data_8Z2D
# 
_entry.id   8Z2D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z2D         pdb_00008z2d 10.2210/pdb8z2d/pdb 
WWPDB D_1300046887 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_DOI'    
5 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
6 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z2D 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'The same protein in the dark-adapted form'                          8Z1J unspecified 
PDB 'The same protein 10 ns after illumination of the dark-adapted form' 8Z24 unspecified 
PDB 'The same protein 30 ns after illumination of the dark-adapted form' 8Z26 unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mmaestre@ntu.edu.tw              Manuel      Maestre-Reyna ? 'principal investigator/group leader' 0000-0002-9566-7216 
3 mdtsai@gate.sinica.edu.tw        Ming-Daw    Tsai          ? 'principal investigator/group leader' 0000-0003-1374-0414 
4 yamamoto.junpei.es@osaka-u.ac.jp Junpei      Yamamoto      ? 'principal investigator/group leader' 0000-0002-5036-991X 
5 essen@chemie.uni-marburg.de      Lars-Oliver Essen         ? 'principal investigator/group leader' 0000-0003-4272-4026 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Maestre-Reyna, M.'  1  ? 
'Hosokawa, Y.'       2  ? 
'Wang, P.-H.'        3  ? 
'Saft, M.'           4  ? 
'Caramello, N.'      5  ? 
'Engilberge, S.'     6  ? 
'Franz-Badur, S.'    7  ? 
'Ngura Putu, E.P.G.' 8  ? 
'Nakamura, M.'       9  ? 
'Wu, W.-J.'          10 ? 
'Wu, H.-Y.'          11 ? 
'Lee, C.-C.'         12 ? 
'Huang, W.-C.'       13 ? 
'Huang, K.-F.'       14 ? 
'Chang, Y.-K.'       15 ? 
'Yang, C.-H.'        16 ? 
'Lin, W.-T.'         17 ? 
'Yang, K.-C.'        18 ? 
'Ban, Y.'            19 ? 
'Imura, T.'          20 ? 
'Kazuoka, A.'        21 ? 
'Tanida, E.'         22 ? 
'Owada, S.'          23 ? 
'Joti, Y.'           24 ? 
'Tanaka, R.'         25 ? 
'Tanaka, T.'         26 ? 
'Luo, F.'            27 ? 
'Tono, K.'           28 ? 
'Kiontke, S.'        29 ? 
'Korf, L.'           30 ? 
'Umena, Y.'          31 ? 
'Tosha, T.'          32 ? 
'Bessho, Y.'         33 ? 
'Nango, E.'          34 ? 
'Iwata, S.'          35 ? 
'Royant, A.'         36 ? 
'Tsai, M.-D.'        37 ? 
'Yamamoto, J.'       38 ? 
'Essen, L.-O.'       39 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                eadu7247 
_citation.page_last                 eadu7247 
_citation.title                     
'Capturing structural intermediates in an animal-like cryptochrome photoreceptor by time-resolved crystallography.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.adu7247 
_citation.pdbx_database_id_PubMed   40378212 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Maestre-Reyna, M.'       1  0000-0002-9566-7216 
primary 'Hosokawa, Y.'            2  0000-0001-9559-8567 
primary 'Wang, P.H.'              3  0000-0001-7359-934X 
primary 'Saft, M.'                4  0000-0003-3943-2786 
primary 'Caramello, N.'           5  0000-0003-0025-0213 
primary 'Engilberge, S.'          6  0000-0001-8680-6790 
primary 'Franz-Badur, S.'         7  ?                   
primary 'Gusti Ngurah Putu, E.P.' 8  0000-0003-1658-4015 
primary 'Nakamura, M.'            9  0009-0001-3017-1981 
primary 'Wu, W.J.'                10 0000-0002-7253-5384 
primary 'Wu, H.Y.'                11 0000-0001-5449-8295 
primary 'Lee, C.C.'               12 0000-0002-8259-4388 
primary 'Huang, W.C.'             13 0000-0003-4437-3530 
primary 'Huang, K.F.'             14 0000-0001-5235-7421 
primary 'Chang, Y.K.'             15 0000-0003-0314-3165 
primary 'Yang, C.H.'              16 0000-0001-7517-3799 
primary 'Fong, M.I.'              17 0009-0002-4710-1039 
primary 'Lin, W.T.'               18 0009-0004-3149-205X 
primary 'Yang, K.C.'              19 0009-0006-9790-1244 
primary 'Ban, Y.'                 20 ?                   
primary 'Imura, T.'               21 ?                   
primary 'Kazuoka, A.'             22 ?                   
primary 'Tanida, E.'              23 ?                   
primary 'Owada, S.'               24 0000-0002-1451-7612 
primary 'Joti, Y.'                25 0000-0002-4040-5972 
primary 'Tanaka, R.'              26 0000-0003-1062-4792 
primary 'Tanaka, T.'              27 ?                   
primary 'Kang, J.'                28 0000-0002-3506-6400 
primary 'Luo, F.'                 29 0000-0003-0631-6236 
primary 'Tono, K.'                30 0000-0003-1218-3759 
primary 'Kiontke, S.'             31 0000-0001-5822-913X 
primary 'Korf, L.'                32 0000-0003-4882-1177 
primary 'Umena, Y.'               33 ?                   
primary 'Tosha, T.'               34 0000-0002-8971-0759 
primary 'Bessho, Y.'              35 0000-0001-9297-7473 
primary 'Nango, E.'               36 0000-0001-9851-7355 
primary 'Iwata, S.'               37 0000-0003-1735-2937 
primary 'Royant, A.'              38 0000-0002-1919-8649 
primary 'Tsai, M.D.'              39 0000-0003-1374-0414 
primary 'Yamamoto, J.'            40 0000-0002-5036-991X 
primary 'Essen, L.O.'             41 0000-0003-4272-4026 
# 
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 'Cryptochrome photoreceptor'  57807.066 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                35.453    1   ? ? ? ? 
4 water       nat water                         18.015    155 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'CHLORIDE ION'                CL  
4 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLY n 
1 4   VAL n 
1 5   LYS n 
1 6   ASN n 
1 7   SER n 
1 8   ILE n 
1 9   ILE n 
1 10  TRP n 
1 11  PHE n 
1 12  ARG n 
1 13  LYS n 
1 14  GLY n 
1 15  LEU n 
1 16  ARG n 
1 17  LEU n 
1 18  HIS n 
1 19  ASP n 
1 20  ASN n 
1 21  PRO n 
1 22  ALA n 
1 23  LEU n 
1 24  LEU n 
1 25  GLU n 
1 26  ALA n 
1 27  CYS n 
1 28  LYS n 
1 29  ASP n 
1 30  ALA n 
1 31  LYS n 
1 32  HIS n 
1 33  VAL n 
1 34  TYR n 
1 35  PRO n 
1 36  VAL n 
1 37  PHE n 
1 38  VAL n 
1 39  LEU n 
1 40  ASP n 
1 41  PRO n 
1 42  HIS n 
1 43  PHE n 
1 44  LEU n 
1 45  GLN n 
1 46  GLN n 
1 47  SER n 
1 48  SER n 
1 49  TYR n 
1 50  LYS n 
1 51  VAL n 
1 52  SER n 
1 53  VAL n 
1 54  ASN n 
1 55  ARG n 
1 56  TYR n 
1 57  ASN n 
1 58  PHE n 
1 59  LEU n 
1 60  LEU n 
1 61  GLU n 
1 62  SER n 
1 63  LEU n 
1 64  GLU n 
1 65  ASP n 
1 66  LEU n 
1 67  GLN n 
1 68  ARG n 
1 69  SER n 
1 70  PHE n 
1 71  GLN n 
1 72  ALA n 
1 73  ARG n 
1 74  GLY n 
1 75  SER n 
1 76  ARG n 
1 77  LEU n 
1 78  LEU n 
1 79  VAL n 
1 80  LEU n 
1 81  ARG n 
1 82  GLY n 
1 83  LYS n 
1 84  PRO n 
1 85  GLU n 
1 86  GLU n 
1 87  VAL n 
1 88  PHE n 
1 89  PRO n 
1 90  ARG n 
1 91  VAL n 
1 92  PHE n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  GLY n 
1 97  VAL n 
1 98  THR n 
1 99  GLN n 
1 100 LEU n 
1 101 CYS n 
1 102 PHE n 
1 103 GLU n 
1 104 HIS n 
1 105 ASP n 
1 106 THR n 
1 107 GLU n 
1 108 PRO n 
1 109 TYR n 
1 110 ALA n 
1 111 LYS n 
1 112 VAL n 
1 113 ARG n 
1 114 ASP n 
1 115 ALA n 
1 116 ALA n 
1 117 VAL n 
1 118 ARG n 
1 119 ARG n 
1 120 LEU n 
1 121 ALA n 
1 122 ALA n 
1 123 GLU n 
1 124 ALA n 
1 125 GLY n 
1 126 VAL n 
1 127 GLU n 
1 128 VAL n 
1 129 VAL n 
1 130 THR n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 HIS n 
1 135 THR n 
1 136 LEU n 
1 137 TYR n 
1 138 ASP n 
1 139 THR n 
1 140 ASP n 
1 141 MET n 
1 142 LEU n 
1 143 VAL n 
1 144 ALA n 
1 145 ARG n 
1 146 ASN n 
1 147 GLY n 
1 148 GLY n 
1 149 ALA n 
1 150 ALA n 
1 151 PRO n 
1 152 LEU n 
1 153 THR n 
1 154 MET n 
1 155 GLN n 
1 156 SER n 
1 157 PHE n 
1 158 THR n 
1 159 LYS n 
1 160 LEU n 
1 161 VAL n 
1 162 ASP n 
1 163 ARG n 
1 164 VAL n 
1 165 GLY n 
1 166 ASP n 
1 167 PRO n 
1 168 PRO n 
1 169 ALA n 
1 170 PRO n 
1 171 ALA n 
1 172 PRO n 
1 173 ASP n 
1 174 PRO n 
1 175 PRO n 
1 176 ALA n 
1 177 ALA n 
1 178 MET n 
1 179 PRO n 
1 180 PRO n 
1 181 PRO n 
1 182 ALA n 
1 183 GLU n 
1 184 ASP n 
1 185 MET n 
1 186 PRO n 
1 187 SER n 
1 188 ALA n 
1 189 ALA n 
1 190 PRO n 
1 191 ALA n 
1 192 ALA n 
1 193 THR n 
1 194 GLY n 
1 195 VAL n 
1 196 PRO n 
1 197 THR n 
1 198 TRP n 
1 199 GLN n 
1 200 GLU n 
1 201 VAL n 
1 202 GLY n 
1 203 PHE n 
1 204 LYS n 
1 205 GLU n 
1 206 PRO n 
1 207 PRO n 
1 208 LEU n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 LYS n 
1 213 GLY n 
1 214 GLY n 
1 215 GLU n 
1 216 THR n 
1 217 GLU n 
1 218 ALA n 
1 219 LEU n 
1 220 ALA n 
1 221 ARG n 
1 222 LEU n 
1 223 GLU n 
1 224 ALA n 
1 225 ALA n 
1 226 PHE n 
1 227 GLN n 
1 228 ASP n 
1 229 PRO n 
1 230 LYS n 
1 231 TRP n 
1 232 VAL n 
1 233 ALA n 
1 234 GLY n 
1 235 PHE n 
1 236 GLN n 
1 237 LYS n 
1 238 PRO n 
1 239 ASP n 
1 240 THR n 
1 241 ASP n 
1 242 PRO n 
1 243 SER n 
1 244 ALA n 
1 245 TRP n 
1 246 GLU n 
1 247 LYS n 
1 248 PRO n 
1 249 ALA n 
1 250 THR n 
1 251 THR n 
1 252 VAL n 
1 253 LEU n 
1 254 SER n 
1 255 PRO n 
1 256 TYR n 
1 257 LEU n 
1 258 LYS n 
1 259 PHE n 
1 260 GLY n 
1 261 CYS n 
1 262 LEU n 
1 263 SER n 
1 264 ALA n 
1 265 ARG n 
1 266 LEU n 
1 267 PHE n 
1 268 HIS n 
1 269 ALA n 
1 270 ARG n 
1 271 LEU n 
1 272 LEU n 
1 273 GLU n 
1 274 VAL n 
1 275 TYR n 
1 276 ARG n 
1 277 ARG n 
1 278 HIS n 
1 279 PRO n 
1 280 ALA n 
1 281 HIS n 
1 282 SER n 
1 283 GLN n 
1 284 PRO n 
1 285 PRO n 
1 286 VAL n 
1 287 SER n 
1 288 LEU n 
1 289 ARG n 
1 290 GLY n 
1 291 GLN n 
1 292 LEU n 
1 293 LEU n 
1 294 TRP n 
1 295 ARG n 
1 296 GLU n 
1 297 PHE n 
1 298 PHE n 
1 299 TYR n 
1 300 THR n 
1 301 VAL n 
1 302 GLY n 
1 303 SER n 
1 304 THR n 
1 305 THR n 
1 306 PRO n 
1 307 ASN n 
1 308 PHE n 
1 309 HIS n 
1 310 ARG n 
1 311 MET n 
1 312 ALA n 
1 313 GLY n 
1 314 ASN n 
1 315 PRO n 
1 316 VAL n 
1 317 CYS n 
1 318 LYS n 
1 319 GLN n 
1 320 ILE n 
1 321 ASP n 
1 322 TRP n 
1 323 ASP n 
1 324 ASP n 
1 325 ASN n 
1 326 PRO n 
1 327 GLU n 
1 328 PHE n 
1 329 LEU n 
1 330 ALA n 
1 331 ALA n 
1 332 TRP n 
1 333 ARG n 
1 334 GLU n 
1 335 ALA n 
1 336 ARG n 
1 337 THR n 
1 338 GLY n 
1 339 PHE n 
1 340 PRO n 
1 341 TRP n 
1 342 ILE n 
1 343 ASP n 
1 344 ALA n 
1 345 ILE n 
1 346 MET n 
1 347 THR n 
1 348 GLN n 
1 349 LEU n 
1 350 VAL n 
1 351 THR n 
1 352 TRP n 
1 353 GLY n 
1 354 TRP n 
1 355 MET n 
1 356 HIS n 
1 357 HIS n 
1 358 LEU n 
1 359 ALA n 
1 360 ARG n 
1 361 HIS n 
1 362 SER n 
1 363 VAL n 
1 364 ALA n 
1 365 CYS n 
1 366 PHE n 
1 367 LEU n 
1 368 THR n 
1 369 ARG n 
1 370 GLY n 
1 371 ASP n 
1 372 LEU n 
1 373 TYR n 
1 374 VAL n 
1 375 SER n 
1 376 TRP n 
1 377 GLU n 
1 378 ARG n 
1 379 GLY n 
1 380 MET n 
1 381 GLU n 
1 382 VAL n 
1 383 PHE n 
1 384 GLU n 
1 385 GLU n 
1 386 HIS n 
1 387 LEU n 
1 388 ILE n 
1 389 ASP n 
1 390 GLN n 
1 391 ASP n 
1 392 HIS n 
1 393 TYR n 
1 394 LEU n 
1 395 ASN n 
1 396 ALA n 
1 397 ALA n 
1 398 ASN n 
1 399 TRP n 
1 400 MET n 
1 401 TRP n 
1 402 LEU n 
1 403 SER n 
1 404 ALA n 
1 405 SER n 
1 406 ALA n 
1 407 PHE n 
1 408 PHE n 
1 409 SER n 
1 410 GLN n 
1 411 TYR n 
1 412 PHE n 
1 413 ARG n 
1 414 VAL n 
1 415 TYR n 
1 416 SER n 
1 417 PRO n 
1 418 VAL n 
1 419 VAL n 
1 420 PHE n 
1 421 GLY n 
1 422 LYS n 
1 423 LYS n 
1 424 TYR n 
1 425 ASP n 
1 426 PRO n 
1 427 GLU n 
1 428 GLY n 
1 429 ARG n 
1 430 PHE n 
1 431 ILE n 
1 432 ARG n 
1 433 LYS n 
1 434 PHE n 
1 435 LEU n 
1 436 PRO n 
1 437 VAL n 
1 438 LEU n 
1 439 LYS n 
1 440 ASP n 
1 441 MET n 
1 442 PRO n 
1 443 ALA n 
1 444 LYS n 
1 445 TYR n 
1 446 ILE n 
1 447 TYR n 
1 448 GLU n 
1 449 PRO n 
1 450 TRP n 
1 451 THR n 
1 452 ALA n 
1 453 PRO n 
1 454 LEU n 
1 455 GLU n 
1 456 VAL n 
1 457 GLN n 
1 458 ARG n 
1 459 LYS n 
1 460 ALA n 
1 461 GLY n 
1 462 CYS n 
1 463 VAL n 
1 464 VAL n 
1 465 GLY n 
1 466 ARG n 
1 467 ASP n 
1 468 TYR n 
1 469 PRO n 
1 470 ALA n 
1 471 PRO n 
1 472 ILE n 
1 473 VAL n 
1 474 ASP n 
1 475 HIS n 
1 476 ALA n 
1 477 VAL n 
1 478 ALA n 
1 479 SER n 
1 480 LYS n 
1 481 ALA n 
1 482 CYS n 
1 483 ILE n 
1 484 ALA n 
1 485 ARG n 
1 486 MET n 
1 487 ALA n 
1 488 ALA n 
1 489 ALA n 
1 490 TYR n 
1 491 ARG n 
1 492 ARG n 
1 493 SER n 
1 494 LYS n 
1 495 GLY n 
1 496 GLU n 
1 497 LYS n 
1 498 LEU n 
1 499 ALA n 
1 500 ALA n 
1 501 ALA n 
1 502 LEU n 
1 503 GLU n 
1 504 HIS n 
1 505 HIS n 
1 506 HIS n 
1 507 HIS n 
1 508 HIS n 
1 509 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   509 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'UVR3, CHLRE_06g278251v5, CHLREDRAFT_206002' 
_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      'Chlamydomonas reinhardtii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3055 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION'                ? 'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  SER 47  47  ?   ?   ?   A . n 
A 1 48  SER 48  48  ?   ?   ?   A . n 
A 1 49  TYR 49  49  ?   ?   ?   A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 TRP 198 198 198 TRP TRP A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 TRP 245 245 245 TRP TRP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 CYS 261 261 261 CYS CYS A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 HIS 278 278 278 HIS HIS A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 GLN 283 283 283 GLN GLN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 TRP 294 294 294 TRP TRP A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 ASN 307 307 307 ASN ASN A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 MET 311 311 311 MET MET A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 PRO 315 315 315 PRO PRO A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 GLN 319 319 319 GLN GLN A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 TRP 322 322 322 TRP TRP A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 MET 346 346 346 MET MET A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 TRP 352 352 352 TRP TRP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 MET 355 355 355 MET MET A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 HIS 357 357 357 HIS HIS A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 CYS 365 365 365 CYS CYS A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 MET 380 380 380 MET MET A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 HIS 392 392 392 HIS HIS A . n 
A 1 393 TYR 393 393 393 TYR TYR A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 TRP 399 399 399 TRP TRP A . n 
A 1 400 MET 400 400 400 MET MET A . n 
A 1 401 TRP 401 401 401 TRP TRP A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 GLN 410 410 410 GLN GLN A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 TYR 424 424 424 TYR TYR A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 PHE 430 430 430 PHE PHE A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 LYS 439 439 439 LYS LYS A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 MET 441 441 441 MET MET A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 ALA 443 443 443 ALA ALA A . n 
A 1 444 LYS 444 444 444 LYS LYS A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 TYR 447 447 447 TYR TYR A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 THR 451 451 451 THR THR A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ARG 458 458 458 ARG ARG A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 VAL 464 464 464 VAL VAL A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 ARG 466 466 466 ARG ARG A . n 
A 1 467 ASP 467 467 467 ASP ASP A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 PRO 471 471 471 PRO PRO A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 VAL 473 473 473 VAL VAL A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 HIS 475 475 475 HIS HIS A . n 
A 1 476 ALA 476 476 476 ALA ALA A . n 
A 1 477 VAL 477 477 477 VAL VAL A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 SER 479 479 479 SER SER A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 CYS 482 482 482 CYS CYS A . n 
A 1 483 ILE 483 483 483 ILE ILE A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 MET 486 486 486 MET MET A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 TYR 490 490 490 TYR TYR A . n 
A 1 491 ARG 491 491 491 ARG ARG A . n 
A 1 492 ARG 492 492 492 ARG ARG A . n 
A 1 493 SER 493 493 493 SER SER A . n 
A 1 494 LYS 494 494 494 LYS LYS A . n 
A 1 495 GLY 495 495 ?   ?   ?   A . n 
A 1 496 GLU 496 496 ?   ?   ?   A . n 
A 1 497 LYS 497 497 ?   ?   ?   A . n 
A 1 498 LEU 498 498 ?   ?   ?   A . n 
A 1 499 ALA 499 499 ?   ?   ?   A . n 
A 1 500 ALA 500 500 ?   ?   ?   A . n 
A 1 501 ALA 501 501 ?   ?   ?   A . n 
A 1 502 LEU 502 502 ?   ?   ?   A . n 
A 1 503 GLU 503 503 ?   ?   ?   A . n 
A 1 504 HIS 504 504 ?   ?   ?   A . n 
A 1 505 HIS 505 505 ?   ?   ?   A . n 
A 1 506 HIS 506 506 ?   ?   ?   A . n 
A 1 507 HIS 507 507 ?   ?   ?   A . n 
A 1 508 HIS 508 508 ?   ?   ?   A . n 
A 1 509 HIS 509 509 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   601 602 FAD FAD A . 
C 3 CL  1   602 1   CL  CL  A . 
D 4 HOH 1   701 109 HOH HOH A . 
D 4 HOH 2   702 104 HOH HOH A . 
D 4 HOH 3   703 85  HOH HOH A . 
D 4 HOH 4   704 11  HOH HOH A . 
D 4 HOH 5   705 101 HOH HOH A . 
D 4 HOH 6   706 90  HOH HOH A . 
D 4 HOH 7   707 69  HOH HOH A . 
D 4 HOH 8   708 132 HOH HOH A . 
D 4 HOH 9   709 74  HOH HOH A . 
D 4 HOH 10  710 124 HOH HOH A . 
D 4 HOH 11  711 24  HOH HOH A . 
D 4 HOH 12  712 27  HOH HOH A . 
D 4 HOH 13  713 21  HOH HOH A . 
D 4 HOH 14  714 76  HOH HOH A . 
D 4 HOH 15  715 131 HOH HOH A . 
D 4 HOH 16  716 67  HOH HOH A . 
D 4 HOH 17  717 122 HOH HOH A . 
D 4 HOH 18  718 143 HOH HOH A . 
D 4 HOH 19  719 105 HOH HOH A . 
D 4 HOH 20  720 2   HOH HOH A . 
D 4 HOH 21  721 18  HOH HOH A . 
D 4 HOH 22  722 22  HOH HOH A . 
D 4 HOH 23  723 4   HOH HOH A . 
D 4 HOH 24  724 144 HOH HOH A . 
D 4 HOH 25  725 12  HOH HOH A . 
D 4 HOH 26  726 47  HOH HOH A . 
D 4 HOH 27  727 63  HOH HOH A . 
D 4 HOH 28  728 103 HOH HOH A . 
D 4 HOH 29  729 106 HOH HOH A . 
D 4 HOH 30  730 155 HOH HOH A . 
D 4 HOH 31  731 154 HOH HOH A . 
D 4 HOH 32  732 51  HOH HOH A . 
D 4 HOH 33  733 43  HOH HOH A . 
D 4 HOH 34  734 126 HOH HOH A . 
D 4 HOH 35  735 140 HOH HOH A . 
D 4 HOH 36  736 1   HOH HOH A . 
D 4 HOH 37  737 52  HOH HOH A . 
D 4 HOH 38  738 112 HOH HOH A . 
D 4 HOH 39  739 36  HOH HOH A . 
D 4 HOH 40  740 5   HOH HOH A . 
D 4 HOH 41  741 42  HOH HOH A . 
D 4 HOH 42  742 8   HOH HOH A . 
D 4 HOH 43  743 23  HOH HOH A . 
D 4 HOH 44  744 79  HOH HOH A . 
D 4 HOH 45  745 59  HOH HOH A . 
D 4 HOH 46  746 57  HOH HOH A . 
D 4 HOH 47  747 17  HOH HOH A . 
D 4 HOH 48  748 28  HOH HOH A . 
D 4 HOH 49  749 6   HOH HOH A . 
D 4 HOH 50  750 111 HOH HOH A . 
D 4 HOH 51  751 119 HOH HOH A . 
D 4 HOH 52  752 129 HOH HOH A . 
D 4 HOH 53  753 45  HOH HOH A . 
D 4 HOH 54  754 128 HOH HOH A . 
D 4 HOH 55  755 108 HOH HOH A . 
D 4 HOH 56  756 134 HOH HOH A . 
D 4 HOH 57  757 84  HOH HOH A . 
D 4 HOH 58  758 139 HOH HOH A . 
D 4 HOH 59  759 151 HOH HOH A . 
D 4 HOH 60  760 10  HOH HOH A . 
D 4 HOH 61  761 83  HOH HOH A . 
D 4 HOH 62  762 150 HOH HOH A . 
D 4 HOH 63  763 96  HOH HOH A . 
D 4 HOH 64  764 37  HOH HOH A . 
D 4 HOH 65  765 125 HOH HOH A . 
D 4 HOH 66  766 39  HOH HOH A . 
D 4 HOH 67  767 38  HOH HOH A . 
D 4 HOH 68  768 13  HOH HOH A . 
D 4 HOH 69  769 30  HOH HOH A . 
D 4 HOH 70  770 98  HOH HOH A . 
D 4 HOH 71  771 15  HOH HOH A . 
D 4 HOH 72  772 26  HOH HOH A . 
D 4 HOH 73  773 142 HOH HOH A . 
D 4 HOH 74  774 87  HOH HOH A . 
D 4 HOH 75  775 81  HOH HOH A . 
D 4 HOH 76  776 35  HOH HOH A . 
D 4 HOH 77  777 19  HOH HOH A . 
D 4 HOH 78  778 49  HOH HOH A . 
D 4 HOH 79  779 113 HOH HOH A . 
D 4 HOH 80  780 48  HOH HOH A . 
D 4 HOH 81  781 29  HOH HOH A . 
D 4 HOH 82  782 121 HOH HOH A . 
D 4 HOH 83  783 78  HOH HOH A . 
D 4 HOH 84  784 7   HOH HOH A . 
D 4 HOH 85  785 95  HOH HOH A . 
D 4 HOH 86  786 61  HOH HOH A . 
D 4 HOH 87  787 136 HOH HOH A . 
D 4 HOH 88  788 118 HOH HOH A . 
D 4 HOH 89  789 141 HOH HOH A . 
D 4 HOH 90  790 116 HOH HOH A . 
D 4 HOH 91  791 50  HOH HOH A . 
D 4 HOH 92  792 9   HOH HOH A . 
D 4 HOH 93  793 20  HOH HOH A . 
D 4 HOH 94  794 120 HOH HOH A . 
D 4 HOH 95  795 127 HOH HOH A . 
D 4 HOH 96  796 71  HOH HOH A . 
D 4 HOH 97  797 86  HOH HOH A . 
D 4 HOH 98  798 88  HOH HOH A . 
D 4 HOH 99  799 65  HOH HOH A . 
D 4 HOH 100 800 3   HOH HOH A . 
D 4 HOH 101 801 114 HOH HOH A . 
D 4 HOH 102 802 32  HOH HOH A . 
D 4 HOH 103 803 91  HOH HOH A . 
D 4 HOH 104 804 137 HOH HOH A . 
D 4 HOH 105 805 149 HOH HOH A . 
D 4 HOH 106 806 80  HOH HOH A . 
D 4 HOH 107 807 60  HOH HOH A . 
D 4 HOH 108 808 40  HOH HOH A . 
D 4 HOH 109 809 62  HOH HOH A . 
D 4 HOH 110 810 107 HOH HOH A . 
D 4 HOH 111 811 16  HOH HOH A . 
D 4 HOH 112 812 92  HOH HOH A . 
D 4 HOH 113 813 97  HOH HOH A . 
D 4 HOH 114 814 138 HOH HOH A . 
D 4 HOH 115 815 14  HOH HOH A . 
D 4 HOH 116 816 133 HOH HOH A . 
D 4 HOH 117 817 110 HOH HOH A . 
D 4 HOH 118 818 25  HOH HOH A . 
D 4 HOH 119 819 135 HOH HOH A . 
D 4 HOH 120 820 44  HOH HOH A . 
D 4 HOH 121 821 54  HOH HOH A . 
D 4 HOH 122 822 75  HOH HOH A . 
D 4 HOH 123 823 64  HOH HOH A . 
D 4 HOH 124 824 77  HOH HOH A . 
D 4 HOH 125 825 82  HOH HOH A . 
D 4 HOH 126 826 148 HOH HOH A . 
D 4 HOH 127 827 147 HOH HOH A . 
D 4 HOH 128 828 33  HOH HOH A . 
D 4 HOH 129 829 31  HOH HOH A . 
D 4 HOH 130 830 56  HOH HOH A . 
D 4 HOH 131 831 41  HOH HOH A . 
D 4 HOH 132 832 99  HOH HOH A . 
D 4 HOH 133 833 34  HOH HOH A . 
D 4 HOH 134 834 93  HOH HOH A . 
D 4 HOH 135 835 53  HOH HOH A . 
D 4 HOH 136 836 102 HOH HOH A . 
D 4 HOH 137 837 146 HOH HOH A . 
D 4 HOH 138 838 130 HOH HOH A . 
D 4 HOH 139 839 115 HOH HOH A . 
D 4 HOH 140 840 152 HOH HOH A . 
D 4 HOH 141 841 145 HOH HOH A . 
D 4 HOH 142 842 58  HOH HOH A . 
D 4 HOH 143 843 46  HOH HOH A . 
D 4 HOH 144 844 55  HOH HOH A . 
D 4 HOH 145 845 100 HOH HOH A . 
D 4 HOH 146 846 73  HOH HOH A . 
D 4 HOH 147 847 72  HOH HOH A . 
D 4 HOH 148 848 70  HOH HOH A . 
D 4 HOH 149 849 153 HOH HOH A . 
D 4 HOH 150 850 94  HOH HOH A . 
D 4 HOH 151 851 66  HOH HOH A . 
D 4 HOH 152 852 68  HOH HOH A . 
D 4 HOH 153 853 89  HOH HOH A . 
D 4 HOH 154 854 123 HOH HOH A . 
D 4 HOH 155 855 117 HOH HOH A . 
# 
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 GLY 3   ? N   ? A GLY 3   N   
2  1 Y 1 A GLY 3   ? CA  ? A GLY 3   CA  
3  1 Y 0 A LYS 28  ? CD  ? A LYS 28  CD  
4  1 Y 0 A LYS 28  ? CE  ? A LYS 28  CE  
5  1 Y 0 A LYS 28  ? NZ  ? A LYS 28  NZ  
6  1 Y 0 A LYS 31  ? NZ  ? A LYS 31  NZ  
7  1 Y 0 A LEU 44  ? CG  ? A LEU 44  CG  
8  1 Y 0 A LEU 44  ? CD1 ? A LEU 44  CD1 
9  1 Y 0 A LEU 44  ? CD2 ? A LEU 44  CD2 
10 1 Y 0 A GLN 45  ? CG  ? A GLN 45  CG  
11 1 Y 0 A GLN 45  ? CD  ? A GLN 45  CD  
12 1 Y 0 A GLN 45  ? OE1 ? A GLN 45  OE1 
13 1 Y 0 A GLN 45  ? NE2 ? A GLN 45  NE2 
14 1 Y 0 A GLN 46  ? CB  ? A GLN 46  CB  
15 1 Y 0 A GLN 46  ? CG  ? A GLN 46  CG  
16 1 Y 0 A GLN 46  ? CD  ? A GLN 46  CD  
17 1 Y 0 A GLN 46  ? OE1 ? A GLN 46  OE1 
18 1 Y 0 A GLN 46  ? NE2 ? A GLN 46  NE2 
19 1 Y 1 A LYS 50  ? CG  ? A LYS 50  CG  
20 1 Y 1 A LYS 50  ? CD  ? A LYS 50  CD  
21 1 Y 1 A LYS 50  ? CE  ? A LYS 50  CE  
22 1 Y 1 A LYS 50  ? NZ  ? A LYS 50  NZ  
23 1 Y 0 A ARG 119 ? CG  ? A ARG 119 CG  
24 1 Y 0 A ARG 119 ? CD  ? A ARG 119 CD  
25 1 Y 0 A ARG 119 ? NE  ? A ARG 119 NE  
26 1 Y 0 A ARG 119 ? CZ  ? A ARG 119 CZ  
27 1 Y 0 A ARG 119 ? NH1 ? A ARG 119 NH1 
28 1 Y 0 A ARG 119 ? NH2 ? A ARG 119 NH2 
29 1 Y 0 A ARG 145 ? CZ  ? A ARG 145 CZ  
30 1 Y 0 A ARG 145 ? NH1 ? A ARG 145 NH1 
31 1 Y 0 A GLN 155 ? CD  ? A GLN 155 CD  
32 1 Y 0 A GLN 155 ? OE1 ? A GLN 155 OE1 
33 1 Y 0 A GLN 155 ? NE2 ? A GLN 155 NE2 
34 1 Y 0 A LYS 159 ? CD  ? A LYS 159 CD  
35 1 Y 0 A LYS 159 ? CE  ? A LYS 159 CE  
36 1 Y 0 A LYS 159 ? NZ  ? A LYS 159 NZ  
37 1 Y 0 A GLU 183 ? CG  ? A GLU 183 CG  
38 1 Y 0 A GLU 183 ? CD  ? A GLU 183 CD  
39 1 Y 0 A GLU 183 ? OE1 ? A GLU 183 OE1 
40 1 Y 0 A GLU 183 ? OE2 ? A GLU 183 OE2 
41 1 Y 0 A LYS 204 ? CD  ? A LYS 204 CD  
42 1 Y 0 A LYS 204 ? CE  ? A LYS 204 CE  
43 1 Y 0 A LYS 204 ? NZ  ? A LYS 204 NZ  
44 1 Y 0 A GLU 205 ? CG  ? A GLU 205 CG  
45 1 Y 0 A GLU 205 ? CD  ? A GLU 205 CD  
46 1 Y 0 A GLU 205 ? OE1 ? A GLU 205 OE1 
47 1 Y 0 A GLU 205 ? OE2 ? A GLU 205 OE2 
48 1 Y 0 A LYS 230 ? CE  ? A LYS 230 CE  
49 1 Y 0 A LYS 230 ? NZ  ? A LYS 230 NZ  
50 1 Y 0 A LYS 247 ? CD  ? A LYS 247 CD  
51 1 Y 0 A LYS 247 ? CE  ? A LYS 247 CE  
52 1 Y 0 A LYS 247 ? NZ  ? A LYS 247 NZ  
53 1 Y 0 A ARG 276 ? CD  ? A ARG 276 CD  
54 1 Y 0 A ARG 276 ? NE  ? A ARG 276 NE  
55 1 Y 0 A ARG 276 ? CZ  ? A ARG 276 CZ  
56 1 Y 0 A ARG 276 ? NH1 ? A ARG 276 NH1 
57 1 Y 0 A ARG 276 ? NH2 ? A ARG 276 NH2 
58 1 Y 0 A ARG 277 ? NE  ? A ARG 277 NE  
59 1 Y 0 A ARG 277 ? CZ  ? A ARG 277 CZ  
60 1 Y 0 A ARG 277 ? NH1 ? A ARG 277 NH1 
61 1 Y 0 A ARG 277 ? NH2 ? A ARG 277 NH2 
62 1 Y 0 A ARG 310 ? CZ  ? A ARG 310 CZ  
63 1 Y 0 A ARG 310 ? NH1 ? A ARG 310 NH1 
64 1 Y 0 A ARG 310 ? NH2 ? A ARG 310 NH2 
65 1 Y 0 A LYS 318 ? CE  ? A LYS 318 CE  
66 1 Y 0 A LYS 318 ? NZ  ? A LYS 318 NZ  
67 1 Y 0 A LYS 423 ? CG  ? A LYS 423 CG  
68 1 Y 0 A LYS 423 ? CD  ? A LYS 423 CD  
69 1 Y 0 A LYS 423 ? CE  ? A LYS 423 CE  
70 1 Y 0 A LYS 423 ? NZ  ? A LYS 423 NZ  
71 1 Y 0 A ARG 429 ? NE  ? A ARG 429 NE  
72 1 Y 0 A ARG 429 ? CZ  ? A ARG 429 CZ  
73 1 Y 0 A LYS 439 ? CD  ? A LYS 439 CD  
74 1 Y 0 A LYS 439 ? CE  ? A LYS 439 CE  
75 1 Y 0 A LYS 439 ? NZ  ? A LYS 439 NZ  
76 1 Y 0 A LYS 444 ? CE  ? A LYS 444 CE  
77 1 Y 0 A LYS 444 ? NZ  ? A LYS 444 NZ  
78 1 Y 0 A GLU 455 ? CD  ? A GLU 455 CD  
79 1 Y 0 A GLU 455 ? OE1 ? A GLU 455 OE1 
80 1 Y 0 A GLU 455 ? OE2 ? A GLU 455 OE2 
81 1 Y 0 A ARG 458 ? CD  ? A ARG 458 CD  
82 1 Y 0 A ARG 458 ? NE  ? A ARG 458 NE  
83 1 Y 0 A ARG 458 ? CZ  ? A ARG 458 CZ  
84 1 Y 0 A ARG 458 ? NH1 ? A ARG 458 NH1 
85 1 Y 0 A ARG 458 ? NH2 ? A ARG 458 NH2 
86 1 Y 0 A LYS 459 ? CD  ? A LYS 459 CD  
87 1 Y 0 A LYS 459 ? CE  ? A LYS 459 CE  
88 1 Y 0 A LYS 459 ? NZ  ? A LYS 459 NZ  
89 1 Y 0 A LYS 480 ? CE  ? A LYS 480 CE  
90 1 Y 0 A LYS 480 ? NZ  ? A LYS 480 NZ  
91 1 Y 1 A LYS 494 ? CG  ? A LYS 494 CG  
92 1 Y 1 A LYS 494 ? CD  ? A LYS 494 CD  
93 1 Y 1 A LYS 494 ? CE  ? A LYS 494 CE  
94 1 Y 1 A LYS 494 ? NZ  ? A LYS 494 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    ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z2D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.840 
_cell.length_a_esd                 ? 
_cell.length_b                     65.600 
_cell.length_b_esd                 ? 
_cell.length_c                     153.130 
_cell.length_c_esd                 ? 
_cell.volume                       510704.476 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8Z2D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z2D 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.48 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.6 
_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    '0.1 M MES, pH 5.6 (w/v) PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         MPCCD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.24 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SACLA BEAMLINE BL2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.24 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL2 
_diffrn_source.pdbx_synchrotron_site       SACLA 
# 
_reflns.B_iso_Wilson_estimate                          13.41 
_reflns.entry_id                                       8Z2D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               33.06 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     43294 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.94 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                307 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.08 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.87 
_reflns_shell.d_res_low                                     1.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.43 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2113 
_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                               63.7 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.515 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_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               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               14.60 
_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                                 8Z2D 
_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                            2.00 
_refine.ls_d_res_low                             30.58 
_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                     35458 
_refine.ls_number_reflns_R_free                  1105 
_refine.ls_number_reflns_R_work                  34353 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 3.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2032 
_refine.ls_R_factor_R_free                       0.2176 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2028 
_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                          0.00 
_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                      6FN3 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.8692 
_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                            0.1781 
_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                       2.00 
_refine_hist.d_res_low                        30.58 
_refine_hist.number_atoms_solvent             155 
_refine_hist.number_atoms_total               4123 
_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        3914 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.0035  ? 4142 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6758  ? 5664 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0420  ? 590  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0070  ? 730  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.7371 ? 1499 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.09  . . 132 4220 100.00 . . . . 0.3013 . . . . . . . . . . . 0.3066 
'X-RAY DIFFRACTION' 2.09 2.20  . . 140 4235 100.00 . . . . 0.2812 . . . . . . . . . . . 0.2752 
'X-RAY DIFFRACTION' 2.20 2.34  . . 141 4222 100.00 . . . . 0.2636 . . . . . . . . . . . 0.2842 
'X-RAY DIFFRACTION' 2.34 2.52  . . 123 4284 100.00 . . . . 0.2535 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 2.52 2.77  . . 154 4227 100.00 . . . . 0.2371 . . . . . . . . . . . 0.2445 
'X-RAY DIFFRACTION' 2.77 3.17  . . 143 4299 100.00 . . . . 0.2126 . . . . . . . . . . . 0.2203 
'X-RAY DIFFRACTION' 3.17 4.00  . . 139 4322 100.00 . . . . 0.1570 . . . . . . . . . . . 0.1463 
'X-RAY DIFFRACTION' 4.00 30.58 . . 133 4544 99.91  . . . . 0.1238 . . . . . . . . . . . 0.1546 
# 
_struct.entry_id                     8Z2D 
_struct.title                        'SFX structure of CraCRY 100 ns after photoexcitation of the oxidized protein' 
_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        8Z2D 
_struct_keywords.text            'photoreceptor, FLAVOPROTEIN, time-resolved crystallography, 100 ns time-point' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8J8W0_CHLRE 
_struct_ref.pdbx_db_accession          A8J8W0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8Z2D 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 496 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A8J8W0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  496 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       496 
# 
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 8Z2D LYS A 497 ? UNP A8J8W0 ? ? 'expression tag' 497 1  
1 8Z2D LEU A 498 ? UNP A8J8W0 ? ? 'expression tag' 498 2  
1 8Z2D ALA A 499 ? UNP A8J8W0 ? ? 'expression tag' 499 3  
1 8Z2D ALA A 500 ? UNP A8J8W0 ? ? 'expression tag' 500 4  
1 8Z2D ALA A 501 ? UNP A8J8W0 ? ? 'expression tag' 501 5  
1 8Z2D LEU A 502 ? UNP A8J8W0 ? ? 'expression tag' 502 6  
1 8Z2D GLU A 503 ? UNP A8J8W0 ? ? 'expression tag' 503 7  
1 8Z2D HIS A 504 ? UNP A8J8W0 ? ? 'expression tag' 504 8  
1 8Z2D HIS A 505 ? UNP A8J8W0 ? ? 'expression tag' 505 9  
1 8Z2D HIS A 506 ? UNP A8J8W0 ? ? 'expression tag' 506 10 
1 8Z2D HIS A 507 ? UNP A8J8W0 ? ? 'expression tag' 507 11 
1 8Z2D HIS A 508 ? UNP A8J8W0 ? ? 'expression tag' 508 12 
1 8Z2D HIS A 509 ? UNP A8J8W0 ? ? 'expression tag' 509 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1380  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  20500 ? 
# 
_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 
# 
_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 ASN A 20  ? LYS A 28  ? ASN A 20  LYS A 28  1 ? 9  
HELX_P HELX_P2  AA2 SER A 52  ? ARG A 73  ? SER A 52  ARG A 73  1 ? 22 
HELX_P HELX_P3  AA3 LYS A 83  ? TRP A 95  ? LYS A 83  TRP A 95  1 ? 13 
HELX_P HELX_P4  AA4 GLU A 107 ? ALA A 124 ? GLU A 107 ALA A 124 1 ? 18 
HELX_P HELX_P5  AA5 ASP A 138 ? ASN A 146 ? ASP A 138 ASN A 146 1 ? 9  
HELX_P HELX_P6  AA6 THR A 153 ? GLY A 165 ? THR A 153 GLY A 165 1 ? 13 
HELX_P HELX_P7  AA7 MET A 185 ? ALA A 188 ? MET A 185 ALA A 188 5 ? 4  
HELX_P HELX_P8  AA8 ALA A 189 ? GLY A 194 ? ALA A 189 GLY A 194 1 ? 6  
HELX_P HELX_P9  AA9 GLY A 214 ? PHE A 226 ? GLY A 214 PHE A 226 1 ? 13 
HELX_P HELX_P10 AB1 ASP A 228 ? GLY A 234 ? ASP A 228 GLY A 234 1 ? 7  
HELX_P HELX_P11 AB2 GLN A 236 ? THR A 240 ? GLN A 236 THR A 240 5 ? 5  
HELX_P HELX_P12 AB3 LEU A 253 ? PHE A 259 ? LEU A 253 PHE A 259 1 ? 7  
HELX_P HELX_P13 AB4 SER A 263 ? HIS A 278 ? SER A 263 HIS A 278 1 ? 16 
HELX_P HELX_P14 AB5 SER A 287 ? THR A 304 ? SER A 287 THR A 304 1 ? 18 
HELX_P HELX_P15 AB6 ASN A 325 ? GLU A 334 ? ASN A 325 GLU A 334 1 ? 10 
HELX_P HELX_P16 AB7 PHE A 339 ? GLY A 353 ? PHE A 339 GLY A 353 1 ? 15 
HELX_P HELX_P17 AB8 HIS A 356 ? THR A 368 ? HIS A 356 THR A 368 1 ? 13 
HELX_P HELX_P18 AB9 SER A 375 ? LEU A 387 ? SER A 375 LEU A 387 1 ? 13 
HELX_P HELX_P19 AC1 ASP A 391 ? SER A 403 ? ASP A 391 SER A 403 1 ? 13 
HELX_P HELX_P20 AC2 PHE A 420 ? TYR A 424 ? PHE A 420 TYR A 424 5 ? 5  
HELX_P HELX_P21 AC3 GLY A 428 ? LEU A 435 ? GLY A 428 LEU A 435 1 ? 8  
HELX_P HELX_P22 AC4 PRO A 436 ? LYS A 439 ? PRO A 436 LYS A 439 5 ? 4  
HELX_P HELX_P23 AC5 PRO A 442 ? ILE A 446 ? PRO A 442 ILE A 446 5 ? 5  
HELX_P HELX_P24 AC6 GLU A 448 ? ALA A 452 ? GLU A 448 ALA A 452 5 ? 5  
HELX_P HELX_P25 AC7 PRO A 453 ? GLY A 461 ? PRO A 453 GLY A 461 1 ? 9  
HELX_P HELX_P26 AC8 ASP A 474 ? ARG A 492 ? ASP A 474 ARG A 492 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           284 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            284 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    285 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     285 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.61 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 78  ? ARG A 81  ? LEU A 78  ARG A 81  
AA1 2 HIS A 32  ? LEU A 39  ? HIS A 32  LEU A 39  
AA1 3 ASN A 6   ? PHE A 11  ? ASN A 6   PHE A 11  
AA1 4 GLN A 99  ? PHE A 102 ? GLN A 99  PHE A 102 
AA1 5 GLU A 127 ? VAL A 129 ? GLU A 127 VAL A 129 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 80  ? O LEU A 80  N LEU A 39  ? N LEU A 39  
AA1 2 3 O VAL A 36  ? O VAL A 36  N PHE A 11  ? N PHE A 11  
AA1 3 4 N TRP A 10  ? N TRP A 10  O CYS A 101 ? O CYS A 101 
AA1 4 5 N LEU A 100 ? N LEU A 100 O GLU A 127 ? O GLU A 127 
# 
_pdbx_entry_details.entry_id                   8Z2D 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 12  ? ? -131.91 -71.82  
2  1 LYS A 13  ? ? -102.45 -166.44 
3  1 GLN A 45  ? ? -111.57 55.34   
4  1 SER A 75  ? ? -122.20 -160.78 
5  1 SER A 133 ? ? -151.66 -10.92  
6  1 TRP A 322 ? ? -42.59  151.73  
7  1 ARG A 336 ? ? -140.75 43.51   
8  1 THR A 368 ? ? -91.66  -109.61 
9  1 ASP A 371 ? ? -138.85 -53.34  
10 1 PHE A 407 ? ? 67.30   -29.94  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.8017650941 7.19376780486  -15.0504043693 0.0777284749964 ? -0.00695553293483 ? 
-0.00480502555072 ? 0.0761271691125 ? -0.00326957875964 ? 0.0648537649017 ? 0.224353257251 ? -0.0927354152489 ? -0.0765018349137 ? 
0.513468936545 ? 0.128666259169  ? 0.236349029901 ? 0.00709575333606 ? 0.0246250729894 ? 0.0155465190955 ? -0.0229578590197 ? 
-0.000204407923443 ? 0.00378015706021  ? -0.0216865679711 ? -0.0393928869191 ? -0.0122517301989 ? 
2 'X-RAY DIFFRACTION' ? refined 11.3664591234 -18.3881245984 -26.160734517  0.0600090772697 ? 0.0142773210709   ? 
-0.00580658957489 ? 0.0482374665707 ? -0.00486340488008 ? 0.0520350012072 ? 0.410330405072 ? 0.258936398486   ? 0.00346944331621 ? 
0.349982935814 ? 0.0789501449552 ? 0.190760192818 ? 0.0157846089169  ? 0.0409476695967 ? -0.027633187389 ? -0.0359569942047 ? 
-0.00456294197339  ? 0.000999637581771 ? 0.00450210748583 ? -0.011681093757  ? -0.0133386984154 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 3   ? A 222 A 227 ? ? 
;chain 'A' and (resid 3 through 227 )
;
2 'X-RAY DIFFRACTION' 2 A 223 A 228 ? A 489 A 494 ? ? 
;chain 'A' and (resid 228 through 494 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A SER 47  ? A SER 47  
4  1 Y 1 A SER 48  ? A SER 48  
5  1 Y 1 A TYR 49  ? A TYR 49  
6  1 Y 1 A GLY 495 ? A GLY 495 
7  1 Y 1 A GLU 496 ? A GLU 496 
8  1 Y 1 A LYS 497 ? A LYS 497 
9  1 Y 1 A LEU 498 ? A LEU 498 
10 1 Y 1 A ALA 499 ? A ALA 499 
11 1 Y 1 A ALA 500 ? A ALA 500 
12 1 Y 1 A ALA 501 ? A ALA 501 
13 1 Y 1 A LEU 502 ? A LEU 502 
14 1 Y 1 A GLU 503 ? A GLU 503 
15 1 Y 1 A HIS 504 ? A HIS 504 
16 1 Y 1 A HIS 505 ? A HIS 505 
17 1 Y 1 A HIS 506 ? A HIS 506 
18 1 Y 1 A HIS 507 ? A HIS 507 
19 1 Y 1 A HIS 508 ? A HIS 508 
20 1 Y 1 A HIS 509 ? A HIS 509 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FAD PA     P  N R 89  
FAD O1A    O  N N 90  
FAD O2A    O  N N 91  
FAD O5B    O  N N 92  
FAD C5B    C  N N 93  
FAD C4B    C  N R 94  
FAD O4B    O  N N 95  
FAD C3B    C  N S 96  
FAD O3B    O  N N 97  
FAD C2B    C  N R 98  
FAD O2B    O  N N 99  
FAD C1B    C  N R 100 
FAD N9A    N  Y N 101 
FAD C8A    C  Y N 102 
FAD N7A    N  Y N 103 
FAD C5A    C  Y N 104 
FAD C6A    C  Y N 105 
FAD N6A    N  N N 106 
FAD N1A    N  Y N 107 
FAD C2A    C  Y N 108 
FAD N3A    N  Y N 109 
FAD C4A    C  Y N 110 
FAD N1     N  N N 111 
FAD C2     C  N N 112 
FAD O2     O  N N 113 
FAD N3     N  N N 114 
FAD C4     C  N N 115 
FAD O4     O  N N 116 
FAD C4X    C  N N 117 
FAD N5     N  N N 118 
FAD C5X    C  Y N 119 
FAD C6     C  Y N 120 
FAD C7     C  Y N 121 
FAD C7M    C  N N 122 
FAD C8     C  Y N 123 
FAD C8M    C  N N 124 
FAD C9     C  Y N 125 
FAD C9A    C  Y N 126 
FAD N10    N  N N 127 
FAD C10    C  N N 128 
FAD "C1'"  C  N N 129 
FAD "C2'"  C  N S 130 
FAD "O2'"  O  N N 131 
FAD "C3'"  C  N S 132 
FAD "O3'"  O  N N 133 
FAD "C4'"  C  N R 134 
FAD "O4'"  O  N N 135 
FAD "C5'"  C  N N 136 
FAD "O5'"  O  N N 137 
FAD P      P  N R 138 
FAD O1P    O  N N 139 
FAD O2P    O  N N 140 
FAD O3P    O  N N 141 
FAD HOA2   H  N N 142 
FAD H51A   H  N N 143 
FAD H52A   H  N N 144 
FAD H4B    H  N N 145 
FAD H3B    H  N N 146 
FAD HO3A   H  N N 147 
FAD H2B    H  N N 148 
FAD HO2A   H  N N 149 
FAD H1B    H  N N 150 
FAD H8A    H  N N 151 
FAD H61A   H  N N 152 
FAD H62A   H  N N 153 
FAD H2A    H  N N 154 
FAD HN3    H  N N 155 
FAD H6     H  N N 156 
FAD HM71   H  N N 157 
FAD HM72   H  N N 158 
FAD HM73   H  N N 159 
FAD HM81   H  N N 160 
FAD HM82   H  N N 161 
FAD HM83   H  N N 162 
FAD H9     H  N N 163 
FAD "H1'1" H  N N 164 
FAD "H1'2" H  N N 165 
FAD "H2'"  H  N N 166 
FAD "HO2'" H  N N 167 
FAD "H3'"  H  N N 168 
FAD "HO3'" H  N N 169 
FAD "H4'"  H  N N 170 
FAD "HO4'" H  N N 171 
FAD "H5'1" H  N N 172 
FAD "H5'2" H  N N 173 
FAD HOP2   H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-105-TPP         1 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-109-TPP2        2 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP20H05442             3 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP22H04751             4 
'Japan Science and Technology'                                           Japan  JPMJFR2057             5 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP19H05776             6 
'National Science Council (NSC, Taiwan)'                                 Taiwan 111-2113-M-002-029-MY3 7 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP21J13329             8 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6fn3 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          10 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              1.77 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_pdbx_serial_crystallography_sample_delivery_injection.diffrn_id               1 
_pdbx_serial_crystallography_sample_delivery_injection.description             'High viscosity injector' 
_pdbx_serial_crystallography_sample_delivery_injection.injector_diameter       75 
_pdbx_serial_crystallography_sample_delivery_injection.injector_temperature    293 
_pdbx_serial_crystallography_sample_delivery_injection.injector_pressure       ? 
_pdbx_serial_crystallography_sample_delivery_injection.flow_rate               2.8 
_pdbx_serial_crystallography_sample_delivery_injection.carrier_solvent         grease 
_pdbx_serial_crystallography_sample_delivery_injection.crystal_concentration   ? 
_pdbx_serial_crystallography_sample_delivery_injection.preparation             ? 
_pdbx_serial_crystallography_sample_delivery_injection.power_by                ? 
_pdbx_serial_crystallography_sample_delivery_injection.injector_nozzle         ? 
_pdbx_serial_crystallography_sample_delivery_injection.jet_diameter            ? 
_pdbx_serial_crystallography_sample_delivery_injection.filter_size             50 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z2D 
_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]   0.019670 
_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]   0.015244 
_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]   0.006530 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    C  C     . GLY A 1 3   ? 30.96151  29.44900  -9.39338  1.000 26.53631 ? 3   GLY A C     1 
ATOM   2    O  O     . GLY A 1 3   ? 32.04354  30.02894  -9.28237  1.000 29.07604 ? 3   GLY A O     1 
ATOM   3    N  N     . VAL A 1 4   ? 30.14850  29.22302  -8.35938  1.000 25.11667 ? 4   VAL A N     1 
ATOM   4    C  CA    . VAL A 1 4   ? 30.06044  27.89701  -7.75441  1.000 23.64222 ? 4   VAL A CA    1 
ATOM   5    C  C     . VAL A 1 4   ? 29.39939  26.92906  -8.72843  1.000 20.09351 ? 4   VAL A C     1 
ATOM   6    O  O     . VAL A 1 4   ? 28.69840  27.32212  -9.66542  1.000 18.48132 ? 4   VAL A O     1 
ATOM   7    C  CB    . VAL A 1 4   ? 29.29445  27.94401  -6.42041  1.000 16.73488 ? 4   VAL A CB    1 
ATOM   8    C  CG1   . VAL A 1 4   ? 29.66351  29.18898  -5.62938  1.000 19.07988 ? 4   VAL A CG1   1 
ATOM   9    C  CG2   . VAL A 1 4   ? 27.78744  27.87410  -6.66040  1.000 19.97673 ? 4   VAL A CG2   1 
ATOM   10   N  N     . LYS A 1 5   ? 29.60632  25.63705  -8.48046  1.000 16.81488 ? 5   LYS A N     1 
ATOM   11   C  CA    . LYS A 1 5   ? 29.10426  24.57409  -9.34349  1.000 14.24666 ? 5   LYS A CA    1 
ATOM   12   C  C     . LYS A 1 5   ? 27.94323  23.86014  -8.66450  1.000 11.92150 ? 5   LYS A C     1 
ATOM   13   O  O     . LYS A 1 5   ? 28.11820  23.26010  -7.59951  1.000 12.26774 ? 5   LYS A O     1 
ATOM   14   C  CB    . LYS A 1 5   ? 30.20121  23.56505  -9.68251  1.000 12.20625 ? 5   LYS A CB    1 
ATOM   15   C  CG    . LYS A 1 5   ? 29.72015  22.44509  -10.59554 1.000 14.53670 ? 5   LYS A CG    1 
ATOM   16   C  CD    . LYS A 1 5   ? 30.72109  21.30804  -10.68057 1.000 14.21129 ? 5   LYS A CD    1 
ATOM   17   C  CE    . LYS A 1 5   ? 30.17103  20.16309  -11.51359 1.000 9.12884  ? 5   LYS A CE    1 
ATOM   18   N  NZ    . LYS A 1 5   ? 31.09897  18.99904  -11.55162 1.000 9.95862  ? 5   LYS A NZ    1 
ATOM   19   N  N     . ASN A 1 6   ? 26.77123  23.91421  -9.29149  1.000 13.09813 ? 6   ASN A N     1 
ATOM   20   C  CA    . ASN A 1 6   ? 25.61819  23.10826  -8.91251  1.000 11.64662 ? 6   ASN A CA    1 
ATOM   21   C  C     . ASN A 1 6   ? 25.23714  22.25131  -10.11152 1.000 11.13335 ? 6   ASN A C     1 
ATOM   22   O  O     . ASN A 1 6   ? 25.04617  22.77534  -11.21351 1.000 10.63305 ? 6   ASN A O     1 
ATOM   23   C  CB    . ASN A 1 6   ? 24.44224  23.98931  -8.48048  1.000 11.54431 ? 6   ASN A CB    1 
ATOM   24   C  CG    . ASN A 1 6   ? 24.80629  24.94126  -7.35546  1.000 15.01701 ? 6   ASN A CG    1 
ATOM   25   O  OD1   . ASN A 1 6   ? 25.45727  24.55021  -6.38447  1.000 18.65701 ? 6   ASN A OD1   1 
ATOM   26   N  ND2   . ASN A 1 6   ? 24.39835  26.20129  -7.48643  1.000 10.63248 ? 6   ASN A ND2   1 
ATOM   27   N  N     . SER A 1 7   ? 25.14208  20.93831  -9.90556  1.000 11.97104 ? 7   SER A N     1 
ATOM   28   C  CA    . SER A 1 7   ? 24.95903  20.00634  -11.00958 1.000 10.93238 ? 7   SER A CA    1 
ATOM   29   C  C     . SER A 1 7   ? 23.76298  19.09740  -10.76359 1.000 8.39382  ? 7   SER A C     1 
ATOM   30   O  O     . SER A 1 7   ? 23.30498  18.91739  -9.63260  1.000 9.11836  ? 7   SER A O     1 
ATOM   31   C  CB    . SER A 1 7   ? 26.21298  19.15028  -11.23660 1.000 11.89927 ? 7   SER A CB    1 
ATOM   32   O  OG    . SER A 1 7   ? 26.49495  18.35224  -10.10362 1.000 10.74935 ? 7   SER A OG    1 
ATOM   33   N  N     . ILE A 1 8   ? 23.27095  18.51845  -11.85660 1.000 7.34646  ? 8   ILE A N     1 
ATOM   34   C  CA    . ILE A 1 8   ? 22.18790  17.54350  -11.84062 1.000 8.11279  ? 8   ILE A CA    1 
ATOM   35   C  C     . ILE A 1 8   ? 22.69983  16.26549  -12.48866 1.000 8.03993  ? 8   ILE A C     1 
ATOM   36   O  O     . ILE A 1 8   ? 23.27883  16.30849  -13.58066 1.000 10.58455 ? 8   ILE A O     1 
ATOM   37   C  CB    . ILE A 1 8   ? 20.94192  18.05758  -12.58361 1.000 6.43059  ? 8   ILE A CB    1 
ATOM   38   C  CG1   . ILE A 1 8   ? 20.35699  19.28460  -11.89358 1.000 7.54936  ? 8   ILE A CG1   1 
ATOM   39   C  CG2   . ILE A 1 8   ? 19.88287  16.97864  -12.66663 1.000 7.28736  ? 8   ILE A CG2   1 
ATOM   40   C  CD1   . ILE A 1 8   ? 19.13501  19.82167  -12.60056 1.000 6.65640  ? 8   ILE A CD1   1 
ATOM   41   N  N     . ILE A 1 9   ? 22.49478  15.13849  -11.81768 1.000 6.93956  ? 9   ILE A N     1 
ATOM   42   C  CA    . ILE A 1 9   ? 22.74271  13.82249  -12.39271 1.000 7.74228  ? 9   ILE A CA    1 
ATOM   43   C  C     . ILE A 1 9   ? 21.37868  13.21456  -12.69572 1.000 6.91534  ? 9   ILE A C     1 
ATOM   44   O  O     . ILE A 1 9   ? 20.64366  12.81258  -11.78373 1.000 6.93932  ? 9   ILE A O     1 
ATOM   45   C  CB    . ILE A 1 9   ? 23.58667  12.93242  -11.46574 1.000 9.14482  ? 9   ILE A CB    1 
ATOM   46   C  CG1   . ILE A 1 9   ? 23.54159  11.46944  -11.92477 1.000 9.15243  ? 9   ILE A CG1   1 
ATOM   47   C  CG2   . ILE A 1 9   ? 23.16568  13.09041  -10.00773 1.000 6.31531  ? 9   ILE A CG2   1 
ATOM   48   C  CD1   . ILE A 1 9   ? 24.13357  11.24244  -13.30278 1.000 9.06348  ? 9   ILE A CD1   1 
ATOM   49   N  N     . TRP A 1 10  ? 21.02767  13.17861  -13.97772 1.000 6.09937  ? 10  TRP A N     1 
ATOM   50   C  CA    . TRP A 1 10  ? 19.70865  12.74369  -14.41573 1.000 6.27523  ? 10  TRP A CA    1 
ATOM   51   C  C     . TRP A 1 10  ? 19.71057  11.23369  -14.60676 1.000 7.53895  ? 10  TRP A C     1 
ATOM   52   O  O     . TRP A 1 10  ? 20.43254  10.71268  -15.46478 1.000 7.49853  ? 10  TRP A O     1 
ATOM   53   C  CB    . TRP A 1 10  ? 19.31668  13.44974  -15.71371 1.000 8.26766  ? 10  TRP A CB    1 
ATOM   54   C  CG    . TRP A 1 10  ? 17.95366  13.08382  -16.22871 1.000 7.98222  ? 10  TRP A CG    1 
ATOM   55   C  CD1   . TRP A 1 10  ? 16.95863  12.44485  -15.54572 1.000 9.45987  ? 10  TRP A CD1   1 
ATOM   56   C  CD2   . TRP A 1 10  ? 17.43766  13.34188  -17.54070 1.000 7.44861  ? 10  TRP A CD2   1 
ATOM   57   N  NE1   . TRP A 1 10  ? 15.85661  12.28793  -16.35172 1.000 8.60488  ? 10  TRP A NE1   1 
ATOM   58   C  CE2   . TRP A 1 10  ? 16.12464  12.83094  -17.58071 1.000 10.02062 ? 10  TRP A CE2   1 
ATOM   59   C  CE3   . TRP A 1 10  ? 17.95769  13.95488  -18.68369 1.000 9.87383  ? 10  TRP A CE3   1 
ATOM   60   C  CZ2   . TRP A 1 10  ? 15.32464  12.91301  -18.71971 1.000 11.32121 ? 10  TRP A CZ2   1 
ATOM   61   C  CZ3   . TRP A 1 10  ? 17.16169  14.03794  -19.81469 1.000 11.74691 ? 10  TRP A CZ3   1 
ATOM   62   C  CH2   . TRP A 1 10  ? 15.86166  13.51801  -19.82369 1.000 10.55211 ? 10  TRP A CH2   1 
ATOM   63   N  N     . PHE A 1 11  ? 18.90054  10.53771  -13.81278 1.000 8.06203  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 18.74446  9.09472   -13.92881 1.000 7.04780  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 17.59844  8.76981   -14.87681 1.000 7.30542  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 16.50247  9.32786   -14.75380 1.000 7.23163  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 18.48144  8.46271   -12.55982 1.000 7.54401  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 19.70043  8.36562   -11.68383 1.000 6.24649  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 20.55838  7.28658   -11.78886 1.000 5.65577  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 19.98349  9.34559   -10.75181 1.000 6.58163  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 21.67538  7.18751   -10.98787 1.000 5.63226  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 21.10249  9.24851   -9.94882  1.000 7.52110  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 21.94843  8.16647   -10.06984 1.000 6.01038  ? 11  PHE A CZ    1 
ATOM   74   N  N     . ARG A 1 12  ? 17.86755  7.88142   -15.83064 1.000 8.05183  ? 12  ARG A N     1 
ATOM   75   C  CA    . ARG A 1 12  ? 16.84292  7.31803   -16.69818 1.000 8.43629  ? 12  ARG A CA    1 
ATOM   76   C  C     . ARG A 1 12  ? 17.04272  5.80949   -16.71825 1.000 7.34941  ? 12  ARG A C     1 
ATOM   77   O  O     . ARG A 1 12  ? 16.25791  5.06095   -16.12980 1.000 11.14222 ? 12  ARG A O     1 
ATOM   78   C  CB    . ARG A 1 12  ? 16.92145  7.90760   -18.10946 1.000 8.50443  ? 12  ARG A CB    1 
ATOM   79   C  CG    . ARG A 1 12  ? 16.86919  9.42693   -18.16194 1.000 8.70772  ? 12  ARG A CG    1 
ATOM   80   C  CD    . ARG A 1 12  ? 18.26184  10.02948  -18.18604 1.000 10.03439 ? 12  ARG A CD    1 
ATOM   81   N  NE    . ARG A 1 12  ? 19.01213  9.58958   -19.35820 1.000 11.56075 ? 12  ARG A NE    1 
ATOM   82   C  CZ    . ARG A 1 12  ? 18.93404  10.16164  -20.55284 1.000 10.90491 ? 12  ARG A CZ    1 
ATOM   83   N  NH1   . ARG A 1 12  ? 18.15427  11.20963  -20.76582 1.000 9.56460  ? 12  ARG A NH1   1 
ATOM   84   N  NH2   . ARG A 1 12  ? 19.65521  9.67030   -21.56006 1.000 9.18846  ? 12  ARG A NH2   1 
ATOM   85   N  N     . LYS A 1 13  ? 18.10226  5.36384   -17.38190 1.000 5.95863  ? 13  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 13  ? 18.63919  4.00981   -17.18893 1.000 5.85409  ? 13  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 13  ? 19.87721  4.27372   -16.29193 1.000 9.13424  ? 13  LYS A C     1 
ATOM   88   O  O     . LYS A 1 13  ? 20.00027  5.40371   -15.79490 1.000 7.53254  ? 13  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 13  ? 18.86815  3.30183   -18.53095 1.000 8.61649  ? 13  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 13  ? 17.63512  2.67990   -19.16696 1.000 13.93768 ? 13  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 13  ? 17.55312  2.87194   -20.66695 1.000 15.12892 ? 13  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 13  ? 18.71909  2.26190   -21.40897 1.000 16.16010 ? 13  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 13  ? 18.29205  1.53195   -22.62299 1.000 19.41504 ? 13  LYS A NZ    1 
ATOM   94   N  N     . GLY A 1 14  ? 20.76716  3.31167   -16.13295 1.000 5.68519  ? 14  GLY A N     1 
ATOM   95   C  CA    . GLY A 1 14  ? 21.92717  3.46860   -15.27595 1.000 5.69022  ? 14  GLY A CA    1 
ATOM   96   C  C     . GLY A 1 14  ? 21.55319  3.76558   -13.83795 1.000 6.46019  ? 14  GLY A C     1 
ATOM   97   O  O     . GLY A 1 14  ? 22.07324  4.70854   -13.23293 1.000 5.58108  ? 14  GLY A O     1 
ATOM   98   N  N     . LEU A 1 15  ? 20.64516  2.96061   -13.28496 1.000 5.60169  ? 15  LEU A N     1 
ATOM   99   C  CA    . LEU A 1 15  ? 20.15617  3.14261   -11.91796 1.000 5.61154  ? 15  LEU A CA    1 
ATOM   100  C  C     . LEU A 1 15  ? 21.10614  2.43954   -10.94998 1.000 6.15681  ? 15  LEU A C     1 
ATOM   101  O  O     . LEU A 1 15  ? 20.79409  1.41354   -10.34200 1.000 6.00413  ? 15  LEU A O     1 
ATOM   102  C  CB    . LEU A 1 15  ? 18.73314  2.61568   -11.78996 1.000 5.76954  ? 15  LEU A CB    1 
ATOM   103  C  CG    . LEU A 1 15  ? 17.72117  3.17275   -12.79195 1.000 5.98408  ? 15  LEU A CG    1 
ATOM   104  C  CD1   . LEU A 1 15  ? 16.36014  2.53881   -12.57795 1.000 5.85000  ? 15  LEU A CD1   1 
ATOM   105  C  CD2   . LEU A 1 15  ? 17.63524  4.68675   -12.69091 1.000 5.75168  ? 15  LEU A CD2   1 
ATOM   106  N  N     . ARG A 1 16  ? 22.28953  3.02851   -10.81439 1.000 5.81402  ? 16  ARG A N     1 
ATOM   107  C  CA    . ARG A 1 16  ? 23.33603  2.45158   -9.98559  1.000 7.75133  ? 16  ARG A CA    1 
ATOM   108  C  C     . ARG A 1 16  ? 24.29157  3.55739   -9.56824  1.000 8.38380  ? 16  ARG A C     1 
ATOM   109  O  O     . ARG A 1 16  ? 24.32127  4.63538   -10.16575 1.000 7.01236  ? 16  ARG A O     1 
ATOM   110  C  CB    . ARG A 1 16  ? 24.09549  1.34907   -10.72886 1.000 6.99539  ? 16  ARG A CB    1 
ATOM   111  C  CG    . ARG A 1 16  ? 24.88582  1.87475   -11.91046 1.000 7.87814  ? 16  ARG A CG    1 
ATOM   112  C  CD    . ARG A 1 16  ? 25.54096  0.76326   -12.69952 1.000 7.97524  ? 16  ARG A CD    1 
ATOM   113  N  NE    . ARG A 1 16  ? 26.27901  1.30264   -13.83514 1.000 7.38529  ? 16  ARG A NE    1 
ATOM   114  C  CZ    . ARG A 1 16  ? 25.76311  1.48263   -15.04458 1.000 7.50471  ? 16  ARG A CZ    1 
ATOM   115  N  NH1   . ARG A 1 16  ? 24.51472  1.15157   -15.31942 1.000 6.56851  ? 16  ARG A NH1   1 
ATOM   116  N  NH2   . ARG A 1 16  ? 26.51840  2.00837   -16.00491 1.000 9.46261  ? 16  ARG A NH2   1 
ATOM   117  N  N     . LEU A 1 17  ? 25.07119  3.27228   -8.52397  1.000 7.88849  ? 17  LEU A N     1 
ATOM   118  C  CA    . LEU A 1 17  ? 26.13924  4.16221   -8.08496  1.000 8.00572  ? 17  LEU A CA    1 
ATOM   119  C  C     . LEU A 1 17  ? 27.52421  3.69815   -8.51697  1.000 6.98788  ? 17  LEU A C     1 
ATOM   120  O  O     . LEU A 1 17  ? 28.43525  4.52811   -8.60996  1.000 6.27076  ? 17  LEU A O     1 
ATOM   121  C  CB    . LEU A 1 17  ? 26.11725  4.32118   -6.55795  1.000 10.21571 ? 17  LEU A CB    1 
ATOM   122  C  CG    . LEU A 1 17  ? 25.39432  5.56320   -6.02292  1.000 10.01034 ? 17  LEU A CG    1 
ATOM   123  C  CD1   . LEU A 1 17  ? 23.89430  5.33928   -5.95492  1.000 10.22603 ? 17  LEU A CD1   1 
ATOM   124  C  CD2   . LEU A 1 17  ? 25.94234  5.98614   -4.66891  1.000 11.73278 ? 17  LEU A CD2   1 
ATOM   125  N  N     . HIS A 1 18  ? 27.70314  2.40615   -8.78900  1.000 6.81139  ? 18  HIS A N     1 
ATOM   126  C  CA    . HIS A 1 18  ? 28.98912  1.87810   -9.22502  1.000 6.30573  ? 18  HIS A CA    1 
ATOM   127  C  C     . HIS A 1 18  ? 29.13512  2.04412   -10.73002 1.000 6.12654  ? 18  HIS A C     1 
ATOM   128  O  O     . HIS A 1 18  ? 28.17611  1.85219   -11.48102 1.000 9.08000  ? 18  HIS A O     1 
ATOM   129  C  CB    . HIS A 1 18  ? 29.13204  0.40108   -8.85106  1.000 8.29500  ? 18  HIS A CB    1 
ATOM   130  C  CG    . HIS A 1 18  ? 28.25399  -0.51586  -9.64707  1.000 6.85250  ? 18  HIS A CG    1 
ATOM   131  N  ND1   . HIS A 1 18  ? 26.95398  -0.80080  -9.28808  1.000 6.65826  ? 18  HIS A ND1   1 
ATOM   132  C  CD2   . HIS A 1 18  ? 28.49195  -1.21684  -10.78209 1.000 6.56684  ? 18  HIS A CD2   1 
ATOM   133  C  CE1   . HIS A 1 18  ? 26.42893  -1.63575  -10.16609 1.000 8.04321  ? 18  HIS A CE1   1 
ATOM   134  N  NE2   . HIS A 1 18  ? 27.34192  -1.90478  -11.08210 1.000 7.21559  ? 18  HIS A NE2   1 
ATOM   135  N  N     . ASP A 1 19  ? 30.34613  2.39507   -11.16001 1.000 8.89320  ? 19  ASP A N     1 
ATOM   136  C  CA    . ASP A 1 19  ? 30.65914  2.63209   -12.56801 1.000 8.08103  ? 19  ASP A CA    1 
ATOM   137  C  C     . ASP A 1 19  ? 29.63519  3.58016   -13.19598 1.000 7.80534  ? 19  ASP A C     1 
ATOM   138  O  O     . ASP A 1 19  ? 28.92717  3.24722   -14.14999 1.000 7.92541  ? 19  ASP A O     1 
ATOM   139  C  CB    . ASP A 1 19  ? 30.74407  1.31010   -13.33904 1.000 7.57351  ? 19  ASP A CB    1 
ATOM   140  C  CG    . ASP A 1 19  ? 31.24907  1.49111   -14.76104 1.000 7.09386  ? 19  ASP A CG    1 
ATOM   141  O  OD1   . ASP A 1 19  ? 31.92613  2.50408   -15.03102 1.000 7.41153  ? 19  ASP A OD1   1 
ATOM   142  O  OD2   . ASP A 1 19  ? 30.95703  0.62615   -15.61206 1.000 6.18891  ? 19  ASP A OD2   1 
ATOM   143  N  N     . ASN A 1 20  ? 29.55525  4.77815   -12.61995 1.000 7.33841  ? 20  ASN A N     1 
ATOM   144  C  CA    . ASN A 1 20  ? 28.64530  5.82720   -13.07993 1.000 6.51230  ? 20  ASN A CA    1 
ATOM   145  C  C     . ASN A 1 20  ? 29.46136  7.09117   -13.31390 1.000 6.34540  ? 20  ASN A C     1 
ATOM   146  O  O     . ASN A 1 20  ? 29.48041  7.99415   -12.46588 1.000 6.01272  ? 20  ASN A O     1 
ATOM   147  C  CB    . ASN A 1 20  ? 27.52532  6.07224   -12.06792 1.000 6.81160  ? 20  ASN A CB    1 
ATOM   148  C  CG    . ASN A 1 20  ? 26.36135  6.84131   -12.65989 1.000 7.53782  ? 20  ASN A CG    1 
ATOM   149  O  OD1   . ASN A 1 20  ? 26.52839  7.62832   -13.59387 1.000 6.12293  ? 20  ASN A OD1   1 
ATOM   150  N  ND2   . ASN A 1 20  ? 25.16934  6.61336   -12.11989 1.000 6.50404  ? 20  ASN A ND2   1 
ATOM   151  N  N     . PRO A 1 21  ? 30.14836  7.19216   -14.45690 1.000 5.97303  ? 21  PRO A N     1 
ATOM   152  C  CA    . PRO A 1 21  ? 30.95342  8.39613   -14.71487 1.000 6.58279  ? 21  PRO A CA    1 
ATOM   153  C  C     . PRO A 1 21  ? 30.12849  9.66517   -14.80184 1.000 6.12418  ? 21  PRO A C     1 
ATOM   154  O  O     . PRO A 1 21  ? 30.66054  10.75414  -14.54982 1.000 6.24310  ? 21  PRO A O     1 
ATOM   155  C  CB    . PRO A 1 21  ? 31.64840  8.07712   -16.04688 1.000 10.07956 ? 21  PRO A CB    1 
ATOM   156  C  CG    . PRO A 1 21  ? 30.77135  7.05818   -16.69690 1.000 8.19337  ? 21  PRO A CG    1 
ATOM   157  C  CD    . PRO A 1 21  ? 30.22731  6.22818   -15.56792 1.000 9.48775  ? 21  PRO A CD    1 
ATOM   158  N  N     . ALA A 1 22  ? 28.84348  9.56524   -15.15484 1.000 7.74282  ? 22  ALA A N     1 
ATOM   159  C  CA    . ALA A 1 22  ? 27.99554  10.75229  -15.14581 1.000 6.05070  ? 22  ALA A CA    1 
ATOM   160  C  C     . ALA A 1 22  ? 27.80657  11.27326  -13.72979 1.000 6.33515  ? 22  ALA A C     1 
ATOM   161  O  O     . ALA A 1 22  ? 27.75364  12.48826  -13.50776 1.000 10.25945 ? 22  ALA A O     1 
ATOM   162  C  CB    . ALA A 1 22  ? 26.64352  10.44737  -15.79181 1.000 8.24337  ? 22  ALA A CB    1 
ATOM   163  N  N     . LEU A 1 23  ? 27.70753  10.36524  -12.75581 1.000 9.80522  ? 23  LEU A N     1 
ATOM   164  C  CA    . LEU A 1 23  ? 27.60556  10.77422  -11.35880 1.000 8.51070  ? 23  LEU A CA    1 
ATOM   165  C  C     . LEU A 1 23  ? 28.92759  11.33414  -10.84480 1.000 7.80250  ? 23  LEU A C     1 
ATOM   166  O  O     . LEU A 1 23  ? 28.93864  12.30012  -10.07477 1.000 8.54639  ? 23  LEU A O     1 
ATOM   167  C  CB    . LEU A 1 23  ? 27.15150  9.58922   -10.50583 1.000 7.49684  ? 23  LEU A CB    1 
ATOM   168  C  CG    . LEU A 1 23  ? 27.14952  9.78218   -8.98983  1.000 12.58302 ? 23  LEU A CG    1 
ATOM   169  C  CD1   . LEU A 1 23  ? 26.25658  10.94922  -8.59380  1.000 12.47485 ? 23  LEU A CD1   1 
ATOM   170  C  CD2   . LEU A 1 23  ? 26.70346  8.50419   -8.29885  1.000 8.36862  ? 23  LEU A CD2   1 
ATOM   171  N  N     . LEU A 1 24  ? 30.04956  10.73909  -11.25482 1.000 7.71720  ? 24  LEU A N     1 
ATOM   172  C  CA    . LEU A 1 24  ? 31.35058  11.20401  -10.78381 1.000 8.49551  ? 24  LEU A CA    1 
ATOM   173  C  C     . LEU A 1 24  ? 31.63965  12.62401  -11.25478 1.000 10.12892 ? 24  LEU A C     1 
ATOM   174  O  O     . LEU A 1 24  ? 32.13970  13.44997  -10.48076 1.000 11.92372 ? 24  LEU A O     1 
ATOM   175  C  CB    . LEU A 1 24  ? 32.44553  10.24697  -11.25084 1.000 10.03479 ? 24  LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 24  ? 32.25646  8.77997   -10.86187 1.000 7.76803  ? 24  LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 24  ? 33.40341  7.93792   -11.38889 1.000 10.79136 ? 24  LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 24  ? 32.12346  8.63094   -9.35587  1.000 12.09344 ? 24  LEU A CD2   1 
ATOM   179  N  N     . GLU A 1 25  ? 31.33866  12.92705  -12.52077 1.000 9.07346  ? 25  GLU A N     1 
ATOM   180  C  CA    . GLU A 1 25  ? 31.57473  14.27605  -13.02574 1.000 10.45773 ? 25  GLU A CA    1 
