data_9D1Y
# 
_entry.id   9D1Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9D1Y         pdb_00009d1y 10.2210/pdb9d1y/pdb 
WWPDB D_1000287167 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2025-02-05 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_citation_author.identifier_ORCID' 
13 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9D1Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              schulman@biochem.mpg.de 
_pdbx_contact_author.name_first         Brenda 
_pdbx_contact_author.name_last          Schulman 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3083-1126 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Schulman, B.A.' 1 ? 
'Scott, D.C.'    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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                9899 
_citation.page_last                 9899 
_citation.title                     'Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-54126-z 
_citation.pdbx_database_id_PubMed   39548056 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Scott, D.C.'    1  ?                   
primary 'Chittori, S.'   2  0000-0003-1417-6552 
primary 'Purser, N.'     3  0000-0003-2686-2277 
primary 'King, M.T.'     4  0000-0002-4192-8337 
primary 'Maiwald, S.A.'  5  0000-0002-7235-2748 
primary 'Churion, K.'    6  ?                   
primary 'Nourse, A.'     7  0000-0003-4595-5321 
primary 'Lee, C.'        8  0000-0002-5512-8146 
primary 'Paulo, J.A.'    9  0000-0002-4291-413X 
primary 'Miller, D.J.'   10 ?                   
primary 'Elledge, S.J.'  11 0000-0001-7923-6283 
primary 'Harper, J.W.'   12 0000-0002-6944-7236 
primary 'Kleiger, G.'    13 0000-0003-3924-1680 
primary 'Schulman, B.A.' 14 0000-0002-3083-1126 
# 
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 'Kelch domain-containing protein 3' 43245.082 1   ? ?    ? ? 
2 polymer     man Elongin-B                           11748.406 1   ? ?    ? ? 
3 polymer     man Elongin-C                           13855.611 1   ? ?    ? ? 
4 polymer     man Ubiquitin                           8676.973  1   ? G75R ? ? 
5 non-polymer syn GLYCEROL                            92.094    2   ? ?    ? ? 
6 water       nat water                               18.015    362 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Testis intracellular mediator protein' 
2 
;EloB,Elongin 18 kDa subunit,RNA polymerase II transcription factor SIII subunit B,SIII p18,Transcription elongation factor B polypeptide 2
;
3 
;EloC,Elongin 15 kDa subunit,RNA polymerase II transcription factor SIII subunit C,SIII p15,Transcription elongation factor B polypeptide 1
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;(ACE)MLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVKSAIRGQAPVVPY
MRYGHSTVLIDDTVLLWGGRNDTEGACNVLYAFDVNTHKWFTPRVSGTVPGARDGHSACVLGKIMYIFGGYEQQADCFSN
DIHKLDTSTMTWTLICTKGSPARWRDFHSATMLGSHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPPTPVL
PEGRRSHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPVSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEE
GLGDEFDLIDHSDLHILDFSPSLKTLCKLAVIQYNLDQSCLPHDIRWELNAMTTNSNISRPIVSSHK
;
;XMLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVKSAIRGQAPVVPYMRYG
HSTVLIDDTVLLWGGRNDTEGACNVLYAFDVNTHKWFTPRVSGTVPGARDGHSACVLGKIMYIFGGYEQQADCFSNDIHK
LDTSTMTWTLICTKGSPARWRDFHSATMLGSHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPPTPVLPEGR
RSHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPVSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEEGLGD
EFDLIDHSDLHILDFSPSLKTLCKLAVIQYNLDQSCLPHDIRWELNAMTTNSNISRPIVSSHK
;
A ? 
2 'polypeptide(L)' no no  
;MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFR
ADDTFEALCIEPFSSPPELPDVMK
;
;MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFR
ADDTFEALCIEPFSSPPELPDVMK
;
B ? 
3 'polypeptide(L)' no no  
;MSYYHHHHHHDYDIPTTENLYGQGAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLS
KVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
;
;MSYYHHHHHHDYDIPTTENLYGQGAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLS
KVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
;
C ? 
4 'polypeptide(L)' no no  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRRG 
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRRG D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5 GLYCEROL GOL 
6 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ACE n 
1 2   MET n 
1 3   LEU n 
1 4   ARG n 
1 5   TRP n 
1 6   THR n 
1 7   VAL n 
1 8   HIS n 
1 9   LEU n 
1 10  GLU n 
1 11  GLY n 
1 12  GLY n 
1 13  PRO n 
1 14  ARG n 
1 15  ARG n 
1 16  VAL n 
1 17  ASN n 
1 18  HIS n 
1 19  ALA n 
1 20  ALA n 
1 21  VAL n 
1 22  ALA n 
1 23  VAL n 
1 24  GLY n 
1 25  HIS n 
1 26  ARG n 
1 27  VAL n 
1 28  TYR n 
1 29  SER n 
1 30  PHE n 
1 31  GLY n 
1 32  GLY n 
1 33  TYR n 
1 34  CYS n 
1 35  SER n 
1 36  GLY n 
1 37  GLU n 
1 38  ASP n 
1 39  TYR n 
1 40  GLU n 
1 41  THR n 
1 42  LEU n 
1 43  ARG n 
1 44  GLN n 
1 45  ILE n 
1 46  ASP n 
1 47  VAL n 
1 48  HIS n 
1 49  ILE n 
1 50  PHE n 
1 51  ASN n 
1 52  ALA n 
1 53  VAL n 
1 54  SER n 
1 55  LEU n 
1 56  ARG n 
1 57  TRP n 
1 58  THR n 
1 59  LYS n 
1 60  LEU n 
1 61  PRO n 
1 62  PRO n 
1 63  VAL n 
1 64  LYS n 
1 65  SER n 
1 66  ALA n 
1 67  ILE n 
1 68  ARG n 
1 69  GLY n 
1 70  GLN n 
1 71  ALA n 
1 72  PRO n 
1 73  VAL n 
1 74  VAL n 
1 75  PRO n 
1 76  TYR n 
1 77  MET n 
1 78  ARG n 
1 79  TYR n 
1 80  GLY n 
1 81  HIS n 
1 82  SER n 
1 83  THR n 
1 84  VAL n 
1 85  LEU n 
1 86  ILE n 
1 87  ASP n 
1 88  ASP n 
1 89  THR n 
1 90  VAL n 
1 91  LEU n 
1 92  LEU n 
1 93  TRP n 
1 94  GLY n 
1 95  GLY n 
1 96  ARG n 
1 97  ASN n 
1 98  ASP n 
1 99  THR n 
1 100 GLU n 
1 101 GLY n 
1 102 ALA n 
1 103 CYS n 
1 104 ASN n 
1 105 VAL n 
1 106 LEU n 
1 107 TYR n 
1 108 ALA n 
1 109 PHE n 
1 110 ASP n 
1 111 VAL n 
1 112 ASN n 
1 113 THR n 
1 114 HIS n 
1 115 LYS n 
1 116 TRP n 
1 117 PHE n 
1 118 THR n 
1 119 PRO n 
1 120 ARG n 
1 121 VAL n 
1 122 SER n 
1 123 GLY n 
1 124 THR n 
1 125 VAL n 
1 126 PRO n 
1 127 GLY n 
1 128 ALA n 
1 129 ARG n 
1 130 ASP n 
1 131 GLY n 
1 132 HIS n 
1 133 SER n 
1 134 ALA n 
1 135 CYS n 
1 136 VAL n 
1 137 LEU n 
1 138 GLY n 
1 139 LYS n 
1 140 ILE n 
1 141 MET n 
1 142 TYR n 
1 143 ILE n 
1 144 PHE n 
1 145 GLY n 
1 146 GLY n 
1 147 TYR n 
1 148 GLU n 
1 149 GLN n 
1 150 GLN n 
1 151 ALA n 
1 152 ASP n 
1 153 CYS n 
1 154 PHE n 
1 155 SER n 
1 156 ASN n 
1 157 ASP n 
1 158 ILE n 
1 159 HIS n 
1 160 LYS n 
1 161 LEU n 
1 162 ASP n 
1 163 THR n 
1 164 SER n 
1 165 THR n 
1 166 MET n 
1 167 THR n 
1 168 TRP n 
1 169 THR n 
1 170 LEU n 
1 171 ILE n 
1 172 CYS n 
1 173 THR n 
1 174 LYS n 
1 175 GLY n 
1 176 SER n 
1 177 PRO n 
1 178 ALA n 
1 179 ARG n 
1 180 TRP n 
1 181 ARG n 
1 182 ASP n 
1 183 PHE n 
1 184 HIS n 
1 185 SER n 
1 186 ALA n 
1 187 THR n 
1 188 MET n 
1 189 LEU n 
1 190 GLY n 
1 191 SER n 
1 192 HIS n 
1 193 MET n 
1 194 TYR n 
1 195 VAL n 
1 196 PHE n 
1 197 GLY n 
1 198 GLY n 
1 199 ARG n 
1 200 ALA n 
1 201 ASP n 
1 202 ARG n 
1 203 PHE n 
1 204 GLY n 
1 205 PRO n 
1 206 PHE n 
1 207 HIS n 
1 208 SER n 
1 209 ASN n 
1 210 ASN n 
1 211 GLU n 
1 212 ILE n 
1 213 TYR n 
1 214 CYS n 
1 215 ASN n 
1 216 ARG n 
1 217 ILE n 
1 218 ARG n 
1 219 VAL n 
1 220 PHE n 
1 221 ASP n 
1 222 THR n 
1 223 ARG n 
1 224 THR n 
1 225 GLU n 
1 226 ALA n 
1 227 TRP n 
1 228 LEU n 
1 229 ASP n 
1 230 CYS n 
1 231 PRO n 
1 232 PRO n 
1 233 THR n 
1 234 PRO n 
1 235 VAL n 
1 236 LEU n 
1 237 PRO n 
1 238 GLU n 
1 239 GLY n 
1 240 ARG n 
1 241 ARG n 
1 242 SER n 
1 243 HIS n 
1 244 SER n 
1 245 ALA n 
1 246 PHE n 
1 247 GLY n 
1 248 TYR n 
1 249 ASN n 
1 250 GLY n 
1 251 GLU n 
1 252 LEU n 
1 253 TYR n 
1 254 ILE n 
1 255 PHE n 
1 256 GLY n 
1 257 GLY n 
1 258 TYR n 
1 259 ASN n 
1 260 ALA n 
1 261 ARG n 
1 262 LEU n 
1 263 ASN n 
1 264 ARG n 
1 265 HIS n 
1 266 PHE n 
1 267 HIS n 
1 268 ASP n 
1 269 LEU n 
1 270 TRP n 
1 271 LYS n 
1 272 PHE n 
1 273 ASN n 
1 274 PRO n 
1 275 VAL n 
1 276 SER n 
1 277 PHE n 
1 278 THR n 
1 279 TRP n 
1 280 LYS n 
1 281 LYS n 
1 282 ILE n 
1 283 GLU n 
1 284 PRO n 
1 285 LYS n 
1 286 GLY n 
1 287 LYS n 
1 288 GLY n 
1 289 PRO n 
1 290 CYS n 
1 291 PRO n 
1 292 ARG n 
1 293 ARG n 
1 294 ARG n 
1 295 GLN n 
1 296 CYS n 
1 297 CYS n 
1 298 CYS n 
1 299 ILE n 
1 300 VAL n 
1 301 GLY n 
1 302 ASP n 
1 303 LYS n 
1 304 ILE n 
1 305 VAL n 
1 306 LEU n 
1 307 PHE n 
1 308 GLY n 
1 309 GLY n 
1 310 THR n 
1 311 SER n 
1 312 PRO n 
1 313 SER n 
1 314 PRO n 
1 315 GLU n 
1 316 GLU n 
1 317 GLY n 
1 318 LEU n 
1 319 GLY n 
1 320 ASP n 
1 321 GLU n 
1 322 PHE n 
1 323 ASP n 
1 324 LEU n 
1 325 ILE n 
1 326 ASP n 
1 327 HIS n 
1 328 SER n 
1 329 ASP n 
1 330 LEU n 
1 331 HIS n 
1 332 ILE n 
1 333 LEU n 
1 334 ASP n 
1 335 PHE n 
1 336 SER n 
1 337 PRO n 
1 338 SER n 
1 339 LEU n 
1 340 LYS n 
1 341 THR n 
1 342 LEU n 
1 343 CYS n 
1 344 LYS n 
1 345 LEU n 
1 346 ALA n 
1 347 VAL n 
1 348 ILE n 
1 349 GLN n 
1 350 TYR n 
1 351 ASN n 
1 352 LEU n 
1 353 ASP n 
1 354 GLN n 
1 355 SER n 
1 356 CYS n 
1 357 LEU n 
1 358 PRO n 
1 359 HIS n 
1 360 ASP n 
1 361 ILE n 
1 362 ARG n 
1 363 TRP n 
1 364 GLU n 
1 365 LEU n 
1 366 ASN n 
1 367 ALA n 
1 368 MET n 
1 369 THR n 
1 370 THR n 
1 371 ASN n 
1 372 SER n 
1 373 ASN n 
1 374 ILE n 
1 375 SER n 
1 376 ARG n 
1 377 PRO n 
1 378 ILE n 
1 379 VAL n 
1 380 SER n 
1 381 SER n 
1 382 HIS n 
1 383 LYS n 
2 1   MET n 
2 2   ASP n 
2 3   VAL n 
2 4   PHE n 
2 5   LEU n 
2 6   MET n 
2 7   ILE n 
2 8   ARG n 
2 9   ARG n 
2 10  HIS n 
2 11  LYS n 
2 12  THR n 
2 13  THR n 
2 14  ILE n 
2 15  PHE n 
2 16  THR n 
2 17  ASP n 
2 18  ALA n 
2 19  LYS n 
2 20  GLU n 
2 21  SER n 
2 22  SER n 
2 23  THR n 
2 24  VAL n 
2 25  PHE n 
2 26  GLU n 
2 27  LEU n 
2 28  LYS n 
2 29  ARG n 
2 30  ILE n 
2 31  VAL n 
2 32  GLU n 
2 33  GLY n 
2 34  ILE n 
2 35  LEU n 
2 36  LYS n 
2 37  ARG n 
2 38  PRO n 
2 39  PRO n 
2 40  ASP n 
2 41  GLU n 
2 42  GLN n 
2 43  ARG n 
2 44  LEU n 
2 45  TYR n 
2 46  LYS n 
2 47  ASP n 
2 48  ASP n 
2 49  GLN n 
2 50  LEU n 
2 51  LEU n 
2 52  ASP n 
2 53  ASP n 
2 54  GLY n 
2 55  LYS n 
2 56  THR n 
2 57  LEU n 
2 58  GLY n 
2 59  GLU n 
2 60  CYS n 
2 61  GLY n 
2 62  PHE n 
2 63  THR n 
2 64  SER n 
2 65  GLN n 
2 66  THR n 
2 67  ALA n 
2 68  ARG n 
2 69  PRO n 
2 70  GLN n 
2 71  ALA n 
2 72  PRO n 
2 73  ALA n 
2 74  THR n 
2 75  VAL n 
2 76  GLY n 
2 77  LEU n 
2 78  ALA n 
2 79  PHE n 
2 80  ARG n 
2 81  ALA n 
2 82  ASP n 
2 83  ASP n 
2 84  THR n 
2 85  PHE n 
2 86  GLU n 
2 87  ALA n 
2 88  LEU n 
2 89  CYS n 
2 90  ILE n 
2 91  GLU n 
2 92  PRO n 
2 93  PHE n 
2 94  SER n 
2 95  SER n 
2 96  PRO n 
2 97  PRO n 
2 98  GLU n 
2 99  LEU n 
2 100 PRO n 
2 101 ASP n 
2 102 VAL n 
2 103 MET n 
2 104 LYS n 
3 1   MET n 
3 2   SER n 
3 3   TYR n 
3 4   TYR n 
3 5   HIS n 
3 6   HIS n 
3 7   HIS n 
3 8   HIS n 
3 9   HIS n 
3 10  HIS n 
3 11  ASP n 
3 12  TYR n 
3 13  ASP n 
3 14  ILE n 
3 15  PRO n 
3 16  THR n 
3 17  THR n 
3 18  GLU n 
3 19  ASN n 
3 20  LEU n 
3 21  TYR n 
3 22  GLY n 
3 23  GLN n 
3 24  GLY n 
3 25  ALA n 
3 26  MET n 
3 27  TYR n 
3 28  VAL n 
3 29  LYS n 
3 30  LEU n 
3 31  ILE n 
3 32  SER n 
3 33  SER n 
3 34  ASP n 
3 35  GLY n 
3 36  HIS n 
3 37  GLU n 
3 38  PHE n 
3 39  ILE n 
3 40  VAL n 
3 41  LYS n 
3 42  ARG n 
3 43  GLU n 
3 44  HIS n 
3 45  ALA n 
3 46  LEU n 
3 47  THR n 
3 48  SER n 
3 49  GLY n 
3 50  THR n 
3 51  ILE n 
3 52  LYS n 
3 53  ALA n 
3 54  MET n 
3 55  LEU n 
3 56  SER n 
3 57  GLY n 
3 58  PRO n 
3 59  GLY n 
3 60  GLN n 
3 61  PHE n 
3 62  ALA n 
3 63  GLU n 
3 64  ASN n 
3 65  GLU n 
3 66  THR n 
3 67  ASN n 
3 68  GLU n 
3 69  VAL n 
3 70  ASN n 
3 71  PHE n 
3 72  ARG n 
3 73  GLU n 
3 74  ILE n 
3 75  PRO n 
3 76  SER n 
3 77  HIS n 
3 78  VAL n 
3 79  LEU n 
3 80  SER n 
3 81  LYS n 
3 82  VAL n 
3 83  CYS n 
3 84  MET n 
3 85  TYR n 
3 86  PHE n 
3 87  THR n 
3 88  TYR n 
3 89  LYS n 
3 90  VAL n 
3 91  ARG n 
3 92  TYR n 
3 93  THR n 
3 94  ASN n 
3 95  SER n 
3 96  SER n 
3 97  THR n 
3 98  GLU n 
3 99  ILE n 
3 100 PRO n 
3 101 GLU n 
3 102 PHE n 
3 103 PRO n 
3 104 ILE n 
3 105 ALA n 
3 106 PRO n 
3 107 GLU n 
3 108 ILE n 
3 109 ALA n 
3 110 LEU n 
3 111 GLU n 
3 112 LEU n 
3 113 LEU n 
3 114 MET n 
3 115 ALA n 
3 116 ALA n 
3 117 ASN n 
3 118 PHE n 
3 119 LEU n 
3 120 ASP n 
3 121 CYS n 
4 1   MET n 
4 2   GLN n 
4 3   ILE n 
4 4   PHE n 
4 5   VAL n 
4 6   LYS n 
4 7   THR n 
4 8   LEU n 
4 9   THR n 
4 10  GLY n 
4 11  LYS n 
4 12  THR n 
4 13  ILE n 
4 14  THR n 
4 15  LEU n 
4 16  GLU n 
4 17  VAL n 
4 18  GLU n 
4 19  PRO n 
4 20  SER n 
4 21  ASP n 
4 22  THR n 
4 23  ILE n 
4 24  GLU n 
4 25  ASN n 
4 26  VAL n 
4 27  LYS n 
4 28  ALA n 
4 29  LYS n 
4 30  ILE n 
4 31  GLN n 
4 32  ASP n 
4 33  LYS n 
4 34  GLU n 
4 35  GLY n 
4 36  ILE n 
4 37  PRO n 
4 38  PRO n 
4 39  ASP n 
4 40  GLN n 
4 41  GLN n 
4 42  ARG n 
4 43  LEU n 
4 44  ILE n 
4 45  PHE n 
4 46  ALA n 
4 47  GLY n 
4 48  LYS n 
4 49  GLN n 
4 50  LEU n 
4 51  GLU n 
4 52  ASP n 
4 53  GLY n 
4 54  ARG n 
4 55  THR n 
4 56  LEU n 
4 57  SER n 
4 58  ASP n 
4 59  TYR n 
4 60  ASN n 
4 61  ILE n 
4 62  GLN n 
4 63  LYS n 
4 64  GLU n 
4 65  SER n 
4 66  THR n 
4 67  LEU n 
4 68  HIS n 
4 69  LEU n 
4 70  VAL n 
4 71  LEU n 
4 72  ARG n 
4 73  LEU n 
4 74  ARG n 
4 75  ARG n 
4 76  GLY n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 383 human ? 'KLHDC3, PEAS' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Trichoplusia ni'  
7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 104 human ? 'ELOB, TCEB2'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Trichoplusia ni'  
7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 121 human ? 'ELOC, TCEB1'  ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Trichoplusia ni'  
7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 76  human ? UBC            ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ACE non-polymer         . 'ACETYL GROUP'  ?                               'C2 H4 O'        44.053  
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
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   ACE 1   0   1   ACE AME A . n 
A 1 2   MET 2   1   1   MET AME A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   ARG 4   3   3   ARG ARG A . n 
A 1 5   TRP 5   4   4   TRP TRP A . n 
A 1 6   THR 6   5   5   THR THR A . n 
A 1 7   VAL 7   6   6   VAL VAL A . n 
A 1 8   HIS 8   7   7   HIS HIS A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  GLU 10  9   9   GLU GLU A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  GLY 12  11  11  GLY GLY A . n 
A 1 13  PRO 13  12  12  PRO PRO A . n 
A 1 14  ARG 14  13  13  ARG ARG A . n 
A 1 15  ARG 15  14  14  ARG ARG A . n 
A 1 16  VAL 16  15  15  VAL VAL A . n 
A 1 17  ASN 17  16  16  ASN ASN A . n 
A 1 18  HIS 18  17  17  HIS HIS A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  ALA 20  19  19  ALA ALA A . n 
A 1 21  VAL 21  20  20  VAL VAL A . n 
A 1 22  ALA 22  21  21  ALA ALA A . n 
A 1 23  VAL 23  22  22  VAL VAL A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  HIS 25  24  24  HIS HIS A . n 
A 1 26  ARG 26  25  25  ARG ARG A . n 
A 1 27  VAL 27  26  26  VAL VAL A . n 
A 1 28  TYR 28  27  27  TYR TYR A . n 
A 1 29  SER 29  28  28  SER SER A . n 
A 1 30  PHE 30  29  29  PHE PHE A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  GLY 32  31  31  GLY GLY A . n 
A 1 33  TYR 33  32  32  TYR TYR A . n 
A 1 34  CYS 34  33  33  CYS CYS A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  GLY 36  35  35  GLY GLY A . n 
A 1 37  GLU 37  36  36  GLU GLU A . n 
A 1 38  ASP 38  37  37  ASP ASP A . n 
A 1 39  TYR 39  38  38  TYR TYR A . n 
A 1 40  GLU 40  39  39  GLU GLU A . n 
A 1 41  THR 41  40  40  THR THR A . n 
A 1 42  LEU 42  41  41  LEU LEU A . n 
A 1 43  ARG 43  42  42  ARG ARG A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  ILE 45  44  44  ILE ILE A . n 
A 1 46  ASP 46  45  45  ASP ASP A . n 
A 1 47  VAL 47  46  46  VAL VAL A . n 
A 1 48  HIS 48  47  47  HIS HIS A . n 
A 1 49  ILE 49  48  48  ILE ILE A . n 
A 1 50  PHE 50  49  49  PHE PHE A . n 
A 1 51  ASN 51  50  50  ASN ASN A . n 
A 1 52  ALA 52  51  51  ALA ALA A . n 
A 1 53  VAL 53  52  52  VAL VAL A . n 
A 1 54  SER 54  53  53  SER SER A . n 
A 1 55  LEU 55  54  54  LEU LEU A . n 
A 1 56  ARG 56  55  55  ARG ARG A . n 
A 1 57  TRP 57  56  56  TRP TRP A . n 
A 1 58  THR 58  57  57  THR THR A . n 
A 1 59  LYS 59  58  58  LYS LYS A . n 
A 1 60  LEU 60  59  59  LEU LEU A . n 
A 1 61  PRO 61  60  60  PRO PRO A . n 
A 1 62  PRO 62  61  61  PRO PRO A . n 
A 1 63  VAL 63  62  62  VAL VAL A . n 
A 1 64  LYS 64  63  63  LYS LYS A . n 
A 1 65  SER 65  64  64  SER SER A . n 
A 1 66  ALA 66  65  65  ALA ALA A . n 
A 1 67  ILE 67  66  66  ILE ILE A . n 
A 1 68  ARG 68  67  67  ARG ARG A . n 
A 1 69  GLY 69  68  68  GLY GLY A . n 
A 1 70  GLN 70  69  69  GLN GLN A . n 
A 1 71  ALA 71  70  70  ALA ALA A . n 
A 1 72  PRO 72  71  71  PRO PRO A . n 
A 1 73  VAL 73  72  72  VAL VAL A . n 
A 1 74  VAL 74  73  73  VAL VAL A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  TYR 76  75  75  TYR TYR A . n 
A 1 77  MET 77  76  76  MET MET A . n 
A 1 78  ARG 78  77  77  ARG ARG A . n 
A 1 79  TYR 79  78  78  TYR TYR A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  SER 82  81  81  SER SER A . n 
A 1 83  THR 83  82  82  THR THR A . n 
A 1 84  VAL 84  83  83  VAL VAL A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  ILE 86  85  85  ILE ILE A . n 
A 1 87  ASP 87  86  86  ASP ASP A . n 
A 1 88  ASP 88  87  87  ASP ASP A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  VAL 90  89  89  VAL VAL A . n 
A 1 91  LEU 91  90  90  LEU LEU A . n 
A 1 92  LEU 92  91  91  LEU LEU A . n 
A 1 93  TRP 93  92  92  TRP TRP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  GLY 95  94  94  GLY GLY A . n 
A 1 96  ARG 96  95  95  ARG ARG A . n 
A 1 97  ASN 97  96  96  ASN ASN A . n 
A 1 98  ASP 98  97  97  ASP ASP A . n 
A 1 99  THR 99  98  98  THR THR A . n 
A 1 100 GLU 100 99  99  GLU GLU A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 ALA 102 101 101 ALA ALA A . n 
A 1 103 CYS 103 102 102 CYS CYS A . n 
A 1 104 ASN 104 103 103 ASN ASN A . n 
A 1 105 VAL 105 104 104 VAL VAL A . n 
A 1 106 LEU 106 105 105 LEU LEU A . n 
A 1 107 TYR 107 106 106 TYR TYR A . n 
A 1 108 ALA 108 107 107 ALA ALA A . n 
A 1 109 PHE 109 108 108 PHE PHE A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 VAL 111 110 110 VAL VAL A . n 
A 1 112 ASN 112 111 111 ASN ASN A . n 
A 1 113 THR 113 112 112 THR THR A . n 
A 1 114 HIS 114 113 113 HIS HIS A . n 
A 1 115 LYS 115 114 114 LYS LYS A . n 
A 1 116 TRP 116 115 115 TRP TRP A . n 
A 1 117 PHE 117 116 116 PHE PHE A . n 
A 1 118 THR 118 117 117 THR THR A . n 
A 1 119 PRO 119 118 118 PRO PRO A . n 
A 1 120 ARG 120 119 119 ARG ARG A . n 
A 1 121 VAL 121 120 120 VAL VAL A . n 
A 1 122 SER 122 121 121 SER SER A . n 
A 1 123 GLY 123 122 122 GLY GLY A . n 
A 1 124 THR 124 123 123 THR THR A . n 
A 1 125 VAL 125 124 124 VAL VAL A . n 
A 1 126 PRO 126 125 125 PRO PRO A . n 
A 1 127 GLY 127 126 126 GLY GLY A . n 
A 1 128 ALA 128 127 127 ALA ALA A . n 
A 1 129 ARG 129 128 128 ARG ARG A . n 
A 1 130 ASP 130 129 129 ASP ASP A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 HIS 132 131 131 HIS HIS A . n 
A 1 133 SER 133 132 132 SER SER A . n 
A 1 134 ALA 134 133 133 ALA ALA A . n 
A 1 135 CYS 135 134 134 CYS CYS A . n 
A 1 136 VAL 136 135 135 VAL VAL A . n 
A 1 137 LEU 137 136 136 LEU LEU A . n 
A 1 138 GLY 138 137 137 GLY GLY A . n 
A 1 139 LYS 139 138 138 LYS LYS A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 MET 141 140 140 MET MET A . n 
A 1 142 TYR 142 141 141 TYR TYR A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 PHE 144 143 143 PHE PHE A . n 
A 1 145 GLY 145 144 144 GLY GLY A . n 
A 1 146 GLY 146 145 145 GLY GLY A . n 
A 1 147 TYR 147 146 146 TYR TYR A . n 
A 1 148 GLU 148 147 147 GLU GLU A . n 
A 1 149 GLN 149 148 148 GLN GLN A . n 
A 1 150 GLN 150 149 149 GLN GLN A . n 
A 1 151 ALA 151 150 150 ALA ALA A . n 
A 1 152 ASP 152 151 151 ASP ASP A . n 
A 1 153 CYS 153 152 152 CYS CYS A . n 
A 1 154 PHE 154 153 153 PHE PHE A . n 
A 1 155 SER 155 154 154 SER SER A . n 
A 1 156 ASN 156 155 155 ASN ASN A . n 
A 1 157 ASP 157 156 156 ASP ASP A . n 
A 1 158 ILE 158 157 157 ILE ILE A . n 
A 1 159 HIS 159 158 158 HIS HIS A . n 
A 1 160 LYS 160 159 159 LYS LYS A . n 
A 1 161 LEU 161 160 160 LEU LEU A . n 
A 1 162 ASP 162 161 161 ASP ASP A . n 
A 1 163 THR 163 162 162 THR THR A . n 
A 1 164 SER 164 163 163 SER SER A . n 
A 1 165 THR 165 164 164 THR THR A . n 
A 1 166 MET 166 165 165 MET MET A . n 
A 1 167 THR 167 166 166 THR THR A . n 
A 1 168 TRP 168 167 167 TRP TRP A . n 
A 1 169 THR 169 168 168 THR THR A . n 
A 1 170 LEU 170 169 169 LEU LEU A . n 
A 1 171 ILE 171 170 170 ILE ILE A . n 
A 1 172 CYS 172 171 171 CYS CYS A . n 
A 1 173 THR 173 172 172 THR THR A . n 
A 1 174 LYS 174 173 173 LYS LYS A . n 
A 1 175 GLY 175 174 174 GLY GLY A . n 
A 1 176 SER 176 175 175 SER SER A . n 
A 1 177 PRO 177 176 176 PRO PRO A . n 
A 1 178 ALA 178 177 177 ALA ALA A . n 
A 1 179 ARG 179 178 178 ARG ARG A . n 
A 1 180 TRP 180 179 179 TRP TRP A . n 
A 1 181 ARG 181 180 180 ARG ARG A . n 
A 1 182 ASP 182 181 181 ASP ASP A . n 
A 1 183 PHE 183 182 182 PHE PHE A . n 
A 1 184 HIS 184 183 183 HIS HIS A . n 
A 1 185 SER 185 184 184 SER SER A . n 
A 1 186 ALA 186 185 185 ALA ALA A . n 
A 1 187 THR 187 186 186 THR THR A . n 
A 1 188 MET 188 187 187 MET MET A . n 
A 1 189 LEU 189 188 188 LEU LEU A . n 
A 1 190 GLY 190 189 189 GLY GLY A . n 
A 1 191 SER 191 190 190 SER SER A . n 
A 1 192 HIS 192 191 191 HIS HIS A . n 
A 1 193 MET 193 192 192 MET MET A . n 
A 1 194 TYR 194 193 193 TYR TYR A . n 
A 1 195 VAL 195 194 194 VAL VAL A . n 
A 1 196 PHE 196 195 195 PHE PHE A . n 
A 1 197 GLY 197 196 196 GLY GLY A . n 
A 1 198 GLY 198 197 197 GLY GLY A . n 
A 1 199 ARG 199 198 198 ARG ARG A . n 
A 1 200 ALA 200 199 199 ALA ALA A . n 
A 1 201 ASP 201 200 200 ASP ASP A . n 
A 1 202 ARG 202 201 201 ARG ARG A . n 
A 1 203 PHE 203 202 202 PHE PHE A . n 
A 1 204 GLY 204 203 203 GLY GLY A . n 
A 1 205 PRO 205 204 204 PRO PRO A . n 
A 1 206 PHE 206 205 205 PHE PHE A . n 
A 1 207 HIS 207 206 206 HIS HIS A . n 
A 1 208 SER 208 207 207 SER SER A . n 
A 1 209 ASN 209 208 208 ASN ASN A . n 
A 1 210 ASN 210 209 209 ASN ASN A . n 
A 1 211 GLU 211 210 210 GLU GLU A . n 
A 1 212 ILE 212 211 211 ILE ILE A . n 
A 1 213 TYR 213 212 212 TYR TYR A . n 
A 1 214 CYS 214 213 213 CYS CYS A . n 
A 1 215 ASN 215 214 214 ASN ASN A . n 
A 1 216 ARG 216 215 215 ARG ARG A . n 
A 1 217 ILE 217 216 216 ILE ILE A . n 
A 1 218 ARG 218 217 217 ARG ARG A . n 
A 1 219 VAL 219 218 218 VAL VAL A . n 
A 1 220 PHE 220 219 219 PHE PHE A . n 
A 1 221 ASP 221 220 220 ASP ASP A . n 
A 1 222 THR 222 221 221 THR THR A . n 
A 1 223 ARG 223 222 222 ARG ARG A . n 
A 1 224 THR 224 223 223 THR THR A . n 
A 1 225 GLU 225 224 224 GLU GLU A . n 
A 1 226 ALA 226 225 225 ALA ALA A . n 
A 1 227 TRP 227 226 226 TRP TRP A . n 
A 1 228 LEU 228 227 227 LEU LEU A . n 
A 1 229 ASP 229 228 228 ASP ASP A . n 
A 1 230 CYS 230 229 229 CYS CYS A . n 
A 1 231 PRO 231 230 230 PRO PRO A . n 
A 1 232 PRO 232 231 231 PRO PRO A . n 
A 1 233 THR 233 232 232 THR THR A . n 
A 1 234 PRO 234 233 233 PRO PRO A . n 
A 1 235 VAL 235 234 234 VAL VAL A . n 
A 1 236 LEU 236 235 235 LEU LEU A . n 
A 1 237 PRO 237 236 236 PRO PRO A . n 
A 1 238 GLU 238 237 237 GLU GLU A . n 
A 1 239 GLY 239 238 238 GLY GLY A . n 
A 1 240 ARG 240 239 239 ARG ARG A . n 
A 1 241 ARG 241 240 240 ARG ARG A . n 
A 1 242 SER 242 241 241 SER SER A . n 
A 1 243 HIS 243 242 242 HIS HIS A . n 
A 1 244 SER 244 243 243 SER SER A . n 
A 1 245 ALA 245 244 244 ALA ALA A . n 
A 1 246 PHE 246 245 245 PHE PHE A . n 
A 1 247 GLY 247 246 246 GLY GLY A . n 
A 1 248 TYR 248 247 247 TYR TYR A . n 
A 1 249 ASN 249 248 248 ASN ASN A . n 
A 1 250 GLY 250 249 249 GLY GLY A . n 
A 1 251 GLU 251 250 250 GLU GLU A . n 
A 1 252 LEU 252 251 251 LEU LEU A . n 
A 1 253 TYR 253 252 252 TYR TYR A . n 
A 1 254 ILE 254 253 253 ILE ILE A . n 
A 1 255 PHE 255 254 254 PHE PHE A . n 
A 1 256 GLY 256 255 255 GLY GLY A . n 
A 1 257 GLY 257 256 256 GLY GLY A . n 
A 1 258 TYR 258 257 257 TYR TYR A . n 
A 1 259 ASN 259 258 258 ASN ASN A . n 
A 1 260 ALA 260 259 259 ALA ALA A . n 
A 1 261 ARG 261 260 260 ARG ARG A . n 
A 1 262 LEU 262 261 261 LEU LEU A . n 
A 1 263 ASN 263 262 262 ASN ASN A . n 
A 1 264 ARG 264 263 263 ARG ARG A . n 
A 1 265 HIS 265 264 264 HIS HIS A . n 
A 1 266 PHE 266 265 265 PHE PHE A . n 
A 1 267 HIS 267 266 266 HIS HIS A . n 
A 1 268 ASP 268 267 267 ASP ASP A . n 
A 1 269 LEU 269 268 268 LEU LEU A . n 
A 1 270 TRP 270 269 269 TRP TRP A . n 
A 1 271 LYS 271 270 270 LYS LYS A . n 
A 1 272 PHE 272 271 271 PHE PHE A . n 
A 1 273 ASN 273 272 272 ASN ASN A . n 
A 1 274 PRO 274 273 273 PRO PRO A . n 
A 1 275 VAL 275 274 274 VAL VAL A . n 
A 1 276 SER 276 275 275 SER SER A . n 
A 1 277 PHE 277 276 276 PHE PHE A . n 
A 1 278 THR 278 277 277 THR THR A . n 
A 1 279 TRP 279 278 278 TRP TRP A . n 
A 1 280 LYS 280 279 279 LYS LYS A . n 
A 1 281 LYS 281 280 280 LYS LYS A . n 
A 1 282 ILE 282 281 281 ILE ILE A . n 
A 1 283 GLU 283 282 282 GLU GLU A . n 
A 1 284 PRO 284 283 283 PRO PRO A . n 
A 1 285 LYS 285 284 284 LYS LYS A . n 
A 1 286 GLY 286 285 285 GLY GLY A . n 
A 1 287 LYS 287 286 286 LYS LYS A . n 
A 1 288 GLY 288 287 287 GLY GLY A . n 
A 1 289 PRO 289 288 288 PRO PRO A . n 
A 1 290 CYS 290 289 289 CYS CYS A . n 
A 1 291 PRO 291 290 290 PRO PRO A . n 
A 1 292 ARG 292 291 291 ARG ARG A . n 
A 1 293 ARG 293 292 292 ARG ARG A . n 
A 1 294 ARG 294 293 293 ARG ARG A . n 
A 1 295 GLN 295 294 294 GLN GLN A . n 
A 1 296 CYS 296 295 295 CYS CYS A . n 
A 1 297 CYS 297 296 296 CYS CYS A . n 
A 1 298 CYS 298 297 297 CYS CYS A . n 
A 1 299 ILE 299 298 298 ILE ILE A . n 
A 1 300 VAL 300 299 299 VAL VAL A . n 
A 1 301 GLY 301 300 300 GLY GLY A . n 
A 1 302 ASP 302 301 301 ASP ASP A . n 
A 1 303 LYS 303 302 302 LYS LYS A . n 
A 1 304 ILE 304 303 303 ILE ILE A . n 
A 1 305 VAL 305 304 304 VAL VAL A . n 
A 1 306 LEU 306 305 305 LEU LEU A . n 
A 1 307 PHE 307 306 306 PHE PHE A . n 
A 1 308 GLY 308 307 307 GLY GLY A . n 
A 1 309 GLY 309 308 308 GLY GLY A . n 
A 1 310 THR 310 309 309 THR THR A . n 
A 1 311 SER 311 310 310 SER SER A . n 
A 1 312 PRO 312 311 311 PRO PRO A . n 
A 1 313 SER 313 312 312 SER SER A . n 
A 1 314 PRO 314 313 313 PRO PRO A . n 
A 1 315 GLU 315 314 ?   ?   ?   A . n 
A 1 316 GLU 316 315 ?   ?   ?   A . n 
A 1 317 GLY 317 316 ?   ?   ?   A . n 
A 1 318 LEU 318 317 ?   ?   ?   A . n 
A 1 319 GLY 319 318 ?   ?   ?   A . n 
A 1 320 ASP 320 319 ?   ?   ?   A . n 
A 1 321 GLU 321 320 ?   ?   ?   A . n 
A 1 322 PHE 322 321 321 PHE PHE A . n 
A 1 323 ASP 323 322 322 ASP ASP A . n 
A 1 324 LEU 324 323 323 LEU LEU A . n 
A 1 325 ILE 325 324 324 ILE ILE A . n 
A 1 326 ASP 326 325 325 ASP ASP A . n 
A 1 327 HIS 327 326 326 HIS HIS A . n 
A 1 328 SER 328 327 327 SER SER A . n 
A 1 329 ASP 329 328 328 ASP ASP A . n 
A 1 330 LEU 330 329 329 LEU LEU A . n 
A 1 331 HIS 331 330 330 HIS HIS A . n 
A 1 332 ILE 332 331 331 ILE ILE A . n 
A 1 333 LEU 333 332 332 LEU LEU A . n 
A 1 334 ASP 334 333 333 ASP ASP A . n 
A 1 335 PHE 335 334 334 PHE PHE A . n 
A 1 336 SER 336 335 335 SER SER A . n 
A 1 337 PRO 337 336 336 PRO PRO A . n 
A 1 338 SER 338 337 337 SER SER A . n 
A 1 339 LEU 339 338 338 LEU LEU A . n 
A 1 340 LYS 340 339 339 LYS LYS A . n 
A 1 341 THR 341 340 340 THR THR A . n 
A 1 342 LEU 342 341 341 LEU LEU A . n 
A 1 343 CYS 343 342 342 CYS CYS A . n 
A 1 344 LYS 344 343 343 LYS LYS A . n 
A 1 345 LEU 345 344 344 LEU LEU A . n 
A 1 346 ALA 346 345 345 ALA ALA A . n 
A 1 347 VAL 347 346 346 VAL VAL A . n 
A 1 348 ILE 348 347 347 ILE ILE A . n 
A 1 349 GLN 349 348 348 GLN GLN A . n 
A 1 350 TYR 350 349 349 TYR TYR A . n 
A 1 351 ASN 351 350 350 ASN ASN A . n 
A 1 352 LEU 352 351 351 LEU LEU A . n 
A 1 353 ASP 353 352 352 ASP ASP A . n 
A 1 354 GLN 354 353 353 GLN GLN A . n 
A 1 355 SER 355 354 354 SER SER A . n 
A 1 356 CYS 356 355 355 CYS CYS A . n 
A 1 357 LEU 357 356 356 LEU LEU A . n 
A 1 358 PRO 358 357 357 PRO PRO A . n 
A 1 359 HIS 359 358 358 HIS HIS A . n 
A 1 360 ASP 360 359 359 ASP ASP A . n 
A 1 361 ILE 361 360 360 ILE ILE A . n 
A 1 362 ARG 362 361 361 ARG ARG A . n 
A 1 363 TRP 363 362 362 TRP TRP A . n 
A 1 364 GLU 364 363 363 GLU GLU A . n 
A 1 365 LEU 365 364 364 LEU LEU A . n 
A 1 366 ASN 366 365 365 ASN ASN A . n 
A 1 367 ALA 367 366 366 ALA ALA A . n 
A 1 368 MET 368 367 367 MET MET A . n 
A 1 369 THR 369 368 368 THR THR A . n 
A 1 370 THR 370 369 369 THR THR A . n 
A 1 371 ASN 371 370 370 ASN ASN A . n 
A 1 372 SER 372 371 371 SER SER A . n 
A 1 373 ASN 373 372 372 ASN ASN A . n 
A 1 374 ILE 374 373 373 ILE ILE A . n 
A 1 375 SER 375 374 374 SER SER A . n 
A 1 376 ARG 376 375 375 ARG ARG A . n 
A 1 377 PRO 377 376 376 PRO PRO A . n 
A 1 378 ILE 378 377 377 ILE ILE A . n 
A 1 379 VAL 379 378 ?   ?   ?   A . n 
A 1 380 SER 380 379 ?   ?   ?   A . n 
A 1 381 SER 381 380 ?   ?   ?   A . n 
A 1 382 HIS 382 381 ?   ?   ?   A . n 
A 1 383 LYS 383 382 ?   ?   ?   A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ASP 2   2   2   ASP ASP B . n 
B 2 3   VAL 3   3   3   VAL VAL B . n 
B 2 4   PHE 4   4   4   PHE PHE B . n 
B 2 5   LEU 5   5   5   LEU LEU B . n 
B 2 6   MET 6   6   6   MET MET B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   ARG 8   8   8   ARG ARG B . n 
B 2 9   ARG 9   9   9   ARG ARG B . n 
B 2 10  HIS 10  10  10  HIS HIS B . n 
B 2 11  LYS 11  11  11  LYS LYS B . n 
B 2 12  THR 12  12  12  THR THR B . n 
B 2 13  THR 13  13  13  THR THR B . n 
B 2 14  ILE 14  14  14  ILE ILE B . n 
B 2 15  PHE 15  15  15  PHE PHE B . n 
B 2 16  THR 16  16  16  THR THR B . n 
B 2 17  ASP 17  17  17  ASP ASP B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  GLU 20  20  20  GLU GLU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  SER 22  22  22  SER SER B . n 
B 2 23  THR 23  23  23  THR THR B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  PHE 25  25  25  PHE PHE B . n 
B 2 26  GLU 26  26  26  GLU GLU B . n 
B 2 27  LEU 27  27  27  LEU LEU B . n 
B 2 28  LYS 28  28  28  LYS LYS B . n 
B 2 29  ARG 29  29  29  ARG ARG B . n 
B 2 30  ILE 30  30  30  ILE ILE B . n 
B 2 31  VAL 31  31  31  VAL VAL B . n 
B 2 32  GLU 32  32  32  GLU GLU B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  ILE 34  34  34  ILE ILE B . n 
B 2 35  LEU 35  35  35  LEU LEU B . n 
B 2 36  LYS 36  36  36  LYS LYS B . n 
B 2 37  ARG 37  37  37  ARG ARG B . n 
B 2 38  PRO 38  38  38  PRO PRO B . n 
B 2 39  PRO 39  39  39  PRO PRO B . n 
B 2 40  ASP 40  40  40  ASP ASP B . n 
B 2 41  GLU 41  41  41  GLU GLU B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  ARG 43  43  43  ARG ARG B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  TYR 45  45  45  TYR TYR B . n 
B 2 46  LYS 46  46  46  LYS LYS B . n 
B 2 47  ASP 47  47  47  ASP ASP B . n 
B 2 48  ASP 48  48  48  ASP ASP B . n 
B 2 49  GLN 49  49  49  GLN GLN B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  LEU 51  51  51  LEU LEU B . n 
B 2 52  ASP 52  52  52  ASP ASP B . n 
B 2 53  ASP 53  53  53  ASP ASP B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  LYS 55  55  55  LYS LYS B . n 
B 2 56  THR 56  56  56  THR THR B . n 
B 2 57  LEU 57  57  57  LEU LEU B . n 
B 2 58  GLY 58  58  58  GLY GLY B . n 
B 2 59  GLU 59  59  59  GLU GLU B . n 
B 2 60  CYS 60  60  60  CYS CYS B . n 
B 2 61  GLY 61  61  61  GLY GLY B . n 
B 2 62  PHE 62  62  62  PHE PHE B . n 
B 2 63  THR 63  63  63  THR THR B . n 
B 2 64  SER 64  64  64  SER SER B . n 
B 2 65  GLN 65  65  65  GLN GLN B . n 
B 2 66  THR 66  66  66  THR THR B . n 
B 2 67  ALA 67  67  67  ALA ALA B . n 
B 2 68  ARG 68  68  68  ARG ARG B . n 
B 2 69  PRO 69  69  69  PRO PRO B . n 
B 2 70  GLN 70  70  70  GLN GLN B . n 
B 2 71  ALA 71  71  71  ALA ALA B . n 
B 2 72  PRO 72  72  72  PRO PRO B . n 
B 2 73  ALA 73  73  73  ALA ALA B . n 
B 2 74  THR 74  74  74  THR THR B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  GLY 76  76  76  GLY GLY B . n 
B 2 77  LEU 77  77  77  LEU LEU B . n 
B 2 78  ALA 78  78  78  ALA ALA B . n 
B 2 79  PHE 79  79  79  PHE PHE B . n 
B 2 80  ARG 80  80  80  ARG ARG B . n 
B 2 81  ALA 81  81  81  ALA ALA B . n 
B 2 82  ASP 82  82  82  ASP ASP B . n 
B 2 83  ASP 83  83  83  ASP ASP B . n 
B 2 84  THR 84  84  84  THR THR B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  GLU 86  86  86  GLU GLU B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  CYS 89  89  89  CYS CYS B . n 
B 2 90  ILE 90  90  90  ILE ILE B . n 
B 2 91  GLU 91  91  91  GLU GLU B . n 
B 2 92  PRO 92  92  92  PRO PRO B . n 
B 2 93  PHE 93  93  93  PHE PHE B . n 
B 2 94  SER 94  94  94  SER SER B . n 
B 2 95  SER 95  95  95  SER SER B . n 
B 2 96  PRO 96  96  96  PRO PRO B . n 
B 2 97  PRO 97  97  97  PRO PRO B . n 
B 2 98  GLU 98  98  ?   ?   ?   B . n 
B 2 99  LEU 99  99  ?   ?   ?   B . n 
B 2 100 PRO 100 100 ?   ?   ?   B . n 
B 2 101 ASP 101 101 ?   ?   ?   B . n 
B 2 102 VAL 102 102 ?   ?   ?   B . n 
B 2 103 MET 103 103 ?   ?   ?   B . n 
B 2 104 LYS 104 104 ?   ?   ?   B . n 
C 3 1   MET 1   -8  ?   ?   ?   C . n 
C 3 2   SER 2   -7  ?   ?   ?   C . n 
C 3 3   TYR 3   -6  ?   ?   ?   C . n 
C 3 4   TYR 4   -5  ?   ?   ?   C . n 
C 3 5   HIS 5   -4  ?   ?   ?   C . n 
C 3 6   HIS 6   -3  ?   ?   ?   C . n 
C 3 7   HIS 7   -2  ?   ?   ?   C . n 
C 3 8   HIS 8   -1  ?   ?   ?   C . n 
C 3 9   HIS 9   0   ?   ?   ?   C . n 
C 3 10  HIS 10  1   ?   ?   ?   C . n 
C 3 11  ASP 11  2   ?   ?   ?   C . n 
C 3 12  TYR 12  3   ?   ?   ?   C . n 
C 3 13  ASP 13  4   ?   ?   ?   C . n 
C 3 14  ILE 14  5   ?   ?   ?   C . n 
C 3 15  PRO 15  6   ?   ?   ?   C . n 
C 3 16  THR 16  7   ?   ?   ?   C . n 
C 3 17  THR 17  8   ?   ?   ?   C . n 
C 3 18  GLU 18  9   ?   ?   ?   C . n 
C 3 19  ASN 19  10  ?   ?   ?   C . n 
C 3 20  LEU 20  11  ?   ?   ?   C . n 
C 3 21  TYR 21  12  ?   ?   ?   C . n 
C 3 22  GLY 22  13  ?   ?   ?   C . n 
C 3 23  GLN 23  14  ?   ?   ?   C . n 
C 3 24  GLY 24  15  ?   ?   ?   C . n 
C 3 25  ALA 25  16  ?   ?   ?   C . n 
C 3 26  MET 26  17  17  MET MET C . n 
C 3 27  TYR 27  18  18  TYR TYR C . n 
C 3 28  VAL 28  19  19  VAL VAL C . n 
C 3 29  LYS 29  20  20  LYS LYS C . n 
C 3 30  LEU 30  21  21  LEU LEU C . n 
C 3 31  ILE 31  22  22  ILE ILE C . n 
C 3 32  SER 32  23  23  SER SER C . n 
C 3 33  SER 33  24  24  SER SER C . n 
C 3 34  ASP 34  25  25  ASP ASP C . n 
C 3 35  GLY 35  26  26  GLY GLY C . n 
C 3 36  HIS 36  27  27  HIS HIS C . n 
C 3 37  GLU 37  28  28  GLU GLU C . n 
C 3 38  PHE 38  29  29  PHE PHE C . n 
C 3 39  ILE 39  30  30  ILE ILE C . n 
C 3 40  VAL 40  31  31  VAL VAL C . n 
C 3 41  LYS 41  32  32  LYS LYS C . n 
C 3 42  ARG 42  33  33  ARG ARG C . n 
C 3 43  GLU 43  34  34  GLU GLU C . n 
C 3 44  HIS 44  35  35  HIS HIS C . n 
C 3 45  ALA 45  36  36  ALA ALA C . n 
C 3 46  LEU 46  37  37  LEU LEU C . n 
C 3 47  THR 47  38  38  THR THR C . n 
C 3 48  SER 48  39  39  SER SER C . n 
C 3 49  GLY 49  40  40  GLY GLY C . n 
C 3 50  THR 50  41  41  THR THR C . n 
C 3 51  ILE 51  42  42  ILE ILE C . n 
C 3 52  LYS 52  43  43  LYS LYS C . n 
C 3 53  ALA 53  44  44  ALA ALA C . n 
C 3 54  MET 54  45  45  MET MET C . n 
C 3 55  LEU 55  46  46  LEU LEU C . n 
C 3 56  SER 56  47  47  SER SER C . n 
C 3 57  GLY 57  48  48  GLY GLY C . n 
C 3 58  PRO 58  49  49  PRO PRO C . n 
C 3 59  GLY 59  50  50  GLY GLY C . n 
C 3 60  GLN 60  51  ?   ?   ?   C . n 
C 3 61  PHE 61  52  ?   ?   ?   C . n 
C 3 62  ALA 62  53  ?   ?   ?   C . n 
C 3 63  GLU 63  54  ?   ?   ?   C . n 
C 3 64  ASN 64  55  ?   ?   ?   C . n 
C 3 65  GLU 65  56  ?   ?   ?   C . n 
C 3 66  THR 66  57  ?   ?   ?   C . n 
C 3 67  ASN 67  58  58  ASN ASN C . n 
C 3 68  GLU 68  59  59  GLU GLU C . n 
C 3 69  VAL 69  60  60  VAL VAL C . n 
C 3 70  ASN 70  61  61  ASN ASN C . n 
C 3 71  PHE 71  62  62  PHE PHE C . n 
C 3 72  ARG 72  63  63  ARG ARG C . n 
C 3 73  GLU 73  64  64  GLU GLU C . n 
C 3 74  ILE 74  65  65  ILE ILE C . n 
C 3 75  PRO 75  66  66  PRO PRO C . n 
C 3 76  SER 76  67  67  SER SER C . n 
C 3 77  HIS 77  68  68  HIS HIS C . n 
C 3 78  VAL 78  69  69  VAL VAL C . n 
C 3 79  LEU 79  70  70  LEU LEU C . n 
C 3 80  SER 80  71  71  SER SER C . n 
C 3 81  LYS 81  72  72  LYS LYS C . n 
C 3 82  VAL 82  73  73  VAL VAL C . n 
C 3 83  CYS 83  74  74  CYS CYS C . n 
C 3 84  MET 84  75  75  MET MET C . n 
C 3 85  TYR 85  76  76  TYR TYR C . n 
C 3 86  PHE 86  77  77  PHE PHE C . n 
C 3 87  THR 87  78  78  THR THR C . n 
C 3 88  TYR 88  79  79  TYR TYR C . n 
C 3 89  LYS 89  80  80  LYS LYS C . n 
C 3 90  VAL 90  81  81  VAL VAL C . n 
C 3 91  ARG 91  82  82  ARG ARG C . n 
C 3 92  TYR 92  83  83  TYR TYR C . n 
C 3 93  THR 93  84  84  THR THR C . n 
C 3 94  ASN 94  85  85  ASN ASN C . n 
C 3 95  SER 95  86  86  SER SER C . n 
C 3 96  SER 96  87  87  SER SER C . n 
C 3 97  THR 97  88  88  THR THR C . n 
C 3 98  GLU 98  89  89  GLU GLU C . n 
C 3 99  ILE 99  90  90  ILE ILE C . n 
C 3 100 PRO 100 91  91  PRO PRO C . n 
C 3 101 GLU 101 92  92  GLU GLU C . n 
C 3 102 PHE 102 93  93  PHE PHE C . n 
C 3 103 PRO 103 94  94  PRO PRO C . n 
C 3 104 ILE 104 95  95  ILE ILE C . n 
C 3 105 ALA 105 96  96  ALA ALA C . n 
C 3 106 PRO 106 97  97  PRO PRO C . n 
C 3 107 GLU 107 98  98  GLU GLU C . n 
C 3 108 ILE 108 99  99  ILE ILE C . n 
C 3 109 ALA 109 100 100 ALA ALA C . n 
C 3 110 LEU 110 101 101 LEU LEU C . n 
C 3 111 GLU 111 102 102 GLU GLU C . n 
C 3 112 LEU 112 103 103 LEU LEU C . n 
C 3 113 LEU 113 104 104 LEU LEU C . n 
C 3 114 MET 114 105 105 MET MET C . n 
C 3 115 ALA 115 106 106 ALA ALA C . n 
C 3 116 ALA 116 107 107 ALA ALA C . n 
C 3 117 ASN 117 108 108 ASN ASN C . n 
C 3 118 PHE 118 109 109 PHE PHE C . n 
C 3 119 LEU 119 110 110 LEU LEU C . n 
C 3 120 ASP 120 111 111 ASP ASP C . n 
C 3 121 CYS 121 112 112 CYS CYS C . n 
D 4 1   MET 1   1   1   MET MET D . n 
D 4 2   GLN 2   2   2   GLN GLN D . n 
D 4 3   ILE 3   3   3   ILE ILE D . n 
D 4 4   PHE 4   4   4   PHE PHE D . n 
D 4 5   VAL 5   5   5   VAL VAL D . n 
D 4 6   LYS 6   6   6   LYS LYS D . n 
D 4 7   THR 7   7   7   THR THR D . n 
D 4 8   LEU 8   8   8   LEU LEU D . n 
D 4 9   THR 9   9   9   THR THR D . n 
D 4 10  GLY 10  10  10  GLY GLY D . n 
D 4 11  LYS 11  11  11  LYS LYS D . n 
D 4 12  THR 12  12  12  THR THR D . n 
D 4 13  ILE 13  13  13  ILE ILE D . n 
D 4 14  THR 14  14  14  THR THR D . n 
D 4 15  LEU 15  15  15  LEU LEU D . n 
D 4 16  GLU 16  16  16  GLU GLU D . n 
D 4 17  VAL 17  17  17  VAL VAL D . n 
D 4 18  GLU 18  18  18  GLU GLU D . n 
D 4 19  PRO 19  19  19  PRO PRO D . n 
D 4 20  SER 20  20  20  SER SER D . n 
D 4 21  ASP 21  21  21  ASP ASP D . n 
D 4 22  THR 22  22  22  THR THR D . n 
D 4 23  ILE 23  23  23  ILE ILE D . n 
D 4 24  GLU 24  24  24  GLU GLU D . n 
D 4 25  ASN 25  25  25  ASN ASN D . n 
D 4 26  VAL 26  26  26  VAL VAL D . n 
D 4 27  LYS 27  27  27  LYS LYS D . n 
D 4 28  ALA 28  28  28  ALA ALA D . n 
D 4 29  LYS 29  29  29  LYS LYS D . n 
D 4 30  ILE 30  30  30  ILE ILE D . n 
D 4 31  GLN 31  31  31  GLN GLN D . n 
D 4 32  ASP 32  32  32  ASP ASP D . n 
D 4 33  LYS 33  33  33  LYS LYS D . n 
D 4 34  GLU 34  34  34  GLU GLU D . n 
D 4 35  GLY 35  35  35  GLY GLY D . n 
D 4 36  ILE 36  36  36  ILE ILE D . n 
D 4 37  PRO 37  37  37  PRO PRO D . n 
D 4 38  PRO 38  38  38  PRO PRO D . n 
D 4 39  ASP 39  39  39  ASP ASP D . n 
D 4 40  GLN 40  40  40  GLN GLN D . n 
D 4 41  GLN 41  41  41  GLN GLN D . n 
D 4 42  ARG 42  42  42  ARG ARG D . n 
D 4 43  LEU 43  43  43  LEU LEU D . n 
D 4 44  ILE 44  44  44  ILE ILE D . n 
D 4 45  PHE 45  45  45  PHE PHE D . n 
D 4 46  ALA 46  46  46  ALA ALA D . n 
D 4 47  GLY 47  47  47  GLY GLY D . n 
D 4 48  LYS 48  48  48  LYS LYS D . n 
D 4 49  GLN 49  49  49  GLN GLN D . n 
D 4 50  LEU 50  50  50  LEU LEU D . n 
D 4 51  GLU 51  51  51  GLU GLU D . n 
D 4 52  ASP 52  52  52  ASP ASP D . n 
D 4 53  GLY 53  53  53  GLY GLY D . n 
D 4 54  ARG 54  54  54  ARG ARG D . n 
D 4 55  THR 55  55  55  THR THR D . n 
D 4 56  LEU 56  56  56  LEU LEU D . n 
D 4 57  SER 57  57  57  SER SER D . n 
D 4 58  ASP 58  58  58  ASP ASP D . n 
D 4 59  TYR 59  59  59  TYR TYR D . n 
D 4 60  ASN 60  60  60  ASN ASN D . n 
D 4 61  ILE 61  61  61  ILE ILE D . n 
D 4 62  GLN 62  62  62  GLN GLN D . n 
D 4 63  LYS 63  63  63  LYS LYS D . n 
D 4 64  GLU 64  64  64  GLU GLU D . n 
D 4 65  SER 65  65  65  SER SER D . n 
D 4 66  THR 66  66  66  THR THR D . n 
D 4 67  LEU 67  67  67  LEU LEU D . n 
D 4 68  HIS 68  68  68  HIS HIS D . n 
D 4 69  LEU 69  69  69  LEU LEU D . n 
D 4 70  VAL 70  70  70  VAL VAL D . n 
D 4 71  LEU 71  71  71  LEU LEU D . n 
D 4 72  ARG 72  72  72  ARG ARG D . n 
D 4 73  LEU 73  73  73  LEU LEU D . n 
D 4 74  ARG 74  74  74  ARG ARG D . n 
D 4 75  ARG 75  75  75  ARG ARG D . n 
D 4 76  GLY 76  76  76  GLY GLY D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ACE ? ? ACE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
E 5 GOL 1   401 1   GOL GOL A . 
F 5 GOL 1   201 2   GOL GOL B . 
G 6 HOH 1   501 194 HOH HOH A . 
G 6 HOH 2   502 50  HOH HOH A . 
G 6 HOH 3   503 311 HOH HOH A . 
G 6 HOH 4   504 176 HOH HOH A . 
G 6 HOH 5   505 165 HOH HOH A . 
G 6 HOH 6   506 286 HOH HOH A . 
G 6 HOH 7   507 58  HOH HOH A . 
G 6 HOH 8   508 19  HOH HOH A . 
G 6 HOH 9   509 266 HOH HOH A . 
G 6 HOH 10  510 276 HOH HOH A . 
G 6 HOH 11  511 36  HOH HOH A . 
G 6 HOH 12  512 116 HOH HOH A . 
G 6 HOH 13  513 120 HOH HOH A . 
G 6 HOH 14  514 150 HOH HOH A . 
G 6 HOH 15  515 160 HOH HOH A . 
G 6 HOH 16  516 117 HOH HOH A . 
G 6 HOH 17  517 63  HOH HOH A . 
G 6 HOH 18  518 315 HOH HOH A . 
G 6 HOH 19  519 254 HOH HOH A . 
G 6 HOH 20  520 7   HOH HOH A . 
G 6 HOH 21  521 115 HOH HOH A . 
G 6 HOH 22  522 54  HOH HOH A . 
G 6 HOH 23  523 40  HOH HOH A . 
G 6 HOH 24  524 13  HOH HOH A . 
G 6 HOH 25  525 162 HOH HOH A . 
G 6 HOH 26  526 198 HOH HOH A . 
G 6 HOH 27  527 128 HOH HOH A . 
G 6 HOH 28  528 30  HOH HOH A . 
G 6 HOH 29  529 103 HOH HOH A . 
G 6 HOH 30  530 92  HOH HOH A . 
G 6 HOH 31  531 268 HOH HOH A . 
G 6 HOH 32  532 132 HOH HOH A . 
G 6 HOH 33  533 11  HOH HOH A . 
G 6 HOH 34  534 245 HOH HOH A . 
G 6 HOH 35  535 284 HOH HOH A . 
G 6 HOH 36  536 43  HOH HOH A . 
G 6 HOH 37  537 154 HOH HOH A . 
G 6 HOH 38  538 4   HOH HOH A . 
G 6 HOH 39  539 143 HOH HOH A . 
G 6 HOH 40  540 97  HOH HOH A . 
G 6 HOH 41  541 289 HOH HOH A . 
G 6 HOH 42  542 240 HOH HOH A . 
G 6 HOH 43  543 9   HOH HOH A . 
G 6 HOH 44  544 106 HOH HOH A . 
G 6 HOH 45  545 214 HOH HOH A . 
G 6 HOH 46  546 85  HOH HOH A . 
G 6 HOH 47  547 303 HOH HOH A . 
G 6 HOH 48  548 87  HOH HOH A . 
G 6 HOH 49  549 278 HOH HOH A . 
G 6 HOH 50  550 39  HOH HOH A . 
G 6 HOH 51  551 139 HOH HOH A . 
G 6 HOH 52  552 89  HOH HOH A . 
G 6 HOH 53  553 319 HOH HOH A . 
G 6 HOH 54  554 152 HOH HOH A . 
G 6 HOH 55  555 69  HOH HOH A . 
G 6 HOH 56  556 95  HOH HOH A . 
G 6 HOH 57  557 93  HOH HOH A . 
G 6 HOH 58  558 17  HOH HOH A . 
G 6 HOH 59  559 49  HOH HOH A . 
G 6 HOH 60  560 26  HOH HOH A . 
G 6 HOH 61  561 210 HOH HOH A . 
G 6 HOH 62  562 67  HOH HOH A . 
G 6 HOH 63  563 21  HOH HOH A . 
G 6 HOH 64  564 84  HOH HOH A . 
G 6 HOH 65  565 142 HOH HOH A . 
G 6 HOH 66  566 135 HOH HOH A . 
G 6 HOH 67  567 81  HOH HOH A . 
G 6 HOH 68  568 90  HOH HOH A . 
G 6 HOH 69  569 56  HOH HOH A . 
G 6 HOH 70  570 51  HOH HOH A . 
G 6 HOH 71  571 137 HOH HOH A . 
G 6 HOH 72  572 25  HOH HOH A . 
G 6 HOH 73  573 211 HOH HOH A . 
G 6 HOH 74  574 195 HOH HOH A . 
G 6 HOH 75  575 313 HOH HOH A . 
G 6 HOH 76  576 126 HOH HOH A . 
G 6 HOH 77  577 72  HOH HOH A . 
G 6 HOH 78  578 149 HOH HOH A . 
G 6 HOH 79  579 119 HOH HOH A . 
G 6 HOH 80  580 23  HOH HOH A . 
G 6 HOH 81  581 59  HOH HOH A . 
G 6 HOH 82  582 5   HOH HOH A . 
G 6 HOH 83  583 8   HOH HOH A . 
G 6 HOH 84  584 185 HOH HOH A . 
G 6 HOH 85  585 100 HOH HOH A . 
G 6 HOH 86  586 362 HOH HOH A . 
G 6 HOH 87  587 45  HOH HOH A . 
G 6 HOH 88  588 86  HOH HOH A . 
G 6 HOH 89  589 208 HOH HOH A . 
G 6 HOH 90  590 186 HOH HOH A . 
G 6 HOH 91  591 173 HOH HOH A . 
G 6 HOH 92  592 188 HOH HOH A . 
G 6 HOH 93  593 203 HOH HOH A . 
G 6 HOH 94  594 44  HOH HOH A . 
G 6 HOH 95  595 24  HOH HOH A . 
G 6 HOH 96  596 78  HOH HOH A . 
G 6 HOH 97  597 16  HOH HOH A . 
G 6 HOH 98  598 68  HOH HOH A . 
G 6 HOH 99  599 323 HOH HOH A . 
G 6 HOH 100 600 83  HOH HOH A . 
G 6 HOH 101 601 223 HOH HOH A . 
G 6 HOH 102 602 181 HOH HOH A . 
G 6 HOH 103 603 333 HOH HOH A . 
G 6 HOH 104 604 174 HOH HOH A . 
G 6 HOH 105 605 10  HOH HOH A . 
G 6 HOH 106 606 47  HOH HOH A . 
G 6 HOH 107 607 360 HOH HOH A . 
G 6 HOH 108 608 250 HOH HOH A . 
G 6 HOH 109 609 182 HOH HOH A . 
G 6 HOH 110 610 321 HOH HOH A . 
G 6 HOH 111 611 131 HOH HOH A . 
G 6 HOH 112 612 193 HOH HOH A . 
G 6 HOH 113 613 159 HOH HOH A . 
G 6 HOH 114 614 33  HOH HOH A . 
G 6 HOH 115 615 199 HOH HOH A . 
G 6 HOH 116 616 76  HOH HOH A . 
G 6 HOH 117 617 38  HOH HOH A . 
G 6 HOH 118 618 156 HOH HOH A . 
G 6 HOH 119 619 290 HOH HOH A . 
G 6 HOH 120 620 6   HOH HOH A . 
G 6 HOH 121 621 234 HOH HOH A . 
G 6 HOH 122 622 262 HOH HOH A . 
G 6 HOH 123 623 121 HOH HOH A . 
G 6 HOH 124 624 167 HOH HOH A . 
G 6 HOH 125 625 293 HOH HOH A . 
G 6 HOH 126 626 28  HOH HOH A . 
G 6 HOH 127 627 261 HOH HOH A . 
G 6 HOH 128 628 98  HOH HOH A . 
G 6 HOH 129 629 138 HOH HOH A . 
G 6 HOH 130 630 104 HOH HOH A . 
G 6 HOH 131 631 158 HOH HOH A . 
G 6 HOH 132 632 220 HOH HOH A . 
G 6 HOH 133 633 79  HOH HOH A . 
G 6 HOH 134 634 122 HOH HOH A . 
G 6 HOH 135 635 201 HOH HOH A . 
G 6 HOH 136 636 180 HOH HOH A . 
G 6 HOH 137 637 248 HOH HOH A . 
G 6 HOH 138 638 37  HOH HOH A . 
G 6 HOH 139 639 96  HOH HOH A . 
G 6 HOH 140 640 256 HOH HOH A . 
G 6 HOH 141 641 275 HOH HOH A . 
G 6 HOH 142 642 12  HOH HOH A . 
G 6 HOH 143 643 314 HOH HOH A . 
G 6 HOH 144 644 123 HOH HOH A . 
G 6 HOH 145 645 42  HOH HOH A . 
G 6 HOH 146 646 22  HOH HOH A . 
G 6 HOH 147 647 35  HOH HOH A . 
G 6 HOH 148 648 166 HOH HOH A . 
G 6 HOH 149 649 124 HOH HOH A . 
G 6 HOH 150 650 171 HOH HOH A . 
G 6 HOH 151 651 239 HOH HOH A . 
G 6 HOH 152 652 237 HOH HOH A . 
G 6 HOH 153 653 279 HOH HOH A . 
G 6 HOH 154 654 257 HOH HOH A . 
G 6 HOH 155 655 27  HOH HOH A . 
G 6 HOH 156 656 207 HOH HOH A . 
G 6 HOH 157 657 217 HOH HOH A . 
G 6 HOH 158 658 179 HOH HOH A . 
G 6 HOH 159 659 163 HOH HOH A . 
G 6 HOH 160 660 219 HOH HOH A . 
G 6 HOH 161 661 153 HOH HOH A . 
G 6 HOH 162 662 270 HOH HOH A . 
G 6 HOH 163 663 222 HOH HOH A . 
G 6 HOH 164 664 287 HOH HOH A . 
G 6 HOH 165 665 46  HOH HOH A . 
G 6 HOH 166 666 110 HOH HOH A . 
G 6 HOH 167 667 80  HOH HOH A . 
G 6 HOH 168 668 342 HOH HOH A . 
G 6 HOH 169 669 151 HOH HOH A . 
G 6 HOH 170 670 228 HOH HOH A . 
G 6 HOH 171 671 18  HOH HOH A . 
G 6 HOH 172 672 242 HOH HOH A . 
G 6 HOH 173 673 177 HOH HOH A . 
G 6 HOH 174 674 322 HOH HOH A . 
G 6 HOH 175 675 260 HOH HOH A . 
G 6 HOH 176 676 125 HOH HOH A . 
G 6 HOH 177 677 190 HOH HOH A . 
G 6 HOH 178 678 175 HOH HOH A . 
G 6 HOH 179 679 14  HOH HOH A . 
G 6 HOH 180 680 109 HOH HOH A . 
G 6 HOH 181 681 57  HOH HOH A . 
G 6 HOH 182 682 107 HOH HOH A . 
G 6 HOH 183 683 118 HOH HOH A . 
G 6 HOH 184 684 253 HOH HOH A . 
G 6 HOH 185 685 241 HOH HOH A . 
G 6 HOH 186 686 247 HOH HOH A . 
G 6 HOH 187 687 233 HOH HOH A . 
G 6 HOH 188 688 133 HOH HOH A . 
G 6 HOH 189 689 130 HOH HOH A . 
G 6 HOH 190 690 178 HOH HOH A . 
G 6 HOH 191 691 246 HOH HOH A . 
G 6 HOH 192 692 77  HOH HOH A . 
G 6 HOH 193 693 189 HOH HOH A . 
G 6 HOH 194 694 20  HOH HOH A . 
G 6 HOH 195 695 53  HOH HOH A . 
G 6 HOH 196 696 191 HOH HOH A . 
G 6 HOH 197 697 1   HOH HOH A . 
G 6 HOH 198 698 55  HOH HOH A . 
G 6 HOH 199 699 255 HOH HOH A . 
G 6 HOH 200 700 99  HOH HOH A . 
G 6 HOH 201 701 60  HOH HOH A . 
G 6 HOH 202 702 308 HOH HOH A . 
G 6 HOH 203 703 205 HOH HOH A . 
G 6 HOH 204 704 213 HOH HOH A . 
G 6 HOH 205 705 70  HOH HOH A . 
G 6 HOH 206 706 88  HOH HOH A . 
G 6 HOH 207 707 221 HOH HOH A . 
G 6 HOH 208 708 226 HOH HOH A . 
G 6 HOH 209 709 316 HOH HOH A . 
G 6 HOH 210 710 339 HOH HOH A . 
G 6 HOH 211 711 358 HOH HOH A . 
G 6 HOH 212 712 206 HOH HOH A . 
G 6 HOH 213 713 307 HOH HOH A . 
G 6 HOH 214 714 161 HOH HOH A . 
G 6 HOH 215 715 325 HOH HOH A . 
G 6 HOH 216 716 183 HOH HOH A . 
G 6 HOH 217 717 2   HOH HOH A . 
G 6 HOH 218 718 336 HOH HOH A . 
G 6 HOH 219 719 112 HOH HOH A . 
G 6 HOH 220 720 281 HOH HOH A . 
G 6 HOH 221 721 243 HOH HOH A . 
G 6 HOH 222 722 355 HOH HOH A . 
G 6 HOH 223 723 285 HOH HOH A . 
G 6 HOH 224 724 172 HOH HOH A . 
G 6 HOH 225 725 168 HOH HOH A . 
G 6 HOH 226 726 271 HOH HOH A . 
G 6 HOH 227 727 235 HOH HOH A . 
G 6 HOH 228 728 197 HOH HOH A . 
G 6 HOH 229 729 212 HOH HOH A . 
G 6 HOH 230 730 225 HOH HOH A . 
G 6 HOH 231 731 331 HOH HOH A . 
G 6 HOH 232 732 273 HOH HOH A . 
G 6 HOH 233 733 349 HOH HOH A . 
G 6 HOH 234 734 361 HOH HOH A . 
G 6 HOH 235 735 282 HOH HOH A . 
G 6 HOH 236 736 351 HOH HOH A . 
G 6 HOH 237 737 346 HOH HOH A . 
G 6 HOH 238 738 148 HOH HOH A . 
G 6 HOH 239 739 296 HOH HOH A . 
G 6 HOH 240 740 230 HOH HOH A . 
G 6 HOH 241 741 218 HOH HOH A . 
G 6 HOH 242 742 209 HOH HOH A . 
G 6 HOH 243 743 302 HOH HOH A . 
G 6 HOH 244 744 304 HOH HOH A . 
G 6 HOH 245 745 334 HOH HOH A . 
G 6 HOH 246 746 114 HOH HOH A . 
G 6 HOH 247 747 251 HOH HOH A . 
G 6 HOH 248 748 350 HOH HOH A . 
G 6 HOH 249 749 48  HOH HOH A . 
G 6 HOH 250 750 274 HOH HOH A . 
G 6 HOH 251 751 300 HOH HOH A . 
G 6 HOH 252 752 343 HOH HOH A . 
G 6 HOH 253 753 264 HOH HOH A . 
G 6 HOH 254 754 283 HOH HOH A . 
G 6 HOH 255 755 272 HOH HOH A . 
G 6 HOH 256 756 113 HOH HOH A . 
G 6 HOH 257 757 332 HOH HOH A . 
G 6 HOH 258 758 204 HOH HOH A . 
G 6 HOH 259 759 340 HOH HOH A . 
G 6 HOH 260 760 227 HOH HOH A . 
G 6 HOH 261 761 288 HOH HOH A . 
G 6 HOH 262 762 298 HOH HOH A . 
G 6 HOH 263 763 345 HOH HOH A . 
G 6 HOH 264 764 330 HOH HOH A . 
G 6 HOH 265 765 352 HOH HOH A . 
G 6 HOH 266 766 309 HOH HOH A . 
H 6 HOH 1   301 265 HOH HOH B . 
H 6 HOH 2   302 344 HOH HOH B . 
H 6 HOH 3   303 320 HOH HOH B . 
H 6 HOH 4   304 299 HOH HOH B . 
H 6 HOH 5   305 231 HOH HOH B . 
H 6 HOH 6   306 62  HOH HOH B . 
H 6 HOH 7   307 312 HOH HOH B . 
H 6 HOH 8   308 155 HOH HOH B . 
H 6 HOH 9   309 294 HOH HOH B . 
H 6 HOH 10  310 200 HOH HOH B . 
H 6 HOH 11  311 82  HOH HOH B . 
H 6 HOH 12  312 170 HOH HOH B . 
H 6 HOH 13  313 232 HOH HOH B . 
H 6 HOH 14  314 74  HOH HOH B . 
H 6 HOH 15  315 341 HOH HOH B . 
H 6 HOH 16  316 157 HOH HOH B . 
H 6 HOH 17  317 236 HOH HOH B . 
H 6 HOH 18  318 73  HOH HOH B . 
H 6 HOH 19  319 29  HOH HOH B . 
H 6 HOH 20  320 41  HOH HOH B . 
H 6 HOH 21  321 52  HOH HOH B . 
H 6 HOH 22  322 66  HOH HOH B . 
H 6 HOH 23  323 34  HOH HOH B . 
H 6 HOH 24  324 280 HOH HOH B . 
H 6 HOH 25  325 105 HOH HOH B . 
H 6 HOH 26  326 94  HOH HOH B . 
H 6 HOH 27  327 101 HOH HOH B . 
H 6 HOH 28  328 91  HOH HOH B . 
H 6 HOH 29  329 64  HOH HOH B . 
H 6 HOH 30  330 297 HOH HOH B . 
H 6 HOH 31  331 305 HOH HOH B . 
H 6 HOH 32  332 348 HOH HOH B . 
H 6 HOH 33  333 75  HOH HOH B . 
H 6 HOH 34  334 140 HOH HOH B . 
H 6 HOH 35  335 224 HOH HOH B . 
H 6 HOH 36  336 65  HOH HOH B . 
H 6 HOH 37  337 238 HOH HOH B . 
H 6 HOH 38  338 249 HOH HOH B . 
H 6 HOH 39  339 169 HOH HOH B . 
H 6 HOH 40  340 324 HOH HOH B . 
H 6 HOH 41  341 357 HOH HOH B . 
H 6 HOH 42  342 277 HOH HOH B . 
H 6 HOH 43  343 301 HOH HOH B . 
H 6 HOH 44  344 134 HOH HOH B . 
H 6 HOH 45  345 291 HOH HOH B . 
H 6 HOH 46  346 164 HOH HOH B . 
H 6 HOH 47  347 335 HOH HOH B . 
H 6 HOH 48  348 354 HOH HOH B . 
H 6 HOH 49  349 259 HOH HOH B . 
H 6 HOH 50  350 129 HOH HOH B . 
H 6 HOH 51  351 244 HOH HOH B . 
H 6 HOH 52  352 326 HOH HOH B . 
H 6 HOH 53  353 337 HOH HOH B . 
H 6 HOH 54  354 146 HOH HOH B . 
I 6 HOH 1   201 3   HOH HOH C . 
I 6 HOH 2   202 61  HOH HOH C . 
I 6 HOH 3   203 356 HOH HOH C . 
I 6 HOH 4   204 192 HOH HOH C . 
I 6 HOH 5   205 108 HOH HOH C . 
I 6 HOH 6   206 15  HOH HOH C . 
I 6 HOH 7   207 187 HOH HOH C . 
I 6 HOH 8   208 32  HOH HOH C . 
I 6 HOH 9   209 141 HOH HOH C . 
I 6 HOH 10  210 338 HOH HOH C . 
I 6 HOH 11  211 111 HOH HOH C . 
I 6 HOH 12  212 229 HOH HOH C . 
I 6 HOH 13  213 102 HOH HOH C . 
I 6 HOH 14  214 196 HOH HOH C . 
I 6 HOH 15  215 184 HOH HOH C . 
I 6 HOH 16  216 127 HOH HOH C . 
I 6 HOH 17  217 269 HOH HOH C . 
I 6 HOH 18  218 359 HOH HOH C . 
I 6 HOH 19  219 147 HOH HOH C . 
I 6 HOH 20  220 71  HOH HOH C . 
I 6 HOH 21  221 136 HOH HOH C . 
I 6 HOH 22  222 216 HOH HOH C . 
I 6 HOH 23  223 202 HOH HOH C . 
I 6 HOH 24  224 306 HOH HOH C . 
I 6 HOH 25  225 353 HOH HOH C . 
I 6 HOH 26  226 318 HOH HOH C . 
I 6 HOH 27  227 215 HOH HOH C . 
I 6 HOH 28  228 145 HOH HOH C . 
I 6 HOH 29  229 144 HOH HOH C . 
I 6 HOH 30  230 347 HOH HOH C . 
I 6 HOH 31  231 292 HOH HOH C . 
I 6 HOH 32  232 328 HOH HOH C . 
I 6 HOH 33  233 310 HOH HOH C . 
I 6 HOH 34  234 317 HOH HOH C . 
I 6 HOH 35  235 267 HOH HOH C . 
I 6 HOH 36  236 329 HOH HOH C . 
J 6 HOH 1   101 327 HOH HOH D . 
J 6 HOH 2   102 31  HOH HOH D . 
J 6 HOH 3   103 258 HOH HOH D . 
J 6 HOH 4   104 252 HOH HOH D . 
J 6 HOH 5   105 295 HOH HOH D . 
J 6 HOH 6   106 263 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 67  ? CG  ? A ARG 68  CG  
2  1 Y 1 A ARG 67  ? CD  ? A ARG 68  CD  
3  1 Y 1 A ARG 67  ? NE  ? A ARG 68  NE  
4  1 Y 1 A ARG 67  ? CZ  ? A ARG 68  CZ  
5  1 Y 1 A ARG 67  ? NH1 ? A ARG 68  NH1 
6  1 Y 1 A ARG 67  ? NH2 ? A ARG 68  NH2 
7  1 Y 1 A GLN 69  ? CG  ? A GLN 70  CG  
8  1 Y 1 A GLN 69  ? CD  ? A GLN 70  CD  
9  1 Y 1 A GLN 69  ? OE1 ? A GLN 70  OE1 
10 1 Y 1 A GLN 69  ? NE2 ? A GLN 70  NE2 
11 1 Y 1 A LYS 114 ? CG  ? A LYS 115 CG  
12 1 Y 1 A LYS 114 ? CD  ? A LYS 115 CD  
13 1 Y 1 A LYS 114 ? CE  ? A LYS 115 CE  
14 1 Y 1 A LYS 114 ? NZ  ? A LYS 115 NZ  
15 1 Y 1 A ARG 119 ? CG  ? A ARG 120 CG  
16 1 Y 1 A ARG 119 ? CD  ? A ARG 120 CD  
17 1 Y 1 A ARG 119 ? NE  ? A ARG 120 NE  
18 1 Y 1 A ARG 119 ? CZ  ? A ARG 120 CZ  
19 1 Y 1 A ARG 119 ? NH1 ? A ARG 120 NH1 
20 1 Y 1 A ARG 119 ? NH2 ? A ARG 120 NH2 
21 1 Y 1 A LYS 173 ? CG  ? A LYS 174 CG  
22 1 Y 1 A LYS 173 ? CD  ? A LYS 174 CD  
23 1 Y 1 A LYS 173 ? CE  ? A LYS 174 CE  
24 1 Y 1 A LYS 173 ? NZ  ? A LYS 174 NZ  
25 1 Y 1 A ARG 215 ? CG  ? A ARG 216 CG  
26 1 Y 1 A ARG 215 ? CD  ? A ARG 216 CD  
27 1 Y 1 A ARG 215 ? NE  ? A ARG 216 NE  
28 1 Y 1 A ARG 215 ? CZ  ? A ARG 216 CZ  
29 1 Y 1 A ARG 215 ? NH1 ? A ARG 216 NH1 
30 1 Y 1 A ARG 215 ? NH2 ? A ARG 216 NH2 
31 1 Y 1 B GLN 65  ? CG  ? B GLN 65  CG  
32 1 Y 1 B GLN 65  ? CD  ? B GLN 65  CD  
33 1 Y 1 B GLN 65  ? OE1 ? B GLN 65  OE1 
34 1 Y 1 B GLN 65  ? NE2 ? B GLN 65  NE2 
35 1 Y 1 C ARG 63  ? CG  ? C ARG 72  CG  
36 1 Y 1 C ARG 63  ? CD  ? C ARG 72  CD  
37 1 Y 1 C ARG 63  ? NE  ? C ARG 72  NE  
38 1 Y 1 C ARG 63  ? CZ  ? C ARG 72  CZ  
39 1 Y 1 C ARG 63  ? NH1 ? C ARG 72  NH1 
40 1 Y 1 C ARG 63  ? NH2 ? C ARG 72  NH2 
41 1 Y 1 D LYS 11  ? CG  ? D LYS 11  CG  
42 1 Y 1 D LYS 11  ? CD  ? D LYS 11  CD  
43 1 Y 1 D LYS 11  ? CE  ? D LYS 11  CE  
44 1 Y 1 D LYS 11  ? NZ  ? D LYS 11  NZ  
45 1 Y 1 D GLU 16  ? CG  ? D GLU 16  CG  
46 1 Y 1 D GLU 16  ? CD  ? D GLU 16  CD  
47 1 Y 1 D GLU 16  ? OE1 ? D GLU 16  OE1 
48 1 Y 1 D GLU 16  ? OE2 ? D GLU 16  OE2 
49 1 Y 1 D GLU 24  ? CG  ? D GLU 24  CG  
50 1 Y 1 D GLU 24  ? CD  ? D GLU 24  CD  
51 1 Y 1 D GLU 24  ? OE1 ? D GLU 24  OE1 
52 1 Y 1 D GLU 24  ? OE2 ? D GLU 24  OE2 
53 1 Y 1 D LYS 33  ? CG  ? D LYS 33  CG  
54 1 Y 1 D LYS 33  ? CD  ? D LYS 33  CD  
55 1 Y 1 D LYS 33  ? CE  ? D LYS 33  CE  
56 1 Y 1 D LYS 33  ? NZ  ? D LYS 33  NZ  
57 1 Y 1 D ARG 54  ? CG  ? D ARG 54  CG  
58 1 Y 1 D ARG 54  ? CD  ? D ARG 54  CD  
59 1 Y 1 D ARG 54  ? NE  ? D ARG 54  NE  
60 1 Y 1 D ARG 54  ? CZ  ? D ARG 54  CZ  
61 1 Y 1 D ARG 54  ? NH1 ? D ARG 54  NH1 
62 1 Y 1 D ARG 54  ? NH2 ? D ARG 54  NH2 
63 1 Y 1 D GLN 62  ? CG  ? D GLN 62  CG  
64 1 Y 1 D GLN 62  ? CD  ? D GLN 62  CD  
65 1 Y 1 D GLN 62  ? OE1 ? D GLN 62  OE1 
66 1 Y 1 D GLN 62  ? NE2 ? D GLN 62  NE2 
67 1 Y 1 D LYS 63  ? CG  ? D LYS 63  CG  
68 1 Y 1 D LYS 63  ? CD  ? D LYS 63  CD  
69 1 Y 1 D LYS 63  ? CE  ? D LYS 63  CE  
70 1 Y 1 D LYS 63  ? NZ  ? D LYS 63  NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21_5207 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D1Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.560 
_cell.length_a_esd                 ? 
_cell.length_b                     121.543 
_cell.length_b_esd                 ? 
_cell.length_c                     152.949 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9D1Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9D1Y 
_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             3.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10%PEG5KMME,
5% Tacsimate pH=7.0,
0.1M HEPES pH=7.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97741 
_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                        'ALS BEAMLINE 5.0.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97741 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D1Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               50.00 
_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                                     33218 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.485 
_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                                0.156 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   1.0 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.146 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
2.60 2.69  ? ? ? ? ? ? 3275 ? ? ? ? ? ? ? ? ? ? ? 8.7 0.433 ? ? 0.830 0.276 ? 1  1 0.849 0.958 ? 100.0 ? 0.782 ? ? ? ? ? ? ? ? ? 
2.69 2.80  ? ? ? ? ? ? 3257 ? ? ? ? ? ? ? ? ? ? ? 8.7 0.432 ? ? 0.624 0.208 ? 2  1 0.904 0.974 ? 100.0 ? 0.587 ? ? ? ? ? ? ? ? ? 
2.80 2.93  ? ? ? ? ? ? 3276 ? ? ? ? ? ? ? ? ? ? ? 8.6 0.442 ? ? 0.477 0.160 ? 3  1 0.939 0.984 ? 100.0 ? 0.449 ? ? ? ? ? ? ? ? ? 
2.93 3.08  ? ? ? ? ? ? 3310 ? ? ? ? ? ? ? ? ? ? ? 8.5 0.460 ? ? 0.356 0.121 ? 4  1 0.959 0.990 ? 100.0 ? 0.334 ? ? ? ? ? ? ? ? ? 
3.08 3.28  ? ? ? ? ? ? 3273 ? ? ? ? ? ? ? ? ? ? ? 8.0 0.484 ? ? 0.265 0.093 ? 5  1 0.971 0.993 ? 100.0 ? 0.248 ? ? ? ? ? ? ? ? ? 
3.28 3.53  ? ? ? ? ? ? 3311 ? ? ? ? ? ? ? ? ? ? ? 7.9 0.501 ? ? 0.182 0.064 ? 6  1 0.987 0.997 ? 100.0 ? 0.170 ? ? ? ? ? ? ? ? ? 
3.53 3.88  ? ? ? ? ? ? 3323 ? ? ? ? ? ? ? ? ? ? ? 8.4 0.503 ? ? 0.127 0.044 ? 7  1 0.993 0.998 ? 100.0 ? 0.120 ? ? ? ? ? ? ? ? ? 
3.88 4.45  ? ? ? ? ? ? 3342 ? ? ? ? ? ? ? ? ? ? ? 8.7 0.509 ? ? 0.083 0.028 ? 8  1 0.997 0.999 ? 100.0 ? 0.078 ? ? ? ? ? ? ? ? ? 
4.45 5.60  ? ? ? ? ? ? 3353 ? ? ? ? ? ? ? ? ? ? ? 8.3 0.490 ? ? 0.069 0.024 ? 9  1 0.998 0.999 ? 100.0 ? 0.065 ? ? ? ? ? ? ? ? ? 
5.60 50.00 ? ? ? ? ? ? 3498 ? ? ? ? ? ? ? ? ? ? ? 8.0 0.603 ? ? 0.066 0.023 ? 10 1 0.997 0.999 ? 100.0 ? 0.062 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9D1Y 
_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                            2.60 
_refine.ls_d_res_low                             45.85 
_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                     32925 
_refine.ls_number_reflns_R_free                  1589 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.14 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1701 
_refine.ls_R_factor_R_free                       0.2162 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1677 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.09 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        45.85 
_refine_hist.number_atoms_solvent             362 
_refine_hist.number_atoms_total               5336 
_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        4962 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_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  ? 5102 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.921  ? 6925 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.749 ? 1849 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 762  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 894  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.60 2.68  . . 131 2757 97.00  . . . . 0.1996 . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 2.68 2.78  . . 121 2811 98.00  . . . . 0.1994 . . . . . . . . . . . 0.3168 
'X-RAY DIFFRACTION' 2.78 2.89  . . 149 2791 98.00  . . . . 0.2166 . . . . . . . . . . . 0.2433 
'X-RAY DIFFRACTION' 2.89 3.02  . . 143 2820 99.00  . . . . 0.1983 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 3.02 3.18  . . 130 2840 99.00  . . . . 0.1944 . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 3.18 3.38  . . 133 2862 100.00 . . . . 0.1818 . . . . . . . . . . . 0.2557 
'X-RAY DIFFRACTION' 3.38 3.64  . . 136 2874 100.00 . . . . 0.1866 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 3.64 4.01  . . 137 2860 100.00 . . . . 0.1505 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 4.01 4.59  . . 147 2880 100.00 . . . . 0.1246 . . . . . . . . . . . 0.1421 
'X-RAY DIFFRACTION' 4.59 5.77  . . 205 2833 100.00 . . . . 0.1347 . . . . . . . . . . . 0.1881 
'X-RAY DIFFRACTION' 5.78 45.85 . . 157 3008 99.00  . . . . 0.1718 . . . . . . . . . . . 0.2159 
# 
_struct.entry_id                     9D1Y 
_struct.title                        'Structure of G75R Ubiquitin bound to KLHDC3-EloB/C' 
_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        9D1Y 
_struct_keywords.text            'KLHDC3, Ubiquitin, C-degron, Cullin-RING, E3, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP KLDC3_HUMAN Q9BQ90 ? 1 
;MLRWTVHLEGGPRRVNHAAVAVGHRVYSFGGYCSGEDYETLRQIDVHIFNAVSLRWTKLPPVKSAIRGQAPVVPYMRYGH
STVLIDDTVLLWGGRNDTEGACNVLYAFDVNTHKWFTPRVSGTVPGARDGHSACVLGKIMYIFGGYEQQADCFSNDIHKL
DTSTMTWTLICTKGSPARWRDFHSATMLGSHMYVFGGRADRFGPFHSNNEIYCNRIRVFDTRTEAWLDCPPTPVLPEGRR
SHSAFGYNGELYIFGGYNARLNRHFHDLWKFNPVSFTWKKIEPKGKGPCPRRRQCCCIVGDKIVLFGGTSPSPEEGLGDE
FDLIDHSDLHILDFSPSLKTLCKLAVIQYNLDQSCLPHDIRWELNAMTTNSNISRPIVSSHG
;
1  
2 UNP ELOB_HUMAN  Q15370 ? 2 
;MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFR
ADDTFEALCIEPFSSPPELPDVMK
;
1  
3 UNP ELOC_HUMAN  Q15369 ? 3 
;AMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPI
APEIALELLMAANFLDC
;
16 
4 UNP UBC_HUMAN   P0CG48 ? 4 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9D1Y A 2  ? 383 ? Q9BQ90 1  ? 382 ? 1  382 
2 2 9D1Y B 1  ? 104 ? Q15370 1  ? 104 ? 1  104 
3 3 9D1Y C 25 ? 121 ? Q15369 16 ? 112 ? 16 112 
4 4 9D1Y D 1  ? 76  ? P0CG48 1  ? 76  ? 1  76  
# 
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 9D1Y ACE A 1   ? UNP Q9BQ90 ?   ?   acetylation             0   1  
1 9D1Y LYS A 383 ? UNP Q9BQ90 GLY 382 conflict                382 2  
3 9D1Y MET C 1   ? UNP Q15369 ?   ?   'initiating methionine' -8  3  
3 9D1Y SER C 2   ? UNP Q15369 ?   ?   'expression tag'        -7  4  
3 9D1Y TYR C 3   ? UNP Q15369 ?   ?   'expression tag'        -6  5  
3 9D1Y TYR C 4   ? UNP Q15369 ?   ?   'expression tag'        -5  6  
3 9D1Y HIS C 5   ? UNP Q15369 ?   ?   'expression tag'        -4  7  
3 9D1Y HIS C 6   ? UNP Q15369 ?   ?   'expression tag'        -3  8  
3 9D1Y HIS C 7   ? UNP Q15369 ?   ?   'expression tag'        -2  9  
3 9D1Y HIS C 8   ? UNP Q15369 ?   ?   'expression tag'        -1  10 
3 9D1Y HIS C 9   ? UNP Q15369 ?   ?   'expression tag'        0   11 
3 9D1Y HIS C 10  ? UNP Q15369 ?   ?   'expression tag'        1   12 
3 9D1Y ASP C 11  ? UNP Q15369 ?   ?   'expression tag'        2   13 
3 9D1Y TYR C 12  ? UNP Q15369 ?   ?   'expression tag'        3   14 
3 9D1Y ASP C 13  ? UNP Q15369 ?   ?   'expression tag'        4   15 
3 9D1Y ILE C 14  ? UNP Q15369 ?   ?   'expression tag'        5   16 
3 9D1Y PRO C 15  ? UNP Q15369 ?   ?   'expression tag'        6   17 
3 9D1Y THR C 16  ? UNP Q15369 ?   ?   'expression tag'        7   18 
3 9D1Y THR C 17  ? UNP Q15369 ?   ?   'expression tag'        8   19 
3 9D1Y GLU C 18  ? UNP Q15369 ?   ?   'expression tag'        9   20 
3 9D1Y ASN C 19  ? UNP Q15369 ?   ?   'expression tag'        10  21 
3 9D1Y LEU C 20  ? UNP Q15369 ?   ?   'expression tag'        11  22 
3 9D1Y TYR C 21  ? UNP Q15369 ?   ?   'expression tag'        12  23 
3 9D1Y GLY C 22  ? UNP Q15369 ?   ?   'expression tag'        13  24 
3 9D1Y GLN C 23  ? UNP Q15369 ?   ?   'expression tag'        14  25 
3 9D1Y GLY C 24  ? UNP Q15369 ?   ?   'expression tag'        15  26 
4 9D1Y ARG D 75  ? UNP P0CG48 GLY 75  'engineered mutation'   75  27 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 338 ? TYR A 350 ? SER A 337 TYR A 349 1 ? 13 
HELX_P HELX_P2  AA2 PRO A 358 ? MET A 368 ? PRO A 357 MET A 367 1 ? 11 
HELX_P HELX_P3  AA3 THR B 23  ? LYS B 36  ? THR B 23  LYS B 36  1 ? 14 
HELX_P HELX_P4  AA4 PRO B 38  ? ASP B 40  ? PRO B 38  ASP B 40  5 ? 3  
HELX_P HELX_P5  AA5 THR B 63  ? ALA B 67  ? THR B 63  ALA B 67  5 ? 5  
HELX_P HELX_P6  AA6 ARG C 42  ? LEU C 46  ? ARG C 33  LEU C 37  1 ? 5  
HELX_P HELX_P7  AA7 SER C 48  ? SER C 56  ? SER C 39  SER C 47  1 ? 9  
HELX_P HELX_P8  AA8 PRO C 75  ? THR C 93  ? PRO C 66  THR C 84  1 ? 19 
HELX_P HELX_P9  AA9 ALA C 105 ? ASP C 120 ? ALA C 96  ASP C 111 1 ? 16 
HELX_P HELX_P10 AB1 THR D 22  ? GLY D 35  ? THR D 22  GLY D 35  1 ? 14 
HELX_P HELX_P11 AB2 PRO D 37  ? ASP D 39  ? PRO D 37  ASP D 39  5 ? 3  
HELX_P HELX_P12 AB3 LEU D 56  ? ASN D 60  ? LEU D 56  ASN D 60  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        both 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           ACE 
_struct_conn.ptnr1_label_seq_id            1 
_struct_conn.ptnr1_label_atom_id           C 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           MET 
_struct_conn.ptnr2_label_seq_id            2 
_struct_conn.ptnr2_label_atom_id           N 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            ACE 
_struct_conn.ptnr1_auth_seq_id             0 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            MET 
_struct_conn.ptnr2_auth_seq_id             1 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.499 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      ACE 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       1 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     MET 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      2 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       ACE 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        0 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      MET 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       1 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                MET 
_pdbx_modification_feature.ref_pcm_id                         4 
_pdbx_modification_feature.ref_comp_id                        ACE 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Terminal acetylation' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 8 ? 
AB2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? parallel      
AB1 4 5 ? anti-parallel 
AB1 5 6 ? parallel      
AB1 6 7 ? anti-parallel 
AB1 7 8 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 4   ? LEU A 9   ? ARG A 3   LEU A 8   
AA1 2 LEU A 330 ? ASP A 334 ? LEU A 329 ASP A 333 
AA1 3 LYS A 303 ? PHE A 307 ? LYS A 302 PHE A 306 
AA1 4 CYS A 296 ? VAL A 300 ? CYS A 295 VAL A 299 
AA2 1 ALA A 19  ? VAL A 23  ? ALA A 18  VAL A 22  
AA2 2 ARG A 26  ? PHE A 30  ? ARG A 25  PHE A 29  
AA2 3 VAL A 47  ? ASN A 51  ? VAL A 46  ASN A 50  
AA2 4 ARG A 56  ? LYS A 59  ? ARG A 55  LYS A 58  
AA3 1 SER A 82  ? ILE A 86  ? SER A 81  ILE A 85  
AA3 2 THR A 89  ? TRP A 93  ? THR A 88  TRP A 92  
AA3 3 TYR A 107 ? ASP A 110 ? TYR A 106 ASP A 109 
AA3 4 TRP A 116 ? PHE A 117 ? TRP A 115 PHE A 116 
AA4 1 SER A 122 ? GLY A 123 ? SER A 121 GLY A 122 
AA4 2 THR A 167 ? LEU A 170 ? THR A 166 LEU A 169 
AA4 3 ILE A 158 ? ASP A 162 ? ILE A 157 ASP A 161 
AA4 4 ILE A 140 ? PHE A 144 ? ILE A 139 PHE A 143 
AA4 5 SER A 133 ? LEU A 137 ? SER A 132 LEU A 136 
AA5 1 ARG A 129 ? ASP A 130 ? ARG A 128 ASP A 129 
AA5 2 TYR A 147 ? GLU A 148 ? TYR A 146 GLU A 147 
AA5 3 CYS A 153 ? PHE A 154 ? CYS A 152 PHE A 153 
AA6 1 SER A 185 ? LEU A 189 ? SER A 184 LEU A 188 
AA6 2 HIS A 192 ? PHE A 196 ? HIS A 191 PHE A 195 
AA6 3 ARG A 218 ? ASP A 221 ? ARG A 217 ASP A 220 
AA6 4 ALA A 226 ? TRP A 227 ? ALA A 225 TRP A 226 
AA7 1 ARG A 199 ? ASP A 201 ? ARG A 198 ASP A 200 
AA7 2 GLU A 211 ? TYR A 213 ? GLU A 210 TYR A 212 
AA8 1 SER A 244 ? TYR A 248 ? SER A 243 TYR A 247 
AA8 2 GLU A 251 ? ASN A 259 ? GLU A 250 ASN A 258 
AA8 3 ARG A 264 ? ASN A 273 ? ARG A 263 ASN A 272 
AA8 4 THR A 278 ? LYS A 281 ? THR A 277 LYS A 280 
AA9 1 THR A 310 ? PRO A 312 ? THR A 309 PRO A 311 
AA9 2 LEU A 324 ? ASP A 326 ? LEU A 323 ASP A 325 
AB1 1 GLN B 49  ? LEU B 50  ? GLN B 49  LEU B 50  
AB1 2 GLN B 42  ? LYS B 46  ? GLN B 42  LYS B 46  
AB1 3 ALA B 73  ? PHE B 79  ? ALA B 73  PHE B 79  
AB1 4 ASP B 2   ? ARG B 9   ? ASP B 2   ARG B 9   
AB1 5 THR B 12  ? LYS B 19  ? THR B 12  LYS B 19  
AB1 6 GLU C 37  ? LYS C 41  ? GLU C 28  LYS C 32  
AB1 7 TYR C 27  ? ILE C 31  ? TYR C 18  ILE C 22  
AB1 8 GLU C 68  ? ASN C 70  ? GLU C 59  ASN C 61  
AB2 1 ILE D 13  ? GLU D 16  ? ILE D 13  GLU D 16  
AB2 2 GLN D 2   ? LYS D 6   ? GLN D 2   LYS D 6   
AB2 3 THR D 66  ? LEU D 71  ? THR D 66  LEU D 71  
AB2 4 GLN D 41  ? PHE D 45  ? GLN D 41  PHE D 45  
AB2 5 LYS D 48  ? GLN D 49  ? LYS D 48  GLN D 49  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 4   ? N ARG A 3   O ASP A 334 ? O ASP A 333 
AA1 2 3 O HIS A 331 ? O HIS A 330 N LEU A 306 ? N LEU A 305 
AA1 3 4 O LYS A 303 ? O LYS A 302 N VAL A 300 ? N VAL A 299 
AA2 1 2 N VAL A 23  ? N VAL A 22  O ARG A 26  ? O ARG A 25  
AA2 2 3 N SER A 29  ? N SER A 28  O HIS A 48  ? O HIS A 47  
AA2 3 4 N ASN A 51  ? N ASN A 50  O ARG A 56  ? O ARG A 55  
AA3 1 2 N VAL A 84  ? N VAL A 83  O LEU A 91  ? O LEU A 90  
AA3 2 3 N LEU A 92  ? N LEU A 91  O TYR A 107 ? O TYR A 106 
AA3 3 4 N ALA A 108 ? N ALA A 107 O PHE A 117 ? O PHE A 116 
AA4 1 2 N SER A 122 ? N SER A 121 O TRP A 168 ? O TRP A 167 
AA4 2 3 O THR A 167 ? O THR A 166 N ASP A 162 ? N ASP A 161 
AA4 3 4 O HIS A 159 ? O HIS A 158 N ILE A 143 ? N ILE A 142 
AA4 4 5 O TYR A 142 ? O TYR A 141 N CYS A 135 ? N CYS A 134 
AA5 1 2 N ASP A 130 ? N ASP A 129 O TYR A 147 ? O TYR A 146 
AA5 2 3 N GLU A 148 ? N GLU A 147 O CYS A 153 ? O CYS A 152 
AA6 1 2 N THR A 187 ? N THR A 186 O TYR A 194 ? O TYR A 193 
AA6 2 3 N VAL A 195 ? N VAL A 194 O ARG A 218 ? O ARG A 217 
AA6 3 4 N ASP A 221 ? N ASP A 220 O ALA A 226 ? O ALA A 225 
AA7 1 2 N ALA A 200 ? N ALA A 199 O ILE A 212 ? O ILE A 211 
AA8 1 2 N PHE A 246 ? N PHE A 245 O TYR A 253 ? O TYR A 252 
AA8 2 3 N LEU A 252 ? N LEU A 251 O PHE A 272 ? O PHE A 271 
AA8 3 4 N LYS A 271 ? N LYS A 270 O LYS A 280 ? O LYS A 279 
AA9 1 2 N SER A 311 ? N SER A 310 O ILE A 325 ? O ILE A 324 
AB1 1 2 O GLN B 49  ? O GLN B 49  N LYS B 46  ? N LYS B 46  
AB1 2 3 N ARG B 43  ? N ARG B 43  O ALA B 78  ? O ALA B 78  
AB1 3 4 O VAL B 75  ? O VAL B 75  N MET B 6   ? N MET B 6   
AB1 4 5 N VAL B 3   ? N VAL B 3   O ALA B 18  ? O ALA B 18  
AB1 5 6 N PHE B 15  ? N PHE B 15  O ILE C 39  ? O ILE C 30  
AB1 6 7 O PHE C 38  ? O PHE C 29  N LEU C 30  ? N LEU C 21  
AB1 7 8 N LYS C 29  ? N LYS C 20  O VAL C 69  ? O VAL C 60  
AB2 1 2 O LEU D 15  ? O LEU D 15  N ILE D 3   ? N ILE D 3   
AB2 2 3 N PHE D 4   ? N PHE D 4   O LEU D 67  ? O LEU D 67  
AB2 3 4 O HIS D 68  ? O HIS D 68  N ILE D 44  ? N ILE D 44  
AB2 4 5 N PHE D 45  ? N PHE D 45  O LYS D 48  ? O LYS D 48  
# 
_pdbx_entry_details.entry_id                   9D1Y 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  A SER 64  ? ? O  A GLN 69  ? ? 2.02 
2 1 NH1 A ARG 260 ? ? O  A HOH 501 ? ? 2.15 
3 1 O   C HOH 204 ? ? O  C HOH 217 ? ? 2.15 
4 1 OE2 B GLU 91  ? ? O  B HOH 301 ? ? 2.16 
5 1 O   B GLY 33  ? ? NZ B LYS 36  ? ? 2.18 
6 1 O   A HOH 536 ? ? O  A HOH 731 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ACE 
_pdbx_validate_rmsd_bond.auth_seq_id_1             0 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            MET 
_pdbx_validate_rmsd_bond.auth_seq_id_2             1 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.499 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.163 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 73  ? ? -171.31 137.44  
2 1 ASP A 86  ? ? 58.60   -113.16 
3 1 THR A 98  ? ? -83.83  -70.55  
4 1 SER A 207 ? ? -147.57 22.69   
5 1 HIS B 10  ? ? 50.14   -116.55 
6 1 ASP B 47  ? ? 46.29   -115.79 
7 1 ALA B 81  ? ? -96.10  -73.60  
8 1 ASP B 82  ? ? -122.79 -74.72  
9 1 LYS D 11  ? ? 62.42   69.90   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 637 ? G HOH . 
2 1 A HOH 721 ? G HOH . 
3 1 A HOH 747 ? G HOH . 
4 1 A HOH 765 ? G HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -27.1684 -7.1999  -13.9286 0.2248 ? -0.0306 ? -0.0318 ? 0.3025 ? 0.0253  ? 0.2810 ? 2.8756 ? 
-0.9279 ? -0.5392 ? 1.9362 ? 0.0191  ? 2.3973 ? 0.1052  ? 0.0895  ? -0.0821 ? -0.1767 ? 0.0149  ? 0.2913  ? -0.1235 ? -0.4861 ? 
-0.0906 ? 
2  'X-RAY DIFFRACTION' ? refined -28.9093 7.2614   -16.8900 0.2844 ? 0.0676  ? -0.0293 ? 0.3662 ? 0.0274  ? 0.3423 ? 1.7543 ? 
0.2279  ? -0.9586 ? 2.5084 ? -0.2319 ? 2.1371 ? -0.0460 ? 0.1949  ? 0.0872  ? -0.1797 ? 0.0650  ? 0.4236  ? -0.2860 ? -0.5691 ? 
0.0082  ? 
3  'X-RAY DIFFRACTION' ? refined -19.4398 12.5680  -24.8479 0.3585 ? 0.0637  ? -0.0136 ? 0.3339 ? 0.0505  ? 0.3000 ? 1.1970 ? 
0.1213  ? -0.6602 ? 2.5065 ? 0.3995  ? 2.4431 ? 0.0446  ? 0.1907  ? 0.0568  ? -0.4161 ? 0.0393  ? 0.0187  ? -0.3968 ? -0.3486 ? 
-0.0038 ? 
4  'X-RAY DIFFRACTION' ? refined -7.9447  -0.3503  -28.7548 0.3103 ? -0.0146 ? 0.0486  ? 0.2818 ? -0.0103 ? 0.2262 ? 1.1329 ? 
-0.5647 ? 0.1658  ? 1.8990 ? -0.9607 ? 1.5526 ? 0.0640  ? 0.1646  ? 0.0768  ? -0.3031 ? -0.0955 ? -0.1342 ? 0.0324  ? 0.0224  ? 
0.0199  ? 
5  'X-RAY DIFFRACTION' ? refined -17.1168 -11.6331 -20.2200 0.2898 ? 0.0222  ? 0.0288  ? 0.2526 ? -0.0134 ? 0.2711 ? 3.3222 ? 
-0.7088 ? 0.6092  ? 2.6947 ? -2.3366 ? 2.7514 ? 0.1539  ? 0.1357  ? -0.3276 ? -0.3424 ? 0.0207  ? 0.0859  ? 0.2574  ? -0.2510 ? 
-0.0309 ? 
6  'X-RAY DIFFRACTION' ? refined -15.6104 -22.0085 -7.2381  0.2932 ? -0.0239 ? 0.0313  ? 0.2283 ? -0.0108 ? 0.3784 ? 1.3559 ? 
-0.5492 ? 0.6703  ? 2.5194 ? -1.8555 ? 2.9679 ? -0.0020 ? -0.0887 ? -0.3822 ? -0.1101 ? 0.0368  ? 0.0779  ? 0.3982  ? -0.1665 ? 
-0.0934 ? 
7  'X-RAY DIFFRACTION' ? refined 18.8694  -23.3827 -2.5318  0.2018 ? 0.0206  ? 0.0166  ? 0.2741 ? -0.0173 ? 0.4828 ? 8.6696 ? 
-0.1823 ? 1.6002  ? 3.9217 ? 3.3539  ? 3.4160 ? -0.2013 ? 0.8425  ? 0.8493  ? -0.1851 ? 0.2734  ? -0.5651 ? -0.1694 ? 0.1124  ? 
0.0931  ? 
8  'X-RAY DIFFRACTION' ? refined 24.0764  -20.7135 1.5243   0.3328 ? -0.0107 ? -0.0328 ? 0.2331 ? 0.0679  ? 0.5617 ? 6.0394 ? 
-2.3054 ? 0.6927  ? 2.0023 ? -0.1649 ? 3.9060 ? -0.1299 ? 0.4121  ? 0.9595  ? -0.2368 ? 0.0973  ? -0.5522 ? -0.6775 ? 0.0865  ? 
0.0822  ? 
9  'X-RAY DIFFRACTION' ? refined 31.0367  -25.5069 6.7946   0.3056 ? 0.0467  ? -0.0358 ? 0.3255 ? -0.0087 ? 0.4515 ? 5.7131 ? 
-2.4936 ? 0.8410  ? 3.3768 ? 0.4088  ? 5.1324 ? -0.3080 ? -0.2225 ? 0.7162  ? -0.0052 ? -0.0623 ? -0.6205 ? -0.0685 ? 0.4667  ? 
0.0612  ? 
10 'X-RAY DIFFRACTION' ? refined 27.3691  -34.1077 -4.6864  0.2670 ? 0.0168  ? 0.0761  ? 0.5154 ? 0.0121  ? 0.4769 ? 3.9090 ? 
-1.6574 ? 5.3839  ? 4.7938 ? 0.2856  ? 9.0070 ? 0.6470  ? 0.1742  ? -0.2314 ? -0.6554 ? -0.0494 ? -0.2172 ? 0.3714  ? -0.0719 ? 
-0.5440 ? 
11 'X-RAY DIFFRACTION' ? refined 27.3315  -24.6680 -9.3830  0.3990 ? 0.0740  ? 0.0442  ? 0.5369 ? 0.0957  ? 0.4485 ? 4.7244 ? 
-2.1013 ? 2.5894  ? 4.5449 ? -0.3766 ? 2.2045 ? 0.2324  ? 1.3456  ? 0.6323  ? -0.5534 ? -0.3701 ? -0.3902 ? 0.4122  ? 0.6565  ? 
0.1984  ? 
12 'X-RAY DIFFRACTION' ? refined 20.6928  -31.5437 3.9335   0.2787 ? 0.0343  ? 0.0120  ? 0.1983 ? 0.0250  ? 0.4390 ? 4.9029 ? 
-1.1260 ? 1.6300  ? 1.6039 ? -0.1200 ? 4.6679 ? -0.2560 ? -0.3323 ? -0.5334 ? 0.2556  ? 0.3040  ? 0.2695  ? -0.1554 ? -0.2457 ? 
-0.0343 ? 
13 'X-RAY DIFFRACTION' ? refined 11.3053  -19.7274 8.1165   0.3282 ? 0.0960  ? -0.0052 ? 0.3426 ? 0.0161  ? 0.4213 ? 4.8081 ? 
-0.0845 ? 0.8989  ? 3.0156 ? 1.3759  ? 2.7100 ? -0.2782 ? -0.5654 ? 0.4104  ? 0.2122  ? 0.1459  ? -0.5328 ? -0.3040 ? -0.1090 ? 
0.1450  ? 
14 'X-RAY DIFFRACTION' ? refined 4.2746   -17.6676 13.7078  0.3598 ? 0.1348  ? 0.0012  ? 0.5032 ? 0.0039  ? 0.4682 ? 2.2116 ? 
-2.8767 ? -1.1368 ? 4.6783 ? 3.7468  ? 5.0332 ? -0.5416 ? -0.8125 ? 0.0650  ? 0.4554  ? 0.0770  ? 0.3680  ? -0.0747 ? -0.3472 ? 
0.5175  ? 
15 'X-RAY DIFFRACTION' ? refined 6.4067   -21.4004 -1.5175  0.2807 ? 0.0428  ? 0.0049  ? 0.2721 ? 0.0535  ? 0.3761 ? 4.5626 ? 
0.1245  ? 0.4515  ? 3.3169 ? -0.3387 ? 4.6149 ? -0.1900 ? 0.1342  ? 0.0797  ? 0.2198  ? 0.1493  ? -0.0897 ? -0.2066 ? 0.3188  ? 
0.0121  ? 
16 'X-RAY DIFFRACTION' ? refined 3.7286   -19.1795 -11.8723 0.3640 ? 0.1108  ? 0.0125  ? 0.3912 ? 0.0635  ? 0.5683 ? 2.6363 ? 
1.8006  ? -2.0339 ? 9.1100 ? -6.4518 ? 7.8035 ? -0.2459 ? 0.5792  ? 0.1513  ? -0.0132 ? -0.2061 ? -0.9850 ? -0.3017 ? -0.1310 ? 
0.2982  ? 
17 'X-RAY DIFFRACTION' ? refined -3.4052  -25.9506 3.1805   0.2269 ? 0.0186  ? 0.0372  ? 0.2955 ? 0.1295  ? 0.3685 ? 4.4109 ? 
0.7682  ? 1.4399  ? 3.2457 ? 1.3423  ? 5.9413 ? -0.0256 ? -0.7221 ? -0.5370 ? 0.1232  ? 0.2824  ? -0.4466 ? -0.0706 ? -0.5585 ? 
-0.2098 ? 
18 'X-RAY DIFFRACTION' ? refined -26.5442 -10.6235 -50.8930 1.1378 ? -0.0771 ? -0.0989 ? 1.1103 ? -0.2344 ? 0.6608 ? 7.8468 ? 
1.8429  ? 5.2152  ? 9.3474 ? 1.9859  ? 6.8424 ? 0.7909  ? 1.6176  ? -1.6497 ? -1.0635 ? -0.2973 ? 0.3782  ? 1.0512  ? -0.5531 ? 
-0.6852 ? 
19 'X-RAY DIFFRACTION' ? refined -36.1062 -6.4665  -55.9978 1.2116 ? -0.2883 ? -0.5368 ? 1.7504 ? -0.0198 ? 1.1682 ? 1.3452 ? 
-0.4932 ? -0.9151 ? 7.0430 ? 2.1385  ? 1.0979 ? 0.0435  ? 1.6095  ? -0.1128 ? -1.4386 ? -0.2573 ? 1.4634  ? 0.1088  ? -1.7794 ? 
0.3372  ? 
20 'X-RAY DIFFRACTION' ? refined -36.9597 -6.4814  -47.2389 1.0012 ? -0.2422 ? -0.3263 ? 1.1426 ? -0.2554 ? 1.0363 ? 5.1597 ? 
0.2152  ? 0.3010  ? 4.0036 ? 3.8277  ? 8.8384 ? 0.1799  ? 1.0984  ? -0.3627 ? -0.7851 ? -0.7363 ? 2.0712  ? 1.0555  ? -1.5500 ? 
0.5562  ? 
21 'X-RAY DIFFRACTION' ? refined -31.9662 -2.6949  -41.7515 0.6917 ? -0.0408 ? 0.0118  ? 0.9668 ? -0.0024 ? 0.6159 ? 3.4264 ? 
3.9559  ? -0.4394 ? 5.6146 ? -3.3637 ? 8.0207 ? 0.1840  ? -0.0170 ? 0.0000  ? 0.0288  ? 0.2669  ? 1.4002  ? 0.1465  ? -1.2225 ? 
-0.1505 ? 
22 'X-RAY DIFFRACTION' ? refined -29.3956 3.9054   -52.0650 1.0340 ? 0.1673  ? -0.3960 ? 1.1074 ? -0.1144 ? 0.7385 ? 9.3458 ? 
0.1561  ? -0.4187 ? 4.9802 ? -3.9374 ? 6.6454 ? -0.1608 ? 1.3614  ? 0.7560  ? -1.1621 ? -0.1563 ? 1.2059  ? -0.9011 ? -1.2418 ? 
0.2926  ? 
23 'X-RAY DIFFRACTION' ? refined -27.4213 -3.2821  -48.1350 1.1784 ? -0.1086 ? -0.1428 ? 0.8320 ? -0.0140 ? 0.3410 ? 1.5760 ? 
-0.1663 ? 0.1797  ? 0.2948 ? -1.0319 ? 4.2186 ? 0.0109  ? 1.0552  ? -0.1774 ? -1.2013 ? 0.2253  ? 0.4758  ? -0.6773 ? -0.4693 ? 
-0.1342 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 68 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 69 through 124 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 125 through 169 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 170 through 294 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 295 through 322 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 377 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 9 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 10 through 35 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 36 through 45 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 46 through 50 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 51 through 66 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 67 through 97 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 17 through 38 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 39 through 66 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 67 through 83 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 84 through 96 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 97 through 112 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 12 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 13 through 22 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 23 through 34 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 35 through 44 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 45 through 56 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 57 through 76 )
;
# 
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 GLU 314 ? A GLU 315 
2  1 Y 1 A GLU 315 ? A GLU 316 
3  1 Y 1 A GLY 316 ? A GLY 317 
4  1 Y 1 A LEU 317 ? A LEU 318 
5  1 Y 1 A GLY 318 ? A GLY 319 
6  1 Y 1 A ASP 319 ? A ASP 320 
7  1 Y 1 A GLU 320 ? A GLU 321 
8  1 Y 1 A VAL 378 ? A VAL 379 
9  1 Y 1 A SER 379 ? A SER 380 
10 1 Y 1 A SER 380 ? A SER 381 
11 1 Y 1 A HIS 381 ? A HIS 382 
12 1 Y 1 A LYS 382 ? A LYS 383 
13 1 Y 1 B GLU 98  ? B GLU 98  
14 1 Y 1 B LEU 99  ? B LEU 99  
15 1 Y 1 B PRO 100 ? B PRO 100 
16 1 Y 1 B ASP 101 ? B ASP 101 
17 1 Y 1 B VAL 102 ? B VAL 102 
18 1 Y 1 B MET 103 ? B MET 103 
19 1 Y 1 B LYS 104 ? B LYS 104 
20 1 Y 1 C MET -8  ? C MET 1   
21 1 Y 1 C SER -7  ? C SER 2   
22 1 Y 1 C TYR -6  ? C TYR 3   
23 1 Y 1 C TYR -5  ? C TYR 4   
24 1 Y 1 C HIS -4  ? C HIS 5   
25 1 Y 1 C HIS -3  ? C HIS 6   
26 1 Y 1 C HIS -2  ? C HIS 7   
27 1 Y 1 C HIS -1  ? C HIS 8   
28 1 Y 1 C HIS 0   ? C HIS 9   
29 1 Y 1 C HIS 1   ? C HIS 10  
30 1 Y 1 C ASP 2   ? C ASP 11  
31 1 Y 1 C TYR 3   ? C TYR 12  
32 1 Y 1 C ASP 4   ? C ASP 13  
33 1 Y 1 C ILE 5   ? C ILE 14  
34 1 Y 1 C PRO 6   ? C PRO 15  
35 1 Y 1 C THR 7   ? C THR 16  
36 1 Y 1 C THR 8   ? C THR 17  
37 1 Y 1 C GLU 9   ? C GLU 18  
38 1 Y 1 C ASN 10  ? C ASN 19  
39 1 Y 1 C LEU 11  ? C LEU 20  
40 1 Y 1 C TYR 12  ? C TYR 21  
41 1 Y 1 C GLY 13  ? C GLY 22  
42 1 Y 1 C GLN 14  ? C GLN 23  
43 1 Y 1 C GLY 15  ? C GLY 24  
44 1 Y 1 C ALA 16  ? C ALA 25  
45 1 Y 1 C GLN 51  ? C GLN 60  
46 1 Y 1 C PHE 52  ? C PHE 61  
47 1 Y 1 C ALA 53  ? C ALA 62  
48 1 Y 1 C GLU 54  ? C GLU 63  
49 1 Y 1 C ASN 55  ? C ASN 64  
50 1 Y 1 C GLU 56  ? C GLU 65  
51 1 Y 1 C THR 57  ? C THR 66  
# 
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 
ACE C    C N N 1   
ACE O    O N N 2   
ACE CH3  C N N 3   
ACE H    H N N 4   
ACE H1   H N N 5   
ACE H2   H N N 6   
ACE H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
CYS N    N N N 81  
CYS CA   C N R 82  
CYS C    C N N 83  
CYS O    O N N 84  
CYS CB   C N N 85  
CYS SG   S N N 86  
CYS OXT  O N N 87  
CYS H    H N N 88  
CYS H2   H N N 89  
CYS HA   H N N 90  
CYS HB2  H N N 91  
CYS HB3  H N N 92  
CYS HG   H N N 93  
CYS HXT  H N N 94  
GLN N    N N N 95  
GLN CA   C N S 96  
GLN C    C N N 97  
GLN O    O N N 98  
GLN CB   C N N 99  
GLN CG   C N N 100 
GLN CD   C N N 101 
GLN OE1  O N N 102 
GLN NE2  N N N 103 
GLN OXT  O N N 104 
GLN H    H N N 105 
GLN H2   H N N 106 
GLN HA   H N N 107 
GLN HB2  H N N 108 
GLN HB3  H N N 109 
GLN HG2  H N N 110 
GLN HG3  H N N 111 
GLN HE21 H N N 112 
GLN HE22 H N N 113 
GLN HXT  H N N 114 
GLU N    N N N 115 
GLU CA   C N S 116 
GLU C    C N N 117 
GLU O    O N N 118 
GLU CB   C N N 119 
GLU CG   C N N 120 
GLU CD   C N N 121 
GLU OE1  O N N 122 
GLU OE2  O N N 123 
GLU OXT  O N N 124 
GLU H    H N N 125 
GLU H2   H N N 126 
GLU HA   H N N 127 
GLU HB2  H N N 128 
GLU HB3  H N N 129 
GLU HG2  H N N 130 
GLU HG3  H N N 131 
GLU HE2  H N N 132 
GLU HXT  H N N 133 
GLY N    N N N 134 
GLY CA   C N N 135 
GLY C    C N N 136 
GLY O    O N N 137 
GLY OXT  O N N 138 
GLY H    H N N 139 
GLY H2   H N N 140 
GLY HA2  H N N 141 
GLY HA3  H N N 142 
GLY HXT  H N N 143 
GOL C1   C N N 144 
GOL O1   O N N 145 
GOL C2   C N N 146 
GOL O2   O N N 147 
GOL C3   C N N 148 
GOL O3   O N N 149 
GOL H11  H N N 150 
GOL H12  H N N 151 
GOL HO1  H N N 152 
GOL H2   H N N 153 
GOL HO2  H N N 154 
GOL H31  H N N 155 
GOL H32  H N N 156 
GOL HO3  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
VAL N    N N N 393 
VAL CA   C N S 394 
VAL C    C N N 395 
VAL O    O N N 396 
VAL CB   C N N 397 
VAL CG1  C N N 398 
VAL CG2  C N N 399 
VAL OXT  O N N 400 
VAL H    H N N 401 
VAL H2   H N N 402 
VAL HA   H N N 403 
VAL HB   H N N 404 
VAL HG11 H N N 405 
VAL HG12 H N N 406 
VAL HG13 H N N 407 
VAL HG21 H N N 408 
VAL HG22 H N N 409 
VAL HG23 H N N 410 
VAL HXT  H N N 411 
# 
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 
ACE C   O    doub N N 1   
ACE C   CH3  sing N N 2   
ACE C   H    sing N N 3   
ACE CH3 H1   sing N N 4   
ACE CH3 H2   sing N N 5   
ACE CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
CYS N   CA   sing N N 76  
CYS N   H    sing N N 77  
CYS N   H2   sing N N 78  
CYS CA  C    sing N N 79  
CYS CA  CB   sing N N 80  
CYS CA  HA   sing N N 81  
CYS C   O    doub N N 82  
CYS C   OXT  sing N N 83  
CYS CB  SG   sing N N 84  
CYS CB  HB2  sing N N 85  
CYS CB  HB3  sing N N 86  
CYS SG  HG   sing N N 87  
CYS OXT HXT  sing N N 88  
GLN N   CA   sing N N 89  
GLN N   H    sing N N 90  
GLN N   H2   sing N N 91  
GLN CA  C    sing N N 92  
GLN CA  CB   sing N N 93  
GLN CA  HA   sing N N 94  
GLN C   O    doub N N 95  
GLN C   OXT  sing N N 96  
GLN CB  CG   sing N N 97  
GLN CB  HB2  sing N N 98  
GLN CB  HB3  sing N N 99  
GLN CG  CD   sing N N 100 
GLN CG  HG2  sing N N 101 
GLN CG  HG3  sing N N 102 
GLN CD  OE1  doub N N 103 
GLN CD  NE2  sing N N 104 
GLN NE2 HE21 sing N N 105 
GLN NE2 HE22 sing N N 106 
GLN OXT HXT  sing N N 107 
GLU N   CA   sing N N 108 
GLU N   H    sing N N 109 
GLU N   H2   sing N N 110 
GLU CA  C    sing N N 111 
GLU CA  CB   sing N N 112 
GLU CA  HA   sing N N 113 
GLU C   O    doub N N 114 
GLU C   OXT  sing N N 115 
GLU CB  CG   sing N N 116 
GLU CB  HB2  sing N N 117 
GLU CB  HB3  sing N N 118 
GLU CG  CD   sing N N 119 
GLU CG  HG2  sing N N 120 
GLU CG  HG3  sing N N 121 
GLU CD  OE1  doub N N 122 
GLU CD  OE2  sing N N 123 
GLU OE2 HE2  sing N N 124 
GLU OXT HXT  sing N N 125 
GLY N   CA   sing N N 126 
GLY N   H    sing N N 127 
GLY N   H2   sing N N 128 
GLY CA  C    sing N N 129 
GLY CA  HA2  sing N N 130 
GLY CA  HA3  sing N N 131 
GLY C   O    doub N N 132 
GLY C   OXT  sing N N 133 
GLY OXT HXT  sing N N 134 
GOL C1  O1   sing N N 135 
GOL C1  C2   sing N N 136 
GOL C1  H11  sing N N 137 
GOL C1  H12  sing N N 138 
GOL O1  HO1  sing N N 139 
GOL C2  O2   sing N N 140 
GOL C2  C3   sing N N 141 
GOL C2  H2   sing N N 142 
GOL O2  HO2  sing N N 143 
GOL C3  O3   sing N N 144 
GOL C3  H31  sing N N 145 
GOL C3  H32  sing N N 146 
GOL O3  HO3  sing N N 147 
HIS N   CA   sing N N 148 
HIS N   H    sing N N 149 
HIS N   H2   sing N N 150 
HIS CA  C    sing N N 151 
HIS CA  CB   sing N N 152 
HIS CA  HA   sing N N 153 
HIS C   O    doub N N 154 
HIS C   OXT  sing N N 155 
HIS CB  CG   sing N N 156 
HIS CB  HB2  sing N N 157 
HIS CB  HB3  sing N N 158 
HIS CG  ND1  sing Y N 159 
HIS CG  CD2  doub Y N 160 
HIS ND1 CE1  doub Y N 161 
HIS ND1 HD1  sing N N 162 
HIS CD2 NE2  sing Y N 163 
HIS CD2 HD2  sing N N 164 
HIS CE1 NE2  sing Y N 165 
HIS CE1 HE1  sing N N 166 
HIS NE2 HE2  sing N N 167 
HIS OXT HXT  sing N N 168 
HOH O   H1   sing N N 169 
HOH O   H2   sing N N 170 
ILE N   CA   sing N N 171 
ILE N   H    sing N N 172 
ILE N   H2   sing N N 173 
ILE CA  C    sing N N 174 
ILE CA  CB   sing N N 175 
ILE CA  HA   sing N N 176 
ILE C   O    doub N N 177 
ILE C   OXT  sing N N 178 
ILE CB  CG1  sing N N 179 
ILE CB  CG2  sing N N 180 
ILE CB  HB   sing N N 181 
ILE CG1 CD1  sing N N 182 
ILE CG1 HG12 sing N N 183 
ILE CG1 HG13 sing N N 184 
ILE CG2 HG21 sing N N 185 
ILE CG2 HG22 sing N N 186 
ILE CG2 HG23 sing N N 187 
ILE CD1 HD11 sing N N 188 
ILE CD1 HD12 sing N N 189 
ILE CD1 HD13 sing N N 190 
ILE OXT HXT  sing N N 191 
LEU N   CA   sing N N 192 
LEU N   H    sing N N 193 
LEU N   H2   sing N N 194 
LEU CA  C    sing N N 195 
LEU CA  CB   sing N N 196 
LEU CA  HA   sing N N 197 
LEU C   O    doub N N 198 
LEU C   OXT  sing N N 199 
LEU CB  CG   sing N N 200 
LEU CB  HB2  sing N N 201 
LEU CB  HB3  sing N N 202 
LEU CG  CD1  sing N N 203 
LEU CG  CD2  sing N N 204 
LEU CG  HG   sing N N 205 
LEU CD1 HD11 sing N N 206 
LEU CD1 HD12 sing N N 207 
LEU CD1 HD13 sing N N 208 
LEU CD2 HD21 sing N N 209 
LEU CD2 HD22 sing N N 210 
LEU CD2 HD23 sing N N 211 
LEU OXT HXT  sing N N 212 
LYS N   CA   sing N N 213 
LYS N   H    sing N N 214 
LYS N   H2   sing N N 215 
LYS CA  C    sing N N 216 
LYS CA  CB   sing N N 217 
LYS CA  HA   sing N N 218 
LYS C   O    doub N N 219 
LYS C   OXT  sing N N 220 
LYS CB  CG   sing N N 221 
LYS CB  HB2  sing N N 222 
LYS CB  HB3  sing N N 223 
LYS CG  CD   sing N N 224 
LYS CG  HG2  sing N N 225 
LYS CG  HG3  sing N N 226 
LYS CD  CE   sing N N 227 
LYS CD  HD2  sing N N 228 
LYS CD  HD3  sing N N 229 
LYS CE  NZ   sing N N 230 
LYS CE  HE2  sing N N 231 
LYS CE  HE3  sing N N 232 
LYS NZ  HZ1  sing N N 233 
LYS NZ  HZ2  sing N N 234 
LYS NZ  HZ3  sing N N 235 
LYS OXT HXT  sing N N 236 
MET N   CA   sing N N 237 
MET N   H    sing N N 238 
MET N   H2   sing N N 239 
MET CA  C    sing N N 240 
MET CA  CB   sing N N 241 
MET CA  HA   sing N N 242 
MET C   O    doub N N 243 
MET C   OXT  sing N N 244 
MET CB  CG   sing N N 245 
MET CB  HB2  sing N N 246 
MET CB  HB3  sing N N 247 
MET CG  SD   sing N N 248 
MET CG  HG2  sing N N 249 
MET CG  HG3  sing N N 250 
MET SD  CE   sing N N 251 
MET CE  HE1  sing N N 252 
MET CE  HE2  sing N N 253 
MET CE  HE3  sing N N 254 
MET OXT HXT  sing N N 255 
PHE N   CA   sing N N 256 
PHE N   H    sing N N 257 
PHE N   H2   sing N N 258 
PHE CA  C    sing N N 259 
PHE CA  CB   sing N N 260 
PHE CA  HA   sing N N 261 
PHE C   O    doub N N 262 
PHE C   OXT  sing N N 263 
PHE CB  CG   sing N N 264 
PHE CB  HB2  sing N N 265 
PHE CB  HB3  sing N N 266 
PHE CG  CD1  doub Y N 267 
PHE CG  CD2  sing Y N 268 
PHE CD1 CE1  sing Y N 269 
PHE CD1 HD1  sing N N 270 
PHE CD2 CE2  doub Y N 271 
PHE CD2 HD2  sing N N 272 
PHE CE1 CZ   doub Y N 273 
PHE CE1 HE1  sing N N 274 
PHE CE2 CZ   sing Y N 275 
PHE CE2 HE2  sing N N 276 
PHE CZ  HZ   sing N N 277 
PHE OXT HXT  sing N N 278 
PRO N   CA   sing N N 279 
PRO N   CD   sing N N 280 
PRO N   H    sing N N 281 
PRO CA  C    sing N N 282 
PRO CA  CB   sing N N 283 
PRO CA  HA   sing N N 284 
PRO C   O    doub N N 285 
PRO C   OXT  sing N N 286 
PRO CB  CG   sing N N 287 
PRO CB  HB2  sing N N 288 
PRO CB  HB3  sing N N 289 
PRO CG  CD   sing N N 290 
PRO CG  HG2  sing N N 291 
PRO CG  HG3  sing N N 292 
PRO CD  HD2  sing N N 293 
PRO CD  HD3  sing N N 294 
PRO OXT HXT  sing N N 295 
SER N   CA   sing N N 296 
SER N   H    sing N N 297 
SER N   H2   sing N N 298 
SER CA  C    sing N N 299 
SER CA  CB   sing N N 300 
SER CA  HA   sing N N 301 
SER C   O    doub N N 302 
SER C   OXT  sing N N 303 
SER CB  OG   sing N N 304 
SER CB  HB2  sing N N 305 
SER CB  HB3  sing N N 306 
SER OG  HG   sing N N 307 
SER OXT HXT  sing N N 308 
THR N   CA   sing N N 309 
THR N   H    sing N N 310 
THR N   H2   sing N N 311 
THR CA  C    sing N N 312 
THR CA  CB   sing N N 313 
THR CA  HA   sing N N 314 
THR C   O    doub N N 315 
THR C   OXT  sing N N 316 
THR CB  OG1  sing N N 317 
THR CB  CG2  sing N N 318 
THR CB  HB   sing N N 319 
THR OG1 HG1  sing N N 320 
THR CG2 HG21 sing N N 321 
THR CG2 HG22 sing N N 322 
THR CG2 HG23 sing N N 323 
THR OXT HXT  sing N N 324 
TRP N   CA   sing N N 325 
TRP N   H    sing N N 326 
TRP N   H2   sing N N 327 
TRP CA  C    sing N N 328 
TRP CA  CB   sing N N 329 
TRP CA  HA   sing N N 330 
TRP C   O    doub N N 331 
TRP C   OXT  sing N N 332 
TRP CB  CG   sing N N 333 
TRP CB  HB2  sing N N 334 
TRP CB  HB3  sing N N 335 
TRP CG  CD1  doub Y N 336 
TRP CG  CD2  sing Y N 337 
TRP CD1 NE1  sing Y N 338 
TRP CD1 HD1  sing N N 339 
TRP CD2 CE2  doub Y N 340 
TRP CD2 CE3  sing Y N 341 
TRP NE1 CE2  sing Y N 342 
TRP NE1 HE1  sing N N 343 
TRP CE2 CZ2  sing Y N 344 
TRP CE3 CZ3  doub Y N 345 
TRP CE3 HE3  sing N N 346 
TRP CZ2 CH2  doub Y N 347 
TRP CZ2 HZ2  sing N N 348 
TRP CZ3 CH2  sing Y N 349 
TRP CZ3 HZ3  sing N N 350 
TRP CH2 HH2  sing N N 351 
TRP OXT HXT  sing N N 352 
TYR N   CA   sing N N 353 
TYR N   H    sing N N 354 
TYR N   H2   sing N N 355 
TYR CA  C    sing N N 356 
TYR CA  CB   sing N N 357 
TYR CA  HA   sing N N 358 
TYR C   O    doub N N 359 
TYR C   OXT  sing N N 360 
TYR CB  CG   sing N N 361 
TYR CB  HB2  sing N N 362 
TYR CB  HB3  sing N N 363 
TYR CG  CD1  doub Y N 364 
TYR CG  CD2  sing Y N 365 
TYR CD1 CE1  sing Y N 366 
TYR CD1 HD1  sing N N 367 
TYR CD2 CE2  doub Y N 368 
TYR CD2 HD2  sing N N 369 
TYR CE1 CZ   doub Y N 370 
TYR CE1 HE1  sing N N 371 
TYR CE2 CZ   sing Y N 372 
TYR CE2 HE2  sing N N 373 
TYR CZ  OH   sing N N 374 
TYR OH  HH   sing N N 375 
TYR OXT HXT  sing N N 376 
VAL N   CA   sing N N 377 
VAL N   H    sing N N 378 
VAL N   H2   sing N N 379 
VAL CA  C    sing N N 380 
VAL CA  CB   sing N N 381 
VAL CA  HA   sing N N 382 
VAL C   O    doub N N 383 
VAL C   OXT  sing N N 384 
VAL CB  CG1  sing N N 385 
VAL CB  CG2  sing N N 386 
VAL CB  HB   sing N N 387 
VAL CG1 HG11 sing N N 388 
VAL CG1 HG12 sing N N 389 
VAL CG1 HG13 sing N N 390 
VAL CG2 HG21 sing N N 391 
VAL CG2 HG22 sing N N 392 
VAL CG2 HG23 sing N N 393 
VAL OXT HXT  sing N N 394 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Institute on Aging (NIH/NIA)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AG011085 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D1Y 
_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]   0.008729 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008228 
_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]   0.006538 
_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 
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 
HETATM 1    C C   . ACE A 1 1   ? 2.034   -14.853 -9.039  1.00 38.96  ? 0   ACE A C   1 
HETATM 2    O O   . ACE A 1 1   ? 2.520   -15.285 -8.038  1.00 30.09  ? 0   ACE A O   1 
HETATM 3    C CH3 . ACE A 1 1   ? 2.076   -13.335 -9.129  1.00 44.84  ? 0   ACE A CH3 1 
ATOM   4    N N   . MET A 1 2   ? 1.417   -15.702 -10.109 1.00 34.13  ? 1   MET A N   1 
ATOM   5    C CA  . MET A 1 2   ? 0.853   -15.219 -11.393 1.00 34.58  ? 1   MET A CA  1 
ATOM   6    C C   . MET A 1 2   ? -0.582  -15.521 -11.934 1.00 38.01  ? 1   MET A C   1 
ATOM   7    O O   . MET A 1 2   ? -1.181  -16.596 -11.669 1.00 33.83  ? 1   MET A O   1 
ATOM   8    C CB  . MET A 1 2   ? 1.749   -15.733 -12.492 1.00 35.63  ? 1   MET A CB  1 
ATOM   9    C CG  . MET A 1 2   ? 2.007   -14.553 -13.404 1.00 43.38  ? 1   MET A CG  1 
ATOM   10   S SD  . MET A 1 2   ? 2.226   -15.362 -14.992 1.00 64.25  ? 1   MET A SD  1 
ATOM   11   C CE  . MET A 1 2   ? 0.981   -16.684 -14.997 1.00 48.11  ? 1   MET A CE  1 
ATOM   12   N N   . LEU A 1 3   ? -1.078  -14.609 -12.784 1.00 35.80  ? 2   LEU A N   1 
ATOM   13   C CA  . LEU A 1 3   ? -2.505  -14.460 -13.076 1.00 32.20  ? 2   LEU A CA  1 
ATOM   14   C C   . LEU A 1 3   ? -3.182  -15.681 -13.685 1.00 32.24  ? 2   LEU A C   1 
ATOM   15   O O   . LEU A 1 3   ? -2.611  -16.399 -14.496 1.00 32.93  ? 2   LEU A O   1 
ATOM   16   C CB  . LEU A 1 3   ? -2.749  -13.242 -13.985 1.00 30.05  ? 2   LEU A CB  1 
ATOM   17   C CG  . LEU A 1 3   ? -2.625  -13.314 -15.506 1.00 33.29  ? 2   LEU A CG  1 
ATOM   18   C CD1 . LEU A 1 3   ? -3.003  -11.971 -16.126 1.00 32.29  ? 2   LEU A CD1 1 
ATOM   19   C CD2 . LEU A 1 3   ? -1.228  -13.704 -15.937 1.00 33.79  ? 2   LEU A CD2 1 
ATOM   20   N N   . ARG A 1 4   ? -4.435  -15.878 -13.285 1.00 28.63  ? 3   ARG A N   1 
ATOM   21   C CA  . ARG A 1 4   ? -5.121  -17.137 -13.496 1.00 30.13  ? 3   ARG A CA  1 
ATOM   22   C C   . ARG A 1 4   ? -6.625  -16.900 -13.506 1.00 28.18  ? 3   ARG A C   1 
ATOM   23   O O   . ARG A 1 4   ? -7.138  -16.099 -12.720 1.00 28.68  ? 3   ARG A O   1 
ATOM   24   C CB  . ARG A 1 4   ? -4.742  -18.126 -12.388 1.00 28.46  ? 3   ARG A CB  1 
ATOM   25   C CG  . ARG A 1 4   ? -5.560  -19.386 -12.353 1.00 25.44  ? 3   ARG A CG  1 
ATOM   26   C CD  . ARG A 1 4   ? -5.108  -20.265 -11.221 1.00 26.43  ? 3   ARG A CD  1 
ATOM   27   N NE  . ARG A 1 4   ? -3.746  -20.756 -11.383 1.00 26.29  ? 3   ARG A NE  1 
ATOM   28   C CZ  . ARG A 1 4   ? -3.450  -21.906 -11.972 1.00 30.39  ? 3   ARG A CZ  1 
ATOM   29   N NH1 . ARG A 1 4   ? -4.396  -22.686 -12.477 1.00 30.01  ? 3   ARG A NH1 1 
ATOM   30   N NH2 . ARG A 1 4   ? -2.175  -22.279 -12.071 1.00 28.84  ? 3   ARG A NH2 1 
ATOM   31   N N   . TRP A 1 5   ? -7.327  -17.603 -14.384 1.00 27.80  ? 4   TRP A N   1 
ATOM   32   C CA  . TRP A 1 5   ? -8.783  -17.664 -14.283 1.00 28.33  ? 4   TRP A CA  1 
ATOM   33   C C   . TRP A 1 5   ? -9.139  -18.549 -13.098 1.00 27.17  ? 4   TRP A C   1 
ATOM   34   O O   . TRP A 1 5   ? -8.877  -19.757 -13.111 1.00 27.36  ? 4   TRP A O   1 
ATOM   35   C CB  . TRP A 1 5   ? -9.394  -18.199 -15.574 1.00 26.19  ? 4   TRP A CB  1 
ATOM   36   C CG  . TRP A 1 5   ? -9.033  -17.369 -16.789 1.00 30.79  ? 4   TRP A CG  1 
ATOM   37   C CD1 . TRP A 1 5   ? -8.125  -17.687 -17.767 1.00 30.85  ? 4   TRP A CD1 1 
ATOM   38   C CD2 . TRP A 1 5   ? -9.585  -16.098 -17.157 1.00 29.26  ? 4   TRP A CD2 1 
ATOM   39   N NE1 . TRP A 1 5   ? -8.078  -16.692 -18.706 1.00 29.95  ? 4   TRP A NE1 1 
ATOM   40   C CE2 . TRP A 1 5   ? -8.958  -15.704 -18.357 1.00 28.87  ? 4   TRP A CE2 1 
ATOM   41   C CE3 . TRP A 1 5   ? -10.547 -15.256 -16.592 1.00 27.99  ? 4   TRP A CE3 1 
ATOM   42   C CZ2 . TRP A 1 5   ? -9.260  -14.504 -18.998 1.00 28.09  ? 4   TRP A CZ2 1 
ATOM   43   C CZ3 . TRP A 1 5   ? -10.845 -14.068 -17.231 1.00 27.19  ? 4   TRP A CZ3 1 
ATOM   44   C CH2 . TRP A 1 5   ? -10.206 -13.702 -18.421 1.00 25.47  ? 4   TRP A CH2 1 
ATOM   45   N N   . THR A 1 6   ? -9.728  -17.964 -12.059 1.00 26.12  ? 5   THR A N   1 
ATOM   46   C CA  . THR A 1 6   ? -9.975  -18.726 -10.844 1.00 27.41  ? 5   THR A CA  1 
ATOM   47   C C   . THR A 1 6   ? -11.430 -19.101 -10.601 1.00 29.34  ? 5   THR A C   1 
ATOM   48   O O   . THR A 1 6   ? -11.680 -20.000 -9.797  1.00 30.09  ? 5   THR A O   1 
ATOM   49   C CB  . THR A 1 6   ? -9.480  -17.953 -9.622  1.00 27.74  ? 5   THR A CB  1 
ATOM   50   O OG1 . THR A 1 6   ? -10.169 -16.700 -9.562  1.00 27.76  ? 5   THR A OG1 1 
ATOM   51   C CG2 . THR A 1 6   ? -7.971  -17.738 -9.711  1.00 27.76  ? 5   THR A CG2 1 
ATOM   52   N N   . VAL A 1 7   ? -12.389 -18.432 -11.235 1.00 29.10  ? 6   VAL A N   1 
ATOM   53   C CA  . VAL A 1 7   ? -13.802 -18.690 -10.996 1.00 26.84  ? 6   VAL A CA  1 
ATOM   54   C C   . VAL A 1 7   ? -14.524 -18.688 -12.329 1.00 26.89  ? 6   VAL A C   1 
ATOM   55   O O   . VAL A 1 7   ? -14.276 -17.823 -13.175 1.00 26.54  ? 6   VAL A O   1 
ATOM   56   C CB  . VAL A 1 7   ? -14.428 -17.645 -10.051 1.00 28.37  ? 6   VAL A CB  1 
ATOM   57   C CG1 . VAL A 1 7   ? -15.947 -17.809 -10.019 1.00 26.61  ? 6   VAL A CG1 1 
ATOM   58   C CG2 . VAL A 1 7   ? -13.845 -17.759 -8.664  1.00 25.63  ? 6   VAL A CG2 1 
ATOM   59   N N   . HIS A 1 8   ? -15.411 -19.664 -12.520 1.00 27.82  ? 7   HIS A N   1 
ATOM   60   C CA  . HIS A 1 8   ? -16.332 -19.662 -13.654 1.00 28.58  ? 7   HIS A CA  1 
ATOM   61   C C   . HIS A 1 8   ? -17.724 -20.041 -13.146 1.00 29.51  ? 7   HIS A C   1 
ATOM   62   O O   . HIS A 1 8   ? -17.952 -21.182 -12.724 1.00 31.14  ? 7   HIS A O   1 
ATOM   63   C CB  . HIS A 1 8   ? -15.854 -20.606 -14.753 1.00 27.53  ? 7   HIS A CB  1 
ATOM   64   C CG  . HIS A 1 8   ? -16.789 -20.695 -15.915 1.00 30.14  ? 7   HIS A CG  1 
ATOM   65   N ND1 . HIS A 1 8   ? -17.356 -19.580 -16.502 1.00 34.29  ? 7   HIS A ND1 1 
ATOM   66   C CD2 . HIS A 1 8   ? -17.275 -21.761 -16.589 1.00 31.83  ? 7   HIS A CD2 1 
ATOM   67   C CE1 . HIS A 1 8   ? -18.134 -19.956 -17.503 1.00 30.95  ? 7   HIS A CE1 1 
ATOM   68   N NE2 . HIS A 1 8   ? -18.103 -21.275 -17.577 1.00 35.20  ? 7   HIS A NE2 1 
ATOM   69   N N   . LEU A 1 9   ? -18.655 -19.090 -13.205 1.00 27.00  ? 8   LEU A N   1 
ATOM   70   C CA  . LEU A 1 9   ? -19.975 -19.248 -12.616 1.00 29.99  ? 8   LEU A CA  1 
ATOM   71   C C   . LEU A 1 9   ? -21.073 -18.988 -13.638 1.00 32.12  ? 8   LEU A C   1 
ATOM   72   O O   . LEU A 1 9   ? -20.945 -18.138 -14.530 1.00 29.31  ? 8   LEU A O   1 
ATOM   73   C CB  . LEU A 1 9   ? -20.152 -18.312 -11.430 1.00 29.28  ? 8   LEU A CB  1 
ATOM   74   C CG  . LEU A 1 9   ? -19.336 -18.690 -10.199 1.00 29.16  ? 8   LEU A CG  1 
ATOM   75   C CD1 . LEU A 1 9   ? -19.411 -17.607 -9.139  1.00 25.80  ? 8   LEU A CD1 1 
ATOM   76   C CD2 . LEU A 1 9   ? -19.831 -20.037 -9.663  1.00 29.36  ? 8   LEU A CD2 1 
ATOM   77   N N   . GLU A 1 10  ? -22.170 -19.717 -13.488 1.00 30.40  ? 9   GLU A N   1 
ATOM   78   C CA  . GLU A 1 10  ? -23.314 -19.551 -14.368 1.00 31.60  ? 9   GLU A CA  1 
ATOM   79   C C   . GLU A 1 10  ? -24.528 -19.049 -13.596 1.00 30.82  ? 9   GLU A C   1 
ATOM   80   O O   . GLU A 1 10  ? -24.519 -18.936 -12.365 1.00 32.10  ? 9   GLU A O   1 
ATOM   81   C CB  . GLU A 1 10  ? -23.643 -20.862 -15.088 1.00 30.94  ? 9   GLU A CB  1 
ATOM   82   C CG  . GLU A 1 10  ? -23.042 -20.960 -16.460 1.00 30.19  ? 9   GLU A CG  1 
ATOM   83   C CD  . GLU A 1 10  ? -23.722 -20.026 -17.470 1.00 34.65  ? 9   GLU A CD  1 
ATOM   84   O OE1 . GLU A 1 10  ? -24.588 -19.200 -17.073 1.00 29.65  ? 9   GLU A OE1 1 
ATOM   85   O OE2 . GLU A 1 10  ? -23.372 -20.127 -18.669 1.00 35.50  ? 9   GLU A OE2 1 
ATOM   86   N N   . GLY A 1 11  ? -25.584 -18.744 -14.346 1.00 33.42  ? 10  GLY A N   1 
ATOM   87   C CA  . GLY A 1 11  ? -26.837 -18.313 -13.760 1.00 31.37  ? 10  GLY A CA  1 
ATOM   88   C C   . GLY A 1 11  ? -26.953 -16.828 -13.493 1.00 33.56  ? 10  GLY A C   1 
ATOM   89   O O   . GLY A 1 11  ? -27.892 -16.414 -12.793 1.00 33.90  ? 10  GLY A O   1 
ATOM   90   N N   . GLY A 1 12  ? -26.030 -16.015 -14.012 1.00 26.41  ? 11  GLY A N   1 
ATOM   91   C CA  . GLY A 1 12  ? -26.141 -14.580 -13.924 1.00 27.13  ? 11  GLY A CA  1 
ATOM   92   C C   . GLY A 1 12  ? -27.112 -14.010 -14.951 1.00 32.97  ? 11  GLY A C   1 
ATOM   93   O O   . GLY A 1 12  ? -27.846 -14.738 -15.641 1.00 28.22  ? 11  GLY A O   1 
ATOM   94   N N   . PRO A 1 13  ? -27.150 -12.684 -15.057 1.00 30.49  ? 12  PRO A N   1 
ATOM   95   C CA  . PRO A 1 13  ? -27.956 -12.075 -16.119 1.00 27.58  ? 12  PRO A CA  1 
ATOM   96   C C   . PRO A 1 13  ? -27.385 -12.460 -17.473 1.00 29.92  ? 12  PRO A C   1 
ATOM   97   O O   . PRO A 1 13  ? -26.169 -12.478 -17.670 1.00 29.98  ? 12  PRO A O   1 
ATOM   98   C CB  . PRO A 1 13  ? -27.843 -10.567 -15.850 1.00 27.45  ? 12  PRO A CB  1 
ATOM   99   C CG  . PRO A 1 13  ? -26.561 -10.395 -15.073 1.00 27.03  ? 12  PRO A CG  1 
ATOM   100  C CD  . PRO A 1 13  ? -26.353 -11.696 -14.296 1.00 26.81  ? 12  PRO A CD  1 
ATOM   101  N N   . ARG A 1 14  ? -28.271 -12.798 -18.406 1.00 31.82  ? 13  ARG A N   1 
ATOM   102  C CA  . ARG A 1 14  ? -27.852 -13.138 -19.761 1.00 29.66  ? 13  ARG A CA  1 
ATOM   103  C C   . ARG A 1 14  ? -27.919 -11.859 -20.584 1.00 30.35  ? 13  ARG A C   1 
ATOM   104  O O   . ARG A 1 14  ? -28.987 -11.468 -21.057 1.00 30.67  ? 13  ARG A O   1 
ATOM   105  C CB  . ARG A 1 14  ? -28.718 -14.247 -20.336 1.00 31.30  ? 13  ARG A CB  1 
ATOM   106  C CG  . ARG A 1 14  ? -28.435 -14.538 -21.804 1.00 36.39  ? 13  ARG A CG  1 
ATOM   107  C CD  . ARG A 1 14  ? -29.155 -15.786 -22.288 1.00 33.01  ? 13  ARG A CD  1 
ATOM   108  N NE  . ARG A 1 14  ? -28.700 -16.969 -21.566 1.00 40.12  ? 13  ARG A NE  1 
ATOM   109  C CZ  . ARG A 1 14  ? -29.484 -17.723 -20.806 1.00 44.94  ? 13  ARG A CZ  1 
ATOM   110  N NH1 . ARG A 1 14  ? -30.775 -17.455 -20.666 1.00 37.44  ? 13  ARG A NH1 1 
ATOM   111  N NH2 . ARG A 1 14  ? -28.962 -18.778 -20.180 1.00 47.98  ? 13  ARG A NH2 1 
ATOM   112  N N   . ARG A 1 15  ? -26.771 -11.197 -20.742 1.00 27.74  ? 14  ARG A N   1 
ATOM   113  C CA  . ARG A 1 15  ? -26.711 -9.859  -21.305 1.00 27.47  ? 14  ARG A CA  1 
ATOM   114  C C   . ARG A 1 15  ? -25.439 -9.681  -22.113 1.00 29.37  ? 14  ARG A C   1 
ATOM   115  O O   . ARG A 1 15  ? -24.376 -10.214 -21.776 1.00 29.14  ? 14  ARG A O   1 
ATOM   116  C CB  . ARG A 1 15  ? -26.758 -8.774  -20.216 1.00 27.90  ? 14  ARG A CB  1 
ATOM   117  C CG  . ARG A 1 15  ? -28.086 -8.709  -19.470 1.00 31.58  ? 14  ARG A CG  1 
ATOM   118  C CD  . ARG A 1 15  ? -29.213 -8.183  -20.356 1.00 29.91  ? 14  ARG A CD  1 
ATOM   119  N NE  . ARG A 1 15  ? -30.513 -8.480  -19.772 1.00 32.70  ? 14  ARG A NE  1 
ATOM   120  C CZ  . ARG A 1 15  ? -31.087 -7.772  -18.806 1.00 32.21  ? 14  ARG A CZ  1 
ATOM   121  N NH1 . ARG A 1 15  ? -30.531 -6.668  -18.331 1.00 29.13  ? 14  ARG A NH1 1 
ATOM   122  N NH2 . ARG A 1 15  ? -32.249 -8.185  -18.303 1.00 33.69  ? 14  ARG A NH2 1 
ATOM   123  N N   . VAL A 1 16  ? -25.574 -8.914  -23.188 1.00 29.21  ? 15  VAL A N   1 
ATOM   124  C CA  . VAL A 1 16  ? -24.464 -8.374  -23.952 1.00 28.51  ? 15  VAL A CA  1 
ATOM   125  C C   . VAL A 1 16  ? -24.773 -6.895  -24.157 1.00 30.63  ? 15  VAL A C   1 
ATOM   126  O O   . VAL A 1 16  ? -25.929 -6.469  -24.086 1.00 29.74  ? 15  VAL A O   1 
ATOM   127  C CB  . VAL A 1 16  ? -24.292 -9.099  -25.301 1.00 27.66  ? 15  VAL A CB  1 
ATOM   128  C CG1 . VAL A 1 16  ? -25.577 -8.964  -26.115 1.00 29.25  ? 15  VAL A CG1 1 
ATOM   129  C CG2 . VAL A 1 16  ? -23.079 -8.567  -26.074 1.00 27.22  ? 15  VAL A CG2 1 
ATOM   130  N N   . ASN A 1 17  ? -23.723 -6.104  -24.390 1.00 29.02  ? 16  ASN A N   1 
ATOM   131  C CA  . ASN A 1 17  ? -23.868 -4.680  -24.653 1.00 28.14  ? 16  ASN A CA  1 
ATOM   132  C C   . ASN A 1 17  ? -24.443 -3.948  -23.445 1.00 29.12  ? 16  ASN A C   1 
ATOM   133  O O   . ASN A 1 17  ? -25.112 -2.918  -23.585 1.00 30.33  ? 16  ASN A O   1 
ATOM   134  C CB  . ASN A 1 17  ? -24.723 -4.438  -25.904 1.00 28.48  ? 16  ASN A CB  1 
ATOM   135  C CG  . ASN A 1 17  ? -24.364 -3.169  -26.602 1.00 29.56  ? 16  ASN A CG  1 
ATOM   136  O OD1 . ASN A 1 17  ? -23.410 -2.489  -26.214 1.00 28.90  ? 16  ASN A OD1 1 
ATOM   137  N ND2 . ASN A 1 17  ? -25.110 -2.835  -27.653 1.00 31.45  ? 16  ASN A ND2 1 
ATOM   138  N N   . HIS A 1 18  ? -24.191 -4.493  -22.256 1.00 26.52  ? 17  HIS A N   1 
ATOM   139  C CA  . HIS A 1 18  ? -24.543 -3.863  -20.993 1.00 26.42  ? 17  HIS A CA  1 
ATOM   140  C C   . HIS A 1 18  ? -23.412 -2.933  -20.547 1.00 27.58  ? 17  HIS A C   1 
ATOM   141  O O   . HIS A 1 18  ? -22.409 -2.757  -21.237 1.00 29.58  ? 17  HIS A O   1 
ATOM   142  C CB  . HIS A 1 18  ? -24.866 -4.935  -19.939 1.00 25.46  ? 17  HIS A CB  1 
ATOM   143  C CG  . HIS A 1 18  ? -23.822 -6.011  -19.807 1.00 28.75  ? 17  HIS A CG  1 
ATOM   144  N ND1 . HIS A 1 18  ? -23.392 -6.777  -20.872 1.00 27.85  ? 17  HIS A ND1 1 
ATOM   145  C CD2 . HIS A 1 18  ? -23.128 -6.453  -18.728 1.00 26.66  ? 17  HIS A CD2 1 
ATOM   146  C CE1 . HIS A 1 18  ? -22.473 -7.632  -20.457 1.00 26.76  ? 17  HIS A CE1 1 
ATOM   147  N NE2 . HIS A 1 18  ? -22.300 -7.460  -19.159 1.00 24.02  ? 17  HIS A NE2 1 
ATOM   148  N N   . ALA A 1 19  ? -23.566 -2.324  -19.376 1.00 27.46  ? 18  ALA A N   1 
ATOM   149  C CA  . ALA A 1 19  ? -22.528 -1.480  -18.806 1.00 25.79  ? 18  ALA A CA  1 
ATOM   150  C C   . ALA A 1 19  ? -22.483 -1.693  -17.298 1.00 26.62  ? 18  ALA A C   1 
ATOM   151  O O   . ALA A 1 19  ? -23.526 -1.819  -16.645 1.00 29.23  ? 18  ALA A O   1 
ATOM   152  C CB  . ALA A 1 19  ? -22.759 -0.005  -19.138 1.00 23.87  ? 18  ALA A CB  1 
ATOM   153  N N   . ALA A 1 20  ? -21.279 -1.723  -16.740 1.00 25.60  ? 19  ALA A N   1 
ATOM   154  C CA  . ALA A 1 20  ? -21.139 -2.101  -15.346 1.00 25.24  ? 19  ALA A CA  1 
ATOM   155  C C   . ALA A 1 20  ? -19.987 -1.341  -14.705 1.00 28.48  ? 19  ALA A C   1 
ATOM   156  O O   . ALA A 1 20  ? -19.008 -0.987  -15.369 1.00 24.27  ? 19  ALA A O   1 
ATOM   157  C CB  . ALA A 1 20  ? -20.929 -3.612  -15.199 1.00 24.72  ? 19  ALA A CB  1 
ATOM   158  N N   . VAL A 1 21  ? -20.120 -1.109  -13.392 1.00 28.01  ? 20  VAL A N   1 
ATOM   159  C CA  . VAL A 1 21  ? -19.076 -0.521  -12.564 1.00 26.19  ? 20  VAL A CA  1 
ATOM   160  C C   . VAL A 1 21  ? -18.918 -1.365  -11.303 1.00 25.71  ? 20  VAL A C   1 
ATOM   161  O O   . VAL A 1 21  ? -19.834 -2.070  -10.874 1.00 27.08  ? 20  VAL A O   1 
ATOM   162  C CB  . VAL A 1 21  ? -19.368 0.949   -12.185 1.00 25.16  ? 20  VAL A CB  1 
ATOM   163  C CG1 . VAL A 1 21  ? -19.351 1.838   -13.409 1.00 25.19  ? 20  VAL A CG1 1 
ATOM   164  C CG2 . VAL A 1 21  ? -20.691 1.066   -11.456 1.00 22.14  ? 20  VAL A CG2 1 
ATOM   165  N N   . ALA A 1 22  ? -17.730 -1.290  -10.717 1.00 26.29  ? 21  ALA A N   1 
ATOM   166  C CA  . ALA A 1 22  ? -17.431 -1.931  -9.442  1.00 24.79  ? 21  ALA A CA  1 
ATOM   167  C C   . ALA A 1 22  ? -17.586 -0.904  -8.324  1.00 24.27  ? 21  ALA A C   1 
ATOM   168  O O   . ALA A 1 22  ? -17.019 0.194   -8.399  1.00 22.65  ? 21  ALA A O   1 
ATOM   169  C CB  . ALA A 1 22  ? -16.017 -2.519  -9.451  1.00 19.61  ? 21  ALA A CB  1 
ATOM   170  N N   . VAL A 1 23  ? -18.382 -1.241  -7.313  1.00 22.41  ? 22  VAL A N   1 
ATOM   171  C CA  . VAL A 1 23  ? -18.509 -0.424  -6.108  1.00 22.69  ? 22  VAL A CA  1 
ATOM   172  C C   . VAL A 1 23  ? -18.013 -1.293  -4.960  1.00 25.47  ? 22  VAL A C   1 
ATOM   173  O O   . VAL A 1 23  ? -18.710 -2.222  -4.533  1.00 27.28  ? 22  VAL A O   1 
ATOM   174  C CB  . VAL A 1 23  ? -19.945 0.053   -5.854  1.00 24.45  ? 22  VAL A CB  1 
ATOM   175  C CG1 . VAL A 1 23  ? -19.985 0.846   -4.564  1.00 25.89  ? 22  VAL A CG1 1 
ATOM   176  C CG2 . VAL A 1 23  ? -20.460 0.887   -7.014  1.00 25.13  ? 22  VAL A CG2 1 
ATOM   177  N N   . GLY A 1 24  ? -16.827 -0.995  -4.449  1.00 22.84  ? 23  GLY A N   1 
ATOM   178  C CA  . GLY A 1 24  ? -16.247 -1.841  -3.420  1.00 22.71  ? 23  GLY A CA  1 
ATOM   179  C C   . GLY A 1 24  ? -15.977 -3.218  -3.978  1.00 23.75  ? 23  GLY A C   1 
ATOM   180  O O   . GLY A 1 24  ? -15.281 -3.361  -4.992  1.00 25.02  ? 23  GLY A O   1 
ATOM   181  N N   . HIS A 1 25  ? -16.544 -4.248  -3.331  1.00 25.15  ? 24  HIS A N   1 
ATOM   182  C CA  . HIS A 1 25  ? -16.444 -5.626  -3.801  1.00 23.78  ? 24  HIS A CA  1 
ATOM   183  C C   . HIS A 1 25  ? -17.721 -6.101  -4.477  1.00 23.85  ? 24  HIS A C   1 
ATOM   184  O O   . HIS A 1 25  ? -17.949 -7.307  -4.579  1.00 26.39  ? 24  HIS A O   1 
ATOM   185  C CB  . HIS A 1 25  ? -16.082 -6.559  -2.642  1.00 23.93  ? 24  HIS A CB  1 
ATOM   186  C CG  . HIS A 1 25  ? -17.010 -6.447  -1.474  1.00 26.41  ? 24  HIS A CG  1 
ATOM   187  N ND1 . HIS A 1 25  ? -18.155 -7.206  -1.354  1.00 30.64  ? 24  HIS A ND1 1 
ATOM   188  C CD2 . HIS A 1 25  ? -16.983 -5.637  -0.393  1.00 29.57  ? 24  HIS A CD2 1 
ATOM   189  C CE1 . HIS A 1 25  ? -18.791 -6.871  -0.247  1.00 29.11  ? 24  HIS A CE1 1 
ATOM   190  N NE2 . HIS A 1 25  ? -18.101 -5.919  0.354   1.00 31.06  ? 24  HIS A NE2 1 
ATOM   191  N N   . ARG A 1 26  ? -18.576 -5.189  -4.918  1.00 23.05  ? 25  ARG A N   1 
ATOM   192  C CA  . ARG A 1 26  ? -19.809 -5.560  -5.596  1.00 24.68  ? 25  ARG A CA  1 
ATOM   193  C C   . ARG A 1 26  ? -19.831 -4.905  -6.965  1.00 27.09  ? 25  ARG A C   1 
ATOM   194  O O   . ARG A 1 26  ? -19.440 -3.739  -7.115  1.00 28.12  ? 25  ARG A O   1 
ATOM   195  C CB  . ARG A 1 26  ? -21.039 -5.166  -4.769  1.00 25.28  ? 25  ARG A CB  1 
ATOM   196  C CG  . ARG A 1 26  ? -21.210 -6.070  -3.554  1.00 23.79  ? 25  ARG A CG  1 
ATOM   197  C CD  . ARG A 1 26  ? -21.930 -5.381  -2.427  1.00 25.95  ? 25  ARG A CD  1 
ATOM   198  N NE  . ARG A 1 26  ? -23.359 -5.237  -2.678  1.00 28.68  ? 25  ARG A NE  1 
ATOM   199  C CZ  . ARG A 1 26  ? -23.964 -4.071  -2.836  1.00 31.20  ? 25  ARG A CZ  1 
ATOM   200  N NH1 . ARG A 1 26  ? -23.289 -2.931  -2.778  1.00 30.18  ? 25  ARG A NH1 1 
ATOM   201  N NH2 . ARG A 1 26  ? -25.280 -4.046  -3.031  1.00 31.17  ? 25  ARG A NH2 1 
ATOM   202  N N   . VAL A 1 27  ? -20.248 -5.673  -7.967  1.00 23.81  ? 26  VAL A N   1 
ATOM   203  C CA  . VAL A 1 27  ? -20.319 -5.194  -9.340  1.00 24.40  ? 26  VAL A CA  1 
ATOM   204  C C   . VAL A 1 27  ? -21.770 -4.902  -9.668  1.00 24.96  ? 26  VAL A C   1 
ATOM   205  O O   . VAL A 1 27  ? -22.636 -5.773  -9.503  1.00 24.25  ? 26  VAL A O   1 
ATOM   206  C CB  . VAL A 1 27  ? -19.739 -6.214  -10.333 1.00 24.53  ? 26  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 27  ? -19.944 -5.713  -11.786 1.00 24.58  ? 26  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 27  ? -18.283 -6.461  -10.043 1.00 23.55  ? 26  VAL A CG2 1 
ATOM   209  N N   . TYR A 1 28  ? -22.031 -3.683  -10.142 1.00 24.51  ? 27  TYR A N   1 
ATOM   210  C CA  . TYR A 1 28  ? -23.360 -3.259  -10.577 1.00 27.09  ? 27  TYR A CA  1 
ATOM   211  C C   . TYR A 1 28  ? -23.435 -3.319  -12.103 1.00 25.90  ? 27  TYR A C   1 
ATOM   212  O O   . TYR A 1 28  ? -22.689 -2.616  -12.791 1.00 25.66  ? 27  TYR A O   1 
ATOM   213  C CB  . TYR A 1 28  ? -23.676 -1.836  -10.100 1.00 26.01  ? 27  TYR A CB  1 
ATOM   214  C CG  . TYR A 1 28  ? -23.952 -1.632  -8.615  1.00 27.69  ? 27  TYR A CG  1 
ATOM   215  C CD1 . TYR A 1 28  ? -22.980 -1.895  -7.653  1.00 26.91  ? 27  TYR A CD1 1 
ATOM   216  C CD2 . TYR A 1 28  ? -25.174 -1.111  -8.183  1.00 30.58  ? 27  TYR A CD2 1 
ATOM   217  C CE1 . TYR A 1 28  ? -23.230 -1.670  -6.298  1.00 27.64  ? 27  TYR A CE1 1 
ATOM   218  C CE2 . TYR A 1 28  ? -25.431 -0.880  -6.832  1.00 29.81  ? 27  TYR A CE2 1 
ATOM   219  C CZ  . TYR A 1 28  ? -24.449 -1.159  -5.892  1.00 29.69  ? 27  TYR A CZ  1 
ATOM   220  O OH  . TYR A 1 28  ? -24.693 -0.929  -4.552  1.00 31.40  ? 27  TYR A OH  1 
ATOM   221  N N   . SER A 1 29  ? -24.347 -4.129  -12.629 1.00 26.16  ? 28  SER A N   1 
ATOM   222  C CA  . SER A 1 29  ? -24.549 -4.241  -14.069 1.00 27.38  ? 28  SER A CA  1 
ATOM   223  C C   . SER A 1 29  ? -25.893 -3.628  -14.457 1.00 29.48  ? 28  SER A C   1 
ATOM   224  O O   . SER A 1 29  ? -26.910 -3.857  -13.780 1.00 28.25  ? 28  SER A O   1 
ATOM   225  C CB  . SER A 1 29  ? -24.486 -5.699  -14.520 1.00 25.56  ? 28  SER A CB  1 
ATOM   226  O OG  . SER A 1 29  ? -24.512 -5.774  -15.935 1.00 27.39  ? 28  SER A OG  1 
ATOM   227  N N   . PHE A 1 30  ? -25.887 -2.842  -15.543 1.00 26.35  ? 29  PHE A N   1 
ATOM   228  C CA  . PHE A 1 30  ? -27.036 -2.036  -15.960 1.00 25.70  ? 29  PHE A CA  1 
ATOM   229  C C   . PHE A 1 30  ? -27.466 -2.418  -17.368 1.00 28.18  ? 29  PHE A C   1 
ATOM   230  O O   . PHE A 1 30  ? -26.656 -2.371  -18.302 1.00 27.55  ? 29  PHE A O   1 
ATOM   231  C CB  . PHE A 1 30  ? -26.719 -0.528  -15.934 1.00 25.50  ? 29  PHE A CB  1 
ATOM   232  C CG  . PHE A 1 30  ? -26.357 -0.001  -14.573 1.00 30.53  ? 29  PHE A CG  1 
ATOM   233  C CD1 . PHE A 1 30  ? -25.054 -0.114  -14.089 1.00 26.99  ? 29  PHE A CD1 1 
ATOM   234  C CD2 . PHE A 1 30  ? -27.323 0.595   -13.765 1.00 28.76  ? 29  PHE A CD2 1 
ATOM   235  C CE1 . PHE A 1 30  ? -24.725 0.354   -12.823 1.00 27.02  ? 29  PHE A CE1 1 
ATOM   236  C CE2 . PHE A 1 30  ? -26.997 1.068   -12.508 1.00 28.49  ? 29  PHE A CE2 1 
ATOM   237  C CZ  . PHE A 1 30  ? -25.688 0.948   -12.034 1.00 28.47  ? 29  PHE A CZ  1 
ATOM   238  N N   . GLY A 1 31  ? -28.747 -2.740  -17.528 1.00 29.72  ? 30  GLY A N   1 
ATOM   239  C CA  . GLY A 1 31  ? -29.296 -2.849  -18.871 1.00 27.75  ? 30  GLY A CA  1 
ATOM   240  C C   . GLY A 1 31  ? -28.607 -3.930  -19.677 1.00 27.69  ? 30  GLY A C   1 
ATOM   241  O O   . GLY A 1 31  ? -28.217 -4.980  -19.151 1.00 25.51  ? 30  GLY A O   1 
ATOM   242  N N   . GLY A 1 32  ? -28.424 -3.658  -20.966 1.00 26.54  ? 31  GLY A N   1 
ATOM   243  C CA  . GLY A 1 32  ? -27.895 -4.635  -21.893 1.00 27.34  ? 31  GLY A CA  1 
ATOM   244  C C   . GLY A 1 32  ? -28.990 -5.258  -22.742 1.00 33.00  ? 31  GLY A C   1 
ATOM   245  O O   . GLY A 1 32  ? -30.187 -5.119  -22.480 1.00 35.38  ? 31  GLY A O   1 
ATOM   246  N N   . TYR A 1 33  ? -28.554 -5.962  -23.781 1.00 32.04  ? 32  TYR A N   1 
ATOM   247  C CA  . TYR A 1 33  ? -29.424 -6.622  -24.741 1.00 32.88  ? 32  TYR A CA  1 
ATOM   248  C C   . TYR A 1 33  ? -29.447 -8.129  -24.480 1.00 35.44  ? 32  TYR A C   1 
ATOM   249  O O   . TYR A 1 33  ? -28.530 -8.687  -23.868 1.00 31.45  ? 32  TYR A O   1 
ATOM   250  C CB  . TYR A 1 33  ? -28.950 -6.329  -26.174 1.00 32.02  ? 32  TYR A CB  1 
ATOM   251  C CG  . TYR A 1 33  ? -29.764 -7.035  -27.228 1.00 37.58  ? 32  TYR A CG  1 
ATOM   252  C CD1 . TYR A 1 33  ? -31.042 -6.589  -27.567 1.00 40.64  ? 32  TYR A CD1 1 
ATOM   253  C CD2 . TYR A 1 33  ? -29.280 -8.167  -27.859 1.00 35.67  ? 32  TYR A CD2 1 
ATOM   254  C CE1 . TYR A 1 33  ? -31.798 -7.244  -28.513 1.00 42.12  ? 32  TYR A CE1 1 
ATOM   255  C CE2 . TYR A 1 33  ? -30.030 -8.825  -28.800 1.00 40.30  ? 32  TYR A CE2 1 
ATOM   256  C CZ  . TYR A 1 33  ? -31.288 -8.361  -29.126 1.00 42.04  ? 32  TYR A CZ  1 
ATOM   257  O OH  . TYR A 1 33  ? -32.025 -9.025  -30.068 1.00 44.48  ? 32  TYR A OH  1 
ATOM   258  N N   . CYS A 1 34  ? -30.525 -8.781  -24.931 1.00 33.90  ? 33  CYS A N   1 
ATOM   259  C CA  . CYS A 1 34  ? -30.585 -10.239 -24.938 1.00 36.51  ? 33  CYS A CA  1 
ATOM   260  C C   . CYS A 1 34  ? -31.613 -10.696 -25.958 1.00 37.94  ? 33  CYS A C   1 
ATOM   261  O O   . CYS A 1 34  ? -32.747 -10.215 -25.931 1.00 43.36  ? 33  CYS A O   1 
ATOM   262  C CB  . CYS A 1 34  ? -30.942 -10.786 -23.550 1.00 38.50  ? 33  CYS A CB  1 
ATOM   263  S SG  . CYS A 1 34  ? -31.004 -12.605 -23.453 1.00 39.20  ? 33  CYS A SG  1 
ATOM   264  N N   . SER A 1 35  ? -31.234 -11.638 -26.826 1.00 36.19  ? 34  SER A N   1 
ATOM   265  C CA  . SER A 1 35  ? -32.139 -12.095 -27.882 1.00 40.54  ? 34  SER A CA  1 
ATOM   266  C C   . SER A 1 35  ? -33.401 -12.706 -27.285 1.00 41.73  ? 34  SER A C   1 
ATOM   267  O O   . SER A 1 35  ? -33.373 -13.339 -26.221 1.00 40.06  ? 34  SER A O   1 
ATOM   268  C CB  . SER A 1 35  ? -31.470 -13.135 -28.799 1.00 43.45  ? 34  SER A CB  1 
ATOM   269  O OG  . SER A 1 35  ? -30.096 -12.854 -29.050 1.00 49.39  ? 34  SER A OG  1 
ATOM   270  N N   . GLY A 1 36  ? -34.525 -12.486 -27.974 1.00 42.69  ? 35  GLY A N   1 
ATOM   271  C CA  . GLY A 1 36  ? -35.796 -13.046 -27.571 1.00 45.12  ? 35  GLY A CA  1 
ATOM   272  C C   . GLY A 1 36  ? -36.537 -12.261 -26.515 1.00 47.00  ? 35  GLY A C   1 
ATOM   273  O O   . GLY A 1 36  ? -37.738 -12.502 -26.309 1.00 53.59  ? 35  GLY A O   1 
ATOM   274  N N   . GLU A 1 37  ? -35.873 -11.328 -25.845 1.00 47.91  ? 36  GLU A N   1 
ATOM   275  C CA  . GLU A 1 37  ? -36.491 -10.499 -24.824 1.00 52.31  ? 36  GLU A CA  1 
ATOM   276  C C   . GLU A 1 37  ? -36.843 -9.148  -25.417 1.00 55.12  ? 36  GLU A C   1 
ATOM   277  O O   . GLU A 1 37  ? -36.475 -8.820  -26.547 1.00 53.18  ? 36  GLU A O   1 
ATOM   278  C CB  . GLU A 1 37  ? -35.571 -10.355 -23.616 1.00 44.96  ? 36  GLU A CB  1 
ATOM   279  C CG  . GLU A 1 37  ? -35.311 -11.707 -22.976 1.00 45.17  ? 36  GLU A CG  1 
ATOM   280  C CD  . GLU A 1 37  ? -34.337 -11.650 -21.814 1.00 46.96  ? 36  GLU A CD  1 
ATOM   281  O OE1 . GLU A 1 37  ? -34.005 -10.528 -21.367 1.00 46.14  ? 36  GLU A OE1 1 
ATOM   282  O OE2 . GLU A 1 37  ? -33.908 -12.737 -21.356 1.00 43.49  ? 36  GLU A OE2 1 
ATOM   283  N N   . ASP A 1 38  ? -37.597 -8.373  -24.657 1.00 62.66  ? 37  ASP A N   1 
ATOM   284  C CA  . ASP A 1 38  ? -38.296 -7.239  -25.234 1.00 61.44  ? 37  ASP A CA  1 
ATOM   285  C C   . ASP A 1 38  ? -37.441 -5.981  -25.126 1.00 64.27  ? 37  ASP A C   1 
ATOM   286  O O   . ASP A 1 38  ? -37.031 -5.589  -24.024 1.00 61.13  ? 37  ASP A O   1 
ATOM   287  C CB  . ASP A 1 38  ? -39.640 -7.030  -24.559 1.00 62.34  ? 37  ASP A CB  1 
ATOM   288  C CG  . ASP A 1 38  ? -40.350 -5.846  -25.116 1.00 68.98  ? 37  ASP A CG  1 
ATOM   289  O OD1 . ASP A 1 38  ? -40.727 -5.906  -26.307 1.00 72.01  ? 37  ASP A OD1 1 
ATOM   290  O OD2 . ASP A 1 38  ? -40.489 -4.846  -24.382 1.00 71.27  ? 37  ASP A OD2 1 
ATOM   291  N N   . TYR A 1 39  ? -37.172 -5.353  -26.280 1.00 62.77  ? 38  TYR A N   1 
ATOM   292  C CA  . TYR A 1 39  ? -36.432 -4.096  -26.345 1.00 59.41  ? 38  TYR A CA  1 
ATOM   293  C C   . TYR A 1 39  ? -37.196 -3.063  -27.165 1.00 64.33  ? 38  TYR A C   1 
ATOM   294  O O   . TYR A 1 39  ? -36.607 -2.082  -27.629 1.00 62.71  ? 38  TYR A O   1 
ATOM   295  C CB  . TYR A 1 39  ? -35.008 -4.327  -26.879 1.00 50.60  ? 38  TYR A CB  1 
ATOM   296  C CG  . TYR A 1 39  ? -34.190 -5.057  -25.829 1.00 52.11  ? 38  TYR A CG  1 
ATOM   297  C CD1 . TYR A 1 39  ? -34.283 -6.447  -25.683 1.00 47.50  ? 38  TYR A CD1 1 
ATOM   298  C CD2 . TYR A 1 39  ? -33.393 -4.352  -24.921 1.00 45.76  ? 38  TYR A CD2 1 
ATOM   299  C CE1 . TYR A 1 39  ? -33.590 -7.111  -24.683 1.00 45.90  ? 38  TYR A CE1 1 
ATOM   300  C CE2 . TYR A 1 39  ? -32.695 -5.010  -23.930 1.00 38.18  ? 38  TYR A CE2 1 
ATOM   301  C CZ  . TYR A 1 39  ? -32.796 -6.387  -23.814 1.00 40.90  ? 38  TYR A CZ  1 
ATOM   302  O OH  . TYR A 1 39  ? -32.109 -7.057  -22.837 1.00 38.70  ? 38  TYR A OH  1 
ATOM   303  N N   . GLU A 1 40  ? -38.508 -3.260  -27.316 1.00 67.58  ? 39  GLU A N   1 
ATOM   304  C CA  . GLU A 1 40  ? -39.404 -2.318  -27.972 1.00 69.92  ? 39  GLU A CA  1 
ATOM   305  C C   . GLU A 1 40  ? -40.273 -1.542  -26.989 1.00 71.74  ? 39  GLU A C   1 
ATOM   306  O O   . GLU A 1 40  ? -40.278 -0.310  -27.008 1.00 74.09  ? 39  GLU A O   1 
ATOM   307  C CB  . GLU A 1 40  ? -40.307 -3.045  -28.967 1.00 70.36  ? 39  GLU A CB  1 
ATOM   308  C CG  . GLU A 1 40  ? -39.575 -3.775  -30.065 1.00 75.33  ? 39  GLU A CG  1 
ATOM   309  C CD  . GLU A 1 40  ? -40.537 -4.451  -31.018 1.00 77.95  ? 39  GLU A CD  1 
ATOM   310  O OE1 . GLU A 1 40  ? -41.702 -3.994  -31.112 1.00 74.13  ? 39  GLU A OE1 1 
ATOM   311  O OE2 . GLU A 1 40  ? -40.132 -5.445  -31.659 1.00 76.70  ? 39  GLU A OE2 1 
ATOM   312  N N   . THR A 1 41  ? -41.006 -2.235  -26.123 1.00 72.97  ? 40  THR A N   1 
ATOM   313  C CA  . THR A 1 41  ? -41.989 -1.581  -25.272 1.00 76.03  ? 40  THR A CA  1 
ATOM   314  C C   . THR A 1 41  ? -41.313 -0.815  -24.125 1.00 77.55  ? 40  THR A C   1 
ATOM   315  O O   . THR A 1 41  ? -40.087 -0.797  -23.969 1.00 72.27  ? 40  THR A O   1 
ATOM   316  C CB  . THR A 1 41  ? -42.996 -2.606  -24.741 1.00 73.35  ? 40  THR A CB  1 
ATOM   317  O OG1 . THR A 1 41  ? -42.377 -3.400  -23.725 1.00 79.51  ? 40  THR A OG1 1 
ATOM   318  C CG2 . THR A 1 41  ? -43.463 -3.526  -25.854 1.00 69.83  ? 40  THR A CG2 1 
ATOM   319  N N   . LEU A 1 42  ? -42.142 -0.153  -23.319 1.00 89.06  ? 41  LEU A N   1 
ATOM   320  C CA  . LEU A 1 42  ? -41.692 0.628   -22.169 1.00 83.54  ? 41  LEU A CA  1 
ATOM   321  C C   . LEU A 1 42  ? -41.300 -0.338  -21.062 1.00 77.39  ? 41  LEU A C   1 
ATOM   322  O O   . LEU A 1 42  ? -42.155 -0.918  -20.387 1.00 79.90  ? 41  LEU A O   1 
ATOM   323  C CB  . LEU A 1 42  ? -42.791 1.584   -21.708 1.00 87.41  ? 41  LEU A CB  1 
ATOM   324  C CG  . LEU A 1 42  ? -43.297 2.572   -22.766 1.00 91.97  ? 41  LEU A CG  1 
ATOM   325  C CD1 . LEU A 1 42  ? -44.764 2.979   -22.542 1.00 82.88  ? 41  LEU A CD1 1 
ATOM   326  C CD2 . LEU A 1 42  ? -42.382 3.796   -22.825 1.00 92.45  ? 41  LEU A CD2 1 
ATOM   327  N N   . ARG A 1 43  ? -40.007 -0.531  -20.881 1.00 64.80  ? 42  ARG A N   1 
ATOM   328  C CA  . ARG A 1 43  ? -39.511 -1.256  -19.727 1.00 53.73  ? 42  ARG A CA  1 
ATOM   329  C C   . ARG A 1 43  ? -38.468 -0.404  -19.041 1.00 46.14  ? 42  ARG A C   1 
ATOM   330  O O   . ARG A 1 43  ? -37.710 0.316   -19.698 1.00 42.98  ? 42  ARG A O   1 
ATOM   331  C CB  . ARG A 1 43  ? -38.874 -2.580  -20.092 1.00 48.91  ? 42  ARG A CB  1 
ATOM   332  C CG  . ARG A 1 43  ? -39.499 -3.297  -21.231 1.00 60.44  ? 42  ARG A CG  1 
ATOM   333  C CD  . ARG A 1 43  ? -38.595 -4.434  -21.581 1.00 57.55  ? 42  ARG A CD  1 
ATOM   334  N NE  . ARG A 1 43  ? -37.982 -4.996  -20.383 1.00 49.20  ? 42  ARG A NE  1 
ATOM   335  C CZ  . ARG A 1 43  ? -37.047 -5.933  -20.398 1.00 49.44  ? 42  ARG A CZ  1 
ATOM   336  N NH1 . ARG A 1 43  ? -36.576 -6.415  -21.539 1.00 48.51  ? 42  ARG A NH1 1 
ATOM   337  N NH2 . ARG A 1 43  ? -36.577 -6.403  -19.241 1.00 46.45  ? 42  ARG A NH2 1 
ATOM   338  N N   . GLN A 1 44  ? -38.434 -0.498  -17.722 1.00 43.42  ? 43  GLN A N   1 
ATOM   339  C CA  . GLN A 1 44  ? -37.359 0.122   -16.980 1.00 39.24  ? 43  GLN A CA  1 
ATOM   340  C C   . GLN A 1 44  ? -36.046 -0.599  -17.249 1.00 37.46  ? 43  GLN A C   1 
ATOM   341  O O   . GLN A 1 44  ? -36.012 -1.811  -17.490 1.00 35.33  ? 43  GLN A O   1 
ATOM   342  C CB  . GLN A 1 44  ? -37.659 0.094   -15.492 1.00 38.11  ? 43  GLN A CB  1 
ATOM   343  C CG  . GLN A 1 44  ? -38.930 0.787   -15.107 1.00 36.55  ? 43  GLN A CG  1 
ATOM   344  C CD  . GLN A 1 44  ? -39.032 0.878   -13.614 1.00 39.78  ? 43  GLN A CD  1 
