PRO   A CA   1 
ATOM   2085 C  C    . PRO   A 1 264 ? 94.168  35.131  32.484  1   37.88 ? 286 PRO   A C    1 
ATOM   2086 O  O    . PRO   A 1 264 ? 94.6    36.235  32.172  1   38.56 ? 286 PRO   A O    1 
ATOM   2087 C  CB   . PRO   A 1 264 ? 94.428  34.296  34.844  1   38.09 ? 286 PRO   A CB   1 
ATOM   2088 C  CG   . PRO   A 1 264 ? 93.513  33.665  35.837  1   38.62 ? 286 PRO   A CG   1 
ATOM   2089 C  CD   . PRO   A 1 264 ? 92.273  33.267  35.09   1   37.45 ? 286 PRO   A CD   1 
ATOM   2090 N  N    . ARG   A 1 265 ? 94.245  34.05   31.675  1   37.12 ? 287 ARG   A N    1 
ATOM   2091 C  CA   . ARG   A 1 265 ? 94.892  34.073  30.363  1   37.01 ? 287 ARG   A CA   1 
ATOM   2092 C  C    . ARG   A 1 265 ? 94.111  34.837  29.296  1   36.53 ? 287 ARG   A C    1 
ATOM   2093 O  O    . ARG   A 1 265 ? 94.703  35.316  28.329  1   36.58 ? 287 ARG   A O    1 
ATOM   2094 C  CB   . ARG   A 1 265 ? 95.211  32.647  29.882  1   38.57 ? 287 ARG   A CB   1 
ATOM   2095 N  N    . PHE   A 1 266 ? 92.801  34.979  29.476  1   35.95 ? 288 PHE   A N    1 
ATOM   2096 C  CA   . PHE   A 1 266 ? 91.966  35.684  28.519  1   36.35 ? 288 PHE   A CA   1 
ATOM   2097 C  C    . PHE   A 1 266 ? 91.517  37.082  28.979  1   35.37 ? 288 PHE   A C    1 
ATOM   2098 O  O    . PHE   A 1 266 ? 90.866  37.771  28.197  1   35.06 ? 288 PHE   A O    1 
ATOM   2099 C  CB   . PHE   A 1 266 ? 90.734  34.83   28.181  1   36.99 ? 288 PHE   A CB   1 
ATOM   2100 C  CG   . PHE   A 1 266 ? 91.026  33.593  27.361  1   38.16 ? 288 PHE   A CG   1 
ATOM   2101 C  CD1  . PHE   A 1 266 ? 91.357  32.397  27.973  1   38.79 ? 288 PHE   A CD1  1 
ATOM   2102 C  CD2  . PHE   A 1 266 ? 90.957  33.626  25.98   1   39.16 ? 288 PHE   A CD2  1 
ATOM   2103 C  CE1  . PHE   A 1 266 ? 91.616  31.263  27.22   1   39.34 ? 288 PHE   A CE1  1 
ATOM   2104 C  CE2  . PHE   A 1 266 ? 91.225  32.487  25.227  1   40.04 ? 288 PHE   A CE2  1 
ATOM   2105 C  CZ   . PHE   A 1 266 ? 91.549  31.313  25.855  1   39.37 ? 288 PHE   A CZ   1 
ATOM   2106 N  N    . SER   A 1 267 ? 91.847  37.503  30.217  1   34.82 ? 289 SER   A N    1 
ATOM   2107 C  CA   . SER   A 1 267 ? 91.364  38.797  30.72   1   35.37 ? 289 SER   A CA   1 
ATOM   2108 C  C    . SER   A 1 267 ? 91.956  40.039  30.016  1   34.41 ? 289 SER   A C    1 
ATOM   2109 O  O    . SER   A 1 267 ? 91.191  40.951  29.671  1   34.58 ? 289 SER   A O    1 
ATOM   2110 C  CB   . SER   A 1 267 ? 91.52   38.914  32.232  1   37.61 ? 289 SER   A CB   1 
ATOM   2111 O  OG   . SER   A 1 267 ? 92.892  38.927  32.571  1   42.74 ? 289 SER   A OG   1 
ATOM   2112 N  N    . GLN   A 1 268 ? 93.279  40.084  29.799  1   32.99 ? 290 GLN   A N    1 
ATOM   2113 C  CA   . GLN   A 1 268 ? 93.884  41.218  29.099  1   32.43 ? 290 GLN   A CA   1 
ATOM   2114 C  C    . GLN   A 1 268 ? 93.507  41.249  27.609  1   32.43 ? 290 GLN   A C    1 
ATOM   2115 O  O    . GLN   A 1 268 ? 93.076  42.312  27.152  1   32.59 ? 290 GLN   A O    1 
ATOM   2116 C  CB   . GLN   A 1 268 ? 95.395  41.325  29.342  1   33.01 ? 290 GLN   A CB   1 
ATOM   2117 C  CG   . GLN   A 1 268 ? 95.736  41.693  30.788  1   34.8  ? 290 GLN   A CG   1 
ATOM   2118 C  CD   . GLN   A 1 268 ? 95.072  42.993  31.194  1   39.17 ? 290 GLN   A CD   1 
ATOM   2119 O  OE1  . GLN   A 1 268 ? 95.38   44.057  30.668  1   40.38 ? 290 GLN   A OE1  1 
ATOM   2120 N  NE2  . GLN   A 1 268 ? 94.11   42.922  32.101  1   40.31 ? 290 GLN   A NE2  1 
ATOM   2121 N  N    . PRO   A 1 269 ? 93.516  40.116  26.857  1   31.9  ? 291 PRO   A N    1 
ATOM   2122 C  CA   . PRO   A 1 269 ? 93.02   40.161  25.465  1   30.94 ? 291 PRO   A CA   1 
ATOM   2123 C  C    . PRO   A 1 269 ? 91.561  40.647  25.383  1   29.55 ? 291 PRO   A C    1 
ATOM   2124 O  O    . PRO   A 1 269 ? 91.202  41.331  24.419  1   29.51 ? 291 PRO   A O    1 
ATOM   2125 C  CB   . PRO   A 1 269 ? 93.149  38.698  24.993  1   32.02 ? 291 PRO   A CB   1 
ATOM   2126 C  CG   . PRO   A 1 269 ? 94.234  38.108  25.883  1   32.46 ? 291 PRO   A CG   1 
ATOM   2127 C  CD   . PRO   A 1 269 ? 94.006  38.761  27.215  1   31.18 ? 291 PRO   A CD   1 
ATOM   2128 N  N    . HIS   A 1 270 ? 90.728  40.332  26.396  1   28.73 ? 292 HIS   A N    1 
ATOM   2129 C  CA   . HIS   A 1 270 ? 89.342  40.824  26.403  1   28.93 ? 292 HIS   A CA   1 
ATOM   2130 C  C    . HIS   A 1 270 ? 89.273  42.339  26.674  1   28.71 ? 292 HIS   A C    1 
ATOM   2131 O  O    . HIS   A 1 270 ? 88.456  43.043  26.073  1   28.77 ? 292 HIS   A O    1 
ATOM   2132 C  CB   . HIS   A 1 270 ? 88.466  40.068  27.389  1   29.74 ? 292 HIS   A CB   1 
ATOM   2133 C  CG   . HIS   A 1 270 ? 87.047  40.544  27.349  1   32.28 ? 292 HIS   A CG   1 
ATOM   2134 N  ND1  . HIS   A 1 270 ? 86.564  41.448  28.278  1   33.96 ? 292 HIS   A ND1  1 
ATOM   2135 C  CD2  . HIS   A 1 270 ? 86.076  40.288  26.439  1   33.21 ? 292 HIS   A CD2  1 
ATOM   2136 C  CE1  . HIS   A 1 270 ? 85.319  41.704  27.912  1   34.28 ? 292 HIS   A CE1  1 
ATOM   2137 N  NE2  . HIS   A 1 270 ? 84.98   41.025  26.816  1   34.21 ? 292 HIS   A NE2  1 
ATOM   2138 N  N    . GLN   A 1 271 ? 90.153  42.829  27.556  1   27.76 ? 293 GLN   A N    1 
ATOM   2139 C  CA   . GLN   A 1 271 ? 90.258  44.246  27.857  1   28.56 ? 293 GLN   A CA   1 
ATOM   2140 C  C    . GLN   A 1 271 ? 90.72   45.018  26.61   1   28.72 ? 293 GLN   A C    1 
ATOM   2141 O  O    . GLN   A 1 271 ? 90.181  46.086  26.319  1   28.02 ? 293 GLN   A O    1 
ATOM   2142 C  CB   . GLN   A 1 271 ? 91.199  44.48   29.068  1   30.83 ? 293 GLN   A CB   1 
ATOM   2143 C  CG   . GLN   A 1 271 ? 91.11   45.887  29.655  1   37.19 ? 293 GLN   A CG   1 
ATOM   2144 C  CD   . GLN   A 1 271 ? 89.704  46.312  30.029  1   43.06 ? 293 GLN   A CD   1 
ATOM   2145 O  OE1  . GLN   A 1 271 ? 88.896  45.521  30.514  1   46.04 ? 293 GLN   A OE1  1 
ATOM   2146 N  NE2  . GLN   A 1 271 ? 89.373  47.573  29.81   1   43.89 ? 293 GLN   A NE2  1 
ATOM   2147 N  N    . LEU   A 1 272 ? 91.644  44.42   25.811  1   28.9  ? 294 LEU   A N    1 
ATOM   2148 C  CA   . LEU   A 1 272 ? 92.123  44.993  24.546  1   28.87 ? 294 LEU   A CA   1 
ATOM   2149 C  C    . LEU   A 1 272 ? 90.908  45.176  23.608  1   29.17 ? 294 LEU   A C    1 
ATOM   2150 O  O    . LEU   A 1 272 ? 90.706  46.266  23.084  1   30.37 ? 294 LEU   A O    1 
ATOM   2151 C  CB   . LEU   A 1 272 ? 93.172  44.033  23.916  1   29.18 ? 294 LEU   A CB   1 
ATOM   2152 C  CG   . LEU   A 1 272 ? 94.125  44.601  22.861  1   31.14 ? 294 LEU   A CG   1 
ATOM   2153 C  CD1  . LEU   A 1 272 ? 95.396  43.8    22.8    1   31.6  ? 294 LEU   A CD1  1 
ATOM   2154 C  CD2  . LEU   A 1 272 ? 93.488  44.663  21.487  1   32.02 ? 294 LEU   A CD2  1 
ATOM   2155 N  N    . LEU   A 1 273 ? 90.067  44.142  23.454  1   28.39 ? 295 LEU   A N    1 
ATOM   2156 C  CA   . LEU   A 1 273 ? 88.863  44.219  22.616  1   28.6  ? 295 LEU   A CA   1 
ATOM   2157 C  C    . LEU   A 1 273 ? 87.853  45.265  23.14   1   28.69 ? 295 LEU   A C    1 
ATOM   2158 O  O    . LEU   A 1 273 ? 87.305  46.024  22.354  1   28.9  ? 295 LEU   A O    1 
ATOM   2159 C  CB   . LEU   A 1 273 ? 88.176  42.848  22.539  1   29.18 ? 295 LEU   A CB   1 
ATOM   2160 C  CG   . LEU   A 1 273 ? 88.904  41.701  21.843  1   30.95 ? 295 LEU   A CG   1 
ATOM   2161 C  CD1  . LEU   A 1 273 ? 88.031  40.471  21.802  1   30.97 ? 295 LEU   A CD1  1 
ATOM   2162 C  CD2  . LEU   A 1 273 ? 89.413  42.094  20.455  1   31.47 ? 295 LEU   A CD2  1 
ATOM   2163 N  N    . THR   A 1 274 ? 87.622  45.311  24.46   1   28.47 ? 296 THR   A N    1 
ATOM   2164 C  CA   . THR   A 1 274 ? 86.719  46.279  25.107  1   28.99 ? 296 THR   A CA   1 
ATOM   2165 C  C    . THR   A 1 274 ? 87.134  47.715  24.825  1   27.94 ? 296 THR   A C    1 
ATOM   2166 O  O    . THR   A 1 274 ? 86.284  48.54   24.494  1   27.92 ? 296 THR   A O    1 
ATOM   2167 C  CB   . THR   A 1 274 ? 86.685  46.039  26.629  1   31.64 ? 296 THR   A CB   1 
ATOM   2168 O  OG1  . THR   A 1 274 ? 86.245  44.716  26.861  1   33.3  ? 296 THR   A OG1  1 
ATOM   2169 C  CG2  . THR   A 1 274 ? 85.757  46.984  27.342  1   33    ? 296 THR   A CG2  1 
ATOM   2170 N  N    . LEU   A 1 275 ? 88.452  47.998  24.898  1   26.81 ? 297 LEU   A N    1 
ATOM   2171 C  CA   . LEU   A 1 275 ? 89.002  49.325  24.662  1   26.13 ? 297 LEU   A CA   1 
ATOM   2172 C  C    . LEU   A 1 275 ? 88.896  49.742  23.205  1   26.61 ? 297 LEU   A C    1 
ATOM   2173 O  O    . LEU   A 1 275 ? 88.657  50.905  22.951  1   26.88 ? 297 LEU   A O    1 
ATOM   2174 C  CB   . LEU   A 1 275 ? 90.437  49.427  25.191  1   25.28 ? 297 LEU   A CB   1 
ATOM   2175 C  CG   . LEU   A 1 275 ? 90.564  49.288  26.707  1   25.42 ? 297 LEU   A CG   1 
ATOM   2176 C  CD1  . LEU   A 1 275 ? 91.989  49.115  27.106  1   26.01 ? 297 LEU   A CD1  1 
ATOM   2177 C  CD2  . LEU   A 1 275 ? 89.903  50.458  27.448  1   24.75 ? 297 LEU   A CD2  1 
ATOM   2178 N  N    . LEU   A 1 276 ? 88.992  48.799  22.26   1   27.33 ? 298 LEU   A N    1 
ATOM   2179 C  CA   . LEU   A 1 276 ? 88.798  49.05   20.824  1   28.68 ? 298 LEU   A CA   1 
ATOM   2180 C  C    . LEU   A 1 276 ? 87.342  49.493  20.582  1   29.58 ? 298 LEU   A C    1 
ATOM   2181 O  O    . LEU   A 1 276 ? 87.095  50.418  19.81   1   29.8  ? 298 LEU   A O    1 
ATOM   2182 C  CB   . LEU   A 1 276 ? 89.087  47.772  20.003  1   28.74 ? 298 LEU   A CB   1 
ATOM   2183 C  CG   . LEU   A 1 276 ? 90.562  47.382  19.877  1   30.18 ? 298 LEU   A CG   1 
ATOM   2184 C  CD1  . LEU   A 1 276 ? 90.694  46.047  19.16   1   30.52 ? 298 LEU   A CD1  1 
ATOM   2185 C  CD2  . LEU   A 1 276 ? 91.386  48.496  19.147  1   30.24 ? 298 LEU   A CD2  1 
ATOM   2186 N  N    . MET   A 1 277 ? 86.394  48.828  21.247  1   29.86 ? 299 MET   A N    1 
ATOM   2187 C  CA   . MET   A 1 277 ? 84.975  49.172  21.184  1   30.87 ? 299 MET   A CA   1 
ATOM   2188 C  C    . MET   A 1 277 ? 84.741  50.541  21.797  1   30.36 ? 299 MET   A C    1 
ATOM   2189 O  O    . MET   A 1 277 ? 84.018  51.339  21.215  1   30.93 ? 299 MET   A O    1 
ATOM   2190 C  CB   . MET   A 1 277 ? 84.138  48.117  21.936  1   32.14 ? 299 MET   A CB   1 
ATOM   2191 C  CG   . MET   A 1 277 ? 83.57   47.073  21.022  1   34.13 ? 299 MET   A CG   1 
ATOM   2192 S  SD   . MET   A 1 277 ? 82.548  45.904  21.91   1   37.46 ? 299 MET   A SD   1 
ATOM   2193 C  CE   . MET   A 1 277 ? 83.778  45.016  22.801  1   33.47 ? 299 MET   A CE   1 
ATOM   2194 N  N    . ASP   A 1 278 ? 85.361  50.827  22.969  1   29.59 ? 300 ASP   A N    1 
ATOM   2195 C  CA   . ASP   A 1 278 ? 85.24   52.126  23.639  1   29.29 ? 300 ASP   A CA   1 
ATOM   2196 C  C    . ASP   A 1 278 ? 85.773  53.26   22.764  1   29.03 ? 300 ASP   A C    1 
ATOM   2197 O  O    . ASP   A 1 278 ? 85.178  54.326  22.729  1   30.38 ? 300 ASP   A O    1 
ATOM   2198 C  CB   . ASP   A 1 278 ? 85.951  52.125  25.008  1   31.34 ? 300 ASP   A CB   1 
ATOM   2199 C  CG   . ASP   A 1 278 ? 85.284  51.237  26.051  1   36.08 ? 300 ASP   A CG   1 
ATOM   2200 O  OD1  . ASP   A 1 278 ? 84.105  50.864  25.85   1   37    ? 300 ASP   A OD1  1 
ATOM   2201 O  OD2  . ASP   A 1 278 ? 85.949  50.889  27.046  1   38.17 ? 300 ASP   A OD2  1 
ATOM   2202 N  N    . ILE   A 1 279 ? 86.863  53.025  22.038  1   27.54 ? 301 ILE   A N    1 
ATOM   2203 C  CA   . ILE   A 1 279 ? 87.464  54.012  21.152  1   27.42 ? 301 ILE   A CA   1 
ATOM   2204 C  C    . ILE   A 1 279 ? 86.526  54.298  19.979  1   28.93 ? 301 ILE   A C    1 
ATOM   2205 O  O    . ILE   A 1 279 ? 86.279  55.454  19.638  1   29.22 ? 301 ILE   A O    1 
ATOM   2206 C  CB   . ILE   A 1 279 ? 88.857  53.494  20.696  1   26.53 ? 301 ILE   A CB   1 
ATOM   2207 C  CG1  . ILE   A 1 279 ? 89.878  53.63   21.84   1   26.85 ? 301 ILE   A CG1  1 
ATOM   2208 C  CG2  . ILE   A 1 279 ? 89.342  54.197  19.421  1   26.37 ? 301 ILE   A CG2  1 
ATOM   2209 C  CD1  . ILE   A 1 279 ? 91.171  53.004  21.586  1   27.61 ? 301 ILE   A CD1  1 
ATOM   2210 N  N    . ASP   A 1 280 ? 85.966  53.233  19.405  1   29.47 ? 302 ASP   A N    1 
ATOM   2211 C  CA   . ASP   A 1 280 ? 85.016  53.276  18.304  1   30.28 ? 302 ASP   A CA   1 
ATOM   2212 C  C    . ASP   A 1 280 ? 83.779  54.096  18.727  1   30.64 ? 302 ASP   A C    1 
ATOM   2213 O  O    . ASP   A 1 280 ? 83.369  55.005  18.009  1   31.16 ? 302 ASP   A O    1 
ATOM   2214 C  CB   . ASP   A 1 280 ? 84.602  51.831  17.983  1   32.06 ? 302 ASP   A CB   1 
ATOM   2215 C  CG   . ASP   A 1 280 ? 84.495  51.476  16.542  1   38.75 ? 302 ASP   A CG   1 
ATOM   2216 O  OD1  . ASP   A 1 280 ? 84.926  52.284  15.693  1   40.18 ? 302 ASP   A OD1  1 
ATOM   2217 O  OD2  . ASP   A 1 280 ? 83.99   50.381  16.247  1   42.57 ? 302 ASP   A OD2  1 
ATOM   2218 N  N    A SER   A 1 281 ? 83.228  53.793  19.9    0.5 30.36 ? 303 SER   A N    1 
ATOM   2219 N  N    B SER   A 1 281 ? 83.221  53.804  19.904  0.5 30.48 ? 303 SER   A N    1 
ATOM   2220 C  CA   A SER   A 1 281 ? 82.05   54.457  20.434  0.5 30.73 ? 303 SER   A CA   1 
ATOM   2221 C  CA   B SER   A 1 281 ? 82.033  54.5    20.405  0.5 30.95 ? 303 SER   A CA   1 
ATOM   2222 C  C    A SER   A 1 281 ? 82.326  55.92   20.793  0.5 31.66 ? 303 SER   A C    1 
ATOM   2223 C  C    B SER   A 1 281 ? 82.336  55.946  20.75   0.5 31.76 ? 303 SER   A C    1 
ATOM   2224 O  O    A SER   A 1 281 ? 81.45   56.769  20.619  0.5 32.19 ? 303 SER   A O    1 
ATOM   2225 O  O    B SER   A 1 281 ? 81.48   56.807  20.555  0.5 32.27 ? 303 SER   A O    1 
ATOM   2226 C  CB   A SER   A 1 281 ? 81.535  53.687  21.646  0.5 30.94 ? 303 SER   A CB   1 
ATOM   2227 C  CB   B SER   A 1 281 ? 81.455  53.807  21.639  0.5 31.51 ? 303 SER   A CB   1 
ATOM   2228 O  OG   A SER   A 1 281 ? 80.44   54.342  22.257  0.5 32.4  ? 303 SER   A OG   1 
ATOM   2229 O  OG   B SER   A 1 281 ? 81.793  52.434  21.739  0.5 33.52 ? 303 SER   A OG   1 
ATOM   2230 N  N    . LEU   A 1 282 ? 83.539  56.218  21.284  1   31.46 ? 304 LEU   A N    1 
ATOM   2231 C  CA   . LEU   A 1 282 ? 83.91   57.588  21.631  1   31.38 ? 304 LEU   A CA   1 
ATOM   2232 C  C    . LEU   A 1 282 ? 84.095  58.441  20.387  1   31.72 ? 304 LEU   A C    1 
ATOM   2233 O  O    . LEU   A 1 282 ? 83.759  59.622  20.424  1   31.57 ? 304 LEU   A O    1 
ATOM   2234 C  CB   . LEU   A 1 282 ? 85.123  57.648  22.566  1   30.4  ? 304 LEU   A CB   1 
ATOM   2235 C  CG   . LEU   A 1 282 ? 84.766  57.417  24.024  1   30.75 ? 304 LEU   A CG   1 
ATOM   2236 C  CD1  . LEU   A 1 282 ? 85.97   56.998  24.833  1   30.72 ? 304 LEU   A CD1  1 
ATOM   2237 C  CD2  . LEU   A 1 282 ? 84.065  58.632  24.63   1   31.04 ? 304 LEU   A CD2  1 
ATOM   2238 N  N    . ILE   A 1 283 ? 84.585  57.848  19.278  1   32.07 ? 305 ILE   A N    1 
ATOM   2239 C  CA   . ILE   A 1 283 ? 84.708  58.583  18.021  1   33.42 ? 305 ILE   A CA   1 
ATOM   2240 C  C    . ILE   A 1 283 ? 83.313  58.927  17.478  1   34.74 ? 305 ILE   A C    1 
ATOM   2241 O  O    . ILE   A 1 283 ? 83.071  60.06   17.077  1   35.15 ? 305 ILE   A O    1 
ATOM   2242 C  CB   . ILE   A 1 283 ? 85.613  57.861  17.005  1   34.06 ? 305 ILE   A CB   1 
ATOM   2243 C  CG1  . ILE   A 1 283 ? 87.077  57.931  17.476  1   34.66 ? 305 ILE   A CG1  1 
ATOM   2244 C  CG2  . ILE   A 1 283 ? 85.478  58.488  15.6    1   34.63 ? 305 ILE   A CG2  1 
ATOM   2245 C  CD1  . ILE   A 1 283 ? 88.07   57.142  16.643  1   35.56 ? 305 ILE   A CD1  1 
ATOM   2246 N  N    . THR   A 1 284 ? 82.363  58.004  17.606  1   35.21 ? 306 THR   A N    1 
ATOM   2247 C  CA   . THR   A 1 284 ? 80.983  58.236  17.202  1   35.64 ? 306 THR   A CA   1 
ATOM   2248 C  C    . THR   A 1 284 ? 80.371  59.307  18.086  1   35.66 ? 306 THR   A C    1 
ATOM   2249 O  O    . THR   A 1 284 ? 79.692  60.176  17.569  1   36.03 ? 306 THR   A O    1 
ATOM   2250 C  CB   . THR   A 1 284 ? 80.173  56.932  17.241  1   36.75 ? 306 THR   A CB   1 
ATOM   2251 O  OG1  . THR   A 1 284 ? 80.781  56.005  16.354  1   37.36 ? 306 THR   A OG1  1 
ATOM   2252 C  CG2  . THR   A 1 284 ? 78.718  57.138  16.841  1   37.51 ? 306 THR   A CG2  1 
ATOM   2253 N  N    . LYS   A 1 285 ? 80.636  59.279  19.401  1   35.48 ? 307 LYS   A N    1 
ATOM   2254 C  CA   . LYS   A 1 285 ? 80.135  60.286  20.345  1   35.4  ? 307 LYS   A CA   1 
ATOM   2255 C  C    . LYS   A 1 285 ? 80.7    61.654  20.006  1   36.42 ? 307 LYS   A C    1 
ATOM   2256 O  O    . LYS   A 1 285 ? 79.969  62.639  20.106  1   37.3  ? 307 LYS   A O    1 
ATOM   2257 C  CB   . LYS   A 1 285 ? 80.44   59.918  21.802  1   36.23 ? 307 LYS   A CB   1 
ATOM   2258 C  CG   . LYS   A 1 285 ? 79.5    58.853  22.363  1   37.57 ? 307 LYS   A CG   1 
ATOM   2259 C  CD   . LYS   A 1 285 ? 79.827  58.475  23.795  1   40.03 ? 307 LYS   A CD   1 
ATOM   2260 C  CE   . LYS   A 1 285 ? 79.087  57.219  24.179  1   43.33 ? 307 LYS   A CE   1 
ATOM   2261 N  NZ   . LYS   A 1 285 ? 79.344  56.843  25.597  1   46.37 ? 307 LYS   A NZ   1 
ATOM   2262 N  N    . TRP   A 1 286 ? 81.974  61.733  19.554  1   36.03 ? 308 TRP   A N    1 
ATOM   2263 C  CA   . TRP   A 1 286 ? 82.538  63.016  19.13   1   36    ? 308 TRP   A CA   1 
ATOM   2264 C  C    . TRP   A 1 286 ? 81.797  63.473  17.864  1   35.26 ? 308 TRP   A C    1 
ATOM   2265 O  O    . TRP   A 1 286 ? 81.458  64.64   17.747  1   35.08 ? 308 TRP   A O    1 
ATOM   2266 C  CB   . TRP   A 1 286 ? 84.071  62.958  18.868  1   36.34 ? 308 TRP   A CB   1 
ATOM   2267 C  CG   . TRP   A 1 286 ? 84.579  64.291  18.391  1   37.34 ? 308 TRP   A CG   1 
ATOM   2268 C  CD1  . TRP   A 1 286 ? 84.812  65.392  19.164  1   38.1  ? 308 TRP   A CD1  1 
ATOM   2269 C  CD2  . TRP   A 1 286 ? 84.617  64.745  17.026  1   37.87 ? 308 TRP   A CD2  1 
ATOM   2270 N  NE1  . TRP   A 1 286 ? 85.043  66.487  18.371  1   38.67 ? 308 TRP   A NE1  1 
ATOM   2271 C  CE2  . TRP   A 1 286 ? 84.935  66.119  17.052  1   38.72 ? 308 TRP   A CE2  1 
ATOM   2272 C  CE3  . TRP   A 1 286 ? 84.417  64.122  15.787  1   38.22 ? 308 TRP   A CE3  1 
ATOM   2273 C  CZ2  . TRP   A 1 286 ? 85.093  66.871  15.886  1   39.3  ? 308 TRP   A CZ2  1 
ATOM   2274 C  CZ3  . TRP   A 1 286 ? 84.542  64.875  14.637  1   39.3  ? 308 TRP   A CZ3  1 
ATOM   2275 C  CH2  . TRP   A 1 286 ? 84.871  66.232  14.691  1   39.51 ? 308 TRP   A CH2  1 
ATOM   2276 N  N    . ARG   A 1 287 ? 81.554  62.554  16.916  1   35.23 ? 309 ARG   A N    1 
ATOM   2277 C  CA   . ARG   A 1 287 ? 80.83   62.864  15.674  1   35.05 ? 309 ARG   A CA   1 
ATOM   2278 C  C    . ARG   A 1 287 ? 79.438  63.436  15.981  1   35.79 ? 309 ARG   A C    1 
ATOM   2279 O  O    . ARG   A 1 287 ? 79.066  64.454  15.414  1   36.01 ? 309 ARG   A O    1 
ATOM   2280 C  CB   . ARG   A 1 287 ? 80.686  61.614  14.791  1   34.95 ? 309 ARG   A CB   1 
ATOM   2281 C  CG   . ARG   A 1 287 ? 81.972  61.094  14.166  1   35.27 ? 309 ARG   A CG   1 
ATOM   2282 C  CD   . ARG   A 1 287 ? 81.648  59.993  13.163  1   33.71 ? 309 ARG   A CD   1 
ATOM   2283 N  NE   . ARG   A 1 287 ? 82.8    59.144  12.851  1   33.58 ? 309 ARG   A NE   1 
ATOM   2284 C  CZ   . ARG   A 1 287 ? 83.743  59.449  11.964  1   34.28 ? 309 ARG   A CZ   1 
ATOM   2285 N  NH1  . ARG   A 1 287 ? 84.745  58.61   11.738  1   33.92 ? 309 ARG   A NH1  1 
ATOM   2286 N  NH2  . ARG   A 1 287 ? 83.704  60.607  11.313  1   33.35 ? 309 ARG   A NH2  1 
ATOM   2287 N  N    . TYR   A 1 288 ? 78.707  62.822  16.908  1   36.19 ? 310 TYR   A N    1 
ATOM   2288 C  CA   . TYR   A 1 288 ? 77.378  63.268  17.284  1   38.16 ? 310 TYR   A CA   1 
ATOM   2289 C  C    . TYR   A 1 288 ? 77.435  64.646  17.935  1   38.45 ? 310 TYR   A C    1 
ATOM   2290 O  O    . TYR   A 1 288 ? 76.71   65.538  17.505  1   38.54 ? 310 TYR   A O    1 
ATOM   2291 C  CB   . TYR   A 1 288 ? 76.703  62.228  18.198  1   39.87 ? 310 TYR   A CB   1 
ATOM   2292 C  CG   . TYR   A 1 288 ? 75.354  62.662  18.731  1   43.43 ? 310 TYR   A CG   1 
ATOM   2293 C  CD1  . TYR   A 1 288 ? 74.223  62.631  17.927  1   45.76 ? 310 TYR   A CD1  1 
ATOM   2294 C  CD2  . TYR   A 1 288 ? 75.21   63.109  20.038  1   45.31 ? 310 TYR   A CD2  1 
ATOM   2295 C  CE1  . TYR   A 1 288 ? 72.98   63.034  18.412  1   47.41 ? 310 TYR   A CE1  1 
ATOM   2296 C  CE2  . TYR   A 1 288 ? 73.975  63.517  20.531  1   47.01 ? 310 TYR   A CE2  1 
ATOM   2297 C  CZ   . TYR   A 1 288 ? 72.857  63.465  19.72   1   48.91 ? 310 TYR   A CZ   1 
ATOM   2298 O  OH   . TYR   A 1 288 ? 71.636  63.886  20.213  1   51.88 ? 310 TYR   A OH   1 
ATOM   2299 N  N    . ASN   A 1 289 ? 78.34   64.849  18.915  1   38.11 ? 311 ASN   A N    1 
ATOM   2300 C  CA   . ASN   A 1 289 ? 78.473  66.146  19.568  1   38.47 ? 311 ASN   A CA   1 
ATOM   2301 C  C    . ASN   A 1 289 ? 78.921  67.242  18.612  1   38.51 ? 311 ASN   A C    1 
ATOM   2302 O  O    . ASN   A 1 289 ? 78.482  68.383  18.752  1   38.61 ? 311 ASN   A O    1 
ATOM   2303 C  CB   . ASN   A 1 289 ? 79.356  66.067  20.803  1   39.39 ? 311 ASN   A CB   1 
ATOM   2304 C  CG   . ASN   A 1 289 ? 78.616  65.465  21.969  1   42.72 ? 311 ASN   A CG   1 
ATOM   2305 O  OD1  . ASN   A 1 289 ? 78.585  64.242  22.174  1   44.59 ? 311 ASN   A OD1  1 
ATOM   2306 N  ND2  . ASN   A 1 289 ? 77.962  66.3    22.737  1   43.43 ? 311 ASN   A ND2  1 
ATOM   2307 N  N    . HIS   A 1 290 ? 79.757  66.902  17.634  1   38.66 ? 312 HIS   A N    1 
ATOM   2308 C  CA   . HIS   A 1 290 ? 80.204  67.848  16.623  1   39.73 ? 312 HIS   A CA   1 
ATOM   2309 C  C    . HIS   A 1 290 ? 79.012  68.289  15.742  1   41.93 ? 312 HIS   A C    1 
ATOM   2310 O  O    . HIS   A 1 290 ? 78.838  69.497  15.571  1   42.12 ? 312 HIS   A O    1 
ATOM   2311 C  CB   . HIS   A 1 290 ? 81.343  67.254  15.784  1   39.5  ? 312 HIS   A CB   1 
ATOM   2312 C  CG   . HIS   A 1 290 ? 81.748  68.084  14.601  1   40.76 ? 312 HIS   A CG   1 
ATOM   2313 N  ND1  . HIS   A 1 290 ? 81.414  67.707  13.317  1   42.28 ? 312 HIS   A ND1  1 
ATOM   2314 C  CD2  . HIS   A 1 290 ? 82.455  69.239  14.544  1   42.05 ? 312 HIS   A CD2  1 
ATOM   2315 C  CE1  . HIS   A 1 290 ? 81.915  68.632  12.519  1   42.96 ? 312 HIS   A CE1  1 
ATOM   2316 N  NE2  . HIS   A 1 290 ? 82.556  69.577  13.211  1   43.13 ? 312 HIS   A NE2  1 
ATOM   2317 N  N    . VAL   A 1 291 ? 78.152  67.336  15.246  1   42.61 ? 313 VAL   A N    1 
ATOM   2318 C  CA   . VAL   A 1 291 ? 76.983  67.689  14.418  1   43.54 ? 313 VAL   A CA   1 
ATOM   2319 C  C    . VAL   A 1 291 ? 75.999  68.56   15.206  1   42.85 ? 313 VAL   A C    1 
ATOM   2320 O  O    . VAL   A 1 291 ? 75.434  69.486  14.637  1   42.62 ? 313 VAL   A O    1 
ATOM   2321 C  CB   . VAL   A 1 291 ? 76.229  66.489  13.75   1   45.07 ? 313 VAL   A CB   1 
ATOM   2322 C  CG1  . VAL   A 1 291 ? 75.4    66.967  12.567  1   45.89 ? 313 VAL   A CG1  1 
ATOM   2323 C  CG2  . VAL   A 1 291 ? 77.184  65.425  13.274  1   45.7  ? 313 VAL   A CG2  1 
ATOM   2324 N  N    . ILE   A 1 292 ? 75.796  68.275  16.502  1   42.24 ? 314 ILE   A N    1 
ATOM   2325 C  CA   . ILE   A 1 292 ? 74.902  69.083  17.326  1   43.09 ? 314 ILE   A CA   1 
ATOM   2326 C  C    . ILE   A 1 292 ? 75.445  70.527  17.43   1   43.88 ? 314 ILE   A C    1 
ATOM   2327 O  O    . ILE   A 1 292 ? 74.679  71.495  17.323  1   44.55 ? 314 ILE   A O    1 
ATOM   2328 C  CB   . ILE   A 1 292 ? 74.667  68.454  18.722  1   43.89 ? 314 ILE   A CB   1 
ATOM   2329 C  CG1  . ILE   A 1 292 ? 74.107  67.031  18.643  1   45.25 ? 314 ILE   A CG1  1 
ATOM   2330 C  CG2  . ILE   A 1 292 ? 73.8    69.34   19.622  1   44.32 ? 314 ILE   A CG2  1 
ATOM   2331 C  CD1  . ILE   A 1 292 ? 72.792  66.902  17.873  1   47.28 ? 314 ILE   A CD1  1 
ATOM   2332 N  N    . MET   A 1 293 ? 76.771  70.669  17.582  1   43.1  ? 315 MET   A N    1 
ATOM   2333 C  CA   . MET   A 1 293 ? 77.398  71.987  17.668  1   42.51 ? 315 MET   A CA   1 
ATOM   2334 C  C    . MET   A 1 293 ? 77.284  72.734  16.343  1   42.56 ? 315 MET   A C    1 
ATOM   2335 O  O    . MET   A 1 293 ? 76.948  73.915  16.338  1   42.24 ? 315 MET   A O    1 
ATOM   2336 C  CB   . MET   A 1 293 ? 78.864  71.876  18.118  1   42.04 ? 315 MET   A CB   1 
ATOM   2337 C  CG   . MET   A 1 293 ? 79.64   73.199  18.027  1   42.13 ? 315 MET   A CG   1 
ATOM   2338 S  SD   . MET   A 1 293 ? 81.354  73.095  18.566  1   39.84 ? 315 MET   A SD   1 
ATOM   2339 C  CE   . MET   A 1 293 ? 81.912  71.635  17.654  1   32.21 ? 315 MET   A CE   1 
ATOM   2340 N  N    . VAL   A 1 294 ? 77.544  72.04   15.215  1   42.99 ? 316 VAL   A N    1 
ATOM   2341 C  CA   . VAL   A 1 294 ? 77.421  72.59   13.866  1   43.65 ? 316 VAL   A CA   1 
ATOM   2342 C  C    . VAL   A 1 294 ? 75.985  73.108  13.671  1   44.89 ? 316 VAL   A C    1 
ATOM   2343 O  O    . VAL   A 1 294 ? 75.793  74.259  13.286  1   44.91 ? 316 VAL   A O    1 
ATOM   2344 C  CB   . VAL   A 1 294 ? 77.776  71.539  12.785  1   43.82 ? 316 VAL   A CB   1 
ATOM   2345 C  CG1  . VAL   A 1 294 ? 77.434  72.052  11.387  1   44.56 ? 316 VAL   A CG1  1 
ATOM   2346 C  CG2  . VAL   A 1 294 ? 79.239  71.12   12.865  1   43.28 ? 316 VAL   A CG2  1 
ATOM   2347 N  N    . GLN   A 1 295 ? 74.993  72.295  14.048  1   45.61 ? 317 GLN   A N    1 
ATOM   2348 C  CA   . GLN   A 1 295 ? 73.597  72.692  13.932  1   47.01 ? 317 GLN   A CA   1 
ATOM   2349 C  C    . GLN   A 1 295 ? 73.21   73.865  14.826  1   48.11 ? 317 GLN   A C    1 
ATOM   2350 O  O    . GLN   A 1 295 ? 72.428  74.72   14.39   1   48.78 ? 317 GLN   A O    1 
ATOM   2351 C  CB   . GLN   A 1 295 ? 72.65   71.519  14.158  1   48.4  ? 317 GLN   A CB   1 
ATOM   2352 C  CG   . GLN   A 1 295 ? 71.294  71.796  13.548  1   52.15 ? 317 GLN   A CG   1 
ATOM   2353 C  CD   . GLN   A 1 295 ? 70.295  70.696  13.763  1   57.64 ? 317 GLN   A CD   1 
ATOM   2354 O  OE1  . GLN   A 1 295 ? 70.47   69.807  14.61   1   58.45 ? 317 GLN   A OE1  1 
ATOM   2355 N  NE2  . GLN   A 1 295 ? 69.207  70.74   12.992  1   58.49 ? 317 GLN   A NE2  1 
ATOM   2356 N  N    . ARG   A 1 296 ? 73.754  73.933  16.046  1   48.01 ? 318 ARG   A N    1 
ATOM   2357 C  CA   . ARG   A 1 296 ? 73.443  75.061  16.906  1   48.69 ? 318 ARG   A CA   1 
ATOM   2358 C  C    . ARG   A 1 296 ? 74.19   76.344  16.448  1   48.22 ? 318 ARG   A C    1 
ATOM   2359 O  O    . ARG   A 1 296 ? 73.676  77.431  16.673  1   48.61 ? 318 ARG   A O    1 
ATOM   2360 C  CB   . ARG   A 1 296 ? 73.623  74.734  18.392  1   51.39 ? 318 ARG   A CB   1 
ATOM   2361 C  CG   . ARG   A 1 296 ? 75.029  74.907  18.922  1   57.1  ? 318 ARG   A CG   1 
ATOM   2362 C  CD   . ARG   A 1 296 ? 75.038  75.054  20.437  1   61.29 ? 318 ARG   A CD   1 
ATOM   2363 N  NE   . ARG   A 1 296 ? 75.015  73.752  21.097  1   65.05 ? 318 ARG   A NE   1 
ATOM   2364 C  CZ   . ARG   A 1 296 ? 74.094  73.368  21.973  1   68.68 ? 318 ARG   A CZ   1 
ATOM   2365 N  NH1  . ARG   A 1 296 ? 73.146  74.213  22.367  1   68.29 ? 318 ARG   A NH1  1 
ATOM   2366 N  NH2  . ARG   A 1 296 ? 74.156  72.161  22.521  1   69.15 ? 318 ARG   A NH2  1 
ATOM   2367 N  N    . MET   A 1 297 ? 75.323  76.231  15.741  1   47.66 ? 319 MET   A N    1 
ATOM   2368 C  CA   . MET   A 1 297 ? 76.035  77.42   15.261  1   48.32 ? 319 MET   A CA   1 
ATOM   2369 C  C    . MET   A 1 297 ? 75.5    77.967  13.964  1   49    ? 319 MET   A C    1 
ATOM   2370 O  O    . MET   A 1 297 ? 75.372  79.174  13.846  1   49.42 ? 319 MET   A O    1 
ATOM   2371 C  CB   . MET   A 1 297 ? 77.532  77.162  15.062  1   49.04 ? 319 MET   A CB   1 
ATOM   2372 C  CG   . MET   A 1 297 ? 78.267  76.988  16.316  1   51.33 ? 319 MET   A CG   1 
ATOM   2373 S  SD   . MET   A 1 297 ? 78.498  78.485  17.294  1   52.76 ? 319 MET   A SD   1 
ATOM   2374 C  CE   . MET   A 1 297 ? 79.449  77.762  18.564  1   50.53 ? 319 MET   A CE   1 
ATOM   2375 N  N    . ILE   A 1 298 ? 75.305  77.101  12.947  1   49.03 ? 320 ILE   A N    1 
ATOM   2376 C  CA   . ILE   A 1 298 ? 74.923  77.505  11.595  1   48.99 ? 320 ILE   A CA   1 
ATOM   2377 C  C    . ILE   A 1 298 ? 73.712  76.756  11.028  1   49.29 ? 320 ILE   A C    1 
ATOM   2378 O  O    . ILE   A 1 298 ? 73.507  76.786  9.822   1   49.72 ? 320 ILE   A O    1 
ATOM   2379 C  CB   . ILE   A 1 298 ? 76.166  77.335  10.668  1   49.26 ? 320 ILE   A CB   1 
ATOM   2380 C  CG1  . ILE   A 1 298 ? 76.614  75.856  10.604  1   49.77 ? 320 ILE   A CG1  1 
ATOM   2381 C  CG2  . ILE   A 1 298 ? 77.331  78.249  11.106  1   49.61 ? 320 ILE   A CG2  1 
ATOM   2382 C  CD1  . ILE   A 1 298 ? 77.814  75.556  9.722   1   50.58 ? 320 ILE   A CD1  1 
ATOM   2383 N  N    . GLY   A 1 299 ? 72.937  76.084  11.878  1   48.99 ? 321 GLY   A N    1 
ATOM   2384 C  CA   . GLY   A 1 299 ? 71.768  75.312  11.468  1   49.04 ? 321 GLY   A CA   1 
ATOM   2385 C  C    . GLY   A 1 299 ? 72.066  74.204  10.476  1   49.27 ? 321 GLY   A C    1 
ATOM   2386 O  O    . GLY   A 1 299 ? 73.224  73.807  10.304  1   49.43 ? 321 GLY   A O    1 
ATOM   2387 N  N    . SER   A 1 300 ? 71.022  73.685  9.807   1   49.18 ? 322 SER   A N    1 
ATOM   2388 C  CA   . SER   A 1 300 ? 71.204  72.681  8.75    1   49.1  ? 322 SER   A CA   1 
ATOM   2389 C  C    . SER   A 1 300 ? 71.78   73.33   7.455   1   49.1  ? 322 SER   A C    1 
ATOM   2390 O  O    . SER   A 1 300 ? 72.402  72.642  6.635   1   49.07 ? 322 SER   A O    1 
ATOM   2391 C  CB   . SER   A 1 300 ? 69.894  71.96   8.458   1   49.63 ? 322 SER   A CB   1 
ATOM   2392 N  N    . GLN   A 1 301 ? 71.602  74.664  7.3     1   49.07 ? 323 GLN   A N    1 
ATOM   2393 C  CA   . GLN   A 1 301 ? 72.13   75.432  6.176   1   49.78 ? 323 GLN   A CA   1 
ATOM   2394 C  C    . GLN   A 1 301 ? 72.197  76.922  6.494   1   50.9  ? 323 GLN   A C    1 
ATOM   2395 O  O    . GLN   A 1 301 ? 71.368  77.449  7.236   1   50.48 ? 323 GLN   A O    1 
ATOM   2396 C  CB   . GLN   A 1 301 ? 71.37   75.162  4.871   1   50.13 ? 323 GLN   A CB   1 
ATOM   2397 C  CG   . GLN   A 1 301 ? 69.86   75.249  4.982   1   51.18 ? 323 GLN   A CG   1 
ATOM   2398 C  CD   . GLN   A 1 301 ? 69.224  74.902  3.649   1   53.29 ? 323 GLN   A CD   1 
ATOM   2399 O  OE1  . GLN   A 1 301 ? 69.443  75.576  2.629   1   54.43 ? 323 GLN   A OE1  1 
ATOM   2400 N  NE2  . GLN   A 1 301 ? 68.429  73.848  3.626   1   52.59 ? 323 GLN   A NE2  1 
ATOM   2401 N  N    . GLN   A 1 302 ? 73.222  77.588  5.97    1   52.01 ? 324 GLN   A N    1 
ATOM   2402 C  CA   . GLN   A 1 302 ? 73.415  79.017  6.207   1   53.43 ? 324 GLN   A CA   1 
ATOM   2403 C  C    . GLN   A 1 302 ? 74.108  79.684  5.006   1   54.64 ? 324 GLN   A C    1 
ATOM   2404 O  O    . GLN   A 1 302 ? 74.568  78.996  4.092   1   54.56 ? 324 GLN   A O    1 
ATOM   2405 C  CB   . GLN   A 1 302 ? 74.23   79.249  7.507   1   54.52 ? 324 GLN   A CB   1 
ATOM   2406 C  CG   . GLN   A 1 302 ? 73.407  79.789  8.682   1   56.75 ? 324 GLN   A CG   1 
ATOM   2407 C  CD   . GLN   A 1 302 ? 72.855  81.175  8.468   1   59.92 ? 324 GLN   A CD   1 
ATOM   2408 O  OE1  . GLN   A 1 302 ? 73.367  81.975  7.669   1   61.87 ? 324 GLN   A OE1  1 
ATOM   2409 N  NE2  . GLN   A 1 302 ? 71.803  81.493  9.19    1   59.78 ? 324 GLN   A NE2  1 
ATOM   2410 N  N    . LEU   A 1 303 ? 74.212  81.029  5.021   1   55.62 ? 325 LEU   A N    1 
ATOM   2411 C  CA   . LEU   A 1 303 ? 74.897  81.791  3.979   1   56.89 ? 325 LEU   A CA   1 
ATOM   2412 C  C    . LEU   A 1 303 ? 76.361  81.348  3.937   1   58.09 ? 325 LEU   A C    1 
ATOM   2413 O  O    . LEU   A 1 303 ? 77.055  81.398  4.945   1   58.47 ? 325 LEU   A O    1 
ATOM   2414 C  CB   . LEU   A 1 303 ? 74.807  83.299  4.265   1   56.98 ? 325 LEU   A CB   1 
ATOM   2415 N  N    . GLY   A 1 304 ? 76.771  80.818  2.807   1   58.5  ? 326 GLY   A N    1 
ATOM   2416 C  CA   . GLY   A 1 304 ? 78.122  80.313  2.626   1   59.42 ? 326 GLY   A CA   1 
ATOM   2417 C  C    . GLY   A 1 304 ? 78.193  78.804  2.508   1   60.12 ? 326 GLY   A C    1 
ATOM   2418 O  O    . GLY   A 1 304 ? 79.2    78.272  2.038   1   60.71 ? 326 GLY   A O    1 
ATOM   2419 N  N    . THR   A 1 305 ? 77.126  78.095  2.904   1   59.87 ? 327 THR   A N    1 
ATOM   2420 C  CA   . THR   A 1 305 ? 77.127  76.632  2.855   1   59.91 ? 327 THR   A CA   1 
ATOM   2421 C  C    . THR   A 1 305 ? 76.562  76.048  1.55    1   59.78 ? 327 THR   A C    1 
ATOM   2422 O  O    . THR   A 1 305 ? 76.739  74.859  1.307   1   60.26 ? 327 THR   A O    1 
ATOM   2423 C  CB   . THR   A 1 305 ? 76.419  76.041  4.093   1   61.12 ? 327 THR   A CB   1 
ATOM   2424 O  OG1  . THR   A 1 305 ? 74.998  76.161  3.961   1   62.06 ? 327 THR   A OG1  1 
ATOM   2425 C  CG2  . THR   A 1 305 ? 76.895  76.676  5.403   1   61.35 ? 327 THR   A CG2  1 
ATOM   2426 N  N    . GLY   A 1 306 ? 75.882  76.858  0.741   1   59.02 ? 328 GLY   A N    1 
ATOM   2427 C  CA   . GLY   A 1 306 ? 75.292  76.397  -0.511  1   58.67 ? 328 GLY   A CA   1 
ATOM   2428 C  C    . GLY   A 1 306 ? 74.304  75.263  -0.33   1   57.94 ? 328 GLY   A C    1 
ATOM   2429 O  O    . GLY   A 1 306 ? 74.34   74.273  -1.068  1   58.03 ? 328 GLY   A O    1 
ATOM   2430 N  N    . GLY   A 1 307 ? 73.457  75.378  0.681   1   57.25 ? 329 GLY   A N    1 
ATOM   2431 C  CA   . GLY   A 1 307 ? 72.491  74.326  0.974   1   57.33 ? 329 GLY   A CA   1 
ATOM   2432 C  C    . GLY   A 1 307 ? 72.873  73.475  2.171   1   56.77 ? 329 GLY   A C    1 
ATOM   2433 O  O    . GLY   A 1 307 ? 73.753  73.848  2.945   1   56.56 ? 329 GLY   A O    1 
ATOM   2434 N  N    . SER   A 1 308 ? 72.209  72.327  2.336   1   56.31 ? 330 SER   A N    1 
ATOM   2435 C  CA   . SER   A 1 308 ? 72.408  71.473  3.497   1   56.39 ? 330 SER   A CA   1 
ATOM   2436 C  C    . SER   A 1 308 ? 73.306  70.255  3.3     1   55.83 ? 330 SER   A C    1 
ATOM   2437 O  O    . SER   A 1 308 ? 73.343  69.408  4.186   1   56.06 ? 330 SER   A O    1 
ATOM   2438 C  CB   . SER   A 1 308 ? 71.059  71.018  4.046   1   57.75 ? 330 SER   A CB   1 
ATOM   2439 O  OG   . SER   A 1 308 ? 70.329  70.272  3.086   1   59.97 ? 330 SER   A OG   1 
ATOM   2440 N  N    . SER   A 1 309 ? 74.041  70.169  2.191   1   55.08 ? 331 SER   A N    1 
ATOM   2441 C  CA   . SER   A 1 309 ? 74.909  69.018  1.923   1   55.1  ? 331 SER   A CA   1 
ATOM   2442 C  C    . SER   A 1 309 ? 75.987  68.744  3.003   1   54.48 ? 331 SER   A C    1 
ATOM   2443 O  O    . SER   A 1 309 ? 76.248  67.577  3.305   1   54.72 ? 331 SER   A O    1 
ATOM   2444 C  CB   . SER   A 1 309 ? 75.549  69.132  0.543   1   56.39 ? 331 SER   A CB   1 
ATOM   2445 O  OG   . SER   A 1 309 ? 76.042  70.44   0.294   1   59.04 ? 331 SER   A OG   1 
ATOM   2446 N  N    . GLY   A 1 310 ? 76.582  69.8    3.567   1   53.31 ? 332 GLY   A N    1 
ATOM   2447 C  CA   . GLY   A 1 310 ? 77.601  69.669  4.611   1   52.51 ? 332 GLY   A CA   1 
ATOM   2448 C  C    . GLY   A 1 310 ? 77.03   69.013  5.85    1   51.41 ? 332 GLY   A C    1 
ATOM   2449 O  O    . GLY   A 1 310 ? 77.557  68.007  6.33    1   51.57 ? 332 GLY   A O    1 
ATOM   2450 N  N    . TYR   A 1 311 ? 75.896  69.542  6.324   1   50.15 ? 333 TYR   A N    1 
ATOM   2451 C  CA   . TYR   A 1 311 ? 75.177  69.028  7.482   1   49.48 ? 333 TYR   A CA   1 
ATOM   2452 C  C    . TYR   A 1 311 ? 74.743  67.58   7.242   1   49.44 ? 333 TYR   A C    1 
ATOM   2453 O  O    . TYR   A 1 311 ? 74.911  66.727  8.11    1   49.08 ? 333 TYR   A O    1 
ATOM   2454 C  CB   . TYR   A 1 311 ? 73.96   69.926  7.791   1   48.87 ? 333 TYR   A CB   1 
ATOM   2455 C  CG   . TYR   A 1 311 ? 73.068  69.385  8.886   1   49.28 ? 333 TYR   A CG   1 
ATOM   2456 C  CD1  . TYR   A 1 311 ? 73.456  69.443  10.217  1   49.98 ? 333 TYR   A CD1  1 
ATOM   2457 C  CD2  . TYR   A 1 311 ? 71.845  68.804  8.59    1   49.93 ? 333 TYR   A CD2  1 
ATOM   2458 C  CE1  . TYR   A 1 311 ? 72.642  68.95   11.228  1   50.58 ? 333 TYR   A CE1  1 
ATOM   2459 C  CE2  . TYR   A 1 311 ? 71.025  68.302  9.592   1   50.72 ? 333 TYR   A CE2  1 
ATOM   2460 C  CZ   . TYR   A 1 311 ? 71.428  68.379  10.912  1   51.62 ? 333 TYR   A CZ   1 
ATOM   2461 O  OH   . TYR   A 1 311 ? 70.629  67.896  11.921  1   53.19 ? 333 TYR   A OH   1 
ATOM   2462 N  N    . GLN   A 1 312 ? 74.181  67.305  6.063   1   49.77 ? 334 GLN   A N    1 
ATOM   2463 C  CA   . GLN   A 1 312 ? 73.712  65.967  5.726   1   50.08 ? 334 GLN   A CA   1 
ATOM   2464 C  C    . GLN   A 1 312 ? 74.849  64.975  5.623   1   49.59 ? 334 GLN   A C    1 
ATOM   2465 O  O    . GLN   A 1 312 ? 74.68   63.839  6.061   1   49.93 ? 334 GLN   A O    1 
ATOM   2466 C  CB   . GLN   A 1 312 ? 72.824  65.968  4.478   1   52.07 ? 334 GLN   A CB   1 
ATOM   2467 C  CG   . GLN   A 1 312 ? 71.469  66.623  4.732   1   56.6  ? 334 GLN   A CG   1 
ATOM   2468 C  CD   . GLN   A 1 312 ? 70.61   65.928  5.772   1   63.18 ? 334 GLN   A CD   1 
ATOM   2469 O  OE1  . GLN   A 1 312 ? 69.764  66.562  6.427   1   65.45 ? 334 GLN   A OE1  1 
ATOM   2470 N  NE2  . GLN   A 1 312 ? 70.767  64.611  5.94    1   64.45 ? 334 GLN   A NE2  1 
ATOM   2471 N  N    . TYR   A 1 313 ? 76.035  65.406  5.144   1   48.92 ? 335 TYR   A N    1 
ATOM   2472 C  CA   . TYR   A 1 313 ? 77.217  64.54   5.125   1   49.31 ? 335 TYR   A CA   1 
ATOM   2473 C  C    . TYR   A 1 313 ? 77.592  64.191  6.581   1   49.42 ? 335 TYR   A C    1 
ATOM   2474 O  O    . TYR   A 1 313 ? 77.815  63.021  6.888   1   49.74 ? 335 TYR   A O    1 
ATOM   2475 C  CB   . TYR   A 1 313 ? 78.423  65.197  4.404   1   49.77 ? 335 TYR   A CB   1 
ATOM   2476 C  CG   . TYR   A 1 313 ? 79.753  64.541  4.759   1   51.07 ? 335 TYR   A CG   1 
ATOM   2477 C  CD1  . TYR   A 1 313 ? 80.119  63.318  4.208   1   52.16 ? 335 TYR   A CD1  1 
ATOM   2478 C  CD2  . TYR   A 1 313 ? 80.58   65.082  5.738   1   51.93 ? 335 TYR   A CD2  1 
ATOM   2479 C  CE1  . TYR   A 1 313 ? 81.302  62.68   4.578   1   52.85 ? 335 TYR   A CE1  1 
ATOM   2480 C  CE2  . TYR   A 1 313 ? 81.735  64.426  6.153   1   52.59 ? 335 TYR   A CE2  1 
ATOM   2481 C  CZ   . TYR   A 1 313 ? 82.113  63.244  5.545   1   53.59 ? 335 TYR   A CZ   1 
ATOM   2482 O  OH   . TYR   A 1 313 ? 83.286  62.621  5.906   1   55.01 ? 335 TYR   A OH   1 
ATOM   2483 N  N    . LEU   A 1 314 ? 77.631  65.199  7.472   1   48.84 ? 336 LEU   A N    1 
ATOM   2484 C  CA   . LEU   A 1 314 ? 77.978  64.97   8.869   1   48.59 ? 336 LEU   A CA   1 
ATOM   2485 C  C    . LEU   A 1 314 ? 77.002  64.009  9.54    1   48.49 ? 336 LEU   A C    1 
ATOM   2486 O  O    . LEU   A 1 314 ? 77.446  63.128  10.274  1   48.23 ? 336 LEU   A O    1 
ATOM   2487 C  CB   . LEU   A 1 314 ? 78.076  66.288  9.637   1   48.4  ? 336 LEU   A CB   1 
ATOM   2488 C  CG   . LEU   A 1 314 ? 79.198  67.234  9.197   1   49.32 ? 336 LEU   A CG   1 
ATOM   2489 C  CD1  . LEU   A 1 314 ? 79.092  68.57   9.919   1   49.48 ? 336 LEU   A CD1  1 
ATOM   2490 C  CD2  . LEU   A 1 314 ? 80.576  66.601  9.399   1   49.55 ? 336 LEU   A CD2  1 
ATOM   2491 N  N    . ARG   A 1 315 ? 75.691  64.12   9.239   1   48.14 ? 337 ARG   A N    1 
ATOM   2492 C  CA   . ARG   A 1 315 ? 74.702  63.198  9.81    1   48.71 ? 337 ARG   A CA   1 
ATOM   2493 C  C    . ARG   A 1 315 ? 74.914  61.751  9.304   1   48.07 ? 337 ARG   A C    1 
ATOM   2494 O  O    . ARG   A 1 315 ? 74.663  60.803  10.044  1   48.12 ? 337 ARG   A O    1 
ATOM   2495 C  CB   . ARG   A 1 315 ? 73.265  63.65   9.505   1   51.4  ? 337 ARG   A CB   1 
ATOM   2496 C  CG   . ARG   A 1 315 ? 72.875  64.979  10.13   1   57.22 ? 337 ARG   A CG   1 
ATOM   2497 C  CD   . ARG   A 1 315 ? 72.568  64.845  11.605  1   63.23 ? 337 ARG   A CD   1 
ATOM   2498 N  NE   . ARG   A 1 315 ? 71.216  64.353  11.859  1   69.01 ? 337 ARG   A NE   1 
ATOM   2499 C  CZ   . ARG   A 1 315 ? 70.621  64.383  13.051  1   72.46 ? 337 ARG   A CZ   1 
ATOM   2500 N  NH1  . ARG   A 1 315 ? 71.253  64.89   14.106  1   71.62 ? 337 ARG   A NH1  1 
ATOM   2501 N  NH2  . ARG   A 1 315 ? 69.382  63.924  13.194  1   72.89 ? 337 ARG   A NH2  1 
ATOM   2502 N  N    . SER   A 1 316 ? 75.376  61.582  8.061   1   47.51 ? 338 SER   A N    1 
ATOM   2503 C  CA   . SER   A 1 316 ? 75.614  60.246  7.512   1   47.79 ? 338 SER   A CA   1 
ATOM   2504 C  C    . SER   A 1 316 ? 76.858  59.564  8.101   1   47.78 ? 338 SER   A C    1 
ATOM   2505 O  O    . SER   A 1 316 ? 76.947  58.332  8.053   1   48.36 ? 338 SER   A O    1 
ATOM   2506 C  CB   . SER   A 1 316 ? 75.653  60.267  5.988   1   48.7  ? 338 SER   A CB   1 
ATOM   2507 O  OG   . SER   A 1 316 ? 76.782  60.979  5.513   1   50.49 ? 338 SER   A OG   1 
ATOM   2508 N  N    . THR   A 1 317 ? 77.798  60.346  8.693   1   46.59 ? 339 THR   A N    1 
ATOM   2509 C  CA   . THR   A 1 317 ? 78.965  59.756  9.361   1   45.66 ? 339 THR   A CA   1 
ATOM   2510 C  C    . THR   A 1 317 ? 78.594  59.092  10.693  1   45.32 ? 339 THR   A C    1 
ATOM   2511 O  O    . THR   A 1 317 ? 79.416  58.364  11.243  1   45.45 ? 339 THR   A O    1 
ATOM   2512 C  CB   . THR   A 1 317 ? 80.112  60.751  9.53    1   46.43 ? 339 THR   A CB   1 
ATOM   2513 O  OG1  . THR   A 1 317 ? 79.744  61.74   10.485  1   46.76 ? 339 THR   A OG1  1 
ATOM   2514 C  CG2  . THR   A 1 317 ? 80.513  61.41   8.225   1   46.9  ? 339 THR   A CG2  1 
ATOM   2515 N  N    . LEU   A 1 318 ? 77.365  59.313  11.207  1   44.84 ? 340 LEU   A N    1 
ATOM   2516 C  CA   . LEU   A 1 318 ? 76.878  58.677  12.424  1   45.35 ? 340 LEU   A CA   1 
ATOM   2517 C  C    . LEU   A 1 318 ? 76.407  57.212  12.202  1   46.97 ? 340 LEU   A C    1 
ATOM   2518 O  O    . LEU   A 1 318 ? 76.027  56.54   13.16   1   47.42 ? 340 LEU   A O    1 
ATOM   2519 C  CB   . LEU   A 1 318 ? 75.73   59.493  13.019  1   45.13 ? 340 LEU   A CB   1 
ATOM   2520 C  CG   . LEU   A 1 318 ? 75.991  60.977  13.267  1   46.13 ? 340 LEU   A CG   1 
ATOM   2521 C  CD1  . LEU   A 1 318 ? 74.788  61.627  13.91   1   46.35 ? 340 LEU   A CD1  1 
ATOM   2522 C  CD2  . LEU   A 1 318 ? 77.184  61.174  14.156  1   46.47 ? 340 LEU   A CD2  1 
ATOM   2523 N  N    . SER   A 1 319 ? 76.416  56.725  10.956  1   47.63 ? 341 SER   A N    1 
ATOM   2524 C  CA   . SER   A 1 319 ? 75.977  55.372  10.647  1   48.71 ? 341 SER   A CA   1 
ATOM   2525 C  C    . SER   A 1 319 ? 77.043  54.319  10.963  1   49.14 ? 341 SER   A C    1 
ATOM   2526 O  O    . SER   A 1 319 ? 78.233  54.64   11.082  1   49.29 ? 341 SER   A O    1 
ATOM   2527 C  CB   . SER   A 1 319 ? 75.568  55.275  9.179   1   50.1  ? 341 SER   A CB   1 
ATOM   2528 O  OG   . SER   A 1 319 ? 76.708  55.319  8.336   1   53.04 ? 341 SER   A OG   1 
ATOM   2529 N  N    . ASP   A 1 320 ? 76.611  53.046  11.053  1   48.85 ? 342 ASP   A N    1 
ATOM   2530 C  CA   . ASP   A 1 320 ? 77.509  51.92   11.289  1   48.81 ? 342 ASP   A CA   1 