ATOM   181  C  C     . GLU A 1 25  ? 30.64678  15.28409  -12.35671 1.000 11.08869 ? 25  GLU A C     1 
ATOM   182  O  O     . GLU A 1 25  ? 31.04184  16.42806  -12.09868 1.000 6.76208  ? 25  GLU A O     1 
ATOM   183  C  CB    . GLU A 1 25  ? 31.39072  14.30510  -14.54574 1.000 10.32461 ? 25  GLU A CB    1 
ATOM   184  C  CG    . GLU A 1 25  ? 31.39079  15.70811  -15.16070 1.000 12.70660 ? 25  GLU A CG    1 
ATOM   185  C  CD    . GLU A 1 25  ? 32.76583  16.35304  -15.16969 1.000 15.10063 ? 25  GLU A CD    1 
ATOM   186  O  OE1   . GLU A 1 25  ? 33.76479  15.62300  -15.33571 1.000 12.67158 ? 25  GLU A OE1   1 
ATOM   187  O  OE2   . GLU A 1 25  ? 32.84489  17.59204  -15.01166 1.000 16.98218 ? 25  GLU A OE2   1 
ATOM   188  N  N     . ALA A 1 26  ? 29.40576  14.86814  -12.06572 1.000 11.65161 ? 26  ALA A N     1 
ATOM   189  C  CA    . ALA A 1 26  ? 28.43781  15.75118  -11.42369 1.000 9.11006  ? 26  ALA A CA    1 
ATOM   190  C  C     . ALA A 1 26  ? 28.85383  16.11212  -10.00568 1.000 10.04703 ? 26  ALA A C     1 
ATOM   191  O  O     . ALA A 1 26  ? 28.53589  17.20713  -9.53066  1.000 8.32700  ? 26  ALA A O     1 
ATOM   192  C  CB    . ALA A 1 26  ? 27.05378  15.09625  -11.42270 1.000 10.26141 ? 26  ALA A CB    1 
ATOM   193  N  N     . CYS A 1 27  ? 29.55879  15.21807  -9.31671  1.000 8.09458  ? 27  CYS A N     1 
ATOM   194  C  CA    . CYS A 1 27  ? 29.97581  15.47802  -7.94570  1.000 13.17163 ? 27  CYS A CA    1 
ATOM   195  C  C     . CYS A 1 27  ? 31.31085  16.19895  -7.85269  1.000 11.44759 ? 27  CYS A C     1 
ATOM   196  O  O     . CYS A 1 27  ? 31.61288  16.77691  -6.80468  1.000 13.64664 ? 27  CYS A O     1 
ATOM   197  C  CB    . CYS A 1 27  ? 30.06475  14.16799  -7.15673  1.000 11.54690 ? 27  CYS A CB    1 
ATOM   198  S  SG    . CYS A 1 27  ? 28.48570  13.33107  -6.93775  1.000 15.77112 ? 27  CYS A SG    1 
ATOM   199  N  N     . LYS A 1 28  ? 32.10584  16.18393  -8.91669  1.000 11.69781 ? 28  LYS A N     1 
ATOM   200  C  CA    . LYS A 1 28  ? 33.45587  16.72586  -8.85569  1.000 15.58447 ? 28  LYS A CA    1 
ATOM   201  C  C     . LYS A 1 28  ? 33.40895  18.24586  -8.76065  1.000 13.23638 ? 28  LYS A C     1 
ATOM   202  O  O     . LYS A 1 28  ? 32.82298  18.91191  -9.62063  1.000 12.42347 ? 28  LYS A O     1 
ATOM   203  C  CB    . LYS A 1 28  ? 34.25084  16.27285  -10.07670 1.000 14.65005 ? 28  LYS A CB    1 
ATOM   204  C  CG    . LYS A 1 28  ? 35.72686  16.61877  -10.04570 1.000 18.23169 ? 28  LYS A CG    1 
ATOM   205  C  CD    . LYS A 1 28  ? 36.43882  16.01077  -11.24872 0.000 17.13363 ? 28  LYS A CD    1 
ATOM   206  C  CE    . LYS A 1 28  ? 37.86185  16.52970  -11.38171 0.000 18.17510 ? 28  LYS A CE    1 
ATOM   207  N  NZ    . LYS A 1 28  ? 38.47782  16.12170  -12.67672 0.000 18.18892 ? 28  LYS A NZ    1 
ATOM   208  N  N     . ASP A 1 29  ? 34.01598  18.78681  -7.70164  1.000 12.31840 ? 29  ASP A N     1 
ATOM   209  C  CA    . ASP A 1 29  ? 34.08005  20.22880  -7.46461  1.000 14.82375 ? 29  ASP A CA    1 
ATOM   210  C  C     . ASP A 1 29  ? 32.69208  20.85486  -7.35759  1.000 14.25902 ? 29  ASP A C     1 
ATOM   211  O  O     . ASP A 1 29  ? 32.51414  22.03788  -7.66056  1.000 17.57620 ? 29  ASP A O     1 
ATOM   212  C  CB    . ASP A 1 29  ? 34.89808  20.93078  -8.55459  1.000 16.97544 ? 29  ASP A CB    1 
ATOM   213  C  CG    . ASP A 1 29  ? 36.30505  20.38571  -8.66661  1.000 18.72214 ? 29  ASP A CG    1 
ATOM   214  O  OD1   . ASP A 1 29  ? 36.94005  20.17066  -7.61462  1.000 16.80437 ? 29  ASP A OD1   1 
ATOM   215  O  OD2   . ASP A 1 29  ? 36.77404  20.16472  -9.80362  1.000 20.78955 ? 29  ASP A OD2   1 
ATOM   216  N  N     . ALA A 1 30  ? 31.72505  20.06990  -6.87660  1.000 9.95568  ? 30  ALA A N     1 
ATOM   217  C  CA    . ALA A 1 30  ? 30.32407  20.52497  -6.80259  1.000 11.86406 ? 30  ALA A CA    1 
ATOM   218  C  C     . ALA A 1 30  ? 29.92409  20.91796  -5.37157  1.000 12.12044 ? 30  ALA A C     1 
ATOM   219  O  O     . ALA A 1 30  ? 30.24506  20.17792  -4.44959  1.000 7.96053  ? 30  ALA A O     1 
ATOM   220  C  CB    . ALA A 1 30  ? 29.44701  19.41703  -7.31661  1.000 13.37832 ? 30  ALA A CB    1 
ATOM   221  N  N     . LYS A 1 31  ? 29.24415  22.05899  -5.24754  1.000 11.95689 ? 31  LYS A N     1 
ATOM   222  C  CA    . LYS A 1 31  ? 28.76218  22.51898  -3.93053  1.000 15.18393 ? 31  LYS A CA    1 
ATOM   223  C  C     . LYS A 1 31  ? 27.43615  21.80104  -3.64754  1.000 15.39226 ? 31  LYS A C     1 
ATOM   224  O  O     . LYS A 1 31  ? 27.19113  21.44903  -2.50555  1.000 13.09578 ? 31  LYS A O     1 
ATOM   225  C  CB    . LYS A 1 31  ? 28.58426  24.03599  -3.90350  1.000 18.78131 ? 31  LYS A CB    1 
ATOM   226  C  CG    . LYS A 1 31  ? 28.29429  24.63497  -2.53748  1.000 24.61062 ? 31  LYS A CG    1 
ATOM   227  C  CD    . LYS A 1 31  ? 29.23827  24.14790  -1.46450  1.000 23.46354 ? 31  LYS A CD    1 
ATOM   228  C  CE    . LYS A 1 31  ? 29.65833  25.25486  -0.52447  1.000 26.71879 ? 31  LYS A CE    1 
ATOM   229  N  NZ    . LYS A 1 31  ? 29.87339  26.53086  -1.24544  0.000 26.02984 ? 31  LYS A NZ    1 
ATOM   230  N  N     . HIS A 1 32  ? 26.60814  21.69011  -4.67954  1.000 15.11517 ? 32  HIS A N     1 
ATOM   231  C  CA    . HIS A 1 32  ? 25.30010  20.99417  -4.53255  1.000 13.44935 ? 32  HIS A CA    1 
ATOM   232  C  C     . HIS A 1 32  ? 25.07805  20.02221  -5.70358  1.000 11.65784 ? 32  HIS A C     1 
ATOM   233  O  O     . HIS A 1 32  ? 25.41306  20.37422  -6.83257  1.000 10.24752 ? 32  HIS A O     1 
ATOM   234  C  CB    . HIS A 1 32  ? 24.16415  22.00322  -4.33553  1.000 12.75149 ? 32  HIS A CB    1 
ATOM   235  C  CG    . HIS A 1 32  ? 24.21420  22.85719  -3.12451  1.000 13.68990 ? 32  HIS A CG    1 
ATOM   236  N  ND1   . HIS A 1 32  ? 24.70627  24.14117  -3.15648  1.000 19.17939 ? 32  HIS A ND1   1 
ATOM   237  C  CD2   . HIS A 1 32  ? 23.81020  22.64618  -1.87551  1.000 13.64586 ? 32  HIS A CD2   1 
ATOM   238  C  CE1   . HIS A 1 32  ? 24.60930  24.66915  -1.95047  1.000 14.18765 ? 32  HIS A CE1   1 
ATOM   239  N  NE2   . HIS A 1 32  ? 24.07226  23.77915  -1.15848  1.000 13.01529 ? 32  HIS A NE2   1 
ATOM   240  N  N     . VAL A 1 33  ? 24.55099  18.83023  -5.41360  1.000 10.81221 ? 33  VAL A N     1 
ATOM   241  C  CA    . VAL A 1 33  ? 24.23493  17.83327  -6.43062  1.000 11.10385 ? 33  VAL A CA    1 
ATOM   242  C  C     . VAL A 1 33  ? 22.77292  17.43834  -6.26863  1.000 7.96320  ? 33  VAL A C     1 
ATOM   243  O  O     . VAL A 1 33  ? 22.34290  17.06734  -5.17064  1.000 9.86590  ? 33  VAL A O     1 
ATOM   244  C  CB    . VAL A 1 33  ? 25.15087  16.59922  -6.32866  1.000 10.49789 ? 33  VAL A CB    1 
ATOM   245  C  CG1   . VAL A 1 33  ? 24.71981  15.52927  -7.32368  1.000 8.44826  ? 33  VAL A CG1   1 
ATOM   246  C  CG2   . VAL A 1 33  ? 26.60189  16.99115  -6.56365  1.000 10.61703 ? 33  VAL A CG2   1 
ATOM   247  N  N     . TYR A 1 34  ? 22.01392  17.52540  -7.36062  1.000 6.51127  ? 34  TYR A N     1 
ATOM   248  C  CA    . TYR A 1 34  ? 20.59790  17.17248  -7.35863  1.000 7.35168  ? 34  TYR A CA    1 
ATOM   249  C  C     . TYR A 1 34  ? 20.39283  15.88051  -8.14166  1.000 8.08008  ? 34  TYR A C     1 
ATOM   250  O  O     . TYR A 1 34  ? 20.29283  15.91054  -9.37765  1.000 8.18275  ? 34  TYR A O     1 
ATOM   251  C  CB    . TYR A 1 34  ? 19.75895  18.30453  -7.95860  1.000 8.68378  ? 34  TYR A CB    1 
ATOM   252  C  CG    . TYR A 1 34  ? 19.83902  19.61951  -7.20557  1.000 8.82840  ? 34  TYR A CG    1 
ATOM   253  C  CD1   . TYR A 1 34  ? 20.87007  20.52046  -7.44655  1.000 9.48794  ? 34  TYR A CD1   1 
ATOM   254  C  CD2   . TYR A 1 34  ? 18.87604  19.96554  -6.26655  1.000 10.53542 ? 34  TYR A CD2   1 
ATOM   255  C  CE1   . TYR A 1 34  ? 20.94213  21.72544  -6.76752  1.000 11.40217 ? 34  TYR A CE1   1 
ATOM   256  C  CE2   . TYR A 1 34  ? 18.94211  21.16752  -5.58053  1.000 13.40357 ? 34  TYR A CE2   1 
ATOM   257  C  CZ    . TYR A 1 34  ? 19.97615  22.04347  -5.83551  1.000 11.63055 ? 34  TYR A CZ    1 
ATOM   258  O  OH    . TYR A 1 34  ? 20.04221  23.23845  -5.15548  1.000 15.44777 ? 34  TYR A OH    1 
ATOM   259  N  N     . PRO A 1 35  ? 20.34177  14.72049  -7.47968  1.000 7.65884  ? 35  PRO A N     1 
ATOM   260  C  CA    . PRO A 1 35  ? 20.07771  13.45652  -8.18571  1.000 7.32094  ? 35  PRO A CA    1 
ATOM   261  C  C     . PRO A 1 35  ? 18.59770  13.35660  -8.52971  1.000 8.02766  ? 35  PRO A C     1 
ATOM   262  O  O     . PRO A 1 35  ? 17.74370  13.35063  -7.64071  1.000 9.44473  ? 35  PRO A O     1 
ATOM   263  C  CB    . PRO A 1 35  ? 20.49566  12.38448  -7.16874  1.000 5.95930  ? 35  PRO A CB    1 
ATOM   264  C  CG    . PRO A 1 35  ? 21.25170  13.12241  -6.08872  1.000 7.66861  ? 35  PRO A CG    1 
ATOM   265  C  CD    . PRO A 1 35  ? 20.66077  14.49444  -6.06269  1.000 7.19198  ? 35  PRO A CD    1 
ATOM   266  N  N     . VAL A 1 36  ? 18.29469  13.27465  -9.82471  1.000 6.01854  ? 36  VAL A N     1 
ATOM   267  C  CA    . VAL A 1 36  ? 16.93470  13.43073  -10.32370 1.000 10.00773 ? 36  VAL A CA    1 
ATOM   268  C  C     . VAL A 1 36  ? 16.56563  12.23577  -11.18873 1.000 9.04719  ? 36  VAL A C     1 
ATOM   269  O  O     . VAL A 1 36  ? 17.34161  11.83175  -12.06174 1.000 10.17979 ? 36  VAL A O     1 
ATOM   270  C  CB    . VAL A 1 36  ? 16.77576  14.73276  -11.13267 1.000 10.79291 ? 36  VAL A CB    1 
ATOM   271  C  CG1   . VAL A 1 36  ? 15.46376  14.72484  -11.90366 1.000 14.11539 ? 36  VAL A CG1   1 
ATOM   272  C  CG2   . VAL A 1 36  ? 16.85682  15.94073  -10.21964 1.000 8.30147  ? 36  VAL A CG2   1 
ATOM   273  N  N     . PHE A 1 37  ? 15.38261  11.67682  -10.94174 1.000 9.11925  ? 37  PHE A N     1 
ATOM   274  C  CA    . PHE A 1 37  ? 14.69856  10.78688  -11.87075 1.000 8.41467  ? 37  PHE A CA    1 
ATOM   275  C  C     . PHE A 1 37  ? 13.35159  11.40996  -12.19873 1.000 12.37093 ? 37  PHE A C     1 
ATOM   276  O  O     . PHE A 1 37  ? 12.58861  11.75297  -11.28772 1.000 9.47447  ? 37  PHE A O     1 
ATOM   277  C  CB    . PHE A 1 37  ? 14.50349  9.38488   -11.28579 1.000 9.42085  ? 37  PHE A CB    1 
ATOM   278  C  CG    . PHE A 1 37  ? 13.88243  8.40593   -12.24781 1.000 10.99860 ? 37  PHE A CG    1 
ATOM   279  C  CD1   . PHE A 1 37  ? 12.50743  8.31200   -12.37680 1.000 12.36268 ? 37  PHE A CD1   1 
ATOM   280  C  CD2   . PHE A 1 37  ? 14.67839  7.57191   -13.01483 1.000 8.82623  ? 37  PHE A CD2   1 
ATOM   281  C  CE1   . PHE A 1 37  ? 11.94538  7.41505   -13.25582 1.000 12.77160 ? 37  PHE A CE1   1 
ATOM   282  C  CE2   . PHE A 1 37  ? 14.12034  6.67196   -13.89385 1.000 9.68404  ? 37  PHE A CE2   1 
ATOM   283  C  CZ    . PHE A 1 37  ? 12.75434  6.59203   -14.01385 1.000 13.52745 ? 37  PHE A CZ    1 
ATOM   284  N  N     . VAL A 1 38  ? 13.06059  11.55800  -13.48673 1.000 10.50277 ? 38  VAL A N     1 
ATOM   285  C  CA    . VAL A 1 38  ? 11.84462  12.22407  -13.93271 1.000 11.68868 ? 38  VAL A CA    1 
ATOM   286  C  C     . VAL A 1 38  ? 10.76657  11.17413  -14.14773 1.000 14.71738 ? 38  VAL A C     1 
ATOM   287  O  O     . VAL A 1 38  ? 10.95552  10.22214  -14.91375 1.000 13.64587 ? 38  VAL A O     1 
ATOM   288  C  CB    . VAL A 1 38  ? 12.08966  13.03709  -15.21069 1.000 13.76695 ? 38  VAL A CB    1 
ATOM   289  C  CG1   . VAL A 1 38  ? 10.76968  13.57317  -15.75767 1.000 13.29440 ? 38  VAL A CG1   1 
ATOM   290  C  CG2   . VAL A 1 38  ? 13.04772  14.17904  -14.93767 1.000 10.92438 ? 38  VAL A CG2   1 
ATOM   291  N  N     . LEU A 1 39  ? 9.63658   11.34818  -13.47572 1.000 12.79306 ? 39  LEU A N     1 
ATOM   292  C  CA    . LEU A 1 39  ? 8.52653   10.41223  -13.54074 1.000 16.99943 ? 39  LEU A CA    1 
ATOM   293  C  C     . LEU A 1 39  ? 7.31856   11.08231  -14.18072 1.000 22.01167 ? 39  LEU A C     1 
ATOM   294  O  O     . LEU A 1 39  ? 7.00762   12.24232  -13.88169 1.000 21.69389 ? 39  LEU A O     1 
ATOM   295  C  CB    . LEU A 1 39  ? 8.16151   9.91122   -12.14075 1.000 23.06352 ? 39  LEU A CB    1 
ATOM   296  C  CG    . LEU A 1 39  ? 7.28345   8.66426   -12.03777 1.000 24.58246 ? 39  LEU A CG    1 
ATOM   297  C  CD1   . LEU A 1 39  ? 8.10838   7.40522   -12.25981 1.000 26.22706 ? 39  LEU A CD1   1 
ATOM   298  C  CD2   . LEU A 1 39  ? 6.57745   8.62026   -10.69477 1.000 17.33448 ? 39  LEU A CD2   1 
ATOM   299  N  N     . ASP A 1 40  ? 6.64152   10.35036  -15.06573 1.000 27.12470 ? 40  ASP A N     1 
ATOM   300  C  CA    A ASP A 1 40  ? 5.43455   10.86044  -15.69372 0.291 28.61070 ? 40  ASP A CA    1 
ATOM   301  C  CA    B ASP A 1 40  ? 5.43355   10.86044  -15.69872 0.709 28.60476 ? 40  ASP A CA    1 
ATOM   302  C  C     . ASP A 1 40  ? 4.22952   10.21449  -15.03773 1.000 31.88791 ? 40  ASP A C     1 
ATOM   303  O  O     . ASP A 1 40  ? 3.98145   9.01850   -15.26275 1.000 32.41776 ? 40  ASP A O     1 
ATOM   304  C  CB    A ASP A 1 40  ? 5.44453   10.57847  -17.19272 0.291 30.71252 ? 40  ASP A CB    1 
ATOM   305  C  CB    B ASP A 1 40  ? 5.44252   10.56848  -17.19772 0.709 30.76117 ? 40  ASP A CB    1 
ATOM   306  C  CG    A ASP A 1 40  ? 4.45657   11.44054  -17.95470 0.291 30.44634 ? 40  ASP A CG    1 
ATOM   307  C  CG    B ASP A 1 40  ? 6.76254   10.92842  -17.85772 0.709 26.92555 ? 40  ASP A CG    1 
ATOM   308  O  OD1   A ASP A 1 40  ? 4.71463   12.65253  -18.11967 0.291 27.81332 ? 40  ASP A OD1   1 
ATOM   309  O  OD1   B ASP A 1 40  ? 7.76255   11.10136  -17.13672 0.709 25.59760 ? 40  ASP A OD1   1 
ATOM   310  O  OD2   A ASP A 1 40  ? 3.41754   10.90061  -18.37971 0.291 34.36046 ? 40  ASP A OD2   1 
ATOM   311  O  OD2   B ASP A 1 40  ? 6.79854   11.04145  -19.10172 0.709 31.28690 ? 40  ASP A OD2   1 
ATOM   312  N  N     . PRO A 1 41  ? 3.45355   10.93851  -14.22871 1.000 34.44539 ? 41  PRO A N     1 
ATOM   313  C  CA    . PRO A 1 41  ? 2.31153   10.31555  -13.54872 1.000 33.74809 ? 41  PRO A CA    1 
ATOM   314  C  C     . PRO A 1 41  ? 1.12251   10.04963  -14.45472 1.000 40.31498 ? 41  PRO A C     1 
ATOM   315  O  O     . PRO A 1 41  ? 0.20647   9.32667   -14.04173 1.000 47.70816 ? 41  PRO A O     1 
ATOM   316  C  CB    . PRO A 1 41  ? 1.96058   11.33754  -12.46169 1.000 41.31712 ? 41  PRO A CB    1 
ATOM   317  C  CG    . PRO A 1 41  ? 2.35165   12.63753  -13.05466 1.000 33.23390 ? 41  PRO A CG    1 
ATOM   318  C  CD    . PRO A 1 41  ? 3.58663   12.36449  -13.88367 1.000 30.35821 ? 41  PRO A CD    1 
ATOM   319  N  N     . HIS A 1 42  ? 1.10153   10.59766  -15.66870 1.000 38.12303 ? 42  HIS A N     1 
ATOM   320  C  CA    . HIS A 1 42  ? 0.05151   10.30573  -16.63471 1.000 41.94345 ? 42  HIS A CA    1 
ATOM   321  C  C     . HIS A 1 42  ? 0.48446   9.25774   -17.65173 1.000 40.78696 ? 42  HIS A C     1 
ATOM   322  O  O     . HIS A 1 42  ? -0.21956  9.02780   -18.64774 1.000 42.63285 ? 42  HIS A O     1 
ATOM   323  C  CB    . HIS A 1 42  ? -0.39142  11.59677  -17.32568 1.000 41.39645 ? 42  HIS A CB    1 
ATOM   324  C  CG    . HIS A 1 42  ? -0.70336  12.70477  -16.36365 1.000 40.40182 ? 42  HIS A CG    1 
ATOM   325  N  ND1   . HIS A 1 42  ? -1.90836  12.80281  -15.70064 1.000 41.85636 ? 42  HIS A ND1   1 
ATOM   326  C  CD2   . HIS A 1 42  ? 0.04569   13.74672  -15.93163 1.000 37.70622 ? 42  HIS A CD2   1 
ATOM   327  C  CE1   . HIS A 1 42  ? -1.89330  13.86379  -14.91262 1.000 40.11107 ? 42  HIS A CE1   1 
ATOM   328  N  NE2   . HIS A 1 42  ? -0.71827  14.45374  -15.03461 1.000 41.47675 ? 42  HIS A NE2   1 
ATOM   329  N  N     . PHE A 1 43  ? 1.63143   8.62067   -17.40975 1.000 37.98913 ? 43  PHE A N     1 
ATOM   330  C  CA    . PHE A 1 43  ? 2.04636   7.41667   -18.11978 1.000 40.93803 ? 43  PHE A CA    1 
ATOM   331  C  C     . PHE A 1 43  ? 1.01031   6.30172   -18.04681 1.000 39.76426 ? 43  PHE A C     1 
ATOM   332  O  O     . PHE A 1 43  ? 1.09525   5.35173   -18.83083 1.000 42.06389 ? 43  PHE A O     1 
ATOM   333  C  CB    . PHE A 1 43  ? 3.39534   6.97759   -17.53880 1.000 38.93589 ? 43  PHE A CB    1 
ATOM   334  C  CG    . PHE A 1 43  ? 4.07328   5.86957   -18.28883 1.000 41.52314 ? 43  PHE A CG    1 
ATOM   335  C  CD1   . PHE A 1 43  ? 4.66529   6.10757   -19.51982 1.000 41.34418 ? 43  PHE A CD1   1 
ATOM   336  C  CD2   . PHE A 1 43  ? 4.15822   4.60055   -17.74186 1.000 41.66439 ? 43  PHE A CD2   1 
ATOM   337  C  CE1   . PHE A 1 43  ? 5.29324   5.09255   -20.20485 1.000 42.14089 ? 43  PHE A CE1   1 
ATOM   338  C  CE2   . PHE A 1 43  ? 4.78817   3.57954   -18.42188 1.000 37.62640 ? 43  PHE A CE2   1 
ATOM   339  C  CZ    . PHE A 1 43  ? 5.35617   3.82554   -19.65588 1.000 43.25189 ? 43  PHE A CZ    1 
ATOM   340  N  N     . LEU A 1 44  ? 0.02931   6.40675   -17.15480 1.000 37.77925 ? 44  LEU A N     1 
ATOM   341  C  CA    . LEU A 1 44  ? -1.06673  5.45480   -17.07982 1.000 41.61771 ? 44  LEU A CA    1 
ATOM   342  C  C     . LEU A 1 44  ? -2.23572  5.83888   -17.97280 1.000 46.53980 ? 44  LEU A C     1 
ATOM   343  O  O     . LEU A 1 44  ? -3.23675  5.11593   -17.99982 1.000 48.32325 ? 44  LEU A O     1 
ATOM   344  C  CB    . LEU A 1 44  ? -1.56474  5.31079   -15.63682 1.000 43.75009 ? 44  LEU A CB    1 
ATOM   345  C  CG    . LEU A 1 44  ? -1.17380  4.03476   -14.89285 0.000 38.26638 ? 44  LEU A CG    1 
ATOM   346  C  CD1   . LEU A 1 44  ? -1.83786  2.82180   -15.51788 0.000 35.76067 ? 44  LEU A CD1   1 
ATOM   347  C  CD2   . LEU A 1 44  ? 0.33620   3.87968   -14.89086 0.000 35.30058 ? 44  LEU A CD2   1 
ATOM   348  N  N     . GLN A 1 45  ? -2.13666  6.95689   -18.69378 1.000 46.52399 ? 45  GLN A N     1 
ATOM   349  C  CA    . GLN A 1 45  ? -3.12565  7.31297   -19.70377 1.000 47.27126 ? 45  GLN A CA    1 
ATOM   350  C  C     . GLN A 1 45  ? -2.48566  7.21697   -21.08077 1.000 45.78015 ? 45  GLN A C     1 
ATOM   351  O  O     . GLN A 1 45  ? -2.46961  8.19698   -21.83175 1.000 47.95721 ? 45  GLN A O     1 
ATOM   352  C  CB    . GLN A 1 45  ? -3.67558  8.72299   -19.47073 1.000 46.09361 ? 45  GLN A CB    1 
ATOM   353  C  CG    . GLN A 1 45  ? -4.43356  8.89300   -18.16772 0.000 45.28396 ? 45  GLN A CG    1 
ATOM   354  C  CD    . GLN A 1 45  ? -3.59553  9.53293   -17.08171 0.000 44.28209 ? 45  GLN A CD    1 
ATOM   355  O  OE1   . GLN A 1 45  ? -3.53147  10.75792  -16.97268 0.000 43.63148 ? 45  GLN A OE1   1 
ATOM   356  N  NE2   . GLN A 1 45  ? -2.95057  8.70688   -16.26873 0.000 43.80398 ? 45  GLN A NE2   1 
ATOM   357  N  N     . GLN A 1 46  ? -1.92372  6.05595   -21.40380 1.000 45.88133 ? 46  GLN A N     1 
ATOM   358  C  CA    . GLN A 1 46  ? -1.20073  5.88294   -22.66081 1.000 45.37270 ? 46  GLN A CA    1 
ATOM   359  C  C     . GLN A 1 46  ? -1.72580  4.68599   -23.44883 1.000 44.66296 ? 46  GLN A C     1 
ATOM   360  O  O     . GLN A 1 46  ? -2.64379  4.82005   -24.25983 1.000 52.67861 ? 46  GLN A O     1 
ATOM   361  C  CB    . GLN A 1 46  ? 0.29826   5.72186   -22.39582 0.000 43.82416 ? 46  GLN A CB    1 
ATOM   362  C  CG    . GLN A 1 46  ? 0.73019   4.30183   -22.07885 0.000 42.06404 ? 46  GLN A CG    1 
ATOM   363  C  CD    . GLN A 1 46  ? 1.87416   3.84579   -22.96187 0.000 40.93017 ? 46  GLN A CD    1 
ATOM   364  O  OE1   . GLN A 1 46  ? 2.49011   2.80875   -22.71689 0.000 38.62232 ? 46  GLN A OE1   1 
ATOM   365  N  NE2   . GLN A 1 46  ? 2.16420   4.62280   -24.00085 0.000 41.47266 ? 46  GLN A NE2   1 
ATOM   366  N  N     . LYS A 1 50  ? -0.17213  -2.07014  -21.59500 1.000 24.38519 ? 50  LYS A N     1 
ATOM   367  C  CA    . LYS A 1 50  ? 1.07789   -1.50319  -22.08299 1.000 18.99831 ? 50  LYS A CA    1 
ATOM   368  C  C     . LYS A 1 50  ? 2.24088   -1.86727  -21.16600 1.000 25.97180 ? 50  LYS A C     1 
ATOM   369  O  O     . LYS A 1 50  ? 3.27685   -2.35031  -21.62402 1.000 22.35233 ? 50  LYS A O     1 
ATOM   370  C  CB    . LYS A 1 50  ? 0.96197   0.01782   -22.20895 1.000 23.92077 ? 50  LYS A CB    1 
ATOM   371  N  N     . VAL A 1 51  ? 2.06590   -1.63029  -19.86800 1.000 23.61565 ? 51  VAL A N     1 
ATOM   372  C  CA    . VAL A 1 51  ? 3.10389   -1.87237  -18.87201 1.000 17.36790 ? 51  VAL A CA    1 
ATOM   373  C  C     . VAL A 1 51  ? 2.50285   -2.69436  -17.74302 1.000 16.77155 ? 51  VAL A C     1 
ATOM   374  O  O     . VAL A 1 51  ? 1.49187   -2.29733  -17.15101 1.000 22.74784 ? 51  VAL A O     1 
ATOM   375  C  CB    . VAL A 1 51  ? 3.69596   -0.56441  -18.32298 1.000 22.30175 ? 51  VAL A CB    1 
ATOM   376  C  CG1   . VAL A 1 51  ? 4.84795   -0.86249  -17.37499 1.000 16.26642 ? 51  VAL A CG1   1 
ATOM   377  C  CG2   . VAL A 1 51  ? 4.14900   0.33759   -19.46196 1.000 29.90089 ? 51  VAL A CG2   1 
ATOM   378  N  N     . SER A 1 52  ? 3.11879   -3.83440  -17.44305 1.000 14.29568 ? 52  SER A N     1 
ATOM   379  C  CA    A SER A 1 52  ? 2.67276   -4.64741  -16.32507 0.605 13.28348 ? 52  SER A CA    1 
ATOM   380  C  CA    B SER A 1 52  ? 2.67176   -4.64641  -16.32607 0.395 13.17654 ? 52  SER A CA    1 
ATOM   381  C  C     . SER A 1 52  ? 3.17079   -4.06346  -15.00806 1.000 11.28021 ? 52  SER A C     1 
ATOM   382  O  O     . SER A 1 52  ? 4.15583   -3.31851  -14.95905 1.000 11.24328 ? 52  SER A O     1 
ATOM   383  C  CB    A SER A 1 52  ? 3.15868   -6.08843  -16.46811 0.605 10.46839 ? 52  SER A CB    1 
ATOM   384  C  CB    B SER A 1 52  ? 3.15968   -6.08643  -16.47011 0.395 10.69748 ? 52  SER A CB    1 
ATOM   385  O  OG    A SER A 1 52  ? 2.82665   -6.85444  -15.32212 0.605 11.12082 ? 52  SER A OG    1 
ATOM   386  O  OG    B SER A 1 52  ? 4.57468   -6.14450  -16.41511 0.395 10.11782 ? 52  SER A OG    1 
ATOM   387  N  N     . VAL A 1 53  ? 2.47378   -4.41645  -13.92606 1.000 11.59469 ? 53  VAL A N     1 
ATOM   388  C  CA    . VAL A 1 53  ? 2.90681   -3.96850  -12.61206 1.000 10.78899 ? 53  VAL A CA    1 
ATOM   389  C  C     . VAL A 1 53  ? 4.23878   -4.60158  -12.22608 1.000 10.54763 ? 53  VAL A C     1 
ATOM   390  O  O     . VAL A 1 53  ? 4.95481   -4.05664  -11.38007 1.000 8.95322  ? 53  VAL A O     1 
ATOM   391  C  CB    . VAL A 1 53  ? 1.81480   -4.26647  -11.56706 1.000 13.32900 ? 53  VAL A CB    1 
ATOM   392  C  CG1   . VAL A 1 53  ? 1.68272   -5.76547  -11.34109 1.000 11.67660 ? 53  VAL A CG1   1 
ATOM   393  C  CG2   . VAL A 1 53  ? 2.10184   -3.53852  -10.26104 1.000 17.15845 ? 53  VAL A CG2   1 
ATOM   394  N  N     . ASN A 1 54  ? 4.60272   -5.72759  -12.84810 1.000 10.60249 ? 54  ASN A N     1 
ATOM   395  C  CA    . ASN A 1 54  ? 5.85868   -6.39466  -12.51412 1.000 8.68709  ? 54  ASN A CA    1 
ATOM   396  C  C     . ASN A 1 54  ? 7.05773   -5.53171  -12.88711 1.000 8.36621  ? 54  ASN A C     1 
ATOM   397  O  O     . ASN A 1 54  ? 7.97274   -5.33777  -12.07811 1.000 9.49851  ? 54  ASN A O     1 
ATOM   398  C  CB    . ASN A 1 54  ? 5.94361   -7.75164  -13.21616 1.000 8.04728  ? 54  ASN A CB    1 
ATOM   399  C  CG    . ASN A 1 54  ? 5.20256   -8.84662  -12.47318 1.000 9.25050  ? 54  ASN A CG    1 
ATOM   400  O  OD1   . ASN A 1 54  ? 4.78557   -8.66763  -11.32917 1.000 10.02143 ? 54  ASN A OD1   1 
ATOM   401  N  ND2   . ASN A 1 54  ? 5.04950   -9.99760  -13.11921 1.000 8.50152  ? 54  ASN A ND2   1 
ATOM   402  N  N     . ARG A 1 55  ? 7.08025   -5.00991  -14.11591 1.000 8.39768  ? 55  ARG A N     1 
ATOM   403  C  CA    . ARG A 1 55  ? 8.22878   -4.21409  -14.53860 1.000 8.20680  ? 55  ARG A CA    1 
ATOM   404  C  C     . ARG A 1 55  ? 8.23625   -2.84126  -13.87800 1.000 7.89487  ? 55  ARG A C     1 
ATOM   405  O  O     . ARG A 1 55  ? 9.30122   -2.33448  -13.50700 1.000 7.43787  ? 55  ARG A O     1 
ATOM   406  C  CB    . ARG A 1 55  ? 8.25622   -4.06883  -16.06015 1.000 9.91096  ? 55  ARG A CB    1 
ATOM   407  C  CG    . ARG A 1 55  ? 9.39149   -3.17329  -16.54156 1.000 7.19983  ? 55  ARG A CG    1 
ATOM   408  C  CD    . ARG A 1 55  ? 9.63959   -3.28673  -18.03300 1.000 11.41422 ? 55  ARG A CD    1 
ATOM   409  N  NE    . ARG A 1 55  ? 8.68483   -2.52298  -18.82514 1.000 8.91296  ? 55  ARG A NE    1 
ATOM   410  C  CZ    . ARG A 1 55  ? 7.64685   -3.04964  -19.45706 1.000 13.67943 ? 55  ARG A CZ    1 
ATOM   411  N  NH1   . ARG A 1 55  ? 7.39068   -4.34714  -19.40374 1.000 14.32473 ? 55  ARG A NH1   1 
ATOM   412  N  NH2   . ARG A 1 55  ? 6.85274   -2.25619  -20.16903 1.000 11.95365 ? 55  ARG A NH2   1 
ATOM   413  N  N     . TYR A 1 56  ? 7.06589   -2.21569  -13.72603 1.000 9.28659  ? 56  TYR A N     1 
ATOM   414  C  CA    . TYR A 1 56  ? 7.03696   -0.86770  -13.16600 1.000 9.57547  ? 56  TYR A CA    1 
ATOM   415  C  C     . TYR A 1 56  ? 7.43197   -0.87676  -11.69500 1.000 9.77668  ? 56  TYR A C     1 
ATOM   416  O  O     . TYR A 1 56  ? 8.09002   0.05520   -11.21698 1.000 8.63407  ? 56  TYR A O     1 
ATOM   417  C  CB    . TYR A 1 56  ? 5.65499   -0.24063  -13.34698 1.000 9.01583  ? 56  TYR A CB    1 
ATOM   418  C  CG    . TYR A 1 56  ? 5.67907   1.27337   -13.33994 1.000 15.94568 ? 56  TYR A CG    1 
ATOM   419  C  CD1   . TYR A 1 56  ? 5.66211   1.98434   -12.14693 1.000 15.50714 ? 56  TYR A CD1   1 
ATOM   420  C  CD2   . TYR A 1 56  ? 5.73110   1.99140   -14.52793 1.000 14.73804 ? 56  TYR A CD2   1 
ATOM   421  C  CE1   . TYR A 1 56  ? 5.68818   3.36834   -12.13789 1.000 20.10362 ? 56  TYR A CE1   1 
ATOM   422  C  CE2   . TYR A 1 56  ? 5.75717   3.37340   -14.52989 1.000 16.26564 ? 56  TYR A CE2   1 
ATOM   423  C  CZ    . TYR A 1 56  ? 5.73621   4.05737   -13.33288 1.000 23.82004 ? 56  TYR A CZ    1 
ATOM   424  O  OH    . TYR A 1 56  ? 5.76128   5.43437   -13.33684 1.000 26.18701 ? 56  TYR A OH    1 
ATOM   425  N  N     . ASN A 1 57  ? 7.04092   -1.92075  -10.96302 1.000 9.57568  ? 57  ASN A N     1 
ATOM   426  C  CA    . ASN A 1 57  ? 7.47292   -2.03981  -9.57503  1.000 7.94403  ? 57  ASN A CA    1 
ATOM   427  C  C     . ASN A 1 57  ? 8.96490   -2.33389  -9.49104  1.000 9.65349  ? 57  ASN A C     1 
ATOM   428  O  O     . ASN A 1 57  ? 9.64193   -1.87794  -8.56203  1.000 11.80446 ? 57  ASN A O     1 
ATOM   429  C  CB    . ASN A 1 57  ? 6.66087   -3.11778  -8.85905  1.000 12.44594 ? 57  ASN A CB    1 
ATOM   430  C  CG    . ASN A 1 57  ? 6.93787   -3.15983  -7.37205  1.000 14.52305 ? 57  ASN A CG    1 
ATOM   431  O  OD1   . ASN A 1 57  ? 7.50482   -4.12587  -6.86108  1.000 19.85111 ? 57  ASN A OD1   1 
ATOM   432  N  ND2   . ASN A 1 57  ? 6.55493   -2.09783  -6.67003  1.000 15.36925 ? 57  ASN A ND2   1 
ATOM   433  N  N     . PHE A 1 58  ? 9.49486   -3.09189  -10.45706 1.000 8.76379  ? 58  PHE A N     1 
ATOM   434  C  CA    . PHE A 1 58  ? 10.93585  -3.30996  -10.52807 1.000 8.17600  ? 58  PHE A CA    1 
ATOM   435  C  C     . PHE A 1 58  ? 11.67392  -1.98499  -10.67604 1.000 7.09246  ? 58  PHE A C     1 
ATOM   436  O  O     . PHE A 1 58  ? 12.71793  -1.76806  -10.04904 1.000 6.40174  ? 58  PHE A O     1 
ATOM   437  C  CB    . PHE A 1 58  ? 11.26480  -4.24695  -11.69510 1.000 7.41733  ? 58  PHE A CB    1 
ATOM   438  C  CG    . PHE A 1 58  ? 12.63777  -4.85802  -11.62511 1.000 7.01272  ? 58  PHE A CG    1 
ATOM   439  C  CD1   . PHE A 1 58  ? 13.76180  -4.13807  -11.99910 1.000 6.37401  ? 58  PHE A CD1   1 
ATOM   440  C  CD2   . PHE A 1 58  ? 12.79970  -6.16604  -11.20415 1.000 9.71596  ? 58  PHE A CD2   1 
ATOM   441  C  CE1   . PHE A 1 58  ? 15.02477  -4.70913  -11.93612 1.000 6.26308  ? 58  PHE A CE1   1 
ATOM   442  C  CE2   . PHE A 1 58  ? 14.05567  -6.74010  -11.14316 1.000 7.25132  ? 58  PHE A CE2   1 
ATOM   443  C  CZ    . PHE A 1 58  ? 15.16971  -6.01015  -11.51015 1.000 6.34792  ? 58  PHE A CZ    1 
ATOM   444  N  N     . LEU A 1 59  ? 11.13696  -1.08095  -11.49502 1.000 10.22928 ? 59  LEU A N     1 
ATOM   445  C  CA    . LEU A 1 59  ? 11.70903  0.25803   -11.59399 1.000 9.09872  ? 59  LEU A CA    1 
ATOM   446  C  C     . LEU A 1 59  ? 11.58507  1.00600   -10.27297 1.000 6.43240  ? 59  LEU A C     1 
ATOM   447  O  O     . LEU A 1 59  ? 12.51511  1.70894   -9.86196  1.000 6.87235  ? 59  LEU A O     1 
ATOM   448  C  CB    . LEU A 1 59  ? 11.02906  1.03609   -12.71997 1.000 8.21525  ? 59  LEU A CB    1 
ATOM   449  C  CG    . LEU A 1 59  ? 11.34514  2.52907   -12.81494 1.000 6.98626  ? 59  LEU A CG    1 
ATOM   450  C  CD1   . LEU A 1 59  ? 12.81315  2.76001   -13.13694 1.000 6.23321  ? 59  LEU A CD1   1 
ATOM   451  C  CD2   . LEU A 1 59  ? 10.45516  3.18714   -13.85292 1.000 9.97353  ? 59  LEU A CD2   1 
ATOM   452  N  N     . LEU A 1 60  ? 10.44906  0.86004   -9.58597  1.000 7.75470  ? 60  LEU A N     1 
ATOM   453  C  CA    . LEU A 1 60  ? 10.24611  1.58802   -8.33595  1.000 8.67609  ? 60  LEU A CA    1 
ATOM   454  C  C     . LEU A 1 60  ? 11.16408  1.07195   -7.23397  1.000 7.22071  ? 60  LEU A C     1 
ATOM   455  O  O     . LEU A 1 60  ? 11.71213  1.86190   -6.45595  1.000 6.52778  ? 60  LEU A O     1 
ATOM   456  C  CB    . LEU A 1 60  ? 8.78210   1.49809   -7.90695  1.000 6.98173  ? 60  LEU A CB    1 
ATOM   457  C  CG    . LEU A 1 60  ? 7.80314   2.30816   -8.75793  1.000 8.79365  ? 60  LEU A CG    1 
ATOM   458  C  CD1   . LEU A 1 60  ? 6.36613   2.01722   -8.35293  1.000 7.45250  ? 60  LEU A CD1   1 
ATOM   459  C  CD2   . LEU A 1 60  ? 8.10622   3.79714   -8.64489  1.000 7.28154  ? 60  LEU A CD2   1 
ATOM   460  N  N     . GLU A 1 61  ? 11.34002  -0.24906  -7.14600  1.000 8.19968  ? 61  GLU A N     1 
ATOM   461  C  CA    . GLU A 1 61  ? 12.28699  -0.80413  -6.18502  1.000 9.07460  ? 61  GLU A CA    1 
ATOM   462  C  C     . GLU A 1 61  ? 13.71601  -0.40120  -6.51501  1.000 6.55613  ? 61  GLU A C     1 
ATOM   463  O  O     . GLU A 1 61  ? 14.55102  -0.27826  -5.61001  1.000 7.44805  ? 61  GLU A O     1 
ATOM   464  C  CB    . GLU A 1 61  ? 12.16192  -2.32413  -6.14405  1.000 9.05648  ? 61  GLU A CB    1 
ATOM   465  C  CG    . GLU A 1 61  ? 10.82289  -2.80207  -5.63406  1.000 12.63522 ? 61  GLU A CG    1 
ATOM   466  C  CD    . GLU A 1 61  ? 10.71382  -4.30906  -5.62609  1.000 11.96996 ? 61  GLU A CD    1 
ATOM   467  O  OE1   . GLU A 1 61  ? 11.57178  -4.97009  -6.24711  1.000 10.03380 ? 61  GLU A OE1   1 
ATOM   468  O  OE2   . GLU A 1 61  ? 9.76979   -4.83203  -4.99610  1.000 9.19804  ? 61  GLU A OE2   1 
ATOM   469  N  N     . SER A 1 62  ? 14.01502  -0.19518  -7.79801  1.000 7.65234  ? 62  SER A N     1 
ATOM   470  C  CA    . SER A 1 62  ? 15.33804  0.28176   -8.18400  1.000 7.04031  ? 62  SER A CA    1 
ATOM   471  C  C     . SER A 1 62  ? 15.55311  1.71874   -7.73397  1.000 8.28019  ? 62  SER A C     1 
ATOM   472  O  O     . SER A 1 62  ? 16.66813  2.09767   -7.35297  1.000 6.75122  ? 62  SER A O     1 
ATOM   473  C  CB    . SER A 1 62  ? 15.51703  0.16779   -9.69701  1.000 6.00832  ? 62  SER A CB    1 
ATOM   474  O  OG    . SER A 1 62  ? 15.34296  -1.16519  -10.13704 1.000 6.06609  ? 62  SER A OG    1 
ATOM   475  N  N     . LEU A 1 63  ? 14.49816  2.53579   -7.77895  1.000 8.44359  ? 63  LEU A N     1 
ATOM   476  C  CA    . LEU A 1 63  ? 14.60323  3.90978   -7.30192  1.000 8.86720  ? 63  LEU A CA    1 
ATOM   477  C  C     . LEU A 1 63  ? 14.70724  3.95774   -5.78291  1.000 9.71808  ? 63  LEU A C     1 
ATOM   478  O  O     . LEU A 1 63  ? 15.43328  4.79369   -5.23190  1.000 10.63736 ? 63  LEU A O     1 
ATOM   479  C  CB    . LEU A 1 63  ? 13.40427  4.72485   -7.78689  1.000 9.03405  ? 63  LEU A CB    1 
ATOM   480  C  CG    . LEU A 1 63  ? 13.19526  4.81090   -9.30189  1.000 7.85877  ? 63  LEU A CG    1 
ATOM   481  C  CD1   . LEU A 1 63  ? 12.03031  5.73496   -9.62886  1.000 8.94199  ? 63  LEU A CD1   1 
ATOM   482  C  CD2   . LEU A 1 63  ? 14.46328  5.26885   -10.00888 1.000 8.09308  ? 63  LEU A CD2   1 
ATOM   483  N  N     . GLU A 1 64  ? 13.99219  3.06876   -5.08793  1.000 10.94620 ? 64  GLU A N     1 
ATOM   484  C  CA    . GLU A 1 64  ? 14.10620  3.00872   -3.63393  1.000 10.23218 ? 64  GLU A CA    1 
ATOM   485  C  C     . GLU A 1 64  ? 15.51818  2.62464   -3.21195  1.000 10.55802 ? 64  GLU A C     1 
ATOM   486  O  O     . GLU A 1 64  ? 16.03921  3.14559   -2.21894  1.000 9.71729  ? 64  GLU A O     1 
ATOM   487  C  CB    . GLU A 1 64  ? 13.09215  2.01775   -3.06095  1.000 12.21183 ? 64  GLU A CB    1 
ATOM   488  C  CG    . GLU A 1 64  ? 11.64717  2.48383   -3.13294  1.000 15.88664 ? 64  GLU A CG    1 
ATOM   489  C  CD    . GLU A 1 64  ? 10.68112  1.47386   -2.54596  1.000 21.72770 ? 64  GLU A CD    1 
ATOM   490  O  OE1   . GLU A 1 64  ? 11.07809  0.75082   -1.60898  1.000 33.29158 ? 64  GLU A OE1   1 
ATOM   491  O  OE2   . GLU A 1 64  ? 9.53012   1.39493   -3.02396  1.000 31.45162 ? 64  GLU A OE2   1 
ATOM   492  N  N     . ASP A 1 65  ? 16.15013  1.70962   -3.94997  1.000 11.55597 ? 65  ASP A N     1 
ATOM   493  C  CA    . ASP A 1 65  ? 17.52311  1.33054   -3.63499  1.000 10.55488 ? 65  ASP A CA    1 
ATOM   494  C  C     . ASP A 1 65  ? 18.47417  2.50050   -3.84396  1.000 8.68747  ? 65  ASP A C     1 
ATOM   495  O  O     . ASP A 1 65  ? 19.40418  2.70043   -3.05496  1.000 12.39212 ? 65  ASP A O     1 
ATOM   496  C  CB    . ASP A 1 65  ? 17.94505  0.13354   -4.48702  1.000 9.35203  ? 65  ASP A CB    1 
ATOM   497  C  CG    . ASP A 1 65  ? 19.27802  -0.44653  -4.06104  1.000 10.37204 ? 65  ASP A CG    1 
ATOM   498  O  OD1   . ASP A 1 65  ? 19.35199  -1.00956  -2.94805  1.000 13.71339 ? 65  ASP A OD1   1 
ATOM   499  O  OD2   . ASP A 1 65  ? 20.24902  -0.34557  -4.84104  1.000 9.28150  ? 65  ASP A OD2   1 
ATOM   500  N  N     . LEU A 1 66  ? 18.25620  3.28554   -4.90294  1.000 8.62847  ? 66  LEU A N     1 
ATOM   501  C  CA    . LEU A 1 66  ? 19.06326  4.48350   -5.10992  1.000 10.79334 ? 66  LEU A CA    1 
ATOM   502  C  C     . LEU A 1 66  ? 18.82632  5.50049   -4.00289  1.000 9.70048  ? 66  LEU A C     1 
ATOM   503  O  O     . LEU A 1 66  ? 19.76836  6.15743   -3.54488  1.000 9.84697  ? 66  LEU A O     1 
ATOM   504  C  CB    . LEU A 1 66  ? 18.75729  5.10355   -6.47390  1.000 11.40483 ? 66  LEU A CB    1 
ATOM   505  C  CG    . LEU A 1 66  ? 19.32725  4.40355   -7.70692  1.000 9.15932  ? 66  LEU A CG    1 
ATOM   506  C  CD1   . LEU A 1 66  ? 18.75528  5.01761   -8.97391  1.000 12.17643 ? 66  LEU A CD1   1 
ATOM   507  C  CD2   . LEU A 1 66  ? 20.84025  4.48947   -7.71293  1.000 11.48106 ? 66  LEU A CD2   1 
ATOM   508  N  N     . GLN A 1 67  ? 17.57533  5.63954   -3.55489  1.000 9.41446  ? 67  GLN A N     1 
ATOM   509  C  CA    . GLN A 1 67  ? 17.26638  6.60053   -2.50086  1.000 9.39481  ? 67  GLN A CA    1 
ATOM   510  C  C     . GLN A 1 67  ? 17.97937  6.24646   -1.20087  1.000 11.34846 ? 67  GLN A C     1 
ATOM   511  O  O     . GLN A 1 67  ? 18.55642  7.11842   -0.53986  1.000 12.38036 ? 67  GLN A O     1 
ATOM   512  C  CB    . GLN A 1 67  ? 15.75539  6.67460   -2.28485  1.000 9.67279  ? 67  GLN A CB    1 
ATOM   513  C  CG    . GLN A 1 67  ? 15.31644  7.63060   -1.18183  1.000 13.41327 ? 67  GLN A CG    1 
ATOM   514  C  CD    . GLN A 1 67  ? 15.54051  9.09159   -1.53480  1.000 14.15051 ? 67  GLN A CD    1 
ATOM   515  O  OE1   . GLN A 1 67  ? 16.67554  9.56554   -1.59079  1.000 17.92489 ? 67  GLN A OE1   1 
ATOM   516  N  NE2   . GLN A 1 67  ? 14.45155  9.81666   -1.76978  1.000 17.06750 ? 67  GLN A NE2   1 
ATOM   517  N  N     . ARG A 1 68  ? 17.94503  4.97071   -0.80931  1.000 11.00828 ? 68  ARG A N     1 
ATOM   518  C  CA    . ARG A 1 68  ? 18.63989  4.55887   0.40785   1.000 12.34453 ? 68  ARG A CA    1 
ATOM   519  C  C     . ARG A 1 68  ? 20.14702  4.71085   0.25942   1.000 13.85255 ? 68  ARG A C     1 
ATOM   520  O  O     . ARG A 1 68  ? 20.84312  5.04815   1.22434   1.000 10.87053 ? 68  ARG A O     1 
ATOM   521  C  CB    . ARG A 1 68  ? 18.28790  3.11473   0.75647   1.000 15.54840 ? 68  ARG A CB    1 
ATOM   522  C  CG    . ARG A 1 68  ? 16.83512  2.89618   1.15373   1.000 16.44777 ? 68  ARG A CG    1 
ATOM   523  C  CD    . ARG A 1 68  ? 16.62267  1.48327   1.66779   1.000 22.78923 ? 68  ARG A CD    1 
ATOM   524  N  NE    . ARG A 1 68  ? 17.09524  0.48302   0.71818   1.000 18.51477 ? 68  ARG A NE    1 
ATOM   525  C  CZ    . ARG A 1 68  ? 16.33614  -0.09234  -0.20370  1.000 15.27177 ? 68  ARG A CZ    1 
ATOM   526  N  NH1   . ARG A 1 68  ? 15.05116  0.19993   -0.32169  1.000 20.65776 ? 68  ARG A NH1   1 
ATOM   527  N  NH2   . ARG A 1 68  ? 16.87940  -0.98500  -1.02642  1.000 21.04236 ? 68  ARG A NH2   1 
ATOM   528  N  N     . SER A 1 69  ? 20.66828  4.46932   -0.94493  1.000 13.75095 ? 69  SER A N     1 
ATOM   529  C  CA    . SER A 1 69  ? 22.09929  4.62625   -1.18093  1.000 14.05986 ? 69  SER A CA    1 
ATOM   530  C  C     . SER A 1 69  ? 22.51936  6.08923   -1.13190  1.000 11.06467 ? 69  SER A C     1 
ATOM   531  O  O     . SER A 1 69  ? 23.62938  6.39617   -0.68389  1.000 16.57314 ? 69  SER A O     1 
ATOM   532  C  CB    . SER A 1 69  ? 22.47725  3.99227   -2.51994  1.000 10.86311 ? 69  SER A CB    1 
ATOM   533  O  OG    . SER A 1 69  ? 22.27218  2.59028   -2.47798  1.000 11.84539 ? 69  SER A OG    1 
ATOM   534  N  N     . PHE A 1 70  ? 21.64941  7.00329   -1.57087  1.000 13.23214 ? 70  PHE A N     1 
ATOM   535  C  CA    . PHE A 1 70  ? 21.96248  8.42527   -1.48984  1.000 12.38359 ? 70  PHE A CA    1 
ATOM   536  C  C     . PHE A 1 70  ? 21.82551  8.96324   -0.07182  1.000 14.10197 ? 70  PHE A C     1 
ATOM   537  O  O     . PHE A 1 70  ? 22.59756  9.84119   0.32719   1.000 15.46360 ? 70  PHE A O     1 
ATOM   538  C  CB    . PHE A 1 70  ? 21.07251  9.22234   -2.44782  1.000 13.45623 ? 70  PHE A CB    1 
ATOM   539  C  CG    . PHE A 1 70  ? 21.54151  9.19735   -3.87882  1.000 10.14226 ? 70  PHE A CG    1 
ATOM   540  C  CD1   . PHE A 1 70  ? 22.77253  9.72029   -4.21981  1.000 12.64119 ? 70  PHE A CD1   1 
ATOM   541  C  CD2   . PHE A 1 70  ? 20.74248  8.67541   -4.88183  1.000 10.72596 ? 70  PHE A CD2   1 
ATOM   542  C  CE1   . PHE A 1 70  ? 23.20953  9.70430   -5.52281  1.000 11.36728 ? 70  PHE A CE1   1 
ATOM   543  C  CE2   . PHE A 1 70  ? 21.17747  8.66042   -6.19083  1.000 13.64820 ? 70  PHE A CE2   1 
ATOM   544  C  CZ    . PHE A 1 70  ? 22.41050  9.17536   -6.50882  1.000 10.38115 ? 70  PHE A CZ    1 
ATOM   545  N  N     . GLN A 1 71  ? 20.86949  8.44727   0.70217   1.000 14.70515 ? 71  GLN A N     1 
ATOM   546  C  CA    . GLN A 1 71  ? 20.73152  8.88625   2.08618   1.000 13.27242 ? 71  GLN A CA    1 
ATOM   547  C  C     . GLN A 1 71  ? 21.94550  8.50617   2.92116   1.000 15.30076 ? 71  GLN A C     1 
ATOM   548  O  O     . GLN A 1 71  ? 22.31854  9.24312   3.84318   1.000 15.02367 ? 71  GLN A O     1 
ATOM   549  C  CB    . GLN A 1 71  ? 19.46249  8.30630   2.70217   1.000 14.98233 ? 71  GLN A CB    1 
ATOM   550  C  CG    . GLN A 1 71  ? 18.17552  8.92137   2.17919   1.000 16.74587 ? 71  GLN A CG    1 
ATOM   551  C  CD    . GLN A 1 71  ? 16.94149  8.35942   2.86818   1.000 26.11999 ? 71  GLN A CD    1 
ATOM   552  O  OE1   . GLN A 1 71  ? 17.00244  7.32440   3.53616   1.000 22.13328 ? 71  GLN A OE1   1 
ATOM   553  N  NE2   . GLN A 1 71  ? 15.81353  9.04248   2.71020   1.000 26.54505 ? 71  GLN A NE2   1 
ATOM   554  N  N     . ALA A 1 72  ? 22.56944  7.36814   2.61913   1.000 14.79842 ? 72  ALA A N     1 
ATOM   555  C  CA    . ALA A 1 72  ? 23.75042  6.94606   3.36012   1.000 15.54339 ? 72  ALA A CA    1 
ATOM   556  C  C     . ALA A 1 72  ? 24.94547  7.85301   3.10414   1.000 14.03254 ? 72  ALA A C     1 
ATOM   557  O  O     . ALA A 1 72  ? 25.85947  7.90694   3.93513   1.000 13.37325 ? 72  ALA A O     1 
ATOM   558  C  CB    . ALA A 1 72  ? 24.10735  5.50205   3.00108   1.000 11.18112 ? 72  ALA A CB    1 
ATOM   559  N  N     . ARG A 1 73  ? 24.97150  8.55199   1.97088   1.000 14.65611 ? 73  ARG A N     1 
ATOM   560  C  CA    . ARG A 1 73  ? 26.04677  9.47789   1.64037   1.000 14.19860 ? 73  ARG A CA    1 
ATOM   561  C  C     . ARG A 1 73  ? 25.61371  10.93392  1.78055   1.000 12.89582 ? 73  ARG A C     1 
ATOM   562  O  O     . ARG A 1 73  ? 26.12458  11.80465  1.07106   1.000 14.57289 ? 73  ARG A O     1 
ATOM   563  C  CB    . ARG A 1 73  ? 26.55874  9.19836   0.22855   1.000 14.82103 ? 73  ARG A CB    1 
ATOM   564  C  CG    . ARG A 1 73  ? 27.01897  7.76378   0.03079   1.000 13.00311 ? 73  ARG A CG    1 
ATOM   565  C  CD    . ARG A 1 73  ? 27.12153  7.39180   -1.43587  1.000 18.43993 ? 73  ARG A CD    1 
ATOM   566  N  NE    . ARG A 1 73  ? 27.24374  5.94954   -1.60917  1.000 19.39502 ? 73  ARG A NE    1 
ATOM   567  C  CZ    . ARG A 1 73  ? 28.39020  5.30849   -1.78828  1.000 18.63822 ? 73  ARG A CZ    1 
ATOM   568  N  NH1   . ARG A 1 73  ? 29.54434  5.95414   -1.83560  1.000 20.99385 ? 73  ARG A NH1   1 
ATOM   569  N  NH2   . ARG A 1 73  ? 28.37793  3.98659   -1.92857  1.000 27.73769 ? 73  ARG A NH2   1 
ATOM   570  N  N     . GLY A 1 74  ? 24.66964  11.21103  2.67822   1.000 10.94457 ? 74  GLY A N     1 
ATOM   571  C  CA    . GLY A 1 74  ? 24.25371  12.57105  2.94925   1.000 9.96077  ? 74  GLY A CA    1 
ATOM   572  C  C     . GLY A 1 74  ? 23.46873  13.24311  1.84827   1.000 15.07133 ? 74  GLY A C     1 
ATOM   573  O  O     . GLY A 1 74  ? 23.36480  14.47312  1.84430   1.000 16.78373 ? 74  GLY A O     1 
ATOM   574  N  N     . SER A 1 75  ? 22.90469  12.47816  0.91325   1.000 10.01287 ? 75  SER A N     1 
ATOM   575  C  CA    . SER A 1 75  ? 22.18472  13.07423  -0.20573  1.000 12.71568 ? 75  SER A CA    1 
ATOM   576  C  C     . SER A 1 75  ? 20.74769  12.57230  -0.25174  1.000 15.87210 ? 75  SER A C     1 
ATOM   577  O  O     . SER A 1 75  ? 20.23367  12.06430  0.75025   1.000 17.66047 ? 75  SER A O     1 
ATOM   578  C  CB    . SER A 1 75  ? 22.90070  12.78222  -1.52674  1.000 16.49940 ? 75  SER A CB    1 
ATOM   579  O  OG    . SER A 1 75  ? 22.54474  13.72926  -2.52072  1.000 14.70039 ? 75  SER A OG    1 
ATOM   580  N  N     . ARG A 1 76  ? 20.09551  12.70579  -1.40508  1.000 14.17056 ? 76  ARG A N     1 
ATOM   581  C  CA    . ARG A 1 76  ? 18.68317  12.36986  -1.52677  1.000 14.61490 ? 76  ARG A CA    1 
ATOM   582  C  C     . ARG A 1 76  ? 18.32687  12.23577  -2.99946  1.000 14.00914 ? 76  ARG A C     1 
ATOM   583  O  O     . ARG A 1 76  ? 18.84929  12.97392  -3.84038  1.000 10.72517 ? 76  ARG A O     1 
ATOM   584  C  CB    . ARG A 1 76  ? 17.81222  13.44073  -0.85274  1.000 14.54469 ? 76  ARG A CB    1 
ATOM   585  C  CG    . ARG A 1 76  ? 16.32829  13.12627  -0.80350  1.000 15.80833 ? 76  ARG A CG    1 
ATOM   586  C  CD    . ARG A 1 76  ? 15.62007  14.00323  0.21969   1.000 12.60306 ? 76  ARG A CD    1 
ATOM   587  N  NE    . ARG A 1 76  ? 15.72156  15.42371  -0.09901  1.000 15.37311 ? 76  ARG A NE    1 
ATOM   588  C  CZ    . ARG A 1 76  ? 14.75986  16.13421  -0.67382  1.000 17.72330 ? 76  ARG A CZ    1 
ATOM   589  N  NH1   . ARG A 1 76  ? 13.60198  15.58768  -1.00504  1.000 15.18152 ? 76  ARG A NH1   1 
ATOM   590  N  NH2   . ARG A 1 76  ? 14.96402  17.42624  -0.92091  1.000 19.50277 ? 76  ARG A NH2   1 
ATOM   591  N  N     . LEU A 1 77  ? 17.44262  11.28754  -3.31075  1.000 15.93783 ? 77  LEU A N     1 
ATOM   592  C  CA    . LEU A 1 77  ? 16.96660  11.09860  -4.67476  1.000 12.25195 ? 77  LEU A CA    1 
ATOM   593  C  C     . LEU A 1 77  ? 15.67364  11.87867  -4.87173  1.000 13.37243 ? 77  LEU A C     1 
ATOM   594  O  O     . LEU A 1 77  ? 14.72263  11.71770  -4.10073  1.000 13.88625 ? 77  LEU A O     1 
ATOM   595  C  CB    . LEU A 1 77  ? 16.73952  9.61662   -4.97879  1.000 11.89727 ? 77  LEU A CB    1 
ATOM   596  C  CG    . LEU A 1 77  ? 16.18850  9.28868   -6.37179  1.000 12.37186 ? 77  LEU A CG    1 
ATOM   597  C  CD1   . LEU A 1 77  ? 17.15052  9.75265   -7.45879  1.000 10.03841 ? 77  LEU A CD1   1 
ATOM   598  C  CD2   . LEU A 1 77  ? 15.88543  7.80069   -6.51983  1.000 11.40667 ? 77  LEU A CD2   1 
ATOM   599  N  N     . LEU A 1 78  ? 15.64168  12.71869  -5.90271  1.000 8.61023  ? 78  LEU A N     1 
ATOM   600  C  CA    . LEU A 1 78  ? 14.48172  13.54876  -6.20169  1.000 10.24760 ? 78  LEU A CA    1 
ATOM   601  C  C     . LEU A 1 78  ? 13.71868  12.93682  -7.36970  1.000 10.61951 ? 78  LEU A C     1 
ATOM   602  O  O     . LEU A 1 78  ? 14.27567  12.76882  -8.46071  1.000 10.00349 ? 78  LEU A O     1 
ATOM   603  C  CB    . LEU A 1 78  ? 14.90179  14.98174  -6.52566  1.000 11.72697 ? 78  LEU A CB    1 
ATOM   604  C  CG    . LEU A 1 78  ? 15.79983  15.68268  -5.50564  1.000 11.11024 ? 78  LEU A CG    1 
ATOM   605  C  CD1   . LEU A 1 78  ? 16.18490  17.06067  -6.01061  1.000 15.70913 ? 78  LEU A CD1   1 
ATOM   606  C  CD2   . LEU A 1 78  ? 15.12784  15.77668  -4.14364  1.000 10.85079 ? 78  LEU A CD2   1 
ATOM   607  N  N     . VAL A 1 79  ? 12.45367  12.60288  -7.13570  1.000 8.88018  ? 79  VAL A N     1 
ATOM   608  C  CA    . VAL A 1 79  ? 11.58063  12.04095  -8.16671  1.000 11.40068 ? 79  VAL A CA    1 
ATOM   609  C  C     . VAL A 1 79  ? 10.66469  13.17501  -8.61668  1.000 9.86408  ? 79  VAL A C     1 
ATOM   610  O  O     . VAL A 1 79  ? 9.57670   13.38305  -8.07667  1.000 12.47633 ? 79  VAL A O     1 
ATOM   611  C  CB    . VAL A 1 79  ? 10.79758  10.82898  -7.65974  1.000 10.89873 ? 79  VAL A CB    1 
ATOM   612  C  CG1   . VAL A 1 79  ? 9.91454   10.26205  -8.76575  1.000 10.03982 ? 79  VAL A CG1   1 
ATOM   613  C  CG2   . VAL A 1 79  ? 11.74752  9.75892   -7.13177  1.000 9.48820  ? 79  VAL A CG2   1 
ATOM   614  N  N     . LEU A 1 80  ? 11.11072  13.91801  -9.62267  1.000 9.81852  ? 80  LEU A N     1 
ATOM   615  C  CA    . LEU A 1 80  ? 10.33078  15.02506  -10.15964 1.000 13.71363 ? 80  LEU A CA    1 
ATOM   616  C  C     . LEU A 1 80  ? 9.21075   14.50814  -11.05464 1.000 16.68608 ? 80  LEU A C     1 
ATOM   617  O  O     . LEU A 1 80  ? 9.43770   13.66415  -11.92867 1.000 14.02788 ? 80  LEU A O     1 
ATOM   618  C  CB    . LEU A 1 80  ? 11.23682  15.97703  -10.93962 1.000 11.82844 ? 80  LEU A CB    1 
ATOM   619  C  CG    . LEU A 1 80  ? 12.31286  16.68196  -10.11161 1.000 18.36750 ? 80  LEU A CG    1 
ATOM   620  C  CD1   . LEU A 1 80  ? 13.27790  17.45493  -10.99859 1.000 14.98524 ? 80  LEU A CD1   1 
ATOM   621  C  CD2   . LEU A 1 80  ? 11.66291  17.60497  -9.09758  1.000 16.58467 ? 80  LEU A CD2   1 
ATOM   622  N  N     . ARG A 1 81  ? 8.00156   15.02665  -10.84254 1.000 14.86214 ? 81  ARG A N     1 
ATOM   623  C  CA    . ARG A 1 81  ? 6.83932   14.62772  -11.62590 1.000 17.76656 ? 81  ARG A CA    1 
ATOM   624  C  C     . ARG A 1 81  ? 6.71163   15.49131  -12.87316 1.000 18.21382 ? 81  ARG A C     1 
ATOM   625  O  O     . ARG A 1 81  ? 6.99820   16.69335  -12.84745 1.000 20.34744 ? 81  ARG A O     1 
ATOM   626  C  CB    . ARG A 1 81  ? 5.55823   14.72680  -10.79308 1.000 15.11787 ? 81  ARG A CB    1 
ATOM   627  C  CG    . ARG A 1 81  ? 5.13149   13.42527  -10.13299 1.000 18.49374 ? 81  ARG A CG    1 
ATOM   628  C  CD    . ARG A 1 81  ? 6.11792   12.97777  -9.06566  1.000 16.23051 ? 81  ARG A CD    1 
ATOM   629  N  NE    . ARG A 1 81  ? 5.62254   11.83200  -8.31176  1.000 12.24678 ? 81  ARG A NE    1 
ATOM   630  C  CZ    . ARG A 1 81  ? 6.19214   11.35520  -7.21372  1.000 15.01232 ? 81  ARG A CZ    1 
ATOM   631  N  NH1   . ARG A 1 81  ? 7.29695   11.88803  -6.71963  1.000 16.51724 ? 81  ARG A NH1   1 
ATOM   632  N  NH2   . ARG A 1 81  ? 5.63561   10.32193  -6.59132  1.000 9.99801  ? 81  ARG A NH2   1 
ATOM   633  N  N     . GLY A 1 82  ? 6.26575   14.87136  -13.96362 1.000 14.69355 ? 82  GLY A N     1 
ATOM   634  C  CA    . GLY A 1 82  ? 6.07579   15.57640  -15.21561 1.000 16.58016 ? 82  GLY A CA    1 
ATOM   635  C  C     . GLY A 1 82  ? 6.98176   15.09538  -16.33062 1.000 23.55921 ? 82  GLY A C     1 
ATOM   636  O  O     . GLY A 1 82  ? 7.55370   14.00435  -16.25065 1.000 17.82334 ? 82  GLY A O     1 
ATOM   637  N  N     . LYS A 1 83  ? 7.11279   15.89739  -17.37760 1.000 22.36072 ? 83  LYS A N     1 
ATOM   638  C  CA    . LYS A 1 83  ? 7.96277   15.59338  -18.51461 1.000 21.06037 ? 83  LYS A CA    1 
ATOM   639  C  C     . LYS A 1 83  ? 9.28481   16.33431  -18.40260 1.000 18.75325 ? 83  LYS A C     1 
ATOM   640  O  O     . LYS A 1 83  ? 9.36587   17.38329  -17.75858 1.000 17.62215 ? 83  LYS A O     1 
ATOM   641  C  CB    . LYS A 1 83  ? 7.26079   15.97644  -19.81960 1.000 24.28071 ? 83  LYS A CB    1 
ATOM   642  C  CG    . LYS A 1 83  ? 5.95475   15.24052  -20.04561 1.000 31.77733 ? 83  LYS A CG    1 
ATOM   643  C  CD    . LYS A 1 83  ? 5.52575   15.26757  -21.50661 1.000 42.74127 ? 83  LYS A CD    1 
ATOM   644  C  CE    . LYS A 1 83  ? 5.10681   16.65760  -21.96058 1.000 37.35699 ? 83  LYS A CE    1 
ATOM   645  N  NZ    . LYS A 1 83  ? 6.24486   17.56156  -22.30856 1.000 39.65846 ? 83  LYS A NZ    1 
ATOM   646  N  N     . PRO A 1 84  ? 10.35378  15.81027  -19.01262 1.000 19.27131 ? 84  PRO A N     1 
ATOM   647  C  CA    . PRO A 1 84  ? 11.65382  16.49420  -18.89761 1.000 16.98270 ? 84  PRO A CA    1 
ATOM   648  C  C     . PRO A 1 84  ? 11.66989  17.88121  -19.51857 1.000 17.21020 ? 84  PRO A C     1 
ATOM   649  O  O     . PRO A 1 84  ? 12.30893  18.78917  -18.97156 1.000 16.90605 ? 84  PRO A O     1 
ATOM   650  C  CB    . PRO A 1 84  ? 12.62077  15.53817  -19.61663 1.000 12.47956 ? 84  PRO A CB    1 
ATOM   651  C  CG    . PRO A 1 84  ? 11.94770  14.21320  -19.59166 1.000 13.04518 ? 84  PRO A CG    1 
ATOM   652  C  CD    . PRO A 1 84  ? 10.47671  14.50828  -19.68665 1.000 14.75315 ? 84  PRO A CD    1 
ATOM   653  N  N     . GLU A 1 85  ? 10.96589  18.07828  -20.63857 1.000 17.45306 ? 85  GLU A N     1 
ATOM   654  C  CA    . GLU A 1 85  ? 11.04095  19.35329  -21.34854 1.000 15.90905 ? 85  GLU A CA    1 
ATOM   655  C  C     . GLU A 1 85  ? 10.40001  20.48730  -20.55751 1.000 17.63428 ? 85  GLU A C     1 
ATOM   656  O  O     . GLU A 1 85  ? 10.73107  21.65629  -20.78048 1.000 14.39898 ? 85  GLU A O     1 
ATOM   657  C  CB    . GLU A 1 85  ? 10.37894  19.23936  -22.72354 1.000 15.32184 ? 85  GLU A CB    1 
ATOM   658  C  CG    . GLU A 1 85  ? 10.90688  18.10935  -23.60457 1.000 23.32779 ? 85  GLU A CG    1 
ATOM   659  C  CD    . GLU A 1 85  ? 10.17682  16.79538  -23.38259 1.000 21.17077 ? 85  GLU A CD    1 
ATOM   660  O  OE1   . GLU A 1 85  ? 9.13882   16.80042  -22.69059 1.000 24.50396 ? 85  GLU A OE1   1 
ATOM   661  O  OE2   . GLU A 1 85  ? 10.64076  15.75537  -23.89562 1.000 26.20501 ? 85  GLU A OE2   1 
ATOM   662  N  N     . GLU A 1 86  ? 9.48600   20.16933  -19.64351 1.000 18.99192 ? 86  GLU A N     1 
ATOM   663  C  CA    . GLU A 1 86  ? 8.83305   21.17734  -18.81849 1.000 18.97069 ? 86  GLU A CA    1 
ATOM   664  C  C     . GLU A 1 86  ? 9.44707   21.31028  -17.43448 1.000 18.38709 ? 86  GLU A C     1 
ATOM   665  O  O     . GLU A 1 86  ? 9.38712   22.39227  -16.84346 1.000 21.56997 ? 86  GLU A O     1 
ATOM   666  C  CB    . GLU A 1 86  ? 7.34304   20.85241  -18.66849 1.000 22.44043 ? 86  GLU A CB    1 
ATOM   667  C  CG    . GLU A 1 86  ? 6.62002   20.65548  -19.98349 1.000 22.48803 ? 86  GLU A CG    1 
ATOM   668  C  CD    . GLU A 1 86  ? 5.30099   19.93254  -19.81150 1.000 25.34460 ? 86  GLU A CD    1 
ATOM   669  O  OE1   . GLU A 1 86  ? 4.87298   19.73754  -18.65450 1.000 23.28110 ? 86  GLU A OE1   1 
ATOM   670  O  OE2   . GLU A 1 86  ? 4.69996   19.54960  -20.83451 1.000 27.52703 ? 86  GLU A OE2   1 
ATOM   671  N  N     . VAL A 1 87  ? 10.03701  20.23924  -16.90751 1.000 16.05797 ? 87  VAL A N     1 
ATOM   672  C  CA    . VAL A 1 87  ? 10.56802  20.27118  -15.54951 1.000 18.88839 ? 87  VAL A CA    1 
ATOM   673  C  C     . VAL A 1 87  ? 11.95205  20.91011  -15.51350 1.000 15.72935 ? 87  VAL A C     1 
ATOM   674  O  O     . VAL A 1 87  ? 12.24710  21.72507  -14.63149 1.000 14.37412 ? 87  VAL A O     1 
ATOM   675  C  CB    . VAL A 1 87  ? 10.58195  18.84916  -14.96055 1.000 18.48247 ? 87  VAL A CB    1 
ATOM   676  C  CG1   . VAL A 1 87  ? 11.41796  18.80809  -13.69655 1.000 15.30582 ? 87  VAL A CG1   1 
ATOM   677  C  CG2   . VAL A 1 87  ? 9.16193   18.38223  -14.67055 1.000 20.10816 ? 87  VAL A CG2   1 
ATOM   678  N  N     . PHE A 1 88  ? 12.81603  20.56308  -16.47352 1.000 12.79904 ? 88  PHE A N     1 
ATOM   679  C  CA    . PHE A 1 88  ? 14.20306  21.02001  -16.41151 1.000 10.82313 ? 88  PHE A CA    1 
ATOM   680  C  C     . PHE A 1 88  ? 14.34713  22.53001  -16.57948 1.000 11.70781 ? 88  PHE A C     1 
ATOM   681  O  O     . PHE A 1 88  ? 15.10217  23.13995  -15.80446 1.000 12.08654 ? 88  PHE A O     1 
ATOM   682  C  CB    . PHE A 1 88  ? 15.05001  20.25199  -17.42953 1.000 12.22882 ? 88  PHE A CB    1 
ATOM   683  C  CG    . PHE A 1 88  ? 15.48995  18.90496  -16.94557 1.000 10.72273 ? 88  PHE A CG    1 
ATOM   684  C  CD1   . PHE A 1 88  ? 16.36595  18.79889  -15.87957 1.000 13.33671 ? 88  PHE A CD1   1 
ATOM   685  C  CD2   . PHE A 1 88  ? 15.03489  17.74800  -17.55359 1.000 12.22622 ? 88  PHE A CD2   1 
ATOM   686  C  CE1   . PHE A 1 88  ? 16.77889  17.56386  -15.42360 1.000 17.25512 ? 88  PHE A CE1   1 
ATOM   687  C  CE2   . PHE A 1 88  ? 15.44583  16.50897  -17.10262 1.000 11.41465 ? 88  PHE A CE2   1 
ATOM   688  C  CZ    . PHE A 1 88  ? 16.31882  16.41690  -16.03563 1.000 11.71220 ? 88  PHE A CZ    1 
ATOM   689  N  N     . PRO A 1 89  ? 13.69416  23.18607  -17.54746 1.000 12.62985 ? 89  PRO A N     1 
ATOM   690  C  CA    . PRO A 1 89  ? 13.82124  24.65306  -17.62742 1.000 16.11326 ? 89  PRO A CA    1 
ATOM   691  C  C     . PRO A 1 89  ? 13.43128  25.37605  -16.35140 1.000 13.47639 ? 89  PRO A C     1 
ATOM   692  O  O     . PRO A 1 89  ? 13.94933  26.46902  -16.09138 1.000 20.16715 ? 89  PRO A O     1 
ATOM   693  C  CB    . PRO A 1 89  ? 12.88525  25.01714  -18.78741 1.000 15.87387 ? 89  PRO A CB    1 
ATOM   694  C  CG    . PRO A 1 89  ? 12.85218  23.81116  -19.62744 1.000 13.48181 ? 89  PRO A CG    1 
ATOM   695  C  CD    . PRO A 1 89  ? 12.94113  22.64713  -18.69547 1.000 12.06672 ? 89  PRO A CD    1 
ATOM   696  N  N     . ARG A 1 90  ? 12.53059  24.80327  -15.55073 1.000 11.31751 ? 90  ARG A N     1 
ATOM   697  C  CA    . ARG A 1 90  ? 12.18394  25.40294  -14.26659 1.000 13.20061 ? 90  ARG A CA    1 
ATOM   698  C  C     . ARG A 1 90  ? 13.30251  25.20819  -13.25037 1.000 14.76854 ? 90  ARG A C     1 
ATOM   699  O  O     . ARG A 1 90  ? 13.79241  26.17366  -12.65462 1.000 10.74844 ? 90  ARG A O     1 
ATOM   700  C  CB    . ARG A 1 90  ? 10.87806  24.80606  -13.73630 1.000 19.37561 ? 90  ARG A CB    1 
ATOM   701  C  CG    . ARG A 1 90  ? 10.36558  25.49516  -12.47922 1.000 20.41399 ? 90  ARG A CG    1 
ATOM   702  C  CD    . ARG A 1 90  ? 10.04067  24.52511  -11.35343 1.000 25.43868 ? 90  ARG A CD    1 
ATOM   703  N  NE    . ARG A 1 90  ? 8.85442   23.71942  -11.61425 1.000 24.53851 ? 90  ARG A NE    1 
ATOM   704  C  CZ    . ARG A 1 90  ? 8.88425   22.44583  -11.98023 1.000 26.64965 ? 90  ARG A CZ    1 
ATOM   705  N  NH1   . ARG A 1 90  ? 10.02865  21.80299  -12.15036 1.000 27.86135 ? 90  ARG A NH1   1 
ATOM   706  N  NH2   . ARG A 1 90  ? 7.73792   21.79942  -12.17540 1.000 29.62978 ? 90  ARG A NH2   1 
ATOM   707  N  N     . VAL A 1 91  ? 13.72522  23.95796  -13.04444 1.000 15.09918 ? 91  VAL A N     1 
ATOM   708  C  CA    . VAL A 1 91  ? 14.67821  23.64888  -11.98445 1.000 14.87858 ? 91  VAL A CA    1 
ATOM   709  C  C     . VAL A 1 91  ? 16.08323  24.12982  -12.31844 1.000 13.52127 ? 91  VAL A C     1 
ATOM   710  O  O     . VAL A 1 91  ? 16.91824  24.25176  -11.41544 1.000 13.89251 ? 91  VAL A O     1 
ATOM   711  C  CB    . VAL A 1 91  ? 14.67813  22.13988  -11.67649 1.000 13.23777 ? 91  VAL A CB    1 
ATOM   712  C  CG1   . VAL A 1 91  ? 13.29111  21.68994  -11.24449 1.000 11.07936 ? 91  VAL A CG1   1 
ATOM   713  C  CG2   . VAL A 1 91  ? 15.16209  21.34288  -12.87751 1.000 13.24594 ? 91  VAL A CG2   1 
ATOM   714  N  N     . PHE A 1 92  ? 16.37424  24.39584  -13.59644 1.000 18.39172 ? 92  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 92  ? 17.65727  24.99178  -13.95943 1.000 14.31942 ? 92  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 92  ? 17.83134  26.35476  -13.30040 1.000 14.19057 ? 92  PHE A C     1 
ATOM   717  O  O     . PHE A 1 92  ? 18.87136  26.63969  -12.69240 1.000 11.68131 ? 92  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 92  ? 17.77127  25.11881  -15.48043 1.000 15.94576 ? 92  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 92  ? 18.03820  23.82081  -16.18246 1.000 12.87494 ? 92  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 92  ? 18.48815  22.71377  -15.48349 1.000 15.44911 ? 92  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 92  ? 17.84219  23.71086  -17.54546 1.000 12.60944 ? 92  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 92  ? 18.73208  21.51778  -16.13352 1.000 14.23865 ? 92  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 92  ? 18.08613  22.52086  -18.19849 1.000 13.16426 ? 92  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 92  ? 18.53107  21.42282  -17.49052 1.000 11.71031 ? 92  PHE A CZ    1 
ATOM   725  N  N     . ARG A 1 93  ? 16.81094  27.20732  -13.40178 1.000 12.18639 ? 93  ARG A N     1 
ATOM   726  C  CA    . ARG A 1 93  ? 16.89190  28.53493  -12.80629 1.000 17.60897 ? 93  ARG A CA    1 
ATOM   727  C  C     . ARG A 1 93  ? 16.69325  28.49313  -11.29710 1.000 12.77750 ? 93  ARG A C     1 
ATOM   728  O  O     . ARG A 1 93  ? 17.25783  29.32440  -10.57687 1.000 12.93640 ? 93  ARG A O     1 
ATOM   729  C  CB    . ARG A 1 93  ? 15.85785  29.46929  -13.44294 1.000 15.35552 ? 93  ARG A CB    1 
ATOM   730  C  CG    . ARG A 1 93  ? 16.20286  29.96072  -14.84904 1.000 17.31252 ? 93  ARG A CG    1 
ATOM   731  C  CD    . ARG A 1 93  ? 15.97411  28.88725  -15.90879 1.000 20.37785 ? 93  ARG A CD    1 
ATOM   732  N  NE    . ARG A 1 93  ? 16.05587  29.40850  -17.26920 1.000 23.10725 ? 93  ARG A NE    1 
ATOM   733  C  CZ    . ARG A 1 93  ? 16.03906  28.65487  -18.36089 1.000 17.12049 ? 93  ARG A CZ    1 
ATOM   734  N  NH1   . ARG A 1 93  ? 15.95436  27.33635  -18.28864 1.000 19.27785 ? 93  ARG A NH1   1 
ATOM   735  N  NH2   . ARG A 1 93  ? 16.11421  29.23812  -19.55465 1.000 20.67623 ? 93  ARG A NH2   1 
ATOM   736  N  N     . GLU A 1 94  ? 15.90241  27.53979  -10.80236 1.000 14.18555 ? 94  GLU A N     1 
ATOM   737  C  CA    . GLU A 1 94  ? 15.62041  27.48278  -9.37236  1.000 15.84411 ? 94  GLU A CA    1 
ATOM   738  C  C     . GLU A 1 94  ? 16.82639  26.98270  -8.58538  1.000 13.25113 ? 94  GLU A C     1 
ATOM   739  O  O     . GLU A 1 94  ? 17.12542  27.49666  -7.50037  1.000 17.37145 ? 94  GLU A O     1 
ATOM   740  C  CB    . GLU A 1 94  ? 14.40637  26.59183  -9.11938  1.000 13.75674 ? 94  GLU A CB    1 
ATOM   741  C  CG    . GLU A 1 94  ? 14.12436  26.31381  -7.65439  1.000 16.10384 ? 94  GLU A CG    1 
ATOM   742  C  CD    . GLU A 1 94  ? 13.00731  25.30786  -7.46540  1.000 10.77696 ? 94  GLU A CD    1 
ATOM   743  O  OE1   . GLU A 1 94  ? 12.02431  25.36193  -8.23140  1.000 14.98258 ? 94  GLU A OE1   1 
ATOM   744  O  OE2   . GLU A 1 94  ? 13.11527  24.45284  -6.56242  1.000 11.76335 ? 94  GLU A OE2   1 
ATOM   745  N  N     . TRP A 1 95  ? 17.53334  25.98667  -9.11241  1.000 12.90444 ? 95  TRP A N     1 
ATOM   746  C  CA    . TRP A 1 95  ? 18.64731  25.36760  -8.40943  1.000 12.71109 ? 95  TRP A CA    1 
ATOM   747  C  C     . TRP A 1 95  ? 19.99734  25.96054  -8.78842  1.000 12.28309 ? 95  TRP A C     1 
ATOM   748  O  O     . TRP A 1 95  ? 21.02331  25.49848  -8.27943  1.000 12.92692 ? 95  TRP A O     1 
ATOM   749  C  CB    . TRP A 1 95  ? 18.65423  23.86061  -8.66946  1.000 11.12824 ? 95  TRP A CB    1 
ATOM   750  C  CG    . TRP A 1 95  ? 17.39520  23.16766  -8.23747  1.000 12.80573 ? 95  TRP A CG    1 
ATOM   751  C  CD1   . TRP A 1 95  ? 16.44822  23.64269  -7.37546  1.000 11.89075 ? 95  TRP A CD1   1 
ATOM   752  C  CD2   . TRP A 1 95  ? 16.94413  21.87169  -8.65350  1.000 10.89214 ? 95  TRP A CD2   1 
ATOM   753  N  NE1   . TRP A 1 95  ? 15.43918  22.72173  -7.22747  1.000 12.10155 ? 95  TRP A NE1   1 
ATOM   754  C  CE2   . TRP A 1 95  ? 15.71912  21.62574  -8.00150  1.000 11.11334 ? 95  TRP A CE2   1 
ATOM   755  C  CE3   . TRP A 1 95  ? 17.45808  20.89669  -9.51453  1.000 14.08100 ? 95  TRP A CE3   1 
ATOM   756  C  CZ2   . TRP A 1 95  ? 15.00106  20.44278  -8.18153  1.000 13.02379 ? 95  TRP A CZ2   1 
ATOM   757  C  CZ3   . TRP A 1 95  ? 16.74502  19.72273  -9.69255  1.000 10.96163 ? 95  TRP A CZ3   1 
ATOM   758  C  CH2   . TRP A 1 95  ? 15.52901  19.50677  -9.02955  1.000 11.57961 ? 95  TRP A CH2   1 
ATOM   759  N  N     . GLY A 1 96  ? 20.02338  26.96856  -9.65639  1.000 10.65572 ? 96  GLY A N     1 
ATOM   760  C  CA    . GLY A 1 96  ? 21.28741  27.53551  -10.10238 1.000 11.19430 ? 96  GLY A CA    1 
ATOM   761  C  C     . GLY A 1 96  ? 22.18336  26.52648  -10.78641 1.000 10.89125 ? 96  GLY A C     1 
ATOM   762  O  O     . GLY A 1 96  ? 23.40636  26.54941  -10.59442 1.000 9.45585  ? 96  GLY A O     1 