ATOM   345  O OE1 . GLN A 1 44  ? -38.150 0.395   -12.900 1.00 37.45  ? 43  GLN A OE1 1 
ATOM   346  N NE2 . GLN A 1 44  ? -40.082 1.511   -13.128 1.00 37.89  ? 43  GLN A NE2 1 
ATOM   347  N N   . ILE A 1 45  ? -34.955 0.164   -17.205 1.00 35.50  ? 44  ILE A N   1 
ATOM   348  C CA  . ILE A 1 45  ? -33.630 -0.440  -17.214 1.00 35.56  ? 44  ILE A CA  1 
ATOM   349  C C   . ILE A 1 45  ? -33.458 -1.267  -15.941 1.00 34.21  ? 44  ILE A C   1 
ATOM   350  O O   . ILE A 1 45  ? -34.196 -1.116  -14.963 1.00 31.07  ? 44  ILE A O   1 
ATOM   351  C CB  . ILE A 1 45  ? -32.502 0.609   -17.354 1.00 35.86  ? 44  ILE A CB  1 
ATOM   352  C CG1 . ILE A 1 45  ? -31.232 -0.045  -17.941 1.00 32.90  ? 44  ILE A CG1 1 
ATOM   353  C CG2 . ILE A 1 45  ? -32.227 1.301   -16.008 1.00 29.28  ? 44  ILE A CG2 1 
ATOM   354  C CD1 . ILE A 1 45  ? -30.019 0.847   -18.036 1.00 28.76  ? 44  ILE A CD1 1 
ATOM   355  N N   . ASP A 1 46  ? -32.420 -2.092  -15.953 1.00 37.35  ? 45  ASP A N   1 
ATOM   356  C CA  . ASP A 1 46  ? -32.169 -3.235  -15.095 1.00 32.84  ? 45  ASP A CA  1 
ATOM   357  C C   . ASP A 1 46  ? -30.936 -2.979  -14.234 1.00 33.35  ? 45  ASP A C   1 
ATOM   358  O O   . ASP A 1 46  ? -29.950 -2.420  -14.723 1.00 33.15  ? 45  ASP A O   1 
ATOM   359  C CB  . ASP A 1 46  ? -31.886 -4.446  -15.995 1.00 31.76  ? 45  ASP A CB  1 
ATOM   360  C CG  . ASP A 1 46  ? -32.699 -5.584  -15.631 1.00 35.85  ? 45  ASP A CG  1 
ATOM   361  O OD1 . ASP A 1 46  ? -33.488 -5.357  -14.697 1.00 41.68  ? 45  ASP A OD1 1 
ATOM   362  O OD2 . ASP A 1 46  ? -32.574 -6.659  -16.249 1.00 37.48  ? 45  ASP A OD2 1 
ATOM   363  N N   . VAL A 1 47  ? -30.943 -3.431  -12.983 1.00 28.59  ? 46  VAL A N   1 
ATOM   364  C CA  . VAL A 1 47  ? -29.718 -3.413  -12.179 1.00 28.79  ? 46  VAL A CA  1 
ATOM   365  C C   . VAL A 1 47  ? -29.547 -4.767  -11.512 1.00 28.73  ? 46  VAL A C   1 
ATOM   366  O O   . VAL A 1 47  ? -30.360 -5.143  -10.665 1.00 26.07  ? 46  VAL A O   1 
ATOM   367  C CB  . VAL A 1 47  ? -29.707 -2.325  -11.089 1.00 30.13  ? 46  VAL A CB  1 
ATOM   368  C CG1 . VAL A 1 47  ? -28.378 -2.399  -10.332 1.00 27.12  ? 46  VAL A CG1 1 
ATOM   369  C CG2 . VAL A 1 47  ? -29.945 -0.933  -11.649 1.00 28.82  ? 46  VAL A CG2 1 
ATOM   370  N N   . HIS A 1 48  ? -28.476 -5.475  -11.859 1.00 31.34  ? 47  HIS A N   1 
ATOM   371  C CA  . HIS A 1 48  ? -28.068 -6.689  -11.167 1.00 28.30  ? 47  HIS A CA  1 
ATOM   372  C C   . HIS A 1 48  ? -26.751 -6.429  -10.451 1.00 25.92  ? 47  HIS A C   1 
ATOM   373  O O   . HIS A 1 48  ? -25.901 -5.674  -10.934 1.00 28.01  ? 47  HIS A O   1 
ATOM   374  C CB  . HIS A 1 48  ? -27.895 -7.870  -12.126 1.00 24.98  ? 47  HIS A CB  1 
ATOM   375  C CG  . HIS A 1 48  ? -29.145 -8.283  -12.833 1.00 26.81  ? 47  HIS A CG  1 
ATOM   376  N ND1 . HIS A 1 48  ? -29.609 -7.642  -13.960 1.00 29.00  ? 47  HIS A ND1 1 
ATOM   377  C CD2 . HIS A 1 48  ? -30.017 -9.290  -12.587 1.00 30.30  ? 47  HIS A CD2 1 
ATOM   378  C CE1 . HIS A 1 48  ? -30.709 -8.238  -14.383 1.00 28.74  ? 47  HIS A CE1 1 
ATOM   379  N NE2 . HIS A 1 48  ? -30.984 -9.235  -13.563 1.00 30.53  ? 47  HIS A NE2 1 
ATOM   380  N N   . ILE A 1 49  ? -26.584 -7.052  -9.290  1.00 25.17  ? 48  ILE A N   1 
ATOM   381  C CA  . ILE A 1 49  ? -25.407 -6.835  -8.460  1.00 25.82  ? 48  ILE A CA  1 
ATOM   382  C C   . ILE A 1 49  ? -24.707 -8.166  -8.229  1.00 25.06  ? 48  ILE A C   1 
ATOM   383  O O   . ILE A 1 49  ? -25.308 -9.110  -7.704  1.00 24.95  ? 48  ILE A O   1 
ATOM   384  C CB  . ILE A 1 49  ? -25.771 -6.159  -7.134  1.00 25.70  ? 48  ILE A CB  1 
ATOM   385  C CG1 . ILE A 1 49  ? -26.343 -4.761  -7.417  1.00 25.66  ? 48  ILE A CG1 1 
ATOM   386  C CG2 . ILE A 1 49  ? -24.535 -6.087  -6.248  1.00 27.01  ? 48  ILE A CG2 1 
ATOM   387  C CD1 . ILE A 1 49  ? -26.948 -4.075  -6.231  1.00 26.39  ? 48  ILE A CD1 1 
ATOM   388  N N   . PHE A 1 50  ? -23.441 -8.249  -8.613  1.00 21.35  ? 49  PHE A N   1 
ATOM   389  C CA  . PHE A 1 50  ? -22.655 -9.436  -8.325  1.00 22.80  ? 49  PHE A CA  1 
ATOM   390  C C   . PHE A 1 50  ? -21.764 -9.150  -7.126  1.00 23.96  ? 49  PHE A C   1 
ATOM   391  O O   . PHE A 1 50  ? -20.991 -8.183  -7.142  1.00 24.38  ? 49  PHE A O   1 
ATOM   392  C CB  . PHE A 1 50  ? -21.821 -9.873  -9.527  1.00 24.93  ? 49  PHE A CB  1 
ATOM   393  C CG  . PHE A 1 50  ? -20.978 -11.064 -9.243  1.00 23.70  ? 49  PHE A CG  1 
ATOM   394  C CD1 . PHE A 1 50  ? -21.549 -12.334 -9.219  1.00 23.04  ? 49  PHE A CD1 1 
ATOM   395  C CD2 . PHE A 1 50  ? -19.624 -10.916 -8.936  1.00 23.21  ? 49  PHE A CD2 1 
ATOM   396  C CE1 . PHE A 1 50  ? -20.776 -13.446 -8.916  1.00 26.39  ? 49  PHE A CE1 1 
ATOM   397  C CE2 . PHE A 1 50  ? -18.831 -12.023 -8.653  1.00 23.57  ? 49  PHE A CE2 1 
ATOM   398  C CZ  . PHE A 1 50  ? -19.401 -13.288 -8.637  1.00 25.22  ? 49  PHE A CZ  1 
ATOM   399  N N   . ASN A 1 51  ? -21.894 -9.965  -6.078  1.00 23.89  ? 50  ASN A N   1 
ATOM   400  C CA  . ASN A 1 51  ? -21.065 -9.812  -4.890  1.00 24.59  ? 50  ASN A CA  1 
ATOM   401  C C   . ASN A 1 51  ? -19.802 -10.647 -5.076  1.00 24.92  ? 50  ASN A C   1 
ATOM   402  O O   . ASN A 1 51  ? -19.876 -11.876 -5.164  1.00 24.01  ? 50  ASN A O   1 
ATOM   403  C CB  . ASN A 1 51  ? -21.820 -10.232 -3.630  1.00 24.90  ? 50  ASN A CB  1 
ATOM   404  C CG  . ASN A 1 51  ? -21.055 -9.910  -2.348  1.00 25.67  ? 50  ASN A CG  1 
ATOM   405  O OD1 . ASN A 1 51  ? -19.872 -10.228 -2.203  1.00 27.19  ? 50  ASN A OD1 1 
ATOM   406  N ND2 . ASN A 1 51  ? -21.736 -9.273  -1.411  1.00 25.74  ? 50  ASN A ND2 1 
ATOM   407  N N   . ALA A 1 52  ? -18.650 -9.989  -5.128  1.00 22.62  ? 51  ALA A N   1 
ATOM   408  C CA  . ALA A 1 52  ? -17.411 -10.700 -5.443  1.00 26.18  ? 51  ALA A CA  1 
ATOM   409  C C   . ALA A 1 52  ? -16.803 -11.401 -4.236  1.00 26.08  ? 51  ALA A C   1 
ATOM   410  O O   . ALA A 1 52  ? -15.752 -12.013 -4.381  1.00 31.69  ? 51  ALA A O   1 
ATOM   411  C CB  . ALA A 1 52  ? -16.370 -9.758  -6.052  1.00 19.83  ? 51  ALA A CB  1 
ATOM   412  N N   . VAL A 1 53  ? -17.400 -11.313 -3.054  1.00 27.48  ? 52  VAL A N   1 
ATOM   413  C CA  . VAL A 1 53  ? -16.998 -12.141 -1.921  1.00 30.01  ? 52  VAL A CA  1 
ATOM   414  C C   . VAL A 1 53  ? -17.875 -13.380 -1.813  1.00 30.36  ? 52  VAL A C   1 
ATOM   415  O O   . VAL A 1 53  ? -17.371 -14.501 -1.770  1.00 32.84  ? 52  VAL A O   1 
ATOM   416  C CB  . VAL A 1 53  ? -17.011 -11.327 -0.604  1.00 31.52  ? 52  VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 53  ? -16.564 -12.197 0.542   1.00 28.75  ? 52  VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 53  ? -16.096 -10.115 -0.706  1.00 23.55  ? 52  VAL A CG2 1 
ATOM   419  N N   . SER A 1 54  ? -19.199 -13.205 -1.800  1.00 27.85  ? 53  SER A N   1 
ATOM   420  C CA  . SER A 1 54  ? -20.088 -14.358 -1.749  1.00 28.50  ? 53  SER A CA  1 
ATOM   421  C C   . SER A 1 54  ? -20.328 -14.972 -3.115  1.00 29.72  ? 53  SER A C   1 
ATOM   422  O O   . SER A 1 54  ? -20.903 -16.067 -3.189  1.00 31.01  ? 53  SER A O   1 
ATOM   423  C CB  . SER A 1 54  ? -21.431 -13.969 -1.145  1.00 26.66  ? 53  SER A CB  1 
ATOM   424  O OG  . SER A 1 54  ? -22.034 -12.989 -1.954  1.00 25.31  ? 53  SER A OG  1 
ATOM   425  N N   . LEU A 1 55  ? -19.909 -14.294 -4.185  1.00 26.51  ? 54  LEU A N   1 
ATOM   426  C CA  . LEU A 1 55  ? -20.041 -14.810 -5.549  1.00 27.09  ? 54  LEU A CA  1 
ATOM   427  C C   . LEU A 1 55  ? -21.511 -15.089 -5.906  1.00 27.93  ? 54  LEU A C   1 
ATOM   428  O O   . LEU A 1 55  ? -21.831 -16.059 -6.590  1.00 29.01  ? 54  LEU A O   1 
ATOM   429  C CB  . LEU A 1 55  ? -19.144 -16.039 -5.740  1.00 26.54  ? 54  LEU A CB  1 
ATOM   430  C CG  . LEU A 1 55  ? -17.653 -15.771 -5.358  1.00 29.44  ? 54  LEU A CG  1 
ATOM   431  C CD1 . LEU A 1 55  ? -16.800 -17.029 -5.271  1.00 21.53  ? 54  LEU A CD1 1 
ATOM   432  C CD2 . LEU A 1 55  ? -16.964 -14.758 -6.291  1.00 25.76  ? 54  LEU A CD2 1 
ATOM   433  N N   . ARG A 1 56  ? -22.410 -14.211 -5.454  1.00 23.88  ? 55  ARG A N   1 
ATOM   434  C CA  . ARG A 1 56  ? -23.836 -14.295 -5.739  1.00 24.83  ? 55  ARG A CA  1 
ATOM   435  C C   . ARG A 1 56  ? -24.283 -13.126 -6.602  1.00 26.73  ? 55  ARG A C   1 
ATOM   436  O O   . ARG A 1 56  ? -23.857 -11.985 -6.389  1.00 28.06  ? 55  ARG A O   1 
ATOM   437  C CB  . ARG A 1 56  ? -24.685 -14.281 -4.464  1.00 27.92  ? 55  ARG A CB  1 
ATOM   438  C CG  . ARG A 1 56  ? -24.304 -15.309 -3.432  1.00 29.59  ? 55  ARG A CG  1 
ATOM   439  C CD  . ARG A 1 56  ? -24.210 -16.677 -4.072  1.00 33.27  ? 55  ARG A CD  1 
ATOM   440  N NE  . ARG A 1 56  ? -25.521 -17.229 -4.408  1.00 43.04  ? 55  ARG A NE  1 
ATOM   441  C CZ  . ARG A 1 56  ? -25.703 -18.275 -5.206  1.00 41.48  ? 55  ARG A CZ  1 
ATOM   442  N NH1 . ARG A 1 56  ? -24.680 -18.850 -5.827  1.00 37.29  ? 55  ARG A NH1 1 
ATOM   443  N NH2 . ARG A 1 56  ? -26.939 -18.758 -5.382  1.00 37.21  ? 55  ARG A NH2 1 
ATOM   444  N N   . TRP A 1 57  ? -25.159 -13.412 -7.561  1.00 24.37  ? 56  TRP A N   1 
ATOM   445  C CA  . TRP A 1 57  ? -25.906 -12.367 -8.254  1.00 26.17  ? 56  TRP A CA  1 
ATOM   446  C C   . TRP A 1 57  ? -27.221 -12.113 -7.532  1.00 27.56  ? 56  TRP A C   1 
ATOM   447  O O   . TRP A 1 57  ? -27.906 -13.057 -7.123  1.00 31.30  ? 56  TRP A O   1 
ATOM   448  C CB  . TRP A 1 57  ? -26.210 -12.763 -9.698  1.00 25.21  ? 56  TRP A CB  1 
ATOM   449  C CG  . TRP A 1 57  ? -25.101 -12.569 -10.689 1.00 24.96  ? 56  TRP A CG  1 
ATOM   450  C CD1 . TRP A 1 57  ? -24.317 -13.542 -11.253 1.00 23.66  ? 56  TRP A CD1 1 
ATOM   451  C CD2 . TRP A 1 57  ? -24.683 -11.330 -11.268 1.00 24.29  ? 56  TRP A CD2 1 
ATOM   452  N NE1 . TRP A 1 57  ? -23.435 -12.975 -12.150 1.00 26.94  ? 56  TRP A NE1 1 
ATOM   453  C CE2 . TRP A 1 57  ? -23.636 -11.620 -12.172 1.00 26.04  ? 56  TRP A CE2 1 
ATOM   454  C CE3 . TRP A 1 57  ? -25.091 -9.999  -11.110 1.00 24.79  ? 56  TRP A CE3 1 
ATOM   455  C CZ2 . TRP A 1 57  ? -22.995 -10.630 -12.917 1.00 25.83  ? 56  TRP A CZ2 1 
ATOM   456  C CZ3 . TRP A 1 57  ? -24.440 -9.006  -11.843 1.00 24.30  ? 56  TRP A CZ3 1 
ATOM   457  C CH2 . TRP A 1 57  ? -23.405 -9.330  -12.734 1.00 24.01  ? 56  TRP A CH2 1 
ATOM   458  N N   . THR A 1 58  ? -27.564 -10.837 -7.372  1.00 25.17  ? 57  THR A N   1 
ATOM   459  C CA  . THR A 1 58  ? -28.895 -10.405 -6.970  1.00 27.32  ? 57  THR A CA  1 
ATOM   460  C C   . THR A 1 58  ? -29.435 -9.456  -8.029  1.00 27.91  ? 57  THR A C   1 
ATOM   461  O O   . THR A 1 58  ? -28.707 -9.023  -8.922  1.00 25.96  ? 57  THR A O   1 
ATOM   462  C CB  . THR A 1 58  ? -28.885 -9.713  -5.602  1.00 28.05  ? 57  THR A CB  1 
ATOM   463  O OG1 . THR A 1 58  ? -27.735 -8.866  -5.511  1.00 30.77  ? 57  THR A OG1 1 
ATOM   464  C CG2 . THR A 1 58  ? -28.865 -10.731 -4.468  1.00 26.33  ? 57  THR A CG2 1 
ATOM   465  N N   . LYS A 1 59  ? -30.730 -9.138  -7.936  1.00 30.58  ? 58  LYS A N   1 
ATOM   466  C CA  . LYS A 1 59  ? -31.362 -8.173  -8.831  1.00 28.25  ? 58  LYS A CA  1 
ATOM   467  C C   . LYS A 1 59  ? -32.170 -7.186  -8.004  1.00 28.06  ? 58  LYS A C   1 
ATOM   468  O O   . LYS A 1 59  ? -32.870 -7.589  -7.074  1.00 34.19  ? 58  LYS A O   1 
ATOM   469  C CB  . LYS A 1 59  ? -32.260 -8.869  -9.854  1.00 31.97  ? 58  LYS A CB  1 
ATOM   470  C CG  . LYS A 1 59  ? -33.052 -7.928  -10.767 1.00 31.82  ? 58  LYS A CG  1 
ATOM   471  C CD  . LYS A 1 59  ? -33.966 -8.732  -11.701 1.00 33.97  ? 58  LYS A CD  1 
ATOM   472  C CE  . LYS A 1 59  ? -34.444 -7.892  -12.890 1.00 35.38  ? 58  LYS A CE  1 
ATOM   473  N NZ  . LYS A 1 59  ? -35.449 -8.568  -13.762 1.00 36.79  ? 58  LYS A NZ  1 
ATOM   474  N N   . LEU A 1 60  ? -32.042 -5.896  -8.322  1.00 28.56  ? 59  LEU A N   1 
ATOM   475  C CA  . LEU A 1 60  ? -32.802 -4.847  -7.665  1.00 31.12  ? 59  LEU A CA  1 
ATOM   476  C C   . LEU A 1 60  ? -34.243 -4.840  -8.170  1.00 33.52  ? 59  LEU A C   1 
ATOM   477  O O   . LEU A 1 60  ? -34.499 -5.121  -9.346  1.00 32.71  ? 59  LEU A O   1 
ATOM   478  C CB  . LEU A 1 60  ? -32.162 -3.480  -7.906  1.00 29.19  ? 59  LEU A CB  1 
ATOM   479  C CG  . LEU A 1 60  ? -30.813 -3.231  -7.212  1.00 30.45  ? 59  LEU A CG  1 
ATOM   480  C CD1 . LEU A 1 60  ? -30.364 -1.775  -7.347  1.00 26.24  ? 59  LEU A CD1 1 
ATOM   481  C CD2 . LEU A 1 60  ? -30.867 -3.658  -5.721  1.00 31.60  ? 59  LEU A CD2 1 
ATOM   482  N N   . PRO A 1 61  ? -35.196 -4.542  -7.292  1.00 36.23  ? 60  PRO A N   1 
ATOM   483  C CA  . PRO A 1 61  ? -36.616 -4.520  -7.687  1.00 36.64  ? 60  PRO A CA  1 
ATOM   484  C C   . PRO A 1 61  ? -36.941 -3.293  -8.517  1.00 35.86  ? 60  PRO A C   1 
ATOM   485  O O   . PRO A 1 61  ? -36.200 -2.299  -8.490  1.00 33.60  ? 60  PRO A O   1 
ATOM   486  C CB  . PRO A 1 61  ? -37.349 -4.482  -6.338  1.00 32.30  ? 60  PRO A CB  1 
ATOM   487  C CG  . PRO A 1 61  ? -36.427 -3.707  -5.476  1.00 31.03  ? 60  PRO A CG  1 
ATOM   488  C CD  . PRO A 1 61  ? -35.039 -4.257  -5.857  1.00 35.97  ? 60  PRO A CD  1 
ATOM   489  N N   . PRO A 1 62  ? -38.065 -3.316  -9.232  1.00 36.76  ? 61  PRO A N   1 
ATOM   490  C CA  . PRO A 1 62  ? -38.430 -2.187  -10.097 1.00 38.95  ? 61  PRO A CA  1 
ATOM   491  C C   . PRO A 1 62  ? -38.517 -0.868  -9.336  1.00 38.02  ? 61  PRO A C   1 
ATOM   492  O O   . PRO A 1 62  ? -38.873 -0.820  -8.160  1.00 40.73  ? 61  PRO A O   1 
ATOM   493  C CB  . PRO A 1 62  ? -39.810 -2.593  -10.643 1.00 35.31  ? 61  PRO A CB  1 
ATOM   494  C CG  . PRO A 1 62  ? -39.845 -4.071  -10.545 1.00 35.09  ? 61  PRO A CG  1 
ATOM   495  C CD  . PRO A 1 62  ? -39.031 -4.427  -9.329  1.00 33.79  ? 61  PRO A CD  1 
ATOM   496  N N   . VAL A 1 63  ? -38.172 0.212   -10.029 1.00 40.95  ? 62  VAL A N   1 
ATOM   497  C CA  . VAL A 1 63  ? -38.319 1.553   -9.478  1.00 41.12  ? 62  VAL A CA  1 
ATOM   498  C C   . VAL A 1 63  ? -39.792 1.921   -9.418  1.00 44.20  ? 62  VAL A C   1 
ATOM   499  O O   . VAL A 1 63  ? -40.520 1.794   -10.410 1.00 42.93  ? 62  VAL A O   1 
ATOM   500  C CB  . VAL A 1 63  ? -37.539 2.561   -10.333 1.00 39.19  ? 62  VAL A CB  1 
ATOM   501  C CG1 . VAL A 1 63  ? -37.711 3.981   -9.784  1.00 39.22  ? 62  VAL A CG1 1 
ATOM   502  C CG2 . VAL A 1 63  ? -36.086 2.143   -10.423 1.00 37.45  ? 62  VAL A CG2 1 
ATOM   503  N N   . LYS A 1 64  ? -40.237 2.401   -8.262  1.00 51.76  ? 63  LYS A N   1 
ATOM   504  C CA  . LYS A 1 64  ? -41.613 2.842   -8.073  1.00 50.02  ? 63  LYS A CA  1 
ATOM   505  C C   . LYS A 1 64  ? -41.727 4.350   -8.231  1.00 52.67  ? 63  LYS A C   1 
ATOM   506  O O   . LYS A 1 64  ? -40.752 5.094   -8.103  1.00 51.55  ? 63  LYS A O   1 
ATOM   507  C CB  . LYS A 1 64  ? -42.138 2.441   -6.694  1.00 54.32  ? 63  LYS A CB  1 
ATOM   508  C CG  . LYS A 1 64  ? -42.874 1.117   -6.668  1.00 60.84  ? 63  LYS A CG  1 
ATOM   509  C CD  . LYS A 1 64  ? -42.316 0.232   -5.577  1.00 64.38  ? 63  LYS A CD  1 
ATOM   510  C CE  . LYS A 1 64  ? -42.310 0.959   -4.246  1.00 65.74  ? 63  LYS A CE  1 
ATOM   511  N NZ  . LYS A 1 64  ? -41.746 0.115   -3.158  1.00 73.25  ? 63  LYS A NZ  1 
ATOM   512  N N   . SER A 1 65  ? -42.946 4.796   -8.503  1.00 59.19  ? 64  SER A N   1 
ATOM   513  C CA  . SER A 1 65  ? -43.197 6.221   -8.621  1.00 60.69  ? 64  SER A CA  1 
ATOM   514  C C   . SER A 1 65  ? -42.995 6.882   -7.268  1.00 65.58  ? 64  SER A C   1 
ATOM   515  O O   . SER A 1 65  ? -43.537 6.425   -6.257  1.00 65.86  ? 64  SER A O   1 
ATOM   516  C CB  . SER A 1 65  ? -44.609 6.466   -9.135  1.00 67.90  ? 64  SER A CB  1 
ATOM   517  O OG  . SER A 1 65  ? -44.679 7.706   -9.810  1.00 77.03  ? 64  SER A OG  1 
ATOM   518  N N   . ALA A 1 66  ? -42.187 7.946   -7.247  1.00 70.75  ? 65  ALA A N   1 
ATOM   519  C CA  . ALA A 1 66  ? -41.914 8.640   -5.992  1.00 75.18  ? 65  ALA A CA  1 
ATOM   520  C C   . ALA A 1 66  ? -43.178 9.283   -5.434  1.00 79.74  ? 65  ALA A C   1 
ATOM   521  O O   . ALA A 1 66  ? -43.459 9.176   -4.236  1.00 80.50  ? 65  ALA A O   1 
ATOM   522  C CB  . ALA A 1 66  ? -40.817 9.687   -6.198  1.00 71.13  ? 65  ALA A CB  1 
ATOM   523  N N   . ILE A 1 67  ? -43.957 9.942   -6.295  1.00 84.21  ? 66  ILE A N   1 
ATOM   524  C CA  . ILE A 1 67  ? -45.238 10.545  -5.945  1.00 84.06  ? 66  ILE A CA  1 
ATOM   525  C C   . ILE A 1 67  ? -46.294 10.000  -6.898  1.00 86.34  ? 66  ILE A C   1 
ATOM   526  O O   . ILE A 1 67  ? -46.016 9.728   -8.072  1.00 81.31  ? 66  ILE A O   1 
ATOM   527  C CB  . ILE A 1 67  ? -45.193 12.095  -6.006  1.00 83.02  ? 66  ILE A CB  1 
ATOM   528  C CG1 . ILE A 1 67  ? -46.559 12.714  -5.676  1.00 86.87  ? 66  ILE A CG1 1 
ATOM   529  C CG2 . ILE A 1 67  ? -44.718 12.572  -7.374  1.00 81.46  ? 66  ILE A CG2 1 
ATOM   530  C CD1 . ILE A 1 67  ? -46.992 12.568  -4.226  1.00 81.84  ? 66  ILE A CD1 1 
ATOM   531  N N   . ARG A 1 68  ? -47.509 9.820   -6.376  1.00 90.19  ? 67  ARG A N   1 
ATOM   532  C CA  . ARG A 1 68  ? -48.625 9.415   -7.216  1.00 86.47  ? 67  ARG A CA  1 
ATOM   533  C C   . ARG A 1 68  ? -48.774 10.388  -8.379  1.00 88.31  ? 67  ARG A C   1 
ATOM   534  O O   . ARG A 1 68  ? -48.650 11.606  -8.215  1.00 82.66  ? 67  ARG A O   1 
ATOM   535  C CB  . ARG A 1 68  ? -49.914 9.356   -6.392  1.00 80.03  ? 67  ARG A CB  1 
ATOM   536  N N   . GLY A 1 69  ? -48.990 9.836   -9.571  1.00 92.40  ? 68  GLY A N   1 
ATOM   537  C CA  . GLY A 1 69  ? -49.171 10.622  -10.770 1.00 91.67  ? 68  GLY A CA  1 
ATOM   538  C C   . GLY A 1 69  ? -47.906 10.888  -11.560 1.00 95.86  ? 68  GLY A C   1 
ATOM   539  O O   . GLY A 1 69  ? -47.986 11.096  -12.779 1.00 96.03  ? 68  GLY A O   1 
ATOM   540  N N   . GLN A 1 70  ? -46.746 10.885  -10.912 1.00 85.65  ? 69  GLN A N   1 
ATOM   541  C CA  . GLN A 1 70  ? -45.490 11.046  -11.621 1.00 80.54  ? 69  GLN A CA  1 
ATOM   542  C C   . GLN A 1 70  ? -45.001 9.679   -12.077 1.00 77.32  ? 69  GLN A C   1 
ATOM   543  O O   . GLN A 1 70  ? -45.328 8.654   -11.475 1.00 77.51  ? 69  GLN A O   1 
ATOM   544  C CB  . GLN A 1 70  ? -44.441 11.725  -10.738 1.00 76.16  ? 69  GLN A CB  1 
ATOM   545  N N   . ALA A 1 71  ? -44.256 9.666   -13.169 1.00 70.85  ? 70  ALA A N   1 
ATOM   546  C CA  . ALA A 1 71  ? -43.673 8.402   -13.579 1.00 60.86  ? 70  ALA A CA  1 
ATOM   547  C C   . ALA A 1 71  ? -42.459 8.090   -12.708 1.00 60.20  ? 70  ALA A C   1 
ATOM   548  O O   . ALA A 1 71  ? -41.837 9.001   -12.158 1.00 63.50  ? 70  ALA A O   1 
ATOM   549  C CB  . ALA A 1 71  ? -43.260 8.450   -15.046 1.00 54.78  ? 70  ALA A CB  1 
ATOM   550  N N   . PRO A 1 72  ? -42.116 6.813   -12.544 1.00 55.43  ? 71  PRO A N   1 
ATOM   551  C CA  . PRO A 1 72  ? -40.847 6.486   -11.888 1.00 52.63  ? 71  PRO A CA  1 
ATOM   552  C C   . PRO A 1 72  ? -39.686 7.109   -12.647 1.00 47.52  ? 71  PRO A C   1 
ATOM   553  O O   . PRO A 1 72  ? -39.705 7.200   -13.877 1.00 46.87  ? 71  PRO A O   1 
ATOM   554  C CB  . PRO A 1 72  ? -40.798 4.953   -11.939 1.00 50.03  ? 71  PRO A CB  1 
ATOM   555  C CG  . PRO A 1 72  ? -42.223 4.530   -12.083 1.00 50.07  ? 71  PRO A CG  1 
ATOM   556  C CD  . PRO A 1 72  ? -42.901 5.609   -12.870 1.00 53.24  ? 71  PRO A CD  1 
ATOM   557  N N   . VAL A 1 73  ? -38.687 7.564   -11.896 1.00 44.03  ? 72  VAL A N   1 
ATOM   558  C CA  . VAL A 1 73  ? -37.461 8.112   -12.465 1.00 43.39  ? 72  VAL A CA  1 
ATOM   559  C C   . VAL A 1 73  ? -36.464 6.966   -12.601 1.00 41.73  ? 72  VAL A C   1 
ATOM   560  O O   . VAL A 1 73  ? -35.939 6.464   -11.603 1.00 39.08  ? 72  VAL A O   1 
ATOM   561  C CB  . VAL A 1 73  ? -36.893 9.239   -11.596 1.00 45.00  ? 72  VAL A CB  1 
ATOM   562  C CG1 . VAL A 1 73  ? -35.597 9.773   -12.187 1.00 38.82  ? 72  VAL A CG1 1 
ATOM   563  C CG2 . VAL A 1 73  ? -37.925 10.341  -11.420 1.00 38.88  ? 72  VAL A CG2 1 
ATOM   564  N N   . VAL A 1 74  ? -36.216 6.550   -13.838 1.00 38.79  ? 73  VAL A N   1 
ATOM   565  C CA  . VAL A 1 74  ? -35.322 5.443   -14.155 1.00 36.70  ? 73  VAL A CA  1 
ATOM   566  C C   . VAL A 1 74  ? -35.144 5.431   -15.672 1.00 37.77  ? 73  VAL A C   1 
ATOM   567  O O   . VAL A 1 74  ? -36.128 5.633   -16.401 1.00 39.31  ? 73  VAL A O   1 
ATOM   568  C CB  . VAL A 1 74  ? -35.893 4.118   -13.615 1.00 38.08  ? 73  VAL A CB  1 
ATOM   569  C CG1 . VAL A 1 74  ? -37.335 3.911   -14.111 1.00 38.72  ? 73  VAL A CG1 1 
ATOM   570  C CG2 . VAL A 1 74  ? -34.991 2.923   -13.976 1.00 32.90  ? 73  VAL A CG2 1 
ATOM   571  N N   . PRO A 1 75  ? -33.936 5.229   -16.201 1.00 35.19  ? 74  PRO A N   1 
ATOM   572  C CA  . PRO A 1 75  ? -33.783 5.163   -17.659 1.00 36.71  ? 74  PRO A CA  1 
ATOM   573  C C   . PRO A 1 75  ? -34.505 3.960   -18.238 1.00 37.37  ? 74  PRO A C   1 
ATOM   574  O O   . PRO A 1 75  ? -34.628 2.909   -17.604 1.00 35.18  ? 74  PRO A O   1 
ATOM   575  C CB  . PRO A 1 75  ? -32.266 5.060   -17.869 1.00 34.00  ? 74  PRO A CB  1 
ATOM   576  C CG  . PRO A 1 75  ? -31.693 4.768   -16.562 1.00 31.84  ? 74  PRO A CG  1 
ATOM   577  C CD  . PRO A 1 75  ? -32.645 5.155   -15.500 1.00 33.45  ? 74  PRO A CD  1 
ATOM   578  N N   . TYR A 1 76  ? -35.015 4.126   -19.455 1.00 38.54  ? 75  TYR A N   1 
ATOM   579  C CA  . TYR A 1 76  ? -35.634 2.980   -20.104 1.00 39.46  ? 75  TYR A CA  1 
ATOM   580  C C   . TYR A 1 76  ? -34.579 1.938   -20.504 1.00 38.83  ? 75  TYR A C   1 
ATOM   581  O O   . TYR A 1 76  ? -33.416 2.259   -20.774 1.00 33.86  ? 75  TYR A O   1 
ATOM   582  C CB  . TYR A 1 76  ? -36.486 3.414   -21.304 1.00 42.40  ? 75  TYR A CB  1 
ATOM   583  C CG  . TYR A 1 76  ? -35.815 4.165   -22.443 1.00 49.04  ? 75  TYR A CG  1 
ATOM   584  C CD1 . TYR A 1 76  ? -34.852 3.550   -23.253 1.00 48.09  ? 75  TYR A CD1 1 
ATOM   585  C CD2 . TYR A 1 76  ? -36.208 5.467   -22.767 1.00 52.88  ? 75  TYR A CD2 1 
ATOM   586  C CE1 . TYR A 1 76  ? -34.267 4.222   -24.317 1.00 50.65  ? 75  TYR A CE1 1 
ATOM   587  C CE2 . TYR A 1 76  ? -35.632 6.147   -23.834 1.00 54.45  ? 75  TYR A CE2 1 
ATOM   588  C CZ  . TYR A 1 76  ? -34.662 5.518   -24.605 1.00 58.46  ? 75  TYR A CZ  1 
ATOM   589  O OH  . TYR A 1 76  ? -34.083 6.182   -25.661 1.00 60.14  ? 75  TYR A OH  1 
ATOM   590  N N   . MET A 1 77  ? -35.008 0.673   -20.510 1.00 37.83  ? 76  MET A N   1 
ATOM   591  C CA  . MET A 1 77  ? -34.163 -0.446  -20.893 1.00 34.37  ? 76  MET A CA  1 
ATOM   592  C C   . MET A 1 77  ? -33.430 -0.149  -22.196 1.00 37.70  ? 76  MET A C   1 
ATOM   593  O O   . MET A 1 77  ? -34.035 0.268   -23.190 1.00 38.57  ? 76  MET A O   1 
ATOM   594  C CB  . MET A 1 77  ? -35.021 -1.707  -21.035 1.00 34.87  ? 76  MET A CB  1 
ATOM   595  C CG  . MET A 1 77  ? -34.237 -2.907  -21.501 1.00 38.13  ? 76  MET A CG  1 
ATOM   596  S SD  . MET A 1 77  ? -32.953 -3.236  -20.247 1.00 33.13  ? 76  MET A SD  1 
ATOM   597  C CE  . MET A 1 77  ? -33.798 -4.383  -19.191 1.00 33.85  ? 76  MET A CE  1 
ATOM   598  N N   . ARG A 1 78  ? -32.118 -0.365  -22.183 1.00 34.80  ? 77  ARG A N   1 
ATOM   599  C CA  . ARG A 1 78  ? -31.273 0.078   -23.276 1.00 33.43  ? 77  ARG A CA  1 
ATOM   600  C C   . ARG A 1 78  ? -29.994 -0.742  -23.286 1.00 34.80  ? 77  ARG A C   1 
ATOM   601  O O   . ARG A 1 78  ? -29.666 -1.451  -22.328 1.00 30.45  ? 77  ARG A O   1 
ATOM   602  C CB  . ARG A 1 78  ? -30.946 1.563   -23.147 1.00 34.32  ? 77  ARG A CB  1 
ATOM   603  C CG  . ARG A 1 78  ? -30.213 1.896   -21.870 1.00 32.85  ? 77  ARG A CG  1 
ATOM   604  C CD  . ARG A 1 78  ? -29.915 3.365   -21.811 1.00 31.82  ? 77  ARG A CD  1 
ATOM   605  N NE  . ARG A 1 78  ? -31.142 4.141   -21.713 1.00 35.46  ? 77  ARG A NE  1 
ATOM   606  C CZ  . ARG A 1 78  ? -31.189 5.465   -21.642 1.00 36.57  ? 77  ARG A CZ  1 
ATOM   607  N NH1 . ARG A 1 78  ? -30.086 6.197   -21.689 1.00 33.24  ? 77  ARG A NH1 1 
ATOM   608  N NH2 . ARG A 1 78  ? -32.371 6.067   -21.518 1.00 36.62  ? 77  ARG A NH2 1 
ATOM   609  N N   . TYR A 1 79  ? -29.271 -0.616  -24.392 1.00 33.12  ? 78  TYR A N   1 
ATOM   610  C CA  . TYR A 1 79  ? -27.991 -1.266  -24.594 1.00 30.58  ? 78  TYR A CA  1 
ATOM   611  C C   . TYR A 1 79  ? -27.076 -0.278  -25.305 1.00 31.52  ? 78  TYR A C   1 
ATOM   612  O O   . TYR A 1 79  ? -27.530 0.735   -25.844 1.00 32.45  ? 78  TYR A O   1 
ATOM   613  C CB  . TYR A 1 79  ? -28.161 -2.567  -25.392 1.00 32.34  ? 78  TYR A CB  1 
ATOM   614  C CG  . TYR A 1 79  ? -29.025 -2.410  -26.625 1.00 34.86  ? 78  TYR A CG  1 
ATOM   615  C CD1 . TYR A 1 79  ? -28.512 -1.835  -27.784 1.00 34.82  ? 78  TYR A CD1 1 
ATOM   616  C CD2 . TYR A 1 79  ? -30.361 -2.835  -26.636 1.00 36.31  ? 78  TYR A CD2 1 
ATOM   617  C CE1 . TYR A 1 79  ? -29.299 -1.684  -28.926 1.00 38.67  ? 78  TYR A CE1 1 
ATOM   618  C CE2 . TYR A 1 79  ? -31.151 -2.687  -27.776 1.00 36.55  ? 78  TYR A CE2 1 
ATOM   619  C CZ  . TYR A 1 79  ? -30.614 -2.109  -28.912 1.00 41.24  ? 78  TYR A CZ  1 
ATOM   620  O OH  . TYR A 1 79  ? -31.376 -1.950  -30.046 1.00 48.31  ? 78  TYR A OH  1 
ATOM   621  N N   . GLY A 1 80  ? -25.773 -0.562  -25.278 1.00 28.83  ? 79  GLY A N   1 
ATOM   622  C CA  . GLY A 1 80  ? -24.812 0.338   -25.875 1.00 27.76  ? 79  GLY A CA  1 
ATOM   623  C C   . GLY A 1 80  ? -24.582 1.607   -25.095 1.00 26.98  ? 79  GLY A C   1 
ATOM   624  O O   . GLY A 1 80  ? -23.911 2.509   -25.589 1.00 28.46  ? 79  GLY A O   1 
ATOM   625  N N   . HIS A 1 81  ? -25.132 1.711   -23.894 1.00 28.50  ? 80  HIS A N   1 
ATOM   626  C CA  . HIS A 1 81  ? -24.921 2.856   -23.023 1.00 29.71  ? 80  HIS A CA  1 
ATOM   627  C C   . HIS A 1 81  ? -23.576 2.722   -22.307 1.00 28.62  ? 80  HIS A C   1 
ATOM   628  O O   . HIS A 1 81  ? -22.891 1.694   -22.405 1.00 25.81  ? 80  HIS A O   1 
ATOM   629  C CB  . HIS A 1 81  ? -26.062 2.956   -22.006 1.00 28.26  ? 80  HIS A CB  1 
ATOM   630  C CG  . HIS A 1 81  ? -26.226 1.721   -21.175 1.00 28.37  ? 80  HIS A CG  1 
ATOM   631  N ND1 . HIS A 1 81  ? -26.682 0.528   -21.699 1.00 27.61  ? 80  HIS A ND1 1 
ATOM   632  C CD2 . HIS A 1 81  ? -25.973 1.485   -19.864 1.00 25.73  ? 80  HIS A CD2 1 
ATOM   633  C CE1 . HIS A 1 81  ? -26.708 -0.387  -20.745 1.00 26.47  ? 80  HIS A CE1 1 
ATOM   634  N NE2 . HIS A 1 81  ? -26.291 0.169   -19.620 1.00 27.10  ? 80  HIS A NE2 1 
ATOM   635  N N   . SER A 1 82  ? -23.208 3.766   -21.557 1.00 26.17  ? 81  SER A N   1 
ATOM   636  C CA  . SER A 1 82  ? -22.008 3.746   -20.730 1.00 24.26  ? 81  SER A CA  1 
ATOM   637  C C   . SER A 1 82  ? -22.351 4.072   -19.282 1.00 28.00  ? 81  SER A C   1 
ATOM   638  O O   . SER A 1 82  ? -23.330 4.775   -19.001 1.00 33.05  ? 81  SER A O   1 
ATOM   639  C CB  . SER A 1 82  ? -20.967 4.733   -21.235 1.00 25.97  ? 81  SER A CB  1 
ATOM   640  O OG  . SER A 1 82  ? -21.403 6.067   -21.058 1.00 29.22  ? 81  SER A OG  1 
ATOM   641  N N   . THR A 1 83  ? -21.554 3.533   -18.360 1.00 26.87  ? 82  THR A N   1 
ATOM   642  C CA  . THR A 1 83  ? -21.673 3.828   -16.934 1.00 26.12  ? 82  THR A CA  1 
ATOM   643  C C   . THR A 1 83  ? -20.293 4.094   -16.367 1.00 29.18  ? 82  THR A C   1 
ATOM   644  O O   . THR A 1 83  ? -19.364 3.315   -16.608 1.00 26.26  ? 82  THR A O   1 
ATOM   645  C CB  . THR A 1 83  ? -22.299 2.672   -16.159 1.00 26.92  ? 82  THR A CB  1 
ATOM   646  O OG1 . THR A 1 83  ? -21.533 1.474   -16.398 1.00 26.13  ? 82  THR A OG1 1 
ATOM   647  C CG2 . THR A 1 83  ? -23.743 2.467   -16.569 1.00 23.26  ? 82  THR A CG2 1 
ATOM   648  N N   . VAL A 1 84  ? -20.159 5.184   -15.612 1.00 29.67  ? 83  VAL A N   1 
ATOM   649  C CA  . VAL A 1 84  ? -18.954 5.456   -14.842 1.00 27.21  ? 83  VAL A CA  1 
ATOM   650  C C   . VAL A 1 84  ? -19.370 5.715   -13.403 1.00 27.87  ? 83  VAL A C   1 
ATOM   651  O O   . VAL A 1 84  ? -20.525 6.049   -13.118 1.00 28.99  ? 83  VAL A O   1 
ATOM   652  C CB  . VAL A 1 84  ? -18.156 6.649   -15.389 1.00 27.08  ? 83  VAL A CB  1 
ATOM   653  C CG1 . VAL A 1 84  ? -17.751 6.398   -16.841 1.00 28.27  ? 83  VAL A CG1 1 
ATOM   654  C CG2 . VAL A 1 84  ? -18.973 7.919   -15.254 1.00 27.56  ? 83  VAL A CG2 1 
ATOM   655  N N   . LEU A 1 85  ? -18.408 5.562   -12.495 1.00 24.36  ? 84  LEU A N   1 
ATOM   656  C CA  . LEU A 1 85  ? -18.611 5.787   -11.071 1.00 26.58  ? 84  LEU A CA  1 
ATOM   657  C C   . LEU A 1 85  ? -17.774 6.971   -10.618 1.00 29.82  ? 84  LEU A C   1 
ATOM   658  O O   . LEU A 1 85  ? -16.563 7.009   -10.862 1.00 32.25  ? 84  LEU A O   1 
ATOM   659  C CB  . LEU A 1 85  ? -18.228 4.546   -10.262 1.00 26.02  ? 84  LEU A CB  1 
ATOM   660  C CG  . LEU A 1 85  ? -18.322 4.692   -8.749  1.00 28.85  ? 84  LEU A CG  1 
ATOM   661  C CD1 . LEU A 1 85  ? -19.780 4.807   -8.306  1.00 26.22  ? 84  LEU A CD1 1 
ATOM   662  C CD2 . LEU A 1 85  ? -17.643 3.527   -8.068  1.00 23.09  ? 84  LEU A CD2 1 
ATOM   663  N N   . ILE A 1 86  ? -18.409 7.942   -9.971  1.00 29.36  ? 85  ILE A N   1 
ATOM   664  C CA  . ILE A 1 86  ? -17.688 9.047   -9.340  1.00 32.11  ? 85  ILE A CA  1 
ATOM   665  C C   . ILE A 1 86  ? -18.236 9.163   -7.924  1.00 34.78  ? 85  ILE A C   1 
ATOM   666  O O   . ILE A 1 86  ? -19.422 9.472   -7.734  1.00 32.42  ? 85  ILE A O   1 
ATOM   667  C CB  . ILE A 1 86  ? -17.821 10.374  -10.107 1.00 32.92  ? 85  ILE A CB  1 
ATOM   668  C CG1 . ILE A 1 86  ? -17.264 10.236  -11.543 1.00 28.88  ? 85  ILE A CG1 1 
ATOM   669  C CG2 . ILE A 1 86  ? -17.128 11.516  -9.335  1.00 26.67  ? 85  ILE A CG2 1 
ATOM   670  C CD1 . ILE A 1 86  ? -17.490 11.463  -12.416 1.00 23.25  ? 85  ILE A CD1 1 
ATOM   671  N N   . ASP A 1 87  ? -17.390 8.868   -6.937  1.00 33.60  ? 86  ASP A N   1 
ATOM   672  C CA  . ASP A 1 87  ? -17.794 8.857   -5.543  1.00 32.16  ? 86  ASP A CA  1 
ATOM   673  C C   . ASP A 1 87  ? -18.933 7.873   -5.298  1.00 30.97  ? 86  ASP A C   1 
ATOM   674  O O   . ASP A 1 87  ? -18.718 6.664   -5.405  1.00 32.68  ? 86  ASP A O   1 
ATOM   675  C CB  . ASP A 1 87  ? -18.126 10.281  -5.118  1.00 34.43  ? 86  ASP A CB  1 
ATOM   676  C CG  . ASP A 1 87  ? -16.875 11.094  -4.930  1.00 38.67  ? 86  ASP A CG  1 
ATOM   677  O OD1 . ASP A 1 87  ? -15.914 10.481  -4.423  1.00 40.53  ? 86  ASP A OD1 1 
ATOM   678  O OD2 . ASP A 1 87  ? -16.818 12.287  -5.303  1.00 38.89  ? 86  ASP A OD2 1 
ATOM   679  N N   . ASP A 1 88  ? -20.129 8.354   -4.950  1.00 27.81  ? 87  ASP A N   1 
ATOM   680  C CA  . ASP A 1 88  ? -21.249 7.474   -4.643  1.00 28.80  ? 87  ASP A CA  1 
ATOM   681  C C   . ASP A 1 88  ? -22.253 7.398   -5.783  1.00 31.18  ? 87  ASP A C   1 
ATOM   682  O O   . ASP A 1 88  ? -23.390 6.950   -5.574  1.00 31.28  ? 87  ASP A O   1 
ATOM   683  C CB  . ASP A 1 88  ? -21.959 7.922   -3.362  1.00 29.26  ? 87  ASP A CB  1 
ATOM   684  C CG  . ASP A 1 88  ? -21.135 7.682   -2.115  1.00 29.85  ? 87  ASP A CG  1 
ATOM   685  O OD1 . ASP A 1 88  ? -20.651 6.540   -1.926  1.00 26.39  ? 87  ASP A OD1 1 
ATOM   686  O OD2 . ASP A 1 88  ? -20.973 8.649   -1.322  1.00 33.38  ? 87  ASP A OD2 1 
ATOM   687  N N   . THR A 1 89  ? -21.866 7.843   -6.978  1.00 29.91  ? 88  THR A N   1 
ATOM   688  C CA  . THR A 1 89  ? -22.812 8.087   -8.058  1.00 29.87  ? 88  THR A CA  1 
ATOM   689  C C   . THR A 1 89  ? -22.347 7.388   -9.321  1.00 28.28  ? 88  THR A C   1 
ATOM   690  O O   . THR A 1 89  ? -21.250 7.660   -9.816  1.00 30.61  ? 88  THR A O   1 
ATOM   691  C CB  . THR A 1 89  ? -22.978 9.592   -8.315  1.00 30.47  ? 88  THR A CB  1 
ATOM   692  O OG1 . THR A 1 89  ? -23.443 10.230  -7.117  1.00 33.24  ? 88  THR A OG1 1 
ATOM   693  C CG2 . THR A 1 89  ? -23.967 9.841   -9.436  1.00 24.74  ? 88  THR A CG2 1 
ATOM   694  N N   . VAL A 1 90  ? -23.185 6.509   -9.848  1.00 27.24  ? 89  VAL A N   1 
ATOM   695  C CA  . VAL A 1 90  ? -23.029 6.042   -11.219 1.00 29.02  ? 89  VAL A CA  1 
ATOM   696  C C   . VAL A 1 90  ? -23.621 7.093   -12.155 1.00 29.55  ? 89  VAL A C   1 
ATOM   697  O O   . VAL A 1 90  ? -24.761 7.531   -11.971 1.00 28.27  ? 89  VAL A O   1 
ATOM   698  C CB  . VAL A 1 90  ? -23.712 4.677   -11.416 1.00 29.68  ? 89  VAL A CB  1 
ATOM   699  C CG1 . VAL A 1 90  ? -23.648 4.251   -12.883 1.00 23.61  ? 89  VAL A CG1 1 
ATOM   700  C CG2 . VAL A 1 90  ? -23.091 3.612   -10.507 1.00 28.03  ? 89  VAL A CG2 1 
ATOM   701  N N   . LEU A 1 91  ? -22.852 7.519   -13.150 1.00 28.39  ? 90  LEU A N   1 
ATOM   702  C CA  . LEU A 1 91  ? -23.390 8.330   -14.231 1.00 28.11  ? 90  LEU A CA  1 
ATOM   703  C C   . LEU A 1 91  ? -23.646 7.419   -15.419 1.00 27.94  ? 90  LEU A C   1 
ATOM   704  O O   . LEU A 1 91  ? -22.707 6.821   -15.958 1.00 31.06  ? 90  LEU A O   1 
ATOM   705  C CB  . LEU A 1 91  ? -22.439 9.464   -14.610 1.00 27.37  ? 90  LEU A CB  1 
ATOM   706  C CG  . LEU A 1 91  ? -22.307 10.416  -13.421 1.00 29.76  ? 90  LEU A CG  1 
ATOM   707  C CD1 . LEU A 1 91  ? -21.126 11.354  -13.618 1.00 26.43  ? 90  LEU A CD1 1 
ATOM   708  C CD2 . LEU A 1 91  ? -23.643 11.180  -13.144 1.00 25.41  ? 90  LEU A CD2 1 
ATOM   709  N N   . LEU A 1 92  ? -24.910 7.313   -15.822 1.00 26.76  ? 91  LEU A N   1 
ATOM   710  C CA  . LEU A 1 92  ? -25.306 6.486   -16.954 1.00 28.82  ? 91  LEU A CA  1 
ATOM   711  C C   . LEU A 1 92  ? -25.706 7.389   -18.112 1.00 30.76  ? 91  LEU A C   1 
ATOM   712  O O   . LEU A 1 92  ? -26.548 8.281   -17.946 1.00 29.56  ? 91  LEU A O   1 
ATOM   713  C CB  . LEU A 1 92  ? -26.460 5.554   -16.575 1.00 27.74  ? 91  LEU A CB  1 
ATOM   714  C CG  . LEU A 1 92  ? -26.888 4.560   -17.651 1.00 29.93  ? 91  LEU A CG  1 
ATOM   715  C CD1 . LEU A 1 92  ? -27.234 3.224   -17.016 1.00 26.49  ? 91  LEU A CD1 1 
ATOM   716  C CD2 . LEU A 1 92  ? -28.059 5.086   -18.487 1.00 28.57  ? 91  LEU A CD2 1 
ATOM   717  N N   . TRP A 1 93  ? -25.107 7.164   -19.283 1.00 31.72  ? 92  TRP A N   1 
ATOM   718  C CA  . TRP A 1 93  ? -25.407 8.015   -20.427 1.00 29.50  ? 92  TRP A CA  1 
ATOM   719  C C   . TRP A 1 93  ? -25.347 7.216   -21.720 1.00 32.27  ? 92  TRP A C   1 
ATOM   720  O O   . TRP A 1 93  ? -24.562 6.265   -21.854 1.00 30.42  ? 92  TRP A O   1 
ATOM   721  C CB  . TRP A 1 93  ? -24.443 9.206   -20.506 1.00 29.60  ? 92  TRP A CB  1 
ATOM   722  C CG  . TRP A 1 93  ? -24.805 10.194  -21.572 1.00 31.93  ? 92  TRP A CG  1 
ATOM   723  C CD1 . TRP A 1 93  ? -25.669 11.241  -21.458 1.00 32.85  ? 92  TRP A CD1 1 
ATOM   724  C CD2 . TRP A 1 93  ? -24.313 10.225  -22.924 1.00 32.08  ? 92  TRP A CD2 1 
ATOM   725  N NE1 . TRP A 1 93  ? -25.749 11.922  -22.652 1.00 31.38  ? 92  TRP A NE1 1 
ATOM   726  C CE2 . TRP A 1 93  ? -24.926 11.321  -23.566 1.00 32.04  ? 92  TRP A CE2 1 
ATOM   727  C CE3 . TRP A 1 93  ? -23.421 9.433   -23.650 1.00 29.69  ? 92  TRP A CE3 1 
ATOM   728  C CZ2 . TRP A 1 93  ? -24.670 11.648  -24.907 1.00 33.77  ? 92  TRP A CZ2 1 
ATOM   729  C CZ3 . TRP A 1 93  ? -23.174 9.753   -24.985 1.00 31.89  ? 92  TRP A CZ3 1 
ATOM   730  C CH2 . TRP A 1 93  ? -23.803 10.847  -25.599 1.00 31.16  ? 92  TRP A CH2 1 
ATOM   731  N N   . GLY A 1 94  ? -26.176 7.642   -22.689 1.00 32.67  ? 93  GLY A N   1 
ATOM   732  C CA  . GLY A 1 94  ? -26.116 7.108   -24.030 1.00 29.27  ? 93  GLY A CA  1 
ATOM   733  C C   . GLY A 1 94  ? -26.900 5.821   -24.169 1.00 31.12  ? 93  GLY A C   1 
ATOM   734  O O   . GLY A 1 94  ? -27.676 5.427   -23.301 1.00 32.52  ? 93  GLY A O   1 
ATOM   735  N N   . GLY A 1 95  ? -26.692 5.158   -25.301 1.00 32.63  ? 94  GLY A N   1 
ATOM   736  C CA  . GLY A 1 95  ? -27.399 3.927   -25.584 1.00 34.30  ? 94  GLY A CA  1 
ATOM   737  C C   . GLY A 1 95  ? -28.712 4.148   -26.308 1.00 40.00  ? 94  GLY A C   1 
ATOM   738  O O   . GLY A 1 95  ? -29.150 5.268   -26.590 1.00 40.70  ? 94  GLY A O   1 
ATOM   739  N N   . ARG A 1 96  ? -29.354 3.026   -26.607 1.00 39.40  ? 95  ARG A N   1 
ATOM   740  C CA  . ARG A 1 96  ? -30.585 3.017   -27.364 1.00 45.00  ? 95  ARG A CA  1 
ATOM   741  C C   . ARG A 1 96  ? -31.346 1.752   -27.010 1.00 45.68  ? 95  ARG A C   1 
ATOM   742  O O   . ARG A 1 96  ? -30.792 0.815   -26.430 1.00 40.36  ? 95  ARG A O   1 
ATOM   743  C CB  . ARG A 1 96  ? -30.307 3.065   -28.870 1.00 48.65  ? 95  ARG A CB  1 
ATOM   744  C CG  . ARG A 1 96  ? -29.517 1.857   -29.340 1.00 45.80  ? 95  ARG A CG  1 
ATOM   745  C CD  . ARG A 1 96  ? -29.400 1.756   -30.845 1.00 48.00  ? 95  ARG A CD  1 
ATOM   746  N NE  . ARG A 1 96  ? -30.700 1.616   -31.482 1.00 56.55  ? 95  ARG A NE  1 
ATOM   747  C CZ  . ARG A 1 96  ? -31.262 2.557   -32.226 1.00 62.85  ? 95  ARG A CZ  1 
ATOM   748  N NH1 . ARG A 1 96  ? -30.634 3.697   -32.486 1.00 64.64  ? 95  ARG A NH1 1 
ATOM   749  N NH2 . ARG A 1 96  ? -32.478 2.348   -32.724 1.00 61.74  ? 95  ARG A NH2 1 
ATOM   750  N N   . ASN A 1 97  ? -32.629 1.742   -27.350 1.00 50.68  ? 96  ASN A N   1 
ATOM   751  C CA  . ASN A 1 97  ? -33.381 0.513   -27.541 1.00 50.47  ? 96  ASN A CA  1 
ATOM   752  C C   . ASN A 1 97  ? -33.856 0.521   -28.992 1.00 55.07  ? 96  ASN A C   1 
ATOM   753  O O   . ASN A 1 97  ? -33.453 1.375   -29.776 1.00 59.88  ? 96  ASN A O   1 
ATOM   754  C CB  . ASN A 1 97  ? -34.521 0.377   -26.520 1.00 52.03  ? 96  ASN A CB  1 
ATOM   755  C CG  . ASN A 1 97  ? -35.624 1.433   -26.687 1.00 60.90  ? 96  ASN A CG  1 
ATOM   756  O OD1 . ASN A 1 97  ? -35.695 2.142   -27.688 1.00 61.94  ? 96  ASN A OD1 1 
ATOM   757  N ND2 . ASN A 1 97  ? -36.498 1.525   -25.688 1.00 60.04  ? 96  ASN A ND2 1 
ATOM   758  N N   . ASP A 1 98  ? -34.712 -0.431  -29.354 1.00 51.59  ? 97  ASP A N   1 
ATOM   759  C CA  . ASP A 1 98  ? -35.201 -0.465  -30.729 1.00 62.88  ? 97  ASP A CA  1 
ATOM   760  C C   . ASP A 1 98  ? -36.295 0.578   -30.990 1.00 69.03  ? 97  ASP A C   1 
ATOM   761  O O   . ASP A 1 98  ? -36.413 1.070   -32.118 1.00 67.74  ? 97  ASP A O   1 
ATOM   762  C CB  . ASP A 1 98  ? -35.702 -1.872  -31.077 1.00 63.14  ? 97  ASP A CB  1 
ATOM   763  C CG  . ASP A 1 98  ? -34.663 -2.964  -30.786 1.00 59.01  ? 97  ASP A CG  1 
ATOM   764  O OD1 . ASP A 1 98  ? -33.453 -2.665  -30.777 1.00 54.81  ? 97  ASP A OD1 1 
ATOM   765  O OD2 . ASP A 1 98  ? -35.063 -4.133  -30.572 1.00 59.07  ? 97  ASP A OD2 1 
ATOM   766  N N   . THR A 1 99  ? -37.094 0.936   -29.976 1.00 73.35  ? 98  THR A N   1 
ATOM   767  C CA  . THR A 1 99  ? -38.226 1.840   -30.203 1.00 75.02  ? 98  THR A CA  1 
ATOM   768  C C   . THR A 1 99  ? -37.832 3.313   -30.181 1.00 75.25  ? 98  THR A C   1 
ATOM   769  O O   . THR A 1 99  ? -37.775 3.971   -31.226 1.00 75.31  ? 98  THR A O   1 
ATOM   770  C CB  . THR A 1 99  ? -39.304 1.600   -29.141 1.00 79.87  ? 98  THR A CB  1 
ATOM   771  O OG1 . THR A 1 99  ? -39.891 0.309   -29.333 1.00 85.26  ? 98  THR A OG1 1 
ATOM   772  C CG2 . THR A 1 99  ? -40.414 2.672   -29.218 1.00 85.16  ? 98  THR A CG2 1 
ATOM   773  N N   . GLU A 1 100 ? -37.494 3.822   -28.994 1.00 76.98  ? 99  GLU A N   1 
ATOM   774  C CA  . GLU A 1 100 ? -37.268 5.247   -28.775 1.00 80.23  ? 99  GLU A CA  1 
ATOM   775  C C   . GLU A 1 100 ? -35.903 5.685   -29.286 1.00 80.79  ? 99  GLU A C   1 
ATOM   776  O O   . GLU A 1 100 ? -35.558 6.875   -29.210 1.00 77.26  ? 99  GLU A O   1 
ATOM   777  C CB  . GLU A 1 100 ? -37.456 5.561   -27.282 1.00 74.48  ? 99  GLU A CB  1 
ATOM   778  C CG  . GLU A 1 100 ? -38.852 5.133   -26.789 1.00 78.01  ? 99  GLU A CG  1 
ATOM   779  C CD  . GLU A 1 100 ? -38.988 5.078   -25.276 1.00 85.53  ? 99  GLU A CD  1 
ATOM   780  O OE1 . GLU A 1 100 ? -38.660 6.087   -24.608 1.00 86.81  ? 99  GLU A OE1 1 
ATOM   781  O OE2 . GLU A 1 100 ? -39.430 4.024   -24.756 1.00 84.27  ? 99  GLU A OE2 1 
ATOM   782  N N   . GLY A 1 101 ? -35.157 4.739   -29.850 1.00 83.96  ? 100 GLY A N   1 
ATOM   783  C CA  . GLY A 1 101 ? -33.825 5.002   -30.325 1.00 77.82  ? 100 GLY A CA  1 
ATOM   784  C C   . GLY A 1 101 ? -32.940 5.412   -29.177 1.00 77.68  ? 100 GLY A C   1 
ATOM   785  O O   . GLY A 1 101 ? -32.995 4.855   -28.069 1.00 71.34  ? 100 GLY A O   1 
ATOM   786  N N   . ALA A 1 102 ? -32.127 6.420   -29.439 1.00 86.49  ? 101 ALA A N   1 
ATOM   787  C CA  . ALA A 1 102 ? -31.158 6.904   -28.480 1.00 79.07  ? 101 ALA A CA  1 
ATOM   788  C C   . ALA A 1 102 ? -31.670 8.182   -27.818 1.00 79.57  ? 101 ALA A C   1 
ATOM   789  O O   . ALA A 1 102 ? -32.393 8.986   -28.425 1.00 81.74  ? 101 ALA A O   1 
ATOM   790  C CB  . ALA A 1 102 ? -29.812 7.130   -29.176 1.00 75.21  ? 101 ALA A CB  1 
ATOM   791  N N   . CYS A 1 103 ? -31.330 8.327   -26.542 1.00 59.35  ? 102 CYS A N   1 
ATOM   792  C CA  . CYS A 1 103 ? -31.583 9.538   -25.779 1.00 56.10  ? 102 CYS A CA  1 
ATOM   793  C C   . CYS A 1 103 ? -30.261 9.980   -25.173 1.00 44.80  ? 102 CYS A C   1 
ATOM   794  O O   . CYS A 1 103 ? -29.355 9.170   -24.963 1.00 42.75  ? 102 CYS A O   1 
ATOM   795  C CB  . CYS A 1 103 ? -32.666 9.340   -24.671 1.00 55.69  ? 102 CYS A CB  1 
ATOM   796  S SG  . CYS A 1 103 ? -32.067 9.106   -22.947 1.00 50.84  ? 102 CYS A SG  1 
ATOM   797  N N   . ASN A 1 104 ? -30.134 11.283  -24.936 1.00 40.60  ? 103 ASN A N   1 
ATOM   798  C CA  . ASN A 1 104 ? -28.902 11.826  -24.387 1.00 39.20  ? 103 ASN A CA  1 
ATOM   799  C C   . ASN A 1 104 ? -29.106 12.445  -23.008 1.00 39.09  ? 103 ASN A C   1 
ATOM   800  O O   . ASN A 1 104 ? -28.311 13.300  -22.600 1.00 36.22  ? 103 ASN A O   1 
ATOM   801  C CB  . ASN A 1 104 ? -28.288 12.834  -25.358 1.00 38.18  ? 103 ASN A CB  1 
ATOM   802  C CG  . ASN A 1 104 ? -29.208 13.988  -25.653 1.00 42.51  ? 103 ASN A CG  1 
ATOM   803  O OD1 . ASN A 1 104 ? -30.310 14.080  -25.094 1.00 42.78  ? 103 ASN A OD1 1 
ATOM   804  N ND2 . ASN A 1 104 ? -28.758 14.895  -26.526 1.00 39.14  ? 103 ASN A ND2 1 
ATOM   805  N N   . VAL A 1 105 ? -30.151 12.024  -22.284 1.00 37.39  ? 104 VAL A N   1 
ATOM   806  C CA  . VAL A 1 105 ? -30.369 12.489  -20.920 1.00 36.69  ? 104 VAL A CA  1 
ATOM   807  C C   . VAL A 1 105 ? -29.355 11.839  -19.986 1.00 37.39  ? 104 VAL A C   1 
ATOM   808  O O   . VAL A 1 105 ? -29.251 10.605  -19.922 1.00 35.40  ? 104 VAL A O   1 
ATOM   809  C CB  . VAL A 1 105 ? -31.800 12.171  -20.459 1.00 37.72  ? 104 VAL A CB  1 
ATOM   810  C CG1 . VAL A 1 105 ? -31.965 12.499  -18.982 1.00 32.90  ? 104 VAL A CG1 1 
ATOM   811  C CG2 . VAL A 1 105 ? -32.838 12.907  -21.311 1.00 37.02  ? 104 VAL A CG2 1 
ATOM   812  N N   . LEU A 1 106 ? -28.615 12.671  -19.244 1.00 38.22  ? 105 LEU A N   1 
ATOM   813  C CA  . LEU A 1 106 ? -27.735 12.174  -18.197 1.00 30.50  ? 105 LEU A CA  1 
ATOM   814  C C   . LEU A 1 106 ? -28.558 11.594  -17.053 1.00 31.04  ? 105 LEU A C   1 
ATOM   815  O O   . LEU A 1 106 ? -29.480 12.234  -16.544 1.00 35.24  ? 105 LEU A O   1 
ATOM   816  C CB  . LEU A 1 106 ? -26.829 13.288  -17.675 1.00 29.76  ? 105 LEU A CB  1 
ATOM   817  C CG  . LEU A 1 106 ? -25.904 12.833  -16.526 1.00 33.54  ? 105 LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 106 ? -24.825 11.855  -17.004 1.00 27.64  ? 105 LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 106 ? -25.273 13.996  -15.800 1.00 31.17  ? 105 LEU A CD2 1 
ATOM   820  N N   . TYR A 1 107 ? -28.221 10.379  -16.651 1.00 30.64  ? 106 TYR A N   1 
ATOM   821  C CA  . TYR A 1 107 ? -28.851 9.708   -15.531 1.00 29.97  ? 106 TYR A CA  1 
ATOM   822  C C   . TYR A 1 107 ? -27.810 9.451   -14.445 1.00 30.07  ? 106 TYR A C   1 
ATOM   823  O O   . TYR A 1 107 ? -26.667 9.055   -14.726 1.00 25.61  ? 106 TYR A O   1 
ATOM   824  C CB  . TYR A 1 107 ? -29.507 8.397   -15.975 1.00 28.61  ? 106 TYR A CB  1 
ATOM   825  C CG  . TYR A 1 107 ? -30.918 8.541   -16.511 1.00 35.06  ? 106 TYR A CG  1 
ATOM   826  C CD1 . TYR A 1 107 ? -32.003 8.486   -15.660 1.00 35.40  ? 106 TYR A CD1 1 
ATOM   827  C CD2 . TYR A 1 107 ? -31.167 8.709   -17.873 1.00 36.49  ? 106 TYR A CD2 1 
ATOM   828  C CE1 . TYR A 1 107 ? -33.304 8.600   -16.138 1.00 37.36  ? 106 TYR A CE1 1 
ATOM   829  C CE2 . TYR A 1 107 ? -32.466 8.832   -18.358 1.00 35.63  ? 106 TYR A CE2 1 
ATOM   830  C CZ  . TYR A 1 107 ? -33.532 8.778   -17.475 1.00 38.82  ? 106 TYR A CZ  1 
ATOM   831  O OH  . TYR A 1 107 ? -34.840 8.891   -17.917 1.00 40.79  ? 106 TYR A OH  1 
ATOM   832  N N   . ALA A 1 108 ? -28.208 9.703   -13.206 1.00 29.66  ? 107 ALA A N   1 
ATOM   833  C CA  . ALA A 1 108 ? -27.369 9.493   -12.043 1.00 30.74  ? 107 ALA A CA  1 
ATOM   834  C C   . ALA A 1 108 ? -28.038 8.465   -11.151 1.00 32.14  ? 107 ALA A C   1 
ATOM   835  O O   . ALA A 1 108 ? -29.261 8.492   -10.960 1.00 34.45  ? 107 ALA A O   1 
ATOM   836  C CB  . ALA A 1 108 ? -27.139 10.792  -11.278 1.00 29.04  ? 107 ALA A CB  1 
ATOM   837  N N   . PHE A 1 109 ? -27.236 7.550   -10.618 1.00 28.29  ? 108 PHE A N   1 
ATOM   838  C CA  . PHE A 1 109 ? -27.727 6.472   -9.771  1.00 29.32  ? 108 PHE A CA  1 
ATOM   839  C C   . PHE A 1 109 ? -26.883 6.412   -8.501  1.00 31.14  ? 108 PHE A C   1 
ATOM   840  O O   . PHE A 1 109 ? -25.655 6.266   -8.568  1.00 30.91  ? 108 PHE A O   1 
ATOM   841  C CB  . PHE A 1 109 ? -27.698 5.153   -10.548 1.00 27.74  ? 108 PHE A CB  1 
ATOM   842  C CG  . PHE A 1 109 ? -27.980 3.941   -9.717  1.00 30.06  ? 108 PHE A CG  1 
ATOM   843  C CD1 . PHE A 1 109 ? -29.271 3.504   -9.531  1.00 30.02  ? 108 PHE A CD1 1 
ATOM   844  C CD2 . PHE A 1 109 ? -26.935 3.213   -9.143  1.00 30.21  ? 108 PHE A CD2 1 
ATOM   845  C CE1 . PHE A 1 109 ? -29.529 2.368   -8.777  1.00 32.40  ? 108 PHE A CE1 1 
ATOM   846  C CE2 . PHE A 1 109 ? -27.182 2.085   -8.399  1.00 27.21  ? 108 PHE A CE2 1 
ATOM   847  C CZ  . PHE A 1 109 ? -28.486 1.655   -8.213  1.00 30.04  ? 108 PHE A CZ  1 
ATOM   848  N N   . ASP A 1 110 ? -27.539 6.540   -7.347  1.00 30.50  ? 109 ASP A N   1 
ATOM   849  C CA  . ASP A 1 110 ? -26.851 6.503   -6.060  1.00 30.73  ? 109 ASP A CA  1 
ATOM   850  C C   . ASP A 1 110 ? -26.632 5.054   -5.648  1.00 30.73  ? 109 ASP A C   1 
ATOM   851  O O   . ASP A 1 110 ? -27.597 4.300   -5.499  1.00 30.06  ? 109 ASP A O   1 
ATOM   852  C CB  . ASP A 1 110 ? -27.665 7.253   -5.009  1.00 29.29  ? 109 ASP A CB  1 
ATOM   853  C CG  . ASP A 1 110 ? -26.901 7.461   -3.711  1.00 31.40  ? 109 ASP A CG  1 
ATOM   854  O OD1 . ASP A 1 110 ? -26.795 6.503   -2.903  1.00 31.47  ? 109 ASP A OD1 1 
ATOM   855  O OD2 . ASP A 1 110 ? -26.407 8.591   -3.505  1.00 31.09  ? 109 ASP A OD2 1 
ATOM   856  N N   . VAL A 1 111 ? -25.370 4.660   -5.450  1.00 30.31  ? 110 VAL A N   1 
ATOM   857  C CA  . VAL A 1 111 ? -25.095 3.250   -5.203  1.00 29.32  ? 110 VAL A CA  1 
ATOM   858  C C   . VAL A 1 111 ? -25.489 2.820   -3.795  1.00 31.24  ? 110 VAL A C   1 
ATOM   859  O O   . VAL A 1 111 ? -25.571 1.615   -3.521  1.00 32.73  ? 110 VAL A O   1 
ATOM   860  C CB  . VAL A 1 111 ? -23.616 2.936   -5.483  1.00 30.08  ? 110 VAL A CB  1 
ATOM   861  C CG1 . VAL A 1 111 ? -23.275 3.346   -6.902  1.00 30.32  ? 110 VAL A CG1 1 
ATOM   862  C CG2 . VAL A 1 111 ? -22.708 3.646   -4.483  1.00 28.05  ? 110 VAL A CG2 1 
ATOM   863  N N   . ASN A 1 112 ? -25.753 3.765   -2.896  1.00 30.37  ? 111 ASN A N   1 
ATOM   864  C CA  . ASN A 1 112 ? -26.181 3.398   -1.552  1.00 31.64  ? 111 ASN A CA  1 
ATOM   865  C C   . ASN A 1 112 ? -27.699 3.415   -1.410  1.00 32.42  ? 111 ASN A C   1 
ATOM   866  O O   . ASN A 1 112 ? -28.275 2.473   -0.858  1.00 38.33  ? 111 ASN A O   1 
ATOM   867  C CB  . ASN A 1 112 ? -25.555 4.338   -0.518  1.00 33.85  ? 111 ASN A CB  1 
ATOM   868  C CG  . ASN A 1 112 ? -24.050 4.437   -0.662  1.00 31.40  ? 111 ASN A CG  1 
ATOM   869  O OD1 . ASN A 1 112 ? -23.336 3.433   -0.631  1.00 30.98  ? 111 ASN A OD1 1 
ATOM   870  N ND2 . ASN A 1 112 ? -23.564 5.654   -0.838  1.00 28.93  ? 111 ASN A ND2 1 
ATOM   871  N N   . THR A 1 113 ? -28.362 4.479   -1.878  1.00 32.54  ? 112 THR A N   1 
ATOM   872  C CA  . THR A 1 113 ? -29.819 4.545   -1.781  1.00 34.78  ? 112 THR A CA  1 
ATOM   873  C C   . THR A 1 113 ? -30.528 3.905   -2.967  1.00 32.29  ? 112 THR A C   1 
ATOM   874  O O   . THR A 1 113 ? -31.700 3.550   -2.841  1.00 29.20  ? 112 THR A O   1 
ATOM   875  C CB  . THR A 1 113 ? -30.307 5.993   -1.662  1.00 33.07  ? 112 THR A CB  1 
ATOM   876  O OG1 . THR A 1 113 ? -30.250 6.633   -2.946  1.00 30.65  ? 112 THR A OG1 1 
ATOM   877  C CG2 . THR A 1 113 ? -29.475 6.764   -0.652  1.00 29.75  ? 112 THR A CG2 1 
ATOM   878  N N   . HIS A 1 114 ? -29.843 3.738   -4.100  1.00 33.17  ? 113 HIS A N   1 
ATOM   879  C CA  . HIS A 1 114 ? -30.409 3.174   -5.324  1.00 29.21  ? 113 HIS A CA  1 
ATOM   880  C C   . HIS A 1 114 ? -31.452 4.082   -5.974  1.00 33.17  ? 113 HIS A C   1 
ATOM   881  O O   . HIS A 1 114 ? -32.237 3.618   -6.814  1.00 34.43  ? 113 HIS A O   1 
ATOM   882  C CB  . HIS A 1 114 ? -31.010 1.790   -5.074  1.00 30.41  ? 113 HIS A CB  1 
ATOM   883  C CG  . HIS A 1 114 ? -30.014 0.778   -4.595  1.00 35.38  ? 113 HIS A CG  1 
ATOM   884  N ND1 . HIS A 1 114 ? -30.385 -0.394  -3.970  1.00 35.52  ? 113 HIS A ND1 1 
ATOM   885  C CD2 . HIS A 1 114 ? -28.660 0.762   -4.652  1.00 31.43  ? 113 HIS A CD2 1 
ATOM   886  C CE1 . HIS A 1 114 ? -29.302 -1.089  -3.668  1.00 33.36  ? 113 HIS A CE1 1 
ATOM   887  N NE2 . HIS A 1 114 ? -28.245 -0.410  -4.071  1.00 31.48  ? 113 HIS A NE2 1 
ATOM   888  N N   . LYS A 1 115 ? -31.498 5.366   -5.601  1.00 32.16  ? 114 LYS A N   1 
ATOM   889  C CA  . LYS A 1 115 ? -32.404 6.299   -6.255  1.00 33.28  ? 114 LYS A CA  1 
ATOM   890  C C   . LYS A 1 115 ? -31.741 6.817   -7.527  1.00 35.97  ? 114 LYS A C   1 
ATOM   891  O O   . LYS A 1 115 ? -30.528 7.064   -7.564  1.00 34.21  ? 114 LYS A O   1 
ATOM   892  C CB  . LYS A 1 115 ? -32.796 7.460   -5.325  1.00 30.22  ? 114 LYS A CB  1 
ATOM   893  N N   . TRP A 1 116 ? -32.535 6.913   -8.588  1.00 34.46  ? 115 TRP A N   1 
ATOM   894  C CA  . TRP A 1 116 ? -32.110 7.534   -9.829  1.00 34.72  ? 115 TRP A CA  1 
ATOM   895  C C   . TRP A 1 116 ? -32.508 8.996   -9.809  1.00 36.30  ? 115 TRP A C   1 
ATOM   896  O O   . TRP A 1 116 ? -33.510 9.369   -9.196  1.00 39.05  ? 115 TRP A O   1 
ATOM   897  C CB  . TRP A 1 116 ? -32.763 6.870   -11.041 1.00 34.41  ? 115 TRP A CB  1 
ATOM   898  C CG  . TRP A 1 116 ? -32.349 5.458   -11.304 1.00 33.48  ? 115 TRP A CG  1 
ATOM   899  C CD1 . TRP A 1 116 ? -32.920 4.322   -10.792 1.00 34.80  ? 115 TRP A CD1 1 
ATOM   900  C CD2 . TRP A 1 116 ? -31.293 5.025   -12.167 1.00 31.46  ? 115 TRP A CD2 1 
ATOM   901  N NE1 . TRP A 1 116 ? -32.273 3.209   -11.278 1.00 31.71  ? 115 TRP A NE1 1 
ATOM   902  C CE2 . TRP A 1 116 ? -31.274 3.611   -12.126 1.00 28.31  ? 115 TRP A CE2 1 
ATOM   903  C CE3 . TRP A 1 116 ? -30.348 5.694   -12.956 1.00 27.66  ? 115 TRP A CE3 1 
ATOM   904  C CZ2 . TRP A 1 116 ? -30.354 2.857   -12.841 1.00 25.61  ? 115 TRP A CZ2 1 
ATOM   905  C CZ3 . TRP A 1 116 ? -29.445 4.939   -13.678 1.00 30.10  ? 115 TRP A CZ3 1 
ATOM   906  C CH2 . TRP A 1 116 ? -29.452 3.534   -13.614 1.00 27.14  ? 115 TRP A CH2 1 
ATOM   907  N N   . PHE A 1 117 ? -31.734 9.822   -10.501 1.00 35.00  ? 116 PHE A N   1 
ATOM   908  C CA  . PHE A 1 117 ? -32.168 11.185  -10.752 1.00 38.28  ? 116 PHE A CA  1 
ATOM   909  C C   . PHE A 1 117 ? -31.534 11.677  -12.052 1.00 35.69  ? 116 PHE A C   1 
ATOM   910  O O   . PHE A 1 117 ? -30.667 11.024  -12.640 1.00 36.42  ? 116 PHE A O   1 
ATOM   911  C CB  . PHE A 1 117 ? -31.893 12.109  -9.539  1.00 38.54  ? 116 PHE A CB  1 
ATOM   912  C CG  . PHE A 1 117 ? -30.475 12.096  -9.039  1.00 44.05  ? 116 PHE A CG  1 
ATOM   913  C CD1 . PHE A 1 117 ? -30.002 11.042  -8.245  1.00 46.72  ? 116 PHE A CD1 1 
ATOM   914  C CD2 . PHE A 1 117 ? -29.613 13.172  -9.315  1.00 46.83  ? 116 PHE A CD2 1 
ATOM   915  C CE1 . PHE A 1 117 ? -28.655 11.045  -7.769  1.00 49.46  ? 116 PHE A CE1 1 
ATOM   916  C CE2 . PHE A 1 117 ? -28.265 13.189  -8.841  1.00 51.49  ? 116 PHE A CE2 1 
ATOM   917  C CZ  . PHE A 1 117 ? -27.788 12.131  -8.062  1.00 44.92  ? 116 PHE A CZ  1 
ATOM   918  N N   . THR A 1 118 ? -32.021 12.815  -12.538 1.00 34.14  ? 117 THR A N   1 
ATOM   919  C CA  . THR A 1 118 ? -31.592 13.370  -13.818 1.00 34.61  ? 117 THR A CA  1 
ATOM   920  C C   . THR A 1 118 ? -31.115 14.790  -13.549 1.00 35.20  ? 117 THR A C   1 
ATOM   921  O O   . THR A 1 118 ? -31.877 15.756  -13.721 1.00 34.57  ? 117 THR A O   1 
ATOM   922  C CB  . THR A 1 118 ? -32.721 13.334  -14.859 1.00 36.42  ? 117 THR A CB  1 
ATOM   923  O OG1 . THR A 1 118 ? -33.815 14.160  -14.446 1.00 36.86  ? 117 THR A OG1 1 
ATOM   924  C CG2 . THR A 1 118 ? -33.243 11.923  -15.045 1.00 37.37  ? 117 THR A CG2 1 
ATOM   925  N N   . PRO A 1 119 ? -29.860 14.967  -13.140 1.00 34.24  ? 118 PRO A N   1 
ATOM   926  C CA  . PRO A 1 119 ? -29.374 16.316  -12.808 1.00 34.24  ? 118 PRO A CA  1 
ATOM   927  C C   . PRO A 1 119 ? -29.485 17.264  -13.991 1.00 36.45  ? 118 PRO A C   1 
ATOM   928  O O   . PRO A 1 119 ? -29.243 16.882  -15.141 1.00 37.67  ? 118 PRO A O   1 
ATOM   929  C CB  . PRO A 1 119 ? -27.914 16.083  -12.415 1.00 34.52  ? 118 PRO A CB  1 
ATOM   930  C CG  . PRO A 1 119 ? -27.563 14.749  -12.980 1.00 36.27  ? 118 PRO A CG  1 
ATOM   931  C CD  . PRO A 1 119 ? -28.809 13.943  -13.051 1.00 33.78  ? 118 PRO A CD  1 
ATOM   932  N N   . ARG A 1 120 ? -29.858 18.513  -13.706 1.00 34.21  ? 119 ARG A N   1 
ATOM   933  C CA  . ARG A 1 120 ? -29.949 19.497  -14.777 1.00 36.89  ? 119 ARG A CA  1 
ATOM   934  C C   . ARG A 1 120 ? -28.547 19.787  -15.291 1.00 37.10  ? 119 ARG A C   1 
ATOM   935  O O   . ARG A 1 120 ? -27.633 20.060  -14.510 1.00 37.96  ? 119 ARG A O   1 
ATOM   936  C CB  . ARG A 1 120 ? -30.630 20.787  -14.301 1.00 37.64  ? 119 ARG A CB  1 
ATOM   937  N N   . VAL A 1 121 ? -28.368 19.695  -16.599 1.00 35.80  ? 120 VAL A N   1 
ATOM   938  C CA  . VAL A 1 121 ? -27.077 19.942  -17.210 1.00 36.40  ? 120 VAL A CA  1 
ATOM   939  C C   . VAL A 1 121 ? -27.156 21.247  -17.985 1.00 38.95  ? 120 VAL A C   1 
ATOM   940  O O   . VAL A 1 121 ? -28.237 21.771  -18.270 1.00 37.49  ? 120 VAL A O   1 
ATOM   941  C CB  . VAL A 1 121 ? -26.644 18.787  -18.128 1.00 36.72  ? 120 VAL A CB  1 
ATOM   942  C CG1 . VAL A 1 121 ? -26.640 17.472  -17.359 1.00 34.43  ? 120 VAL A CG1 1 
ATOM   943  C CG2 . VAL A 1 121 ? -27.544 18.717  -19.344 1.00 33.81  ? 120 VAL A CG2 1 
ATOM   944  N N   . SER A 1 122 ? -25.986 21.780  -18.320 1.00 36.79  ? 121 SER A N   1 
ATOM   945  C CA  . SER A 1 122 ? -25.877 22.934  -19.197 1.00 37.31  ? 121 SER A CA  1 
ATOM   946  C C   . SER A 1 122 ? -24.726 22.679  -20.153 1.00 40.51  ? 121 SER A C   1 
ATOM   947  O O   . SER A 1 122 ? -23.980 21.700  -20.008 1.00 38.18  ? 121 SER A O   1 
ATOM   948  C CB  . SER A 1 122 ? -25.656 24.235  -18.417 1.00 38.60  ? 121 SER A CB  1 
ATOM   949  O OG  . SER A 1 122 ? -24.514 24.139  -17.587 1.00 40.35  ? 121 SER A OG  1 
ATOM   950  N N   . GLY A 1 123 ? -24.591 23.570  -21.139 1.00 39.85  ? 122 GLY A N   1 
ATOM   951  C CA  . GLY A 1 123 ? -23.552 23.441  -22.131 1.00 41.29  ? 122 GLY A CA  1 
ATOM   952  C C   . GLY A 1 123 ? -24.017 22.698  -23.364 1.00 46.17  ? 122 GLY A C   1 
ATOM   953  O O   . GLY A 1 123 ? -25.207 22.466  -23.591 1.00 45.96  ? 122 GLY A O   1 
ATOM   954  N N   . THR A 1 124 ? -23.035 22.323  -24.183 1.00 51.00  ? 123 THR A N   1 
ATOM   955  C CA  . THR A 1 124 ? -23.307 21.654  -25.454 1.00 52.23  ? 123 THR A CA  1 
ATOM   956  C C   . THR A 1 124 ? -23.464 20.154  -25.178 1.00 50.11  ? 123 THR A C   1 
ATOM   957  O O   . THR A 1 124 ? -22.479 19.421  -25.044 1.00 48.84  ? 123 THR A O   1 
ATOM   958  C CB  . THR A 1 124 ? -22.211 21.966  -26.485 1.00 52.58  ? 123 THR A CB  1 
ATOM   959  O OG1 . THR A 1 124 ? -21.195 20.959  -26.469 1.00 55.17  ? 123 THR A OG1 1 
ATOM   960  C CG2 . THR A 1 124 ? -21.548 23.320  -26.210 1.00 51.69  ? 123 THR A CG2 1 
ATOM   961  N N   . VAL A 1 125 ? -24.714 19.701  -25.094 1.00 42.81  ? 124 VAL A N   1 
ATOM   962  C CA  . VAL A 1 125 ? -25.021 18.292  -24.802 1.00 40.68  ? 124 VAL A CA  1 
ATOM   963  C C   . VAL A 1 125 ? -24.649 17.429  -26.002 1.00 39.33  ? 124 VAL A C   1 
ATOM   964  O O   . VAL A 1 125 ? -25.123 17.692  -27.121 1.00 38.04  ? 124 VAL A O   1 
ATOM   965  C CB  . VAL A 1 125 ? -26.504 18.129  -24.462 1.00 40.90  ? 124 VAL A CB  1 
ATOM   966  C CG1 . VAL A 1 125 ? -26.820 16.667  -24.171 1.00 35.97  ? 124 VAL A CG1 1 
ATOM   967  C CG2 . VAL A 1 125 ? -26.909 19.039  -23.299 1.00 37.07  ? 124 VAL A CG2 1 
ATOM   968  N N   . PRO A 1 126 ? -23.850 16.382  -25.826 1.00 38.69  ? 125 PRO A N   1 
ATOM   969  C CA  . PRO A 1 126 ? -23.553 15.498  -26.958 1.00 34.88  ? 125 PRO A CA  1 
ATOM   970  C C   . PRO A 1 126 ? -24.828 14.859  -27.491 1.00 37.33  ? 125 PRO A C   1 
ATOM   971  O O   . PRO A 1 126 ? -25.755 14.550  -26.738 1.00 38.23  ? 125 PRO A O   1 
ATOM   972  C CB  . PRO A 1 126 ? -22.606 14.444  -26.364 1.00 35.10  ? 125 PRO A CB  1 
ATOM   973  C CG  . PRO A 1 126 ? -22.359 14.837  -24.951 1.00 35.25  ? 125 PRO A CG  1 
ATOM   974  C CD  . PRO A 1 126 ? -23.402 15.822  -24.540 1.00 36.41  ? 125 PRO A CD  1 
ATOM   975  N N   . GLY A 1 127 ? -24.874 14.679  -28.808 1.00 37.62  ? 126 GLY A N   1 
ATOM   976  C CA  . GLY A 1 127 ? -26.004 14.005  -29.415 1.00 36.27  ? 126 GLY A CA  1 
ATOM   977  C C   . GLY A 1 127 ? -26.072 12.542  -29.013 1.00 38.88  ? 126 GLY A C   1 
ATOM   978  O O   . GLY A 1 127 ? -25.056 11.891  -28.740 1.00 40.53  ? 126 GLY A O   1 
ATOM   979  N N   . ALA A 1 128 ? -27.298 12.027  -28.990 1.00 41.32  ? 127 ALA A N   1 
ATOM   980  C CA  . ALA A 1 128 ? -27.552 10.657  -28.576 1.00 38.19  ? 127 ALA A CA  1 
ATOM   981  C C   . ALA A 1 128 ? -26.810 9.679   -29.472 1.00 39.92  ? 127 ALA A C   1 
ATOM   982  O O   . ALA A 1 128 ? -26.672 9.900   -30.677 1.00 40.55  ? 127 ALA A O   1 
ATOM   983  C CB  . ALA A 1 128 ? -29.049 10.386  -28.615 1.00 36.85  ? 127 ALA A CB  1 
ATOM   984  N N   . ARG A 1 129 ? -26.327 8.593   -28.875 1.00 39.04  ? 128 ARG A N   1 
ATOM   985  C CA  . ARG A 1 129 ? -25.420 7.687   -29.568 1.00 39.86  ? 128 ARG A CA  1 
ATOM   986  C C   . ARG A 1 129 ? -25.292 6.377   -28.794 1.00 35.93  ? 128 ARG A C   1 
ATOM   987  O O   . ARG A 1 129 ? -25.564 6.310   -27.591 1.00 34.89  ? 128 ARG A O   1 
ATOM   988  C CB  . ARG A 1 129 ? -24.042 8.334   -29.745 1.00 36.09  ? 128 ARG A CB  1 
ATOM   989  C CG  . ARG A 1 129 ? -23.278 8.476   -28.451 1.00 34.06  ? 128 ARG A CG  1 
ATOM   990  C CD  . ARG A 1 129 ? -22.000 9.221   -28.686 1.00 30.36  ? 128 ARG A CD  1 
ATOM   991  N NE  . ARG A 1 129 ? -22.272 10.615  -28.999 1.00 32.88  ? 128 ARG A NE  1 
ATOM   992  C CZ  . ARG A 1 129 ? -21.332 11.517  -29.220 1.00 32.62  ? 128 ARG A CZ  1 
ATOM   993  N NH1 . ARG A 1 129 ? -20.056 11.179  -29.260 1.00 35.33  ? 128 ARG A NH1 1 
ATOM   994  N NH2 . ARG A 1 129 ? -21.677 12.789  -29.383 1.00 35.52  ? 128 ARG A NH2 1 
ATOM   995  N N   . ASP A 1 130 ? -24.844 5.339   -29.492 1.00 33.98  ? 129 ASP A N   1 
ATOM   996  C CA  . ASP A 1 130 ? -24.472 4.100   -28.831 1.00 32.75  ? 129 ASP A CA  1 
ATOM   997  C C   . ASP A 1 130 ? -23.033 3.735   -29.196 1.00 31.42  ? 129 ASP A C   1 
ATOM   998  O O   . ASP A 1 130 ? -22.476 4.202   -30.195 1.00 30.10  ? 129 ASP A O   1 
ATOM   999  C CB  . ASP A 1 130 ? -25.463 2.955   -29.155 1.00 32.81  ? 129 ASP A CB  1 
ATOM   1000 C CG  . ASP A 1 130 ? -25.550 2.632   -30.642 1.00 35.24  ? 129 ASP A CG  1 
ATOM   1001 O OD1 . ASP A 1 130 ? -24.975 3.363   -31.466 1.00 39.88  ? 129 ASP A OD1 1 
ATOM   1002 O OD2 . ASP A 1 130 ? -26.194 1.626   -30.993 1.00 38.96  ? 129 ASP A OD2 1 
ATOM   1003 N N   . GLY A 1 131 ? -22.415 2.931   -28.331 1.00 30.46  ? 130 GLY A N   1 
ATOM   1004 C CA  . GLY A 1 131 ? -21.093 2.407   -28.591 1.00 29.17  ? 130 GLY A CA  1 
ATOM   1005 C C   . GLY A 1 131 ? -19.955 3.331   -28.233 1.00 30.18  ? 130 GLY A C   1 
ATOM   1006 O O   . GLY A 1 131 ? -18.796 2.991   -28.507 1.00 27.85  ? 130 GLY A O   1 
ATOM   1007 N N   . HIS A 1 132 ? -20.251 4.486   -27.646 1.00 28.67  ? 131 HIS A N   1 
ATOM   1008 C CA  . HIS A 1 132 ? -19.242 5.406   -27.165 1.00 26.50  ? 131 HIS A CA  1 
ATOM   1009 C C   . HIS A 1 132 ? -18.453 4.790   -26.005 1.00 28.30  ? 131 HIS A C   1 
ATOM   1010 O O   . HIS A 1 132 ? -18.778 3.719   -25.472 1.00 26.26  ? 131 HIS A O   1 
ATOM   1011 C CB  . HIS A 1 132 ? -19.904 6.698   -26.705 1.00 27.22  ? 131 HIS A CB  1 
ATOM   1012 C CG  . HIS A 1 132 ? -20.971 6.471   -25.681 1.00 30.62  ? 131 HIS A CG  1 
ATOM   1013 N ND1 . HIS A 1 132 ? -22.128 5.772   -25.959 1.00 27.54  ? 131 HIS A ND1 1 
ATOM   1014 C CD2 . HIS A 1 132 ? -21.037 6.810   -24.370 1.00 28.97  ? 131 HIS A CD2 1 
ATOM   1015 C CE1 . HIS A 1 132 ? -22.870 5.709   -24.865 1.00 30.68  ? 131 HIS A CE1 1 
ATOM   1016 N NE2 . HIS A 1 132 ? -22.233 6.333   -23.889 1.00 29.02  ? 131 HIS A NE2 1 
ATOM   1017 N N   . SER A 1 133 ? -17.382 5.484   -25.631 1.00 29.32  ? 132 SER A N   1 
ATOM   1018 C CA  . SER A 1 133 ? -16.614 5.179   -24.435 1.00 25.45  ? 132 SER A CA  1 
ATOM   1019 C C   . SER A 1 133 ? -16.819 6.286   -23.414 1.00 26.76  ? 132 SER A C   1 
ATOM   1020 O O   . SER A 1 133 ? -17.027 7.451   -23.764 1.00 26.40  ? 132 SER A O   1 
ATOM   1021 C CB  . SER A 1 133 ? -15.124 5.037   -24.746 1.00 25.70  ? 132 SER A CB  1 
ATOM   1022 O OG  . SER A 1 133 ? -14.620 6.212   -25.363 1.00 27.84  ? 132 SER A OG  1 
ATOM   1023 N N   . ALA A 1 134 ? -16.784 5.914   -22.141 1.00 27.48  ? 133 ALA A N   1 
ATOM   1024 C CA  . ALA A 1 134 ? -16.825 6.908   -21.086 1.00 25.20  ? 133 ALA A CA  1 
ATOM   1025 C C   . ALA A 1 134 ? -15.777 6.546   -20.063 1.00 26.21  ? 133 ALA A C   1 
ATOM   1026 O O   . ALA A 1 134 ? -15.541 5.362   -19.796 1.00 29.30  ? 133 ALA A O   1 
ATOM   1027 C CB  . ALA A 1 134 ? -18.203 6.996   -20.420 1.00 27.10  ? 133 ALA A CB  1 
ATOM   1028 N N   . CYS A 1 135 ? -15.151 7.572   -19.509 1.00 23.65  ? 134 CYS A N   1 
ATOM   1029 C CA  . CYS A 1 135 ? -14.168 7.389   -18.462 1.00 24.68  ? 134 CYS A CA  1 
ATOM   1030 C C   . CYS A 1 135 ? -14.079 8.704   -17.713 1.00 28.74  ? 134 CYS A C   1 
ATOM   1031 O O   . CYS A 1 135 ? -14.616 9.723   -18.157 1.00 29.11  ? 134 CYS A O   1 
ATOM   1032 C CB  . CYS A 1 135 ? -12.816 6.947   -19.031 1.00 29.09  ? 134 CYS A CB  1 
ATOM   1033 S SG  . CYS A 1 135 ? -12.094 8.089   -20.209 1.00 32.81  ? 134 CYS A SG  1 
ATOM   1034 N N   . VAL A 1 136 ? -13.434 8.665   -16.541 1.00 27.66  ? 135 VAL A N   1 
ATOM   1035 C CA  . VAL A 1 136 ? -13.439 9.809   -15.642 1.00 30.20  ? 135 VAL A CA  1 
ATOM   1036 C C   . VAL A 1 136 ? -12.028 10.108  -15.159 1.00 30.15  ? 135 VAL A C   1 
ATOM   1037 O O   . VAL A 1 136 ? -11.157 9.238   -15.102 1.00 29.88  ? 135 VAL A O   1 
ATOM   1038 C CB  . VAL A 1 136 ? -14.377 9.614   -14.420 1.00 26.77  ? 135 VAL A CB  1 
ATOM   1039 C CG1 . VAL A 1 136 ? -15.741 9.148   -14.856 1.00 27.83  ? 135 VAL A CG1 1 
ATOM   1040 C CG2 . VAL A 1 136 ? -13.785 8.653   -13.437 1.00 27.77  ? 135 VAL A CG2 1 
ATOM   1041 N N   . LEU A 1 137 ? -11.827 11.368  -14.788 1.00 31.50  ? 136 LEU A N   1 
ATOM   1042 C CA  . LEU A 1 137 ? -10.635 11.820  -14.075 1.00 30.93  ? 136 LEU A CA  1 
ATOM   1043 C C   . LEU A 1 137 ? -11.103 12.873  -13.084 1.00 31.79  ? 136 LEU A C   1 
ATOM   1044 O O   . LEU A 1 137 ? -11.496 13.973  -13.489 1.00 31.79  ? 136 LEU A O   1 
ATOM   1045 C CB  . LEU A 1 137 ? -9.587  12.387  -15.028 1.00 32.13  ? 136 LEU A CB  1 
ATOM   1046 C CG  . LEU A 1 137 ? -8.330  12.952  -14.389 1.00 26.58  ? 136 LEU A CG  1 
ATOM   1047 C CD1 . LEU A 1 137 ? -7.524  11.836  -13.756 1.00 26.89  ? 136 LEU A CD1 1 
ATOM   1048 C CD2 . LEU A 1 137 ? -7.534  13.666  -15.451 1.00 29.19  ? 136 LEU A CD2 1 
ATOM   1049 N N   . GLY A 1 138 ? -11.074 12.536  -11.799 1.00 29.42  ? 137 GLY A N   1 
ATOM   1050 C CA  . GLY A 1 138 ? -11.612 13.445  -10.815 1.00 28.51  ? 137 GLY A CA  1 
ATOM   1051 C C   . GLY A 1 138 ? -13.108 13.544  -10.979 1.00 31.65  ? 137 GLY A C   1 
ATOM   1052 O O   . GLY A 1 138 ? -13.822 12.538  -11.004 1.00 33.08  ? 137 GLY A O   1 
ATOM   1053 N N   . LYS A 1 139 ? -13.602 14.763  -11.091 1.00 32.00  ? 138 LYS A N   1 
ATOM   1054 C CA  . LYS A 1 139 ? -15.029 14.979  -11.261 1.00 34.50  ? 138 LYS A CA  1 
ATOM   1055 C C   . LYS A 1 139 ? -15.438 15.084  -12.730 1.00 34.56  ? 138 LYS A C   1 
ATOM   1056 O O   . LYS A 1 139 ? -16.607 15.385  -13.016 1.00 35.26  ? 138 LYS A O   1 
ATOM   1057 C CB  . LYS A 1 139 ? -15.455 16.235  -10.495 1.00 33.76  ? 138 LYS A CB  1 
ATOM   1058 C CG  . LYS A 1 139 ? -15.086 16.201  -9.018  1.00 34.44  ? 138 LYS A CG  1 
ATOM   1059 C CD  . LYS A 1 139 ? -15.990 15.274  -8.232  1.00 36.04  ? 138 LYS A CD  1 
ATOM   1060 C CE  . LYS A 1 139 ? -15.429 14.971  -6.848  1.00 44.92  ? 138 LYS A CE  1 
ATOM   1061 N NZ  . LYS A 1 139 ? -14.270 14.000  -6.896  1.00 49.29  ? 138 LYS A NZ  1 
ATOM   1062 N N   . ILE A 1 140 ? -14.510 14.852  -13.664 1.00 28.78  ? 139 ILE A N   1 
ATOM   1063 C CA  . ILE A 1 140 ? -14.772 15.024  -15.093 1.00 32.86  ? 139 ILE A CA  1 
ATOM   1064 C C   . ILE A 1 140 ? -15.017 13.665  -15.734 1.00 32.33  ? 139 ILE A C   1 
ATOM   1065 O O   . ILE A 1 140 ? -14.176 12.762  -15.625 1.00 31.69  ? 139 ILE A O   1 
ATOM   1066 C CB  . ILE A 1 140 ? -13.607 15.728  -15.809 1.00 33.01  ? 139 ILE A CB  1 
ATOM   1067 C CG1 . ILE A 1 140 ? -13.168 16.988  -15.066 1.00 31.41  ? 139 ILE A CG1 1 
ATOM   1068 C CG2 . ILE A 1 140 ? -14.000 16.017  -17.261 1.00 31.82  ? 139 ILE A CG2 1 
ATOM   1069 C CD1 . ILE A 1 140 ? -14.238 18.013  -14.934 1.00 32.91  ? 139 ILE A CD1 1 
ATOM   1070 N N   . MET A 1 141 ? -16.143 13.536  -16.438 1.00 28.86  ? 140 MET A N   1 
ATOM   1071 C CA  . MET A 1 141 ? -16.425 12.394  -17.297 1.00 28.98  ? 140 MET A CA  1 
ATOM   1072 C C   . MET A 1 141 ? -16.058 12.751  -18.738 1.00 30.46  ? 140 MET A C   1 
ATOM   1073 O O   . MET A 1 141 ? -16.372 13.850  -19.205 1.00 30.20  ? 140 MET A O   1 
ATOM   1074 C CB  . MET A 1 141 ? -17.897 11.995  -17.201 1.00 28.45  ? 140 MET A CB  1 
ATOM   1075 C CG  . MET A 1 141 ? -18.274 10.792  -18.054 1.00 28.22  ? 140 MET A CG  1 
ATOM   1076 S SD  . MET A 1 141 ? -19.997 10.292  -17.834 1.00 32.43  ? 140 MET A SD  1 
ATOM   1077 C CE  . MET A 1 141 ? -20.865 11.606  -18.746 1.00 27.04  ? 140 MET A CE  1 
ATOM   1078 N N   . TYR A 1 142 ? -15.379 11.841  -19.433 1.00 26.09  ? 141 TYR A N   1 
ATOM   1079 C CA  . TYR A 1 142 ? -15.028 12.048  -20.829 1.00 28.23  ? 141 TYR A CA  1 
ATOM   1080 C C   . TYR A 1 142 ? -15.751 11.031  -21.705 1.00 30.28  ? 141 TYR A C   1 
ATOM   1081 O O   . TYR A 1 142 ? -15.564 9.819   -21.538 1.00 26.83  ? 141 TYR A O   1 
ATOM   1082 C CB  . TYR A 1 142 ? -13.520 11.949  -21.043 1.00 30.65  ? 141 TYR A CB  1 
ATOM   1083 C CG  . TYR A 1 142 ? -12.722 13.019  -20.337 1.00 30.51  ? 141 TYR A CG  1 
ATOM   1084 C CD1 . TYR A 1 142 ? -12.285 12.825  -19.027 1.00 29.09  ? 141 TYR A CD1 1 
ATOM   1085 C CD2 . TYR A 1 142 ? -12.391 14.219  -20.981 1.00 30.89  ? 141 TYR A CD2 1 
ATOM   1086 C CE1 . TYR A 1 142 ? -11.546 13.790  -18.364 1.00 30.28  ? 141 TYR A CE1 1 
ATOM   1087 C CE2 . TYR A 1 142 ? -11.636 15.205  -20.318 1.00 33.39  ? 141 TYR A CE2 1 
ATOM   1088 C CZ  . TYR A 1 142 ? -11.225 14.969  -19.009 1.00 31.10  ? 141 TYR A CZ  1 
ATOM   1089 O OH  . TYR A 1 142 ? -10.492 15.899  -18.333 1.00 32.93  ? 141 TYR A OH  1 
ATOM   1090 N N   . ILE A 1 143 ? -16.545 11.541  -22.656 1.00 28.15  ? 142 ILE A N   1 
ATOM   1091 C CA  . ILE A 1 143 ? -17.251 10.746  -23.655 1.00 26.77  ? 142 ILE A CA  1 
ATOM   1092 C C   . ILE A 1 143 ? -16.517 10.879  -24.986 1.00 29.19  ? 142 ILE A C   1 
ATOM   1093 O O   . ILE A 1 143 ? -16.251 11.997  -25.454 1.00 31.79  ? 142 ILE A O   1 
ATOM   1094 C CB  . ILE A 1 143 ? -18.710 11.219  -23.792 1.00 30.21  ? 142 ILE A CB  1 
ATOM   1095 C CG1 . ILE A 1 143 ? -19.449 11.084  -22.467 1.00 28.52  ? 142 ILE A CG1 1 
ATOM   1096 C CG2 . ILE A 1 143 ? -19.439 10.489  -24.935 1.00 30.80  ? 142 ILE A CG2 1 
ATOM   1097 C CD1 . ILE A 1 143 ? -19.818 9.673   -22.096 1.00 28.21  ? 142 ILE A CD1 1 
ATOM   1098 N N   . PHE A 1 144 ? -16.192 9.753   -25.609 1.00 29.17  ? 143 PHE A N   1 
ATOM   1099 C CA  . PHE A 1 144 ? -15.543 9.778   -26.913 1.00 28.01  ? 143 PHE A CA  1 
ATOM   1100 C C   . PHE A 1 144 ? -16.204 8.784   -27.864 1.00 28.23  ? 143 PHE A C   1 
ATOM   1101 O O   . PHE A 1 144 ? -16.615 7.689   -27.453 1.00 26.09  ? 143 PHE A O   1 
ATOM   1102 C CB  . PHE A 1 144 ? -14.038 9.468   -26.804 1.00 27.50  ? 143 PHE A CB  1 
ATOM   1103 C CG  . PHE A 1 144 ? -13.404 9.206   -28.133 1.00 30.35  ? 143 PHE A CG  1 
ATOM   1104 C CD1 . PHE A 1 144 ? -13.067 10.263  -28.973 1.00 30.66  ? 143 PHE A CD1 1 
ATOM   1105 C CD2 . PHE A 1 144 ? -13.215 7.910   -28.581 1.00 26.44  ? 143 PHE A CD2 1 
ATOM   1106 C CE1 . PHE A 1 144 ? -12.534 10.033  -30.215 1.00 30.48  ? 143 PHE A CE1 1 
ATOM   1107 C CE2 . PHE A 1 144 ? -12.677 7.675   -29.823 1.00 30.04  ? 143 PHE A CE2 1 
ATOM   1108 C CZ  . PHE A 1 144 ? -12.333 8.735   -30.644 1.00 30.51  ? 143 PHE A CZ  1 
ATOM   1109 N N   . GLY A 1 145 ? -16.285 9.162   -29.145 1.00 27.10  ? 144 GLY A N   1 
ATOM   1110 C CA  . GLY A 1 145 ? -16.733 8.219   -30.156 1.00 28.28  ? 144 GLY A CA  1 
ATOM   1111 C C   . GLY A 1 145 ? -18.193 7.795   -30.007 1.00 31.21  ? 144 GLY A C   1 
ATOM   1112 O O   . GLY A 1 145 ? -19.033 8.473   -29.390 1.00 27.93  ? 144 GLY A O   1 
ATOM   1113 N N   . GLY A 1 146 ? -18.479 6.626   -30.569 1.00 28.74  ? 145 GLY A N   1 
ATOM   1114 C CA  . GLY A 1 146 ? -19.836 6.143   -30.680 1.00 31.05  ? 145 GLY A CA  1 
ATOM   1115 C C   . GLY A 1 146 ? -20.461 6.505   -32.013 1.00 32.39  ? 145 GLY A C   1 
ATOM   1116 O O   . GLY A 1 146 ? -19.900 7.241   -32.826 1.00 34.25  ? 145 GLY A O   1 
ATOM   1117 N N   . TYR A 1 147 ? -21.647 5.954   -32.251 1.00 35.63  ? 146 TYR A N   1 
ATOM   1118 C CA  . TYR A 1 147 ? -22.388 6.221   -33.475 1.00 35.96  ? 146 TYR A CA  1 
ATOM   1119 C C   . TYR A 1 147 ? -23.543 7.155   -33.152 1.00 37.69  ? 146 TYR A C   1 
ATOM   1120 O O   . TYR A 1 147 ? -24.446 6.783   -32.398 1.00 37.54  ? 146 TYR A O   1 
ATOM   1121 C CB  . TYR A 1 147 ? -22.907 4.933   -34.102 1.00 36.54  ? 146 TYR A CB  1 
ATOM   1122 C CG  . TYR A 1 147 ? -23.318 5.166   -35.513 1.00 38.33  ? 146 TYR A CG  1 
ATOM   1123 C CD1 . TYR A 1 147 ? -22.365 5.213   -36.534 1.00 41.09  ? 146 TYR A CD1 1 
ATOM   1124 C CD2 . TYR A 1 147 ? -24.641 5.403   -35.833 1.00 39.53  ? 146 TYR A CD2 1 
ATOM   1125 C CE1 . TYR A 1 147 ? -22.731 5.459   -37.865 1.00 40.92  ? 146 TYR A CE1 1 
ATOM   1126 C CE2 . TYR A 1 147 ? -25.023 5.651   -37.155 1.00 44.15  ? 146 TYR A CE2 1 
ATOM   1127 C CZ  . TYR A 1 147 ? -24.065 5.676   -38.159 1.00 44.41  ? 146 TYR A CZ  1 
ATOM   1128 O OH  . TYR A 1 147 ? -24.448 5.914   -39.444 1.00 41.87  ? 146 TYR A OH  1 
ATOM   1129 N N   . GLU A 1 148 ? -23.514 8.360   -33.714 1.00 36.12  ? 147 GLU A N   1 
ATOM   1130 C CA  . GLU A 1 148 ? -24.551 9.345   -33.425 1.00 40.15  ? 147 GLU A CA  1 
ATOM   1131 C C   . GLU A 1 148 ? -25.845 9.014   -34.156 1.00 40.61  ? 147 GLU A C   1 
ATOM   1132 O O   . GLU A 1 148 ? -25.841 8.762   -35.361 1.00 44.74  ? 147 GLU A O   1 
ATOM   1133 C CB  . GLU A 1 148 ? -24.078 10.741  -33.811 1.00 40.85  ? 147 GLU A CB  1 
ATOM   1134 C CG  . GLU A 1 148 ? -23.442 11.494  -32.671 1.00 42.05  ? 147 GLU A CG  1 
ATOM   1135 C CD  . GLU A 1 148 ? -22.655 12.686  -33.153 1.00 46.29  ? 147 GLU A CD  1 
ATOM   1136 O OE1 . GLU A 1 148 ? -23.275 13.721  -33.482 1.00 44.22  ? 147 GLU A OE1 1 
ATOM   1137 O OE2 . GLU A 1 148 ? -21.409 12.574  -33.211 1.00 48.07  ? 147 GLU A OE2 1 
ATOM   1138 N N   . GLN A 1 149 ? -26.962 9.034   -33.430 1.00 44.34  ? 148 GLN A N   1 
ATOM   1139 C CA  . GLN A 1 149 ? -28.222 8.659   -34.056 1.00 51.44  ? 148 GLN A CA  1 
ATOM   1140 C C   . GLN A 1 149 ? -28.757 9.749   -34.981 1.00 53.27  ? 148 GLN A C   1 
ATOM   1141 O O   . GLN A 1 149 ? -29.203 9.444   -36.091 1.00 49.91  ? 148 GLN A O   1 
ATOM   1142 C CB  . GLN A 1 149 ? -29.254 8.311   -32.998 1.00 54.23  ? 148 GLN A CB  1 
ATOM   1143 C CG  . GLN A 1 149 ? -30.236 7.288   -33.496 1.00 64.35  ? 148 GLN A CG  1 
ATOM   1144 C CD  . GLN A 1 149 ? -31.608 7.478   -32.908 1.00 72.08  ? 148 GLN A CD  1 
ATOM   1145 O OE1 . GLN A 1 149 ? -31.787 7.418   -31.688 1.00 76.27  ? 148 GLN A OE1 1 
ATOM   1146 N NE2 . GLN A 1 149 ? -32.597 7.715   -33.773 1.00 72.60  ? 148 GLN A NE2 1 
ATOM   1147 N N   . GLN A 1 150 ? -28.704 11.020  -34.565 1.00 57.84  ? 149 GLN A N   1 
ATOM   1148 C CA  . GLN A 1 150 ? -29.241 12.093  -35.404 1.00 59.38  ? 149 GLN A CA  1 
ATOM   1149 C C   . GLN A 1 150 ? -28.320 12.395  -36.582 1.00 59.19  ? 149 GLN A C   1 
ATOM   1150 O O   . GLN A 1 150 ? -28.748 12.371  -37.741 1.00 60.53  ? 149 GLN A O   1 
ATOM   1151 C CB  . GLN A 1 150 ? -29.483 13.364  -34.581 1.00 62.93  ? 149 GLN A CB  1 
ATOM   1152 C CG  . GLN A 1 150 ? -30.702 13.325  -33.680 1.00 66.25  ? 149 GLN A CG  1 
ATOM   1153 C CD  . GLN A 1 150 ? -31.863 12.591  -34.307 1.00 72.11  ? 149 GLN A CD  1 
ATOM   1154 O OE1 . GLN A 1 150 ? -32.025 11.382  -34.108 1.00 72.12  ? 149 GLN A OE1 1 
ATOM   1155 N NE2 . GLN A 1 150 ? -32.683 13.314  -35.072 1.00 76.97  ? 149 GLN A NE2 1 
ATOM   1156 N N   . ALA A 1 151 ? -27.050 12.701  -36.306 1.00 51.60  ? 150 ALA A N   1 
ATOM   1157 C CA  . ALA A 1 151 ? -26.112 12.949  -37.392 1.00 49.15  ? 150 ALA A CA  1 
ATOM   1158 C C   . ALA A 1 151 ? -25.948 11.729  -38.287 1.00 49.24  ? 150 ALA A C   1 
ATOM   1159 O O   . ALA A 1 151 ? -25.577 11.874  -39.459 1.00 46.54  ? 150 ALA A O   1 
ATOM   1160 C CB  . ALA A 1 151 ? -24.755 13.380  -36.831 1.00 46.32  ? 150 ALA A CB  1 
ATOM   1161 N N   . ASP A 1 152 ? -26.247 10.537  -37.768 1.00 49.64  ? 151 ASP A N   1 
ATOM   1162 C CA  . ASP A 1 152 ? -26.083 9.291   -38.507 1.00 47.42  ? 151 ASP A CA  1 
ATOM   1163 C C   . ASP A 1 152 ? -24.636 9.153   -38.986 1.00 43.61  ? 151 ASP A C   1 
ATOM   1164 O O   . ASP A 1 152 ? -24.340 9.151   -40.174 1.00 43.59  ? 151 ASP A O   1 
ATOM   1165 C CB  . ASP A 1 152 ? -27.074 9.217   -39.674 1.00 46.15  ? 151 ASP A CB  1 
ATOM   1166 C CG  . ASP A 1 152 ? -27.224 7.810   -40.219 1.00 46.82  ? 151 ASP A CG  1 
ATOM   1167 O OD1 . ASP A 1 152 ? -26.877 6.857   -39.492 1.00 49.05  ? 151 ASP A OD1 1 
ATOM   1168 O OD2 . ASP A 1 152 ? -27.679 7.655   -41.368 1.00 50.69  ? 151 ASP A OD2 1 
ATOM   1169 N N   . CYS A 1 153 ? -23.726 9.074   -38.024 1.00 40.24  ? 152 CYS A N   1 
ATOM   1170 C CA  . CYS A 1 153 ? -22.315 9.054   -38.374 1.00 41.52  ? 152 CYS A CA  1 
ATOM   1171 C C   . CYS A 1 153 ? -21.519 8.586   -37.167 1.00 41.52  ? 152 CYS A C   1 
ATOM   1172 O O   . CYS A 1 153 ? -21.966 8.697   -36.021 1.00 41.39  ? 152 CYS A O   1 
ATOM   1173 C CB  . CYS A 1 153 ? -21.830 10.439  -38.826 1.00 40.15  ? 152 CYS A CB  1 
ATOM   1174 S SG  . CYS A 1 153 ? -21.725 11.658  -37.476 1.00 44.79  ? 152 CYS A SG  1 
ATOM   1175 N N   . PHE A 1 154 ? -20.330 8.068   -37.435 1.00 39.63  ? 153 PHE A N   1 
ATOM   1176 C CA  . PHE A 1 154 ? -19.390 7.863   -36.347 1.00 39.96  ? 153 PHE A CA  1 
ATOM   1177 C C   . PHE A 1 154 ? -18.949 9.218   -35.801 1.00 37.52  ? 153 PHE A C   1 
ATOM   1178 O O   . PHE A 1 154 ? -18.975 10.237  -36.498 1.00 37.76  ? 153 PHE A O   1 
ATOM   1179 C CB  . PHE A 1 154 ? -18.180 7.058   -36.818 1.00 36.32  ? 153 PHE A CB  1 
ATOM   1180 C CG  . PHE A 1 154 ? -18.498 5.644   -37.211 1.00 37.23  ? 153 PHE A CG  1 
ATOM   1181 C CD1 . PHE A 1 154 ? -18.891 5.338   -38.512 1.00 39.22  ? 153 PHE A CD1 1 
ATOM   1182 C CD2 . PHE A 1 154 ? -18.372 4.612   -36.288 1.00 34.20  ? 153 PHE A CD2 1 
ATOM   1183 C CE1 . PHE A 1 154 ? -19.177 4.027   -38.872 1.00 40.61  ? 153 PHE A CE1 1 
ATOM   1184 C CE2 . PHE A 1 154 ? -18.639 3.306   -36.640 1.00 34.44  ? 153 PHE A CE2 1 
ATOM   1185 C CZ  . PHE A 1 154 ? -19.048 3.006   -37.930 1.00 36.57  ? 153 PHE A CZ  1 
ATOM   1186 N N   . SER A 1 155 ? -18.571 9.233   -34.533 1.00 35.65  ? 154 SER A N   1 
ATOM   1187 C CA  . SER A 1 155 ? -18.095 10.444  -33.886 1.00 36.17  ? 154 SER A CA  1 
ATOM   1188 C C   . SER A 1 155 ? -16.632 10.270  -33.518 1.00 36.31  ? 154 SER A C   1 
ATOM   1189 O O   . SER A 1 155 ? -16.210 9.166   -33.155 1.00 33.62  ? 154 SER A O   1 
ATOM   1190 C CB  . SER A 1 155 ? -18.903 10.761  -32.626 1.00 32.73  ? 154 SER A CB  1 
ATOM   1191 O OG  . SER A 1 155 ? -18.305 11.819  -31.881 1.00 33.26  ? 154 SER A OG  1 
ATOM   1192 N N   . ASN A 1 156 ? -15.861 11.362  -33.619 1.00 33.34  ? 155 ASN A N   1 
ATOM   1193 C CA  . ASN A 1 156 ? -14.551 11.432  -32.984 1.00 33.51  ? 155 ASN A CA  1 
ATOM   1194 C C   . ASN A 1 156 ? -14.435 12.636  -32.059 1.00 32.25  ? 155 ASN A C   1 
ATOM   1195 O O   . ASN A 1 156 ? -13.324 13.080  -31.765 1.00 35.09  ? 155 ASN A O   1 
ATOM   1196 C CB  . ASN A 1 156 ? -13.416 11.423  -34.019 1.00 35.52  ? 155 ASN A CB  1 
ATOM   1197 C CG  . ASN A 1 156 ? -13.361 12.673  -34.870 1.00 36.20  ? 155 ASN A CG  1 
ATOM   1198 O OD1 . ASN A 1 156 ? -14.105 13.637  -34.667 1.00 36.80  ? 155 ASN A OD1 1 
ATOM   1199 N ND2 . ASN A 1 156 ? -12.459 12.661  -35.843 1.00 36.22  ? 155 ASN A ND2 1 
ATOM   1200 N N   . ASP A 1 157 ? -15.563 13.174  -31.606 1.00 32.71  ? 156 ASP A N   1 
ATOM   1201 C CA  . ASP A 1 157 ? -15.549 14.239  -30.621 1.00 33.97  ? 156 ASP A CA  1 
ATOM   1202 C C   . ASP A 1 157 ? -15.188 13.708  -29.237 1.00 33.86  ? 156 ASP A C   1 
ATOM   1203 O O   . ASP A 1 157 ? -15.435 12.548  -28.896 1.00 33.13  ? 156 ASP A O   1 
ATOM   1204 C CB  . ASP A 1 157 ? -16.916 14.909  -30.516 1.00 32.89  ? 156 ASP A CB  1 
ATOM   1205 C CG  . ASP A 1 157 ? -17.332 15.573  -31.784 1.00 35.73  ? 156 ASP A CG  1 
ATOM   1206 O OD1 . ASP A 1 157 ? -16.437 15.941  -32.572 1.00 35.38  ? 156 ASP A OD1 1 
ATOM   1207 O OD2 . ASP A 1 157 ? -18.560 15.722  -31.982 1.00 39.70  ? 156 ASP A OD2 1 
ATOM   1208 N N   . ILE A 1 158 ? -14.643 14.596  -28.413 1.00 35.36  ? 157 ILE A N   1 
ATOM   1209 C CA  . ILE A 1 158 ? -14.618 14.404  -26.969 1.00 31.18  ? 157 ILE A CA  1 
ATOM   1210 C C   . ILE A 1 158 ? -15.526 15.450  -26.345 1.00 34.45  ? 157 ILE A C   1 
ATOM   1211 O O   . ILE A 1 158 ? -15.264 16.656  -26.455 1.00 38.31  ? 157 ILE A O   1 
ATOM   1212 C CB  . ILE A 1 158 ? -13.205 14.513  -26.394 1.00 29.53  ? 157 ILE A CB  1 
ATOM   1213 C CG1 . ILE A 1 158 ? -12.297 13.457  -27.020 1.00 30.23  ? 157 ILE A CG1 1 
ATOM   1214 C CG2 . ILE A 1 158 ? -13.278 14.382  -24.875 1.00 31.14  ? 157 ILE A CG2 1 
ATOM   1215 C CD1 . ILE A 1 158 ? -10.822 13.648  -26.667 1.00 33.82  ? 157 ILE A CD1 1 
ATOM   1216 N N   . HIS A 1 159 ? -16.595 14.992  -25.701 1.00 32.87  ? 158 HIS A N   1 
ATOM   1217 C CA  . HIS A 1 159 ? -17.410 15.831  -24.835 1.00 32.48  ? 158 HIS A CA  1 
ATOM   1218 C C   . HIS A 1 159 ? -17.031 15.502  -23.403 1.00 31.84  ? 158 HIS A C   1 
ATOM   1219 O O   . HIS A 1 159 ? -16.965 14.323  -23.035 1.00 32.80  ? 158 HIS A O   1 
ATOM   1220 C CB  . HIS A 1 159 ? -18.904 15.588  -25.056 1.00 31.54  ? 158 HIS A CB  1 
ATOM   1221 C CG  . HIS A 1 159 ? -19.414 16.066  -26.383 1.00 36.13  ? 158 HIS A CG  1 
ATOM   1222 N ND1 . HIS A 1 159 ? -19.264 15.340  -27.547 1.00 34.96  ? 158 HIS A ND1 1 
ATOM   1223 C CD2 . HIS A 1 159 ? -20.095 17.188  -26.726 1.00 37.16  ? 158 HIS A CD2 1 
ATOM   1224 C CE1 . HIS A 1 159 ? -19.819 16.000  -28.550 1.00 35.46  ? 158 HIS A CE1 1 
ATOM   1225 N NE2 . HIS A 1 159 ? -20.330 17.124  -28.079 1.00 35.38  ? 158 HIS A NE2 1 
ATOM   1226 N N   . LYS A 1 160 ? -16.730 16.523  -22.612 1.00 31.49  ? 159 LYS A N   1 
ATOM   1227 C CA  . LYS A 1 160 ? -16.468 16.323  -21.195 1.00 32.49  ? 159 LYS A CA  1 
ATOM   1228 C C   . LYS A 1 160 ? -17.613 16.907  -20.381 1.00 34.86  ? 159 LYS A C   1 
ATOM   1229 O O   . LYS A 1 160 ? -18.121 17.995  -20.685 1.00 34.49  ? 159 LYS A O   1 
ATOM   1230 C CB  . LYS A 1 160 ? -15.142 16.946  -20.764 1.00 32.32  ? 159 LYS A CB  1 
ATOM   1231 C CG  . LYS A 1 160 ? -15.053 18.441  -20.988 1.00 36.46  ? 159 LYS A CG  1 
ATOM   1232 C CD  . LYS A 1 160 ? -13.750 19.004  -20.445 1.00 33.05  ? 159 LYS A CD  1 
ATOM   1233 C CE  . LYS A 1 160 ? -13.680 20.503  -20.679 1.00 33.71  ? 159 LYS A CE  1 
ATOM   1234 N NZ  . LYS A 1 160 ? -12.334 21.058  -20.385 1.00 36.25  ? 159 LYS A NZ  1 
ATOM   1235 N N   . LEU A 1 161 ? -18.042 16.154  -19.374 1.00 32.58  ? 160 LEU A N   1 
ATOM   1236 C CA  . LEU A 1 161 ? -19.034 16.611  -18.409 1.00 34.19  ? 160 LEU A CA  1 
ATOM   1237 C C   . LEU A 1 161 ? -18.320 16.892  -17.099 1.00 32.68  ? 160 LEU A C   1 
ATOM   1238 O O   . LEU A 1 161 ? -17.746 15.980  -16.492 1.00 31.67  ? 160 LEU A O   1 
ATOM   1239 C CB  . LEU A 1 161 ? -20.138 15.574  -18.197 1.00 33.49  ? 160 LEU A CB  1 
ATOM   1240 C CG  . LEU A 1 161 ? -21.128 15.923  -17.084 1.00 33.97  ? 160 LEU A CG  1 
ATOM   1241 C CD1 . LEU A 1 161 ? -22.013 17.104  -17.475 1.00 32.82  ? 160 LEU A CD1 1 
ATOM   1242 C CD2 . LEU A 1 161 ? -21.955 14.722  -16.736 1.00 33.37  ? 160 LEU A CD2 1 
ATOM   1243 N N   . ASP A 1 162 ? -18.351 18.149  -16.671 1.00 34.44  ? 161 ASP A N   1 
ATOM   1244 C CA  . ASP A 1 162 ? -17.798 18.545  -15.381 1.00 32.93  ? 161 ASP A CA  1 
ATOM   1245 C C   . ASP A 1 162 ? -18.900 18.360  -14.348 1.00 35.17  ? 161 ASP A C   1 
ATOM   1246 O O   . ASP A 1 162 ? -19.805 19.196  -14.233 1.00 35.58  ? 161 ASP A O   1 
ATOM   1247 C CB  . ASP A 1 162 ? -17.297 19.981  -15.444 1.00 34.97  ? 161 ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 162 ? -16.539 20.395  -14.194 1.00 37.27  ? 161 ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 162 ? -16.603 19.665  -13.177 1.00 34.98  ? 161 ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 162 ? -15.877 21.458  -14.243 1.00 39.04  ? 161 ASP A OD2 1 
ATOM   1251 N N   . THR A 1 163 ? -18.833 17.256  -13.594 1.00 36.36  ? 162 THR A N   1 
ATOM   1252 C CA  . THR A 1 163 ? -19.933 16.947  -12.687 1.00 34.26  ? 162 THR A CA  1 
ATOM   1253 C C   . THR A 1 163 ? -20.017 17.916  -11.519 1.00 33.38  ? 162 THR A C   1 
ATOM   1254 O O   . THR A 1 163 ? -21.040 17.913  -10.827 1.00 35.47  ? 162 THR A O   1 
ATOM   1255 C CB  . THR A 1 163 ? -19.838 15.511  -12.163 1.00 32.97  ? 162 THR A CB  1 
ATOM   1256 O OG1 . THR A 1 163 ? -18.741 15.386  -11.242 1.00 34.52  ? 162 THR A OG1 1 
ATOM   1257 C CG2 . THR A 1 163 ? -19.644 14.550  -13.299 1.00 31.82  ? 162 THR A CG2 1 
ATOM   1258 N N   . SER A 1 164 ? -18.993 18.755  -11.300 1.00 32.48  ? 163 SER A N   1 
ATOM   1259 C CA  . SER A 1 164 ? -19.073 19.759  -10.237 1.00 36.64  ? 163 SER A CA  1 
ATOM   1260 C C   . SER A 1 164 ? -20.107 20.823  -10.558 1.00 39.69  ? 163 SER A C   1 
ATOM   1261 O O   . SER A 1 164 ? -20.767 21.347  -9.651  1.00 42.65  ? 163 SER A O   1 
ATOM   1262 C CB  . SER A 1 164 ? -17.719 20.413  -10.012 1.00 34.71  ? 163 SER A CB  1 
ATOM   1263 O OG  . SER A 1 164 ? -16.853 19.482  -9.418  1.00 43.76  ? 163 SER A OG  1 
ATOM   1264 N N   . THR A 1 165 ? -20.238 21.170  -11.840 1.00 37.23  ? 164 THR A N   1 
ATOM   1265 C CA  . THR A 1 165 ? -21.241 22.110  -12.308 1.00 37.83  ? 164 THR A CA  1 
ATOM   1266 C C   . THR A 1 165 ? -22.221 21.482  -13.287 1.00 37.55  ? 164 THR A C   1 
ATOM   1267 O O   . THR A 1 165 ? -23.095 22.190  -13.801 1.00 39.18  ? 164 THR A O   1 
ATOM   1268 C CB  . THR A 1 165 ? -20.568 23.315  -12.985 1.00 38.13  ? 164 THR A CB  1 
ATOM   1269 O OG1 . THR A 1 165 ? -19.882 22.873  -14.163 1.00 34.92  ? 164 THR A OG1 1 
ATOM   1270 C CG2 . THR A 1 165 ? -19.568 23.962  -12.055 1.00 39.71  ? 164 THR A CG2 1 
ATOM   1271 N N   . MET A 1 166 ? -22.081 20.192  -13.589 1.00 36.86  ? 165 MET A N   1 
ATOM   1272 C CA  . MET A 1 166 ? -22.929 19.513  -14.571 1.00 36.23  ? 165 MET A CA  1 
ATOM   1273 C C   . MET A 1 166 ? -22.948 20.261  -15.904 1.00 37.15  ? 165 MET A C   1 
ATOM   1274 O O   . MET A 1 166 ? -24.006 20.595  -16.445 1.00 36.27  ? 165 MET A O   1 
ATOM   1275 C CB  . MET A 1 166 ? -24.339 19.320  -14.029 1.00 33.92  ? 165 MET A CB  1 
ATOM   1276 C CG  . MET A 1 166 ? -24.402 18.242  -12.964 1.00 35.66  ? 165 MET A CG  1 
ATOM   1277 S SD  . MET A 1 166 ? -23.784 16.685  -13.610 1.00 39.52  ? 165 MET A SD  1 
ATOM   1278 C CE  . MET A 1 166 ? -23.870 15.648  -12.151 1.00 31.07  ? 165 MET A CE  1 
ATOM   1279 N N   . THR A 1 167 ? -21.753 20.534  -16.430 1.00 36.01  ? 166 THR A N   1 
ATOM   1280 C CA  . THR A 1 167 ? -21.600 21.311  -17.651 1.00 37.57  ? 166 THR A CA  1 
ATOM   1281 C C   . THR A 1 167 ? -20.852 20.504  -18.703 1.00 36.75  ? 166 THR A C   1 
ATOM   1282 O O   . THR A 1 167 ? -19.744 20.009  -18.452 1.00 34.94  ? 166 THR A O   1 
ATOM   1283 C CB  . THR A 1 167 ? -20.865 22.628  -17.399 1.00 36.80  ? 166 THR A CB  1 
ATOM   1284 O OG1 . THR A 1 167 ? -21.583 23.385  -16.424 1.00 33.50  ? 166 THR A OG1 1 
ATOM   1285 C CG2 . THR A 1 167 ? -20.765 23.433  -18.707 1.00 33.85  ? 166 THR A CG2 1 
ATOM   1286 N N   . TRP A 1 168 ? -21.461 20.399  -19.882 1.00 34.25  ? 167 TRP A N   1 
ATOM   1287 C CA  . TRP A 1 168 ? -20.864 19.746  -21.031 1.00 35.88  ? 167 TRP A CA  1 
ATOM   1288 C C   . TRP A 1 168 ? -20.041 20.741  -21.831 1.00 36.30  ? 167 TRP A C   1 
ATOM   1289 O O   . TRP A 1 168 ? -20.475 21.871  -22.069 1.00 39.34  ? 167 TRP A O   1 
ATOM   1290 C CB  . TRP A 1 168 ? -21.938 19.155  -21.936 1.00 36.52  ? 167 TRP A CB  1 
ATOM   1291 C CG  . TRP A 1 168 ? -22.622 17.946  -21.439 1.00 33.75  ? 167 TRP A CG  1 
ATOM   1292 C CD1 . TRP A 1 168 ? -23.887 17.867  -20.933 1.00 36.26  ? 167 TRP A CD1 1 
ATOM   1293 C CD2 . TRP A 1 168 ? -22.106 16.614  -21.442 1.00 33.19  ? 167 TRP A CD2 1 
ATOM   1294 N NE1 . TRP A 1 168 ? -24.186 16.564  -20.609 1.00 33.58  ? 167 TRP A NE1 1 
ATOM   1295 C CE2 . TRP A 1 168 ? -23.106 15.777  -20.918 1.00 33.33  ? 167 TRP A CE2 1 
ATOM   1296 C CE3 . TRP A 1 168 ? -20.892 16.046  -21.840 1.00 34.57  ? 167 TRP A CE3 1 
ATOM   1297 C CZ2 . TRP A 1 168 ? -22.924 14.409  -20.774 1.00 35.34  ? 167 TRP A CZ2 1 
ATOM   1298 C CZ3 . TRP A 1 168 ? -20.718 14.692  -21.709 1.00 30.87  ? 167 TRP A CZ3 1 
ATOM   1299 C CH2 . TRP A 1 168 ? -21.721 13.886  -21.173 1.00 31.98  ? 167 TRP A CH2 1 
ATOM   1300 N N   . THR A 1 169 ? -18.849 20.312  -22.245 1.00 36.34  ? 168 THR A N   1 
ATOM   1301 C CA  . THR A 1 169 ? -18.014 21.057  -23.177 1.00 33.62  ? 168 THR A CA  1 
ATOM   1302 C C   . THR A 1 169 ? -17.646 20.134  -24.330 1.00 37.82  ? 168 THR A C   1 
ATOM   1303 O O   . THR A 1 169 ? -17.211 18.997  -24.111 1.00 37.76  ? 168 THR A O   1 
ATOM   1304 C CB  . THR A 1 169 ? -16.739 21.585  -22.501 1.00 35.78  ? 168 THR A CB  1 
ATOM   1305 O OG1 . THR A 1 169 ? -17.086 22.342  -21.338 1.00 39.29  ? 168 THR A OG1 1 
ATOM   1306 C CG2 . THR A 1 169 ? -15.917 22.467  -23.450 1.00 31.60  ? 168 THR A CG2 1 
ATOM   1307 N N   . LEU A 1 170 ? -17.838 20.611  -25.554 1.00 38.82  ? 169 LEU A N   1 
ATOM   1308 C CA  . LEU A 1 170 ? -17.204 19.978  -26.701 1.00 37.86  ? 169 LEU A CA  1 
ATOM   1309 C C   . LEU A 1 170 ? -15.760 20.458  -26.736 1.00 36.72  ? 169 LEU A C   1 
ATOM   1310 O O   . LEU A 1 170 ? -15.505 21.650  -26.930 1.00 37.39  ? 169 LEU A O   1 
ATOM   1311 C CB  . LEU A 1 170 ? -17.945 20.329  -27.986 1.00 37.02  ? 169 LEU A CB  1 
ATOM   1312 C CG  . LEU A 1 170 ? -17.261 19.798  -29.248 1.00 37.73  ? 169 LEU A CG  1 
ATOM   1313 C CD1 . LEU A 1 170 ? -16.979 18.318  -29.110 1.00 37.04  ? 169 LEU A CD1 1 
ATOM   1314 C CD2 . LEU A 1 170 ? -18.107 20.067  -30.475 1.00 34.76  ? 169 LEU A CD2 1 
ATOM   1315 N N   . ILE A 1 171 ? -14.810 19.553  -26.518 1.00 37.90  ? 170 ILE A N   1 
ATOM   1316 C CA  . ILE A 1 171 ? -13.419 19.969  -26.362 1.00 35.54  ? 170 ILE A CA  1 
ATOM   1317 C C   . ILE A 1 171 ? -12.838 20.268  -27.730 1.00 36.58  ? 170 ILE A C   1 
ATOM   1318 O O   . ILE A 1 171 ? -12.821 19.401  -28.609 1.00 40.66  ? 170 ILE A O   1 
ATOM   1319 C CB  . ILE A 1 171 ? -12.577 18.904  -25.649 1.00 36.25  ? 170 ILE A CB  1 
ATOM   1320 C CG1 . ILE A 1 171 ? -13.110 18.627  -24.250 1.00 37.32  ? 170 ILE A CG1 1 
ATOM   1321 C CG2 . ILE A 1 171 ? -11.122 19.366  -25.548 1.00 37.33  ? 170 ILE A CG2 1 
ATOM   1322 C CD1 . ILE A 1 171 ? -12.293 17.624  -23.505 1.00 34.99  ? 170 ILE A CD1 1 
ATOM   1323 N N   . CYS A 1 172 ? -12.350 21.489  -27.910 1.00 37.52  ? 171 CYS A N   1 
ATOM   1324 C CA  A CYS A 1 172 ? -11.577 21.829  -29.103 0.56 41.09  ? 171 CYS A CA  1 
ATOM   1325 C CA  B CYS A 1 172 ? -11.581 21.832  -29.100 0.44 39.14  ? 171 CYS A CA  1 
ATOM   1326 C C   . CYS A 1 172 ? -10.175 21.276  -28.898 1.00 39.82  ? 171 CYS A C   1 
ATOM   1327 O O   . CYS A 1 172 ? -9.332  21.903  -28.250 1.00 42.40  ? 171 CYS A O   1 
ATOM   1328 C CB  A CYS A 1 172 ? -11.558 23.335  -29.341 0.56 43.63  ? 171 CYS A CB  1 
ATOM   1329 C CB  B CYS A 1 172 ? -11.588 23.341  -29.318 0.44 39.96  ? 171 CYS A CB  1 
ATOM   1330 S SG  A CYS A 1 172 ? -10.806 23.820  -30.925 0.56 39.36  ? 171 CYS A SG  1 
ATOM   1331 S SG  B CYS A 1 172 ? -13.261 24.069  -29.302 0.44 41.39  ? 171 CYS A SG  1 
ATOM   1332 N N   . THR A 1 173 ? -9.930  20.078  -29.423 1.00 38.93  ? 172 THR A N   1 
ATOM   1333 C CA  . THR A 1 173 ? -8.659  19.425  -29.164 1.00 38.68  ? 172 THR A CA  1 
ATOM   1334 C C   . THR A 1 173 ? -7.581  19.948  -30.098 1.00 38.52  ? 172 THR A C   1 
ATOM   1335 O O   . THR A 1 173 ? -7.855  20.548  -31.138 1.00 39.51  ? 172 THR A O   1 
ATOM   1336 C CB  . THR A 1 173 ? -8.775  17.912  -29.328 1.00 40.10  ? 172 THR A CB  1 
ATOM   1337 O OG1 . THR A 1 173 ? -9.077  17.605  -30.695 1.00 38.41  ? 172 THR A OG1 1 
ATOM   1338 C CG2 . THR A 1 173 ? -9.860  17.336  -28.421 1.00 37.13  ? 172 THR A CG2 1 
ATOM   1339 N N   . LYS A 1 174 ? -6.340  19.716  -29.705 1.00 40.15  ? 173 LYS A N   1 
ATOM   1340 C CA  . LYS A 1 174 ? -5.195  19.895  -30.582 1.00 41.51  ? 173 LYS A CA  1 
ATOM   1341 C C   . LYS A 1 174 ? -4.716  18.513  -31.037 1.00 39.62  ? 173 LYS A C   1 
ATOM   1342 O O   . LYS A 1 174 ? -5.179  17.478  -30.537 1.00 36.81  ? 173 LYS A O   1 
ATOM   1343 C CB  . LYS A 1 174 ? -4.091  20.690  -29.865 1.00 36.35  ? 173 LYS A CB  1 
ATOM   1344 N N   . GLY A 1 175 ? -3.814  18.497  -32.030 1.00 34.97  ? 174 GLY A N   1 
ATOM   1345 C CA  . GLY A 1 175 ? -3.283  17.244  -32.547 1.00 37.87  ? 174 GLY A CA  1 
ATOM   1346 C C   . GLY A 1 175 ? -4.255  16.487  -33.449 1.00 39.75  ? 174 GLY A C   1 
ATOM   1347 O O   . GLY A 1 175 ? -5.389  16.906  -33.696 1.00 41.84  ? 174 GLY A O   1 
ATOM   1348 N N   . SER A 1 176 ? -3.801  15.325  -33.941 1.00 36.63  ? 175 SER A N   1 
ATOM   1349 C CA  . SER A 1 176 ? -4.640  14.544  -34.843 1.00 36.04  ? 175 SER A CA  1 
ATOM   1350 C C   . SER A 1 176 ? -5.593  13.678  -34.035 1.00 43.17  ? 175 SER A C   1 
ATOM   1351 O O   . SER A 1 176 ? -5.161  12.718  -33.377 1.00 40.74  ? 175 SER A O   1 
ATOM   1352 C CB  . SER A 1 176 ? -3.810  13.656  -35.766 1.00 35.73  ? 175 SER A CB  1 
ATOM   1353 O OG  . SER A 1 176 ? -2.896  14.436  -36.510 1.00 47.90  ? 175 SER A OG  1 
ATOM   1354 N N   . PRO A 1 177 ? -6.895  13.964  -34.088 1.00 39.66  ? 176 PRO A N   1 
ATOM   1355 C CA  . PRO A 1 177 ? -7.850  13.180  -33.297 1.00 36.64  ? 176 PRO A CA  1 
ATOM   1356 C C   . PRO A 1 177 ? -7.882  11.735  -33.760 1.00 38.02  ? 176 PRO A C   1 
ATOM   1357 O O   . PRO A 1 177 ? -7.539  11.416  -34.900 1.00 41.98  ? 176 PRO A O   1 
ATOM   1358 C CB  . PRO A 1 177 ? -9.188  13.888  -33.537 1.00 34.76  ? 176 PRO A CB  1 
ATOM   1359 C CG  . PRO A 1 177 ? -8.996  14.648  -34.811 1.00 41.32  ? 176 PRO A CG  1 
ATOM   1360 C CD  . PRO A 1 177 ? -7.545  14.971  -34.941 1.00 37.66  ? 176 PRO A CD  1 
ATOM   1361 N N   . ALA A 1 178 ? -8.236  10.847  -32.838 1.00 37.76  ? 177 ALA A N   1 
ATOM   1362 C CA  . ALA A 1 178 ? -8.398  9.447   -33.193 1.00 34.93  ? 177 ALA A CA  1 
ATOM   1363 C C   . ALA A 1 178 ? -9.568  9.296   -34.156 1.00 35.03  ? 177 ALA A C   1 
ATOM   1364 O O   . ALA A 1 178 ? -10.517 10.083  -34.142 1.00 37.01  ? 177 ALA A O   1 
ATOM   1365 C CB  . ALA A 1 178 ? -8.626  8.607   -31.943 1.00 33.26  ? 177 ALA A CB  1 
ATOM   1366 N N   . ARG A 1 179 ? -9.489  8.281   -35.005 1.00 33.75  ? 178 ARG A N   1 
ATOM   1367 C CA  . ARG A 1 179 ? -10.486 8.109   -36.049 1.00 33.15  ? 178 ARG A CA  1 
ATOM   1368 C C   . ARG A 1 179 ? -11.869 7.856   -35.453 1.00 34.87  ? 178 ARG A C   1 
ATOM   1369 O O   . ARG A 1 179 ? -12.013 7.115   -34.474 1.00 31.80  ? 178 ARG A O   1 
ATOM   1370 C CB  . ARG A 1 179 ? -10.069 6.955   -36.955 1.00 36.39  ? 178 ARG A CB  1 
ATOM   1371 C CG  . ARG A 1 179 ? -11.150 6.443   -37.878 1.00 37.44  ? 178 ARG A CG  1 
ATOM   1372 C CD  . ARG A 1 179 ? -10.601 5.325   -38.743 1.00 37.29  ? 178 ARG A CD  1 
ATOM   1373 N NE  . ARG A 1 179 ? -9.324  5.737   -39.299 1.00 39.18  ? 178 ARG A NE  1 
ATOM   1374 C CZ  . ARG A 1 179 ? -9.179  6.500   -40.375 1.00 38.64  ? 178 ARG A CZ  1 
ATOM   1375 N NH1 . ARG A 1 179 ? -10.216 6.855   -41.123 1.00 37.07  ? 178 ARG A NH1 1 
ATOM   1376 N NH2 . ARG A 1 179 ? -7.962  6.920   -40.707 1.00 41.05  ? 178 ARG A NH2 1 
ATOM   1377 N N   . TRP A 1 180 ? -12.885 8.513   -36.041 1.00 35.72  ? 179 TRP A N   1 
ATOM   1378 C CA  . TRP A 1 180 ? -14.288 8.243   -35.735 1.00 34.37  ? 179 TRP A CA  1 
ATOM   1379 C C   . TRP A 1 180 ? -14.532 6.739   -35.662 1.00 33.29  ? 179 TRP A C   1 
ATOM   1380 O O   . TRP A 1 180 ? -14.007 5.979   -36.477 1.00 34.31  ? 179 TRP A O   1 
ATOM   1381 C CB  . TRP A 1 180 ? -15.204 8.843   -36.808 1.00 34.92  ? 179 TRP A CB  1 
ATOM   1382 C CG  . TRP A 1 180 ? -14.791 10.146  -37.437 1.00 35.92  ? 179 TRP A CG  1 
ATOM   1383 C CD1 . TRP A 1 180 ? -15.276 11.388  -37.140 1.00 36.82  ? 179 TRP A CD1 1 
ATOM   1384 C CD2 . TRP A 1 180 ? -13.870 10.329  -38.522 1.00 35.18  ? 179 TRP A CD2 1 
ATOM   1385 N NE1 . TRP A 1 180 ? -14.690 12.338  -37.949 1.00 34.26  ? 179 TRP A NE1 1 
ATOM   1386 C CE2 . TRP A 1 180 ? -13.824 11.712  -38.806 1.00 37.45  ? 179 TRP A CE2 1 
ATOM   1387 C CE3 . TRP A 1 180 ? -13.076 9.460   -39.276 1.00 35.54  ? 179 TRP A CE3 1 
ATOM   1388 C CZ2 . TRP A 1 180 ? -13.006 12.248  -39.817 1.00 37.93  ? 179 TRP A CZ2 1 
ATOM   1389 C CZ3 . TRP A 1 180 ? -12.263 9.994   -40.278 1.00 37.50  ? 179 TRP A CZ3 1 
ATOM   1390 C CH2 . TRP A 1 180 ? -12.237 11.377  -40.537 1.00 32.80  ? 179 TRP A CH2 1 
ATOM   1391 N N   . ARG A 1 181 ? -15.323 6.310   -34.683 1.00 29.82  ? 180 ARG A N   1 
ATOM   1392 C CA  . ARG A 1 181 ? -15.381 4.883   -34.393 1.00 34.72  ? 180 ARG A CA  1 
ATOM   1393 C C   . ARG A 1 181 ? -16.406 4.634   -33.298 1.00 31.81  ? 180 ARG A C   1 
ATOM   1394 O O   . ARG A 1 181 ? -16.737 5.533   -32.519 1.00 31.16  ? 180 ARG A O   1 
ATOM   1395 C CB  . ARG A 1 181 ? -14.011 4.332   -33.944 1.00 30.24  ? 180 ARG A CB  1 
ATOM   1396 C CG  . ARG A 1 181 ? -13.594 4.866   -32.598 1.00 30.88  ? 180 ARG A CG  1 
ATOM   1397 C CD  . ARG A 1 181 ? -12.215 4.391   -32.202 1.00 31.38  ? 180 ARG A CD  1 
ATOM   1398 N NE  . ARG A 1 181 ? -11.173 5.124   -32.902 1.00 32.23  ? 180 ARG A NE  1 
ATOM   1399 C CZ  . ARG A 1 181 ? -9.920  4.705   -33.013 1.00 33.42  ? 180 ARG A CZ  1 
ATOM   1400 N NH1 . ARG A 1 181 ? -9.527  3.557   -32.484 1.00 33.99  ? 180 ARG A NH1 1 
ATOM   1401 N NH2 . ARG A 1 181 ? -9.042  5.454   -33.672 1.00 31.04  ? 180 ARG A NH2 1 
ATOM   1402 N N   . ASP A 1 182 ? -16.880 3.394   -33.226 1.00 28.39  ? 181 ASP A N   1 
ATOM   1403 C CA  . ASP A 1 182 ? -17.728 2.996   -32.118 1.00 30.95  ? 181 ASP A CA  1 
ATOM   1404 C C   . ASP A 1 182 ? -17.289 1.625   -31.610 1.00 32.31  ? 181 ASP A C   1 
ATOM   1405 O O   . ASP A 1 182 ? -16.534 0.897   -32.272 1.00 29.97  ? 181 ASP A O   1 
ATOM   1406 C CB  . ASP A 1 182 ? -19.249 3.039   -32.486 1.00 31.23  ? 181 ASP A CB  1 
ATOM   1407 C CG  . ASP A 1 182 ? -19.640 2.132   -33.661 1.00 32.84  ? 181 ASP A CG  1 
ATOM   1408 O OD1 . ASP A 1 182 ? -18.831 1.306   -34.140 1.00 34.30  ? 181 ASP A OD1 1 
ATOM   1409 O OD2 . ASP A 1 182 ? -20.798 2.254   -34.125 1.00 35.40  ? 181 ASP A OD2 1 
ATOM   1410 N N   . PHE A 1 183 ? -17.767 1.297   -30.401 1.00 29.10  ? 182 PHE A N   1 
ATOM   1411 C CA  . PHE A 1 183 ? -17.446 0.038   -29.720 1.00 29.90  ? 182 PHE A CA  1 
ATOM   1412 C C   . PHE A 1 183 ? -15.946 -0.120  -29.527 1.00 27.82  ? 182 PHE A C   1 
ATOM   1413 O O   . PHE A 1 183 ? -15.414 -1.232  -29.466 1.00 28.98  ? 182 PHE A O   1 
ATOM   1414 C CB  . PHE A 1 183 ? -18.068 -1.153  -30.448 1.00 29.95  ? 182 PHE A CB  1 
ATOM   1415 C CG  . PHE A 1 183 ? -19.558 -1.081  -30.463 1.00 32.24  ? 182 PHE A CG  1 
ATOM   1416 C CD1 . PHE A 1 183 ? -20.289 -1.494  -29.360 1.00 28.12  ? 182 PHE A CD1 1 
ATOM   1417 C CD2 . PHE A 1 183 ? -20.229 -0.505  -31.534 1.00 31.92  ? 182 PHE A CD2 1 
ATOM   1418 C CE1 . PHE A 1 183 ? -21.667 -1.399  -29.353 1.00 29.03  ? 182 PHE A CE1 1 
ATOM   1419 C CE2 . PHE A 1 183 ? -21.616 -0.396  -31.515 1.00 32.42  ? 182 PHE A CE2 1 
ATOM   1420 C CZ  . PHE A 1 183 ? -22.328 -0.846  -30.419 1.00 28.20  ? 182 PHE A CZ  1 
ATOM   1421 N N   . HIS A 1 184 ? -15.288 1.021   -29.417 1.00 26.54  ? 183 HIS A N   1 
ATOM   1422 C CA  . HIS A 1 184 ? -13.918 1.148   -28.969 1.00 27.70  ? 183 HIS A CA  1 
ATOM   1423 C C   . HIS A 1 184 ? -13.881 1.097   -27.448 1.00 28.60  ? 183 HIS A C   1 
ATOM   1424 O O   . HIS A 1 184 ? -14.911 0.973   -26.774 1.00 27.68  ? 183 HIS A O   1 
ATOM   1425 C CB  . HIS A 1 184 ? -13.347 2.470   -29.459 1.00 28.50  ? 183 HIS A CB  1 
ATOM   1426 C CG  . HIS A 1 184 ? -14.136 3.649   -28.984 1.00 26.72  ? 183 HIS A CG  1 
ATOM   1427 N ND1 . HIS A 1 184 ? -15.370 3.971   -29.502 1.00 27.76  ? 183 HIS A ND1 1 
ATOM   1428 C CD2 . HIS A 1 184 ? -13.896 4.544   -27.997 1.00 27.90  ? 183 HIS A CD2 1 
ATOM   1429 C CE1 . HIS A 1 184 ? -15.846 5.030   -28.873 1.00 28.88  ? 183 HIS A CE1 1 
ATOM   1430 N NE2 . HIS A 1 184 ? -14.970 5.398   -27.957 1.00 29.68  ? 183 HIS A NE2 1 
ATOM   1431 N N   . SER A 1 185 ? -12.685 1.242   -26.896 1.00 26.14  ? 184 SER A N   1 
ATOM   1432 C CA  . SER A 1 185 ? -12.535 1.500   -25.474 1.00 26.99  ? 184 SER A CA  1 
ATOM   1433 C C   . SER A 1 185 ? -11.697 2.748   -25.268 1.00 27.27  ? 184 SER A C   1 
ATOM   1434 O O   . SER A 1 185 ? -10.914 3.152   -26.139 1.00 26.33  ? 184 SER A O   1 
ATOM   1435 C CB  . SER A 1 185 ? -11.892 0.334   -24.739 1.00 25.53  ? 184 SER A CB  1 
ATOM   1436 O OG  . SER A 1 185 ? -10.579 0.103   -25.204 1.00 25.75  ? 184 SER A OG  1 
ATOM   1437 N N   . ALA A 1 186 ? -11.902 3.368   -24.110 1.00 26.23  ? 185 ALA A N   1 
ATOM   1438 C CA  . ALA A 1 186 ? -11.087 4.483   -23.655 1.00 26.10  ? 185 ALA A CA  1 
ATOM   1439 C C   . ALA A 1 186 ? -10.816 4.267   -22.171 1.00 29.01  ? 185 ALA A C   1 
ATOM   1440 O O   . ALA A 1 186 ? -11.745 4.030   -21.391 1.00 31.39  ? 185 ALA A O   1 
ATOM   1441 C CB  . ALA A 1 186 ? -11.775 5.833   -23.918 1.00 23.37  ? 185 ALA A CB  1 
ATOM   1442 N N   . THR A 1 187 ? -9.541  4.315   -21.793 1.00 28.71  ? 186 THR A N   1 
ATOM   1443 C CA  . THR A 1 187 ? -9.104  3.980   -20.445 1.00 28.28  ? 186 THR A CA  1 
ATOM   1444 C C   . THR A 1 187 ? -8.160  5.059   -19.954 1.00 28.25  ? 186 THR A C   1 
ATOM   1445 O O   . THR A 1 187 ? -7.230  5.451   -20.666 1.00 26.75  ? 186 THR A O   1 
ATOM   1446 C CB  . THR A 1 187 ? -8.401  2.617   -20.406 1.00 28.08  ? 186 THR A CB  1 
ATOM   1447 O OG1 . THR A 1 187 ? -9.203  1.645   -21.096 1.00 27.43  ? 186 THR A OG1 1 
ATOM   1448 C CG2 . THR A 1 187 ? -8.167  2.174   -18.962 1.00 21.12  ? 186 THR A CG2 1 
ATOM   1449 N N   . MET A 1 188 ? -8.395  5.522   -18.737 1.00 30.42  ? 187 MET A N   1 
ATOM   1450 C CA  . MET A 1 188 ? -7.589  6.571   -18.135 1.00 28.55  ? 187 MET A CA  1 
ATOM   1451 C C   . MET A 1 188 ? -6.412  5.920   -17.404 1.00 28.39  ? 187 MET A C   1 
ATOM   1452 O O   . MET A 1 188 ? -6.611  5.047   -16.551 1.00 31.64  ? 187 MET A O   1 
ATOM   1453 C CB  . MET A 1 188 ? -8.489  7.394   -17.206 1.00 27.73  ? 187 MET A CB  1 
ATOM   1454 C CG  . MET A 1 188 ? -8.074  8.845   -16.958 1.00 36.03  ? 187 MET A CG  1 
ATOM   1455 S SD  . MET A 1 188 ? -8.003  9.943   -18.416 1.00 36.09  ? 187 MET A SD  1 
ATOM   1456 C CE  . MET A 1 188 ? -9.443  9.417   -19.222 1.00 27.68  ? 187 MET A CE  1 
ATOM   1457 N N   . LEU A 1 189 ? -5.188  6.282   -17.782 1.00 30.60  ? 188 LEU A N   1 
ATOM   1458 C CA  . LEU A 1 189 ? -3.978  5.913   -17.034 1.00 31.28  ? 188 LEU A CA  1 
ATOM   1459 C C   . LEU A 1 189 ? -3.282  7.209   -16.654 1.00 31.04  ? 188 LEU A C   1 
ATOM   1460 O O   . LEU A 1 189 ? -2.686  7.870   -17.513 1.00 31.32  ? 188 LEU A O   1 
ATOM   1461 C CB  . LEU A 1 189 ? -3.033  5.009   -17.839 1.00 30.73  ? 188 LEU A CB  1 
ATOM   1462 C CG  . LEU A 1 189 ? -3.488  3.564   -18.116 1.00 29.30  ? 188 LEU A CG  1 
ATOM   1463 C CD1 . LEU A 1 189 ? -2.479  2.803   -18.950 1.00 28.53  ? 188 LEU A CD1 1 
ATOM   1464 C CD2 . LEU A 1 189 ? -3.782  2.816   -16.825 1.00 26.27  ? 188 LEU A CD2 1 
ATOM   1465 N N   . GLY A 1 190 ? -3.369  7.576   -15.379 1.00 28.40  ? 189 GLY A N   1 
ATOM   1466 C CA  . GLY A 1 190 ? -2.884  8.888   -14.987 1.00 33.61  ? 189 GLY A CA  1 
ATOM   1467 C C   . GLY A 1 190 ? -3.806  9.967   -15.532 1.00 35.73  ? 189 GLY A C   1 
ATOM   1468 O O   . GLY A 1 190 ? -5.020  9.946   -15.303 1.00 35.11  ? 189 GLY A O   1 
ATOM   1469 N N   . SER A 1 191 ? -3.243  10.929  -16.258 1.00 34.63  ? 190 SER A N   1 
ATOM   1470 C CA  . SER A 1 191 ? -4.042  11.979  -16.874 1.00 33.35  ? 190 SER A CA  1 
ATOM   1471 C C   . SER A 1 191 ? -4.304  11.735  -18.351 1.00 33.38  ? 190 SER A C   1 
ATOM   1472 O O   . SER A 1 191 ? -4.848  12.613  -19.020 1.00 35.30  ? 190 SER A O   1 
ATOM   1473 C CB  . SER A 1 191 ? -3.367  13.330  -16.692 1.00 35.38  ? 190 SER A CB  1 
ATOM   1474 O OG  . SER A 1 191 ? -3.494  13.750  -15.352 1.00 46.19  ? 190 SER A OG  1 
ATOM   1475 N N   . HIS A 1 192 ? -3.941  10.570  -18.874 1.00 36.94  ? 191 HIS A N   1 
ATOM   1476 C CA  . HIS A 1 192 ? -3.982  10.315  -20.305 1.00 31.76  ? 191 HIS A CA  1 
ATOM   1477 C C   . HIS A 1 192 ? -5.055  9.289   -20.620 1.00 29.09  ? 191 HIS A C   1 
ATOM   1478 O O   . HIS A 1 192 ? -5.181  8.274   -19.932 1.00 27.83  ? 191 HIS A O   1 
ATOM   1479 C CB  . HIS A 1 192 ? -2.622  9.838   -20.814 1.00 31.91  ? 191 HIS A CB  1 
ATOM   1480 C CG  . HIS A 1 192 ? -1.561  10.892  -20.753 1.00 36.14  ? 191 HIS A CG  1 
ATOM   1481 N ND1 . HIS A 1 192 ? -0.866  11.186  -19.598 1.00 35.16  ? 191 HIS A ND1 1 
ATOM   1482 C CD2 . HIS A 1 192 ? -1.089  11.735  -21.702 1.00 32.44  ? 191 HIS A CD2 1 
ATOM   1483 C CE1 . HIS A 1 192 ? -0.016  12.167  -19.842 1.00 34.91  ? 191 HIS A CE1 1 
ATOM   1484 N NE2 . HIS A 1 192 ? -0.132  12.517  -21.110 1.00 30.53  ? 191 HIS A NE2 1 
ATOM   1485 N N   . MET A 1 193 ? -5.832  9.564   -21.661 1.00 31.19  ? 192 MET A N   1 
ATOM   1486 C CA  . MET A 1 193 ? -6.884  8.666   -22.111 1.00 28.80  ? 192 MET A CA  1 
ATOM   1487 C C   . MET A 1 193 ? -6.356  7.824   -23.266 1.00 27.03  ? 192 MET A C   1 
ATOM   1488 O O   . MET A 1 193 ? -5.953  8.364   -24.303 1.00 29.73  ? 192 MET A O   1 
ATOM   1489 C CB  . MET A 1 193 ? -8.127  9.455   -22.524 1.00 25.79  ? 192 MET A CB  1 
ATOM   1490 C CG  . MET A 1 193 ? -9.341  8.578   -22.721 1.00 26.96  ? 192 MET A CG  1 
ATOM   1491 S SD  . MET A 1 193 ? -10.855 9.466   -23.178 1.00 34.04  ? 192 MET A SD  1 
ATOM   1492 C CE  . MET A 1 193 ? -10.394 10.194  -24.750 1.00 27.62  ? 192 MET A CE  1 
ATOM   1493 N N   . TYR A 1 194 ? -6.358  6.508   -23.088 1.00 25.80  ? 193 TYR A N   1 
ATOM   1494 C CA  . TYR A 1 194 ? -5.871  5.577   -24.100 1.00 27.61  ? 193 TYR A CA  1 
ATOM   1495 C C   . TYR A 1 194 ? -7.058  4.973   -24.851 1.00 27.68  ? 193 TYR A C   1 
ATOM   1496 O O   . TYR A 1 194 ? -7.900  4.294   -24.256 1.00 28.36  ? 193 TYR A O   1 
ATOM   1497 C CB  . TYR A 1 194 ? -5.004  4.503   -23.445 1.00 26.10  ? 193 TYR A CB  1 
ATOM   1498 C CG  . TYR A 1 194 ? -3.749  5.097   -22.838 1.00 30.22  ? 193 TYR A CG  1 
ATOM   1499 C CD1 . TYR A 1 194 ? -3.801  5.781   -21.621 1.00 29.05  ? 193 TYR A CD1 1 
ATOM   1500 C CD2 . TYR A 1 194 ? -2.521  5.013   -23.493 1.00 28.30  ? 193 TYR A CD2 1 
ATOM   1501 C CE1 . TYR A 1 194 ? -2.670  6.352   -21.073 1.00 31.76  ? 193 TYR A CE1 1 
ATOM   1502 C CE2 . TYR A 1 194 ? -1.371  5.582   -22.941 1.00 28.13  ? 193 TYR A CE2 1 
ATOM   1503 C CZ  . TYR A 1 194 ? -1.453  6.250   -21.736 1.00 31.77  ? 193 TYR A CZ  1 
ATOM   1504 O OH  . TYR A 1 194 ? -0.340  6.823   -21.172 1.00 35.26  ? 193 TYR A OH  1 
ATOM   1505 N N   . VAL A 1 195 ? -7.131  5.235   -26.153 1.00 27.15  ? 194 VAL A N   1 
ATOM   1506 C CA  . VAL A 1 195 ? -8.239  4.788   -26.993 1.00 26.98  ? 194 VAL A CA  1 
ATOM   1507 C C   . VAL A 1 195 ? -7.756  3.621   -27.843 1.00 25.93  ? 194 VAL A C   1 
ATOM   1508 O O   . VAL A 1 195 ? -6.768  3.740   -28.576 1.00 27.13  ? 194 VAL A O   1 
ATOM   1509 C CB  . VAL A 1 195 ? -8.772  5.926   -27.875 1.00 29.81  ? 194 VAL A CB  1 
ATOM   1510 C CG1 . VAL A 1 195 ? -9.851  5.408   -28.810 1.00 26.77  ? 194 VAL A CG1 1 
ATOM   1511 C CG2 . VAL A 1 195 ? -9.283  7.067   -27.005 1.00 26.70  ? 194 VAL A CG2 1 
ATOM   1512 N N   . PHE A 1 196 ? -8.436  2.487   -27.739 1.00 27.81  ? 195 PHE A N   1 
ATOM   1513 C CA  . PHE A 1 196 ? -8.043  1.313   -28.503 1.00 26.82  ? 195 PHE A CA  1 
ATOM   1514 C C   . PHE A 1 196 ? -9.240  0.670   -29.194 1.00 27.10  ? 195 PHE A C   1 
ATOM   1515 O O   . PHE A 1 196 ? -10.345 0.624   -28.643 1.00 27.34  ? 195 PHE A O   1 
ATOM   1516 C CB  . PHE A 1 196 ? -7.361  0.263   -27.636 1.00 23.65  ? 195 PHE A CB  1 
ATOM   1517 C CG  . PHE A 1 196 ? -6.901  -0.908  -28.422 1.00 25.44  ? 195 PHE A CG  1 
ATOM   1518 C CD1 . PHE A 1 196 ? -5.779  -0.809  -29.219 1.00 24.94  ? 195 PHE A CD1 1 
ATOM   1519 C CD2 . PHE A 1 196 ? -7.631  -2.087  -28.426 1.00 26.97  ? 195 PHE A CD2 1 
ATOM   1520 C CE1 . PHE A 1 196 ? -5.367  -1.873  -29.978 1.00 28.94  ? 195 PHE A CE1 1 
ATOM   1521 C CE2 . PHE A 1 196 ? -7.228  -3.162  -29.192 1.00 28.97  ? 195 PHE A CE2 1 
ATOM   1522 C CZ  . PHE A 1 196 ? -6.101  -3.060  -29.974 1.00 28.93  ? 195 PHE A CZ  1 
ATOM   1523 N N   . GLY A 1 197 ? -8.992  0.148   -30.398 1.00 28.13  ? 196 GLY A N   1 
ATOM   1524 C CA  . GLY A 1 197 ? -9.928  -0.672  -31.136 1.00 29.22  ? 196 GLY A CA  1 
ATOM   1525 C C   . GLY A 1 197 ? -11.163 0.091   -31.587 1.00 29.71  ? 196 GLY A C   1 
ATOM   1526 O O   . GLY A 1 197 ? -11.190 1.326   -31.654 1.00 30.30  ? 196 GLY A O   1 
ATOM   1527 N N   . GLY A 1 198 ? -12.203 -0.681  -31.887 1.00 28.67  ? 197 GLY A N   1 
ATOM   1528 C CA  . GLY A 1 198 ? -13.467 -0.157  -32.355 1.00 29.64  ? 197 GLY A CA  1 
ATOM   1529 C C   . GLY A 1 198 ? -13.650 -0.338  -33.856 1.00 31.26  ? 197 GLY A C   1 
ATOM   1530 O O   . GLY A 1 198 ? -12.699 -0.524  -34.618 1.00 33.69  ? 197 GLY A O   1 
ATOM   1531 N N   . ARG A 1 199 ? -14.911 -0.296  -34.271 1.00 35.07  ? 198 ARG A N   1 
ATOM   1532 C CA  . ARG A 1 199 ? -15.291 -0.327  -35.673 1.00 31.07  ? 198 ARG A CA  1 
ATOM   1533 C C   . ARG A 1 199 ? -15.245 1.084   -36.237 1.00 32.97  ? 198 ARG A C   1 
ATOM   1534 O O   . ARG A 1 199 ? -15.586 2.043   -35.542 1.00 32.18  ? 198 ARG A O   1 
ATOM   1535 C CB  . ARG A 1 199 ? -16.696 -0.907  -35.804 1.00 33.49  ? 198 ARG A CB  1 
ATOM   1536 C CG  . ARG A 1 199 ? -17.273 -0.898  -37.199 1.00 35.72  ? 198 ARG A CG  1 
ATOM   1537 C CD  . ARG A 1 199 ? -18.727 -1.318  -37.169 1.00 37.88  ? 198 ARG A CD  1 
ATOM   1538 N NE  . ARG A 1 199 ? -19.589 -0.361  -36.479 1.00 36.20  ? 198 ARG A NE  1 
ATOM   1539 C CZ  . ARG A 1 199 ? -20.892 -0.267  -36.703 1.00 37.44  ? 198 ARG A CZ  1 
ATOM   1540 N NH1 . ARG A 1 199 ? -21.492 -1.044  -37.594 1.00 36.34  ? 198 ARG A NH1 1 
ATOM   1541 N NH2 . ARG A 1 199 ? -21.606 0.630   -36.027 1.00 36.17  ? 198 ARG A NH2 1 
ATOM   1542 N N   . ALA A 1 200 ? -14.812 1.209   -37.494 1.00 34.13  ? 199 ALA A N   1 
ATOM   1543 C CA  . ALA A 1 200 ? -14.672 2.508   -38.148 1.00 35.27  ? 199 ALA A CA  1 
ATOM   1544 C C   . ALA A 1 200 ? -14.721 2.322   -39.660 1.00 37.48  ? 199 ALA A C   1 
ATOM   1545 O O   . ALA A 1 200 ? -14.778 1.200   -40.169 1.00 38.71  ? 199 ALA A O   1 
ATOM   1546 C CB  . ALA A 1 200 ? -13.373 3.205   -37.737 1.00 33.96  ? 199 ALA A CB  1 
ATOM   1547 N N   . ASP A 1 201 ? -14.686 3.446   -40.375 1.00 39.31  ? 200 ASP A N   1 
ATOM   1548 C CA  . ASP A 1 201 ? -14.647 3.487   -41.833 1.00 39.80  ? 200 ASP A CA  1 
ATOM   1549 C C   . ASP A 1 201 ? -13.287 4.013   -42.262 1.00 41.37  ? 200 ASP A C   1 
ATOM   1550 O O   . ASP A 1 201 ? -12.797 5.000   -41.698 1.00 44.10  ? 200 ASP A O   1 
ATOM   1551 C CB  . ASP A 1 201 ? -15.753 4.388   -42.384 1.00 42.51  ? 200 ASP A CB  1 
ATOM   1552 C CG  . ASP A 1 201 ? -15.795 4.408   -43.904 1.00 46.60  ? 200 ASP A CG  1 
ATOM   1553 O OD1 . ASP A 1 201 ? -16.235 3.395   -44.498 1.00 46.67  ? 200 ASP A OD1 1 
ATOM   1554 O OD2 . ASP A 1 201 ? -15.408 5.439   -44.501 1.00 46.61  ? 200 ASP A OD2 1 
ATOM   1555 N N   . ARG A 1 202 ? -12.670 3.368   -43.248 1.00 46.29  ? 201 ARG A N   1 
ATOM   1556 C CA  . ARG A 1 202 ? -11.289 3.748   -43.525 1.00 50.45  ? 201 ARG A CA  1 
ATOM   1557 C C   . ARG A 1 202 ? -11.173 5.058   -44.290 1.00 50.48  ? 201 ARG A C   1 
ATOM   1558 O O   . ARG A 1 202 ? -10.044 5.498   -44.554 1.00 49.21  ? 201 ARG A O   1 
ATOM   1559 C CB  . ARG A 1 202 ? -10.522 2.640   -44.273 1.00 47.14  ? 201 ARG A CB  1 
ATOM   1560 C CG  . ARG A 1 202 ? -10.951 2.350   -45.680 1.00 49.95  ? 201 ARG A CG  1 
ATOM   1561 C CD  . ARG A 1 202 ? -10.311 1.045   -46.177 1.00 49.87  ? 201 ARG A CD  1 
ATOM   1562 N NE  . ARG A 1 202 ? -8.920  1.231   -46.562 1.00 46.52  ? 201 ARG A NE  1 
ATOM   1563 C CZ  . ARG A 1 202 ? -8.498  1.394   -47.808 1.00 43.60  ? 201 ARG A CZ  1 
ATOM   1564 N NH1 . ARG A 1 202 ? -9.324  1.312   -48.835 1.00 44.71  ? 201 ARG A NH1 1 
ATOM   1565 N NH2 . ARG A 1 202 ? -7.212  1.644   -48.028 1.00 45.61  ? 201 ARG A NH2 1 
ATOM   1566 N N   . PHE A 1 203 ? -12.286 5.712   -44.621 1.00 42.15  ? 202 PHE A N   1 
ATOM   1567 C CA  . PHE A 1 203 ? -12.183 6.988   -45.301 1.00 45.32  ? 202 PHE A CA  1 
ATOM   1568 C C   . PHE A 1 203 ? -12.800 8.154   -44.547 1.00 45.58  ? 202 PHE A C   1 
ATOM   1569 O O   . PHE A 1 203 ? -12.302 9.276   -44.671 1.00 45.58  ? 202 PHE A O   1 
ATOM   1570 C CB  . PHE A 1 203 ? -12.797 6.886   -46.700 1.00 43.65  ? 202 PHE A CB  1 
ATOM   1571 C CG  . PHE A 1 203 ? -12.015 6.002   -47.624 1.00 43.03  ? 202 PHE A CG  1 
ATOM   1572 C CD1 . PHE A 1 203 ? -10.881 6.474   -48.253 1.00 44.53  ? 202 PHE A CD1 1 
ATOM   1573 C CD2 . PHE A 1 203 ? -12.399 4.690   -47.846 1.00 45.70  ? 202 PHE A CD2 1 
ATOM   1574 C CE1 . PHE A 1 203 ? -10.148 5.661   -49.106 1.00 44.95  ? 202 PHE A CE1 1 
ATOM   1575 C CE2 . PHE A 1 203 ? -11.671 3.874   -48.694 1.00 45.43  ? 202 PHE A CE2 1 
ATOM   1576 C CZ  . PHE A 1 203 ? -10.540 4.363   -49.321 1.00 42.93  ? 202 PHE A CZ  1 
ATOM   1577 N N   . GLY A 1 204 ? -13.842 7.932   -43.756 1.00 45.31  ? 203 GLY A N   1 
ATOM   1578 C CA  . GLY A 1 204 ? -14.501 9.034   -43.098 1.00 41.61  ? 203 GLY A CA  1 
ATOM   1579 C C   . GLY A 1 204 ? -15.444 8.613   -41.998 1.00 40.51  ? 203 GLY A C   1 
ATOM   1580 O O   . GLY A 1 204 ? -15.409 7.474   -41.514 1.00 39.57  ? 203 GLY A O   1 
ATOM   1581 N N   . PRO A 1 205 ? -16.316 9.533   -41.583 1.00 41.47  ? 204 PRO A N   1 
ATOM   1582 C CA  . PRO A 1 205 ? -17.249 9.257   -40.481 1.00 38.54  ? 204 PRO A CA  1 
ATOM   1583 C C   . PRO A 1 205 ? -18.566 8.604   -40.887 1.00 38.00  ? 204 PRO A C   1 
ATOM   1584 O O   . PRO A 1 205 ? -19.493 8.619   -40.073 1.00 42.21  ? 204 PRO A O   1 
ATOM   1585 C CB  . PRO A 1 205 ? -17.513 10.666  -39.932 1.00 38.35  ? 204 PRO A CB  1 
ATOM   1586 C CG  . PRO A 1 205 ? -17.505 11.518  -41.194 1.00 37.38  ? 204 PRO A CG  1 
ATOM   1587 C CD  . PRO A 1 205 ? -16.481 10.901  -42.119 1.00 37.42  ? 204 PRO A CD  1 
ATOM   1588 N N   . PHE A 1 206 ? -18.690 8.039   -42.092 1.00 38.58  ? 205 PHE A N   1 
ATOM   1589 C CA  . PHE A 1 206 ? -19.927 7.419   -42.554 1.00 43.07  ? 205 PHE A CA  1 
ATOM   1590 C C   . PHE A 1 206 ? -19.713 5.977   -42.993 1.00 45.67  ? 205 PHE A C   1 
ATOM   1591 O O   . PHE A 1 206 ? -18.659 5.632   -43.537 1.00 42.62  ? 205 PHE A O   1 
ATOM   1592 C CB  . PHE A 1 206 ? -20.518 8.180   -43.731 1.00 40.91  ? 205 PHE A CB  1 
ATOM   1593 C CG  . PHE A 1 206 ? -20.750 9.617   -43.453 1.00 40.51  ? 205 PHE A CG  1 
ATOM   1594 C CD1 . PHE A 1 206 ? -21.740 10.006  -42.572 1.00 38.56  ? 205 PHE A CD1 1 
ATOM   1595 C CD2 . PHE A 1 206 ? -19.988 10.584  -44.078 1.00 39.60  ? 205 PHE A CD2 1 
ATOM   1596 C CE1 . PHE A 1 206 ? -21.961 11.337  -42.311 1.00 40.01  ? 205 PHE A CE1 1 
ATOM   1597 C CE2 . PHE A 1 206 ? -20.202 11.912  -43.822 1.00 38.96  ? 205 PHE A CE2 1 
ATOM   1598 C CZ  . PHE A 1 206 ? -21.188 12.292  -42.931 1.00 39.68  ? 205 PHE A CZ  1 
ATOM   1599 N N   . HIS A 1 207 ? -20.736 5.140   -42.775 1.00 45.79  ? 206 HIS A N   1 
ATOM   1600 C CA  . HIS A 1 207 ? -20.746 3.813   -43.387 1.00 48.27  ? 206 HIS A CA  1 
ATOM   1601 C C   . HIS A 1 207 ? -20.600 3.951   -44.896 1.00 47.44  ? 206 HIS A C   1 
ATOM   1602 O O   . HIS A 1 207 ? -21.268 4.781   -45.515 1.00 51.09  ? 206 HIS A O   1 
ATOM   1603 C CB  . HIS A 1 207 ? -22.044 3.062   -43.077 1.00 49.21  ? 206 HIS A CB  1 
ATOM   1604 C CG  . HIS A 1 207 ? -22.207 2.672   -41.644 1.00 47.77  ? 206 HIS A CG  1 
ATOM   1605 N ND1 . HIS A 1 207 ? -21.472 1.666   -41.057 1.00 48.46  ? 206 HIS A ND1 1 
ATOM   1606 C CD2 . HIS A 1 207 ? -23.053 3.128   -40.690 1.00 46.81  ? 206 HIS A CD2 1 
ATOM   1607 C CE1 . HIS A 1 207 ? -21.840 1.539   -39.792 1.00 47.61  ? 206 HIS A CE1 1 
ATOM   1608 N NE2 . HIS A 1 207 ? -22.800 2.413   -39.545 1.00 43.81  ? 206 HIS A NE2 1 
ATOM   1609 N N   . SER A 1 208 ? -19.672 3.185   -45.481 1.00 49.34  ? 207 SER A N   1 
ATOM   1610 C CA  . SER A 1 208 ? -19.534 3.191   -46.935 1.00 52.18  ? 207 SER A CA  1 
ATOM   1611 C C   . SER A 1 208 ? -19.091 1.853   -47.519 1.00 52.86  ? 207 SER A C   1 
ATOM   1612 O O   . SER A 1 208 ? -18.524 1.842   -48.616 1.00 54.71  ? 207 SER A O   1 
ATOM   1613 C CB  . SER A 1 208 ? -18.545 4.253   -47.362 1.00 48.40  ? 207 SER A CB  1 
ATOM   1614 O OG  . SER A 1 208 ? -17.259 3.901   -46.921 1.00 48.07  ? 207 SER A OG  1 
ATOM   1615 N N   . ASN A 1 209 ? -19.307 0.741   -46.818 1.00 54.19  ? 208 ASN A N   1 
ATOM   1616 C CA  . ASN A 1 209 ? -18.750 -0.560  -47.194 1.00 53.70  ? 208 ASN A CA  1 
ATOM   1617 C C   . ASN A 1 209 ? -17.218 -0.521  -47.211 1.00 52.64  ? 208 ASN A C   1 
ATOM   1618 O O   . ASN A 1 209 ? -16.573 -1.109  -48.082 1.00 52.67  ? 208 ASN A O   1 
ATOM   1619 C CB  . ASN A 1 209 ? -19.317 -1.038  -48.536 1.00 57.31  ? 208 ASN A CB  1 
ATOM   1620 C CG  . ASN A 1 209 ? -19.246 -2.551  -48.702 1.00 61.68  ? 208 ASN A CG  1 
ATOM   1621 O OD1 . ASN A 1 209 ? -18.859 -3.270  -47.776 1.00 60.33  ? 208 ASN A OD1 1 
ATOM   1622 N ND2 . ASN A 1 209 ? -19.660 -3.044  -49.875 1.00 61.99  ? 208 ASN A ND2 1 
ATOM   1623 N N   . ASN A 1 210 ? -16.632 0.176   -46.236 1.00 49.74  ? 209 ASN A N   1 
ATOM   1624 C CA  . ASN A 1 210 ? -15.182 0.229   -46.028 1.00 47.07  ? 209 ASN A CA  1 
ATOM   1625 C C   . ASN A 1 210 ? -14.869 0.113   -44.540 1.00 47.12  ? 209 ASN A C   1 
ATOM   1626 O O   . ASN A 1 210 ? -14.073 0.873   -43.982 1.00 43.61  ? 209 ASN A O   1 
ATOM   1627 C CB  . ASN A 1 210 ? -14.569 1.508   -46.596 1.00 47.01  ? 209 ASN A CB  1 
ATOM   1628 C CG  . ASN A 1 210 ? -14.481 1.493   -48.106 1.00 50.07  ? 209 ASN A CG  1 
ATOM   1629 O OD1 . ASN A 1 210 ? -13.638 0.805   -48.689 1.00 51.99  ? 209 ASN A OD1 1 
ATOM   1630 N ND2 . ASN A 1 210 ? -15.337 2.273   -48.750 1.00 46.72  ? 209 ASN A ND2 1 
ATOM   1631 N N   . GLU A 1 211 ? -15.516 -0.849  -43.887 1.00 47.93  ? 210 GLU A N   1 
ATOM   1632 C CA  . GLU A 1 211 ? -15.420 -1.013  -42.442 1.00 43.07  ? 210 GLU A CA  1 
ATOM   1633 C C   . GLU A 1 211 ? -14.034 -1.518  -42.045 1.00 37.71  ? 210 GLU A C   1 
ATOM   1634 O O   . GLU A 1 211 ? -13.453 -2.373  -42.710 1.00 36.96  ? 210 GLU A O   1 
ATOM   1635 C CB  . GLU A 1 211 ? -16.521 -1.977  -41.990 1.00 41.92  ? 210 GLU A CB  1 
ATOM   1636 C CG  . GLU A 1 211 ? -16.651 -2.260  -40.504 1.00 38.62  ? 210 GLU A CG  1 
ATOM   1637 C CD  . GLU A 1 211 ? -17.937 -3.021  -40.206 1.00 39.95  ? 210 GLU A CD  1 
ATOM   1638 O OE1 . GLU A 1 211 ? -19.023 -2.473  -40.512 1.00 38.02  ? 210 GLU A OE1 1 
ATOM   1639 O OE2 . GLU A 1 211 ? -17.867 -4.165  -39.694 1.00 41.14  ? 210 GLU A OE2 1 
ATOM   1640 N N   . ILE A 1 212 ? -13.477 -0.960  -40.974 1.00 40.46  ? 211 ILE A N   1 
ATOM   1641 C CA  . ILE A 1 212 ? -12.141 -1.341  -40.528 1.00 39.00  ? 211 ILE A CA  1 
ATOM   1642 C C   . ILE A 1 212 ? -12.116 -1.490  -39.019 1.00 37.34  ? 211 ILE A C   1 
ATOM   1643 O O   . ILE A 1 212 ? -12.928 -0.915  -38.284 1.00 33.66  ? 211 ILE A O   1 
ATOM   1644 C CB  . ILE A 1 212 ? -11.035 -0.345  -40.949 1.00 40.09  ? 211 ILE A CB  1 
ATOM   1645 C CG1 . ILE A 1 212 ? -11.395 1.080   -40.527 1.00 40.12  ? 211 ILE A CG1 1 
ATOM   1646 C CG2 . ILE A 1 212 ? -10.775 -0.430  -42.429 1.00 42.11  ? 211 ILE A CG2 1 
ATOM   1647 C CD1 . ILE A 1 212 ? -10.256 1.817   -39.840 1.00 40.44  ? 211 ILE A CD1 1 
ATOM   1648 N N   . TYR A 1 213 ? -11.127 -2.241  -38.562 1.00 38.81  ? 212 TYR A N   1 
ATOM   1649 C CA  . TYR A 1 213 ? -10.966 -2.537  -37.147 1.00 35.55  ? 212 TYR A CA  1 
ATOM   1650 C C   . TYR A 1 213 ? -9.637  -1.957  -36.686 1.00 35.64  ? 212 TYR A C   1 
ATOM   1651 O O   . TYR A 1 213 ? -8.566  -2.396  -37.128 1.00 38.79  ? 212 TYR A O   1 
ATOM   1652 C CB  . TYR A 1 213 ? -11.136 -4.041  -36.919 1.00 34.35  ? 212 TYR A CB  1 
ATOM   1653 C CG  . TYR A 1 213 ? -12.611 -4.300  -37.085 1.00 34.54  ? 212 TYR A CG  1 
ATOM   1654 C CD1 . TYR A 1 213 ? -13.162 -4.585  -38.335 1.00 34.45  ? 212 TYR A CD1 1 
ATOM   1655 C CD2 . TYR A 1 213 ? -13.476 -4.113  -36.013 1.00 34.80  ? 212 TYR A CD2 1 
ATOM   1656 C CE1 . TYR A 1 213 ? -14.538 -4.749  -38.478 1.00 38.38  ? 212 TYR A CE1 1 
ATOM   1657 C CE2 . TYR A 1 213 ? -14.840 -4.273  -36.146 1.00 34.41  ? 212 TYR A CE2 1 
ATOM   1658 C CZ  . TYR A 1 213 ? -15.374 -4.580  -37.374 1.00 34.60  ? 212 TYR A CZ  1 
ATOM   1659 O OH  . TYR A 1 213 ? -16.747 -4.726  -37.472 1.00 36.98  ? 212 TYR A OH  1 
ATOM   1660 N N   . CYS A 1 214 ? -9.732  -0.928  -35.840 1.00 34.52  ? 213 CYS A N   1 
ATOM   1661 C CA  . CYS A 1 214 ? -8.575  -0.138  -35.436 1.00 36.43  ? 213 CYS A CA  1 
ATOM   1662 C C   . CYS A 1 214 ? -7.665  -0.923  -34.501 1.00 34.63  ? 213 CYS A C   1 
ATOM   1663 O O   . CYS A 1 214 ? -8.137  -1.680  -33.648 1.00 33.13  ? 213 CYS A O   1 
ATOM   1664 C CB  . CYS A 1 214 ? -9.036  1.139   -34.743 1.00 31.43  ? 213 CYS A CB  1 
ATOM   1665 S SG  . CYS A 1 214 ? -10.124 2.115   -35.769 1.00 38.55  ? 213 CYS A SG  1 
ATOM   1666 N N   . ASN A 1 215 ? -6.345  -0.749  -34.673 1.00 32.04  ? 214 ASN A N   1 
ATOM   1667 C CA  . ASN A 1 215 ? -5.416  -1.206  -33.652 1.00 30.57  ? 214 ASN A CA  1 
ATOM   1668 C C   . ASN A 1 215 ? -4.237  -0.264  -33.407 1.00 33.51  ? 214 ASN A C   1 
ATOM   1669 O O   . ASN A 1 215 ? -3.354  -0.609  -32.617 1.00 32.78  ? 214 ASN A O   1 
ATOM   1670 C CB  . ASN A 1 215 ? -4.906  -2.611  -33.985 1.00 30.75  ? 214 ASN A CB  1 
ATOM   1671 C CG  . ASN A 1 215 ? -4.127  -2.659  -35.275 1.00 37.43  ? 214 ASN A CG  1 
ATOM   1672 O OD1 . ASN A 1 215 ? -3.981  -1.644  -35.969 1.00 39.52  ? 214 ASN A OD1 1 
ATOM   1673 N ND2 . ASN A 1 215 ? -3.611  -3.846  -35.611 1.00 35.17  ? 214 ASN A ND2 1 
ATOM   1674 N N   . ARG A 1 216 ? -4.178  0.902   -34.045 1.00 34.44  ? 215 ARG A N   1 
ATOM   1675 C CA  . ARG A 1 216 ? -3.162  1.884   -33.672 1.00 32.52  ? 215 ARG A CA  1 
ATOM   1676 C C   . ARG A 1 216 ? -3.716  2.660   -32.484 1.00 32.37  ? 215 ARG A C   1 
ATOM   1677 O O   . ARG A 1 216 ? -4.612  3.501   -32.628 1.00 32.35  ? 215 ARG A O   1 
ATOM   1678 C CB  . ARG A 1 216 ? -2.799  2.805   -34.836 1.00 31.90  ? 215 ARG A CB  1 
ATOM   1679 N N   . ILE A 1 217 ? -3.188  2.355   -31.297 1.00 28.94  ? 216 ILE A N   1 
ATOM   1680 C CA  . ILE A 1 217 ? -3.661  2.989   -30.078 1.00 27.81  ? 216 ILE A CA  1 
ATOM   1681 C C   . ILE A 1 217 ? -3.486  4.500   -30.179 1.00 29.00  ? 216 ILE A C   1 
ATOM   1682 O O   . ILE A 1 217 ? -2.529  4.998   -30.776 1.00 34.55  ? 216 ILE A O   1 
ATOM   1683 C CB  . ILE A 1 217 ? -2.904  2.400   -28.880 1.00 30.03  ? 216 ILE A CB  1 
ATOM   1684 C CG1 . ILE A 1 217 ? -3.563  2.799   -27.574 1.00 27.91  ? 216 ILE A CG1 1 
ATOM   1685 C CG2 . ILE A 1 217 ? -1.423  2.834   -28.886 1.00 28.46  ? 216 ILE A CG2 1 
ATOM   1686 C CD1 . ILE A 1 217 ? -2.944  2.110   -26.415 1.00 27.43  ? 216 ILE A CD1 1 
ATOM   1687 N N   . ARG A 1 218 ? -4.428  5.240   -29.620 1.00 31.56  ? 217 ARG A N   1 
ATOM   1688 C CA  . ARG A 1 218 ? -4.375  6.691   -29.634 1.00 31.56  ? 217 ARG A CA  1 
ATOM   1689 C C   . ARG A 1 218 ? -4.458  7.199   -28.203 1.00 31.29  ? 217 ARG A C   1 
ATOM   1690 O O   . ARG A 1 218 ? -5.117  6.590   -27.346 1.00 31.58  ? 217 ARG A O   1 
ATOM   1691 C CB  . ARG A 1 218 ? -5.498  7.282   -30.492 1.00 28.71  ? 217 ARG A CB  1 
ATOM   1692 C CG  . ARG A 1 218 ? -5.537  6.746   -31.927 1.00 31.92  ? 217 ARG A CG  1 
ATOM   1693 C CD  . ARG A 1 218 ? -4.285  7.073   -32.739 1.00 34.13  ? 217 ARG A CD  1 
ATOM   1694 N NE  . ARG A 1 218 ? -3.760  8.398   -32.425 1.00 42.33  ? 217 ARG A NE  1 
ATOM   1695 C CZ  . ARG A 1 218 ? -4.218  9.548   -32.919 1.00 45.05  ? 217 ARG A CZ  1 
ATOM   1696 N NH1 . ARG A 1 218 ? -5.193  9.584   -33.818 1.00 42.27  ? 217 ARG A NH1 1 
ATOM   1697 N NH2 . ARG A 1 218 ? -3.683  10.694  -32.499 1.00 41.56  ? 217 ARG A NH2 1 
ATOM   1698 N N   . VAL A 1 219 ? -3.753  8.299   -27.938 1.00 30.10  ? 218 VAL A N   1 
ATOM   1699 C CA  . VAL A 1 219 ? -3.560  8.799   -26.580 1.00 30.61  ? 218 VAL A CA  1 
ATOM   1700 C C   . VAL A 1 219 ? -3.978  10.256  -26.525 1.00 32.78  ? 218 VAL A C   1 
ATOM   1701 O O   . VAL A 1 219 ? -3.501  11.076  -27.319 1.00 35.36  ? 218 VAL A O   1 
ATOM   1702 C CB  . VAL A 1 219 ? -2.103  8.659   -26.105 1.00 30.95  ? 218 VAL A CB  1 
ATOM   1703 C CG1 . VAL A 1 219 ? -1.978  9.159   -24.680 1.00 32.68  ? 218 VAL A CG1 1 
ATOM   1704 C CG2 . VAL A 1 219 ? -1.648  7.224   -26.204 1.00 31.92  ? 218 VAL A CG2 1 
ATOM   1705 N N   . PHE A 1 220 ? -4.836  10.582  -25.566 1.00 31.72  ? 219 PHE A N   1 
ATOM   1706 C CA  . PHE A 1 220 ? -5.321  11.938  -25.358 1.00 33.13  ? 219 PHE A CA  1 
ATOM   1707 C C   . PHE A 1 220 ? -4.866  12.433  -23.989 1.00 34.55  ? 219 PHE A C   1 
ATOM   1708 O O   . PHE A 1 220 ? -5.234  11.853  -22.958 1.00 31.07  ? 219 PHE A O   1 
ATOM   1709 C CB  . PHE A 1 220 ? -6.846  11.982  -25.472 1.00 33.01  ? 219 PHE A CB  1 
ATOM   1710 C CG  . PHE A 1 220 ? -7.434  13.340  -25.217 1.00 35.67  ? 219 PHE A CG  1 
ATOM   1711 C CD1 . PHE A 1 220 ? -7.173  14.401  -26.087 1.00 35.55  ? 219 PHE A CD1 1 
ATOM   1712 C CD2 . PHE A 1 220 ? -8.251  13.558  -24.114 1.00 31.74  ? 219 PHE A CD2 1 
ATOM   1713 C CE1 . PHE A 1 220 ? -7.716  15.650  -25.856 1.00 35.08  ? 219 PHE A CE1 1 
ATOM   1714 C CE2 . PHE A 1 220 ? -8.793  14.802  -23.874 1.00 32.35  ? 219 PHE A CE2 1 
ATOM   1715 C CZ  . PHE A 1 220 ? -8.532  15.853  -24.746 1.00 35.16  ? 219 PHE A CZ  1 
ATOM   1716 N N   . ASP A 1 221 ? -4.092  13.520  -23.981 1.00 35.53  ? 220 ASP A N   1 
ATOM   1717 C CA  . ASP A 1 221 ? -3.681  14.157  -22.736 1.00 37.59  ? 220 ASP A CA  1 
ATOM   1718 C C   . ASP A 1 221 ? -4.774  15.114  -22.279 1.00 36.96  ? 220 ASP A C   1 
ATOM   1719 O O   . ASP A 1 221 ? -5.085  16.076  -22.986 1.00 36.97  ? 220 ASP A O   1 
ATOM   1720 C CB  . ASP A 1 221 ? -2.365  14.907  -22.926 1.00 35.46  ? 220 ASP A CB  1 
ATOM   1721 C CG  . ASP A 1 221 ? -1.949  15.675  -21.685 1.00 38.25  ? 220 ASP A CG  1 
ATOM   1722 O OD1 . ASP A 1 221 ? -2.374  15.310  -20.571 1.00 37.43  ? 220 ASP A OD1 1 
ATOM   1723 O OD2 . ASP A 1 221 ? -1.186  16.654  -21.826 1.00 45.18  ? 220 ASP A OD2 1 
ATOM   1724 N N   . THR A 1 222 ? -5.360  14.849  -21.100 1.00 35.93  ? 221 THR A N   1 
ATOM   1725 C CA  . THR A 1 222 ? -6.405  15.726  -20.571 1.00 37.86  ? 221 THR A CA  1 
ATOM   1726 C C   . THR A 1 222 ? -5.859  17.031  -19.997 1.00 40.77  ? 221 THR A C   1 
ATOM   1727 O O   . THR A 1 222 ? -6.613  18.004  -19.912 1.00 39.68  ? 221 THR A O   1 
ATOM   1728 C CB  . THR A 1 222 ? -7.246  15.019  -19.490 1.00 34.97  ? 221 THR A CB  1 
ATOM   1729 O OG1 . THR A 1 222 ? -6.424  14.644  -18.384 1.00 35.54  ? 221 THR A OG1 1 
ATOM   1730 C CG2 . THR A 1 222 ? -7.935  13.786  -20.039 1.00 32.53  ? 221 THR A CG2 1 
ATOM   1731 N N   . ARG A 1 223 ? -4.584  17.081  -19.589 1.00 41.35  ? 222 ARG A N   1 
ATOM   1732 C CA  . ARG A 1 223 ? -4.033  18.332  -19.077 1.00 41.57  ? 222 ARG A CA  1 