ATOM   2531 C  C    . ASP   A 1 320 ? 78.565  51.744  10.176  1   48.53 ? 342 ASP   A C    1 
ATOM   2532 O  O    . ASP   A 1 320 ? 79.519  51.002  10.372  1   48.8  ? 342 ASP   A O    1 
ATOM   2533 C  CB   . ASP   A 1 320 ? 76.707  50.628  11.519  1   50.35 ? 342 ASP   A CB   1 
ATOM   2534 C  CG   . ASP   A 1 320 ? 75.916  50.59   12.818  1   54.66 ? 342 ASP   A CG   1 
ATOM   2535 O  OD1  . ASP   A 1 320 ? 76.138  51.467  13.676  1   55.54 ? 342 ASP   A OD1  1 
ATOM   2536 O  OD2  . ASP   A 1 320 ? 75.082  49.673  12.978  1   56.75 ? 342 ASP   A OD2  1 
ATOM   2537 N  N    . ARG   A 1 321 ? 78.438  52.472  9.045   1   48.06 ? 343 ARG   A N    1 
ATOM   2538 C  CA   . ARG   A 1 321 ? 79.412  52.465  7.951   1   48.02 ? 343 ARG   A CA   1 
ATOM   2539 C  C    . ARG   A 1 321 ? 80.769  52.994  8.411   1   47.82 ? 343 ARG   A C    1 
ATOM   2540 O  O    . ARG   A 1 321 ? 81.796  52.598  7.859   1   48.43 ? 343 ARG   A O    1 
ATOM   2541 C  CB   . ARG   A 1 321 ? 78.911  53.315  6.769   1   49.56 ? 343 ARG   A CB   1 
ATOM   2542 N  N    . TYR   A 1 322 ? 80.778  53.923  9.39    1   46.84 ? 344 TYR   A N    1 
ATOM   2543 C  CA   . TYR   A 1 322 ? 82.009  54.501  9.93    1   45.96 ? 344 TYR   A CA   1 
ATOM   2544 C  C    . TYR   A 1 322 ? 82.521  53.797  11.211  1   44.43 ? 344 TYR   A C    1 
ATOM   2545 O  O    . TYR   A 1 322 ? 83.571  54.183  11.727  1   44.96 ? 344 TYR   A O    1 
ATOM   2546 C  CB   . TYR   A 1 322 ? 81.842  56.005  10.161  1   45.96 ? 344 TYR   A CB   1 
ATOM   2547 C  CG   . TYR   A 1 322 ? 81.899  56.806  8.882   1   46.52 ? 344 TYR   A CG   1 
ATOM   2548 C  CD1  . TYR   A 1 322 ? 80.787  56.917  8.056   1   47.22 ? 344 TYR   A CD1  1 
ATOM   2549 C  CD2  . TYR   A 1 322 ? 83.063  57.458  8.5     1   47    ? 344 TYR   A CD2  1 
ATOM   2550 C  CE1  . TYR   A 1 322 ? 80.829  57.671  6.887   1   47.89 ? 344 TYR   A CE1  1 
ATOM   2551 C  CE2  . TYR   A 1 322 ? 83.12   58.204  7.33    1   47.77 ? 344 TYR   A CE2  1 
ATOM   2552 C  CZ   . TYR   A 1 322 ? 82      58.318  6.527   1   48.7  ? 344 TYR   A CZ   1 
ATOM   2553 O  OH   . TYR   A 1 322 ? 82.06   59.084  5.378   1   49.57 ? 344 TYR   A OH   1 
ATOM   2554 N  N    . LYS   A 1 323 ? 81.775  52.807  11.732  1   42.18 ? 345 LYS   A N    1 
ATOM   2555 C  CA   . LYS   A 1 323 ? 82.157  52.021  12.901  1   41.12 ? 345 LYS   A CA   1 
ATOM   2556 C  C    . LYS   A 1 323 ? 83.176  50.997  12.402  1   39.2  ? 345 LYS   A C    1 
ATOM   2557 O  O    . LYS   A 1 323 ? 82.916  50.31   11.422  1   40.37 ? 345 LYS   A O    1 
ATOM   2558 C  CB   . LYS   A 1 323 ? 80.934  51.303  13.479  1   43.64 ? 345 LYS   A CB   1 
ATOM   2559 C  CG   . LYS   A 1 323 ? 80.936  51.179  14.991  1   48.93 ? 345 LYS   A CG   1 
ATOM   2560 C  CD   . LYS   A 1 323 ? 80.593  52.499  15.66   1   54.42 ? 345 LYS   A CD   1 
ATOM   2561 C  CE   . LYS   A 1 323 ? 80.317  52.343  17.133  1   58.01 ? 345 LYS   A CE   1 
ATOM   2562 N  NZ   . LYS   A 1 323 ? 79.484  53.463  17.651  1   60.66 ? 345 LYS   A NZ   1 
ATOM   2563 N  N    . VAL   A 1 324 ? 84.354  50.955  13.002  1   36.41 ? 346 VAL   A N    1 
ATOM   2564 C  CA   . VAL   A 1 324 ? 85.432  50.085  12.562  1   35.01 ? 346 VAL   A CA   1 
ATOM   2565 C  C    . VAL   A 1 324 ? 85.299  48.666  13.109  1   34.05 ? 346 VAL   A C    1 
ATOM   2566 O  O    . VAL   A 1 324 ? 85.376  47.704  12.354  1   33.48 ? 346 VAL   A O    1 
ATOM   2567 C  CB   . VAL   A 1 324 ? 86.803  50.719  12.92   1   34.94 ? 346 VAL   A CB   1 
ATOM   2568 C  CG1  . VAL   A 1 324 ? 87.953  49.778  12.601  1   34.77 ? 346 VAL   A CG1  1 
ATOM   2569 C  CG2  . VAL   A 1 324 ? 86.979  52.062  12.226  1   35    ? 346 VAL   A CG2  1 
ATOM   2570 N  N    . PHE   A 1 325 ? 85.109  48.53   14.42   1   33.66 ? 347 PHE   A N    1 
ATOM   2571 C  CA   . PHE   A 1 325 ? 85.031  47.227  15.067  1   33.76 ? 347 PHE   A CA   1 
ATOM   2572 C  C    . PHE   A 1 325 ? 83.593  46.836  15.32   1   34.83 ? 347 PHE   A C    1 
ATOM   2573 O  O    . PHE   A 1 325 ? 83.233  46.393  16.408  1   34.91 ? 347 PHE   A O    1 
ATOM   2574 C  CB   . PHE   A 1 325 ? 85.85   47.25   16.361  1   32.9  ? 347 PHE   A CB   1 
ATOM   2575 C  CG   . PHE   A 1 325 ? 87.326  47.414  16.086  1   32.37 ? 347 PHE   A CG   1 
ATOM   2576 C  CD1  . PHE   A 1 325 ? 88.104  46.33   15.735  1   32.23 ? 347 PHE   A CD1  1 
ATOM   2577 C  CD2  . PHE   A 1 325 ? 87.927  48.656  16.173  1   32.95 ? 347 PHE   A CD2  1 
ATOM   2578 C  CE1  . PHE   A 1 325 ? 89.454  46.483  15.479  1   33.11 ? 347 PHE   A CE1  1 
ATOM   2579 C  CE2  . PHE   A 1 325 ? 89.28   48.81   15.907  1   33.57 ? 347 PHE   A CE2  1 
ATOM   2580 C  CZ   . PHE   A 1 325 ? 90.039  47.719  15.576  1   33.29 ? 347 PHE   A CZ   1 
ATOM   2581 N  N    . LEU   A 1 326 ? 82.773  46.989  14.292  1   35.59 ? 348 LEU   A N    1 
ATOM   2582 C  CA   . LEU   A 1 326 ? 81.34   46.688  14.324  1   36.46 ? 348 LEU   A CA   1 
ATOM   2583 C  C    . LEU   A 1 326 ? 81.031  45.285  14.866  1   34.99 ? 348 LEU   A C    1 
ATOM   2584 O  O    . LEU   A 1 326 ? 80.113  45.139  15.661  1   35.21 ? 348 LEU   A O    1 
ATOM   2585 C  CB   . LEU   A 1 326 ? 80.764  46.862  12.903  1   37.78 ? 348 LEU   A CB   1 
ATOM   2586 C  CG   . LEU   A 1 326 ? 79.27   47.01   12.822  1   40.16 ? 348 LEU   A CG   1 
ATOM   2587 C  CD1  . LEU   A 1 326 ? 78.813  48.263  13.561  1   41.81 ? 348 LEU   A CD1  1 
ATOM   2588 C  CD2  . LEU   A 1 326 ? 78.82   47.061  11.387  1   40.81 ? 348 LEU   A CD2  1 
ATOM   2589 N  N    . ASP   A 1 327 ? 81.816  44.272  14.456  1   33.91 ? 349 ASP   A N    1 
ATOM   2590 C  CA   . ASP   A 1 327 ? 81.681  42.881  14.889  1   33.82 ? 349 ASP   A CA   1 
ATOM   2591 C  C    . ASP   A 1 327 ? 81.747  42.699  16.395  1   34.26 ? 349 ASP   A C    1 
ATOM   2592 O  O    . ASP   A 1 327 ? 80.984  41.902  16.948  1   34.96 ? 349 ASP   A O    1 
ATOM   2593 C  CB   . ASP   A 1 327 ? 82.783  42.04   14.265  1   35.95 ? 349 ASP   A CB   1 
ATOM   2594 C  CG   . ASP   A 1 327 ? 82.752  42.061  12.764  1   41.68 ? 349 ASP   A CG   1 
ATOM   2595 O  OD1  . ASP   A 1 327 ? 83.037  43.122  12.181  1   44.39 ? 349 ASP   A OD1  1 
ATOM   2596 O  OD2  . ASP   A 1 327 ? 82.464  41.015  12.166  1   42.91 ? 349 ASP   A OD2  1 
ATOM   2597 N  N    . LEU   A 1 328 ? 82.656  43.439  17.073  1   33.32 ? 350 LEU   A N    1 
ATOM   2598 C  CA   . LEU   A 1 328 ? 82.824  43.325  18.516  1   32.47 ? 350 LEU   A CA   1 
ATOM   2599 C  C    . LEU   A 1 328 ? 81.578  43.659  19.304  1   32    ? 350 LEU   A C    1 
ATOM   2600 O  O    . LEU   A 1 328 ? 81.301  42.998  20.285  1   32.18 ? 350 LEU   A O    1 
ATOM   2601 C  CB   . LEU   A 1 328 ? 84.001  44.172  18.995  1   32.33 ? 350 LEU   A CB   1 
ATOM   2602 C  CG   . LEU   A 1 328 ? 85.376  43.83   18.404  1   33.27 ? 350 LEU   A CG   1 
ATOM   2603 C  CD1  . LEU   A 1 328 ? 86.475  44.708  19.026  1   32.99 ? 350 LEU   A CD1  1 
ATOM   2604 C  CD2  . LEU   A 1 328 ? 85.702  42.335  18.562  1   33.71 ? 350 LEU   A CD2  1 
ATOM   2605 N  N    . PHE   A 1 329 ? 80.808  44.645  18.871  1   31.8  ? 351 PHE   A N    1 
ATOM   2606 C  CA   . PHE   A 1 329 ? 79.588  45.056  19.574  1   31.96 ? 351 PHE   A CA   1 
ATOM   2607 C  C    . PHE   A 1 329 ? 78.507  43.993  19.606  1   32.13 ? 351 PHE   A C    1 
ATOM   2608 O  O    . PHE   A 1 329 ? 77.693  44.022  20.516  1   32.49 ? 351 PHE   A O    1 
ATOM   2609 C  CB   . PHE   A 1 329 ? 78.992  46.334  18.969  1   31.47 ? 351 PHE   A CB   1 
ATOM   2610 C  CG   . PHE   A 1 329 ? 79.85   47.551  19.167  1   31.59 ? 351 PHE   A CG   1 
ATOM   2611 C  CD1  . PHE   A 1 329 ? 80.827  47.89   18.24   1   32.04 ? 351 PHE   A CD1  1 
ATOM   2612 C  CD2  . PHE   A 1 329 ? 79.681  48.365  20.273  1   31.94 ? 351 PHE   A CD2  1 
ATOM   2613 C  CE1  . PHE   A 1 329 ? 81.629  49.01   18.424  1   32.42 ? 351 PHE   A CE1  1 
ATOM   2614 C  CE2  . PHE   A 1 329 ? 80.488  49.491  20.457  1   32.36 ? 351 PHE   A CE2  1 
ATOM   2615 C  CZ   . PHE   A 1 329 ? 81.449  49.809  19.528  1   31.85 ? 351 PHE   A CZ   1 
ATOM   2616 N  N    . ASN   A 1 330 ? 78.49   43.057  18.647  1   31.51 ? 352 ASN   A N    1 
ATOM   2617 C  CA   . ASN   A 1 330 ? 77.445  42.054  18.594  1   31.84 ? 352 ASN   A CA   1 
ATOM   2618 C  C    . ASN   A 1 330 ? 77.826  40.683  19.152  1   32.19 ? 352 ASN   A C    1 
ATOM   2619 O  O    . ASN   A 1 330 ? 76.987  39.793  19.128  1   32.94 ? 352 ASN   A O    1 
ATOM   2620 C  CB   . ASN   A 1 330 ? 76.931  41.93   17.167  1   33.34 ? 352 ASN   A CB   1 
ATOM   2621 C  CG   . ASN   A 1 330 ? 75.49   41.441  17.06   1   38.15 ? 352 ASN   A CG   1 
ATOM   2622 O  OD1  . ASN   A 1 330 ? 74.576  41.823  17.826  1   38.55 ? 352 ASN   A OD1  1 
ATOM   2623 N  ND2  . ASN   A 1 330 ? 75.263  40.552  16.117  1   39.88 ? 352 ASN   A ND2  1 
ATOM   2624 N  N    . LEU   A 1 331 ? 79.037  40.508  19.712  1   31.41 ? 353 LEU   A N    1 
ATOM   2625 C  CA   . LEU   A 1 331 ? 79.501  39.195  20.183  1   31.63 ? 353 LEU   A CA   1 
ATOM   2626 C  C    . LEU   A 1 331 ? 78.61   38.494  21.241  1   32.36 ? 353 LEU   A C    1 
ATOM   2627 O  O    . LEU   A 1 331 ? 78.57   37.261  21.253  1   32.68 ? 353 LEU   A O    1 
ATOM   2628 C  CB   . LEU   A 1 331 ? 80.953  39.242  20.683  1   31.4  ? 353 LEU   A CB   1 
ATOM   2629 C  CG   . LEU   A 1 331 ? 81.993  39.653  19.639  1   32.73 ? 353 LEU   A CG   1 
ATOM   2630 C  CD1  . LEU   A 1 331 ? 83.401  39.722  20.245  1   32.61 ? 353 LEU   A CD1  1 
ATOM   2631 C  CD2  . LEU   A 1 331 ? 81.973  38.725  18.404  1   33.28 ? 353 LEU   A CD2  1 
ATOM   2632 N  N    . SER   A 1 332 ? 77.897  39.244  22.105  1   31.8  ? 354 SER   A N    1 
ATOM   2633 C  CA   . SER   A 1 332 ? 77.051  38.617  23.122  1   31.49 ? 354 SER   A CA   1 
ATOM   2634 C  C    . SER   A 1 332 ? 75.821  37.895  22.545  1   30.91 ? 354 SER   A C    1 
ATOM   2635 O  O    . SER   A 1 332 ? 75.182  37.143  23.265  1   30.92 ? 354 SER   A O    1 
ATOM   2636 C  CB   . SER   A 1 332 ? 76.656  39.609  24.203  1   32.66 ? 354 SER   A CB   1 
ATOM   2637 O  OG   . SER   A 1 332 ? 77.782  39.958  24.99   1   35.94 ? 354 SER   A OG   1 
ATOM   2638 N  N    . THR   A 1 333 ? 75.515  38.097  21.259  1   30.48 ? 355 THR   A N    1 
ATOM   2639 C  CA   . THR   A 1 333 ? 74.437  37.403  20.559  1   30.72 ? 355 THR   A CA   1 
ATOM   2640 C  C    . THR   A 1 333 ? 74.727  35.881  20.504  1   31.1  ? 355 THR   A C    1 
ATOM   2641 O  O    . THR   A 1 333 ? 73.792  35.105  20.449  1   31.81 ? 355 THR   A O    1 
ATOM   2642 C  CB   . THR   A 1 333 ? 74.332  37.969  19.121  1   30.7  ? 355 THR   A CB   1 
ATOM   2643 O  OG1  . THR   A 1 333 ? 74.138  39.378  19.192  1   30.99 ? 355 THR   A OG1  1 
ATOM   2644 C  CG2  . THR   A 1 333 ? 73.218  37.333  18.286  1   30.49 ? 355 THR   A CG2  1 
ATOM   2645 N  N    . PHE   A 1 334 ? 76.011  35.468  20.533  1   30.81 ? 356 PHE   A N    1 
ATOM   2646 C  CA   . PHE   A 1 334 ? 76.451  34.074  20.377  1   31.51 ? 356 PHE   A CA   1 
ATOM   2647 C  C    . PHE   A 1 334 ? 76.732  33.304  21.673  1   33.17 ? 356 PHE   A C    1 
ATOM   2648 O  O    . PHE   A 1 334 ? 77.082  32.122  21.64   1   33.23 ? 356 PHE   A O    1 
ATOM   2649 C  CB   . PHE   A 1 334 ? 77.696  34.033  19.471  1   30.86 ? 356 PHE   A CB   1 
ATOM   2650 C  CG   . PHE   A 1 334 ? 77.575  34.907  18.244  1   31.48 ? 356 PHE   A CG   1 
ATOM   2651 C  CD1  . PHE   A 1 334 ? 76.537  34.728  17.344  1   32.19 ? 356 PHE   A CD1  1 
ATOM   2652 C  CD2  . PHE   A 1 334 ? 78.446  35.962  18.038  1   32.22 ? 356 PHE   A CD2  1 
ATOM   2653 C  CE1  . PHE   A 1 334 ? 76.383  35.578  16.251  1   32.59 ? 356 PHE   A CE1  1 
ATOM   2654 C  CE2  . PHE   A 1 334 ? 78.297  36.798  16.944  1   32.81 ? 356 PHE   A CE2  1 
ATOM   2655 C  CZ   . PHE   A 1 334 ? 77.276  36.591  16.046  1   32.41 ? 356 PHE   A CZ   1 
ATOM   2656 N  N    . LEU   A 1 335 ? 76.593  33.974  22.809  1   34.26 ? 357 LEU   A N    1 
ATOM   2657 C  CA   . LEU   A 1 335 ? 76.876  33.452  24.129  1   35.36 ? 357 LEU   A CA   1 
ATOM   2658 C  C    . LEU   A 1 335 ? 75.88   32.364  24.584  1   37.11 ? 357 LEU   A C    1 
ATOM   2659 O  O    . LEU   A 1 335 ? 74.676  32.447  24.323  1   37.81 ? 357 LEU   A O    1 
ATOM   2660 C  CB   . LEU   A 1 335 ? 76.803  34.652  25.089  1   35.53 ? 357 LEU   A CB   1 
ATOM   2661 C  CG   . LEU   A 1 335 ? 77.392  34.47   26.468  1   37.23 ? 357 LEU   A CG   1 
ATOM   2662 C  CD1  . LEU   A 1 335 ? 78.901  34.237  26.386  1   37.77 ? 357 LEU   A CD1  1 
ATOM   2663 C  CD2  . LEU   A 1 335 ? 77.05   35.659  27.349  1   37.43 ? 357 LEU   A CD2  1 
ATOM   2664 N  N    . ILE   A 1 336 ? 76.395  31.362  25.287  1   37.22 ? 358 ILE   A N    1 
ATOM   2665 C  CA   . ILE   A 1 336 ? 75.648  30.286  25.937  1   38    ? 358 ILE   A CA   1 
ATOM   2666 C  C    . ILE   A 1 336 ? 76.031  30.332  27.439  1   38.42 ? 358 ILE   A C    1 
ATOM   2667 O  O    . ILE   A 1 336 ? 77.097  30.852  27.783  1   37.95 ? 358 ILE   A O    1 
ATOM   2668 C  CB   . ILE   A 1 336 ? 75.95   28.9    25.301  1   38.67 ? 358 ILE   A CB   1 
ATOM   2669 C  CG1  . ILE   A 1 336 ? 77.462  28.654  25.182  1   39.58 ? 358 ILE   A CG1  1 
ATOM   2670 C  CG2  . ILE   A 1 336 ? 75.247  28.754  23.946  1   39.29 ? 358 ILE   A CG2  1 
ATOM   2671 C  CD1  . ILE   A 1 336 ? 77.846  27.291  24.732  1   40.63 ? 358 ILE   A CD1  1 
ATOM   2672 N  N    . PRO   A 1 337 ? 75.188  29.812  28.348  1   38.73 ? 359 PRO   A N    1 
ATOM   2673 C  CA   . PRO   A 1 337 ? 75.523  29.875  29.778  1   39.07 ? 359 PRO   A CA   1 
ATOM   2674 C  C    . PRO   A 1 337 ? 76.849  29.224  30.149  1   40.17 ? 359 PRO   A C    1 
ATOM   2675 O  O    . PRO   A 1 337 ? 77.404  28.436  29.382  1   39.43 ? 359 PRO   A O    1 
ATOM   2676 C  CB   . PRO   A 1 337 ? 74.338  29.184  30.46   1   39.8  ? 359 PRO   A CB   1 
ATOM   2677 C  CG   . PRO   A 1 337 ? 73.244  29.218  29.471  1   40.27 ? 359 PRO   A CG   1 
ATOM   2678 C  CD   . PRO   A 1 337 ? 73.877  29.172  28.125  1   38.3  ? 359 PRO   A CD   1 
ATOM   2679 N  N    . ARG   A 1 338 ? 77.37   29.586  31.33   1   41.46 ? 360 ARG   A N    1 
ATOM   2680 C  CA   . ARG   A 1 338 ? 78.648  29.078  31.817  1   43.33 ? 360 ARG   A CA   1 
ATOM   2681 C  C    . ARG   A 1 338 ? 78.714  27.545  31.839  1   44.83 ? 360 ARG   A C    1 
ATOM   2682 O  O    . ARG   A 1 338 ? 79.694  26.969  31.362  1   45.04 ? 360 ARG   A O    1 
ATOM   2683 C  CB   . ARG   A 1 338 ? 78.955  29.654  33.203  1   44.52 ? 360 ARG   A CB   1 
ATOM   2684 C  CG   . ARG   A 1 338 ? 80.291  30.375  33.245  1   47.58 ? 360 ARG   A CG   1 
ATOM   2685 C  CD   . ARG   A 1 338 ? 80.631  30.851  34.644  1   49.87 ? 360 ARG   A CD   1 
ATOM   2686 N  NE   . ARG   A 1 338 ? 79.593  31.736  35.155  1   50.99 ? 360 ARG   A NE   1 
ATOM   2687 C  CZ   . ARG   A 1 338 ? 79.673  33.059  35.16   1   52.37 ? 360 ARG   A CZ   1 
ATOM   2688 N  NH1  . ARG   A 1 338 ? 80.776  33.67   34.736  1   51.76 ? 360 ARG   A NH1  1 
ATOM   2689 N  NH2  . ARG   A 1 338 ? 78.668  33.784  35.622  1   52.16 ? 360 ARG   A NH2  1 
ATOM   2690 N  N    . GLU   A 1 339 ? 77.647  26.894  32.34   1   45.35 ? 361 GLU   A N    1 
ATOM   2691 C  CA   . GLU   A 1 339 ? 77.54   25.434  32.413  1   45.83 ? 361 GLU   A CA   1 
ATOM   2692 C  C    . GLU   A 1 339 ? 77.675  24.774  31.032  1   46.76 ? 361 GLU   A C    1 
ATOM   2693 O  O    . GLU   A 1 339 ? 78.202  23.67   30.931  1   47.29 ? 361 GLU   A O    1 
ATOM   2694 C  CB   . GLU   A 1 339 ? 76.215  25.034  33.074  1   47.24 ? 361 GLU   A CB   1 
ATOM   2695 N  N    . ALA   A 1 340 ? 77.251  25.46   29.961  1   46.85 ? 362 ALA   A N    1 
ATOM   2696 C  CA   . ALA   A 1 340 ? 77.339  24.912  28.605  1   46.76 ? 362 ALA   A CA   1 
ATOM   2697 C  C    . ALA   A 1 340 ? 78.636  25.251  27.875  1   47.18 ? 362 ALA   A C    1 
ATOM   2698 O  O    . ALA   A 1 340 ? 78.899  24.675  26.824  1   47.22 ? 362 ALA   A O    1 
ATOM   2699 C  CB   . ALA   A 1 340 ? 76.146  25.363  27.782  1   46.62 ? 362 ALA   A CB   1 
ATOM   2700 N  N    . ILE   A 1 341 ? 79.443  26.187  28.399  1   47.46 ? 363 ILE   A N    1 
ATOM   2701 C  CA   . ILE   A 1 341 ? 80.699  26.57   27.74   1   47.9  ? 363 ILE   A CA   1 
ATOM   2702 C  C    . ILE   A 1 341 ? 81.741  25.453  27.882  1   49.24 ? 363 ILE   A C    1 
ATOM   2703 O  O    . ILE   A 1 341 ? 81.932  24.928  28.978  1   49.46 ? 363 ILE   A O    1 
ATOM   2704 C  CB   . ILE   A 1 341 ? 81.203  27.959  28.241  1   47.2  ? 363 ILE   A CB   1 
ATOM   2705 C  CG1  . ILE   A 1 341 ? 80.263  29.096  27.745  1   47.58 ? 363 ILE   A CG1  1 
ATOM   2706 C  CG2  . ILE   A 1 341 ? 82.626  28.218  27.806  1   47.14 ? 363 ILE   A CG2  1 
ATOM   2707 C  CD1  . ILE   A 1 341 ? 80.66   30.529  28.159  1   47.97 ? 363 ILE   A CD1  1 
ATOM   2708 N  N    . PRO   A 1 342 ? 82.382  25.048  26.768  1   50.09 ? 364 PRO   A N    1 
ATOM   2709 C  CA   . PRO   A 1 342 ? 83.382  23.968  26.84   1   51.14 ? 364 PRO   A CA   1 
ATOM   2710 C  C    . PRO   A 1 342 ? 84.497  24.249  27.846  1   52.97 ? 364 PRO   A C    1 
ATOM   2711 O  O    . PRO   A 1 342 ? 85.159  25.278  27.766  1   53.34 ? 364 PRO   A O    1 
ATOM   2712 C  CB   . PRO   A 1 342 ? 83.929  23.888  25.409  1   51.68 ? 364 PRO   A CB   1 
ATOM   2713 C  CG   . PRO   A 1 342 ? 82.883  24.506  24.552  1   51.91 ? 364 PRO   A CG   1 
ATOM   2714 C  CD   . PRO   A 1 342 ? 82.235  25.569  25.395  1   49.92 ? 364 PRO   A CD   1 
ATOM   2715 N  N    . PRO   A 1 343 ? 84.694  23.353  28.828  1   53.71 ? 365 PRO   A N    1 
ATOM   2716 C  CA   . PRO   A 1 343 ? 85.712  23.613  29.862  1   54.14 ? 365 PRO   A CA   1 
ATOM   2717 C  C    . PRO   A 1 343 ? 87.138  23.692  29.339  1   54.28 ? 365 PRO   A C    1 
ATOM   2718 O  O    . PRO   A 1 343 ? 87.529  22.867  28.525  1   54.71 ? 365 PRO   A O    1 
ATOM   2719 C  CB   . PRO   A 1 343 ? 85.517  22.461  30.859  1   54.86 ? 365 PRO   A CB   1 
ATOM   2720 C  CG   . PRO   A 1 343 ? 84.14   21.907  30.559  1   55.15 ? 365 PRO   A CG   1 
ATOM   2721 C  CD   . PRO   A 1 343 ? 83.962  22.1    29.086  1   53.38 ? 365 PRO   A CD   1 
ATOM   2722 N  N    . LEU   A 1 344 ? 87.906  24.697  29.805  1   54.06 ? 366 LEU   A N    1 
ATOM   2723 C  CA   . LEU   A 1 344 ? 89.297  24.909  29.403  1   54.44 ? 366 LEU   A CA   1 
ATOM   2724 C  C    . LEU   A 1 344 ? 90.227  23.769  29.858  1   54.85 ? 366 LEU   A C    1 
ATOM   2725 O  O    . LEU   A 1 344 ? 90.086  23.266  30.969  1   55.13 ? 366 LEU   A O    1 
ATOM   2726 C  CB   . LEU   A 1 344 ? 89.804  26.247  29.954  1   54.41 ? 366 LEU   A CB   1 
ATOM   2727 C  CG   . LEU   A 1 344 ? 89.624  27.455  29.058  1   55.45 ? 366 LEU   A CG   1 
ATOM   2728 C  CD1  . LEU   A 1 344 ? 90.062  28.7    29.762  1   55.48 ? 366 LEU   A CD1  1 
ATOM   2729 C  CD2  . LEU   A 1 344 ? 90.411  27.309  27.77   1   56.21 ? 366 LEU   A CD2  1 
ATOM   2730 N  N    . LYS   B 1 3   ? 62.293  61.891  64.873  1   48.48 ? 25  LYS   B N    1 
ATOM   2731 C  CA   . LYS   B 1 3   ? 62.632  62.529  63.592  1   48.9  ? 25  LYS   B CA   1 
ATOM   2732 C  C    . LYS   B 1 3   ? 64.139  62.484  63.335  1   48.28 ? 25  LYS   B C    1 
ATOM   2733 O  O    . LYS   B 1 3   ? 64.738  63.482  62.917  1   48.46 ? 25  LYS   B O    1 
ATOM   2734 C  CB   . LYS   B 1 3   ? 62.111  63.98   63.531  1   51.06 ? 25  LYS   B CB   1 
ATOM   2735 N  N    . ILE   B 1 4   ? 64.753  61.32   63.59   1   47.16 ? 26  ILE   B N    1 
ATOM   2736 C  CA   . ILE   B 1 4   ? 66.175  61.141  63.338  1   46.94 ? 26  ILE   B CA   1 
ATOM   2737 C  C    . ILE   B 1 4   ? 66.436  60.829  61.843  1   45.83 ? 26  ILE   B C    1 
ATOM   2738 O  O    . ILE   B 1 4   ? 65.486  60.645  61.088  1   46.17 ? 26  ILE   B O    1 
ATOM   2739 C  CB   . ILE   B 1 4   ? 66.798  60.115  64.319  1   47.98 ? 26  ILE   B CB   1 
ATOM   2740 C  CG1  . ILE   B 1 4   ? 66.289  58.676  64.062  1   48.94 ? 26  ILE   B CG1  1 
ATOM   2741 C  CG2  . ILE   B 1 4   ? 66.568  60.561  65.766  1   48.49 ? 26  ILE   B CG2  1 
ATOM   2742 N  N    . TYR   B 1 5   ? 67.708  60.818  61.41   1   44.47 ? 27  TYR   B N    1 
ATOM   2743 C  CA   . TYR   B 1 5   ? 68.115  60.621  60.01   1   43.46 ? 27  TYR   B CA   1 
ATOM   2744 C  C    . TYR   B 1 5   ? 67.394  59.456  59.307  1   43.19 ? 27  TYR   B C    1 
ATOM   2745 O  O    . TYR   B 1 5   ? 66.696  59.679  58.328  1   42.97 ? 27  TYR   B O    1 
ATOM   2746 C  CB   . TYR   B 1 5   ? 69.642  60.484  59.94   1   42.84 ? 27  TYR   B CB   1 
ATOM   2747 C  CG   . TYR   B 1 5   ? 70.235  60.325  58.557  1   42.46 ? 27  TYR   B CG   1 
ATOM   2748 C  CD1  . TYR   B 1 5   ? 70.692  61.425  57.845  1   42.54 ? 27  TYR   B CD1  1 
ATOM   2749 C  CD2  . TYR   B 1 5   ? 70.488  59.065  58.032  1   42.58 ? 27  TYR   B CD2  1 
ATOM   2750 C  CE1  . TYR   B 1 5   ? 71.306  61.279  56.607  1   43.28 ? 27  TYR   B CE1  1 
ATOM   2751 C  CE2  . TYR   B 1 5   ? 71.087  58.906  56.793  1   43.06 ? 27  TYR   B CE2  1 
ATOM   2752 C  CZ   . TYR   B 1 5   ? 71.51   60.013  56.085  1   43.64 ? 27  TYR   B CZ   1 
ATOM   2753 O  OH   . TYR   B 1 5   ? 72.12   59.828  54.866  1   43.8  ? 27  TYR   B OH   1 
ATOM   2754 N  N    . GLY   B 1 6   ? 67.525  58.248  59.839  1   43.79 ? 28  GLY   B N    1 
ATOM   2755 C  CA   . GLY   B 1 6   ? 66.908  57.053  59.271  1   44.43 ? 28  GLY   B CA   1 
ATOM   2756 C  C    . GLY   B 1 6   ? 65.4    57.108  59.195  1   44.68 ? 28  GLY   B C    1 
ATOM   2757 O  O    . GLY   B 1 6   ? 64.809  56.615  58.231  1   45.19 ? 28  GLY   B O    1 
ATOM   2758 N  N    . GLU   B 1 7   ? 64.765  57.732  60.196  1   44.19 ? 29  GLU   B N    1 
ATOM   2759 C  CA   . GLU   B 1 7   ? 63.307  57.855  60.231  1   43.63 ? 29  GLU   B CA   1 
ATOM   2760 C  C    . GLU   B 1 7   ? 62.809  58.912  59.242  1   42.36 ? 29  GLU   B C    1 
ATOM   2761 O  O    . GLU   B 1 7   ? 61.826  58.681  58.537  1   43.05 ? 29  GLU   B O    1 
ATOM   2762 C  CB   . GLU   B 1 7   ? 62.818  58.144  61.669  1   45.91 ? 29  GLU   B CB   1 
ATOM   2763 N  N    . TYR   B 1 8   ? 63.503  60.044  59.159  1   40.74 ? 30  TYR   B N    1 
ATOM   2764 C  CA   . TYR   B 1 8   ? 63.17   61.128  58.24   1   40.13 ? 30  TYR   B CA   1 
ATOM   2765 C  C    . TYR   B 1 8   ? 63.274  60.639  56.786  1   39.88 ? 30  TYR   B C    1 
ATOM   2766 O  O    . TYR   B 1 8   ? 62.454  61.011  55.952  1   39.96 ? 30  TYR   B O    1 
ATOM   2767 C  CB   . TYR   B 1 8   ? 64.11   62.327  58.479  1   39.77 ? 30  TYR   B CB   1 
ATOM   2768 C  CG   . TYR   B 1 8   ? 63.997  63.427  57.443  1   40.24 ? 30  TYR   B CG   1 
ATOM   2769 C  CD1  . TYR   B 1 8   ? 62.873  64.246  57.384  1   40.99 ? 30  TYR   B CD1  1 
ATOM   2770 C  CD2  . TYR   B 1 8   ? 64.994  63.624  56.495  1   40.39 ? 30  TYR   B CD2  1 
ATOM   2771 C  CE1  . TYR   B 1 8   ? 62.74   65.225  56.401  1   41.36 ? 30  TYR   B CE1  1 
ATOM   2772 C  CE2  . TYR   B 1 8   ? 64.879  64.608  55.517  1   41    ? 30  TYR   B CE2  1 
ATOM   2773 C  CZ   . TYR   B 1 8   ? 63.754  65.414  55.478  1   41.73 ? 30  TYR   B CZ   1 
ATOM   2774 O  OH   . TYR   B 1 8   ? 63.66   66.411  54.533  1   41.77 ? 30  TYR   B OH   1 
ATOM   2775 N  N    . LEU   B 1 9   ? 64.293  59.822  56.481  1   39.38 ? 31  LEU   B N    1 
ATOM   2776 C  CA   . LEU   B 1 9   ? 64.49   59.303  55.128  1   38.83 ? 31  LEU   B CA   1 
ATOM   2777 C  C    . LEU   B 1 9   ? 63.791  57.965  54.875  1   40.22 ? 31  LEU   B C    1 
ATOM   2778 O  O    . LEU   B 1 9   ? 63.9    57.437  53.772  1   41.43 ? 31  LEU   B O    1 
ATOM   2779 C  CB   . LEU   B 1 9   ? 65.982  59.183  54.826  1   37.49 ? 31  LEU   B CB   1 
ATOM   2780 C  CG   . LEU   B 1 9   ? 66.766  60.492  54.802  1   36.43 ? 31  LEU   B CG   1 
ATOM   2781 C  CD1  . LEU   B 1 9   ? 68.236  60.235  54.689  1   36.24 ? 31  LEU   B CD1  1 
ATOM   2782 C  CD2  . LEU   B 1 9   ? 66.312  61.389  53.705  1   35.87 ? 31  LEU   B CD2  1 
ATOM   2783 N  N    . MET   B 1 10  ? 63.103  57.408  55.891  1   40.11 ? 32  MET   B N    1 
ATOM   2784 C  CA   . MET   B 1 10  ? 62.381  56.145  55.865  1   40.07 ? 32  MET   B CA   1 
ATOM   2785 C  C    . MET   B 1 10  ? 63.241  55.017  55.31   1   39.8  ? 32  MET   B C    1 
ATOM   2786 O  O    . MET   B 1 10  ? 62.799  54.262  54.435  1   40.32 ? 32  MET   B O    1 
ATOM   2787 C  CB   . MET   B 1 10  ? 61.039  56.284  55.13   1   41.27 ? 32  MET   B CB   1 
ATOM   2788 C  CG   . MET   B 1 10  ? 60.198  57.426  55.66   1   43.99 ? 32  MET   B CG   1 
ATOM   2789 S  SD   . MET   B 1 10  ? 58.594  57.603  54.84   1   49.87 ? 32  MET   B SD   1 
ATOM   2790 C  CE   . MET   B 1 10  ? 57.839  56.09   55.354  1   50.79 ? 32  MET   B CE   1 
ATOM   2791 N  N    . LEU   B 1 11  ? 64.474  54.915  55.818  1   38.71 ? 33  LEU   B N    1 
ATOM   2792 C  CA   . LEU   B 1 11  ? 65.409  53.87   55.416  1   39.01 ? 33  LEU   B CA   1 
ATOM   2793 C  C    . LEU   B 1 11  ? 64.938  52.468  55.799  1   39.97 ? 33  LEU   B C    1 
ATOM   2794 O  O    . LEU   B 1 11  ? 65.421  51.486  55.239  1   39.43 ? 33  LEU   B O    1 
ATOM   2795 C  CB   . LEU   B 1 11  ? 66.813  54.141  55.981  1   38.88 ? 33  LEU   B CB   1 
ATOM   2796 C  CG   . LEU   B 1 11  ? 67.403  55.527  55.668  1   39.44 ? 33  LEU   B CG   1 
ATOM   2797 C  CD1  . LEU   B 1 11  ? 68.785  55.666  56.258  1   38.82 ? 33  LEU   B CD1  1 
ATOM   2798 C  CD2  . LEU   B 1 11  ? 67.449  55.791  54.147  1   40.02 ? 33  LEU   B CD2  1 
ATOM   2799 N  N    . ASP   B 1 12  ? 63.981  52.364  56.748  1   40.78 ? 34  ASP   B N    1 
ATOM   2800 C  CA   . ASP   B 1 12  ? 63.363  51.101  57.16   1   41.56 ? 34  ASP   B CA   1 
ATOM   2801 C  C    . ASP   B 1 12  ? 62.668  50.489  55.924  1   40.9  ? 34  ASP   B C    1 
ATOM   2802 O  O    . ASP   B 1 12  ? 62.858  49.322  55.62   1   41.04 ? 34  ASP   B O    1 
ATOM   2803 C  CB   . ASP   B 1 12  ? 62.332  51.362  58.31   1   44.82 ? 34  ASP   B CB   1 
ATOM   2804 C  CG   . ASP   B 1 12  ? 61.044  52.121  57.927  1   53.05 ? 34  ASP   B CG   1 
ATOM   2805 O  OD1  . ASP   B 1 12  ? 61.133  53.341  57.61   1   54.71 ? 34  ASP   B OD1  1 
ATOM   2806 O  OD2  . ASP   B 1 12  ? 59.936  51.497  57.971  1   56.4  ? 34  ASP   B OD2  1 
ATOM   2807 N  N    . LYS   B 1 13  ? 61.936  51.338  55.183  1   40.39 ? 35  LYS   B N    1 
ATOM   2808 C  CA   . LYS   B 1 13  ? 61.197  51.054  53.973  1   40.45 ? 35  LYS   B CA   1 
ATOM   2809 C  C    . LYS   B 1 13  ? 62.17   51.024  52.756  1   39.84 ? 35  LYS   B C    1 
ATOM   2810 O  O    . LYS   B 1 13  ? 62.219  50.012  52.056  1   40.26 ? 35  LYS   B O    1 
ATOM   2811 C  CB   . LYS   B 1 13  ? 60.134  52.158  53.809  1   43.15 ? 35  LYS   B CB   1 
ATOM   2812 C  CG   . LYS   B 1 13  ? 58.849  51.731  53.127  1   48.43 ? 35  LYS   B CG   1 
ATOM   2813 C  CD   . LYS   B 1 13  ? 57.83   52.869  53.157  1   53.39 ? 35  LYS   B CD   1 
ATOM   2814 N  N    . LEU   B 1 14  ? 62.954  52.108  52.534  1   38.45 ? 36  LEU   B N    1 
ATOM   2815 C  CA   . LEU   B 1 14  ? 63.883  52.241  51.403  1   37.77 ? 36  LEU   B CA   1 
ATOM   2816 C  C    . LEU   B 1 14  ? 64.906  51.126  51.298  1   36.89 ? 36  LEU   B C    1 
ATOM   2817 O  O    . LEU   B 1 14  ? 65.157  50.637  50.2    1   37.02 ? 36  LEU   B O    1 
ATOM   2818 C  CB   . LEU   B 1 14  ? 64.615  53.598  51.45   1   37.72 ? 36  LEU   B CB   1 
ATOM   2819 C  CG   . LEU   B 1 14  ? 65.408  53.962  50.192  1   37.86 ? 36  LEU   B CG   1 
ATOM   2820 C  CD1  . LEU   B 1 14  ? 64.538  54.719  49.199  1   37.52 ? 36  LEU   B CD1  1 
ATOM   2821 C  CD2  . LEU   B 1 14  ? 66.668  54.771  50.538  1   37.52 ? 36  LEU   B CD2  1 
ATOM   2822 N  N    . LEU   B 1 15  ? 65.498  50.733  52.433  1   35.79 ? 37  LEU   B N    1 
ATOM   2823 C  CA   . LEU   B 1 15  ? 66.529  49.709  52.489  1   34.94 ? 37  LEU   B CA   1 
ATOM   2824 C  C    . LEU   B 1 15  ? 66.026  48.308  52.78   1   35.92 ? 37  LEU   B C    1 
ATOM   2825 O  O    . LEU   B 1 15  ? 66.834  47.415  53.026  1   36.08 ? 37  LEU   B O    1 
ATOM   2826 C  CB   . LEU   B 1 15  ? 67.645  50.092  53.455  1   34.19 ? 37  LEU   B CB   1 
ATOM   2827 C  CG   . LEU   B 1 15  ? 68.298  51.451  53.177  1   35.23 ? 37  LEU   B CG   1 
ATOM   2828 C  CD1  . LEU   B 1 15  ? 69.343  51.766  54.242  1   35.71 ? 37  LEU   B CD1  1 
ATOM   2829 C  CD2  . LEU   B 1 15  ? 68.922  51.506  51.756  1   34.98 ? 37  LEU   B CD2  1 
ATOM   2830 N  N    . ASP   B 1 16  ? 64.718  48.081  52.669  1   36.7  ? 38  ASP   B N    1 
ATOM   2831 C  CA   . ASP   B 1 16  ? 64.126  46.739  52.731  1   37.8  ? 38  ASP   B CA   1 
ATOM   2832 C  C    . ASP   B 1 16  ? 63.363  46.457  51.386  1   38.74 ? 38  ASP   B C    1 
ATOM   2833 O  O    . ASP   B 1 16  ? 62.435  45.645  51.337  1   40.08 ? 38  ASP   B O    1 
ATOM   2834 C  CB   . ASP   B 1 16  ? 63.192  46.571  53.945  1   40.01 ? 38  ASP   B CB   1 
ATOM   2835 C  CG   . ASP   B 1 16  ? 62.831  45.116  54.222  1   45.53 ? 38  ASP   B CG   1 
ATOM   2836 O  OD1  . ASP   B 1 16  ? 63.74   44.26   54.172  1   46.05 ? 38  ASP   B OD1  1 
ATOM   2837 O  OD2  . ASP   B 1 16  ? 61.628  44.83   54.453  1   48.81 ? 38  ASP   B OD2  1 
ATOM   2838 N  N    . ALA   B 1 17  ? 63.754  47.137  50.299  1   37.29 ? 39  ALA   B N    1 
ATOM   2839 C  CA   . ALA   B 1 17  ? 63.147  46.965  48.996  1   36.16 ? 39  ALA   B CA   1 
ATOM   2840 C  C    . ALA   B 1 17  ? 64.066  46.208  48.029  1   35.07 ? 39  ALA   B C    1 
ATOM   2841 O  O    . ALA   B 1 17  ? 63.805  46.224  46.831  1   35.31 ? 39  ALA   B O    1 
ATOM   2842 C  CB   . ALA   B 1 17  ? 62.772  48.327  48.424  1   35.64 ? 39  ALA   B CB   1 
ATOM   2843 N  N    . GLN   B 1 18  ? 65.108  45.515  48.531  1   33.73 ? 40  GLN   B N    1 
ATOM   2844 C  CA   . GLN   B 1 18  ? 66.039  44.812  47.664  1   33.36 ? 40  GLN   B CA   1 
ATOM   2845 C  C    . GLN   B 1 18  ? 65.868  43.315  47.818  1   34.59 ? 40  GLN   B C    1 
ATOM   2846 O  O    . GLN   B 1 18  ? 66.252  42.737  48.838  1   34.89 ? 40  GLN   B O    1 
ATOM   2847 C  CB   . GLN   B 1 18  ? 67.497  45.269  47.914  1   32.88 ? 40  GLN   B CB   1 
ATOM   2848 C  CG   . GLN   B 1 18  ? 67.753  46.766  47.629  1   31.57 ? 40  GLN   B CG   1 
ATOM   2849 C  CD   . GLN   B 1 18  ? 67.128  47.683  48.656  1   33.1  ? 40  GLN   B CD   1 
ATOM   2850 O  OE1  . GLN   B 1 18  ? 67.153  47.413  49.852  1   34.46 ? 40  GLN   B OE1  1 
ATOM   2851 N  NE2  . GLN   B 1 18  ? 66.53   48.781  48.222  1   32.02 ? 40  GLN   B NE2  1 
ATOM   2852 N  N    . CYS   B 1 19  ? 65.246  42.679  46.811  1   34.49 ? 41  CYS   B N    1 
ATOM   2853 C  CA   . CYS   B 1 19  ? 64.987  41.252  46.868  1   34.45 ? 41  CYS   B CA   1 
ATOM   2854 C  C    . CYS   B 1 19  ? 65.572  40.53   45.651  1   33.65 ? 41  CYS   B C    1 
ATOM   2855 O  O    . CYS   B 1 19  ? 64.965  40.538  44.592  1   33.82 ? 41  CYS   B O    1 
ATOM   2856 C  CB   . CYS   B 1 19  ? 63.485  40.991  47.008  1   35.84 ? 41  CYS   B CB   1 
ATOM   2857 S  SG   . CYS   B 1 19  ? 63.024  39.23   47.03   1   40.95 ? 41  CYS   B SG   1 
ATOM   2858 N  N    . MET   B 1 20  ? 66.717  39.872  45.815  1   33    ? 42  MET   B N    1 
ATOM   2859 C  CA   . MET   B 1 20  ? 67.351  39.128  44.739  1   32.78 ? 42  MET   B CA   1 
ATOM   2860 C  C    . MET   B 1 20  ? 66.619  37.828  44.487  1   33.96 ? 42  MET   B C    1 
ATOM   2861 O  O    . MET   B 1 20  ? 66.602  36.95   45.363  1   34.4  ? 42  MET   B O    1 
ATOM   2862 C  CB   . MET   B 1 20  ? 68.833  38.856  45.05   1   31.95 ? 42  MET   B CB   1 
ATOM   2863 C  CG   . MET   B 1 20  ? 69.71   40.117  45.05   1   33.51 ? 42  MET   B CG   1 
ATOM   2864 S  SD   . MET   B 1 20  ? 71.206  39.863  46.051  1   38.42 ? 42  MET   B SD   1 
ATOM   2865 C  CE   . MET   B 1 20  ? 72.028  38.62   45.128  1   29.97 ? 42  MET   B CE   1 
ATOM   2866 N  N    . LEU   B 1 21  ? 66.031  37.68   43.283  1   34.32 ? 43  LEU   B N    1 
ATOM   2867 C  CA   . LEU   B 1 21  ? 65.322  36.459  42.904  1   35.12 ? 43  LEU   B CA   1 
ATOM   2868 C  C    . LEU   B 1 21  ? 66.237  35.269  42.76   1   35.46 ? 43  LEU   B C    1 
ATOM   2869 O  O    . LEU   B 1 21  ? 65.843  34.171  43.127  1   35.55 ? 43  LEU   B O    1 
ATOM   2870 C  CB   . LEU   B 1 21  ? 64.455  36.661  41.67   1   35.8  ? 43  LEU   B CB   1 
ATOM   2871 C  CG   . LEU   B 1 21  ? 63.261  37.615  41.881  1   38.08 ? 43  LEU   B CG   1 
ATOM   2872 C  CD1  . LEU   B 1 21  ? 62.417  37.722  40.617  1   38.42 ? 43  LEU   B CD1  1 
ATOM   2873 C  CD2  . LEU   B 1 21  ? 62.376  37.171  43.059  1   38.45 ? 43  LEU   B CD2  1 
ATOM   2874 N  N    . SER   B 1 22  ? 67.488  35.481  42.34   1   36.04 ? 44  SER   B N    1 
ATOM   2875 C  CA   . SER   B 1 22  ? 68.461  34.385  42.276  1   36.79 ? 44  SER   B CA   1 
ATOM   2876 C  C    . SER   B 1 22  ? 68.777  33.869  43.702  1   37.9  ? 44  SER   B C    1 
ATOM   2877 O  O    . SER   B 1 22  ? 69.027  32.683  43.878  1   38.01 ? 44  SER   B O    1 
ATOM   2878 C  CB   . SER   B 1 22  ? 69.736  34.825  41.563  1   36.81 ? 44  SER   B CB   1 
ATOM   2879 O  OG   . SER   B 1 22  ? 70.443  35.821  42.288  1   37.36 ? 44  SER   B OG   1 
ATOM   2880 N  N    . GLU   B 1 23  ? 68.764  34.753  44.706  1   38.85 ? 45  GLU   B N    1 
ATOM   2881 C  CA   . GLU   B 1 23  ? 68.992  34.363  46.091  1   41.36 ? 45  GLU   B CA   1 
ATOM   2882 C  C    . GLU   B 1 23  ? 67.775  33.546  46.598  1   42.77 ? 45  GLU   B C    1 
ATOM   2883 O  O    . GLU   B 1 23  ? 67.956  32.499  47.223  1   43.28 ? 45  GLU   B O    1 
ATOM   2884 C  CB   . GLU   B 1 23  ? 69.245  35.605  46.966  1   44.89 ? 45  GLU   B CB   1 
ATOM   2885 C  CG   . GLU   B 1 23  ? 69.379  35.285  48.438  1   51.13 ? 45  GLU   B CG   1 
ATOM   2886 C  CD   . GLU   B 1 23  ? 69.201  36.459  49.375  1   59.92 ? 45  GLU   B CD   1 
ATOM   2887 O  OE1  . GLU   B 1 23  ? 68.52   36.279  50.413  1   63.02 ? 45  GLU   B OE1  1 
ATOM   2888 O  OE2  . GLU   B 1 23  ? 69.738  37.553  49.079  1   61.09 ? 45  GLU   B OE2  1 
ATOM   2889 N  N    . GLU   B 1 24  ? 66.552  33.976  46.242  1   43.24 ? 46  GLU   B N    1 
ATOM   2890 C  CA   . GLU   B 1 24  ? 65.323  33.268  46.581  1   44.64 ? 46  GLU   B CA   1 
ATOM   2891 C  C    . GLU   B 1 24  ? 65.298  31.842  45.988  1   44.58 ? 46  GLU   B C    1 
ATOM   2892 O  O    . GLU   B 1 24  ? 64.754  30.923  46.598  1   45.82 ? 46  GLU   B O    1 
ATOM   2893 C  CB   . GLU   B 1 24  ? 64.102  34.058  46.089  1   49.69 ? 46  GLU   B CB   1 
ATOM   2894 C  CG   . GLU   B 1 24  ? 63.545  35.044  47.105  1   58.85 ? 46  GLU   B CG   1 
ATOM   2895 C  CD   . GLU   B 1 24  ? 62.062  34.877  47.399  1   71.28 ? 46  GLU   B CD   1 
ATOM   2896 O  OE1  . GLU   B 1 24  ? 61.389  34.113  46.665  1   72.53 ? 46  GLU   B OE1  1 
ATOM   2897 O  OE2  . GLU   B 1 24  ? 61.58   35.492  48.382  1   75.95 ? 46  GLU   B OE2  1 
ATOM   2898 N  N    . ASP   B 1 25  ? 65.901  31.65   44.823  1   42.82 ? 47  ASP   B N    1 
ATOM   2899 C  CA   . ASP   B 1 25  ? 65.981  30.344  44.186  1   41.64 ? 47  ASP   B CA   1 
ATOM   2900 C  C    . ASP   B 1 25  ? 67.227  29.542  44.61   1   41    ? 47  ASP   B C    1 
ATOM   2901 O  O    . ASP   B 1 25  ? 67.584  28.562  43.95   1   41.09 ? 47  ASP   B O    1 
ATOM   2902 C  CB   . ASP   B 1 25  ? 65.937  30.501  42.67   1   42.91 ? 47  ASP   B CB   1 
ATOM   2903 C  CG   . ASP   B 1 25  ? 65.513  29.252  41.919  1   47.42 ? 47  ASP   B CG   1 
ATOM   2904 O  OD1  . ASP   B 1 25  ? 64.529  28.605  42.346  1   49.49 ? 47  ASP   B OD1  1 
ATOM   2905 O  OD2  . ASP   B 1 25  ? 66.175  28.911  40.92   1   48.27 ? 47  ASP   B OD2  1 
ATOM   2906 N  N    . LYS   B 1 26  ? 67.871  29.934  45.728  1   40.19 ? 48  LYS   B N    1 
ATOM   2907 C  CA   . LYS   B 1 26  ? 69.021  29.257  46.33   1   39.26 ? 48  LYS   B CA   1 
ATOM   2908 C  C    . LYS   B 1 26  ? 70.22   29.157  45.418  1   39.5  ? 48  LYS   B C    1 
ATOM   2909 O  O    . LYS   B 1 26  ? 70.994  28.21   45.52   1   39.42 ? 48  LYS   B O    1 
ATOM   2910 C  CB   . LYS   B 1 26  ? 68.628  27.873  46.881  1   39.45 ? 48  LYS   B CB   1 
ATOM   2911 C  CG   . LYS   B 1 26  ? 67.501  27.943  47.917  1   40.25 ? 48  LYS   B CG   1 
ATOM   2912 C  CD   . LYS   B 1 26  ? 66.145  27.632  47.328  1   41.71 ? 48  LYS   B CD   1 
ATOM   2913 C  CE   . LYS   B 1 26  ? 65.049  27.983  48.286  1   43.37 ? 48  LYS   B CE   1 
ATOM   2914 N  NZ   . LYS   B 1 26  ? 63.696  27.796  47.696  1   44.47 ? 48  LYS   B NZ   1 
ATOM   2915 N  N    . ARG   B 1 27  ? 70.38   30.132  44.51   1   39.65 ? 49  ARG   B N    1 
ATOM   2916 C  CA   . ARG   B 1 27  ? 71.549  30.2    43.616  1   39.85 ? 49  ARG   B CA   1 
ATOM   2917 C  C    . ARG   B 1 27  ? 71.891  31.667  43.411  1   38.58 ? 49  ARG   B C    1 
ATOM   2918 O  O    . ARG   B 1 27  ? 71.683  32.205  42.325  1   38.98 ? 49  ARG   B O    1 
ATOM   2919 C  CB   . ARG   B 1 27  ? 71.31   29.478  42.271  1   41.72 ? 49  ARG   B CB   1 
ATOM   2920 C  CG   . ARG   B 1 27  ? 69.864  29.398  41.812  1   45.27 ? 49  ARG   B CG   1 
ATOM   2921 C  CD   . ARG   B 1 27  ? 69.679  28.287  40.78   1   50.09 ? 49  ARG   B CD   1 
ATOM   2922 N  NE   . ARG   B 1 27  ? 69.841  26.948  41.353  1   53.45 ? 49  ARG   B NE   1 
ATOM   2923 N  N    . PRO   B 1 28  ? 72.304  32.369  44.485  1   36.63 ? 50  PRO   B N    1 
ATOM   2924 C  CA   . PRO   B 1 28  ? 72.53   33.816  44.361  1   35.18 ? 50  PRO   B CA   1 
ATOM   2925 C  C    . PRO   B 1 28  ? 73.626  34.232  43.396  1   33.3  ? 50  PRO   B C    1 
ATOM   2926 O  O    . PRO   B 1 28  ? 74.661  33.588  43.31   1   33.45 ? 50  PRO   B O    1 
ATOM   2927 C  CB   . PRO   B 1 28  ? 72.838  34.254  45.797  1   36.14 ? 50  PRO   B CB   1 
ATOM   2928 C  CG   . PRO   B 1 28  ? 73.376  33.009  46.456  1   36.97 ? 50  PRO   B CG   1 
ATOM   2929 C  CD   . PRO   B 1 28  ? 72.558  31.894  45.862  1   35.59 ? 50  PRO   B CD   1 
ATOM   2930 N  N    . VAL   B 1 29  ? 73.368  35.304  42.639  1   31.77 ? 51  VAL   B N    1 
ATOM   2931 C  CA   . VAL   B 1 29  ? 74.331  35.896  41.715  1   30.28 ? 51  VAL   B CA   1 
ATOM   2932 C  C    . VAL   B 1 29  ? 74.627  37.265  42.287  1   29.21 ? 51  VAL   B C    1 
ATOM   2933 O  O    . VAL   B 1 29  ? 73.736  38.106  42.362  1   29.16 ? 51  VAL   B O    1 
ATOM   2934 C  CB   . VAL   B 1 29  ? 73.78   35.995  40.271  1   30.55 ? 51  VAL   B CB   1 
ATOM   2935 C  CG1  . VAL   B 1 29  ? 74.826  36.598  39.328  1   30.52 ? 51  VAL   B CG1  1 
ATOM   2936 C  CG2  . VAL   B 1 29  ? 73.343  34.624  39.776  1   30.3  ? 51  VAL   B CG2  1 
ATOM   2937 N  N    . HIS   B 1 30  ? 75.863  37.471  42.752  1   28.18 ? 52  HIS   B N    1 
ATOM   2938 C  CA   . HIS   B 1 30  ? 76.328  38.715  43.35   1   27.27 ? 52  HIS   B CA   1 
ATOM   2939 C  C    . HIS   B 1 30  ? 75.891  39.992  42.58   1   27.04 ? 52  HIS   B C    1 
ATOM   2940 O  O    . HIS   B 1 30  ? 75.412  40.937  43.204  1   27.37 ? 52  HIS   B O    1 
ATOM   2941 C  CB   . HIS   B 1 30  ? 77.869  38.667  43.531  1   27.17 ? 52  HIS   B CB   1 
ATOM   2942 C  CG   . HIS   B 1 30  ? 78.445  39.904  44.155  1   29.05 ? 52  HIS   B CG   1 
ATOM   2943 N  ND1  . HIS   B 1 30  ? 78.897  40.982  43.381  1   30.87 ? 52  HIS   B ND1  1 
ATOM   2944 C  CD2  . HIS   B 1 30  ? 78.621  40.209  45.458  1   29.53 ? 52  HIS   B CD2  1 
ATOM   2945 C  CE1  . HIS   B 1 30  ? 79.3    41.904  44.245  1   30.69 ? 52  HIS   B CE1  1 
ATOM   2946 N  NE2  . HIS   B 1 30  ? 79.158  41.482  45.502  1   31    ? 52  HIS   B NE2  1 
ATOM   2947 N  N    . ASP   B 1 31  ? 76.024  40.007  41.248  1   26.23 ? 53  ASP   B N    1 
ATOM   2948 C  CA   . ASP   B 1 31  ? 75.7    41.213  40.477  1   26.69 ? 53  ASP   B CA   1 
ATOM   2949 C  C    . ASP   B 1 31  ? 74.222  41.541  40.367  1   26.93 ? 53  ASP   B C    1 
ATOM   2950 O  O    . ASP   B 1 31  ? 73.909  42.642  39.925  1   26.78 ? 53  ASP   B O    1 
ATOM   2951 C  CB   . ASP   B 1 31  ? 76.337  41.178  39.086  1   27.69 ? 53  ASP   B CB   1 
ATOM   2952 C  CG   . ASP   B 1 31  ? 77.846  41.37   39.085  1   30.3  ? 53  ASP   B CG   1 
ATOM   2953 O  OD1  . ASP   B 1 31  ? 78.44   41.496  40.186  1   29.6  ? 53  ASP   B OD1  1 
ATOM   2954 O  OD2  . ASP   B 1 31  ? 78.438  41.355  37.998  1   32.16 ? 53  ASP   B OD2  1 
ATOM   2955 N  N    . GLU   B 1 32  ? 73.314  40.636  40.799  1   26.8  ? 54  GLU   B N    1 
ATOM   2956 C  CA   . GLU   B 1 32  ? 71.889  40.964  40.787  1   26.68 ? 54  GLU   B CA   1 
ATOM   2957 C  C    . GLU   B 1 32  ? 71.588  42.124  41.746  1   26.55 ? 54  GLU   B C    1 
ATOM   2958 O  O    . GLU   B 1 32  ? 70.722  42.957  41.475  1   27.61 ? 54  GLU   B O    1 
ATOM   2959 C  CB   . GLU   B 1 32  ? 71.029  39.748  41.125  1   28.49 ? 54  GLU   B CB   1 
ATOM   2960 C  CG   . GLU   B 1 32  ? 69.564  40.09   40.963  1   31.59 ? 54  GLU   B CG   1 
ATOM   2961 C  CD   . GLU   B 1 32  ? 68.569  38.995  41.274  1   33.03 ? 54  GLU   B CD   1 
ATOM   2962 O  OE1  . GLU   B 1 32  ? 68.99   37.888  41.681  1   34.28 ? 54  GLU   B OE1  1 
ATOM   2963 O  OE2  . GLU   B 1 32  ? 67.356  39.258  41.122  1   30.87 ? 54  GLU   B OE2  1 
ATOM   2964 N  N    . HIS   B 1 33  ? 72.346  42.22   42.836  1   25.19 ? 55  HIS   B N    1 
ATOM   2965 C  CA   . HIS   B 1 33  ? 72.214  43.302  43.792  1   24.41 ? 55  HIS   B CA   1 
ATOM   2966 C  C    . HIS   B 1 33  ? 72.503  44.657  43.096  1   23.73 ? 55  HIS   B C    1 
ATOM   2967 O  O    . HIS   B 1 33  ? 71.755  45.614  43.283  1   24.08 ? 55  HIS   B O    1 
ATOM   2968 C  CB   . HIS   B 1 33  ? 73.195  43.052  44.949  1   24.51 ? 55  HIS   B CB   1 
ATOM   2969 C  CG   . HIS   B 1 33  ? 72.894  43.846  46.178  1   26.43 ? 55  HIS   B CG   1 
ATOM   2970 N  ND1  . HIS   B 1 33  ? 73.227  45.186  46.273  1   27.58 ? 55  HIS   B ND1  1 
ATOM   2971 C  CD2  . HIS   B 1 33  ? 72.326  43.449  47.346  1   27.6  ? 55  HIS   B CD2  1 
ATOM   2972 C  CE1  . HIS   B 1 33  ? 72.842  45.563  47.485  1   28.62 ? 55  HIS   B CE1  1 
ATOM   2973 N  NE2  . HIS   B 1 33  ? 72.292  44.55   48.165  1   28.55 ? 55  HIS   B NE2  1 
ATOM   2974 N  N    . LEU   B 1 34  ? 73.578  44.725  42.28   1   23.02 ? 56  LEU   B N    1 
ATOM   2975 C  CA   . LEU   B 1 34  ? 73.917  45.929  41.528  1   23.19 ? 56  LEU   B CA   1 