ATOM   763  N  N     . VAL A 1 97  ? 21.59731  25.63853  -11.59143 1.000 10.74146 ? 97  VAL A N     1 
ATOM   764  C  CA    . VAL A 1 97  ? 22.34825  24.54350  -12.19146 1.000 10.86985 ? 97  VAL A CA    1 
ATOM   765  C  C     . VAL A 1 97  ? 23.32027  25.08248  -13.23045 1.000 11.32084 ? 97  VAL A C     1 
ATOM   766  O  O     . VAL A 1 97  ? 22.98032  25.95951  -14.03643 1.000 15.42834 ? 97  VAL A O     1 
ATOM   767  C  CB    . VAL A 1 97  ? 21.38220  23.51957  -12.81048 1.000 10.58975 ? 97  VAL A CB    1 
ATOM   768  C  CG1   . VAL A 1 97  ? 22.13613  22.28254  -13.27451 1.000 9.60978  ? 97  VAL A CG1   1 
ATOM   769  C  CG2   . VAL A 1 97  ? 20.29718  23.15260  -11.81248 1.000 12.41628 ? 97  VAL A CG2   1 
ATOM   770  N  N     . THR A 1 98  ? 24.54625  24.55941  -13.21047 1.000 13.20702 ? 98  THR A N     1 
ATOM   771  C  CA    . THR A 1 98  ? 25.55526  24.89339  -14.20146 1.000 11.14006 ? 98  THR A CA    1 
ATOM   772  C  C     . THR A 1 98  ? 25.97720  23.71039  -15.05649 1.000 14.11366 ? 98  THR A C     1 
ATOM   773  O  O     . THR A 1 98  ? 26.57920  23.92238  -16.11449 1.000 15.77739 ? 98  THR A O     1 
ATOM   774  C  CB    . THR A 1 98  ? 26.80629  25.48531  -13.52545 1.000 11.66068 ? 98  THR A CB    1 
ATOM   775  O  OG1   . THR A 1 98  ? 27.38025  24.52026  -12.63648 1.000 14.57158 ? 98  THR A OG1   1 
ATOM   776  C  CG2   . THR A 1 98  ? 26.44936  26.73631  -12.73642 1.000 12.98915 ? 98  THR A CG2   1 
ATOM   777  N  N     . GLN A 1 99  ? 25.67714  22.48139  -14.64052 1.000 11.89791 ? 99  GLN A N     1 
ATOM   778  C  CA    . GLN A 1 99  ? 26.09307  21.29139  -15.37255 1.000 11.61791 ? 99  GLN A CA    1 
ATOM   779  C  C     . GLN A 1 99  ? 25.02502  20.21844  -15.24357 1.000 10.80566 ? 99  GLN A C     1 
ATOM   780  O  O     . GLN A 1 99  ? 24.56301  19.92944  -14.13458 1.000 11.37789 ? 99  GLN A O     1 
ATOM   781  C  CB    . GLN A 1 99  ? 27.43505  20.75731  -14.85557 1.000 10.13206 ? 99  GLN A CB    1 
ATOM   782  C  CG    . GLN A 1 99  ? 28.07199  19.70230  -15.75760 1.000 13.37815 ? 99  GLN A CG    1 
ATOM   783  C  CD    . GLN A 1 99  ? 29.25396  19.00722  -15.10662 1.000 13.83231 ? 99  GLN A CD    1 
ATOM   784  O  OE1   . GLN A 1 99  ? 30.37996  19.06618  -15.60662 1.000 16.22800 ? 99  GLN A OE1   1 
ATOM   785  N  NE2   . GLN A 1 99  ? 28.99793  18.33321  -13.98863 1.000 12.56148 ? 99  GLN A NE2   1 
ATOM   786  N  N     . LEU A 1 100 ? 24.64299  19.63348  -16.37658 1.000 10.67268 ? 100 LEU A N     1 
ATOM   787  C  CA    . LEU A 1 100 ? 23.70093  18.52353  -16.43361 1.000 8.91713  ? 100 LEU A CA    1 
ATOM   788  C  C     . LEU A 1 100 ? 24.43886  17.27251  -16.89264 1.000 11.31906 ? 100 LEU A C     1 
ATOM   789  O  O     . LEU A 1 100 ? 25.23386  17.32349  -17.83664 1.000 10.56767 ? 100 LEU A O     1 
ATOM   790  C  CB    . LEU A 1 100 ? 22.53294  18.84561  -17.37359 1.000 8.55854  ? 100 LEU A CB    1 
ATOM   791  C  CG    . LEU A 1 100 ? 21.50289  17.73767  -17.60262 1.000 9.49901  ? 100 LEU A CG    1 
ATOM   792  C  CD1   . LEU A 1 100 ? 20.85687  17.34167  -16.28762 1.000 6.55197  ? 100 LEU A CD1   1 
ATOM   793  C  CD2   . LEU A 1 100 ? 20.44990  18.15375  -18.62060 1.000 9.21617  ? 100 LEU A CD2   1 
ATOM   794  N  N     . CYS A 1 101 ? 24.19081  16.15850  -16.21066 1.000 10.93397 ? 101 CYS A N     1 
ATOM   795  C  CA    . CYS A 1 101 ? 24.89675  14.91347  -16.47070 1.000 8.72583  ? 101 CYS A CA    1 
ATOM   796  C  C     . CYS A 1 101 ? 23.89069  13.77753  -16.53672 1.000 10.32840 ? 101 CYS A C     1 
ATOM   797  O  O     . CYS A 1 101 ? 23.02769  13.65755  -15.66072 1.000 11.82074 ? 101 CYS A O     1 
ATOM   798  C  CB    . CYS A 1 101 ? 25.94474  14.63140  -15.38771 1.000 9.53937  ? 101 CYS A CB    1 
ATOM   799  S  SG    . CYS A 1 101 ? 27.28380  15.84632  -15.27068 1.000 13.45259 ? 101 CYS A SG    1 
ATOM   800  N  N     . PHE A 1 102 ? 23.99364  12.95555  -17.57774 1.000 7.93556  ? 102 PHE A N     1 
ATOM   801  C  CA    . PHE A 1 102 ? 23.17658  11.75459  -17.67676 1.000 9.05159  ? 102 PHE A CA    1 
ATOM   802  C  C     . PHE A 1 102 ? 23.85753  10.77858  -18.62379 1.000 10.45772 ? 102 PHE A C     1 
ATOM   803  O  O     . PHE A 1 102 ? 24.65255  11.16856  -19.48378 1.000 8.71584  ? 102 PHE A O     1 
ATOM   804  C  CB    . PHE A 1 102 ? 21.74260  12.06667  -18.13275 1.000 9.32274  ? 102 PHE A CB    1 
ATOM   805  C  CG    . PHE A 1 102 ? 21.65463  12.84671  -19.41673 1.000 7.78858  ? 102 PHE A CG    1 
ATOM   806  C  CD1   . PHE A 1 102 ? 21.66270  14.22971  -19.40070 1.000 8.83236  ? 102 PHE A CD1   1 
ATOM   807  C  CD2   . PHE A 1 102 ? 21.53359  12.19674  -20.63575 1.000 10.44180 ? 102 PHE A CD2   1 
ATOM   808  C  CE1   . PHE A 1 102 ? 21.57073  14.95174  -20.57368 1.000 7.95675  ? 102 PHE A CE1   1 
ATOM   809  C  CE2   . PHE A 1 102 ? 21.43962  12.91277  -21.81473 1.000 8.22826  ? 102 PHE A CE2   1 
ATOM   810  C  CZ    . PHE A 1 102 ? 21.45669  14.29177  -21.78470 1.000 11.40514 ? 102 PHE A CZ    1 
ATOM   811  N  N     . GLU A 1 103 ? 23.53347  9.50059   -18.44582 1.000 8.26285  ? 103 GLU A N     1 
ATOM   812  C  CA    . GLU A 1 103 ? 24.14141  8.44258   -19.24185 1.000 9.02616  ? 103 GLU A CA    1 
ATOM   813  C  C     . GLU A 1 103 ? 23.60640  8.47164   -20.66984 1.000 8.14526  ? 103 GLU A C     1 
ATOM   814  O  O     . GLU A 1 103 ? 22.44142  8.79370   -20.90283 1.000 10.51996 ? 103 GLU A O     1 
ATOM   815  C  CB    . GLU A 1 103 ? 23.86534  7.08858   -18.58288 1.000 8.46576  ? 103 GLU A CB    1 
ATOM   816  C  CG    . GLU A 1 103 ? 24.44228  5.87956   -19.29191 1.000 7.92658  ? 103 GLU A CG    1 
ATOM   817  C  CD    . GLU A 1 103 ? 24.13022  4.58956   -18.55894 1.000 8.02260  ? 103 GLU A CD    1 
ATOM   818  O  OE1   . GLU A 1 103 ? 22.94420  4.19362   -18.52094 1.000 8.16534  ? 103 GLU A OE1   1 
ATOM   819  O  OE2   . GLU A 1 103 ? 25.06719  3.98250   -17.99996 1.000 8.03696  ? 103 GLU A OE2   1 
ATOM   820  N  N     . HIS A 1 104 ? 24.47138  8.14762   -21.63185 1.000 8.56982  ? 104 HIS A N     1 
ATOM   821  C  CA    . HIS A 1 104 ? 24.06138  8.14567   -23.02985 1.000 8.38608  ? 104 HIS A CA    1 
ATOM   822  C  C     . HIS A 1 104 ? 23.03832  7.04673   -23.28887 1.000 11.81377 ? 104 HIS A C     1 
ATOM   823  O  O     . HIS A 1 104 ? 23.11427  5.95671   -22.71590 1.000 10.90971 ? 104 HIS A O     1 
ATOM   824  C  CB    . HIS A 1 104 ? 25.27037  7.95763   -23.94586 1.000 8.97581  ? 104 HIS A CB    1 
ATOM   825  C  CG    . HIS A 1 104 ? 24.95137  8.10768   -25.40186 1.000 10.41895 ? 104 HIS A CG    1 
ATOM   826  N  ND1   . HIS A 1 104 ? 24.66643  9.32671   -25.98083 1.000 14.10598 ? 104 HIS A ND1   1 
ATOM   827  C  CD2   . HIS A 1 104 ? 24.86932  7.19171   -26.39588 1.000 10.84801 ? 104 HIS A CD2   1 
ATOM   828  C  CE1   . HIS A 1 104 ? 24.42441  9.15475   -27.26783 1.000 14.20622 ? 104 HIS A CE1   1 
ATOM   829  N  NE2   . HIS A 1 104 ? 24.54035  7.86875   -27.54586 1.000 17.44966 ? 104 HIS A NE2   1 
ATOM   830  N  N     . ASP A 1 105 ? 22.07233  7.34380   -24.15786 1.000 11.25652 ? 105 ASP A N     1 
ATOM   831  C  CA    . ASP A 1 105 ? 21.04528  6.39086   -24.54888 1.000 15.93238 ? 105 ASP A CA    1 
ATOM   832  C  C     . ASP A 1 105 ? 20.84528  6.47790   -26.05488 1.000 16.18345 ? 105 ASP A C     1 
ATOM   833  O  O     . ASP A 1 105 ? 20.89234  7.56892   -26.63185 1.000 18.01603 ? 105 ASP A O     1 
ATOM   834  C  CB    . ASP A 1 105 ? 19.72530  6.65891   -23.81887 1.000 16.26959 ? 105 ASP A CB    1 
ATOM   835  C  CG    . ASP A 1 105 ? 18.79824  5.45596   -23.82090 1.000 20.76984 ? 105 ASP A CG    1 
ATOM   836  O  OD1   . ASP A 1 105 ? 19.14119  4.43095   -24.44992 1.000 25.80341 ? 105 ASP A OD1   1 
ATOM   837  O  OD2   . ASP A 1 105 ? 17.72725  5.53499   -23.18189 1.000 21.51600 ? 105 ASP A OD2   1 
ATOM   838  N  N     . THR A 1 106 ? 20.62222  5.32593   -26.68591 1.000 14.74227 ? 106 THR A N     1 
ATOM   839  C  CA    . THR A 1 106 ? 20.51221  5.24097   -28.13691 1.000 18.12687 ? 106 THR A CA    1 
ATOM   840  C  C     . THR A 1 106 ? 19.11719  4.84805   -28.60691 1.000 20.26302 ? 106 THR A C     1 
ATOM   841  O  O     . THR A 1 106 ? 18.92717  4.59809   -29.80292 1.000 21.26955 ? 106 THR A O     1 
ATOM   842  C  CB    . THR A 1 106 ? 21.54816  4.25393   -28.68793 1.000 18.94948 ? 106 THR A CB    1 
ATOM   843  O  OG1   . THR A 1 106 ? 21.42410  2.99792   -28.00896 1.000 13.98649 ? 106 THR A OG1   1 
ATOM   844  C  CG2   . THR A 1 106 ? 22.95619  4.78586   -28.48193 1.000 15.55632 ? 106 THR A CG2   1 
ATOM   845  N  N     . GLU A 1 107 ? 18.14019  4.78508   -27.70591 1.000 23.66770 ? 107 GLU A N     1 
ATOM   846  C  CA    . GLU A 1 107 ? 16.78317  4.45416   -28.11291 1.000 23.49770 ? 107 GLU A CA    1 
ATOM   847  C  C     . GLU A 1 107 ? 16.16523  5.61621   -28.89188 1.000 19.37343 ? 107 GLU A C     1 
ATOM   848  O  O     . GLU A 1 107 ? 16.52829  6.77619   -28.67686 1.000 21.38305 ? 107 GLU A O     1 
ATOM   849  C  CB    . GLU A 1 107 ? 15.92616  4.11817   -26.89392 1.000 24.49895 ? 107 GLU A CB    1 
ATOM   850  C  CG    . GLU A 1 107 ? 16.39310  2.88413   -26.13595 1.000 23.72985 ? 107 GLU A CG    1 
ATOM   851  C  CD    . GLU A 1 107 ? 15.43208  2.47315   -25.03895 1.000 25.49024 ? 107 GLU A CD    1 
ATOM   852  O  OE1   . GLU A 1 107 ? 14.21608  2.38722   -25.30895 1.000 22.12580 ? 107 GLU A OE1   1 
ATOM   853  O  OE2   . GLU A 1 107 ? 15.89508  2.24110   -23.90196 1.000 30.86684 ? 107 GLU A OE2   1 
ATOM   854  N  N     . PRO A 1 108 ? 15.24221  5.32928   -29.81888 1.000 22.81277 ? 108 PRO A N     1 
ATOM   855  C  CA    . PRO A 1 108 ? 14.69926  6.41232   -30.66386 1.000 23.89434 ? 108 PRO A CA    1 
ATOM   856  C  C     . PRO A 1 108 ? 14.05032  7.53634   -29.87283 1.000 23.72577 ? 108 PRO A C     1 
ATOM   857  O  O     . PRO A 1 108 ? 14.36938  8.71133   -30.09780 1.000 22.73221 ? 108 PRO A O     1 
ATOM   858  C  CB    . PRO A 1 108 ? 13.69022  5.67840   -31.55987 1.000 28.44917 ? 108 PRO A CB    1 
ATOM   859  C  CG    . PRO A 1 108 ? 14.19015  4.27337   -31.61491 1.000 26.31008 ? 108 PRO A CG    1 
ATOM   860  C  CD    . PRO A 1 108 ? 14.77314  4.00131   -30.25291 1.000 26.45478 ? 108 PRO A CD    1 
ATOM   861  N  N     . TYR A 1 109 ? 13.14631  7.20936   -28.94383 1.000 25.30064 ? 109 TYR A N     1 
ATOM   862  C  CA    . TYR A 1 109 ? 12.54336  8.24637   -28.11281 1.000 25.67180 ? 109 TYR A CA    1 
ATOM   863  C  C     . TYR A 1 109 ? 13.58640  8.95730   -27.26079 1.000 23.34039 ? 109 TYR A C     1 
ATOM   864  O  O     . TYR A 1 109 ? 13.45247  10.15630  -26.98976 1.000 23.92550 ? 109 TYR A O     1 
ATOM   865  C  CB    . TYR A 1 109 ? 11.44334  7.65241   -27.23381 1.000 22.35316 ? 109 TYR A CB    1 
ATOM   866  C  CG    . TYR A 1 109 ? 10.92339  8.60741   -26.17979 1.000 32.75806 ? 109 TYR A CG    1 
ATOM   867  C  CD1   . TYR A 1 109 ? 10.17645  9.72646   -26.53176 1.000 33.70830 ? 109 TYR A CD1   1 
ATOM   868  C  CD2   . TYR A 1 109 ? 11.17838  8.38937   -24.83280 1.000 28.64869 ? 109 TYR A CD2   1 
ATOM   869  C  CE1   . TYR A 1 109 ? 9.70449   10.60346  -25.57074 1.000 34.31013 ? 109 TYR A CE1   1 
ATOM   870  C  CE2   . TYR A 1 109 ? 10.70943  9.25737   -23.86577 1.000 29.00991 ? 109 TYR A CE2   1 
ATOM   871  C  CZ    . TYR A 1 109 ? 9.97349   10.36241  -24.23875 1.000 34.87628 ? 109 TYR A CZ    1 
ATOM   872  O  OH    . TYR A 1 109 ? 9.50553   11.22941  -23.27572 1.000 40.16860 ? 109 TYR A OH    1 
ATOM   873  N  N     . ALA A 1 110 ? 14.63637  8.24724   -26.84281 1.000 23.90325 ? 110 ALA A N     1 
ATOM   874  C  CA    . ALA A 1 110 ? 15.68140  8.88817   -26.05080 1.000 19.97251 ? 110 ALA A CA    1 
ATOM   875  C  C     . ALA A 1 110 ? 16.41945  9.94415   -26.86478 1.000 21.65352 ? 110 ALA A C     1 
ATOM   876  O  O     . ALA A 1 110 ? 16.70551  11.03812  -26.36076 1.000 19.49119 ? 110 ALA A O     1 
ATOM   877  C  CB    . ALA A 1 110 ? 16.65635  7.84210   -25.51483 1.000 16.54435 ? 110 ALA A CB    1 
ATOM   878  N  N     . LYS A 1 111 ? 16.72443  9.64316   -28.13079 1.000 20.80428 ? 111 LYS A N     1 
ATOM   879  C  CA    . LYS A 1 111 ? 17.43148  10.61315  -28.96377 1.000 23.29864 ? 111 LYS A CA    1 
ATOM   880  C  C     . LYS A 1 111 ? 16.58854  11.86319  -29.19274 1.000 22.37512 ? 111 LYS A C     1 
ATOM   881  O  O     . LYS A 1 111 ? 17.10460  12.98717  -29.14971 1.000 20.48593 ? 111 LYS A O     1 
ATOM   882  C  CB    . LYS A 1 111 ? 17.82344  9.98116   -30.29879 1.000 21.19808 ? 111 LYS A CB    1 
ATOM   883  C  CG    . LYS A 1 111 ? 18.81039  8.82811   -30.18882 1.000 24.95536 ? 111 LYS A CG    1 
ATOM   884  C  CD    . LYS A 1 111 ? 19.25936  8.36512   -31.56883 1.000 21.12798 ? 111 LYS A CD    1 
ATOM   885  C  CE    . LYS A 1 111 ? 20.17730  7.15807   -31.47986 1.000 19.99577 ? 111 LYS A CE    1 
ATOM   886  N  NZ    . LYS A 1 111 ? 20.58627  6.68408   -32.83087 1.000 16.14082 ? 111 LYS A NZ    1 
ATOM   887  N  N     . VAL A 1 112 ? 15.28953  11.68727  -29.43773 1.000 16.26718 ? 112 VAL A N     1 
ATOM   888  C  CA    . VAL A 1 112 ? 14.40659  12.83631  -29.60370 1.000 17.80000 ? 112 VAL A CA    1 
ATOM   889  C  C     . VAL A 1 112 ? 14.29363  13.61029  -28.29569 1.000 17.01963 ? 112 VAL A C     1 
ATOM   890  O  O     . VAL A 1 112 ? 14.27070  14.84629  -28.28766 1.000 20.50257 ? 112 VAL A O     1 
ATOM   891  C  CB    . VAL A 1 112 ? 13.03056  12.37240  -30.11871 1.000 19.40979 ? 112 VAL A CB    1 
ATOM   892  C  CG1   . VAL A 1 112 ? 12.07862  13.54845  -30.26068 1.000 22.95731 ? 112 VAL A CG1   1 
ATOM   893  C  CG2   . VAL A 1 112 ? 13.17752  11.63842  -31.44473 1.000 27.05297 ? 112 VAL A CG2   1 
ATOM   894  N  N     . ARG A 1 113 ? 14.23803  12.89558  -27.17018 1.000 20.38030 ? 113 ARG A N     1 
ATOM   895  C  CA    . ARG A 1 113 ? 14.09742  13.54532  -25.87095 1.000 18.40802 ? 113 ARG A CA    1 
ATOM   896  C  C     . ARG A 1 113 ? 15.37846  14.26010  -25.46235 1.000 17.40598 ? 113 ARG A C     1 
ATOM   897  O  O     . ARG A 1 113 ? 15.35038  15.44000  -25.09526 1.000 20.32803 ? 113 ARG A O     1 
ATOM   898  C  CB    . ARG A 1 113 ? 13.70470  12.51284  -24.81746 1.000 19.31886 ? 113 ARG A CB    1 
ATOM   899  C  CG    . ARG A 1 113 ? 13.72732  13.02714  -23.39013 1.000 17.14361 ? 113 ARG A CG    1 
ATOM   900  C  CD    . ARG A 1 113 ? 13.83504  11.87198  -22.41441 1.000 17.77851 ? 113 ARG A CD    1 
ATOM   901  N  NE    . ARG A 1 113 ? 15.07620  11.13207  -22.60912 1.000 17.83190 ? 113 ARG A NE    1 
ATOM   902  C  CZ    . ARG A 1 113 ? 15.31134  9.91791   -22.13126 1.000 13.23866 ? 113 ARG A CZ    1 
ATOM   903  N  NH1   . ARG A 1 113 ? 14.40624  9.26662   -21.42005 1.000 17.32554 ? 113 ARG A NH1   1 
ATOM   904  N  NH2   . ARG A 1 113 ? 16.48130  9.33837   -22.38129 1.000 14.23605 ? 113 ARG A NH2   1 
ATOM   905  N  N     . ASP A 1 114 ? 16.51664  13.55911  -25.51870 1.000 13.90660 ? 114 ASP A N     1 
ATOM   906  C  CA    . ASP A 1 114 ? 17.77267  14.14404  -25.05769 1.000 16.87216 ? 114 ASP A CA    1 
ATOM   907  C  C     . ASP A 1 114 ? 18.17373  15.35204  -25.89366 1.000 17.97312 ? 114 ASP A C     1 
ATOM   908  O  O     . ASP A 1 114 ? 18.83778  16.26499  -25.38764 1.000 20.20528 ? 114 ASP A O     1 
ATOM   909  C  CB    . ASP A 1 114 ? 18.88562  13.09498  -25.07872 1.000 16.97193 ? 114 ASP A CB    1 
ATOM   910  C  CG    . ASP A 1 114 ? 18.59357  11.91097  -24.17374 1.000 12.78724 ? 114 ASP A CG    1 
ATOM   911  O  OD1   . ASP A 1 114 ? 17.72957  12.03300  -23.27674 1.000 14.18814 ? 114 ASP A OD1   1 
ATOM   912  O  OD2   . ASP A 1 114 ? 19.23151  10.85595  -24.35577 1.000 12.67298 ? 114 ASP A OD2   1 
ATOM   913  N  N     . ALA A 1 115 ? 17.78073  15.38309  -27.16666 1.000 17.84141 ? 115 ALA A N     1 
ATOM   914  C  CA    . ALA A 1 115 ? 18.11678  16.52609  -28.00863 1.000 18.62524 ? 115 ALA A CA    1 
ATOM   915  C  C     . ALA A 1 115 ? 17.46285  17.79911  -27.48260 1.000 19.72843 ? 115 ALA A C     1 
ATOM   916  O  O     . ALA A 1 115 ? 18.13490  18.81207  -27.25758 1.000 25.39283 ? 115 ALA A O     1 
ATOM   917  C  CB    . ALA A 1 115 ? 17.70376  16.25514  -29.45464 1.000 18.03557 ? 115 ALA A CB    1 
ATOM   918  N  N     . ALA A 1 116 ? 16.14585  17.76317  -27.26559 1.000 13.93986 ? 116 ALA A N     1 
ATOM   919  C  CA    . ALA A 1 116 ? 15.45191  18.95019  -26.77456 1.000 19.05046 ? 116 ALA A CA    1 
ATOM   920  C  C     . ALA A 1 116 ? 15.97494  19.37514  -25.40756 1.000 17.04642 ? 116 ALA A C     1 
ATOM   921  O  O     . ALA A 1 116 ? 16.07600  20.57412  -25.12453 1.000 11.56563 ? 116 ALA A O     1 
ATOM   922  C  CB    . ALA A 1 116 ? 13.94490  18.69927  -26.72256 1.000 22.99015 ? 116 ALA A CB    1 
ATOM   923  N  N     . VAL A 1 117 ? 16.31889  18.40810  -24.54958 1.000 14.38726 ? 117 VAL A N     1 
ATOM   924  C  CA    . VAL A 1 117 ? 16.86691  18.72804  -23.23057 1.000 16.09217 ? 117 VAL A CA    1 
ATOM   925  C  C     . VAL A 1 117 ? 18.19495  19.46798  -23.36156 1.000 17.20573 ? 117 VAL A C     1 
ATOM   926  O  O     . VAL A 1 117 ? 18.47500  20.41294  -22.61154 1.000 16.24787 ? 117 VAL A O     1 
ATOM   927  C  CB    . VAL A 1 117 ? 17.01785  17.44401  -22.39061 1.000 18.12971 ? 117 VAL A CB    1 
ATOM   928  C  CG1   . VAL A 1 117 ? 17.78487  17.72394  -21.10460 1.000 13.74163 ? 117 VAL A CG1   1 
ATOM   929  C  CG2   . VAL A 1 117 ? 15.65582  16.84107  -22.07861 1.000 12.56133 ? 117 VAL A CG2   1 
ATOM   930  N  N     . ARG A 1 118 ? 19.02888  19.05807  -24.32113 1.000 14.95528 ? 118 ARG A N     1 
ATOM   931  C  CA    . ARG A 1 118 ? 20.29992  19.74479  -24.54201 1.000 17.75056 ? 118 ARG A CA    1 
ATOM   932  C  C     . ARG A 1 118 ? 20.08216  21.16874  -25.03536 1.000 14.09178 ? 118 ARG A C     1 
ATOM   933  O  O     . ARG A 1 118 ? 20.77731  22.09902  -24.61155 1.000 12.11350 ? 118 ARG A O     1 
ATOM   934  C  CB    . ARG A 1 118 ? 21.15912  18.96794  -25.53828 1.000 18.56404 ? 118 ARG A CB    1 
ATOM   935  C  CG    . ARG A 1 118 ? 21.81685  17.73545  -24.96503 1.000 18.96393 ? 118 ARG A CG    1 
ATOM   936  C  CD    . ARG A 1 118 ? 22.92717  17.24504  -25.87362 1.000 18.58230 ? 118 ARG A CD    1 
ATOM   937  N  NE    . ARG A 1 118 ? 23.24590  15.84779  -25.61056 1.000 17.65984 ? 118 ARG A NE    1 
ATOM   938  C  CZ    . ARG A 1 118 ? 22.54790  14.82463  -26.08369 1.000 27.03672 ? 118 ARG A CZ    1 
ATOM   939  N  NH1   . ARG A 1 118 ? 21.47982  15.00983  -26.84118 1.000 27.42822 ? 118 ARG A NH1   1 
ATOM   940  N  NH2   . ARG A 1 118 ? 22.92911  13.58500  -25.78719 1.000 28.74971 ? 118 ARG A NH2   1 
ATOM   941  N  N     . ARG A 1 119 ? 19.13044  21.35226  -25.95096 1.000 17.06603 ? 119 ARG A N     1 
ATOM   942  C  CA    . ARG A 1 119 ? 18.84283  22.68792  -26.45300 1.000 14.17016 ? 119 ARG A CA    1 
ATOM   943  C  C     . ARG A 1 119 ? 18.30413  23.57797  -25.34301 1.000 17.77679 ? 119 ARG A C     1 
ATOM   944  O  O     . ARG A 1 119 ? 18.61989  24.77131  -25.28836 1.000 19.48785 ? 119 ARG A O     1 
ATOM   945  C  CB    . ARG A 1 119 ? 17.85644  22.60771  -27.61700 1.000 17.07296 ? 119 ARG A CB    1 
ATOM   946  C  CG    . ARG A 1 119 ? 18.34979  21.77095  -28.79377 0.000 17.75477 ? 119 ARG A CG    1 
ATOM   947  C  CD    . ARG A 1 119 ? 17.48144  21.96540  -30.02875 0.000 19.27396 ? 119 ARG A CD    1 
ATOM   948  N  NE    . ARG A 1 119 ? 16.09552  21.57559  -29.79826 0.000 19.20242 ? 119 ARG A NE    1 
ATOM   949  C  CZ    . ARG A 1 119 ? 15.60350  20.37074  -30.05255 0.000 19.57180 ? 119 ARG A CZ    1 
ATOM   950  N  NH1   . ARG A 1 119 ? 16.36108  19.40452  -30.54494 0.000 19.85080 ? 119 ARG A NH1   1 
ATOM   951  N  NH2   . ARG A 1 119 ? 14.31858  20.12957  -29.80791 0.000 19.93548 ? 119 ARG A NH2   1 
ATOM   952  N  N     . LEU A 1 120 ? 17.50113  23.01104  -24.44048 1.000 12.97582 ? 120 LEU A N     1 
ATOM   953  C  CA    . LEU A 1 120 ? 17.03417  23.77203  -23.28746 1.000 17.17958 ? 120 LEU A CA    1 
ATOM   954  C  C     . LEU A 1 120 ? 18.17219  24.09695  -22.33045 1.000 15.46778 ? 120 LEU A C     1 
ATOM   955  O  O     . LEU A 1 120 ? 18.14324  25.13994  -21.66843 1.000 14.58123 ? 120 LEU A O     1 
ATOM   956  C  CB    . LEU A 1 120 ? 15.93513  23.00007  -22.55547 1.000 17.10880 ? 120 LEU A CB    1 
ATOM   957  C  CG    . LEU A 1 120 ? 14.59012  22.85516  -23.27147 1.000 11.13306 ? 120 LEU A CG    1 
ATOM   958  C  CD1   . LEU A 1 120 ? 13.69307  21.84718  -22.56649 1.000 14.90653 ? 120 LEU A CD1   1 
ATOM   959  C  CD2   . LEU A 1 120 ? 13.90319  24.20319  -23.37443 1.000 12.40932 ? 120 LEU A CD2   1 
ATOM   960  N  N     . ALA A 1 121 ? 19.17714  23.22290  -22.23948 1.000 12.48277 ? 121 ALA A N     1 
ATOM   961  C  CA    . ALA A 1 121 ? 20.29516  23.48882  -21.34048 1.000 16.33290 ? 121 ALA A CA    1 
ATOM   962  C  C     . ALA A 1 121 ? 21.22021  24.55979  -21.90545 1.000 15.90182 ? 121 ALA A C     1 
ATOM   963  O  O     . ALA A 1 121 ? 21.71426  25.41375  -21.15944 1.000 14.87418 ? 121 ALA A O     1 
ATOM   964  C  CB    . ALA A 1 121 ? 21.06910  22.19978  -21.06551 1.000 15.22001 ? 121 ALA A CB    1 
ATOM   965  N  N     . ALA A 1 122 ? 21.47321  24.52981  -23.21746 1.000 16.39935 ? 122 ALA A N     1 
ATOM   966  C  CA    . ALA A 1 122 ? 22.31726  25.55378  -23.82344 1.000 15.54346 ? 122 ALA A CA    1 
ATOM   967  C  C     . ALA A 1 122 ? 21.68933  26.93781  -23.70740 1.000 18.26852 ? 122 ALA A C     1 
ATOM   968  O  O     . ALA A 1 122 ? 22.40938  27.94177  -23.64638 1.000 16.31070 ? 122 ALA A O     1 
ATOM   969  C  CB    . ALA A 1 122 ? 22.59323  25.21180  -25.28844 1.000 17.65710 ? 122 ALA A CB    1 
ATOM   970  N  N     . GLU A 1 123 ? 20.35533  27.01587  -23.67039 1.000 19.59157 ? 123 GLU A N     1 
ATOM   971  C  CA    . GLU A 1 123 ? 19.69640  28.30090  -23.45336 1.000 17.56243 ? 123 GLU A CA    1 
ATOM   972  C  C     . GLU A 1 123 ? 19.94343  28.81586  -22.04135 1.000 18.00355 ? 123 GLU A C     1 
ATOM   973  O  O     . GLU A 1 123 ? 20.12149  30.02184  -21.83632 1.000 20.11174 ? 123 GLU A O     1 
ATOM   974  C  CB    . GLU A 1 123 ? 18.19439  28.18098  -23.71336 1.000 18.58358 ? 123 GLU A CB    1 
ATOM   975  C  CG    . GLU A 1 123 ? 17.82737  27.88704  -25.15536 1.000 19.65538 ? 123 GLU A CG    1 
ATOM   976  C  CD    . GLU A 1 123 ? 16.32837  27.82412  -25.37536 1.000 15.82287 ? 123 GLU A CD    1 
ATOM   977  O  OE1   . GLU A 1 123 ? 15.57237  27.93113  -24.38535 1.000 17.52094 ? 123 GLU A OE1   1 
ATOM   978  O  OE2   . GLU A 1 123 ? 15.90735  27.66717  -26.53936 1.000 18.15866 ? 123 GLU A OE2   1 
ATOM   979  N  N     . ALA A 1 124 ? 19.94839  27.92283  -21.05537 1.000 16.50495 ? 124 ALA A N     1 
ATOM   980  C  CA    . ALA A 1 124 ? 20.15741  28.31779  -19.67036 1.000 20.27738 ? 124 ALA A CA    1 
ATOM   981  C  C     . ALA A 1 124 ? 21.62942  28.41471  -19.29536 1.000 17.62404 ? 124 ALA A C     1 
ATOM   982  O  O     . ALA A 1 124 ? 21.93744  28.68166  -18.12836 1.000 19.94615 ? 124 ALA A O     1 
ATOM   983  C  CB    . ALA A 1 124 ? 19.44737  27.33780  -18.73238 1.000 16.41186 ? 124 ALA A CB    1 
ATOM   984  N  N     . GLY A 1 125 ? 22.53941  28.22168  -20.24837 1.000 15.61164 ? 125 GLY A N     1 
ATOM   985  C  CA    . GLY A 1 125 ? 23.95241  28.23460  -19.93638 1.000 18.14838 ? 125 GLY A CA    1 
ATOM   986  C  C     . GLY A 1 125 ? 24.43635  27.02156  -19.18241 1.000 17.64489 ? 125 GLY A C     1 
ATOM   987  O  O     . GLY A 1 125 ? 25.46036  27.09349  -18.49941 1.000 18.54300 ? 125 GLY A O     1 
ATOM   988  N  N     . VAL A 1 126 ? 23.72729  25.90260  -19.29243 1.000 18.89614 ? 126 VAL A N     1 
ATOM   989  C  CA    . VAL A 1 126 ? 24.04623  24.67457  -18.57246 1.000 13.76267 ? 126 VAL A CA    1 
ATOM   990  C  C     . VAL A 1 126 ? 24.88518  23.77755  -19.47249 1.000 13.87204 ? 126 VAL A C     1 
ATOM   991  O  O     . VAL A 1 126 ? 24.49116  23.48159  -20.60649 1.000 13.26445 ? 126 VAL A O     1 
ATOM   992  C  CB    . VAL A 1 126 ? 22.76820  23.94662  -18.11747 1.000 12.30103 ? 126 VAL A CB    1 
ATOM   993  C  CG1   . VAL A 1 126 ? 23.11413  22.64959  -17.39551 1.000 11.21743 ? 126 VAL A CG1   1 
ATOM   994  C  CG2   . VAL A 1 126 ? 21.92625  24.85664  -17.23445 1.000 14.19632 ? 126 VAL A CG2   1 
ATOM   995  N  N     . GLU A 1 127 ? 26.03416  23.33848  -18.96450 1.000 15.56724 ? 127 GLU A N     1 
ATOM   996  C  CA    . GLU A 1 127 ? 26.86411  22.36545  -19.66353 1.000 13.76413 ? 127 GLU A CA    1 
ATOM   997  C  C     . GLU A 1 127 ? 26.25804  20.97148  -19.55556 1.000 12.20464 ? 127 GLU A C     1 
ATOM   998  O  O     . GLU A 1 127 ? 25.75103  20.57948  -18.50157 1.000 14.32512 ? 127 GLU A O     1 
ATOM   999  C  CB    . GLU A 1 127 ? 28.28011  22.37036  -19.08453 1.000 14.12595 ? 127 GLU A CB    1 
ATOM   1000 C  CG    . GLU A 1 127 ? 29.19706  21.28233  -19.62156 1.000 15.83093 ? 127 GLU A CG    1 
ATOM   1001 C  CD    . GLU A 1 127 ? 30.48905  21.16525  -18.82457 1.000 19.43755 ? 127 GLU A CD    1 
ATOM   1002 O  OE1   . GLU A 1 127 ? 30.73210  22.02421  -17.95055 1.000 20.29027 ? 127 GLU A OE1   1 
ATOM   1003 O  OE2   . GLU A 1 127 ? 31.26001  20.21321  -19.06560 1.000 21.42483 ? 127 GLU A OE2   1 
ATOM   1004 N  N     . VAL A 1 128 ? 26.31900  20.22150  -20.65158 1.000 13.89995 ? 128 VAL A N     1 
ATOM   1005 C  CA    . VAL A 1 128 ? 25.76693  18.87353  -20.72461 1.000 12.26009 ? 128 VAL A CA    1 
ATOM   1006 C  C     . VAL A 1 128 ? 26.91588  17.88948  -20.87163 1.000 9.84854  ? 128 VAL A C     1 
ATOM   1007 O  O     . VAL A 1 128 ? 27.74988  18.02945  -21.77463 1.000 7.39934  ? 128 VAL A O     1 
ATOM   1008 C  CB    . VAL A 1 128 ? 24.77392  18.73361  -21.89061 1.000 14.40815 ? 128 VAL A CB    1 
ATOM   1009 C  CG1   . VAL A 1 128 ? 24.23585  17.30764  -21.95964 1.000 14.83442 ? 128 VAL A CG1   1 
ATOM   1010 C  CG2   . VAL A 1 128 ? 23.64097  19.72666  -21.73758 1.000 11.98435 ? 128 VAL A CG2   1 
ATOM   1011 N  N     . VAL A 1 129 ? 26.96283  16.90345  -19.98066 1.000 10.27758 ? 129 VAL A N     1 
ATOM   1012 C  CA    . VAL A 1 129 ? 27.98378  15.86340  -19.99269 1.000 10.10700 ? 129 VAL A CA    1 
ATOM   1013 C  C     . VAL A 1 129 ? 27.26771  14.52344  -20.06371 1.000 10.77472 ? 129 VAL A C     1 
ATOM   1014 O  O     . VAL A 1 129 ? 26.46270  14.19946  -19.18172 1.000 9.23821  ? 129 VAL A O     1 
ATOM   1015 C  CB    . VAL A 1 129 ? 28.89079  15.93633  -18.75469 1.000 8.20992  ? 129 VAL A CB    1 
ATOM   1016 C  CG1   . VAL A 1 129 ? 29.86373  14.76428  -18.73672 1.000 17.06028 ? 129 VAL A CG1   1 
ATOM   1017 C  CG2   . VAL A 1 129 ? 29.63686  17.25529  -18.71866 1.000 13.48528 ? 129 VAL A CG2   1 
ATOM   1018 N  N     . THR A 1 130 ? 27.55367  13.74745  -21.10873 1.000 10.40985 ? 130 THR A N     1 
ATOM   1019 C  CA    . THR A 1 130 ? 26.85761  12.48849  -21.37676 1.000 10.51333 ? 130 THR A CA    1 
ATOM   1020 C  C     . THR A 1 130 ? 27.86855  11.39045  -21.67079 1.000 8.35618  ? 130 THR A C     1 
ATOM   1021 O  O     . THR A 1 130 ? 28.18053  11.11346  -22.83880 1.000 6.87687  ? 130 THR A O     1 
ATOM   1022 C  CB    . THR A 1 130 ? 25.88161  12.63157  -22.54475 1.000 7.43477  ? 130 THR A CB    1 
ATOM   1023 O  OG1   . THR A 1 130 ? 26.60662  12.97956  -23.72875 1.000 10.27111 ? 130 THR A OG1   1 
ATOM   1024 C  CG2   . THR A 1 130 ? 24.85666  13.70761  -22.25872 1.000 13.19021 ? 130 THR A CG2   1 
ATOM   1025 N  N     . PRO A 1 131 ? 28.39252  10.73340  -20.64181 1.000 9.44556  ? 131 PRO A N     1 
ATOM   1026 C  CA    . PRO A 1 131 ? 29.31846  9.62335   -20.86884 1.000 9.19165  ? 131 PRO A CA    1 
ATOM   1027 C  C     . PRO A 1 131 ? 28.58340  8.36340   -21.29787 1.000 6.38365  ? 131 PRO A C     1 
ATOM   1028 O  O     . PRO A 1 131 ? 27.37739  8.20846   -21.09986 1.000 6.38477  ? 131 PRO A O     1 
ATOM   1029 C  CB    . PRO A 1 131 ? 29.98346  9.43329   -19.50285 1.000 8.63884  ? 131 PRO A CB    1 
ATOM   1030 C  CG    . PRO A 1 131 ? 28.95348  9.87032   -18.54283 1.000 7.43787  ? 131 PRO A CG    1 
ATOM   1031 C  CD    . PRO A 1 131 ? 28.20354  11.00237  -19.20680 1.000 6.85843  ? 131 PRO A CD    1 
ATOM   1032 N  N     . ILE A 1 132 ? 29.34735  7.45638   -21.90089 1.000 9.18029  ? 132 ILE A N     1 
ATOM   1033 C  CA    . ILE A 1 132 ? 28.84228  6.16841   -22.35992 1.000 8.87663  ? 132 ILE A CA    1 
ATOM   1034 C  C     . ILE A 1 132 ? 29.16523  5.12537   -21.29794 1.000 9.53685  ? 132 ILE A C     1 
ATOM   1035 O  O     . ILE A 1 132 ? 30.33722  4.90130   -20.96795 1.000 8.19884  ? 132 ILE A O     1 
ATOM   1036 C  CB    . ILE A 1 132 ? 29.44826  5.78641   -23.71993 1.000 8.85902  ? 132 ILE A CB    1 
ATOM   1037 C  CG1   . ILE A 1 132 ? 28.92730  6.72447   -24.81091 1.000 7.51009  ? 132 ILE A CG1   1 
ATOM   1038 C  CG2   . ILE A 1 132 ? 29.13918  4.33744   -24.05796 1.000 8.75399  ? 132 ILE A CG2   1 
ATOM   1039 C  CD1   . ILE A 1 132 ? 29.73329  6.68046   -26.08591 1.000 8.78801  ? 132 ILE A CD1   1 
ATOM   1040 N  N     . SER A 1 133 ? 28.12420  4.48741   -20.76196 1.000 6.09599  ? 133 SER A N     1 
ATOM   1041 C  CA    . SER A 1 133 ? 28.29416  3.53838   -19.66998 1.000 7.18148  ? 133 SER A CA    1 
ATOM   1042 C  C     . SER A 1 133 ? 27.21410  2.46243   -19.66100 1.000 7.22533  ? 133 SER A C     1 
ATOM   1043 O  O     . SER A 1 133 ? 27.32606  1.48141   -18.92102 1.000 6.89308  ? 133 SER A O     1 
ATOM   1044 C  CB    . SER A 1 133 ? 28.30020  4.27435   -18.32996 1.000 7.12075  ? 133 SER A CB    1 
ATOM   1045 O  OG    . SER A 1 133 ? 27.39726  5.36339   -18.35993 1.000 8.72472  ? 133 SER A OG    1 
ATOM   1046 N  N     . HIS A 1 134 ? 26.16211  2.62950   -20.46099 1.000 6.11221  ? 134 HIS A N     1 
ATOM   1047 C  CA    . HIS A 1 134 ? 25.12706  1.60256   -20.51301 1.000 6.13465  ? 134 HIS A CA    1 
ATOM   1048 C  C     . HIS A 1 134 ? 25.58699  0.37855   -21.29504 1.000 5.97935  ? 134 HIS A C     1 
ATOM   1049 O  O     . HIS A 1 134 ? 25.18494  -0.74543  -20.97407 1.000 5.94503  ? 134 HIS A O     1 
ATOM   1050 C  CB    . HIS A 1 134 ? 23.84208  2.17664   -21.11599 1.000 5.97531  ? 134 HIS A CB    1 
ATOM   1051 C  CG    . HIS A 1 134 ? 22.72303  1.18570   -21.21001 1.000 10.30445 ? 134 HIS A CG    1 
ATOM   1052 N  ND1   . HIS A 1 134 ? 22.16001  0.58770   -20.10302 1.000 8.62451  ? 134 HIS A ND1   1 
ATOM   1053 C  CD2   . HIS A 1 134 ? 22.06500  0.68475   -22.28202 1.000 8.68990  ? 134 HIS A CD2   1 
ATOM   1054 C  CE1   . HIS A 1 134 ? 21.19897  -0.23324  -20.48804 1.000 7.92337  ? 134 HIS A CE1   1 
ATOM   1055 N  NE2   . HIS A 1 134 ? 21.12396  -0.19621  -21.80604 1.000 8.57481  ? 134 HIS A NE2   1 
ATOM   1056 N  N     . THR A 1 135 ? 26.42500  0.56853   -22.30504 1.000 6.44086  ? 135 THR A N     1 
ATOM   1057 C  CA    . THR A 1 135 ? 26.95094  -0.51547  -23.12107 1.000 8.10480  ? 135 THR A CA    1 
ATOM   1058 C  C     . THR A 1 135 ? 28.42893  -0.71756  -22.80608 1.000 6.29139  ? 135 THR A C     1 
ATOM   1059 O  O     . THR A 1 135 ? 29.02997  0.02540   -22.02606 1.000 6.15907  ? 135 THR A O     1 
ATOM   1060 C  CB    . THR A 1 135 ? 26.74695  -0.23043  -24.61206 1.000 6.37461  ? 135 THR A CB    1 
ATOM   1061 O  OG1   . THR A 1 135 ? 27.33101  1.03655   -24.94703 1.000 6.45378  ? 135 THR A OG1   1 
ATOM   1062 C  CG2   . THR A 1 135 ? 25.26595  -0.21134  -24.95105 1.000 7.77738  ? 135 THR A CG2   1 
ATOM   1063 N  N     . LEU A 1 136 ? 29.01688  -1.74357  -23.42711 1.000 7.88767  ? 136 LEU A N     1 
ATOM   1064 C  CA    . LEU A 1 136 ? 30.42686  -2.03065  -23.18612 1.000 9.07918  ? 136 LEU A CA    1 
ATOM   1065 C  C     . LEU A 1 136 ? 31.32191  -1.01668  -23.88710 1.000 9.10717  ? 136 LEU A C     1 
ATOM   1066 O  O     . LEU A 1 136 ? 32.28594  -0.51674  -23.29609 1.000 10.09493 ? 136 LEU A O     1 
ATOM   1067 C  CB    . LEU A 1 136 ? 30.76679  -3.44965  -23.64115 1.000 7.09037  ? 136 LEU A CB    1 
ATOM   1068 C  CG    . LEU A 1 136 ? 30.24774  -4.58265  -22.75418 1.000 8.13565  ? 136 LEU A CG    1 
ATOM   1069 C  CD1   . LEU A 1 136 ? 30.59067  -5.91465  -23.38521 1.000 6.44364  ? 136 LEU A CD1   1 
ATOM   1070 C  CD2   . LEU A 1 136 ? 30.83075  -4.48171  -21.35318 1.000 7.44558  ? 136 LEU A CD2   1 
ATOM   1071 N  N     . TYR A 1 137 ? 31.01592  -0.69363  -25.14109 1.000 7.26184  ? 137 TYR A N     1 
ATOM   1072 C  CA    . TYR A 1 137 ? 31.82197  0.21635   -25.93707 1.000 8.59051  ? 137 TYR A CA    1 
ATOM   1073 C  C     . TYR A 1 137 ? 30.98302  1.38040   -26.44004 1.000 9.58664  ? 137 TYR A C     1 
ATOM   1074 O  O     . TYR A 1 137 ? 29.75202  1.36446   -26.37504 1.000 8.16886  ? 137 TYR A O     1 
ATOM   1075 C  CB    . TYR A 1 137 ? 32.44393  -0.49866  -27.14409 1.000 8.07647  ? 137 TYR A CB    1 
ATOM   1076 C  CG    . TYR A 1 137 ? 33.28987  -1.70271  -26.81912 1.000 11.98021 ? 137 TYR A CG    1 
ATOM   1077 C  CD1   . TYR A 1 137 ? 32.72080  -2.96368  -26.68615 1.000 11.98531 ? 137 TYR A CD1   1 
ATOM   1078 C  CD2   . TYR A 1 137 ? 34.66587  -1.58478  -26.67312 1.000 12.11783 ? 137 TYR A CD2   1 
ATOM   1079 C  CE1   . TYR A 1 137 ? 33.49975  -4.06873  -26.40318 1.000 10.28112 ? 137 TYR A CE1   1 
ATOM   1080 C  CE2   . TYR A 1 137 ? 35.44782  -2.67983  -26.39015 1.000 11.99944 ? 137 TYR A CE2   1 
ATOM   1081 C  CZ    . TYR A 1 137 ? 34.86176  -3.91780  -26.25618 1.000 10.10532 ? 137 TYR A CZ    1 
ATOM   1082 O  OH    . TYR A 1 137 ? 35.64470  -5.00785  -25.97521 1.000 9.66721  ? 137 TYR A OH    1 
ATOM   1083 N  N     . ASP A 1 138 ? 31.67907  2.40238   -26.93702 1.000 8.22632  ? 138 ASP A N     1 
ATOM   1084 C  CA    . ASP A 1 138 ? 31.05012  3.42643   -27.76099 1.000 12.25020 ? 138 ASP A CA    1 
ATOM   1085 C  C     . ASP A 1 138 ? 30.58008  2.74248   -29.03901 1.000 9.74152  ? 138 ASP A C     1 
ATOM   1086 O  O     . ASP A 1 138 ? 31.38906  2.41846   -29.91502 1.000 10.87815 ? 138 ASP A O     1 
ATOM   1087 C  CB    . ASP A 1 138 ? 32.03018  4.57439   -28.03497 1.000 9.72755  ? 138 ASP A CB    1 
ATOM   1088 C  CG    . ASP A 1 138 ? 31.42323  5.69344   -28.86194 1.000 11.48466 ? 138 ASP A CG    1 
ATOM   1089 O  OD1   . ASP A 1 138 ? 30.24923  5.59251   -29.27694 1.000 11.93524 ? 138 ASP A OD1   1 
ATOM   1090 O  OD2   . ASP A 1 138 ? 32.13828  6.69041   -29.09492 1.000 9.48199  ? 138 ASP A OD2   1 
ATOM   1091 N  N     . THR A 1 139 ? 29.27607  2.48855   -29.14201 1.000 9.43819  ? 139 THR A N     1 
ATOM   1092 C  CA    . THR A 1 139 ? 28.78002  1.70660   -30.26602 1.000 12.38603 ? 139 THR A CA    1 
ATOM   1093 C  C     . THR A 1 139 ? 28.89906  2.46763   -31.57901 1.000 10.12817 ? 139 THR A C     1 
ATOM   1094 O  O     . THR A 1 139 ? 28.99502  1.84865   -32.64502 1.000 12.47895 ? 139 THR A O     1 
ATOM   1095 C  CB    . THR A 1 139 ? 27.33300  1.28967   -30.02503 1.000 11.64587 ? 139 THR A CB    1 
ATOM   1096 O  OG1   . THR A 1 139 ? 26.54906  2.43570   -29.67400 1.000 13.19583 ? 139 THR A OG1   1 
ATOM   1097 C  CG2   . THR A 1 139 ? 27.26596  0.27365   -28.90905 1.000 12.39481 ? 139 THR A CG2   1 
ATOM   1098 N  N     . ASP A 1 140 ? 28.90113  3.80163   -31.52997 1.000 11.87356 ? 140 ASP A N     1 
ATOM   1099 C  CA    . ASP A 1 140 ? 29.21816  4.57164   -32.72796 1.000 11.75223 ? 140 ASP A CA    1 
ATOM   1100 C  C     . ASP A 1 140 ? 30.69015  4.45157   -33.10597 1.000 12.55021 ? 140 ASP A C     1 
ATOM   1101 O  O     . ASP A 1 140 ? 31.03916  4.64458   -34.27596 1.000 12.07925 ? 140 ASP A O     1 
ATOM   1102 C  CB    . ASP A 1 140 ? 28.83024  6.03765   -32.52392 1.000 11.01697 ? 140 ASP A CB    1 
ATOM   1103 C  CG    . ASP A 1 140 ? 27.33125  6.24073   -32.51591 1.000 13.85408 ? 140 ASP A CG    1 
ATOM   1104 O  OD1   . ASP A 1 140 ? 26.63220  5.49278   -33.22893 1.000 16.75667 ? 140 ASP A OD1   1 
ATOM   1105 O  OD2   . ASP A 1 140 ? 26.85029  7.13774   -31.79289 1.000 13.81999 ? 140 ASP A OD2   1 
ATOM   1106 N  N     . MET A 1 141 ? 31.55814  4.12751   -32.14498 1.000 12.13424 ? 141 MET A N     1 
ATOM   1107 C  CA    . MET A 1 141 ? 32.96813  3.91844   -32.45099 1.000 13.44871 ? 141 MET A CA    1 
ATOM   1108 C  C     . MET A 1 141 ? 33.20306  2.56345   -33.10502 1.000 14.39648 ? 141 MET A C     1 
ATOM   1109 O  O     . MET A 1 141 ? 34.06705  2.44242   -33.97903 1.000 15.38890 ? 141 MET A O     1 
ATOM   1110 C  CB    . MET A 1 141 ? 33.80614  4.05437   -31.17699 1.000 16.22759 ? 141 MET A CB    1 
ATOM   1111 C  CG    . MET A 1 141 ? 35.28012  3.71930   -31.34200 1.000 13.07109 ? 141 MET A CG    1 
ATOM   1112 S  SD    . MET A 1 141 ? 35.67204  2.02827   -30.86004 1.000 20.16942 ? 141 MET A SD    1 
ATOM   1113 C  CE    . MET A 1 141 ? 35.38605  2.10524   -29.09404 1.000 7.76646  ? 141 MET A CE    1 
ATOM   1114 N  N     . LEU A 1 142 ? 32.44101  1.54348   -32.70104 1.000 12.10667 ? 142 LEU A N     1 
ATOM   1115 C  CA    . LEU A 1 142 ? 32.52794  0.24549   -33.36007 1.000 12.46115 ? 142 LEU A CA    1 
ATOM   1116 C  C     . LEU A 1 142 ? 32.10294  0.33654   -34.82207 1.000 12.78433 ? 142 LEU A C     1 
ATOM   1117 O  O     . LEU A 1 142 ? 32.69490  -0.31947  -35.68609 1.000 16.01131 ? 142 LEU A O     1 
ATOM   1118 C  CB    . LEU A 1 142 ? 31.67189  -0.77349  -32.61809 1.000 10.60562 ? 142 LEU A CB    1 
ATOM   1119 C  CG    . LEU A 1 142 ? 32.09988  -1.13854  -31.19710 1.000 11.77181 ? 142 LEU A CG    1 
ATOM   1120 C  CD1   . LEU A 1 142 ? 31.10083  -2.10151  -30.59012 1.000 10.33355 ? 142 LEU A CD1   1 
ATOM   1121 C  CD2   . LEU A 1 142 ? 33.49685  -1.73961  -31.19612 1.000 16.33129 ? 142 LEU A CD2   1 
ATOM   1122 N  N     . VAL A 1 143 ? 31.07398  1.13360   -35.11705 1.000 10.89871 ? 143 VAL A N     1 
ATOM   1123 C  CA    . VAL A 1 143 ? 30.62098  1.28366   -36.50004 1.000 12.40501 ? 143 VAL A CA    1 
ATOM   1124 C  C     . VAL A 1 143 ? 31.69901  1.95662   -37.33903 1.000 15.17548 ? 143 VAL A C     1 
ATOM   1125 O  O     . VAL A 1 143 ? 31.98298  1.54163   -38.47004 1.000 20.35969 ? 143 VAL A O     1 
ATOM   1126 C  CB    . VAL A 1 143 ? 29.30002  2.07072   -36.55202 1.000 15.11014 ? 143 VAL A CB    1 
ATOM   1127 C  CG1   . VAL A 1 143 ? 28.90403  2.35078   -37.99501 1.000 18.42109 ? 143 VAL A CG1   1 
ATOM   1128 C  CG2   . VAL A 1 143 ? 28.19898  1.31076   -35.83303 1.000 13.22266 ? 143 VAL A CG2   1 
ATOM   1129 N  N     . ALA A 1 144 ? 32.31606  3.00658   -36.79101 1.000 14.36735 ? 144 ALA A N     1 
ATOM   1130 C  CA    . ALA A 1 144 ? 33.36110  3.71854   -37.51799 1.000 14.57175 ? 144 ALA A CA    1 
ATOM   1131 C  C     . ALA A 1 144 ? 34.60105  2.85348   -37.70502 1.000 17.67649 ? 144 ALA A C     1 
ATOM   1132 O  O     . ALA A 1 144 ? 35.23405  2.89148   -38.76702 1.000 21.18326 ? 144 ALA A O     1 
ATOM   1133 C  CB    . ALA A 1 144 ? 33.71517  5.01351   -36.78996 1.000 17.91726 ? 144 ALA A CB    1 
ATOM   1134 N  N     . ARG A 1 145 ? 34.96146  2.06672   -36.68372 1.000 14.39743 ? 145 ARG A N     1 
ATOM   1135 C  CA    . ARG A 1 145 ? 36.11053  1.17128   -36.78703 1.000 19.69101 ? 145 ARG A CA    1 
ATOM   1136 C  C     . ARG A 1 145 ? 35.90723  0.08906   -37.83463 1.000 20.32708 ? 145 ARG A C     1 
ATOM   1137 O  O     . ARG A 1 145 ? 36.88923  -0.43654  -38.37369 1.000 22.93088 ? 145 ARG A O     1 
ATOM   1138 C  CB    . ARG A 1 145 ? 36.39889  0.51012   -35.43864 1.000 20.41705 ? 145 ARG A CB    1 
ATOM   1139 C  CG    . ARG A 1 145 ? 37.06617  1.41555   -34.42146 1.000 24.69419 ? 145 ARG A CG    1 
ATOM   1140 C  CD    . ARG A 1 145 ? 38.53934  1.06643   -34.20290 1.000 25.21547 ? 145 ARG A CD    1 
ATOM   1141 N  NE    . ARG A 1 145 ? 39.42107  1.69470   -35.17742 1.000 26.86243 ? 145 ARG A NE    1 
ATOM   1142 C  CZ    . ARG A 1 145 ? 40.69481  1.98955   -34.95523 0.000 25.62023 ? 145 ARG A CZ    1 
ATOM   1143 N  NH1   . ARG A 1 145 ? 41.26850  1.75171   -33.78493 0.000 25.99437 ? 145 ARG A NH1   1 
ATOM   1144 N  NH2   . ARG A 1 145 ? 41.40955  2.54292   -35.93000 1.000 26.14434 ? 145 ARG A NH2   1 
ATOM   1145 N  N     . ASN A 1 146 ? 34.66089  -0.25951  -38.12609 1.000 20.68128 ? 146 ASN A N     1 
ATOM   1146 C  CA    . ASN A 1 146 ? 34.34684  -1.31247  -39.08112 1.000 21.19677 ? 146 ASN A CA    1 
ATOM   1147 C  C     . ASN A 1 146 ? 34.17286  -0.77643  -40.49910 1.000 25.62199 ? 146 ASN A C     1 
ATOM   1148 O  O     . ASN A 1 146 ? 33.77082  -1.52639  -41.39512 1.000 34.93998 ? 146 ASN A O     1 
ATOM   1149 C  CB    . ASN A 1 146 ? 33.08680  -2.05842  -38.62913 1.000 20.58855 ? 146 ASN A CB    1 
ATOM   1150 C  CG    . ASN A 1 146 ? 32.89473  -3.38739  -39.34416 1.000 23.79865 ? 146 ASN A CG    1 
ATOM   1151 O  OD1   . ASN A 1 146 ? 33.70169  -4.30644  -39.20318 1.000 26.29110 ? 146 ASN A OD1   1 
ATOM   1152 N  ND2   . ASN A 1 146 ? 31.81372  -3.49532  -40.10816 1.000 17.78841 ? 146 ASN A ND2   1 
ATOM   1153 N  N     . GLY A 1 147 ? 34.46392  0.50456   -40.72507 1.000 24.22375 ? 147 GLY A N     1 
ATOM   1154 C  CA    . GLY A 1 147 ? 34.32095  1.10860   -42.03606 1.000 21.90677 ? 147 GLY A CA    1 
ATOM   1155 C  C     . GLY A 1 147 ? 33.10399  1.99067   -42.21403 1.000 20.08037 ? 147 GLY A C     1 
ATOM   1156 O  O     . GLY A 1 147 ? 32.95702  2.59570   -43.28302 1.000 23.53404 ? 147 GLY A O     1 
ATOM   1157 N  N     . GLY A 1 148 ? 32.23500  2.08469   -41.21403 1.000 20.63658 ? 148 GLY A N     1 
ATOM   1158 C  CA    . GLY A 1 148 ? 31.07304  2.94375   -41.25700 1.000 22.66967 ? 148 GLY A CA    1 
ATOM   1159 C  C     . GLY A 1 148 ? 29.73901  2.22582   -41.35101 1.000 22.81018 ? 148 GLY A C     1 
ATOM   1160 O  O     . GLY A 1 148 ? 28.72904  2.87287   -41.66000 1.000 26.65881 ? 148 GLY A O     1 
ATOM   1161 N  N     . ALA A 1 149 ? 29.70394  0.92181   -41.10505 1.000 16.54814 ? 149 ALA A N     1 
ATOM   1162 C  CA    . ALA A 1 149 ? 28.46690  0.15788   -41.12906 1.000 20.03570 ? 149 ALA A CA    1 
ATOM   1163 C  C     . ALA A 1 149 ? 28.51486  -0.88715  -40.02808 1.000 18.21069 ? 149 ALA A C     1 
ATOM   1164 O  O     . ALA A 1 149 ? 29.58683  -1.37122  -39.65610 1.000 21.11239 ? 149 ALA A O     1 
ATOM   1165 C  CB    . ALA A 1 149 ? 28.23386  -0.51708  -42.48907 1.000 20.49298 ? 149 ALA A CB    1 
ATOM   1166 N  N     . ALA A 1 150 ? 27.33984  -1.23311  -39.51609 1.000 17.15830 ? 150 ALA A N     1 
ATOM   1167 C  CA    . ALA A 1 150 ? 27.27680  -2.19213  -38.42311 1.000 17.48729 ? 150 ALA A CA    1 
ATOM   1168 C  C     . ALA A 1 150 ? 27.48172  -3.61413  -38.94414 1.000 17.76022 ? 150 ALA A C     1 
ATOM   1169 O  O     . ALA A 1 150 ? 26.96170  -3.96708  -40.00415 1.000 18.61642 ? 150 ALA A O     1 
ATOM   1170 C  CB    . ALA A 1 150 ? 25.93680  -2.09608  -37.69810 1.000 17.79951 ? 150 ALA A CB    1 
ATOM   1171 N  N     . PRO A 1 151 ? 28.24368  -4.43918  -38.22717 1.000 19.51731 ? 151 PRO A N     1 
ATOM   1172 C  CA    . PRO A 1 151 ? 28.34561  -5.85318  -38.60320 1.000 16.62677 ? 151 PRO A CA    1 
ATOM   1173 C  C     . PRO A 1 151 ? 27.00658  -6.54312  -38.40421 1.000 17.51348 ? 151 PRO A C     1 
ATOM   1174 O  O     . PRO A 1 151 ? 26.30159  -6.28810  -37.42420 1.000 12.10942 ? 151 PRO A O     1 
ATOM   1175 C  CB    . PRO A 1 151 ? 29.41059  -6.40325  -37.64522 1.000 19.10583 ? 151 PRO A CB    1 
ATOM   1176 C  CG    . PRO A 1 151 ? 30.10465  -5.19930  -37.08519 1.000 17.20700 ? 151 PRO A CG    1 
ATOM   1177 C  CD    . PRO A 1 151 ? 29.08370  -4.11125  -37.06316 1.000 18.15531 ? 151 PRO A CD    1 
ATOM   1178 N  N     . LEU A 1 152 ? 26.64953  -7.41508  -39.34823 1.000 15.95878 ? 152 LEU A N     1 
ATOM   1179 C  CA    . LEU A 1 152 ? 25.34749  -8.07101  -39.33624 1.000 15.41031 ? 152 LEU A CA    1 
ATOM   1180 C  C     . LEU A 1 152 ? 25.40742  -9.53202  -38.91128 1.000 13.81465 ? 152 LEU A C     1 
ATOM   1181 O  O     . LEU A 1 152 ? 24.35739  -10.17797 -38.81329 1.000 14.85226 ? 152 LEU A O     1 
ATOM   1182 C  CB    . LEU A 1 152 ? 24.68449  -7.95694  -40.71724 1.000 20.19678 ? 152 LEU A CB    1 
ATOM   1183 C  CG    . LEU A 1 152 ? 24.37657  -6.52792  -41.17220 1.000 22.58870 ? 152 LEU A CG    1 
ATOM   1184 C  CD1   . LEU A 1 152 ? 23.41656  -6.52484  -42.35620 1.000 21.10936 ? 152 LEU A CD1   1 
ATOM   1185 C  CD2   . LEU A 1 152 ? 23.82261  -5.69892  -40.02118 1.000 20.84934 ? 152 LEU A CD2   1 
ATOM   1186 N  N     . THR A 1 153 ? 26.59640  -10.07009 -38.65329 1.000 14.81729 ? 153 THR A N     1 
ATOM   1187 C  CA    . THR A 1 153 ? 26.74433  -11.41711 -38.12333 1.000 20.10522 ? 153 THR A CA    1 
ATOM   1188 C  C     . THR A 1 153 ? 27.59634  -11.37018 -36.86433 1.000 17.28642 ? 153 THR A C     1 
ATOM   1189 O  O     . THR A 1 153 ? 28.49738  -10.53623 -36.73631 1.000 12.11099 ? 153 THR A O     1 
ATOM   1190 C  CB    . THR A 1 153 ? 27.38828  -12.37612 -39.13735 1.000 17.13317 ? 153 THR A CB    1 
ATOM   1191 O  OG1   . THR A 1 153 ? 28.79029  -12.09819 -39.23335 1.000 16.88396 ? 153 THR A OG1   1 
ATOM   1192 C  CG2   . THR A 1 153 ? 26.74828  -12.21805 -40.51034 1.000 17.66496 ? 153 THR A CG2   1 
ATOM   1193 N  N     . MET A 1 154 ? 27.30030  -12.28019 -35.93135 1.000 13.31789 ? 154 MET A N     1 
ATOM   1194 C  CA    . MET A 1 154 ? 28.05930  -12.33726 -34.68735 1.000 16.12544 ? 154 MET A CA    1 
ATOM   1195 C  C     . MET A 1 154 ? 29.50828  -12.72932 -34.93537 1.000 17.42517 ? 154 MET A C     1 
ATOM   1196 O  O     . MET A 1 154 ? 30.40630  -12.29239 -34.20436 1.000 22.65417 ? 154 MET A O     1 
ATOM   1197 C  CB    . MET A 1 154 ? 27.39425  -13.31525 -33.71537 1.000 14.90305 ? 154 MET A CB    1 
ATOM   1198 C  CG    . MET A 1 154 ? 28.20524  -13.61232 -32.46338 1.000 17.56029 ? 154 MET A CG    1 
ATOM   1199 S  SD    . MET A 1 154 ? 28.69532  -12.13636 -31.54935 1.000 20.92952 ? 154 MET A SD    1 
ATOM   1200 C  CE    . MET A 1 154 ? 27.11035  -11.53730 -30.98233 1.000 11.15604 ? 154 MET A CE    1 
ATOM   1201 N  N     . GLN A 1 155 ? 29.75823  -13.53731 -35.96639 1.000 16.56401 ? 155 GLN A N     1 
ATOM   1202 C  CA    . GLN A 1 155 ? 31.12121  -13.96637 -36.25840 1.000 19.19255 ? 155 GLN A CA    1 
ATOM   1203 C  C     . GLN A 1 155 ? 32.01127  -12.77941 -36.61238 1.000 16.72299 ? 155 GLN A C     1 
ATOM   1204 O  O     . GLN A 1 155 ? 33.16027  -12.70148 -36.16338 1.000 21.14670 ? 155 GLN A O     1 
ATOM   1205 C  CB    . GLN A 1 155 ? 31.10715  -14.99635 -37.38643 1.000 17.01509 ? 155 GLN A CB    1 
ATOM   1206 C  CG    . GLN A 1 155 ? 32.45712  -15.61841 -37.67945 1.000 26.08364 ? 155 GLN A CG    1 
ATOM   1207 C  CD    . GLN A 1 155 ? 32.43704  -17.12841 -37.55848 0.000 22.07217 ? 155 GLN A CD    1 
ATOM   1208 O  OE1   . GLN A 1 155 ? 32.72800  -17.84240 -38.51750 0.000 22.39417 ? 155 GLN A OE1   1 
ATOM   1209 N  NE2   . GLN A 1 155 ? 32.09702  -17.62242 -36.37449 0.000 21.73793 ? 155 GLN A NE2   1 
ATOM   1210 N  N     . SER A 1 156 ? 31.49231  -11.83837 -37.40435 1.000 14.77749 ? 156 SER A N     1 
ATOM   1211 C  CA    . SER A 1 156 ? 32.26737  -10.65440 -37.76233 1.000 18.51498 ? 156 SER A CA    1 
ATOM   1212 C  C     . SER A 1 156 ? 32.30343  -9.62743  -36.63530 1.000 16.15585 ? 156 SER A C     1 
ATOM   1213 O  O     . SER A 1 156 ? 33.30346  -8.91748  -36.48529 1.000 16.41591 ? 156 SER A O     1 
ATOM   1214 C  CB    . SER A 1 156 ? 31.69940  -10.01634 -39.03131 1.000 21.49242 ? 156 SER A CB    1 
ATOM   1215 O  OG    . SER A 1 156 ? 30.37342  -9.56128  -38.82630 1.000 21.27074 ? 156 SER A OG    1 
ATOM   1216 N  N     . PHE A 1 157 ? 31.23243  -9.53439  -35.84330 1.000 16.72607 ? 157 PHE A N     1 
ATOM   1217 C  CA    . PHE A 1 157 ? 31.21849  -8.60242  -34.71828 1.000 15.33990 ? 157 PHE A CA    1 
ATOM   1218 C  C     . PHE A 1 157 ? 32.25247  -8.98649  -33.66829 1.000 15.25016 ? 157 PHE A C     1 
ATOM   1219 O  O     . PHE A 1 157 ? 32.90852  -8.11654  -33.08227 1.000 16.23315 ? 157 PHE A O     1 
ATOM   1220 C  CB    . PHE A 1 157 ? 29.82349  -8.55536  -34.09427 1.000 12.53632 ? 157 PHE A CB    1 
ATOM   1221 C  CG    . PHE A 1 157 ? 29.70554  -7.59838  -32.93725 1.000 14.18465 ? 157 PHE A CG    1 
ATOM   1222 C  CD1   . PHE A 1 157 ? 29.51661  -6.24337  -33.15821 1.000 13.17807 ? 157 PHE A CD1   1 
ATOM   1223 C  CD2   . PHE A 1 157 ? 29.77853  -8.05242  -31.63026 1.000 14.68656 ? 157 PHE A CD2   1 
ATOM   1224 C  CE1   . PHE A 1 157 ? 29.40466  -5.35539  -32.09819 1.000 12.02586 ? 157 PHE A CE1   1 
ATOM   1225 C  CE2   . PHE A 1 157 ? 29.66557  -7.16843  -30.56524 1.000 12.46440 ? 157 PHE A CE2   1 
ATOM   1226 C  CZ    . PHE A 1 157 ? 29.47864  -5.81942  -30.80220 1.000 8.93674  ? 157 PHE A CZ    1 
ATOM   1227 N  N     . THR A 1 158 ? 32.40041  -10.28651 -33.40432 1.000 16.94863 ? 158 THR A N     1 
ATOM   1228 C  CA    . THR A 1 158 ? 33.37239  -10.72558 -32.41033 1.000 18.38628 ? 158 THR A CA    1 
ATOM   1229 C  C     . THR A 1 158 ? 34.79740  -10.48364 -32.88533 1.000 17.49991 ? 158 THR A C     1 
ATOM   1230 O  O     . THR A 1 158 ? 35.68841  -10.22570 -32.06733 1.000 22.33192 ? 158 THR A O     1 
ATOM   1231 C  CB    . THR A 1 158 ? 33.16231  -12.20258 -32.08237 1.000 18.75659 ? 158 THR A CB    1 
ATOM   1232 O  OG1   . THR A 1 158 ? 31.75730  -12.49251 -32.05237 1.000 16.28806 ? 158 THR A OG1   1 
ATOM   1233 C  CG2   . THR A 1 158 ? 33.76730  -12.52664 -30.72438 1.000 15.78895 ? 158 THR A CG2   1 
ATOM   1234 N  N     . LYS A 1 159 ? 35.03139  -10.55762 -34.19734 1.000 16.76753 ? 159 LYS A N     1 
ATOM   1235 C  CA    . LYS A 1 159 ? 36.34540  -10.22067 -34.73233 1.000 20.79898 ? 159 LYS A CA    1 
ATOM   1236 C  C     . LYS A 1 159 ? 36.63748  -8.73369  -34.58830 1.000 18.67951 ? 159 LYS A C     1 
ATOM   1237 O  O     . LYS A 1 159 ? 37.79850  -8.34176  -34.42930 1.000 17.47504 ? 159 LYS A O     1 
ATOM   1238 C  CB    . LYS A 1 159 ? 36.44138  -10.63964 -36.20034 1.000 17.13627 ? 159 LYS A CB    1 
ATOM   1239 C  CG    . LYS A 1 159 ? 36.41730  -12.14564 -36.42438 1.000 20.42925 ? 159 LYS A CG    1 
ATOM   1240 C  CD    . LYS A 1 159 ? 36.55328  -12.48361 -37.90239 0.000 18.62840 ? 159 LYS A CD    1 
ATOM   1241 C  CE    . LYS A 1 159 ? 36.55720  -13.98760 -38.13342 0.000 18.77406 ? 159 LYS A CE    1 
ATOM   1242 N  NZ    . LYS A 1 159 ? 36.66518  -14.32758 -39.58043 0.000 18.14741 ? 159 LYS A NZ    1 
ATOM   1243 N  N     . LEU A 1 160 ? 35.60052  -7.89764  -34.63028 1.000 19.48662 ? 160 LEU A N     1 
ATOM   1244 C  CA    . LEU A 1 160 ? 35.79960  -6.45965  -34.49024 1.000 18.48309 ? 160 LEU A CA    1 
ATOM   1245 C  C     . LEU A 1 160 ? 36.15562  -6.08770  -33.05524 1.000 18.23720 ? 160 LEU A C     1 
ATOM   1246 O  O     . LEU A 1 160 ? 37.06966  -5.29076  -32.81922 1.000 18.85128 ? 160 LEU A O     1 
ATOM   1247 C  CB    . LEU A 1 160 ? 34.54463  -5.71758  -34.94422 1.000 14.67142 ? 160 LEU A CB    1 
ATOM   1248 C  CG    . LEU A 1 160 ? 34.59271  -4.19258  -34.83319 1.000 22.21968 ? 160 LEU A CG    1 
ATOM   1249 C  CD1   . LEU A 1 160 ? 35.60873  -3.62061  -35.80718 1.000 19.24070 ? 160 LEU A CD1   1 
ATOM   1250 C  CD2   . LEU A 1 160 ? 33.21674  -3.58251  -35.06117 1.000 19.14505 ? 160 LEU A CD2   1 
ATOM   1251 N  N     . VAL A 1 161 ? 35.44059  -6.65369  -32.08025 1.000 16.80412 ? 161 VAL A N     1 
ATOM   1252 C  CA    . VAL A 1 161 ? 35.67862  -6.27274  -30.69124 1.000 17.05335 ? 161 VAL A CA    1 
ATOM   1253 C  C     . VAL A 1 161 ? 37.03260  -6.78482  -30.20526 1.000 20.31001 ? 161 VAL A C     1 
ATOM   1254 O  O     . VAL A 1 161 ? 37.64663  -6.17987  -29.31724 1.000 16.64922 ? 161 VAL A O     1 
ATOM   1255 C  CB    . VAL A 1 161 ? 34.51960  -6.75670  -29.79725 1.000 19.20087 ? 161 VAL A CB    1 
ATOM   1256 C  CG1   . VAL A 1 161 ? 33.19363  -6.18862  -30.29723 1.000 15.11146 ? 161 VAL A CG1   1 
ATOM   1257 C  CG2   . VAL A 1 161 ? 34.46552  -8.27270  -29.74728 1.000 17.84514 ? 161 VAL A CG2   1 
ATOM   1258 N  N     . ASP A 1 162 ? 37.53054  -7.88783  -30.77628 1.000 21.10354 ? 162 ASP A N     1 
ATOM   1259 C  CA    . ASP A 1 162 ? 38.85751  -8.36690  -30.40130 1.000 19.24720 ? 162 ASP A CA    1 
ATOM   1260 C  C     . ASP A 1 162 ? 39.94556  -7.44995  -30.93528 1.000 20.41098 ? 162 ASP A C     1 
ATOM   1261 O  O     . ASP A 1 162 ? 40.97957  -7.27401  -30.28228 1.000 17.81396 ? 162 ASP A O     1 
ATOM   1262 C  CB    . ASP A 1 162 ? 39.07044  -9.80190  -30.89134 1.000 21.26674 ? 162 ASP A CB    1 
ATOM   1263 C  CG    . ASP A 1 162 ? 38.19439  -10.81088 -30.15436 1.000 19.75522 ? 162 ASP A CG    1 
ATOM   1264 O  OD1   . ASP A 1 162 ? 37.20942  -10.39184 -29.50534 1.000 19.50085 ? 162 ASP A OD1   1 
ATOM   1265 O  OD2   . ASP A 1 162 ? 38.49333  -12.02289 -30.21439 1.000 26.24623 ? 162 ASP A OD2   1 
ATOM   1266 N  N     A ARG A 1 163 ? 39.74275  -6.87222  -32.12164 0.620 19.56671 ? 163 ARG A N     1 
ATOM   1267 N  N     B ARG A 1 163 ? 39.73177  -6.85805  -32.11341 0.380 19.58273 ? 163 ARG A N     1 
ATOM   1268 C  CA    A ARG A 1 163 ? 40.69268  -5.90242  -32.64998 0.620 20.47622 ? 163 ARG A CA    1 
ATOM   1269 C  CA    B ARG A 1 163 ? 40.68094  -5.90215  -32.66842 0.380 20.47854 ? 163 ARG A CA    1 
ATOM   1270 C  C     A ARG A 1 163 ? 40.52919  -4.52714  -32.01849 0.620 21.46127 ? 163 ARG A C     1 
ATOM   1271 C  C     B ARG A 1 163 ? 40.49447  -4.50079  -32.09870 0.380 21.43712 ? 163 ARG A C     1 
ATOM   1272 O  O     A ARG A 1 163 ? 41.47229  -3.72865  -32.05114 0.620 21.71914 ? 163 ARG A O     1 
ATOM   1273 O  O     B ARG A 1 163 ? 41.38901  -3.66066  -32.24892 0.380 21.61544 ? 163 ARG A O     1 
ATOM   1274 C  CB    A ARG A 1 163 ? 40.55221  -5.78276  -34.16991 0.620 20.68027 ? 163 ARG A CB    1 
ATOM   1275 C  CB    B ARG A 1 163 ? 40.56103  -5.87019  -34.19668 0.380 20.69046 ? 163 ARG A CB    1 
ATOM   1276 C  CG    A ARG A 1 163 ? 40.74413  -7.08479  -34.92873 0.620 19.83089 ? 163 ARG A CG    1 
ATOM   1277 C  CG    B ARG A 1 163 ? 39.71908  -4.72599  -34.74347 0.380 21.88611 ? 163 ARG A CG    1 
ATOM   1278 C  CD    A ARG A 1 163 ? 40.90742  -6.82408  -36.41869 0.620 22.99618 ? 163 ARG A CD    1 
ATOM   1279 C  CD    B ARG A 1 163 ? 39.12577  -5.04054  -36.11229 0.380 21.29202 ? 163 ARG A CD    1 
ATOM   1280 N  NE    A ARG A 1 163 ? 40.13717  -5.66543  -36.85757 0.620 24.73894 ? 163 ARG A NE    1 
ATOM   1281 N  NE    B ARG A 1 163 ? 40.11300  -5.51466  -37.07648 0.380 24.53473 ? 163 ARG A NE    1 
ATOM   1282 C  CZ    A ARG A 1 163 ? 38.95323  -5.72711  -37.45161 0.620 23.70798 ? 163 ARG A CZ    1 
ATOM   1283 C  CZ    B ARG A 1 163 ? 40.21824  -6.77348  -37.48158 0.380 23.10432 ? 163 ARG A CZ    1 
ATOM   1284 N  NH1   A ARG A 1 163 ? 38.36676  -6.88507  -37.70609 0.620 22.95996 ? 163 ARG A NH1   1 
ATOM   1285 N  NH1   B ARG A 1 163 ? 39.42321  -7.71947  -37.00978 0.380 20.89145 ? 163 ARG A NH1   1 
ATOM   1286 N  NH2   A ARG A 1 163 ? 38.34435  -4.59784  -37.80266 0.620 23.02169 ? 163 ARG A NH2   1 
ATOM   1287 N  NH2   B ARG A 1 163 ? 41.14009  -7.09009  -38.38679 0.380 25.36848 ? 163 ARG A NH2   1 
ATOM   1288 N  N     . VAL A 1 164 ? 39.35972  -4.23190  -31.44921 1.000 18.29506 ? 164 VAL A N     1 
ATOM   1289 C  CA    . VAL A 1 164 ? 39.15679  -2.93991  -30.80317 1.000 22.16027 ? 164 VAL A CA    1 
ATOM   1290 C  C     . VAL A 1 164 ? 39.81679  -2.91398  -29.42718 1.000 18.89060 ? 164 VAL A C     1 
ATOM   1291 O  O     . VAL A 1 164 ? 40.35385  -1.88001  -29.01215 1.000 22.35233 ? 164 VAL A O     1 
ATOM   1292 C  CB    . VAL A 1 164 ? 37.64880  -2.62483  -30.72916 1.000 20.25711 ? 164 VAL A CB    1 
ATOM   1293 C  CG1   . VAL A 1 164 ? 37.34286  -1.61285  -29.63214 1.000 20.60259 ? 164 VAL A CG1   1 
ATOM   1294 C  CG2   . VAL A 1 164 ? 37.14982  -2.10978  -32.07315 1.000 23.39671 ? 164 VAL A CG2   1 
ATOM   1295 N  N     . GLY A 1 165 ? 39.80274  -4.03199  -28.71020 1.000 17.10971 ? 165 GLY A N     1 
ATOM   1296 C  CA    . GLY A 1 165 ? 40.45774  -4.15105  -27.42321 1.000 18.83814 ? 165 GLY A CA    1 
ATOM   1297 C  C     . GLY A 1 165 ? 39.47673  -4.46703  -26.30821 1.000 16.56905 ? 165 GLY A C     1 
ATOM   1298 O  O     . GLY A 1 165 ? 38.27872  -4.64597  -26.52021 1.000 13.91102 ? 165 GLY A O     1 
ATOM   1299 N  N     . ASP A 1 166 ? 40.02273  -4.54109  -25.09722 1.000 17.65492 ? 166 ASP A N     1 
ATOM   1300 C  CA    . ASP A 1 166 ? 39.18872  -4.73607  -23.92622 1.000 13.23936 ? 166 ASP A CA    1 
ATOM   1301 C  C     . ASP A 1 166 ? 38.27079  -3.53203  -23.72518 1.000 14.57276 ? 166 ASP A C     1 
ATOM   1302 O  O     . ASP A 1 166 ? 38.63084  -2.40204  -24.06716 1.000 10.32716 ? 166 ASP A O     1 
ATOM   1303 C  CB    . ASP A 1 166 ? 40.04572  -4.94615  -22.68022 1.000 11.48622 ? 166 ASP A CB    1 
ATOM   1304 C  CG    . ASP A 1 166 ? 40.48765  -6.38517  -22.51326 1.000 10.99060 ? 166 ASP A CG    1 
ATOM   1305 O  OD1   . ASP A 1 166 ? 39.69560  -7.29012  -22.84128 1.000 17.39943 ? 166 ASP A OD1   1 
ATOM   1306 O  OD2   . ASP A 1 166 ? 41.62664  -6.61024  -22.05327 1.000 23.74001 ? 166 ASP A OD2   1 
ATOM   1307 N  N     . PRO A 1 167 ? 37.08178  -3.74998  -23.17518 1.000 11.58362 ? 167 PRO A N     1 
ATOM   1308 C  CA    . PRO A 1 167 ? 36.16283  -2.63694  -22.91315 1.000 11.29357 ? 167 PRO A CA    1 
ATOM   1309 C  C     . PRO A 1 167 ? 36.74389  -1.67900  -21.88913 1.000 13.46696 ? 167 PRO A C     1 
ATOM   1310 O  O     . PRO A 1 167 ? 37.63287  -2.05806  -21.11015 1.000 8.93314  ? 167 PRO A O     1 
ATOM   1311 C  CB    . PRO A 1 167 ? 34.90480  -3.33389  -22.37017 1.000 11.25820 ? 167 PRO A CB    1 
ATOM   1312 C  CG    . PRO A 1 167 ? 35.03873  -4.75889  -22.77920 1.000 8.81375  ? 167 PRO A CG    1 
ATOM   1313 C  CD    . PRO A 1 167 ? 36.49871  -5.04996  -22.80721 1.000 8.32755  ? 167 PRO A CD    1 
ATOM   1314 N  N     . PRO A 1 168 ? 36.28595  -0.42397  -21.87410 1.000 9.77143  ? 168 PRO A N     1 
ATOM   1315 C  CA    . PRO A 1 168 ? 36.73100  0.51098   -20.83408 1.000 10.56563 ? 168 PRO A CA    1 
ATOM   1316 C  C     . PRO A 1 168 ? 36.43798  -0.03904  -19.44409 1.000 12.19916 ? 168 PRO A C     1 
ATOM   1317 O  O     . PRO A 1 168 ? 35.37895  -0.61799  -19.19610 1.000 13.78260 ? 168 PRO A O     1 
ATOM   1318 C  CB    . PRO A 1 168 ? 35.92306  1.78103   -21.13105 1.000 10.89962 ? 168 PRO A CB    1 
ATOM   1319 C  CG    . PRO A 1 168 ? 35.65806  1.71107   -22.61005 1.000 8.73876  ? 168 PRO A CG    1 
ATOM   1320 C  CD    . PRO A 1 168 ? 35.46298  0.24009   -22.90208 1.000 11.93329 ? 168 PRO A CD    1 
ATOM   1321 N  N     . ALA A 1 169 ? 37.40499  0.11989   -18.54309 1.000 14.53235 ? 169 ALA A N     1 
ATOM   1322 C  CA    . ALA A 1 169 ? 37.26797  -0.43613  -17.20711 1.000 13.59774 ? 169 ALA A CA    1 
ATOM   1323 C  C     . ALA A 1 169 ? 36.17001  0.29790   -16.43409 1.000 9.86611  ? 169 ALA A C     1 
ATOM   1324 O  O     . ALA A 1 169 ? 35.85407  1.45393   -16.73806 1.000 12.25457 ? 169 ALA A O     1 
ATOM   1325 C  CB    . ALA A 1 169 ? 38.59198  -0.34922  -16.45311 1.000 13.68817 ? 169 ALA A CB    1 
ATOM   1326 N  N     . PRO A 1 170 ? 35.55898  -0.36109  -15.44510 1.000 9.66069  ? 170 PRO A N     1 
ATOM   1327 C  CA    . PRO A 1 170 ? 34.49701  0.29495   -14.67308 1.000 8.02013  ? 170 PRO A CA    1 
ATOM   1328 C  C     . PRO A 1 170 ? 35.03908  1.47490   -13.88305 1.000 11.69374 ? 170 PRO A C     1 
ATOM   1329 O  O     . PRO A 1 170 ? 36.16708  1.44883   -13.39006 1.000 10.18606 ? 170 PRO A O     1 
ATOM   1330 C  CB    . PRO A 1 170 ? 33.98596  -0.82105  -13.75410 1.000 7.47134  ? 170 PRO A CB    1 
ATOM   1331 C  CG    . PRO A 1 170 ? 35.07291  -1.82511  -13.71213 1.000 9.32084  ? 170 PRO A CG    1 
ATOM   1332 C  CD    . PRO A 1 170 ? 35.71791  -1.77511  -15.06313 1.000 9.70912  ? 170 PRO A CD    1 
ATOM   1333 N  N     . ALA A 1 171 ? 34.22213  2.52094   -13.77603 1.000 9.27665  ? 171 ALA A N     1 
ATOM   1334 C  CA    . ALA A 1 171 ? 34.64119  3.71790   -13.07000 1.000 10.81039 ? 171 ALA A CA    1 
ATOM   1335 C  C     . ALA A 1 171 ? 34.64819  3.46386   -11.56001 1.000 12.10170 ? 171 ALA A C     1 
ATOM   1336 O  O     . ALA A 1 171 ? 33.90415  2.61689   -11.06002 1.000 14.70612 ? 171 ALA A O     1 
ATOM   1337 C  CB    . ALA A 1 171 ? 33.71825  4.88596   -13.40897 1.000 12.87537 ? 171 ALA A CB    1 
ATOM   1338 N  N     . PRO A 1 172 ? 35.49023  4.17680   -10.81499 1.000 13.65782 ? 172 PRO A N     1 
ATOM   1339 C  CA    . PRO A 1 172 ? 35.55822  3.95977   -9.36600  1.000 16.73616 ? 172 PRO A CA    1 
ATOM   1340 C  C     . PRO A 1 172 ? 34.26424  4.37582   -8.67998  1.000 14.03025 ? 172 PRO A C     1 
ATOM   1341 O  O     . PRO A 1 172 ? 33.41028  5.07087   -9.23696  1.000 13.23336 ? 172 PRO A O     1 
ATOM   1342 C  CB    . PRO A 1 172 ? 36.73127  4.84070   -8.93298  1.000 14.87225 ? 172 PRO A CB    1 
ATOM   1343 C  CG    . PRO A 1 172 ? 36.82232  5.88672   -9.99196  1.000 13.98405 ? 172 PRO A CG    1 
ATOM   1344 C  CD    . PRO A 1 172 ? 36.43628  5.21077   -11.26697 1.000 11.76310 ? 172 PRO A CD    1 
ATOM   1345 N  N     . ASP A 1 173 ? 34.13123  3.92279   -7.43899  1.000 16.27003 ? 173 ASP A N     1 