ATOM   1733 C C   . ARG A 1 223 ? -3.959  19.384  -20.179 1.00 42.17  ? 222 ARG A C   1 
ATOM   1734 O O   . ARG A 1 223 ? -4.382  20.528  -19.990 1.00 44.21  ? 222 ARG A O   1 
ATOM   1735 C CB  . ARG A 1 223 ? -2.649  18.103  -18.446 1.00 43.38  ? 222 ARG A CB  1 
ATOM   1736 C CG  . ARG A 1 223 ? -2.273  19.172  -17.406 1.00 49.70  ? 222 ARG A CG  1 
ATOM   1737 C CD  . ARG A 1 223 ? -0.823  19.720  -17.512 1.00 56.31  ? 222 ARG A CD  1 
ATOM   1738 N NE  . ARG A 1 223 ? -0.686  21.003  -16.813 1.00 62.12  ? 222 ARG A NE  1 
ATOM   1739 C CZ  . ARG A 1 223 ? 0.447   21.496  -16.314 1.00 66.39  ? 222 ARG A CZ  1 
ATOM   1740 N NH1 . ARG A 1 223 ? 1.594   20.830  -16.397 1.00 62.49  ? 222 ARG A NH1 1 
ATOM   1741 N NH2 . ARG A 1 223 ? 0.428   22.687  -15.705 1.00 60.61  ? 222 ARG A NH2 1 
ATOM   1742 N N   . THR A 1 224 ? -3.427  19.024  -21.340 1.00 41.01  ? 223 THR A N   1 
ATOM   1743 C CA  . THR A 1 224 ? -3.319  19.971  -22.442 1.00 41.15  ? 223 THR A CA  1 
ATOM   1744 C C   . THR A 1 224 ? -4.453  19.825  -23.440 1.00 40.58  ? 223 THR A C   1 
ATOM   1745 O O   . THR A 1 224 ? -4.483  20.563  -24.435 1.00 43.53  ? 223 THR A O   1 
ATOM   1746 C CB  . THR A 1 224 ? -1.974  19.813  -23.167 1.00 38.99  ? 223 THR A CB  1 
ATOM   1747 O OG1 . THR A 1 224 ? -1.879  18.492  -23.719 1.00 40.50  ? 223 THR A OG1 1 
ATOM   1748 C CG2 . THR A 1 224 ? -0.829  20.036  -22.210 1.00 35.22  ? 223 THR A CG2 1 
ATOM   1749 N N   . GLU A 1 225 ? -5.380  18.904  -23.188 1.00 38.90  ? 224 GLU A N   1 
ATOM   1750 C CA  . GLU A 1 225 ? -6.464  18.554  -24.102 1.00 37.30  ? 224 GLU A CA  1 
ATOM   1751 C C   . GLU A 1 225 ? -5.960  18.457  -25.543 1.00 38.29  ? 224 GLU A C   1 
ATOM   1752 O O   . GLU A 1 225 ? -6.426  19.152  -26.446 1.00 37.94  ? 224 GLU A O   1 
ATOM   1753 C CB  . GLU A 1 225 ? -7.627  19.530  -23.962 1.00 35.41  ? 224 GLU A CB  1 
ATOM   1754 C CG  . GLU A 1 225 ? -8.429  19.244  -22.693 1.00 35.89  ? 224 GLU A CG  1 
ATOM   1755 C CD  . GLU A 1 225 ? -9.551  20.233  -22.423 1.00 38.21  ? 224 GLU A CD  1 
ATOM   1756 O OE1 . GLU A 1 225 ? -9.604  21.300  -23.076 1.00 41.25  ? 224 GLU A OE1 1 
ATOM   1757 O OE2 . GLU A 1 225 ? -10.386 19.941  -21.540 1.00 34.62  ? 224 GLU A OE2 1 
ATOM   1758 N N   . ALA A 1 226 ? -4.988  17.555  -25.737 1.00 36.89  ? 225 ALA A N   1 
ATOM   1759 C CA  . ALA A 1 226 ? -4.366  17.322  -27.034 1.00 38.27  ? 225 ALA A CA  1 
ATOM   1760 C C   . ALA A 1 226 ? -4.238  15.831  -27.326 1.00 36.13  ? 225 ALA A C   1 
ATOM   1761 O O   . ALA A 1 226 ? -3.883  15.041  -26.446 1.00 35.58  ? 225 ALA A O   1 
ATOM   1762 C CB  . ALA A 1 226 ? -2.980  17.972  -27.103 1.00 38.84  ? 225 ALA A CB  1 
ATOM   1763 N N   . TRP A 1 227 ? -4.511  15.453  -28.572 1.00 37.33  ? 226 TRP A N   1 
ATOM   1764 C CA  . TRP A 1 227 ? -4.154  14.123  -29.050 1.00 36.98  ? 226 TRP A CA  1 
ATOM   1765 C C   . TRP A 1 227 ? -2.651  14.078  -29.319 1.00 39.89  ? 226 TRP A C   1 
ATOM   1766 O O   . TRP A 1 227 ? -2.108  14.941  -30.016 1.00 40.45  ? 226 TRP A O   1 
ATOM   1767 C CB  . TRP A 1 227 ? -4.935  13.775  -30.316 1.00 36.32  ? 226 TRP A CB  1 
ATOM   1768 C CG  . TRP A 1 227 ? -6.445  13.610  -30.125 1.00 37.31  ? 226 TRP A CG  1 
ATOM   1769 C CD1 . TRP A 1 227 ? -7.415  14.550  -30.364 1.00 37.08  ? 226 TRP A CD1 1 
ATOM   1770 C CD2 . TRP A 1 227 ? -7.137  12.433  -29.668 1.00 36.73  ? 226 TRP A CD2 1 
ATOM   1771 N NE1 . TRP A 1 227 ? -8.664  14.030  -30.089 1.00 34.43  ? 226 TRP A NE1 1 
ATOM   1772 C CE2 . TRP A 1 227 ? -8.522  12.737  -29.657 1.00 34.89  ? 226 TRP A CE2 1 
ATOM   1773 C CE3 . TRP A 1 227 ? -6.719  11.155  -29.257 1.00 33.01  ? 226 TRP A CE3 1 
ATOM   1774 C CZ2 . TRP A 1 227 ? -9.490  11.809  -29.256 1.00 32.83  ? 226 TRP A CZ2 1 
ATOM   1775 C CZ3 . TRP A 1 227 ? -7.685  10.233  -28.856 1.00 33.56  ? 226 TRP A CZ3 1 
ATOM   1776 C CH2 . TRP A 1 227 ? -9.057  10.566  -28.863 1.00 33.03  ? 226 TRP A CH2 1 
ATOM   1777 N N   . LEU A 1 228 ? -1.979  13.085  -28.756 1.00 39.59  ? 227 LEU A N   1 
ATOM   1778 C CA  . LEU A 1 228 ? -0.527  13.018  -28.801 1.00 39.48  ? 227 LEU A CA  1 
ATOM   1779 C C   . LEU A 1 228 ? -0.054  12.220  -30.012 1.00 42.30  ? 227 LEU A C   1 
ATOM   1780 O O   . LEU A 1 228 ? -0.740  11.309  -30.479 1.00 40.96  ? 227 LEU A O   1 
ATOM   1781 C CB  . LEU A 1 228 ? 0.021   12.381  -27.518 1.00 39.69  ? 227 LEU A CB  1 
ATOM   1782 C CG  . LEU A 1 228 ? -0.244  13.074  -26.177 1.00 37.61  ? 227 LEU A CG  1 
ATOM   1783 C CD1 . LEU A 1 228 ? 0.489   12.384  -25.036 1.00 32.28  ? 227 LEU A CD1 1 
ATOM   1784 C CD2 . LEU A 1 228 ? 0.148   14.546  -26.244 1.00 37.35  ? 227 LEU A CD2 1 
ATOM   1785 N N   . ASP A 1 229 ? 1.126   12.586  -30.526 1.00 43.57  ? 228 ASP A N   1 
ATOM   1786 C CA  . ASP A 1 229 ? 1.861   11.751  -31.468 1.00 43.31  ? 228 ASP A CA  1 
ATOM   1787 C C   . ASP A 1 229 ? 2.736   10.790  -30.683 1.00 39.54  ? 228 ASP A C   1 
ATOM   1788 O O   . ASP A 1 229 ? 3.547   11.215  -29.864 1.00 41.08  ? 228 ASP A O   1 
ATOM   1789 C CB  . ASP A 1 229 ? 2.742   12.577  -32.399 1.00 45.57  ? 228 ASP A CB  1 
ATOM   1790 C CG  . ASP A 1 229 ? 1.964   13.580  -33.187 1.00 57.77  ? 228 ASP A CG  1 
ATOM   1791 O OD1 . ASP A 1 229 ? 2.434   14.744  -33.278 1.00 61.63  ? 228 ASP A OD1 1 
ATOM   1792 O OD2 . ASP A 1 229 ? 0.883   13.198  -33.709 1.00 56.21  ? 228 ASP A OD2 1 
ATOM   1793 N N   . CYS A 1 230 ? 2.607   9.510   -30.962 1.00 37.04  ? 229 CYS A N   1 
ATOM   1794 C CA  . CYS A 1 230 ? 3.216   8.481   -30.141 1.00 38.20  ? 229 CYS A CA  1 
ATOM   1795 C C   . CYS A 1 230 ? 4.056   7.520   -30.966 1.00 38.48  ? 229 CYS A C   1 
ATOM   1796 O O   . CYS A 1 230 ? 3.808   7.327   -32.160 1.00 40.08  ? 229 CYS A O   1 
ATOM   1797 C CB  . CYS A 1 230 ? 2.118   7.715   -29.405 1.00 40.36  ? 229 CYS A CB  1 
ATOM   1798 S SG  . CYS A 1 230 ? 1.254   8.752   -28.231 1.00 50.67  ? 229 CYS A SG  1 
ATOM   1799 N N   . PRO A 1 231 ? 5.049   6.889   -30.351 1.00 38.95  ? 230 PRO A N   1 
ATOM   1800 C CA  . PRO A 1 231 ? 5.990   6.053   -31.108 1.00 39.83  ? 230 PRO A CA  1 
ATOM   1801 C C   . PRO A 1 231 ? 5.316   4.817   -31.676 1.00 36.17  ? 230 PRO A C   1 
ATOM   1802 O O   . PRO A 1 231 ? 4.256   4.397   -31.192 1.00 41.42  ? 230 PRO A O   1 
ATOM   1803 C CB  . PRO A 1 231 ? 7.051   5.682   -30.061 1.00 39.03  ? 230 PRO A CB  1 
ATOM   1804 C CG  . PRO A 1 231 ? 6.369   5.832   -28.768 1.00 39.91  ? 230 PRO A CG  1 
ATOM   1805 C CD  . PRO A 1 231 ? 5.390   6.939   -28.921 1.00 38.34  ? 230 PRO A CD  1 
ATOM   1806 N N   . PRO A 1 232 ? 5.893   4.215   -32.716 1.00 39.40  ? 231 PRO A N   1 
ATOM   1807 C CA  . PRO A 1 232 ? 5.325   2.978   -33.256 1.00 39.67  ? 231 PRO A CA  1 
ATOM   1808 C C   . PRO A 1 232 ? 5.356   1.855   -32.232 1.00 43.26  ? 231 PRO A C   1 
ATOM   1809 O O   . PRO A 1 232 ? 6.187   1.818   -31.322 1.00 44.18  ? 231 PRO A O   1 
ATOM   1810 C CB  . PRO A 1 232 ? 6.235   2.655   -34.448 1.00 33.03  ? 231 PRO A CB  1 
ATOM   1811 C CG  . PRO A 1 232 ? 6.910   3.903   -34.763 1.00 34.22  ? 231 PRO A CG  1 
ATOM   1812 C CD  . PRO A 1 232 ? 7.085   4.630   -33.474 1.00 38.32  ? 231 PRO A CD  1 
ATOM   1813 N N   . THR A 1 233 ? 4.422   0.942   -32.375 1.00 42.04  ? 232 THR A N   1 
ATOM   1814 C CA  . THR A 1 233 ? 4.476   -0.289  -31.603 1.00 47.55  ? 232 THR A CA  1 
ATOM   1815 C C   . THR A 1 233 ? 4.874   -1.425  -32.534 1.00 48.67  ? 232 THR A C   1 
ATOM   1816 O O   . THR A 1 233 ? 4.095   -1.781  -33.431 1.00 52.45  ? 232 THR A O   1 
ATOM   1817 C CB  . THR A 1 233 ? 3.128   -0.569  -30.941 1.00 42.65  ? 232 THR A CB  1 
ATOM   1818 O OG1 . THR A 1 233 ? 2.085   -0.511  -31.933 1.00 38.90  ? 232 THR A OG1 1 
ATOM   1819 C CG2 . THR A 1 233 ? 2.872   0.482   -29.836 1.00 35.43  ? 232 THR A CG2 1 
ATOM   1820 N N   . PRO A 1 234 ? 6.064   -2.010  -32.380 1.00 55.84  ? 233 PRO A N   1 
ATOM   1821 C CA  . PRO A 1 234 ? 6.448   -3.128  -33.272 1.00 55.58  ? 233 PRO A CA  1 
ATOM   1822 C C   . PRO A 1 234 ? 5.473   -4.301  -33.236 1.00 55.40  ? 233 PRO A C   1 
ATOM   1823 O O   . PRO A 1 234 ? 5.219   -4.936  -34.272 1.00 56.58  ? 233 PRO A O   1 
ATOM   1824 C CB  . PRO A 1 234 ? 7.839   -3.527  -32.747 1.00 54.22  ? 233 PRO A CB  1 
ATOM   1825 C CG  . PRO A 1 234 ? 7.855   -3.069  -31.297 1.00 54.99  ? 233 PRO A CG  1 
ATOM   1826 C CD  . PRO A 1 234 ? 7.027   -1.803  -31.280 1.00 57.27  ? 233 PRO A CD  1 
ATOM   1827 N N   . VAL A 1 235 ? 4.917   -4.593  -32.064 1.00 48.28  ? 234 VAL A N   1 
ATOM   1828 C CA  . VAL A 1 235 ? 3.984   -5.688  -31.848 1.00 43.09  ? 234 VAL A CA  1 
ATOM   1829 C C   . VAL A 1 235 ? 2.676   -5.100  -31.354 1.00 40.42  ? 234 VAL A C   1 
ATOM   1830 O O   . VAL A 1 235 ? 2.672   -4.196  -30.510 1.00 41.53  ? 234 VAL A O   1 
ATOM   1831 C CB  . VAL A 1 235 ? 4.539   -6.695  -30.826 1.00 43.95  ? 234 VAL A CB  1 
ATOM   1832 C CG1 . VAL A 1 235 ? 3.466   -7.692  -30.423 1.00 42.76  ? 234 VAL A CG1 1 
ATOM   1833 C CG2 . VAL A 1 235 ? 5.768   -7.379  -31.384 1.00 42.35  ? 234 VAL A CG2 1 
ATOM   1834 N N   . LEU A 1 236 ? 1.566   -5.602  -31.876 1.00 39.83  ? 235 LEU A N   1 
ATOM   1835 C CA  . LEU A 1 236 ? 0.280   -5.041  -31.493 1.00 36.26  ? 235 LEU A CA  1 
ATOM   1836 C C   . LEU A 1 236 ? -0.808  -6.095  -31.622 1.00 33.50  ? 235 LEU A C   1 
ATOM   1837 O O   . LEU A 1 236 ? -0.679  -7.037  -32.411 1.00 32.42  ? 235 LEU A O   1 
ATOM   1838 C CB  . LEU A 1 236 ? -0.067  -3.805  -32.333 1.00 34.85  ? 235 LEU A CB  1 
ATOM   1839 C CG  . LEU A 1 236 ? -0.273  -3.895  -33.843 1.00 36.35  ? 235 LEU A CG  1 
ATOM   1840 C CD1 . LEU A 1 236 ? -0.749  -2.529  -34.297 1.00 34.87  ? 235 LEU A CD1 1 
ATOM   1841 C CD2 . LEU A 1 236 ? 0.991   -4.295  -34.575 1.00 38.36  ? 235 LEU A CD2 1 
ATOM   1842 N N   . PRO A 1 237 ? -1.883  -5.968  -30.862 1.00 34.67  ? 236 PRO A N   1 
ATOM   1843 C CA  . PRO A 1 237 ? -2.996  -6.901  -31.018 1.00 33.06  ? 236 PRO A CA  1 
ATOM   1844 C C   . PRO A 1 237 ? -3.725  -6.657  -32.328 1.00 34.52  ? 236 PRO A C   1 
ATOM   1845 O O   . PRO A 1 237 ? -3.659  -5.579  -32.925 1.00 35.50  ? 236 PRO A O   1 
ATOM   1846 C CB  . PRO A 1 237 ? -3.888  -6.598  -29.813 1.00 33.71  ? 236 PRO A CB  1 
ATOM   1847 C CG  . PRO A 1 237 ? -3.528  -5.226  -29.406 1.00 31.59  ? 236 PRO A CG  1 
ATOM   1848 C CD  . PRO A 1 237 ? -2.136  -4.943  -29.834 1.00 30.93  ? 236 PRO A CD  1 
ATOM   1849 N N   . GLU A 1 238 ? -4.403  -7.703  -32.786 1.00 34.64  ? 237 GLU A N   1 
ATOM   1850 C CA  . GLU A 1 238 ? -5.275  -7.587  -33.942 1.00 34.03  ? 237 GLU A CA  1 
ATOM   1851 C C   . GLU A 1 238 ? -6.380  -6.557  -33.686 1.00 35.54  ? 237 GLU A C   1 
ATOM   1852 O O   . GLU A 1 238 ? -6.939  -6.478  -32.584 1.00 32.56  ? 237 GLU A O   1 
ATOM   1853 C CB  . GLU A 1 238 ? -5.886  -8.953  -34.244 1.00 32.52  ? 237 GLU A CB  1 
ATOM   1854 C CG  . GLU A 1 238 ? -6.499  -9.054  -35.593 1.00 39.23  ? 237 GLU A CG  1 
ATOM   1855 C CD  . GLU A 1 238 ? -5.469  -9.389  -36.646 1.00 49.35  ? 237 GLU A CD  1 
ATOM   1856 O OE1 . GLU A 1 238 ? -4.710  -10.365 -36.435 1.00 50.95  ? 237 GLU A OE1 1 
ATOM   1857 O OE2 . GLU A 1 238 ? -5.412  -8.671  -37.671 1.00 48.19  ? 237 GLU A OE2 1 
ATOM   1858 N N   . GLY A 1 239 ? -6.707  -5.772  -34.715 1.00 33.92  ? 238 GLY A N   1 
ATOM   1859 C CA  . GLY A 1 239 ? -7.843  -4.864  -34.610 1.00 36.05  ? 238 GLY A CA  1 
ATOM   1860 C C   . GLY A 1 239 ? -9.127  -5.589  -34.240 1.00 34.85  ? 238 GLY A C   1 
ATOM   1861 O O   . GLY A 1 239 ? -9.342  -6.749  -34.596 1.00 34.32  ? 238 GLY A O   1 
ATOM   1862 N N   . ARG A 1 240 ? -9.994  -4.894  -33.507 1.00 31.70  ? 239 ARG A N   1 
ATOM   1863 C CA  . ARG A 1 240 ? -11.185 -5.532  -32.956 1.00 30.59  ? 239 ARG A CA  1 
ATOM   1864 C C   . ARG A 1 240 ? -12.127 -4.464  -32.424 1.00 32.80  ? 239 ARG A C   1 
ATOM   1865 O O   . ARG A 1 240 ? -11.734 -3.318  -32.179 1.00 33.50  ? 239 ARG A O   1 
ATOM   1866 C CB  . ARG A 1 240 ? -10.829 -6.477  -31.816 1.00 31.29  ? 239 ARG A CB  1 
ATOM   1867 C CG  . ARG A 1 240 ? -10.258 -5.685  -30.648 1.00 30.37  ? 239 ARG A CG  1 
ATOM   1868 C CD  . ARG A 1 240 ? -9.544  -6.561  -29.679 1.00 30.30  ? 239 ARG A CD  1 
ATOM   1869 N NE  . ARG A 1 240 ? -8.442  -7.264  -30.312 1.00 32.00  ? 239 ARG A NE  1 
ATOM   1870 C CZ  . ARG A 1 240 ? -7.924  -8.388  -29.840 1.00 35.11  ? 239 ARG A CZ  1 
ATOM   1871 N NH1 . ARG A 1 240 ? -8.446  -8.995  -28.785 1.00 32.11  ? 239 ARG A NH1 1 
ATOM   1872 N NH2 . ARG A 1 240 ? -6.849  -8.910  -30.432 1.00 37.97  ? 239 ARG A NH2 1 
ATOM   1873 N N   . ARG A 1 241 ? -13.368 -4.873  -32.204 1.00 30.85  ? 240 ARG A N   1 
ATOM   1874 C CA  . ARG A 1 241 ? -14.351 -4.058  -31.517 1.00 30.90  ? 240 ARG A CA  1 
ATOM   1875 C C   . ARG A 1 241 ? -14.918 -4.871  -30.362 1.00 32.27  ? 240 ARG A C   1 
ATOM   1876 O O   . ARG A 1 241 ? -14.809 -6.102  -30.336 1.00 29.82  ? 240 ARG A O   1 
ATOM   1877 C CB  . ARG A 1 241 ? -15.488 -3.633  -32.443 1.00 30.62  ? 240 ARG A CB  1 
ATOM   1878 C CG  . ARG A 1 241 ? -16.502 -4.734  -32.654 1.00 28.87  ? 240 ARG A CG  1 
ATOM   1879 C CD  . ARG A 1 241 ? -17.554 -4.289  -33.606 1.00 33.52  ? 240 ARG A CD  1 
ATOM   1880 N NE  . ARG A 1 241 ? -18.689 -5.201  -33.621 1.00 36.30  ? 240 ARG A NE  1 
ATOM   1881 C CZ  . ARG A 1 241 ? -19.127 -5.832  -34.698 1.00 34.09  ? 240 ARG A CZ  1 
ATOM   1882 N NH1 . ARG A 1 241 ? -18.551 -5.661  -35.874 1.00 32.94  ? 240 ARG A NH1 1 
ATOM   1883 N NH2 . ARG A 1 241 ? -20.160 -6.664  -34.586 1.00 35.40  ? 240 ARG A NH2 1 
ATOM   1884 N N   . SER A 1 242 ? -15.527 -4.168  -29.401 1.00 28.86  ? 241 SER A N   1 
ATOM   1885 C CA  . SER A 1 242 ? -16.275 -4.798  -28.318 1.00 29.76  ? 241 SER A CA  1 
ATOM   1886 C C   . SER A 1 242 ? -15.400 -5.659  -27.421 1.00 27.73  ? 241 SER A C   1 
ATOM   1887 O O   . SER A 1 242 ? -15.898 -6.545  -26.726 1.00 28.61  ? 241 SER A O   1 
ATOM   1888 C CB  . SER A 1 242 ? -17.441 -5.622  -28.866 1.00 25.85  ? 241 SER A CB  1 
ATOM   1889 O OG  . SER A 1 242 ? -18.391 -4.743  -29.393 1.00 27.76  ? 241 SER A OG  1 
ATOM   1890 N N   . HIS A 1 243 ? -14.099 -5.428  -27.455 1.00 27.92  ? 242 HIS A N   1 
ATOM   1891 C CA  . HIS A 1 243 ? -13.215 -5.862  -26.395 1.00 27.44  ? 242 HIS A CA  1 
ATOM   1892 C C   . HIS A 1 243 ? -13.596 -5.154  -25.090 1.00 28.19  ? 242 HIS A C   1 
ATOM   1893 O O   . HIS A 1 243 ? -14.387 -4.212  -25.075 1.00 25.95  ? 242 HIS A O   1 
ATOM   1894 C CB  . HIS A 1 243 ? -11.775 -5.537  -26.773 1.00 23.90  ? 242 HIS A CB  1 
ATOM   1895 C CG  . HIS A 1 243 ? -11.573 -4.095  -27.106 1.00 25.25  ? 242 HIS A CG  1 
ATOM   1896 N ND1 . HIS A 1 243 ? -12.086 -3.515  -28.247 1.00 26.92  ? 242 HIS A ND1 1 
ATOM   1897 C CD2 . HIS A 1 243 ? -10.936 -3.105  -26.438 1.00 28.39  ? 242 HIS A CD2 1 
ATOM   1898 C CE1 . HIS A 1 243 ? -11.769 -2.233  -28.272 1.00 26.72  ? 242 HIS A CE1 1 
ATOM   1899 N NE2 . HIS A 1 243 ? -11.072 -1.957  -27.185 1.00 29.09  ? 242 HIS A NE2 1 
ATOM   1900 N N   . SER A 1 244 ? -13.010 -5.611  -23.986 1.00 27.60  ? 243 SER A N   1 
ATOM   1901 C CA  . SER A 1 244 ? -13.052 -4.890  -22.722 1.00 25.85  ? 243 SER A CA  1 
ATOM   1902 C C   . SER A 1 244 ? -11.682 -4.290  -22.457 1.00 25.64  ? 243 SER A C   1 
ATOM   1903 O O   . SER A 1 244 ? -10.667 -4.876  -22.831 1.00 26.99  ? 243 SER A O   1 
ATOM   1904 C CB  . SER A 1 244 ? -13.451 -5.809  -21.565 1.00 25.06  ? 243 SER A CB  1 
ATOM   1905 O OG  . SER A 1 244 ? -14.866 -5.893  -21.460 1.00 29.33  ? 243 SER A OG  1 
ATOM   1906 N N   . ALA A 1 245 ? -11.654 -3.116  -21.833 1.00 23.66  ? 244 ALA A N   1 
ATOM   1907 C CA  . ALA A 1 245 ? -10.403 -2.471  -21.472 1.00 24.90  ? 244 ALA A CA  1 
ATOM   1908 C C   . ALA A 1 245 ? -10.421 -2.100  -19.999 1.00 27.56  ? 244 ALA A C   1 
ATOM   1909 O O   . ALA A 1 245 ? -11.448 -1.651  -19.477 1.00 26.99  ? 244 ALA A O   1 
ATOM   1910 C CB  . ALA A 1 245 ? -10.144 -1.220  -22.305 1.00 25.04  ? 244 ALA A CB  1 
ATOM   1911 N N   . PHE A 1 246 ? -9.282  -2.288  -19.333 1.00 27.36  ? 245 PHE A N   1 
ATOM   1912 C CA  . PHE A 1 246 ? -9.142  -1.830  -17.953 1.00 29.13  ? 245 PHE A CA  1 
ATOM   1913 C C   . PHE A 1 246 ? -7.681  -1.497  -17.652 1.00 27.35  ? 245 PHE A C   1 
ATOM   1914 O O   . PHE A 1 246 ? -6.759  -2.072  -18.245 1.00 26.45  ? 245 PHE A O   1 
ATOM   1915 C CB  . PHE A 1 246 ? -9.665  -2.865  -16.946 1.00 23.42  ? 245 PHE A CB  1 
ATOM   1916 C CG  . PHE A 1 246 ? -9.026  -4.224  -17.069 1.00 24.89  ? 245 PHE A CG  1 
ATOM   1917 C CD1 . PHE A 1 246 ? -7.906  -4.553  -16.324 1.00 27.27  ? 245 PHE A CD1 1 
ATOM   1918 C CD2 . PHE A 1 246 ? -9.571  -5.189  -17.902 1.00 27.99  ? 245 PHE A CD2 1 
ATOM   1919 C CE1 . PHE A 1 246 ? -7.316  -5.810  -16.429 1.00 26.93  ? 245 PHE A CE1 1 
ATOM   1920 C CE2 . PHE A 1 246 ? -9.001  -6.447  -18.002 1.00 25.17  ? 245 PHE A CE2 1 
ATOM   1921 C CZ  . PHE A 1 246 ? -7.868  -6.757  -17.269 1.00 26.91  ? 245 PHE A CZ  1 
ATOM   1922 N N   . GLY A 1 247 ? -7.490  -0.566  -16.735 1.00 27.49  ? 246 GLY A N   1 
ATOM   1923 C CA  . GLY A 1 247 ? -6.167  -0.183  -16.278 1.00 24.92  ? 246 GLY A CA  1 
ATOM   1924 C C   . GLY A 1 247 ? -5.917  -0.801  -14.917 1.00 27.01  ? 246 GLY A C   1 
ATOM   1925 O O   . GLY A 1 247 ? -6.727  -0.657  -14.003 1.00 27.87  ? 246 GLY A O   1 
ATOM   1926 N N   . TYR A 1 248 ? -4.795  -1.496  -14.800 1.00 29.12  ? 247 TYR A N   1 
ATOM   1927 C CA  . TYR A 1 248 ? -4.421  -2.172  -13.569 1.00 28.32  ? 247 TYR A CA  1 
ATOM   1928 C C   . TYR A 1 248 ? -2.933  -1.982  -13.384 1.00 28.60  ? 247 TYR A C   1 
ATOM   1929 O O   . TYR A 1 248 ? -2.166  -2.222  -14.319 1.00 30.39  ? 247 TYR A O   1 
ATOM   1930 C CB  . TYR A 1 248 ? -4.767  -3.664  -13.622 1.00 28.44  ? 247 TYR A CB  1 
ATOM   1931 C CG  . TYR A 1 248 ? -4.250  -4.468  -12.457 1.00 30.49  ? 247 TYR A CG  1 
ATOM   1932 C CD1 . TYR A 1 248 ? -4.770  -4.297  -11.181 1.00 31.37  ? 247 TYR A CD1 1 
ATOM   1933 C CD2 . TYR A 1 248 ? -3.248  -5.406  -12.625 1.00 33.84  ? 247 TYR A CD2 1 
ATOM   1934 C CE1 . TYR A 1 248 ? -4.311  -5.034  -10.108 1.00 31.16  ? 247 TYR A CE1 1 
ATOM   1935 C CE2 . TYR A 1 248 ? -2.768  -6.150  -11.537 1.00 31.83  ? 247 TYR A CE2 1 
ATOM   1936 C CZ  . TYR A 1 248 ? -3.307  -5.959  -10.293 1.00 32.70  ? 247 TYR A CZ  1 
ATOM   1937 O OH  . TYR A 1 248 ? -2.843  -6.699  -9.230  1.00 35.73  ? 247 TYR A OH  1 
ATOM   1938 N N   . ASN A 1 249 ? -2.535  -1.532  -12.194 1.00 32.79  ? 248 ASN A N   1 
ATOM   1939 C CA  . ASN A 1 249 ? -1.132  -1.273  -11.868 1.00 31.70  ? 248 ASN A CA  1 
ATOM   1940 C C   . ASN A 1 249 ? -0.451  -0.444  -12.946 1.00 30.74  ? 248 ASN A C   1 
ATOM   1941 O O   . ASN A 1 249 ? 0.655   -0.750  -13.392 1.00 31.63  ? 248 ASN A O   1 
ATOM   1942 C CB  . ASN A 1 249 ? -0.375  -2.577  -11.626 1.00 36.53  ? 248 ASN A CB  1 
ATOM   1943 C CG  . ASN A 1 249 ? -0.656  -3.156  -10.253 1.00 44.68  ? 248 ASN A CG  1 
ATOM   1944 O OD1 . ASN A 1 249 ? -1.458  -2.608  -9.484  1.00 45.60  ? 248 ASN A OD1 1 
ATOM   1945 N ND2 . ASN A 1 249 ? -0.001  -4.266  -9.933  1.00 52.81  ? 248 ASN A ND2 1 
ATOM   1946 N N   . GLY A 1 250 ? -1.135  0.615   -13.373 1.00 28.22  ? 249 GLY A N   1 
ATOM   1947 C CA  . GLY A 1 250 ? -0.584  1.580   -14.303 1.00 25.79  ? 249 GLY A CA  1 
ATOM   1948 C C   . GLY A 1 250 ? -0.565  1.161   -15.760 1.00 30.27  ? 249 GLY A C   1 
ATOM   1949 O O   . GLY A 1 250 ? -0.064  1.925   -16.599 1.00 32.87  ? 249 GLY A O   1 
ATOM   1950 N N   . GLU A 1 251 ? -1.089  -0.010  -16.098 1.00 27.82  ? 250 GLU A N   1 
ATOM   1951 C CA  . GLU A 1 251 ? -1.007  -0.524  -17.453 1.00 28.45  ? 250 GLU A CA  1 
ATOM   1952 C C   . GLU A 1 251 ? -2.400  -0.800  -18.001 1.00 28.37  ? 250 GLU A C   1 
ATOM   1953 O O   . GLU A 1 251 ? -3.349  -1.050  -17.248 1.00 27.31  ? 250 GLU A O   1 
ATOM   1954 C CB  . GLU A 1 251 ? -0.159  -1.794  -17.512 1.00 27.45  ? 250 GLU A CB  1 
ATOM   1955 C CG  . GLU A 1 251 ? 1.250   -1.592  -16.992 1.00 27.69  ? 250 GLU A CG  1 
ATOM   1956 C CD  . GLU A 1 251 ? 2.107   -2.846  -17.132 1.00 32.02  ? 250 GLU A CD  1 
ATOM   1957 O OE1 . GLU A 1 251 ? 1.903   -3.801  -16.341 1.00 31.59  ? 250 GLU A OE1 1 
ATOM   1958 O OE2 . GLU A 1 251 ? 2.975   -2.880  -18.049 1.00 31.07  ? 250 GLU A OE2 1 
ATOM   1959 N N   . LEU A 1 252 ? -2.510  -0.734  -19.325 1.00 28.58  ? 251 LEU A N   1 
ATOM   1960 C CA  . LEU A 1 252 ? -3.761  -1.000  -20.010 1.00 26.64  ? 251 LEU A CA  1 
ATOM   1961 C C   . LEU A 1 252 ? -3.840  -2.476  -20.372 1.00 27.67  ? 251 LEU A C   1 
ATOM   1962 O O   . LEU A 1 252 ? -2.860  -3.069  -20.836 1.00 27.24  ? 251 LEU A O   1 
ATOM   1963 C CB  . LEU A 1 252 ? -3.882  -0.134  -21.264 1.00 28.97  ? 251 LEU A CB  1 
ATOM   1964 C CG  . LEU A 1 252 ? -5.071  -0.458  -22.185 1.00 30.84  ? 251 LEU A CG  1 
ATOM   1965 C CD1 . LEU A 1 252 ? -6.386  -0.216  -21.464 1.00 23.77  ? 251 LEU A CD1 1 
ATOM   1966 C CD2 . LEU A 1 252 ? -4.994  0.321   -23.516 1.00 24.09  ? 251 LEU A CD2 1 
ATOM   1967 N N   . TYR A 1 253 ? -5.003  -3.071  -20.130 1.00 26.48  ? 252 TYR A N   1 
ATOM   1968 C CA  . TYR A 1 253 ? -5.309  -4.425  -20.569 1.00 27.96  ? 252 TYR A CA  1 
ATOM   1969 C C   . TYR A 1 253 ? -6.548  -4.412  -21.458 1.00 29.54  ? 252 TYR A C   1 
ATOM   1970 O O   . TYR A 1 253 ? -7.527  -3.704  -21.179 1.00 28.02  ? 252 TYR A O   1 
ATOM   1971 C CB  . TYR A 1 253 ? -5.555  -5.368  -19.396 1.00 26.40  ? 252 TYR A CB  1 
ATOM   1972 C CG  . TYR A 1 253 ? -4.365  -5.586  -18.521 1.00 25.99  ? 252 TYR A CG  1 
ATOM   1973 C CD1 . TYR A 1 253 ? -3.968  -4.611  -17.610 1.00 27.22  ? 252 TYR A CD1 1 
ATOM   1974 C CD2 . TYR A 1 253 ? -3.642  -6.769  -18.582 1.00 25.96  ? 252 TYR A CD2 1 
ATOM   1975 C CE1 . TYR A 1 253 ? -2.879  -4.801  -16.802 1.00 28.34  ? 252 TYR A CE1 1 
ATOM   1976 C CE2 . TYR A 1 253 ? -2.554  -6.973  -17.777 1.00 24.88  ? 252 TYR A CE2 1 
ATOM   1977 C CZ  . TYR A 1 253 ? -2.179  -5.987  -16.885 1.00 27.17  ? 252 TYR A CZ  1 
ATOM   1978 O OH  . TYR A 1 253 ? -1.103  -6.167  -16.069 1.00 26.43  ? 252 TYR A OH  1 
ATOM   1979 N N   . ILE A 1 254 ? -6.511  -5.204  -22.521 1.00 25.69  ? 253 ILE A N   1 
ATOM   1980 C CA  . ILE A 1 254 ? -7.678  -5.382  -23.361 1.00 27.94  ? 253 ILE A CA  1 
ATOM   1981 C C   . ILE A 1 254 ? -7.936  -6.885  -23.501 1.00 31.37  ? 253 ILE A C   1 
ATOM   1982 O O   . ILE A 1 254 ? -6.994  -7.668  -23.696 1.00 30.98  ? 253 ILE A O   1 
ATOM   1983 C CB  . ILE A 1 254 ? -7.518  -4.674  -24.729 1.00 27.93  ? 253 ILE A CB  1 
ATOM   1984 C CG1 . ILE A 1 254 ? -6.426  -5.305  -25.550 1.00 29.87  ? 253 ILE A CG1 1 
ATOM   1985 C CG2 . ILE A 1 254 ? -7.176  -3.187  -24.569 1.00 25.23  ? 253 ILE A CG2 1 
ATOM   1986 C CD1 . ILE A 1 254 ? -6.889  -5.586  -26.940 1.00 34.58  ? 253 ILE A CD1 1 
ATOM   1987 N N   . PHE A 1 255 ? -9.208  -7.288  -23.327 1.00 27.98  ? 254 PHE A N   1 
ATOM   1988 C CA  . PHE A 1 255 ? -9.649  -8.673  -23.443 1.00 26.62  ? 254 PHE A CA  1 
ATOM   1989 C C   . PHE A 1 255 ? -10.665 -8.822  -24.564 1.00 28.18  ? 254 PHE A C   1 
ATOM   1990 O O   . PHE A 1 255 ? -11.591 -8.016  -24.677 1.00 27.41  ? 254 PHE A O   1 
ATOM   1991 C CB  . PHE A 1 255 ? -10.333 -9.211  -22.172 1.00 25.17  ? 254 PHE A CB  1 
ATOM   1992 C CG  . PHE A 1 255 ? -11.110 -10.486 -22.430 1.00 27.94  ? 254 PHE A CG  1 
ATOM   1993 C CD1 . PHE A 1 255 ? -10.469 -11.716 -22.400 1.00 27.50  ? 254 PHE A CD1 1 
ATOM   1994 C CD2 . PHE A 1 255 ? -12.460 -10.449 -22.795 1.00 26.41  ? 254 PHE A CD2 1 
ATOM   1995 C CE1 . PHE A 1 255 ? -11.163 -12.886 -22.687 1.00 29.59  ? 254 PHE A CE1 1 
ATOM   1996 C CE2 . PHE A 1 255 ? -13.149 -11.609 -23.085 1.00 25.91  ? 254 PHE A CE2 1 
ATOM   1997 C CZ  . PHE A 1 255 ? -12.505 -12.832 -23.024 1.00 27.99  ? 254 PHE A CZ  1 
ATOM   1998 N N   . GLY A 1 256 ? -10.536 -9.903  -25.337 1.00 28.94  ? 255 GLY A N   1 
ATOM   1999 C CA  . GLY A 1 256 ? -11.641 -10.350 -26.168 1.00 28.82  ? 255 GLY A CA  1 
ATOM   2000 C C   . GLY A 1 256 ? -11.989 -9.388  -27.290 1.00 30.77  ? 255 GLY A C   1 
ATOM   2001 O O   . GLY A 1 256 ? -11.154 -8.600  -27.760 1.00 30.36  ? 255 GLY A O   1 
ATOM   2002 N N   . GLY A 1 257 ? -13.245 -9.461  -27.730 1.00 27.19  ? 256 GLY A N   1 
ATOM   2003 C CA  . GLY A 1 257 ? -13.739 -8.629  -28.808 1.00 30.21  ? 256 GLY A CA  1 
ATOM   2004 C C   . GLY A 1 257 ? -13.978 -9.425  -30.083 1.00 32.48  ? 256 GLY A C   1 
ATOM   2005 O O   . GLY A 1 257 ? -13.895 -10.657 -30.114 1.00 30.66  ? 256 GLY A O   1 
ATOM   2006 N N   . TYR A 1 258 ? -14.276 -8.685  -31.155 1.00 30.05  ? 257 TYR A N   1 
ATOM   2007 C CA  . TYR A 1 258 ? -14.663 -9.269  -32.430 1.00 34.10  ? 257 TYR A CA  1 
ATOM   2008 C C   . TYR A 1 258 ? -14.115 -8.439  -33.585 1.00 34.69  ? 257 TYR A C   1 
ATOM   2009 O O   . TYR A 1 258 ? -14.143 -7.203  -33.547 1.00 31.89  ? 257 TYR A O   1 
ATOM   2010 C CB  . TYR A 1 258 ? -16.189 -9.370  -32.533 1.00 33.81  ? 257 TYR A CB  1 
ATOM   2011 C CG  . TYR A 1 258 ? -16.720 -9.820  -33.874 1.00 33.88  ? 257 TYR A CG  1 
ATOM   2012 C CD1 . TYR A 1 258 ? -16.623 -11.148 -34.278 1.00 35.95  ? 257 TYR A CD1 1 
ATOM   2013 C CD2 . TYR A 1 258 ? -17.359 -8.924  -34.722 1.00 37.18  ? 257 TYR A CD2 1 
ATOM   2014 C CE1 . TYR A 1 258 ? -17.137 -11.572 -35.513 1.00 40.39  ? 257 TYR A CE1 1 
ATOM   2015 C CE2 . TYR A 1 258 ? -17.873 -9.331  -35.957 1.00 38.32  ? 257 TYR A CE2 1 
ATOM   2016 C CZ  . TYR A 1 258 ? -17.756 -10.657 -36.348 1.00 41.19  ? 257 TYR A CZ  1 
ATOM   2017 O OH  . TYR A 1 258 ? -18.268 -11.060 -37.566 1.00 41.82  ? 257 TYR A OH  1 
ATOM   2018 N N   . ASN A 1 259 ? -13.644 -9.134  -34.619 1.00 32.76  ? 258 ASN A N   1 
ATOM   2019 C CA  . ASN A 1 259 ? -13.163 -8.517  -35.849 1.00 35.92  ? 258 ASN A CA  1 
ATOM   2020 C C   . ASN A 1 259 ? -14.009 -9.048  -37.002 1.00 38.35  ? 258 ASN A C   1 
ATOM   2021 O O   . ASN A 1 259 ? -13.986 -10.249 -37.297 1.00 37.57  ? 258 ASN A O   1 
ATOM   2022 C CB  . ASN A 1 259 ? -11.670 -8.816  -36.046 1.00 37.43  ? 258 ASN A CB  1 
ATOM   2023 C CG  . ASN A 1 259 ? -11.096 -8.197  -37.308 1.00 38.06  ? 258 ASN A CG  1 
ATOM   2024 O OD1 . ASN A 1 259 ? -11.611 -8.397  -38.410 1.00 41.67  ? 258 ASN A OD1 1 
ATOM   2025 N ND2 . ASN A 1 259 ? -10.010 -7.454  -37.154 1.00 37.28  ? 258 ASN A ND2 1 
ATOM   2026 N N   . ALA A 1 260 ? -14.764 -8.160  -37.644 1.00 37.35  ? 259 ALA A N   1 
ATOM   2027 C CA  . ALA A 1 260 ? -15.704 -8.603  -38.667 1.00 40.45  ? 259 ALA A CA  1 
ATOM   2028 C C   . ALA A 1 260 ? -15.003 -8.940  -39.973 1.00 42.64  ? 259 ALA A C   1 
ATOM   2029 O O   . ALA A 1 260 ? -15.482 -9.798  -40.723 1.00 42.28  ? 259 ALA A O   1 
ATOM   2030 C CB  . ALA A 1 260 ? -16.775 -7.537  -38.904 1.00 40.80  ? 259 ALA A CB  1 
ATOM   2031 N N   . ARG A 1 261 ? -13.876 -8.277  -40.259 1.00 41.52  ? 260 ARG A N   1 
ATOM   2032 C CA  . ARG A 1 261 ? -13.104 -8.613  -41.448 1.00 38.58  ? 260 ARG A CA  1 
ATOM   2033 C C   . ARG A 1 261 ? -12.651 -10.061 -41.397 1.00 39.91  ? 260 ARG A C   1 
ATOM   2034 O O   . ARG A 1 261 ? -12.725 -10.775 -42.396 1.00 43.62  ? 260 ARG A O   1 
ATOM   2035 C CB  . ARG A 1 261 ? -11.898 -7.674  -41.591 1.00 39.60  ? 260 ARG A CB  1 
ATOM   2036 C CG  . ARG A 1 261 ? -10.963 -8.012  -42.773 1.00 41.83  ? 260 ARG A CG  1 
ATOM   2037 C CD  . ARG A 1 261 ? -9.680  -7.177  -42.783 1.00 44.17  ? 260 ARG A CD  1 
ATOM   2038 N NE  . ARG A 1 261 ? -8.472  -7.982  -42.587 1.00 47.60  ? 260 ARG A NE  1 
ATOM   2039 C CZ  . ARG A 1 261 ? -7.762  -8.020  -41.465 1.00 51.26  ? 260 ARG A CZ  1 
ATOM   2040 N NH1 . ARG A 1 261 ? -8.103  -7.304  -40.402 1.00 50.22  ? 260 ARG A NH1 1 
ATOM   2041 N NH2 . ARG A 1 261 ? -6.683  -8.799  -41.404 1.00 52.26  ? 260 ARG A NH2 1 
ATOM   2042 N N   . LEU A 1 262 ? -12.189 -10.515 -40.237 1.00 41.54  ? 261 LEU A N   1 
ATOM   2043 C CA  . LEU A 1 262 ? -11.813 -11.906 -40.037 1.00 41.25  ? 261 LEU A CA  1 
ATOM   2044 C C   . LEU A 1 262 ? -12.987 -12.783 -39.618 1.00 41.41  ? 261 LEU A C   1 
ATOM   2045 O O   . LEU A 1 262 ? -12.834 -14.008 -39.556 1.00 40.45  ? 261 LEU A O   1 
ATOM   2046 C CB  . LEU A 1 262 ? -10.706 -11.989 -38.978 1.00 45.29  ? 261 LEU A CB  1 
ATOM   2047 C CG  . LEU A 1 262 ? -9.477  -11.115 -39.270 1.00 46.48  ? 261 LEU A CG  1 
ATOM   2048 C CD1 . LEU A 1 262 ? -8.514  -11.101 -38.064 1.00 44.86  ? 261 LEU A CD1 1 
ATOM   2049 C CD2 . LEU A 1 262 ? -8.771  -11.567 -40.553 1.00 37.56  ? 261 LEU A CD2 1 
ATOM   2050 N N   . ASN A 1 263 ? -14.150 -12.185 -39.363 1.00 43.09  ? 262 ASN A N   1 
ATOM   2051 C CA  . ASN A 1 263 ? -15.284 -12.852 -38.724 1.00 43.71  ? 262 ASN A CA  1 
ATOM   2052 C C   . ASN A 1 263 ? -14.811 -13.709 -37.557 1.00 38.26  ? 262 ASN A C   1 
ATOM   2053 O O   . ASN A 1 263 ? -15.109 -14.901 -37.458 1.00 41.17  ? 262 ASN A O   1 
ATOM   2054 C CB  . ASN A 1 263 ? -16.092 -13.679 -39.728 1.00 41.55  ? 262 ASN A CB  1 
ATOM   2055 C CG  . ASN A 1 263 ? -17.347 -14.272 -39.107 1.00 44.22  ? 262 ASN A CG  1 
ATOM   2056 O OD1 . ASN A 1 263 ? -17.827 -13.797 -38.074 1.00 44.25  ? 262 ASN A OD1 1 
ATOM   2057 N ND2 . ASN A 1 263 ? -17.869 -15.322 -39.718 1.00 46.73  ? 262 ASN A ND2 1 
ATOM   2058 N N   . ARG A 1 264 ? -14.040 -13.089 -36.672 1.00 34.38  ? 263 ARG A N   1 
ATOM   2059 C CA  . ARG A 1 264 ? -13.365 -13.815 -35.606 1.00 37.19  ? 263 ARG A CA  1 
ATOM   2060 C C   . ARG A 1 264 ? -13.690 -13.188 -34.259 1.00 36.81  ? 263 ARG A C   1 
ATOM   2061 O O   . ARG A 1 264 ? -13.557 -11.970 -34.088 1.00 35.77  ? 263 ARG A O   1 
ATOM   2062 C CB  . ARG A 1 264 ? -11.847 -13.825 -35.843 1.00 42.27  ? 263 ARG A CB  1 
ATOM   2063 C CG  . ARG A 1 264 ? -11.032 -14.573 -34.795 1.00 44.35  ? 263 ARG A CG  1 
ATOM   2064 C CD  . ARG A 1 264 ? -9.531  -14.475 -35.070 1.00 47.16  ? 263 ARG A CD  1 
ATOM   2065 N NE  . ARG A 1 264 ? -9.186  -14.885 -36.430 1.00 60.82  ? 263 ARG A NE  1 
ATOM   2066 C CZ  . ARG A 1 264 ? -8.003  -14.674 -36.999 1.00 62.19  ? 263 ARG A CZ  1 
ATOM   2067 N NH1 . ARG A 1 264 ? -7.012  -14.087 -36.337 1.00 56.44  ? 263 ARG A NH1 1 
ATOM   2068 N NH2 . ARG A 1 264 ? -7.814  -15.047 -38.267 1.00 55.34  ? 263 ARG A NH2 1 
ATOM   2069 N N   . HIS A 1 265 ? -14.112 -14.021 -33.307 1.00 39.62  ? 264 HIS A N   1 
ATOM   2070 C CA  . HIS A 1 265 ? -14.220 -13.611 -31.912 1.00 34.25  ? 264 HIS A CA  1 
ATOM   2071 C C   . HIS A 1 265 ? -12.910 -13.914 -31.202 1.00 33.24  ? 264 HIS A C   1 
ATOM   2072 O O   . HIS A 1 265 ? -12.154 -14.801 -31.605 1.00 35.46  ? 264 HIS A O   1 
ATOM   2073 C CB  . HIS A 1 265 ? -15.386 -14.314 -31.206 1.00 32.49  ? 264 HIS A CB  1 
ATOM   2074 C CG  . HIS A 1 265 ? -16.729 -13.830 -31.647 1.00 35.64  ? 264 HIS A CG  1 
ATOM   2075 N ND1 . HIS A 1 265 ? -17.328 -14.261 -32.814 1.00 37.20  ? 264 HIS A ND1 1 
ATOM   2076 C CD2 . HIS A 1 265 ? -17.572 -12.918 -31.104 1.00 34.62  ? 264 HIS A CD2 1 
ATOM   2077 C CE1 . HIS A 1 265 ? -18.487 -13.646 -32.961 1.00 36.82  ? 264 HIS A CE1 1 
ATOM   2078 N NE2 . HIS A 1 265 ? -18.661 -12.829 -31.935 1.00 36.59  ? 264 HIS A NE2 1 
ATOM   2079 N N   . PHE A 1 266 ? -12.646 -13.164 -30.136 1.00 31.24  ? 265 PHE A N   1 
ATOM   2080 C CA  . PHE A 1 266 ? -11.373 -13.211 -29.435 1.00 31.45  ? 265 PHE A CA  1 
ATOM   2081 C C   . PHE A 1 266 ? -11.584 -13.525 -27.961 1.00 35.38  ? 265 PHE A C   1 
ATOM   2082 O O   . PHE A 1 266 ? -12.588 -13.129 -27.359 1.00 33.25  ? 265 PHE A O   1 
ATOM   2083 C CB  . PHE A 1 266 ? -10.609 -11.884 -29.550 1.00 29.54  ? 265 PHE A CB  1 
ATOM   2084 C CG  . PHE A 1 266 ? -10.106 -11.584 -30.941 1.00 33.32  ? 265 PHE A CG  1 
ATOM   2085 C CD1 . PHE A 1 266 ? -8.961  -12.184 -31.423 1.00 34.56  ? 265 PHE A CD1 1 
ATOM   2086 C CD2 . PHE A 1 266 ? -10.774 -10.685 -31.760 1.00 33.88  ? 265 PHE A CD2 1 
ATOM   2087 C CE1 . PHE A 1 266 ? -8.487  -11.903 -32.705 1.00 38.77  ? 265 PHE A CE1 1 
ATOM   2088 C CE2 . PHE A 1 266 ? -10.308 -10.397 -33.037 1.00 36.19  ? 265 PHE A CE2 1 
ATOM   2089 C CZ  . PHE A 1 266 ? -9.160  -11.016 -33.512 1.00 36.24  ? 265 PHE A CZ  1 
ATOM   2090 N N   . HIS A 1 267 ? -10.616 -14.248 -27.382 1.00 33.85  ? 266 HIS A N   1 
ATOM   2091 C CA  . HIS A 1 267 ? -10.520 -14.360 -25.931 1.00 30.84  ? 266 HIS A CA  1 
ATOM   2092 C C   . HIS A 1 267 ? -9.072  -14.183 -25.461 1.00 33.27  ? 266 HIS A C   1 
ATOM   2093 O O   . HIS A 1 267 ? -8.684  -14.719 -24.410 1.00 31.30  ? 266 HIS A O   1 
ATOM   2094 C CB  . HIS A 1 267 ? -11.111 -15.681 -25.429 1.00 30.05  ? 266 HIS A CB  1 
ATOM   2095 C CG  . HIS A 1 267 ? -10.379 -16.904 -25.888 1.00 32.26  ? 266 HIS A CG  1 
ATOM   2096 N ND1 . HIS A 1 267 ? -10.685 -18.163 -25.417 1.00 33.49  ? 266 HIS A ND1 1 
ATOM   2097 C CD2 . HIS A 1 267 ? -9.355  -17.067 -26.761 1.00 30.70  ? 266 HIS A CD2 1 
ATOM   2098 C CE1 . HIS A 1 267 ? -9.879  -19.049 -25.979 1.00 34.33  ? 266 HIS A CE1 1 
ATOM   2099 N NE2 . HIS A 1 267 ? -9.060  -18.409 -26.794 1.00 31.40  ? 266 HIS A NE2 1 
ATOM   2100 N N   . ASP A 1 268 ? -8.274  -13.415 -26.214 1.00 28.83  ? 267 ASP A N   1 
ATOM   2101 C CA  . ASP A 1 268 ? -6.910  -13.107 -25.819 1.00 32.47  ? 267 ASP A CA  1 
ATOM   2102 C C   . ASP A 1 268 ? -6.876  -11.950 -24.820 1.00 33.44  ? 267 ASP A C   1 
ATOM   2103 O O   . ASP A 1 268 ? -7.899  -11.319 -24.515 1.00 29.69  ? 267 ASP A O   1 
ATOM   2104 C CB  . ASP A 1 268 ? -6.027  -12.797 -27.038 1.00 33.66  ? 267 ASP A CB  1 
ATOM   2105 C CG  . ASP A 1 268 ? -6.618  -11.735 -27.966 1.00 35.03  ? 267 ASP A CG  1 
ATOM   2106 O OD1 . ASP A 1 268 ? -7.740  -11.248 -27.704 1.00 32.15  ? 267 ASP A OD1 1 
ATOM   2107 O OD2 . ASP A 1 268 ? -5.938  -11.394 -28.969 1.00 35.93  ? 267 ASP A OD2 1 
ATOM   2108 N N   . LEU A 1 269 ? -5.663  -11.701 -24.304 1.00 34.36  ? 268 LEU A N   1 
ATOM   2109 C CA  . LEU A 1 269 ? -5.387  -10.701 -23.274 1.00 31.67  ? 268 LEU A CA  1 
ATOM   2110 C C   . LEU A 1 269 ? -4.093  -9.992  -23.626 1.00 31.69  ? 268 LEU A C   1 
ATOM   2111 O O   . LEU A 1 269 ? -3.040  -10.626 -23.711 1.00 31.90  ? 268 LEU A O   1 
ATOM   2112 C CB  . LEU A 1 269 ? -5.270  -11.330 -21.883 1.00 30.54  ? 268 LEU A CB  1 
ATOM   2113 C CG  . LEU A 1 269 ? -5.206  -10.300 -20.753 1.00 28.55  ? 268 LEU A CG  1 
ATOM   2114 C CD1 . LEU A 1 269 ? -6.460  -9.435  -20.788 1.00 27.71  ? 268 LEU A CD1 1 
ATOM   2115 C CD2 . LEU A 1 269 ? -5.050  -10.959 -19.390 1.00 27.13  ? 268 LEU A CD2 1 
ATOM   2116 N N   . TRP A 1 270 ? -4.164  -8.684  -23.818 1.00 31.81  ? 269 TRP A N   1 
ATOM   2117 C CA  . TRP A 1 270 ? -3.009  -7.900  -24.215 1.00 31.47  ? 269 TRP A CA  1 
ATOM   2118 C C   . TRP A 1 270 ? -2.747  -6.833  -23.168 1.00 31.80  ? 269 TRP A C   1 
ATOM   2119 O O   . TRP A 1 270 ? -3.682  -6.261  -22.600 1.00 32.11  ? 269 TRP A O   1 
ATOM   2120 C CB  . TRP A 1 270 ? -3.217  -7.261  -25.587 1.00 31.54  ? 269 TRP A CB  1 
ATOM   2121 C CG  . TRP A 1 270 ? -3.119  -8.249  -26.724 1.00 33.17  ? 269 TRP A CG  1 
ATOM   2122 C CD1 . TRP A 1 270 ? -4.081  -9.132  -27.132 1.00 30.30  ? 269 TRP A CD1 1 
ATOM   2123 C CD2 . TRP A 1 270 ? -1.997  -8.441  -27.600 1.00 34.51  ? 269 TRP A CD2 1 
ATOM   2124 N NE1 . TRP A 1 270 ? -3.626  -9.864  -28.200 1.00 36.38  ? 269 TRP A NE1 1 
ATOM   2125 C CE2 . TRP A 1 270 ? -2.349  -9.462  -28.508 1.00 34.99  ? 269 TRP A CE2 1 
ATOM   2126 C CE3 . TRP A 1 270 ? -0.724  -7.851  -27.700 1.00 34.96  ? 269 TRP A CE3 1 
ATOM   2127 C CZ2 . TRP A 1 270 ? -1.481  -9.908  -29.505 1.00 29.61  ? 269 TRP A CZ2 1 
ATOM   2128 C CZ3 . TRP A 1 270 ? 0.140   -8.289  -28.706 1.00 33.98  ? 269 TRP A CZ3 1 
ATOM   2129 C CH2 . TRP A 1 270 ? -0.249  -9.310  -29.589 1.00 32.62  ? 269 TRP A CH2 1 
ATOM   2130 N N   . LYS A 1 271 ? -1.475  -6.593  -22.895 1.00 30.38  ? 270 LYS A N   1 
ATOM   2131 C CA  . LYS A 1 271 ? -1.064  -5.552  -21.970 1.00 31.67  ? 270 LYS A CA  1 
ATOM   2132 C C   . LYS A 1 271 ? -0.324  -4.478  -22.757 1.00 32.28  ? 270 LYS A C   1 
ATOM   2133 O O   . LYS A 1 271 ? 0.535   -4.790  -23.588 1.00 31.91  ? 270 LYS A O   1 
ATOM   2134 C CB  . LYS A 1 271 ? -0.181  -6.130  -20.856 1.00 30.89  ? 270 LYS A CB  1 
ATOM   2135 C CG  . LYS A 1 271 ? 0.179   -5.145  -19.753 1.00 27.53  ? 270 LYS A CG  1 
ATOM   2136 C CD  . LYS A 1 271 ? 0.918   -5.830  -18.623 1.00 29.69  ? 270 LYS A CD  1 
ATOM   2137 C CE  . LYS A 1 271 ? 2.244   -6.420  -19.086 1.00 29.89  ? 270 LYS A CE  1 
ATOM   2138 N NZ  . LYS A 1 271 ? 3.262   -5.354  -19.311 1.00 31.68  ? 270 LYS A NZ  1 
ATOM   2139 N N   . PHE A 1 272 ? -0.684  -3.226  -22.525 1.00 30.47  ? 271 PHE A N   1 
ATOM   2140 C CA  . PHE A 1 272 ? 0.035   -2.094  -23.083 1.00 30.36  ? 271 PHE A CA  1 
ATOM   2141 C C   . PHE A 1 272 ? 0.702   -1.342  -21.942 1.00 29.68  ? 271 PHE A C   1 
ATOM   2142 O O   . PHE A 1 272 ? 0.045   -1.016  -20.950 1.00 28.49  ? 271 PHE A O   1 
ATOM   2143 C CB  . PHE A 1 272 ? -0.907  -1.171  -23.854 1.00 30.93  ? 271 PHE A CB  1 
ATOM   2144 C CG  . PHE A 1 272 ? -0.218  0.018   -24.468 1.00 31.31  ? 271 PHE A CG  1 
ATOM   2145 C CD1 . PHE A 1 272 ? 0.576   -0.137  -25.602 1.00 28.70  ? 271 PHE A CD1 1 
ATOM   2146 C CD2 . PHE A 1 272 ? -0.373  1.284   -23.921 1.00 25.94  ? 271 PHE A CD2 1 
ATOM   2147 C CE1 . PHE A 1 272 ? 1.201   0.946   -26.180 1.00 30.00  ? 271 PHE A CE1 1 
ATOM   2148 C CE2 . PHE A 1 272 ? 0.245   2.373   -24.491 1.00 30.87  ? 271 PHE A CE2 1 
ATOM   2149 C CZ  . PHE A 1 272 ? 1.043   2.207   -25.626 1.00 33.11  ? 271 PHE A CZ  1 
ATOM   2150 N N   . ASN A 1 273 ? 2.012   -1.093  -22.067 1.00 34.02  ? 272 ASN A N   1 
ATOM   2151 C CA  . ASN A 1 273 ? 2.714   -0.317  -21.056 1.00 32.31  ? 272 ASN A CA  1 
ATOM   2152 C C   . ASN A 1 273 ? 2.934   1.081   -21.598 1.00 32.65  ? 272 ASN A C   1 
ATOM   2153 O O   . ASN A 1 273 ? 3.755   1.254   -22.509 1.00 35.43  ? 272 ASN A O   1 
ATOM   2154 C CB  . ASN A 1 273 ? 4.050   -0.954  -20.682 1.00 32.75  ? 272 ASN A CB  1 
ATOM   2155 C CG  . ASN A 1 273 ? 4.836   -0.096  -19.679 1.00 34.33  ? 272 ASN A CG  1 
ATOM   2156 O OD1 . ASN A 1 273 ? 5.427   0.916   -20.039 1.00 36.02  ? 272 ASN A OD1 1 
ATOM   2157 N ND2 . ASN A 1 273 ? 4.809   -0.486  -18.416 1.00 32.19  ? 272 ASN A ND2 1 
ATOM   2158 N N   . PRO A 1 274 ? 2.260   2.102   -21.070 1.00 32.52  ? 273 PRO A N   1 
ATOM   2159 C CA  . PRO A 1 274 ? 2.407   3.446   -21.643 1.00 34.16  ? 273 PRO A CA  1 
ATOM   2160 C C   . PRO A 1 274 ? 3.823   3.977   -21.572 1.00 38.55  ? 273 PRO A C   1 
ATOM   2161 O O   . PRO A 1 274 ? 4.187   4.832   -22.384 1.00 40.89  ? 273 PRO A O   1 
ATOM   2162 C CB  . PRO A 1 274 ? 1.449   4.295   -20.797 1.00 35.39  ? 273 PRO A CB  1 
ATOM   2163 C CG  . PRO A 1 274 ? 1.336   3.565   -19.512 1.00 34.71  ? 273 PRO A CG  1 
ATOM   2164 C CD  . PRO A 1 274 ? 1.404   2.106   -19.873 1.00 33.85  ? 273 PRO A CD  1 
ATOM   2165 N N   . VAL A 1 275 ? 4.640   3.485   -20.643 1.00 37.05  ? 274 VAL A N   1 
ATOM   2166 C CA  . VAL A 1 275 ? 5.957   4.071   -20.427 1.00 40.08  ? 274 VAL A CA  1 
ATOM   2167 C C   . VAL A 1 275 ? 6.939   3.599   -21.491 1.00 36.97  ? 274 VAL A C   1 
ATOM   2168 O O   . VAL A 1 275 ? 7.531   4.411   -22.207 1.00 38.10  ? 274 VAL A O   1 
ATOM   2169 C CB  . VAL A 1 275 ? 6.450   3.768   -19.002 1.00 41.04  ? 274 VAL A CB  1 
ATOM   2170 C CG1 . VAL A 1 275 ? 7.899   4.210   -18.837 1.00 39.82  ? 274 VAL A CG1 1 
ATOM   2171 C CG2 . VAL A 1 275 ? 5.548   4.490   -18.013 1.00 39.01  ? 274 VAL A CG2 1 
ATOM   2172 N N   . SER A 1 276 ? 7.104   2.284   -21.629 1.00 35.33  ? 275 SER A N   1 
ATOM   2173 C CA  . SER A 1 276 ? 7.844   1.734   -22.760 1.00 34.70  ? 275 SER A CA  1 
ATOM   2174 C C   . SER A 1 276 ? 7.099   1.924   -24.073 1.00 38.23  ? 275 SER A C   1 
ATOM   2175 O O   . SER A 1 276 ? 7.716   1.815   -25.142 1.00 37.14  ? 275 SER A O   1 
ATOM   2176 C CB  . SER A 1 276 ? 8.093   0.247   -22.545 1.00 35.11  ? 275 SER A CB  1 
ATOM   2177 O OG  . SER A 1 276 ? 6.861   -0.463  -22.604 1.00 36.97  ? 275 SER A OG  1 
ATOM   2178 N N   . PHE A 1 277 ? 5.796   2.208   -23.999 1.00 36.65  ? 276 PHE A N   1 
ATOM   2179 C CA  . PHE A 1 277 ? 4.877   2.287   -25.135 1.00 36.08  ? 276 PHE A CA  1 
ATOM   2180 C C   . PHE A 1 277 ? 4.920   1.007   -25.964 1.00 38.15  ? 276 PHE A C   1 
ATOM   2181 O O   . PHE A 1 277 ? 5.171   1.033   -27.168 1.00 36.03  ? 276 PHE A O   1 
ATOM   2182 C CB  . PHE A 1 277 ? 5.144   3.509   -26.016 1.00 36.45  ? 276 PHE A CB  1 
ATOM   2183 C CG  . PHE A 1 277 ? 3.884   4.126   -26.566 1.00 37.68  ? 276 PHE A CG  1 
ATOM   2184 C CD1 . PHE A 1 277 ? 3.196   5.090   -25.840 1.00 36.89  ? 276 PHE A CD1 1 
ATOM   2185 C CD2 . PHE A 1 277 ? 3.354   3.702   -27.778 1.00 38.91  ? 276 PHE A CD2 1 
ATOM   2186 C CE1 . PHE A 1 277 ? 2.020   5.647   -26.328 1.00 37.04  ? 276 PHE A CE1 1 
ATOM   2187 C CE2 . PHE A 1 277 ? 2.163   4.248   -28.267 1.00 33.00  ? 276 PHE A CE2 1 
ATOM   2188 C CZ  . PHE A 1 277 ? 1.498   5.208   -27.540 1.00 33.34  ? 276 PHE A CZ  1 
ATOM   2189 N N   . THR A 1 278 ? 4.646   -0.123  -25.299 1.00 32.63  ? 277 THR A N   1 
ATOM   2190 C CA  . THR A 1 278 ? 4.764   -1.422  -25.941 1.00 35.44  ? 277 THR A CA  1 
ATOM   2191 C C   . THR A 1 278 ? 3.616   -2.336  -25.540 1.00 34.14  ? 277 THR A C   1 
ATOM   2192 O O   . THR A 1 278 ? 3.045   -2.212  -24.453 1.00 32.99  ? 277 THR A O   1 
ATOM   2193 C CB  . THR A 1 278 ? 6.107   -2.113  -25.611 1.00 36.16  ? 277 THR A CB  1 
ATOM   2194 O OG1 . THR A 1 278 ? 6.287   -2.175  -24.190 1.00 34.77  ? 277 THR A OG1 1 
ATOM   2195 C CG2 . THR A 1 278 ? 7.273   -1.361  -26.239 1.00 34.74  ? 277 THR A CG2 1 
ATOM   2196 N N   . TRP A 1 279 ? 3.314   -3.279  -26.431 1.00 34.15  ? 278 TRP A N   1 
ATOM   2197 C CA  . TRP A 1 279 ? 2.269   -4.283  -26.274 1.00 33.66  ? 278 TRP A CA  1 
ATOM   2198 C C   . TRP A 1 279 ? 2.887   -5.642  -25.963 1.00 35.65  ? 278 TRP A C   1 
ATOM   2199 O O   . TRP A 1 279 ? 4.007   -5.945  -26.392 1.00 37.11  ? 278 TRP A O   1 
ATOM   2200 C CB  . TRP A 1 279 ? 1.427   -4.424  -27.550 1.00 32.80  ? 278 TRP A CB  1 
ATOM   2201 C CG  . TRP A 1 279 ? 0.373   -3.381  -27.783 1.00 32.88  ? 278 TRP A CG  1 
ATOM   2202 C CD1 . TRP A 1 279 ? 0.428   -2.343  -28.668 1.00 32.52  ? 278 TRP A CD1 1 
ATOM   2203 C CD2 . TRP A 1 279 ? -0.915  -3.309  -27.160 1.00 30.42  ? 278 TRP A CD2 1 
ATOM   2204 N NE1 . TRP A 1 279 ? -0.738  -1.621  -28.620 1.00 29.22  ? 278 TRP A NE1 1 
ATOM   2205 C CE2 . TRP A 1 279 ? -1.577  -2.193  -27.699 1.00 28.11  ? 278 TRP A CE2 1 
ATOM   2206 C CE3 . TRP A 1 279 ? -1.568  -4.077  -26.188 1.00 31.76  ? 278 TRP A CE3 1 
ATOM   2207 C CZ2 . TRP A 1 279 ? -2.865  -1.823  -27.298 1.00 30.11  ? 278 TRP A CZ2 1 
ATOM   2208 C CZ3 . TRP A 1 279 ? -2.848  -3.708  -25.795 1.00 30.32  ? 278 TRP A CZ3 1 
ATOM   2209 C CH2 . TRP A 1 279 ? -3.482  -2.595  -26.354 1.00 28.77  ? 278 TRP A CH2 1 
ATOM   2210 N N   . LYS A 1 280 ? 2.126   -6.478  -25.248 1.00 34.38  ? 279 LYS A N   1 
ATOM   2211 C CA  . LYS A 1 280 ? 2.563   -7.824  -24.898 1.00 32.42  ? 279 LYS A CA  1 
ATOM   2212 C C   . LYS A 1 280 ? 1.334   -8.701  -24.676 1.00 36.12  ? 279 LYS A C   1 
ATOM   2213 O O   . LYS A 1 280 ? 0.439   -8.352  -23.898 1.00 34.11  ? 279 LYS A O   1 
ATOM   2214 C CB  . LYS A 1 280 ? 3.458   -7.788  -23.654 1.00 35.53  ? 279 LYS A CB  1 
ATOM   2215 C CG  . LYS A 1 280 ? 4.225   -9.059  -23.333 1.00 37.58  ? 279 LYS A CG  1 
ATOM   2216 C CD  . LYS A 1 280 ? 4.843   -8.941  -21.922 1.00 42.02  ? 279 LYS A CD  1 
ATOM   2217 C CE  . LYS A 1 280 ? 5.874   -10.046 -21.607 1.00 53.16  ? 279 LYS A CE  1 
ATOM   2218 N NZ  . LYS A 1 280 ? 5.321   -11.439 -21.556 1.00 55.46  ? 279 LYS A NZ  1 
ATOM   2219 N N   . LYS A 1 281 ? 1.278   -9.821  -25.393 1.00 37.67  ? 280 LYS A N   1 
ATOM   2220 C CA  . LYS A 1 281 ? 0.215   -10.800 -25.213 1.00 32.97  ? 280 LYS A CA  1 
ATOM   2221 C C   . LYS A 1 281 ? 0.480   -11.588 -23.931 1.00 36.82  ? 280 LYS A C   1 
ATOM   2222 O O   . LYS A 1 281 ? 1.605   -12.048 -23.702 1.00 39.33  ? 280 LYS A O   1 
ATOM   2223 C CB  . LYS A 1 281 ? 0.138   -11.728 -26.427 1.00 31.46  ? 280 LYS A CB  1 
ATOM   2224 C CG  . LYS A 1 281 ? -1.160  -12.532 -26.537 1.00 35.09  ? 280 LYS A CG  1 
ATOM   2225 C CD  . LYS A 1 281 ? -1.090  -13.523 -27.691 1.00 38.17  ? 280 LYS A CD  1 
ATOM   2226 C CE  . LYS A 1 281 ? -2.413  -14.256 -27.935 1.00 42.13  ? 280 LYS A CE  1 
ATOM   2227 N NZ  . LYS A 1 281 ? -2.732  -15.235 -26.837 1.00 46.18  ? 280 LYS A NZ  1 
ATOM   2228 N N   . ILE A 1 282 ? -0.551  -11.714 -23.087 1.00 36.79  ? 281 ILE A N   1 
ATOM   2229 C CA  . ILE A 1 282 ? -0.459  -12.332 -21.766 1.00 34.40  ? 281 ILE A CA  1 
ATOM   2230 C C   . ILE A 1 282 ? -1.229  -13.644 -21.810 1.00 38.39  ? 281 ILE A C   1 
ATOM   2231 O O   . ILE A 1 282 ? -2.313  -13.714 -22.398 1.00 40.27  ? 281 ILE A O   1 
ATOM   2232 C CB  . ILE A 1 282 ? -1.022  -11.406 -20.665 1.00 34.22  ? 281 ILE A CB  1 
ATOM   2233 C CG1 . ILE A 1 282 ? -0.215  -10.117 -20.562 1.00 36.67  ? 281 ILE A CG1 1 
ATOM   2234 C CG2 . ILE A 1 282 ? -1.034  -12.089 -19.324 1.00 34.99  ? 281 ILE A CG2 1 
ATOM   2235 C CD1 . ILE A 1 282 ? 1.263   -10.339 -20.445 1.00 40.41  ? 281 ILE A CD1 1 
ATOM   2236 N N   . GLU A 1 283 ? -0.671  -14.689 -21.199 1.00 37.41  ? 282 GLU A N   1 
ATOM   2237 C CA  . GLU A 1 283 ? -1.310  -16.006 -21.161 1.00 38.95  ? 282 GLU A CA  1 
ATOM   2238 C C   . GLU A 1 283 ? -1.638  -16.357 -19.719 1.00 36.04  ? 282 GLU A C   1 
ATOM   2239 O O   . GLU A 1 283 ? -0.780  -16.881 -18.988 1.00 38.98  ? 282 GLU A O   1 
ATOM   2240 C CB  . GLU A 1 283 ? -0.411  -17.073 -21.779 1.00 44.09  ? 282 GLU A CB  1 
ATOM   2241 C CG  . GLU A 1 283 ? -0.066  -16.829 -23.225 1.00 50.04  ? 282 GLU A CG  1 
ATOM   2242 C CD  . GLU A 1 283 ? -1.202  -17.202 -24.158 1.00 56.05  ? 282 GLU A CD  1 
ATOM   2243 O OE1 . GLU A 1 283 ? -2.229  -17.736 -23.663 1.00 56.73  ? 282 GLU A OE1 1 
ATOM   2244 O OE2 . GLU A 1 283 ? -1.058  -16.962 -25.381 1.00 53.28  ? 282 GLU A OE2 1 
ATOM   2245 N N   . PRO A 1 284 ? -2.857  -16.086 -19.263 1.00 36.65  ? 283 PRO A N   1 
ATOM   2246 C CA  . PRO A 1 284 ? -3.239  -16.502 -17.909 1.00 35.94  ? 283 PRO A CA  1 
ATOM   2247 C C   . PRO A 1 284 ? -3.319  -18.016 -17.797 1.00 32.49  ? 283 PRO A C   1 
ATOM   2248 O O   . PRO A 1 284 ? -3.560  -18.725 -18.777 1.00 33.21  ? 283 PRO A O   1 
ATOM   2249 C CB  . PRO A 1 284 ? -4.614  -15.843 -17.688 1.00 30.35  ? 283 PRO A CB  1 
ATOM   2250 C CG  . PRO A 1 284 ? -5.061  -15.344 -19.007 1.00 33.63  ? 283 PRO A CG  1 
ATOM   2251 C CD  . PRO A 1 284 ? -3.873  -15.235 -19.914 1.00 36.86  ? 283 PRO A CD  1 
ATOM   2252 N N   . LYS A 1 285 ? -3.095  -18.505 -16.581 1.00 32.36  ? 284 LYS A N   1 
ATOM   2253 C CA  . LYS A 1 285 ? -3.339  -19.905 -16.281 1.00 32.51  ? 284 LYS A CA  1 
ATOM   2254 C C   . LYS A 1 285 ? -4.836  -20.172 -16.203 1.00 33.20  ? 284 LYS A C   1 
ATOM   2255 O O   . LYS A 1 285 ? -5.649  -19.273 -15.951 1.00 31.89  ? 284 LYS A O   1 
ATOM   2256 C CB  . LYS A 1 285 ? -2.693  -20.318 -14.953 1.00 32.92  ? 284 LYS A CB  1 
ATOM   2257 C CG  . LYS A 1 285 ? -1.234  -19.953 -14.785 1.00 33.82  ? 284 LYS A CG  1 
ATOM   2258 C CD  . LYS A 1 285 ? -0.358  -20.662 -15.775 1.00 39.52  ? 284 LYS A CD  1 
ATOM   2259 C CE  . LYS A 1 285 ? 1.104   -20.273 -15.558 1.00 44.85  ? 284 LYS A CE  1 
ATOM   2260 N NZ  . LYS A 1 285 ? 1.941   -20.579 -16.742 1.00 48.94  ? 284 LYS A NZ  1 
ATOM   2261 N N   . GLY A 1 286 ? -5.196  -21.436 -16.403 1.00 33.86  ? 285 GLY A N   1 
ATOM   2262 C CA  . GLY A 1 286 ? -6.577  -21.853 -16.331 1.00 31.33  ? 285 GLY A CA  1 
ATOM   2263 C C   . GLY A 1 286 ? -7.301  -21.674 -17.650 1.00 35.10  ? 285 GLY A C   1 
ATOM   2264 O O   . GLY A 1 286 ? -6.842  -21.001 -18.574 1.00 36.62  ? 285 GLY A O   1 
ATOM   2265 N N   . LYS A 1 287 ? -8.467  -22.300 -17.730 1.00 40.70  ? 286 LYS A N   1 
ATOM   2266 C CA  . LYS A 1 287 ? -9.329  -22.185 -18.899 1.00 39.12  ? 286 LYS A CA  1 
ATOM   2267 C C   . LYS A 1 287 ? -10.139 -20.899 -18.785 1.00 40.37  ? 286 LYS A C   1 
ATOM   2268 O O   . LYS A 1 287 ? -10.903 -20.712 -17.826 1.00 42.02  ? 286 LYS A O   1 
ATOM   2269 C CB  . LYS A 1 287 ? -10.234 -23.410 -18.988 1.00 40.47  ? 286 LYS A CB  1 
ATOM   2270 C CG  . LYS A 1 287 ? -11.230 -23.396 -20.114 1.00 45.41  ? 286 LYS A CG  1 
ATOM   2271 C CD  . LYS A 1 287 ? -12.051 -24.679 -20.114 1.00 56.48  ? 286 LYS A CD  1 
ATOM   2272 C CE  . LYS A 1 287 ? -12.936 -24.731 -21.339 1.00 64.88  ? 286 LYS A CE  1 
ATOM   2273 N NZ  . LYS A 1 287 ? -12.232 -24.060 -22.473 1.00 68.48  ? 286 LYS A NZ  1 
ATOM   2274 N N   . GLY A 1 288 ? -9.964  -19.995 -19.734 1.00 36.63  ? 287 GLY A N   1 
ATOM   2275 C CA  . GLY A 1 288 ? -10.664 -18.734 -19.643 1.00 34.92  ? 287 GLY A CA  1 
ATOM   2276 C C   . GLY A 1 288 ? -12.076 -18.810 -20.188 1.00 33.62  ? 287 GLY A C   1 
ATOM   2277 O O   . GLY A 1 288 ? -12.629 -19.894 -20.422 1.00 31.95  ? 287 GLY A O   1 
ATOM   2278 N N   . PRO A 1 289 ? -12.695 -17.647 -20.388 1.00 33.07  ? 288 PRO A N   1 
ATOM   2279 C CA  . PRO A 1 289 ? -13.935 -17.601 -21.162 1.00 29.34  ? 288 PRO A CA  1 
ATOM   2280 C C   . PRO A 1 289 ? -13.690 -17.930 -22.626 1.00 30.52  ? 288 PRO A C   1 
ATOM   2281 O O   . PRO A 1 289 ? -12.621 -17.672 -23.180 1.00 31.51  ? 288 PRO A O   1 
ATOM   2282 C CB  . PRO A 1 289 ? -14.404 -16.156 -20.989 1.00 27.47  ? 288 PRO A CB  1 
ATOM   2283 C CG  . PRO A 1 289 ? -13.180 -15.413 -20.659 1.00 30.13  ? 288 PRO A CG  1 
ATOM   2284 C CD  . PRO A 1 289 ? -12.316 -16.322 -19.873 1.00 28.82  ? 288 PRO A CD  1 
ATOM   2285 N N   . CYS A 1 290 ? -14.714 -18.497 -23.254 1.00 30.18  ? 289 CYS A N   1 
ATOM   2286 C CA  . CYS A 1 290 ? -14.706 -18.713 -24.686 1.00 30.64  ? 289 CYS A CA  1 
ATOM   2287 C C   . CYS A 1 290 ? -14.623 -17.373 -25.416 1.00 28.32  ? 289 CYS A C   1 
ATOM   2288 O O   . CYS A 1 290 ? -14.973 -16.330 -24.859 1.00 27.66  ? 289 CYS A O   1 
ATOM   2289 C CB  . CYS A 1 290 ? -15.972 -19.465 -25.101 1.00 32.91  ? 289 CYS A CB  1 
ATOM   2290 S SG  . CYS A 1 290 ? -17.497 -18.544 -24.814 1.00 32.76  ? 289 CYS A SG  1 
ATOM   2291 N N   . PRO A 1 291 ? -14.126 -17.368 -26.650 1.00 30.23  ? 290 PRO A N   1 
ATOM   2292 C CA  . PRO A 1 291 ? -14.038 -16.105 -27.395 1.00 30.83  ? 290 PRO A CA  1 
ATOM   2293 C C   . PRO A 1 291 ? -15.409 -15.450 -27.484 1.00 32.03  ? 290 PRO A C   1 
ATOM   2294 O O   . PRO A 1 291 ? -16.423 -16.118 -27.702 1.00 34.22  ? 290 PRO A O   1 
ATOM   2295 C CB  . PRO A 1 291 ? -13.518 -16.542 -28.770 1.00 32.97  ? 290 PRO A CB  1 
ATOM   2296 C CG  . PRO A 1 291 ? -12.791 -17.820 -28.498 1.00 32.13  ? 290 PRO A CG  1 
ATOM   2297 C CD  . PRO A 1 291 ? -13.603 -18.500 -27.433 1.00 30.73  ? 290 PRO A CD  1 
ATOM   2298 N N   . ARG A 1 292 ? -15.443 -14.144 -27.264 1.00 29.49  ? 291 ARG A N   1 
ATOM   2299 C CA  . ARG A 1 292 ? -16.715 -13.454 -27.116 1.00 29.17  ? 291 ARG A CA  1 
ATOM   2300 C C   . ARG A 1 292 ? -16.468 -11.965 -27.262 1.00 29.41  ? 291 ARG A C   1 
ATOM   2301 O O   . ARG A 1 292 ? -15.336 -11.488 -27.187 1.00 30.62  ? 291 ARG A O   1 
ATOM   2302 C CB  . ARG A 1 292 ? -17.378 -13.759 -25.766 1.00 28.20  ? 291 ARG A CB  1 
ATOM   2303 C CG  . ARG A 1 292 ? -16.582 -13.244 -24.573 1.00 27.81  ? 291 ARG A CG  1 
ATOM   2304 C CD  . ARG A 1 292 ? -17.238 -13.570 -23.232 1.00 26.34  ? 291 ARG A CD  1 
ATOM   2305 N NE  . ARG A 1 292 ? -17.368 -15.006 -22.989 1.00 29.16  ? 291 ARG A NE  1 
ATOM   2306 C CZ  . ARG A 1 292 ? -18.028 -15.540 -21.968 1.00 29.39  ? 291 ARG A CZ  1 
ATOM   2307 N NH1 . ARG A 1 292 ? -18.609 -14.787 -21.052 1.00 26.38  ? 291 ARG A NH1 1 
ATOM   2308 N NH2 . ARG A 1 292 ? -18.108 -16.865 -21.866 1.00 29.42  ? 291 ARG A NH2 1 
ATOM   2309 N N   . ARG A 1 293 ? -17.544 -11.231 -27.451 1.00 29.75  ? 292 ARG A N   1 
ATOM   2310 C CA  . ARG A 1 293 ? -17.451 -9.796  -27.617 1.00 29.18  ? 292 ARG A CA  1 
ATOM   2311 C C   . ARG A 1 293 ? -18.442 -9.111  -26.693 1.00 28.12  ? 292 ARG A C   1 
ATOM   2312 O O   . ARG A 1 293 ? -19.507 -9.655  -26.379 1.00 29.71  ? 292 ARG A O   1 
ATOM   2313 C CB  . ARG A 1 293 ? -17.731 -9.394  -29.063 1.00 29.20  ? 292 ARG A CB  1 
ATOM   2314 C CG  . ARG A 1 293 ? -19.093 -9.859  -29.558 1.00 32.16  ? 292 ARG A CG  1 
ATOM   2315 C CD  . ARG A 1 293 ? -19.373 -9.232  -30.890 1.00 35.03  ? 292 ARG A CD  1 
ATOM   2316 N NE  . ARG A 1 293 ? -20.783 -9.212  -31.256 1.00 35.05  ? 292 ARG A NE  1 
ATOM   2317 C CZ  . ARG A 1 293 ? -21.307 -9.917  -32.250 1.00 34.61  ? 292 ARG A CZ  1 
ATOM   2318 N NH1 . ARG A 1 293 ? -20.606 -10.836 -32.896 1.00 34.72  ? 292 ARG A NH1 1 
ATOM   2319 N NH2 . ARG A 1 293 ? -22.556 -9.676  -32.622 1.00 36.50  ? 292 ARG A NH2 1 
ATOM   2320 N N   . ARG A 1 294 ? -18.073 -7.905  -26.265 1.00 27.95  ? 293 ARG A N   1 
ATOM   2321 C CA  . ARG A 1 294 ? -19.005 -6.966  -25.648 1.00 27.18  ? 293 ARG A CA  1 
ATOM   2322 C C   . ARG A 1 294 ? -19.552 -7.527  -24.335 1.00 27.16  ? 293 ARG A C   1 
ATOM   2323 O O   . ARG A 1 294 ? -20.670 -7.223  -23.913 1.00 25.46  ? 293 ARG A O   1 
ATOM   2324 C CB  . ARG A 1 294 ? -20.116 -6.586  -26.638 1.00 25.84  ? 293 ARG A CB  1 
ATOM   2325 C CG  . ARG A 1 294 ? -20.759 -5.250  -26.363 1.00 28.24  ? 293 ARG A CG  1 
ATOM   2326 C CD  . ARG A 1 294 ? -19.759 -4.107  -26.159 1.00 26.77  ? 293 ARG A CD  1 
ATOM   2327 N NE  . ARG A 1 294 ? -20.482 -2.880  -25.833 1.00 27.87  ? 293 ARG A NE  1 
ATOM   2328 C CZ  . ARG A 1 294 ? -19.972 -1.657  -25.829 1.00 26.45  ? 293 ARG A CZ  1 
ATOM   2329 N NH1 . ARG A 1 294 ? -18.695 -1.436  -26.093 1.00 29.57  ? 293 ARG A NH1 1 
ATOM   2330 N NH2 . ARG A 1 294 ? -20.765 -0.626  -25.557 1.00 25.01  ? 293 ARG A NH2 1 
ATOM   2331 N N   . GLN A 1 295 ? -18.749 -8.385  -23.711 1.00 27.55  ? 294 GLN A N   1 
ATOM   2332 C CA  . GLN A 1 295 ? -18.813 -8.635  -22.287 1.00 25.87  ? 294 GLN A CA  1 
ATOM   2333 C C   . GLN A 1 295 ? -18.457 -7.354  -21.527 1.00 27.34  ? 294 GLN A C   1 
ATOM   2334 O O   . GLN A 1 295 ? -17.998 -6.367  -22.104 1.00 23.44  ? 294 GLN A O   1 
ATOM   2335 C CB  . GLN A 1 295 ? -17.842 -9.749  -21.912 1.00 24.19  ? 294 GLN A CB  1 
ATOM   2336 C CG  . GLN A 1 295 ? -16.357 -9.366  -22.048 1.00 23.64  ? 294 GLN A CG  1 
ATOM   2337 C CD  . GLN A 1 295 ? -15.949 -9.061  -23.471 1.00 27.82  ? 294 GLN A CD  1 
ATOM   2338 O OE1 . GLN A 1 295 ? -16.253 -9.834  -24.376 1.00 30.78  ? 294 GLN A OE1 1 
ATOM   2339 N NE2 . GLN A 1 295 ? -15.273 -7.922  -23.689 1.00 25.19  ? 294 GLN A NE2 1 
ATOM   2340 N N   . CYS A 1 296 ? -18.667 -7.380  -20.210 1.00 25.84  ? 295 CYS A N   1 
ATOM   2341 C CA  . CYS A 1 296 ? -18.187 -6.320  -19.337 1.00 25.95  ? 295 CYS A CA  1 
ATOM   2342 C C   . CYS A 1 296 ? -17.089 -6.834  -18.404 1.00 29.58  ? 295 CYS A C   1 
ATOM   2343 O O   . CYS A 1 296 ? -17.095 -7.995  -17.986 1.00 28.99  ? 295 CYS A O   1 
ATOM   2344 C CB  . CYS A 1 296 ? -19.332 -5.719  -18.528 1.00 25.16  ? 295 CYS A CB  1 
ATOM   2345 S SG  . CYS A 1 296 ? -20.327 -4.573  -19.477 1.00 34.28  ? 295 CYS A SG  1 
ATOM   2346 N N   . CYS A 1 297 ? -16.130 -5.951  -18.098 1.00 28.59  ? 296 CYS A N   1 
ATOM   2347 C CA  . CYS A 1 297 ? -15.022 -6.232  -17.191 1.00 24.73  ? 296 CYS A CA  1 
ATOM   2348 C C   . CYS A 1 297 ? -14.937 -5.152  -16.126 1.00 28.82  ? 296 CYS A C   1 
ATOM   2349 O O   . CYS A 1 297 ? -14.936 -3.963  -16.452 1.00 29.63  ? 296 CYS A O   1 
ATOM   2350 C CB  . CYS A 1 297 ? -13.697 -6.293  -17.937 1.00 25.48  ? 296 CYS A CB  1 
ATOM   2351 S SG  . CYS A 1 297 ? -13.452 -7.847  -18.752 1.00 32.27  ? 296 CYS A SG  1 
ATOM   2352 N N   . CYS A 1 298 ? -14.839 -5.560  -14.860 1.00 28.03  ? 297 CYS A N   1 
ATOM   2353 C CA  . CYS A 1 298 ? -14.685 -4.631  -13.751 1.00 25.11  ? 297 CYS A CA  1 
ATOM   2354 C C   . CYS A 1 298 ? -13.586 -5.124  -12.833 1.00 27.48  ? 297 CYS A C   1 
ATOM   2355 O O   . CYS A 1 298 ? -13.360 -6.333  -12.707 1.00 27.00  ? 297 CYS A O   1 
ATOM   2356 C CB  . CYS A 1 298 ? -15.986 -4.466  -12.950 1.00 25.76  ? 297 CYS A CB  1 
ATOM   2357 S SG  . CYS A 1 298 ? -17.309 -3.744  -13.914 1.00 29.15  ? 297 CYS A SG  1 
ATOM   2358 N N   . ILE A 1 299 ? -12.918 -4.174  -12.177 1.00 27.33  ? 298 ILE A N   1 
ATOM   2359 C CA  . ILE A 1 299 ? -11.778 -4.456  -11.317 1.00 25.31  ? 298 ILE A CA  1 
ATOM   2360 C C   . ILE A 1 299 ? -12.256 -4.504  -9.871  1.00 30.20  ? 298 ILE A C   1 
ATOM   2361 O O   . ILE A 1 299 ? -12.964 -3.598  -9.411  1.00 30.42  ? 298 ILE A O   1 
ATOM   2362 C CB  . ILE A 1 299 ? -10.678 -3.398  -11.500 1.00 27.99  ? 298 ILE A CB  1 
ATOM   2363 C CG1 . ILE A 1 299 ? -10.218 -3.358  -12.950 1.00 29.54  ? 298 ILE A CG1 1 
ATOM   2364 C CG2 . ILE A 1 299 ? -9.481  -3.699  -10.614 1.00 30.57  ? 298 ILE A CG2 1 
ATOM   2365 C CD1 . ILE A 1 299 ? -9.167  -2.289  -13.215 1.00 25.14  ? 298 ILE A CD1 1 
ATOM   2366 N N   . VAL A 1 300 ? -11.881 -5.558  -9.150  1.00 28.45  ? 299 VAL A N   1 
ATOM   2367 C CA  . VAL A 1 300 ? -12.161 -5.669  -7.724  1.00 31.17  ? 299 VAL A CA  1 
ATOM   2368 C C   . VAL A 1 300 ? -10.860 -6.069  -7.055  1.00 29.90  ? 299 VAL A C   1 
ATOM   2369 O O   . VAL A 1 300 ? -10.500 -7.253  -7.048  1.00 31.06  ? 299 VAL A O   1 
ATOM   2370 C CB  . VAL A 1 300 ? -13.272 -6.679  -7.410  1.00 30.47  ? 299 VAL A CB  1 
ATOM   2371 C CG1 . VAL A 1 300 ? -13.550 -6.667  -5.920  1.00 26.70  ? 299 VAL A CG1 1 
ATOM   2372 C CG2 . VAL A 1 300 ? -14.535 -6.350  -8.192  1.00 28.91  ? 299 VAL A CG2 1 
ATOM   2373 N N   . GLY A 1 301 ? -10.156 -5.093  -6.483  1.00 30.92  ? 300 GLY A N   1 
ATOM   2374 C CA  . GLY A 1 301 ? -8.831  -5.366  -5.939  1.00 26.74  ? 300 GLY A CA  1 
ATOM   2375 C C   . GLY A 1 301 ? -7.901  -5.838  -7.050  1.00 34.50  ? 300 GLY A C   1 
ATOM   2376 O O   . GLY A 1 301 ? -7.705  -5.158  -8.074  1.00 32.12  ? 300 GLY A O   1 
ATOM   2377 N N   . ASP A 1 302 ? -7.341  -7.031  -6.872  1.00 30.20  ? 301 ASP A N   1 
ATOM   2378 C CA  . ASP A 1 302 ? -6.442  -7.636  -7.842  1.00 31.28  ? 301 ASP A CA  1 
ATOM   2379 C C   . ASP A 1 302 ? -7.149  -8.571  -8.798  1.00 32.50  ? 301 ASP A C   1 
ATOM   2380 O O   . ASP A 1 302 ? -6.483  -9.361  -9.479  1.00 30.20  ? 301 ASP A O   1 
ATOM   2381 C CB  . ASP A 1 302 ? -5.346  -8.404  -7.127  1.00 34.96  ? 301 ASP A CB  1 
ATOM   2382 C CG  . ASP A 1 302 ? -4.471  -7.512  -6.331  1.00 36.66  ? 301 ASP A CG  1 
ATOM   2383 O OD1 . ASP A 1 302 ? -4.158  -6.402  -6.832  1.00 37.06  ? 301 ASP A OD1 1 
ATOM   2384 O OD2 . ASP A 1 302 ? -4.111  -7.917  -5.206  1.00 39.77  ? 301 ASP A OD2 1 
ATOM   2385 N N   . LYS A 1 303 ? -8.476  -8.516  -8.850  1.00 29.13  ? 302 LYS A N   1 
ATOM   2386 C CA  . LYS A 1 303 ? -9.261  -9.411  -9.678  1.00 28.80  ? 302 LYS A CA  1 
ATOM   2387 C C   . LYS A 1 303 ? -10.078 -8.616  -10.684 1.00 29.06  ? 302 LYS A C   1 
ATOM   2388 O O   . LYS A 1 303 ? -10.447 -7.467  -10.445 1.00 32.05  ? 302 LYS A O   1 
ATOM   2389 C CB  . LYS A 1 303 ? -10.169 -10.264 -8.821  1.00 26.22  ? 302 LYS A CB  1 
ATOM   2390 C CG  . LYS A 1 303 ? -9.411  -11.033 -7.775  1.00 29.25  ? 302 LYS A CG  1 
ATOM   2391 C CD  . LYS A 1 303 ? -10.356 -11.689 -6.817  1.00 28.91  ? 302 LYS A CD  1 
ATOM   2392 C CE  . LYS A 1 303 ? -9.655  -12.152 -5.574  1.00 32.22  ? 302 LYS A CE  1 
ATOM   2393 N NZ  . LYS A 1 303 ? -10.685 -12.708 -4.646  1.00 36.86  ? 302 LYS A NZ  1 
ATOM   2394 N N   . ILE A 1 304 ? -10.328 -9.231  -11.829 1.00 28.65  ? 303 ILE A N   1 
ATOM   2395 C CA  . ILE A 1 304 ? -11.233 -8.704  -12.838 1.00 26.48  ? 303 ILE A CA  1 
ATOM   2396 C C   . ILE A 1 304 ? -12.457 -9.603  -12.867 1.00 25.68  ? 303 ILE A C   1 
ATOM   2397 O O   . ILE A 1 304 ? -12.328 -10.829 -12.986 1.00 23.28  ? 303 ILE A O   1 
ATOM   2398 C CB  . ILE A 1 304 ? -10.566 -8.648  -14.224 1.00 29.63  ? 303 ILE A CB  1 
ATOM   2399 C CG1 . ILE A 1 304 ? -9.105  -8.209  -14.100 1.00 26.93  ? 303 ILE A CG1 1 
ATOM   2400 C CG2 . ILE A 1 304 ? -11.349 -7.726  -15.158 1.00 27.44  ? 303 ILE A CG2 1 
ATOM   2401 C CD1 . ILE A 1 304 ? -8.949  -6.768  -13.676 1.00 28.51  ? 303 ILE A CD1 1 
ATOM   2402 N N   . VAL A 1 305 ? -13.632 -9.004  -12.720 1.00 28.54  ? 304 VAL A N   1 
ATOM   2403 C CA  . VAL A 1 305 ? -14.898 -9.703  -12.921 1.00 27.03  ? 304 VAL A CA  1 
ATOM   2404 C C   . VAL A 1 305 ? -15.314 -9.487  -14.370 1.00 26.38  ? 304 VAL A C   1 
ATOM   2405 O O   . VAL A 1 305 ? -15.540 -8.345  -14.793 1.00 25.46  ? 304 VAL A O   1 
ATOM   2406 C CB  . VAL A 1 305 ? -15.973 -9.200  -11.943 1.00 27.75  ? 304 VAL A CB  1 
ATOM   2407 C CG1 . VAL A 1 305 ? -17.271 -9.950  -12.135 1.00 24.35  ? 304 VAL A CG1 1 
ATOM   2408 C CG2 . VAL A 1 305 ? -15.485 -9.341  -10.510 1.00 25.37  ? 304 VAL A CG2 1 
ATOM   2409 N N   . LEU A 1 306 ? -15.384 -10.583 -15.131 1.00 24.77  ? 305 LEU A N   1 
ATOM   2410 C CA  . LEU A 1 306 ? -15.720 -10.589 -16.551 1.00 22.60  ? 305 LEU A CA  1 
ATOM   2411 C C   . LEU A 1 306 ? -16.996 -11.403 -16.725 1.00 27.42  ? 305 LEU A C   1 
ATOM   2412 O O   . LEU A 1 306 ? -17.081 -12.531 -16.234 1.00 29.98  ? 305 LEU A O   1 
ATOM   2413 C CB  . LEU A 1 306 ? -14.570 -11.188 -17.365 1.00 24.36  ? 305 LEU A CB  1 
ATOM   2414 C CG  . LEU A 1 306 ? -14.564 -11.293 -18.904 1.00 29.95  ? 305 LEU A CG  1 
ATOM   2415 C CD1 . LEU A 1 306 ? -13.151 -11.573 -19.408 1.00 24.24  ? 305 LEU A CD1 1 
ATOM   2416 C CD2 . LEU A 1 306 ? -15.545 -12.355 -19.490 1.00 25.98  ? 305 LEU A CD2 1 
ATOM   2417 N N   . PHE A 1 307 ? -17.984 -10.851 -17.424 1.00 25.71  ? 306 PHE A N   1 
ATOM   2418 C CA  . PHE A 1 307 ? -19.267 -11.540 -17.503 1.00 27.77  ? 306 PHE A CA  1 
ATOM   2419 C C   . PHE A 1 307 ? -20.077 -10.999 -18.675 1.00 27.36  ? 306 PHE A C   1 
ATOM   2420 O O   . PHE A 1 307 ? -19.912 -9.841  -19.077 1.00 26.11  ? 306 PHE A O   1 
ATOM   2421 C CB  . PHE A 1 307 ? -20.056 -11.384 -16.191 1.00 26.04  ? 306 PHE A CB  1 
ATOM   2422 C CG  . PHE A 1 307 ? -20.484 -9.977  -15.920 1.00 26.61  ? 306 PHE A CG  1 
ATOM   2423 C CD1 . PHE A 1 307 ? -19.563 -9.032  -15.484 1.00 27.06  ? 306 PHE A CD1 1 
ATOM   2424 C CD2 . PHE A 1 307 ? -21.805 -9.580  -16.135 1.00 28.13  ? 306 PHE A CD2 1 
ATOM   2425 C CE1 . PHE A 1 307 ? -19.944 -7.719  -15.253 1.00 25.84  ? 306 PHE A CE1 1 
ATOM   2426 C CE2 . PHE A 1 307 ? -22.196 -8.269  -15.902 1.00 27.96  ? 306 PHE A CE2 1 
ATOM   2427 C CZ  . PHE A 1 307 ? -21.256 -7.334  -15.457 1.00 25.26  ? 306 PHE A CZ  1 
ATOM   2428 N N   . GLY A 1 308 ? -20.967 -11.857 -19.212 1.00 26.31  ? 307 GLY A N   1 
ATOM   2429 C CA  . GLY A 1 308 ? -21.833 -11.480 -20.314 1.00 24.80  ? 307 GLY A CA  1 
ATOM   2430 C C   . GLY A 1 308 ? -21.141 -11.556 -21.666 1.00 28.32  ? 307 GLY A C   1 
ATOM   2431 O O   . GLY A 1 308 ? -20.034 -12.093 -21.807 1.00 26.75  ? 307 GLY A O   1 
ATOM   2432 N N   . GLY A 1 309 ? -21.821 -11.009 -22.680 1.00 27.29  ? 308 GLY A N   1 
ATOM   2433 C CA  . GLY A 1 309 ? -21.296 -10.896 -24.029 1.00 26.41  ? 308 GLY A CA  1 
ATOM   2434 C C   . GLY A 1 309 ? -21.935 -11.895 -24.983 1.00 28.68  ? 308 GLY A C   1 
ATOM   2435 O O   . GLY A 1 309 ? -22.813 -12.678 -24.622 1.00 28.07  ? 308 GLY A O   1 
ATOM   2436 N N   . THR A 1 310 ? -21.454 -11.866 -26.230 1.00 29.94  ? 309 THR A N   1 
ATOM   2437 C CA  . THR A 1 310 ? -21.991 -12.707 -27.291 1.00 31.92  ? 309 THR A CA  1 
ATOM   2438 C C   . THR A 1 310 ? -20.864 -13.508 -27.920 1.00 31.30  ? 309 THR A C   1 
ATOM   2439 O O   . THR A 1 310 ? -19.716 -13.073 -27.916 1.00 33.03  ? 309 THR A O   1 
ATOM   2440 C CB  . THR A 1 310 ? -22.710 -11.860 -28.351 1.00 31.71  ? 309 THR A CB  1 
ATOM   2441 O OG1 . THR A 1 310 ? -23.786 -11.160 -27.727 1.00 34.91  ? 309 THR A OG1 1 
ATOM   2442 C CG2 . THR A 1 310 ? -23.283 -12.712 -29.455 1.00 33.68  ? 309 THR A CG2 1 
ATOM   2443 N N   . SER A 1 311 ? -21.195 -14.692 -28.432 1.00 33.11  ? 310 SER A N   1 
ATOM   2444 C CA  . SER A 1 311 ? -20.233 -15.547 -29.113 1.00 37.63  ? 310 SER A CA  1 
ATOM   2445 C C   . SER A 1 311 ? -20.992 -16.488 -30.049 1.00 42.02  ? 310 SER A C   1 
ATOM   2446 O O   . SER A 1 311 ? -22.216 -16.628 -29.935 1.00 43.02  ? 310 SER A O   1 
ATOM   2447 C CB  . SER A 1 311 ? -19.388 -16.338 -28.104 1.00 36.71  ? 310 SER A CB  1 
ATOM   2448 O OG  . SER A 1 311 ? -20.181 -17.218 -27.335 1.00 34.33  ? 310 SER A OG  1 
ATOM   2449 N N   . PRO A 1 312 ? -20.307 -17.108 -31.010 1.00 44.92  ? 311 PRO A N   1 
ATOM   2450 C CA  . PRO A 1 312 ? -20.995 -18.049 -31.911 1.00 51.83  ? 311 PRO A CA  1 
ATOM   2451 C C   . PRO A 1 312 ? -21.469 -19.315 -31.202 1.00 53.94  ? 311 PRO A C   1 
ATOM   2452 O O   . PRO A 1 312 ? -20.864 -19.788 -30.240 1.00 54.27  ? 311 PRO A O   1 
ATOM   2453 C CB  . PRO A 1 312 ? -19.939 -18.372 -32.983 1.00 45.01  ? 311 PRO A CB  1 
ATOM   2454 C CG  . PRO A 1 312 ? -18.679 -17.739 -32.558 1.00 42.60  ? 311 PRO A CG  1 
ATOM   2455 C CD  . PRO A 1 312 ? -18.972 -16.726 -31.505 1.00 43.32  ? 311 PRO A CD  1 
ATOM   2456 N N   . SER A 1 313 ? -22.563 -19.876 -31.710 1.00 73.71  ? 312 SER A N   1 
ATOM   2457 C CA  . SER A 1 313 ? -23.226 -21.007 -31.065 1.00 78.67  ? 312 SER A CA  1 
ATOM   2458 C C   . SER A 1 313 ? -22.664 -22.330 -31.572 1.00 90.07  ? 312 SER A C   1 
ATOM   2459 O O   . SER A 1 313 ? -22.759 -22.606 -32.778 1.00 90.56  ? 312 SER A O   1 
ATOM   2460 C CB  . SER A 1 313 ? -24.717 -20.962 -31.333 1.00 80.28  ? 312 SER A CB  1 
ATOM   2461 O OG  . SER A 1 313 ? -25.286 -22.256 -31.248 1.00 93.60  ? 312 SER A OG  1 
ATOM   2462 N N   . PRO A 1 314 ? -22.106 -23.194 -30.699 1.00 85.01  ? 313 PRO A N   1 
ATOM   2463 C CA  . PRO A 1 314 ? -21.572 -24.506 -31.114 1.00 84.68  ? 313 PRO A CA  1 
ATOM   2464 C C   . PRO A 1 314 ? -22.615 -25.423 -31.765 1.00 78.27  ? 313 PRO A C   1 
ATOM   2465 O O   . PRO A 1 314 ? -22.616 -25.548 -32.991 1.00 76.85  ? 313 PRO A O   1 
ATOM   2466 C CB  . PRO A 1 314 ? -21.067 -25.115 -29.797 1.00 81.45  ? 313 PRO A CB  1 
ATOM   2467 C CG  . PRO A 1 314 ? -20.843 -23.935 -28.885 1.00 73.32  ? 313 PRO A CG  1 
ATOM   2468 C CD  . PRO A 1 314 ? -21.901 -22.938 -29.260 1.00 73.14  ? 313 PRO A CD  1 
ATOM   2469 N N   . PHE A 1 322 ? -25.455 -14.915 -37.721 1.00 99.53  ? 321 PHE A N   1 
ATOM   2470 C CA  . PHE A 1 322 ? -25.314 -16.355 -37.905 1.00 99.59  ? 321 PHE A CA  1 
ATOM   2471 C C   . PHE A 1 322 ? -25.063 -17.041 -36.566 1.00 91.91  ? 321 PHE A C   1 
ATOM   2472 O O   . PHE A 1 322 ? -23.917 -17.113 -36.116 1.00 94.54  ? 321 PHE A O   1 
ATOM   2473 C CB  . PHE A 1 322 ? -24.171 -16.668 -38.894 1.00 100.00 ? 321 PHE A CB  1 
ATOM   2474 C CG  . PHE A 1 322 ? -23.931 -18.148 -39.126 1.00 102.71 ? 321 PHE A CG  1 
ATOM   2475 C CD1 . PHE A 1 322 ? -24.666 -18.845 -40.078 1.00 108.10 ? 321 PHE A CD1 1 
ATOM   2476 C CD2 . PHE A 1 322 ? -22.951 -18.835 -38.411 1.00 101.49 ? 321 PHE A CD2 1 
ATOM   2477 C CE1 . PHE A 1 322 ? -24.443 -20.206 -40.301 1.00 111.26 ? 321 PHE A CE1 1 
ATOM   2478 C CE2 . PHE A 1 322 ? -22.725 -20.191 -38.623 1.00 103.27 ? 321 PHE A CE2 1 
ATOM   2479 C CZ  . PHE A 1 322 ? -23.473 -20.876 -39.573 1.00 109.10 ? 321 PHE A CZ  1 
ATOM   2480 N N   . ASP A 1 323 ? -26.128 -17.525 -35.925 1.00 75.60  ? 322 ASP A N   1 
ATOM   2481 C CA  . ASP A 1 323 ? -26.007 -18.471 -34.815 1.00 73.98  ? 322 ASP A CA  1 
ATOM   2482 C C   . ASP A 1 323 ? -25.099 -17.924 -33.708 1.00 63.31  ? 322 ASP A C   1 
ATOM   2483 O O   . ASP A 1 323 ? -23.988 -18.397 -33.482 1.00 62.94  ? 322 ASP A O   1 
ATOM   2484 C CB  . ASP A 1 323 ? -25.487 -19.826 -35.311 1.00 83.19  ? 322 ASP A CB  1 
ATOM   2485 C CG  . ASP A 1 323 ? -26.511 -20.587 -36.139 1.00 88.82  ? 322 ASP A CG  1 
ATOM   2486 O OD1 . ASP A 1 323 ? -27.631 -20.821 -35.630 1.00 83.88  ? 322 ASP A OD1 1 
ATOM   2487 O OD2 . ASP A 1 323 ? -26.195 -20.953 -37.298 1.00 94.99  ? 322 ASP A OD2 1 
ATOM   2488 N N   . LEU A 1 324 ? -25.580 -16.875 -33.058 1.00 56.52  ? 323 LEU A N   1 
ATOM   2489 C CA  . LEU A 1 324 ? -24.920 -16.323 -31.888 1.00 49.78  ? 323 LEU A CA  1 
ATOM   2490 C C   . LEU A 1 324 ? -25.707 -16.664 -30.631 1.00 45.73  ? 323 LEU A C   1 
ATOM   2491 O O   . LEU A 1 324 ? -26.909 -16.929 -30.682 1.00 52.63  ? 323 LEU A O   1 
ATOM   2492 C CB  . LEU A 1 324 ? -24.774 -14.804 -32.001 1.00 47.68  ? 323 LEU A CB  1 
ATOM   2493 C CG  . LEU A 1 324 ? -23.944 -14.259 -33.156 1.00 48.22  ? 323 LEU A CG  1 
ATOM   2494 C CD1 . LEU A 1 324 ? -23.999 -12.738 -33.140 1.00 37.86  ? 323 LEU A CD1 1 
ATOM   2495 C CD2 . LEU A 1 324 ? -22.503 -14.759 -33.079 1.00 45.73  ? 323 LEU A CD2 1 
ATOM   2496 N N   . ILE A 1 325 ? -25.014 -16.646 -29.490 1.00 45.63  ? 324 ILE A N   1 
ATOM   2497 C CA  . ILE A 1 325 ? -25.638 -16.800 -28.180 1.00 37.17  ? 324 ILE A CA  1 
ATOM   2498 C C   . ILE A 1 325 ? -25.190 -15.658 -27.280 1.00 39.92  ? 324 ILE A C   1 
ATOM   2499 O O   . ILE A 1 325 ? -24.114 -15.070 -27.456 1.00 38.75  ? 324 ILE A O   1 
ATOM   2500 C CB  . ILE A 1 325 ? -25.290 -18.136 -27.499 1.00 37.97  ? 324 ILE A CB  1 
ATOM   2501 C CG1 . ILE A 1 325 ? -23.777 -18.207 -27.300 1.00 40.06  ? 324 ILE A CG1 1 
ATOM   2502 C CG2 . ILE A 1 325 ? -25.795 -19.304 -28.296 1.00 40.70  ? 324 ILE A CG2 1 
ATOM   2503 C CD1 . ILE A 1 325 ? -23.327 -19.302 -26.401 1.00 40.66  ? 324 ILE A CD1 1 
ATOM   2504 N N   . ASP A 1 326 ? -26.021 -15.379 -26.280 1.00 35.35  ? 325 ASP A N   1 
ATOM   2505 C CA  . ASP A 1 326 ? -25.719 -14.406 -25.246 1.00 34.37  ? 325 ASP A CA  1 
ATOM   2506 C C   . ASP A 1 326 ? -25.366 -15.124 -23.951 1.00 34.28  ? 325 ASP A C   1 
ATOM   2507 O O   . ASP A 1 326 ? -25.890 -16.203 -23.659 1.00 33.77  ? 325 ASP A O   1 
ATOM   2508 C CB  . ASP A 1 326 ? -26.909 -13.477 -25.047 1.00 36.82  ? 325 ASP A CB  1 
ATOM   2509 C CG  . ASP A 1 326 ? -27.388 -12.904 -26.349 1.00 37.77  ? 325 ASP A CG  1 
ATOM   2510 O OD1 . ASP A 1 326 ? -26.547 -12.310 -27.040 1.00 34.12  ? 325 ASP A OD1 1 
ATOM   2511 O OD2 . ASP A 1 326 ? -28.574 -13.089 -26.706 1.00 39.74  ? 325 ASP A OD2 1 
ATOM   2512 N N   . HIS A 1 327 ? -24.471 -14.522 -23.171 1.00 30.31  ? 326 HIS A N   1 
ATOM   2513 C CA  . HIS A 1 327 ? -23.853 -15.221 -22.055 1.00 30.70  ? 326 HIS A CA  1 
ATOM   2514 C C   . HIS A 1 327 ? -24.417 -14.789 -20.707 1.00 30.39  ? 326 HIS A C   1 
ATOM   2515 O O   . HIS A 1 327 ? -24.580 -13.595 -20.435 1.00 28.25  ? 326 HIS A O   1 
ATOM   2516 C CB  . HIS A 1 327 ? -22.343 -15.030 -22.085 1.00 29.43  ? 326 HIS A CB  1 
ATOM   2517 C CG  . HIS A 1 327 ? -21.670 -15.927 -23.066 1.00 32.45  ? 326 HIS A CG  1 
ATOM   2518 N ND1 . HIS A 1 327 ? -21.438 -17.260 -22.805 1.00 33.30  ? 326 HIS A ND1 1 
ATOM   2519 C CD2 . HIS A 1 327 ? -21.226 -15.700 -24.327 1.00 32.79  ? 326 HIS A CD2 1 
ATOM   2520 C CE1 . HIS A 1 327 ? -20.854 -17.810 -23.857 1.00 35.11  ? 326 HIS A CE1 1 
ATOM   2521 N NE2 . HIS A 1 327 ? -20.716 -16.887 -24.793 1.00 32.78  ? 326 HIS A NE2 1 
ATOM   2522 N N   . SER A 1 328 ? -24.722 -15.778 -19.875 1.00 28.67  ? 327 SER A N   1 
ATOM   2523 C CA  . SER A 1 328 ? -25.043 -15.557 -18.475 1.00 31.28  ? 327 SER A CA  1 
ATOM   2524 C C   . SER A 1 328 ? -23.897 -15.936 -17.553 1.00 33.17  ? 327 SER A C   1 
ATOM   2525 O O   . SER A 1 328 ? -24.074 -15.914 -16.333 1.00 33.12  ? 327 SER A O   1 
ATOM   2526 C CB  . SER A 1 328 ? -26.292 -16.349 -18.089 1.00 29.96  ? 327 SER A CB  1 
ATOM   2527 O OG  . SER A 1 328 ? -26.317 -17.590 -18.764 1.00 30.63  ? 327 SER A OG  1 
ATOM   2528 N N   . ASP A 1 329 ? -22.739 -16.300 -18.094 1.00 29.23  ? 328 ASP A N   1 
ATOM   2529 C CA  . ASP A 1 329 ? -21.653 -16.715 -17.231 1.00 28.50  ? 328 ASP A CA  1 
ATOM   2530 C C   . ASP A 1 329 ? -20.807 -15.518 -16.795 1.00 30.13  ? 328 ASP A C   1 
ATOM   2531 O O   . ASP A 1 329 ? -21.018 -14.366 -17.202 1.00 27.39  ? 328 ASP A O   1 
ATOM   2532 C CB  . ASP A 1 329 ? -20.797 -17.790 -17.901 1.00 30.27  ? 328 ASP A CB  1 
ATOM   2533 C CG  . ASP A 1 329 ? -20.061 -17.294 -19.136 1.00 31.37  ? 328 ASP A CG  1 
ATOM   2534 O OD1 . ASP A 1 329 ? -20.448 -16.258 -19.728 1.00 31.40  ? 328 ASP A OD1 1 
ATOM   2535 O OD2 . ASP A 1 329 ? -19.088 -17.968 -19.531 1.00 30.42  ? 328 ASP A OD2 1 
ATOM   2536 N N   . LEU A 1 330 ? -19.866 -15.818 -15.901 1.00 31.46  ? 329 LEU A N   1 
ATOM   2537 C CA  . LEU A 1 330 ? -19.034 -14.837 -15.221 1.00 27.28  ? 329 LEU A CA  1 
ATOM   2538 C C   . LEU A 1 330 ? -17.708 -15.510 -14.922 1.00 28.40  ? 329 LEU A C   1 
ATOM   2539 O O   . LEU A 1 330 ? -17.674 -16.642 -14.421 1.00 28.13  ? 329 LEU A O   1 
ATOM   2540 C CB  . LEU A 1 330 ? -19.685 -14.325 -13.922 1.00 25.48  ? 329 LEU A CB  1 
ATOM   2541 C CG  . LEU A 1 330 ? -18.895 -13.340 -13.032 1.00 25.56  ? 329 LEU A CG  1 
ATOM   2542 C CD1 . LEU A 1 330 ? -19.846 -12.488 -12.198 1.00 23.26  ? 329 LEU A CD1 1 
ATOM   2543 C CD2 . LEU A 1 330 ? -17.904 -14.039 -12.097 1.00 24.14  ? 329 LEU A CD2 1 
ATOM   2544 N N   . HIS A 1 331 ? -16.628 -14.797 -15.203 1.00 27.70  ? 330 HIS A N   1 
ATOM   2545 C CA  . HIS A 1 331 ? -15.285 -15.287 -14.976 1.00 26.04  ? 330 HIS A CA  1 
ATOM   2546 C C   . HIS A 1 331 ? -14.571 -14.322 -14.047 1.00 28.28  ? 330 HIS A C   1 
ATOM   2547 O O   . HIS A 1 331 ? -14.870 -13.118 -14.027 1.00 26.25  ? 330 HIS A O   1 
ATOM   2548 C CB  . HIS A 1 331 ? -14.531 -15.434 -16.303 1.00 24.91  ? 330 HIS A CB  1 
ATOM   2549 C CG  . HIS A 1 331 ? -15.144 -16.433 -17.224 1.00 26.91  ? 330 HIS A CG  1 
ATOM   2550 N ND1 . HIS A 1 331 ? -14.581 -17.667 -17.459 1.00 29.09  ? 330 HIS A ND1 1 
ATOM   2551 C CD2 . HIS A 1 331 ? -16.297 -16.402 -17.934 1.00 28.64  ? 330 HIS A CD2 1 
ATOM   2552 C CE1 . HIS A 1 331 ? -15.343 -18.345 -18.299 1.00 28.82  ? 330 HIS A CE1 1 
ATOM   2553 N NE2 . HIS A 1 331 ? -16.393 -17.601 -18.599 1.00 31.20  ? 330 HIS A NE2 1 
ATOM   2554 N N   . ILE A 1 332 ? -13.638 -14.852 -13.261 1.00 24.64  ? 331 ILE A N   1 
ATOM   2555 C CA  . ILE A 1 332 ? -12.761 -14.008 -12.475 1.00 26.48  ? 331 ILE A CA  1 
ATOM   2556 C C   . ILE A 1 332 ? -11.329 -14.320 -12.859 1.00 27.99  ? 331 ILE A C   1 
ATOM   2557 O O   . ILE A 1 332 ? -10.907 -15.484 -12.827 1.00 26.79  ? 331 ILE A O   1 
ATOM   2558 C CB  . ILE A 1 332 ? -12.981 -14.179 -10.972 1.00 29.44  ? 331 ILE A CB  1 
ATOM   2559 C CG1 . ILE A 1 332 ? -14.322 -13.557 -10.577 1.00 22.83  ? 331 ILE A CG1 1 
ATOM   2560 C CG2 . ILE A 1 332 ? -11.786 -13.551 -10.203 1.00 26.32  ? 331 ILE A CG2 1 
ATOM   2561 C CD1 . ILE A 1 332 ? -14.822 -14.021 -9.236  1.00 22.86  ? 331 ILE A CD1 1 
ATOM   2562 N N   . LEU A 1 333 ? -10.605 -13.280 -13.257 1.00 30.05  ? 332 LEU A N   1 
ATOM   2563 C CA  . LEU A 1 333 ? -9.172  -13.331 -13.497 1.00 28.39  ? 332 LEU A CA  1 
ATOM   2564 C C   . LEU A 1 333 ? -8.488  -12.733 -12.277 1.00 27.94  ? 332 LEU A C   1 
ATOM   2565 O O   . LEU A 1 333 ? -8.789  -11.595 -11.891 1.00 25.90  ? 332 LEU A O   1 
ATOM   2566 C CB  . LEU A 1 333 ? -8.807  -12.561 -14.764 1.00 26.75  ? 332 LEU A CB  1 
ATOM   2567 C CG  . LEU A 1 333 ? -7.335  -12.471 -15.169 1.00 26.71  ? 332 LEU A CG  1 
ATOM   2568 C CD1 . LEU A 1 333 ? -6.767  -13.831 -15.579 1.00 23.66  ? 332 LEU A CD1 1 
ATOM   2569 C CD2 . LEU A 1 333 ? -7.185  -11.454 -16.295 1.00 25.09  ? 332 LEU A CD2 1 
ATOM   2570 N N   . ASP A 1 334 ? -7.611  -13.518 -11.647 1.00 29.61  ? 333 ASP A N   1 
ATOM   2571 C CA  . ASP A 1 334 ? -6.909  -13.126 -10.427 1.00 27.73  ? 333 ASP A CA  1 
ATOM   2572 C C   . ASP A 1 334 ? -5.452  -12.860 -10.786 1.00 28.54  ? 333 ASP A C   1 
ATOM   2573 O O   . ASP A 1 334 ? -4.717  -13.785 -11.146 1.00 29.03  ? 333 ASP A O   1 
ATOM   2574 C CB  . ASP A 1 334 ? -7.025  -14.221 -9.375  1.00 30.33  ? 333 ASP A CB  1 
ATOM   2575 C CG  . ASP A 1 334 ? -6.509  -13.796 -7.994  1.00 30.50  ? 333 ASP A CG  1 
ATOM   2576 O OD1 . ASP A 1 334 ? -5.643  -12.898 -7.874  1.00 27.10  ? 333 ASP A OD1 1 
ATOM   2577 O OD2 . ASP A 1 334 ? -7.000  -14.394 -7.013  1.00 32.00  ? 333 ASP A OD2 1 
ATOM   2578 N N   . PHE A 1 335 ? -5.028  -11.603 -10.652 1.00 28.18  ? 334 PHE A N   1 
ATOM   2579 C CA  . PHE A 1 335 ? -3.653  -11.248 -10.966 1.00 28.30  ? 334 PHE A CA  1 
ATOM   2580 C C   . PHE A 1 335 ? -2.636  -11.796 -9.975  1.00 29.70  ? 334 PHE A C   1 
ATOM   2581 O O   . PHE A 1 335 ? -1.445  -11.866 -10.317 1.00 36.24  ? 334 PHE A O   1 
ATOM   2582 C CB  . PHE A 1 335 ? -3.514  -9.738  -11.065 1.00 25.88  ? 334 PHE A CB  1 
ATOM   2583 C CG  . PHE A 1 335 ? -3.892  -9.208  -12.405 1.00 28.05  ? 334 PHE A CG  1 
ATOM   2584 C CD1 . PHE A 1 335 ? -5.214  -8.890  -12.697 1.00 29.43  ? 334 PHE A CD1 1 
ATOM   2585 C CD2 . PHE A 1 335 ? -2.939  -9.061  -13.396 1.00 25.64  ? 334 PHE A CD2 1 
ATOM   2586 C CE1 . PHE A 1 335 ? -5.569  -8.405  -13.957 1.00 27.61  ? 334 PHE A CE1 1 
ATOM   2587 C CE2 . PHE A 1 335 ? -3.284  -8.577  -14.653 1.00 29.11  ? 334 PHE A CE2 1 
ATOM   2588 C CZ  . PHE A 1 335 ? -4.597  -8.253  -14.934 1.00 26.59  ? 334 PHE A CZ  1 
ATOM   2589 N N   . SER A 1 336 ? -3.046  -12.184 -8.765  1.00 29.66  ? 335 SER A N   1 
ATOM   2590 C CA  . SER A 1 336 ? -2.098  -12.636 -7.741  1.00 30.78  ? 335 SER A CA  1 
ATOM   2591 C C   . SER A 1 336 ? -2.745  -13.680 -6.841  1.00 30.42  ? 335 SER A C   1 
ATOM   2592 O O   . SER A 1 336 ? -3.047  -13.419 -5.669  1.00 33.49  ? 335 SER A O   1 
ATOM   2593 C CB  . SER A 1 336 ? -1.581  -11.457 -6.919  1.00 29.33  ? 335 SER A CB  1 
ATOM   2594 O OG  . SER A 1 336 ? -0.415  -11.863 -6.204  1.00 42.00  ? 335 SER A OG  1 
ATOM   2595 N N   . PRO A 1 337 ? -2.930  -14.901 -7.345  1.00 27.80  ? 336 PRO A N   1 
ATOM   2596 C CA  . PRO A 1 337 ? -3.696  -15.896 -6.581  1.00 28.93  ? 336 PRO A CA  1 
ATOM   2597 C C   . PRO A 1 337 ? -2.975  -16.295 -5.298  1.00 29.62  ? 336 PRO A C   1 
ATOM   2598 O O   . PRO A 1 337 ? -1.799  -16.667 -5.306  1.00 29.57  ? 336 PRO A O   1 
ATOM   2599 C CB  . PRO A 1 337 ? -3.828  -17.077 -7.556  1.00 29.19  ? 336 PRO A CB  1 
ATOM   2600 C CG  . PRO A 1 337 ? -3.452  -16.534 -8.895  1.00 30.36  ? 336 PRO A CG  1 
ATOM   2601 C CD  . PRO A 1 337 ? -2.460  -15.441 -8.627  1.00 28.25  ? 336 PRO A CD  1 
ATOM   2602 N N   . SER A 1 338 ? -3.689  -16.194 -4.188  1.00 31.45  ? 337 SER A N   1 
ATOM   2603 C CA  . SER A 1 338 ? -3.158  -16.665 -2.922  1.00 28.77  ? 337 SER A CA  1 
ATOM   2604 C C   . SER A 1 338 ? -2.969  -18.175 -2.973  1.00 29.14  ? 337 SER A C   1 
ATOM   2605 O O   . SER A 1 338 ? -3.552  -18.877 -3.812  1.00 28.78  ? 337 SER A O   1 
ATOM   2606 C CB  . SER A 1 338 ? -4.113  -16.323 -1.784  1.00 29.12  ? 337 SER A CB  1 
ATOM   2607 O OG  . SER A 1 338 ? -5.300  -17.102 -1.903  1.00 26.34  ? 337 SER A OG  1 
ATOM   2608 N N   . LEU A 1 339 ? -2.160  -18.683 -2.048  1.00 27.51  ? 338 LEU A N   1 
ATOM   2609 C CA  . LEU A 1 339 ? -2.027  -20.128 -1.957  1.00 28.04  ? 338 LEU A CA  1 
ATOM   2610 C C   . LEU A 1 339 ? -3.373  -20.773 -1.631  1.00 29.27  ? 338 LEU A C   1 
ATOM   2611 O O   . LEU A 1 339 ? -3.719  -21.826 -2.188  1.00 27.55  ? 338 LEU A O   1 
ATOM   2612 C CB  . LEU A 1 339 ? -0.950  -20.504 -0.932  1.00 29.44  ? 338 LEU A CB  1 
ATOM   2613 C CG  . LEU A 1 339 ? -0.726  -22.004 -0.749  1.00 30.23  ? 338 LEU A CG  1 
ATOM   2614 C CD1 . LEU A 1 339 ? -0.299  -22.688 -2.056  1.00 30.75  ? 338 LEU A CD1 1 
ATOM   2615 C CD2 . LEU A 1 339 ? 0.234   -22.280 0.399   1.00 31.63  ? 338 LEU A CD2 1 
ATOM   2616 N N   . LYS A 1 340 ? -4.176  -20.127 -0.775  1.00 30.02  ? 339 LYS A N   1 
ATOM   2617 C CA  . LYS A 1 340 ? -5.491  -20.681 -0.464  1.00 25.97  ? 339 LYS A CA  1 
ATOM   2618 C C   . LYS A 1 340 ? -6.337  -20.828 -1.723  1.00 27.29  ? 339 LYS A C   1 
ATOM   2619 O O   . LYS A 1 340 ? -7.014  -21.845 -1.910  1.00 29.14  ? 339 LYS A O   1 
ATOM   2620 C CB  . LYS A 1 340 ? -6.201  -19.817 0.572   1.00 28.05  ? 339 LYS A CB  1 
ATOM   2621 C CG  . LYS A 1 340 ? -7.603  -20.322 0.913   1.00 30.81  ? 339 LYS A CG  1 
ATOM   2622 C CD  . LYS A 1 340 ? -8.138  -19.695 2.183   1.00 32.16  ? 339 LYS A CD  1 
ATOM   2623 C CE  . LYS A 1 340 ? -8.508  -18.245 1.979   1.00 31.36  ? 339 LYS A CE  1 
ATOM   2624 N NZ  . LYS A 1 340 ? -9.415  -17.848 3.078   1.00 34.13  ? 339 LYS A NZ  1 
ATOM   2625 N N   . THR A 1 341 ? -6.289  -19.837 -2.614  1.00 26.79  ? 340 THR A N   1 
ATOM   2626 C CA  . THR A 1 341 ? -7.010  -19.950 -3.880  1.00 26.63  ? 340 THR A CA  1 
ATOM   2627 C C   . THR A 1 341 ? -6.476  -21.102 -4.735  1.00 29.27  ? 340 THR A C   1 
ATOM   2628 O O   . THR A 1 341 ? -7.257  -21.870 -5.315  1.00 28.98  ? 340 THR A O   1 
ATOM   2629 C CB  . THR A 1 341 ? -6.925  -18.624 -4.636  1.00 25.58  ? 340 THR A CB  1 
ATOM   2630 O OG1 . THR A 1 341 ? -7.726  -17.649 -3.963  1.00 30.20  ? 340 THR A OG1 1 
ATOM   2631 C CG2 . THR A 1 341 ? -7.425  -18.773 -6.056  1.00 24.96  ? 340 THR A CG2 1 
ATOM   2632 N N   . LEU A 1 342 ? -5.152  -21.247 -4.827  1.00 25.61  ? 341 LEU A N   1 
ATOM   2633 C CA  . LEU A 1 342 ? -4.628  -22.332 -5.642  1.00 26.57  ? 341 LEU A CA  1 
ATOM   2634 C C   . LEU A 1 342 ? -4.999  -23.678 -5.057  1.00 27.14  ? 341 LEU A C   1 
ATOM   2635 O O   . LEU A 1 342 ? -5.139  -24.655 -5.794  1.00 28.50  ? 341 LEU A O   1 
ATOM   2636 C CB  . LEU A 1 342 ? -3.109  -22.224 -5.778  1.00 27.72  ? 341 LEU A CB  1 
ATOM   2637 C CG  . LEU A 1 342 ? -2.582  -20.940 -6.403  1.00 27.54  ? 341 LEU A CG  1 
ATOM   2638 C CD1 . LEU A 1 342 ? -1.084  -20.975 -6.341  1.00 29.90  ? 341 LEU A CD1 1 
ATOM   2639 C CD2 . LEU A 1 342 ? -3.064  -20.816 -7.837  1.00 27.88  ? 341 LEU A CD2 1 
ATOM   2640 N N   . CYS A 1 343 ? -5.139  -23.753 -3.740  1.00 28.66  ? 342 CYS A N   1 
ATOM   2641 C CA  . CYS A 1 343 ? -5.465  -25.024 -3.119  1.00 27.77  ? 342 CYS A CA  1 
ATOM   2642 C C   . CYS A 1 343 ? -6.942  -25.364 -3.272  1.00 30.40  ? 342 CYS A C   1 
ATOM   2643 O O   . CYS A 1 343 ? -7.280  -26.531 -3.512  1.00 29.80  ? 342 CYS A O   1 
ATOM   2644 C CB  . CYS A 1 343 ? -5.054  -25.001 -1.653  1.00 28.40  ? 342 CYS A CB  1 
ATOM   2645 S SG  . CYS A 1 343 ? -3.257  -25.094 -1.450  1.00 31.89  ? 342 CYS A SG  1 
ATOM   2646 N N   . LYS A 1 344 ? -7.839  -24.374 -3.136  1.00 28.11  ? 343 LYS A N   1 
ATOM   2647 C CA  . LYS A 1 344 ? -9.244  -24.643 -3.431  1.00 30.04  ? 343 LYS A CA  1 
ATOM   2648 C C   . LYS A 1 344 ? -9.389  -25.164 -4.851  1.00 31.78  ? 343 LYS A C   1 
ATOM   2649 O O   . LYS A 1 344 ? -10.083 -26.161 -5.085  1.00 34.05  ? 343 LYS A O   1 
ATOM   2650 C CB  . LYS A 1 344 ? -10.111 -23.397 -3.229  1.00 26.39  ? 343 LYS A CB  1 
ATOM   2651 C CG  . LYS A 1 344 ? -10.178 -22.933 -1.806  1.00 28.45  ? 343 LYS A CG  1 
ATOM   2652 C CD  . LYS A 1 344 ? -11.117 -21.774 -1.612  1.00 25.94  ? 343 LYS A CD  1 
ATOM   2653 C CE  . LYS A 1 344 ? -10.610 -20.517 -2.252  1.00 26.35  ? 343 LYS A CE  1 
ATOM   2654 N NZ  . LYS A 1 344 ? -11.340 -19.333 -1.704  1.00 25.13  ? 343 LYS A NZ  1 
ATOM   2655 N N   . LEU A 1 345 ? -8.689  -24.539 -5.803  1.00 28.99  ? 344 LEU A N   1 
ATOM   2656 C CA  . LEU A 1 345 ? -8.761  -24.993 -7.186  1.00 29.95  ? 344 LEU A CA  1 
ATOM   2657 C C   . LEU A 1 345 ? -8.275  -26.426 -7.319  1.00 34.10  ? 344 LEU A C   1 
ATOM   2658 O O   . LEU A 1 345 ? -8.819  -27.201 -8.115  1.00 37.96  ? 344 LEU A O   1 
ATOM   2659 C CB  . LEU A 1 345 ? -7.948  -24.076 -8.079  1.00 29.93  ? 344 LEU A CB  1 
ATOM   2660 C CG  . LEU A 1 345 ? -8.530  -22.694 -8.287  1.00 31.38  ? 344 LEU A CG  1 
ATOM   2661 C CD1 . LEU A 1 345 ? -7.472  -21.809 -8.971  1.00 29.64  ? 344 LEU A CD1 1 
ATOM   2662 C CD2 . LEU A 1 345 ? -9.789  -22.797 -9.125  1.00 27.93  ? 344 LEU A CD2 1 
ATOM   2663 N N   . ALA A 1 346 ? -7.248  -26.796 -6.558  1.00 32.54  ? 345 ALA A N   1 
ATOM   2664 C CA  . ALA A 1 346 ? -6.772  -28.174 -6.596  1.00 32.90  ? 345 ALA A CA  1 
ATOM   2665 C C   . ALA A 1 346 ? -7.802  -29.113 -5.987  1.00 36.31  ? 345 ALA A C   1 
ATOM   2666 O O   . ALA A 1 346 ? -8.115  -30.164 -6.560  1.00 39.11  ? 345 ALA A O   1 
ATOM   2667 C CB  . ALA A 1 346 ? -5.431  -28.294 -5.871  1.00 30.90  ? 345 ALA A CB  1 
ATOM   2668 N N   . VAL A 1 347 ? -8.362  -28.738 -4.832  1.00 34.44  ? 346 VAL A N   1 
ATOM   2669 C CA  . VAL A 1 347 ? -9.350  -29.590 -4.178  1.00 35.53  ? 346 VAL A CA  1 
ATOM   2670 C C   . VAL A 1 347 ? -10.547 -29.810 -5.099  1.00 37.25  ? 346 VAL A C   1 
ATOM   2671 O O   . VAL A 1 347 ? -11.102 -30.913 -5.171  1.00 36.67  ? 346 VAL A O   1 
ATOM   2672 C CB  . VAL A 1 347 ? -9.765  -28.987 -2.820  1.00 32.73  ? 346 VAL A CB  1 
ATOM   2673 C CG1 . VAL A 1 347 ? -10.935 -29.737 -2.239  1.00 32.96  ? 346 VAL A CG1 1 
ATOM   2674 C CG2 . VAL A 1 347 ? -8.607  -29.032 -1.844  1.00 33.03  ? 346 VAL A CG2 1 
ATOM   2675 N N   . ILE A 1 348 ? -10.952 -28.769 -5.829  1.00 34.29  ? 347 ILE A N   1 
ATOM   2676 C CA  . ILE A 1 348 ? -12.050 -28.918 -6.774  1.00 36.43  ? 347 ILE A CA  1 
ATOM   2677 C C   . ILE A 1 348 ? -11.629 -29.799 -7.939  1.00 39.32  ? 347 ILE A C   1 
ATOM   2678 O O   . ILE A 1 348 ? -12.335 -30.748 -8.314  1.00 39.57  ? 347 ILE A O   1 
ATOM   2679 C CB  . ILE A 1 348 ? -12.531 -27.543 -7.261  1.00 35.19  ? 347 ILE A CB  1 
ATOM   2680 C CG1 . ILE A 1 348 ? -13.194 -26.772 -6.124  1.00 27.33  ? 347 ILE A CG1 1 
ATOM   2681 C CG2 . ILE A 1 348 ? -13.463 -27.714 -8.449  1.00 32.00  ? 347 ILE A CG2 1 
ATOM   2682 C CD1 . ILE A 1 348 ? -13.064 -25.277 -6.275  1.00 26.20  ? 347 ILE A CD1 1 
ATOM   2683 N N   . GLN A 1 349 ? -10.459 -29.508 -8.513  1.00 39.69  ? 348 GLN A N   1 
ATOM   2684 C CA  . GLN A 1 349 ? -10.007 -30.211 -9.713  1.00 39.81  ? 348 GLN A CA  1 
ATOM   2685 C C   . GLN A 1 349 ? -9.828  -31.705 -9.462  1.00 37.68  ? 348 GLN A C   1 
ATOM   2686 O O   . GLN A 1 349 ? -10.292 -32.533 -10.253 1.00 37.78  ? 348 GLN A O   1 
ATOM   2687 C CB  . GLN A 1 349 ? -8.710  -29.586 -10.214 1.00 40.05  ? 348 GLN A CB  1 
ATOM   2688 C CG  . GLN A 1 349 ? -8.055  -30.314 -11.363 1.00 43.84  ? 348 GLN A CG  1 
ATOM   2689 C CD  . GLN A 1 349 ? -6.608  -29.899 -11.515 1.00 50.01  ? 348 GLN A CD  1 
ATOM   2690 O OE1 . GLN A 1 349 ? -6.129  -29.004 -10.809 1.00 50.77  ? 348 GLN A OE1 1 
ATOM   2691 N NE2 . GLN A 1 349 ? -5.897  -30.550 -12.427 1.00 51.46  ? 348 GLN A NE2 1 
ATOM   2692 N N   . TYR A 1 350 ? -9.164  -32.073 -8.364  1.00 38.79  ? 349 TYR A N   1 
ATOM   2693 C CA  . TYR A 1 350 ? -8.965  -33.485 -8.047  1.00 38.33  ? 349 TYR A CA  1 
ATOM   2694 C C   . TYR A 1 350 ? -10.203 -34.119 -7.435  1.00 39.57  ? 349 TYR A C   1 
ATOM   2695 O O   . TYR A 1 350 ? -10.182 -35.317 -7.125  1.00 40.58  ? 349 TYR A O   1 
ATOM   2696 C CB  . TYR A 1 350 ? -7.778  -33.668 -7.098  1.00 39.16  ? 349 TYR A CB  1 
ATOM   2697 C CG  . TYR A 1 350 ? -6.470  -33.111 -7.621  1.00 43.63  ? 349 TYR A CG  1 
ATOM   2698 C CD1 . TYR A 1 350 ? -6.020  -33.408 -8.912  1.00 43.63  ? 349 TYR A CD1 1 
ATOM   2699 C CD2 . TYR A 1 350 ? -5.685  -32.270 -6.823  1.00 41.68  ? 349 TYR A CD2 1 
ATOM   2700 C CE1 . TYR A 1 350 ? -4.815  -32.884 -9.392  1.00 46.13  ? 349 TYR A CE1 1 
ATOM   2701 C CE2 . TYR A 1 350 ? -4.483  -31.745 -7.290  1.00 41.22  ? 349 TYR A CE2 1 
ATOM   2702 C CZ  . TYR A 1 350 ? -4.052  -32.050 -8.570  1.00 47.36  ? 349 TYR A CZ  1 
ATOM   2703 O OH  . TYR A 1 350 ? -2.857  -31.515 -9.018  1.00 49.75  ? 349 TYR A OH  1 
ATOM   2704 N N   . ASN A 1 351 ? -11.259 -33.332 -7.240  1.00 47.82  ? 350 ASN A N   1 
ATOM   2705 C CA  . ASN A 1 351 ? -12.546 -33.812 -6.732  1.00 47.61  ? 350 ASN A CA  1 
ATOM   2706 C C   . ASN A 1 351 ? -12.409 -34.469 -5.358  1.00 43.59  ? 350 ASN A C   1 
ATOM   2707 O O   . ASN A 1 351 ? -13.085 -35.449 -5.049  1.00 43.41  ? 350 ASN A O   1 
ATOM   2708 C CB  . ASN A 1 351 ? -13.206 -34.761 -7.738  1.00 47.77  ? 350 ASN A CB  1 
ATOM   2709 C CG  . ASN A 1 351 ? -14.719 -34.717 -7.672  1.00 58.28  ? 350 ASN A CG  1 
ATOM   2710 O OD1 . ASN A 1 351 ? -15.372 -35.755 -7.547  1.00 61.93  ? 350 ASN A OD1 1 
ATOM   2711 N ND2 . ASN A 1 351 ? -15.289 -33.505 -7.735  1.00 61.03  ? 350 ASN A ND2 1 
ATOM   2712 N N   . LEU A 1 352 ? -11.552 -33.909 -4.509  1.00 39.50  ? 351 LEU A N   1 
ATOM   2713 C CA  . LEU A 1 352 ? -11.318 -34.495 -3.199  1.00 38.52  ? 351 LEU A CA  1 
ATOM   2714 C C   . LEU A 1 352 ? -12.499 -34.259 -2.255  1.00 38.75  ? 351 LEU A C   1 
ATOM   2715 O O   . LEU A 1 352 ? -13.269 -33.307 -2.401  1.00 36.12  ? 351 LEU A O   1 
ATOM   2716 C CB  . LEU A 1 352 ? -10.043 -33.920 -2.596  1.00 40.71  ? 351 LEU A CB  1 
ATOM   2717 C CG  . LEU A 1 352 ? -8.813  -34.077 -3.493  1.00 41.20  ? 351 LEU A CG  1 
ATOM   2718 C CD1 . LEU A 1 352 ? -7.714  -33.157 -3.029  1.00 36.14  ? 351 LEU A CD1 1 
ATOM   2719 C CD2 . LEU A 1 352 ? -8.343  -35.518 -3.472  1.00 38.08  ? 351 LEU A CD2 1 
ATOM   2720 N N   . ASP A 1 353 ? -12.632 -35.152 -1.277  1.00 37.16  ? 352 ASP A N   1 
ATOM   2721 C CA  . ASP A 1 353 ? -13.625 -35.005 -0.223  1.00 36.89  ? 352 ASP A CA  1 
ATOM   2722 C C   . ASP A 1 353 ? -13.371 -33.728 0.561   1.00 37.54  ? 352 ASP A C   1 
ATOM   2723 O O   . ASP A 1 353 ? -12.260 -33.505 1.046   1.00 40.06  ? 352 ASP A O   1 
ATOM   2724 C CB  . ASP A 1 353 ? -13.550 -36.222 0.700   1.00 38.61  ? 352 ASP A CB  1 
ATOM   2725 C CG  . ASP A 1 353 ? -14.668 -36.277 1.720   1.00 44.44  ? 352 ASP A CG  1 
ATOM   2726 O OD1 . ASP A 1 353 ? -15.403 -35.282 1.888   1.00 43.63  ? 352 ASP A OD1 1 
ATOM   2727 O OD2 . ASP A 1 353 ? -14.801 -37.339 2.363   1.00 50.58  ? 352 ASP A OD2 1 
ATOM   2728 N N   . GLN A 1 354 ? -14.409 -32.901 0.710   1.00 36.85  ? 353 GLN A N   1 
ATOM   2729 C CA  . GLN A 1 354 ? -14.286 -31.625 1.401   1.00 35.73  ? 353 GLN A CA  1 
ATOM   2730 C C   . GLN A 1 354 ? -14.781 -31.652 2.837   1.00 37.70  ? 353 GLN A C   1 
ATOM   2731 O O   . GLN A 1 354 ? -14.680 -30.633 3.523   1.00 40.45  ? 353 GLN A O   1 
ATOM   2732 C CB  . GLN A 1 354 ? -15.048 -30.535 0.648   1.00 34.18  ? 353 GLN A CB  1 
ATOM   2733 C CG  . GLN A 1 354 ? -14.555 -30.298 -0.750  1.00 35.50  ? 353 GLN A CG  1 
ATOM   2734 C CD  . GLN A 1 354 ? -15.433 -29.333 -1.490  1.00 35.24  ? 353 GLN A CD  1 
ATOM   2735 O OE1 . GLN A 1 354 ? -16.204 -28.587 -0.881  1.00 35.49  ? 353 GLN A OE1 1 
ATOM   2736 N NE2 . GLN A 1 354 ? -15.338 -29.343 -2.812  1.00 35.67  ? 353 GLN A NE2 1 
ATOM   2737 N N   . SER A 1 355 ? -15.310 -32.775 3.314   1.00 40.71  ? 354 SER A N   1 
ATOM   2738 C CA  . SER A 1 355 ? -15.967 -32.784 4.620   1.00 42.15  ? 354 SER A CA  1 
ATOM   2739 C C   . SER A 1 355 ? -14.988 -32.753 5.794   1.00 46.31  ? 354 SER A C   1 
ATOM   2740 O O   . SER A 1 355 ? -15.438 -32.598 6.935   1.00 47.10  ? 354 SER A O   1 
ATOM   2741 C CB  . SER A 1 355 ? -16.871 -34.008 4.738   1.00 42.18  ? 354 SER A CB  1 
ATOM   2742 O OG  . SER A 1 355 ? -16.117 -35.199 4.561   1.00 44.03  ? 354 SER A OG  1 
ATOM   2743 N N   . CYS A 1 356 ? -13.678 -32.925 5.553   1.00 44.27  ? 355 CYS A N   1 
ATOM   2744 C CA  . CYS A 1 356 ? -12.676 -32.727 6.596   1.00 45.20  ? 355 CYS A CA  1 
ATOM   2745 C C   . CYS A 1 356 ? -12.384 -31.254 6.845   1.00 43.87  ? 355 CYS A C   1 
ATOM   2746 O O   . CYS A 1 356 ? -11.820 -30.909 7.891   1.00 44.19  ? 355 CYS A O   1 
ATOM   2747 C CB  . CYS A 1 356 ? -11.352 -33.418 6.222   1.00 55.91  ? 355 CYS A CB  1 
ATOM   2748 S SG  . CYS A 1 356 ? -10.140 -32.402 5.149   1.00 60.94  ? 355 CYS A SG  1 
ATOM   2749 N N   . LEU A 1 357 ? -12.708 -30.393 5.897   1.00 41.48  ? 356 LEU A N   1 
ATOM   2750 C CA  . LEU A 1 357 ? -12.195 -29.041 5.943   1.00 38.22  ? 356 LEU A CA  1 
ATOM   2751 C C   . LEU A 1 357 ? -12.997 -28.197 6.931   1.00 37.96  ? 356 LEU A C   1 
ATOM   2752 O O   . LEU A 1 357 ? -14.162 -28.492 7.205   1.00 38.57  ? 356 LEU A O   1 
ATOM   2753 C CB  . LEU A 1 357 ? -12.237 -28.427 4.552   1.00 33.87  ? 356 LEU A CB  1 
ATOM   2754 C CG  . LEU A 1 357 ? -11.366 -29.161 3.538   1.00 35.81  ? 356 LEU A CG  1 
ATOM   2755 C CD1 . LEU A 1 357 ? -11.674 -28.668 2.150   1.00 30.98  ? 356 LEU A CD1 1 
ATOM   2756 C CD2 . LEU A 1 357 ? -9.876  -28.978 3.847   1.00 32.39  ? 356 LEU A CD2 1 
ATOM   2757 N N   . PRO A 1 358 ? -12.381 -27.166 7.510   1.00 38.98  ? 357 PRO A N   1 
ATOM   2758 C CA  . PRO A 1 358 ? -13.133 -26.260 8.388   1.00 38.01  ? 357 PRO A CA  1 
ATOM   2759 C C   . PRO A 1 358 ? -14.213 -25.505 7.618   1.00 37.72  ? 357 PRO A C   1 
ATOM   2760 O O   . PRO A 1 358 ? -14.108 -25.281 6.411   1.00 35.33  ? 357 PRO A O   1 
ATOM   2761 C CB  . PRO A 1 358 ? -12.051 -25.314 8.926   1.00 35.36  ? 357 PRO A CB  1 
ATOM   2762 C CG  . PRO A 1 358 ? -10.961 -25.384 7.932   1.00 31.28  ? 357 PRO A CG  1 
ATOM   2763 C CD  . PRO A 1 358 ? -10.957 -26.798 7.432   1.00 31.67  ? 357 PRO A CD  1 
ATOM   2764 N N   . HIS A 1 359 ? -15.272 -25.113 8.331   1.00 39.86  ? 358 HIS A N   1 
ATOM   2765 C CA  . HIS A 1 359 ? -16.453 -24.571 7.660   1.00 34.76  ? 358 HIS A CA  1 
ATOM   2766 C C   . HIS A 1 359 ? -16.192 -23.263 6.936   1.00 34.69  ? 358 HIS A C   1 
ATOM   2767 O O   . HIS A 1 359 ? -16.905 -22.957 5.974   1.00 36.52  ? 358 HIS A O   1 
ATOM   2768 C CB  . HIS A 1 359 ? -17.588 -24.383 8.654   1.00 37.88  ? 358 HIS A CB  1 
ATOM   2769 C CG  . HIS A 1 359 ? -18.202 -25.673 9.084   1.00 43.13  ? 358 HIS A CG  1 
ATOM   2770 N ND1 . HIS A 1 359 ? -17.948 -26.248 10.312  1.00 47.65  ? 358 HIS A ND1 1 
ATOM   2771 C CD2 . HIS A 1 359 ? -19.022 -26.528 8.429   1.00 42.37  ? 358 HIS A CD2 1 
ATOM   2772 C CE1 . HIS A 1 359 ? -18.607 -27.388 10.407  1.00 47.33  ? 358 HIS A CE1 1 
ATOM   2773 N NE2 . HIS A 1 359 ? -19.263 -27.583 9.277   1.00 48.10  ? 358 HIS A NE2 1 
ATOM   2774 N N   . ASP A 1 360 ? -15.198 -22.479 7.361   1.00 37.52  ? 359 ASP A N   1 
ATOM   2775 C CA  . ASP A 1 360 ? -14.896 -21.251 6.631   1.00 33.66  ? 359 ASP A CA  1 
ATOM   2776 C C   . ASP A 1 360 ? -14.359 -21.554 5.232   1.00 33.75  ? 359 ASP A C   1 
ATOM   2777 O O   . ASP A 1 360 ? -14.765 -20.906 4.258   1.00 35.63  ? 359 ASP A O   1 
ATOM   2778 C CB  . ASP A 1 360 ? -13.925 -20.373 7.435   1.00 35.60  ? 359 ASP A CB  1 
ATOM   2779 C CG  . ASP A 1 360 ? -12.643 -21.114 7.874   1.00 37.50  ? 359 ASP A CG  1 
ATOM   2780 O OD1 . ASP A 1 360 ? -12.498 -22.337 7.647   1.00 37.27  ? 359 ASP A OD1 1 
ATOM   2781 O OD2 . ASP A 1 360 ? -11.769 -20.449 8.458   1.00 35.98  ? 359 ASP A OD2 1 
ATOM   2782 N N   . ILE A 1 361 ? -13.456 -22.536 5.112   1.00 30.96  ? 360 ILE A N   1 
ATOM   2783 C CA  . ILE A 1 361 ? -12.963 -22.959 3.801   1.00 31.42  ? 360 ILE A CA  1 
ATOM   2784 C C   . ILE A 1 361 ? -14.100 -23.552 2.974   1.00 31.67  ? 360 ILE A C   1 
ATOM   2785 O O   . ILE A 1 361 ? -14.216 -23.286 1.771   1.00 30.48  ? 360 ILE A O   1 
ATOM   2786 C CB  . ILE A 1 361 ? -11.798 -23.967 3.954   1.00 31.21  ? 360 ILE A CB  1 
ATOM   2787 C CG1 . ILE A 1 361 ? -10.544 -23.303 4.501   1.00 38.77  ? 360 ILE A CG1 1 
ATOM   2788 C CG2 . ILE A 1 361 ? -11.397 -24.567 2.636   1.00 27.12  ? 360 ILE A CG2 1 
ATOM   2789 C CD1 . ILE A 1 361 ? -9.361  -24.285 4.633   1.00 37.60  ? 360 ILE A CD1 1 
ATOM   2790 N N   . ARG A 1 362 ? -14.939 -24.384 3.595   1.00 30.05  ? 361 ARG A N   1 
ATOM   2791 C CA  . ARG A 1 362 ? -16.028 -25.012 2.855   1.00 32.58  ? 361 ARG A CA  1 
ATOM   2792 C C   . ARG A 1 362 ? -16.989 -23.971 2.307   1.00 29.64  ? 361 ARG A C   1 
ATOM   2793 O O   . ARG A 1 362 ? -17.462 -24.093 1.172   1.00 27.61  ? 361 ARG A O   1 
ATOM   2794 C CB  . ARG A 1 362 ? -16.769 -26.017 3.735   1.00 36.00  ? 361 ARG A CB  1 
ATOM   2795 C CG  . ARG A 1 362 ? -15.863 -27.114 4.295   1.00 36.59  ? 361 ARG A CG  1 
ATOM   2796 C CD  . ARG A 1 362 ? -16.666 -28.166 4.980   1.00 34.27  ? 361 ARG A CD  1 
ATOM   2797 N NE  . ARG A 1 362 ? -17.545 -28.822 4.026   1.00 34.91  ? 361 ARG A NE  1 
ATOM   2798 C CZ  . ARG A 1 362 ? -18.444 -29.735 4.360   1.00 39.43  ? 361 ARG A CZ  1 
ATOM   2799 N NH1 . ARG A 1 362 ? -18.650 -30.070 5.620   1.00 38.84  ? 361 ARG A NH1 1 
ATOM   2800 N NH2 . ARG A 1 362 ? -19.144 -30.334 3.404   1.00 41.90  ? 361 ARG A NH2 1 
ATOM   2801 N N   . TRP A 1 363 ? -17.284 -22.932 3.090   1.00 30.74  ? 362 TRP A N   1 
ATOM   2802 C CA  . TRP A 1 363 ? -18.114 -21.848 2.570   1.00 31.66  ? 362 TRP A CA  1 
ATOM   2803 C C   . TRP A 1 363 ? -17.508 -21.263 1.302   1.00 32.55  ? 362 TRP A C   1 
ATOM   2804 O O   . TRP A 1 363 ? -18.221 -21.035 0.320   1.00 34.14  ? 362 TRP A O   1 
ATOM   2805 C CB  . TRP A 1 363 ? -18.299 -20.757 3.629   1.00 32.73  ? 362 TRP A CB  1 
ATOM   2806 C CG  . TRP A 1 363 ? -19.169 -19.600 3.179   1.00 35.07  ? 362 TRP A CG  1 
ATOM   2807 C CD1 . TRP A 1 363 ? -20.510 -19.452 3.399   1.00 32.65  ? 362 TRP A CD1 1 
ATOM   2808 C CD2 . TRP A 1 363 ? -18.751 -18.429 2.437   1.00 36.27  ? 362 TRP A CD2 1 
ATOM   2809 N NE1 . TRP A 1 363 ? -20.953 -18.270 2.843   1.00 38.54  ? 362 TRP A NE1 1 
ATOM   2810 C CE2 . TRP A 1 363 ? -19.899 -17.624 2.247   1.00 34.12  ? 362 TRP A CE2 1 
ATOM   2811 C CE3 . TRP A 1 363 ? -17.518 -17.987 1.917   1.00 35.15  ? 362 TRP A CE3 1 
ATOM   2812 C CZ2 . TRP A 1 363 ? -19.857 -16.400 1.564   1.00 33.21  ? 362 TRP A CZ2 1 
ATOM   2813 C CZ3 . TRP A 1 363 ? -17.478 -16.762 1.233   1.00 33.74  ? 362 TRP A CZ3 1 
ATOM   2814 C CH2 . TRP A 1 363 ? -18.646 -15.987 1.065   1.00 34.61  ? 362 TRP A CH2 1 
ATOM   2815 N N   . GLU A 1 364 ? -16.186 -21.036 1.303   1.00 30.17  ? 363 GLU A N   1 
ATOM   2816 C CA  . GLU A 1 364 ? -15.497 -20.510 0.129   1.00 28.96  ? 363 GLU A CA  1 
ATOM   2817 C C   . GLU A 1 364 ? -15.587 -21.477 -1.045  1.00 30.48  ? 363 GLU A C   1 
ATOM   2818 O O   . GLU A 1 364 ? -15.957 -21.086 -2.160  1.00 32.45  ? 363 GLU A O   1 
ATOM   2819 C CB  . GLU A 1 364 ? -14.026 -20.219 0.469   1.00 30.94  ? 363 GLU A CB  1 
ATOM   2820 C CG  . GLU A 1 364 ? -13.824 -19.145 1.537   1.00 31.47  ? 363 GLU A CG  1 
ATOM   2821 C CD  . GLU A 1 364 ? -12.357 -18.764 1.764   1.00 35.16  ? 363 GLU A CD  1 
ATOM   2822 O OE1 . GLU A 1 364 ? -11.541 -18.934 0.828   1.00 30.28  ? 363 GLU A OE1 1 
ATOM   2823 O OE2 . GLU A 1 364 ? -12.026 -18.276 2.884   1.00 37.49  ? 363 GLU A OE2 1 
ATOM   2824 N N   . LEU A 1 365 ? -15.238 -22.749 -0.817  1.00 29.13  ? 364 LEU A N   1 
ATOM   2825 C CA  . LEU A 1 365 ? -15.350 -23.739 -1.879  1.00 28.75  ? 364 LEU A CA  1 
ATOM   2826 C C   . LEU A 1 365 ? -16.746 -23.737 -2.473  1.00 30.45  ? 364 LEU A C   1 
ATOM   2827 O O   . LEU A 1 365 ? -16.917 -23.788 -3.696  1.00 28.57  ? 364 LEU A O   1 
ATOM   2828 C CB  . LEU A 1 365 ? -15.015 -25.125 -1.347  1.00 29.89  ? 364 LEU A CB  1 
ATOM   2829 C CG  . LEU A 1 365 ? -13.533 -25.397 -1.146  1.00 29.82  ? 364 LEU A CG  1 
ATOM   2830 C CD1 . LEU A 1 365 ? -13.388 -26.550 -0.195  1.00 27.57  ? 364 LEU A CD1 1 
ATOM   2831 C CD2 . LEU A 1 365 ? -12.878 -25.702 -2.487  1.00 28.85  ? 364 LEU A CD2 1 
ATOM   2832 N N   . ASN A 1 366 ? -17.760 -23.668 -1.615  1.00 31.28  ? 365 ASN A N   1 
ATOM   2833 C CA  . ASN A 1 366 ? -19.127 -23.649 -2.101  1.00 30.95  ? 365 ASN A CA  1 
ATOM   2834 C C   . ASN A 1 366 ? -19.403 -22.405 -2.933  1.00 30.80  ? 365 ASN A C   1 
ATOM   2835 O O   . ASN A 1 366 ? -20.018 -22.487 -4.002  1.00 27.82  ? 365 ASN A O   1 
ATOM   2836 C CB  . ASN A 1 366 ? -20.099 -23.707 -0.934  1.00 30.56  ? 365 ASN A CB  1 
ATOM   2837 C CG  . ASN A 1 366 ? -21.524 -23.468 -1.385  1.00 35.81  ? 365 ASN A CG  1 
ATOM   2838 O OD1 . ASN A 1 366 ? -22.030 -22.339 -1.340  1.00 34.85  ? 365 ASN A OD1 1 
ATOM   2839 N ND2 . ASN A 1 366 ? -22.167 -24.528 -1.878  1.00 37.19  ? 365 ASN A ND2 1 
ATOM   2840 N N   . ALA A 1 367 ? -18.964 -21.244 -2.446  1.00 29.88  ? 366 ALA A N   1 
ATOM   2841 C CA  . ALA A 1 367 ? -19.221 -19.996 -3.150  1.00 30.63  ? 366 ALA A CA  1 
ATOM   2842 C C   . ALA A 1 367 ? -18.731 -20.074 -4.584  1.00 30.04  ? 366 ALA A C   1 
ATOM   2843 O O   . ALA A 1 367 ? -19.465 -19.738 -5.517  1.00 33.08  ? 366 ALA A O   1 
ATOM   2844 C CB  . ALA A 1 367 ? -18.555 -18.828 -2.420  1.00 28.87  ? 366 ALA A CB  1 
ATOM   2845 N N   . MET A 1 368 ? -17.500 -20.542 -4.788  1.00 32.28  ? 367 MET A N   1 
ATOM   2846 C CA  . MET A 1 368 ? -16.949 -20.528 -6.137  1.00 30.09  ? 367 MET A CA  1 
ATOM   2847 C C   . MET A 1 368 ? -17.459 -21.675 -7.002  1.00 28.87  ? 367 MET A C   1 
ATOM   2848 O O   . MET A 1 368 ? -17.046 -21.779 -8.165  1.00 28.17  ? 367 MET A O   1 
ATOM   2849 C CB  . MET A 1 368 ? -15.417 -20.527 -6.084  1.00 27.12  ? 367 MET A CB  1 
ATOM   2850 C CG  . MET A 1 368 ? -14.814 -21.784 -5.537  1.00 30.61  ? 367 MET A CG  1 
ATOM   2851 S SD  . MET A 1 368 ? -13.166 -21.544 -4.808  1.00 32.70  ? 367 MET A SD  1 
ATOM   2852 C CE  . MET A 1 368 ? -12.176 -21.339 -6.339  1.00 29.65  ? 367 MET A CE  1 
ATOM   2853 N N   . THR A 1 369 ? -18.359 -22.521 -6.488  1.00 27.58  ? 368 THR A N   1 
ATOM   2854 C CA  . THR A 1 369 ? -18.848 -23.656 -7.262  1.00 30.04  ? 368 THR A CA  1 
ATOM   2855 C C   . THR A 1 369 ? -20.368 -23.714 -7.365  1.00 31.80  ? 368 THR A C   1 
ATOM   2856 O O   . THR A 1 369 ? -20.898 -24.761 -7.754  1.00 31.03  ? 368 THR A O   1 
ATOM   2857 C CB  . THR A 1 369 ? -18.332 -24.987 -6.680  1.00 32.82  ? 368 THR A CB  1 
ATOM   2858 O OG1 . THR A 1 369 ? -18.835 -25.167 -5.348  1.00 34.31  ? 368 THR A OG1 1 
ATOM   2859 C CG2 . THR A 1 369 ? -16.798 -25.025 -6.661  1.00 27.96  ? 368 THR A CG2 1 
ATOM   2860 N N   . THR A 1 370 ? -21.084 -22.633 -7.038  1.00 29.14  ? 369 THR A N   1 
ATOM   2861 C CA  . THR A 1 370 ? -22.545 -22.643 -7.009  1.00 33.56  ? 369 THR A CA  1 
ATOM   2862 C C   . THR A 1 370 ? -23.075 -21.545 -7.923  1.00 34.38  ? 369 THR A C   1 
ATOM   2863 O O   . THR A 1 370 ? -22.724 -20.372 -7.754  1.00 29.77  ? 369 THR A O   1 
ATOM   2864 C CB  . THR A 1 370 ? -23.083 -22.452 -5.586  1.00 33.42  ? 369 THR A CB  1 
ATOM   2865 O OG1 . THR A 1 370 ? -22.352 -23.270 -4.670  1.00 34.59  ? 369 THR A OG1 1 
ATOM   2866 C CG2 . THR A 1 370 ? -24.537 -22.849 -5.513  1.00 30.20  ? 369 THR A CG2 1 
ATOM   2867 N N   . ASN A 1 371 ? -23.925 -21.929 -8.878  1.00 32.20  ? 370 ASN A N   1 
ATOM   2868 C CA  . ASN A 1 371 ? -24.509 -20.972 -9.809  1.00 30.69  ? 370 ASN A CA  1 
ATOM   2869 C C   . ASN A 1 371 ? -25.495 -20.052 -9.096  1.00 34.49  ? 370 ASN A C   1 
ATOM   2870 O O   . ASN A 1 371 ? -26.088 -20.409 -8.074  1.00 33.96  ? 370 ASN A O   1 
ATOM   2871 C CB  . ASN A 1 371 ? -25.241 -21.695 -10.933 1.00 33.67  ? 370 ASN A CB  1 
ATOM   2872 C CG  . ASN A 1 371 ? -24.301 -22.326 -11.925 1.00 35.35  ? 370 ASN A CG  1 
ATOM   2873 O OD1 . ASN A 1 371 ? -23.107 -22.061 -11.898 1.00 32.78  ? 370 ASN A OD1 1 
ATOM   2874 N ND2 . ASN A 1 371 ? -24.837 -23.161 -12.820 1.00 31.87  ? 370 ASN A ND2 1 
ATOM   2875 N N   . SER A 1 372 ? -25.681 -18.859 -9.654  1.00 32.65  ? 371 SER A N   1 
ATOM   2876 C CA  . SER A 1 372 ? -26.776 -18.003 -9.225  1.00 34.49  ? 371 SER A CA  1 
ATOM   2877 C C   . SER A 1 372 ? -28.054 -18.417 -9.963  1.00 35.12  ? 371 SER A C   1 
ATOM   2878 O O   . SER A 1 372 ? -28.047 -19.323 -10.801 1.00 31.34  ? 371 SER A O   1 
ATOM   2879 C CB  . SER A 1 372 ? -26.433 -16.531 -9.460  1.00 33.42  ? 371 SER A CB  1 
ATOM   2880 O OG  . SER A 1 372 ? -25.281 -16.139 -8.711  1.00 28.40  ? 371 SER A OG  1 
ATOM   2881 N N   . ASN A 1 373 ? -29.172 -17.774 -9.622  1.00 35.85  ? 372 ASN A N   1 
ATOM   2882 C CA  . ASN A 1 373 ? -30.453 -18.129 -10.223 1.00 37.16  ? 372 ASN A CA  1 
ATOM   2883 C C   . ASN A 1 373 ? -31.137 -16.935 -10.883 1.00 35.29  ? 372 ASN A C   1 
ATOM   2884 O O   . ASN A 1 373 ? -32.364 -16.843 -10.889 1.00 41.47  ? 372 ASN A O   1 
ATOM   2885 C CB  . ASN A 1 373 ? -31.393 -18.782 -9.207  1.00 41.77  ? 372 ASN A CB  1 
ATOM   2886 C CG  . ASN A 1 373 ? -32.504 -19.644 -9.894  1.00 54.59  ? 372 ASN A CG  1 
ATOM   2887 O OD1 . ASN A 1 373 ? -32.299 -20.195 -10.991 1.00 53.85  ? 372 ASN A OD1 1 
ATOM   2888 N ND2 . ASN A 1 373 ? -33.675 -19.745 -9.251  1.00 51.19  ? 372 ASN A ND2 1 
ATOM   2889 N N   . ILE A 1 374 ? -30.359 -16.018 -11.451 1.00 37.14  ? 373 ILE A N   1 
ATOM   2890 C CA  . ILE A 1 374 ? -30.927 -15.014 -12.347 1.00 36.60  ? 373 ILE A CA  1 
ATOM   2891 C C   . ILE A 1 374 ? -31.464 -15.677 -13.607 1.00 33.37  ? 373 ILE A C   1 
ATOM   2892 O O   . ILE A 1 374 ? -32.539 -15.330 -14.096 1.00 36.65  ? 373 ILE A O   1 
ATOM   2893 C CB  . ILE A 1 374 ? -29.872 -13.941 -12.694 1.00 36.15  ? 373 ILE A CB  1 
ATOM   2894 C CG1 . ILE A 1 374 ? -29.303 -13.323 -11.416 1.00 33.15  ? 373 ILE A CG1 1 
ATOM   2895 C CG2 . ILE A 1 374 ? -30.480 -12.872 -13.609 1.00 30.53  ? 373 ILE A CG2 1 
ATOM   2896 C CD1 . ILE A 1 374 ? -30.411 -12.822 -10.434 1.00 34.01  ? 373 ILE A CD1 1 
ATOM   2897 N N   . SER A 1 375 ? -30.726 -16.638 -14.154 1.00 37.04  ? 374 SER A N   1 
ATOM   2898 C CA  . SER A 1 375 ? -31.075 -17.265 -15.418 1.00 39.79  ? 374 SER A CA  1 
ATOM   2899 C C   . SER A 1 375 ? -30.932 -18.776 -15.319 1.00 44.40  ? 374 SER A C   1 
ATOM   2900 O O   . SER A 1 375 ? -30.246 -19.307 -14.442 1.00 43.64  ? 374 SER A O   1 
ATOM   2901 C CB  . SER A 1 375 ? -30.203 -16.748 -16.568 1.00 40.94  ? 374 SER A CB  1 
ATOM   2902 O OG  . SER A 1 375 ? -28.816 -16.893 -16.272 1.00 38.67  ? 374 SER A OG  1 
ATOM   2903 N N   . ARG A 1 376 ? -31.619 -19.453 -16.226 1.00 49.68  ? 375 ARG A N   1 
ATOM   2904 C CA  . ARG A 1 376 ? -31.562 -20.883 -16.461 1.00 51.76  ? 375 ARG A CA  1 
ATOM   2905 C C   . ARG A 1 376 ? -30.982 -21.106 -17.854 1.00 55.55  ? 375 ARG A C   1 
ATOM   2906 O O   . ARG A 1 376 ? -31.007 -20.199 -18.696 1.00 54.91  ? 375 ARG A O   1 
ATOM   2907 C CB  . ARG A 1 376 ? -32.965 -21.507 -16.355 1.00 54.42  ? 375 ARG A CB  1 
ATOM   2908 C CG  . ARG A 1 376 ? -33.611 -21.432 -14.961 1.00 55.43  ? 375 ARG A CG  1 
ATOM   2909 C CD  . ARG A 1 376 ? -35.054 -20.864 -14.990 1.00 65.66  ? 375 ARG A CD  1 
ATOM   2910 N NE  . ARG A 1 376 ? -35.119 -19.400 -14.945 1.00 68.79  ? 375 ARG A NE  1 
ATOM   2911 C CZ  . ARG A 1 376 ? -34.788 -18.657 -13.891 1.00 62.42  ? 375 ARG A CZ  1 
ATOM   2912 N NH1 . ARG A 1 376 ? -34.322 -19.202 -12.775 1.00 55.94  ? 375 ARG A NH1 1 
ATOM   2913 N NH2 . ARG A 1 376 ? -34.915 -17.332 -13.964 1.00 55.21  ? 375 ARG A NH2 1 
ATOM   2914 N N   . PRO A 1 377 ? -30.425 -22.285 -18.127 1.00 58.32  ? 376 PRO A N   1 
ATOM   2915 C CA  . PRO A 1 377 ? -29.882 -22.542 -19.468 1.00 59.18  ? 376 PRO A CA  1 
ATOM   2916 C C   . PRO A 1 377 ? -30.981 -22.493 -20.513 1.00 62.50  ? 376 PRO A C   1 
ATOM   2917 O O   . PRO A 1 377 ? -32.144 -22.783 -20.232 1.00 63.18  ? 376 PRO A O   1 
ATOM   2918 C CB  . PRO A 1 377 ? -29.292 -23.954 -19.354 1.00 56.68  ? 376 PRO A CB  1 
ATOM   2919 C CG  . PRO A 1 377 ? -29.135 -24.193 -17.884 1.00 58.07  ? 376 PRO A CG  1 
ATOM   2920 C CD  . PRO A 1 377 ? -30.242 -23.436 -17.226 1.00 55.99  ? 376 PRO A CD  1 
ATOM   2921 N N   . ILE A 1 378 ? -30.607 -22.108 -21.729 1.00 65.03  ? 377 ILE A N   1 
ATOM   2922 C CA  . ILE A 1 378 ? -31.568 -22.091 -22.826 1.00 67.74  ? 377 ILE A CA  1 
ATOM   2923 C C   . ILE A 1 378 ? -31.695 -23.488 -23.426 1.00 66.73  ? 377 ILE A C   1 
ATOM   2924 O O   . ILE A 1 378 ? -32.766 -23.877 -23.898 1.00 72.37  ? 377 ILE A O   1 
ATOM   2925 C CB  . ILE A 1 378 ? -31.178 -21.058 -23.897 1.00 72.15  ? 377 ILE A CB  1 
ATOM   2926 C CG1 . ILE A 1 378 ? -30.001 -21.563 -24.726 1.00 80.40  ? 377 ILE A CG1 1 
ATOM   2927 C CG2 . ILE A 1 378 ? -30.815 -19.724 -23.256 1.00 65.85  ? 377 ILE A CG2 1 
ATOM   2928 C CD1 . ILE A 1 378 ? -30.379 -21.958 -26.147 1.00 81.18  ? 377 ILE A CD1 1 
ATOM   2929 N N   . MET B 2 1   ? 20.059  -17.366 -14.650 1.00 87.19  ? 1   MET B N   1 
ATOM   2930 C CA  . MET B 2 1   ? 20.395  -16.261 -13.758 1.00 84.80  ? 1   MET B CA  1 
ATOM   2931 C C   . MET B 2 1   ? 20.301  -16.642 -12.274 1.00 79.10  ? 1   MET B C   1 
ATOM   2932 O O   . MET B 2 1   ? 21.315  -16.933 -11.645 1.00 78.18  ? 1   MET B O   1 
ATOM   2933 C CB  . MET B 2 1   ? 19.494  -15.063 -14.053 1.00 91.69  ? 1   MET B CB  1 
ATOM   2934 C CG  . MET B 2 1   ? 20.110  -14.069 -15.018 1.00 101.36 ? 1   MET B CG  1 
ATOM   2935 S SD  . MET B 2 1   ? 21.513  -13.238 -14.244 1.00 109.01 ? 1   MET B SD  1 
ATOM   2936 C CE  . MET B 2 1   ? 20.737  -12.660 -12.727 1.00 94.76  ? 1   MET B CE  1 
ATOM   2937 N N   . ASP B 2 2   ? 19.092  -16.635 -11.716 1.00 70.00  ? 2   ASP B N   1 
ATOM   2938 C CA  . ASP B 2 2   ? 18.889  -16.955 -10.307 1.00 62.23  ? 2   ASP B CA  1 
ATOM   2939 C C   . ASP B 2 2   ? 18.603  -18.435 -10.115 1.00 56.84  ? 2   ASP B C   1 
ATOM   2940 O O   . ASP B 2 2   ? 17.800  -19.027 -10.840 1.00 59.37  ? 2   ASP B O   1 
ATOM   2941 C CB  . ASP B 2 2   ? 17.725  -16.158 -9.720  1.00 62.04  ? 2   ASP B CB  1 
ATOM   2942 C CG  . ASP B 2 2   ? 18.074  -14.719 -9.469  1.00 69.57  ? 2   ASP B CG  1 
ATOM   2943 O OD1 . ASP B 2 2   ? 19.187  -14.294 -9.855  1.00 69.87  ? 2   ASP B OD1 1 
ATOM   2944 O OD2 . ASP B 2 2   ? 17.224  -14.016 -8.881  1.00 70.45  ? 2   ASP B OD2 1 
ATOM   2945 N N   . VAL B 2 3   ? 19.245  -19.023 -9.116  1.00 54.44  ? 3   VAL B N   1 
ATOM   2946 C CA  . VAL B 2 3   ? 18.966  -20.391 -8.698  1.00 49.64  ? 3   VAL B CA  1 
ATOM   2947 C C   . VAL B 2 3   ? 18.303  -20.329 -7.332  1.00 43.26  ? 3   VAL B C   1 
ATOM   2948 O O   . VAL B 2 3   ? 18.752  -19.591 -6.446  1.00 41.97  ? 3   VAL B O   1 
ATOM   2949 C CB  . VAL B 2 3   ? 20.241  -21.257 -8.668  1.00 46.07  ? 3   VAL B CB  1 
ATOM   2950 C CG1 . VAL B 2 3   ? 20.656  -21.630 -10.084 1.00 49.84  ? 3   VAL B CG1 1 
ATOM   2951 C CG2 . VAL B 2 3   ? 21.357  -20.521 -7.977  1.00 45.76  ? 3   VAL B CG2 1 
ATOM   2952 N N   . PHE B 2 4   ? 17.229  -21.082 -7.162  1.00 42.00  ? 4   PHE B N   1 
ATOM   2953 C CA  . PHE B 2 4   ? 16.525  -21.126 -5.895  1.00 35.61  ? 4   PHE B CA  1 
ATOM   2954 C C   . PHE B 2 4   ? 16.816  -22.454 -5.219  1.00 37.10  ? 4   PHE B C   1 
ATOM   2955 O O   . PHE B 2 4   ? 16.700  -23.518 -5.839  1.00 33.49  ? 4   PHE B O   1 
ATOM   2956 C CB  . PHE B 2 4   ? 15.041  -20.874 -6.113  1.00 34.02  ? 4   PHE B CB  1 
ATOM   2957 C CG  . PHE B 2 4   ? 14.777  -19.516 -6.675  1.00 34.76  ? 4   PHE B CG  1 
ATOM   2958 C CD1 . PHE B 2 4   ? 14.886  -19.285 -8.043  1.00 38.02  ? 4   PHE B CD1 1 
ATOM   2959 C CD2 . PHE B 2 4   ? 14.509  -18.450 -5.834  1.00 35.27  ? 4   PHE B CD2 1 
ATOM   2960 C CE1 . PHE B 2 4   ? 14.682  -18.023 -8.566  1.00 41.85  ? 4   PHE B CE1 1 
ATOM   2961 C CE2 . PHE B 2 4   ? 14.301  -17.177 -6.342  1.00 38.96  ? 4   PHE B CE2 1 
ATOM   2962 C CZ  . PHE B 2 4   ? 14.382  -16.958 -7.716  1.00 42.35  ? 4   PHE B CZ  1 
ATOM   2963 N N   . LEU B 2 5   ? 17.227  -22.372 -3.955  1.00 34.44  ? 5   LEU B N   1 
ATOM   2964 C CA  . LEU B 2 5   ? 17.906  -23.452 -3.265  1.00 34.99  ? 5   LEU B CA  1 
ATOM   2965 C C   . LEU B 2 5   ? 17.243  -23.785 -1.934  1.00 34.90  ? 5   LEU B C   1 
ATOM   2966 O O   . LEU B 2 5   ? 16.579  -22.958 -1.298  1.00 33.14  ? 5   LEU B O   1 
ATOM   2967 C CB  . LEU B 2 5   ? 19.371  -23.094 -2.993  1.00 33.25  ? 5   LEU B CB  1 
ATOM   2968 C CG  . LEU B 2 5   ? 20.165  -22.737 -4.232  1.00 34.52  ? 5   LEU B CG  1 
ATOM   2969 C CD1 . LEU B 2 5   ? 21.567  -22.288 -3.828  1.00 30.05  ? 5   LEU B CD1 1 
ATOM   2970 C CD2 . LEU B 2 5   ? 20.184  -23.959 -5.154  1.00 35.40  ? 5   LEU B CD2 1 
ATOM   2971 N N   . MET B 2 6   ? 17.472  -25.023 -1.517  1.00 32.33  ? 6   MET B N   1 
ATOM   2972 C CA  . MET B 2 6   ? 17.250  -25.475 -0.152  1.00 30.40  ? 6   MET B CA  1 
ATOM   2973 C C   . MET B 2 6   ? 18.571  -26.081 0.292   1.00 30.22  ? 6   MET B C   1 
ATOM   2974 O O   . MET B 2 6   ? 19.019  -27.074 -0.296  1.00 30.62  ? 6   MET B O   1 
ATOM   2975 C CB  . MET B 2 6   ? 16.121  -26.507 -0.061  1.00 30.80  ? 6   MET B CB  1 
ATOM   2976 C CG  . MET B 2 6   ? 14.705  -25.977 -0.209  1.00 31.39  ? 6   MET B CG  1 
ATOM   2977 S SD  . MET B 2 6   ? 13.552  -27.355 0.030   1.00 33.23  ? 6   MET B SD  1 
ATOM   2978 C CE  . MET B 2 6   ? 14.096  -28.488 -1.239  1.00 26.84  ? 6   MET B CE  1 
ATOM   2979 N N   . ILE B 2 7   ? 19.201  -25.463 1.294   1.00 29.37  ? 7   ILE B N   1 
ATOM   2980 C CA  . ILE B 2 7   ? 20.419  -25.978 1.922   1.00 30.73  ? 7   ILE B CA  1 
ATOM   2981 C C   . ILE B 2 7   ? 19.994  -26.759 3.155   1.00 30.68  ? 7   ILE B C   1 
ATOM   2982 O O   . ILE B 2 7   ? 19.366  -26.197 4.060   1.00 32.13  ? 7   ILE B O   1 
ATOM   2983 C CB  . ILE B 2 7   ? 21.381  -24.841 2.302   1.00 29.84  ? 7   ILE B CB  1 
ATOM   2984 C CG1 . ILE B 2 7   ? 21.574  -23.894 1.111   1.00 30.32  ? 7   ILE B CG1 1 
ATOM   2985 C CG2 . ILE B 2 7   ? 22.714  -25.406 2.783   1.00 29.28  ? 7   ILE B CG2 1 
ATOM   2986 C CD1 . ILE B 2 7   ? 22.333  -22.623 1.445   1.00 30.27  ? 7   ILE B CD1 1 
ATOM   2987 N N   . ARG B 2 8   ? 20.313  -28.054 3.185   1.00 30.69  ? 8   ARG B N   1 
ATOM   2988 C CA  . ARG B 2 8   ? 19.679  -28.979 4.116   1.00 32.15  ? 8   ARG B CA  1 
ATOM   2989 C C   . ARG B 2 8   ? 20.723  -29.772 4.885   1.00 33.32  ? 8   ARG B C   1 
ATOM   2990 O O   . ARG B 2 8   ? 21.655  -30.333 4.293   1.00 33.95  ? 8   ARG B O   1 
ATOM   2991 C CB  . ARG B 2 8   ? 18.716  -29.925 3.385   1.00 29.52  ? 8   ARG B CB  1 
ATOM   2992 C CG  . ARG B 2 8   ? 17.685  -29.173 2.524   1.00 30.16  ? 8   ARG B CG  1 
ATOM   2993 C CD  . ARG B 2 8   ? 16.527  -30.069 2.103   1.00 28.40  ? 8   ARG B CD  1 
ATOM   2994 N NE  . ARG B 2 8   ? 15.888  -30.640 3.279   1.00 28.46  ? 8   ARG B NE  1 
ATOM   2995 C CZ  . ARG B 2 8   ? 15.311  -31.831 3.315   1.00 29.42  ? 8   ARG B CZ  1 
ATOM   2996 N NH1 . ARG B 2 8   ? 15.176  -32.567 2.223   1.00 27.85  ? 8   ARG B NH1 1 
ATOM   2997 N NH2 . ARG B 2 8   ? 14.891  -32.308 4.483   1.00 29.93  ? 8   ARG B NH2 1 
ATOM   2998 N N   . ARG B 2 9   ? 20.550  -29.816 6.204   1.00 31.97  ? 9   ARG B N   1 
ATOM   2999 C CA  . ARG B 2 9   ? 21.378  -30.609 7.097   1.00 30.85  ? 9   ARG B CA  1 
ATOM   3000 C C   . ARG B 2 9   ? 20.482  -31.115 8.209   1.00 31.91  ? 9   ARG B C   1 
ATOM   3001 O O   . ARG B 2 9   ? 19.788  -30.315 8.841   1.00 34.83  ? 9   ARG B O   1 
ATOM   3002 C CB  . ARG B 2 9   ? 22.529  -29.774 7.667   1.00 32.15  ? 9   ARG B CB  1 
ATOM   3003 C CG  . ARG B 2 9   ? 23.425  -30.537 8.628   1.00 34.03  ? 9   ARG B CG  1 
ATOM   3004 C CD  . ARG B 2 9   ? 24.175  -29.585 9.499   1.00 33.65  ? 9   ARG B CD  1 
ATOM   3005 N NE  . ARG B 2 9   ? 24.906  -30.299 10.534  1.00 37.55  ? 9   ARG B NE  1 
ATOM   3006 C CZ  . ARG B 2 9   ? 24.529  -30.392 11.803  1.00 39.26  ? 9   ARG B CZ  1 
ATOM   3007 N NH1 . ARG B 2 9   ? 23.417  -29.820 12.242  1.00 38.66  ? 9   ARG B NH1 1 
ATOM   3008 N NH2 . ARG B 2 9   ? 25.290  -31.073 12.653  1.00 42.76  ? 9   ARG B NH2 1 
ATOM   3009 N N   . HIS B 2 10  ? 20.501  -32.426 8.449   1.00 32.38  ? 10  HIS B N   1 
ATOM   3010 C CA  . HIS B 2 10  ? 19.671  -33.032 9.485   1.00 34.68  ? 10  HIS B CA  1 
ATOM   3011 C C   . HIS B 2 10  ? 18.222  -32.577 9.347   1.00 39.17  ? 10  HIS B C   1 
ATOM   3012 O O   . HIS B 2 10  ? 17.582  -32.855 8.330   1.00 37.53  ? 10  HIS B O   1 
ATOM   3013 C CB  . HIS B 2 10  ? 20.199  -32.689 10.874  1.00 35.67  ? 10  HIS B CB  1 
ATOM   3014 C CG  . HIS B 2 10  ? 21.555  -33.248 11.159  1.00 40.73  ? 10  HIS B CG  1 
ATOM   3015 N ND1 . HIS B 2 10  ? 22.134  -33.188 12.409  1.00 40.93  ? 10  HIS B ND1 1 
ATOM   3016 C CD2 . HIS B 2 10  ? 22.456  -33.864 10.356  1.00 38.58  ? 10  HIS B CD2 1 
ATOM   3017 C CE1 . HIS B 2 10  ? 23.328  -33.750 12.365  1.00 38.51  ? 10  HIS B CE1 1 
ATOM   3018 N NE2 . HIS B 2 10  ? 23.548  -34.169 11.131  1.00 35.72  ? 10  HIS B NE2 1 
ATOM   3019 N N   . LYS B 2 11  ? 17.696  -31.864 10.349  1.00 37.75  ? 11  LYS B N   1 
ATOM   3020 C CA  . LYS B 2 11  ? 16.338  -31.334 10.291  1.00 38.74  ? 11  LYS B CA  1 
ATOM   3021 C C   . LYS B 2 11  ? 16.315  -29.823 10.086  1.00 40.73  ? 11  LYS B C   1 
ATOM   3022 O O   . LYS B 2 11  ? 15.315  -29.171 10.420  1.00 40.09  ? 11  LYS B O   1 
ATOM   3023 C CB  . LYS B 2 11  ? 15.553  -31.713 11.547  1.00 40.36  ? 11  LYS B CB  1 
ATOM   3024 C CG  . LYS B 2 11  ? 15.169  -33.181 11.612  1.00 41.24  ? 11  LYS B CG  1 
ATOM   3025 C CD  . LYS B 2 11  ? 14.382  -33.465 12.853  1.00 42.68  ? 11  LYS B CD  1 
ATOM   3026 C CE  . LYS B 2 11  ? 13.168  -34.325 12.578  1.00 43.50  ? 11  LYS B CE  1 
ATOM   3027 N NZ  . LYS B 2 11  ? 12.389  -34.478 13.839  1.00 43.24  ? 11  LYS B NZ  1 
ATOM   3028 N N   . THR B 2 12  ? 17.393  -29.260 9.535   1.00 35.85  ? 12  THR B N   1 
ATOM   3029 C CA  . THR B 2 12  ? 17.458  -27.856 9.158   1.00 35.14  ? 12  THR B CA  1 
ATOM   3030 C C   . THR B 2 12  ? 17.365  -27.727 7.646   1.00 34.97  ? 12  THR B C   1 
ATOM   3031 O O   . THR B 2 12  ? 18.007  -28.483 6.912   1.00 34.36  ? 12  THR B O   1 
ATOM   3032 C CB  . THR B 2 12  ? 18.758  -27.205 9.635   1.00 36.63  ? 12  THR B CB  1 
ATOM   3033 O OG1 . THR B 2 12  ? 18.871  -27.343 11.057  1.00 44.16  ? 12  THR B OG1 1 
ATOM   3034 C CG2 . THR B 2 12  ? 18.771  -25.723 9.264   1.00 32.63  ? 12  THR B CG2 1 
ATOM   3035 N N   . THR B 2 13  ? 16.570  -26.761 7.184   1.00 34.99  ? 13  THR B N   1 
ATOM   3036 C CA  . THR B 2 13  ? 16.413  -26.477 5.758   1.00 31.86  ? 13  THR B CA  1 
ATOM   3037 C C   . THR B 2 13  ? 16.433  -24.962 5.588   1.00 34.95  ? 13  THR B C   1 
ATOM   3038 O O   . THR B 2 13  ? 15.505  -24.277 6.044   1.00 32.15  ? 13  THR B O   1 
ATOM   3039 C CB  . THR B 2 13  ? 15.104  -27.072 5.213   1.00 31.33  ? 13  THR B CB  1 
ATOM   3040 O OG1 . THR B 2 13  ? 15.137  -28.501 5.295   1.00 30.33  ? 13  THR B OG1 1 
ATOM   3041 C CG2 . THR B 2 13  ? 14.850  -26.646 3.759   1.00 27.64  ? 13  THR B CG2 1 
ATOM   3042 N N   . ILE B 2 14  ? 17.464  -24.434 4.916   1.00 31.19  ? 14  ILE B N   1 
ATOM   3043 C CA  . ILE B 2 14  ? 17.502  -23.015 4.553   1.00 32.88  ? 14  ILE B CA  1 
ATOM   3044 C C   . ILE B 2 14  ? 16.963  -22.819 3.135   1.00 33.02  ? 14  ILE B C   1 
ATOM   3045 O O   . ILE B 2 14  ? 17.412  -23.484 2.192   1.00 31.91  ? 14  ILE B O   1 
ATOM   3046 C CB  . ILE B 2 14  ? 18.921  -22.438 4.672   1.00 30.26  ? 14  ILE B CB  1 
ATOM   3047 C CG1 . ILE B 2 14  ? 19.414  -22.512 6.125   1.00 33.42  ? 14  ILE B CG1 1 
ATOM   3048 C CG2 . ILE B 2 14  ? 18.945  -20.987 4.162   1.00 29.55  ? 14  ILE B CG2 1 
ATOM   3049 C CD1 . ILE B 2 14  ? 20.919  -22.518 6.238   1.00 30.86  ? 14  ILE B CD1 1 
ATOM   3050 N N   . PHE B 2 15  ? 16.014  -21.893 2.981   1.00 29.97  ? 15  PHE B N   1 
ATOM   3051 C CA  . PHE B 2 15  ? 15.549  -21.434 1.675   1.00 32.04  ? 15  PHE B CA  1 
ATOM   3052 C C   . PHE B 2 15  ? 16.303  -20.168 1.299   1.00 37.05  ? 15  PHE B C   1 
ATOM   3053 O O   . PHE B 2 15  ? 16.204  -19.156 2.004   1.00 36.64  ? 15  PHE B O   1 
ATOM   3054 C CB  . PHE B 2 15  ? 14.047  -21.139 1.679   1.00 30.24  ? 15  PHE B CB  1 
ATOM   3055 C CG  . PHE B 2 15  ? 13.198  -22.365 1.675   1.00 32.42  ? 15  PHE B CG  1 
ATOM   3056 C CD1 . PHE B 2 15  ? 12.973  -23.072 2.848   1.00 30.90  ? 15  PHE B CD1 1 
ATOM   3057 C CD2 . PHE B 2 15  ? 12.637  -22.828 0.499   1.00 33.69  ? 15  PHE B CD2 1 
ATOM   3058 C CE1 . PHE B 2 15  ? 12.207  -24.212 2.843   1.00 29.64  ? 15  PHE B CE1 1 
ATOM   3059 C CE2 . PHE B 2 15  ? 11.855  -23.968 0.492   1.00 32.00  ? 15  PHE B CE2 1 
ATOM   3060 C CZ  . PHE B 2 15  ? 11.647  -24.659 1.660   1.00 29.59  ? 15  PHE B CZ  1 
ATOM   3061 N N   . THR B 2 16  ? 17.029  -20.208 0.183   1.00 33.94  ? 16  THR B N   1 
ATOM   3062 C CA  . THR B 2 16  ? 17.688  -18.999 -0.279  1.00 37.96  ? 16  THR B CA  1 
ATOM   3063 C C   . THR B 2 16  ? 17.904  -19.072 -1.782  1.00 38.93  ? 16  THR B C   1 
ATOM   3064 O O   . THR B 2 16  ? 17.850  -20.145 -2.389  1.00 37.80  ? 16  THR B O   1 
ATOM   3065 C CB  . THR B 2 16  ? 19.019  -18.764 0.455   1.00 40.51  ? 16  THR B CB  1 
ATOM   3066 O OG1 . THR B 2 16  ? 19.452  -17.421 0.205   1.00 41.43  ? 16  THR B OG1 1 
ATOM   3067 C CG2 . THR B 2 16  ? 20.089  -19.754 -0.006  1.00 35.11  ? 16  THR B CG2 1 
ATOM   3068 N N   . ASP B 2 17  ? 18.139  -17.903 -2.375  1.00 37.49  ? 17  ASP B N   1 
ATOM   3069 C CA  . ASP B 2 17  ? 18.483  -17.783 -3.783  1.00 43.01  ? 17  ASP B CA  1 
ATOM   3070 C C   . ASP B 2 17  ? 19.915  -17.282 -3.947  1.00 43.41  ? 17  ASP B C   1 
ATOM   3071 O O   . ASP B 2 17  ? 20.517  -16.734 -3.019  1.00 42.79  ? 17  ASP B O   1 
ATOM   3072 C CB  . ASP B 2 17  ? 17.528  -16.832 -4.511  1.00 41.23  ? 17  ASP B CB  1 
ATOM   3073 C CG  . ASP B 2 17  ? 17.286  -15.566 -3.732  1.00 45.87  ? 17  ASP B CG  1 
ATOM   3074 O OD1 . ASP B 2 17  ? 16.603  -15.644 -2.682  1.00 54.91  ? 17  ASP B OD1 1 
ATOM   3075 O OD2 . ASP B 2 17  ? 17.790  -14.507 -4.149  1.00 46.95  ? 17  ASP B OD2 1 
ATOM   3076 N N   . ALA B 2 18  ? 20.444  -17.469 -5.158  1.00 47.26  ? 18  ALA B N   1 
ATOM   3077 C CA  . ALA B 2 18  ? 21.759  -16.969 -5.536  1.00 48.25  ? 18  ALA B CA  1 
ATOM   3078 C C   . ALA B 2 18  ? 21.832  -16.913 -7.054  1.00 52.61  ? 18  ALA B C   1 
ATOM   3079 O O   . ALA B 2 18  ? 20.952  -17.421 -7.753  1.00 55.30  ? 18  ALA B O   1 
ATOM   3080 C CB  . ALA B 2 18  ? 22.879  -17.843 -4.968  1.00 41.85  ? 18  ALA B CB  1 
ATOM   3081 N N   . LYS B 2 19  ? 22.886  -16.272 -7.556  1.00 53.45  ? 19  LYS B N   1 
ATOM   3082 C CA  . LYS B 2 19  ? 23.142  -16.245 -8.989  1.00 56.65  ? 19  LYS B CA  1 
ATOM   3083 C C   . LYS B 2 19  ? 23.812  -17.540 -9.430  1.00 56.68  ? 19  LYS B C   1 
ATOM   3084 O O   . LYS B 2 19  ? 24.554  -18.167 -8.671  1.00 53.10  ? 19  LYS B O   1 
ATOM   3085 C CB  . LYS B 2 19  ? 24.045  -15.072 -9.366  1.00 57.54  ? 19  LYS B CB  1 
ATOM   3086 C CG  . LYS B 2 19  ? 23.564  -13.721 -8.902  1.00 61.85  ? 19  LYS B CG  1 
ATOM   3087 C CD  . LYS B 2 19  ? 22.239  -13.372 -9.533  1.00 67.10  ? 19  LYS B CD  1 
ATOM   3088 C CE  . LYS B 2 19  ? 21.934  -11.890 -9.416  1.00 61.78  ? 19  LYS B CE  1 
ATOM   3089 N NZ  . LYS B 2 19  ? 20.478  -11.639 -9.623  1.00 67.92  ? 19  LYS B NZ  1 
ATOM   3090 N N   . GLU B 2 20  ? 23.562  -17.929 -10.682 1.00 59.27  ? 20  GLU B N   1 
ATOM   3091 C CA  . GLU B 2 20  ? 24.322  -19.035 -11.250 1.00 56.22  ? 20  GLU B CA  1 
ATOM   3092 C C   . GLU B 2 20  ? 25.817  -18.768 -11.156 1.00 55.99  ? 20  GLU B C   1 
ATOM   3093 O O   . GLU B 2 20  ? 26.605  -19.702 -10.961 1.00 52.34  ? 20  GLU B O   1 
ATOM   3094 C CB  . GLU B 2 20  ? 23.930  -19.275 -12.710 1.00 56.69  ? 20  GLU B CB  1 
ATOM   3095 C CG  . GLU B 2 20  ? 22.576  -19.938 -12.937 1.00 60.04  ? 20  GLU B CG  1 
ATOM   3096 C CD  . GLU B 2 20  ? 22.468  -20.567 -14.319 1.00 62.63  ? 20  GLU B CD  1 
ATOM   3097 O OE1 . GLU B 2 20  ? 23.466  -21.177 -14.764 1.00 65.60  ? 20  GLU B OE1 1 
ATOM   3098 O OE2 . GLU B 2 20  ? 21.403  -20.446 -14.965 1.00 61.77  ? 20  GLU B OE2 1 
ATOM   3099 N N   . SER B 2 21  ? 26.218  -17.498 -11.261 1.00 57.39  ? 21  SER B N   1 
ATOM   3100 C CA  . SER B 2 21  ? 27.622  -17.109 -11.314 1.00 58.29  ? 21  SER B CA  1 
ATOM   3101 C C   . SER B 2 21  ? 28.263  -16.925 -9.944  1.00 58.73  ? 21  SER B C   1 
ATOM   3102 O O   . SER B 2 21  ? 29.470  -16.667 -9.880  1.00 58.16  ? 21  SER B O   1 
ATOM   3103 C CB  . SER B 2 21  ? 27.775  -15.807 -12.089 1.00 62.91  ? 21  SER B CB  1 
ATOM   3104 O OG  . SER B 2 21  ? 27.335  -14.717 -11.302 1.00 63.21  ? 21  SER B OG  1 
ATOM   3105 N N   . SER B 2 22  ? 27.493  -17.015 -8.861  1.00 56.32  ? 22  SER B N   1 
ATOM   3106 C CA  . SER B 2 22  ? 28.065  -16.867 -7.531  1.00 55.48  ? 22  SER B CA  1 
ATOM   3107 C C   . SER B 2 22  ? 28.695  -18.184 -7.076  1.00 51.39  ? 22  SER B C   1 
ATOM   3108 O O   . SER B 2 22  ? 28.390  -19.264 -7.589  1.00 50.65  ? 22  SER B O   1 
ATOM   3109 C CB  . SER B 2 22  ? 27.002  -16.387 -6.532  1.00 54.82  ? 22  SER B CB  1 
ATOM   3110 O OG  . SER B 2 22  ? 25.983  -17.338 -6.318  1.00 46.77  ? 22  SER B OG  1 
ATOM   3111 N N   . THR B 2 23  ? 29.588  -18.087 -6.103  1.00 49.94  ? 23  THR B N   1 
ATOM   3112 C CA  . THR B 2 23  ? 30.466  -19.205 -5.794  1.00 50.63  ? 23  THR B CA  1 
ATOM   3113 C C   . THR B 2 23  ? 29.953  -20.013 -4.609  1.00 49.41  ? 23  THR B C   1 
ATOM   3114 O O   . THR B 2 23  ? 29.150  -19.541 -3.794  1.00 46.57  ? 23  THR B O   1 
ATOM   3115 C CB  . THR B 2 23  ? 31.882  -18.711 -5.508  1.00 50.56  ? 23  THR B CB  1 
ATOM   3116 O OG1 . THR B 2 23  ? 31.881  -17.943 -4.299  1.00 52.84  ? 23  THR B OG1 1 
ATOM   3117 C CG2 . THR B 2 23  ? 32.375  -17.845 -6.658  1.00 53.54  ? 23  THR B CG2 1 
ATOM   3118 N N   . VAL B 2 24  ? 30.441  -21.255 -4.535  1.00 49.47  ? 24  VAL B N   1 
ATOM   3119 C CA  . VAL B 2 24  ? 30.115  -22.141 -3.420  1.00 45.94  ? 24  VAL B CA  1 
ATOM   3120 C C   . VAL B 2 24  ? 30.538  -21.499 -2.108  1.00 43.37  ? 24  VAL B C   1 
ATOM   3121 O O   . VAL B 2 24  ? 29.836  -21.585 -1.097  1.00 42.11  ? 24  VAL B O   1 
ATOM   3122 C CB  . VAL B 2 24  ? 30.785  -23.514 -3.629  1.00 45.09  ? 24  VAL B CB  1 