ATOM   2976 C  C    . LEU   B 1 34  ? 72.795  46.242  40.527  1   24.98 ? 56  LEU   B C    1 
ATOM   2977 O  O    . LEU   B 1 34  ? 72.366  47.391  40.404  1   25.05 ? 56  LEU   B O    1 
ATOM   2978 C  CB   . LEU   B 1 34  ? 75.252  45.732  40.78   1   22.57 ? 56  LEU   B CB   1 
ATOM   2979 C  CG   . LEU   B 1 34  ? 75.689  46.95   39.93   1   22.6  ? 56  LEU   B CG   1 
ATOM   2980 C  CD1  . LEU   B 1 34  ? 75.999  48.137  40.814  1   21.61 ? 56  LEU   B CD1  1 
ATOM   2981 C  CD2  . LEU   B 1 34  ? 76.853  46.607  39.021  1   22.58 ? 56  LEU   B CD2  1 
ATOM   2982 N  N    . PHE   B 1 35  ? 72.276  45.204  39.849  1   26.22 ? 57  PHE   B N    1 
ATOM   2983 C  CA   . PHE   B 1 35  ? 71.182  45.351  38.891  1   27.5  ? 57  PHE   B CA   1 
ATOM   2984 C  C    . PHE   B 1 35  ? 69.942  46.002  39.557  1   27.85 ? 57  PHE   B C    1 
ATOM   2985 O  O    . PHE   B 1 35  ? 69.359  46.933  39.002  1   28.3  ? 57  PHE   B O    1 
ATOM   2986 C  CB   . PHE   B 1 35  ? 70.843  43.977  38.26   1   28    ? 57  PHE   B CB   1 
ATOM   2987 C  CG   . PHE   B 1 35  ? 69.775  44.007  37.181  1   29    ? 57  PHE   B CG   1 
ATOM   2988 C  CD1  . PHE   B 1 35  ? 70.099  44.318  35.868  1   29.24 ? 57  PHE   B CD1  1 
ATOM   2989 C  CD2  . PHE   B 1 35  ? 68.439  43.756  37.49   1   29.49 ? 57  PHE   B CD2  1 
ATOM   2990 C  CE1  . PHE   B 1 35  ? 69.113  44.362  34.885  1   29.6  ? 57  PHE   B CE1  1 
ATOM   2991 C  CE2  . PHE   B 1 35  ? 67.459  43.801  36.504  1   29.62 ? 57  PHE   B CE2  1 
ATOM   2992 C  CZ   . PHE   B 1 35  ? 67.805  44.093  35.209  1   29.37 ? 57  PHE   B CZ   1 
ATOM   2993 N  N    . ILE   B 1 36  ? 69.577  45.553  40.76   1   27.22 ? 58  ILE   B N    1 
ATOM   2994 C  CA   . ILE   B 1 36  ? 68.442  46.125  41.492  1   26.54 ? 58  ILE   B CA   1 
ATOM   2995 C  C    . ILE   B 1 36  ? 68.73   47.546  41.964  1   26.69 ? 58  ILE   B C    1 
ATOM   2996 O  O    . ILE   B 1 36  ? 67.915  48.441  41.738  1   27.19 ? 58  ILE   B O    1 
ATOM   2997 C  CB   . ILE   B 1 36  ? 68.061  45.185  42.688  1   26.47 ? 58  ILE   B CB   1 
ATOM   2998 C  CG1  . ILE   B 1 36  ? 67.522  43.826  42.19   1   25.96 ? 58  ILE   B CG1  1 
ATOM   2999 C  CG2  . ILE   B 1 36  ? 67.071  45.854  43.661  1   26.36 ? 58  ILE   B CG2  1 
ATOM   3000 C  CD1  . ILE   B 1 36  ? 67.355  42.781  43.332  1   26.26 ? 58  ILE   B CD1  1 
ATOM   3001 N  N    . ILE   B 1 37  ? 69.876  47.763  42.639  1   26.44 ? 59  ILE   B N    1 
ATOM   3002 C  CA   . ILE   B 1 37  ? 70.248  49.09   43.158  1   26.36 ? 59  ILE   B CA   1 
ATOM   3003 C  C    . ILE   B 1 37  ? 70.317  50.158  42.059  1   25.68 ? 59  ILE   B C    1 
ATOM   3004 O  O    . ILE   B 1 37  ? 69.807  51.263  42.252  1   25.67 ? 59  ILE   B O    1 
ATOM   3005 C  CB   . ILE   B 1 37  ? 71.57   49.02   44      1   26.95 ? 59  ILE   B CB   1 
ATOM   3006 C  CG1  . ILE   B 1 37  ? 71.325  48.312  45.368  1   28.28 ? 59  ILE   B CG1  1 
ATOM   3007 C  CG2  . ILE   B 1 37  ? 72.209  50.419  44.214  1   27.13 ? 59  ILE   B CG2  1 
ATOM   3008 C  CD1  . ILE   B 1 37  ? 70.497  49.137  46.431  1   28.54 ? 59  ILE   B CD1  1 
ATOM   3009 N  N    . THR   B 1 38  ? 70.933  49.834  40.903  1   25.28 ? 60  THR   B N    1 
ATOM   3010 C  CA   . THR   B 1 38  ? 71.062  50.774  39.799  1   25.75 ? 60  THR   B CA   1 
ATOM   3011 C  C    . THR   B 1 38  ? 69.679  51.228  39.324  1   26.45 ? 60  THR   B C    1 
ATOM   3012 O  O    . THR   B 1 38  ? 69.456  52.433  39.185  1   26.91 ? 60  THR   B O    1 
ATOM   3013 C  CB   . THR   B 1 38  ? 71.866  50.159  38.61   1   25.98 ? 60  THR   B CB   1 
ATOM   3014 O  OG1  . THR   B 1 38  ? 73.133  49.694  39.077  1   26.28 ? 60  THR   B OG1  1 
ATOM   3015 C  CG2  . THR   B 1 38  ? 72.082  51.158  37.489  1   25.32 ? 60  THR   B CG2  1 
ATOM   3016 N  N    . HIS   B 1 39  ? 68.755  50.269  39.116  1   26.02 ? 61  HIS   B N    1 
ATOM   3017 C  CA   . HIS   B 1 39  ? 67.385  50.581  38.69   1   26.23 ? 61  HIS   B CA   1 
ATOM   3018 C  C    . HIS   B 1 39  ? 66.659  51.404  39.748  1   26.02 ? 61  HIS   B C    1 
ATOM   3019 O  O    . HIS   B 1 39  ? 66.015  52.382  39.402  1   26.33 ? 61  HIS   B O    1 
ATOM   3020 C  CB   . HIS   B 1 39  ? 66.592  49.301  38.429  1   26.38 ? 61  HIS   B CB   1 
ATOM   3021 C  CG   . HIS   B 1 39  ? 66.829  48.715  37.082  1   27.46 ? 61  HIS   B CG   1 
ATOM   3022 N  ND1  . HIS   B 1 39  ? 67.934  47.92   36.822  1   28.35 ? 61  HIS   B ND1  1 
ATOM   3023 C  CD2  . HIS   B 1 39  ? 66.113  48.854  35.945  1   28.09 ? 61  HIS   B CD2  1 
ATOM   3024 C  CE1  . HIS   B 1 39  ? 67.838  47.58   35.55   1   28.18 ? 61  HIS   B CE1  1 
ATOM   3025 N  NE2  . HIS   B 1 39  ? 66.758  48.111  34.983  1   28.65 ? 61  HIS   B NE2  1 
ATOM   3026 N  N    . GLN   B 1 40  ? 66.82   51.064  41.033  1   25.9  ? 62  GLN   B N    1 
ATOM   3027 C  CA   . GLN   B 1 40  ? 66.183  51.828  42.117  1   26.29 ? 62  GLN   B CA   1 
ATOM   3028 C  C    . GLN   B 1 40  ? 66.706  53.264  42.205  1   27.18 ? 62  GLN   B C    1 
ATOM   3029 O  O    . GLN   B 1 40  ? 65.927  54.175  42.415  1   28.63 ? 62  GLN   B O    1 
ATOM   3030 C  CB   . GLN   B 1 40  ? 66.327  51.081  43.432  1   27.44 ? 62  GLN   B CB   1 
ATOM   3031 C  CG   . GLN   B 1 40  ? 65.449  49.854  43.476  1   29.68 ? 62  GLN   B CG   1 
ATOM   3032 C  CD   . GLN   B 1 40  ? 65.646  49.068  44.75   1   34.12 ? 62  GLN   B CD   1 
ATOM   3033 O  OE1  . GLN   B 1 40  ? 66.721  49.08   45.371  1   35.31 ? 62  GLN   B OE1  1 
ATOM   3034 N  NE2  . GLN   B 1 40  ? 64.616  48.345  45.146  1   33.13 ? 62  GLN   B NE2  1 
ATOM   3035 N  N    . ALA   B 1 41  ? 67.992  53.485  41.916  1   26.69 ? 63  ALA   B N    1 
ATOM   3036 C  CA   . ALA   B 1 41  ? 68.578  54.832  41.881  1   26.44 ? 63  ALA   B CA   1 
ATOM   3037 C  C    . ALA   B 1 41  ? 67.996  55.614  40.694  1   26.9  ? 63  ALA   B C    1 
ATOM   3038 O  O    . ALA   B 1 41  ? 67.629  56.78   40.852  1   26.99 ? 63  ALA   B O    1 
ATOM   3039 C  CB   . ALA   B 1 41  ? 70.104  54.745  41.782  1   25.79 ? 63  ALA   B CB   1 
ATOM   3040 N  N    . TYR   B 1 42  ? 67.844  54.952  39.506  1   26.62 ? 64  TYR   B N    1 
ATOM   3041 C  CA   . TYR   B 1 42  ? 67.175  55.561  38.35   1   26.54 ? 64  TYR   B CA   1 
ATOM   3042 C  C    . TYR   B 1 42  ? 65.73   55.982  38.745  1   28.12 ? 64  TYR   B C    1 
ATOM   3043 O  O    . TYR   B 1 42  ? 65.348  57.119  38.52   1   28.98 ? 64  TYR   B O    1 
ATOM   3044 C  CB   . TYR   B 1 42  ? 67.071  54.563  37.173  1   25.74 ? 64  TYR   B CB   1 
ATOM   3045 C  CG   . TYR   B 1 42  ? 68.217  54.643  36.197  1   25.5  ? 64  TYR   B CG   1 
ATOM   3046 C  CD1  . TYR   B 1 42  ? 68.301  55.677  35.282  1   25.85 ? 64  TYR   B CD1  1 
ATOM   3047 C  CD2  . TYR   B 1 42  ? 69.226  53.695  36.203  1   25.62 ? 64  TYR   B CD2  1 
ATOM   3048 C  CE1  . TYR   B 1 42  ? 69.383  55.793  34.432  1   26.6  ? 64  TYR   B CE1  1 
ATOM   3049 C  CE2  . TYR   B 1 42  ? 70.3    53.785  35.335  1   26.39 ? 64  TYR   B CE2  1 
ATOM   3050 C  CZ   . TYR   B 1 42  ? 70.367  54.831  34.442  1   27.17 ? 64  TYR   B CZ   1 
ATOM   3051 O  OH   . TYR   B 1 42  ? 71.427  54.956  33.586  1   28.99 ? 64  TYR   B OH   1 
ATOM   3052 N  N    . GLU   B 1 43  ? 64.957  55.079  39.352  1   28.08 ? 65  GLU   B N    1 
ATOM   3053 C  CA   . GLU   B 1 43  ? 63.58   55.359  39.722  1   28.91 ? 65  GLU   B CA   1 
ATOM   3054 C  C    . GLU   B 1 43  ? 63.446  56.473  40.76   1   30.81 ? 65  GLU   B C    1 
ATOM   3055 O  O    . GLU   B 1 43  ? 62.503  57.267  40.662  1   31.66 ? 65  GLU   B O    1 
ATOM   3056 C  CB   . GLU   B 1 43  ? 62.859  54.073  40.152  1   29.62 ? 65  GLU   B CB   1 
ATOM   3057 C  CG   . GLU   B 1 43  ? 62.695  53.075  39.008  1   31.18 ? 65  GLU   B CG   1 
ATOM   3058 C  CD   . GLU   B 1 43  ? 61.741  53.508  37.898  1   36.28 ? 65  GLU   B CD   1 
ATOM   3059 O  OE1  . GLU   B 1 43  ? 60.844  54.336  38.163  1   37.8  ? 65  GLU   B OE1  1 
ATOM   3060 O  OE2  . GLU   B 1 43  ? 61.897  53.031  36.753  1   38.94 ? 65  GLU   B OE2  1 
ATOM   3061 N  N    . LEU   B 1 44  ? 64.408  56.6    41.706  1   30.96 ? 66  LEU   B N    1 
ATOM   3062 C  CA   . LEU   B 1 44  ? 64.367  57.728  42.648  1   31.38 ? 66  LEU   B CA   1 
ATOM   3063 C  C    . LEU   B 1 44  ? 64.537  59.048  41.891  1   31.79 ? 66  LEU   B C    1 
ATOM   3064 O  O    . LEU   B 1 44  ? 63.782  59.991  42.121  1   33.24 ? 66  LEU   B O    1 
ATOM   3065 C  CB   . LEU   B 1 44  ? 65.467  57.618  43.712  1   31.37 ? 66  LEU   B CB   1 
ATOM   3066 C  CG   . LEU   B 1 44  ? 65.299  56.593  44.817  1   32.01 ? 66  LEU   B CG   1 
ATOM   3067 C  CD1  . LEU   B 1 44  ? 66.413  56.771  45.835  1   31.86 ? 66  LEU   B CD1  1 
ATOM   3068 C  CD2  . LEU   B 1 44  ? 63.927  56.725  45.522  1   32.1  ? 66  LEU   B CD2  1 
ATOM   3069 N  N    . TRP   B 1 45  ? 65.499  59.104  40.957  1   30.61 ? 67  TRP   B N    1 
ATOM   3070 C  CA   . TRP   B 1 45  ? 65.746  60.303  40.178  1   30.33 ? 67  TRP   B CA   1 
ATOM   3071 C  C    . TRP   B 1 45  ? 64.638  60.599  39.175  1   30.57 ? 67  TRP   B C    1 
ATOM   3072 O  O    . TRP   B 1 45  ? 64.356  61.767  38.94   1   30.53 ? 67  TRP   B O    1 
ATOM   3073 C  CB   . TRP   B 1 45  ? 67.133  60.258  39.51   1   30.26 ? 67  TRP   B CB   1 
ATOM   3074 C  CG   . TRP   B 1 45  ? 68.265  60.369  40.501  1   30.41 ? 67  TRP   B CG   1 
ATOM   3075 C  CD1  . TRP   B 1 45  ? 69.173  59.402  40.822  1   30.58 ? 67  TRP   B CD1  1 
ATOM   3076 C  CD2  . TRP   B 1 45  ? 68.555  61.491  41.349  1   30.13 ? 67  TRP   B CD2  1 
ATOM   3077 N  NE1  . TRP   B 1 45  ? 70.023  59.858  41.798  1   31.03 ? 67  TRP   B NE1  1 
ATOM   3078 C  CE2  . TRP   B 1 45  ? 69.667  61.138  42.143  1   30.94 ? 67  TRP   B CE2  1 
ATOM   3079 C  CE3  . TRP   B 1 45  ? 67.993  62.766  41.498  1   30.21 ? 67  TRP   B CE3  1 
ATOM   3080 C  CZ2  . TRP   B 1 45  ? 70.228  62.013  43.071  1   31.13 ? 67  TRP   B CZ2  1 
ATOM   3081 C  CZ3  . TRP   B 1 45  ? 68.551  63.633  42.415  1   31.28 ? 67  TRP   B CZ3  1 
ATOM   3082 C  CH2  . TRP   B 1 45  ? 69.643  63.247  43.205  1   31.34 ? 67  TRP   B CH2  1 
ATOM   3083 N  N    . PHE   B 1 46  ? 63.973  59.561  38.62   1   30.27 ? 68  PHE   B N    1 
ATOM   3084 C  CA   . PHE   B 1 46  ? 62.817  59.722  37.729  1   30.71 ? 68  PHE   B CA   1 
ATOM   3085 C  C    . PHE   B 1 46  ? 61.697  60.432  38.542  1   33.03 ? 68  PHE   B C    1 
ATOM   3086 O  O    . PHE   B 1 46  ? 61.079  61.372  38.039  1   33.61 ? 68  PHE   B O    1 
ATOM   3087 C  CB   . PHE   B 1 46  ? 62.279  58.35   37.246  1   28.76 ? 68  PHE   B CB   1 
ATOM   3088 C  CG   . PHE   B 1 46  ? 63.058  57.644  36.162  1   27.59 ? 68  PHE   B CG   1 
ATOM   3089 C  CD1  . PHE   B 1 46  ? 64.088  58.286  35.494  1   27.25 ? 68  PHE   B CD1  1 
ATOM   3090 C  CD2  . PHE   B 1 46  ? 62.782  56.329  35.833  1   27.82 ? 68  PHE   B CD2  1 
ATOM   3091 C  CE1  . PHE   B 1 46  ? 64.833  57.618  34.535  1   27.58 ? 68  PHE   B CE1  1 
ATOM   3092 C  CE2  . PHE   B 1 46  ? 63.524  55.664  34.864  1   27.72 ? 68  PHE   B CE2  1 
ATOM   3093 C  CZ   . PHE   B 1 46  ? 64.54   56.315  34.218  1   27.17 ? 68  PHE   B CZ   1 
ATOM   3094 N  N    . LYS   B 1 47  ? 61.496  60.023  39.822  1   33.62 ? 69  LYS   B N    1 
ATOM   3095 C  CA   . LYS   B 1 47  ? 60.511  60.663  40.691  1   34.44 ? 69  LYS   B CA   1 
ATOM   3096 C  C    . LYS   B 1 47  ? 60.857  62.145  40.909  1   35.23 ? 69  LYS   B C    1 
ATOM   3097 O  O    . LYS   B 1 47  ? 59.967  62.981  40.909  1   35.99 ? 69  LYS   B O    1 
ATOM   3098 C  CB   . LYS   B 1 47  ? 60.368  59.903  42.02   1   35.94 ? 69  LYS   B CB   1 
ATOM   3099 C  CG   . LYS   B 1 47  ? 59.212  60.426  42.871  1   37.93 ? 69  LYS   B CG   1 
ATOM   3100 C  CD   . LYS   B 1 47  ? 58.918  59.554  44.066  1   40.25 ? 69  LYS   B CD   1 
ATOM   3101 C  CE   . LYS   B 1 47  ? 57.73   60.099  44.834  1   42.63 ? 69  LYS   B CE   1 
ATOM   3102 N  NZ   . LYS   B 1 47  ? 57.231  59.123  45.823  1   43.32 ? 69  LYS   B NZ   1 
ATOM   3103 N  N    . GLN   B 1 48  ? 62.149  62.483  41.029  1   34.74 ? 70  GLN   B N    1 
ATOM   3104 C  CA   . GLN   B 1 48  ? 62.575  63.874  41.167  1   34.06 ? 70  GLN   B CA   1 
ATOM   3105 C  C    . GLN   B 1 48  ? 62.331  64.673  39.876  1   34.76 ? 70  GLN   B C    1 
ATOM   3106 O  O    . GLN   B 1 48  ? 61.83   65.8    39.928  1   35.41 ? 70  GLN   B O    1 
ATOM   3107 C  CB   . GLN   B 1 48  ? 64.052  63.967  41.575  1   33.26 ? 70  GLN   B CB   1 
ATOM   3108 C  CG   . GLN   B 1 48  ? 64.49   65.391  41.883  1   32.82 ? 70  GLN   B CG   1 
ATOM   3109 C  CD   . GLN   B 1 48  ? 63.781  65.927  43.101  1   32.37 ? 70  GLN   B CD   1 
ATOM   3110 O  OE1  . GLN   B 1 48  ? 63.543  65.204  44.075  1   32.32 ? 70  GLN   B OE1  1 
ATOM   3111 N  NE2  . GLN   B 1 48  ? 63.436  67.197  43.073  1   31.54 ? 70  GLN   B NE2  1 
ATOM   3112 N  N    . ILE   B 1 49  ? 62.673  64.098  38.721  1   34.33 ? 71  ILE   B N    1 
ATOM   3113 C  CA   . ILE   B 1 49  ? 62.439  64.735  37.423  1   34.58 ? 71  ILE   B CA   1 
ATOM   3114 C  C    . ILE   B 1 49  ? 60.928  64.97   37.216  1   35.52 ? 71  ILE   B C    1 
ATOM   3115 O  O    . ILE   B 1 49  ? 60.543  66.033  36.779  1   35.42 ? 71  ILE   B O    1 
ATOM   3116 C  CB   . ILE   B 1 49  ? 63.047  63.881  36.276  1   34.19 ? 71  ILE   B CB   1 
ATOM   3117 C  CG1  . ILE   B 1 49  ? 64.597  63.852  36.373  1   34.47 ? 71  ILE   B CG1  1 
ATOM   3118 C  CG2  . ILE   B 1 49  ? 62.574  64.39   34.902  1   34.57 ? 71  ILE   B CG2  1 
ATOM   3119 C  CD1  . ILE   B 1 49  ? 65.279  62.865  35.413  1   35.32 ? 71  ILE   B CD1  1 
ATOM   3120 N  N    . ILE   B 1 50  ? 60.08   64.004  37.591  1   36.48 ? 72  ILE   B N    1 
ATOM   3121 C  CA   . ILE   B 1 50  ? 58.634  64.157  37.473  1   38.22 ? 72  ILE   B CA   1 
ATOM   3122 C  C    . ILE   B 1 50  ? 58.154  65.292  38.37   1   40.45 ? 72  ILE   B C    1 
ATOM   3123 O  O    . ILE   B 1 50  ? 57.448  66.188  37.91   1   41.14 ? 72  ILE   B O    1 
ATOM   3124 C  CB   . ILE   B 1 50  ? 57.908  62.817  37.71   1   38.29 ? 72  ILE   B CB   1 
ATOM   3125 C  CG1  . ILE   B 1 50  ? 58.229  61.857  36.544  1   38.71 ? 72  ILE   B CG1  1 
ATOM   3126 C  CG2  . ILE   B 1 50  ? 56.385  63.028  37.857  1   38.9  ? 72  ILE   B CG2  1 
ATOM   3127 C  CD1  . ILE   B 1 50  ? 57.817  60.482  36.74   1   40    ? 72  ILE   B CD1  1 
ATOM   3128 N  N    . PHE   B 1 51  ? 58.663  65.333  39.598  1   41.11 ? 73  PHE   B N    1 
ATOM   3129 C  CA   . PHE   B 1 51  ? 58.347  66.392  40.55   1   42.09 ? 73  PHE   B CA   1 
ATOM   3130 C  C    . PHE   B 1 51  ? 58.724  67.776  40.007  1   41.94 ? 73  PHE   B C    1 
ATOM   3131 O  O    . PHE   B 1 51  ? 57.923  68.703  40.109  1   42.35 ? 73  PHE   B O    1 
ATOM   3132 C  CB   . PHE   B 1 51  ? 59.057  66.124  41.877  1   42.53 ? 73  PHE   B CB   1 
ATOM   3133 C  CG   . PHE   B 1 51  ? 58.519  66.918  43.035  1   43.62 ? 73  PHE   B CG   1 
ATOM   3134 C  CD1  . PHE   B 1 51  ? 57.326  66.566  43.639  1   44.66 ? 73  PHE   B CD1  1 
ATOM   3135 C  CD2  . PHE   B 1 51  ? 59.229  67.985  43.553  1   44.39 ? 73  PHE   B CD2  1 
ATOM   3136 C  CE1  . PHE   B 1 51  ? 56.843  67.278  44.727  1   45.36 ? 73  PHE   B CE1  1 
ATOM   3137 C  CE2  . PHE   B 1 51  ? 58.734  68.703  44.634  1   45.52 ? 73  PHE   B CE2  1 
ATOM   3138 C  CZ   . PHE   B 1 51  ? 57.549  68.344  45.215  1   45.16 ? 73  PHE   B CZ   1 
ATOM   3139 N  N    . GLU   B 1 52  ? 59.929  67.917  39.424  1   41.29 ? 74  GLU   B N    1 
ATOM   3140 C  CA   . GLU   B 1 52  ? 60.371  69.187  38.868  1   40.65 ? 74  GLU   B CA   1 
ATOM   3141 C  C    . GLU   B 1 52  ? 59.521  69.557  37.663  1   41.12 ? 74  GLU   B C    1 
ATOM   3142 O  O    . GLU   B 1 52  ? 59.09   70.703  37.562  1   40.72 ? 74  GLU   B O    1 
ATOM   3143 C  CB   . GLU   B 1 52  ? 61.856  69.136  38.468  1   41.38 ? 74  GLU   B CB   1 
ATOM   3144 C  CG   . GLU   B 1 52  ? 62.807  68.811  39.611  1   43.16 ? 74  GLU   B CG   1 
ATOM   3145 C  CD   . GLU   B 1 52  ? 62.905  69.855  40.709  1   44.95 ? 74  GLU   B CD   1 
ATOM   3146 O  OE1  . GLU   B 1 52  ? 62.555  71.026  40.44   1   44.04 ? 74  GLU   B OE1  1 
ATOM   3147 O  OE2  . GLU   B 1 52  ? 63.342  69.508  41.834  1   45.11 ? 74  GLU   B OE2  1 
ATOM   3148 N  N    . PHE   B 1 53  ? 59.262  68.586  36.761  1   41.15 ? 75  PHE   B N    1 
ATOM   3149 C  CA   . PHE   B 1 53  ? 58.46   68.796  35.556  1   41.48 ? 75  PHE   B CA   1 
ATOM   3150 C  C    . PHE   B 1 53  ? 57.051  69.283  35.899  1   41.69 ? 75  PHE   B C    1 
ATOM   3151 O  O    . PHE   B 1 53  ? 56.629  70.288  35.344  1   41.49 ? 75  PHE   B O    1 
ATOM   3152 C  CB   . PHE   B 1 53  ? 58.389  67.506  34.713  1   41.42 ? 75  PHE   B CB   1 
ATOM   3153 C  CG   . PHE   B 1 53  ? 59.519  67.267  33.723  1   41.77 ? 75  PHE   B CG   1 
ATOM   3154 C  CD1  . PHE   B 1 53  ? 60.635  68.092  33.698  1   42.27 ? 75  PHE   B CD1  1 
ATOM   3155 C  CD2  . PHE   B 1 53  ? 59.446  66.235  32.801  1   42.06 ? 75  PHE   B CD2  1 
ATOM   3156 C  CE1  . PHE   B 1 53  ? 61.655  67.88   32.776  1   42.64 ? 75  PHE   B CE1  1 
ATOM   3157 C  CE2  . PHE   B 1 53  ? 60.474  66.018  31.897  1   42.47 ? 75  PHE   B CE2  1 
ATOM   3158 C  CZ   . PHE   B 1 53  ? 61.57   66.843  31.889  1   42.27 ? 75  PHE   B CZ   1 
ATOM   3159 N  N    . ASP   B 1 54  ? 56.351  68.613  36.838  1   41.8  ? 76  ASP   B N    1 
ATOM   3160 C  CA   . ASP   B 1 54  ? 55.002  69.003  37.249  1   42.78 ? 76  ASP   B CA   1 
ATOM   3161 C  C    . ASP   B 1 54  ? 54.954  70.423  37.811  1   45.14 ? 76  ASP   B C    1 
ATOM   3162 O  O    . ASP   B 1 54  ? 54.047  71.187  37.459  1   45.8  ? 76  ASP   B O    1 
ATOM   3163 C  CB   . ASP   B 1 54  ? 54.404  67.994  38.238  1   42.59 ? 76  ASP   B CB   1 
ATOM   3164 C  CG   . ASP   B 1 54  ? 53.981  66.678  37.598  1   46.42 ? 76  ASP   B CG   1 
ATOM   3165 O  OD1  . ASP   B 1 54  ? 53.874  66.626  36.353  1   47.96 ? 76  ASP   B OD1  1 
ATOM   3166 O  OD2  . ASP   B 1 54  ? 53.753  65.699  38.34   1   47.55 ? 76  ASP   B OD2  1 
ATOM   3167 N  N    . SER   B 1 55  ? 55.969  70.811  38.608  1   45.73 ? 77  SER   B N    1 
ATOM   3168 C  CA   . SER   B 1 55  ? 56.045  72.157  39.166  1   46.79 ? 77  SER   B CA   1 
ATOM   3169 C  C    . SER   B 1 55  ? 56.297  73.196  38.077  1   48.05 ? 77  SER   B C    1 
ATOM   3170 O  O    . SER   B 1 55  ? 55.767  74.302  38.168  1   49.09 ? 77  SER   B O    1 
ATOM   3171 C  CB   . SER   B 1 55  ? 57.095  72.234  40.283  1   48.09 ? 77  SER   B CB   1 
ATOM   3172 O  OG   . SER   B 1 55  ? 58.424  72.501  39.846  1   49.63 ? 77  SER   B OG   1 
ATOM   3173 N  N    . ILE   B 1 56  ? 57.086  72.848  37.046  1   48.06 ? 78  ILE   B N    1 
ATOM   3174 C  CA   . ILE   B 1 56  ? 57.375  73.752  35.927  1   49.28 ? 78  ILE   B CA   1 
ATOM   3175 C  C    . ILE   B 1 56  ? 56.119  73.892  35.045  1   51.17 ? 78  ILE   B C    1 
ATOM   3176 O  O    . ILE   B 1 56  ? 55.817  74.987  34.577  1   50.9  ? 78  ILE   B O    1 
ATOM   3177 C  CB   . ILE   B 1 56  ? 58.628  73.289  35.122  1   49.05 ? 78  ILE   B CB   1 
ATOM   3178 C  CG1  . ILE   B 1 56  ? 59.905  73.379  35.976  1   49.72 ? 78  ILE   B CG1  1 
ATOM   3179 C  CG2  . ILE   B 1 56  ? 58.805  74.073  33.825  1   48.99 ? 78  ILE   B CG2  1 
ATOM   3180 C  CD1  . ILE   B 1 56  ? 61.077  72.576  35.409  1   50.76 ? 78  ILE   B CD1  1 
ATOM   3181 N  N    . ARG   B 1 57  ? 55.363  72.796  34.869  1   52.5  ? 79  ARG   B N    1 
ATOM   3182 C  CA   . ARG   B 1 57  ? 54.13   72.801  34.097  1   54.21 ? 79  ARG   B CA   1 
ATOM   3183 C  C    . ARG   B 1 57  ? 53.09   73.699  34.773  1   55.97 ? 79  ARG   B C    1 
ATOM   3184 O  O    . ARG   B 1 57  ? 52.411  74.446  34.086  1   55.75 ? 79  ARG   B O    1 
ATOM   3185 C  CB   . ARG   B 1 57  ? 53.582  71.378  33.908  1   55.03 ? 79  ARG   B CB   1 
ATOM   3186 C  CG   . ARG   B 1 57  ? 54.391  70.503  32.937  1   57.09 ? 79  ARG   B CG   1 
ATOM   3187 C  CD   . ARG   B 1 57  ? 53.74   69.157  32.603  1   59.25 ? 79  ARG   B CD   1 
ATOM   3188 N  NE   . ARG   B 1 57  ? 53.084  68.545  33.763  1   61.43 ? 79  ARG   B NE   1 
ATOM   3189 C  CZ   . ARG   B 1 57  ? 51.766  68.488  33.941  1   62.45 ? 79  ARG   B CZ   1 
ATOM   3190 N  NH1  . ARG   B 1 57  ? 50.944  68.965  33.017  1   61.98 ? 79  ARG   B NH1  1 
ATOM   3191 N  NH2  . ARG   B 1 57  ? 51.263  67.943  35.039  1   62.1  ? 79  ARG   B NH2  1 
ATOM   3192 N  N    . ASP   B 1 58  ? 53.002  73.663  36.114  1   57.7  ? 80  ASP   B N    1 
ATOM   3193 C  CA   . ASP   B 1 58  ? 52.078  74.525  36.855  1   59.52 ? 80  ASP   B CA   1 
ATOM   3194 C  C    . ASP   B 1 58  ? 52.462  75.995  36.708  1   60.59 ? 80  ASP   B C    1 
ATOM   3195 O  O    . ASP   B 1 58  ? 51.577  76.833  36.528  1   61.29 ? 80  ASP   B O    1 
ATOM   3196 C  CB   . ASP   B 1 58  ? 52.008  74.142  38.34   1   62.28 ? 80  ASP   B CB   1 
ATOM   3197 C  CG   . ASP   B 1 58  ? 51.442  72.756  38.593  1   69.79 ? 80  ASP   B CG   1 
ATOM   3198 O  OD1  . ASP   B 1 58  ? 50.734  72.228  37.7    1   71.56 ? 80  ASP   B OD1  1 
ATOM   3199 O  OD2  . ASP   B 1 58  ? 51.724  72.188  39.672  1   72.58 ? 80  ASP   B OD2  1 
ATOM   3200 N  N    . MET   B 1 59  ? 53.767  76.312  36.746  1   60.62 ? 81  MET   B N    1 
ATOM   3201 C  CA   . MET   B 1 59  ? 54.214  77.695  36.584  1   61.57 ? 81  MET   B CA   1 
ATOM   3202 C  C    . MET   B 1 59  ? 53.969  78.204  35.15   1   63    ? 81  MET   B C    1 
ATOM   3203 O  O    . MET   B 1 59  ? 53.67   79.379  34.958  1   63.54 ? 81  MET   B O    1 
ATOM   3204 C  CB   . MET   B 1 59  ? 55.696  77.861  36.97   1   61.69 ? 81  MET   B CB   1 
ATOM   3205 C  CG   . MET   B 1 59  ? 55.975  77.644  38.43   1   63.39 ? 81  MET   B CG   1 
ATOM   3206 S  SD   . MET   B 1 59  ? 57.706  77.993  38.823  1   66.63 ? 81  MET   B SD   1 
ATOM   3207 C  CE   . MET   B 1 59  ? 57.567  79.587  39.472  1   67.85 ? 81  MET   B CE   1 
ATOM   3208 N  N    . LEU   B 1 60  ? 54.093  77.323  34.153  1   63.64 ? 82  LEU   B N    1 
ATOM   3209 C  CA   . LEU   B 1 60  ? 53.872  77.665  32.748  1   64.94 ? 82  LEU   B CA   1 
ATOM   3210 C  C    . LEU   B 1 60  ? 52.371  77.723  32.375  1   66.38 ? 82  LEU   B C    1 
ATOM   3211 O  O    . LEU   B 1 60  ? 52.012  78.365  31.385  1   66.1  ? 82  LEU   B O    1 
ATOM   3212 C  CB   . LEU   B 1 60  ? 54.609  76.673  31.832  1   64.97 ? 82  LEU   B CB   1 
ATOM   3213 C  CG   . LEU   B 1 60  ? 56.128  76.825  31.749  1   66.44 ? 82  LEU   B CG   1 
ATOM   3214 C  CD1  . LEU   B 1 60  ? 56.728  75.748  30.861  1   67.08 ? 82  LEU   B CD1  1 
ATOM   3215 C  CD2  . LEU   B 1 60  ? 56.525  78.207  31.224  1   67.02 ? 82  LEU   B CD2  1 
ATOM   3216 N  N    . ASP   B 1 61  ? 51.502  77.049  33.152  1   67.63 ? 83  ASP   B N    1 
ATOM   3217 C  CA   . ASP   B 1 61  ? 50.063  77.05   32.896  1   69.41 ? 83  ASP   B CA   1 
ATOM   3218 C  C    . ASP   B 1 61  ? 49.418  78.247  33.593  1   71.12 ? 83  ASP   B C    1 
ATOM   3219 O  O    . ASP   B 1 61  ? 48.574  78.096  34.478  1   71.28 ? 83  ASP   B O    1 
ATOM   3220 C  CB   . ASP   B 1 61  ? 49.399  75.732  33.347  1   71.05 ? 83  ASP   B CB   1 
ATOM   3221 C  CG   . ASP   B 1 61  ? 48.131  75.371  32.575  1   75.7  ? 83  ASP   B CG   1 
ATOM   3222 O  OD1  . ASP   B 1 61  ? 47.756  76.125  31.65   1   76.24 ? 83  ASP   B OD1  1 
ATOM   3223 O  OD2  . ASP   B 1 61  ? 47.529  74.322  32.879  1   78.11 ? 83  ASP   B OD2  1 
ATOM   3224 N  N    . ALA   B 1 62  ? 49.829  79.44   33.187  1   72.09 ? 84  ALA   B N    1 
ATOM   3225 C  CA   . ALA   B 1 62  ? 49.327  80.687  33.736  1   73.32 ? 84  ALA   B CA   1 
ATOM   3226 C  C    . ALA   B 1 62  ? 49.436  81.791  32.673  1   74.43 ? 84  ALA   B C    1 
ATOM   3227 O  O    . ALA   B 1 62  ? 50.313  81.731  31.802  1   74.6  ? 84  ALA   B O    1 
ATOM   3228 C  CB   . ALA   B 1 62  ? 50.129  81.067  34.974  1   73.58 ? 84  ALA   B CB   1 
ATOM   3229 N  N    . GLU   B 1 63  ? 48.54   82.792  32.73   1   74.83 ? 85  GLU   B N    1 
ATOM   3230 C  CA   . GLU   B 1 63  ? 48.578  83.898  31.77   1   75.41 ? 85  GLU   B CA   1 
ATOM   3231 C  C    . GLU   B 1 63  ? 49.806  84.775  32.019  1   75.42 ? 85  GLU   B C    1 
ATOM   3232 O  O    . GLU   B 1 63  ? 50.471  85.199  31.068  1   75.3  ? 85  GLU   B O    1 
ATOM   3233 C  CB   . GLU   B 1 63  ? 47.29   84.735  31.85   1   77.66 ? 85  GLU   B CB   1 
ATOM   3234 N  N    . VAL   B 1 64  ? 50.131  85.007  33.308  1   75.17 ? 86  VAL   B N    1 
ATOM   3235 C  CA   . VAL   B 1 64  ? 51.278  85.823  33.693  1   75.13 ? 86  VAL   B CA   1 
ATOM   3236 C  C    . VAL   B 1 64  ? 52.541  85.012  34.068  1   74.65 ? 86  VAL   B C    1 
ATOM   3237 O  O    . VAL   B 1 64  ? 52.589  84.397  35.138  1   74.72 ? 86  VAL   B O    1 
ATOM   3238 C  CB   . VAL   B 1 64  ? 50.894  86.802  34.824  1   75.91 ? 86  VAL   B CB   1 
ATOM   3239 N  N    . ILE   B 1 65  ? 53.578  85.058  33.207  1   73.76 ? 87  ILE   B N    1 
ATOM   3240 C  CA   . ILE   B 1 65  ? 54.875  84.422  33.476  1   73.11 ? 87  ILE   B CA   1 
ATOM   3241 C  C    . ILE   B 1 65  ? 55.917  85.539  33.68   1   71.89 ? 87  ILE   B C    1 
ATOM   3242 O  O    . ILE   B 1 65  ? 56.522  86.021  32.719  1   71.58 ? 87  ILE   B O    1 
ATOM   3243 C  CB   . ILE   B 1 65  ? 55.279  83.395  32.377  1   73.87 ? 87  ILE   B CB   1 
ATOM   3244 C  CG1  . ILE   B 1 65  ? 54.193  82.298  32.238  1   74.5  ? 87  ILE   B CG1  1 
ATOM   3245 C  CG2  . ILE   B 1 65  ? 56.655  82.769  32.684  1   74.63 ? 87  ILE   B CG2  1 
ATOM   3246 C  CD1  . ILE   B 1 65  ? 54.352  81.411  31.111  1   75.5  ? 87  ILE   B CD1  1 
ATOM   3247 N  N    . ASP   B 1 66  ? 56.078  85.993  34.934  1   71.16 ? 88  ASP   B N    1 
ATOM   3248 C  CA   . ASP   B 1 66  ? 57      87.088  35.246  1   71.1  ? 88  ASP   B CA   1 
ATOM   3249 C  C    . ASP   B 1 66  ? 58.491  86.65   35.246  1   69.78 ? 88  ASP   B C    1 
ATOM   3250 O  O    . ASP   B 1 66  ? 58.788  85.466  35.091  1   69.87 ? 88  ASP   B O    1 
ATOM   3251 C  CB   . ASP   B 1 66  ? 56.588  87.815  36.56   1   73.84 ? 88  ASP   B CB   1 
ATOM   3252 C  CG   . ASP   B 1 66  ? 56.691  87.023  37.862  1   80.38 ? 88  ASP   B CG   1 
ATOM   3253 O  OD1  . ASP   B 1 66  ? 57.371  85.984  37.872  1   82.05 ? 88  ASP   B OD1  1 
ATOM   3254 O  OD2  . ASP   B 1 66  ? 56.105  87.466  38.878  1   82.5  ? 88  ASP   B OD2  1 
ATOM   3255 N  N    . GLU   B 1 67  ? 59.417  87.608  35.392  1   68.58 ? 89  GLU   B N    1 
ATOM   3256 C  CA   . GLU   B 1 67  ? 60.85   87.333  35.413  1   68.02 ? 89  GLU   B CA   1 
ATOM   3257 C  C    . GLU   B 1 67  ? 61.281  86.508  36.631  1   67.02 ? 89  GLU   B C    1 
ATOM   3258 O  O    . GLU   B 1 67  ? 62.272  85.788  36.553  1   67.28 ? 89  GLU   B O    1 
ATOM   3259 C  CB   . GLU   B 1 67  ? 61.642  88.637  35.359  1   70.35 ? 89  GLU   B CB   1 
ATOM   3260 C  CG   . GLU   B 1 67  ? 61.469  89.381  34.055  1   76.46 ? 89  GLU   B CG   1 
ATOM   3261 C  CD   . GLU   B 1 67  ? 62.154  90.73   34.021  1   85.21 ? 89  GLU   B CD   1 
ATOM   3262 O  OE1  . GLU   B 1 67  ? 61.466  91.75   34.259  1   87.44 ? 89  GLU   B OE1  1 
ATOM   3263 O  OE2  . GLU   B 1 67  ? 63.377  90.769  33.754  1   87.76 ? 89  GLU   B OE2  1 
ATOM   3264 N  N    . THR   B 1 68  ? 60.549  86.612  37.745  1   65.59 ? 90  THR   B N    1 
ATOM   3265 C  CA   . THR   B 1 68  ? 60.861  85.876  38.965  1   64.59 ? 90  THR   B CA   1 
ATOM   3266 C  C    . THR   B 1 68  ? 60.558  84.39   38.768  1   63.49 ? 90  THR   B C    1 
ATOM   3267 O  O    . THR   B 1 68  ? 61.364  83.543  39.154  1   63.93 ? 90  THR   B O    1 
ATOM   3268 C  CB   . THR   B 1 68  ? 60.129  86.513  40.163  1   65.4  ? 90  THR   B CB   1 
ATOM   3269 O  OG1  . THR   B 1 68  ? 60.54   87.87   40.271  1   66.27 ? 90  THR   B OG1  1 
ATOM   3270 C  CG2  . THR   B 1 68  ? 60.405  85.81   41.476  1   65.54 ? 90  THR   B CG2  1 
ATOM   3271 N  N    . LYS   B 1 69  ? 59.421  84.078  38.14   1   61.9  ? 91  LYS   B N    1 
ATOM   3272 C  CA   . LYS   B 1 69  ? 59.021  82.701  37.858  1   60.94 ? 91  LYS   B CA   1 
ATOM   3273 C  C    . LYS   B 1 69  ? 59.893  82.09   36.754  1   59.38 ? 91  LYS   B C    1 
ATOM   3274 O  O    . LYS   B 1 69  ? 60.183  80.902  36.813  1   59.37 ? 91  LYS   B O    1 
ATOM   3275 C  CB   . LYS   B 1 69  ? 57.525  82.619  37.492  1   62.65 ? 91  LYS   B CB   1 
ATOM   3276 N  N    . THR   B 1 70  ? 60.34   82.905  35.781  1   58    ? 92  THR   B N    1 
ATOM   3277 C  CA   . THR   B 1 70  ? 61.203  82.484  34.673  1   57.27 ? 92  THR   B CA   1 
ATOM   3278 C  C    . THR   B 1 70  ? 62.554  82.007  35.215  1   55.89 ? 92  THR   B C    1 
ATOM   3279 O  O    . THR   B 1 70  ? 63.048  80.956  34.8    1   55.81 ? 92  THR   B O    1 
ATOM   3280 C  CB   . THR   B 1 70  ? 61.349  83.641  33.669  1   59.14 ? 92  THR   B CB   1 
ATOM   3281 O  OG1  . THR   B 1 70  ? 60.046  83.984  33.191  1   60.99 ? 92  THR   B OG1  1 
ATOM   3282 C  CG2  . THR   B 1 70  ? 62.286  83.312  32.49   1   59.46 ? 92  THR   B CG2  1 
ATOM   3283 N  N    . LEU   B 1 71  ? 63.117  82.753  36.185  1   54.25 ? 93  LEU   B N    1 
ATOM   3284 C  CA   . LEU   B 1 71  ? 64.373  82.4    36.846  1   53.2  ? 93  LEU   B CA   1 
ATOM   3285 C  C    . LEU   B 1 71  ? 64.249  81.071  37.598  1   51.1  ? 93  LEU   B C    1 
ATOM   3286 O  O    . LEU   B 1 71  ? 65.201  80.294  37.637  1   51.4  ? 93  LEU   B O    1 
ATOM   3287 C  CB   . LEU   B 1 71  ? 64.756  83.491  37.852  1   54.03 ? 93  LEU   B CB   1 
ATOM   3288 C  CG   . LEU   B 1 71  ? 65.333  84.752  37.261  1   56.12 ? 93  LEU   B CG   1 
ATOM   3289 C  CD1  . LEU   B 1 71  ? 65.556  85.789  38.346  1   56.77 ? 93  LEU   B CD1  1 
ATOM   3290 C  CD2  . LEU   B 1 71  ? 66.626  84.461  36.52   1   56.77 ? 93  LEU   B CD2  1 
ATOM   3291 N  N    . GLU   B 1 72  ? 63.091  80.833  38.213  1   48.84 ? 94  GLU   B N    1 
ATOM   3292 C  CA   . GLU   B 1 72  ? 62.825  79.622  38.964  1   47.87 ? 94  GLU   B CA   1 
ATOM   3293 C  C    . GLU   B 1 72  ? 62.661  78.42   38.03   1   47.54 ? 94  GLU   B C    1 
ATOM   3294 O  O    . GLU   B 1 72  ? 63.044  77.304  38.393  1   48.12 ? 94  GLU   B O    1 
ATOM   3295 C  CB   . GLU   B 1 72  ? 61.589  79.806  39.86   1   48.63 ? 94  GLU   B CB   1 
ATOM   3296 C  CG   . GLU   B 1 72  ? 61.4    78.702  40.886  1   52.86 ? 94  GLU   B CG   1 
ATOM   3297 C  CD   . GLU   B 1 72  ? 62.368  78.717  42.053  1   59.65 ? 94  GLU   B CD   1 
ATOM   3298 O  OE1  . GLU   B 1 72  ? 63.074  79.735  42.24   1   60.26 ? 94  GLU   B OE1  1 
ATOM   3299 O  OE2  . GLU   B 1 72  ? 62.405  77.715  42.8    1   63.48 ? 94  GLU   B OE2  1 
ATOM   3300 N  N    . ILE   B 1 73  ? 62.081  78.64   36.846  1   46.16 ? 95  ILE   B N    1 
ATOM   3301 C  CA   . ILE   B 1 73  ? 61.923  77.586  35.86   1   45.75 ? 95  ILE   B CA   1 
ATOM   3302 C  C    . ILE   B 1 73  ? 63.326  77.215  35.332  1   45.41 ? 95  ILE   B C    1 
ATOM   3303 O  O    . ILE   B 1 73  ? 63.645  76.039  35.269  1   45.75 ? 95  ILE   B O    1 
ATOM   3304 C  CB   . ILE   B 1 73  ? 60.956  78.034  34.727  1   45.54 ? 95  ILE   B CB   1 
ATOM   3305 C  CG1  . ILE   B 1 73  ? 59.503  78.142  35.248  1   45.85 ? 95  ILE   B CG1  1 
ATOM   3306 C  CG2  . ILE   B 1 73  ? 61.035  77.076  33.542  1   46.07 ? 95  ILE   B CG2  1 
ATOM   3307 C  CD1  . ILE   B 1 73  ? 58.538  78.883  34.308  1   46.79 ? 95  ILE   B CD1  1 
ATOM   3308 N  N    . VAL   B 1 74  ? 64.163  78.22   34.997  1   44.41 ? 96  VAL   B N    1 
ATOM   3309 C  CA   . VAL   B 1 74  ? 65.533  78.029  34.525  1   44.12 ? 96  VAL   B CA   1 
ATOM   3310 C  C    . VAL   B 1 74  ? 66.357  77.246  35.57   1   44.08 ? 96  VAL   B C    1 
ATOM   3311 O  O    . VAL   B 1 74  ? 67.045  76.293  35.214  1   44.11 ? 96  VAL   B O    1 
ATOM   3312 C  CB   . VAL   B 1 74  ? 66.182  79.379  34.121  1   44.63 ? 96  VAL   B CB   1 
ATOM   3313 C  CG1  . VAL   B 1 74  ? 67.7    79.272  34.008  1   45.06 ? 96  VAL   B CG1  1 
ATOM   3314 C  CG2  . VAL   B 1 74  ? 65.584  79.907  32.818  1   44.98 ? 96  VAL   B CG2  1 
ATOM   3315 N  N    . LYS   B 1 75  ? 66.19   77.567  36.857  1   43.87 ? 97  LYS   B N    1 
ATOM   3316 C  CA   . LYS   B 1 75  ? 66.877  76.845  37.924  1   43.85 ? 97  LYS   B CA   1 
ATOM   3317 C  C    . LYS   B 1 75  ? 66.488  75.368  37.953  1   43.98 ? 97  LYS   B C    1 
ATOM   3318 O  O    . LYS   B 1 75  ? 67.364  74.51   38.062  1   44.82 ? 97  LYS   B O    1 
ATOM   3319 C  CB   . LYS   B 1 75  ? 66.627  77.51   39.296  1   44.99 ? 97  LYS   B CB   1 
ATOM   3320 C  CG   . LYS   B 1 75  ? 67.163  76.714  40.5    1   47.68 ? 97  LYS   B CG   1 
ATOM   3321 C  CD   . LYS   B 1 75  ? 66.901  77.43   41.835  1   51.24 ? 97  LYS   B CD   1 
ATOM   3322 N  N    . ARG   B 1 76  ? 65.197  75.063  37.861  1   43.18 ? 98  ARG   B N    1 
ATOM   3323 C  CA   . ARG   B 1 76  ? 64.73   73.68   37.932  1   42.63 ? 98  ARG   B CA   1 
ATOM   3324 C  C    . ARG   B 1 76  ? 65.001  72.881  36.649  1   41.58 ? 98  ARG   B C    1 
ATOM   3325 O  O    . ARG   B 1 76  ? 65.265  71.679  36.736  1   41.95 ? 98  ARG   B O    1 
ATOM   3326 C  CB   . ARG   B 1 76  ? 63.26   73.615  38.355  1   44.15 ? 98  ARG   B CB   1 
ATOM   3327 C  CG   . ARG   B 1 76  ? 63.036  74.327  39.681  1   46.88 ? 98  ARG   B CG   1 
ATOM   3328 C  CD   . ARG   B 1 76  ? 61.618  74.195  40.197  1   48.78 ? 98  ARG   B CD   1 
ATOM   3329 N  NE   . ARG   B 1 76  ? 61.41   75.018  41.388  1   49.97 ? 98  ARG   B NE   1 
ATOM   3330 C  CZ   . ARG   B 1 76  ? 60.231  75.213  41.969  1   50.75 ? 98  ARG   B CZ   1 
ATOM   3331 N  NH1  . ARG   B 1 76  ? 59.14   74.635  41.485  1   49.99 ? 98  ARG   B NH1  1 
ATOM   3332 N  NH2  . ARG   B 1 76  ? 60.136  75.982  43.048  1   49.98 ? 98  ARG   B NH2  1 
ATOM   3333 N  N    . LEU   B 1 77  ? 65.006  73.538  35.485  1   40.2  ? 99  LEU   B N    1 
ATOM   3334 C  CA   . LEU   B 1 77  ? 65.367  72.868  34.24   1   40.04 ? 99  LEU   B CA   1 
ATOM   3335 C  C    . LEU   B 1 77  ? 66.867  72.512  34.302  1   40.45 ? 99  LEU   B C    1 
ATOM   3336 O  O    . LEU   B 1 77  ? 67.246  71.406  33.936  1   41.28 ? 99  LEU   B O    1 
ATOM   3337 C  CB   . LEU   B 1 77  ? 65.085  73.748  33.012  1   39.79 ? 99  LEU   B CB   1 
ATOM   3338 C  CG   . LEU   B 1 77  ? 63.597  73.914  32.601  1   40.98 ? 99  LEU   B CG   1 
ATOM   3339 C  CD1  . LEU   B 1 77  ? 63.437  74.972  31.529  1   40.97 ? 99  LEU   B CD1  1 
ATOM   3340 C  CD2  . LEU   B 1 77  ? 62.994  72.606  32.148  1   41.04 ? 99  LEU   B CD2  1 
ATOM   3341 N  N    . ASN   B 1 78  ? 67.702  73.422  34.819  1   39.55 ? 100 ASN   B N    1 
ATOM   3342 C  CA   . ASN   B 1 78  ? 69.135  73.189  34.97   1   39.26 ? 100 ASN   B CA   1 
ATOM   3343 C  C    . ASN   B 1 78  ? 69.397  72.006  35.929  1   38.78 ? 100 ASN   B C    1 
ATOM   3344 O  O    . ASN   B 1 78  ? 70.296  71.203  35.686  1   39.06 ? 100 ASN   B O    1 
ATOM   3345 C  CB   . ASN   B 1 78  ? 69.846  74.454  35.448  1   39.5  ? 100 ASN   B CB   1 
ATOM   3346 C  CG   . ASN   B 1 78  ? 71.333  74.252  35.588  1   42.59 ? 100 ASN   B CG   1 
ATOM   3347 O  OD1  . ASN   B 1 78  ? 72.063  74.176  34.591  1   44.42 ? 100 ASN   B OD1  1 
ATOM   3348 N  ND2  . ASN   B 1 78  ? 71.807  74.121  36.822  1   41.89 ? 100 ASN   B ND2  1 
ATOM   3349 N  N    . ARG   B 1 79  ? 68.585  71.89   36.984  1   37.31 ? 101 ARG   B N    1 
ATOM   3350 C  CA   . ARG   B 1 79  ? 68.653  70.804  37.936  1   36.56 ? 101 ARG   B CA   1 
ATOM   3351 C  C    . ARG   B 1 79  ? 68.352  69.484  37.242  1   36.65 ? 101 ARG   B C    1 
ATOM   3352 O  O    . ARG   B 1 79  ? 69.064  68.504  37.473  1   37.08 ? 101 ARG   B O    1 
ATOM   3353 C  CB   . ARG   B 1 79  ? 67.656  71.058  39.068  1   36.94 ? 101 ARG   B CB   1 
ATOM   3354 C  CG   . ARG   B 1 79  ? 67.557  69.952  40.098  1   37.74 ? 101 ARG   B CG   1 
ATOM   3355 C  CD   . ARG   B 1 79  ? 66.517  70.302  41.13   1   40.14 ? 101 ARG   B CD   1 
ATOM   3356 N  NE   . ARG   B 1 79  ? 66.85   71.553  41.818  1   43.17 ? 101 ARG   B NE   1 
ATOM   3357 C  CZ   . ARG   B 1 79  ? 66.064  72.162  42.706  1   43.34 ? 101 ARG   B CZ   1 
ATOM   3358 N  NH1  . ARG   B 1 79  ? 64.872  71.657  43.005  1   40.71 ? 101 ARG   B NH1  1 
ATOM   3359 N  NH2  . ARG   B 1 79  ? 66.462  73.281  43.295  1   42.93 ? 101 ARG   B NH2  1 
ATOM   3360 N  N    . VAL   B 1 80  ? 67.326  69.461  36.363  1   36.08 ? 102 VAL   B N    1 
ATOM   3361 C  CA   . VAL   B 1 80  ? 66.966  68.27   35.602  1   35.99 ? 102 VAL   B CA   1 
ATOM   3362 C  C    . VAL   B 1 80  ? 68.123  67.882  34.667  1   35.54 ? 102 VAL   B C    1 
ATOM   3363 O  O    . VAL   B 1 80  ? 68.438  66.705  34.57   1   35.88 ? 102 VAL   B O    1 
ATOM   3364 C  CB   . VAL   B 1 80  ? 65.611  68.427  34.859  1   36.88 ? 102 VAL   B CB   1 
ATOM   3365 C  CG1  . VAL   B 1 80  ? 65.401  67.306  33.83   1   37.27 ? 102 VAL   B CG1  1 
ATOM   3366 C  CG2  . VAL   B 1 80  ? 64.446  68.479  35.851  1   37.29 ? 102 VAL   B CG2  1 
ATOM   3367 N  N    . VAL   B 1 81  ? 68.791  68.865  34.042  1   34.91 ? 103 VAL   B N    1 
ATOM   3368 C  CA   . VAL   B 1 81  ? 69.974  68.654  33.204  1   34.95 ? 103 VAL   B CA   1 
ATOM   3369 C  C    . VAL   B 1 81  ? 71.081  67.924  34.017  1   35    ? 103 VAL   B C    1 
ATOM   3370 O  O    . VAL   B 1 81  ? 71.614  66.913  33.56   1   35.33 ? 103 VAL   B O    1 
ATOM   3371 C  CB   . VAL   B 1 81  ? 70.488  69.987  32.597  1   35.61 ? 103 VAL   B CB   1 
ATOM   3372 C  CG1  . VAL   B 1 81  ? 71.899  69.849  32.035  1   36.43 ? 103 VAL   B CG1  1 
ATOM   3373 C  CG2  . VAL   B 1 81  ? 69.55   70.495  31.521  1   36.17 ? 103 VAL   B CG2  1 
ATOM   3374 N  N    . LEU   B 1 82  ? 71.365  68.394  35.243  1   34.11 ? 104 LEU   B N    1 
ATOM   3375 C  CA   . LEU   B 1 82  ? 72.375  67.774  36.097  1   33.22 ? 104 LEU   B CA   1 
ATOM   3376 C  C    . LEU   B 1 82  ? 71.969  66.355  36.48   1   32.17 ? 104 LEU   B C    1 
ATOM   3377 O  O    . LEU   B 1 82  ? 72.807  65.46   36.497  1   32.23 ? 104 LEU   B O    1 
ATOM   3378 C  CB   . LEU   B 1 82  ? 72.612  68.614  37.366  1   33.35 ? 104 LEU   B CB   1 
ATOM   3379 C  CG   . LEU   B 1 82  ? 73.124  70.04   37.169  1   34.51 ? 104 LEU   B CG   1 
ATOM   3380 C  CD1  . LEU   B 1 82  ? 73.286  70.731  38.512  1   34.9  ? 104 LEU   B CD1  1 
ATOM   3381 C  CD2  . LEU   B 1 82  ? 74.442  70.048  36.447  1   34.62 ? 104 LEU   B CD2  1 
ATOM   3382 N  N    . ILE   B 1 83  ? 70.692  66.142  36.797  1   31.29 ? 105 ILE   B N    1 
ATOM   3383 C  CA   . ILE   B 1 83  ? 70.208  64.803  37.156  1   30.79 ? 105 ILE   B CA   1 
ATOM   3384 C  C    . ILE   B 1 83  ? 70.339  63.857  35.954  1   31.14 ? 105 ILE   B C    1 
ATOM   3385 O  O    . ILE   B 1 83  ? 70.759  62.717  36.132  1   31.63 ? 105 ILE   B O    1 
ATOM   3386 C  CB   . ILE   B 1 83  ? 68.76   64.842  37.687  1   30.32 ? 105 ILE   B CB   1 
ATOM   3387 C  CG1  . ILE   B 1 83  ? 68.668  65.636  39.003  1   30.95 ? 105 ILE   B CG1  1 
ATOM   3388 C  CG2  . ILE   B 1 83  ? 68.174  63.427  37.839  1   29.79 ? 105 ILE   B CG2  1 
ATOM   3389 C  CD1  . ILE   B 1 83  ? 67.181  65.938  39.431  1   31.29 ? 105 ILE   B CD1  1 
ATOM   3390 N  N    . LEU   B 1 84  ? 70.001  64.332  34.74   1   30.72 ? 106 LEU   B N    1 
ATOM   3391 C  CA   . LEU   B 1 84  ? 70.106  63.525  33.521  1   30.87 ? 106 LEU   B CA   1 
ATOM   3392 C  C    . LEU   B 1 84  ? 71.573  63.176  33.19   1   30.56 ? 106 LEU   B C    1 
ATOM   3393 O  O    . LEU   B 1 84  ? 71.832  62.06   32.739  1   30.86 ? 106 LEU   B O    1 
ATOM   3394 C  CB   . LEU   B 1 84  ? 69.408  64.217  32.321  1   30.67 ? 106 LEU   B CB   1 
ATOM   3395 C  CG   . LEU   B 1 84  ? 67.873  64.131  32.315  1   30.44 ? 106 LEU   B CG   1 
ATOM   3396 C  CD1  . LEU   B 1 84  ? 67.274  65.044  31.264  1   29.58 ? 106 LEU   B CD1  1 
ATOM   3397 C  CD2  . LEU   B 1 84  ? 67.4    62.691  32.143  1   31.01 ? 106 LEU   B CD2  1 
ATOM   3398 N  N    . LYS   B 1 85  ? 72.532  64.097  33.436  1   29.41 ? 107 LYS   B N    1 
ATOM   3399 C  CA   . LYS   B 1 85  ? 73.944  63.788  33.205  1   29.18 ? 107 LYS   B CA   1 
ATOM   3400 C  C    . LYS   B 1 85  ? 74.406  62.692  34.185  1   28.88 ? 107 LYS   B C    1 
ATOM   3401 O  O    . LYS   B 1 85  ? 75.178  61.824  33.81   1   29.01 ? 107 LYS   B O    1 
ATOM   3402 C  CB   . LYS   B 1 85  ? 74.821  65.037  33.368  1   31.28 ? 107 LYS   B CB   1 
ATOM   3403 C  CG   . LYS   B 1 85  ? 74.64   66.062  32.265  1   35.56 ? 107 LYS   B CG   1 
ATOM   3404 C  CD   . LYS   B 1 85  ? 75.387  67.351  32.572  1   40.08 ? 107 LYS   B CD   1 
ATOM   3405 C  CE   . LYS   B 1 85  ? 75.785  68.081  31.314  1   44.69 ? 107 LYS   B CE   1 
ATOM   3406 N  NZ   . LYS   B 1 85  ? 76.596  69.299  31.619  1   47.83 ? 107 LYS   B NZ   1 
ATOM   3407 N  N    . LEU   B 1 86  ? 73.905  62.731  35.429  1   28.53 ? 108 LEU   B N    1 
ATOM   3408 C  CA   . LEU   B 1 86  ? 74.195  61.732  36.438  1   28.66 ? 108 LEU   B CA   1 
ATOM   3409 C  C    . LEU   B 1 86  ? 73.62   60.372  36.029  1   28.7  ? 108 LEU   B C    1 
ATOM   3410 O  O    . LEU   B 1 86  ? 74.278  59.35   36.199  1   29.51 ? 108 LEU   B O    1 
ATOM   3411 C  CB   . LEU   B 1 86  ? 73.628  62.172  37.792  1   27.82 ? 108 LEU   B CB   1 
ATOM   3412 C  CG   . LEU   B 1 86  ? 74.041  61.316  38.994  1   27.99 ? 108 LEU   B CG   1 
ATOM   3413 C  CD1  . LEU   B 1 86  ? 75.372  61.811  39.573  1   28.36 ? 108 LEU   B CD1  1 
ATOM   3414 C  CD2  . LEU   B 1 86  ? 72.948  61.344  40.076  1   27.71 ? 108 LEU   B CD2  1 
ATOM   3415 N  N    . LEU   B 1 87  ? 72.412  60.357  35.475  1   28.19 ? 109 LEU   B N    1 
ATOM   3416 C  CA   . LEU   B 1 87  ? 71.758  59.119  35.016  1   27.84 ? 109 LEU   B CA   1 
ATOM   3417 C  C    . LEU   B 1 87  ? 72.459  58.503  33.83   1   27.58 ? 109 LEU   B C    1 
ATOM   3418 O  O    . LEU   B 1 87  ? 72.533  57.274  33.725  1   27.88 ? 109 LEU   B O    1 
ATOM   3419 C  CB   . LEU   B 1 87  ? 70.263  59.332  34.724  1   27.67 ? 109 LEU   B CB   1 
ATOM   3420 C  CG   . LEU   B 1 87  ? 69.408  59.713  35.953  1   28.42 ? 109 LEU   B CG   1 
ATOM   3421 C  CD1  . LEU   B 1 87  ? 67.935  59.868  35.572  1   29.09 ? 109 LEU   B CD1  1 