ATOM   1346 C  CA    . ASP A 1 173 ? 32.95525  4.23883   -6.65198  1.000 15.51759 ? 173 ASP A CA    1 
ATOM   1347 C  C     . ASP A 1 173 ? 32.92532  5.72883   -6.31294  1.000 15.48157 ? 173 ASP A C     1 
ATOM   1348 O  O     . ASP A 1 173 ? 33.97336  6.36377   -6.16893  1.000 13.37822 ? 173 ASP A O     1 
ATOM   1349 C  CB    . ASP A 1 173 ? 32.93521  3.41381   -5.36800  1.000 16.18551 ? 173 ASP A CB    1 
ATOM   1350 C  CG    . ASP A 1 173 ? 32.96713  1.92181   -5.63303  1.000 22.55155 ? 173 ASP A CG    1 
ATOM   1351 O  OD1   . ASP A 1 173 ? 32.54711  1.49786   -6.72904  1.000 19.08286 ? 173 ASP A OD1   1 
ATOM   1352 O  OD2   . ASP A 1 173 ? 33.41110  1.17077   -4.74005  1.000 25.42425 ? 173 ASP A OD2   1 
ATOM   1353 N  N     . PRO A 1 174 ? 31.73635  6.30588   -6.17693  1.000 11.95605 ? 174 PRO A N     1 
ATOM   1354 C  CA    . PRO A 1 174 ? 31.62743  7.72188   -5.81089  1.000 17.01416 ? 174 PRO A CA    1 
ATOM   1355 C  C     . PRO A 1 174 ? 32.15644  7.95982   -4.40689  1.000 14.28390 ? 174 PRO A C     1 
ATOM   1356 O  O     . PRO A 1 174 ? 32.35440  7.00379   -3.64391  1.000 14.43695 ? 174 PRO A O     1 
ATOM   1357 C  CB    . PRO A 1 174 ? 30.11744  7.98696   -5.89688  1.000 14.66979 ? 174 PRO A CB    1 
ATOM   1358 C  CG    . PRO A 1 174 ? 29.49437  6.65499   -5.68991  1.000 17.05742 ? 174 PRO A CG    1 
ATOM   1359 C  CD    . PRO A 1 174 ? 30.41632  5.66996   -6.32894  1.000 15.28721 ? 174 PRO A CD    1 
ATOM   1360 N  N     . PRO A 1 175 ? 32.41651  9.21480   -4.03486  1.000 16.44832 ? 175 PRO A N     1 
ATOM   1361 C  CA    . PRO A 1 175 ? 32.92753  9.48774   -2.68586  1.000 15.81416 ? 175 PRO A CA    1 
ATOM   1362 C  C     . PRO A 1 175 ? 31.95951  9.00977   -1.61486  1.000 15.05813 ? 175 PRO A C     1 
ATOM   1363 O  O     . PRO A 1 175 ? 30.75550  8.87083   -1.84286  1.000 12.71021 ? 175 PRO A O     1 
ATOM   1364 C  CB    . PRO A 1 175 ? 33.08060  11.01573  -2.65982  1.000 18.24244 ? 175 PRO A CB    1 
ATOM   1365 C  CG    . PRO A 1 175 ? 32.22763  11.51680  -3.78781  1.000 18.07252 ? 175 PRO A CG    1 
ATOM   1366 C  CD    . PRO A 1 175 ? 32.30557  10.44582  -4.83583  1.000 17.71336 ? 175 PRO A CD    1 
ATOM   1367 N  N     . ALA A 1 176 ? 32.51150  8.74971   -0.42587  1.000 13.65022 ? 176 ALA A N     1 
ATOM   1368 C  CA    . ALA A 1 176 ? 31.69548  8.27472   0.68512   1.000 15.40097 ? 176 ALA A CA    1 
ATOM   1369 C  C     . ALA A 1 176 ? 30.64753  9.29677   1.09815   1.000 14.58798 ? 176 ALA A C     1 
ATOM   1370 O  O     . ALA A 1 176 ? 29.66552  8.93480   1.75514   1.000 15.04862 ? 176 ALA A O     1 
ATOM   1371 C  CB    . ALA A 1 176 ? 32.57947  7.91765   1.88211   1.000 16.69457 ? 176 ALA A CB    1 
ATOM   1372 N  N     . ALA A 1 177 ? 30.83659  10.56077  0.72718   1.000 15.43702 ? 177 ALA A N     1 
ATOM   1373 C  CA    . ALA A 1 177 ? 29.86365  11.61481  0.95921   1.000 15.55031 ? 177 ALA A CA    1 
ATOM   1374 C  C     . ALA A 1 177 ? 29.74369  12.44685  -0.30777  1.000 14.61514 ? 177 ALA A C     1 
ATOM   1375 O  O     . ALA A 1 177 ? 30.73970  12.69681  -0.99277  1.000 14.92426 ? 177 ALA A O     1 
ATOM   1376 C  CB    . ALA A 1 177 ? 30.26570  12.50276  2.14723   1.000 14.81055 ? 177 ALA A CB    1 
ATOM   1377 N  N     . MET A 1 178 ? 28.52271  12.86192  -0.62176  1.000 14.98209 ? 178 MET A N     1 
ATOM   1378 C  CA    . MET A 1 178 ? 28.27974  13.64696  -1.81874  1.000 15.74971 ? 178 MET A CA    1 
ATOM   1379 C  C     . MET A 1 178 ? 27.63781  14.97998  -1.45971  1.000 10.82857 ? 178 MET A C     1 
ATOM   1380 O  O     . MET A 1 178 ? 26.97182  15.09099  -0.42570  1.000 13.62997 ? 178 MET A O     1 
ATOM   1381 C  CB    . MET A 1 178 ? 27.37270  12.89303  -2.80075  1.000 17.75845 ? 178 MET A CB    1 
ATOM   1382 C  CG    . MET A 1 178 ? 28.07364  11.80401  -3.59078  1.000 18.67684 ? 178 MET A CG    1 
ATOM   1383 S  SD    . MET A 1 178 ? 26.85858  10.75109  -4.38880  1.000 25.66034 ? 178 MET A SD    1 
ATOM   1384 C  CE    . MET A 1 178 ? 25.77858  10.46911  -2.99780  1.000 19.63777 ? 178 MET A CE    1 
ATOM   1385 N  N     . PRO A 1 179 ? 27.82186  16.00499  -2.28768  1.000 14.46034 ? 179 PRO A N     1 
ATOM   1386 C  CA    . PRO A 1 179 ? 27.18492  17.30002  -2.02465  1.000 15.06789 ? 179 PRO A CA    1 
ATOM   1387 C  C     . PRO A 1 179 ? 25.67492  17.17409  -2.05465  1.000 13.76623 ? 179 PRO A C     1 
ATOM   1388 O  O     . PRO A 1 179 ? 25.10089  16.65315  -3.02366  1.000 14.27706 ? 179 PRO A O     1 
ATOM   1389 C  CB    . PRO A 1 179 ? 27.69497  18.18802  -3.17163  1.000 12.41346 ? 179 PRO A CB    1 
ATOM   1390 C  CG    . PRO A 1 179 ? 28.93193  17.51797  -3.65865  1.000 11.48188 ? 179 PRO A CG    1 
ATOM   1391 C  CD    . PRO A 1 179 ? 28.70886  16.05197  -3.46368  1.000 13.52988 ? 179 PRO A CD    1 
ATOM   1392 N  N     . PRO A 1 180 ? 24.99495  17.63910  -1.01463  1.000 13.48124 ? 180 PRO A N     1 
ATOM   1393 C  CA    . PRO A 1 180 ? 23.54394  17.47318  -0.93563  1.000 12.99453 ? 180 PRO A CA    1 
ATOM   1394 C  C     . PRO A 1 180 ? 22.82899  18.55423  -1.72260  1.000 13.80504 ? 180 PRO A C     1 
ATOM   1395 O  O     . PRO A 1 180 ? 23.44604  19.55421  -2.12258  1.000 9.39726  ? 180 PRO A O     1 
ATOM   1396 C  CB    . PRO A 1 180 ? 23.26795  17.60915  0.56737   1.000 16.18708 ? 180 PRO A CB    1 
ATOM   1397 C  CG    . PRO A 1 180 ? 24.32200  18.57809  1.02139   1.000 16.69013 ? 180 PRO A CG    1 
ATOM   1398 C  CD    . PRO A 1 180 ? 25.54498  18.30405  0.17938   1.000 14.20960 ? 180 PRO A CD    1 
ATOM   1399 N  N     . PRO A 1 181 ? 21.53198  18.39330  -1.97460  1.000 14.26298 ? 181 PRO A N     1 
ATOM   1400 C  CA    . PRO A 1 181 ? 20.75903  19.49935  -2.54357  1.000 12.88103 ? 181 PRO A CA    1 
ATOM   1401 C  C     . PRO A 1 181 ? 20.66810  20.65134  -1.55754  1.000 14.14216 ? 181 PRO A C     1 
ATOM   1402 O  O     . PRO A 1 181 ? 20.76909  20.47030  -0.34155  1.000 12.82563 ? 181 PRO A O     1 
ATOM   1403 C  CB    . PRO A 1 181 ? 19.38000  18.88143  -2.80258  1.000 16.97924 ? 181 PRO A CB    1 
ATOM   1404 C  CG    . PRO A 1 181 ? 19.61193  17.40542  -2.81662  1.000 15.50054 ? 181 PRO A CG    1 
ATOM   1405 C  CD    . PRO A 1 181 ? 20.72692  17.16734  -1.84963  1.000 13.39620 ? 181 PRO A CD    1 
ATOM   1406 N  N     . ALA A 1 182 ? 20.48715  21.85236  -2.10052  1.000 14.81372 ? 182 ALA A N     1 
ATOM   1407 C  CA    . ALA A 1 182 ? 20.29222  23.02235  -1.25749  1.000 15.88478 ? 182 ALA A CA    1 
ATOM   1408 C  C     . ALA A 1 182 ? 18.94922  22.93040  -0.54748  1.000 18.09196 ? 182 ALA A C     1 
ATOM   1409 O  O     . ALA A 1 182 ? 17.96319  22.44846  -1.11049  1.000 18.07777 ? 182 ALA A O     1 
ATOM   1410 C  CB    . ALA A 1 182 ? 20.36328  24.30236  -2.08846  1.000 14.26643 ? 182 ALA A CB    1 
ATOM   1411 N  N     . GLU A 1 183 ? 18.91224  23.39337  0.69653   1.000 18.09401 ? 183 GLU A N     1 
ATOM   1412 C  CA    . GLU A 1 183 ? 17.70224  23.30541  1.49653   1.000 15.86128 ? 183 GLU A CA    1 
ATOM   1413 C  C     . GLU A 1 183 ? 16.68829  24.36847  1.08556   1.000 16.16689 ? 183 GLU A C     1 
ATOM   1414 O  O     . GLU A 1 183 ? 17.04235  25.44047  0.58758   1.000 21.32961 ? 183 GLU A O     1 
ATOM   1415 C  CB    . GLU A 1 183 ? 18.03226  23.44936  2.98253   1.000 18.98991 ? 183 GLU A CB    1 
ATOM   1416 C  CG    . GLU A 1 183 ? 18.82920  22.29231  3.56350   0.000 17.50177 ? 183 GLU A CG    1 
ATOM   1417 C  CD    . GLU A 1 183 ? 19.12621  22.47826  5.03750   0.000 17.18598 ? 183 GLU A CD    1 
ATOM   1418 O  OE1   . GLU A 1 183 ? 19.19528  23.64224  5.48653   0.000 17.14102 ? 183 GLU A OE1   1 
ATOM   1419 O  OE2   . GLU A 1 183 ? 19.28317  21.46323  5.74848   0.000 17.00325 ? 183 GLU A OE2   1 
ATOM   1420 N  N     . ASP A 1 184 ? 15.41028  24.04853  1.30056   1.000 18.01298 ? 184 ASP A N     1 
ATOM   1421 C  CA    . ASP A 1 184 ? 14.28832  24.95660  1.06758   1.000 20.86380 ? 184 ASP A CA    1 
ATOM   1422 C  C     . ASP A 1 184 ? 14.16634  25.38864  -0.39241  1.000 17.87285 ? 184 ASP A C     1 
ATOM   1423 O  O     . ASP A 1 184 ? 13.77040  26.52166  -0.67638  1.000 20.16672 ? 184 ASP A O     1 
ATOM   1424 C  CB    . ASP A 1 184 ? 14.36939  26.18157  1.98561   1.000 20.21152 ? 184 ASP A CB    1 
ATOM   1425 C  CG    . ASP A 1 184 ? 14.26438  25.81054  3.44860   1.000 22.50246 ? 184 ASP A CG    1 
ATOM   1426 O  OD1   . ASP A 1 184 ? 13.75732  24.70456  3.74558   1.000 26.81818 ? 184 ASP A OD1   1 
ATOM   1427 O  OD2   . ASP A 1 184 ? 14.68642  26.61650  4.30462   1.000 27.82602 ? 184 ASP A OD2   1 
ATOM   1428 N  N     . MET A 1 185 ? 14.49229  24.49264  -1.32843  1.000 15.26426 ? 185 MET A N     1 
ATOM   1429 C  CA    . MET A 1 185 ? 14.15330  24.72669  -2.73142  1.000 13.33738 ? 185 MET A CA    1 
ATOM   1430 C  C     . MET A 1 185 ? 12.76627  24.15777  -3.01943  1.000 13.22849 ? 185 MET A C     1 
ATOM   1431 O  O     . MET A 1 185 ? 12.50521  22.99378  -2.69246  1.000 15.43015 ? 185 MET A O     1 
ATOM   1432 C  CB    . MET A 1 185 ? 15.17626  24.08366  -3.65644  1.000 15.91905 ? 185 MET A CB    1 
ATOM   1433 C  CG    . MET A 1 185 ? 16.56629  24.69959  -3.58043  1.000 17.37240 ? 185 MET A CG    1 
ATOM   1434 S  SD    . MET A 1 185 ? 16.61438  26.37760  -4.23939  1.000 19.92549 ? 185 MET A SD    1 
ATOM   1435 C  CE    . MET A 1 185 ? 18.33340  26.79951  -3.97039  1.000 21.32018 ? 185 MET A CE    1 
ATOM   1436 N  N     . PRO A 1 186 ? 11.86230  24.93683  -3.62441  1.000 11.93146 ? 186 PRO A N     1 
ATOM   1437 C  CA    . PRO A 1 186 ? 10.46128  24.48290  -3.72241  1.000 13.08300 ? 186 PRO A CA    1 
ATOM   1438 C  C     . PRO A 1 186 ? 10.27521  23.21493  -4.53644  1.000 12.53437 ? 186 PRO A C     1 
ATOM   1439 O  O     . PRO A 1 186 ? 9.49917   22.34096  -4.13046  1.000 8.35227  ? 186 PRO A O     1 
ATOM   1440 C  CB    . PRO A 1 186 ? 9.75034   25.68295  -4.36638  1.000 17.82725 ? 186 PRO A CB    1 
ATOM   1441 C  CG    . PRO A 1 186 ? 10.83538  26.47192  -5.02837  1.000 16.60552 ? 186 PRO A CG    1 
ATOM   1442 C  CD    . PRO A 1 186 ? 12.04937  26.28983  -4.17238  1.000 13.89144 ? 186 PRO A CD    1 
ATOM   1443 N  N     . SER A 1 187 ? 10.95220  23.08392  -5.67845  1.000 11.04604 ? 187 SER A N     1 
ATOM   1444 C  CA    . SER A 1 187 ? 10.81714  21.86995  -6.47448  1.000 12.95102 ? 187 SER A CA    1 
ATOM   1445 C  C     . SER A 1 187 ? 11.47408  20.66190  -5.82551  1.000 14.56400 ? 187 SER A C     1 
ATOM   1446 O  O     . SER A 1 187 ? 11.27102  19.53992  -6.30253  1.000 12.57264 ? 187 SER A O     1 
ATOM   1447 C  CB    . SER A 1 187 ? 11.40114  22.08395  -7.87147  1.000 11.81981 ? 187 SER A CB    1 
ATOM   1448 O  OG    . SER A 1 187 ? 10.59119  22.97001  -8.62345  1.000 17.09015 ? 187 SER A OG    1 
ATOM   1449 N  N     . ALA A 1 188 ? 12.24809  20.86184  -4.75951  1.000 15.10451 ? 188 ALA A N     1 
ATOM   1450 C  CA    . ALA A 1 188 ? 12.88404  19.77679  -4.02953  1.000 16.00568 ? 188 ALA A CA    1 
ATOM   1451 C  C     . ALA A 1 188 ? 12.12803  19.40680  -2.75854  1.000 13.90940 ? 188 ALA A C     1 
ATOM   1452 O  O     . ALA A 1 188 ? 12.68400  18.71675  -1.89656  1.000 16.22067 ? 188 ALA A O     1 
ATOM   1453 C  CB    . ALA A 1 188 ? 14.33306  20.14671  -3.69653  1.000 13.68527 ? 188 ALA A CB    1 
ATOM   1454 N  N     . ALA A 1 189 ? 10.88105  19.84886  -2.62352  1.000 12.17719 ? 189 ALA A N     1 
ATOM   1455 C  CA    . ALA A 1 189 ? 10.09204  19.51087  -1.44853  1.000 12.00996 ? 189 ALA A CA    1 
ATOM   1456 C  C     . ALA A 1 189 ? 9.93296   17.99687  -1.34956  1.000 15.36481 ? 189 ALA A C     1 
ATOM   1457 O  O     . ALA A 1 189 ? 9.57793   17.35092  -2.34558  1.000 9.45319  ? 189 ALA A O     1 
ATOM   1458 C  CB    . ALA A 1 189 ? 8.72207   20.18294  -1.50651  1.000 12.46916 ? 189 ALA A CB    1 
ATOM   1459 N  N     . PRO A 1 190 ? 10.18694  17.39583  -0.18358  1.000 13.85629 ? 190 PRO A N     1 
ATOM   1460 C  CA    . PRO A 1 190 ? 10.13986  15.92783  -0.09061  1.000 15.63114 ? 190 PRO A CA    1 
ATOM   1461 C  C     . PRO A 1 190 ? 8.77483   15.33991  -0.39162  1.000 11.72305 ? 190 PRO A C     1 
ATOM   1462 O  O     . PRO A 1 190 ? 8.69577   14.21693  -0.90365  1.000 10.64617 ? 190 PRO A O     1 
ATOM   1463 C  CB    . PRO A 1 190 ? 10.55885  15.65578  1.36238   1.000 17.46019 ? 190 PRO A CB    1 
ATOM   1464 C  CG    . PRO A 1 190 ? 11.32192  16.87273  1.77640   1.000 13.52253 ? 190 PRO A CG    1 
ATOM   1465 C  CD    . PRO A 1 190 ? 10.63497  18.01278  1.07643   1.000 15.67899 ? 190 PRO A CD    1 
ATOM   1466 N  N     . ALA A 1 191 ? 7.69387   16.06096  -0.09360  1.000 14.94952 ? 191 ALA A N     1 
ATOM   1467 C  CA    . ALA A 1 191 ? 6.35784   15.52903  -0.32861  1.000 12.77197 ? 191 ALA A CA    1 
ATOM   1468 C  C     . ALA A 1 191 ? 6.00783   15.44108  -1.80761  1.000 12.37036 ? 191 ALA A C     1 
ATOM   1469 O  O     . ALA A 1 191 ? 5.00580   14.80414  -2.15162  1.000 14.23039 ? 191 ALA A O     1 
ATOM   1470 C  CB    . ALA A 1 191 ? 5.32089   16.38207  0.40042   1.000 10.75554 ? 191 ALA A CB    1 
ATOM   1471 N  N     . ALA A 1 192 ? 6.79986   16.05706  -2.68360  1.000 12.70762 ? 192 ALA A N     1 
ATOM   1472 C  CA    . ALA A 1 192 ? 6.54485   16.03111  -4.11460  1.000 14.10454 ? 192 ALA A CA    1 
ATOM   1473 C  C     . ALA A 1 192 ? 7.65582   15.35807  -4.90562  1.000 14.75392 ? 192 ALA A C     1 
ATOM   1474 O  O     . ALA A 1 192 ? 7.56181   15.29011  -6.13762  1.000 12.64006 ? 192 ALA A O     1 
ATOM   1475 C  CB    . ALA A 1 192 ? 6.33392   17.45513  -4.64556  1.000 15.36411 ? 192 ALA A CB    1 
ATOM   1476 N  N     . THR A 1 193 ? 8.70679   14.86400  -4.24063  1.000 13.98227 ? 193 THR A N     1 
ATOM   1477 C  CA    . THR A 1 193 ? 9.83276   14.23596  -4.92265  1.000 12.96031 ? 193 THR A CA    1 
ATOM   1478 C  C     . THR A 1 193 ? 10.16369  12.86093  -4.35069  1.000 11.88385 ? 193 THR A C     1 
ATOM   1479 O  O     . THR A 1 193 ? 11.25966  12.34388  -4.59670  1.000 10.37103 ? 193 THR A O     1 
ATOM   1480 C  CB    . THR A 1 193 ? 11.07180  15.13590  -4.86164  1.000 10.93262 ? 193 THR A CB    1 
ATOM   1481 O  OG1   . THR A 1 193 ? 11.36783  15.44985  -3.49563  1.000 11.86578 ? 193 THR A OG1   1 
ATOM   1482 C  CG2   . THR A 1 193 ? 10.83187  16.42493  -5.63361  1.000 13.44982 ? 193 THR A CG2   1 
ATOM   1483 N  N     . GLY A 1 194 ? 9.24566   12.25596  -3.59470  1.000 13.33502 ? 194 GLY A N     1 
ATOM   1484 C  CA    . GLY A 1 194 ? 9.48760   10.94394  -3.03773  1.000 7.22389  ? 194 GLY A CA    1 
ATOM   1485 C  C     . GLY A 1 194 ? 9.26554   9.83297   -4.04375  1.000 13.96079 ? 194 GLY A C     1 
ATOM   1486 O  O     . GLY A 1 194 ? 8.68054   10.02303  -5.10775  1.000 10.44988 ? 194 GLY A O     1 
ATOM   1487 N  N     . VAL A 1 195 ? 9.75348   8.64794   -3.69078  1.000 16.19729 ? 195 VAL A N     1 
ATOM   1488 C  CA    . VAL A 1 195 ? 9.59342   7.46797   -4.53781  1.000 13.71917 ? 195 VAL A CA    1 
ATOM   1489 C  C     . VAL A 1 195 ? 8.20139   6.89203   -4.30382  1.000 17.14608 ? 195 VAL A C     1 
ATOM   1490 O  O     . VAL A 1 195 ? 7.88537   6.47402   -3.17983  1.000 14.24639 ? 195 VAL A O     1 
ATOM   1491 C  CB    . VAL A 1 195 ? 10.68337  6.42090   -4.25884  1.000 11.98857 ? 195 VAL A CB    1 
ATOM   1492 C  CG1   . VAL A 1 195 ? 10.49630  5.21894   -5.16887  1.000 12.94076 ? 195 VAL A CG1   1 
ATOM   1493 C  CG2   . VAL A 1 195 ? 12.06440  7.02884   -4.44783  1.000 14.08605 ? 195 VAL A CG2   1 
ATOM   1494 N  N     . PRO A 1 196 ? 7.34738   6.84910   -5.31982  1.000 15.48345 ? 196 PRO A N     1 
ATOM   1495 C  CA    . PRO A 1 196 ? 5.98036   6.35916   -5.12682  1.000 15.99300 ? 196 PRO A CA    1 
ATOM   1496 C  C     . PRO A 1 196 ? 5.93228   4.83716   -5.05986  1.000 17.23675 ? 196 PRO A C     1 
ATOM   1497 O  O     . PRO A 1 196 ? 6.87525   4.13012   -5.41888  1.000 17.23970 ? 196 PRO A O     1 
ATOM   1498 C  CB    . PRO A 1 196 ? 5.24638   6.87823   -6.36681  1.000 17.65318 ? 196 PRO A CB    1 
ATOM   1499 C  CG    . PRO A 1 196 ? 6.30338   6.93120   -7.41381  1.000 19.47395 ? 196 PRO A CG    1 
ATOM   1500 C  CD    . PRO A 1 196 ? 7.58640   7.29912   -6.70281  1.000 15.56459 ? 196 PRO A CD    1 
ATOM   1501 N  N     . THR A 1 197 ? 4.79626   4.34321   -4.58387  1.000 21.03572 ? 197 THR A N     1 
ATOM   1502 C  CA    . THR A 1 197 ? 4.50019   2.91922   -4.56890  1.000 22.80811 ? 197 THR A CA    1 
ATOM   1503 C  C     . THR A 1 197 ? 3.67716   2.55630   -5.80290  1.000 17.89847 ? 197 THR A C     1 
ATOM   1504 O  O     . THR A 1 197 ? 3.21621   3.42534   -6.54688  1.000 23.58550 ? 197 THR A O     1 
ATOM   1505 C  CB    . THR A 1 197 ? 3.75717   2.53523   -3.28291  1.000 20.25521 ? 197 THR A CB    1 
ATOM   1506 O  OG1   . THR A 1 197 ? 2.40120   2.98830   -3.35489  1.000 28.08622 ? 197 THR A OG1   1 
ATOM   1507 C  CG2   . THR A 1 197 ? 4.42021   3.17417   -2.07189  1.000 25.11553 ? 197 THR A CG2   1 
ATOM   1508 N  N     . TRP A 1 198 ? 3.49910   1.25031   -6.02193  1.000 18.55120 ? 198 TRP A N     1 
ATOM   1509 C  CA    . TRP A 1 198 ? 2.75207   0.80938   -7.19494  1.000 20.61396 ? 198 TRP A CA    1 
ATOM   1510 C  C     . TRP A 1 198 ? 1.25608   1.06345   -7.06093  1.000 22.40884 ? 198 TRP A C     1 
ATOM   1511 O  O     . TRP A 1 198 ? 0.55108   1.06851   -8.07493  1.000 21.22076 ? 198 TRP A O     1 
ATOM   1512 C  CB    . TRP A 1 198 ? 3.00799   -0.67663  -7.48298  1.000 24.61856 ? 198 TRP A CB    1 
ATOM   1513 C  CG    . TRP A 1 198 ? 2.52095   -1.63263  -6.42600  1.000 19.33874 ? 198 TRP A CG    1 
ATOM   1514 C  CD1   . TRP A 1 198 ? 3.26192   -2.19869  -5.42902  1.000 21.83334 ? 198 TRP A CD1   1 
ATOM   1515 C  CD2   . TRP A 1 198 ? 1.19092   -2.14557  -6.27501  1.000 18.85933 ? 198 TRP A CD2   1 
ATOM   1516 N  NE1   . TRP A 1 198 ? 2.47389   -3.02367  -4.66203  1.000 20.39348 ? 198 TRP A NE1   1 
ATOM   1517 C  CE2   . TRP A 1 198 ? 1.19789   -3.00759  -5.16103  1.000 20.44551 ? 198 TRP A CE2   1 
ATOM   1518 C  CE3   . TRP A 1 198 ? -0.00607  -1.95449  -6.97000  1.000 20.77207 ? 198 TRP A CE3   1 
ATOM   1519 C  CZ2   . TRP A 1 198 ? 0.05585   -3.67755  -4.72604  1.000 22.73396 ? 198 TRP A CZ2   1 
ATOM   1520 C  CZ3   . TRP A 1 198 ? -1.14010  -2.61944  -6.53701  1.000 22.01407 ? 198 TRP A CZ3   1 
ATOM   1521 C  CH2   . TRP A 1 198 ? -1.10114  -3.46947  -5.42603  1.000 20.16581 ? 198 TRP A CH2   1 
ATOM   1522 N  N     . GLN A 1 199 ? 0.75510   1.27544   -5.84192  1.000 22.26827 ? 199 GLN A N     1 
ATOM   1523 C  CA    . GLN A 1 199 ? -0.65388  1.60351   -5.66091  1.000 21.56005 ? 199 GLN A CA    1 
ATOM   1524 C  C     . GLN A 1 199 ? -0.95981  3.06453   -5.96187  1.000 20.36659 ? 199 GLN A C     1 
ATOM   1525 O  O     . GLN A 1 199 ? -2.10480  3.38860   -6.29286  1.000 27.37909 ? 199 GLN A O     1 
ATOM   1526 C  CB    . GLN A 1 199 ? -1.10189  1.28650   -4.23192  1.000 22.38647 ? 199 GLN A CB    1 
ATOM   1527 C  CG    . GLN A 1 199 ? -0.85896  -0.14452  -3.78795  1.000 27.55219 ? 199 GLN A CG    1 
ATOM   1528 C  CD    . GLN A 1 199 ? 0.34503   -0.26961  -2.87596  1.000 28.45448 ? 199 GLN A CD    1 
ATOM   1529 O  OE1   . GLN A 1 199 ? 1.30007   0.49835   -2.98294  1.000 23.55242 ? 199 GLN A OE1   1 
ATOM   1530 N  NE2   . GLN A 1 199 ? 0.30199   -1.23562  -1.96698  1.000 29.22313 ? 199 GLN A NE2   1 
ATOM   1531 N  N     . GLU A 1 200 ? 0.03023   3.94848   -5.85086  1.000 22.72576 ? 200 GLU A N     1 
ATOM   1532 C  CA    . GLU A 1 200 ? -0.19969  5.37250   -6.05182  1.000 26.46801 ? 200 GLU A CA    1 
ATOM   1533 C  C     . GLU A 1 200 ? -0.15868  5.77953   -7.51781  1.000 27.12579 ? 200 GLU A C     1 
ATOM   1534 O  O     . GLU A 1 200 ? -0.64263  6.86456   -7.85979  1.000 28.31105 ? 200 GLU A O     1 
ATOM   1535 C  CB    . GLU A 1 200 ? 0.83235   6.17743   -5.26781  1.000 22.99633 ? 200 GLU A CB    1 
ATOM   1536 C  CG    . GLU A 1 200 ? 0.82434   5.87739   -3.78482  1.000 27.78809 ? 200 GLU A CG    1 
ATOM   1537 C  CD    . GLU A 1 200 ? 1.98038   6.52832   -3.05380  1.000 24.69352 ? 200 GLU A CD    1 
ATOM   1538 O  OE1   . GLU A 1 200 ? 3.00539   6.83328   -3.69980  1.000 24.76646 ? 200 GLU A OE1   1 
ATOM   1539 O  OE2   . GLU A 1 200 ? 1.86439   6.73829   -1.83180  1.000 30.40086 ? 200 GLU A OE2   1 
ATOM   1540 N  N     . VAL A 1 201 ? 0.41527   4.94452   -8.39084  1.000 24.45210 ? 201 VAL A N     1 
ATOM   1541 C  CA    . VAL A 1 201 ? 0.45928   5.25655   -9.81383  1.000 25.44765 ? 201 VAL A CA    1 
ATOM   1542 C  C     . VAL A 1 201 ? -0.72075  4.67163   -10.57384 1.000 27.29724 ? 201 VAL A C     1 
ATOM   1543 O  O     . VAL A 1 201 ? -0.78674  4.82466   -11.80083 1.000 30.23008 ? 201 VAL A O     1 
ATOM   1544 C  CB    . VAL A 1 201 ? 1.78326   4.76750   -10.43384 1.000 26.13453 ? 201 VAL A CB    1 
ATOM   1545 C  CG1   . VAL A 1 201 ? 2.96330   5.45443   -9.76583  1.000 21.20685 ? 201 VAL A CG1   1 
ATOM   1546 C  CG2   . VAL A 1 201 ? 1.89618   3.26049   -10.30388 1.000 21.74674 ? 201 VAL A CG2   1 
ATOM   1547 N  N     . GLY A 1 202 ? -1.64578  3.99866   -9.89585  1.000 25.94938 ? 202 GLY A N     1 
ATOM   1548 C  CA    . GLY A 1 202 ? -2.86181  3.49574   -10.51086 1.000 27.84220 ? 202 GLY A CA    1 
ATOM   1549 C  C     . GLY A 1 202 ? -2.98588  1.98575   -10.58689 1.000 29.72827 ? 202 GLY A C     1 
ATOM   1550 O  O     . GLY A 1 202 ? -4.11091  1.47981   -10.70990 1.000 36.07420 ? 202 GLY A O     1 
ATOM   1551 N  N     . PHE A 1 203 ? -1.88392  1.24269   -10.51491 1.000 26.46563 ? 203 PHE A N     1 
ATOM   1552 C  CA    . PHE A 1 203 ? -1.96199  -0.21131  -10.61695 1.000 26.66918 ? 203 PHE A CA    1 
ATOM   1553 C  C     . PHE A 1 203 ? -2.84402  -0.78529  -9.51396  1.000 24.20435 ? 203 PHE A C     1 
ATOM   1554 O  O     . PHE A 1 203 ? -2.71200  -0.42032  -8.34295  1.000 24.31983 ? 203 PHE A O     1 
ATOM   1555 C  CB    . PHE A 1 203 ? -0.56403  -0.83338  -10.55897 1.000 25.50054 ? 203 PHE A CB    1 
ATOM   1556 C  CG    . PHE A 1 203 ? 0.23398   -0.64339  -11.81697 1.000 19.22625 ? 203 PHE A CG    1 
ATOM   1557 C  CD1   . PHE A 1 203 ? -0.21805  -1.15934  -13.02098 1.000 18.45064 ? 203 PHE A CD1   1 
ATOM   1558 C  CD2   . PHE A 1 203 ? 1.43501   0.04155   -11.79496 1.000 18.46609 ? 203 PHE A CD2   1 
ATOM   1559 C  CE1   . PHE A 1 203 ? 0.50595   -0.98535  -14.17898 1.000 15.89264 ? 203 PHE A CE1   1 
ATOM   1560 C  CE2   . PHE A 1 203 ? 2.16502   0.21654   -12.95195 1.000 19.33968 ? 203 PHE A CE2   1 
ATOM   1561 C  CZ    . PHE A 1 203 ? 1.70099   -0.29741  -14.14496 1.000 20.05467 ? 203 PHE A CZ    1 
ATOM   1562 N  N     . LYS A 1 204 ? -3.74107  -1.69523  -9.89898  1.000 24.12437 ? 204 LYS A N     1 
ATOM   1563 C  CA    . LYS A 1 204 ? -4.75109  -2.24620  -9.00498  1.000 28.59449 ? 204 LYS A CA    1 
ATOM   1564 C  C     . LYS A 1 204 ? -4.46516  -3.66723  -8.54002  1.000 26.92690 ? 204 LYS A C     1 
ATOM   1565 O  O     . LYS A 1 204 ? -4.94618  -4.06023  -7.47503  1.000 33.67070 ? 204 LYS A O     1 
ATOM   1566 C  CB    . LYS A 1 204 ? -6.12409  -2.21412  -9.68798  1.000 25.86765 ? 204 LYS A CB    1 
ATOM   1567 C  CG    . LYS A 1 204 ? -6.15005  -1.35209  -10.93996 1.000 28.77075 ? 204 LYS A CG    1 
ATOM   1568 C  CD    . LYS A 1 204 ? -7.55405  -1.18400  -11.48795 0.000 28.11237 ? 204 LYS A CD    1 
ATOM   1569 C  CE    . LYS A 1 204 ? -8.37800  -0.25698  -10.61092 0.000 27.73242 ? 204 LYS A CE    1 
ATOM   1570 N  NZ    . LYS A 1 204 ? -9.78099  -0.13890  -11.09692 0.000 26.78714 ? 204 LYS A NZ    1 
ATOM   1571 N  N     . GLU A 1 205 ? -3.71120  -4.44925  -9.30804  1.000 26.52466 ? 205 GLU A N     1 
ATOM   1572 C  CA    . GLU A 1 205 ? -3.32727  -5.81028  -8.95407  1.000 26.74312 ? 205 GLU A CA    1 
ATOM   1573 C  C     . GLU A 1 205 ? -1.86727  -5.84736  -8.51708  1.000 23.83135 ? 205 GLU A C     1 
ATOM   1574 O  O     . GLU A 1 205 ? -1.02124  -5.18539  -9.12907  1.000 19.97095 ? 205 GLU A O     1 
ATOM   1575 C  CB    . GLU A 1 205 ? -3.53532  -6.74924  -10.14310 1.000 26.21838 ? 205 GLU A CB    1 
ATOM   1576 C  CG    . GLU A 1 205 ? -4.02139  -8.14122  -9.77813  0.000 25.95868 ? 205 GLU A CG    1 
ATOM   1577 C  CD    . GLU A 1 205 ? -4.88243  -8.75415  -10.86414 0.000 26.34791 ? 205 GLU A CD    1 
ATOM   1578 O  OE1   . GLU A 1 205 ? -5.80240  -8.06409  -11.35112 0.000 26.60505 ? 205 GLU A OE1   1 
ATOM   1579 O  OE2   . GLU A 1 205 ? -4.63449  -9.92016  -11.23517 0.000 26.37240 ? 205 GLU A OE2   1 
ATOM   1580 N  N     . PRO A 1 206 ? -1.54031  -6.59040  -7.46210  1.000 23.97648 ? 206 PRO A N     1 
ATOM   1581 C  CA    . PRO A 1 206 ? -0.17930  -6.54948  -6.91110  1.000 17.60035 ? 206 PRO A CA    1 
ATOM   1582 C  C     . PRO A 1 206 ? 0.80966   -7.25451  -7.82012  1.000 14.57773 ? 206 PRO A C     1 
ATOM   1583 O  O     . PRO A 1 206 ? 0.42461   -8.10947  -8.63114  1.000 19.80850 ? 206 PRO A O     1 
ATOM   1584 C  CB    . PRO A 1 206 ? -0.32333  -7.28451  -5.57112  1.000 17.26957 ? 206 PRO A CB    1 
ATOM   1585 C  CG    . PRO A 1 206 ? -1.46538  -8.21444  -5.78714  1.000 19.07605 ? 206 PRO A CG    1 
ATOM   1586 C  CD    . PRO A 1 206 ? -2.42135  -7.48538  -6.69112  1.000 27.53015 ? 206 PRO A CD    1 
ATOM   1587 N  N     . PRO A 1 207 ? 2.09368   -6.92258  -7.71812  1.000 13.84577 ? 207 PRO A N     1 
ATOM   1588 C  CA    . PRO A 1 207 ? 3.10564   -7.64161  -8.49914  1.000 13.48250 ? 207 PRO A CA    1 
ATOM   1589 C  C     . PRO A 1 207 ? 3.36457   -9.02764  -7.92818  1.000 15.95590 ? 207 PRO A C     1 
ATOM   1590 O  O     . PRO A 1 207 ? 3.26356   -9.25666  -6.72118  1.000 19.45987 ? 207 PRO A O     1 
ATOM   1591 C  CB    . PRO A 1 207 ? 4.34468   -6.74868  -8.37413  1.000 12.97424 ? 207 PRO A CB    1 
ATOM   1592 C  CG    . PRO A 1 207 ? 4.15972   -6.05270  -7.07511  1.000 11.92127 ? 207 PRO A CG    1 
ATOM   1593 C  CD    . PRO A 1 207 ? 2.68174   -5.83663  -6.91510  1.000 14.62042 ? 207 PRO A CD    1 
ATOM   1594 N  N     . LEU A 1 208 ? 3.71052   -9.96264  -8.81920  1.000 11.24326 ? 208 LEU A N     1 
ATOM   1595 C  CA    . LEU A 1 208 ? 3.94745   -11.34666 -8.43223  1.000 15.51057 ? 208 LEU A CA    1 
ATOM   1596 C  C     . LEU A 1 208 ? 5.37343   -11.82672 -8.66425  1.000 11.73418 ? 208 LEU A C     1 
ATOM   1597 O  O     . LEU A 1 208 ? 5.72537   -12.90975 -8.18028  1.000 8.87679  ? 208 LEU A O     1 
ATOM   1598 C  CB    . LEU A 1 208 ? 2.99240   -12.29059 -9.18225  1.000 10.59686 ? 208 LEU A CB    1 
ATOM   1599 C  CG    . LEU A 1 208 ? 1.50041   -12.18152 -8.86424  1.000 18.91213 ? 208 LEU A CG    1 
ATOM   1600 C  CD1   . LEU A 1 208 ? 0.71335   -13.24646 -9.61527  1.000 19.98590 ? 208 LEU A CD1   1 
ATOM   1601 C  CD2   . LEU A 1 208 ? 1.26941   -12.29255 -7.36625  1.000 16.65114 ? 208 LEU A CD2   1 
ATOM   1602 N  N     . THR A 1 209 ? 6.19746   -11.06775 -9.38124  1.000 11.62272 ? 209 THR A N     1 
ATOM   1603 C  CA    . THR A 1 209 ? 7.53244   -11.53781 -9.71925  1.000 9.31149  ? 209 THR A CA    1 
ATOM   1604 C  C     . THR A 1 209 ? 8.38443   -11.68688 -8.46426  1.000 11.99742 ? 209 THR A C     1 
ATOM   1605 O  O     . THR A 1 209 ? 8.19047   -10.99189 -7.46224  1.000 12.88986 ? 209 THR A O     1 
ATOM   1606 C  CB    . THR A 1 209 ? 8.20248   -10.58082 -10.70523 1.000 10.01296 ? 209 THR A CB    1 
ATOM   1607 O  OG1   . THR A 1 209 ? 9.47345   -11.11287 -11.09525 1.000 11.62176 ? 209 THR A OG1   1 
ATOM   1608 C  CG2   . THR A 1 209 ? 8.39955   -9.20984  -10.08120 1.000 8.42127  ? 209 THR A CG2   1 
ATOM   1609 N  N     . VAL A 1 210 ? 9.33539   -12.62293 -8.52429  1.000 8.47569  ? 210 VAL A N     1 
ATOM   1610 C  CA    . VAL A 1 210 ? 10.18737  -12.93400 -7.38230  1.000 8.86408  ? 210 VAL A CA    1 
ATOM   1611 C  C     . VAL A 1 210 ? 11.53541  -12.23906 -7.45428  1.000 10.28737 ? 210 VAL A C     1 
ATOM   1612 O  O     . VAL A 1 210 ? 12.36140  -12.41713 -6.54929  1.000 15.71340 ? 210 VAL A O     1 
ATOM   1613 C  CB    . VAL A 1 210 ? 10.38930  -14.45501 -7.24633  1.000 8.89424  ? 210 VAL A CB    1 
ATOM   1614 C  CG1   . VAL A 1 210 ? 9.05226   -15.14895 -7.05034  1.000 10.05264 ? 210 VAL A CG1   1 
ATOM   1615 C  CG2   . VAL A 1 210 ? 11.10227  -14.99602 -8.47435  1.000 8.83512  ? 210 VAL A CG2   1 
ATOM   1616 N  N     . PHE A 1 211 ? 11.78744  -11.45905 -8.50127  1.000 9.48131  ? 211 PHE A N     1 
ATOM   1617 C  CA    . PHE A 1 211 ? 13.05548  -10.76511 -8.67526  1.000 12.43178 ? 211 PHE A CA    1 
ATOM   1618 C  C     . PHE A 1 211 ? 12.87855  -9.30911  -8.26122  1.000 11.85348 ? 211 PHE A C     1 
ATOM   1619 O  O     . PHE A 1 211 ? 12.05459  -8.58906  -8.83720  1.000 15.05481 ? 211 PHE A O     1 
ATOM   1620 C  CB    . PHE A 1 211 ? 13.54247  -10.86310 -10.12126 1.000 11.59996 ? 211 PHE A CB    1 
ATOM   1621 C  CG    . PHE A 1 211 ? 13.48240  -12.25309 -10.68829 1.000 10.34894 ? 211 PHE A CG    1 
ATOM   1622 C  CD1   . PHE A 1 211 ? 14.38235  -13.22214 -10.28432 1.000 8.94655  ? 211 PHE A CD1   1 
ATOM   1623 C  CD2   . PHE A 1 211 ? 12.52338  -12.58801 -11.63230 1.000 12.30010 ? 211 PHE A CD2   1 
ATOM   1624 C  CE1   . PHE A 1 211 ? 14.32228  -14.49712 -10.80935 1.000 8.70172  ? 211 PHE A CE1   1 
ATOM   1625 C  CE2   . PHE A 1 211 ? 12.46031  -13.86200 -12.16133 1.000 8.18424  ? 211 PHE A CE2   1 
ATOM   1626 C  CZ    . PHE A 1 211 ? 13.35926  -14.81505 -11.75235 1.000 7.92735  ? 211 PHE A CZ    1 
ATOM   1627 N  N     . LYS A 1 212 ? 13.64658  -8.88117  -7.26321  1.000 13.57025 ? 212 LYS A N     1 
ATOM   1628 C  CA    . LYS A 1 212 ? 13.54565  -7.52618  -6.74518  1.000 12.89457 ? 212 LYS A CA    1 
ATOM   1629 C  C     . LYS A 1 212 ? 14.52569  -6.61121  -7.45816  1.000 8.56767  ? 212 LYS A C     1 
ATOM   1630 O  O     . LYS A 1 212 ? 15.63967  -7.01726  -7.79418  1.000 11.02940 ? 212 LYS A O     1 
ATOM   1631 C  CB    . LYS A 1 212 ? 13.80666  -7.48923  -5.23518  1.000 15.41393 ? 212 LYS A CB    1 
ATOM   1632 C  CG    . LYS A 1 212 ? 13.27160  -8.67722  -4.43321  1.000 20.86933 ? 212 LYS A CG    1 
ATOM   1633 C  CD    . LYS A 1 212 ? 11.79458  -8.98114  -4.68521  1.000 18.89161 ? 212 LYS A CD    1 
ATOM   1634 C  CE    . LYS A 1 212 ? 10.91265  -7.75010  -4.54318  1.000 19.88546 ? 212 LYS A CE    1 
ATOM   1635 N  NZ    . LYS A 1 212 ? 11.20469  -6.96114  -3.31516  1.000 31.45171 ? 212 LYS A NZ    1 
ATOM   1636 N  N     . GLY A 1 213 ? 14.10376  -5.36919  -7.67413  1.000 7.52995  ? 213 GLY A N     1 
ATOM   1637 C  CA    . GLY A 1 213 ? 14.94180  -4.41021  -8.34911  1.000 8.10698  ? 213 GLY A CA    1 
ATOM   1638 C  C     . GLY A 1 213 ? 15.93184  -3.73929  -7.42010  1.000 8.87885  ? 213 GLY A C     1 
ATOM   1639 O  O     . GLY A 1 213 ? 15.88184  -3.86631  -6.19610  1.000 6.50958  ? 213 GLY A O     1 
ATOM   1640 N  N     . GLY A 1 214 ? 16.86187  -3.00932  -8.03109  1.000 7.04583  ? 214 GLY A N     1 
ATOM   1641 C  CA    . GLY A 1 214 ? 17.84691  -2.26439  -7.27207  1.000 6.04215  ? 214 GLY A CA    1 
ATOM   1642 C  C     . GLY A 1 214 ? 19.27389  -2.69145  -7.54209  1.000 8.03482  ? 214 GLY A C     1 
ATOM   1643 O  O     . GLY A 1 214 ? 19.52783  -3.83946  -7.91912  1.000 7.72888  ? 214 GLY A O     1 
ATOM   1644 N  N     . GLU A 1 215 ? 20.21094  -1.76050  -7.35207  1.000 6.91374  ? 215 GLU A N     1 
ATOM   1645 C  CA    . GLU A 1 215 ? 21.62492  -2.06357  -7.55008  1.000 8.20020  ? 215 GLU A CA    1 
ATOM   1646 C  C     . GLU A 1 215 ? 22.11387  -3.10662  -6.55411  1.000 7.69943  ? 215 GLU A C     1 
ATOM   1647 O  O     . GLU A 1 215 ? 22.95483  -3.94965  -6.88913  1.000 8.27516  ? 215 GLU A O     1 
ATOM   1648 C  CB    . GLU A 1 215 ? 22.44899  -0.78062  -7.42606  1.000 8.81012  ? 215 GLU A CB    1 
ATOM   1649 C  CG    . GLU A 1 215 ? 23.95398  -0.96869  -7.51907  1.000 7.60128  ? 215 GLU A CG    1 
ATOM   1650 C  CD    . GLU A 1 215 ? 24.71704  0.30826   -7.21404  1.000 8.50916  ? 215 GLU A CD    1 
ATOM   1651 O  OE1   . GLU A 1 215 ? 24.10010  1.26528   -6.69702  1.000 6.79364  ? 215 GLU A OE1   1 
ATOM   1652 O  OE2   . GLU A 1 215 ? 25.93305  0.35621   -7.49304  1.000 5.78646  ? 215 GLU A OE2   1 
ATOM   1653 N  N     . THR A 1 216 ? 21.59988  -3.06062  -5.32411  1.000 6.82494  ? 216 THR A N     1 
ATOM   1654 C  CA    . THR A 1 216 ? 22.02784  -4.00067  -4.29213  1.000 8.74479  ? 216 THR A CA    1 
ATOM   1655 C  C     . THR A 1 216 ? 21.74176  -5.43864  -4.70416  1.000 8.83947  ? 216 THR A C     1 
ATOM   1656 O  O     . THR A 1 216 ? 22.59572  -6.31969  -4.55019  1.000 8.43927  ? 216 THR A O     1 
ATOM   1657 C  CB    . THR A 1 216 ? 21.33186  -3.67366  -2.97012  1.000 9.23565  ? 216 THR A CB    1 
ATOM   1658 O  OG1   . THR A 1 216 ? 21.75093  -2.38170  -2.51409  1.000 11.28451 ? 216 THR A OG1   1 
ATOM   1659 C  CG2   . THR A 1 216 ? 21.66681  -4.72171  -1.90915  1.000 8.11588  ? 216 THR A CG2   1 
ATOM   1660 N  N     . GLU A 1 217 ? 20.53675  -5.69557  -5.22517  1.000 7.86623  ? 217 GLU A N     1 
ATOM   1661 C  CA    . GLU A 1 217 ? 20.19068  -7.03454  -5.69420  1.000 7.68606  ? 217 GLU A CA    1 
ATOM   1662 C  C     . GLU A 1 217 ? 21.01365  -7.42456  -6.91221  1.000 7.97564  ? 217 GLU A C     1 
ATOM   1663 O  O     . GLU A 1 217 ? 21.41160  -8.58757  -7.05324  1.000 10.83043 ? 217 GLU A O     1 
ATOM   1664 C  CB    . GLU A 1 217 ? 18.69667  -7.11146  -6.01219  1.000 8.29265  ? 217 GLU A CB    1 
ATOM   1665 C  CG    . GLU A 1 217 ? 17.80068  -7.03944  -4.78419  1.000 12.28639 ? 217 GLU A CG    1 
ATOM   1666 C  CD    . GLU A 1 217 ? 18.00963  -8.20948  -3.83922  1.000 12.12112 ? 217 GLU A CD    1 
ATOM   1667 O  OE1   . GLU A 1 217 ? 18.12857  -9.35347  -4.32424  1.000 15.07398 ? 217 GLU A OE1   1 
ATOM   1668 O  OE2   . GLU A 1 217 ? 18.06164  -7.98551  -2.61121  1.000 19.71814 ? 217 GLU A OE2   1 
ATOM   1669 N  N     . ALA A 1 218 ? 21.27370  -6.46755  -7.80619  1.000 8.42493  ? 218 ALA A N     1 
ATOM   1670 C  CA    . ALA A 1 218 ? 22.08768  -6.75756  -8.98120  1.000 7.81343  ? 218 ALA A CA    1 
ATOM   1671 C  C     . ALA A 1 218 ? 23.48266  -7.21764  -8.58221  1.000 9.59151  ? 218 ALA A C     1 
ATOM   1672 O  O     . ALA A 1 218 ? 24.04261  -8.13565  -9.19324  1.000 10.88856 ? 218 ALA A O     1 
ATOM   1673 C  CB    . ALA A 1 218 ? 22.16974  -5.52454  -9.87817  1.000 7.22402  ? 218 ALA A CB    1 
ATOM   1674 N  N     . LEU A 1 219 ? 24.05669  -6.59069  -7.55320  1.000 9.54729  ? 219 LEU A N     1 
ATOM   1675 C  CA    . LEU A 1 219 ? 25.37868  -6.98277  -7.08022  1.000 6.61855  ? 219 LEU A CA    1 
ATOM   1676 C  C     . LEU A 1 219 ? 25.34161  -8.32079  -6.35225  1.000 8.59239  ? 219 LEU A C     1 
ATOM   1677 O  O     . LEU A 1 219 ? 26.31757  -9.07784  -6.40027  1.000 8.52779  ? 219 LEU A O     1 
ATOM   1678 C  CB    . LEU A 1 219 ? 25.95074  -5.89482  -6.17219  1.000 7.12343  ? 219 LEU A CB    1 
ATOM   1679 C  CG    . LEU A 1 219 ? 26.18280  -4.52382  -6.81716  1.000 10.58467 ? 219 LEU A CG    1 
ATOM   1680 C  CD1   . LEU A 1 219 ? 26.60686  -3.49187  -5.78214  1.000 11.50517 ? 219 LEU A CD1   1 
ATOM   1681 C  CD2   . LEU A 1 219 ? 27.21479  -4.62085  -7.93217  1.000 8.29842  ? 219 LEU A CD2   1 
ATOM   1682 N  N     . ALA A 1 220 ? 24.23160  -8.63475  -5.67725  1.000 9.99404  ? 220 ALA A N     1 
ATOM   1683 C  CA    . ALA A 1 220 ? 24.14454  -9.90576  -4.96428  1.000 7.82372  ? 220 ALA A CA    1 
ATOM   1684 C  C     . ALA A 1 220 ? 23.98847  -11.07273 -5.93131  1.000 7.93309  ? 220 ALA A C     1 
ATOM   1685 O  O     . ALA A 1 220 ? 24.57442  -12.14076 -5.71733  1.000 7.72388  ? 220 ALA A O     1 
ATOM   1686 C  CB    . ALA A 1 220 ? 22.98854  -9.87572  -3.96627  1.000 6.77821  ? 220 ALA A CB    1 
ATOM   1687 N  N     . ARG A 1 221 ? 23.18787  -10.89695 -6.98919  1.000 9.16867  ? 221 ARG A N     1 
ATOM   1688 C  CA    . ARG A 1 221 ? 23.08541  -11.92526 -8.01995  1.000 8.64812  ? 221 ARG A CA    1 
ATOM   1689 C  C     . ARG A 1 221 ? 24.40770  -12.12081 -8.74590  1.000 7.74934  ? 221 ARG A C     1 
ATOM   1690 O  O     . ARG A 1 221 ? 24.73062  -13.24009 -9.15438  1.000 8.19507  ? 221 ARG A O     1 
ATOM   1691 C  CB    . ARG A 1 221 ? 22.00071  -11.56686 -9.03339  1.000 9.46776  ? 221 ARG A CB    1 
ATOM   1692 C  CG    . ARG A 1 221 ? 20.59877  -11.48673 -8.47846  1.000 12.72881 ? 221 ARG A CG    1 
ATOM   1693 C  CD    . ARG A 1 221 ? 19.59882  -11.77255 -9.57869  1.000 14.13876 ? 221 ARG A CD    1 
ATOM   1694 N  NE    . ARG A 1 221 ? 19.67113  -13.16074 -10.01542 1.000 19.26724 ? 221 ARG A NE    1 
ATOM   1695 C  CZ    . ARG A 1 221 ? 18.89180  -14.12736 -9.55294  1.000 18.77240 ? 221 ARG A CZ    1 
ATOM   1696 N  NH1   . ARG A 1 221 ? 17.95739  -13.88788 -8.64808  1.000 21.68023 ? 221 ARG A NH1   1 
ATOM   1697 N  NH2   . ARG A 1 221 ? 19.05117  -15.36410 -10.01297 1.000 22.03451 ? 221 ARG A NH2   1 
ATOM   1698 N  N     . LEU A 1 222 ? 25.17046  -11.04172 -8.93231  1.000 10.46803 ? 222 LEU A N     1 
ATOM   1699 C  CA    . LEU A 1 222 ? 26.48146  -11.14777 -9.56732  1.000 9.49142  ? 222 LEU A CA    1 
ATOM   1700 C  C     . LEU A 1 222 ? 27.43042  -11.99884 -8.73034  1.000 8.11356  ? 222 LEU A C     1 
ATOM   1701 O  O     . LEU A 1 222 ? 28.08037  -12.91586 -9.24437  1.000 11.07874 ? 222 LEU A O     1 
ATOM   1702 C  CB    . LEU A 1 222 ? 27.06553  -9.75279  -9.79329  1.000 7.47377  ? 222 LEU A CB    1 
ATOM   1703 C  CG    . LEU A 1 222 ? 28.45453  -9.65085  -10.43029 1.000 10.41591 ? 222 LEU A CG    1 
ATOM   1704 C  CD1   . LEU A 1 222 ? 28.42450  -10.13381 -11.87130 1.000 11.63181 ? 222 LEU A CD1   1 
ATOM   1705 C  CD2   . LEU A 1 222 ? 28.98060  -8.22588  -10.34726 1.000 14.21800 ? 222 LEU A CD2   1 
ATOM   1706 N  N     . GLU A 1 223 ? 27.52544  -11.70387 -7.43133  1.000 9.87387  ? 223 GLU A N     1 
ATOM   1707 C  CA    . GLU A 1 223 ? 28.40340  -12.47094 -6.55236  1.000 9.99741  ? 223 GLU A CA    1 
ATOM   1708 C  C     . GLU A 1 223 ? 27.94333  -13.91392 -6.42039  1.000 13.74131 ? 223 GLU A C     1 
ATOM   1709 O  O     . GLU A 1 223 ? 28.77328  -14.82296 -6.30241  1.000 16.97006 ? 223 GLU A O     1 
ATOM   1710 C  CB    . GLU A 1 223 ? 28.47944  -11.81397 -5.17434  1.000 12.47770 ? 223 GLU A CB    1 
ATOM   1711 C  CG    . GLU A 1 223 ? 29.04451  -10.40300 -5.17331  1.000 13.14468 ? 223 GLU A CG    1 
ATOM   1712 C  CD    . GLU A 1 223 ? 30.54851  -10.36607 -5.36532  1.000 15.34301 ? 223 GLU A CD    1 
ATOM   1713 O  OE1   . GLU A 1 223 ? 31.19146  -11.43711 -5.30334  1.000 27.72418 ? 223 GLU A OE1   1 
ATOM   1714 O  OE2   . GLU A 1 223 ? 31.08857  -9.26010  -5.57729  1.000 13.42355 ? 223 GLU A OE2   1 
ATOM   1715 N  N     . ALA A 1 224 ? 26.63132  -14.14485 -6.43939  1.000 11.24192 ? 224 ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 224 ? 26.12925  -15.50983 -6.33542  1.000 14.90655 ? 224 ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 224 ? 26.51620  -16.33682 -7.55544  1.000 12.01490 ? 224 ALA A C     1 
ATOM   1718 O  O     . ALA A 1 224 ? 26.84314  -17.52284 -7.43047  1.000 14.16754 ? 224 ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 224 ? 24.61325  -15.49976 -6.15041  1.000 14.32457 ? 224 ALA A CB    1 
ATOM   1720 N  N     . ALA A 1 225 ? 26.49323  -15.72979 -8.74343  1.000 10.29280 ? 225 ALA A N     1 
ATOM   1721 C  CA    . ALA A 1 225 ? 26.88619  -16.46478 -9.94044  1.000 15.74095 ? 225 ALA A CA    1 
ATOM   1722 C  C     . ALA A 1 225 ? 28.38317  -16.73686 -9.96546  1.000 15.74339 ? 225 ALA A C     1 
ATOM   1723 O  O     . ALA A 1 225 ? 28.82412  -17.71486 -10.58148 1.000 16.91496 ? 225 ALA A O     1 
ATOM   1724 C  CB    . ALA A 1 225 ? 26.46722  -15.69973 -11.19543 1.000 13.97177 ? 225 ALA A CB    1 
ATOM   1725 N  N     . PHE A 1 226 ? 29.17522  -15.89091 -9.31044  1.000 16.25249 ? 226 PHE A N     1 
ATOM   1726 C  CA    . PHE A 1 226 ? 30.62221  -16.03999 -9.26345  1.000 15.88284 ? 226 PHE A CA    1 
ATOM   1727 C  C     . PHE A 1 226 ? 31.10217  -16.82504 -8.04747  1.000 18.68170 ? 226 PHE A C     1 
ATOM   1728 O  O     . PHE A 1 226 ? 32.31417  -16.91011 -7.82148  1.000 18.32419 ? 226 PHE A O     1 
ATOM   1729 C  CB    . PHE A 1 226 ? 31.29228  -14.66102 -9.29542  1.000 18.61150 ? 226 PHE A CB    1 
ATOM   1730 C  CG    . PHE A 1 226 ? 31.44030  -14.09099 -10.67841 1.000 14.73654 ? 226 PHE A CG    1 
ATOM   1731 C  CD1   . PHE A 1 226 ? 30.36033  -13.52192 -11.32939 1.000 15.03759 ? 226 PHE A CD1   1 
ATOM   1732 C  CD2   . PHE A 1 226 ? 32.66230  -14.12404 -11.32741 1.000 14.74144 ? 226 PHE A CD2   1 
ATOM   1733 C  CE1   . PHE A 1 226 ? 30.49835  -13.00090 -12.59938 1.000 12.06614 ? 226 PHE A CE1   1 
ATOM   1734 C  CE2   . PHE A 1 226 ? 32.80332  -13.60502 -12.59540 1.000 12.07374 ? 226 PHE A CE2   1 
ATOM   1735 C  CZ    . PHE A 1 226 ? 31.72135  -13.04295 -13.23138 1.000 11.75132 ? 226 PHE A CZ    1 
ATOM   1736 N  N     . GLN A 1 227 ? 30.18515  -17.39701 -7.25848  1.000 20.44712 ? 227 GLN A N     1 
ATOM   1737 C  CA    . GLN A 1 227 ? 30.60011  -18.26906 -6.16350  1.000 19.89085 ? 227 GLN A CA    1 
ATOM   1738 C  C     . GLN A 1 227 ? 31.24404  -19.54408 -6.68753  1.000 17.88732 ? 227 GLN A C     1 
ATOM   1739 O  O     . GLN A 1 227 ? 32.09702  -20.13114 -6.01255  1.000 15.53879 ? 227 GLN A O     1 
ATOM   1740 C  CB    . GLN A 1 227 ? 29.40710  -18.61402 -5.26851  1.000 20.99539 ? 227 GLN A CB    1 
ATOM   1741 C  CG    . GLN A 1 227 ? 28.80216  -17.43001 -4.52348  1.000 25.27070 ? 227 GLN A CG    1 
ATOM   1742 C  CD    . GLN A 1 227 ? 29.63119  -16.98208 -3.32847  1.000 27.25087 ? 227 GLN A CD    1 
ATOM   1743 O  OE1   . GLN A 1 227 ? 29.34224  -15.95708 -2.71044  1.000 32.68661 ? 227 GLN A OE1   1 
ATOM   1744 N  NE2   . GLN A 1 227 ? 30.65915  -17.75214 -2.99449  1.000 19.97670 ? 227 GLN A NE2   1 
ATOM   1745 N  N     . ASP A 1 228 ? 30.85302  -19.97803 -7.88154  1.000 16.38737 ? 228 ASP A N     1 
ATOM   1746 C  CA    . ASP A 1 228 ? 31.43495  -21.15204 -8.52957  1.000 16.63812 ? 228 ASP A CA    1 
ATOM   1747 C  C     . ASP A 1 228 ? 32.14897  -20.71105 -9.79957  1.000 12.29092 ? 228 ASP A C     1 
ATOM   1748 O  O     . ASP A 1 228 ? 31.50997  -20.56899 -10.85756 1.000 10.73729 ? 228 ASP A O     1 
ATOM   1749 C  CB    . ASP A 1 228 ? 30.35690  -22.18898 -8.84559  1.000 14.20335 ? 228 ASP A CB    1 
ATOM   1750 C  CG    . ASP A 1 228 ? 30.93783  -23.51600 -9.28563  1.000 11.26812 ? 228 ASP A CG    1 
ATOM   1751 O  OD1   . ASP A 1 228 ? 32.16782  -23.68907 -9.17864  1.000 15.81179 ? 228 ASP A OD1   1 
ATOM   1752 O  OD2   . ASP A 1 228 ? 30.16679  -24.38895 -9.73964  1.000 17.57317 ? 228 ASP A OD2   1 
ATOM   1753 N  N     . PRO A 1 229 ? 33.46198  -20.47812 -9.75157  1.000 14.91416 ? 229 PRO A N     1 
ATOM   1754 C  CA    . PRO A 1 229 ? 34.15800  -20.00212 -10.95756 1.000 13.58640 ? 229 PRO A CA    1 
ATOM   1755 C  C     . PRO A 1 229 ? 34.17195  -21.00810 -12.09658 1.000 12.45032 ? 229 PRO A C     1 
ATOM   1756 O  O     . PRO A 1 229 ? 34.19896  -20.59907 -13.26357 1.000 9.43844  ? 229 PRO A O     1 
ATOM   1757 C  CB    . PRO A 1 229 ? 35.57302  -19.70521 -10.44456 1.000 14.06154 ? 229 PRO A CB    1 
ATOM   1758 C  CG    . PRO A 1 229 ? 35.72198  -20.55424 -9.23258  1.000 14.58580 ? 229 PRO A CG    1 
ATOM   1759 C  CD    . PRO A 1 229 ? 34.36498  -20.58219 -8.59457  1.000 17.17249 ? 229 PRO A CD    1 
ATOM   1760 N  N     . LYS A 1 230 ? 34.15588  -22.31210 -11.79761 1.000 12.64183 ? 230 LYS A N     1 
ATOM   1761 C  CA    . LYS A 1 230 ? 34.12583  -23.31208 -12.86163 1.000 12.43662 ? 230 LYS A CA    1 
ATOM   1762 C  C     . LYS A 1 230 ? 32.82683  -23.23999 -13.65363 1.000 11.17773 ? 230 LYS A C     1 
ATOM   1763 O  O     . LYS A 1 230 ? 32.82581  -23.44897 -14.87563 1.000 7.44441  ? 230 LYS A O     1 
ATOM   1764 C  CB    . LYS A 1 230 ? 34.31476  -24.71510 -12.28567 1.000 13.68346 ? 230 LYS A CB    1 
ATOM   1765 C  CG    . LYS A 1 230 ? 35.71875  -25.01618 -11.79468 1.000 18.11986 ? 230 LYS A CG    1 
ATOM   1766 C  CD    . LYS A 1 230 ? 35.85567  -26.49320 -11.47072 1.000 22.46833 ? 230 LYS A CD    1 
ATOM   1767 C  CE    . LYS A 1 230 ? 37.13366  -26.78228 -10.70973 0.000 21.24188 ? 230 LYS A CE    1 
ATOM   1768 N  NZ    . LYS A 1 230 ? 37.19159  -28.20229 -10.26676 0.000 21.49587 ? 230 LYS A NZ    1 
ATOM   1769 N  N     . TRP A 1 231 ? 31.71085  -22.95295 -12.97862 1.000 8.53638  ? 231 TRP A N     1 
ATOM   1770 C  CA    . TRP A 1 231 ? 30.44585  -22.81487 -13.69161 1.000 8.87255  ? 231 TRP A CA    1 
ATOM   1771 C  C     . TRP A 1 231 ? 30.47591  -21.61985 -14.63458 1.000 8.13314  ? 231 TRP A C     1 
ATOM   1772 O  O     . TRP A 1 231 ? 29.96090  -21.68980 -15.75758 1.000 8.21776  ? 231 TRP A O     1 
ATOM   1773 C  CB    . TRP A 1 231 ? 29.28686  -22.68484 -12.70360 1.000 9.42543  ? 231 TRP A CB    1 
ATOM   1774 C  CG    . TRP A 1 231 ? 27.95487  -22.49075 -13.37459 1.000 9.19782  ? 231 TRP A CG    1 
ATOM   1775 C  CD1   . TRP A 1 231 ? 27.11682  -23.46770 -13.83361 1.000 8.87546  ? 231 TRP A CD1   1 
ATOM   1776 C  CD2   . TRP A 1 231 ? 27.31393  -21.24271 -13.67156 1.000 8.01808  ? 231 TRP A CD2   1 
ATOM   1777 N  NE1   . TRP A 1 231 ? 25.99584  -22.90463 -14.39359 1.000 12.58913 ? 231 TRP A NE1   1 
ATOM   1778 C  CE2   . TRP A 1 231 ? 26.09091  -21.54064 -14.30556 1.000 9.54936  ? 231 TRP A CE2   1 
ATOM   1779 C  CE3   . TRP A 1 231 ? 27.65400  -19.90274 -13.46053 1.000 8.14193  ? 231 TRP A CE3   1 
ATOM   1780 C  CZ2   . TRP A 1 231 ? 25.20696  -20.54858 -14.72953 1.000 10.94781 ? 231 TRP A CZ2   1 
ATOM   1781 C  CZ3   . TRP A 1 231 ? 26.77705  -18.91968 -13.88350 1.000 8.98505  ? 231 TRP A CZ3   1 
ATOM   1782 C  CH2   . TRP A 1 231 ? 25.56803  -19.24761 -14.50951 1.000 7.87899  ? 231 TRP A CH2   1 
ATOM   1783 N  N     . VAL A 1 232 ? 31.07696  -20.51389 -14.19356 1.000 7.03715  ? 232 VAL A N     1 
ATOM   1784 C  CA    . VAL A 1 232 ? 31.19102  -19.33388 -15.04253 1.000 8.39708  ? 232 VAL A CA    1 
ATOM   1785 C  C     . VAL A 1 232 ? 32.12200  -19.60690 -16.21654 1.000 8.38519  ? 232 VAL A C     1 
ATOM   1786 O  O     . VAL A 1 232 ? 31.83202  -19.22786 -17.35753 1.000 8.43971  ? 232 VAL A O     1 
ATOM   1787 C  CB    . VAL A 1 232 ? 31.66908  -18.12992 -14.21050 1.000 9.61232  ? 232 VAL A CB    1 
ATOM   1788 C  CG1   . VAL A 1 232 ? 32.11914  -17.00092 -15.11748 1.000 8.85955  ? 232 VAL A CG1   1 
ATOM   1789 C  CG2   . VAL A 1 232 ? 30.57111  -17.65689 -13.27849 1.000 9.74968  ? 232 VAL A CG2   1 
ATOM   1790 N  N     . ALA A 1 233 ? 33.25097  -20.27096 -15.95556 1.000 7.75560  ? 233 ALA A N     1 
ATOM   1791 C  CA    . ALA A 1 233 ? 34.24795  -20.49899 -16.99757 1.000 9.32812  ? 233 ALA A CA    1 
ATOM   1792 C  C     . ALA A 1 233 ? 33.70690  -21.40893 -18.09159 1.000 9.55468  ? 233 ALA A C     1 
ATOM   1793 O  O     . ALA A 1 233 ? 33.88291  -21.13491 -19.28358 1.000 10.13297 ? 233 ALA A O     1 
ATOM   1794 C  CB    . ALA A 1 233 ? 35.51993  -21.09307 -16.38959 1.000 8.03894  ? 233 ALA A CB    1 
ATOM   1795 N  N     . GLY A 1 234 ? 33.05285  -22.50091 -17.70861 1.000 10.58225 ? 234 GLY A N     1 
ATOM   1796 C  CA    . GLY A 1 234 ? 32.53880  -23.45886 -18.66463 1.000 9.10164  ? 234 GLY A CA    1 
ATOM   1797 C  C     . GLY A 1 234 ? 31.12081  -23.20978 -19.12062 1.000 8.40149  ? 234 GLY A C     1 
ATOM   1798 O  O     . GLY A 1 234 ? 30.49176  -24.11873 -19.67264 1.000 10.14260 ? 234 GLY A O     1 
ATOM   1799 N  N     . PHE A 1 235 ? 30.59787  -22.00476 -18.90759 1.000 6.21945  ? 235 PHE A N     1 
ATOM   1800 C  CA    . PHE A 1 235 ? 29.21688  -21.70768 -19.26258 1.000 9.19062  ? 235 PHE A CA    1 
ATOM   1801 C  C     . PHE A 1 235 ? 28.99887  -21.84463 -20.76458 1.000 9.58209  ? 235 PHE A C     1 
ATOM   1802 O  O     . PHE A 1 235 ? 29.74190  -21.27765 -21.56957 1.000 12.30965 ? 235 PHE A O     1 
ATOM   1803 C  CB    . PHE A 1 235 ? 28.85396  -20.29567 -18.79854 1.000 9.07635  ? 235 PHE A CB    1 
ATOM   1804 C  CG    . PHE A 1 235 ? 27.49198  -19.83659 -19.24353 1.000 8.17682  ? 235 PHE A CG    1 
ATOM   1805 C  CD1   . PHE A 1 235 ? 26.36297  -20.14455 -18.50253 1.000 8.42914  ? 235 PHE A CD1   1 
ATOM   1806 C  CD2   . PHE A 1 235 ? 27.34301  -19.08356 -20.39851 1.000 8.43178  ? 235 PHE A CD2   1 
ATOM   1807 C  CE1   . PHE A 1 235 ? 25.11099  -19.71848 -18.91051 1.000 8.47043  ? 235 PHE A CE1   1 
ATOM   1808 C  CE2   . PHE A 1 235 ? 26.09503  -18.65548 -20.81149 1.000 9.47607  ? 235 PHE A CE2   1 
ATOM   1809 C  CZ    . PHE A 1 235 ? 24.97902  -18.97345 -20.06750 1.000 5.83296  ? 235 PHE A CZ    1 
ATOM   1810 N  N     . GLN A 1 236 ? 27.97383  -22.60557 -21.14259 1.000 10.36357 ? 236 GLN A N     1 
ATOM   1811 C  CA    . GLN A 1 236 ? 27.56282  -22.72652 -22.53860 1.000 9.92725  ? 236 GLN A CA    1 
ATOM   1812 C  C     . GLN A 1 236 ? 26.05683  -22.51444 -22.60958 1.000 12.26134 ? 236 GLN A C     1 
ATOM   1813 O  O     . GLN A 1 236 ? 25.28579  -23.32941 -22.09460 1.000 10.44756 ? 236 GLN A O     1 
ATOM   1814 C  CB    . GLN A 1 236 ? 27.96475  -24.07852 -23.12463 1.000 11.48800 ? 236 GLN A CB    1 
ATOM   1815 C  CG    . GLN A 1 236 ? 29.46574  -24.23460 -23.29564 1.000 13.77738 ? 236 GLN A CG    1 
ATOM   1816 C  CD    . GLN A 1 236 ? 29.84268  -25.45560 -24.10967 1.000 16.89412 ? 236 GLN A CD    1 
ATOM   1817 O  OE1   . GLN A 1 236 ? 29.17765  -25.79354 -25.08767 1.000 15.49942 ? 236 GLN A OE1   1 
ATOM   1818 N  NE2   . GLN A 1 236 ? 30.91564  -26.12666 -23.70669 1.000 22.96054 ? 236 GLN A NE2   1 
ATOM   1819 N  N     . LYS A 1 237 ? 25.64888  -21.42040 -23.25656 1.000 6.20587  ? 237 LYS A N     1 
ATOM   1820 C  CA    . LYS A 1 237 ? 24.24390  -21.01533 -23.24954 1.000 9.26934  ? 237 LYS A CA    1 
ATOM   1821 C  C     . LYS A 1 237 ? 23.29385  -22.07427 -23.80256 1.000 9.68784  ? 237 LYS A C     1 
ATOM   1822 O  O     . LYS A 1 237 ? 22.26884  -22.34224 -23.15357 1.000 7.94552  ? 237 LYS A O     1 
ATOM   1823 C  CB    . LYS A 1 237 ? 24.09797  -19.68831 -24.00451 1.000 8.77433  ? 237 LYS A CB    1 
ATOM   1824 C  CG    . LYS A 1 237 ? 22.69200  -19.11224 -23.99749 1.000 9.35926  ? 237 LYS A CG    1 
ATOM   1825 C  CD    . LYS A 1 237 ? 22.21101  -18.87525 -22.57748 1.000 9.16140  ? 237 LYS A CD    1 
ATOM   1826 C  CE    . LYS A 1 237 ? 21.08107  -17.86319 -22.53346 1.000 9.41341  ? 237 LYS A CE    1 
ATOM   1827 N  NZ    . LYS A 1 237 ? 21.54513  -16.48221 -22.84942 1.000 7.10754  ? 237 LYS A NZ    1 
ATOM   1828 N  N     . PRO A 1 238 ? 23.54081  -22.69426 -24.96558 1.000 9.67635  ? 238 PRO A N     1 
ATOM   1829 C  CA    . PRO A 1 238 ? 22.56176  -23.66020 -25.49760 1.000 12.52973 ? 238 PRO A CA    1 
ATOM   1830 C  C     . PRO A 1 238 ? 22.39470  -24.91521 -24.65563 1.000 10.72180 ? 238 PRO A C     1 
ATOM   1831 O  O     . PRO A 1 238 ? 21.44666  -25.67315 -24.90164 1.000 11.28776 ? 238 PRO A O     1 
ATOM   1832 C  CB    . PRO A 1 238 ? 23.12474  -24.00919 -26.88261 1.000 15.10420 ? 238 PRO A CB    1 
ATOM   1833 C  CG    . PRO A 1 238 ? 24.03779  -22.89923 -27.22059 1.000 12.21857 ? 238 PRO A CG    1 
ATOM   1834 C  CD    . PRO A 1 238 ? 24.63082  -22.45529 -25.92758 1.000 9.63198  ? 238 PRO A CD    1 
ATOM   1835 N  N     . ASP A 1 239 ? 23.27569  -25.17027 -23.69364 1.000 11.77133 ? 239 ASP A N     1 
ATOM   1836 C  CA    . ASP A 1 239 ? 23.19663  -26.36329 -22.86166 1.000 11.69255 ? 239 ASP A CA    1 
ATOM   1837 C  C     . ASP A 1 239 ? 22.45465  -26.12728 -21.55266 1.000 13.12791 ? 239 ASP A C     1 
ATOM   1838 O  O     . ASP A 1 239 ? 22.27061  -27.07629 -20.78268 1.000 15.82865 ? 239 ASP A O     1 
ATOM   1839 C  CB    . ASP A 1 239 ? 24.60561  -26.89537 -22.56468 1.000 10.74557 ? 239 ASP A CB    1 
ATOM   1840 C  CG    . ASP A 1 239 ? 25.36758  -27.27938 -23.82269 1.000 13.34012 ? 239 ASP A CG    1 
ATOM   1841 O  OD1   . ASP A 1 239 ? 24.72857  -27.46032 -24.87870 1.000 16.56469 ? 239 ASP A OD1   1 
ATOM   1842 O  OD2   . ASP A 1 239 ? 26.60758  -27.40744 -23.75270 1.000 15.69091 ? 239 ASP A OD2   1 
ATOM   1843 N  N     . THR A 1 240 ? 22.02671  -24.89827 -21.27962 1.000 9.10730  ? 240 THR A N     1 
ATOM   1844 C  CA    . THR A 1 240 ? 21.34673  -24.60926 -20.02862 1.000 7.81924  ? 240 THR A CA    1 
ATOM   1845 C  C     . THR A 1 240 ? 19.90671  -25.11619 -20.06862 1.000 11.53742 ? 240 THR A C     1 
ATOM   1846 O  O     . THR A 1 240 ? 19.32669  -25.34713 -21.13362 1.000 9.33369  ? 240 THR A O     1 
ATOM   1847 C  CB    . THR A 1 240 ? 21.38081  -23.10927 -19.72558 1.000 9.89377  ? 240 THR A CB    1 
ATOM   1848 O  OG1   . THR A 1 240 ? 20.91284  -22.37322 -20.86156 1.000 13.86880 ? 240 THR A OG1   1 
ATOM   1849 C  CG2   . THR A 1 240 ? 22.79883  -22.67035 -19.39058 1.000 14.18850 ? 240 THR A CG2   1 
ATOM   1850 N  N     . ASP A 1 241 ? 19.33170  -25.28519 -18.87662 1.000 8.07079  ? 241 ASP A N     1 
ATOM   1851 C  CA    . ASP A 1 241 ? 18.04467  -25.94513 -18.71163 1.000 11.36272 ? 241 ASP A CA    1 
ATOM   1852 C  C     . ASP A 1 241 ? 16.92772  -24.91407 -18.71161 1.000 7.83736  ? 241 ASP A C     1 
ATOM   1853 O  O     . ASP A 1 241 ? 16.86777  -24.07909 -17.79559 1.000 8.59298  ? 241 ASP A O     1 
ATOM   1854 C  CB    . ASP A 1 241 ? 18.02864  -26.74716 -17.41165 1.000 12.02697 ? 241 ASP A CB    1 
ATOM   1855 C  CG    . ASP A 1 241 ? 16.90058  -27.76310 -17.35667 1.000 9.06707  ? 241 ASP A CG    1 
ATOM   1856 O  OD1   . ASP A 1 241 ? 15.85259  -27.54603 -17.99966 1.000 7.39348  ? 241 ASP A OD1   1 
ATOM   1857 O  OD2   . ASP A 1 241 ? 17.06854  -28.78513 -16.65870 1.000 9.24233  ? 241 ASP A OD2   1 
ATOM   1858 N  N     . PRO A 1 242 ? 16.01672  -24.93400 -19.69060 1.000 7.82636  ? 242 PRO A N     1 
ATOM   1859 C  CA    . PRO A 1 242 ? 14.90877  -23.96795 -19.67557 1.000 7.19844  ? 242 PRO A CA    1 
ATOM   1860 C  C     . PRO A 1 242 ? 13.81676  -24.28591 -18.66958 1.000 8.01624  ? 242 PRO A C     1 
ATOM   1861 O  O     . PRO A 1 242 ? 13.06580  -23.37388 -18.29455 1.000 9.30162  ? 242 PRO A O     1 
ATOM   1862 C  CB    . PRO A 1 242 ? 14.36576  -24.03588 -21.11057 1.000 5.83762  ? 242 PRO A CB    1 
ATOM   1863 C  CG    . PRO A 1 242 ? 14.68969  -25.43589 -21.55461 1.000 7.60729  ? 242 PRO A CG    1 
ATOM   1864 C  CD    . PRO A 1 242 ? 15.99667  -25.78897 -20.89162 1.000 6.72307  ? 242 PRO A CD    1 
ATOM   1865 N  N     . SER A 1 243 ? 13.70469  -25.53192 -18.21561 1.000 6.65192  ? 243 SER A N     1 
ATOM   1866 C  CA    . SER A 1 243 ? 12.65668  -25.92889 -17.28661 1.000 8.68625  ? 243 SER A CA    1 
ATOM   1867 C  C     . SER A 1 243 ? 13.05069  -25.73694 -15.83061 1.000 8.92269  ? 243 SER A C     1 
ATOM   1868 O  O     . SER A 1 243 ? 12.23668  -26.01392 -14.94461 1.000 10.11960 ? 243 SER A O     1 
ATOM   1869 C  CB    . SER A 1 243 ? 12.27160  -27.39286 -17.51665 1.000 8.30152  ? 243 SER A CB    1 
ATOM   1870 O  OG    . SER A 1 243 ? 13.35856  -28.25692 -17.23867 1.000 5.67603  ? 243 SER A OG    1 
ATOM   1871 N  N     . ALA A 1 244 ? 14.26872  -25.27901 -15.56260 1.000 7.92383  ? 244 ALA A N     1 
ATOM   1872 C  CA    . ALA A 1 244 ? 14.70574  -25.03106 -14.19660 1.000 9.47418  ? 244 ALA A CA    1 
ATOM   1873 C  C     . ALA A 1 244 ? 14.11380  -23.71605 -13.70957 1.000 10.35910 ? 244 ALA A C     1 
ATOM   1874 O  O     . ALA A 1 244 ? 14.30185  -22.67404 -14.34654 1.000 9.99823  ? 244 ALA A O     1 
ATOM   1875 C  CB    . ALA A 1 244 ? 16.23074  -24.99914 -14.12460 1.000 10.41654 ? 244 ALA A CB    1 
ATOM   1876 N  N     . TRP A 1 245 ? 13.40681  -23.75904 -12.58056 1.000 12.43196 ? 245 TRP A N     1 
ATOM   1877 C  CA    . TRP A 1 245 ? 12.76887  -22.55902 -12.05353 1.000 11.72129 ? 245 TRP A CA    1 
ATOM   1878 C  C     . TRP A 1 245 ? 13.14289  -22.32507 -10.59553 1.000 12.69010 ? 245 TRP A C     1 
ATOM   1879 O  O     . TRP A 1 245 ? 13.20695  -21.17708 -10.14350 1.000 15.71905 ? 245 TRP A O     1 
ATOM   1880 C  CB    . TRP A 1 245 ? 11.24686  -22.64294 -12.20953 1.000 13.93618 ? 245 TRP A CB    1 
ATOM   1881 C  CG    . TRP A 1 245 ? 10.62481  -23.84792 -11.56956 1.000 15.14668 ? 245 TRP A CG    1 
ATOM   1882 C  CD1   . TRP A 1 245 ? 10.41974  -25.06590 -12.14758 1.000 15.35849 ? 245 TRP A CD1   1 
ATOM   1883 C  CD2   . TRP A 1 245 ? 10.10881  -23.94593 -10.23456 1.000 21.67766 ? 245 TRP A CD2   1 
ATOM   1884 N  NE1   . TRP A 1 245 ? 9.81770   -25.91889 -11.25460 1.000 15.44437 ? 245 TRP A NE1   1 
ATOM   1885 C  CE2   . TRP A 1 245 ? 9.61574   -25.25590 -10.07358 1.000 17.85068 ? 245 TRP A CE2   1 
ATOM   1886 C  CE3   . TRP A 1 245 ? 10.02086  -23.05395 -9.16053  1.000 18.45744 ? 245 TRP A CE3   1 
ATOM   1887 C  CZ2   . TRP A 1 245 ? 9.04272   -25.69690 -8.88359  1.000 26.59449 ? 245 TRP A CZ2   1 
ATOM   1888 C  CZ3   . TRP A 1 245 ? 9.45084   -23.49395 -7.97854  1.000 18.70282 ? 245 TRP A CZ3   1 
ATOM   1889 C  CH2   . TRP A 1 245 ? 8.96977   -24.80392 -7.85057  1.000 24.56415 ? 245 TRP A CH2   1 
ATOM   1890 N  N     . GLU A 1 246 ? 13.39083  -23.40310 -9.85156  1.000 16.50670 ? 246 GLU A N     1 
ATOM   1891 C  CA    . GLU A 1 246 ? 13.79985  -23.25715 -8.45855  1.000 13.56959 ? 246 GLU A CA    1 
ATOM   1892 C  C     . GLU A 1 246 ? 15.16088  -22.57923 -8.36154  1.000 14.54678 ? 246 GLU A C     1 
ATOM   1893 O  O     . GLU A 1 246 ? 15.34593  -21.63825 -7.58052  1.000 11.91664 ? 246 GLU A O     1 
ATOM   1894 C  CB    . GLU A 1 246 ? 13.81878  -24.62617 -7.78059  1.000 20.14389 ? 246 GLU A CB    1 
ATOM   1895 C  CG    . GLU A 1 246 ? 12.56174  -25.44110 -8.04560  1.000 23.67004 ? 246 GLU A CG    1 
ATOM   1896 C  CD    . GLU A 1 246 ? 12.49668  -26.70812 -7.21763  1.000 32.88327 ? 246 GLU A CD    1 
ATOM   1897 O  OE1   . GLU A 1 246 ? 13.52766  -27.09218 -6.62464  1.000 30.50205 ? 246 GLU A OE1   1 
ATOM   1898 O  OE2   . GLU A 1 246 ? 11.40765  -27.32006 -7.15664  1.000 36.04708 ? 246 GLU A OE2   1 
ATOM   1899 N  N     . LYS A 1 247 ? 16.12386  -23.05026 -9.14856  1.000 12.40114 ? 247 LYS A N     1 
ATOM   1900 C  CA    . LYS A 1 247 ? 17.39289  -22.35531 -9.35855  1.000 12.92250 ? 247 LYS A CA    1 
ATOM   1901 C  C     . LYS A 1 247 ? 17.55889  -22.19129 -10.86054 1.000 11.62016 ? 247 LYS A C     1 
ATOM   1902 O  O     . LYS A 1 247 ? 17.94784  -23.15029 -11.54857 1.000 13.90650 ? 247 LYS A O     1 
ATOM   1903 C  CB    . LYS A 1 247 ? 18.56185  -23.13439 -8.75857  1.000 13.21464 ? 247 LYS A CB    1 
ATOM   1904 C  CG    . LYS A 1 247 ? 19.67890  -22.27346 -8.17555  1.000 12.79510 ? 247 LYS A CG    1 
ATOM   1905 C  CD    . LYS A 1 247 ? 20.70492  -21.86349 -9.22155  0.000 12.64264 ? 247 LYS A CD    1 
ATOM   1906 C  CE    . LYS A 1 247 ? 22.12392  -21.90957 -8.65355  0.000 12.79952 ? 247 LYS A CE    1 
ATOM   1907 N  NZ    . LYS A 1 247 ? 22.33797  -20.95161 -7.53053  0.000 13.08016 ? 247 LYS A NZ    1 
ATOM   1908 N  N     . PRO A 1 248 ? 17.24595  -21.01926 -11.41851 1.000 12.43067 ? 248 PRO A N     1 
ATOM   1909 C  CA    . PRO A 1 248 ? 17.32495  -20.85023 -12.87451 1.000 11.84599 ? 248 PRO A CA    1 
ATOM   1910 C  C     . PRO A 1 248 ? 18.71293  -21.17029 -13.40752 1.000 8.94574  ? 248 PRO A C     1 
ATOM   1911 O  O     . PRO A 1 248 ? 19.72895  -20.93335 -12.75052 1.000 8.23774  ? 248 PRO A O     1 
ATOM   1912 C  CB    . PRO A 1 248 ? 16.97103  -19.37521 -13.07747 1.000 11.26072 ? 248 PRO A CB    1 
ATOM   1913 C  CG    . PRO A 1 248 ? 16.11505  -19.04319 -11.91046 1.000 11.13412 ? 248 PRO A CG    1 
ATOM   1914 C  CD    . PRO A 1 248 ? 16.68601  -19.82925 -10.75748 1.000 10.45232 ? 248 PRO A CD    1 
ATOM   1915 N  N     . ALA A 1 249 ? 18.74290  -21.72726 -14.61954 1.000 7.55644  ? 249 ALA A N     1 
ATOM   1916 C  CA    . ALA A 1 249 ? 19.97887  -22.23831 -15.19655 1.000 10.19488 ? 249 ALA A CA    1 
ATOM   1917 C  C     . ALA A 1 249 ? 20.94093  -21.14035 -15.62953 1.000 8.56585  ? 249 ALA A C     1 
ATOM   1918 O  O     . ALA A 1 249 ? 22.11891  -21.43340 -15.86454 1.000 12.16058 ? 249 ALA A O     1 
ATOM   1919 C  CB    . ALA A 1 249 ? 19.65882  -23.14426 -16.38557 1.000 11.75570 ? 249 ALA A CB    1 
ATOM   1920 N  N     . THR A 1 250 ? 20.48399  -19.89932 -15.74850 1.000 8.27982  ? 250 THR A N     1 
ATOM   1921 C  CA    . THR A 1 250 ? 21.34904  -18.79235 -16.13748 1.000 8.10682  ? 250 THR A CA    1 
ATOM   1922 C  C     . THR A 1 250 ? 21.35610  -17.73338 -15.03145 1.000 7.17221  ? 250 THR A C     1 
ATOM   1923 O  O     . THR A 1 250 ? 20.80410  -17.93138 -13.94546 1.000 11.06033 ? 250 THR A O     1 
ATOM   1924 C  CB    . THR A 1 250 ? 20.91607  -18.21730 -17.48946 1.000 6.59299  ? 250 THR A CB    1 
ATOM   1925 O  OG1   . THR A 1 250 ? 19.56209  -17.75523 -17.40945 1.000 8.17364  ? 250 THR A OG1   1 
ATOM   1926 C  CG2   . THR A 1 250 ? 21.02601  -19.28028 -18.57649 1.000 6.38273  ? 250 THR A CG2   1 
ATOM   1927 N  N     . THR A 1 251 ? 21.98516  -16.59341 -15.32343 1.000 7.45310  ? 251 THR A N     1 
ATOM   1928 C  CA    . THR A 1 251 ? 22.27721  -15.60745 -14.28741 1.000 7.30087  ? 251 THR A CA    1 