ATOM   3123 C CG1 . VAL B 2 24  ? 30.621  -24.406 -2.411  1.00 44.34  ? 24  VAL B CG1 1 
ATOM   3124 C CG2 . VAL B 2 24  ? 30.237  -24.201 -4.875  1.00 40.36  ? 24  VAL B CG2 1 
ATOM   3125 N N   . PHE B 2 25  ? 31.678  -20.815 -2.117  1.00 44.45  ? 25  PHE B N   1 
ATOM   3126 C CA  . PHE B 2 25  ? 32.120  -20.089 -0.934  1.00 46.05  ? 25  PHE B CA  1 
ATOM   3127 C C   . PHE B 2 25  ? 31.128  -18.997 -0.538  1.00 46.91  ? 25  PHE B C   1 
ATOM   3128 O O   . PHE B 2 25  ? 30.795  -18.854 0.647   1.00 44.33  ? 25  PHE B O   1 
ATOM   3129 C CB  . PHE B 2 25  ? 33.506  -19.504 -1.188  1.00 44.15  ? 25  PHE B CB  1 
ATOM   3130 C CG  . PHE B 2 25  ? 34.148  -18.904 0.035   1.00 49.05  ? 25  PHE B CG  1 
ATOM   3131 C CD1 . PHE B 2 25  ? 34.817  -19.711 0.953   1.00 43.86  ? 25  PHE B CD1 1 
ATOM   3132 C CD2 . PHE B 2 25  ? 34.102  -17.524 0.256   1.00 50.27  ? 25  PHE B CD2 1 
ATOM   3133 C CE1 . PHE B 2 25  ? 35.417  -19.156 2.068   1.00 45.24  ? 25  PHE B CE1 1 
ATOM   3134 C CE2 . PHE B 2 25  ? 34.699  -16.964 1.369   1.00 49.60  ? 25  PHE B CE2 1 
ATOM   3135 C CZ  . PHE B 2 25  ? 35.361  -17.783 2.279   1.00 48.32  ? 25  PHE B CZ  1 
ATOM   3136 N N   . GLU B 2 26  ? 30.639  -18.214 -1.509  1.00 46.24  ? 26  GLU B N   1 
ATOM   3137 C CA  . GLU B 2 26  ? 29.598  -17.240 -1.189  1.00 44.91  ? 26  GLU B CA  1 
ATOM   3138 C C   . GLU B 2 26  ? 28.390  -17.931 -0.576  1.00 44.32  ? 26  GLU B C   1 
ATOM   3139 O O   . GLU B 2 26  ? 27.765  -17.409 0.358   1.00 42.50  ? 26  GLU B O   1 
ATOM   3140 C CB  . GLU B 2 26  ? 29.189  -16.457 -2.436  1.00 46.54  ? 26  GLU B CB  1 
ATOM   3141 C CG  . GLU B 2 26  ? 30.279  -15.546 -3.001  1.00 52.34  ? 26  GLU B CG  1 
ATOM   3142 C CD  . GLU B 2 26  ? 29.860  -14.864 -4.303  1.00 61.16  ? 26  GLU B CD  1 
ATOM   3143 O OE1 . GLU B 2 26  ? 28.642  -14.684 -4.519  1.00 66.40  ? 26  GLU B OE1 1 
ATOM   3144 O OE2 . GLU B 2 26  ? 30.742  -14.501 -5.112  1.00 68.20  ? 26  GLU B OE2 1 
ATOM   3145 N N   . LEU B 2 27  ? 28.061  -19.123 -1.072  1.00 42.79  ? 27  LEU B N   1 
ATOM   3146 C CA  . LEU B 2 27  ? 26.971  -19.880 -0.478  1.00 41.42  ? 27  LEU B CA  1 
ATOM   3147 C C   . LEU B 2 27  ? 27.298  -20.243 0.960   1.00 42.81  ? 27  LEU B C   1 
ATOM   3148 O O   . LEU B 2 27  ? 26.435  -20.166 1.843   1.00 44.00  ? 27  LEU B O   1 
ATOM   3149 C CB  . LEU B 2 27  ? 26.694  -21.131 -1.304  1.00 40.78  ? 27  LEU B CB  1 
ATOM   3150 C CG  . LEU B 2 27  ? 25.255  -21.602 -1.257  1.00 39.00  ? 27  LEU B CG  1 
ATOM   3151 C CD1 . LEU B 2 27  ? 24.377  -20.522 -1.834  1.00 41.49  ? 27  LEU B CD1 1 
ATOM   3152 C CD2 . LEU B 2 27  ? 25.103  -22.897 -2.019  1.00 35.20  ? 27  LEU B CD2 1 
ATOM   3153 N N   . LYS B 2 28  ? 28.551  -20.626 1.217   1.00 42.39  ? 28  LYS B N   1 
ATOM   3154 C CA  . LYS B 2 28  ? 28.945  -20.972 2.576   1.00 41.33  ? 28  LYS B CA  1 
ATOM   3155 C C   . LYS B 2 28  ? 28.830  -19.779 3.507   1.00 41.34  ? 28  LYS B C   1 
ATOM   3156 O O   . LYS B 2 28  ? 28.514  -19.954 4.690   1.00 41.76  ? 28  LYS B O   1 
ATOM   3157 C CB  . LYS B 2 28  ? 30.374  -21.521 2.603   1.00 39.59  ? 28  LYS B CB  1 
ATOM   3158 C CG  . LYS B 2 28  ? 30.504  -22.941 2.134   1.00 37.31  ? 28  LYS B CG  1 
ATOM   3159 C CD  . LYS B 2 28  ? 31.955  -23.389 2.209   1.00 39.45  ? 28  LYS B CD  1 
ATOM   3160 C CE  . LYS B 2 28  ? 32.081  -24.879 1.895   1.00 41.04  ? 28  LYS B CE  1 
ATOM   3161 N NZ  . LYS B 2 28  ? 33.496  -25.339 1.776   1.00 43.16  ? 28  LYS B NZ  1 
ATOM   3162 N N   . ARG B 2 29  ? 29.075  -18.561 3.003   1.00 39.76  ? 29  ARG B N   1 
ATOM   3163 C CA  . ARG B 2 29  ? 29.020  -17.402 3.891   1.00 43.83  ? 29  ARG B CA  1 
ATOM   3164 C C   . ARG B 2 29  ? 27.584  -17.017 4.234   1.00 44.20  ? 29  ARG B C   1 
ATOM   3165 O O   . ARG B 2 29  ? 27.344  -16.435 5.299   1.00 44.82  ? 29  ARG B O   1 
ATOM   3166 C CB  . ARG B 2 29  ? 29.793  -16.222 3.295   1.00 43.42  ? 29  ARG B CB  1 
ATOM   3167 C CG  . ARG B 2 29  ? 31.318  -16.426 3.390   1.00 45.19  ? 29  ARG B CG  1 
ATOM   3168 C CD  . ARG B 2 29  ? 32.089  -15.188 3.859   1.00 51.43  ? 29  ARG B CD  1 
ATOM   3169 N NE  . ARG B 2 29  ? 33.463  -15.534 4.219   1.00 59.25  ? 29  ARG B NE  1 
ATOM   3170 C CZ  . ARG B 2 29  ? 33.920  -15.638 5.463   1.00 59.82  ? 29  ARG B CZ  1 
ATOM   3171 N NH1 . ARG B 2 29  ? 33.160  -15.342 6.506   1.00 62.98  ? 29  ARG B NH1 1 
ATOM   3172 N NH2 . ARG B 2 29  ? 35.171  -16.048 5.666   1.00 54.50  ? 29  ARG B NH2 1 
ATOM   3173 N N   . ILE B 2 30  ? 26.616  -17.353 3.372   1.00 43.85  ? 30  ILE B N   1 
ATOM   3174 C CA  . ILE B 2 30  ? 25.207  -17.209 3.743   1.00 42.58  ? 30  ILE B CA  1 
ATOM   3175 C C   . ILE B 2 30  ? 24.869  -18.151 4.889   1.00 40.91  ? 30  ILE B C   1 
ATOM   3176 O O   . ILE B 2 30  ? 24.265  -17.750 5.891   1.00 43.36  ? 30  ILE B O   1 
ATOM   3177 C CB  . ILE B 2 30  ? 24.297  -17.463 2.527   1.00 44.16  ? 30  ILE B CB  1 
ATOM   3178 C CG1 . ILE B 2 30  ? 24.558  -16.433 1.428   1.00 41.57  ? 30  ILE B CG1 1 
ATOM   3179 C CG2 . ILE B 2 30  ? 22.810  -17.475 2.933   1.00 37.32  ? 30  ILE B CG2 1 
ATOM   3180 C CD1 . ILE B 2 30  ? 24.024  -16.885 0.079   1.00 46.01  ? 30  ILE B CD1 1 
ATOM   3181 N N   . VAL B 2 31  ? 25.278  -19.416 4.762   1.00 40.18  ? 31  VAL B N   1 
ATOM   3182 C CA  . VAL B 2 31  ? 25.125  -20.378 5.851   1.00 39.82  ? 31  VAL B CA  1 
ATOM   3183 C C   . VAL B 2 31  ? 25.804  -19.873 7.116   1.00 40.65  ? 31  VAL B C   1 
ATOM   3184 O O   . VAL B 2 31  ? 25.269  -20.015 8.226   1.00 40.66  ? 31  VAL B O   1 
ATOM   3185 C CB  . VAL B 2 31  ? 25.690  -21.744 5.428   1.00 39.16  ? 31  VAL B CB  1 
ATOM   3186 C CG1 . VAL B 2 31  ? 25.691  -22.711 6.610   1.00 33.77  ? 31  VAL B CG1 1 
ATOM   3187 C CG2 . VAL B 2 31  ? 24.915  -22.284 4.229   1.00 32.56  ? 31  VAL B CG2 1 
ATOM   3188 N N   . GLU B 2 32  ? 26.993  -19.272 6.975   1.00 39.04  ? 32  GLU B N   1 
ATOM   3189 C CA  . GLU B 2 32  ? 27.723  -18.834 8.158   1.00 40.29  ? 32  GLU B CA  1 
ATOM   3190 C C   . GLU B 2 32  ? 26.930  -17.799 8.940   1.00 40.45  ? 32  GLU B C   1 
ATOM   3191 O O   . GLU B 2 32  ? 26.888  -17.846 10.174  1.00 41.59  ? 32  GLU B O   1 
ATOM   3192 C CB  . GLU B 2 32  ? 29.092  -18.273 7.783   1.00 41.89  ? 32  GLU B CB  1 
ATOM   3193 C CG  . GLU B 2 32  ? 29.814  -17.689 9.000   1.00 40.92  ? 32  GLU B CG  1 
ATOM   3194 C CD  . GLU B 2 32  ? 31.155  -17.082 8.662   1.00 46.44  ? 32  GLU B CD  1 
ATOM   3195 O OE1 . GLU B 2 32  ? 31.306  -16.572 7.535   1.00 50.14  ? 32  GLU B OE1 1 
ATOM   3196 O OE2 . GLU B 2 32  ? 32.062  -17.123 9.524   1.00 50.01  ? 32  GLU B OE2 1 
ATOM   3197 N N   . GLY B 2 33  ? 26.287  -16.860 8.241   1.00 38.01  ? 33  GLY B N   1 
ATOM   3198 C CA  . GLY B 2 33  ? 25.540  -15.826 8.925   1.00 39.25  ? 33  GLY B CA  1 
ATOM   3199 C C   . GLY B 2 33  ? 24.250  -16.318 9.534   1.00 42.98  ? 33  GLY B C   1 
ATOM   3200 O O   . GLY B 2 33  ? 23.688  -15.640 10.400  1.00 49.15  ? 33  GLY B O   1 
ATOM   3201 N N   . ILE B 2 34  ? 23.767  -17.476 9.103   1.00 40.45  ? 34  ILE B N   1 
ATOM   3202 C CA  . ILE B 2 34  ? 22.569  -18.086 9.662   1.00 39.77  ? 34  ILE B CA  1 
ATOM   3203 C C   . ILE B 2 34  ? 22.912  -19.057 10.774  1.00 40.34  ? 34  ILE B C   1 
ATOM   3204 O O   . ILE B 2 34  ? 22.377  -18.962 11.876  1.00 40.64  ? 34  ILE B O   1 
ATOM   3205 C CB  . ILE B 2 34  ? 21.756  -18.795 8.557   1.00 37.67  ? 34  ILE B CB  1 
ATOM   3206 C CG1 . ILE B 2 34  ? 21.256  -17.775 7.522   1.00 38.55  ? 34  ILE B CG1 1 
ATOM   3207 C CG2 . ILE B 2 34  ? 20.630  -19.595 9.200   1.00 35.41  ? 34  ILE B CG2 1 
ATOM   3208 C CD1 . ILE B 2 34  ? 20.459  -18.376 6.376   1.00 37.14  ? 34  ILE B CD1 1 
ATOM   3209 N N   . LEU B 2 35  ? 23.819  -19.995 10.502  1.00 38.78  ? 35  LEU B N   1 
ATOM   3210 C CA  . LEU B 2 35  ? 24.098  -21.110 11.394  1.00 37.15  ? 35  LEU B CA  1 
ATOM   3211 C C   . LEU B 2 35  ? 25.405  -20.939 12.175  1.00 41.01  ? 35  LEU B C   1 
ATOM   3212 O O   . LEU B 2 35  ? 25.803  -21.856 12.904  1.00 39.57  ? 35  LEU B O   1 
ATOM   3213 C CB  . LEU B 2 35  ? 24.099  -22.418 10.576  1.00 36.99  ? 35  LEU B CB  1 
ATOM   3214 C CG  . LEU B 2 35  ? 22.757  -22.649 9.854   1.00 37.55  ? 35  LEU B CG  1 
ATOM   3215 C CD1 . LEU B 2 35  ? 22.788  -23.888 9.004   1.00 31.95  ? 35  LEU B CD1 1 
ATOM   3216 C CD2 . LEU B 2 35  ? 21.578  -22.718 10.838  1.00 30.32  ? 35  LEU B CD2 1 
ATOM   3217 N N   . LYS B 2 36  ? 26.075  -19.790 12.030  1.00 37.70  ? 36  LYS B N   1 
ATOM   3218 C CA  . LYS B 2 36  ? 27.219  -19.397 12.859  1.00 39.37  ? 36  LYS B CA  1 
ATOM   3219 C C   . LYS B 2 36  ? 28.354  -20.420 12.829  1.00 41.44  ? 36  LYS B C   1 
ATOM   3220 O O   . LYS B 2 36  ? 28.967  -20.720 13.856  1.00 43.24  ? 36  LYS B O   1 
ATOM   3221 C CB  . LYS B 2 36  ? 26.775  -19.130 14.292  1.00 41.87  ? 36  LYS B CB  1 
ATOM   3222 C CG  . LYS B 2 36  ? 25.450  -18.390 14.399  1.00 44.91  ? 36  LYS B CG  1 
ATOM   3223 C CD  . LYS B 2 36  ? 25.572  -16.950 13.945  1.00 48.13  ? 36  LYS B CD  1 
ATOM   3224 C CE  . LYS B 2 36  ? 24.205  -16.264 13.950  1.00 53.72  ? 36  LYS B CE  1 
ATOM   3225 N NZ  . LYS B 2 36  ? 23.769  -15.857 12.570  1.00 55.20  ? 36  LYS B NZ  1 
ATOM   3226 N N   . ARG B 2 37  ? 28.643  -20.957 11.646  1.00 41.67  ? 37  ARG B N   1 
ATOM   3227 C CA  . ARG B 2 37  ? 29.794  -21.826 11.437  1.00 41.11  ? 37  ARG B CA  1 
ATOM   3228 C C   . ARG B 2 37  ? 30.533  -21.299 10.212  1.00 41.10  ? 37  ARG B C   1 
ATOM   3229 O O   . ARG B 2 37  ? 29.896  -21.021 9.183   1.00 40.35  ? 37  ARG B O   1 
ATOM   3230 C CB  . ARG B 2 37  ? 29.382  -23.292 11.220  1.00 41.39  ? 37  ARG B CB  1 
ATOM   3231 C CG  . ARG B 2 37  ? 28.596  -23.915 12.365  1.00 41.15  ? 37  ARG B CG  1 
ATOM   3232 C CD  . ARG B 2 37  ? 29.461  -24.093 13.606  1.00 39.03  ? 37  ARG B CD  1 
ATOM   3233 N NE  . ARG B 2 37  ? 30.515  -25.085 13.399  1.00 43.53  ? 37  ARG B NE  1 
ATOM   3234 C CZ  . ARG B 2 37  ? 30.355  -26.400 13.516  1.00 42.20  ? 37  ARG B CZ  1 
ATOM   3235 N NH1 . ARG B 2 37  ? 29.180  -26.935 13.820  1.00 40.49  ? 37  ARG B NH1 1 
ATOM   3236 N NH2 . ARG B 2 37  ? 31.400  -27.199 13.319  1.00 36.28  ? 37  ARG B NH2 1 
ATOM   3237 N N   . PRO B 2 38  ? 31.853  -21.153 10.268  1.00 45.65  ? 38  PRO B N   1 
ATOM   3238 C CA  . PRO B 2 38  ? 32.576  -20.522 9.157   1.00 41.01  ? 38  PRO B CA  1 
ATOM   3239 C C   . PRO B 2 38  ? 32.669  -21.462 7.966   1.00 41.09  ? 38  PRO B C   1 
ATOM   3240 O O   . PRO B 2 38  ? 32.430  -22.670 8.095   1.00 38.64  ? 38  PRO B O   1 
ATOM   3241 C CB  . PRO B 2 38  ? 33.957  -20.224 9.765   1.00 41.44  ? 38  PRO B CB  1 
ATOM   3242 C CG  . PRO B 2 38  ? 34.142  -21.292 10.814  1.00 41.39  ? 38  PRO B CG  1 
ATOM   3243 C CD  . PRO B 2 38  ? 32.762  -21.624 11.339  1.00 44.93  ? 38  PRO B CD  1 
ATOM   3244 N N   . PRO B 2 39  ? 32.981  -20.939 6.780   1.00 41.49  ? 39  PRO B N   1 
ATOM   3245 C CA  . PRO B 2 39  ? 33.116  -21.809 5.596   1.00 39.96  ? 39  PRO B CA  1 
ATOM   3246 C C   . PRO B 2 39  ? 34.062  -22.982 5.775   1.00 45.49  ? 39  PRO B C   1 
ATOM   3247 O O   . PRO B 2 39  ? 33.781  -24.074 5.255   1.00 45.23  ? 39  PRO B O   1 
ATOM   3248 C CB  . PRO B 2 39  ? 33.648  -20.846 4.530   1.00 39.54  ? 39  PRO B CB  1 
ATOM   3249 C CG  . PRO B 2 39  ? 33.043  -19.538 4.914   1.00 45.65  ? 39  PRO B CG  1 
ATOM   3250 C CD  . PRO B 2 39  ? 32.959  -19.512 6.419   1.00 42.40  ? 39  PRO B CD  1 
ATOM   3251 N N   . ASP B 2 40  ? 35.183  -22.788 6.485   1.00 44.66  ? 40  ASP B N   1 
ATOM   3252 C CA  . ASP B 2 40  ? 36.153  -23.862 6.674   1.00 45.92  ? 40  ASP B CA  1 
ATOM   3253 C C   . ASP B 2 40  ? 35.604  -24.993 7.531   1.00 47.28  ? 40  ASP B C   1 
ATOM   3254 O O   . ASP B 2 40  ? 36.227  -26.061 7.598   1.00 49.96  ? 40  ASP B O   1 
ATOM   3255 C CB  . ASP B 2 40  ? 37.447  -23.311 7.287   1.00 49.94  ? 40  ASP B CB  1 
ATOM   3256 C CG  . ASP B 2 40  ? 37.185  -22.398 8.488   1.00 59.83  ? 40  ASP B CG  1 
ATOM   3257 O OD1 . ASP B 2 40  ? 37.623  -22.735 9.616   1.00 55.59  ? 40  ASP B OD1 1 
ATOM   3258 O OD2 . ASP B 2 40  ? 36.521  -21.343 8.295   1.00 58.51  ? 40  ASP B OD2 1 
ATOM   3259 N N   . GLU B 2 41  ? 34.457  -24.788 8.176   1.00 40.70  ? 41  GLU B N   1 
ATOM   3260 C CA  . GLU B 2 41  ? 33.802  -25.830 8.949   1.00 42.36  ? 41  GLU B CA  1 
ATOM   3261 C C   . GLU B 2 41  ? 32.568  -26.385 8.239   1.00 42.00  ? 41  GLU B C   1 
ATOM   3262 O O   . GLU B 2 41  ? 31.759  -27.076 8.869   1.00 41.68  ? 41  GLU B O   1 
ATOM   3263 C CB  . GLU B 2 41  ? 33.459  -25.301 10.344  1.00 43.22  ? 41  GLU B CB  1 
ATOM   3264 C CG  . GLU B 2 41  ? 34.715  -25.002 11.188  1.00 45.05  ? 41  GLU B CG  1 
ATOM   3265 C CD  . GLU B 2 41  ? 34.411  -24.573 12.613  1.00 46.45  ? 41  GLU B CD  1 
ATOM   3266 O OE1 . GLU B 2 41  ? 33.300  -24.860 13.107  1.00 48.38  ? 41  GLU B OE1 1 
ATOM   3267 O OE2 . GLU B 2 41  ? 35.284  -23.939 13.245  1.00 49.78  ? 41  GLU B OE2 1 
ATOM   3268 N N   . GLN B 2 42  ? 32.412  -26.109 6.937   1.00 39.07  ? 42  GLN B N   1 
ATOM   3269 C CA  . GLN B 2 42  ? 31.258  -26.558 6.170   1.00 39.53  ? 42  GLN B CA  1 
ATOM   3270 C C   . GLN B 2 42  ? 31.702  -27.336 4.941   1.00 39.10  ? 42  GLN B C   1 
ATOM   3271 O O   . GLN B 2 42  ? 32.702  -27.001 4.306   1.00 37.08  ? 42  GLN B O   1 
ATOM   3272 C CB  . GLN B 2 42  ? 30.375  -25.397 5.674   1.00 37.77  ? 42  GLN B CB  1 
ATOM   3273 C CG  . GLN B 2 42  ? 29.924  -24.358 6.681   1.00 40.42  ? 42  GLN B CG  1 
ATOM   3274 C CD  . GLN B 2 42  ? 29.304  -23.148 5.982   1.00 37.99  ? 42  GLN B CD  1 
ATOM   3275 O OE1 . GLN B 2 42  ? 28.660  -23.286 4.939   1.00 38.23  ? 42  GLN B OE1 1 
ATOM   3276 N NE2 . GLN B 2 42  ? 29.529  -21.963 6.533   1.00 34.26  ? 42  GLN B NE2 1 
ATOM   3277 N N   . ARG B 2 43  ? 30.918  -28.353 4.590   1.00 35.83  ? 43  ARG B N   1 
ATOM   3278 C CA  . ARG B 2 43  ? 30.986  -29.012 3.292   1.00 35.50  ? 43  ARG B CA  1 
ATOM   3279 C C   . ARG B 2 43  ? 29.624  -28.896 2.620   1.00 36.37  ? 43  ARG B C   1 
ATOM   3280 O O   . ARG B 2 43  ? 28.591  -29.152 3.256   1.00 35.14  ? 43  ARG B O   1 
ATOM   3281 C CB  . ARG B 2 43  ? 31.379  -30.487 3.428   1.00 33.29  ? 43  ARG B CB  1 
ATOM   3282 C CG  . ARG B 2 43  ? 32.828  -30.722 3.819   1.00 36.03  ? 43  ARG B CG  1 
ATOM   3283 C CD  . ARG B 2 43  ? 33.091  -32.183 4.046   1.00 30.32  ? 43  ARG B CD  1 
ATOM   3284 N NE  . ARG B 2 43  ? 34.508  -32.442 4.220   1.00 33.40  ? 43  ARG B NE  1 
ATOM   3285 C CZ  . ARG B 2 43  ? 35.024  -33.646 4.442   1.00 36.06  ? 43  ARG B CZ  1 
ATOM   3286 N NH1 . ARG B 2 43  ? 34.252  -34.719 4.564   1.00 34.49  ? 43  ARG B NH1 1 
ATOM   3287 N NH2 . ARG B 2 43  ? 36.347  -33.778 4.543   1.00 33.91  ? 43  ARG B NH2 1 
ATOM   3288 N N   . LEU B 2 44  ? 29.617  -28.506 1.347   1.00 31.86  ? 44  LEU B N   1 
ATOM   3289 C CA  . LEU B 2 44  ? 28.384  -28.400 0.573   1.00 36.73  ? 44  LEU B CA  1 
ATOM   3290 C C   . LEU B 2 44  ? 28.392  -29.434 -0.547  1.00 39.67  ? 44  LEU B C   1 
ATOM   3291 O O   . LEU B 2 44  ? 29.426  -29.654 -1.195  1.00 38.50  ? 44  LEU B O   1 
ATOM   3292 C CB  . LEU B 2 44  ? 28.190  -26.982 -0.005  1.00 33.66  ? 44  LEU B CB  1 
ATOM   3293 C CG  . LEU B 2 44  ? 28.018  -25.850 1.023   1.00 33.64  ? 44  LEU B CG  1 
ATOM   3294 C CD1 . LEU B 2 44  ? 27.698  -24.506 0.371   1.00 34.63  ? 44  LEU B CD1 1 
ATOM   3295 C CD2 . LEU B 2 44  ? 26.962  -26.212 2.071   1.00 34.73  ? 44  LEU B CD2 1 
ATOM   3296 N N   . TYR B 2 45  ? 27.232  -30.068 -0.767  1.00 35.40  ? 45  TYR B N   1 
ATOM   3297 C CA  . TYR B 2 45  ? 27.095  -31.157 -1.724  1.00 38.13  ? 45  TYR B CA  1 
ATOM   3298 C C   . TYR B 2 45  ? 25.973  -30.890 -2.715  1.00 41.11  ? 45  TYR B C   1 
ATOM   3299 O O   . TYR B 2 45  ? 24.932  -30.330 -2.354  1.00 42.95  ? 45  TYR B O   1 
ATOM   3300 C CB  . TYR B 2 45  ? 26.796  -32.475 -1.033  1.00 36.92  ? 45  TYR B CB  1 
ATOM   3301 C CG  . TYR B 2 45  ? 27.851  -32.952 -0.082  1.00 36.71  ? 45  TYR B CG  1 
ATOM   3302 C CD1 . TYR B 2 45  ? 27.892  -32.492 1.229   1.00 35.33  ? 45  TYR B CD1 1 
ATOM   3303 C CD2 . TYR B 2 45  ? 28.783  -33.902 -0.475  1.00 38.37  ? 45  TYR B CD2 1 
ATOM   3304 C CE1 . TYR B 2 45  ? 28.850  -32.936 2.110   1.00 32.02  ? 45  TYR B CE1 1 
ATOM   3305 C CE2 . TYR B 2 45  ? 29.749  -34.359 0.406   1.00 35.82  ? 45  TYR B CE2 1 
ATOM   3306 C CZ  . TYR B 2 45  ? 29.773  -33.875 1.695   1.00 34.79  ? 45  TYR B CZ  1 
ATOM   3307 O OH  . TYR B 2 45  ? 30.732  -34.337 2.573   1.00 38.37  ? 45  TYR B OH  1 
ATOM   3308 N N   . LYS B 2 46  ? 26.190  -31.308 -3.963  1.00 41.70  ? 46  LYS B N   1 
ATOM   3309 C CA  . LYS B 2 46  ? 25.122  -31.490 -4.944  1.00 42.42  ? 46  LYS B CA  1 
ATOM   3310 C C   . LYS B 2 46  ? 24.906  -32.994 -5.069  1.00 45.36  ? 46  LYS B C   1 
ATOM   3311 O O   . LYS B 2 46  ? 25.768  -33.707 -5.607  1.00 42.86  ? 46  LYS B O   1 
ATOM   3312 C CB  . LYS B 2 46  ? 25.476  -30.868 -6.293  1.00 42.82  ? 46  LYS B CB  1 
ATOM   3313 C CG  . LYS B 2 46  ? 24.313  -30.868 -7.281  1.00 48.15  ? 46  LYS B CG  1 
ATOM   3314 C CD  . LYS B 2 46  ? 24.654  -30.119 -8.557  1.00 48.51  ? 46  LYS B CD  1 
ATOM   3315 C CE  . LYS B 2 46  ? 23.461  -30.033 -9.480  1.00 48.63  ? 46  LYS B CE  1 
ATOM   3316 N NZ  . LYS B 2 46  ? 23.003  -31.394 -9.861  1.00 54.18  ? 46  LYS B NZ  1 
ATOM   3317 N N   . ASP B 2 47  ? 23.765  -33.471 -4.557  1.00 42.23  ? 47  ASP B N   1 
ATOM   3318 C CA  . ASP B 2 47  ? 23.595  -34.884 -4.242  1.00 41.29  ? 47  ASP B CA  1 
ATOM   3319 C C   . ASP B 2 47  ? 24.826  -35.388 -3.483  1.00 47.40  ? 47  ASP B C   1 
ATOM   3320 O O   . ASP B 2 47  ? 25.117  -34.912 -2.381  1.00 44.97  ? 47  ASP B O   1 
ATOM   3321 C CB  . ASP B 2 47  ? 23.335  -35.691 -5.512  1.00 41.75  ? 47  ASP B CB  1 
ATOM   3322 C CG  . ASP B 2 47  ? 22.027  -35.298 -6.194  1.00 48.97  ? 47  ASP B CG  1 
ATOM   3323 O OD1 . ASP B 2 47  ? 20.953  -35.519 -5.597  1.00 50.18  ? 47  ASP B OD1 1 
ATOM   3324 O OD2 . ASP B 2 47  ? 22.071  -34.745 -7.318  1.00 50.22  ? 47  ASP B OD2 1 
ATOM   3325 N N   . ASP B 2 48  ? 25.584  -36.318 -4.054  1.00 47.88  ? 48  ASP B N   1 
ATOM   3326 C CA  . ASP B 2 48  ? 26.724  -36.875 -3.340  1.00 48.32  ? 48  ASP B CA  1 
ATOM   3327 C C   . ASP B 2 48  ? 28.046  -36.198 -3.676  1.00 43.53  ? 48  ASP B C   1 
ATOM   3328 O O   . ASP B 2 48  ? 29.066  -36.563 -3.096  1.00 39.83  ? 48  ASP B O   1 
ATOM   3329 C CB  . ASP B 2 48  ? 26.843  -38.379 -3.602  1.00 50.97  ? 48  ASP B CB  1 
ATOM   3330 C CG  . ASP B 2 48  ? 25.992  -39.196 -2.659  1.00 61.65  ? 48  ASP B CG  1 
ATOM   3331 O OD1 . ASP B 2 48  ? 25.370  -40.177 -3.121  1.00 70.68  ? 48  ASP B OD1 1 
ATOM   3332 O OD2 . ASP B 2 48  ? 25.930  -38.843 -1.457  1.00 65.26  ? 48  ASP B OD2 1 
ATOM   3333 N N   . GLN B 2 49  ? 28.047  -35.208 -4.563  1.00 42.14  ? 49  GLN B N   1 
ATOM   3334 C CA  . GLN B 2 49  ? 29.274  -34.582 -5.032  1.00 40.64  ? 49  GLN B CA  1 
ATOM   3335 C C   . GLN B 2 49  ? 29.659  -33.408 -4.132  1.00 43.08  ? 49  GLN B C   1 
ATOM   3336 O O   . GLN B 2 49  ? 28.932  -32.409 -4.050  1.00 44.61  ? 49  GLN B O   1 
ATOM   3337 C CB  . GLN B 2 49  ? 29.099  -34.125 -6.478  1.00 40.87  ? 49  GLN B CB  1 
ATOM   3338 C CG  . GLN B 2 49  ? 30.278  -33.369 -7.033  1.00 48.46  ? 49  GLN B CG  1 
ATOM   3339 C CD  . GLN B 2 49  ? 31.493  -34.253 -7.226  1.00 50.32  ? 49  GLN B CD  1 
ATOM   3340 O OE1 . GLN B 2 49  ? 32.472  -34.161 -6.477  1.00 50.37  ? 49  GLN B OE1 1 
ATOM   3341 N NE2 . GLN B 2 49  ? 31.436  -35.118 -8.233  1.00 49.75  ? 49  GLN B NE2 1 
ATOM   3342 N N   . LEU B 2 50  ? 30.802  -33.528 -3.464  1.00 41.63  ? 50  LEU B N   1 
ATOM   3343 C CA  . LEU B 2 50  ? 31.351  -32.413 -2.708  1.00 39.83  ? 50  LEU B CA  1 
ATOM   3344 C C   . LEU B 2 50  ? 31.631  -31.236 -3.637  1.00 42.10  ? 50  LEU B C   1 
ATOM   3345 O O   . LEU B 2 50  ? 32.115  -31.409 -4.759  1.00 46.53  ? 50  LEU B O   1 
ATOM   3346 C CB  . LEU B 2 50  ? 32.637  -32.855 -2.005  1.00 42.89  ? 50  LEU B CB  1 
ATOM   3347 C CG  . LEU B 2 50  ? 33.344  -31.851 -1.103  1.00 37.90  ? 50  LEU B CG  1 
ATOM   3348 C CD1 . LEU B 2 50  ? 32.508  -31.611 0.138   1.00 36.38  ? 50  LEU B CD1 1 
ATOM   3349 C CD2 . LEU B 2 50  ? 34.701  -32.377 -0.739  1.00 36.56  ? 50  LEU B CD2 1 
ATOM   3350 N N   . LEU B 2 51  ? 31.337  -30.030 -3.165  1.00 41.10  ? 51  LEU B N   1 
ATOM   3351 C CA  . LEU B 2 51  ? 31.415  -28.824 -3.979  1.00 42.34  ? 51  LEU B CA  1 
ATOM   3352 C C   . LEU B 2 51  ? 32.599  -27.962 -3.552  1.00 44.55  ? 51  LEU B C   1 
ATOM   3353 O O   . LEU B 2 51  ? 32.803  -27.722 -2.356  1.00 42.48  ? 51  LEU B O   1 
ATOM   3354 C CB  . LEU B 2 51  ? 30.109  -28.033 -3.888  1.00 41.64  ? 51  LEU B CB  1 
ATOM   3355 C CG  . LEU B 2 51  ? 28.894  -28.789 -4.446  1.00 42.07  ? 51  LEU B CG  1 
ATOM   3356 C CD1 . LEU B 2 51  ? 27.686  -27.897 -4.444  1.00 41.26  ? 51  LEU B CD1 1 
ATOM   3357 C CD2 . LEU B 2 51  ? 29.156  -29.316 -5.853  1.00 41.18  ? 51  LEU B CD2 1 
ATOM   3358 N N   . ASP B 2 52  ? 33.370  -27.493 -4.534  1.00 43.95  ? 52  ASP B N   1 
ATOM   3359 C CA  . ASP B 2 52  ? 34.567  -26.706 -4.267  1.00 44.17  ? 52  ASP B CA  1 
ATOM   3360 C C   . ASP B 2 52  ? 34.235  -25.233 -4.057  1.00 45.97  ? 52  ASP B C   1 
ATOM   3361 O O   . ASP B 2 52  ? 33.429  -24.656 -4.795  1.00 46.58  ? 52  ASP B O   1 
ATOM   3362 C CB  . ASP B 2 52  ? 35.555  -26.848 -5.419  1.00 43.69  ? 52  ASP B CB  1 
ATOM   3363 C CG  . ASP B 2 52  ? 36.258  -28.183 -5.418  1.00 43.02  ? 52  ASP B CG  1 
ATOM   3364 O OD1 . ASP B 2 52  ? 36.129  -28.929 -4.427  1.00 43.34  ? 52  ASP B OD1 1 
ATOM   3365 O OD2 . ASP B 2 52  ? 36.946  -28.492 -6.411  1.00 46.92  ? 52  ASP B OD2 1 
ATOM   3366 N N   . ASP B 2 53  ? 34.918  -24.614 -3.079  1.00 43.55  ? 53  ASP B N   1 
ATOM   3367 C CA  . ASP B 2 53  ? 34.624  -23.233 -2.691  1.00 45.61  ? 53  ASP B CA  1 
ATOM   3368 C C   . ASP B 2 53  ? 34.650  -22.282 -3.884  1.00 48.03  ? 53  ASP B C   1 
ATOM   3369 O O   . ASP B 2 53  ? 33.861  -21.330 -3.946  1.00 48.43  ? 53  ASP B O   1 
ATOM   3370 C CB  . ASP B 2 53  ? 35.625  -22.746 -1.631  1.00 45.39  ? 53  ASP B CB  1 
ATOM   3371 C CG  . ASP B 2 53  ? 35.319  -23.270 -0.234  1.00 50.05  ? 53  ASP B CG  1 
ATOM   3372 O OD1 . ASP B 2 53  ? 34.235  -23.872 -0.056  1.00 51.40  ? 53  ASP B OD1 1 
ATOM   3373 O OD2 . ASP B 2 53  ? 36.155  -23.079 0.684   1.00 43.06  ? 53  ASP B OD2 1 
ATOM   3374 N N   . GLY B 2 54  ? 35.557  -22.516 -4.837  1.00 48.21  ? 54  GLY B N   1 
ATOM   3375 C CA  . GLY B 2 54  ? 35.784  -21.586 -5.928  1.00 47.57  ? 54  GLY B CA  1 
ATOM   3376 C C   . GLY B 2 54  ? 35.005  -21.825 -7.204  1.00 50.04  ? 54  GLY B C   1 
ATOM   3377 O O   . GLY B 2 54  ? 35.094  -21.015 -8.134  1.00 50.74  ? 54  GLY B O   1 
ATOM   3378 N N   . LYS B 2 55  ? 34.264  -22.924 -7.298  1.00 48.63  ? 55  LYS B N   1 
ATOM   3379 C CA  . LYS B 2 55  ? 33.390  -23.109 -8.439  1.00 51.05  ? 55  LYS B CA  1 
ATOM   3380 C C   . LYS B 2 55  ? 32.143  -22.246 -8.278  1.00 51.77  ? 55  LYS B C   1 
ATOM   3381 O O   . LYS B 2 55  ? 31.661  -22.008 -7.164  1.00 51.13  ? 55  LYS B O   1 
ATOM   3382 C CB  . LYS B 2 55  ? 32.992  -24.577 -8.586  1.00 51.58  ? 55  LYS B CB  1 
ATOM   3383 C CG  . LYS B 2 55  ? 34.151  -25.517 -8.769  1.00 48.11  ? 55  LYS B CG  1 
ATOM   3384 C CD  . LYS B 2 55  ? 34.453  -25.766 -10.233 1.00 53.43  ? 55  LYS B CD  1 
ATOM   3385 C CE  . LYS B 2 55  ? 35.829  -25.222 -10.613 1.00 58.17  ? 55  LYS B CE  1 
ATOM   3386 N NZ  . LYS B 2 55  ? 36.309  -25.743 -11.924 1.00 67.19  ? 55  LYS B NZ  1 
ATOM   3387 N N   . THR B 2 56  ? 31.626  -21.766 -9.401  1.00 51.71  ? 56  THR B N   1 
ATOM   3388 C CA  . THR B 2 56  ? 30.325  -21.123 -9.350  1.00 52.91  ? 56  THR B CA  1 
ATOM   3389 C C   . THR B 2 56  ? 29.225  -22.181 -9.307  1.00 51.09  ? 56  THR B C   1 
ATOM   3390 O O   . THR B 2 56  ? 29.447  -23.357 -9.614  1.00 52.15  ? 56  THR B O   1 
ATOM   3391 C CB  . THR B 2 56  ? 30.137  -20.198 -10.549 1.00 51.88  ? 56  THR B CB  1 
ATOM   3392 O OG1 . THR B 2 56  ? 29.761  -20.972 -11.692 1.00 50.96  ? 56  THR B OG1 1 
ATOM   3393 C CG2 . THR B 2 56  ? 31.440  -19.485 -10.849 1.00 50.63  ? 56  THR B CG2 1 
ATOM   3394 N N   . LEU B 2 57  ? 28.024  -21.745 -8.909  1.00 52.09  ? 57  LEU B N   1 
ATOM   3395 C CA  . LEU B 2 57  ? 26.889  -22.661 -8.816  1.00 49.46  ? 57  LEU B CA  1 
ATOM   3396 C C   . LEU B 2 57  ? 26.563  -23.262 -10.171 1.00 51.99  ? 57  LEU B C   1 
ATOM   3397 O O   . LEU B 2 57  ? 26.278  -24.463 -10.278 1.00 50.54  ? 57  LEU B O   1 
ATOM   3398 C CB  . LEU B 2 57  ? 25.666  -21.937 -8.254  1.00 49.68  ? 57  LEU B CB  1 
ATOM   3399 C CG  . LEU B 2 57  ? 25.851  -21.333 -6.866  1.00 48.65  ? 57  LEU B CG  1 
ATOM   3400 C CD1 . LEU B 2 57  ? 24.511  -21.080 -6.204  1.00 42.62  ? 57  LEU B CD1 1 
ATOM   3401 C CD2 . LEU B 2 57  ? 26.708  -22.257 -6.015  1.00 43.61  ? 57  LEU B CD2 1 
ATOM   3402 N N   . GLY B 2 58  ? 26.592  -22.434 -11.217 1.00 51.36  ? 58  GLY B N   1 
ATOM   3403 C CA  . GLY B 2 58  ? 26.399  -22.949 -12.556 1.00 49.85  ? 58  GLY B CA  1 
ATOM   3404 C C   . GLY B 2 58  ? 27.440  -23.983 -12.929 1.00 53.57  ? 58  GLY B C   1 
ATOM   3405 O O   . GLY B 2 58  ? 27.115  -25.006 -13.540 1.00 58.33  ? 58  GLY B O   1 
ATOM   3406 N N   . GLU B 2 59  ? 28.708  -23.738 -12.559 1.00 49.29  ? 59  GLU B N   1 
ATOM   3407 C CA  . GLU B 2 59  ? 29.762  -24.707 -12.846 1.00 51.84  ? 59  GLU B CA  1 
ATOM   3408 C C   . GLU B 2 59  ? 29.509  -26.021 -12.128 1.00 53.22  ? 59  GLU B C   1 
ATOM   3409 O O   . GLU B 2 59  ? 29.941  -27.077 -12.607 1.00 55.13  ? 59  GLU B O   1 
ATOM   3410 C CB  . GLU B 2 59  ? 31.141  -24.144 -12.468 1.00 54.35  ? 59  GLU B CB  1 
ATOM   3411 C CG  . GLU B 2 59  ? 31.696  -23.143 -13.484 1.00 51.44  ? 59  GLU B CG  1 
ATOM   3412 C CD  . GLU B 2 59  ? 32.840  -22.288 -12.945 1.00 53.58  ? 59  GLU B CD  1 
ATOM   3413 O OE1 . GLU B 2 59  ? 33.128  -22.372 -11.740 1.00 55.39  ? 59  GLU B OE1 1 
ATOM   3414 O OE2 . GLU B 2 59  ? 33.452  -21.523 -13.729 1.00 59.02  ? 59  GLU B OE2 1 
ATOM   3415 N N   . CYS B 2 60  ? 28.800  -25.974 -10.991 1.00 52.62  ? 60  CYS B N   1 
ATOM   3416 C CA  . CYS B 2 60  ? 28.419  -27.156 -10.222 1.00 51.00  ? 60  CYS B CA  1 
ATOM   3417 C C   . CYS B 2 60  ? 27.183  -27.859 -10.762 1.00 55.07  ? 60  CYS B C   1 
ATOM   3418 O O   . CYS B 2 60  ? 26.831  -28.924 -10.239 1.00 53.88  ? 60  CYS B O   1 
ATOM   3419 C CB  . CYS B 2 60  ? 28.145  -26.790 -8.766  1.00 48.49  ? 60  CYS B CB  1 
ATOM   3420 S SG  . CYS B 2 60  ? 29.549  -26.225 -7.851  1.00 50.09  ? 60  CYS B SG  1 
ATOM   3421 N N   . GLY B 2 61  ? 26.504  -27.283 -11.757 1.00 52.68  ? 61  GLY B N   1 
ATOM   3422 C CA  . GLY B 2 61  ? 25.319  -27.873 -12.342 1.00 49.52  ? 61  GLY B CA  1 
ATOM   3423 C C   . GLY B 2 61  ? 24.018  -27.186 -11.992 1.00 53.36  ? 61  GLY B C   1 
ATOM   3424 O O   . GLY B 2 61  ? 22.983  -27.547 -12.562 1.00 59.19  ? 61  GLY B O   1 
ATOM   3425 N N   . PHE B 2 62  ? 24.018  -26.216 -11.084 1.00 53.52  ? 62  PHE B N   1 
ATOM   3426 C CA  . PHE B 2 62  ? 22.785  -25.517 -10.739 1.00 52.86  ? 62  PHE B CA  1 
ATOM   3427 C C   . PHE B 2 62  ? 22.440  -24.520 -11.834 1.00 57.86  ? 62  PHE B C   1 
ATOM   3428 O O   . PHE B 2 62  ? 23.214  -23.595 -12.104 1.00 60.17  ? 62  PHE B O   1 
ATOM   3429 C CB  . PHE B 2 62  ? 22.920  -24.807 -9.398  1.00 46.79  ? 62  PHE B CB  1 
ATOM   3430 C CG  . PHE B 2 62  ? 23.148  -25.742 -8.268  1.00 48.47  ? 62  PHE B CG  1 
ATOM   3431 C CD1 . PHE B 2 62  ? 22.112  -26.521 -7.786  1.00 46.81  ? 62  PHE B CD1 1 
ATOM   3432 C CD2 . PHE B 2 62  ? 24.405  -25.879 -7.706  1.00 46.24  ? 62  PHE B CD2 1 
ATOM   3433 C CE1 . PHE B 2 62  ? 22.323  -27.402 -6.750  1.00 41.53  ? 62  PHE B CE1 1 
ATOM   3434 C CE2 . PHE B 2 62  ? 24.616  -26.763 -6.674  1.00 43.41  ? 62  PHE B CE2 1 
ATOM   3435 C CZ  . PHE B 2 62  ? 23.576  -27.527 -6.198  1.00 40.32  ? 62  PHE B CZ  1 
ATOM   3436 N N   . THR B 2 63  ? 21.280  -24.707 -12.461 1.00 56.20  ? 63  THR B N   1 
ATOM   3437 C CA  . THR B 2 63  ? 20.794  -23.820 -13.506 1.00 55.41  ? 63  THR B CA  1 
ATOM   3438 C C   . THR B 2 63  ? 19.443  -23.266 -13.086 1.00 53.03  ? 63  THR B C   1 
ATOM   3439 O O   . THR B 2 63  ? 18.673  -23.939 -12.394 1.00 52.38  ? 63  THR B O   1 
ATOM   3440 C CB  . THR B 2 63  ? 20.662  -24.551 -14.851 1.00 54.36  ? 63  THR B CB  1 
ATOM   3441 O OG1 . THR B 2 63  ? 19.317  -25.019 -15.005 1.00 59.01  ? 63  THR B OG1 1 
ATOM   3442 C CG2 . THR B 2 63  ? 21.596  -25.749 -14.904 1.00 52.63  ? 63  THR B CG2 1 
ATOM   3443 N N   . SER B 2 64  ? 19.158  -22.033 -13.512 1.00 55.37  ? 64  SER B N   1 
ATOM   3444 C CA  . SER B 2 64  ? 17.872  -21.425 -13.185 1.00 55.55  ? 64  SER B CA  1 
ATOM   3445 C C   . SER B 2 64  ? 16.706  -22.281 -13.663 1.00 54.98  ? 64  SER B C   1 
ATOM   3446 O O   . SER B 2 64  ? 15.656  -22.314 -13.009 1.00 56.05  ? 64  SER B O   1 
ATOM   3447 C CB  . SER B 2 64  ? 17.775  -20.026 -13.784 1.00 55.99  ? 64  SER B CB  1 
ATOM   3448 O OG  . SER B 2 64  ? 17.742  -20.091 -15.190 1.00 58.43  ? 64  SER B OG  1 
ATOM   3449 N N   . GLN B 2 65  ? 16.871  -22.994 -14.782 1.00 53.95  ? 65  GLN B N   1 
ATOM   3450 C CA  . GLN B 2 65  ? 15.799  -23.850 -15.277 1.00 54.34  ? 65  GLN B CA  1 
ATOM   3451 C C   . GLN B 2 65  ? 15.498  -25.014 -14.340 1.00 54.98  ? 65  GLN B C   1 
ATOM   3452 O O   . GLN B 2 65  ? 14.378  -25.535 -14.365 1.00 57.24  ? 65  GLN B O   1 
ATOM   3453 C CB  . GLN B 2 65  ? 16.138  -24.375 -16.677 1.00 53.68  ? 65  GLN B CB  1 
ATOM   3454 N N   . THR B 2 66  ? 16.452  -25.423 -13.501 1.00 51.68  ? 66  THR B N   1 
ATOM   3455 C CA  . THR B 2 66  ? 16.265  -26.573 -12.618 1.00 50.39  ? 66  THR B CA  1 
ATOM   3456 C C   . THR B 2 66  ? 16.307  -26.205 -11.137 1.00 49.90  ? 66  THR B C   1 
ATOM   3457 O O   . THR B 2 66  ? 16.290  -27.098 -10.283 1.00 47.59  ? 66  THR B O   1 
ATOM   3458 C CB  . THR B 2 66  ? 17.318  -27.643 -12.923 1.00 51.60  ? 66  THR B CB  1 
ATOM   3459 O OG1 . THR B 2 66  ? 18.630  -27.067 -12.822 1.00 53.30  ? 66  THR B OG1 1 
ATOM   3460 C CG2 . THR B 2 66  ? 17.122  -28.179 -14.320 1.00 53.42  ? 66  THR B CG2 1 
ATOM   3461 N N   . ALA B 2 67  ? 16.374  -24.918 -10.814 1.00 51.52  ? 67  ALA B N   1 
ATOM   3462 C CA  . ALA B 2 67  ? 16.380  -24.429 -9.442  1.00 42.02  ? 67  ALA B CA  1 
ATOM   3463 C C   . ALA B 2 67  ? 15.330  -23.317 -9.314  1.00 41.81  ? 67  ALA B C   1 
ATOM   3464 O O   . ALA B 2 67  ? 15.638  -22.174 -8.981  1.00 40.85  ? 67  ALA B O   1 
ATOM   3465 C CB  . ALA B 2 67  ? 17.763  -23.963 -9.036  1.00 41.08  ? 67  ALA B CB  1 
ATOM   3466 N N   . ARG B 2 68  ? 14.092  -23.631 -9.698  1.00 36.93  ? 68  ARG B N   1 
ATOM   3467 C CA  . ARG B 2 68  ? 13.025  -22.638 -9.734  1.00 41.43  ? 68  ARG B CA  1 
ATOM   3468 C C   . ARG B 2 68  ? 12.443  -22.386 -8.342  1.00 38.61  ? 68  ARG B C   1 
ATOM   3469 O O   . ARG B 2 68  ? 12.535  -23.239 -7.455  1.00 37.70  ? 68  ARG B O   1 
ATOM   3470 C CB  . ARG B 2 68  ? 11.939  -23.092 -10.699 1.00 41.02  ? 68  ARG B CB  1 
ATOM   3471 C CG  . ARG B 2 68  ? 12.396  -23.075 -12.155 1.00 49.25  ? 68  ARG B CG  1 
ATOM   3472 C CD  . ARG B 2 68  ? 11.589  -24.050 -13.028 1.00 59.59  ? 68  ARG B CD  1 
ATOM   3473 N NE  . ARG B 2 68  ? 10.761  -23.374 -14.024 1.00 67.67  ? 68  ARG B NE  1 
ATOM   3474 C CZ  . ARG B 2 68  ? 11.232  -22.750 -15.101 1.00 68.04  ? 68  ARG B CZ  1 
ATOM   3475 N NH1 . ARG B 2 68  ? 12.536  -22.653 -15.339 1.00 67.66  ? 68  ARG B NH1 1 
ATOM   3476 N NH2 . ARG B 2 68  ? 10.377  -22.207 -15.961 1.00 63.59  ? 68  ARG B NH2 1 
ATOM   3477 N N   . PRO B 2 69  ? 11.850  -21.207 -8.115  1.00 36.40  ? 69  PRO B N   1 
ATOM   3478 C CA  . PRO B 2 69  ? 11.385  -20.884 -6.753  1.00 35.44  ? 69  PRO B CA  1 
ATOM   3479 C C   . PRO B 2 69  ? 10.375  -21.878 -6.197  1.00 35.87  ? 69  PRO B C   1 
ATOM   3480 O O   . PRO B 2 69  ? 10.395  -22.151 -4.989  1.00 34.01  ? 69  PRO B O   1 
ATOM   3481 C CB  . PRO B 2 69  ? 10.788  -19.476 -6.896  1.00 35.77  ? 69  PRO B CB  1 
ATOM   3482 C CG  . PRO B 2 69  ? 10.905  -19.106 -8.290  1.00 36.69  ? 69  PRO B CG  1 
ATOM   3483 C CD  . PRO B 2 69  ? 11.750  -20.060 -9.029  1.00 35.09  ? 69  PRO B CD  1 
ATOM   3484 N N   . GLN B 2 70  ? 9.515   -22.448 -7.046  1.00 34.40  ? 70  GLN B N   1 
ATOM   3485 C CA  . GLN B 2 70  ? 8.517   -23.434 -6.644  1.00 34.37  ? 70  GLN B CA  1 
ATOM   3486 C C   . GLN B 2 70  ? 9.073   -24.849 -6.615  1.00 34.08  ? 70  GLN B C   1 
ATOM   3487 O O   . GLN B 2 70  ? 8.368   -25.770 -6.192  1.00 35.02  ? 70  GLN B O   1 
ATOM   3488 C CB  . GLN B 2 70  ? 7.305   -23.387 -7.594  1.00 36.25  ? 70  GLN B CB  1 
ATOM   3489 C CG  . GLN B 2 70  ? 7.622   -23.749 -9.076  1.00 37.68  ? 70  GLN B CG  1 
ATOM   3490 C CD  . GLN B 2 70  ? 8.218   -22.588 -9.871  1.00 41.89  ? 70  GLN B CD  1 
ATOM   3491 O OE1 . GLN B 2 70  ? 8.990   -21.786 -9.345  1.00 42.66  ? 70  GLN B OE1 1 
ATOM   3492 N NE2 . GLN B 2 70  ? 7.828   -22.477 -11.145 1.00 51.23  ? 70  GLN B NE2 1 
ATOM   3493 N N   . ALA B 2 71  ? 10.301  -25.051 -7.080  1.00 34.96  ? 71  ALA B N   1 
ATOM   3494 C CA  . ALA B 2 71  ? 10.941  -26.366 -7.062  1.00 34.72  ? 71  ALA B CA  1 
ATOM   3495 C C   . ALA B 2 71  ? 12.429  -26.184 -6.795  1.00 36.80  ? 71  ALA B C   1 
ATOM   3496 O O   . ALA B 2 71  ? 13.272  -26.494 -7.645  1.00 37.34  ? 71  ALA B O   1 
ATOM   3497 C CB  . ALA B 2 71  ? 10.691  -27.097 -8.378  1.00 31.72  ? 71  ALA B CB  1 
ATOM   3498 N N   . PRO B 2 72  ? 12.786  -25.660 -5.616  1.00 33.51  ? 72  PRO B N   1 
ATOM   3499 C CA  . PRO B 2 72  ? 14.195  -25.344 -5.346  1.00 34.68  ? 72  PRO B CA  1 
ATOM   3500 C C   . PRO B 2 72  ? 15.076  -26.579 -5.402  1.00 36.70  ? 72  PRO B C   1 
ATOM   3501 O O   . PRO B 2 72  ? 14.678  -27.673 -4.981  1.00 35.25  ? 72  PRO B O   1 
ATOM   3502 C CB  . PRO B 2 72  ? 14.166  -24.744 -3.932  1.00 34.11  ? 72  PRO B CB  1 
ATOM   3503 C CG  . PRO B 2 72  ? 12.917  -25.283 -3.325  1.00 33.88  ? 72  PRO B CG  1 
ATOM   3504 C CD  . PRO B 2 72  ? 11.932  -25.333 -4.461  1.00 33.99  ? 72  PRO B CD  1 
ATOM   3505 N N   . ALA B 2 73  ? 16.283  -26.389 -5.931  1.00 36.49  ? 73  ALA B N   1 
ATOM   3506 C CA  . ALA B 2 73  ? 17.289  -27.437 -5.909  1.00 35.11  ? 73  ALA B CA  1 
ATOM   3507 C C   . ALA B 2 73  ? 17.845  -27.595 -4.499  1.00 32.01  ? 73  ALA B C   1 
ATOM   3508 O O   . ALA B 2 73  ? 18.007  -26.617 -3.769  1.00 32.56  ? 73  ALA B O   1 
ATOM   3509 C CB  . ALA B 2 73  ? 18.411  -27.109 -6.891  1.00 34.99  ? 73  ALA B CB  1 
ATOM   3510 N N   . THR B 2 74  ? 18.161  -28.839 -4.126  1.00 31.40  ? 74  THR B N   1 
ATOM   3511 C CA  . THR B 2 74  ? 18.708  -29.142 -2.805  1.00 31.88  ? 74  THR B CA  1 
ATOM   3512 C C   . THR B 2 74  ? 20.240  -29.095 -2.790  1.00 33.24  ? 74  THR B C   1 
ATOM   3513 O O   . THR B 2 74  ? 20.909  -29.602 -3.691  1.00 32.64  ? 74  THR B O   1 
ATOM   3514 C CB  . THR B 2 74  ? 18.220  -30.516 -2.331  1.00 33.29  ? 74  THR B CB  1 
ATOM   3515 O OG1 . THR B 2 74  ? 16.826  -30.444 -2.002  1.00 34.58  ? 74  THR B OG1 1 
ATOM   3516 C CG2 . THR B 2 74  ? 18.978  -30.971 -1.087  1.00 34.30  ? 74  THR B CG2 1 
ATOM   3517 N N   . VAL B 2 75  ? 20.786  -28.478 -1.750  1.00 32.93  ? 75  VAL B N   1 
ATOM   3518 C CA  . VAL B 2 75  ? 22.219  -28.463 -1.464  1.00 33.85  ? 75  VAL B CA  1 
ATOM   3519 C C   . VAL B 2 75  ? 22.428  -29.088 -0.091  1.00 33.74  ? 75  VAL B C   1 
ATOM   3520 O O   . VAL B 2 75  ? 21.928  -28.566 0.914   1.00 32.13  ? 75  VAL B O   1 
ATOM   3521 C CB  . VAL B 2 75  ? 22.785  -27.034 -1.486  1.00 33.85  ? 75  VAL B CB  1 
ATOM   3522 C CG1 . VAL B 2 75  ? 24.259  -27.032 -1.075  1.00 33.68  ? 75  VAL B CG1 1 
ATOM   3523 C CG2 . VAL B 2 75  ? 22.595  -26.400 -2.862  1.00 34.17  ? 75  VAL B CG2 1 
ATOM   3524 N N   . GLY B 2 76  ? 23.172  -30.192 -0.037  1.00 32.48  ? 76  GLY B N   1 
ATOM   3525 C CA  . GLY B 2 76  ? 23.468  -30.809 1.246   1.00 31.93  ? 76  GLY B CA  1 
ATOM   3526 C C   . GLY B 2 76  ? 24.520  -30.030 2.020   1.00 34.54  ? 76  GLY B C   1 
ATOM   3527 O O   . GLY B 2 76  ? 25.407  -29.396 1.447   1.00 35.79  ? 76  GLY B O   1 
ATOM   3528 N N   . LEU B 2 77  ? 24.421  -30.079 3.350   1.00 32.48  ? 77  LEU B N   1 
ATOM   3529 C CA  . LEU B 2 77  ? 25.374  -29.398 4.221   1.00 33.12  ? 77  LEU B CA  1 
ATOM   3530 C C   . LEU B 2 77  ? 25.864  -30.346 5.309   1.00 32.13  ? 77  LEU B C   1 
ATOM   3531 O O   . LEU B 2 77  ? 25.059  -30.991 5.983   1.00 29.04  ? 77  LEU B O   1 
ATOM   3532 C CB  . LEU B 2 77  ? 24.747  -28.142 4.854   1.00 33.28  ? 77  LEU B CB  1 
ATOM   3533 C CG  . LEU B 2 77  ? 25.435  -27.576 6.102   1.00 31.55  ? 77  LEU B CG  1 
ATOM   3534 C CD1 . LEU B 2 77  ? 26.789  -26.966 5.738   1.00 32.81  ? 77  LEU B CD1 1 
ATOM   3535 C CD2 . LEU B 2 77  ? 24.556  -26.547 6.814   1.00 29.73  ? 77  LEU B CD2 1 
ATOM   3536 N N   . ALA B 2 78  ? 27.188  -30.415 5.493   1.00 35.40  ? 78  ALA B N   1 
ATOM   3537 C CA  . ALA B 2 78  ? 27.795  -31.148 6.601   1.00 33.73  ? 78  ALA B CA  1 
ATOM   3538 C C   . ALA B 2 78  ? 28.746  -30.232 7.367   1.00 33.71  ? 78  ALA B C   1 
ATOM   3539 O O   . ALA B 2 78  ? 29.500  -29.462 6.766   1.00 34.97  ? 78  ALA B O   1 
ATOM   3540 C CB  . ALA B 2 78  ? 28.538  -32.403 6.100   1.00 29.68  ? 78  ALA B CB  1 
ATOM   3541 N N   . PHE B 2 79  ? 28.705  -30.310 8.693   1.00 31.32  ? 79  PHE B N   1 
ATOM   3542 C CA  . PHE B 2 79  ? 29.600  -29.531 9.537   1.00 38.44  ? 79  PHE B CA  1 
ATOM   3543 C C   . PHE B 2 79  ? 30.792  -30.359 10.009  1.00 40.47  ? 79  PHE B C   1 
ATOM   3544 O O   . PHE B 2 79  ? 30.703  -31.580 10.176  1.00 40.72  ? 79  PHE B O   1 
ATOM   3545 C CB  . PHE B 2 79  ? 28.874  -28.990 10.769  1.00 38.11  ? 79  PHE B CB  1 
ATOM   3546 C CG  . PHE B 2 79  ? 27.955  -27.863 10.481  1.00 36.27  ? 79  PHE B CG  1 
ATOM   3547 C CD1 . PHE B 2 79  ? 28.219  -26.988 9.437   1.00 34.87  ? 79  PHE B CD1 1 
ATOM   3548 C CD2 . PHE B 2 79  ? 26.820  -27.672 11.261  1.00 34.81  ? 79  PHE B CD2 1 
ATOM   3549 C CE1 . PHE B 2 79  ? 27.372  -25.940 9.184   1.00 34.88  ? 79  PHE B CE1 1 
ATOM   3550 C CE2 . PHE B 2 79  ? 25.966  -26.637 11.010  1.00 32.17  ? 79  PHE B CE2 1 
ATOM   3551 C CZ  . PHE B 2 79  ? 26.232  -25.767 9.972   1.00 33.42  ? 79  PHE B CZ  1 
ATOM   3552 N N   . ARG B 2 80  ? 31.909  -29.677 10.251  1.00 39.97  ? 80  ARG B N   1 
ATOM   3553 C CA  . ARG B 2 80  ? 33.021  -30.336 10.917  1.00 45.29  ? 80  ARG B CA  1 
ATOM   3554 C C   . ARG B 2 80  ? 32.605  -30.765 12.325  1.00 47.24  ? 80  ARG B C   1 
ATOM   3555 O O   . ARG B 2 80  ? 31.884  -30.045 13.026  1.00 46.28  ? 80  ARG B O   1 
ATOM   3556 C CB  . ARG B 2 80  ? 34.234  -29.407 10.970  1.00 45.83  ? 80  ARG B CB  1 
ATOM   3557 C CG  . ARG B 2 80  ? 35.470  -30.080 11.517  1.00 46.12  ? 80  ARG B CG  1 
ATOM   3558 C CD  . ARG B 2 80  ? 36.560  -29.070 11.781  1.00 54.84  ? 80  ARG B CD  1 
ATOM   3559 N NE  . ARG B 2 80  ? 37.130  -28.563 10.539  1.00 61.27  ? 80  ARG B NE  1 
ATOM   3560 C CZ  . ARG B 2 80  ? 38.252  -29.013 9.993   1.00 60.59  ? 80  ARG B CZ  1 
ATOM   3561 N NH1 . ARG B 2 80  ? 38.982  -29.951 10.586  1.00 59.08  ? 80  ARG B NH1 1 
ATOM   3562 N NH2 . ARG B 2 80  ? 38.649  -28.512 8.824   1.00 59.09  ? 80  ARG B NH2 1 
ATOM   3563 N N   . ALA B 2 81  ? 33.017  -31.972 12.726  1.00 50.80  ? 81  ALA B N   1 
ATOM   3564 C CA  . ALA B 2 81  ? 32.637  -32.409 14.062  1.00 51.15  ? 81  ALA B CA  1 
ATOM   3565 C C   . ALA B 2 81  ? 33.747  -32.127 15.067  1.00 55.79  ? 81  ALA B C   1 
ATOM   3566 O O   . ALA B 2 81  ? 33.639  -31.153 15.815  1.00 65.39  ? 81  ALA B O   1 
ATOM   3567 C CB  . ALA B 2 81  ? 32.276  -33.897 14.059  1.00 47.82  ? 81  ALA B CB  1 
ATOM   3568 N N   . ASP B 2 82  ? 34.853  -32.876 15.065  1.00 50.20  ? 82  ASP B N   1 
ATOM   3569 C CA  . ASP B 2 82  ? 36.006  -32.440 15.850  1.00 56.82  ? 82  ASP B CA  1 
ATOM   3570 C C   . ASP B 2 82  ? 37.251  -32.282 14.992  1.00 55.56  ? 82  ASP B C   1 
ATOM   3571 O O   . ASP B 2 82  ? 37.570  -31.163 14.588  1.00 56.72  ? 82  ASP B O   1 
ATOM   3572 C CB  . ASP B 2 82  ? 36.275  -33.419 16.992  1.00 59.28  ? 82  ASP B CB  1 
ATOM   3573 C CG  . ASP B 2 82  ? 35.182  -33.418 18.036  1.00 60.30  ? 82  ASP B CG  1 
ATOM   3574 O OD1 . ASP B 2 82  ? 34.735  -32.322 18.442  1.00 60.09  ? 82  ASP B OD1 1 
ATOM   3575 O OD2 . ASP B 2 82  ? 34.775  -34.523 18.453  1.00 65.39  ? 82  ASP B OD2 1 
ATOM   3576 N N   . ASP B 2 83  ? 37.878  -33.376 14.586  1.00 56.15  ? 83  ASP B N   1 
ATOM   3577 C CA  . ASP B 2 83  ? 39.000  -33.311 13.671  1.00 57.06  ? 83  ASP B CA  1 
ATOM   3578 C C   . ASP B 2 83  ? 38.564  -33.697 12.289  1.00 56.94  ? 83  ASP B C   1 
ATOM   3579 O O   . ASP B 2 83  ? 39.325  -33.535 11.329  1.00 62.80  ? 83  ASP B O   1 
ATOM   3580 C CB  . ASP B 2 83  ? 40.121  -34.250 14.106  1.00 57.38  ? 83  ASP B CB  1 
ATOM   3581 C CG  . ASP B 2 83  ? 40.379  -34.190 15.574  1.00 67.27  ? 83  ASP B CG  1 
ATOM   3582 O OD1 . ASP B 2 83  ? 40.224  -33.088 16.151  1.00 66.92  ? 83  ASP B OD1 1 
ATOM   3583 O OD2 . ASP B 2 83  ? 40.736  -35.250 16.140  1.00 72.81  ? 83  ASP B OD2 1 
ATOM   3584 N N   . THR B 2 84  ? 37.364  -34.233 12.198  1.00 48.85  ? 84  THR B N   1 
ATOM   3585 C CA  . THR B 2 84  ? 36.828  -34.823 11.003  1.00 43.99  ? 84  THR B CA  1 
ATOM   3586 C C   . THR B 2 84  ? 35.453  -34.228 10.803  1.00 42.63  ? 84  THR B C   1 
ATOM   3587 O O   . THR B 2 84  ? 34.920  -33.536 11.679  1.00 44.64  ? 84  THR B O   1 
ATOM   3588 C CB  . THR B 2 84  ? 36.790  -36.354 11.115  1.00 41.88  ? 84  THR B CB  1 
ATOM   3589 O OG1 . THR B 2 84  ? 36.053  -36.724 12.283  1.00 39.02  ? 84  THR B OG1 1 
ATOM   3590 C CG2 . THR B 2 84  ? 38.220  -36.925 11.223  1.00 36.94  ? 84  THR B CG2 1 
ATOM   3591 N N   . PHE B 2 85  ? 34.902  -34.466 9.622   1.00 40.81  ? 85  PHE B N   1 
ATOM   3592 C CA  . PHE B 2 85  ? 33.585  -33.961 9.285   1.00 38.31  ? 85  PHE B CA  1 
ATOM   3593 C C   . PHE B 2 85  ? 32.538  -35.029 9.559   1.00 36.26  ? 85  PHE B C   1 
ATOM   3594 O O   . PHE B 2 85  ? 32.782  -36.233 9.403   1.00 35.17  ? 85  PHE B O   1 
ATOM   3595 C CB  . PHE B 2 85  ? 33.532  -33.531 7.816   1.00 35.44  ? 85  PHE B CB  1 
ATOM   3596 C CG  . PHE B 2 85  ? 34.083  -32.158 7.569   1.00 37.69  ? 85  PHE B CG  1 
ATOM   3597 C CD1 . PHE B 2 85  ? 35.447  -31.960 7.411   1.00 37.13  ? 85  PHE B CD1 1 
ATOM   3598 C CD2 . PHE B 2 85  ? 33.230  -31.057 7.495   1.00 37.91  ? 85  PHE B CD2 1 
ATOM   3599 C CE1 . PHE B 2 85  ? 35.955  -30.689 7.200   1.00 40.86  ? 85  PHE B CE1 1 
ATOM   3600 C CE2 . PHE B 2 85  ? 33.733  -29.779 7.268   1.00 39.57  ? 85  PHE B CE2 1 
ATOM   3601 C CZ  . PHE B 2 85  ? 35.097  -29.593 7.125   1.00 40.25  ? 85  PHE B CZ  1 
ATOM   3602 N N   . GLU B 2 86  ? 31.370  -34.579 9.988   1.00 36.86  ? 86  GLU B N   1 
ATOM   3603 C CA  . GLU B 2 86  ? 30.244  -35.489 10.087  1.00 37.55  ? 86  GLU B CA  1 
ATOM   3604 C C   . GLU B 2 86  ? 29.857  -35.965 8.689   1.00 35.95  ? 86  GLU B C   1 
ATOM   3605 O O   . GLU B 2 86  ? 30.106  -35.290 7.682   1.00 32.43  ? 86  GLU B O   1 
ATOM   3606 C CB  . GLU B 2 86  ? 29.063  -34.798 10.764  1.00 33.03  ? 86  GLU B CB  1 
ATOM   3607 C CG  . GLU B 2 86  ? 28.389  -33.804 9.828   1.00 34.88  ? 86  GLU B CG  1 
ATOM   3608 C CD  . GLU B 2 86  ? 27.389  -32.881 10.503  1.00 35.11  ? 86  GLU B CD  1 
ATOM   3609 O OE1 . GLU B 2 86  ? 27.302  -32.844 11.758  1.00 35.84  ? 86  GLU B OE1 1 
ATOM   3610 O OE2 . GLU B 2 86  ? 26.700  -32.181 9.747   1.00 35.42  ? 86  GLU B OE2 1 
ATOM   3611 N N   . ALA B 2 87  ? 29.277  -37.158 8.632   1.00 34.79  ? 87  ALA B N   1 
ATOM   3612 C CA  . ALA B 2 87  ? 28.713  -37.655 7.387   1.00 35.35  ? 87  ALA B CA  1 
ATOM   3613 C C   . ALA B 2 87  ? 27.530  -36.798 6.968   1.00 33.74  ? 87  ALA B C   1 
ATOM   3614 O O   . ALA B 2 87  ? 26.765  -36.326 7.811   1.00 35.53  ? 87  ALA B O   1 
ATOM   3615 C CB  . ALA B 2 87  ? 28.274  -39.109 7.548   1.00 36.96  ? 87  ALA B CB  1 
ATOM   3616 N N   . LEU B 2 88  ? 27.392  -36.589 5.657   1.00 34.59  ? 88  LEU B N   1 
ATOM   3617 C CA  . LEU B 2 88  ? 26.245  -35.868 5.115   1.00 34.46  ? 88  LEU B CA  1 
ATOM   3618 C C   . LEU B 2 88  ? 24.963  -36.595 5.472   1.00 33.38  ? 88  LEU B C   1 
ATOM   3619 O O   . LEU B 2 88  ? 24.761  -37.740 5.067   1.00 34.46  ? 88  LEU B O   1 
ATOM   3620 C CB  . LEU B 2 88  ? 26.361  -35.743 3.597   1.00 34.02  ? 88  LEU B CB  1 
ATOM   3621 C CG  . LEU B 2 88  ? 25.159  -35.119 2.884   1.00 35.22  ? 88  LEU B CG  1 
ATOM   3622 C CD1 . LEU B 2 88  ? 25.063  -33.636 3.211   1.00 33.83  ? 88  LEU B CD1 1 
ATOM   3623 C CD2 . LEU B 2 88  ? 25.190  -35.348 1.366   1.00 32.88  ? 88  LEU B CD2 1 
ATOM   3624 N N   . CYS B 2 89  ? 24.088  -35.937 6.224   1.00 35.89  ? 89  CYS B N   1 
ATOM   3625 C CA  . CYS B 2 89  ? 22.859  -36.579 6.680   1.00 37.92  ? 89  CYS B CA  1 
ATOM   3626 C C   . CYS B 2 89  ? 21.696  -35.602 6.589   1.00 36.14  ? 89  CYS B C   1 
ATOM   3627 O O   . CYS B 2 89  ? 21.691  -34.582 7.284   1.00 39.10  ? 89  CYS B O   1 
ATOM   3628 C CB  . CYS B 2 89  ? 23.006  -37.094 8.112   1.00 34.62  ? 89  CYS B CB  1 
ATOM   3629 S SG  . CYS B 2 89  ? 21.581  -38.070 8.585   1.00 50.19  ? 89  CYS B SG  1 
ATOM   3630 N N   . ILE B 2 90  ? 20.710  -35.926 5.751   1.00 38.32  ? 90  ILE B N   1 
ATOM   3631 C CA  . ILE B 2 90  ? 19.527  -35.092 5.547   1.00 38.36  ? 90  ILE B CA  1 
ATOM   3632 C C   . ILE B 2 90  ? 18.304  -35.885 5.983   1.00 40.55  ? 90  ILE B C   1 
ATOM   3633 O O   . ILE B 2 90  ? 18.022  -36.959 5.435   1.00 38.39  ? 90  ILE B O   1 
ATOM   3634 C CB  . ILE B 2 90  ? 19.387  -34.631 4.088   1.00 35.49  ? 90  ILE B CB  1 
ATOM   3635 C CG1 . ILE B 2 90  ? 20.571  -33.749 3.676   1.00 35.73  ? 90  ILE B CG1 1 
ATOM   3636 C CG2 . ILE B 2 90  ? 18.085  -33.871 3.902   1.00 34.72  ? 90  ILE B CG2 1 
ATOM   3637 C CD1 . ILE B 2 90  ? 20.630  -33.462 2.176   1.00 31.34  ? 90  ILE B CD1 1 
ATOM   3638 N N   . GLU B 2 91  ? 17.576  -35.354 6.963   1.00 41.75  ? 91  GLU B N   1 
ATOM   3639 C CA  . GLU B 2 91  ? 16.372  -36.023 7.457   1.00 40.54  ? 91  GLU B CA  1 
ATOM   3640 C C   . GLU B 2 91  ? 15.216  -35.769 6.496   1.00 42.05  ? 91  GLU B C   1 
ATOM   3641 O O   . GLU B 2 91  ? 14.977  -34.617 6.117   1.00 41.63  ? 91  GLU B O   1 
ATOM   3642 C CB  . GLU B 2 91  ? 16.030  -35.528 8.854   1.00 40.40  ? 91  GLU B CB  1 
ATOM   3643 C CG  . GLU B 2 91  ? 14.771  -36.114 9.441   1.00 46.01  ? 91  GLU B CG  1 
ATOM   3644 C CD  . GLU B 2 91  ? 14.954  -37.545 9.911   1.00 58.45  ? 91  GLU B CD  1 
ATOM   3645 O OE1 . GLU B 2 91  ? 13.958  -38.140 10.413  1.00 55.86  ? 91  GLU B OE1 1 
ATOM   3646 O OE2 . GLU B 2 91  ? 16.096  -38.064 9.784   1.00 57.74  ? 91  GLU B OE2 1 
ATOM   3647 N N   . PRO B 2 92  ? 14.527  -36.812 6.033   1.00 44.94  ? 92  PRO B N   1 
ATOM   3648 C CA  . PRO B 2 92  ? 13.403  -36.610 5.107   1.00 42.34  ? 92  PRO B CA  1 
ATOM   3649 C C   . PRO B 2 92  ? 12.248  -35.877 5.763   1.00 41.84  ? 92  PRO B C   1 
ATOM   3650 O O   . PRO B 2 92  ? 11.993  -36.017 6.962   1.00 40.47  ? 92  PRO B O   1 
ATOM   3651 C CB  . PRO B 2 92  ? 12.988  -38.040 4.728   1.00 39.09  ? 92  PRO B CB  1 
ATOM   3652 C CG  . PRO B 2 92  ? 13.514  -38.891 5.837   1.00 43.38  ? 92  PRO B CG  1 
ATOM   3653 C CD  . PRO B 2 92  ? 14.809  -38.237 6.256   1.00 43.72  ? 92  PRO B CD  1 
ATOM   3654 N N   . PHE B 2 93  ? 11.527  -35.109 4.948   1.00 39.88  ? 93  PHE B N   1 
ATOM   3655 C CA  . PHE B 2 93  ? 10.279  -34.529 5.412   1.00 38.74  ? 93  PHE B CA  1 
ATOM   3656 C C   . PHE B 2 93  ? 9.257   -35.632 5.663   1.00 41.30  ? 93  PHE B C   1 
ATOM   3657 O O   . PHE B 2 93  ? 9.394   -36.772 5.199   1.00 41.98  ? 93  PHE B O   1 
ATOM   3658 C CB  . PHE B 2 93  ? 9.720   -33.528 4.397   1.00 39.24  ? 93  PHE B CB  1 
ATOM   3659 C CG  . PHE B 2 93  ? 10.648  -32.385 4.082   1.00 37.01  ? 93  PHE B CG  1 
ATOM   3660 C CD1 . PHE B 2 93  ? 11.381  -31.762 5.078   1.00 36.19  ? 93  PHE B CD1 1 
ATOM   3661 C CD2 . PHE B 2 93  ? 10.789  -31.932 2.779   1.00 36.23  ? 93  PHE B CD2 1 
ATOM   3662 C CE1 . PHE B 2 93  ? 12.229  -30.697 4.781   1.00 34.31  ? 93  PHE B CE1 1 
ATOM   3663 C CE2 . PHE B 2 93  ? 11.647  -30.872 2.477   1.00 32.68  ? 93  PHE B CE2 1 
ATOM   3664 C CZ  . PHE B 2 93  ? 12.366  -30.259 3.477   1.00 30.69  ? 93  PHE B CZ  1 
ATOM   3665 N N   . SER B 2 94  ? 8.214   -35.284 6.410   1.00 43.51  ? 94  SER B N   1 
ATOM   3666 C CA  . SER B 2 94  ? 7.151   -36.236 6.680   1.00 47.03  ? 94  SER B CA  1 
ATOM   3667 C C   . SER B 2 94  ? 6.458   -36.624 5.379   1.00 48.57  ? 94  SER B C   1 
ATOM   3668 O O   . SER B 2 94  ? 6.795   -36.115 4.307   1.00 50.17  ? 94  SER B O   1 
ATOM   3669 C CB  . SER B 2 94  ? 6.152   -35.650 7.681   1.00 49.57  ? 94  SER B CB  1 
ATOM   3670 O OG  . SER B 2 94  ? 5.503   -34.501 7.149   1.00 48.94  ? 94  SER B OG  1 
ATOM   3671 N N   . SER B 2 95  ? 5.495   -37.524 5.451   1.00 51.87  ? 95  SER B N   1 
ATOM   3672 C CA  . SER B 2 95  ? 4.862   -37.981 4.229   1.00 58.77  ? 95  SER B CA  1 
ATOM   3673 C C   . SER B 2 95  ? 3.350   -37.848 4.337   1.00 63.20  ? 95  SER B C   1 
ATOM   3674 O O   . SER B 2 95  ? 2.780   -38.002 5.423   1.00 65.94  ? 95  SER B O   1 
ATOM   3675 C CB  . SER B 2 95  ? 5.242   -39.438 3.956   1.00 64.14  ? 95  SER B CB  1 
ATOM   3676 O OG  . SER B 2 95  ? 5.138   -40.177 5.160   1.00 70.57  ? 95  SER B OG  1 
ATOM   3677 N N   . PRO B 2 96  ? 2.675   -37.551 3.230   1.00 66.53  ? 96  PRO B N   1 
ATOM   3678 C CA  . PRO B 2 96  ? 1.216   -37.407 3.266   1.00 70.20  ? 96  PRO B CA  1 
ATOM   3679 C C   . PRO B 2 96  ? 0.546   -38.761 3.399   1.00 75.51  ? 96  PRO B C   1 
ATOM   3680 O O   . PRO B 2 96  ? 1.211   -39.802 3.288   1.00 75.07  ? 96  PRO B O   1 
ATOM   3681 C CB  . PRO B 2 96  ? 0.891   -36.747 1.915   1.00 65.35  ? 96  PRO B CB  1 
ATOM   3682 C CG  . PRO B 2 96  ? 1.993   -37.166 1.021   1.00 64.71  ? 96  PRO B CG  1 
ATOM   3683 C CD  . PRO B 2 96  ? 3.227   -37.242 1.899   1.00 64.84  ? 96  PRO B CD  1 
ATOM   3684 N N   . PRO B 2 97  ? -0.771  -38.793 3.661   1.00 82.81  ? 97  PRO B N   1 
ATOM   3685 C CA  . PRO B 2 97  ? -1.495  -40.069 3.695   1.00 86.02  ? 97  PRO B CA  1 
ATOM   3686 C C   . PRO B 2 97  ? -1.893  -40.545 2.296   1.00 87.54  ? 97  PRO B C   1 
ATOM   3687 O O   . PRO B 2 97  ? -2.516  -41.603 2.162   1.00 98.28  ? 97  PRO B O   1 
ATOM   3688 C CB  . PRO B 2 97  ? -2.724  -39.738 4.537   1.00 87.93  ? 97  PRO B CB  1 
ATOM   3689 C CG  . PRO B 2 97  ? -2.982  -38.292 4.238   1.00 84.75  ? 97  PRO B CG  1 
ATOM   3690 C CD  . PRO B 2 97  ? -1.631  -37.660 4.058   1.00 79.51  ? 97  PRO B CD  1 
ATOM   3691 N N   . MET C 3 26  ? 16.146  -10.685 9.575   1.00 43.41  ? 17  MET C N   1 
ATOM   3692 C CA  . MET C 3 26  ? 16.443  -10.942 8.159   1.00 42.45  ? 17  MET C CA  1 
ATOM   3693 C C   . MET C 3 26  ? 15.974  -12.317 7.656   1.00 41.16  ? 17  MET C C   1 
ATOM   3694 O O   . MET C 3 26  ? 15.344  -12.418 6.606   1.00 42.60  ? 17  MET C O   1 
ATOM   3695 C CB  . MET C 3 26  ? 17.934  -10.814 7.897   1.00 46.11  ? 17  MET C CB  1 
ATOM   3696 C CG  . MET C 3 26  ? 18.373  -11.371 6.534   1.00 45.20  ? 17  MET C CG  1 
ATOM   3697 S SD  . MET C 3 26  ? 17.731  -10.474 5.087   1.00 64.98  ? 17  MET C SD  1 
ATOM   3698 C CE  . MET C 3 26  ? 19.069  -10.767 3.931   1.00 58.74  ? 17  MET C CE  1 
ATOM   3699 N N   . TYR C 3 27  ? 16.324  -13.372 8.383   1.00 38.64  ? 18  TYR C N   1 
ATOM   3700 C CA  . TYR C 3 27  ? 15.695  -14.674 8.250   1.00 39.01  ? 18  TYR C CA  1 
ATOM   3701 C C   . TYR C 3 27  ? 14.910  -14.973 9.519   1.00 39.07  ? 18  TYR C C   1 
ATOM   3702 O O   . TYR C 3 27  ? 15.198  -14.432 10.590  1.00 40.13  ? 18  TYR C O   1 
ATOM   3703 C CB  . TYR C 3 27  ? 16.728  -15.786 8.018   1.00 37.76  ? 18  TYR C CB  1 
ATOM   3704 C CG  . TYR C 3 27  ? 17.407  -15.751 6.671   1.00 37.26  ? 18  TYR C CG  1 
ATOM   3705 C CD1 . TYR C 3 27  ? 18.469  -14.887 6.421   1.00 40.99  ? 18  TYR C CD1 1 
ATOM   3706 C CD2 . TYR C 3 27  ? 17.006  -16.595 5.662   1.00 35.22  ? 18  TYR C CD2 1 
ATOM   3707 C CE1 . TYR C 3 27  ? 19.099  -14.856 5.184   1.00 40.07  ? 18  TYR C CE1 1 
ATOM   3708 C CE2 . TYR C 3 27  ? 17.618  -16.573 4.430   1.00 38.91  ? 18  TYR C CE2 1 
ATOM   3709 C CZ  . TYR C 3 27  ? 18.666  -15.710 4.191   1.00 42.15  ? 18  TYR C CZ  1 
ATOM   3710 O OH  . TYR C 3 27  ? 19.264  -15.709 2.948   1.00 43.22  ? 18  TYR C OH  1 
ATOM   3711 N N   . VAL C 3 28  ? 13.917  -15.854 9.392   1.00 35.14  ? 19  VAL C N   1 
ATOM   3712 C CA  . VAL C 3 28  ? 13.151  -16.342 10.530  1.00 37.13  ? 19  VAL C CA  1 
ATOM   3713 C C   . VAL C 3 28  ? 13.101  -17.858 10.424  1.00 37.10  ? 19  VAL C C   1 
ATOM   3714 O O   . VAL C 3 28  ? 13.343  -18.436 9.365   1.00 39.49  ? 19  VAL C O   1 
ATOM   3715 C CB  . VAL C 3 28  ? 11.718  -15.748 10.599  1.00 41.56  ? 19  VAL C CB  1 
ATOM   3716 C CG1 . VAL C 3 28  ? 11.763  -14.234 10.804  1.00 41.34  ? 19  VAL C CG1 1 
ATOM   3717 C CG2 . VAL C 3 28  ? 10.905  -16.102 9.345   1.00 37.55  ? 19  VAL C CG2 1 
ATOM   3718 N N   . LYS C 3 29  ? 12.793  -18.503 11.537  1.00 38.20  ? 20  LYS C N   1 
ATOM   3719 C CA  . LYS C 3 29  ? 12.748  -19.956 11.605  1.00 38.65  ? 20  LYS C CA  1 
ATOM   3720 C C   . LYS C 3 29  ? 11.307  -20.401 11.821  1.00 39.74  ? 20  LYS C C   1 
ATOM   3721 O O   . LYS C 3 29  ? 10.670  -20.008 12.806  1.00 40.07  ? 20  LYS C O   1 
ATOM   3722 C CB  . LYS C 3 29  ? 13.647  -20.481 12.727  1.00 36.78  ? 20  LYS C CB  1 
ATOM   3723 C CG  . LYS C 3 29  ? 13.671  -21.994 12.808  1.00 40.70  ? 20  LYS C CG  1 
ATOM   3724 C CD  . LYS C 3 29  ? 14.452  -22.488 14.015  1.00 40.88  ? 20  LYS C CD  1 
ATOM   3725 C CE  . LYS C 3 29  ? 15.912  -22.168 13.893  1.00 36.40  ? 20  LYS C CE  1 
ATOM   3726 N NZ  . LYS C 3 29  ? 16.651  -22.880 14.967  1.00 46.18  ? 20  LYS C NZ  1 
ATOM   3727 N N   . LEU C 3 30  ? 10.805  -21.230 10.913  1.00 37.24  ? 21  LEU C N   1 
ATOM   3728 C CA  . LEU C 3 30  ? 9.487   -21.844 11.029  1.00 37.94  ? 21  LEU C CA  1 
ATOM   3729 C C   . LEU C 3 30  ? 9.676   -23.324 11.323  1.00 36.52  ? 21  LEU C C   1 
ATOM   3730 O O   . LEU C 3 30  ? 10.211  -24.060 10.487  1.00 40.44  ? 21  LEU C O   1 
ATOM   3731 C CB  . LEU C 3 30  ? 8.670   -21.667 9.743   1.00 36.94  ? 21  LEU C CB  1 
ATOM   3732 C CG  . LEU C 3 30  ? 8.763   -20.318 9.039   1.00 34.93  ? 21  LEU C CG  1 
ATOM   3733 C CD1 . LEU C 3 30  ? 7.840   -20.304 7.842   1.00 32.85  ? 21  LEU C CD1 1 
ATOM   3734 C CD2 . LEU C 3 30  ? 8.426   -19.194 10.013  1.00 35.50  ? 21  LEU C CD2 1 
ATOM   3735 N N   . ILE C 3 31  ? 9.222   -23.764 12.490  1.00 38.92  ? 22  ILE C N   1 
ATOM   3736 C CA  . ILE C 3 31  ? 9.378   -25.146 12.919  1.00 40.34  ? 22  ILE C CA  1 
ATOM   3737 C C   . ILE C 3 31  ? 8.052   -25.861 12.732  1.00 42.92  ? 22  ILE C C   1 
ATOM   3738 O O   . ILE C 3 31  ? 7.008   -25.386 13.202  1.00 41.93  ? 22  ILE C O   1 
ATOM   3739 C CB  . ILE C 3 31  ? 9.851   -25.236 14.379  1.00 41.25  ? 22  ILE C CB  1 
ATOM   3740 C CG1 . ILE C 3 31  ? 11.174  -24.495 14.553  1.00 43.33  ? 22  ILE C CG1 1 
ATOM   3741 C CG2 . ILE C 3 31  ? 10.049  -26.677 14.767  1.00 39.71  ? 22  ILE C CG2 1 
ATOM   3742 C CD1 . ILE C 3 31  ? 11.095  -23.360 15.518  1.00 43.51  ? 22  ILE C CD1 1 
ATOM   3743 N N   . SER C 3 32  ? 8.096   -27.008 12.053  1.00 40.73  ? 23  SER C N   1 
ATOM   3744 C CA  . SER C 3 32  ? 6.914   -27.818 11.803  1.00 40.81  ? 23  SER C CA  1 
ATOM   3745 C C   . SER C 3 32  ? 6.613   -28.734 12.996  1.00 42.09  ? 23  SER C C   1 
ATOM   3746 O O   . SER C 3 32  ? 7.378   -28.834 13.961  1.00 41.09  ? 23  SER C O   1 
ATOM   3747 C CB  . SER C 3 32  ? 7.102   -28.644 10.534  1.00 38.33  ? 23  SER C CB  1 
ATOM   3748 O OG  . SER C 3 32  ? 7.937   -29.756 10.781  1.00 40.87  ? 23  SER C OG  1 
ATOM   3749 N N   . SER C 3 33  ? 5.470   -29.416 12.912  1.00 43.71  ? 24  SER C N   1 
ATOM   3750 C CA  . SER C 3 33  ? 5.043   -30.276 14.008  1.00 43.50  ? 24  SER C CA  1 
ATOM   3751 C C   . SER C 3 33  ? 6.055   -31.384 14.272  1.00 41.99  ? 24  SER C C   1 
ATOM   3752 O O   . SER C 3 33  ? 6.318   -31.738 15.427  1.00 39.87  ? 24  SER C O   1 
ATOM   3753 C CB  . SER C 3 33  ? 3.678   -30.874 13.692  1.00 43.03  ? 24  SER C CB  1 
ATOM   3754 O OG  . SER C 3 33  ? 3.749   -31.735 12.566  1.00 40.71  ? 24  SER C OG  1 
ATOM   3755 N N   . ASP C 3 34  ? 6.617   -31.959 13.212  1.00 40.56  ? 25  ASP C N   1 
ATOM   3756 C CA  . ASP C 3 34  ? 7.566   -33.053 13.340  1.00 40.17  ? 25  ASP C CA  1 
ATOM   3757 C C   . ASP C 3 34  ? 8.992   -32.562 13.573  1.00 40.78  ? 25  ASP C C   1 
ATOM   3758 O O   . ASP C 3 34  ? 9.926   -33.367 13.520  1.00 41.03  ? 25  ASP C O   1 
ATOM   3759 C CB  . ASP C 3 34  ? 7.506   -33.959 12.101  1.00 39.01  ? 25  ASP C CB  1 
ATOM   3760 C CG  . ASP C 3 34  ? 7.758   -33.202 10.804  1.00 43.62  ? 25  ASP C CG  1 
ATOM   3761 O OD1 . ASP C 3 34  ? 7.231   -32.072 10.650  1.00 43.31  ? 25  ASP C OD1 1 
ATOM   3762 O OD2 . ASP C 3 34  ? 8.483   -33.741 9.937   1.00 41.60  ? 25  ASP C OD2 1 
ATOM   3763 N N   . GLY C 3 35  ? 9.174   -31.265 13.824  1.00 39.67  ? 26  GLY C N   1 
ATOM   3764 C CA  . GLY C 3 35  ? 10.428  -30.746 14.327  1.00 41.21  ? 26  GLY C CA  1 
ATOM   3765 C C   . GLY C 3 35  ? 11.429  -30.322 13.283  1.00 42.88  ? 26  GLY C C   1 
ATOM   3766 O O   . GLY C 3 35  ? 12.589  -30.063 13.630  1.00 42.11  ? 26  GLY C O   1 
ATOM   3767 N N   . HIS C 3 36  ? 11.031  -30.266 12.019  1.00 41.14  ? 27  HIS C N   1 
ATOM   3768 C CA  . HIS C 3 36  ? 11.898  -29.701 11.002  1.00 38.46  ? 27  HIS C CA  1 
ATOM   3769 C C   . HIS C 3 36  ? 11.948  -28.195 11.173  1.00 41.25  ? 27  HIS C C   1 
ATOM   3770 O O   . HIS C 3 36  ? 10.944  -27.561 11.513  1.00 41.32  ? 27  HIS C O   1 
ATOM   3771 C CB  . HIS C 3 36  ? 11.392  -30.054 9.608   1.00 38.43  ? 27  HIS C CB  1 
ATOM   3772 C CG  . HIS C 3 36  ? 11.873  -31.377 9.106   1.00 37.72  ? 27  HIS C CG  1 
ATOM   3773 N ND1 . HIS C 3 36  ? 12.899  -31.496 8.192   1.00 39.96  ? 27  HIS C ND1 1 
ATOM   3774 C CD2 . HIS C 3 36  ? 11.460  -32.637 9.375   1.00 38.00  ? 27  HIS C CD2 1 
ATOM   3775 C CE1 . HIS C 3 36  ? 13.097  -32.774 7.922   1.00 38.85  ? 27  HIS C CE1 1 
ATOM   3776 N NE2 . HIS C 3 36  ? 12.236  -33.487 8.625   1.00 37.44  ? 27  HIS C NE2 1 
ATOM   3777 N N   . GLU C 3 37  ? 13.122  -27.620 10.945  1.00 39.42  ? 28  GLU C N   1 
ATOM   3778 C CA  . GLU C 3 37  ? 13.300  -26.179 11.022  1.00 39.90  ? 28  GLU C CA  1 
ATOM   3779 C C   . GLU C 3 37  ? 13.431  -25.627 9.611   1.00 34.62  ? 28  GLU C C   1 
ATOM   3780 O O   . GLU C 3 37  ? 14.207  -26.149 8.808   1.00 36.08  ? 28  GLU C O   1 
ATOM   3781 C CB  . GLU C 3 37  ? 14.518  -25.830 11.878  1.00 36.65  ? 28  GLU C CB  1 
ATOM   3782 C CG  . GLU C 3 37  ? 14.296  -26.191 13.328  1.00 42.29  ? 28  GLU C CG  1 
ATOM   3783 C CD  . GLU C 3 37  ? 15.514  -25.955 14.198  1.00 48.87  ? 28  GLU C CD  1 
ATOM   3784 O OE1 . GLU C 3 37  ? 16.566  -25.535 13.648  1.00 50.52  ? 28  GLU C OE1 1 
ATOM   3785 O OE2 . GLU C 3 37  ? 15.409  -26.208 15.426  1.00 46.26  ? 28  GLU C OE2 1 
ATOM   3786 N N   . PHE C 3 38  ? 12.657  -24.596 9.299   1.00 34.64  ? 29  PHE C N   1 
ATOM   3787 C CA  . PHE C 3 38  ? 12.709  -23.966 7.985   1.00 33.24  ? 29  PHE C CA  1 
ATOM   3788 C C   . PHE C 3 38  ? 13.129  -22.529 8.195   1.00 34.78  ? 29  PHE C C   1 
ATOM   3789 O O   . PHE C 3 38  ? 12.471  -21.785 8.929   1.00 40.42  ? 29  PHE C O   1 
ATOM   3790 C CB  . PHE C 3 38  ? 11.368  -24.062 7.247   1.00 31.98  ? 29  PHE C CB  1 
ATOM   3791 C CG  . PHE C 3 38  ? 10.967  -25.478 6.931   1.00 34.36  ? 29  PHE C CG  1 
ATOM   3792 C CD1 . PHE C 3 38  ? 11.482  -26.123 5.808   1.00 30.59  ? 29  PHE C CD1 1 
ATOM   3793 C CD2 . PHE C 3 38  ? 10.111  -26.183 7.780   1.00 31.90  ? 29  PHE C CD2 1 
ATOM   3794 C CE1 . PHE C 3 38  ? 11.134  -27.445 5.517   1.00 33.69  ? 29  PHE C CE1 1 
ATOM   3795 C CE2 . PHE C 3 38  ? 9.762   -27.506 7.507   1.00 32.50  ? 29  PHE C CE2 1 
ATOM   3796 C CZ  . PHE C 3 38  ? 10.274  -28.143 6.373   1.00 34.53  ? 29  PHE C CZ  1 
ATOM   3797 N N   . ILE C 3 39  ? 14.251  -22.158 7.603   1.00 34.73  ? 30  ILE C N   1 
ATOM   3798 C CA  . ILE C 3 39  ? 14.805  -20.825 7.750   1.00 34.39  ? 30  ILE C CA  1 
ATOM   3799 C C   . ILE C 3 39  ? 14.604  -20.123 6.416   1.00 36.34  ? 30  ILE C C   1 
ATOM   3800 O O   . ILE C 3 39  ? 15.149  -20.546 5.388   1.00 32.69  ? 30  ILE C O   1 
ATOM   3801 C CB  . ILE C 3 39  ? 16.269  -20.883 8.184   1.00 32.56  ? 30  ILE C CB  1 
ATOM   3802 C CG1 . ILE C 3 39  ? 16.337  -21.556 9.557   1.00 31.97  ? 30  ILE C CG1 1 
ATOM   3803 C CG2 . ILE C 3 39  ? 16.868  -19.513 8.202   1.00 33.08  ? 30  ILE C CG2 1 
ATOM   3804 C CD1 . ILE C 3 39  ? 17.719  -21.729 10.075  1.00 34.85  ? 30  ILE C CD1 1 
ATOM   3805 N N   . VAL C 3 40  ? 13.762  -19.085 6.432   1.00 34.32  ? 31  VAL C N   1 
ATOM   3806 C CA  . VAL C 3 40  ? 13.330  -18.364 5.248   1.00 34.06  ? 31  VAL C CA  1 
ATOM   3807 C C   . VAL C 3 40  ? 13.540  -16.886 5.505   1.00 35.78  ? 31  VAL C C   1 
ATOM   3808 O O   . VAL C 3 40  ? 13.552  -16.430 6.650   1.00 38.57  ? 31  VAL C O   1 
ATOM   3809 C CB  . VAL C 3 40  ? 11.845  -18.622 4.892   1.00 35.04  ? 31  VAL C CB  1 
ATOM   3810 C CG1 . VAL C 3 40  ? 11.638  -20.055 4.479   1.00 37.23  ? 31  VAL C CG1 1 
ATOM   3811 C CG2 . VAL C 3 40  ? 10.961  -18.289 6.066   1.00 36.55  ? 31  VAL C CG2 1 
ATOM   3812 N N   . LYS C 3 41  ? 13.685  -16.132 4.419   1.00 36.29  ? 32  LYS C N   1 
ATOM   3813 C CA  . LYS C 3 41  ? 13.750  -14.686 4.545   1.00 38.13  ? 32  LYS C CA  1 
ATOM   3814 C C   . LYS C 3 41  ? 12.511  -14.157 5.258   1.00 39.65  ? 32  LYS C C   1 
ATOM   3815 O O   . LYS C 3 41  ? 11.381  -14.581 4.996   1.00 37.81  ? 32  LYS C O   1 
ATOM   3816 C CB  . LYS C 3 41  ? 13.899  -14.039 3.171   1.00 37.47  ? 32  LYS C CB  1 
ATOM   3817 C CG  . LYS C 3 41  ? 15.349  -13.865 2.786   1.00 42.07  ? 32  LYS C CG  1 
ATOM   3818 C CD  . LYS C 3 41  ? 15.528  -13.569 1.312   1.00 47.08  ? 32  LYS C CD  1 
ATOM   3819 C CE  . LYS C 3 41  ? 16.998  -13.678 0.916   1.00 48.68  ? 32  LYS C CE  1 
ATOM   3820 N NZ  . LYS C 3 41  ? 17.231  -13.153 -0.457  1.00 52.27  ? 32  LYS C NZ  1 
ATOM   3821 N N   . ARG C 3 42  ? 12.738  -13.233 6.186   1.00 40.40  ? 33  ARG C N   1 
ATOM   3822 C CA  . ARG C 3 42  ? 11.630  -12.620 6.907   1.00 40.57  ? 33  ARG C CA  1 
ATOM   3823 C C   . ARG C 3 42  ? 10.636  -11.977 5.939   1.00 39.43  ? 33  ARG C C   1 
ATOM   3824 O O   . ARG C 3 42  ? 9.418   -12.083 6.125   1.00 38.49  ? 33  ARG C O   1 
ATOM   3825 C CB  . ARG C 3 42  ? 12.186  -11.597 7.908   1.00 41.15  ? 33  ARG C CB  1 
ATOM   3826 C CG  . ARG C 3 42  ? 11.142  -10.781 8.657   1.00 39.67  ? 33  ARG C CG  1 
ATOM   3827 C CD  . ARG C 3 42  ? 11.806  -9.890  9.703   1.00 43.79  ? 33  ARG C CD  1 
ATOM   3828 N NE  . ARG C 3 42  ? 11.197  -10.116 11.006  1.00 46.41  ? 33  ARG C NE  1 
ATOM   3829 C CZ  . ARG C 3 42  ? 11.758  -10.785 12.002  1.00 48.97  ? 33  ARG C CZ  1 
ATOM   3830 N NH1 . ARG C 3 42  ? 13.025  -11.178 11.947  1.00 46.10  ? 33  ARG C NH1 1 
ATOM   3831 N NH2 . ARG C 3 42  ? 11.028  -11.067 13.081  1.00 55.85  ? 33  ARG C NH2 1 
ATOM   3832 N N   . GLU C 3 43  ? 11.145  -11.328 4.887   1.00 39.41  ? 34  GLU C N   1 
ATOM   3833 C CA  . GLU C 3 43  ? 10.277  -10.699 3.899   1.00 39.68  ? 34  GLU C CA  1 
ATOM   3834 C C   . GLU C 3 43  ? 9.404   -11.727 3.187   1.00 39.69  ? 34  GLU C C   1 
ATOM   3835 O O   . GLU C 3 43  ? 8.257   -11.438 2.834   1.00 40.58  ? 34  GLU C O   1 
ATOM   3836 C CB  . GLU C 3 43  ? 11.115  -9.928  2.880   1.00 42.28  ? 34  GLU C CB  1 
ATOM   3837 C CG  . GLU C 3 43  ? 10.304  -9.393  1.692   1.00 47.67  ? 34  GLU C CG  1 
ATOM   3838 C CD  . GLU C 3 43  ? 11.159  -9.069  0.458   1.00 52.82  ? 34  GLU C CD  1 
ATOM   3839 O OE1 . GLU C 3 43  ? 10.570  -8.817  -0.621  1.00 56.43  ? 34  GLU C OE1 1 
ATOM   3840 O OE2 . GLU C 3 43  ? 12.410  -9.066  0.560   1.00 56.08  ? 34  GLU C OE2 1 
ATOM   3841 N N   . HIS C 3 44  ? 9.941   -12.921 2.935   1.00 38.74  ? 35  HIS C N   1 
ATOM   3842 C CA  . HIS C 3 44  ? 9.143   -13.971 2.312   1.00 37.88  ? 35  HIS C CA  1 
ATOM   3843 C C   . HIS C 3 44  ? 8.061   -14.470 3.256   1.00 36.78  ? 35  HIS C C   1 
ATOM   3844 O O   . HIS C 3 44  ? 6.900   -14.619 2.862   1.00 37.39  ? 35  HIS C O   1 
ATOM   3845 C CB  . HIS C 3 44  ? 10.048  -15.118 1.867   1.00 36.38  ? 35  HIS C CB  1 
ATOM   3846 C CG  . HIS C 3 44  ? 10.985  -14.742 0.764   1.00 37.34  ? 35  HIS C CG  1 
ATOM   3847 N ND1 . HIS C 3 44  ? 11.700  -15.673 0.042   1.00 41.89  ? 35  HIS C ND1 1 
ATOM   3848 C CD2 . HIS C 3 44  ? 11.308  -13.534 0.243   1.00 36.73  ? 35  HIS C CD2 1 
ATOM   3849 C CE1 . HIS C 3 44  ? 12.431  -15.054 -0.869  1.00 38.25  ? 35  HIS C CE1 1 
ATOM   3850 N NE2 . HIS C 3 44  ? 12.212  -13.756 -0.766  1.00 35.10  ? 35  HIS C NE2 1 
ATOM   3851 N N   . ALA C 3 45  ? 8.424   -14.713 4.516   1.00 38.38  ? 36  ALA C N   1 
ATOM   3852 C CA  . ALA C 3 45  ? 7.461   -15.204 5.495   1.00 36.25  ? 36  ALA C CA  1 
ATOM   3853 C C   . ALA C 3 45  ? 6.312   -14.230 5.694   1.00 37.45  ? 36  ALA C C   1 
ATOM   3854 O O   . ALA C 3 45  ? 5.216   -14.643 6.087   1.00 36.50  ? 36  ALA C O   1 
ATOM   3855 C CB  . ALA C 3 45  ? 8.157   -15.469 6.827   1.00 34.17  ? 36  ALA C CB  1 
ATOM   3856 N N   . LEU C 3 46  ? 6.539   -12.940 5.430   1.00 36.49  ? 37  LEU C N   1 
ATOM   3857 C CA  . LEU C 3 46  ? 5.486   -11.942 5.567   1.00 39.89  ? 37  LEU C CA  1 
ATOM   3858 C C   . LEU C 3 46  ? 4.358   -12.152 4.570   1.00 37.03  ? 37  LEU C C   1 
ATOM   3859 O O   . LEU C 3 46  ? 3.305   -11.531 4.719   1.00 40.71  ? 37  LEU C O   1 
ATOM   3860 C CB  . LEU C 3 46  ? 6.061   -10.533 5.410   1.00 40.62  ? 37  LEU C CB  1 
ATOM   3861 C CG  . LEU C 3 46  ? 6.946   -10.057 6.566   1.00 44.20  ? 37  LEU C CG  1 
ATOM   3862 C CD1 . LEU C 3 46  ? 7.318   -8.574  6.397   1.00 42.90  ? 37  LEU C CD1 1 
ATOM   3863 C CD2 . LEU C 3 46  ? 6.270   -10.313 7.905   1.00 42.20  ? 37  LEU C CD2 1 
ATOM   3864 N N   . THR C 3 47  ? 4.562   -13.001 3.563   1.00 34.75  ? 38  THR C N   1 
ATOM   3865 C CA  . THR C 3 47  ? 3.482   -13.385 2.674   1.00 33.61  ? 38  THR C CA  1 
ATOM   3866 C C   . THR C 3 47  ? 2.331   -13.979 3.458   1.00 34.42  ? 38  THR C C   1 
ATOM   3867 O O   . THR C 3 47  ? 1.172   -13.869 3.047   1.00 34.84  ? 38  THR C O   1 
ATOM   3868 C CB  . THR C 3 47  ? 4.007   -14.384 1.636   1.00 39.46  ? 38  THR C CB  1 
ATOM   3869 O OG1 . THR C 3 47  ? 5.159   -13.826 0.978   1.00 40.13  ? 38  THR C OG1 1 
ATOM   3870 C CG2 . THR C 3 47  ? 2.928   -14.736 0.599   1.00 34.57  ? 38  THR C CG2 1 
ATOM   3871 N N   . SER C 3 48  ? 2.633   -14.604 4.587   1.00 36.49  ? 39  SER C N   1 
ATOM   3872 C CA  . SER C 3 48  ? 1.628   -15.116 5.505   1.00 36.71  ? 39  SER C CA  1 
ATOM   3873 C C   . SER C 3 48  ? 1.202   -14.005 6.452   1.00 37.65  ? 39  SER C C   1 
ATOM   3874 O O   . SER C 3 48  ? 2.026   -13.493 7.221   1.00 37.39  ? 39  SER C O   1 
ATOM   3875 C CB  . SER C 3 48  ? 2.181   -16.294 6.299   1.00 32.20  ? 39  SER C CB  1 
ATOM   3876 O OG  . SER C 3 48  ? 1.424   -16.464 7.470   1.00 33.28  ? 39  SER C OG  1 
ATOM   3877 N N   . GLY C 3 49  ? -0.077  -13.639 6.409   1.00 36.86  ? 40  GLY C N   1 
ATOM   3878 C CA  . GLY C 3 49  ? -0.573  -12.664 7.366   1.00 38.33  ? 40  GLY C CA  1 
ATOM   3879 C C   . GLY C 3 49  ? -0.471  -13.161 8.794   1.00 38.61  ? 40  GLY C C   1 
ATOM   3880 O O   . GLY C 3 49  ? -0.212  -12.389 9.724   1.00 39.84  ? 40  GLY C O   1 
ATOM   3881 N N   . THR C 3 50  ? -0.682  -14.460 8.986   1.00 40.47  ? 41  THR C N   1 
ATOM   3882 C CA  . THR C 3 50  ? -0.581  -15.058 10.311  1.00 40.31  ? 41  THR C CA  1 
ATOM   3883 C C   . THR C 3 50  ? 0.833   -14.930 10.864  1.00 41.38  ? 41  THR C C   1 
ATOM   3884 O O   . THR C 3 50  ? 1.024   -14.476 11.997  1.00 45.48  ? 41  THR C O   1 
ATOM   3885 C CB  . THR C 3 50  ? -1.022  -16.522 10.231  1.00 37.83  ? 41  THR C CB  1 
ATOM   3886 O OG1 . THR C 3 50  ? -2.384  -16.578 9.799   1.00 39.76  ? 41  THR C OG1 1 
ATOM   3887 C CG2 . THR C 3 50  ? -0.865  -17.234 11.569  1.00 38.45  ? 41  THR C CG2 1 
ATOM   3888 N N   . ILE C 3 51  ? 1.839   -15.311 10.068  1.00 37.63  ? 42  ILE C N   1 
ATOM   3889 C CA  . ILE C 3 51  ? 3.231   -15.147 10.486  1.00 39.93  ? 42  ILE C CA  1 
ATOM   3890 C C   . ILE C 3 51  ? 3.555   -13.669 10.684  1.00 42.65  ? 42  ILE C C   1 
ATOM   3891 O O   . ILE C 3 51  ? 4.244   -13.293 11.639  1.00 42.36  ? 42  ILE C O   1 
ATOM   3892 C CB  . ILE C 3 51  ? 4.173   -15.812 9.463   1.00 38.64  ? 42  ILE C CB  1 
ATOM   3893 C CG1 . ILE C 3 51  ? 4.066   -17.333 9.559   1.00 36.23  ? 42  ILE C CG1 1 
ATOM   3894 C CG2 . ILE C 3 51  ? 5.632   -15.331 9.624   1.00 37.00  ? 42  ILE C CG2 1 
ATOM   3895 C CD1 . ILE C 3 51  ? 4.537   -18.029 8.322   1.00 33.12  ? 42  ILE C CD1 1 
ATOM   3896 N N   . LYS C 3 52  ? 3.050   -12.807 9.793   1.00 43.12  ? 43  LYS C N   1 
ATOM   3897 C CA  . LYS C 3 52  ? 3.210   -11.365 9.968   1.00 43.83  ? 43  LYS C CA  1 
ATOM   3898 C C   . LYS C 3 52  ? 2.766   -10.950 11.362  1.00 45.44  ? 43  LYS C C   1 
ATOM   3899 O O   . LYS C 3 52  ? 3.505   -10.277 12.092  1.00 46.13  ? 43  LYS C O   1 
ATOM   3900 C CB  . LYS C 3 52  ? 2.408   -10.622 8.895   1.00 44.32  ? 43  LYS C CB  1 
ATOM   3901 C CG  . LYS C 3 52  ? 2.544   -9.102  8.890   1.00 48.28  ? 43  LYS C CG  1 
ATOM   3902 C CD  . LYS C 3 52  ? 2.413   -8.528  7.459   1.00 49.53  ? 43  LYS C CD  1 
ATOM   3903 C CE  . LYS C 3 52  ? 3.517   -7.480  7.177   1.00 63.49  ? 43  LYS C CE  1 
ATOM   3904 N NZ  . LYS C 3 52  ? 3.603   -6.979  5.759   1.00 61.66  ? 43  LYS C NZ  1 
ATOM   3905 N N   . ALA C 3 53  ? 1.578   -11.405 11.770  1.00 44.39  ? 44  ALA C N   1 
ATOM   3906 C CA  . ALA C 3 53  ? 1.091   -11.109 13.111  1.00 41.61  ? 44  ALA C CA  1 
ATOM   3907 C C   . ALA C 3 53  ? 2.012   -11.685 14.177  1.00 45.99  ? 44  ALA C C   1 
ATOM   3908 O O   . ALA C 3 53  ? 2.323   -11.007 15.163  1.00 49.18  ? 44  ALA C O   1 
ATOM   3909 C CB  . ALA C 3 53  ? -0.329  -11.649 13.288  1.00 41.01  ? 44  ALA C CB  1 
ATOM   3910 N N   . MET C 3 54  ? 2.454   -12.935 14.002  1.00 46.50  ? 45  MET C N   1 
ATOM   3911 C CA  . MET C 3 54  ? 3.214   -13.600 15.059  1.00 46.01  ? 45  MET C CA  1 
ATOM   3912 C C   . MET C 3 54  ? 4.565   -12.931 15.292  1.00 47.79  ? 45  MET C C   1 
ATOM   3913 O O   . MET C 3 54  ? 4.988   -12.767 16.443  1.00 50.41  ? 45  MET C O   1 
ATOM   3914 C CB  . MET C 3 54  ? 3.391   -15.077 14.728  1.00 43.34  ? 45  MET C CB  1 
ATOM   3915 C CG  . MET C 3 54  ? 2.115   -15.877 14.812  1.00 39.40  ? 45  MET C CG  1 
ATOM   3916 S SD  . MET C 3 54  ? 2.307   -17.563 14.195  1.00 54.36  ? 45  MET C SD  1 
ATOM   3917 C CE  . MET C 3 54  ? 0.690   -18.232 14.583  1.00 47.43  ? 45  MET C CE  1 
ATOM   3918 N N   . LEU C 3 55  ? 5.253   -12.533 14.220  1.00 47.34  ? 46  LEU C N   1 
ATOM   3919 C CA  . LEU C 3 55  ? 6.536   -11.853 14.366  1.00 47.11  ? 46  LEU C CA  1 
ATOM   3920 C C   . LEU C 3 55  ? 6.405   -10.459 14.982  1.00 52.35  ? 46  LEU C C   1 
ATOM   3921 O O   . LEU C 3 55  ? 7.411   -9.908  15.450  1.00 54.63  ? 46  LEU C O   1 
ATOM   3922 C CB  . LEU C 3 55  ? 7.235   -11.758 13.010  1.00 47.46  ? 46  LEU C CB  1 
ATOM   3923 C CG  . LEU C 3 55  ? 7.659   -13.080 12.364  1.00 45.91  ? 46  LEU C CG  1 
ATOM   3924 C CD1 . LEU C 3 55  ? 8.254   -12.802 11.006  1.00 46.67  ? 46  LEU C CD1 1 
ATOM   3925 C CD2 . LEU C 3 55  ? 8.658   -13.818 13.223  1.00 47.59  ? 46  LEU C CD2 1 
ATOM   3926 N N   . SER C 3 56  ? 5.196   -9.879  14.997  1.00 49.56  ? 47  SER C N   1 
ATOM   3927 C CA  . SER C 3 56  ? 4.937   -8.568  15.587  1.00 47.57  ? 47  SER C CA  1 
ATOM   3928 C C   . SER C 3 56  ? 4.121   -8.660  16.878  1.00 49.25  ? 47  SER C C   1 
ATOM   3929 O O   . SER C 3 56  ? 3.400   -7.721  17.223  1.00 47.30  ? 47  SER C O   1 
ATOM   3930 C CB  . SER C 3 56  ? 4.215   -7.648  14.600  1.00 50.02  ? 47  SER C CB  1 
ATOM   3931 O OG  . SER C 3 56  ? 4.974   -7.375  13.436  1.00 54.71  ? 47  SER C OG  1 
ATOM   3932 N N   . GLY C 3 57  ? 4.227   -9.771  17.606  1.00 50.40  ? 48  GLY C N   1 
ATOM   3933 C CA  . GLY C 3 57  ? 3.501   -9.922  18.847  1.00 48.77  ? 48  GLY C CA  1 
ATOM   3934 C C   . GLY C 3 57  ? 4.037   -8.998  19.922  1.00 48.59  ? 48  GLY C C   1 
ATOM   3935 O O   . GLY C 3 57  ? 5.103   -8.397  19.770  1.00 47.77  ? 48  GLY C O   1 
ATOM   3936 N N   . PRO C 3 58  ? 3.314   -8.866  21.031  1.00 49.79  ? 49  PRO C N   1 
ATOM   3937 C CA  . PRO C 3 58  ? 3.749   -7.940  22.086  1.00 52.11  ? 49  PRO C CA  1 
ATOM   3938 C C   . PRO C 3 58  ? 5.032   -8.407  22.761  1.00 53.54  ? 49  PRO C C   1 
ATOM   3939 O O   . PRO C 3 58  ? 5.491   -9.539  22.567  1.00 54.67  ? 49  PRO C O   1 
ATOM   3940 C CB  . PRO C 3 58  ? 2.569   -7.931  23.063  1.00 52.34  ? 49  PRO C CB  1 
ATOM   3941 C CG  . PRO C 3 58  ? 1.894   -9.219  22.831  1.00 51.54  ? 49  PRO C CG  1 
ATOM   3942 C CD  . PRO C 3 58  ? 2.055   -9.540  21.375  1.00 49.05  ? 49  PRO C CD  1 
ATOM   3943 N N   . GLY C 3 59  ? 5.623   -7.489  23.544  1.00 57.51  ? 50  GLY C N   1 
ATOM   3944 C CA  . GLY C 3 59  ? 6.907   -7.694  24.213  1.00 59.05  ? 50  GLY C CA  1 
ATOM   3945 C C   . GLY C 3 59  ? 8.080   -7.947  23.269  1.00 59.02  ? 50  GLY C C   1 
ATOM   3946 O O   . GLY C 3 59  ? 9.206   -7.497  23.504  1.00 59.73  ? 50  GLY C O   1 
ATOM   3947 N N   . ASN C 3 67  ? 14.215  -14.520 15.695  1.00 44.40  ? 58  ASN C N   1 
ATOM   3948 C CA  . ASN C 3 67  ? 12.762  -14.676 15.787  1.00 51.30  ? 58  ASN C CA  1 
ATOM   3949 C C   . ASN C 3 67  ? 12.278  -15.948 15.055  1.00 49.85  ? 58  ASN C C   1 
ATOM   3950 O O   . ASN C 3 67  ? 12.663  -16.206 13.912  1.00 41.56  ? 58  ASN C O   1 
ATOM   3951 C CB  . ASN C 3 67  ? 12.065  -13.436 15.226  1.00 50.57  ? 58  ASN C CB  1 
ATOM   3952 C CG  . ASN C 3 67  ? 11.275  -12.671 16.289  1.00 63.05  ? 58  ASN C CG  1 
ATOM   3953 O OD1 . ASN C 3 67  ? 10.800  -13.247 17.273  1.00 67.68  ? 58  ASN C OD1 1 
ATOM   3954 N ND2 . ASN C 3 67  ? 11.128  -11.365 16.087  1.00 64.23  ? 58  ASN C ND2 1 
ATOM   3955 N N   . GLU C 3 68  ? 11.432  -16.739 15.720  1.00 46.22  ? 59  GLU C N   1 
ATOM   3956 C CA  . GLU C 3 68  ? 11.037  -18.043 15.204  1.00 43.08  ? 59  GLU C CA  1 
ATOM   3957 C C   . GLU C 3 68  ? 9.601   -18.358 15.612  1.00 46.27  ? 59  GLU C C   1 
ATOM   3958 O O   . GLU C 3 68  ? 9.052   -17.773 16.550  1.00 45.93  ? 59  GLU C O   1 
ATOM   3959 C CB  . GLU C 3 68  ? 11.975  -19.140 15.704  1.00 45.05  ? 59  GLU C CB  1 
ATOM   3960 C CG  . GLU C 3 68  ? 11.722  -19.542 17.128  1.00 44.04  ? 59  GLU C CG  1 
ATOM   3961 C CD  . GLU C 3 68  ? 12.643  -20.647 17.586  1.00 49.32  ? 59  GLU C CD  1 
ATOM   3962 O OE1 . GLU C 3 68  ? 13.816  -20.650 17.141  1.00 49.43  ? 59  GLU C OE1 1 
ATOM   3963 O OE2 . GLU C 3 68  ? 12.192  -21.509 18.383  1.00 50.48  ? 59  GLU C OE2 1 
ATOM   3964 N N   . VAL C 3 69  ? 8.989   -19.294 14.890  1.00 45.18  ? 60  VAL C N   1 
ATOM   3965 C CA  . VAL C 3 69  ? 7.574   -19.622 15.062  1.00 45.11  ? 60  VAL C CA  1 
ATOM   3966 C C   . VAL C 3 69  ? 7.425   -21.136 15.085  1.00 41.31  ? 60  VAL C C   1 
ATOM   3967 O O   . VAL C 3 69  ? 7.992   -21.833 14.240  1.00 41.64  ? 60  VAL C O   1 
ATOM   3968 C CB  . VAL C 3 69  ? 6.705   -19.012 13.942  1.00 45.14  ? 60  VAL C CB  1 
ATOM   3969 C CG1 . VAL C 3 69  ? 5.267   -19.481 14.068  1.00 46.36  ? 60  VAL C CG1 1 
ATOM   3970 C CG2 . VAL C 3 69  ? 6.767   -17.494 13.979  1.00 45.07  ? 60  VAL C CG2 1 
ATOM   3971 N N   . ASN C 3 70  ? 6.666   -21.648 16.038  1.00 43.85  ? 61  ASN C N   1 
ATOM   3972 C CA  . ASN C 3 70  ? 6.476   -23.085 16.160  1.00 44.67  ? 61  ASN C CA  1 
ATOM   3973 C C   . ASN C 3 70  ? 5.055   -23.416 15.731  1.00 47.86  ? 61  ASN C C   1 
ATOM   3974 O O   . ASN C 3 70  ? 4.092   -22.864 16.280  1.00 51.52  ? 61  ASN C O   1 
ATOM   3975 C CB  . ASN C 3 70  ? 6.763   -23.558 17.586  1.00 45.49  ? 61  ASN C CB  1 
ATOM   3976 C CG  . ASN C 3 70  ? 7.415   -24.931 17.619  1.00 55.10  ? 61  ASN C CG  1 
ATOM   3977 O OD1 . ASN C 3 70  ? 7.105   -25.801 16.792  1.00 52.20  ? 61  ASN C OD1 1 
ATOM   3978 N ND2 . ASN C 3 70  ? 8.329   -25.135 18.572  1.00 60.85  ? 61  ASN C ND2 1 
ATOM   3979 N N   . PHE C 3 71  ? 4.927   -24.288 14.731  1.00 46.98  ? 62  PHE C N   1 
ATOM   3980 C CA  . PHE C 3 71  ? 3.637   -24.687 14.174  1.00 44.05  ? 62  PHE C CA  1 
ATOM   3981 C C   . PHE C 3 71  ? 3.387   -26.134 14.574  1.00 47.05  ? 62  PHE C C   1 
ATOM   3982 O O   . PHE C 3 71  ? 3.752   -27.067 13.859  1.00 48.70  ? 62  PHE C O   1 
ATOM   3983 C CB  . PHE C 3 71  ? 3.608   -24.522 12.654  1.00 45.68  ? 62  PHE C CB  1 
ATOM   3984 C CG  . PHE C 3 71  ? 3.600   -23.089 12.191  1.00 44.64  ? 62  PHE C CG  1 
ATOM   3985 C CD1 . PHE C 3 71  ? 2.500   -22.270 12.427  1.00 44.55  ? 62  PHE C CD1 1 
ATOM   3986 C CD2 . PHE C 3 71  ? 4.674   -22.571 11.501  1.00 40.38  ? 62  PHE C CD2 1 
ATOM   3987 C CE1 . PHE C 3 71  ? 2.490   -20.958 12.004  1.00 43.52  ? 62  PHE C CE1 1 
ATOM   3988 C CE2 . PHE C 3 71  ? 4.663   -21.254 11.071  1.00 41.37  ? 62  PHE C CE2 1 
ATOM   3989 C CZ  . PHE C 3 71  ? 3.575   -20.452 11.320  1.00 42.02  ? 62  PHE C CZ  1 
ATOM   3990 N N   . ARG C 3 72  ? 2.737   -26.317 15.721  1.00 51.56  ? 63  ARG C N   1 
ATOM   3991 C CA  . ARG C 3 72  ? 2.536   -27.662 16.247  1.00 54.11  ? 63  ARG C CA  1 
ATOM   3992 C C   . ARG C 3 72  ? 1.599   -28.502 15.385  1.00 54.40  ? 63  ARG C C   1 
ATOM   3993 O O   . ARG C 3 72  ? 1.537   -29.720 15.582  1.00 53.44  ? 63  ARG C O   1 
ATOM   3994 C CB  . ARG C 3 72  ? 2.010   -27.586 17.689  1.00 53.73  ? 63  ARG C CB  1 
ATOM   3995 N N   . GLU C 3 73  ? 0.891   -27.901 14.429  1.00 54.36  ? 64  GLU C N   1 
ATOM   3996 C CA  . GLU C 3 73  ? -0.135  -28.608 13.678  1.00 55.04  ? 64  GLU C CA  1 
ATOM   3997 C C   . GLU C 3 73  ? 0.173   -28.769 12.194  1.00 53.95  ? 64  GLU C C   1 
ATOM   3998 O O   . GLU C 3 73  ? -0.605  -29.416 11.489  1.00 54.79  ? 64  GLU C O   1 
ATOM   3999 C CB  . GLU C 3 73  ? -1.476  -27.890 13.850  1.00 65.74  ? 64  GLU C CB  1 
ATOM   4000 C CG  . GLU C 3 73  ? -1.876  -27.681 15.306  1.00 68.93  ? 64  GLU C CG  1 
ATOM   4001 C CD  . GLU C 3 73  ? -2.509  -28.919 15.929  1.00 77.11  ? 64  GLU C CD  1 
ATOM   4002 O OE1 . GLU C 3 73  ? -1.999  -30.039 15.702  1.00 72.85  ? 64  GLU C OE1 1 
ATOM   4003 O OE2 . GLU C 3 73  ? -3.531  -28.768 16.638  1.00 78.78  ? 64  GLU C OE2 1 
ATOM   4004 N N   . ILE C 3 74  ? 1.273   -28.213 11.700  1.00 49.98  ? 65  ILE C N   1 
ATOM   4005 C CA  . ILE C 3 74  ? 1.602   -28.261 10.281  1.00 44.09  ? 65  ILE C CA  1 
ATOM   4006 C C   . ILE C 3 74  ? 2.834   -29.151 10.110  1.00 43.19  ? 65  ILE C C   1 
ATOM   4007 O O   . ILE C 3 74  ? 3.930   -28.773 10.544  1.00 42.88  ? 65  ILE C O   1 
ATOM   4008 C CB  . ILE C 3 74  ? 1.848   -26.856 9.718   1.00 42.08  ? 65  ILE C CB  1 
ATOM   4009 C CG1 . ILE C 3 74  ? 0.686   -25.923 10.048  1.00 37.56  ? 65  ILE C CG1 1 
ATOM   4010 C CG2 . ILE C 3 74  ? 2.106   -26.935 8.215   1.00 38.13  ? 65  ILE C CG2 1 
ATOM   4011 C CD1 . ILE C 3 74  ? 0.861   -24.493 9.573   1.00 35.78  ? 65  ILE C CD1 1 
ATOM   4012 N N   . PRO C 3 75  ? 2.721   -30.311 9.466   1.00 38.00  ? 66  PRO C N   1 
ATOM   4013 C CA  . PRO C 3 75  ? 3.891   -31.187 9.294   1.00 38.36  ? 66  PRO C CA  1 
ATOM   4014 C C   . PRO C 3 75  ? 4.857   -30.658 8.239   1.00 39.95  ? 66  PRO C C   1 
ATOM   4015 O O   . PRO C 3 75  ? 4.563   -29.730 7.474   1.00 36.70  ? 66  PRO C O   1 
ATOM   4016 C CB  . PRO C 3 75  ? 3.272   -32.520 8.866   1.00 38.79  ? 66  PRO C CB  1 
ATOM   4017 C CG  . PRO C 3 75  ? 2.048   -32.133 8.151   1.00 39.30  ? 66  PRO C CG  1 
ATOM   4018 C CD  . PRO C 3 75  ? 1.517   -30.889 8.857   1.00 39.62  ? 66  PRO C CD  1 
ATOM   4019 N N   . SER C 3 76  ? 6.044   -31.282 8.206   1.00 38.64  ? 67  SER C N   1 
ATOM   4020 C CA  . SER C 3 76  ? 7.138   -30.738 7.404   1.00 36.70  ? 67  SER C CA  1 
ATOM   4021 C C   . SER C 3 76  ? 6.839   -30.787 5.913   1.00 34.92  ? 67  SER C C   1 
ATOM   4022 O O   . SER C 3 76  ? 7.196   -29.856 5.186   1.00 34.64  ? 67  SER C O   1 
ATOM   4023 C CB  . SER C 3 76  ? 8.447   -31.464 7.704   1.00 38.50  ? 67  SER C CB  1 
ATOM   4024 O OG  . SER C 3 76  ? 8.399   -32.818 7.312   1.00 41.04  ? 67  SER C OG  1 
ATOM   4025 N N   . HIS C 3 77  ? 6.198   -31.853 5.421   1.00 36.87  ? 68  HIS C N   1 
ATOM   4026 C CA  . HIS C 3 77  ? 5.956   -31.909 3.978   1.00 39.72  ? 68  HIS C CA  1 
ATOM   4027 C C   . HIS C 3 77  ? 4.973   -30.829 3.527   1.00 38.78  ? 68  HIS C C   1 
ATOM   4028 O O   . HIS C 3 77  ? 5.041   -30.378 2.379   1.00 38.23  ? 68  HIS C O   1 
ATOM   4029 C CB  . HIS C 3 77  ? 5.472   -33.305 3.549   1.00 42.57  ? 68  HIS C CB  1 
ATOM   4030 C CG  . HIS C 3 77  ? 4.082   -33.641 3.997   1.00 48.39  ? 68  HIS C CG  1 
ATOM   4031 N ND1 . HIS C 3 77  ? 3.812   -34.230 5.216   1.00 48.17  ? 68  HIS C ND1 1 
ATOM   4032 C CD2 . HIS C 3 77  ? 2.883   -33.475 3.387   1.00 47.14  ? 68  HIS C CD2 1 
ATOM   4033 C CE1 . HIS C 3 77  ? 2.507   -34.403 5.339   1.00 48.03  ? 68  HIS C CE1 1 
ATOM   4034 N NE2 . HIS C 3 77  ? 1.921   -33.958 4.243   1.00 44.55  ? 68  HIS C NE2 1 
ATOM   4035 N N   . VAL C 3 78  ? 4.079   -30.386 4.415   1.00 36.90  ? 69  VAL C N   1 
ATOM   4036 C CA  . VAL C 3 78  ? 3.197   -29.261 4.108   1.00 37.46  ? 69  VAL C CA  1 
ATOM   4037 C C   . VAL C 3 78  ? 3.939   -27.936 4.243   1.00 33.98  ? 69  VAL C C   1 
ATOM   4038 O O   . VAL C 3 78  ? 3.814   -27.048 3.389   1.00 30.97  ? 69  VAL C O   1 
ATOM   4039 C CB  . VAL C 3 78  ? 1.949   -29.285 5.015   1.00 34.31  ? 69  VAL C CB  1 
ATOM   4040 C CG1 . VAL C 3 78  ? 1.089   -28.070 4.753   1.00 29.23  ? 69  VAL C CG1 1 
ATOM   4041 C CG2 . VAL C 3 78  ? 1.166   -30.541 4.798   1.00 35.59  ? 69  VAL C CG2 1 
ATOM   4042 N N   . LEU C 3 79  ? 4.691   -27.768 5.340   1.00 36.50  ? 70  LEU C N   1 
ATOM   4043 C CA  . LEU C 3 79  ? 5.327   -26.478 5.611   1.00 34.75  ? 70  LEU C CA  1 
ATOM   4044 C C   . LEU C 3 79  ? 6.457   -26.182 4.623   1.00 32.05  ? 70  LEU C C   1 
ATOM   4045 O O   . LEU C 3 79  ? 6.679   -25.013 4.275   1.00 30.01  ? 70  LEU C O   1 
ATOM   4046 C CB  . LEU C 3 79  ? 5.824   -26.421 7.065   1.00 31.89  ? 70  LEU C CB  1 
ATOM   4047 C CG  . LEU C 3 79  ? 6.482   -25.094 7.500   1.00 32.26  ? 70  LEU C CG  1 
ATOM   4048 C CD1 . LEU C 3 79  ? 5.588   -23.869 7.214   1.00 29.46  ? 70  LEU C CD1 1 
ATOM   4049 C CD2 . LEU C 3 79  ? 6.925   -25.117 8.957   1.00 32.20  ? 70  LEU C CD2 1 
ATOM   4050 N N   . SER C 3 80  ? 7.163   -27.217 4.148   1.00 29.99  ? 71  SER C N   1 
ATOM   4051 C CA  . SER C 3 80  ? 8.145   -27.009 3.084   1.00 31.08  ? 71  SER C CA  1 
ATOM   4052 C C   . SER C 3 80  ? 7.483   -26.454 1.826   1.00 31.82  ? 71  SER C C   1 
ATOM   4053 O O   . SER C 3 80  ? 8.021   -25.547 1.177   1.00 29.98  ? 71  SER C O   1 
ATOM   4054 C CB  . SER C 3 80  ? 8.870   -28.319 2.775   1.00 32.24  ? 71  SER C CB  1 
ATOM   4055 O OG  . SER C 3 80  ? 7.939   -29.384 2.612   1.00 34.37  ? 71  SER C OG  1 
ATOM   4056 N N   . LYS C 3 81  ? 6.311   -26.985 1.470   1.00 31.14  ? 72  LYS C N   1 
ATOM   4057 C CA  . LYS C 3 81  ? 5.607   -26.500 0.293   1.00 30.15  ? 72  LYS C CA  1 
ATOM   4058 C C   . LYS C 3 81  ? 5.159   -25.060 0.489   1.00 29.65  ? 72  LYS C C   1 
ATOM   4059 O O   . LYS C 3 81  ? 5.215   -24.254 -0.445  1.00 29.29  ? 72  LYS C O   1 
ATOM   4060 C CB  . LYS C 3 81  ? 4.418   -27.412 -0.014  1.00 33.91  ? 72  LYS C CB  1 
ATOM   4061 C CG  . LYS C 3 81  ? 4.061   -27.510 -1.486  1.00 35.79  ? 72  LYS C CG  1 
ATOM   4062 C CD  . LYS C 3 81  ? 5.111   -28.307 -2.255  1.00 37.69  ? 72  LYS C CD  1 
ATOM   4063 C CE  . LYS C 3 81  ? 4.903   -28.194 -3.780  1.00 37.40  ? 72  LYS C CE  1 
ATOM   4064 N NZ  . LYS C 3 81  ? 3.872   -29.128 -4.304  1.00 40.39  ? 72  LYS C NZ  1 
ATOM   4065 N N   . VAL C 3 82  ? 4.737   -24.712 1.707   1.00 29.29  ? 73  VAL C N   1 
ATOM   4066 C CA  . VAL C 3 82  ? 4.335   -23.335 1.992   1.00 29.53  ? 73  VAL C CA  1 
ATOM   4067 C C   . VAL C 3 82  ? 5.505   -22.378 1.774   1.00 30.92  ? 73  VAL C C   1 
ATOM   4068 O O   . VAL C 3 82  ? 5.336   -21.288 1.207   1.00 30.26  ? 73  VAL C O   1 
ATOM   4069 C CB  . VAL C 3 82  ? 3.769   -23.229 3.423   1.00 31.50  ? 73  VAL C CB  1 
ATOM   4070 C CG1 . VAL C 3 82  ? 3.697   -21.777 3.879   1.00 27.42  ? 73  VAL C CG1 1 
ATOM   4071 C CG2 . VAL C 3 82  ? 2.390   -23.891 3.503   1.00 29.72  ? 73  VAL C CG2 1 
ATOM   4072 N N   . CYS C 3 83  ? 6.709   -22.771 2.214   1.00 29.83  ? 74  CYS C N   1 
ATOM   4073 C CA  . CYS C 3 83  ? 7.896   -21.941 2.016   1.00 29.58  ? 74  CYS C CA  1 
ATOM   4074 C C   . CYS C 3 83  ? 8.219   -21.767 0.538   1.00 32.74  ? 74  CYS C C   1 
ATOM   4075 O O   . CYS C 3 83  ? 8.612   -20.673 0.102   1.00 30.23  ? 74  CYS C O   1 
ATOM   4076 C CB  . CYS C 3 83  ? 9.090   -22.546 2.748   1.00 27.60  ? 74  CYS C CB  1 
ATOM   4077 S SG  . CYS C 3 83  ? 8.941   -22.434 4.527   1.00 29.90  ? 74  CYS C SG  1 
ATOM   4078 N N   . MET C 3 84  ? 8.079   -22.840 -0.247  1.00 32.31  ? 75  MET C N   1 
ATOM   4079 C CA  . MET C 3 84  ? 8.260   -22.713 -1.683  1.00 28.22  ? 75  MET C CA  1 
ATOM   4080 C C   . MET C 3 84  ? 7.268   -21.725 -2.269  1.00 31.49  ? 75  MET C C   1 
ATOM   4081 O O   . MET C 3 84  ? 7.617   -20.938 -3.166  1.00 31.11  ? 75  MET C O   1 
ATOM   4082 C CB  . MET C 3 84  ? 8.114   -24.069 -2.340  1.00 27.37  ? 75  MET C CB  1 
ATOM   4083 C CG  . MET C 3 84  ? 9.243   -24.984 -2.013  1.00 29.78  ? 75  MET C CG  1 
ATOM   4084 S SD  . MET C 3 84  ? 8.857   -26.660 -2.541  1.00 34.56  ? 75  MET C SD  1 
ATOM   4085 C CE  . MET C 3 84  ? 10.186  -27.524 -1.709  1.00 27.97  ? 75  MET C CE  1 
ATOM   4086 N N   . TYR C 3 85  ? 6.024   -21.744 -1.772  1.00 28.58  ? 76  TYR C N   1 
ATOM   4087 C CA  . TYR C 3 85  ? 5.042   -20.782 -2.250  1.00 29.64  ? 76  TYR C CA  1 
ATOM   4088 C C   . TYR C 3 85  ? 5.455   -19.359 -1.908  1.00 31.40  ? 76  TYR C C   1 
ATOM   4089 O O   . TYR C 3 85  ? 5.241   -18.439 -2.707  1.00 30.06  ? 76  TYR C O   1 
ATOM   4090 C CB  . TYR C 3 85  ? 3.650   -21.077 -1.688  1.00 28.65  ? 76  TYR C CB  1 
ATOM   4091 C CG  . TYR C 3 85  ? 2.696   -19.956 -2.048  1.00 29.95  ? 76  TYR C CG  1 
ATOM   4092 C CD1 . TYR C 3 85  ? 2.147   -19.874 -3.322  1.00 28.75  ? 76  TYR C CD1 1 
ATOM   4093 C CD2 . TYR C 3 85  ? 2.401   -18.935 -1.140  1.00 29.55  ? 76  TYR C CD2 1 
ATOM   4094 C CE1 . TYR C 3 85  ? 1.294   -18.824 -3.670  1.00 29.50  ? 76  TYR C CE1 1 
ATOM   4095 C CE2 . TYR C 3 85  ? 1.554   -17.880 -1.487  1.00 31.19  ? 76  TYR C CE2 1 
ATOM   4096 C CZ  . TYR C 3 85  ? 1.000   -17.836 -2.748  1.00 30.46  ? 76  TYR C CZ  1 
ATOM   4097 O OH  . TYR C 3 85  ? 0.168   -16.802 -3.104  1.00 33.02  ? 76  TYR C OH  1 
ATOM   4098 N N   . PHE C 3 86  ? 5.998   -19.149 -0.705  1.00 31.36  ? 77  PHE C N   1 
ATOM   4099 C CA  . PHE C 3 86  ? 6.549   -17.841 -0.361  1.00 30.87  ? 77  PHE C CA  1 
ATOM   4100 C C   . PHE C 3 86  ? 7.547   -17.396 -1.417  1.00 31.76  ? 77  PHE C C   1 
ATOM   4101 O O   . PHE C 3 86  ? 7.461   -16.281 -1.942  1.00 34.83  ? 77  PHE C O   1 
ATOM   4102 C CB  . PHE C 3 86  ? 7.254   -17.876 1.003   1.00 34.02  ? 77  PHE C CB  1 
ATOM   4103 C CG  . PHE C 3 86  ? 6.348   -18.099 2.185   1.00 33.20  ? 77  PHE C CG  1 
ATOM   4104 C CD1 . PHE C 3 86  ? 4.962   -17.928 2.084   1.00 33.24  ? 77  PHE C CD1 1 
ATOM   4105 C CD2 . PHE C 3 86  ? 6.899   -18.453 3.419   1.00 28.99  ? 77  PHE C CD2 1 
ATOM   4106 C CE1 . PHE C 3 86  ? 4.130   -18.135 3.190   1.00 30.40  ? 77  PHE C CE1 1 
ATOM   4107 C CE2 . PHE C 3 86  ? 6.076   -18.655 4.527   1.00 32.95  ? 77  PHE C CE2 1 
ATOM   4108 C CZ  . PHE C 3 86  ? 4.683   -18.502 4.406   1.00 29.99  ? 77  PHE C CZ  1 
ATOM   4109 N N   . THR C 3 87  ? 8.510   -18.267 -1.735  1.00 31.47  ? 78  THR C N   1 
ATOM   4110 C CA  . THR C 3 87  ? 9.567   -17.903 -2.672  1.00 34.52  ? 78  THR C CA  1 
ATOM   4111 C C   . THR C 3 87  ? 8.973   -17.588 -4.034  1.00 33.05  ? 78  THR C C   1 
ATOM   4112 O O   . THR C 3 87  ? 9.303   -16.574 -4.662  1.00 33.40  ? 78  THR C O   1 
ATOM   4113 C CB  . THR C 3 87  ? 10.591  -19.042 -2.779  1.00 33.71  ? 78  THR C CB  1 
ATOM   4114 O OG1 . THR C 3 87  ? 11.038  -19.418 -1.476  1.00 32.85  ? 78  THR C OG1 1 
ATOM   4115 C CG2 . THR C 3 87  ? 11.796  -18.622 -3.605  1.00 30.21  ? 78  THR C CG2 1 
ATOM   4116 N N   . TYR C 3 88  ? 8.061   -18.442 -4.483  1.00 32.17  ? 79  TYR C N   1 
ATOM   4117 C CA  . TYR C 3 88  ? 7.409   -18.250 -5.768  1.00 31.77  ? 79  TYR C CA  1 
ATOM   4118 C C   . TYR C 3 88  ? 6.647   -16.929 -5.800  1.00 34.49  ? 79  TYR C C   1 
ATOM   4119 O O   . TYR C 3 88  ? 6.758   -16.160 -6.764  1.00 36.70  ? 79  TYR C O   1 
ATOM   4120 C CB  . TYR C 3 88  ? 6.498   -19.454 -6.006  1.00 31.90  ? 79  TYR C CB  1 
ATOM   4121 C CG  . TYR C 3 88  ? 5.557   -19.414 -7.188  1.00 35.61  ? 79  TYR C CG  1 
ATOM   4122 C CD1 . TYR C 3 88  ? 5.962   -19.871 -8.433  1.00 35.85  ? 79  TYR C CD1 1 
ATOM   4123 C CD2 . TYR C 3 88  ? 4.230   -18.990 -7.037  1.00 32.77  ? 79  TYR C CD2 1 
ATOM   4124 C CE1 . TYR C 3 88  ? 5.093   -19.872 -9.510  1.00 39.43  ? 79  TYR C CE1 1 
ATOM   4125 C CE2 . TYR C 3 88  ? 3.352   -18.980 -8.116  1.00 37.12  ? 79  TYR C CE2 1 
ATOM   4126 C CZ  . TYR C 3 88  ? 3.791   -19.426 -9.350  1.00 37.58  ? 79  TYR C CZ  1 
ATOM   4127 O OH  . TYR C 3 88  ? 2.939   -19.431 -10.422 1.00 36.50  ? 79  TYR C OH  1 
ATOM   4128 N N   . LYS C 3 89  ? 5.912   -16.626 -4.728  1.00 32.81  ? 80  LYS C N   1 
ATOM   4129 C CA  . LYS C 3 89  ? 5.069   -15.439 -4.705  1.00 32.23  ? 80  LYS C CA  1 
ATOM   4130 C C   . LYS C 3 89  ? 5.903   -14.173 -4.807  1.00 36.38  ? 80  LYS C C   1 
ATOM   4131 O O   . LYS C 3 89  ? 5.630   -13.294 -5.635  1.00 36.62  ? 80  LYS C O   1 
ATOM   4132 C CB  . LYS C 3 89  ? 4.233   -15.432 -3.423  1.00 34.67  ? 80  LYS C CB  1 
ATOM   4133 C CG  . LYS C 3 89  ? 3.442   -14.160 -3.207  1.00 37.17  ? 80  LYS C CG  1 
ATOM   4134 C CD  . LYS C 3 89  ? 2.245   -14.119 -4.116  1.00 34.45  ? 80  LYS C CD  1 
ATOM   4135 C CE  . LYS C 3 89  ? 1.140   -13.271 -3.492  1.00 39.18  ? 80  LYS C CE  1 
ATOM   4136 N NZ  . LYS C 3 89  ? -0.234  -13.836 -3.758  1.00 41.18  ? 80  LYS C NZ  1 
ATOM   4137 N N   . VAL C 3 90  ? 6.936   -14.071 -3.970  1.00 35.39  ? 81  VAL C N   1 
ATOM   4138 C CA  . VAL C 3 90  ? 7.779   -12.886 -3.960  1.00 34.98  ? 81  VAL C CA  1 
ATOM   4139 C C   . VAL C 3 90  ? 8.532   -12.757 -5.280  1.00 38.43  ? 81  VAL C C   1 
ATOM   4140 O O   . VAL C 3 90  ? 8.683   -11.653 -5.811  1.00 42.53  ? 81  VAL C O   1 
ATOM   4141 C CB  . VAL C 3 90  ? 8.736   -12.927 -2.752  1.00 37.57  ? 81  VAL C CB  1 
ATOM   4142 C CG1 . VAL C 3 90  ? 9.736   -11.789 -2.822  1.00 35.63  ? 81  VAL C CG1 1 
ATOM   4143 C CG2 . VAL C 3 90  ? 7.954   -12.878 -1.439  1.00 34.71  ? 81  VAL C CG2 1 
ATOM   4144 N N   . ARG C 3 91  ? 8.992   -13.878 -5.849  1.00 33.89  ? 82  ARG C N   1 
ATOM   4145 C CA  . ARG C 3 91  ? 9.766   -13.788 -7.086  1.00 35.01  ? 82  ARG C CA  1 
ATOM   4146 C C   . ARG C 3 91  ? 8.901   -13.399 -8.276  1.00 39.45  ? 82  ARG C C   1 
ATOM   4147 O O   . ARG C 3 91  ? 9.368   -12.687 -9.170  1.00 42.19  ? 82  ARG C O   1 
ATOM   4148 C CB  . ARG C 3 91  ? 10.490  -15.112 -7.373  1.00 35.26  ? 82  ARG C CB  1 
ATOM   4149 C CG  . ARG C 3 91  ? 11.092  -15.237 -8.781  1.00 36.93  ? 82  ARG C CG  1 
ATOM   4150 C CD  . ARG C 3 91  ? 12.131  -14.152 -9.101  1.00 37.42  ? 82  ARG C CD  1 
ATOM   4151 N NE  . ARG C 3 91  ? 12.713  -14.306 -10.434 1.00 44.22  ? 82  ARG C NE  1 
ATOM   4152 C CZ  . ARG C 3 91  ? 12.194  -13.796 -11.547 1.00 47.49  ? 82  ARG C CZ  1 
ATOM   4153 N NH1 . ARG C 3 91  ? 11.070  -13.099 -11.530 1.00 46.29  ? 82  ARG C NH1 1 
ATOM   4154 N NH2 . ARG C 3 91  ? 12.817  -13.992 -12.709 1.00 42.46  ? 82  ARG C NH2 1 
ATOM   4155 N N   . TYR C 3 92  ? 7.650   -13.846 -8.326  1.00 37.49  ? 83  TYR C N   1 
ATOM   4156 C CA  . TYR C 3 92  ? 6.863   -13.654 -9.530  1.00 41.37  ? 83  TYR C CA  1 
ATOM   4157 C C   . TYR C 3 92  ? 5.759   -12.611 -9.385  1.00 44.32  ? 83  TYR C C   1 
ATOM   4158 O O   . TYR C 3 92  ? 4.940   -12.469 -10.291 1.00 47.11  ? 83  TYR C O   1 
ATOM   4159 C CB  . TYR C 3 92  ? 6.289   -14.989 -9.975  1.00 41.08  ? 83  TYR C CB  1 
ATOM   4160 C CG  . TYR C 3 92  ? 7.320   -15.958 -10.475 1.00 39.53  ? 83  TYR C CG  1 
ATOM   4161 C CD1 . TYR C 3 92  ? 8.212   -15.609 -11.482 1.00 43.20  ? 83  TYR C CD1 1 
ATOM   4162 C CD2 . TYR C 3 92  ? 7.402   -17.238 -9.943  1.00 41.44  ? 83  TYR C CD2 1 
ATOM   4163 C CE1 . TYR C 3 92  ? 9.169   -16.522 -11.947 1.00 42.62  ? 83  TYR C CE1 1 
ATOM   4164 C CE2 . TYR C 3 92  ? 8.345   -18.153 -10.400 1.00 42.66  ? 83  TYR C CE2 1 
ATOM   4165 C CZ  . TYR C 3 92  ? 9.223   -17.793 -11.399 1.00 41.85  ? 83  TYR C CZ  1 
ATOM   4166 O OH  . TYR C 3 92  ? 10.136  -18.714 -11.844 1.00 38.63  ? 83  TYR C OH  1 
ATOM   4167 N N   . THR C 3 93  ? 5.723   -11.865 -8.290  1.00 46.24  ? 84  THR C N   1 
ATOM   4168 C CA  . THR C 3 93  ? 4.762   -10.774 -8.181  1.00 53.17  ? 84  THR C CA  1 
ATOM   4169 C C   . THR C 3 93  ? 5.099   -9.681  -9.191  1.00 62.29  ? 84  THR C C   1 
ATOM   4170 O O   . THR C 3 93  ? 6.271   -9.398  -9.453  1.00 61.99  ? 84  THR C O   1 
ATOM   4171 C CB  . THR C 3 93  ? 4.751   -10.221 -6.754  1.00 50.89  ? 84  THR C CB  1 
ATOM   4172 O OG1 . THR C 3 93  ? 4.117   -11.168 -5.880  1.00 49.06  ? 84  THR C OG1 1 
ATOM   4173 C CG2 . THR C 3 93  ? 4.006   -8.919  -6.687  1.00 57.20  ? 84  THR C CG2 1 
ATOM   4174 N N   . ASN C 3 94  ? 4.062   -9.088  -9.788  1.00 75.41  ? 85  ASN C N   1 
ATOM   4175 C CA  . ASN C 3 94  ? 4.238   -8.029  -10.784 1.00 79.80  ? 85  ASN C CA  1 
ATOM   4176 C C   . ASN C 3 94  ? 5.142   -8.496  -11.922 1.00 80.03  ? 85  ASN C C   1 
ATOM   4177 O O   . ASN C 3 94  ? 6.007   -7.760  -12.404 1.00 82.62  ? 85  ASN C O   1 
ATOM   4178 C CB  . ASN C 3 94  ? 4.783   -6.749  -10.145 1.00 79.97  ? 85  ASN C CB  1 
ATOM   4179 C CG  . ASN C 3 94  ? 3.929   -6.263  -8.986  1.00 80.33  ? 85  ASN C CG  1 
ATOM   4180 O OD1 . ASN C 3 94  ? 2.718   -6.480  -8.956  1.00 80.33  ? 85  ASN C OD1 1 
ATOM   4181 N ND2 . ASN C 3 94  ? 4.561   -5.604  -8.022  1.00 83.37  ? 85  ASN C ND2 1 
ATOM   4182 N N   . SER C 3 95  ? 4.945   -9.742  -12.341 1.00 67.04  ? 86  SER C N   1 
ATOM   4183 C CA  . SER C 3 95  ? 5.677   -10.358 -13.437 1.00 61.96  ? 86  SER C CA  1 
ATOM   4184 C C   . SER C 3 95  ? 4.688   -10.826 -14.500 1.00 59.43  ? 86  SER C C   1 
ATOM   4185 O O   . SER C 3 95  ? 3.630   -11.376 -14.173 1.00 61.30  ? 86  SER C O   1 
ATOM   4186 C CB  . SER C 3 95  ? 6.526   -11.528 -12.919 1.00 57.26  ? 86  SER C CB  1 
ATOM   4187 O OG  . SER C 3 95  ? 6.553   -12.602 -13.840 1.00 61.36  ? 86  SER C OG  1 
ATOM   4188 N N   . SER C 3 96  ? 5.021   -10.585 -15.774 1.00 60.22  ? 87  SER C N   1 
ATOM   4189 C CA  . SER C 3 96  ? 4.151   -10.938 -16.892 1.00 57.86  ? 87  SER C CA  1 
ATOM   4190 C C   . SER C 3 96  ? 4.732   -11.996 -17.817 1.00 59.69  ? 87  SER C C   1 
ATOM   4191 O O   . SER C 3 96  ? 3.979   -12.592 -18.595 1.00 62.01  ? 87  SER C O   1 
ATOM   4192 C CB  . SER C 3 96  ? 3.801   -9.696  -17.731 1.00 50.04  ? 87  SER C CB  1 
ATOM   4193 O OG  . SER C 3 96  ? 4.940   -9.123  -18.358 1.00 50.05  ? 87  SER C OG  1 
ATOM   4194 N N   . THR C 3 97  ? 6.034   -12.238 -17.758 1.00 59.97  ? 88  THR C N   1 
ATOM   4195 C CA  . THR C 3 97  ? 6.639   -13.323 -18.512 1.00 62.65  ? 88  THR C CA  1 
ATOM   4196 C C   . THR C 3 97  ? 6.021   -14.659 -18.100 1.00 63.29  ? 88  THR C C   1 
ATOM   4197 O O   . THR C 3 97  ? 5.700   -14.878 -16.927 1.00 64.12  ? 88  THR C O   1 
ATOM   4198 C CB  . THR C 3 97  ? 8.153   -13.316 -18.269 1.00 59.90  ? 88  THR C CB  1 
ATOM   4199 O OG1 . THR C 3 97  ? 8.717   -14.551 -18.714 1.00 61.33  ? 88  THR C OG1 1 
ATOM   4200 C CG2 . THR C 3 97  ? 8.454   -13.131 -16.785 1.00 62.06  ? 88  THR C CG2 1 
ATOM   4201 N N   . GLU C 3 98  ? 5.833   -15.553 -19.073 1.00 62.32  ? 89  GLU C N   1 
ATOM   4202 C CA  . GLU C 3 98  ? 5.224   -16.845 -18.773 1.00 61.17  ? 89  GLU C CA  1 
ATOM   4203 C C   . GLU C 3 98  ? 6.139   -17.694 -17.892 1.00 59.98  ? 89  GLU C C   1 
ATOM   4204 O O   . GLU C 3 98  ? 7.355   -17.762 -18.093 1.00 58.40  ? 89  GLU C O   1 
ATOM   4205 C CB  . GLU C 3 98  ? 4.874   -17.603 -20.056 1.00 65.20  ? 89  GLU C CB  1 
ATOM   4206 C CG  . GLU C 3 98  ? 4.305   -19.001 -19.784 1.00 64.39  ? 89  GLU C CG  1 
ATOM   4207 C CD  . GLU C 3 98  ? 3.296   -19.452 -20.820 1.00 70.43  ? 89  GLU C CD  1 
ATOM   4208 O OE1 . GLU C 3 98  ? 3.676   -19.575 -22.007 1.00 75.55  ? 89  GLU C OE1 1 
ATOM   4209 O OE2 . GLU C 3 98  ? 2.120   -19.675 -20.441 1.00 70.72  ? 89  GLU C OE2 1 
ATOM   4210 N N   . ILE C 3 99  ? 5.531   -18.342 -16.905 1.00 57.97  ? 90  ILE C N   1 
ATOM   4211 C CA  . ILE C 3 99  ? 6.231   -19.072 -15.852 1.00 54.37  ? 90  ILE C CA  1 
ATOM   4212 C C   . ILE C 3 99  ? 5.440   -20.333 -15.555 1.00 52.14  ? 90  ILE C C   1 
ATOM   4213 O O   . ILE C 3 99  ? 4.265   -20.432 -15.911 1.00 54.89  ? 90  ILE C O   1 
ATOM   4214 C CB  . ILE C 3 99  ? 6.360   -18.231 -14.577 1.00 54.71  ? 90  ILE C CB  1 
ATOM   4215 C CG1 . ILE C 3 99  ? 4.967   -17.794 -14.133 1.00 50.63  ? 90  ILE C CG1 1 
ATOM   4216 C CG2 . ILE C 3 99  ? 7.243   -17.005 -14.829 1.00 57.14  ? 90  ILE C CG2 1 
ATOM   4217 C CD1 . ILE C 3 99  ? 4.940   -17.144 -12.784 1.00 48.60  ? 90  ILE C CD1 1 
ATOM   4218 N N   . PRO C 3 100 ? 6.066   -21.317 -14.921 1.00 54.25  ? 91  PRO C N   1 
ATOM   4219 C CA  . PRO C 3 100 ? 5.315   -22.525 -14.573 1.00 52.79  ? 91  PRO C CA  1 
ATOM   4220 C C   . PRO C 3 100 ? 4.279   -22.243 -13.502 1.00 45.70  ? 91  PRO C C   1 
ATOM   4221 O O   . PRO C 3 100 ? 4.289   -21.214 -12.819 1.00 45.46  ? 91  PRO C O   1 
ATOM   4222 C CB  . PRO C 3 100 ? 6.393   -23.488 -14.065 1.00 54.32  ? 91  PRO C CB  1 
ATOM   4223 C CG  . PRO C 3 100 ? 7.621   -23.026 -14.735 1.00 57.77  ? 91  PRO C CG  1 
ATOM   4224 C CD  . PRO C 3 100 ? 7.504   -21.521 -14.728 1.00 56.49  ? 91  PRO C CD  1 
ATOM   4225 N N   . GLU C 3 101 ? 3.349   -23.171 -13.385 1.00 43.54  ? 92  GLU C N   1 
ATOM   4226 C CA  . GLU C 3 101 ? 2.397   -23.022 -12.312 1.00 41.24  ? 92  GLU C CA  1 
ATOM   4227 C C   . GLU C 3 101 ? 3.032   -23.470 -11.000 1.00 42.14  ? 92  GLU C C   1 
ATOM   4228 O O   . GLU C 3 101 ? 4.141   -24.015 -10.958 1.00 43.59  ? 92  GLU C O   1 
ATOM   4229 C CB  . GLU C 3 101 ? 1.133   -23.815 -12.602 1.00 43.47  ? 92  GLU C CB  1 
ATOM   4230 C CG  . GLU C 3 101 ? 1.263   -25.286 -12.300 1.00 44.82  ? 92  GLU C CG  1 
ATOM   4231 C CD  . GLU C 3 101 ? -0.083  -25.984 -12.327 1.00 53.99  ? 92  GLU C CD  1 
ATOM   4232 O OE1 . GLU C 3 101 ? -0.100  -27.225 -12.154 1.00 61.44  ? 92  GLU C OE1 1 
ATOM   4233 O OE2 . GLU C 3 101 ? -1.121  -25.291 -12.516 1.00 52.80  ? 92  GLU C OE2 1 
ATOM   4234 N N   . PHE C 3 102 ? 2.329   -23.196 -9.909  1.00 40.52  ? 93  PHE C N   1 
ATOM   4235 C CA  . PHE C 3 102 ? 2.736   -23.709 -8.617  1.00 33.56  ? 93  PHE C CA  1 
ATOM   4236 C C   . PHE C 3 102 ? 2.138   -25.098 -8.470  1.00 35.18  ? 93  PHE C C   1 
ATOM   4237 O O   . PHE C 3 102 ? 0.916   -25.219 -8.314  1.00 38.44  ? 93  PHE C O   1 
ATOM   4238 C CB  . PHE C 3 102 ? 2.269   -22.802 -7.503  1.00 32.80  ? 93  PHE C CB  1 
ATOM   4239 C CG  . PHE C 3 102 ? 2.836   -23.177 -6.171  1.00 36.42  ? 93  PHE C CG  1 
ATOM   4240 C CD1 . PHE C 3 102 ? 4.110   -22.764 -5.818  1.00 32.76  ? 93  PHE C CD1 1 
ATOM   4241 C CD2 . PHE C 3 102 ? 2.112   -23.970 -5.290  1.00 31.01  ? 93  PHE C CD2 1 
ATOM   4242 C CE1 . PHE C 3 102 ? 4.655   -23.122 -4.609  1.00 33.71  ? 93  PHE C CE1 1 
ATOM   4243 C CE2 . PHE C 3 102 ? 2.648   -24.336 -4.088  1.00 33.10  ? 93  PHE C CE2 1 
ATOM   4244 C CZ  . PHE C 3 102 ? 3.931   -23.903 -3.733  1.00 34.97  ? 93  PHE C CZ  1 
ATOM   4245 N N   . PRO C 3 103 ? 2.937   -26.162 -8.504  1.00 34.62  ? 94  PRO C N   1 
ATOM   4246 C CA  . PRO C 3 103 ? 2.368   -27.511 -8.581  1.00 36.98  ? 94  PRO C CA  1 
ATOM   4247 C C   . PRO C 3 103 ? 1.833   -27.937 -7.220  1.00 36.72  ? 94  PRO C C   1 
ATOM   4248 O O   . PRO C 3 103 ? 2.492   -27.740 -6.196  1.00 32.58  ? 94  PRO C O   1 
ATOM   4249 C CB  . PRO C 3 103 ? 3.564   -28.368 -9.008  1.00 34.38  ? 94  PRO C CB  1 
ATOM   4250 C CG  . PRO C 3 103 ? 4.731   -27.670 -8.383  1.00 34.80  ? 94  PRO C CG  1 
ATOM   4251 C CD  . PRO C 3 103 ? 4.404   -26.194 -8.334  1.00 35.91  ? 94  PRO C CD  1 
ATOM   4252 N N   . ILE C 3 104 ? 0.629   -28.509 -7.210  1.00 34.67  ? 95  ILE C N   1 
ATOM   4253 C CA  . ILE C 3 104 ? 0.002   -29.001 -5.987  1.00 35.06  ? 95  ILE C CA  1 
ATOM   4254 C C   . ILE C 3 104 ? -0.473  -30.427 -6.245  1.00 38.13  ? 95  ILE C C   1 
ATOM   4255 O O   . ILE C 3 104 ? -1.483  -30.637 -6.927  1.00 37.42  ? 95  ILE C O   1 
ATOM   4256 C CB  . ILE C 3 104 ? -1.159  -28.111 -5.533  1.00 32.93  ? 95  ILE C CB  1 
ATOM   4257 C CG1 . ILE C 3 104 ? -0.688  -26.667 -5.375  1.00 30.94  ? 95  ILE C CG1 1 
ATOM   4258 C CG2 . ILE C 3 104 ? -1.753  -28.635 -4.233  1.00 30.60  ? 95  ILE C CG2 1 
ATOM   4259 C CD1 . ILE C 3 104 ? -1.794  -25.691 -5.018  1.00 29.73  ? 95  ILE C CD1 1 
ATOM   4260 N N   . ALA C 3 105 ? 0.254   -31.401 -5.697  1.00 41.52  ? 96  ALA C N   1 
ATOM   4261 C CA  . ALA C 3 105 ? -0.102  -32.804 -5.816  1.00 37.59  ? 96  ALA C CA  1 
ATOM   4262 C C   . ALA C 3 105 ? -1.428  -33.088 -5.107  1.00 41.48  ? 96  ALA C C   1 
ATOM   4263 O O   . ALA C 3 105 ? -1.735  -32.483 -4.075  1.00 37.48  ? 96  ALA C O   1 
ATOM   4264 C CB  . ALA C 3 105 ? 0.996   -33.677 -5.219  1.00 34.09  ? 96  ALA C CB  1 
ATOM   4265 N N   . PRO C 3 106 ? -2.234  -34.010 -5.646  1.00 44.57  ? 97  PRO C N   1 
ATOM   4266 C CA  . PRO C 3 106 ? -3.520  -34.326 -4.995  1.00 42.35  ? 97  PRO C CA  1 
ATOM   4267 C C   . PRO C 3 106 ? -3.365  -34.803 -3.559  1.00 43.39  ? 97  PRO C C   1 
ATOM   4268 O O   . PRO C 3 106 ? -4.202  -34.478 -2.704  1.00 41.74  ? 97  PRO C O   1 
ATOM   4269 C CB  . PRO C 3 106 ? -4.105  -35.428 -5.889  1.00 39.51  ? 97  PRO C CB  1 
ATOM   4270 C CG  . PRO C 3 106 ? -3.303  -35.413 -7.150  1.00 41.97  ? 97  PRO C CG  1 
ATOM   4271 C CD  . PRO C 3 106 ? -1.973  -34.845 -6.832  1.00 42.94  ? 97  PRO C CD  1 
ATOM   4272 N N   . GLU C 3 107 ? -2.298  -35.558 -3.271  1.00 42.08  ? 98  GLU C N   1 
ATOM   4273 C CA  . GLU C 3 107 ? -2.101  -36.147 -1.948  1.00 45.57  ? 98  GLU C CA  1 
ATOM   4274 C C   . GLU C 3 107 ? -1.865  -35.098 -0.876  1.00 42.28  ? 98  GLU C C   1 
ATOM   4275 O O   . GLU C 3 107 ? -1.982  -35.405 0.313   1.00 46.03  ? 98  GLU C O   1 
ATOM   4276 C CB  . GLU C 3 107 ? -0.916  -37.125 -1.968  1.00 46.08  ? 98  GLU C CB  1 
ATOM   4277 C CG  . GLU C 3 107 ? -0.805  -37.952 -3.246  1.00 46.61  ? 98  GLU C CG  1 
ATOM   4278 C CD  . GLU C 3 107 ? 0.066   -37.279 -4.317  1.00 52.46  ? 98  GLU C CD  1 
ATOM   4279 O OE1 . GLU C 3 107 ? 1.185   -36.807 -3.983  1.00 57.93  ? 98  GLU C OE1 1 
ATOM   4280 O OE2 . GLU C 3 107 ? -0.360  -37.224 -5.494  1.00 54.97  ? 98  GLU C OE2 1 
ATOM   4281 N N   . ILE C 3 108 ? -1.546  -33.873 -1.274  1.00 38.29  ? 99  ILE C N   1 
ATOM   4282 C CA  . ILE C 3 108 ? -1.196  -32.812 -0.342  1.00 38.62  ? 99  ILE C CA  1 
ATOM   4283 C C   . ILE C 3 108 ? -2.217  -31.686 -0.336  1.00 37.96  ? 99  ILE C C   1 
ATOM   4284 O O   . ILE C 3 108 ? -2.130  -30.799 0.530   1.00 37.76  ? 99  ILE C O   1 
ATOM   4285 C CB  . ILE C 3 108 ? 0.210   -32.255 -0.653  1.00 42.08  ? 99  ILE C CB  1 
ATOM   4286 C CG1 . ILE C 3 108 ? 0.862   -31.687 0.600   1.00 41.79  ? 99  ILE C CG1 1 
ATOM   4287 C CG2 . ILE C 3 108 ? 0.148   -31.196 -1.764  1.00 34.66  ? 99  ILE C CG2 1 
ATOM   4288 C CD1 . ILE C 3 108 ? 2.131   -30.939 0.297   1.00 40.08  ? 99  ILE C CD1 1 
ATOM   4289 N N   . ALA C 3 109 ? -3.195  -31.708 -1.249  1.00 37.42  ? 100 ALA C N   1 
ATOM   4290 C CA  . ALA C 3 109 ? -4.027  -30.536 -1.496  1.00 35.34  ? 100 ALA C CA  1 
ATOM   4291 C C   . ALA C 3 109 ? -4.871  -30.160 -0.279  1.00 35.01  ? 100 ALA C C   1 
ATOM   4292 O O   . ALA C 3 109 ? -4.971  -28.977 0.063   1.00 33.91  ? 100 ALA C O   1 
ATOM   4293 C CB  . ALA C 3 109 ? -4.909  -30.777 -2.719  1.00 33.28  ? 100 ALA C CB  1 
ATOM   4294 N N   . LEU C 3 110 ? -5.491  -31.139 0.380   1.00 33.41  ? 101 LEU C N   1 
ATOM   4295 C CA  . LEU C 3 110 ? -6.329  -30.831 1.536   1.00 34.71  ? 101 LEU C CA  1 
ATOM   4296 C C   . LEU C 3 110 ? -5.513  -30.231 2.679   1.00 37.81  ? 101 LEU C C   1 
ATOM   4297 O O   . LEU C 3 110 ? -5.903  -29.218 3.274   1.00 37.87  ? 101 LEU C O   1 
ATOM   4298 C CB  . LEU C 3 110 ? -7.051  -32.086 2.006   1.00 31.68  ? 101 LEU C CB  1 
ATOM   4299 C CG  . LEU C 3 110 ? -8.225  -32.622 1.180   1.00 34.66  ? 101 LEU C CG  1 
ATOM   4300 C CD1 . LEU C 3 110 ? -8.775  -33.860 1.857   1.00 32.87  ? 101 LEU C CD1 1 
ATOM   4301 C CD2 . LEU C 3 110 ? -9.331  -31.577 0.990   1.00 31.93  ? 101 LEU C CD2 1 
ATOM   4302 N N   . GLU C 3 111 ? -4.373  -30.842 3.006   1.00 35.87  ? 102 GLU C N   1 
ATOM   4303 C CA  . GLU C 3 111 ? -3.546  -30.289 4.072   1.00 35.44  ? 102 GLU C CA  1 
ATOM   4304 C C   . GLU C 3 111 ? -2.986  -28.928 3.692   1.00 34.21  ? 102 GLU C C   1 
ATOM   4305 O O   . GLU C 3 111 ? -2.925  -28.014 4.527   1.00 33.60  ? 102 GLU C O   1 
ATOM   4306 C CB  . GLU C 3 111 ? -2.399  -31.228 4.391   1.00 37.54  ? 102 GLU C CB  1 
ATOM   4307 C CG  . GLU C 3 111 ? -2.803  -32.575 4.862   1.00 40.89  ? 102 GLU C CG  1 
ATOM   4308 C CD  . GLU C 3 111 ? -1.583  -33.453 5.054   1.00 49.51  ? 102 GLU C CD  1 
ATOM   4309 O OE1 . GLU C 3 111 ? -1.138  -34.067 4.050   1.00 50.98  ? 102 GLU C OE1 1 
ATOM   4310 O OE2 . GLU C 3 111 ? -1.054  -33.488 6.198   1.00 43.36  ? 102 GLU C OE2 1 
ATOM   4311 N N   . LEU C 3 112 ? -2.540  -28.785 2.442   1.00 34.12  ? 103 LEU C N   1 
ATOM   4312 C CA  . LEU C 3 112 ? -2.002  -27.502 2.006   1.00 33.75  ? 103 LEU C CA  1 
ATOM   4313 C C   . LEU C 3 112 ? -3.061  -26.409 2.101   1.00 32.13  ? 103 LEU C C   1 
ATOM   4314 O O   . LEU C 3 112 ? -2.780  -25.301 2.579   1.00 28.31  ? 103 LEU C O   1 
ATOM   4315 C CB  . LEU C 3 112 ? -1.456  -27.621 0.584   1.00 29.73  ? 103 LEU C CB  1 
ATOM   4316 C CG  . LEU C 3 112 ? -0.510  -26.496 0.166   1.00 30.08  ? 103 LEU C CG  1 
ATOM   4317 C CD1 . LEU C 3 112 ? 0.609   -26.310 1.183   1.00 26.86  ? 103 LEU C CD1 1 
ATOM   4318 C CD2 . LEU C 3 112 ? 0.036   -26.766 -1.226  1.00 28.49  ? 103 LEU C CD2 1 
ATOM   4319 N N   . LEU C 3 113 ? -4.297  -26.723 1.698   1.00 34.06  ? 104 LEU C N   1 
ATOM   4320 C CA  . LEU C 3 113 ? -5.389  -25.758 1.789   1.00 31.42  ? 104 LEU C CA  1 
ATOM   4321 C C   . LEU C 3 113 ? -5.642  -25.356 3.230   1.00 30.60  ? 104 LEU C C   1 
ATOM   4322 O O   . LEU C 3 113 ? -5.763  -24.168 3.547   1.00 32.05  ? 104 LEU C O   1 
ATOM   4323 C CB  . LEU C 3 113 ? -6.657  -26.341 1.173   1.00 29.91  ? 104 LEU C CB  1 
ATOM   4324 C CG  . LEU C 3 113 ? -7.932  -25.530 1.324   1.00 28.24  ? 104 LEU C CG  1 
ATOM   4325 C CD1 . LEU C 3 113 ? -7.726  -24.109 0.821   1.00 25.75  ? 104 LEU C CD1 1 
ATOM   4326 C CD2 . LEU C 3 113 ? -9.047  -26.222 0.557   1.00 30.80  ? 104 LEU C CD2 1 
ATOM   4327 N N   . MET C 3 114 ? -5.704  -26.333 4.126   1.00 30.81  ? 105 MET C N   1 
ATOM   4328 C CA  . MET C 3 114 ? -5.883  -26.003 5.535   1.00 31.42  ? 105 MET C CA  1 
ATOM   4329 C C   . MET C 3 114 ? -4.712  -25.178 6.061   1.00 32.71  ? 105 MET C C   1 
ATOM   4330 O O   . MET C 3 114 ? -4.916  -24.213 6.813   1.00 31.69  ? 105 MET C O   1 
ATOM   4331 C CB  . MET C 3 114 ? -6.088  -27.277 6.350   1.00 29.44  ? 105 MET C CB  1 
ATOM   4332 C CG  . MET C 3 114 ? -7.463  -27.883 6.136   1.00 34.10  ? 105 MET C CG  1 
ATOM   4333 S SD  . MET C 3 114 ? -7.794  -29.385 7.070   1.00 41.78  ? 105 MET C SD  1 
ATOM   4334 C CE  . MET C 3 114 ? -6.626  -30.517 6.292   1.00 36.84  ? 105 MET C CE  1 
ATOM   4335 N N   . ALA C 3 115 ? -3.479  -25.511 5.651   1.00 27.24  ? 106 ALA C N   1 
ATOM   4336 C CA  . ALA C 3 115 ? -2.347  -24.686 6.066   1.00 30.87  ? 106 ALA C CA  1 
ATOM   4337 C C   . ALA C 3 115 ? -2.465  -23.269 5.511   1.00 30.65  ? 106 ALA C C   1 
ATOM   4338 O O   . ALA C 3 115 ? -2.336  -22.293 6.254   1.00 33.27  ? 106 ALA C O   1 
ATOM   4339 C CB  . ALA C 3 115 ? -1.020  -25.327 5.653   1.00 30.32  ? 106 ALA C CB  1 
ATOM   4340 N N   . ALA C 3 116 ? -2.733  -23.131 4.210   1.00 31.38  ? 107 ALA C N   1 
ATOM   4341 C CA  . ALA C 3 116 ? -2.820  -21.788 3.638   1.00 30.84  ? 107 ALA C CA  1 
ATOM   4342 C C   . ALA C 3 116 ? -3.905  -20.972 4.329   1.00 32.77  ? 107 ALA C C   1 
ATOM   4343 O O   . ALA C 3 116 ? -3.723  -19.782 4.602   1.00 34.58  ? 107 ALA C O   1 
ATOM   4344 C CB  . ALA C 3 116 ? -3.080  -21.852 2.134   1.00 25.14  ? 107 ALA C CB  1 
ATOM   4345 N N   . ASN C 3 117 ? -5.037  -21.597 4.635   1.00 31.66  ? 108 ASN C N   1 
ATOM   4346 C CA  . ASN C 3 117 ? -6.085  -20.881 5.349   1.00 31.07  ? 108 ASN C CA  1 
ATOM   4347 C C   . ASN C 3 117 ? -5.643  -20.477 6.749   1.00 34.06  ? 108 ASN C C   1 
ATOM   4348 O O   . ASN C 3 117 ? -5.919  -19.359 7.193   1.00 32.15  ? 108 ASN C O   1 
ATOM   4349 C CB  . ASN C 3 117 ? -7.335  -21.725 5.448   1.00 31.54  ? 108 ASN C CB  1 
ATOM   4350 C CG  . ASN C 3 117 ? -8.492  -20.933 5.950   1.00 33.25  ? 108 ASN C CG  1 
ATOM   4351 O OD1 . ASN C 3 117 ? -8.675  -19.779 5.560   1.00 37.78  ? 108 ASN C OD1 1 
ATOM   4352 N ND2 . ASN C 3 117 ? -9.256  -21.513 6.854   1.00 34.42  ? 108 ASN C ND2 1 
ATOM   4353 N N   . PHE C 3 118 ? -4.976  -21.379 7.472   1.00 32.87  ? 109 PHE C N   1 
ATOM   4354 C CA  . PHE C 3 118 ? -4.484  -21.020 8.793   1.00 32.46  ? 109 PHE C CA  1 
ATOM   4355 C C   . PHE C 3 118 ? -3.428  -19.917 8.713   1.00 35.66  ? 109 PHE C C   1 
ATOM   4356 O O   . PHE C 3 118 ? -3.345  -19.059 9.602   1.00 35.90  ? 109 PHE C O   1 
ATOM   4357 C CB  . PHE C 3 118 ? -3.923  -22.253 9.489   1.00 33.41  ? 109 PHE C CB  1 
ATOM   4358 C CG  . PHE C 3 118 ? -3.133  -21.937 10.732  1.00 37.40  ? 109 PHE C CG  1 
ATOM   4359 C CD1 . PHE C 3 118 ? -3.773  -21.755 11.951  1.00 35.07  ? 109 PHE C CD1 1 
ATOM   4360 C CD2 . PHE C 3 118 ? -1.755  -21.818 10.683  1.00 34.44  ? 109 PHE C CD2 1 
ATOM   4361 C CE1 . PHE C 3 118 ? -3.061  -21.465 13.085  1.00 39.23  ? 109 PHE C CE1 1 
ATOM   4362 C CE2 . PHE C 3 118 ? -1.037  -21.524 11.821  1.00 37.79  ? 109 PHE C CE2 1 
ATOM   4363 C CZ  . PHE C 3 118 ? -1.688  -21.351 13.026  1.00 42.13  ? 109 PHE C CZ  1 
ATOM   4364 N N   . LEU C 3 119 ? -2.612  -19.921 7.663   1.00 32.06  ? 110 LEU C N   1 
ATOM   4365 C CA  . LEU C 3 119 ? -1.504  -18.984 7.548   1.00 34.38  ? 110 LEU C CA  1 
ATOM   4366 C C   . LEU C 3 119 ? -1.891  -17.689 6.858   1.00 35.24  ? 110 LEU C C   1 
ATOM   4367 O O   . LEU C 3 119 ? -1.047  -16.795 6.738   1.00 35.12  ? 110 LEU C O   1 
ATOM   4368 C CB  . LEU C 3 119 ? -0.334  -19.638 6.796   1.00 33.31  ? 110 LEU C CB  1 
ATOM   4369 C CG  . LEU C 3 119 ? 0.261   -20.879 7.460   1.00 32.40  ? 110 LEU C CG  1 
ATOM   4370 C CD1 . LEU C 3 119 ? 1.229   -21.614 6.518   1.00 31.58  ? 110 LEU C CD1 1 
ATOM   4371 C CD2 . LEU C 3 119 ? 0.950   -20.487 8.772   1.00 34.94  ? 110 LEU C CD2 1 
ATOM   4372 N N   . ASP C 3 120 ? -3.137  -17.579 6.408   1.00 36.22  ? 111 ASP C N   1 
ATOM   4373 C CA  . ASP C 3 120 ? -3.625  -16.463 5.603   1.00 38.17  ? 111 ASP C CA  1 
ATOM   4374 C C   . ASP C 3 120 ? -2.647  -16.091 4.486   1.00 37.86  ? 111 ASP C C   1 
ATOM   4375 O O   . ASP C 3 120 ? -2.099  -14.984 4.434   1.00 39.64  ? 111 ASP C O   1 
ATOM   4376 C CB  . ASP C 3 120 ? -3.937  -15.250 6.476   1.00 40.76  ? 111 ASP C CB  1 
ATOM   4377 C CG  . ASP C 3 120 ? -4.569  -14.113 5.669   1.00 47.61  ? 111 ASP C CG  1 
ATOM   4378 O OD1 . ASP C 3 120 ? -4.170  -12.939 5.869   1.00 49.12  ? 111 ASP C OD1 1 
ATOM   4379 O OD2 . ASP C 3 120 ? -5.425  -14.417 4.801   1.00 48.38  ? 111 ASP C OD2 1 
ATOM   4380 N N   . CYS C 3 121 ? -2.435  -17.036 3.579   1.00 34.97  ? 112 CYS C N   1 
ATOM   4381 C CA  . CYS C 3 121 ? -1.495  -16.803 2.492   1.00 35.08  ? 112 CYS C CA  1 
ATOM   4382 C C   . CYS C 3 121 ? -1.959  -17.474 1.198   1.00 32.27  ? 112 CYS C C   1 
ATOM   4383 O O   . CYS C 3 121 ? -1.392  -17.236 0.131   1.00 28.53  ? 112 CYS C O   1 
ATOM   4384 C CB  . CYS C 3 121 ? -0.099  -17.300 2.887   1.00 32.01  ? 112 CYS C CB  1 
ATOM   4385 S SG  . CYS C 3 121 ? 0.098   -19.092 2.809   1.00 31.62  ? 112 CYS C SG  1 
ATOM   4386 O OXT . CYS C 3 121 ? -2.910  -18.258 1.185   1.00 30.86  ? 112 CYS C OXT 1 
ATOM   4387 N N   . MET D 4 1   ? -35.839 -9.809  -62.825 1.00 138.99 ? 1   MET D N   1 
ATOM   4388 C CA  . MET D 4 1   ? -34.469 -9.559  -62.371 1.00 139.80 ? 1   MET D CA  1 
ATOM   4389 C C   . MET D 4 1   ? -34.244 -10.009 -60.924 1.00 136.88 ? 1   MET D C   1 
ATOM   4390 O O   . MET D 4 1   ? -35.196 -10.221 -60.176 1.00 135.43 ? 1   MET D O   1 
ATOM   4391 C CB  . MET D 4 1   ? -34.125 -8.073  -62.495 1.00 140.92 ? 1   MET D CB  1 
ATOM   4392 C CG  . MET D 4 1   ? -34.243 -7.306  -61.183 1.00 140.98 ? 1   MET D CG  1 
ATOM   4393 S SD  . MET D 4 1   ? -33.806 -5.564  -61.300 1.00 142.10 ? 1   MET D SD  1 
ATOM   4394 C CE  . MET D 4 1   ? -32.223 -5.676  -62.119 1.00 123.12 ? 1   MET D CE  1 
ATOM   4395 N N   . GLN D 4 2   ? -32.976 -10.139 -60.532 1.00 132.28 ? 2   GLN D N   1 
ATOM   4396 C CA  . GLN D 4 2   ? -32.616 -10.525 -59.176 1.00 125.62 ? 2   GLN D CA  1 
ATOM   4397 C C   . GLN D 4 2   ? -31.444 -9.688  -58.688 1.00 122.22 ? 2   GLN D C   1 
ATOM   4398 O O   . GLN D 4 2   ? -30.651 -9.176  -59.484 1.00 117.60 ? 2   GLN D O   1 
ATOM   4399 C CB  . GLN D 4 2   ? -32.247 -12.011 -59.081 1.00 129.31 ? 2   GLN D CB  1 
ATOM   4400 C CG  . GLN D 4 2   ? -33.285 -12.868 -58.383 1.00 134.32 ? 2   GLN D CG  1 
ATOM   4401 C CD  . GLN D 4 2   ? -32.739 -14.222 -57.970 1.00 135.50 ? 2   GLN D CD  1 
ATOM   4402 O OE1 . GLN D 4 2   ? -31.617 -14.589 -58.323 1.00 134.54 ? 2   GLN D OE1 1 
ATOM   4403 N NE2 . GLN D 4 2   ? -33.532 -14.971 -57.214 1.00 137.51 ? 2   GLN D NE2 1 
ATOM   4404 N N   . ILE D 4 3   ? -31.348 -9.554  -57.361 1.00 112.50 ? 3   ILE D N   1 
ATOM   4405 C CA  . ILE D 4 3   ? -30.232 -8.892  -56.694 1.00 100.31 ? 3   ILE D CA  1 
ATOM   4406 C C   . ILE D 4 3   ? -29.839 -9.720  -55.476 1.00 100.97 ? 3   ILE D C   1 
ATOM   4407 O O   . ILE D 4 3   ? -30.561 -10.622 -55.049 1.00 99.68  ? 3   ILE D O   1 
ATOM   4408 C CB  . ILE D 4 3   ? -30.561 -7.441  -56.274 1.00 99.68  ? 3   ILE D CB  1 
ATOM   4409 C CG1 . ILE D 4 3   ? -31.715 -7.406  -55.272 1.00 98.42  ? 3   ILE D CG1 1 
ATOM   4410 C CG2 . ILE D 4 3   ? -30.888 -6.583  -57.488 1.00 101.22 ? 3   ILE D CG2 1 
ATOM   4411 C CD1 . ILE D 4 3   ? -32.071 -6.003  -54.813 1.00 94.44  ? 3   ILE D CD1 1 
ATOM   4412 N N   . PHE D 4 4   ? -28.667 -9.407  -54.924 1.00 92.98  ? 4   PHE D N   1 
ATOM   4413 C CA  . PHE D 4 4   ? -28.168 -10.033 -53.707 1.00 94.22  ? 4   PHE D CA  1 
ATOM   4414 C C   . PHE D 4 4   ? -27.908 -8.980  -52.632 1.00 87.46  ? 4   PHE D C   1 
ATOM   4415 O O   . PHE D 4 4   ? -27.499 -7.853  -52.928 1.00 85.21  ? 4   PHE D O   1 
ATOM   4416 C CB  . PHE D 4 4   ? -26.863 -10.809 -53.954 1.00 95.43  ? 4   PHE D CB  1 
ATOM   4417 C CG  . PHE D 4 4   ? -26.843 -11.598 -55.229 1.00 95.69  ? 4   PHE D CG  1 
ATOM   4418 C CD1 . PHE D 4 4   ? -27.715 -12.655 -55.424 1.00 100.49 ? 4   PHE D CD1 1 
ATOM   4419 C CD2 . PHE D 4 4   ? -25.918 -11.306 -56.220 1.00 99.50  ? 4   PHE D CD2 1 
ATOM   4420 C CE1 . PHE D 4 4   ? -27.685 -13.393 -56.596 1.00 102.87 ? 4   PHE D CE1 1 
ATOM   4421 C CE2 . PHE D 4 4   ? -25.880 -12.037 -57.394 1.00 102.87 ? 4   PHE D CE2 1 
ATOM   4422 C CZ  . PHE D 4 4   ? -26.767 -13.082 -57.583 1.00 105.55 ? 4   PHE D CZ  1 
ATOM   4423 N N   . VAL D 4 5   ? -28.140 -9.348  -51.374 1.00 86.36  ? 5   VAL D N   1 
ATOM   4424 C CA  . VAL D 4 5   ? -27.711 -8.543  -50.235 1.00 84.67  ? 5   VAL D CA  1 
ATOM   4425 C C   . VAL D 4 5   ? -26.800 -9.410  -49.371 1.00 86.09  ? 5   VAL D C   1 
ATOM   4426 O O   . VAL D 4 5   ? -27.096 -10.585 -49.127 1.00 90.20  ? 5   VAL D O   1 
ATOM   4427 C CB  . VAL D 4 5   ? -28.903 -7.962  -49.440 1.00 86.09  ? 5   VAL D CB  1 
ATOM   4428 C CG1 . VAL D 4 5   ? -29.903 -7.294  -50.390 1.00 83.94  ? 5   VAL D CG1 1 
ATOM   4429 C CG2 . VAL D 4 5   ? -29.600 -9.008  -48.579 1.00 86.96  ? 5   VAL D CG2 1 
ATOM   4430 N N   . LYS D 4 6   ? -25.654 -8.855  -48.986 1.00 80.36  ? 6   LYS D N   1 
ATOM   4431 C CA  . LYS D 4 6   ? -24.633 -9.557  -48.215 1.00 83.52  ? 6   LYS D CA  1 
ATOM   4432 C C   . LYS D 4 6   ? -24.212 -8.652  -47.068 1.00 77.13  ? 6   LYS D C   1 
ATOM   4433 O O   . LYS D 4 6   ? -23.942 -7.464  -47.281 1.00 72.15  ? 6   LYS D O   1 
ATOM   4434 C CB  . LYS D 4 6   ? -23.416 -9.927  -49.095 1.00 83.72  ? 6   LYS D CB  1 
ATOM   4435 C CG  . LYS D 4 6   ? -22.399 -10.921 -48.498 1.00 89.56  ? 6   LYS D CG  1 
ATOM   4436 C CD  . LYS D 4 6   ? -22.814 -12.405 -48.606 1.00 96.69  ? 6   LYS D CD  1 
ATOM   4437 C CE  . LYS D 4 6   ? -21.579 -13.339 -48.553 1.00 102.29 ? 6   LYS D CE  1 
ATOM   4438 N NZ  . LYS D 4 6   ? -21.936 -14.832 -48.640 1.00 96.20  ? 6   LYS D NZ  1 
ATOM   4439 N N   . THR D 4 7   ? -24.199 -9.202  -45.854 1.00 83.63  ? 7   THR D N   1 
ATOM   4440 C CA  . THR D 4 7   ? -23.583 -8.531  -44.718 1.00 80.98  ? 7   THR D CA  1 
ATOM   4441 C C   . THR D 4 7   ? -22.068 -8.749  -44.763 1.00 83.26  ? 7   THR D C   1 
ATOM   4442 O O   . THR D 4 7   ? -21.546 -9.464  -45.623 1.00 86.88  ? 7   THR D O   1 
ATOM   4443 C CB  . THR D 4 7   ? -24.179 -9.028  -43.394 1.00 74.89  ? 7   THR D CB  1 
ATOM   4444 O OG1 . THR D 4 7   ? -23.897 -10.420 -43.210 1.00 76.76  ? 7   THR D OG1 1 
ATOM   4445 C CG2 . THR D 4 7   ? -25.684 -8.820  -43.367 1.00 68.17  ? 7   THR D CG2 1 
ATOM   4446 N N   . LEU D 4 8   ? -21.346 -8.108  -43.839 1.00 78.56  ? 8   LEU D N   1 
ATOM   4447 C CA  . LEU D 4 8   ? -19.892 -8.259  -43.825 1.00 78.20  ? 8   LEU D CA  1 
ATOM   4448 C C   . LEU D 4 8   ? -19.485 -9.699  -43.510 1.00 84.48  ? 8   LEU D C   1 
ATOM   4449 O O   . LEU D 4 8   ? -18.514 -10.215 -44.080 1.00 85.19  ? 8   LEU D O   1 
ATOM   4450 C CB  . LEU D 4 8   ? -19.264 -7.278  -42.831 1.00 76.96  ? 8   LEU D CB  1 
ATOM   4451 C CG  . LEU D 4 8   ? -17.866 -6.714  -43.139 1.00 68.57  ? 8   LEU D CG  1 
ATOM   4452 C CD1 . LEU D 4 8   ? -16.768 -7.736  -42.910 1.00 67.06  ? 8   LEU D CD1 1 
ATOM   4453 C CD2 . LEU D 4 8   ? -17.798 -6.211  -44.562 1.00 73.58  ? 8   LEU D CD2 1 
ATOM   4454 N N   . THR D 4 9   ? -20.222 -10.369 -42.611 1.00 87.83  ? 9   THR D N   1 
ATOM   4455 C CA  . THR D 4 9   ? -19.900 -11.747 -42.237 1.00 86.87  ? 9   THR D CA  1 
ATOM   4456 C C   . THR D 4 9   ? -20.261 -12.758 -43.325 1.00 90.80  ? 9   THR D C   1 
ATOM   4457 O O   . THR D 4 9   ? -19.675 -13.846 -43.370 1.00 88.47  ? 9   THR D O   1 
ATOM   4458 C CB  . THR D 4 9   ? -20.612 -12.130 -40.931 1.00 79.15  ? 9   THR D CB  1 
ATOM   4459 O OG1 . THR D 4 9   ? -21.944 -12.583 -41.212 1.00 86.43  ? 9   THR D OG1 1 
ATOM   4460 C CG2 . THR D 4 9   ? -20.687 -10.936 -39.989 1.00 74.92  ? 9   THR D CG2 1 
ATOM   4461 N N   . GLY D 4 10  ? -21.209 -12.437 -44.197 1.00 94.32  ? 10  GLY D N   1 
ATOM   4462 C CA  . GLY D 4 10  ? -21.627 -13.383 -45.213 1.00 97.14  ? 10  GLY D CA  1 
ATOM   4463 C C   . GLY D 4 10  ? -23.131 -13.519 -45.356 1.00 99.79  ? 10  GLY D C   1 
ATOM   4464 O O   . GLY D 4 10  ? -23.873 -12.540 -45.210 1.00 100.40 ? 10  GLY D O   1 
ATOM   4465 N N   . LYS D 4 11  ? -23.583 -14.738 -45.649 1.00 99.72  ? 11  LYS D N   1 
ATOM   4466 C CA  . LYS D 4 11  ? -25.004 -15.071 -45.730 1.00 104.49 ? 11  LYS D CA  1 
ATOM   4467 C C   . LYS D 4 11  ? -25.717 -14.283 -46.841 1.00 103.61 ? 11  LYS D C   1 
ATOM   4468 O O   . LYS D 4 11  ? -26.562 -13.426 -46.606 1.00 105.37 ? 11  LYS D O   1 
ATOM   4469 C CB  . LYS D 4 11  ? -25.694 -14.841 -44.393 1.00 97.45  ? 11  LYS D CB  1 
ATOM   4470 N N   . THR D 4 12  ? -25.395 -14.623 -48.084 1.00 100.13 ? 12  THR D N   1 
ATOM   4471 C CA  . THR D 4 12  ? -26.097 -14.042 -49.234 1.00 101.17 ? 12  THR D CA  1 
ATOM   4472 C C   . THR D 4 12  ? -27.595 -14.258 -49.103 1.00 107.24 ? 12  THR D C   1 
ATOM   4473 O O   . THR D 4 12  ? -28.056 -15.347 -48.731 1.00 109.81 ? 12  THR D O   1 
ATOM   4474 C CB  . THR D 4 12  ? -25.669 -14.629 -50.589 1.00 102.55 ? 12  THR D CB  1 
ATOM   4475 O OG1 . THR D 4 12  ? -24.490 -15.405 -50.441 1.00 108.00 ? 12  THR D OG1 1 
ATOM   4476 C CG2 . THR D 4 12  ? -25.421 -13.490 -51.449 1.00 95.34  ? 12  THR D CG2 1 
ATOM   4477 N N   . ILE D 4 13  ? -28.364 -13.234 -49.470 1.00 104.96 ? 13  ILE D N   1 
ATOM   4478 C CA  . ILE D 4 13  ? -29.820 -13.332 -49.524 1.00 105.99 ? 13  ILE D CA  1 
ATOM   4479 C C   . ILE D 4 13  ? -30.246 -12.876 -50.917 1.00 106.75 ? 13  ILE D C   1 
ATOM   4480 O O   . ILE D 4 13  ? -30.355 -11.675 -51.179 1.00 106.70 ? 13  ILE D O   1 
ATOM   4481 C CB  . ILE D 4 13  ? -30.509 -12.517 -48.415 1.00 106.65 ? 13  ILE D CB  1 
ATOM   4482 C CG1 . ILE D 4 13  ? -29.835 -12.778 -47.067 1.00 106.49 ? 13  ILE D CG1 1 
ATOM   4483 C CG2 . ILE D 4 13  ? -32.024 -12.844 -48.316 1.00 112.70 ? 13  ILE D CG2 1 
ATOM   4484 C CD1 . ILE D 4 13  ? -29.890 -14.241 -46.605 1.00 113.69 ? 13  ILE D CD1 1 
ATOM   4485 N N   . THR D 4 14  ? -30.467 -13.829 -51.823 1.00 105.20 ? 14  THR D N   1 
ATOM   4486 C CA  . THR D 4 14  ? -30.915 -13.488 -53.163 1.00 106.48 ? 14  THR D CA  1 
ATOM   4487 C C   . THR D 4 14  ? -32.395 -13.133 -53.097 1.00 108.83 ? 14  THR D C   1 
ATOM   4488 O O   . THR D 4 14  ? -33.193 -13.867 -52.504 1.00 106.64 ? 14  THR D O   1 
ATOM   4489 C CB  . THR D 4 14  ? -30.673 -14.642 -54.143 1.00 107.83 ? 14  THR D CB  1 
ATOM   4490 O OG1 . THR D 4 14  ? -31.711 -15.624 -54.010 1.00 113.28 ? 14  THR D OG1 1 
ATOM   4491 C CG2 . THR D 4 14  ? -29.320 -15.304 -53.898 1.00 96.24  ? 14  THR D CG2 1 
ATOM   4492 N N   . LEU D 4 15  ? -32.756 -11.994 -53.678 1.00 108.55 ? 15  LEU D N   1 
ATOM   4493 C CA  . LEU D 4 15  ? -34.114 -11.482 -53.588 1.00 110.50 ? 15  LEU D CA  1 
ATOM   4494 C C   . LEU D 4 15  ? -34.667 -11.219 -54.978 1.00 113.87 ? 15  LEU D C   1 
ATOM   4495 O O   . LEU D 4 15  ? -33.970 -10.677 -55.839 1.00 114.84 ? 15  LEU D O   1 
ATOM   4496 C CB  . LEU D 4 15  ? -34.177 -10.192 -52.764 1.00 108.56 ? 15  LEU D CB  1 
ATOM   4497 C CG  . LEU D 4 15  ? -33.959 -10.304 -51.258 1.00 111.09 ? 15  LEU D CG  1 
ATOM   4498 C CD1 . LEU D 4 15  ? -34.263 -8.966  -50.637 1.00 104.87 ? 15  LEU D CD1 1 
ATOM   4499 C CD2 . LEU D 4 15  ? -34.825 -11.407 -50.645 1.00 111.47 ? 15  LEU D CD2 1 
ATOM   4500 N N   . GLU D 4 16  ? -35.927 -11.600 -55.183 1.00 117.72 ? 16  GLU D N   1 
ATOM   4501 C CA  . GLU D 4 16  ? -36.632 -11.306 -56.426 1.00 121.25 ? 16  GLU D CA  1 
ATOM   4502 C C   . GLU D 4 16  ? -37.229 -9.904  -56.347 1.00 120.83 ? 16  GLU D C   1 
ATOM   4503 O O   . GLU D 4 16  ? -38.027 -9.611  -55.450 1.00 118.04 ? 16  GLU D O   1 
ATOM   4504 C CB  . GLU D 4 16  ? -37.717 -12.348 -56.685 1.00 117.45 ? 16  GLU D CB  1 
ATOM   4505 N N   . VAL D 4 17  ? -36.846 -9.042  -57.288 1.00 126.44 ? 17  VAL D N   1 
ATOM   4506 C CA  . VAL D 4 17  ? -37.168 -7.621  -57.251 1.00 130.39 ? 17  VAL D CA  1 
ATOM   4507 C C   . VAL D 4 17  ? -37.251 -7.121  -58.690 1.00 136.62 ? 17  VAL D C   1 
ATOM   4508 O O   . VAL D 4 17  ? -36.898 -7.829  -59.634 1.00 140.34 ? 17  VAL D O   1 
ATOM   4509 C CB  . VAL D 4 17  ? -36.115 -6.831  -56.435 1.00 133.85 ? 17  VAL D CB  1 
ATOM   4510 C CG1 . VAL D 4 17  ? -34.826 -6.635  -57.239 1.00 127.64 ? 17  VAL D CG1 1 
ATOM   4511 C CG2 . VAL D 4 17  ? -36.681 -5.510  -55.931 1.00 137.53 ? 17  VAL D CG2 1 
ATOM   4512 N N   . GLU D 4 18  ? -37.748 -5.904  -58.862 1.00 138.46 ? 18  GLU D N   1 