ATOM   3422 C  CD2  . LEU   B 1 87  ? 69.553  58.704  37.085  1   27.99 ? 109 LEU   B CD2  1 
ATOM   3423 N  N    . VAL   B 1 88  ? 73.036  59.344  32.957  1   26.74 ? 110 VAL   B N    1 
ATOM   3424 C  CA   . VAL   B 1 88  ? 73.825  58.862  31.841  1   27.04 ? 110 VAL   B CA   1 
ATOM   3425 C  C    . VAL   B 1 88  ? 75.086  58.16   32.411  1   27.07 ? 110 VAL   B C    1 
ATOM   3426 O  O    . VAL   B 1 88  ? 75.415  57.076  31.953  1   27.71 ? 110 VAL   B O    1 
ATOM   3427 C  CB   . VAL   B 1 88  ? 74.154  60.002  30.835  1   28.15 ? 110 VAL   B CB   1 
ATOM   3428 C  CG1  . VAL   B 1 88  ? 75.294  59.605  29.893  1   29.01 ? 110 VAL   B CG1  1 
ATOM   3429 C  CG2  . VAL   B 1 88  ? 72.917  60.399  30.033  1   28.59 ? 110 VAL   B CG2  1 
ATOM   3430 N  N    . ASP   B 1 89  ? 75.699  58.71   33.486  1   26.63 ? 111 ASP   B N    1 
ATOM   3431 C  CA   . ASP   B 1 89  ? 76.879  58.127  34.15   1   27.21 ? 111 ASP   B CA   1 
ATOM   3432 C  C    . ASP   B 1 89  ? 76.616  56.852  34.957  1   27.31 ? 111 ASP   B C    1 
ATOM   3433 O  O    . ASP   B 1 89  ? 77.559  56.185  35.372  1   27.9  ? 111 ASP   B O    1 
ATOM   3434 C  CB   . ASP   B 1 89  ? 77.586  59.16   35.036  1   30.46 ? 111 ASP   B CB   1 
ATOM   3435 C  CG   . ASP   B 1 89  ? 78.37   60.209  34.273  1   38.15 ? 111 ASP   B CG   1 
ATOM   3436 O  OD1  . ASP   B 1 89  ? 78.514  60.07   33.025  1   39.48 ? 111 ASP   B OD1  1 
ATOM   3437 O  OD2  . ASP   B 1 89  ? 78.842  61.168  34.912  1   42.87 ? 111 ASP   B OD2  1 
ATOM   3438 N  N    . GLN   B 1 90  ? 75.349  56.518  35.21   1   26.76 ? 112 GLN   B N    1 
ATOM   3439 C  CA   . GLN   B 1 90  ? 75.005  55.272  35.89   1   26.09 ? 112 GLN   B CA   1 
ATOM   3440 C  C    . GLN   B 1 90  ? 75.123  54.075  34.953  1   26.45 ? 112 GLN   B C    1 
ATOM   3441 O  O    . GLN   B 1 90  ? 75.172  52.939  35.442  1   27.28 ? 112 GLN   B O    1 
ATOM   3442 C  CB   . GLN   B 1 90  ? 73.605  55.331  36.521  1   25.95 ? 112 GLN   B CB   1 
ATOM   3443 C  CG   . GLN   B 1 90  ? 73.57   56.304  37.685  1   27.34 ? 112 GLN   B CG   1 
ATOM   3444 C  CD   . GLN   B 1 90  ? 72.274  56.349  38.433  1   28.21 ? 112 GLN   B CD   1 
ATOM   3445 O  OE1  . GLN   B 1 90  ? 71.339  55.575  38.18   1   29.72 ? 112 GLN   B OE1  1 
ATOM   3446 N  NE2  . GLN   B 1 90  ? 72.207  57.249  39.389  1   27.23 ? 112 GLN   B NE2  1 
ATOM   3447 N  N    . VAL   B 1 91  ? 75.156  54.302  33.617  1   25.6  ? 113 VAL   B N    1 
ATOM   3448 C  CA   . VAL   B 1 91  ? 75.271  53.193  32.67   1   25.56 ? 113 VAL   B CA   1 
ATOM   3449 C  C    . VAL   B 1 91  ? 76.644  52.486  32.809  1   24.83 ? 113 VAL   B C    1 
ATOM   3450 O  O    . VAL   B 1 91  ? 76.644  51.277  33.014  1   25.19 ? 113 VAL   B O    1 
ATOM   3451 C  CB   . VAL   B 1 91  ? 74.901  53.577  31.211  1   25.63 ? 113 VAL   B CB   1 
ATOM   3452 C  CG1  . VAL   B 1 91  ? 75.163  52.414  30.252  1   25.58 ? 113 VAL   B CG1  1 
ATOM   3453 C  CG2  . VAL   B 1 91  ? 73.444  54.016  31.125  1   25.79 ? 113 VAL   B CG2  1 
ATOM   3454 N  N    . PRO   B 1 92  ? 77.803  53.19   32.794  1   23.59 ? 114 PRO   B N    1 
ATOM   3455 C  CA   . PRO   B 1 92  ? 79.082  52.477  32.964  1   23.05 ? 114 PRO   B CA   1 
ATOM   3456 C  C    . PRO   B 1 92  ? 79.191  51.665  34.246  1   23.13 ? 114 PRO   B C    1 
ATOM   3457 O  O    . PRO   B 1 92  ? 79.972  50.732  34.282  1   22.8  ? 114 PRO   B O    1 
ATOM   3458 C  CB   . PRO   B 1 92  ? 80.131  53.596  32.91   1   23.25 ? 114 PRO   B CB   1 
ATOM   3459 C  CG   . PRO   B 1 92  ? 79.461  54.688  32.082  1   23.62 ? 114 PRO   B CG   1 
ATOM   3460 C  CD   . PRO   B 1 92  ? 78.023  54.63   32.524  1   22.54 ? 114 PRO   B CD   1 
ATOM   3461 N  N    . ILE   B 1 93  ? 78.437  52.017  35.294  1   24.25 ? 115 ILE   B N    1 
ATOM   3462 C  CA   . ILE   B 1 93  ? 78.466  51.284  36.565  1   24.98 ? 115 ILE   B CA   1 
ATOM   3463 C  C    . ILE   B 1 93  ? 77.852  49.89   36.322  1   25.3  ? 115 ILE   B C    1 
ATOM   3464 O  O    . ILE   B 1 93  ? 78.451  48.869  36.711  1   25.33 ? 115 ILE   B O    1 
ATOM   3465 C  CB   . ILE   B 1 93  ? 77.714  52.039  37.706  1   24.82 ? 115 ILE   B CB   1 
ATOM   3466 C  CG1  . ILE   B 1 93  ? 78.446  53.322  38.129  1   25.37 ? 115 ILE   B CG1  1 
ATOM   3467 C  CG2  . ILE   B 1 93  ? 77.505  51.124  38.932  1   24.83 ? 115 ILE   B CG2  1 
ATOM   3468 C  CD1  . ILE   B 1 93  ? 77.652  54.276  39.032  1   24.37 ? 115 ILE   B CD1  1 
ATOM   3469 N  N    . LEU   B 1 94  ? 76.649  49.848  35.696  1   24.82 ? 116 LEU   B N    1 
ATOM   3470 C  CA   . LEU   B 1 94  ? 75.988  48.558  35.415  1   24.85 ? 116 LEU   B CA   1 
ATOM   3471 C  C    . LEU   B 1 94  ? 76.775  47.719  34.379  1   24.35 ? 116 LEU   B C    1 
ATOM   3472 O  O    . LEU   B 1 94  ? 76.797  46.505  34.491  1   24.85 ? 116 LEU   B O    1 
ATOM   3473 C  CB   . LEU   B 1 94  ? 74.503  48.722  35.025  1   25.01 ? 116 LEU   B CB   1 
ATOM   3474 C  CG   . LEU   B 1 94  ? 73.648  47.425  35.029  1   26.18 ? 116 LEU   B CG   1 
ATOM   3475 C  CD1  . LEU   B 1 94  ? 73.8    46.609  36.323  1   25.78 ? 116 LEU   B CD1  1 
ATOM   3476 C  CD2  . LEU   B 1 94  ? 72.208  47.724  34.759  1   27.13 ? 116 LEU   B CD2  1 
ATOM   3477 N  N    . GLU   B 1 95  ? 77.496  48.379  33.451  1   23.13 ? 117 GLU   B N    1 
ATOM   3478 C  CA   . GLU   B 1 95  ? 78.371  47.74   32.461  1   23.18 ? 117 GLU   B CA   1 
ATOM   3479 C  C    . GLU   B 1 95  ? 79.542  46.957  33.066  1   23.35 ? 117 GLU   B C    1 
ATOM   3480 O  O    . GLU   B 1 95  ? 80.138  46.159  32.37   1   22.97 ? 117 GLU   B O    1 
ATOM   3481 C  CB   . GLU   B 1 95  ? 78.883  48.737  31.419  1   23.41 ? 117 GLU   B CB   1 
ATOM   3482 C  CG   . GLU   B 1 95  ? 77.776  49.228  30.511  1   25.09 ? 117 GLU   B CG   1 
ATOM   3483 C  CD   . GLU   B 1 95  ? 78.238  50.234  29.473  1   32.32 ? 117 GLU   B CD   1 
ATOM   3484 O  OE1  . GLU   B 1 95  ? 79.063  51.114  29.808  1   36.4  ? 117 GLU   B OE1  1 
ATOM   3485 O  OE2  . GLU   B 1 95  ? 77.753  50.16   28.322  1   32.91 ? 117 GLU   B OE2  1 
ATOM   3486 N  N    . THR   B 1 96  ? 79.84   47.151  34.358  1   24.46 ? 118 THR   B N    1 
ATOM   3487 C  CA   . THR   B 1 96  ? 80.869  46.368  35.078  1   25.35 ? 118 THR   B CA   1 
ATOM   3488 C  C    . THR   B 1 96  ? 80.381  44.913  35.367  1   26.66 ? 118 THR   B C    1 
ATOM   3489 O  O    . THR   B 1 96  ? 81.185  44.053  35.751  1   27.74 ? 118 THR   B O    1 
ATOM   3490 C  CB   . THR   B 1 96  ? 81.351  47.091  36.33   1   26.02 ? 118 THR   B CB   1 
ATOM   3491 O  OG1  . THR   B 1 96  ? 80.304  47.195  37.299  1   28.54 ? 118 THR   B OG1  1 
ATOM   3492 C  CG2  . THR   B 1 96  ? 81.908  48.455  36.037  1   25.95 ? 118 THR   B CG2  1 
ATOM   3493 N  N    . MET   B 1 97  ? 79.076  44.631  35.15   1   25.79 ? 119 MET   B N    1 
ATOM   3494 C  CA   . MET   B 1 97  ? 78.501  43.302  35.267  1   25.42 ? 119 MET   B CA   1 
ATOM   3495 C  C    . MET   B 1 97  ? 78.765  42.612  33.955  1   24.13 ? 119 MET   B C    1 
ATOM   3496 O  O    . MET   B 1 97  ? 78.459  43.171  32.906  1   23.63 ? 119 MET   B O    1 
ATOM   3497 C  CB   . MET   B 1 97  ? 76.974  43.385  35.51   1   26.17 ? 119 MET   B CB   1 
ATOM   3498 C  CG   . MET   B 1 97  ? 76.262  42.031  35.38   1   26.71 ? 119 MET   B CG   1 
ATOM   3499 S  SD   . MET   B 1 97  ? 74.539  42.061  35.865  1   29.34 ? 119 MET   B SD   1 
ATOM   3500 C  CE   . MET   B 1 97  ? 73.818  43.201  34.623  1   24.59 ? 119 MET   B CE   1 
ATOM   3501 N  N    . THR   B 1 98  ? 79.316  41.4    33.997  1   24.05 ? 120 THR   B N    1 
ATOM   3502 C  CA   . THR   B 1 98  ? 79.611  40.664  32.769  1   24.49 ? 120 THR   B CA   1 
ATOM   3503 C  C    . THR   B 1 98  ? 78.356  39.997  32.184  1   24.97 ? 120 THR   B C    1 
ATOM   3504 O  O    . THR   B 1 98  ? 77.436  39.604  32.921  1   24.81 ? 120 THR   B O    1 
ATOM   3505 C  CB   . THR   B 1 98  ? 80.662  39.609  33.025  1   25.73 ? 120 THR   B CB   1 
ATOM   3506 O  OG1  . THR   B 1 98  ? 80.107  38.649  33.934  1   27.31 ? 120 THR   B OG1  1 
ATOM   3507 C  CG2  . THR   B 1 98  ? 81.979  40.205  33.551  1   25.9  ? 120 THR   B CG2  1 
ATOM   3508 N  N    . PRO   B 1 99  ? 78.337  39.821  30.855  1   25.26 ? 121 PRO   B N    1 
ATOM   3509 C  CA   . PRO   B 1 99  ? 77.193  39.129  30.223  1   26.4  ? 121 PRO   B CA   1 
ATOM   3510 C  C    . PRO   B 1 99  ? 76.876  37.75   30.826  1   27.57 ? 121 PRO   B C    1 
ATOM   3511 O  O    . PRO   B 1 99  ? 75.699  37.425  30.955  1   27.56 ? 121 PRO   B O    1 
ATOM   3512 C  CB   . PRO   B 1 99  ? 77.615  39.016  28.751  1   26.62 ? 121 PRO   B CB   1 
ATOM   3513 C  CG   . PRO   B 1 99  ? 78.6    40.137  28.558  1   26.52 ? 121 PRO   B CG   1 
ATOM   3514 C  CD   . PRO   B 1 99  ? 79.325  40.282  29.855  1   24.6  ? 121 PRO   B CD   1 
ATOM   3515 N  N    . LEU   B 1 100 ? 77.91   36.962  31.22   1   27.99 ? 122 LEU   B N    1 
ATOM   3516 C  CA   . LEU   B 1 100 ? 77.719  35.637  31.809  1   28.69 ? 122 LEU   B CA   1 
ATOM   3517 C  C    . LEU   B 1 100 ? 77.089  35.67   33.168  1   29.78 ? 122 LEU   B C    1 
ATOM   3518 O  O    . LEU   B 1 100 ? 76.342  34.741  33.513  1   30.72 ? 122 LEU   B O    1 
ATOM   3519 C  CB   . LEU   B 1 100 ? 79.019  34.825  31.836  1   29.29 ? 122 LEU   B CB   1 
ATOM   3520 C  CG   . LEU   B 1 100 ? 79.397  34.204  30.484  1   31.58 ? 122 LEU   B CG   1 
ATOM   3521 C  CD1  . LEU   B 1 100 ? 80.783  33.635  30.518  1   32.07 ? 122 LEU   B CD1  1 
ATOM   3522 C  CD2  . LEU   B 1 100 ? 78.376  33.16   30.052  1   32.59 ? 122 LEU   B CD2  1 
ATOM   3523 N  N    . ASP   B 1 101 ? 77.37   36.723  33.969  1   29.13 ? 123 ASP   B N    1 
ATOM   3524 C  CA   . ASP   B 1 101 ? 76.753  36.84   35.288  1   29.1  ? 123 ASP   B CA   1 
ATOM   3525 C  C    . ASP   B 1 101 ? 75.294  37.246  35.148  1   28.54 ? 123 ASP   B C    1 
ATOM   3526 O  O    . ASP   B 1 101 ? 74.435  36.707  35.858  1   28.66 ? 123 ASP   B O    1 
ATOM   3527 C  CB   . ASP   B 1 101 ? 77.524  37.824  36.199  1   31.15 ? 123 ASP   B CB   1 
ATOM   3528 C  CG   . ASP   B 1 101 ? 78.826  37.25   36.771  1   36.62 ? 123 ASP   B CG   1 
ATOM   3529 O  OD1  . ASP   B 1 101 ? 79.044  36.038  36.648  1   36.61 ? 123 ASP   B OD1  1 
ATOM   3530 O  OD2  . ASP   B 1 101 ? 79.619  38.023  37.348  1   40.01 ? 123 ASP   B OD2  1 
ATOM   3531 N  N    . PHE   B 1 102 ? 75.007  38.181  34.233  1   27.88 ? 124 PHE   B N    1 
ATOM   3532 C  CA   . PHE   B 1 102 ? 73.638  38.6    33.944  1   28.52 ? 124 PHE   B CA   1 
ATOM   3533 C  C    . PHE   B 1 102 ? 72.82   37.407  33.419  1   29.32 ? 124 PHE   B C    1 
ATOM   3534 O  O    . PHE   B 1 102 ? 71.663  37.283  33.775  1   29.83 ? 124 PHE   B O    1 
ATOM   3535 C  CB   . PHE   B 1 102 ? 73.604  39.735  32.917  1   28.12 ? 124 PHE   B CB   1 
ATOM   3536 C  CG   . PHE   B 1 102 ? 72.203  40.232  32.612  1   28.84 ? 124 PHE   B CG   1 
ATOM   3537 C  CD1  . PHE   B 1 102 ? 71.38   40.695  33.622  1   29.78 ? 124 PHE   B CD1  1 
ATOM   3538 C  CD2  . PHE   B 1 102 ? 71.73   40.266  31.311  1   29.54 ? 124 PHE   B CD2  1 
ATOM   3539 C  CE1  . PHE   B 1 102 ? 70.109  41.171  33.341  1   30.82 ? 124 PHE   B CE1  1 
ATOM   3540 C  CE2  . PHE   B 1 102 ? 70.452  40.726  31.031  1   30.07 ? 124 PHE   B CE2  1 
ATOM   3541 C  CZ   . PHE   B 1 102 ? 69.655  41.182  32.044  1   30.61 ? 124 PHE   B CZ   1 
ATOM   3542 N  N    . MET   B 1 103 ? 73.443  36.497  32.648  1   29.58 ? 125 MET   B N    1 
ATOM   3543 C  CA   . MET   B 1 103 ? 72.791  35.285  32.131  1   30.63 ? 125 MET   B CA   1 
ATOM   3544 C  C    . MET   B 1 103 ? 72.324  34.379  33.268  1   31.79 ? 125 MET   B C    1 
ATOM   3545 O  O    . MET   B 1 103 ? 71.292  33.719  33.131  1   32.82 ? 125 MET   B O    1 
ATOM   3546 C  CB   . MET   B 1 103 ? 73.744  34.498  31.204  1   30.94 ? 125 MET   B CB   1 
ATOM   3547 C  CG   . MET   B 1 103 ? 73.02   33.707  30.115  1   33.71 ? 125 MET   B CG   1 
ATOM   3548 S  SD   . MET   B 1 103 ? 74.168  33.11   28.859  1   39.53 ? 125 MET   B SD   1 
ATOM   3549 C  CE   . MET   B 1 103 ? 73.745  34.094  27.505  1   37.72 ? 125 MET   B CE   1 
ATOM   3550 N  N    . ASP   B 1 104 ? 73.057  34.355  34.407  1   31.41 ? 126 ASP   B N    1 
ATOM   3551 C  CA   . ASP   B 1 104 ? 72.692  33.5    35.539  1   31.06 ? 126 ASP   B CA   1 
ATOM   3552 C  C    . ASP   B 1 104 ? 71.502  34.007  36.351  1   30.62 ? 126 ASP   B C    1 
ATOM   3553 O  O    . ASP   B 1 104 ? 71.007  33.255  37.186  1   30.8  ? 126 ASP   B O    1 
ATOM   3554 C  CB   . ASP   B 1 104 ? 73.891  33.22   36.452  1   33.18 ? 126 ASP   B CB   1 
ATOM   3555 C  CG   . ASP   B 1 104 ? 74.936  32.291  35.866  1   38.81 ? 126 ASP   B CG   1 
ATOM   3556 O  OD1  . ASP   B 1 104 ? 74.656  31.652  34.834  1   40.15 ? 126 ASP   B OD1  1 
ATOM   3557 O  OD2  . ASP   B 1 104 ? 76.036  32.205  36.437  1   42.17 ? 126 ASP   B OD2  1 
ATOM   3558 N  N    . PHE   B 1 105 ? 70.999  35.244  36.107  1   30.2  ? 127 PHE   B N    1 
ATOM   3559 C  CA   . PHE   B 1 105 ? 69.792  35.699  36.813  1   29.79 ? 127 PHE   B CA   1 
ATOM   3560 C  C    . PHE   B 1 105 ? 68.721  36.315  35.893  1   30.99 ? 127 PHE   B C    1 
ATOM   3561 O  O    . PHE   B 1 105 ? 67.604  36.581  36.356  1   30.85 ? 127 PHE   B O    1 
ATOM   3562 C  CB   . PHE   B 1 105 ? 70.104  36.625  37.98   1   28.87 ? 127 PHE   B CB   1 
ATOM   3563 C  CG   . PHE   B 1 105 ? 70.55   38.026  37.65   1   28.59 ? 127 PHE   B CG   1 
ATOM   3564 C  CD1  . PHE   B 1 105 ? 71.899  38.348  37.596  1   28.7  ? 127 PHE   B CD1  1 
ATOM   3565 C  CD2  . PHE   B 1 105 ? 69.625  39.042  37.47   1   28.77 ? 127 PHE   B CD2  1 
ATOM   3566 C  CE1  . PHE   B 1 105 ? 72.304  39.652  37.317  1   29    ? 127 PHE   B CE1  1 
ATOM   3567 C  CE2  . PHE   B 1 105 ? 70.037  40.335  37.179  1   29.34 ? 127 PHE   B CE2  1 
ATOM   3568 C  CZ   . PHE   B 1 105 ? 71.371  40.634  37.124  1   28.63 ? 127 PHE   B CZ   1 
ATOM   3569 N  N    . ARG   B 1 106 ? 69.05   36.578  34.614  1   31.69 ? 128 ARG   B N    1 
ATOM   3570 C  CA   . ARG   B 1 106 ? 68.082  37.218  33.711  1   33.18 ? 128 ARG   B CA   1 
ATOM   3571 C  C    . ARG   B 1 106 ? 66.821  36.378  33.505  1   34.27 ? 128 ARG   B C    1 
ATOM   3572 O  O    . ARG   B 1 106 ? 65.767  36.958  33.288  1   33.8  ? 128 ARG   B O    1 
ATOM   3573 C  CB   . ARG   B 1 106 ? 68.706  37.592  32.358  1   34.52 ? 128 ARG   B CB   1 
ATOM   3574 C  CG   . ARG   B 1 106 ? 69.21   36.38   31.601  1   38.05 ? 128 ARG   B CG   1 
ATOM   3575 C  CD   . ARG   B 1 106 ? 70.129  36.738  30.456  1   40.7  ? 128 ARG   B CD   1 
ATOM   3576 N  NE   . ARG   B 1 106 ? 69.939  35.775  29.377  1   42.91 ? 128 ARG   B NE   1 
ATOM   3577 C  CZ   . ARG   B 1 106 ? 70.629  35.756  28.249  1   43.36 ? 128 ARG   B CZ   1 
ATOM   3578 N  NH1  . ARG   B 1 106 ? 71.591  36.649  28.035  1   41.59 ? 128 ARG   B NH1  1 
ATOM   3579 N  NH2  . ARG   B 1 106 ? 70.346  34.864  27.31   1   42.93 ? 128 ARG   B NH2  1 
ATOM   3580 N  N    . LYS   B 1 107 ? 66.908  35.039  33.648  1   35.6  ? 129 LYS   B N    1 
ATOM   3581 C  CA   . LYS   B 1 107 ? 65.748  34.151  33.494  1   37.45 ? 129 LYS   B CA   1 
ATOM   3582 C  C    . LYS   B 1 107 ? 64.67   34.392  34.538  1   38.22 ? 129 LYS   B C    1 
ATOM   3583 O  O    . LYS   B 1 107 ? 63.504  34.108  34.271  1   39.63 ? 129 LYS   B O    1 
ATOM   3584 C  CB   . LYS   B 1 107 ? 66.163  32.674  33.488  1   40.4  ? 129 LYS   B CB   1 
ATOM   3585 C  CG   . LYS   B 1 107 ? 66.449  32.147  32.084  1   45.64 ? 129 LYS   B CG   1 
ATOM   3586 N  N    . TYR   B 1 108 ? 65.037  34.909  35.721  1   37.37 ? 130 TYR   B N    1 
ATOM   3587 C  CA   . TYR   B 1 108 ? 64.062  35.234  36.775  1   37.2  ? 130 TYR   B CA   1 
ATOM   3588 C  C    . TYR   B 1 108 ? 63.291  36.505  36.482  1   37.87 ? 130 TYR   B C    1 
ATOM   3589 O  O    . TYR   B 1 108 ? 62.269  36.733  37.121  1   38.33 ? 130 TYR   B O    1 
ATOM   3590 C  CB   . TYR   B 1 108 ? 64.747  35.427  38.143  1   36.78 ? 130 TYR   B CB   1 
ATOM   3591 C  CG   . TYR   B 1 108 ? 65.542  34.23   38.587  1   36.85 ? 130 TYR   B CG   1 
ATOM   3592 C  CD1  . TYR   B 1 108 ? 64.914  33.104  39.102  1   37.31 ? 130 TYR   B CD1  1 
ATOM   3593 C  CD2  . TYR   B 1 108 ? 66.926  34.237  38.54   1   37.1  ? 130 TYR   B CD2  1 
ATOM   3594 C  CE1  . TYR   B 1 108 ? 65.643  31.979  39.47   1   37.84 ? 130 TYR   B CE1  1 
ATOM   3595 C  CE2  . TYR   B 1 108 ? 67.667  33.131  38.931  1   37.97 ? 130 TYR   B CE2  1 
ATOM   3596 C  CZ   . TYR   B 1 108 ? 67.022  32.006  39.406  1   38.68 ? 130 TYR   B CZ   1 
ATOM   3597 O  OH   . TYR   B 1 108 ? 67.76   30.917  39.775  1   39.99 ? 130 TYR   B OH   1 
ATOM   3598 N  N    . LEU   B 1 109 ? 63.825  37.384  35.621  1   38.28 ? 131 LEU   B N    1 
ATOM   3599 C  CA   . LEU   B 1 109 ? 63.221  38.661  35.271  1   39.76 ? 131 LEU   B CA   1 
ATOM   3600 C  C    . LEU   B 1 109 ? 61.897  38.394  34.583  1   42.33 ? 131 LEU   B C    1 
ATOM   3601 O  O    . LEU   B 1 109 ? 60.923  39.037  34.93   1   42.84 ? 131 LEU   B O    1 
ATOM   3602 C  CB   . LEU   B 1 109 ? 64.174  39.482  34.382  1   39.28 ? 131 LEU   B CB   1 
ATOM   3603 C  CG   . LEU   B 1 109 ? 65.371  40.248  35.032  1   40.5  ? 131 LEU   B CG   1 
ATOM   3604 C  CD1  . LEU   B 1 109 ? 65.89   39.697  36.332  1   40.45 ? 131 LEU   B CD1  1 
ATOM   3605 C  CD2  . LEU   B 1 109 ? 66.427  40.668  34.012  1   40.84 ? 131 LEU   B CD2  1 
ATOM   3606 N  N    . ALA   B 1 110 ? 61.867  37.395  33.669  1   43.96 ? 132 ALA   B N    1 
ATOM   3607 C  CA   . ALA   B 1 110 ? 60.733  36.787  32.959  1   46.29 ? 132 ALA   B CA   1 
ATOM   3608 C  C    . ALA   B 1 110 ? 59.598  37.742  32.609  1   47.66 ? 132 ALA   B C    1 
ATOM   3609 O  O    . ALA   B 1 110 ? 59.66   38.278  31.489  1   49.72 ? 132 ALA   B O    1 
ATOM   3610 C  CB   . ALA   B 1 110 ? 60.214  35.573  33.733  1   47.28 ? 132 ALA   B CB   1 
ATOM   3611 N  N    . PRO   B 1 111 ? 58.556  38.011  33.458  1   45.72 ? 133 PRO   B N    1 
ATOM   3612 C  CA   . PRO   B 1 111 ? 57.512  38.956  33.003  1   44.32 ? 133 PRO   B CA   1 
ATOM   3613 C  C    . PRO   B 1 111 ? 57.94   40.433  33.056  1   42.71 ? 133 PRO   B C    1 
ATOM   3614 O  O    . PRO   B 1 111 ? 57.301  41.275  32.432  1   42.88 ? 133 PRO   B O    1 
ATOM   3615 C  CB   . PRO   B 1 111 ? 56.299  38.638  33.891  1   45.01 ? 133 PRO   B CB   1 
ATOM   3616 C  CG   . PRO   B 1 111 ? 56.834  37.883  35.051  1   45.78 ? 133 PRO   B CG   1 
ATOM   3617 C  CD   . PRO   B 1 111 ? 58.275  37.491  34.814  1   44.46 ? 133 PRO   B CD   1 
ATOM   3618 N  N    . ALA   B 1 112 ? 59.005  40.755  33.815  1   40.98 ? 134 ALA   B N    1 
ATOM   3619 C  CA   . ALA   B 1 112 ? 59.485  42.131  33.938  1   39.49 ? 134 ALA   B CA   1 
ATOM   3620 C  C    . ALA   B 1 112 ? 60.052  42.635  32.637  1   37.58 ? 134 ALA   B C    1 
ATOM   3621 O  O    . ALA   B 1 112 ? 60.702  41.897  31.9    1   37.5  ? 134 ALA   B O    1 
ATOM   3622 C  CB   . ALA   B 1 112 ? 60.538  42.246  35.034  1   39.38 ? 134 ALA   B CB   1 
ATOM   3623 N  N    . SER   B 1 113 ? 59.815  43.909  32.364  1   35.96 ? 135 SER   B N    1 
ATOM   3624 C  CA   . SER   B 1 113 ? 60.319  44.534  31.162  1   35.05 ? 135 SER   B CA   1 
ATOM   3625 C  C    . SER   B 1 113 ? 60.608  45.996  31.437  1   34.61 ? 135 SER   B C    1 
ATOM   3626 O  O    . SER   B 1 113 ? 59.895  46.631  32.21   1   33.94 ? 135 SER   B O    1 
ATOM   3627 C  CB   . SER   B 1 113 ? 59.301  44.398  30.029  1   35.88 ? 135 SER   B CB   1 
ATOM   3628 O  OG   . SER   B 1 113 ? 59.69   45.135  28.886  1   38.6  ? 135 SER   B OG   1 
ATOM   3629 N  N    . GLY   B 1 114 ? 61.609  46.544  30.742  1   34.4  ? 136 GLY   B N    1 
ATOM   3630 C  CA   . GLY   B 1 114 ? 61.917  47.967  30.818  1   34.17 ? 136 GLY   B CA   1 
ATOM   3631 C  C    . GLY   B 1 114 ? 60.746  48.827  30.357  1   34.27 ? 136 GLY   B C    1 
ATOM   3632 O  O    . GLY   B 1 114 ? 60.597  49.979  30.783  1   34.14 ? 136 GLY   B O    1 
ATOM   3633 N  N    . PHE   B 1 115 ? 59.874  48.251  29.496  1   34.12 ? 137 PHE   B N    1 
ATOM   3634 C  CA   . PHE   B 1 115 ? 58.643  48.879  29.005  1   34.26 ? 137 PHE   B CA   1 
ATOM   3635 C  C    . PHE   B 1 115 ? 57.658  49.156  30.183  1   33.66 ? 137 PHE   B C    1 
ATOM   3636 O  O    . PHE   B 1 115 ? 56.827  50.047  30.067  1   33.4  ? 137 PHE   B O    1 
ATOM   3637 C  CB   . PHE   B 1 115 ? 57.96   47.949  27.972  1   34.65 ? 137 PHE   B CB   1 
ATOM   3638 C  CG   . PHE   B 1 115 ? 58.726  47.731  26.685  1   35.9  ? 137 PHE   B CG   1 
ATOM   3639 C  CD1  . PHE   B 1 115 ? 59.629  48.678  26.226  1   36.51 ? 137 PHE   B CD1  1 
ATOM   3640 C  CD2  . PHE   B 1 115 ? 58.465  46.631  25.883  1   37.26 ? 137 PHE   B CD2  1 
ATOM   3641 C  CE1  . PHE   B 1 115 ? 60.294  48.5    25.024  1   37.41 ? 137 PHE   B CE1  1 
ATOM   3642 C  CE2  . PHE   B 1 115 ? 59.133  46.459  24.669  1   37.89 ? 137 PHE   B CE2  1 
ATOM   3643 C  CZ   . PHE   B 1 115 ? 60.039  47.395  24.248  1   37.38 ? 137 PHE   B CZ   1 
ATOM   3644 N  N    . GLN   B 1 116 ? 57.747  48.384  31.285  1   32.95 ? 138 GLN   B N    1 
ATOM   3645 C  CA   . GLN   B 1 116 ? 56.892  48.529  32.46   1   33.51 ? 138 GLN   B CA   1 
ATOM   3646 C  C    . GLN   B 1 116 ? 57.331  49.623  33.45   1   34.8  ? 138 GLN   B C    1 
ATOM   3647 O  O    . GLN   B 1 116 ? 56.779  49.681  34.552  1   35.02 ? 138 GLN   B O    1 
ATOM   3648 C  CB   . GLN   B 1 116 ? 56.717  47.199  33.196  1   33.89 ? 138 GLN   B CB   1 
ATOM   3649 C  CG   . GLN   B 1 116 ? 56.076  46.118  32.351  1   36.18 ? 138 GLN   B CG   1 
ATOM   3650 C  CD   . GLN   B 1 116 ? 56.305  44.737  32.877  1   39.14 ? 138 GLN   B CD   1 
ATOM   3651 O  OE1  . GLN   B 1 116 ? 57.199  44.49   33.689  1   41.78 ? 138 GLN   B OE1  1 
ATOM   3652 N  NE2  . GLN   B 1 116 ? 55.544  43.787  32.386  1   38.49 ? 138 GLN   B NE2  1 
ATOM   3653 N  N    . SER   B 1 117 ? 58.285  50.505  33.064  1   34.93 ? 139 SER   B N    1 
ATOM   3654 C  CA   . SER   B 1 117 ? 58.644  51.614  33.947  1   35.02 ? 139 SER   B CA   1 
ATOM   3655 C  C    . SER   B 1 117 ? 57.649  52.709  33.679  1   35.44 ? 139 SER   B C    1 
ATOM   3656 O  O    . SER   B 1 117 ? 57.774  53.416  32.681  1   35.42 ? 139 SER   B O    1 
ATOM   3657 C  CB   . SER   B 1 117 ? 60.057  52.13   33.686  1   35.62 ? 139 SER   B CB   1 
ATOM   3658 O  OG   . SER   B 1 117 ? 60.267  53.373  34.344  1   36.25 ? 139 SER   B OG   1 
ATOM   3659 N  N    . LEU   B 1 118 ? 56.67   52.869  34.574  1   35.75 ? 140 LEU   B N    1 
ATOM   3660 C  CA   . LEU   B 1 118 ? 55.657  53.902  34.453  1   36.14 ? 140 LEU   B CA   1 
ATOM   3661 C  C    . LEU   B 1 118 ? 56.296  55.289  34.485  1   36.44 ? 140 LEU   B C    1 
ATOM   3662 O  O    . LEU   B 1 118 ? 55.965  56.142  33.659  1   36.9  ? 140 LEU   B O    1 
ATOM   3663 C  CB   . LEU   B 1 118 ? 54.634  53.721  35.598  1   37.03 ? 140 LEU   B CB   1 
ATOM   3664 C  CG   . LEU   B 1 118 ? 53.624  54.862  35.827  1   38.63 ? 140 LEU   B CG   1 
ATOM   3665 C  CD1  . LEU   B 1 118 ? 52.708  55.044  34.586  1   38.84 ? 140 LEU   B CD1  1 
ATOM   3666 C  CD2  . LEU   B 1 118 ? 52.794  54.612  37.101  1   38.77 ? 140 LEU   B CD2  1 
ATOM   3667 N  N    . GLN   B 1 119 ? 57.255  55.504  35.404  1   36.17 ? 141 GLN   B N    1 
ATOM   3668 C  CA   . GLN   B 1 119 ? 57.925  56.796  35.538  1   35.56 ? 141 GLN   B CA   1 
ATOM   3669 C  C    . GLN   B 1 119 ? 58.672  57.216  34.291  1   35    ? 141 GLN   B C    1 
ATOM   3670 O  O    . GLN   B 1 119 ? 58.631  58.397  33.952  1   35.83 ? 141 GLN   B O    1 
ATOM   3671 C  CB   . GLN   B 1 119 ? 58.834  56.833  36.777  1   36.47 ? 141 GLN   B CB   1 
ATOM   3672 C  CG   . GLN   B 1 119 ? 58.04   56.792  38.083  1   38.48 ? 141 GLN   B CG   1 
ATOM   3673 C  CD   . GLN   B 1 119 ? 58.864  57.254  39.264  1   41.91 ? 141 GLN   B CD   1 
ATOM   3674 O  OE1  . GLN   B 1 119 ? 58.551  58.254  39.909  1   43.79 ? 141 GLN   B OE1  1 
ATOM   3675 N  NE2  . GLN   B 1 119 ? 59.945  56.541  39.565  1   40.13 ? 141 GLN   B NE2  1 
ATOM   3676 N  N    . PHE   B 1 120 ? 59.317  56.278  33.576  1   34.22 ? 142 PHE   B N    1 
ATOM   3677 C  CA   . PHE   B 1 120 ? 60.016  56.647  32.339  1   34.03 ? 142 PHE   B CA   1 
ATOM   3678 C  C    . PHE   B 1 120 ? 59.005  57.164  31.286  1   34.16 ? 142 PHE   B C    1 
ATOM   3679 O  O    . PHE   B 1 120 ? 59.246  58.192  30.652  1   34.49 ? 142 PHE   B O    1 
ATOM   3680 C  CB   . PHE   B 1 120 ? 60.897  55.497  31.803  1   33.43 ? 142 PHE   B CB   1 
ATOM   3681 C  CG   . PHE   B 1 120 ? 61.7    55.896  30.582  1   34.1  ? 142 PHE   B CG   1 
ATOM   3682 C  CD1  . PHE   B 1 120 ? 62.866  56.629  30.709  1   34.25 ? 142 PHE   B CD1  1 
ATOM   3683 C  CD2  . PHE   B 1 120 ? 61.283  55.536  29.305  1   34.83 ? 142 PHE   B CD2  1 
ATOM   3684 C  CE1  . PHE   B 1 120 ? 63.594  56.997  29.595  1   35.05 ? 142 PHE   B CE1  1 
ATOM   3685 C  CE2  . PHE   B 1 120 ? 62.022  55.902  28.189  1   35.02 ? 142 PHE   B CE2  1 
ATOM   3686 C  CZ   . PHE   B 1 120 ? 63.17   56.631  28.343  1   34.98 ? 142 PHE   B CZ   1 
ATOM   3687 N  N    . ARG   B 1 121 ? 57.855  56.487  31.154  1   33.99 ? 143 ARG   B N    1 
ATOM   3688 C  CA   . ARG   B 1 121 ? 56.798  56.918  30.228  1   34.49 ? 143 ARG   B CA   1 
ATOM   3689 C  C    . ARG   B 1 121 ? 56.247  58.28   30.637  1   36.17 ? 143 ARG   B C    1 
ATOM   3690 O  O    . ARG   B 1 121 ? 56.099  59.151  29.78   1   36.7  ? 143 ARG   B O    1 
ATOM   3691 C  CB   . ARG   B 1 121 ? 55.664  55.871  30.173  1   33.42 ? 143 ARG   B CB   1 
ATOM   3692 C  CG   . ARG   B 1 121 ? 56.116  54.481  29.664  1   31.86 ? 143 ARG   B CG   1 
ATOM   3693 C  CD   . ARG   B 1 121 ? 56.807  54.586  28.309  1   30.56 ? 143 ARG   B CD   1 
ATOM   3694 N  NE   . ARG   B 1 121 ? 57.184  53.277  27.781  1   31.18 ? 143 ARG   B NE   1 
ATOM   3695 C  CZ   . ARG   B 1 121 ? 58.189  53.079  26.925  1   30.97 ? 143 ARG   B CZ   1 
ATOM   3696 N  NH1  . ARG   B 1 121 ? 58.924  54.103  26.498  1   29.76 ? 143 ARG   B NH1  1 
ATOM   3697 N  NH2  . ARG   B 1 121 ? 58.469  51.859  26.496  1   28.56 ? 143 ARG   B NH2  1 
ATOM   3698 N  N    . LEU   B 1 122 ? 56.013  58.486  31.955  1   36.55 ? 144 LEU   B N    1 
ATOM   3699 C  CA   . LEU   B 1 122 ? 55.527  59.765  32.48   1   37.43 ? 144 LEU   B CA   1 
ATOM   3700 C  C    . LEU   B 1 122 ? 56.497  60.902  32.157  1   37.59 ? 144 LEU   B C    1 
ATOM   3701 O  O    . LEU   B 1 122 ? 56.049  61.977  31.783  1   38.13 ? 144 LEU   B O    1 
ATOM   3702 C  CB   . LEU   B 1 122 ? 55.279  59.683  33.99   1   38.08 ? 144 LEU   B CB   1 
ATOM   3703 C  CG   . LEU   B 1 122 ? 54.121  58.774  34.431  1   39.96 ? 144 LEU   B CG   1 
ATOM   3704 C  CD1  . LEU   B 1 122 ? 54.039  58.714  35.948  1   40.76 ? 144 LEU   B CD1  1 
ATOM   3705 C  CD2  . LEU   B 1 122 ? 52.774  59.271  33.892  1   40.46 ? 144 LEU   B CD2  1 
ATOM   3706 N  N    . ILE   B 1 123 ? 57.826  60.668  32.248  1   36.69 ? 145 ILE   B N    1 
ATOM   3707 C  CA   . ILE   B 1 123 ? 58.814  61.707  31.894  1   35.89 ? 145 ILE   B CA   1 
ATOM   3708 C  C    . ILE   B 1 123 ? 58.705  62.051  30.407  1   35.86 ? 145 ILE   B C    1 
ATOM   3709 O  O    . ILE   B 1 123 ? 58.667  63.224  30.06   1   35.82 ? 145 ILE   B O    1 
ATOM   3710 C  CB   . ILE   B 1 123 ? 60.261  61.249  32.273  1   35.1  ? 145 ILE   B CB   1 
ATOM   3711 C  CG1  . ILE   B 1 123 ? 60.438  61.225  33.789  1   35.27 ? 145 ILE   B CG1  1 
ATOM   3712 C  CG2  . ILE   B 1 123 ? 61.339  62.105  31.591  1   34.61 ? 145 ILE   B CG2  1 
ATOM   3713 C  CD1  . ILE   B 1 123 ? 61.682  60.565  34.246  1   35.61 ? 145 ILE   B CD1  1 
ATOM   3714 N  N    . GLU   B 1 124 ? 58.663  61.027  29.532  1   36.24 ? 146 GLU   B N    1 
ATOM   3715 C  CA   . GLU   B 1 124 ? 58.52   61.205  28.079  1   36.6  ? 146 GLU   B CA   1 
ATOM   3716 C  C    . GLU   B 1 124 ? 57.259  62.011  27.741  1   37.82 ? 146 GLU   B C    1 
ATOM   3717 O  O    . GLU   B 1 124 ? 57.334  62.966  26.96   1   38.11 ? 146 GLU   B O    1 
ATOM   3718 C  CB   . GLU   B 1 124 ? 58.427  59.836  27.373  1   37.29 ? 146 GLU   B CB   1 
ATOM   3719 C  CG   . GLU   B 1 124 ? 59.729  59.066  27.304  1   38.51 ? 146 GLU   B CG   1 
ATOM   3720 C  CD   . GLU   B 1 124 ? 59.604  57.763  26.549  1   39.06 ? 146 GLU   B CD   1 
ATOM   3721 O  OE1  . GLU   B 1 124 ? 58.731  56.942  26.906  1   39.49 ? 146 GLU   B OE1  1 
ATOM   3722 O  OE2  . GLU   B 1 124 ? 60.398  57.547  25.61   1   39.55 ? 146 GLU   B OE2  1 
ATOM   3723 N  N    . ASN   B 1 125 ? 56.097  61.623  28.316  1   38.15 ? 147 ASN   B N    1 
ATOM   3724 C  CA   . ASN   B 1 125 ? 54.836  62.294  28.022  1   39.59 ? 147 ASN   B CA   1 
ATOM   3725 C  C    . ASN   B 1 125 ? 54.782  63.704  28.589  1   41.5  ? 147 ASN   B C    1 
ATOM   3726 O  O    . ASN   B 1 125 ? 54.403  64.625  27.867  1   42.35 ? 147 ASN   B O    1 
ATOM   3727 C  CB   . ASN   B 1 125 ? 53.64   61.466  28.475  1   40.24 ? 147 ASN   B CB   1 
ATOM   3728 C  CG   . ASN   B 1 125 ? 53.517  60.139  27.757  1   42.12 ? 147 ASN   B CG   1 
ATOM   3729 O  OD1  . ASN   B 1 125 ? 54.208  59.875  26.757  1   43.35 ? 147 ASN   B OD1  1 
ATOM   3730 N  ND2  . ASN   B 1 125 ? 52.654  59.268  28.262  1   41.19 ? 147 ASN   B ND2  1 
ATOM   3731 N  N    . LYS   B 1 126 ? 55.231  63.898  29.84   1   41.64 ? 148 LYS   B N    1 
ATOM   3732 C  CA   . LYS   B 1 126 ? 55.243  65.218  30.442  1   41.92 ? 148 LYS   B CA   1 
ATOM   3733 C  C    . LYS   B 1 126 ? 56.178  66.158  29.711  1   43.71 ? 148 LYS   B C    1 
ATOM   3734 O  O    . LYS   B 1 126 ? 55.886  67.338  29.637  1   44.52 ? 148 LYS   B O    1 
ATOM   3735 C  CB   . LYS   B 1 126 ? 55.534  65.142  31.936  1   42.7  ? 148 LYS   B CB   1 
ATOM   3736 C  CG   . LYS   B 1 126 ? 54.396  64.483  32.71   1   44.8  ? 148 LYS   B CG   1 
ATOM   3737 C  CD   . LYS   B 1 126 ? 54.812  64.054  34.107  1   48.55 ? 148 LYS   B CD   1 
ATOM   3738 C  CE   . LYS   B 1 126 ? 53.662  63.447  34.873  1   51.88 ? 148 LYS   B CE   1 
ATOM   3739 N  NZ   . LYS   B 1 126 ? 52.629  64.463  35.2    1   53.74 ? 148 LYS   B NZ   1 
ATOM   3740 N  N    . LEU   B 1 127 ? 57.277  65.646  29.117  1   44.16 ? 149 LEU   B N    1 
ATOM   3741 C  CA   . LEU   B 1 127 ? 58.172  66.49   28.328  1   44.51 ? 149 LEU   B CA   1 
ATOM   3742 C  C    . LEU   B 1 127 ? 57.448  66.829  27.008  1   45.84 ? 149 LEU   B C    1 
ATOM   3743 O  O    . LEU   B 1 127 ? 57.408  67.991  26.604  1   46.01 ? 149 LEU   B O    1 
ATOM   3744 C  CB   . LEU   B 1 127 ? 59.516  65.793  28.074  1   43.84 ? 149 LEU   B CB   1 
ATOM   3745 C  CG   . LEU   B 1 127 ? 60.534  66.601  27.284  1   44.2  ? 149 LEU   B CG   1 
ATOM   3746 C  CD1  . LEU   B 1 127 ? 60.957  67.837  28.044  1   44.29 ? 149 LEU   B CD1  1 
ATOM   3747 C  CD2  . LEU   B 1 127 ? 61.738  65.753  26.917  1   44.24 ? 149 LEU   B CD2  1 
ATOM   3748 N  N    . GLY   B 1 128 ? 56.834  65.827  26.381  1   46.41 ? 150 GLY   B N    1 
ATOM   3749 C  CA   . GLY   B 1 128 ? 56.045  66.054  25.176  1   47.21 ? 150 GLY   B CA   1 
ATOM   3750 C  C    . GLY   B 1 128 ? 56.124  65.045  24.046  1   47.28 ? 150 GLY   B C    1 
ATOM   3751 O  O    . GLY   B 1 128 ? 55.789  65.393  22.915  1   47.51 ? 150 GLY   B O    1 
ATOM   3752 N  N    . VAL   B 1 129 ? 56.561  63.799  24.316  1   46.93 ? 151 VAL   B N    1 
ATOM   3753 C  CA   . VAL   B 1 129 ? 56.636  62.777  23.269  1   46.78 ? 151 VAL   B CA   1 
ATOM   3754 C  C    . VAL   B 1 129 ? 55.21   62.422  22.826  1   47.16 ? 151 VAL   B C    1 
ATOM   3755 O  O    . VAL   B 1 129 ? 54.396  61.988  23.645  1   46.93 ? 151 VAL   B O    1 
ATOM   3756 C  CB   . VAL   B 1 129 ? 57.415  61.517  23.724  1   46.84 ? 151 VAL   B CB   1 
ATOM   3757 C  CG1  . VAL   B 1 129 ? 57.287  60.395  22.7    1   47.18 ? 151 VAL   B CG1  1 
ATOM   3758 C  CG2  . VAL   B 1 129 ? 58.881  61.84   23.976  1   47.08 ? 151 VAL   B CG2  1 
ATOM   3759 N  N    . LEU   B 1 130 ? 54.899  62.634  21.544  1   47.35 ? 152 LEU   B N    1 
ATOM   3760 C  CA   . LEU   B 1 130 ? 53.56   62.328  21.037  1   48.01 ? 152 LEU   B CA   1 
ATOM   3761 C  C    . LEU   B 1 130 ? 53.383  60.817  20.831  1   47.95 ? 152 LEU   B C    1 
ATOM   3762 O  O    . LEU   B 1 130 ? 54.281  60.158  20.317  1   48.01 ? 152 LEU   B O    1 
ATOM   3763 C  CB   . LEU   B 1 130 ? 53.288  63.106  19.738  1   48.41 ? 152 LEU   B CB   1 
ATOM   3764 N  N    . THR   B 1 131 ? 52.24   60.27   21.242  1   47.77 ? 153 THR   B N    1 
ATOM   3765 C  CA   . THR   B 1 131 ? 51.951  58.849  21.092  1   49.12 ? 153 THR   B CA   1 
ATOM   3766 C  C    . THR   B 1 131 ? 52.007  58.367  19.614  1   50.19 ? 153 THR   B C    1 
ATOM   3767 O  O    . THR   B 1 131 ? 52.49   57.256  19.326  1   50.16 ? 153 THR   B O    1 
ATOM   3768 C  CB   . THR   B 1 131 ? 50.602  58.546  21.742  1   51.02 ? 153 THR   B CB   1 
ATOM   3769 O  OG1  . THR   B 1 131 ? 50.636  58.985  23.102  1   52.53 ? 153 THR   B OG1  1 
ATOM   3770 C  CG2  . THR   B 1 131 ? 50.237  57.07   21.682  1   51.19 ? 153 THR   B CG2  1 
ATOM   3771 N  N    . GLU   B 1 132 ? 51.542  59.232  18.685  1   50.28 ? 154 GLU   B N    1 
ATOM   3772 C  CA   . GLU   B 1 132 ? 51.523  58.962  17.25   1   50.73 ? 154 GLU   B CA   1 
ATOM   3773 C  C    . GLU   B 1 132 ? 52.942  58.898  16.661  1   50.49 ? 154 GLU   B C    1 
ATOM   3774 O  O    . GLU   B 1 132 ? 53.16   58.199  15.668  1   50.41 ? 154 GLU   B O    1 
ATOM   3775 C  CB   . GLU   B 1 132 ? 50.668  60.019  16.511  1   52.69 ? 154 GLU   B CB   1 
ATOM   3776 N  N    . GLN   B 1 133 ? 53.908  59.624  17.263  1   49.92 ? 155 GLN   B N    1 
ATOM   3777 C  CA   . GLN   B 1 133 ? 55.285  59.599  16.769  1   49.81 ? 155 GLN   B CA   1 
ATOM   3778 C  C    . GLN   B 1 133 ? 56.122  58.416  17.285  1   48.29 ? 155 GLN   B C    1 
ATOM   3779 O  O    . GLN   B 1 133 ? 57.255  58.248  16.846  1   48.51 ? 155 GLN   B O    1 
ATOM   3780 C  CB   . GLN   B 1 133 ? 56.001  60.928  17.039  1   52.86 ? 155 GLN   B CB   1 
ATOM   3781 C  CG   . GLN   B 1 133 ? 55.462  62.087  16.192  1   59.11 ? 155 GLN   B CG   1 
ATOM   3782 C  CD   . GLN   B 1 133 ? 56.156  62.265  14.857  1   66.31 ? 155 GLN   B CD   1 
ATOM   3783 O  OE1  . GLN   B 1 133 ? 57.363  62.543  14.775  1   68.99 ? 155 GLN   B OE1  1 
ATOM   3784 N  NE2  . GLN   B 1 133 ? 55.399  62.137  13.777  1   67.49 ? 155 GLN   B NE2  1 
ATOM   3785 N  N    . ARG   B 1 134 ? 55.573  57.589  18.175  1   46.96 ? 156 ARG   B N    1 
ATOM   3786 C  CA   . ARG   B 1 134 ? 56.302  56.442  18.713  1   46.17 ? 156 ARG   B CA   1 
ATOM   3787 C  C    . ARG   B 1 134 ? 56.395  55.314  17.696  1   46.42 ? 156 ARG   B C    1 
ATOM   3788 O  O    . ARG   B 1 134 ? 55.452  55.078  16.94   1   46.55 ? 156 ARG   B O    1 
ATOM   3789 C  CB   . ARG   B 1 134 ? 55.629  55.914  19.996  1   45.33 ? 156 ARG   B CB   1 
ATOM   3790 C  CG   . ARG   B 1 134 ? 55.66   56.874  21.185  1   44.63 ? 156 ARG   B CG   1 
ATOM   3791 C  CD   . ARG   B 1 134 ? 54.962  56.257  22.38   1   45.05 ? 156 ARG   B CD   1 
ATOM   3792 N  NE   . ARG   B 1 134 ? 55.043  57.108  23.57   1   45.94 ? 156 ARG   B NE   1 
ATOM   3793 C  CZ   . ARG   B 1 134 ? 56.003  57.022  24.494  1   43.57 ? 156 ARG   B CZ   1 
ATOM   3794 N  NH1  . ARG   B 1 134 ? 56.969  56.121  24.376  1   39.76 ? 156 ARG   B NH1  1 
ATOM   3795 N  NH2  . ARG   B 1 134 ? 56.011  57.852  25.532  1   42.13 ? 156 ARG   B NH2  1 
ATOM   3796 N  N    . VAL   B 1 135 ? 57.527  54.605  17.687  1   45.98 ? 157 VAL   B N    1 
ATOM   3797 C  CA   . VAL   B 1 135 ? 57.705  53.446  16.815  1   46    ? 157 VAL   B CA   1 
ATOM   3798 C  C    . VAL   B 1 135 ? 57.04   52.251  17.494  1   45.36 ? 157 VAL   B C    1 
ATOM   3799 O  O    . VAL   B 1 135 ? 57.31   51.966  18.656  1   45.17 ? 157 VAL   B O    1 
ATOM   3800 C  CB   . VAL   B 1 135 ? 59.183  53.167  16.408  1   47.01 ? 157 VAL   B CB   1 
ATOM   3801 C  CG1  . VAL   B 1 135 ? 60.133  53.408  17.562  1   48.49 ? 157 VAL   B CG1  1 
ATOM   3802 C  CG2  . VAL   B 1 135 ? 59.357  51.751  15.861  1   46.94 ? 157 VAL   B CG2  1 
ATOM   3803 N  N    . ARG   B 1 136 ? 56.129  51.589  16.787  1   45.09 ? 158 ARG   B N    1 
ATOM   3804 C  CA   . ARG   B 1 136 ? 55.403  50.461  17.332  1   45.33 ? 158 ARG   B CA   1 
ATOM   3805 C  C    . ARG   B 1 136 ? 55.519  49.252  16.411  1   45.61 ? 158 ARG   B C    1 
ATOM   3806 O  O    . ARG   B 1 136 ? 55.329  49.384  15.197  1   46.58 ? 158 ARG   B O    1 
ATOM   3807 C  CB   . ARG   B 1 136 ? 53.932  50.854  17.517  1   47    ? 158 ARG   B CB   1 
ATOM   3808 C  CG   . ARG   B 1 136 ? 53.164  49.872  18.363  1   50.31 ? 158 ARG   B CG   1 
ATOM   3809 C  CD   . ARG   B 1 136 ? 51.755  49.622  17.87   1   52.12 ? 158 ARG   B CD   1 
ATOM   3810 N  NE   . ARG   B 1 136 ? 50.823  50.689  18.232  1   53.5  ? 158 ARG   B NE   1 
ATOM   3811 C  CZ   . ARG   B 1 136 ? 49.566  50.489  18.628  1   53.12 ? 158 ARG   B CZ   1 
ATOM   3812 N  NH1  . ARG   B 1 136 ? 49.095  49.255  18.776  1   50.86 ? 158 ARG   B NH1  1 
ATOM   3813 N  NH2  . ARG   B 1 136 ? 48.779  51.519  18.896  1   51.9  ? 158 ARG   B NH2  1 
ATOM   3814 N  N    . TYR   B 1 137 ? 55.877  48.095  16.957  1   44.94 ? 159 TYR   B N    1 
ATOM   3815 C  CA   . TYR   B 1 137 ? 55.973  46.872  16.159  1   45.7  ? 159 TYR   B CA   1 
ATOM   3816 C  C    . TYR   B 1 137 ? 54.771  45.986  16.379  1   48.23 ? 159 TYR   B C    1 
ATOM   3817 O  O    . TYR   B 1 137 ? 54.428  45.222  15.486  1   49.07 ? 159 TYR   B O    1 
ATOM   3818 C  CB   . TYR   B 1 137 ? 57.249  46.062  16.427  1   44.85 ? 159 TYR   B CB   1 
ATOM   3819 C  CG   . TYR   B 1 137 ? 58.539  46.767  16.084  1   44.88 ? 159 TYR   B CG   1 
ATOM   3820 C  CD1  . TYR   B 1 137 ? 58.577  47.768  15.123  1   45.26 ? 159 TYR   B CD1  1 
ATOM   3821 C  CD2  . TYR   B 1 137 ? 59.731  46.418  16.704  1   45.57 ? 159 TYR   B CD2  1 
ATOM   3822 C  CE1  . TYR   B 1 137 ? 59.757  48.429  14.815  1   45.96 ? 159 TYR   B CE1  1 
ATOM   3823 C  CE2  . TYR   B 1 137 ? 60.922  47.072  16.399  1   46.02 ? 159 TYR   B CE2  1 
ATOM   3824 C  CZ   . TYR   B 1 137 ? 60.927  48.092  15.472  1   46.51 ? 159 TYR   B CZ   1 
ATOM   3825 O  OH   . TYR   B 1 137 ? 62.091  48.756  15.174  1   47.34 ? 159 TYR   B OH   1 
ATOM   3826 N  N    . ASN   B 1 138 ? 54.131  46.061  17.553  1   49.02 ? 160 ASN   B N    1 
ATOM   3827 C  CA   . ASN   B 1 138 ? 52.956  45.266  17.818  1   50.23 ? 160 ASN   B CA   1 
ATOM   3828 C  C    . ASN   B 1 138 ? 52.033  46.004  18.772  1   50.83 ? 160 ASN   B C    1 
ATOM   3829 O  O    . ASN   B 1 138 ? 51.066  46.636  18.357  1   51.46 ? 160 ASN   B O    1 
ATOM   3830 C  CB   . ASN   B 1 138 ? 53.341  43.843  18.335  1   52.18 ? 160 ASN   B CB   1 
ATOM   3831 C  CG   . ASN   B 1 138 ? 54.621  43.777  19.163  1   56.13 ? 160 ASN   B CG   1 
ATOM   3832 O  OD1  . ASN   B 1 138 ? 54.745  44.393  20.233  1   56.14 ? 160 ASN   B OD1  1 
ATOM   3833 N  ND2  . ASN   B 1 138 ? 55.606  43.016  18.676  1   57.86 ? 160 ASN   B ND2  1 
ATOM   3834 N  N    . GLN   B 1 139 ? 52.391  45.961  20.047  1   50.42 ? 161 GLN   B N    1 
ATOM   3835 C  CA   . GLN   B 1 139 ? 51.711  46.429  21.226  1   50.26 ? 161 GLN   B CA   1 
ATOM   3836 C  C    . GLN   B 1 139 ? 51.902  47.911  21.441  1   49.94 ? 161 GLN   B C    1 
ATOM   3837 O  O    . GLN   B 1 139 ? 53.011  48.41   21.284  1   50.26 ? 161 GLN   B O    1 
ATOM   3838 C  CB   . GLN   B 1 139 ? 52.315  45.632  22.394  1   51.59 ? 161 GLN   B CB   1 
ATOM   3839 C  CG   . GLN   B 1 139 ? 51.634  45.768  23.734  1   54.76 ? 161 GLN   B CG   1 
ATOM   3840 C  CD   . GLN   B 1 139 ? 52.084  44.682  24.708  1   58.15 ? 161 GLN   B CD   1 
ATOM   3841 O  OE1  . GLN   B 1 139 ? 51.281  44.112  25.447  1   58.97 ? 161 GLN   B OE1  1 
ATOM   3842 N  NE2  . GLN   B 1 139 ? 53.375  44.363  24.737  1   58.36 ? 161 GLN   B NE2  1 
ATOM   3843 N  N    . LYS   B 1 140 ? 50.825  48.622  21.802  1   49.39 ? 162 LYS   B N    1 
ATOM   3844 C  CA   . LYS   B 1 140 ? 50.904  50.044  22.138  1   49.34 ? 162 LYS   B CA   1 
ATOM   3845 C  C    . LYS   B 1 140 ? 51.712  50.163  23.459  1   49.18 ? 162 LYS   B C    1 
ATOM   3846 O  O    . LYS   B 1 140 ? 51.613  49.284  24.323  1   49.11 ? 162 LYS   B O    1 
ATOM   3847 C  CB   . LYS   B 1 140 ? 49.494  50.632  22.324  1   51.03 ? 162 LYS   B CB   1 
ATOM   3848 C  CG   . LYS   B 1 140 ? 49.481  52.156  22.379  1   55.47 ? 162 LYS   B CG   1 
ATOM   3849 C  CD   . LYS   B 1 140 ? 48.079  52.742  22.505  1   60.62 ? 162 LYS   B CD   1 
ATOM   3850 C  CE   . LYS   B 1 140 ? 48.088  54.187  22.046  1   65.49 ? 162 LYS   B CE   1 
ATOM   3851 N  NZ   . LYS   B 1 140 ? 46.754  54.857  22.17   1   68.42 ? 162 LYS   B NZ   1 
ATOM   3852 N  N    . TYR   B 1 141 ? 52.521  51.217  23.609  1   48.94 ? 163 TYR   B N    1 
ATOM   3853 C  CA   . TYR   B 1 141 ? 53.355  51.368  24.808  1   49.29 ? 163 TYR   B CA   1 
ATOM   3854 C  C    . TYR   B 1 141 ? 52.551  51.3    26.139  1   49.78 ? 163 TYR   B C    1 
ATOM   3855 O  O    . TYR   B 1 141 ? 53.039  50.742  27.122  1   50.13 ? 163 TYR   B O    1 
ATOM   3856 C  CB   . TYR   B 1 141 ? 54.216  52.638  24.72   1   48.72 ? 163 TYR   B CB   1 
ATOM   3857 C  CG   . TYR   B 1 141 ? 53.52   53.889  25.211  1   49.06 ? 163 TYR   B CG   1 
ATOM   3858 C  CD1  . TYR   B 1 141 ? 52.548  54.515  24.442  1   49.66 ? 163 TYR   B CD1  1 
ATOM   3859 C  CD2  . TYR   B 1 141 ? 53.81   54.426  26.457  1   49.49 ? 163 TYR   B CD2  1 
ATOM   3860 C  CE1  . TYR   B 1 141 ? 51.91   55.663  24.886  1   50.29 ? 163 TYR   B CE1  1 
ATOM   3861 C  CE2  . TYR   B 1 141 ? 53.174  55.569  26.914  1   50.17 ? 163 TYR   B CE2  1 
ATOM   3862 C  CZ   . TYR   B 1 141 ? 52.222  56.184  26.127  1   50.94 ? 163 TYR   B CZ   1 
ATOM   3863 O  OH   . TYR   B 1 141 ? 51.607  57.325  26.572  1   52.26 ? 163 TYR   B OH   1 
ATOM   3864 N  N    . SER   B 1 142 ? 51.326  51.853  26.155  1   49.57 ? 164 SER   B N    1 
ATOM   3865 C  CA   . SER   B 1 142 ? 50.457  51.885  27.332  1   49.41 ? 164 SER   B CA   1 
ATOM   3866 C  C    . SER   B 1 142 ? 49.808  50.549  27.643  1   49.46 ? 164 SER   B C    1 
ATOM   3867 O  O    . SER   B 1 142 ? 49.416  50.331  28.777  1   49.6  ? 164 SER   B O    1 