ATOM   1929 C  C     . THR A 1 251 ? 21.05025  -14.81739 -13.84738 1.000 8.19454  ? 251 THR A C     1 
ATOM   1930 O  O     . THR A 1 251 ? 21.00928  -14.34842 -12.70337 1.000 7.58410  ? 251 THR A O     1 
ATOM   1931 C  CB    . THR A 1 251 ? 23.35726  -14.63949 -14.77239 1.000 6.36190  ? 251 THR A CB    1 
ATOM   1932 O  OG1   . THR A 1 251 ? 22.86429  -13.88144 -15.88737 1.000 5.41182  ? 251 THR A OG1   1 
ATOM   1933 C  CG2   . THR A 1 251 ? 24.60722  -15.40554 -15.17941 1.000 4.62423  ? 251 THR A CG2   1 
ATOM   1934 N  N     . VAL A 1 252 ? 20.05826  -14.66032 -14.72638 1.000 7.70615  ? 252 VAL A N     1 
ATOM   1935 C  CA    . VAL A 1 252 ? 18.88430  -13.82427 -14.48035 1.000 9.18519  ? 252 VAL A CA    1 
ATOM   1936 C  C     . VAL A 1 252 ? 19.33937  -12.42330 -14.08532 1.000 7.72574  ? 252 VAL A C     1 
ATOM   1937 O  O     . VAL A 1 252 ? 18.82241  -11.82830 -13.13330 1.000 8.63863  ? 252 VAL A O     1 
ATOM   1938 C  CB    . VAL A 1 252 ? 17.96027  -14.44225 -13.41136 1.000 11.92951 ? 252 VAL A CB    1 
ATOM   1939 C  CG1   . VAL A 1 252 ? 16.55930  -13.85317 -13.50634 1.000 11.59190 ? 252 VAL A CG1   1 
ATOM   1940 C  CG2   . VAL A 1 252 ? 17.90420  -15.95424 -13.56340 1.000 10.84805 ? 252 VAL A CG2   1 
ATOM   1941 N  N     . LEU A 1 253 ? 20.32340  -11.89333 -14.80831 1.000 4.17204  ? 253 LEU A N     1 
ATOM   1942 C  CA    . LEU A 1 253 ? 20.76847  -10.51836 -14.63728 1.000 5.38419  ? 253 LEU A CA    1 
ATOM   1943 C  C     . LEU A 1 253 ? 20.19351  -9.58131  -15.68926 1.000 4.66594  ? 253 LEU A C     1 
ATOM   1944 O  O     . LEU A 1 253 ? 20.53657  -8.39532  -15.69623 1.000 8.36121  ? 253 LEU A O     1 
ATOM   1945 C  CB    . LEU A 1 253 ? 22.29847  -10.44544 -14.66528 1.000 5.18539  ? 253 LEU A CB    1 
ATOM   1946 C  CG    . LEU A 1 253 ? 23.01945  -10.95250 -13.41730 1.000 5.79279  ? 253 LEU A CG    1 
ATOM   1947 C  CD1   . LEU A 1 253 ? 24.51445  -11.04157 -13.66831 1.000 6.13186  ? 253 LEU A CD1   1 
ATOM   1948 C  CD2   . LEU A 1 253 ? 22.72550  -10.04152 -12.23328 1.000 6.42372  ? 253 LEU A CD2   1 
ATOM   1949 N  N     . SER A 1 254 ? 19.32748  -10.08124 -16.56926 1.000 4.19442  ? 254 SER A N     1 
ATOM   1950 C  CA    . SER A 1 254 ? 18.79052  -9.23919  -17.63624 1.000 5.19982  ? 254 SER A CA    1 
ATOM   1951 C  C     . SER A 1 254 ? 17.95558  -8.05716  -17.14421 1.000 5.18171  ? 254 SER A C     1 
ATOM   1952 O  O     . SER A 1 254 ? 18.11964  -6.95815  -17.70319 1.000 5.08376  ? 254 SER A O     1 
ATOM   1953 C  CB    . SER A 1 254 ? 17.99447  -10.10313 -18.62326 1.000 5.93696  ? 254 SER A CB    1 
ATOM   1954 O  OG    . SER A 1 254 ? 17.03044  -10.90809 -17.96727 1.000 3.91467  ? 254 SER A OG    1 
ATOM   1955 N  N     . PRO A 1 255 ? 17.06558  -8.18214  -16.15121 1.000 5.46763  ? 255 PRO A N     1 
ATOM   1956 C  CA    . PRO A 1 255 ? 16.32964  -6.98811  -15.70518 1.000 6.09885  ? 255 PRO A CA    1 
ATOM   1957 C  C     . PRO A 1 255 ? 17.22070  -5.95017  -15.05116 1.000 5.60961  ? 255 PRO A C     1 
ATOM   1958 O  O     . PRO A 1 255 ? 16.86476  -4.76415  -15.03913 1.000 4.23975  ? 255 PRO A O     1 
ATOM   1959 C  CB    . PRO A 1 255 ? 15.30762  -7.55308  -14.71519 1.000 5.84644  ? 255 PRO A CB    1 
ATOM   1960 C  CG    . PRO A 1 255 ? 15.95056  -8.78813  -14.20922 1.000 4.11220  ? 255 PRO A CG    1 
ATOM   1961 C  CD    . PRO A 1 255 ? 16.67952  -9.36914  -15.36724 1.000 5.18908  ? 255 PRO A CD    1 
ATOM   1962 N  N     . TYR A 1 256 ? 18.37368  -6.35624  -14.51917 1.000 4.16388  ? 256 TYR A N     1 
ATOM   1963 C  CA    . TYR A 1 256 ? 19.28673  -5.40030  -13.90815 1.000 4.24315  ? 256 TYR A CA    1 
ATOM   1964 C  C     . TYR A 1 256 ? 20.16176  -4.72632  -14.95614 1.000 7.51169  ? 256 TYR A C     1 
ATOM   1965 O  O     . TYR A 1 256 ? 20.48782  -3.54034  -14.82511 1.000 7.04931  ? 256 TYR A O     1 
ATOM   1966 C  CB    . TYR A 1 256 ? 20.14270  -6.09837  -12.85217 1.000 5.15130  ? 256 TYR A CB    1 
ATOM   1967 C  CG    . TYR A 1 256 ? 19.32766  -6.85435  -11.83119 1.000 5.82714  ? 256 TYR A CG    1 
ATOM   1968 C  CD1   . TYR A 1 256 ? 18.83470  -6.22036  -10.69817 1.000 5.67910  ? 256 TYR A CD1   1 
ATOM   1969 C  CD2   . TYR A 1 256 ? 19.03960  -8.20134  -12.00722 1.000 5.06279  ? 256 TYR A CD2   1 
ATOM   1970 C  CE1   . TYR A 1 256 ? 18.08267  -6.90834  -9.76718  1.000 7.78689  ? 256 TYR A CE1   1 
ATOM   1971 C  CE2   . TYR A 1 256 ? 18.28656  -8.89532  -11.08323 1.000 7.60029  ? 256 TYR A CE2   1 
ATOM   1972 C  CZ    . TYR A 1 256 ? 17.81060  -8.24532  -9.96522  1.000 8.06675  ? 256 TYR A CZ    1 
ATOM   1973 O  OH    . TYR A 1 256 ? 17.06257  -8.93531  -9.04123  1.000 8.27728  ? 256 TYR A OH    1 
ATOM   1974 N  N     . LEU A 1 257 ? 20.55072  -5.46532  -16.00016 1.000 4.70910  ? 257 LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 257 ? 21.30074  -4.86133  -17.09515 1.000 4.83563  ? 257 LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 257 ? 20.42079  -3.94527  -17.93112 1.000 5.92620  ? 257 LEU A C     1 
ATOM   1977 O  O     . LEU A 1 257 ? 20.91384  -2.95528  -18.48510 1.000 5.50014  ? 257 LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 257 ? 21.92169  -5.94734  -17.97318 1.000 6.64731  ? 257 LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 257 ? 23.02365  -6.78041  -17.32020 1.000 6.03225  ? 257 LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 257 ? 23.28558  -8.04341  -18.12623 1.000 7.15686  ? 257 LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 257 ? 24.29169  -5.95848  -17.19019 1.000 7.74838  ? 257 LEU A CD2   1 
ATOM   1982 N  N     . LYS A 1 258 ? 19.12277  -4.25220  -18.02813 1.000 5.03390  ? 258 LYS A N     1 
ATOM   1983 C  CA    . LYS A 1 258 ? 18.20281  -3.38013  -18.75210 1.000 5.29376  ? 258 LYS A CA    1 
ATOM   1984 C  C     . LYS A 1 258 ? 18.09888  -2.01814  -18.07807 1.000 5.58003  ? 258 LYS A C     1 
ATOM   1985 O  O     . LYS A 1 258 ? 18.30093  -0.97914  -18.71705 1.000 6.09629  ? 258 LYS A O     1 
ATOM   1986 C  CB    . LYS A 1 258 ? 16.82378  -4.04106  -18.85611 1.000 6.20721  ? 258 LYS A CB    1 
ATOM   1987 C  CG    . LYS A 1 258 ? 15.75182  -3.21299  -19.57609 1.000 10.10135 ? 258 LYS A CG    1 
ATOM   1988 C  CD    . LYS A 1 258 ? 14.93687  -2.34197  -18.61606 1.000 8.24063  ? 258 LYS A CD    1 
ATOM   1989 C  CE    . LYS A 1 258 ? 13.75790  -1.68290  -19.31904 1.000 10.00986 ? 258 LYS A CE    1 
ATOM   1990 N  NZ    . LYS A 1 258 ? 14.14792  -1.02989  -20.60003 1.000 15.88357 ? 258 LYS A NZ    1 
ATOM   1991 N  N     . PHE A 1 259 ? 17.75889  -2.00416  -16.79007 1.000 4.65326  ? 259 PHE A N     1 
ATOM   1992 C  CA    . PHE A 1 259 ? 17.59896  -0.76217  -16.04504 1.000 6.59044  ? 259 PHE A CA    1 
ATOM   1993 C  C     . PHE A 1 259 ? 18.92199  -0.13224  -15.63603 1.000 8.31845  ? 259 PHE A C     1 
ATOM   1994 O  O     . PHE A 1 259 ? 18.91105  0.94974   -15.03800 1.000 7.34957  ? 259 PHE A O     1 
ATOM   1995 C  CB    . PHE A 1 259 ? 16.74995  -1.00015  -14.79704 1.000 6.60345  ? 259 PHE A CB    1 
ATOM   1996 C  CG    . PHE A 1 259 ? 15.28094  -1.08007  -15.07104 1.000 5.31923  ? 259 PHE A CG    1 
ATOM   1997 C  CD1   . PHE A 1 259 ? 14.56800  0.05297   -15.42501 1.000 6.27123  ? 259 PHE A CD1   1 
ATOM   1998 C  CD2   . PHE A 1 259 ? 14.60688  -2.28304  -14.96106 1.000 4.85666  ? 259 PHE A CD2   1 
ATOM   1999 C  CE1   . PHE A 1 259 ? 13.21200  -0.01795  -15.67400 1.000 8.71358  ? 259 PHE A CE1   1 
ATOM   2000 C  CE2   . PHE A 1 259 ? 13.25388  -2.35897  -15.20406 1.000 5.46480  ? 259 PHE A CE2   1 
ATOM   2001 C  CZ    . PHE A 1 259 ? 12.55493  -1.22692  -15.56103 1.000 5.89887  ? 259 PHE A CZ    1 
ATOM   2002 N  N     . GLY A 1 260 ? 20.04996  -0.76829  -15.93605 1.000 9.07617  ? 260 GLY A N     1 
ATOM   2003 C  CA    . GLY A 1 260 ? 21.32199  -0.21837  -15.51904 1.000 8.15570  ? 260 GLY A CA    1 
ATOM   2004 C  C     . GLY A 1 260 ? 21.62198  -0.37342  -14.04704 1.000 9.59411  ? 260 GLY A C     1 
ATOM   2005 O  O     . GLY A 1 260 ? 22.51702  0.30352   -13.53503 1.000 9.81442  ? 260 GLY A O     1 
ATOM   2006 N  N     . CYS A 1 261 ? 20.88594  -1.23740  -13.34206 1.000 6.33021  ? 261 CYS A N     1 
ATOM   2007 C  CA    . CYS A 1 261 ? 21.21093  -1.54345  -11.95307 1.000 6.82206  ? 261 CYS A CA    1 
ATOM   2008 C  C     . CYS A 1 261 ? 22.55390  -2.24552  -11.82809 1.000 6.60990  ? 261 CYS A C     1 
ATOM   2009 O  O     . CYS A 1 261 ? 23.19291  -2.15557  -10.77409 1.000 9.12109  ? 261 CYS A O     1 
ATOM   2010 C  CB    . CYS A 1 261 ? 20.11889  -2.41641  -11.33009 1.000 7.98205  ? 261 CYS A CB    1 
ATOM   2011 S  SG    . CYS A 1 261 ? 18.45993  -1.71932  -11.40506 1.000 7.76709  ? 261 CYS A SG    1 
ATOM   2012 N  N     . LEU A 1 262 ? 22.98286  -2.94551  -12.87411 1.000 6.02284  ? 262 LEU A N     1 
ATOM   2013 C  CA    . LEU A 1 262 ? 24.27882  -3.60258  -12.92413 1.000 7.30844  ? 262 LEU A CA    1 
ATOM   2014 C  C     . LEU A 1 262 ? 25.05385  -3.09159  -14.13012 1.000 6.45855  ? 262 LEU A C     1 
ATOM   2015 O  O     . LEU A 1 262 ? 24.49985  -2.97054  -15.22712 1.000 7.64556  ? 262 LEU A O     1 
ATOM   2016 C  CB    . LEU A 1 262 ? 24.12675  -5.12557  -13.00917 1.000 5.86817  ? 262 LEU A CB    1 
ATOM   2017 C  CG    . LEU A 1 262 ? 25.41771  -5.94663  -13.02019 1.000 6.77804  ? 262 LEU A CG    1 
ATOM   2018 C  CD1   . LEU A 1 262 ? 26.13972  -5.82770  -11.68819 1.000 8.05662  ? 262 LEU A CD1   1 
ATOM   2019 C  CD2   . LEU A 1 262 ? 25.14263  -7.40461  -13.36022 1.000 6.54158  ? 262 LEU A CD2   1 
ATOM   2020 N  N     . SER A 1 263 ? 26.33486  -2.79766  -13.92212 1.000 6.97998  ? 263 SER A N     1 
ATOM   2021 C  CA    . SER A 1 263 ? 27.19888  -2.32968  -14.99811 1.000 6.37296  ? 263 SER A CA    1 
ATOM   2022 C  C     . SER A 1 263 ? 27.62882  -3.49868  -15.87314 1.000 6.88965  ? 263 SER A C     1 
ATOM   2023 O  O     . SER A 1 263 ? 28.10077  -4.52271  -15.36617 1.000 5.35511  ? 263 SER A O     1 
ATOM   2024 C  CB    . SER A 1 263 ? 28.43092  -1.62675  -14.43010 1.000 9.71702  ? 263 SER A CB    1 
ATOM   2025 O  OG    . SER A 1 263 ? 29.37693  -1.35778  -15.45610 1.000 9.19941  ? 263 SER A OG    1 
ATOM   2026 N  N     . ALA A 1 264 ? 27.46582  -3.34264  -17.19114 1.000 4.47344  ? 264 ALA A N     1 
ATOM   2027 C  CA    . ALA A 1 264 ? 27.94277  -4.35964  -18.12216 1.000 4.59365  ? 264 ALA A CA    1 
ATOM   2028 C  C     . ALA A 1 264 ? 29.46276  -4.43572  -18.11617 1.000 6.77678  ? 264 ALA A C     1 
ATOM   2029 O  O     . ALA A 1 264 ? 30.03471  -5.52174  -18.25520 1.000 4.61799  ? 264 ALA A O     1 
ATOM   2030 C  CB    . ALA A 1 264 ? 27.42377  -4.06758  -19.53215 1.000 4.43343  ? 264 ALA A CB    1 
ATOM   2031 N  N     . ARG A 1 265 ? 30.13195  -3.29195  -17.94762 1.000 7.26103  ? 265 ARG A N     1 
ATOM   2032 C  CA    . ARG A 1 265 ? 31.59242  -3.28261  -17.90974 1.000 9.64295  ? 265 ARG A CA    1 
ATOM   2033 C  C     . ARG A 1 265 ? 32.12978  -3.91112  -16.62982 1.000 8.10152  ? 265 ARG A C     1 
ATOM   2034 O  O     . ARG A 1 265 ? 33.20996  -4.51252  -16.64771 1.000 9.38330  ? 265 ARG A O     1 
ATOM   2035 C  CB    . ARG A 1 265 ? 32.10666  -1.85227  -18.06415 1.000 8.74237  ? 265 ARG A CB    1 
ATOM   2036 C  CG    . ARG A 1 265 ? 31.81829  -1.24093  -19.42940 1.000 10.12030 ? 265 ARG A CG    1 
ATOM   2037 C  CD    . ARG A 1 265 ? 32.17203  0.23283   -19.46851 1.000 9.03098  ? 265 ARG A CD    1 
ATOM   2038 N  NE    . ARG A 1 265 ? 31.93747  0.81418   -20.78660 1.000 10.47543 ? 265 ARG A NE    1 
ATOM   2039 C  CZ    . ARG A 1 265 ? 32.06030  2.10435   -21.06787 1.000 11.37914 ? 265 ARG A CZ    1 
ATOM   2040 N  NH1   . ARG A 1 265 ? 32.41688  2.98121   -20.14193 1.000 12.16576 ? 265 ARG A NH1   1 
ATOM   2041 N  NH2   . ARG A 1 265 ? 31.81583  2.52558   -22.30741 1.000 10.27930 ? 265 ARG A NH2   1 
ATOM   2042 N  N     . LEU A 1 266 ? 31.40681  -3.77888  -15.51616 1.000 8.02875  ? 266 LEU A N     1 
ATOM   2043 C  CA    . LEU A 1 266 ? 31.77777  -4.49793  -14.30018 1.000 9.45616  ? 266 LEU A CA    1 
ATOM   2044 C  C     . LEU A 1 266 ? 31.59670  -5.99891  -14.48222 1.000 8.34143  ? 266 LEU A C     1 
ATOM   2045 O  O     . LEU A 1 266 ? 32.47366  -6.79197  -14.12024 1.000 8.21213  ? 266 LEU A O     1 
ATOM   2046 C  CB    . LEU A 1 266 ? 30.94780  -3.99791  -13.11617 1.000 7.45365  ? 266 LEU A CB    1 
ATOM   2047 C  CG    . LEU A 1 266 ? 31.00877  -4.83694  -11.83419 1.000 15.65686 ? 266 LEU A CG    1 
ATOM   2048 C  CD1   . LEU A 1 266 ? 32.36478  -4.71003  -11.15019 1.000 16.14006 ? 266 LEU A CD1   1 
ATOM   2049 C  CD2   . LEU A 1 266 ? 29.87779  -4.47091  -10.87417 1.000 12.40720 ? 266 LEU A CD2   1 
ATOM   2050 N  N     . PHE A 1 267 ? 30.45167  -6.40484  -15.03122 1.000 7.57192  ? 267 PHE A N     1 
ATOM   2051 C  CA    . PHE A 1 267 ? 30.23460  -7.80082  -15.38925 1.000 6.46576  ? 267 PHE A CA    1 
ATOM   2052 C  C     . PHE A 1 267 ? 31.37057  -8.31986  -16.26727 1.000 6.66853  ? 267 PHE A C     1 
ATOM   2053 O  O     . PHE A 1 267 ? 31.95352  -9.37789  -15.99830 1.000 5.53844  ? 267 PHE A O     1 
ATOM   2054 C  CB    . PHE A 1 267 ? 28.87959  -7.91974  -16.09525 1.000 7.81700  ? 267 PHE A CB    1 
ATOM   2055 C  CG    . PHE A 1 267 ? 28.32952  -9.31971  -16.16628 1.000 7.46135  ? 267 PHE A CG    1 
ATOM   2056 C  CD1   . PHE A 1 267 ? 29.09147  -10.41575 -15.79531 1.000 7.52111  ? 267 PHE A CD1   1 
ATOM   2057 C  CD2   . PHE A 1 267 ? 27.03651  -9.53363  -16.61828 1.000 9.40255  ? 267 PHE A CD2   1 
ATOM   2058 C  CE1   . PHE A 1 267 ? 28.57740  -11.69973 -15.87334 1.000 10.27834 ? 267 PHE A CE1   1 
ATOM   2059 C  CE2   . PHE A 1 267 ? 26.51444  -10.81660 -16.69831 1.000 8.19267  ? 267 PHE A CE2   1 
ATOM   2060 C  CZ    . PHE A 1 267 ? 27.28839  -11.90165 -16.32434 1.000 6.45898  ? 267 PHE A CZ    1 
ATOM   2061 N  N     . HIS A 1 268 ? 31.71261  -7.56685  -17.31725 1.000 5.40113  ? 268 HIS A N     1 
ATOM   2062 C  CA    . HIS A 1 268 ? 32.77758  -7.98788  -18.22127 1.000 7.32130  ? 268 HIS A CA    1 
ATOM   2063 C  C     . HIS A 1 268 ? 34.13258  -8.00797  -17.52927 1.000 7.73719  ? 268 HIS A C     1 
ATOM   2064 O  O     . HIS A 1 268 ? 34.98054  -8.84700  -17.85730 1.000 8.39528  ? 268 HIS A O     1 
ATOM   2065 C  CB    . HIS A 1 268 ? 32.82662  -7.06986  -19.44225 1.000 8.61256  ? 268 HIS A CB    1 
ATOM   2066 C  CG    . HIS A 1 268 ? 33.64759  -7.61087  -20.57126 1.000 7.88133  ? 268 HIS A CG    1 
ATOM   2067 N  ND1   . HIS A 1 268 ? 35.02360  -7.52994  -20.59927 1.000 6.65714  ? 268 HIS A ND1   1 
ATOM   2068 C  CD2   . HIS A 1 268 ? 33.28556  -8.24483  -21.71228 1.000 5.54296  ? 268 HIS A CD2   1 
ATOM   2069 C  CE1   . HIS A 1 268 ? 35.47356  -8.08994  -21.70828 1.000 7.81998  ? 268 HIS A CE1   1 
ATOM   2070 N  NE2   . HIS A 1 268 ? 34.43854  -8.52887  -22.40129 1.000 7.48587  ? 268 HIS A NE2   1 
ATOM   2071 N  N     . ALA A 1 269 ? 34.35963  -7.09800  -16.57925 1.000 7.10474  ? 269 ALA A N     1 
ATOM   2072 C  CA    . ALA A 1 269 ? 35.63164  -7.08408  -15.86326 1.000 7.68483  ? 269 ALA A CA    1 
ATOM   2073 C  C     . ALA A 1 269 ? 35.77058  -8.30311  -14.96429 1.000 8.33273  ? 269 ALA A C     1 
ATOM   2074 O  O     . ALA A 1 269 ? 36.86855  -8.85117  -14.81630 1.000 7.66016  ? 269 ALA A O     1 
ATOM   2075 C  CB    . ALA A 1 269 ? 35.76570  -5.80011  -15.04823 1.000 9.10647  ? 269 ALA A CB    1 
ATOM   2076 N  N     . ARG A 1 270 ? 34.67037  -8.74615  -14.35551 1.000 9.81762  ? 270 ARG A N     1 
ATOM   2077 C  CA    . ARG A 1 270 ? 34.73639  -9.92333  -13.49546 1.000 9.11025  ? 270 ARG A CA    1 
ATOM   2078 C  C     . ARG A 1 270 ? 34.89538  -11.20076 -14.30788 1.000 10.30313 ? 270 ARG A C     1 
ATOM   2079 O  O     . ARG A 1 270 ? 35.51725  -12.16045 -13.82949 1.000 16.00220 ? 270 ARG A O     1 
ATOM   2080 C  CB    . ARG A 1 270 ? 33.48918  -10.00131 -12.61799 1.000 11.57793 ? 270 ARG A CB    1 
ATOM   2081 C  CG    . ARG A 1 270 ? 33.30860  -8.80961  -11.68565 1.000 13.67000 ? 270 ARG A CG    1 
ATOM   2082 C  CD    . ARG A 1 270 ? 34.18899  -8.91751  -10.44902 1.000 11.37645 ? 270 ARG A CD    1 
ATOM   2083 N  NE    . ARG A 1 270 ? 33.88191  -10.11090 -9.66897  1.000 14.73112 ? 270 ARG A NE    1 
ATOM   2084 C  CZ    . ARG A 1 270 ? 32.86322  -10.21422 -8.82500  1.000 21.76251 ? 270 ARG A CZ    1 
ATOM   2085 N  NH1   . ARG A 1 270 ? 32.02483  -9.21138  -8.62699  1.000 23.85090 ? 270 ARG A NH1   1 
ATOM   2086 N  NH2   . ARG A 1 270 ? 32.67739  -11.35475 -8.16621  1.000 21.88019 ? 270 ARG A NH2   1 
ATOM   2087 N  N     . LEU A 1 271 ? 34.35643  -11.23603 -15.52935 1.000 6.24301  ? 271 LEU A N     1 
ATOM   2088 C  CA    . LEU A 1 271 ? 34.50136  -12.43001 -16.35838 1.000 9.46603  ? 271 LEU A CA    1 
ATOM   2089 C  C     . LEU A 1 271 ? 35.94835  -12.63408 -16.78839 1.000 11.84510 ? 271 LEU A C     1 
ATOM   2090 O  O     . LEU A 1 271 ? 36.42929  -13.77210 -16.84242 1.000 12.01017 ? 271 LEU A O     1 
ATOM   2091 C  CB    . LEU A 1 271 ? 33.59236  -12.33594 -17.58237 1.000 8.37224  ? 271 LEU A CB    1 
ATOM   2092 C  CG    . LEU A 1 271 ? 32.09836  -12.49287 -17.31337 1.000 6.96950  ? 271 LEU A CG    1 
ATOM   2093 C  CD1   . LEU A 1 271 ? 31.30237  -12.10780 -18.54236 1.000 7.38369  ? 271 LEU A CD1   1 
ATOM   2094 C  CD2   . LEU A 1 271 ? 31.79029  -13.92286 -16.90440 1.000 8.24075  ? 271 LEU A CD2   1 
ATOM   2095 N  N     . LEU A 1 272 ? 36.65441  -11.54611 -17.10437 1.000 8.97634  ? 272 LEU A N     1 
ATOM   2096 C  CA    . LEU A 1 272 ? 38.05140  -11.66817 -17.50538 1.000 11.49833 ? 272 LEU A CA    1 
ATOM   2097 C  C     . LEU A 1 272 ? 38.91938  -12.17124 -16.36039 1.000 13.24055 ? 272 LEU A C     1 
ATOM   2098 O  O     . LEU A 1 272 ? 39.88634  -12.90328 -16.59441 1.000 14.32437 ? 272 LEU A O     1 
ATOM   2099 C  CB    . LEU A 1 272 ? 38.57046  -10.32818 -18.02535 1.000 11.07963 ? 272 LEU A CB    1 
ATOM   2100 C  CG    . LEU A 1 272 ? 37.95448  -9.82012  -19.33233 1.000 11.62602 ? 272 LEU A CG    1 
ATOM   2101 C  CD1   . LEU A 1 272 ? 38.51955  -8.45314  -19.69230 1.000 13.10494 ? 272 LEU A CD1   1 
ATOM   2102 C  CD2   . LEU A 1 272 ? 38.18843  -10.81210 -20.46336 1.000 15.37354 ? 272 LEU A CD2   1 
ATOM   2103 N  N     . GLU A 1 273 ? 38.59040  -11.80125 -15.12038 1.000 12.91612 ? 273 GLU A N     1 
ATOM   2104 C  CA    . GLU A 1 273 ? 39.34938  -12.30732 -13.98140 1.000 14.99728 ? 273 GLU A CA    1 
ATOM   2105 C  C     . GLU A 1 273 ? 39.25630  -13.82531 -13.89143 1.000 13.49132 ? 273 GLU A C     1 
ATOM   2106 O  O     . GLU A 1 273 ? 40.26127  -14.50437 -13.64245 1.000 10.73783 ? 273 GLU A O     1 
ATOM   2107 C  CB    . GLU A 1 273 ? 38.85042  -11.65932 -12.69138 1.000 19.15327 ? 273 GLU A CB    1 
ATOM   2108 C  CG    . GLU A 1 273 ? 39.00949  -10.14533 -12.64634 1.000 20.56815 ? 273 GLU A CG    1 
ATOM   2109 C  CD    . GLU A 1 273 ? 38.41553  -9.54733  -11.38533 1.000 27.53778 ? 273 GLU A CD    1 
ATOM   2110 O  OE1   . GLU A 1 273 ? 37.95549  -10.32933 -10.52734 1.000 31.00710 ? 273 GLU A OE1   1 
ATOM   2111 O  OE2   . GLU A 1 273 ? 38.40059  -8.30533  -11.24930 1.000 29.40777 ? 273 GLU A OE2   1 
ATOM   2112 N  N     . VAL A 1 274 ? 38.05927  -14.37725 -14.11044 1.000 13.09836 ? 274 VAL A N     1 
ATOM   2113 C  CA    . VAL A 1 274 ? 37.87820  -15.82624 -14.04647 1.000 15.74604 ? 274 VAL A CA    1 
ATOM   2114 C  C     . VAL A 1 274 ? 38.51516  -16.50224 -15.25449 1.000 11.20138 ? 274 VAL A C     1 
ATOM   2115 O  O     . VAL A 1 274 ? 39.12011  -17.57528 -15.13352 1.000 12.85835 ? 274 VAL A O     1 
ATOM   2116 C  CB    . VAL A 1 274 ? 36.38218  -16.17517 -13.92648 1.000 11.77582 ? 274 VAL A CB    1 
ATOM   2117 C  CG1   . VAL A 1 274 ? 36.17011  -17.68415 -14.02551 1.000 11.05758 ? 274 VAL A CG1   1 
ATOM   2118 C  CG2   . VAL A 1 274 ? 35.81722  -15.64117 -12.62146 1.000 11.19693 ? 274 VAL A CG2   1 
ATOM   2119 N  N     . TYR A 1 275 ? 38.39419  -15.88721 -16.43548 1.000 9.29092  ? 275 TYR A N     1 
ATOM   2120 C  CA    . TYR A 1 275 ? 38.95215  -16.47921 -17.64949 1.000 11.18745 ? 275 TYR A CA    1 
ATOM   2121 C  C     . TYR A 1 275 ? 40.47115  -16.56329 -17.58950 1.000 12.00123 ? 275 TYR A C     1 
ATOM   2122 O  O     . TYR A 1 275 ? 41.06410  -17.49830 -18.14253 1.000 9.80052  ? 275 TYR A O     1 
ATOM   2123 C  CB    . TYR A 1 275 ? 38.53119  -15.67116 -18.87947 1.000 8.85952  ? 275 TYR A CB    1 
ATOM   2124 C  CG    . TYR A 1 275 ? 37.07018  -15.79808 -19.25747 1.000 9.30331  ? 275 TYR A CG    1 
ATOM   2125 C  CD1   . TYR A 1 275 ? 36.24614  -16.72705 -18.63549 1.000 6.19213  ? 275 TYR A CD1   1 
ATOM   2126 C  CD2   . TYR A 1 275 ? 36.51922  -14.99303 -20.24545 1.000 7.75721  ? 275 TYR A CD2   1 
ATOM   2127 C  CE1   . TYR A 1 275 ? 34.91413  -16.84797 -18.98549 1.000 9.25454  ? 275 TYR A CE1   1 
ATOM   2128 C  CE2   . TYR A 1 275 ? 35.18821  -15.10595 -20.60145 1.000 8.19588  ? 275 TYR A CE2   1 
ATOM   2129 C  CZ    . TYR A 1 275 ? 34.39017  -16.03492 -19.96846 1.000 7.49144  ? 275 TYR A CZ    1 
ATOM   2130 O  OH    . TYR A 1 275 ? 33.06416  -16.14985 -20.31646 1.000 6.01165  ? 275 TYR A OH    1 
ATOM   2131 N  N     . ARG A 1 276 ? 41.11846  -15.60712 -16.91488 1.000 14.62099 ? 276 ARG A N     1 
ATOM   2132 C  CA    . ARG A 1 276 ? 42.57784  -15.59480 -16.85250 1.000 14.07199 ? 276 ARG A CA    1 
ATOM   2133 C  C     . ARG A 1 276 ? 43.12379  -16.78376 -16.07348 1.000 13.46619 ? 276 ARG A C     1 
ATOM   2134 O  O     . ARG A 1 276 ? 44.20695  -17.29203 -16.38008 1.000 16.29470 ? 276 ARG A O     1 
ATOM   2135 C  CB    . ARG A 1 276 ? 43.06515  -14.27847 -16.24053 1.000 15.35655 ? 276 ARG A CB    1 
ATOM   2136 C  CG    . ARG A 1 276 ? 42.94259  -13.09982 -17.20330 1.000 16.89128 ? 276 ARG A CG    1 
ATOM   2137 C  CD    . ARG A 1 276 ? 43.29547  -11.75038 -16.59130 0.000 18.30216 ? 276 ARG A CD    1 
ATOM   2138 N  NE    . ARG A 1 276 ? 42.82147  -10.66789 -17.44849 0.000 18.86956 ? 276 ARG A NE    1 
ATOM   2139 C  CZ    . ARG A 1 276 ? 43.20050  -9.39979  -17.35753 0.000 20.36396 ? 276 ARG A CZ    1 
ATOM   2140 N  NH1   . ARG A 1 276 ? 44.08075  -9.00229  -16.45346 0.000 21.35860 ? 276 ARG A NH1   1 
ATOM   2141 N  NH2   . ARG A 1 276 ? 42.68751  -8.50834  -18.20139 0.000 20.48565 ? 276 ARG A NH2   1 
ATOM   2142 N  N     . ARG A 1 277 ? 42.38254  -17.25275 -15.07082 1.000 12.56997 ? 277 ARG A N     1 
ATOM   2143 C  CA    . ARG A 1 277 ? 42.80257  -18.38603 -14.25722 1.000 14.04379 ? 277 ARG A CA    1 
ATOM   2144 C  C     . ARG A 1 277 ? 42.20631  -19.70318 -14.72832 1.000 13.70600 ? 277 ARG A C     1 
ATOM   2145 O  O     . ARG A 1 277 ? 42.52259  -20.75128 -14.15560 1.000 12.80509 ? 277 ARG A O     1 
ATOM   2146 C  CB    . ARG A 1 277 ? 42.42942  -18.15443 -12.78945 1.000 15.98167 ? 277 ARG A CB    1 
ATOM   2147 C  CG    . ARG A 1 277 ? 42.96990  -16.86551 -12.19290 1.000 15.55012 ? 277 ARG A CG    1 
ATOM   2148 C  CD    . ARG A 1 277 ? 41.94425  -16.26784 -11.23925 1.000 18.76032 ? 277 ARG A CD    1 
ATOM   2149 N  NE    . ARG A 1 277 ? 42.51329  -15.27206 -10.33829 0.000 18.04769 ? 277 ARG A NE    1 
ATOM   2150 C  CZ    . ARG A 1 277 ? 43.18400  -15.56457 -9.23201  0.000 18.49036 ? 277 ARG A CZ    1 
ATOM   2151 N  NH1   . ARG A 1 277 ? 43.43548  -16.81687 -8.88818  0.000 18.52248 ? 277 ARG A NH1   1 
ATOM   2152 N  NH2   . ARG A 1 277 ? 43.61535  -14.57655 -8.45228  0.000 18.74348 ? 277 ARG A NH2   1 
ATOM   2153 N  N     . HIS A 1 278 ? 41.35400  -19.67638 -15.75358 1.000 13.63815 ? 278 HIS A N     1 
ATOM   2154 C  CA    . HIS A 1 278 ? 40.72594  -20.87733 -16.30360 1.000 13.75782 ? 278 HIS A CA    1 
ATOM   2155 C  C     . HIS A 1 278 ? 40.96593  -20.88431 -17.80860 1.000 11.82547 ? 278 HIS A C     1 
ATOM   2156 O  O     . HIS A 1 278 ? 40.16196  -20.34425 -18.58059 1.000 13.46080 ? 278 HIS A O     1 
ATOM   2157 C  CB    . HIS A 1 278 ? 39.23494  -20.92726 -15.97860 1.000 12.22756 ? 278 HIS A CB    1 
ATOM   2158 C  CG    . HIS A 1 278 ? 38.93894  -21.04828 -14.51660 1.000 14.17677 ? 278 HIS A CG    1 
ATOM   2159 N  ND1   . HIS A 1 278 ? 39.04199  -19.98531 -13.64458 1.000 12.17554 ? 278 HIS A ND1   1 
ATOM   2160 C  CD2   . HIS A 1 278 ? 38.53989  -22.10728 -13.77262 1.000 12.94012 ? 278 HIS A CD2   1 
ATOM   2161 C  CE1   . HIS A 1 278 ? 38.71998  -20.38432 -12.42658 1.000 12.85346 ? 278 HIS A CE1   1 
ATOM   2162 N  NE2   . HIS A 1 278 ? 38.41191  -21.66830 -12.47761 1.000 12.48027 ? 278 HIS A NE2   1 
ATOM   2163 N  N     . PRO A 1 279 ? 42.06590  -21.49235 -18.26062 1.000 8.75935  ? 279 PRO A N     1 
ATOM   2164 C  CA    . PRO A 1 279 ? 42.42290  -21.40634 -19.68662 1.000 10.76485 ? 279 PRO A CA    1 
ATOM   2165 C  C     . PRO A 1 279 ? 41.48586  -22.16927 -20.60564 1.000 12.25735 ? 279 PRO A C     1 
ATOM   2166 O  O     . PRO A 1 279 ? 41.45387  -21.87424 -21.80663 1.000 10.38375 ? 279 PRO A O     1 
ATOM   2167 C  CB    . PRO A 1 279 ? 43.84087  -21.98941 -19.72964 1.000 10.56632 ? 279 PRO A CB    1 
ATOM   2168 C  CG    . PRO A 1 279 ? 43.90483  -22.89444 -18.54266 1.000 13.07546 ? 279 PRO A CG    1 
ATOM   2169 C  CD    . PRO A 1 279 ? 43.06586  -22.23942 -17.48164 1.000 12.57801 ? 279 PRO A CD    1 
ATOM   2170 N  N     . ALA A 1 280 ? 40.73181  -23.14024 -20.09066 1.000 11.53939 ? 280 ALA A N     1 
ATOM   2171 C  CA    . ALA A 1 280 ? 39.75277  -23.87117 -20.88167 1.000 12.21770 ? 280 ALA A CA    1 
ATOM   2172 C  C     . ALA A 1 280 ? 38.36680  -23.23810 -20.83065 1.000 11.61863 ? 280 ALA A C     1 
ATOM   2173 O  O     . ALA A 1 280 ? 37.36776  -23.93505 -21.04266 1.000 11.29736 ? 280 ALA A O     1 
ATOM   2174 C  CB    . ALA A 1 280 ? 39.68270  -25.32918 -20.41970 1.000 14.53090 ? 280 ALA A CB    1 
ATOM   2175 N  N     . HIS A 1 281 ? 38.28387  -21.93811 -20.55862 1.000 10.51771 ? 281 HIS A N     1 
ATOM   2176 C  CA    . HIS A 1 281 ? 36.99090  -21.27804 -20.45560 1.000 9.57873  ? 281 HIS A CA    1 
ATOM   2177 C  C     . HIS A 1 281 ? 36.30190  -21.22398 -21.81259 1.000 10.58463 ? 281 HIS A C     1 
ATOM   2178 O  O     . HIS A 1 281 ? 36.94490  -21.19198 -22.86560 1.000 7.74158  ? 281 HIS A O     1 
ATOM   2179 C  CB    . HIS A 1 281 ? 37.15297  -19.86307 -19.90057 1.000 9.74901  ? 281 HIS A CB    1 
ATOM   2180 C  CG    . HIS A 1 281 ? 37.85002  -18.92308 -20.83455 1.000 9.33220  ? 281 HIS A CG    1 
ATOM   2181 N  ND1   . HIS A 1 281 ? 37.17405  -18.14902 -21.75353 1.000 9.22327  ? 281 HIS A ND1   1 
ATOM   2182 C  CD2   . HIS A 1 281 ? 39.16303  -18.63414 -20.99254 1.000 10.99581 ? 281 HIS A CD2   1 
ATOM   2183 C  CE1   . HIS A 1 281 ? 38.04109  -17.42505 -22.43751 1.000 10.23256 ? 281 HIS A CE1   1 
ATOM   2184 N  NE2   . HIS A 1 281 ? 39.25508  -17.69912 -21.99452 1.000 10.99870 ? 281 HIS A NE2   1 
ATOM   2185 N  N     . SER A 1 282 ? 34.97290  -21.21291 -21.77659 1.000 11.23241 ? 282 SER A N     1 
ATOM   2186 C  CA    . SER A 1 282 ? 34.19490  -21.13684 -23.00258 1.000 13.23281 ? 282 SER A CA    1 
ATOM   2187 C  C     . SER A 1 282 ? 34.42596  -19.80184 -23.70855 1.000 12.99921 ? 282 SER A C     1 
ATOM   2188 O  O     . SER A 1 282 ? 34.72502  -18.78087 -23.08353 1.000 11.15864 ? 282 SER A O     1 
ATOM   2189 C  CB    . SER A 1 282 ? 32.70889  -21.33577 -22.69858 1.000 10.76841 ? 282 SER A CB    1 
ATOM   2190 O  OG    . SER A 1 282 ? 32.28593  -20.51978 -21.61856 1.000 10.41398 ? 282 SER A OG    1 
ATOM   2191 N  N     . GLN A 1 283 ? 34.29296  -19.82580 -25.02755 1.000 11.02587 ? 283 GLN A N     1 
ATOM   2192 C  CA    . GLN A 1 283 ? 34.52501  -18.69579 -25.90853 1.000 10.70705 ? 283 GLN A CA    1 
ATOM   2193 C  C     . GLN A 1 283 ? 33.21303  -18.29971 -26.58251 1.000 10.79414 ? 283 GLN A C     1 
ATOM   2194 O  O     . GLN A 1 283 ? 32.25799  -19.08866 -26.59553 1.000 12.54467 ? 283 GLN A O     1 
ATOM   2195 C  CB    . GLN A 1 283 ? 35.58799  -19.05882 -26.95954 1.000 14.83961 ? 283 GLN A CB    1 
ATOM   2196 C  CG    . GLN A 1 283 ? 36.70604  -18.02887 -27.15952 1.000 20.02591 ? 283 GLN A CG    1 
ATOM   2197 C  CD    . GLN A 1 283 ? 37.71804  -18.00595 -26.02852 1.000 19.18568 ? 283 GLN A CD    1 
ATOM   2198 O  OE1   . GLN A 1 283 ? 38.20710  -16.94398 -25.63950 1.000 20.09262 ? 283 GLN A OE1   1 
ATOM   2199 N  NE2   . GLN A 1 283 ? 38.04999  -19.18198 -25.50555 1.000 19.21968 ? 283 GLN A NE2   1 
ATOM   2200 N  N     . PRO A 1 284 ? 33.11509  -17.08669 -27.11848 1.000 10.22998 ? 284 PRO A N     1 
ATOM   2201 C  CA    . PRO A 1 284 ? 31.89310  -16.69061 -27.82047 1.000 12.26970 ? 284 PRO A CA    1 
ATOM   2202 C  C     . PRO A 1 284 ? 31.55905  -17.66857 -28.92349 1.000 12.55587 ? 284 PRO A C     1 
ATOM   2203 O  O     . PRO A 1 284 ? 32.44401  -18.35760 -29.46651 1.000 15.36512 ? 284 PRO A O     1 
ATOM   2204 C  CB    . PRO A 1 284 ? 32.24117  -15.30662 -28.38344 1.000 14.51413 ? 284 PRO A CB    1 
ATOM   2205 C  CG    . PRO A 1 284 ? 33.22420  -14.75669 -27.41943 1.000 11.92074 ? 284 PRO A CG    1 
ATOM   2206 C  CD    . PRO A 1 284 ? 34.01815  -15.93574 -26.90946 1.000 12.67766 ? 284 PRO A CD    1 
ATOM   2207 N  N     . PRO A 1 285 ? 30.27804  -17.76550 -29.30549 1.000 12.46205 ? 285 PRO A N     1 
ATOM   2208 C  CA    . PRO A 1 285 ? 29.13508  -16.99545 -28.79247 1.000 13.13032 ? 285 PRO A CA    1 
ATOM   2209 C  C     . PRO A 1 285 ? 28.43606  -17.66044 -27.60748 1.000 11.70714 ? 285 PRO A C     1 
ATOM   2210 O  O     . PRO A 1 285 ? 27.44908  -17.13640 -27.09946 1.000 12.66602 ? 285 PRO A O     1 
ATOM   2211 C  CB    . PRO A 1 285 ? 28.21808  -16.92937 -30.01546 1.000 13.77775 ? 285 PRO A CB    1 
ATOM   2212 C  CG    . PRO A 1 285 ? 28.42001  -18.28437 -30.65649 1.000 13.70770 ? 285 PRO A CG    1 
ATOM   2213 C  CD    . PRO A 1 285 ? 29.87800  -18.63545 -30.42651 1.000 12.97992 ? 285 PRO A CD    1 
ATOM   2214 N  N     . VAL A 1 286 ? 28.92500  -18.81248 -27.14451 1.000 8.74346  ? 286 VAL A N     1 
ATOM   2215 C  CA    . VAL A 1 286 ? 28.21796  -19.57547 -26.12052 1.000 9.44697  ? 286 VAL A CA    1 
ATOM   2216 C  C     . VAL A 1 286 ? 28.60599  -19.18152 -24.70052 1.000 9.15378  ? 286 VAL A C     1 
ATOM   2217 O  O     . VAL A 1 286 ? 27.84898  -19.46850 -23.76252 1.000 7.09833  ? 286 VAL A O     1 
ATOM   2218 C  CB    . VAL A 1 286 ? 28.45189  -21.08447 -26.31356 1.000 9.31455  ? 286 VAL A CB    1 
ATOM   2219 C  CG1   . VAL A 1 286 ? 28.03886  -21.50342 -27.71257 1.000 13.78438 ? 286 VAL A CG1   1 
ATOM   2220 C  CG2   . VAL A 1 286 ? 29.91187  -21.42655 -26.05457 1.000 11.82176 ? 286 VAL A CG2   1 
ATOM   2221 N  N     . SER A 1 287 ? 29.74902  -18.52558 -24.51550 1.000 8.73807  ? 287 SER A N     1 
ATOM   2222 C  CA    . SER A 1 287 ? 30.24005  -18.20764 -23.18450 1.000 8.44187  ? 287 SER A CA    1 
ATOM   2223 C  C     . SER A 1 287 ? 29.40910  -17.09261 -22.54647 1.000 7.17835  ? 287 SER A C     1 
ATOM   2224 O  O     . SER A 1 287 ? 28.55013  -16.46855 -23.17945 1.000 4.95602  ? 287 SER A O     1 
ATOM   2225 C  CB    . SER A 1 287 ? 31.70907  -17.79771 -23.24450 1.000 6.25512  ? 287 SER A CB    1 
ATOM   2226 O  OG    . SER A 1 287 ? 31.87013  -16.55470 -23.90347 1.000 7.05703  ? 287 SER A OG    1 
ATOM   2227 N  N     . LEU A 1 288 ? 29.67612  -16.84966 -21.25846 1.000 5.98719  ? 288 LEU A N     1 
ATOM   2228 C  CA    . LEU A 1 288 ? 28.99318  -15.76464 -20.56044 1.000 6.19173  ? 288 LEU A CA    1 
ATOM   2229 C  C     . LEU A 1 288 ? 29.38625  -14.41364 -21.14041 1.000 6.10827  ? 288 LEU A C     1 
ATOM   2230 O  O     . LEU A 1 288 ? 28.53229  -13.53760 -21.32638 1.000 4.68707  ? 288 LEU A O     1 
ATOM   2231 C  CB    . LEU A 1 288 ? 29.29918  -15.81369 -19.06244 1.000 8.79130  ? 288 LEU A CB    1 
ATOM   2232 C  CG    . LEU A 1 288 ? 28.16116  -16.29765 -18.16245 1.000 11.34261 ? 288 LEU A CG    1 
ATOM   2233 C  CD1   . LEU A 1 288 ? 28.52718  -16.11770 -16.69544 1.000 13.26966 ? 288 LEU A CD1   1 
ATOM   2234 C  CD2   . LEU A 1 288 ? 26.87420  -15.55858 -18.49442 1.000 6.82414  ? 288 LEU A CD2   1 
ATOM   2235 N  N     . ARG A 1 289 ? 30.67782  -14.22819 -21.43260 1.000 6.65376  ? 289 ARG A N     1 
ATOM   2236 C  CA    . ARG A 1 289 ? 31.11301  -13.01750 -22.12113 1.000 6.61211  ? 289 ARG A CA    1 
ATOM   2237 C  C     . ARG A 1 289 ? 30.43561  -12.88869 -23.47830 1.000 8.50995  ? 289 ARG A C     1 
ATOM   2238 O  O     . ARG A 1 289 ? 30.09194  -11.78034 -23.90877 1.000 8.53815  ? 289 ARG A O     1 
ATOM   2239 C  CB    . ARG A 1 289 ? 32.63535  -13.01532 -22.28204 1.000 9.58724  ? 289 ARG A CB    1 
ATOM   2240 C  CG    . ARG A 1 289 ? 33.16887  -11.81946 -23.06912 1.000 10.44639 ? 289 ARG A CG    1 
ATOM   2241 C  CD    . ARG A 1 289 ? 34.66606  -11.94147 -23.33347 1.000 8.61377  ? 289 ARG A CD    1 
ATOM   2242 N  NE    . ARG A 1 289 ? 35.15704  -10.85382 -24.17134 1.000 10.74596 ? 289 ARG A NE    1 
ATOM   2243 C  CZ    . ARG A 1 289 ? 35.37357  -10.94952 -25.47636 1.000 9.84510  ? 289 ARG A CZ    1 
ATOM   2244 N  NH1   . ARG A 1 289 ? 35.17804  -12.08274 -26.12969 1.000 12.22291 ? 289 ARG A NH1   1 
ATOM   2245 N  NH2   . ARG A 1 289 ? 35.79843  -9.88134  -26.14319 1.000 11.25349 ? 289 ARG A NH2   1 
ATOM   2246 N  N     . GLY A 1 290 ? 30.23625  -14.01461 -24.16740 1.000 7.65764  ? 290 GLY A N     1 
ATOM   2247 C  CA    . GLY A 1 290 ? 29.55125  -13.97055 -25.44640 1.000 6.64867  ? 290 GLY A CA    1 
ATOM   2248 C  C     . GLY A 1 290 ? 28.11728  -13.49648 -25.32938 1.000 6.25221  ? 290 GLY A C     1 
ATOM   2249 O  O     . GLY A 1 290 ? 27.58030  -12.89643 -26.26436 1.000 4.79104  ? 290 GLY A O     1 
ATOM   2250 N  N     . GLN A 1 291 ? 27.47827  -13.75747 -24.18338 1.000 5.74585  ? 291 GLN A N     1 
ATOM   2251 C  CA    . GLN A 1 291 ? 26.11329  -13.28741 -23.96637 1.000 5.68961  ? 291 GLN A CA    1 
ATOM   2252 C  C     . GLN A 1 291 ? 26.05637  -11.76741 -23.88333 1.000 5.77363  ? 291 GLN A C     1 
ATOM   2253 O  O     . GLN A 1 291 ? 25.10640  -11.14735 -24.37631 1.000 4.93439  ? 291 GLN A O     1 
ATOM   2254 C  CB    . GLN A 1 291 ? 25.53526  -13.91541 -22.69838 1.000 5.79716  ? 291 GLN A CB    1 
ATOM   2255 C  CG    . GLN A 1 291 ? 25.52619  -15.43541 -22.70742 1.000 5.84877  ? 291 GLN A CG    1 
ATOM   2256 C  CD    . GLN A 1 291 ? 24.90715  -16.00535 -23.96843 1.000 6.69665  ? 291 GLN A CD    1 
ATOM   2257 O  OE1   . GLN A 1 291 ? 23.72716  -15.78928 -24.24842 1.000 7.20394  ? 291 GLN A OE1   1 
ATOM   2258 N  NE2   . GLN A 1 291 ? 25.70611  -16.73337 -24.74345 1.000 8.58951  ? 291 GLN A NE2   1 
ATOM   2259 N  N     . LEU A 1 292 ? 27.05740  -11.15048 -23.25032 1.000 4.75228  ? 292 LEU A N     1 
ATOM   2260 C  CA    . LEU A 1 292 ? 27.14948  -9.69348  -23.26729 1.000 5.74336  ? 292 LEU A CA    1 
ATOM   2261 C  C     . LEU A 1 292 ? 27.43350  -9.17646  -24.66927 1.000 6.61356  ? 292 LEU A C     1 
ATOM   2262 O  O     . LEU A 1 292 ? 27.01855  -8.06443  -25.01725 1.000 4.88420  ? 292 LEU A O     1 
ATOM   2263 C  CB    . LEU A 1 292 ? 28.23450  -9.21956  -22.30428 1.000 5.55940  ? 292 LEU A CB    1 
ATOM   2264 C  CG    . LEU A 1 292 ? 28.06549  -9.61558  -20.83729 1.000 8.47015  ? 292 LEU A CG    1 
ATOM   2265 C  CD1   . LEU A 1 292 ? 29.30051  -9.24466  -20.03328 1.000 6.09658  ? 292 LEU A CD1   1 
ATOM   2266 C  CD2   . LEU A 1 292 ? 26.82252  -8.96453  -20.25427 1.000 7.11450  ? 292 LEU A CD2   1 
ATOM   2267 N  N     . LEU A 1 293 ? 28.13245  -9.96648  -25.48730 1.000 4.77409  ? 293 LEU A N     1 
ATOM   2268 C  CA    . LEU A 1 293 ? 28.40747  -9.54146  -26.85329 1.000 6.08957  ? 293 LEU A CA    1 
ATOM   2269 C  C     . LEU A 1 293 ? 27.15046  -9.59438  -27.71028 1.000 6.90016  ? 293 LEU A C     1 
ATOM   2270 O  O     . LEU A 1 293 ? 26.95650  -8.73934  -28.58126 1.000 8.37137  ? 293 LEU A O     1 
ATOM   2271 C  CB    . LEU A 1 293 ? 29.51742  -10.39750 -27.45631 1.000 7.99893  ? 293 LEU A CB    1 
ATOM   2272 C  CG    . LEU A 1 293 ? 30.87143  -10.27559 -26.75531 1.000 9.21343  ? 293 LEU A CG    1 
ATOM   2273 C  CD1   . LEU A 1 293 ? 31.86038  -11.25862 -27.34934 1.000 8.69290  ? 293 LEU A CD1   1 
ATOM   2274 C  CD2   . LEU A 1 293 ? 31.40550  -8.85061  -26.84028 1.000 11.67133 ? 293 LEU A CD2   1 
ATOM   2275 N  N     . TRP A 1 294 ? 26.28641  -10.59134 -27.48530 1.000 5.18108  ? 294 TRP A N     1 
ATOM   2276 C  CA    . TRP A 1 294 ? 24.97541  -10.58626 -28.12830 1.000 5.38283  ? 294 TRP A CA    1 
ATOM   2277 C  C     . TRP A 1 294 ? 24.21548  -9.30922  -27.79927 1.000 5.67744  ? 294 TRP A C     1 
ATOM   2278 O  O     . TRP A 1 294 ? 23.56250  -8.72017  -28.66825 1.000 6.61031  ? 294 TRP A O     1 
ATOM   2279 C  CB    . TRP A 1 294 ? 24.16135  -11.80622 -27.69332 1.000 6.99609  ? 294 TRP A CB    1 
ATOM   2280 C  CG    . TRP A 1 294 ? 24.59928  -13.10523 -28.29736 1.000 6.97418  ? 294 TRP A CG    1 
ATOM   2281 C  CD1   . TRP A 1 294 ? 25.20623  -14.14428 -27.65338 1.000 5.94655  ? 294 TRP A CD1   1 
ATOM   2282 C  CD2   . TRP A 1 294 ? 24.45226  -13.51119 -29.66337 1.000 10.18374 ? 294 TRP A CD2   1 
ATOM   2283 N  NE1   . TRP A 1 294 ? 25.45018  -15.16927 -28.53341 1.000 9.31794  ? 294 TRP A NE1   1 
ATOM   2284 C  CE2   . TRP A 1 294 ? 24.99819  -14.80622 -29.77440 1.000 9.61981  ? 294 TRP A CE2   1 
ATOM   2285 C  CE3   . TRP A 1 294 ? 23.91528  -12.90614 -30.80435 1.000 9.17801  ? 294 TRP A CE3   1 
ATOM   2286 C  CZ2   . TRP A 1 294 ? 25.02515  -15.50719 -30.97941 1.000 14.18020 ? 294 TRP A CZ2   1 
ATOM   2287 C  CZ3   . TRP A 1 294 ? 23.94324  -13.60311 -32.00237 1.000 12.66242 ? 294 TRP A CZ3   1 
ATOM   2288 C  CH2   . TRP A 1 294 ? 24.49318  -14.89114 -32.07940 1.000 15.83777 ? 294 TRP A CH2   1 
ATOM   2289 N  N     . ARG A 1 295 ? 24.27820  -8.88181  -26.53707 1.000 6.55787  ? 295 ARG A N     1 
ATOM   2290 C  CA    . ARG A 1 295 ? 23.64484  -7.63204  -26.13255 1.000 6.58922  ? 295 ARG A CA    1 
ATOM   2291 C  C     . ARG A 1 295 ? 24.26551  -6.44435  -26.86156 1.000 6.89104  ? 295 ARG A C     1 
ATOM   2292 O  O     . ARG A 1 295 ? 23.55521  -5.59233  -27.40554 1.000 7.26669  ? 295 ARG A O     1 
ATOM   2293 C  CB    . ARG A 1 295 ? 23.75705  -7.47421  -24.61569 1.000 5.12989  ? 295 ARG A CB    1 
ATOM   2294 C  CG    . ARG A 1 295 ? 23.19917  -6.18268  -24.06072 1.000 4.68162  ? 295 ARG A CG    1 
ATOM   2295 C  CD    . ARG A 1 295 ? 23.30242  -6.17869  -22.54127 1.000 6.18937  ? 295 ARG A CD    1 
ATOM   2296 N  NE    . ARG A 1 295 ? 22.68381  -5.00717  -21.93692 1.000 5.25683  ? 295 ARG A NE    1 
ATOM   2297 C  CZ    . ARG A 1 295 ? 23.31021  -3.85975  -21.71825 1.000 8.35232  ? 295 ARG A CZ    1 
ATOM   2298 N  NH1   . ARG A 1 295 ? 24.58042  -3.69068  -22.05247 1.000 4.35545  ? 295 ARG A NH1   1 
ATOM   2299 N  NH2   . ARG A 1 295 ? 22.64442  -2.85548  -21.15303 1.000 4.92779  ? 295 ARG A NH2   1 
ATOM   2300 N  N     . GLU A 1 296 ? 25.60163  -6.38232  -26.89320 1.000 5.17606  ? 296 GLU A N     1 
ATOM   2301 C  CA    . GLU A 1 296 ? 26.28468  -5.28233  -27.57018 1.000 7.49341  ? 296 GLU A CA    1 
ATOM   2302 C  C     . GLU A 1 296 ? 26.06367  -5.34229  -29.07618 1.000 7.04603  ? 296 GLU A C     1 
ATOM   2303 O  O     . GLU A 1 296 ? 25.96372  -4.30227  -29.73915 1.000 9.80103  ? 296 GLU A O     1 
ATOM   2304 C  CB    . GLU A 1 296 ? 27.78068  -5.31742  -27.24519 1.000 8.88377  ? 296 GLU A CB    1 
ATOM   2305 C  CG    . GLU A 1 296 ? 28.51875  -4.01045  -27.51016 1.000 9.07897  ? 296 GLU A CG    1 
ATOM   2306 C  CD    . GLU A 1 296 ? 28.37680  -3.02247  -26.37013 1.000 7.65946  ? 296 GLU A CD    1 
ATOM   2307 O  OE1   . GLU A 1 296 ? 27.75579  -3.37846  -25.34314 1.000 8.22151  ? 296 GLU A OE1   1 
ATOM   2308 O  OE2   . GLU A 1 296 ? 28.89086  -1.89249  -26.49911 1.000 8.24663  ? 296 GLU A OE2   1 
ATOM   2309 N  N     . PHE A 1 297 ? 25.98061  -6.55527  -29.62521 1.000 4.95425  ? 297 PHE A N     1 
ATOM   2310 C  CA    . PHE A 1 297 ? 25.75059  -6.73523  -31.05421 1.000 8.09053  ? 297 PHE A CA    1 
ATOM   2311 C  C     . PHE A 1 297 ? 24.42262  -6.12115  -31.48019 1.000 9.70929  ? 297 PHE A C     1 
ATOM   2312 O  O     . PHE A 1 297 ? 24.36566  -5.32112  -32.42217 1.000 7.05195  ? 297 PHE A O     1 
ATOM   2313 C  CB    . PHE A 1 297 ? 25.79252  -8.22622  -31.38925 1.000 6.89762  ? 297 PHE A CB    1 
ATOM   2314 C  CG    . PHE A 1 297 ? 25.49950  -8.54317  -32.82325 1.000 10.23050 ? 297 PHE A CG    1 
ATOM   2315 C  CD1   . PHE A 1 297 ? 26.24452  -7.97418  -33.84224 1.000 10.52392 ? 297 PHE A CD1   1 
ATOM   2316 C  CD2   . PHE A 1 297 ? 24.49345  -9.43911  -33.14927 1.000 8.43141  ? 297 PHE A CD2   1 
ATOM   2317 C  CE1   . PHE A 1 297 ? 25.97850  -8.27914  -35.16425 1.000 13.63596 ? 297 PHE A CE1   1 
ATOM   2318 C  CE2   . PHE A 1 297 ? 24.22343  -9.74807  -34.46528 1.000 11.02409 ? 297 PHE A CE2   1 
ATOM   2319 C  CZ    . PHE A 1 297 ? 24.96645  -9.16708  -35.47627 1.000 13.10502 ? 297 PHE A CZ    1 
ATOM   2320 N  N     . PHE A 1 298 ? 23.33661  -6.48111  -30.78920 1.000 7.57789  ? 298 PHE A N     1 
ATOM   2321 C  CA    . PHE A 1 298 ? 22.02563  -5.98703  -31.19518 1.000 8.40338  ? 298 PHE A CA    1 
ATOM   2322 C  C     . PHE A 1 298 ? 21.87871  -4.49203  -30.92714 1.000 8.56458  ? 298 PHE A C     1 
ATOM   2323 O  O     . PHE A 1 298 ? 21.07374  -3.82198  -31.58412 1.000 5.78190  ? 298 PHE A O     1 
ATOM   2324 C  CB    . PHE A 1 298 ? 20.92859  -6.77999  -30.48719 1.000 5.92420  ? 298 PHE A CB    1 
ATOM   2325 C  CG    . PHE A 1 298 ? 20.85752  -8.21498  -30.91123 1.000 5.78508  ? 298 PHE A CG    1 
ATOM   2326 C  CD1   . PHE A 1 298 ? 21.13550  -8.58096  -32.21624 1.000 8.04169  ? 298 PHE A CD1   1 
ATOM   2327 C  CD2   . PHE A 1 298 ? 20.52747  -9.19999  -30.00425 1.000 5.97167  ? 298 PHE A CD2   1 
ATOM   2328 C  CE1   . PHE A 1 298 ? 21.07643  -9.90195  -32.60627 1.000 8.35346  ? 298 PHE A CE1   1 
ATOM   2329 C  CE2   . PHE A 1 298 ? 20.46741  -10.51897 -30.38428 1.000 8.01405  ? 298 PHE A CE2   1 
ATOM   2330 C  CZ    . PHE A 1 298 ? 20.74338  -10.87396 -31.68829 1.000 9.95210  ? 298 PHE A CZ    1 
ATOM   2331 N  N     . TYR A 1 299 ? 22.64774  -3.94809  -29.97913 1.000 9.44739  ? 299 TYR A N     1 
ATOM   2332 C  CA    . TYR A 1 299 ? 22.64381  -2.50310  -29.76910 1.000 10.43530 ? 299 TYR A CA    1 
ATOM   2333 C  C     . TYR A 1 299 ? 23.35285  -1.78111  -30.90708 1.000 9.71956  ? 299 TYR A C     1 
ATOM   2334 O  O     . TYR A 1 299 ? 22.92190  -0.70208  -31.32806 1.000 9.17807  ? 299 TYR A O     1 
ATOM   2335 C  CB    . TYR A 1 299 ? 23.29284  -2.16716  -28.42709 1.000 6.71169  ? 299 TYR A CB    1 
ATOM   2336 C  CG    . TYR A 1 299 ? 22.30985  -1.98314  -27.29409 1.000 8.84451  ? 299 TYR A CG    1 
ATOM   2337 C  CD1   . TYR A 1 299 ? 21.68880  -3.07412  -26.70111 1.000 7.49502  ? 299 TYR A CD1   1 
ATOM   2338 C  CD2   . TYR A 1 299 ? 22.01292  -0.71614  -26.81105 1.000 8.37785  ? 299 TYR A CD2   1 
ATOM   2339 C  CE1   . TYR A 1 299 ? 20.79081  -2.90710  -25.66210 1.000 8.70223  ? 299 TYR A CE1   1 
ATOM   2340 C  CE2   . TYR A 1 299 ? 21.11893  -0.53912  -25.77505 1.000 10.69657 ? 299 TYR A CE2   1 
ATOM   2341 C  CZ    . TYR A 1 299 ? 20.51088  -1.63710  -25.20407 1.000 8.47471  ? 299 TYR A CZ    1 
ATOM   2342 O  OH    . TYR A 1 299 ? 19.62089  -1.46408  -24.16806 1.000 10.45481 ? 299 TYR A OH    1 
ATOM   2343 N  N     . THR A 1 300 ? 24.43581  -2.36415  -31.42110 1.000 9.34447  ? 300 THR A N     1 
ATOM   2344 C  CA    . THR A 1 300 ? 25.16884  -1.73616  -32.51509 1.000 10.50844 ? 300 THR A CA    1 
ATOM   2345 C  C     . THR A 1 300 ? 24.33784  -1.72109  -33.79309 1.000 9.96626  ? 300 THR A C     1 
ATOM   2346 O  O     . THR A 1 300 ? 24.27289  -0.70207  -34.49206 1.000 15.04621 ? 300 THR A O     1 
ATOM   2347 C  CB    . THR A 1 300 ? 26.49480  -2.46722  -32.73911 1.000 9.31864  ? 300 THR A CB    1 
ATOM   2348 O  OG1   . THR A 1 300 ? 27.14780  -2.66729  -31.47812 1.000 9.51860  ? 300 THR A OG1   1 
ATOM   2349 C  CG2   . THR A 1 300 ? 27.40484  -1.65725  -33.65010 1.000 9.34656  ? 300 THR A CG2   1 
ATOM   2350 N  N     . VAL A 1 301 ? 23.68778  -2.84105  -34.11011 1.000 10.32207 ? 301 VAL A N     1 
ATOM   2351 C  CA    . VAL A 1 301 ? 22.86877  -2.91098  -35.31611 1.000 13.86121 ? 301 VAL A CA    1 
ATOM   2352 C  C     . VAL A 1 301 ? 21.57281  -2.13192  -35.13109 1.000 11.12250 ? 301 VAL A C     1 
ATOM   2353 O  O     . VAL A 1 301 ? 21.16885  -1.35188  -36.00207 1.000 12.25260 ? 301 VAL A O     1 
ATOM   2354 C  CB    . VAL A 1 301 ? 22.59270  -4.37796  -35.68714 1.000 12.45323 ? 301 VAL A CB    1 
ATOM   2355 C  CG1   . VAL A 1 301 ? 21.81369  -4.45989  -36.99014 1.000 15.15757 ? 301 VAL A CG1   1 
ATOM   2356 C  CG2   . VAL A 1 301 ? 23.89166  -5.15202  -35.78217 1.000 11.30057 ? 301 VAL A CG2   1 
ATOM   2357 N  N     . GLY A 1 302 ? 20.90381  -2.32691  -33.99209 1.000 10.77047 ? 302 GLY A N     1 
ATOM   2358 C  CA    . GLY A 1 302 ? 19.59584  -1.72085  -33.80007 1.000 10.30670 ? 302 GLY A CA    1 
ATOM   2359 C  C     . GLY A 1 302 ? 19.63491  -0.20485  -33.77303 1.000 11.83855 ? 302 GLY A C     1 
ATOM   2360 O  O     . GLY A 1 302 ? 18.73895  0.45621   -34.30101 1.000 10.96815 ? 302 GLY A O     1 
ATOM   2361 N  N     . SER A 1 303 ? 20.67095  0.36708   -33.15302 1.000 13.25981 ? 303 SER A N     1 
ATOM   2362 C  CA    . SER A 1 303 ? 20.78002  1.81907   -33.06899 1.000 11.38802 ? 303 SER A CA    1 
ATOM   2363 C  C     . SER A 1 303 ? 21.07105  2.46209   -34.41998 1.000 13.23097 ? 303 SER A C     1 
ATOM   2364 O  O     . SER A 1 303 ? 20.76611  3.64611   -34.60395 1.000 17.20295 ? 303 SER A O     1 
ATOM   2365 C  CB    . SER A 1 303 ? 21.86304  2.20800   -32.05898 1.000 17.79210 ? 303 SER A CB    1 
ATOM   2366 O  OG    . SER A 1 303 ? 23.11601  1.63094   -32.39300 1.000 12.17770 ? 303 SER A OG    1 
ATOM   2367 N  N     . THR A 1 304 ? 21.64301  1.71808   -35.36500 1.000 9.72246  ? 304 THR A N     1 
ATOM   2368 C  CA    . THR A 1 304 ? 21.98603  2.25110   -36.67698 1.000 13.80981 ? 304 THR A CA    1 
ATOM   2369 C  C     . THR A 1 304 ? 21.04400  1.76417   -37.77099 1.000 12.45648 ? 304 THR A C     1 
ATOM   2370 O  O     . THR A 1 304 ? 21.31201  1.99719   -38.95499 1.000 12.00566 ? 304 THR A O     1 
ATOM   2371 C  CB    . THR A 1 304 ? 23.43101  1.89203   -37.03400 1.000 17.59733 ? 304 THR A CB    1 
ATOM   2372 O  OG1   . THR A 1 304 ? 23.58694  0.46603   -37.04903 1.000 8.37683  ? 304 THR A OG1   1 
ATOM   2373 C  CG2   . THR A 1 304 ? 24.39304  2.49396   -36.01799 1.000 10.16122 ? 304 THR A CG2   1 
ATOM   2374 N  N     . THR A 1 305 ? 19.94997  1.09922   -37.40800 1.000 12.15120 ? 305 THR A N     1 
ATOM   2375 C  CA    . THR A 1 305 ? 18.98794  0.58129   -38.37401 1.000 17.26321 ? 305 THR A CA    1 
ATOM   2376 C  C     . THR A 1 305 ? 17.63897  1.25535   -38.16699 1.000 17.13385 ? 305 THR A C     1 
ATOM   2377 O  O     . THR A 1 305 ? 17.03597  1.10536   -37.08999 1.000 14.62789 ? 305 THR A O     1 
ATOM   2378 C  CB    . THR A 1 305 ? 18.84886  -0.93971  -38.24905 1.000 14.40370 ? 305 THR A CB    1 
ATOM   2379 O  OG1   . THR A 1 305 ? 20.11283  -1.56176  -38.51907 1.000 15.37658 ? 305 THR A OG1   1 
ATOM   2380 C  CG2   . THR A 1 305 ? 17.81383  -1.46463  -39.23306 1.000 14.53956 ? 305 THR A CG2   1 
ATOM   2381 N  N     . PRO A 1 306 ? 17.12600  1.99540   -39.14697 1.000 17.91203 ? 306 PRO A N     1 
ATOM   2382 C  CA    . PRO A 1 306 ? 15.81904  2.63646   -38.97595 1.000 20.03714 ? 306 PRO A CA    1 
ATOM   2383 C  C     . PRO A 1 306 ? 14.68899  1.61852   -38.99997 1.000 16.41078 ? 306 PRO A C     1 
ATOM   2384 O  O     . PRO A 1 306 ? 14.74093  0.60954   -39.70999 1.000 15.97945 ? 306 PRO A O     1 
ATOM   2385 C  CB    . PRO A 1 306 ? 15.73308  3.59050   -40.17193 1.000 23.58131 ? 306 PRO A CB    1 
ATOM   2386 C  CG    . PRO A 1 306 ? 16.62905  2.98048   -41.20095 1.000 21.98405 ? 306 PRO A CG    1 
ATOM   2387 C  CD    . PRO A 1 306 ? 17.74702  2.32640   -40.44097 1.000 18.09354 ? 306 PRO A CD    1 
ATOM   2388 N  N     . ASN A 1 307 ? 13.65600  1.89856   -38.19796 1.000 17.44757 ? 307 ASN A N     1 
ATOM   2389 C  CA    . ASN A 1 307 ? 12.48896  1.02261   -38.07498 1.000 14.82236 ? 307 ASN A CA    1 
ATOM   2390 C  C     . ASN A 1 307 ? 12.89789  -0.38242  -37.63601 1.000 15.16873 ? 307 ASN A C     1 
ATOM   2391 O  O     . ASN A 1 307 ? 12.31284  -1.38238  -38.05603 1.000 17.57689 ? 307 ASN A O     1 
ATOM   2392 C  CB    . ASN A 1 307 ? 11.68995  0.97868   -39.37997 1.000 16.52680 ? 307 ASN A CB    1 
ATOM   2393 C  CG    . ASN A 1 307 ? 11.26702  2.35672   -39.85194 1.000 19.36883 ? 307 ASN A CG    1 
ATOM   2394 O  OD1   . ASN A 1 307 ? 10.91607  3.22171   -39.05092 1.000 19.08082 ? 307 ASN A OD1   1 
ATOM   2395 N  ND2   . ASN A 1 307 ? 11.30603  2.56774   -41.15993 1.000 15.32448 ? 307 ASN A ND2   1 
ATOM   2396 N  N     . PHE A 1 308 ? 13.91089  -0.45149  -36.76802 1.000 15.41859 ? 308 PHE A N     1 
ATOM   2397 C  CA    . PHE A 1 308 ? 14.44583  -1.73953  -36.33705 1.000 15.03306 ? 308 PHE A CA    1 
ATOM   2398 C  C     . PHE A 1 308 ? 13.40879  -2.55449  -35.57706 1.000 15.73074 ? 308 PHE A C     1 
ATOM   2399 O  O     . PHE A 1 308 ? 13.41373  -3.78849  -35.65109 1.000 16.66140 ? 308 PHE A O     1 
ATOM   2400 C  CB    . PHE A 1 308 ? 15.69184  -1.52061  -35.47805 1.000 13.24349 ? 308 PHE A CB    1 
ATOM   2401 C  CG    . PHE A 1 308 ? 16.35778  -2.79366  -35.03208 1.000 12.21824 ? 308 PHE A CG    1 
ATOM   2402 C  CD1   . PHE A 1 308 ? 17.18074  -3.49968  -35.89510 1.000 14.28960 ? 308 PHE A CD1   1 
ATOM   2403 C  CD2   . PHE A 1 308 ? 16.17276  -3.27568  -33.74809 1.000 9.63359  ? 308 PHE A CD2   1 
ATOM   2404 C  CE1   . PHE A 1 308 ? 17.79768  -4.66572  -35.49013 1.000 11.15418 ? 308 PHE A CE1   1 
ATOM   2405 C  CE2   . PHE A 1 308 ? 16.78870  -4.43872  -33.33812 1.000 8.77472  ? 308 PHE A CE2   1 
ATOM   2406 C  CZ    . PHE A 1 308 ? 17.60266  -5.13574  -34.21114 1.000 12.70993 ? 308 PHE A CZ    1 
ATOM   2407 N  N     . HIS A 1 309 ? 12.51282  -1.88947  -34.85104 1.000 17.89550 ? 309 HIS A N     1 
ATOM   2408 C  CA    . HIS A 1 309 ? 11.47879  -2.55943  -34.07106 1.000 16.30572 ? 309 HIS A CA    1 
ATOM   2409 C  C     . HIS A 1 309 ? 10.25877  -2.94335  -34.89506 1.000 18.85177 ? 309 HIS A C     1 
ATOM   2410 O  O     . HIS A 1 309 ? 9.28575   -3.45232  -34.32807 1.000 22.37791 ? 309 HIS A O     1 
ATOM   2411 C  CB    . HIS A 1 309 ? 11.03200  -1.66200  -32.92000 1.000 17.32563 ? 309 HIS A CB    1 
ATOM   2412 C  CG    . HIS A 1 309 ? 10.43300  -0.38000  -33.36600 1.000 22.69266 ? 309 HIS A CG    1 
ATOM   2413 N  ND1   . HIS A 1 309 ? 11.19100  0.71500   -33.71400 1.000 20.87524 ? 309 HIS A ND1   1 
ATOM   2414 C  CD2   . HIS A 1 309 ? 9.16000   -0.00100  -33.48600 1.000 22.20115 ? 309 HIS A CD2   1 
ATOM   2415 C  CE1   . HIS A 1 309 ? 10.38800  1.70600   -34.05700 1.000 17.97370 ? 309 HIS A CE1   1 
ATOM   2416 N  NE2   . HIS A 1 309 ? 9.15100   1.29700   -33.92000 1.000 22.17480 ? 309 HIS A NE2   1 
ATOM   2417 N  N     . ARG A 1 310 ? 10.27538  -2.70501  -36.20310 1.000 15.13949 ? 310 ARG A N     1 
ATOM   2418 C  CA    . ARG A 1 310 ? 9.12951   -2.95355  -37.06340 1.000 16.72076 ? 310 ARG A CA    1 
ATOM   2419 C  C     . ARG A 1 310 ? 9.57635   -3.75980  -38.27547 1.000 17.10815 ? 310 ARG A C     1 
ATOM   2420 O  O     . ARG A 1 310 ? 10.76997  -3.91538  -38.53859 1.000 19.39230 ? 310 ARG A O     1 
ATOM   2421 C  CB    . ARG A 1 310 ? 8.47889   -1.63890  -37.51228 1.000 20.14813 ? 310 ARG A CB    1 
ATOM   2422 C  CG    . ARG A 1 310 ? 6.98911   -1.54370  -37.24435 1.000 24.49569 ? 310 ARG A CG    1 
ATOM   2423 C  CD    . ARG A 1 310 ? 6.29589   -0.86211  -38.40517 1.000 24.45128 ? 310 ARG A CD    1 
ATOM   2424 N  NE    . ARG A 1 310 ? 6.99509   0.35774   -38.78593 1.000 26.17971 ? 310 ARG A NE    1 
ATOM   2425 C  CZ    . ARG A 1 310 ? 6.80941   1.00414   -39.92775 0.000 22.54186 ? 310 ARG A CZ    1 
ATOM   2426 N  NH1   . ARG A 1 310 ? 5.95637   0.56663   -40.83874 0.000 22.70300 ? 310 ARG A NH1   1 
ATOM   2427 N  NH2   . ARG A 1 310 ? 7.50409   2.11278   -40.16508 0.000 21.83444 ? 310 ARG A NH2   1 
ATOM   2428 N  N     . MET A 1 311 ? 8.59569   -4.27517  -39.01909 1.000 15.82208 ? 311 MET A N     1 
ATOM   2429 C  CA    . MET A 1 311 ? 8.86965   -5.01515  -40.24710 1.000 16.99207 ? 311 MET A CA    1 
ATOM   2430 C  C     . MET A 1 311 ? 8.91669   -4.08313  -41.45608 1.000 16.62467 ? 311 MET A C     1 
ATOM   2431 O  O     . MET A 1 311 ? 9.92769   -4.02316  -42.16308 1.000 21.93659 ? 311 MET A O     1 
ATOM   2432 C  CB    . MET A 1 311 ? 7.81959   -6.11310  -40.45813 1.000 18.51728 ? 311 MET A CB    1 
ATOM   2433 C  CG    . MET A 1 311 ? 8.17853   -7.10409  -41.56015 1.000 15.68148 ? 311 MET A CG    1 
ATOM   2434 S  SD    . MET A 1 311 ? 6.86947   -8.29301  -41.91717 1.000 25.78883 ? 311 MET A SD    1 
ATOM   2435 C  CE    . MET A 1 311 ? 5.64352   -7.23093  -42.68214 1.000 16.86459 ? 311 MET A CE    1 
ATOM   2436 N  N     . ALA A 1 312 ? 7.83072   -3.35707  -41.70706 1.000 17.49186 ? 312 ALA A N     1 
ATOM   2437 C  CA    . ALA A 1 312 ? 7.80277   -2.42304  -42.82404 1.000 20.83270 ? 312 ALA A CA    1 
ATOM   2438 C  C     . ALA A 1 312 ? 8.75983   -1.26709  -42.56001 1.000 20.27473 ? 312 ALA A C     1 
ATOM   2439 O  O     . ALA A 1 312 ? 8.79386   -0.71212  -41.45700 1.000 21.34439 ? 312 ALA A O     1 
ATOM   2440 C  CB    . ALA A 1 312 ? 6.38379   -1.90696  -43.05202 1.000 20.86008 ? 312 ALA A CB    1 
ATOM   2441 N  N     . GLY A 1 313 ? 9.54984   -0.91211  -43.57201 1.000 22.77717 ? 313 GLY A N     1 
ATOM   2442 C  CA    . GLY A 1 313 ? 10.56689  0.10483   -43.42299 1.000 22.98694 ? 313 GLY A CA    1 
ATOM   2443 C  C     . GLY A 1 313 ? 11.86587  -0.37225  -42.81201 1.000 21.13287 ? 313 GLY A C     1 
ATOM   2444 O  O     . GLY A 1 313 ? 12.84391  0.38771   -42.80899 1.000 21.80616 ? 313 GLY A O     1 
ATOM   2445 N  N     . ASN A 1 314 ? 11.91381  -1.59526  -42.29304 1.000 20.08680 ? 314 ASN A N     1 
ATOM   2446 C  CA    . ASN A 1 314 ? 13.14579  -2.14134  -41.73705 1.000 18.42631 ? 314 ASN A CA    1 
ATOM   2447 C  C     . ASN A 1 314 ? 13.98975  -2.73435  -42.85707 1.000 16.94748 ? 314 ASN A C     1 
ATOM   2448 O  O     . ASN A 1 314 ? 13.51670  -3.62931  -43.56809 1.000 18.48233 ? 314 ASN A O     1 
ATOM   2449 C  CB    . ASN A 1 314 ? 12.83074  -3.20934  -40.69508 1.000 20.29825 ? 314 ASN A CB    1 
ATOM   2450 C  CG    . ASN A 1 314 ? 14.03572  -3.58143  -39.83609 1.000 17.32773 ? 314 ASN A CG    1 
ATOM   2451 O  OD1   . ASN A 1 314 ? 15.16974  -3.20948  -40.13209 1.000 19.76790 ? 314 ASN A OD1   1 
ATOM   2452 N  ND2   . ASN A 1 314 ? 13.78669  -4.32844  -38.76511 1.000 14.72320 ? 314 ASN A ND2   1 
ATOM   2453 N  N     . PRO A 1 315 ? 15.22877  -2.27241  -43.05706 1.000 20.47293 ? 315 PRO A N     1 
ATOM   2454 C  CA    . PRO A 1 315 ? 16.04074  -2.84543  -44.14308 1.000 17.45651 ? 315 PRO A CA    1 
ATOM   2455 C  C     . PRO A 1 315 ? 16.54167  -4.24646  -43.84412 1.000 16.73786 ? 315 PRO A C     1 
ATOM   2456 O  O     . PRO A 1 315 ? 16.62162  -5.07644  -44.75814 1.000 22.06633 ? 315 PRO A O     1 
ATOM   2457 C  CB    . PRO A 1 315 ? 17.19379  -1.84148  -44.27806 1.000 15.36336 ? 315 PRO A CB    1 
ATOM   2458 C  CG    . PRO A 1 315 ? 17.30383  -1.21352  -42.92605 1.000 17.07306 ? 315 PRO A CG    1 
ATOM   2459 C  CD    . PRO A 1 315 ? 15.89283  -1.12846  -42.40804 1.000 24.13099 ? 315 PRO A CD    1 
ATOM   2460 N  N     . VAL A 1 316 ? 16.88566  -4.53850  -42.58612 1.000 17.53904 ? 316 VAL A N     1 
ATOM   2461 C  CA    . VAL A 1 316 ? 17.43260  -5.84954  -42.24316 1.000 16.30560 ? 316 VAL A CA    1 
ATOM   2462 C  C     . VAL A 1 316 ? 16.36654  -6.91249  -42.04018 1.000 15.13491 ? 316 VAL A C     1 
ATOM   2463 O  O     . VAL A 1 316 ? 16.71148  -8.08651  -41.85621 1.000 14.64196 ? 316 VAL A O     1 
ATOM   2464 C  CB    . VAL A 1 316 ? 18.29860  -5.78261  -40.96916 1.000 16.59439 ? 316 VAL A CB    1 
ATOM   2465 C  CG1   . VAL A 1 316 ? 19.34166  -4.67666  -41.08414 1.000 18.14424 ? 316 VAL A CG1   1 
ATOM   2466 C  CG2   . VAL A 1 316 ? 17.43062  -5.58660  -39.73215 1.000 14.90132 ? 316 VAL A CG2   1 
ATOM   2467 N  N     . CYS A 1 317 ? 15.08956  -6.54543  -42.06716 1.000 13.41320 ? 317 CYS A N     1 
ATOM   2468 C  CA    . CYS A 1 317 ? 14.00552  -7.46938  -41.76218 1.000 15.79390 ? 317 CYS A CA    1 
ATOM   2469 C  C     . CYS A 1 317 ? 13.31949  -7.93331  -43.03919 1.000 14.84261 ? 317 CYS A C     1 
ATOM   2470 O  O     . CYS A 1 317 ? 13.05752  -7.13628  -43.94417 1.000 15.98457 ? 317 CYS A O     1 
ATOM   2471 C  CB    . CYS A 1 317 ? 12.97655  -6.82535  -40.83316 1.000 12.74848 ? 317 CYS A CB    1 
ATOM   2472 S  SG    . CYS A 1 317 ? 11.66850  -7.94929  -40.30218 1.000 15.53203 ? 317 CYS A SG    1 
ATOM   2473 N  N     . LYS A 1 318 ? 13.03142  -9.22930  -43.10122 1.000 16.12199 ? 318 LYS A N     1 
ATOM   2474 C  CA    . LYS A 1 318 ? 12.33939  -9.80924  -44.24023 1.000 19.70397 ? 318 LYS A CA    1 
ATOM   2475 C  C     . LYS A 1 318 ? 10.84540  -9.54316  -44.13822 1.000 14.41168 ? 318 LYS A C     1 
ATOM   2476 O  O     . LYS A 1 318 ? 10.25440  -9.64816  -43.06122 1.000 16.09910 ? 318 LYS A O     1 
ATOM   2477 C  CB    . LYS A 1 318 ? 12.60931  -11.31125 -44.30727 1.000 16.82751 ? 318 LYS A CB    1 
ATOM   2478 C  CG    . LYS A 1 318 ? 12.05727  -11.99019 -45.53928 1.000 21.31956 ? 318 LYS A CG    1 
ATOM   2479 C  CD    . LYS A 1 318 ? 12.88421  -13.21622 -45.87031 1.000 28.37518 ? 318 LYS A CD    1 
ATOM   2480 C  CE    . LYS A 1 318 ? 14.35523  -12.85030 -45.97731 0.000 26.47249 ? 318 LYS A CE    1 
ATOM   2481 N  NZ    . LYS A 1 318 ? 15.07018  -13.65631 -47.00233 0.000 30.13491 ? 318 LYS A NZ    1 
ATOM   2482 N  N     . GLN A 1 319 ? 10.23541  -9.19010  -45.26821 1.000 16.70344 ? 319 GLN A N     1 
ATOM   2483 C  CA    . GLN A 1 319 ? 8.80843   -8.87803  -45.31819 1.000 19.77809 ? 319 GLN A CA    1 
ATOM   2484 C  C     . GLN A 1 319 ? 8.05136   -10.16699 -45.62522 1.000 18.16204 ? 319 GLN A C     1 
ATOM   2485 O  O     . GLN A 1 319 ? 8.03234   -10.63196 -46.76623 1.000 23.18197 ? 319 GLN A O     1 
ATOM   2486 C  CB    . GLN A 1 319 ? 8.52848   -7.79599  -46.35617 1.000 21.50071 ? 319 GLN A CB    1 
ATOM   2487 C  CG    . GLN A 1 319 ? 9.52454   -6.63704  -46.33814 1.000 24.29656 ? 319 GLN A CG    1 
ATOM   2488 C  CD    . GLN A 1 319 ? 9.55258   -5.89308  -45.01313 1.000 19.97509 ? 319 GLN A CD    1 
ATOM   2489 O  OE1   . GLN A 1 319 ? 8.51060   -5.60004  -44.42712 1.000 17.05859 ? 319 GLN A OE1   1 
ATOM   2490 N  NE2   . GLN A 1 319 ? 10.75160  -5.58115  -44.53712 1.000 20.47462 ? 319 GLN A NE2   1 
ATOM   2491 N  N     . ILE A 1 320 ? 7.43034   -10.74998 -44.59923 1.000 17.43456 ? 320 ILE A N     1 
ATOM   2492 C  CA    . ILE A 1 320 ? 6.70927   -12.01294 -44.71526 1.000 19.20476 ? 320 ILE A CA    1 
ATOM   2493 C  C     . ILE A 1 320 ? 5.22529   -11.74087 -44.50925 1.000 20.22360 ? 320 ILE A C     1 
ATOM   2494 O  O     . ILE A 1 320 ? 4.84234   -10.86287 -43.72723 1.000 19.76196 ? 320 ILE A O     1 
ATOM   2495 C  CB    . ILE A 1 320 ? 7.24023   -13.04999 -43.70029 1.000 17.48565 ? 320 ILE A CB    1 
ATOM   2496 C  CG1   . ILE A 1 320 ? 8.76122   -13.17806 -43.83030 1.000 18.77457 ? 320 ILE A CG1   1 
ATOM   2497 C  CG2   . ILE A 1 320 ? 6.56716   -14.39895 -43.90132 1.000 20.64245 ? 320 ILE A CG2   1 
ATOM   2498 C  CD1   . ILE A 1 320 ? 9.40018   -14.10612 -42.82432 1.000 18.50680 ? 320 ILE A CD1   1 
ATOM   2499 N  N     . ASP A 1 321 ? 4.38000   -12.49200 -45.22000 1.000 23.51848 ? 321 ASP A N     1 
ATOM   2500 C  CA    . ASP A 1 321 ? 2.92600   -12.17800 -45.22500 1.000 24.09293 ? 321 ASP A CA    1 
ATOM   2501 C  C     . ASP A 1 321 ? 2.26900   -12.86100 -44.01000 1.000 17.51500 ? 321 ASP A C     1 
ATOM   2502 O  O     . ASP A 1 321 ? 1.26900   -13.52800 -44.19300 1.000 26.23432 ? 321 ASP A O     1 
ATOM   2503 C  CB    . ASP A 1 321 ? 2.29800   -12.73800 -46.53000 1.000 27.51565 ? 321 ASP A CB    1 
ATOM   2504 C  CG    . ASP A 1 321 ? 2.23700   -11.75300 -47.70700 1.000 38.07927 ? 321 ASP A CG    1 
ATOM   2505 O  OD1   . ASP A 1 321 ? 3.16800   -10.91900 -47.85800 1.000 42.50779 ? 321 ASP A OD1   1 
ATOM   2506 O  OD2   . ASP A 1 321 ? 1.25100   -11.82000 -48.47400 1.000 46.02439 ? 321 ASP A OD2   1 
ATOM   2507 N  N     . TRP A 1 322 ? 2.80000   -12.61700 -42.77800 1.000 17.05754 ? 322 TRP A N     1 
ATOM   2508 C  CA    . TRP A 1 322 ? 2.17823   -13.08679 -41.54027 1.000 17.02327 ? 322 TRP A CA    1 
ATOM   2509 C  C     . TRP A 1 322 ? 0.66024   -12.90771 -41.52226 1.000 18.14560 ? 322 TRP A C     1 
ATOM   2510 O  O     . TRP A 1 322 ? 0.12629   -11.99267 -42.15723 1.000 15.66353 ? 322 TRP A O     1 