ATOM   4513 C CA  . GLU D 4 18  ? -37.782 -5.211  -60.141 1.00 139.73 ? 18  GLU D CA  1 
ATOM   4514 C C   . GLU D 4 18  ? -37.274 -3.792  -59.925 1.00 138.92 ? 18  GLU D C   1 
ATOM   4515 O O   . GLU D 4 18  ? -37.336 -3.272  -58.805 1.00 136.54 ? 18  GLU D O   1 
ATOM   4516 C CB  . GLU D 4 18  ? -39.200 -5.197  -60.737 1.00 139.56 ? 18  GLU D CB  1 
ATOM   4517 C CG  . GLU D 4 18  ? -39.749 -6.580  -61.151 1.00 146.61 ? 18  GLU D CG  1 
ATOM   4518 C CD  . GLU D 4 18  ? -39.151 -7.122  -62.452 1.00 146.09 ? 18  GLU D CD  1 
ATOM   4519 O OE1 . GLU D 4 18  ? -38.653 -6.321  -63.270 1.00 148.13 ? 18  GLU D OE1 1 
ATOM   4520 O OE2 . GLU D 4 18  ? -39.182 -8.355  -62.660 1.00 140.50 ? 18  GLU D OE2 1 
ATOM   4521 N N   . PRO D 4 19  ? -36.746 -3.141  -60.972 1.00 138.90 ? 19  PRO D N   1 
ATOM   4522 C CA  . PRO D 4 19  ? -36.097 -1.830  -60.758 1.00 131.91 ? 19  PRO D CA  1 
ATOM   4523 C C   . PRO D 4 19  ? -37.019 -0.765  -60.183 1.00 133.00 ? 19  PRO D C   1 
ATOM   4524 O O   . PRO D 4 19  ? -36.533 0.175   -59.539 1.00 128.09 ? 19  PRO D O   1 
ATOM   4525 C CB  . PRO D 4 19  ? -35.598 -1.451  -62.163 1.00 127.80 ? 19  PRO D CB  1 
ATOM   4526 C CG  . PRO D 4 19  ? -36.402 -2.285  -63.103 1.00 133.41 ? 19  PRO D CG  1 
ATOM   4527 C CD  . PRO D 4 19  ? -36.663 -3.568  -62.380 1.00 132.21 ? 19  PRO D CD  1 
ATOM   4528 N N   . SER D 4 20  ? -38.334 -0.880  -60.393 1.00 138.11 ? 20  SER D N   1 
ATOM   4529 C CA  . SER D 4 20  ? -39.273 0.099   -59.855 1.00 135.78 ? 20  SER D CA  1 
ATOM   4530 C C   . SER D 4 20  ? -39.374 0.044   -58.335 1.00 135.55 ? 20  SER D C   1 
ATOM   4531 O O   . SER D 4 20  ? -39.774 1.039   -57.721 1.00 131.89 ? 20  SER D O   1 
ATOM   4532 C CB  . SER D 4 20  ? -40.655 -0.113  -60.472 1.00 138.02 ? 20  SER D CB  1 
ATOM   4533 O OG  . SER D 4 20  ? -41.104 -1.439  -60.258 1.00 138.69 ? 20  SER D OG  1 
ATOM   4534 N N   . ASP D 4 21  ? -39.031 -1.088  -57.721 1.00 143.33 ? 21  ASP D N   1 
ATOM   4535 C CA  . ASP D 4 21  ? -39.142 -1.224  -56.274 1.00 141.97 ? 21  ASP D CA  1 
ATOM   4536 C C   . ASP D 4 21  ? -38.206 -0.257  -55.558 1.00 137.85 ? 21  ASP D C   1 
ATOM   4537 O O   . ASP D 4 21  ? -37.035 -0.110  -55.921 1.00 136.90 ? 21  ASP D O   1 
ATOM   4538 C CB  . ASP D 4 21  ? -38.830 -2.660  -55.843 1.00 141.37 ? 21  ASP D CB  1 
ATOM   4539 C CG  . ASP D 4 21  ? -39.815 -3.664  -56.402 1.00 147.13 ? 21  ASP D CG  1 
ATOM   4540 O OD1 . ASP D 4 21  ? -39.785 -3.911  -57.626 1.00 149.81 ? 21  ASP D OD1 1 
ATOM   4541 O OD2 . ASP D 4 21  ? -40.620 -4.208  -55.616 1.00 149.80 ? 21  ASP D OD2 1 
ATOM   4542 N N   . THR D 4 22  ? -38.731 0.393   -54.524 1.00 125.57 ? 22  THR D N   1 
ATOM   4543 C CA  . THR D 4 22  ? -37.965 1.342   -53.735 1.00 123.04 ? 22  THR D CA  1 
ATOM   4544 C C   . THR D 4 22  ? -36.987 0.607   -52.818 1.00 118.51 ? 22  THR D C   1 
ATOM   4545 O O   . THR D 4 22  ? -37.035 -0.616  -52.662 1.00 118.11 ? 22  THR D O   1 
ATOM   4546 C CB  . THR D 4 22  ? -38.900 2.229   -52.913 1.00 121.01 ? 22  THR D CB  1 
ATOM   4547 O OG1 . THR D 4 22  ? -39.631 1.419   -51.982 1.00 117.53 ? 22  THR D OG1 1 
ATOM   4548 C CG2 . THR D 4 22  ? -39.881 2.957   -53.825 1.00 113.83 ? 22  THR D CG2 1 
ATOM   4549 N N   . ILE D 4 23  ? -36.075 1.372   -52.213 1.00 114.33 ? 23  ILE D N   1 
ATOM   4550 C CA  . ILE D 4 23  ? -35.170 0.789   -51.224 1.00 113.01 ? 23  ILE D CA  1 
ATOM   4551 C C   . ILE D 4 23  ? -35.950 0.344   -49.988 1.00 113.11 ? 23  ILE D C   1 
ATOM   4552 O O   . ILE D 4 23  ? -35.570 -0.627  -49.318 1.00 107.34 ? 23  ILE D O   1 
ATOM   4553 C CB  . ILE D 4 23  ? -34.045 1.782   -50.872 1.00 105.34 ? 23  ILE D CB  1 
ATOM   4554 C CG1 . ILE D 4 23  ? -33.273 2.190   -52.133 1.00 102.36 ? 23  ILE D CG1 1 
ATOM   4555 C CG2 . ILE D 4 23  ? -33.110 1.193   -49.830 1.00 97.01  ? 23  ILE D CG2 1 
ATOM   4556 C CD1 . ILE D 4 23  ? -32.636 1.041   -52.877 1.00 100.52 ? 23  ILE D CD1 1 
ATOM   4557 N N   . GLU D 4 24  ? -37.053 1.033   -49.672 1.00 116.30 ? 24  GLU D N   1 
ATOM   4558 C CA  . GLU D 4 24  ? -37.949 0.566   -48.617 1.00 111.65 ? 24  GLU D CA  1 
ATOM   4559 C C   . GLU D 4 24  ? -38.558 -0.785  -48.975 1.00 111.94 ? 24  GLU D C   1 
ATOM   4560 O O   . GLU D 4 24  ? -38.745 -1.640  -48.101 1.00 107.88 ? 24  GLU D O   1 
ATOM   4561 C CB  . GLU D 4 24  ? -39.046 1.602   -48.362 1.00 112.50 ? 24  GLU D CB  1 
ATOM   4562 N N   . ASN D 4 25  ? -38.883 -0.991  -50.259 1.00 117.28 ? 25  ASN D N   1 
ATOM   4563 C CA  . ASN D 4 25  ? -39.373 -2.290  -50.716 1.00 110.48 ? 25  ASN D CA  1 
ATOM   4564 C C   . ASN D 4 25  ? -38.337 -3.389  -50.496 1.00 107.41 ? 25  ASN D C   1 
ATOM   4565 O O   . ASN D 4 25  ? -38.676 -4.490  -50.045 1.00 104.48 ? 25  ASN D O   1 
ATOM   4566 C CB  . ASN D 4 25  ? -39.754 -2.216  -52.197 1.00 117.37 ? 25  ASN D CB  1 
ATOM   4567 C CG  . ASN D 4 25  ? -41.220 -1.887  -52.414 1.00 122.38 ? 25  ASN D CG  1 
ATOM   4568 O OD1 . ASN D 4 25  ? -42.049 -2.066  -51.523 1.00 119.80 ? 25  ASN D OD1 1 
ATOM   4569 N ND2 . ASN D 4 25  ? -41.549 -1.419  -53.617 1.00 118.36 ? 25  ASN D ND2 1 
ATOM   4570 N N   . VAL D 4 26  ? -37.071 -3.115  -50.821 1.00 107.48 ? 26  VAL D N   1 
ATOM   4571 C CA  . VAL D 4 26  ? -36.030 -4.128  -50.675 1.00 103.13 ? 26  VAL D CA  1 
ATOM   4572 C C   . VAL D 4 26  ? -35.787 -4.442  -49.204 1.00 101.01 ? 26  VAL D C   1 
ATOM   4573 O O   . VAL D 4 26  ? -35.518 -5.593  -48.841 1.00 100.95 ? 26  VAL D O   1 
ATOM   4574 C CB  . VAL D 4 26  ? -34.742 -3.678  -51.385 1.00 96.34  ? 26  VAL D CB  1 
ATOM   4575 C CG1 . VAL D 4 26  ? -33.741 -4.816  -51.415 1.00 90.26  ? 26  VAL D CG1 1 
ATOM   4576 C CG2 . VAL D 4 26  ? -35.056 -3.208  -52.796 1.00 100.19 ? 26  VAL D CG2 1 
ATOM   4577 N N   . LYS D 4 27  ? -35.867 -3.430  -48.334 1.00 99.07  ? 27  LYS D N   1 
ATOM   4578 C CA  . LYS D 4 27  ? -35.815 -3.694  -46.897 1.00 97.89  ? 27  LYS D CA  1 
ATOM   4579 C C   . LYS D 4 27  ? -37.012 -4.525  -46.443 1.00 99.26  ? 27  LYS D C   1 
ATOM   4580 O O   . LYS D 4 27  ? -36.891 -5.347  -45.527 1.00 94.93  ? 27  LYS D O   1 
ATOM   4581 C CB  . LYS D 4 27  ? -35.752 -2.379  -46.111 1.00 93.35  ? 27  LYS D CB  1 
ATOM   4582 C CG  . LYS D 4 27  ? -34.410 -1.651  -46.149 1.00 88.77  ? 27  LYS D CG  1 
ATOM   4583 C CD  . LYS D 4 27  ? -34.498 -0.328  -45.400 1.00 83.85  ? 27  LYS D CD  1 
ATOM   4584 C CE  . LYS D 4 27  ? -33.126 0.265   -45.112 1.00 79.44  ? 27  LYS D CE  1 
ATOM   4585 N NZ  . LYS D 4 27  ? -33.232 1.412   -44.161 1.00 79.78  ? 27  LYS D NZ  1 
ATOM   4586 N N   . ALA D 4 28  ? -38.173 -4.318  -47.066 1.00 103.82 ? 28  ALA D N   1 
ATOM   4587 C CA  . ALA D 4 28  ? -39.348 -5.120  -46.742 1.00 104.11 ? 28  ALA D CA  1 
ATOM   4588 C C   . ALA D 4 28  ? -39.136 -6.582  -47.114 1.00 106.53 ? 28  ALA D C   1 
ATOM   4589 O O   . ALA D 4 28  ? -39.381 -7.480  -46.301 1.00 105.72 ? 28  ALA D O   1 
ATOM   4590 C CB  . ALA D 4 28  ? -40.579 -4.555  -47.451 1.00 99.05  ? 28  ALA D CB  1 
ATOM   4591 N N   . LYS D 4 29  ? -38.672 -6.838  -48.342 1.00 112.39 ? 29  LYS D N   1 
ATOM   4592 C CA  . LYS D 4 29  ? -38.437 -8.212  -48.775 1.00 113.16 ? 29  LYS D CA  1 
ATOM   4593 C C   . LYS D 4 29  ? -37.357 -8.886  -47.940 1.00 114.84 ? 29  LYS D C   1 
ATOM   4594 O O   . LYS D 4 29  ? -37.430 -10.097 -47.692 1.00 115.25 ? 29  LYS D O   1 
ATOM   4595 C CB  . LYS D 4 29  ? -38.051 -8.237  -50.253 1.00 114.08 ? 29  LYS D CB  1 
ATOM   4596 C CG  . LYS D 4 29  ? -39.027 -7.525  -51.163 1.00 117.12 ? 29  LYS D CG  1 
ATOM   4597 C CD  . LYS D 4 29  ? -38.322 -7.006  -52.404 1.00 121.61 ? 29  LYS D CD  1 
ATOM   4598 C CE  . LYS D 4 29  ? -39.255 -6.167  -53.268 1.00 127.56 ? 29  LYS D CE  1 
ATOM   4599 N NZ  . LYS D 4 29  ? -40.333 -6.986  -53.879 1.00 130.24 ? 29  LYS D NZ  1 
ATOM   4600 N N   . ILE D 4 30  ? -36.345 -8.125  -47.510 1.00 105.61 ? 30  ILE D N   1 
ATOM   4601 C CA  . ILE D 4 30  ? -35.299 -8.685  -46.658 1.00 100.67 ? 30  ILE D CA  1 
ATOM   4602 C C   . ILE D 4 30  ? -35.892 -9.169  -45.339 1.00 102.36 ? 30  ILE D C   1 
ATOM   4603 O O   . ILE D 4 30  ? -35.571 -10.266 -44.862 1.00 102.86 ? 30  ILE D O   1 
ATOM   4604 C CB  . ILE D 4 30  ? -34.177 -7.650  -46.443 1.00 95.77  ? 30  ILE D CB  1 
ATOM   4605 C CG1 . ILE D 4 30  ? -33.281 -7.560  -47.681 1.00 90.65  ? 30  ILE D CG1 1 
ATOM   4606 C CG2 . ILE D 4 30  ? -33.345 -7.995  -45.213 1.00 94.44  ? 30  ILE D CG2 1 
ATOM   4607 C CD1 . ILE D 4 30  ? -32.472 -6.281  -47.774 1.00 88.64  ? 30  ILE D CD1 1 
ATOM   4608 N N   . GLN D 4 31  ? -36.784 -8.371  -44.741 1.00 102.06 ? 31  GLN D N   1 
ATOM   4609 C CA  . GLN D 4 31  ? -37.437 -8.785  -43.501 1.00 100.00 ? 31  GLN D CA  1 
ATOM   4610 C C   . GLN D 4 31  ? -38.253 -10.055 -43.702 1.00 104.87 ? 31  GLN D C   1 
ATOM   4611 O O   . GLN D 4 31  ? -38.321 -10.904 -42.806 1.00 103.39 ? 31  GLN D O   1 
ATOM   4612 C CB  . GLN D 4 31  ? -38.329 -7.665  -42.966 1.00 97.09  ? 31  GLN D CB  1 
ATOM   4613 C CG  . GLN D 4 31  ? -38.944 -7.980  -41.613 1.00 93.59  ? 31  GLN D CG  1 
ATOM   4614 C CD  . GLN D 4 31  ? -40.032 -7.004  -41.218 1.00 93.60  ? 31  GLN D CD  1 
ATOM   4615 O OE1 . GLN D 4 31  ? -40.405 -6.914  -40.048 1.00 90.17  ? 31  GLN D OE1 1 
ATOM   4616 N NE2 . GLN D 4 31  ? -40.556 -6.273  -42.195 1.00 95.62  ? 31  GLN D NE2 1 
ATOM   4617 N N   . ASP D 4 32  ? -38.891 -10.197 -44.869 1.00 112.39 ? 32  ASP D N   1 
ATOM   4618 C CA  . ASP D 4 32  ? -39.635 -11.416 -45.174 1.00 112.76 ? 32  ASP D CA  1 
ATOM   4619 C C   . ASP D 4 32  ? -38.720 -12.632 -45.275 1.00 110.96 ? 32  ASP D C   1 
ATOM   4620 O O   . ASP D 4 32  ? -39.120 -13.738 -44.893 1.00 110.09 ? 32  ASP D O   1 
ATOM   4621 C CB  . ASP D 4 32  ? -40.417 -11.250 -46.479 1.00 115.53 ? 32  ASP D CB  1 
ATOM   4622 C CG  . ASP D 4 32  ? -41.291 -10.014 -46.487 1.00 118.33 ? 32  ASP D CG  1 
ATOM   4623 O OD1 . ASP D 4 32  ? -41.257 -9.259  -45.491 1.00 118.47 ? 32  ASP D OD1 1 
ATOM   4624 O OD2 . ASP D 4 32  ? -42.011 -9.799  -47.488 1.00 118.16 ? 32  ASP D OD2 1 
ATOM   4625 N N   . LYS D 4 33  ? -37.499 -12.450 -45.784 1.00 109.19 ? 33  LYS D N   1 
ATOM   4626 C CA  . LYS D 4 33  ? -36.591 -13.554 -46.064 1.00 108.10 ? 33  LYS D CA  1 
ATOM   4627 C C   . LYS D 4 33  ? -35.567 -13.807 -44.962 1.00 110.96 ? 33  LYS D C   1 
ATOM   4628 O O   . LYS D 4 33  ? -34.898 -14.848 -44.995 1.00 108.44 ? 33  LYS D O   1 
ATOM   4629 C CB  . LYS D 4 33  ? -35.855 -13.308 -47.391 1.00 103.32 ? 33  LYS D CB  1 
ATOM   4630 N N   . GLU D 4 34  ? -35.413 -12.890 -43.998 1.00 108.01 ? 34  GLU D N   1 
ATOM   4631 C CA  . GLU D 4 34  ? -34.462 -13.101 -42.914 1.00 104.76 ? 34  GLU D CA  1 
ATOM   4632 C C   . GLU D 4 34  ? -34.959 -12.692 -41.532 1.00 100.18 ? 34  GLU D C   1 
ATOM   4633 O O   . GLU D 4 34  ? -34.244 -12.929 -40.554 1.00 100.78 ? 34  GLU D O   1 
ATOM   4634 C CB  . GLU D 4 34  ? -33.148 -12.363 -43.214 1.00 105.67 ? 34  GLU D CB  1 
ATOM   4635 C CG  . GLU D 4 34  ? -32.265 -13.089 -44.206 1.00 109.17 ? 34  GLU D CG  1 
ATOM   4636 C CD  . GLU D 4 34  ? -31.814 -14.440 -43.691 1.00 113.03 ? 34  GLU D CD  1 
ATOM   4637 O OE1 . GLU D 4 34  ? -31.493 -14.542 -42.487 1.00 114.94 ? 34  GLU D OE1 1 
ATOM   4638 O OE2 . GLU D 4 34  ? -31.789 -15.403 -44.485 1.00 113.81 ? 34  GLU D OE2 1 
ATOM   4639 N N   . GLY D 4 35  ? -36.148 -12.113 -41.410 1.00 98.42  ? 35  GLY D N   1 
ATOM   4640 C CA  . GLY D 4 35  ? -36.656 -11.709 -40.107 1.00 92.65  ? 35  GLY D CA  1 
ATOM   4641 C C   . GLY D 4 35  ? -35.895 -10.575 -39.455 1.00 94.44  ? 35  GLY D C   1 
ATOM   4642 O O   . GLY D 4 35  ? -35.698 -10.584 -38.231 1.00 93.94  ? 35  GLY D O   1 
ATOM   4643 N N   . ILE D 4 36  ? -35.463 -9.599  -40.244 1.00 94.97  ? 36  ILE D N   1 
ATOM   4644 C CA  . ILE D 4 36  ? -34.728 -8.425  -39.783 1.00 90.59  ? 36  ILE D CA  1 
ATOM   4645 C C   . ILE D 4 36  ? -35.613 -7.201  -40.004 1.00 91.34  ? 36  ILE D C   1 
ATOM   4646 O O   . ILE D 4 36  ? -35.912 -6.864  -41.157 1.00 91.61  ? 36  ILE D O   1 
ATOM   4647 C CB  . ILE D 4 36  ? -33.389 -8.270  -40.524 1.00 88.82  ? 36  ILE D CB  1 
ATOM   4648 C CG1 . ILE D 4 36  ? -32.499 -9.497  -40.319 1.00 84.77  ? 36  ILE D CG1 1 
ATOM   4649 C CG2 . ILE D 4 36  ? -32.678 -7.010  -40.074 1.00 82.93  ? 36  ILE D CG2 1 
ATOM   4650 C CD1 . ILE D 4 36  ? -31.290 -9.519  -41.237 1.00 79.54  ? 36  ILE D CD1 1 
ATOM   4651 N N   . PRO D 4 37  ? -36.045 -6.511  -38.952 1.00 90.77  ? 37  PRO D N   1 
ATOM   4652 C CA  . PRO D 4 37  ? -36.896 -5.316  -39.130 1.00 90.98  ? 37  PRO D CA  1 
ATOM   4653 C C   . PRO D 4 37  ? -36.188 -4.252  -39.950 1.00 95.35  ? 37  PRO D C   1 
ATOM   4654 O O   . PRO D 4 37  ? -34.964 -4.075  -39.832 1.00 94.27  ? 37  PRO D O   1 
ATOM   4655 C CB  . PRO D 4 37  ? -37.139 -4.835  -37.691 1.00 93.96  ? 37  PRO D CB  1 
ATOM   4656 C CG  . PRO D 4 37  ? -36.843 -6.033  -36.823 1.00 88.66  ? 37  PRO D CG  1 
ATOM   4657 C CD  . PRO D 4 37  ? -35.791 -6.821  -37.534 1.00 86.37  ? 37  PRO D CD  1 
ATOM   4658 N N   . PRO D 4 38  ? -36.919 -3.523  -40.797 1.00 96.90  ? 38  PRO D N   1 
ATOM   4659 C CA  . PRO D 4 38  ? -36.265 -2.506  -41.645 1.00 96.35  ? 38  PRO D CA  1 
ATOM   4660 C C   . PRO D 4 38  ? -35.580 -1.371  -40.880 1.00 98.90  ? 38  PRO D C   1 
ATOM   4661 O O   . PRO D 4 38  ? -34.676 -0.740  -41.441 1.00 94.10  ? 38  PRO D O   1 
ATOM   4662 C CB  . PRO D 4 38  ? -37.416 -1.981  -42.521 1.00 94.51  ? 38  PRO D CB  1 
ATOM   4663 C CG  . PRO D 4 38  ? -38.685 -2.478  -41.874 1.00 95.21  ? 38  PRO D CG  1 
ATOM   4664 C CD  . PRO D 4 38  ? -38.321 -3.750  -41.182 1.00 94.09  ? 38  PRO D CD  1 
ATOM   4665 N N   . ASP D 4 39  ? -35.970 -1.080  -39.634 1.00 123.81 ? 39  ASP D N   1 
ATOM   4666 C CA  . ASP D 4 39  ? -35.319 0.004   -38.899 1.00 121.86 ? 39  ASP D CA  1 
ATOM   4667 C C   . ASP D 4 39  ? -33.888 -0.339  -38.506 1.00 113.69 ? 39  ASP D C   1 
ATOM   4668 O O   . ASP D 4 39  ? -33.078 0.571   -38.297 1.00 109.04 ? 39  ASP D O   1 
ATOM   4669 C CB  . ASP D 4 39  ? -36.119 0.369   -37.645 1.00 124.99 ? 39  ASP D CB  1 
ATOM   4670 C CG  . ASP D 4 39  ? -35.754 -0.496  -36.443 1.00 123.95 ? 39  ASP D CG  1 
ATOM   4671 O OD1 . ASP D 4 39  ? -35.712 -1.736  -36.594 1.00 122.95 ? 39  ASP D OD1 1 
ATOM   4672 O OD2 . ASP D 4 39  ? -35.501 0.062   -35.349 1.00 119.68 ? 39  ASP D OD2 1 
ATOM   4673 N N   . GLN D 4 40  ? -33.561 -1.626  -38.391 1.00 97.22  ? 40  GLN D N   1 
ATOM   4674 C CA  . GLN D 4 40  ? -32.206 -2.071  -38.105 1.00 88.60  ? 40  GLN D CA  1 
ATOM   4675 C C   . GLN D 4 40  ? -31.413 -2.372  -39.365 1.00 78.12  ? 40  GLN D C   1 
ATOM   4676 O O   . GLN D 4 40  ? -30.381 -3.045  -39.287 1.00 71.15  ? 40  GLN D O   1 
ATOM   4677 C CB  . GLN D 4 40  ? -32.234 -3.309  -37.213 1.00 83.51  ? 40  GLN D CB  1 
ATOM   4678 C CG  . GLN D 4 40  ? -32.752 -3.047  -35.824 1.00 86.50  ? 40  GLN D CG  1 
ATOM   4679 C CD  . GLN D 4 40  ? -33.318 -4.287  -35.211 1.00 79.11  ? 40  GLN D CD  1 
ATOM   4680 O OE1 . GLN D 4 40  ? -32.928 -5.397  -35.573 1.00 74.24  ? 40  GLN D OE1 1 
ATOM   4681 N NE2 . GLN D 4 40  ? -34.269 -4.118  -34.294 1.00 83.67  ? 40  GLN D NE2 1 
ATOM   4682 N N   . GLN D 4 41  ? -31.872 -1.895  -40.517 1.00 79.69  ? 41  GLN D N   1 
ATOM   4683 C CA  . GLN D 4 41  ? -31.252 -2.192  -41.797 1.00 77.35  ? 41  GLN D CA  1 
ATOM   4684 C C   . GLN D 4 41  ? -30.691 -0.929  -42.428 1.00 70.86  ? 41  GLN D C   1 
ATOM   4685 O O   . GLN D 4 41  ? -31.300 0.144   -42.361 1.00 72.94  ? 41  GLN D O   1 
ATOM   4686 C CB  . GLN D 4 41  ? -32.241 -2.840  -42.760 1.00 80.03  ? 41  GLN D CB  1 
ATOM   4687 C CG  . GLN D 4 41  ? -32.592 -4.258  -42.403 1.00 84.31  ? 41  GLN D CG  1 
ATOM   4688 C CD  . GLN D 4 41  ? -33.586 -4.863  -43.372 1.00 88.70  ? 41  GLN D CD  1 
ATOM   4689 O OE1 . GLN D 4 41  ? -33.619 -4.503  -44.553 1.00 82.11  ? 41  GLN D OE1 1 
ATOM   4690 N NE2 . GLN D 4 41  ? -34.412 -5.783  -42.874 1.00 91.16  ? 41  GLN D NE2 1 
ATOM   4691 N N   . ARG D 4 42  ? -29.523 -1.080  -43.040 1.00 66.52  ? 42  ARG D N   1 
ATOM   4692 C CA  . ARG D 4 42  ? -28.859 -0.011  -43.770 1.00 65.83  ? 42  ARG D CA  1 
ATOM   4693 C C   . ARG D 4 42  ? -28.266 -0.632  -45.022 1.00 66.52  ? 42  ARG D C   1 
ATOM   4694 O O   . ARG D 4 42  ? -27.396 -1.503  -44.929 1.00 67.11  ? 42  ARG D O   1 
ATOM   4695 C CB  . ARG D 4 42  ? -27.776 0.646   -42.909 1.00 59.49  ? 42  ARG D CB  1 
ATOM   4696 C CG  . ARG D 4 42  ? -27.076 1.829   -43.539 1.00 62.94  ? 42  ARG D CG  1 
ATOM   4697 C CD  . ARG D 4 42  ? -25.917 2.290   -42.658 1.00 60.90  ? 42  ARG D CD  1 
ATOM   4698 N NE  . ARG D 4 42  ? -26.361 2.541   -41.291 1.00 62.44  ? 42  ARG D NE  1 
ATOM   4699 C CZ  . ARG D 4 42  ? -26.802 3.711   -40.848 1.00 57.36  ? 42  ARG D CZ  1 
ATOM   4700 N NH1 . ARG D 4 42  ? -26.812 4.786   -41.628 1.00 54.87  ? 42  ARG D NH1 1 
ATOM   4701 N NH2 . ARG D 4 42  ? -27.251 3.802   -39.596 1.00 53.24  ? 42  ARG D NH2 1 
ATOM   4702 N N   . LEU D 4 43  ? -28.751 -0.213  -46.186 1.00 70.25  ? 43  LEU D N   1 
ATOM   4703 C CA  . LEU D 4 43  ? -28.321 -0.779  -47.459 1.00 68.63  ? 43  LEU D CA  1 
ATOM   4704 C C   . LEU D 4 43  ? -27.340 0.171   -48.128 1.00 68.40  ? 43  LEU D C   1 
ATOM   4705 O O   . LEU D 4 43  ? -27.586 1.379   -48.190 1.00 73.99  ? 43  LEU D O   1 
ATOM   4706 C CB  . LEU D 4 43  ? -29.521 -1.047  -48.365 1.00 74.07  ? 43  LEU D CB  1 
ATOM   4707 C CG  . LEU D 4 43  ? -30.401 -2.199  -47.885 1.00 73.80  ? 43  LEU D CG  1 
ATOM   4708 C CD1 . LEU D 4 43  ? -31.603 -2.367  -48.790 1.00 78.71  ? 43  LEU D CD1 1 
ATOM   4709 C CD2 . LEU D 4 43  ? -29.585 -3.480  -47.831 1.00 71.68  ? 43  LEU D CD2 1 
ATOM   4710 N N   . ILE D 4 44  ? -26.223 -0.370  -48.603 1.00 73.36  ? 44  ILE D N   1 
ATOM   4711 C CA  . ILE D 4 44  ? -25.163 0.425   -49.209 1.00 75.02  ? 44  ILE D CA  1 
ATOM   4712 C C   . ILE D 4 44  ? -24.812 -0.176  -50.564 1.00 78.15  ? 44  ILE D C   1 
ATOM   4713 O O   . ILE D 4 44  ? -24.587 -1.386  -50.677 1.00 77.33  ? 44  ILE D O   1 
ATOM   4714 C CB  . ILE D 4 44  ? -23.926 0.507   -48.292 1.00 71.26  ? 44  ILE D CB  1 
ATOM   4715 C CG1 . ILE D 4 44  ? -24.197 1.504   -47.162 1.00 66.97  ? 44  ILE D CG1 1 
ATOM   4716 C CG2 . ILE D 4 44  ? -22.670 0.870   -49.083 1.00 68.97  ? 44  ILE D CG2 1 
ATOM   4717 C CD1 . ILE D 4 44  ? -22.994 1.866   -46.366 1.00 62.06  ? 44  ILE D CD1 1 
ATOM   4718 N N   . PHE D 4 45  ? -24.800 0.663   -51.595 1.00 77.61  ? 45  PHE D N   1 
ATOM   4719 C CA  . PHE D 4 45  ? -24.376 0.257   -52.926 1.00 82.03  ? 45  PHE D CA  1 
ATOM   4720 C C   . PHE D 4 45  ? -23.409 1.294   -53.473 1.00 84.46  ? 45  PHE D C   1 
ATOM   4721 O O   . PHE D 4 45  ? -23.676 2.499   -53.389 1.00 82.33  ? 45  PHE D O   1 
ATOM   4722 C CB  . PHE D 4 45  ? -25.561 0.091   -53.876 1.00 83.99  ? 45  PHE D CB  1 
ATOM   4723 C CG  . PHE D 4 45  ? -25.174 -0.462  -55.208 1.00 87.63  ? 45  PHE D CG  1 
ATOM   4724 C CD1 . PHE D 4 45  ? -24.778 -1.786  -55.327 1.00 89.36  ? 45  PHE D CD1 1 
ATOM   4725 C CD2 . PHE D 4 45  ? -25.187 0.336   -56.338 1.00 92.11  ? 45  PHE D CD2 1 
ATOM   4726 C CE1 . PHE D 4 45  ? -24.407 -2.309  -56.555 1.00 91.49  ? 45  PHE D CE1 1 
ATOM   4727 C CE2 . PHE D 4 45  ? -24.820 -0.181  -57.569 1.00 97.09  ? 45  PHE D CE2 1 
ATOM   4728 C CZ  . PHE D 4 45  ? -24.428 -1.506  -57.676 1.00 94.75  ? 45  PHE D CZ  1 
ATOM   4729 N N   . ALA D 4 46  ? -22.290 0.818   -54.030 1.00 85.33  ? 46  ALA D N   1 
ATOM   4730 C CA  . ALA D 4 46  ? -21.241 1.680   -54.576 1.00 86.45  ? 46  ALA D CA  1 
ATOM   4731 C C   . ALA D 4 46  ? -20.745 2.682   -53.534 1.00 85.61  ? 46  ALA D C   1 
ATOM   4732 O O   . ALA D 4 46  ? -20.435 3.834   -53.850 1.00 84.16  ? 46  ALA D O   1 
ATOM   4733 C CB  . ALA D 4 46  ? -21.717 2.398   -55.843 1.00 88.50  ? 46  ALA D CB  1 
ATOM   4734 N N   . GLY D 4 47  ? -20.676 2.241   -52.276 1.00 83.36  ? 47  GLY D N   1 
ATOM   4735 C CA  . GLY D 4 47  ? -20.209 3.091   -51.198 1.00 75.61  ? 47  GLY D CA  1 
ATOM   4736 C C   . GLY D 4 47  ? -21.137 4.218   -50.808 1.00 76.26  ? 47  GLY D C   1 
ATOM   4737 O O   . GLY D 4 47  ? -20.705 5.137   -50.110 1.00 73.83  ? 47  GLY D O   1 
ATOM   4738 N N   . LYS D 4 48  ? -22.396 4.182   -51.234 1.00 80.64  ? 48  LYS D N   1 
ATOM   4739 C CA  . LYS D 4 48  ? -23.376 5.214   -50.921 1.00 82.81  ? 48  LYS D CA  1 
ATOM   4740 C C   . LYS D 4 48  ? -24.543 4.591   -50.168 1.00 77.87  ? 48  LYS D C   1 
ATOM   4741 O O   . LYS D 4 48  ? -24.988 3.489   -50.499 1.00 76.07  ? 48  LYS D O   1 
ATOM   4742 C CB  . LYS D 4 48  ? -23.883 5.905   -52.204 1.00 84.21  ? 48  LYS D CB  1 
ATOM   4743 C CG  . LYS D 4 48  ? -22.827 6.735   -52.935 1.00 88.59  ? 48  LYS D CG  1 
ATOM   4744 C CD  . LYS D 4 48  ? -22.662 8.128   -52.315 1.00 92.00  ? 48  LYS D CD  1 
ATOM   4745 C CE  . LYS D 4 48  ? -21.333 8.772   -52.706 1.00 88.34  ? 48  LYS D CE  1 
ATOM   4746 N NZ  . LYS D 4 48  ? -21.040 8.652   -54.165 1.00 94.41  ? 48  LYS D NZ  1 
ATOM   4747 N N   . GLN D 4 49  ? -25.038 5.287   -49.150 1.00 79.34  ? 49  GLN D N   1 
ATOM   4748 C CA  . GLN D 4 49  ? -26.195 4.789   -48.422 1.00 81.18  ? 49  GLN D CA  1 
ATOM   4749 C C   . GLN D 4 49  ? -27.460 5.045   -49.234 1.00 85.69  ? 49  GLN D C   1 
ATOM   4750 O O   . GLN D 4 49  ? -27.693 6.158   -49.714 1.00 90.12  ? 49  GLN D O   1 
ATOM   4751 C CB  . GLN D 4 49  ? -26.282 5.429   -47.038 1.00 81.37  ? 49  GLN D CB  1 
ATOM   4752 C CG  . GLN D 4 49  ? -25.103 5.052   -46.137 1.00 77.19  ? 49  GLN D CG  1 
ATOM   4753 C CD  . GLN D 4 49  ? -25.361 5.285   -44.653 1.00 78.04  ? 49  GLN D CD  1 
ATOM   4754 O OE1 . GLN D 4 49  ? -26.508 5.323   -44.195 1.00 82.56  ? 49  GLN D OE1 1 
ATOM   4755 N NE2 . GLN D 4 49  ? -24.287 5.437   -43.894 1.00 71.64  ? 49  GLN D NE2 1 
ATOM   4756 N N   . LEU D 4 50  ? -28.268 4.003   -49.397 1.00 86.50  ? 50  LEU D N   1 
ATOM   4757 C CA  . LEU D 4 50  ? -29.432 4.062   -50.265 1.00 89.78  ? 50  LEU D CA  1 
ATOM   4758 C C   . LEU D 4 50  ? -30.613 4.654   -49.502 1.00 100.95 ? 50  LEU D C   1 
ATOM   4759 O O   . LEU D 4 50  ? -30.998 4.144   -48.445 1.00 99.70  ? 50  LEU D O   1 
ATOM   4760 C CB  . LEU D 4 50  ? -29.754 2.666   -50.795 1.00 88.20  ? 50  LEU D CB  1 
ATOM   4761 C CG  . LEU D 4 50  ? -28.606 1.975   -51.538 1.00 80.97  ? 50  LEU D CG  1 
ATOM   4762 C CD1 . LEU D 4 50  ? -29.018 0.604   -52.041 1.00 80.18  ? 50  LEU D CD1 1 
ATOM   4763 C CD2 . LEU D 4 50  ? -28.107 2.837   -52.679 1.00 82.26  ? 50  LEU D CD2 1 
ATOM   4764 N N   . GLU D 4 51  ? -31.177 5.738   -50.034 1.00 110.00 ? 51  GLU D N   1 
ATOM   4765 C CA  . GLU D 4 51  ? -32.326 6.383   -49.412 1.00 113.09 ? 51  GLU D CA  1 
ATOM   4766 C C   . GLU D 4 51  ? -33.581 5.536   -49.598 1.00 114.18 ? 51  GLU D C   1 
ATOM   4767 O O   . GLU D 4 51  ? -33.778 4.916   -50.646 1.00 112.57 ? 51  GLU D O   1 
ATOM   4768 C CB  . GLU D 4 51  ? -32.541 7.773   -50.012 1.00 115.78 ? 51  GLU D CB  1 
ATOM   4769 C CG  . GLU D 4 51  ? -31.281 8.621   -50.143 1.00 120.11 ? 51  GLU D CG  1 
ATOM   4770 C CD  . GLU D 4 51  ? -30.969 9.422   -48.892 1.00 131.55 ? 51  GLU D CD  1 
ATOM   4771 O OE1 . GLU D 4 51  ? -30.475 8.830   -47.908 1.00 129.54 ? 51  GLU D OE1 1 
ATOM   4772 O OE2 . GLU D 4 51  ? -31.223 10.648  -48.897 1.00 138.42 ? 51  GLU D OE2 1 
ATOM   4773 N N   . ASP D 4 52  ? -34.447 5.535   -48.578 1.00 112.18 ? 52  ASP D N   1 
ATOM   4774 C CA  . ASP D 4 52  ? -35.643 4.694   -48.595 1.00 110.25 ? 52  ASP D CA  1 
ATOM   4775 C C   . ASP D 4 52  ? -36.641 5.109   -49.673 1.00 112.60 ? 52  ASP D C   1 
ATOM   4776 O O   . ASP D 4 52  ? -37.548 4.330   -49.996 1.00 109.17 ? 52  ASP D O   1 
ATOM   4777 C CB  . ASP D 4 52  ? -36.318 4.724   -47.222 1.00 107.30 ? 52  ASP D CB  1 
ATOM   4778 C CG  . ASP D 4 52  ? -35.371 4.327   -46.102 1.00 106.53 ? 52  ASP D CG  1 
ATOM   4779 O OD1 . ASP D 4 52  ? -34.295 4.959   -45.980 1.00 107.92 ? 52  ASP D OD1 1 
ATOM   4780 O OD2 . ASP D 4 52  ? -35.688 3.379   -45.349 1.00 103.09 ? 52  ASP D OD2 1 
ATOM   4781 N N   . GLY D 4 53  ? -36.501 6.310   -50.234 1.00 114.22 ? 53  GLY D N   1 
ATOM   4782 C CA  . GLY D 4 53  ? -37.444 6.814   -51.217 1.00 108.68 ? 53  GLY D CA  1 
ATOM   4783 C C   . GLY D 4 53  ? -37.088 6.495   -52.655 1.00 111.68 ? 53  GLY D C   1 
ATOM   4784 O O   . GLY D 4 53  ? -37.944 6.040   -53.421 1.00 110.82 ? 53  GLY D O   1 
ATOM   4785 N N   . ARG D 4 54  ? -35.835 6.738   -53.038 1.00 113.60 ? 54  ARG D N   1 
ATOM   4786 C CA  . ARG D 4 54  ? -35.396 6.419   -54.389 1.00 117.46 ? 54  ARG D CA  1 
ATOM   4787 C C   . ARG D 4 54  ? -35.510 4.917   -54.632 1.00 117.60 ? 54  ARG D C   1 
ATOM   4788 O O   . ARG D 4 54  ? -35.422 4.108   -53.706 1.00 116.88 ? 54  ARG D O   1 
ATOM   4789 C CB  . ARG D 4 54  ? -33.956 6.894   -54.606 1.00 110.73 ? 54  ARG D CB  1 
ATOM   4790 N N   . THR D 4 55  ? -35.741 4.540   -55.885 1.00 119.22 ? 55  THR D N   1 
ATOM   4791 C CA  . THR D 4 55  ? -35.912 3.134   -56.214 1.00 120.76 ? 55  THR D CA  1 
ATOM   4792 C C   . THR D 4 55  ? -34.581 2.557   -56.696 1.00 118.23 ? 55  THR D C   1 
ATOM   4793 O O   . THR D 4 55  ? -33.539 3.218   -56.651 1.00 117.71 ? 55  THR D O   1 
ATOM   4794 C CB  . THR D 4 55  ? -37.032 2.952   -57.247 1.00 126.16 ? 55  THR D CB  1 
ATOM   4795 O OG1 . THR D 4 55  ? -36.541 3.233   -58.565 1.00 125.59 ? 55  THR D OG1 1 
ATOM   4796 C CG2 . THR D 4 55  ? -38.203 3.878   -56.936 1.00 121.94 ? 55  THR D CG2 1 
ATOM   4797 N N   . LEU D 4 56  ? -34.609 1.302   -57.154 1.00 119.71 ? 56  LEU D N   1 
ATOM   4798 C CA  . LEU D 4 56  ? -33.373 0.621   -57.535 1.00 120.47 ? 56  LEU D CA  1 
ATOM   4799 C C   . LEU D 4 56  ? -32.749 1.228   -58.791 1.00 118.59 ? 56  LEU D C   1 
ATOM   4800 O O   . LEU D 4 56  ? -31.523 1.389   -58.862 1.00 110.38 ? 56  LEU D O   1 
ATOM   4801 C CB  . LEU D 4 56  ? -33.638 -0.873  -57.736 1.00 118.06 ? 56  LEU D CB  1 
ATOM   4802 C CG  . LEU D 4 56  ? -33.801 -1.756  -56.495 1.00 118.22 ? 56  LEU D CG  1 
ATOM   4803 C CD1 . LEU D 4 56  ? -34.185 -3.158  -56.917 1.00 115.98 ? 56  LEU D CD1 1 
ATOM   4804 C CD2 . LEU D 4 56  ? -32.527 -1.781  -55.642 1.00 107.30 ? 56  LEU D CD2 1 
ATOM   4805 N N   . SER D 4 57  ? -33.566 1.565   -59.796 1.00 118.64 ? 57  SER D N   1 
ATOM   4806 C CA  . SER D 4 57  ? -33.017 2.106   -61.036 1.00 120.25 ? 57  SER D CA  1 
ATOM   4807 C C   . SER D 4 57  ? -32.469 3.520   -60.866 1.00 119.05 ? 57  SER D C   1 
ATOM   4808 O O   . SER D 4 57  ? -31.708 3.983   -61.723 1.00 117.40 ? 57  SER D O   1 
ATOM   4809 C CB  . SER D 4 57  ? -34.074 2.079   -62.146 1.00 121.85 ? 57  SER D CB  1 
ATOM   4810 O OG  . SER D 4 57  ? -35.277 2.697   -61.730 1.00 123.10 ? 57  SER D OG  1 
ATOM   4811 N N   . ASP D 4 58  ? -32.835 4.214   -59.784 1.00 118.26 ? 58  ASP D N   1 
ATOM   4812 C CA  . ASP D 4 58  ? -32.279 5.535   -59.515 1.00 120.01 ? 58  ASP D CA  1 
ATOM   4813 C C   . ASP D 4 58  ? -30.816 5.473   -59.090 1.00 116.76 ? 58  ASP D C   1 
ATOM   4814 O O   . ASP D 4 58  ? -30.108 6.480   -59.218 1.00 113.10 ? 58  ASP D O   1 
ATOM   4815 C CB  . ASP D 4 58  ? -33.099 6.243   -58.434 1.00 122.37 ? 58  ASP D CB  1 
ATOM   4816 C CG  . ASP D 4 58  ? -34.587 6.134   -58.673 1.00 125.11 ? 58  ASP D CG  1 
ATOM   4817 O OD1 . ASP D 4 58  ? -35.067 4.995   -58.849 1.00 124.96 ? 58  ASP D OD1 1 
ATOM   4818 O OD2 . ASP D 4 58  ? -35.273 7.178   -58.684 1.00 126.81 ? 58  ASP D OD2 1 
ATOM   4819 N N   . TYR D 4 59  ? -30.357 4.328   -58.570 1.00 116.64 ? 59  TYR D N   1 
ATOM   4820 C CA  . TYR D 4 59  ? -28.962 4.125   -58.191 1.00 111.41 ? 59  TYR D CA  1 
ATOM   4821 C C   . TYR D 4 59  ? -28.209 3.210   -59.152 1.00 109.43 ? 59  TYR D C   1 
ATOM   4822 O O   . TYR D 4 59  ? -27.097 2.778   -58.823 1.00 105.61 ? 59  TYR D O   1 
ATOM   4823 C CB  . TYR D 4 59  ? -28.849 3.545   -56.780 1.00 104.01 ? 59  TYR D CB  1 
ATOM   4824 C CG  . TYR D 4 59  ? -29.428 4.369   -55.653 1.00 102.92 ? 59  TYR D CG  1 
ATOM   4825 C CD1 . TYR D 4 59  ? -28.808 5.536   -55.216 1.00 101.87 ? 59  TYR D CD1 1 
ATOM   4826 C CD2 . TYR D 4 59  ? -30.561 3.940   -54.982 1.00 102.17 ? 59  TYR D CD2 1 
ATOM   4827 C CE1 . TYR D 4 59  ? -29.328 6.268   -54.168 1.00 98.77  ? 59  TYR D CE1 1 
ATOM   4828 C CE2 . TYR D 4 59  ? -31.087 4.664   -53.934 1.00 101.39 ? 59  TYR D CE2 1 
ATOM   4829 C CZ  . TYR D 4 59  ? -30.469 5.827   -53.530 1.00 100.84 ? 59  TYR D CZ  1 
ATOM   4830 O OH  . TYR D 4 59  ? -30.996 6.548   -52.481 1.00 103.45 ? 59  TYR D OH  1 
ATOM   4831 N N   . ASN D 4 60  ? -28.797 2.872   -60.307 1.00 109.58 ? 60  ASN D N   1 
ATOM   4832 C CA  . ASN D 4 60  ? -28.103 2.142   -61.374 1.00 106.17 ? 60  ASN D CA  1 
ATOM   4833 C C   . ASN D 4 60  ? -27.802 0.689   -60.981 1.00 104.22 ? 60  ASN D C   1 
ATOM   4834 O O   . ASN D 4 60  ? -26.742 0.149   -61.309 1.00 103.35 ? 60  ASN D O   1 
ATOM   4835 C CB  . ASN D 4 60  ? -26.821 2.879   -61.782 1.00 102.15 ? 60  ASN D CB  1 
ATOM   4836 C CG  . ASN D 4 60  ? -26.267 2.407   -63.099 1.00 103.43 ? 60  ASN D CG  1 
ATOM   4837 O OD1 . ASN D 4 60  ? -26.978 1.819   -63.911 1.00 107.14 ? 60  ASN D OD1 1 
ATOM   4838 N ND2 . ASN D 4 60  ? -24.983 2.667   -63.323 1.00 103.35 ? 60  ASN D ND2 1 
ATOM   4839 N N   . ILE D 4 61  ? -28.748 0.043   -60.299 1.00 104.39 ? 61  ILE D N   1 
ATOM   4840 C CA  . ILE D 4 61  ? -28.590 -1.324  -59.805 1.00 102.07 ? 61  ILE D CA  1 
ATOM   4841 C C   . ILE D 4 61  ? -29.230 -2.260  -60.829 1.00 102.51 ? 61  ILE D C   1 
ATOM   4842 O O   . ILE D 4 61  ? -30.448 -2.468  -60.827 1.00 102.12 ? 61  ILE D O   1 
ATOM   4843 C CB  . ILE D 4 61  ? -29.207 -1.495  -58.410 1.00 101.42 ? 61  ILE D CB  1 
ATOM   4844 C CG1 . ILE D 4 61  ? -28.445 -0.667  -57.368 1.00 97.07  ? 61  ILE D CG1 1 
ATOM   4845 C CG2 . ILE D 4 61  ? -29.229 -2.958  -57.988 1.00 96.59  ? 61  ILE D CG2 1 
ATOM   4846 C CD1 . ILE D 4 61  ? -29.346 0.084   -56.412 1.00 95.46  ? 61  ILE D CD1 1 
ATOM   4847 N N   . GLN D 4 62  ? -28.409 -2.840  -61.704 1.00 105.18 ? 62  GLN D N   1 
ATOM   4848 C CA  . GLN D 4 62  ? -28.893 -3.734  -62.748 1.00 108.92 ? 62  GLN D CA  1 
ATOM   4849 C C   . GLN D 4 62  ? -28.911 -5.173  -62.218 1.00 111.57 ? 62  GLN D C   1 
ATOM   4850 O O   . GLN D 4 62  ? -28.718 -5.421  -61.023 1.00 101.91 ? 62  GLN D O   1 
ATOM   4851 C CB  . GLN D 4 62  ? -28.042 -3.578  -64.009 1.00 99.04  ? 62  GLN D CB  1 
ATOM   4852 N N   . LYS D 4 63  ? -29.155 -6.138  -63.106 1.00 110.11 ? 63  LYS D N   1 
ATOM   4853 C CA  . LYS D 4 63  ? -29.263 -7.532  -62.697 1.00 108.83 ? 63  LYS D CA  1 
ATOM   4854 C C   . LYS D 4 63  ? -27.933 -8.052  -62.164 1.00 109.64 ? 63  LYS D C   1 
ATOM   4855 O O   . LYS D 4 63  ? -26.859 -7.626  -62.594 1.00 113.87 ? 63  LYS D O   1 
ATOM   4856 C CB  . LYS D 4 63  ? -29.726 -8.399  -63.868 1.00 109.89 ? 63  LYS D CB  1 
ATOM   4857 N N   . GLU D 4 64  ? -28.019 -8.974  -61.204 1.00 104.45 ? 64  GLU D N   1 
ATOM   4858 C CA  . GLU D 4 64  ? -26.902 -9.723  -60.615 1.00 106.25 ? 64  GLU D CA  1 
ATOM   4859 C C   . GLU D 4 64  ? -26.061 -8.911  -59.636 1.00 106.72 ? 64  GLU D C   1 
ATOM   4860 O O   . GLU D 4 64  ? -25.056 -9.440  -59.141 1.00 106.01 ? 64  GLU D O   1 
ATOM   4861 C CB  . GLU D 4 64  ? -25.948 -10.298 -61.672 1.00 113.76 ? 64  GLU D CB  1 
ATOM   4862 C CG  . GLU D 4 64  ? -26.597 -11.156 -62.759 1.00 114.32 ? 64  GLU D CG  1 
ATOM   4863 C CD  . GLU D 4 64  ? -26.917 -12.556 -62.283 1.00 111.40 ? 64  GLU D CD  1 
ATOM   4864 O OE1 . GLU D 4 64  ? -26.256 -13.043 -61.336 1.00 114.16 ? 64  GLU D OE1 1 
ATOM   4865 O OE2 . GLU D 4 64  ? -27.841 -13.165 -62.852 1.00 105.26 ? 64  GLU D OE2 1 
ATOM   4866 N N   . SER D 4 65  ? -26.418 -7.666  -59.328 1.00 103.54 ? 65  SER D N   1 
ATOM   4867 C CA  . SER D 4 65  ? -25.584 -6.838  -58.467 1.00 97.29  ? 65  SER D CA  1 
ATOM   4868 C C   . SER D 4 65  ? -25.906 -7.080  -56.990 1.00 95.08  ? 65  SER D C   1 
ATOM   4869 O O   . SER D 4 65  ? -26.992 -7.544  -56.629 1.00 94.92  ? 65  SER D O   1 
ATOM   4870 C CB  . SER D 4 65  ? -25.744 -5.354  -58.817 1.00 95.68  ? 65  SER D CB  1 
ATOM   4871 O OG  . SER D 4 65  ? -27.102 -5.009  -59.005 1.00 98.39  ? 65  SER D OG  1 
ATOM   4872 N N   . THR D 4 66  ? -24.933 -6.763  -56.132 1.00 91.31  ? 66  THR D N   1 
ATOM   4873 C CA  . THR D 4 66  ? -25.032 -7.021  -54.698 1.00 88.82  ? 66  THR D CA  1 
ATOM   4874 C C   . THR D 4 66  ? -25.026 -5.711  -53.921 1.00 81.34  ? 66  THR D C   1 
ATOM   4875 O O   . THR D 4 66  ? -24.174 -4.848  -54.159 1.00 80.43  ? 66  THR D O   1 
ATOM   4876 C CB  . THR D 4 66  ? -23.891 -7.925  -54.216 1.00 82.31  ? 66  THR D CB  1 
ATOM   4877 O OG1 . THR D 4 66  ? -23.945 -9.170  -54.922 1.00 90.19  ? 66  THR D OG1 1 
ATOM   4878 C CG2 . THR D 4 66  ? -24.022 -8.205  -52.738 1.00 77.27  ? 66  THR D CG2 1 
ATOM   4879 N N   . LEU D 4 67  ? -25.989 -5.567  -53.011 1.00 74.70  ? 67  LEU D N   1 
ATOM   4880 C CA  . LEU D 4 67  ? -26.035 -4.488  -52.035 1.00 80.51  ? 67  LEU D CA  1 
ATOM   4881 C C   . LEU D 4 67  ? -25.462 -4.980  -50.707 1.00 78.69  ? 67  LEU D C   1 
ATOM   4882 O O   . LEU D 4 67  ? -25.519 -6.173  -50.396 1.00 79.23  ? 67  LEU D O   1 
ATOM   4883 C CB  . LEU D 4 67  ? -27.472 -3.992  -51.819 1.00 80.41  ? 67  LEU D CB  1 
ATOM   4884 C CG  . LEU D 4 67  ? -28.440 -3.800  -52.991 1.00 80.66  ? 67  LEU D CG  1 
ATOM   4885 C CD1 . LEU D 4 67  ? -29.843 -3.527  -52.465 1.00 80.04  ? 67  LEU D CD1 1 
ATOM   4886 C CD2 . LEU D 4 67  ? -27.997 -2.684  -53.922 1.00 85.33  ? 67  LEU D CD2 1 
ATOM   4887 N N   . HIS D 4 68  ? -24.919 -4.056  -49.917 1.00 74.50  ? 68  HIS D N   1 
ATOM   4888 C CA  . HIS D 4 68  ? -24.306 -4.387  -48.635 1.00 72.85  ? 68  HIS D CA  1 
ATOM   4889 C C   . HIS D 4 68  ? -25.272 -4.032  -47.505 1.00 74.27  ? 68  HIS D C   1 
ATOM   4890 O O   . HIS D 4 68  ? -25.838 -2.934  -47.490 1.00 75.32  ? 68  HIS D O   1 
ATOM   4891 C CB  . HIS D 4 68  ? -22.966 -3.656  -48.480 1.00 68.43  ? 68  HIS D CB  1 
ATOM   4892 C CG  . HIS D 4 68  ? -22.300 -3.863  -47.147 1.00 81.12  ? 68  HIS D CG  1 
ATOM   4893 N ND1 . HIS D 4 68  ? -21.272 -3.059  -46.695 1.00 74.65  ? 68  HIS D ND1 1 
ATOM   4894 C CD2 . HIS D 4 68  ? -22.515 -4.776  -46.167 1.00 76.14  ? 68  HIS D CD2 1 
ATOM   4895 C CE1 . HIS D 4 68  ? -20.882 -3.469  -45.502 1.00 72.16  ? 68  HIS D CE1 1 
ATOM   4896 N NE2 . HIS D 4 68  ? -21.623 -4.508  -45.157 1.00 77.91  ? 68  HIS D NE2 1 
ATOM   4897 N N   . LEU D 4 69  ? -25.470 -4.966  -46.569 1.00 73.31  ? 69  LEU D N   1 
ATOM   4898 C CA  . LEU D 4 69  ? -26.389 -4.794  -45.444 1.00 69.42  ? 69  LEU D CA  1 
ATOM   4899 C C   . LEU D 4 69  ? -25.614 -4.536  -44.154 1.00 66.23  ? 69  LEU D C   1 
ATOM   4900 O O   . LEU D 4 69  ? -24.825 -5.383  -43.720 1.00 65.78  ? 69  LEU D O   1 
ATOM   4901 C CB  . LEU D 4 69  ? -27.277 -6.027  -45.282 1.00 67.97  ? 69  LEU D CB  1 
ATOM   4902 C CG  . LEU D 4 69  ? -28.356 -5.952  -44.201 1.00 66.58  ? 69  LEU D CG  1 
ATOM   4903 C CD1 . LEU D 4 69  ? -29.427 -4.925  -44.553 1.00 69.37  ? 69  LEU D CD1 1 
ATOM   4904 C CD2 . LEU D 4 69  ? -28.974 -7.319  -43.966 1.00 66.45  ? 69  LEU D CD2 1 
ATOM   4905 N N   . VAL D 4 70  ? -25.869 -3.382  -43.532 1.00 64.91  ? 70  VAL D N   1 
ATOM   4906 C CA  . VAL D 4 70  ? -25.293 -2.997  -42.244 1.00 60.36  ? 70  VAL D CA  1 
ATOM   4907 C C   . VAL D 4 70  ? -26.420 -2.966  -41.221 1.00 60.44  ? 70  VAL D C   1 
ATOM   4908 O O   . VAL D 4 70  ? -27.472 -2.366  -41.466 1.00 62.70  ? 70  VAL D O   1 
ATOM   4909 C CB  . VAL D 4 70  ? -24.586 -1.628  -42.312 1.00 59.84  ? 70  VAL D CB  1 
ATOM   4910 C CG1 . VAL D 4 70  ? -24.077 -1.204  -40.937 1.00 54.01  ? 70  VAL D CG1 1 
ATOM   4911 C CG2 . VAL D 4 70  ? -23.444 -1.648  -43.316 1.00 58.80  ? 70  VAL D CG2 1 
ATOM   4912 N N   . LEU D 4 71  ? -26.204 -3.609  -40.081 1.00 58.72  ? 71  LEU D N   1 
ATOM   4913 C CA  . LEU D 4 71  ? -27.236 -3.770  -39.072 1.00 55.17  ? 71  LEU D CA  1 
ATOM   4914 C C   . LEU D 4 71  ? -26.860 -3.044  -37.786 1.00 55.45  ? 71  LEU D C   1 
ATOM   4915 O O   . LEU D 4 71  ? -25.687 -2.784  -37.504 1.00 51.32  ? 71  LEU D O   1 
ATOM   4916 C CB  . LEU D 4 71  ? -27.472 -5.255  -38.782 1.00 54.96  ? 71  LEU D CB  1 
ATOM   4917 C CG  . LEU D 4 71  ? -27.808 -6.128  -39.999 1.00 59.11  ? 71  LEU D CG  1 
ATOM   4918 C CD1 . LEU D 4 71  ? -28.001 -7.581  -39.604 1.00 53.39  ? 71  LEU D CD1 1 
ATOM   4919 C CD2 . LEU D 4 71  ? -29.037 -5.613  -40.742 1.00 61.45  ? 71  LEU D CD2 1 
ATOM   4920 N N   . ARG D 4 72  ? -27.884 -2.699  -37.013 1.00 55.33  ? 72  ARG D N   1 
ATOM   4921 C CA  . ARG D 4 72  ? -27.667 -2.228  -35.654 1.00 52.00  ? 72  ARG D CA  1 
ATOM   4922 C C   . ARG D 4 72  ? -26.832 -3.248  -34.885 1.00 45.99  ? 72  ARG D C   1 
ATOM   4923 O O   . ARG D 4 72  ? -27.111 -4.449  -34.913 1.00 43.69  ? 72  ARG D O   1 
ATOM   4924 C CB  . ARG D 4 72  ? -29.018 -2.008  -34.961 1.00 55.78  ? 72  ARG D CB  1 
ATOM   4925 C CG  . ARG D 4 72  ? -29.334 -0.564  -34.646 1.00 58.49  ? 72  ARG D CG  1 
ATOM   4926 C CD  . ARG D 4 72  ? -30.776 -0.253  -34.947 1.00 69.91  ? 72  ARG D CD  1 
ATOM   4927 N NE  . ARG D 4 72  ? -31.025 1.181   -34.958 1.00 74.10  ? 72  ARG D NE  1 
ATOM   4928 C CZ  . ARG D 4 72  ? -30.648 2.005   -35.929 1.00 79.25  ? 72  ARG D CZ  1 
ATOM   4929 N NH1 . ARG D 4 72  ? -29.984 1.572   -36.993 1.00 78.24  ? 72  ARG D NH1 1 
ATOM   4930 N NH2 . ARG D 4 72  ? -30.943 3.299   -35.830 1.00 82.16  ? 72  ARG D NH2 1 
ATOM   4931 N N   . LEU D 4 73  ? -25.786 -2.771  -34.215 1.00 45.01  ? 73  LEU D N   1 
ATOM   4932 C CA  . LEU D 4 73  ? -24.943 -3.655  -33.412 1.00 40.51  ? 73  LEU D CA  1 
ATOM   4933 C C   . LEU D 4 73  ? -25.548 -3.779  -32.019 1.00 38.81  ? 73  LEU D C   1 
ATOM   4934 O O   . LEU D 4 73  ? -25.022 -3.274  -31.029 1.00 37.38  ? 73  LEU D O   1 
ATOM   4935 C CB  . LEU D 4 73  ? -23.514 -3.135  -33.346 1.00 36.92  ? 73  LEU D CB  1 
ATOM   4936 C CG  . LEU D 4 73  ? -22.773 -2.948  -34.659 1.00 37.93  ? 73  LEU D CG  1 
ATOM   4937 C CD1 . LEU D 4 73  ? -21.335 -2.646  -34.330 1.00 37.83  ? 73  LEU D CD1 1 
ATOM   4938 C CD2 . LEU D 4 73  ? -22.887 -4.179  -35.569 1.00 34.27  ? 73  LEU D CD2 1 
ATOM   4939 N N   . ARG D 4 74  ? -26.704 -4.446  -31.966 1.00 39.75  ? 74  ARG D N   1 
ATOM   4940 C CA  . ARG D 4 74  ? -27.375 -4.653  -30.685 1.00 38.33  ? 74  ARG D CA  1 
ATOM   4941 C C   . ARG D 4 74  ? -26.552 -5.540  -29.761 1.00 34.86  ? 74  ARG D C   1 
ATOM   4942 O O   . ARG D 4 74  ? -26.610 -5.386  -28.538 1.00 34.47  ? 74  ARG D O   1 
ATOM   4943 C CB  . ARG D 4 74  ? -28.764 -5.262  -30.903 1.00 40.21  ? 74  ARG D CB  1 
ATOM   4944 C CG  . ARG D 4 74  ? -29.714 -4.352  -31.612 1.00 44.72  ? 74  ARG D CG  1 
ATOM   4945 C CD  . ARG D 4 74  ? -31.103 -4.905  -31.552 1.00 49.18  ? 74  ARG D CD  1 
ATOM   4946 N NE  . ARG D 4 74  ? -31.161 -6.238  -32.126 1.00 53.61  ? 74  ARG D NE  1 
ATOM   4947 C CZ  . ARG D 4 74  ? -32.291 -6.876  -32.395 1.00 57.08  ? 74  ARG D CZ  1 
ATOM   4948 N NH1 . ARG D 4 74  ? -33.467 -6.329  -32.132 1.00 55.78  ? 74  ARG D NH1 1 
ATOM   4949 N NH2 . ARG D 4 74  ? -32.239 -8.090  -32.945 1.00 57.14  ? 74  ARG D NH2 1 
ATOM   4950 N N   . ARG D 4 75  ? -25.796 -6.482  -30.320 1.00 35.68  ? 75  ARG D N   1 
ATOM   4951 C CA  . ARG D 4 75  ? -24.929 -7.349  -29.542 1.00 34.06  ? 75  ARG D CA  1 
ATOM   4952 C C   . ARG D 4 75  ? -23.473 -6.950  -29.659 1.00 34.77  ? 75  ARG D C   1 
ATOM   4953 O O   . ARG D 4 75  ? -22.594 -7.790  -29.439 1.00 36.36  ? 75  ARG D O   1 
ATOM   4954 C CB  . ARG D 4 75  ? -25.112 -8.802  -29.965 1.00 33.06  ? 75  ARG D CB  1 
ATOM   4955 C CG  . ARG D 4 75  ? -26.544 -9.255  -29.884 1.00 34.91  ? 75  ARG D CG  1 
ATOM   4956 C CD  . ARG D 4 75  ? -26.628 -10.748 -29.676 1.00 33.40  ? 75  ARG D CD  1 
ATOM   4957 N NE  . ARG D 4 75  ? -27.204 -11.408 -30.831 1.00 39.30  ? 75  ARG D NE  1 
ATOM   4958 C CZ  . ARG D 4 75  ? -27.516 -12.692 -30.873 1.00 43.59  ? 75  ARG D CZ  1 
ATOM   4959 N NH1 . ARG D 4 75  ? -27.371 -13.473 -29.813 1.00 42.34  ? 75  ARG D NH1 1 
ATOM   4960 N NH2 . ARG D 4 75  ? -27.986 -13.207 -32.006 1.00 44.90  ? 75  ARG D NH2 1 
ATOM   4961 N N   . GLY D 4 76  ? -23.203 -5.696  -30.016 1.00 33.41  ? 76  GLY D N   1 
ATOM   4962 C CA  . GLY D 4 76  ? -21.845 -5.193  -30.076 1.00 30.96  ? 76  GLY D CA  1 
ATOM   4963 C C   . GLY D 4 76  ? -21.025 -5.760  -31.225 1.00 34.69  ? 76  GLY D C   1 
ATOM   4964 O O   . GLY D 4 76  ? -21.515 -6.406  -32.155 1.00 36.86  ? 76  GLY D O   1 
ATOM   4965 O OXT . GLY D 4 76  ? -19.819 -5.563  -31.268 1.00 32.67  ? 76  GLY D OXT 1 
HETATM 4966 C C1  . GOL E 5 .   ? -10.195 -15.622 -5.542  1.00 37.86  ? 401 GOL A C1  1 
HETATM 4967 O O1  . GOL E 5 .   ? -9.896  -15.814 -6.931  1.00 32.53  ? 401 GOL A O1  1 
HETATM 4968 C C2  . GOL E 5 .   ? -11.509 -16.204 -5.026  1.00 30.69  ? 401 GOL A C2  1 
HETATM 4969 O O2  . GOL E 5 .   ? -12.639 -15.505 -5.549  1.00 31.22  ? 401 GOL A O2  1 
HETATM 4970 C C3  . GOL E 5 .   ? -11.547 -17.691 -5.336  1.00 32.42  ? 401 GOL A C3  1 
HETATM 4971 O O3  . GOL E 5 .   ? -10.488 -18.310 -4.625  1.00 32.19  ? 401 GOL A O3  1 
HETATM 4972 C C1  . GOL F 5 .   ? 19.222  -29.724 13.372  1.00 45.56  ? 201 GOL B C1  1 
HETATM 4973 O O1  . GOL F 5 .   ? 18.673  -29.809 12.074  1.00 42.84  ? 201 GOL B O1  1 
HETATM 4974 C C2  . GOL F 5 .   ? 18.229  -29.045 14.304  1.00 50.38  ? 201 GOL B C2  1 
HETATM 4975 O O2  . GOL F 5 .   ? 17.112  -29.890 14.509  1.00 49.18  ? 201 GOL B O2  1 
HETATM 4976 C C3  . GOL F 5 .   ? 18.900  -28.666 15.621  1.00 55.01  ? 201 GOL B C3  1 
HETATM 4977 O O3  . GOL F 5 .   ? 20.169  -28.118 15.325  1.00 61.47  ? 201 GOL B O3  1 
HETATM 4978 O O   . HOH G 6 .   ? -8.022  -5.934  -38.748 1.00 44.23  ? 501 HOH A O   1 
HETATM 4979 O O   . HOH G 6 .   ? -15.949 -3.987  -20.564 1.00 25.13  ? 502 HOH A O   1 
HETATM 4980 O O   . HOH G 6 .   ? -12.105 -33.825 3.397   1.00 44.44  ? 503 HOH A O   1 
HETATM 4981 O O   . HOH G 6 .   ? -14.148 16.762  -32.527 1.00 42.18  ? 504 HOH A O   1 
HETATM 4982 O O   . HOH G 6 .   ? -13.054 11.889  -7.246  1.00 46.70  ? 505 HOH A O   1 
HETATM 4983 O O   . HOH G 6 .   ? -17.603 23.480  -14.877 1.00 40.27  ? 506 HOH A O   1 
HETATM 4984 O O   . HOH G 6 .   ? -17.411 21.031  -19.232 1.00 34.96  ? 507 HOH A O   1 
HETATM 4985 O O   . HOH G 6 .   ? -17.798 1.499   -43.954 1.00 40.08  ? 508 HOH A O   1 
HETATM 4986 O O   . HOH G 6 .   ? -19.380 -19.460 -28.180 1.00 39.90  ? 509 HOH A O   1 
HETATM 4987 O O   . HOH G 6 .   ? -24.634 -24.520 -1.296  1.00 35.92  ? 510 HOH A O   1 
HETATM 4988 O O   . HOH G 6 .   ? -1.409  0.106   -31.154 1.00 33.24  ? 511 HOH A O   1 
HETATM 4989 O O   . HOH G 6 .   ? 2.186   14.737  -29.697 1.00 46.31  ? 512 HOH A O   1 
HETATM 4990 O O   . HOH G 6 .   ? -2.040  9.106   -30.458 1.00 39.30  ? 513 HOH A O   1 
HETATM 4991 O O   . HOH G 6 .   ? -28.159 -19.335 -16.726 1.00 39.40  ? 514 HOH A O   1 
HETATM 4992 O O   . HOH G 6 .   ? -30.811 -10.630 -31.685 1.00 47.95  ? 515 HOH A O   1 
HETATM 4993 O O   . HOH G 6 .   ? -35.207 7.408   -20.001 1.00 38.14  ? 516 HOH A O   1 
HETATM 4994 O O   . HOH G 6 .   ? -24.229 -12.104 -0.901  1.00 27.85  ? 517 HOH A O   1 
HETATM 4995 O O   . HOH G 6 .   ? -35.707 3.767   -32.773 1.00 64.57  ? 518 HOH A O   1 
HETATM 4996 O O   . HOH G 6 .   ? -1.704  -19.174 -11.134 1.00 33.58  ? 519 HOH A O   1 
HETATM 4997 O O   . HOH G 6 .   ? -6.339  -15.464 -4.736  1.00 27.98  ? 520 HOH A O   1 
HETATM 4998 O O   . HOH G 6 .   ? -15.402 -18.467 4.903   1.00 36.42  ? 521 HOH A O   1 
HETATM 4999 O O   . HOH G 6 .   ? -26.995 -5.841  -16.727 1.00 25.37  ? 522 HOH A O   1 
HETATM 5000 O O   . HOH G 6 .   ? -9.745  17.884  -20.072 1.00 36.55  ? 523 HOH A O   1 
HETATM 5001 O O   . HOH G 6 .   ? -25.420 -9.754  -4.691  1.00 24.75  ? 524 HOH A O   1 
HETATM 5002 O O   . HOH G 6 .   ? -40.302 -2.480  -6.733  1.00 41.45  ? 525 HOH A O   1 
HETATM 5003 O O   . HOH G 6 .   ? -33.677 1.585   -7.612  1.00 37.79  ? 526 HOH A O   1 
HETATM 5004 O O   . HOH G 6 .   ? -38.984 7.561   -9.283  1.00 48.57  ? 527 HOH A O   1 
HETATM 5005 O O   . HOH G 6 .   ? -22.838 -15.167 -14.129 1.00 25.33  ? 528 HOH A O   1 
HETATM 5006 O O   . HOH G 6 .   ? -33.455 -3.862  -11.424 1.00 33.79  ? 529 HOH A O   1 
HETATM 5007 O O   . HOH G 6 .   ? -6.962  -15.700 -0.393  1.00 31.30  ? 530 HOH A O   1 
HETATM 5008 O O   . HOH G 6 .   ? 5.579   -4.572  -23.287 1.00 38.75  ? 531 HOH A O   1 
HETATM 5009 O O   . HOH G 6 .   ? -28.799 -6.939  -4.020  1.00 35.46  ? 532 HOH A O   1 
HETATM 5010 O O   . HOH G 6 .   ? -0.106  -3.974  -14.607 1.00 28.40  ? 533 HOH A O   1 
HETATM 5011 O O   . HOH G 6 .   ? -34.287 -7.719  -21.167 1.00 42.19  ? 534 HOH A O   1 
HETATM 5012 O O   . HOH G 6 .   ? -26.542 5.034   -32.820 1.00 38.50  ? 535 HOH A O   1 
HETATM 5013 O O   . HOH G 6 .   ? -25.607 10.185  -5.485  1.00 38.54  ? 536 HOH A O   1 
HETATM 5014 O O   . HOH G 6 .   ? -7.284  -2.526  -8.168  1.00 34.95  ? 537 HOH A O   1 
HETATM 5015 O O   . HOH G 6 .   ? -8.782  1.678   -24.013 1.00 22.90  ? 538 HOH A O   1 
HETATM 5016 O O   . HOH G 6 .   ? -36.943 0.348   -23.332 1.00 47.52  ? 539 HOH A O   1 
HETATM 5017 O O   . HOH G 6 .   ? -13.559 -2.142  -6.633  1.00 33.43  ? 540 HOH A O   1 
HETATM 5018 O O   . HOH G 6 .   ? -32.414 -22.699 -11.934 1.00 48.64  ? 541 HOH A O   1 
HETATM 5019 O O   . HOH G 6 .   ? -6.974  -17.436 -21.031 1.00 38.54  ? 542 HOH A O   1 
HETATM 5020 O O   . HOH G 6 .   ? -22.808 -0.684  -23.641 1.00 25.84  ? 543 HOH A O   1 
HETATM 5021 O O   . HOH G 6 .   ? -32.769 -18.040 -18.196 1.00 50.97  ? 544 HOH A O   1 
HETATM 5022 O O   . HOH G 6 .   ? -9.488  17.077  -16.140 1.00 33.14  ? 545 HOH A O   1 
HETATM 5023 O O   . HOH G 6 .   ? -27.466 -5.436  -2.323  1.00 30.12  ? 546 HOH A O   1 
HETATM 5024 O O   . HOH G 6 .   ? -8.246  22.936  -24.717 1.00 44.36  ? 547 HOH A O   1 
HETATM 5025 O O   . HOH G 6 .   ? -20.930 2.212   -24.902 1.00 25.14  ? 548 HOH A O   1 
HETATM 5026 O O   . HOH G 6 .   ? -7.058  -15.052 -22.294 1.00 34.60  ? 549 HOH A O   1 
HETATM 5027 O O   . HOH G 6 .   ? -30.052 14.850  -16.804 1.00 33.43  ? 550 HOH A O   1 
HETATM 5028 O O   . HOH G 6 .   ? -16.524 0.027   -15.603 1.00 33.46  ? 551 HOH A O   1 
HETATM 5029 O O   . HOH G 6 .   ? -19.354 0.204   -41.857 1.00 40.80  ? 552 HOH A O   1 
HETATM 5030 O O   . HOH G 6 .   ? -17.614 -27.995 1.340   1.00 39.20  ? 553 HOH A O   1 
HETATM 5031 O O   . HOH G 6 .   ? -9.580  -3.772  -40.159 1.00 36.55  ? 554 HOH A O   1 
HETATM 5032 O O   . HOH G 6 .   ? -0.293  -22.176 -10.132 1.00 29.65  ? 555 HOH A O   1 
HETATM 5033 O O   . HOH G 6 .   ? -36.071 -1.332  -12.801 1.00 36.59  ? 556 HOH A O   1 
HETATM 5034 O O   . HOH G 6 .   ? -27.977 10.395  -2.235  1.00 35.47  ? 557 HOH A O   1 
HETATM 5035 O O   . HOH G 6 .   ? -21.399 7.209   -18.602 1.00 26.69  ? 558 HOH A O   1 
HETATM 5036 O O   . HOH G 6 .   ? -13.697 -31.126 -4.024  1.00 36.59  ? 559 HOH A O   1 
HETATM 5037 O O   . HOH G 6 .   ? -18.207 12.704  -27.985 1.00 30.53  ? 560 HOH A O   1 
HETATM 5038 O O   . HOH G 6 .   ? -13.814 -3.377  -18.855 1.00 31.19  ? 561 HOH A O   1 
HETATM 5039 O O   . HOH G 6 .   ? -34.493 -1.731  -10.528 1.00 34.91  ? 562 HOH A O   1 
HETATM 5040 O O   . HOH G 6 .   ? -23.076 -17.708 -8.421  1.00 31.63  ? 563 HOH A O   1 
HETATM 5041 O O   . HOH G 6 .   ? -12.210 23.239  -25.824 1.00 35.55  ? 564 HOH A O   1 
HETATM 5042 O O   . HOH G 6 .   ? -13.424 10.033  -9.996  1.00 35.75  ? 565 HOH A O   1 
HETATM 5043 O O   . HOH G 6 .   ? -16.785 -18.666 -28.613 1.00 33.14  ? 566 HOH A O   1 
HETATM 5044 O O   . HOH G 6 .   ? -10.133 10.029  -11.258 1.00 28.99  ? 567 HOH A O   1 
HETATM 5045 O O   . HOH G 6 .   ? -12.914 -18.544 -15.434 1.00 28.08  ? 568 HOH A O   1 
HETATM 5046 O O   . HOH G 6 .   ? -20.085 -1.376  -21.669 1.00 25.01  ? 569 HOH A O   1 
HETATM 5047 O O   . HOH G 6 .   ? -20.986 -4.692  -22.551 1.00 31.70  ? 570 HOH A O   1 
HETATM 5048 O O   . HOH G 6 .   ? -35.814 11.134  -19.152 1.00 39.61  ? 571 HOH A O   1 
HETATM 5049 O O   . HOH G 6 .   ? -4.137  -14.049 -24.416 1.00 31.58  ? 572 HOH A O   1 
HETATM 5050 O O   . HOH G 6 .   ? -33.011 -10.500 -14.906 1.00 34.92  ? 573 HOH A O   1 
HETATM 5051 O O   . HOH G 6 .   ? -19.171 -19.962 -21.412 1.00 37.74  ? 574 HOH A O   1 
HETATM 5052 O O   . HOH G 6 .   ? 5.719   -6.560  -19.115 1.00 38.11  ? 575 HOH A O   1 
HETATM 5053 O O   . HOH G 6 .   ? -0.419  10.769  -16.922 1.00 37.60  ? 576 HOH A O   1 
HETATM 5054 O O   . HOH G 6 .   ? -14.740 6.049   -39.124 1.00 38.19  ? 577 HOH A O   1 
HETATM 5055 O O   . HOH G 6 .   ? -5.960  -5.953  -37.358 1.00 38.75  ? 578 HOH A O   1 
HETATM 5056 O O   . HOH G 6 .   ? -17.420 -3.072  -45.437 1.00 50.65  ? 579 HOH A O   1 
HETATM 5057 O O   . HOH G 6 .   ? -24.661 8.158   -1.186  1.00 29.50  ? 580 HOH A O   1 
HETATM 5058 O O   . HOH G 6 .   ? -28.685 9.156   -22.288 1.00 36.76  ? 581 HOH A O   1 
HETATM 5059 O O   . HOH G 6 .   ? -17.650 1.232   -26.547 1.00 25.64  ? 582 HOH A O   1 
HETATM 5060 O O   . HOH G 6 .   ? -14.017 8.176   -23.132 1.00 24.65  ? 583 HOH A O   1 
HETATM 5061 O O   . HOH G 6 .   ? -35.457 -6.670  -16.125 1.00 38.03  ? 584 HOH A O   1 
HETATM 5062 O O   . HOH G 6 .   ? 0.051   -17.235 -7.282  1.00 30.99  ? 585 HOH A O   1 
HETATM 5063 O O   . HOH G 6 .   ? -17.962 18.968  -6.935  1.00 41.85  ? 586 HOH A O   1 
HETATM 5064 O O   . HOH G 6 .   ? -6.318  8.197   -13.587 1.00 25.56  ? 587 HOH A O   1 
HETATM 5065 O O   . HOH G 6 .   ? -19.549 2.113   -19.651 1.00 30.33  ? 588 HOH A O   1 
HETATM 5066 O O   . HOH G 6 .   ? -14.376 -16.759 -33.688 1.00 38.28  ? 589 HOH A O   1 
HETATM 5067 O O   . HOH G 6 .   ? -12.284 6.253   -15.781 1.00 29.26  ? 590 HOH A O   1 
HETATM 5068 O O   . HOH G 6 .   ? 3.167   -4.499  -21.953 1.00 35.03  ? 591 HOH A O   1 
HETATM 5069 O O   . HOH G 6 .   ? -25.681 -0.767  -29.675 1.00 33.45  ? 592 HOH A O   1 
HETATM 5070 O O   . HOH G 6 .   ? -11.832 -21.264 -15.258 1.00 35.06  ? 593 HOH A O   1 
HETATM 5071 O O   . HOH G 6 .   ? -23.484 1.988   -33.420 1.00 35.67  ? 594 HOH A O   1 
HETATM 5072 O O   . HOH G 6 .   ? -22.033 -18.698 -4.947  1.00 33.42  ? 595 HOH A O   1 
HETATM 5073 O O   . HOH G 6 .   ? -17.081 -4.594  -24.442 1.00 33.27  ? 596 HOH A O   1 
HETATM 5074 O O   . HOH G 6 .   ? -28.950 -5.094  -15.239 1.00 28.54  ? 597 HOH A O   1 
HETATM 5075 O O   . HOH G 6 .   ? -32.363 -10.573 -6.176  1.00 34.34  ? 598 HOH A O   1 
HETATM 5076 O O   . HOH G 6 .   ? -5.942  -11.732 -5.343  1.00 35.45  ? 599 HOH A O   1 
HETATM 5077 O O   . HOH G 6 .   ? -13.471 16.762  -29.751 1.00 36.09  ? 600 HOH A O   1 
HETATM 5078 O O   . HOH G 6 .   ? -19.458 -24.064 5.628   1.00 36.46  ? 601 HOH A O   1 
HETATM 5079 O O   . HOH G 6 .   ? -10.772 -2.374  -6.169  1.00 36.77  ? 602 HOH A O   1 
HETATM 5080 O O   . HOH G 6 .   ? -4.374  -21.530 -19.804 1.00 43.91  ? 603 HOH A O   1 
HETATM 5081 O O   . HOH G 6 .   ? -20.273 21.417  -6.887  1.00 41.67  ? 604 HOH A O   1 
HETATM 5082 O O   . HOH G 6 .   ? -31.626 -11.125 -19.995 1.00 33.60  ? 605 HOH A O   1 
HETATM 5083 O O   . HOH G 6 .   ? -11.757 1.160   -20.020 1.00 32.03  ? 606 HOH A O   1 
HETATM 5084 O O   . HOH G 6 .   ? -12.146 17.158  -11.368 1.00 39.19  ? 607 HOH A O   1 
HETATM 5085 O O   . HOH G 6 .   ? -16.437 -15.835 -35.156 1.00 37.94  ? 608 HOH A O   1 
HETATM 5086 O O   . HOH G 6 .   ? -3.523  20.786  -33.649 1.00 46.56  ? 609 HOH A O   1 
HETATM 5087 O O   . HOH G 6 .   ? -37.674 -2.254  -23.888 1.00 58.98  ? 610 HOH A O   1 
HETATM 5088 O O   . HOH G 6 .   ? -28.914 -21.993 -11.071 1.00 37.41  ? 611 HOH A O   1 
HETATM 5089 O O   . HOH G 6 .   ? -21.654 10.761  -5.000  1.00 32.45  ? 612 HOH A O   1 
HETATM 5090 O O   . HOH G 6 .   ? -1.727  13.780  -32.807 1.00 42.94  ? 613 HOH A O   1 
HETATM 5091 O O   . HOH G 6 .   ? -6.851  7.327   -35.343 1.00 38.21  ? 614 HOH A O   1 
HETATM 5092 O O   . HOH G 6 .   ? -9.245  8.242   -13.274 1.00 33.37  ? 615 HOH A O   1 
HETATM 5093 O O   . HOH G 6 .   ? -27.996 12.166  -31.732 1.00 47.58  ? 616 HOH A O   1 
HETATM 5094 O O   . HOH G 6 .   ? -26.451 13.310  -33.607 1.00 44.68  ? 617 HOH A O   1 
HETATM 5095 O O   . HOH G 6 .   ? -33.087 -1.242  -4.034  1.00 38.71  ? 618 HOH A O   1 
HETATM 5096 O O   . HOH G 6 .   ? -26.093 25.884  -21.796 1.00 47.44  ? 619 HOH A O   1 
HETATM 5097 O O   . HOH G 6 .   ? -15.546 -21.810 -10.666 1.00 27.54  ? 620 HOH A O   1 
HETATM 5098 O O   . HOH G 6 .   ? -20.199 3.743   -2.129  1.00 35.68  ? 621 HOH A O   1 
HETATM 5099 O O   . HOH G 6 .   ? -20.665 -1.946  -2.291  1.00 33.29  ? 622 HOH A O   1 
HETATM 5100 O O   . HOH G 6 .   ? -4.557  -13.048 -30.828 1.00 36.76  ? 623 HOH A O   1 
HETATM 5101 O O   . HOH G 6 .   ? 3.365   -10.514 -27.200 1.00 33.40  ? 624 HOH A O   1 
HETATM 5102 O O   . HOH G 6 .   ? -3.271  -23.490 -16.842 1.00 39.70  ? 625 HOH A O   1 
HETATM 5103 O O   . HOH G 6 .   ? -20.988 -20.138 0.139   1.00 30.30  ? 626 HOH A O   1 
HETATM 5104 O O   . HOH G 6 .   ? 1.777   14.110  -22.503 1.00 37.68  ? 627 HOH A O   1 
HETATM 5105 O O   . HOH G 6 .   ? -21.876 -17.790 -1.137  1.00 32.17  ? 628 HOH A O   1 
HETATM 5106 O O   . HOH G 6 .   ? -6.452  4.583   -34.518 1.00 32.82  ? 629 HOH A O   1 
HETATM 5107 O O   . HOH G 6 .   ? -26.053 -18.464 -21.923 1.00 36.32  ? 630 HOH A O   1 
HETATM 5108 O O   . HOH G 6 .   ? -38.435 4.779   -17.857 1.00 37.98  ? 631 HOH A O   1 
HETATM 5109 O O   . HOH G 6 .   ? -36.641 -5.792  -11.126 1.00 37.84  ? 632 HOH A O   1 
HETATM 5110 O O   . HOH G 6 .   ? -23.773 -12.670 -16.111 1.00 27.59  ? 633 HOH A O   1 
HETATM 5111 O O   . HOH G 6 .   ? -20.887 -21.100 -19.712 1.00 35.31  ? 634 HOH A O   1 
HETATM 5112 O O   . HOH G 6 .   ? -15.661 -2.005  -26.389 1.00 32.50  ? 635 HOH A O   1 
HETATM 5113 O O   . HOH G 6 .   ? -29.262 15.458  -19.051 1.00 33.27  ? 636 HOH A O   1 
HETATM 5114 O O   . HOH G 6 .   ? -29.447 0.000   0.000   0.50 44.82  ? 637 HOH A O   1 
HETATM 5115 O O   . HOH G 6 .   ? -11.417 14.875  -30.593 1.00 33.59  ? 638 HOH A O   1 
HETATM 5116 O O   . HOH G 6 .   ? -32.810 0.677   -10.031 1.00 31.95  ? 639 HOH A O   1 
HETATM 5117 O O   . HOH G 6 .   ? -12.210 22.510  -23.103 1.00 37.91  ? 640 HOH A O   1 
HETATM 5118 O O   . HOH G 6 .   ? -6.810  16.744  -16.454 1.00 38.37  ? 641 HOH A O   1 
HETATM 5119 O O   . HOH G 6 .   ? -7.232  -22.320 -12.822 1.00 28.31  ? 642 HOH A O   1 
HETATM 5120 O O   . HOH G 6 .   ? -16.517 2.906   -16.372 1.00 38.27  ? 643 HOH A O   1 
HETATM 5121 O O   . HOH G 6 .   ? -33.543 17.709  -15.049 1.00 37.18  ? 644 HOH A O   1 
HETATM 5122 O O   . HOH G 6 .   ? 2.319   -17.787 -17.401 1.00 53.27  ? 645 HOH A O   1 
HETATM 5123 O O   . HOH G 6 .   ? -16.685 -19.547 -21.387 1.00 30.10  ? 646 HOH A O   1 
HETATM 5124 O O   . HOH G 6 .   ? -23.790 -18.316 -20.967 1.00 31.62  ? 647 HOH A O   1 
HETATM 5125 O O   . HOH G 6 .   ? -35.466 6.455   -8.725  1.00 36.49  ? 648 HOH A O   1 
HETATM 5126 O O   . HOH G 6 .   ? -26.661 -1.066  -1.702  1.00 36.53  ? 649 HOH A O   1 
HETATM 5127 O O   . HOH G 6 .   ? -14.572 8.359   -7.569  1.00 39.02  ? 650 HOH A O   1 
HETATM 5128 O O   . HOH G 6 .   ? -18.678 13.156  -36.613 1.00 43.60  ? 651 HOH A O   1 
HETATM 5129 O O   . HOH G 6 .   ? -36.827 9.235   -15.777 1.00 41.09  ? 652 HOH A O   1 
HETATM 5130 O O   . HOH G 6 .   ? -10.536 -22.483 10.192  1.00 40.99  ? 653 HOH A O   1 
HETATM 5131 O O   . HOH G 6 .   ? -10.421 -26.265 -10.413 1.00 39.43  ? 654 HOH A O   1 
HETATM 5132 O O   . HOH G 6 .   ? -16.039 3.060   -21.978 1.00 25.38  ? 655 HOH A O   1 
HETATM 5133 O O   . HOH G 6 .   ? -19.924 -14.231 -36.033 1.00 37.94  ? 656 HOH A O   1 
HETATM 5134 O O   . HOH G 6 .   ? -27.283 20.162  -11.574 1.00 36.84  ? 657 HOH A O   1 
HETATM 5135 O O   . HOH G 6 .   ? -18.255 -26.937 -2.244  1.00 35.21  ? 658 HOH A O   1 
HETATM 5136 O O   . HOH G 6 .   ? -13.071 23.855  -21.045 1.00 41.58  ? 659 HOH A O   1 
HETATM 5137 O O   . HOH G 6 .   ? -4.121  -24.996 -8.565  1.00 32.90  ? 660 HOH A O   1 
HETATM 5138 O O   . HOH G 6 .   ? -3.679  -27.854 -9.576  1.00 43.49  ? 661 HOH A O   1 
HETATM 5139 O O   . HOH G 6 .   ? -11.704 -29.098 10.251  1.00 41.18  ? 662 HOH A O   1 
HETATM 5140 O O   . HOH G 6 .   ? -30.999 19.240  -17.916 1.00 36.92  ? 663 HOH A O   1 
HETATM 5141 O O   . HOH G 6 .   ? -20.894 -4.251  -39.019 1.00 35.33  ? 664 HOH A O   1 
HETATM 5142 O O   . HOH G 6 .   ? -23.112 -24.483 -14.866 1.00 35.53  ? 665 HOH A O   1 
HETATM 5143 O O   . HOH G 6 .   ? -3.970  -10.519 -31.883 1.00 36.08  ? 666 HOH A O   1 
HETATM 5144 O O   . HOH G 6 .   ? -26.911 15.322  -20.671 1.00 31.71  ? 667 HOH A O   1 
HETATM 5145 O O   . HOH G 6 .   ? -1.702  -4.046  -37.918 1.00 40.24  ? 668 HOH A O   1 
HETATM 5146 O O   . HOH G 6 .   ? -36.931 -4.279  -16.049 1.00 39.47  ? 669 HOH A O   1 
HETATM 5147 O O   . HOH G 6 .   ? -7.611  -9.341  -4.973  1.00 35.54  ? 670 HOH A O   1 
HETATM 5148 O O   . HOH G 6 .   ? -13.568 -1.422  -13.199 1.00 29.78  ? 671 HOH A O   1 
HETATM 5149 O O   . HOH G 6 .   ? -5.627  -26.057 -10.470 1.00 39.94  ? 672 HOH A O   1 
HETATM 5150 O O   . HOH G 6 .   ? -28.942 -16.069 -26.497 1.00 39.91  ? 673 HOH A O   1 
HETATM 5151 O O   . HOH G 6 .   ? -15.466 -0.033  -12.258 1.00 33.63  ? 674 HOH A O   1 
HETATM 5152 O O   . HOH G 6 .   ? -8.815  3.375   -15.342 1.00 35.58  ? 675 HOH A O   1 
HETATM 5153 O O   . HOH G 6 .   ? -34.787 -0.651  -6.385  1.00 35.33  ? 676 HOH A O   1 
HETATM 5154 O O   . HOH G 6 .   ? -17.160 13.872  -34.696 1.00 35.67  ? 677 HOH A O   1 
HETATM 5155 O O   . HOH G 6 .   ? 1.167   -8.130  -15.671 1.00 42.84  ? 678 HOH A O   1 
HETATM 5156 O O   . HOH G 6 .   ? -15.833 4.196   -13.330 1.00 25.47  ? 679 HOH A O   1 
HETATM 5157 O O   . HOH G 6 .   ? -9.834  -16.761 -31.501 1.00 39.37  ? 680 HOH A O   1 
HETATM 5158 O O   . HOH G 6 .   ? -24.385 2.157   -36.964 1.00 43.95  ? 681 HOH A O   1 
HETATM 5159 O O   . HOH G 6 .   ? -40.375 5.389   -16.244 1.00 41.67  ? 682 HOH A O   1 
HETATM 5160 O O   . HOH G 6 .   ? -27.876 -23.240 -13.198 1.00 37.53  ? 683 HOH A O   1 
HETATM 5161 O O   . HOH G 6 .   ? -8.363  -15.097 -29.287 1.00 32.92  ? 684 HOH A O   1 
HETATM 5162 O O   . HOH G 6 .   ? -21.330 -11.662 -35.771 1.00 39.67  ? 685 HOH A O   1 
HETATM 5163 O O   . HOH G 6 .   ? -34.265 -10.450 -17.770 1.00 37.99  ? 686 HOH A O   1 
HETATM 5164 O O   . HOH G 6 .   ? -15.333 15.275  -37.268 1.00 51.32  ? 687 HOH A O   1 
HETATM 5165 O O   . HOH G 6 .   ? -1.199  -9.986  -33.152 1.00 36.63  ? 688 HOH A O   1 
HETATM 5166 O O   . HOH G 6 .   ? 0.242   8.372   -32.588 1.00 40.03  ? 689 HOH A O   1 
HETATM 5167 O O   . HOH G 6 .   ? -13.412 -22.555 -9.589  1.00 33.69  ? 690 HOH A O   1 
HETATM 5168 O O   . HOH G 6 .   ? -4.582  5.605   -13.319 1.00 33.61  ? 691 HOH A O   1 
HETATM 5169 O O   . HOH G 6 .   ? -10.784 4.437   -17.070 1.00 31.87  ? 692 HOH A O   1 
HETATM 5170 O O   . HOH G 6 .   ? -20.200 -26.693 -0.806  1.00 34.25  ? 693 HOH A O   1 
HETATM 5171 O O   . HOH G 6 .   ? -24.575 -8.103  -2.516  1.00 26.08  ? 694 HOH A O   1 
HETATM 5172 O O   . HOH G 6 .   ? -23.508 10.481  -1.389  1.00 29.51  ? 695 HOH A O   1 
HETATM 5173 O O   . HOH G 6 .   ? -29.211 3.759   1.836   1.00 38.33  ? 696 HOH A O   1 
HETATM 5174 O O   . HOH G 6 .   ? -6.227  1.659   -36.668 1.00 25.63  ? 697 HOH A O   1 
HETATM 5175 O O   . HOH G 6 .   ? -19.785 1.263   -22.327 1.00 19.55  ? 698 HOH A O   1 
HETATM 5176 O O   . HOH G 6 .   ? -10.072 0.736   -15.516 1.00 29.97  ? 699 HOH A O   1 
HETATM 5177 O O   . HOH G 6 .   ? -29.051 -16.569 -36.565 1.00 64.18  ? 700 HOH A O   1 
HETATM 5178 O O   . HOH G 6 .   ? -13.629 1.446   -22.246 1.00 28.71  ? 701 HOH A O   1 
HETATM 5179 O O   . HOH G 6 .   ? -39.530 2.962   -19.688 1.00 51.87  ? 702 HOH A O   1 
HETATM 5180 O O   . HOH G 6 .   ? -13.147 3.254   -18.605 1.00 35.47  ? 703 HOH A O   1 
HETATM 5181 O O   . HOH G 6 .   ? -20.887 1.356   -0.802  1.00 35.63  ? 704 HOH A O   1 
HETATM 5182 O O   . HOH G 6 .   ? -36.093 6.643   -32.396 1.00 63.21  ? 705 HOH A O   1 
HETATM 5183 O O   . HOH G 6 .   ? -17.418 1.371   -23.697 1.00 22.86  ? 706 HOH A O   1 
HETATM 5184 O O   . HOH G 6 .   ? -15.723 -23.577 -12.564 1.00 40.11  ? 707 HOH A O   1 
HETATM 5185 O O   . HOH G 6 .   ? -17.171 -2.388  -18.258 1.00 32.11  ? 708 HOH A O   1 
HETATM 5186 O O   . HOH G 6 .   ? -15.174 -25.050 11.612  1.00 41.05  ? 709 HOH A O   1 
HETATM 5187 O O   . HOH G 6 .   ? -28.163 22.138  -22.185 1.00 43.29  ? 710 HOH A O   1 
HETATM 5188 O O   . HOH G 6 .   ? -21.741 -8.854  -36.472 1.00 46.76  ? 711 HOH A O   1 
HETATM 5189 O O   . HOH G 6 .   ? -23.041 -19.479 -2.627  1.00 35.54  ? 712 HOH A O   1 
HETATM 5190 O O   . HOH G 6 .   ? -8.924  -12.679 -1.811  1.00 43.61  ? 713 HOH A O   1 
HETATM 5191 O O   . HOH G 6 .   ? -16.892 2.342   -19.227 1.00 33.22  ? 714 HOH A O   1 
HETATM 5192 O O   . HOH G 6 .   ? -5.057  -3.328  -38.763 1.00 47.84  ? 715 HOH A O   1 
HETATM 5193 O O   . HOH G 6 .   ? -12.377 16.636  -34.289 1.00 47.08  ? 716 HOH A O   1 
HETATM 5194 O O   . HOH G 6 .   ? -6.483  4.253   -37.897 1.00 23.67  ? 717 HOH A O   1 
HETATM 5195 O O   . HOH G 6 .   ? -35.708 3.897   -7.305  1.00 38.91  ? 718 HOH A O   1 
HETATM 5196 O O   . HOH G 6 .   ? -15.792 -0.806  -23.863 1.00 27.92  ? 719 HOH A O   1 
HETATM 5197 O O   . HOH G 6 .   ? 6.377   -4.323  -28.744 1.00 51.16  ? 720 HOH A O   1 
HETATM 5198 O O   . HOH G 6 .   ? -24.444 0.000   0.000   0.50 37.03  ? 721 HOH A O   1 
HETATM 5199 O O   . HOH G 6 .   ? -5.567  -0.546  -39.091 1.00 47.17  ? 722 HOH A O   1 
HETATM 5200 O O   . HOH G 6 .   ? -35.285 -10.290 -7.686  1.00 47.67  ? 723 HOH A O   1 
HETATM 5201 O O   . HOH G 6 .   ? -15.028 6.053   -6.523  1.00 44.44  ? 724 HOH A O   1 
HETATM 5202 O O   . HOH G 6 .   ? -31.546 -12.975 -6.394  1.00 41.47  ? 725 HOH A O   1 
HETATM 5203 O O   . HOH G 6 .   ? 6.624   -4.269  -20.643 1.00 39.96  ? 726 HOH A O   1 
HETATM 5204 O O   . HOH G 6 .   ? -23.612 -16.796 0.535   1.00 37.45  ? 727 HOH A O   1 
HETATM 5205 O O   . HOH G 6 .   ? -26.393 7.795   0.736   1.00 30.64  ? 728 HOH A O   1 
HETATM 5206 O O   . HOH G 6 .   ? -6.862  -13.691 -2.945  1.00 37.19  ? 729 HOH A O   1 
HETATM 5207 O O   . HOH G 6 .   ? -11.836 -22.319 -13.014 1.00 36.16  ? 730 HOH A O   1 
HETATM 5208 O O   . HOH G 6 .   ? -26.214 12.276  -5.244  1.00 48.40  ? 731 HOH A O   1 
HETATM 5209 O O   . HOH G 6 .   ? -14.551 4.964   -15.780 1.00 36.46  ? 732 HOH A O   1 
HETATM 5210 O O   . HOH G 6 .   ? -28.886 15.296  -30.550 1.00 46.25  ? 733 HOH A O   1 
HETATM 5211 O O   . HOH G 6 .   ? -20.190 -21.036 -23.062 1.00 43.90  ? 734 HOH A O   1 
HETATM 5212 O O   . HOH G 6 .   ? -3.811  -12.788 -1.790  1.00 45.81  ? 735 HOH A O   1 
HETATM 5213 O O   . HOH G 6 .   ? -11.154 -28.019 -12.167 1.00 43.63  ? 736 HOH A O   1 
HETATM 5214 O O   . HOH G 6 .   ? -14.786 14.748  -2.877  1.00 42.13  ? 737 HOH A O   1 
HETATM 5215 O O   . HOH G 6 .   ? -36.852 -3.717  -13.248 1.00 38.71  ? 738 HOH A O   1 
HETATM 5216 O O   . HOH G 6 .   ? -20.382 12.542  -2.276  1.00 40.00  ? 739 HOH A O   1 
HETATM 5217 O O   . HOH G 6 .   ? -37.413 -7.909  -8.958  1.00 41.78  ? 740 HOH A O   1 
HETATM 5218 O O   . HOH G 6 .   ? -34.953 9.355   -21.950 1.00 48.56  ? 741 HOH A O   1 
HETATM 5219 O O   . HOH G 6 .   ? -35.640 13.809  -18.065 1.00 43.13  ? 742 HOH A O   1 
HETATM 5220 O O   . HOH G 6 .   ? -5.909  9.761   -11.336 1.00 44.04  ? 743 HOH A O   1 
HETATM 5221 O O   . HOH G 6 .   ? -15.174 -0.032  -19.040 1.00 36.79  ? 744 HOH A O   1 
HETATM 5222 O O   . HOH G 6 .   ? -32.252 9.489   -0.816  1.00 37.53  ? 745 HOH A O   1 
HETATM 5223 O O   . HOH G 6 .   ? -24.953 -14.267 0.651   1.00 30.99  ? 746 HOH A O   1 
HETATM 5224 O O   . HOH G 6 .   ? -31.585 0.000   0.000   0.50 36.54  ? 747 HOH A O   1 
HETATM 5225 O O   . HOH G 6 .   ? -37.183 8.062   -7.615  1.00 46.09  ? 748 HOH A O   1 
HETATM 5226 O O   . HOH G 6 .   ? -26.189 -11.258 -2.360  1.00 23.91  ? 749 HOH A O   1 
HETATM 5227 O O   . HOH G 6 .   ? -24.043 12.232  -3.399  1.00 39.20  ? 750 HOH A O   1 
HETATM 5228 O O   . HOH G 6 .   ? -17.878 16.647  -36.546 1.00 54.45  ? 751 HOH A O   1 
HETATM 5229 O O   . HOH G 6 .   ? -22.667 -14.312 2.826   1.00 40.49  ? 752 HOH A O   1 
HETATM 5230 O O   . HOH G 6 .   ? -27.623 -13.784 -2.718  1.00 35.78  ? 753 HOH A O   1 
HETATM 5231 O O   . HOH G 6 .   ? -9.943  -10.321 -1.055  1.00 44.95  ? 754 HOH A O   1 
HETATM 5232 O O   . HOH G 6 .   ? -31.945 -4.211  -2.055  1.00 37.49  ? 755 HOH A O   1 
HETATM 5233 O O   . HOH G 6 .   ? -8.272  -25.173 -12.242 1.00 34.06  ? 756 HOH A O   1 
HETATM 5234 O O   . HOH G 6 .   ? -34.284 -12.735 -10.011 1.00 47.72  ? 757 HOH A O   1 
HETATM 5235 O O   . HOH G 6 .   ? -27.897 -9.868  -0.969  1.00 29.92  ? 758 HOH A O   1 
HETATM 5236 O O   . HOH G 6 .   ? -1.929  -12.825 -31.508 1.00 46.35  ? 759 HOH A O   1 
HETATM 5237 O O   . HOH G 6 .   ? -12.432 -24.735 -10.269 1.00 36.96  ? 760 HOH A O   1 
HETATM 5238 O O   . HOH G 6 .   ? -15.572 -19.056 -31.478 1.00 40.42  ? 761 HOH A O   1 
HETATM 5239 O O   . HOH G 6 .   ? -30.569 -9.900  -1.620  1.00 41.65  ? 762 HOH A O   1 
HETATM 5240 O O   . HOH G 6 .   ? -12.510 10.424  -0.537  1.00 41.07  ? 763 HOH A O   1 
HETATM 5241 O O   . HOH G 6 .   ? 12.105  4.848   -19.770 1.00 51.13  ? 764 HOH A O   1 
HETATM 5242 O O   . HOH G 6 .   ? -34.449 0.000   0.000   0.50 43.92  ? 765 HOH A O   1 
HETATM 5243 O O   . HOH G 6 .   ? 0.338   2.686   -36.750 1.00 49.25  ? 766 HOH A O   1 
HETATM 5244 O O   . HOH H 6 .   ? 18.031  -38.686 9.066   1.00 51.65  ? 301 HOH B O   1 
HETATM 5245 O O   . HOH H 6 .   ? 37.477  -22.852 12.050  1.00 52.24  ? 302 HOH B O   1 
HETATM 5246 O O   . HOH H 6 .   ? 18.738  -16.669 -16.601 1.00 68.87  ? 303 HOH B O   1 
HETATM 5247 O O   . HOH H 6 .   ? 24.904  -24.809 -14.691 1.00 57.15  ? 304 HOH B O   1 
HETATM 5248 O O   . HOH H 6 .   ? 19.721  -26.953 -10.509 1.00 49.47  ? 305 HOH B O   1 
HETATM 5249 O O   . HOH H 6 .   ? 31.325  -34.707 5.059   1.00 36.19  ? 306 HOH B O   1 
HETATM 5250 O O   . HOH H 6 .   ? 21.269  -32.179 -8.111  1.00 49.43  ? 307 HOH B O   1 
HETATM 5251 O O   . HOH H 6 .   ? 11.669  -22.030 -2.742  1.00 33.25  ? 308 HOH B O   1 
HETATM 5252 O O   . HOH H 6 .   ? 35.121  -31.365 -4.628  1.00 42.47  ? 309 HOH B O   1 
HETATM 5253 O O   . HOH H 6 .   ? 21.110  -32.258 14.727  1.00 41.34  ? 310 HOH B O   1 
HETATM 5254 O O   . HOH H 6 .   ? 21.559  -32.175 -3.091  1.00 37.50  ? 311 HOH B O   1 
HETATM 5255 O O   . HOH H 6 .   ? 37.623  -19.598 10.083  1.00 50.73  ? 312 HOH B O   1 
HETATM 5256 O O   . HOH H 6 .   ? 36.817  -19.221 6.599   1.00 47.20  ? 313 HOH B O   1 
HETATM 5257 O O   . HOH H 6 .   ? 26.622  -26.284 14.528  1.00 40.97  ? 314 HOH B O   1 
HETATM 5258 O O   . HOH H 6 .   ? 2.788   -40.936 1.350   1.00 66.38  ? 315 HOH B O   1 
HETATM 5259 O O   . HOH H 6 .   ? 14.780  -35.287 1.933   1.00 43.24  ? 316 HOH B O   1 
HETATM 5260 O O   . HOH H 6 .   ? 19.171  -13.808 -6.445  1.00 55.45  ? 317 HOH B O   1 
HETATM 5261 O O   . HOH H 6 .   ? 15.195  -30.547 -4.256  1.00 31.03  ? 318 HOH B O   1 
HETATM 5262 O O   . HOH H 6 .   ? 16.851  -30.979 6.366   1.00 30.92  ? 319 HOH B O   1 
HETATM 5263 O O   . HOH H 6 .   ? 24.917  -33.462 7.311   1.00 31.26  ? 320 HOH B O   1 
HETATM 5264 O O   . HOH H 6 .   ? 15.345  -32.495 -0.585  1.00 30.28  ? 321 HOH B O   1 
HETATM 5265 O O   . HOH H 6 .   ? 32.502  -27.687 0.568   1.00 33.19  ? 322 HOH B O   1 
HETATM 5266 O O   . HOH H 6 .   ? 14.135  -17.248 1.798   1.00 39.42  ? 323 HOH B O   1 
HETATM 5267 O O   . HOH H 6 .   ? 28.750  -31.105 13.453  1.00 39.95  ? 324 HOH B O   1 
HETATM 5268 O O   . HOH H 6 .   ? 16.877  -37.366 2.859   1.00 41.47  ? 325 HOH B O   1 
HETATM 5269 O O   . HOH H 6 .   ? 23.271  -33.374 -0.837  1.00 34.81  ? 326 HOH B O   1 
HETATM 5270 O O   . HOH H 6 .   ? 25.589  -36.050 10.438  1.00 40.88  ? 327 HOH B O   1 
HETATM 5271 O O   . HOH H 6 .   ? 17.676  -31.079 -5.848  1.00 35.27  ? 328 HOH B O   1 
HETATM 5272 O O   . HOH H 6 .   ? 11.900  -35.606 2.143   1.00 39.27  ? 329 HOH B O   1 
HETATM 5273 O O   . HOH H 6 .   ? 5.614   -39.067 7.897   1.00 53.26  ? 330 HOH B O   1 
HETATM 5274 O O   . HOH H 6 .   ? 37.298  -38.020 14.581  1.00 40.41  ? 331 HOH B O   1 
HETATM 5275 O O   . HOH H 6 .   ? 27.543  -14.496 0.664   1.00 47.48  ? 332 HOH B O   1 
HETATM 5276 O O   . HOH H 6 .   ? 21.789  -27.469 11.545  1.00 34.78  ? 333 HOH B O   1 
HETATM 5277 O O   . HOH H 6 .   ? 14.464  -21.243 -2.429  1.00 36.61  ? 334 HOH B O   1 
HETATM 5278 O O   . HOH H 6 .   ? 20.245  -30.586 -6.397  1.00 37.82  ? 335 HOH B O   1 
HETATM 5279 O O   . HOH H 6 .   ? 36.667  -30.355 3.980   1.00 31.42  ? 336 HOH B O   1 
HETATM 5280 O O   . HOH H 6 .   ? 18.721  -39.721 6.476   1.00 42.77  ? 337 HOH B O   1 
HETATM 5281 O O   . HOH H 6 .   ? 20.993  -38.402 3.964   1.00 39.08  ? 338 HOH B O   1 
HETATM 5282 O O   . HOH H 6 .   ? 19.903  -34.156 -2.997  1.00 38.76  ? 339 HOH B O   1 
HETATM 5283 O O   . HOH H 6 .   ? 13.224  -26.429 -10.803 1.00 48.91  ? 340 HOH B O   1 
HETATM 5284 O O   . HOH H 6 .   ? 39.025  -22.242 -0.301  1.00 49.85  ? 341 HOH B O   1 
HETATM 5285 O O   . HOH H 6 .   ? 11.835  -29.058 -4.648  1.00 38.72  ? 342 HOH B O   1 
HETATM 5286 O O   . HOH H 6 .   ? 30.377  -30.184 -11.626 1.00 56.59  ? 343 HOH B O   1 
HETATM 5287 O O   . HOH H 6 .   ? 32.849  -28.862 -7.520  1.00 45.03  ? 344 HOH B O   1 
HETATM 5288 O O   . HOH H 6 .   ? 39.303  -32.245 4.796   1.00 42.97  ? 345 HOH B O   1 
HETATM 5289 O O   . HOH H 6 .   ? 14.576  -18.530 -1.565  1.00 35.09  ? 346 HOH B O   1 
HETATM 5290 O O   . HOH H 6 .   ? 18.988  -36.374 10.618  1.00 46.73  ? 347 HOH B O   1 
HETATM 5291 O O   . HOH H 6 .   ? 18.695  -32.961 13.862  1.00 47.97  ? 348 HOH B O   1 
HETATM 5292 O O   . HOH H 6 .   ? 35.054  -28.522 0.863   1.00 38.97  ? 349 HOH B O   1 
HETATM 5293 O O   . HOH H 6 .   ? 22.682  -26.139 13.478  1.00 34.82  ? 350 HOH B O   1 
HETATM 5294 O O   . HOH H 6 .   ? 21.940  -35.550 -0.397  1.00 42.70  ? 351 HOH B O   1 
HETATM 5295 O O   . HOH H 6 .   ? 40.194  -31.922 7.241   1.00 39.00  ? 352 HOH B O   1 
HETATM 5296 O O   . HOH H 6 .   ? 17.585  -34.681 -0.393  1.00 41.94  ? 353 HOH B O   1 
HETATM 5297 O O   . HOH H 6 .   ? 31.455  -29.986 -8.991  1.00 46.98  ? 354 HOH B O   1 
HETATM 5298 O O   . HOH I 6 .   ? 15.755  -11.661 11.728  1.00 36.42  ? 201 HOH C O   1 
HETATM 5299 O O   . HOH I 6 .   ? 12.195  -18.265 0.320   1.00 35.91  ? 202 HOH C O   1 
HETATM 5300 O O   . HOH I 6 .   ? 1.433   -37.441 -7.133  1.00 55.63  ? 203 HOH C O   1 
HETATM 5301 O O   . HOH I 6 .   ? 15.800  -9.416  11.697  1.00 39.22  ? 204 HOH C O   1 
HETATM 5302 O O   . HOH I 6 .   ? -0.558  -14.929 -0.563  1.00 34.52  ? 205 HOH C O   1 
HETATM 5303 O O   . HOH I 6 .   ? 14.196  -29.153 7.865   1.00 34.05  ? 206 HOH C O   1 
HETATM 5304 O O   . HOH I 6 .   ? 12.635  -12.349 19.086  1.00 50.51  ? 207 HOH C O   1 
HETATM 5305 O O   . HOH I 6 .   ? -1.416  -23.792 -8.445  1.00 28.34  ? 208 HOH C O   1 
HETATM 5306 O O   . HOH I 6 .   ? 13.728  -28.333 15.855  1.00 43.09  ? 209 HOH C O   1 
HETATM 5307 O O   . HOH I 6 .   ? 11.915  -7.532  23.961  1.00 51.09  ? 210 HOH C O   1 
HETATM 5308 O O   . HOH I 6 .   ? 4.506   -11.555 -0.479  1.00 37.05  ? 211 HOH C O   1 
HETATM 5309 O O   . HOH I 6 .   ? -1.086  -24.385 -15.186 1.00 47.77  ? 212 HOH C O   1 
HETATM 5310 O O   . HOH I 6 .   ? -5.034  -33.986 -0.004  1.00 33.21  ? 213 HOH C O   1 
HETATM 5311 O O   . HOH I 6 .   ? 8.724   -8.792  10.368  1.00 37.26  ? 214 HOH C O   1 
HETATM 5312 O O   . HOH I 6 .   ? -1.090  -28.059 -9.584  1.00 41.77  ? 215 HOH C O   1 
HETATM 5313 O O   . HOH I 6 .   ? 1.033   -6.049  17.060  1.00 42.87  ? 216 HOH C O   1 
HETATM 5314 O O   . HOH I 6 .   ? 15.819  -7.864  10.207  1.00 46.27  ? 217 HOH C O   1 
HETATM 5315 O O   . HOH I 6 .   ? 7.642   -8.611  -0.577  1.00 44.03  ? 218 HOH C O   1 
HETATM 5316 O O   . HOH I 6 .   ? -7.563  -23.955 8.062   1.00 31.25  ? 219 HOH C O   1 
HETATM 5317 O O   . HOH I 6 .   ? -3.776  -33.557 2.009   1.00 37.02  ? 220 HOH C O   1 
HETATM 5318 O O   . HOH I 6 .   ? 0.610   -8.612  15.480  1.00 39.12  ? 221 HOH C O   1 
HETATM 5319 O O   . HOH I 6 .   ? 14.385  -30.896 15.923  1.00 49.77  ? 222 HOH C O   1 
HETATM 5320 O O   . HOH I 6 .   ? 0.181   -19.159 -9.183  1.00 32.87  ? 223 HOH C O   1 
HETATM 5321 O O   . HOH I 6 .   ? 4.390   -34.615 11.704  1.00 43.38  ? 224 HOH C O   1 
HETATM 5322 O O   . HOH I 6 .   ? 15.121  -24.611 18.066  1.00 54.22  ? 225 HOH C O   1 
HETATM 5323 O O   . HOH I 6 .   ? 5.851   -31.745 -0.292  1.00 41.88  ? 226 HOH C O   1 
HETATM 5324 O O   . HOH I 6 .   ? -5.082  -16.189 2.105   1.00 35.12  ? 227 HOH C O   1 
HETATM 5325 O O   . HOH I 6 .   ? 14.221  -10.473 4.369   1.00 44.49  ? 228 HOH C O   1 
HETATM 5326 O O   . HOH I 6 .   ? 12.958  -9.903  18.417  1.00 48.18  ? 229 HOH C O   1 
HETATM 5327 O O   . HOH I 6 .   ? 6.367   -31.314 -3.347  1.00 47.81  ? 230 HOH C O   1 
HETATM 5328 O O   . HOH I 6 .   ? -3.579  -13.500 1.025   1.00 38.67  ? 231 HOH C O   1 
HETATM 5329 O O   . HOH I 6 .   ? 6.326   -9.844  -2.766  1.00 44.33  ? 232 HOH C O   1 
HETATM 5330 O O   . HOH I 6 .   ? 18.294  -16.482 12.358  1.00 39.61  ? 233 HOH C O   1 
HETATM 5331 O O   . HOH I 6 .   ? 17.060  -18.366 13.153  1.00 46.43  ? 234 HOH C O   1 
HETATM 5332 O O   . HOH I 6 .   ? 14.547  -6.736  11.807  1.00 43.17  ? 235 HOH C O   1 
HETATM 5333 O O   . HOH I 6 .   ? 14.024  -5.441  21.099  1.00 48.77  ? 236 HOH C O   1 
HETATM 5334 O O   . HOH J 6 .   ? -27.248 2.299   -37.547 1.00 57.56  ? 101 HOH D O   1 
HETATM 5335 O O   . HOH J 6 .   ? -24.308 -0.530  -37.566 1.00 45.66  ? 102 HOH D O   1 
HETATM 5336 O O   . HOH J 6 .   ? -22.989 6.505   -41.760 1.00 46.63  ? 103 HOH D O   1 
HETATM 5337 O O   . HOH J 6 .   ? -24.091 -6.938  -32.985 1.00 36.76  ? 104 HOH D O   1 
HETATM 5338 O O   . HOH J 6 .   ? -25.629 -7.034  -35.476 1.00 44.20  ? 105 HOH D O   1 
HETATM 5339 O O   . HOH J 6 .   ? -27.270 0.269   -39.317 1.00 57.53  ? 106 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
12   N N   . LEU A 3   ? 0.3574 0.4949 0.5079 -0.0084 0.0181  -0.0194 2   LEU A N   
13   C CA  . LEU A 3   ? 0.3301 0.4360 0.4576 -0.0146 0.0170  -0.0176 2   LEU A CA  
14   C C   . LEU A 3   ? 0.3460 0.4235 0.4554 -0.0057 0.0179  -0.0140 2   LEU A C   
15   O O   . LEU A 3   ? 0.3562 0.4294 0.4655 0.0034  0.0242  -0.0148 2   LEU A O   
16   C CB  . LEU A 3   ? 0.3066 0.4042 0.4311 -0.0267 0.0253  -0.0210 2   LEU A CB  
17   C CG  . LEU A 3   ? 0.3553 0.4388 0.4706 -0.0244 0.0372  -0.0208 2   LEU A CG  
18   C CD1 . LEU A 3   ? 0.3468 0.4222 0.4578 -0.0362 0.0442  -0.0209 2   LEU A CD1 
19   C CD2 . LEU A 3   ? 0.3491 0.4533 0.4813 -0.0167 0.0454  -0.0218 2   LEU A CD2 
20   N N   . ARG A 4   ? 0.3113 0.3699 0.4066 -0.0091 0.0117  -0.0108 3   ARG A N   
21   C CA  . ARG A 4   ? 0.3427 0.3765 0.4258 -0.0023 0.0099  -0.0074 3   ARG A CA  
22   C C   . ARG A 4   ? 0.3290 0.3436 0.3984 -0.0116 0.0059  -0.0063 3   ARG A C   
23   O O   . ARG A 4   ? 0.3321 0.3554 0.4024 -0.0187 0.0019  -0.0046 3   ARG A O   
24   C CB  . ARG A 4   ? 0.3168 0.3578 0.4069 0.0085  0.0048  -0.0002 3   ARG A CB  
25   C CG  . ARG A 4   ? 0.2913 0.3039 0.3714 0.0133  0.0032  0.0053  3   ARG A CG  
26   C CD  . ARG A 4   ? 0.2992 0.3193 0.3859 0.0254  -0.0002 0.0153  3   ARG A CD  
27   N NE  . ARG A 4   ? 0.2890 0.3230 0.3867 0.0396  0.0030  0.0149  3   ARG A NE  
28   C CZ  . ARG A 4   ? 0.3482 0.3618 0.4445 0.0512  0.0077  0.0153  3   ARG A CZ  
29   N NH1 . ARG A 4   ? 0.3594 0.3367 0.4442 0.0486  0.0091  0.0147  3   ARG A NH1 
30   N NH2 . ARG A 4   ? 0.3192 0.3495 0.4271 0.0657  0.0111  0.0151  3   ARG A NH2 
31   N N   . TRP A 5   ? 0.3362 0.3264 0.3938 -0.0110 0.0068  -0.0084 4   TRP A N   
32   C CA  . TRP A 5   ? 0.3510 0.3256 0.3997 -0.0186 0.0016  -0.0067 4   TRP A CA  
33   C C   . TRP A 5   ? 0.3356 0.3072 0.3894 -0.0158 -0.0028 0.0020  4   TRP A C   
34   O O   . TRP A 5   ? 0.3420 0.3002 0.3974 -0.0082 -0.0019 0.0042  4   TRP A O   
35   C CB  . TRP A 5   ? 0.3354 0.2877 0.3718 -0.0193 0.0023  -0.0135 4   TRP A CB  
36   C CG  . TRP A 5   ? 0.3956 0.3511 0.4231 -0.0196 0.0079  -0.0199 4   TRP A CG  
37   C CD1 . TRP A 5   ? 0.3986 0.3519 0.4216 -0.0116 0.0148  -0.0254 4   TRP A CD1 
38   C CD2 . TRP A 5   ? 0.3767 0.3372 0.3977 -0.0268 0.0085  -0.0199 4   TRP A CD2 
39   N NE1 . TRP A 5   ? 0.3890 0.3466 0.4025 -0.0140 0.0202  -0.0277 4   TRP A NE1 
40   C CE2 . TRP A 5   ? 0.3746 0.3355 0.3869 -0.0231 0.0163  -0.0240 4   TRP A CE2 
41   C CE3 . TRP A 5   ? 0.3592 0.3237 0.3806 -0.0346 0.0042  -0.0162 4   TRP A CE3 
42   C CZ2 . TRP A 5   ? 0.3668 0.3300 0.3704 -0.0270 0.0200  -0.0228 4   TRP A CZ2 
43   C CZ3 . TRP A 5   ? 0.3511 0.3172 0.3648 -0.0380 0.0072  -0.0164 4   TRP A CZ3 
44   C CH2 . TRP A 5   ? 0.3328 0.2974 0.3375 -0.0343 0.0151  -0.0189 4   TRP A CH2 
45   N N   . THR A 6   ? 0.3180 0.3009 0.3736 -0.0209 -0.0064 0.0075  5   THR A N   
46   C CA  . THR A 6   ? 0.3330 0.3167 0.3919 -0.0168 -0.0090 0.0181  5   THR A CA  
47   C C   . THR A 6   ? 0.3631 0.3326 0.4192 -0.0240 -0.0106 0.0236  5   THR A C   
48   O O   . THR A 6   ? 0.3737 0.3372 0.4324 -0.0204 -0.0104 0.0341  5   THR A O   
49   C CB  . THR A 6   ? 0.3269 0.3378 0.3894 -0.0146 -0.0116 0.0214  5   THR A CB  
50   O OG1 . THR A 6   ? 0.3259 0.3439 0.3849 -0.0242 -0.0127 0.0168  5   THR A OG1 
51   C CG2 . THR A 6   ? 0.3181 0.3476 0.3890 -0.0075 -0.0107 0.0167  5   THR A CG2 
52   N N   . VAL A 7   ? 0.3627 0.3284 0.4146 -0.0335 -0.0118 0.0180  6   VAL A N   
53   C CA  . VAL A 7   ? 0.3360 0.2944 0.3892 -0.0412 -0.0136 0.0226  6   VAL A CA  
54   C C   . VAL A 7   ? 0.3423 0.2874 0.3920 -0.0479 -0.0157 0.0131  6   VAL A C   
55   O O   . VAL A 7   ? 0.3388 0.2881 0.3814 -0.0482 -0.0157 0.0052  6   VAL A O   
56   C CB  . VAL A 7   ? 0.3493 0.3266 0.4019 -0.0444 -0.0144 0.0269  6   VAL A CB  
57   C CG1 . VAL A 7   ? 0.3273 0.3003 0.3836 -0.0527 -0.0154 0.0306  6   VAL A CG1 
58   C CG2 . VAL A 7   ? 0.3096 0.3013 0.3630 -0.0371 -0.0136 0.0358  6   VAL A CG2 
59   N N   . HIS A 8   ? 0.3576 0.2871 0.4124 -0.0534 -0.0175 0.0141  7   HIS A N   
60   C CA  . HIS A 8   ? 0.3705 0.2923 0.4232 -0.0609 -0.0220 0.0043  7   HIS A CA  
61   C C   . HIS A 8   ? 0.3779 0.3004 0.4427 -0.0707 -0.0243 0.0102  7   HIS A C   
62   O O   . HIS A 8   ? 0.3999 0.3083 0.4749 -0.0737 -0.0226 0.0157  7   HIS A O   
63   C CB  . HIS A 8   ? 0.3659 0.2664 0.4139 -0.0584 -0.0228 -0.0064 7   HIS A CB  
64   C CG  . HIS A 8   ? 0.4023 0.2964 0.4465 -0.0655 -0.0293 -0.0184 7   HIS A CG  
65   N ND1 . HIS A 8   ? 0.4525 0.3616 0.4888 -0.0675 -0.0329 -0.0223 7   HIS A ND1 
66   C CD2 . HIS A 8   ? 0.4291 0.3041 0.4763 -0.0706 -0.0335 -0.0280 7   HIS A CD2 
67   C CE1 . HIS A 8   ? 0.4131 0.3160 0.4467 -0.0726 -0.0400 -0.0334 7   HIS A CE1 
68   N NE2 . HIS A 8   ? 0.4715 0.3539 0.5120 -0.0755 -0.0409 -0.0385 7   HIS A NE2 
69   N N   . LEU A 9   ? 0.3407 0.2792 0.4059 -0.0755 -0.0272 0.0097  8   LEU A N   
70   C CA  . LEU A 9   ? 0.3711 0.3179 0.4503 -0.0840 -0.0281 0.0165  8   LEU A CA  
71   C C   . LEU A 9   ? 0.3953 0.3476 0.4775 -0.0912 -0.0355 0.0070  8   LEU A C   
72   O O   . LEU A 9   ? 0.3623 0.3196 0.4317 -0.0872 -0.0391 -0.0011 8   LEU A O   
73   C CB  . LEU A 9   ? 0.3555 0.3227 0.4345 -0.0806 -0.0238 0.0268  8   LEU A CB  
74   C CG  . LEU A 9   ? 0.3543 0.3215 0.4322 -0.0740 -0.0178 0.0379  8   LEU A CG  
75   C CD1 . LEU A 9   ? 0.3062 0.2948 0.3794 -0.0693 -0.0149 0.0437  8   LEU A CD1 
76   C CD2 . LEU A 9   ? 0.3563 0.3116 0.4475 -0.0790 -0.0144 0.0483  8   LEU A CD2 
77   N N   . GLU A 10  ? 0.3675 0.3202 0.4675 -0.1016 -0.0377 0.0089  9   GLU A N   
78   C CA  . GLU A 10  ? 0.3768 0.3400 0.4838 -0.1091 -0.0465 -0.0003 9   GLU A CA  
79   C C   . GLU A 10  ? 0.3534 0.3412 0.4766 -0.1138 -0.0451 0.0093  9   GLU A C   
80   O O   . GLU A 10  ? 0.3656 0.3601 0.4938 -0.1119 -0.0366 0.0229  9   GLU A O   
81   C CB  . GLU A 10  ? 0.3708 0.3161 0.4888 -0.1194 -0.0522 -0.0109 9   GLU A CB  
82   C CG  . GLU A 10  ? 0.3717 0.3040 0.4713 -0.1148 -0.0590 -0.0279 9   GLU A CG  
83   C CD  . GLU A 10  ? 0.4245 0.3769 0.5150 -0.1130 -0.0685 -0.0371 9   GLU A CD  
84   O OE1 . GLU A 10  ? 0.3505 0.3269 0.4493 -0.1139 -0.0694 -0.0298 9   GLU A OE1 
85   O OE2 . GLU A 10  ? 0.4435 0.3879 0.5173 -0.1090 -0.0746 -0.0513 9   GLU A OE2 
86   N N   . GLY A 11  ? 0.3784 0.3821 0.5093 -0.1187 -0.0536 0.0019  10  GLY A N   
87   C CA  . GLY A 11  ? 0.3373 0.3678 0.4870 -0.1229 -0.0528 0.0096  10  GLY A CA  
88   C C   . GLY A 11  ? 0.3626 0.4118 0.5006 -0.1112 -0.0504 0.0143  10  GLY A C   
89   O O   . GLY A 11  ? 0.3547 0.4262 0.5070 -0.1118 -0.0470 0.0225  10  GLY A O   
90   N N   . GLY A 12  ? 0.2830 0.3234 0.3969 -0.1005 -0.0508 0.0097  11  GLY A N   
91   C CA  . GLY A 12  ? 0.2915 0.3446 0.3946 -0.0899 -0.0487 0.0126  11  GLY A CA  
92   C C   . GLY A 12  ? 0.3596 0.4291 0.4639 -0.0875 -0.0579 0.0070  11  GLY A C   
93   O O   . GLY A 12  ? 0.2929 0.3696 0.4095 -0.0954 -0.0672 0.0002  11  GLY A O   
94   N N   . PRO A 13  ? 0.3301 0.4061 0.4222 -0.0760 -0.0558 0.0096  12  PRO A N   
95   C CA  . PRO A 13  ? 0.2895 0.3801 0.3785 -0.0700 -0.0646 0.0059  12  PRO A CA  
96   C C   . PRO A 13  ? 0.3293 0.4065 0.4012 -0.0695 -0.0723 -0.0043 12  PRO A C   
97   O O   . PRO A 13  ? 0.3430 0.3985 0.3976 -0.0671 -0.0673 -0.0061 12  PRO A O   
98   C CB  . PRO A 13  ? 0.2917 0.3831 0.3683 -0.0564 -0.0576 0.0124  12  PRO A CB  
99   C CG  . PRO A 13  ? 0.2968 0.3675 0.3627 -0.0561 -0.0472 0.0145  12  PRO A CG  
100  C CD  . PRO A 13  ? 0.2906 0.3584 0.3697 -0.0675 -0.0458 0.0150  12  PRO A CD  
101  N N   . ARG A 14  ? 0.3464 0.4390 0.4237 -0.0716 -0.0848 -0.0117 13  ARG A N   
102  C CA  . ARG A 14  ? 0.3287 0.4119 0.3866 -0.0694 -0.0932 -0.0229 13  ARG A CA  
103  C C   . ARG A 14  ? 0.3425 0.4321 0.3786 -0.0531 -0.0944 -0.0189 13  ARG A C   
104  O O   . ARG A 14  ? 0.3370 0.4505 0.3778 -0.0479 -0.1036 -0.0189 13  ARG A O   
105  C CB  . ARG A 14  ? 0.3397 0.4356 0.4139 -0.0807 -0.1072 -0.0354 13  ARG A CB  
106  C CG  . ARG A 14  ? 0.4136 0.5040 0.4649 -0.0764 -0.1179 -0.0495 13  ARG A CG  
107  C CD  . ARG A 14  ? 0.3623 0.4606 0.4312 -0.0904 -0.1320 -0.0658 13  ARG A CD  
108  N NE  . ARG A 14  ? 0.4545 0.5305 0.5395 -0.1048 -0.1260 -0.0685 13  ARG A NE  
109  C CZ  . ARG A 14  ? 0.5015 0.5856 0.6204 -0.1203 -0.1268 -0.0675 13  ARG A CZ  
110  N NH1 . ARG A 14  ? 0.3875 0.5046 0.5304 -0.1246 -0.1339 -0.0654 13  ARG A NH1 
111  N NH2 . ARG A 14  ? 0.5446 0.6038 0.6746 -0.1311 -0.1196 -0.0675 13  ARG A NH2 
112  N N   . ARG A 15  ? 0.3239 0.3926 0.3373 -0.0449 -0.0844 -0.0145 14  ARG A N   
113  C CA  . ARG A 15  ? 0.3271 0.3958 0.3210 -0.0295 -0.0807 -0.0066 14  ARG A CA  
114  C C   . ARG A 15  ? 0.3674 0.4140 0.3344 -0.0239 -0.0742 -0.0075 14  ARG A C   
115  O O   . ARG A 15  ? 0.3706 0.3998 0.3368 -0.0303 -0.0672 -0.0105 14  ARG A O   
116  C CB  . ARG A 15  ? 0.3304 0.3977 0.3319 -0.0250 -0.0695 0.0050  14  ARG A CB  
117  C CG  . ARG A 15  ? 0.3606 0.4530 0.3864 -0.0264 -0.0737 0.0081  14  ARG A CG  
118  C CD  . ARG A 15  ? 0.3323 0.4480 0.3562 -0.0152 -0.0840 0.0097  14  ARG A CD  
119  N NE  . ARG A 15  ? 0.3482 0.4936 0.4008 -0.0197 -0.0902 0.0099  14  ARG A NE  
120  C CZ  . ARG A 15  ? 0.3338 0.4897 0.4003 -0.0146 -0.0829 0.0183  14  ARG A CZ  
121  N NH1 . ARG A 15  ? 0.3052 0.4427 0.3590 -0.0047 -0.0705 0.0258  14  ARG A NH1 
122  N NH2 . ARG A 15  ? 0.3331 0.5190 0.4281 -0.0200 -0.0877 0.0184  14  ARG A NH2 
123  N N   . VAL A 16  ? 0.3717 0.4212 0.3170 -0.0105 -0.0760 -0.0037 15  VAL A N   
124  C CA  . VAL A 16  ? 0.3779 0.4086 0.2969 -0.0020 -0.0661 0.0005  15  VAL A CA  
125  C C   . VAL A 16  ? 0.4081 0.4387 0.3168 0.0123  -0.0598 0.0149  15  VAL A C   
126  O O   . VAL A 16  ? 0.3883 0.4370 0.3047 0.0186  -0.0671 0.0188  15  VAL A O   
127  C CB  . VAL A 16  ? 0.3740 0.4064 0.2708 0.0018  -0.0744 -0.0096 15  VAL A CB  
128  C CG1 . VAL A 16  ? 0.3878 0.4450 0.2784 0.0106  -0.0899 -0.0116 15  VAL A CG1 
129  C CG2 . VAL A 16  ? 0.3834 0.3976 0.2532 0.0109  -0.0614 -0.0036 15  VAL A CG2 
130  N N   . ASN A 17  ? 0.3997 0.4096 0.2932 0.0176  -0.0453 0.0234  16  ASN A N   
131  C CA  . ASN A 17  ? 0.3948 0.3973 0.2772 0.0312  -0.0366 0.0383  16  ASN A CA  
132  C C   . ASN A 17  ? 0.3999 0.4031 0.3036 0.0301  -0.0331 0.0432  16  ASN A C   
133  O O   . ASN A 17  ? 0.4160 0.4204 0.3158 0.0431  -0.0312 0.0536  16  ASN A O   
134  C CB  . ASN A 17  ? 0.4011 0.4188 0.2623 0.0473  -0.0463 0.0428  16  ASN A CB  
135  C CG  . ASN A 17  ? 0.4275 0.4293 0.2662 0.0628  -0.0336 0.0597  16  ASN A CG  
136  O OD1 . ASN A 17  ? 0.4267 0.4044 0.2671 0.0596  -0.0168 0.0669  16  ASN A OD1 
137  N ND2 . ASN A 17  ? 0.4539 0.4692 0.2718 0.0799  -0.0413 0.0665  16  ASN A ND2 
138  N N   . HIS A 18  ? 0.3600 0.3628 0.2849 0.0163  -0.0320 0.0359  17  HIS A N   
139  C CA  . HIS A 18  ? 0.3529 0.3550 0.2959 0.0146  -0.0270 0.0386  17  HIS A CA  
140  C C   . HIS A 18  ? 0.3769 0.3534 0.3174 0.0131  -0.0113 0.0426  17  HIS A C   
141  O O   . HIS A 18  ? 0.4119 0.3730 0.3391 0.0131  -0.0037 0.0452  17  HIS A O   
142  C CB  . HIS A 18  ? 0.3287 0.3450 0.2936 0.0017  -0.0334 0.0297  17  HIS A CB  
143  C CG  . HIS A 18  ? 0.3727 0.3811 0.3387 -0.0106 -0.0328 0.0218  17  HIS A CG  
144  N ND1 . HIS A 18  ? 0.3664 0.3725 0.3193 -0.0115 -0.0374 0.0167  17  HIS A ND1 
145  C CD2 . HIS A 18  ? 0.3439 0.3469 0.3219 -0.0207 -0.0282 0.0181  17  HIS A CD2 
146  C CE1 . HIS A 18  ? 0.3534 0.3516 0.3116 -0.0212 -0.0349 0.0106  17  HIS A CE1 
147  N NE2 . HIS A 18  ? 0.3140 0.3110 0.2875 -0.0268 -0.0297 0.0120  17  HIS A NE2 
148  N N   . ALA A 19  ? 0.3721 0.3450 0.3264 0.0114  -0.0061 0.0424  18  ALA A N   
149  C CA  . ALA A 19  ? 0.3579 0.3082 0.3139 0.0074  0.0070  0.0426  18  ALA A CA  
150  C C   . ALA A 19  ? 0.3607 0.3166 0.3340 -0.0014 0.0069  0.0344  18  ALA A C   
151  O O   . ALA A 19  ? 0.3855 0.3571 0.3679 0.0016  0.0017  0.0335  18  ALA A O   
152  C CB  . ALA A 19  ? 0.3422 0.2744 0.2903 0.0196  0.0165  0.0527  18  ALA A CB  
153  N N   . ALA A 20  ? 0.3497 0.2954 0.3276 -0.0113 0.0129  0.0286  19  ALA A N   
154  C CA  . ALA A 20  ? 0.3379 0.2923 0.3288 -0.0189 0.0112  0.0205  19  ALA A CA  
155  C C   . ALA A 20  ? 0.3826 0.3218 0.3778 -0.0250 0.0199  0.0147  19  ALA A C   
156  O O   . ALA A 20  ? 0.3349 0.2601 0.3270 -0.0283 0.0266  0.0161  19  ALA A O   
157  C CB  . ALA A 20  ? 0.3248 0.2941 0.3205 -0.0268 0.0033  0.0167  19  ALA A CB  
158  N N   . VAL A 21  ? 0.3724 0.3165 0.3754 -0.0268 0.0198  0.0077  20  VAL A N   
159  C CA  . VAL A 21  ? 0.3502 0.2855 0.3594 -0.0339 0.0249  -0.0018 20  VAL A CA  
160  C C   . VAL A 21  ? 0.3357 0.2904 0.3508 -0.0386 0.0187  -0.0091 20  VAL A C   
161  O O   . VAL A 21  ? 0.3477 0.3184 0.3629 -0.0350 0.0135  -0.0062 20  VAL A O   
162  C CB  . VAL A 21  ? 0.3433 0.2603 0.3524 -0.0289 0.0325  -0.0050 20  VAL A CB  
163  C CG1 . VAL A 21  ? 0.3533 0.2474 0.3562 -0.0239 0.0406  0.0045  20  VAL A CG1 
164  C CG2 . VAL A 21  ? 0.3019 0.2295 0.3098 -0.0190 0.0296  -0.0050 20  VAL A CG2 
165  N N   . ALA A 22  ? 0.3412 0.2957 0.3621 -0.0467 0.0197  -0.0180 21  ALA A N   
166  C CA  . ALA A 22  ? 0.3148 0.2876 0.3393 -0.0494 0.0142  -0.0251 21  ALA A CA  
167  C C   . ALA A 22  ? 0.3093 0.2795 0.3334 -0.0474 0.0163  -0.0360 21  ALA A C   
168  O O   . ALA A 22  ? 0.2931 0.2466 0.3208 -0.0510 0.0215  -0.0438 21  ALA A O   
169  C CB  . ALA A 22  ? 0.2449 0.2241 0.2763 -0.0576 0.0123  -0.0291 21  ALA A CB  
170  N N   . VAL A 23  ? 0.2820 0.2676 0.3019 -0.0414 0.0131  -0.0367 22  VAL A N   
171  C CA  . VAL A 23  ? 0.2862 0.2732 0.3026 -0.0380 0.0143  -0.0490 22  VAL A CA  
172  C C   . VAL A 23  ? 0.3143 0.3249 0.3287 -0.0394 0.0079  -0.0532 22  VAL A C   
173  O O   . VAL A 23  ? 0.3328 0.3602 0.3434 -0.0345 0.0059  -0.0442 22  VAL A O   
174  C CB  . VAL A 23  ? 0.3105 0.2971 0.3213 -0.0265 0.0181  -0.0456 22  VAL A CB  
175  C CG1 . VAL A 23  ? 0.3302 0.3183 0.3351 -0.0220 0.0197  -0.0605 22  VAL A CG1 
176  C CG2 . VAL A 23  ? 0.3261 0.2908 0.3379 -0.0224 0.0238  -0.0393 22  VAL A CG2 
177  N N   . GLY A 24  ? 0.2791 0.2920 0.2967 -0.0458 0.0050  -0.0662 23  GLY A N   
178  C CA  . GLY A 24  ? 0.2702 0.3076 0.2849 -0.0454 -0.0021 -0.0691 23  GLY A CA  
179  C C   . GLY A 24  ? 0.2792 0.3254 0.2979 -0.0471 -0.0050 -0.0549 23  GLY A C   
180  O O   . GLY A 24  ? 0.2953 0.3326 0.3228 -0.0535 -0.0042 -0.0523 23  GLY A O   
181  N N   . HIS A 25  ? 0.2937 0.3562 0.3058 -0.0408 -0.0071 -0.0450 24  HIS A N   
182  C CA  . HIS A 25  ? 0.2735 0.3407 0.2893 -0.0417 -0.0091 -0.0311 24  HIS A CA  
183  C C   . HIS A 25  ? 0.2763 0.3370 0.2930 -0.0401 -0.0056 -0.0183 24  HIS A C   
184  O O   . HIS A 25  ? 0.3061 0.3717 0.3250 -0.0400 -0.0068 -0.0071 24  HIS A O   
185  C CB  . HIS A 25  ? 0.2702 0.3585 0.2803 -0.0365 -0.0134 -0.0273 24  HIS A CB  
186  C CG  . HIS A 25  ? 0.3014 0.4024 0.2997 -0.0283 -0.0113 -0.0255 24  HIS A CG  
187  N ND1 . HIS A 25  ? 0.3541 0.4590 0.3509 -0.0245 -0.0069 -0.0104 24  HIS A ND1 
188  C CD2 . HIS A 25  ? 0.3415 0.4528 0.3292 -0.0232 -0.0122 -0.0376 24  HIS A CD2 
189  C CE1 . HIS A 25  ? 0.3340 0.4522 0.3197 -0.0166 -0.0039 -0.0116 24  HIS A CE1 
190  N NE2 . HIS A 25  ? 0.3600 0.4818 0.3382 -0.0149 -0.0074 -0.0287 24  HIS A NE2 
191  N N   . ARG A 26  ? 0.2697 0.3202 0.2859 -0.0385 -0.0016 -0.0200 25  ARG A N   
192  C CA  . ARG A 26  ? 0.2898 0.3387 0.3093 -0.0368 0.0002  -0.0092 25  ARG A CA  
193  C C   . ARG A 26  ? 0.3256 0.3564 0.3473 -0.0389 0.0016  -0.0100 25  ARG A C   
194  O O   . ARG A 26  ? 0.3435 0.3616 0.3633 -0.0386 0.0047  -0.0181 25  ARG A O   
195  C CB  . ARG A 26  ? 0.2948 0.3547 0.3111 -0.0291 0.0041  -0.0073 25  ARG A CB  
196  C CG  . ARG A 26  ? 0.2705 0.3500 0.2836 -0.0263 0.0043  -0.0012 25  ARG A CG  
197  C CD  . ARG A 26  ? 0.2964 0.3879 0.3015 -0.0173 0.0092  -0.0048 25  ARG A CD  
198  N NE  . ARG A 26  ? 0.3269 0.4241 0.3386 -0.0130 0.0141  0.0027  25  ARG A NE  
199  C CZ  . ARG A 26  ? 0.3612 0.4525 0.3719 -0.0065 0.0177  -0.0037 25  ARG A CZ  
200  N NH1 . ARG A 26  ? 0.3560 0.4315 0.3591 -0.0049 0.0178  -0.0180 25  ARG A NH1 
201  N NH2 . ARG A 26  ? 0.3545 0.4562 0.3735 -0.0014 0.0217  0.0044  25  ARG A NH2 
202  N N   . VAL A 27  ? 0.2834 0.3124 0.3088 -0.0409 -0.0006 -0.0018 26  VAL A N   
203  C CA  . VAL A 27  ? 0.2961 0.3107 0.3204 -0.0410 0.0002  -0.0006 26  VAL A CA  
204  C C   . VAL A 27  ? 0.3011 0.3206 0.3266 -0.0349 0.0002  0.0050  26  VAL A C   
205  O O   . VAL A 27  ? 0.2852 0.3191 0.3170 -0.0354 -0.0029 0.0108  26  VAL A O   
206  C CB  . VAL A 27  ? 0.2989 0.3093 0.3239 -0.0461 -0.0032 0.0023  26  VAL A CB  
207  C CG1 . VAL A 27  ? 0.3053 0.3034 0.3251 -0.0439 -0.0023 0.0044  26  VAL A CG1 
208  C CG2 . VAL A 27  ? 0.2868 0.2953 0.3128 -0.0504 -0.0027 -0.0028 26  VAL A CG2 
209  N N   . TYR A 28  ? 0.3006 0.3084 0.3220 -0.0290 0.0041  0.0038  27  TYR A N   
210  C CA  . TYR A 28  ? 0.3312 0.3443 0.3540 -0.0206 0.0039  0.0095  27  TYR A CA  
211  C C   . TYR A 28  ? 0.3200 0.3257 0.3384 -0.0194 0.0008  0.0146  27  TYR A C   
212  O O   . TYR A 28  ? 0.3258 0.3127 0.3365 -0.0186 0.0050  0.0140  27  TYR A O   
213  C CB  . TYR A 28  ? 0.3217 0.3254 0.3411 -0.0115 0.0107  0.0060  27  TYR A CB  
214  C CG  . TYR A 28  ? 0.3391 0.3533 0.3599 -0.0086 0.0138  0.0003  27  TYR A CG  
215  C CD1 . TYR A 28  ? 0.3295 0.3449 0.3480 -0.0149 0.0138  -0.0077 27  TYR A CD1 
216  C CD2 . TYR A 28  ? 0.3714 0.3959 0.3946 0.0025  0.0171  0.0024  27  TYR A CD2 
217  C CE1 . TYR A 28  ? 0.3361 0.3624 0.3517 -0.0104 0.0164  -0.0136 27  TYR A CE1 
218  C CE2 . TYR A 28  ? 0.3588 0.3934 0.3805 0.0070  0.0212  -0.0034 27  TYR A CE2 
219  C CZ  . TYR A 28  ? 0.3590 0.3940 0.3752 0.0005  0.0207  -0.0116 27  TYR A CZ  
220  O OH  . TYR A 28  ? 0.3786 0.4251 0.3895 0.0065  0.0245  -0.0180 27  TYR A OH  
221  N N   . SER A 29  ? 0.3164 0.3376 0.3400 -0.0192 -0.0061 0.0193  28  SER A N   
222  C CA  . SER A 29  ? 0.3348 0.3534 0.3520 -0.0165 -0.0109 0.0227  28  SER A CA  
223  C C   . SER A 29  ? 0.3566 0.3873 0.3762 -0.0052 -0.0134 0.0282  28  SER A C   
224  O O   . SER A 29  ? 0.3298 0.3811 0.3625 -0.0038 -0.0154 0.0295  28  SER A O   
225  C CB  . SER A 29  ? 0.3076 0.3348 0.3288 -0.0255 -0.0190 0.0210  28  SER A CB  
226  O OG  . SER A 29  ? 0.3355 0.3589 0.3463 -0.0223 -0.0239 0.0217  28  SER A OG  
227  N N   . PHE A 30  ? 0.3247 0.3443 0.3320 0.0039  -0.0125 0.0326  29  PHE A N   
228  C CA  . PHE A 30  ? 0.3136 0.3421 0.3207 0.0185  -0.0139 0.0393  29  PHE A CA  
229  C C   . PHE A 30  ? 0.3443 0.3829 0.3435 0.0231  -0.0236 0.0429  29  PHE A C   
230  O O   . PHE A 30  ? 0.3472 0.3697 0.3300 0.0232  -0.0223 0.0441  29  PHE A O   
231  C CB  . PHE A 30  ? 0.3227 0.3263 0.3199 0.0293  -0.0027 0.0432  29  PHE A CB  
232  C CG  . PHE A 30  ? 0.3877 0.3812 0.3911 0.0263  0.0059  0.0369  29  PHE A CG  
233  C CD1 . PHE A 30  ? 0.3490 0.3263 0.3503 0.0144  0.0107  0.0297  29  PHE A CD1 
234  C CD2 . PHE A 30  ? 0.3596 0.3625 0.3707 0.0362  0.0089  0.0371  29  PHE A CD2 
235  C CE1 . PHE A 30  ? 0.3500 0.3211 0.3557 0.0120  0.0166  0.0217  29  PHE A CE1 
236  C CE2 . PHE A 30  ? 0.3581 0.3525 0.3718 0.0345  0.0163  0.0292  29  PHE A CE2 
237  C CZ  . PHE A 30  ? 0.3643 0.3428 0.3746 0.0220  0.0194  0.0209  29  PHE A CZ  
238  N N   . GLY A 31  ? 0.3506 0.4176 0.3613 0.0278  -0.0330 0.0444  30  GLY A N   
239  C CA  . GLY A 31  ? 0.3243 0.4040 0.3260 0.0359  -0.0434 0.0474  30  GLY A CA  
240  C C   . GLY A 31  ? 0.3279 0.4041 0.3203 0.0252  -0.0504 0.0404  30  GLY A C   
241  O O   . GLY A 31  ? 0.2966 0.3733 0.2992 0.0100  -0.0520 0.0327  30  GLY A O   
242  N N   . GLY A 32  ? 0.3221 0.3932 0.2930 0.0346  -0.0536 0.0437  31  GLY A N   
243  C CA  . GLY A 32  ? 0.3367 0.4068 0.2954 0.0279  -0.0610 0.0361  31  GLY A CA  
244  C C   . GLY A 32  ? 0.3975 0.4979 0.3585 0.0311  -0.0786 0.0310  31  GLY A C   
245  O O   . GLY A 32  ? 0.4131 0.5397 0.3914 0.0353  -0.0859 0.0327  31  GLY A O   
246  N N   . TYR A 33  ? 0.3918 0.4902 0.3355 0.0292  -0.0856 0.0235  32  TYR A N   
247  C CA  . TYR A 33  ? 0.3940 0.5195 0.3357 0.0313  -0.1040 0.0148  32  TYR A CA  
248  C C   . TYR A 33  ? 0.4185 0.5498 0.3784 0.0115  -0.1129 -0.0017 32  TYR A C   
249  O O   . TYR A 33  ? 0.3738 0.4834 0.3377 -0.0006 -0.1041 -0.0052 32  TYR A O   
250  C CB  . TYR A 33  ? 0.3976 0.5163 0.3028 0.0453  -0.1058 0.0167  32  TYR A CB  
251  C CG  . TYR A 33  ? 0.4605 0.6079 0.3593 0.0482  -0.1265 0.0048  32  TYR A CG  
252  C CD1 . TYR A 33  ? 0.4863 0.6667 0.3912 0.0604  -0.1394 0.0085  32  TYR A CD1 
253  C CD2 . TYR A 33  ? 0.4413 0.5845 0.3297 0.0390  -0.1339 -0.0117 32  TYR A CD2 
254  C CE1 . TYR A 33  ? 0.4962 0.7070 0.3973 0.0622  -0.1604 -0.0046 32  TYR A CE1 
255  C CE2 . TYR A 33  ? 0.4929 0.6625 0.3758 0.0406  -0.1541 -0.0258 32  TYR A CE2 
256  C CZ  . TYR A 33  ? 0.5010 0.7056 0.3906 0.0516  -0.1680 -0.0227 32  TYR A CZ  
257  O OH  . TYR A 33  ? 0.5235 0.7578 0.4088 0.0526  -0.1899 -0.0388 32  TYR A OH  
258  N N   . CYS A 34  ? 0.3847 0.5461 0.3574 0.0082  -0.1305 -0.0117 33  CYS A N   
259  C CA  . CYS A 34  ? 0.4116 0.5761 0.3995 -0.0103 -0.1403 -0.0289 33  CYS A CA  
260  C C   . CYS A 34  ? 0.4184 0.6150 0.4081 -0.0088 -0.1617 -0.0416 33  CYS A C   
261  O O   . CYS A 34  ? 0.4712 0.6997 0.4764 -0.0024 -0.1700 -0.0371 33  CYS A O   
262  C CB  . CYS A 34  ? 0.4234 0.5912 0.4482 -0.0269 -0.1354 -0.0280 33  CYS A CB  
263  S SG  . CYS A 34  ? 0.4257 0.5908 0.4728 -0.0509 -0.1445 -0.0467 33  CYS A SG  
264  N N   . SER A 35  ? 0.4033 0.5931 0.3786 -0.0144 -0.1711 -0.0586 34  SER A N   
265  C CA  . SER A 35  ? 0.4487 0.6693 0.4224 -0.0130 -0.1934 -0.0742 34  SER A CA  
266  C C   . SER A 35  ? 0.4381 0.6902 0.4573 -0.0291 -0.2053 -0.0816 34  SER A C   
267  O O   . SER A 35  ? 0.4104 0.6522 0.4595 -0.0470 -0.1975 -0.0814 34  SER A O   
268  C CB  . SER A 35  ? 0.4982 0.7024 0.4502 -0.0185 -0.2007 -0.0949 34  SER A CB  
269  O OG  . SER A 35  ? 0.5962 0.7658 0.5147 -0.0097 -0.1849 -0.0885 34  SER A OG  
270  N N   . GLY A 36  ? 0.4347 0.7277 0.4596 -0.0217 -0.2238 -0.0867 35  GLY A N   
271  C CA  . GLY A 36  ? 0.4380 0.7680 0.5083 -0.0368 -0.2368 -0.0949 35  GLY A CA  
272  C C   . GLY A 36  ? 0.4452 0.7955 0.5450 -0.0332 -0.2276 -0.0760 35  GLY A C   
273  O O   . GLY A 36  ? 0.5047 0.8907 0.6409 -0.0409 -0.2372 -0.0787 35  GLY A O   
274  N N   . GLU A 37  ? 0.4701 0.7952 0.5553 -0.0217 -0.2075 -0.0565 36  GLU A N   
275  C CA  . GLU A 37  ? 0.5130 0.8533 0.6212 -0.0156 -0.1970 -0.0393 36  GLU A CA  
276  C C   . GLU A 37  ? 0.5508 0.9062 0.6373 0.0123  -0.1988 -0.0261 36  GLU A C   
277  O O   . GLU A 37  ? 0.5399 0.8898 0.5909 0.0269  -0.2055 -0.0275 36  GLU A O   
278  C CB  . GLU A 37  ? 0.4326 0.7353 0.5403 -0.0214 -0.1742 -0.0283 36  GLU A CB  
279  C CG  . GLU A 37  ? 0.4320 0.7215 0.5626 -0.0470 -0.1720 -0.0385 36  GLU A CG  
280  C CD  . GLU A 37  ? 0.4675 0.7219 0.5949 -0.0517 -0.1513 -0.0283 36  GLU A CD  
281  O OE1 . GLU A 37  ? 0.4652 0.7095 0.5786 -0.0371 -0.1388 -0.0145 36  GLU A OE1 
282  O OE2 . GLU A 37  ? 0.4255 0.6623 0.5645 -0.0695 -0.1480 -0.0347 36  GLU A OE2 
283  N N   . ASP A 38  ? 0.6324 1.0078 0.7405 0.0210  -0.1923 -0.0126 37  ASP A N   
284  C CA  . ASP A 38  ? 0.6120 1.0126 0.7099 0.0473  -0.1980 -0.0015 37  ASP A CA  
285  C C   . ASP A 38  ? 0.6719 1.0340 0.7361 0.0670  -0.1794 0.0162  37  ASP A C   
286  O O   . ASP A 38  ? 0.6378 0.9760 0.7090 0.0639  -0.1610 0.0247  37  ASP A O   
287  C CB  . ASP A 38  ? 0.5943 1.0400 0.7345 0.0490  -0.2013 0.0033  37  ASP A CB  
288  C CG  . ASP A 38  ? 0.6731 1.1442 0.8034 0.0787  -0.2065 0.0159  37  ASP A CG  
289  O OD1 . ASP A 38  ? 0.7138 1.1942 0.8281 0.0857  -0.2205 0.0102  37  ASP A OD1 
290  O OD2 . ASP A 38  ? 0.7035 1.1676 0.8369 0.0932  -0.1912 0.0317  37  ASP A OD2 
291  N N   . TYR A 39  ? 0.6671 1.0235 0.6945 0.0871  -0.1841 0.0215  38  TYR A N   
292  C CA  . TYR A 39  ? 0.6468 0.9677 0.6428 0.1068  -0.1668 0.0396  38  TYR A CA  
293  C C   . TYR A 39  ? 0.7064 1.0501 0.6877 0.1365  -0.1740 0.0531  38  TYR A C   
294  O O   . TYR A 39  ? 0.7063 1.0217 0.6548 0.1553  -0.1628 0.0682  38  TYR A O   
295  C CB  . TYR A 39  ? 0.5609 0.8396 0.5218 0.1016  -0.1586 0.0369  38  TYR A CB  
296  C CG  . TYR A 39  ? 0.5839 0.8356 0.5602 0.0771  -0.1469 0.0290  38  TYR A CG  
297  C CD1 . TYR A 39  ? 0.5153 0.7782 0.5113 0.0545  -0.1573 0.0111  38  TYR A CD1 
298  C CD2 . TYR A 39  ? 0.5161 0.7328 0.4898 0.0769  -0.1259 0.0394  38  TYR A CD2 
299  C CE1 . TYR A 39  ? 0.4980 0.7375 0.5084 0.0346  -0.1464 0.0063  38  TYR A CE1 
300  C CE2 . TYR A 39  ? 0.4220 0.6189 0.4097 0.0567  -0.1167 0.0328  38  TYR A CE2 
301  C CZ  . TYR A 39  ? 0.4468 0.6552 0.4519 0.0366  -0.1266 0.0175  38  TYR A CZ  
302  O OH  . TYR A 39  ? 0.4213 0.6101 0.4391 0.0187  -0.1173 0.0130  38  TYR A OH  
303  N N   . GLU A 40  ? 0.7217 1.1172 0.7290 0.1412  -0.1917 0.0489  39  GLU A N   
304  C CA  . GLU A 40  ? 0.7478 1.1607 0.7481 0.1658  -0.1952 0.0606  39  GLU A CA  
305  C C   . GLU A 40  ? 0.7556 1.1840 0.7861 0.1761  -0.1866 0.0719  39  GLU A C   
306  O O   . GLU A 40  ? 0.7966 1.2073 0.8112 0.1996  -0.1744 0.0896  39  GLU A O   
307  C CB  . GLU A 40  ? 0.7395 1.1871 0.7467 0.1602  -0.2163 0.0458  39  GLU A CB  
308  C CG  . GLU A 40  ? 0.8176 1.2517 0.7927 0.1532  -0.2253 0.0333  39  GLU A CG  
309  C CD  . GLU A 40  ? 0.8367 1.3055 0.8197 0.1485  -0.2464 0.0182  39  GLU A CD  
310  O OE1 . GLU A 40  ? 0.7715 1.2720 0.7731 0.1595  -0.2529 0.0233  39  GLU A OE1 
311  O OE2 . GLU A 40  ? 0.8263 1.2907 0.7975 0.1341  -0.2564 0.0007  39  GLU A OE2 
312  N N   . THR A 41  ? 0.7466 1.2053 0.8205 0.1587  -0.1908 0.0621  40  THR A N   
313  C CA  . THR A 41  ? 0.7684 1.2481 0.8724 0.1687  -0.1834 0.0710  40  THR A CA  
314  C C   . THR A 41  ? 0.7983 1.2482 0.9002 0.1762  -0.1620 0.0836  40  THR A C   
315  O O   . THR A 41  ? 0.7558 1.1572 0.8330 0.1676  -0.1495 0.0836  40  THR A O   
316  C CB  . THR A 41  ? 0.7047 1.2259 0.8563 0.1467  -0.1930 0.0573  40  THR A CB  
317  O OG1 . THR A 41  ? 0.7800 1.2918 0.9491 0.1233  -0.1855 0.0507  40  THR A OG1 
318  C CG2 . THR A 41  ? 0.6522 1.1956 0.8053 0.1350  -0.2145 0.0417  40  THR A CG2 
319  N N   . LEU A 42  ? 0.9311 1.3959 1.0568 0.1874  -0.1529 0.0912  41  LEU A N   
320  C CA  . LEU A 42  ? 0.8721 1.3047 0.9973 0.1936  -0.1306 0.1001  41  LEU A CA  
321  C C   . LEU A 42  ? 0.7900 1.2147 0.9359 0.1631  -0.1231 0.0882  41  LEU A C   
322  O O   . LEU A 42  ? 0.7961 1.2598 0.9798 0.1529  -0.1258 0.0835  41  LEU A O   
323  C CB  . LEU A 42  ? 0.9075 1.3623 1.0514 0.2168  -0.1242 0.1102  41  LEU A CB  
324  C CG  . LEU A 42  ? 0.9738 1.4248 1.0957 0.2426  -0.1276 0.1204  41  LEU A CG  
325  C CD1 . LEU A 42  ? 0.8364 1.3261 0.9866 0.2551  -0.1292 0.1227  41  LEU A CD1 
326  C CD2 . LEU A 42  ? 1.0103 1.4059 1.0965 0.2626  -0.1104 0.1349  41  LEU A CD2 
327  N N   . ARG A 43  ? 0.6545 1.0306 0.7768 0.1489  -0.1132 0.0845  42  ARG A N   
328  C CA  . ARG A 43  ? 0.5143 0.8764 0.6510 0.1247  -0.1030 0.0765  42  ARG A CA  
329  C C   . ARG A 43  ? 0.4430 0.7532 0.5567 0.1289  -0.0830 0.0812  42  ARG A C   
330  O O   . ARG A 43  ? 0.4249 0.7004 0.5076 0.1397  -0.0788 0.0868  42  ARG A O   
331  C CB  . ARG A 43  ? 0.4558 0.8121 0.5905 0.0988  -0.1123 0.0639  42  ARG A CB  
332  C CG  . ARG A 43  ? 0.5876 0.9799 0.7291 0.0960  -0.1344 0.0565  42  ARG A CG  
333  C CD  . ARG A 43  ? 0.5615 0.9329 0.6924 0.0731  -0.1395 0.0438  42  ARG A CD  
334  N NE  . ARG A 43  ? 0.4595 0.8081 0.6016 0.0535  -0.1258 0.0409  42  ARG A NE  
335  C CZ  . ARG A 43  ? 0.4739 0.7971 0.6076 0.0343  -0.1253 0.0319  42  ARG A CZ  
336  N NH1 . ARG A 43  ? 0.4717 0.7866 0.5849 0.0315  -0.1369 0.0235  42  ARG A NH1 
337  N NH2 . ARG A 43  ? 0.4379 0.7443 0.5827 0.0192  -0.1129 0.0314  42  ARG A NH2 
338  N N   . GLN A 44  ? 0.4047 0.7109 0.5340 0.1201  -0.0705 0.0787  43  GLN A N   
339  C CA  . GLN A 44  ? 0.3740 0.6331 0.4837 0.1192  -0.0536 0.0788  43  GLN A CA  
340  C C   . GLN A 44  ? 0.3678 0.5959 0.4595 0.0994  -0.0544 0.0718  43  GLN A C   
341  O O   . GLN A 44  ? 0.3326 0.5759 0.4339 0.0815  -0.0646 0.0647  43  GLN A O   
342  C CB  . GLN A 44  ? 0.3508 0.6177 0.4795 0.1149  -0.0415 0.0764  43  GLN A CB  
343  C CG  . GLN A 44  ? 0.3140 0.6125 0.4621 0.1350  -0.0382 0.0827  43  GLN A CG  
344  C CD  . GLN A 44  ? 0.3510 0.6501 0.5102 0.1326  -0.0233 0.0801  43  GLN A CD  
345  O OE1 . GLN A 44  ? 0.3314 0.6084 0.4830 0.1157  -0.0171 0.0738  43  GLN A OE1 
346  N NE2 . GLN A 44  ? 0.3131 0.6380 0.4886 0.1510  -0.0173 0.0848  43  GLN A NE2 
347  N N   . ILE A 45  ? 0.3660 0.5500 0.4330 0.1028  -0.0431 0.0734  44  ILE A N   
348  C CA  . ILE A 45  ? 0.3809 0.5361 0.4341 0.0846  -0.0408 0.0667  44  ILE A CA  
349  C C   . ILE A 45  ? 0.3562 0.5173 0.4263 0.0669  -0.0366 0.0593  44  ILE A C   
350  O O   . ILE A 45  ? 0.3046 0.4838 0.3920 0.0704  -0.0314 0.0601  44  ILE A O   
351  C CB  . ILE A 45  ? 0.4083 0.5177 0.4365 0.0907  -0.0284 0.0701  44  ILE A CB  
352  C CG1 . ILE A 45  ? 0.3832 0.4711 0.3956 0.0757  -0.0298 0.0655  44  ILE A CG1 
353  C CG2 . ILE A 45  ? 0.3298 0.4207 0.3622 0.0913  -0.0141 0.0669  44  ILE A CG2 
354  C CD1 . ILE A 45  ? 0.3512 0.3971 0.3443 0.0773  -0.0169 0.0680  44  ILE A CD1 
355  N N   . ASP A 46  ? 0.4040 0.5483 0.4669 0.0497  -0.0374 0.0530  45  ASP A N   
356  C CA  . ASP A 46  ? 0.3401 0.4911 0.4166 0.0313  -0.0372 0.0471  45  ASP A CA  
357  C C   . ASP A 46  ? 0.3608 0.4811 0.4251 0.0256  -0.0258 0.0436  45  ASP A C   
358  O O   . ASP A 46  ? 0.3742 0.4659 0.4195 0.0277  -0.0221 0.0430  45  ASP A O   
359  C CB  . ASP A 46  ? 0.3253 0.4800 0.4013 0.0178  -0.0490 0.0420  45  ASP A CB  
360  C CG  . ASP A 46  ? 0.3588 0.5425 0.4608 0.0055  -0.0555 0.0394  45  ASP A CG  
361  O OD1 . ASP A 46  ? 0.4203 0.6234 0.5400 0.0088  -0.0499 0.0435  45  ASP A OD1 
362  O OD2 . ASP A 46  ? 0.3772 0.5640 0.4827 -0.0068 -0.0651 0.0334  45  ASP A OD2 
363  N N   . VAL A 47  ? 0.2945 0.4220 0.3699 0.0180  -0.0204 0.0416  46  VAL A N   
364  C CA  . VAL A 47  ? 0.3085 0.4123 0.3731 0.0110  -0.0128 0.0367  46  VAL A CA  
365  C C   . VAL A 47  ? 0.3005 0.4151 0.3759 -0.0038 -0.0146 0.0355  46  VAL A C   
366  O O   . VAL A 47  ? 0.2543 0.3912 0.3451 -0.0048 -0.0120 0.0388  46  VAL A O   
367  C CB  . VAL A 47  ? 0.3295 0.4254 0.3898 0.0207  -0.0018 0.0348  46  VAL A CB  
368  C CG1 . VAL A 47  ? 0.3018 0.3770 0.3516 0.0121  0.0031  0.0278  46  VAL A CG1 
369  C CG2 . VAL A 47  ? 0.3209 0.4021 0.3720 0.0367  0.0020  0.0370  46  VAL A CG2 
370  N N   . HIS A 48  ? 0.3416 0.4399 0.4093 -0.0142 -0.0174 0.0320  47  HIS A N   
371  C CA  . HIS A 48  ? 0.2999 0.4008 0.3744 -0.0265 -0.0174 0.0317  47  HIS A CA  
372  C C   . HIS A 48  ? 0.2807 0.3622 0.3419 -0.0277 -0.0113 0.0277  47  HIS A C   
373  O O   . HIS A 48  ? 0.3181 0.3802 0.3661 -0.0247 -0.0098 0.0236  47  HIS A O   
374  C CB  . HIS A 48  ? 0.2573 0.3563 0.3356 -0.0368 -0.0263 0.0299  47  HIS A CB  
375  C CG  . HIS A 48  ? 0.2680 0.3888 0.3618 -0.0383 -0.0347 0.0311  47  HIS A CG  
376  N ND1 . HIS A 48  ? 0.2961 0.4213 0.3843 -0.0299 -0.0412 0.0300  47  HIS A ND1 
377  C CD2 . HIS A 48  ? 0.2980 0.4391 0.4142 -0.0477 -0.0382 0.0332  47  HIS A CD2 
378  C CE1 . HIS A 48  ? 0.2786 0.4284 0.3850 -0.0338 -0.0500 0.0298  47  HIS A CE1 
379  N NE2 . HIS A 48  ? 0.2917 0.4512 0.4171 -0.0458 -0.0479 0.0313  47  HIS A NE2 
380  N N   . ILE A 49  ? 0.2674 0.3560 0.3328 -0.0320 -0.0076 0.0294  48  ILE A N   
381  C CA  . ILE A 49  ? 0.2833 0.3601 0.3374 -0.0322 -0.0033 0.0249  48  ILE A CA  
382  C C   . ILE A 49  ? 0.2735 0.3486 0.3300 -0.0412 -0.0056 0.0273  48  ILE A C   
383  O O   . ILE A 49  ? 0.2644 0.3523 0.3314 -0.0451 -0.0048 0.0345  48  ILE A O   
384  C CB  . ILE A 49  ? 0.2792 0.3665 0.3307 -0.0246 0.0038  0.0242  48  ILE A CB  
385  C CG1 . ILE A 49  ? 0.2813 0.3645 0.3294 -0.0140 0.0068  0.0207  48  ILE A CG1 
386  C CG2 . ILE A 49  ? 0.3022 0.3816 0.3423 -0.0257 0.0057  0.0181  48  ILE A CG2 
387  C CD1 . ILE A 49  ? 0.2872 0.3819 0.3335 -0.0044 0.0142  0.0190  48  ILE A CD1 
388  N N   . PHE A 50  ? 0.2347 0.2937 0.2828 -0.0441 -0.0073 0.0223  49  PHE A N   
389  C CA  . PHE A 50  ? 0.2536 0.3098 0.3030 -0.0497 -0.0088 0.0245  49  PHE A CA  
390  C C   . PHE A 50  ? 0.2700 0.3288 0.3116 -0.0464 -0.0056 0.0220  49  PHE A C   
391  O O   . PHE A 50  ? 0.2800 0.3319 0.3144 -0.0442 -0.0048 0.0137  49  PHE A O   
392  C CB  . PHE A 50  ? 0.2867 0.3274 0.3332 -0.0538 -0.0129 0.0206  49  PHE A CB  
393  C CG  . PHE A 50  ? 0.2720 0.3083 0.3201 -0.0573 -0.0137 0.0227  49  PHE A CG  
394  C CD1 . PHE A 50  ? 0.2601 0.2975 0.3179 -0.0623 -0.0153 0.0290  49  PHE A CD1 
395  C CD2 . PHE A 50  ? 0.2694 0.3011 0.3112 -0.0555 -0.0126 0.0187  49  PHE A CD2 
396  C CE1 . PHE A 50  ? 0.3046 0.3347 0.3636 -0.0637 -0.0150 0.0323  49  PHE A CE1 
397  C CE2 . PHE A 50  ? 0.2743 0.3033 0.3179 -0.0562 -0.0134 0.0217  49  PHE A CE2 
398  C CZ  . PHE A 50  ? 0.2936 0.3200 0.3446 -0.0594 -0.0142 0.0290  49  PHE A CZ  
399  N N   . ASN A 51  ? 0.2648 0.3345 0.3083 -0.0459 -0.0036 0.0293  50  ASN A N   
400  C CA  . ASN A 51  ? 0.2746 0.3509 0.3087 -0.0413 -0.0021 0.0272  50  ASN A CA  
401  C C   . ASN A 51  ? 0.2815 0.3505 0.3150 -0.0436 -0.0056 0.0274  50  ASN A C   
402  O O   . ASN A 51  ? 0.2690 0.3351 0.3082 -0.0461 -0.0058 0.0365  50  ASN A O   
403  C CB  . ASN A 51  ? 0.2730 0.3667 0.3063 -0.0368 0.0029  0.0370  50  ASN A CB  
404  C CG  . ASN A 51  ? 0.2840 0.3881 0.3032 -0.0295 0.0035  0.0332  50  ASN A CG  
405  O OD1 . ASN A 51  ? 0.3054 0.4073 0.3203 -0.0292 -0.0006 0.0304  50  ASN A OD1 
406  N ND2 . ASN A 51  ? 0.2827 0.4005 0.2947 -0.0225 0.0083  0.0323  50  ASN A ND2 
407  N N   . ALA A 52  ? 0.2551 0.3209 0.2835 -0.0428 -0.0079 0.0172  51  ALA A N   
408  C CA  . ALA A 52  ? 0.3010 0.3622 0.3314 -0.0441 -0.0109 0.0166  51  ALA A CA  
409  C C   . ALA A 52  ? 0.2967 0.3712 0.3230 -0.0383 -0.0121 0.0220  51  ALA A C   
410  O O   . ALA A 52  ? 0.3674 0.4409 0.3959 -0.0370 -0.0148 0.0222  51  ALA A O   
411  C CB  . ALA A 52  ? 0.2224 0.2778 0.2531 -0.0465 -0.0120 0.0046  51  ALA A CB  
412  N N   . VAL A 53  ? 0.3122 0.4005 0.3315 -0.0330 -0.0100 0.0266  52  VAL A N   
413  C CA  . VAL A 53  ? 0.3420 0.4434 0.3548 -0.0255 -0.0103 0.0359  52  VAL A CA  
414  C C   . VAL A 53  ? 0.3464 0.4432 0.3638 -0.0258 -0.0051 0.0538  52  VAL A C   
415  O O   . VAL A 53  ? 0.3788 0.4703 0.3985 -0.0236 -0.0053 0.0635  52  VAL A O   
416  C CB  . VAL A 53  ? 0.3591 0.4804 0.3582 -0.0179 -0.0106 0.0302  52  VAL A CB  
417  C CG1 . VAL A 53  ? 0.3222 0.4589 0.3114 -0.0080 -0.0114 0.0412  52  VAL A CG1 
418  C CG2 . VAL A 53  ? 0.2578 0.3815 0.2557 -0.0199 -0.0161 0.0105  52  VAL A CG2 
419  N N   . SER A 54  ? 0.3129 0.4112 0.3340 -0.0288 0.0001  0.0584  53  SER A N   
420  C CA  . SER A 54  ? 0.3193 0.4138 0.3499 -0.0320 0.0057  0.0749  53  SER A CA  
421  C C   . SER A 54  ? 0.3362 0.4111 0.3818 -0.0422 0.0035  0.0737  53  SER A C   
422  O O   . SER A 54  ? 0.3514 0.4190 0.4079 -0.0471 0.0071  0.0853  53  SER A O   
423  C CB  . SER A 54  ? 0.2907 0.3995 0.3228 -0.0314 0.0128  0.0807  53  SER A CB  
424  O OG  . SER A 54  ? 0.2722 0.3794 0.3099 -0.0357 0.0108  0.0694  53  SER A OG  
425  N N   . LEU A 55  ? 0.2984 0.3645 0.3443 -0.0456 -0.0020 0.0597  54  LEU A N   
426  C CA  . LEU A 55  ? 0.3082 0.3571 0.3639 -0.0535 -0.0051 0.0562  54  LEU A CA  
427  C C   . LEU A 55  ? 0.3139 0.3646 0.3828 -0.0609 -0.0035 0.0609  54  LEU A C   
428  O O   . LEU A 55  ? 0.3279 0.3666 0.4078 -0.0682 -0.0049 0.0628  54  LEU A O   
429  C CB  . LEU A 55  ? 0.3055 0.3400 0.3630 -0.0528 -0.0060 0.0604  54  LEU A CB  
430  C CG  . LEU A 55  ? 0.3440 0.3828 0.3917 -0.0445 -0.0083 0.0559  54  LEU A CG  
431  C CD1 . LEU A 55  ? 0.2468 0.2752 0.2962 -0.0399 -0.0080 0.0632  54  LEU A CD1 
432  C CD2 . LEU A 55  ? 0.2992 0.3355 0.3441 -0.0460 -0.0119 0.0409  54  LEU A CD2 
433  N N   . ARG A 56  ? 0.2572 0.3239 0.3263 -0.0591 -0.0007 0.0612  55  ARG A N   
434  C CA  . ARG A 56  ? 0.2613 0.3368 0.3454 -0.0650 0.0007  0.0651  55  ARG A CA  
435  C C   . ARG A 56  ? 0.2847 0.3635 0.3675 -0.0637 -0.0034 0.0545  55  ARG A C   
436  O O   . ARG A 56  ? 0.3051 0.3855 0.3754 -0.0565 -0.0029 0.0479  55  ARG A O   
437  C CB  . ARG A 56  ? 0.2926 0.3880 0.3802 -0.0617 0.0094  0.0768  55  ARG A CB  
438  C CG  . ARG A 56  ? 0.3148 0.4092 0.4002 -0.0599 0.0155  0.0907  55  ARG A CG  
439  C CD  . ARG A 56  ? 0.3632 0.4386 0.4622 -0.0695 0.0140  0.0957  55  ARG A CD  
440  N NE  . ARG A 56  ? 0.4774 0.5579 0.6000 -0.0808 0.0164  0.1013  55  ARG A NE  
441  C CZ  . ARG A 56  ? 0.4578 0.5218 0.5964 -0.0922 0.0134  0.1007  55  ARG A CZ  
442  N NH1 . ARG A 56  ? 0.4150 0.4551 0.5467 -0.0922 0.0082  0.0945  55  ARG A NH1 
443  N NH2 . ARG A 56  ? 0.3926 0.4652 0.5560 -0.1038 0.0156  0.1053  55  ARG A NH2 
444  N N   . TRP A 57  ? 0.2499 0.3298 0.3461 -0.0705 -0.0077 0.0530  56  TRP A N   
445  C CA  . TRP A 57  ? 0.2695 0.3582 0.3668 -0.0674 -0.0109 0.0471  56  TRP A CA  
446  C C   . TRP A 57  ? 0.2745 0.3873 0.3852 -0.0657 -0.0057 0.0545  56  TRP A C   
447  O O   . TRP A 57  ? 0.3129 0.4356 0.4406 -0.0730 -0.0026 0.0632  56  TRP A O   
448  C CB  . TRP A 57  ? 0.2572 0.3398 0.3610 -0.0737 -0.0199 0.0407  56  TRP A CB  
449  C CG  . TRP A 57  ? 0.2659 0.3286 0.3537 -0.0718 -0.0244 0.0318  56  TRP A CG  
450  C CD1 . TRP A 57  ? 0.2560 0.3017 0.3413 -0.0767 -0.0275 0.0281  56  TRP A CD1 
451  C CD2 . TRP A 57  ? 0.2641 0.3217 0.3372 -0.0639 -0.0249 0.0262  56  TRP A CD2 
452  N NE1 . TRP A 57  ? 0.3068 0.3403 0.3765 -0.0721 -0.0296 0.0206  56  TRP A NE1 
453  C CE2 . TRP A 57  ? 0.2957 0.3356 0.3581 -0.0649 -0.0277 0.0201  56  TRP A CE2 
454  C CE3 . TRP A 57  ? 0.2696 0.3343 0.3379 -0.0555 -0.0220 0.0262  56  TRP A CE3 
455  C CZ2 . TRP A 57  ? 0.3010 0.3315 0.3489 -0.0590 -0.0269 0.0156  56  TRP A CZ2 
456  C CZ3 . TRP A 57  ? 0.2726 0.3243 0.3264 -0.0496 -0.0216 0.0215  56  TRP A CZ3 
457  C CH2 . TRP A 57  ? 0.2775 0.3131 0.3218 -0.0520 -0.0237 0.0170  56  TRP A CH2 
458  N N   . THR A 58  ? 0.2435 0.3652 0.3475 -0.0560 -0.0035 0.0513  57  THR A N   
459  C CA  . THR A 58  ? 0.2581 0.4045 0.3755 -0.0518 0.0008  0.0563  57  THR A CA  
460  C C   . THR A 58  ? 0.2645 0.4138 0.3824 -0.0460 -0.0051 0.0501  57  THR A C   
461  O O   . THR A 58  ? 0.2503 0.3811 0.3548 -0.0442 -0.0105 0.0429  57  THR A O   
462  C CB  . THR A 58  ? 0.2677 0.4232 0.3748 -0.0416 0.0108  0.0590  57  THR A CB  
463  O OG1 . THR A 58  ? 0.3158 0.4526 0.4008 -0.0352 0.0100  0.0495  57  THR A OG1 
464  C CG2 . THR A 58  ? 0.2420 0.4055 0.3530 -0.0455 0.0182  0.0701  57  THR A CG2 
465  N N   . LYS A 59  ? 0.2845 0.4589 0.4184 -0.0419 -0.0034 0.0542  58  LYS A N   
466  C CA  . LYS A 59  ? 0.2525 0.4336 0.3873 -0.0328 -0.0084 0.0506  58  LYS A CA  
467  C C   . LYS A 59  ? 0.2431 0.4422 0.3807 -0.0193 0.0004  0.0537  58  LYS A C   
468  O O   . LYS A 59  ? 0.3086 0.5298 0.4606 -0.0206 0.0078  0.0608  58  LYS A O   
469  C CB  . LYS A 59  ? 0.2868 0.4852 0.4426 -0.0407 -0.0186 0.0508  58  LYS A CB  
470  C CG  . LYS A 59  ? 0.2797 0.4916 0.4375 -0.0291 -0.0250 0.0489  58  LYS A CG  
471  C CD  . LYS A 59  ? 0.2917 0.5266 0.4723 -0.0382 -0.0371 0.0474  58  LYS A CD  
472  C CE  . LYS A 59  ? 0.3086 0.5521 0.4838 -0.0258 -0.0469 0.0445  58  LYS A CE  
473  N NZ  . LYS A 59  ? 0.3089 0.5818 0.5073 -0.0329 -0.0606 0.0412  58  LYS A NZ  
474  N N   . LEU A 60  ? 0.2580 0.4460 0.3812 -0.0057 0.0011  0.0491  59  LEU A N   
475  C CA  . LEU A 60  ? 0.2856 0.4867 0.4099 0.0098  0.0094  0.0503  59  LEU A CA  
476  C C   . LEU A 60  ? 0.2972 0.5310 0.4455 0.0147  0.0060  0.0560  59  LEU A C   
477  O O   . LEU A 60  ? 0.2830 0.5213 0.4386 0.0109  -0.0052 0.0557  59  LEU A O   
478  C CB  . LEU A 60  ? 0.2776 0.4512 0.3802 0.0222  0.0117  0.0433  59  LEU A CB  
479  C CG  . LEU A 60  ? 0.3096 0.4559 0.3916 0.0191  0.0162  0.0356  59  LEU A CG  
480  C CD1 . LEU A 60  ? 0.2702 0.3906 0.3360 0.0308  0.0202  0.0282  59  LEU A CD1 
481  C CD2 . LEU A 60  ? 0.3193 0.4799 0.4014 0.0181  0.0242  0.0365  59  LEU A CD2 
482  N N   . PRO A 61  ? 0.3186 0.5784 0.4796 0.0236  0.0152  0.0606  60  PRO A N   
483  C CA  . PRO A 61  ? 0.3021 0.5995 0.4904 0.0290  0.0125  0.0663  60  PRO A CA  
484  C C   . PRO A 61  ? 0.2962 0.5892 0.4771 0.0474  0.0085  0.0643  60  PRO A C   
485  O O   . PRO A 61  ? 0.2866 0.5476 0.4425 0.0579  0.0124  0.0593  60  PRO A O   
486  C CB  . PRO A 61  ? 0.2346 0.5581 0.4345 0.0351  0.0269  0.0721  60  PRO A CB  
487  C CG  . PRO A 61  ? 0.2384 0.5326 0.4081 0.0441  0.0360  0.0657  60  PRO A CG  
488  C CD  . PRO A 61  ? 0.3184 0.5785 0.4699 0.0296  0.0286  0.0606  60  PRO A CD  
489  N N   . PRO A 62  ? 0.2892 0.6148 0.4929 0.0523  0.0010  0.0685  61  PRO A N   
490  C CA  . PRO A 62  ? 0.3200 0.6433 0.5165 0.0721  -0.0035 0.0690  61  PRO A CA  
491  C C   . PRO A 62  ? 0.3167 0.6277 0.5004 0.0937  0.0102  0.0688  61  PRO A C   
492  O O   . PRO A 62  ? 0.3443 0.6687 0.5347 0.0971  0.0222  0.0694  61  PRO A O   
493  C CB  . PRO A 62  ? 0.2460 0.6192 0.4763 0.0734  -0.0126 0.0741  61  PRO A CB  
494  C CG  . PRO A 62  ? 0.2311 0.6203 0.4819 0.0481  -0.0177 0.0733  61  PRO A CG  
495  C CD  . PRO A 62  ? 0.2263 0.5927 0.4648 0.0388  -0.0044 0.0730  61  PRO A CD  
496  N N   . VAL A 63  ? 0.3697 0.6529 0.5334 0.1087  0.0090  0.0679  62  VAL A N   
497  C CA  . VAL A 63  ? 0.3809 0.6483 0.5333 0.1308  0.0212  0.0668  62  VAL A CA  
498  C C   . VAL A 63  ? 0.3977 0.7073 0.5742 0.1496  0.0231  0.0738  62  VAL A C   
499  O O   . VAL A 63  ? 0.3681 0.7038 0.5594 0.1546  0.0117  0.0801  62  VAL A O   
500  C CB  . VAL A 63  ? 0.3797 0.6031 0.5064 0.1405  0.0201  0.0659  62  VAL A CB  
501  C CG1 . VAL A 63  ? 0.3906 0.5926 0.5070 0.1635  0.0333  0.0640  62  VAL A CG1 
502  C CG2 . VAL A 63  ? 0.3761 0.5635 0.4833 0.1211  0.0183  0.0593  62  VAL A CG2 
503  N N   . LYS A 64  ? 0.4894 0.8076 0.6695 0.1614  0.0372  0.0721  63  LYS A N   
504  C CA  . LYS A 64  ? 0.4461 0.8049 0.6496 0.1819  0.0419  0.0784  63  LYS A CA  
505  C C   . LYS A 64  ? 0.4937 0.8261 0.6813 0.2104  0.0490  0.0780  63  LYS A C   
506  O O   . LYS A 64  ? 0.5058 0.7877 0.6652 0.2131  0.0546  0.0708  63  LYS A O   
507  C CB  . LYS A 64  ? 0.4860 0.8741 0.7040 0.1801  0.0554  0.0779  63  LYS A CB  
508  C CG  . LYS A 64  ? 0.5403 0.9787 0.7927 0.1620  0.0502  0.0851  63  LYS A CG  
509  C CD  . LYS A 64  ? 0.5880 1.0224 0.8358 0.1429  0.0587  0.0831  63  LYS A CD  
510  C CE  . LYS A 64  ? 0.6128 1.0401 0.8449 0.1589  0.0772  0.0788  63  LYS A CE  
511  N NZ  . LYS A 64  ? 0.7115 1.1364 0.9353 0.1427  0.0853  0.0781  63  LYS A NZ  
512  N N   . SER A 65  ? 0.5576 0.9256 0.7659 0.2319  0.0490  0.0858  64  SER A N   
513  C CA  . SER A 65  ? 0.5883 0.9333 0.7844 0.2623  0.0570  0.0871  64  SER A CA  
514  C C   . SER A 65  ? 0.6620 0.9850 0.8448 0.2717  0.0756  0.0769  64  SER A C   
515  O O   . SER A 65  ? 0.6492 1.0062 0.8470 0.2698  0.0841  0.0752  64  SER A O   
516  C CB  . SER A 65  ? 0.6536 1.0485 0.8778 0.2846  0.0527  0.0982  64  SER A CB  
517  O OG  . SER A 65  ? 0.7836 1.1503 0.9928 0.3120  0.0540  0.1034  64  SER A OG  
518  N N   . ALA A 66  ? 0.7561 1.0218 0.9103 0.2812  0.0824  0.0697  65  ALA A N   
519  C CA  . ALA A 66  ? 0.8258 1.0662 0.9644 0.2901  0.0988  0.0562  65  ALA A CA  
520  C C   . ALA A 66  ? 0.8685 1.1390 1.0224 0.3196  0.1106  0.0586  65  ALA A C   
521  O O   . ALA A 66  ? 0.8717 1.1596 1.0272 0.3225  0.1225  0.0510  65  ALA A O   
522  C CB  . ALA A 66  ? 0.8073 0.9791 0.9163 0.2930  0.1027  0.0472  65  ALA A CB  
523  N N   . ILE A 67  ? 0.9186 1.1977 1.0831 0.3432  0.1079  0.0698  66  ILE A N   
524  C CA  . ILE A 67  ? 0.9053 1.2073 1.0814 0.3612  0.1137  0.0721  66  ILE A CA  
525  C C   . ILE A 67  ? 0.9078 1.2611 1.1118 0.3601  0.0994  0.0871  66  ILE A C   
526  O O   . ILE A 67  ? 0.8445 1.1962 1.0488 0.3546  0.0852  0.0954  66  ILE A O   
527  C CB  . ILE A 67  ? 0.9166 1.1660 1.0716 0.3848  0.1225  0.0676  66  ILE A CB  
528  C CG1 . ILE A 67  ? 0.9522 1.2279 1.1207 0.4052  0.1285  0.0707  66  ILE A CG1 
529  C CG2 . ILE A 67  ? 0.9120 1.1270 1.0560 0.3891  0.1132  0.0776  66  ILE A CG2 
530  C CD1 . ILE A 67  ? 0.8800 1.1773 1.0522 0.4057  0.1418  0.0598  66  ILE A CD1 
531  N N   . ARG A 68  ? 0.9335 1.3330 1.1602 0.3646  0.1029  0.0896  67  ARG A N   
532  C CA  . ARG A 68  ? 0.8606 1.3093 1.1154 0.3648  0.0898  0.1013  67  ARG A CA  
533  C C   . ARG A 68  ? 0.8956 1.3208 1.1392 0.3846  0.0823  0.1089  67  ARG A C   
534  O O   . ARG A 68  ? 0.8446 1.2279 1.0682 0.4054  0.0925  0.1064  67  ARG A O   
535  C CB  . ARG A 68  ? 0.7560 1.2499 1.0348 0.3713  0.0984  0.1020  67  ARG A CB  
536  N N   . GLY A 69  ? 0.9355 1.3851 1.1903 0.3770  0.0642  0.1177  68  GLY A N   
537  C CA  . GLY A 69  ? 0.9355 1.3689 1.1789 0.3945  0.0555  0.1269  68  GLY A CA  
538  C C   . GLY A 69  ? 1.0159 1.3969 1.2293 0.3918  0.0514  0.1289  68  GLY A C   
539  O O   . GLY A 69  ? 1.0214 1.3999 1.2272 0.3982  0.0394  0.1384  68  GLY A O   
540  N N   . GLN A 70  ? 0.7427 1.2386 1.2731 0.2327  0.0443  0.0700  69  GLN A N   
541  C CA  . GLN A 70  ? 0.7008 1.1674 1.1921 0.2308  0.0307  0.0729  69  GLN A CA  
542  C C   . GLN A 70  ? 0.6540 1.1391 1.1446 0.2061  0.0189  0.0692  69  GLN A C   
543  O O   . GLN A 70  ? 0.6437 1.1482 1.1531 0.1904  0.0291  0.0631  69  GLN A O   
544  C CB  . GLN A 70  ? 0.6773 1.0900 1.1263 0.2394  0.0499  0.0700  69  GLN A CB  
545  N N   . ALA A 71  ? 0.5851 1.0576 1.0492 0.1998  -0.0025 0.0711  70  ALA A N   
546  C CA  . ALA A 71  ? 0.4640 0.9354 0.9129 0.1716  -0.0125 0.0628  70  ALA A CA  
547  C C   . ALA A 71  ? 0.4863 0.9082 0.8929 0.1607  0.0033  0.0542  70  ALA A C   
548  O O   . ALA A 71  ? 0.5500 0.9336 0.9289 0.1736  0.0141  0.0548  70  ALA A O   
549  C CB  . ALA A 71  ? 0.3936 0.8642 0.8237 0.1667  -0.0392 0.0662  70  ALA A CB  
550  N N   . PRO A 72  ? 0.4273 0.8495 0.8292 0.1370  0.0050  0.0463  71  PRO A N   
551  C CA  . PRO A 72  ? 0.4210 0.7974 0.7812 0.1268  0.0155  0.0399  71  PRO A CA  
552  C C   . PRO A 72  ? 0.3819 0.7219 0.7017 0.1292  0.0031  0.0411  71  PRO A C   
553  O O   . PRO A 72  ? 0.3706 0.7207 0.6895 0.1280  -0.0161 0.0443  71  PRO A O   
554  C CB  . PRO A 72  ? 0.3817 0.7703 0.7490 0.1016  0.0149  0.0334  71  PRO A CB  
555  C CG  . PRO A 72  ? 0.3480 0.7887 0.7656 0.0993  0.0134  0.0348  71  PRO A CG  
556  C CD  . PRO A 72  ? 0.3742 0.8383 0.8103 0.1186  -0.0010 0.0429  71  PRO A CD  
557  N N   . VAL A 73  ? 0.3629 0.6610 0.6489 0.1323  0.0145  0.0386  72  VAL A N   
558  C CA  . VAL A 73  ? 0.3801 0.6410 0.6277 0.1323  0.0061  0.0387  72  VAL A CA  
559  C C   . VAL A 73  ? 0.3703 0.6170 0.5984 0.1106  0.0034  0.0328  72  VAL A C   
560  O O   . VAL A 73  ? 0.3458 0.5766 0.5625 0.1033  0.0160  0.0285  72  VAL A O   
561  C CB  . VAL A 73  ? 0.4209 0.6451 0.6439 0.1456  0.0192  0.0384  72  VAL A CB  
562  C CG1 . VAL A 73  ? 0.3673 0.5543 0.5534 0.1432  0.0112  0.0382  72  VAL A CG1 
563  C CG2 . VAL A 73  ? 0.3326 0.5685 0.5764 0.1684  0.0250  0.0442  72  VAL A CG2 
564  N N   . VAL A 74  ? 0.3328 0.5849 0.5561 0.1011  -0.0126 0.0329  73  VAL A N   
565  C CA  . VAL A 74  ? 0.3161 0.5553 0.5230 0.0814  -0.0151 0.0274  73  VAL A CA  
566  C C   . VAL A 74  ? 0.3319 0.5739 0.5293 0.0766  -0.0332 0.0285  73  VAL A C   
567  O O   . VAL A 74  ? 0.3351 0.6065 0.5520 0.0812  -0.0450 0.0321  73  VAL A O   
568  C CB  . VAL A 74  ? 0.3186 0.5797 0.5484 0.0672  -0.0074 0.0229  73  VAL A CB  
569  C CG1 . VAL A 74  ? 0.2992 0.6051 0.5668 0.0672  -0.0151 0.0243  73  VAL A CG1 
570  C CG2 . VAL A 74  ? 0.2635 0.5091 0.4774 0.0477  -0.0085 0.0176  73  VAL A CG2 
571  N N   . PRO A 75  ? 0.3185 0.5319 0.4865 0.0678  -0.0360 0.0261  74  PRO A N   
572  C CA  . PRO A 75  ? 0.3417 0.5561 0.4970 0.0622  -0.0515 0.0267  74  PRO A CA  
573  C C   . PRO A 75  ? 0.3345 0.5778 0.5077 0.0462  -0.0588 0.0214  74  PRO A C   
574  O O   . PRO A 75  ? 0.2999 0.5500 0.4867 0.0341  -0.0496 0.0157  74  PRO A O   
575  C CB  . PRO A 75  ? 0.3309 0.5074 0.4535 0.0549  -0.0475 0.0240  74  PRO A CB  
576  C CG  . PRO A 75  ? 0.3083 0.4706 0.4310 0.0532  -0.0325 0.0214  74  PRO A CG  
577  C CD  . PRO A 75  ? 0.3156 0.4951 0.4602 0.0640  -0.0252 0.0235  74  PRO A CD  
578  N N   . TYR A 76  ? 0.3439 0.6040 0.5163 0.0456  -0.0758 0.0234  75  TYR A N   
579  C CA  . TYR A 76  ? 0.3427 0.6284 0.5283 0.0274  -0.0844 0.0165  75  TYR A CA  
580  C C   . TYR A 76  ? 0.3522 0.6104 0.5126 0.0084  -0.0795 0.0077  75  TYR A C   
581  O O   . TYR A 76  ? 0.3107 0.5349 0.4408 0.0103  -0.0761 0.0086  75  TYR A O   
582  C CB  . TYR A 76  ? 0.3693 0.6827 0.5591 0.0310  -0.1060 0.0209  75  TYR A CB  
583  C CG  . TYR A 76  ? 0.4732 0.7637 0.6263 0.0368  -0.1174 0.0260  75  TYR A CG  
584  C CD1 . TYR A 76  ? 0.4813 0.7450 0.6010 0.0213  -0.1180 0.0192  75  TYR A CD1 
585  C CD2 . TYR A 76  ? 0.5203 0.8164 0.6724 0.0578  -0.1268 0.0382  75  TYR A CD2 
586  C CE1 . TYR A 76  ? 0.5323 0.7749 0.6172 0.0260  -0.1269 0.0242  75  TYR A CE1 
587  C CE2 . TYR A 76  ? 0.5594 0.8333 0.6763 0.0629  -0.1365 0.0441  75  TYR A CE2 
588  C CZ  . TYR A 76  ? 0.6303 0.8778 0.7132 0.0463  -0.1364 0.0369  75  TYR A CZ  
589  O OH  . TYR A 76  ? 0.6716 0.8957 0.7179 0.0508  -0.1439 0.0430  75  TYR A OH  
590  N N   . MET A 77  ? 0.3295 0.6026 0.5051 -0.0100 -0.0775 -0.0009 76  MET A N   
591  C CA  . MET A 77  ? 0.3003 0.5491 0.4563 -0.0284 -0.0712 -0.0099 76  MET A CA  
592  C C   . MET A 77  ? 0.3613 0.5892 0.4817 -0.0306 -0.0811 -0.0108 76  MET A C   
593  O O   . MET A 77  ? 0.3681 0.6136 0.4837 -0.0297 -0.0985 -0.0092 76  MET A O   
594  C CB  . MET A 77  ? 0.2916 0.5641 0.4693 -0.0485 -0.0720 -0.0193 76  MET A CB  
595  C CG  . MET A 77  ? 0.3485 0.5941 0.5061 -0.0679 -0.0645 -0.0295 76  MET A CG  
596  S SD  . MET A 77  ? 0.3003 0.5083 0.4500 -0.0626 -0.0406 -0.0264 76  MET A SD  
597  C CE  . MET A 77  ? 0.2925 0.5178 0.4759 -0.0741 -0.0273 -0.0300 76  MET A CE  
598  N N   . ARG A 78  ? 0.3451 0.5362 0.4408 -0.0332 -0.0698 -0.0126 77  ARG A N   
599  C CA  . ARG A 78  ? 0.3474 0.5143 0.4084 -0.0327 -0.0750 -0.0119 77  ARG A CA  
600  C C   . ARG A 78  ? 0.3819 0.5151 0.4251 -0.0428 -0.0599 -0.0178 77  ARG A C   