ATOM   3868 C  CB   . SER   B 1 142 ? 49.418  52.994  27.22   1   51.26 ? 164 SER   B CB   1 
ATOM   3869 O  OG   . SER   B 1 142 ? 48.973  53.22   25.89   1   54.53 ? 164 SER   B OG   1 
ATOM   3870 N  N    . ASP   B 1 143 ? 49.735  49.632  26.667  1   49.71 ? 165 ASP   B N    1 
ATOM   3871 C  CA   . ASP   B 1 143 ? 49.172  48.286  26.841  1   50.33 ? 165 ASP   B CA   1 
ATOM   3872 C  C    . ASP   B 1 143 ? 49.981  47.378  27.769  1   49.65 ? 165 ASP   B C    1 
ATOM   3873 O  O    . ASP   B 1 143 ? 49.476  46.383  28.294  1   49.87 ? 165 ASP   B O    1 
ATOM   3874 C  CB   . ASP   B 1 143 ? 49.012  47.605  25.482  1   53.63 ? 165 ASP   B CB   1 
ATOM   3875 C  CG   . ASP   B 1 143 ? 47.61   47.731  24.948  1   60.71 ? 165 ASP   B CG   1 
ATOM   3876 O  OD1  . ASP   B 1 143 ? 46.968  48.779  25.208  1   61.24 ? 165 ASP   B OD1  1 
ATOM   3877 O  OD2  . ASP   B 1 143 ? 47.141  46.772  24.294  1   64.05 ? 165 ASP   B OD2  1 
ATOM   3878 N  N    . VAL   B 1 144 ? 51.251  47.7    27.928  1   48.66 ? 166 VAL   B N    1 
ATOM   3879 C  CA   . VAL   B 1 144 ? 52.189  47.013  28.787  1   47.97 ? 166 VAL   B CA   1 
ATOM   3880 C  C    . VAL   B 1 144 ? 51.764  47.105  30.284  1   46.91 ? 166 VAL   B C    1 
ATOM   3881 O  O    . VAL   B 1 144 ? 52.07   46.205  31.063  1   46.57 ? 166 VAL   B O    1 
ATOM   3882 C  CB   . VAL   B 1 144 ? 53.55   47.666  28.473  1   48.45 ? 166 VAL   B CB   1 
ATOM   3883 C  CG1  . VAL   B 1 144 ? 54.505  47.614  29.647  1   49.18 ? 166 VAL   B CG1  1 
ATOM   3884 C  CG2  . VAL   B 1 144 ? 54.154  47.058  27.219  1   47.99 ? 166 VAL   B CG2  1 
ATOM   3885 N  N    . PHE   B 1 145 ? 50.998  48.14   30.651  1   46.3  ? 167 PHE   B N    1 
ATOM   3886 C  CA   . PHE   B 1 145 ? 50.52   48.343  32.015  1   46.83 ? 167 PHE   B CA   1 
ATOM   3887 C  C    . PHE   B 1 145 ? 49.122  47.75   32.244  1   48.41 ? 167 PHE   B C    1 
ATOM   3888 O  O    . PHE   B 1 145 ? 48.165  48.21   31.643  1   48.25 ? 167 PHE   B O    1 
ATOM   3889 C  CB   . PHE   B 1 145 ? 50.528  49.842  32.347  1   45.85 ? 167 PHE   B CB   1 
ATOM   3890 C  CG   . PHE   B 1 145 ? 51.875  50.493  32.152  1   44.88 ? 167 PHE   B CG   1 
ATOM   3891 C  CD1  . PHE   B 1 145 ? 52.816  50.484  33.162  1   45.06 ? 167 PHE   B CD1  1 
ATOM   3892 C  CD2  . PHE   B 1 145 ? 52.213  51.077  30.948  1   44.78 ? 167 PHE   B CD2  1 
ATOM   3893 C  CE1  . PHE   B 1 145 ? 54.061  51.053  32.971  1   45.38 ? 167 PHE   B CE1  1 
ATOM   3894 C  CE2  . PHE   B 1 145 ? 53.461  51.649  30.761  1   45.28 ? 167 PHE   B CE2  1 
ATOM   3895 C  CZ   . PHE   B 1 145 ? 54.373  51.645  31.78   1   44.98 ? 167 PHE   B CZ   1 
ATOM   3896 N  N    . SER   B 1 146 ? 49.015  46.755  33.137  1   49.79 ? 168 SER   B N    1 
ATOM   3897 C  CA   . SER   B 1 146 ? 47.775  46.075  33.51   1   51.81 ? 168 SER   B CA   1 
ATOM   3898 C  C    . SER   B 1 146 ? 47.035  46.772  34.681  1   54.11 ? 168 SER   B C    1 
ATOM   3899 O  O    . SER   B 1 146 ? 45.827  46.596  34.835  1   54.99 ? 168 SER   B O    1 
ATOM   3900 C  CB   . SER   B 1 146 ? 48.083  44.636  33.919  1   52.87 ? 168 SER   B CB   1 
ATOM   3901 N  N    . ASP   B 1 147 ? 47.763  47.52   35.517  1   54.53 ? 169 ASP   B N    1 
ATOM   3902 C  CA   . ASP   B 1 147 ? 47.222  48.208  36.683  1   55.04 ? 169 ASP   B CA   1 
ATOM   3903 C  C    . ASP   B 1 147 ? 46.386  49.413  36.262  1   54.52 ? 169 ASP   B C    1 
ATOM   3904 O  O    . ASP   B 1 147 ? 46.825  50.2    35.43   1   54.6  ? 169 ASP   B O    1 
ATOM   3905 C  CB   . ASP   B 1 147 ? 48.377  48.624  37.613  1   57.79 ? 169 ASP   B CB   1 
ATOM   3906 C  CG   . ASP   B 1 147 ? 47.958  49.379  38.853  1   64.36 ? 169 ASP   B CG   1 
ATOM   3907 O  OD1  . ASP   B 1 147 ? 47.594  48.719  39.857  1   66.52 ? 169 ASP   B OD1  1 
ATOM   3908 O  OD2  . ASP   B 1 147 ? 48.014  50.625  38.833  1   66.33 ? 169 ASP   B OD2  1 
ATOM   3909 N  N    . GLU   B 1 148 ? 45.183  49.564  36.847  1   53.72 ? 170 GLU   B N    1 
ATOM   3910 C  CA   . GLU   B 1 148 ? 44.282  50.659  36.497  1   52.82 ? 170 GLU   B CA   1 
ATOM   3911 C  C    . GLU   B 1 148 ? 44.841  52.042  36.833  1   51.48 ? 170 GLU   B C    1 
ATOM   3912 O  O    . GLU   B 1 148 ? 44.673  52.967  36.045  1   51.33 ? 170 GLU   B O    1 
ATOM   3913 C  CB   . GLU   B 1 148 ? 42.892  50.449  37.118  1   54.93 ? 170 GLU   B CB   1 
ATOM   3914 N  N    . GLU   B 1 149 ? 45.5    52.191  37.986  1   50.62 ? 171 GLU   B N    1 
ATOM   3915 C  CA   . GLU   B 1 149 ? 46.072  53.482  38.376  1   50.24 ? 171 GLU   B CA   1 
ATOM   3916 C  C    . GLU   B 1 149 ? 47.253  53.844  37.457  1   49.02 ? 171 GLU   B C    1 
ATOM   3917 O  O    . GLU   B 1 149 ? 47.411  55.015  37.114  1   49.26 ? 171 GLU   B O    1 
ATOM   3918 C  CB   . GLU   B 1 149 ? 46.486  53.485  39.863  1   52.99 ? 171 GLU   B CB   1 
ATOM   3919 N  N    . ALA   B 1 150 ? 48.042  52.835  37.009  1   47.33 ? 172 ALA   B N    1 
ATOM   3920 C  CA   . ALA   B 1 150 ? 49.142  53.063  36.067  1   46.12 ? 172 ALA   B CA   1 
ATOM   3921 C  C    . ALA   B 1 150 ? 48.575  53.563  34.722  1   45.13 ? 172 ALA   B C    1 
ATOM   3922 O  O    . ALA   B 1 150 ? 49.033  54.582  34.214  1   44.22 ? 172 ALA   B O    1 
ATOM   3923 C  CB   . ALA   B 1 150 ? 49.944  51.782  35.87   1   45.89 ? 172 ALA   B CB   1 
ATOM   3924 N  N    . ARG   B 1 151 ? 47.516  52.892  34.192  1   45.23 ? 173 ARG   B N    1 
ATOM   3925 C  CA   . ARG   B 1 151 ? 46.845  53.283  32.941  1   45.23 ? 173 ARG   B CA   1 
ATOM   3926 C  C    . ARG   B 1 151 ? 46.255  54.685  33.061  1   45.6  ? 173 ARG   B C    1 
ATOM   3927 O  O    . ARG   B 1 151 ? 46.333  55.476  32.126  1   45.31 ? 173 ARG   B O    1 
ATOM   3928 C  CB   . ARG   B 1 151 ? 45.725  52.283  32.581  1   46.27 ? 173 ARG   B CB   1 
ATOM   3929 C  CG   . ARG   B 1 151 ? 46.217  50.871  32.281  1   47.86 ? 173 ARG   B CG   1 
ATOM   3930 C  CD   . ARG   B 1 151 ? 45.124  49.984  31.73   1   50.4  ? 173 ARG   B CD   1 
ATOM   3931 N  NE   . ARG   B 1 151 ? 44.835  50.249  30.318  1   53.32 ? 173 ARG   B NE   1 
ATOM   3932 C  CZ   . ARG   B 1 151 ? 45.423  49.627  29.299  1   55.41 ? 173 ARG   B CZ   1 
ATOM   3933 N  NH1  . ARG   B 1 151 ? 46.35   48.703  29.52   1   54.54 ? 173 ARG   B NH1  1 
ATOM   3934 N  NH2  . ARG   B 1 151 ? 45.083  49.92   28.05   1   55.66 ? 173 ARG   B NH2  1 
ATOM   3935 N  N    . ASN   B 1 152 ? 45.679  55.004  34.223  1   46.52 ? 174 ASN   B N    1 
ATOM   3936 C  CA   . ASN   B 1 152 ? 45.092  56.319  34.469  1   47.13 ? 174 ASN   B CA   1 
ATOM   3937 C  C    . ASN   B 1 152 ? 46.175  57.384  34.463  1   46.74 ? 174 ASN   B C    1 
ATOM   3938 O  O    . ASN   B 1 152 ? 45.994  58.41   33.818  1   47.34 ? 174 ASN   B O    1 
ATOM   3939 C  CB   . ASN   B 1 152 ? 44.33   56.319  35.78   1   49.25 ? 174 ASN   B CB   1 
ATOM   3940 C  CG   . ASN   B 1 152 ? 43.428  57.5    35.939  1   54.36 ? 174 ASN   B CG   1 
ATOM   3941 O  OD1  . ASN   B 1 152 ? 42.614  57.805  35.055  1   56.56 ? 174 ASN   B OD1  1 
ATOM   3942 N  ND2  . ASN   B 1 152 ? 43.55   58.194  37.078  1   54.82 ? 174 ASN   B ND2  1 
ATOM   3943 N  N    . SER   B 1 153 ? 47.324  57.114  35.111  1   45.98 ? 175 SER   B N    1 
ATOM   3944 C  CA   . SER   B 1 153 ? 48.476  58.026  35.131  1   45.78 ? 175 SER   B CA   1 
ATOM   3945 C  C    . SER   B 1 153 ? 48.995  58.31   33.716  1   45.31 ? 175 SER   B C    1 
ATOM   3946 O  O    . SER   B 1 153 ? 49.167  59.48   33.353  1   45.19 ? 175 SER   B O    1 
ATOM   3947 C  CB   . SER   B 1 153 ? 49.591  57.457  35.997  1   47.27 ? 175 SER   B CB   1 
ATOM   3948 O  OG   . SER   B 1 153 ? 49.186  57.372  37.352  1   49.9  ? 175 SER   B OG   1 
ATOM   3949 N  N    . ILE   B 1 154 ? 49.187  57.244  32.901  1   45.06 ? 176 ILE   B N    1 
ATOM   3950 C  CA   . ILE   B 1 154 ? 49.605  57.365  31.506  1   45.66 ? 176 ILE   B CA   1 
ATOM   3951 C  C    . ILE   B 1 154 ? 48.596  58.21   30.716  1   46.4  ? 176 ILE   B C    1 
ATOM   3952 O  O    . ILE   B 1 154 ? 48.989  59.179  30.064  1   46.72 ? 176 ILE   B O    1 
ATOM   3953 C  CB   . ILE   B 1 154 ? 49.833  55.968  30.882  1   46.21 ? 176 ILE   B CB   1 
ATOM   3954 C  CG1  . ILE   B 1 154 ? 51.153  55.377  31.378  1   47.76 ? 176 ILE   B CG1  1 
ATOM   3955 C  CG2  . ILE   B 1 154 ? 49.815  56      29.35   1   46.54 ? 176 ILE   B CG2  1 
ATOM   3956 C  CD1  . ILE   B 1 154 ? 51.105  54.082  31.433  1   49.34 ? 176 ILE   B CD1  1 
ATOM   3957 N  N    . ARG   B 1 155 ? 47.3    57.883  30.813  1   46.69 ? 177 ARG   B N    1 
ATOM   3958 C  CA   . ARG   B 1 155 ? 46.236  58.632  30.134  1   47.97 ? 177 ARG   B CA   1 
ATOM   3959 C  C    . ARG   B 1 155 ? 46.273  60.124  30.51   1   48.07 ? 177 ARG   B C    1 
ATOM   3960 O  O    . ARG   B 1 155 ? 46.232  60.981  29.631  1   47.77 ? 177 ARG   B O    1 
ATOM   3961 C  CB   . ARG   B 1 155 ? 44.871  58.024  30.476  1   50.8  ? 177 ARG   B CB   1 
ATOM   3962 C  CG   . ARG   B 1 155 ? 43.919  57.917  29.273  1   56.08 ? 177 ARG   B CG   1 
ATOM   3963 C  CD   . ARG   B 1 155 ? 42.674  57.037  29.459  1   60.25 ? 177 ARG   B CD   1 
ATOM   3964 N  NE   . ARG   B 1 155 ? 42.57   56.367  30.764  1   64.74 ? 177 ARG   B NE   1 
ATOM   3965 C  CZ   . ARG   B 1 155 ? 42.786  55.07   30.962  1   67.6  ? 177 ARG   B CZ   1 
ATOM   3966 N  NH1  . ARG   B 1 155 ? 42.665  54.549  32.179  1   67.07 ? 177 ARG   B NH1  1 
ATOM   3967 N  NH2  . ARG   B 1 155 ? 43.092  54.276  29.941  1   67.71 ? 177 ARG   B NH2  1 
ATOM   3968 N  N    . ASN   B 1 156 ? 46.432  60.428  31.808  1   48.46 ? 178 ASN   B N    1 
ATOM   3969 C  CA   . ASN   B 1 156 ? 46.52   61.807  32.29   1   49.28 ? 178 ASN   B CA   1 
ATOM   3970 C  C    . ASN   B 1 156 ? 47.757  62.522  31.723  1   49.33 ? 178 ASN   B C    1 
ATOM   3971 O  O    . ASN   B 1 156 ? 47.641  63.652  31.268  1   49.25 ? 178 ASN   B O    1 
ATOM   3972 C  CB   . ASN   B 1 156 ? 46.516  61.853  33.822  1   51.06 ? 178 ASN   B CB   1 
ATOM   3973 C  CG   . ASN   B 1 156 ? 45.229  61.356  34.451  1   55.91 ? 178 ASN   B CG   1 
ATOM   3974 O  OD1  . ASN   B 1 156 ? 44.156  61.41   33.844  1   57.96 ? 178 ASN   B OD1  1 
ATOM   3975 N  ND2  . ASN   B 1 156 ? 45.302  60.844  35.68   1   56.71 ? 178 ASN   B ND2  1 
ATOM   3976 N  N    . SER   B 1 157 ? 48.922  61.849  31.686  1   48.88 ? 179 SER   B N    1 
ATOM   3977 C  CA   . SER   B 1 157 ? 50.136  62.459  31.131  1   48.93 ? 179 SER   B CA   1 
ATOM   3978 C  C    . SER   B 1 157 ? 50.027  62.759  29.628  1   49.3  ? 179 SER   B C    1 
ATOM   3979 O  O    . SER   B 1 157 ? 50.646  63.709  29.142  1   49.1  ? 179 SER   B O    1 
ATOM   3980 C  CB   . SER   B 1 157 ? 51.376  61.622  31.439  1   49.32 ? 179 SER   B CB   1 
ATOM   3981 O  OG   . SER   B 1 157 ? 51.378  60.361  30.793  1   50.47 ? 179 SER   B OG   1 
ATOM   3982 N  N    . GLU   B 1 158 ? 49.207  61.985  28.902  1   49.67 ? 180 GLU   B N    1 
ATOM   3983 C  CA   . GLU   B 1 158 ? 48.985  62.244  27.476  1   50.66 ? 180 GLU   B CA   1 
ATOM   3984 C  C    . GLU   B 1 158 ? 48.021  63.424  27.265  1   51.72 ? 180 GLU   B C    1 
ATOM   3985 O  O    . GLU   B 1 158 ? 48.259  64.255  26.389  1   52.09 ? 180 GLU   B O    1 
ATOM   3986 C  CB   . GLU   B 1 158 ? 48.383  61.022  26.768  1   51.9  ? 180 GLU   B CB   1 
ATOM   3987 C  CG   . GLU   B 1 158 ? 49.2    59.753  26.801  1   55.28 ? 180 GLU   B CG   1 
ATOM   3988 C  CD   . GLU   B 1 158 ? 48.453  58.563  26.227  1   61.94 ? 180 GLU   B CD   1 
ATOM   3989 O  OE1  . GLU   B 1 158 ? 47.202  58.575  26.258  1   64.78 ? 180 GLU   B OE1  1 
ATOM   3990 O  OE2  . GLU   B 1 158 ? 49.116  57.616  25.747  1   63.29 ? 180 GLU   B OE2  1 
ATOM   3991 N  N    . LYS   B 1 159 ? 46.913  63.475  28.033  1   52.06 ? 181 LYS   B N    1 
ATOM   3992 C  CA   . LYS   B 1 159 ? 45.889  64.507  27.847  1   53.07 ? 181 LYS   B CA   1 
ATOM   3993 C  C    . LYS   B 1 159 ? 46.237  65.852  28.471  1   54.03 ? 181 LYS   B C    1 
ATOM   3994 O  O    . LYS   B 1 159 ? 45.874  66.888  27.913  1   54.66 ? 181 LYS   B O    1 
ATOM   3995 C  CB   . LYS   B 1 159 ? 44.516  64.014  28.335  1   54.92 ? 181 LYS   B CB   1 
ATOM   3996 N  N    . ASP   B 1 160 ? 46.916  65.855  29.623  1   54.01 ? 182 ASP   B N    1 
ATOM   3997 C  CA   . ASP   B 1 160 ? 47.316  67.112  30.262  1   54.34 ? 182 ASP   B CA   1 
ATOM   3998 C  C    . ASP   B 1 160 ? 48.352  67.817  29.385  1   53.63 ? 182 ASP   B C    1 
ATOM   3999 O  O    . ASP   B 1 160 ? 49.149  67.15   28.716  1   53.67 ? 182 ASP   B O    1 
ATOM   4000 C  CB   . ASP   B 1 160 ? 47.933  66.861  31.648  1   57.04 ? 182 ASP   B CB   1 
ATOM   4001 C  CG   . ASP   B 1 160 ? 47.026  66.204  32.675  1   62.59 ? 182 ASP   B CG   1 
ATOM   4002 O  OD1  . ASP   B 1 160 ? 45.789  66.264  32.504  1   62.28 ? 182 ASP   B OD1  1 
ATOM   4003 O  OD2  . ASP   B 1 160 ? 47.561  65.618  33.649  1   66.52 ? 182 ASP   B OD2  1 
ATOM   4004 N  N    . PRO   B 1 161 ? 48.369  69.163  29.368  1   52.78 ? 183 PRO   B N    1 
ATOM   4005 C  CA   . PRO   B 1 161 ? 49.382  69.859  28.558  1   52.46 ? 183 PRO   B CA   1 
ATOM   4006 C  C    . PRO   B 1 161 ? 50.815  69.492  28.963  1   52.58 ? 183 PRO   B C    1 
ATOM   4007 O  O    . PRO   B 1 161 ? 51.18   69.535  30.143  1   52.91 ? 183 PRO   B O    1 
ATOM   4008 C  CB   . PRO   B 1 161 ? 49.077  71.345  28.782  1   52.89 ? 183 PRO   B CB   1 
ATOM   4009 C  CG   . PRO   B 1 161 ? 48.271  71.398  30.034  1   53.4  ? 183 PRO   B CG   1 
ATOM   4010 C  CD   . PRO   B 1 161 ? 47.499  70.111  30.092  1   51.95 ? 183 PRO   B CD   1 
ATOM   4011 N  N    . SER   B 1 162 ? 51.6    69.061  27.978  1   51.69 ? 184 SER   B N    1 
ATOM   4012 C  CA   . SER   B 1 162 ? 52.997  68.694  28.157  1   51.31 ? 184 SER   B CA   1 
ATOM   4013 C  C    . SER   B 1 162 ? 53.851  69.977  28.237  1   50.71 ? 184 SER   B C    1 
ATOM   4014 O  O    . SER   B 1 162 ? 53.343  71.076  27.996  1   51.02 ? 184 SER   B O    1 
ATOM   4015 C  CB   . SER   B 1 162 ? 53.446  67.84   26.965  1   52.03 ? 184 SER   B CB   1 
ATOM   4016 O  OG   . SER   B 1 162 ? 53.541  68.605  25.771  1   53.2  ? 184 SER   B OG   1 
ATOM   4017 N  N    . LEU   B 1 163 ? 55.156  69.845  28.531  1   49.62 ? 185 LEU   B N    1 
ATOM   4018 C  CA   . LEU   B 1 163 ? 56.067  70.992  28.53   1   49.07 ? 185 LEU   B CA   1 
ATOM   4019 C  C    . LEU   B 1 163 ? 56.135  71.57   27.088  1   48.45 ? 185 LEU   B C    1 
ATOM   4020 O  O    . LEU   B 1 163 ? 56.224  72.781  26.92   1   48.14 ? 185 LEU   B O    1 
ATOM   4021 C  CB   . LEU   B 1 163 ? 57.471  70.554  28.983  1   49.3  ? 185 LEU   B CB   1 
ATOM   4022 C  CG   . LEU   B 1 163 ? 57.835  70.684  30.46   1   51.46 ? 185 LEU   B CG   1 
ATOM   4023 C  CD1  . LEU   B 1 163 ? 57.268  69.589  31.288  1   52.38 ? 185 LEU   B CD1  1 
ATOM   4024 C  CD2  . LEU   B 1 163 ? 59.345  70.603  30.626  1   52.2  ? 185 LEU   B CD2  1 
ATOM   4025 N  N    . LEU   B 1 164 ? 56.066  70.7    26.056  1   47.64 ? 186 LEU   B N    1 
ATOM   4026 C  CA   . LEU   B 1 164 ? 56.069  71.124  24.664  1   47.6  ? 186 LEU   B CA   1 
ATOM   4027 C  C    . LEU   B 1 164 ? 54.863  72.06   24.385  1   48.19 ? 186 LEU   B C    1 
ATOM   4028 O  O    . LEU   B 1 164 ? 55.05   73.128  23.803  1   47.94 ? 186 LEU   B O    1 
ATOM   4029 C  CB   . LEU   B 1 164 ? 56.027  69.885  23.748  1   47    ? 186 LEU   B CB   1 
ATOM   4030 C  CG   . LEU   B 1 164 ? 55.812  70.138  22.261  1   47.12 ? 186 LEU   B CG   1 
ATOM   4031 C  CD1  . LEU   B 1 164 ? 56.94   70.966  21.673  1   47.44 ? 186 LEU   B CD1  1 
ATOM   4032 C  CD2  . LEU   B 1 164 ? 55.663  68.831  21.505  1   47.31 ? 186 LEU   B CD2  1 
ATOM   4033 N  N    . GLU   B 1 165 ? 53.647  71.668  24.809  1   48.65 ? 187 GLU   B N    1 
ATOM   4034 C  CA   . GLU   B 1 165 ? 52.446  72.481  24.593  1   49.87 ? 187 GLU   B CA   1 
ATOM   4035 C  C    . GLU   B 1 165 ? 52.531  73.79   25.37   1   50.7  ? 187 GLU   B C    1 
ATOM   4036 O  O    . GLU   B 1 165 ? 52.309  74.856  24.799  1   51.39 ? 187 GLU   B O    1 
ATOM   4037 C  CB   . GLU   B 1 165 ? 51.168  71.712  24.995  1   52.08 ? 187 GLU   B CB   1 
ATOM   4038 C  CG   . GLU   B 1 165 ? 50.981  70.378  24.289  1   56.55 ? 187 GLU   B CG   1 
ATOM   4039 N  N    . LEU   B 1 166 ? 52.887  73.72   26.653  1   50.51 ? 188 LEU   B N    1 
ATOM   4040 C  CA   . LEU   B 1 166 ? 52.992  74.901  27.503  1   50.93 ? 188 LEU   B CA   1 
ATOM   4041 C  C    . LEU   B 1 166 ? 54.062  75.892  27.054  1   51.61 ? 188 LEU   B C    1 
ATOM   4042 O  O    . LEU   B 1 166 ? 53.835  77.103  27.113  1   52.08 ? 188 LEU   B O    1 
ATOM   4043 C  CB   . LEU   B 1 166 ? 53.192  74.476  28.949  1   51.29 ? 188 LEU   B CB   1 
ATOM   4044 C  CG   . LEU   B 1 166 ? 52.009  73.704  29.52   1   53.15 ? 188 LEU   B CG   1 
ATOM   4045 C  CD1  . LEU   B 1 166 ? 52.364  73.055  30.836  1   53.61 ? 188 LEU   B CD1  1 
ATOM   4046 C  CD2  . LEU   B 1 166 ? 50.789  74.615  29.674  1   53.75 ? 188 LEU   B CD2  1 
ATOM   4047 N  N    . VAL   B 1 167 ? 55.209  75.4    26.577  1   51.63 ? 189 VAL   B N    1 
ATOM   4048 C  CA   . VAL   B 1 167 ? 56.28   76.278  26.101  1   52.25 ? 189 VAL   B CA   1 
ATOM   4049 C  C    . VAL   B 1 167 ? 55.833  77.021  24.842  1   53.41 ? 189 VAL   B C    1 
ATOM   4050 O  O    . VAL   B 1 167 ? 56.157  78.198  24.679  1   53.62 ? 189 VAL   B O    1 
ATOM   4051 C  CB   . VAL   B 1 167 ? 57.635  75.528  25.948  1   52.3  ? 189 VAL   B CB   1 
ATOM   4052 C  CG1  . VAL   B 1 167 ? 58.623  76.286  25.067  1   52.27 ? 189 VAL   B CG1  1 
ATOM   4053 C  CG2  . VAL   B 1 167 ? 58.246  75.248  27.314  1   52.68 ? 189 VAL   B CG2  1 
ATOM   4054 N  N    . GLN   B 1 168 ? 55.059  76.345  23.975  1   53.99 ? 190 GLN   B N    1 
ATOM   4055 C  CA   . GLN   B 1 168 ? 54.502  76.939  22.762  1   55.04 ? 190 GLN   B CA   1 
ATOM   4056 C  C    . GLN   B 1 168 ? 53.533  78.09   23.09   1   55.66 ? 190 GLN   B C    1 
ATOM   4057 O  O    . GLN   B 1 168 ? 53.684  79.16   22.51   1   55.49 ? 190 GLN   B O    1 
ATOM   4058 C  CB   . GLN   B 1 168 ? 53.794  75.876  21.925  1   56.71 ? 190 GLN   B CB   1 
ATOM   4059 C  CG   . GLN   B 1 168 ? 54.728  75.08   21.033  1   59.08 ? 190 GLN   B CG   1 
ATOM   4060 C  CD   . GLN   B 1 168 ? 53.927  74.038  20.312  1   62.06 ? 190 GLN   B CD   1 
ATOM   4061 O  OE1  . GLN   B 1 168 ? 53.858  72.876  20.721  1   62.96 ? 190 GLN   B OE1  1 
ATOM   4062 N  NE2  . GLN   B 1 168 ? 53.261  74.447  19.249  1   62.33 ? 190 GLN   B NE2  1 
ATOM   4063 N  N    . ARG   B 1 169 ? 52.598  77.905  24.061  1   56.18 ? 191 ARG   B N    1 
ATOM   4064 C  CA   . ARG   B 1 169 ? 51.668  78.973  24.468  1   57.55 ? 191 ARG   B CA   1 
ATOM   4065 C  C    . ARG   B 1 169 ? 52.444  80.194  24.971  1   58.9  ? 191 ARG   B C    1 
ATOM   4066 O  O    . ARG   B 1 169 ? 52.118  81.324  24.607  1   59.58 ? 191 ARG   B O    1 
ATOM   4067 C  CB   . ARG   B 1 169 ? 50.681  78.501  25.557  1   58.67 ? 191 ARG   B CB   1 
ATOM   4068 C  CG   . ARG   B 1 169 ? 49.931  77.225  25.211  1   61.92 ? 191 ARG   B CG   1 
ATOM   4069 N  N    . TRP   B 1 170 ? 53.496  79.957  25.769  1   58.88 ? 192 TRP   B N    1 
ATOM   4070 C  CA   . TRP   B 1 170 ? 54.362  80.996  26.304  1   59.48 ? 192 TRP   B CA   1 
ATOM   4071 C  C    . TRP   B 1 170 ? 55.107  81.719  25.165  1   59.98 ? 192 TRP   B C    1 
ATOM   4072 O  O    . TRP   B 1 170 ? 55.251  82.937  25.202  1   60.43 ? 192 TRP   B O    1 
ATOM   4073 C  CB   . TRP   B 1 170 ? 55.338  80.371  27.329  1   59.74 ? 192 TRP   B CB   1 
ATOM   4074 C  CG   . TRP   B 1 170 ? 56.503  81.227  27.725  1   60.55 ? 192 TRP   B CG   1 
ATOM   4075 C  CD1  . TRP   B 1 170 ? 56.486  82.292  28.574  1   61.49 ? 192 TRP   B CD1  1 
ATOM   4076 C  CD2  . TRP   B 1 170 ? 57.87   81.057  27.323  1   60.82 ? 192 TRP   B CD2  1 
ATOM   4077 N  NE1  . TRP   B 1 170 ? 57.751  82.813  28.705  1   61.77 ? 192 TRP   B NE1  1 
ATOM   4078 C  CE2  . TRP   B 1 170 ? 58.621  82.072  27.948  1   61.47 ? 192 TRP   B CE2  1 
ATOM   4079 C  CE3  . TRP   B 1 170 ? 58.536  80.143  26.494  1   61.34 ? 192 TRP   B CE3  1 
ATOM   4080 C  CZ2  . TRP   B 1 170 ? 59.997  82.207  27.758  1   61.94 ? 192 TRP   B CZ2  1 
ATOM   4081 C  CZ3  . TRP   B 1 170 ? 59.899  80.286  26.302  1   61.87 ? 192 TRP   B CZ3  1 
ATOM   4082 C  CH2  . TRP   B 1 170 ? 60.611  81.311  26.923  1   61.89 ? 192 TRP   B CH2  1 
ATOM   4083 N  N    . LEU   B 1 171 ? 55.564  80.976  24.156  1   59.89 ? 193 LEU   B N    1 
ATOM   4084 C  CA   . LEU   B 1 171 ? 56.28   81.547  23.012  1   60.63 ? 193 LEU   B CA   1 
ATOM   4085 C  C    . LEU   B 1 171 ? 55.363  82.386  22.12   1   61.77 ? 193 LEU   B C    1 
ATOM   4086 O  O    . LEU   B 1 171 ? 55.816  83.372  21.535  1   61.79 ? 193 LEU   B O    1 
ATOM   4087 C  CB   . LEU   B 1 171 ? 56.94   80.447  22.164  1   60.5  ? 193 LEU   B CB   1 
ATOM   4088 C  CG   . LEU   B 1 171 ? 58.25   79.876  22.685  1   61.29 ? 193 LEU   B CG   1 
ATOM   4089 C  CD1  . LEU   B 1 171 ? 58.709  78.727  21.822  1   61.51 ? 193 LEU   B CD1  1 
ATOM   4090 C  CD2  . LEU   B 1 171 ? 59.318  80.94   22.742  1   61.45 ? 193 LEU   B CD2  1 
ATOM   4091 N  N    . GLU   B 1 172 ? 54.09   81.981  21.999  1   62.26 ? 194 GLU   B N    1 
ATOM   4092 C  CA   . GLU   B 1 172 ? 53.09   82.68   21.192  1   62.94 ? 194 GLU   B CA   1 
ATOM   4093 C  C    . GLU   B 1 172 ? 52.828  84.083  21.768  1   64    ? 194 GLU   B C    1 
ATOM   4094 O  O    . GLU   B 1 172 ? 52.729  85.055  21.018  1   64.05 ? 194 GLU   B O    1 
ATOM   4095 C  CB   . GLU   B 1 172 ? 51.789  81.859  21.146  1   63.98 ? 194 GLU   B CB   1 
ATOM   4096 C  CG   . GLU   B 1 172 ? 51.852  80.662  20.212  1   66.35 ? 194 GLU   B CG   1 
ATOM   4097 C  CD   . GLU   B 1 172 ? 50.82   79.578  20.467  1   71.39 ? 194 GLU   B CD   1 
ATOM   4098 O  OE1  . GLU   B 1 172 ? 49.963  79.769  21.361  1   72.08 ? 194 GLU   B OE1  1 
ATOM   4099 O  OE2  . GLU   B 1 172 ? 50.871  78.532  19.778  1   73.37 ? 194 GLU   B OE2  1 
ATOM   4100 N  N    . ARG   B 1 173 ? 52.785  84.187  23.11   1   64.6  ? 195 ARG   B N    1 
ATOM   4101 C  CA   . ARG   B 1 173 ? 52.567  85.439  23.839  1   65.28 ? 195 ARG   B CA   1 
ATOM   4102 C  C    . ARG   B 1 173 ? 53.857  86.232  24.051  1   66.95 ? 195 ARG   B C    1 
ATOM   4103 O  O    . ARG   B 1 173 ? 53.918  87.04   24.977  1   67.46 ? 195 ARG   B O    1 
ATOM   4104 C  CB   . ARG   B 1 173 ? 51.923  85.151  25.206  1   65.53 ? 195 ARG   B CB   1 
ATOM   4105 C  CG   . ARG   B 1 173 ? 50.697  84.252  25.129  1   67.34 ? 195 ARG   B CG   1 
ATOM   4106 C  CD   . ARG   B 1 173 ? 50.327  83.669  26.477  1   69.18 ? 195 ARG   B CD   1 
ATOM   4107 N  N    . THR   B 1 174 ? 54.887  86.011  23.221  1   67.94 ? 196 THR   B N    1 
ATOM   4108 C  CA   . THR   B 1 174 ? 56.146  86.736  23.365  1   69.44 ? 196 THR   B CA   1 
ATOM   4109 C  C    . THR   B 1 174 ? 55.973  88.227  23.082  1   71    ? 196 THR   B C    1 
ATOM   4110 O  O    . THR   B 1 174 ? 55.569  88.623  21.984  1   71.09 ? 196 THR   B O    1 
ATOM   4111 C  CB   . THR   B 1 174 ? 57.238  86.148  22.463  1   70.77 ? 196 THR   B CB   1 
ATOM   4112 O  OG1  . THR   B 1 174 ? 57.501  84.801  22.858  1   72.03 ? 196 THR   B OG1  1 
ATOM   4113 C  CG2  . THR   B 1 174 ? 58.53   86.957  22.507  1   71.06 ? 196 THR   B CG2  1 
ATOM   4114 N  N    . PRO   B 1 175 ? 56.299  89.073  24.074  1   71.86 ? 197 PRO   B N    1 
ATOM   4115 C  CA   . PRO   B 1 175 ? 56.235  90.52   23.841  1   72.26 ? 197 PRO   B CA   1 
ATOM   4116 C  C    . PRO   B 1 175 ? 57.312  90.908  22.829  1   72.45 ? 197 PRO   B C    1 
ATOM   4117 O  O    . PRO   B 1 175 ? 58.49   90.601  23.022  1   72.77 ? 197 PRO   B O    1 
ATOM   4118 C  CB   . PRO   B 1 175 ? 56.518  91.118  25.231  1   73.08 ? 197 PRO   B CB   1 
ATOM   4119 C  CG   . PRO   B 1 175 ? 56.386  89.962  26.207  1   73.52 ? 197 PRO   B CG   1 
ATOM   4120 C  CD   . PRO   B 1 175 ? 56.808  88.763  25.424  1   71.75 ? 197 PRO   B CD   1 
ATOM   4121 N  N    . GLY   B 1 176 ? 56.887  91.524  21.74   1   72.01 ? 198 GLY   B N    1 
ATOM   4122 C  CA   . GLY   B 1 176 ? 57.782  91.898  20.652  1   72.25 ? 198 GLY   B CA   1 
ATOM   4123 C  C    . GLY   B 1 176 ? 57.214  91.475  19.315  1   72.48 ? 198 GLY   B C    1 
ATOM   4124 O  O    . GLY   B 1 176 ? 57.465  92.121  18.296  1   72.52 ? 198 GLY   B O    1 
ATOM   4125 N  N    . LEU   B 1 177 ? 56.442  90.369  19.317  1   72.65 ? 199 LEU   B N    1 
ATOM   4126 C  CA   . LEU   B 1 177 ? 55.757  89.851  18.14   1   73.48 ? 199 LEU   B CA   1 
ATOM   4127 C  C    . LEU   B 1 177 ? 54.485  90.678  17.831  1   74.5  ? 199 LEU   B C    1 
ATOM   4128 O  O    . LEU   B 1 177 ? 54.016  90.652  16.69   1   74.67 ? 199 LEU   B O    1 
ATOM   4129 C  CB   . LEU   B 1 177 ? 55.347  88.381  18.358  1   73.4  ? 199 LEU   B CB   1 
ATOM   4130 C  CG   . LEU   B 1 177 ? 56.436  87.31   18.364  1   74.14 ? 199 LEU   B CG   1 
ATOM   4131 C  CD1  . LEU   B 1 177 ? 55.811  85.937  18.522  1   74.5  ? 199 LEU   B CD1  1 
ATOM   4132 C  CD2  . LEU   B 1 177 ? 57.279  87.357  17.089  1   74.42 ? 199 LEU   B CD2  1 
ATOM   4133 N  N    . GLU   B 1 178 ? 53.91   91.374  18.849  1   74.91 ? 200 GLU   B N    1 
ATOM   4134 C  CA   . GLU   B 1 178 ? 52.693  92.185  18.721  1   75.77 ? 200 GLU   B CA   1 
ATOM   4135 C  C    . GLU   B 1 178 ? 52.755  93.131  17.52   1   76.42 ? 200 GLU   B C    1 
ATOM   4136 O  O    . GLU   B 1 178 ? 53.671  93.949  17.435  1   76.44 ? 200 GLU   B O    1 
ATOM   4137 C  CB   . GLU   B 1 178 ? 52.419  92.962  20.021  1   77.58 ? 200 GLU   B CB   1 
ATOM   4138 N  N    . GLU   B 1 179 ? 51.817  92.977  16.567  1   76.68 ? 201 GLU   B N    1 
ATOM   4139 C  CA   . GLU   B 1 179 ? 51.784  93.807  15.36   1   77.46 ? 201 GLU   B CA   1 
ATOM   4140 C  C    . GLU   B 1 179 ? 51.583  95.302  15.681  1   77.86 ? 201 GLU   B C    1 
ATOM   4141 O  O    . GLU   B 1 179 ? 52.1    96.16   14.962  1   78.09 ? 201 GLU   B O    1 
ATOM   4142 C  CB   . GLU   B 1 179 ? 50.736  93.285  14.368  1   79.48 ? 201 GLU   B CB   1 
ATOM   4143 N  N    . SER   B 1 180 ? 50.888  95.601  16.795  1   77.67 ? 202 SER   B N    1 
ATOM   4144 C  CA   . SER   B 1 180 ? 50.676  96.965  17.28   1   77.97 ? 202 SER   B CA   1 
ATOM   4145 C  C    . SER   B 1 180 ? 51.965  97.548  17.915  1   77.81 ? 202 SER   B C    1 
ATOM   4146 O  O    . SER   B 1 180 ? 52.208  98.755  17.837  1   77.85 ? 202 SER   B O    1 
ATOM   4147 C  CB   . SER   B 1 180 ? 49.548  96.983  18.308  1   79.18 ? 202 SER   B CB   1 
ATOM   4148 N  N    . GLY   B 1 181 ? 52.76   96.684  18.544  1   77.19 ? 203 GLY   B N    1 
ATOM   4149 C  CA   . GLY   B 1 181 ? 53.993  97.073  19.212  1   77.04 ? 203 GLY   B CA   1 
ATOM   4150 C  C    . GLY   B 1 181 ? 55.251  96.999  18.369  1   76.47 ? 203 GLY   B C    1 
ATOM   4151 O  O    . GLY   B 1 181 ? 55.35   97.667  17.334  1   76.68 ? 203 GLY   B O    1 
ATOM   4152 N  N    . PHE   B 1 182 ? 56.235  96.189  18.815  1   75.35 ? 204 PHE   B N    1 
ATOM   4153 C  CA   . PHE   B 1 182 ? 57.513  96.051  18.12   1   74.48 ? 204 PHE   B CA   1 
ATOM   4154 C  C    . PHE   B 1 182 ? 57.371  95.462  16.712  1   73.16 ? 204 PHE   B C    1 
ATOM   4155 O  O    . PHE   B 1 182 ? 58.138  95.834  15.82   1   73.11 ? 204 PHE   B O    1 
ATOM   4156 C  CB   . PHE   B 1 182 ? 58.533  95.269  18.969  1   74.57 ? 204 PHE   B CB   1 
ATOM   4157 C  CG   . PHE   B 1 182 ? 59.931  95.313  18.401  1   75.19 ? 204 PHE   B CG   1 
ATOM   4158 C  CD1  . PHE   B 1 182 ? 60.681  96.477  18.454  1   75.81 ? 204 PHE   B CD1  1 
ATOM   4159 C  CD2  . PHE   B 1 182 ? 60.478  94.206  17.778  1   75.98 ? 204 PHE   B CD2  1 
ATOM   4160 C  CE1  . PHE   B 1 182 ? 61.953  96.527  17.901  1   76.45 ? 204 PHE   B CE1  1 
ATOM   4161 C  CE2  . PHE   B 1 182 ? 61.748  94.261  17.221  1   76.59 ? 204 PHE   B CE2  1 
ATOM   4162 C  CZ   . PHE   B 1 182 ? 62.482  95.417  17.297  1   76.31 ? 204 PHE   B CZ   1 
ATOM   4163 N  N    . ASN   B 1 183 ? 56.371  94.578  16.506  1   71.94 ? 205 ASN   B N    1 
ATOM   4164 C  CA   . ASN   B 1 183 ? 56.076  93.968  15.207  1   71.42 ? 205 ASN   B CA   1 
ATOM   4165 C  C    . ASN   B 1 183 ? 57.315  93.328  14.573  1   70.37 ? 205 ASN   B C    1 
ATOM   4166 O  O    . ASN   B 1 183 ? 57.717  93.699  13.463  1   70.27 ? 205 ASN   B O    1 
ATOM   4167 C  CB   . ASN   B 1 183 ? 55.436  95.006  14.27   1   72.89 ? 205 ASN   B CB   1 
ATOM   4168 N  N    . PHE   B 1 184 ? 57.947  92.396  15.312  1   69.15 ? 206 PHE   B N    1 
ATOM   4169 C  CA   . PHE   B 1 184 ? 59.18   91.746  14.883  1   68.13 ? 206 PHE   B CA   1 
ATOM   4170 C  C    . PHE   B 1 184 ? 59.075  91.005  13.545  1   67.1  ? 206 PHE   B C    1 
ATOM   4171 O  O    . PHE   B 1 184 ? 59.972  91.148  12.714  1   67.01 ? 206 PHE   B O    1 
ATOM   4172 C  CB   . PHE   B 1 184 ? 59.739  90.803  15.988  1   67.79 ? 206 PHE   B CB   1 
ATOM   4173 C  CG   . PHE   B 1 184 ? 60.873  89.906  15.521  1   67.73 ? 206 PHE   B CG   1 
ATOM   4174 C  CD1  . PHE   B 1 184 ? 62.149  90.411  15.341  1   68.12 ? 206 PHE   B CD1  1 
ATOM   4175 C  CD2  . PHE   B 1 184 ? 60.639  88.584  15.179  1   68.03 ? 206 PHE   B CD2  1 
ATOM   4176 C  CE1  . PHE   B 1 184 ? 63.173  89.603  14.861  1   68.58 ? 206 PHE   B CE1  1 
ATOM   4177 C  CE2  . PHE   B 1 184 ? 61.665  87.783  14.694  1   68.62 ? 206 PHE   B CE2  1 
ATOM   4178 C  CZ   . PHE   B 1 184 ? 62.924  88.298  14.538  1   68.26 ? 206 PHE   B CZ   1 
ATOM   4179 N  N    . TRP   B 1 185 ? 58.048  90.165  13.366  1   66.37 ? 207 TRP   B N    1 
ATOM   4180 C  CA   . TRP   B 1 185 ? 57.948  89.343  12.163  1   66.7  ? 207 TRP   B CA   1 
ATOM   4181 C  C    . TRP   B 1 185 ? 58      90.122  10.862  1   66.29 ? 207 TRP   B C    1 
ATOM   4182 O  O    . TRP   B 1 185 ? 58.742  89.73   9.962   1   66.52 ? 207 TRP   B O    1 
ATOM   4183 C  CB   . TRP   B 1 185 ? 56.716  88.435  12.202  1   67.34 ? 207 TRP   B CB   1 
ATOM   4184 C  CG   . TRP   B 1 185 ? 56.854  87.174  11.395  1   69.13 ? 207 TRP   B CG   1 
ATOM   4185 C  CD1  . TRP   B 1 185 ? 56.07   86.781  10.351  1   70.38 ? 207 TRP   B CD1  1 
ATOM   4186 C  CD2  . TRP   B 1 185 ? 57.822  86.126  11.587  1   69.92 ? 207 TRP   B CD2  1 
ATOM   4187 N  NE1  . TRP   B 1 185 ? 56.476  85.55   9.889   1   70.95 ? 207 TRP   B NE1  1 
ATOM   4188 C  CE2  . TRP   B 1 185 ? 57.561  85.134  10.619  1   70.9  ? 207 TRP   B CE2  1 
ATOM   4189 C  CE3  . TRP   B 1 185 ? 58.89   85.934  12.477  1   70.61 ? 207 TRP   B CE3  1 
ATOM   4190 C  CZ2  . TRP   B 1 185 ? 58.324  83.971  10.521  1   71.75 ? 207 TRP   B CZ2  1 
ATOM   4191 C  CZ3  . TRP   B 1 185 ? 59.635  84.777  12.383  1   71.6  ? 207 TRP   B CZ3  1 
ATOM   4192 C  CH2  . TRP   B 1 185 ? 59.362  83.821  11.404  1   71.86 ? 207 TRP   B CH2  1 
ATOM   4193 N  N    . ALA   B 1 186 ? 57.264  91.241  10.772  1   65.44 ? 208 ALA   B N    1 
ATOM   4194 C  CA   . ALA   B 1 186 ? 57.251  92.054  9.563   1   65    ? 208 ALA   B CA   1 
ATOM   4195 C  C    . ALA   B 1 186 ? 58.602  92.721  9.332   1   64.09 ? 208 ALA   B C    1 
ATOM   4196 O  O    . ALA   B 1 186 ? 59.108  92.68   8.21    1   64.23 ? 208 ALA   B O    1 
ATOM   4197 C  CB   . ALA   B 1 186 ? 56.145  93.095  9.642   1   65.34 ? 208 ALA   B CB   1 
ATOM   4198 N  N    . LYS   B 1 187 ? 59.213  93.288  10.397  1   63.06 ? 209 LYS   B N    1 
ATOM   4199 C  CA   . LYS   B 1 187 ? 60.526  93.932  10.297  1   62.72 ? 209 LYS   B CA   1 
ATOM   4200 C  C    . LYS   B 1 187 ? 61.595  92.938  9.831   1   62.41 ? 209 LYS   B C    1 
ATOM   4201 O  O    . LYS   B 1 187 ? 62.451  93.28   9.014   1   62.42 ? 209 LYS   B O    1 
ATOM   4202 C  CB   . LYS   B 1 187 ? 60.927  94.542  11.642  1   64.34 ? 209 LYS   B CB   1 
ATOM   4203 N  N    . PHE   B 1 188 ? 61.521  91.701  10.346  1   61.91 ? 210 PHE   B N    1 
ATOM   4204 C  CA   . PHE   B 1 188 ? 62.419  90.6    10.014  1   61.56 ? 210 PHE   B CA   1 
ATOM   4205 C  C    . PHE   B 1 188 ? 62.328  90.295  8.512   1   61.1  ? 210 PHE   B C    1 
ATOM   4206 O  O    . PHE   B 1 188 ? 63.368  90.238  7.852   1   61    ? 210 PHE   B O    1 
ATOM   4207 C  CB   . PHE   B 1 188 ? 62.087  89.381  10.909  1   61.41 ? 210 PHE   B CB   1 
ATOM   4208 C  CG   . PHE   B 1 188 ? 62.786  88.064  10.65   1   61.7  ? 210 PHE   B CG   1 
ATOM   4209 C  CD1  . PHE   B 1 188 ? 64.095  88.028  10.198  1   62.33 ? 210 PHE   B CD1  1 
ATOM   4210 C  CD2  . PHE   B 1 188 ? 62.156  86.864  10.925  1   62.39 ? 210 PHE   B CD2  1 
ATOM   4211 C  CE1  . PHE   B 1 188 ? 64.724  86.819  9.939   1   62.96 ? 210 PHE   B CE1  1 
ATOM   4212 C  CE2  . PHE   B 1 188 ? 62.799  85.656  10.7    1   63.14 ? 210 PHE   B CE2  1 
ATOM   4213 C  CZ   . PHE   B 1 188 ? 64.081  85.64   10.211  1   62.93 ? 210 PHE   B CZ   1 
ATOM   4214 N  N    . GLN   B 1 189 ? 61.102  90.209  7.952   1   60.6  ? 211 GLN   B N    1 
ATOM   4215 C  CA   . GLN   B 1 189 ? 60.915  89.964  6.511   1   60.44 ? 211 GLN   B CA   1 
ATOM   4216 C  C    . GLN   B 1 189 ? 61.543  91.062  5.652   1   60.1  ? 211 GLN   B C    1 
ATOM   4217 O  O    . GLN   B 1 189 ? 62.201  90.752  4.656   1   59.83 ? 211 GLN   B O    1 
ATOM   4218 C  CB   . GLN   B 1 189 ? 59.435  89.785  6.154   1   61.61 ? 211 GLN   B CB   1 
ATOM   4219 C  CG   . GLN   B 1 189 ? 58.759  88.726  6.997   1   63.96 ? 211 GLN   B CG   1 
ATOM   4220 C  CD   . GLN   B 1 189 ? 57.365  88.394  6.552   1   67.29 ? 211 GLN   B CD   1 
ATOM   4221 O  OE1  . GLN   B 1 189 ? 56.407  88.448  7.343   1   68.3  ? 211 GLN   B OE1  1 
ATOM   4222 N  NE2  . GLN   B 1 189 ? 57.226  88.019  5.282   1   67.36 ? 211 GLN   B NE2  1 
ATOM   4223 N  N    . GLU   B 1 190 ? 61.393  92.333  6.068   1   59.99 ? 212 GLU   B N    1 
ATOM   4224 C  CA   . GLU   B 1 190 ? 61.973  93.466  5.346   1   60.81 ? 212 GLU   B CA   1 
ATOM   4225 C  C    . GLU   B 1 190 ? 63.494  93.411  5.411   1   61.62 ? 212 GLU   B C    1 
ATOM   4226 O  O    . GLU   B 1 190 ? 64.163  93.625  4.393   1   61.61 ? 212 GLU   B O    1 
ATOM   4227 C  CB   . GLU   B 1 190 ? 61.464  94.802  5.91    1   62.87 ? 212 GLU   B CB   1 
ATOM   4228 C  CG   . GLU   B 1 190 ? 61.908  96.012  5.104   1   67    ? 212 GLU   B CG   1 
ATOM   4229 N  N    . SER   B 1 191 ? 64.044  93.077  6.607   1   61.8  ? 213 SER   B N    1 
ATOM   4230 C  CA   . SER   B 1 191 ? 65.485  92.951  6.819   1   62.11 ? 213 SER   B CA   1 
ATOM   4231 C  C    . SER   B 1 191 ? 66.067  91.853  5.949   1   62.31 ? 213 SER   B C    1 
ATOM   4232 O  O    . SER   B 1 191 ? 67.155  92.023  5.403   1   62.05 ? 213 SER   B O    1 
ATOM   4233 C  CB   . SER   B 1 191 ? 65.785  92.667  8.281   1   63.58 ? 213 SER   B CB   1 
ATOM   4234 O  OG   . SER   B 1 191 ? 65.692  93.848  9.057   1   65.95 ? 213 SER   B OG   1 
ATOM   4235 N  N    . VAL   B 1 192 ? 65.338  90.738  5.798   1   62.67 ? 214 VAL   B N    1 
ATOM   4236 C  CA   . VAL   B 1 192 ? 65.775  89.641  4.947   1   63.72 ? 214 VAL   B CA   1 
ATOM   4237 C  C    . VAL   B 1 192 ? 65.84   90.103  3.49    1   64.92 ? 214 VAL   B C    1 
ATOM   4238 O  O    . VAL   B 1 192 ? 66.829  89.835  2.813   1   65.09 ? 214 VAL   B O    1 
ATOM   4239 C  CB   . VAL   B 1 192 ? 64.904  88.374  5.141   1   64.41 ? 214 VAL   B CB   1 
ATOM   4240 C  CG1  . VAL   B 1 192 ? 65.159  87.352  4.041   1   64.85 ? 214 VAL   B CG1  1 
ATOM   4241 C  CG2  . VAL   B 1 192 ? 65.162  87.749  6.504   1   65.09 ? 214 VAL   B CG2  1 
ATOM   4242 N  N    . ASP   B 1 193 ? 64.81   90.834  3.018   1   65.59 ? 215 ASP   B N    1 
ATOM   4243 C  CA   . ASP   B 1 193 ? 64.797  91.347  1.643   1   66.16 ? 215 ASP   B CA   1 
ATOM   4244 C  C    . ASP   B 1 193 ? 65.956  92.307  1.422   1   66.18 ? 215 ASP   B C    1 
ATOM   4245 O  O    . ASP   B 1 193 ? 66.718  92.112  0.49    1   65.97 ? 215 ASP   B O    1 
ATOM   4246 C  CB   . ASP   B 1 193 ? 63.46   92.027  1.303   1   68.01 ? 215 ASP   B CB   1 
ATOM   4247 C  CG   . ASP   B 1 193 ? 62.305  91.065  1.165   1   72.78 ? 215 ASP   B CG   1 
ATOM   4248 O  OD1  . ASP   B 1 193 ? 62.542  89.91   0.728   1   73.73 ? 215 ASP   B OD1  1 
ATOM   4249 O  OD2  . ASP   B 1 193 ? 61.159  91.463  1.494   1   74.71 ? 215 ASP   B OD2  1 
ATOM   4250 N  N    . ARG   B 1 194 ? 66.138  93.286  2.315   1   66.54 ? 216 ARG   B N    1 
ATOM   4251 C  CA   . ARG   B 1 194 ? 67.224  94.25   2.198   1   67.73 ? 216 ARG   B CA   1 
ATOM   4252 C  C    . ARG   B 1 194 ? 68.589  93.564  2.219   1   69.16 ? 216 ARG   B C    1 
ATOM   4253 O  O    . ARG   B 1 194 ? 69.426  93.852  1.363   1   69.18 ? 216 ARG   B O    1 
ATOM   4254 C  CB   . ARG   B 1 194 ? 67.117  95.316  3.297   1   68.91 ? 216 ARG   B CB   1 
ATOM   4255 N  N    . PHE   B 1 195 ? 68.789  92.616  3.161   1   70.12 ? 217 PHE   B N    1 
ATOM   4256 C  CA   . PHE   B 1 195 ? 70.032  91.856  3.302   1   71.32 ? 217 PHE   B CA   1 
ATOM   4257 C  C    . PHE   B 1 195 ? 70.331  91.007  2.058   1   72.01 ? 217 PHE   B C    1 
ATOM   4258 O  O    . PHE   B 1 195 ? 71.436  91.083  1.525   1   72.13 ? 217 PHE   B O    1 
ATOM   4259 C  CB   . PHE   B 1 195 ? 70.008  90.985  4.586   1   71.6  ? 217 PHE   B CB   1 
ATOM   4260 C  CG   . PHE   B 1 195 ? 71.171  90.028  4.719   1   72.39 ? 217 PHE   B CG   1 
ATOM   4261 C  CD1  . PHE   B 1 195 ? 72.436  90.489  5.039   1   73.16 ? 217 PHE   B CD1  1 
ATOM   4262 C  CD2  . PHE   B 1 195 ? 71.008  88.675  4.475   1   73.13 ? 217 PHE   B CD2  1 
ATOM   4263 C  CE1  . PHE   B 1 195 ? 73.513  89.617  5.106   1   73.82 ? 217 PHE   B CE1  1 
ATOM   4264 C  CE2  . PHE   B 1 195 ? 72.087  87.804  4.55    1   73.75 ? 217 PHE   B CE2  1 
ATOM   4265 C  CZ   . PHE   B 1 195 ? 73.329  88.28   4.872   1   73.57 ? 217 PHE   B CZ   1 
ATOM   4266 N  N    . LEU   B 1 196 ? 69.351  90.208  1.597   1   72.32 ? 218 LEU   B N    1 
ATOM   4267 C  CA   . LEU   B 1 196 ? 69.522  89.351  0.426   1   73.31 ? 218 LEU   B CA   1 
ATOM   4268 C  C    . LEU   B 1 196 ? 69.699  90.148  -0.869  1   74.47 ? 218 LEU   B C    1 
ATOM   4269 O  O    . LEU   B 1 196 ? 70.513  89.756  -1.703  1   74.55 ? 218 LEU   B O    1 
ATOM   4270 C  CB   . LEU   B 1 196 ? 68.372  88.343  0.303   1   73.42 ? 218 LEU   B CB   1 
ATOM   4271 N  N    . GLU   B 1 197 ? 68.999  91.291  -1.014  1   75.24 ? 219 GLU   B N    1 
ATOM   4272 C  CA   . GLU   B 1 197 ? 69.119  92.151  -2.199  1   76.64 ? 219 GLU   B CA   1 
ATOM   4273 C  C    . GLU   B 1 197 ? 70.539  92.693  -2.302  1   77.8  ? 219 GLU   B C    1 
ATOM   4274 O  O    . GLU   B 1 197 ? 71.107  92.698  -3.392  1   77.86 ? 219 GLU   B O    1 
ATOM   4275 C  CB   . GLU   B 1 197 ? 68.105  93.311  -2.171  1   78.79 ? 219 GLU   B CB   1 
ATOM   4276 N  N    . ALA   B 1 198 ? 71.126  93.097  -1.159  1   78.44 ? 220 ALA   B N    1 
ATOM   4277 C  CA   . ALA   B 1 198 ? 72.504  93.581  -1.086  1   79.46 ? 220 ALA   B CA   1 
ATOM   4278 C  C    . ALA   B 1 198 ? 73.486  92.456  -1.421  1   80.43 ? 220 ALA   B C    1 
ATOM   4279 O  O    . ALA   B 1 198 ? 74.494  92.701  -2.082  1   80.46 ? 220 ALA   B O    1 
ATOM   4280 C  CB   . ALA   B 1 198 ? 72.793  94.122  0.305   1   79.64 ? 220 ALA   B CB   1 
ATOM   4281 N  N    . GLN   B 1 199 ? 73.183  91.222  -0.981  1   81.03 ? 221 GLN   B N    1 
ATOM   4282 C  CA   . GLN   B 1 199 ? 74.013  90.058  -1.275  1   82.1  ? 221 GLN   B CA   1 
ATOM   4283 C  C    . GLN   B 1 199 ? 74.033  89.793  -2.78   1   82.95 ? 221 GLN   B C    1 
ATOM   4284 O  O    . GLN   B 1 199 ? 75.082  89.448  -3.319  1   82.91 ? 221 GLN   B O    1 
ATOM   4285 C  CB   . GLN   B 1 199 ? 73.519  88.805  -0.517  1   83.5  ? 221 GLN   B CB   1 
ATOM   4286 C  CG   . GLN   B 1 199 ? 73.789  88.809  0.987   1   85.6  ? 221 GLN   B CG   1 
ATOM   4287 C  CD   . GLN   B 1 199 ? 75.254  88.972  1.311   1   88.49 ? 221 GLN   B CD   1 
ATOM   4288 O  OE1  . GLN   B 1 199 ? 75.654  89.9    2.025   1   89.9  ? 221 GLN   B OE1  1 
ATOM   4289 N  NE2  . GLN   B 1 199 ? 76.085  88.08   0.786   1   88.33 ? 221 GLN   B NE2  1 
ATOM   4290 N  N    . VAL   B 1 200 ? 72.877  89.96   -3.455  1   83.6  ? 222 VAL   B N    1 
ATOM   4291 C  CA   . VAL   B 1 200 ? 72.756  89.772  -4.903  1   84.7  ? 222 VAL   B CA   1 
ATOM   4292 C  C    . VAL   B 1 200 ? 73.579  90.821  -5.654  1   85.6  ? 222 VAL   B C    1 
ATOM   4293 O  O    . VAL   B 1 200 ? 74.33   90.467  -6.562  1   85.46 ? 222 VAL   B O    1 
ATOM   4294 C  CB   . VAL   B 1 200 ? 71.282  89.753  -5.371  1   85.32 ? 222 VAL   B CB   1 
ATOM   4295 N  N    . GLN   B 1 201 ? 73.489  92.096  -5.231  1   86.25 ? 223 GLN   B N    1 
ATOM   4296 C  CA   . GLN   B 1 201 ? 74.241  93.196  -5.837  1   87.4  ? 223 GLN   B CA   1 
ATOM   4297 C  C    . GLN   B 1 201 ? 75.749  93.002  -5.664  1   88.68 ? 223 GLN   B C    1 
ATOM   4298 O  O    . GLN   B 1 201 ? 76.516  93.314  -6.575  1   88.94 ? 223 GLN   B O    1 
ATOM   4299 C  CB   . GLN   B 1 201 ? 73.8    94.548  -5.252  1   88.61 ? 223 GLN   B CB   1 
ATOM   4300 N  N    . SER   B 1 202 ? 76.171  92.456  -4.511  1   89.22 ? 224 SER   B N    1 
ATOM   4301 C  CA   . SER   B 1 202 ? 77.582  92.197  -4.239  1   90.02 ? 224 SER   B CA   1 
ATOM   4302 C  C    . SER   B 1 202 ? 78.093  90.986  -5.033  1   90.8  ? 224 SER   B C    1 
ATOM   4303 O  O    . SER   B 1 202 ? 79.246  90.983  -5.472  1   91.19 ? 224 SER   B O    1 
ATOM   4304 C  CB   . SER   B 1 202 ? 77.807  91.988  -2.745  1   91.12 ? 224 SER   B CB   1 
ATOM   4305 N  N    . ALA   B 1 203 ? 77.236  89.97   -5.233  1   90.89 ? 225 ALA   B N    1 
ATOM   4306 C  CA   . ALA   B 1 203 ? 77.595  88.762  -5.983  1   91.62 ? 225 ALA   B CA   1 
ATOM   4307 C  C    . ALA   B 1 203 ? 77.855  89.048  -7.465  1   92.02 ? 225 ALA   B C    1 
ATOM   4308 O  O    . ALA   B 1 203 ? 78.686  88.384  -8.082  1   92.07 ? 225 ALA   B O    1 
ATOM   4309 C  CB   . ALA   B 1 203 ? 76.498  87.717  -5.85   1   91.83 ? 225 ALA   B CB   1 
ATOM   4310 N  N    . MET   B 1 204 ? 77.134  90.029  -8.031  1   92.05 ? 226 MET   B N    1 
ATOM   4311 C  CA   . MET   B 1 204 ? 77.274  90.415  -9.432  1   92.48 ? 226 MET   B CA   1 
ATOM   4312 C  C    . MET   B 1 204 ? 78.657  91.013  -9.729  1   93.04 ? 226 MET   B C    1 
ATOM   4313 O  O    . MET   B 1 204 ? 79.182  90.83   -10.826 1   93.25 ? 226 MET   B O    1 