ATOM   2511 C  CB    . TRP A 1 322 ? 2.77727   -12.35984 -40.33325 1.000 16.13636 ? 322 TRP A CB    1 
ATOM   2512 C  CG    . TRP A 1 322 ? 4.26527   -12.39292 -40.28426 1.000 14.51813 ? 322 TRP A CG    1 
ATOM   2513 C  CD1   . TRP A 1 322 ? 5.11532   -11.35496 -40.52524 1.000 14.67982 ? 322 TRP A CD1   1 
ATOM   2514 C  CD2   . TRP A 1 322 ? 5.08922   -13.52297 -39.98029 1.000 16.83843 ? 322 TRP A CD2   1 
ATOM   2515 N  NE1   . TRP A 1 322 ? 6.41830   -11.76703 -40.39125 1.000 16.46668 ? 322 TRP A NE1   1 
ATOM   2516 C  CE2   . TRP A 1 322 ? 6.42924   -13.09604 -40.05728 1.000 13.38239 ? 322 TRP A CE2   1 
ATOM   2517 C  CE3   . TRP A 1 322 ? 4.82315   -14.85596 -39.65232 1.000 16.16961 ? 322 TRP A CE3   1 
ATOM   2518 C  CZ2   . TRP A 1 322 ? 7.49820   -13.95010 -39.81631 1.000 10.92671 ? 322 TRP A CZ2   1 
ATOM   2519 C  CZ3   . TRP A 1 322 ? 5.88711   -15.70302 -39.41334 1.000 12.47927 ? 322 TRP A CZ3   1 
ATOM   2520 C  CH2   . TRP A 1 322 ? 7.20713   -15.24709 -39.49634 1.000 14.96052 ? 322 TRP A CH2   1 
ATOM   2521 N  N     . ASP A 1 323 ? -0.04080  -13.76469 -40.78428 1.000 20.14748 ? 323 ASP A N     1 
ATOM   2522 C  CA    . ASP A 1 323 ? -1.49580  -13.74562 -40.75027 1.000 18.88673 ? 323 ASP A CA    1 
ATOM   2523 C  C     . ASP A 1 323 ? -2.01874  -12.76862 -39.70524 1.000 19.67420 ? 323 ASP A C     1 
ATOM   2524 O  O     . ASP A 1 323 ? -1.33672  -12.43667 -38.73324 1.000 19.99526 ? 323 ASP A O     1 
ATOM   2525 C  CB    . ASP A 1 323 ? -2.05587  -15.13860 -40.45830 1.000 22.65984 ? 323 ASP A CB    1 
ATOM   2526 C  CG    . ASP A 1 323 ? -1.72092  -16.14459 -41.53932 1.000 19.20723 ? 323 ASP A CG    1 
ATOM   2527 O  OD1   . ASP A 1 323 ? -1.49191  -15.72857 -42.69432 1.000 17.78419 ? 323 ASP A OD1   1 
ATOM   2528 O  OD2   . ASP A 1 323 ? -1.68798  -17.35560 -41.23235 1.000 16.65810 ? 323 ASP A OD2   1 
ATOM   2529 N  N     . ASP A 1 324 ? -3.24972  -12.31455 -39.91723 1.000 20.38215 ? 324 ASP A N     1 
ATOM   2530 C  CA    . ASP A 1 324 ? -3.98368  -11.50953 -38.94621 1.000 20.79956 ? 324 ASP A CA    1 
ATOM   2531 C  C     . ASP A 1 324 ? -5.05172  -12.42449 -38.35322 1.000 24.18597 ? 324 ASP A C     1 
ATOM   2532 O  O     . ASP A 1 324 ? -6.15473  -12.55043 -38.88722 1.000 20.55533 ? 324 ASP A O     1 
ATOM   2533 C  CB    . ASP A 1 324 ? -4.58762  -10.26349 -39.59417 1.000 25.31319 ? 324 ASP A CB    1 
ATOM   2534 C  CG    . ASP A 1 324 ? -5.20557  -9.31348  -38.57915 1.000 26.77579 ? 324 ASP A CG    1 
ATOM   2535 O  OD1   . ASP A 1 324 ? -5.13357  -9.59751  -37.36616 1.000 26.05499 ? 324 ASP A OD1   1 
ATOM   2536 O  OD2   . ASP A 1 324 ? -5.76551  -8.27844  -38.99812 1.000 30.79563 ? 324 ASP A OD2   1 
ATOM   2537 N  N     . ASN A 1 325 ? -4.70875  -13.07754 -37.24624 1.000 22.23097 ? 325 ASN A N     1 
ATOM   2538 C  CA    . ASN A 1 325 ? -5.58080  -14.05151 -36.59526 1.000 22.18252 ? 325 ASN A CA    1 
ATOM   2539 C  C     . ASN A 1 325 ? -5.69077  -13.67154 -35.12725 1.000 19.10559 ? 325 ASN A C     1 
ATOM   2540 O  O     . ASN A 1 325 ? -4.84079  -14.05960 -34.31126 1.000 19.67747 ? 325 ASN A O     1 
ATOM   2541 C  CB    . ASN A 1 325 ? -5.03787  -15.47053 -36.76330 1.000 20.36141 ? 325 ASN A CB    1 
ATOM   2542 C  CG    . ASN A 1 325 ? -6.09592  -16.53648 -36.54432 1.000 23.90932 ? 325 ASN A CG    1 
ATOM   2543 O  OD1   . ASN A 1 325 ? -6.23697  -17.45546 -37.35034 1.000 28.74721 ? 325 ASN A OD1   1 
ATOM   2544 N  ND2   . ASN A 1 325 ? -6.84391  -16.42147 -35.45431 1.000 22.31175 ? 325 ASN A ND2   1 
ATOM   2545 N  N     . PRO A 1 326 ? -6.72373  -12.91050 -34.74723 1.000 21.60745 ? 326 PRO A N     1 
ATOM   2546 C  CA    . PRO A 1 326 ? -6.86871  -12.52352 -33.33322 1.000 21.83137 ? 326 PRO A CA    1 
ATOM   2547 C  C     . PRO A 1 326 ? -7.17376  -13.68953 -32.41325 1.000 18.66136 ? 326 PRO A C     1 
ATOM   2548 O  O     . PRO A 1 326 ? -7.01575  -13.55356 -31.19524 1.000 18.00719 ? 326 PRO A O     1 
ATOM   2549 C  CB    . PRO A 1 326 ? -8.02866  -11.51446 -33.35519 1.000 20.98529 ? 326 PRO A CB    1 
ATOM   2550 C  CG    . PRO A 1 326 ? -8.20464  -11.13642 -34.78818 1.000 18.73342 ? 326 PRO A CG    1 
ATOM   2551 C  CD    . PRO A 1 326 ? -7.78771  -12.33142 -35.58421 1.000 20.62599 ? 326 PRO A CD    1 
ATOM   2552 N  N     . GLU A 1 327 ? -7.61282  -14.82349 -32.95327 1.000 20.33660 ? 327 GLU A N     1 
ATOM   2553 C  CA    A GLU A 1 327 ? -7.90588  -15.97950 -32.11530 0.696 22.02713 ? 327 GLU A CA    1 
ATOM   2554 C  CA    B GLU A 1 327 ? -7.90688  -15.98950 -32.12630 0.304 21.96600 ? 327 GLU A CA    1 
ATOM   2555 C  C     . GLU A 1 327 ? -6.63191  -16.70557 -31.69932 1.000 20.62493 ? 327 GLU A C     1 
ATOM   2556 O  O     . GLU A 1 327 ? -6.52293  -17.16360 -30.55633 1.000 17.70584 ? 327 GLU A O     1 
ATOM   2557 C  CB    A GLU A 1 327 ? -8.85193  -16.93543 -32.84232 0.696 20.42937 ? 327 GLU A CB    1 
ATOM   2558 C  CB    B GLU A 1 327 ? -8.81593  -16.95343 -32.88532 0.304 20.49035 ? 327 GLU A CB    1 
ATOM   2559 C  CG    A GLU A 1 327 ? -10.27990 -16.42136 -32.97330 0.696 22.74730 ? 327 GLU A CG    1 
ATOM   2560 C  CG    B GLU A 1 327 ? -9.83490  -16.25936 -33.77030 0.304 22.40318 ? 327 GLU A CG    1 
ATOM   2561 C  CD    A GLU A 1 327 ? -10.39985 -15.22433 -33.89927 0.696 24.13262 ? 327 GLU A CD    1 
ATOM   2562 C  CD    B GLU A 1 327 ? -10.44295 -17.19231 -34.79732 0.304 24.19308 ? 327 GLU A CD    1 
ATOM   2563 O  OE1   A GLU A 1 327 ? -9.58584  -15.11535 -34.84027 0.696 26.43614 ? 327 GLU A OE1   1 
ATOM   2564 O  OE1   B GLU A 1 327 ? -10.35801 -18.42331 -34.60634 0.304 24.91233 ? 327 GLU A OE1   1 
ATOM   2565 O  OE2   A GLU A 1 327 ? -11.30280 -14.38729 -33.68225 0.696 26.07072 ? 327 GLU A OE2   1 
ATOM   2566 O  OE2   B GLU A 1 327 ? -11.00093 -16.69525 -35.79830 0.304 26.29144 ? 327 GLU A OE2   1 
ATOM   2567 N  N     . PHE A 1 328 ? -5.66092  -16.81860 -32.60733 1.000 22.89109 ? 328 PHE A N     1 
ATOM   2568 C  CA    . PHE A 1 328 ? -4.39595  -17.44867 -32.24935 1.000 16.21594 ? 328 PHE A CA    1 
ATOM   2569 C  C     . PHE A 1 328 ? -3.58490  -16.55473 -31.32333 1.000 13.98318 ? 328 PHE A C     1 
ATOM   2570 O  O     . PHE A 1 328 ? -2.87192  -17.04779 -30.44434 1.000 13.68586 ? 328 PHE A O     1 
ATOM   2571 C  CB    . PHE A 1 328 ? -3.59797  -17.77868 -33.51036 1.000 19.34082 ? 328 PHE A CB    1 
ATOM   2572 C  CG    . PHE A 1 328 ? -4.13104  -18.95264 -34.27538 1.000 21.31983 ? 328 PHE A CG    1 
ATOM   2573 C  CD1   . PHE A 1 328 ? -4.91008  -19.90961 -33.64840 1.000 19.76986 ? 328 PHE A CD1   1 
ATOM   2574 C  CD2   . PHE A 1 328 ? -3.85005  -19.10362 -35.61839 1.000 18.39531 ? 328 PHE A CD2   1 
ATOM   2575 C  CE1   . PHE A 1 328 ? -5.39914  -20.98657 -34.35242 1.000 22.46702 ? 328 PHE A CE1   1 
ATOM   2576 C  CE2   . PHE A 1 328 ? -4.33611  -20.17758 -36.32641 1.000 16.69371 ? 328 PHE A CE2   1 
ATOM   2577 C  CZ    . PHE A 1 328 ? -5.11315  -21.12155 -35.69243 1.000 19.09512 ? 328 PHE A CZ    1 
ATOM   2578 N  N     . LEU A 1 329 ? -3.67784  -15.23673 -31.50830 1.000 13.17551 ? 329 LEU A N     1 
ATOM   2579 C  CA    . LEU A 1 329 ? -2.99079  -14.31478 -30.60928 1.000 14.27525 ? 329 LEU A CA    1 
ATOM   2580 C  C     . LEU A 1 329 ? -3.59678  -14.36778 -29.21228 1.000 12.64371 ? 329 LEU A C     1 
ATOM   2581 O  O     . LEU A 1 329 ? -2.87279  -14.46784 -28.21628 1.000 15.75334 ? 329 LEU A O     1 
ATOM   2582 C  CB    . LEU A 1 329 ? -3.03872  -12.88977 -31.17524 1.000 15.12246 ? 329 LEU A CB    1 
ATOM   2583 C  CG    . LEU A 1 329 ? -1.96666  -11.88183 -30.74522 1.000 15.13161 ? 329 LEU A CG    1 
ATOM   2584 C  CD1   . LEU A 1 329 ? -2.20963  -11.35885 -29.33521 1.000 18.29066 ? 329 LEU A CD1   1 
ATOM   2585 C  CD2   . LEU A 1 329 ? -0.57470  -12.49190 -30.86024 1.000 12.23170 ? 329 LEU A CD2   1 
ATOM   2586 N  N     . ALA A 1 330 ? -4.92878  -14.31372 -29.12027 1.000 15.45199 ? 330 ALA A N     1 
ATOM   2587 C  CA    . ALA A 1 330 ? -5.57578  -14.31372 -27.81227 1.000 15.34850 ? 330 ALA A CA    1 
ATOM   2588 C  C     . ALA A 1 330 ? -5.31584  -15.61575 -27.06430 1.000 14.93036 ? 330 ALA A C     1 
ATOM   2589 O  O     . ALA A 1 330 ? -5.03583  -15.60279 -25.86030 1.000 14.45999 ? 330 ALA A O     1 
ATOM   2590 C  CB    . ALA A 1 330 ? -7.07676  -14.07464 -27.96325 1.000 14.06120 ? 330 ALA A CB    1 
ATOM   2591 N  N     . ALA A 1 331 ? -5.39990  -16.75273 -27.76232 1.000 12.72863 ? 331 ALA A N     1 
ATOM   2592 C  CA    . ALA A 1 331 ? -5.14396  -18.03876 -27.12136 1.000 10.95052 ? 331 ALA A CA    1 
ATOM   2593 C  C     . ALA A 1 331 ? -3.69397  -18.14984 -26.66636 1.000 12.26567 ? 331 ALA A C     1 
ATOM   2594 O  O     . ALA A 1 331 ? -3.41299  -18.68688 -25.58938 1.000 8.59915  ? 331 ALA A O     1 
ATOM   2595 C  CB    . ALA A 1 331 ? -5.49702  -19.18171 -28.07438 1.000 12.79577 ? 331 ALA A CB    1 
ATOM   2596 N  N     . TRP A 1 332 ? -2.76194  -17.64787 -27.47936 1.000 13.11275 ? 332 TRP A N     1 
ATOM   2597 C  CA    . TRP A 1 332 ? -1.35194  -17.65695 -27.10336 1.000 9.55998  ? 332 TRP A CA    1 
ATOM   2598 C  C     . TRP A 1 332 ? -1.07289  -16.65999 -25.98434 1.000 13.60814 ? 332 TRP A C     1 
ATOM   2599 O  O     . TRP A 1 332 ? -0.29390  -16.94705 -25.06835 1.000 12.11939 ? 332 TRP A O     1 
ATOM   2600 C  CB    . TRP A 1 332 ? -0.49293  -17.35096 -28.33136 1.000 12.82806 ? 332 TRP A CB    1 
ATOM   2601 C  CG    . TRP A 1 332 ? 0.98407   -17.39104 -28.09836 1.000 9.20709  ? 332 TRP A CG    1 
ATOM   2602 C  CD1   . TRP A 1 332 ? 1.78101   -18.49808 -28.08239 1.000 13.78775 ? 332 TRP A CD1   1 
ATOM   2603 C  CD2   . TRP A 1 332 ? 1.84812   -16.27309 -27.87734 1.000 9.68771  ? 332 TRP A CD2   1 
ATOM   2604 N  NE1   . TRP A 1 332 ? 3.08603   -18.14015 -27.85239 1.000 9.62594  ? 332 TRP A NE1   1 
ATOM   2605 C  CE2   . TRP A 1 332 ? 3.15410   -16.77816 -27.72336 1.000 9.77109  ? 332 TRP A CE2   1 
ATOM   2606 C  CE3   . TRP A 1 332 ? 1.64519   -14.89308 -27.78831 1.000 9.82973  ? 332 TRP A CE3   1 
ATOM   2607 C  CZ2   . TRP A 1 332 ? 4.25014   -15.95422 -27.48434 1.000 9.09090  ? 332 TRP A CZ2   1 
ATOM   2608 C  CZ3   . TRP A 1 332 ? 2.73424   -14.07714 -27.55229 1.000 13.58173 ? 332 TRP A CZ3   1 
ATOM   2609 C  CH2   . TRP A 1 332 ? 4.02021   -14.61021 -27.40031 1.000 9.66596  ? 332 TRP A CH2   1 
ATOM   2610 N  N     . ARG A 1 333 ? -1.71953  -15.49262 -26.03531 1.000 11.41714 ? 333 ARG A N     1 
ATOM   2611 C  CA    . ARG A 1 333 ? -1.47394  -14.44565 -25.04639 1.000 10.50727 ? 333 ARG A CA    1 
ATOM   2612 C  C     . ARG A 1 333 ? -2.03848  -14.82377 -23.68346 1.000 9.75690  ? 333 ARG A C     1 
ATOM   2613 O  O     . ARG A 1 333 ? -1.42267  -14.53427 -22.64826 1.000 5.25439  ? 333 ARG A O     1 
ATOM   2614 C  CB    . ARG A 1 333 ? -2.08112  -13.13139 -25.54139 1.000 13.63212 ? 333 ARG A CB    1 
ATOM   2615 C  CG    . ARG A 1 333 ? -2.14230  -12.00032 -24.53582 1.000 12.11910 ? 333 ARG A CG    1 
ATOM   2616 C  CD    . ARG A 1 333 ? -2.84488  -10.80500 -25.16500 1.000 14.78504 ? 333 ARG A CD    1 
ATOM   2617 N  NE    . ARG A 1 333 ? -4.23658  -11.11215 -25.46999 1.000 18.29410 ? 333 ARG A NE    1 
ATOM   2618 C  CZ    . ARG A 1 333 ? -4.93398  -10.56346 -26.45526 1.000 18.73446 ? 333 ARG A CZ    1 
ATOM   2619 N  NH1   . ARG A 1 333 ? -4.37959  -9.71648  -27.30910 1.000 20.05241 ? 333 ARG A NH1   1 
ATOM   2620 N  NH2   . ARG A 1 333 ? -6.21993  -10.87530 -26.58907 1.000 16.52670 ? 333 ARG A NH2   1 
ATOM   2621 N  N     . GLU A 1 334 ? -3.20082  -15.47094 -23.66130 1.000 11.82164 ? 334 GLU A N     1 
ATOM   2622 C  CA    . GLU A 1 334 ? -3.87883  -15.84293 -22.42731 1.000 12.89645 ? 334 GLU A CA    1 
ATOM   2623 C  C     . GLU A 1 334 ? -3.48590  -17.22896 -21.92934 1.000 14.00293 ? 334 GLU A C     1 
ATOM   2624 O  O     . GLU A 1 334 ? -4.11292  -17.73595 -20.99335 1.000 14.93868 ? 334 GLU A O     1 
ATOM   2625 C  CB    . GLU A 1 334 ? -5.39383  -15.76785 -22.62530 1.000 10.35480 ? 334 GLU A CB    1 
ATOM   2626 C  CG    . GLU A 1 334 ? -5.88276  -14.38981 -23.02727 1.000 11.41812 ? 334 GLU A CG    1 
ATOM   2627 C  CD    . GLU A 1 334 ? -7.28676  -14.40973 -23.58626 1.000 13.00386 ? 334 GLU A CD    1 
ATOM   2628 O  OE1   . GLU A 1 334 ? -7.95482  -15.46070 -23.49428 1.000 12.94148 ? 334 GLU A OE1   1 
ATOM   2629 O  OE2   . GLU A 1 334 ? -7.71871  -13.37170 -24.12724 1.000 21.91955 ? 334 GLU A OE2   1 
ATOM   2630 N  N     . ALA A 1 335 ? -2.46893  -17.84600 -22.53736 1.000 9.99283  ? 335 ALA A N     1 
ATOM   2631 C  CA    . ALA A 1 335 ? -1.94200  -19.14304 -22.10839 1.000 11.07028 ? 335 ALA A CA    1 
ATOM   2632 C  C     . ALA A 1 335 ? -3.02705  -20.21998 -22.10342 1.000 11.28745 ? 335 ALA A C     1 
ATOM   2633 O  O     . ALA A 1 335 ? -3.26308  -20.88999 -21.09643 1.000 11.08666 ? 335 ALA A O     1 
ATOM   2634 C  CB    . ALA A 1 335 ? -1.27099  -19.03810 -20.73539 1.000 12.68369 ? 335 ALA A CB    1 
ATOM   2635 N  N     . ARG A 1 336 ? -3.68156  -20.38216 -23.25444 1.000 7.85787  ? 336 ARG A N     1 
ATOM   2636 C  CA    . ARG A 1 336 ? -4.69773  -21.41348 -23.44992 1.000 11.49132 ? 336 ARG A CA    1 
ATOM   2637 C  C     . ARG A 1 336 ? -4.57514  -22.01572 -24.84213 1.000 11.70985 ? 336 ARG A C     1 
ATOM   2638 O  O     . ARG A 1 336 ? -5.57278  -22.23552 -25.53860 1.000 8.39314  ? 336 ARG A O     1 
ATOM   2639 C  CB    . ARG A 1 336 ? -6.10809  -20.86882 -23.21397 1.000 10.78619 ? 336 ARG A CB    1 
ATOM   2640 C  CG    . ARG A 1 336 ? -6.43940  -19.57654 -23.95050 1.000 10.43746 ? 336 ARG A CG    1 
ATOM   2641 C  CD    . ARG A 1 336 ? -7.90633  -19.19965 -23.74842 1.000 12.54342 ? 336 ARG A CD    1 
ATOM   2642 N  NE    . ARG A 1 336 ? -8.26663  -17.95854 -24.42604 1.000 12.57949 ? 336 ARG A NE    1 
ATOM   2643 C  CZ    . ARG A 1 336 ? -8.66685  -17.88351 -25.68866 1.000 11.24401 ? 336 ARG A CZ    1 
ATOM   2644 N  NH1   . ARG A 1 336 ? -8.76143  -18.96213 -26.45003 1.000 19.36395 ? 336 ARG A NH1   1 
ATOM   2645 N  NH2   . ARG A 1 336 ? -8.97610  -16.69635 -26.20214 1.000 14.56602 ? 336 ARG A NH2   1 
ATOM   2646 N  N     . THR A 1 337 ? -3.34317  -22.29289 -25.26446 1.000 9.33661  ? 337 THR A N     1 
ATOM   2647 C  CA    . THR A 1 337 ? -3.12821  -22.93187 -26.55748 1.000 11.16552 ? 337 THR A CA    1 
ATOM   2648 C  C     . THR A 1 337 ? -3.49228  -24.41085 -26.53851 1.000 9.09017  ? 337 THR A C     1 
ATOM   2649 O  O     . THR A 1 337 ? -3.72432  -24.99582 -27.60153 1.000 11.64030 ? 337 THR A O     1 
ATOM   2650 C  CB    . THR A 1 337 ? -1.66820  -22.76893 -26.98648 1.000 7.90976  ? 337 THR A CB    1 
ATOM   2651 O  OG1   . THR A 1 337 ? -0.81723  -23.39700 -26.02050 1.000 9.31391  ? 337 THR A OG1   1 
ATOM   2652 C  CG2   . THR A 1 337 ? -1.29913  -21.30195 -27.07245 1.000 11.99817 ? 337 THR A CG2   1 
ATOM   2653 N  N     . GLY A 1 338 ? -3.55531  -25.02388 -25.35853 1.000 9.40778  ? 338 GLY A N     1 
ATOM   2654 C  CA    . GLY A 1 338 ? -3.75538  -26.44987 -25.24456 1.000 10.90762 ? 338 GLY A CA    1 
ATOM   2655 C  C     . GLY A 1 338 ? -2.48342  -27.25594 -25.10958 1.000 12.13154 ? 338 GLY A C     1 
ATOM   2656 O  O     . GLY A 1 338 ? -2.55848  -28.46194 -24.83761 1.000 11.60148 ? 338 GLY A O     1 
ATOM   2657 N  N     . PHE A 1 339 ? -1.31839  -26.63099 -25.29557 1.000 7.87086  ? 339 PHE A N     1 
ATOM   2658 C  CA    . PHE A 1 339 ? -0.04042  -27.29806 -25.10459 1.000 10.59472 ? 339 PHE A CA    1 
ATOM   2659 C  C     . PHE A 1 339 ? 0.52960   -26.87812 -23.76059 1.000 8.65215  ? 339 PHE A C     1 
ATOM   2660 O  O     . PHE A 1 339 ? 0.89966   -25.70514 -23.59556 1.000 9.82560  ? 339 PHE A O     1 
ATOM   2661 C  CB    . PHE A 1 339 ? 0.92959   -26.94708 -26.23059 1.000 9.93362  ? 339 PHE A CB    1 
ATOM   2662 C  CG    . PHE A 1 339 ? 0.46956   -27.38903 -27.59160 1.000 10.26203 ? 339 PHE A CG    1 
ATOM   2663 C  CD1   . PHE A 1 339 ? 0.80450   -28.64403 -28.08063 1.000 13.56545 ? 339 PHE A CD1   1 
ATOM   2664 C  CD2   . PHE A 1 339 ? -0.29140  -26.54697 -28.38458 1.000 11.41358 ? 339 PHE A CD2   1 
ATOM   2665 C  CE1   . PHE A 1 339 ? 0.38547   -29.05198 -29.33564 1.000 15.15980 ? 339 PHE A CE1   1 
ATOM   2666 C  CE2   . PHE A 1 339 ? -0.71242  -26.94592 -29.63658 1.000 12.47590 ? 339 PHE A CE2   1 
ATOM   2667 C  CZ    . PHE A 1 339 ? -0.37449  -28.20293 -30.11361 1.000 18.93280 ? 339 PHE A CZ    1 
ATOM   2668 N  N     . PRO A 1 340 ? 0.61056   -27.77915 -22.77761 1.000 8.52423  ? 340 PRO A N     1 
ATOM   2669 C  CA    . PRO A 1 340 ? 1.05959   -27.37120 -21.43560 1.000 10.14622 ? 340 PRO A CA    1 
ATOM   2670 C  C     . PRO A 1 340 ? 2.44362   -26.74827 -21.40859 1.000 9.70257  ? 340 PRO A C     1 
ATOM   2671 O  O     . PRO A 1 340 ? 2.69367   -25.86531 -20.57857 1.000 7.72319  ? 340 PRO A O     1 
ATOM   2672 C  CB    . PRO A 1 340 ? 1.01653   -28.68622 -20.64463 1.000 9.88802  ? 340 PRO A CB    1 
ATOM   2673 C  CG    . PRO A 1 340 ? -0.01752  -29.50915 -21.35465 1.000 9.46306  ? 340 PRO A CG    1 
ATOM   2674 C  CD    . PRO A 1 340 ? 0.13049   -29.17112 -22.80664 1.000 9.73533  ? 340 PRO A CD    1 
ATOM   2675 N  N     . TRP A 1 341 ? 3.35060   -27.17730 -22.28861 1.000 8.28089  ? 341 TRP A N     1 
ATOM   2676 C  CA    . TRP A 1 341 ? 4.67663   -26.56837 -22.33160 1.000 8.95113  ? 341 TRP A CA    1 
ATOM   2677 C  C     . TRP A 1 341 ? 4.59770   -25.10235 -22.73956 1.000 9.36759  ? 341 TRP A C     1 
ATOM   2678 O  O     . TRP A 1 341 ? 5.30374   -24.25640 -22.17954 1.000 6.88637  ? 341 TRP A O     1 
ATOM   2679 C  CB    . TRP A 1 341 ? 5.58358   -27.34739 -23.28462 1.000 8.93940  ? 341 TRP A CB    1 
ATOM   2680 C  CG    . TRP A 1 341 ? 6.97361   -26.79746 -23.38661 1.000 8.71192  ? 341 TRP A CG    1 
ATOM   2681 C  CD1   . TRP A 1 341 ? 7.53364   -26.18446 -24.46960 1.000 9.33305  ? 341 TRP A CD1   1 
ATOM   2682 C  CD2   . TRP A 1 341 ? 7.97961   -26.80253 -22.36561 1.000 7.35714  ? 341 TRP A CD2   1 
ATOM   2683 N  NE1   . TRP A 1 341 ? 8.82566   -25.81053 -24.18959 1.000 9.14352  ? 341 TRP A NE1   1 
ATOM   2684 C  CE2   . TRP A 1 341 ? 9.12364   -26.17758 -22.90460 1.000 8.71036  ? 341 TRP A CE2   1 
ATOM   2685 C  CE3   . TRP A 1 341 ? 8.02460   -27.27356 -21.04963 1.000 8.42884  ? 341 TRP A CE3   1 
ATOM   2686 C  CZ2   . TRP A 1 341 ? 10.29565  -26.01565 -22.17560 1.000 8.90968  ? 341 TRP A CZ2   1 
ATOM   2687 C  CZ3   . TRP A 1 341 ? 9.19061   -27.10864 -20.32863 1.000 6.68221  ? 341 TRP A CZ3   1 
ATOM   2688 C  CH2   . TRP A 1 341 ? 10.30964  -26.48568 -20.89262 1.000 9.88954  ? 341 TRP A CH2   1 
ATOM   2689 N  N     . ILE A 1 342 ? 3.73571   -24.77729 -23.70455 1.000 7.84278  ? 342 ILE A N     1 
ATOM   2690 C  CA    . ILE A 1 342 ? 3.61178   -23.39327 -24.15352 1.000 7.35836  ? 342 ILE A CA    1 
ATOM   2691 C  C     . ILE A 1 342 ? 2.85683   -22.56025 -23.12049 1.000 7.15468  ? 342 ILE A C     1 
ATOM   2692 O  O     . ILE A 1 342 ? 3.27688   -21.45428 -22.76347 1.000 9.67308  ? 342 ILE A O     1 
ATOM   2693 C  CB    . ILE A 1 342 ? 2.93478   -23.33920 -25.53651 1.000 6.12477  ? 342 ILE A CB    1 
ATOM   2694 C  CG1   . ILE A 1 342 ? 3.74973   -24.11722 -26.57653 1.000 6.80804  ? 342 ILE A CG1   1 
ATOM   2695 C  CG2   . ILE A 1 342 ? 2.71685   -21.89818 -25.98148 1.000 10.13267 ? 342 ILE A CG2   1 
ATOM   2696 C  CD1   . ILE A 1 342 ? 5.19176   -23.66929 -26.71353 1.000 4.64771  ? 342 ILE A CD1   1 
ATOM   2697 N  N     . ASP A 1 343 ? 1.73880   -23.08921 -22.61350 1.000 6.99075  ? 343 ASP A N     1 
ATOM   2698 C  CA    . ASP A 1 343 ? 0.91384   -22.34919 -21.66148 1.000 7.22308  ? 343 ASP A CA    1 
ATOM   2699 C  C     . ASP A 1 343 ? 1.63686   -22.10726 -20.33948 1.000 7.31816  ? 343 ASP A C     1 
ATOM   2700 O  O     . ASP A 1 343 ? 1.38391   -21.09626 -19.67345 1.000 6.76141  ? 343 ASP A O     1 
ATOM   2701 C  CB    . ASP A 1 343 ? -0.40120  -23.09813 -21.42949 1.000 7.40906  ? 343 ASP A CB    1 
ATOM   2702 C  CG    . ASP A 1 343 ? -1.21721  -23.25906 -22.70749 1.000 9.07539  ? 343 ASP A CG    1 
ATOM   2703 O  OD1   . ASP A 1 343 ? -0.87418  -22.61705 -23.72148 1.000 9.73686  ? 343 ASP A OD1   1 
ATOM   2704 O  OD2   . ASP A 1 343 ? -2.20325  -24.02901 -22.69951 1.000 8.54616  ? 343 ASP A OD2   1 
ATOM   2705 N  N     . ALA A 1 344 ? 2.53681   -23.01231 -19.94550 1.000 6.09224  ? 344 ALA A N     1 
ATOM   2706 C  CA    . ALA A 1 344 ? 3.28783   -22.81938 -18.70650 1.000 5.94975  ? 344 ALA A CA    1 
ATOM   2707 C  C     . ALA A 1 344 ? 4.28889   -21.67943 -18.83548 1.000 5.16246  ? 344 ALA A C     1 
ATOM   2708 O  O     . ALA A 1 344 ? 4.48093   -20.90446 -17.88946 1.000 4.39929  ? 344 ALA A O     1 
ATOM   2709 C  CB    . ALA A 1 344 ? 4.00877   -24.10743 -18.31654 1.000 6.91144  ? 344 ALA A CB    1 
ATOM   2710 N  N     . ILE A 1 345 ? 4.95289   -21.57643 -19.98948 1.000 4.35302  ? 345 ILE A N     1 
ATOM   2711 C  CA    . ILE A 1 345 ? 5.91294   -20.49948 -20.20246 1.000 5.11681  ? 345 ILE A CA    1 
ATOM   2712 C  C     . ILE A 1 345 ? 5.20301   -19.15144 -20.24742 1.000 5.24678  ? 345 ILE A C     1 
ATOM   2713 O  O     . ILE A 1 345 ? 5.66706   -18.17148 -19.65140 1.000 5.76644  ? 345 ILE A O     1 
ATOM   2714 C  CB    . ILE A 1 345 ? 6.72992   -20.75549 -21.48247 1.000 5.37091  ? 345 ILE A CB    1 
ATOM   2715 C  CG1   . ILE A 1 345 ? 7.53786   -22.05053 -21.35550 1.000 5.66824  ? 345 ILE A CG1   1 
ATOM   2716 C  CG2   . ILE A 1 345 ? 7.64598   -19.57953 -21.77744 1.000 6.46850  ? 345 ILE A CG2   1 
ATOM   2717 C  CD1   . ILE A 1 345 ? 8.26083   -22.45554 -22.63051 1.000 7.86987  ? 345 ILE A CD1   1 
ATOM   2718 N  N     . MET A 1 346 ? 4.06701   -19.07737 -20.94842 1.000 5.50909  ? 346 MET A N     1 
ATOM   2719 C  CA    . MET A 1 346 ? 3.29807   -17.83633 -20.98438 1.000 6.08844  ? 346 MET A CA    1 
ATOM   2720 C  C     . MET A 1 346 ? 2.73510   -17.48633 -19.61037 1.000 6.41387  ? 346 MET A C     1 
ATOM   2721 O  O     . MET A 1 346 ? 2.50516   -16.30733 -19.31335 1.000 7.03588  ? 346 MET A O     1 
ATOM   2722 C  CB    . MET A 1 346 ? 2.16806   -17.94325 -22.00838 1.000 6.82287  ? 346 MET A CB    1 
ATOM   2723 C  CG    . MET A 1 346 ? 2.63704   -18.21224 -23.43239 1.000 9.99622  ? 346 MET A CG    1 
ATOM   2724 S  SD    . MET A 1 346 ? 3.77410   -16.96228 -24.06337 1.000 10.34382 ? 346 MET A SD    1 
ATOM   2725 C  CE    . MET A 1 346 ? 2.71618   -15.51822 -24.09233 1.000 9.72009  ? 346 MET A CE    1 
ATOM   2726 N  N     . THR A 1 347 ? 2.49005   -18.49434 -18.77240 1.000 7.12468  ? 347 THR A N     1 
ATOM   2727 C  CA    . THR A 1 347 ? 2.10507   -18.23435 -17.38939 1.000 7.11185  ? 347 THR A CA    1 
ATOM   2728 C  C     . THR A 1 347 ? 3.28010   -17.67943 -16.59538 1.000 5.65405  ? 347 THR A C     1 
ATOM   2729 O  O     . THR A 1 347 ? 3.11615   -16.74244 -15.80636 1.000 5.88489  ? 347 THR A O     1 
ATOM   2730 C  CB    . THR A 1 347 ? 1.57100   -19.51334 -16.74242 1.000 7.48014  ? 347 THR A CB    1 
ATOM   2731 O  OG1   . THR A 1 347 ? 0.39798   -19.95426 -17.43942 1.000 5.49182  ? 347 THR A OG1   1 
ATOM   2732 C  CG2   . THR A 1 347 ? 1.22602   -19.27236 -15.28241 1.000 7.86699  ? 347 THR A CG2   1 
ATOM   2733 N  N     . GLN A 1 348 ? 4.47607   -18.23649 -16.79640 1.000 5.44455  ? 348 GLN A N     1 
ATOM   2734 C  CA    . GLN A 1 348 ? 5.66210   -17.67356 -16.16039 1.000 4.97823  ? 348 GLN A CA    1 
ATOM   2735 C  C     . GLN A 1 348 ? 5.91317   -16.24556 -16.62936 1.000 5.96442  ? 348 GLN A C     1 
ATOM   2736 O  O     . GLN A 1 348 ? 6.44421   -15.42661 -15.87034 1.000 4.27893  ? 348 GLN A O     1 
ATOM   2737 C  CB    . GLN A 1 348 ? 6.87905   -18.55662 -16.44542 1.000 6.57416  ? 348 GLN A CB    1 
ATOM   2738 C  CG    . GLN A 1 348 ? 8.16908   -18.10670 -15.76441 1.000 6.80464  ? 348 GLN A CG    1 
ATOM   2739 C  CD    . GLN A 1 348 ? 9.38704   -18.89175 -16.22543 1.000 5.21594  ? 348 GLN A CD    1 
ATOM   2740 O  OE1   . GLN A 1 348 ? 9.40000   -19.46072 -17.31845 1.000 7.26025  ? 348 GLN A OE1   1 
ATOM   2741 N  NE2   . GLN A 1 348 ? 10.41804  -18.92582 -15.39044 1.000 10.03393 ? 348 GLN A NE2   1 
ATOM   2742 N  N     . LEU A 1 349 ? 5.53218   -15.93151 -17.87035 1.000 6.43787  ? 349 LEU A N     1 
ATOM   2743 C  CA    . LEU A 1 349 ? 5.70725   -14.57951 -18.39232 1.000 5.61578  ? 349 LEU A CA    1 
ATOM   2744 C  C     . LEU A 1 349 ? 4.88130   -13.57049 -17.60229 1.000 7.51749  ? 349 LEU A C     1 
ATOM   2745 O  O     . LEU A 1 349 ? 5.39336   -12.53152 -17.17427 1.000 6.49896  ? 349 LEU A O     1 
ATOM   2746 C  CB    . LEU A 1 349 ? 5.32924   -14.54146 -19.87331 1.000 4.26927  ? 349 LEU A CB    1 
ATOM   2747 C  CG    . LEU A 1 349 ? 5.19531   -13.15543 -20.50528 1.000 5.35282  ? 349 LEU A CG    1 
ATOM   2748 C  CD1   . LEU A 1 349 ? 6.52335   -12.44150 -20.50427 1.000 10.44541 ? 349 LEU A CD1   1 
ATOM   2749 C  CD2   . LEU A 1 349 ? 4.63830   -13.25037 -21.91528 1.000 12.86487 ? 349 LEU A CD2   1 
ATOM   2750 N  N     . VAL A 1 350 ? 3.59529   -13.86343 -17.39629 1.000 7.42891  ? 350 VAL A N     1 
ATOM   2751 C  CA    . VAL A 1 350 ? 2.71634   -12.91040 -16.72227 1.000 5.77181  ? 350 VAL A CA    1 
ATOM   2752 C  C     . VAL A 1 350 ? 2.90535   -12.89944 -15.21027 1.000 6.12163  ? 350 VAL A C     1 
ATOM   2753 O  O     . VAL A 1 350 ? 2.53840   -11.91444 -14.55724 1.000 9.41505  ? 350 VAL A O     1 
ATOM   2754 C  CB    . VAL A 1 350 ? 1.24532   -13.19932 -17.06527 1.000 9.06286  ? 350 VAL A CB    1 
ATOM   2755 C  CG1   . VAL A 1 350 ? 1.02232   -13.12727 -18.57026 1.000 6.48620  ? 350 VAL A CG1   1 
ATOM   2756 C  CG2   . VAL A 1 350 ? 0.82926   -14.55831 -16.52830 1.000 8.61853  ? 350 VAL A CG2   1 
ATOM   2757 N  N     . THR A 1 351 ? 3.46429   -13.96249 -14.63229 1.000 5.53711  ? 351 THR A N     1 
ATOM   2758 C  CA    . THR A 1 351 ? 3.66529   -14.04953 -13.18930 1.000 6.41343  ? 351 THR A CA    1 
ATOM   2759 C  C     . THR A 1 351 ? 5.05732   -13.61561 -12.74929 1.000 6.69416  ? 351 THR A C     1 
ATOM   2760 O  O     . THR A 1 351 ? 5.18836   -12.92964 -11.73228 1.000 5.36991  ? 351 THR A O     1 
ATOM   2761 C  CB    . THR A 1 351 ? 3.40222   -15.47653 -12.69333 1.000 5.78373  ? 351 THR A CB    1 
ATOM   2762 O  OG1   . THR A 1 351 ? 4.23518   -16.39355 -13.41135 1.000 10.50634 ? 351 THR A OG1   1 
ATOM   2763 C  CG2   . THR A 1 351 ? 1.93520   -15.85645 -12.88733 1.000 7.50562  ? 351 THR A CG2   1 
ATOM   2764 N  N     . TRP A 1 352 ? 6.09830   -14.00565 -13.48531 1.000 6.16805  ? 352 TRP A N     1 
ATOM   2765 C  CA    . TRP A 1 352 ? 7.46832   -13.64672 -13.13730 1.000 7.84054  ? 352 TRP A CA    1 
ATOM   2766 C  C     . TRP A 1 352 ? 8.03637   -12.52473 -13.99128 1.000 6.63282  ? 352 TRP A C     1 
ATOM   2767 O  O     . TRP A 1 352 ? 8.93141   -11.80879 -13.53326 1.000 10.96889 ? 352 TRP A O     1 
ATOM   2768 C  CB    . TRP A 1 352 ? 8.39825   -14.85877 -13.26633 1.000 7.38659  ? 352 TRP A CB    1 
ATOM   2769 C  CG    . TRP A 1 352 ? 8.25021   -15.88279 -12.19036 1.000 9.54509  ? 352 TRP A CG    1 
ATOM   2770 C  CD1   . TRP A 1 352 ? 7.21820   -16.00675 -11.30936 1.000 9.01586  ? 352 TRP A CD1   1 
ATOM   2771 C  CD2   . TRP A 1 352 ? 9.17715   -16.92984 -11.87639 1.000 10.70387 ? 352 TRP A CD2   1 
ATOM   2772 N  NE1   . TRP A 1 352 ? 7.44215   -17.06878 -10.47038 1.000 13.58793 ? 352 TRP A NE1   1 
ATOM   2773 C  CE2   . TRP A 1 352 ? 8.63812   -17.65284 -10.79640 1.000 8.29507  ? 352 TRP A CE2   1 
ATOM   2774 C  CE3   . TRP A 1 352 ? 10.41013  -17.32489 -12.40540 1.000 11.27771 ? 352 TRP A CE3   1 
ATOM   2775 C  CZ2   . TRP A 1 352 ? 9.28607   -18.75288 -10.23443 1.000 11.53260 ? 352 TRP A CZ2   1 
ATOM   2776 C  CZ3   . TRP A 1 352 ? 11.05308  -18.41794 -11.84543 1.000 12.67146 ? 352 TRP A CZ3   1 
ATOM   2777 C  CH2   . TRP A 1 352 ? 10.49005  -19.11793 -10.77144 1.000 10.06336 ? 352 TRP A CH2   1 
ATOM   2778 N  N     . GLY A 1 353 ? 7.55437   -12.36168 -15.22127 1.000 5.24701  ? 353 GLY A N     1 
ATOM   2779 C  CA    . GLY A 1 353 ? 8.15642   -11.39869 -16.12225 1.000 6.49579  ? 353 GLY A CA    1 
ATOM   2780 C  C     . GLY A 1 353 ? 9.50539   -11.80474 -16.66527 1.000 6.64786  ? 353 GLY A C     1 
ATOM   2781 O  O     . GLY A 1 353 ? 10.20243  -10.96576 -17.24725 1.000 5.44455  ? 353 GLY A O     1 
ATOM   2782 N  N     . TRP A 1 354 ? 9.89533   -13.06577 -16.48830 1.000 4.28381  ? 354 TRP A N     1 
ATOM   2783 C  CA    . TRP A 1 354 ? 11.18230  -13.56382 -16.94631 1.000 6.97698  ? 354 TRP A CA    1 
ATOM   2784 C  C     . TRP A 1 354 ? 11.04823  -15.04481 -17.25835 1.000 6.71266  ? 354 TRP A C     1 
ATOM   2785 O  O     . TRP A 1 354 ? 10.41419  -15.78879 -16.50336 1.000 6.61487  ? 354 TRP A O     1 
ATOM   2786 C  CB    . TRP A 1 354 ? 12.28432  -13.34890 -15.90031 1.000 5.73389  ? 354 TRP A CB    1 
ATOM   2787 C  CG    . TRP A 1 354 ? 13.63929  -13.80896 -16.35533 1.000 5.42529  ? 354 TRP A CG    1 
ATOM   2788 C  CD1   . TRP A 1 354 ? 14.60433  -13.04799 -16.94732 1.000 4.68798  ? 354 TRP A CD1   1 
ATOM   2789 C  CD2   . TRP A 1 354 ? 14.17723  -15.13499 -16.26236 1.000 6.07262  ? 354 TRP A CD2   1 
ATOM   2790 N  NE1   . TRP A 1 354 ? 15.71229  -13.81504 -17.22534 1.000 4.60201  ? 354 TRP A NE1   1 
ATOM   2791 C  CE2   . TRP A 1 354 ? 15.47323  -15.10004 -16.81437 1.000 6.47565  ? 354 TRP A CE2   1 
ATOM   2792 C  CE3   . TRP A 1 354 ? 13.68917  -16.34698 -15.76439 1.000 8.21446  ? 354 TRP A CE3   1 
ATOM   2793 C  CZ2   . TRP A 1 354 ? 16.28517  -16.23108 -16.88240 1.000 7.97363  ? 354 TRP A CZ2   1 
ATOM   2794 C  CZ3   . TRP A 1 354 ? 14.49611  -17.46702 -15.83542 1.000 6.14209  ? 354 TRP A CZ3   1 
ATOM   2795 C  CH2   . TRP A 1 354 ? 15.77811  -17.40207 -16.38942 1.000 7.19230  ? 354 TRP A CH2   1 
ATOM   2796 N  N     . MET A 1 355 ? 11.64420  -15.45881 -18.37536 1.000 4.57897  ? 355 MET A N     1 
ATOM   2797 C  CA    . MET A 1 355 ? 11.72013  -16.85881 -18.76739 1.000 4.74512  ? 355 MET A CA    1 
ATOM   2798 C  C     . MET A 1 355 ? 13.12111  -17.14586 -19.28541 1.000 6.58170  ? 355 MET A C     1 
ATOM   2799 O  O     . MET A 1 355 ? 13.84916  -16.24189 -19.70439 1.000 6.92768  ? 355 MET A O     1 
ATOM   2800 C  CB    . MET A 1 355 ? 10.69111  -17.22273 -19.84740 1.000 4.47153  ? 355 MET A CB    1 
ATOM   2801 C  CG    . MET A 1 355 ? 9.27013   -16.80866 -19.53238 1.000 6.45773  ? 355 MET A CG    1 
ATOM   2802 S  SD    . MET A 1 355 ? 8.79020   -15.35462 -20.47535 1.000 9.30472  ? 355 MET A SD    1 
ATOM   2803 C  CE    . MET A 1 355 ? 8.76416   -16.03558 -22.13036 1.000 7.46896  ? 355 MET A CE    1 
ATOM   2804 N  N     . HIS A 1 356 ? 13.49005  -18.42188 -19.25344 1.000 6.56627  ? 356 HIS A N     1 
ATOM   2805 C  CA    . HIS A 1 356 ? 14.77403  -18.83594 -19.79445 1.000 5.59354  ? 356 HIS A CA    1 
ATOM   2806 C  C     . HIS A 1 356 ? 14.82003  -18.57290 -21.29645 1.000 5.71127  ? 356 HIS A C     1 
ATOM   2807 O  O     . HIS A 1 356 ? 13.78703  -18.51483 -21.97044 1.000 6.04201  ? 356 HIS A O     1 
ATOM   2808 C  CB    . HIS A 1 356 ? 15.01495  -20.31695 -19.49949 1.000 7.11827  ? 356 HIS A CB    1 
ATOM   2809 C  CG    . HIS A 1 356 ? 16.36193  -20.81201 -19.92651 1.000 7.25101  ? 356 HIS A CG    1 
ATOM   2810 N  ND1   . HIS A 1 356 ? 16.58489  -21.39200 -21.15752 1.000 7.44219  ? 356 HIS A ND1   1 
ATOM   2811 C  CD2   . HIS A 1 356 ? 17.55393  -20.82009 -19.28451 1.000 7.90684  ? 356 HIS A CD2   1 
ATOM   2812 C  CE1   . HIS A 1 356 ? 17.85587  -21.73506 -21.25553 1.000 7.00008  ? 356 HIS A CE1   1 
ATOM   2813 N  NE2   . HIS A 1 356 ? 18.46690  -21.39711 -20.13353 1.000 7.93498  ? 356 HIS A NE2   1 
ATOM   2814 N  N     . HIS A 1 357 ? 16.03904  -18.40995 -21.81745 1.000 6.26411  ? 357 HIS A N     1 
ATOM   2815 C  CA    . HIS A 1 357 ? 16.21405  -18.04493 -23.22144 1.000 7.38850  ? 357 HIS A CA    1 
ATOM   2816 C  C     . HIS A 1 357 ? 15.54800  -19.05087 -24.15446 1.000 7.26638  ? 357 HIS A C     1 
ATOM   2817 O  O     . HIS A 1 357 ? 14.89301  -18.66282 -25.12945 1.000 6.27611  ? 357 HIS A O     1 
ATOM   2818 C  CB    . HIS A 1 357 ? 17.70106  -17.91900 -23.54444 1.000 8.14721  ? 357 HIS A CB    1 
ATOM   2819 C  CG    . HIS A 1 357 ? 17.98307  -17.58498 -24.97644 1.000 8.52061  ? 357 HIS A CG    1 
ATOM   2820 N  ND1   . HIS A 1 357 ? 17.43612  -16.48893 -25.60641 1.000 8.10550  ? 357 HIS A ND1   1 
ATOM   2821 C  CD2   . HIS A 1 357 ? 18.76204  -18.19799 -25.89845 1.000 12.11809 ? 357 HIS A CD2   1 
ATOM   2822 C  CE1   . HIS A 1 357 ? 17.86312  -16.44193 -26.85541 1.000 9.00564  ? 357 HIS A CE1   1 
ATOM   2823 N  NE2   . HIS A 1 357 ? 18.66907  -17.46796 -27.05844 1.000 10.24454 ? 357 HIS A NE2   1 
ATOM   2824 N  N     . LEU A 1 358 ? 15.70293  -20.34489 -23.87849 1.000 6.38522  ? 358 LEU A N     1 
ATOM   2825 C  CA    . LEU A 1 358 ? 15.06488  -21.36083 -24.70751 1.000 7.33608  ? 358 LEU A CA    1 
ATOM   2826 C  C     . LEU A 1 358 ? 13.57387  -21.50577 -24.42751 1.000 6.27555  ? 358 LEU A C     1 
ATOM   2827 O  O     . LEU A 1 358 ? 12.84584  -22.03671 -25.27352 1.000 5.76201  ? 358 LEU A O     1 
ATOM   2828 C  CB    . LEU A 1 358 ? 15.76781  -22.70687 -24.51955 1.000 7.79347  ? 358 LEU A CB    1 
ATOM   2829 C  CG    . LEU A 1 358 ? 17.16781  -22.75893 -25.13256 1.000 9.06659  ? 358 LEU A CG    1 
ATOM   2830 C  CD1   . LEU A 1 358 ? 17.83274  -24.10997 -24.90759 1.000 14.75968 ? 358 LEU A CD1   1 
ATOM   2831 C  CD2   . LEU A 1 358 ? 17.09782  -22.43189 -26.61755 1.000 13.08770 ? 358 LEU A CD2   1 
ATOM   2832 N  N     . ALA A 1 359 ? 13.10190  -21.05977 -23.26350 1.000 5.19083  ? 359 ALA A N     1 
ATOM   2833 C  CA    . ALA A 1 359 ? 11.66190  -21.00470 -23.03949 1.000 5.16817  ? 359 ALA A CA    1 
ATOM   2834 C  C     . ALA A 1 359 ? 11.01795  -19.95165 -23.93446 1.000 5.43419  ? 359 ALA A C     1 
ATOM   2835 O  O     . ALA A 1 359 ? 9.91994   -20.16158 -24.46447 1.000 5.19678  ? 359 ALA A O     1 
ATOM   2836 C  CB    . ALA A 1 359 ? 11.36992  -20.72072 -21.56748 1.000 5.77256  ? 359 ALA A CB    1 
ATOM   2837 N  N     . ARG A 1 360 ? 11.69506  -18.81378 -24.11195 1.000 5.23256  ? 360 ARG A N     1 
ATOM   2838 C  CA    . ARG A 1 360 ? 11.21731  -17.79364 -25.03487 1.000 4.82365  ? 360 ARG A CA    1 
ATOM   2839 C  C     . ARG A 1 360 ? 11.31400  -18.26694 -26.47778 1.000 4.97529  ? 360 ARG A C     1 
ATOM   2840 O  O     . ARG A 1 360 ? 10.48706  -17.87805 -27.30875 1.000 4.45770  ? 360 ARG A O     1 
ATOM   2841 C  CB    . ARG A 1 360 ? 12.00922  -16.49860 -24.84088 1.000 5.73123  ? 360 ARG A CB    1 
ATOM   2842 C  CG    . ARG A 1 360 ? 12.21836  -16.09399 -23.39152 1.000 4.78405  ? 360 ARG A CG    1 
ATOM   2843 C  CD    . ARG A 1 360 ? 12.82595  -14.70062 -23.27269 1.000 6.95698  ? 360 ARG A CD    1 
ATOM   2844 N  NE    . ARG A 1 360 ? 13.24449  -14.43114 -21.90192 1.000 6.84271  ? 360 ARG A NE    1 
ATOM   2845 C  CZ    . ARG A 1 360 ? 13.56917  -13.23843 -21.42314 1.000 4.47629  ? 360 ARG A CZ    1 
ATOM   2846 N  NH1   . ARG A 1 360 ? 13.61161  -12.16666 -22.19659 1.000 5.34068  ? 360 ARG A NH1   1 
ATOM   2847 N  NH2   . ARG A 1 360 ? 13.84341  -13.11509 -20.12911 1.000 4.85223  ? 360 ARG A NH2   1 
ATOM   2848 N  N     . HIS A 1 361 ? 12.31299  -19.10265 -26.78945 1.000 5.66391  ? 361 HIS A N     1 
ATOM   2849 C  CA    . HIS A 1 361 ? 12.40595  -19.70362 -28.11746 1.000 6.10996  ? 361 HIS A CA    1 
ATOM   2850 C  C     . HIS A 1 361 ? 11.16491  -20.53155 -28.43048 1.000 7.66444  ? 361 HIS A C     1 
ATOM   2851 O  O     . HIS A 1 361 ? 10.65690  -20.49850 -29.55948 1.000 7.07415  ? 361 HIS A O     1 
ATOM   2852 C  CB    . HIS A 1 361 ? 13.65791  -20.58168 -28.22149 1.000 8.04294  ? 361 HIS A CB    1 
ATOM   2853 C  CG    . HIS A 1 361 ? 14.87894  -19.86573 -28.71548 1.000 11.28124 ? 361 HIS A CG    1 
ATOM   2854 N  ND1   . HIS A 1 361 ? 15.62091  -20.31474 -29.78849 1.000 11.72102 ? 361 HIS A ND1   1 
ATOM   2855 C  CD2   . HIS A 1 361 ? 15.50000  -18.74777 -28.27245 1.000 10.99797 ? 361 HIS A CD2   1 
ATOM   2856 C  CE1   . HIS A 1 361 ? 16.64095  -19.49979 -29.98848 1.000 9.34361  ? 361 HIS A CE1   1 
ATOM   2857 N  NE2   . HIS A 1 361 ? 16.59001  -18.53981 -29.08345 1.000 11.26293 ? 361 HIS A NE2   1 
ATOM   2858 N  N     . SER A 1 362 ? 10.66487  -21.28155 -27.44249 1.000 7.61991  ? 362 SER A N     1 
ATOM   2859 C  CA    . SER A 1 362 ? 9.51683   -22.15648 -27.66851 1.000 6.44683  ? 362 SER A CA    1 
ATOM   2860 C  C     . SER A 1 362 ? 8.26887   -21.35941 -28.03249 1.000 5.20201  ? 362 SER A C     1 
ATOM   2861 O  O     . SER A 1 362 ? 7.61485   -21.63636 -29.04649 1.000 5.89068  ? 362 SER A O     1 
ATOM   2862 C  CB    . SER A 1 362 ? 9.26379   -23.01850 -26.43153 1.000 6.25716  ? 362 SER A CB    1 
ATOM   2863 O  OG    . SER A 1 362 ? 10.35075  -23.89156 -26.17856 1.000 8.04680  ? 362 SER A OG    1 
ATOM   2864 N  N     . VAL A 1 363 ? 7.91992   -20.36541 -27.21446 1.000 4.81391  ? 363 VAL A N     1 
ATOM   2865 C  CA    . VAL A 1 363 ? 6.68196   -19.62835 -27.44944 1.000 5.06100  ? 363 VAL A CA    1 
ATOM   2866 C  C     . VAL A 1 363 ? 6.81100   -18.66832 -28.63342 1.000 6.25169  ? 363 VAL A C     1 
ATOM   2867 O  O     . VAL A 1 363 ? 5.81701   -18.38026 -29.30941 1.000 6.34501  ? 363 VAL A O     1 
ATOM   2868 C  CB    . VAL A 1 363 ? 6.24900   -18.89335 -26.16842 1.000 6.39673  ? 363 VAL A CB    1 
ATOM   2869 C  CG1   . VAL A 1 363 ? 5.95795   -19.89737 -25.05844 1.000 5.43947  ? 363 VAL A CG1   1 
ATOM   2870 C  CG2   . VAL A 1 363 ? 7.31505   -17.90142 -25.72640 1.000 6.18345  ? 363 VAL A CG2   1 
ATOM   2871 N  N     . ALA A 1 364 ? 8.01403   -18.15938 -28.91441 1.000 5.31398  ? 364 ALA A N     1 
ATOM   2872 C  CA    . ALA A 1 364 ? 8.18106   -17.29136 -30.07639 1.000 6.39935  ? 364 ALA A CA    1 
ATOM   2873 C  C     . ALA A 1 364 ? 8.08602   -18.08632 -31.37041 1.000 7.13743  ? 364 ALA A C     1 
ATOM   2874 O  O     . ALA A 1 364 ? 7.46504   -17.63527 -32.34040 1.000 6.11409  ? 364 ALA A O     1 
ATOM   2875 C  CB    . ALA A 1 364 ? 9.51210   -16.54743 -29.99938 1.000 7.09849  ? 364 ALA A CB    1 
ATOM   2876 N  N     . CYS A 1 365 ? 8.69496   -19.27435 -31.40444 1.000 7.45510  ? 365 CYS A N     1 
ATOM   2877 C  CA    . CYS A 1 365 ? 8.56391   -20.13332 -32.57546 1.000 7.05098  ? 365 CYS A CA    1 
ATOM   2878 C  C     . CYS A 1 365 ? 7.12589   -20.60224 -32.75346 1.000 7.68997  ? 365 CYS A C     1 
ATOM   2879 O  O     . CYS A 1 365 ? 6.62188   -20.65819 -33.88146 1.000 9.88980  ? 365 CYS A O     1 
ATOM   2880 C  CB    . CYS A 1 365 ? 9.50685   -21.32937 -32.45749 1.000 9.85134  ? 365 CYS A CB    1 
ATOM   2881 S  SG    . CYS A 1 365 ? 9.53279   -22.40534 -33.90352 1.000 10.44869 ? 365 CYS A SG    1 
ATOM   2882 N  N     . PHE A 1 366 ? 6.44787   -20.93323 -31.65047 1.000 6.15654  ? 366 PHE A N     1 
ATOM   2883 C  CA    . PHE A 1 366 ? 5.07285   -21.42116 -31.73148 1.000 7.56011  ? 366 PHE A CA    1 
ATOM   2884 C  C     . PHE A 1 366 ? 4.15290   -20.37010 -32.34045 1.000 7.50176  ? 366 PHE A C     1 
ATOM   2885 O  O     . PHE A 1 366 ? 3.31488   -20.67804 -33.19545 1.000 8.46745  ? 366 PHE A O     1 
ATOM   2886 C  CB    . PHE A 1 366 ? 4.58183   -21.82017 -30.33748 1.000 10.21957 ? 366 PHE A CB    1 
ATOM   2887 C  CG    . PHE A 1 366 ? 3.21980   -22.46210 -30.32749 1.000 9.33552  ? 366 PHE A CG    1 
ATOM   2888 C  CD1   . PHE A 1 366 ? 3.08673   -23.83309 -30.47653 1.000 7.68002  ? 366 PHE A CD1   1 
ATOM   2889 C  CD2   . PHE A 1 366 ? 2.07484   -21.69805 -30.15847 1.000 9.28664  ? 366 PHE A CD2   1 
ATOM   2890 C  CE1   . PHE A 1 366 ? 1.83870   -24.43203 -30.46453 1.000 10.44798 ? 366 PHE A CE1   1 
ATOM   2891 C  CE2   . PHE A 1 366 ? 0.81981   -22.29199 -30.14548 1.000 7.36256  ? 366 PHE A CE2   1 
ATOM   2892 C  CZ    . PHE A 1 366 ? 0.70374   -23.65998 -30.29851 1.000 10.46361 ? 366 PHE A CZ    1 
ATOM   2893 N  N     . LEU A 1 367 ? 4.29896   -19.11812 -31.90742 1.000 7.45072  ? 367 LEU A N     1 
ATOM   2894 C  CA    . LEU A 1 367 ? 3.43502   -18.05206 -32.40139 1.000 9.11177  ? 367 LEU A CA    1 
ATOM   2895 C  C     . LEU A 1 367 ? 3.74503   -17.71005 -33.85438 1.000 10.54266 ? 367 LEU A C     1 
ATOM   2896 O  O     . LEU A 1 367 ? 2.82803   -17.54698 -34.66638 1.000 8.33281  ? 367 LEU A O     1 
ATOM   2897 C  CB    . LEU A 1 367 ? 3.58308   -16.81209 -31.51936 1.000 7.50289  ? 367 LEU A CB    1 
ATOM   2898 C  CG    . LEU A 1 367 ? 2.91415   -15.54305 -32.04233 1.000 6.95430  ? 367 LEU A CG    1 
ATOM   2899 C  CD1   . LEU A 1 367 ? 1.41814   -15.56998 -31.77132 1.000 11.73097 ? 367 LEU A CD1   1 
ATOM   2900 C  CD2   . LEU A 1 367 ? 3.55821   -14.31109 -31.43630 1.000 9.41803  ? 367 LEU A CD2   1 
ATOM   2901 N  N     . THR A 1 368 ? 5.02703   -17.60610 -34.20239 1.000 9.59825  ? 368 THR A N     1 
ATOM   2902 C  CA    . THR A 1 368 ? 5.40805   -17.10009 -35.51638 1.000 12.72469 ? 368 THR A CA    1 
ATOM   2903 C  C     . THR A 1 368 ? 5.56399   -18.21907 -36.53940 1.000 10.73900 ? 368 THR A C     1 
ATOM   2904 O  O     . THR A 1 368 ? 4.58296   -18.88002 -36.89641 1.000 10.64824 ? 368 THR A O     1 
ATOM   2905 C  CB    . THR A 1 368 ? 6.70209   -16.28716 -35.42136 1.000 10.14876 ? 368 THR A CB    1 
ATOM   2906 O  OG1   . THR A 1 368 ? 7.78405   -17.14622 -35.04139 1.000 6.57629  ? 368 THR A OG1   1 
ATOM   2907 C  CG2   . THR A 1 368 ? 6.56015   -15.17418 -34.39633 1.000 9.25756  ? 368 THR A CG2   1 
ATOM   2908 N  N     . ARG A 1 369 ? 6.79910   -18.49722 -36.95108 1.000 9.56861  ? 369 ARG A N     1 
ATOM   2909 C  CA    . ARG A 1 369 ? 7.09130   -19.39944 -38.06082 1.000 9.54596  ? 369 ARG A CA    1 
ATOM   2910 C  C     . ARG A 1 369 ? 6.87377   -20.88125 -37.74010 1.000 13.93730 ? 369 ARG A C     1 
ATOM   2911 O  O     . ARG A 1 369 ? 7.16647   -21.71912 -38.59945 1.000 17.42700 ? 369 ARG A O     1 
ATOM   2912 C  CB    . ARG A 1 369 ? 8.53736   -19.19837 -38.52087 1.000 13.03267 ? 369 ARG A CB    1 
ATOM   2913 C  CG    . ARG A 1 369 ? 9.54390   -19.63006 -37.47124 1.000 7.83562  ? 369 ARG A CG    1 
ATOM   2914 C  CD    . ARG A 1 369 ? 10.96344  -19.60713 -37.99607 1.000 10.84555 ? 369 ARG A CD    1 
ATOM   2915 N  NE    . ARG A 1 369 ? 11.90596  -20.00174 -36.95733 1.000 12.41499 ? 369 ARG A NE    1 
ATOM   2916 C  CZ    . ARG A 1 369 ? 12.20573  -21.25827 -36.65862 1.000 11.78940 ? 369 ARG A CZ    1 
ATOM   2917 N  NH1   . ARG A 1 369 ? 11.65433  -22.27303 -37.30419 1.000 11.09853 ? 369 ARG A NH1   1 
ATOM   2918 N  NH2   . ARG A 1 369 ? 13.07770  -21.50326 -35.68520 1.000 17.88292 ? 369 ARG A NH2   1 
ATOM   2919 N  N     . GLY A 1 370 ? 6.38584   -21.24212 -36.55548 1.000 10.17146 ? 370 GLY A N     1 
ATOM   2920 C  CA    . GLY A 1 370 ? 6.29077   -22.65312 -36.24051 1.000 11.70310 ? 370 GLY A CA    1 
ATOM   2921 C  C     . GLY A 1 370 ? 4.90074   -23.25005 -36.32752 1.000 12.41909 ? 370 GLY A C     1 
ATOM   2922 O  O     . GLY A 1 370 ? 4.73368   -24.36903 -36.82554 1.000 13.35864 ? 370 GLY A O     1 
ATOM   2923 N  N     . ASP A 1 371 ? 3.89078   -22.52701 -35.84350 1.000 11.06613 ? 371 ASP A N     1 
ATOM   2924 C  CA    . ASP A 1 371 ? 2.55275   -23.10294 -35.76551 1.000 10.34213 ? 371 ASP A CA    1 
ATOM   2925 C  C     . ASP A 1 371 ? 1.45180   -22.12888 -36.17148 1.000 10.44869 ? 371 ASP A C     1 
ATOM   2926 O  O     . ASP A 1 371 ? 0.63078   -22.44981 -37.03748 1.000 13.34626 ? 371 ASP A O     1 
ATOM   2927 C  CB    . ASP A 1 371 ? 2.28973   -23.62396 -34.34952 1.000 9.58377  ? 371 ASP A CB    1 
ATOM   2928 C  CG    . ASP A 1 371 ? 3.21567   -24.76202 -33.96755 1.000 11.07020 ? 371 ASP A CG    1 
ATOM   2929 O  OD1   . ASP A 1 371 ? 4.40169   -24.49508 -33.66955 1.000 7.48244  ? 371 ASP A OD1   1 
ATOM   2930 O  OD2   . ASP A 1 371 ? 2.75561   -25.92299 -33.96057 1.000 11.49168 ? 371 ASP A OD2   1 
ATOM   2931 N  N     . LEU A 1 372 ? 1.41886   -20.94389 -35.55745 1.000 14.02033 ? 372 LEU A N     1 
ATOM   2932 C  CA    . LEU A 1 372 ? 0.29090   -20.02883 -35.71442 1.000 10.46088 ? 372 LEU A CA    1 
ATOM   2933 C  C     . LEU A 1 372 ? 0.47495   -19.00681 -36.82940 1.000 12.20418 ? 372 LEU A C     1 
ATOM   2934 O  O     . LEU A 1 372 ? -0.52603  -18.50275 -37.35339 1.000 13.51216 ? 372 LEU A O     1 
ATOM   2935 C  CB    . LEU A 1 372 ? 0.02095   -19.29884 -34.39541 1.000 9.86658  ? 372 LEU A CB    1 
ATOM   2936 C  CG    . LEU A 1 372 ? -0.28109  -20.19086 -33.19143 1.000 12.83887 ? 372 LEU A CG    1 
ATOM   2937 C  CD1   . LEU A 1 372 ? -0.63805  -19.36287 -31.96040 1.000 10.50719 ? 372 LEU A CD1   1 
ATOM   2938 C  CD2   . LEU A 1 372 ? -1.39715  -21.17379 -33.52144 1.000 13.57771 ? 372 LEU A CD2   1 
ATOM   2939 N  N     . TYR A 1 373 ? 1.71797   -18.67986 -37.18540 1.000 10.50692 ? 373 TYR A N     1 
ATOM   2940 C  CA    . TYR A 1 373 ? 2.02101   -17.78185 -38.30238 1.000 11.32512 ? 373 TYR A CA    1 
ATOM   2941 C  C     . TYR A 1 373 ? 1.45408   -16.38283 -38.07134 1.000 12.96523 ? 373 TYR A C     1 
ATOM   2942 O  O     . TYR A 1 373 ? 0.94411   -15.73678 -38.99133 1.000 14.69885 ? 373 TYR A O     1 
ATOM   2943 C  CB    . TYR A 1 373 ? 1.52897   -18.35680 -39.63239 1.000 15.37253 ? 373 TYR A CB    1 
ATOM   2944 C  CG    . TYR A 1 373 ? 2.49998   -18.15382 -40.77139 1.000 19.14825 ? 373 TYR A CG    1 
ATOM   2945 C  CD1   . TYR A 1 373 ? 3.57493   -19.01387 -40.95041 1.000 15.92725 ? 373 TYR A CD1   1 
ATOM   2946 C  CD2   . TYR A 1 373 ? 2.34603   -17.10079 -41.66536 1.000 20.31614 ? 373 TYR A CD2   1 
ATOM   2947 C  CE1   . TYR A 1 373 ? 4.46794   -18.83389 -41.98841 1.000 19.79550 ? 373 TYR A CE1   1 
ATOM   2948 C  CE2   . TYR A 1 373 ? 3.23703   -16.91481 -42.70736 1.000 22.05730 ? 373 TYR A CE2   1 
ATOM   2949 C  CZ    . TYR A 1 373 ? 4.29499   -17.78386 -42.86339 1.000 21.16098 ? 373 TYR A CZ    1 
ATOM   2950 O  OH    . TYR A 1 373 ? 5.18099   -17.60288 -43.89739 1.000 27.54526 ? 373 TYR A OH    1 
ATOM   2951 N  N     . VAL A 1 374 ? 1.55711   -15.90786 -36.83733 1.000 9.07958  ? 374 VAL A N     1 
ATOM   2952 C  CA    . VAL A 1 374 ? 1.20818   -14.53686 -36.48930 1.000 11.84042 ? 374 VAL A CA    1 
ATOM   2953 C  C     . VAL A 1 374 ? 2.48622   -13.70792 -36.47728 1.000 13.29315 ? 374 VAL A C     1 
ATOM   2954 O  O     . VAL A 1 374 ? 3.56720   -14.20098 -36.13430 1.000 8.66722  ? 374 VAL A O     1 
ATOM   2955 C  CB    . VAL A 1 374 ? 0.47119   -14.47985 -35.13229 1.000 12.87246 ? 374 VAL A CB    1 
ATOM   2956 C  CG1   . VAL A 1 374 ? 0.18926   -13.04185 -34.70826 1.000 16.60151 ? 374 VAL A CG1   1 
ATOM   2957 C  CG2   . VAL A 1 374 ? -0.82585  -15.27278 -35.20631 1.000 10.17363 ? 374 VAL A CG2   1 
ATOM   2958 N  N     . SER A 1 375 ? 2.36228   -12.44190 -36.87425 1.000 13.04424 ? 375 SER A N     1 
ATOM   2959 C  CA    . SER A 1 375 ? 3.51633   -11.55396 -36.95424 1.000 12.36103 ? 375 SER A CA    1 
ATOM   2960 C  C     . SER A 1 375 ? 4.23834   -11.46603 -35.61624 1.000 11.01065 ? 375 SER A C     1 
ATOM   2961 O  O     . SER A 1 375 ? 3.61235   -11.39802 -34.55523 1.000 8.66272  ? 375 SER A O     1 
ATOM   2962 C  CB    . SER A 1 375 ? 3.07640   -10.15893 -37.40220 1.000 12.19586 ? 375 SER A CB    1 
ATOM   2963 O  OG    . SER A 1 375 ? 4.17144   -9.25898  -37.42719 1.000 12.60673 ? 375 SER A OG    1 
ATOM   2964 N  N     . TRP A 1 376 ? 5.57334   -11.46110 -35.67824 1.000 10.88191 ? 376 TRP A N     1 
ATOM   2965 C  CA    . TRP A 1 376 ? 6.38435   -11.30316 -34.47824 1.000 9.31648  ? 376 TRP A CA    1 
ATOM   2966 C  C     . TRP A 1 376 ? 6.17242   -9.94817  -33.81221 1.000 8.35184  ? 376 TRP A C     1 
ATOM   2967 O  O     . TRP A 1 376 ? 6.47443   -9.79921  -32.62221 1.000 9.87181  ? 376 TRP A O     1 
ATOM   2968 C  CB    . TRP A 1 376 ? 7.86434   -11.49823 -34.82125 1.000 10.79840 ? 376 TRP A CB    1 
ATOM   2969 C  CG    . TRP A 1 376 ? 8.37338   -10.54623 -35.86423 1.000 8.05085  ? 376 TRP A CG    1 
ATOM   2970 C  CD1   . TRP A 1 376 ? 8.42537   -10.75520 -37.21324 1.000 9.25336  ? 376 TRP A CD1   1 
ATOM   2971 C  CD2   . TRP A 1 376 ? 8.90145   -9.23326  -35.64220 1.000 9.42054  ? 376 TRP A CD2   1 
ATOM   2972 N  NE1   . TRP A 1 376 ? 8.95242   -9.65422  -37.84321 1.000 10.85229 ? 376 TRP A NE1   1 
ATOM   2973 C  CE2   . TRP A 1 376 ? 9.25347   -8.70625  -36.90119 1.000 11.62340 ? 376 TRP A CE2   1 
ATOM   2974 C  CE3   . TRP A 1 376 ? 9.11149   -8.45230  -34.50119 1.000 10.55820 ? 376 TRP A CE3   1 
ATOM   2975 C  CZ2   . TRP A 1 376 ? 9.80154   -7.43428  -37.04816 1.000 10.71148 ? 376 TRP A CZ2   1 
ATOM   2976 C  CZ3   . TRP A 1 376 ? 9.65556   -7.19133  -34.65116 1.000 10.75701 ? 376 TRP A CZ3   1 
ATOM   2977 C  CH2   . TRP A 1 376 ? 9.99458   -6.69431  -35.91415 1.000 9.09042  ? 376 TRP A CH2   1 
ATOM   2978 N  N     . GLU A 1 377 ? 5.67047   -8.95713  -34.55118 1.000 9.55843  ? 377 GLU A N     1 
ATOM   2979 C  CA    . GLU A 1 377 ? 5.32554   -7.68112  -33.93515 1.000 11.51405 ? 377 GLU A CA    1 
ATOM   2980 C  C     . GLU A 1 377 ? 4.23253   -7.85309  -32.88915 1.000 10.18291 ? 377 GLU A C     1 
ATOM   2981 O  O     . GLU A 1 377 ? 4.25857   -7.19812  -31.84114 1.000 12.34694 ? 377 GLU A O     1 
ATOM   2982 C  CB    . GLU A 1 377 ? 4.88858   -6.68808  -35.01013 1.000 12.23584 ? 377 GLU A CB    1 
ATOM   2983 C  CG    . GLU A 1 377 ? 6.00760   -6.21011  -35.91312 1.000 11.39836 ? 377 GLU A CG    1 
ATOM   2984 C  CD    . GLU A 1 377 ? 5.48963   -5.51206  -37.15410 1.000 18.77418 ? 377 GLU A CD    1 
ATOM   2985 O  OE1   . GLU A 1 377 ? 4.60160   -6.06900  -37.83411 1.000 26.85982 ? 377 GLU A OE1   1 
ATOM   2986 O  OE2   . GLU A 1 377 ? 5.96269   -4.39907  -37.44608 1.000 21.29192 ? 377 GLU A OE2   1 
ATOM   2987 N  N     . ARG A 1 378 ? 3.26300   -8.73294  -33.15468 1.000 11.43358 ? 378 ARG A N     1 
ATOM   2988 C  CA    . ARG A 1 378 ? 2.20711   -8.98305  -32.17872 1.000 12.99635 ? 378 ARG A CA    1 
ATOM   2989 C  C     . ARG A 1 378 ? 2.76522   -9.63319  -30.91862 1.000 9.39020  ? 378 ARG A C     1 
ATOM   2990 O  O     . ARG A 1 378 ? 2.36713   -9.28023  -29.80225 1.000 11.78508 ? 378 ARG A O     1 
ATOM   2991 C  CB    . ARG A 1 378 ? 1.11316   -9.85764  -32.79397 1.000 13.87262 ? 378 ARG A CB    1 
ATOM   2992 C  CG    . ARG A 1 378 ? 0.38199   -9.24138  -33.97612 1.000 13.68131 ? 378 ARG A CG    1 
ATOM   2993 C  CD    . ARG A 1 378 ? -0.41340  -8.00957  -33.57514 1.000 16.17314 ? 378 ARG A CD    1 
ATOM   2994 N  NE    . ARG A 1 378 ? 0.37994   -6.79128  -33.66686 1.000 12.92651 ? 378 ARG A NE    1 
ATOM   2995 C  CZ    . ARG A 1 378 ? 0.53096   -6.08149  -34.77576 1.000 17.35771 ? 378 ARG A CZ    1 
ATOM   2996 N  NH1   . ARG A 1 378 ? -0.04501  -6.44195  -35.91115 1.000 19.46873 ? 378 ARG A NH1   1 
ATOM   2997 N  NH2   . ARG A 1 378 ? 1.27962   -4.98347  -34.74519 1.000 18.95580 ? 378 ARG A NH2   1 
ATOM   2998 N  N     . GLY A 1 379 ? 3.68440   -10.58711 -31.07821 1.000 8.03668  ? 379 GLY A N     1 
ATOM   2999 C  CA    . GLY A 1 379 ? 4.30837   -11.19717 -29.91723 1.000 9.47738  ? 379 GLY A CA    1 
ATOM   3000 C  C     . GLY A 1 379 ? 5.23542   -10.24523 -29.18721 1.000 9.58335  ? 379 GLY A C     1 
ATOM   3001 O  O     . GLY A 1 379 ? 5.31243   -10.26326 -27.95521 1.000 8.26911  ? 379 GLY A O     1 
ATOM   3002 N  N     . MET A 1 380 ? 5.95546   -9.40425  -29.93520 1.000 9.47911  ? 380 MET A N     1 
ATOM   3003 C  CA    . MET A 1 380 ? 6.81952   -8.41631  -29.29918 1.000 9.59071  ? 380 MET A CA    1 
ATOM   3004 C  C     . MET A 1 380 ? 6.01057   -7.45129  -28.44415 1.000 7.63092  ? 380 MET A C     1 
ATOM   3005 O  O     . MET A 1 380 ? 6.47760   -7.00034  -27.39214 1.000 7.12456  ? 380 MET A O     1 
ATOM   3006 C  CB    . MET A 1 380 ? 7.61955   -7.65832  -30.35516 1.000 9.89890  ? 380 MET A CB    1 
ATOM   3007 C  CG    . MET A 1 380 ? 8.68960   -6.75639  -29.78314 1.000 11.20595 ? 380 MET A CG    1 
ATOM   3008 S  SD    . MET A 1 380 ? 9.49464   -5.77140  -31.05212 1.000 18.03078 ? 380 MET A SD    1 
ATOM   3009 C  CE    . MET A 1 380 ? 8.14670   -4.70032  -31.53109 1.000 10.83575 ? 380 MET A CE    1 
ATOM   3010 N  N     . GLU A 1 381 ? 4.78958   -7.12722  -28.87614 1.000 10.34066 ? 381 GLU A N     1 
ATOM   3011 C  CA    . GLU A 1 381 ? 3.92263   -6.27419  -28.06911 1.000 9.14546  ? 381 GLU A CA    1 
ATOM   3012 C  C     . GLU A 1 381 ? 3.54460   -6.95120  -26.75513 1.000 7.55210  ? 381 GLU A C     1 
ATOM   3013 O  O     . GLU A 1 381 ? 3.40764   -6.28522  -25.72311 1.000 9.13379  ? 381 GLU A O     1 
ATOM   3014 C  CB    . GLU A 1 381 ? 2.66565   -5.90211  -28.85910 1.000 8.88352  ? 381 GLU A CB    1 
ATOM   3015 C  CG    . GLU A 1 381 ? 2.91769   -4.98209  -30.04408 1.000 9.59247  ? 381 GLU A CG    1 
ATOM   3016 C  CD    . GLU A 1 381 ? 1.73469   -4.90901  -30.99407 1.000 13.02794 ? 381 GLU A CD    1 
ATOM   3017 O  OE1   . GLU A 1 381 ? 0.66566   -5.47297  -30.67308 1.000 14.51590 ? 381 GLU A OE1   1 
ATOM   3018 O  OE2   . GLU A 1 381 ? 1.87771   -4.28899  -32.06906 1.000 16.99529 ? 381 GLU A OE2   1 
ATOM   3019 N  N     . VAL A 1 382 ? 3.37053   -8.27419  -26.77316 1.000 5.88966  ? 382 VAL A N     1 
ATOM   3020 C  CA    . VAL A 1 382 ? 2.98550   -8.98620  -25.55917 1.000 9.52024  ? 382 VAL A CA    1 
ATOM   3021 C  C     . VAL A 1 382 ? 4.17050   -9.10929  -24.60818 1.000 9.38081  ? 382 VAL A C     1 
ATOM   3022 O  O     . VAL A 1 382 ? 4.02651   -8.95531  -23.38918 1.000 6.07745  ? 382 VAL A O     1 
ATOM   3023 C  CB    . VAL A 1 382 ? 2.39743   -10.36317 -25.91520 1.000 9.95727  ? 382 VAL A CB    1 
ATOM   3024 C  CG1   . VAL A 1 382 ? 2.16839   -11.18518 -24.66022 1.000 10.39514 ? 382 VAL A CG1   1 
ATOM   3025 C  CG2   . VAL A 1 382 ? 1.09944   -10.19608 -26.68820 1.000 7.06632  ? 382 VAL A CG2   1 
ATOM   3026 N  N     . PHE A 1 383 ? 5.36048   -9.38833  -25.14519 1.000 9.99281  ? 383 PHE A N     1 
ATOM   3027 C  CA    . PHE A 1 383 ? 6.53948   -9.48441  -24.29120 1.000 8.83005  ? 383 PHE A CA    1 
ATOM   3028 C  C     . PHE A 1 383 ? 6.88355   -8.13745  -23.66717 1.000 8.63602  ? 383 PHE A C     1 
ATOM   3029 O  O     . PHE A 1 383 ? 7.22656   -8.06749  -22.48317 1.000 9.85801  ? 383 PHE A O     1 
ATOM   3030 C  CB    . PHE A 1 383 ? 7.72945   -10.01545 -25.08822 1.000 10.82040 ? 383 PHE A CB    1 
ATOM   3031 C  CG    . PHE A 1 383 ? 7.81438   -11.51246 -25.13025 1.000 8.69503  ? 383 PHE A CG    1 
ATOM   3032 C  CD1   . PHE A 1 383 ? 6.73334   -12.29141 -24.76327 1.000 8.24323  ? 383 PHE A CD1   1 
ATOM   3033 C  CD2   . PHE A 1 383 ? 8.98734   -12.13951 -25.51827 1.000 10.93868 ? 383 PHE A CD2   1 
ATOM   3034 C  CE1   . PHE A 1 383 ? 6.81727   -13.66842 -24.80030 1.000 9.30370  ? 383 PHE A CE1   1 
ATOM   3035 C  CE2   . PHE A 1 383 ? 9.07827   -13.51851 -25.55331 1.000 8.36098  ? 383 PHE A CE2   1 
ATOM   3036 C  CZ    . PHE A 1 383 ? 7.99124   -14.28247 -25.19232 1.000 6.54097  ? 383 PHE A CZ    1 
ATOM   3037 N  N     . GLU A 1 384 ? 6.80460   -7.05742  -24.44914 1.000 9.79912  ? 384 GLU A N     1 
ATOM   3038 C  CA    . GLU A 1 384 ? 7.15267   -5.73045  -23.94611 1.000 9.67327  ? 384 GLU A CA    1 
ATOM   3039 C  C     . GLU A 1 384 ? 6.28370   -5.33144  -22.76610 1.000 13.20111 ? 384 GLU A C     1 
ATOM   3040 O  O     . GLU A 1 384 ? 6.71374   -4.55248  -21.90808 1.000 12.88149 ? 384 GLU A O     1 
ATOM   3041 C  CB    . GLU A 1 384 ? 7.01300   -4.72800  -25.08500 1.000 12.31190 ? 384 GLU A CB    1 
ATOM   3042 C  CG    . GLU A 1 384 ? 7.03400   -3.25300  -24.78400 1.000 15.68349 ? 384 GLU A CG    1 
ATOM   3043 C  CD    . GLU A 1 384 ? 7.06300   -2.40100  -26.03600 1.000 18.47097 ? 384 GLU A CD    1 
ATOM   3044 O  OE1   . GLU A 1 384 ? 6.89800   -2.95400  -27.13600 1.000 24.13622 ? 384 GLU A OE1   1 
ATOM   3045 O  OE2   . GLU A 1 384 ? 7.25400   -1.19200  -25.90300 1.000 22.29732 ? 384 GLU A OE2   1 
ATOM   3046 N  N     . GLU A 1 385 ? 5.06067   -5.85638  -22.71111 1.000 10.76349 ? 385 GLU A N     1 
ATOM   3047 C  CA    . GLU A 1 385 ? 4.13369   -5.53735  -21.63610 1.000 10.54599 ? 385 GLU A CA    1 
ATOM   3048 C  C     . GLU A 1 385 ? 4.49566   -6.25140  -20.33712 1.000 9.84211  ? 385 GLU A C     1 
ATOM   3049 O  O     . GLU A 1 385 ? 4.45270   -5.64243  -19.26410 1.000 9.66755  ? 385 GLU A O     1 
ATOM   3050 C  CB    . GLU A 1 385 ? 2.71767   -5.90027  -22.07510 1.000 9.00718  ? 385 GLU A CB    1 
ATOM   3051 C  CG    . GLU A 1 385 ? 1.66468   -5.74424  -21.00809 1.000 13.16665 ? 385 GLU A CG    1 
ATOM   3052 C  CD    . GLU A 1 385 ? 0.29266   -6.10716  -21.52510 1.000 14.71905 ? 385 GLU A CD    1 
ATOM   3053 O  OE1   . GLU A 1 385 ? 0.18464   -6.52213  -22.69911 1.000 21.09766 ? 385 GLU A OE1   1 
ATOM   3054 O  OE2   . GLU A 1 385 ? -0.67633  -5.97713  -20.75409 1.000 18.93608 ? 385 GLU A OE2   1 
ATOM   3055 N  N     . HIS A 1 386 ? 4.85960   -7.53342  -20.41015 1.000 9.56995  ? 386 HIS A N     1 
ATOM   3056 C  CA    . HIS A 1 386 ? 5.03556   -8.34646  -19.21317 1.000 9.52812  ? 386 HIS A CA    1 
ATOM   3057 C  C     . HIS A 1 386 ? 6.48855   -8.56854  -18.81818 1.000 8.00798  ? 386 HIS A C     1 
ATOM   3058 O  O     . HIS A 1 386 ? 6.75254   -8.85058  -17.64519 1.000 7.84920  ? 386 HIS A O     1 
ATOM   3059 C  CB    . HIS A 1 386 ? 4.36949   -9.71542  -19.39520 1.000 7.08455  ? 386 HIS A CB    1 
ATOM   3060 C  CG    . HIS A 1 386 ? 2.88049   -9.65134  -19.53319 1.000 10.12068 ? 386 HIS A CG    1 
ATOM   3061 N  ND1   . HIS A 1 386 ? 2.04951   -9.31232  -18.48718 1.000 9.21375  ? 386 HIS A ND1   1 
ATOM   3062 C  CD2   . HIS A 1 386 ? 2.07248   -9.89327  -20.59219 1.000 10.82114 ? 386 HIS A CD2   1 
ATOM   3063 C  CE1   . HIS A 1 386 ? 0.79351   -9.34325  -18.89717 1.000 9.47841  ? 386 HIS A CE1   1 
ATOM   3064 N  NE2   . HIS A 1 386 ? 0.78049   -9.69322  -20.17118 1.000 10.21930 ? 386 HIS A NE2   1 
ATOM   3065 N  N     . LEU A 1 387 ? 7.42855   -8.45357  -19.75118 1.000 9.05505  ? 387 LEU A N     1 
ATOM   3066 C  CA    . LEU A 1 387 ? 8.82254   -8.78464  -19.47219 1.000 6.58449  ? 387 LEU A CA    1 
ATOM   3067 C  C     . LEU A 1 387 ? 9.45959   -7.72670  -18.57317 1.000 7.87638  ? 387 LEU A C     1 
ATOM   3068 O  O     . LEU A 1 387 ? 9.47465   -6.53769  -18.91414 1.000 9.25837  ? 387 LEU A O     1 
ATOM   3069 C  CB    . LEU A 1 387 ? 9.58653   -8.91065  -20.78720 1.000 7.30435  ? 387 LEU A CB    1 
ATOM   3070 C  CG    . LEU A 1 387 ? 10.52246  -10.09169 -21.03023 1.000 9.90788  ? 387 LEU A CG    1 
ATOM   3071 C  CD1   . LEU A 1 387 ? 9.82240   -11.41666 -20.86626 1.000 9.86207  ? 387 LEU A CD1   1 
ATOM   3072 C  CD2   . LEU A 1 387 ? 11.12946  -9.98269  -22.41923 1.000 9.88139  ? 387 LEU A CD2   1 
ATOM   3073 N  N     . ILE A 1 388 ? 9.99258   -8.15175  -17.42418 1.000 6.70697  ? 388 ILE A N     1 
ATOM   3074 C  CA    . ILE A 1 388 ? 10.67563  -7.21681  -16.53716 1.000 6.58303  ? 388 ILE A CA    1 
ATOM   3075 C  C     . ILE A 1 388 ? 12.03265  -6.78986  -17.07116 1.000 6.93514  ? 388 ILE A C     1 
ATOM   3076 O  O     . ILE A 1 388 ? 12.61570  -5.82890  -16.55414 1.000 7.16487  ? 388 ILE A O     1 
ATOM   3077 C  CB    . ILE A 1 388 ? 10.86760  -7.80685  -15.12618 1.000 6.35861  ? 388 ILE A CB    1 
ATOM   3078 C  CG1   . ILE A 1 388 ? 11.78254  -9.03189  -15.17921 1.000 5.35335  ? 388 ILE A CG1   1 
ATOM   3079 C  CG2   . ILE A 1 388 ? 9.51859   -8.12780  -14.49018 1.000 7.68743  ? 388 ILE A CG2   1 
ATOM   3080 C  CD1   . ILE A 1 388 ? 12.23852  -9.51595  -13.81622 1.000 10.54787 ? 388 ILE A CD1   1 
ATOM   3081 N  N     . ASP A 1 389 ? 12.55961  -7.48386  -18.08018 1.000 7.44770  ? 389 ASP A N     1 
ATOM   3082 C  CA    . ASP A 1 389 ? 13.81762  -7.11091  -18.71217 1.000 5.54965  ? 389 ASP A CA    1 
ATOM   3083 C  C     . ASP A 1 389 ? 13.61564  -6.65287  -20.15316 1.000 6.42977  ? 389 ASP A C     1 
ATOM   3084 O  O     . ASP A 1 389 ? 14.51763  -6.79689  -20.98117 1.000 5.06755  ? 389 ASP A O     1 
ATOM   3085 C  CB    . ASP A 1 389 ? 14.81657  -8.26996  -18.65120 1.000 5.18609  ? 389 ASP A CB    1 
ATOM   3086 C  CG    . ASP A 1 389 ? 14.31450  -9.53292  -19.34123 1.000 5.93192  ? 389 ASP A CG    1 
ATOM   3087 O  OD1   . ASP A 1 389 ? 13.31550  -9.46686  -20.08223 1.000 8.96230  ? 389 ASP A OD1   1 
ATOM   3088 O  OD2   . ASP A 1 389 ? 14.92045  -10.60496 -19.14126 1.000 4.46346  ? 389 ASP A OD2   1 
ATOM   3089 N  N     . GLN A 1 390 ? 12.43667  -6.11580  -20.46914 1.000 7.69024  ? 390 GLN A N     1 
ATOM   3090 C  CA    . GLN A 1 390 ? 12.14768  -5.73775  -21.84613 1.000 9.23721  ? 390 GLN A CA    1 
ATOM   3091 C  C     . GLN A 1 390 ? 13.13973  -4.67779  -22.30611 1.000 9.30380  ? 390 GLN A C     1 
ATOM   3092 O  O     . GLN A 1 390 ? 13.26979  -3.61781  -21.68909 1.000 10.34237 ? 390 GLN A O     1 
ATOM   3093 C  CB    . GLN A 1 390 ? 10.69471  -5.25668  -21.99012 1.000 11.01591 ? 390 GLN A CB    1 