601  O O   . ARG A 78  ? 0.3245 0.4511 0.3814 -0.0462 -0.0459 -0.0198 77  ARG A O   
602  C CB  . ARG A 78  ? 0.3651 0.5225 0.4163 -0.0125 -0.0779 -0.0007 77  ARG A CB  
603  C CG  . ARG A 78  ? 0.3500 0.4906 0.4075 -0.0034 -0.0629 0.0029  77  ARG A CG  
604  C CD  . ARG A 78  ? 0.3447 0.4733 0.3909 0.0142  -0.0653 0.0121  77  ARG A CD  
605  N NE  . ARG A 78  ? 0.3759 0.5315 0.4401 0.0271  -0.0753 0.0184  77  ARG A NE  
606  C CZ  . ARG A 78  ? 0.3940 0.5428 0.4529 0.0444  -0.0778 0.0272  77  ARG A CZ  
607  N NH1 . ARG A 78  ? 0.3707 0.4864 0.4057 0.0493  -0.0717 0.0302  77  ARG A NH1 
608  N NH2 . ARG A 78  ? 0.3788 0.5543 0.4585 0.0571  -0.0855 0.0333  77  ARG A NH2 
609  N N   . TYR A 79  ? 0.3783 0.4898 0.3903 -0.0466 -0.0622 -0.0197 78  TYR A N   
610  C CA  . TYR A 79  ? 0.3630 0.4419 0.3569 -0.0543 -0.0476 -0.0245 78  TYR A CA  
611  C C   . TYR A 79  ? 0.3921 0.4482 0.3573 -0.0461 -0.0484 -0.0188 78  TYR A C   
612  O O   . TYR A 79  ? 0.4047 0.4686 0.3596 -0.0373 -0.0615 -0.0125 78  TYR A O   
613  C CB  . TYR A 79  ? 0.3896 0.4645 0.3746 -0.0744 -0.0458 -0.0371 78  TYR A CB  
614  C CG  . TYR A 79  ? 0.4217 0.5122 0.3906 -0.0816 -0.0642 -0.0411 78  TYR A CG  
615  C CD1 . TYR A 79  ? 0.4390 0.5119 0.3722 -0.0804 -0.0697 -0.0397 78  TYR A CD1 
616  C CD2 . TYR A 79  ? 0.4220 0.5461 0.4115 -0.0902 -0.0764 -0.0457 78  TYR A CD2 
617  C CE1 . TYR A 79  ? 0.4890 0.5765 0.4037 -0.0867 -0.0883 -0.0424 78  TYR A CE1 
618  C CE2 . TYR A 79  ? 0.4238 0.5658 0.3991 -0.0972 -0.0959 -0.0489 78  TYR A CE2 
619  C CZ  . TYR A 79  ? 0.5026 0.6257 0.4388 -0.0950 -0.1024 -0.0469 78  TYR A CZ  
620  O OH  . TYR A 79  ? 0.5923 0.7329 0.5104 -0.1015 -0.1232 -0.0490 78  TYR A OH  
621  N N   . GLY A 80  ? 0.3712 0.3990 0.3252 -0.0482 -0.0335 -0.0201 79  GLY A N   
622  C CA  . GLY A 80  ? 0.3733 0.3784 0.3031 -0.0417 -0.0312 -0.0148 79  GLY A CA  
623  C C   . GLY A 80  ? 0.3607 0.3660 0.2985 -0.0258 -0.0323 -0.0045 79  GLY A C   
624  O O   . GLY A 80  ? 0.3917 0.3792 0.3103 -0.0202 -0.0313 0.0007  79  GLY A O   
625  N N   . HIS A 81  ? 0.3654 0.3883 0.3293 -0.0192 -0.0332 -0.0018 80  HIS A N   
626  C CA  . HIS A 81  ? 0.3791 0.3999 0.3500 -0.0053 -0.0326 0.0060  80  HIS A CA  
627  C C   . HIS A 81  ? 0.3706 0.3727 0.3441 -0.0060 -0.0190 0.0063  80  HIS A C   
628  O O   . HIS A 81  ? 0.3377 0.3311 0.3118 -0.0153 -0.0097 0.0017  80  HIS A O   
629  C CB  . HIS A 81  ? 0.3437 0.3902 0.3400 0.0015  -0.0372 0.0077  80  HIS A CB  
630  C CG  . HIS A 81  ? 0.3350 0.3915 0.3515 -0.0068 -0.0295 0.0025  80  HIS A CG  
631  N ND1 . HIS A 81  ? 0.3214 0.3863 0.3413 -0.0202 -0.0300 -0.0048 80  HIS A ND1 
632  C CD2 . HIS A 81  ? 0.2963 0.3533 0.3281 -0.0042 -0.0205 0.0037  80  HIS A CD2 
633  C CE1 . HIS A 81  ? 0.2995 0.3685 0.3376 -0.0249 -0.0205 -0.0071 80  HIS A CE1 
634  N NE2 . HIS A 81  ? 0.3066 0.3717 0.3515 -0.0148 -0.0151 -0.0013 80  HIS A NE2 
635  N N   . SER A 82  ? 0.3408 0.3370 0.3167 0.0040  -0.0178 0.0118  81  SER A N   
636  C CA  . SER A 82  ? 0.3188 0.3028 0.3002 0.0035  -0.0079 0.0126  81  SER A CA  
637  C C   . SER A 82  ? 0.3574 0.3519 0.3547 0.0107  -0.0079 0.0146  81  SER A C   
638  O O   . SER A 82  ? 0.4169 0.4214 0.4172 0.0190  -0.0141 0.0166  81  SER A O   
639  C CB  . SER A 82  ? 0.3531 0.3155 0.3182 0.0054  -0.0049 0.0158  81  SER A CB  
640  O OG  . SER A 82  ? 0.3971 0.3567 0.3564 0.0156  -0.0107 0.0204  81  SER A OG  
641  N N   . THR A 83  ? 0.3406 0.3328 0.3475 0.0079  -0.0007 0.0143  82  THR A N   
642  C CA  . THR A 83  ? 0.3258 0.3243 0.3423 0.0135  0.0001  0.0160  82  THR A CA  
643  C C   . THR A 83  ? 0.3690 0.3555 0.3842 0.0121  0.0044  0.0176  82  THR A C   
644  O O   . THR A 83  ? 0.3321 0.3144 0.3512 0.0060  0.0097  0.0178  82  THR A O   
645  C CB  . THR A 83  ? 0.3257 0.3396 0.3576 0.0108  0.0034  0.0151  82  THR A CB  
646  O OG1 . THR A 83  ? 0.3160 0.3248 0.3519 0.0026  0.0100  0.0142  82  THR A OG1 
647  C CG2 . THR A 83  ? 0.2717 0.3021 0.3099 0.0113  -0.0014 0.0131  82  THR A CG2 
648  N N   . VAL A 84  ? 0.3783 0.3599 0.3890 0.0175  0.0024  0.0185  83  VAL A N   
649  C CA  . VAL A 84  ? 0.3492 0.3240 0.3605 0.0150  0.0043  0.0192  83  VAL A CA  
650  C C   . VAL A 84  ? 0.3552 0.3361 0.3675 0.0194  0.0031  0.0188  83  VAL A C   
651  O O   . VAL A 84  ? 0.3682 0.3542 0.3790 0.0258  0.0021  0.0178  83  VAL A O   
652  C CB  . VAL A 84  ? 0.3571 0.3146 0.3574 0.0140  0.0040  0.0190  83  VAL A CB  
653  C CG1 . VAL A 84  ? 0.3762 0.3258 0.3719 0.0097  0.0069  0.0197  83  VAL A CG1 
654  C CG2 . VAL A 84  ? 0.3695 0.3192 0.3585 0.0218  0.0010  0.0182  83  VAL A CG2 
655  N N   . LEU A 85  ? 0.3099 0.2912 0.3246 0.0160  0.0032  0.0197  84  LEU A N   
656  C CA  . LEU A 85  ? 0.3381 0.3230 0.3487 0.0186  0.0020  0.0191  84  LEU A CA  
657  C C   . LEU A 85  ? 0.3868 0.3596 0.3868 0.0163  -0.0011 0.0161  84  LEU A C   
658  O O   . LEU A 85  ? 0.4169 0.3873 0.4212 0.0098  -0.0026 0.0169  84  LEU A O   
659  C CB  . LEU A 85  ? 0.3241 0.3206 0.3439 0.0162  0.0033  0.0235  84  LEU A CB  
660  C CG  . LEU A 85  ? 0.3618 0.3613 0.3731 0.0181  0.0018  0.0238  84  LEU A CG  
661  C CD1 . LEU A 85  ? 0.3291 0.3316 0.3357 0.0244  0.0059  0.0217  84  LEU A CD1 
662  C CD2 . LEU A 85  ? 0.2831 0.2921 0.3021 0.0160  0.0018  0.0305  84  LEU A CD2 
663  N N   . ILE A 86  ? 0.3877 0.3527 0.3751 0.0209  -0.0011 0.0120  85  ILE A N   
664  C CA  . ILE A 86  ? 0.4314 0.3828 0.4060 0.0170  -0.0034 0.0072  85  ILE A CA  
665  C C   . ILE A 86  ? 0.4684 0.4213 0.4316 0.0201  -0.0027 0.0042  85  ILE A C   
666  O O   . ILE A 86  ? 0.4411 0.3915 0.3992 0.0284  0.0021  0.0025  85  ILE A O   
667  C CB  . ILE A 86  ? 0.4517 0.3826 0.4165 0.0192  -0.0015 0.0039  85  ILE A CB  
668  C CG1 . ILE A 86  ? 0.3990 0.3270 0.3714 0.0158  -0.0010 0.0076  85  ILE A CG1 
669  C CG2 . ILE A 86  ? 0.3829 0.2970 0.3333 0.0134  -0.0025 -0.0027 85  ILE A CG2 
670  C CD1 . ILE A 86  ? 0.3386 0.2452 0.2996 0.0193  0.0016  0.0068  85  ILE A CD1 
671  N N   . ASP A 87  ? 0.4530 0.4113 0.4125 0.0137  -0.0074 0.0042  86  ASP A N   
672  C CA  . ASP A 87  ? 0.4393 0.3987 0.3837 0.0153  -0.0069 0.0019  86  ASP A CA  
673  C C   . ASP A 87  ? 0.4182 0.3898 0.3686 0.0228  -0.0008 0.0067  86  ASP A C   
674  O O   . ASP A 87  ? 0.4307 0.4163 0.3945 0.0216  -0.0015 0.0139  86  ASP A O   
675  C CB  . ASP A 87  ? 0.4821 0.4203 0.4058 0.0164  -0.0040 -0.0075 86  ASP A CB  
676  C CG  . ASP A 87  ? 0.5421 0.4697 0.4573 0.0053  -0.0107 -0.0132 86  ASP A CG  
677  O OD1 . ASP A 87  ? 0.5598 0.5011 0.4791 -0.0023 -0.0188 -0.0102 86  ASP A OD1 
678  O OD2 . ASP A 87  ? 0.5547 0.4615 0.4612 0.0038  -0.0080 -0.0197 86  ASP A OD2 
679  N N   . ASP A 88  ? 0.3828 0.3490 0.3250 0.0304  0.0065  0.0030  87  ASP A N   
680  C CA  . ASP A 88  ? 0.3885 0.3677 0.3382 0.0364  0.0136  0.0070  87  ASP A CA  
681  C C   . ASP A 88  ? 0.4104 0.3962 0.3780 0.0424  0.0172  0.0084  87  ASP A C   
682  O O   . ASP A 88  ? 0.4054 0.4020 0.3811 0.0477  0.0240  0.0099  87  ASP A O   
683  C CB  . ASP A 88  ? 0.4029 0.3756 0.3334 0.0407  0.0208  0.0027  87  ASP A CB  
684  C CG  . ASP A 88  ? 0.4175 0.3881 0.3283 0.0344  0.0166  0.0029  87  ASP A CG  
685  O OD1 . ASP A 88  ? 0.3671 0.3504 0.2851 0.0310  0.0130  0.0110  87  ASP A OD1 
686  O OD2 . ASP A 88  ? 0.4754 0.4306 0.3622 0.0329  0.0169  -0.0049 87  ASP A OD2 
687  N N   . THR A 89  ? 0.3942 0.3745 0.3676 0.0413  0.0127  0.0080  88  THR A N   
688  C CA  . THR A 89  ? 0.3889 0.3729 0.3733 0.0479  0.0139  0.0088  88  THR A CA  
689  C C   . THR A 89  ? 0.3628 0.3527 0.3592 0.0425  0.0092  0.0124  88  THR A C   
690  O O   . THR A 89  ? 0.3970 0.3768 0.3891 0.0369  0.0055  0.0123  88  THR A O   
691  C CB  . THR A 89  ? 0.4063 0.3719 0.3795 0.0542  0.0147  0.0049  88  THR A CB  
692  O OG1 . THR A 89  ? 0.4484 0.4057 0.4087 0.0593  0.0213  0.0002  88  THR A OG1 
693  C CG2 . THR A 89  ? 0.3279 0.2994 0.3126 0.0626  0.0143  0.0079  88  THR A CG2 
694  N N   . VAL A 90  ? 0.3394 0.3452 0.3506 0.0433  0.0104  0.0149  89  VAL A N   
695  C CA  . VAL A 90  ? 0.3584 0.3672 0.3771 0.0392  0.0066  0.0165  89  VAL A CA  
696  C C   . VAL A 90  ? 0.3679 0.3716 0.3831 0.0462  0.0033  0.0163  89  VAL A C   
697  O O   . VAL A 90  ? 0.3476 0.3590 0.3676 0.0549  0.0044  0.0163  89  VAL A O   
698  C CB  . VAL A 90  ? 0.3557 0.3821 0.3899 0.0354  0.0089  0.0180  89  VAL A CB  
699  C CG1 . VAL A 90  ? 0.2771 0.3048 0.3151 0.0304  0.0051  0.0178  89  VAL A CG1 
700  C CG2 . VAL A 90  ? 0.3334 0.3616 0.3701 0.0299  0.0133  0.0204  89  VAL A CG2 
701  N N   . LEU A 91  ? 0.3603 0.3510 0.3674 0.0433  -0.0001 0.0169  90  LEU A N   
702  C CA  . LEU A 91  ? 0.3601 0.3458 0.3622 0.0496  -0.0039 0.0188  90  LEU A CA  
703  C C   . LEU A 91  ? 0.3523 0.3492 0.3600 0.0445  -0.0079 0.0201  90  LEU A C   
704  O O   . LEU A 91  ? 0.3950 0.3856 0.3993 0.0355  -0.0069 0.0195  90  LEU A O   
705  C CB  . LEU A 91  ? 0.3643 0.3251 0.3503 0.0495  -0.0037 0.0191  90  LEU A CB  
706  C CG  . LEU A 91  ? 0.4012 0.3495 0.3800 0.0535  0.0003  0.0159  90  LEU A CG  
707  C CD1 . LEU A 91  ? 0.3719 0.2955 0.3367 0.0486  0.0015  0.0145  90  LEU A CD1 
708  C CD2 . LEU A 91  ? 0.3450 0.2953 0.3251 0.0674  0.0020  0.0168  90  LEU A CD2 
709  N N   . LEU A 92  ? 0.3288 0.3427 0.3452 0.0497  -0.0122 0.0214  91  LEU A N   
710  C CA  . LEU A 92  ? 0.3498 0.3757 0.3697 0.0436  -0.0176 0.0213  91  LEU A CA  
711  C C   . LEU A 92  ? 0.3795 0.4010 0.3882 0.0505  -0.0254 0.0254  91  LEU A C   
712  O O   . LEU A 92  ? 0.3613 0.3880 0.3737 0.0627  -0.0282 0.0291  91  LEU A O   
713  C CB  . LEU A 92  ? 0.3204 0.3729 0.3608 0.0419  -0.0180 0.0195  91  LEU A CB  
714  C CG  . LEU A 92  ? 0.3424 0.4080 0.3867 0.0322  -0.0235 0.0171  91  LEU A CG  
715  C CD1 . LEU A 92  ? 0.2884 0.3683 0.3499 0.0232  -0.0176 0.0133  91  LEU A CD1 
716  C CD2 . LEU A 92  ? 0.3181 0.4011 0.3664 0.0388  -0.0346 0.0198  91  LEU A CD2 
717  N N   . TRP A 93  ? 0.3999 0.4112 0.3940 0.0434  -0.0280 0.0255  92  TRP A N   
718  C CA  . TRP A 93  ? 0.3793 0.3838 0.3578 0.0498  -0.0356 0.0309  92  TRP A CA  
719  C C   . TRP A 93  ? 0.4174 0.4242 0.3845 0.0397  -0.0406 0.0290  92  TRP A C   
720  O O   . TRP A 93  ? 0.3968 0.3975 0.3617 0.0276  -0.0345 0.0236  92  TRP A O   
721  C CB  . TRP A 93  ? 0.3966 0.3712 0.3569 0.0543  -0.0306 0.0345  92  TRP A CB  
722  C CG  . TRP A 93  ? 0.4353 0.3998 0.3782 0.0632  -0.0370 0.0422  92  TRP A CG  
723  C CD1 . TRP A 93  ? 0.4459 0.4116 0.3906 0.0786  -0.0410 0.0488  92  TRP A CD1 
724  C CD2 . TRP A 93  ? 0.4498 0.3999 0.3693 0.0582  -0.0393 0.0451  92  TRP A CD2 
725  N NE1 . TRP A 93  ? 0.4383 0.3917 0.3625 0.0842  -0.0468 0.0569  92  TRP A NE1 
726  C CE2 . TRP A 93  ? 0.4558 0.3991 0.3625 0.0713  -0.0460 0.0546  92  TRP A CE2 
727  C CE3 . TRP A 93  ? 0.4266 0.3677 0.3339 0.0447  -0.0352 0.0409  92  TRP A CE3 
728  C CZ2 . TRP A 93  ? 0.4920 0.4196 0.3714 0.0706  -0.0495 0.0606  92  TRP A CZ2 
729  C CZ3 . TRP A 93  ? 0.4686 0.3940 0.3489 0.0434  -0.0374 0.0455  92  TRP A CZ3 
730  C CH2 . TRP A 93  ? 0.4666 0.3854 0.3319 0.0559  -0.0451 0.0554  92  TRP A CH2 
731  N N   . GLY A 94  ? 0.4226 0.4375 0.3813 0.0453  -0.0518 0.0338  93  GLY A N   
732  C CA  . GLY A 94  ? 0.3864 0.3996 0.3263 0.0361  -0.0579 0.0323  93  GLY A CA  
733  C C   . GLY A 94  ? 0.3964 0.4356 0.3503 0.0253  -0.0634 0.0251  93  GLY A C   
734  O O   . GLY A 94  ? 0.3978 0.4598 0.3780 0.0266  -0.0640 0.0230  93  GLY A O   
735  N N   . GLY A 95  ? 0.4239 0.4578 0.3582 0.0136  -0.0664 0.0207  94  GLY A N   
736  C CA  . GLY A 95  ? 0.4350 0.4898 0.3785 0.0006  -0.0716 0.0123  94  GLY A CA  
737  C C   . GLY A 95  ? 0.4977 0.5798 0.4424 0.0033  -0.0905 0.0152  94  GLY A C   
738  O O   . GLY A 95  ? 0.5070 0.5931 0.4464 0.0176  -0.1001 0.0254  94  GLY A O   
739  N N   . ARG A 96  ? 0.4809 0.5824 0.4337 -0.0112 -0.0959 0.0062  95  ARG A N   
740  C CA  . ARG A 96  ? 0.5409 0.6728 0.4963 -0.0129 -0.1156 0.0069  95  ARG A CA  
741  C C   . ARG A 96  ? 0.5321 0.6898 0.5138 -0.0284 -0.1162 -0.0040 95  ARG A C   
742  O O   . ARG A 96  ? 0.4667 0.6114 0.4553 -0.0390 -0.1009 -0.0122 95  ARG A O   
743  C CB  . ARG A 96  ? 0.6056 0.7229 0.5200 -0.0199 -0.1248 0.0061  95  ARG A CB  
744  C CG  . ARG A 96  ? 0.5835 0.6784 0.4783 -0.0402 -0.1135 -0.0075 95  ARG A CG  
745  C CD  . ARG A 96  ? 0.6295 0.7122 0.4820 -0.0499 -0.1226 -0.0107 95  ARG A CD  
746  N NE  . ARG A 96  ? 0.7254 0.8429 0.5805 -0.0551 -0.1458 -0.0119 95  ARG A NE  
747  C CZ  . ARG A 96  ? 0.8064 0.9360 0.6458 -0.0442 -0.1647 -0.0007 95  ARG A CZ  
748  N NH1 . ARG A 96  ? 0.8446 0.9501 0.6612 -0.0284 -0.1618 0.0121  95  ARG A NH1 
749  N NH2 . ARG A 96  ? 0.7771 0.9442 0.6245 -0.0496 -0.1872 -0.0019 95  ARG A NH2 
750  N N   . ASN A 97  ? 0.5775 0.7724 0.5756 -0.0295 -0.1340 -0.0032 96  ASN A N   
751  C CA  . ASN A 97  ? 0.5620 0.7807 0.5751 -0.0496 -0.1391 -0.0153 96  ASN A CA  
752  C C   . ASN A 97  ? 0.6251 0.8550 0.6124 -0.0580 -0.1603 -0.0173 96  ASN A C   
753  O O   . ASN A 97  ? 0.7020 0.9158 0.6575 -0.0484 -0.1673 -0.0092 96  ASN A O   
754  C CB  . ASN A 97  ? 0.5527 0.8104 0.6140 -0.0462 -0.1404 -0.0139 96  ASN A CB  
755  C CG  . ASN A 97  ? 0.6466 0.9407 0.7265 -0.0292 -0.1592 -0.0019 96  ASN A CG  
756  O OD1 . ASN A 97  ? 0.6675 0.9620 0.7240 -0.0223 -0.1749 0.0050  96  ASN A OD1 
757  N ND2 . ASN A 97  ? 0.6113 0.9359 0.7339 -0.0217 -0.1564 0.0014  96  ASN A ND2 
758  N N   . ASP A 98  ? 0.5679 0.8248 0.5673 -0.0769 -0.1705 -0.0282 97  ASP A N   
759  C CA  . ASP A 98  ? 0.7154 0.9853 0.6883 -0.0868 -0.1928 -0.0311 97  ASP A CA  
760  C C   . ASP A 98  ? 0.7742 1.0851 0.7637 -0.0700 -0.2170 -0.0167 97  ASP A C   
761  O O   . ASP A 98  ? 0.7678 1.0804 0.7257 -0.0679 -0.2353 -0.0115 97  ASP A O   
762  C CB  . ASP A 98  ? 0.7129 0.9958 0.6905 -0.1157 -0.1958 -0.0495 97  ASP A CB  
763  C CG  . ASP A 98  ? 0.6789 0.9202 0.6430 -0.1310 -0.1701 -0.0630 97  ASP A CG  
764  O OD1 . ASP A 98  ? 0.6478 0.8487 0.5859 -0.1227 -0.1546 -0.0596 97  ASP A OD1 
765  O OD2 . ASP A 98  ? 0.6713 0.9207 0.6525 -0.1515 -0.1649 -0.0768 97  ASP A OD2 
766  N N   . THR A 99  ? 0.8020 1.1456 0.8396 -0.0570 -0.2168 -0.0094 98  THR A N   
767  C CA  . THR A 99  ? 0.8012 1.1881 0.8612 -0.0405 -0.2391 0.0043  98  THR A CA  
768  C C   . THR A 99  ? 0.8150 1.1834 0.8606 -0.0117 -0.2386 0.0228  98  THR A C   
769  O O   . THR A 99  ? 0.8285 1.1914 0.8415 -0.0046 -0.2543 0.0317  98  THR A O   
770  C CB  . THR A 99  ? 0.8279 1.2588 0.9482 -0.0384 -0.2371 0.0043  98  THR A CB  
771  O OG1 . THR A 99  ? 0.8828 1.3378 1.0187 -0.0661 -0.2421 -0.0117 98  THR A OG1 
772  C CG2 . THR A 99  ? 0.8703 1.3454 1.0201 -0.0159 -0.2564 0.0210  98  THR A CG2 
773  N N   . GLU A 100 ? 0.8349 1.1894 0.9007 0.0040  -0.2192 0.0283  99  GLU A N   
774  C CA  . GLU A 100 ? 0.8830 1.2223 0.9432 0.0315  -0.2167 0.0450  99  GLU A CA  
775  C C   . GLU A 100 ? 0.9246 1.2104 0.9345 0.0332  -0.2071 0.0470  99  GLU A C   
776  O O   . GLU A 100 ? 0.8906 1.1558 0.8890 0.0537  -0.2034 0.0601  99  GLU A O   
777  C CB  . GLU A 100 ? 0.7954 1.1397 0.8948 0.0449  -0.1989 0.0476  99  GLU A CB  
778  C CG  . GLU A 100 ? 0.8043 1.2035 0.9561 0.0432  -0.2066 0.0462  99  GLU A CG  
779  C CD  . GLU A 100 ? 0.8869 1.2887 1.0741 0.0495  -0.1853 0.0444  99  GLU A CD  
780  O OE1 . GLU A 100 ? 0.9104 1.2917 1.0963 0.0701  -0.1737 0.0532  99  GLU A OE1 
781  O OE2 . GLU A 100 ? 0.8548 1.2779 1.0692 0.0330  -0.1797 0.0338  99  GLU A OE2 
782  N N   . GLY A 101 ? 0.9821 1.2454 0.9626 0.0115  -0.2024 0.0340  100 GLY A N   
783  C CA  . GLY A 101 ? 0.9354 1.1497 0.8715 0.0104  -0.1906 0.0342  100 GLY A CA  
784  C C   . GLY A 101 ? 0.9399 1.1261 0.8856 0.0201  -0.1677 0.0360  100 GLY A C   
785  O O   . GLY A 101 ? 0.8467 1.0408 0.8230 0.0163  -0.1557 0.0293  100 GLY A O   
786  N N   . ALA A 102 ? 1.0716 1.2246 0.9899 0.0324  -0.1619 0.0455  101 ALA A N   
787  C CA  . ALA A 102 ? 0.9866 1.1097 0.9081 0.0399  -0.1415 0.0468  101 ALA A CA  
788  C C   . ALA A 102 ? 0.9847 1.1139 0.9248 0.0635  -0.1425 0.0600  101 ALA A C   
789  O O   . ALA A 102 ? 1.0094 1.1510 0.9455 0.0774  -0.1571 0.0720  101 ALA A O   
790  C CB  . ALA A 102 ? 0.9660 1.0456 0.8462 0.0352  -0.1312 0.0469  101 ALA A CB  
791  N N   . CYS A 103 ? 0.7244 0.8455 0.6851 0.0681  -0.1268 0.0575  102 CYS A N   
792  C CA  . CYS A 103 ? 0.6802 0.7969 0.6543 0.0891  -0.1221 0.0673  102 CYS A CA  
793  C C   . CYS A 103 ? 0.5557 0.6320 0.5147 0.0887  -0.1037 0.0652  102 CYS A C   
794  O O   . CYS A 103 ? 0.5362 0.5991 0.4890 0.0734  -0.0940 0.0556  102 CYS A O   
795  C CB  . CYS A 103 ? 0.6489 0.8005 0.6665 0.0955  -0.1212 0.0658  102 CYS A CB  
796  S SG  . CYS A 103 ? 0.5861 0.7240 0.6215 0.0931  -0.0988 0.0572  102 CYS A SG  
797  N N   . ASN A 104 ? 0.5113 0.5674 0.4640 0.1056  -0.0992 0.0746  103 ASN A N   
798  C CA  . ASN A 104 ? 0.5108 0.5291 0.4494 0.1045  -0.0831 0.0726  103 ASN A CA  
799  C C   . ASN A 104 ? 0.5032 0.5195 0.4626 0.1155  -0.0728 0.0720  103 ASN A C   
800  O O   . ASN A 104 ? 0.4816 0.4661 0.4284 0.1192  -0.0619 0.0729  103 ASN A O   
801  C CB  . ASN A 104 ? 0.5200 0.5055 0.4251 0.1104  -0.0830 0.0822  103 ASN A CB  
802  C CG  . ASN A 104 ? 0.5739 0.5619 0.4793 0.1319  -0.0909 0.0963  103 ASN A CG  
803  O OD1 . ASN A 104 ? 0.5585 0.5745 0.4923 0.1435  -0.0960 0.0987  103 ASN A OD1 
804  N ND2 . ASN A 104 ? 0.5515 0.5094 0.4263 0.1384  -0.0907 0.1067  103 ASN A ND2 
805  N N   . VAL A 105 ? 0.4605 0.5094 0.4507 0.1195  -0.0752 0.0696  104 VAL A N   
806  C CA  . VAL A 105 ? 0.4464 0.4934 0.4544 0.1286  -0.0636 0.0675  104 VAL A CA  
807  C C   . VAL A 105 ? 0.4604 0.4941 0.4664 0.1140  -0.0515 0.0566  104 VAL A C   
808  O O   . VAL A 105 ? 0.4271 0.4766 0.4413 0.0997  -0.0525 0.0497  104 VAL A O   
809  C CB  . VAL A 105 ? 0.4344 0.5218 0.4769 0.1366  -0.0681 0.0686  104 VAL A CB  
810  C CG1 . VAL A 105 ? 0.3695 0.4532 0.4275 0.1437  -0.0533 0.0645  104 VAL A CG1 
811  C CG2 . VAL A 105 ? 0.4178 0.5221 0.4667 0.1539  -0.0811 0.0812  104 VAL A CG2 
812  N N   . LEU A 106 ? 0.4842 0.4885 0.4795 0.1177  -0.0402 0.0552  105 LEU A N   
813  C CA  . LEU A 106 ? 0.3896 0.3845 0.3849 0.1061  -0.0302 0.0461  105 LEU A CA  
814  C C   . LEU A 106 ? 0.3802 0.3997 0.3996 0.1078  -0.0261 0.0418  105 LEU A C   
815  O O   . LEU A 106 ? 0.4268 0.4538 0.4583 0.1219  -0.0232 0.0445  105 LEU A O   
816  C CB  . LEU A 106 ? 0.3978 0.3572 0.3758 0.1089  -0.0208 0.0451  105 LEU A CB  
817  C CG  . LEU A 106 ? 0.4481 0.4003 0.4258 0.0971  -0.0126 0.0361  105 LEU A CG  
818  C CD1 . LEU A 106 ? 0.3752 0.3270 0.3479 0.0806  -0.0143 0.0331  105 LEU A CD1 
819  C CD2 . LEU A 106 ? 0.4329 0.3547 0.3967 0.1000  -0.0040 0.0334  105 LEU A CD2 
820  N N   . TYR A 107 ? 0.3690 0.3998 0.3954 0.0940  -0.0242 0.0356  106 TYR A N   
821  C CA  . TYR A 107 ? 0.3474 0.3981 0.3934 0.0931  -0.0183 0.0318  106 TYR A CA  
822  C C   . TYR A 107 ? 0.3573 0.3912 0.3938 0.0849  -0.0093 0.0262  106 TYR A C   
823  O O   . TYR A 107 ? 0.3092 0.3298 0.3339 0.0740  -0.0099 0.0244  106 TYR A O   
824  C CB  . TYR A 107 ? 0.3142 0.3948 0.3783 0.0838  -0.0240 0.0304  106 TYR A CB  
825  C CG  . TYR A 107 ? 0.3794 0.4891 0.4636 0.0927  -0.0321 0.0348  106 TYR A CG  
826  C CD1 . TYR A 107 ? 0.3676 0.5005 0.4769 0.0998  -0.0268 0.0349  106 TYR A CD1 
827  C CD2 . TYR A 107 ? 0.3972 0.5132 0.4759 0.0937  -0.0453 0.0394  106 TYR A CD2 
828  C CE1 . TYR A 107 ? 0.3740 0.5385 0.5071 0.1080  -0.0346 0.0396  106 TYR A CE1 
829  C CE2 . TYR A 107 ? 0.3691 0.5162 0.4684 0.1019  -0.0551 0.0443  106 TYR A CE2 
830  C CZ  . TYR A 107 ? 0.3911 0.5639 0.5201 0.1092  -0.0498 0.0444  106 TYR A CZ  
831  O OH  . TYR A 107 ? 0.3954 0.6040 0.5506 0.1177  -0.0596 0.0498  106 TYR A OH  
832  N N   . ALA A 108 ? 0.3501 0.3852 0.3917 0.0906  -0.0007 0.0240  107 ALA A N   
833  C CA  . ALA A 108 ? 0.3716 0.3936 0.4029 0.0839  0.0066  0.0193  107 ALA A CA  
834  C C   . ALA A 108 ? 0.3770 0.4204 0.4239 0.0810  0.0123  0.0179  107 ALA A C   
835  O O   . ALA A 108 ? 0.3943 0.4564 0.4581 0.0889  0.0154  0.0192  107 ALA A O   
836  C CB  . ALA A 108 ? 0.3632 0.3613 0.3789 0.0920  0.0131  0.0168  107 ALA A CB  
837  N N   . PHE A 109 ? 0.3306 0.3715 0.3729 0.0700  0.0143  0.0162  108 PHE A N   
838  C CA  . PHE A 109 ? 0.3344 0.3914 0.3882 0.0658  0.0208  0.0161  108 PHE A CA  
839  C C   . PHE A 109 ? 0.3679 0.4104 0.4049 0.0624  0.0263  0.0146  108 PHE A C   
840  O O   . PHE A 109 ? 0.3730 0.4030 0.3986 0.0554  0.0221  0.0146  108 PHE A O   
841  C CB  . PHE A 109 ? 0.3056 0.3762 0.3721 0.0551  0.0171  0.0173  108 PHE A CB  
842  C CG  . PHE A 109 ? 0.3282 0.4097 0.4043 0.0488  0.0249  0.0180  108 PHE A CG  
843  C CD1 . PHE A 109 ? 0.3136 0.4170 0.4099 0.0500  0.0299  0.0182  108 PHE A CD1 
844  C CD2 . PHE A 109 ? 0.3371 0.4074 0.4033 0.0417  0.0276  0.0194  108 PHE A CD2 
845  C CE1 . PHE A 109 ? 0.3386 0.4494 0.4429 0.0432  0.0389  0.0193  108 PHE A CE1 
846  C CE2 . PHE A 109 ? 0.2944 0.3718 0.3676 0.0366  0.0355  0.0217  108 PHE A CE2 
847  C CZ  . PHE A 109 ? 0.3181 0.4142 0.4092 0.0369  0.0420  0.0215  108 PHE A CZ  
848  N N   . ASP A 110 ? 0.3593 0.4046 0.3948 0.0675  0.0356  0.0134  109 ASP A N   
849  C CA  . ASP A 110 ? 0.3732 0.4056 0.3889 0.0645  0.0403  0.0120  109 ASP A CA  
850  C C   . ASP A 110 ? 0.3681 0.4104 0.3892 0.0560  0.0425  0.0163  109 ASP A C   
851  O O   . ASP A 110 ? 0.3489 0.4073 0.3859 0.0560  0.0495  0.0184  109 ASP A O   
852  C CB  . ASP A 110 ? 0.3591 0.3872 0.3666 0.0735  0.0511  0.0087  109 ASP A CB  
853  C CG  . ASP A 110 ? 0.4009 0.4116 0.3804 0.0701  0.0543  0.0057  109 ASP A CG  
854  O OD1 . ASP A 110 ? 0.4014 0.4177 0.3767 0.0651  0.0580  0.0089  109 ASP A OD1 
855  O OD2 . ASP A 110 ? 0.4101 0.4006 0.3705 0.0721  0.0528  0.0002  109 ASP A OD2 
856  N N   . VAL A 111 ? 0.3696 0.4026 0.3794 0.0490  0.0372  0.0182  110 VAL A N   
857  C CA  . VAL A 111 ? 0.3525 0.3927 0.3688 0.0424  0.0394  0.0240  110 VAL A CA  
858  C C   . VAL A 111 ? 0.3799 0.4210 0.3862 0.0436  0.0489  0.0268  110 VAL A C   
859  O O   . VAL A 111 ? 0.3944 0.4414 0.4076 0.0395  0.0540  0.0327  110 VAL A O   
860  C CB  . VAL A 111 ? 0.3665 0.3987 0.3778 0.0363  0.0312  0.0268  110 VAL A CB  
861  C CG1 . VAL A 111 ? 0.3676 0.3974 0.3869 0.0348  0.0244  0.0241  110 VAL A CG1 
862  C CG2 . VAL A 111 ? 0.3520 0.3726 0.3409 0.0364  0.0271  0.0257  110 VAL A CG2 
863  N N   . ASN A 112 ? 0.3776 0.4105 0.3659 0.0490  0.0529  0.0227  111 ASN A N   
864  C CA  . ASN A 112 ? 0.3985 0.4304 0.3731 0.0502  0.0635  0.0251  111 ASN A CA  
865  C C   . ASN A 112 ? 0.3997 0.4433 0.3889 0.0558  0.0769  0.0236  111 ASN A C   
866  O O   . ASN A 112 ? 0.4700 0.5216 0.4649 0.0538  0.0873  0.0284  111 ASN A O   
867  C CB  . ASN A 112 ? 0.4431 0.4578 0.3853 0.0514  0.0615  0.0207  111 ASN A CB  
868  C CG  . ASN A 112 ? 0.4181 0.4252 0.3499 0.0452  0.0471  0.0216  111 ASN A CG  
869  O OD1 . ASN A 112 ? 0.4096 0.4219 0.3455 0.0406  0.0424  0.0294  111 ASN A OD1 
870  N ND2 . ASN A 112 ? 0.3947 0.3894 0.3150 0.0452  0.0409  0.0139  111 ASN A ND2 
871  N N   . THR A 113 ? 0.3983 0.4432 0.3949 0.0633  0.0779  0.0176  112 THR A N   
872  C CA  . THR A 113 ? 0.4152 0.4753 0.4310 0.0699  0.0905  0.0168  112 THR A CA  
873  C C   . THR A 113 ? 0.3641 0.4475 0.4151 0.0676  0.0870  0.0192  112 THR A C   
874  O O   . THR A 113 ? 0.3116 0.4137 0.3842 0.0694  0.0972  0.0202  112 THR A O   
875  C CB  . THR A 113 ? 0.3986 0.4500 0.4081 0.0814  0.0948  0.0104  112 THR A CB  
876  O OG1 . THR A 113 ? 0.3624 0.4163 0.3859 0.0849  0.0836  0.0093  112 THR A OG1 
877  C CG2 . THR A 113 ? 0.3780 0.4027 0.3495 0.0815  0.0957  0.0054  112 THR A CG2 
878  N N   . HIS A 114 ? 0.3735 0.4566 0.4301 0.0626  0.0734  0.0197  113 HIS A N   
879  C CA  . HIS A 114 ? 0.3075 0.4102 0.3920 0.0587  0.0678  0.0205  113 HIS A CA  
880  C C   . HIS A 114 ? 0.3468 0.4640 0.4494 0.0684  0.0661  0.0184  113 HIS A C   
881  O O   . HIS A 114 ? 0.3466 0.4864 0.4751 0.0657  0.0626  0.0191  113 HIS A O   
882  C CB  . HIS A 114 ? 0.3119 0.4297 0.4137 0.0501  0.0764  0.0237  113 HIS A CB  
883  C CG  . HIS A 114 ? 0.3843 0.4883 0.4715 0.0416  0.0778  0.0279  113 HIS A CG  
884  N ND1 . HIS A 114 ? 0.3825 0.4910 0.4762 0.0353  0.0892  0.0323  113 HIS A ND1 
885  C CD2 . HIS A 114 ? 0.3464 0.4329 0.4147 0.0392  0.0696  0.0295  113 HIS A CD2 
886  C CE1 . HIS A 114 ? 0.3654 0.4585 0.4437 0.0306  0.0876  0.0371  113 HIS A CE1 
887  N NE2 . HIS A 114 ? 0.3501 0.4316 0.4144 0.0330  0.0754  0.0355  113 HIS A NE2 
888  N N   . LYS A 115 ? 0.3424 0.4473 0.4323 0.0799  0.0685  0.0160  114 LYS A N   
889  C CA  . LYS A 115 ? 0.3471 0.4634 0.4539 0.0917  0.0665  0.0158  114 LYS A CA  
890  C C   . LYS A 115 ? 0.3860 0.4936 0.4872 0.0917  0.0512  0.0164  114 LYS A C   
891  O O   . LYS A 115 ? 0.3793 0.4635 0.4569 0.0872  0.0461  0.0149  114 LYS A O   
892  C CB  . LYS A 115 ? 0.3164 0.4198 0.4121 0.1051  0.0785  0.0131  114 LYS A CB  
893  N N   . TRP A 116 ? 0.3525 0.4808 0.4761 0.0957  0.0436  0.0189  115 TRP A N   
894  C CA  . TRP A 116 ? 0.3605 0.4811 0.4777 0.0981  0.0302  0.0207  115 TRP A CA  
895  C C   . TRP A 116 ? 0.3850 0.4955 0.4989 0.1153  0.0326  0.0222  115 TRP A C   
896  O O   . TRP A 116 ? 0.4108 0.5332 0.5399 0.1264  0.0423  0.0228  115 TRP A O   
897  C CB  . TRP A 116 ? 0.3399 0.4880 0.4796 0.0932  0.0190  0.0231  115 TRP A CB  
898  C CG  . TRP A 116 ? 0.3255 0.4793 0.4673 0.0758  0.0166  0.0209  115 TRP A CG  
899  C CD1 . TRP A 116 ? 0.3301 0.5023 0.4898 0.0670  0.0237  0.0196  115 TRP A CD1 
900  C CD2 . TRP A 116 ? 0.3101 0.4493 0.4359 0.0653  0.0081  0.0198  115 TRP A CD2 
901  N NE1 . TRP A 116 ? 0.2940 0.4617 0.4490 0.0519  0.0202  0.0177  115 TRP A NE1 
902  C CE2 . TRP A 116 ? 0.2642 0.4126 0.3990 0.0511  0.0109  0.0176  115 TRP A CE2 
903  C CE3 . TRP A 116 ? 0.2762 0.3939 0.3810 0.0665  0.0005  0.0206  115 TRP A CE3 
904  C CZ2 . TRP A 116 ? 0.2376 0.3740 0.3614 0.0393  0.0066  0.0158  115 TRP A CZ2 
905  C CZ3 . TRP A 116 ? 0.3135 0.4218 0.4082 0.0542  -0.0039 0.0189  115 TRP A CZ3 
906  C CH2 . TRP A 116 ? 0.2699 0.3873 0.3741 0.0413  -0.0006 0.0164  115 TRP A CH2 
907  N N   . PHE A 117 ? 0.3824 0.4700 0.4772 0.1179  0.0252  0.0232  116 PHE A N   
908  C CA  . PHE A 117 ? 0.4279 0.5052 0.5212 0.1348  0.0264  0.0264  116 PHE A CA  
909  C C   . PHE A 117 ? 0.4043 0.4675 0.4844 0.1345  0.0139  0.0305  116 PHE A C   
910  O O   . PHE A 117 ? 0.4183 0.4772 0.4884 0.1209  0.0063  0.0294  116 PHE A O   
911  C CB  . PHE A 117 ? 0.4470 0.4960 0.5212 0.1417  0.0405  0.0214  116 PHE A CB  
912  C CG  . PHE A 117 ? 0.5364 0.5565 0.5809 0.1291  0.0409  0.0154  116 PHE A CG  
913  C CD1 . PHE A 117 ? 0.5699 0.5952 0.6101 0.1160  0.0434  0.0119  116 PHE A CD1 
914  C CD2 . PHE A 117 ? 0.5900 0.5777 0.6116 0.1305  0.0394  0.0140  116 PHE A CD2 
915  C CE1 . PHE A 117 ? 0.6208 0.6230 0.6357 0.1050  0.0419  0.0075  116 PHE A CE1 
916  C CE2 . PHE A 117 ? 0.6650 0.6293 0.6622 0.1176  0.0388  0.0081  116 PHE A CE2 
917  C CZ  . PHE A 117 ? 0.5795 0.5529 0.5743 0.1053  0.0391  0.0051  116 PHE A CZ  
918  N N   . THR A 118 ? 0.3866 0.4430 0.4676 0.1506  0.0128  0.0361  117 THR A N   
919  C CA  . THR A 118 ? 0.4012 0.4444 0.4693 0.1527  0.0018  0.0421  117 THR A CA  
920  C C   . THR A 118 ? 0.4288 0.4333 0.4754 0.1631  0.0100  0.0424  117 THR A C   
921  O O   . THR A 118 ? 0.4196 0.4211 0.4727 0.1815  0.0127  0.0488  117 THR A O   
922  C CB  . THR A 118 ? 0.4065 0.4806 0.4966 0.1626  -0.0099 0.0512  117 THR A CB  
923  O OG1 . THR A 118 ? 0.4030 0.4860 0.5115 0.1829  -0.0032 0.0561  117 THR A OG1 
924  C CG2 . THR A 118 ? 0.3987 0.5104 0.5107 0.1501  -0.0170 0.0489  117 THR A CG2 
925  N N   . PRO A 119 ? 0.4349 0.4092 0.4569 0.1518  0.0144  0.0358  118 PRO A N   
926  C CA  . PRO A 119 ? 0.4551 0.3901 0.4559 0.1587  0.0234  0.0340  118 PRO A CA  
927  C C   . PRO A 119 ? 0.4904 0.4102 0.4844 0.1703  0.0185  0.0439  118 PRO A C   
928  O O   . PRO A 119 ? 0.5037 0.4316 0.4958 0.1652  0.0069  0.0499  118 PRO A O   
929  C CB  . PRO A 119 ? 0.4727 0.3867 0.4523 0.1400  0.0242  0.0258  118 PRO A CB  
930  C CG  . PRO A 119 ? 0.4839 0.4222 0.4721 0.1263  0.0140  0.0268  118 PRO A CG  
931  C CD  . PRO A 119 ? 0.4315 0.4067 0.4455 0.1320  0.0107  0.0303  118 PRO A CD  
932  N N   . ARG A 120 ? 0.4720 0.3676 0.4604 0.1863  0.0285  0.0460  119 ARG A N   
933  C CA  . ARG A 120 ? 0.5152 0.3916 0.4949 0.1990  0.0254  0.0571  119 ARG A CA  
934  C C   . ARG A 120 ? 0.5380 0.3815 0.4901 0.1843  0.0242  0.0550  119 ARG A C   
935  O O   . ARG A 120 ? 0.5627 0.3807 0.4991 0.1729  0.0328  0.0447  119 ARG A O   
936  C CB  . ARG A 120 ? 0.5323 0.3856 0.5122 0.2203  0.0390  0.0600  119 ARG A CB  
937  N N   . VAL A 121 ? 0.5228 0.3687 0.4690 0.1835  0.0135  0.0646  120 VAL A N   
938  C CA  . VAL A 121 ? 0.5481 0.3648 0.4700 0.1699  0.0136  0.0639  120 VAL A CA  
939  C C   . VAL A 121 ? 0.5971 0.3804 0.5025 0.1842  0.0173  0.0752  120 VAL A C   
940  O O   . VAL A 121 ? 0.5736 0.3630 0.4880 0.2051  0.0159  0.0857  120 VAL A O   
941  C CB  . VAL A 121 ? 0.5445 0.3837 0.4668 0.1557  0.0013  0.0653  120 VAL A CB  
942  C CG1 . VAL A 121 ? 0.4993 0.3698 0.4390 0.1432  -0.0012 0.0556  120 VAL A CG1 
943  C CG2 . VAL A 121 ? 0.5002 0.3582 0.4264 0.1677  -0.0107 0.0784  120 VAL A CG2 
944  N N   . SER A 122 ? 0.5891 0.3370 0.4715 0.1731  0.0228  0.0737  121 SER A N   
945  C CA  . SER A 122 ? 0.6142 0.3264 0.4769 0.1834  0.0270  0.0854  121 SER A CA  
946  C C   . SER A 122 ? 0.6651 0.3649 0.5094 0.1665  0.0242  0.0870  121 SER A C   
947  O O   . SER A 122 ? 0.6285 0.3451 0.4771 0.1476  0.0208  0.0779  121 SER A O   
948  C CB  . SER A 122 ? 0.6491 0.3172 0.5003 0.1888  0.0439  0.0808  121 SER A CB  
949  O OG  . SER A 122 ? 0.6787 0.3319 0.5226 0.1673  0.0509  0.0652  121 SER A OG  
950  N N   . GLY A 123 ? 0.6737 0.3431 0.4974 0.1743  0.0271  0.0995  122 GLY A N   
951  C CA  . GLY A 123 ? 0.7036 0.3577 0.5075 0.1598  0.0270  0.1026  122 GLY A CA  
952  C C   . GLY A 123 ? 0.7579 0.4382 0.5579 0.1633  0.0124  0.1134  122 GLY A C   
953  O O   . GLY A 123 ? 0.7423 0.4503 0.5537 0.1789  0.0010  0.1211  122 GLY A O   
954  N N   . THR A 124 ? 0.8276 0.4993 0.6109 0.1476  0.0132  0.1134  123 THR A N   
955  C CA  . THR A 124 ? 0.8412 0.5306 0.6127 0.1478  0.0011  0.1224  123 THR A CA  
956  C C   . THR A 124 ? 0.7928 0.5261 0.5849 0.1364  -0.0089 0.1114  123 THR A C   
957  O O   . THR A 124 ? 0.7754 0.5111 0.5694 0.1176  -0.0043 0.1012  123 THR A O   
958  C CB  . THR A 124 ? 0.8664 0.5231 0.6081 0.1369  0.0094  0.1275  123 THR A CB  
959  O OG1 . THR A 124 ? 0.8941 0.5618 0.6402 0.1150  0.0123  0.1156  123 THR A OG1 
960  C CG2 . THR A 124 ? 0.8755 0.4841 0.6044 0.1379  0.0263  0.1299  123 THR A CG2 
961  N N   . VAL A 125 ? 0.6830 0.4512 0.4923 0.1479  -0.0219 0.1142  124 VAL A N   
962  C CA  . VAL A 125 ? 0.6354 0.4446 0.4656 0.1378  -0.0308 0.1043  124 VAL A CA  
963  C C   . VAL A 125 ? 0.6218 0.4381 0.4344 0.1255  -0.0377 0.1050  124 VAL A C   
964  O O   . VAL A 125 ? 0.6124 0.4271 0.4057 0.1334  -0.0468 0.1167  124 VAL A O   
965  C CB  . VAL A 125 ? 0.6186 0.4628 0.4729 0.1532  -0.0420 0.1078  124 VAL A CB  
966  C CG1 . VAL A 125 ? 0.5357 0.4197 0.4112 0.1411  -0.0497 0.0975  124 VAL A CG1 
967  C CG2 . VAL A 125 ? 0.5684 0.4023 0.4377 0.1670  -0.0325 0.1071  124 VAL A CG2 
968  N N   . PRO A 126 ? 0.5346 0.5072 0.4284 0.1313  -0.0399 0.0762  125 PRO A N   
969  C CA  . PRO A 126 ? 0.4888 0.4635 0.3732 0.1213  -0.0441 0.0742  125 PRO A CA  
970  C C   . PRO A 126 ? 0.5057 0.5133 0.3994 0.1271  -0.0600 0.0741  125 PRO A C   
971  O O   . PRO A 126 ? 0.4975 0.5367 0.4184 0.1311  -0.0656 0.0721  125 PRO A O   
972  C CB  . PRO A 126 ? 0.4829 0.4641 0.3865 0.1027  -0.0366 0.0663  125 PRO A CB  
973  C CG  . PRO A 126 ? 0.4794 0.4606 0.3994 0.1028  -0.0297 0.0649  125 PRO A CG  
974  C CD  . PRO A 126 ? 0.4933 0.4778 0.4124 0.1202  -0.0334 0.0699  125 PRO A CD  
975  N N   . GLY A 127 ? 0.5197 0.5198 0.3899 0.1268  -0.0668 0.0757  126 GLY A N   
976  C CA  . GLY A 127 ? 0.4894 0.5215 0.3671 0.1295  -0.0834 0.0741  126 GLY A CA  
977  C C   . GLY A 127 ? 0.5035 0.5641 0.4095 0.1124  -0.0842 0.0644  126 GLY A C   
978  O O   . GLY A 127 ? 0.5272 0.5762 0.4366 0.0976  -0.0732 0.0595  126 GLY A O   
979  N N   . ALA A 128 ? 0.5148 0.6132 0.4419 0.1149  -0.0974 0.0618  127 ALA A N   
980  C CA  . ALA A 128 ? 0.4570 0.5829 0.4112 0.0988  -0.0982 0.0527  127 ALA A CA  
981  C C   . ALA A 128 ? 0.4895 0.6009 0.4266 0.0824  -0.0963 0.0469  127 ALA A C   
982  O O   . ALA A 128 ? 0.5128 0.6081 0.4197 0.0845  -0.1018 0.0486  127 ALA A O   
983  C CB  . ALA A 128 ? 0.4179 0.5869 0.3952 0.1040  -0.1133 0.0506  127 ALA A CB  
984  N N   . ARG A 129 ? 0.4715 0.5862 0.4259 0.0668  -0.0879 0.0400  128 ARG A N   
985  C CA  . ARG A 129 ? 0.4932 0.5888 0.4327 0.0521  -0.0818 0.0343  128 ARG A CA  
986  C C   . ARG A 129 ? 0.4311 0.5384 0.3956 0.0373  -0.0758 0.0269  128 ARG A C   
987  O O   . ARG A 129 ? 0.4048 0.5266 0.3942 0.0381  -0.0726 0.0277  128 ARG A O   
988  C CB  . ARG A 129 ? 0.4648 0.5233 0.3831 0.0535  -0.0685 0.0380  128 ARG A CB  
989  C CG  . ARG A 129 ? 0.4345 0.4874 0.3722 0.0523  -0.0565 0.0389  128 ARG A CG  
990  C CD  . ARG A 129 ? 0.4047 0.4252 0.3239 0.0531  -0.0446 0.0419  128 ARG A CD  
991  N NE  . ARG A 129 ? 0.4476 0.4548 0.3469 0.0669  -0.0471 0.0496  128 ARG A NE  
992  C CZ  . ARG A 129 ? 0.4606 0.4379 0.3411 0.0687  -0.0368 0.0532  128 ARG A CZ  
993  N NH1 . ARG A 129 ? 0.5003 0.4614 0.3808 0.0577  -0.0239 0.0493  128 ARG A NH1 
994  N NH2 . ARG A 129 ? 0.5080 0.4712 0.3704 0.0820  -0.0386 0.0608  128 ARG A NH2 
995  N N   . ASP A 130 ? 0.4130 0.5102 0.3677 0.0240  -0.0732 0.0200  129 ASP A N   
996  C CA  . ASP A 130 ? 0.3913 0.4893 0.3638 0.0108  -0.0648 0.0139  129 ASP A CA  
997  C C   . ASP A 130 ? 0.3895 0.4564 0.3479 0.0051  -0.0518 0.0118  129 ASP A C   
998  O O   . ASP A 130 ? 0.3879 0.4349 0.3207 0.0074  -0.0497 0.0126  129 ASP A O   
999  C CB  . ASP A 130 ? 0.3821 0.5014 0.3634 -0.0016 -0.0729 0.0056  129 ASP A CB  
1000 C CG  . ASP A 130 ? 0.4246 0.5356 0.3789 -0.0076 -0.0798 -0.0001 129 ASP A CG  
1001 O OD1 . ASP A 130 ? 0.4994 0.5894 0.4265 -0.0007 -0.0790 0.0035  129 ASP A OD1 
1002 O OD2 . ASP A 130 ? 0.4662 0.5898 0.4242 -0.0204 -0.0853 -0.0087 129 ASP A OD2 
1003 N N   . GLY A 131 ? 0.3731 0.4357 0.3486 -0.0013 -0.0424 0.0096  130 GLY A N   
1004 C CA  . GLY A 131 ? 0.3670 0.4051 0.3360 -0.0062 -0.0301 0.0066  130 GLY A CA  
1005 C C   . GLY A 131 ? 0.3848 0.4082 0.3535 0.0014  -0.0216 0.0119  130 GLY A C   
1006 O O   . GLY A 131 ? 0.3622 0.3680 0.3281 -0.0019 -0.0108 0.0092  130 GLY A O   
1007 N N   . HIS A 132 ? 0.3623 0.3927 0.3344 0.0110  -0.0254 0.0186  131 HIS A N   
1008 C CA  . HIS A 132 ? 0.3386 0.3562 0.3120 0.0164  -0.0178 0.0228  131 HIS A CA  
1009 C C   . HIS A 132 ? 0.3535 0.3724 0.3494 0.0134  -0.0118 0.0218  131 HIS A C   
1010 O O   . HIS A 132 ? 0.3202 0.3483 0.3294 0.0085  -0.0132 0.0194  131 HIS A O   
1011 C CB  . HIS A 132 ? 0.3463 0.3702 0.3178 0.0271  -0.0237 0.0293  131 HIS A CB  
1012 C CG  . HIS A 132 ? 0.3752 0.4227 0.3657 0.0295  -0.0308 0.0304  131 HIS A CG  
1013 N ND1 . HIS A 132 ? 0.3280 0.3951 0.3234 0.0263  -0.0392 0.0276  131 HIS A ND1 
1014 C CD2 . HIS A 132 ? 0.3468 0.4013 0.3525 0.0333  -0.0296 0.0332  131 HIS A CD2 
1015 C CE1 . HIS A 132 ? 0.3552 0.4410 0.3695 0.0282  -0.0416 0.0289  131 HIS A CE1 
1016 N NE2 . HIS A 132 ? 0.3354 0.4127 0.3544 0.0329  -0.0357 0.0325  131 HIS A NE2 
1017 N N   . SER A 133 ? 0.3688 0.3774 0.3678 0.0160  -0.0050 0.0237  132 SER A N   
1018 C CA  . SER A 133 ? 0.3120 0.3236 0.3315 0.0154  -0.0020 0.0238  132 SER A CA  
1019 C C   . SER A 133 ? 0.3259 0.3420 0.3488 0.0217  -0.0054 0.0285  132 SER A C   
1020 O O   . SER A 133 ? 0.3280 0.3375 0.3376 0.0264  -0.0056 0.0311  132 SER A O   
1021 C CB  . SER A 133 ? 0.3174 0.3171 0.3419 0.0124  0.0080  0.0207  132 SER A CB  
1022 O OG  . SER A 133 ? 0.3529 0.3405 0.3645 0.0135  0.0134  0.0216  132 SER A OG  
1023 N N   . ALA A 134 ? 0.3273 0.3517 0.3653 0.0220  -0.0077 0.0295  133 ALA A N   
1024 C CA  . ALA A 134 ? 0.2972 0.3232 0.3371 0.0268  -0.0097 0.0326  133 ALA A CA  
1025 C C   . ALA A 134 ? 0.3055 0.3313 0.3592 0.0248  -0.0087 0.0318  133 ALA A C   
1026 O O   . ALA A 134 ? 0.3403 0.3693 0.4038 0.0221  -0.0091 0.0310  133 ALA A O   
1027 C CB  . ALA A 134 ? 0.3169 0.3557 0.3570 0.0309  -0.0153 0.0354  133 ALA A CB  
1028 N N   . CYS A 135 ? 0.2748 0.2957 0.3283 0.0262  -0.0079 0.0320  134 CYS A N   
1029 C CA  . CYS A 135 ? 0.2828 0.3060 0.3490 0.0247  -0.0097 0.0311  134 CYS A CA  
1030 C C   . CYS A 135 ? 0.3379 0.3564 0.3977 0.0262  -0.0107 0.0312  134 CYS A C   
1031 O O   . CYS A 135 ? 0.3497 0.3603 0.3959 0.0287  -0.0081 0.0321  134 CYS A O   
1032 C CB  . CYS A 135 ? 0.3349 0.3565 0.4138 0.0208  -0.0050 0.0273  134 CYS A CB  
1033 S SG  . CYS A 135 ? 0.3884 0.3982 0.4602 0.0172  0.0045  0.0241  134 CYS A SG  
1034 N N   . VAL A 136 ? 0.3205 0.3424 0.3880 0.0251  -0.0151 0.0304  135 VAL A N   
1035 C CA  . VAL A 136 ? 0.3573 0.3737 0.4163 0.0255  -0.0168 0.0296  135 VAL A CA  
1036 C C   . VAL A 136 ? 0.3525 0.3701 0.4227 0.0202  -0.0188 0.0251  135 VAL A C   
1037 O O   . VAL A 136 ? 0.3404 0.3673 0.4274 0.0186  -0.0216 0.0240  135 VAL A O   
1038 C CB  . VAL A 136 ? 0.3152 0.3350 0.3669 0.0295  -0.0215 0.0326  135 VAL A CB  
1039 C CG1 . VAL A 136 ? 0.3285 0.3531 0.3758 0.0335  -0.0198 0.0360  135 VAL A CG1 
1040 C CG2 . VAL A 136 ? 0.3229 0.3491 0.3830 0.0282  -0.0281 0.0333  135 VAL A CG2 
1041 N N   . LEU A 137 ? 0.3759 0.3841 0.4370 0.0176  -0.0174 0.0222  136 LEU A N   
1042 C CA  . LEU A 137 ? 0.3649 0.3755 0.4349 0.0110  -0.0212 0.0168  136 LEU A CA  
1043 C C   . LEU A 137 ? 0.3858 0.3849 0.4372 0.0110  -0.0229 0.0153  136 LEU A C   
1044 O O   . LEU A 137 ? 0.3961 0.3789 0.4327 0.0109  -0.0156 0.0145  136 LEU A O   
1045 C CB  . LEU A 137 ? 0.3777 0.3853 0.4578 0.0034  -0.0134 0.0118  136 LEU A CB  
1046 C CG  . LEU A 137 ? 0.3013 0.3144 0.3943 -0.0057 -0.0166 0.0045  136 LEU A CG  
1047 C CD1 . LEU A 137 ? 0.2899 0.3252 0.4065 -0.0046 -0.0272 0.0038  136 LEU A CD1 
1048 C CD2 . LEU A 137 ? 0.3345 0.3407 0.4337 -0.0144 -0.0048 -0.0002 136 LEU A CD2 
1049 N N   . GLY A 138 ? 0.3545 0.3593 0.4039 0.0117  -0.0320 0.0152  137 GLY A N   
1050 C CA  . GLY A 138 ? 0.3542 0.3463 0.3827 0.0121  -0.0326 0.0135  137 GLY A CA  
1051 C C   . GLY A 138 ? 0.4014 0.3864 0.4149 0.0208  -0.0265 0.0186  137 GLY A C   
1052 O O   . GLY A 138 ? 0.4151 0.4097 0.4321 0.0259  -0.0277 0.0239  137 GLY A O   
1053 N N   . LYS A 139 ? 0.4166 0.3848 0.4143 0.0225  -0.0194 0.0169  138 LYS A N   
1054 C CA  . LYS A 139 ? 0.4535 0.4174 0.4398 0.0326  -0.0138 0.0214  138 LYS A CA  
1055 C C   . LYS A 139 ? 0.4537 0.4165 0.4431 0.0370  -0.0083 0.0250  138 LYS A C   
1056 O O   . LYS A 139 ? 0.4657 0.4266 0.4476 0.0464  -0.0046 0.0286  138 LYS A O   
1057 C CB  . LYS A 139 ? 0.4576 0.4021 0.4229 0.0350  -0.0090 0.0180  138 LYS A CB  
1058 C CG  . LYS A 139 ? 0.4698 0.4125 0.4263 0.0300  -0.0145 0.0137  138 LYS A CG  
1059 C CD  . LYS A 139 ? 0.4871 0.4410 0.4414 0.0355  -0.0165 0.0181  138 LYS A CD  
1060 C CE  . LYS A 139 ? 0.6031 0.5561 0.5475 0.0298  -0.0244 0.0151  138 LYS A CE  
1061 N NZ  . LYS A 139 ? 0.6481 0.6154 0.6093 0.0237  -0.0355 0.0157  138 LYS A NZ  
1062 N N   . ILE A 140 ? 0.3763 0.3408 0.3764 0.0310  -0.0077 0.0240  139 ILE A N   
1063 C CA  . ILE A 140 ? 0.4306 0.3898 0.4283 0.0341  -0.0022 0.0270  139 ILE A CA  
1064 C C   . ILE A 140 ? 0.4133 0.3906 0.4244 0.0351  -0.0056 0.0301  139 ILE A C   
1065 O O   . ILE A 140 ? 0.3966 0.3844 0.4229 0.0292  -0.0088 0.0283  139 ILE A O   
1066 C CB  . ILE A 140 ? 0.4373 0.3826 0.4342 0.0256  0.0039  0.0233  139 ILE A CB  
1067 C CG1 . ILE A 140 ? 0.4272 0.3538 0.4123 0.0209  0.0072  0.0182  139 ILE A CG1 
1068 C CG2 . ILE A 140 ? 0.4294 0.3637 0.4158 0.0300  0.0103  0.0274  139 ILE A CG2 
1069 C CD1 . ILE A 140 ? 0.4600 0.3675 0.4230 0.0306  0.0117  0.0209  139 ILE A CD1 
1070 N N   . MET A 141 ? 0.3701 0.3505 0.3758 0.0428  -0.0050 0.0344  140 MET A N   
1071 C CA  . MET A 141 ? 0.3645 0.3579 0.3789 0.0424  -0.0071 0.0363  140 MET A CA  
1072 C C   . MET A 141 ? 0.3897 0.3717 0.3961 0.0413  -0.0022 0.0367  140 MET A C   
1073 O O   . MET A 141 ? 0.3970 0.3635 0.3870 0.0463  0.0013  0.0387  140 MET A O   
1074 C CB  . MET A 141 ? 0.3533 0.3599 0.3678 0.0497  -0.0104 0.0397  140 MET A CB  
1075 C CG  . MET A 141 ? 0.3433 0.3631 0.3657 0.0474  -0.0130 0.0403  140 MET A CG  
1076 S SD  . MET A 141 ? 0.3882 0.4284 0.4157 0.0531  -0.0168 0.0426  140 MET A SD  
1077 C CE  . MET A 141 ? 0.3262 0.3614 0.3400 0.0649  -0.0173 0.0457  140 MET A CE  
1078 N N   . TYR A 142 ? 0.3297 0.3165 0.3452 0.0353  -0.0011 0.0349  141 TYR A N   
1079 C CA  . TYR A 142 ? 0.3641 0.3391 0.3694 0.0333  0.0048  0.0349  141 TYR A CA  
1080 C C   . TYR A 142 ? 0.3873 0.3718 0.3916 0.0348  0.0016  0.0361  141 TYR A C   
1081 O O   . TYR A 142 ? 0.3348 0.3313 0.3533 0.0308  -0.0004 0.0339  141 TYR A O   
1082 C CB  . TYR A 142 ? 0.3929 0.3633 0.4084 0.0240  0.0116  0.0301  141 TYR A CB  
1083 C CG  . TYR A 142 ? 0.3939 0.3548 0.4103 0.0198  0.0151  0.0274  141 TYR A CG  
1084 C CD1 . TYR A 142 ? 0.3671 0.3394 0.3989 0.0173  0.0094  0.0246  141 TYR A CD1 
1085 C CD2 . TYR A 142 ? 0.4118 0.3505 0.4115 0.0174  0.0240  0.0273  141 TYR A CD2 
1086 C CE1 . TYR A 142 ? 0.3846 0.3491 0.4168 0.0118  0.0113  0.0207  141 TYR A CE1 
1087 C CE2 . TYR A 142 ? 0.4464 0.3751 0.4470 0.0111  0.0279  0.0235  141 TYR A CE2 
1088 C CZ  . TYR A 142 ? 0.4068 0.3500 0.4246 0.0080  0.0208  0.0196  141 TYR A CZ  
1089 O OH  . TYR A 142 ? 0.4326 0.3674 0.4510 0.0004  0.0232  0.0144  141 TYR A OH  
1090 N N   . ILE A 143 ? 0.3689 0.3461 0.3546 0.0405  0.0008  0.0394  142 ILE A N   
1091 C CA  . ILE A 143 ? 0.3509 0.3353 0.3310 0.0410  -0.0032 0.0397  142 ILE A CA  
1092 C C   . ILE A 143 ? 0.3931 0.3594 0.3566 0.0368  0.0041  0.0386  142 ILE A C   
1093 O O   . ILE A 143 ? 0.4388 0.3851 0.3839 0.0392  0.0095  0.0413  142 ILE A O   
1094 C CB  . ILE A 143 ? 0.3949 0.3870 0.3660 0.0514  -0.0113 0.0441  142 ILE A CB  
1095 C CG1 . ILE A 143 ? 0.3620 0.3720 0.3497 0.0550  -0.0158 0.0446  142 ILE A CG1 
1096 C CG2 . ILE A 143 ? 0.4022 0.4026 0.3656 0.0510  -0.0174 0.0436  142 ILE A CG2 
1097 C CD1 . ILE A 143 ? 0.3455 0.3757 0.3507 0.0489  -0.0196 0.0416  142 ILE A CD1 
1098 N N   . PHE A 144 ? 0.3902 0.3603 0.3578 0.0302  0.0059  0.0346  143 PHE A N   
1099 C CA  . PHE A 144 ? 0.3874 0.3397 0.3371 0.0257  0.0144  0.0329  143 PHE A CA  
1100 C C   . PHE A 144 ? 0.3919 0.3490 0.3318 0.0239  0.0097  0.0306  143 PHE A C   
1101 O O   . PHE A 144 ? 0.3539 0.3277 0.3097 0.0213  0.0044  0.0277  143 PHE A O   
1102 C CB  . PHE A 144 ? 0.3776 0.3251 0.3424 0.0174  0.0263  0.0278  143 PHE A CB  
1103 C CG  . PHE A 144 ? 0.4241 0.3559 0.3733 0.0118  0.0370  0.0245  143 PHE A CG  
1104 C CD1 . PHE A 144 ? 0.4440 0.3526 0.3682 0.0111  0.0459  0.0268  143 PHE A CD1 
1105 C CD2 . PHE A 144 ? 0.3708 0.3076 0.3264 0.0073  0.0392  0.0193  143 PHE A CD2 
1106 C CE1 . PHE A 144 ? 0.4534 0.3453 0.3592 0.0057  0.0571  0.0240  143 PHE A CE1 
1107 C CE2 . PHE A 144 ? 0.4275 0.3480 0.3658 0.0023  0.0503  0.0156  143 PHE A CE2 
1108 C CZ  . PHE A 144 ? 0.4492 0.3477 0.3622 0.0013  0.0595  0.0180  143 PHE A CZ  
1109 N N   . GLY A 145 ? 0.3929 0.3328 0.3039 0.0243  0.0122  0.0318  144 GLY A N   
1110 C CA  . GLY A 145 ? 0.4119 0.3528 0.3096 0.0203  0.0088  0.0280  144 GLY A CA  
1111 C C   . GLY A 145 ? 0.4407 0.4035 0.3418 0.0242  -0.0072 0.0289  144 GLY A C   
1112 O O   . GLY A 145 ? 0.3933 0.3679 0.2999 0.0329  -0.0160 0.0340  144 GLY A O   
1113 N N   . GLY A 146 ? 0.4080 0.3764 0.3074 0.0170  -0.0099 0.0228  145 GLY A N   
1114 C CA  . GLY A 146 ? 0.4299 0.4191 0.3306 0.0175  -0.0245 0.0217  145 GLY A CA  
1115 C C   . GLY A 146 ? 0.4603 0.4422 0.3282 0.0202  -0.0327 0.0227  145 GLY A C   
1116 O O   . GLY A 146 ? 0.5013 0.4588 0.3414 0.0229  -0.0267 0.0258  145 GLY A O   
1117 N N   . TYR A 147 ? 0.4934 0.4967 0.3635 0.0187  -0.0469 0.0198  146 TYR A N   
1118 C CA  . TYR A 147 ? 0.5082 0.5099 0.3482 0.0217  -0.0590 0.0205  146 TYR A CA  
1119 C C   . TYR A 147 ? 0.5210 0.5438 0.3672 0.0360  -0.0740 0.0279  146 TYR A C   
1120 O O   . TYR A 147 ? 0.4991 0.5529 0.3743 0.0360  -0.0823 0.0261  146 TYR A O   
1121 C CB  . TYR A 147 ? 0.5131 0.5251 0.3500 0.0089  -0.0658 0.0104  146 TYR A CB  
1122 C CG  . TYR A 147 ? 0.5521 0.5542 0.3501 0.0101  -0.0759 0.0100  146 TYR A CG  
1123 C CD1 . TYR A 147 ? 0.6107 0.5779 0.3727 0.0061  -0.0645 0.0085  146 TYR A CD1 
1124 C CD2 . TYR A 147 ? 0.5595 0.5869 0.3554 0.0161  -0.0968 0.0114  146 TYR A CD2 
1125 C CE1 . TYR A 147 ? 0.6271 0.5812 0.3466 0.0074  -0.0739 0.0087  146 TYR A CE1 
1126 C CE2 . TYR A 147 ? 0.6344 0.6523 0.3908 0.0183  -0.1086 0.0117  146 TYR A CE2 
1127 C CZ  . TYR A 147 ? 0.6640 0.6434 0.3800 0.0138  -0.0971 0.0106  146 TYR A CZ  
1128 O OH  . TYR A 147 ? 0.6503 0.6178 0.3230 0.0159  -0.1089 0.0112  146 TYR A OH  
1129 N N   . GLU A 148 ? 0.5161 0.5210 0.3352 0.0484  -0.0760 0.0363  147 GLU A N   
1130 C CA  . GLU A 148 ? 0.5600 0.5815 0.3839 0.0651  -0.0891 0.0444  147 GLU A CA  
1131 C C   . GLU A 148 ? 0.5585 0.6065 0.3780 0.0678  -0.1101 0.0423  147 GLU A C   
1132 O O   . GLU A 148 ? 0.6255 0.6612 0.4130 0.0638  -0.1160 0.0401  147 GLU A O   
1133 C CB  . GLU A 148 ? 0.5900 0.5788 0.3832 0.0780  -0.0837 0.0546  147 GLU A CB  
1134 C CG  . GLU A 148 ? 0.6030 0.5817 0.4131 0.0823  -0.0704 0.0586  147 GLU A CG  
1135 C CD  . GLU A 148 ? 0.6813 0.6195 0.4579 0.0886  -0.0598 0.0662  147 GLU A CD  
1136 O OE1 . GLU A 148 ? 0.6648 0.5941 0.4214 0.1046  -0.0676 0.0751  147 GLU A OE1 
1137 O OE2 . GLU A 148 ? 0.7135 0.6286 0.4843 0.0776  -0.0432 0.0632  147 GLU A OE2 
1138 N N   . GLN A 149 ? 0.5827 0.6678 0.4341 0.0743  -0.1213 0.0426  148 GLN A N   
1139 C CA  . GLN A 149 ? 0.6608 0.7783 0.5153 0.0755  -0.1423 0.0391  148 GLN A CA  
1140 C C   . GLN A 149 ? 0.6966 0.8073 0.5203 0.0944  -0.1571 0.0485  148 GLN A C   
1141 O O   . GLN A 149 ? 0.6603 0.7752 0.4608 0.0923  -0.1720 0.0458  148 GLN A O   
1142 C CB  . GLN A 149 ? 0.6657 0.8277 0.5671 0.0757  -0.1481 0.0357  148 GLN A CB  
1143 C CG  . GLN A 149 ? 0.7782 0.9749 0.6920 0.0641  -0.1637 0.0259  148 GLN A CG  
1144 C CD  . GLN A 149 ? 0.8473 1.0923 0.7991 0.0729  -0.1766 0.0259  148 GLN A CD  
1145 O OE1 . GLN A 149 ? 0.8837 1.1445 0.8696 0.0727  -0.1671 0.0257  148 GLN A OE1 
1146 N NE2 . GLN A 149 ? 0.8475 1.1173 0.7938 0.0812  -0.1985 0.0262  148 GLN A NE2 
1147 N N   . GLN A 150 ? 0.7601 0.8576 0.5801 0.1131  -0.1534 0.0595  149 GLN A N   
1148 C CA  . GLN A 150 ? 0.7929 0.8808 0.5822 0.1337  -0.1675 0.0699  149 GLN A CA  
1149 C C   . GLN A 150 ? 0.8250 0.8647 0.5594 0.1313  -0.1616 0.0739  149 GLN A C   
1150 O O   . GLN A 150 ? 0.8535 0.8904 0.5558 0.1347  -0.1771 0.0753  149 GLN A O   
1151 C CB  . GLN A 150 ? 0.8355 0.9198 0.6359 0.1549  -0.1637 0.0802  149 GLN A CB  
1152 C CG  . GLN A 150 ? 0.8453 0.9790 0.6930 0.1640  -0.1737 0.0784  149 GLN A CG  
1153 C CD  . GLN A 150 ? 0.9001 1.0783 0.7616 0.1620  -0.1966 0.0724  149 GLN A CD  
1154 O OE1 . GLN A 150 ? 0.8833 1.0876 0.7692 0.1422  -0.1971 0.0609  149 GLN A OE1 
1155 N NE2 . GLN A 150 ? 0.9640 1.1508 0.8096 0.1824  -0.2162 0.0801  149 GLN A NE2 
1156 N N   . ALA A 151 ? 0.7456 0.7470 0.4678 0.1251  -0.1390 0.0756  150 ALA A N   
1157 C CA  . ALA A 151 ? 0.7467 0.7020 0.4186 0.1206  -0.1296 0.0785  150 ALA A CA  
1158 C C   . ALA A 151 ? 0.7522 0.7095 0.4093 0.1025  -0.1326 0.0679  150 ALA A C   
1159 O O   . ALA A 151 ? 0.7444 0.6702 0.3537 0.1011  -0.1319 0.0701  150 ALA A O   
1160 C CB  . ALA A 151 ? 0.7226 0.6437 0.3936 0.1142  -0.1036 0.0799  150 ALA A CB  
1161 N N   . ASP A 152 ? 0.7335 0.7248 0.4276 0.0887  -0.1354 0.0565  151 ASP A N   
1162 C CA  . ASP A 152 ? 0.7090 0.7010 0.3918 0.0700  -0.1364 0.0447  151 ASP A CA  
1163 C C   . ASP A 152 ? 0.6850 0.6327 0.3391 0.0589  -0.1134 0.0426  151 ASP A C   
1164 O O   . ASP A 152 ? 0.7091 0.6293 0.3178 0.0557  -0.1128 0.0423  151 ASP A O   
1165 C CB  . ASP A 152 ? 0.6990 0.7020 0.3525 0.0742  -0.1606 0.0443  151 ASP A CB  
1166 C CG  . ASP A 152 ? 0.7039 0.7189 0.3560 0.0536  -0.1654 0.0296  151 ASP A CG  
1167 O OD1 . ASP A 152 ? 0.7178 0.7431 0.4026 0.0387  -0.1535 0.0203  151 ASP A OD1 
1168 O OD2 . ASP A 152 ? 0.7659 0.7779 0.3822 0.0524  -0.1810 0.0273  151 ASP A OD2 
1169 N N   . CYS A 153 ? 0.6353 0.5768 0.3166 0.0534  -0.0940 0.0412  152 CYS A N   
1170 C CA  . CYS A 153 ? 0.6708 0.5746 0.3322 0.0444  -0.0710 0.0395  152 CYS A CA  
1171 C C   . CYS A 153 ? 0.6539 0.5659 0.3578 0.0365  -0.0552 0.0348  152 CYS A C   
1172 O O   . CYS A 153 ? 0.6316 0.5691 0.3721 0.0415  -0.0600 0.0367  152 CYS A O   
1173 C CB  . CYS A 153 ? 0.6774 0.5450 0.3030 0.0557  -0.0631 0.0511  152 CYS A CB  
1174 S SG  . CYS A 153 ? 0.7255 0.5960 0.3804 0.0689  -0.0575 0.0608  152 CYS A SG  
1175 N N   . PHE A 154 ? 0.6391 0.5293 0.3373 0.0248  -0.0361 0.0288  153 PHE A N   
1176 C CA  . PHE A 154 ? 0.6303 0.5235 0.3644 0.0201  -0.0206 0.0265  153 PHE A CA  
1177 C C   . PHE A 154 ? 0.6033 0.4836 0.3385 0.0297  -0.0136 0.0359  153 PHE A C   
1178 O O   . PHE A 154 ? 0.6256 0.4824 0.3265 0.0371  -0.0131 0.0434  153 PHE A O   
1179 C CB  . PHE A 154 ? 0.5924 0.4660 0.3215 0.0073  -0.0015 0.0180  153 PHE A CB  
1180 C CG  . PHE A 154 ? 0.6004 0.4831 0.3310 -0.0032 -0.0054 0.0073  153 PHE A CG  
1181 C CD1 . PHE A 154 ? 0.6434 0.5126 0.3341 -0.0075 -0.0108 0.0033  153 PHE A CD1 
1182 C CD2 . PHE A 154 ? 0.5431 0.4445 0.3119 -0.0093 -0.0030 0.0010  153 PHE A CD2 
1183 C CE1 . PHE A 154 ? 0.6591 0.5342 0.3496 -0.0189 -0.0137 -0.0079 153 PHE A CE1 
1184 C CE2 . PHE A 154 ? 0.5450 0.4501 0.3135 -0.0198 -0.0048 -0.0091 153 PHE A CE2 
1185 C CZ  . PHE A 154 ? 0.5890 0.4813 0.3192 -0.0253 -0.0099 -0.0142 153 PHE A CZ  
1186 N N   . SER A 155 ? 0.5626 0.4568 0.3353 0.0295  -0.0084 0.0356  154 SER A N   
1187 C CA  . SER A 155 ? 0.5716 0.4542 0.3484 0.0361  -0.0009 0.0424  154 SER A CA  
1188 C C   . SER A 155 ? 0.5716 0.4435 0.3646 0.0261  0.0185  0.0376  154 SER A C   
1189 O O   . SER A 155 ? 0.5247 0.4102 0.3424 0.0181  0.0221  0.0301  154 SER A O   
1190 C CB  . SER A 155 ? 0.5099 0.4180 0.3158 0.0449  -0.0120 0.0460  154 SER A CB  
1191 O OG  . SER A 155 ? 0.5188 0.4143 0.3307 0.0487  -0.0030 0.0504  154 SER A OG  
1192 N N   . ASN A 156 ? 0.5466 0.3939 0.3261 0.0268  0.0310  0.0418  155 ASN A N   
1193 C CA  . ASN A 156 ? 0.5418 0.3861 0.3453 0.0187  0.0470  0.0377  155 ASN A CA  
1194 C C   . ASN A 156 ? 0.5245 0.3646 0.3365 0.0237  0.0482  0.0429  155 ASN A C   
1195 O O   . ASN A 156 ? 0.5605 0.3906 0.3823 0.0166  0.0624  0.0405  155 ASN A O   
1196 C CB  . ASN A 156 ? 0.5823 0.4009 0.3663 0.0091  0.0666  0.0340  155 ASN A CB  
1197 C CG  . ASN A 156 ? 0.6165 0.4003 0.3585 0.0118  0.0741  0.0413  155 ASN A CG  
1198 O OD1 . ASN A 156 ? 0.6314 0.4080 0.3588 0.0221  0.0649  0.0496  155 ASN A OD1 
1199 N ND2 . ASN A 156 ? 0.6319 0.3915 0.3527 0.0029  0.0924  0.0382  155 ASN A ND2 
1200 N N   . ASP A 157 ? 0.5287 0.3765 0.3376 0.0354  0.0340  0.0491  156 ASP A N   
1201 C CA  . ASP A 157 ? 0.5430 0.3870 0.3606 0.0406  0.0347  0.0530  156 ASP A CA  
1202 C C   . ASP A 157 ? 0.5195 0.3889 0.3780 0.0360  0.0334  0.0475  156 ASP A C   
1203 O O   . ASP A 157 ? 0.4949 0.3889 0.3750 0.0337  0.0265  0.0433  156 ASP A O   
1204 C CB  . ASP A 157 ? 0.5330 0.3795 0.3373 0.0563  0.0204  0.0609  156 ASP A CB  
1205 C CG  . ASP A 157 ? 0.5921 0.4121 0.3535 0.0640  0.0192  0.0681  156 ASP A CG  
1206 O OD1 . ASP A 157 ? 0.6056 0.3957 0.3429 0.0568  0.0336  0.0685  156 ASP A OD1 
1207 O OD2 . ASP A 157 ? 0.6422 0.4719 0.3943 0.0773  0.0039  0.0735  156 ASP A OD2 
1208 N N   . ILE A 158 ? 0.5387 0.4000 0.4051 0.0348  0.0395  0.0478  157 ILE A N   
1209 C CA  . ILE A 158 ? 0.4683 0.3508 0.3655 0.0345  0.0343  0.0448  157 ILE A CA  
1210 C C   . ILE A 158 ? 0.5146 0.3916 0.4026 0.0459  0.0282  0.0504  157 ILE A C   
1211 O O   . ILE A 158 ? 0.5787 0.4292 0.4478 0.0475  0.0357  0.0534  157 ILE A O   
1212 C CB  . ILE A 158 ? 0.4415 0.3225 0.3582 0.0228  0.0451  0.0387  157 ILE A CB  
1213 C CG1 . ILE A 158 ? 0.4439 0.3318 0.3728 0.0135  0.0523  0.0329  157 ILE A CG1 
1214 C CG2 . ILE A 158 ? 0.4466 0.3475 0.3891 0.0237  0.0374  0.0365  157 ILE A CG2 
1215 C CD1 . ILE A 158 ? 0.4827 0.3702 0.4319 0.0022  0.0641  0.0266  157 ILE A CD1 
1216 N N   . HIS A 159 ? 0.4825 0.3829 0.3834 0.0538  0.0161  0.0516  158 HIS A N   
1217 C CA  . HIS A 159 ? 0.4776 0.3784 0.3779 0.0646  0.0114  0.0552  158 HIS A CA  
1218 C C   . HIS A 159 ? 0.4557 0.3721 0.3819 0.0590  0.0111  0.0502  158 HIS A C   
1219 O O   . HIS A 159 ? 0.4536 0.3923 0.4004 0.0536  0.0068  0.0467  158 HIS A O   
1220 C CB  . HIS A 159 ? 0.4604 0.3790 0.3591 0.0773  -0.0009 0.0595  158 HIS A CB  
1221 C CG  . HIS A 159 ? 0.5332 0.4364 0.4031 0.0859  -0.0037 0.0656  158 HIS A CG  
1222 N ND1 . HIS A 159 ? 0.5221 0.4252 0.3811 0.0804  -0.0053 0.0647  158 HIS A ND1 
1223 C CD2 . HIS A 159 ? 0.5595 0.4455 0.4069 0.1005  -0.0059 0.0730  158 HIS A CD2 
1224 C CE1 . HIS A 159 ? 0.5437 0.4304 0.3732 0.0907  -0.0092 0.0714  158 HIS A CE1 
1225 N NE2 . HIS A 159 ? 0.5485 0.4247 0.3710 0.1038  -0.0099 0.0770  158 HIS A NE2 
1226 N N   . LYS A 160 ? 0.4575 0.3591 0.3800 0.0596  0.0159  0.0496  159 LYS A N   
1227 C CA  . LYS A 160 ? 0.4594 0.3739 0.4013 0.0554  0.0141  0.0451  159 LYS A CA  
1228 C C   . LYS A 160 ? 0.4899 0.4067 0.4279 0.0675  0.0101  0.0479  159 LYS A C   
1229 O O   . LYS A 160 ? 0.4982 0.3954 0.4168 0.0774  0.0130  0.0520  159 LYS A O   
1230 C CB  . LYS A 160 ? 0.4620 0.3609 0.4052 0.0441  0.0222  0.0399  159 LYS A CB  
1231 C CG  . LYS A 160 ? 0.5334 0.3995 0.4523 0.0465  0.0307  0.0417  159 LYS A CG  
1232 C CD  . LYS A 160 ? 0.4926 0.3468 0.4164 0.0324  0.0383  0.0347  159 LYS A CD  
1233 C CE  . LYS A 160 ? 0.5224 0.3392 0.4193 0.0333  0.0485  0.0360  159 LYS A CE  
1234 N NZ  . LYS A 160 ? 0.5570 0.3615 0.4587 0.0163  0.0576  0.0282  159 LYS A NZ  
1235 N N   . LEU A 161 ? 0.4475 0.3871 0.4032 0.0675  0.0045  0.0459  160 LEU A N   
1236 C CA  . LEU A 161 ? 0.4666 0.4106 0.4219 0.0772  0.0030  0.0470  160 LEU A CA  
1237 C C   . LEU A 161 ? 0.4487 0.3863 0.4066 0.0700  0.0058  0.0418  160 LEU A C   
1238 O O   . LEU A 161 ? 0.4265 0.3780 0.3988 0.0611  0.0024  0.0386  160 LEU A O   
1239 C CB  . LEU A 161 ? 0.4426 0.4162 0.4137 0.0816  -0.0039 0.0484  160 LEU A CB  
1240 C CG  . LEU A 161 ? 0.4451 0.4264 0.4193 0.0903  -0.0032 0.0485  160 LEU A CG  
1241 C CD1 . LEU A 161 ? 0.4385 0.4089 0.3997 0.1061  -0.0012 0.0525  160 LEU A CD1 
1242 C CD2 . LEU A 161 ? 0.4213 0.4323 0.4142 0.0891  -0.0079 0.0483  160 LEU A CD2 
1243 N N   . ASP A 162 ? 0.4838 0.3987 0.4259 0.0743  0.0114  0.0410  161 ASP A N   
1244 C CA  . ASP A 162 ? 0.4680 0.3748 0.4082 0.0677  0.0135  0.0352  161 ASP A CA  
1245 C C   . ASP A 162 ? 0.4913 0.4109 0.4342 0.0763  0.0118  0.0356  161 ASP A C   
1246 O O   . ASP A 162 ? 0.5035 0.4131 0.4355 0.0886  0.0162  0.0376  161 ASP A O   
1247 C CB  . ASP A 162 ? 0.5121 0.3850 0.4317 0.0665  0.0219  0.0329  161 ASP A CB  
1248 C CG  . ASP A 162 ? 0.5452 0.4089 0.4618 0.0562  0.0231  0.0250  161 ASP A CG  
1249 O OD1 . ASP A 162 ? 0.5068 0.3889 0.4335 0.0535  0.0171  0.0225  161 ASP A OD1 
1250 O OD2 . ASP A 162 ? 0.5816 0.4179 0.4838 0.0501  0.0301  0.0211  161 ASP A OD2 
1251 N N   . THR A 163 ? 0.4947 0.4353 0.4515 0.0704  0.0065  0.0341  162 THR A N   
1252 C CA  . THR A 163 ? 0.4627 0.4166 0.4223 0.0774  0.0068  0.0349  162 THR A CA  
1253 C C   . THR A 163 ? 0.4631 0.3987 0.4065 0.0795  0.0125  0.0307  162 THR A C   
1254 O O   . THR A 163 ? 0.4875 0.4301 0.4302 0.0873  0.0160  0.0311  162 THR A O   
1255 C CB  . THR A 163 ? 0.4341 0.4100 0.4084 0.0700  0.0011  0.0350  162 THR A CB  
1256 O OG1 . THR A 163 ? 0.4575 0.4262 0.4279 0.0599  -0.0017 0.0309  162 THR A OG1 
1257 C CG2 . THR A 163 ? 0.4103 0.4001 0.3985 0.0666  -0.0034 0.0378  162 THR A CG2 
1258 N N   . SER A 164 ? 0.4638 0.3760 0.3941 0.0721  0.0145  0.0258  163 SER A N   
1259 C CA  . SER A 164 ? 0.5302 0.4207 0.4412 0.0732  0.0205  0.0206  163 SER A CA  
1260 C C   . SER A 164 ? 0.5780 0.4527 0.4773 0.0889  0.0294  0.0230  163 SER A C   
1261 O O   . SER A 164 ? 0.6222 0.4880 0.5103 0.0958  0.0359  0.0203  163 SER A O   
1262 C CB  . SER A 164 ? 0.5161 0.3858 0.4170 0.0597  0.0202  0.0137  163 SER A CB  
1263 O OG  . SER A 164 ? 0.6216 0.5076 0.5333 0.0477  0.0110  0.0109  163 SER A OG  
1264 N N   . THR A 165 ? 0.5485 0.4178 0.4483 0.0955  0.0303  0.0281  164 THR A N   
1265 C CA  . THR A 165 ? 0.5640 0.4198 0.4538 0.1133  0.0367  0.0324  164 THR A CA  
1266 C C   . THR A 165 ? 0.5462 0.4284 0.4522 0.1250  0.0313  0.0400  164 THR A C   
1267 O O   . THR A 165 ? 0.5709 0.4464 0.4714 0.1419  0.0342  0.0447  164 THR A O   
1268 C CB  . THR A 165 ? 0.5873 0.4055 0.4560 0.1124  0.0429  0.0323  164 THR A CB  
1269 O OG1 . THR A 165 ? 0.5432 0.3658 0.4178 0.1049  0.0383  0.0358  164 THR A OG1 
1270 C CG2 . THR A 165 ? 0.6209 0.4136 0.4744 0.0983  0.0478  0.0232  164 THR A CG2 
1271 N N   . MET A 166 ? 0.5216 0.4324 0.4467 0.1168  0.0231  0.0413  165 MET A N   
1272 C CA  . MET A 166 ? 0.5000 0.4365 0.4402 0.1246  0.0168  0.0470  165 MET A CA  
1273 C C   . MET A 166 ? 0.5217 0.4410 0.4487 0.1335  0.0162  0.0525  165 MET A C   
1274 O O   . MET A 166 ? 0.5079 0.4342 0.4359 0.1498  0.0143  0.0576  165 MET A O   
1275 C CB  . MET A 166 ? 0.4583 0.4186 0.4119 0.1369  0.0178  0.0480  165 MET A CB  
1276 C CG  . MET A 166 ? 0.4687 0.4501 0.4360 0.1265  0.0176  0.0442  165 MET A CG  
1277 S SD  . MET A 166 ? 0.5054 0.5077 0.4883 0.1112  0.0080  0.0451  165 MET A SD  
1278 C CE  . MET A 166 ? 0.3909 0.4076 0.3820 0.1015  0.0100  0.0418  165 MET A CE  
1279 N N   . THR A 167 ? 0.5191 0.4156 0.4335 0.1227  0.0181  0.0516  166 THR A N   
1280 C CA  . THR A 167 ? 0.5532 0.4254 0.4487 0.1288  0.0200  0.0569  166 THR A CA  
1281 C C   . THR A 167 ? 0.5394 0.4184 0.4384 0.1173  0.0157  0.0578  166 THR A C   
1282 O O   . THR A 167 ? 0.5140 0.3937 0.4199 0.1009  0.0171  0.0526  166 THR A O   
1283 C CB  . THR A 167 ? 0.5657 0.3957 0.4370 0.1264  0.0306  0.0546  166 THR A CB  
1284 O OG1 . THR A 167 ? 0.5288 0.3497 0.3945 0.1377  0.0357  0.0530  166 THR A OG1 
1285 C CG2 . THR A 167 ? 0.5459 0.3467 0.3936 0.1333  0.0338  0.0615  166 THR A CG2 
1286 N N   . TRP A 168 ? 0.5081 0.3917 0.4017 0.1267  0.0104  0.0642  167 TRP A N   
1287 C CA  . TRP A 168 ? 0.5290 0.4142 0.4201 0.1178  0.0077  0.0653  167 TRP A CA  
1288 C C   . TRP A 168 ? 0.5569 0.4023 0.4200 0.1155  0.0165  0.0679  167 TRP A C   
1289 O O   . TRP A 168 ? 0.6113 0.4308 0.4525 0.1286  0.0201  0.0733  167 TRP A O   
1290 C CB  . TRP A 168 ? 0.5282 0.4364 0.4232 0.1280  -0.0030 0.0702  167 TRP A CB  
1291 C CG  . TRP A 168 ? 0.4705 0.4184 0.3934 0.1254  -0.0108 0.0670  167 TRP A CG  
1292 C CD1 . TRP A 168 ? 0.4891 0.4617 0.4270 0.1371  -0.0159 0.0680  167 TRP A CD1 
1293 C CD2 . TRP A 168 ? 0.4517 0.4185 0.3909 0.1102  -0.0133 0.0623  167 TRP A CD2 
1294 N NE1 . TRP A 168 ? 0.4364 0.4413 0.3981 0.1281  -0.0208 0.0640  167 TRP A NE1 
1295 C CE2 . TRP A 168 ? 0.4350 0.4350 0.3965 0.1122  -0.0196 0.0608  167 TRP A CE2 
1296 C CE3 . TRP A 168 ? 0.4724 0.4307 0.4103 0.0954  -0.0098 0.0590  167 TRP A CE3 
1297 C CZ2 . TRP A 168 ? 0.4479 0.4682 0.4266 0.0996  -0.0224 0.0567  167 TRP A CZ2 
1298 C CZ3 . TRP A 168 ? 0.4120 0.3922 0.3686 0.0850  -0.0132 0.0550  167 TRP A CZ3 
1299 C CH2 . TRP A 168 ? 0.4104 0.4193 0.3856 0.0869  -0.0194 0.0541  167 TRP A CH2 
1300 N N   . THR A 169 ? 0.5590 0.3989 0.4229 0.0990  0.0211  0.0642  168 THR A N   
1301 C CA  . THR A 169 ? 0.5446 0.3494 0.3834 0.0937  0.0310  0.0663  168 THR A CA  
1302 C C   . THR A 169 ? 0.5949 0.4088 0.4335 0.0865  0.0292  0.0668  168 THR A C   
1303 O O   . THR A 169 ? 0.5776 0.4172 0.4398 0.0759  0.0263  0.0613  168 THR A O   
1304 C CB  . THR A 169 ? 0.5774 0.3639 0.4181 0.0778  0.0423  0.0592  168 THR A CB  
1305 O OG1 . THR A 169 ? 0.6246 0.4034 0.4648 0.0831  0.0436  0.0570  168 THR A OG1 
1306 C CG2 . THR A 169 ? 0.5465 0.2939 0.3602 0.0712  0.0554  0.0611  168 THR A CG2 
1307 N N   . LEU A 170 ? 0.6250 0.4157 0.4344 0.0930  0.0311  0.0737  169 LEU A N   
1308 C CA  . LEU A 170 ? 0.6166 0.4041 0.4176 0.0833  0.0344  0.0732  169 LEU A CA  
1309 C C   . LEU A 170 ? 0.6122 0.3746 0.4085 0.0668  0.0511  0.0685  169 LEU A C   
1310 O O   . LEU A 170 ? 0.6413 0.3672 0.4122 0.0679  0.0612  0.0719  169 LEU A O   
1311 C CB  . LEU A 170 ? 0.6230 0.3932 0.3904 0.0962  0.0299  0.0824  169 LEU A CB  
1312 C CG  . LEU A 170 ? 0.6413 0.4007 0.3917 0.0858  0.0356  0.0818  169 LEU A CG  
1313 C CD1 . LEU A 170 ? 0.6105 0.4052 0.3915 0.0745  0.0313  0.0736  169 LEU A CD1 
1314 C CD2 . LEU A 170 ? 0.6204 0.3650 0.3352 0.0996  0.0278  0.0911  169 LEU A CD2 
1315 N N   . ILE A 171 ? 0.5825 0.3911 0.4663 0.0398  0.0395  0.0229  170 ILE A N   
1316 C CA  . ILE A 171 ? 0.5569 0.3491 0.4444 0.0276  0.0364  0.0214  170 ILE A CA  
1317 C C   . ILE A 171 ? 0.5672 0.3612 0.4614 0.0222  0.0393  0.0322  170 ILE A C   
1318 O O   . ILE A 171 ? 0.6101 0.4259 0.5089 0.0205  0.0420  0.0367  170 ILE A O   
1319 C CB  . ILE A 171 ? 0.5599 0.3635 0.4540 0.0177  0.0331  0.0142  170 ILE A CB  
1320 C CG1 . ILE A 171 ? 0.5773 0.3778 0.4628 0.0235  0.0307  0.0041  170 ILE A CG1 
1321 C CG2 . ILE A 171 ? 0.5758 0.3651 0.4775 0.0046  0.0291  0.0147  170 ILE A CG2 
1322 C CD1 . ILE A 171 ? 0.5426 0.3531 0.4336 0.0145  0.0270  -0.0024 170 ILE A CD1 
1323 N N   . CYS A 172 ? 0.5875 0.3572 0.4808 0.0197  0.0387  0.0367  171 CYS A N   
1324 C CA  A CYS A 172 ? 0.6300 0.3999 0.5311 0.0131  0.0421  0.0481  171 CYS A CA  
1325 C CA  B CYS A 172 ? 0.6054 0.3752 0.5064 0.0131  0.0421  0.0481  171 CYS A CA  
1326 C C   . CYS A 172 ? 0.6074 0.3838 0.5220 -0.0013 0.0402  0.0471  171 CYS A C   
1327 O O   . CYS A 172 ? 0.6443 0.4024 0.5643 -0.0100 0.0352  0.0451  171 CYS A O   
1328 C CB  A CYS A 172 ? 0.6731 0.4143 0.5704 0.0150  0.0421  0.0545  171 CYS A CB  
1329 C CB  B CYS A 172 ? 0.6267 0.3677 0.5237 0.0153  0.0421  0.0542  171 CYS A CB  
1330 S SG  A CYS A 172 ? 0.6157 0.3583 0.5215 0.0095  0.0484  0.0717  171 CYS A SG  
1331 S SG  B CYS A 172 ? 0.6534 0.3844 0.5347 0.0343  0.0441  0.0546  171 CYS A SG  
1332 N N   . THR A 173 ? 0.5858 0.3878 0.5058 -0.0036 0.0436  0.0485  172 THR A N   
1333 C CA  . THR A 173 ? 0.5749 0.3861 0.5085 -0.0153 0.0426  0.0477  172 THR A CA  
1334 C C   . THR A 173 ? 0.5697 0.3787 0.5153 -0.0230 0.0471  0.0605  172 THR A C   
1335 O O   . THR A 173 ? 0.5850 0.3899 0.5263 -0.0184 0.0526  0.0705  172 THR A O   
1336 C CB  . THR A 173 ? 0.5841 0.4213 0.5180 -0.0140 0.0450  0.0441  172 THR A CB  
1337 O OG1 . THR A 173 ? 0.5604 0.4093 0.4896 -0.0090 0.0517  0.0524  172 THR A OG1 
1338 C CG2 . THR A 173 ? 0.5480 0.3899 0.4727 -0.0070 0.0411  0.0333  172 THR A CG2 
1339 N N   . LYS A 174 ? 0.5838 0.3964 0.5453 -0.0344 0.0451  0.0614  173 LYS A N   
1340 C CA  . LYS A 174 ? 0.5937 0.4125 0.5711 -0.0420 0.0511  0.0751  173 LYS A CA  
1341 C C   . LYS A 174 ? 0.5592 0.4048 0.5416 -0.0417 0.0576  0.0764  173 LYS A C   
1342 O O   . LYS A 174 ? 0.5221 0.3789 0.4975 -0.0379 0.0553  0.0660  173 LYS A O   
1343 C CB  . LYS A 174 ? 0.5272 0.3315 0.5224 -0.0556 0.0439  0.0774  173 LYS A CB  
1344 N N   . GLY A 175 ? 0.4934 0.3486 0.4869 -0.0446 0.0665  0.0900  174 GLY A N   
1345 C CA  . GLY A 175 ? 0.5215 0.3995 0.5180 -0.0428 0.0742  0.0922  174 GLY A CA  
1346 C C   . GLY A 175 ? 0.5501 0.4360 0.5243 -0.0305 0.0797  0.0899  174 GLY A C   
1347 O O   . GLY A 175 ? 0.5851 0.4618 0.5430 -0.0234 0.0775  0.0873  174 GLY A O   
1348 N N   . SER A 176 ? 0.5054 0.4081 0.4784 -0.0278 0.0865  0.0909  175 SER A N   
1349 C CA  . SER A 176 ? 0.5036 0.4117 0.4538 -0.0172 0.0904  0.0884  175 SER A CA  
1350 C C   . SER A 176 ? 0.5960 0.5073 0.5371 -0.0149 0.0817  0.0733  175 SER A C   
1351 O O   . SER A 176 ? 0.5598 0.4804 0.5077 -0.0180 0.0801  0.0668  175 SER A O   
1352 C CB  . SER A 176 ? 0.4962 0.4171 0.4444 -0.0136 0.1016  0.0953  175 SER A CB  
1353 O OG  . SER A 176 ? 0.6470 0.5673 0.6056 -0.0152 0.1113  0.1113  175 SER A OG  
1354 N N   . PRO A 177 ? 0.5585 0.4634 0.4852 -0.0091 0.0764  0.0687  176 PRO A N   
1355 C CA  . PRO A 177 ? 0.5206 0.4301 0.4415 -0.0072 0.0686  0.0562  176 PRO A CA  
1356 C C   . PRO A 177 ? 0.5372 0.4586 0.4489 -0.0043 0.0705  0.0523  176 PRO A C   
1357 O O   . PRO A 177 ? 0.5898 0.5135 0.4919 -0.0005 0.0773  0.0583  176 PRO A O   
1358 C CB  . PRO A 177 ? 0.5032 0.4054 0.4124 -0.0004 0.0645  0.0563  176 PRO A CB  
1359 C CG  . PRO A 177 ? 0.5904 0.4868 0.4928 0.0032  0.0709  0.0684  176 PRO A CG  
1360 C CD  . PRO A 177 ? 0.5399 0.4349 0.4561 -0.0035 0.0780  0.0764  176 PRO A CD  
1361 N N   . ALA A 178 ? 0.5310 0.4586 0.4450 -0.0060 0.0647  0.0421  177 ALA A N   
1362 C CA  . ALA A 178 ? 0.4956 0.4317 0.4001 -0.0036 0.0649  0.0373  177 ALA A CA  
1363 C C   . ALA A 178 ? 0.5034 0.4384 0.3891 0.0030  0.0619  0.0375  177 ALA A C   
1364 O O   . ALA A 178 ? 0.5304 0.4620 0.4138 0.0057  0.0575  0.0388  177 ALA A O   
1365 C CB  . ALA A 178 ? 0.4700 0.4120 0.3818 -0.0070 0.0589  0.0275  177 ALA A CB  
1366 N N   . ARG A 179 ? 0.4912 0.4284 0.3628 0.0061  0.0638  0.0365  178 ARG A N   
1367 C CA  . ARG A 179 ? 0.4911 0.4259 0.3426 0.0118  0.0596  0.0371  178 ARG A CA  
1368 C C   . ARG A 179 ? 0.5106 0.4504 0.3639 0.0111  0.0484  0.0309  178 ARG A C   
1369 O O   . ARG A 179 ? 0.4667 0.4122 0.3294 0.0072  0.0446  0.0239  178 ARG A O   
1370 C CB  . ARG A 179 ? 0.5388 0.4717 0.3724 0.0150  0.0628  0.0352  178 ARG A CB  
1371 C CG  . ARG A 179 ? 0.5607 0.4901 0.3716 0.0193  0.0546  0.0326  178 ARG A CG  
1372 C CD  . ARG A 179 ? 0.5681 0.4909 0.3577 0.0232  0.0583  0.0298  178 ARG A CD  
1373 N NE  . ARG A 179 ? 0.5937 0.5135 0.3814 0.0272  0.0726  0.0381  178 ARG A NE  
1374 C CZ  . ARG A 179 ? 0.5934 0.5076 0.3671 0.0334  0.0787  0.0473  178 ARG A CZ  
1375 N NH1 . ARG A 179 ? 0.5809 0.4904 0.3371 0.0371  0.0709  0.0486  178 ARG A NH1 
1376 N NH2 . ARG A 179 ? 0.6223 0.5367 0.4008 0.0360  0.0928  0.0565  178 ARG A NH2 
1377 N N   . TRP A 180 ? 0.5244 0.4630 0.3699 0.0155  0.0437  0.0350  179 TRP A N   
1378 C CA  . TRP A 180 ? 0.5043 0.4501 0.3513 0.0161  0.0332  0.0318  179 TRP A CA  
1379 C C   . TRP A 180 ? 0.4905 0.4411 0.3331 0.0127  0.0272  0.0242  179 TRP A C   
1380 O O   . TRP A 180 ? 0.5106 0.4556 0.3376 0.0133  0.0287  0.0224  179 TRP A O   
1381 C CB  . TRP A 180 ? 0.5160 0.4605 0.3502 0.0220  0.0284  0.0384  179 TRP A CB  
1382 C CG  . TRP A 180 ? 0.5330 0.4688 0.3630 0.0266  0.0354  0.0476  179 TRP A CG  
1383 C CD1 . TRP A 180 ? 0.5424 0.4760 0.3807 0.0299  0.0357  0.0532  179 TRP A CD1 
1384 C CD2 . TRP A 180 ? 0.5314 0.4587 0.3467 0.0292  0.0434  0.0535  179 TRP A CD2 
1385 N NE1 . TRP A 180 ? 0.5156 0.4394 0.3466 0.0332  0.0427  0.0621  179 TRP A NE1 
1386 C CE2 . TRP A 180 ? 0.5616 0.4824 0.3790 0.0329  0.0479  0.0630  179 TRP A CE2 
1387 C CE3 . TRP A 180 ? 0.5423 0.4660 0.3421 0.0298  0.0480  0.0521  179 TRP A CE3 
1388 C CZ2 . TRP A 180 ? 0.5740 0.4866 0.3804 0.0362  0.0571  0.0723  179 TRP A CZ2 
1389 C CZ3 . TRP A 180 ? 0.5737 0.4897 0.3615 0.0344  0.0580  0.0611  179 TRP A CZ3 
1390 C CH2 . TRP A 180 ? 0.5142 0.4256 0.3063 0.0371  0.0624  0.0715  179 TRP A CH2 
1391 N N   . ARG A 181 ? 0.4392 0.3990 0.2949 0.0097  0.0208  0.0200  180 ARG A N   
1392 C CA  . ARG A 181 ? 0.5003 0.4634 0.3555 0.0050  0.0162  0.0130  180 ARG A CA  
1393 C C   . ARG A 181 ? 0.4537 0.4289 0.3259 0.0025  0.0100  0.0114  180 ARG A C   
1394 O O   . ARG A 181 ? 0.4400 0.4195 0.3245 0.0048  0.0123  0.0141  180 ARG A O   
1395 C CB  . ARG A 181 ? 0.4442 0.4029 0.3019 0.0023  0.0245  0.0090  180 ARG A CB  
1396 C CG  . ARG A 181 ? 0.4446 0.4073 0.3213 0.0000  0.0288  0.0084  180 ARG A CG  
1397 C CD  . ARG A 181 ? 0.4505 0.4106 0.3313 -0.0027 0.0358  0.0059  180 ARG A CD  
1398 N NE  . ARG A 181 ? 0.4645 0.4183 0.3417 -0.0007 0.0441  0.0115  180 ARG A NE  
1399 C CZ  . ARG A 181 ? 0.4797 0.4320 0.3582 -0.0015 0.0514  0.0122  180 ARG A CZ  
1400 N NH1 . ARG A 181 ? 0.4848 0.4401 0.3666 -0.0037 0.0513  0.0069  180 ARG A NH1 
1401 N NH2 . ARG A 181 ? 0.4510 0.3996 0.3288 0.0004  0.0595  0.0195  180 ARG A NH2 
1402 N N   . ASP A 182 ? 0.4092 0.3885 0.2812 -0.0019 0.0028  0.0072  181 ASP A N   
1403 C CA  . ASP A 182 ? 0.4314 0.4233 0.3213 -0.0048 -0.0015 0.0067  181 ASP A CA  
1404 C C   . ASP A 182 ? 0.4485 0.4392 0.3401 -0.0106 -0.0023 0.0005  181 ASP A C   
1405 O O   . ASP A 182 ? 0.4272 0.4071 0.3046 -0.0120 -0.0016 -0.0037 181 ASP A O   
1406 C CB  . ASP A 182 ? 0.4295 0.4328 0.3244 -0.0043 -0.0122 0.0120  181 ASP A CB  
1407 C CG  . ASP A 182 ? 0.4562 0.4551 0.3364 -0.0080 -0.0233 0.0104  181 ASP A CG  
1408 O OD1 . ASP A 182 ? 0.4842 0.4702 0.3488 -0.0104 -0.0227 0.0043  181 ASP A OD1 
1409 O OD2 . ASP A 182 ? 0.4846 0.4924 0.3681 -0.0080 -0.0334 0.0155  181 ASP A OD2 
1410 N N   . PHE A 183 ? 0.3985 0.3999 0.3071 -0.0129 -0.0029 0.0004  182 PHE A N   
1411 C CA  . PHE A 183 ? 0.4071 0.4086 0.3203 -0.0182 -0.0034 -0.0042 182 PHE A CA  
1412 C C   . PHE A 183 ? 0.3861 0.3775 0.2934 -0.0179 0.0052  -0.0087 182 PHE A C   
1413 O O   . PHE A 183 ? 0.4037 0.3898 0.3074 -0.0210 0.0051  -0.0129 182 PHE A O   
1414 C CB  . PHE A 183 ? 0.4106 0.4100 0.3176 -0.0235 -0.0140 -0.0058 182 PHE A CB  
1415 C CG  . PHE A 183 ? 0.4309 0.4443 0.3499 -0.0253 -0.0235 0.0002  182 PHE A CG  
1416 C CD1 . PHE A 183 ? 0.3671 0.3948 0.3065 -0.0282 -0.0246 0.0037  182 PHE A CD1 
1417 C CD2 . PHE A 183 ? 0.4290 0.4431 0.3406 -0.0232 -0.0304 0.0040  182 PHE A CD2 
1418 C CE1 . PHE A 183 ? 0.3683 0.4122 0.3227 -0.0293 -0.0323 0.0113  182 PHE A CE1 
1419 C CE2 . PHE A 183 ? 0.4251 0.4552 0.3514 -0.0246 -0.0393 0.0112  182 PHE A CE2 
1420 C CZ  . PHE A 183 ? 0.3590 0.4047 0.3079 -0.0277 -0.0400 0.0151  182 PHE A CZ  
1421 N N   . HIS A 184 ? 0.3708 0.3595 0.2783 -0.0140 0.0123  -0.0070 183 HIS A N   
1422 C CA  . HIS A 184 ? 0.3868 0.3701 0.2956 -0.0141 0.0201  -0.0091 183 HIS A CA  
1423 C C   . HIS A 184 ? 0.3915 0.3812 0.3140 -0.0154 0.0215  -0.0105 183 HIS A C   
1424 O O   . HIS A 184 ? 0.3745 0.3726 0.3046 -0.0153 0.0180  -0.0094 183 HIS A O   
1425 C CB  . HIS A 184 ? 0.3999 0.3776 0.3052 -0.0107 0.0254  -0.0054 183 HIS A CB  
1426 C CG  . HIS A 184 ? 0.3742 0.3552 0.2860 -0.0077 0.0244  -0.0022 183 HIS A CG  
1427 N ND1 . HIS A 184 ? 0.3866 0.3720 0.2963 -0.0049 0.0193  0.0013  183 HIS A ND1 
1428 C CD2 . HIS A 184 ? 0.3870 0.3666 0.3065 -0.0066 0.0274  -0.0020 183 HIS A CD2 
1429 C CE1 . HIS A 184 ? 0.3981 0.3850 0.3144 -0.0010 0.0206  0.0040  183 HIS A CE1 
1430 N NE2 . HIS A 184 ? 0.4084 0.3901 0.3291 -0.0019 0.0254  0.0014  183 HIS A NE2 
1431 N N   . SER A 185 ? 0.3604 0.3467 0.2861 -0.0161 0.0267  -0.0120 184 SER A N   
1432 C CA  . SER A 185 ? 0.3670 0.3566 0.3021 -0.0164 0.0276  -0.0133 184 SER A CA  
1433 C C   . SER A 185 ? 0.3721 0.3553 0.3086 -0.0156 0.0309  -0.0123 184 SER A C   
1434 O O   . SER A 185 ? 0.3630 0.3410 0.2966 -0.0161 0.0341  -0.0101 184 SER A O   
1435 C CB  . SER A 185 ? 0.3462 0.3382 0.2858 -0.0194 0.0281  -0.0162 184 SER A CB  
1436 O OG  . SER A 185 ? 0.3510 0.3383 0.2892 -0.0205 0.0321  -0.0166 184 SER A OG  
1437 N N   . ALA A 186 ? 0.3579 0.3405 0.2982 -0.0142 0.0301  -0.0136 185 ALA A N   
1438 C CA  . ALA A 186 ? 0.3588 0.3326 0.3003 -0.0148 0.0310  -0.0138 185 ALA A CA  
1439 C C   . ALA A 186 ? 0.3946 0.3687 0.3389 -0.0155 0.0291  -0.0177 185 ALA A C   
1440 O O   . ALA A 186 ? 0.4239 0.4020 0.3665 -0.0119 0.0282  -0.0189 185 ALA A O   
1441 C CB  . ALA A 186 ? 0.3281 0.2947 0.2652 -0.0104 0.0311  -0.0115 185 ALA A CB  
1442 N N   . THR A 187 ? 0.3903 0.3612 0.3392 -0.0199 0.0284  -0.0187 186 THR A N   
1443 C CA  . THR A 187 ? 0.3843 0.3555 0.3348 -0.0211 0.0253  -0.0222 186 THR A CA  
1444 C C   . THR A 187 ? 0.3870 0.3474 0.3388 -0.0245 0.0217  -0.0232 186 THR A C   
1445 O O   . THR A 187 ? 0.3663 0.3249 0.3253 -0.0290 0.0224  -0.0197 186 THR A O   
1446 C CB  . THR A 187 ? 0.3765 0.3569 0.3336 -0.0242 0.0262  -0.0219 186 THR A CB  
1447 O OG1 . THR A 187 ? 0.3666 0.3536 0.3219 -0.0225 0.0286  -0.0209 186 THR A OG1 
1448 C CG2 . THR A 187 ? 0.2878 0.2696 0.2449 -0.0243 0.0227  -0.0248 186 THR A CG2 
1449 N N   . MET A 188 ? 0.4197 0.3722 0.3641 -0.0222 0.0176  -0.0274 187 MET A N   
1450 C CA  . MET A 188 ? 0.4012 0.3398 0.3440 -0.0258 0.0115  -0.0297 187 MET A CA  
1451 C C   . MET A 188 ? 0.3949 0.3385 0.3454 -0.0316 0.0065  -0.0305 187 MET A C   
1452 O O   . MET A 188 ? 0.4352 0.3849 0.3821 -0.0291 0.0058  -0.0328 187 MET A O   
1453 C CB  . MET A 188 ? 0.4009 0.3254 0.3274 -0.0187 0.0095  -0.0346 187 MET A CB  
1454 C CG  . MET A 188 ? 0.5153 0.4183 0.4352 -0.0206 0.0038  -0.0372 187 MET A CG  
1455 S SD  . MET A 188 ? 0.5163 0.4121 0.4427 -0.0232 0.0067  -0.0313 187 MET A SD  
1456 C CE  . MET A 188 ? 0.4063 0.3154 0.3302 -0.0143 0.0156  -0.0281 187 MET A CE  
1457 N N   . LEU A 189 ? 0.4189 0.3621 0.3818 -0.0392 0.0036  -0.0270 188 LEU A N   
1458 C CA  . LEU A 189 ? 0.4228 0.3703 0.3953 -0.0454 -0.0031 -0.0267 188 LEU A CA  
1459 C C   . LEU A 189 ? 0.4245 0.3565 0.3982 -0.0519 -0.0124 -0.0276 188 LEU A C   
1460 O O   . LEU A 189 ? 0.4245 0.3553 0.4103 -0.0574 -0.0114 -0.0219 188 LEU A O   
1461 C CB  . LEU A 189 ? 0.4041 0.3686 0.3951 -0.0489 0.0018  -0.0196 188 LEU A CB  
1462 C CG  . LEU A 189 ? 0.3820 0.3594 0.3719 -0.0437 0.0090  -0.0192 188 LEU A CG  
1463 C CD1 . LEU A 189 ? 0.3628 0.3530 0.3683 -0.0457 0.0144  -0.0125 188 LEU A CD1 
1464 C CD2 . LEU A 189 ? 0.3455 0.3245 0.3280 -0.0410 0.0049  -0.0238 188 LEU A CD2 
1465 N N   . GLY A 190 ? 0.4001 0.3189 0.3601 -0.0512 -0.0215 -0.0344 189 GLY A N   
1466 C CA  . GLY A 190 ? 0.4740 0.3725 0.4304 -0.0571 -0.0319 -0.0370 189 GLY A CA  
1467 C C   . GLY A 190 ? 0.5105 0.3923 0.4549 -0.0523 -0.0277 -0.0385 189 GLY A C   
1468 O O   . GLY A 190 ? 0.5099 0.3870 0.4371 -0.0420 -0.0224 -0.0428 189 GLY A O   
1469 N N   . SER A 191 ? 0.4956 0.3693 0.4507 -0.0594 -0.0296 -0.0338 190 SER A N   
1470 C CA  . SER A 191 ? 0.4880 0.3458 0.4334 -0.0549 -0.0254 -0.0338 190 SER A CA  
1471 C C   . SER A 191 ? 0.4795 0.3523 0.4364 -0.0531 -0.0135 -0.0252 190 SER A C   
1472 O O   . SER A 191 ? 0.5092 0.3708 0.4612 -0.0501 -0.0099 -0.0231 190 SER A O   
1473 C CB  . SER A 191 ? 0.5214 0.3555 0.4674 -0.0633 -0.0358 -0.0341 190 SER A CB  
1474 O OG  . SER A 191 ? 0.6724 0.4849 0.5978 -0.0616 -0.0467 -0.0444 190 SER A OG  
1475 N N   . HIS A 192 ? 0.5124 0.4084 0.4826 -0.0541 -0.0075 -0.0204 191 HIS A N   
1476 C CA  . HIS A 192 ? 0.4396 0.3479 0.4191 -0.0530 0.0028  -0.0123 191 HIS A CA  
1477 C C   . HIS A 192 ? 0.4049 0.3251 0.3754 -0.0440 0.0103  -0.0143 191 HIS A C   
1478 O O   . HIS A 192 ? 0.3865 0.3158 0.3550 -0.0421 0.0095  -0.0182 191 HIS A O   
1479 C CB  . HIS A 192 ? 0.4291 0.3526 0.4307 -0.0607 0.0044  -0.0040 191 HIS A CB  
1480 C CG  . HIS A 192 ? 0.4810 0.3955 0.4967 -0.0710 -0.0024 0.0012  191 HIS A CG  
1481 N ND1 . HIS A 192 ? 0.4697 0.3769 0.4893 -0.0784 -0.0152 -0.0025 191 HIS A ND1 
1482 C CD2 . HIS A 192 ? 0.4314 0.3428 0.4584 -0.0755 0.0009  0.0104  191 HIS A CD2 
1483 C CE1 . HIS A 192 ? 0.4642 0.3637 0.4984 -0.0881 -0.0203 0.0041  191 HIS A CE1 
1484 N NE2 . HIS A 192 ? 0.4060 0.3084 0.4457 -0.0865 -0.0100 0.0125  191 HIS A NE2 
1485 N N   . MET A 193 ? 0.4333 0.3531 0.3988 -0.0391 0.0169  -0.0111 192 MET A N   
1486 C CA  . MET A 193 ? 0.4017 0.3323 0.3602 -0.0319 0.0224  -0.0120 192 MET A CA  
1487 C C   . MET A 193 ? 0.3722 0.3161 0.3385 -0.0334 0.0288  -0.0062 192 MET A C   
1488 O O   . MET A 193 ? 0.4059 0.3480 0.3758 -0.0347 0.0329  0.0003  192 MET A O   
1489 C CB  . MET A 193 ? 0.3701 0.2925 0.3173 -0.0249 0.0244  -0.0118 192 MET A CB  
1490 C CG  . MET A 193 ? 0.3832 0.3168 0.3244 -0.0183 0.0273  -0.0130 192 MET A CG  
1491 S SD  . MET A 193 ? 0.4780 0.4060 0.4094 -0.0092 0.0291  -0.0111 192 MET A SD  
1492 C CE  . MET A 193 ? 0.3975 0.3211 0.3308 -0.0112 0.0326  -0.0032 192 MET A CE  
1493 N N   . TYR A 194 ? 0.3525 0.3081 0.3197 -0.0324 0.0301  -0.0083 193 TYR A N   
1494 C CA  . TYR A 194 ? 0.3708 0.3364 0.3418 -0.0322 0.0363  -0.0042 193 TYR A CA  
1495 C C   . TYR A 194 ? 0.3749 0.3428 0.3339 -0.0266 0.0387  -0.0055 193 TYR A C   
1496 O O   . TYR A 194 ? 0.3839 0.3552 0.3386 -0.0245 0.0360  -0.0101 193 TYR A O   
1497 C CB  . TYR A 194 ? 0.3457 0.3203 0.3255 -0.0347 0.0356  -0.0053 193 TYR A CB  
1498 C CG  . TYR A 194 ? 0.3933 0.3675 0.3873 -0.0412 0.0319  -0.0023 193 TYR A CG  
1499 C CD1 . TYR A 194 ? 0.3815 0.3475 0.3745 -0.0442 0.0233  -0.0069 193 TYR A CD1 
1500 C CD2 . TYR A 194 ? 0.3618 0.3434 0.3700 -0.0442 0.0367  0.0055  193 TYR A CD2 
1501 C CE1 . TYR A 194 ? 0.4122 0.3764 0.4179 -0.0514 0.0174  -0.0044 193 TYR A CE1 
1502 C CE2 . TYR A 194 ? 0.3535 0.3368 0.3784 -0.0514 0.0319  0.0097  193 TYR A CE2 
1503 C CZ  . TYR A 194 ? 0.4031 0.3772 0.4268 -0.0558 0.0212  0.0043  193 TYR A CZ  
1504 O OH  . TYR A 194 ? 0.4420 0.4161 0.4816 -0.0642 0.0138  0.0080  193 TYR A OH  
1505 N N   . VAL A 195 ? 0.3704 0.3366 0.3244 -0.0244 0.0433  -0.0009 194 VAL A N   
1506 C CA  . VAL A 195 ? 0.3721 0.3392 0.3139 -0.0198 0.0437  -0.0016 194 VAL A CA  
1507 C C   . VAL A 195 ? 0.3591 0.3299 0.2963 -0.0186 0.0479  -0.0009 194 VAL A C   
1508 O O   . VAL A 195 ? 0.3740 0.3442 0.3128 -0.0183 0.0542  0.0042  194 VAL A O   
1509 C CB  . VAL A 195 ? 0.4124 0.3729 0.3475 -0.0168 0.0447  0.0029  194 VAL A CB  
1510 C CG1 . VAL A 195 ? 0.3773 0.3397 0.2999 -0.0126 0.0434  0.0027  194 VAL A CG1 
1511 C CG2 . VAL A 195 ? 0.3743 0.3283 0.3118 -0.0165 0.0408  0.0017  194 VAL A CG2 
1512 N N   . PHE A 196 ? 0.3838 0.3575 0.3153 -0.0176 0.0450  -0.0055 195 PHE A N   
1513 C CA  . PHE A 196 ? 0.3741 0.3471 0.2979 -0.0158 0.0483  -0.0062 195 PHE A CA  
1514 C C   . PHE A 196 ? 0.3833 0.3533 0.2929 -0.0140 0.0434  -0.0092 195 PHE A C   
1515 O O   . PHE A 196 ? 0.3844 0.3579 0.2963 -0.0154 0.0369  -0.0114 195 PHE A O   
1516 C CB  . PHE A 196 ? 0.3297 0.3070 0.2617 -0.0177 0.0488  -0.0090 195 PHE A CB  
1517 C CG  . PHE A 196 ? 0.3568 0.3304 0.2794 -0.0145 0.0530  -0.0097 195 PHE A CG  
1518 C CD1 . PHE A 196 ? 0.3512 0.3237 0.2727 -0.0110 0.0617  -0.0048 195 PHE A CD1 
1519 C CD2 . PHE A 196 ? 0.3801 0.3504 0.2941 -0.0144 0.0485  -0.0148 195 PHE A CD2 
1520 C CE1 . PHE A 196 ? 0.4077 0.3745 0.3172 -0.0060 0.0668  -0.0057 195 PHE A CE1 
1521 C CE2 . PHE A 196 ? 0.4122 0.3747 0.3138 -0.0107 0.0520  -0.0165 195 PHE A CE2 
1522 C CZ  . PHE A 196 ? 0.4138 0.3738 0.3116 -0.0056 0.0615  -0.0124 195 PHE A CZ  
1523 N N   . GLY A 197 ? 0.4035 0.3669 0.2983 -0.0106 0.0465  -0.0087 196 GLY A N   
1524 C CA  . GLY A 197 ? 0.4246 0.3822 0.3035 -0.0096 0.0404  -0.0123 196 GLY A CA  
1525 C C   . GLY A 197 ? 0.4321 0.3906 0.3062 -0.0093 0.0338  -0.0105 196 GLY A C   
1526 O O   . GLY A 197 ? 0.4376 0.3980 0.3158 -0.0080 0.0360  -0.0059 196 GLY A O   
1527 N N   . GLY A 198 ? 0.4221 0.3790 0.2883 -0.0109 0.0249  -0.0138 197 GLY A N   
1528 C CA  . GLY A 198 ? 0.4346 0.3943 0.2974 -0.0108 0.0168  -0.0115 197 GLY A CA  
1529 C C   . GLY A 198 ? 0.4667 0.4155 0.3057 -0.0076 0.0136  -0.0115 197 GLY A C   
1530 O O   . GLY A 198 ? 0.5059 0.4443 0.3297 -0.0034 0.0205  -0.0120 197 GLY A O   
1531 N N   . ARG A 199 ? 0.5151 0.4667 0.3507 -0.0090 0.0026  -0.0105 198 ARG A N   
1532 C CA  . ARG A 199 ? 0.4757 0.4173 0.2876 -0.0060 -0.0034 -0.0101 198 ARG A CA  
1533 C C   . ARG A 199 ? 0.5003 0.4434 0.3091 -0.0004 0.0015  -0.0029 198 ARG A C   
1534 O O   . ARG A 199 ? 0.4806 0.4344 0.3076 -0.0003 0.0033  0.0016  198 ARG A O   
1535 C CB  . ARG A 199 ? 0.5045 0.4503 0.3175 -0.0113 -0.0193 -0.0111 198 ARG A CB  
1536 C CG  . ARG A 199 ? 0.5439 0.4804 0.3328 -0.0091 -0.0292 -0.0106 198 ARG A CG  
1537 C CD  . ARG A 199 ? 0.5654 0.5108 0.3630 -0.0157 -0.0463 -0.0096 198 ARG A CD  
1538 N NE  . ARG A 199 ? 0.5287 0.4947 0.3521 -0.0157 -0.0470 -0.0016 198 ARG A NE  
1539 C CZ  . ARG A 199 ? 0.5377 0.5152 0.3695 -0.0185 -0.0603 0.0034  198 ARG A CZ  
1540 N NH1 . ARG A 199 ? 0.5313 0.5013 0.3481 -0.0231 -0.0759 0.0010  198 ARG A NH1 
1541 N NH2 . ARG A 199 ? 0.5076 0.5039 0.3630 -0.0164 -0.0585 0.0113  198 ARG A NH2 
1542 N N   . ALA A 200 ? 0.5273 0.4581 0.3115 0.0052  0.0042  -0.0017 199 ALA A N   
1543 C CA  . ALA A 200 ? 0.5436 0.4739 0.3226 0.0111  0.0099  0.0063  199 ALA A CA  
1544 C C   . ALA A 200 ? 0.5869 0.5035 0.3335 0.0169  0.0070  0.0069  199 ALA A C   
1545 O O   . ALA A 200 ? 0.6127 0.5184 0.3397 0.0165  0.0010  0.0001  199 ALA A O   
1546 C CB  . ALA A 200 ? 0.5233 0.4540 0.3131 0.0131  0.0252  0.0102  199 ALA A CB  
1547 N N   . ASP A 201 ? 0.6130 0.5284 0.3521 0.0227  0.0113  0.0150  200 ASP A N   
1548 C CA  . ASP A 201 ? 0.6346 0.5368 0.3410 0.0300  0.0106  0.0175  200 ASP A CA  
1549 C C   . ASP A 201 ? 0.6587 0.5548 0.3583 0.0366  0.0287  0.0236  200 ASP A C   
1550 O O   . ASP A 201 ? 0.6835 0.5873 0.4047 0.0359  0.0380  0.0303  200 ASP A O   
1551 C CB  . ASP A 201 ? 0.6684 0.5752 0.3716 0.0322  0.0011  0.0242  200 ASP A CB  
1552 C CG  . ASP A 201 ? 0.7372 0.6297 0.4035 0.0400  -0.0014 0.0269  200 ASP A CG  
1553 O OD1 . ASP A 201 ? 0.7492 0.6316 0.3923 0.0393  -0.0133 0.0196  200 ASP A OD1 
1554 O OD2 . ASP A 201 ? 0.7404 0.6306 0.3998 0.0469  0.0079  0.0363  200 ASP A OD2 
1555 N N   . ARG A 202 ? 0.7358 0.6174 0.4055 0.0433  0.0337  0.0218  201 ARG A N   
1556 C CA  . ARG A 202 ? 0.7899 0.6688 0.4582 0.0496  0.0528  0.0288  201 ARG A CA  
1557 C C   . ARG A 202 ? 0.7922 0.6710 0.4550 0.0556  0.0600  0.0415  201 ARG A C   
1558 O O   . ARG A 202 ? 0.7755 0.6539 0.4403 0.0603  0.0764  0.0499  201 ARG A O   
1559 C CB  . ARG A 202 ? 0.7628 0.6265 0.4017 0.0570  0.0596  0.0241  201 ARG A CB  
1560 C CG  . ARG A 202 ? 0.8188 0.6647 0.4143 0.0657  0.0543  0.0227  201 ARG A CG  
1561 C CD  . ARG A 202 ? 0.8336 0.6615 0.3999 0.0725  0.0589  0.0146  201 ARG A CD  
1562 N NE  . ARG A 202 ? 0.7932 0.6196 0.3549 0.0826  0.0812  0.0229  201 ARG A NE  
1563 C CZ  . ARG A 202 ? 0.7721 0.5854 0.2993 0.0956  0.0910  0.0287  201 ARG A CZ  
1564 N NH1 . ARG A 202 ? 0.8040 0.6014 0.2935 0.1006  0.0795  0.0255  201 ARG A NH1 
1565 N NH2 . ARG A 202 ? 0.7951 0.6118 0.3260 0.1041  0.1129  0.0388  201 ARG A NH2 
1566 N N   . PHE A 203 ? 0.6875 0.5678 0.3461 0.0555  0.0488  0.0443  202 PHE A N   
1567 C CA  . PHE A 203 ? 0.7293 0.6089 0.3837 0.0614  0.0558  0.0571  202 PHE A CA  
1568 C C   . PHE A 203 ? 0.7195 0.6100 0.4024 0.0565  0.0519  0.0625  202 PHE A C   
1569 O O   . PHE A 203 ? 0.7165 0.6072 0.4081 0.0589  0.0621  0.0734  202 PHE A O   
1570 C CB  . PHE A 203 ? 0.7252 0.5927 0.3406 0.0698  0.0487  0.0588  202 PHE A CB  
1571 C CG  . PHE A 203 ? 0.7338 0.5861 0.3149 0.0781  0.0566  0.0559  202 PHE A CG  
1572 C CD1 . PHE A 203 ? 0.7573 0.6053 0.3292 0.0868  0.0759  0.0665  202 PHE A CD1 
1573 C CD2 . PHE A 203 ? 0.7789 0.6203 0.3371 0.0777  0.0452  0.0432  202 PHE A CD2 
1574 C CE1 . PHE A 203 ? 0.7785 0.6122 0.3173 0.0967  0.0852  0.0646  202 PHE A CE1 
1575 C CE2 . PHE A 203 ? 0.7930 0.6170 0.3162 0.0870  0.0532  0.0399  202 PHE A CE2 
1576 C CZ  . PHE A 203 ? 0.7658 0.5864 0.2788 0.0974  0.0739  0.0507  202 PHE A CZ  
1577 N N   . GLY A 204 ? 0.7082 0.6071 0.4063 0.0503  0.0382  0.0559  203 GLY A N   
1578 C CA  . GLY A 204 ? 0.6507 0.5582 0.3720 0.0482  0.0351  0.0611  203 GLY A CA  
1579 C C   . GLY A 204 ? 0.6262 0.5450 0.3681 0.0415  0.0236  0.0535  203 GLY A C   
1580 O O   . GLY A 204 ? 0.6128 0.5337 0.3570 0.0364  0.0195  0.0442  203 GLY A O   
1581 N N   . PRO A 205 ? 0.6309 0.5568 0.3880 0.0422  0.0189  0.0584  204 PRO A N   
1582 C CA  . PRO A 205 ? 0.5824 0.5208 0.3611 0.0374  0.0100  0.0533  204 PRO A CA  
1583 C C   . PRO A 205 ? 0.5750 0.5212 0.3475 0.0368  -0.0062 0.0517  204 PRO A C   
1584 O O   . PRO A 205 ? 0.6174 0.5765 0.4101 0.0346  -0.0128 0.0514  204 PRO A O   
1585 C CB  . PRO A 205 ? 0.5737 0.5141 0.3694 0.0407  0.0144  0.0607  204 PRO A CB  
1586 C CG  . PRO A 205 ? 0.5702 0.5023 0.3476 0.0481  0.0166  0.0708  204 PRO A CG  
1587 C CD  . PRO A 205 ? 0.5816 0.5038 0.3365 0.0486  0.0227  0.0698  204 PRO A CD  
1588 N N   . PHE A 206 ? 0.5938 0.5326 0.3395 0.0389  -0.0131 0.0511  205 PHE A N   
1589 C CA  . PHE A 206 ? 0.6507 0.5958 0.3900 0.0370  -0.0311 0.0498  205 PHE A CA  
1590 C C   . PHE A 206 ? 0.6935 0.6291 0.4125 0.0325  -0.0384 0.0399  205 PHE A C   
1591 O O   . PHE A 206 ? 0.6672 0.5877 0.3644 0.0353  -0.0295 0.0366  205 PHE A O   
1592 C CB  . PHE A 206 ? 0.6302 0.5728 0.3514 0.0444  -0.0373 0.0590  205 PHE A CB  
1593 C CG  . PHE A 206 ? 0.6178 0.5664 0.3552 0.0503  -0.0304 0.0694  205 PHE A CG  
1594 C CD1 . PHE A 206 ? 0.5785 0.5432 0.3435 0.0495  -0.0354 0.0725  205 PHE A CD1 
1595 C CD2 . PHE A 206 ? 0.6144 0.5514 0.3389 0.0572  -0.0185 0.0768  205 PHE A CD2 
1596 C CE1 . PHE A 206 ? 0.5919 0.5590 0.3694 0.0562  -0.0288 0.0816  205 PHE A CE1 
1597 C CE2 . PHE A 206 ? 0.6008 0.5401 0.3393 0.0624  -0.0127 0.0863  205 PHE A CE2 
1598 C CZ  . PHE A 206 ? 0.5968 0.5500 0.3608 0.0622  -0.0180 0.0881  205 PHE A CZ  
1599 N N   . HIS A 207 ? 0.6897 0.6338 0.4162 0.0258  -0.0546 0.0360  206 HIS A N   
1600 C CA  . HIS A 207 ? 0.7332 0.6647 0.4362 0.0215  -0.0657 0.0270  206 HIS A CA  
1601 C C   . HIS A 207 ? 0.7415 0.6560 0.4051 0.0288  -0.0693 0.0286  206 HIS A C   
1602 O O   . HIS A 207 ? 0.7874 0.7070 0.4467 0.0335  -0.0754 0.0371  206 HIS A O   
1603 C CB  . HIS A 207 ? 0.7359 0.6798 0.4541 0.0125  -0.0854 0.0253  206 HIS A CB  
1604 C CG  . HIS A 207 ? 0.7013 0.6600 0.4538 0.0053  -0.0824 0.0232  206 HIS A CG  
1605 N ND1 . HIS A 207 ? 0.7125 0.6632 0.4654 0.0002  -0.0772 0.0141  206 HIS A ND1 
1606 C CD2 . HIS A 207 ? 0.6704 0.6514 0.4568 0.0033  -0.0838 0.0297  206 HIS A CD2 
1607 C CE1 . HIS A 207 ? 0.6856 0.6529 0.4707 -0.0050 -0.0756 0.0151  206 HIS A CE1 
1608 N NE2 . HIS A 207 ? 0.6246 0.6102 0.4299 -0.0030 -0.0791 0.0244  206 HIS A NE2 
1609 N N   . SER A 208 ? 0.7823 0.6763 0.4161 0.0313  -0.0641 0.0211  207 SER A N   
1610 C CA  . SER A 208 ? 0.8387 0.7141 0.4299 0.0395  -0.0676 0.0218  207 SER A CA  
1611 C C   . SER A 208 ? 0.8666 0.7185 0.4235 0.0394  -0.0721 0.0099  207 SER A C   
1612 O O   . SER A 208 ? 0.9094 0.7419 0.4274 0.0490  -0.0671 0.0096  207 SER A O   
1613 C CB  . SER A 208 ? 0.7953 0.6662 0.3775 0.0500  -0.0474 0.0304  207 SER A CB  
1614 O OG  . SER A 208 ? 0.7923 0.6570 0.3771 0.0512  -0.0297 0.0266  207 SER A OG  
1615 N N   . ASN A 209 ? 0.8795 0.7311 0.4482 0.0298  -0.0804 0.0005  208 ASN A N   
1616 C CA  . ASN A 209 ? 0.8916 0.7187 0.4303 0.0301  -0.0821 -0.0115 208 ASN A CA  
1617 C C   . ASN A 209 ? 0.8851 0.7019 0.4130 0.0396  -0.0574 -0.0119 208 ASN A C   
1618 O O   . ASN A 209 ? 0.9066 0.6994 0.3952 0.0478  -0.0531 -0.0173 208 ASN A O   
1619 C CB  . ASN A 209 ? 0.9596 0.7647 0.4534 0.0328  -0.1004 -0.0161 208 ASN A CB  
1620 C CG  . ASN A 209 ? 1.0312 0.8117 0.5006 0.0284  -0.1112 -0.0302 208 ASN A CG  
1621 O OD1 . ASN A 209 ? 1.0070 0.7891 0.4964 0.0226  -0.1057 -0.0358 208 ASN A OD1 
1622 N ND2 . ASN A 209 ? 1.0580 0.8142 0.4832 0.0309  -0.1280 -0.0361 208 ASN A ND2 
1623 N N   . ASN A 210 ? 0.8307 0.6658 0.3936 0.0388  -0.0411 -0.0057 209 ASN A N   
1624 C CA  . ASN A 210 ? 0.7979 0.6291 0.3614 0.0454  -0.0183 -0.0045 209 ASN A CA  
1625 C C   . ASN A 210 ? 0.7791 0.6270 0.3840 0.0373  -0.0118 -0.0056 209 ASN A C   
1626 O O   . ASN A 210 ? 0.7239 0.5828 0.3503 0.0391  0.0039  0.0010  209 ASN A O   
1627 C CB  . ASN A 210 ? 0.7976 0.6320 0.3567 0.0550  -0.0029 0.0076  209 ASN A CB  
1628 C CG  . ASN A 210 ? 0.8588 0.6730 0.3707 0.0662  -0.0033 0.0089  209 ASN A CG  
1629 O OD1 . ASN A 210 ? 0.8989 0.6948 0.3815 0.0744  0.0060  0.0047  209 ASN A OD1 
1630 N ND2 . ASN A 210 ? 0.8183 0.6353 0.3215 0.0679  -0.0134 0.0153  209 ASN A ND2 
1631 N N   . GLU A 211 ? 0.7853 0.6347 0.4013 0.0279  -0.0250 -0.0136 210 GLU A N   
1632 C CA  . GLU A 211 ? 0.7057 0.5712 0.3595 0.0200  -0.0215 -0.0145 210 GLU A CA  
1633 C C   . GLU A 211 ? 0.6395 0.4990 0.2942 0.0236  -0.0048 -0.0174 210 GLU A C   
1634 O O   . GLU A 211 ? 0.6460 0.4861 0.2724 0.0291  -0.0018 -0.0231 210 GLU A O   
1635 C CB  . GLU A 211 ? 0.6876 0.5551 0.3502 0.0095  -0.0403 -0.0210 210 GLU A CB  
1636 C CG  . GLU A 211 ? 0.6279 0.5121 0.3275 0.0011  -0.0391 -0.0216 210 GLU A CG  
1637 C CD  . GLU A 211 ? 0.6396 0.5287 0.3496 -0.0093 -0.0586 -0.0244 210 GLU A CD  
1638 O OE1 . GLU A 211 ? 0.6099 0.5093 0.3253 -0.0115 -0.0704 -0.0191 210 GLU A OE1 
1639 O OE2 . GLU A 211 ? 0.6555 0.5384 0.3691 -0.0152 -0.0622 -0.0309 210 GLU A OE2 
1640 N N   . ILE A 212 ? 0.6584 0.5340 0.3448 0.0213  0.0062  -0.0130 211 ILE A N   
1641 C CA  . ILE A 212 ? 0.6385 0.5123 0.3308 0.0242  0.0215  -0.0138 211 ILE A CA  
1642 C C   . ILE A 212 ? 0.6008 0.4900 0.3279 0.0160  0.0217  -0.0151 211 ILE A C   
1643 O O   . ILE A 212 ? 0.5422 0.4455 0.2913 0.0100  0.0150  -0.0128 211 ILE A O   
1644 C CB  . ILE A 212 ? 0.6517 0.5278 0.3436 0.0322  0.0390  -0.0044 211 ILE A CB  
1645 C CG1 . ILE A 212 ? 0.6392 0.5308 0.3544 0.0291  0.0395  0.0040  211 ILE A CG1 
1646 C CG2 . ILE A 212 ? 0.6959 0.5546 0.3494 0.0427  0.0430  -0.0031 211 ILE A CG2 
1647 C CD1 . ILE A 212 ? 0.6317 0.5334 0.3715 0.0289  0.0541  0.0109  211 ILE A CD1 
1648 N N   . TYR A 213 ? 0.6192 0.5052 0.3501 0.0172  0.0305  -0.0181 212 TYR A N   
1649 C CA  . TYR A 213 ? 0.5641 0.4624 0.3241 0.0104  0.0310  -0.0197 212 TYR A CA  
1650 C C   . TYR A 213 ? 0.5571 0.4637 0.3334 0.0134  0.0464  -0.0138 212 TYR A C   
1651 O O   . TYR A 213 ? 0.6028 0.5023 0.3689 0.0200  0.0572  -0.0129 212 TYR A O   
1652 C CB  . TYR A 213 ? 0.5549 0.4428 0.3074 0.0076  0.0243  -0.0283 212 TYR A CB  
1653 C CG  . TYR A 213 ? 0.5591 0.4457 0.3074 0.0011  0.0068  -0.0316 212 TYR A CG  
1654 C CD1 . TYR A 213 ? 0.5734 0.4439 0.2916 0.0036  -0.0022 -0.0347 212 TYR A CD1 
1655 C CD2 . TYR A 213 ? 0.5479 0.4511 0.3233 -0.0072 -0.0005 -0.0300 212 TYR A CD2 
1656 C CE1 . TYR A 213 ? 0.6227 0.4948 0.3409 -0.0035 -0.0199 -0.0361 212 TYR A CE1 
1657 C CE2 . TYR A 213 ? 0.5415 0.4478 0.3182 -0.0132 -0.0160 -0.0304 212 TYR A CE2 
1658 C CZ  . TYR A 213 ? 0.5576 0.4493 0.3075 -0.0121 -0.0263 -0.0332 212 TYR A CZ  
1659 O OH  . TYR A 213 ? 0.5843 0.4815 0.3393 -0.0192 -0.0432 -0.0324 212 TYR A OH  
1660 N N   . CYS A 214 ? 0.5299 0.4510 0.3309 0.0090  0.0470  -0.0090 213 CYS A N   
1661 C CA  . CYS A 214 ? 0.5456 0.4746 0.3638 0.0100  0.0589  -0.0022 213 CYS A CA  
1662 C C   . CYS A 214 ? 0.5163 0.4500 0.3494 0.0082  0.0636  -0.0045 213 CYS A C   
1663 O O   . CYS A 214 ? 0.4942 0.4300 0.3345 0.0035  0.0564  -0.0104 213 CYS A O   
1664 C CB  . CYS A 214 ? 0.4725 0.4116 0.3099 0.0055  0.0558  0.0018  213 CYS A CB  
1665 S SG  . CYS A 214 ? 0.5690 0.5041 0.3916 0.0084  0.0503  0.0058  213 CYS A SG  
1666 N N   . ASN A 215 ? 0.4808 0.4169 0.3196 0.0122  0.0759  0.0016  214 ASN A N   
1667 C CA  . ASN A 215 ? 0.4526 0.3973 0.3118 0.0098  0.0800  0.0019  214 ASN A CA  
1668 C C   . ASN A 215 ? 0.4793 0.4347 0.3594 0.0091  0.0891  0.0116  214 ASN A C   
1669 O O   . ASN A 215 ? 0.4613 0.4250 0.3594 0.0073  0.0922  0.0131  214 ASN A O   
1670 C CB  . ASN A 215 ? 0.4622 0.3984 0.3079 0.0158  0.0845  -0.0020 214 ASN A CB  
1671 C CG  . ASN A 215 ? 0.5555 0.4840 0.3828 0.0262  0.0969  0.0032  214 ASN A CG  
1672 O OD1 . ASN A 215 ? 0.5822 0.5124 0.4070 0.0285  0.1021  0.0105  214 ASN A OD1 
1673 N ND2 . ASN A 215 ? 0.5348 0.4536 0.3479 0.0335  0.1025  0.0000  214 ASN A ND2 
1674 N N   . ARG A 216 ? 0.4911 0.4466 0.3707 0.0099  0.0928  0.0189  215 ARG A N   
1675 C CA  . ARG A 216 ? 0.4556 0.4211 0.3590 0.0064  0.0988  0.0284  215 ARG A CA  
1676 C C   . ARG A 216 ? 0.4470 0.4162 0.3667 -0.0025 0.0883  0.0252  215 ARG A C   
1677 O O   . ARG A 216 ? 0.4501 0.4146 0.3643 -0.0039 0.0830  0.0246  215 ARG A O   
1678 C CB  . ARG A 216 ? 0.4506 0.4138 0.3477 0.0109  0.1080  0.0389  215 ARG A CB  
1679 N N   . ILE A 217 ? 0.3948 0.3717 0.3332 -0.0076 0.0853  0.0232  216 ILE A N   
1680 C CA  . ILE A 217 ? 0.3760 0.3544 0.3264 -0.0148 0.0755  0.0192  216 ILE A CA  
1681 C C   . ILE A 217 ? 0.3889 0.3650 0.3479 -0.0183 0.0756  0.0258  216 ILE A C   
1682 O O   . ILE A 217 ? 0.4555 0.4342 0.4229 -0.0183 0.0833  0.0355  216 ILE A O   
1683 C CB  . ILE A 217 ? 0.3957 0.3823 0.3630 -0.0188 0.0731  0.0173  216 ILE A CB  
1684 C CG1 . ILE A 217 ? 0.3675 0.3530 0.3400 -0.0242 0.0626  0.0110  216 ILE A CG1 
1685 C CG2 . ILE A 217 ? 0.3661 0.3613 0.3540 -0.0213 0.0792  0.0273  216 ILE A CG2 
1686 C CD1 . ILE A 217 ? 0.3549 0.3475 0.3397 -0.0272 0.0593  0.0087  216 ILE A CD1 
1687 N N   . ARG A 218 ? 0.4240 0.3944 0.3808 -0.0209 0.0676  0.0215  217 ARG A N   
1688 C CA  . ARG A 218 ? 0.4239 0.3882 0.3869 -0.0240 0.0665  0.0267  217 ARG A CA  
1689 C C   . ARG A 218 ? 0.4181 0.3796 0.3911 -0.0298 0.0576  0.0215  217 ARG A C   
1690 O O   . ARG A 218 ? 0.4228 0.3856 0.3917 -0.0292 0.0520  0.0133  217 ARG A O   
1691 C CB  . ARG A 218 ? 0.3960 0.3524 0.3425 -0.0191 0.0662  0.0274  217 ARG A CB  
1692 C CG  . ARG A 218 ? 0.4419 0.3984 0.3727 -0.0124 0.0735  0.0313  217 ARG A CG  
1693 C CD  . ARG A 218 ? 0.4668 0.4256 0.4042 -0.0116 0.0843  0.0425  217 ARG A CD  
1694 N NE  . ARG A 218 ? 0.5661 0.5223 0.5200 -0.0175 0.0841  0.0497  217 ARG A NE  
1695 C CZ  . ARG A 218 ? 0.6050 0.5523 0.5543 -0.0167 0.0840  0.0548  217 ARG A CZ  
1696 N NH1 . ARG A 218 ? 0.5784 0.5205 0.5072 -0.0098 0.0843  0.0545  217 ARG A NH1 
1697 N NH2 . ARG A 218 ? 0.5571 0.4997 0.5225 -0.0233 0.0826  0.0606  217 ARG A NH2 
1698 N N   . VAL A 219 ? 0.4004 0.3571 0.3860 -0.0355 0.0562  0.0267  218 VAL A N   
1699 C CA  . VAL A 219 ? 0.4058 0.3574 0.4000 -0.0417 0.0470  0.0220  218 VAL A CA  
1700 C C   . VAL A 219 ? 0.4397 0.3754 0.4306 -0.0431 0.0432  0.0230  218 VAL A C   
1701 O O   . VAL A 219 ? 0.4717 0.4034 0.4685 -0.0452 0.0472  0.0321  218 VAL A O   
1702 C CB  . VAL A 219 ? 0.4005 0.3601 0.4155 -0.0492 0.0458  0.0267  218 VAL A CB  
1703 C CG1 . VAL A 219 ? 0.4236 0.3752 0.4430 -0.0554 0.0341  0.0205  218 VAL A CG1 
1704 C CG2 . VAL A 219 ? 0.4068 0.3812 0.4249 -0.0462 0.0507  0.0266  218 VAL A CG2 
1705 N N   . PHE A 220 ? 0.4326 0.3585 0.4141 -0.0414 0.0360  0.0146  219 PHE A N   
1706 C CA  . PHE A 220 ? 0.4585 0.3662 0.4341 -0.0411 0.0321  0.0140  219 PHE A CA  
1707 C C   . PHE A 220 ? 0.4793 0.3754 0.4580 -0.0470 0.0222  0.0081  219 PHE A C   
1708 O O   . PHE A 220 ? 0.4369 0.3345 0.4090 -0.0448 0.0178  -0.0003 219 PHE A O   
1709 C CB  . PHE A 220 ? 0.4637 0.3679 0.4224 -0.0315 0.0330  0.0096  219 PHE A CB  
1710 C CG  . PHE A 220 ? 0.5067 0.3912 0.4576 -0.0287 0.0299  0.0088  219 PHE A CG  
1711 C CD1 . PHE A 220 ? 0.5078 0.3819 0.4610 -0.0301 0.0325  0.0170  219 PHE A CD1 
1712 C CD2 . PHE A 220 ? 0.4636 0.3388 0.4037 -0.0237 0.0252  0.0006  219 PHE A CD2 
1713 C CE1 . PHE A 220 ? 0.5114 0.3649 0.4565 -0.0269 0.0297  0.0164  219 PHE A CE1 
1714 C CE2 . PHE A 220 ? 0.4811 0.3359 0.4120 -0.0194 0.0231  -0.0004 219 PHE A CE2 
1715 C CZ  . PHE A 220 ? 0.5198 0.3629 0.4531 -0.0211 0.0250  0.0072  219 PHE A CZ  
1716 N N   . ASP A 221 ? 0.4930 0.3763 0.4807 -0.0545 0.0182  0.0127  220 ASP A N   
1717 C CA  . ASP A 221 ? 0.5245 0.3916 0.5121 -0.0607 0.0067  0.0067  220 ASP A CA  
1718 C C   . ASP A 221 ? 0.5310 0.3749 0.4984 -0.0538 0.0034  -0.0002 220 ASP A C   
1719 O O   . ASP A 221 ? 0.5362 0.3677 0.5008 -0.0520 0.0063  0.0048  220 ASP A O   
1720 C CB  . ASP A 221 ? 0.4924 0.3550 0.5000 -0.0730 0.0023  0.0152  220 ASP A CB  
1721 C CG  . ASP A 221 ? 0.5353 0.3770 0.5409 -0.0806 -0.0123 0.0086  220 ASP A CG  
1722 O OD1 . ASP A 221 ? 0.5316 0.3681 0.5227 -0.0769 -0.0186 -0.0025 220 ASP A OD1 
1723 O OD2 . ASP A 221 ? 0.6231 0.4525 0.6410 -0.0905 -0.0179 0.0147  220 ASP A OD2 
1724 N N   . THR A 222 ? 0.5249 0.3627 0.4777 -0.0488 -0.0017 -0.0108 221 THR A N   
1725 C CA  . THR A 222 ? 0.5636 0.3790 0.4957 -0.0400 -0.0036 -0.0173 221 THR A CA  
1726 C C   . THR A 222 ? 0.6121 0.3975 0.5395 -0.0462 -0.0137 -0.0200 221 THR A C   
1727 O O   . THR A 222 ? 0.6110 0.3741 0.5227 -0.0390 -0.0136 -0.0227 221 THR A O   
1728 C CB  . THR A 222 ? 0.5312 0.3498 0.4477 -0.0310 -0.0040 -0.0266 221 THR A CB  
1729 O OG1 . THR A 222 ? 0.5389 0.3556 0.4559 -0.0375 -0.0131 -0.0323 221 THR A OG1 
1730 C CG2 . THR A 222 ? 0.4901 0.3353 0.4105 -0.0251 0.0048  -0.0239 221 THR A CG2 
1731 N N   . ARG A 223 ? 0.6157 0.3991 0.5564 -0.0592 -0.0230 -0.0192 222 ARG A N   
1732 C CA  . ARG A 223 ? 0.6297 0.3828 0.5668 -0.0670 -0.0348 -0.0216 222 ARG A CA  
1733 C C   . ARG A 223 ? 0.6384 0.3803 0.5837 -0.0699 -0.0308 -0.0119 222 ARG A C   
1734 O O   . ARG A 223 ? 0.6792 0.3910 0.6097 -0.0670 -0.0346 -0.0152 222 ARG A O   
1735 C CB  . ARG A 223 ? 0.6460 0.4028 0.5995 -0.0818 -0.0472 -0.0212 222 ARG A CB  
1736 C CG  . ARG A 223 ? 0.7420 0.4635 0.6827 -0.0884 -0.0640 -0.0294 222 ARG A CG  
1737 C CD  . ARG A 223 ? 0.8184 0.5363 0.7849 -0.1076 -0.0760 -0.0215 222 ARG A CD  
1738 N NE  . ARG A 223 ? 0.9107 0.5877 0.8621 -0.1133 -0.0913 -0.0285 222 ARG A NE  
1739 C CZ  . ARG A 223 ? 0.9645 0.6292 0.9288 -0.1299 -0.1087 -0.0275 222 ARG A CZ  
1740 N NH1 . ARG A 223 ? 0.8955 0.5882 0.8907 -0.1424 -0.1129 -0.0186 222 ARG A NH1 
1741 N NH2 . ARG A 223 ? 0.9117 0.5342 0.8572 -0.1339 -0.1228 -0.0353 222 ARG A NH2 
1742 N N   . THR A 224 ? 0.6088 0.3734 0.5762 -0.0747 -0.0226 0.0005  223 THR A N   
1743 C CA  . THR A 224 ? 0.6106 0.3667 0.5862 -0.0771 -0.0176 0.0116  223 THR A CA  
1744 C C   . THR A 224 ? 0.6039 0.3686 0.5694 -0.0637 -0.0043 0.0152  223 THR A C   
1745 O O   . THR A 224 ? 0.6419 0.4006 0.6116 -0.0636 0.0011  0.0251  223 THR A O   
1746 C CB  . THR A 224 ? 0.5672 0.3411 0.5731 -0.0903 -0.0160 0.0253  223 THR A CB  
1747 O OG1 . THR A 224 ? 0.5725 0.3793 0.5869 -0.0864 -0.0058 0.0291  223 THR A OG1 
1748 C CG2 . THR A 224 ? 0.5175 0.2838 0.5368 -0.1049 -0.0309 0.0234  223 THR A CG2 
1749 N N   . GLU A 225 ? 0.5822 0.3607 0.5351 -0.0529 0.0001  0.0082  224 GLU A N   
1750 C CA  . GLU A 225 ? 0.5602 0.3515 0.5055 -0.0412 0.0109  0.0116  224 GLU A CA  
1751 C C   . GLU A 225 ? 0.5632 0.3691 0.5225 -0.0444 0.0193  0.0249  224 GLU A C   
1752 O O   . GLU A 225 ? 0.5625 0.3616 0.5177 -0.0396 0.0246  0.0321  224 GLU A O   
1753 C CB  . GLU A 225 ? 0.5500 0.3191 0.4764 -0.0302 0.0112  0.0083  224 GLU A CB  
1754 C CG  . GLU A 225 ? 0.5637 0.3269 0.4731 -0.0217 0.0076  -0.0041 224 GLU A CG  
1755 C CD  . GLU A 225 ? 0.6071 0.3474 0.4973 -0.0090 0.0086  -0.0073 224 GLU A CD  
1756 O OE1 . GLU A 225 ? 0.6516 0.3747 0.5409 -0.0083 0.0099  -0.0012 224 GLU A OE1 
1757 O OE2 . GLU A 225 ? 0.5666 0.3060 0.4426 0.0010  0.0090  -0.0153 224 GLU A OE2 
1758 N N   . ALA A 226 ? 0.5333 0.3597 0.5086 -0.0516 0.0211  0.0287  225 ALA A N   
1759 C CA  . ALA A 226 ? 0.5415 0.3833 0.5294 -0.0539 0.0304  0.0415  225 ALA A CA  
1760 C C   . ALA A 226 ? 0.5049 0.3725 0.4953 -0.0512 0.0362  0.0407  225 ALA A C   
1761 O O   . ALA A 226 ? 0.4937 0.3697 0.4886 -0.0543 0.0316  0.0340  225 ALA A O   
1762 C CB  . ALA A 226 ? 0.5427 0.3804 0.5525 -0.0669 0.0278  0.0511  225 ALA A CB  
1763 N N   . TRP A 227 ? 0.5180 0.3965 0.5039 -0.0450 0.0459  0.0476  226 TRP A N   
1764 C CA  . TRP A 227 ? 0.5057 0.4053 0.4942 -0.0431 0.0523  0.0487  226 TRP A CA  
1765 C C   . TRP A 227 ? 0.5322 0.4411 0.5423 -0.0512 0.0563  0.0590  226 TRP A C   
1766 O O   . TRP A 227 ? 0.5378 0.4422 0.5568 -0.0545 0.0607  0.0707  226 TRP A O   
1767 C CB  . TRP A 227 ? 0.5006 0.4055 0.4737 -0.0335 0.0601  0.0523  226 TRP A CB  
1768 C CG  . TRP A 227 ? 0.5202 0.4219 0.4755 -0.0253 0.0561  0.0437  226 TRP A CG  
1769 C CD1 . TRP A 227 ? 0.5248 0.4143 0.4699 -0.0199 0.0547  0.0448  226 TRP A CD1 
1770 C CD2 . TRP A 227 ? 0.5119 0.4238 0.4600 -0.0217 0.0534  0.0343  226 TRP A CD2 
1771 N NE1 . TRP A 227 ? 0.4935 0.3874 0.4272 -0.0129 0.0514  0.0373  226 TRP A NE1 
1772 C CE2 . TRP A 227 ? 0.4943 0.4016 0.4299 -0.0145 0.0503  0.0309  226 TRP A CE2 
1773 C CE3 . TRP A 227 ? 0.4591 0.3836 0.4113 -0.0237 0.0533  0.0294  226 TRP A CE3 
1774 C CZ2 . TRP A 227 ? 0.4674 0.3836 0.3965 -0.0104 0.0471  0.0236  226 TRP A CZ2 
1775 C CZ3 . TRP A 227 ? 0.4669 0.3977 0.4106 -0.0196 0.0499  0.0214  226 TRP A CZ3 
1776 C CH2 . TRP A 227 ? 0.4649 0.3922 0.3980 -0.0135 0.0468  0.0189  226 TRP A CH2 
1777 N N   . LEU A 228 ? 0.5204 0.4432 0.5405 -0.0543 0.0552  0.0560  227 LEU A N   
1778 C CA  . LEU A 228 ? 0.5072 0.4412 0.5517 -0.0623 0.0578  0.0660  227 LEU A CA  
1779 C C   . LEU A 228 ? 0.5370 0.4873 0.5827 -0.0561 0.0718  0.0754  227 LEU A C   
1780 O O   . LEU A 228 ? 0.5248 0.4793 0.5522 -0.0468 0.0765  0.0700  227 LEU A O   
1781 C CB  . LEU A 228 ? 0.5039 0.4447 0.5594 -0.0683 0.0488  0.0589  227 LEU A CB  
1782 C CG  . LEU A 228 ? 0.4840 0.4081 0.5371 -0.0744 0.0341  0.0491  227 LEU A CG  
1783 C CD1 . LEU A 228 ? 0.4094 0.3427 0.4743 -0.0803 0.0258  0.0445  227 LEU A CD1 
1784 C CD2 . LEU A 228 ? 0.4831 0.3904 0.5456 -0.0828 0.0293  0.0559  227 LEU A CD2 
1785 N N   . ASP A 229 ? 0.5432 0.5019 0.6103 -0.0610 0.0785  0.0901  228 ASP A N   
1786 C CA  . ASP A 229 ? 0.5326 0.5087 0.6045 -0.0549 0.0926  0.0999  228 ASP A CA  
1787 C C   . ASP A 229 ? 0.4736 0.4657 0.5631 -0.0582 0.0904  0.0983  228 ASP A C   
1788 O O   . ASP A 229 ? 0.4837 0.4795 0.5975 -0.0691 0.0825  0.1019  228 ASP A O   
1789 C CB  . ASP A 229 ? 0.5542 0.5344 0.6429 -0.0575 0.1027  0.1188  228 ASP A CB  
1790 C CG  . ASP A 229 ? 0.7194 0.6836 0.7921 -0.0542 0.1051  0.1222  228 ASP A CG  
1791 O OD1 . ASP A 229 ? 0.7648 0.7226 0.8541 -0.0623 0.1042  0.1332  228 ASP A OD1 
1792 O OD2 . ASP A 229 ? 0.7113 0.6690 0.7556 -0.0440 0.1071  0.1144  228 ASP A OD2 
1793 N N   . CYS A 230 ? 0.4431 0.4439 0.5204 -0.0490 0.0970  0.0938  229 CYS A N   
1794 C CA  . CYS A 230 ? 0.4495 0.4633 0.5387 -0.0502 0.0941  0.0900  229 CYS A CA  
1795 C C   . CYS A 230 ? 0.4462 0.4758 0.5402 -0.0416 0.1093  0.0994  229 CYS A C   
1796 O O   . CYS A 230 ? 0.4732 0.5002 0.5494 -0.0317 0.1213  0.1033  229 CYS A O   
1797 C CB  . CYS A 230 ? 0.4865 0.4926 0.5544 -0.0469 0.0856  0.0727  229 CYS A CB  
1798 S SG  . CYS A 230 ? 0.6243 0.6133 0.6877 -0.0551 0.0689  0.0621  229 CYS A SG  
1799 N N   . PRO A 231 ? 0.4395 0.4849 0.5556 -0.0442 0.1090  0.1032  230 PRO A N   
1800 C CA  . PRO A 231 ? 0.4426 0.5041 0.5667 -0.0350 0.1248  0.1143  230 PRO A CA  
1801 C C   . PRO A 231 ? 0.4090 0.4638 0.5016 -0.0213 0.1321  0.1047  230 PRO A C   
1802 O O   . PRO A 231 ? 0.4863 0.5291 0.5582 -0.0210 0.1226  0.0893  230 PRO A O   
1803 C CB  . PRO A 231 ? 0.4161 0.4952 0.5716 -0.0420 0.1188  0.1185  230 PRO A CB  
1804 C CG  . PRO A 231 ? 0.4325 0.5010 0.5830 -0.0507 0.1001  0.1037  230 PRO A CG  
1805 C CD  . PRO A 231 ? 0.4243 0.4735 0.5588 -0.0548 0.0940  0.0982  230 PRO A CD  
1806 N N   . PRO A 232 ? 0.4494 0.5109 0.5369 -0.0095 0.1489  0.1137  231 PRO A N   
1807 C CA  . PRO A 232 ? 0.4665 0.5184 0.5223 0.0035  0.1549  0.1039  231 PRO A CA  
1808 C C   . PRO A 232 ? 0.5098 0.5650 0.5689 0.0031  0.1476  0.0941  231 PRO A C   
1809 O O   . PRO A 232 ? 0.5068 0.5769 0.5949 -0.0033 0.1433  0.0989  231 PRO A O   
1810 C CB  . PRO A 232 ? 0.3802 0.4400 0.4348 0.0163  0.1754  0.1182  231 PRO A CB  
1811 C CG  . PRO A 232 ? 0.3836 0.4538 0.4628 0.0101  0.1803  0.1349  231 PRO A CG  
1812 C CD  . PRO A 232 ? 0.4233 0.5001 0.5327 -0.0069 0.1639  0.1339  231 PRO A CD  
1813 N N   . THR A 233 ? 0.5090 0.5499 0.5384 0.0096  0.1452  0.0806  232 THR A N   
1814 C CA  . THR A 233 ? 0.5784 0.6207 0.6075 0.0117  0.1413  0.0726  232 THR A CA  
1815 C C   . THR A 233 ? 0.5999 0.6382 0.6113 0.0270  0.1559  0.0744  232 THR A C   
1816 O O   . THR A 233 ? 0.6646 0.6855 0.6430 0.0345  0.1588  0.0675  232 THR A O   
1817 C CB  . THR A 233 ? 0.5271 0.5554 0.5379 0.0069  0.1268  0.0563  232 THR A CB  
1818 O OG1 . THR A 233 ? 0.4953 0.5072 0.4754 0.0119  0.1278  0.0504  232 THR A OG1 
1819 C CG2 . THR A 233 ? 0.4285 0.4606 0.4573 -0.0064 0.1131  0.0546  232 THR A CG2 
1820 N N   . PRO A 234 ? 0.6792 0.7323 0.7101 0.0325  0.1653  0.0838  233 PRO A N   
1821 C CA  . PRO A 234 ? 0.6848 0.7313 0.6957 0.0493  0.1805  0.0852  233 PRO A CA  
1822 C C   . PRO A 234 ? 0.7007 0.7254 0.6789 0.0541  0.1743  0.0684  233 PRO A C   
1823 O O   . PRO A 234 ? 0.7321 0.7394 0.6782 0.0663  0.1828  0.0645  233 PRO A O   
1824 C CB  . PRO A 234 ? 0.6488 0.7180 0.6933 0.0522  0.1881  0.0978  233 PRO A CB  
1825 C CG  . PRO A 234 ? 0.6448 0.7264 0.7184 0.0360  0.1708  0.0958  233 PRO A CG  
1826 C CD  . PRO A 234 ? 0.6772 0.7517 0.7470 0.0241  0.1604  0.0919  233 PRO A CD  
1827 N N   . VAL A 235 ? 0.6085 0.6324 0.5935 0.0444  0.1592  0.0586  234 VAL A N   
1828 C CA  . VAL A 235 ? 0.5572 0.5627 0.5175 0.0463  0.1516  0.0441  234 VAL A CA  
1829 C C   . VAL A 235 ? 0.5278 0.5263 0.4818 0.0343  0.1356  0.0341  234 VAL A C   
1830 O O   . VAL A 235 ? 0.5305 0.5410 0.5064 0.0235  0.1275  0.0364  234 VAL A O   
1831 C CB  . VAL A 235 ? 0.5605 0.5731 0.5363 0.0472  0.1497  0.0435  234 VAL A CB  
1832 C CG1 . VAL A 235 ? 0.5587 0.5529 0.5132 0.0457  0.1394  0.0291  234 VAL A CG1 
1833 C CG2 . VAL A 235 ? 0.5369 0.5552 0.5169 0.0615  0.1667  0.0534  234 VAL A CG2 
1834 N N   . LEU A 236 ? 0.5369 0.5157 0.4607 0.0364  0.1308  0.0233  235 LEU A N   
1835 C CA  . LEU A 236 ? 0.4950 0.4689 0.4137 0.0263  0.1168  0.0154  235 LEU A CA  
1836 C C   . LEU A 236 ? 0.4745 0.4302 0.3683 0.0273  0.1091  0.0036  235 LEU A C   
1837 O O   . LEU A 236 ? 0.4730 0.4139 0.3448 0.0366  0.1149  0.0006  235 LEU A O   
1838 C CB  . LEU A 236 ? 0.4798 0.4526 0.3919 0.0252  0.1182  0.0194  235 LEU A CB  
1839 C CG  . LEU A 236 ? 0.5137 0.4718 0.3958 0.0350  0.1259  0.0197  235 LEU A CG  
1840 C CD1 . LEU A 236 ? 0.4944 0.4543 0.3762 0.0308  0.1237  0.0239  235 LEU A CD1 
1841 C CD2 . LEU A 236 ? 0.5390 0.4992 0.4192 0.0471  0.1429  0.0286  235 LEU A CD2 
1842 N N   . PRO A 237 ? 0.4884 0.4438 0.3850 0.0181  0.0961  -0.0030 236 PRO A N   
1843 C CA  . PRO A 237 ? 0.4802 0.4197 0.3562 0.0173  0.0876  -0.0128 236 PRO A CA  
1844 C C   . PRO A 237 ? 0.5123 0.4377 0.3616 0.0206  0.0863  -0.0156 236 PRO A C   
1845 O O   . PRO A 237 ? 0.5237 0.4532 0.3722 0.0214  0.0898  -0.0104 236 PRO A O   
1846 C CB  . PRO A 237 ? 0.4805 0.4286 0.3717 0.0069  0.0758  -0.0158 236 PRO A CB  
1847 C CG  . PRO A 237 ? 0.4427 0.4052 0.3525 0.0029  0.0769  -0.0096 236 PRO A CG  
1848 C CD  . PRO A 237 ? 0.4293 0.3984 0.3476 0.0084  0.0888  -0.0013 236 PRO A CD  
1849 N N   . GLU A 238 ? 0.5275 0.4346 0.3540 0.0223  0.0806  -0.0236 237 GLU A N   
1850 C CA  . GLU A 238 ? 0.5339 0.4260 0.3331 0.0239  0.0753  -0.0277 237 GLU A CA  
1851 C C   . GLU A 238 ? 0.5467 0.4486 0.3552 0.0151  0.0650  -0.0270 237 GLU A C   
1852 O O   . GLU A 238 ? 0.4988 0.4115 0.3269 0.0068  0.0575  -0.0280 237 GLU A O   
1853 C CB  . GLU A 238 ? 0.5296 0.3999 0.3061 0.0245  0.0673  -0.0371 237 GLU A CB  
1854 C CG  . GLU A 238 ? 0.6327 0.4828 0.3751 0.0286  0.0627  -0.0418 237 GLU A CG  
1855 C CD  . GLU A 238 ? 0.7743 0.6093 0.4914 0.0430  0.0765  -0.0408 237 GLU A CD  
1856 O OE1 . GLU A 238 ? 0.7982 0.6250 0.5127 0.0492  0.0836  -0.0424 237 GLU A OE1 
1857 O OE2 . GLU A 238 ? 0.7665 0.5981 0.4664 0.0489  0.0811  -0.0375 237 GLU A OE2 
1858 N N   . GLY A 239 ? 0.5325 0.4304 0.3258 0.0179  0.0652  -0.0249 238 GLY A N   
1859 C CA  . GLY A 239 ? 0.5551 0.4602 0.3542 0.0112  0.0552  -0.0242 238 GLY A CA  
1860 C C   . GLY A 239 ? 0.5418 0.4430 0.3393 0.0039  0.0403  -0.0309 238 GLY A C   
1861 O O   . GLY A 239 ? 0.5459 0.4317 0.3264 0.0046  0.0354  -0.0372 238 GLY A O   
1862 N N   . ARG A 240 ? 0.4911 0.4062 0.3071 -0.0030 0.0332  -0.0289 239 ARG A N   
1863 C CA  . ARG A 240 ? 0.4745 0.3913 0.2965 -0.0105 0.0205  -0.0327 239 ARG A CA  
1864 C C   . ARG A 240 ? 0.4916 0.4241 0.3306 -0.0146 0.0154  -0.0283 239 ARG A C   
1865 O O   . ARG A 240 ? 0.4942 0.4354 0.3431 -0.0126 0.0219  -0.0236 239 ARG A O   
1866 C CB  . ARG A 240 ? 0.4776 0.3972 0.3139 -0.0136 0.0216  -0.0348 239 ARG A CB  
1867 C CG  . ARG A 240 ? 0.4524 0.3887 0.3128 -0.0145 0.0284  -0.0302 239 ARG A CG  
1868 C CD  . ARG A 240 ? 0.4474 0.3854 0.3185 -0.0151 0.0321  -0.0314 239 ARG A CD  
1869 N NE  . ARG A 240 ? 0.4771 0.4034 0.3354 -0.0087 0.0400  -0.0328 239 ARG A NE  
1870 C CZ  . ARG A 240 ? 0.5177 0.4389 0.3775 -0.0077 0.0420  -0.0349 239 ARG A CZ  
1871 N NH1 . ARG A 240 ? 0.4740 0.3998 0.3462 -0.0134 0.0360  -0.0360 239 ARG A NH1 
1872 N NH2 . ARG A 240 ? 0.5607 0.4723 0.4094 0.0003  0.0511  -0.0350 239 ARG A NH2 
1873 N N   . ARG A 241 ? 0.4643 0.4001 0.3078 -0.0205 0.0037  -0.0294 240 ARG A N   
1874 C CA  . ARG A 241 ? 0.4532 0.4054 0.3154 -0.0236 -0.0006 -0.0248 240 ARG A CA  
1875 C C   . ARG A 241 ? 0.4620 0.4225 0.3416 -0.0296 -0.0051 -0.0252 240 ARG A C   
1876 O O   . ARG A 241 ? 0.4356 0.3871 0.3105 -0.0327 -0.0084 -0.0291 240 ARG A O   
1877 C CB  . ARG A 241 ? 0.4521 0.4049 0.3062 -0.0242 -0.0105 -0.0226 240 ARG A CB  
1878 C CG  . ARG A 241 ? 0.4318 0.3814 0.2836 -0.0308 -0.0242 -0.0249 240 ARG A CG  
1879 C CD  . ARG A 241 ? 0.4928 0.4438 0.3369 -0.0315 -0.0352 -0.0221 240 ARG A CD  
1880 N NE  . ARG A 241 ? 0.5256 0.4785 0.3753 -0.0399 -0.0503 -0.0222 240 ARG A NE  
1881 C CZ  . ARG A 241 ? 0.5089 0.4476 0.3387 -0.0429 -0.0633 -0.0258 240 ARG A CZ  
1882 N NH1 . ARG A 241 ? 0.5102 0.4312 0.3102 -0.0368 -0.0620 -0.0298 240 ARG A NH1 
1883 N NH2 . ARG A 241 ? 0.5213 0.4629 0.3607 -0.0524 -0.0781 -0.0251 240 ARG A NH2 
1884 N N   . SER A 242 ? 0.4072 0.3835 0.3058 -0.0305 -0.0046 -0.0206 241 SER A N   
1885 C CA  . SER A 242 ? 0.4093 0.3962 0.3252 -0.0353 -0.0084 -0.0186 241 SER A CA  
1886 C C   . SER A 242 ? 0.3833 0.3671 0.3034 -0.0363 -0.0030 -0.0214 241 SER A C   
1887 O O   . SER A 242 ? 0.3897 0.3775 0.3198 -0.0408 -0.0066 -0.0203 241 SER A O   
1888 C CB  . SER A 242 ? 0.3600 0.3466 0.2756 -0.0415 -0.0212 -0.0178 241 SER A CB  
1889 O OG  . SER A 242 ? 0.3805 0.3758 0.2985 -0.0404 -0.0264 -0.0131 241 SER A OG  
1890 N N   . HIS A 243 ? 0.3899 0.3671 0.3036 -0.0321 0.0054  -0.0239 242 HIS A N   
1891 C CA  . HIS A 243 ? 0.3806 0.3595 0.3023 -0.0317 0.0114  -0.0247 242 HIS A CA  
1892 C C   . HIS A 243 ? 0.3803 0.3731 0.3176 -0.0314 0.0133  -0.0212 242 HIS A C   
1893 O O   . HIS A 243 ? 0.3483 0.3483 0.2894 -0.0301 0.0118  -0.0182 242 HIS A O   
1894 C CB  . HIS A 243 ? 0.3404 0.3126 0.2551 -0.0272 0.0197  -0.0262 242 HIS A CB  
1895 C CG  . HIS A 243 ? 0.3564 0.3320 0.2710 -0.0242 0.0232  -0.0236 242 HIS A CG  
1896 N ND1 . HIS A 243 ? 0.3825 0.3541 0.2862 -0.0227 0.0208  -0.0226 242 HIS A ND1 
1897 C CD2 . HIS A 243 ? 0.3914 0.3724 0.3149 -0.0229 0.0281  -0.0215 242 HIS A CD2 
1898 C CE1 . HIS A 243 ? 0.3779 0.3525 0.2847 -0.0202 0.0251  -0.0195 242 HIS A CE1 
1899 N NE2 . HIS A 243 ? 0.4022 0.3818 0.3210 -0.0207 0.0291  -0.0191 242 HIS A NE2 
1900 N N   . SER A 244 ? 0.3695 0.3650 0.3141 -0.0315 0.0167  -0.0213 243 SER A N   
1901 C CA  . SER A 244 ? 0.3412 0.3459 0.2951 -0.0295 0.0196  -0.0192 243 SER A CA  
1902 C C   . SER A 244 ? 0.3400 0.3415 0.2927 -0.0272 0.0246  -0.0209 243 SER A C   
1903 O O   . SER A 244 ? 0.3599 0.3557 0.3097 -0.0272 0.0270  -0.0224 243 SER A O   
1904 C CB  . SER A 244 ? 0.3263 0.3372 0.2888 -0.0313 0.0189  -0.0171 243 SER A CB  
1905 O OG  . SER A 244 ? 0.3752 0.3947 0.3446 -0.0329 0.0151  -0.0127 243 SER A OG  
1906 N N   . ALA A 245 ? 0.3131 0.3175 0.2683 -0.0249 0.0259  -0.0202 244 ALA A N   
1907 C CA  . ALA A 245 ? 0.3294 0.3310 0.2858 -0.0243 0.0286  -0.0211 244 ALA A CA  
1908 C C   . ALA A 245 ? 0.3610 0.3656 0.3205 -0.0229 0.0277  -0.0215 244 ALA A C   
1909 O O   . ALA A 245 ? 0.3532 0.3606 0.3116 -0.0203 0.0270  -0.0206 244 ALA A O   
1910 C CB  . ALA A 245 ? 0.3338 0.3306 0.2868 -0.0233 0.0299  -0.0204 244 ALA A CB  
1911 N N   . PHE A 246 ? 0.3575 0.3616 0.3202 -0.0240 0.0278  -0.0223 245 PHE A N   
1912 C CA  . PHE A 246 ? 0.3802 0.3844 0.3422 -0.0225 0.0257  -0.0234 245 PHE A CA  
1913 C C   . PHE A 246 ? 0.3570 0.3589 0.3231 -0.0250 0.0238  -0.0240 245 PHE A C   
1914 O O   . PHE A 246 ? 0.3428 0.3469 0.3153 -0.0271 0.0256  -0.0223 245 PHE A O   
1915 C CB  . PHE A 246 ? 0.3059 0.3156 0.2682 -0.0210 0.0257  -0.0223 245 PHE A CB  
1916 C CG  . PHE A 246 ? 0.3221 0.3342 0.2895 -0.0233 0.0264  -0.0211 245 PHE A CG  
1917 C CD1 . PHE A 246 ? 0.3509 0.3638 0.3213 -0.0236 0.0251  -0.0210 245 PHE A CD1 
1918 C CD2 . PHE A 246 ? 0.3609 0.3733 0.3294 -0.0247 0.0276  -0.0200 245 PHE A CD2 
1919 C CE1 . PHE A 246 ? 0.3445 0.3591 0.3196 -0.0243 0.0265  -0.0193 245 PHE A CE1 
1920 C CE2 . PHE A 246 ? 0.3247 0.3360 0.2958 -0.0258 0.0284  -0.0193 245 PHE A CE2 
1921 C CZ  . PHE A 246 ? 0.3451 0.3577 0.3197 -0.0250 0.0287  -0.0187 245 PHE A CZ  
1922 N N   . GLY A 247 ? 0.3617 0.3587 0.3241 -0.0245 0.0200  -0.0260 246 GLY A N   
1923 C CA  . GLY A 247 ? 0.3281 0.3231 0.2956 -0.0281 0.0156  -0.0262 246 GLY A CA  
1924 C C   . GLY A 247 ? 0.3546 0.3520 0.3196 -0.0269 0.0117  -0.0271 246 GLY A C   
1925 O O   . GLY A 247 ? 0.3703 0.3644 0.3242 -0.0227 0.0108  -0.0293 246 GLY A O   
1926 N N   . TYR A 248 ? 0.3759 0.3796 0.3509 -0.0296 0.0102  -0.0246 247 TYR A N   
1927 C CA  . TYR A 248 ? 0.3653 0.3721 0.3387 -0.0285 0.0061  -0.0244 247 TYR A CA  
1928 C C   . TYR A 248 ? 0.3637 0.3740 0.3489 -0.0332 0.0002  -0.0221 247 TYR A C   
1929 O O   . TYR A 248 ? 0.3797 0.3962 0.3787 -0.0356 0.0037  -0.0180 247 TYR A O   
1930 C CB  . TYR A 248 ? 0.3636 0.3776 0.3395 -0.0258 0.0114  -0.0216 247 TYR A CB  
1931 C CG  . TYR A 248 ? 0.3881 0.4062 0.3641 -0.0243 0.0079  -0.0197 247 TYR A CG  
1932 C CD1 . TYR A 248 ? 0.4047 0.4194 0.3678 -0.0209 0.0045  -0.0215 247 TYR A CD1 
1933 C CD2 . TYR A 248 ? 0.4242 0.4493 0.4120 -0.0251 0.0086  -0.0156 247 TYR A CD2 
1934 C CE1 . TYR A 248 ? 0.4015 0.4196 0.3628 -0.0189 0.0012  -0.0192 247 TYR A CE1 
1935 C CE2 . TYR A 248 ? 0.3974 0.4267 0.3855 -0.0232 0.0051  -0.0131 247 TYR A CE2 
1936 C CZ  . TYR A 248 ? 0.4140 0.4398 0.3885 -0.0205 0.0010  -0.0149 247 TYR A CZ  
1937 O OH  . TYR A 248 ? 0.4517 0.4812 0.4247 -0.0180 -0.0026 -0.0118 247 TYR A OH  
1938 N N   . ASN A 249 ? 0.4202 0.4262 0.3995 -0.0341 -0.0089 -0.0243 248 ASN A N   
1939 C CA  . ASN A 249 ? 0.4010 0.4109 0.3927 -0.0398 -0.0175 -0.0216 248 ASN A CA  
1940 C C   . ASN A 249 ? 0.3836 0.3944 0.3900 -0.0457 -0.0169 -0.0186 248 ASN A C   
1941 O O   . ASN A 249 ? 0.3846 0.4067 0.4104 -0.0490 -0.0165 -0.0121 248 ASN A O   
1942 C CB  . ASN A 249 ? 0.4537 0.4769 0.4571 -0.0385 -0.0165 -0.0161 248 ASN A CB  
1943 C CG  . ASN A 249 ? 0.5620 0.5837 0.5521 -0.0344 -0.0213 -0.0177 248 ASN A CG  
1944 O OD1 . ASN A 249 ? 0.5837 0.5945 0.5545 -0.0316 -0.0243 -0.0231 248 ASN A OD1 
1945 N ND2 . ASN A 249 ? 0.6583 0.6905 0.6577 -0.0327 -0.0212 -0.0125 248 ASN A ND2 
1946 N N   . GLY A 250 ? 0.3584 0.3577 0.3560 -0.0462 -0.0160 -0.0223 249 GLY A N   
1947 C CA  . GLY A 250 ? 0.3245 0.3218 0.3337 -0.0519 -0.0159 -0.0191 249 GLY A CA  
1948 C C   . GLY A 250 ? 0.3749 0.3808 0.3945 -0.0504 -0.0042 -0.0138 249 GLY A C   
1949 O O   . GLY A 250 ? 0.4045 0.4100 0.4343 -0.0545 -0.0026 -0.0095 249 GLY A O   
1950 N N   . GLU A 251 ? 0.3431 0.3550 0.3591 -0.0448 0.0038  -0.0136 250 GLU A N   
1951 C CA  . GLU A 251 ? 0.3471 0.3647 0.3691 -0.0425 0.0140  -0.0093 250 GLU A CA  
1952 C C   . GLU A 251 ? 0.3532 0.3648 0.3600 -0.0378 0.0195  -0.0134 250 GLU A C   
1953 O O   . GLU A 251 ? 0.3447 0.3528 0.3403 -0.0353 0.0172  -0.0178 250 GLU A O   
1954 C CB  . GLU A 251 ? 0.3270 0.3561 0.3601 -0.0403 0.0180  -0.0045 250 GLU A CB  
1955 C CG  . GLU A 251 ? 0.3205 0.3592 0.3725 -0.0448 0.0122  0.0014  250 GLU A CG  
1956 C CD  . GLU A 251 ? 0.3670 0.4182 0.4313 -0.0408 0.0176  0.0075  250 GLU A CD  
1957 O OE1 . GLU A 251 ? 0.3630 0.4152 0.4220 -0.0376 0.0156  0.0054  250 GLU A OE1 
1958 O OE2 . GLU A 251 ? 0.3474 0.4070 0.4263 -0.0400 0.0246  0.0151  250 GLU A OE2 
1959 N N   . LEU A 252 ? 0.3560 0.3670 0.3627 -0.0365 0.0266  -0.0110 251 LEU A N   
1960 C CA  . LEU A 252 ? 0.3374 0.3436 0.3312 -0.0328 0.0304  -0.0139 251 LEU A CA  
1961 C C   . LEU A 252 ? 0.3501 0.3593 0.3418 -0.0295 0.0349  -0.0138 251 LEU A C   
1962 O O   . LEU A 252 ? 0.3410 0.3543 0.3397 -0.0282 0.0395  -0.0101 251 LEU A O   
1963 C CB  . LEU A 252 ? 0.3692 0.3710 0.3606 -0.0328 0.0345  -0.0116 251 LEU A CB  
1964 C CG  . LEU A 252 ? 0.3986 0.3963 0.3771 -0.0292 0.0376  -0.0136 251 LEU A CG  
1965 C CD1 . LEU A 252 ? 0.3124 0.3075 0.2834 -0.0283 0.0330  -0.0178 251 LEU A CD1 
1966 C CD2 . LEU A 252 ? 0.3154 0.3092 0.2909 -0.0283 0.0421  -0.0101 251 LEU A CD2 
1967 N N   . TYR A 253 ? 0.3389 0.3457 0.3215 -0.0279 0.0337  -0.0173 252 TYR A N   
1968 C CA  . TYR A 253 ? 0.3595 0.3651 0.3377 -0.0256 0.0366  -0.0178 252 TYR A CA  
1969 C C   . TYR A 253 ? 0.3848 0.3851 0.3526 -0.0251 0.0366  -0.0199 252 TYR A C   
1970 O O   . TYR A 253 ? 0.3663 0.3669 0.3314 -0.0258 0.0335  -0.0209 252 TYR A O   
1971 C CB  . TYR A 253 ? 0.3383 0.3467 0.3180 -0.0255 0.0338  -0.0185 252 TYR A CB  
1972 C CG  . TYR A 253 ? 0.3280 0.3422 0.3172 -0.0255 0.0327  -0.0161 252 TYR A CG  
1973 C CD1 . TYR A 253 ? 0.3414 0.3583 0.3345 -0.0276 0.0277  -0.0161 252 TYR A CD1 
1974 C CD2 . TYR A 253 ? 0.3257 0.3414 0.3192 -0.0232 0.0358  -0.0138 252 TYR A CD2 
1975 C CE1 . TYR A 253 ? 0.3506 0.3733 0.3528 -0.0284 0.0246  -0.0135 252 TYR A CE1 
1976 C CE2 . TYR A 253 ? 0.3063 0.3290 0.3101 -0.0228 0.0341  -0.0105 252 TYR A CE2 
1977 C CZ  . TYR A 253 ? 0.3323 0.3593 0.3409 -0.0259 0.0279  -0.0102 252 TYR A CZ  
1978 O OH  . TYR A 253 ? 0.3168 0.3514 0.3360 -0.0263 0.0242  -0.0066 252 TYR A OH  
1979 N N   . ILE A 254 ? 0.3400 0.3348 0.3011 -0.0234 0.0397  -0.0202 253 ILE A N   
1980 C CA  . ILE A 254 ? 0.3741 0.3632 0.3245 -0.0236 0.0375  -0.0223 253 ILE A CA  
1981 C C   . ILE A 254 ? 0.4212 0.4042 0.3665 -0.0236 0.0364  -0.0242 253 ILE A C   
1982 O O   . ILE A 254 ? 0.4181 0.3968 0.3622 -0.0208 0.0405  -0.0241 253 ILE A O   
1983 C CB  . ILE A 254 ? 0.3785 0.3623 0.3203 -0.0215 0.0406  -0.0215 253 ILE A CB  
1984 C CG1 . ILE A 254 ? 0.4065 0.3850 0.3435 -0.0176 0.0472  -0.0205 253 ILE A CG1 
1985 C CG2 . ILE A 254 ? 0.3407 0.3288 0.2891 -0.0222 0.0416  -0.0187 253 ILE A CG2 
1986 C CD1 . ILE A 254 ? 0.4759 0.4432 0.3948 -0.0148 0.0477  -0.0224 253 ILE A CD1 
1987 N N   . PHE A 255 ? 0.3789 0.3616 0.3226 -0.0266 0.0307  -0.0252 254 PHE A N   
1988 C CA  . PHE A 255 ? 0.3655 0.3407 0.3051 -0.0285 0.0276  -0.0267 254 PHE A CA  
1989 C C   . PHE A 255 ? 0.3915 0.3590 0.3204 -0.0308 0.0219  -0.0287 254 PHE A C   
1990 O O   . PHE A 255 ? 0.3788 0.3529 0.3100 -0.0326 0.0182  -0.0272 254 PHE A O   
1991 C CB  . PHE A 255 ? 0.3412 0.3238 0.2914 -0.0317 0.0245  -0.0243 254 PHE A CB  
1992 C CG  . PHE A 255 ? 0.3799 0.3543 0.3273 -0.0357 0.0193  -0.0248 254 PHE A CG  
1993 C CD1 . PHE A 255 ? 0.3791 0.3428 0.3230 -0.0348 0.0207  -0.0261 254 PHE A CD1 
1994 C CD2 . PHE A 255 ? 0.3596 0.3360 0.3080 -0.0404 0.0124  -0.0236 254 PHE A CD2 
1995 C CE1 . PHE A 255 ? 0.4105 0.3631 0.3507 -0.0392 0.0149  -0.0269 254 PHE A CE1 
1996 C CE2 . PHE A 255 ? 0.3565 0.3243 0.3035 -0.0456 0.0059  -0.0238 254 PHE A CE2 
1997 C CZ  . PHE A 255 ? 0.3890 0.3435 0.3311 -0.0454 0.0069  -0.0258 254 PHE A CZ  
1998 N N   . GLY A 256 ? 0.4102 0.3627 0.3268 -0.0305 0.0203  -0.0320 255 GLY A N   
1999 C CA  . GLY A 256 ? 0.4149 0.3584 0.3218 -0.0348 0.0114  -0.0342 255 GLY A CA  
2000 C C   . GLY A 256 ? 0.4436 0.3857 0.3397 -0.0332 0.0095  -0.0350 255 GLY A C   
2001 O O   . GLY A 256 ? 0.4404 0.3824 0.3309 -0.0277 0.0167  -0.0347 255 GLY A O   
2002 N N   . GLY A 257 ? 0.3990 0.3408 0.2933 -0.0384 -0.0006 -0.0348 256 GLY A N   
2003 C CA  . GLY A 257 ? 0.4413 0.3818 0.3248 -0.0372 -0.0044 -0.0348 256 GLY A CA  
2004 C C   . GLY A 257 ? 0.4847 0.4047 0.3449 -0.0380 -0.0123 -0.0401 256 GLY A C   
2005 O O   . GLY A 257 ? 0.4687 0.3744 0.3218 -0.0404 -0.0160 -0.0440 256 GLY A O   
2006 N N   . TYR A 258 ? 0.4595 0.3765 0.3059 -0.0356 -0.0152 -0.0402 257 TYR A N   
2007 C CA  . TYR A 258 ? 0.5258 0.4230 0.3469 -0.0362 -0.0249 -0.0452 257 TYR A CA  
2008 C C   . TYR A 258 ? 0.5428 0.4327 0.3423 -0.0278 -0.0192 -0.0457 257 TYR A C   
2009 O O   . TYR A 258 ? 0.4998 0.4039 0.3081 -0.0252 -0.0145 -0.0403 257 TYR A O   
2010 C CB  . TYR A 258 ? 0.5172 0.4210 0.3464 -0.0453 -0.0410 -0.0429 257 TYR A CB  
2011 C CG  . TYR A 258 ? 0.5335 0.4176 0.3362 -0.0471 -0.0544 -0.0478 257 TYR A CG  
2012 C CD1 . TYR A 258 ? 0.5742 0.4336 0.3582 -0.0499 -0.0618 -0.0552 257 TYR A CD1 
2013 C CD2 . TYR A 258 ? 0.5763 0.4651 0.3714 -0.0458 -0.0607 -0.0451 257 TYR A CD2 
2014 C CE1 . TYR A 258 ? 0.6468 0.4849 0.4028 -0.0518 -0.0761 -0.0608 257 TYR A CE1 
2015 C CE2 . TYR A 258 ? 0.6059 0.4759 0.3743 -0.0475 -0.0748 -0.0497 257 TYR A CE2 
2016 C CZ  . TYR A 258 ? 0.6577 0.5016 0.4057 -0.0507 -0.0829 -0.0580 257 TYR A CZ  
2017 O OH  . TYR A 258 ? 0.6827 0.5050 0.4011 -0.0525 -0.0984 -0.0636 257 TYR A OH  
2018 N N   . ASN A 259 ? 0.5363 0.4024 0.3061 -0.0230 -0.0195 -0.0518 258 ASN A N   
2019 C CA  . ASN A 259 ? 0.5883 0.4441 0.3324 -0.0140 -0.0143 -0.0520 258 ASN A CA  
2020 C C   . ASN A 259 ? 0.6353 0.4710 0.3508 -0.0159 -0.0296 -0.0576 258 ASN A C   
2021 O O   . ASN A 259 ? 0.6391 0.4525 0.3360 -0.0169 -0.0358 -0.0650 258 ASN A O   
2022 C CB  . ASN A 259 ? 0.6151 0.4602 0.3469 -0.0037 0.0020  -0.0534 258 ASN A CB  
2023 C CG  . ASN A 259 ? 0.6351 0.4704 0.3406 0.0069  0.0100  -0.0520 258 ASN A CG  
2024 O OD1 . ASN A 259 ? 0.6964 0.5142 0.3725 0.0090  0.0015  -0.0561 258 ASN A OD1 
2025 N ND2 . ASN A 259 ? 0.6182 0.4645 0.3338 0.0136  0.0262  -0.0456 258 ASN A ND2 
2026 N N   . ALA A 260 ? 0.6219 0.4642 0.3331 -0.0164 -0.0368 -0.0540 259 ALA A N   
2027 C CA  . ALA A 260 ? 0.6748 0.5007 0.3615 -0.0199 -0.0547 -0.0585 259 ALA A CA  
2028 C C   . ALA A 260 ? 0.7269 0.5238 0.3693 -0.0093 -0.0512 -0.0648 259 ALA A C   
2029 O O   . ALA A 260 ? 0.7395 0.5125 0.3544 -0.0115 -0.0656 -0.0724 259 ALA A O   
2030 C CB  . ALA A 260 ? 0.6695 0.5135 0.3673 -0.0233 -0.0640 -0.0515 259 ALA A CB  
2031 N N   . ARG A 261 ? 0.7150 0.5130 0.3497 0.0024  -0.0324 -0.0613 260 ARG A N   
2032 C CA  . ARG A 261 ? 0.7006 0.4720 0.2933 0.0148  -0.0255 -0.0660 260 ARG A CA  
2033 C C   . ARG A 261 ? 0.7316 0.4780 0.3068 0.0164  -0.0259 -0.0755 260 ARG A C   
2034 O O   . ARG A 261 ? 0.8020 0.5182 0.3370 0.0213  -0.0329 -0.0836 260 ARG A O   
2035 C CB  . ARG A 261 ? 0.7092 0.4907 0.3047 0.0263  -0.0031 -0.0580 260 ARG A CB  
2036 C CG  . ARG A 261 ? 0.7599 0.5162 0.3133 0.0417  0.0084  -0.0607 260 ARG A CG  
2037 C CD  . ARG A 261 ? 0.7818 0.5513 0.3450 0.0521  0.0320  -0.0507 260 ARG A CD  
2038 N NE  . ARG A 261 ? 0.8294 0.5903 0.3890 0.0608  0.0474  -0.0522 260 ARG A NE  
2039 C CZ  . ARG A 261 ? 0.8580 0.6371 0.4525 0.0580  0.0570  -0.0482 260 ARG A CZ  
2040 N NH1 . ARG A 261 ? 0.8231 0.6282 0.4568 0.0469  0.0533  -0.0432 260 ARG A NH1 
2041 N NH2 . ARG A 261 ? 0.8755 0.6460 0.4643 0.0673  0.0705  -0.0490 260 ARG A NH2 
2042 N N   . LEU A 262 ? 0.7394 0.4962 0.3427 0.0129  -0.0188 -0.0747 261 LEU A N   
2043 C CA  . LEU A 262 ? 0.7472 0.4815 0.3386 0.0137  -0.0195 -0.0828 261 LEU A CA  
2044 C C   . LEU A 262 ? 0.7488 0.4765 0.3479 -0.0009 -0.0408 -0.0880 261 LEU A C   
2045 O O   . LEU A 262 ? 0.7490 0.4532 0.3348 -0.0014 -0.0446 -0.0955 261 LEU A O   
2046 C CB  . LEU A 262 ? 0.7844 0.5338 0.4028 0.0174  -0.0017 -0.0782 261 LEU A CB  
2047 C CG  . LEU A 262 ? 0.7959 0.5558 0.4144 0.0303  0.0195  -0.0708 261 LEU A CG  
2048 C CD1 . LEU A 262 ? 0.7573 0.5373 0.4099 0.0308  0.0334  -0.0650 261 LEU A CD1 
2049 C CD2 . LEU A 262 ? 0.7074 0.4384 0.2814 0.0456  0.0280  -0.0752 261 LEU A CD2 
2050 N N   . ASN A 263 ? 0.7564 0.5039 0.3769 -0.0122 -0.0543 -0.0835 262 ASN A N   
2051 C CA  . ASN A 263 ? 0.7563 0.5077 0.3969 -0.0275 -0.0725 -0.0843 262 ASN A CA  
2052 C C   . ASN A 263 ? 0.6794 0.4327 0.3414 -0.0305 -0.0657 -0.0846 262 ASN A C   
2053 O O   . ASN A 263 ? 0.7252 0.4586 0.3805 -0.0368 -0.0762 -0.0904 262 ASN A O   
2054 C CB  . ASN A 263 ? 0.7495 0.4711 0.3581 -0.0328 -0.0940 -0.0929 262 ASN A CB  
2055 C CG  . ASN A 263 ? 0.7722 0.5015 0.4065 -0.0503 -0.1140 -0.0913 262 ASN A CG  