ATOM   4314 C  CB   . MET   B 1 204 ? 76.162  91.399  -9.833  1   92.8  ? 226 MET   B CB   1 
ATOM   4315 C  CG   . MET   B 1 204 ? 74.774  90.801  -9.781  1   94.43 ? 226 MET   B CG   1 
ATOM   4316 N  N    . GLU   B 1 205 ? 79.266  91.687  -8.745  1   93.07 ? 227 GLU   B N    1 
ATOM   4317 C  CA   . GLU   B 1 205 ? 80.575  92.311  -8.918  1   93.65 ? 227 GLU   B CA   1 
ATOM   4318 C  C    . GLU   B 1 205 ? 81.76   91.331  -8.923  1   94.3  ? 227 GLU   B C    1 
ATOM   4319 O  O    . GLU   B 1 205 ? 82.884  91.76   -9.174  1   94.52 ? 227 GLU   B O    1 
ATOM   4320 C  CB   . GLU   B 1 205 ? 80.785  93.409  -7.863  1   95.36 ? 227 GLU   B CB   1 
ATOM   4321 N  N    . GLU   B 1 206 ? 81.523  90.034  -8.656  1   94.48 ? 228 GLU   B N    1 
ATOM   4322 C  CA   . GLU   B 1 206 ? 82.586  89.022  -8.617  1   95.14 ? 228 GLU   B CA   1 
ATOM   4323 C  C    . GLU   B 1 206 ? 83.337  88.878  -9.952  1   95.44 ? 228 GLU   B C    1 
ATOM   4324 O  O    . GLU   B 1 206 ? 82.714  88.809  -11.009 1   95.51 ? 228 GLU   B O    1 
ATOM   4325 C  CB   . GLU   B 1 206 ? 82.027  87.663  -8.156  1   97.38 ? 228 GLU   B CB   1 
ATOM   4326 N  N    . PRO   B 1 207 ? 84.68   88.849  -9.921  1   95.43 ? 229 PRO   B N    1 
ATOM   4327 C  CA   . PRO   B 1 207 ? 85.434  88.727  -11.177 1   95.5  ? 229 PRO   B CA   1 
ATOM   4328 C  C    . PRO   B 1 207 ? 85.317  87.337  -11.802 1   95.62 ? 229 PRO   B C    1 
ATOM   4329 O  O    . PRO   B 1 207 ? 85.031  87.235  -12.993 1   95.95 ? 229 PRO   B O    1 
ATOM   4330 C  CB   . PRO   B 1 207 ? 86.879  89.082  -10.779 1   96.21 ? 229 PRO   B CB   1 
ATOM   4331 C  CG   . PRO   B 1 207 ? 86.817  89.535  -9.343  1   96.63 ? 229 PRO   B CG   1 
ATOM   4332 C  CD   . PRO   B 1 207 ? 85.577  88.939  -8.756  1   95.02 ? 229 PRO   B CD   1 
ATOM   4333 N  N    . VAL   B 1 208 ? 85.51   86.273  -11.008 1   95.21 ? 230 VAL   B N    1 
ATOM   4334 C  CA   . VAL   B 1 208 ? 85.397  84.91   -11.519 1   95.37 ? 230 VAL   B CA   1 
ATOM   4335 C  C    . VAL   B 1 208 ? 83.925  84.552  -11.683 1   95.13 ? 230 VAL   B C    1 
ATOM   4336 O  O    . VAL   B 1 208 ? 83.125  84.835  -10.79  1   95.18 ? 230 VAL   B O    1 
ATOM   4337 C  CB   . VAL   B 1 208 ? 86.134  83.896  -10.617 1   96.17 ? 230 VAL   B CB   1 
ATOM   4338 N  N    . GLU   B 1 209 ? 83.56   83.963  -12.833 1   94.66 ? 231 GLU   B N    1 
ATOM   4339 C  CA   . GLU   B 1 209 ? 82.174  83.596  -13.118 1   94.73 ? 231 GLU   B CA   1 
ATOM   4340 C  C    . GLU   B 1 209 ? 81.691  82.416  -12.279 1   94.47 ? 231 GLU   B C    1 
ATOM   4341 O  O    . GLU   B 1 209 ? 80.511  82.357  -11.93  1   94.6  ? 231 GLU   B O    1 
ATOM   4342 C  CB   . GLU   B 1 209 ? 81.975  83.325  -14.617 1   96.8  ? 231 GLU   B CB   1 
ATOM   4343 N  N    . LYS   B 1 210 ? 82.598  81.49   -11.94  1   93.9  ? 232 LYS   B N    1 
ATOM   4344 C  CA   . LYS   B 1 210 ? 82.257  80.333  -11.112 1   93.85 ? 232 LYS   B CA   1 
ATOM   4345 C  C    . LYS   B 1 210 ? 81.891  80.78   -9.686  1   93.55 ? 232 LYS   B C    1 
ATOM   4346 O  O    . LYS   B 1 210 ? 80.966  80.226  -9.083  1   93.91 ? 232 LYS   B O    1 
ATOM   4347 C  CB   . LYS   B 1 210 ? 83.422  79.333  -11.082 1   95.59 ? 232 LYS   B CB   1 
ATOM   4348 N  N    . ALA   B 1 211 ? 82.599  81.804  -9.166  1   92.57 ? 233 ALA   B N    1 
ATOM   4349 C  CA   . ALA   B 1 211 ? 82.365  82.364  -7.833  1   91.87 ? 233 ALA   B CA   1 
ATOM   4350 C  C    . ALA   B 1 211 ? 81.071  83.187  -7.783  1   90.75 ? 233 ALA   B C    1 
ATOM   4351 O  O    . ALA   B 1 211 ? 80.374  83.177  -6.766  1   90.82 ? 233 ALA   B O    1 
ATOM   4352 C  CB   . ALA   B 1 211 ? 83.55   83.224  -7.418  1   92.02 ? 233 ALA   B CB   1 
ATOM   4353 N  N    . LYS   B 1 212 ? 80.751  83.897  -8.879  1   89.44 ? 234 LYS   B N    1 
ATOM   4354 C  CA   . LYS   B 1 212 ? 79.531  84.697  -8.966  1   88.51 ? 234 LYS   B CA   1 
ATOM   4355 C  C    . LYS   B 1 212 ? 78.296  83.789  -8.941  1   87.08 ? 234 LYS   B C    1 
ATOM   4356 O  O    . LYS   B 1 212 ? 77.3    84.112  -8.293  1   86.93 ? 234 LYS   B O    1 
ATOM   4357 C  CB   . LYS   B 1 212 ? 79.536  85.536  -10.252 1   90.23 ? 234 LYS   B CB   1 
ATOM   4358 N  N    . ASN   B 1 213 ? 78.378  82.646  -9.641  1   85.84 ? 235 ASN   B N    1 
ATOM   4359 C  CA   . ASN   B 1 213 ? 77.29   81.683  -9.728  1   85.08 ? 235 ASN   B CA   1 
ATOM   4360 C  C    . ASN   B 1 213 ? 77.078  80.939  -8.42   1   83.88 ? 235 ASN   B C    1 
ATOM   4361 O  O    . ASN   B 1 213 ? 75.932  80.691  -8.068  1   83.85 ? 235 ASN   B O    1 
ATOM   4362 C  CB   . ASN   B 1 213 ? 77.51   80.708  -10.887 1   86.2  ? 235 ASN   B CB   1 
ATOM   4363 N  N    . TYR   B 1 214 ? 78.159  80.61   -7.679  1   82.71 ? 236 TYR   B N    1 
ATOM   4364 C  CA   . TYR   B 1 214 ? 78.022  79.92   -6.39   1   81.89 ? 236 TYR   B CA   1 
ATOM   4365 C  C    . TYR   B 1 214 ? 77.247  80.784  -5.405  1   80.02 ? 236 TYR   B C    1 
ATOM   4366 O  O    . TYR   B 1 214 ? 76.358  80.282  -4.721  1   79.69 ? 236 TYR   B O    1 
ATOM   4367 C  CB   . TYR   B 1 214 ? 79.389  79.531  -5.795  1   82.38 ? 236 TYR   B CB   1 
ATOM   4368 C  CG   . TYR   B 1 214 ? 79.278  78.665  -4.552  1   83.62 ? 236 TYR   B CG   1 
ATOM   4369 C  CD1  . TYR   B 1 214 ? 79.233  79.232  -3.283  1   84.51 ? 236 TYR   B CD1  1 
ATOM   4370 C  CD2  . TYR   B 1 214 ? 79.223  77.282  -4.645  1   84.63 ? 236 TYR   B CD2  1 
ATOM   4371 C  CE1  . TYR   B 1 214 ? 79.102  78.445  -2.144  1   85.41 ? 236 TYR   B CE1  1 
ATOM   4372 C  CE2  . TYR   B 1 214 ? 79.104  76.484  -3.512  1   85.57 ? 236 TYR   B CE2  1 
ATOM   4373 C  CZ   . TYR   B 1 214 ? 79.041  77.07   -2.262  1   86.37 ? 236 TYR   B CZ   1 
ATOM   4374 O  OH   . TYR   B 1 214 ? 78.934  76.284  -1.141  1   87.84 ? 236 TYR   B OH   1 
ATOM   4375 N  N    . ARG   B 1 215 ? 77.563  82.085  -5.365  1   78.8  ? 237 ARG   B N    1 
ATOM   4376 C  CA   . ARG   B 1 215 ? 76.892  83.037  -4.487  1   78.28 ? 237 ARG   B CA   1 
ATOM   4377 C  C    . ARG   B 1 215 ? 75.431  83.23   -4.86   1   78.03 ? 237 ARG   B C    1 
ATOM   4378 O  O    . ARG   B 1 215 ? 74.589  83.266  -3.97   1   78.14 ? 237 ARG   B O    1 
ATOM   4379 C  CB   . ARG   B 1 215 ? 77.628  84.374  -4.47   1   78.92 ? 237 ARG   B CB   1 
ATOM   4380 C  CG   . ARG   B 1 215 ? 78.965  84.302  -3.752  1   80.43 ? 237 ARG   B CG   1 
ATOM   4381 C  CD   . ARG   B 1 215 ? 79.566  85.671  -3.537  1   82.16 ? 237 ARG   B CD   1 
ATOM   4382 N  NE   . ARG   B 1 215 ? 78.655  86.577  -2.828  1   83.56 ? 237 ARG   B NE   1 
ATOM   4383 C  CZ   . ARG   B 1 215 ? 78.942  87.839  -2.526  1   84.75 ? 237 ARG   B CZ   1 
ATOM   4384 N  NH1  . ARG   B 1 215 ? 80.119  88.359  -2.857  1   84.33 ? 237 ARG   B NH1  1 
ATOM   4385 N  NH2  . ARG   B 1 215 ? 78.055  88.592  -1.888  1   84.05 ? 237 ARG   B NH2  1 
ATOM   4386 N  N    . LEU   B 1 216 ? 75.113  83.305  -6.167  1   77.37 ? 238 LEU   B N    1 
ATOM   4387 C  CA   . LEU   B 1 216 ? 73.723  83.431  -6.612  1   76.81 ? 238 LEU   B CA   1 
ATOM   4388 C  C    . LEU   B 1 216 ? 72.94   82.153  -6.285  1   75.81 ? 238 LEU   B C    1 
ATOM   4389 O  O    . LEU   B 1 216 ? 71.767  82.235  -5.932  1   76.23 ? 238 LEU   B O    1 
ATOM   4390 C  CB   . LEU   B 1 216 ? 73.65   83.737  -8.113  1   77.19 ? 238 LEU   B CB   1 
ATOM   4391 N  N    . MET   B 1 217 ? 73.59   80.981  -6.383  1   74.41 ? 239 MET   B N    1 
ATOM   4392 C  CA   . MET   B 1 217 ? 72.977  79.699  -6.042  1   73.75 ? 239 MET   B CA   1 
ATOM   4393 C  C    . MET   B 1 217 ? 72.698  79.668  -4.537  1   72.71 ? 239 MET   B C    1 
ATOM   4394 O  O    . MET   B 1 217 ? 71.615  79.249  -4.117  1   72.9  ? 239 MET   B O    1 
ATOM   4395 C  CB   . MET   B 1 217 ? 73.904  78.532  -6.452  1   74.61 ? 239 MET   B CB   1 
ATOM   4396 C  CG   . MET   B 1 217 ? 73.404  77.158  -6.034  1   77.23 ? 239 MET   B CG   1 
ATOM   4397 S  SD   . MET   B 1 217 ? 73.856  76.659  -4.336  1   80.45 ? 239 MET   B SD   1 
ATOM   4398 C  CE   . MET   B 1 217 ? 75.615  76.696  -4.451  1   77.8  ? 239 MET   B CE   1 
ATOM   4399 N  N    . ASP   B 1 218 ? 73.671  80.125  -3.728  1   71.34 ? 240 ASP   B N    1 
ATOM   4400 C  CA   . ASP   B 1 218 ? 73.544  80.16   -2.28   1   70.21 ? 240 ASP   B CA   1 
ATOM   4401 C  C    . ASP   B 1 218 ? 72.431  81.1    -1.84   1   68.5  ? 240 ASP   B C    1 
ATOM   4402 O  O    . ASP   B 1 218 ? 71.666  80.74   -0.944  1   68.46 ? 240 ASP   B O    1 
ATOM   4403 C  CB   . ASP   B 1 218 ? 74.873  80.533  -1.616  1   72.23 ? 240 ASP   B CB   1 
ATOM   4404 C  CG   . ASP   B 1 218 ? 74.792  80.498  -0.103  1   77.39 ? 240 ASP   B CG   1 
ATOM   4405 O  OD1  . ASP   B 1 218 ? 74.461  79.423  0.452   1   77.71 ? 240 ASP   B OD1  1 
ATOM   4406 O  OD2  . ASP   B 1 218 ? 75.04   81.549  0.529   1   79.91 ? 240 ASP   B OD2  1 
ATOM   4407 N  N    . ILE   B 1 219 ? 72.311  82.281  -2.485  1   66.94 ? 241 ILE   B N    1 
ATOM   4408 C  CA   . ILE   B 1 219 ? 71.257  83.251  -2.173  1   65.92 ? 241 ILE   B CA   1 
ATOM   4409 C  C    . ILE   B 1 219 ? 69.865  82.651  -2.444  1   64.52 ? 241 ILE   B C    1 
ATOM   4410 O  O    . ILE   B 1 219 ? 68.932  82.884  -1.669  1   64.42 ? 241 ILE   B O    1 
ATOM   4411 C  CB   . ILE   B 1 219 ? 71.492  84.593  -2.91   1   66.5  ? 241 ILE   B CB   1 
ATOM   4412 C  CG1  . ILE   B 1 219 ? 72.775  85.274  -2.399  1   67.58 ? 241 ILE   B CG1  1 
ATOM   4413 C  CG2  . ILE   B 1 219 ? 70.295  85.536  -2.764  1   66.69 ? 241 ILE   B CG2  1 
ATOM   4414 C  CD1  . ILE   B 1 219 ? 73.304  86.327  -3.296  1   68.72 ? 241 ILE   B CD1  1 
ATOM   4415 N  N    . GLU   B 1 220 ? 69.745  81.818  -3.493  1   63.12 ? 242 GLU   B N    1 
ATOM   4416 C  CA   . GLU   B 1 220 ? 68.488  81.135  -3.792  1   62.36 ? 242 GLU   B CA   1 
ATOM   4417 C  C    . GLU   B 1 220 ? 68.16   80.12   -2.682  1   61.36 ? 242 GLU   B C    1 
ATOM   4418 O  O    . GLU   B 1 220 ? 67.01   80.062  -2.248  1   61.36 ? 242 GLU   B O    1 
ATOM   4419 C  CB   . GLU   B 1 220 ? 68.526  80.461  -5.173  1   64.28 ? 242 GLU   B CB   1 
ATOM   4420 N  N    . LYS   B 1 221 ? 69.178  79.379  -2.166  1   60.15 ? 243 LYS   B N    1 
ATOM   4421 C  CA   . LYS   B 1 221 ? 69.005  78.44   -1.044  1   59.16 ? 243 LYS   B CA   1 
ATOM   4422 C  C    . LYS   B 1 221 ? 68.453  79.192  0.176   1   58    ? 243 LYS   B C    1 
ATOM   4423 O  O    . LYS   B 1 221 ? 67.521  78.712  0.821   1   57.88 ? 243 LYS   B O    1 
ATOM   4424 C  CB   . LYS   B 1 221 ? 70.338  77.753  -0.676  1   60.38 ? 243 LYS   B CB   1 
ATOM   4425 C  CG   . LYS   B 1 221 ? 70.824  76.715  -1.68   1   62.89 ? 243 LYS   B CG   1 
ATOM   4426 C  CD   . LYS   B 1 221 ? 69.871  75.551  -1.751  1   66.1  ? 243 LYS   B CD   1 
ATOM   4427 C  CE   . LYS   B 1 221 ? 70.459  74.355  -2.441  1   69.15 ? 243 LYS   B CE   1 
ATOM   4428 N  NZ   . LYS   B 1 221 ? 69.415  73.336  -2.697  1   71.22 ? 243 LYS   B NZ   1 
ATOM   4429 N  N    . ARG   B 1 222 ? 68.979  80.409  0.434   1   57.22 ? 244 ARG   B N    1 
ATOM   4430 C  CA   . ARG   B 1 222 ? 68.516  81.277  1.523   1   57.07 ? 244 ARG   B CA   1 
ATOM   4431 C  C    . ARG   B 1 222 ? 67.053  81.672  1.339   1   57.24 ? 244 ARG   B C    1 
ATOM   4432 O  O    . ARG   B 1 222 ? 66.277  81.583  2.293   1   56.88 ? 244 ARG   B O    1 
ATOM   4433 C  CB   . ARG   B 1 222 ? 69.395  82.54   1.665   1   57.34 ? 244 ARG   B CB   1 
ATOM   4434 C  CG   . ARG   B 1 222 ? 70.866  82.266  2.003   1   59.01 ? 244 ARG   B CG   1 
ATOM   4435 C  CD   . ARG   B 1 222 ? 71.057  81.386  3.231   1   60.15 ? 244 ARG   B CD   1 
ATOM   4436 N  NE   . ARG   B 1 222 ? 70.48   81.987  4.432   1   62.05 ? 244 ARG   B NE   1 
ATOM   4437 C  CZ   . ARG   B 1 222 ? 70.012  81.3    5.472   1   62.56 ? 244 ARG   B CZ   1 
ATOM   4438 N  NH1  . ARG   B 1 222 ? 70.019  79.972  5.458   1   61.04 ? 244 ARG   B NH1  1 
ATOM   4439 N  NH2  . ARG   B 1 222 ? 69.516  81.936  6.524   1   61.54 ? 244 ARG   B NH2  1 
ATOM   4440 N  N    . ARG   B 1 223 ? 66.659  82.048  0.106   1   57.2  ? 245 ARG   B N    1 
ATOM   4441 C  CA   . ARG   B 1 223 ? 65.274  82.418  -0.206  1   57.55 ? 245 ARG   B CA   1 
ATOM   4442 C  C    . ARG   B 1 223 ? 64.316  81.254  0.05    1   57.48 ? 245 ARG   B C    1 
ATOM   4443 O  O    . ARG   B 1 223 ? 63.217  81.471  0.551   1   57.68 ? 245 ARG   B O    1 
ATOM   4444 C  CB   . ARG   B 1 223 ? 65.153  82.913  -1.656  1   58.93 ? 245 ARG   B CB   1 
ATOM   4445 N  N    . GLU   B 1 224 ? 64.738  80.018  -0.268  1   57.24 ? 246 GLU   B N    1 
ATOM   4446 C  CA   . GLU   B 1 224 ? 63.934  78.817  -0.014  1   57.53 ? 246 GLU   B CA   1 
ATOM   4447 C  C    . GLU   B 1 224 ? 63.799  78.58   1.506   1   57.73 ? 246 GLU   B C    1 
ATOM   4448 O  O    . GLU   B 1 224 ? 62.726  78.177  1.975   1   57.64 ? 246 GLU   B O    1 
ATOM   4449 C  CB   . GLU   B 1 224 ? 64.559  77.581  -0.693  1   59.43 ? 246 GLU   B CB   1 
ATOM   4450 C  CG   . GLU   B 1 224 ? 64.679  77.677  -2.204  1   63.4  ? 246 GLU   B CG   1 
ATOM   4451 N  N    . VAL   B 1 225 ? 64.879  78.865  2.277   1   57.38 ? 247 VAL   B N    1 
ATOM   4452 C  CA   . VAL   B 1 225 ? 64.869  78.747  3.738   1   57.26 ? 247 VAL   B CA   1 
ATOM   4453 C  C    . VAL   B 1 225 ? 63.843  79.733  4.31    1   57.25 ? 247 VAL   B C    1 
ATOM   4454 O  O    . VAL   B 1 225 ? 63.016  79.353  5.145   1   56.93 ? 247 VAL   B O    1 
ATOM   4455 C  CB   . VAL   B 1 225 ? 66.29   78.975  4.339   1   57.71 ? 247 VAL   B CB   1 
ATOM   4456 C  CG1  . VAL   B 1 225 ? 66.239  79.289  5.832   1   57.96 ? 247 VAL   B CG1  1 
ATOM   4457 C  CG2  . VAL   B 1 225 ? 67.188  77.782  4.08    1   58.03 ? 247 VAL   B CG2  1 
ATOM   4458 N  N    . TYR   B 1 226 ? 63.884  80.994  3.841   1   57.21 ? 248 TYR   B N    1 
ATOM   4459 C  CA   . TYR   B 1 226 ? 62.97   82.017  4.336   1   57.4  ? 248 TYR   B CA   1 
ATOM   4460 C  C    . TYR   B 1 226 ? 61.539  81.802  3.889   1   57.92 ? 248 TYR   B C    1 
ATOM   4461 O  O    . TYR   B 1 226 ? 60.639  82.168  4.63    1   58.13 ? 248 TYR   B O    1 
ATOM   4462 C  CB   . TYR   B 1 226 ? 63.473  83.416  4.017   1   57.23 ? 248 TYR   B CB   1 
ATOM   4463 C  CG   . TYR   B 1 226 ? 64.683  83.719  4.867   1   57.92 ? 248 TYR   B CG   1 
ATOM   4464 C  CD1  . TYR   B 1 226 ? 64.585  83.777  6.25    1   58.58 ? 248 TYR   B CD1  1 
ATOM   4465 C  CD2  . TYR   B 1 226 ? 65.943  83.819  4.302   1   58.74 ? 248 TYR   B CD2  1 
ATOM   4466 C  CE1  . TYR   B 1 226 ? 65.702  83.99   7.042   1   59.37 ? 248 TYR   B CE1  1 
ATOM   4467 C  CE2  . TYR   B 1 226 ? 67.07   84.008  5.083   1   59.63 ? 248 TYR   B CE2  1 
ATOM   4468 C  CZ   . TYR   B 1 226 ? 66.945  84.1    6.454   1   60.4  ? 248 TYR   B CZ   1 
ATOM   4469 O  OH   . TYR   B 1 226 ? 68.061  84.301  7.218   1   61.98 ? 248 TYR   B OH   1 
ATOM   4470 N  N    . ARG   B 1 227 ? 61.313  81.142  2.74    1   58.06 ? 249 ARG   B N    1 
ATOM   4471 C  CA   . ARG   B 1 227 ? 59.952  80.817  2.313   1   58.87 ? 249 ARG   B CA   1 
ATOM   4472 C  C    . ARG   B 1 227 ? 59.334  79.817  3.296   1   59.27 ? 249 ARG   B C    1 
ATOM   4473 O  O    . ARG   B 1 227 ? 58.151  79.922  3.601   1   59.61 ? 249 ARG   B O    1 
ATOM   4474 C  CB   . ARG   B 1 227 ? 59.943  80.234  0.889   1   60.48 ? 249 ARG   B CB   1 
ATOM   4475 N  N    . SER   B 1 228 ? 60.145  78.868  3.825   1   59.11 ? 250 SER   B N    1 
ATOM   4476 C  CA   . SER   B 1 228 ? 59.687  77.863  4.786   1   59.15 ? 250 SER   B CA   1 
ATOM   4477 C  C    . SER   B 1 228 ? 59.181  78.456  6.108   1   58.11 ? 250 SER   B C    1 
ATOM   4478 O  O    . SER   B 1 228 ? 58.474  77.769  6.843   1   57.57 ? 250 SER   B O    1 
ATOM   4479 C  CB   . SER   B 1 228 ? 60.775  76.823  5.053   1   61.28 ? 250 SER   B CB   1 
ATOM   4480 O  OG   . SER   B 1 228 ? 61.801  77.324  5.898   1   64.13 ? 250 SER   B OG   1 
ATOM   4481 N  N    . ILE   B 1 229 ? 59.539  79.716  6.413   1   57.8  ? 251 ILE   B N    1 
ATOM   4482 C  CA   . ILE   B 1 229 ? 59.075  80.362  7.633   1   58.53 ? 251 ILE   B CA   1 
ATOM   4483 C  C    . ILE   B 1 229 ? 58.144  81.548  7.353   1   59.52 ? 251 ILE   B C    1 
ATOM   4484 O  O    . ILE   B 1 229 ? 57.271  81.831  8.163   1   59.27 ? 251 ILE   B O    1 
ATOM   4485 C  CB   . ILE   B 1 229 ? 60.236  80.75   8.581   1   58.94 ? 251 ILE   B CB   1 
ATOM   4486 C  CG1  . ILE   B 1 229 ? 61.256  81.667  7.888   1   59.72 ? 251 ILE   B CG1  1 
ATOM   4487 C  CG2  . ILE   B 1 229 ? 60.901  79.505  9.154   1   59.29 ? 251 ILE   B CG2  1 
ATOM   4488 C  CD1  . ILE   B 1 229 ? 62.17   82.428  8.857   1   60.92 ? 251 ILE   B CD1  1 
ATOM   4489 N  N    . PHE   B 1 230 ? 58.322  82.239  6.221   1   60.44 ? 252 PHE   B N    1 
ATOM   4490 C  CA   . PHE   B 1 230 ? 57.474  83.392  5.903   1   61.71 ? 252 PHE   B CA   1 
ATOM   4491 C  C    . PHE   B 1 230 ? 56.156  82.996  5.216   1   62.45 ? 252 PHE   B C    1 
ATOM   4492 O  O    . PHE   B 1 230 ? 55.221  83.789  5.216   1   62.42 ? 252 PHE   B O    1 
ATOM   4493 C  CB   . PHE   B 1 230 ? 58.247  84.462  5.121   1   61.8  ? 252 PHE   B CB   1 
ATOM   4494 C  CG   . PHE   B 1 230 ? 59.384  85.078  5.909   1   62.61 ? 252 PHE   B CG   1 
ATOM   4495 C  CD1  . PHE   B 1 230 ? 59.306  85.212  7.289   1   63.41 ? 252 PHE   B CD1  1 
ATOM   4496 C  CD2  . PHE   B 1 230 ? 60.525  85.534  5.269   1   63.36 ? 252 PHE   B CD2  1 
ATOM   4497 C  CE1  . PHE   B 1 230 ? 60.349  85.776  8.008   1   64.04 ? 252 PHE   B CE1  1 
ATOM   4498 C  CE2  . PHE   B 1 230 ? 61.563  86.11   5.992   1   64.03 ? 252 PHE   B CE2  1 
ATOM   4499 C  CZ   . PHE   B 1 230 ? 61.461  86.241  7.353   1   63.8  ? 252 PHE   B CZ   1 
ATOM   4500 N  N    . ASP   B 1 231 ? 56.062  81.761  4.687   1   62.78 ? 253 ASP   B N    1 
ATOM   4501 C  CA   . ASP   B 1 231 ? 54.838  81.257  4.087   1   63.28 ? 253 ASP   B CA   1 
ATOM   4502 C  C    . ASP   B 1 231 ? 54.244  80.25   5.062   1   63.68 ? 253 ASP   B C    1 
ATOM   4503 O  O    . ASP   B 1 231 ? 54.691  79.105  5.12    1   63.85 ? 253 ASP   B O    1 
ATOM   4504 C  CB   . ASP   B 1 231 ? 55.121  80.6    2.725   1   64.95 ? 253 ASP   B CB   1 
ATOM   4505 C  CG   . ASP   B 1 231 ? 53.899  80.08   1.979   1   68.7  ? 253 ASP   B CG   1 
ATOM   4506 O  OD1  . ASP   B 1 231 ? 52.785  80.108  2.559   1   68.72 ? 253 ASP   B OD1  1 
ATOM   4507 O  OD2  . ASP   B 1 231 ? 54.058  79.641  0.818   1   70.52 ? 253 ASP   B OD2  1 
ATOM   4508 N  N    . PRO   B 1 232 ? 53.2    80.659  5.805   1   63.76 ? 254 PRO   B N    1 
ATOM   4509 C  CA   . PRO   B 1 232 ? 52.585  79.753  6.782   1   64.08 ? 254 PRO   B CA   1 
ATOM   4510 C  C    . PRO   B 1 232 ? 52.18   78.387  6.261   1   65.17 ? 254 PRO   B C    1 
ATOM   4511 O  O    . PRO   B 1 232 ? 52.174  77.435  7.036   1   65.5  ? 254 PRO   B O    1 
ATOM   4512 C  CB   . PRO   B 1 232 ? 51.372  80.541  7.268   1   64.58 ? 254 PRO   B CB   1 
ATOM   4513 C  CG   . PRO   B 1 232 ? 51.767  81.963  7.098   1   64.83 ? 254 PRO   B CG   1 
ATOM   4514 C  CD   . PRO   B 1 232 ? 52.576  81.996  5.843   1   63.19 ? 254 PRO   B CD   1 
ATOM   4515 N  N    . ALA   B 1 233 ? 51.845  78.28   4.97    1   65.6  ? 255 ALA   B N    1 
ATOM   4516 C  CA   . ALA   B 1 233 ? 51.456  77.001  4.38    1   66.35 ? 255 ALA   B CA   1 
ATOM   4517 C  C    . ALA   B 1 233 ? 52.658  76.047  4.285   1   66.82 ? 255 ALA   B C    1 
ATOM   4518 O  O    . ALA   B 1 233 ? 52.501  74.837  4.487   1   66.8  ? 255 ALA   B O    1 
ATOM   4519 C  CB   . ALA   B 1 233 ? 50.842  77.222  3.003   1   66.24 ? 255 ALA   B CB   1 
ATOM   4520 N  N    . VAL   B 1 234 ? 53.855  76.591  3.991   1   66.79 ? 256 VAL   B N    1 
ATOM   4521 C  CA   . VAL   B 1 234 ? 55.06   75.769  3.918   1   67.39 ? 256 VAL   B CA   1 
ATOM   4522 C  C    . VAL   B 1 234 ? 55.433  75.264  5.326   1   67.72 ? 256 VAL   B C    1 
ATOM   4523 O  O    . VAL   B 1 234 ? 55.825  74.103  5.479   1   67.64 ? 256 VAL   B O    1 
ATOM   4524 C  CB   . VAL   B 1 234 ? 56.224  76.492  3.205   1   68.13 ? 256 VAL   B CB   1 
ATOM   4525 N  N    . HIS   B 1 235 ? 55.236  76.111  6.362   1   67.72 ? 257 HIS   B N    1 
ATOM   4526 C  CA   . HIS   B 1 235 ? 55.484  75.701  7.738   1   68.17 ? 257 HIS   B CA   1 
ATOM   4527 C  C    . HIS   B 1 235 ? 54.502  74.601  8.126   1   68.5  ? 257 HIS   B C    1 
ATOM   4528 O  O    . HIS   B 1 235 ? 54.921  73.611  8.719   1   68.67 ? 257 HIS   B O    1 
ATOM   4529 C  CB   . HIS   B 1 235 ? 55.361  76.883  8.717   1   68.88 ? 257 HIS   B CB   1 
ATOM   4530 C  CG   . HIS   B 1 235 ? 55.418  76.464  10.163  1   70.55 ? 257 HIS   B CG   1 
ATOM   4531 N  ND1  . HIS   B 1 235 ? 56.621  76.373  10.841  1   72.04 ? 257 HIS   B ND1  1 
ATOM   4532 C  CD2  . HIS   B 1 235 ? 54.42   76.073  10.993  1   71.45 ? 257 HIS   B CD2  1 
ATOM   4533 C  CE1  . HIS   B 1 235 ? 56.317  75.948  12.059  1   72.47 ? 257 HIS   B CE1  1 
ATOM   4534 N  NE2  . HIS   B 1 235 ? 55.006  75.753  12.197  1   72.35 ? 257 HIS   B NE2  1 
ATOM   4535 N  N    . ASP   B 1 236 ? 53.206  74.773  7.788   1   68.33 ? 258 ASP   B N    1 
ATOM   4536 C  CA   . ASP   B 1 236 ? 52.148  73.814  8.113   1   68.51 ? 258 ASP   B CA   1 
ATOM   4537 C  C    . ASP   B 1 236 ? 52.378  72.448  7.484   1   68.32 ? 258 ASP   B C    1 
ATOM   4538 O  O    . ASP   B 1 236 ? 52.048  71.431  8.096   1   68.49 ? 258 ASP   B O    1 
ATOM   4539 C  CB   . ASP   B 1 236 ? 50.771  74.367  7.725   1   70.43 ? 258 ASP   B CB   1 
ATOM   4540 C  CG   . ASP   B 1 236 ? 50.314  75.506  8.614   1   75.51 ? 258 ASP   B CG   1 
ATOM   4541 O  OD1  . ASP   B 1 236 ? 50.568  75.444  9.837   1   76.1  ? 258 ASP   B OD1  1 
ATOM   4542 O  OD2  . ASP   B 1 236 ? 49.709  76.465  8.087   1   77.99 ? 258 ASP   B OD2  1 
ATOM   4543 N  N    . ALA   B 1 237 ? 52.964  72.418  6.284   1   67.86 ? 259 ALA   B N    1 
ATOM   4544 C  CA   . ALA   B 1 237 ? 53.259  71.157  5.609   1   68.35 ? 259 ALA   B CA   1 
ATOM   4545 C  C    . ALA   B 1 237 ? 54.393  70.427  6.335   1   68.58 ? 259 ALA   B C    1 
ATOM   4546 O  O    . ALA   B 1 237 ? 54.326  69.209  6.523   1   68.78 ? 259 ALA   B O    1 
ATOM   4547 C  CB   . ALA   B 1 237 ? 53.64   71.416  4.161   1   68.6  ? 259 ALA   B CB   1 
ATOM   4548 N  N    . LEU   B 1 238 ? 55.414  71.18   6.775   1   68.22 ? 260 LEU   B N    1 
ATOM   4549 C  CA   . LEU   B 1 238 ? 56.545  70.637  7.529   1   68.12 ? 260 LEU   B CA   1 
ATOM   4550 C  C    . LEU   B 1 238 ? 56.071  70.074  8.87    1   68.35 ? 260 LEU   B C    1 
ATOM   4551 O  O    . LEU   B 1 238 ? 56.571  69.04   9.306   1   68.5  ? 260 LEU   B O    1 
ATOM   4552 C  CB   . LEU   B 1 238 ? 57.606  71.719  7.747   1   67.83 ? 260 LEU   B CB   1 
ATOM   4553 C  CG   . LEU   B 1 238 ? 58.345  72.146  6.497   1   69.08 ? 260 LEU   B CG   1 
ATOM   4554 N  N    . VAL   B 1 239 ? 55.085  70.732  9.505   1   68.3  ? 261 VAL   B N    1 
ATOM   4555 C  CA   . VAL   B 1 239 ? 54.505  70.273  10.766  1   68.7  ? 261 VAL   B CA   1 
ATOM   4556 C  C    . VAL   B 1 239 ? 53.767  68.942  10.545  1   69.14 ? 261 VAL   B C    1 
ATOM   4557 O  O    . VAL   B 1 239 ? 53.924  68.005  11.333  1   69.32 ? 261 VAL   B O    1 
ATOM   4558 C  CB   . VAL   B 1 239 ? 53.6    71.362  11.405  1   69.08 ? 261 VAL   B CB   1 
ATOM   4559 C  CG1  . VAL   B 1 239 ? 52.779  70.801  12.563  1   69.56 ? 261 VAL   B CG1  1 
ATOM   4560 C  CG2  . VAL   B 1 239 ? 54.43   72.55   11.874  1   69.34 ? 261 VAL   B CG2  1 
ATOM   4561 N  N    . ARG   B 1 240 ? 53.018  68.843  9.434   1   69.14 ? 262 ARG   B N    1 
ATOM   4562 C  CA   . ARG   B 1 240 ? 52.273  67.641  9.059   1   69.3  ? 262 ARG   B CA   1 
ATOM   4563 C  C    . ARG   B 1 240 ? 53.183  66.432  8.83    1   69.04 ? 262 ARG   B C    1 
ATOM   4564 O  O    . ARG   B 1 240 ? 52.851  65.337  9.282   1   69.09 ? 262 ARG   B O    1 
ATOM   4565 C  CB   . ARG   B 1 240 ? 51.414  67.901  7.808   1   70.53 ? 262 ARG   B CB   1 
ATOM   4566 N  N    . ARG   B 1 241 ? 54.34   66.624  8.156   1   68.54 ? 263 ARG   B N    1 
ATOM   4567 C  CA   . ARG   B 1 241 ? 55.251  65.508  7.895   1   68.36 ? 263 ARG   B CA   1 
ATOM   4568 C  C    . ARG   B 1 241 ? 56.229  65.197  9.049   1   67.88 ? 263 ARG   B C    1 
ATOM   4569 O  O    . ARG   B 1 241 ? 57.124  64.369  8.882   1   68.39 ? 263 ARG   B O    1 
ATOM   4570 C  CB   . ARG   B 1 241 ? 56.007  65.686  6.565   1   69.88 ? 263 ARG   B CB   1 
ATOM   4571 C  CG   . ARG   B 1 241 ? 56.986  66.844  6.532   1   73    ? 263 ARG   B CG   1 
ATOM   4572 N  N    . GLY   B 1 242 ? 56.038  65.824  10.206  1   66.77 ? 264 GLY   B N    1 
ATOM   4573 C  CA   . GLY   B 1 242 ? 56.856  65.569  11.386  1   66.05 ? 264 GLY   B CA   1 
ATOM   4574 C  C    . GLY   B 1 242 ? 58.177  66.305  11.461  1   64.78 ? 264 GLY   B C    1 
ATOM   4575 O  O    . GLY   B 1 242 ? 58.912  66.134  12.433  1   64.88 ? 264 GLY   B O    1 
ATOM   4576 N  N    . ASP   B 1 243 ? 58.497  67.119  10.445  1   63.44 ? 265 ASP   B N    1 
ATOM   4577 C  CA   . ASP   B 1 243 ? 59.746  67.883  10.421  1   62.65 ? 265 ASP   B CA   1 
ATOM   4578 C  C    . ASP   B 1 243 ? 59.766  69.004  11.468  1   61.15 ? 265 ASP   B C    1 
ATOM   4579 O  O    . ASP   B 1 243 ? 60.838  69.409  11.916  1   61.08 ? 265 ASP   B O    1 
ATOM   4580 C  CB   . ASP   B 1 243 ? 60.01   68.459  9.021   1   65.27 ? 265 ASP   B CB   1 
ATOM   4581 C  CG   . ASP   B 1 243 ? 60.295  67.425  7.945   1   71.94 ? 265 ASP   B CG   1 
ATOM   4582 O  OD1  . ASP   B 1 243 ? 60.138  66.212  8.227   1   73.71 ? 265 ASP   B OD1  1 
ATOM   4583 O  OD2  . ASP   B 1 243 ? 60.675  67.826  6.819   1   74.06 ? 265 ASP   B OD2  1 
ATOM   4584 N  N    . ARG   B 1 244 ? 58.579  69.522  11.833  1   59.69 ? 266 ARG   B N    1 
ATOM   4585 C  CA   . ARG   B 1 244 ? 58.385  70.568  12.832  1   58.38 ? 266 ARG   B CA   1 
ATOM   4586 C  C    . ARG   B 1 244 ? 57.238  70.169  13.769  1   58.06 ? 266 ARG   B C    1 
ATOM   4587 O  O    . ARG   B 1 244 ? 56.367  69.393  13.387  1   58.4  ? 266 ARG   B O    1 
ATOM   4588 C  CB   . ARG   B 1 244 ? 58.097  71.92   12.153  1   58.22 ? 266 ARG   B CB   1 
ATOM   4589 C  CG   . ARG   B 1 244 ? 59.316  72.527  11.465  1   58.89 ? 266 ARG   B CG   1 
ATOM   4590 C  CD   . ARG   B 1 244 ? 59.058  73.916  10.925  1   60.44 ? 266 ARG   B CD   1 
ATOM   4591 N  NE   . ARG   B 1 244 ? 60.126  74.366  10.029  1   61.94 ? 266 ARG   B NE   1 
ATOM   4592 C  CZ   . ARG   B 1 244 ? 60.078  75.477  9.295   1   62.98 ? 266 ARG   B CZ   1 
ATOM   4593 N  NH1  . ARG   B 1 244 ? 59.011  76.267  9.342   1   62.39 ? 266 ARG   B NH1  1 
ATOM   4594 N  NH2  . ARG   B 1 244 ? 61.091  75.802  8.503   1   61.96 ? 266 ARG   B NH2  1 
ATOM   4595 N  N    . ARG   B 1 245 ? 57.252  70.67   15      1   57.58 ? 267 ARG   B N    1 
ATOM   4596 C  CA   . ARG   B 1 245 ? 56.212  70.402  16.005  1   57.72 ? 267 ARG   B CA   1 
ATOM   4597 C  C    . ARG   B 1 245 ? 55.517  71.693  16.477  1   57.03 ? 267 ARG   B C    1 
ATOM   4598 O  O    . ARG   B 1 245 ? 54.398  71.643  16.984  1   57.16 ? 267 ARG   B O    1 
ATOM   4599 C  CB   . ARG   B 1 245 ? 56.829  69.734  17.242  1   59.67 ? 267 ARG   B CB   1 
ATOM   4600 C  CG   . ARG   B 1 245 ? 57.001  68.235  17.139  1   63.79 ? 267 ARG   B CG   1 
ATOM   4601 C  CD   . ARG   B 1 245 ? 58.385  67.841  17.611  1   66.77 ? 267 ARG   B CD   1 
ATOM   4602 N  NE   . ARG   B 1 245 ? 58.606  66.394  17.646  1   70.1  ? 267 ARG   B NE   1 
ATOM   4603 C  CZ   . ARG   B 1 245 ? 58.92   65.652  16.588  1   72.92 ? 267 ARG   B CZ   1 
ATOM   4604 N  NH1  . ARG   B 1 245 ? 58.993  66.2    15.381  1   73.21 ? 267 ARG   B NH1  1 
ATOM   4605 N  NH2  . ARG   B 1 245 ? 59.137  64.352  16.724  1   72.95 ? 267 ARG   B NH2  1 
ATOM   4606 N  N    . PHE   B 1 246 ? 56.217  72.829  16.382  1   56.1  ? 268 PHE   B N    1 
ATOM   4607 C  CA   . PHE   B 1 246 ? 55.749  74.12   16.852  1   55.85 ? 268 PHE   B CA   1 
ATOM   4608 C  C    . PHE   B 1 246 ? 54.697  74.737  15.965  1   55.52 ? 268 PHE   B C    1 
ATOM   4609 O  O    . PHE   B 1 246 ? 54.757  74.616  14.74   1   55.68 ? 268 PHE   B O    1 
ATOM   4610 C  CB   . PHE   B 1 246 ? 56.921  75.11   16.919  1   55.68 ? 268 PHE   B CB   1 
ATOM   4611 C  CG   . PHE   B 1 246 ? 57.785  75.082  18.155  1   56.2  ? 268 PHE   B CG   1 
ATOM   4612 C  CD1  . PHE   B 1 246 ? 57.74   74.011  19.031  1   56.98 ? 268 PHE   B CD1  1 
ATOM   4613 C  CD2  . PHE   B 1 246 ? 58.679  76.103  18.414  1   56.78 ? 268 PHE   B CD2  1 
ATOM   4614 C  CE1  . PHE   B 1 246 ? 58.56   73.971  20.148  1   57.5  ? 268 PHE   B CE1  1 
ATOM   4615 C  CE2  . PHE   B 1 246 ? 59.504  76.057  19.527  1   57.51 ? 268 PHE   B CE2  1 
ATOM   4616 C  CZ   . PHE   B 1 246 ? 59.439  74.992  20.388  1   57.25 ? 268 PHE   B CZ   1 
ATOM   4617 N  N    . SER   B 1 247 ? 53.791  75.513  16.581  1   54.68 ? 269 SER   B N    1 
ATOM   4618 C  CA   . SER   B 1 247 ? 52.827  76.316  15.833  1   53.91 ? 269 SER   B CA   1 
ATOM   4619 C  C    . SER   B 1 247 ? 53.636  77.44   15.159  1   53.65 ? 269 SER   B C    1 
ATOM   4620 O  O    . SER   B 1 247 ? 54.709  77.82   15.653  1   53.54 ? 269 SER   B O    1 
ATOM   4621 C  CB   . SER   B 1 247 ? 51.781  76.915  16.768  1   54.17 ? 269 SER   B CB   1 
ATOM   4622 O  OG   . SER   B 1 247 ? 52.28   78.002  17.531  1   56.21 ? 269 SER   B OG   1 
ATOM   4623 N  N    . HIS   B 1 248 ? 53.124  77.987  14.057  1   53.12 ? 270 HIS   B N    1 
ATOM   4624 C  CA   . HIS   B 1 248 ? 53.815  79.051  13.342  1   53.19 ? 270 HIS   B CA   1 
ATOM   4625 C  C    . HIS   B 1 248 ? 54.163  80.253  14.234  1   53.76 ? 270 HIS   B C    1 
ATOM   4626 O  O    . HIS   B 1 248 ? 55.247  80.823  14.091  1   53.96 ? 270 HIS   B O    1 
ATOM   4627 C  CB   . HIS   B 1 248 ? 53.008  79.495  12.109  1   53.52 ? 270 HIS   B CB   1 
ATOM   4628 C  CG   . HIS   B 1 248 ? 53.802  80.334  11.165  1   54.24 ? 270 HIS   B CG   1 
ATOM   4629 N  ND1  . HIS   B 1 248 ? 53.527  81.678  10.986  1   55.9  ? 270 HIS   B ND1  1 
ATOM   4630 C  CD2  . HIS   B 1 248 ? 54.884  80.006  10.424  1   55.26 ? 270 HIS   B CD2  1 
ATOM   4631 C  CE1  . HIS   B 1 248 ? 54.431  82.117  10.124  1   56.5  ? 270 HIS   B CE1  1 
ATOM   4632 N  NE2  . HIS   B 1 248 ? 55.268  81.147  9.759   1   56.27 ? 270 HIS   B NE2  1 
ATOM   4633 N  N    . ARG   B 1 249 ? 53.265  80.613  15.169  1   53.85 ? 271 ARG   B N    1 
ATOM   4634 C  CA   . ARG   B 1 249 ? 53.508  81.74   16.069  1   54.41 ? 271 ARG   B CA   1 
ATOM   4635 C  C    . ARG   B 1 249 ? 54.527  81.395  17.168  1   54.88 ? 271 ARG   B C    1 
ATOM   4636 O  O    . ARG   B 1 249 ? 55.36   82.248  17.509  1   54.93 ? 271 ARG   B O    1 
ATOM   4637 C  CB   . ARG   B 1 249 ? 52.206  82.312  16.647  1   55.34 ? 271 ARG   B CB   1 
ATOM   4638 N  N    . ALA   B 1 250 ? 54.51   80.13   17.683  1   54.6  ? 272 ALA   B N    1 
ATOM   4639 C  CA   . ALA   B 1 250 ? 55.5    79.687  18.676  1   54.03 ? 272 ALA   B CA   1 
ATOM   4640 C  C    . ALA   B 1 250 ? 56.897  79.727  18.034  1   53.4  ? 272 ALA   B C    1 
ATOM   4641 O  O    . ALA   B 1 250 ? 57.835  80.224  18.652  1   53.62 ? 272 ALA   B O    1 
ATOM   4642 C  CB   . ALA   B 1 250 ? 55.18   78.284  19.155  1   54.11 ? 272 ALA   B CB   1 
ATOM   4643 N  N    . LEU   B 1 251 ? 57.008  79.287  16.767  1   52.82 ? 273 LEU   B N    1 
ATOM   4644 C  CA   . LEU   B 1 251 ? 58.265  79.325  16.025  1   53.28 ? 273 LEU   B CA   1 
ATOM   4645 C  C    . LEU   B 1 251 ? 58.787  80.762  15.842  1   54.29 ? 273 LEU   B C    1 
ATOM   4646 O  O    . LEU   B 1 251 ? 59.992  80.984  15.978  1   54.89 ? 273 LEU   B O    1 
ATOM   4647 C  CB   . LEU   B 1 251 ? 58.146  78.604  14.677  1   53.09 ? 273 LEU   B CB   1 
ATOM   4648 C  CG   . LEU   B 1 251 ? 59.449  78.544  13.886  1   54.89 ? 273 LEU   B CG   1 
ATOM   4649 C  CD1  . LEU   B 1 251 ? 60.48   77.68   14.587  1   55.64 ? 273 LEU   B CD1  1 
ATOM   4650 C  CD2  . LEU   B 1 251 ? 59.223  78.047  12.476  1   55.54 ? 273 LEU   B CD2  1 
ATOM   4651 N  N    . GLN   B 1 252 ? 57.886  81.74   15.588  1   54.3  ? 274 GLN   B N    1 
ATOM   4652 C  CA   . GLN   B 1 252 ? 58.252  83.159  15.435  1   54.69 ? 274 GLN   B CA   1 
ATOM   4653 C  C    . GLN   B 1 252 ? 58.875  83.685  16.735  1   53.9  ? 274 GLN   B C    1 
ATOM   4654 O  O    . GLN   B 1 252 ? 59.88   84.4    16.697  1   53.32 ? 274 GLN   B O    1 
ATOM   4655 C  CB   . GLN   B 1 252 ? 57.023  84.031  15.079  1   57.03 ? 274 GLN   B CB   1 
ATOM   4656 C  CG   . GLN   B 1 252 ? 56.362  83.717  13.741  1   61.91 ? 274 GLN   B CG   1 
ATOM   4657 C  CD   . GLN   B 1 252 ? 55.125  84.568  13.504  1   66.56 ? 274 GLN   B CD   1 
ATOM   4658 O  OE1  . GLN   B 1 252 ? 55.2    85.79   13.391  1   67.88 ? 274 GLN   B OE1  1 
ATOM   4659 N  NE2  . GLN   B 1 252 ? 53.958  83.948  13.425  1   66.88 ? 274 GLN   B NE2  1 
ATOM   4660 N  N    . GLY   B 1 253 ? 58.254  83.338  17.861  1   53.61 ? 275 GLY   B N    1 
ATOM   4661 C  CA   . GLY   B 1 253 ? 58.732  83.732  19.177  1   53.96 ? 275 GLY   B CA   1 
ATOM   4662 C  C    . GLY   B 1 253 ? 60.098  83.151  19.479  1   54.11 ? 275 GLY   B C    1 
ATOM   4663 O  O    . GLY   B 1 253 ? 60.991  83.869  19.925  1   54.23 ? 275 GLY   B O    1 
ATOM   4664 N  N    . ALA   B 1 254 ? 60.286  81.857  19.195  1   54.12 ? 276 ALA   B N    1 
ATOM   4665 C  CA   . ALA   B 1 254 ? 61.561  81.179  19.425  1   54.64 ? 276 ALA   B CA   1 
ATOM   4666 C  C    . ALA   B 1 254 ? 62.675  81.804  18.582  1   54.71 ? 276 ALA   B C    1 
ATOM   4667 O  O    . ALA   B 1 254 ? 63.785  81.983  19.083  1   54.7  ? 276 ALA   B O    1 
ATOM   4668 C  CB   . ALA   B 1 254 ? 61.428  79.698  19.106  1   54.9  ? 276 ALA   B CB   1 
ATOM   4669 N  N    . ILE   B 1 255 ? 62.374  82.167  17.316  1   54.36 ? 277 ILE   B N    1 
ATOM   4670 C  CA   . ILE   B 1 255 ? 63.353  82.807  16.437  1   54.69 ? 277 ILE   B CA   1 
ATOM   4671 C  C    . ILE   B 1 255 ? 63.753  84.188  16.982  1   55.67 ? 277 ILE   B C    1 
ATOM   4672 O  O    . ILE   B 1 255 ? 64.942  84.526  17.021  1   56.08 ? 277 ILE   B O    1 
ATOM   4673 C  CB   . ILE   B 1 255 ? 62.833  82.872  14.981  1   54.94 ? 277 ILE   B CB   1 
ATOM   4674 C  CG1  . ILE   B 1 255 ? 62.779  81.471  14.361  1   55.73 ? 277 ILE   B CG1  1 
ATOM   4675 C  CG2  . ILE   B 1 255 ? 63.698  83.798  14.117  1   55.48 ? 277 ILE   B CG2  1 
ATOM   4676 C  CD1  . ILE   B 1 255 ? 61.957  81.388  13.078  1   56.82 ? 277 ILE   B CD1  1 
ATOM   4677 N  N    . MET   B 1 256 ? 62.761  84.967  17.435  1   55.62 ? 278 MET   B N    1 
ATOM   4678 C  CA   . MET   B 1 256 ? 63      86.292  17.989  1   55.97 ? 278 MET   B CA   1 
ATOM   4679 C  C    . MET   B 1 256 ? 63.872  86.198  19.244  1   55.59 ? 278 MET   B C    1 
ATOM   4680 O  O    . MET   B 1 256 ? 64.805  86.983  19.414  1   55.81 ? 278 MET   B O    1 
ATOM   4681 C  CB   . MET   B 1 256 ? 61.667  86.965  18.323  1   57.3  ? 278 MET   B CB   1 
ATOM   4682 C  CG   . MET   B 1 256 ? 61.823  88.428  18.635  1   60.5  ? 278 MET   B CG   1 
ATOM   4683 S  SD   . MET   B 1 256 ? 60.346  89.219  19.319  1   66.22 ? 278 MET   B SD   1 
ATOM   4684 C  CE   . MET   B 1 256 ? 61.028  90.894  19.531  1   66.63 ? 278 MET   B CE   1 
ATOM   4685 N  N    . ILE   B 1 257 ? 63.599  85.207  20.104  1   54.62 ? 279 ILE   B N    1 
ATOM   4686 C  CA   . ILE   B 1 257 ? 64.39   85.001  21.311  1   53.75 ? 279 ILE   B CA   1 
ATOM   4687 C  C    . ILE   B 1 257 ? 65.882  84.756  20.975  1   53.66 ? 279 ILE   B C    1 
ATOM   4688 O  O    . ILE   B 1 257 ? 66.748  85.391  21.575  1   53.44 ? 279 ILE   B O    1 
ATOM   4689 C  CB   . ILE   B 1 257 ? 63.756  83.899  22.197  1   53.38 ? 279 ILE   B CB   1 
ATOM   4690 C  CG1  . ILE   B 1 257 ? 62.462  84.409  22.845  1   53.42 ? 279 ILE   B CG1  1 
ATOM   4691 C  CG2  . ILE   B 1 257 ? 64.736  83.412  23.261  1   53.86 ? 279 ILE   B CG2  1 
ATOM   4692 C  CD1  . ILE   B 1 257 ? 61.728  83.406  23.733  1   54.15 ? 279 ILE   B CD1  1 
ATOM   4693 N  N    . THR   B 1 258 ? 66.172  83.92   19.962  1   53.72 ? 280 THR   B N    1 
ATOM   4694 C  CA   . THR   B 1 258 ? 67.555  83.64   19.565  1   54.66 ? 280 THR   B CA   1 
ATOM   4695 C  C    . THR   B 1 258 ? 68.268  84.839  18.965  1   56.13 ? 280 THR   B C    1 
ATOM   4696 O  O    . THR   B 1 258 ? 69.488  84.945  19.077  1   56.46 ? 280 THR   B O    1 
ATOM   4697 C  CB   . THR   B 1 258 ? 67.648  82.431  18.626  1   55.3  ? 280 THR   B CB   1 
ATOM   4698 O  OG1  . THR   B 1 258 ? 67.077  82.746  17.353  1   56.39 ? 280 THR   B OG1  1 
ATOM   4699 C  CG2  . THR   B 1 258 ? 67.032  81.181  19.218  1   55.29 ? 280 THR   B CG2  1 
ATOM   4700 N  N    . PHE   B 1 259 ? 67.52   85.731  18.309  1   56.99 ? 281 PHE   B N    1 
ATOM   4701 C  CA   . PHE   B 1 259 ? 68.088  86.924  17.682  1   58.09 ? 281 PHE   B CA   1 
ATOM   4702 C  C    . PHE   B 1 259 ? 68.54   87.934  18.734  1   57.76 ? 281 PHE   B C    1 
ATOM   4703 O  O    . PHE   B 1 259 ? 69.561  88.593  18.557  1   57.4  ? 281 PHE   B O    1 
ATOM   4704 C  CB   . PHE   B 1 259 ? 67.044  87.584  16.77   1   59.17 ? 281 PHE   B CB   1 
ATOM   4705 C  CG   . PHE   B 1 259 ? 66.961  87.061  15.353  1   61.03 ? 281 PHE   B CG   1 
ATOM   4706 C  CD1  . PHE   B 1 259 ? 67.252  85.737  15.064  1   62.27 ? 281 PHE   B CD1  1 
ATOM   4707 C  CD2  . PHE   B 1 259 ? 66.553  87.885  14.317  1   62.31 ? 281 PHE   B CD2  1 
ATOM   4708 C  CE1  . PHE   B 1 259 ? 67.14   85.25   13.767  1   63.21 ? 281 PHE   B CE1  1 
ATOM   4709 C  CE2  . PHE   B 1 259 ? 66.457  87.399  13.017  1   63.27 ? 281 PHE   B CE2  1 
ATOM   4710 C  CZ   . PHE   B 1 259 ? 66.753  86.086  12.751  1   63.16 ? 281 PHE   B CZ   1 
ATOM   4711 N  N    . TYR   B 1 260 ? 67.78   88.06   19.828  1   57.9  ? 282 TYR   B N    1 
ATOM   4712 C  CA   . TYR   B 1 260 ? 68.091  89.048  20.856  1   58.62 ? 282 TYR   B CA   1 
ATOM   4713 C  C    . TYR   B 1 260 ? 68.623  88.466  22.163  1   57.91 ? 282 TYR   B C    1 
ATOM   4714 O  O    . TYR   B 1 260 ? 68.607  89.16   23.17   1   57.51 ? 282 TYR   B O    1 
ATOM   4715 C  CB   . TYR   B 1 260 ? 66.861  89.931  21.119  1   59.34 ? 282 TYR   B CB   1 
ATOM   4716 C  CG   . TYR   B 1 260 ? 66.363  90.616  19.868  1   60.95 ? 282 TYR   B CG   1 
ATOM   4717 C  CD1  . TYR   B 1 260 ? 67.059  91.675  19.308  1   62.26 ? 282 TYR   B CD1  1 
ATOM   4718 C  CD2  . TYR   B 1 260 ? 65.218  90.176  19.22   1   62.06 ? 282 TYR   B CD2  1 
ATOM   4719 C  CE1  . TYR   B 1 260 ? 66.614  92.297  18.15   1   63.46 ? 282 TYR   B CE1  1 
ATOM   4720 C  CE2  . TYR   B 1 260 ? 64.773  90.777  18.051  1   63.12 ? 282 TYR   B CE2  1 
ATOM   4721 C  CZ   . TYR   B 1 260 ? 65.471  91.84   17.52   1   64.16 ? 282 TYR   B CZ   1 
ATOM   4722 O  OH   . TYR   B 1 260 ? 65.028  92.436  16.367  1   65.54 ? 282 TYR   B OH   1 
ATOM   4723 N  N    . ARG   B 1 261 ? 69.131  87.226  22.146  1   57.7  ? 283 ARG   B N    1 
ATOM   4724 C  CA   . ARG   B 1 261 ? 69.648  86.545  23.344  1   57.66 ? 283 ARG   B CA   1 
ATOM   4725 C  C    . ARG   B 1 261 ? 70.693  87.341  24.156  1   57.68 ? 283 ARG   B C    1 
ATOM   4726 O  O    . ARG   B 1 261 ? 70.726  87.201  25.371  1   57.57 ? 283 ARG   B O    1 
ATOM   4727 C  CB   . ARG   B 1 261 ? 70.198  85.17   22.98   1   58.49 ? 283 ARG   B CB   1 
ATOM   4728 C  CG   . ARG   B 1 261 ? 71.293  85.234  21.936  1   60.33 ? 283 ARG   B CG   1 
ATOM   4729 C  CD   . ARG   B 1 261 ? 71.825  83.859  21.641  1   62.65 ? 283 ARG   B CD   1 
ATOM   4730 N  NE   . ARG   B 1 261 ? 72.63   83.36   22.752  1   65.42 ? 283 ARG   B NE   1 
ATOM   4731 C  CZ   . ARG   B 1 261 ? 73.184  82.153  22.794  1   67.99 ? 283 ARG   B CZ   1 
ATOM   4732 N  NH1  . ARG   B 1 261 ? 73.011  81.298  21.793  1   67.69 ? 283 ARG   B NH1  1 
ATOM   4733 N  NH2  . ARG   B 1 261 ? 73.907  81.786  23.844  1   67.9  ? 283 ARG   B NH2  1 
ATOM   4734 N  N    . ASP   B 1 262 ? 71.515  88.181  23.503  1   57.84 ? 284 ASP   B N    1 
ATOM   4735 C  CA   . ASP   B 1 262 ? 72.514  89.03   24.167  1   58.72 ? 284 ASP   B CA   1 
ATOM   4736 C  C    . ASP   B 1 262 ? 71.875  90.173  25.003  1   59.34 ? 284 ASP   B C    1 
ATOM   4737 O  O    . ASP   B 1 262 ? 72.571  90.793  25.818  1   59.53 ? 284 ASP   B O    1 
ATOM   4738 C  CB   . ASP   B 1 262 ? 73.441  89.679  23.125  1   60.99 ? 284 ASP   B CB   1 
ATOM   4739 C  CG   . ASP   B 1 262 ? 74.468  88.766  22.493  1   67.05 ? 284 ASP   B CG   1 
ATOM   4740 O  OD1  . ASP   B 1 262 ? 74.469  87.556  22.82   1   68.82 ? 284 ASP   B OD1  1 
ATOM   4741 O  OD2  . ASP   B 1 262 ? 75.278  89.264  21.668  1   68.8  ? 284 ASP   B OD2  1 
ATOM   4742 N  N    . GLU   B 1 263 ? 70.584  90.489  24.755  1   59.18 ? 285 GLU   B N    1 
ATOM   4743 C  CA   . GLU   B 1 263 ? 69.86   91.553  25.425  1   59.61 ? 285 GLU   B CA   1 
ATOM   4744 C  C    . GLU   B 1 263 ? 69.349  91.082  26.748  1   59.55 ? 285 GLU   B C    1 
ATOM   4745 O  O    . GLU   B 1 263 ? 68.732  90.029  26.814  1   59.59 ? 285 GLU   B O    1 
ATOM   4746 C  CB   . GLU   B 1 263 ? 68.677  92.027  24.573  1   62.75 ? 285 GLU   B CB   1 
ATOM   4747 C  CG   . GLU   B 1 263 ? 69.102  92.597  23.237  1   69.05 ? 285 GLU   B CG   1 
ATOM   4748 C  CD   . GLU   B 1 263 ? 69.912  93.869  23.378  1   77.32 ? 285 GLU   B CD   1 
ATOM   4749 O  OE1  . GLU   B 1 263 ? 69.55   94.713  24.233  1   78.69 ? 285 GLU   B OE1  1 
ATOM   4750 O  OE2  . GLU   B 1 263 ? 70.913  94.017  22.64   1   80.09 ? 285 GLU   B OE2  1 
ATOM   4751 N  N    . PRO   B 1 264 ? 69.533  91.889  27.806  1   59.53 ? 286 PRO   B N    1 
ATOM   4752 C  CA   . PRO   B 1 264 ? 69.051  91.494  29.139  1   59.55 ? 286 PRO   B CA   1 
ATOM   4753 C  C    . PRO   B 1 264 ? 67.631  90.944  29.227  1   59.8  ? 286 PRO   B C    1 
ATOM   4754 O  O    . PRO   B 1 264 ? 67.402  90.002  29.981  1   60.25 ? 286 PRO   B O    1 
ATOM   4755 C  CB   . PRO   B 1 264 ? 69.193  92.781  29.948  1   60.36 ? 286 PRO   B CB   1 
ATOM   4756 C  CG   . PRO   B 1 264 ? 70.361  93.462  29.322  1   60.83 ? 286 PRO   B CG   1 
ATOM   4757 C  CD   . PRO   B 1 264 ? 70.269  93.167  27.856  1   59.02 ? 286 PRO   B CD   1 
ATOM   4758 N  N    . ARG   B 1 265 ? 66.679  91.514  28.469  1   59.54 ? 287 ARG   B N    1 