ATOM   3094 C  CG    . GLN A 1 390 ? 10.35378  -3.89267  -21.40808 1.000 13.60347 ? 390 GLN A CG    1 
ATOM   3095 C  CD    . GLN A 1 390 ? 10.53083  -2.76166  -22.40806 1.000 15.07424 ? 390 GLN A CD    1 
ATOM   3096 O  OE1   . GLN A 1 390 ? 10.40382  -2.95662  -23.61806 1.000 18.61828 ? 390 GLN A OE1   1 
ATOM   3097 N  NE2   . GLN A 1 390 ? 10.83189  -1.57069  -21.90303 1.000 9.26281  ? 390 GLN A NE2   1 
ATOM   3098 N  N     . ASP A 1 391 ? 13.89071  -4.99781  -23.35312 1.000 9.89997  ? 391 ASP A N     1 
ATOM   3099 C  CA    . ASP A 1 391 ? 14.87076  -4.08684  -23.92611 1.000 10.40270 ? 391 ASP A CA    1 
ATOM   3100 C  C     . ASP A 1 391 ? 14.49976  -3.86379  -25.38310 1.000 10.69888 ? 391 ASP A C     1 
ATOM   3101 O  O     . ASP A 1 391 ? 14.36171  -4.82777  -26.14312 1.000 7.69121  ? 391 ASP A O     1 
ATOM   3102 C  CB    . ASP A 1 391 ? 16.28773  -4.64692  -23.78812 1.000 8.32966  ? 391 ASP A CB    1 
ATOM   3103 C  CG    . ASP A 1 391 ? 17.35478  -3.61796  -24.09110 1.000 11.23608 ? 391 ASP A CG    1 
ATOM   3104 O  OD1   . ASP A 1 391 ? 17.34880  -3.06194  -25.21009 1.000 11.09014 ? 391 ASP A OD1   1 
ATOM   3105 O  OD2   . ASP A 1 391 ? 18.19280  -3.36003  -23.20210 1.000 11.22269 ? 391 ASP A OD2   1 
ATOM   3106 N  N     . HIS A 1 392 ? 14.32483  -2.59277  -25.75707 1.000 11.45737 ? 392 HIS A N     1 
ATOM   3107 C  CA    . HIS A 1 392 ? 13.86484  -2.21972  -27.09106 1.000 13.10380 ? 392 HIS A CA    1 
ATOM   3108 C  C     . HIS A 1 392 ? 14.60080  -2.97973  -28.19008 1.000 10.92134 ? 392 HIS A C     1 
ATOM   3109 O  O     . HIS A 1 392 ? 13.97900  -3.63300  -29.03800 1.000 11.39367 ? 392 HIS A O     1 
ATOM   3110 C  CB    . HIS A 1 392 ? 14.02300  -0.70600  -27.27100 1.000 14.39719 ? 392 HIS A CB    1 
ATOM   3111 C  CG    . HIS A 1 392 ? 13.44100  -0.18000  -28.54600 1.000 14.82418 ? 392 HIS A CG    1 
ATOM   3112 N  ND1   . HIS A 1 392 ? 12.08500  -0.15100  -28.79100 1.000 17.68905 ? 392 HIS A ND1   1 
ATOM   3113 C  CD2   . HIS A 1 392 ? 14.03400  0.34100   -29.64600 1.000 14.98151 ? 392 HIS A CD2   1 
ATOM   3114 C  CE1   . HIS A 1 392 ? 11.86800  0.35900   -29.99100 1.000 19.22967 ? 392 HIS A CE1   1 
ATOM   3115 N  NE2   . HIS A 1 392 ? 13.03400  0.66700   -30.53000 1.000 17.58593 ? 392 HIS A NE2   1 
ATOM   3116 N  N     . TYR A 1 393 ? 15.93480  -2.93380  -28.15808 1.000 5.45861  ? 393 TYR A N     1 
ATOM   3117 C  CA    . TYR A 1 393 ? 16.74076  -3.54581  -29.21010 1.000 7.90291  ? 393 TYR A CA    1 
ATOM   3118 C  C     . TYR A 1 393 ? 16.84169  -5.05882  -29.07414 1.000 8.48849  ? 393 TYR A C     1 
ATOM   3119 O  O     . TYR A 1 393 ? 16.90165  -5.75980  -30.09015 1.000 6.33290  ? 393 TYR A O     1 
ATOM   3120 C  CB    . TYR A 1 393 ? 18.13779  -2.91888  -29.23009 1.000 9.20071  ? 393 TYR A CB    1 
ATOM   3121 C  CG    . TYR A 1 393 ? 18.15187  -1.47387  -29.68706 1.000 8.10572  ? 393 TYR A CG    1 
ATOM   3122 C  CD1   . TYR A 1 393 ? 17.47888  -1.08681  -30.83904 1.000 8.62413  ? 393 TYR A CD1   1 
ATOM   3123 C  CD2   . TYR A 1 393 ? 18.83092  -0.49992  -28.96504 1.000 10.84554 ? 393 TYR A CD2   1 
ATOM   3124 C  CE1   . TYR A 1 393 ? 17.48595  0.22220   -31.26201 1.000 10.52381 ? 393 TYR A CE1   1 
ATOM   3125 C  CE2   . TYR A 1 393 ? 18.84198  0.81808   -29.38501 1.000 16.80088 ? 393 TYR A CE2   1 
ATOM   3126 C  CZ    . TYR A 1 393 ? 18.16700  1.17015   -30.53299 1.000 13.51965 ? 393 TYR A CZ    1 
ATOM   3127 O  OH    . TYR A 1 393 ? 18.17206  2.47816   -30.95796 1.000 14.77057 ? 393 TYR A OH    1 
ATOM   3128 N  N     . LEU A 1 394 ? 16.85167  -5.58185  -27.84915 1.000 7.55554  ? 394 LEU A N     1 
ATOM   3129 C  CA    . LEU A 1 394 ? 17.05759  -7.01587  -27.65718 1.000 9.20209  ? 394 LEU A CA    1 
ATOM   3130 C  C     . LEU A 1 394 ? 15.79055  -7.81379  -27.95720 1.000 8.63818  ? 394 LEU A C     1 
ATOM   3131 O  O     . LEU A 1 394 ? 15.84050  -8.84478  -28.63722 1.000 7.55699  ? 394 LEU A O     1 
ATOM   3132 C  CB    . LEU A 1 394 ? 17.53259  -7.29592  -26.22619 1.000 8.05930  ? 394 LEU A CB    1 
ATOM   3133 C  CG    . LEU A 1 394 ? 18.78862  -6.54900  -25.76018 1.000 8.06998  ? 394 LEU A CG    1 
ATOM   3134 C  CD1   . LEU A 1 394 ? 19.22961  -6.98305  -24.35719 1.000 7.40226  ? 394 LEU A CD1   1 
ATOM   3135 C  CD2   . LEU A 1 394 ? 19.91961  -6.72303  -26.75919 1.000 4.38673  ? 394 LEU A CD2   1 
ATOM   3136 N  N     . ASN A 1 395 ? 14.65358  -7.36075  -27.42918 1.000 6.58123  ? 395 ASN A N     1 
ATOM   3137 C  CA    . ASN A 1 395 ? 13.37154  -8.01568  -27.68019 1.000 7.40452  ? 395 ASN A CA    1 
ATOM   3138 C  C     . ASN A 1 395 ? 13.08253  -8.08863  -29.17519 1.000 8.95387  ? 395 ASN A C     1 
ATOM   3139 O  O     . ASN A 1 395 ? 12.69848  -9.14060  -29.69822 1.000 8.29291  ? 395 ASN A O     1 
ATOM   3140 C  CB    . ASN A 1 395 ? 12.29000  -7.22200  -26.95500 1.000 5.87070  ? 395 ASN A CB    1 
ATOM   3141 C  CG    . ASN A 1 395 ? 11.07900  -8.02800  -26.53400 1.000 9.75669  ? 395 ASN A CG    1 
ATOM   3142 O  OD1   . ASN A 1 395 ? 10.06100  -8.01600  -27.21400 1.000 12.42736 ? 395 ASN A OD1   1 
ATOM   3143 N  ND2   . ASN A 1 395 ? 11.21200  -8.73600  -25.41500 1.000 12.92566 ? 395 ASN A ND2   1 
ATOM   3144 N  N     . ALA A 1 396 ? 13.26559  -6.96662  -29.87817 1.000 8.99757  ? 396 ALA A N     1 
ATOM   3145 C  CA    . ALA A 1 396 ? 12.96858  -6.90957  -31.30616 1.000 8.45640  ? 396 ALA A CA    1 
ATOM   3146 C  C     . ALA A 1 396 ? 13.94154  -7.75760  -32.11519 1.000 9.20002  ? 396 ALA A C     1 
ATOM   3147 O  O     . ALA A 1 396 ? 13.53950  -8.40856  -33.08620 1.000 6.67727  ? 396 ALA A O     1 
ATOM   3148 C  CB    . ALA A 1 396 ? 12.99766  -5.45956  -31.79113 1.000 10.75677 ? 396 ALA A CB    1 
ATOM   3149 N  N     . ALA A 1 397 ? 15.22554  -7.75368  -31.74319 1.000 8.75859  ? 397 ALA A N     1 
ATOM   3150 C  CA    . ALA A 1 397 ? 16.20950  -8.52871  -32.49322 1.000 10.18485 ? 397 ALA A CA    1 
ATOM   3151 C  C     . ALA A 1 397 ? 15.98642  -10.02470 -32.31425 1.000 8.06335  ? 397 ALA A C     1 
ATOM   3152 O  O     . ALA A 1 397 ? 16.03838  -10.78368 -33.28927 1.000 9.57953  ? 397 ALA A O     1 
ATOM   3153 C  CB    . ALA A 1 397 ? 17.62852  -8.14679  -32.07421 1.000 9.56525  ? 397 ALA A CB    1 
ATOM   3154 N  N     . ASN A 1 398 ? 15.72941  -10.47072 -31.08026 1.000 9.33554  ? 398 ASN A N     1 
ATOM   3155 C  CA    . ASN A 1 398 ? 15.48533  -11.89071 -30.85329 1.000 8.89107  ? 398 ASN A CA    1 
ATOM   3156 C  C     . ASN A 1 398 ? 14.13331  -12.33763 -31.39630 1.000 8.72758  ? 398 ASN A C     1 
ATOM   3157 O  O     . ASN A 1 398 ? 13.95425  -13.52861 -31.67432 1.000 8.57339  ? 398 ASN A O     1 
ATOM   3158 C  CB    . ASN A 1 398 ? 15.59132  -12.22375 -29.36330 1.000 7.58509  ? 398 ASN A CB    1 
ATOM   3159 C  CG    . ASN A 1 398 ? 17.02333  -12.20584 -28.86631 1.000 7.28164  ? 398 ASN A CG    1 
ATOM   3160 O  OD1   . ASN A 1 398 ? 17.72028  -13.21987 -28.90333 1.000 8.35998  ? 398 ASN A OD1   1 
ATOM   3161 N  ND2   . ASN A 1 398 ? 17.47339  -11.04587 -28.41128 1.000 7.39547  ? 398 ASN A ND2   1 
ATOM   3162 N  N     . TRP A 1 399 ? 13.17836  -11.41658 -31.55527 1.000 6.68510  ? 399 TRP A N     1 
ATOM   3163 C  CA    . TRP A 1 399 ? 11.90833  -11.78150 -32.17728 1.000 8.20106  ? 399 TRP A CA    1 
ATOM   3164 C  C     . TRP A 1 399 ? 12.06932  -11.96047 -33.68228 1.000 9.92332  ? 399 TRP A C     1 
ATOM   3165 O  O     . TRP A 1 399 ? 11.51227  -12.89943 -34.26530 1.000 6.48215  ? 399 TRP A O     1 
ATOM   3166 C  CB    . TRP A 1 399 ? 10.84539  -10.72745 -31.86725 1.000 10.45592 ? 399 TRP A CB    1 
ATOM   3167 C  CG    . TRP A 1 399 ? 10.00938  -11.06444 -30.67325 1.000 9.85566  ? 399 TRP A CG    1 
ATOM   3168 C  CD1   . TRP A 1 399 ? 10.06041  -10.48047 -29.44124 1.000 9.54053  ? 399 TRP A CD1   1 
ATOM   3169 C  CD2   . TRP A 1 399 ? 9.00333   -12.08039 -30.59227 1.000 7.71793  ? 399 TRP A CD2   1 
ATOM   3170 N  NE1   . TRP A 1 399 ? 9.14239   -11.06244 -28.60225 1.000 7.91486  ? 399 TRP A NE1   1 
ATOM   3171 C  CE2   . TRP A 1 399 ? 8.47933   -12.04739 -29.28427 1.000 7.18102  ? 399 TRP A CE2   1 
ATOM   3172 C  CE3   . TRP A 1 399 ? 8.49028   -13.01034 -31.50029 1.000 8.27176  ? 399 TRP A CE3   1 
ATOM   3173 C  CZ2   . TRP A 1 399 ? 7.47129   -12.90835 -28.86328 1.000 7.44960  ? 399 TRP A CZ2   1 
ATOM   3174 C  CZ3   . TRP A 1 399 ? 7.48523   -13.86430 -31.07931 1.000 7.90859  ? 399 TRP A CZ3   1 
ATOM   3175 C  CH2   . TRP A 1 399 ? 6.99024   -13.80931 -29.77330 1.000 5.42092  ? 399 TRP A CH2   1 
ATOM   3176 N  N     . MET A 1 400 ? 12.82636  -11.06749 -34.32626 1.000 9.57003  ? 400 MET A N     1 
ATOM   3177 C  CA    . MET A 1 400 ? 13.15935  -11.25448 -35.73327 1.000 10.41358 ? 400 MET A CA    1 
ATOM   3178 C  C     . MET A 1 400 ? 14.01528  -12.49452 -35.94330 1.000 9.39074  ? 400 MET A C     1 
ATOM   3179 O  O     . MET A 1 400 ? 13.92825  -13.13249 -36.99732 1.000 9.46643  ? 400 MET A O     1 
ATOM   3180 C  CB    . MET A 1 400 ? 13.87541  -10.01950 -36.27524 1.000 10.96611 ? 400 MET A CB    1 
ATOM   3181 C  CG    . MET A 1 400 ? 12.99647  -8.78546  -36.33721 1.000 14.51815 ? 400 MET A CG    1 
ATOM   3182 S  SD    . MET A 1 400 ? 13.81754  -7.39048  -37.12418 1.000 11.38056 ? 400 MET A SD    1 
ATOM   3183 C  CE    . MET A 1 400 ? 15.04256  -6.97857  -35.88817 1.000 10.99441 ? 400 MET A CE    1 
ATOM   3184 N  N     . TRP A 1 401 ? 14.84227  -12.84658 -34.95631 1.000 9.48331  ? 401 TRP A N     1 
ATOM   3185 C  CA    . TRP A 1 401 ? 15.63321  -14.06962 -35.04634 1.000 10.13756 ? 401 TRP A CA    1 
ATOM   3186 C  C     . TRP A 1 401 ? 14.73515  -15.29957 -35.02737 1.000 10.36215 ? 401 TRP A C     1 
ATOM   3187 O  O     . TRP A 1 401 ? 14.81110  -16.15456 -35.91639 1.000 13.06819 ? 401 TRP A O     1 
ATOM   3188 C  CB    . TRP A 1 401 ? 16.64221  -14.11770 -33.89735 1.000 9.47017  ? 401 TRP A CB    1 
ATOM   3189 C  CG    . TRP A 1 401 ? 17.57315  -15.30074 -33.91038 1.000 11.94495 ? 401 TRP A CG    1 
ATOM   3190 C  CD1   . TRP A 1 401 ? 17.23908  -16.61873 -33.77341 1.000 11.57023 ? 401 TRP A CD1   1 
ATOM   3191 C  CD2   . TRP A 1 401 ? 18.99915  -15.26181 -34.02939 1.000 13.61502 ? 401 TRP A CD2   1 
ATOM   3192 N  NE1   . TRP A 1 401 ? 18.36804  -17.40179 -33.82243 1.000 13.78526 ? 401 TRP A NE1   1 
ATOM   3193 C  CE2   . TRP A 1 401 ? 19.46208  -16.59084 -33.97642 1.000 16.27026 ? 401 TRP A CE2   1 
ATOM   3194 C  CE3   . TRP A 1 401 ? 19.92820  -14.22986 -34.18336 1.000 14.64986 ? 401 TRP A CE3   1 
ATOM   3195 C  CZ2   . TRP A 1 401 ? 20.81207  -16.91390 -34.07443 1.000 13.73907 ? 401 TRP A CZ2   1 
ATOM   3196 C  CZ3   . TRP A 1 401 ? 21.26519  -14.55192 -34.28038 1.000 12.55319 ? 401 TRP A CZ3   1 
ATOM   3197 C  CH2   . TRP A 1 401 ? 21.69612  -15.88195 -34.22441 1.000 15.82484 ? 401 TRP A CH2   1 
ATOM   3198 N  N     . LEU A 1 402 ? 13.87014  -15.40255 -34.01437 1.000 9.55591  ? 402 LEU A N     1 
ATOM   3199 C  CA    . LEU A 1 402 ? 13.02909  -16.58552 -33.86939 1.000 9.61423  ? 402 LEU A CA    1 
ATOM   3200 C  C     . LEU A 1 402 ? 12.02207  -16.71144 -35.00339 1.000 12.08324 ? 402 LEU A C     1 
ATOM   3201 O  O     . LEU A 1 402 ? 11.64802  -17.82941 -35.37242 1.000 12.05869 ? 402 LEU A O     1 
ATOM   3202 C  CB    . LEU A 1 402 ? 12.30109  -16.55751 -32.52439 1.000 7.75683  ? 402 LEU A CB    1 
ATOM   3203 C  CG    . LEU A 1 402 ? 12.94606  -17.34657 -31.38541 1.000 8.85986  ? 402 LEU A CG    1 
ATOM   3204 C  CD1   . LEU A 1 402 ? 13.01798  -18.83157 -31.72545 1.000 9.05094  ? 402 LEU A CD1   1 
ATOM   3205 C  CD2   . LEU A 1 402 ? 14.32609  -16.79965 -31.06740 1.000 11.59297 ? 402 LEU A CD2   1 
ATOM   3206 N  N     . SER A 1 403 ? 11.56813  -15.59240 -35.55936 1.000 8.19482  ? 403 SER A N     1 
ATOM   3207 C  CA    . SER A 1 403 ? 10.64712  -15.63333 -36.68736 1.000 9.32932  ? 403 SER A CA    1 
ATOM   3208 C  C     . SER A 1 403 ? 11.35411  -15.83733 -38.02037 1.000 9.25521  ? 403 SER A C     1 
ATOM   3209 O  O     . SER A 1 403 ? 10.68810  -15.81227 -39.06137 1.000 8.91289  ? 403 SER A O     1 
ATOM   3210 C  CB    . SER A 1 403 ? 9.81419   -14.34929 -36.73333 1.000 9.71871  ? 403 SER A CB    1 
ATOM   3211 O  OG    . SER A 1 403 ? 10.64825  -13.20133 -36.71830 1.000 9.01117  ? 403 SER A OG    1 
ATOM   3212 N  N     . ALA A 1 404 ? 12.67510  -16.04240 -38.00738 1.000 9.11086  ? 404 ALA A N     1 
ATOM   3213 C  CA    . ALA A 1 404 ? 13.47708  -16.20741 -39.22439 1.000 12.33427 ? 404 ALA A CA    1 
ATOM   3214 C  C     . ALA A 1 404 ? 13.28514  -15.03738 -40.18736 1.000 12.10994 ? 404 ALA A C     1 
ATOM   3215 O  O     . ALA A 1 404 ? 13.24713  -15.21035 -41.40736 1.000 12.98354 ? 404 ALA A O     1 
ATOM   3216 C  CB    . ALA A 1 404 ? 13.17701  -17.54038 -39.91642 1.000 14.16403 ? 404 ALA A CB    1 
ATOM   3217 N  N     . SER A 1 405 ? 13.16520  -13.82939 -39.63833 1.000 9.40285  ? 405 SER A N     1 
ATOM   3218 C  CA    . SER A 1 405 ? 13.03326  -12.62936 -40.45330 1.000 14.79124 ? 405 SER A CA    1 
ATOM   3219 C  C     . SER A 1 405 ? 14.31730  -11.81542 -40.52429 1.000 12.14436 ? 405 SER A C     1 
ATOM   3220 O  O     . SER A 1 405 ? 14.41334  -10.91341 -41.36126 1.000 15.33683 ? 405 SER A O     1 
ATOM   3221 C  CB    . SER A 1 405 ? 11.89731  -11.74232 -39.92327 1.000 12.32345 ? 405 SER A CB    1 
ATOM   3222 O  OG    . SER A 1 405 ? 10.66327  -12.43725 -39.92329 1.000 10.40564 ? 405 SER A OG    1 
ATOM   3223 N  N     . ALA A 1 406 ? 15.29629  -12.11249 -39.67430 1.000 18.08047 ? 406 ALA A N     1 
ATOM   3224 C  CA    . ALA A 1 406 ? 16.57632  -11.41856 -39.66429 1.000 14.39373 ? 406 ALA A CA    1 
ATOM   3225 C  C     . ALA A 1 406 ? 17.56129  -12.23263 -38.84131 1.000 13.97972 ? 406 ALA A C     1 
ATOM   3226 O  O     . ALA A 1 406 ? 17.16725  -12.93063 -37.90232 1.000 14.66092 ? 406 ALA A O     1 
ATOM   3227 C  CB    . ALA A 1 406 ? 16.44840  -10.00157 -39.09125 1.000 14.96676 ? 406 ALA A CB    1 
ATOM   3228 N  N     . PHE A 1 407 ? 18.83929  -12.15468 -39.22431 1.000 14.87728 ? 407 PHE A N     1 
ATOM   3229 C  CA    . PHE A 1 407 ? 19.95226  -12.78776 -38.51633 1.000 14.21015 ? 407 PHE A CA    1 
ATOM   3230 C  C     . PHE A 1 407 ? 19.91418  -14.31275 -38.57637 1.000 17.56590 ? 407 PHE A C     1 
ATOM   3231 O  O     . PHE A 1 407 ? 20.96515  -14.95981 -38.54039 1.000 16.85494 ? 407 PHE A O     1 
ATOM   3232 C  CB    . PHE A 1 407 ? 19.99229  -12.32779 -37.05432 1.000 14.84830 ? 407 PHE A CB    1 
ATOM   3233 C  CG    . PHE A 1 407 ? 19.87836  -10.83979 -36.88028 1.000 15.13748 ? 407 PHE A CG    1 
ATOM   3234 C  CD1   . PHE A 1 407 ? 20.83041  -9.98983  -37.41727 1.000 15.00077 ? 407 PHE A CD1   1 
ATOM   3235 C  CD2   . PHE A 1 407 ? 18.82139  -10.29275 -36.16827 1.000 15.72420 ? 407 PHE A CD2   1 
ATOM   3236 C  CE1   . PHE A 1 407 ? 20.72548  -8.61782  -37.25624 1.000 14.85342 ? 407 PHE A CE1   1 
ATOM   3237 C  CE2   . PHE A 1 407 ? 18.71146  -8.92375  -36.00123 1.000 12.08720 ? 407 PHE A CE2   1 
ATOM   3238 C  CZ    . PHE A 1 407 ? 19.66450  -8.08479  -36.54522 1.000 17.98093 ? 407 PHE A CZ    1 
ATOM   3239 N  N     . PHE A 1 408 ? 18.71815  -14.89469 -38.66238 1.000 16.45317 ? 408 PHE A N     1 
ATOM   3240 C  CA    . PHE A 1 408 ? 18.52308  -16.33768 -38.66241 1.000 16.37657 ? 408 PHE A CA    1 
ATOM   3241 C  C     . PHE A 1 408 ? 17.68205  -16.73061 -39.86741 1.000 17.34969 ? 408 PHE A C     1 
ATOM   3242 O  O     . PHE A 1 408 ? 16.71409  -16.04455 -40.20939 1.000 17.25728 ? 408 PHE A O     1 
ATOM   3243 C  CB    . PHE A 1 408 ? 17.83706  -16.80068 -37.36742 1.000 13.72395 ? 408 PHE A CB    1 
ATOM   3244 C  CG    . PHE A 1 408 ? 17.72099  -18.29367 -37.23445 1.000 16.44567 ? 408 PHE A CG    1 
ATOM   3245 C  CD1   . PHE A 1 408 ? 18.79795  -19.04774 -36.79647 1.000 15.80798 ? 408 PHE A CD1   1 
ATOM   3246 C  CD2   . PHE A 1 408 ? 16.52995  -18.94061 -37.52646 1.000 14.87958 ? 408 PHE A CD2   1 
ATOM   3247 C  CE1   . PHE A 1 408 ? 18.69688  -20.41474 -36.66251 1.000 12.39470 ? 408 PHE A CE1   1 
ATOM   3248 C  CE2   . PHE A 1 408 ? 16.42288  -20.31060 -37.39249 1.000 15.09727 ? 408 PHE A CE2   1 
ATOM   3249 C  CZ    . PHE A 1 408 ? 17.50785  -21.04867 -36.96052 1.000 15.35377 ? 408 PHE A CZ    1 
ATOM   3250 N  N     . SER A 1 409 ? 18.05000  -17.83861 -40.50844 1.000 15.28237 ? 409 SER A N     1 
ATOM   3251 C  CA    . SER A 1 409 ? 17.38297  -18.25855 -41.73045 1.000 14.68624 ? 409 SER A CA    1 
ATOM   3252 C  C     . SER A 1 409 ? 16.91890  -19.70653 -41.73348 1.000 15.71356 ? 409 SER A C     1 
ATOM   3253 O  O     . SER A 1 409 ? 16.15287  -20.07847 -42.62849 1.000 12.93653 ? 409 SER A O     1 
ATOM   3254 C  CB    . SER A 1 409 ? 18.30298  -18.04657 -42.93945 1.000 17.26041 ? 409 SER A CB    1 
ATOM   3255 O  OG    . SER A 1 409 ? 19.33593  -19.01462 -42.95448 1.000 18.57044 ? 409 SER A OG    1 
ATOM   3256 N  N     . GLN A 1 410 ? 17.35286  -20.53257 -40.78250 1.000 18.30776 ? 410 GLN A N     1 
ATOM   3257 C  CA    . GLN A 1 410 ? 17.04879  -21.96456 -40.80054 1.000 13.65942 ? 410 GLN A CA    1 
ATOM   3258 C  C     . GLN A 1 410 ? 15.61178  -22.17449 -40.32554 1.000 12.77278 ? 410 GLN A C     1 
ATOM   3259 O  O     . GLN A 1 410 ? 15.33676  -22.51251 -39.17154 1.000 17.33673 ? 410 GLN A O     1 
ATOM   3260 C  CB    . GLN A 1 410 ? 18.05175  -22.72863 -39.94456 1.000 13.27003 ? 410 GLN A CB    1 
ATOM   3261 C  CG    . GLN A 1 410 ? 17.90067  -24.23462 -39.99959 1.000 16.98288 ? 410 GLN A CG    1 
ATOM   3262 C  CD    . GLN A 1 410 ? 18.00764  -24.77659 -41.40961 1.000 15.40739 ? 410 GLN A CD    1 
ATOM   3263 O  OE1   . GLN A 1 410 ? 16.99963  -24.99752 -42.07961 1.000 16.25820 ? 410 GLN A OE1   1 
ATOM   3264 N  NE2   . GLN A 1 410 ? 19.23363  -24.99364 -41.86862 1.000 13.92412 ? 410 GLN A NE2   1 
ATOM   3265 N  N     . TYR A 1 411 ? 14.67078  -21.97042 -41.24953 1.000 13.95529 ? 411 TYR A N     1 
ATOM   3266 C  CA    . TYR A 1 411 ? 13.25578  -22.11036 -40.92652 1.000 15.16562 ? 411 TYR A CA    1 
ATOM   3267 C  C     . TYR A 1 411 ? 12.79070  -23.56034 -40.89056 1.000 15.88479 ? 411 TYR A C     1 
ATOM   3268 O  O     . TYR A 1 411 ? 11.66169  -23.81729 -40.45656 1.000 17.11155 ? 411 TYR A O     1 
ATOM   3269 C  CB    . TYR A 1 411 ? 12.40081  -21.31829 -41.92350 1.000 15.25285 ? 411 TYR A CB    1 
ATOM   3270 C  CG    . TYR A 1 411 ? 12.64779  -21.65927 -43.37751 1.000 16.51455 ? 411 TYR A CG    1 
ATOM   3271 C  CD1   . TYR A 1 411 ? 13.63782  -21.01030 -44.10250 1.000 20.74720 ? 411 TYR A CD1   1 
ATOM   3272 C  CD2   . TYR A 1 411 ? 11.88374  -22.62022 -44.02753 1.000 19.72767 ? 411 TYR A CD2   1 
ATOM   3273 C  CE1   . TYR A 1 411 ? 13.86880  -21.31329 -45.42651 1.000 18.38627 ? 411 TYR A CE1   1 
ATOM   3274 C  CE2   . TYR A 1 411 ? 12.10672  -22.92820 -45.35654 1.000 16.76631 ? 411 TYR A CE2   1 
ATOM   3275 C  CZ    . TYR A 1 411 ? 13.10275  -22.27023 -46.05053 1.000 20.18941 ? 411 TYR A CZ    1 
ATOM   3276 O  OH    . TYR A 1 411 ? 13.33973  -22.56421 -47.37054 1.000 26.32628 ? 411 TYR A OH    1 
ATOM   3277 N  N     . PHE A 1 412 ? 13.61666  -24.50737 -41.33958 1.000 16.02400 ? 412 PHE A N     1 
ATOM   3278 C  CA    . PHE A 1 412 ? 13.27158  -25.91835 -41.22161 1.000 14.68918 ? 412 PHE A CA    1 
ATOM   3279 C  C     . PHE A 1 412 ? 13.45956  -26.45040 -39.80963 1.000 15.41953 ? 412 PHE A C     1 
ATOM   3280 O  O     . PHE A 1 412 ? 12.98351  -27.55138 -39.51065 1.000 16.03882 ? 412 PHE A O     1 
ATOM   3281 C  CB    . PHE A 1 412 ? 14.10354  -26.75837 -42.19564 1.000 17.22454 ? 412 PHE A CB    1 
ATOM   3282 C  CG    . PHE A 1 412 ? 13.74954  -26.54032 -43.64063 1.000 17.27425 ? 412 PHE A CG    1 
ATOM   3283 C  CD1   . PHE A 1 412 ? 12.60051  -27.09725 -44.17464 1.000 19.61631 ? 412 PHE A CD1   1 
ATOM   3284 C  CD2   . PHE A 1 412 ? 14.56858  -25.78634 -44.46562 1.000 16.96937 ? 412 PHE A CD2   1 
ATOM   3285 C  CE1   . PHE A 1 412 ? 12.26752  -26.90020 -45.50063 1.000 18.13647 ? 412 PHE A CE1   1 
ATOM   3286 C  CE2   . PHE A 1 412 ? 14.24158  -25.59030 -45.79561 1.000 17.02806 ? 412 PHE A CE2   1 
ATOM   3287 C  CZ    . PHE A 1 412 ? 13.08855  -26.14622 -46.31162 1.000 15.39163 ? 412 PHE A CZ    1 
ATOM   3288 N  N     . ARG A 1 413 ? 14.16045  -25.71338 -38.95184 1.000 16.67285 ? 413 ARG A N     1 
ATOM   3289 C  CA    . ARG A 1 413 ? 14.33729  -26.08333 -37.55000 1.000 16.36523 ? 413 ARG A CA    1 
ATOM   3290 C  C     . ARG A 1 413 ? 13.15885  -25.52082 -36.76382 1.000 15.88317 ? 413 ARG A C     1 
ATOM   3291 O  O     . ARG A 1 413 ? 13.11848  -24.32818 -36.45391 1.000 14.38916 ? 413 ARG A O     1 
ATOM   3292 C  CB    . ARG A 1 413 ? 15.66495  -25.55169 -37.02434 1.000 17.49111 ? 413 ARG A CB    1 
ATOM   3293 C  CG    . ARG A 1 413 ? 16.34456  -26.46063 -36.01802 1.000 20.75115 ? 413 ARG A CG    1 
ATOM   3294 C  CD    . ARG A 1 413 ? 15.95971  -26.11004 -34.59855 1.000 23.55371 ? 413 ARG A CD    1 
ATOM   3295 N  NE    . ARG A 1 413 ? 16.44108  -27.11000 -33.65490 1.000 24.59650 ? 413 ARG A NE    1 
ATOM   3296 C  CZ    . ARG A 1 413 ? 15.68259  -28.05388 -33.11677 1.000 26.52851 ? 413 ARG A CZ    1 
ATOM   3297 N  NH1   . ARG A 1 413 ? 14.39412  -28.14918 -33.40014 1.000 21.84972 ? 413 ARG A NH1   1 
ATOM   3298 N  NH2   . ARG A 1 413 ? 16.22887  -28.91863 -32.26710 1.000 31.30028 ? 413 ARG A NH2   1 
ATOM   3299 N  N     . VAL A 1 414 ? 12.19158  -26.37641 -36.44362 1.000 13.65109 ? 414 VAL A N     1 
ATOM   3300 C  CA    . VAL A 1 414 ? 10.96260  -25.97437 -35.76461 1.000 14.23280 ? 414 VAL A CA    1 
ATOM   3301 C  C     . VAL A 1 414 ? 10.86557  -26.74239 -34.45562 1.000 15.38414 ? 414 VAL A C     1 
ATOM   3302 O  O     . VAL A 1 414 ? 10.84751  -27.98039 -34.45665 1.000 17.07294 ? 414 VAL A O     1 
ATOM   3303 C  CB    . VAL A 1 414 ? 9.72259   -26.22628 -36.63561 1.000 13.25458 ? 414 VAL A CB    1 
ATOM   3304 C  CG1   . VAL A 1 414 ? 8.46061   -25.80624 -35.89959 1.000 14.11596 ? 414 VAL A CG1   1 
ATOM   3305 C  CG2   . VAL A 1 414 ? 9.84162   -25.48926 -37.96159 1.000 19.21928 ? 414 VAL A CG2   1 
ATOM   3306 N  N     . TYR A 1 415 ? 10.79461  -26.01341 -33.34461 1.000 12.29561 ? 415 TYR A N     1 
ATOM   3307 C  CA    . TYR A 1 415 ? 10.69358  -26.65144 -32.04062 1.000 12.94577 ? 415 TYR A CA    1 
ATOM   3308 C  C     . TYR A 1 415 ? 9.33255   -27.31238 -31.87763 1.000 14.56378 ? 415 TYR A C     1 
ATOM   3309 O  O     . TYR A 1 415 ? 8.31857   -26.81131 -32.36762 1.000 12.57047 ? 415 TYR A O     1 
ATOM   3310 C  CB    . TYR A 1 415 ? 10.90964  -25.63248 -30.92460 1.000 15.64727 ? 415 TYR A CB    1 
ATOM   3311 C  CG    . TYR A 1 415 ? 12.25867  -24.95555 -30.94659 1.000 17.05146 ? 415 TYR A CG    1 
ATOM   3312 C  CD1   . TYR A 1 415 ? 13.41664  -25.66861 -30.66761 1.000 15.18285 ? 415 TYR A CD1   1 
ATOM   3313 C  CD2   . TYR A 1 415 ? 12.37474  -23.60054 -31.23056 1.000 12.02340 ? 415 TYR A CD2   1 
ATOM   3314 C  CE1   . TYR A 1 415 ? 14.65267  -25.05367 -30.67860 1.000 16.07771 ? 415 TYR A CE1   1 
ATOM   3315 C  CE2   . TYR A 1 415 ? 13.60977  -22.97661 -31.24455 1.000 12.12245 ? 415 TYR A CE2   1 
ATOM   3316 C  CZ    . TYR A 1 415 ? 14.74374  -23.70867 -30.96757 1.000 14.12652 ? 415 TYR A CZ    1 
ATOM   3317 O  OH    . TYR A 1 415 ? 15.97677  -23.09273 -30.97856 1.000 12.67705 ? 415 TYR A OH    1 
ATOM   3318 N  N     . SER A 1 416 ? 9.31550   -28.44439 -31.17966 1.000 14.29720 ? 416 SER A N     1 
ATOM   3319 C  CA    . SER A 1 416 ? 8.07546   -29.16133 -30.92067 1.000 12.94723 ? 416 SER A CA    1 
ATOM   3320 C  C     . SER A 1 416 ? 7.51649   -28.74434 -29.56966 1.000 12.11340 ? 416 SER A C     1 
ATOM   3321 O  O     . SER A 1 416 ? 8.20348   -28.90540 -28.55266 1.000 9.28801  ? 416 SER A O     1 
ATOM   3322 C  CB    . SER A 1 416 ? 8.30738   -30.66235 -30.94571 1.000 11.41174 ? 416 SER A CB    1 
ATOM   3323 O  OG    . SER A 1 416 ? 7.20235   -31.36130 -30.39872 1.000 10.01208 ? 416 SER A OG    1 
ATOM   3324 N  N     . PRO A 1 417 ? 6.29051   -28.21328 -29.50364 1.000 13.10191 ? 417 PRO A N     1 
ATOM   3325 C  CA    . PRO A 1 417 ? 5.69754   -27.87928 -28.20063 1.000 9.63386  ? 417 PRO A CA    1 
ATOM   3326 C  C     . PRO A 1 417 ? 5.38948   -29.09128 -27.33766 1.000 12.64960 ? 417 PRO A C     1 
ATOM   3327 O  O     . PRO A 1 417 ? 4.94249   -28.92229 -26.19865 1.000 11.09269 ? 417 PRO A O     1 
ATOM   3328 C  CB    . PRO A 1 417 ? 4.41057   -27.13320 -28.58861 1.000 7.66610  ? 417 PRO A CB    1 
ATOM   3329 C  CG    . PRO A 1 417 ? 4.06854   -27.66315 -29.93762 1.000 12.43153 ? 417 PRO A CG    1 
ATOM   3330 C  CD    . PRO A 1 417 ? 5.38653   -27.89621 -30.62163 1.000 9.33818  ? 417 PRO A CD    1 
ATOM   3331 N  N     . VAL A 1 418 ? 5.61842   -30.30228 -27.83769 1.000 10.42282 ? 418 VAL A N     1 
ATOM   3332 C  CA    . VAL A 1 418 ? 5.36036   -31.52429 -27.09572 1.000 16.99949 ? 418 VAL A CA    1 
ATOM   3333 C  C     . VAL A 1 418 ? 6.65632   -32.18536 -26.63274 1.000 11.52434 ? 418 VAL A C     1 
ATOM   3334 O  O     . VAL A 1 418 ? 6.73931   -32.66039 -25.49775 1.000 16.29350 ? 418 VAL A O     1 
ATOM   3335 C  CB    . VAL A 1 418 ? 4.51330   -32.49922 -27.94674 1.000 13.93565 ? 418 VAL A CB    1 
ATOM   3336 C  CG1   . VAL A 1 418 ? 4.38624   -33.84123 -27.26077 1.000 15.97400 ? 418 VAL A CG1   1 
ATOM   3337 C  CG2   . VAL A 1 418 ? 3.13633   -31.90615 -28.23272 1.000 15.51417 ? 418 VAL A CG2   1 
ATOM   3338 N  N     . VAL A 1 419 ? 7.67732   -32.19440 -27.48174 1.000 13.67896 ? 419 VAL A N     1 
ATOM   3339 C  CA    . VAL A 1 419 ? 8.89128   -32.97346 -27.25376 1.000 12.90252 ? 419 VAL A CA    1 
ATOM   3340 C  C     . VAL A 1 419 ? 9.99533   -32.13853 -26.61575 1.000 11.57213 ? 419 VAL A C     1 
ATOM   3341 O  O     . VAL A 1 419 ? 10.76230  -32.65059 -25.79976 1.000 13.80933 ? 419 VAL A O     1 
ATOM   3342 C  CB    . VAL A 1 419 ? 9.37025   -33.60046 -28.58278 1.000 9.30111  ? 419 VAL A CB    1 
ATOM   3343 C  CG1   . VAL A 1 419 ? 10.80222  -34.12753 -28.46180 1.000 13.89891 ? 419 VAL A CG1   1 
ATOM   3344 C  CG2   . VAL A 1 419 ? 8.42719   -34.70740 -29.01780 1.000 14.97649 ? 419 VAL A CG2   1 
ATOM   3345 N  N     . PHE A 1 420 ? 10.08039  -30.85253 -26.97372 1.000 11.99615 ? 420 PHE A N     1 
ATOM   3346 C  CA    . PHE A 1 420 ? 11.21443  -30.02560 -26.56570 1.000 12.31384 ? 420 PHE A CA    1 
ATOM   3347 C  C     . PHE A 1 420 ? 11.38444  -30.01064 -25.05170 1.000 10.36819 ? 420 PHE A C     1 
ATOM   3348 O  O     . PHE A 1 420 ? 12.50244  -30.14071 -24.53971 1.000 9.83999  ? 420 PHE A O     1 
ATOM   3349 C  CB    . PHE A 1 420 ? 11.03850  -28.60257 -27.10067 1.000 12.50136 ? 420 PHE A CB    1 
ATOM   3350 C  CG    . PHE A 1 420 ? 12.24955  -27.72964 -26.92065 1.000 12.56627 ? 420 PHE A CG    1 
ATOM   3351 C  CD1   . PHE A 1 420 ? 13.44353  -28.03469 -27.55567 1.000 16.42086 ? 420 PHE A CD1   1 
ATOM   3352 C  CD2   . PHE A 1 420 ? 12.19061  -26.59666 -26.12863 1.000 13.47110 ? 420 PHE A CD2   1 
ATOM   3353 C  CE1   . PHE A 1 420 ? 14.55757  -27.23075 -27.39565 1.000 16.29459 ? 420 PHE A CE1   1 
ATOM   3354 C  CE2   . PHE A 1 420 ? 13.29765  -25.78972 -25.96561 1.000 11.61178 ? 420 PHE A CE2   1 
ATOM   3355 C  CZ    . PHE A 1 420 ? 14.48263  -26.10576 -26.59862 1.000 16.38441 ? 420 PHE A CZ    1 
ATOM   3356 N  N     . GLY A 1 421 ? 10.28045  -29.86060 -24.31570 1.000 12.26800 ? 421 GLY A N     1 
ATOM   3357 C  CA    . GLY A 1 421 ? 10.36946  -29.80264 -22.86769 1.000 11.81135 ? 421 GLY A CA    1 
ATOM   3358 C  C     . GLY A 1 421 ? 10.63139  -31.14767 -22.22173 1.000 13.14946 ? 421 GLY A C     1 
ATOM   3359 O  O     . GLY A 1 421 ? 11.28340  -31.21773 -21.17573 1.000 14.70088 ? 421 GLY A O     1 
ATOM   3360 N  N     . LYS A 1 422 ? 10.13934  -32.22963 -22.83175 1.000 11.17212 ? 422 LYS A N     1 
ATOM   3361 C  CA    . LYS A 1 422 ? 10.27927  -33.55565 -22.23878 1.000 16.28823 ? 422 LYS A CA    1 
ATOM   3362 C  C     . LYS A 1 422 ? 11.73225  -34.00173 -22.14980 1.000 12.86557 ? 422 LYS A C     1 
ATOM   3363 O  O     . LYS A 1 422 ? 12.04821  -34.89076 -21.35082 1.000 19.49231 ? 422 LYS A O     1 
ATOM   3364 C  CB    . LYS A 1 422 ? 9.47122   -34.57759 -23.04280 1.000 15.60440 ? 422 LYS A CB    1 
ATOM   3365 C  CG    . LYS A 1 422 ? 9.00116   -35.77159 -22.22483 1.000 19.03453 ? 422 LYS A CG    1 
ATOM   3366 C  CD    . LYS A 1 422 ? 8.31110   -36.81353 -23.09285 1.000 21.51704 ? 422 LYS A CD    1 
ATOM   3367 C  CE    . LYS A 1 422 ? 7.12313   -36.23145 -23.84283 1.000 22.29928 ? 422 LYS A CE    1 
ATOM   3368 N  NZ    . LYS A 1 422 ? 6.36307   -37.29440 -24.56386 1.000 21.40118 ? 422 LYS A NZ    1 
ATOM   3369 N  N     . LYS A 1 423 ? 12.61928  -33.40075 -22.94379 1.000 14.75667 ? 423 LYS A N     1 
ATOM   3370 C  CA    . LYS A 1 423 ? 14.02126  -33.79982 -22.92480 1.000 15.04446 ? 423 LYS A CA    1 
ATOM   3371 C  C     . LYS A 1 423 ? 14.69728  -33.37989 -21.62380 1.000 13.41032 ? 423 LYS A C     1 
ATOM   3372 O  O     . LYS A 1 423 ? 15.56225  -34.09794 -21.10782 1.000 13.73021 ? 423 LYS A O     1 
ATOM   3373 C  CB    . LYS A 1 423 ? 14.74128  -33.21083 -24.13779 1.000 10.23564 ? 423 LYS A CB    1 
ATOM   3374 C  CG    . LYS A 1 423 ? 15.84824  -34.09187 -24.68582 0.000 13.95524 ? 423 LYS A CG    1 
ATOM   3375 C  CD    . LYS A 1 423 ? 16.09824  -33.82885 -26.16381 0.000 14.60534 ? 423 LYS A CD    1 
ATOM   3376 C  CE    . LYS A 1 423 ? 16.53631  -32.39587 -26.41478 0.000 14.00295 ? 423 LYS A CE    1 
ATOM   3377 N  NZ    . LYS A 1 423 ? 17.52231  -32.31989 -27.53178 0.000 14.51055 ? 423 LYS A NZ    1 
ATOM   3378 N  N     . TYR A 1 424 ? 14.30434  -32.23288 -21.07177 1.000 9.65831  ? 424 TYR A N     1 
ATOM   3379 C  CA    . TYR A 1 424 ? 14.84137  -31.74894 -19.80476 1.000 11.43865 ? 424 TYR A CA    1 
ATOM   3380 C  C     . TYR A 1 424 ? 14.01935  -32.22593 -18.61277 1.000 11.66069 ? 424 TYR A C     1 
ATOM   3381 O  O     . TYR A 1 424 ? 14.57233  -32.74198 -17.63678 1.000 16.68744 ? 424 TYR A O     1 
ATOM   3382 C  CB    . TYR A 1 424 ? 14.89545  -30.21794 -19.79572 1.000 11.66910 ? 424 TYR A CB    1 
ATOM   3383 C  CG    . TYR A 1 424 ? 15.59548  -29.59795 -20.97871 1.000 7.74174  ? 424 TYR A CG    1 
ATOM   3384 C  CD1   . TYR A 1 424 ? 16.96649  -29.38302 -20.96671 1.000 8.84311  ? 424 TYR A CD1   1 
ATOM   3385 C  CD2   . TYR A 1 424 ? 14.87949  -29.21189 -22.10270 1.000 10.35858 ? 424 TYR A CD2   1 
ATOM   3386 C  CE1   . TYR A 1 424 ? 17.60851  -28.80903 -22.04770 1.000 8.52033  ? 424 TYR A CE1   1 
ATOM   3387 C  CE2   . TYR A 1 424 ? 15.51152  -28.63589 -23.18669 1.000 10.66598 ? 424 TYR A CE2   1 
ATOM   3388 C  CZ    . TYR A 1 424 ? 16.87553  -28.43796 -23.15469 1.000 8.13028  ? 424 TYR A CZ    1 
ATOM   3389 O  OH    . TYR A 1 424 ? 17.51155  -27.86397 -24.23268 1.000 10.55754 ? 424 TYR A OH    1 
ATOM   3390 N  N     . ASP A 1 425 ? 12.69736  -32.05186 -18.67776 1.000 11.26576 ? 425 ASP A N     1 
ATOM   3391 C  CA    . ASP A 1 425 ? 11.79136  -32.27284 -17.55376 1.000 13.39567 ? 425 ASP A CA    1 
ATOM   3392 C  C     . ASP A 1 425 ? 10.78130  -33.34578 -17.94578 1.000 11.99307 ? 425 ASP A C     1 
ATOM   3393 O  O     . ASP A 1 425 ? 9.65831   -33.02871 -18.36577 1.000 11.52166 ? 425 ASP A O     1 
ATOM   3394 C  CB    . ASP A 1 425 ? 11.09442  -30.96881 -17.16373 1.000 11.70161 ? 425 ASP A CB    1 
ATOM   3395 C  CG    . ASP A 1 425 ? 10.38942  -31.05181 -15.82372 1.000 12.78194 ? 425 ASP A CG    1 
ATOM   3396 O  OD1   . ASP A 1 425 ? 10.35937  -32.14582 -15.22175 1.000 15.19190 ? 425 ASP A OD1   1 
ATOM   3397 O  OD2   . ASP A 1 425 ? 9.86748   -30.01279 -15.36870 1.000 16.17383 ? 425 ASP A OD2   1 
ATOM   3398 N  N     . PRO A 1 426 ? 11.13924  -34.62780 -17.81681 1.000 11.32068 ? 426 PRO A N     1 
ATOM   3399 C  CA    . PRO A 1 426 ? 10.19418  -35.68874 -18.19883 1.000 12.91259 ? 426 PRO A CA    1 
ATOM   3400 C  C     . PRO A 1 426 ? 8.98518   -35.79270 -17.28383 1.000 14.13370 ? 426 PRO A C     1 
ATOM   3401 O  O     . PRO A 1 426 ? 7.94615   -36.30264 -17.71784 1.000 13.64149 ? 426 PRO A O     1 
ATOM   3402 C  CB    . PRO A 1 426 ? 11.05112  -36.95879 -18.13687 1.000 14.26437 ? 426 PRO A CB    1 
ATOM   3403 C  CG    . PRO A 1 426 ? 12.11914  -36.63386 -17.14686 1.000 16.82141 ? 426 PRO A CG    1 
ATOM   3404 C  CD    . PRO A 1 426 ? 12.42121  -35.17187 -17.33483 1.000 12.52421 ? 426 PRO A CD    1 
ATOM   3405 N  N     . GLU A 1 427 ? 9.07821   -35.32874 -16.03882 1.000 15.93128 ? 427 GLU A N     1 
ATOM   3406 C  CA    . GLU A 1 427 ? 7.95021   -35.38670 -15.11682 1.000 15.34528 ? 427 GLU A CA    1 
ATOM   3407 C  C     . GLU A 1 427 ? 7.04527   -34.16565 -15.19978 1.000 14.81420 ? 427 GLU A C     1 
ATOM   3408 O  O     . GLU A 1 427 ? 5.96427   -34.17561 -14.60078 1.000 15.48955 ? 427 GLU A O     1 
ATOM   3409 C  CB    . GLU A 1 427 ? 8.44921   -35.54676 -13.68082 1.000 17.92362 ? 427 GLU A CB    1 
ATOM   3410 C  CG    . GLU A 1 427 ? 9.09714   -36.88280 -13.43286 1.000 19.41541 ? 427 GLU A CG    1 
ATOM   3411 C  CD    . GLU A 1 427 ? 8.17208   -38.02774 -13.78088 1.000 20.85389 ? 427 GLU A CD    1 
ATOM   3412 O  OE1   . GLU A 1 427 ? 7.18107   -38.23571 -13.05088 1.000 26.04003 ? 427 GLU A OE1   1 
ATOM   3413 O  OE2   . GLU A 1 427 ? 8.43004   -38.71373 -14.79290 1.000 27.73020 ? 427 GLU A OE2   1 
ATOM   3414 N  N     . GLY A 1 428 ? 7.45832   -33.12466 -15.91676 1.000 14.56097 ? 428 GLY A N     1 
ATOM   3415 C  CA    . GLY A 1 428 ? 6.64838   -31.92961 -16.03373 1.000 12.51125 ? 428 GLY A CA    1 
ATOM   3416 C  C     . GLY A 1 428 ? 6.56943   -31.09264 -14.77671 1.000 14.29505 ? 428 GLY A C     1 
ATOM   3417 O  O     . GLY A 1 428 ? 5.55146   -30.43159 -14.55069 1.000 15.79999 ? 428 GLY A O     1 
ATOM   3418 N  N     . ARG A 1 429 ? 7.62080   -31.10487 -13.95001 1.000 16.39799 ? 429 ARG A N     1 
ATOM   3419 C  CA    . ARG A 1 429 ? 7.60739   -30.30784 -12.72760 1.000 14.74411 ? 429 ARG A CA    1 
ATOM   3420 C  C     . ARG A 1 429 ? 7.44761   -28.82773 -13.04190 1.000 13.58438 ? 429 ARG A C     1 
ATOM   3421 O  O     . ARG A 1 429 ? 6.80025   -28.09046 -12.29008 1.000 16.44620 ? 429 ARG A O     1 
ATOM   3422 C  CB    . ARG A 1 429 ? 8.88247   -30.55275 -11.91898 1.000 17.64169 ? 429 ARG A CB    1 
ATOM   3423 C  CG    . ARG A 1 429 ? 9.27385   -32.01971 -11.80738 1.000 19.38565 ? 429 ARG A CG    1 
ATOM   3424 C  CD    . ARG A 1 429 ? 10.01973  -32.32360 -10.51634 0.062 19.61645 ? 429 ARG A CD    1 
ATOM   3425 N  NE    . ARG A 1 429 ? 9.12813   -32.85632 -9.49276  0.000 20.28259 ? 429 ARG A NE    1 
ATOM   3426 C  CZ    . ARG A 1 429 ? 9.51471   -33.64111 -8.49601  0.000 20.60425 ? 429 ARG A CZ    1 
ATOM   3427 N  NH1   . ARG A 1 429 ? 10.77653  -34.01389 -8.35876  0.245 19.67433 ? 429 ARG A NH1   1 
ATOM   3428 N  NH2   . ARG A 1 429 ? 8.61071   -34.07063 -7.62026  0.134 20.69738 ? 429 ARG A NH2   1 
ATOM   3429 N  N     . PHE A 1 430 ? 8.01757   -28.37873 -14.16365 1.000 13.31966 ? 430 PHE A N     1 
ATOM   3430 C  CA    . PHE A 1 430 ? 7.82763   -26.99671 -14.59062 1.000 11.21315 ? 430 PHE A CA    1 
ATOM   3431 C  C     . PHE A 1 430 ? 6.36865   -26.73163 -14.94361 1.000 10.32518 ? 430 PHE A C     1 
ATOM   3432 O  O     . PHE A 1 430 ? 5.83870   -25.64760 -14.67058 1.000 12.59491 ? 430 PHE A O     1 
ATOM   3433 C  CB    . PHE A 1 430 ? 8.72965   -26.68872 -15.78561 1.000 10.70682 ? 430 PHE A CB    1 
ATOM   3434 C  CG    . PHE A 1 430 ? 8.61071   -25.27971 -16.29658 1.000 10.58561 ? 430 PHE A CG    1 
ATOM   3435 C  CD1   . PHE A 1 430 ? 9.35977   -24.26276 -15.73056 1.000 10.40776 ? 430 PHE A CD1   1 
ATOM   3436 C  CD2   . PHE A 1 430 ? 7.76473   -24.97364 -17.35557 1.000 8.96996  ? 430 PHE A CD2   1 
ATOM   3437 C  CE1   . PHE A 1 430 ? 9.26483   -22.96174 -16.20353 1.000 10.86927 ? 430 PHE A CE1   1 
ATOM   3438 C  CE2   . PHE A 1 430 ? 7.66179   -23.67362 -17.83254 1.000 11.15309 ? 430 PHE A CE2   1 
ATOM   3439 C  CZ    . PHE A 1 430 ? 8.41184   -22.66667 -17.25452 1.000 8.73046  ? 430 PHE A CZ    1 
ATOM   3440 N  N     . ILE A 1 431 ? 5.70859   -27.71558 -15.55363 1.000 12.26312 ? 431 ILE A N     1 
ATOM   3441 C  CA    . ILE A 1 431 ? 4.31160   -27.55350 -15.94462 1.000 12.98685 ? 431 ILE A CA    1 
ATOM   3442 C  C     . ILE A 1 431 ? 3.40761   -27.55348 -14.71661 1.000 11.99857 ? 431 ILE A C     1 
ATOM   3443 O  O     . ILE A 1 431 ? 2.50765   -26.71544 -14.58859 1.000 12.11612 ? 431 ILE A O     1 
ATOM   3444 C  CB    . ILE A 1 431 ? 3.90654   -28.65445 -16.94164 1.000 10.76952 ? 431 ILE A CB    1 
ATOM   3445 C  CG1   . ILE A 1 431 ? 4.70554   -28.52446 -18.23864 1.000 11.32212 ? 431 ILE A CG1   1 
ATOM   3446 C  CG2   . ILE A 1 431 ? 2.41854   -28.59737 -17.22863 1.000 15.55722 ? 431 ILE A CG2   1 
ATOM   3447 C  CD1   . ILE A 1 431 ? 4.36049   -29.57842 -19.26767 1.000 14.24374 ? 431 ILE A CD1   1 
ATOM   3448 N  N     . ARG A 1 432 ? 3.63001   -28.49425 -13.79715 1.000 9.94394  ? 432 ARG A N     1 
ATOM   3449 C  CA    . ARG A 1 432 ? 2.77412   -28.57397 -12.61754 1.000 15.30180 ? 432 ARG A CA    1 
ATOM   3450 C  C     . ARG A 1 432 ? 2.90261   -27.33343 -11.74235 1.000 13.42838 ? 432 ARG A C     1 
ATOM   3451 O  O     . ARG A 1 432 ? 1.93698   -26.94435 -11.07640 1.000 12.85283 ? 432 ARG A O     1 
ATOM   3452 C  CB    . ARG A 1 432 ? 3.10378   -29.83046 -11.81371 1.000 17.59241 ? 432 ARG A CB    1 
ATOM   3453 C  CG    . ARG A 1 432 ? 3.08019   -31.09578 -12.63506 1.000 16.70468 ? 432 ARG A CG    1 
ATOM   3454 C  CD    . ARG A 1 432 ? 3.64559   -32.26695 -11.85886 1.000 18.89676 ? 432 ARG A CD    1 
ATOM   3455 N  NE    . ARG A 1 432 ? 3.90589   -33.40857 -12.72365 1.000 16.33018 ? 432 ARG A NE    1 
ATOM   3456 C  CZ    . ARG A 1 432 ? 3.00441   -34.32607 -13.03896 1.000 14.43328 ? 432 ARG A CZ    1 
ATOM   3457 N  NH1   . ARG A 1 432 ? 1.76375   -34.26422 -12.58204 1.000 16.47017 ? 432 ARG A NH1   1 
ATOM   3458 N  NH2   . ARG A 1 432 ? 3.35601   -35.33154 -13.83188 1.000 20.32507 ? 432 ARG A NH2   1 
ATOM   3459 N  N     . LYS A 1 433 ? 4.07666   -26.70058 -11.73360 1.000 11.93224 ? 433 LYS A N     1 
ATOM   3460 C  CA    . LYS A 1 433 ? 4.26373   -25.48961 -10.94157 1.000 14.69468 ? 433 LYS A CA    1 
ATOM   3461 C  C     . LYS A 1 433 ? 3.40278   -24.34356 -11.46654 1.000 13.87758 ? 433 LYS A C     1 
ATOM   3462 O  O     . LYS A 1 433 ? 2.68682   -23.68654 -10.70252 1.000 10.97812 ? 433 LYS A O     1 
ATOM   3463 C  CB    . LYS A 1 433 ? 5.74174   -25.10169 -10.94057 1.000 14.81246 ? 433 LYS A CB    1 
ATOM   3464 C  CG    . LYS A 1 433 ? 6.01482   -23.63471 -10.66153 1.000 18.31227 ? 433 LYS A CG    1 
ATOM   3465 C  CD    . LYS A 1 433 ? 5.81084   -23.27273 -9.20252  1.000 22.16643 ? 433 LYS A CD    1 
ATOM   3466 C  CE    . LYS A 1 433 ? 6.23592   -21.83376 -8.94449  1.000 19.96125 ? 433 LYS A CE    1 
ATOM   3467 N  NZ    . LYS A 1 433 ? 6.05694   -21.45578 -7.51748  1.000 20.55167 ? 433 LYS A NZ    1 
ATOM   3468 N  N     . PHE A 1 434 ? 3.45779   -24.08953 -12.77353 1.000 13.70429 ? 434 PHE A N     1 
ATOM   3469 C  CA    . PHE A 1 434 ? 2.77684   -22.93348 -13.34250 1.000 10.24710 ? 434 PHE A CA    1 
ATOM   3470 C  C     . PHE A 1 434 ? 1.36683   -23.24440 -13.82250 1.000 12.01985 ? 434 PHE A C     1 
ATOM   3471 O  O     . PHE A 1 434 ? 0.51487   -22.34736 -13.83448 1.000 15.71261 ? 434 PHE A O     1 
ATOM   3472 C  CB    . PHE A 1 434 ? 3.60687   -22.35350 -14.49049 1.000 11.13015 ? 434 PHE A CB    1 
ATOM   3473 C  CG    . PHE A 1 434 ? 4.86691   -21.66957 -14.03648 1.000 12.34985 ? 434 PHE A CG    1 
ATOM   3474 C  CD1   . PHE A 1 434 ? 4.81997   -20.39858 -13.48245 1.000 13.51308 ? 434 PHE A CD1   1 
ATOM   3475 C  CD2   . PHE A 1 434 ? 6.09687   -22.29463 -14.16150 1.000 11.86702 ? 434 PHE A CD2   1 
ATOM   3476 C  CE1   . PHE A 1 434 ? 5.97801   -19.76365 -13.06244 1.000 10.10621 ? 434 PHE A CE1   1 
ATOM   3477 C  CE2   . PHE A 1 434 ? 7.25891   -21.66670 -13.74249 1.000 12.56048 ? 434 PHE A CE2   1 
ATOM   3478 C  CZ    . PHE A 1 434 ? 7.19897   -20.39971 -13.19246 1.000 12.98565 ? 434 PHE A CZ    1 
ATOM   3479 N  N     . LEU A 1 435 ? 1.09476   -24.48438 -14.21753 1.000 12.52197 ? 435 LEU A N     1 
ATOM   3480 C  CA    . LEU A 1 435 ? -0.26826  -24.88130 -14.54954 1.000 9.89073  ? 435 LEU A CA    1 
ATOM   3481 C  C     . LEU A 1 435 ? -0.75130  -25.86930 -13.49656 1.000 11.12440 ? 435 LEU A C     1 
ATOM   3482 O  O     . LEU A 1 435 ? -0.67337  -27.08830 -13.70159 1.000 11.67151 ? 435 LEU A O     1 
ATOM   3483 C  CB    . LEU A 1 435 ? -0.34029  -25.49526 -15.94855 1.000 11.82798 ? 435 LEU A CB    1 
ATOM   3484 C  CG    . LEU A 1 435 ? 0.11974   -24.62326 -17.11853 1.000 10.29397 ? 435 LEU A CG    1 
ATOM   3485 C  CD1   . LEU A 1 435 ? -0.18430  -25.32421 -18.43055 1.000 12.08378 ? 435 LEU A CD1   1 
ATOM   3486 C  CD2   . LEU A 1 435 ? -0.53519  -23.25123 -17.07150 1.000 7.40719  ? 435 LEU A CD2   1 
ATOM   3487 N  N     . PRO A 1 436 ? -1.24528  -25.38530 -12.35254 1.000 8.82858  ? 436 PRO A N     1 
ATOM   3488 C  CA    . PRO A 1 436 ? -1.58832  -26.29831 -11.25256 1.000 13.62705 ? 436 PRO A CA    1 
ATOM   3489 C  C     . PRO A 1 436 ? -2.78336  -27.18724 -11.54058 1.000 9.99785  ? 436 PRO A C     1 
ATOM   3490 O  O     . PRO A 1 436 ? -2.98141  -28.16925 -10.81560 1.000 11.67296 ? 436 PRO A O     1 
ATOM   3491 C  CB    . PRO A 1 436 ? -1.87826  -25.34832 -10.07854 1.000 15.77363 ? 436 PRO A CB    1 
ATOM   3492 C  CG    . PRO A 1 436 ? -1.33020  -24.01034 -10.49551 1.000 13.54960 ? 436 PRO A CG    1 
ATOM   3493 C  CD    . PRO A 1 436 ? -1.46420  -23.97730 -11.98451 1.000 12.70138 ? 436 PRO A CD    1 
ATOM   3494 N  N     . VAL A 1 437 ? -3.58335  -26.88218 -12.56557 1.000 12.89299 ? 437 VAL A N     1 
ATOM   3495 C  CA    . VAL A 1 437 ? -4.71440  -27.73511 -12.90959 1.000 14.80118 ? 437 VAL A CA    1 
ATOM   3496 C  C     . VAL A 1 437 ? -4.24747  -29.09212 -13.42562 1.000 13.94396 ? 437 VAL A C     1 
ATOM   3497 O  O     . VAL A 1 437 ? -5.00852  -30.06709 -13.38564 1.000 13.49564 ? 437 VAL A O     1 
ATOM   3498 C  CB    . VAL A 1 437 ? -5.61736  -27.01504 -13.93357 1.000 15.72436 ? 437 VAL A CB    1 
ATOM   3499 C  CG1   . VAL A 1 437 ? -4.89936  -26.84605 -15.26856 1.000 14.28509 ? 437 VAL A CG1   1 
ATOM   3500 C  CG2   . VAL A 1 437 ? -6.94040  -27.74597 -14.10658 1.000 17.31770 ? 437 VAL A CG2   1 
ATOM   3501 N  N     . LEU A 1 438 ? -3.00047  -29.18618 -13.88963 1.000 12.02999 ? 438 LEU A N     1 
ATOM   3502 C  CA    . LEU A 1 438 ? -2.41954  -30.43119 -14.37366 1.000 15.64712 ? 438 LEU A CA    1 
ATOM   3503 C  C     . LEU A 1 438 ? -1.49157  -31.08426 -13.35368 1.000 14.37822 ? 438 LEU A C     1 
ATOM   3504 O  O     . LEU A 1 438 ? -0.60861  -31.85930 -13.73870 1.000 17.00139 ? 438 LEU A O     1 
ATOM   3505 C  CB    . LEU A 1 438 ? -1.65553  -30.18120 -15.67366 1.000 16.74508 ? 438 LEU A CB    1 
ATOM   3506 C  CG    . LEU A 1 438 ? -2.44153  -30.01913 -16.96965 1.000 10.44027 ? 438 LEU A CG    1 
ATOM   3507 C  CD1   . LEU A 1 438 ? -1.62149  -29.21915 -17.95663 1.000 14.91202 ? 438 LEU A CD1   1 
ATOM   3508 C  CD2   . LEU A 1 438 ? -2.78660  -31.38110 -17.54168 1.000 16.78661 ? 438 LEU A CD2   1 
ATOM   3509 N  N     . LYS A 1 439 ? -1.67855  -30.80429 -12.06367 1.000 18.77202 ? 439 LYS A N     1 
ATOM   3510 C  CA    . LYS A 1 439 ? -0.70757  -31.25536 -11.07069 1.000 17.88510 ? 439 LYS A CA    1 
ATOM   3511 C  C     . LYS A 1 439 ? -0.81264  -32.75236 -10.78572 1.000 19.67293 ? 439 LYS A C     1 
ATOM   3512 O  O     . LYS A 1 439 ? 0.16733   -33.36142 -10.34374 1.000 17.82472 ? 439 LYS A O     1 
ATOM   3513 C  CB    . LYS A 1 439 ? -0.87352  -30.45338 -9.77967  1.000 19.82496 ? 439 LYS A CB    1 
ATOM   3514 C  CG    . LYS A 1 439 ? -1.68055  -31.14937 -8.69568  1.000 23.57097 ? 439 LYS A CG    1 
ATOM   3515 C  CD    . LYS A 1 439 ? -3.04952  -30.51330 -8.51866  0.000 22.17662 ? 439 LYS A CD    1 
ATOM   3516 C  CE    . LYS A 1 439 ? -3.39351  -30.34332 -7.04465  0.000 24.60329 ? 439 LYS A CE    1 
ATOM   3517 N  NZ    . LYS A 1 439 ? -2.42546  -29.44638 -6.35064  0.000 24.77622 ? 439 LYS A NZ    1 
ATOM   3518 N  N     . ASP A 1 440 ? -1.97167  -33.36530 -11.03073 1.000 17.13466 ? 440 ASP A N     1 
ATOM   3519 C  CA    . ASP A 1 440 ? -2.17474  -34.77629 -10.72376 1.000 19.27680 ? 440 ASP A CA    1 
ATOM   3520 C  C     . ASP A 1 440 ? -2.26179  -35.63926 -11.97778 1.000 16.26335 ? 440 ASP A C     1 
ATOM   3521 O  O     . ASP A 1 440 ? -2.69185  -36.79424 -11.90181 1.000 22.08364 ? 440 ASP A O     1 
ATOM   3522 C  CB    . ASP A 1 440 ? -3.42675  -34.96025 -9.86476  1.000 21.00400 ? 440 ASP A CB    1 
ATOM   3523 C  CG    . ASP A 1 440 ? -3.29871  -34.31529 -8.49775  1.000 25.83863 ? 440 ASP A CG    1 
ATOM   3524 O  OD1   . ASP A 1 440 ? -2.16871  -34.25836 -7.96675  1.000 30.51348 ? 440 ASP A OD1   1 
ATOM   3525 O  OD2   . ASP A 1 440 ? -4.32869  -33.86925 -7.95173  1.000 28.84031 ? 440 ASP A OD2   1 
ATOM   3526 N  N     . MET A 1 441 ? -1.86477  -35.09925 -13.12777 1.000 16.04219 ? 441 MET A N     1 
ATOM   3527 C  CA    . MET A 1 441 ? -1.86181  -35.85022 -14.37779 1.000 17.02424 ? 441 MET A CA    1 
ATOM   3528 C  C     . MET A 1 441 ? -0.56485  -36.63828 -14.49281 1.000 13.52324 ? 441 MET A C     1 
ATOM   3529 O  O     . MET A 1 441 ? 0.51518   -36.04534 -14.36780 1.000 13.59019 ? 441 MET A O     1 
ATOM   3530 C  CB    . MET A 1 441 ? -2.00577  -34.90419 -15.56177 1.000 18.87615 ? 441 MET A CB    1 
ATOM   3531 C  CG    . MET A 1 441 ? -1.79581  -35.52817 -16.93678 1.000 20.88667 ? 441 MET A CG    1 
ATOM   3532 S  SD    . MET A 1 441 ? -3.24285  -36.41308 -17.54780 1.000 27.52863 ? 441 MET A SD    1 
ATOM   3533 C  CE    . MET A 1 441 ? -4.56080  -35.35102 -16.94777 1.000 16.98165 ? 441 MET A CE    1 
ATOM   3534 N  N     . PRO A 1 442 ? -0.61492  -37.95628 -14.71484 1.000 17.06209 ? 442 PRO A N     1 
ATOM   3535 C  CA    . PRO A 1 442 ? 0.62404   -38.73934 -14.83187 1.000 16.73570 ? 442 PRO A CA    1 
ATOM   3536 C  C     . PRO A 1 442 ? 1.55606   -38.19236 -15.90786 1.000 17.01624 ? 442 PRO A C     1 
ATOM   3537 O  O     . PRO A 1 442 ? 1.11909   -37.59731 -16.89384 1.000 15.82782 ? 442 PRO A O     1 
ATOM   3538 C  CB    . PRO A 1 442 ? 0.12197   -40.14330 -15.18490 1.000 16.29761 ? 442 PRO A CB    1 
ATOM   3539 C  CG    . PRO A 1 442 ? -1.25503  -40.20825 -14.58789 1.000 17.14700 ? 442 PRO A CG    1 
ATOM   3540 C  CD    . PRO A 1 442 ? -1.81796  -38.81122 -14.72486 1.000 19.55698 ? 442 PRO A CD    1 
ATOM   3541 N  N     . ALA A 1 443 ? 2.85905   -38.41643 -15.71187 1.000 20.93417 ? 443 ALA A N     1 
ATOM   3542 C  CA    . ALA A 1 443 ? 3.86108   -37.82746 -16.59386 1.000 14.97989 ? 443 ALA A CA    1 
ATOM   3543 C  C     . ALA A 1 443 ? 3.76405   -38.35042 -18.02187 1.000 15.80354 ? 443 ALA A C     1 
ATOM   3544 O  O     . ALA A 1 443 ? 4.22908   -37.67542 -18.94786 1.000 15.93790 ? 443 ALA A O     1 
ATOM   3545 C  CB    . ALA A 1 443 ? 5.26307   -38.08254 -16.03787 1.000 19.08048 ? 443 ALA A CB    1 
ATOM   3546 N  N     . LYS A 1 444 ? 3.17399   -39.53339 -18.22190 1.000 15.55278 ? 444 LYS A N     1 
ATOM   3547 C  CA    . LYS A 1 444 ? 3.00895   -40.07635 -19.56591 1.000 17.93612 ? 444 LYS A CA    1 
ATOM   3548 C  C     . LYS A 1 444 ? 2.13799   -39.18628 -20.44388 1.000 14.94019 ? 444 LYS A C     1 
ATOM   3549 O  O     . LYS A 1 444 ? 2.27099   -39.22726 -21.67189 1.000 15.16011 ? 444 LYS A O     1 
ATOM   3550 C  CB    . LYS A 1 444 ? 2.41188   -41.48332 -19.48694 1.000 17.48287 ? 444 LYS A CB    1 
ATOM   3551 C  CG    . LYS A 1 444 ? 2.49884   -42.30829 -20.76796 1.000 21.66827 ? 444 LYS A CG    1 
ATOM   3552 C  CD    . LYS A 1 444 ? 1.53878   -43.48625 -20.68498 1.000 20.49915 ? 444 LYS A CD    1 
ATOM   3553 C  CE    . LYS A 1 444 ? 2.03371   -44.70725 -21.44301 0.000 22.34472 ? 444 LYS A CE    1 
ATOM   3554 N  NZ    . LYS A 1 444 ? 2.01071   -44.53922 -22.92101 0.000 22.20653 ? 444 LYS A NZ    1 
ATOM   3555 N  N     . TYR A 1 445 ? 1.25404   -38.38125 -19.84686 1.000 15.95489 ? 445 TYR A N     1 
ATOM   3556 C  CA    . TYR A 1 445 ? 0.36208   -37.51819 -20.61184 1.000 12.61295 ? 445 TYR A CA    1 
ATOM   3557 C  C     . TYR A 1 445 ? 0.42015   -36.05420 -20.18480 1.000 17.18782 ? 445 TYR A C     1 
ATOM   3558 O  O     . TYR A 1 445 ? -0.46581  -35.28115 -20.56778 1.000 16.62864 ? 445 TYR A O     1 
ATOM   3559 C  CB    . TYR A 1 445 ? -1.08895  -38.00812 -20.50784 1.000 18.31658 ? 445 TYR A CB    1 
ATOM   3560 C  CG    . TYR A 1 445 ? -1.26302  -39.50610 -20.62688 1.000 20.06494 ? 445 TYR A CG    1 
ATOM   3561 C  CD1   . TYR A 1 445 ? -1.05306  -40.15709 -21.83489 1.000 15.96405 ? 445 TYR A CD1   1 
ATOM   3562 C  CD2   . TYR A 1 445 ? -1.65406  -40.26611 -19.53189 1.000 19.76560 ? 445 TYR A CD2   1 
ATOM   3563 C  CE1   . TYR A 1 445 ? -1.21613  -41.52508 -21.94593 1.000 20.03228 ? 445 TYR A CE1   1 
ATOM   3564 C  CE2   . TYR A 1 445 ? -1.82013  -41.63310 -19.63393 1.000 18.66120 ? 445 TYR A CE2   1 
ATOM   3565 C  CZ    . TYR A 1 445 ? -1.60216  -42.25708 -20.84294 1.000 21.39980 ? 445 TYR A CZ    1 
ATOM   3566 O  OH    . TYR A 1 445 ? -1.76523  -43.62007 -20.94497 1.000 33.85892 ? 445 TYR A OH    1 
ATOM   3567 N  N     . ILE A 1 446 ? 1.42718   -35.64327 -19.40680 1.000 14.26254 ? 446 ILE A N     1 
ATOM   3568 C  CA    . ILE A 1 446 ? 1.45225   -34.26328 -18.92376 1.000 15.19709 ? 446 ILE A CA    1 
ATOM   3569 C  C     . ILE A 1 446 ? 1.72829   -33.29527 -20.06974 1.000 16.21996 ? 446 ILE A C     1 
ATOM   3570 O  O     . ILE A 1 446 ? 1.20435   -32.17524 -20.08171 1.000 14.94861 ? 446 ILE A O     1 
ATOM   3571 C  CB    . ILE A 1 446 ? 2.47126   -34.10336 -17.77577 1.000 15.48861 ? 446 ILE A CB    1 
ATOM   3572 C  CG1   . ILE A 1 446 ? 2.41434   -32.68637 -17.19273 1.000 14.18101 ? 446 ILE A CG1   1 
ATOM   3573 C  CG2   . ILE A 1 446 ? 3.88224   -34.42842 -18.24478 1.000 16.45063 ? 446 ILE A CG2   1 
ATOM   3574 C  CD1   . ILE A 1 446 ? 1.81035   -32.61337 -15.81273 1.000 14.72911 ? 446 ILE A CD1   1 
ATOM   3575 N  N     . TYR A 1 447 ? 2.52827   -33.70929 -21.05676 1.000 12.13901 ? 447 TYR A N     1 
ATOM   3576 C  CA    . TYR A 1 447 ? 2.76431   -32.88427 -22.23574 1.000 15.71160 ? 447 TYR A CA    1 
ATOM   3577 C  C     . TYR A 1 447 ? 1.67329   -33.03519 -23.28874 1.000 13.94755 ? 447 TYR A C     1 
ATOM   3578 O  O     . TYR A 1 447 ? 1.56333   -32.17716 -24.17272 1.000 13.36830 ? 447 TYR A O     1 
ATOM   3579 C  CB    . TYR A 1 447 ? 4.12529   -33.22032 -22.85175 1.000 14.26756 ? 447 TYR A CB    1 
ATOM   3580 C  CG    . TYR A 1 447 ? 5.30131   -32.77140 -22.01274 1.000 14.22413 ? 447 TYR A CG    1 
ATOM   3581 C  CD1   . TYR A 1 447 ? 5.83138   -31.49543 -22.15472 1.000 13.84984 ? 447 TYR A CD1   1 
ATOM   3582 C  CD2   . TYR A 1 447 ? 5.87927   -33.62046 -21.07977 1.000 15.77950 ? 447 TYR A CD2   1 
ATOM   3583 C  CE1   . TYR A 1 447 ? 6.90440   -31.07750 -21.38971 1.000 12.90176 ? 447 TYR A CE1   1 
ATOM   3584 C  CE2   . TYR A 1 447 ? 6.95430   -33.21153 -20.30876 1.000 17.75306 ? 447 TYR A CE2   1 
ATOM   3585 C  CZ    . TYR A 1 447 ? 7.46136   -31.93855 -20.46973 1.000 14.82303 ? 447 TYR A CZ    1 
ATOM   3586 O  OH    . TYR A 1 447 ? 8.53039   -31.52262 -19.70773 1.000 15.68923 ? 447 TYR A OH    1 
ATOM   3587 N  N     . GLU A 1 448 ? 0.87824   -34.10415 -23.22176 1.000 15.08266 ? 448 GLU A N     1 
ATOM   3588 C  CA    . GLU A 1 448 ? -0.22877  -34.33907 -24.15276 1.000 16.28666 ? 448 GLU A CA    1 
ATOM   3589 C  C     . GLU A 1 448 ? -1.45079  -34.76803 -23.35377 1.000 13.65887 ? 448 GLU A C     1 
ATOM   3590 O  O     . GLU A 1 448 ? -1.84285  -35.94101 -23.36579 1.000 23.48484 ? 448 GLU A O     1 
ATOM   3591 C  CB    . GLU A 1 448 ? 0.14117   -35.40207 -25.19079 1.000 18.14730 ? 448 GLU A CB    1 
ATOM   3592 C  CG    . GLU A 1 448 ? 1.55817   -35.30513 -25.71479 1.000 19.72234 ? 448 GLU A CG    1 
ATOM   3593 C  CD    . GLU A 1 448 ? 1.88311   -36.38112 -26.72782 1.000 19.49478 ? 448 GLU A CD    1 
ATOM   3594 O  OE1   . GLU A 1 448 ? 1.02609   -36.66306 -27.59082 1.000 25.69406 ? 448 GLU A OE1   1 
ATOM   3595 O  OE2   . GLU A 1 448 ? 2.99508   -36.94818 -26.65583 1.000 23.05702 ? 448 GLU A OE2   1 
ATOM   3596 N  N     . PRO A 1 449 ? -2.08474  -33.83302 -22.64074 1.000 16.00378 ? 449 PRO A N     1 
ATOM   3597 C  CA    . PRO A 1 449 ? -3.23876  -34.20898 -21.80575 1.000 18.57917 ? 449 PRO A CA    1 
ATOM   3598 C  C     . PRO A 1 449 ? -4.42979  -34.71890 -22.59875 1.000 16.92305 ? 449 PRO A C     1 
ATOM   3599 O  O     . PRO A 1 449 ? -5.25582  -35.45187 -22.04077 1.000 15.54331 ? 449 PRO A O     1 
ATOM   3600 C  CB    . PRO A 1 449 ? -3.57369  -32.90598 -21.06471 1.000 9.98712  ? 449 PRO A CB    1 
ATOM   3601 C  CG    . PRO A 1 449 ? -3.04564  -31.82298 -21.95269 1.000 12.09174 ? 449 PRO A CG    1 
ATOM   3602 C  CD    . PRO A 1 449 ? -1.80467  -32.38803 -22.58471 1.000 15.54387 ? 449 PRO A CD    1 
ATOM   3603 N  N     . TRP A 1 450 ? -4.54477  -34.35686 -23.88074 1.000 14.55968 ? 450 TRP A N     1 
ATOM   3604 C  CA    . TRP A 1 450 ? -5.63480  -34.86279 -24.70975 1.000 13.77857 ? 450 TRP A CA    1 
ATOM   3605 C  C     . TRP A 1 450 ? -5.44988  -36.32779 -25.07879 1.000 16.66387 ? 450 TRP A C     1 
ATOM   3606 O  O     . TRP A 1 450 ? -6.42091  -36.98073 -25.47680 1.000 21.65558 ? 450 TRP A O     1 
ATOM   3607 C  CB    . TRP A 1 450 ? -5.77077  -34.01475 -25.97773 1.000 16.37826 ? 450 TRP A CB    1 
ATOM   3608 C  CG    . TRP A 1 450 ? -4.56677  -34.06279 -26.87574 1.000 17.26282 ? 450 TRP A CG    1 
ATOM   3609 C  CD1   . TRP A 1 450 ? -4.37282  -34.89477 -27.94076 1.000 19.20745 ? 450 TRP A CD1   1 
ATOM   3610 C  CD2   . TRP A 1 450 ? -3.39273  -33.24485 -26.78772 1.000 13.25658 ? 450 TRP A CD2   1 
ATOM   3611 N  NE1   . TRP A 1 450 ? -3.15181  -34.64682 -28.51976 1.000 16.14045 ? 450 TRP A NE1   1 
ATOM   3612 C  CE2   . TRP A 1 450 ? -2.53075  -33.63787 -27.83073 1.000 15.66547 ? 450 TRP A CE2   1 
ATOM   3613 C  CE3   . TRP A 1 450 ? -2.98767  -32.21789 -25.92870 1.000 13.29877 ? 450 TRP A CE3   1 
ATOM   3614 C  CZ2   . TRP A 1 450 ? -1.28772  -33.04293 -28.03673 1.000 16.94102 ? 450 TRP A CZ2   1 
ATOM   3615 C  CZ3   . TRP A 1 450 ? -1.75465  -31.62695 -26.13569 1.000 15.29489 ? 450 TRP A CZ3   1 
ATOM   3616 C  CH2   . TRP A 1 450 ? -0.91967  -32.04097 -27.18070 1.000 15.95793 ? 450 TRP A CH2   1 
ATOM   3617 N  N     . THR A 1 451 ? -4.23291  -36.85685 -24.95880 1.000 18.73210 ? 451 THR A N     1 
ATOM   3618 C  CA    . THR A 1 451 ? -3.96398  -38.26186 -25.23484 1.000 19.80168 ? 451 THR A CA    1 
ATOM   3619 C  C     . THR A 1 451 ? -4.24302  -39.16687 -24.04086 1.000 20.26531 ? 451 THR A C     1 
ATOM   3620 O  O     . THR A 1 451 ? -4.17208  -40.39187 -24.18289 1.000 15.28432 ? 451 THR A O     1 
ATOM   3621 C  CB    . THR A 1 451 ? -2.50699  -38.45492 -25.67885 1.000 19.23730 ? 451 THR A CB    1 
ATOM   3622 O  OG1   . THR A 1 451 ? -1.62497  -38.09499 -24.60884 1.000 18.25066 ? 451 THR A OG1   1 
ATOM   3623 C  CG2   . THR A 1 451 ? -2.19195  -37.59691 -26.89583 1.000 22.08520 ? 451 THR A CG2   1 
ATOM   3624 N  N     . ALA A 1 452 ? -4.54899  -38.60089 -22.87584 1.000 22.21722 ? 452 ALA A N     1 
ATOM   3625 C  CA    . ALA A 1 452 ? -4.82902  -39.41890 -21.70486 1.000 20.44526 ? 452 ALA A CA    1 
ATOM   3626 C  C     . ALA A 1 452 ? -6.21805  -40.04283 -21.81887 1.000 19.80943 ? 452 ALA A C     1 
ATOM   3627 O  O     . ALA A 1 452 ? -7.14102  -39.41177 -22.34285 1.000 21.30426 ? 452 ALA A O     1 
ATOM   3628 C  CB    . ALA A 1 452 ? -4.74397  -38.58293 -20.43184 1.000 18.05630 ? 452 ALA A CB    1 
ATOM   3629 N  N     . PRO A 1 453 ? -6.39411  -41.27683 -21.34690 1.000 18.05366 ? 453 PRO A N     1 
ATOM   3630 C  CA    . PRO A 1 453 ? -7.73914  -41.85976 -21.31291 1.000 20.04847 ? 453 PRO A CA    1 
ATOM   3631 C  C     . PRO A 1 453 ? -8.66110  -41.03074 -20.43188 1.000 17.14596 ? 453 PRO A C     1 
ATOM   3632 O  O     . PRO A 1 453 ? -8.22306  -40.37278 -19.48587 1.000 15.59948 ? 453 PRO A O     1 
ATOM   3633 C  CB    . PRO A 1 453 ? -7.50821  -43.25879 -20.72894 1.000 21.85501 ? 453 PRO A CB    1 
ATOM   3634 C  CG    . PRO A 1 453 ? -6.05823  -43.54985 -20.99395 1.000 20.87181 ? 453 PRO A CG    1 
ATOM   3635 C  CD    . PRO A 1 453 ? -5.36616  -42.22289 -20.87893 1.000 19.65902 ? 453 PRO A CD    1 
ATOM   3636 N  N     . LEU A 1 454 ? -9.95610  -41.06066 -20.76088 1.000 16.53517 ? 454 LEU A N     1 
ATOM   3637 C  CA    . LEU A 1 454 ? -10.92406 -40.26163 -20.01286 1.000 16.81864 ? 454 LEU A CA    1 
ATOM   3638 C  C     . LEU A 1 454 ? -10.97507 -40.66966 -18.54587 1.000 19.54418 ? 454 LEU A C     1 
ATOM   3639 O  O     . LEU A 1 454 ? -11.23603 -39.82867 -17.67685 1.000 23.21394 ? 454 LEU A O     1 
ATOM   3640 C  CB    . LEU A 1 454 ? -12.30907 -40.37755 -20.65386 1.000 17.90875 ? 454 LEU A CB    1 
ATOM   3641 C  CG    . LEU A 1 454 ? -13.40402 -39.47050 -20.08583 1.000 13.27682 ? 454 LEU A CG    1 
ATOM   3642 C  CD1   . LEU A 1 454 ? -12.92395 -38.02853 -20.03280 1.000 19.84692 ? 454 LEU A CD1   1 
ATOM   3643 C  CD2   . LEU A 1 454 ? -14.69203 -39.57542 -20.89083 1.000 20.29635 ? 454 LEU A CD2   1 
ATOM   3644 N  N     . GLU A 1 455 ? -10.73114 -41.94968 -18.25190 1.000 15.49506 ? 455 GLU A N     1 
ATOM   3645 C  CA    . GLU A 1 455 ? -10.62415 -42.38772 -16.86391 1.000 18.26645 ? 455 GLU A CA    1 
ATOM   3646 C  C     . GLU A 1 455 ? -9.46812  -41.69080 -16.15790 1.000 16.32805 ? 455 GLU A C     1 
ATOM   3647 O  O     . GLU A 1 455 ? -9.59609  -41.27082 -15.00189 1.000 18.57371 ? 455 GLU A O     1 
ATOM   3648 C  CB    . GLU A 1 455 ? -10.44823 -43.90773 -16.80595 1.000 17.94035 ? 455 GLU A CB    1 
ATOM   3649 C  CG    . GLU A 1 455 ? -9.93325  -44.43579 -15.47196 1.000 16.92903 ? 455 GLU A CG    1 
ATOM   3650 C  CD    . GLU A 1 455 ? -11.02826 -44.59976 -14.43396 0.000 17.85834 ? 455 GLU A CD    1 
ATOM   3651 O  OE1   . GLU A 1 455 ? -11.79631 -45.57872 -14.53298 0.000 17.57493 ? 455 GLU A OE1   1 
ATOM   3652 O  OE2   . GLU A 1 455 ? -11.12021 -43.75277 -13.51894 0.000 18.46460 ? 455 GLU A OE2   1 
ATOM   3653 N  N     . VAL A 1 456 ? -8.33211  -41.54884 -16.84290 1.000 16.46765 ? 456 VAL A N     1 
ATOM   3654 C  CA    . VAL A 1 456 ? -7.17008  -40.90891 -16.23689 1.000 18.61754 ? 456 VAL A CA    1 
ATOM   3655 C  C     . VAL A 1 456 ? -7.40300  -39.41190 -16.08685 1.000 17.16380 ? 456 VAL A C     1 
ATOM   3656 O  O     . VAL A 1 456 ? -7.00096  -38.80495 -15.08684 1.000 14.21286 ? 456 VAL A O     1 
ATOM   3657 C  CB    . VAL A 1 456 ? -5.90609  -41.20995 -17.06390 1.000 16.83101 ? 456 VAL A CB    1 
ATOM   3658 C  CG1   . VAL A 1 456 ? -4.67806  -40.57403 -16.42189 1.000 14.39171 ? 456 VAL A CG1   1 
ATOM   3659 C  CG2   . VAL A 1 456 ? -5.71817  -42.71196 -17.20994 1.000 15.74828 ? 456 VAL A CG2   1 
ATOM   3660 N  N     . GLN A 1 457 ? -8.05797  -38.79385 -17.07483 1.000 14.38325 ? 457 GLN A N     1 
ATOM   3661 C  CA    . GLN A 1 457 ? -8.34790  -37.36583 -16.99280 1.000 17.69429 ? 457 GLN A CA    1 
ATOM   3662 C  C     . GLN A 1 457 ? -9.25588  -37.05681 -15.80779 1.000 18.13882 ? 457 GLN A C     1 
ATOM   3663 O  O     . GLN A 1 457 ? -9.06883  -36.04484 -15.12177 1.000 16.85251 ? 457 GLN A O     1 
ATOM   3664 C  CB    . GLN A 1 457 ? -8.98588  -36.87677 -18.29579 1.000 16.36924 ? 457 GLN A CB    1 
ATOM   3665 C  CG    . GLN A 1 457 ? -8.14390  -37.09678 -19.54579 1.000 18.68547 ? 457 GLN A CG    1 
ATOM   3666 C  CD    . GLN A 1 457 ? -8.80787  -36.55872 -20.80078 1.000 19.68582 ? 457 GLN A CD    1 
ATOM   3667 O  OE1   . GLN A 1 457 ? -9.75383  -35.77067 -20.73276 1.000 19.12110 ? 457 GLN A OE1   1 
ATOM   3668 N  NE2   . GLN A 1 457 ? -8.31590  -36.98672 -21.95779 1.000 17.84010 ? 457 GLN A NE2   1 
ATOM   3669 N  N     . ARG A 1 458 ? -10.24879 -37.91495 -15.55684 1.000 18.51414 ? 458 ARG A N     1 
ATOM   3670 C  CA    . ARG A 1 458 ? -11.13302 -37.71171 -14.41291 1.000 18.74815 ? 458 ARG A CA    1 
ATOM   3671 C  C     . ARG A 1 458 ? -10.40744 -37.97335 -13.09828 1.000 18.16239 ? 458 ARG A C     1 
ATOM   3672 O  O     . ARG A 1 458 ? -10.67395 -37.30379 -12.09341 1.000 19.47491 ? 458 ARG A O     1 
ATOM   3673 C  CB    . ARG A 1 458 ? -12.36665 -38.60862 -14.53586 1.000 20.37205 ? 458 ARG A CB    1 
ATOM   3674 C  CG    . ARG A 1 458 ? -13.29525 -38.22703 -15.67813 1.000 17.66302 ? 458 ARG A CG    1 
ATOM   3675 C  CD    . ARG A 1 458 ? -14.36631 -39.27902 -15.91002 0.000 18.60685 ? 458 ARG A CD    1 
ATOM   3676 N  NE    . ARG A 1 458 ? -15.07997 -39.04511 -17.15988 0.000 18.58503 ? 458 ARG A NE    1 