2056 O OD1 . ASN A 263 ? 0.7483 0.5095 0.4235 -0.0575 -0.1123 -0.0821 262 ASN A OD1 
2057 N ND2 . ASN A 263 ? 0.8221 0.5213 0.4323 -0.0569 -0.1327 -0.0996 262 ASN A ND2 
2058 N N   . ARG A 264 ? 0.6142 0.3906 0.3014 -0.0259 -0.0485 -0.0781 263 ARG A N   
2059 C CA  . ARG A 264 ? 0.6435 0.4218 0.3479 -0.0259 -0.0395 -0.0777 263 ARG A CA  
2060 C C   . ARG A 264 ? 0.6135 0.4254 0.3598 -0.0328 -0.0365 -0.0690 263 ARG A C   
2061 O O   . ARG A 264 ? 0.5888 0.4221 0.3484 -0.0299 -0.0291 -0.0630 263 ARG A O   
2062 C CB  . ARG A 264 ? 0.7155 0.4853 0.4054 -0.0113 -0.0201 -0.0788 263 ARG A CB  
2063 C CG  . ARG A 264 ? 0.7355 0.5074 0.4422 -0.0095 -0.0103 -0.0777 263 ARG A CG  
2064 C CD  . ARG A 264 ? 0.7758 0.5439 0.4720 0.0055  0.0092  -0.0766 263 ARG A CD  
2065 N NE  . ARG A 264 ? 0.9730 0.7108 0.6272 0.0162  0.0111  -0.0833 263 ARG A NE  
2066 C CZ  . ARG A 264 ? 0.9968 0.7301 0.6362 0.0311  0.0283  -0.0813 263 ARG A CZ  
2067 N NH1 . ARG A 264 ? 0.9072 0.6647 0.5726 0.0357  0.0439  -0.0726 263 ARG A NH1 
2068 N NH2 . ARG A 264 ? 0.9337 0.6377 0.5311 0.0416  0.0296  -0.0876 263 ARG A NH2 
2069 N N   . HIS A 265 ? 0.6417 0.4564 0.4072 -0.0414 -0.0422 -0.0680 264 HIS A N   
2070 C CA  . HIS A 265 ? 0.5524 0.3953 0.3536 -0.0455 -0.0366 -0.0602 264 HIS A CA  
2071 C C   . HIS A 265 ? 0.5379 0.3809 0.3440 -0.0379 -0.0214 -0.0599 264 HIS A C   
2072 O O   . HIS A 265 ? 0.5801 0.4005 0.3667 -0.0321 -0.0176 -0.0653 264 HIS A O   
2073 C CB  . HIS A 265 ? 0.5215 0.3702 0.3427 -0.0582 -0.0496 -0.0571 264 HIS A CB  
2074 C CG  . HIS A 265 ? 0.5562 0.4148 0.3834 -0.0662 -0.0640 -0.0539 264 HIS A CG  
2075 N ND1 . HIS A 265 ? 0.5903 0.4284 0.3947 -0.0703 -0.0791 -0.0593 264 HIS A ND1 
2076 C CD2 . HIS A 265 ? 0.5254 0.4120 0.3780 -0.0699 -0.0655 -0.0454 264 HIS A CD2 
2077 C CE1 . HIS A 265 ? 0.5751 0.4306 0.3934 -0.0770 -0.0901 -0.0535 264 HIS A CE1 
2078 N NE2 . HIS A 265 ? 0.5524 0.4376 0.4003 -0.0764 -0.0813 -0.0448 264 HIS A NE2 
2079 N N   . PHE A 266 ? 0.4958 0.3638 0.3273 -0.0375 -0.0130 -0.0534 265 PHE A N   
2080 C CA  . PHE A 266 ? 0.4944 0.3672 0.3335 -0.0306 0.0006  -0.0517 265 PHE A CA  
2081 C C   . PHE A 266 ? 0.5305 0.4185 0.3952 -0.0359 0.0007  -0.0469 265 PHE A C   
2082 O O   . PHE A 266 ? 0.4926 0.3964 0.3742 -0.0428 -0.0053 -0.0426 265 PHE A O   
2083 C CB  . PHE A 266 ? 0.4641 0.3513 0.3071 -0.0239 0.0113  -0.0482 265 PHE A CB  
2084 C CG  . PHE A 266 ? 0.5252 0.3982 0.3428 -0.0161 0.0155  -0.0511 265 PHE A CG  
2085 C CD1 . PHE A 266 ? 0.5510 0.4092 0.3530 -0.0067 0.0252  -0.0534 265 PHE A CD1 
2086 C CD2 . PHE A 266 ? 0.5343 0.4095 0.3434 -0.0169 0.0106  -0.0506 265 PHE A CD2 
2087 C CE1 . PHE A 266 ? 0.6169 0.4622 0.3939 0.0021  0.0308  -0.0551 265 PHE A CE1 
2088 C CE2 . PHE A 266 ? 0.5764 0.4384 0.3603 -0.0089 0.0151  -0.0524 265 PHE A CE2 
2089 C CZ  . PHE A 266 ? 0.5876 0.4344 0.3548 0.0008  0.0257  -0.0547 265 PHE A CZ  
2090 N N   . HIS A 267 ? 0.5118 0.3953 0.3790 -0.0316 0.0081  -0.0468 266 HIS A N   
2091 C CA  . HIS A 267 ? 0.4607 0.3603 0.3507 -0.0340 0.0109  -0.0414 266 HIS A CA  
2092 C C   . HIS A 267 ? 0.4880 0.3935 0.3828 -0.0257 0.0228  -0.0394 266 HIS A C   
2093 O O   . HIS A 267 ? 0.4572 0.3680 0.3641 -0.0254 0.0254  -0.0362 266 HIS A O   
2094 C CB  . HIS A 267 ? 0.4528 0.3425 0.3465 -0.0402 0.0041  -0.0410 266 HIS A CB  
2095 C CG  . HIS A 267 ? 0.4948 0.3592 0.3718 -0.0354 0.0062  -0.0457 266 HIS A CG  
2096 N ND1 . HIS A 267 ? 0.5137 0.3657 0.3931 -0.0399 0.0014  -0.0453 266 HIS A ND1 
2097 C CD2 . HIS A 267 ? 0.4868 0.3356 0.3442 -0.0257 0.0133  -0.0503 266 HIS A CD2 
2098 C CE1 . HIS A 267 ? 0.5387 0.3664 0.3994 -0.0329 0.0050  -0.0503 266 HIS A CE1 
2099 N NE2 . HIS A 267 ? 0.5067 0.3327 0.3537 -0.0236 0.0129  -0.0533 266 HIS A NE2 
2100 N N   . ASP A 268 ? 0.4342 0.3402 0.3210 -0.0191 0.0298  -0.0401 267 ASP A N   
2101 C CA  . ASP A 268 ? 0.4743 0.3895 0.3697 -0.0122 0.0403  -0.0365 267 ASP A CA  
2102 C C   . ASP A 268 ? 0.4725 0.4103 0.3878 -0.0154 0.0407  -0.0318 267 ASP A C   
2103 O O   . ASP A 268 ? 0.4207 0.3664 0.3411 -0.0211 0.0346  -0.0314 267 ASP A O   
2104 C CB  . ASP A 268 ? 0.4970 0.4042 0.3775 -0.0036 0.0486  -0.0374 267 ASP A CB  
2105 C CG  . ASP A 268 ? 0.5172 0.4252 0.3884 -0.0051 0.0461  -0.0384 267 ASP A CG  
2106 O OD1 . ASP A 268 ? 0.4767 0.3914 0.3533 -0.0125 0.0375  -0.0387 267 ASP A OD1 
2107 O OD2 . ASP A 268 ? 0.5347 0.4371 0.3933 0.0022  0.0536  -0.0380 267 ASP A OD2 
2108 N N   . LEU A 269 ? 0.4773 0.4247 0.4035 -0.0111 0.0477  -0.0279 268 LEU A N   
2109 C CA  . LEU A 269 ? 0.4316 0.3971 0.3748 -0.0136 0.0474  -0.0240 268 LEU A CA  
2110 C C   . LEU A 269 ? 0.4276 0.3998 0.3767 -0.0091 0.0547  -0.0202 268 LEU A C   
2111 O O   . LEU A 269 ? 0.4296 0.4010 0.3813 -0.0034 0.0609  -0.0176 268 LEU A O   
2112 C CB  . LEU A 269 ? 0.4112 0.3833 0.3660 -0.0151 0.0453  -0.0216 268 LEU A CB  
2113 C CG  . LEU A 269 ? 0.3767 0.3639 0.3440 -0.0179 0.0427  -0.0190 268 LEU A CG  
2114 C CD1 . LEU A 269 ? 0.3664 0.3557 0.3307 -0.0222 0.0380  -0.0209 268 LEU A CD1 
2115 C CD2 . LEU A 269 ? 0.3543 0.3470 0.3297 -0.0182 0.0407  -0.0164 268 LEU A CD2 
2116 N N   . TRP A 270 ? 0.4255 0.4048 0.3781 -0.0113 0.0543  -0.0189 269 TRP A N   
2117 C CA  . TRP A 270 ? 0.4163 0.4026 0.3767 -0.0086 0.0607  -0.0139 269 TRP A CA  
2118 C C   . TRP A 270 ? 0.4109 0.4100 0.3874 -0.0137 0.0565  -0.0112 269 TRP A C   
2119 O O   . TRP A 270 ? 0.4151 0.4148 0.3903 -0.0180 0.0501  -0.0140 269 TRP A O   
2120 C CB  . TRP A 270 ? 0.4237 0.4033 0.3715 -0.0063 0.0645  -0.0140 269 TRP A CB  
2121 C CG  . TRP A 270 ? 0.4554 0.4204 0.3846 0.0007  0.0700  -0.0163 269 TRP A CG  
2122 C CD1 . TRP A 270 ? 0.4299 0.3799 0.3415 0.0005  0.0651  -0.0226 269 TRP A CD1 
2123 C CD2 . TRP A 270 ? 0.4744 0.4372 0.3997 0.0093  0.0812  -0.0119 269 TRP A CD2 
2124 N NE1 . TRP A 270 ? 0.5177 0.4532 0.4114 0.0086  0.0717  -0.0240 269 TRP A NE1 
2125 C CE2 . TRP A 270 ? 0.4949 0.4384 0.3961 0.0151  0.0828  -0.0173 269 TRP A CE2 
2126 C CE3 . TRP A 270 ? 0.4707 0.4461 0.4113 0.0127  0.0900  -0.0033 269 TRP A CE3 
2127 C CZ2 . TRP A 270 ? 0.4339 0.3687 0.3224 0.0260  0.0942  -0.0149 269 TRP A CZ2 
2128 C CZ3 . TRP A 270 ? 0.4629 0.4333 0.3948 0.0232  0.1022  0.0007  269 TRP A CZ3 
2129 C CH2 . TRP A 270 ? 0.4618 0.4113 0.3663 0.0306  0.1047  -0.0055 269 TRP A CH2 
2130 N N   . LYS A 271 ? 0.3847 0.3935 0.3760 -0.0127 0.0598  -0.0054 270 LYS A N   
2131 C CA  . LYS A 271 ? 0.3930 0.4116 0.3987 -0.0181 0.0543  -0.0029 270 LYS A CA  
2132 C C   . LYS A 271 ? 0.3967 0.4194 0.4103 -0.0189 0.0587  0.0028  270 LYS A C   
2133 O O   . LYS A 271 ? 0.3899 0.4154 0.4073 -0.0140 0.0674  0.0084  270 LYS A O   
2134 C CB  . LYS A 271 ? 0.3754 0.4032 0.3950 -0.0182 0.0517  0.0003  270 LYS A CB  
2135 C CG  . LYS A 271 ? 0.3265 0.3618 0.3577 -0.0244 0.0431  0.0016  270 LYS A CG  
2136 C CD  . LYS A 271 ? 0.3475 0.3911 0.3892 -0.0241 0.0389  0.0043  270 LYS A CD  
2137 C CE  . LYS A 271 ? 0.3417 0.3952 0.3988 -0.0198 0.0457  0.0125  270 LYS A CE  
2138 N NZ  . LYS A 271 ? 0.3548 0.4188 0.4303 -0.0241 0.0450  0.0196  270 LYS A NZ  
2139 N N   . PHE A 272 ? 0.3736 0.3955 0.3887 -0.0243 0.0534  0.0020  271 PHE A N   
2140 C CA  . PHE A 272 ? 0.3675 0.3931 0.3930 -0.0268 0.0560  0.0084  271 PHE A CA  
2141 C C   . PHE A 272 ? 0.3512 0.3833 0.3932 -0.0338 0.0473  0.0106  271 PHE A C   
2142 O O   . PHE A 272 ? 0.3396 0.3669 0.3758 -0.0370 0.0385  0.0045  271 PHE A O   
2143 C CB  . PHE A 272 ? 0.3822 0.3983 0.3948 -0.0273 0.0563  0.0061  271 PHE A CB  
2144 C CG  . PHE A 272 ? 0.3829 0.4011 0.4056 -0.0301 0.0594  0.0135  271 PHE A CG  
2145 C CD1 . PHE A 272 ? 0.3472 0.3697 0.3737 -0.0256 0.0702  0.0215  271 PHE A CD1 
2146 C CD2 . PHE A 272 ? 0.3145 0.3292 0.3421 -0.0365 0.0520  0.0131  271 PHE A CD2 
2147 C CE1 . PHE A 272 ? 0.3591 0.3845 0.3964 -0.0283 0.0739  0.0301  271 PHE A CE1 
2148 C CE2 . PHE A 272 ? 0.3732 0.3884 0.4112 -0.0399 0.0544  0.0207  271 PHE A CE2 
2149 C CZ  . PHE A 272 ? 0.3973 0.4191 0.4416 -0.0362 0.0655  0.0300  271 PHE A CZ  
2150 N N   . ASN A 273 ? 0.3958 0.4389 0.4580 -0.0358 0.0496  0.0196  272 ASN A N   
2151 C CA  . ASN A 273 ? 0.3668 0.4153 0.4456 -0.0439 0.0393  0.0222  272 ASN A CA  
2152 C C   . ASN A 273 ? 0.3697 0.4151 0.4557 -0.0497 0.0387  0.0269  272 ASN A C   
2153 O O   . ASN A 273 ? 0.3976 0.4514 0.4974 -0.0490 0.0471  0.0369  272 ASN A O   
2154 C CB  . ASN A 273 ? 0.3595 0.4244 0.4605 -0.0440 0.0397  0.0305  272 ASN A CB  
2155 C CG  . ASN A 273 ? 0.3715 0.4421 0.4909 -0.0539 0.0266  0.0338  272 ASN A CG  
2156 O OD1 . ASN A 273 ? 0.3870 0.4603 0.5212 -0.0603 0.0253  0.0407  272 ASN A OD1 
2157 N ND2 . ASN A 273 ? 0.3451 0.4159 0.4621 -0.0555 0.0162  0.0291  272 ASN A ND2 
2158 N N   . PRO A 274 ? 0.3752 0.4082 0.4524 -0.0548 0.0297  0.0208  273 PRO A N   
2159 C CA  . PRO A 274 ? 0.3961 0.4231 0.4788 -0.0601 0.0294  0.0254  273 PRO A CA  
2160 C C   . PRO A 274 ? 0.4387 0.4768 0.5494 -0.0680 0.0264  0.0364  273 PRO A C   
2161 O O   . PRO A 274 ? 0.4651 0.5030 0.5855 -0.0712 0.0306  0.0445  273 PRO A O   
2162 C CB  . PRO A 274 ? 0.4226 0.4327 0.4894 -0.0630 0.0188  0.0156  273 PRO A CB  
2163 C CG  . PRO A 274 ? 0.4151 0.4266 0.4769 -0.0623 0.0110  0.0090  273 PRO A CG  
2164 C CD  . PRO A 274 ? 0.4002 0.4236 0.4625 -0.0554 0.0198  0.0105  273 PRO A CD  
2165 N N   . VAL A 275 ? 0.4112 0.4601 0.5365 -0.0713 0.0191  0.0383  274 VAL A N   
2166 C CA  . VAL A 275 ? 0.4359 0.4962 0.5907 -0.0808 0.0128  0.0491  274 VAL A CA  
2167 C C   . VAL A 275 ? 0.3827 0.4628 0.5593 -0.0768 0.0271  0.0636  274 VAL A C   
2168 O O   . VAL A 275 ? 0.3897 0.4744 0.5834 -0.0815 0.0311  0.0746  274 VAL A O   
2169 C CB  . VAL A 275 ? 0.4444 0.5090 0.6061 -0.0859 -0.0021 0.0460  274 VAL A CB  
2170 C CG1 . VAL A 275 ? 0.4120 0.4926 0.6085 -0.0959 -0.0091 0.0591  274 VAL A CG1 
2171 C CG2 . VAL A 275 ? 0.4336 0.4761 0.5724 -0.0896 -0.0155 0.0328  274 VAL A CG2 
2172 N N   . SER A 276 ? 0.3588 0.4496 0.5340 -0.0674 0.0358  0.0645  275 SER A N   
2173 C CA  . SER A 276 ? 0.3415 0.4473 0.5296 -0.0596 0.0525  0.0767  275 SER A CA  
2174 C C   . SER A 276 ? 0.3967 0.4913 0.5644 -0.0525 0.0656  0.0755  275 SER A C   
2175 O O   . SER A 276 ? 0.3768 0.4809 0.5534 -0.0466 0.0800  0.0869  275 SER A O   
2176 C CB  . SER A 276 ? 0.3441 0.4591 0.5307 -0.0499 0.0581  0.0760  275 SER A CB  
2177 O OG  . SER A 276 ? 0.3837 0.4824 0.5384 -0.0427 0.0604  0.0626  275 SER A OG  
2178 N N   . PHE A 277 ? 0.3923 0.4676 0.5329 -0.0523 0.0611  0.0627  276 PHE A N   
2179 C CA  . PHE A 277 ? 0.3969 0.4600 0.5139 -0.0453 0.0707  0.0594  276 PHE A CA  
2180 C C   . PHE A 277 ? 0.4259 0.4922 0.5315 -0.0328 0.0842  0.0602  276 PHE A C   
2181 O O   . PHE A 277 ? 0.3997 0.4672 0.5019 -0.0262 0.0972  0.0676  276 PHE A O   
2182 C CB  . PHE A 277 ? 0.3995 0.4612 0.5244 -0.0489 0.0755  0.0690  276 PHE A CB  
2183 C CG  . PHE A 277 ? 0.4295 0.4731 0.5291 -0.0470 0.0754  0.0617  276 PHE A CG  
2184 C CD1 . PHE A 277 ? 0.4256 0.4562 0.5199 -0.0544 0.0630  0.0545  276 PHE A CD1 
2185 C CD2 . PHE A 277 ? 0.4536 0.4921 0.5328 -0.0370 0.0871  0.0615  276 PHE A CD2 
2186 C CE1 . PHE A 277 ? 0.4398 0.4551 0.5123 -0.0516 0.0632  0.0487  276 PHE A CE1 
2187 C CE2 . PHE A 277 ? 0.3913 0.4146 0.4481 -0.0353 0.0856  0.0553  276 PHE A CE2 
2188 C CZ  . PHE A 277 ? 0.3996 0.4127 0.4546 -0.0424 0.0741  0.0494  276 PHE A CZ  
2189 N N   . THR A 278 ? 0.3589 0.4245 0.4565 -0.0291 0.0811  0.0524  277 THR A N   
2190 C CA  . THR A 278 ? 0.3979 0.4639 0.4848 -0.0176 0.0924  0.0525  277 THR A CA  
2191 C C   . THR A 278 ? 0.3938 0.4465 0.4570 -0.0148 0.0872  0.0391  277 THR A C   
2192 O O   . THR A 278 ? 0.3805 0.4304 0.4427 -0.0210 0.0754  0.0319  277 THR A O   
2193 C CB  . THR A 278 ? 0.3929 0.4770 0.5040 -0.0145 0.0970  0.0624  277 THR A CB  
2194 O OG1 . THR A 278 ? 0.3687 0.4590 0.4933 -0.0221 0.0834  0.0596  277 THR A OG1 
2195 C CG2 . THR A 278 ? 0.3613 0.4609 0.4976 -0.0155 0.1054  0.0785  277 THR A CG2 
2196 N N   . TRP A 279 ? 0.4033 0.4474 0.4470 -0.0050 0.0963  0.0364  278 TRP A N   
2197 C CA  . TRP A 279 ? 0.4088 0.4395 0.4305 -0.0020 0.0926  0.0252  278 TRP A CA  
2198 C C   . TRP A 279 ? 0.4321 0.4656 0.4568 0.0047  0.0968  0.0261  278 TRP A C   
2199 O O   . TRP A 279 ? 0.4440 0.4863 0.4797 0.0115  0.1070  0.0351  278 TRP A O   
2200 C CB  . TRP A 279 ? 0.4122 0.4273 0.4068 0.0037  0.0977  0.0207  278 TRP A CB  
2201 C CG  . TRP A 279 ? 0.4187 0.4270 0.4036 -0.0018 0.0913  0.0168  278 TRP A CG  
2202 C CD1 . TRP A 279 ? 0.4151 0.4225 0.3979 -0.0016 0.0958  0.0221  278 TRP A CD1 
2203 C CD2 . TRP A 279 ? 0.3928 0.3944 0.3688 -0.0071 0.0803  0.0078  278 TRP A CD2 
2204 N NE1 . TRP A 279 ? 0.3790 0.3792 0.3520 -0.0063 0.0877  0.0165  278 TRP A NE1 
2205 C CE2 . TRP A 279 ? 0.3672 0.3644 0.3365 -0.0095 0.0785  0.0079  278 TRP A CE2 
2206 C CE3 . TRP A 279 ? 0.4110 0.4107 0.3851 -0.0095 0.0726  0.0009  278 TRP A CE3 
2207 C CZ2 . TRP A 279 ? 0.3968 0.3888 0.3584 -0.0135 0.0694  0.0014  278 TRP A CZ2 
2208 C CZ3 . TRP A 279 ? 0.3967 0.3918 0.3634 -0.0139 0.0641  -0.0050 278 TRP A CZ3 
2209 C CH2 . TRP A 279 ? 0.3801 0.3719 0.3410 -0.0155 0.0627  -0.0047 278 TRP A CH2 
2210 N N   . LYS A 280 ? 0.4218 0.4476 0.4368 0.0036  0.0896  0.0176  279 LYS A N   
2211 C CA  . LYS A 280 ? 0.3971 0.4221 0.4126 0.0100  0.0926  0.0177  279 LYS A CA  
2212 C C   . LYS A 280 ? 0.4560 0.4650 0.4512 0.0093  0.0865  0.0074  279 LYS A C   
2213 O O   . LYS A 280 ? 0.4309 0.4395 0.4255 0.0017  0.0766  0.0024  279 LYS A O   
2214 C CB  . LYS A 280 ? 0.4222 0.4645 0.4633 0.0062  0.0877  0.0237  279 LYS A CB  
2215 C CG  . LYS A 280 ? 0.4450 0.4906 0.4922 0.0141  0.0925  0.0274  279 LYS A CG  
2216 C CD  . LYS A 280 ? 0.4882 0.5500 0.5582 0.0085  0.0833  0.0318  279 LYS A CD  
2217 C CE  . LYS A 280 ? 0.6222 0.6926 0.7049 0.0169  0.0887  0.0390  279 LYS A CE  
2218 N NZ  . LYS A 280 ? 0.6630 0.7172 0.7272 0.0237  0.0909  0.0328  279 LYS A NZ  
2219 N N   . LYS A 281 ? 0.4860 0.4809 0.4644 0.0176  0.0927  0.0046  280 LYS A N   
2220 C CA  . LYS A 281 ? 0.4375 0.4163 0.3989 0.0164  0.0866  -0.0040 280 LYS A CA  
2221 C C   . LYS A 281 ? 0.4801 0.4648 0.4542 0.0153  0.0826  -0.0026 280 LYS A C   
2222 O O   . LYS A 281 ? 0.5053 0.4976 0.4915 0.0215  0.0887  0.0037  280 LYS A O   
2223 C CB  . LYS A 281 ? 0.4334 0.3916 0.3704 0.0256  0.0935  -0.0078 280 LYS A CB  
2224 C CG  . LYS A 281 ? 0.4926 0.4311 0.4095 0.0220  0.0850  -0.0172 280 LYS A CG  
2225 C CD  . LYS A 281 ? 0.5485 0.4629 0.4390 0.0316  0.0907  -0.0216 280 LYS A CD  
2226 C CE  . LYS A 281 ? 0.6124 0.5056 0.4827 0.0263  0.0801  -0.0308 280 LYS A CE  
2227 N NZ  . LYS A 281 ? 0.6615 0.5524 0.5407 0.0218  0.0739  -0.0319 280 LYS A NZ  
2228 N N   . ILE A 282 ? 0.4810 0.4635 0.4535 0.0080  0.0729  -0.0074 281 ILE A N   
2229 C CA  . ILE A 282 ? 0.4452 0.4337 0.4284 0.0062  0.0682  -0.0057 281 ILE A CA  
2230 C C   . ILE A 282 ? 0.5061 0.4772 0.4752 0.0073  0.0664  -0.0104 281 ILE A C   
2231 O O   . ILE A 282 ? 0.5389 0.4977 0.4935 0.0039  0.0628  -0.0161 281 ILE A O   
2232 C CB  . ILE A 282 ? 0.4362 0.4360 0.4282 -0.0023 0.0592  -0.0061 281 ILE A CB  
2233 C CG1 . ILE A 282 ? 0.4578 0.4718 0.4638 -0.0045 0.0592  -0.0018 281 ILE A CG1 
2234 C CG2 . ILE A 282 ? 0.4422 0.4463 0.4410 -0.0033 0.0545  -0.0044 281 ILE A CG2 
2235 C CD1 . ILE A 282 ? 0.4960 0.5212 0.5181 0.0002  0.0641  0.0059  281 ILE A CD1 
2236 N N   . GLU A 283 ? 0.4925 0.4623 0.4666 0.0117  0.0682  -0.0073 282 GLU A N   
2237 C CA  . GLU A 283 ? 0.5220 0.4736 0.4843 0.0125  0.0664  -0.0107 282 GLU A CA  
2238 C C   . GLU A 283 ? 0.4790 0.4385 0.4520 0.0079  0.0602  -0.0077 282 GLU A C   
2239 O O   . GLU A 283 ? 0.5107 0.4765 0.4938 0.0126  0.0624  -0.0023 282 GLU A O   
2240 C CB  . GLU A 283 ? 0.5938 0.5322 0.5490 0.0235  0.0750  -0.0095 282 GLU A CB  
2241 C CG  . GLU A 283 ? 0.6774 0.6059 0.6181 0.0303  0.0827  -0.0120 282 GLU A CG  
2242 C CD  . GLU A 283 ? 0.7698 0.6742 0.6857 0.0274  0.0783  -0.0209 282 GLU A CD  
2243 O OE1 . GLU A 283 ? 0.7821 0.6783 0.6952 0.0198  0.0693  -0.0243 282 GLU A OE1 
2244 O OE2 . GLU A 283 ? 0.7436 0.6377 0.6432 0.0329  0.0834  -0.0238 282 GLU A OE2 
2245 N N   . PRO A 284 ? 0.4870 0.4473 0.4583 -0.0003 0.0530  -0.0102 283 PRO A N   
2246 C CA  . PRO A 284 ? 0.4735 0.4398 0.4524 -0.0034 0.0486  -0.0065 283 PRO A CA  
2247 C C   . PRO A 284 ? 0.4364 0.3872 0.4108 -0.0008 0.0495  -0.0052 283 PRO A C   
2248 O O   . PRO A 284 ? 0.4562 0.3876 0.4181 0.0005  0.0508  -0.0094 283 PRO A O   
2249 C CB  . PRO A 284 ? 0.4020 0.3719 0.3791 -0.0114 0.0427  -0.0088 283 PRO A CB  
2250 C CG  . PRO A 284 ? 0.4496 0.4116 0.4167 -0.0130 0.0427  -0.0142 283 PRO A CG  
2251 C CD  . PRO A 284 ? 0.4926 0.4514 0.4566 -0.0061 0.0493  -0.0149 283 PRO A CD  
2252 N N   . LYS A 285 ? 0.4296 0.3872 0.4126 0.0001  0.0484  0.0005  284 LYS A N   
2253 C CA  . LYS A 285 ? 0.4373 0.3804 0.4174 0.0012  0.0484  0.0030  284 LYS A CA  
2254 C C   . LYS A 285 ? 0.4497 0.3856 0.4261 -0.0077 0.0428  0.0017  284 LYS A C   
2255 O O   . LYS A 285 ? 0.4283 0.3758 0.4076 -0.0136 0.0393  0.0012  284 LYS A O   
2256 C CB  . LYS A 285 ? 0.4355 0.3893 0.4260 0.0050  0.0488  0.0109  284 LYS A CB  
2257 C CG  . LYS A 285 ? 0.4396 0.4065 0.4391 0.0125  0.0522  0.0145  284 LYS A CG  
2258 C CD  . LYS A 285 ? 0.5172 0.4715 0.5129 0.0213  0.0595  0.0139  284 LYS A CD  
2259 C CE  . LYS A 285 ? 0.5741 0.5462 0.5839 0.0286  0.0631  0.0199  284 LYS A CE  
2260 N NZ  . LYS A 285 ? 0.6298 0.5935 0.6362 0.0379  0.0723  0.0194  284 LYS A NZ  
2261 N N   . GLY A 286 ? 0.4664 0.3827 0.4373 -0.0086 0.0419  0.0020  285 GLY A N   
2262 C CA  . GLY A 286 ? 0.4368 0.3460 0.4075 -0.0180 0.0359  0.0027  285 GLY A CA  
2263 C C   . GLY A 286 ? 0.4926 0.3884 0.4524 -0.0231 0.0316  -0.0051 285 GLY A C   
2264 O O   . GLY A 286 ? 0.5150 0.4099 0.4665 -0.0195 0.0337  -0.0110 285 GLY A O   
2265 N N   . LYS A 287 ? 0.5668 0.4525 0.5271 -0.0320 0.0248  -0.0041 286 LYS A N   
2266 C CA  . LYS A 287 ? 0.5540 0.4275 0.5048 -0.0387 0.0178  -0.0106 286 LYS A CA  
2267 C C   . LYS A 287 ? 0.5594 0.4556 0.5189 -0.0437 0.0154  -0.0094 286 LYS A C   
2268 O O   . LYS A 287 ? 0.5700 0.4826 0.5440 -0.0484 0.0142  -0.0020 286 LYS A O   
2269 C CB  . LYS A 287 ? 0.5779 0.4316 0.5284 -0.0474 0.0099  -0.0089 286 LYS A CB  
2270 C CG  . LYS A 287 ? 0.6476 0.4882 0.5895 -0.0562 -0.0004 -0.0148 286 LYS A CG  
2271 C CD  . LYS A 287 ? 0.7942 0.6139 0.7378 -0.0660 -0.0096 -0.0122 286 LYS A CD  
2272 C CE  . LYS A 287 ? 0.9098 0.7130 0.8421 -0.0749 -0.0221 -0.0191 286 LYS A CE  
2273 N NZ  . LYS A 287 ? 0.9656 0.7608 0.8756 -0.0661 -0.0192 -0.0298 286 LYS A NZ  
2274 N N   . GLY A 288 ? 0.5147 0.4120 0.4650 -0.0415 0.0156  -0.0158 287 GLY A N   
2275 C CA  . GLY A 288 ? 0.4838 0.4013 0.4416 -0.0448 0.0139  -0.0146 287 GLY A CA  
2276 C C   . GLY A 288 ? 0.4677 0.3824 0.4272 -0.0546 0.0044  -0.0144 287 GLY A C   
2277 O O   . GLY A 288 ? 0.4523 0.3511 0.4104 -0.0609 -0.0023 -0.0140 287 GLY A O   
2278 N N   . PRO A 289 ? 0.4543 0.3845 0.4178 -0.0563 0.0028  -0.0142 288 PRO A N   
2279 C CA  . PRO A 289 ? 0.4075 0.3356 0.3715 -0.0646 -0.0071 -0.0146 288 PRO A CA  
2280 C C   . PRO A 289 ? 0.4377 0.3418 0.3802 -0.0644 -0.0124 -0.0237 288 PRO A C   
2281 O O   . PRO A 289 ? 0.4581 0.3536 0.3857 -0.0561 -0.0062 -0.0296 288 PRO A O   
2282 C CB  . PRO A 289 ? 0.3738 0.3244 0.3457 -0.0631 -0.0051 -0.0121 288 PRO A CB  
2283 C CG  . PRO A 289 ? 0.4074 0.3629 0.3744 -0.0539 0.0044  -0.0146 288 PRO A CG  
2284 C CD  . PRO A 289 ? 0.3922 0.3421 0.3606 -0.0507 0.0092  -0.0130 288 PRO A CD  
2285 N N   . CYS A 290 ? 0.4375 0.3308 0.3783 -0.0736 -0.0243 -0.0243 289 CYS A N   
2286 C CA  . CYS A 290 ? 0.4590 0.3289 0.3764 -0.0741 -0.0317 -0.0333 289 CYS A CA  
2287 C C   . CYS A 290 ? 0.4288 0.3089 0.3385 -0.0692 -0.0294 -0.0362 289 CYS A C   
2288 O O   . CYS A 290 ? 0.4068 0.3118 0.3323 -0.0688 -0.0260 -0.0307 289 CYS A O   
2289 C CB  . CYS A 290 ? 0.4901 0.3497 0.4106 -0.0870 -0.0476 -0.0321 289 CYS A CB  
2290 S SG  . CYS A 290 ? 0.4689 0.3601 0.4156 -0.0959 -0.0550 -0.0223 289 CYS A SG  
2291 N N   . PRO A 291 ? 0.4682 0.3281 0.3522 -0.0642 -0.0304 -0.0446 290 PRO A N   
2292 C CA  . PRO A 291 ? 0.4757 0.3443 0.3516 -0.0594 -0.0279 -0.0463 290 PRO A CA  
2293 C C   . PRO A 291 ? 0.4810 0.3661 0.3700 -0.0676 -0.0381 -0.0417 290 PRO A C   
2294 O O   . PRO A 291 ? 0.5098 0.3887 0.4018 -0.0774 -0.0513 -0.0407 290 PRO A O   
2295 C CB  . PRO A 291 ? 0.5234 0.3627 0.3667 -0.0540 -0.0298 -0.0556 290 PRO A CB  
2296 C CG  . PRO A 291 ? 0.5222 0.3409 0.3578 -0.0511 -0.0262 -0.0587 290 PRO A CG  
2297 C CD  . PRO A 291 ? 0.4940 0.3207 0.3530 -0.0616 -0.0330 -0.0526 290 PRO A CD  
2298 N N   . ARG A 292 ? 0.4385 0.3450 0.3370 -0.0638 -0.0323 -0.0378 291 ARG A N   
2299 C CA  . ARG A 292 ? 0.4222 0.3485 0.3375 -0.0697 -0.0394 -0.0314 291 ARG A CA  
2300 C C   . ARG A 292 ? 0.4206 0.3609 0.3358 -0.0626 -0.0320 -0.0301 291 ARG A C   
2301 O O   . ARG A 292 ? 0.4388 0.3775 0.3470 -0.0547 -0.0212 -0.0326 291 ARG A O   
2302 C CB  . ARG A 292 ? 0.3948 0.3395 0.3373 -0.0750 -0.0388 -0.0226 291 ARG A CB  
2303 C CG  . ARG A 292 ? 0.3821 0.3402 0.3342 -0.0678 -0.0250 -0.0198 291 ARG A CG  
2304 C CD  . ARG A 292 ? 0.3501 0.3251 0.3255 -0.0715 -0.0235 -0.0108 291 ARG A CD  
2305 N NE  . ARG A 292 ? 0.3888 0.3519 0.3674 -0.0782 -0.0284 -0.0095 291 ARG A NE  
2306 C CZ  . ARG A 292 ? 0.3813 0.3560 0.3796 -0.0829 -0.0284 -0.0005 291 ARG A CZ  
2307 N NH1 . ARG A 292 ? 0.3294 0.3283 0.3447 -0.0806 -0.0230 0.0078  291 ARG A NH1 
2308 N NH2 . ARG A 292 ? 0.3858 0.3464 0.3857 -0.0895 -0.0335 0.0005  291 ARG A NH2 
2309 N N   . ARG A 293 ? 0.4170 0.3717 0.3416 -0.0655 -0.0383 -0.0253 292 ARG A N   
2310 C CA  . ARG A 293 ? 0.4059 0.3724 0.3306 -0.0590 -0.0324 -0.0235 292 ARG A CA  
2311 C C   . ARG A 293 ? 0.3762 0.3671 0.3250 -0.0601 -0.0319 -0.0146 292 ARG A C   
2312 O O   . ARG A 293 ? 0.3882 0.3882 0.3525 -0.0670 -0.0396 -0.0089 292 ARG A O   
2313 C CB  . ARG A 293 ? 0.4155 0.3723 0.3215 -0.0583 -0.0398 -0.0265 292 ARG A CB  
2314 C CG  . ARG A 293 ? 0.4509 0.4095 0.3617 -0.0672 -0.0560 -0.0237 292 ARG A CG  
2315 C CD  . ARG A 293 ? 0.4955 0.4475 0.3880 -0.0650 -0.0630 -0.0257 292 ARG A CD  
2316 N NE  . ARG A 293 ? 0.4886 0.4511 0.3919 -0.0724 -0.0781 -0.0200 292 ARG A NE  
2317 C CZ  . ARG A 293 ? 0.4929 0.4403 0.3817 -0.0790 -0.0941 -0.0236 292 ARG A CZ  
2318 N NH1 . ARG A 293 ? 0.5129 0.4317 0.3747 -0.0791 -0.0968 -0.0333 292 ARG A NH1 
2319 N NH2 . ARG A 293 ? 0.5086 0.4690 0.4091 -0.0850 -0.1081 -0.0171 292 ARG A NH2 
2320 N N   . ARG A 294 ? 0.3699 0.3705 0.3216 -0.0529 -0.0226 -0.0131 293 ARG A N   
2321 C CA  . ARG A 294 ? 0.3478 0.3686 0.3163 -0.0508 -0.0212 -0.0055 293 ARG A CA  
2322 C C   . ARG A 294 ? 0.3365 0.3707 0.3247 -0.0532 -0.0191 0.0008  293 ARG A C   
2323 O O   . ARG A 294 ? 0.3036 0.3552 0.3085 -0.0535 -0.0206 0.0092  293 ARG A O   
2324 C CB  . ARG A 294 ? 0.3288 0.3549 0.2982 -0.0531 -0.0313 -0.0018 293 ARG A CB  
2325 C CG  . ARG A 294 ? 0.3503 0.3927 0.3299 -0.0469 -0.0274 0.0046  293 ARG A CG  
2326 C CD  . ARG A 294 ? 0.3368 0.3739 0.3065 -0.0383 -0.0164 0.0010  293 ARG A CD  
2327 N NE  . ARG A 294 ? 0.3433 0.3936 0.3221 -0.0320 -0.0132 0.0072  293 ARG A NE  
2328 C CZ  . ARG A 294 ? 0.3291 0.3752 0.3008 -0.0248 -0.0063 0.0059  293 ARG A CZ  
2329 N NH1 . ARG A 294 ? 0.3780 0.4098 0.3359 -0.0237 -0.0016 -0.0005 293 ARG A NH1 
2330 N NH2 . ARG A 294 ? 0.3047 0.3613 0.2842 -0.0185 -0.0041 0.0118  293 ARG A NH2 
2331 N N   . GLN A 295 ? 0.3448 0.3711 0.3309 -0.0543 -0.0151 -0.0022 294 GLN A N   
2332 C CA  . GLN A 295 ? 0.3155 0.3524 0.3150 -0.0530 -0.0087 0.0029  294 GLN A CA  
2333 C C   . GLN A 295 ? 0.3319 0.3763 0.3307 -0.0440 0.0007  0.0032  294 GLN A C   
2334 O O   . GLN A 295 ? 0.2874 0.3269 0.2761 -0.0398 0.0024  -0.0008 294 GLN A O   
2335 C CB  . GLN A 295 ? 0.3002 0.3245 0.2943 -0.0549 -0.0066 -0.0012 294 GLN A CB  
2336 C CG  . GLN A 295 ? 0.3021 0.3149 0.2812 -0.0491 0.0000  -0.0087 294 GLN A CG  
2337 C CD  . GLN A 295 ? 0.3647 0.3647 0.3279 -0.0485 -0.0029 -0.0147 294 GLN A CD  
2338 O OE1 . GLN A 295 ? 0.4082 0.3972 0.3641 -0.0531 -0.0104 -0.0170 294 GLN A OE1 
2339 N NE2 . GLN A 295 ? 0.3335 0.3336 0.2902 -0.0427 0.0026  -0.0169 294 GLN A NE2 
2340 N N   . CYS A 296 ? 0.3342 0.3357 0.3121 0.0394  0.0453  0.0025  295 CYS A N   
2341 C CA  . CYS A 296 ? 0.3367 0.3342 0.3149 0.0451  0.0528  0.0031  295 CYS A CA  
2342 C C   . CYS A 296 ? 0.3853 0.3731 0.3655 0.0413  0.0529  -0.0005 295 CYS A C   
2343 O O   . CYS A 296 ? 0.3753 0.3651 0.3610 0.0355  0.0489  -0.0003 295 CYS A O   
2344 C CB  . CYS A 296 ? 0.3214 0.3315 0.3029 0.0504  0.0558  0.0096  295 CYS A CB  
2345 S SG  . CYS A 296 ? 0.4335 0.4536 0.4154 0.0588  0.0589  0.0169  295 CYS A SG  
2346 N N   . CYS A 297 ? 0.3770 0.3543 0.3548 0.0436  0.0562  -0.0021 296 CYS A N   
2347 C CA  . CYS A 297 ? 0.3295 0.2997 0.3103 0.0393  0.0547  -0.0031 296 CYS A CA  
2348 C C   . CYS A 297 ? 0.3864 0.3488 0.3600 0.0412  0.0543  -0.0048 296 CYS A C   
2349 O O   . CYS A 297 ? 0.4011 0.3541 0.3707 0.0454  0.0557  -0.0056 296 CYS A O   
2350 C CB  . CYS A 297 ? 0.3394 0.3034 0.3255 0.0382  0.0560  -0.0016 296 CYS A CB  
2351 S SG  . CYS A 297 ? 0.4242 0.3893 0.4126 0.0379  0.0565  -0.0032 296 CYS A SG  
2352 N N   . CYS A 298 ? 0.3769 0.3411 0.3473 0.0385  0.0516  -0.0054 297 CYS A N   
2353 C CA  . CYS A 298 ? 0.3484 0.3011 0.3045 0.0407  0.0493  -0.0100 297 CYS A CA  
2354 C C   . CYS A 298 ? 0.3786 0.3296 0.3360 0.0323  0.0423  -0.0089 297 CYS A C   
2355 O O   . CYS A 298 ? 0.3645 0.3281 0.3334 0.0276  0.0418  -0.0033 297 CYS A O   
2356 C CB  . CYS A 298 ? 0.3583 0.3190 0.3015 0.0502  0.0543  -0.0108 297 CYS A CB  
2357 S SG  . CYS A 298 ? 0.3990 0.3650 0.3436 0.0612  0.0622  -0.0083 297 CYS A SG  
2358 N N   . ILE A 299 ? 0.3863 0.3200 0.3321 0.0299  0.0355  -0.0137 298 ILE A N   
2359 C CA  . ILE A 299 ? 0.3608 0.2929 0.3079 0.0200  0.0256  -0.0112 298 ILE A CA  
2360 C C   . ILE A 299 ? 0.4305 0.3635 0.3537 0.0232  0.0230  -0.0162 298 ILE A C   
2361 O O   . ILE A 299 ? 0.4461 0.3651 0.3447 0.0324  0.0246  -0.0258 298 ILE A O   
2362 C CB  . ILE A 299 ? 0.4002 0.3129 0.3503 0.0123  0.0157  -0.0114 298 ILE A CB  
2363 C CG1 . ILE A 299 ? 0.4104 0.3279 0.3842 0.0116  0.0209  -0.0030 298 ILE A CG1 
2364 C CG2 . ILE A 299 ? 0.4308 0.3454 0.3853 0.0000  0.0029  -0.0059 298 ILE A CG2 
2365 C CD1 . ILE A 299 ? 0.3560 0.2591 0.3401 0.0034  0.0115  0.0022  298 ILE A CD1 
2366 N N   . VAL A 300 ? 0.4007 0.3503 0.3301 0.0176  0.0200  -0.0087 299 VAL A N   
2367 C CA  . VAL A 300 ? 0.4411 0.3959 0.3472 0.0202  0.0168  -0.0105 299 VAL A CA  
2368 C C   . VAL A 300 ? 0.4219 0.3801 0.3342 0.0073  0.0039  -0.0038 299 VAL A C   
2369 O O   . VAL A 300 ? 0.4221 0.4006 0.3575 0.0023  0.0050  0.0091  299 VAL A O   
2370 C CB  . VAL A 300 ? 0.4223 0.4029 0.3326 0.0276  0.0272  -0.0023 299 VAL A CB  
2371 C CG1 . VAL A 300 ? 0.3810 0.3695 0.2638 0.0329  0.0257  -0.0025 299 VAL A CG1 
2372 C CG2 . VAL A 300 ? 0.4015 0.3839 0.3129 0.0385  0.0385  -0.0046 299 VAL A CG2 
2373 N N   . GLY A 301 ? 0.4483 0.3855 0.3410 0.0014  -0.0097 -0.0117 300 GLY A N   
2374 C CA  . GLY A 301 ? 0.3905 0.3324 0.2931 -0.0134 -0.0250 -0.0027 300 GLY A CA  
2375 C C   . GLY A 301 ? 0.4716 0.4233 0.4161 -0.0212 -0.0235 0.0112  300 GLY A C   
2376 O O   . GLY A 301 ? 0.4419 0.3810 0.3976 -0.0214 -0.0216 0.0094  300 GLY A O   
2377 N N   . ASP A 302 ? 0.4013 0.3767 0.3694 -0.0255 -0.0227 0.0266  301 ASP A N   
2378 C CA  . ASP A 302 ? 0.3986 0.3851 0.4047 -0.0287 -0.0184 0.0409  301 ASP A CA  
2379 C C   . ASP A 302 ? 0.4070 0.4008 0.4269 -0.0181 -0.0014 0.0416  301 ASP A C   
2380 O O   . ASP A 302 ? 0.3658 0.3688 0.4128 -0.0171 0.0043  0.0528  301 ASP A O   
2381 C CB  . ASP A 302 ? 0.4323 0.4382 0.4579 -0.0379 -0.0273 0.0586  301 ASP A CB  
2382 C CG  . ASP A 302 ? 0.4591 0.4584 0.4753 -0.0516 -0.0479 0.0603  301 ASP A CG  
2383 O OD1 . ASP A 302 ? 0.4709 0.4517 0.4856 -0.0564 -0.0545 0.0552  301 ASP A OD1 
2384 O OD2 . ASP A 302 ? 0.4962 0.5082 0.5065 -0.0585 -0.0589 0.0677  301 ASP A OD2 
2385 N N   . LYS A 303 ? 0.3719 0.3613 0.3736 -0.0098 0.0061  0.0306  302 LYS A N   
2386 C CA  . LYS A 303 ? 0.3622 0.3570 0.3751 -0.0025 0.0179  0.0310  302 LYS A CA  
2387 C C   . LYS A 303 ? 0.3730 0.3555 0.3757 0.0043  0.0244  0.0199  302 LYS A C   
2388 O O   . LYS A 303 ? 0.4211 0.3923 0.4042 0.0062  0.0219  0.0112  302 LYS A O   
2389 C CB  . LYS A 303 ? 0.3264 0.3350 0.3349 -0.0005 0.0198  0.0346  302 LYS A CB  
2390 C CG  . LYS A 303 ? 0.3565 0.3799 0.3751 -0.0068 0.0133  0.0478  302 LYS A CG  
2391 C CD  . LYS A 303 ? 0.3487 0.3886 0.3610 -0.0044 0.0151  0.0538  302 LYS A CD  
2392 C CE  . LYS A 303 ? 0.3847 0.4409 0.3988 -0.0102 0.0070  0.0667  302 LYS A CE  
2393 N NZ  . LYS A 303 ? 0.4393 0.5152 0.4460 -0.0061 0.0106  0.0747  302 LYS A NZ  
2394 N N   . ILE A 304 ? 0.3636 0.3465 0.3784 0.0085  0.0320  0.0203  303 ILE A N   
2395 C CA  . ILE A 304 ? 0.3411 0.3173 0.3476 0.0147  0.0377  0.0123  303 ILE A CA  
2396 C C   . ILE A 304 ? 0.3280 0.3125 0.3353 0.0171  0.0405  0.0123  303 ILE A C   
2397 O O   . ILE A 304 ? 0.2920 0.2798 0.3128 0.0149  0.0404  0.0172  303 ILE A O   
2398 C CB  . ILE A 304 ? 0.3796 0.3504 0.3958 0.0175  0.0424  0.0132  303 ILE A CB  
2399 C CG1 . ILE A 304 ? 0.3415 0.3122 0.3696 0.0131  0.0390  0.0214  303 ILE A CG1 
2400 C CG2 . ILE A 304 ? 0.3574 0.3223 0.3629 0.0230  0.0462  0.0067  303 ILE A CG2 
2401 C CD1 . ILE A 304 ? 0.3677 0.3290 0.3864 0.0088  0.0319  0.0188  303 ILE A CD1 
2402 N N   . VAL A 305 ? 0.3673 0.3547 0.3622 0.0215  0.0425  0.0086  304 VAL A N   
2403 C CA  . VAL A 305 ? 0.3429 0.3414 0.3428 0.0227  0.0440  0.0119  304 VAL A CA  
2404 C C   . VAL A 305 ? 0.3368 0.3289 0.3365 0.0251  0.0457  0.0071  304 VAL A C   
2405 O O   . VAL A 305 ? 0.3299 0.3177 0.3199 0.0303  0.0487  0.0029  304 VAL A O   
2406 C CB  . VAL A 305 ? 0.3512 0.3626 0.3404 0.0282  0.0468  0.0148  304 VAL A CB  
2407 C CG1 . VAL A 305 ? 0.2983 0.3272 0.2999 0.0278  0.0474  0.0238  304 VAL A CG1 
2408 C CG2 . VAL A 305 ? 0.3213 0.3388 0.3038 0.0271  0.0448  0.0187  304 VAL A CG2 
2409 N N   . LEU A 306 ? 0.3143 0.3038 0.3232 0.0215  0.0429  0.0075  305 LEU A N   
2410 C CA  . LEU A 306 ? 0.2906 0.2730 0.2950 0.0233  0.0424  0.0020  305 LEU A CA  
2411 C C   . LEU A 306 ? 0.3470 0.3370 0.3580 0.0181  0.0356  0.0059  305 LEU A C   
2412 O O   . LEU A 306 ? 0.3751 0.3658 0.3984 0.0119  0.0304  0.0108  305 LEU A O   
2413 C CB  . LEU A 306 ? 0.3180 0.2855 0.3221 0.0248  0.0438  -0.0027 305 LEU A CB  
2414 C CG  . LEU A 306 ? 0.3963 0.3531 0.3885 0.0294  0.0445  -0.0101 305 LEU A CG  
2415 C CD1 . LEU A 306 ? 0.3277 0.2742 0.3191 0.0361  0.0513  -0.0116 305 LEU A CD1 
2416 C CD2 . LEU A 306 ? 0.3494 0.2993 0.3384 0.0246  0.0351  -0.0144 305 LEU A CD2 
2417 N N   . PHE A 307 ? 0.3245 0.3216 0.3308 0.0196  0.0342  0.0061  306 PHE A N   
2418 C CA  . PHE A 307 ? 0.3429 0.3521 0.3602 0.0126  0.0255  0.0140  306 PHE A CA  
2419 C C   . PHE A 307 ? 0.3387 0.3521 0.3489 0.0136  0.0219  0.0129  306 PHE A C   
2420 O O   . PHE A 307 ? 0.3261 0.3402 0.3259 0.0220  0.0293  0.0102  306 PHE A O   
2421 C CB  . PHE A 307 ? 0.3089 0.3420 0.3386 0.0135  0.0288  0.0278  306 PHE A CB  
2422 C CG  . PHE A 307 ? 0.3154 0.3596 0.3362 0.0246  0.0385  0.0296  306 PHE A CG  
2423 C CD1 . PHE A 307 ? 0.3299 0.3621 0.3362 0.0323  0.0464  0.0213  306 PHE A CD1 
2424 C CD2 . PHE A 307 ? 0.3252 0.3902 0.3533 0.0275  0.0387  0.0403  306 PHE A CD2 
2425 C CE1 . PHE A 307 ? 0.3170 0.3517 0.3131 0.0433  0.0542  0.0209  306 PHE A CE1 
2426 C CE2 . PHE A 307 ? 0.3236 0.3955 0.3433 0.0407  0.0492  0.0418  306 PHE A CE2 
2427 C CZ  . PHE A 307 ? 0.3015 0.3550 0.3034 0.0490  0.0569  0.0306  306 PHE A CZ  
2428 N N   . GLY A 308 ? 0.3220 0.3382 0.3395 0.0038  0.0087  0.0168  307 GLY A N   
2429 C CA  . GLY A 308 ? 0.3024 0.3257 0.3143 0.0022  0.0015  0.0181  307 GLY A CA  
2430 C C   . GLY A 308 ? 0.3627 0.3630 0.3502 0.0044  -0.0015 0.0026  307 GLY A C   
2431 O O   . GLY A 308 ? 0.3541 0.3316 0.3308 0.0070  0.0014  -0.0090 307 GLY A O   
2432 N N   . GLY A 309 ? 0.3497 0.3589 0.3284 0.0048  -0.0065 0.0043  308 GLY A N   
2433 C CA  . GLY A 309 ? 0.3527 0.3463 0.3044 0.0094  -0.0080 -0.0079 308 GLY A CA  
2434 C C   . GLY A 309 ? 0.3897 0.3715 0.3284 -0.0018 -0.0286 -0.0143 308 GLY A C   
2435 O O   . GLY A 309 ? 0.3751 0.3609 0.3304 -0.0155 -0.0438 -0.0075 308 GLY A O   
2436 N N   . THR A 310 ? 0.4213 0.3877 0.3286 0.0043  -0.0299 -0.0270 309 THR A N   
2437 C CA  . THR A 310 ? 0.4596 0.4094 0.3438 -0.0047 -0.0509 -0.0370 309 THR A CA  
2438 C C   . THR A 310 ? 0.4753 0.3875 0.3264 0.0041  -0.0483 -0.0586 309 THR A C   
2439 O O   . THR A 310 ? 0.5007 0.4099 0.3445 0.0196  -0.0283 -0.0620 309 THR A O   
2440 C CB  . THR A 310 ? 0.4546 0.4250 0.3253 -0.0038 -0.0567 -0.0305 309 THR A CB  
2441 O OG1 . THR A 310 ? 0.4722 0.4778 0.3765 -0.0097 -0.0577 -0.0086 309 THR A OG1 
2442 C CG2 . THR A 310 ? 0.4950 0.4474 0.3372 -0.0146 -0.0819 -0.0418 309 THR A CG2 
2443 N N   . SER A 311 ? 0.5144 0.3970 0.3468 -0.0055 -0.0689 -0.0722 310 SER A N   
2444 C CA  . SER A 311 ? 0.5976 0.4390 0.3930 0.0053  -0.0673 -0.0949 310 SER A CA  
2445 C C   . SER A 311 ? 0.6735 0.4850 0.4382 -0.0068 -0.0962 -0.1102 310 SER A C   
2446 O O   . SER A 311 ? 0.6759 0.4998 0.4587 -0.0272 -0.1187 -0.0999 310 SER A O   
2447 C CB  . SER A 311 ? 0.5862 0.4080 0.4005 0.0083  -0.0580 -0.0976 310 SER A CB  
2448 O OG  . SER A 311 ? 0.5493 0.3642 0.3908 -0.0110 -0.0766 -0.0919 310 SER A OG  
2449 N N   . PRO A 312 ? 0.7391 0.5116 0.4559 0.0060  -0.0968 -0.1339 311 PRO A N   
2450 C CA  . PRO A 312 ? 0.8513 0.5867 0.5315 -0.0058 -0.1274 -0.1526 311 PRO A CA  
2451 C C   . PRO A 312 ? 0.8808 0.5851 0.5838 -0.0258 -0.1499 -0.1555 311 PRO A C   
2452 O O   . PRO A 312 ? 0.8789 0.5739 0.6092 -0.0225 -0.1379 -0.1523 311 PRO A O   
2453 C CB  . PRO A 312 ? 0.7971 0.4959 0.4173 0.0192  -0.1159 -0.1783 311 PRO A CB  
2454 C CG  . PRO A 312 ? 0.7556 0.4737 0.3894 0.0423  -0.0798 -0.1699 311 PRO A CG  
2455 C CD  . PRO A 312 ? 0.7296 0.4974 0.4191 0.0332  -0.0695 -0.1421 311 PRO A CD  
2456 N N   . SER A 313 ? 1.1398 0.8284 0.8326 -0.0477 -0.1846 -0.1599 312 SER A N   
2457 C CA  . SER A 313 ? 1.2007 0.8654 0.9230 -0.0720 -0.2111 -0.1567 312 SER A CA  
2458 C C   . SER A 313 ? 1.3833 0.9750 1.0639 -0.0674 -0.2240 -0.1883 312 SER A C   
2459 O O   . SER A 313 ? 1.4203 0.9768 1.0435 -0.0647 -0.2409 -0.2125 312 SER A O   
2460 C CB  . SER A 313 ? 1.2088 0.8944 0.9472 -0.1006 -0.2451 -0.1420 312 SER A CB  
2461 O OG  . SER A 313 ? 1.3890 1.0328 1.1343 -0.1242 -0.2794 -0.1481 312 SER A OG  
2462 N N   . PRO A 314 ? 1.3199 0.8849 1.0253 -0.0658 -0.2179 -0.1891 313 PRO A N   
2463 C CA  . PRO A 314 ? 1.3493 0.8459 1.0222 -0.0592 -0.2267 -0.2161 313 PRO A CA  
2464 C C   . PRO A 314 ? 1.2779 0.7517 0.9444 -0.0824 -0.2616 -0.2212 313 PRO A C   
2465 O O   . PRO A 314 ? 1.2830 0.7377 0.8991 -0.0744 -0.2668 -0.2413 313 PRO A O   
2466 C CB  . PRO A 314 ? 1.2953 0.7837 1.0157 -0.0601 -0.2166 -0.2041 313 PRO A CB  
2467 C CG  . PRO A 314 ? 1.1549 0.7127 0.9181 -0.0537 -0.1872 -0.1758 313 PRO A CG  
2468 C CD  . PRO A 314 ? 1.1359 0.7400 0.9030 -0.0673 -0.1979 -0.1620 313 PRO A CD  
2469 N N   . PHE A 322 ? 1.4623 1.3142 1.0050 -0.0389 -0.2197 -0.1279 321 PHE A N   
2470 C CA  . PHE A 322 ? 1.4962 1.2855 1.0024 -0.0468 -0.2424 -0.1585 321 PHE A CA  
2471 C C   . PHE A 322 ? 1.3892 1.1605 0.9425 -0.0535 -0.2359 -0.1571 321 PHE A C   
2472 O O   . PHE A 322 ? 1.4276 1.1838 0.9806 -0.0328 -0.2067 -0.1657 321 PHE A O   
2473 C CB  . PHE A 322 ? 1.5395 1.2885 0.9716 -0.0189 -0.2286 -0.1896 321 PHE A CB  
2474 C CG  . PHE A 322 ? 1.6023 1.2912 1.0091 -0.0221 -0.2413 -0.2190 321 PHE A CG  
2475 C CD1 . PHE A 322 ? 1.6852 1.3564 1.0657 -0.0373 -0.2697 -0.2314 321 PHE A CD1 
2476 C CD2 . PHE A 322 ? 1.5954 1.2496 1.0111 -0.0089 -0.2217 -0.2314 321 PHE A CD2 
2477 C CE1 . PHE A 322 ? 1.7501 1.3660 1.1113 -0.0390 -0.2792 -0.2567 321 PHE A CE1 
2478 C CE2 . PHE A 322 ? 1.6405 1.2429 1.0405 -0.0102 -0.2302 -0.2542 321 PHE A CE2 
2479 C CZ  . PHE A 322 ? 1.7309 1.3123 1.1022 -0.0249 -0.2591 -0.2676 321 PHE A CZ  
2480 N N   . ASP A 323 ? 1.1662 0.9436 0.7627 -0.0824 -0.2627 -0.1430 322 ASP A N   
2481 C CA  . ASP A 323 ? 1.1423 0.8938 0.7749 -0.0925 -0.2654 -0.1442 322 ASP A CA  
2482 C C   . ASP A 323 ? 0.9874 0.7605 0.6575 -0.0735 -0.2249 -0.1326 322 ASP A C   
2483 O O   . ASP A 323 ? 0.9990 0.7389 0.6537 -0.0566 -0.2066 -0.1500 322 ASP A O   
2484 C CB  . ASP A 323 ? 1.3007 0.9774 0.8826 -0.0915 -0.2824 -0.1803 322 ASP A CB  
2485 C CG  . ASP A 323 ? 1.3844 1.0413 0.9492 -0.1152 -0.3220 -0.1873 322 ASP A CG  
2486 O OD1 . ASP A 323 ? 1.2987 0.9761 0.9124 -0.1441 -0.3472 -0.1647 322 ASP A OD1 
2487 O OD2 . ASP A 323 ? 1.4897 1.1187 1.0006 -0.1031 -0.3224 -0.2113 322 ASP A OD2 
2488 N N   . LEU A 324 ? 0.8958 0.6556 0.5962 -0.1105 -0.1719 -0.1211 323 LEU A N   
2489 C CA  . LEU A 324 ? 0.7839 0.5796 0.5279 -0.0976 -0.1462 -0.1147 323 LEU A CA  
2490 C C   . LEU A 324 ? 0.7071 0.5301 0.5004 -0.1131 -0.1526 -0.1038 323 LEU A C   
2491 O O   . LEU A 324 ? 0.7865 0.6190 0.5942 -0.1338 -0.1756 -0.0956 323 LEU A O   
2492 C CB  . LEU A 324 ? 0.7358 0.5732 0.5027 -0.0858 -0.1335 -0.1060 323 LEU A CB  
2493 C CG  . LEU A 324 ? 0.7617 0.5825 0.4881 -0.0692 -0.1235 -0.1124 323 LEU A CG  
2494 C CD1 . LEU A 324 ? 0.6061 0.4700 0.3622 -0.0621 -0.1149 -0.1007 323 LEU A CD1 
2495 C CD2 . LEU A 324 ? 0.7471 0.5416 0.4490 -0.0503 -0.1008 -0.1216 323 LEU A CD2 
2496 N N   . ILE A 325 ? 0.6920 0.5298 0.5120 -0.1030 -0.1320 -0.1018 324 ILE A N   
2497 C CA  . ILE A 325 ? 0.5585 0.4275 0.4265 -0.1130 -0.1324 -0.0899 324 ILE A CA  
2498 C C   . ILE A 325 ? 0.5678 0.4775 0.4715 -0.0979 -0.1107 -0.0824 324 ILE A C   
2499 O O   . ILE A 325 ? 0.5582 0.4643 0.4497 -0.0806 -0.0935 -0.0878 324 ILE A O   
2500 C CB  . ILE A 325 ? 0.5807 0.4196 0.4422 -0.1179 -0.1319 -0.0949 324 ILE A CB  
2501 C CG1 . ILE A 325 ? 0.6195 0.4397 0.4630 -0.0960 -0.1079 -0.1048 324 ILE A CG1 
2502 C CG2 . ILE A 325 ? 0.6431 0.4357 0.4675 -0.1348 -0.1564 -0.1021 324 ILE A CG2 
2503 C CD1 . ILE A 325 ? 0.6329 0.4329 0.4790 -0.0965 -0.1026 -0.1071 324 ILE A CD1 
2504 N N   . ASP A 326 ? 0.4830 0.4302 0.4300 -0.1047 -0.1118 -0.0689 325 ASP A N   
2505 C CA  . ASP A 326 ? 0.4493 0.4295 0.4272 -0.0914 -0.0934 -0.0619 325 ASP A CA  
2506 C C   . ASP A 326 ? 0.4430 0.4223 0.4374 -0.0912 -0.0838 -0.0604 325 ASP A C   
2507 O O   . ASP A 326 ? 0.4381 0.4081 0.4368 -0.1054 -0.0942 -0.0578 325 ASP A O   
2508 C CB  . ASP A 326 ? 0.4553 0.4779 0.4659 -0.0943 -0.0992 -0.0471 325 ASP A CB  
2509 C CG  . ASP A 326 ? 0.4722 0.4956 0.4674 -0.0970 -0.1121 -0.0469 325 ASP A CG  
2510 O OD1 . ASP A 326 ? 0.4389 0.4479 0.4095 -0.0853 -0.1044 -0.0552 325 ASP A OD1 
2511 O OD2 . ASP A 326 ? 0.4881 0.5264 0.4954 -0.1114 -0.1305 -0.0374 325 ASP A OD2 
2512 N N   . HIS A 327 ? 0.3870 0.3747 0.3899 -0.0762 -0.0655 -0.0611 326 HIS A N   
2513 C CA  . HIS A 327 ? 0.3919 0.3723 0.4024 -0.0738 -0.0555 -0.0617 326 HIS A CA  
2514 C C   . HIS A 327 ? 0.3654 0.3788 0.4102 -0.0723 -0.0493 -0.0496 326 HIS A C   
2515 O O   . HIS A 327 ? 0.3265 0.3633 0.3837 -0.0630 -0.0432 -0.0445 326 HIS A O   
2516 C CB  . HIS A 327 ? 0.3871 0.3505 0.3805 -0.0588 -0.0406 -0.0701 326 HIS A CB  
2517 C CG  . HIS A 327 ? 0.4496 0.3753 0.4081 -0.0577 -0.0426 -0.0813 326 HIS A CG  
2518 N ND1 . HIS A 327 ? 0.4733 0.3713 0.4205 -0.0620 -0.0446 -0.0858 326 HIS A ND1 
2519 C CD2 . HIS A 327 ? 0.4695 0.3781 0.3984 -0.0516 -0.0429 -0.0885 326 HIS A CD2 
2520 C CE1 . HIS A 327 ? 0.5203 0.3833 0.4303 -0.0568 -0.0454 -0.0963 326 HIS A CE1 
2521 N NE2 . HIS A 327 ? 0.4926 0.3625 0.3906 -0.0502 -0.0438 -0.0979 326 HIS A NE2 
2522 N N   . SER A 328 ? 0.3400 0.3524 0.3970 -0.0808 -0.0509 -0.0447 327 SER A N   
2523 C CA  . SER A 328 ? 0.3554 0.3938 0.4393 -0.0769 -0.0418 -0.0339 327 SER A CA  
2524 C C   . SER A 328 ? 0.3863 0.4094 0.4647 -0.0686 -0.0294 -0.0385 327 SER A C   
2525 O O   . SER A 328 ? 0.3746 0.4137 0.4700 -0.0655 -0.0221 -0.0303 327 SER A O   
2526 C CB  . SER A 328 ? 0.3256 0.3807 0.4320 -0.0927 -0.0518 -0.0205 327 SER A CB  
2527 O OG  . SER A 328 ? 0.3494 0.3743 0.4401 -0.1084 -0.0659 -0.0256 327 SER A OG  
2528 N N   . ASP A 329 ? 0.3539 0.3477 0.4090 -0.0641 -0.0266 -0.0501 328 ASP A N   
2529 C CA  . ASP A 329 ? 0.3493 0.3313 0.4023 -0.0566 -0.0160 -0.0522 328 ASP A CA  
2530 C C   . ASP A 329 ? 0.3655 0.3586 0.4206 -0.0426 -0.0053 -0.0524 328 ASP A C   
2531 O O   . ASP A 329 ? 0.3263 0.3325 0.3820 -0.0381 -0.0055 -0.0518 328 ASP A O   
2532 C CB  . ASP A 329 ? 0.3916 0.3378 0.4205 -0.0566 -0.0170 -0.0619 328 ASP A CB  
2533 C CG  . ASP A 329 ? 0.4175 0.3509 0.4237 -0.0479 -0.0147 -0.0707 328 ASP A CG  
2534 O OD1 . ASP A 329 ? 0.4122 0.3613 0.4197 -0.0469 -0.0171 -0.0698 328 ASP A OD1 
2535 O OD2 . ASP A 329 ? 0.4206 0.3282 0.4071 -0.0410 -0.0097 -0.0774 328 ASP A OD2 
2536 N N   . LEU A 330 ? 0.3841 0.3707 0.4404 -0.0368 0.0026  -0.0520 329 LEU A N   
2537 C CA  . LEU A 330 ? 0.3276 0.3220 0.3868 -0.0266 0.0099  -0.0502 329 LEU A CA  
2538 C C   . LEU A 330 ? 0.3485 0.3276 0.4028 -0.0219 0.0156  -0.0518 329 LEU A C   
2539 O O   . LEU A 330 ? 0.3481 0.3171 0.4037 -0.0251 0.0161  -0.0508 329 LEU A O   
2540 C CB  . LEU A 330 ? 0.2947 0.3067 0.3667 -0.0245 0.0121  -0.0425 329 LEU A CB  
2541 C CG  . LEU A 330 ? 0.2960 0.3095 0.3656 -0.0151 0.0166  -0.0409 329 LEU A CG  
2542 C CD1 . LEU A 330 ? 0.2608 0.2889 0.3341 -0.0100 0.0179  -0.0354 329 LEU A CD1 
2543 C CD2 . LEU A 330 ? 0.2813 0.2851 0.3509 -0.0137 0.0201  -0.0393 329 LEU A CD2 
2544 N N   . HIS A 331 ? 0.3410 0.3201 0.3914 -0.0145 0.0195  -0.0523 330 HIS A N   
2545 C CA  . HIS A 331 ? 0.3230 0.2938 0.3728 -0.0085 0.0254  -0.0508 330 HIS A CA  
2546 C C   . HIS A 331 ? 0.3447 0.3266 0.4033 -0.0051 0.0260  -0.0444 330 HIS A C   
2547 O O   . HIS A 331 ? 0.3161 0.3065 0.3749 -0.0053 0.0227  -0.0433 330 HIS A O   
2548 C CB  . HIS A 331 ? 0.3158 0.2774 0.3533 -0.0028 0.0294  -0.0544 330 HIS A CB  
2549 C CG  . HIS A 331 ? 0.3531 0.2954 0.3740 -0.0056 0.0269  -0.0622 330 HIS A CG  
2550 N ND1 . HIS A 331 ? 0.3922 0.3122 0.4009 -0.0007 0.0310  -0.0654 330 HIS A ND1 
2551 C CD2 . HIS A 331 ? 0.3788 0.3179 0.3916 -0.0134 0.0188  -0.0669 330 HIS A CD2 
2552 C CE1 . HIS A 331 ? 0.4020 0.3013 0.3917 -0.0059 0.0246  -0.0731 330 HIS A CE1 
2553 N NE2 . HIS A 331 ? 0.4265 0.3389 0.4200 -0.0148 0.0164  -0.0736 330 HIS A NE2 
2554 N N   . ILE A 332 ? 0.2976 0.2769 0.3617 -0.0023 0.0289  -0.0396 331 ILE A N   
2555 C CA  . ILE A 332 ? 0.3163 0.3030 0.3869 -0.0006 0.0267  -0.0326 331 ILE A CA  
2556 C C   . ILE A 332 ? 0.3326 0.3214 0.4095 0.0047  0.0313  -0.0266 331 ILE A C   
2557 O O   . ILE A 332 ? 0.3192 0.3013 0.3973 0.0088  0.0367  -0.0258 331 ILE A O   
2558 C CB  . ILE A 332 ? 0.3534 0.3392 0.4260 -0.0021 0.0240  -0.0293 331 ILE A CB  
2559 C CG1 . ILE A 332 ? 0.2707 0.2593 0.3375 -0.0040 0.0213  -0.0322 331 ILE A CG1 
2560 C CG2 . ILE A 332 ? 0.3117 0.3000 0.3883 -0.0013 0.0195  -0.0213 331 ILE A CG2 
2561 C CD1 . ILE A 332 ? 0.2715 0.2594 0.3376 -0.0040 0.0219  -0.0290 331 ILE A CD1 
2562 N N   . LEU A 333 ? 0.3541 0.3524 0.4355 0.0050  0.0294  -0.0209 332 LEU A N   
2563 C CA  . LEU A 333 ? 0.3257 0.3340 0.4190 0.0095  0.0332  -0.0100 332 LEU A CA  
2564 C C   . LEU A 333 ? 0.3145 0.3289 0.4183 0.0044  0.0239  -0.0002 332 LEU A C   
2565 O O   . LEU A 333 ? 0.2910 0.3031 0.3900 -0.0020 0.0142  -0.0003 332 LEU A O   
2566 C CB  . LEU A 333 ? 0.3020 0.3191 0.3951 0.0115  0.0362  -0.0069 332 LEU A CB  
2567 C CG  . LEU A 333 ? 0.2904 0.3248 0.3995 0.0168  0.0417  0.0083  332 LEU A CG  
2568 C CD1 . LEU A 333 ? 0.2526 0.2850 0.3614 0.0297  0.0551  0.0093  332 LEU A CD1 
2569 C CD2 . LEU A 333 ? 0.2672 0.3109 0.3753 0.0161  0.0427  0.0125  332 LEU A CD2 
2570 N N   . ASP A 334 ? 0.3304 0.3490 0.4455 0.0075  0.0257  0.0081  333 ASP A N   
2571 C CA  . ASP A 334 ? 0.3024 0.3252 0.4261 0.0019  0.0150  0.0182  333 ASP A CA  
2572 C C   . ASP A 334 ? 0.2986 0.3419 0.4439 0.0027  0.0147  0.0354  333 ASP A C   
2573 O O   . ASP A 334 ? 0.2973 0.3508 0.4549 0.0121  0.0252  0.0426  333 ASP A O   
2574 C CB  . ASP A 334 ? 0.3383 0.3535 0.4607 0.0042  0.0160  0.0174  333 ASP A CB  
2575 C CG  . ASP A 334 ? 0.3400 0.3547 0.4642 -0.0022 0.0028  0.0259  333 ASP A CG  
2576 O OD1 . ASP A 334 ? 0.2912 0.3144 0.4240 -0.0082 -0.0077 0.0366  333 ASP A OD1 
2577 O OD2 . ASP A 334 ? 0.3654 0.3698 0.4807 -0.0018 0.0018  0.0224  333 ASP A OD2 
2578 N N   . PHE A 335 ? 0.2906 0.3394 0.4406 -0.0069 0.0023  0.0436  334 PHE A N   
2579 C CA  . PHE A 335 ? 0.2758 0.3484 0.4508 -0.0091 -0.0001 0.0639  334 PHE A CA  
2580 C C   . PHE A 335 ? 0.2838 0.3678 0.4770 -0.0101 -0.0059 0.0786  334 PHE A C   
2581 O O   . PHE A 335 ? 0.3487 0.4594 0.5688 -0.0081 -0.0034 0.0982  334 PHE A O   
2582 C CB  . PHE A 335 ? 0.2457 0.3176 0.4200 -0.0220 -0.0149 0.0697  334 PHE A CB  
2583 C CG  . PHE A 335 ? 0.2735 0.3487 0.4435 -0.0192 -0.0066 0.0660  334 PHE A CG  
2584 C CD1 . PHE A 335 ? 0.3060 0.3609 0.4514 -0.0181 -0.0053 0.0475  334 PHE A CD1 
2585 C CD2 . PHE A 335 ? 0.2274 0.3283 0.4185 -0.0166 0.0009  0.0825  334 PHE A CD2 
2586 C CE1 . PHE A 335 ? 0.2834 0.3415 0.4240 -0.0156 0.0013  0.0447  334 PHE A CE1 
2587 C CE2 . PHE A 335 ? 0.2727 0.3761 0.4571 -0.0134 0.0090  0.0797  334 PHE A CE2 
2588 C CZ  . PHE A 335 ? 0.2571 0.3379 0.4155 -0.0134 0.0084  0.0602  334 PHE A CZ  
2589 N N   . SER A 336 ? 0.2928 0.3603 0.4737 -0.0125 -0.0133 0.0720  335 SER A N   
2590 C CA  . SER A 336 ? 0.2987 0.3758 0.4949 -0.0147 -0.0216 0.0866  335 SER A CA  
2591 C C   . SER A 336 ? 0.3048 0.3648 0.4862 -0.0091 -0.0179 0.0761  335 SER A C   
2592 O O   . SER A 336 ? 0.3542 0.3985 0.5199 -0.0161 -0.0310 0.0731  335 SER A O   
2593 C CB  . SER A 336 ? 0.2814 0.3555 0.4776 -0.0312 -0.0457 0.0968  335 SER A CB  
2594 O OG  . SER A 336 ? 0.4282 0.5203 0.6473 -0.0341 -0.0543 0.1165  335 SER A OG  
2595 N N   . PRO A 337 ? 0.2705 0.3312 0.4544 0.0039  -0.0005 0.0715  336 PRO A N   
2596 C CA  . PRO A 337 ? 0.2961 0.3382 0.4649 0.0077  0.0031  0.0614  336 PRO A CA  
2597 C C   . PRO A 337 ? 0.3010 0.3466 0.4777 0.0056  -0.0067 0.0738  336 PRO A C   
2598 O O   . PRO A 337 ? 0.2859 0.3512 0.4865 0.0099  -0.0062 0.0907  336 PRO A O   
2599 C CB  . PRO A 337 ? 0.2996 0.3395 0.4701 0.0214  0.0216  0.0563  336 PRO A CB  
2600 C CG  . PRO A 337 ? 0.3075 0.3607 0.4855 0.0252  0.0288  0.0588  336 PRO A CG  
2601 C CD  . PRO A 337 ? 0.2671 0.3420 0.4642 0.0163  0.0163  0.0756  336 PRO A CD  
2602 N N   . SER A 338 ? 0.3371 0.3647 0.4933 -0.0001 -0.0153 0.0667  337 SER A N   
2603 C CA  . SER A 338 ? 0.3028 0.3296 0.4606 -0.0016 -0.0244 0.0769  337 SER A CA  
2604 C C   . SER A 338 ? 0.3033 0.3321 0.4718 0.0101  -0.0109 0.0804  337 SER A C   
2605 O O   . SER A 338 ? 0.3020 0.3239 0.4677 0.0180  0.0041  0.0707  337 SER A O   
2606 C CB  . SER A 338 ? 0.3248 0.3292 0.4525 -0.0070 -0.0328 0.0672  337 SER A CB  
2607 O OG  . SER A 338 ? 0.2975 0.2902 0.4132 -0.0011 -0.0189 0.0547  337 SER A OG  
2608 N N   . LEU A 339 ? 0.2772 0.3124 0.4558 0.0109  -0.0179 0.0945  338 LEU A N   
2609 C CA  . LEU A 339 ? 0.2825 0.3148 0.4680 0.0226  -0.0062 0.0980  338 LEU A CA  
2610 C C   . LEU A 339 ? 0.3145 0.3216 0.4759 0.0227  0.0005  0.0828  338 LEU A C   
2611 O O   . LEU A 339 ? 0.2963 0.2932 0.4573 0.0312  0.0136  0.0777  338 LEU A O   
2612 C CB  . LEU A 339 ? 0.2913 0.3357 0.4917 0.0230  -0.0166 0.1172  338 LEU A CB  
2613 C CG  . LEU A 339 ? 0.3005 0.3402 0.5079 0.0363  -0.0054 0.1230  338 LEU A CG  
2614 C CD1 . LEU A 339 ? 0.2997 0.3461 0.5225 0.0524  0.0129  0.1243  338 LEU A CD1 
2615 C CD2 . LEU A 339 ? 0.3101 0.3616 0.5302 0.0354  -0.0181 0.1424  338 LEU A CD2 
2616 N N   . LYS A 340 ? 0.3349 0.3309 0.4749 0.0137  -0.0085 0.0760  339 LYS A N   
2617 C CA  . LYS A 340 ? 0.2956 0.2740 0.4170 0.0135  -0.0014 0.0652  339 LYS A CA  
2618 C C   . LYS A 340 ? 0.3144 0.2878 0.4346 0.0153  0.0105  0.0522  339 LYS A C   
2619 O O   . LYS A 340 ? 0.3429 0.3044 0.4597 0.0177  0.0190  0.0478  339 LYS A O   
2620 C CB  . LYS A 340 ? 0.3329 0.3028 0.4301 0.0067  -0.0107 0.0611  339 LYS A CB  
2621 C CG  . LYS A 340 ? 0.3769 0.3352 0.4585 0.0070  -0.0019 0.0534  339 LYS A CG  
2622 C CD  . LYS A 340 ? 0.4054 0.3555 0.4611 0.0050  -0.0088 0.0535  339 LYS A CD  
2623 C CE  . LYS A 340 ? 0.4016 0.3485 0.4413 0.0028  -0.0144 0.0447  339 LYS A CE  
2624 N NZ  . LYS A 340 ? 0.4506 0.3859 0.4603 0.0054  -0.0147 0.0424  339 LYS A NZ  
2625 N N   . THR A 341 ? 0.3048 0.2859 0.4271 0.0133  0.0096  0.0469  340 THR A N   
2626 C CA  . THR A 341 ? 0.3051 0.2816 0.4251 0.0151  0.0194  0.0354  340 THR A CA  
2627 C C   . THR A 341 ? 0.3366 0.3093 0.4662 0.0250  0.0300  0.0372  340 THR A C   
2628 O O   . THR A 341 ? 0.3411 0.2979 0.4619 0.0264  0.0370  0.0283  340 THR A O   
2629 C CB  . THR A 341 ? 0.2885 0.2746 0.4089 0.0116  0.0157  0.0317  340 THR A CB  
2630 O OG1 . THR A 341 ? 0.3539 0.3351 0.4582 0.0048  0.0079  0.0264  340 THR A OG1 
2631 C CG2 . THR A 341 ? 0.2821 0.2652 0.4011 0.0148  0.0253  0.0219  340 THR A CG2 
2632 N N   . LEU A 342 ? 0.2804 0.2660 0.4266 0.0325  0.0308  0.0495  341 LEU A N   
2633 C CA  . LEU A 342 ? 0.2930 0.2724 0.4443 0.0462  0.0430  0.0514  341 LEU A CA  
2634 C C   . LEU A 342 ? 0.3100 0.2677 0.4535 0.0495  0.0460  0.0507  341 LEU A C   
2635 O O   . LEU A 342 ? 0.3367 0.2745 0.4717 0.0582  0.0551  0.0452  341 LEU A O   
2636 C CB  . LEU A 342 ? 0.2919 0.2949 0.4663 0.0557  0.0447  0.0685  341 LEU A CB  
2637 C CG  . LEU A 342 ? 0.2777 0.3045 0.4641 0.0519  0.0415  0.0734  341 LEU A CG  
2638 C CD1 . LEU A 342 ? 0.2890 0.3435 0.5035 0.0600  0.0422  0.0952  341 LEU A CD1 
2639 C CD2 . LEU A 342 ? 0.2883 0.3077 0.4634 0.0570  0.0524  0.0613  341 LEU A CD2 
2640 N N   . CYS A 343 ? 0.3291 0.2875 0.4724 0.0428  0.0378  0.0568  342 CYS A N   
2641 C CA  . CYS A 343 ? 0.3264 0.2651 0.4635 0.0450  0.0401  0.0588  342 CYS A CA  
2642 C C   . CYS A 343 ? 0.3719 0.2908 0.4923 0.0360  0.0414  0.0463  342 CYS A C   
2643 O O   . CYS A 343 ? 0.3744 0.2699 0.4878 0.0388  0.0459  0.0440  342 CYS A O   
2644 C CB  . CYS A 343 ? 0.3299 0.2773 0.4717 0.0416  0.0310  0.0715  342 CYS A CB  
2645 S SG  . CYS A 343 ? 0.3587 0.3279 0.5250 0.0529  0.0288  0.0911  342 CYS A SG  
2646 N N   . LYS A 344 ? 0.3423 0.2694 0.4564 0.0254  0.0369  0.0396  343 LYS A N   
2647 C CA  . LYS A 344 ? 0.3745 0.2891 0.4778 0.0171  0.0383  0.0303  343 LYS A CA  
2648 C C   . LYS A 344 ? 0.4038 0.3019 0.5019 0.0205  0.0436  0.0207  343 LYS A C   
2649 O O   . LYS A 344 ? 0.4427 0.3186 0.5327 0.0169  0.0443  0.0174  343 LYS A O   
2650 C CB  . LYS A 344 ? 0.3251 0.2540 0.4237 0.0090  0.0344  0.0254  343 LYS A CB  
2651 C CG  . LYS A 344 ? 0.3497 0.2872 0.4441 0.0066  0.0294  0.0329  343 LYS A CG  
2652 C CD  . LYS A 344 ? 0.3181 0.2647 0.4030 0.0021  0.0275  0.0276  343 LYS A CD  
2653 C CE  . LYS A 344 ? 0.3205 0.2752 0.4053 0.0034  0.0235  0.0223  343 LYS A CE  
2654 N NZ  . LYS A 344 ? 0.3085 0.2672 0.3789 0.0018  0.0200  0.0192  343 LYS A NZ  
2655 N N   . LEU A 345 ? 0.3647 0.2712 0.4655 0.0276  0.0467  0.0174  344 LEU A N   
2656 C CA  . LEU A 345 ? 0.3864 0.2750 0.4765 0.0333  0.0523  0.0080  344 LEU A CA  
2657 C C   . LEU A 345 ? 0.4504 0.3119 0.5334 0.0439  0.0575  0.0101  344 LEU A C   
2658 O O   . LEU A 345 ? 0.5151 0.3469 0.5802 0.0439  0.0584  0.0009  344 LEU A O   
2659 C CB  . LEU A 345 ? 0.3788 0.2845 0.4740 0.0412  0.0564  0.0075  344 LEU A CB  
2660 C CG  . LEU A 345 ? 0.3906 0.3146 0.4871 0.0315  0.0513  0.0027  344 LEU A CG  
2661 C CD1 . LEU A 345 ? 0.3589 0.3024 0.4649 0.0390  0.0546  0.0075  344 LEU A CD1 
2662 C CD2 . LEU A 345 ? 0.3569 0.2658 0.4384 0.0242  0.0501  -0.0100 344 LEU A CD2 
2663 N N   . ALA A 346 ? 0.4243 0.2928 0.5191 0.0532  0.0597  0.0225  345 ALA A N   
2664 C CA  . ALA A 346 ? 0.4406 0.2814 0.5280 0.0654  0.0650  0.0257  345 ALA A CA  
2665 C C   . ALA A 346 ? 0.4959 0.3106 0.5730 0.0536  0.0590  0.0240  345 ALA A C   
2666 O O   . ALA A 346 ? 0.5499 0.3276 0.6087 0.0563  0.0599  0.0177  345 ALA A O   
2667 C CB  . ALA A 346 ? 0.4027 0.2622 0.5090 0.0780  0.0680  0.0421  345 ALA A CB  
2668 N N   . VAL A 347 ? 0.4633 0.2952 0.5499 0.0404  0.0523  0.0301  346 VAL A N   
2669 C CA  . VAL A 347 ? 0.4854 0.2986 0.5661 0.0286  0.0474  0.0324  346 VAL A CA  
2670 C C   . VAL A 347 ? 0.5183 0.3114 0.5856 0.0170  0.0438  0.0207  346 VAL A C   
2671 O O   . VAL A 347 ? 0.5249 0.2867 0.5816 0.0109  0.0401  0.0205  346 VAL A O   
2672 C CB  . VAL A 347 ? 0.4379 0.2770 0.5289 0.0187  0.0430  0.0416  346 VAL A CB  
2673 C CG1 . VAL A 347 ? 0.4462 0.2725 0.5335 0.0053  0.0394  0.0457  346 VAL A CG1 
2674 C CG2 . VAL A 347 ? 0.4345 0.2856 0.5349 0.0283  0.0431  0.0543  346 VAL A CG2 
2675 N N   . ILE A 348 ? 0.4754 0.2850 0.5425 0.0129  0.0433  0.0119  347 ILE A N   
2676 C CA  . ILE A 348 ? 0.5122 0.3050 0.5672 0.0018  0.0382  0.0018  347 ILE A CA  
2677 C C   . ILE A 348 ? 0.5693 0.3224 0.6021 0.0115  0.0399  -0.0075 347 ILE A C   
2678 O O   . ILE A 348 ? 0.5894 0.3077 0.6064 0.0027  0.0328  -0.0116 347 ILE A O   
2679 C CB  . ILE A 348 ? 0.4853 0.3063 0.5454 -0.0031 0.0374  -0.0044 347 ILE A CB  
2680 C CG1 . ILE A 348 ? 0.3706 0.2224 0.4454 -0.0122 0.0354  0.0037  347 ILE A CG1 
2681 C CG2 . ILE A 348 ? 0.4558 0.2583 0.5019 -0.0122 0.0316  -0.0150 347 ILE A CG2 
2682 C CD1 . ILE A 348 ? 0.3451 0.2252 0.4251 -0.0094 0.0368  0.0004  347 ILE A CD1 
2683 N N   . GLN A 349 ? 0.5739 0.3305 0.6038 0.0301  0.0489  -0.0099 348 GLN A N   
2684 C CA  . GLN A 349 ? 0.5964 0.3160 0.6004 0.0441  0.0535  -0.0193 348 GLN A CA  
2685 C C   . GLN A 349 ? 0.5892 0.2650 0.5774 0.0498  0.0526  -0.0171 348 GLN A C   
2686 O O   . GLN A 349 ? 0.6154 0.2454 0.5745 0.0481  0.0474  -0.0271 348 GLN A O   
2687 C CB  . GLN A 349 ? 0.5908 0.3308 0.6002 0.0650  0.0660  -0.0172 348 GLN A CB  
2688 C CG  . GLN A 349 ? 0.6600 0.3644 0.6413 0.0859  0.0750  -0.0244 348 GLN A CG  
2689 C CD  . GLN A 349 ? 0.7243 0.4560 0.7199 0.1088  0.0896  -0.0145 348 GLN A CD  
2690 O OE1 . GLN A 349 ? 0.7088 0.4850 0.7354 0.1056  0.0899  -0.0030 348 GLN A OE1 
2691 N NE2 . GLN A 349 ? 0.7595 0.4639 0.7317 0.1323  0.1013  -0.0178 348 GLN A NE2 
2692 N N   . TYR A 350 ? 0.5946 0.2803 0.5990 0.0562  0.0560  -0.0040 349 TYR A N   
2693 C CA  . TYR A 350 ? 0.6074 0.2512 0.5978 0.0624  0.0552  -0.0003 349 TYR A CA  
2694 C C   . TYR A 350 ? 0.6296 0.2553 0.6184 0.0387  0.0420  0.0022  349 TYR A C   
2695 O O   . TYR A 350 ? 0.6593 0.2467 0.6360 0.0399  0.0387  0.0062  349 TYR A O   
2696 C CB  . TYR A 350 ? 0.6053 0.2678 0.6148 0.0784  0.0631  0.0149  349 TYR A CB  
2697 C CG  . TYR A 350 ? 0.6516 0.3373 0.6690 0.1017  0.0761  0.0177  349 TYR A CG  
2698 C CD1 . TYR A 350 ? 0.6686 0.3277 0.6615 0.1208  0.0853  0.0082  349 TYR A CD1 
2699 C CD2 . TYR A 350 ? 0.6002 0.3349 0.6488 0.1045  0.0787  0.0314  349 TYR A CD2 
2700 C CE1 . TYR A 350 ? 0.6877 0.3739 0.6913 0.1429  0.0990  0.0143  349 TYR A CE1 
2701 C CE2 . TYR A 350 ? 0.5815 0.3423 0.6425 0.1235  0.0893  0.0378  349 TYR A CE2 
2702 C CZ  . TYR A 350 ? 0.6731 0.4125 0.7139 0.1430  0.1005  0.0303  349 TYR A CZ  
2703 O OH  . TYR A 350 ? 0.6876 0.4585 0.7443 0.1623  0.1126  0.0401  349 TYR A OH  
2704 N N   . ASN A 351 ? 0.7204 0.3741 0.7226 0.0180  0.0348  0.0019  350 ASN A N   
2705 C CA  . ASN A 351 ? 0.7193 0.3647 0.7249 -0.0059 0.0229  0.0072  350 ASN A CA  
2706 C C   . ASN A 351 ? 0.6631 0.3112 0.6819 -0.0081 0.0230  0.0234  350 ASN A C   
2707 O O   . ASN A 351 ? 0.6717 0.2923 0.6854 -0.0216 0.0144  0.0294  350 ASN A O   
2708 C CB  . ASN A 351 ? 0.7489 0.3408 0.7255 -0.0148 0.0119  -0.0028 350 ASN A CB  
2709 C CG  . ASN A 351 ? 0.8767 0.4757 0.8620 -0.0433 -0.0021 0.0008  350 ASN A CG  
2710 O OD1 . ASN A 351 ? 0.9370 0.5020 0.9141 -0.0585 -0.0139 0.0058  350 ASN A OD1 
2711 N ND2 . ASN A 351 ? 0.8904 0.5346 0.8937 -0.0508 -0.0011 0.0003  350 ASN A ND2 
2712 N N   . LEU A 352 ? 0.5944 0.2760 0.6304 0.0036  0.0313  0.0318  351 LEU A N   
2713 C CA  . LEU A 352 ? 0.5776 0.2621 0.6239 0.0035  0.0315  0.0475  351 LEU A CA  
2714 C C   . LEU A 352 ? 0.5680 0.2763 0.6280 -0.0171 0.0262  0.0578  351 LEU A C   
2715 O O   . LEU A 352 ? 0.5228 0.2593 0.5904 -0.0269 0.0252  0.0544  351 LEU A O   
2716 C CB  . LEU A 352 ? 0.5913 0.3049 0.6506 0.0210  0.0394  0.0542  351 LEU A CB  
2717 C CG  . LEU A 352 ? 0.6049 0.3046 0.6561 0.0437  0.0472  0.0482  351 LEU A CG  
2718 C CD1 . LEU A 352 ? 0.5207 0.2614 0.5912 0.0556  0.0525  0.0558  351 LEU A CD1 
2719 C CD2 . LEU A 352 ? 0.5848 0.2402 0.6219 0.0552  0.0484  0.0524  351 LEU A CD2 
2720 N N   . ASP A 353 ? 0.5506 0.2477 0.6135 -0.0221 0.0239  0.0720  352 ASP A N   
2721 C CA  . ASP A 353 ? 0.5342 0.2567 0.6106 -0.0380 0.0219  0.0859  352 ASP A CA  
2722 C C   . ASP A 353 ? 0.5237 0.2921 0.6106 -0.0317 0.0282  0.0889  352 ASP A C   
2723 O O   . ASP A 353 ? 0.5529 0.3289 0.6403 -0.0172 0.0318  0.0913  352 ASP A O   
2724 C CB  . ASP A 353 ? 0.5637 0.2641 0.6393 -0.0408 0.0195  0.1019  352 ASP A CB  
2725 C CG  . ASP A 353 ? 0.6258 0.3487 0.7141 -0.0580 0.0180  0.1190  352 ASP A CG  
2726 O OD1 . ASP A 353 ? 0.5999 0.3601 0.6978 -0.0642 0.0209  0.1196  352 ASP A OD1 
2727 O OD2 . ASP A 353 ? 0.7104 0.4131 0.7984 -0.0641 0.0148  0.1333  352 ASP A OD2 
2728 N N   . GLN A 354 ? 0.5027 0.3003 0.5970 -0.0425 0.0285  0.0899  353 GLN A N   
2729 C CA  . GLN A 354 ? 0.4751 0.3096 0.5729 -0.0362 0.0335  0.0909  353 GLN A CA  
2730 C C   . GLN A 354 ? 0.4930 0.3462 0.5934 -0.0397 0.0364  0.1078  353 GLN A C   
2731 O O   . GLN A 354 ? 0.5207 0.3986 0.6175 -0.0332 0.0400  0.1087  353 GLN A O   
2732 C CB  . GLN A 354 ? 0.4478 0.3026 0.5483 -0.0409 0.0339  0.0806  353 GLN A CB  
2733 C CG  . GLN A 354 ? 0.4709 0.3117 0.5662 -0.0362 0.0321  0.0639  353 GLN A CG  
2734 C CD  . GLN A 354 ? 0.4605 0.3198 0.5588 -0.0425 0.0313  0.0557  353 GLN A CD  
2735 O OE1 . GLN A 354 ? 0.4524 0.3394 0.5566 -0.0460 0.0339  0.0615  353 GLN A OE1 
2736 N NE2 . GLN A 354 ? 0.4733 0.3164 0.5654 -0.0426 0.0283  0.0426  353 GLN A NE2 
2737 N N   . SER A 355 ? 0.5343 0.3743 0.6383 -0.0494 0.0348  0.1217  354 SER A N   
2738 C CA  . SER A 355 ? 0.5446 0.4058 0.6513 -0.0533 0.0393  0.1398  354 SER A CA  
2739 C C   . SER A 355 ? 0.5997 0.4632 0.6967 -0.0407 0.0415  0.1473  354 SER A C   
2740 O O   . SER A 355 ? 0.6050 0.4864 0.6982 -0.0406 0.0462  0.1612  354 SER A O   
2741 C CB  . SER A 355 ? 0.5463 0.3941 0.6623 -0.0699 0.0360  0.1551  354 SER A CB  
2742 O OG  . SER A 355 ? 0.5846 0.3932 0.6953 -0.0689 0.0301  0.1558  354 SER A OG  
2743 N N   . CYS A 356 ? 0.5810 0.4274 0.6737 -0.0296 0.0381  0.1404  355 CYS A N   
2744 C CA  . CYS A 356 ? 0.5934 0.4457 0.6783 -0.0181 0.0376  0.1473  355 CYS A CA  
2745 C C   . CYS A 356 ? 0.5715 0.4476 0.6479 -0.0109 0.0377  0.1394  355 CYS A C   
2746 O O   . CYS A 356 ? 0.5766 0.4601 0.6422 -0.0043 0.0355  0.1464  355 CYS A O   
2747 C CB  . CYS A 356 ? 0.7357 0.5656 0.8230 -0.0079 0.0338  0.1455  355 CYS A CB  
2748 S SG  . CYS A 356 ? 0.7956 0.6334 0.8865 0.0048  0.0323  0.1282  355 CYS A SG  
2749 N N   . LEU A 357 ? 0.5374 0.4222 0.6165 -0.0124 0.0385  0.1251  356 LEU A N   
2750 C CA  . LEU A 357 ? 0.4939 0.3936 0.5647 -0.0053 0.0362  0.1162  356 LEU A CA  
2751 C C   . LEU A 357 ? 0.4901 0.4068 0.5453 -0.0047 0.0396  0.1206  356 LEU A C   
2752 O O   . LEU A 357 ? 0.4948 0.4190 0.5516 -0.0105 0.0463  0.1282  356 LEU A O   
2753 C CB  . LEU A 357 ? 0.4359 0.3372 0.5138 -0.0062 0.0361  0.1002  356 LEU A CB  
2754 C CG  . LEU A 357 ? 0.4632 0.3464 0.5509 -0.0026 0.0345  0.0950  356 LEU A CG  
2755 C CD1 . LEU A 357 ? 0.4009 0.2840 0.4921 -0.0047 0.0357  0.0803  356 LEU A CD1 
2756 C CD2 . LEU A 357 ? 0.4186 0.3041 0.5080 0.0082  0.0302  0.0985  356 LEU A CD2 
2757 N N   . PRO A 358 ? 0.5068 0.4287 0.5455 0.0025  0.0348  0.1175  357 PRO A N   
2758 C CA  . PRO A 358 ? 0.4986 0.4307 0.5148 0.0065  0.0385  0.1192  357 PRO A CA  
2759 C C   . PRO A 358 ? 0.4897 0.4340 0.5095 0.0047  0.0452  0.1101  357 PRO A C   
2760 O O   . PRO A 358 ? 0.4547 0.3988 0.4889 0.0012  0.0432  0.0988  357 PRO A O   
2761 C CB  . PRO A 358 ? 0.4736 0.4002 0.4697 0.0131  0.0274  0.1149  357 PRO A CB  
2762 C CG  . PRO A 358 ? 0.4165 0.3397 0.4325 0.0112  0.0199  0.1082  357 PRO A CG  
2763 C CD  . PRO A 358 ? 0.4158 0.3332 0.4542 0.0077  0.0247  0.1140  357 PRO A CD  
2764 N N   . HIS A 359 ? 0.5174 0.4735 0.5235 0.0086  0.0540  0.1164  358 HIS A N   
2765 C CA  . HIS A 359 ? 0.4447 0.4169 0.4590 0.0074  0.0619  0.1123  358 HIS A CA  
2766 C C   . HIS A 359 ? 0.4471 0.4177 0.4533 0.0120  0.0573  0.0955  358 HIS A C   
2767 O O   . HIS A 359 ? 0.4620 0.4432 0.4825 0.0085  0.0606  0.0897  358 HIS A O   
2768 C CB  . HIS A 359 ? 0.4833 0.4716 0.4843 0.0143  0.0744  0.1254  358 HIS A CB  
2769 C CG  . HIS A 359 ? 0.5413 0.5382 0.5591 0.0062  0.0808  0.1445  358 HIS A CG  
2770 N ND1 . HIS A 359 ? 0.6052 0.5972 0.6083 0.0100  0.0829  0.1585  358 HIS A ND1 
2771 C CD2 . HIS A 359 ? 0.5181 0.5259 0.5660 -0.0073 0.0834  0.1529  358 HIS A CD2 
2772 C CE1 . HIS A 359 ? 0.5910 0.5917 0.6156 -0.0004 0.0879  0.1754  358 HIS A CE1 
2773 N NE2 . HIS A 359 ? 0.5886 0.5982 0.6407 -0.0118 0.0874  0.1724  358 HIS A NE2 
2774 N N   . ASP A 360 ? 0.4948 0.4520 0.4789 0.0185  0.0483  0.0887  359 ASP A N   
2775 C CA  . ASP A 360 ? 0.4491 0.4027 0.4269 0.0209  0.0422  0.0741  359 ASP A CA  
2776 C C   . ASP A 360 ? 0.4409 0.3950 0.4465 0.0124  0.0376  0.0662  359 ASP A C   
2777 O O   . ASP A 360 ? 0.4606 0.4204 0.4729 0.0113  0.0388  0.0569  359 ASP A O   
2778 C CB  . ASP A 360 ? 0.4896 0.4261 0.4370 0.0269  0.0303  0.0706  359 ASP A CB  
2779 C CG  . ASP A 360 ? 0.5149 0.4428 0.4673 0.0228  0.0197  0.0774  359 ASP A CG  
2780 O OD1 . ASP A 360 ? 0.5024 0.4350 0.4788 0.0177  0.0231  0.0847  359 ASP A OD1 
2781 O OD2 . ASP A 360 ? 0.5069 0.4218 0.4382 0.0247  0.0067  0.0761  359 ASP A OD2 
2782 N N   . ILE A 361 ? 0.4030 0.3504 0.4229 0.0081  0.0332  0.0704  360 ILE A N   
2783 C CA  . ILE A 361 ? 0.4020 0.3474 0.4443 0.0032  0.0314  0.0639  360 ILE A CA  
2784 C C   . ILE A 361 ? 0.3987 0.3489 0.4558 -0.0034 0.0388  0.0626  360 ILE A C   
2785 O O   . ILE A 361 ? 0.3803 0.3315 0.4465 -0.0061 0.0384  0.0529  360 ILE A O   
2786 C CB  . ILE A 361 ? 0.3992 0.3353 0.4514 0.0036  0.0271  0.0708  360 ILE A CB  
2787 C CG1 . ILE A 361 ? 0.4980 0.4330 0.5420 0.0078  0.0165  0.0727  360 ILE A CG1 
2788 C CG2 . ILE A 361 ? 0.3430 0.2737 0.4138 0.0020  0.0284  0.0651  360 ILE A CG2 
2789 C CD1 . ILE A 361 ? 0.4801 0.4106 0.5378 0.0099  0.0127  0.0820  360 ILE A CD1 
2790 N N   . ARG A 362 ? 0.3763 0.3296 0.4361 -0.0071 0.0444  0.0737  361 ARG A N   
2791 C CA  . ARG A 362 ? 0.4015 0.3593 0.4772 -0.0166 0.0482  0.0753  361 ARG A CA  
2792 C C   . ARG A 362 ? 0.3584 0.3330 0.4347 -0.0163 0.0514  0.0692  361 ARG A C   
2793 O O   . ARG A 362 ? 0.3282 0.3038 0.4170 -0.0236 0.0498  0.0634  361 ARG A O   
2794 C CB  . ARG A 362 ? 0.4421 0.4033 0.5224 -0.0220 0.0529  0.0921  361 ARG A CB  
2795 C CG  . ARG A 362 ? 0.4560 0.3988 0.5356 -0.0220 0.0496  0.0995  361 ARG A CG  
2796 C CD  . ARG A 362 ? 0.4236 0.3683 0.5102 -0.0298 0.0534  0.1168  361 ARG A CD  
2797 N NE  . ARG A 362 ? 0.4269 0.3689 0.5308 -0.0436 0.0516  0.1175  361 ARG A NE  
2798 C CZ  . ARG A 362 ? 0.4793 0.4243 0.5947 -0.0552 0.0528  0.1336  361 ARG A CZ  
2799 N NH1 . ARG A 362 ? 0.4698 0.4239 0.5819 -0.0533 0.0585  0.1509  361 ARG A NH1 
2800 N NH2 . ARG A 362 ? 0.5081 0.4459 0.6379 -0.0699 0.0471  0.1335  361 ARG A NH2 
2801 N N   . TRP A 363 ? 0.3741 0.3596 0.4343 -0.0070 0.0554  0.0704  362 TRP A N   
2802 C CA  . TRP A 363 ? 0.3814 0.3812 0.4403 -0.0035 0.0587  0.0645  362 TRP A CA  
2803 C C   . TRP A 363 ? 0.3941 0.3862 0.4565 -0.0052 0.0517  0.0492  362 TRP A C   
2804 O O   . TRP A 363 ? 0.4074 0.4085 0.4811 -0.0096 0.0523  0.0450  362 TRP A O   
2805 C CB  . TRP A 363 ? 0.4025 0.4059 0.4351 0.0105  0.0633  0.0658  362 TRP A CB  
2806 C CG  . TRP A 363 ? 0.4293 0.4454 0.4579 0.0174  0.0679  0.0607  362 TRP A CG  
2807 C CD1 . TRP A 363 ? 0.3890 0.4282 0.4233 0.0219  0.0790  0.0709  362 TRP A CD1 
2808 C CD2 . TRP A 363 ? 0.4503 0.4580 0.4698 0.0213  0.0617  0.0462  362 TRP A CD2 
2809 N NE1 . TRP A 363 ? 0.4638 0.5085 0.4922 0.0299  0.0803  0.0629  362 TRP A NE1 
2810 C CE2 . TRP A 363 ? 0.4181 0.4419 0.4363 0.0290  0.0694  0.0473  362 TRP A CE2 
2811 C CE3 . TRP A 363 ? 0.4438 0.4339 0.4579 0.0191  0.0507  0.0347  362 TRP A CE3 
2812 C CZ2 . TRP A 363 ? 0.4114 0.4302 0.4204 0.0345  0.0658  0.0358  362 TRP A CZ2 
2813 C CZ3 . TRP A 363 ? 0.4296 0.4164 0.4360 0.0230  0.0468  0.0242  362 TRP A CZ3 
2814 C CH2 . TRP A 363 ? 0.4378 0.4368 0.4403 0.0306  0.0541  0.0241  362 TRP A CH2 
2815 N N   . GLU A 364 ? 0.3715 0.3490 0.4259 -0.0021 0.0449  0.0429  363 GLU A N   
2816 C CA  . GLU A 364 ? 0.3563 0.3287 0.4152 -0.0031 0.0393  0.0313  363 GLU A CA  
2817 C C   . GLU A 364 ? 0.3714 0.3392 0.4474 -0.0110 0.0393  0.0283  363 GLU A C   
2818 O O   . GLU A 364 ? 0.3938 0.3647 0.4745 -0.0136 0.0386  0.0205  363 GLU A O   
2819 C CB  . GLU A 364 ? 0.3873 0.3494 0.4390 0.0008  0.0319  0.0301  363 GLU A CB  
2820 C CG  . GLU A 364 ? 0.4028 0.3617 0.4312 0.0073  0.0275  0.0309  363 GLU A CG  
2821 C CD  . GLU A 364 ? 0.4539 0.4041 0.4780 0.0077  0.0162  0.0314  363 GLU A CD  
2822 O OE1 . GLU A 364 ? 0.3858 0.3379 0.4269 0.0049  0.0135  0.0294  363 GLU A OE1 
2823 O OE2 . GLU A 364 ? 0.4934 0.4350 0.4960 0.0110  0.0095  0.0348  363 GLU A OE2 
2824 N N   . LEU A 365 ? 0.3561 0.3128 0.4381 -0.0143 0.0393  0.0343  364 LEU A N   
2825 C CA  . LEU A 365 ? 0.3525 0.2964 0.4435 -0.0210 0.0382  0.0309  364 LEU A CA  
2826 C C   . LEU A 365 ? 0.3688 0.3215 0.4665 -0.0302 0.0384  0.0306  364 LEU A C   
2827 O O   . LEU A 365 ? 0.3467 0.2926 0.4461 -0.0344 0.0352  0.0221  364 LEU A O   
2828 C CB  . LEU A 365 ? 0.3715 0.2993 0.4650 -0.0231 0.0381  0.0394  364 LEU A CB  
2829 C CG  . LEU A 365 ? 0.3749 0.2918 0.4662 -0.0140 0.0370  0.0399  364 LEU A CG  
2830 C CD1 . LEU A 365 ? 0.3498 0.2558 0.4419 -0.0148 0.0374  0.0518  364 LEU A CD1 
2831 C CD2 . LEU A 365 ? 0.3674 0.2693 0.4595 -0.0104 0.0368  0.0305  364 LEU A CD2 
2832 N N   . ASN A 366 ? 0.3724 0.3420 0.4739 -0.0329 0.0421  0.0412  365 ASN A N   
2833 C CA  . ASN A 366 ? 0.3594 0.3441 0.4724 -0.0419 0.0420  0.0451  365 ASN A CA  
2834 C C   . ASN A 366 ? 0.3542 0.3507 0.4653 -0.0379 0.0416  0.0352  365 ASN A C   
2835 O O   . ASN A 366 ? 0.3135 0.3113 0.4322 -0.0461 0.0369  0.0315  365 ASN A O   
2836 C CB  . ASN A 366 ? 0.3452 0.3518 0.4641 -0.0422 0.0489  0.0616  365 ASN A CB  
2837 C CG  . ASN A 366 ? 0.3981 0.4293 0.5332 -0.0495 0.0497  0.0688  365 ASN A CG  
2838 O OD1 . ASN A 366 ? 0.3800 0.4313 0.5129 -0.0406 0.0549  0.0680  365 ASN A OD1 
2839 N ND2 . ASN A 366 ? 0.4114 0.4394 0.5623 -0.0662 0.0431  0.0762  365 ASN A ND2 
2840 N N   . ALA A 367 ? 0.3446 0.3471 0.4436 -0.0258 0.0448  0.0312  366 ALA A N   
2841 C CA  . ALA A 367 ? 0.3523 0.3637 0.4476 -0.0210 0.0443  0.0229  366 ALA A CA  
2842 C C   . ALA A 367 ? 0.3483 0.3475 0.4458 -0.0258 0.0382  0.0114  366 ALA A C   
2843 O O   . ALA A 367 ? 0.3823 0.3893 0.4851 -0.0300 0.0358  0.0081  366 ALA A O   
2844 C CB  . ALA A 367 ? 0.3370 0.3459 0.4140 -0.0084 0.0456  0.0192  366 ALA A CB  
2845 N N   . MET A 368 ? 0.3844 0.3649 0.4771 -0.0243 0.0359  0.0064  367 MET A N   
2846 C CA  . MET A 368 ? 0.3611 0.3302 0.4519 -0.0250 0.0326  -0.0039 367 MET A CA  
2847 C C   . MET A 368 ? 0.3493 0.3046 0.4429 -0.0348 0.0289  -0.0056 367 MET A C   
2848 O O   . MET A 368 ? 0.3474 0.2889 0.4341 -0.0342 0.0266  -0.0146 367 MET A O   
2849 C CB  . MET A 368 ? 0.3287 0.2870 0.4148 -0.0173 0.0330  -0.0063 367 MET A CB  
2850 C CG  . MET A 368 ? 0.3772 0.3212 0.4648 -0.0169 0.0340  -0.0008 367 MET A CG  
2851 S SD  . MET A 368 ? 0.4039 0.3476 0.4911 -0.0071 0.0341  0.0038  367 MET A SD  
2852 C CE  . MET A 368 ? 0.3666 0.3054 0.4546 -0.0010 0.0356  -0.0037 367 MET A CE  
2853 N N   . THR A 369 ? 0.3298 0.2867 0.4313 -0.0441 0.0275  0.0035  368 THR A N   
2854 C CA  . THR A 369 ? 0.3673 0.3052 0.4688 -0.0561 0.0205  0.0026  368 THR A CA  
2855 C C   . THR A 369 ? 0.3792 0.3348 0.4943 -0.0696 0.0153  0.0112  368 THR A C   
2856 O O   . THR A 369 ? 0.3742 0.3139 0.4911 -0.0834 0.0067  0.0144  368 THR A O   
2857 C CB  . THR A 369 ? 0.4112 0.3257 0.5100 -0.0579 0.0202  0.0077  368 THR A CB  
2858 O OG1 . THR A 369 ? 0.4207 0.3522 0.5308 -0.0606 0.0237  0.0222  368 THR A OG1 
2859 C CG2 . THR A 369 ? 0.3581 0.2575 0.4467 -0.0437 0.0250  0.0016  368 THR A CG2 
2860 N N   . THR A 370 ? 0.3319 0.3189 0.4565 -0.0661 0.0195  0.0162  369 THR A N   
2861 C CA  . THR A 370 ? 0.3734 0.3855 0.5163 -0.0769 0.0166  0.0288  369 THR A CA  
2862 C C   . THR A 370 ? 0.3777 0.4063 0.5224 -0.0747 0.0143  0.0233  369 THR A C   
2863 O O   . THR A 370 ? 0.3183 0.3567 0.4562 -0.0606 0.0212  0.0181  369 THR A O   
2864 C CB  . THR A 370 ? 0.3588 0.3980 0.5131 -0.0717 0.0266  0.0449  369 THR A CB  
2865 O OG1 . THR A 370 ? 0.3811 0.4038 0.5294 -0.0701 0.0298  0.0484  369 THR A OG1 
2866 C CG2 . THR A 370 ? 0.3011 0.3667 0.4795 -0.0851 0.0237  0.0629  369 THR A CG2 
2867 N N   . ASN A 371 ? 0.3471 0.3765 0.4997 -0.0893 0.0030  0.0253  370 ASN A N   
2868 C CA  . ASN A 371 ? 0.3219 0.3673 0.4771 -0.0885 -0.0008 0.0217  370 ASN A CA  
2869 C C   . ASN A 371 ? 0.3498 0.4369 0.5239 -0.0812 0.0075  0.0359  370 ASN A C   
2870 O O   . ASN A 371 ? 0.3311 0.4382 0.5209 -0.0826 0.0134  0.0520  370 ASN A O   
2871 C CB  . ASN A 371 ? 0.3619 0.3974 0.5202 -0.1078 -0.0175 0.0225  370 ASN A CB  
2872 C CG  . ASN A 371 ? 0.4071 0.3980 0.5381 -0.1099 -0.0251 0.0051  370 ASN A CG  
2873 O OD1 . ASN A 371 ? 0.3857 0.3600 0.4998 -0.0957 -0.0166 -0.0065 370 ASN A OD1 
2874 N ND2 . ASN A 371 ? 0.3717 0.3422 0.4970 -0.1274 -0.0416 0.0043  370 ASN A ND2 
2875 N N   . SER A 372 ? 0.3230 0.4230 0.4946 -0.0720 0.0089  0.0307  371 SER A N   
2876 C CA  . SER A 372 ? 0.3275 0.4662 0.5166 -0.0643 0.0157  0.0446  371 SER A CA  
2877 C C   . SER A 372 ? 0.3198 0.4812 0.5334 -0.0813 0.0040  0.0578  371 SER A C   
2878 O O   . SER A 372 ? 0.2790 0.4206 0.4910 -0.0996 -0.0109 0.0540  371 SER A O   
2879 C CB  . SER A 372 ? 0.3185 0.4582 0.4930 -0.0464 0.0216  0.0346  371 SER A CB  
2880 O OG  . SER A 372 ? 0.2689 0.3882 0.4220 -0.0332 0.0296  0.0249  371 SER A OG  
2881 N N   . ASN A 373 ? 0.3080 0.5106 0.5436 -0.0749 0.0101  0.0747  372 ASN A N   
2882 C CA  . ASN A 373 ? 0.3049 0.5369 0.5699 -0.0917 -0.0017 0.0920  372 ASN A CA  
2883 C C   . ASN A 373 ? 0.2698 0.5282 0.5428 -0.0819 -0.0017 0.0948  372 ASN A C   
2884 O O   . ASN A 373 ? 0.3238 0.6240 0.6279 -0.0858 -0.0032 0.1163  372 ASN A O   
2885 C CB  . ASN A 373 ? 0.3415 0.6084 0.6371 -0.0977 0.0040  0.1186  372 ASN A CB  
2886 C CG  . ASN A 373 ? 0.4867 0.7738 0.8137 -0.1256 -0.0154 0.1372  372 ASN A CG  
2887 O OD1 . ASN A 373 ? 0.4909 0.7482 0.8070 -0.1442 -0.0353 0.1258  372 ASN A OD1 
2888 N ND2 . ASN A 373 ? 0.4146 0.7515 0.7788 -0.1281 -0.0100 0.1668  372 ASN A ND2 
2889 N N   . ILE A 374 ? 0.3093 0.5453 0.5565 -0.0693 -0.0002 0.0752  373 ILE A N   
2890 C CA  . ILE A 374 ? 0.2952 0.5482 0.5470 -0.0638 -0.0046 0.0759  373 ILE A CA  
2891 C C   . ILE A 374 ? 0.2514 0.5035 0.5129 -0.0878 -0.0264 0.0781  373 ILE A C   
2892 O O   . ILE A 374 ? 0.2743 0.5595 0.5588 -0.0917 -0.0334 0.0927  373 ILE A O   
2893 C CB  . ILE A 374 ? 0.3095 0.5343 0.5296 -0.0472 0.0005  0.0548  373 ILE A CB  
2894 C CG1 . ILE A 374 ? 0.2782 0.4974 0.4841 -0.0260 0.0183  0.0521  373 ILE A CG1 
2895 C CG2 . ILE A 374 ? 0.2315 0.4730 0.4557 -0.0408 -0.0040 0.0566  373 ILE A CG2 
2896 C CD1 . ILE A 374 ? 0.2695 0.5282 0.4944 -0.0103 0.0320  0.0724  373 ILE A CD1 
2897 N N   . SER A 375 ? 0.3176 0.5301 0.5596 -0.1033 -0.0381 0.0641  374 SER A N   
2898 C CA  . SER A 375 ? 0.3581 0.5567 0.5971 -0.1250 -0.0606 0.0617  374 SER A CA  
2899 C C   . SER A 375 ? 0.4266 0.5983 0.6622 -0.1461 -0.0721 0.0621  374 SER A C   
2900 O O   . SER A 375 ? 0.4247 0.5802 0.6534 -0.1418 -0.0619 0.0587  374 SER A O   
2901 C CB  . SER A 375 ? 0.3952 0.5601 0.6001 -0.1194 -0.0650 0.0393  374 SER A CB  
2902 O OG  . SER A 375 ? 0.3877 0.5167 0.5650 -0.1091 -0.0544 0.0214  374 SER A OG  
2903 N N   . ARG A 376 ? 0.4941 0.6598 0.7335 -0.1693 -0.0950 0.0672  375 ARG A N   
2904 C CA  . ARG A 376 ? 0.5360 0.6659 0.7649 -0.1926 -0.1126 0.0657  375 ARG A CA  
2905 C C   . ARG A 376 ? 0.6143 0.6948 0.8017 -0.1981 -0.1281 0.0436  375 ARG A C   
2906 O O   . ARG A 376 ? 0.6074 0.6939 0.7852 -0.1902 -0.1297 0.0366  375 ARG A O   
2907 C CB  . ARG A 376 ? 0.5459 0.7087 0.8131 -0.2178 -0.1300 0.0932  375 ARG A CB  
2908 C CG  . ARG A 376 ? 0.5277 0.7417 0.8369 -0.2127 -0.1136 0.1189  375 ARG A CG  
2909 C CD  . ARG A 376 ? 0.6230 0.8979 0.9739 -0.2153 -0.1166 0.1462  375 ARG A CD  
2910 N NE  . ARG A 376 ? 0.6484 0.9579 1.0074 -0.1903 -0.0999 0.1460  375 ARG A NE  
2911 C CZ  . ARG A 376 ? 0.5616 0.8883 0.9217 -0.1631 -0.0729 0.1462  375 ARG A CZ  
2912 N NH1 . ARG A 376 ? 0.4831 0.8014 0.8408 -0.1587 -0.0594 0.1476  375 ARG A NH1 
2913 N NH2 . ARG A 376 ? 0.4627 0.8120 0.8231 -0.1397 -0.0601 0.1447  375 ARG A NH2 
2914 N N   . PRO A 377 ? 0.6760 0.7049 0.8349 -0.2095 -0.1388 0.0322  376 PRO A N   
2915 C CA  . PRO A 377 ? 0.7190 0.6971 0.8324 -0.2121 -0.1525 0.0111  376 PRO A CA  
2916 C C   . PRO A 377 ? 0.7573 0.7432 0.8742 -0.2324 -0.1785 0.0189  376 PRO A C   
2917 O O   . PRO A 377 ? 0.7434 0.7613 0.8958 -0.2522 -0.1922 0.0414  376 PRO A O   
2918 C CB  . PRO A 377 ? 0.7148 0.6378 0.8010 -0.2212 -0.1596 0.0023  376 PRO A CB  
2919 C CG  . PRO A 377 ? 0.7155 0.6608 0.8300 -0.2158 -0.1425 0.0142  376 PRO A CG  
2920 C CD  . PRO A 377 ? 0.6508 0.6624 0.8143 -0.2184 -0.1380 0.0380  376 PRO A CD  
2921 N N   . ILE A 378 ? 0.8105 0.7694 0.8911 -0.2270 -0.1852 0.0019  377 ILE A N   
2922 C CA  . ILE A 378 ? 0.8458 0.8055 0.9224 -0.2462 -0.2123 0.0074  377 ILE A CA  
2923 C C   . ILE A 378 ? 0.8628 0.7685 0.9041 -0.2589 -0.2296 0.0012  377 ILE A C   
2924 O O   . ILE A 378 ? 0.9295 0.8421 0.9781 -0.2744 -0.2482 0.0142  377 ILE A O   
2925 C CB  . ILE A 378 ? 0.9122 0.8674 0.9618 -0.2306 -0.2090 -0.0068 377 ILE A CB  
2926 C CG1 . ILE A 378 ? 1.0595 0.9478 1.0477 -0.2213 -0.2082 -0.0333 377 ILE A CG1 
2927 C CG2 . ILE A 378 ? 0.8095 0.8089 0.8835 -0.2046 -0.1806 -0.0042 377 ILE A CG2 
2928 C CD1 . ILE A 378 ? 1.0953 0.9463 1.0430 -0.2323 -0.2320 -0.0411 377 ILE A CD1 
2929 N N   . MET B 1   ? 0.9497 1.3088 1.0543 -0.1438 0.1364  0.4366  1   MET B N   
2930 C CA  . MET B 1   ? 0.9225 1.1994 1.1000 -0.1501 0.1261  0.4555  1   MET B CA  
2931 C C   . MET B 1   ? 0.8457 1.0789 1.0807 -0.1286 0.1102  0.3944  1   MET B C   
2932 O O   . MET B 1   ? 0.8177 1.0554 1.0974 -0.1380 0.1256  0.3559  1   MET B O   
2933 C CB  . MET B 1   ? 1.0322 1.2491 1.2026 -0.1400 0.0951  0.5115  1   MET B CB  
2934 C CG  . MET B 1   ? 1.1625 1.3717 1.3172 -0.1648 0.1061  0.5599  1   MET B CG  
2935 S SD  . MET B 1   ? 1.2451 1.4079 1.4889 -0.1916 0.1235  0.5503  1   MET B SD  
2936 C CE  . MET B 1   ? 1.0650 1.1439 1.3914 -0.1618 0.0828  0.5297  1   MET B CE  
2937 N N   . ASP B 2   ? 0.7445 0.9386 0.9764 -0.0986 0.0779  0.3812  2   ASP B N   
2938 C CA  . ASP B 2   ? 0.6445 0.7998 0.9200 -0.0778 0.0618  0.3244  2   ASP B CA  
2939 C C   . ASP B 2   ? 0.5755 0.7707 0.8134 -0.0628 0.0658  0.2677  2   ASP B C   
2940 O O   . ASP B 2   ? 0.6132 0.8449 0.7976 -0.0535 0.0627  0.2680  2   ASP B O   
2941 C CB  . ASP B 2   ? 0.6532 0.7510 0.9530 -0.0552 0.0267  0.3337  2   ASP B CB  
2942 C CG  . ASP B 2   ? 0.7454 0.7866 1.1113 -0.0654 0.0160  0.3721  2   ASP B CG  
2943 O OD1 . ASP B 2   ? 0.7402 0.7861 1.1284 -0.0937 0.0385  0.4002  2   ASP B OD1 
2944 O OD2 . ASP B 2   ? 0.7602 0.7545 1.1623 -0.0456 -0.0149 0.3707  2   ASP B OD2 
2945 N N   . VAL B 3   ? 0.5376 0.7235 0.8072 -0.0595 0.0699  0.2187  3   VAL B N   
2946 C CA  . VAL B 3   ? 0.4785 0.6836 0.7238 -0.0445 0.0687  0.1664  3   VAL B CA  
2947 C C   . VAL B 3   ? 0.4070 0.5606 0.6759 -0.0248 0.0465  0.1396  3   VAL B C   
2948 O O   . VAL B 3   ? 0.3871 0.5028 0.7048 -0.0244 0.0391  0.1361  3   VAL B O   
2949 C CB  . VAL B 3   ? 0.4181 0.6574 0.6752 -0.0544 0.0883  0.1311  3   VAL B CB  
2950 C CG1 . VAL B 3   ? 0.4532 0.7642 0.6762 -0.0710 0.1115  0.1436  3   VAL B CG1 
2951 C CG2 . VAL B 3   ? 0.4031 0.6154 0.7200 -0.0647 0.0922  0.1296  3   VAL B CG2 
2952 N N   . PHE B 4   ? 0.4004 0.5580 0.6375 -0.0098 0.0369  0.1182  4   PHE B N   
2953 C CA  . PHE B 4   ? 0.3269 0.4474 0.5785 0.0057  0.0202  0.0913  4   PHE B CA  
2954 C C   . PHE B 4   ? 0.3494 0.4733 0.5871 0.0094  0.0256  0.0496  4   PHE B C   
2955 O O   . PHE B 4   ? 0.3034 0.4585 0.5105 0.0077  0.0342  0.0366  4   PHE B O   
2956 C CB  . PHE B 4   ? 0.3125 0.4327 0.5472 0.0176  0.0051  0.0991  4   PHE B CB  
2957 C CG  . PHE B 4   ? 0.3202 0.4262 0.5744 0.0177  -0.0073 0.1422  4   PHE B CG  
2958 C CD1 . PHE B 4   ? 0.3615 0.4959 0.5872 0.0087  -0.0010 0.1829  4   PHE B CD1 
2959 C CD2 . PHE B 4   ? 0.3239 0.3887 0.6276 0.0262  -0.0262 0.1428  4   PHE B CD2 
2960 C CE1 . PHE B 4   ? 0.4119 0.5249 0.6534 0.0079  -0.0148 0.2314  4   PHE B CE1 
2961 C CE2 . PHE B 4   ? 0.3688 0.4113 0.7002 0.0269  -0.0418 0.1843  4   PHE B CE2 
2962 C CZ  . PHE B 4   ? 0.4164 0.4782 0.7146 0.0173  -0.0368 0.2331  4   PHE B CZ  
2963 N N   . LEU B 5   ? 0.3180 0.4100 0.5806 0.0152  0.0182  0.0286  5   LEU B N   
2964 C CA  . LEU B 5   ? 0.3288 0.4158 0.5850 0.0182  0.0201  -0.0027 5   LEU B CA  
2965 C C   . LEU B 5   ? 0.3407 0.3989 0.5865 0.0294  0.0081  -0.0240 5   LEU B C   
2966 O O   . LEU B 5   ? 0.3186 0.3624 0.5781 0.0352  -0.0017 -0.0226 5   LEU B O   
2967 C CB  . LEU B 5   ? 0.2950 0.3786 0.5897 0.0143  0.0225  -0.0091 5   LEU B CB  
2968 C CG  . LEU B 5   ? 0.2952 0.4132 0.6032 -0.0021 0.0395  0.0113  5   LEU B CG  
2969 C CD1 . LEU B 5   ? 0.2228 0.3383 0.5806 -0.0075 0.0423  -0.0003 5   LEU B CD1 
2970 C CD2 . LEU B 5   ? 0.3041 0.4630 0.5778 -0.0055 0.0511  -0.0008 5   LEU B CD2 
2971 N N   . MET B 6   ? 0.3177 0.3697 0.5410 0.0318  0.0086  -0.0445 6   MET B N   
2972 C CA  . MET B 6   ? 0.3077 0.3313 0.5160 0.0396  -0.0012 -0.0613 6   MET B CA  
2973 C C   . MET B 6   ? 0.3068 0.3184 0.5229 0.0452  -0.0074 -0.0766 6   MET B C   
2974 O O   . MET B 6   ? 0.3114 0.3307 0.5211 0.0431  -0.0038 -0.0842 6   MET B O   
2975 C CB  . MET B 6   ? 0.3262 0.3468 0.4973 0.0360  0.0030  -0.0661 6   MET B CB  
2976 C CG  . MET B 6   ? 0.3309 0.3648 0.4971 0.0335  0.0058  -0.0608 6   MET B CG  
2977 S SD  . MET B 6   ? 0.3668 0.3979 0.4979 0.0248  0.0139  -0.0726 6   MET B SD  
2978 C CE  . MET B 6   ? 0.2813 0.3269 0.4114 0.0206  0.0199  -0.0764 6   MET B CE  
2979 N N   . ILE B 7   ? 0.2941 0.2915 0.5302 0.0543  -0.0193 -0.0861 7   ILE B N   
2980 C CA  . ILE B 7   ? 0.3126 0.2980 0.5572 0.0647  -0.0315 -0.1051 7   ILE B CA  
2981 C C   . ILE B 7   ? 0.3362 0.2942 0.5352 0.0727  -0.0439 -0.1095 7   ILE B C   
2982 O O   . ILE B 7   ? 0.3595 0.3138 0.5474 0.0764  -0.0483 -0.1104 7   ILE B O   
2983 C CB  . ILE B 7   ? 0.2862 0.2810 0.5666 0.0633  -0.0378 -0.1097 7   ILE B CB  
2984 C CG1 . ILE B 7   ? 0.2673 0.2827 0.6019 0.0550  -0.0226 -0.0988 7   ILE B CG1 
2985 C CG2 . ILE B 7   ? 0.2788 0.2744 0.5592 0.0673  -0.0504 -0.1259 7   ILE B CG2 
2986 C CD1 . ILE B 7   ? 0.2509 0.2686 0.6306 0.0493  -0.0273 -0.1016 7   ILE B CD1 
2987 N N   . ARG B 8   ? 0.3499 0.2899 0.5263 0.0757  -0.0500 -0.1132 8   ARG B N   
2988 C CA  . ARG B 8   ? 0.3954 0.3022 0.5241 0.0788  -0.0580 -0.1080 8   ARG B CA  
2989 C C   . ARG B 8   ? 0.4225 0.3040 0.5394 0.0928  -0.0805 -0.1145 8   ARG B C   
2990 O O   . ARG B 8   ? 0.4206 0.3115 0.5577 0.0925  -0.0845 -0.1205 8   ARG B O   
2991 C CB  . ARG B 8   ? 0.3702 0.2727 0.4788 0.0640  -0.0441 -0.0976 8   ARG B CB  
2992 C CG  . ARG B 8   ? 0.3640 0.2994 0.4825 0.0512  -0.0246 -0.0907 8   ARG B CG  
2993 C CD  . ARG B 8   ? 0.3494 0.2832 0.4463 0.0377  -0.0127 -0.0857 8   ARG B CD  
2994 N NE  . ARG B 8   ? 0.3729 0.2771 0.4312 0.0329  -0.0145 -0.0784 8   ARG B NE  
2995 C CZ  . ARG B 8   ? 0.3991 0.2809 0.4380 0.0214  -0.0100 -0.0734 8   ARG B CZ  
2996 N NH1 . ARG B 8   ? 0.3695 0.2595 0.4292 0.0156  -0.0046 -0.0817 8   ARG B NH1 
2997 N NH2 . ARG B 8   ? 0.4284 0.2809 0.4280 0.0147  -0.0110 -0.0605 8   ARG B NH2 
2998 N N   . ARG B 9   ? 0.4256 0.2832 0.5059 0.1037  -0.0953 -0.1121 9   ARG B N   
2999 C CA  . ARG B 9   ? 0.4300 0.2547 0.4873 0.1218  -0.1229 -0.1142 9   ARG B CA  
3000 C C   . ARG B 9   ? 0.4751 0.2737 0.4636 0.1166  -0.1246 -0.0903 9   ARG B C   
3001 O O   . ARG B 9   ? 0.5104 0.3329 0.4800 0.1118  -0.1150 -0.0897 9   ARG B O   
3002 C CB  . ARG B 9   ? 0.4268 0.2849 0.5097 0.1320  -0.1363 -0.1304 9   ARG B CB  
3003 C CG  . ARG B 9   ? 0.4676 0.2992 0.5262 0.1529  -0.1690 -0.1349 9   ARG B CG  
3004 C CD  . ARG B 9   ? 0.4480 0.3100 0.5204 0.1657  -0.1843 -0.1555 9   ARG B CD  
3005 N NE  . ARG B 9   ? 0.5182 0.3518 0.5567 0.1913  -0.2205 -0.1609 9   ARG B NE  
3006 C CZ  . ARG B 9   ? 0.5688 0.3747 0.5481 0.2185  -0.2441 -0.1567 9   ARG B CZ  
3007 N NH1 . ARG B 9   ? 0.5665 0.3899 0.5125 0.2070  -0.2250 -0.1464 9   ARG B NH1 
3008 N NH2 . ARG B 9   ? 0.6328 0.4138 0.5782 0.2416  -0.2793 -0.1561 9   ARG B NH2 
3009 N N   . HIS B 10  ? 0.3134 0.3669 0.5499 0.0447  -0.0401 0.0478  10  HIS B N   
3010 C CA  . HIS B 10  ? 0.3322 0.4068 0.5786 0.0525  -0.0373 0.0684  10  HIS B CA  
3011 C C   . HIS B 10  ? 0.3833 0.4758 0.6292 0.0505  -0.0388 0.0774  10  HIS B C   
3012 O O   . HIS B 10  ? 0.3629 0.4476 0.6156 0.0349  -0.0409 0.0757  10  HIS B O   
3013 C CB  . HIS B 10  ? 0.3401 0.4359 0.5792 0.0746  -0.0368 0.0715  10  HIS B CB  
3014 C CG  . HIS B 10  ? 0.4060 0.4932 0.6484 0.0796  -0.0356 0.0654  10  HIS B CG  
3015 N ND1 . HIS B 10  ? 0.4025 0.5128 0.6400 0.1010  -0.0361 0.0680  10  HIS B ND1 
3016 C CD2 . HIS B 10  ? 0.3845 0.4477 0.6337 0.0690  -0.0346 0.0556  10  HIS B CD2 
3017 C CE1 . HIS B 10  ? 0.3733 0.4738 0.6161 0.1023  -0.0355 0.0612  10  HIS B CE1 
3018 N NE2 . HIS B 10  ? 0.3452 0.4167 0.5953 0.0833  -0.0341 0.0537  10  HIS B NE2 
3019 N N   . LYS B 11  ? 0.3589 0.4794 0.5959 0.0687  -0.0390 0.0847  11  LYS B N   
3020 C CA  . LYS B 11  ? 0.3642 0.5081 0.5996 0.0715  -0.0403 0.0927  11  LYS B CA  
3021 C C   . LYS B 11  ? 0.3984 0.5371 0.6119 0.0830  -0.0473 0.0758  11  LYS B C   
3022 O O   . LYS B 11  ? 0.3844 0.5477 0.5913 0.0964  -0.0492 0.0806  11  LYS B O   
3023 C CB  . LYS B 11  ? 0.3685 0.5540 0.6109 0.0860  -0.0340 0.1162  11  LYS B CB  
3024 C CG  . LYS B 11  ? 0.3671 0.5587 0.6410 0.0707  -0.0267 0.1412  11  LYS B CG  
3025 C CD  . LYS B 11  ? 0.3723 0.6040 0.6453 0.0826  -0.0167 0.1661  11  LYS B CD  
3026 C CE  . LYS B 11  ? 0.3607 0.6167 0.6754 0.0651  -0.0127 0.1944  11  LYS B CE  
3027 N NZ  . LYS B 11  ? 0.3456 0.6441 0.6533 0.0773  0.0003  0.2205  11  LYS B NZ  
3028 N N   . THR B 12  ? 0.3499 0.4576 0.5547 0.0783  -0.0509 0.0576  12  THR B N   
3029 C CA  . THR B 12  ? 0.3509 0.4432 0.5412 0.0843  -0.0575 0.0441  12  THR B CA  
3030 C C   . THR B 12  ? 0.3565 0.4276 0.5446 0.0668  -0.0572 0.0425  12  THR B C   
3031 O O   . THR B 12  ? 0.3509 0.4093 0.5453 0.0512  -0.0535 0.0404  12  THR B O   
3032 C CB  . THR B 12  ? 0.3760 0.4520 0.5638 0.0903  -0.0619 0.0272  12  THR B CB  
3033 O OG1 . THR B 12  ? 0.4631 0.5650 0.6497 0.1106  -0.0637 0.0262  12  THR B OG1 
3034 C CG2 . THR B 12  ? 0.3355 0.3893 0.5149 0.0946  -0.0695 0.0154  12  THR B CG2 
3035 N N   . THR B 13  ? 0.3607 0.4309 0.5379 0.0730  -0.0613 0.0433  13  THR B N   
3036 C CA  . THR B 13  ? 0.3280 0.3840 0.4984 0.0619  -0.0612 0.0441  13  THR B CA  
3037 C C   . THR B 13  ? 0.3780 0.4139 0.5360 0.0731  -0.0659 0.0413  13  THR B C   
3038 O O   . THR B 13  ? 0.3413 0.3877 0.4924 0.0905  -0.0710 0.0432  13  THR B O   
3039 C CB  . THR B 13  ? 0.3118 0.3934 0.4852 0.0580  -0.0621 0.0530  13  THR B CB  
3040 O OG1 . THR B 13  ? 0.2897 0.3816 0.4810 0.0443  -0.0591 0.0552  13  THR B OG1 
3041 C CG2 . THR B 13  ? 0.2715 0.3461 0.4326 0.0528  -0.0639 0.0529  13  THR B CG2 
3042 N N   . ILE B 14  ? 0.3400 0.3479 0.4973 0.0638  -0.0639 0.0381  14  ILE B N   
3043 C CA  . ILE B 14  ? 0.3723 0.3541 0.5230 0.0705  -0.0675 0.0402  14  ILE B CA  
3044 C C   . ILE B 14  ? 0.3783 0.3603 0.5162 0.0668  -0.0641 0.0538  14  ILE B C   
3045 O O   . ILE B 14  ? 0.3627 0.3505 0.4993 0.0531  -0.0575 0.0569  14  ILE B O   
3046 C CB  . ILE B 14  ? 0.3441 0.2979 0.5078 0.0614  -0.0669 0.0332  14  ILE B CB  
3047 C CG1 . ILE B 14  ? 0.3791 0.3375 0.5534 0.0696  -0.0735 0.0163  14  ILE B CG1 
3048 C CG2 . ILE B 14  ? 0.3464 0.2670 0.5094 0.0646  -0.0700 0.0400  14  ILE B CG2 
3049 C CD1 . ILE B 14  ? 0.3443 0.2913 0.5370 0.0558  -0.0721 0.0073  14  ILE B CD1 
3050 N N   . PHE B 15  ? 0.3446 0.3229 0.4713 0.0826  -0.0692 0.0608  15  PHE B N   
3051 C CA  . PHE B 15  ? 0.3761 0.3531 0.4881 0.0845  -0.0670 0.0758  15  PHE B CA  
3052 C C   . PHE B 15  ? 0.4526 0.3887 0.5663 0.0844  -0.0651 0.0855  15  PHE B C   
3053 O O   . PHE B 15  ? 0.4548 0.3641 0.5732 0.0970  -0.0725 0.0817  15  PHE B O   
3054 C CB  . PHE B 15  ? 0.3499 0.3491 0.4500 0.1041  -0.0738 0.0807  15  PHE B CB  
3055 C CG  . PHE B 15  ? 0.3615 0.4053 0.4649 0.0997  -0.0748 0.0771  15  PHE B CG  
3056 C CD1 . PHE B 15  ? 0.3312 0.3943 0.4487 0.0995  -0.0761 0.0691  15  PHE B CD1 
3057 C CD2 . PHE B 15  ? 0.3722 0.4407 0.4671 0.0955  -0.0750 0.0822  15  PHE B CD2 
3058 C CE1 . PHE B 15  ? 0.2988 0.4002 0.4270 0.0918  -0.0765 0.0693  15  PHE B CE1 
3059 C CE2 . PHE B 15  ? 0.3343 0.4417 0.4400 0.0881  -0.0784 0.0764  15  PHE B CE2 
3060 C CZ  . PHE B 15  ? 0.2927 0.4140 0.4176 0.0844  -0.0786 0.0715  15  PHE B CZ  
3061 N N   . THR B 16  ? 0.4153 0.3476 0.5266 0.0714  -0.0556 0.0983  16  THR B N   
3062 C CA  . THR B 16  ? 0.4763 0.3723 0.5938 0.0692  -0.0516 0.1150  16  THR B CA  
3063 C C   . THR B 16  ? 0.4884 0.3989 0.5918 0.0642  -0.0398 0.1374  16  THR B C   
3064 O O   . THR B 16  ? 0.4660 0.4125 0.5579 0.0598  -0.0356 0.1327  16  THR B O   
3065 C CB  . THR B 16  ? 0.5076 0.3783 0.6531 0.0537  -0.0511 0.1048  16  THR B CB  
3066 O OG1 . THR B 16  ? 0.5286 0.3576 0.6879 0.0519  -0.0507 0.1204  16  THR B OG1 
3067 C CG2 . THR B 16  ? 0.4295 0.3226 0.5819 0.0345  -0.0400 0.1033  16  THR B CG2 
3068 N N   . ASP B 17  ? 0.4791 0.3614 0.5840 0.0668  -0.0350 0.1622  17  ASP B N   
3069 C CA  . ASP B 17  ? 0.5483 0.4455 0.6404 0.0644  -0.0213 0.1900  17  ASP B CA  
3070 C C   . ASP B 17  ? 0.5516 0.4272 0.6706 0.0445  -0.0095 0.2053  17  ASP B C   
3071 O O   . ASP B 17  ? 0.5456 0.3853 0.6948 0.0341  -0.0148 0.1961  17  ASP B O   
3072 C CB  . ASP B 17  ? 0.5354 0.4245 0.6067 0.0858  -0.0223 0.2164  17  ASP B CB  
3073 C CG  . ASP B 17  ? 0.6068 0.4420 0.6942 0.0944  -0.0314 0.2203  17  ASP B CG  
3074 O OD1 . ASP B 17  ? 0.7225 0.5525 0.8114 0.1047  -0.0453 0.1952  17  ASP B OD1 
3075 O OD2 . ASP B 17  ? 0.6284 0.4269 0.7286 0.0915  -0.0249 0.2481  17  ASP B OD2 
3076 N N   . ALA B 18  ? 0.5944 0.4979 0.7033 0.0404  0.0061  0.2282  18  ALA B N   
3077 C CA  . ALA B 18  ? 0.6012 0.4959 0.7364 0.0220  0.0211  0.2512  18  ALA B CA  
3078 C C   . ALA B 18  ? 0.6524 0.5829 0.7634 0.0300  0.0383  0.2863  18  ALA B C   
3079 O O   . ALA B 18  ? 0.6875 0.6526 0.7610 0.0492  0.0363  0.2846  18  ALA B O   
3080 C CB  . ALA B 18  ? 0.5071 0.4179 0.6650 0.0027  0.0234  0.2268  18  ALA B CB  
3081 N N   . LYS B 19  ? 0.6567 0.5830 0.7913 0.0158  0.0550  0.3188  19  LYS B N   
3082 C CA  . LYS B 19  ? 0.6899 0.6597 0.8028 0.0241  0.0750  0.3558  19  LYS B CA  
3083 C C   . LYS B 19  ? 0.6747 0.7041 0.7749 0.0220  0.0832  0.3362  19  LYS B C   
3084 O O   . LYS B 19  ? 0.6215 0.6504 0.7456 0.0057  0.0800  0.3078  19  LYS B O   
3085 C CB  . LYS B 19  ? 0.6970 0.6444 0.8450 0.0085  0.0922  0.4036  19  LYS B CB  
3086 C CG  . LYS B 19  ? 0.7672 0.6512 0.9315 0.0083  0.0803  0.4065  19  LYS B CG  
3087 C CD  . LYS B 19  ? 0.8475 0.7332 0.9686 0.0381  0.0755  0.4189  19  LYS B CD  
3088 C CE  . LYS B 19  ? 0.7946 0.6236 0.9292 0.0391  0.0699  0.4318  19  LYS B CE  
3089 N NZ  . LYS B 19  ? 0.8874 0.7107 0.9828 0.0694  0.0585  0.4310  19  LYS B NZ  
3090 N N   . GLU B 20  ? 0.7028 0.7854 0.7640 0.0416  0.0933  0.3507  20  GLU B N   
3091 C CA  . GLU B 20  ? 0.6488 0.7891 0.6984 0.0429  0.1029  0.3353  20  GLU B CA  
3092 C C   . GLU B 20  ? 0.6304 0.7761 0.7207 0.0203  0.1209  0.3540  20  GLU B C   
3093 O O   . GLU B 20  ? 0.5723 0.7454 0.6711 0.0137  0.1229  0.3276  20  GLU B O   
3094 C CB  . GLU B 20  ? 0.6504 0.8512 0.6525 0.0705  0.1124  0.3529  20  GLU B CB  
3095 C CG  . GLU B 20  ? 0.7008 0.9178 0.6626 0.0933  0.0927  0.3226  20  GLU B CG  
3096 C CD  . GLU B 20  ? 0.7242 1.0143 0.6410 0.1200  0.0989  0.3225  20  GLU B CD  
3097 O OE1 . GLU B 20  ? 0.7486 1.0791 0.6647 0.1197  0.1115  0.3172  20  GLU B OE1 
3098 O OE2 . GLU B 20  ? 0.7179 1.0294 0.5996 0.1438  0.0905  0.3263  20  GLU B OE2 
3099 N N   . SER B 21  ? 0.6473 0.7661 0.7671 0.0077  0.1332  0.3992  21  SER B N   
3100 C CA  . SER B 21  ? 0.6398 0.7702 0.8046 -0.0159 0.1522  0.4252  21  SER B CA  
3101 C C   . SER B 21  ? 0.6431 0.7267 0.8616 -0.0447 0.1402  0.4003  21  SER B C   
3102 O O   . SER B 21  ? 0.6179 0.7137 0.8783 -0.0659 0.1512  0.4110  21  SER B O   
3103 C CB  . SER B 21  ? 0.6982 0.8186 0.8736 -0.0164 0.1633  0.4683  21  SER B CB  
3104 O OG  . SER B 21  ? 0.7181 0.7642 0.9195 -0.0273 0.1479  0.4668  21  SER B OG  
3105 N N   . SER B 22  ? 0.6290 0.6647 0.8461 -0.0435 0.1160  0.3634  22  SER B N   
3106 C CA  . SER B 22  ? 0.6157 0.6133 0.8788 -0.0658 0.1026  0.3362  22  SER B CA  
3107 C C   . SER B 22  ? 0.5518 0.5865 0.8142 -0.0678 0.0995  0.2963  22  SER B C   
3108 O O   . SER B 22  ? 0.5423 0.6167 0.7654 -0.0500 0.1012  0.2802  22  SER B O   
3109 C CB  . SER B 22  ? 0.6284 0.5656 0.8887 -0.0594 0.0789  0.3144  22  SER B CB  
3110 O OG  . SER B 22  ? 0.5366 0.4861 0.7544 -0.0388 0.0660  0.2821  22  SER B OG  
3111 N N   . THR B 23  ? 0.5230 0.5437 0.8308 -0.0886 0.0935  0.2792  23  THR B N   
3112 C CA  . THR B 23  ? 0.5159 0.5771 0.8307 -0.0914 0.0951  0.2513  23  THR B CA  
3113 C C   . THR B 23  ? 0.5110 0.5524 0.8140 -0.0832 0.0733  0.2048  23  THR B C   
3114 O O   . THR B 23  ? 0.4902 0.4864 0.7928 -0.0807 0.0563  0.1926  23  THR B O   
3115 C CB  . THR B 23  ? 0.4915 0.5641 0.8653 -0.1180 0.1033  0.2621  23  THR B CB  
3116 O OG1 . THR B 23  ? 0.5253 0.5450 0.9372 -0.1333 0.0840  0.2457  23  THR B OG1 
3117 C CG2 . THR B 23  ? 0.5166 0.6096 0.9083 -0.1285 0.1271  0.3155  23  THR B CG2 
3118 N N   . VAL B 24  ? 0.5026 0.5809 0.7960 -0.0767 0.0747  0.1806  24  VAL B N   
3119 C CA  . VAL B 24  ? 0.4647 0.5300 0.7509 -0.0692 0.0571  0.1416  24  VAL B CA  
3120 C C   . VAL B 24  ? 0.4288 0.4642 0.7549 -0.0833 0.0436  0.1280  24  VAL B C   
3121 O O   . VAL B 24  ? 0.4246 0.4320 0.7434 -0.0759 0.0264  0.1060  24  VAL B O   
3122 C CB  . VAL B 24  ? 0.4428 0.5511 0.7193 -0.0605 0.0628  0.1225  24  VAL B CB  
3123 C CG1 . VAL B 24  ? 0.4379 0.5325 0.7142 -0.0542 0.0465  0.0882  24  VAL B CG1 
3124 C CG2 . VAL B 24  ? 0.3879 0.5238 0.6219 -0.0427 0.0711  0.1270  24  VAL B CG2 
3125 N N   . PHE B 25  ? 0.4246 0.4692 0.7950 -0.1032 0.0506  0.1410  25  PHE B N   
3126 C CA  . PHE B 25  ? 0.4398 0.4570 0.8527 -0.1176 0.0351  0.1255  25  PHE B CA  
3127 C C   . PHE B 25  ? 0.4699 0.4308 0.8816 -0.1163 0.0214  0.1286  25  PHE B C   
3128 O O   . PHE B 25  ? 0.4443 0.3794 0.8607 -0.1108 0.0015  0.1004  25  PHE B O   
3129 C CB  . PHE B 25  ? 0.3898 0.4307 0.8569 -0.1426 0.0459  0.1422  25  PHE B CB  
3130 C CG  . PHE B 25  ? 0.4428 0.4657 0.9552 -0.1568 0.0272  0.1179  25  PHE B CG  
3131 C CD1 . PHE B 25  ? 0.3631 0.4145 0.8888 -0.1535 0.0176  0.0857  25  PHE B CD1 
3132 C CD2 . PHE B 25  ? 0.4675 0.4470 0.9954 -0.1663 0.0174  0.1225  25  PHE B CD2 
3133 C CE1 . PHE B 25  ? 0.3759 0.4163 0.9268 -0.1591 -0.0014 0.0593  25  PHE B CE1 
3134 C CE2 . PHE B 25  ? 0.4538 0.4202 1.0105 -0.1733 -0.0019 0.0939  25  PHE B CE2 
3135 C CZ  . PHE B 25  ? 0.4234 0.4221 0.9905 -0.1695 -0.0114 0.0623  25  PHE B CZ  
3136 N N   . GLU B 26  ? 0.4699 0.4137 0.8733 -0.1178 0.0318  0.1628  26  GLU B N   
3137 C CA  . GLU B 26  ? 0.4733 0.3629 0.8702 -0.1109 0.0185  0.1655  26  GLU B CA  
3138 C C   . GLU B 26  ? 0.4826 0.3656 0.8357 -0.0862 0.0047  0.1388  26  GLU B C   
3139 O O   . GLU B 26  ? 0.4708 0.3183 0.8257 -0.0781 -0.0133 0.1204  26  GLU B O   
3140 C CB  . GLU B 26  ? 0.5010 0.3793 0.8880 -0.1107 0.0337  0.2102  26  GLU B CB  
3141 C CG  . GLU B 26  ? 0.5609 0.4445 0.9832 -0.1312 0.0460  0.2360  26  GLU B CG  
3142 C CD  . GLU B 26  ? 0.6799 0.5617 1.0823 -0.1251 0.0624  0.2808  26  GLU B CD  
3143 O OE1 . GLU B 26  ? 0.7655 0.6233 1.1339 -0.1060 0.0578  0.2882  26  GLU B OE1 
3144 O OE2 . GLU B 26  ? 0.7545 0.6624 1.1742 -0.1374 0.0797  0.3090  26  GLU B OE2 
3145 N N   . LEU B 27  ? 0.4634 0.3829 0.7798 -0.0737 0.0125  0.1353  27  LEU B N   
3146 C CA  . LEU B 27  ? 0.4575 0.3757 0.7405 -0.0543 0.0005  0.1122  27  LEU B CA  
3147 C C   . LEU B 27  ? 0.4706 0.3861 0.7699 -0.0533 -0.0142 0.0797  27  LEU B C   
3148 O O   . LEU B 27  ? 0.4952 0.3937 0.7829 -0.0396 -0.0284 0.0635  27  LEU B O   
3149 C CB  . LEU B 27  ? 0.4480 0.4041 0.6976 -0.0447 0.0101  0.1124  27  LEU B CB  
3150 C CG  . LEU B 27  ? 0.4379 0.3911 0.6527 -0.0270 0.0015  0.1043  27  LEU B CG  
3151 C CD1 . LEU B 27  ? 0.4809 0.4125 0.6831 -0.0201 0.0013  0.1271  27  LEU B CD1 
3152 C CD2 . LEU B 27  ? 0.3863 0.3747 0.5763 -0.0203 0.0077  0.0982  27  LEU B CD2 
3153 N N   . LYS B 28  ? 0.4488 0.3868 0.7749 -0.0653 -0.0108 0.0707  28  LYS B N   
3154 C CA  . LYS B 28  ? 0.4292 0.3711 0.7701 -0.0618 -0.0250 0.0407  28  LYS B CA  
3155 C C   . LYS B 28  ? 0.4333 0.3401 0.7974 -0.0631 -0.0424 0.0281  28  LYS B C   
3156 O O   . LYS B 28  ? 0.4409 0.3461 0.7998 -0.0490 -0.0577 0.0027  28  LYS B O   
3157 C CB  . LYS B 28  ? 0.3864 0.3632 0.7545 -0.0733 -0.0183 0.0346  28  LYS B CB  
3158 C CG  . LYS B 28  ? 0.3543 0.3651 0.6984 -0.0641 -0.0076 0.0332  28  LYS B CG  
3159 C CD  . LYS B 28  ? 0.3597 0.4066 0.7325 -0.0724 -0.0017 0.0265  28  LYS B CD  
3160 C CE  . LYS B 28  ? 0.3784 0.4537 0.7272 -0.0583 0.0058  0.0196  28  LYS B CE  
3161 N NZ  . LYS B 28  ? 0.3835 0.4993 0.7573 -0.0626 0.0139  0.0155  28  LYS B NZ  
3162 N N   . ARG B 29  ? 0.4138 0.2926 0.8041 -0.0782 -0.0408 0.0454  29  ARG B N   
3163 C CA  . ARG B 29  ? 0.4695 0.3090 0.8866 -0.0793 -0.0604 0.0285  29  ARG B CA  
3164 C C   . ARG B 29  ? 0.4953 0.3045 0.8797 -0.0557 -0.0713 0.0234  29  ARG B C   
3165 O O   . ARG B 29  ? 0.5075 0.2949 0.9004 -0.0447 -0.0913 -0.0031 29  ARG B O   
3166 C CB  . ARG B 29  ? 0.4588 0.2811 0.9098 -0.1007 -0.0548 0.0479  29  ARG B CB  
3167 C CG  . ARG B 29  ? 0.4572 0.3147 0.9450 -0.1206 -0.0502 0.0423  29  ARG B CG  
3168 C CD  . ARG B 29  ? 0.5303 0.3689 1.0549 -0.1338 -0.0617 0.0324  29  ARG B CD  
3169 N NE  . ARG B 29  ? 0.6055 0.4828 1.1627 -0.1481 -0.0618 0.0191  29  ARG B NE  
3170 C CZ  . ARG B 29  ? 0.6042 0.4931 1.1756 -0.1420 -0.0810 -0.0182 29  ARG B CZ  
3171 N NH1 . ARG B 29  ? 0.6565 0.5217 1.2147 -0.1221 -0.1022 -0.0470 29  ARG B NH1 
3172 N NH2 . ARG B 29  ? 0.5143 0.4442 1.1124 -0.1538 -0.0790 -0.0269 29  ARG B NH2 
3173 N N   . ILE B 30  ? 0.5022 0.3151 0.8489 -0.0452 -0.0597 0.0456  30  ILE B N   
3174 C CA  . ILE B 30  ? 0.5019 0.3002 0.8159 -0.0203 -0.0693 0.0395  30  ILE B CA  
3175 C C   . ILE B 30  ? 0.4771 0.3034 0.7740 -0.0034 -0.0784 0.0118  30  ILE B C   
3176 O O   . ILE B 30  ? 0.5136 0.3290 0.8050 0.0153  -0.0940 -0.0084 30  ILE B O   
3177 C CB  . ILE B 30  ? 0.5305 0.3366 0.8108 -0.0137 -0.0555 0.0682  30  ILE B CB  
3178 C CG1 . ILE B 30  ? 0.5017 0.2813 0.7962 -0.0258 -0.0457 0.1010  30  ILE B CG1 
3179 C CG2 . ILE B 30  ? 0.4554 0.2588 0.7038 0.0123  -0.0649 0.0611  30  ILE B CG2 
3180 C CD1 . ILE B 30  ? 0.5606 0.3647 0.8228 -0.0211 -0.0292 0.1298  30  ILE B CD1 
3181 N N   . VAL B 31  ? 0.4579 0.3218 0.7468 -0.0079 -0.0685 0.0116  31  VAL B N   
3182 C CA  . VAL B 31  ? 0.4481 0.3392 0.7259 0.0063  -0.0750 -0.0091 31  VAL B CA  
3183 C C   . VAL B 31  ? 0.4518 0.3397 0.7532 0.0105  -0.0914 -0.0366 31  VAL B C   
3184 O O   . VAL B 31  ? 0.4525 0.3513 0.7411 0.0318  -0.1028 -0.0546 31  VAL B O   
3185 C CB  . VAL B 31  ? 0.4303 0.3542 0.7035 -0.0013 -0.0620 -0.0040 31  VAL B CB  
3186 C CG1 . VAL B 31  ? 0.3556 0.3046 0.6229 0.0128  -0.0680 -0.0211 31  VAL B CG1 
3187 C CG2 . VAL B 31  ? 0.3532 0.2829 0.6013 -0.0018 -0.0498 0.0163  31  VAL B CG2 
3188 N N   . GLU B 32  ? 0.4224 0.3006 0.7603 -0.0090 -0.0933 -0.0406 32  GLU B N   
3189 C CA  . GLU B 32  ? 0.4287 0.3091 0.7931 -0.0062 -0.1116 -0.0716 32  GLU B CA  
3190 C C   . GLU B 32  ? 0.4420 0.2926 0.8023 0.0128  -0.1311 -0.0910 32  GLU B C   
3191 O O   . GLU B 32  ? 0.4525 0.3193 0.8086 0.0330  -0.1471 -0.1201 32  GLU B O   
3192 C CB  . GLU B 32  ? 0.4347 0.3102 0.8469 -0.0343 -0.1111 -0.0713 32  GLU B CB  
3193 C CG  . GLU B 32  ? 0.4110 0.2879 0.8560 -0.0323 -0.1346 -0.1084 32  GLU B CG  
3194 C CD  . GLU B 32  ? 0.4650 0.3476 0.9520 -0.0584 -0.1313 -0.1042 32  GLU B CD  
3195 O OE1 . GLU B 32  ? 0.5146 0.3795 1.0108 -0.0778 -0.1159 -0.0736 32  GLU B OE1 
3196 O OE2 . GLU B 32  ? 0.4943 0.4031 1.0028 -0.0575 -0.1433 -0.1300 32  GLU B OE2 
3197 N N   . GLY B 33  ? 0.4251 0.2345 0.7845 0.0102  -0.1301 -0.0754 33  GLY B N   
3198 C CA  . GLY B 33  ? 0.4522 0.2338 0.8053 0.0306  -0.1481 -0.0938 33  GLY B CA  
3199 C C   . GLY B 33  ? 0.5069 0.3065 0.8196 0.0639  -0.1515 -0.1004 33  GLY B C   
3200 O O   . GLY B 33  ? 0.5902 0.3860 0.8912 0.0862  -0.1666 -0.1220 33  GLY B O   
3201 N N   . ILE B 34  ? 0.4728 0.3059 0.7582 0.0649  -0.1343 -0.0791 34  ILE B N   
3202 C CA  . ILE B 34  ? 0.4659 0.3285 0.7166 0.0917  -0.1337 -0.0792 34  ILE B CA  
3203 C C   . ILE B 34  ? 0.4600 0.3675 0.7053 0.1034  -0.1361 -0.0948 34  ILE B C   
3204 O O   . ILE B 34  ? 0.4618 0.3893 0.6931 0.1313  -0.1471 -0.1124 34  ILE B O   
3205 C CB  . ILE B 34  ? 0.4430 0.3161 0.6721 0.0854  -0.1157 -0.0475 34  ILE B CB  
3206 C CG1 . ILE B 34  ? 0.4674 0.3017 0.6955 0.0817  -0.1141 -0.0301 34  ILE B CG1 
3207 C CG2 . ILE B 34  ? 0.4103 0.3221 0.6131 0.1079  -0.1142 -0.0462 34  ILE B CG2 
3208 C CD1 . ILE B 34  ? 0.4521 0.3007 0.6585 0.0776  -0.0991 -0.0021 34  ILE B CD1 
3209 N N   . LEU B 35  ? 0.4305 0.3569 0.6860 0.0851  -0.1257 -0.0873 35  LEU B N   
3210 C CA  . LEU B 35  ? 0.3981 0.3673 0.6461 0.0963  -0.1241 -0.0932 35  LEU B CA  
3211 C C   . LEU B 35  ? 0.4353 0.4155 0.7073 0.0950  -0.1363 -0.1191 35  LEU B C   
3212 O O   . LEU B 35  ? 0.4065 0.4235 0.6737 0.1053  -0.1351 -0.1230 35  LEU B O   
3213 C CB  . LEU B 35  ? 0.3936 0.3776 0.6344 0.0818  -0.1050 -0.0677 35  LEU B CB  
3214 C CG  . LEU B 35  ? 0.4089 0.3891 0.6285 0.0837  -0.0959 -0.0460 35  LEU B CG  
3215 C CD1 . LEU B 35  ? 0.3356 0.3265 0.5518 0.0689  -0.0810 -0.0274 35  LEU B CD1 
3216 C CD2 . LEU B 35  ? 0.3159 0.3200 0.5163 0.1110  -0.1010 -0.0476 35  LEU B CD2 
3217 N N   . LYS B 36  ? 0.4339 0.4287 0.5699 0.0981  -0.1685 -0.1765 36  LYS B N   
3218 C CA  . LYS B 36  ? 0.4442 0.4473 0.6043 0.0985  -0.1909 -0.1917 36  LYS B CA  
3219 C C   . LYS B 36  ? 0.4615 0.4862 0.6269 0.0892  -0.1766 -0.1697 36  LYS B C   
3220 O O   . LYS B 36  ? 0.4762 0.5294 0.6374 0.1007  -0.1868 -0.1820 36  LYS B O   
3221 C CB  . LYS B 36  ? 0.4750 0.5031 0.6129 0.1255  -0.2101 -0.2275 36  LYS B CB  
3222 C CG  . LYS B 36  ? 0.5220 0.5404 0.6439 0.1427  -0.2182 -0.2496 36  LYS B CG  
3223 C CD  . LYS B 36  ? 0.5667 0.5379 0.7243 0.1369  -0.2459 -0.2651 36  LYS B CD  
3224 C CE  . LYS B 36  ? 0.6451 0.6104 0.7856 0.1578  -0.2485 -0.2779 36  LYS B CE  
3225 N NZ  . LYS B 36  ? 0.6743 0.5972 0.8261 0.1451  -0.2434 -0.2600 36  LYS B NZ  
3226 N N   . ARG B 37  ? 0.4659 0.4794 0.6381 0.0724  -0.1539 -0.1382 37  ARG B N   
3227 C CA  . ARG B 37  ? 0.4494 0.4810 0.6316 0.0653  -0.1408 -0.1171 37  ARG B CA  
3228 C C   . ARG B 37  ? 0.4416 0.4559 0.6641 0.0433  -0.1366 -0.0959 37  ARG B C   
3229 O O   . ARG B 37  ? 0.4426 0.4310 0.6596 0.0365  -0.1260 -0.0827 37  ARG B O   
3230 C CB  . ARG B 37  ? 0.4638 0.5035 0.6052 0.0718  -0.1117 -0.0979 37  ARG B CB  
3231 C CG  . ARG B 37  ? 0.4683 0.5256 0.5694 0.0908  -0.1090 -0.1098 37  ARG B CG  
3232 C CD  . ARG B 37  ? 0.4323 0.5190 0.5315 0.1061  -0.1235 -0.1207 37  ARG B CD  
3233 N NE  . ARG B 37  ? 0.4854 0.5820 0.5866 0.1060  -0.1110 -0.0992 37  ARG B NE  
3234 C CZ  . ARG B 37  ? 0.4802 0.5771 0.5460 0.1149  -0.0889 -0.0804 37  ARG B CZ  
3235 N NH1 . ARG B 37  ? 0.4729 0.5634 0.5023 0.1198  -0.0743 -0.0774 37  ARG B NH1 
3236 N NH2 . ARG B 37  ? 0.4016 0.5055 0.4715 0.1188  -0.0812 -0.0637 37  ARG B NH2 
3237 N N   . PRO B 38  ? 0.4793 0.5121 0.7428 0.0330  -0.1437 -0.0905 38  PRO B N   
3238 C CA  . PRO B 38  ? 0.4095 0.4313 0.7176 0.0101  -0.1383 -0.0676 38  PRO B CA  
3239 C C   . PRO B 38  ? 0.4156 0.4416 0.7041 0.0090  -0.1051 -0.0351 38  PRO B C   
3240 O O   . PRO B 38  ? 0.3937 0.4316 0.6429 0.0238  -0.0895 -0.0325 38  PRO B O   
3241 C CB  . PRO B 38  ? 0.3865 0.4405 0.7477 0.0006  -0.1563 -0.0753 38  PRO B CB  
3242 C CG  . PRO B 38  ? 0.3846 0.4737 0.7144 0.0236  -0.1575 -0.0887 38  PRO B CG  
3243 C CD  . PRO B 38  ? 0.4550 0.5261 0.7260 0.0432  -0.1553 -0.1029 38  PRO B CD  
3244 N N   . PRO B 39  ? 0.4167 0.4307 0.7292 -0.0068 -0.0937 -0.0096 39  PRO B N   
3245 C CA  . PRO B 39  ? 0.4019 0.4240 0.6923 -0.0034 -0.0630 0.0187  39  PRO B CA  
3246 C C   . PRO B 39  ? 0.4595 0.5206 0.7483 0.0059  -0.0499 0.0247  39  PRO B C   
3247 O O   . PRO B 39  ? 0.4696 0.5305 0.7183 0.0197  -0.0298 0.0328  39  PRO B O   
3248 C CB  . PRO B 39  ? 0.3864 0.4005 0.7153 -0.0227 -0.0561 0.0463  39  PRO B CB  
3249 C CG  . PRO B 39  ? 0.4708 0.4465 0.8170 -0.0318 -0.0811 0.0317  39  PRO B CG  
3250 C CD  . PRO B 39  ? 0.4259 0.4093 0.7759 -0.0246 -0.1078 -0.0058 39  PRO B CD  
3251 N N   . ASP B 40  ? 0.4232 0.5176 0.7562 0.0003  -0.0627 0.0191  40  ASP B N   
3252 C CA  . ASP B 40  ? 0.4251 0.5605 0.7592 0.0134  -0.0523 0.0248  40  ASP B CA  
3253 C C   . ASP B 40  ? 0.4617 0.5916 0.7429 0.0375  -0.0529 0.0094  40  ASP B C   
3254 O O   . ASP B 40  ? 0.4925 0.6446 0.7612 0.0538  -0.0418 0.0161  40  ASP B O   
3255 C CB  . ASP B 40  ? 0.4399 0.6185 0.8390 0.0021  -0.0701 0.0192  40  ASP B CB  
3256 C CG  . ASP B 40  ? 0.5624 0.7306 0.9801 -0.0038 -0.1051 -0.0124 40  ASP B CG  
3257 O OD1 . ASP B 40  ? 0.4986 0.6956 0.9179 0.0102  -0.1233 -0.0335 40  ASP B OD1 
3258 O OD2 . ASP B 40  ? 0.5552 0.6854 0.9823 -0.0187 -0.1156 -0.0172 40  ASP B OD2 
3259 N N   . GLU B 41  ? 0.3981 0.4997 0.6488 0.0411  -0.0644 -0.0091 41  GLU B N   
3260 C CA  . GLU B 41  ? 0.4381 0.5329 0.6386 0.0607  -0.0608 -0.0180 41  GLU B CA  
3261 C C   . GLU B 41  ? 0.4590 0.5200 0.6166 0.0618  -0.0425 -0.0119 41  GLU B C   
3262 O O   . GLU B 41  ? 0.4709 0.5213 0.5914 0.0719  -0.0394 -0.0189 41  GLU B O   
3263 C CB  . GLU B 41  ? 0.4478 0.5488 0.6455 0.0674  -0.0858 -0.0440 41  GLU B CB  
3264 C CG  . GLU B 41  ? 0.4454 0.5858 0.6807 0.0714  -0.1071 -0.0552 41  GLU B CG  
3265 C CD  . GLU B 41  ? 0.4632 0.6140 0.6876 0.0846  -0.1337 -0.0846 41  GLU B CD  
3266 O OE1 . GLU B 41  ? 0.5083 0.6432 0.6866 0.0966  -0.1293 -0.0913 41  GLU B OE1 
3267 O OE2 . GLU B 41  ? 0.4830 0.6621 0.7463 0.0837  -0.1595 -0.1023 41  GLU B OE2 
3268 N N   . GLN B 42  ? 0.4248 0.4721 0.5877 0.0519  -0.0304 0.0018  42  GLN B N   
3269 C CA  . GLN B 42  ? 0.4518 0.4718 0.5784 0.0531  -0.0172 0.0037  42  GLN B CA  
3270 C C   . GLN B 42  ? 0.4502 0.4700 0.5654 0.0581  0.0037  0.0213  42  GLN B C   
3271 O O   . GLN B 42  ? 0.4093 0.4485 0.5511 0.0552  0.0096  0.0365  42  GLN B O   
3272 C CB  . GLN B 42  ? 0.4336 0.4348 0.5665 0.0429  -0.0257 -0.0005 42  GLN B CB  
3273 C CG  . GLN B 42  ? 0.4635 0.4615 0.6108 0.0402  -0.0488 -0.0205 42  GLN B CG  
3274 C CD  . GLN B 42  ? 0.4367 0.4117 0.5950 0.0326  -0.0570 -0.0200 42  GLN B CD  
3275 O OE1 . GLN B 42  ? 0.4509 0.4124 0.5894 0.0339  -0.0455 -0.0103 42  GLN B OE1 
3276 N NE2 . GLN B 42  ? 0.3813 0.3497 0.5708 0.0267  -0.0786 -0.0309 42  GLN B NE2 
3277 N N   . ARG B 43  ? 0.4283 0.4278 0.5054 0.0654  0.0147  0.0180  43  ARG B N   
3278 C CA  . ARG B 43  ? 0.4330 0.4252 0.4908 0.0725  0.0310  0.0268  43  ARG B CA  
3279 C C   . ARG B 43  ? 0.4590 0.4290 0.4940 0.0682  0.0303  0.0178  43  ARG B C   
3280 O O   . ARG B 43  ? 0.4520 0.4090 0.4743 0.0641  0.0245  0.0037  43  ARG B O   
3281 C CB  . ARG B 43  ? 0.4151 0.4000 0.4496 0.0878  0.0416  0.0265  43  ARG B CB  
3282 C CG  . ARG B 43  ? 0.4335 0.4469 0.4885 0.0989  0.0439  0.0365  43  ARG B CG  
3283 C CD  . ARG B 43  ? 0.3758 0.3731 0.4030 0.1180  0.0520  0.0354  43  ARG B CD  
3284 N NE  . ARG B 43  ? 0.3978 0.4278 0.4436 0.1341  0.0548  0.0447  43  ARG B NE  
3285 C CZ  . ARG B 43  ? 0.4413 0.4618 0.4671 0.1568  0.0605  0.0459  43  ARG B CZ  
3286 N NH1 . ARG B 43  ? 0.4501 0.4226 0.4376 0.1628  0.0641  0.0400  43  ARG B NH1 
3287 N NH2 . ARG B 43  ? 0.3937 0.4536 0.4411 0.1739  0.0622  0.0535  43  ARG B NH2 
3288 N N   . LEU B 44  ? 0.4032 0.3742 0.4333 0.0705  0.0365  0.0268  44  LEU B N   
3289 C CA  . LEU B 44  ? 0.4776 0.4333 0.4846 0.0708  0.0338  0.0175  44  LEU B CA  
3290 C C   . LEU B 44  ? 0.5270 0.4774 0.5030 0.0849  0.0455  0.0152  44  LEU B C   
3291 O O   . LEU B 44  ? 0.5080 0.4724 0.4823 0.0963  0.0577  0.0291  44  LEU B O   
3292 C CB  . LEU B 44  ? 0.4338 0.3916 0.4535 0.0665  0.0275  0.0284  44  LEU B CB  
3293 C CG  . LEU B 44  ? 0.4246 0.3797 0.4736 0.0547  0.0112  0.0244  44  LEU B CG  
3294 C CD1 . LEU B 44  ? 0.4377 0.3825 0.4954 0.0526  0.0038  0.0351  44  LEU B CD1 
3295 C CD2 . LEU B 44  ? 0.4432 0.3930 0.4835 0.0528  0.0013  0.0006  44  LEU B CD2 
3296 N N   . TYR B 45  ? 0.4859 0.4194 0.4397 0.0847  0.0408  -0.0044 45  TYR B N   
3297 C CA  . TYR B 45  ? 0.5341 0.4565 0.4582 0.0977  0.0465  -0.0155 45  TYR B CA  
3298 C C   . TYR B 45  ? 0.5781 0.5001 0.4836 0.1010  0.0380  -0.0290 45  TYR B C   
3299 O O   . TYR B 45  ? 0.5979 0.5211 0.5130 0.0898  0.0266  -0.0380 45  TYR B O   
3300 C CB  . TYR B 45  ? 0.5291 0.4268 0.4467 0.0934  0.0468  -0.0306 45  TYR B CB  
3301 C CG  . TYR B 45  ? 0.5238 0.4194 0.4515 0.0963  0.0539  -0.0188 45  TYR B CG  
3302 C CD1 . TYR B 45  ? 0.4968 0.4000 0.4457 0.0848  0.0496  -0.0123 45  TYR B CD1 
3303 C CD2 . TYR B 45  ? 0.5523 0.4401 0.4656 0.1148  0.0632  -0.0167 45  TYR B CD2 
3304 C CE1 . TYR B 45  ? 0.4521 0.3573 0.4074 0.0912  0.0536  -0.0026 45  TYR B CE1 
3305 C CE2 . TYR B 45  ? 0.5169 0.4053 0.4386 0.1216  0.0680  -0.0062 45  TYR B CE2 
3306 C CZ  . TYR B 45  ? 0.4940 0.3917 0.4364 0.1095  0.0627  0.0013  45  TYR B CZ  
3307 O OH  . TYR B 45  ? 0.5359 0.4381 0.4838 0.1199  0.0652  0.0109  45  TYR B OH  
3308 N N   . LYS B 46  ? 0.3607 0.6458 0.5780 0.0165  0.1078  0.0273  46  LYS B N   
3309 C CA  . LYS B 46  ? 0.3816 0.6582 0.5719 0.0238  0.0960  0.0310  46  LYS B CA  
3310 C C   . LYS B 46  ? 0.4197 0.6923 0.6115 0.0139  0.0701  0.0325  46  LYS B C   
3311 O O   . LYS B 46  ? 0.4015 0.6451 0.5817 0.0199  0.0677  0.0234  46  LYS B O   
3312 C CB  . LYS B 46  ? 0.4123 0.6498 0.5650 0.0380  0.1113  0.0279  46  LYS B CB  
3313 C CG  . LYS B 46  ? 0.4961 0.7180 0.6153 0.0501  0.0959  0.0297  46  LYS B CG  
3314 C CD  . LYS B 46  ? 0.5316 0.7089 0.6025 0.0642  0.1118  0.0293  46  LYS B CD  
3315 C CE  . LYS B 46  ? 0.5527 0.7085 0.5867 0.0798  0.0920  0.0289  46  LYS B CE  
3316 N NZ  . LYS B 46  ? 0.6228 0.7787 0.6573 0.0798  0.0657  0.0255  46  LYS B NZ  
3317 N N   . ASP B 47  ? 0.3653 0.6692 0.5700 -0.0009 0.0480  0.0443  47  ASP B N   
3318 C CA  . ASP B 47  ? 0.3535 0.6516 0.5637 -0.0226 0.0163  0.0525  47  ASP B CA  
3319 C C   . ASP B 47  ? 0.4334 0.7144 0.6531 -0.0269 0.0175  0.0456  47  ASP B C   
3320 O O   . ASP B 47  ? 0.3857 0.6954 0.6275 -0.0326 0.0317  0.0479  47  ASP B O   
3321 C CB  . ASP B 47  ? 0.3857 0.6367 0.5640 -0.0160 -0.0104 0.0484  47  ASP B CB  
3322 C CG  . ASP B 47  ? 0.4733 0.7420 0.6453 -0.0136 -0.0196 0.0553  47  ASP B CG  
3323 O OD1 . ASP B 47  ? 0.4629 0.7821 0.6616 -0.0372 -0.0362 0.0723  47  ASP B OD1 
3324 O OD2 . ASP B 47  ? 0.5100 0.7478 0.6504 0.0119  -0.0100 0.0443  47  ASP B OD2 
3325 N N   . ASP B 48  ? 0.4618 0.6953 0.6620 -0.0182 0.0000  0.0335  48  ASP B N   
3326 C CA  . ASP B 48  ? 0.4693 0.6879 0.6788 -0.0173 -0.0058 0.0231  48  ASP B CA  
3327 C C   . ASP B 48  ? 0.4041 0.6270 0.6227 0.0073  0.0274  0.0032  48  ASP B C   
3328 O O   . ASP B 48  ? 0.3532 0.5734 0.5867 0.0120  0.0239  -0.0089 48  ASP B O   
3329 C CB  . ASP B 48  ? 0.5303 0.6943 0.7120 -0.0183 -0.0534 0.0180  48  ASP B CB  
3330 C CG  . ASP B 48  ? 0.6664 0.8268 0.8493 -0.0574 -0.0904 0.0430  48  ASP B CG  
3331 O OD1 . ASP B 48  ? 0.8034 0.9223 0.9600 -0.0707 -0.1345 0.0516  48  ASP B OD1 
3332 O OD2 . ASP B 48  ? 0.6912 0.8900 0.8982 -0.0766 -0.0771 0.0561  48  ASP B OD2 
3333 N N   . GLN B 49  ? 0.3862 0.6183 0.5967 0.0202  0.0574  0.0016  49  GLN B N   
3334 C CA  . GLN B 49  ? 0.3611 0.6042 0.5791 0.0356  0.0893  -0.0106 49  GLN B CA  
3335 C C   . GLN B 49  ? 0.3718 0.6417 0.6233 0.0223  0.1127  -0.0043 49  GLN B C   
3336 O O   . GLN B 49  ? 0.3920 0.6648 0.6380 0.0162  0.1220  0.0073  49  GLN B O   
3337 C CB  . GLN B 49  ? 0.3799 0.6112 0.5616 0.0513  0.1068  -0.0105 49  GLN B CB  
3338 C CG  . GLN B 49  ? 0.4668 0.7203 0.6540 0.0586  0.1445  -0.0146 49  GLN B CG  
3339 C CD  . GLN B 49  ? 0.4807 0.7535 0.6779 0.0789  0.1448  -0.0356 49  GLN B CD  
3340 O OE1 . GLN B 49  ? 0.4560 0.7613 0.6964 0.0733  0.1534  -0.0423 49  GLN B OE1 
3341 N NE2 . GLN B 49  ? 0.4941 0.7467 0.6494 0.1073  0.1313  -0.0493 49  GLN B NE2 
3342 N N   . LEU B 50  ? 0.3377 0.6229 0.6211 0.0218  0.1165  -0.0147 50  LEU B N   
3343 C CA  . LEU B 50  ? 0.2989 0.6018 0.6129 0.0104  0.1336  -0.0111 50  LEU B CA  
3344 C C   . LEU B 50  ? 0.3297 0.6350 0.6350 0.0076  0.1627  -0.0030 50  LEU B C   
3345 O O   . LEU B 50  ? 0.3876 0.7007 0.6795 0.0164  0.1790  -0.0059 50  LEU B O   
3346 C CB  . LEU B 50  ? 0.3189 0.6395 0.6711 0.0122  0.1291  -0.0263 50  LEU B CB  
3347 C CG  . LEU B 50  ? 0.2475 0.5730 0.6197 0.0000  0.1315  -0.0229 50  LEU B CG  
3348 C CD1 . LEU B 50  ? 0.2337 0.5459 0.6028 -0.0065 0.1156  -0.0168 50  LEU B CD1 
3349 C CD2 . LEU B 50  ? 0.2142 0.5583 0.6166 0.0060  0.1249  -0.0384 50  LEU B CD2 
3350 N N   . LEU B 51  ? 0.5398 0.4824 0.5395 0.1088  -0.0017 -0.0464 51  LEU B N   
3351 C CA  . LEU B 51  ? 0.5258 0.5196 0.5632 0.1040  0.0121  -0.0186 51  LEU B CA  
3352 C C   . LEU B 51  ? 0.5260 0.5451 0.6217 0.1030  0.0131  -0.0018 51  LEU B C   
3353 O O   . LEU B 51  ? 0.5053 0.4911 0.6175 0.0959  -0.0008 -0.0085 51  LEU B O   
3354 C CB  . LEU B 51  ? 0.5203 0.5009 0.5610 0.0840  0.0109  -0.0090 51  LEU B CB  
3355 C CG  . LEU B 51  ? 0.5471 0.5091 0.5422 0.0835  0.0085  -0.0222 51  LEU B CG  
3356 C CD1 . LEU B 51  ? 0.5336 0.4919 0.5422 0.0652  0.0083  -0.0106 51  LEU B CD1 
3357 C CD2 . LEU B 51  ? 0.5324 0.5297 0.5024 0.1032  0.0156  -0.0231 51  LEU B CD2 
3358 N N   . ASP B 52  ? 0.4877 0.5667 0.6156 0.1111  0.0287  0.0211  52  ASP B N   
3359 C CA  . ASP B 52  ? 0.4574 0.5681 0.6530 0.1097  0.0297  0.0412  52  ASP B CA  
3360 C C   . ASP B 52  ? 0.4605 0.5772 0.7090 0.0883  0.0249  0.0681  52  ASP B C   
3361 O O   . ASP B 52  ? 0.4643 0.5972 0.7083 0.0797  0.0331  0.0857  52  ASP B O   
3362 C CB  . ASP B 52  ? 0.4226 0.6017 0.6358 0.1280  0.0517  0.0588  52  ASP B CB  
3363 C CG  . ASP B 52  ? 0.4260 0.6017 0.6067 0.1528  0.0514  0.0303  52  ASP B CG  
3364 O OD1 . ASP B 52  ? 0.4583 0.5766 0.6120 0.1532  0.0315  0.0007  52  ASP B OD1 
3365 O OD2 . ASP B 52  ? 0.4568 0.6881 0.6379 0.1738  0.0709  0.0380  52  ASP B OD2 
3366 N N   . ASP B 53  ? 0.4165 0.5200 0.7182 0.0816  0.0081  0.0705  53  ASP B N   
3367 C CA  . ASP B 53  ? 0.4266 0.5248 0.7815 0.0632  -0.0051 0.0895  53  ASP B CA  
3368 C C   . ASP B 53  ? 0.4237 0.5789 0.8222 0.0548  0.0108  0.1312  53  ASP B C   
3369 O O   . ASP B 53  ? 0.4255 0.5734 0.8412 0.0400  0.0037  0.1452  53  ASP B O   
3370 C CB  . ASP B 53  ? 0.4090 0.4924 0.8231 0.0622  -0.0286 0.0867  53  ASP B CB  
3371 C CG  . ASP B 53  ? 0.5048 0.5208 0.8762 0.0670  -0.0508 0.0493  53  ASP B CG  
3372 O OD1 . ASP B 53  ? 0.5553 0.5380 0.8595 0.0669  -0.0464 0.0306  53  ASP B OD1 
3373 O OD2 . ASP B 53  ? 0.4111 0.4080 0.8169 0.0712  -0.0733 0.0403  53  ASP B OD2 
3374 N N   . GLY B 54  ? 0.4003 0.6142 0.8172 0.0654  0.0325  0.1527  54  GLY B N   
3375 C CA  . GLY B 54  ? 0.3563 0.6305 0.8207 0.0583  0.0497  0.1996  54  GLY B CA  
3376 C C   . GLY B 54  ? 0.3977 0.6986 0.8051 0.0650  0.0722  0.2108  54  GLY B C   
3377 O O   . GLY B 54  ? 0.3799 0.7289 0.8192 0.0593  0.0866  0.2530  54  GLY B O   
3378 N N   . LYS B 55  ? 0.4171 0.6882 0.7425 0.0778  0.0737  0.1757  55  LYS B N   
3379 C CA  . LYS B 55  ? 0.4609 0.7476 0.7312 0.0845  0.0870  0.1815  55  LYS B CA  
3380 C C   . LYS B 55  ? 0.4793 0.7344 0.7532 0.0637  0.0721  0.1876  55  LYS B C   
3381 O O   . LYS B 55  ? 0.4836 0.6893 0.7700 0.0503  0.0513  0.1686  55  LYS B O   
3382 C CB  . LYS B 55  ? 0.5030 0.7644 0.6926 0.1049  0.0872  0.1403  55  LYS B CB  
3383 C CG  . LYS B 55  ? 0.4527 0.7420 0.6332 0.1295  0.0991  0.1283  55  LYS B CG  
3384 C CD  . LYS B 55  ? 0.5096 0.8611 0.6596 0.1539  0.1247  0.1446  55  LYS B CD  
3385 C CE  . LYS B 55  ? 0.5245 0.9478 0.7377 0.1602  0.1481  0.1818  55  LYS B CE  
3386 N NZ  . LYS B 55  ? 0.6304 1.1179 0.8045 0.1930  0.1765  0.1904  55  LYS B NZ  
3387 N N   . THR B 56  ? 0.4726 0.7581 0.7341 0.0634  0.0827  0.2142  56  THR B N   
3388 C CA  . THR B 56  ? 0.5001 0.7541 0.7559 0.0475  0.0674  0.2143  56  THR B CA  
3389 C C   . THR B 56  ? 0.5150 0.7280 0.6982 0.0553  0.0603  0.1738  56  THR B C   
3390 O O   . THR B 56  ? 0.5448 0.7591 0.6775 0.0746  0.0676  0.1512  56  THR B O   
3391 C CB  . THR B 56  ? 0.4682 0.7652 0.7380 0.0439  0.0773  0.2588  56  THR B CB  
3392 O OG1 . THR B 56  ? 0.4741 0.7906 0.6716 0.0647  0.0909  0.2532  56  THR B OG1 
3393 C CG2 . THR B 56  ? 0.4119 0.7637 0.7481 0.0413  0.0920  0.3035  56  THR B CG2 
3394 N N   . LEU B 57  ? 0.5396 0.7161 0.7235 0.0403  0.0442  0.1647  57  LEU B N   
3395 C CA  . LEU B 57  ? 0.5372 0.6758 0.6664 0.0435  0.0359  0.1305  57  LEU B CA  
3396 C C   . LEU B 57  ? 0.5798 0.7405 0.6553 0.0608  0.0429  0.1310  57  LEU B C   
3397 O O   . LEU B 57  ? 0.5846 0.7254 0.6102 0.0738  0.0393  0.1007  57  LEU B O   
3398 C CB  . LEU B 57  ? 0.5437 0.6507 0.6932 0.0253  0.0202  0.1261  57  LEU B CB  
3399 C CG  . LEU B 57  ? 0.5245 0.6052 0.7187 0.0130  0.0099  0.1198  57  LEU B CG  
3400 C CD1 . LEU B 57  ? 0.4596 0.5054 0.6543 0.0024  -0.0026 0.1021  57  LEU B CD1 
3401 C CD2 . LEU B 57  ? 0.4712 0.5349 0.6508 0.0213  0.0125  0.0982  57  LEU B CD2 
3402 N N   . GLY B 58  ? 0.5558 0.7557 0.6401 0.0622  0.0502  0.1656  58  GLY B N   
3403 C CA  . GLY B 58  ? 0.5475 0.7722 0.5744 0.0838  0.0569  0.1676  58  GLY B CA  
3404 C C   . GLY B 58  ? 0.5981 0.8480 0.5892 0.1103  0.0722  0.1557  58  GLY B C   
3405 O O   . GLY B 58  ? 0.6814 0.9236 0.6114 0.1320  0.0676  0.1292  58  GLY B O   
3406 N N   . GLU B 59  ? 0.5203 0.7997 0.5528 0.1104  0.0878  0.1731  59  GLU B N   
3407 C CA  . GLU B 59  ? 0.5524 0.8591 0.5582 0.1371  0.1028  0.1603  59  GLU B CA  
3408 C C   . GLU B 59  ? 0.5991 0.8543 0.5689 0.1444  0.0865  0.1102  59  GLU B C   
3409 O O   . GLU B 59  ? 0.6350 0.9000 0.5597 0.1722  0.0902  0.0879  59  GLU B O   
3410 C CB  . GLU B 59  ? 0.5490 0.8961 0.6200 0.1326  0.1197  0.1889  59  GLU B CB  
3411 C CG  . GLU B 59  ? 0.4796 0.8948 0.5799 0.1344  0.1430  0.2434  59  GLU B CG  
3412 C CD  . GLU B 59  ? 0.4662 0.9133 0.6563 0.1186  0.1522  0.2783  59  GLU B CD  
3413 O OE1 . GLU B 59  ? 0.4885 0.8996 0.7163 0.1060  0.1367  0.2579  59  GLU B OE1 
3414 O OE2 . GLU B 59  ? 0.5032 1.0115 0.7279 0.1191  0.1737  0.3279  59  GLU B OE2 
3415 N N   . CYS B 60  ? 0.6032 0.8042 0.5919 0.1213  0.0680  0.0930  60  CYS B N   
3416 C CA  . CYS B 60  ? 0.6103 0.7582 0.5693 0.1231  0.0517  0.0518  60  CYS B CA  
3417 C C   . CYS B 60  ? 0.6881 0.8068 0.5975 0.1283  0.0357  0.0286  60  CYS B C   
3418 O O   . CYS B 60  ? 0.6951 0.7706 0.5813 0.1300  0.0207  -0.0030 60  CYS B O   
3419 C CB  . CYS B 60  ? 0.5798 0.6857 0.5769 0.0979  0.0411  0.0465  60  CYS B CB  
3420 S SG  . CYS B 60  ? 0.5761 0.6970 0.6302 0.0932  0.0479  0.0610  60  CYS B SG  
3421 N N   . GLY B 61  ? 0.6554 0.7940 0.5522 0.1297  0.0357  0.0447  61  GLY B N   
3422 C CA  . GLY B 61  ? 0.6380 0.7502 0.4935 0.1354  0.0165  0.0233  61  GLY B CA  
3423 C C   . GLY B 61  ? 0.6864 0.7727 0.5685 0.1093  0.0037  0.0288  61  GLY B C   
3424 O O   . GLY B 61  ? 0.7746 0.8431 0.6311 0.1128  -0.0139 0.0146  61  GLY B O   
3425 N N   . PHE B 62  ? 0.6720 0.7552 0.6062 0.0856  0.0093  0.0467  62  PHE B N   
3426 C CA  . PHE B 62  ? 0.6613 0.7239 0.6231 0.0640  -0.0022 0.0502  62  PHE B CA  
3427 C C   . PHE B 62  ? 0.7134 0.8067 0.6784 0.0655  -0.0024 0.0779  62  PHE B C   
3428 O O   . PHE B 62  ? 0.7230 0.8512 0.7121 0.0648  0.0107  0.1099  62  PHE B O   
3429 C CB  . PHE B 62  ? 0.5726 0.6208 0.5845 0.0435  0.0013  0.0562  62  PHE B CB  
3430 C CG  . PHE B 62  ? 0.6077 0.6221 0.6120 0.0418  0.0002  0.0313  62  PHE B CG  
3431 C CD1 . PHE B 62  ? 0.6031 0.5806 0.5948 0.0346  -0.0105 0.0086  62  PHE B CD1 
3432 C CD2 . PHE B 62  ? 0.5749 0.5951 0.5870 0.0475  0.0090  0.0327  62  PHE B CD2 
3433 C CE1 . PHE B 62  ? 0.5500 0.4956 0.5325 0.0326  -0.0112 -0.0095 62  PHE B CE1 
3434 C CE2 . PHE B 62  ? 0.5543 0.5402 0.5548 0.0472  0.0058  0.0107  62  PHE B CE2 
3435 C CZ  . PHE B 62  ? 0.5335 0.4817 0.5168 0.0397  -0.0038 -0.0090 62  PHE B CZ  
3436 N N   . THR B 63  ? 0.7040 0.7834 0.6481 0.0671  -0.0192 0.0674  63  THR B N   
3437 C CA  . THR B 63  ? 0.6873 0.7891 0.6290 0.0693  -0.0245 0.0915  63  THR B CA  
3438 C C   . THR B 63  ? 0.6539 0.7299 0.6313 0.0488  -0.0419 0.0868  63  THR B C   
3439 O O   . THR B 63  ? 0.6543 0.6974 0.6384 0.0403  -0.0521 0.0594  63  THR B O   
3440 C CB  . THR B 63  ? 0.6922 0.8043 0.5689 0.0971  -0.0328 0.0817  63  THR B CB  
3441 O OG1 . THR B 63  ? 0.7656 0.8435 0.6331 0.0942  -0.0596 0.0564  63  THR B OG1 
3442 C CG2 . THR B 63  ? 0.6827 0.7979 0.5189 0.1196  -0.0247 0.0602  63  THR B CG2 
3443 N N   . SER B 64  ? 0.6690 0.7621 0.6727 0.0413  -0.0450 0.1154  64  SER B N   
3444 C CA  . SER B 64  ? 0.6657 0.7385 0.7066 0.0247  -0.0626 0.1108  64  SER B CA  
3445 C C   . SER B 64  ? 0.6747 0.7254 0.6890 0.0307  -0.0833 0.0833  64  SER B C   
3446 O O   . SER B 64  ? 0.6845 0.7127 0.7324 0.0164  -0.0943 0.0667  64  SER B O   
3447 C CB  . SER B 64  ? 0.6553 0.7490 0.7230 0.0195  -0.0675 0.1465  64  SER B CB  
3448 O OG  . SER B 64  ? 0.6958 0.8082 0.7160 0.0373  -0.0729 0.1608  64  SER B OG  
3449 N N   . GLN B 65  ? 0.6785 0.7362 0.6352 0.0531  -0.0899 0.0775  65  GLN B N   
3450 C CA  . GLN B 65  ? 0.6992 0.7322 0.6332 0.0606  -0.1162 0.0490  65  GLN B CA  
3451 C C   . GLN B 65  ? 0.7144 0.7156 0.6592 0.0525  -0.1198 0.0167  65  GLN B C   
3452 O O   . GLN B 65  ? 0.7469 0.7240 0.7041 0.0474  -0.1424 -0.0039 65  GLN B O   
3453 C CB  . GLN B 65  ? 0.7101 0.7561 0.5732 0.0920  -0.1251 0.0465  65  GLN B CB  
3454 N N   . THR B 66  ? 0.6728 0.6731 0.6178 0.0503  -0.0995 0.0139  66  THR B N   
3455 C CA  . THR B 66  ? 0.6651 0.6340 0.6154 0.0435  -0.1026 -0.0125 66  THR B CA  
3456 C C   . THR B 66  ? 0.6463 0.6070 0.6426 0.0212  -0.0852 -0.0077 66  THR B C   
3457 O O   . THR B 66  ? 0.6241 0.5607 0.6234 0.0149  -0.0832 -0.0237 66  THR B O   
3458 C CB  . THR B 66  ? 0.6976 0.6649 0.5979 0.0655  -0.0995 -0.0267 66  THR B CB  
3459 O OG1 . THR B 66  ? 0.7109 0.7085 0.6058 0.0716  -0.0740 -0.0057 66  THR B OG1 
3460 C CG2 . THR B 66  ? 0.7370 0.7065 0.5860 0.0921  -0.1213 -0.0397 66  THR B CG2 
3461 N N   . ALA B 67  ? 0.6277 0.6354 0.6944 -0.0053 -0.0805 -0.0136 67  ALA B N   
3462 C CA  . ALA B 67  ? 0.5234 0.4895 0.5838 0.0014  -0.0770 -0.0065 67  ALA B CA  
3463 C C   . ALA B 67  ? 0.5342 0.4781 0.5762 0.0209  -0.0855 0.0045  67  ALA B C   
3464 O O   . ALA B 67  ? 0.5466 0.4473 0.5581 0.0241  -0.0924 0.0172  67  ALA B O   
3465 C CB  . ALA B 67  ? 0.5279 0.4657 0.5673 -0.0129 -0.0760 0.0014  67  ALA B CB  
3466 N N   . ARG B 68  ? 0.4558 0.4308 0.5166 0.0341  -0.0875 -0.0014 68  ARG B N   
3467 C CA  . ARG B 68  ? 0.5216 0.4854 0.5671 0.0566  -0.0967 0.0073  68  ARG B CA  
3468 C C   . ARG B 68  ? 0.4911 0.4355 0.5404 0.0756  -0.0920 0.0064  68  ARG B C   
3469 O O   . ARG B 68  ? 0.4678 0.4234 0.5413 0.0712  -0.0800 -0.0009 68  ARG B O   
3470 C CB  . ARG B 68  ? 0.4927 0.5068 0.5590 0.0638  -0.1014 0.0004  68  ARG B CB  
3471 C CG  . ARG B 68  ? 0.5946 0.6297 0.6469 0.0520  -0.1089 0.0024  68  ARG B CG  
3472 C CD  . ARG B 68  ? 0.6953 0.7900 0.7789 0.0523  -0.1116 -0.0144 68  ARG B CD  
3473 N NE  . ARG B 68  ? 0.7959 0.9113 0.8639 0.0674  -0.1248 -0.0073 68  ARG B NE  
3474 C CZ  . ARG B 68  ? 0.8110 0.9279 0.8461 0.0645  -0.1331 0.0051  68  ARG B CZ  
3475 N NH1 . ARG B 68  ? 0.8181 0.9197 0.8328 0.0459  -0.1291 0.0125  68  ARG B NH1 
3476 N NH2 . ARG B 68  ? 0.7514 0.8905 0.7742 0.0809  -0.1457 0.0121  68  ARG B NH2 
3477 N N   . PRO B 69  ? 0.4812 0.3968 0.5050 0.0989  -0.1018 0.0141  69  PRO B N   
3478 C CA  . PRO B 69  ? 0.4753 0.3742 0.4972 0.1209  -0.0977 0.0108  69  PRO B CA  
3479 C C   . PRO B 69  ? 0.4490 0.4025 0.5116 0.1293  -0.0849 0.0028  69  PRO B C   
3480 O O   . PRO B 69  ? 0.4229 0.3762 0.4929 0.1352  -0.0745 0.0002  69  PRO B O   
3481 C CB  . PRO B 69  ? 0.5024 0.3658 0.4910 0.1485  -0.1141 0.0177  69  PRO B CB  
3482 C CG  . PRO B 69  ? 0.5190 0.3810 0.4939 0.1392  -0.1256 0.0283  69  PRO B CG  
3483 C CD  . PRO B 69  ? 0.4841 0.3742 0.4749 0.1066  -0.1180 0.0272  69  PRO B CD  
3484 N N   . GLN B 70  ? 0.4044 0.4077 0.4948 0.1282  -0.0858 -0.0002 70  GLN B N   
3485 C CA  . GLN B 70  ? 0.3702 0.4300 0.5055 0.1302  -0.0754 -0.0054 70  GLN B CA  
3486 C C   . GLN B 70  ? 0.3491 0.4273 0.5185 0.1007  -0.0651 -0.0109 70  GLN B C   
3487 O O   . GLN B 70  ? 0.3340 0.4528 0.5437 0.0963  -0.0564 -0.0123 70  GLN B O   
3488 C CB  . GLN B 70  ? 0.3728 0.4795 0.5251 0.1415  -0.0843 -0.0076 70  GLN B CB  
3489 C CG  . GLN B 70  ? 0.3857 0.5055 0.5403 0.1224  -0.0939 -0.0122 70  GLN B CG  
3490 C CD  . GLN B 70  ? 0.4691 0.5469 0.5757 0.1282  -0.1072 -0.0030 70  GLN B CD  
3491 O OE1 . GLN B 70  ? 0.5082 0.5314 0.5812 0.1309  -0.1082 0.0052  70  GLN B OE1 
3492 N NE2 . GLN B 70  ? 0.5794 0.6841 0.6829 0.1296  -0.1189 -0.0032 70  GLN B NE2 
3493 N N   . ALA B 71  ? 0.3738 0.4249 0.5295 0.0805  -0.0668 -0.0134 71  ALA B N   
3494 C CA  . ALA B 71  ? 0.3576 0.4195 0.5421 0.0566  -0.0593 -0.0208 71  ALA B CA  
3495 C C   . ALA B 71  ? 0.4066 0.4273 0.5645 0.0455  -0.0573 -0.0192 71  ALA B C   
3496 O O   . ALA B 71  ? 0.4148 0.4354 0.5686 0.0300  -0.0609 -0.0252 71  ALA B O   
3497 C CB  . ALA B 71  ? 0.3006 0.3971 0.5077 0.0437  -0.0670 -0.0329 71  ALA B CB  
3498 N N   . PRO B 72  ? 0.3812 0.3715 0.5203 0.0544  -0.0521 -0.0122 72  PRO B N   
3499 C CA  . PRO B 72  ? 0.4172 0.3703 0.5303 0.0439  -0.0525 -0.0106 72  PRO B CA  
3500 C C   . PRO B 72  ? 0.4313 0.3959 0.5673 0.0242  -0.0458 -0.0176 72  PRO B C   
3501 O O   . PRO B 72  ? 0.3947 0.3803 0.5645 0.0214  -0.0381 -0.0206 72  PRO B O   
3502 C CB  . PRO B 72  ? 0.4242 0.3517 0.5200 0.0602  -0.0486 -0.0058 72  PRO B CB  
3503 C CG  . PRO B 72  ? 0.3999 0.3633 0.5242 0.0740  -0.0398 -0.0046 72  PRO B CG  
3504 C CD  . PRO B 72  ? 0.3854 0.3799 0.5260 0.0756  -0.0461 -0.0069 72  PRO B CD  
3505 N N   . ALA B 73  ? 0.4391 0.3903 0.5569 0.0108  -0.0496 -0.0192 73  ALA B N   
3506 C CA  . ALA B 73  ? 0.4134 0.3731 0.5477 -0.0032 -0.0444 -0.0272 73  ALA B CA  
3507 C C   . ALA B 73  ? 0.3815 0.3209 0.5140 -0.0005 -0.0369 -0.0227 73  ALA B C   
3508 O O   . ALA B 73  ? 0.4061 0.3190 0.5119 0.0070  -0.0388 -0.0155 73  ALA B O   
3509 C CB  . ALA B 73  ? 0.4174 0.3797 0.5325 -0.0164 -0.0498 -0.0291 73  ALA B CB  
3510 N N   . THR B 74  ? 0.3610 0.3113 0.5208 -0.0056 -0.0303 -0.0278 74  THR B N   