ATOM   4759 C  CA   . ARG   B 1 265 ? 65.279  91.072  28.496  1   59.49 ? 287 ARG   B CA   1 
ATOM   4760 C  C    . ARG   B 1 265 ? 65.046  89.703  27.837  1   58.76 ? 287 ARG   B C    1 
ATOM   4761 O  O    . ARG   B 1 265 ? 64.071  89.019  28.161  1   58.35 ? 287 ARG   B O    1 
ATOM   4762 C  CB   . ARG   B 1 265 ? 64.366  92.137  27.864  1   60.77 ? 287 ARG   B CB   1 
ATOM   4763 N  N    . PHE   B 1 266 ? 65.94   89.306  26.925  1   58.47 ? 288 PHE   B N    1 
ATOM   4764 C  CA   . PHE   B 1 266 ? 65.815  88.039  26.219  1   58.95 ? 288 PHE   B CA   1 
ATOM   4765 C  C    . PHE   B 1 266 ? 66.789  86.942  26.687  1   57.97 ? 288 PHE   B C    1 
ATOM   4766 O  O    . PHE   B 1 266 ? 66.687  85.82   26.194  1   57.89 ? 288 PHE   B O    1 
ATOM   4767 C  CB   . PHE   B 1 266 ? 65.979  88.262  24.713  1   59.82 ? 288 PHE   B CB   1 
ATOM   4768 C  CG   . PHE   B 1 266 ? 64.845  89.012  24.059  1   61.49 ? 288 PHE   B CG   1 
ATOM   4769 C  CD1  . PHE   B 1 266 ? 64.858  90.395  23.985  1   62.77 ? 288 PHE   B CD1  1 
ATOM   4770 C  CD2  . PHE   B 1 266 ? 63.768  88.336  23.514  1   62.53 ? 288 PHE   B CD2  1 
ATOM   4771 C  CE1  . PHE   B 1 266 ? 63.819  91.083  23.38   1   63.55 ? 288 PHE   B CE1  1 
ATOM   4772 C  CE2  . PHE   B 1 266 ? 62.726  89.029  22.918  1   63.3  ? 288 PHE   B CE2  1 
ATOM   4773 C  CZ   . PHE   B 1 266 ? 62.757  90.396  22.857  1   63.29 ? 288 PHE   B CZ   1 
ATOM   4774 N  N    . SER   B 1 267 ? 67.721  87.242  27.617  1   56.74 ? 289 SER   B N    1 
ATOM   4775 C  CA   . SER   B 1 267 ? 68.715  86.253  28.054  1   55.97 ? 289 SER   B CA   1 
ATOM   4776 C  C    . SER   B 1 267 ? 68.138  85.051  28.832  1   54.83 ? 289 SER   B C    1 
ATOM   4777 O  O    . SER   B 1 267 ? 68.513  83.919  28.526  1   54.76 ? 289 SER   B O    1 
ATOM   4778 C  CB   . SER   B 1 267 ? 69.837  86.913  28.844  1   57.23 ? 289 SER   B CB   1 
ATOM   4779 O  OG   . SER   B 1 267 ? 69.35   87.418  30.077  1   59.84 ? 289 SER   B OG   1 
ATOM   4780 N  N    . GLN   B 1 268 ? 67.256  85.278  29.826  1   53.76 ? 290 GLN   B N    1 
ATOM   4781 C  CA   . GLN   B 1 268 ? 66.652  84.165  30.568  1   53.51 ? 290 GLN   B CA   1 
ATOM   4782 C  C    . GLN   B 1 268 ? 65.684  83.347  29.707  1   53.89 ? 290 GLN   B C    1 
ATOM   4783 O  O    . GLN   B 1 268 ? 65.812  82.121  29.703  1   53.76 ? 290 GLN   B O    1 
ATOM   4784 C  CB   . GLN   B 1 268 ? 66.031  84.596  31.907  1   54.25 ? 290 GLN   B CB   1 
ATOM   4785 C  CG   . GLN   B 1 268 ? 67.104  85.002  32.929  1   57.61 ? 290 GLN   B CG   1 
ATOM   4786 C  CD   . GLN   B 1 268 ? 68.129  83.898  33.162  1   60.66 ? 290 GLN   B CD   1 
ATOM   4787 O  OE1  . GLN   B 1 268 ? 67.807  82.826  33.702  1   61.57 ? 290 GLN   B OE1  1 
ATOM   4788 N  NE2  . GLN   B 1 268 ? 69.37   84.124  32.717  1   59.51 ? 290 GLN   B NE2  1 
ATOM   4789 N  N    . PRO   B 1 269 ? 64.795  83.959  28.884  1   54    ? 291 PRO   B N    1 
ATOM   4790 C  CA   . PRO   B 1 269 ? 63.957  83.14   27.985  1   53.6  ? 291 PRO   B CA   1 
ATOM   4791 C  C    . PRO   B 1 269 ? 64.807  82.286  27.027  1   52.85 ? 291 PRO   B C    1 
ATOM   4792 O  O    . PRO   B 1 269 ? 64.409  81.168  26.698  1   52.62 ? 291 PRO   B O    1 
ATOM   4793 C  CB   . PRO   B 1 269 ? 63.126  84.186  27.224  1   54.39 ? 291 PRO   B CB   1 
ATOM   4794 C  CG   . PRO   B 1 269 ? 63.108  85.39   28.127  1   55.03 ? 291 PRO   B CG   1 
ATOM   4795 C  CD   . PRO   B 1 269 ? 64.477  85.399  28.75   1   53.57 ? 291 PRO   B CD   1 
ATOM   4796 N  N    . HIS   B 1 270 ? 65.99   82.79   26.607  1   52.19 ? 292 HIS   B N    1 
ATOM   4797 C  CA   . HIS   B 1 270 ? 66.868  82.008  25.738  1   52.52 ? 292 HIS   B CA   1 
ATOM   4798 C  C    . HIS   B 1 270 ? 67.516  80.838  26.501  1   52.85 ? 292 HIS   B C    1 
ATOM   4799 O  O    . HIS   B 1 270 ? 67.676  79.747  25.946  1   52.89 ? 292 HIS   B O    1 
ATOM   4800 C  CB   . HIS   B 1 270 ? 67.936  82.871  25.064  1   53.15 ? 292 HIS   B CB   1 
ATOM   4801 C  CG   . HIS   B 1 270 ? 68.78   82.065  24.132  1   56.01 ? 292 HIS   B CG   1 
ATOM   4802 N  ND1  . HIS   B 1 270 ? 70.021  81.584  24.516  1   57.95 ? 292 HIS   B ND1  1 
ATOM   4803 C  CD2  . HIS   B 1 270 ? 68.49   81.594  22.897  1   57.22 ? 292 HIS   B CD2  1 
ATOM   4804 C  CE1  . HIS   B 1 270 ? 70.468  80.887  23.484  1   58.52 ? 292 HIS   B CE1  1 
ATOM   4805 N  NE2  . HIS   B 1 270 ? 69.579  80.862  22.488  1   58.48 ? 292 HIS   B NE2  1 
ATOM   4806 N  N    . GLN   B 1 271 ? 67.862  81.068  27.777  1   52.56 ? 293 GLN   B N    1 
ATOM   4807 C  CA   . GLN   B 1 271 ? 68.419  80.038  28.647  1   52.83 ? 293 GLN   B CA   1 
ATOM   4808 C  C    . GLN   B 1 271 ? 67.378  78.946  28.897  1   51.71 ? 293 GLN   B C    1 
ATOM   4809 O  O    . GLN   B 1 271 ? 67.719  77.766  28.879  1   51.9  ? 293 GLN   B O    1 
ATOM   4810 C  CB   . GLN   B 1 271 ? 68.932  80.646  29.969  1   55.68 ? 293 GLN   B CB   1 
ATOM   4811 C  CG   . GLN   B 1 271 ? 69.82   79.707  30.789  1   62.13 ? 293 GLN   B CG   1 
ATOM   4812 C  CD   . GLN   B 1 271 ? 70.992  79.151  30.004  1   69.06 ? 293 GLN   B CD   1 
ATOM   4813 O  OE1  . GLN   B 1 271 ? 71.612  79.839  29.181  1   71.93 ? 293 GLN   B OE1  1 
ATOM   4814 N  NE2  . GLN   B 1 271 ? 71.307  77.883  30.226  1   69.93 ? 293 GLN   B NE2  1 
ATOM   4815 N  N    . LEU   B 1 272 ? 66.092  79.329  29.031  1   50.55 ? 294 LEU   B N    1 
ATOM   4816 C  CA   . LEU   B 1 272 ? 64.977  78.395  29.209  1   49.96 ? 294 LEU   B CA   1 
ATOM   4817 C  C    . LEU   B 1 272 ? 64.928  77.454  27.98   1   49.84 ? 294 LEU   B C    1 
ATOM   4818 O  O    . LEU   B 1 272 ? 64.904  76.237  28.141  1   50.62 ? 294 LEU   B O    1 
ATOM   4819 C  CB   . LEU   B 1 272 ? 63.654  79.182  29.379  1   49.48 ? 294 LEU   B CB   1 
ATOM   4820 C  CG   . LEU   B 1 272 ? 62.463  78.437  29.987  1   50.5  ? 294 LEU   B CG   1 
ATOM   4821 C  CD1  . LEU   B 1 272 ? 61.495  79.396  30.635  1   50.87 ? 294 LEU   B CD1  1 
ATOM   4822 C  CD2  . LEU   B 1 272 ? 61.729  77.604  28.94   1   51.03 ? 294 LEU   B CD2  1 
ATOM   4823 N  N    . LEU   B 1 273 ? 64.997  78.017  26.774  1   48.71 ? 295 LEU   B N    1 
ATOM   4824 C  CA   . LEU   B 1 273 ? 64.99   77.249  25.538  1   48.4  ? 295 LEU   B CA   1 
ATOM   4825 C  C    . LEU   B 1 273 ? 66.225  76.339  25.417  1   48.1  ? 295 LEU   B C    1 
ATOM   4826 O  O    . LEU   B 1 273 ? 66.091  75.187  25.026  1   48.93 ? 295 LEU   B O    1 
ATOM   4827 C  CB   . LEU   B 1 273 ? 64.906  78.228  24.347  1   48.28 ? 295 LEU   B CB   1 
ATOM   4828 C  CG   . LEU   B 1 273 ? 63.54   78.422  23.655  1   49.81 ? 295 LEU   B CG   1 
ATOM   4829 C  CD1  . LEU   B 1 273 ? 62.346  78.34   24.596  1   50.01 ? 295 LEU   B CD1  1 
ATOM   4830 C  CD2  . LEU   B 1 273 ? 63.534  79.659  22.76   1   50.4  ? 295 LEU   B CD2  1 
ATOM   4831 N  N    . THR   B 1 274 ? 67.413  76.851  25.758  1   46.96 ? 296 THR   B N    1 
ATOM   4832 C  CA   . THR   B 1 274 ? 68.675  76.103  25.728  1   46.27 ? 296 THR   B CA   1 
ATOM   4833 C  C    . THR   B 1 274 ? 68.614  74.866  26.635  1   44.42 ? 296 THR   B C    1 
ATOM   4834 O  O    . THR   B 1 274 ? 69.039  73.794  26.225  1   44.24 ? 296 THR   B O    1 
ATOM   4835 C  CB   . THR   B 1 274 ? 69.834  77.014  26.127  1   48.05 ? 296 THR   B CB   1 
ATOM   4836 O  OG1  . THR   B 1 274 ? 69.885  78.101  25.201  1   49.17 ? 296 THR   B OG1  1 
ATOM   4837 C  CG2  . THR   B 1 274 ? 71.164  76.298  26.098  1   48.91 ? 296 THR   B CG2  1 
ATOM   4838 N  N    . LEU   B 1 275 ? 68.033  75.008  27.831  1   42.76 ? 297 LEU   B N    1 
ATOM   4839 C  CA   . LEU   B 1 275 ? 67.894  73.922  28.794  1   41.96 ? 297 LEU   B CA   1 
ATOM   4840 C  C    . LEU   B 1 275 ? 66.905  72.857  28.346  1   41.84 ? 297 LEU   B C    1 
ATOM   4841 O  O    . LEU   B 1 275 ? 67.122  71.684  28.619  1   42.18 ? 297 LEU   B O    1 
ATOM   4842 C  CB   . LEU   B 1 275 ? 67.545  74.47   30.183  1   41.65 ? 297 LEU   B CB   1 
ATOM   4843 C  CG   . LEU   B 1 275 ? 68.647  75.311  30.802  1   42.53 ? 297 LEU   B CG   1 
ATOM   4844 C  CD1  . LEU   B 1 275 ? 68.151  76.03   32.016  1   42.81 ? 297 LEU   B CD1  1 
ATOM   4845 C  CD2  . LEU   B 1 275 ? 69.9    74.471  31.101  1   42.84 ? 297 LEU   B CD2  1 
ATOM   4846 N  N    . LEU   B 1 276 ? 65.859  73.246  27.605  1   41.51 ? 298 LEU   B N    1 
ATOM   4847 C  CA   . LEU   B 1 276 ? 64.885  72.306  27.033  1   41.43 ? 298 LEU   B CA   1 
ATOM   4848 C  C    . LEU   B 1 276 ? 65.606  71.435  25.983  1   40.87 ? 298 LEU   B C    1 
ATOM   4849 O  O    . LEU   B 1 276 ? 65.393  70.225  25.94   1   40.83 ? 298 LEU   B O    1 
ATOM   4850 C  CB   . LEU   B 1 276 ? 63.729  73.075  26.367  1   41.47 ? 298 LEU   B CB   1 
ATOM   4851 C  CG   . LEU   B 1 276 ? 62.742  73.738  27.316  1   43.24 ? 298 LEU   B CG   1 
ATOM   4852 C  CD1  . LEU   B 1 276 ? 61.73   74.576  26.538  1   43.83 ? 298 LEU   B CD1  1 
ATOM   4853 C  CD2  . LEU   B 1 276 ? 62.024  72.698  28.177  1   43.82 ? 298 LEU   B CD2  1 
ATOM   4854 N  N    . MET   B 1 277 ? 66.464  72.064  25.159  1   40.33 ? 299 MET   B N    1 
ATOM   4855 C  CA   . MET   B 1 277 ? 67.276  71.385  24.163  1   41.09 ? 299 MET   B CA   1 
ATOM   4856 C  C    . MET   B 1 277 ? 68.271  70.443  24.858  1   40.68 ? 299 MET   B C    1 
ATOM   4857 O  O    . MET   B 1 277 ? 68.409  69.3    24.427  1   40.99 ? 299 MET   B O    1 
ATOM   4858 C  CB   . MET   B 1 277 ? 68.052  72.407  23.321  1   42.92 ? 299 MET   B CB   1 
ATOM   4859 C  CG   . MET   B 1 277 ? 67.392  72.732  22.006  1   47.33 ? 299 MET   B CG   1 
ATOM   4860 S  SD   . MET   B 1 277 ? 68.303  73.926  20.981  1   56.45 ? 299 MET   B SD   1 
ATOM   4861 C  CE   . MET   B 1 277 ? 69.97   73.231  21.006  1   58.9  ? 299 MET   B CE   1 
ATOM   4862 N  N    . ASP   B 1 278 ? 68.946  70.911  25.935  1   39.35 ? 300 ASP   B N    1 
ATOM   4863 C  CA   . ASP   B 1 278 ? 69.902  70.113  26.694  1   38.87 ? 300 ASP   B CA   1 
ATOM   4864 C  C    . ASP   B 1 278 ? 69.251  68.881  27.299  1   37.92 ? 300 ASP   B C    1 
ATOM   4865 O  O    . ASP   B 1 278 ? 69.852  67.816  27.262  1   37.86 ? 300 ASP   B O    1 
ATOM   4866 C  CB   . ASP   B 1 278 ? 70.601  70.947  27.783  1   40.74 ? 300 ASP   B CB   1 
ATOM   4867 C  CG   . ASP   B 1 278 ? 71.548  72.003  27.24   1   46.82 ? 300 ASP   B CG   1 
ATOM   4868 O  OD1  . ASP   B 1 278 ? 71.941  71.9    26.06   1   48.21 ? 300 ASP   B OD1  1 
ATOM   4869 O  OD2  . ASP   B 1 278 ? 71.874  72.953  27.988  1   50.22 ? 300 ASP   B OD2  1 
ATOM   4870 N  N    . ILE   B 1 279 ? 68.016  69.013  27.809  1   37.28 ? 301 ILE   B N    1 
ATOM   4871 C  CA   . ILE   B 1 279 ? 67.262  67.903  28.386  1   37.21 ? 301 ILE   B CA   1 
ATOM   4872 C  C    . ILE   B 1 279 ? 66.929  66.88   27.311  1   37.42 ? 301 ILE   B C    1 
ATOM   4873 O  O    . ILE   B 1 279 ? 67.148  65.682  27.491  1   37.44 ? 301 ILE   B O    1 
ATOM   4874 C  CB   . ILE   B 1 279 ? 66.001  68.455  29.087  1   37.55 ? 301 ILE   B CB   1 
ATOM   4875 C  CG1  . ILE   B 1 279 ? 66.375  69.162  30.399  1   37.98 ? 301 ILE   B CG1  1 
ATOM   4876 C  CG2  . ILE   B 1 279 ? 64.925  67.391  29.306  1   37.87 ? 301 ILE   B CG2  1 
ATOM   4877 C  CD1  . ILE   B 1 279 ? 65.253  69.942  31.031  1   39.05 ? 301 ILE   B CD1  1 
ATOM   4878 N  N    . ASP   B 1 280 ? 66.459  67.373  26.158  1   37.39 ? 302 ASP   B N    1 
ATOM   4879 C  CA   . ASP   B 1 280 ? 66.104  66.573  24.991  1   37.41 ? 302 ASP   B CA   1 
ATOM   4880 C  C    . ASP   B 1 280 ? 67.302  65.739  24.545  1   36.84 ? 302 ASP   B C    1 
ATOM   4881 O  O    . ASP   B 1 280 ? 67.185  64.531  24.388  1   37.02 ? 302 ASP   B O    1 
ATOM   4882 C  CB   . ASP   B 1 280 ? 65.704  67.534  23.862  1   39.47 ? 302 ASP   B CB   1 
ATOM   4883 C  CG   . ASP   B 1 280 ? 64.48   67.169  23.085  1   45.07 ? 302 ASP   B CG   1 
ATOM   4884 O  OD1  . ASP   B 1 280 ? 63.752  66.247  23.517  1   44.67 ? 302 ASP   B OD1  1 
ATOM   4885 O  OD2  . ASP   B 1 280 ? 64.222  67.823  22.058  1   49.61 ? 302 ASP   B OD2  1 
ATOM   4886 N  N    . SER   B 1 281 ? 68.449  66.396  24.394  1   36.54 ? 303 SER   B N    1 
ATOM   4887 C  CA   . SER   B 1 281 ? 69.728  65.853  23.977  1   37.28 ? 303 SER   B CA   1 
ATOM   4888 C  C    . SER   B 1 281 ? 70.247  64.821  24.998  1   37.56 ? 303 SER   B C    1 
ATOM   4889 O  O    . SER   B 1 281 ? 70.712  63.758  24.604  1   38.26 ? 303 SER   B O    1 
ATOM   4890 C  CB   . SER   B 1 281 ? 70.716  67      23.837  1   39.35 ? 303 SER   B CB   1 
ATOM   4891 O  OG   . SER   B 1 281 ? 71.794  66.71   22.972  1   44.27 ? 303 SER   B OG   1 
ATOM   4892 N  N    . LEU   B 1 282 ? 70.115  65.107  26.301  1   36.64 ? 304 LEU   B N    1 
ATOM   4893 C  CA   . LEU   B 1 282 ? 70.551  64.195  27.354  1   36.12 ? 304 LEU   B CA   1 
ATOM   4894 C  C    . LEU   B 1 282 ? 69.698  62.927  27.443  1   35.75 ? 304 LEU   B C    1 
ATOM   4895 O  O    . LEU   B 1 282 ? 70.239  61.846  27.723  1   35.86 ? 304 LEU   B O    1 
ATOM   4896 C  CB   . LEU   B 1 282 ? 70.65   64.903  28.704  1   35.79 ? 304 LEU   B CB   1 
ATOM   4897 C  CG   . LEU   B 1 282 ? 71.932  65.699  28.867  1   35.98 ? 304 LEU   B CG   1 
ATOM   4898 C  CD1  . LEU   B 1 282 ? 71.797  66.746  29.941  1   36.25 ? 304 LEU   B CD1  1 
ATOM   4899 C  CD2  . LEU   B 1 282 ? 73.099  64.775  29.138  1   36.27 ? 304 LEU   B CD2  1 
ATOM   4900 N  N    . ILE   B 1 283 ? 68.388  63.034  27.156  1   34.68 ? 305 ILE   B N    1 
ATOM   4901 C  CA   . ILE   B 1 283 ? 67.529  61.845  27.107  1   33.62 ? 305 ILE   B CA   1 
ATOM   4902 C  C    . ILE   B 1 283 ? 67.97   60.951  25.937  1   32.9  ? 305 ILE   B C    1 
ATOM   4903 O  O    . ILE   B 1 283 ? 68.086  59.744  26.103  1   33.08 ? 305 ILE   B O    1 
ATOM   4904 C  CB   . ILE   B 1 283 ? 66.021  62.218  27.058  1   33.57 ? 305 ILE   B CB   1 
ATOM   4905 C  CG1  . ILE   B 1 283 ? 65.569  62.785  28.415  1   33.66 ? 305 ILE   B CG1  1 
ATOM   4906 C  CG2  . ILE   B 1 283 ? 65.16   61.011  26.676  1   33.87 ? 305 ILE   B CG2  1 
ATOM   4907 C  CD1  . ILE   B 1 283 ? 64.144  63.341  28.454  1   33.96 ? 305 ILE   B CD1  1 
ATOM   4908 N  N    . THR   B 1 284 ? 68.34   61.551  24.811  1   32.57 ? 306 THR   B N    1 
ATOM   4909 C  CA   . THR   B 1 284 ? 68.842  60.817  23.658  1   33.5  ? 306 THR   B CA   1 
ATOM   4910 C  C    . THR   B 1 284 ? 70.176  60.141  24.008  1   32.84 ? 306 THR   B C    1 
ATOM   4911 O  O    . THR   B 1 284 ? 70.371  58.986  23.651  1   32.5  ? 306 THR   B O    1 
ATOM   4912 C  CB   . THR   B 1 284 ? 68.978  61.746  22.441  1   35.16 ? 306 THR   B CB   1 
ATOM   4913 O  OG1  . THR   B 1 284 ? 67.704  62.312  22.168  1   37.02 ? 306 THR   B OG1  1 
ATOM   4914 C  CG2  . THR   B 1 284 ? 69.438  61.008  21.221  1   35.81 ? 306 THR   B CG2  1 
ATOM   4915 N  N    . LYS   B 1 285 ? 71.063  60.842  24.747  1   31.88 ? 307 LYS   B N    1 
ATOM   4916 C  CA   . LYS   B 1 285 ? 72.353  60.303  25.18   1   31.14 ? 307 LYS   B CA   1 
ATOM   4917 C  C    . LYS   B 1 285 ? 72.14   59.112  26.106  1   29.84 ? 307 LYS   B C    1 
ATOM   4918 O  O    . LYS   B 1 285 ? 72.878  58.125  25.989  1   31.07 ? 307 LYS   B O    1 
ATOM   4919 C  CB   . LYS   B 1 285 ? 73.238  61.377  25.842  1   33.12 ? 307 LYS   B CB   1 
ATOM   4920 C  CG   . LYS   B 1 285 ? 73.933  62.262  24.829  1   37.53 ? 307 LYS   B CG   1 
ATOM   4921 C  CD   . LYS   B 1 285 ? 74.798  63.351  25.453  1   41.73 ? 307 LYS   B CD   1 
ATOM   4922 C  CE   . LYS   B 1 285 ? 75.106  64.407  24.408  1   44.97 ? 307 LYS   B CE   1 
ATOM   4923 N  NZ   . LYS   B 1 285 ? 75.982  65.494  24.932  1   46.98 ? 307 LYS   B NZ   1 
ATOM   4924 N  N    . TRP   B 1 286 ? 71.122  59.162  26.987  1   27.26 ? 308 TRP   B N    1 
ATOM   4925 C  CA   . TRP   B 1 286 ? 70.813  58.028  27.837  1   26.34 ? 308 TRP   B CA   1 
ATOM   4926 C  C    . TRP   B 1 286 ? 70.339  56.859  26.959  1   27.89 ? 308 TRP   B C    1 
ATOM   4927 O  O    . TRP   B 1 286 ? 70.765  55.726  27.188  1   28.26 ? 308 TRP   B O    1 
ATOM   4928 C  CB   . TRP   B 1 286 ? 69.749  58.356  28.923  1   25.59 ? 308 TRP   B CB   1 
ATOM   4929 C  CG   . TRP   B 1 286 ? 69.426  57.129  29.733  1   25.3  ? 308 TRP   B CG   1 
ATOM   4930 C  CD1  . TRP   B 1 286 ? 70.194  56.597  30.726  1   25.85 ? 308 TRP   B CD1  1 
ATOM   4931 C  CD2  . TRP   B 1 286 ? 68.433  56.124  29.413  1   25.2  ? 308 TRP   B CD2  1 
ATOM   4932 N  NE1  . TRP   B 1 286 ? 69.698  55.372  31.105  1   26.11 ? 308 TRP   B NE1  1 
ATOM   4933 C  CE2  . TRP   B 1 286 ? 68.632  55.046  30.297  1   26.1  ? 308 TRP   B CE2  1 
ATOM   4934 C  CE3  . TRP   B 1 286 ? 67.412  56.023  28.448  1   25.25 ? 308 TRP   B CE3  1 
ATOM   4935 C  CZ2  . TRP   B 1 286 ? 67.793  53.917  30.302  1   26.53 ? 308 TRP   B CZ2  1 
ATOM   4936 C  CZ3  . TRP   B 1 286 ? 66.615  54.887  28.427  1   25.61 ? 308 TRP   B CZ3  1 
ATOM   4937 C  CH2  . TRP   B 1 286 ? 66.796  53.862  29.356  1   25.69 ? 308 TRP   B CH2  1 
ATOM   4938 N  N    . ARG   B 1 287 ? 69.463  57.136  25.956  1   28.36 ? 309 ARG   B N    1 
ATOM   4939 C  CA   . ARG   B 1 287 ? 68.951  56.12   25.039  1   29.41 ? 309 ARG   B CA   1 
ATOM   4940 C  C    . ARG   B 1 287 ? 70.098  55.42   24.31   1   30.19 ? 309 ARG   B C    1 
ATOM   4941 O  O    . ARG   B 1 287 ? 70.112  54.19   24.234  1   30.6  ? 309 ARG   B O    1 
ATOM   4942 C  CB   . ARG   B 1 287 ? 67.983  56.741  24      1   30.63 ? 309 ARG   B CB   1 
ATOM   4943 C  CG   . ARG   B 1 287 ? 66.654  57.256  24.548  1   32.57 ? 309 ARG   B CG   1 
ATOM   4944 C  CD   . ARG   B 1 287 ? 65.747  57.645  23.389  1   35.66 ? 309 ARG   B CD   1 
ATOM   4945 N  NE   . ARG   B 1 287 ? 64.639  58.528  23.776  1   35.33 ? 309 ARG   B NE   1 
ATOM   4946 C  CZ   . ARG   B 1 287 ? 63.49   58.106  24.291  1   34.76 ? 309 ARG   B CZ   1 
ATOM   4947 N  NH1  . ARG   B 1 287 ? 62.545  58.978  24.624  1   33.08 ? 309 ARG   B NH1  1 
ATOM   4948 N  NH2  . ARG   B 1 287 ? 63.285  56.813  24.507  1   34.74 ? 309 ARG   B NH2  1 
ATOM   4949 N  N    . TYR   B 1 288 ? 71.077  56.19   23.819  1   30.17 ? 310 TYR   B N    1 
ATOM   4950 C  CA   . TYR   B 1 288 ? 72.224  55.644  23.104  1   31.17 ? 310 TYR   B CA   1 
ATOM   4951 C  C    . TYR   B 1 288 ? 73.07   54.771  24.03   1   30.12 ? 310 TYR   B C    1 
ATOM   4952 O  O    . TYR   B 1 288 ? 73.356  53.624  23.69   1   30    ? 310 TYR   B O    1 
ATOM   4953 C  CB   . TYR   B 1 288 ? 73.05   56.782  22.476  1   33.29 ? 310 TYR   B CB   1 
ATOM   4954 C  CG   . TYR   B 1 288 ? 74.311  56.312  21.781  1   37.29 ? 310 TYR   B CG   1 
ATOM   4955 C  CD1  . TYR   B 1 288 ? 74.256  55.713  20.534  1   39.66 ? 310 TYR   B CD1  1 
ATOM   4956 C  CD2  . TYR   B 1 288 ? 75.556  56.465  22.373  1   39.66 ? 310 TYR   B CD2  1 
ATOM   4957 C  CE1  . TYR   B 1 288 ? 75.41   55.284  19.885  1   41.91 ? 310 TYR   B CE1  1 
ATOM   4958 C  CE2  . TYR   B 1 288 ? 76.713  55.999  21.755  1   41.78 ? 310 TYR   B CE2  1 
ATOM   4959 C  CZ   . TYR   B 1 288 ? 76.641  55.424  20.499  1   43.82 ? 310 TYR   B CZ   1 
ATOM   4960 O  OH   . TYR   B 1 288 ? 77.782  54.947  19.87   1   47.01 ? 310 TYR   B OH   1 
ATOM   4961 N  N    . ASN   B 1 289 ? 73.397  55.268  25.238  1   29.09 ? 311 ASN   B N    1 
ATOM   4962 C  CA   . ASN   B 1 289 ? 74.195  54.492  26.182  1   29.05 ? 311 ASN   B CA   1 
ATOM   4963 C  C    . ASN   B 1 289 ? 73.49   53.228  26.645  1   28.48 ? 311 ASN   B C    1 
ATOM   4964 O  O    . ASN   B 1 289 ? 74.134  52.194  26.852  1   27.47 ? 311 ASN   B O    1 
ATOM   4965 C  CB   . ASN   B 1 289 ? 74.664  55.357  27.351  1   31.27 ? 311 ASN   B CB   1 
ATOM   4966 C  CG   . ASN   B 1 289 ? 75.819  56.228  26.93   1   36.73 ? 311 ASN   B CG   1 
ATOM   4967 O  OD1  . ASN   B 1 289 ? 75.647  57.338  26.438  1   40.48 ? 311 ASN   B OD1  1 
ATOM   4968 N  ND2  . ASN   B 1 289 ? 77.012  55.721  27.032  1   37.51 ? 311 ASN   B ND2  1 
ATOM   4969 N  N    . HIS   B 1 290 ? 72.156  53.297  26.786  1   28.75 ? 312 HIS   B N    1 
ATOM   4970 C  CA   . HIS   B 1 290 ? 71.363  52.139  27.171  1   28.65 ? 312 HIS   B CA   1 
ATOM   4971 C  C    . HIS   B 1 290 ? 71.428  51.068  26.066  1   28.7  ? 312 HIS   B C    1 
ATOM   4972 O  O    . HIS   B 1 290 ? 71.704  49.924  26.402  1   28.64 ? 312 HIS   B O    1 
ATOM   4973 C  CB   . HIS   B 1 290 ? 69.917  52.577  27.49   1   28.89 ? 312 HIS   B CB   1 
ATOM   4974 C  CG   . HIS   B 1 290 ? 68.953  51.449  27.697  1   29.31 ? 312 HIS   B CG   1 
ATOM   4975 N  ND1  . HIS   B 1 290 ? 68.007  51.114  26.731  1   30.3  ? 312 HIS   B ND1  1 
ATOM   4976 C  CD2  . HIS   B 1 290 ? 68.812  50.615  28.751  1   30.35 ? 312 HIS   B CD2  1 
ATOM   4977 C  CE1  . HIS   B 1 290 ? 67.332  50.082  27.222  1   30.71 ? 312 HIS   B CE1  1 
ATOM   4978 N  NE2  . HIS   B 1 290 ? 67.762  49.75   28.438  1   31.28 ? 312 HIS   B NE2  1 
ATOM   4979 N  N    . VAL   B 1 291 ? 71.254  51.433  24.751  1   29.11 ? 313 VAL   B N    1 
ATOM   4980 C  CA   . VAL   B 1 291 ? 71.325  50.448  23.64   1   30.22 ? 313 VAL   B CA   1 
ATOM   4981 C  C    . VAL   B 1 291 ? 72.704  49.793  23.566  1   29.35 ? 313 VAL   B C    1 
ATOM   4982 O  O    . VAL   B 1 291 ? 72.79   48.59   23.311  1   29.32 ? 313 VAL   B O    1 
ATOM   4983 C  CB   . VAL   B 1 291 ? 70.924  50.958  22.212  1   32.76 ? 313 VAL   B CB   1 
ATOM   4984 C  CG1  . VAL   B 1 291 ? 70.53   49.787  21.32   1   34.06 ? 313 VAL   B CG1  1 
ATOM   4985 C  CG2  . VAL   B 1 291 ? 69.78   51.931  22.26   1   34.49 ? 313 VAL   B CG2  1 
ATOM   4986 N  N    . ILE   B 1 292 ? 73.784  50.574  23.771  1   28.52 ? 314 ILE   B N    1 
ATOM   4987 C  CA   . ILE   B 1 292 ? 75.141  50.033  23.761  1   28.66 ? 314 ILE   B CA   1 
ATOM   4988 C  C    . ILE   B 1 292 ? 75.297  48.987  24.879  1   28.11 ? 314 ILE   B C    1 
ATOM   4989 O  O    . ILE   B 1 292 ? 75.845  47.911  24.646  1   28.7  ? 314 ILE   B O    1 
ATOM   4990 C  CB   . ILE   B 1 292 ? 76.202  51.181  23.885  1   29.8  ? 314 ILE   B CB   1 
ATOM   4991 C  CG1  . ILE   B 1 292 ? 76.06   52.223  22.746  1   31.52 ? 314 ILE   B CG1  1 
ATOM   4992 C  CG2  . ILE   B 1 292 ? 77.639  50.639  23.972  1   29.45 ? 314 ILE   B CG2  1 
ATOM   4993 C  CD1  . ILE   B 1 292 ? 76.137  51.63   21.329  1   33.83 ? 314 ILE   B CD1  1 
ATOM   4994 N  N    . MET   B 1 293 ? 74.765  49.285  26.069  1   26.98 ? 315 MET   B N    1 
ATOM   4995 C  CA   . MET   B 1 293 ? 74.841  48.368  27.199  1   26.57 ? 315 MET   B CA   1 
ATOM   4996 C  C    . MET   B 1 293 ? 74.021  47.095  26.917  1   26.85 ? 315 MET   B C    1 
ATOM   4997 O  O    . MET   B 1 293 ? 74.494  45.985  27.183  1   26.52 ? 315 MET   B O    1 
ATOM   4998 C  CB   . MET   B 1 293 ? 74.375  49.055  28.503  1   25.83 ? 315 MET   B CB   1 
ATOM   4999 C  CG   . MET   B 1 293 ? 74.218  48.096  29.688  1   26.14 ? 315 MET   B CG   1 
ATOM   5000 S  SD   . MET   B 1 293 ? 73.736  48.926  31.22   1   29.44 ? 315 MET   B SD   1 
ATOM   5001 C  CE   . MET   B 1 293 ? 72.241  49.878  30.651  1   20.63 ? 315 MET   B CE   1 
ATOM   5002 N  N    . VAL   B 1 294 ? 72.792  47.252  26.374  1   27.21 ? 316 VAL   B N    1 
ATOM   5003 C  CA   . VAL   B 1 294 ? 71.915  46.131  26.006  1   27.64 ? 316 VAL   B CA   1 
ATOM   5004 C  C    . VAL   B 1 294 ? 72.654  45.219  25.022  1   28.03 ? 316 VAL   B C    1 
ATOM   5005 O  O    . VAL   B 1 294 ? 72.738  44.018  25.24   1   27.88 ? 316 VAL   B O    1 
ATOM   5006 C  CB   . VAL   B 1 294 ? 70.581  46.626  25.388  1   28.85 ? 316 VAL   B CB   1 
ATOM   5007 C  CG1  . VAL   B 1 294 ? 69.778  45.451  24.821  1   29.69 ? 316 VAL   B CG1  1 
ATOM   5008 C  CG2  . VAL   B 1 294 ? 69.748  47.428  26.391  1   28.81 ? 316 VAL   B CG2  1 
ATOM   5009 N  N    . GLN   B 1 295 ? 73.289  45.82   24.002  1   28.55 ? 317 GLN   B N    1 
ATOM   5010 C  CA   . GLN   B 1 295 ? 74.022  45.055  23.017  1   29.41 ? 317 GLN   B CA   1 
ATOM   5011 C  C    . GLN   B 1 295 ? 75.234  44.346  23.574  1   30.24 ? 317 GLN   B C    1 
ATOM   5012 O  O    . GLN   B 1 295 ? 75.514  43.217  23.162  1   30.11 ? 317 GLN   B O    1 
ATOM   5013 C  CB   . GLN   B 1 295 ? 74.399  45.897  21.808  1   30.31 ? 317 GLN   B CB   1 
ATOM   5014 C  CG   . GLN   B 1 295 ? 74.676  45.001  20.617  1   33.34 ? 317 GLN   B CG   1 
ATOM   5015 C  CD   . GLN   B 1 295 ? 75.126  45.752  19.392  1   37.62 ? 317 GLN   B CD   1 
ATOM   5016 O  OE1  . GLN   B 1 295 ? 75.482  46.939  19.448  1   39.53 ? 317 GLN   B OE1  1 
ATOM   5017 N  NE2  . GLN   B 1 295 ? 75.125  45.054  18.264  1   37.03 ? 317 GLN   B NE2  1 
ATOM   5018 N  N    . ARG   B 1 296 ? 75.949  44.983  24.512  1   30.7  ? 318 ARG   B N    1 
ATOM   5019 C  CA   . ARG   B 1 296 ? 77.097  44.338  25.119  1   31.43 ? 318 ARG   B CA   1 
ATOM   5020 C  C    . ARG   B 1 296 ? 76.67   43.239  26.114  1   29.53 ? 318 ARG   B C    1 
ATOM   5021 O  O    . ARG   B 1 296 ? 77.398  42.271  26.264  1   28.81 ? 318 ARG   B O    1 
ATOM   5022 C  CB   . ARG   B 1 296 ? 78.083  45.361  25.704  1   35.57 ? 318 ARG   B CB   1 
ATOM   5023 C  CG   . ARG   B 1 296 ? 78.863  46.068  24.57   1   43.89 ? 318 ARG   B CG   1 
ATOM   5024 C  CD   . ARG   B 1 296 ? 80.281  46.45   24.981  1   50.41 ? 318 ARG   B CD   1 
ATOM   5025 N  NE   . ARG   B 1 296 ? 80.456  47.868  25.286  1   55.51 ? 318 ARG   B NE   1 
ATOM   5026 C  CZ   . ARG   B 1 296 ? 80.237  48.417  26.483  1   59.11 ? 318 ARG   B CZ   1 
ATOM   5027 N  NH1  . ARG   B 1 296 ? 79.729  47.685  27.476  1   57.49 ? 318 ARG   B NH1  1 
ATOM   5028 N  NH2  . ARG   B 1 296 ? 80.461  49.716  26.677  1   58.9  ? 318 ARG   B NH2  1 
ATOM   5029 N  N    . MET   B 1 297 ? 75.467  43.324  26.711  1   29.32 ? 319 MET   B N    1 
ATOM   5030 C  CA   . MET   B 1 297 ? 74.993  42.284  27.631  1   29.66 ? 319 MET   B CA   1 
ATOM   5031 C  C    . MET   B 1 297 ? 74.368  41.087  26.943  1   29.72 ? 319 MET   B C    1 
ATOM   5032 O  O    . MET   B 1 297 ? 74.651  39.958  27.337  1   29.84 ? 319 MET   B O    1 
ATOM   5033 C  CB   . MET   B 1 297 ? 73.964  42.824  28.624  1   30.46 ? 319 MET   B CB   1 
ATOM   5034 C  CG   . MET   B 1 297 ? 74.532  43.707  29.621  1   33.61 ? 319 MET   B CG   1 
ATOM   5035 S  SD   . MET   B 1 297 ? 75.551  42.937  30.904  1   35.31 ? 319 MET   B SD   1 
ATOM   5036 C  CE   . MET   B 1 297 ? 75.849  44.476  31.824  1   31.98 ? 319 MET   B CE   1 
ATOM   5037 N  N    . ILE   B 1 298 ? 73.44   41.323  25.988  1   29.68 ? 320 ILE   B N    1 
ATOM   5038 C  CA   . ILE   B 1 298 ? 72.664  40.259  25.346  1   30.42 ? 320 ILE   B CA   1 
ATOM   5039 C  C    . ILE   B 1 298 ? 72.673  40.301  23.815  1   31.55 ? 320 ILE   B C    1 
ATOM   5040 O  O    . ILE   B 1 298 ? 71.87   39.629  23.199  1   32.68 ? 320 ILE   B O    1 
ATOM   5041 C  CB   . ILE   B 1 298 ? 71.212  40.299  25.891  1   30.61 ? 320 ILE   B CB   1 
ATOM   5042 C  CG1  . ILE   B 1 298 ? 70.549  41.653  25.56   1   31.9  ? 320 ILE   B CG1  1 
ATOM   5043 C  CG2  . ILE   B 1 298 ? 71.174  40.029  27.404  1   30.3  ? 320 ILE   B CG2  1 
ATOM   5044 C  CD1  . ILE   B 1 298 ? 69.124  41.823  26.018  1   33.45 ? 320 ILE   B CD1  1 
ATOM   5045 N  N    . GLY   B 1 299 ? 73.566  41.073  23.212  1   31.02 ? 321 GLY   B N    1 
ATOM   5046 C  CA   . GLY   B 1 299 ? 73.648  41.197  21.766  1   31.04 ? 321 GLY   B CA   1 
ATOM   5047 C  C    . GLY   B 1 299 ? 72.407  41.776  21.125  1   31.63 ? 321 GLY   B C    1 
ATOM   5048 O  O    . GLY   B 1 299 ? 71.583  42.397  21.801  1   32.29 ? 321 GLY   B O    1 
ATOM   5049 N  N    . SER   B 1 300 ? 72.263  41.604  19.809  1   31.2  ? 322 SER   B N    1 
ATOM   5050 C  CA   . SER   B 1 300 ? 71.032  42.046  19.118  1   30.9  ? 322 SER   B CA   1 
ATOM   5051 C  C    . SER   B 1 300 ? 69.841  41.055  19.374  1   31.19 ? 322 SER   B C    1 
ATOM   5052 O  O    . SER   B 1 300 ? 68.667  41.421  19.221  1   30.79 ? 322 SER   B O    1 
ATOM   5053 C  CB   . SER   B 1 300 ? 71.27   42.23   17.625  1   30.37 ? 322 SER   B CB   1 
ATOM   5054 O  OG   . SER   B 1 300 ? 72.007  41.16   17.073  1   32.06 ? 322 SER   B OG   1 
ATOM   5055 N  N    . GLN   B 1 301 ? 70.155  39.82   19.798  1   31.21 ? 323 GLN   B N    1 
ATOM   5056 C  CA   . GLN   B 1 301 ? 69.168  38.795  20.145  1   31.45 ? 323 GLN   B CA   1 
ATOM   5057 C  C    . GLN   B 1 301 ? 69.791  37.706  21.004  1   31.82 ? 323 GLN   B C    1 
ATOM   5058 O  O    . GLN   B 1 301 ? 70.967  37.41   20.867  1   32.75 ? 323 GLN   B O    1 
ATOM   5059 C  CB   . GLN   B 1 301 ? 68.449  38.212  18.919  1   31.54 ? 323 GLN   B CB   1 
ATOM   5060 C  CG   . GLN   B 1 301 ? 69.355  37.769  17.796  1   32.41 ? 323 GLN   B CG   1 
ATOM   5061 C  CD   . GLN   B 1 301 ? 68.519  37.261  16.641  1   32.59 ? 323 GLN   B CD   1 
ATOM   5062 O  OE1  . GLN   B 1 301 ? 67.786  36.268  16.771  1   32.67 ? 323 GLN   B OE1  1 
ATOM   5063 N  NE2  . GLN   B 1 301 ? 68.618  37.925  15.499  1   30.75 ? 323 GLN   B NE2  1 
ATOM   5064 N  N    . GLN   B 1 302 ? 69.017  37.147  21.919  1   31.45 ? 324 GLN   B N    1 
ATOM   5065 C  CA   . GLN   B 1 302 ? 69.498  36.096  22.806  1   32.18 ? 324 GLN   B CA   1 
ATOM   5066 C  C    . GLN   B 1 302 ? 68.361  35.124  23.188  1   32.97 ? 324 GLN   B C    1 
ATOM   5067 O  O    . GLN   B 1 302 ? 67.193  35.373  22.863  1   33.41 ? 324 GLN   B O    1 
ATOM   5068 C  CB   . GLN   B 1 302 ? 70.177  36.707  24.069  1   32.55 ? 324 GLN   B CB   1 
ATOM   5069 C  CG   . GLN   B 1 302 ? 71.711  36.566  24.082  1   32.72 ? 324 GLN   B CG   1 
ATOM   5070 C  CD   . GLN   B 1 302 ? 72.196  35.148  24.193  1   34.26 ? 324 GLN   B CD   1 
ATOM   5071 O  OE1  . GLN   B 1 302 ? 71.503  34.26   24.712  1   35.36 ? 324 GLN   B OE1  1 
ATOM   5072 N  NE2  . GLN   B 1 302 ? 73.405  34.893  23.731  1   33.44 ? 324 GLN   B NE2  1 
ATOM   5073 N  N    . LEU   B 1 303 ? 68.695  34.025  23.906  1   33.2  ? 325 LEU   B N    1 
ATOM   5074 C  CA   . LEU   B 1 303 ? 67.721  33.055  24.403  1   34.23 ? 325 LEU   B CA   1 
ATOM   5075 C  C    . LEU   B 1 303 ? 66.772  33.769  25.34   1   34.93 ? 325 LEU   B C    1 
ATOM   5076 O  O    . LEU   B 1 303 ? 67.21   34.398  26.289  1   35.46 ? 325 LEU   B O    1 
ATOM   5077 C  CB   . LEU   B 1 303 ? 68.416  31.919  25.162  1   34.68 ? 325 LEU   B CB   1 
ATOM   5078 C  CG   . LEU   B 1 303 ? 67.515  30.727  25.486  1   36.16 ? 325 LEU   B CG   1 
ATOM   5079 C  CD1  . LEU   B 1 303 ? 67.25   29.893  24.24   1   36.39 ? 325 LEU   B CD1  1 
ATOM   5080 C  CD2  . LEU   B 1 303 ? 68.136  29.867  26.557  1   36.76 ? 325 LEU   B CD2  1 
ATOM   5081 N  N    . GLY   B 1 304 ? 65.504  33.77   24.991  1   34.85 ? 326 GLY   B N    1 
ATOM   5082 C  CA   . GLY   B 1 304 ? 64.47   34.432  25.755  1   35.42 ? 326 GLY   B CA   1 
ATOM   5083 C  C    . GLY   B 1 304 ? 63.933  35.679  25.084  1   37.09 ? 326 GLY   B C    1 
ATOM   5084 O  O    . GLY   B 1 304 ? 62.895  36.183  25.509  1   38.72 ? 326 GLY   B O    1 
ATOM   5085 N  N    . THR   B 1 305 ? 64.626  36.218  24.049  1   36.33 ? 327 THR   B N    1 
ATOM   5086 C  CA   . THR   B 1 305 ? 64.176  37.459  23.414  1   36.04 ? 327 THR   B CA   1 
ATOM   5087 C  C    . THR   B 1 305 ? 63.247  37.275  22.212  1   36.16 ? 327 THR   B C    1 
ATOM   5088 O  O    . THR   B 1 305 ? 62.672  38.254  21.752  1   37.24 ? 327 THR   B O    1 
ATOM   5089 C  CB   . THR   B 1 305 ? 65.372  38.344  23.036  1   36.78 ? 327 THR   B CB   1 
ATOM   5090 O  OG1  . THR   B 1 305 ? 66.04   37.806  21.88   1   36.9  ? 327 THR   B OG1  1 
ATOM   5091 C  CG2  . THR   B 1 305 ? 66.354  38.553  24.212  1   36.72 ? 327 THR   B CG2  1 
ATOM   5092 N  N    . GLY   B 1 306 ? 63.135  36.069  21.688  1   35.55 ? 328 GLY   B N    1 
ATOM   5093 C  CA   . GLY   B 1 306 ? 62.28   35.807  20.531  1   35.79 ? 328 GLY   B CA   1 
ATOM   5094 C  C    . GLY   B 1 306 ? 62.677  36.595  19.295  1   35.47 ? 328 GLY   B C    1 
ATOM   5095 O  O    . GLY   B 1 306 ? 61.82   37.134  18.595  1   35.1  ? 328 GLY   B O    1 
ATOM   5096 N  N    . GLY   B 1 307 ? 63.986  36.699  19.048  1   35.13 ? 329 GLY   B N    1 
ATOM   5097 C  CA   . GLY   B 1 307 ? 64.485  37.477  17.921  1   34.56 ? 329 GLY   B CA   1 
ATOM   5098 C  C    . GLY   B 1 307 ? 65.036  38.839  18.312  1   33.77 ? 329 GLY   B C    1 
ATOM   5099 O  O    . GLY   B 1 307 ? 65.289  39.09   19.483  1   33.35 ? 329 GLY   B O    1 
ATOM   5100 N  N    . SER   B 1 308 ? 65.233  39.727  17.329  1   33.61 ? 330 SER   B N    1 
ATOM   5101 C  CA   . SER   B 1 308 ? 65.862  41.027  17.525  1   33.8  ? 330 SER   B CA   1 
ATOM   5102 C  C    . SER   B 1 308 ? 64.954  42.237  17.62   1   34.83 ? 330 SER   B C    1 
ATOM   5103 O  O    . SER   B 1 308 ? 65.46   43.353  17.598  1   34.94 ? 330 SER   B O    1 
ATOM   5104 C  CB   . SER   B 1 308 ? 66.878  41.284  16.426  1   34.01 ? 330 SER   B CB   1 
ATOM   5105 O  OG   . SER   B 1 308 ? 66.262  41.224  15.155  1   35.65 ? 330 SER   B OG   1 
ATOM   5106 N  N    . SER   B 1 309 ? 63.647  42.044  17.77   1   35.33 ? 331 SER   B N    1 
ATOM   5107 C  CA   . SER   B 1 309 ? 62.708  43.167  17.808  1   36.44 ? 331 SER   B CA   1 
ATOM   5108 C  C    . SER   B 1 309 ? 62.947  44.152  18.964  1   35.77 ? 331 SER   B C    1 
ATOM   5109 O  O    . SER   B 1 309 ? 62.791  45.353  18.768  1   35.47 ? 331 SER   B O    1 
ATOM   5110 C  CB   . SER   B 1 309 ? 61.258  42.687  17.784  1   39.26 ? 331 SER   B CB   1 
ATOM   5111 O  OG   . SER   B 1 309 ? 61.09   41.536  18.595  1   44.89 ? 331 SER   B OG   1 
ATOM   5112 N  N    . GLY   B 1 310 ? 63.344  43.66   20.131  1   35.35 ? 332 GLY   B N    1 
ATOM   5113 C  CA   . GLY   B 1 310 ? 63.638  44.532  21.267  1   35.28 ? 332 GLY   B CA   1 
ATOM   5114 C  C    . GLY   B 1 310 ? 64.792  45.475  20.977  1   35.2  ? 332 GLY   B C    1 
ATOM   5115 O  O    . GLY   B 1 310 ? 64.669  46.691  21.122  1   34.72 ? 332 GLY   B O    1 
ATOM   5116 N  N    . TYR   B 1 311 ? 65.903  44.916  20.5    1   35.71 ? 333 TYR   B N    1 
ATOM   5117 C  CA   . TYR   B 1 311 ? 67.084  45.683  20.122  1   36.78 ? 333 TYR   B CA   1 
ATOM   5118 C  C    . TYR   B 1 311 ? 66.758  46.687  19.009  1   36.27 ? 333 TYR   B C    1 
ATOM   5119 O  O    . TYR   B 1 311 ? 67.154  47.856  19.094  1   36.26 ? 333 TYR   B O    1 
ATOM   5120 C  CB   . TYR   B 1 311 ? 68.193  44.721  19.664  1   37.81 ? 333 TYR   B CB   1 
ATOM   5121 C  CG   . TYR   B 1 311 ? 69.408  45.424  19.109  1   40.02 ? 333 TYR   B CG   1 
ATOM   5122 C  CD1  . TYR   B 1 311 ? 70.279  46.113  19.945  1   41.37 ? 333 TYR   B CD1  1 
ATOM   5123 C  CD2  . TYR   B 1 311 ? 69.677  45.418  17.747  1   41.25 ? 333 TYR   B CD2  1 
ATOM   5124 C  CE1  . TYR   B 1 311 ? 71.396  46.766  19.44   1   42.46 ? 333 TYR   B CE1  1 
ATOM   5125 C  CE2  . TYR   B 1 311 ? 70.786  46.074  17.231  1   42.7  ? 333 TYR   B CE2  1 
ATOM   5126 C  CZ   . TYR   B 1 311 ? 71.647  46.744  18.083  1   44.15 ? 333 TYR   B CZ   1 
ATOM   5127 O  OH   . TYR   B 1 311 ? 72.741  47.398  17.572  1   47.16 ? 333 TYR   B OH   1 
ATOM   5128 N  N    . GLN   B 1 312 ? 66.041  46.228  17.967  1   35.52 ? 334 GLN   B N    1 
ATOM   5129 C  CA   . GLN   B 1 312 ? 65.679  47.081  16.842  1   35.48 ? 334 GLN   B CA   1 
ATOM   5130 C  C    . GLN   B 1 312 ? 64.757  48.201  17.249  1   33.29 ? 334 GLN   B C    1 
ATOM   5131 O  O    . GLN   B 1 312 ? 64.932  49.321  16.791  1   33.02 ? 334 GLN   B O    1 
ATOM   5132 C  CB   . GLN   B 1 312 ? 65.12   46.267  15.664  1   38.8  ? 334 GLN   B CB   1 
ATOM   5133 C  CG   . GLN   B 1 312 ? 66.204  45.444  14.977  1   46.15 ? 334 GLN   B CG   1 
ATOM   5134 C  CD   . GLN   B 1 312 ? 67.32   46.283  14.352  1   54.72 ? 334 GLN   B CD   1 
ATOM   5135 O  OE1  . GLN   B 1 312 ? 68.47   45.83   14.224  1   56.93 ? 334 GLN   B OE1  1 
ATOM   5136 N  NE2  . GLN   B 1 312 ? 67.017  47.517  13.911  1   56.54 ? 334 GLN   B NE2  1 
ATOM   5137 N  N    . TYR   B 1 313 ? 63.847  47.939  18.188  1   32.25 ? 335 TYR   B N    1 
ATOM   5138 C  CA   . TYR   B 1 313 ? 62.988  48.985  18.722  1   31.91 ? 335 TYR   B CA   1 
ATOM   5139 C  C    . TYR   B 1 313 ? 63.853  50.032  19.444  1   31.29 ? 335 TYR   B C    1 
ATOM   5140 O  O    . TYR   B 1 313 ? 63.685  51.212  19.207  1   31.3  ? 335 TYR   B O    1 
ATOM   5141 C  CB   . TYR   B 1 313 ? 61.916  48.403  19.671  1   32.18 ? 335 TYR   B CB   1 
ATOM   5142 C  CG   . TYR   B 1 313 ? 61.305  49.464  20.562  1   32.98 ? 335 TYR   B CG   1 
ATOM   5143 C  CD1  . TYR   B 1 313 ? 60.344  50.337  20.074  1   33.55 ? 335 TYR   B CD1  1 
ATOM   5144 C  CD2  . TYR   B 1 313 ? 61.779  49.673  21.85   1   33.67 ? 335 TYR   B CD2  1 
ATOM   5145 C  CE1  . TYR   B 1 313 ? 59.816  51.343  20.872  1   34.59 ? 335 TYR   B CE1  1 
ATOM   5146 C  CE2  . TYR   B 1 313 ? 61.302  50.711  22.632  1   34.59 ? 335 TYR   B CE2  1 
ATOM   5147 C  CZ   . TYR   B 1 313 ? 60.289  51.516  22.159  1   35.31 ? 335 TYR   B CZ   1 
ATOM   5148 O  OH   . TYR   B 1 313 ? 59.804  52.52   22.956  1   36.61 ? 335 TYR   B OH   1 
ATOM   5149 N  N    . LEU   B 1 314 ? 64.788  49.595  20.302  1   31.09 ? 336 LEU   B N    1 
ATOM   5150 C  CA   . LEU   B 1 314 ? 65.652  50.526  21.037  1   30.77 ? 336 LEU   B CA   1 
ATOM   5151 C  C    . LEU   B 1 314 ? 66.481  51.389  20.095  1   31.51 ? 336 LEU   B C    1 
ATOM   5152 O  O    . LEU   B 1 314 ? 66.613  52.584  20.342  1   31.35 ? 336 LEU   B O    1 
ATOM   5153 C  CB   . LEU   B 1 314 ? 66.556  49.775  22.012  1   29.85 ? 336 LEU   B CB   1 
ATOM   5154 C  CG   . LEU   B 1 314 ? 65.841  49.065  23.146  1   30.27 ? 336 LEU   B CG   1 
ATOM   5155 C  CD1  . LEU   B 1 314 ? 66.838  48.214  23.959  1   30.38 ? 336 LEU   B CD1  1 
ATOM   5156 C  CD2  . LEU   B 1 314 ? 65.087  50.07   24.044  1   29.65 ? 336 LEU   B CD2  1 
ATOM   5157 N  N    . ARG   B 1 315 ? 66.996  50.804  18.991  1   32.23 ? 337 ARG   B N    1 
ATOM   5158 C  CA   . ARG   B 1 315 ? 67.762  51.584  18.015  1   33.78 ? 337 ARG   B CA   1 
ATOM   5159 C  C    . ARG   B 1 315 ? 66.863  52.648  17.326  1   34.95 ? 337 ARG   B C    1 
ATOM   5160 O  O    . ARG   B 1 315 ? 67.351  53.727  16.984  1   35.61 ? 337 ARG   B O    1 
ATOM   5161 C  CB   . ARG   B 1 315 ? 68.387  50.67   16.949  1   35.45 ? 337 ARG   B CB   1 
ATOM   5162 C  CG   . ARG   B 1 315 ? 69.415  49.704  17.468  1   39.45 ? 337 ARG   B CG   1 
ATOM   5163 C  CD   . ARG   B 1 315 ? 70.754  50.39   17.642  1   43.62 ? 337 ARG   B CD   1 
ATOM   5164 N  N    . SER   B 1 316 ? 65.572  52.344  17.113  1   35.13 ? 338 SER   B N    1 
ATOM   5165 C  CA   . SER   B 1 316 ? 64.672  53.298  16.461  1   36.46 ? 338 SER   B CA   1 
ATOM   5166 C  C    . SER   B 1 316 ? 64.255  54.455  17.381  1   37.68 ? 338 SER   B C    1 
ATOM   5167 O  O    . SER   B 1 316 ? 63.827  55.501  16.881  1   38.08 ? 338 SER   B O    1 
ATOM   5168 C  CB   . SER   B 1 316 ? 63.457  52.603  15.855  1   37.38 ? 338 SER   B CB   1 
ATOM   5169 O  OG   . SER   B 1 316 ? 62.647  52.032  16.862  1   39.08 ? 338 SER   B OG   1 
ATOM   5170 N  N    . THR   B 1 317 ? 64.412  54.304  18.716  1   37.58 ? 339 THR   B N    1 
ATOM   5171 C  CA   . THR   B 1 317 ? 64.136  55.414  19.63   1   38.15 ? 339 THR   B CA   1 
ATOM   5172 C  C    . THR   B 1 317 ? 65.214  56.5    19.558  1   38.88 ? 339 THR   B C    1 
ATOM   5173 O  O    . THR   B 1 317 ? 65.007  57.577  20.104  1   39.3  ? 339 THR   B O    1 
ATOM   5174 C  CB   . THR   B 1 317 ? 63.908  54.951  21.061  1   39.44 ? 339 THR   B CB   1 
ATOM   5175 O  OG1  . THR   B 1 317 ? 65.14   54.468  21.602  1   40.6  ? 339 THR   B OG1  1 
ATOM   5176 C  CG2  . THR   B 1 317 ? 62.818  53.903  21.163  1   39.4  ? 339 THR   B CG2  1 
ATOM   5177 N  N    . LEU   B 1 318 ? 66.342  56.25   18.858  1   39.24 ? 340 LEU   B N    1 
ATOM   5178 C  CA   . LEU   B 1 318 ? 67.39   57.239  18.656  1   40.35 ? 340 LEU   B CA   1 
ATOM   5179 C  C    . LEU   B 1 318 ? 67.042  58.261  17.529  1   43.21 ? 340 LEU   B C    1 
ATOM   5180 O  O    . LEU   B 1 318 ? 67.804  59.195  17.294  1   44.22 ? 340 LEU   B O    1 
ATOM   5181 C  CB   . LEU   B 1 318 ? 68.717  56.537  18.34   1   39.57 ? 340 LEU   B CB   1 
ATOM   5182 C  CG   . LEU   B 1 318 ? 69.194  55.472  19.334  1   40.1  ? 340 LEU   B CG   1 
ATOM   5183 C  CD1  . LEU   B 1 318 ? 70.533  54.868  18.902  1   39.75 ? 340 LEU   B CD1  1 
ATOM   5184 C  CD2  . LEU   B 1 318 ? 69.293  56.028  20.734  1   39.74 ? 340 LEU   B CD2  1 
ATOM   5185 N  N    . SER   B 1 319 ? 65.918  58.078  16.826  1   44.17 ? 341 SER   B N    1 
ATOM   5186 C  CA   . SER   B 1 319 ? 65.513  58.967  15.755  1   45.73 ? 341 SER   B CA   1 
ATOM   5187 C  C    . SER   B 1 319 ? 64.894  60.283  16.262  1   46.99 ? 341 SER   B C    1 
ATOM   5188 O  O    . SER   B 1 319 ? 64.461  60.388  17.419  1   46.76 ? 341 SER   B O    1 
ATOM   5189 C  CB   . SER   B 1 319 ? 64.537  58.256  14.828  1   47.66 ? 341 SER   B CB   1 
ATOM   5190 O  OG   . SER   B 1 319 ? 63.261  58.125  15.437  1   51.49 ? 341 SER   B OG   1 
ATOM   5191 N  N    . ASP   B 1 320 ? 64.834  61.285  15.368  1   47.7  ? 342 ASP   B N    1 
ATOM   5192 C  CA   . ASP   B 1 320 ? 64.229  62.577  15.663  1   48.37 ? 342 ASP   B CA   1 
ATOM   5193 C  C    . ASP   B 1 320 ? 62.733  62.47   16.005  1   48.05 ? 342 ASP   B C    1 
ATOM   5194 O  O    . ASP   B 1 320 ? 62.173  63.429  16.521  1   48.56 ? 342 ASP   B O    1 
ATOM   5195 C  CB   . ASP   B 1 320 ? 64.476  63.555  14.504  1   51.35 ? 342 ASP   B CB   1 
ATOM   5196 C  CG   . ASP   B 1 320 ? 65.924  64.011  14.36   1   57.33 ? 342 ASP   B CG   1 
ATOM   5197 O  OD1  . ASP   B 1 320 ? 66.735  63.725  15.273  1   58.32 ? 342 ASP   B OD1  1 
ATOM   5198 O  OD2  . ASP   B 1 320 ? 66.243  64.659  13.336  1   59.94 ? 342 ASP   B OD2  1 
ATOM   5199 N  N    . ARG   B 1 321 ? 62.101  61.298  15.782  1   47.54 ? 343 ARG   B N    1 
ATOM   5200 C  CA   . ARG   B 1 321 ? 60.708  61.048  16.139  1   48.04 ? 343 ARG   B CA   1 
ATOM   5201 C  C    . ARG   B 1 321 ? 60.474  61.17   17.65   1   47.26 ? 343 ARG   B C    1 
ATOM   5202 O  O    . ARG   B 1 321 ? 59.366  61.519  18.075  1   47.32 ? 343 ARG   B O    1 
ATOM   5203 C  CB   . ARG   B 1 321 ? 60.29   59.649  15.686  1   51.16 ? 343 ARG   B CB   1 
ATOM   5204 C  CG   . ARG   B 1 321 ? 60.111  59.518  14.183  1   56.96 ? 343 ARG   B CG   1 