3511 C CA  . THR B 74  ? 0.3718 0.3083 0.5313 -0.0020 -0.0232 -0.0221 74  THR B CA  
3512 C C   . THR B 74  ? 0.3969 0.3245 0.5415 -0.0109 -0.0252 -0.0260 74  THR B C   
3513 O O   . THR B 74  ? 0.3815 0.3241 0.5344 -0.0204 -0.0278 -0.0357 74  THR B O   
3514 C CB  . THR B 74  ? 0.3724 0.3226 0.5698 -0.0025 -0.0159 -0.0208 74  THR B CB  
3515 O OG1 . THR B 74  ? 0.3798 0.3433 0.5907 0.0056  -0.0120 -0.0126 74  THR B OG1 
3516 C CG2 . THR B 74  ? 0.3896 0.3280 0.5857 0.0006  -0.0094 -0.0135 74  THR B CG2 
3517 N N   . VAL B 75  ? 0.4069 0.3147 0.5297 -0.0063 -0.0247 -0.0199 75  VAL B N   
3518 C CA  . VAL B 75  ? 0.4234 0.3272 0.5354 -0.0140 -0.0265 -0.0224 75  VAL B CA  
3519 C C   . VAL B 75  ? 0.4211 0.3213 0.5396 -0.0044 -0.0199 -0.0180 75  VAL B C   
3520 O O   . VAL B 75  ? 0.4096 0.2974 0.5138 0.0078  -0.0181 -0.0114 75  VAL B O   
3521 C CB  . VAL B 75  ? 0.4418 0.3244 0.5199 -0.0201 -0.0357 -0.0192 75  VAL B CB  
3522 C CG1 . VAL B 75  ? 0.4413 0.3262 0.5124 -0.0298 -0.0380 -0.0214 75  VAL B CG1 
3523 C CG2 . VAL B 75  ? 0.4473 0.3338 0.5171 -0.0302 -0.0423 -0.0181 75  VAL B CG2 
3524 N N   . GLY B 76  ? 0.3946 0.3071 0.5326 -0.0071 -0.0170 -0.0217 76  GLY B N   
3525 C CA  . GLY B 76  ? 0.3871 0.2967 0.5295 0.0025  -0.0117 -0.0145 76  GLY B CA  
3526 C C   . GLY B 76  ? 0.4318 0.3340 0.5465 0.0036  -0.0163 -0.0148 76  GLY B C   
3527 O O   . GLY B 76  ? 0.4513 0.3554 0.5533 -0.0081 -0.0236 -0.0217 76  GLY B O   
3528 N N   . LEU B 77  ? 0.4103 0.3077 0.5161 0.0168  -0.0126 -0.0066 77  LEU B N   
3529 C CA  . LEU B 77  ? 0.4288 0.3207 0.5088 0.0196  -0.0188 -0.0091 77  LEU B CA  
3530 C C   . LEU B 77  ? 0.4103 0.3134 0.4973 0.0313  -0.0139 -0.0017 77  LEU B C   
3531 O O   . LEU B 77  ? 0.3667 0.2733 0.4633 0.0431  -0.0048 0.0112  77  LEU B O   
3532 C CB  . LEU B 77  ? 0.4473 0.3199 0.4971 0.0290  -0.0232 -0.0095 77  LEU B CB  
3533 C CG  . LEU B 77  ? 0.4364 0.3030 0.4594 0.0384  -0.0298 -0.0131 77  LEU B CG  
3534 C CD1 . LEU B 77  ? 0.4570 0.3191 0.4705 0.0202  -0.0429 -0.0231 77  LEU B CD1 
3535 C CD2 . LEU B 77  ? 0.4284 0.2775 0.4238 0.0555  -0.0333 -0.0160 77  LEU B CD2 
3536 N N   . ALA B 78  ? 0.4500 0.3624 0.5326 0.0277  -0.0202 -0.0078 78  ALA B N   
3537 C CA  . ALA B 78  ? 0.4249 0.3484 0.5082 0.0411  -0.0183 -0.0009 78  ALA B CA  
3538 C C   . ALA B 78  ? 0.4330 0.3594 0.4883 0.0419  -0.0288 -0.0087 78  ALA B C   
3539 O O   . ALA B 78  ? 0.4509 0.3783 0.4995 0.0257  -0.0385 -0.0202 78  ALA B O   
3540 C CB  . ALA B 78  ? 0.3598 0.2970 0.4710 0.0402  -0.0174 -0.0021 78  ALA B CB  
3541 N N   . PHE B 79  ? 0.4066 0.3371 0.4462 0.0596  -0.0276 -0.0016 79  PHE B N   
3542 C CA  . PHE B 79  ? 0.5039 0.4394 0.5172 0.0626  -0.0396 -0.0113 79  PHE B CA  
3543 C C   . PHE B 79  ? 0.5180 0.4795 0.5403 0.0684  -0.0423 -0.0094 79  PHE B C   
3544 O O   . PHE B 79  ? 0.5120 0.4823 0.5530 0.0795  -0.0336 0.0043  79  PHE B O   
3545 C CB  . PHE B 79  ? 0.5112 0.4411 0.4956 0.0828  -0.0389 -0.0088 79  PHE B CB  
3546 C CG  . PHE B 79  ? 0.5020 0.4067 0.4695 0.0813  -0.0421 -0.0171 79  PHE B CG  
3547 C CD1 . PHE B 79  ? 0.4914 0.3750 0.4583 0.0598  -0.0526 -0.0289 79  PHE B CD1 
3548 C CD2 . PHE B 79  ? 0.4886 0.3937 0.4402 0.1030  -0.0349 -0.0115 79  PHE B CD2 
3549 C CE1 . PHE B 79  ? 0.5065 0.3620 0.4566 0.0611  -0.0576 -0.0354 79  PHE B CE1 
3550 C CE2 . PHE B 79  ? 0.4679 0.3506 0.4036 0.1065  -0.0391 -0.0207 79  PHE B CE2 
3551 C CZ  . PHE B 79  ? 0.4938 0.3478 0.4283 0.0862  -0.0513 -0.0328 79  PHE B CZ  
3552 N N   . ARG B 80  ? 0.5121 0.4851 0.5214 0.0608  -0.0562 -0.0228 80  ARG B N   
3553 C CA  . ARG B 80  ? 0.5682 0.5711 0.5813 0.0709  -0.0607 -0.0219 80  ARG B CA  
3554 C C   . ARG B 80  ? 0.5972 0.6048 0.5928 0.0979  -0.0562 -0.0088 80  ARG B C   
3555 O O   . ARG B 80  ? 0.5977 0.5935 0.5671 0.1068  -0.0567 -0.0101 80  ARG B O   
3556 C CB  . ARG B 80  ? 0.5730 0.5920 0.5763 0.0553  -0.0781 -0.0391 80  ARG B CB  
3557 C CG  . ARG B 80  ? 0.5609 0.6193 0.5722 0.0650  -0.0839 -0.0399 80  ARG B CG  
3558 C CD  . ARG B 80  ? 0.6687 0.7459 0.6691 0.0490  -0.1028 -0.0567 80  ARG B CD  
3559 N NE  . ARG B 80  ? 0.7410 0.8273 0.7596 0.0182  -0.1070 -0.0642 80  ARG B NE  
3560 C CZ  . ARG B 80  ? 0.7094 0.8404 0.7522 0.0099  -0.1090 -0.0671 80  ARG B CZ  
3561 N NH1 . ARG B 80  ? 0.6753 0.8421 0.7272 0.0311  -0.1094 -0.0655 80  ARG B NH1 
3562 N NH2 . ARG B 80  ? 0.6814 0.8248 0.7391 -0.0186 -0.1106 -0.0708 80  ARG B NH2 
3563 N N   . ALA B 81  ? 0.6316 0.6574 0.6410 0.1132  -0.0516 0.0051  81  ALA B N   
3564 C CA  . ALA B 81  ? 0.6392 0.6736 0.6308 0.1383  -0.0466 0.0227  81  ALA B CA  
3565 C C   . ALA B 81  ? 0.6955 0.7586 0.6657 0.1500  -0.0604 0.0142  81  ALA B C   
3566 O O   . ALA B 81  ? 0.8267 0.8918 0.7659 0.1549  -0.0683 0.0028  81  ALA B O   
3567 C CB  . ALA B 81  ? 0.5897 0.6210 0.6062 0.1496  -0.0343 0.0485  81  ALA B CB  
3568 N N   . ASP B 82  ? 0.6117 0.6985 0.5973 0.1552  -0.0660 0.0155  82  ASP B N   
3569 C CA  . ASP B 82  ? 0.6904 0.8100 0.6585 0.1616  -0.0824 0.0022  82  ASP B CA  
3570 C C   . ASP B 82  ? 0.6597 0.8016 0.6498 0.1429  -0.0936 -0.0161 82  ASP B C   
3571 O O   . ASP B 82  ? 0.6762 0.8176 0.6614 0.1195  -0.1041 -0.0358 82  ASP B O   
3572 C CB  . ASP B 82  ? 0.7168 0.8592 0.6764 0.1921  -0.0809 0.0229  82  ASP B CB  
3573 C CG  . ASP B 82  ? 0.7410 0.8767 0.6733 0.2110  -0.0710 0.0418  82  ASP B CG  
3574 O OD1 . ASP B 82  ? 0.7490 0.8808 0.6534 0.2094  -0.0751 0.0271  82  ASP B OD1 
3575 O OD2 . ASP B 82  ? 0.8034 0.9386 0.7423 0.2283  -0.0596 0.0719  82  ASP B OD2 
3576 N N   . ASP B 83  ? 0.6525 0.8120 0.6691 0.1513  -0.0911 -0.0092 83  ASP B N   
3577 C CA  . ASP B 83  ? 0.6459 0.8358 0.6864 0.1357  -0.0990 -0.0258 83  ASP B CA  
3578 C C   . ASP B 83  ? 0.6419 0.8130 0.7085 0.1225  -0.0882 -0.0262 83  ASP B C   
3579 O O   . ASP B 83  ? 0.7009 0.8985 0.7866 0.1067  -0.0919 -0.0400 83  ASP B O   
3580 C CB  . ASP B 83  ? 0.6323 0.8633 0.6846 0.1588  -0.1058 -0.0229 83  ASP B CB  
3581 C CG  . ASP B 83  ? 0.7608 1.0091 0.7859 0.1802  -0.1144 -0.0165 83  ASP B CG  
3582 O OD1 . ASP B 83  ? 0.7657 1.0123 0.7648 0.1701  -0.1222 -0.0269 83  ASP B OD1 
3583 O OD2 . ASP B 83  ? 0.8251 1.0874 0.8539 0.2087  -0.1146 -0.0015 83  ASP B OD2 
3584 N N   . THR B 84  ? 0.5520 0.6837 0.6203 0.1295  -0.0753 -0.0110 84  THR B N   
3585 C CA  . THR B 84  ? 0.4889 0.6004 0.5822 0.1223  -0.0660 -0.0105 84  THR B CA  
3586 C C   . THR B 84  ? 0.4878 0.5614 0.5706 0.1096  -0.0571 -0.0050 84  THR B C   
3587 O O   . THR B 84  ? 0.5253 0.5886 0.5822 0.1121  -0.0572 -0.0001 84  THR B O   
3588 C CB  . THR B 84  ? 0.4588 0.5608 0.5718 0.1466  -0.0618 0.0039  84  THR B CB  
3589 O OG1 . THR B 84  ? 0.4345 0.5160 0.5321 0.1629  -0.0566 0.0282  84  THR B OG1 
3590 C CG2 . THR B 84  ? 0.3788 0.5219 0.5030 0.1631  -0.0722 -0.0044 84  THR B CG2 
3591 N N   . PHE B 85  ? 0.4636 0.5209 0.5660 0.0978  -0.0505 -0.0085 85  PHE B N   
3592 C CA  . PHE B 85  ? 0.4444 0.4701 0.5411 0.0865  -0.0425 -0.0041 85  PHE B CA  
3593 C C   . PHE B 85  ? 0.4223 0.4235 0.5319 0.0996  -0.0320 0.0159  85  PHE B C   
3594 O O   . PHE B 85  ? 0.4018 0.4006 0.5337 0.1106  -0.0315 0.0217  85  PHE B O   
3595 C CB  . PHE B 85  ? 0.4039 0.4296 0.5132 0.0647  -0.0425 -0.0184 85  PHE B CB  
3596 C CG  . PHE B 85  ? 0.4341 0.4714 0.5265 0.0442  -0.0513 -0.0307 85  PHE B CG  
3597 C CD1 . PHE B 85  ? 0.4128 0.4880 0.5097 0.0368  -0.0603 -0.0413 85  PHE B CD1 
3598 C CD2 . PHE B 85  ? 0.4521 0.4625 0.5257 0.0321  -0.0517 -0.0308 85  PHE B CD2 
3599 C CE1 . PHE B 85  ? 0.4614 0.5454 0.5458 0.0132  -0.0699 -0.0495 85  PHE B CE1 
3600 C CE2 . PHE B 85  ? 0.4776 0.4896 0.5363 0.0115  -0.0625 -0.0403 85  PHE B CE2 
3601 C CZ  . PHE B 85  ? 0.4721 0.5199 0.5371 -0.0003 -0.0718 -0.0486 85  PHE B CZ  
3602 N N   . GLU B 86  ? 0.4401 0.4238 0.5365 0.0987  -0.0248 0.0268  86  GLU B N   
3603 C CA  . GLU B 86  ? 0.4495 0.4142 0.5631 0.1040  -0.0140 0.0473  86  GLU B CA  
3604 C C   . GLU B 86  ? 0.4242 0.3745 0.5673 0.0903  -0.0127 0.0381  86  GLU B C   
3605 O O   . GLU B 86  ? 0.3780 0.3334 0.5207 0.0761  -0.0168 0.0184  86  GLU B O   
3606 C CB  . GLU B 86  ? 0.4003 0.3604 0.4943 0.1060  -0.0059 0.0587  86  GLU B CB  
3607 C CG  . GLU B 86  ? 0.4283 0.3777 0.5193 0.0897  -0.0059 0.0436  86  GLU B CG  
3608 C CD  . GLU B 86  ? 0.4398 0.3883 0.5061 0.0962  -0.0011 0.0480  86  GLU B CD  
3609 O OE1 . GLU B 86  ? 0.4514 0.4129 0.4974 0.1136  0.0018  0.0596  86  GLU B OE1 
3610 O OE2 . GLU B 86  ? 0.4474 0.3848 0.5135 0.0860  -0.0010 0.0389  86  GLU B OE2 
3611 N N   . ALA B 87  ? 0.4066 0.3396 0.5756 0.0944  -0.0083 0.0529  87  ALA B N   
3612 C CA  . ALA B 87  ? 0.4095 0.3270 0.6067 0.0824  -0.0083 0.0434  87  ALA B CA  
3613 C C   . ALA B 87  ? 0.3918 0.3064 0.5839 0.0685  -0.0022 0.0423  87  ALA B C   
3614 O O   . ALA B 87  ? 0.4186 0.3355 0.5960 0.0716  0.0051  0.0581  87  ALA B O   
3615 C CB  . ALA B 87  ? 0.4278 0.3214 0.6550 0.0881  -0.0076 0.0610  87  ALA B CB  
3616 N N   . LEU B 88  ? 0.3991 0.3130 0.6021 0.0557  -0.0055 0.0231  88  LEU B N   
3617 C CA  . LEU B 88  ? 0.3990 0.3101 0.6001 0.0441  -0.0013 0.0216  88  LEU B CA  
3618 C C   . LEU B 88  ? 0.3815 0.2820 0.6048 0.0435  0.0061  0.0417  88  LEU B C   
3619 O O   . LEU B 88  ? 0.3892 0.2767 0.6435 0.0404  0.0037  0.0435  88  LEU B O   
3620 C CB  . LEU B 88  ? 0.3886 0.3040 0.6001 0.0323  -0.0070 -0.0007 88  LEU B CB  
3621 C CG  . LEU B 88  ? 0.4041 0.3176 0.6166 0.0217  -0.0046 -0.0026 88  LEU B CG  
3622 C CD1 . LEU B 88  ? 0.3968 0.3128 0.5758 0.0205  -0.0041 -0.0014 88  LEU B CD1 
3623 C CD2 . LEU B 88  ? 0.3671 0.2874 0.5947 0.0126  -0.0106 -0.0228 88  LEU B CD2 
3624 N N   . CYS B 89  ? 0.4158 0.3235 0.6244 0.0464  0.0142  0.0563  89  CYS B N   
3625 C CA  . CYS B 89  ? 0.4338 0.3428 0.6643 0.0447  0.0232  0.0799  89  CYS B CA  
3626 C C   . CYS B 89  ? 0.4095 0.3329 0.6306 0.0429  0.0292  0.0803  89  CYS B C   
3627 O O   . CYS B 89  ? 0.4545 0.3880 0.6430 0.0543  0.0318  0.0803  89  CYS B O   
3628 C CB  . CYS B 89  ? 0.3923 0.3068 0.6163 0.0574  0.0299  0.1070  89  CYS B CB  
3629 S SG  . CYS B 89  ? 0.5761 0.4964 0.8346 0.0498  0.0411  0.1418  89  CYS B SG  
3630 N N   . ILE B 90  ? 0.4273 0.3519 0.6769 0.0305  0.0296  0.0791  90  ILE B N   
3631 C CA  . ILE B 90  ? 0.4232 0.3653 0.6690 0.0303  0.0342  0.0791  90  ILE B CA  
3632 C C   . ILE B 90  ? 0.4339 0.3941 0.7127 0.0247  0.0438  0.1043  90  ILE B C   
3633 O O   . ILE B 90  ? 0.3968 0.3479 0.7140 0.0093  0.0403  0.1078  90  ILE B O   
3634 C CB  . ILE B 90  ? 0.3872 0.3242 0.6369 0.0202  0.0252  0.0552  90  ILE B CB  
3635 C CG1 . ILE B 90  ? 0.4051 0.3301 0.6224 0.0226  0.0167  0.0354  90  ILE B CG1 
3636 C CG2 . ILE B 90  ? 0.3712 0.3276 0.6202 0.0225  0.0290  0.0574  90  ILE B CG2 
3637 C CD1 . ILE B 90  ? 0.3487 0.2720 0.5700 0.0116  0.0080  0.0151  90  ILE B CD1 
3638 N N   . GLU B 91  ? 0.4447 0.4324 0.7092 0.0369  0.0550  0.1212  91  GLU B N   
3639 C CA  . GLU B 91  ? 0.4090 0.4261 0.7051 0.0307  0.0663  0.1494  91  GLU B CA  
3640 C C   . GLU B 91  ? 0.4142 0.4491 0.7342 0.0206  0.0647  0.1406  91  GLU B C   
3641 O O   . GLU B 91  ? 0.4148 0.4566 0.7102 0.0318  0.0620  0.1225  91  GLU B O   
3642 C CB  . GLU B 91  ? 0.4046 0.4558 0.6748 0.0509  0.0798  0.1697  91  GLU B CB  
3643 C CG  . GLU B 91  ? 0.4508 0.5456 0.7518 0.0452  0.0942  0.2027  91  GLU B CG  
3644 C CD  . GLU B 91  ? 0.6009 0.6865 0.9336 0.0293  0.0975  0.2344  91  GLU B CD  
3645 O OE1 . GLU B 91  ? 0.5459 0.6676 0.9087 0.0192  0.1093  0.2675  91  GLU B OE1 
3646 O OE2 . GLU B 91  ? 0.6074 0.6509 0.9356 0.0272  0.0878  0.2274  91  GLU B OE2 
3647 N N   . PRO B 92  ? 0.4334 0.4728 0.8012 -0.0007 0.0637  0.1515  92  PRO B N   
3648 C CA  . PRO B 92  ? 0.3845 0.4465 0.7776 -0.0109 0.0606  0.1422  92  PRO B CA  
3649 C C   . PRO B 92  ? 0.3625 0.4769 0.7504 0.0023  0.0737  0.1570  92  PRO B C   
3650 O O   . PRO B 92  ? 0.3371 0.4792 0.7214 0.0104  0.0875  0.1840  92  PRO B O   
3651 C CB  . PRO B 92  ? 0.3275 0.3820 0.7758 -0.0382 0.0557  0.1542  92  PRO B CB  
3652 C CG  . PRO B 92  ? 0.3851 0.4259 0.8371 -0.0393 0.0624  0.1831  92  PRO B CG  
3653 C CD  . PRO B 92  ? 0.4138 0.4321 0.8154 -0.0171 0.0618  0.1703  92  PRO B CD  
3654 N N   . PHE B 93  ? 0.3319 0.4641 0.7193 0.0062  0.0689  0.1393  93  PHE B N   
3655 C CA  . PHE B 93  ? 0.2975 0.4859 0.6886 0.0191  0.0798  0.1513  93  PHE B CA  
3656 C C   . PHE B 93  ? 0.2975 0.5273 0.7445 -0.0036 0.0881  0.1804  93  PHE B C   
3657 O O   . PHE B 93  ? 0.3008 0.5080 0.7864 -0.0313 0.0809  0.1853  93  PHE B O   
3658 C CB  . PHE B 93  ? 0.3044 0.5010 0.6855 0.0289  0.0704  0.1266  93  PHE B CB  
3659 C CG  . PHE B 93  ? 0.3076 0.4623 0.6365 0.0474  0.0607  0.1015  93  PHE B CG  
3660 C CD1 . PHE B 93  ? 0.3167 0.4555 0.6028 0.0676  0.0649  0.1023  93  PHE B CD1 
3661 C CD2 . PHE B 93  ? 0.3070 0.4397 0.6300 0.0430  0.0462  0.0783  93  PHE B CD2 
3662 C CE1 . PHE B 93  ? 0.3212 0.4196 0.5629 0.0802  0.0539  0.0804  93  PHE B CE1 
3663 C CE2 . PHE B 93  ? 0.2900 0.3844 0.5671 0.0559  0.0370  0.0600  93  PHE B CE2 
3664 C CZ  . PHE B 93  ? 0.2840 0.3596 0.5225 0.0728  0.0403  0.0613  93  PHE B CZ  
3665 N N   . SER B 94  ? 0.3027 0.5953 0.7551 0.0086  0.1026  0.1997  94  SER B N   
3666 C CA  . SER B 94  ? 0.3118 0.6553 0.8199 -0.0151 0.1117  0.2312  94  SER B CA  
3667 C C   . SER B 94  ? 0.3147 0.6623 0.8682 -0.0398 0.0979  0.2167  94  SER B C   
3668 O O   . SER B 94  ? 0.3514 0.6663 0.8886 -0.0349 0.0828  0.1833  94  SER B O   
3669 C CB  . SER B 94  ? 0.3196 0.7422 0.8217 0.0070  0.1308  0.2521  94  SER B CB  
3670 O OG  . SER B 94  ? 0.3081 0.7579 0.7936 0.0310  0.1268  0.2271  94  SER B OG  
3671 N N   . SER B 95  ? 0.3278 0.7121 0.9308 -0.0662 0.1005  0.2395  95  SER B N   
3672 C CA  . SER B 95  ? 0.4066 0.7855 1.0408 -0.0893 0.0828  0.2195  95  SER B CA  
3673 C C   . SER B 95  ? 0.4320 0.8836 1.0856 -0.0916 0.0886  0.2292  95  SER B C   
3674 O O   . SER B 95  ? 0.4526 0.9471 1.1056 -0.0892 0.1042  0.2584  95  SER B O   
3675 C CB  . SER B 95  ? 0.4865 0.8086 1.1420 -0.1210 0.0690  0.2219  95  SER B CB  
3676 O OG  . SER B 95  ? 0.5643 0.8936 1.2233 -0.1287 0.0806  0.2587  95  SER B OG  
3677 N N   . PRO B 96  ? 0.4625 0.9330 1.1322 -0.0951 0.0762  0.2049  96  PRO B N   
3678 C CA  . PRO B 96  ? 0.4778 1.0213 1.1681 -0.0966 0.0808  0.2112  96  PRO B CA  
3679 C C   . PRO B 96  ? 0.5304 1.0789 1.2596 -0.1347 0.0778  0.2296  96  PRO B C   
3680 O O   . PRO B 96  ? 0.5419 1.0302 1.2802 -0.1581 0.0684  0.2326  96  PRO B O   
3681 C CB  . PRO B 96  ? 0.4119 0.9642 1.1068 -0.0890 0.0647  0.1771  96  PRO B CB  
3682 C CG  . PRO B 96  ? 0.4294 0.9081 1.1212 -0.1020 0.0477  0.1555  96  PRO B CG  
3683 C CD  . PRO B 96  ? 0.4552 0.8866 1.1218 -0.0942 0.0575  0.1696  96  PRO B CD  
3684 N N   . PRO B 97  ? 0.5919 1.2103 1.3442 -0.1404 0.0850  0.2422  97  PRO B N   
3685 C CA  . PRO B 97  ? 0.6161 1.2419 1.4103 -0.1794 0.0806  0.2589  97  PRO B CA  
3686 C C   . PRO B 97  ? 0.6297 1.2418 1.4544 -0.2033 0.0583  0.2289  97  PRO B C   
3687 O O   . PRO B 97  ? 0.7527 1.3677 1.6140 -0.2370 0.0514  0.2372  97  PRO B O   
3688 C CB  . PRO B 97  ? 0.6076 1.3214 1.4119 -0.1714 0.0983  0.2825  97  PRO B CB  
3689 C CG  . PRO B 97  ? 0.5625 1.3166 1.3412 -0.1317 0.1016  0.2597  97  PRO B CG  
3690 C CD  . PRO B 97  ? 0.5298 1.2230 1.2682 -0.1085 0.0980  0.2430  97  PRO B CD  
3691 N N   . MET C 26  ? 0.4933 0.3715 0.7844 0.0688  -0.1123 -0.1020 17  MET C N   
3692 C CA  . MET C 26  ? 0.4851 0.3455 0.7823 0.0488  -0.0900 -0.0713 17  MET C CA  
3693 C C   . MET C 26  ? 0.4720 0.3554 0.7367 0.0516  -0.0697 -0.0494 17  MET C C   
3694 O O   . MET C 26  ? 0.5017 0.3693 0.7476 0.0474  -0.0548 -0.0286 17  MET C O   
3695 C CB  . MET C 26  ? 0.5156 0.3773 0.8592 0.0263  -0.0871 -0.0712 17  MET C CB  
3696 C CG  . MET C 26  ? 0.5036 0.3629 0.8511 0.0057  -0.0602 -0.0418 17  MET C CG  
3697 S SD  . MET C 26  ? 0.7753 0.5852 1.1085 -0.0076 -0.0470 -0.0145 17  MET C SD  
3698 C CE  . MET C 26  ? 0.6833 0.5009 1.0478 -0.0400 -0.0212 0.0054  17  MET C CE  
3699 N N   . TYR C 27  ? 0.4296 0.3489 0.6896 0.0582  -0.0707 -0.0540 18  TYR C N   
3700 C CA  . TYR C 27  ? 0.4378 0.3786 0.6660 0.0655  -0.0571 -0.0387 18  TYR C CA  
3701 C C   . TYR C 27  ? 0.4408 0.4043 0.6393 0.0862  -0.0695 -0.0523 18  TYR C C   
3702 O O   . TYR C 27  ? 0.4491 0.4214 0.6543 0.0945  -0.0888 -0.0749 18  TYR C O   
3703 C CB  . TYR C 27  ? 0.4085 0.3707 0.6556 0.0561  -0.0474 -0.0292 18  TYR C CB  
3704 C CG  . TYR C 27  ? 0.3982 0.3482 0.6691 0.0353  -0.0287 -0.0145 18  TYR C CG  
3705 C CD1 . TYR C 27  ? 0.4356 0.3748 0.7469 0.0188  -0.0311 -0.0209 18  TYR C CD1 
3706 C CD2 . TYR C 27  ? 0.3772 0.3297 0.6313 0.0310  -0.0081 0.0043  18  TYR C CD2 
3707 C CE1 . TYR C 27  ? 0.4196 0.3523 0.7505 -0.0024 -0.0109 -0.0063 18  TYR C CE1 
3708 C CE2 . TYR C 27  ? 0.4202 0.3667 0.6915 0.0122  0.0104  0.0163  18  TYR C CE2 
3709 C CZ  . TYR C 27  ? 0.4519 0.3896 0.7601 -0.0049 0.0102  0.0121  18  TYR C CZ  
3710 O OH  . TYR C 27  ? 0.4611 0.3975 0.7837 -0.0254 0.0319  0.0253  18  TYR C OH  
3711 N N   . VAL C 28  ? 0.3980 0.3736 0.5637 0.0934  -0.0575 -0.0393 19  VAL C N   
3712 C CA  . VAL C 28  ? 0.4247 0.4268 0.5592 0.1096  -0.0635 -0.0468 19  VAL C CA  
3713 C C   . VAL C 28  ? 0.4229 0.4431 0.5434 0.1074  -0.0501 -0.0261 19  VAL C C   
3714 O O   . VAL C 28  ? 0.4526 0.4638 0.5842 0.0963  -0.0353 -0.0095 19  VAL C O   
3715 C CB  . VAL C 28  ? 0.4899 0.4893 0.6001 0.1217  -0.0631 -0.0551 19  VAL C CB  
3716 C CG1 . VAL C 28  ? 0.4882 0.4666 0.6157 0.1266  -0.0799 -0.0785 19  VAL C CG1 
3717 C CG2 . VAL C 28  ? 0.4464 0.4331 0.5473 0.1164  -0.0450 -0.0353 19  VAL C CG2 
3718 N N   . LYS C 29  ? 0.4366 0.4822 0.5325 0.1179  -0.0557 -0.0275 20  LYS C N   
3719 C CA  . LYS C 29  ? 0.4420 0.5013 0.5254 0.1163  -0.0461 -0.0069 20  LYS C CA  
3720 C C   . LYS C 29  ? 0.4629 0.5352 0.5117 0.1218  -0.0349 -0.0001 20  LYS C C   
3721 O O   . LYS C 29  ? 0.4692 0.5596 0.4939 0.1324  -0.0416 -0.0126 20  LYS C O   
3722 C CB  . LYS C 29  ? 0.4126 0.4897 0.4952 0.1219  -0.0620 -0.0080 20  LYS C CB  
3723 C CG  . LYS C 29  ? 0.4629 0.5476 0.5359 0.1206  -0.0549 0.0158  20  LYS C CG  
3724 C CD  . LYS C 29  ? 0.4620 0.5635 0.5277 0.1291  -0.0743 0.0172  20  LYS C CD  
3725 C CE  . LYS C 29  ? 0.3924 0.4908 0.4997 0.1271  -0.0889 0.0057  20  LYS C CE  
3726 N NZ  . LYS C 29  ? 0.5131 0.6279 0.6137 0.1369  -0.1090 0.0110  20  LYS C NZ  
3727 N N   . LEU C 30  ? 0.4333 0.4999 0.4819 0.1144  -0.0175 0.0174  21  LEU C N   
3728 C CA  . LEU C 30  ? 0.4459 0.5269 0.4689 0.1164  -0.0050 0.0254  21  LEU C CA  
3729 C C   . LEU C 30  ? 0.4272 0.5158 0.4448 0.1117  0.0008  0.0466  21  LEU C C   
3730 O O   . LEU C 30  ? 0.4742 0.5493 0.5129 0.1035  0.0074  0.0581  21  LEU C O   
3731 C CB  . LEU C 30  ? 0.4353 0.5042 0.4642 0.1116  0.0085  0.0275  21  LEU C CB  
3732 C CG  . LEU C 30  ? 0.4125 0.4605 0.4543 0.1129  0.0026  0.0145  21  LEU C CG  
3733 C CD1 . LEU C 30  ? 0.3895 0.4291 0.4295 0.1101  0.0142  0.0199  21  LEU C CD1 
3734 C CD2 . LEU C 30  ? 0.4202 0.4757 0.4530 0.1257  -0.0117 -0.0073 21  LEU C CD2 
3735 N N   . ILE C 31  ? 0.4598 0.5697 0.4493 0.1167  -0.0013 0.0517  22  ILE C N   
3736 C CA  . ILE C 31  ? 0.4795 0.5926 0.4608 0.1125  0.0016  0.0753  22  ILE C CA  
3737 C C   . ILE C 31  ? 0.5136 0.6362 0.4808 0.1058  0.0205  0.0873  22  ILE C C   
3738 O O   . ILE C 31  ? 0.5012 0.6455 0.4466 0.1093  0.0262  0.0782  22  ILE C O   
3739 C CB  . ILE C 31  ? 0.4939 0.6236 0.4499 0.1208  -0.0143 0.0781  22  ILE C CB  
3740 C CG1 . ILE C 31  ? 0.5155 0.6390 0.4917 0.1271  -0.0348 0.0622  22  ILE C CG1 
3741 C CG2 . ILE C 31  ? 0.4781 0.6044 0.4262 0.1165  -0.0133 0.1070  22  ILE C CG2 
3742 C CD1 . ILE C 31  ? 0.5181 0.6604 0.4747 0.1378  -0.0484 0.0386  22  ILE C CD1 
3743 N N   . SER C 32  ? 0.4852 0.5937 0.4687 0.0963  0.0299  0.1049  23  SER C N   
3744 C CA  . SER C 32  ? 0.4856 0.6012 0.4636 0.0873  0.0474  0.1164  23  SER C CA  
3745 C C   . SER C 32  ? 0.5064 0.6343 0.4583 0.0840  0.0490  0.1385  23  SER C C   
3746 O O   . SER C 32  ? 0.4988 0.6277 0.4348 0.0900  0.0350  0.1469  23  SER C O   
3747 C CB  . SER C 32  ? 0.4508 0.5453 0.4603 0.0783  0.0556  0.1225  23  SER C CB  
3748 O OG  . SER C 32  ? 0.4842 0.5634 0.5052 0.0758  0.0499  0.1407  23  SER C OG  
3749 N N   . SER C 33  ? 0.5252 0.6633 0.4725 0.0735  0.0661  0.1488  24  SER C N   
3750 C CA  . SER C 33  ? 0.5273 0.6777 0.4477 0.0667  0.0715  0.1731  24  SER C CA  
3751 C C   . SER C 33  ? 0.5152 0.6380 0.4422 0.0646  0.0605  0.1994  24  SER C C   
3752 O O   . SER C 33  ? 0.4966 0.6246 0.3937 0.0664  0.0527  0.2190  24  SER C O   
3753 C CB  . SER C 33  ? 0.5152 0.6793 0.4404 0.0524  0.0933  0.1790  24  SER C CB  
3754 O OG  . SER C 33  ? 0.4825 0.6205 0.4439 0.0431  0.0982  0.1846  24  SER C OG  
3755 N N   . ASP C 34  ? 0.4937 0.5882 0.4591 0.0616  0.0590  0.1998  25  ASP C N   
3756 C CA  . ASP C 34  ? 0.4929 0.5595 0.4738 0.0615  0.0475  0.2214  25  ASP C CA  
3757 C C   . ASP C 34  ? 0.5007 0.5603 0.4885 0.0761  0.0253  0.2130  25  ASP C C   
3758 O O   . ASP C 34  ? 0.5039 0.5412 0.5138 0.0793  0.0131  0.2248  25  ASP C O   
3759 C CB  . ASP C 34  ? 0.4718 0.5150 0.4953 0.0525  0.0563  0.2211  25  ASP C CB  
3760 C CG  . ASP C 34  ? 0.5212 0.5645 0.5715 0.0559  0.0595  0.1918  25  ASP C CG  
3761 O OD1 . ASP C 34  ? 0.5156 0.5786 0.5515 0.0587  0.0644  0.1737  25  ASP C OD1 
3762 O OD2 . ASP C 34  ? 0.4903 0.5143 0.5759 0.0561  0.0569  0.1870  25  ASP C OD2 
3763 N N   . GLY C 35  ? 0.4850 0.5634 0.4588 0.0851  0.0190  0.1912  26  GLY C N   
3764 C CA  . GLY C 35  ? 0.5039 0.5822 0.4798 0.0977  -0.0032 0.1833  26  GLY C CA  
3765 C C   . GLY C 35  ? 0.5148 0.5806 0.5340 0.1005  -0.0082 0.1634  26  GLY C C   
3766 O O   . GLY C 35  ? 0.5011 0.5664 0.5324 0.1095  -0.0270 0.1573  26  GLY C O   
3767 N N   . HIS C 36  ? 0.4873 0.5455 0.5301 0.0926  0.0079  0.1533  27  HIS C N   
3768 C CA  . HIS C 36  ? 0.4442 0.4954 0.5218 0.0932  0.0067  0.1341  27  HIS C CA  
3769 C C   . HIS C 36  ? 0.4792 0.5421 0.5459 0.0976  0.0016  0.1138  27  HIS C C   
3770 O O   . HIS C 36  ? 0.4855 0.5604 0.5242 0.0984  0.0069  0.1089  27  HIS C O   
3771 C CB  . HIS C 36  ? 0.4398 0.4821 0.5384 0.0836  0.0253  0.1297  27  HIS C CB  
3772 C CG  . HIS C 36  ? 0.4257 0.4526 0.5550 0.0808  0.0268  0.1388  27  HIS C CG  
3773 N ND1 . HIS C 36  ? 0.4432 0.4643 0.6109 0.0810  0.0266  0.1264  27  HIS C ND1 
3774 C CD2 . HIS C 36  ? 0.4326 0.4485 0.5628 0.0773  0.0288  0.1577  27  HIS C CD2 
3775 C CE1 . HIS C 36  ? 0.4253 0.4335 0.6174 0.0801  0.0273  0.1344  27  HIS C CE1 
3776 N NE2 . HIS C 36  ? 0.4168 0.4184 0.5875 0.0776  0.0277  0.1544  27  HIS C NE2 
3777 N N   . GLU C 37  ? 0.4483 0.5085 0.5410 0.1004  -0.0089 0.1006  28  GLU C N   
3778 C CA  . GLU C 37  ? 0.4531 0.5188 0.5440 0.1028  -0.0150 0.0806  28  GLU C CA  
3779 C C   . GLU C 37  ? 0.3816 0.4360 0.4976 0.0939  -0.0022 0.0707  28  GLU C C   
3780 O O   . GLU C 37  ? 0.3918 0.4402 0.5389 0.0886  0.0028  0.0717  28  GLU C O   
3781 C CB  . GLU C 37  ? 0.4057 0.4787 0.5082 0.1106  -0.0373 0.0723  28  GLU C CB  
3782 C CG  . GLU C 37  ? 0.4844 0.5712 0.5513 0.1204  -0.0514 0.0818  28  GLU C CG  
3783 C CD  . GLU C 37  ? 0.5611 0.6576 0.6383 0.1298  -0.0768 0.0732  28  GLU C CD  
3784 O OE1 . GLU C 37  ? 0.5692 0.6623 0.6881 0.1274  -0.0824 0.0589  28  GLU C OE1 
3785 O OE2 . GLU C 37  ? 0.5347 0.6447 0.5781 0.1390  -0.0909 0.0810  28  GLU C OE2 
3786 N N   . PHE C 38  ? 0.3873 0.4398 0.4891 0.0929  0.0031  0.0612  29  PHE C N   
3787 C CA  . PHE C 38  ? 0.3685 0.4083 0.4864 0.0845  0.0139  0.0553  29  PHE C CA  
3788 C C   . PHE C 38  ? 0.3879 0.4221 0.5116 0.0858  0.0030  0.0403  29  PHE C C   
3789 O O   . PHE C 38  ? 0.4650 0.5029 0.5680 0.0939  -0.0053 0.0315  29  PHE C O   
3790 C CB  . PHE C 38  ? 0.3595 0.3970 0.4586 0.0823  0.0284  0.0595  29  PHE C CB  
3791 C CG  . PHE C 38  ? 0.3881 0.4292 0.4881 0.0786  0.0395  0.0719  29  PHE C CG  
3792 C CD1 . PHE C 38  ? 0.3346 0.3695 0.4580 0.0708  0.0498  0.0738  29  PHE C CD1 
3793 C CD2 . PHE C 38  ? 0.3603 0.4121 0.4399 0.0820  0.0400  0.0809  29  PHE C CD2 
3794 C CE1 . PHE C 38  ? 0.3715 0.4075 0.5009 0.0678  0.0582  0.0819  29  PHE C CE1 
3795 C CE2 . PHE C 38  ? 0.3662 0.4172 0.4514 0.0767  0.0494  0.0929  29  PHE C CE2 
3796 C CZ  . PHE C 38  ? 0.3862 0.4277 0.4980 0.0703  0.0574  0.0923  29  PHE C CZ  
3797 N N   . ILE C 39  ? 0.3792 0.4062 0.5341 0.0776  0.0028  0.0357  30  ILE C N   
3798 C CA  . ILE C 39  ? 0.3731 0.3915 0.5420 0.0754  -0.0076 0.0220  30  ILE C CA  
3799 C C   . ILE C 39  ? 0.4027 0.4018 0.5762 0.0642  0.0058  0.0257  30  ILE C C   
3800 O O   . ILE C 39  ? 0.3511 0.3492 0.5417 0.0529  0.0199  0.0328  30  ILE C O   
3801 C CB  . ILE C 39  ? 0.3353 0.3628 0.5391 0.0729  -0.0190 0.0141  30  ILE C CB  
3802 C CG1 . ILE C 39  ? 0.3263 0.3718 0.5164 0.0865  -0.0355 0.0132  30  ILE C CG1 
3803 C CG2 . ILE C 39  ? 0.3381 0.3554 0.5634 0.0668  -0.0281 -0.0006 30  ILE C CG2 
3804 C CD1 . ILE C 39  ? 0.3477 0.4056 0.5710 0.0876  -0.0507 0.0050  30  ILE C CD1 
3805 N N   . VAL C 40  ? 0.3876 0.3726 0.5437 0.0685  0.0012  0.0209  31  VAL C N   
3806 C CA  . VAL C 40  ? 0.3932 0.3563 0.5446 0.0611  0.0103  0.0277  31  VAL C CA  
3807 C C   . VAL C 40  ? 0.4186 0.3603 0.5808 0.0607  -0.0035 0.0169  31  VAL C C   
3808 O O   . VAL C 40  ? 0.4515 0.3984 0.6155 0.0708  -0.0202 0.0006  31  VAL C O   
3809 C CB  . VAL C 40  ? 0.4160 0.3797 0.5357 0.0695  0.0165  0.0335  31  VAL C CB  
3810 C CG1 . VAL C 40  ? 0.4399 0.4206 0.5540 0.0670  0.0308  0.0435  31  VAL C CG1 
3811 C CG2 . VAL C 40  ? 0.4378 0.4108 0.5402 0.0854  0.0035  0.0208  31  VAL C CG2 
3812 N N   . LYS C 41  ? 0.4313 0.3480 0.5996 0.0488  0.0031  0.0262  32  LYS C N   
3813 C CA  . LYS C 41  ? 0.4604 0.3486 0.6398 0.0478  -0.0105 0.0189  32  LYS C CA  
3814 C C   . LYS C 41  ? 0.4881 0.3721 0.6462 0.0679  -0.0251 0.0060  32  LYS C C   
3815 O O   . LYS C 41  ? 0.4714 0.3625 0.6027 0.0778  -0.0198 0.0113  32  LYS C O   
3816 C CB  . LYS C 41  ? 0.4614 0.3203 0.6422 0.0319  0.0003  0.0376  32  LYS C CB  
3817 C CG  . LYS C 41  ? 0.5086 0.3659 0.7241 0.0099  0.0085  0.0415  32  LYS C CG  
3818 C CD  . LYS C 41  ? 0.5804 0.4188 0.7896 -0.0088 0.0263  0.0649  32  LYS C CD  
3819 C CE  . LYS C 41  ? 0.5845 0.4350 0.8301 -0.0322 0.0406  0.0674  32  LYS C CE  
3820 N NZ  . LYS C 41  ? 0.6390 0.4694 0.8774 -0.0533 0.0581  0.0911  32  LYS C NZ  
3821 N N   . ARG C 42  ? 0.4951 0.3712 0.6687 0.0743  -0.0439 -0.0143 33  ARG C N   
3822 C CA  . ARG C 42  ? 0.5027 0.3777 0.6612 0.0945  -0.0583 -0.0322 33  ARG C CA  
3823 C C   . ARG C 42  ? 0.5021 0.3484 0.6477 0.0986  -0.0575 -0.0215 33  ARG C C   
3824 O O   . ARG C 42  ? 0.4933 0.3513 0.6180 0.1153  -0.0596 -0.0278 33  ARG C O   
3825 C CB  . ARG C 42  ? 0.5044 0.3714 0.6876 0.0988  -0.0796 -0.0587 33  ARG C CB  
3826 C CG  . ARG C 42  ? 0.4894 0.3543 0.6636 0.1204  -0.0963 -0.0835 33  ARG C CG  
3827 C CD  . ARG C 42  ? 0.5339 0.3958 0.7342 0.1244  -0.1178 -0.1140 33  ARG C CD  
3828 N NE  . ARG C 42  ? 0.5610 0.4612 0.7410 0.1448  -0.1266 -0.1403 33  ARG C NE  
3829 C CZ  . ARG C 42  ? 0.5839 0.5202 0.7567 0.1467  -0.1298 -0.1500 33  ARG C CZ  
3830 N NH1 . ARG C 42  ? 0.5402 0.4785 0.7328 0.1315  -0.1292 -0.1414 33  ARG C NH1 
3831 N NH2 . ARG C 42  ? 0.6681 0.6412 0.8127 0.1645  -0.1338 -0.1684 33  ARG C NH2 
3832 N N   . GLU C 43  ? 0.5097 0.3201 0.6676 0.0831  -0.0544 -0.0042 34  GLU C N   
3833 C CA  . GLU C 43  ? 0.5284 0.3079 0.6715 0.0870  -0.0560 0.0102  34  GLU C CA  
3834 C C   . GLU C 43  ? 0.5316 0.3328 0.6437 0.0912  -0.0411 0.0248  34  GLU C C   
3835 O O   . GLU C 43  ? 0.5510 0.3445 0.6462 0.1052  -0.0472 0.0258  34  GLU C O   
3836 C CB  . GLU C 43  ? 0.5699 0.3087 0.7278 0.0655  -0.0526 0.0316  34  GLU C CB  
3837 C CG  . GLU C 43  ? 0.6568 0.3621 0.7923 0.0676  -0.0535 0.0542  34  GLU C CG  
3838 C CD  . GLU C 43  ? 0.7311 0.4077 0.8680 0.0413  -0.0405 0.0849  34  GLU C CD  
3839 O OE1 . GLU C 43  ? 0.7930 0.4471 0.9038 0.0412  -0.0388 0.1083  34  GLU C OE1 
3840 O OE2 . GLU C 43  ? 0.7626 0.4418 0.9262 0.0207  -0.0318 0.0857  34  GLU C OE2 
3841 N N   . HIS C 44  ? 0.5120 0.3400 0.6200 0.0795  -0.0229 0.0346  35  HIS C N   
3842 C CA  . HIS C 44  ? 0.5021 0.3521 0.5853 0.0828  -0.0094 0.0447  35  HIS C CA  
3843 C C   . HIS C 44  ? 0.4821 0.3618 0.5537 0.1016  -0.0142 0.0278  35  HIS C C   
3844 O O   . HIS C 44  ? 0.4932 0.3797 0.5478 0.1119  -0.0137 0.0288  35  HIS C O   
3845 C CB  . HIS C 44  ? 0.4748 0.3446 0.5627 0.0664  0.0098  0.0555  35  HIS C CB  
3846 C CG  . HIS C 44  ? 0.4914 0.3405 0.5870 0.0465  0.0200  0.0728  35  HIS C CG  
3847 N ND1 . HIS C 44  ? 0.5421 0.4088 0.6408 0.0320  0.0393  0.0823  35  HIS C ND1 
3848 C CD2 . HIS C 44  ? 0.4939 0.3068 0.5951 0.0378  0.0144  0.0828  35  HIS C CD2 
3849 C CE1 . HIS C 44  ? 0.5007 0.3478 0.6047 0.0145  0.0473  0.0968  35  HIS C CE1 
3850 N NE2 . HIS C 44  ? 0.4721 0.2845 0.5770 0.0165  0.0326  0.0996  35  HIS C NE2 
3851 N N   . ALA C 45  ? 0.4925 0.3926 0.5732 0.1059  -0.0190 0.0119  36  ALA C N   
3852 C CA  . ALA C 45  ? 0.4592 0.3915 0.5266 0.1212  -0.0208 -0.0027 36  ALA C CA  
3853 C C   . ALA C 45  ? 0.4780 0.4042 0.5408 0.1393  -0.0341 -0.0183 36  ALA C C   
3854 O O   . ALA C 45  ? 0.4606 0.4153 0.5110 0.1510  -0.0313 -0.0273 36  ALA C O   
3855 C CB  . ALA C 45  ? 0.4239 0.3765 0.4977 0.1226  -0.0262 -0.0158 36  ALA C CB  
3856 N N   . LEU C 46  ? 0.4735 0.3632 0.5498 0.1416  -0.0486 -0.0225 37  LEU C N   
3857 C CA  . LEU C 46  ? 0.5196 0.3988 0.5972 0.1612  -0.0644 -0.0389 37  LEU C CA  
3858 C C   . LEU C 46  ? 0.4882 0.3682 0.5507 0.1678  -0.0605 -0.0275 37  LEU C C   
3859 O O   . LEU C 46  ? 0.5337 0.4150 0.5980 0.1871  -0.0728 -0.0432 37  LEU C O   
3860 C CB  . LEU C 46  ? 0.5376 0.3693 0.6366 0.1605  -0.0822 -0.0426 37  LEU C CB  
3861 C CG  . LEU C 46  ? 0.5757 0.4085 0.6954 0.1597  -0.0930 -0.0649 37  LEU C CG  
3862 C CD1 . LEU C 46  ? 0.5672 0.3494 0.7133 0.1601  -0.1128 -0.0716 37  LEU C CD1 
3863 C CD2 . LEU C 46  ? 0.5384 0.4149 0.6502 0.1781  -0.0971 -0.0948 37  LEU C CD2 
3864 N N   . THR C 47  ? 0.4630 0.3445 0.5130 0.1534  -0.0449 -0.0034 38  THR C N   
3865 C CA  . THR C 47  ? 0.4504 0.3414 0.4851 0.1595  -0.0411 0.0046  38  THR C CA  
3866 C C   . THR C 47  ? 0.4466 0.3824 0.4788 0.1735  -0.0382 -0.0148 38  THR C C   
3867 O O   . THR C 47  ? 0.4497 0.3955 0.4784 0.1865  -0.0432 -0.0201 38  THR C O   
3868 C CB  . THR C 47  ? 0.5275 0.4215 0.5503 0.1406  -0.0229 0.0281  38  THR C CB  
3869 O OG1 . THR C 47  ? 0.5467 0.4048 0.5733 0.1252  -0.0223 0.0453  38  THR C OG1 
3870 C CG2 . THR C 47  ? 0.4680 0.3709 0.4745 0.1464  -0.0212 0.0352  38  THR C CG2 
3871 N N   . SER C 48  ? 0.4643 0.3797 0.5423 0.1644  -0.0975 -0.0359 39  SER C N   
3872 C CA  . SER C 48  ? 0.4300 0.4140 0.5508 0.1665  -0.0933 -0.0515 39  SER C CA  
3873 C C   . SER C 48  ? 0.4441 0.4339 0.5526 0.1807  -0.1020 -0.0691 39  SER C C   
3874 O O   . SER C 48  ? 0.4504 0.4270 0.5434 0.1703  -0.0977 -0.0602 39  SER C O   
3875 C CB  . SER C 48  ? 0.3499 0.3729 0.5007 0.1396  -0.0697 -0.0321 39  SER C CB  
3876 O OG  . SER C 48  ? 0.3386 0.4118 0.5141 0.1407  -0.0596 -0.0440 39  SER C OG  
3877 N N   . GLY C 49  ? 0.4229 0.4365 0.5411 0.2061  -0.1157 -0.0980 40  GLY C N   
3878 C CA  . GLY C 49  ? 0.4402 0.4665 0.5496 0.2215  -0.1239 -0.1166 40  GLY C CA  
3879 C C   . GLY C 49  ? 0.4167 0.4955 0.5548 0.2035  -0.1030 -0.1104 40  GLY C C   
3880 O O   . GLY C 49  ? 0.4395 0.5145 0.5597 0.2075  -0.1059 -0.1131 40  GLY C O   
3881 N N   . THR C 50  ? 0.4123 0.5353 0.5903 0.1856  -0.0807 -0.1026 41  THR C N   
3882 C CA  . THR C 50  ? 0.3925 0.5538 0.5852 0.1717  -0.0557 -0.0931 41  THR C CA  
3883 C C   . THR C 50  ? 0.4263 0.5584 0.5878 0.1606  -0.0531 -0.0686 41  THR C C   
3884 O O   . THR C 50  ? 0.4791 0.6221 0.6269 0.1666  -0.0515 -0.0711 41  THR C O   
3885 C CB  . THR C 50  ? 0.3358 0.5327 0.5690 0.1534  -0.0284 -0.0876 41  THR C CB  
3886 O OG1 . THR C 50  ? 0.3338 0.5693 0.6074 0.1636  -0.0314 -0.1202 41  THR C OG1 
3887 C CG2 . THR C 50  ? 0.3359 0.5560 0.5690 0.1414  0.0033  -0.0730 41  THR C CG2 
3888 N N   . ILE C 51  ? 0.3931 0.4917 0.5450 0.1465  -0.0540 -0.0486 42  ILE C N   
3889 C CA  . ILE C 51  ? 0.4366 0.5138 0.5669 0.1365  -0.0540 -0.0331 42  ILE C CA  
3890 C C   . ILE C 51  ? 0.4892 0.5365 0.5949 0.1464  -0.0730 -0.0476 42  ILE C C   
3891 O O   . ILE C 51  ? 0.4864 0.5399 0.5832 0.1462  -0.0744 -0.0499 42  ILE C O   
3892 C CB  . ILE C 51  ? 0.4294 0.4798 0.5589 0.1197  -0.0506 -0.0133 42  ILE C CB  
3893 C CG1 . ILE C 51  ? 0.3833 0.4610 0.5323 0.1090  -0.0298 0.0026  42  ILE C CG1 
3894 C CG2 . ILE C 51  ? 0.4222 0.4485 0.5352 0.1099  -0.0551 -0.0074 42  ILE C CG2 
3895 C CD1 . ILE C 51  ? 0.3497 0.4053 0.5033 0.0974  -0.0289 0.0168  42  ILE C CD1 
3896 N N   . LYS C 52  ? 0.5121 0.5233 0.6029 0.1582  -0.0884 -0.0599 43  LYS C N   
3897 C CA  . LYS C 52  ? 0.5438 0.5164 0.6052 0.1693  -0.1040 -0.0750 43  LYS C CA  
3898 C C   . LYS C 52  ? 0.5498 0.5613 0.6154 0.1820  -0.1071 -0.0905 43  LYS C C   
3899 O O   . LYS C 52  ? 0.5654 0.5675 0.6198 0.1797  -0.1118 -0.0960 43  LYS C O   
3900 C CB  . LYS C 52  ? 0.5734 0.5017 0.6087 0.1905  -0.1195 -0.0877 43  LYS C CB  
3901 C CG  . LYS C 52  ? 0.6579 0.5261 0.6502 0.2038  -0.1337 -0.1016 43  LYS C CG  
3902 C CD  . LYS C 52  ? 0.7155 0.5053 0.6613 0.2185  -0.1417 -0.1010 43  LYS C CD  
3903 C CE  . LYS C 52  ? 0.9341 0.6400 0.8380 0.2049  -0.1353 -0.0958 43  LYS C CE  
3904 N NZ  . LYS C 52  ? 0.9616 0.5740 0.8072 0.2165  -0.1340 -0.0887 43  LYS C NZ  
3905 N N   . ALA C 53  ? 0.5138 0.5735 0.5995 0.1947  -0.1023 -0.0998 44  ALA C N   
3906 C CA  . ALA C 53  ? 0.4646 0.5637 0.5526 0.2081  -0.1008 -0.1134 44  ALA C CA  
3907 C C   . ALA C 53  ? 0.5137 0.6332 0.6005 0.1979  -0.0869 -0.0989 44  ALA C C   
3908 O O   . ALA C 53  ? 0.5576 0.6818 0.6293 0.2086  -0.0949 -0.1093 44  ALA C O   
3909 C CB  . ALA C 53  ? 0.4304 0.5810 0.5470 0.2185  -0.0902 -0.1267 44  ALA C CB  
3910 N N   . MET C 54  ? 0.5126 0.6429 0.6115 0.1812  -0.0681 -0.0771 45  MET C N   
3911 C CA  . MET C 54  ? 0.5035 0.6525 0.5924 0.1801  -0.0551 -0.0647 45  MET C CA  
3912 C C   . MET C 54  ? 0.5376 0.6661 0.6122 0.1783  -0.0720 -0.0691 45  MET C C   
3913 O O   . MET C 54  ? 0.5697 0.7160 0.6299 0.1919  -0.0752 -0.0764 45  MET C O   
3914 C CB  . MET C 54  ? 0.4642 0.6199 0.5628 0.1652  -0.0321 -0.0411 45  MET C CB  
3915 C CG  . MET C 54  ? 0.3988 0.5817 0.5167 0.1640  -0.0076 -0.0406 45  MET C CG  
3916 S SD  . MET C 54  ? 0.5854 0.7637 0.7162 0.1427  0.0192  -0.0150 45  MET C SD  
3917 C CE  . MET C 54  ? 0.4758 0.6904 0.6359 0.1397  0.0525  -0.0256 45  MET C CE  
3918 N N   . LEU C 55  ? 0.5426 0.6343 0.6216 0.1624  -0.0816 -0.0679 46  LEU C N   
3919 C CA  . LEU C 55  ? 0.5464 0.6209 0.6227 0.1548  -0.0934 -0.0783 46  LEU C CA  
3920 C C   . LEU C 55  ? 0.6200 0.6836 0.6856 0.1673  -0.1106 -0.1044 46  LEU C C   
3921 O O   . LEU C 55  ? 0.6482 0.7102 0.7174 0.1635  -0.1198 -0.1205 46  LEU C O   
3922 C CB  . LEU C 55  ? 0.5629 0.5951 0.6454 0.1319  -0.0920 -0.0706 46  LEU C CB  
3923 C CG  . LEU C 55  ? 0.5368 0.5772 0.6303 0.1184  -0.0780 -0.0471 46  LEU C CG  
3924 C CD1 . LEU C 55  ? 0.5617 0.5555 0.6560 0.0989  -0.0761 -0.0416 46  LEU C CD1 
3925 C CD2 . LEU C 55  ? 0.5451 0.6201 0.6432 0.1198  -0.0753 -0.0452 46  LEU C CD2 
3926 N N   . SER C 56  ? 0.5895 0.6483 0.6451 0.1831  -0.1159 -0.1130 47  SER C N   
3927 C CA  . SER C 56  ? 0.5735 0.6196 0.6144 0.1988  -0.1330 -0.1380 47  SER C CA  
3928 C C   . SER C 56  ? 0.5805 0.6747 0.6161 0.2243  -0.1332 -0.1468 47  SER C C   
3929 O O   . SER C 56  ? 0.5614 0.6512 0.5848 0.2428  -0.1459 -0.1658 47  SER C O   
3930 C CB  . SER C 56  ? 0.6274 0.6224 0.6509 0.2037  -0.1423 -0.1454 47  SER C CB  
3931 O OG  . SER C 56  ? 0.7088 0.6452 0.7247 0.1831  -0.1393 -0.1380 47  SER C OG  
3932 N N   . GLY C 57  ? 0.5804 0.7155 0.6191 0.2279  -0.1176 -0.1333 48  GLY C N   
3933 C CA  . GLY C 57  ? 0.5510 0.7249 0.5770 0.2523  -0.1110 -0.1390 48  GLY C CA  
3934 C C   . GLY C 57  ? 0.5526 0.7315 0.5621 0.2714  -0.1307 -0.1621 48  GLY C C   
3935 O O   . GLY C 57  ? 0.5473 0.7055 0.5620 0.2621  -0.1472 -0.1746 48  GLY C O   
3936 N N   . PRO C 58  ? 0.5639 0.7719 0.5559 0.2981  -0.1280 -0.1711 49  PRO C N   
3937 C CA  . PRO C 58  ? 0.5969 0.8114 0.5717 0.3210  -0.1499 -0.1967 49  PRO C CA  
3938 C C   . PRO C 58  ? 0.6139 0.8408 0.5795 0.3276  -0.1549 -0.1982 49  PRO C C   
3939 O O   . PRO C 58  ? 0.6271 0.8588 0.5914 0.3192  -0.1386 -0.1763 49  PRO C O   
3940 C CB  . PRO C 58  ? 0.5960 0.8415 0.5511 0.3495  -0.1394 -0.2013 49  PRO C CB  
3941 C CG  . PRO C 58  ? 0.5790 0.8405 0.5388 0.3399  -0.1045 -0.1748 49  PRO C CG  
3942 C CD  . PRO C 58  ? 0.5457 0.7829 0.5350 0.3079  -0.1027 -0.1615 49  PRO C CD  
3943 N N   . GLY C 59  ? 0.6645 0.8966 0.6240 0.3452  -0.1802 -0.2284 50  GLY C N   
3944 C CA  . GLY C 59  ? 0.6791 0.9291 0.6356 0.3570  -0.1942 -0.2435 50  GLY C CA  
3945 C C   . GLY C 59  ? 0.6717 0.9088 0.6621 0.3248  -0.1967 -0.2429 50  GLY C C   
3946 O O   . GLY C 59  ? 0.6709 0.9176 0.6810 0.3236  -0.2168 -0.2727 50  GLY C O   
3947 N N   . ASN C 67  ? 0.4474 0.6482 0.5912 0.1383  -0.1148 -0.1209 58  ASN C N   
3948 C CA  . ASN C 67  ? 0.5526 0.7312 0.6654 0.1472  -0.1040 -0.0942 58  ASN C CA  
3949 C C   . ASN C 67  ? 0.5437 0.7075 0.6428 0.1414  -0.0846 -0.0568 58  ASN C C   
3950 O O   . ASN C 67  ? 0.4383 0.5852 0.5557 0.1181  -0.0778 -0.0466 58  ASN C O   
3951 C CB  . ASN C 67  ? 0.5516 0.6952 0.6745 0.1295  -0.1040 -0.1005 58  ASN C CB  
3952 C CG  . ASN C 67  ? 0.7129 0.8645 0.8183 0.1522  -0.1141 -0.1151 58  ASN C CG  
3953 O OD1 . ASN C 67  ? 0.7726 0.9477 0.8513 0.1796  -0.1127 -0.1083 58  ASN C OD1 
3954 N ND2 . ASN C 67  ? 0.7332 0.8592 0.8482 0.1419  -0.1220 -0.1348 58  ASN C ND2 
3955 N N   . GLU C 68  ? 0.5073 0.6751 0.5738 0.1620  -0.0734 -0.0378 59  GLU C N   
3956 C CA  . GLU C 68  ? 0.4760 0.6310 0.5299 0.1575  -0.0531 -0.0066 59  GLU C CA  
3957 C C   . GLU C 68  ? 0.5248 0.6732 0.5601 0.1651  -0.0341 0.0084  59  GLU C C   
3958 O O   . GLU C 68  ? 0.5216 0.6805 0.5429 0.1821  -0.0364 -0.0031 59  GLU C O   
3959 C CB  . GLU C 68  ? 0.5052 0.6725 0.5338 0.1769  -0.0529 -0.0007 59  GLU C CB  
3960 C CG  . GLU C 68  ? 0.5065 0.6811 0.4857 0.2136  -0.0485 0.0005  59  GLU C CG  
3961 C CD  . GLU C 68  ? 0.5855 0.7621 0.5263 0.2402  -0.0496 0.0064  59  GLU C CD  
3962 O OE1 . GLU C 68  ? 0.5730 0.7677 0.5373 0.2363  -0.0673 -0.0090 59  GLU C OE1 
3963 O OE2 . GLU C 68  ? 0.6253 0.7828 0.5101 0.2660  -0.0309 0.0253  59  GLU C OE2 
3964 N N   . VAL C 69  ? 0.5146 0.6483 0.5538 0.1516  -0.0142 0.0312  60  VAL C N   
3965 C CA  . VAL C 69  ? 0.5148 0.6467 0.5522 0.1508  0.0079  0.0401  60  VAL C CA  
3966 C C   . VAL C 69  ? 0.4775 0.5964 0.4957 0.1496  0.0356  0.0647  60  VAL C C   
3967 O O   . VAL C 69  ? 0.4834 0.5899 0.5091 0.1375  0.0357  0.0768  60  VAL C O   
3968 C CB  . VAL C 69  ? 0.5049 0.6312 0.5791 0.1319  0.0033  0.0332  60  VAL C CB  
3969 C CG1 . VAL C 69  ? 0.5139 0.6496 0.5981 0.1300  0.0266  0.0355  60  VAL C CG1 
3970 C CG2 . VAL C 69  ? 0.5016 0.6277 0.5832 0.1357  -0.0204 0.0101  60  VAL C CG2 
3971 N N   . ASN C 70  ? 0.5194 0.6363 0.5103 0.1617  0.0618  0.0720  61  ASN C N   
3972 C CA  . ASN C 70  ? 0.5465 0.6393 0.5113 0.1599  0.0951  0.0956  61  ASN C CA  
3973 C C   . ASN C 70  ? 0.5741 0.6700 0.5745 0.1371  0.1232  0.0957  61  ASN C C   
3974 O O   . ASN C 70  ? 0.6111 0.7251 0.6212 0.1398  0.1332  0.0825  61  ASN C O   
3975 C CB  . ASN C 70  ? 0.5852 0.6617 0.4817 0.1923  0.1113  0.1048  61  ASN C CB  
3976 C CG  . ASN C 70  ? 0.7346 0.7741 0.5850 0.2012  0.1285  0.1287  61  ASN C CG  
3977 O OD1 . ASN C 70  ? 0.6977 0.7189 0.5668 0.1775  0.1475  0.1430  61  ASN C OD1 
3978 N ND2 . ASN C 70  ? 0.8326 0.8596 0.6198 0.2391  0.1198  0.1306  61  ASN C ND2 
3979 N N   . PHE C 71  ? 0.5592 0.6423 0.5835 0.1156  0.1341  0.1060  62  PHE C N   
3980 C CA  . PHE C 71  ? 0.5038 0.5963 0.5736 0.0923  0.1580  0.0990  62  PHE C CA  
3981 C C   . PHE C 71  ? 0.5612 0.6217 0.6049 0.0849  0.2034  0.1191  62  PHE C C   
3982 O O   . PHE C 71  ? 0.5890 0.6267 0.6346 0.0731  0.2089  0.1325  62  PHE C O   
3983 C CB  . PHE C 71  ? 0.5052 0.6062 0.6244 0.0751  0.1343  0.0902  62  PHE C CB  
3984 C CG  . PHE C 71  ? 0.4786 0.5987 0.6188 0.0812  0.0977  0.0697  62  PHE C CG  
3985 C CD1 . PHE C 71  ? 0.4603 0.6073 0.6250 0.0849  0.0961  0.0462  62  PHE C CD1 
3986 C CD2 . PHE C 71  ? 0.4310 0.5386 0.5648 0.0833  0.0678  0.0726  62  PHE C CD2 
3987 C CE1 . PHE C 71  ? 0.4421 0.5955 0.6158 0.0939  0.0634  0.0283  62  PHE C CE1 
3988 C CE2 . PHE C 71  ? 0.4385 0.5498 0.5834 0.0879  0.0402  0.0552  62  PHE C CE2 
3989 C CZ  . PHE C 71  ? 0.4352 0.5655 0.5960 0.0947  0.0370  0.0342  62  PHE C CZ  
3990 N N   . ARG C 72  ? 0.6298 0.6834 0.6457 0.0918  0.2390  0.1210  63  ARG C N   
3991 C CA  . ARG C 72  ? 0.6908 0.6986 0.6663 0.0867  0.2898  0.1425  63  ARG C CA  
3992 C C   . ARG C 72  ? 0.6745 0.6837 0.7088 0.0500  0.3196  0.1355  63  ARG C C   
3993 O O   . ARG C 72  ? 0.6877 0.6500 0.6926 0.0400  0.3593  0.1529  63  ARG C O   
3994 C CB  . ARG C 72  ? 0.7065 0.7015 0.6334 0.1035  0.3261  0.1456  63  ARG C CB  
3995 N N   . GLU C 73  ? 0.6314 0.6895 0.7446 0.0322  0.2981  0.1074  64  GLU C N   
3996 C CA  . GLU C 73  ? 0.6133 0.6854 0.7926 0.0000  0.3242  0.0900  64  GLU C CA  
3997 C C   . GLU C 73  ? 0.5824 0.6633 0.8042 -0.0100 0.2901  0.0836  64  GLU C C   
3998 O O   . GLU C 73  ? 0.5698 0.6635 0.8484 -0.0342 0.3070  0.0659  64  GLU C O   
3999 C CB  . GLU C 73  ? 0.7098 0.8379 0.9502 -0.0086 0.3330  0.0534  64  GLU C CB  
4000 C CG  . GLU C 73  ? 0.7651 0.8881 0.9660 0.0016  0.3692  0.0574  64  GLU C CG  
4001 C CD  . GLU C 73  ? 0.8892 0.9719 1.0686 -0.0205 0.4155  0.0623  64  GLU C CD  
4002 O OE1 . GLU C 73  ? 0.8642 0.8932 1.0107 -0.0285 0.4227  0.0826  64  GLU C OE1 
4003 O OE2 . GLU C 73  ? 0.8984 1.0017 1.0930 -0.0284 0.4402  0.0437  64  GLU C OE2 
4004 N N   . ILE C 74  ? 0.5420 0.6171 0.7398 0.0077  0.2448  0.0946  65  ILE C N   
4005 C CA  . ILE C 74  ? 0.4550 0.5349 0.6852 0.0019  0.2128  0.0895  65  ILE C CA  
4006 C C   . ILE C 74  ? 0.4745 0.5096 0.6569 0.0059  0.2121  0.1206  65  ILE C C   
4007 O O   . ILE C 74  ? 0.4913 0.5129 0.6249 0.0258  0.1934  0.1366  65  ILE C O   
4008 C CB  . ILE C 74  ? 0.4173 0.5223 0.6592 0.0174  0.1650  0.0747  65  ILE C CB  
4009 C CG1 . ILE C 74  ? 0.3347 0.4808 0.6117 0.0208  0.1634  0.0440  65  ILE C CG1 
4010 C CG2 . ILE C 74  ? 0.3594 0.4621 0.6274 0.0138  0.1370  0.0698  65  ILE C CG2 
4011 C CD1 . ILE C 74  ? 0.3077 0.4664 0.5853 0.0389  0.1195  0.0295  65  ILE C CD1 
4012 N N   . PRO C 75  ? 0.4107 0.4251 0.6079 -0.0109 0.2297  0.1260  66  PRO C N   
4013 C CA  . PRO C 75  ? 0.4459 0.4169 0.5946 -0.0039 0.2278  0.1544  66  PRO C CA  
4014 C C   . PRO C 75  ? 0.4609 0.4421 0.6148 0.0059  0.1817  0.1554  66  PRO C C   
4015 O O   . PRO C 75  ? 0.3965 0.4084 0.5896 0.0053  0.1538  0.1360  66  PRO C O   
4016 C CB  . PRO C 75  ? 0.4534 0.4015 0.6189 -0.0251 0.2513  0.1473  66  PRO C CB  
4017 C CG  . PRO C 75  ? 0.4171 0.4108 0.6652 -0.0442 0.2527  0.1157  66  PRO C CG  
4018 C CD  . PRO C 75  ? 0.4034 0.4358 0.6661 -0.0363 0.2510  0.1020  66  PRO C CD  
4019 N N   . SER C 76  ? 0.5413 0.3994 0.5274 0.1352  0.0169  0.1514  67  SER C N   
4020 C CA  . SER C 76  ? 0.5024 0.3828 0.5094 0.1394  0.0047  0.1330  67  SER C CA  
4021 C C   . SER C 76  ? 0.4683 0.3512 0.5073 0.1311  0.0118  0.1169  67  SER C C   
4022 O O   . SER C 76  ? 0.4533 0.3593 0.5035 0.1260  0.0087  0.1010  67  SER C O   
4023 C CB  . SER C 76  ? 0.5225 0.4049 0.5354 0.1570  -0.0112 0.1405  67  SER C CB  
4024 O OG  . SER C 76  ? 0.5582 0.4128 0.5883 0.1648  -0.0078 0.1488  67  SER C OG  
4025 N N   . HIS C 77  ? 0.4966 0.3555 0.5489 0.1281  0.0203  0.1208  68  HIS C N   
4026 C CA  . HIS C 77  ? 0.5227 0.3861 0.6005 0.1199  0.0249  0.1029  68  HIS C CA  
4027 C C   . HIS C 77  ? 0.5051 0.3856 0.5827 0.1045  0.0323  0.0950  68  HIS C C   
4028 O O   . HIS C 77  ? 0.4878 0.3844 0.5804 0.0987  0.0319  0.0799  68  HIS C O   
4029 C CB  . HIS C 77  ? 0.5657 0.3954 0.6563 0.1180  0.0303  0.1056  68  HIS C CB  
4030 C CG  . HIS C 77  ? 0.6476 0.4592 0.7317 0.1028  0.0413  0.1194  68  HIS C CG  
4031 N ND1 . HIS C 77  ? 0.6581 0.4479 0.7242 0.1048  0.0442  0.1437  68  HIS C ND1 
4032 C CD2 . HIS C 77  ? 0.6262 0.4435 0.7213 0.0846  0.0501  0.1139  68  HIS C CD2 
4033 C CE1 . HIS C 77  ? 0.6576 0.4419 0.7254 0.0872  0.0566  0.1523  68  HIS C CE1 
4034 N NE2 . HIS C 77  ? 0.6010 0.4031 0.6887 0.0752  0.0595  0.1340  68  HIS C NE2 
4035 N N   . VAL C 78  ? 0.4875 0.3668 0.5479 0.0997  0.0394  0.1056  69  VAL C N   
4036 C CA  . VAL C 78  ? 0.4883 0.3849 0.5500 0.0905  0.0455  0.0987  69  VAL C CA  
4037 C C   . VAL C 78  ? 0.4425 0.3552 0.4934 0.0945  0.0370  0.0895  69  VAL C C   
4038 O O   . VAL C 78  ? 0.3966 0.3223 0.4578 0.0886  0.0358  0.0791  69  VAL C O   
4039 C CB  . VAL C 78  ? 0.4534 0.3467 0.5035 0.0863  0.0588  0.1118  69  VAL C CB  
4040 C CG1 . VAL C 78  ? 0.3812 0.2940 0.4354 0.0825  0.0646  0.1039  69  VAL C CG1 
4041 C CG2 . VAL C 78  ? 0.4696 0.3478 0.5349 0.0766  0.0667  0.1216  69  VAL C CG2 
4042 N N   . LEU C 79  ? 0.4825 0.3932 0.5111 0.1031  0.0299  0.0943  70  LEU C N   
4043 C CA  . LEU C 79  ? 0.4607 0.3828 0.4769 0.1033  0.0206  0.0846  70  LEU C CA  
4044 C C   . LEU C 79  ? 0.4139 0.3526 0.4511 0.1004  0.0098  0.0745  70  LEU C C   
4045 O O   . LEU C 79  ? 0.3849 0.3322 0.4231 0.0933  0.0052  0.0655  70  LEU C O   
4046 C CB  . LEU C 79  ? 0.4365 0.3548 0.4206 0.1113  0.0135  0.0911  70  LEU C CB  
4047 C CG  . LEU C 79  ? 0.4442 0.3700 0.4115 0.1091  0.0015  0.0784  70  LEU C CG  
4048 C CD1 . LEU C 79  ? 0.4115 0.3315 0.3762 0.1032  0.0096  0.0672  70  LEU C CD1 
4049 C CD2 . LEU C 79  ? 0.4565 0.3801 0.3869 0.1163  -0.0072 0.0833  70  LEU C CD2 
4050 N N   . SER C 80  ? 0.3806 0.3234 0.4354 0.1060  0.0067  0.0760  71  SER C N   
4051 C CA  . SER C 80  ? 0.3793 0.3448 0.4569 0.1035  0.0012  0.0658  71  SER C CA  
4052 C C   . SER C 80  ? 0.3831 0.3541 0.4719 0.0913  0.0086  0.0580  71  SER C C   
4053 O O   . SER C 80  ? 0.3513 0.3406 0.4473 0.0831  0.0047  0.0520  71  SER C O   
4054 C CB  . SER C 80  ? 0.3876 0.3547 0.4826 0.1159  -0.0001 0.0666  71  SER C CB  
4055 O OG  . SER C 80  ? 0.4233 0.3636 0.5190 0.1175  0.0095  0.0708  71  SER C OG  
4056 N N   . LYS C 81  ? 0.3785 0.3353 0.4693 0.0885  0.0184  0.0597  72  LYS C N   
4057 C CA  . LYS C 81  ? 0.3602 0.3250 0.4603 0.0778  0.0227  0.0540  72  LYS C CA  
4058 C C   . LYS C 81  ? 0.3565 0.3227 0.4473 0.0722  0.0212  0.0554  72  LYS C C   
4059 O O   . LYS C 81  ? 0.3462 0.3237 0.4428 0.0642  0.0189  0.0524  72  LYS C O   
4060 C CB  . LYS C 81  ? 0.4099 0.3623 0.5163 0.0745  0.0308  0.0556  72  LYS C CB  
4061 C CG  . LYS C 81  ? 0.4256 0.3899 0.5444 0.0653  0.0319  0.0464  72  LYS C CG  
4062 C CD  . LYS C 81  ? 0.4452 0.4153 0.5715 0.0695  0.0305  0.0352  72  LYS C CD  
4063 C CE  . LYS C 81  ? 0.4342 0.4220 0.5648 0.0598  0.0313  0.0240  72  LYS C CE  
4064 N NZ  . LYS C 81  ? 0.4749 0.4499 0.6097 0.0528  0.0335  0.0178  72  LYS C NZ  
4065 N N   . VAL C 82  ? 0.3620 0.3150 0.4360 0.0772  0.0225  0.0601  73  VAL C N   
4066 C CA  . VAL C 82  ? 0.3702 0.3180 0.4337 0.0755  0.0213  0.0582  73  VAL C CA  
4067 C C   . VAL C 82  ? 0.3866 0.3397 0.4487 0.0692  0.0098  0.0529  73  VAL C C   
4068 O O   . VAL C 82  ? 0.3784 0.3286 0.4426 0.0624  0.0072  0.0516  73  VAL C O   
4069 C CB  . VAL C 82  ? 0.4073 0.3413 0.4484 0.0841  0.0265  0.0608  73  VAL C CB  
4070 C CG1 . VAL C 82  ? 0.3645 0.2874 0.3900 0.0853  0.0229  0.0534  73  VAL C CG1 
4071 C CG2 . VAL C 82  ? 0.3824 0.3167 0.4302 0.0862  0.0405  0.0680  73  VAL C CG2 
4072 N N   . CYS C 83  ? 0.3702 0.3323 0.4311 0.0707  0.0018  0.0516  74  CYS C N   
4073 C CA  . CYS C 83  ? 0.3612 0.3359 0.4267 0.0612  -0.0096 0.0475  74  CYS C CA  
4074 C C   . CYS C 83  ? 0.3879 0.3819 0.4741 0.0507  -0.0076 0.0478  74  CYS C C   
4075 O O   . CYS C 83  ? 0.3545 0.3511 0.4431 0.0378  -0.0129 0.0480  74  CYS C O   
4076 C CB  . CYS C 83  ? 0.3308 0.3207 0.3971 0.0665  -0.0191 0.0474  74  CYS C CB  
4077 S SG  . CYS C 83  ? 0.3776 0.3484 0.4101 0.0751  -0.0258 0.0474  74  CYS C SG  
4078 N N   . MET C 84  ? 0.3742 0.3803 0.4731 0.0551  0.0000  0.0478  75  MET C N   
4079 C CA  . MET C 84  ? 0.3114 0.3374 0.4233 0.0459  0.0036  0.0469  75  MET C CA  
4080 C C   . MET C 84  ? 0.3591 0.3730 0.4645 0.0375  0.0047  0.0518  75  MET C C   
4081 O O   . MET C 84  ? 0.3494 0.3748 0.4580 0.0253  0.0028  0.0558  75  MET C O   
4082 C CB  . MET C 84  ? 0.2950 0.3291 0.4159 0.0534  0.0113  0.0417  75  MET C CB  
4083 C CG  . MET C 84  ? 0.3171 0.3654 0.4491 0.0642  0.0100  0.0373  75  MET C CG  
4084 S SD  . MET C 84  ? 0.3785 0.4173 0.5172 0.0762  0.0185  0.0292  75  MET C SD  
4085 C CE  . MET C 84  ? 0.2880 0.3354 0.4392 0.0949  0.0133  0.0289  75  MET C CE  
4086 N N   . TYR C 85  ? 0.3318 0.3245 0.4295 0.0444  0.0080  0.0537  76  TYR C N   
4087 C CA  . TYR C 85  ? 0.3492 0.3321 0.4447 0.0409  0.0078  0.0593  76  TYR C CA  
4088 C C   . TYR C 85  ? 0.3797 0.3462 0.4671 0.0351  0.0001  0.0616  76  TYR C C   
4089 O O   . TYR C 85  ? 0.3638 0.3261 0.4524 0.0276  -0.0031 0.0689  76  TYR C O   
4090 C CB  . TYR C 85  ? 0.3411 0.3120 0.4354 0.0511  0.0140  0.0605  76  TYR C CB  
4091 C CG  . TYR C 85  ? 0.3599 0.3223 0.4555 0.0522  0.0124  0.0665  76  TYR C CG  
4092 C CD1 . TYR C 85  ? 0.3366 0.3139 0.4418 0.0468  0.0104  0.0728  76  TYR C CD1 
4093 C CD2 . TYR C 85  ? 0.3662 0.3049 0.4518 0.0599  0.0114  0.0653  76  TYR C CD2 
4094 C CE1 . TYR C 85  ? 0.3476 0.3174 0.4559 0.0506  0.0066  0.0812  76  TYR C CE1 
4095 C CE2 . TYR C 85  ? 0.3896 0.3169 0.4788 0.0649  0.0095  0.0708  76  TYR C CE2 
4096 C CZ  . TYR C 85  ? 0.3705 0.3142 0.4728 0.0609  0.0065  0.0805  76  TYR C CZ  
4097 O OH  . TYR C 85  ? 0.4045 0.3377 0.5123 0.0685  0.0025  0.0889  76  TYR C OH  
4098 N N   . PHE C 86  ? 0.3870 0.3407 0.4640 0.0381  -0.0041 0.0558  77  PHE C N   
4099 C CA  . PHE C 86  ? 0.3898 0.3246 0.4586 0.0291  -0.0136 0.0543  77  PHE C CA  
4100 C C   . PHE C 86  ? 0.3908 0.3440 0.4719 0.0106  -0.0186 0.0608  77  PHE C C   
4101 O O   . PHE C 86  ? 0.4356 0.3725 0.5155 0.0001  -0.0229 0.0680  77  PHE C O   
4102 C CB  . PHE C 86  ? 0.4365 0.3643 0.4917 0.0316  -0.0204 0.0449  77  PHE C CB  
4103 C CG  . PHE C 86  ? 0.4391 0.3477 0.4748 0.0480  -0.0148 0.0392  77  PHE C CG  
4104 C CD1 . PHE C 86  ? 0.4443 0.3399 0.4788 0.0588  -0.0046 0.0413  77  PHE C CD1 
4105 C CD2 . PHE C 86  ? 0.3916 0.2999 0.4099 0.0526  -0.0199 0.0327  77  PHE C CD2 
4106 C CE1 . PHE C 86  ? 0.4174 0.3023 0.4352 0.0735  0.0038  0.0367  77  PHE C CE1 
4107 C CE2 . PHE C 86  ? 0.4542 0.3480 0.4497 0.0669  -0.0127 0.0289  77  PHE C CE2 
4108 C CZ  . PHE C 86  ? 0.4201 0.3032 0.4161 0.0771  0.0008  0.0307  77  PHE C CZ  
4109 N N   . THR C 87  ? 0.3715 0.3591 0.4652 0.0072  -0.0171 0.0595  78  THR C N   
4110 C CA  . THR C 87  ? 0.3965 0.4113 0.5037 -0.0107 -0.0188 0.0653  78  THR C CA  
4111 C C   . THR C 87  ? 0.3767 0.3952 0.4838 -0.0172 -0.0132 0.0762  78  THR C C   
4112 O O   . THR C 87  ? 0.3818 0.3979 0.4892 -0.0343 -0.0168 0.0872  78  THR C O   
4113 C CB  . THR C 87  ? 0.3671 0.4231 0.4906 -0.0067 -0.0153 0.0600  78  THR C CB  
4114 O OG1 . THR C 87  ? 0.3579 0.4106 0.4796 0.0024  -0.0226 0.0527  78  THR C OG1 
4115 C CG2 . THR C 87  ? 0.3047 0.3977 0.4455 -0.0253 -0.0152 0.0654  78  THR C CG2 
4116 N N   . TYR C 88  ? 0.3645 0.3877 0.4699 -0.0051 -0.0058 0.0744  79  TYR C N   
4117 C CA  . TYR C 88  ? 0.3580 0.3887 0.4604 -0.0100 -0.0029 0.0839  79  TYR C CA  
4118 C C   . TYR C 88  ? 0.4061 0.4040 0.5003 -0.0131 -0.0099 0.0962  79  TYR C C   
4119 O O   . TYR C 88  ? 0.4344 0.4349 0.5253 -0.0259 -0.0125 0.1108  79  TYR C O   
4120 C CB  . TYR C 88  ? 0.3571 0.3951 0.4599 0.0029  0.0032  0.0763  79  TYR C CB  
4121 C CG  . TYR C 88  ? 0.4028 0.4492 0.5009 0.0003  0.0033  0.0833  79  TYR C CG  
4122 C CD1 . TYR C 88  ? 0.3969 0.4742 0.4912 -0.0077 0.0075  0.0823  79  TYR C CD1 
4123 C CD2 . TYR C 88  ? 0.3734 0.4009 0.4707 0.0077  -0.0008 0.0897  79  TYR C CD2 
4124 C CE1 . TYR C 88  ? 0.4417 0.5293 0.5274 -0.0107 0.0051  0.0880  79  TYR C CE1 
4125 C CE2 . TYR C 88  ? 0.4250 0.4656 0.5199 0.0057  -0.0038 0.0971  79  TYR C CE2 
4126 C CZ  . TYR C 88  ? 0.4236 0.4935 0.5106 -0.0045 -0.0021 0.0963  79  TYR C CZ  
4127 O OH  . TYR C 88  ? 0.4071 0.4924 0.4873 -0.0074 -0.0075 0.1029  79  TYR C OH  
4128 N N   . LYS C 89  ? 0.3968 0.3629 0.4869 -0.0004 -0.0125 0.0912  80  LYS C N   
4129 C CA  . LYS C 89  ? 0.4026 0.3347 0.4873 0.0033  -0.0181 0.1001  80  LYS C CA  
4130 C C   . LYS C 89  ? 0.4639 0.3737 0.5446 -0.0138 -0.0265 0.1086  80  LYS C C   
4131 O O   . LYS C 89  ? 0.4723 0.3684 0.5508 -0.0206 -0.0312 0.1254  80  LYS C O   
4132 C CB  . LYS C 89  ? 0.4433 0.3502 0.5239 0.0222  -0.0160 0.0889  80  LYS C CB  
4133 C CG  . LYS C 89  ? 0.4894 0.3573 0.5657 0.0311  -0.0208 0.0936  80  LYS C CG  
4134 C CD  . LYS C 89  ? 0.4483 0.3263 0.5344 0.0405  -0.0202 0.1064  80  LYS C CD  
4135 C CE  . LYS C 89  ? 0.5182 0.3648 0.6058 0.0616  -0.0204 0.1050  80  LYS C CE  
4136 N NZ  . LYS C 89  ? 0.5290 0.4025 0.6332 0.0779  -0.0150 0.1087  80  LYS C NZ  
4137 N N   . VAL C 90  ? 0.4528 0.3588 0.5330 -0.0224 -0.0300 0.0986  81  VAL C N   
4138 C CA  . VAL C 90  ? 0.4556 0.3393 0.5344 -0.0432 -0.0394 0.1048  81  VAL C CA  
4139 C C   . VAL C 90  ? 0.4861 0.4010 0.5732 -0.0653 -0.0375 0.1229  81  VAL C C   
4140 O O   . VAL C 90  ? 0.5467 0.4382 0.6310 -0.0817 -0.0435 0.1394  81  VAL C O   
4141 C CB  . VAL C 90  ? 0.4892 0.3709 0.5673 -0.0490 -0.0457 0.0884  81  VAL C CB  
4142 C CG1 . VAL C 90  ? 0.4690 0.3344 0.5504 -0.0767 -0.0567 0.0943  81  VAL C CG1 
4143 C CG2 . VAL C 90  ? 0.4699 0.3172 0.5319 -0.0282 -0.0470 0.0716  81  VAL C CG2 
4144 N N   . ARG C 91  ? 0.4086 0.3748 0.5042 -0.0654 -0.0283 0.1205  82  ARG C N   
4145 C CA  . ARG C 91  ? 0.4089 0.4117 0.5098 -0.0857 -0.0233 0.1356  82  ARG C CA  
4146 C C   . ARG C 91  ? 0.4713 0.4681 0.5597 -0.0862 -0.0222 0.1548  82  ARG C C   
4147 O O   . ARG C 91  ? 0.5046 0.5085 0.5897 -0.1070 -0.0223 0.1752  82  ARG C O   
4148 C CB  . ARG C 91  ? 0.3895 0.4483 0.5019 -0.0816 -0.0123 0.1242  82  ARG C CB  
4149 C CG  . ARG C 91  ? 0.3949 0.4998 0.5087 -0.0967 -0.0021 0.1364  82  ARG C CG  
4150 C CD  . ARG C 91  ? 0.3954 0.5093 0.5172 -0.1267 -0.0041 0.1540  82  ARG C CD  
4151 N NE  . ARG C 91  ? 0.4650 0.6294 0.5858 -0.1410 0.0089  0.1666  82  ARG C NE  
4152 C CZ  . ARG C 91  ? 0.5144 0.6750 0.6149 -0.1500 0.0110  0.1876  82  ARG C CZ  
4153 N NH1 . ARG C 91  ? 0.5220 0.6309 0.6059 -0.1444 -0.0002 0.1994  82  ARG C NH1 
4154 N NH2 . ARG C 91  ? 0.4349 0.6474 0.5310 -0.1633 0.0249  0.1976  82  ARG C NH2 
4155 N N   . TYR C 92  ? 0.4518 0.4392 0.5336 -0.0652 -0.0219 0.1510  83  TYR C N   
4156 C CA  . TYR C 92  ? 0.5024 0.4961 0.5733 -0.0650 -0.0228 0.1686  83  TYR C CA  
4157 C C   . TYR C 92  ? 0.5572 0.5035 0.6233 -0.0547 -0.0335 0.1818  83  TYR C C   
4158 O O   . TYR C 92  ? 0.5931 0.5450 0.6520 -0.0502 -0.0373 0.1972  83  TYR C O   
4159 C CB  . TYR C 92  ? 0.4875 0.5162 0.5573 -0.0518 -0.0159 0.1558  83  TYR C CB  
4160 C CG  . TYR C 92  ? 0.4516 0.5269 0.5234 -0.0597 -0.0047 0.1452  83  TYR C CG  
4161 C CD1 . TYR C 92  ? 0.4904 0.5953 0.5558 -0.0795 0.0005  0.1588  83  TYR C CD1 
4162 C CD2 . TYR C 92  ? 0.4680 0.5581 0.5486 -0.0463 0.0018  0.1222  83  TYR C CD2 
4163 C CE1 . TYR C 92  ? 0.4658 0.6186 0.5351 -0.0832 0.0135  0.1465  83  TYR C CE1 
4164 C CE2 . TYR C 92  ? 0.4686 0.5990 0.5532 -0.0489 0.0125  0.1105  83  TYR C CE2 
4165 C CZ  . TYR C 92  ? 0.4489 0.6126 0.5286 -0.0660 0.0189  0.1211  83  TYR C CZ  
4166 O OH  . TYR C 92  ? 0.3916 0.5990 0.4772 -0.0647 0.0317  0.1070  83  TYR C OH  
4167 N N   . THR C 93  ? 0.7052 0.3383 0.7135 0.0475  -0.1387 0.1326  84  THR C N   
4168 C CA  . THR C 93  ? 0.8496 0.4011 0.7695 0.0723  -0.1200 0.1245  84  THR C CA  
4169 C C   . THR C 93  ? 0.9623 0.5104 0.8939 0.0693  -0.1149 0.1454  84  THR C C   
4170 O O   . THR C 93  ? 0.9425 0.4983 0.9148 0.0324  -0.1414 0.1669  84  THR C O   
4171 C CB  . THR C 93  ? 0.9040 0.3173 0.7124 0.0546  -0.1421 0.1148  84  THR C CB  
4172 O OG1 . THR C 93  ? 0.8881 0.3020 0.6741 0.0698  -0.1345 0.0943  84  THR C OG1 
4173 C CG2 . THR C 93  ? 1.0528 0.3578 0.7628 0.0791  -0.1168 0.1132  84  THR C CG2 
4174 N N   . ASN C 94  ? 1.1379 0.6839 1.0432 0.1088  -0.0801 0.1455  85  ASN C N   
4175 C CA  . ASN C 94  ? 1.1930 0.7346 1.1045 0.1116  -0.0710 0.1668  85  ASN C CA  
4176 C C   . ASN C 94  ? 1.1293 0.7739 1.1375 0.0923  -0.0756 0.1829  85  ASN C C   
4177 O O   . ASN C 94  ? 1.1606 0.7918 1.1867 0.0687  -0.0873 0.2049  85  ASN C O   
4178 C CB  . ASN C 94  ? 1.2683 0.6729 1.0972 0.0852  -0.0917 0.1746  85  ASN C CB  
4179 C CG  . ASN C 94  ? 1.3530 0.6333 1.0660 0.1055  -0.0766 0.1568  85  ASN C CG  
4180 O OD1 . ASN C 94  ? 1.3455 0.6541 1.0524 0.1525  -0.0382 0.1488  85  ASN C OD1 
4181 N ND2 . ASN C 94  ? 1.4470 0.6322 1.0884 0.0631  -0.1002 0.1472  85  ASN C ND2 
4182 N N   . SER C 95  ? 0.9144 0.6539 0.9788 0.1021  -0.0624 0.1732  86  SER C N   
4183 C CA  . SER C 95  ? 0.7958 0.6218 0.9367 0.0920  -0.0523 0.1855  86  SER C CA  
4184 C C   . SER C 95  ? 0.7407 0.6333 0.8839 0.1187  -0.0214 0.1790  86  SER C C   
4185 O O   . SER C 95  ? 0.7675 0.6741 0.8873 0.1371  -0.0143 0.1624  86  SER C O   
4186 C CB  . SER C 95  ? 0.7072 0.5668 0.9015 0.0721  -0.0641 0.1827  86  SER C CB  
4187 O OG  . SER C 95  ? 0.7185 0.6549 0.9583 0.0822  -0.0345 0.1792  86  SER C OG  
4188 N N   . SER C 96  ? 0.7296 0.6614 0.8971 0.1169  -0.0053 0.1961  87  SER C N   
4189 C CA  . SER C 96  ? 0.6852 0.6722 0.8409 0.1316  0.0169  0.1952  87  SER C CA  
4190 C C   . SER C 96  ? 0.6837 0.7187 0.8655 0.1195  0.0383  0.1919  87  SER C C   
4191 O O   . SER C 96  ? 0.7109 0.7803 0.8648 0.1219  0.0519  0.1845  87  SER C O   
4192 C CB  . SER C 96  ? 0.5957 0.5749 0.7308 0.1428  0.0228  0.2197  87  SER C CB  
4193 O OG  . SER C 96  ? 0.5899 0.5606 0.7512 0.1267  0.0265  0.2397  87  SER C OG  
4194 N N   . THR C 97  ? 0.6717 0.7051 0.9019 0.1054  0.0433  0.2016  88  THR C N   
4195 C CA  . THR C 97  ? 0.6882 0.7522 0.9401 0.1016  0.0760  0.2004  88  THR C CA  
4196 C C   . THR C 97  ? 0.7005 0.7731 0.9311 0.1043  0.0815  0.1707  88  THR C C   
4197 O O   . THR C 97  ? 0.7137 0.7745 0.9478 0.1056  0.0580  0.1574  88  THR C O   
4198 C CB  . THR C 97  ? 0.6265 0.6946 0.9549 0.0912  0.0803  0.2275  88  THR C CB  
4199 O OG1 . THR C 97  ? 0.6294 0.7184 0.9823 0.0965  0.1201  0.2270  88  THR C OG1 
4200 C CG2 . THR C 97  ? 0.6523 0.6978 1.0079 0.0792  0.0390  0.2293  88  THR C CG2 
4201 N N   . GLU C 98  ? 0.6963 0.7789 0.8926 0.1024  0.1135  0.1600  89  GLU C N   
4202 C CA  . GLU C 98  ? 0.6926 0.7737 0.8578 0.0993  0.1193  0.1321  89  GLU C CA  
4203 C C   . GLU C 98  ? 0.6618 0.7356 0.8817 0.1030  0.1281  0.1306  89  GLU C C   
4204 O O   . GLU C 98  ? 0.6232 0.6987 0.8969 0.1070  0.1519  0.1533  89  GLU C O   
4205 C CB  . GLU C 98  ? 0.7706 0.8419 0.8648 0.0881  0.1512  0.1209  89  GLU C CB  
4206 C CG  . GLU C 98  ? 0.7794 0.8356 0.8315 0.0779  0.1582  0.0921  89  GLU C CG  
4207 C CD  . GLU C 98  ? 0.8915 0.9379 0.8468 0.0529  0.1599  0.0799  89  GLU C CD  
4208 O OE1 . GLU C 98  ? 0.9860 0.9999 0.8848 0.0432  0.1923  0.0828  89  GLU C OE1 
4209 O OE2 . GLU C 98  ? 0.8946 0.9649 0.8277 0.0403  0.1281  0.0714  89  GLU C OE2 
4210 N N   . ILE C 99  ? 0.6398 0.7108 0.8519 0.1027  0.1095  0.1099  90  ILE C N   
4211 C CA  . ILE C 99  ? 0.5789 0.6452 0.8417 0.1056  0.1070  0.1109  90  ILE C CA  
4212 C C   . ILE C 99  ? 0.5676 0.6245 0.7890 0.1036  0.1148  0.0814  90  ILE C C   
4213 O O   . ILE C 99  ? 0.6214 0.6814 0.7828 0.0961  0.1084  0.0634  90  ILE C O   
4214 C CB  . ILE C 99  ? 0.5752 0.6350 0.8686 0.1029  0.0620  0.1207  90  ILE C CB  
4215 C CG1 . ILE C 99  ? 0.5461 0.5956 0.7821 0.1064  0.0386  0.1007  90  ILE C CG1 
4216 C CG2 . ILE C 99  ? 0.5931 0.6530 0.9249 0.0966  0.0508  0.1527  90  ILE C CG2 
4217 C CD1 . ILE C 99  ? 0.5319 0.5481 0.7666 0.1054  0.0034  0.1027  90  ILE C CD1 
4218 N N   . PRO C 100 ? 0.5854 0.6340 0.8419 0.1082  0.1275  0.0815  91  PRO C N   
4219 C CA  . PRO C 100 ? 0.5861 0.6188 0.8007 0.1044  0.1342  0.0537  91  PRO C CA  
4220 C C   . PRO C 100 ? 0.4984 0.5400 0.6979 0.1010  0.0923  0.0403  91  PRO C C   
4221 O O   . PRO C 100 ? 0.4874 0.5331 0.7067 0.1046  0.0610  0.0514  91  PRO C O   
4222 C CB  . PRO C 100 ? 0.5904 0.6131 0.8605 0.1157  0.1587  0.0667  91  PRO C CB  
4223 C CG  . PRO C 100 ? 0.6115 0.6457 0.9377 0.1257  0.1850  0.1010  91  PRO C CG  
4224 C CD  . PRO C 100 ? 0.5845 0.6406 0.9213 0.1172  0.1453  0.1130  91  PRO C CD  
4225 N N   . GLU C 101 ? 0.4878 0.5236 0.6429 0.0929  0.0956  0.0176  92  GLU C N   
4226 C CA  . GLU C 101 ? 0.4581 0.5034 0.6055 0.0943  0.0649  0.0098  92  GLU C CA  
4227 C C   . GLU C 101 ? 0.4626 0.4909 0.6476 0.1013  0.0548  0.0116  92  GLU C C   
4228 O O   . GLU C 101 ? 0.4706 0.4899 0.6958 0.1045  0.0707  0.0223  92  GLU C O   
4229 C CB  . GLU C 101 ? 0.5002 0.5554 0.5961 0.0787  0.0672  -0.0071 92  GLU C CB  
4230 C CG  . GLU C 101 ? 0.5310 0.5587 0.6133 0.0699  0.0857  -0.0243 92  GLU C CG  
4231 C CD  . GLU C 101 ? 0.6590 0.6983 0.6940 0.0479  0.0769  -0.0369 92  GLU C CD  
4232 O OE1 . GLU C 101 ? 0.7718 0.7801 0.7825 0.0356  0.0923  -0.0525 92  GLU C OE1 
4233 O OE2 . GLU C 101 ? 0.6327 0.7139 0.6594 0.0427  0.0553  -0.0258 92  GLU C OE2 
4234 N N   . PHE C 102 ? 0.4479 0.4713 0.6202 0.1052  0.0296  0.0069  93  PHE C N   
4235 C CA  . PHE C 102 ? 0.3613 0.3631 0.5509 0.1069  0.0162  0.0070  93  PHE C CA  
4236 C C   . PHE C 102 ? 0.3880 0.3899 0.5588 0.1024  0.0329  -0.0112 93  PHE C C   
4237 O O   . PHE C 102 ? 0.4372 0.4498 0.5734 0.0999  0.0294  -0.0224 93  PHE C O   
4238 C CB  . PHE C 102 ? 0.3687 0.3450 0.5326 0.1125  -0.0121 0.0087  93  PHE C CB  
4239 C CG  . PHE C 102 ? 0.4234 0.3672 0.5931 0.1081  -0.0325 0.0127  93  PHE C CG  
4240 C CD1 . PHE C 102 ? 0.3704 0.2997 0.5747 0.0968  -0.0555 0.0355  93  PHE C CD1 
4241 C CD2 . PHE C 102 ? 0.3676 0.2996 0.5109 0.1112  -0.0315 -0.0010 93  PHE C CD2 
4242 C CE1 . PHE C 102 ? 0.3899 0.2928 0.5982 0.0862  -0.0817 0.0458  93  PHE C CE1 
4243 C CE2 . PHE C 102 ? 0.4050 0.3050 0.5476 0.1050  -0.0519 0.0049  93  PHE C CE2 
4244 C CZ  . PHE C 102 ? 0.4236 0.3084 0.5967 0.0911  -0.0798 0.0291  93  PHE C CZ  
4245 N N   . PRO C 103 ? 0.3766 0.3668 0.5718 0.1018  0.0533  -0.0098 94  PRO C N   
4246 C CA  . PRO C 103 ? 0.4215 0.3980 0.5855 0.0941  0.0752  -0.0288 94  PRO C CA  
4247 C C   . PRO C 103 ? 0.4226 0.3915 0.5809 0.0952  0.0557  -0.0344 94  PRO C C   
4248 O O   . PRO C 103 ? 0.3635 0.3226 0.5517 0.1027  0.0363  -0.0206 94  PRO C O   
4249 C CB  . PRO C 103 ? 0.3859 0.3401 0.5803 0.1018  0.1113  -0.0188 94  PRO C CB  
4250 C CG  . PRO C 103 ? 0.3616 0.3326 0.6279 0.1136  0.0916  0.0130  94  PRO C CG  
4251 C CD  . PRO C 103 ? 0.3728 0.3609 0.6307 0.1087  0.0568  0.0161  94  PRO C CD  
4252 N N   . ILE C 104 ? 0.4087 0.3824 0.5262 0.0837  0.0586  -0.0507 95  ILE C N   
4253 C CA  . ILE C 104 ? 0.4191 0.3859 0.5272 0.0850  0.0471  -0.0551 95  ILE C CA  
4254 C C   . ILE C 104 ? 0.4721 0.4241 0.5525 0.0671  0.0682  -0.0700 95  ILE C C   
4255 O O   . ILE C 104 ? 0.4690 0.4381 0.5146 0.0459  0.0702  -0.0775 95  ILE C O   
4256 C CB  . ILE C 104 ? 0.3902 0.3806 0.4802 0.0907  0.0297  -0.0513 95  ILE C CB  
4257 C CG1 . ILE C 104 ? 0.3646 0.3480 0.4631 0.1062  0.0137  -0.0389 95  ILE C CG1 
4258 C CG2 . ILE C 104 ? 0.3698 0.3465 0.4465 0.0952  0.0252  -0.0532 95  ILE C CG2 
4259 C CD1 . ILE C 104 ? 0.3537 0.3469 0.4289 0.1205  0.0088  -0.0311 95  ILE C CD1 
4260 N N   . ALA C 105 ? 0.5215 0.4398 0.6160 0.0725  0.0816  -0.0700 96  ALA C N   
4261 C CA  . ALA C 105 ? 0.4940 0.3794 0.5547 0.0566  0.1050  -0.0841 96  ALA C CA  
4262 C C   . ALA C 105 ? 0.5453 0.4487 0.5819 0.0421  0.0885  -0.0899 96  ALA C C   
4263 O O   . ALA C 105 ? 0.4823 0.4059 0.5358 0.0564  0.0673  -0.0807 96  ALA C O   
4264 C CB  . ALA C 105 ? 0.4515 0.2999 0.5438 0.0737  0.1240  -0.0744 96  ALA C CB  
4265 N N   . PRO C 106 ? 0.5076 0.3888 0.7970 -0.0705 0.0581  0.0300  97  PRO C N   
4266 C CA  . PRO C 106 ? 0.4826 0.3726 0.7539 -0.0808 0.0455  0.0593  97  PRO C CA  
4267 C C   . PRO C 106 ? 0.4899 0.3813 0.7774 -0.0747 0.0291  0.0846  97  PRO C C   
4268 O O   . PRO C 106 ? 0.4667 0.3821 0.7370 -0.0788 0.0244  0.1102  97  PRO C O   
4269 C CB  . PRO C 106 ? 0.4544 0.3243 0.7227 -0.0966 0.0412  0.0506  97  PRO C CB  
4270 C CG  . PRO C 106 ? 0.4877 0.3434 0.7635 -0.0937 0.0545  0.0161  97  PRO C CG  
4271 C CD  . PRO C 106 ? 0.4905 0.3516 0.7894 -0.0762 0.0628  0.0036  97  PRO C CD  
4272 N N   . GLU C 107 ? 0.4695 0.3387 0.7905 -0.0644 0.0198  0.0777  98  GLU C N   
4273 C CA  . GLU C 107 ? 0.5110 0.3749 0.8456 -0.0595 0.0000  0.1036  98  GLU C CA  
4274 C C   . GLU C 107 ? 0.4608 0.3526 0.7930 -0.0503 0.0000  0.1203  98  GLU C C   
4275 O O   . GLU C 107 ? 0.5075 0.4037 0.8377 -0.0500 -0.0158 0.1480  98  GLU C O   
4276 C CB  . GLU C 107 ? 0.5145 0.3478 0.8886 -0.0463 -0.0123 0.0893  98  GLU C CB  
4277 C CG  . GLU C 107 ? 0.5273 0.3340 0.9098 -0.0498 -0.0075 0.0608  98  GLU C CG  
4278 C CD  . GLU C 107 ? 0.5912 0.4110 0.9911 -0.0412 0.0137  0.0229  98  GLU C CD  
4279 O OE1 . GLU C 107 ? 0.6454 0.4795 1.0763 -0.0258 0.0162  0.0115  98  GLU C OE1 
4280 O OE2 . GLU C 107 ? 0.6297 0.4476 1.0115 -0.0520 0.0280  0.0042  98  GLU C OE2 
4281 N N   . ILE C 108 ? 0.4064 0.3146 0.7339 -0.0446 0.0170  0.1043  99  ILE C N   
4282 C CA  . ILE C 108 ? 0.4041 0.3328 0.7306 -0.0357 0.0179  0.1154  99  ILE C CA  
4283 C C   . ILE C 108 ? 0.4000 0.3549 0.6876 -0.0401 0.0301  0.1244  99  ILE C C   
4284 O O   . ILE C 108 ? 0.3951 0.3717 0.6679 -0.0307 0.0291  0.1323  99  ILE C O   
4285 C CB  . ILE C 108 ? 0.4395 0.3627 0.7969 -0.0249 0.0264  0.0875  99  ILE C CB  
4286 C CG1 . ILE C 108 ? 0.4281 0.3712 0.7886 -0.0117 0.0149  0.0968  99  ILE C CG1 
4287 C CG2 . ILE C 108 ? 0.3518 0.2800 0.6852 -0.0308 0.0504  0.0631  99  ILE C CG2 
4288 C CD1 . ILE C 108 ? 0.3966 0.3484 0.7779 -0.0045 0.0246  0.0655  99  ILE C CD1 
4289 N N   . ALA C 109 ? 0.3999 0.3580 0.6638 -0.0500 0.0381  0.1187  100 ALA C N   
4290 C CA  . ALA C 109 ? 0.3769 0.3570 0.6091 -0.0493 0.0499  0.1209  100 ALA C CA  
4291 C C   . ALA C 109 ? 0.3659 0.3846 0.5799 -0.0447 0.0435  0.1473  100 ALA C C   
4292 O O   . ALA C 109 ? 0.3545 0.3906 0.5433 -0.0304 0.0480  0.1427  100 ALA C O   
4293 C CB  . ALA C 109 ? 0.3572 0.3345 0.5729 -0.0609 0.0555  0.1113  100 ALA C CB  
4294 N N   . LEU C 110 ? 0.3397 0.3720 0.5579 -0.0553 0.0318  0.1695  101 LEU C N   
4295 C CA  . LEU C 110 ? 0.3470 0.4255 0.5462 -0.0540 0.0284  0.1937  101 LEU C CA  
4296 C C   . LEU C 110 ? 0.3855 0.4710 0.5803 -0.0382 0.0235  0.1980  101 LEU C C   
4297 O O   . LEU C 110 ? 0.3837 0.5029 0.5523 -0.0247 0.0275  0.1964  101 LEU C O   
4298 C CB  . LEU C 110 ? 0.3062 0.3925 0.5050 -0.0716 0.0162  0.2110  101 LEU C CB  
4299 C CG  . LEU C 110 ? 0.3428 0.4386 0.5354 -0.0880 0.0185  0.2067  101 LEU C CG  
4300 C CD1 . LEU C 110 ? 0.3197 0.4177 0.5115 -0.1077 0.0066  0.2264  101 LEU C CD1 
4301 C CD2 . LEU C 110 ? 0.2969 0.4452 0.4711 -0.0818 0.0288  0.2047  101 LEU C CD2 
4302 N N   . GLU C 111 ? 0.3630 0.4177 0.5822 -0.0369 0.0124  0.1992  102 GLU C N   
4303 C CA  . GLU C 111 ? 0.3560 0.4198 0.5706 -0.0217 0.0043  0.1993  102 GLU C CA  
4304 C C   . GLU C 111 ? 0.3448 0.4061 0.5490 -0.0066 0.0153  0.1693  102 GLU C C   
4305 O O   . GLU C 111 ? 0.3374 0.4203 0.5191 0.0056  0.0138  0.1669  102 GLU C O   
4306 C CB  . GLU C 111 ? 0.3819 0.4148 0.6297 -0.0206 -0.0128 0.2040  102 GLU C CB  
4307 C CG  . GLU C 111 ? 0.4263 0.4469 0.6805 -0.0356 -0.0284 0.2363  102 GLU C CG  
4308 C CD  . GLU C 111 ? 0.5366 0.5197 0.8248 -0.0274 -0.0482 0.2346  102 GLU C CD  
4309 O OE1 . GLU C 111 ? 0.5565 0.5071 0.8734 -0.0271 -0.0464 0.2125  102 GLU C OE1 
4310 O OE2 . GLU C 111 ? 0.4576 0.4489 0.7411 -0.0187 -0.0658 0.2505  102 GLU C OE2 
4311 N N   . LEU C 112 ? 0.3488 0.3813 0.5665 -0.0091 0.0262  0.1458  103 LEU C N   
4312 C CA  . LEU C 112 ? 0.3520 0.3751 0.5554 -0.0008 0.0372  0.1202  103 LEU C CA  
4313 C C   . LEU C 112 ? 0.3396 0.3810 0.5002 0.0080  0.0433  0.1210  103 LEU C C   
4314 O O   . LEU C 112 ? 0.2979 0.3402 0.4374 0.0198  0.0434  0.1102  103 LEU C O   
4315 C CB  . LEU C 112 ? 0.3058 0.2984 0.5253 -0.0099 0.0500  0.0978  103 LEU C CB  
4316 C CG  . LEU C 112 ? 0.3176 0.2950 0.5302 -0.0086 0.0605  0.0725  103 LEU C CG  
4317 C CD1 . LEU C 112 ? 0.2665 0.2539 0.5001 -0.0019 0.0501  0.0674  103 LEU C CD1 
4318 C CD2 . LEU C 112 ? 0.2999 0.2546 0.5278 -0.0213 0.0752  0.0516  103 LEU C CD2 
4319 N N   . LEU C 113 ? 0.3624 0.4201 0.5118 0.0035  0.0465  0.1324  104 LEU C N   
4320 C CA  . LEU C 113 ? 0.3322 0.4150 0.4467 0.0167  0.0501  0.1319  104 LEU C CA  
4321 C C   . LEU C 113 ? 0.3144 0.4347 0.4138 0.0298  0.0434  0.1408  104 LEU C C   
4322 O O   . LEU C 113 ? 0.3408 0.4643 0.4127 0.0484  0.0445  0.1274  104 LEU C O   
4323 C CB  . LEU C 113 ? 0.3053 0.4114 0.4196 0.0078  0.0524  0.1429  104 LEU C CB  
4324 C CG  . LEU C 113 ? 0.2796 0.4265 0.3667 0.0240  0.0537  0.1432  104 LEU C CG  
4325 C CD1 . LEU C 113 ? 0.2684 0.3845 0.3253 0.0446  0.0565  0.1219  104 LEU C CD1 
4326 C CD2 . LEU C 113 ? 0.3011 0.4729 0.3963 0.0108  0.0548  0.1515  104 LEU C CD2 
4327 N N   . MET C 114 ? 0.3039 0.4492 0.4173 0.0200  0.0356  0.1630  105 MET C N   
4328 C CA  . MET C 114 ? 0.3050 0.4893 0.3994 0.0299  0.0297  0.1719  105 MET C CA  
4329 C C   . MET C 114 ? 0.3308 0.4932 0.4188 0.0426  0.0242  0.1540  105 MET C C   
4330 O O   . MET C 114 ? 0.3204 0.5034 0.3802 0.0591  0.0236  0.1440  105 MET C O   
4331 C CB  . MET C 114 ? 0.2684 0.4762 0.3740 0.0119  0.0210  0.2034  105 MET C CB  
4332 C CG  . MET C 114 ? 0.3151 0.5613 0.4193 -0.0030 0.0272  0.2213  105 MET C CG  
4333 S SD  . MET C 114 ? 0.4037 0.6699 0.5137 -0.0319 0.0169  0.2620  105 MET C SD  
4334 C CE  . MET C 114 ? 0.3545 0.5435 0.5017 -0.0441 0.0047  0.2641  105 MET C CE  
4335 N N   . ALA C 115 ? 0.2654 0.3889 0.3807 0.0353  0.0202  0.1463  106 ALA C N   
4336 C CA  . ALA C 115 ? 0.3174 0.4249 0.4307 0.0436  0.0152  0.1266  106 ALA C CA  
4337 C C   . ALA C 115 ? 0.3311 0.4171 0.4165 0.0539  0.0250  0.1015  106 ALA C C   
4338 O O   . ALA C 115 ? 0.3710 0.4615 0.4314 0.0665  0.0208  0.0890  106 ALA C O   
4339 C CB  . ALA C 115 ? 0.3057 0.3857 0.4605 0.0340  0.0103  0.1200  106 ALA C CB  
4340 N N   . ALA C 116 ? 0.3495 0.4081 0.4346 0.0487  0.0364  0.0942  107 ALA C N   
4341 C CA  . ALA C 116 ? 0.3638 0.3909 0.4168 0.0574  0.0427  0.0742  107 ALA C CA  
4342 C C   . ALA C 116 ? 0.3924 0.4437 0.4089 0.0804  0.0394  0.0732  107 ALA C C   
4343 O O   . ALA C 116 ? 0.4323 0.4612 0.4205 0.0935  0.0367  0.0553  107 ALA C O   
4344 C CB  . ALA C 116 ? 0.3023 0.2995 0.3536 0.0479  0.0537  0.0712  107 ALA C CB  
4345 N N   . ASN C 117 ? 0.3622 0.4607 0.3800 0.0851  0.0395  0.0903  108 ASN C N   
4346 C CA  . ASN C 117 ? 0.3519 0.4878 0.3407 0.1089  0.0380  0.0861  108 ASN C CA  
4347 C C   . ASN C 117 ? 0.3877 0.5433 0.3631 0.1184  0.0306  0.0795  108 ASN C C   
4348 O O   . ASN C 117 ? 0.3741 0.5283 0.3190 0.1412  0.0282  0.0599  108 ASN C O   
4349 C CB  . ASN C 117 ? 0.3349 0.5302 0.3334 0.1062  0.0414  0.1059  108 ASN C CB  
4350 C CG  . ASN C 117 ? 0.3497 0.5906 0.3232 0.1334  0.0425  0.0963  108 ASN C CG  
4351 O OD1 . ASN C 117 ? 0.4245 0.6367 0.3742 0.1569  0.0407  0.0753  108 ASN C OD1 
4352 N ND2 . ASN C 117 ? 0.3396 0.6513 0.3169 0.1310  0.0448  0.1107  108 ASN C ND2 
4353 N N   . PHE C 118 ? 0.3601 0.5329 0.3557 0.1027  0.0247  0.0947  109 PHE C N   
4354 C CA  . PHE C 118 ? 0.3538 0.5458 0.3337 0.1101  0.0153  0.0887  109 PHE C CA  
4355 C C   . PHE C 118 ? 0.4143 0.5565 0.3839 0.1149  0.0104  0.0605  109 PHE C C   
4356 O O   . PHE C 118 ? 0.4244 0.5735 0.3662 0.1294  0.0041  0.0430  109 PHE C O   
4357 C CB  . PHE C 118 ? 0.3512 0.5644 0.3537 0.0923  0.0060  0.1138  109 PHE C CB  
4358 C CG  . PHE C 118 ? 0.4023 0.6277 0.3910 0.0968  -0.0076 0.1073  109 PHE C CG  
4359 C CD1 . PHE C 118 ? 0.3665 0.6438 0.3223 0.1067  -0.0100 0.1113  109 PHE C CD1 
4360 C CD2 . PHE C 118 ? 0.3694 0.5609 0.3781 0.0903  -0.0179 0.0953  109 PHE C CD2 
4361 C CE1 . PHE C 118 ? 0.4207 0.7105 0.3593 0.1103  -0.0238 0.1042  109 PHE C CE1 
4362 C CE2 . PHE C 118 ? 0.4109 0.6175 0.4073 0.0940  -0.0330 0.0881  109 PHE C CE2 
4363 C CZ  . PHE C 118 ? 0.4628 0.7160 0.4218 0.1041  -0.0369 0.0930  109 PHE C CZ  
4364 N N   . LEU C 119 ? 0.3781 0.4715 0.3686 0.1005  0.0137  0.0544  110 LEU C N   
4365 C CA  . LEU C 119 ? 0.4240 0.4727 0.4095 0.0960  0.0102  0.0301  110 LEU C CA  
4366 C C   . LEU C 119 ? 0.4626 0.4635 0.4129 0.1068  0.0154  0.0106  110 LEU C C   
4367 O O   . LEU C 119 ? 0.4796 0.4361 0.4189 0.0998  0.0127  -0.0094 110 LEU C O   
4368 C CB  . LEU C 119 ? 0.4037 0.4309 0.4312 0.0722  0.0127  0.0315  110 LEU C CB  
4369 C CG  . LEU C 119 ? 0.3679 0.4302 0.4330 0.0645  0.0023  0.0483  110 LEU C CG  
4370 C CD1 . LEU C 119 ? 0.3480 0.3924 0.4595 0.0468  0.0068  0.0467  110 LEU C CD1 
4371 C CD2 . LEU C 119 ? 0.3961 0.4782 0.4534 0.0695  -0.0140 0.0394  110 LEU C CD2 
4372 N N   . ASP C 120 ? 0.4784 0.4869 0.4109 0.1229  0.0209  0.0165  111 ASP C N   
4373 C CA  . ASP C 120 ? 0.5310 0.4896 0.4296 0.1367  0.0226  0.0027  111 ASP C CA  
4374 C C   . ASP C 120 ? 0.5491 0.4412 0.4484 0.1129  0.0276  -0.0037 111 ASP C C   
4375 O O   . ASP C 120 ? 0.5985 0.4366 0.4711 0.1110  0.0236  -0.0218 111 ASP C O   
4376 C CB  . ASP C 120 ? 0.5799 0.5289 0.4398 0.1638  0.0132  -0.0199 111 ASP C CB  
4377 C CG  . ASP C 120 ? 0.6984 0.5901 0.5205 0.1840  0.0107  -0.0323 111 ASP C CG  
4378 O OD1 . ASP C 120 ? 0.7470 0.5823 0.5370 0.1917  0.0022  -0.0542 111 ASP C OD1 
4379 O OD2 . ASP C 120 ? 0.7050 0.6042 0.5292 0.1906  0.0152  -0.0195 111 ASP C OD2 
4380 N N   . CYS C 121 ? 0.5012 0.3977 0.4297 0.0925  0.0371  0.0105  112 CYS C N   
4381 C CA  . CYS C 121 ? 0.5187 0.3644 0.4498 0.0667  0.0456  0.0041  112 CYS C CA  
4382 C C   . CYS C 121 ? 0.4821 0.3240 0.4202 0.0572  0.0561  0.0169  112 CYS C C   
4383 O O   . CYS C 121 ? 0.4507 0.2517 0.3815 0.0366  0.0655  0.0124  112 CYS C O   
4384 C CB  . CYS C 121 ? 0.4617 0.3215 0.4330 0.0440  0.0465  -0.0022 112 CYS C CB  
4385 S SG  . CYS C 121 ? 0.4202 0.3320 0.4493 0.0340  0.0501  0.0152  112 CYS C SG  
4386 O OXT . CYS C 121 ? 0.4474 0.3287 0.3965 0.0673  0.0557  0.0311  112 CYS C OXT 
4387 N N   . MET D 1   ? 2.0183 2.1685 1.0943 -0.0457 -0.6118 -0.4608 1   MET D N   
4388 C CA  . MET D 1   ? 2.0503 2.1859 1.0757 -0.0329 -0.5353 -0.4440 1   MET D CA  
4389 C C   . MET D 1   ? 1.9706 2.1246 1.1056 -0.0375 -0.5085 -0.4513 1   MET D C   
4390 O O   . MET D 1   ? 1.9013 2.0915 1.1531 -0.0543 -0.5444 -0.4570 1   MET D O   
4391 C CB  . MET D 1   ? 2.0810 2.2285 1.0447 -0.0217 -0.5116 -0.3817 1   MET D CB  
4392 C CG  . MET D 1   ? 2.0370 2.2256 1.0939 -0.0134 -0.4957 -0.3448 1   MET D CG  
4393 S SD  . MET D 1   ? 2.0737 2.2596 1.0659 -0.0011 -0.4745 -0.2698 1   MET D SD  
4394 C CE  . MET D 1   ? 1.8962 2.0329 0.7489 -0.0082 -0.4052 -0.2645 1   MET D CE  
4395 N N   . GLN D 2   ? 1.9296 2.0647 1.0319 -0.0270 -0.4445 -0.4506 2   GLN D N   
4396 C CA  . GLN D 2   ? 1.8107 1.9489 1.0136 -0.0384 -0.4081 -0.4424 2   GLN D CA  
4397 C C   . GLN D 2   ? 1.7769 1.9194 0.9476 -0.0230 -0.3373 -0.3986 2   GLN D C   
4398 O O   . GLN D 2   ? 1.7563 1.8962 0.8157 -0.0032 -0.3131 -0.3960 2   GLN D O   
4399 C CB  . GLN D 2   ? 1.8648 1.9534 1.0952 -0.0475 -0.4147 -0.4978 2   GLN D CB  
4400 C CG  . GLN D 2   ? 1.8882 1.9718 1.2436 -0.0860 -0.4569 -0.5056 2   GLN D CG  
4401 C CD  . GLN D 2   ? 1.9121 1.9306 1.3057 -0.0987 -0.4588 -0.5426 2   GLN D CD  
4402 O OE1 . GLN D 2   ? 1.9336 1.9138 1.2646 -0.0707 -0.4345 -0.5758 2   GLN D OE1 
4403 N NE2 . GLN D 2   ? 1.9053 1.9125 1.4069 -0.1426 -0.4897 -0.5374 2   GLN D NE2 
4404 N N   . ILE D 3   ? 1.6190 1.7681 0.8873 -0.0371 -0.3040 -0.3621 3   ILE D N   
4405 C CA  . ILE D 3   ? 1.4688 1.6149 0.7278 -0.0265 -0.2420 -0.3223 3   ILE D CA  
4406 C C   . ILE D 3   ? 1.4577 1.5740 0.8049 -0.0448 -0.2184 -0.3225 3   ILE D C   
4407 O O   . ILE D 3   ? 1.4220 1.5251 0.8405 -0.0715 -0.2484 -0.3406 3   ILE D O   
4408 C CB  . ILE D 3   ? 1.4456 1.6264 0.7156 -0.0216 -0.2326 -0.2627 3   ILE D CB  
4409 C CG1 . ILE D 3   ? 1.3801 1.5916 0.7678 -0.0425 -0.2505 -0.2481 3   ILE D CG1 
4410 C CG2 . ILE D 3   ? 1.4927 1.6871 0.6662 -0.0054 -0.2655 -0.2549 3   ILE D CG2 
4411 C CD1 . ILE D 3   ? 1.3106 1.5566 0.7210 -0.0305 -0.2450 -0.2015 3   ILE D CD1 
4412 N N   . PHE D 4   ? 1.3637 1.4656 0.7037 -0.0341 -0.1687 -0.2992 4   PHE D N   
4413 C CA  . PHE D 4   ? 1.3678 1.4324 0.7796 -0.0501 -0.1494 -0.2898 4   PHE D CA  
4414 C C   . PHE D 4   ? 1.2686 1.3472 0.7072 -0.0534 -0.1128 -0.2299 4   PHE D C   
4415 O O   . PHE D 4   ? 1.2477 1.3507 0.6392 -0.0338 -0.0904 -0.2017 4   PHE D O   
4416 C CB  . PHE D 4   ? 1.4033 1.4278 0.7949 -0.0305 -0.1316 -0.3274 4   PHE D CB  
4417 C CG  . PHE D 4   ? 1.4269 1.4439 0.7650 -0.0133 -0.1575 -0.3947 4   PHE D CG  
4418 C CD1 . PHE D 4   ? 1.4877 1.4750 0.8555 -0.0308 -0.2111 -0.4343 4   PHE D CD1 
4419 C CD2 . PHE D 4   ? 1.4945 1.5348 0.7511 0.0177  -0.1272 -0.4206 4   PHE D CD2 
4420 C CE1 . PHE D 4   ? 1.5406 1.5141 0.8538 -0.0123 -0.2397 -0.5027 4   PHE D CE1 
4421 C CE2 . PHE D 4   ? 1.5589 1.5947 0.7550 0.0351  -0.1475 -0.4899 4   PHE D CE2 
4422 C CZ  . PHE D 4   ? 1.5965 1.5947 0.8192 0.0229  -0.2065 -0.5333 4   PHE D CZ  
4423 N N   . VAL D 5   ? 1.2383 1.2963 0.7465 -0.0814 -0.1094 -0.2096 5   VAL D N   
4424 C CA  . VAL D 5   ? 1.2110 1.2673 0.7386 -0.0844 -0.0749 -0.1611 5   VAL D CA  
4425 C C   . VAL D 5   ? 1.2417 1.2337 0.7958 -0.0970 -0.0668 -0.1606 5   VAL D C   
4426 O O   . VAL D 5   ? 1.2957 1.2485 0.8828 -0.1226 -0.0938 -0.1815 5   VAL D O   
4427 C CB  . VAL D 5   ? 1.1986 1.2976 0.7747 -0.1063 -0.0765 -0.1339 5   VAL D CB  
4428 C CG1 . VAL D 5   ? 1.1554 1.3129 0.7212 -0.0913 -0.1019 -0.1439 5   VAL D CG1 
4429 C CG2 . VAL D 5   ? 1.1940 1.2786 0.8316 -0.1526 -0.0890 -0.1381 5   VAL D CG2 
4430 N N   . LYS D 6   ? 1.1792 1.1546 0.7194 -0.0789 -0.0371 -0.1377 6   LYS D N   
4431 C CA  . LYS D 6   ? 1.2316 1.1437 0.7980 -0.0833 -0.0354 -0.1366 6   LYS D CA  
4432 C C   . LYS D 6   ? 1.1518 1.0550 0.7238 -0.0884 -0.0107 -0.0856 6   LYS D C   
4433 O O   . LYS D 6   ? 1.0851 1.0247 0.6316 -0.0681 0.0128  -0.0631 6   LYS D O   
4434 C CB  . LYS D 6   ? 1.2417 1.1461 0.7934 -0.0481 -0.0281 -0.1760 6   LYS D CB  
4435 C CG  . LYS D 6   ? 1.3235 1.1593 0.9200 -0.0452 -0.0423 -0.1931 6   LYS D CG  
4436 C CD  . LYS D 6   ? 1.4236 1.2024 1.0476 -0.0597 -0.0901 -0.2361 6   LYS D CD  
4437 C CE  . LYS D 6   ? 1.5001 1.2208 1.1655 -0.0347 -0.1087 -0.2753 6   LYS D CE  
4438 N NZ  . LYS D 6   ? 1.4379 1.0840 1.1333 -0.0472 -0.1676 -0.3193 6   LYS D NZ  
4439 N N   . THR D 7   ? 1.2435 1.0922 0.8418 -0.1188 -0.0210 -0.0657 7   THR D N   
4440 C CA  . THR D 7   ? 1.2197 1.0416 0.8155 -0.1226 -0.0043 -0.0237 7   THR D CA  
4441 C C   . THR D 7   ? 1.2584 1.0387 0.8663 -0.0971 -0.0055 -0.0311 7   THR D C   
4442 O O   . THR D 7   ? 1.3008 1.0777 0.9225 -0.0763 -0.0155 -0.0728 7   THR D O   
4443 C CB  . THR D 7   ? 1.1542 0.9333 0.7578 -0.1705 -0.0153 0.0025  7   THR D CB  
4444 O OG1 . THR D 7   ? 1.1965 0.9015 0.8186 -0.1920 -0.0512 -0.0122 7   THR D OG1 
4445 C CG2 . THR D 7   ? 1.0464 0.8876 0.6562 -0.1964 -0.0079 0.0035  7   THR D CG2 
4446 N N   . LEU D 8   ? 1.2079 0.9613 0.8155 -0.0963 0.0040  0.0046  8   LEU D N   
4447 C CA  . LEU D 8   ? 1.2041 0.9268 0.8402 -0.0723 0.0004  -0.0023 8   LEU D CA  
4448 C C   . LEU D 8   ? 1.2967 0.9439 0.9691 -0.0807 -0.0404 -0.0267 8   LEU D C   
4449 O O   . LEU D 8   ? 1.2937 0.9367 1.0062 -0.0506 -0.0482 -0.0639 8   LEU D O   
4450 C CB  . LEU D 8   ? 1.1970 0.8993 0.8278 -0.0733 0.0094  0.0424  8   LEU D CB  
4451 C CG  . LEU D 8   ? 1.0751 0.7940 0.7361 -0.0430 0.0227  0.0432  8   LEU D CG  
4452 C CD1 . LEU D 8   ? 1.0536 0.7215 0.7729 -0.0323 -0.0054 0.0193  8   LEU D CD1 
4453 C CD2 . LEU D 8   ? 1.1145 0.9160 0.7650 -0.0194 0.0546  0.0219  8   LEU D CD2 
4454 N N   . THR D 9   ? 1.3629 0.9505 1.0238 -0.1228 -0.0682 -0.0077 9   THR D N   
4455 C CA  . THR D 9   ? 1.3717 0.8679 1.0611 -0.1376 -0.1193 -0.0227 9   THR D CA  
4456 C C   . THR D 9   ? 1.4119 0.9144 1.1237 -0.1273 -0.1400 -0.0781 9   THR D C   
4457 O O   . THR D 9   ? 1.3925 0.8259 1.1432 -0.1179 -0.1846 -0.1090 9   THR D O   
4458 C CB  . THR D 9   ? 1.3079 0.7353 0.9640 -0.1972 -0.1425 0.0232  9   THR D CB  
4459 O OG1 . THR D 9   ? 1.3954 0.8488 1.0397 -0.2325 -0.1425 0.0165  9   THR D OG1 
4460 C CG2 . THR D 9   ? 1.2618 0.7088 0.8759 -0.2095 -0.1102 0.0710  9   THR D CG2 
4461 N N   . GLY D 10  ? 1.4390 1.0162 1.1285 -0.1266 -0.1159 -0.0946 10  GLY D N   
4462 C CA  . GLY D 10  ? 1.4701 1.0486 1.1723 -0.1193 -0.1406 -0.1486 10  GLY D CA  
4463 C C   . GLY D 10  ? 1.5004 1.1070 1.1844 -0.1583 -0.1460 -0.1422 10  GLY D C   
4464 O O   . GLY D 10  ? 1.4940 1.1657 1.1548 -0.1701 -0.1130 -0.1119 10  GLY D O   
4465 N N   . LYS D 11  ? 1.5090 1.0670 1.2130 -0.1770 -0.1921 -0.1741 11  LYS D N   
4466 C CA  . LYS D 11  ? 1.5626 1.1408 1.2666 -0.2222 -0.2070 -0.1695 11  LYS D CA  
4467 C C   . LYS D 11  ? 1.5239 1.2051 1.2075 -0.1987 -0.1798 -0.1917 11  LYS D C   
4468 O O   . LYS D 11  ? 1.5263 1.2744 1.2027 -0.2155 -0.1527 -0.1613 11  LYS D O   
4469 C CB  . LYS D 11  ? 1.4779 1.0478 1.1771 -0.2821 -0.1963 -0.1067 11  LYS D CB  
4470 N N   . THR D 12  ? 1.4800 1.1712 1.1533 -0.1587 -0.1923 -0.2498 12  THR D N   
4471 C CA  . THR D 12  ? 1.4770 1.2489 1.1182 -0.1403 -0.1810 -0.2732 12  THR D CA  
4472 C C   . THR D 12  ? 1.5377 1.3339 1.2029 -0.1867 -0.2050 -0.2620 12  THR D C   
4473 O O   . THR D 12  ? 1.5767 1.3174 1.2782 -0.2272 -0.2461 -0.2678 12  THR D O   
4474 C CB  . THR D 12  ? 1.5041 1.2727 1.1198 -0.1000 -0.1995 -0.3447 12  THR D CB  
4475 O OG1 . THR D 12  ? 1.5867 1.2908 1.2260 -0.0767 -0.2111 -0.3759 12  THR D OG1 
4476 C CG2 . THR D 12  ? 1.4062 1.2519 0.9644 -0.0650 -0.1583 -0.3452 12  THR D CG2 
4477 N N   . ILE D 13  ? 1.4122 1.3067 1.2693 -0.4489 -0.2787 -0.1473 13  ILE D N   
4478 C CA  . ILE D 13  ? 1.3883 1.3614 1.2773 -0.4640 -0.2888 -0.1499 13  ILE D CA  
4479 C C   . ILE D 13  ? 1.3760 1.4232 1.2569 -0.4580 -0.3128 -0.1447 13  ILE D C   
4480 O O   . ILE D 13  ? 1.3632 1.4406 1.2502 -0.4259 -0.3214 -0.1164 13  ILE D O   
4481 C CB  . ILE D 13  ? 1.3794 1.3646 1.3083 -0.4450 -0.2806 -0.1274 13  ILE D CB  
4482 C CG1 . ILE D 13  ? 1.4129 1.3040 1.3293 -0.4419 -0.2588 -0.1279 13  ILE D CG1 
4483 C CG2 . ILE D 13  ? 1.4162 1.4745 1.3914 -0.4673 -0.2847 -0.1385 13  ILE D CG2 
4484 C CD1 . ILE D 13  ? 1.5251 1.3692 1.4254 -0.4794 -0.2466 -0.1591 13  ILE D CD1 
4485 N N   . THR D 14  ? 1.3549 1.4258 1.2164 -0.4878 -0.3245 -0.1721 14  THR D N   
4486 C CA  . THR D 14  ? 1.3567 1.4903 1.1988 -0.4829 -0.3518 -0.1702 14  THR D CA  
4487 C C   . THR D 14  ? 1.3393 1.5608 1.2350 -0.4816 -0.3736 -0.1666 14  THR D C   
4488 O O   . THR D 14  ? 1.2892 1.5334 1.2294 -0.5081 -0.3691 -0.1873 14  THR D O   
4489 C CB  . THR D 14  ? 1.3897 1.5160 1.1914 -0.5144 -0.3577 -0.2030 14  THR D CB  
4490 O OG1 . THR D 14  ? 1.4307 1.5967 1.2767 -0.5292 -0.3563 -0.2265 14  THR D OG1 
4491 C CG2 . THR D 14  ? 1.2810 1.3171 1.0587 -0.5115 -0.3240 -0.2119 14  THR D CG2 
4492 N N   . LEU D 15  ? 1.3206 1.5882 1.2158 -0.4501 -0.3953 -0.1410 15  LEU D N   
4493 C CA  . LEU D 15  ? 1.2972 1.6485 1.2529 -0.4422 -0.4183 -0.1352 15  LEU D CA  
4494 C C   . LEU D 15  ? 1.3284 1.7394 1.2588 -0.4338 -0.4610 -0.1372 15  LEU D C   
4495 O O   . LEU D 15  ? 1.3720 1.7560 1.2354 -0.4124 -0.4681 -0.1205 15  LEU D O   
4496 C CB  . LEU D 15  ? 1.2612 1.6129 1.2508 -0.4059 -0.4071 -0.0986 15  LEU D CB  
4497 C CG  . LEU D 15  ? 1.2990 1.6010 1.3209 -0.4105 -0.3708 -0.0954 15  LEU D CG  
4498 C CD1 . LEU D 15  ? 1.2018 1.5218 1.2610 -0.3745 -0.3666 -0.0612 15  LEU D CD1 
4499 C CD2 . LEU D 15  ? 1.2823 1.6027 1.3504 -0.4491 -0.3613 -0.1270 15  LEU D CD2 
4500 N N   . GLU D 16  ? 1.3337 1.8216 1.3176 -0.4500 -0.4892 -0.1590 16  GLU D N   
4501 C CA  . GLU D 16  ? 1.3628 1.9132 1.3308 -0.4386 -0.5391 -0.1627 16  GLU D CA  
4502 C C   . GLU D 16  ? 1.3309 1.9264 1.3337 -0.3967 -0.5589 -0.1287 16  GLU D C   
4503 O O   . GLU D 16  ? 1.2524 1.8898 1.3426 -0.3947 -0.5524 -0.1261 16  GLU D O   
4504 C CB  . GLU D 16  ? 1.2758 1.8907 1.2962 -0.4739 -0.5645 -0.2058 16  GLU D CB  
4505 N N   . VAL D 17  ? 1.4296 2.0121 1.3625 -0.3636 -0.5801 -0.1032 17  VAL D N   
4506 C CA  . VAL D 17  ? 1.4658 2.0734 1.4152 -0.3193 -0.5939 -0.0653 17  VAL D CA  
4507 C C   . VAL D 17  ? 1.5687 2.1838 1.4384 -0.2943 -0.6386 -0.0551 17  VAL D C   
4508 O O   . VAL D 17  ? 1.6495 2.2387 1.4440 -0.3109 -0.6512 -0.0749 17  VAL D O   
4509 C CB  . VAL D 17  ? 1.5369 2.0772 1.4717 -0.2974 -0.5471 -0.0310 17  VAL D CB  
4510 C CG1 . VAL D 17  ? 1.5192 1.9824 1.3484 -0.2854 -0.5326 -0.0173 17  VAL D CG1 
4511 C CG2 . VAL D 17  ? 1.5528 2.1303 1.5425 -0.2599 -0.5524 0.0024  17  VAL D CG2 
4512 N N   . GLU D 18  ? 1.5771 2.2242 1.4594 -0.2539 -0.6632 -0.0247 18  GLU D N   
4513 C CA  . GLU D 18  ? 1.6244 2.2644 1.4202 -0.2215 -0.7034 -0.0066 18  GLU D CA  
4514 C C   . GLU D 18  ? 1.6330 2.2380 1.4073 -0.1776 -0.6826 0.0416  18  GLU D C   
4515 O O   . GLU D 18  ? 1.5727 2.1903 1.4248 -0.1694 -0.6546 0.0576  18  GLU D O   
4516 C CB  . GLU D 18  ? 1.5783 2.3063 1.4181 -0.2140 -0.7719 -0.0238 18  GLU D CB  
4517 C CG  . GLU D 18  ? 1.6498 2.4146 1.5060 -0.2558 -0.7996 -0.0749 18  GLU D CG  
4518 C CD  . GLU D 18  ? 1.7051 2.4160 1.4297 -0.2633 -0.8175 -0.0872 18  GLU D CD  
4519 O OE1 . GLU D 18  ? 1.7826 2.4427 1.4029 -0.2300 -0.8267 -0.0574 18  GLU D OE1 
4520 O OE2 . GLU D 18  ? 1.6348 2.3417 1.3617 -0.2969 -0.8120 -0.1286 18  GLU D OE2 
4521 N N   . PRO D 19  ? 1.6859 2.2404 1.3513 -0.1490 -0.6924 0.0652  19  PRO D N   
4522 C CA  . PRO D 19  ? 1.6208 2.1297 1.2615 -0.1098 -0.6625 0.1102  19  PRO D CA  
4523 C C   . PRO D 19  ? 1.5850 2.1571 1.3112 -0.0775 -0.6825 0.1347  19  PRO D C   
4524 O O   . PRO D 19  ? 1.5255 2.0709 1.2704 -0.0539 -0.6470 0.1664  19  PRO D O   
4525 C CB  . PRO D 19  ? 1.6358 2.0825 1.1375 -0.0878 -0.6764 0.1254  19  PRO D CB  
4526 C CG  . PRO D 19  ? 1.7055 2.1899 1.1738 -0.1041 -0.7341 0.0934  19  PRO D CG  
4527 C CD  . PRO D 19  ? 1.6477 2.1746 1.2011 -0.1517 -0.7260 0.0518  19  PRO D CD  
4528 N N   . SER D 20  ? 1.6024 2.2581 1.3870 -0.0757 -0.7383 0.1190  20  SER D N   
4529 C CA  . SER D 20  ? 1.5205 2.2408 1.3977 -0.0460 -0.7582 0.1388  20  SER D CA  
4530 C C   . SER D 20  ? 1.4707 2.2154 1.4641 -0.0629 -0.7140 0.1357  20  SER D C   
4531 O O   . SER D 20  ? 1.3936 2.1661 1.4515 -0.0358 -0.7090 0.1608  20  SER D O   
4532 C CB  . SER D 20  ? 1.5057 2.3108 1.4277 -0.0423 -0.8311 0.1156  20  SER D CB  
4533 O OG  . SER D 20  ? 1.4818 2.3278 1.4601 -0.0883 -0.8378 0.0683  20  SER D OG  
4534 N N   . ASP D 21  ? 1.5667 2.2966 1.5827 -0.1062 -0.6818 0.1057  21  ASP D N   
4535 C CA  . ASP D 21  ? 1.5136 2.2548 1.6256 -0.1235 -0.6399 0.1009  21  ASP D CA  
4536 C C   . ASP D 21  ? 1.4866 2.1680 1.5832 -0.0987 -0.5929 0.1380  21  ASP D C   
4537 O O   . ASP D 21  ? 1.5278 2.1352 1.5385 -0.0913 -0.5695 0.1522  21  ASP D O   
4538 C CB  . ASP D 21  ? 1.5115 2.2311 1.6290 -0.1730 -0.6144 0.0629  21  ASP D CB  
4539 C CG  . ASP D 21  ? 1.5522 2.3354 1.7026 -0.2014 -0.6562 0.0218  21  ASP D CG  
4540 O OD1 . ASP D 21  ? 1.6107 2.3930 1.6886 -0.1988 -0.6948 0.0131  21  ASP D OD1 
4541 O OD2 . ASP D 21  ? 1.5378 2.3682 1.7856 -0.2267 -0.6487 -0.0033 21  ASP D OD2 
4542 N N   . THR D 22  ? 1.2911 2.0039 1.4761 -0.0870 -0.5773 0.1512  22  THR D N   
4543 C CA  . THR D 22  ? 1.2761 1.9390 1.4598 -0.0632 -0.5349 0.1839  22  THR D CA  
4544 C C   . THR D 22  ? 1.2455 1.8406 1.4169 -0.0915 -0.4862 0.1704  22  THR D C   
4545 O O   . THR D 22  ? 1.2402 1.8322 1.4152 -0.1298 -0.4826 0.1369  22  THR D O   
4546 C CB  . THR D 22  ? 1.1991 1.9169 1.4817 -0.0433 -0.5343 0.1995  22  THR D CB  
4547 O OG1 . THR D 22  ? 1.1155 1.8679 1.4823 -0.0775 -0.5213 0.1694  22  THR D OG1 
4548 C CG2 . THR D 22  ? 1.0799 1.8649 1.3801 -0.0127 -0.5879 0.2116  22  THR D CG2 
4549 N N   . ILE D 23  ? 1.4392 1.6310 1.2736 0.0370  -0.5404 -0.0555 23  ILE D N   
4550 C CA  . ILE D 23  ? 1.4346 1.5964 1.2630 0.0041  -0.4765 -0.0583 23  ILE D CA  
4551 C C   . ILE D 23  ? 1.3819 1.5870 1.3289 -0.0190 -0.4508 -0.0904 23  ILE D C   
4552 O O   . ILE D 23  ? 1.3129 1.5041 1.2613 -0.0517 -0.4118 -0.1075 23  ILE D O   
4553 C CB  . ILE D 23  ? 1.3765 1.4801 1.1458 0.0123  -0.4393 -0.0154 23  ILE D CB  
4554 C CG1 . ILE D 23  ? 1.3944 1.4564 1.0385 0.0259  -0.4601 0.0157  23  ILE D CG1 
4555 C CG2 . ILE D 23  ? 1.2791 1.3625 1.0441 -0.0157 -0.3778 -0.0218 23  ILE D CG2 
4556 C CD1 . ILE D 23  ? 1.3969 1.4580 0.9642 0.0091  -0.4606 -0.0030 23  ILE D CD1 
4557 N N   . GLU D 24  ? 1.3725 1.6299 1.4164 -0.0017 -0.4724 -0.1001 24  GLU D N   
4558 C CA  . GLU D 24  ? 1.2550 1.5714 1.4157 -0.0284 -0.4510 -0.1377 24  GLU D CA  
4559 C C   . GLU D 24  ? 1.2391 1.5930 1.4212 -0.0632 -0.4660 -0.1813 24  GLU D C   
4560 O O   . GLU D 24  ? 1.1706 1.5321 1.3963 -0.1058 -0.4281 -0.2061 24  GLU D O   
4561 C CB  . GLU D 24  ? 1.2110 1.5901 1.4732 0.0032  -0.4777 -0.1468 24  GLU D CB  
4562 N N   . ASN D 25  ? 1.3122 1.6853 1.4587 -0.0478 -0.5212 -0.1914 25  ASN D N   
4563 C CA  . ASN D 25  ? 1.2135 1.6151 1.3691 -0.0828 -0.5372 -0.2357 25  ASN D CA  
4564 C C   . ASN D 25  ? 1.2269 1.5512 1.3028 -0.1168 -0.4952 -0.2342 25  ASN D C   
4565 O O   . ASN D 25  ? 1.1793 1.5038 1.2867 -0.1613 -0.4749 -0.2683 25  ASN D O   
4566 C CB  . ASN D 25  ? 1.3037 1.7365 1.4194 -0.0544 -0.6057 -0.2441 25  ASN D CB  
4567 C CG  . ASN D 25  ? 1.2949 1.8347 1.5202 -0.0392 -0.6552 -0.2803 25  ASN D CG  
4568 O OD1 . ASN D 25  ? 1.2038 1.8058 1.5424 -0.0651 -0.6357 -0.3137 25  ASN D OD1 
4569 N ND2 . ASN D 25  ? 1.2481 1.8127 1.4361 0.0023  -0.7153 -0.2736 25  ASN D ND2 
4570 N N   . VAL D 26  ? 1.2858 1.5423 1.2557 -0.0964 -0.4822 -0.1971 26  VAL D N   
4571 C CA  . VAL D 26  ? 1.2793 1.4681 1.1712 -0.1176 -0.4479 -0.1993 26  VAL D CA  
4572 C C   . VAL D 26  ? 1.2500 1.4096 1.1784 -0.1438 -0.3897 -0.1975 26  VAL D C   
4573 O O   . VAL D 26  ? 1.2724 1.3876 1.1759 -0.1725 -0.3662 -0.2162 26  VAL D O   
4574 C CB  . VAL D 26  ? 1.2468 1.3896 1.0240 -0.0889 -0.4472 -0.1653 26  VAL D CB  
4575 C CG1 . VAL D 26  ? 1.2142 1.3014 0.9138 -0.1030 -0.4222 -0.1788 26  VAL D CG1 
4576 C CG2 . VAL D 26  ? 1.2999 1.4711 1.0358 -0.0626 -0.5046 -0.1606 26  VAL D CG2 
4577 N N   . LYS D 27  ? 1.2017 1.3795 1.1829 -0.1328 -0.3667 -0.1750 27  LYS D N   
4578 C CA  . LYS D 27  ? 1.1774 1.3407 1.2011 -0.1593 -0.3140 -0.1766 27  LYS D CA  
4579 C C   . LYS D 27  ? 1.1545 1.3558 1.2611 -0.2027 -0.3114 -0.2164 27  LYS D C   
4580 O O   . LYS D 27  ? 1.1134 1.2763 1.2174 -0.2377 -0.2710 -0.2243 27  LYS D O   
4581 C CB  . LYS D 27  ? 1.0976 1.2821 1.1670 -0.1385 -0.2931 -0.1508 27  LYS D CB  
4582 C CG  . LYS D 27  ? 1.0827 1.2191 1.0711 -0.1115 -0.2746 -0.1129 27  LYS D CG  
4583 C CD  . LYS D 27  ? 0.9961 1.1521 1.0376 -0.0945 -0.2571 -0.0934 27  LYS D CD  
4584 C CE  . LYS D 27  ? 0.9791 1.0891 0.9500 -0.0822 -0.2243 -0.0629 27  LYS D CE  
4585 N NZ  . LYS D 27  ? 0.9591 1.0836 0.9883 -0.0735 -0.1997 -0.0514 27  LYS D NZ  
4586 N N   . ALA D 28  ? 1.1633 1.4405 1.3409 -0.2020 -0.3541 -0.2427 28  ALA D N   
4587 C CA  . ALA D 28  ? 1.1224 1.4501 1.3833 -0.2499 -0.3525 -0.2881 28  ALA D CA  
4588 C C   . ALA D 28  ? 1.1938 1.4607 1.3929 -0.2879 -0.3504 -0.3111 28  ALA D C   
4589 O O   . ALA D 28  ? 1.1886 1.4256 1.4027 -0.3382 -0.3136 -0.3285 28  ALA D O   
4590 C CB  . ALA D 28  ? 0.9931 1.4280 1.3425 -0.2338 -0.4057 -0.3167 28  ALA D CB  
4591 N N   . LYS D 29  ? 1.3020 1.5436 1.4249 -0.2653 -0.3889 -0.3117 29  LYS D N   
4592 C CA  . LYS D 29  ? 1.3535 1.5324 1.4138 -0.2959 -0.3906 -0.3379 29  LYS D CA  
4593 C C   . LYS D 29  ? 1.4363 1.5073 1.4197 -0.3055 -0.3409 -0.3176 29  LYS D C   
4594 O O   . LYS D 29  ? 1.4709 1.4788 1.4291 -0.3456 -0.3247 -0.3408 29  LYS D O   
4595 C CB  . LYS D 29  ? 1.3893 1.5679 1.3772 -0.2631 -0.4404 -0.3420 29  LYS D CB  
4596 C CG  . LYS D 29  ? 1.3746 1.6545 1.4209 -0.2428 -0.4969 -0.3575 29  LYS D CG  
4597 C CD  . LYS D 29  ? 1.4649 1.7359 1.4199 -0.1942 -0.5359 -0.3347 29  LYS D CD  
4598 C CE  . LYS D 29  ? 1.4943 1.8572 1.4953 -0.1641 -0.5956 -0.3416 29  LYS D CE  
4599 N NZ  . LYS D 29  ? 1.4923 1.9145 1.5416 -0.1932 -0.6262 -0.3932 29  LYS D NZ  
4600 N N   . ILE D 30  ? 1.3417 1.3872 1.2837 -0.2685 -0.3181 -0.2760 30  ILE D N   
4601 C CA  . ILE D 30  ? 1.3323 1.2876 1.2049 -0.2697 -0.2740 -0.2579 30  ILE D CA  
4602 C C   . ILE D 30  ? 1.3434 1.2800 1.2658 -0.3163 -0.2322 -0.2642 30  ILE D C   
4603 O O   . ILE D 30  ? 1.3977 1.2456 1.2651 -0.3402 -0.2086 -0.2699 30  ILE D O   
4604 C CB  . ILE D 30  ? 1.2841 1.2380 1.1169 -0.2241 -0.2584 -0.2177 30  ILE D CB  
4605 C CG1 . ILE D 30  ? 1.2514 1.1938 0.9990 -0.1878 -0.2875 -0.2128 30  ILE D CG1 
4606 C CG2 . ILE D 30  ? 1.3013 1.1912 1.0959 -0.2263 -0.2093 -0.2004 30  ILE D CG2 
4607 C CD1 . ILE D 30  ? 1.2256 1.1919 0.9502 -0.1508 -0.2815 -0.1770 30  ILE D CD1 
4608 N N   . GLN D 31  ? 1.2795 1.2962 1.3022 -0.3295 -0.2228 -0.2644 31  GLN D N   
4609 C CA  . GLN D 31  ? 1.2377 1.2507 1.3111 -0.3798 -0.1802 -0.2734 31  GLN D CA  
4610 C C   . GLN D 31  ? 1.3054 1.2924 1.3869 -0.4391 -0.1837 -0.3126 31  GLN D C   
4611 O O   . GLN D 31  ? 1.3173 1.2356 1.3752 -0.4842 -0.1443 -0.3140 31  GLN D O   
4612 C CB  . GLN D 31  ? 1.1260 1.2482 1.3150 -0.3806 -0.1743 -0.2764 31  GLN D CB  
4613 C CG  . GLN D 31  ? 1.0619 1.1921 1.3020 -0.4332 -0.1240 -0.2850 31  GLN D CG  
4614 C CD  . GLN D 31  ? 0.9770 1.2331 1.3461 -0.4378 -0.1231 -0.3037 31  GLN D CD  
4615 O OE1 . GLN D 31  ? 0.9104 1.1907 1.3250 -0.4690 -0.0790 -0.3063 31  GLN D OE1 
4616 N NE2 . GLN D 31  ? 0.9565 1.2945 1.3821 -0.4042 -0.1733 -0.3185 31  GLN D NE2 
4617 N N   . ASP D 32  ? 1.3738 1.4122 1.4844 -0.4420 -0.2306 -0.3453 32  ASP D N   
4618 C CA  . ASP D 32  ? 1.3846 1.3988 1.5011 -0.5012 -0.2367 -0.3887 32  ASP D CA  
4619 C C   . ASP D 32  ? 1.4508 1.3197 1.4453 -0.5070 -0.2265 -0.3844 32  ASP D C   
4620 O O   . ASP D 32  ? 1.4684 1.2677 1.4467 -0.5659 -0.2049 -0.4059 32  ASP D O   
4621 C CB  . ASP D 32  ? 1.3712 1.4789 1.5395 -0.4949 -0.2948 -0.4269 32  ASP D CB  
4622 C CG  . ASP D 32  ? 1.3212 1.5701 1.6046 -0.4749 -0.3148 -0.4325 32  ASP D CG  
4623 O OD1 . ASP D 32  ? 1.3017 1.5743 1.6254 -0.4660 -0.2817 -0.4078 32  ASP D OD1 
4624 O OD2 . ASP D 32  ? 1.2739 1.6100 1.6056 -0.4646 -0.3657 -0.4639 32  ASP D OD2 
4625 N N   . LYS D 33  ? 1.4739 1.2943 1.3807 -0.4474 -0.2410 -0.3592 33  LYS D N   
4626 C CA  . LYS D 33  ? 1.5399 1.2347 1.3329 -0.4389 -0.2410 -0.3625 33  LYS D CA  
4627 C C   . LYS D 33  ? 1.6345 1.2289 1.3525 -0.4219 -0.1986 -0.3267 33  LYS D C   
4628 O O   . LYS D 33  ? 1.6728 1.1502 1.2972 -0.4167 -0.1954 -0.3318 33  LYS D O   
4629 C CB  . LYS D 33  ? 1.4916 1.2037 1.2302 -0.3839 -0.2846 -0.3660 33  LYS D CB  
4630 N N   . GLU D 34  ? 1.5710 1.2075 1.3251 -0.4090 -0.1686 -0.2935 34  GLU D N   
4631 C CA  . GLU D 34  ? 1.5815 1.1333 1.2655 -0.3912 -0.1306 -0.2616 34  GLU D CA  
4632 C C   . GLU D 34  ? 1.4977 1.0734 1.2353 -0.4232 -0.0861 -0.2425 34  GLU D C   
4633 O O   . GLU D 34  ? 1.5499 1.0537 1.2257 -0.4121 -0.0543 -0.2166 34  GLU D O   
4634 C CB  . GLU D 34  ? 1.6041 1.1723 1.2386 -0.3205 -0.1395 -0.2374 34  GLU D CB  
4635 C CG  . GLU D 34  ? 1.6994 1.2060 1.2425 -0.2853 -0.1678 -0.2530 34  GLU D CG  
4636 C CD  . GLU D 34  ? 1.8248 1.1918 1.2781 -0.2913 -0.1529 -0.2584 34  GLU D CD  
4637 O OE1 . GLU D 34  ? 1.8744 1.1906 1.3021 -0.2916 -0.1182 -0.2335 34  GLU D OE1 
4638 O OE2 . GLU D 34  ? 1.8723 1.1757 1.2762 -0.2943 -0.1774 -0.2882 34  GLU D OE2 
4639 N N   . GLY D 35  ? 1.2016 1.4390 1.0989 -0.3464 -0.1120 0.0671  35  GLY D N   
4640 C CA  . GLY D 35  ? 1.0855 1.3957 1.0390 -0.3394 -0.0826 0.0821  35  GLY D CA  
4641 C C   . GLY D 35  ? 1.1010 1.4196 1.0675 -0.2860 -0.0472 0.0688  35  GLY D C   
4642 O O   . GLY D 35  ? 1.0951 1.4147 1.0593 -0.2832 -0.0206 0.0702  35  GLY D O   
4643 N N   . ILE D 36  ? 1.1055 1.4257 1.0772 -0.2498 -0.0480 0.0573  36  ILE D N   
4644 C CA  . ILE D 36  ? 1.0494 1.3697 1.0228 -0.2035 -0.0183 0.0448  36  ILE D CA  
4645 C C   . ILE D 36  ? 1.0083 1.4105 1.0516 -0.1800 -0.0063 0.0566  36  ILE D C   
4646 O O   . ILE D 36  ? 0.9989 1.4206 1.0612 -0.1768 -0.0314 0.0618  36  ILE D O   
4647 C CB  . ILE D 36  ? 1.0700 1.3184 0.9863 -0.1801 -0.0285 0.0231  36  ILE D CB  
4648 C CG1 . ILE D 36  ? 1.0650 1.2335 0.9225 -0.1944 -0.0363 0.0153  36  ILE D CG1 
4649 C CG2 . ILE D 36  ? 0.9957 1.2469 0.9085 -0.1409 -0.0020 0.0140  36  ILE D CG2 
4650 C CD1 . ILE D 36  ? 1.0358 1.1413 0.8450 -0.1728 -0.0454 -0.0037 36  ILE D CD1 
4651 N N   . PRO D 37  ? 0.9738 1.4209 1.0541 -0.1629 0.0326  0.0622  37  PRO D N   
4652 C CA  . PRO D 37  ? 0.9283 1.4479 1.0805 -0.1312 0.0508  0.0749  37  PRO D CA  
4653 C C   . PRO D 37  ? 1.0016 1.4873 1.1339 -0.0940 0.0439  0.0621  37  PRO D C   
4654 O O   . PRO D 37  ? 1.0348 1.4487 1.0984 -0.0834 0.0476  0.0400  37  PRO D O   
4655 C CB  . PRO D 37  ? 0.9557 1.4943 1.1200 -0.1180 0.1047  0.0727  37  PRO D CB  
4656 C CG  . PRO D 37  ? 0.9147 1.4208 1.0333 -0.1596 0.1038  0.0701  37  PRO D CG  
4657 C CD  . PRO D 37  ? 0.9328 1.3619 0.9870 -0.1736 0.0638  0.0583  37  PRO D CD  
4658 N N   . PRO D 38  ? 0.9832 1.5230 1.1755 -0.0759 0.0315  0.0796  38  PRO D N   
4659 C CA  . PRO D 38  ? 0.9959 1.5003 1.1646 -0.0452 0.0203  0.0699  38  PRO D CA  
4660 C C   . PRO D 38  ? 1.0545 1.5142 1.1891 -0.0067 0.0615  0.0515  38  PRO D C   
4661 O O   . PRO D 38  ? 1.0275 1.4352 1.1125 0.0081  0.0505  0.0375  38  PRO D O   
4662 C CB  . PRO D 38  ? 0.9172 1.5020 1.1718 -0.0360 -0.0001 0.1022  38  PRO D CB  
4663 C CG  . PRO D 38  ? 0.8699 1.5433 1.2045 -0.0508 0.0147  0.1292  38  PRO D CG  
4664 C CD  . PRO D 38  ? 0.8858 1.5225 1.1667 -0.0917 0.0160  0.1143  38  PRO D CD  
4665 N N   . ASP D 39  ? 1.3598 1.8337 1.5106 0.0051  0.1091  0.0508  39  ASP D N   
4666 C CA  . ASP D 39  ? 1.3711 1.7878 1.4713 0.0334  0.1490  0.0320  39  ASP D CA  
4667 C C   . ASP D 39  ? 1.3260 1.6649 1.3287 0.0130  0.1435  0.0098  39  ASP D C   
4668 O O   . ASP D 39  ? 1.3054 1.5881 1.2497 0.0280  0.1583  -0.0041 39  ASP D O   
4669 C CB  . ASP D 39  ? 1.3913 1.8352 1.5225 0.0465  0.2068  0.0344  39  ASP D CB  
4670 C CG  . ASP D 39  ? 1.4025 1.8235 1.4836 0.0096  0.2255  0.0238  39  ASP D CG  
4671 O OD1 . ASP D 39  ? 1.3841 1.8208 1.4669 -0.0266 0.1932  0.0306  39  ASP D OD1 
4672 O OD2 . ASP D 39  ? 1.3783 1.7581 1.4109 0.0135  0.2716  0.0095  39  ASP D OD2 
4673 N N   . GLN D 40  ? 1.1250 1.4593 1.1095 -0.0216 0.1220  0.0099  40  GLN D N   
4674 C CA  . GLN D 40  ? 1.0619 1.3344 0.9699 -0.0379 0.1124  -0.0030 40  GLN D CA  
4675 C C   . GLN D 40  ? 0.9452 1.1928 0.8302 -0.0378 0.0719  -0.0084 40  GLN D C   
4676 O O   . GLN D 40  ? 0.8849 1.0941 0.7242 -0.0505 0.0602  -0.0139 40  GLN D O   
4677 C CB  . GLN D 40  ? 1.0004 1.2728 0.8997 -0.0716 0.1147  0.0026  40  GLN D CB  
4678 C CG  . GLN D 40  ? 1.0340 1.3192 0.9333 -0.0797 0.1584  0.0047  40  GLN D CG  
4679 C CD  . GLN D 40  ? 0.9257 1.2364 0.8438 -0.1151 0.1554  0.0168  40  GLN D CD  
4680 O OE1 . GLN D 40  ? 0.8748 1.1662 0.7800 -0.1360 0.1217  0.0213  40  GLN D OE1 
4681 N NE2 . GLN D 40  ? 0.9603 1.3114 0.9073 -0.1222 0.1929  0.0222  40  GLN D NE2 
4682 N N   . GLN D 41  ? 0.9470 1.2171 0.8638 -0.0239 0.0518  -0.0047 41  GLN D N   
4683 C CA  . GLN D 41  ? 0.9332 1.1810 0.8248 -0.0291 0.0156  -0.0111 41  GLN D CA  
4684 C C   . GLN D 41  ? 0.8660 1.0942 0.7323 -0.0058 0.0124  -0.0174 41  GLN D C   
4685 O O   . GLN D 41  ? 0.8769 1.1229 0.7716 0.0162  0.0258  -0.0101 41  GLN D O   
4686 C CB  . GLN D 41  ? 0.9397 1.2254 0.8756 -0.0477 -0.0146 0.0013  41  GLN D CB  
4687 C CG  . GLN D 41  ? 0.9924 1.2792 0.9320 -0.0801 -0.0213 0.0056  41  GLN D CG  
4688 C CD  . GLN D 41  ? 1.0261 1.3465 0.9978 -0.1084 -0.0542 0.0202  41  GLN D CD  
4689 O OE1 . GLN D 41  ? 0.9434 1.2653 0.9111 -0.1098 -0.0803 0.0215  41  GLN D OE1 
4690 N NE2 . GLN D 41  ? 1.0390 1.3872 1.0375 -0.1378 -0.0556 0.0340  41  GLN D NE2 
4691 N N   . ARG D 42  ? 0.8415 1.0317 0.6544 -0.0101 -0.0038 -0.0295 42  ARG D N   
4692 C CA  . ARG D 42  ? 0.8509 1.0207 0.6295 0.0034  -0.0127 -0.0353 42  ARG D CA  
4693 C C   . ARG D 42  ? 0.8733 1.0289 0.6252 -0.0103 -0.0418 -0.0439 42  ARG D C   
4694 O O   . ARG D 42  ? 0.8988 1.0310 0.6201 -0.0183 -0.0400 -0.0529 42  ARG D O   
4695 C CB  . ARG D 42  ? 0.8003 0.9356 0.5244 0.0092  0.0092  -0.0416 42  ARG D CB  
4696 C CG  . ARG D 42  ? 0.8669 0.9777 0.5471 0.0178  0.0011  -0.0456 42  ARG D CG  
4697 C CD  . ARG D 42  ? 0.8724 0.9512 0.4905 0.0113  0.0182  -0.0481 42  ARG D CD  
4698 N NE  . ARG D 42  ? 0.8961 0.9640 0.5121 0.0110  0.0504  -0.0454 42  ARG D NE  
4699 C CZ  . ARG D 42  ? 0.8466 0.8874 0.4454 0.0230  0.0729  -0.0466 42  ARG D CZ  
4700 N NH1 . ARG D 42  ? 0.8274 0.8472 0.4102 0.0372  0.0632  -0.0474 42  ARG D NH1 
4701 N NH2 . ARG D 42  ? 0.8004 0.8287 0.3937 0.0203  0.1079  -0.0471 42  ARG D NH2 
4702 N N   . LEU D 43  ? 0.9127 1.0809 0.6757 -0.0131 -0.0669 -0.0396 43  LEU D N   
4703 C CA  . LEU D 43  ? 0.9094 1.0597 0.6385 -0.0324 -0.0925 -0.0496 43  LEU D CA  
4704 C C   . LEU D 43  ? 0.9297 1.0593 0.6100 -0.0257 -0.0986 -0.0575 43  LEU D C   
4705 O O   . LEU D 43  ? 0.9960 1.1326 0.6829 -0.0131 -0.1020 -0.0478 43  LEU D O   
4706 C CB  . LEU D 43  ? 0.9572 1.1360 0.7213 -0.0535 -0.1220 -0.0361 43  LEU D CB  
4707 C CG  . LEU D 43  ? 0.9354 1.1328 0.7358 -0.0721 -0.1214 -0.0282 43  LEU D CG  
4708 C CD1 . LEU D 43  ? 0.9734 1.2087 0.8085 -0.1001 -0.1553 -0.0076 43  LEU D CD1 
4709 C CD2 . LEU D 43  ? 0.9423 1.0884 0.6926 -0.0860 -0.1141 -0.0484 43  LEU D CD2 
4710 N N   . ILE D 44  ? 1.0177 1.1206 0.6491 -0.0331 -0.0976 -0.0738 44  ILE D N   
4711 C CA  . ILE D 44  ? 1.0594 1.1495 0.6415 -0.0314 -0.1010 -0.0809 44  ILE D CA  
4712 C C   . ILE D 44  ? 1.1175 1.1902 0.6617 -0.0515 -0.1158 -0.0956 44  ILE D C   
4713 O O   . ILE D 44  ? 1.1171 1.1697 0.6515 -0.0574 -0.1066 -0.1079 44  ILE D O   
4714 C CB  . ILE D 44  ? 1.0216 1.1059 0.5798 -0.0191 -0.0769 -0.0828 44  ILE D CB  
4715 C CG1 . ILE D 44  ? 0.9631 1.0506 0.5310 -0.0080 -0.0643 -0.0705 44  ILE D CG1 
4716 C CG2 . ILE D 44  ? 1.0113 1.0906 0.5186 -0.0240 -0.0797 -0.0907 44  ILE D CG2 
4717 C CD1 . ILE D 44  ? 0.9155 0.9966 0.4458 -0.0076 -0.0486 -0.0671 44  ILE D CD1 
4718 N N   . PHE D 45  ? 1.1193 1.1182 0.7113 0.0525  -0.2500 -0.1280 45  PHE D N   
4719 C CA  . PHE D 45  ? 1.2015 1.1946 0.7206 0.0510  -0.2515 -0.1249 45  PHE D CA  
4720 C C   . PHE D 45  ? 1.2648 1.2211 0.7231 0.0576  -0.2499 -0.0743 45  PHE D C   
4721 O O   . PHE D 45  ? 1.2430 1.1801 0.7051 0.0718  -0.2747 -0.0485 45  PHE D O   
4722 C CB  . PHE D 45  ? 1.2206 1.2468 0.7237 0.0611  -0.2943 -0.1500 45  PHE D CB  
4723 C CG  . PHE D 45  ? 1.2958 1.3198 0.7139 0.0570  -0.2948 -0.1578 45  PHE D CG  
4724 C CD1 . PHE D 45  ? 1.3231 1.3415 0.7306 0.0395  -0.2642 -0.1931 45  PHE D CD1 
4725 C CD2 . PHE D 45  ? 1.3756 1.4018 0.7223 0.0726  -0.3232 -0.1292 45  PHE D CD2 
4726 C CE1 . PHE D 45  ? 1.3823 1.3926 0.7012 0.0389  -0.2601 -0.2083 45  PHE D CE1 
4727 C CE2 . PHE D 45  ? 1.4672 1.4977 0.7240 0.0701  -0.3212 -0.1388 45  PHE D CE2 
4728 C CZ  . PHE D 45  ? 1.4471 1.4671 0.6859 0.0539  -0.2885 -0.1827 45  PHE D CZ  
4729 N N   . ALA D 46  ? 1.2961 1.2423 0.7036 0.0487  -0.2185 -0.0577 46  ALA D N   
4730 C CA  . ALA D 46  ? 1.3361 1.2580 0.6906 0.0509  -0.2112 -0.0016 46  ALA D CA  
4731 C C   . ALA D 46  ? 1.3222 1.2132 0.7175 0.0409  -0.2091 0.0327  46  ALA D C   
4732 O O   . ALA D 46  ? 1.3212 1.1833 0.6932 0.0450  -0.2262 0.0767  46  ALA D O   
4733 C CB  . ALA D 46  ? 1.3809 1.3079 0.6738 0.0704  -0.2488 0.0177  46  ALA D CB  
4734 N N   . GLY D 47  ? 1.2719 1.1683 0.7274 0.0256  -0.1892 0.0128  47  GLY D N   
4735 C CA  . GLY D 47  ? 1.1723 1.0414 0.6593 0.0109  -0.1877 0.0353  47  GLY D CA  
4736 C C   . GLY D 47  ? 1.1842 1.0228 0.6905 0.0265  -0.2235 0.0255  47  GLY D C   
4737 O O   . GLY D 47  ? 1.1642 0.9620 0.6792 0.0149  -0.2272 0.0440  47  GLY D O   
4738 N N   . LYS D 48  ? 1.2309 1.0874 0.7457 0.0523  -0.2500 -0.0029 48  LYS D N   
4739 C CA  . LYS D 48  ? 1.2574 1.0906 0.7983 0.0766  -0.2804 -0.0102 48  LYS D CA  
4740 C C   . LYS D 48  ? 1.1596 1.0387 0.7606 0.0879  -0.2812 -0.0585 48  LYS D C   
4741 O O   . LYS D 48  ? 1.1159 1.0461 0.7282 0.0845  -0.2785 -0.0828 48  LYS D O   
4742 C CB  . LYS D 48  ? 1.2891 1.1156 0.7948 0.1026  -0.3154 0.0163  48  LYS D CB  
4743 C CG  . LYS D 48  ? 1.3768 1.1592 0.8302 0.0947  -0.3174 0.0747  48  LYS D CG  
4744 C CD  . LYS D 48  ? 1.4381 1.1465 0.9109 0.0975  -0.3293 0.0985  48  LYS D CD  
4745 C CE  . LYS D 48  ? 1.4184 1.0841 0.8541 0.0731  -0.3229 0.1579  48  LYS D CE  
4746 N NZ  . LYS D 48  ? 1.5027 1.2004 0.8842 0.0804  -0.3289 0.2013  48  LYS D NZ  
4747 N N   . GLN D 49  ? 1.1716 1.0319 0.8112 0.1006  -0.2839 -0.0729 49  GLN D N   
4748 C CA  . GLN D 49  ? 1.1565 1.0702 0.8577 0.1156  -0.2826 -0.1117 49  GLN D CA  
4749 C C   . GLN D 49  ? 1.1979 1.1412 0.9167 0.1499  -0.3173 -0.1134 49  GLN D C   
4750 O O   . GLN D 49  ? 1.2721 1.1758 0.9761 0.1760  -0.3406 -0.0898 49  GLN D O   
4751 C CB  . GLN D 49  ? 1.1576 1.0474 0.8868 0.1212  -0.2686 -0.1289 49  GLN D CB  
4752 C CG  . GLN D 49  ? 1.1112 0.9929 0.8287 0.0821  -0.2378 -0.1266 49  GLN D CG  
4753 C CD  . GLN D 49  ? 1.1100 0.9989 0.8563 0.0832  -0.2210 -0.1550 49  GLN D CD  
4754 O OE1 . GLN D 49  ? 1.1418 1.0650 0.9301 0.1133  -0.2223 -0.1819 49  GLN D OE1 
4755 N NE2 . GLN D 49  ? 1.0449 0.9094 0.7676 0.0501  -0.2050 -0.1470 49  GLN D NE2 
4756 N N   . LEU D 50  ? 1.1721 1.1872 0.9274 0.1477  -0.3225 -0.1371 50  LEU D N   
4757 C CA  . LEU D 50  ? 1.1924 1.2536 0.9651 0.1713  -0.3601 -0.1356 50  LEU D CA  
4758 C C   . LEU D 50  ? 1.3005 1.3905 1.1447 0.2079  -0.3671 -0.1442 50  LEU D C   
4759 O O   . LEU D 50  ? 1.2531 1.3823 1.1528 0.2049  -0.3450 -0.1694 50  LEU D O   
4760 C CB  . LEU D 50  ? 1.1497 1.2718 0.9299 0.1459  -0.3659 -0.1591 50  LEU D CB  
4761 C CG  . LEU D 50  ? 1.0917 1.1846 0.8003 0.1158  -0.3512 -0.1569 50  LEU D CG  
4762 C CD1 . LEU D 50  ? 1.0639 1.2031 0.7797 0.0923  -0.3575 -0.1895 50  LEU D CD1 
4763 C CD2 . LEU D 50  ? 1.1459 1.2012 0.7782 0.1274  -0.3709 -0.1208 50  LEU D CD2 
4764 N N   . GLU D 51  ? 1.4200 1.4942 1.2653 0.2454  -0.3947 -0.1190 51  GLU D N   
4765 C CA  . GLU D 51  ? 1.4270 1.5276 1.3423 0.2901  -0.3987 -0.1226 51  GLU D CA  
4766 C C   . GLU D 51  ? 1.3810 1.5933 1.3640 0.2940  -0.4182 -0.1329 51  GLU D C   
4767 O O   . GLU D 51  ? 1.3518 1.6080 1.3171 0.2744  -0.4485 -0.1261 51  GLU D O   
4768 C CB  . GLU D 51  ? 1.4823 1.5308 1.3860 0.3319  -0.4222 -0.0851 51  GLU D CB  
4769 C CG  . GLU D 51  ? 1.5968 1.5347 1.4320 0.3203  -0.4137 -0.0639 51  GLU D CG  
4770 C CD  . GLU D 51  ? 1.7649 1.6245 1.6088 0.3327  -0.3845 -0.0842 51  GLU D CD  
4771 O OE1 . GLU D 51  ? 1.7396 1.6021 1.5802 0.3040  -0.3543 -0.1176 51  GLU D OE1 
4772 O OE2 . GLU D 51  ? 1.8708 1.6647 1.7238 0.3711  -0.3923 -0.0667 51  GLU D OE2 
4773 N N   . ASP D 52  ? 1.3137 1.5749 1.3737 0.3188  -0.4015 -0.1488 52  ASP D N   
4774 C CA  . ASP D 52  ? 1.2241 1.6011 1.3638 0.3180  -0.4173 -0.1545 52  ASP D CA  
4775 C C   . ASP D 52  ? 1.2264 1.6591 1.3930 0.3453  -0.4656 -0.1222 52  ASP D C   
4776 O O   . ASP D 52  ? 1.1312 1.6637 1.3533 0.3318  -0.4916 -0.1222 52  ASP D O   
4777 C CB  . ASP D 52  ? 1.1457 1.5686 1.3627 0.3443  -0.3834 -0.1708 52  ASP D CB  
4778 C CG  . ASP D 52  ? 1.1584 1.5402 1.3488 0.3167  -0.3380 -0.1982 52  ASP D CG  
4779 O OD1 . ASP D 52  ? 1.2329 1.5159 1.3515 0.3113  -0.3243 -0.2004 52  ASP D OD1 
4780 O OD2 . ASP D 52  ? 1.0730 1.5264 1.3176 0.2977  -0.3179 -0.2124 52  ASP D OD2 
4781 N N   . GLY D 53  ? 1.2776 1.6518 1.4106 0.3807  -0.4805 -0.0906 53  GLY D N   
4782 C CA  . GLY D 53  ? 1.1778 1.6101 1.3413 0.4122  -0.5261 -0.0497 53  GLY D CA  
4783 C C   . GLY D 53  ? 1.2369 1.6780 1.3286 0.3794  -0.5683 -0.0306 53  GLY D C   
4784 O O   . GLY D 53  ? 1.1848 1.7221 1.3038 0.3712  -0.6110 -0.0177 53  GLY D O   
4785 N N   . ARG D 54  ? 1.3236 1.6710 1.3218 0.3596  -0.5575 -0.0273 54  ARG D N   
4786 C CA  . ARG D 54  ? 1.3967 1.7522 1.3139 0.3303  -0.5902 -0.0112 54  ARG D CA  
4787 C C   . ARG D 54  ? 1.3814 1.7985 1.2884 0.2789  -0.5989 -0.0533 54  ARG D C   
4788 O O   . ARG D 54  ? 1.3594 1.7795 1.3021 0.2569  -0.5680 -0.0927 54  ARG D O   
4789 C CB  . ARG D 54  ? 1.3773 1.6259 1.2042 0.3179  -0.5674 0.0013  54  ARG D CB  
4790 N N   . THR D 55  ? 1.4014 1.8675 1.2609 0.2581  -0.6405 -0.0440 55  THR D N   
4791 C CA  . THR D 55  ? 1.4112 1.9166 1.2604 0.2006  -0.6406 -0.0841 55  THR D CA  
4792 C C   . THR D 55  ? 1.4386 1.8720 1.1817 0.1659  -0.6150 -0.1072 55  THR D C   
4793 O O   . THR D 55  ? 1.4744 1.8369 1.1612 0.1837  -0.5962 -0.0901 55  THR D O   
4794 C CB  . THR D 55  ? 1.4453 2.0378 1.3105 0.1823  -0.6848 -0.0621 55  THR D CB  
4795 O OG1 . THR D 55  ? 1.4772 2.0518 1.2430 0.1696  -0.7017 -0.0372 55  THR D OG1 
4796 C CG2 . THR D 55  ? 1.3366 1.9960 1.3006 0.2304  -0.7076 -0.0178 55  THR D CG2 
4797 N N   . LEU D 56  ? 1.4608 1.9089 1.1787 0.1164  -0.6130 -0.1445 56  LEU D N   
4798 C CA  . LEU D 56  ? 1.5228 1.9045 1.1501 0.0881  -0.5809 -0.1708 56  LEU D CA  
4799 C C   . LEU D 56  ? 1.5400 1.9008 1.0651 0.0926  -0.5891 -0.1375 56  LEU D C   
4800 O O   . LEU D 56  ? 1.4782 1.7777 0.9382 0.0966  -0.5572 -0.1315 56  LEU D O   
4801 C CB  . LEU D 56  ? 1.4879 1.8809 1.1169 0.0386  -0.5778 -0.2204 56  LEU D CB  
4802 C CG  . LEU D 56  ? 1.4609 1.8552 1.1757 0.0243  -0.5535 -0.2555 56  LEU D CG  
4803 C CD1 . LEU D 56  ? 1.4308 1.8313 1.1447 -0.0257 -0.5603 -0.2968 56  LEU D CD1 
4804 C CD2 . LEU D 56  ? 1.3501 1.6774 1.0493 0.0347  -0.5044 -0.2647 56  LEU D CD2 
4805 N N   . SER D 57  ? 1.9678 1.7430 0.7969 -0.0102 -0.2938 0.1086  57  SER D N   
4806 C CA  . SER D 57  ? 2.0058 1.7731 0.7900 -0.0132 -0.2852 0.1123  57  SER D CA  
4807 C C   . SER D 57  ? 2.0145 1.7347 0.7741 -0.0040 -0.2642 0.1371  57  SER D C   
4808 O O   . SER D 57  ? 2.0099 1.7155 0.7354 -0.0109 -0.2517 0.1387  57  SER D O   
4809 C CB  . SER D 57  ? 2.0156 1.8305 0.7838 -0.0034 -0.3099 0.1209  57  SER D CB  
4810 O OG  . SER D 57  ? 2.0201 1.8544 0.8025 0.0195  -0.3247 0.1489  57  SER D OG  
4811 N N   . ASP D 58  ? 2.0068 1.7030 0.7836 0.0113  -0.2604 0.1559  58  ASP D N   
4812 C CA  . ASP D 58  ? 2.0534 1.6976 0.8087 0.0180  -0.2401 0.1764  58  ASP D CA  
4813 C C   . ASP D 58  ? 2.0251 1.6312 0.7799 -0.0038 -0.2134 0.1608  58  ASP D C   
4814 O O   . ASP D 58  ? 2.0002 1.5672 0.7300 -0.0064 -0.1961 0.1734  58  ASP D O   
4815 C CB  . ASP D 58  ? 2.0813 1.7105 0.8575 0.0421  -0.2432 0.1982  58  ASP D CB  
4816 C CG  . ASP D 58  ? 2.0946 1.7744 0.8847 0.0635  -0.2699 0.2130  58  ASP D CG  
4817 O OD1 . ASP D 58  ? 2.0690 1.7981 0.8810 0.0561  -0.2880 0.1969  58  ASP D OD1 
4818 O OD2 . ASP D 58  ? 2.1221 1.7935 0.9026 0.0867  -0.2730 0.2404  58  ASP D OD2 
4819 N N   . TYR D 59  ? 2.0097 1.6285 0.7935 -0.0201 -0.2100 0.1346  59  TYR D N   
4820 C CA  . TYR D 59  ? 1.9497 1.5446 0.7389 -0.0413 -0.1846 0.1188  59  TYR D CA  
4821 C C   . TYR D 59  ? 1.9187 1.5397 0.6994 -0.0596 -0.1811 0.0946  59  TYR D C   
4822 O O   . TYR D 59  ? 1.8682 1.4825 0.6621 -0.0762 -0.1615 0.0783  59  TYR D O   
4823 C CB  . TYR D 59  ? 1.8443 1.4323 0.6754 -0.0453 -0.1787 0.1075  59  TYR D CB  
4824 C CG  . TYR D 59  ? 1.8350 1.3960 0.6796 -0.0272 -0.1783 0.1280  59  TYR D CG  
4825 C CD1 . TYR D 59  ? 1.8418 1.3558 0.6728 -0.0264 -0.1585 0.1429  59  TYR D CD1 
4826 C CD2 . TYR D 59  ? 1.8077 1.3922 0.6821 -0.0113 -0.1977 0.1309  59  TYR D CD2 
4827 C CE1 . TYR D 59  ? 1.8071 1.2948 0.6509 -0.0083 -0.1575 0.1590  59  TYR D CE1 
4828 C CE2 . TYR D 59  ? 1.7994 1.3635 0.6895 0.0085  -0.1965 0.1491  59  TYR D CE2 
4829 C CZ  . TYR D 59  ? 1.8146 1.3285 0.6884 0.0107  -0.1758 0.1622  59  TYR D CZ  
4830 O OH  . TYR D 59  ? 1.8498 1.3418 0.7392 0.0318  -0.1740 0.1780  59  TYR D OH  
4831 N N   . ASN D 60  ? 1.9159 1.5700 0.6775 -0.0556 -0.1993 0.0914  60  ASN D N   
4832 C CA  . ASN D 60  ? 1.8699 1.5473 0.6169 -0.0691 -0.1959 0.0701  60  ASN D CA  
4833 C C   . ASN D 60  ? 1.8280 1.5242 0.6077 -0.0818 -0.1959 0.0377  60  ASN D C   
4834 O O   . ASN D 60  ? 1.8157 1.5163 0.5949 -0.0940 -0.1802 0.0190  60  ASN D O   
4835 C CB  . ASN D 60  ? 1.8341 1.4897 0.5576 -0.0783 -0.1711 0.0766  60  ASN D CB  
4836 C CG  . ASN D 60  ? 1.8489 1.5321 0.5489 -0.0851 -0.1701 0.0623  60  ASN D CG  
4837 O OD1 . ASN D 60  ? 1.8888 1.6029 0.5791 -0.0803 -0.1896 0.0529  60  ASN D OD1 
4838 N ND2 . ASN D 60  ? 1.8536 1.5285 0.5447 -0.0959 -0.1475 0.0607  60  ASN D ND2 
4839 N N   . ILE D 61  ? 1.8160 1.5255 0.6250 -0.0779 -0.2142 0.0318  61  ILE D N   
4840 C CA  . ILE D 61  ? 1.7704 1.4940 0.6137 -0.0898 -0.2163 0.0026  61  ILE D CA  
4841 C C   . ILE D 61  ? 1.7663 1.5259 0.6027 -0.0923 -0.2393 -0.0157 61  ILE D C   
4842 O O   . ILE D 61  ? 1.7504 1.5329 0.5967 -0.0860 -0.2653 -0.0109 61  ILE D O   
4843 C CB  . ILE D 61  ? 1.7512 1.4690 0.6334 -0.0862 -0.2230 0.0070  61  ILE D CB  
4844 C CG1 . ILE D 61  ? 1.7059 1.3866 0.5955 -0.0855 -0.1979 0.0208  61  ILE D CG1 
4845 C CG2 . ILE D 61  ? 1.6719 1.4078 0.5902 -0.0987 -0.2299 -0.0225 61  ILE D CG2 
4846 C CD1 . ILE D 61  ? 1.6855 1.3537 0.5878 -0.0689 -0.2069 0.0450  61  ILE D CD1 
4847 N N   . GLN D 62  ? 1.8027 1.5700 0.6235 -0.1008 -0.2300 -0.0366 62  GLN D N   
4848 C CA  . GLN D 62  ? 1.8438 1.6409 0.6539 -0.1036 -0.2497 -0.0566 62  GLN D CA  
4849 C C   . GLN D 62  ? 1.8631 1.6667 0.7092 -0.1147 -0.2552 -0.0870 62  GLN D C   
4850 O O   . GLN D 62  ? 1.7340 1.5234 0.6146 -0.1187 -0.2467 -0.0893 62  GLN D O   
4851 C CB  . GLN D 62  ? 1.7297 1.5319 0.5016 -0.1037 -0.2378 -0.0625 62  GLN D CB  
4852 N N   . LYS D 63  ? 1.8405 1.6644 0.6787 -0.1197 -0.2697 -0.1106 63  LYS D N   
4853 C CA  . LYS D 63  ? 1.8124 1.6398 0.6829 -0.1304 -0.2773 -0.1395 63  LYS D CA  
4854 C C   . LYS D 63  ? 1.8243 1.6316 0.7100 -0.1342 -0.2487 -0.1567 63  LYS D C   
4855 O O   . LYS D 63  ? 1.8876 1.6880 0.7510 -0.1301 -0.2261 -0.1547 63  LYS D O   
4856 C CB  . LYS D 63  ? 1.8246 1.6733 0.6774 -0.1345 -0.2975 -0.1614 63  LYS D CB  
4857 N N   . GLU D 64  ? 1.7470 1.5485 0.6733 -0.1417 -0.2501 -0.1720 64  GLU D N   
4858 C CA  . GLU D 64  ? 1.7673 1.5544 0.7154 -0.1444 -0.2262 -0.1912 64  GLU D CA  
4859 C C   . GLU D 64  ? 1.7742 1.5453 0.7352 -0.1415 -0.1993 -0.1734 64  GLU D C   
4860 O O   . GLU D 64  ? 1.7615 1.5254 0.7409 -0.1422 -0.1773 -0.1863 64  GLU D O   
4861 C CB  . GLU D 64  ? 1.8703 1.6605 0.7915 -0.1408 -0.2139 -0.2129 64  GLU D CB  
4862 C CG  . GLU D 64  ? 1.8793 1.6824 0.7819 -0.1435 -0.2375 -0.2343 64  GLU D CG  
4863 C CD  . GLU D 64  ? 1.8336 1.6306 0.7684 -0.1520 -0.2479 -0.2604 64  GLU D CD  
4864 O OE1 . GLU D 64  ? 1.8630 1.6461 0.8284 -0.1523 -0.2304 -0.2682 64  GLU D OE1 
4865 O OE2 . GLU D 64  ? 1.7542 1.5609 0.6842 -0.1589 -0.2738 -0.2723 64  GLU D OE2 
4866 N N   . SER D 65  ? 1.7389 1.5042 0.6910 -0.1375 -0.1999 -0.1442 65  SER D N   
4867 C CA  . SER D 65  ? 1.6629 1.4103 0.6234 -0.1361 -0.1739 -0.1273 65  SER D CA  
4868 C C   . SER D 65  ? 1.6231 1.3621 0.6274 -0.1396 -0.1740 -0.1254 65  SER D C   
4869 O O   . SER D 65  ? 1.6113 1.3591 0.6361 -0.1415 -0.1980 -0.1280 65  SER D O   
4870 C CB  . SER D 65  ? 1.6562 1.3949 0.5844 -0.1293 -0.1727 -0.0968 65  SER D CB  
4871 O OG  . SER D 65  ? 1.6905 1.4370 0.6108 -0.1235 -0.2006 -0.0832 65  SER D OG  
4872 N N   . THR D 66  ? 1.5743 1.3001 0.5948 -0.1410 -0.1471 -0.1201 66  THR D N   
4873 C CA  . THR D 66  ? 1.5309 1.2501 0.5936 -0.1444 -0.1424 -0.1199 66  THR D CA  
4874 C C   . THR D 66  ? 1.4435 1.1440 0.5029 -0.1406 -0.1326 -0.0917 66  THR D C   
4875 O O   . THR D 66  ? 1.4425 1.1319 0.4815 -0.1401 -0.1125 -0.0790 66  THR D O   
4876 C CB  . THR D 66  ? 1.4381 1.1604 0.5290 -0.1488 -0.1184 -0.1400 66  THR D CB  
4877 O OG1 . THR D 66  ? 1.5336 1.2676 0.6256 -0.1497 -0.1284 -0.1667 66  THR D OG1 
4878 C CG2 . THR D 66  ? 1.3606 1.0789 0.4964 -0.1524 -0.1137 -0.1398 66  THR D CG2 
4879 N N   . LEU D 67  ? 1.3537 1.0512 0.4335 -0.1373 -0.1483 -0.0814 67  LEU D N   
4880 C CA  . LEU D 67  ? 1.4332 1.1100 0.5160 -0.1315 -0.1393 -0.0573 67  LEU D CA  
4881 C C   . LEU D 67  ? 1.3966 1.0717 0.5217 -0.1384 -0.1215 -0.0662 67  LEU D C   
4882 O O   . LEU D 67  ? 1.3872 1.0788 0.5445 -0.1450 -0.1262 -0.0877 67  LEU D O   
4883 C CB  . LEU D 67  ? 1.4320 1.1109 0.5121 -0.1185 -0.1681 -0.0379 67  LEU D CB  
4884 C CG  . LEU D 67  ? 1.4395 1.1338 0.4912 -0.1102 -0.1945 -0.0305 67  LEU D CG  
4885 C CD1 . LEU D 67  ? 1.4219 1.1300 0.4891 -0.0957 -0.2222 -0.0117 67  LEU D CD1 
4886 C CD2 . LEU D 67  ? 1.5197 1.1968 0.5258 -0.1044 -0.1830 -0.0144 67  LEU D CD2 
4887 N N   . HIS D 68  ? 1.3498 1.0049 0.4762 -0.1371 -0.1009 -0.0496 68  HIS D N   
4888 C CA  . HIS D 68  ? 1.3155 0.9711 0.4813 -0.1436 -0.0811 -0.0555 68  HIS D CA  
4889 C C   . HIS D 68  ? 1.3308 0.9783 0.5128 -0.1351 -0.0946 -0.0413 68  HIS D C   
4890 O O   . HIS D 68  ? 1.3587 0.9865 0.5166 -0.1223 -0.1024 -0.0176 68  HIS D O   
4891 C CB  . HIS D 68  ? 1.2645 0.9091 0.4264 -0.1497 -0.0488 -0.0474 68  HIS D CB  
4892 C CG  . HIS D 68  ? 1.4101 1.0588 0.6135 -0.1560 -0.0269 -0.0504 68  HIS D CG  
4893 N ND1 . HIS D 68  ? 1.3293 0.9692 0.5378 -0.1619 -0.0018 -0.0386 68  HIS D ND1 
4894 C CD2 . HIS D 68  ? 1.3282 0.9917 0.5729 -0.1582 -0.0272 -0.0636 68  HIS D CD2 
4895 C CE1 . HIS D 68  ? 1.2800 0.9310 0.5309 -0.1665 0.0132  -0.0440 68  HIS D CE1 
4896 N NE2 . HIS D 68  ? 1.3410 1.0058 0.6135 -0.1638 -0.0008 -0.0591 68  HIS D NE2 
4897 N N   . LEU D 69  ? 1.2891 0.9620 0.5344 -0.1363 -0.0954 -0.0537 69  LEU D N   
4898 C CA  . LEU D 69  ? 1.2149 0.9045 0.5183 -0.1218 -0.1050 -0.0398 69  LEU D CA  
4899 C C   . LEU D 69  ? 1.1648 0.8494 0.5023 -0.1241 -0.0770 -0.0364 69  LEU D C   
4900 O O   . LEU D 69  ? 1.1444 0.8428 0.5123 -0.1360 -0.0599 -0.0542 69  LEU D O   
4901 C CB  . LEU D 69  ? 1.1646 0.8936 0.5244 -0.1217 -0.1279 -0.0532 69  LEU D CB  
4902 C CG  . LEU D 69  ? 1.1167 0.8738 0.5393 -0.1065 -0.1415 -0.0378 69  LEU D CG  
4903 C CD1 . LEU D 69  ? 1.1616 0.9164 0.5579 -0.0865 -0.1624 -0.0124 69  LEU D CD1 
4904 C CD2 . LEU D 69  ? 1.0827 0.8787 0.5632 -0.1137 -0.1596 -0.0534 69  LEU D CD2 
4905 N N   . VAL D 70  ? 1.1566 0.8215 0.4881 -0.1115 -0.0730 -0.0135 70  VAL D N   
4906 C CA  . VAL D 70  ? 1.0908 0.7497 0.4529 -0.1122 -0.0494 -0.0076 70  VAL D CA  
4907 C C   . VAL D 70  ? 1.0643 0.7470 0.4852 -0.0920 -0.0639 0.0041  70  VAL D C   
4908 O O   . VAL D 70  ? 1.0986 0.7778 0.5059 -0.0727 -0.0848 0.0210  70  VAL D O   
4909 C CB  . VAL D 70  ? 1.1212 0.7311 0.4215 -0.1157 -0.0315 0.0090  70  VAL D CB  
4910 C CG1 . VAL D 70  ? 1.0393 0.6426 0.3704 -0.1172 -0.0093 0.0151  70  VAL D CG1 
4911 C CG2 . VAL D 70  ? 1.1327 0.7260 0.3755 -0.1369 -0.0167 -0.0004 70  VAL D CG2 
4912 N N   . LEU D 71  ? 1.0117 0.7218 0.4975 -0.0949 -0.0524 -0.0037 71  LEU D N   
4913 C CA  . LEU D 71  ? 0.9347 0.6774 0.4841 -0.0773 -0.0657 0.0056  71  LEU D CA  
4914 C C   . LEU D 71  ? 0.9355 0.6669 0.5044 -0.0709 -0.0448 0.0165  71  LEU D C   
4915 O O   . LEU D 71  ? 0.8962 0.6061 0.4476 -0.0861 -0.0182 0.0116  71  LEU D O   
4916 C CB  . LEU D 71  ? 0.8946 0.6841 0.5097 -0.0857 -0.0740 -0.0121 71  LEU D CB  
4917 C CG  . LEU D 71  ? 0.9498 0.7490 0.5471 -0.0952 -0.0950 -0.0267 71  LEU D CG  
4918 C CD1 . LEU D 71  ? 0.8438 0.6807 0.5040 -0.1050 -0.1021 -0.0440 71  LEU D CD1 
4919 C CD2 . LEU D 71  ? 0.9870 0.7897 0.5582 -0.0801 -0.1249 -0.0111 71  LEU D CD2 
4920 N N   . ARG D 72  ? 0.9166 0.6653 0.5205 -0.0481 -0.0574 0.0321  72  ARG D N   
4921 C CA  . ARG D 72  ? 0.8642 0.6120 0.4997 -0.0404 -0.0401 0.0399  72  ARG D CA  
4922 C C   . ARG D 72  ? 0.7592 0.5377 0.4506 -0.0592 -0.0210 0.0224  72  ARG D C   
4923 O O   . ARG D 72  ? 0.7004 0.5197 0.4400 -0.0651 -0.0311 0.0102  72  ARG D O   
4924 C CB  . ARG D 72  ? 0.8886 0.6661 0.5648 -0.0110 -0.0598 0.0568  72  ARG D CB  
4925 C CG  . ARG D 72  ? 0.9512 0.6866 0.5846 0.0128  -0.0575 0.0778  72  ARG D CG  
4926 C CD  . ARG D 72  ? 1.0896 0.8441 0.7225 0.0432  -0.0859 0.0957  72  ARG D CD  
4927 N NE  . ARG D 72  ? 1.1804 0.8817 0.7532 0.0675  -0.0844 0.1154  72  ARG D NE  
4928 C CZ  . ARG D 72  ? 1.2917 0.9347 0.7847 0.0640  -0.0822 0.1205  72  ARG D CZ  
4929 N NH1 . ARG D 72  ? 1.2922 0.9255 0.7550 0.0374  -0.0806 0.1074  72  ARG D NH1 
4930 N NH2 . ARG D 72  ? 1.3633 0.9549 0.8034 0.0886  -0.0814 0.1396  72  ARG D NH2 
4931 N N   . LEU D 73  ? 0.7568 0.5143 0.4390 -0.0696 0.0066  0.0217  73  LEU D N   
4932 C CA  . LEU D 73  ? 0.6721 0.4607 0.4064 -0.0854 0.0271  0.0074  73  LEU D CA  
4933 C C   . LEU D 73  ? 0.6155 0.4396 0.4194 -0.0700 0.0261  0.0150  73  LEU D C   
4934 O O   . LEU D 73  ? 0.5960 0.4143 0.4100 -0.0709 0.0459  0.0195  73  LEU D O   
4935 C CB  . LEU D 73  ? 0.6501 0.4088 0.3440 -0.1059 0.0571  0.0039  73  LEU D CB  
4936 C CG  . LEU D 73  ? 0.6969 0.4240 0.3204 -0.1226 0.0617  -0.0020 73  LEU D CG  
4937 C CD1 . LEU D 73  ? 0.7064 0.4223 0.3086 -0.1449 0.0930  -0.0052 73  LEU D CD1 
4938 C CD2 . LEU D 73  ? 0.6384 0.3908 0.2731 -0.1278 0.0495  -0.0194 73  LEU D CD2 
4939 N N   . ARG D 74  ? 0.5988 0.4621 0.4495 -0.0564 0.0016  0.0174  74  ARG D N   
4940 C CA  . ARG D 74  ? 0.5434 0.4490 0.4641 -0.0411 -0.0018 0.0259  74  ARG D CA  
4941 C C   . ARG D 74  ? 0.4700 0.4070 0.4476 -0.0562 0.0193  0.0136  74  ARG D C   
4942 O O   . ARG D 74  ? 0.4430 0.4022 0.4645 -0.0476 0.0288  0.0205  74  ARG D O   
4943 C CB  . ARG D 74  ? 0.5406 0.4880 0.4993 -0.0274 -0.0336 0.0320  74  ARG D CB  
4944 C CG  . ARG D 74  ? 0.6198 0.5476 0.5317 -0.0068 -0.0548 0.0481  74  ARG D CG  
4945 C CD  . ARG D 74  ? 0.6425 0.6243 0.6020 0.0077  -0.0844 0.0577  74  ARG D CD  
4946 N NE  . ARG D 74  ? 0.6804 0.6898 0.6667 -0.0136 -0.0972 0.0420  74  ARG D NE  
4947 C CZ  . ARG D 74  ? 0.6994 0.7525 0.7170 -0.0104 -0.1262 0.0472  74  ARG D CZ  
4948 N NH1 . ARG D 74  ? 0.6688 0.7513 0.6991 0.0149  -0.1450 0.0690  74  ARG D NH1 
4949 N NH2 . ARG D 74  ? 0.6898 0.7575 0.7239 -0.0332 -0.1367 0.0306  74  ARG D NH2 
4950 N N   . ARG D 75  ? 0.4795 0.4197 0.4564 -0.0768 0.0268  -0.0044 75  ARG D N   
4951 C CA  . ARG D 75  ? 0.4339 0.4016 0.4588 -0.0899 0.0483  -0.0160 75  ARG D CA  
4952 C C   . ARG D 75  ? 0.4661 0.4065 0.4484 -0.1068 0.0783  -0.0232 75  ARG D C   
4953 O O   . ARG D 75  ? 0.4719 0.4316 0.4780 -0.1199 0.0961  -0.0360 75  ARG D O   
4954 C CB  . ARG D 75  ? 0.4011 0.3950 0.4601 -0.0986 0.0364  -0.0310 75  ARG D CB  
4955 C CG  . ARG D 75  ? 0.4000 0.4254 0.5011 -0.0869 0.0052  -0.0231 75  ARG D CG  
4956 C CD  . ARG D 75  ? 0.3513 0.4097 0.5082 -0.0973 -0.0006 -0.0354 75  ARG D CD  
4957 N NE  . ARG D 75  ? 0.4359 0.4863 0.5711 -0.1043 -0.0259 -0.0446 75  ARG D NE  
4958 C CZ  . ARG D 75  ? 0.4709 0.5414 0.6439 -0.1143 -0.0388 -0.0550 75  ARG D CZ  
4959 N NH1 . ARG D 75  ? 0.4230 0.5249 0.6607 -0.1169 -0.0297 -0.0558 75  ARG D NH1 
4960 N NH2 . ARG D 75  ? 0.5020 0.5587 0.6451 -0.1227 -0.0617 -0.0646 75  ARG D NH2 
4961 N N   . GLY D 76  ? 0.4849 0.3814 0.4031 -0.1071 0.0839  -0.0142 76  GLY D N   
4962 C CA  . GLY D 76  ? 0.4760 0.3487 0.3515 -0.1259 0.1117  -0.0175 76  GLY D CA  
4963 C C   . GLY D 76  ? 0.5388 0.4031 0.3760 -0.1426 0.1181  -0.0322 76  GLY D C   
4964 O O   . GLY D 76  ? 0.5686 0.4337 0.3982 -0.1399 0.0996  -0.0405 76  GLY D O   
4965 O OXT . GLY D 76  ? 0.5220 0.3824 0.3370 -0.1538 0.1362  -0.0370 76  GLY D OXT 
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