ATOM   5205 C  CD   . ARG   B 1 321 ? 58.813  58.802  13.872  1   61.85 ? 343 ARG   B CD   1 
ATOM   5206 N  NE   . ARG   B 1 321 ? 59.002  57.363  13.696  1   65.23 ? 343 ARG   B NE   1 
ATOM   5207 C  CZ   . ARG   B 1 321 ? 58.031  56.462  13.806  1   68.14 ? 343 ARG   B CZ   1 
ATOM   5208 N  NH1  . ARG   B 1 321 ? 56.798  56.839  14.136  1   67.71 ? 343 ARG   B NH1  1 
ATOM   5209 N  NH2  . ARG   B 1 321 ? 58.285  55.177  13.605  1   68.85 ? 343 ARG   B NH2  1 
ATOM   5210 N  N    . TYR   B 1 322 ? 61.509  60.841  18.46   1   45.9  ? 344 TYR   B N    1 
ATOM   5211 C  CA   . TYR   B 1 322 ? 61.463  60.912  19.919  1   44.38 ? 344 TYR   B CA   1 
ATOM   5212 C  C    . TYR   B 1 322 ? 62.005  62.221  20.503  1   44.94 ? 344 TYR   B C    1 
ATOM   5213 O  O    . TYR   B 1 322 ? 61.94   62.407  21.719  1   45.51 ? 344 TYR   B O    1 
ATOM   5214 C  CB   . TYR   B 1 322 ? 62.168  59.705  20.534  1   42.66 ? 344 TYR   B CB   1 
ATOM   5215 C  CG   . TYR   B 1 322 ? 61.342  58.446  20.434  1   41.12 ? 344 TYR   B CG   1 
ATOM   5216 C  CD1  . TYR   B 1 322 ? 61.332  57.69   19.277  1   41.04 ? 344 TYR   B CD1  1 
ATOM   5217 C  CD2  . TYR   B 1 322 ? 60.563  58.018  21.495  1   40.88 ? 344 TYR   B CD2  1 
ATOM   5218 C  CE1  . TYR   B 1 322 ? 60.599  56.52   19.188  1   41.08 ? 344 TYR   B CE1  1 
ATOM   5219 C  CE2  . TYR   B 1 322 ? 59.796  56.869  21.403  1   41.25 ? 344 TYR   B CE2  1 
ATOM   5220 C  CZ   . TYR   B 1 322 ? 59.831  56.112  20.253  1   41.72 ? 344 TYR   B CZ   1 
ATOM   5221 O  OH   . TYR   B 1 322 ? 59.109  54.948  20.172  1   43.25 ? 344 TYR   B OH   1 
ATOM   5222 N  N    . LYS   B 1 323 ? 62.536  63.122  19.654  1   45.04 ? 345 LYS   B N    1 
ATOM   5223 C  CA   . LYS   B 1 323 ? 63.032  64.431  20.061  1   46.15 ? 345 LYS   B CA   1 
ATOM   5224 C  C    . LYS   B 1 323 ? 61.787  65.334  20.203  1   47.52 ? 345 LYS   B C    1 
ATOM   5225 O  O    . LYS   B 1 323 ? 60.967  65.404  19.29   1   47.68 ? 345 LYS   B O    1 
ATOM   5226 C  CB   . LYS   B 1 323 ? 63.958  64.974  18.974  1   48.26 ? 345 LYS   B CB   1 
ATOM   5227 C  CG   . LYS   B 1 323 ? 65.131  65.759  19.499  1   54.07 ? 345 LYS   B CG   1 
ATOM   5228 C  CD   . LYS   B 1 323 ? 66.201  64.85   20.095  1   58.99 ? 345 LYS   B CD   1 
ATOM   5229 C  CE   . LYS   B 1 323 ? 67.473  65.609  20.379  1   62.8  ? 345 LYS   B CE   1 
ATOM   5230 N  NZ   . LYS   B 1 323 ? 68.66   64.713  20.446  1   65.71 ? 345 LYS   B NZ   1 
ATOM   5231 N  N    . VAL   B 1 324 ? 61.595  65.943  21.37   1   47.89 ? 346 VAL   B N    1 
ATOM   5232 C  CA   . VAL   B 1 324 ? 60.427  66.768  21.651  1   48.41 ? 346 VAL   B CA   1 
ATOM   5233 C  C    . VAL   B 1 324 ? 60.545  68.199  21.121  1   49.04 ? 346 VAL   B C    1 
ATOM   5234 O  O    . VAL   B 1 324 ? 59.64   68.691  20.455  1   49.68 ? 346 VAL   B O    1 
ATOM   5235 C  CB   . VAL   B 1 324 ? 60.125  66.751  23.162  1   48.65 ? 346 VAL   B CB   1 
ATOM   5236 C  CG1  . VAL   B 1 324 ? 58.979  67.698  23.508  1   48.85 ? 346 VAL   B CG1  1 
ATOM   5237 C  CG2  . VAL   B 1 324 ? 59.836  65.332  23.63   1   48.87 ? 346 VAL   B CG2  1 
ATOM   5238 N  N    . PHE   B 1 325 ? 61.642  68.873  21.43   1   48.62 ? 347 PHE   B N    1 
ATOM   5239 C  CA   . PHE   B 1 325 ? 61.855  70.255  21.009  1   48.23 ? 347 PHE   B CA   1 
ATOM   5240 C  C    . PHE   B 1 325 ? 62.733  70.305  19.778  1   48.25 ? 347 PHE   B C    1 
ATOM   5241 O  O    . PHE   B 1 325 ? 63.687  71.078  19.713  1   48.04 ? 347 PHE   B O    1 
ATOM   5242 C  CB   . PHE   B 1 325 ? 62.447  71.064  22.162  1   47.69 ? 347 PHE   B CB   1 
ATOM   5243 C  CG   . PHE   B 1 325 ? 61.469  71.175  23.305  1   47.78 ? 347 PHE   B CG   1 
ATOM   5244 C  CD1  . PHE   B 1 325 ? 60.472  72.136  23.294  1   48.21 ? 347 PHE   B CD1  1 
ATOM   5245 C  CD2  . PHE   B 1 325 ? 61.533  70.308  24.38   1   47.99 ? 347 PHE   B CD2  1 
ATOM   5246 C  CE1  . PHE   B 1 325 ? 59.573  72.236  24.342  1   48.6  ? 347 PHE   B CE1  1 
ATOM   5247 C  CE2  . PHE   B 1 325 ? 60.619  70.398  25.417  1   48.4  ? 347 PHE   B CE2  1 
ATOM   5248 C  CZ   . PHE   B 1 325 ? 59.648  71.364  25.393  1   48.32 ? 347 PHE   B CZ   1 
ATOM   5249 N  N    . LEU   B 1 326 ? 62.383  69.478  18.788  1   48.55 ? 348 LEU   B N    1 
ATOM   5250 C  CA   . LEU   B 1 326 ? 63.092  69.357  17.519  1   49.2  ? 348 LEU   B CA   1 
ATOM   5251 C  C    . LEU   B 1 326 ? 63.304  70.701  16.826  1   48.97 ? 348 LEU   B C    1 
ATOM   5252 O  O    . LEU   B 1 326 ? 64.381  70.939  16.282  1   49.08 ? 348 LEU   B O    1 
ATOM   5253 C  CB   . LEU   B 1 326 ? 62.322  68.394  16.601  1   49.88 ? 348 LEU   B CB   1 
ATOM   5254 C  CG   . LEU   B 1 326 ? 63.1    67.849  15.426  1   52.24 ? 348 LEU   B CG   1 
ATOM   5255 C  CD1  . LEU   B 1 326 ? 64.267  67.016  15.897  1   53.17 ? 348 LEU   B CD1  1 
ATOM   5256 C  CD2  . LEU   B 1 326 ? 62.203  67.042  14.507  1   53.1  ? 348 LEU   B CD2  1 
ATOM   5257 N  N    . ASP   B 1 327 ? 62.283  71.579  16.853  1   48.82 ? 349 ASP   B N    1 
ATOM   5258 C  CA   . ASP   B 1 327 ? 62.344  72.909  16.237  1   49.28 ? 349 ASP   B CA   1 
ATOM   5259 C  C    . ASP   B 1 327 ? 63.491  73.764  16.761  1   48.08 ? 349 ASP   B C    1 
ATOM   5260 O  O    . ASP   B 1 327 ? 64.149  74.451  15.977  1   48.42 ? 349 ASP   B O    1 
ATOM   5261 C  CB   . ASP   B 1 327 ? 61.029  73.654  16.484  1   52.21 ? 349 ASP   B CB   1 
ATOM   5262 C  CG   . ASP   B 1 327 ? 59.847  72.93   15.909  1   58.27 ? 349 ASP   B CG   1 
ATOM   5263 O  OD1  . ASP   B 1 327 ? 59.504  71.843  16.434  1   59.1  ? 349 ASP   B OD1  1 
ATOM   5264 O  OD2  . ASP   B 1 327 ? 59.253  73.446  14.939  1   61    ? 349 ASP   B OD2  1 
ATOM   5265 N  N    . LEU   B 1 328 ? 63.718  73.734  18.08   1   46.49 ? 350 LEU   B N    1 
ATOM   5266 C  CA   . LEU   B 1 328 ? 64.753  74.539  18.707  1   45.85 ? 350 LEU   B CA   1 
ATOM   5267 C  C    . LEU   B 1 328 ? 66.142  74.291  18.169  1   45.77 ? 350 LEU   B C    1 
ATOM   5268 O  O    . LEU   B 1 328 ? 66.908  75.238  18.03   1   45.77 ? 350 LEU   B O    1 
ATOM   5269 C  CB   . LEU   B 1 328 ? 64.727  74.372  20.229  1   45.7  ? 350 LEU   B CB   1 
ATOM   5270 C  CG   . LEU   B 1 328 ? 63.437  74.754  20.942  1   46.65 ? 350 LEU   B CG   1 
ATOM   5271 C  CD1  . LEU   B 1 328 ? 63.586  74.583  22.454  1   46.84 ? 350 LEU   B CD1  1 
ATOM   5272 C  CD2  . LEU   B 1 328 ? 63.005  76.188  20.587  1   47.11 ? 350 LEU   B CD2  1 
ATOM   5273 N  N    . PHE   B 1 329 ? 66.463  73.036  17.826  1   45.65 ? 351 PHE   B N    1 
ATOM   5274 C  CA   . PHE   B 1 329 ? 67.786  72.671  17.318  1   45.74 ? 351 PHE   B CA   1 
ATOM   5275 C  C    . PHE   B 1 329 ? 68.136  73.302  16.006  1   46.88 ? 351 PHE   B C    1 
ATOM   5276 O  O    . PHE   B 1 329 ? 69.323  73.495  15.739  1   47.16 ? 351 PHE   B O    1 
ATOM   5277 C  CB   . PHE   B 1 329 ? 67.934  71.145  17.194  1   45.1  ? 351 PHE   B CB   1 
ATOM   5278 C  CG   . PHE   B 1 329 ? 67.967  70.438  18.526  1   44.84 ? 351 PHE   B CG   1 
ATOM   5279 C  CD1  . PHE   B 1 329 ? 66.799  70.014  19.132  1   45.1  ? 351 PHE   B CD1  1 
ATOM   5280 C  CD2  . PHE   B 1 329 ? 69.162  70.23   19.188  1   45.2  ? 351 PHE   B CD2  1 
ATOM   5281 C  CE1  . PHE   B 1 329 ? 66.826  69.381  20.368  1   45.63 ? 351 PHE   B CE1  1 
ATOM   5282 C  CE2  . PHE   B 1 329 ? 69.184  69.62   20.433  1   45.72 ? 351 PHE   B CE2  1 
ATOM   5283 C  CZ   . PHE   B 1 329 ? 68.018  69.186  21.009  1   45.43 ? 351 PHE   B CZ   1 
ATOM   5284 N  N    . ASN   B 1 330 ? 67.131  73.63   15.175  1   47.3  ? 352 ASN   B N    1 
ATOM   5285 C  CA   . ASN   B 1 330 ? 67.39   74.164  13.837  1   48.11 ? 352 ASN   B CA   1 
ATOM   5286 C  C    . ASN   B 1 330 ? 67.218  75.693  13.686  1   48.33 ? 352 ASN   B C    1 
ATOM   5287 O  O    . ASN   B 1 330 ? 67.346  76.203  12.574  1   48.53 ? 352 ASN   B O    1 
ATOM   5288 C  CB   . ASN   B 1 330 ? 66.494  73.423  12.83   1   49.81 ? 352 ASN   B CB   1 
ATOM   5289 C  CG   . ASN   B 1 330 ? 66.98   73.447  11.411  1   53.02 ? 352 ASN   B CG   1 
ATOM   5290 O  OD1  . ASN   B 1 330 ? 68.172  73.274  11.127  1   54.39 ? 352 ASN   B OD1  1 
ATOM   5291 N  ND2  . ASN   B 1 330 ? 66.063  73.686  10.494  1   53.71 ? 352 ASN   B ND2  1 
ATOM   5292 N  N    . LEU   B 1 331 ? 66.976  76.425  14.781  1   48.03 ? 353 LEU   B N    1 
ATOM   5293 C  CA   . LEU   B 1 331 ? 66.742  77.87   14.711  1   48.16 ? 353 LEU   B CA   1 
ATOM   5294 C  C    . LEU   B 1 331 ? 67.866  78.705  14.062  1   48.97 ? 353 LEU   B C    1 
ATOM   5295 O  O    . LEU   B 1 331 ? 67.554  79.732  13.453  1   49.64 ? 353 LEU   B O    1 
ATOM   5296 C  CB   . LEU   B 1 331 ? 66.371  78.454  16.088  1   47.84 ? 353 LEU   B CB   1 
ATOM   5297 C  CG   . LEU   B 1 331 ? 65.068  77.905  16.697  1   48.85 ? 353 LEU   B CG   1 
ATOM   5298 C  CD1  . LEU   B 1 331 ? 64.78   78.501  18.053  1   49.02 ? 353 LEU   B CD1  1 
ATOM   5299 C  CD2  . LEU   B 1 331 ? 63.896  78.147  15.792  1   49.73 ? 353 LEU   B CD2  1 
ATOM   5300 N  N    . SER   B 1 332 ? 69.137  78.29   14.157  1   48.78 ? 354 SER   B N    1 
ATOM   5301 C  CA   . SER   B 1 332 ? 70.23   79.063  13.553  1   49.24 ? 354 SER   B CA   1 
ATOM   5302 C  C    . SER   B 1 332 ? 70.224  79.067  12.019  1   49.83 ? 354 SER   B C    1 
ATOM   5303 O  O    . SER   B 1 332 ? 70.948  79.851  11.41   1   49.65 ? 354 SER   B O    1 
ATOM   5304 C  CB   . SER   B 1 332 ? 71.587  78.627  14.092  1   50.2  ? 354 SER   B CB   1 
ATOM   5305 O  OG   . SER   B 1 332 ? 71.709  78.984  15.458  1   51.72 ? 354 SER   B OG   1 
ATOM   5306 N  N    . THR   B 1 333 ? 69.397  78.224  11.393  1   50.47 ? 355 THR   B N    1 
ATOM   5307 C  CA   . THR   B 1 333 ? 69.226  78.198  9.939   1   51.22 ? 355 THR   B CA   1 
ATOM   5308 C  C    . THR   B 1 333 ? 68.615  79.543  9.435   1   52.25 ? 355 THR   B C    1 
ATOM   5309 O  O    . THR   B 1 333 ? 68.875  79.939  8.309   1   53.07 ? 355 THR   B O    1 
ATOM   5310 C  CB   . THR   B 1 333 ? 68.286  77.029  9.571   1   51.94 ? 355 THR   B CB   1 
ATOM   5311 O  OG1  . THR   B 1 333 ? 68.8    75.815  10.117  1   52.56 ? 355 THR   B OG1  1 
ATOM   5312 C  CG2  . THR   B 1 333 ? 68.058  76.885  8.073   1   51.97 ? 355 THR   B CG2  1 
ATOM   5313 N  N    . PHE   B 1 334 ? 67.845  80.247  10.277  1   52.03 ? 356 PHE   B N    1 
ATOM   5314 C  CA   . PHE   B 1 334 ? 67.116  81.479  9.945   1   52.45 ? 356 PHE   B CA   1 
ATOM   5315 C  C    . PHE   B 1 334 ? 67.806  82.795  10.333  1   54.3  ? 356 PHE   B C    1 
ATOM   5316 O  O    . PHE   B 1 334 ? 67.267  83.877  10.085  1   54.4  ? 356 PHE   B O    1 
ATOM   5317 C  CB   . PHE   B 1 334 ? 65.718  81.434  10.594  1   51.5  ? 356 PHE   B CB   1 
ATOM   5318 C  CG   . PHE   B 1 334 ? 65.035  80.092  10.449  1   51.07 ? 356 PHE   B CG   1 
ATOM   5319 C  CD1  . PHE   B 1 334 ? 64.819  79.54   9.2     1   51.36 ? 356 PHE   B CD1  1 
ATOM   5320 C  CD2  . PHE   B 1 334 ? 64.692  79.346  11.563  1   51.14 ? 356 PHE   B CD2  1 
ATOM   5321 C  CE1  . PHE   B 1 334 ? 64.253  78.279  9.068   1   51.67 ? 356 PHE   B CE1  1 
ATOM   5322 C  CE2  . PHE   B 1 334 ? 64.105  78.094  11.426  1   51.35 ? 356 PHE   B CE2  1 
ATOM   5323 C  CZ   . PHE   B 1 334 ? 63.887  77.571  10.182  1   51.04 ? 356 PHE   B CZ   1 
ATOM   5324 N  N    . LEU   B 1 335 ? 68.977  82.703  10.952  1   55.13 ? 357 LEU   B N    1 
ATOM   5325 C  CA   . LEU   B 1 335 ? 69.75   83.836  11.436  1   56.16 ? 357 LEU   B CA   1 
ATOM   5326 C  C    . LEU   B 1 335 ? 70.366  84.701  10.314  1   56.65 ? 357 LEU   B C    1 
ATOM   5327 O  O    . LEU   B 1 335 ? 70.825  84.188  9.295   1   56.6  ? 357 LEU   B O    1 
ATOM   5328 C  CB   . LEU   B 1 335 ? 70.874  83.266  12.315  1   56.41 ? 357 LEU   B CB   1 
ATOM   5329 C  CG   . LEU   B 1 335 ? 71.62   84.229  13.203  1   57.97 ? 357 LEU   B CG   1 
ATOM   5330 C  CD1  . LEU   B 1 335 ? 70.712  84.78   14.286  1   58.2  ? 357 LEU   B CD1  1 
ATOM   5331 C  CD2  . LEU   B 1 335 ? 72.826  83.547  13.826  1   59.2  ? 357 LEU   B CD2  1 
ATOM   5332 N  N    . ILE   B 1 336 ? 70.387  86.017  10.534  1   56.86 ? 358 ILE   B N    1 
ATOM   5333 C  CA   . ILE   B 1 336 ? 71.025  87.015  9.666   1   57.61 ? 358 ILE   B CA   1 
ATOM   5334 C  C    . ILE   B 1 336 ? 72.055  87.773  10.535  1   58.46 ? 358 ILE   B C    1 
ATOM   5335 O  O    . ILE   B 1 336 ? 71.911  87.803  11.764  1   58.32 ? 358 ILE   B O    1 
ATOM   5336 C  CB   . ILE   B 1 336 ? 69.983  87.979  9.028   1   57.94 ? 358 ILE   B CB   1 
ATOM   5337 C  CG1  . ILE   B 1 336 ? 69.014  88.535  10.093  1   59.16 ? 358 ILE   B CG1  1 
ATOM   5338 C  CG2  . ILE   B 1 336 ? 69.239  87.301  7.894   1   58.25 ? 358 ILE   B CG2  1 
ATOM   5339 C  CD1  . ILE   B 1 336 ? 68.078  89.59   9.627   1   60.48 ? 358 ILE   B CD1  1 
ATOM   5340 N  N    . PRO   B 1 337 ? 73.094  88.396  9.944   1   59.34 ? 359 PRO   B N    1 
ATOM   5341 C  CA   . PRO   B 1 337 ? 74.094  89.097  10.772  1   60.52 ? 359 PRO   B CA   1 
ATOM   5342 C  C    . PRO   B 1 337 ? 73.533  90.185  11.677  1   62.71 ? 359 PRO   B C    1 
ATOM   5343 O  O    . PRO   B 1 337 ? 72.402  90.634  11.488  1   62.98 ? 359 PRO   B O    1 
ATOM   5344 C  CB   . PRO   B 1 337 ? 75.097  89.643  9.754   1   60.68 ? 359 PRO   B CB   1 
ATOM   5345 C  CG   . PRO   B 1 337 ? 74.899  88.823  8.54    1   60.85 ? 359 PRO   B CG   1 
ATOM   5346 C  CD   . PRO   B 1 337 ? 73.446  88.45   8.516   1   58.98 ? 359 PRO   B CD   1 
ATOM   5347 N  N    . ARG   B 1 338 ? 74.315  90.583  12.687  1   64.11 ? 360 ARG   B N    1 
ATOM   5348 C  CA   . ARG   B 1 338 ? 73.905  91.59   13.665  1   65.88 ? 360 ARG   B CA   1 
ATOM   5349 C  C    . ARG   B 1 338 ? 73.472  92.899  13.015  1   66.93 ? 360 ARG   B C    1 
ATOM   5350 O  O    . ARG   B 1 338 ? 72.428  93.443  13.382  1   67.12 ? 360 ARG   B O    1 
ATOM   5351 C  CB   . ARG   B 1 338 ? 75.028  91.848  14.682  1   67.51 ? 360 ARG   B CB   1 
ATOM   5352 C  CG   . ARG   B 1 338 ? 74.554  91.772  16.134  1   70.93 ? 360 ARG   B CG   1 
ATOM   5353 C  CD   . ARG   B 1 338 ? 75.666  92.099  17.115  1   74.16 ? 360 ARG   B CD   1 
ATOM   5354 N  NE   . ARG   B 1 338 ? 76.835  91.248  16.896  1   76.89 ? 360 ARG   B NE   1 
ATOM   5355 C  CZ   . ARG   B 1 338 ? 77.114  90.156  17.598  1   78.4  ? 360 ARG   B CZ   1 
ATOM   5356 N  NH1  . ARG   B 1 338 ? 76.332  89.79   18.609  1   77.6  ? 360 ARG   B NH1  1 
ATOM   5357 N  NH2  . ARG   B 1 338 ? 78.187  89.434  17.311  1   78.03 ? 360 ARG   B NH2  1 
ATOM   5358 N  N    . GLU   B 1 339 ? 74.246  93.37   12.019  1   67.55 ? 361 GLU   B N    1 
ATOM   5359 C  CA   . GLU   B 1 339 ? 73.965  94.603  11.282  1   68.72 ? 361 GLU   B CA   1 
ATOM   5360 C  C    . GLU   B 1 339 ? 72.584  94.563  10.609  1   69.51 ? 361 GLU   B C    1 
ATOM   5361 O  O    . GLU   B 1 339 ? 71.916  95.594  10.525  1   69.86 ? 361 GLU   B O    1 
ATOM   5362 C  CB   . GLU   B 1 339 ? 75.067  94.877  10.242  1   70.81 ? 361 GLU   B CB   1 
ATOM   5363 N  N    . ALA   B 1 340 ? 72.138  93.373  10.179  1   69.37 ? 362 ALA   B N    1 
ATOM   5364 C  CA   . ALA   B 1 340 ? 70.846  93.223  9.524   1   69.9  ? 362 ALA   B CA   1 
ATOM   5365 C  C    . ALA   B 1 340 ? 69.674  92.962  10.478  1   70.7  ? 362 ALA   B C    1 
ATOM   5366 O  O    . ALA   B 1 340 ? 68.53   93.055  10.049  1   70.81 ? 362 ALA   B O    1 
ATOM   5367 C  CB   . ALA   B 1 340 ? 70.922  92.13   8.477   1   69.89 ? 362 ALA   B CB   1 
ATOM   5368 N  N    . ILE   B 1 341 ? 69.936  92.635  11.753  1   71.12 ? 363 ILE   B N    1 
ATOM   5369 C  CA   . ILE   B 1 341 ? 68.851  92.356  12.703  1   71.99 ? 363 ILE   B CA   1 
ATOM   5370 C  C    . ILE   B 1 341 ? 68.116  93.644  13.088  1   73.29 ? 363 ILE   B C    1 
ATOM   5371 O  O    . ILE   B 1 341 ? 68.765  94.64   13.417  1   73.65 ? 363 ILE   B O    1 
ATOM   5372 C  CB   . ILE   B 1 341 ? 69.356  91.539  13.935  1   71.89 ? 363 ILE   B CB   1 
ATOM   5373 C  CG1  . ILE   B 1 341 ? 69.762  90.104  13.516  1   72.33 ? 363 ILE   B CG1  1 
ATOM   5374 C  CG2  . ILE   B 1 341 ? 68.31   91.512  15.056  1   72.02 ? 363 ILE   B CG2  1 
ATOM   5375 C  CD1  . ILE   B 1 341 ? 70.278  89.195  14.659  1   73.2  ? 363 ILE   B CD1  1 
ATOM   5376 N  N    . PRO   B 1 342 ? 66.767  93.657  13.005  1   73.71 ? 364 PRO   B N    1 
ATOM   5377 C  CA   . PRO   B 1 342 ? 66.014  94.875  13.358  1   74.18 ? 364 PRO   B CA   1 
ATOM   5378 C  C    . PRO   B 1 342 ? 66.319  95.391  14.761  1   74.87 ? 364 PRO   B C    1 
ATOM   5379 O  O    . PRO   B 1 342 ? 66.155  94.66   15.729  1   74.93 ? 364 PRO   B O    1 
ATOM   5380 C  CB   . PRO   B 1 342 ? 64.548  94.435  13.235  1   74.76 ? 364 PRO   B CB   1 
ATOM   5381 C  CG   . PRO   B 1 342 ? 64.57   93.245  12.341  1   74.95 ? 364 PRO   B CG   1 
ATOM   5382 C  CD   . PRO   B 1 342 ? 65.869  92.555  12.609  1   73.26 ? 364 PRO   B CD   1 
ATOM   5383 N  N    . PRO   B 1 343 ? 66.788  96.644  14.891  1   75.32 ? 365 PRO   B N    1 
ATOM   5384 C  CA   . PRO   B 1 343 ? 67.155  97.155  16.221  1   75.72 ? 365 PRO   B CA   1 
ATOM   5385 C  C    . PRO   B 1 343 ? 65.996  97.276  17.203  1   76.35 ? 365 PRO   B C    1 
ATOM   5386 O  O    . PRO   B 1 343 ? 64.928  97.745  16.838  1   76.37 ? 365 PRO   B O    1 
ATOM   5387 C  CB   . PRO   B 1 343 ? 67.795  98.518  15.914  1   76.18 ? 365 PRO   B CB   1 
ATOM   5388 C  CG   . PRO   B 1 343 ? 68.164  98.461  14.467  1   76.42 ? 365 PRO   B CG   1 
ATOM   5389 C  CD   . PRO   B 1 343 ? 67.09   97.628  13.838  1   74.86 ? 365 PRO   B CD   1 
ATOM   5390 N  N    . LEU   B 1 344 ? 66.212  96.843  18.448  1   76.9  ? 366 LEU   B N    1 
ATOM   5391 C  CA   . LEU   B 1 344 ? 65.209  96.919  19.511  1   78.14 ? 366 LEU   B CA   1 
ATOM   5392 C  C    . LEU   B 1 344 ? 65.01   98.388  19.948  1   79.67 ? 366 LEU   B C    1 
ATOM   5393 O  O    . LEU   B 1 344 ? 66.002  99.108  20.104  1   79.94 ? 366 LEU   B O    1 
ATOM   5394 C  CB   . LEU   B 1 344 ? 65.688  96.105  20.728  1   78.06 ? 366 LEU   B CB   1 
ATOM   5395 C  CG   . LEU   B 1 344 ? 65.353  94.628  20.768  1   78.97 ? 366 LEU   B CG   1 
ATOM   5396 C  CD1  . LEU   B 1 344 ? 65.979  93.985  21.96   1   79.43 ? 366 LEU   B CD1  1 
ATOM   5397 C  CD2  . LEU   B 1 344 ? 63.873  94.419  20.857  1   79.56 ? 366 LEU   B CD2  1 
ATOM   5398 N  N    . ASP   B 1 345 ? 63.755  98.84   20.157  1   80.34 ? 367 ASP   B N    1 
ATOM   5399 C  CA   . ASP   B 1 345 ? 63.518  100.216 20.616  1   81.4  ? 367 ASP   B CA   1 
ATOM   5400 C  C    . ASP   B 1 345 ? 63.624  100.234 22.151  1   82.55 ? 367 ASP   B C    1 
ATOM   5401 O  O    . ASP   B 1 345 ? 64.466  100.952 22.69   1   82.76 ? 367 ASP   B O    1 
ATOM   5402 C  CB   . ASP   B 1 345 ? 62.136  100.762 20.174  1   82.75 ? 367 ASP   B CB   1 
ATOM   5403 C  CG   . ASP   B 1 345 ? 61.647  100.33  18.809  1   86.08 ? 367 ASP   B CG   1 
ATOM   5404 O  OD1  . ASP   B 1 345 ? 62.458  100.343 17.853  1   86.47 ? 367 ASP   B OD1  1 
ATOM   5405 O  OD2  . ASP   B 1 345 ? 60.444  100.002 18.689  1   87.7  ? 367 ASP   B OD2  1 
ATOM   5406 N  N    . GLU   B 1 346 ? 62.773  99.413  22.837  1   82.94 ? 368 GLU   B N    1 
ATOM   5407 C  CA   . GLU   B 1 346 ? 62.666  99.215  24.29   1   83.63 ? 368 GLU   B CA   1 
ATOM   5408 C  C    . GLU   B 1 346 ? 61.479  98.299  24.607  1   84.03 ? 368 GLU   B C    1 
ATOM   5409 O  O    . GLU   B 1 346 ? 60.472  98.31   23.895  1   84.26 ? 368 GLU   B O    1 
ATOM   5410 C  CB   . GLU   B 1 346 ? 62.501  100.545 25.044  1   86.04 ? 368 GLU   B CB   1 
HETATM 5411 C  CHA  . HEM   C 2 .   ? 83.59   69.115  9.364   1   44.46 ? 401 HEM   A CHA  1 
HETATM 5412 C  CHB  . HEM   C 2 .   ? 81.288  73.049  11.061  1   44.32 ? 401 HEM   A CHB  1 
HETATM 5413 C  CHC  . HEM   C 2 .   ? 83.998  72.91   15.105  1   42.85 ? 401 HEM   A CHC  1 
HETATM 5414 C  CHD  . HEM   C 2 .   ? 86.474  69.177  13.273  1   43.06 ? 401 HEM   A CHD  1 
HETATM 5415 C  C1A  . HEM   C 2 .   ? 82.695  70.219  9.467   1   45.21 ? 401 HEM   A C1A  1 
HETATM 5416 C  C2A  . HEM   C 2 .   ? 81.78   70.639  8.418   1   46.88 ? 401 HEM   A C2A  1 
HETATM 5417 C  C3A  . HEM   C 2 .   ? 81.102  71.742  8.907   1   46    ? 401 HEM   A C3A  1 
HETATM 5418 C  C4A  . HEM   C 2 .   ? 81.638  71.994  10.234  1   44.76 ? 401 HEM   A C4A  1 
HETATM 5419 C  CMA  . HEM   C 2 .   ? 79.995  72.519  8.26    1   46.07 ? 401 HEM   A CMA  1 
HETATM 5420 C  CAA  . HEM   C 2 .   ? 81.681  70.033  7.043   1   48.89 ? 401 HEM   A CAA  1 
HETATM 5421 C  CBA  . HEM   C 2 .   ? 82.616  70.706  6.04    1   51.08 ? 401 HEM   A CBA  1 
HETATM 5422 C  CGA  . HEM   C 2 .   ? 82.089  72.008  5.502   1   53.34 ? 401 HEM   A CGA  1 
HETATM 5423 O  O1A  . HEM   C 2 .   ? 82.643  73.09   5.686   1   54.02 ? 401 HEM   A O1A  1 
HETATM 5424 O  O2A  . HEM   C 2 .   ? 80.957  71.87   4.816   1   54.14 ? 401 HEM   A O2A  1 
HETATM 5425 C  C1B  . HEM   C 2 .   ? 81.836  73.382  12.328  1   43.97 ? 401 HEM   A C1B  1 
HETATM 5426 C  C2B  . HEM   C 2 .   ? 81.394  74.499  13.149  1   43.62 ? 401 HEM   A C2B  1 
HETATM 5427 C  C3B  . HEM   C 2 .   ? 82.162  74.437  14.293  1   43.36 ? 401 HEM   A C3B  1 
HETATM 5428 C  C4B  . HEM   C 2 .   ? 83.048  73.311  14.166  1   43.37 ? 401 HEM   A C4B  1 
HETATM 5429 C  CMB  . HEM   C 2 .   ? 80.309  75.469  12.785  1   43.81 ? 401 HEM   A CMB  1 
HETATM 5430 C  CAB  . HEM   C 2 .   ? 82.11   75.317  15.469  1   43.26 ? 401 HEM   A CAB  1 
HETATM 5431 C  CBB  . HEM   C 2 .   ? 82.069  76.629  15.553  1   43.05 ? 401 HEM   A CBB  1 
HETATM 5432 C  C1C  . HEM   C 2 .   ? 84.927  71.85   14.969  1   42.6  ? 401 HEM   A C1C  1 
HETATM 5433 C  C2C  . HEM   C 2 .   ? 85.938  71.508  15.954  1   42.46 ? 401 HEM   A C2C  1 
HETATM 5434 C  C3C  . HEM   C 2 .   ? 86.655  70.467  15.392  1   42.34 ? 401 HEM   A C3C  1 
HETATM 5435 C  C4C  . HEM   C 2 .   ? 86.07   70.182  14.123  1   42.61 ? 401 HEM   A C4C  1 
HETATM 5436 C  CMC  . HEM   C 2 .   ? 86.101  72.164  17.29   1   42.35 ? 401 HEM   A CMC  1 
HETATM 5437 C  CAC  . HEM   C 2 .   ? 87.823  69.76   15.923  1   41.59 ? 401 HEM   A CAC  1 
HETATM 5438 C  CBC  . HEM   C 2 .   ? 89.017  69.591  15.383  1   41.08 ? 401 HEM   A CBC  1 
HETATM 5439 C  C1D  . HEM   C 2 .   ? 85.904  68.822  12.03   1   43.23 ? 401 HEM   A C1D  1 
HETATM 5440 C  C2D  . HEM   C 2 .   ? 86.313  67.674  11.245  1   43.46 ? 401 HEM   A C2D  1 
HETATM 5441 C  C3D  . HEM   C 2 .   ? 85.453  67.613  10.172  1   43.72 ? 401 HEM   A C3D  1 
HETATM 5442 C  C4D  . HEM   C 2 .   ? 84.572  68.764  10.285  1   43.88 ? 401 HEM   A C4D  1 
HETATM 5443 C  CMD  . HEM   C 2 .   ? 87.509  66.817  11.521  1   43.16 ? 401 HEM   A CMD  1 
HETATM 5444 C  CAD  . HEM   C 2 .   ? 85.321  66.452  9.227   1   43.09 ? 401 HEM   A CAD  1 
HETATM 5445 C  CBD  . HEM   C 2 .   ? 84.405  65.392  9.829   1   42.95 ? 401 HEM   A CBD  1 
HETATM 5446 C  CGD  . HEM   C 2 .   ? 84.152  64.174  8.983   1   42.9  ? 401 HEM   A CGD  1 
HETATM 5447 O  O1D  . HEM   C 2 .   ? 83.53   63.217  9.411   1   42.55 ? 401 HEM   A O1D  1 
HETATM 5448 O  O2D  . HEM   C 2 .   ? 84.635  64.213  7.769   1   43.25 ? 401 HEM   A O2D  1 
HETATM 5449 N  NA   . HEM   C 2 .   ? 82.587  71.042  10.546  1   44.36 ? 401 HEM   A NA   1 
HETATM 5450 N  NB   . HEM   C 2 .   ? 82.824  72.678  12.947  1   43.6  ? 401 HEM   A NB   1 
HETATM 5451 N  NC   . HEM   C 2 .   ? 85.014  71.043  13.883  1   42.89 ? 401 HEM   A NC   1 
HETATM 5452 N  ND   . HEM   C 2 .   ? 84.874  69.475  11.438  1   42.92 ? 401 HEM   A ND   1 
HETATM 5453 FE FE   . HEM   C 2 .   ? 83.8    71.02   12.217  1   43.17 ? 401 HEM   A FE   1 
HETATM 5454 C  C4   . A1IER D 3 .   ? 83.186  76.794  7.338   1   61.32 ? 402 A1IER A C4   1 
HETATM 5455 C  C6   . A1IER D 3 .   ? 81.184  78.266  7.706   1   63.51 ? 402 A1IER A C6   1 
HETATM 5456 C  C7   . A1IER D 3 .   ? 81.637  79.429  7.092   1   64.19 ? 402 A1IER A C7   1 
HETATM 5457 C  C8   . A1IER D 3 .   ? 80.731  80.427  6.767   1   64.44 ? 402 A1IER A C8   1 
HETATM 5458 C  C10  . A1IER D 3 .   ? 78.937  79.109  7.647   1   64.3  ? 402 A1IER A C10  1 
HETATM 5459 N  N12  . A1IER D 3 .   ? 81.953  76.498  9.165   1   61.63 ? 402 A1IER A N12  1 
HETATM 5460 C  C15  . A1IER D 3 .   ? 86.965  75.71   9.006   1   57.02 ? 402 A1IER A C15  1 
HETATM 5461 C  C20  . A1IER D 3 .   ? 86.244  72.81   11.847  1   56.82 ? 402 A1IER A C20  1 
HETATM 5462 C  C22  . A1IER D 3 .   ? 84.847  72.921  10.233  1   57.05 ? 402 A1IER A C22  1 
HETATM 5463 O  O1   . A1IER D 3 .   ? 84.526  73.618  7.404   1   58.71 ? 402 A1IER A O1   1 
HETATM 5464 C  C2   . A1IER D 3 .   ? 84.911  74.909  7.821   1   58.96 ? 402 A1IER A C2   1 
HETATM 5465 C  C3   . A1IER D 3 .   ? 83.709  75.774  8.085   1   60.47 ? 402 A1IER A C3   1 
HETATM 5466 N  N5   . A1IER D 3 .   ? 82.107  77.223  8.031   1   62.23 ? 402 A1IER A N5   1 
HETATM 5467 C  C9   . A1IER D 3 .   ? 79.385  80.268  7.042   1   64.47 ? 402 A1IER A C9   1 
HETATM 5468 C  C11  . A1IER D 3 .   ? 79.829  78.102  7.979   1   63.91 ? 402 A1IER A C11  1 
HETATM 5469 N  N13  . A1IER D 3 .   ? 82.929  75.62   9.195   1   61.01 ? 402 A1IER A N13  1 
HETATM 5470 C  C14  . A1IER D 3 .   ? 85.904  74.855  8.956   1   57.76 ? 402 A1IER A C14  1 
HETATM 5471 C  C16  . A1IER D 3 .   ? 87.9    75.655  10.063  1   56.5  ? 402 A1IER A C16  1 
HETATM 5472 CL CL17 . A1IER D 3 .   ? 89.224  76.781  10.067  1   55.67 ? 402 A1IER A CL17 1 
HETATM 5473 C  C18  . A1IER D 3 .   ? 87.776  74.747  11.063  1   56.74 ? 402 A1IER A C18  1 
HETATM 5474 C  C19  . A1IER D 3 .   ? 86.699  73.839  11.049  1   57    ? 402 A1IER A C19  1 
HETATM 5475 N  N21  . A1IER D 3 .   ? 85.1    72.248  11.332  1   56.78 ? 402 A1IER A N21  1 
HETATM 5476 N  N23  . A1IER D 3 .   ? 85.774  73.9    9.995   1   57.3  ? 402 A1IER A N23  1 
HETATM 5477 C  CHA  . HEM   E 2 .   ? 64.057  48.648  27.531  1   30.91 ? 401 HEM   B CHA  1 
HETATM 5478 C  CHB  . HEM   E 2 .   ? 67.697  45.479  28.177  1   30.5  ? 401 HEM   B CHB  1 
HETATM 5479 C  CHC  . HEM   E 2 .   ? 69.372  48.179  31.856  1   29.54 ? 401 HEM   B CHC  1 
HETATM 5480 C  CHD  . HEM   E 2 .   ? 65.573  51.133  31.409  1   31.19 ? 401 HEM   B CHD  1 
HETATM 5481 C  C1A  . HEM   E 2 .   ? 64.908  47.52   27.377  1   31.41 ? 401 HEM   B C1A  1 
HETATM 5482 C  C2A  . HEM   E 2 .   ? 64.684  46.448  26.427  1   32.45 ? 401 HEM   B C2A  1 
HETATM 5483 C  C3A  . HEM   E 2 .   ? 65.733  45.565  26.576  1   31.74 ? 401 HEM   B C3A  1 
HETATM 5484 C  C4A  . HEM   E 2 .   ? 66.562  46.092  27.643  1   31.04 ? 401 HEM   B C4A  1 
HETATM 5485 C  CMA  . HEM   E 2 .   ? 66.021  44.319  25.793  1   31.78 ? 401 HEM   B CMA  1 
HETATM 5486 C  CAA  . HEM   E 2 .   ? 63.474  46.31   25.544  1   33.82 ? 401 HEM   B CAA  1 
HETATM 5487 C  CBA  . HEM   E 2 .   ? 62.368  45.492  26.199  1   35.47 ? 401 HEM   B CBA  1 
HETATM 5488 C  CGA  . HEM   E 2 .   ? 62.597  44.005  26.147  1   37.61 ? 401 HEM   B CGA  1 
HETATM 5489 O  O1A  . HEM   E 2 .   ? 62.729  43.302  27.143  1   38.44 ? 401 HEM   B O1A  1 
HETATM 5490 O  O2A  . HEM   E 2 .   ? 62.657  43.521  24.931  1   38.11 ? 401 HEM   B O2A  1 
HETATM 5491 C  C1B  . HEM   E 2 .   ? 68.486  45.927  29.262  1   30.18 ? 401 HEM   B C1B  1 
HETATM 5492 C  C2B  . HEM   E 2 .   ? 69.681  45.254  29.738  1   30.16 ? 401 HEM   B C2B  1 
HETATM 5493 C  C3B  . HEM   E 2 .   ? 70.16   46.05   30.776  1   29.95 ? 401 HEM   B C3B  1 
HETATM 5494 C  C4B  . HEM   E 2 .   ? 69.262  47.163  30.918  1   29.62 ? 401 HEM   B C4B  1 
HETATM 5495 C  CMB  . HEM   E 2 .   ? 70.23   43.97   29.189  1   29.77 ? 401 HEM   B CMB  1 
HETATM 5496 C  CAB  . HEM   E 2 .   ? 71.353  45.834  31.609  1   29.36 ? 401 HEM   B CAB  1 
HETATM 5497 C  CBB  . HEM   E 2 .   ? 71.799  44.73   32.19   1   28.55 ? 401 HEM   B CBB  1 
HETATM 5498 C  C1C  . HEM   E 2 .   ? 68.468  49.245  32.068  1   30.11 ? 401 HEM   B C1C  1 
HETATM 5499 C  C2C  . HEM   E 2 .   ? 68.597  50.253  33.118  1   30.3  ? 401 HEM   B C2C  1 
HETATM 5500 C  C3C  . HEM   E 2 .   ? 67.485  51.056  32.989  1   30.56 ? 401 HEM   B C3C  1 
HETATM 5501 C  C4C  . HEM   E 2 .   ? 66.724  50.557  31.888  1   30.64 ? 401 HEM   B C4C  1 
HETATM 5502 C  CMC  . HEM   E 2 .   ? 69.736  50.359  34.09   1   29.5  ? 401 HEM   B CMC  1 
HETATM 5503 C  CAC  . HEM   E 2 .   ? 67.11   52.216  33.802  1   30.71 ? 401 HEM   B CAC  1 
HETATM 5504 C  CBC  . HEM   E 2 .   ? 65.987  52.438  34.455  1   30.78 ? 401 HEM   B CBC  1 
HETATM 5505 C  C1D  . HEM   E 2 .   ? 64.809  50.716  30.303  1   31.29 ? 401 HEM   B C1D  1 
HETATM 5506 C  C2D  . HEM   E 2 .   ? 63.655  51.429  29.793  1   31.35 ? 401 HEM   B C2D  1 
HETATM 5507 C  C3D  . HEM   E 2 .   ? 63.266  50.766  28.648  1   31.28 ? 401 HEM   B C3D  1 
HETATM 5508 C  C4D  . HEM   E 2 .   ? 64.144  49.617  28.52   1   31.14 ? 401 HEM   B C4D  1 
HETATM 5509 C  CMD  . HEM   E 2 .   ? 62.986  52.592  30.462  1   30.82 ? 401 HEM   B CMD  1 
HETATM 5510 C  CAD  . HEM   E 2 .   ? 62.304  51.279  27.615  1   31    ? 401 HEM   B CAD  1 
HETATM 5511 C  CBD  . HEM   E 2 .   ? 63.013  52.244  26.673  1   31.2  ? 401 HEM   B CBD  1 
HETATM 5512 C  CGD  . HEM   E 2 .   ? 62.182  52.818  25.56   1   31.94 ? 401 HEM   B CGD  1 
HETATM 5513 O  O1D  . HEM   E 2 .   ? 62.626  53.656  24.806  1   32.45 ? 401 HEM   B O1D  1 
HETATM 5514 O  O2D  . HEM   E 2 .   ? 60.971  52.365  25.454  1   32.41 ? 401 HEM   B O2D  1 
HETATM 5515 N  NA   . HEM   E 2 .   ? 66.038  47.284  28.092  1   30.85 ? 401 HEM   B NA   1 
HETATM 5516 N  NB   . HEM   E 2 .   ? 68.243  47.06   29.977  1   29.96 ? 401 HEM   B NB   1 
HETATM 5517 N  NC   . HEM   E 2 .   ? 67.339  49.447  31.335  1   30.56 ? 401 HEM   B NC   1 
HETATM 5518 N  ND   . HEM   E 2 .   ? 65.083  49.625  29.545  1   31.07 ? 401 HEM   B ND   1 
HETATM 5519 FE FE   . HEM   E 2 .   ? 66.695  48.379  29.674  1   30.12 ? 401 HEM   B FE   1 
HETATM 5520 C  C4   . A1IER F 3 .   ? 64.652  41.079  29.912  1   35.63 ? 402 A1IER B C4   1 
HETATM 5521 C  C6   . A1IER F 3 .   ? 66.401  39.468  29.126  1   36.25 ? 402 A1IER B C6   1 
HETATM 5522 C  C7   . A1IER F 3 .   ? 65.96   38.326  29.783  1   36.53 ? 402 A1IER B C7   1 
HETATM 5523 C  C8   . A1IER F 3 .   ? 66.438  37.086  29.394  1   36.07 ? 402 A1IER B C8   1 
HETATM 5524 C  C10  . A1IER F 3 .   ? 67.77   38.116  27.7    1   35.46 ? 402 A1IER B C10  1 
HETATM 5525 N  N12  . A1IER F 3 .   ? 66.698  41.841  29.486  1   35.33 ? 402 A1IER B N12  1 
HETATM 5526 C  C15  . A1IER F 3 .   ? 63.614  43.74   33.06   1   33.94 ? 402 A1IER B C15  1 
HETATM 5527 C  C20  . A1IER F 3 .   ? 65.523  47.324  32.309  1   32.8  ? 402 A1IER B C20  1 
HETATM 5528 C  C22  . A1IER F 3 .   ? 65.047  46.125  30.608  1   33.18 ? 402 A1IER B C22  1 
HETATM 5529 O  O1   . A1IER F 3 .   ? 63.156  44.155  29.56   1   35.03 ? 402 A1IER B O1   1 
HETATM 5530 C  C2   . A1IER F 3 .   ? 63.605  43.342  30.61   1   34.57 ? 402 A1IER B C2   1 
HETATM 5531 C  C3   . A1IER F 3 .   ? 64.698  42.421  30.147  1   35.27 ? 402 A1IER B C3   1 
HETATM 5532 N  N5   . A1IER F 3 .   ? 65.898  40.748  29.509  1   35.75 ? 402 A1IER B N5   1 
HETATM 5533 C  C9   . A1IER F 3 .   ? 67.339  36.981  28.355  1   35.67 ? 402 A1IER B C9   1 
HETATM 5534 C  C11  . A1IER F 3 .   ? 67.301  39.363  28.075  1   35.72 ? 402 A1IER B C11  1 
HETATM 5535 N  N13  . A1IER F 3 .   ? 65.967  42.858  29.873  1   35.29 ? 402 A1IER B N13  1 
HETATM 5536 C  C14  . A1IER F 3 .   ? 63.946  44.174  31.82   1   34.09 ? 402 A1IER B C14  1 
HETATM 5537 C  C16  . A1IER F 3 .   ? 63.914  44.504  34.199  1   34.01 ? 402 A1IER B C16  1 
HETATM 5538 CL CL17 . A1IER F 3 .   ? 63.462  43.867  35.747  1   34.31 ? 402 A1IER B CL17 1 
HETATM 5539 C  C18  . A1IER F 3 .   ? 64.542  45.704  34.108  1   33.47 ? 402 A1IER B C18  1 
HETATM 5540 C  C19  . A1IER F 3 .   ? 64.902  46.205  32.823  1   33.23 ? 402 A1IER B C19  1 
HETATM 5541 N  N21  . A1IER F 3 .   ? 65.606  47.266  30.939  1   32.84 ? 402 A1IER B N21  1 
HETATM 5542 N  N23  . A1IER F 3 .   ? 64.596  45.428  31.695  1   33.59 ? 402 A1IER B N23  1 
HETATM 5543 O  O    . HOH   G 4 .   ? 84.75   77.095  3.622   1   54    ? 501 HOH   A O    1 
HETATM 5544 O  O    . HOH   G 4 .   ? 88.741  25.649  16.402  1   55.88 ? 502 HOH   A O    1 
HETATM 5545 O  O    . HOH   G 4 .   ? 79.698  56.619  13.017  1   35.04 ? 503 HOH   A O    1 
HETATM 5546 O  O    . HOH   G 4 .   ? 94.614  50.15   5.834   1   49.5  ? 504 HOH   A O    1 
HETATM 5547 O  O    . HOH   G 4 .   ? 77.254  69.187  20.802  1   36.99 ? 505 HOH   A O    1 
HETATM 5548 O  O    . HOH   G 4 .   ? 85.063  55.828  12.921  1   45.51 ? 506 HOH   A O    1 
HETATM 5549 O  O    . HOH   G 4 .   ? 81.918  63.231  11.388  1   37.54 ? 507 HOH   A O    1 
HETATM 5550 O  O    . HOH   G 4 .   ? 79.619  80.44   29.013  1   34.73 ? 508 HOH   A O    1 
HETATM 5551 O  O    . HOH   G 4 .   ? 104.034 45.442  30.127  1   39.58 ? 509 HOH   A O    1 
HETATM 5552 O  O    . HOH   G 4 .   ? 88.051  39.613  32.838  1   37.66 ? 510 HOH   A O    1 
HETATM 5553 O  O    . HOH   G 4 .   ? 89.259  65.167  3.925   1   46.73 ? 511 HOH   A O    1 
HETATM 5554 O  O    . HOH   G 4 .   ? 96.274  53.718  30.571  1   34.27 ? 512 HOH   A O    1 
HETATM 5555 O  O    . HOH   G 4 .   ? 66.015  35.045  20.385  1   39.31 ? 513 HOH   A O    1 
HETATM 5556 O  O    . HOH   G 4 .   ? 112.397 70.108  24.342  1   28.65 ? 514 HOH   A O    1 
HETATM 5557 O  O    . HOH   G 4 .   ? 87.966  84.128  23.1    1   36.03 ? 515 HOH   A O    1 
HETATM 5558 O  O    . HOH   G 4 .   ? 82.198  56.601  14.12   1   31.93 ? 516 HOH   A O    1 
HETATM 5559 O  O    . HOH   G 4 .   ? 81.243  37.499  27.78   1   28.38 ? 517 HOH   A O    1 
HETATM 5560 O  O    . HOH   G 4 .   ? 95.881  68.103  10.987  1   31.46 ? 518 HOH   A O    1 
HETATM 5561 O  O    . HOH   G 4 .   ? 87.957  25.093  12.426  1   56.39 ? 519 HOH   A O    1 
HETATM 5562 O  O    . HOH   G 4 .   ? 79.863  36.094  23.353  1   38.12 ? 520 HOH   A O    1 
HETATM 5563 O  O    . HOH   G 4 .   ? 84.009  55.012  15.356  1   47.45 ? 521 HOH   A O    1 
HETATM 5564 O  O    . HOH   G 4 .   ? 102.56  47.609  30.528  1   28.45 ? 522 HOH   A O    1 
HETATM 5565 O  O    . HOH   G 4 .   ? 95.525  69.76   8.799   1   33.87 ? 523 HOH   A O    1 
HETATM 5566 O  O    . HOH   G 4 .   ? 97.171  52.478  8.709   1   33.34 ? 524 HOH   A O    1 
HETATM 5567 O  O    . HOH   G 4 .   ? 84.835  61.014  7.785   1   42.76 ? 525 HOH   A O    1 
HETATM 5568 O  O    . HOH   G 4 .   ? 83.396  62.833  27.589  1   40.38 ? 526 HOH   A O    1 
HETATM 5569 O  O    . HOH   G 4 .   ? 70.571  78.11   3.181   1   61.61 ? 527 HOH   A O    1 
HETATM 5570 O  O    . HOH   G 4 .   ? 99.381  53.967  9.029   1   42.05 ? 528 HOH   A O    1 
HETATM 5571 O  O    . HOH   G 4 .   ? 80.527  42.601  22.998  1   41.85 ? 529 HOH   A O    1 
HETATM 5572 O  O    . HOH   G 4 .   ? 72.772  77.794  2.223   1   43.12 ? 530 HOH   A O    1 
HETATM 5573 O  O    . HOH   G 4 .   ? 104.731 56.031  17.622  1   32.56 ? 531 HOH   A O    1 
HETATM 5574 O  O    . HOH   G 4 .   ? 89.036  62.059  30.166  1   31.1  ? 532 HOH   A O    1 
HETATM 5575 O  O    . HOH   G 4 .   ? 102.01  61.624  15.827  1   33.89 ? 533 HOH   A O    1 
HETATM 5576 O  O    . HOH   G 4 .   ? 89.425  65.893  8.285   1   50.54 ? 534 HOH   A O    1 
HETATM 5577 O  O    . HOH   G 4 .   ? 80.506  64.995  12.635  1   40.29 ? 535 HOH   A O    1 
HETATM 5578 O  O    . HOH   G 4 .   ? 84.368  34.109  31.402  1   31.48 ? 536 HOH   A O    1 
HETATM 5579 O  O    . HOH   G 4 .   ? 72.287  26.068  13.77   1   43.63 ? 537 HOH   A O    1 
HETATM 5580 O  O    . HOH   G 4 .   ? 71.783  30.14   22.927  1   32.74 ? 538 HOH   A O    1 
HETATM 5581 O  O    . HOH   G 4 .   ? 79.68   37.768  25.611  1   45.21 ? 539 HOH   A O    1 
HETATM 5582 O  O    . HOH   G 4 .   ? 73.682  84.215  18.602  1   41.46 ? 540 HOH   A O    1 
HETATM 5583 O  O    . HOH   G 4 .   ? 88.703  41.876  31.027  1   39.04 ? 541 HOH   A O    1 
HETATM 5584 O  O    . HOH   G 4 .   ? 96.787  70.596  1.439   1   44.85 ? 542 HOH   A O    1 
HETATM 5585 O  O    . HOH   G 4 .   ? 82.475  36.315  31.994  1   41.7  ? 543 HOH   A O    1 
HETATM 5586 O  O    . HOH   G 4 .   ? 83.298  54.552  25.111  1   41.86 ? 544 HOH   A O    1 
HETATM 5587 O  O    . HOH   G 4 .   ? 77.245  39.891  13.882  1   30.76 ? 545 HOH   A O    1 
HETATM 5588 O  O    . HOH   G 4 .   ? 101.358 35.615  33.819  1   50.92 ? 546 HOH   A O    1 
HETATM 5589 O  O    . HOH   G 4 .   ? 96.879  42.429  7.151   1   54.07 ? 547 HOH   A O    1 
HETATM 5590 O  O    . HOH   G 4 .   ? 68.481  69.473  5.529   1   57.54 ? 548 HOH   A O    1 
HETATM 5591 O  O    . HOH   G 4 .   ? 109.583 82.949  24.031  1   62.78 ? 549 HOH   A O    1 
HETATM 5592 O  O    . HOH   G 4 .   ? 81.573  60.998  26.696  1   45.03 ? 550 HOH   A O    1 
HETATM 5593 O  O    . HOH   H 4 .   ? 60.472  39.924  30.004  1   42.64 ? 501 HOH   B O    1 
HETATM 5594 O  O    . HOH   H 4 .   ? 80.363  40.393  36.883  1   20.9  ? 502 HOH   B O    1 
HETATM 5595 O  O    . HOH   H 4 .   ? 62.576  61.807  24.079  1   32.71 ? 503 HOH   B O    1 
HETATM 5596 O  O    . HOH   H 4 .   ? 76.932  52.307  27.211  1   24.28 ? 504 HOH   B O    1 
HETATM 5597 O  O    . HOH   H 4 .   ? 81.822  37.22   35.194  1   41.33 ? 505 HOH   B O    1 
HETATM 5598 O  O    . HOH   H 4 .   ? 77.672  42.09   22.307  1   30.61 ? 506 HOH   B O    1 
HETATM 5599 O  O    . HOH   H 4 .   ? 70.669  40.01   15.166  1   38.26 ? 507 HOH   B O    1 
HETATM 5600 O  O    . HOH   H 4 .   ? 80.921  40.735  40.323  1   32.57 ? 508 HOH   B O    1 
HETATM 5601 O  O    . HOH   H 4 .   ? 57.73   54.116  22.218  1   30.73 ? 509 HOH   B O    1 
HETATM 5602 O  O    . HOH   H 4 .   ? 69.083  33.268  34.443  1   47.55 ? 510 HOH   B O    1 
HETATM 5603 O  O    . HOH   H 4 .   ? 70.136  75.986  15.587  1   52.88 ? 511 HOH   B O    1 
HETATM 5604 O  O    . HOH   H 4 .   ? 63.124  83.684  41.125  1   55.57 ? 512 HOH   B O    1 
HETATM 5605 O  O    . HOH   H 4 .   ? 82.161  50.271  32.831  1   30.16 ? 513 HOH   B O    1 
HETATM 5606 O  O    . HOH   H 4 .   ? 72.159  57.903  41.976  1   23.25 ? 514 HOH   B O    1 
HETATM 5607 O  O    . HOH   H 4 .   ? 76.166  32.068  32.66   1   39.75 ? 515 HOH   B O    1 
HETATM 5608 O  O    . HOH   H 4 .   ? 80.167  55.805  35.864  1   32.76 ? 516 HOH   B O    1 
HETATM 5609 O  O    . HOH   H 4 .   ? 65.367  61.02   22.443  1   34.26 ? 517 HOH   B O    1 
HETATM 5610 O  O    . HOH   H 4 .   ? 60.75   43.452  23.037  1   36.89 ? 518 HOH   B O    1 
HETATM 5611 O  O    . HOH   H 4 .   ? 68.235  34.671  18.894  1   35.76 ? 519 HOH   B O    1 
HETATM 5612 O  O    . HOH   H 4 .   ? 73.765  38.295  29.274  1   27.43 ? 520 HOH   B O    1 
HETATM 5613 O  O    . HOH   H 4 .   ? 83.401  43.928  34.191  1   32.23 ? 521 HOH   B O    1 
HETATM 5614 O  O    . HOH   H 4 .   ? 65.278  54.062  24.397  1   29.67 ? 522 HOH   B O    1 
HETATM 5615 O  O    . HOH   H 4 .   ? 81.73   51.134  30.327  1   33.16 ? 523 HOH   B O    1 
HETATM 5616 O  O    . HOH   H 4 .   ? 72.003  31.611  25.069  1   35.91 ? 524 HOH   B O    1 
HETATM 5617 O  O    . HOH   H 4 .   ? 78.955  44.24   30.452  1   37.11 ? 525 HOH   B O    1 
HETATM 5618 O  O    . HOH   H 4 .   ? 55.954  50.77   27.588  1   47.66 ? 526 HOH   B O    1 
HETATM 5619 O  O    . HOH   H 4 .   ? 76.509  43.449  43.212  1   26.76 ? 527 HOH   B O    1 
HETATM 5620 O  O    . HOH   H 4 .   ? 63.981  44.381  44.806  1   31.81 ? 528 HOH   B O    1 
HETATM 5621 O  O    . HOH   H 4 .   ? 67.564  52.744  24.556  1   27.34 ? 529 HOH   B O    1 
HETATM 5622 O  O    . HOH   H 4 .   ? 65.708  60.273  20.115  1   36.28 ? 530 HOH   B O    1 
HETATM 5623 O  O    . HOH   H 4 .   ? 63.637  36.673  31.484  1   44.22 ? 531 HOH   B O    1 
HETATM 5624 O  O    . HOH   H 4 .   ? 64.744  63.292  23.757  1   39.3  ? 532 HOH   B O    1 
HETATM 5625 O  O    . HOH   H 4 .   ? 78.304  53.948  28.79   1   34.04 ? 533 HOH   B O    1 
HETATM 5626 O  O    . HOH   H 4 .   ? 65.824  50.074  14.007  1   48.19 ? 534 HOH   B O    1 
HETATM 5627 O  O    . HOH   H 4 .   ? 60.203  55.12   24.168  1   41.89 ? 535 HOH   B O    1 
HETATM 5628 O  O    . HOH   H 4 .   ? 66.303  41.845  20.801  1   26.45 ? 536 HOH   B O    1 
HETATM 5629 O  O    . HOH   H 4 .   ? 63.631  41.036  21.315  1   34.11 ? 537 HOH   B O    1 
HETATM 5630 O  O    . HOH   H 4 .   ? 77.813  38.172  39.872  1   30.96 ? 538 HOH   B O    1 
HETATM 5631 O  O    . HOH   H 4 .   ? 53.204  52.925  21.352  1   35.5  ? 539 HOH   B O    1 
HETATM 5632 O  O    . HOH   H 4 .   ? 58.075  53.457  37.33   1   35.77 ? 540 HOH   B O    1 
HETATM 5633 O  O    . HOH   H 4 .   ? 77.219  62.363  31.708  1   40.56 ? 541 HOH   B O    1 
HETATM 5634 O  O    . HOH   H 4 .   ? 68.279  33.343  29.365  1   44.19 ? 542 HOH   B O    1 
HETATM 5635 O  O    . HOH   H 4 .   ? 69.203  40.784  22.722  1   38.66 ? 543 HOH   B O    1 
HETATM 5636 O  O    . HOH   H 4 .   ? 70.397  84.8    5.329   1   51.13 ? 544 HOH   B O    1 
HETATM 5637 O  O    . HOH   H 4 .   ? 63.086  73.667  10.79   1   37.51 ? 545 HOH   B O    1 
HETATM 5638 O  O    . HOH   H 4 .   ? 61.015  28.805  48.619  1   40.48 ? 546 HOH   B O    1 
HETATM 5639 O  O    . HOH   H 4 .   ? 70.889  39.953  50.496  1   48.07 ? 547 HOH   B O    1 
HETATM 5640 O  O    . HOH   H 4 .   ? 67.441  62.154  17.816  1   43.96 ? 548 HOH   B O    1 
HETATM 5641 O  O    . HOH   H 4 .   ? 74.059  74.081  26.222  1   57.8  ? 549 HOH   B O    1 
HETATM 5642 O  O    . HOH   H 4 .   ? 80.847  37.383  30.497  1   24.64 ? 550 HOH   B O    1 
HETATM 5643 O  O    . HOH   H 4 .   ? 64.783  46.458  12.021  1   61.2  ? 551 HOH   B O    1 
HETATM 5644 O  O    . HOH   H 4 .   ? 66.567  60.929  12.753  1   50.95 ? 552 HOH   B O    1 
HETATM 5645 O  O    . HOH   H 4 .   ? 50.935  47.42   35.555  1   39.32 ? 553 HOH   B O    1 
HETATM 5646 O  O    . HOH   H 4 .   ? 62.485  38.531  29.868  1   39.81 ? 554 HOH   B O    1 
HETATM 5647 O  O    . HOH   H 4 .   ? 78.154  35.576  41.276  1   46.5  ? 555 HOH   B O    1 
HETATM 5648 O  O    . HOH   H 4 .   ? 70.93   31.342  28.24   1   37.1  ? 556 HOH   B O    1 
HETATM 5649 O  O    . HOH   H 4 .   ? 78.052  37.979  47.571  1   53.36 ? 557 HOH   B O    1 
HETATM 5650 O  O    . HOH   H 4 .   ? 84.933  45.897  34.806  1   34.48 ? 558 HOH   B O    1 
# 