ATOM   3677 C  CZ    . ARG A 1 458 ? -16.21201 -38.36228 -17.26253 0.000 18.50620 ? 458 ARG A CZ    1 
ATOM   3678 N  NH1   . ARG A 1 458 ? -16.80785 -37.84779 -16.19947 0.000 18.60923 ? 458 ARG A NH1   1 
ATOM   3679 N  NH2   . ARG A 1 458 ? -16.76040 -38.19171 -18.46232 0.000 18.43826 ? 458 ARG A NH2   1 
ATOM   3680 N  N     . LYS A 1 459 ? -9.48996  -38.94487 -13.08483 1.000 21.87244 ? 459 LYS A N     1 
ATOM   3681 C  CA    . LYS A 1 459 ? -8.71997  -39.22293 -11.87784 1.000 17.55060 ? 459 LYS A CA    1 
ATOM   3682 C  C     . LYS A 1 459 ? -7.87791  -38.02099 -11.47582 1.000 13.88250 ? 459 LYS A C     1 
ATOM   3683 O  O     . LYS A 1 459 ? -7.70589  -37.74402 -10.28281 1.000 17.79231 ? 459 LYS A O     1 
ATOM   3684 C  CB    . LYS A 1 459 ? -7.83104  -40.44997 -12.09087 1.000 23.67772 ? 459 LYS A CB    1 
ATOM   3685 C  CG    . LYS A 1 459 ? -8.57010  -41.77194 -11.96290 1.000 24.17298 ? 459 LYS A CG    1 
ATOM   3686 C  CD    . LYS A 1 459 ? -8.97711  -42.03095 -10.52191 0.000 21.26770 ? 459 LYS A CD    1 
ATOM   3687 C  CE    . LYS A 1 459 ? -10.13216 -43.01690 -10.43393 0.000 21.05733 ? 459 LYS A CE    1 
ATOM   3688 N  NZ    . LYS A 1 459 ? -9.82423  -44.32090 -11.08596 0.000 20.48940 ? 459 LYS A NZ    1 
ATOM   3689 N  N     . ALA A 1 460 ? -7.35288  -37.28799 -12.45680 1.000 17.74419 ? 460 ALA A N     1 
ATOM   3690 C  CA    . ALA A 1 460 ? -6.48982  -36.14704 -12.18778 1.000 15.99267 ? 460 ALA A CA    1 
ATOM   3691 C  C     . ALA A 1 460 ? -7.25975  -34.85101 -11.98174 1.000 17.19701 ? 460 ALA A C     1 
ATOM   3692 O  O     . ALA A 1 460 ? -6.69170  -33.88905 -11.45472 1.000 19.52846 ? 460 ALA A O     1 
ATOM   3693 C  CB    . ALA A 1 460 ? -5.48881  -35.96206 -13.33078 1.000 18.85816 ? 460 ALA A CB    1 
ATOM   3694 N  N     . GLY A 1 461 ? -8.53075  -34.80593 -12.36674 1.000 17.56808 ? 461 GLY A N     1 
ATOM   3695 C  CA    . GLY A 1 461 ? -9.28569  -33.57290 -12.27371 1.000 22.19034 ? 461 GLY A CA    1 
ATOM   3696 C  C     . GLY A 1 461 ? -8.93664  -32.58489 -13.35968 1.000 17.02098 ? 461 GLY A C     1 
ATOM   3697 O  O     . GLY A 1 461 ? -8.91358  -31.37290 -13.10866 1.000 21.16947 ? 461 GLY A O     1 
ATOM   3698 N  N     . CYS A 1 462 ? -8.64567  -33.07587 -14.57070 1.000 22.27883 ? 462 CYS A N     1 
ATOM   3699 C  CA    . CYS A 1 462 ? -8.26463  -32.23187 -15.68468 1.000 19.79877 ? 462 CYS A CA    1 
ATOM   3700 C  C     . CYS A 1 462 ? -8.86967  -32.80981 -16.96569 1.000 20.68756 ? 462 CYS A C     1 
ATOM   3701 O  O     . CYS A 1 462 ? -8.17570  -33.32882 -17.83970 1.000 21.16592 ? 462 CYS A O     1 
ATOM   3702 C  CB    . CYS A 1 462 ? -6.74563  -32.10794 -15.79268 1.000 22.65409 ? 462 CYS A CB    1 
ATOM   3703 S  SG    . CYS A 1 462 ? -6.23556  -30.72294 -16.81265 1.000 18.45790 ? 462 CYS A SG    1 
ATOM   3704 N  N     . VAL A 1 463 ? -10.19266 -32.72074 -17.07668 1.000 17.37173 ? 463 VAL A N     1 
ATOM   3705 C  CA    . VAL A 1 463 ? -10.87369 -33.17367 -18.28369 1.000 16.95985 ? 463 VAL A CA    1 
ATOM   3706 C  C     . VAL A 1 463 ? -10.59565 -32.18166 -19.40467 1.000 16.48828 ? 463 VAL A C     1 
ATOM   3707 O  O     . VAL A 1 463 ? -10.93659 -30.99765 -19.30264 1.000 19.68154 ? 463 VAL A O     1 
ATOM   3708 C  CB    . VAL A 1 463 ? -12.37870 -33.32760 -18.04169 1.000 18.13265 ? 463 VAL A CB    1 
ATOM   3709 C  CG1   . VAL A 1 463 ? -13.08372 -33.63854 -19.34969 1.000 14.99845 ? 463 VAL A CG1   1 
ATOM   3710 C  CG2   . VAL A 1 463 ? -12.63775 -34.41961 -17.01571 1.000 24.09001 ? 463 VAL A CG2   1 
ATOM   3711 N  N     . VAL A 1 464 ? -9.98468  -32.66367 -20.48468 1.000 18.74956 ? 464 VAL A N     1 
ATOM   3712 C  CA    . VAL A 1 464 ? -9.63164  -31.78966 -21.59866 1.000 18.49539 ? 464 VAL A CA    1 
ATOM   3713 C  C     . VAL A 1 464 ? -10.90461 -31.24958 -22.23565 1.000 16.37022 ? 464 VAL A C     1 
ATOM   3714 O  O     . VAL A 1 464 ? -11.76765 -32.01352 -22.68466 1.000 15.66438 ? 464 VAL A O     1 
ATOM   3715 C  CB    . VAL A 1 464 ? -8.76468  -32.52768 -22.62368 1.000 15.49062 ? 464 VAL A CB    1 
ATOM   3716 C  CG1   . VAL A 1 464 ? -8.60064  -31.67766 -23.87366 1.000 13.79184 ? 464 VAL A CG1   1 
ATOM   3717 C  CG2   . VAL A 1 464 ? -7.41069  -32.85276 -22.02070 1.000 13.56289 ? 464 VAL A CG2   1 
ATOM   3718 N  N     . GLY A 1 465 ? -11.02554 -29.92057 -22.27861 1.000 15.88666 ? 465 GLY A N     1 
ATOM   3719 C  CA    . GLY A 1 465 ? -12.20051 -29.24350 -22.78159 1.000 13.24500 ? 465 GLY A CA    1 
ATOM   3720 C  C     . GLY A 1 465 ? -13.02647 -28.58548 -21.69457 1.000 16.63196 ? 465 GLY A C     1 
ATOM   3721 O  O     . GLY A 1 465 ? -13.76143 -27.63144 -21.97755 1.000 23.51728 ? 465 GLY A O     1 
ATOM   3722 N  N     . ARG A 1 466 ? -12.92311 -29.07024 -20.45785 1.000 14.03633 ? 466 ARG A N     1 
ATOM   3723 C  CA    . ARG A 1 466 ? -13.62070 -28.51166 -19.30513 1.000 14.27100 ? 466 ARG A CA    1 
ATOM   3724 C  C     . ARG A 1 466 ? -12.68180 -27.80765 -18.34137 1.000 17.25126 ? 466 ARG A C     1 
ATOM   3725 O  O     . ARG A 1 466 ? -12.94042 -26.66376 -17.94914 1.000 11.91672 ? 466 ARG A O     1 
ATOM   3726 C  CB    . ARG A 1 466 ? -14.38495 -29.62657 -18.57226 1.000 20.06389 ? 466 ARG A CB    1 
ATOM   3727 C  CG    . ARG A 1 466 ? -15.14013 -29.16826 -17.33323 1.000 23.82118 ? 466 ARG A CG    1 
ATOM   3728 C  CD    . ARG A 1 466 ? -15.86301 -30.33165 -16.66824 1.000 27.03861 ? 466 ARG A CD    1 
ATOM   3729 N  NE    . ARG A 1 466 ? -14.93089 -31.31134 -16.12383 1.000 32.03969 ? 466 ARG A NE    1 
ATOM   3730 C  CZ    . ARG A 1 466 ? -14.43162 -31.26559 -14.89679 1.000 35.77356 ? 466 ARG A CZ    1 
ATOM   3731 N  NH1   . ARG A 1 466 ? -14.76122 -30.30077 -14.05321 1.000 29.19596 ? 466 ARG A NH1   1 
ATOM   3732 N  NH2   . ARG A 1 466 ? -13.57802 -32.20931 -14.50783 1.000 33.17912 ? 466 ARG A NH2   1 
ATOM   3733 N  N     . ASP A 1 467 ? -11.58645 -28.46265 -17.94558 1.000 20.76742 ? 467 ASP A N     1 
ATOM   3734 C  CA    . ASP A 1 467 ? -10.61642 -27.88572 -17.02357 1.000 17.42238 ? 467 ASP A CA    1 
ATOM   3735 C  C     . ASP A 1 467 ? -9.38839  -27.32176 -17.71956 1.000 12.99586 ? 467 ASP A C     1 
ATOM   3736 O  O     . ASP A 1 467 ? -8.81534  -26.33880 -17.23754 1.000 12.19332 ? 467 ASP A O     1 
ATOM   3737 C  CB    . ASP A 1 467 ? -10.16847 -28.93276 -15.99959 1.000 16.70188 ? 467 ASP A CB    1 
ATOM   3738 C  CG    . ASP A 1 467 ? -11.32950 -29.53772 -15.23760 1.000 19.39356 ? 467 ASP A CG    1 
ATOM   3739 O  OD1   . ASP A 1 467 ? -12.18446 -28.77169 -14.74358 1.000 17.06750 ? 467 ASP A OD1   1 
ATOM   3740 O  OD2   . ASP A 1 467 ? -11.38756 -30.78072 -15.13863 1.000 23.39747 ? 467 ASP A OD2   1 
ATOM   3741 N  N     . TYR A 1 468 ? -8.96243  -27.92176 -18.83057 1.000 14.08434 ? 468 TYR A N     1 
ATOM   3742 C  CA    . TYR A 1 468 ? -7.83341  -27.43780 -19.61057 1.000 10.77025 ? 468 TYR A CA    1 
ATOM   3743 C  C     . TYR A 1 468 ? -8.21542  -27.54374 -21.08057 1.000 12.97653 ? 468 TYR A C     1 
ATOM   3744 O  O     . TYR A 1 468 ? -8.81547  -28.54970 -21.49059 1.000 13.26875 ? 468 TYR A O     1 
ATOM   3745 C  CB    . TYR A 1 468 ? -6.56145  -28.24487 -19.32559 1.000 13.74655 ? 468 TYR A CB    1 
ATOM   3746 C  CG    . TYR A 1 468 ? -5.32042  -27.70891 -19.99958 1.000 13.97641 ? 468 TYR A CG    1 
ATOM   3747 C  CD1   . TYR A 1 468 ? -4.64736  -26.60496 -19.48756 1.000 11.02254 ? 468 TYR A CD1   1 
ATOM   3748 C  CD2   . TYR A 1 468 ? -4.81546  -28.31291 -21.14160 1.000 14.74236 ? 468 TYR A CD2   1 
ATOM   3749 C  CE1   . TYR A 1 468 ? -3.50934  -26.11400 -20.10655 1.000 11.55385 ? 468 TYR A CE1   1 
ATOM   3750 C  CE2   . TYR A 1 468 ? -3.68144  -27.83396 -21.76259 1.000 12.03186 ? 468 TYR A CE2   1 
ATOM   3751 C  CZ    . TYR A 1 468 ? -3.03238  -26.73600 -21.24357 1.000 10.03746 ? 468 TYR A CZ    1 
ATOM   3752 O  OH    . TYR A 1 468 ? -1.90736  -26.26704 -21.87656 1.000 9.42098  ? 468 TYR A OH    1 
ATOM   3753 N  N     . PRO A 1 469 ? -7.90737  -26.53374 -21.89155 1.000 12.22199 ? 469 PRO A N     1 
ATOM   3754 C  CA    . PRO A 1 469 ? -8.37438  -26.54168 -23.28054 1.000 13.78130 ? 469 PRO A CA    1 
ATOM   3755 C  C     . PRO A 1 469 ? -7.66643  -27.59370 -24.12157 1.000 13.90249 ? 469 PRO A C     1 
ATOM   3756 O  O     . PRO A 1 469 ? -6.55645  -28.03976 -23.81959 1.000 12.93663 ? 469 PRO A O     1 
ATOM   3757 C  CB    . PRO A 1 469 ? -8.03831  -25.13069 -23.77451 1.000 12.99472 ? 469 PRO A CB    1 
ATOM   3758 C  CG    . PRO A 1 469 ? -6.87928  -24.72477 -22.94851 1.000 10.52694 ? 469 PRO A CG    1 
ATOM   3759 C  CD    . PRO A 1 469 ? -7.14131  -25.31378 -21.58552 1.000 11.47053 ? 469 PRO A CD    1 
ATOM   3760 N  N     . ALA A 1 470 ? -8.34646  -27.98864 -25.19858 1.000 11.96343 ? 470 ALA A N     1 
ATOM   3761 C  CA    . ALA A 1 470 ? -7.80550  -28.83864 -26.24460 1.000 12.80607 ? 470 ALA A CA    1 
ATOM   3762 C  C     . ALA A 1 470 ? -6.80547  -28.05967 -27.08759 1.000 13.85397 ? 470 ALA A C     1 
ATOM   3763 O  O     . ALA A 1 470 ? -6.88141  -26.83267 -27.17356 1.000 12.58546 ? 470 ALA A O     1 
ATOM   3764 C  CB    . ALA A 1 470 ? -8.93753  -29.36856 -27.11961 1.000 11.08130 ? 470 ALA A CB    1 
ATOM   3765 N  N     . PRO A 1 471 ? -5.84651  -28.74471 -27.71161 1.000 14.75895 ? 471 PRO A N     1 
ATOM   3766 C  CA    . PRO A 1 471 ? -4.87447  -28.03474 -28.55259 1.000 12.42957 ? 471 PRO A CA    1 
ATOM   3767 C  C     . PRO A 1 471 ? -5.56844  -27.31167 -29.69857 1.000 12.22799 ? 471 PRO A C     1 
ATOM   3768 O  O     . PRO A 1 471 ? -6.32647  -27.91062 -30.46258 1.000 13.51741 ? 471 PRO A O     1 
ATOM   3769 C  CB    . PRO A 1 471 ? -3.95253  -29.15377 -29.05662 1.000 12.56783 ? 471 PRO A CB    1 
ATOM   3770 C  CG    . PRO A 1 471 ? -4.73159  -30.40673 -28.88865 1.000 12.91562 ? 471 PRO A CG    1 
ATOM   3771 C  CD    . PRO A 1 471 ? -5.57758  -30.19072 -27.67064 1.000 18.07079 ? 471 PRO A CD    1 
ATOM   3772 N  N     . ILE A 1 472 ? -5.30238  -26.00668 -29.80754 1.000 13.63495 ? 472 ILE A N     1 
ATOM   3773 C  CA    . ILE A 1 472 ? -5.96634  -25.18663 -30.81852 1.000 15.98355 ? 472 ILE A CA    1 
ATOM   3774 C  C     . ILE A 1 472 ? -5.57837  -25.62861 -32.22153 1.000 15.93116 ? 472 ILE A C     1 
ATOM   3775 O  O     . ILE A 1 472 ? -6.35336  -25.45455 -33.16953 1.000 19.91388 ? 472 ILE A O     1 
ATOM   3776 C  CB    . ILE A 1 472 ? -5.65126  -23.69365 -30.59749 1.000 17.17983 ? 472 ILE A CB    1 
ATOM   3777 C  CG1   . ILE A 1 472 ? -4.13625  -23.46473 -30.55749 1.000 14.77638 ? 472 ILE A CG1   1 
ATOM   3778 C  CG2   . ILE A 1 472 ? -6.31923  -23.18564 -29.32947 1.000 16.86353 ? 472 ILE A CG2   1 
ATOM   3779 C  CD1   . ILE A 1 472 ? -3.73518  -22.00874 -30.61246 1.000 13.76094 ? 472 ILE A CD1   1 
ATOM   3780 N  N     . VAL A 1 473 ? -4.37739  -26.18767 -32.38355 1.000 13.81838 ? 473 VAL A N     1 
ATOM   3781 C  CA    . VAL A 1 473 ? -3.91643  -26.71666 -33.65857 1.000 16.98511 ? 473 VAL A CA    1 
ATOM   3782 C  C     . VAL A 1 473 ? -3.24949  -28.06470 -33.42360 1.000 15.14835 ? 473 VAL A C     1 
ATOM   3783 O  O     . VAL A 1 473 ? -2.80151  -28.38275 -32.32061 1.000 15.08333 ? 473 VAL A O     1 
ATOM   3784 C  CB    . VAL A 1 473 ? -2.93238  -25.76570 -34.37455 1.000 13.41228 ? 473 VAL A CB    1 
ATOM   3785 C  CG1   . VAL A 1 473 ? -3.59231  -24.42866 -34.68451 1.000 18.97864 ? 473 VAL A CG1   1 
ATOM   3786 C  CG2   . VAL A 1 473 ? -1.67537  -25.57478 -33.53455 1.000 17.98388 ? 473 VAL A CG2   1 
ATOM   3787 N  N     . ASP A 1 474 ? -3.19654  -28.86268 -34.48662 1.000 16.76018 ? 474 ASP A N     1 
ATOM   3788 C  CA    . ASP A 1 474 ? -2.35660  -30.05072 -34.52665 1.000 20.80745 ? 474 ASP A CA    1 
ATOM   3789 C  C     . ASP A 1 474 ? -0.97458  -29.62778 -35.01165 1.000 18.13741 ? 474 ASP A C     1 
ATOM   3790 O  O     . ASP A 1 474 ? -0.84255  -29.06576 -36.10563 1.000 17.56674 ? 474 ASP A O     1 
ATOM   3791 C  CB    . ASP A 1 474 ? -2.95966  -31.11167 -35.44367 1.000 20.96600 ? 474 ASP A CB    1 
ATOM   3792 C  CG    . ASP A 1 474 ? -2.14972  -32.39071 -35.46771 1.000 25.68000 ? 474 ASP A CG    1 
ATOM   3793 O  OD1   . ASP A 1 474 ? -1.20072  -32.51578 -34.66271 1.000 27.99374 ? 474 ASP A OD1   1 
ATOM   3794 O  OD2   . ASP A 1 474 ? -2.46177  -33.27267 -36.29373 1.000 26.15535 ? 474 ASP A OD2   1 
ATOM   3795 N  N     . HIS A 1 475 ? 0.04841   -29.88685 -34.19366 1.000 19.96251 ? 475 HIS A N     1 
ATOM   3796 C  CA    . HIS A 1 475 ? 1.39043   -29.40591 -34.51265 1.000 17.60703 ? 475 HIS A CA    1 
ATOM   3797 C  C     . HIS A 1 475 ? 1.87540   -29.95890 -35.84566 1.000 16.27521 ? 475 HIS A C     1 
ATOM   3798 O  O     . HIS A 1 475 ? 2.43843   -29.22691 -36.66565 1.000 18.94562 ? 475 HIS A O     1 
ATOM   3799 C  CB    . HIS A 1 475 ? 2.37242   -29.77699 -33.40366 1.000 19.47893 ? 475 HIS A CB    1 
ATOM   3800 C  CG    . HIS A 1 475 ? 3.79344   -29.44205 -33.73266 1.000 15.15616 ? 475 HIS A CG    1 
ATOM   3801 N  ND1   . HIS A 1 475 ? 4.26550   -28.14707 -33.75363 1.000 12.84981 ? 475 HIS A ND1   1 
ATOM   3802 C  CD2   . HIS A 1 475 ? 4.83939   -30.23110 -34.07468 1.000 16.88893 ? 475 HIS A CD2   1 
ATOM   3803 C  CE1   . HIS A 1 475 ? 5.54550   -28.15313 -34.08264 1.000 13.04216 ? 475 HIS A CE1   1 
ATOM   3804 N  NE2   . HIS A 1 475 ? 5.91744   -29.40515 -34.28367 1.000 17.35861 ? 475 HIS A NE2   1 
ATOM   3805 N  N     . ALA A 1 476 ? 1.66133   -31.25689 -36.07469 1.000 16.92056 ? 476 ALA A N     1 
ATOM   3806 C  CA    . ALA A 1 476 ? 2.13330   -31.89988 -37.29771 1.000 15.35270 ? 476 ALA A CA    1 
ATOM   3807 C  C     . ALA A 1 476 ? 1.61133   -31.19283 -38.54069 1.000 18.19035 ? 476 ALA A C     1 
ATOM   3808 O  O     . ALA A 1 476 ? 2.33933   -31.03784 -39.52869 1.000 20.17770 ? 476 ALA A O     1 
ATOM   3809 C  CB    . ALA A 1 476 ? 1.71822   -33.37186 -37.30574 1.000 18.11326 ? 476 ALA A CB    1 
ATOM   3810 N  N     . VAL A 1 477 ? 0.35735   -30.74776 -38.50868 1.000 18.60492 ? 477 VAL A N     1 
ATOM   3811 C  CA    . VAL A 1 477 ? -0.22262  -30.07771 -39.66666 1.000 18.64076 ? 477 VAL A CA    1 
ATOM   3812 C  C     . VAL A 1 477 ? 0.19645   -28.61573 -39.70663 1.000 18.63250 ? 477 VAL A C     1 
ATOM   3813 O  O     . VAL A 1 477 ? 0.61648   -28.10373 -40.75162 1.000 20.92008 ? 477 VAL A O     1 
ATOM   3814 C  CB    . VAL A 1 477 ? -1.75463  -30.21963 -39.65366 1.000 18.99992 ? 477 VAL A CB    1 
ATOM   3815 C  CG1   . VAL A 1 477 ? -2.34161  -29.71057 -40.96364 1.000 22.52610 ? 477 VAL A CG1   1 
ATOM   3816 C  CG2   . VAL A 1 477 ? -2.14870  -31.66362 -39.40169 1.000 21.90495 ? 477 VAL A CG2   1 
ATOM   3817 N  N     . ALA A 1 478 ? 0.08449   -27.92275 -38.56961 1.000 13.55863 ? 478 ALA A N     1 
ATOM   3818 C  CA    . ALA A 1 478 ? 0.41657   -26.50277 -38.52858 1.000 14.16552 ? 478 ALA A CA    1 
ATOM   3819 C  C     . ALA A 1 478 ? 1.89558   -26.26084 -38.79958 1.000 17.74088 ? 478 ALA A C     1 
ATOM   3820 O  O     . ALA A 1 478 ? 2.25663   -25.23484 -39.38755 1.000 15.29372 ? 478 ALA A O     1 
ATOM   3821 C  CB    . ALA A 1 478 ? 0.01360   -25.90978 -37.17756 1.000 14.47005 ? 478 ALA A CB    1 
ATOM   3822 N  N     . SER A 1 479 ? 2.76253   -27.19289 -38.39260 1.000 13.90703 ? 479 SER A N     1 
ATOM   3823 C  CA    . SER A 1 479 ? 4.19054   -27.03796 -38.65961 1.000 18.22301 ? 479 SER A CA    1 
ATOM   3824 C  C     . SER A 1 479 ? 4.49752   -27.19094 -40.14361 1.000 17.08505 ? 479 SER A C     1 
ATOM   3825 O  O     . SER A 1 479 ? 5.26656   -26.40496 -40.70759 1.000 16.93225 ? 479 SER A O     1 
ATOM   3826 C  CB    . SER A 1 479 ? 4.99649   -28.04802 -37.84463 1.000 17.70209 ? 479 SER A CB    1 
ATOM   3827 O  OG    . SER A 1 479 ? 4.67442   -29.37399 -38.22566 1.000 22.41902 ? 479 SER A OG    1 
ATOM   3828 N  N     . LYS A 1 480 ? 3.91247   -28.19889 -40.79563 1.000 19.12253 ? 480 LYS A N     1 
ATOM   3829 C  CA    . LYS A 1 480 ? 4.16046   -28.39087 -42.21864 1.000 21.12320 ? 480 LYS A CA    1 
ATOM   3830 C  C     . LYS A 1 480 ? 3.51751   -27.31182 -43.07861 1.000 19.59400 ? 480 LYS A C     1 
ATOM   3831 O  O     . LYS A 1 480 ? 3.81351   -27.24080 -44.27561 1.000 27.15500 ? 480 LYS A O     1 
ATOM   3832 C  CB    . LYS A 1 480 ? 3.65738   -29.76283 -42.66867 1.000 21.12818 ? 480 LYS A CB    1 
ATOM   3833 C  CG    . LYS A 1 480 ? 4.42033   -30.92989 -42.06570 1.000 30.59306 ? 480 LYS A CG    1 
ATOM   3834 C  CD    . LYS A 1 480 ? 3.87626   -32.26485 -42.55573 1.000 32.90051 ? 480 LYS A CD    1 
ATOM   3835 C  CE    . LYS A 1 480 ? 4.66020   -33.42890 -41.96676 0.000 32.66974 ? 480 LYS A CE    1 
ATOM   3836 N  NZ    . LYS A 1 480 ? 4.12913   -34.74986 -42.40779 0.000 34.40712 ? 480 LYS A NZ    1 
ATOM   3837 N  N     . ALA A 1 481 ? 2.64555   -26.48179 -42.50959 1.000 20.71144 ? 481 ALA A N     1 
ATOM   3838 C  CA    . ALA A 1 481 ? 2.04960   -25.38774 -43.26256 1.000 20.34673 ? 481 ALA A CA    1 
ATOM   3839 C  C     . ALA A 1 481 ? 2.82667   -24.09078 -43.10353 1.000 20.41865 ? 481 ALA A C     1 
ATOM   3840 O  O     . ALA A 1 481 ? 2.90771   -23.30576 -44.05451 1.000 25.95745 ? 481 ALA A O     1 
ATOM   3841 C  CB    . ALA A 1 481 ? 0.59662   -25.17468 -42.82755 1.000 19.32446 ? 481 ALA A CB    1 
ATOM   3842 N  N     . CYS A 1 482 ? 3.39369   -23.84684 -41.91753 1.000 20.10692 ? 482 CYS A N     1 
ATOM   3843 C  CA    . CYS A 1 482 ? 4.22875   -22.66588 -41.71950 1.000 17.94318 ? 482 CYS A CA    1 
ATOM   3844 C  C     . CYS A 1 482 ? 5.54374   -22.79093 -42.47951 1.000 18.37613 ? 482 CYS A C     1 
ATOM   3845 O  O     . CYS A 1 482 ? 6.01878   -21.81494 -43.07149 1.000 19.15751 ? 482 CYS A O     1 
ATOM   3846 C  CB    . CYS A 1 482 ? 4.47876   -22.45393 -40.22650 1.000 16.18729 ? 482 CYS A CB    1 
ATOM   3847 S  SG    . CYS A 1 482 ? 2.98579   -22.08788 -39.27148 1.000 13.51486 ? 482 CYS A SG    1 
ATOM   3848 N  N     . ILE A 1 483 ? 6.14368   -23.98396 -42.47354 1.000 17.26637 ? 483 ILE A N     1 
ATOM   3849 C  CA    . ILE A 1 483 ? 7.39666   -24.20301 -43.19155 1.000 18.35421 ? 483 ILE A CA    1 
ATOM   3850 C  C     . ILE A 1 483 ? 7.20367   -23.96997 -44.68454 1.000 20.88853 ? 483 ILE A C     1 
ATOM   3851 O  O     . ILE A 1 483 ? 8.02870   -23.31899 -45.33853 1.000 18.61423 ? 483 ILE A O     1 
ATOM   3852 C  CB    . ILE A 1 483 ? 7.93559   -25.61604 -42.90059 1.000 18.36109 ? 483 ILE A CB    1 
ATOM   3853 C  CG1   . ILE A 1 483 ? 8.32159   -25.74710 -41.42559 1.000 19.97606 ? 483 ILE A CG1   1 
ATOM   3854 C  CG2   . ILE A 1 483 ? 9.12557   -25.93408 -43.78760 1.000 19.49584 ? 483 ILE A CG2   1 
ATOM   3855 C  CD1   . ILE A 1 483 ? 8.75652   -27.14013 -41.03263 1.000 20.18767 ? 483 ILE A CD1   1 
ATOM   3856 N  N     . ALA A 1 484 ? 6.10764   -24.48390 -45.24655 1.000 20.31222 ? 484 ALA A N     1 
ATOM   3857 C  CA    . ALA A 1 484 ? 5.88364   -24.32485 -46.67955 1.000 22.71136 ? 484 ALA A CA    1 
ATOM   3858 C  C     . ALA A 1 484 ? 5.69972   -22.85783 -47.04851 1.000 21.49094 ? 484 ALA A C     1 
ATOM   3859 O  O     . ALA A 1 484 ? 6.14673   -22.41783 -48.11350 1.000 23.18107 ? 484 ALA A O     1 
ATOM   3860 C  CB    . ALA A 1 484 ? 4.67360   -25.14478 -47.12156 1.000 19.72578 ? 484 ALA A CB    1 
ATOM   3861 N  N     . ARG A 1 485 ? 5.05397   -22.08051 -46.17561 1.000 18.96307 ? 485 ARG A N     1 
ATOM   3862 C  CA    . ARG A 1 485 ? 4.86704   -20.66042 -46.45122 1.000 19.78367 ? 485 ARG A CA    1 
ATOM   3863 C  C     . ARG A 1 485 ? 6.13861   -19.85998 -46.19431 1.000 21.55229 ? 485 ARG A C     1 
ATOM   3864 O  O     . ARG A 1 485 ? 6.34570   -18.81562 -46.81964 1.000 24.93746 ? 485 ARG A O     1 
ATOM   3865 C  CB    . ARG A 1 485 ? 3.71049   -20.11409 -45.61618 1.000 19.85524 ? 485 ARG A CB    1 
ATOM   3866 C  CG    . ARG A 1 485 ? 2.38407   -20.81567 -45.89138 1.000 23.84958 ? 485 ARG A CG    1 
ATOM   3867 C  CD    . ARG A 1 485 ? 1.33828   -20.47116 -44.85091 1.000 20.81278 ? 485 ARG A CD    1 
ATOM   3868 N  NE    . ARG A 1 485 ? 0.85295   -19.10546 -44.99652 1.000 24.44999 ? 485 ARG A NE    1 
ATOM   3869 C  CZ    . ARG A 1 485 ? 0.18206   -18.44670 -44.06205 1.000 19.16752 ? 485 ARG A CZ    1 
ATOM   3870 N  NH1   . ARG A 1 485 ? -0.06997  -18.98734 -42.88076 1.000 22.42928 ? 485 ARG A NH1   1 
ATOM   3871 N  NH2   . ARG A 1 485 ? -0.24395  -17.21327 -44.31765 1.000 20.08937 ? 485 ARG A NH2   1 
ATOM   3872 N  N     . MET A 1 486 ? 7.00285   -20.32994 -45.28946 1.000 21.84667 ? 486 MET A N     1 
ATOM   3873 C  CA    . MET A 1 486 ? 8.28289   -19.65901 -45.08545 1.000 22.53464 ? 486 MET A CA    1 
ATOM   3874 C  C     . MET A 1 486 ? 9.19787   -19.85703 -46.28646 1.000 23.07051 ? 486 MET A C     1 
ATOM   3875 O  O     . MET A 1 486 ? 9.91192   -18.93206 -46.69244 1.000 24.15181 ? 486 MET A O     1 
ATOM   3876 C  CB    . MET A 1 486 ? 8.95686   -20.17207 -43.81246 1.000 22.14335 ? 486 MET A CB    1 
ATOM   3877 C  CG    . MET A 1 486 ? 8.26889   -19.75107 -42.52545 1.000 21.84253 ? 486 MET A CG    1 
ATOM   3878 S  SD    . MET A 1 486 ? 8.29498   -17.97008 -42.25741 1.000 25.83383 ? 486 MET A SD    1 
ATOM   3879 C  CE    . MET A 1 486 ? 10.04100  -17.69617 -41.96441 1.000 22.30957 ? 486 MET A CE    1 
ATOM   3880 N  N     . ALA A 1 487 ? 9.18981   -21.06201 -46.86248 1.000 24.80360 ? 487 ALA A N     1 
ATOM   3881 C  CA    . ALA A 1 487 ? 9.95379   -21.31902 -48.07849 1.000 24.17388 ? 487 ALA A CA    1 
ATOM   3882 C  C     . ALA A 1 487 ? 9.47583   -20.43997 -49.22847 1.000 27.87602 ? 487 ALA A C     1 
ATOM   3883 O  O     . ALA A 1 487 ? 10.28885  -19.92100 -50.00146 1.000 31.14693 ? 487 ALA A O     1 
ATOM   3884 C  CB    . ALA A 1 487 ? 9.85271   -22.79601 -48.45453 1.000 17.10764 ? 487 ALA A CB    1 
ATOM   3885 N  N     . ALA A 1 488 ? 8.15884   -20.26690 -49.36646 1.000 28.82584 ? 488 ALA A N     1 
ATOM   3886 C  CA    . ALA A 1 488 ? 7.64188   -19.37385 -50.39844 1.000 27.82376 ? 488 ALA A CA    1 
ATOM   3887 C  C     . ALA A 1 488 ? 8.07295   -17.93788 -50.12941 1.000 34.69692 ? 488 ALA A C     1 
ATOM   3888 O  O     . ALA A 1 488 ? 8.51999   -17.22888 -51.03939 1.000 34.90648 ? 488 ALA A O     1 
ATOM   3889 C  CB    . ALA A 1 488 ? 6.11787   -19.47877 -50.47543 1.000 24.92561 ? 488 ALA A CB    1 
ATOM   3890 N  N     . ALA A 1 489 ? 7.96198   -17.49890 -48.87039 1.000 34.87396 ? 489 ALA A N     1 
ATOM   3891 C  CA    . ALA A 1 489 ? 8.38505   -16.14893 -48.51236 1.000 34.98176 ? 489 ALA A CA    1 
ATOM   3892 C  C     . ALA A 1 489 ? 9.87506   -15.95300 -48.76337 1.000 35.42843 ? 489 ALA A C     1 
ATOM   3893 O  O     . ALA A 1 489 ? 10.30111  -14.87602 -49.19434 1.000 34.67643 ? 489 ALA A O     1 
ATOM   3894 C  CB    . ALA A 1 489 ? 8.04407   -15.85595 -47.04936 1.000 31.28963 ? 489 ALA A CB    1 
ATOM   3895 N  N     . TYR A 1 490 ? 10.68201  -16.99005 -48.52139 1.000 34.30495 ? 490 TYR A N     1 
ATOM   3896 C  CA    . TYR A 1 490 ? 12.12401  -16.87312 -48.68540 1.000 33.29439 ? 490 TYR A CA    1 
ATOM   3897 C  C     . TYR A 1 490 ? 12.55701  -16.90411 -50.14440 1.000 37.56754 ? 490 TYR A C     1 
ATOM   3898 O  O     . TYR A 1 490 ? 13.68602  -16.50316 -50.44739 1.000 41.95153 ? 490 TYR A O     1 
ATOM   3899 C  CB    . TYR A 1 490 ? 12.83896  -17.98217 -47.91243 1.000 30.18133 ? 490 TYR A CB    1 
ATOM   3900 C  CG    . TYR A 1 490 ? 13.42199  -17.50923 -46.60042 1.000 25.91582 ? 490 TYR A CG    1 
ATOM   3901 C  CD1   . TYR A 1 490 ? 14.62402  -16.81530 -46.56740 1.000 30.09039 ? 490 TYR A CD1   1 
ATOM   3902 C  CD2   . TYR A 1 490 ? 12.77098  -17.74923 -45.39742 1.000 24.91682 ? 490 TYR A CD2   1 
ATOM   3903 C  CE1   . TYR A 1 490 ? 15.16305  -16.37535 -45.37440 1.000 29.52206 ? 490 TYR A CE1   1 
ATOM   3904 C  CE2   . TYR A 1 490 ? 13.30501  -17.31229 -44.19641 1.000 22.26380 ? 490 TYR A CE2   1 
ATOM   3905 C  CZ    . TYR A 1 490 ? 14.50204  -16.62435 -44.19240 1.000 24.23038 ? 490 TYR A CZ    1 
ATOM   3906 O  OH    . TYR A 1 490 ? 15.04507  -16.18640 -43.00839 1.000 17.82690 ? 490 TYR A OH    1 
ATOM   3907 N  N     . ARG A 1 491 ? 11.70141  -17.38019 -51.04939 1.000 36.61559 ? 491 ARG A N     1 
ATOM   3908 C  CA    . ARG A 1 491 ? 12.00099  -17.29492 -52.47363 1.000 41.73409 ? 491 ARG A CA    1 
ATOM   3909 C  C     . ARG A 1 491 ? 11.53094  -15.97221 -53.06199 1.000 40.70340 ? 491 ARG A C     1 
ATOM   3910 O  O     . ARG A 1 491 ? 12.25283  -15.35559 -53.85261 1.000 45.58214 ? 491 ARG A O     1 
ATOM   3911 C  CB    . ARG A 1 491 ? 11.37399  -18.47264 -53.22605 1.000 39.26009 ? 491 ARG A CB    1 
ATOM   3912 C  CG    . ARG A 1 491 ? 11.90327  -19.82274 -52.76992 1.000 35.91205 ? 491 ARG A CG    1 
ATOM   3913 C  CD    . ARG A 1 491 ? 11.80462  -20.88733 -53.85656 1.000 38.69979 ? 491 ARG A CD    1 
ATOM   3914 N  NE    . ARG A 1 491 ? 10.43436  -21.13768 -54.28547 1.000 38.71450 ? 491 ARG A NE    1 
ATOM   3915 C  CZ    . ARG A 1 491 ? 9.54725   -21.84029 -53.59465 1.000 33.39985 ? 491 ARG A CZ    1 
ATOM   3916 N  NH1   . ARG A 1 491 ? 9.83808   -22.34897 -52.40815 1.000 30.96347 ? 491 ARG A NH1   1 
ATOM   3917 N  NH2   . ARG A 1 491 ? 8.33498   -22.03199 -54.10446 1.000 39.27675 ? 491 ARG A NH2   1 
ATOM   3918 N  N     A ARG A 1 492 ? 10.33188  -15.52161 -52.68851 0.560 43.94212 ? 492 ARG A N     1 
ATOM   3919 N  N     B ARG A 1 492 ? 10.33323  -15.52013 -52.69091 0.440 43.92337 ? 492 ARG A N     1 
ATOM   3920 C  CA    A ARG A 1 492 ? 9.86670   -14.19051 -53.06040 0.560 44.92694 ? 492 ARG A CA    1 
ATOM   3921 C  CA    B ARG A 1 492 ? 9.88658   -14.18818 -53.07893 0.440 44.91628 ? 492 ARG A CA    1 
ATOM   3922 C  C     A ARG A 1 492 ? 10.62385  -13.08772 -52.33601 0.560 44.58108 ? 492 ARG A C     1 
ATOM   3923 C  C     B ARG A 1 492 ? 10.65532  -13.08761 -52.36539 0.440 44.58319 ? 492 ARG A C     1 
ATOM   3924 O  O     A ARG A 1 492 ? 10.36804  -11.90785 -52.60106 0.560 44.36176 ? 492 ARG A O     1 
ATOM   3925 O  O     B ARG A 1 492 ? 10.43893  -11.90888 -52.66812 0.440 44.36889 ? 492 ARG A O     1 
ATOM   3926 C  CB    A ARG A 1 492 ? 8.36903   -14.05613 -52.77626 0.560 43.18842 ? 492 ARG A CB    1 
ATOM   3927 C  CB    B ARG A 1 492 ? 8.39089   -14.02841 -52.80334 0.440 43.19259 ? 492 ARG A CB    1 
ATOM   3928 C  CG    A ARG A 1 492 ? 8.03850   -14.07695 -51.29723 0.560 43.91931 ? 492 ARG A CG    1 
ATOM   3929 C  CG    B ARG A 1 492 ? 8.03873   -14.06067 -51.32766 0.440 43.91242 ? 492 ARG A CG    1 
ATOM   3930 C  CD    A ARG A 1 492 ? 6.54669   -14.19463 -51.01983 0.560 43.92201 ? 492 ARG A CD    1 
ATOM   3931 C  CD    B ARG A 1 492 ? 6.57232   -13.74467 -51.06875 0.440 44.26782 ? 492 ARG A CD    1 
ATOM   3932 N  NE    A ARG A 1 492 ? 5.84498   -14.99064 -52.01875 0.560 44.79326 ? 492 ARG A NE    1 
ATOM   3933 N  NE    B ARG A 1 492 ? 5.66954   -14.67736 -51.73197 0.440 44.91720 ? 492 ARG A NE    1 
ATOM   3934 C  CZ    A ARG A 1 492 ? 4.75727   -14.58658 -52.66010 0.560 45.10483 ? 492 ARG A CZ    1 
ATOM   3935 C  CZ    B ARG A 1 492 ? 5.03581   -14.42348 -52.86834 0.440 45.21972 ? 492 ARG A CZ    1 
ATOM   3936 N  NH1   A ARG A 1 492 ? 4.19879   -13.41506 -52.40222 0.560 45.18154 ? 492 ARG A NH1   1 
ATOM   3937 N  NH1   B ARG A 1 492 ? 5.18467   -13.27009 -53.49942 0.440 43.70471 ? 492 ARG A NH1   1 
ATOM   3938 N  NH2   A ARG A 1 492 ? 4.21061   -15.38117 -53.57555 0.560 45.37582 ? 492 ARG A NH2   1 
ATOM   3939 N  NH2   B ARG A 1 492 ? 4.23288   -15.34947 -53.38390 0.440 45.33516 ? 492 ARG A NH2   1 
ATOM   3940 N  N     . SER A 1 493 ? 11.53218  -13.44103 -51.42631 1.000 42.95009 ? 493 SER A N     1 
ATOM   3941 C  CA    . SER A 1 493 ? 12.36623  -12.47108 -50.72929 1.000 46.55562 ? 493 SER A CA    1 
ATOM   3942 C  C     . SER A 1 493 ? 13.60624  -12.08613 -51.52329 1.000 50.56179 ? 493 SER A C     1 
ATOM   3943 O  O     . SER A 1 493 ? 14.38829  -11.25018 -51.05527 1.000 58.55698 ? 493 SER A O     1 
ATOM   3944 C  CB    . SER A 1 493 ? 12.79620  -13.02114 -49.36831 1.000 46.30087 ? 493 SER A CB    1 
ATOM   3945 O  OG    . SER A 1 493 ? 13.70915  -14.09618 -49.52334 1.000 46.19346 ? 493 SER A OG    1 
ATOM   3946 N  N     . LYS A 1 494 ? 13.80421  -12.67911 -52.69930 1.000 47.24591 ? 494 LYS A N     1 
ATOM   3947 C  CA    . LYS A 1 494 ? 14.95422  -12.38815 -53.55430 1.000 53.25176 ? 494 LYS A CA    1 
ATOM   3948 C  C     . LYS A 1 494 ? 16.27821  -12.57123 -52.81731 1.000 54.07632 ? 494 LYS A C     1 
ATOM   3949 O  O     . LYS A 1 494 ? 17.33523  -12.19427 -53.32331 1.000 57.79238 ? 494 LYS A O     1 
ATOM   3950 C  CB    . LYS A 1 494 ? 14.85629  -10.96713 -54.11727 1.000 50.90992 ? 494 LYS A CB    1 
HETATM 3951 P  PA    . FAD B 2 .   ? 22.36422  -14.98133 -19.51739 1.000 3.86219  ? 601 FAD A PA    1 
HETATM 3952 O  O1A   . FAD B 2 .   ? 22.89523  -14.91439 -18.14439 1.000 8.33598  ? 601 FAD A O1A   1 
HETATM 3953 O  O2A   . FAD B 2 .   ? 22.45015  -16.29231 -20.18642 1.000 10.17381 ? 601 FAD A O2A   1 
HETATM 3954 O  O5B   . FAD B 2 .   ? 23.02728  -13.85034 -20.41937 1.000 4.75269  ? 601 FAD A O5B   1 
HETATM 3955 C  C5B   . FAD B 2 .   ? 23.62633  -12.76039 -19.72034 1.000 6.17155  ? 601 FAD A C5B   1 
HETATM 3956 C  C4B   . FAD B 2 .   ? 23.15440  -11.45035 -20.29631 1.000 5.09701  ? 601 FAD A C4B   1 
HETATM 3957 O  O4B   . FAD B 2 .   ? 23.49440  -11.39433 -21.69731 1.000 5.61465  ? 601 FAD A O4B   1 
HETATM 3958 C  C3B   . FAD B 2 .   ? 21.64541  -11.19727 -20.23330 1.000 5.80926  ? 601 FAD A C3B   1 
HETATM 3959 O  O3B   . FAD B 2 .   ? 21.28945  -10.60028 -18.99728 1.000 5.36759  ? 601 FAD A O3B   1 
HETATM 3960 C  C2B   . FAD B 2 .   ? 21.44546  -10.22724 -21.40028 1.000 5.77441  ? 601 FAD A C2B   1 
HETATM 3961 O  O2B   . FAD B 2 .   ? 21.78652  -8.89526  -21.09125 1.000 5.17106  ? 601 FAD A O2B   1 
HETATM 3962 C  C1B   . FAD B 2 .   ? 22.43542  -10.78326 -22.42329 1.000 5.38707  ? 601 FAD A C1B   1 
HETATM 3963 N  N9A   . FAD B 2 .   ? 21.83837  -11.76821 -23.32231 1.000 5.84802  ? 601 FAD A N9A   1 
HETATM 3964 C  C8A   . FAD B 2 .   ? 21.63930  -13.10820 -23.12734 1.000 5.50714  ? 601 FAD A C8A   1 
HETATM 3965 N  N7A   . FAD B 2 .   ? 21.07227  -13.70915 -24.13936 1.000 5.30171  ? 601 FAD A N7A   1 
HETATM 3966 C  C5A   . FAD B 2 .   ? 20.88732  -12.69612 -25.06433 1.000 6.81322  ? 601 FAD A C5A   1 
HETATM 3967 C  C6A   . FAD B 2 .   ? 20.32731  -12.69206 -26.35433 1.000 5.71345  ? 601 FAD A C6A   1 
HETATM 3968 N  N6A   . FAD B 2 .   ? 19.83525  -13.77402 -26.94635 1.000 7.22063  ? 601 FAD A N6A   1 
HETATM 3969 N  N1A   . FAD B 2 .   ? 20.28837  -11.51204 -27.01130 1.000 4.46548  ? 601 FAD A N1A   1 
HETATM 3970 C  C2A   . FAD B 2 .   ? 20.79243  -10.43308 -26.40828 1.000 6.65292  ? 601 FAD A C2A   1 
HETATM 3971 N  N3A   . FAD B 2 .   ? 21.33644  -10.31514 -25.20528 1.000 4.40107  ? 601 FAD A N3A   1 
HETATM 3972 C  C4A   . FAD B 2 .   ? 21.35438  -11.49516 -24.57231 1.000 5.87530  ? 601 FAD A C4A   1 
HETATM 3973 N  N1    . FAD B 2 .   ? 16.49300  -10.33600 -23.22400 1.000 7.02814  ? 601 FAD A N1    1 
HETATM 3974 C  C2    . FAD B 2 .   ? 16.31700  -9.16200  -22.59400 1.000 7.36799  ? 601 FAD A C2    1 
HETATM 3975 O  O2    . FAD B 2 .   ? 17.04700  -8.82500  -21.67800 1.000 7.61873  ? 601 FAD A O2    1 
HETATM 3976 N  N3    . FAD B 2 .   ? 15.35100  -8.28900  -22.96400 1.000 5.17835  ? 601 FAD A N3    1 
HETATM 3977 C  C4    . FAD B 2 .   ? 14.45000  -8.56300  -23.95600 1.000 7.61585  ? 601 FAD A C4    1 
HETATM 3978 O  O4    . FAD B 2 .   ? 13.61300  -7.70700  -24.26800 1.000 6.36918  ? 601 FAD A O4    1 
HETATM 3979 C  C4X   . FAD B 2 .   ? 14.52500  -9.86000  -24.56800 1.000 7.28156  ? 601 FAD A C4X   1 
HETATM 3980 N  N5    . FAD B 2 .   ? 13.52100  -10.31500 -25.30700 1.000 9.04086  ? 601 FAD A N5    1 
HETATM 3981 C  C5X   . FAD B 2 .   ? 13.70600  -11.52200 -25.95000 1.000 8.06359  ? 601 FAD A C5X   1 
HETATM 3982 C  C6    . FAD B 2 .   ? 12.73000  -11.96300 -26.86700 1.000 7.01865  ? 601 FAD A C6    1 
HETATM 3983 C  C7    . FAD B 2 .   ? 12.76000  -13.23500 -27.40300 1.000 8.54385  ? 601 FAD A C7    1 
HETATM 3984 C  C7M   . FAD B 2 .   ? 11.70000  -13.65600 -28.38300 1.000 9.68265  ? 601 FAD A C7M   1 
HETATM 3985 C  C8    . FAD B 2 .   ? 13.79700  -14.13200 -27.00500 1.000 8.05347  ? 601 FAD A C8    1 
HETATM 3986 C  C8M   . FAD B 2 .   ? 13.88400  -15.52600 -27.57100 1.000 8.68930  ? 601 FAD A C8M   1 
HETATM 3987 C  C9    . FAD B 2 .   ? 14.79700  -13.68400 -26.17500 1.000 5.97953  ? 601 FAD A C9    1 
HETATM 3988 C  C9A   . FAD B 2 .   ? 14.77700  -12.38600 -25.61800 1.000 7.42948  ? 601 FAD A C9A   1 
HETATM 3989 N  N10   . FAD B 2 .   ? 15.83300  -11.84700 -24.87900 1.000 8.00963  ? 601 FAD A N10   1 
HETATM 3990 C  C10   . FAD B 2 .   ? 15.60200  -10.69900 -24.12400 1.000 6.86786  ? 601 FAD A C10   1 
HETATM 3991 C  "C1'" . FAD B 2 .   ? 16.98132  -12.69794 -24.51332 1.000 7.38958  ? 601 FAD A "C1'" 1 
HETATM 3992 C  "C2'" . FAD B 2 .   ? 17.06026  -13.88996 -23.62935 1.000 5.52050  ? 601 FAD A "C2'" 1 
HETATM 3993 O  "O2'" . FAD B 2 .   ? 15.85622  -14.62690 -23.72136 1.000 8.46233  ? 601 FAD A "O2'" 1 
HETATM 3994 C  "C3'" . FAD B 2 .   ? 17.38530  -13.21101 -22.30533 1.000 8.55745  ? 601 FAD A "C3'" 1 
HETATM 3995 O  "O3'" . FAD B 2 .   ? 18.27436  -12.11805 -22.52831 1.000 6.23705  ? 601 FAD A "O3'" 1 
HETATM 3996 C  "C4'" . FAD B 2 .   ? 17.99426  -14.17006 -21.30136 1.000 7.30752  ? 601 FAD A "C4'" 1 
HETATM 3997 O  "O4'" . FAD B 2 .   ? 17.14220  -15.31002 -21.25338 1.000 9.48160  ? 601 FAD A "O4'" 1 
HETATM 3998 C  "C5'" . FAD B 2 .   ? 18.09930  -13.48210 -19.96434 1.000 5.50875  ? 601 FAD A "C5'" 1 
HETATM 3999 O  "O5'" . FAD B 2 .   ? 18.50825  -14.43114 -18.99336 1.000 5.82351  ? 601 FAD A "O5'" 1 
HETATM 4000 P  P     . FAD B 2 .   ? 19.90527  -14.19923 -18.29236 1.000 4.85393  ? 601 FAD A P     1 
HETATM 4001 O  O1P   . FAD B 2 .   ? 20.01134  -12.79225 -17.85133 1.000 2.88884  ? 601 FAD A O1P   1 
HETATM 4002 O  O2P   . FAD B 2 .   ? 20.08222  -15.23826 -17.26239 1.000 5.67958  ? 601 FAD A O2P   1 
HETATM 4003 O  O3P   . FAD B 2 .   ? 20.87625  -14.46725 -19.50237 1.000 6.94633  ? 601 FAD A O3P   1 
HETATM 4004 CL CL    . CL  C 3 .   ? 12.48841  -30.17256 -30.71471 1.000 22.58369 ? 602 CL  A CL    1 
HETATM 4005 O  O     . HOH D 4 .   ? 16.12151  -28.29576 -30.08768 1.000 21.99219 ? 701 HOH A O     1 
HETATM 4006 O  O     . HOH D 4 .   ? 22.28507  -16.64989 -37.66443 1.000 21.34692 ? 702 HOH A O     1 
HETATM 4007 O  O     . HOH D 4 .   ? 17.58717  -16.81533 -8.95342  1.000 31.46477 ? 703 HOH A O     1 
HETATM 4008 O  O     . HOH D 4 .   ? 32.62210  1.51692   -9.40604  1.000 11.12129 ? 704 HOH A O     1 
HETATM 4009 O  O     . HOH D 4 .   ? 21.75829  24.73939  -6.11245  1.000 14.57852 ? 705 HOH A O     1 
HETATM 4010 O  O     . HOH D 4 .   ? 3.11751   9.25828   -3.90174  1.000 27.48896 ? 706 HOH A O     1 
HETATM 4011 O  O     . HOH D 4 .   ? 16.74739  -9.73047  -43.65825 1.000 19.21506 ? 707 HOH A O     1 
HETATM 4012 O  O     . HOH D 4 .   ? -6.26051  -8.98566  -28.70714 1.000 20.18206 ? 708 HOH A O     1 
HETATM 4013 O  O     . HOH D 4 .   ? 15.26536  -32.31707 -15.29477 1.000 23.62553 ? 709 HOH A O     1 
HETATM 4014 O  O     . HOH D 4 .   ? 31.33433  -13.90010 -5.76040  1.000 23.27883 ? 710 HOH A O     1 
HETATM 4015 O  O     . HOH D 4 .   ? 7.76513   1.70706   -4.77994  1.000 11.02682 ? 711 HOH A O     1 
HETATM 4016 O  O     . HOH D 4 .   ? 10.99047  8.22082   -1.51380  1.000 12.84770 ? 712 HOH A O     1 
HETATM 4017 O  O     . HOH D 4 .   ? 6.98068   -24.67125 -32.07656 1.000 7.87363  ? 713 HOH A O     1 
HETATM 4018 O  O     . HOH D 4 .   ? 26.50171  -5.08743  -23.93217 1.000 12.52426 ? 714 HOH A O     1 
HETATM 4019 O  O     . HOH D 4 .   ? 27.02936  7.24137   -16.67689 1.000 9.17478  ? 715 HOH A O     1 
HETATM 4020 O  O     . HOH D 4 .   ? 8.32788   -3.22299  -3.62106  1.000 18.74919 ? 716 HOH A O     1 
HETATM 4021 O  O     . HOH D 4 .   ? 16.27088  -22.09609 -16.28354 1.000 10.34197 ? 717 HOH A O     1 
HETATM 4022 O  O     . HOH D 4 .   ? 27.31303  20.98750  -22.89256 1.000 20.78880 ? 718 HOH A O     1 
HETATM 4023 O  O     . HOH D 4 .   ? 11.63178  -3.07254  -29.94307 1.000 18.73968 ? 719 HOH A O     1 
HETATM 4024 O  O     . HOH D 4 .   ? 31.88204  -18.57080 -19.85051 1.000 8.52740  ? 720 HOH A O     1 
HETATM 4025 O  O     . HOH D 4 .   ? 12.65373  13.52376  -2.34168  1.000 13.31672 ? 721 HOH A O     1 
HETATM 4026 O  O     . HOH D 4 .   ? -4.67064  -32.66812 -12.53070 1.000 17.83913 ? 722 HOH A O     1 
HETATM 4027 O  O     . HOH D 4 .   ? 33.03114  2.95508   -17.34501 1.000 13.88616 ? 723 HOH A O     1 
HETATM 4028 O  O     . HOH D 4 .   ? 21.83213  1.89336   -4.94899  1.000 15.77535 ? 724 HOH A O     1 
HETATM 4029 O  O     . HOH D 4 .   ? -4.88755  -29.98483 -24.31164 1.000 8.45406  ? 725 HOH A O     1 
HETATM 4030 O  O     . HOH D 4 .   ? 23.33306  21.83076  -25.12253 1.000 24.57146 ? 726 HOH A O     1 
HETATM 4031 O  O     . HOH D 4 .   ? 18.98758  31.01766  -11.59429 1.000 23.92467 ? 727 HOH A O     1 
HETATM 4032 O  O     . HOH D 4 .   ? 23.10407  1.70159   -17.69900 1.000 7.36098  ? 728 HOH A O     1 
HETATM 4033 O  O     . HOH D 4 .   ? 18.38456  -27.44396 -26.67867 1.000 19.86635 ? 729 HOH A O     1 
HETATM 4034 O  O     . HOH D 4 .   ? 11.77491  -0.93367  -24.59702 1.000 28.16344 ? 730 HOH A O     1 
HETATM 4035 O  O     . HOH D 4 .   ? 10.42391  -0.73655  -26.82601 1.000 28.03498 ? 731 HOH A O     1 
HETATM 4036 O  O     A HOH D 4 .   ? -0.00727  -5.29932  -14.14108 0.504 14.47693 ? 732 HOH A O     1 
HETATM 4037 O  O     B HOH D 4 .   ? -0.69421  -4.10524  -15.99204 0.496 15.11529 ? 732 HOH A O     1 
HETATM 4038 O  O     . HOH D 4 .   ? 29.65522  6.07969   -36.01092 1.000 12.09499 ? 733 HOH A O     1 
HETATM 4039 O  O     . HOH D 4 .   ? 8.74436   -10.53514 -40.69923 1.000 18.36464 ? 734 HOH A O     1 
HETATM 4040 O  O     . HOH D 4 .   ? 24.14401  1.32382   -29.48601 1.000 17.60873 ? 735 HOH A O     1 
HETATM 4041 O  O     . HOH D 4 .   ? 30.78929  5.33403   -10.32695 1.000 8.86056  ? 736 HOH A O     1 
HETATM 4042 O  O     . HOH D 4 .   ? 14.48599  -1.09332  -3.07003  1.000 11.87882 ? 737 HOH A O     1 
HETATM 4043 O  O     . HOH D 4 .   ? 21.22123  5.04575   -20.38291 1.000 13.53652 ? 738 HOH A O     1 
HETATM 4044 O  O     . HOH D 4 .   ? 35.25347  8.71971   -6.32788  1.000 17.75348 ? 739 HOH A O     1 
HETATM 4045 O  O     . HOH D 4 .   ? 2.97547   -29.41223 -24.41766 1.000 10.97533 ? 740 HOH A O     1 
HETATM 4046 O  O     . HOH D 4 .   ? 15.57349  -10.66029 -6.61526  1.000 17.15963 ? 741 HOH A O     1 
HETATM 4047 O  O     . HOH D 4 .   ? 19.49260  -7.51215  -20.65920 1.000 7.31801  ? 742 HOH A O     1 
HETATM 4048 O  O     . HOH D 4 .   ? 35.00580  -3.59799  -18.46817 1.000 7.05421  ? 743 HOH A O     1 
HETATM 4049 O  O     . HOH D 4 .   ? 18.85505  0.61559   -8.60701  1.000 8.52796  ? 744 HOH A O     1 
HETATM 4050 O  O     . HOH D 4 .   ? 22.92425  -15.02756 -10.88940 1.000 16.75933 ? 745 HOH A O     1 
HETATM 4051 O  O     . HOH D 4 .   ? 42.70376  -3.97822  -25.08621 1.000 25.32305 ? 746 HOH A O     1 
HETATM 4052 O  O     . HOH D 4 .   ? 12.98896  -20.44495 -15.25848 1.000 11.17481 ? 747 HOH A O     1 
HETATM 4053 O  O     . HOH D 4 .   ? 8.57441   -29.77427 -34.87069 1.000 9.77709  ? 748 HOH A O     1 
HETATM 4054 O  O     A HOH D 4 .   ? 4.85350   -9.82953  -15.85420 0.687 6.08095  ? 749 HOH A O     1 
HETATM 4055 O  O     B HOH D 4 .   ? 2.37753   -9.17540  -15.73018 0.313 8.28017  ? 749 HOH A O     1 
HETATM 4056 O  O     . HOH D 4 .   ? 20.70536  7.46074   -18.91086 1.000 13.17946 ? 750 HOH A O     1 
HETATM 4057 O  O     . HOH D 4 .   ? 14.49394  -0.51082  -23.95502 1.000 21.11315 ? 751 HOH A O     1 
HETATM 4058 O  O     . HOH D 4 .   ? 37.390    3.553     -40.360   1.000 16.62579 ? 752 HOH A O     1 
HETATM 4059 O  O     . HOH D 4 .   ? 27.74415  -15.05718 -37.09742 1.000 21.13488 ? 753 HOH A O     1 
HETATM 4060 O  O     . HOH D 4 .   ? 20.00972  -4.96617  -21.20115 1.000 8.63627  ? 754 HOH A O     1 
HETATM 4061 O  O     . HOH D 4 .   ? 18.84710  -17.28713 -20.31443 1.000 13.31112 ? 755 HOH A O     1 
HETATM 4062 O  O     . HOH D 4 .   ? 38.35016  3.13671   -13.09603 1.000 19.92043 ? 756 HOH A O     1 
HETATM 4063 O  O     . HOH D 4 .   ? -0.42981  -15.64115 -20.30432 1.000 13.35019 ? 757 HOH A O     1 
HETATM 4064 O  O     . HOH D 4 .   ? 21.87842  8.45962   -16.20684 1.000 16.60260 ? 758 HOH A O     1 
HETATM 4065 O  O     . HOH D 4 .   ? 32.01828  24.71789  -7.11549  1.000 20.54459 ? 759 HOH A O     1 
HETATM 4066 O  O     . HOH D 4 .   ? 25.99794  -0.84754  -18.17807 1.000 6.45648  ? 760 HOH A O     1 
HETATM 4067 O  O     . HOH D 4 .   ? 0.98998   -39.08412 -24.69888 1.000 16.13310 ? 761 HOH A O     1 
HETATM 4068 O  O     . HOH D 4 .   ? -3.97118  -3.73917  -12.01902 1.000 31.44109 ? 762 HOH A O     1 
HETATM 4069 O  O     . HOH D 4 .   ? 20.03375  -24.91838 -12.23662 1.000 16.25329 ? 763 HOH A O     1 
HETATM 4070 O  O     . HOH D 4 .   ? 26.93820  5.07166   -28.72494 1.000 20.59360 ? 764 HOH A O     1 
HETATM 4071 O  O     . HOH D 4 .   ? 11.99694  -20.76084 -18.10649 1.000 12.52049 ? 765 HOH A O     1 
HETATM 4072 O  O     . HOH D 4 .   ? 39.82278  -23.85726 -17.50767 1.000 13.33498 ? 766 HOH A O     1 
HETATM 4073 O  O     . HOH D 4 .   ? 10.09369  -6.65497  -8.15415  1.000 19.44708 ? 767 HOH A O     1 
HETATM 4074 O  O     . HOH D 4 .   ? 21.90410  2.72483   -25.21497 1.000 22.17399 ? 768 HOH A O     1 
HETATM 4075 O  O     . HOH D 4 .   ? 5.88566   12.11310  -2.46669  1.000 17.94210 ? 769 HOH A O     1 
HETATM 4076 O  O     . HOH D 4 .   ? -9.26091  -16.93550 -29.03131 1.000 15.74321 ? 770 HOH A O     1 
HETATM 4077 O  O     . HOH D 4 .   ? 18.13185  -3.80547  -4.44211  1.000 11.85844 ? 771 HOH A O     1 
HETATM 4078 O  O     . HOH D 4 .   ? 7.87387   16.79115  -8.55759  1.000 12.84903 ? 772 HOH A O     1 
HETATM 4079 O  O     . HOH D 4 .   ? 30.26344  9.50338   -23.96985 1.000 19.52609 ? 773 HOH A O     1 
HETATM 4080 O  O     . HOH D 4 .   ? 0.69009   -15.47160 -46.39632 1.000 27.85883 ? 774 HOH A O     1 
HETATM 4081 O  O     . HOH D 4 .   ? 4.57844   9.19959   -20.38475 1.000 33.39563 ? 775 HOH A O     1 
HETATM 4082 O  O     . HOH D 4 .   ? 12.58652  10.64517  -19.66475 1.000 14.83536 ? 776 HOH A O     1 
HETATM 4083 O  O     . HOH D 4 .   ? 23.60488  -2.10143  -17.88309 1.000 8.29586  ? 777 HOH A O     1 
HETATM 4084 O  O     . HOH D 4 .   ? 27.51984  15.35590  2.39630   1.000 19.22067 ? 778 HOH A O     1 
HETATM 4085 O  O     . HOH D 4 .   ? 10.99641  -8.99108  -48.04821 1.000 24.58567 ? 779 HOH A O     1 
HETATM 4086 O  O     A HOH D 4 .   ? 19.13606  -17.46392 -29.92744 0.398 10.00841 ? 780 HOH A O     1 
HETATM 4087 O  O     B HOH D 4 .   ? 18.00315  -15.54885 -30.51839 0.602 9.93454  ? 780 HOH A O     1 
HETATM 4088 O  O     . HOH D 4 .   ? 32.08438  8.09025   -22.60689 1.000 10.47665 ? 781 HOH A O     1 
HETATM 4089 O  O     . HOH D 4 .   ? -1.06749  -9.11907  -22.37516 1.000 18.86249 ? 782 HOH A O     1 
HETATM 4090 O  O     A HOH D 4 .   ? 36.59421  -14.83893 -24.45144 0.682 6.58227  ? 783 HOH A O     1 
HETATM 4091 O  O     B HOH D 4 .   ? 34.54415  -16.10685 -23.54447 0.318 8.20039  ? 783 HOH A O     1 
HETATM 4092 O  O     . HOH D 4 .   ? 13.63949  9.83503   -15.99177 1.000 12.78308 ? 784 HOH A O     1 
HETATM 4093 O  O     . HOH D 4 .   ? 41.93100  1.92014   -38.74507 1.000 26.59652 ? 785 HOH A O     1 
HETATM 4094 O  O     . HOH D 4 .   ? 20.84692  -19.26276 -40.43849 1.000 20.33501 ? 786 HOH A O     1 
HETATM 4095 O  O     . HOH D 4 .   ? 33.51083  -22.26973 -26.48461 1.000 17.40707 ? 787 HOH A O     1 
HETATM 4096 O  O     B HOH D 4 .   ? 10.03598  -0.08874  -17.81399 0.469 11.96189 ? 788 HOH A O     1 
HETATM 4097 O  O     C HOH D 4 .   ? 11.03909  2.08020   -17.72394 0.531 14.34167 ? 788 HOH A O     1 
HETATM 4098 O  O     . HOH D 4 .   ? 6.09752   9.41612   -3.72475  1.000 20.18165 ? 789 HOH A O     1 
HETATM 4099 O  O     . HOH D 4 .   ? 12.33520  22.49471  0.26553   1.000 22.26479 ? 790 HOH A O     1 
HETATM 4100 O  O     . HOH D 4 .   ? 6.33657   -28.71575 -9.38665  1.000 22.87787 ? 791 HOH A O     1 
HETATM 4101 O  O     A HOH D 4 .   ? 25.43513  3.34266   -25.32897 0.332 8.07709  ? 792 HOH A O     1 
HETATM 4102 O  O     B HOH D 4 .   ? 25.52319  4.31059   -22.83195 0.668 5.80678  ? 792 HOH A O     1 
HETATM 4103 O  O     . HOH D 4 .   ? -0.25867  -31.58489 -31.71969 1.000 17.32265 ? 793 HOH A O     1 
HETATM 4104 O  O     A HOH D 4 .   ? 38.31957  -7.66097  -26.61328 0.730 11.77989 ? 794 HOH A O     1 
HETATM 4105 O  O     B HOH D 4 .   ? 36.67157  -7.65493  -24.66928 0.270 11.45818 ? 794 HOH A O     1 
HETATM 4106 O  O     . HOH D 4 .   ? 13.11768  -26.42505 -11.19363 1.000 15.90142 ? 795 HOH A O     1 
HETATM 4107 O  O     . HOH D 4 .   ? 36.85570  -5.48206  -19.34622 1.000 11.83374 ? 796 HOH A O     1 
HETATM 4108 O  O     . HOH D 4 .   ? 35.81605  0.53377   -9.99508  1.000 17.59631 ? 797 HOH A O     1 
HETATM 4109 O  O     . HOH D 4 .   ? -10.67772 -13.34553 -24.82722 1.000 28.21312 ? 798 HOH A O     1 
HETATM 4110 O  O     . HOH D 4 .   ? -5.96459  -10.93781 -22.97219 1.000 21.24848 ? 799 HOH A O     1 
HETATM 4111 O  O     . HOH D 4 .   ? 23.17836  7.15152   -14.67987 1.000 3.36516  ? 800 HOH A O     1 
HETATM 4112 O  O     . HOH D 4 .   ? 8.86564   -25.81844 -28.06759 1.000 9.86331  ? 801 HOH A O     1 
HETATM 4113 O  O     . HOH D 4 .   ? 20.12967  -25.33902 -27.66963 1.000 19.42304 ? 802 HOH A O     1 
HETATM 4114 O  O     . HOH D 4 .   ? 19.61209  -18.25539 -11.11046 1.000 15.05321 ? 803 HOH A O     1 
HETATM 4115 O  O     . HOH D 4 .   ? 5.70524   -33.37718 -32.20876 1.000 27.41869 ? 804 HOH A O     1 
HETATM 4116 O  O     . HOH D 4 .   ? 20.31627  -11.44642 -53.69430 1.000 26.02044 ? 805 HOH A O     1 
HETATM 4117 O  O     . HOH D 4 .   ? 3.28215   -14.04565 -49.50729 1.000 40.05622 ? 806 HOH A O     1 
HETATM 4118 O  O     . HOH D 4 .   ? 33.88121  4.76117   -22.93497 1.000 15.88767 ? 807 HOH A O     1 
HETATM 4119 O  O     . HOH D 4 .   ? 6.49413   -17.73481 -7.56839  1.000 17.74266 ? 808 HOH A O     1 
HETATM 4120 O  O     . HOH D 4 .   ? -1.05655  -9.09672  -37.23716 1.000 27.53503 ? 809 HOH A O     1 
HETATM 4121 O  O     . HOH D 4 .   ? 24.97353  8.86092   6.79016   1.000 23.50470 ? 810 HOH A O     1 
HETATM 4122 O  O     . HOH D 4 .   ? 8.01152   -28.95064 -17.95567 1.000 13.51193 ? 811 HOH A O     1 
HETATM 4123 O  O     . HOH D 4 .   ? 19.59432  -11.22965 -42.14529 1.000 23.51642 ? 812 HOH A O     1 
HETATM 4124 O  O     . HOH D 4 .   ? -7.00046  -27.22746 -35.72557 1.000 19.39640 ? 813 HOH A O     1 
HETATM 4125 O  O     . HOH D 4 .   ? 25.09140  -12.78886 -2.64835  1.000 15.40057 ? 814 HOH A O     1 
HETATM 4126 O  O     . HOH D 4 .   ? 21.43866  -26.29435 -16.71666 1.000 10.04409 ? 815 HOH A O     1 
HETATM 4127 O  O     . HOH D 4 .   ? 32.70979  14.84180  -4.52473  1.000 21.60985 ? 816 HOH A O     1 
HETATM 4128 O  O     . HOH D 4 .   ? -2.48392  -36.22364 -37.52880 1.000 28.06550 ? 817 HOH A O     1 
HETATM 4129 O  O     . HOH D 4 .   ? 22.15212  -16.38814 -26.97542 1.000 17.50906 ? 818 HOH A O     1 
HETATM 4130 O  O     . HOH D 4 .   ? 2.88795   -40.58549 -13.30092 1.000 24.74064 ? 819 HOH A O     1 
HETATM 4131 O  O     . HOH D 4 .   ? 28.58907  0.71003   -5.64905  1.000 17.89667 ? 820 HOH A O     1 
HETATM 4132 O  O     . HOH D 4 .   ? 14.26814  4.34048   -36.12290 1.000 24.97710 ? 821 HOH A O     1 
HETATM 4133 O  O     . HOH D 4 .   ? 4.50106   -16.10178 -46.82335 1.000 27.32885 ? 822 HOH A O     1 
HETATM 4134 O  O     . HOH D 4 .   ? 18.56758  31.50182  -17.59328 1.000 30.61035 ? 823 HOH A O     1 
HETATM 4135 O  O     . HOH D 4 .   ? -4.59950  -27.86454 -37.28859 1.000 11.71859 ? 824 HOH A O     1 
HETATM 4136 O  O     . HOH D 4 .   ? 11.71705  -38.04572 -22.22389 1.000 20.55839 ? 825 HOH A O     1 
HETATM 4137 O  O     . HOH D 4 .   ? -1.24706  -0.92316  -18.35097 1.000 22.11403 ? 826 HOH A O     1 
HETATM 4138 O  O     . HOH D 4 .   ? 6.42527   -34.54174 -10.33479 1.000 20.77834 ? 827 HOH A O     1 
HETATM 4139 O  O     . HOH D 4 .   ? 28.71646  -8.55613  -41.65027 1.000 25.61996 ? 828 HOH A O     1 
HETATM 4140 O  O     . HOH D 4 .   ? 8.22302   19.56211  -7.61252  1.000 11.68016 ? 829 HOH A O     1 
HETATM 4141 O  O     . HOH D 4 .   ? 23.98821  -13.77998 -37.69437 1.000 22.78118 ? 830 HOH A O     1 
HETATM 4142 O  O     . HOH D 4 .   ? 16.26069  -26.33325 -9.83164  1.000 22.66193 ? 831 HOH A O     1 
HETATM 4143 O  O     . HOH D 4 .   ? 17.82581  -4.83052  -1.45013  1.000 23.38561 ? 832 HOH A O     1 
HETATM 4144 O  O     . HOH D 4 .   ? 39.10644  -10.39607 -24.03935 1.000 19.83734 ? 833 HOH A O     1 
HETATM 4145 O  O     . HOH D 4 .   ? 1.98900   -17.13064 -47.50536 1.000 22.04705 ? 834 HOH A O     1 
HETATM 4146 O  O     . HOH D 4 .   ? 15.65203  2.08036   -34.11496 1.000 24.61256 ? 835 HOH A O     1 
HETATM 4147 O  O     . HOH D 4 .   ? 24.27902  -18.44923 -27.53948 1.000 14.98291 ? 836 HOH A O     1 
HETATM 4148 O  O     . HOH D 4 .   ? 30.20449  -11.07214 -1.89833  1.000 17.80820 ? 837 HOH A O     1 
HETATM 4149 O  O     . HOH D 4 .   ? 23.67536  8.54792   -32.60484 1.000 17.92660 ? 838 HOH A O     1 
HETATM 4150 O  O     . HOH D 4 .   ? 0.50847   -27.74060 -45.61161 1.000 31.43145 ? 839 HOH A O     1 
HETATM 4151 O  O     . HOH D 4 .   ? 10.07772  -4.48551  -27.96110 1.000 22.97979 ? 840 HOH A O     1 
HETATM 4152 O  O     . HOH D 4 .   ? 21.97554  11.87792  -28.92176 1.000 24.75588 ? 841 HOH A O     1 
HETATM 4153 O  O     . HOH D 4 .   ? 4.28320   -16.31567 -8.44535  1.000 18.47625 ? 842 HOH A O     1 
HETATM 4154 O  O     . HOH D 4 .   ? 12.68225  3.87871   -0.29391  1.000 28.51767 ? 843 HOH A O     1 
HETATM 4155 O  O     . HOH D 4 .   ? 5.16503   -0.40385  -3.02798  1.000 28.55455 ? 844 HOH A O     1 
HETATM 4156 O  O     . HOH D 4 .   ? 21.78841  27.17235  -4.52939  1.000 15.44120 ? 845 HOH A O     1 
HETATM 4157 O  O     . HOH D 4 .   ? 16.79984  -20.42740 -46.64250 1.000 26.67703 ? 846 HOH A O     1 
HETATM 4158 O  O     . HOH D 4 .   ? 4.30266   -26.93769 -7.63260  1.000 23.12381 ? 847 HOH A O     1 
HETATM 4159 O  O     . HOH D 4 .   ? 14.32424  5.27010   -20.26988 1.000 20.37264 ? 848 HOH A O     1 
HETATM 4160 O  O     . HOH D 4 .   ? 38.15929  -13.44905 -22.86042 1.000 24.01477 ? 849 HOH A O     1 
HETATM 4161 O  O     . HOH D 4 .   ? 3.724     -4.323    -41.757   1.000 36.10991 ? 850 HOH A O     1 
HETATM 4162 O  O     . HOH D 4 .   ? 34.33429  6.07503   -17.96794 1.000 19.10864 ? 851 HOH A O     1 
HETATM 4163 O  O     . HOH D 4 .   ? 5.18494   18.25230  -9.18754  1.000 25.02268 ? 852 HOH A O     1 
HETATM 4164 O  O     . HOH D 4 .   ? -0.58897  -37.31280 -35.15483 1.000 28.75676 ? 853 HOH A O     1 
HETATM 4165 O  O     . HOH D 4 .   ? -3.14713  -2.47511  -16.26600 1.000 21.70083 ? 854 HOH A O     1 
HETATM 4166 O  O     . HOH D 4 .   ? 12.11119  4.19919   -19.40790 1.000 32.75080 ? 855 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    C C   . GLY A 3   ? 0.34570 0.29488 0.36768 -0.01404 0.01332  -0.01760 3   GLY A C   
2    O O   . GLY A 3   ? 0.37640 0.32427 0.40408 -0.01611 0.01440  -0.01983 3   GLY A O   
3    N N   . VAL A 4   ? 0.32827 0.27898 0.34707 -0.01245 0.01041  -0.01836 4   VAL A N   
4    C CA  . VAL A 4   ? 0.30838 0.26394 0.32597 -0.01191 0.00718  -0.01906 4   VAL A CA  
5    C C   . VAL A 4   ? 0.26399 0.22157 0.27790 -0.01086 0.00776  -0.01589 4   VAL A C   
6    O O   . VAL A 4   ? 0.24532 0.20064 0.25625 -0.00989 0.00993  -0.01315 4   VAL A O   
7    C CB  . VAL A 4   ? 0.22185 0.17777 0.23623 -0.01042 0.00452  -0.02048 4   VAL A CB  
8    C CG1 . VAL A 4   ? 0.25189 0.20445 0.26861 -0.01106 0.00453  -0.02318 4   VAL A CG1 
9    C CG2 . VAL A 4   ? 0.26491 0.22051 0.27361 -0.00815 0.00506  -0.01769 4   VAL A CG2 
10   N N   . LYS A 5   ? 0.22110 0.18280 0.23500 -0.01092 0.00558  -0.01635 5   LYS A N   
11   C CA  . LYS A 5   ? 0.18878 0.15276 0.19977 -0.01021 0.00581  -0.01387 5   LYS A CA  
12   C C   . LYS A 5   ? 0.16007 0.12624 0.16665 -0.00845 0.00360  -0.01329 5   LYS A C   
13   O O   . LYS A 5   ? 0.16376 0.13191 0.17044 -0.00842 0.00112  -0.01511 5   LYS A O   
14   C CB  . LYS A 5   ? 0.16082 0.12766 0.17530 -0.01162 0.00542  -0.01469 5   LYS A CB  
15   C CG  . LYS A 5   ? 0.19066 0.15959 0.20208 -0.01097 0.00571  -0.01235 5   LYS A CG  
16   C CD  . LYS A 5   ? 0.18442 0.15648 0.19906 -0.01206 0.00478  -0.01349 5   LYS A CD  
17   C CE  . LYS A 5   ? 0.12055 0.09450 0.13180 -0.01137 0.00491  -0.01138 5   LYS A CE  
18   N NZ  . LYS A 5   ? 0.12909 0.10597 0.14331 -0.01223 0.00396  -0.01251 5   LYS A NZ  
19   N N   . ASN A 6   ? 0.17641 0.14210 0.17916 -0.00696 0.00453  -0.01079 6   ASN A N   
20   C CA  . ASN A 6   ? 0.15836 0.12656 0.15759 -0.00547 0.00300  -0.00994 6   ASN A CA  
21   C C   . ASN A 6   ? 0.15182 0.12180 0.14939 -0.00517 0.00357  -0.00768 6   ASN A C   
22   O O   . ASN A 6   ? 0.14648 0.11447 0.14306 -0.00479 0.00538  -0.00586 6   ASN A O   
23   C CB  . ASN A 6   ? 0.15846 0.12489 0.15528 -0.00377 0.00333  -0.00944 6   ASN A CB  
24   C CG  . ASN A 6   ? 0.20283 0.16687 0.20088 -0.00402 0.00298  -0.01179 6   ASN A CG  
25   O OD1 . ASN A 6   ? 0.24824 0.21330 0.24734 -0.00480 0.00122  -0.01403 6   ASN A OD1 
26   N ND2 . ASN A 6   ? 0.14854 0.10915 0.14629 -0.00325 0.00452  -0.01136 6   ASN A ND2 
27   N N   . SER A 7   ? 0.16154 0.13484 0.15846 -0.00529 0.00201  -0.00782 7   SER A N   
28   C CA  . SER A 7   ? 0.14820 0.12326 0.14393 -0.00530 0.00235  -0.00617 7   SER A CA  
29   C C   . SER A 7   ? 0.11597 0.09377 0.10919 -0.00422 0.00102  -0.00546 7   SER A C   
30   O O   . SER A 7   ? 0.12506 0.10372 0.11768 -0.00378 -0.00013 -0.00642 7   SER A O   
31   C CB  . SER A 7   ? 0.15913 0.13554 0.15744 -0.00686 0.00216  -0.00712 7   SER A CB  
32   O OG  . SER A 7   ? 0.14363 0.12207 0.14272 -0.00712 0.00002  -0.00880 7   SER A OG  
33   N N   . ILE A 8   ? 0.10283 0.08179 0.09451 -0.00384 0.00133  -0.00385 8   ILE A N   
34   C CA  . ILE A 8   ? 0.11212 0.09396 0.10217 -0.00311 0.00022  -0.00326 8   ILE A CA  
35   C C   . ILE A 8   ? 0.11056 0.09422 0.10070 -0.00410 -0.00013 -0.00314 8   ILE A C   
36   O O   . ILE A 8   ? 0.14319 0.12581 0.13317 -0.00452 0.00091  -0.00243 8   ILE A O   
37   C CB  . ILE A 8   ? 0.09144 0.07320 0.07969 -0.00147 0.00051  -0.00165 8   ILE A CB  
38   C CG1 . ILE A 8   ? 0.10618 0.08617 0.09449 -0.00028 0.00089  -0.00182 8   ILE A CG1 
39   C CG2 . ILE A 8   ? 0.10138 0.08656 0.08894 -0.00100 -0.00065 -0.00134 8   ILE A CG2 
40   C CD1 . ILE A 8   ? 0.09532 0.07531 0.08229 0.00166  0.00094  -0.00032 8   ILE A CD1 
41   N N   . ILE A 9   ? 0.09585 0.08182 0.08600 -0.00443 -0.00135 -0.00383 9   ILE A N   
42   C CA  . ILE A 9   ? 0.10546 0.09323 0.09548 -0.00516 -0.00177 -0.00370 9   ILE A CA  
43   C C   . ILE A 9   ? 0.09477 0.08467 0.08332 -0.00442 -0.00231 -0.00290 9   ILE A C   
44   O O   . ILE A 9   ? 0.09467 0.08587 0.08313 -0.00419 -0.00291 -0.00331 9   ILE A O   
45   C CB  . ILE A 9   ? 0.12261 0.11102 0.11383 -0.00605 -0.00274 -0.00507 9   ILE A CB  
46   C CG1 . ILE A 9   ? 0.12224 0.11250 0.11301 -0.00656 -0.00321 -0.00488 9   ILE A CG1 
47   C CG2 . ILE A 9   ? 0.08706 0.07527 0.07763 -0.00555 -0.00359 -0.00591 9   ILE A CG2 
48   C CD1 . ILE A 9   ? 0.12109 0.11117 0.11211 -0.00708 -0.00228 -0.00435 9   ILE A CD1 
49   N N   . TRP A 10  ? 0.08475 0.07486 0.07213 -0.00404 -0.00205 -0.00184 10  TRP A N   
50   C CA  . TRP A 10  ? 0.08653 0.07884 0.07306 -0.00322 -0.00284 -0.00127 10  TRP A CA  
51   C C   . TRP A 10  ? 0.10180 0.09619 0.08846 -0.00421 -0.00350 -0.00176 10  TRP A C   
52   O O   . TRP A 10  ? 0.10169 0.09558 0.08765 -0.00485 -0.00326 -0.00168 10  TRP A O   
53   C CB  . TRP A 10  ? 0.11276 0.10398 0.09740 -0.00205 -0.00266 -0.00001 10  TRP A CB  
54   C CG  . TRP A 10  ? 0.10845 0.10219 0.09265 -0.00099 -0.00395 0.00033  10  TRP A CG  
55   C CD1 . TRP A 10  ? 0.12553 0.12232 0.11158 -0.00101 -0.00478 -0.00038 10  TRP A CD1 
56   C CD2 . TRP A 10  ? 0.10260 0.09595 0.08447 0.00029  -0.00459 0.00132  10  TRP A CD2 
57   N NE1 . TRP A 10  ? 0.11405 0.11292 0.09998 0.00006  -0.00603 -0.00010 10  TRP A NE1 
58   C CE2 . TRP A 10  ? 0.13363 0.13040 0.11671 0.00100  -0.00619 0.00093  10  TRP A CE2 
59   C CE3 . TRP A 10  ? 0.13543 0.12563 0.11410 0.00096  -0.00391 0.00248  10  TRP A CE3 
60   C CZ2 . TRP A 10  ? 0.15044 0.14790 0.13181 0.00250  -0.00766 0.00149  10  TRP A CZ2 
61   C CZ3 . TRP A 10  ? 0.16002 0.15031 0.13600 0.00255  -0.00517 0.00329  10  TRP A CZ3 
62   C CH2 . TRP A 10  ? 0.14316 0.13721 0.12057 0.00337  -0.00729 0.00271  10  TRP A CH2 
63   N N   . PHE A 11  ? 0.10746 0.10388 0.09498 -0.00435 -0.00407 -0.00228 11  PHE A N   
64   C CA  . PHE A 11  ? 0.09395 0.09212 0.08172 -0.00531 -0.00456 -0.00274 11  PHE A CA  
65   C C   . PHE A 11  ? 0.09646 0.09686 0.08425 -0.00483 -0.00532 -0.00250 11  PHE A C   
66   O O   . PHE A 11  ? 0.09478 0.09654 0.08345 -0.00382 -0.00562 -0.00233 11  PHE A O   
67   C CB  . PHE A 11  ? 0.09983 0.09850 0.08831 -0.00581 -0.00446 -0.00340 11  PHE A CB  
68   C CG  . PHE A 11  ? 0.08419 0.08084 0.07230 -0.00632 -0.00437 -0.00393 11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.07683 0.07317 0.06490 -0.00721 -0.00466 -0.00432 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.08902 0.08410 0.07695 -0.00578 -0.00418 -0.00420 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.07705 0.07180 0.06515 -0.00742 -0.00498 -0.00494 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.10153 0.09495 0.08929 -0.00613 -0.00458 -0.00495 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.08234 0.07572 0.07030 -0.00688 -0.00508 -0.00532 11  PHE A CZ  
74   N N   . ARG A 12  ? 0.10605 0.10685 0.09303 -0.00547 -0.00573 -0.00266 12  ARG A N   
75   C CA  . ARG A 12  ? 0.11013 0.11320 0.09721 -0.00524 -0.00684 -0.00288 12  ARG A CA  
76   C C   . ARG A 12  ? 0.09592 0.09982 0.08351 -0.00672 -0.00695 -0.00377 12  ARG A C   
77   O O   . ARG A 12  ? 0.14267 0.14845 0.13223 -0.00736 -0.00708 -0.00441 12  ARG A O   
78   C CB  . ARG A 12  ? 0.11224 0.11421 0.09668 -0.00418 -0.00737 -0.00217 12  ARG A CB  
79   C CG  . ARG A 12  ? 0.11574 0.11595 0.09917 -0.00265 -0.00701 -0.00109 12  ARG A CG  
80   C CD  . ARG A 12  ? 0.13413 0.13094 0.11620 -0.00303 -0.00542 -0.00054 12  ARG A CD  
81   N NE  . ARG A 12  ? 0.15482 0.15009 0.13434 -0.00343 -0.00500 -0.00035 12  ARG A NE  
82   C CZ  . ARG A 12  ? 0.14829 0.14165 0.12440 -0.00228 -0.00497 0.00061  12  ARG A CZ  
83   N NH1 . ARG A 12  ? 0.13189 0.12464 0.10688 -0.00054 -0.00557 0.00155  12  ARG A NH1 
84   N NH2 . ARG A 12  ? 0.12798 0.11969 0.10145 -0.00273 -0.00425 0.00066  12  ARG A NH2 
85   N N   . LYS A 13  ? 0.07939 0.08165 0.06536 -0.00729 -0.00663 -0.00381 13  LYS A N   
86   C CA  . LYS A 13  ? 0.07794 0.08009 0.06439 -0.00863 -0.00639 -0.00460 13  LYS A CA  
87   C C   . LYS A 13  ? 0.12007 0.12018 0.10681 -0.00886 -0.00547 -0.00444 13  LYS A C   
88   O O   . LYS A 13  ? 0.09999 0.09934 0.08687 -0.00816 -0.00517 -0.00394 13  LYS A O   
89   C CB  . LYS A 13  ? 0.11356 0.11551 0.09831 -0.00894 -0.00675 -0.00503 13  LYS A CB  
90   C CG  . LYS A 13  ? 0.18006 0.18435 0.16516 -0.00902 -0.00811 -0.00577 13  LYS A CG  
91   C CD  . LYS A 13  ? 0.19631 0.20013 0.17839 -0.00824 -0.00898 -0.00578 13  LYS A CD  
92   C CE  . LYS A 13  ? 0.21090 0.21245 0.19066 -0.00883 -0.00805 -0.00605 13  LYS A CE  
93   N NZ  . LYS A 13  ? 0.25273 0.25463 0.23032 -0.00886 -0.00921 -0.00701 13  LYS A NZ  
94   N N   . GLY A 14  ? 0.07660 0.07583 0.06358 -0.00969 -0.00519 -0.00496 14  GLY A N   
95   C CA  . GLY A 14  ? 0.07693 0.07461 0.06466 -0.00976 -0.00481 -0.00509 14  GLY A CA  
96   C C   . GLY A 14  ? 0.08659 0.08413 0.07474 -0.00948 -0.00504 -0.00503 14  GLY A C   
97   O O   . GLY A 14  ? 0.07571 0.07223 0.06412 -0.00899 -0.00498 -0.00497 14  GLY A O   
98   N N   . LEU A 15  ? 0.07547 0.07378 0.06358 -0.00983 -0.00513 -0.00514 15  LEU A N   
99   C CA  . LEU A 15  ? 0.07586 0.07368 0.06367 -0.00955 -0.00493 -0.00504 15  LEU A CA  
100  C C   . LEU A 15  ? 0.08377 0.07947 0.07070 -0.00966 -0.00517 -0.00532 15  LEU A C   
101  O O   . LEU A 15  ? 0.08236 0.07729 0.06847 -0.01005 -0.00492 -0.00532 15  LEU A O   
102  C CB  . LEU A 15  ? 0.07712 0.07657 0.06553 -0.00995 -0.00449 -0.00504 15  LEU A CB  
103  C CG  . LEU A 15  ? 0.07859 0.08053 0.06824 -0.00965 -0.00478 -0.00498 15  LEU A CG  
104  C CD1 . LEU A 15  ? 0.07564 0.07961 0.06702 -0.01021 -0.00437 -0.00535 15  LEU A CD1 
105  C CD2 . LEU A 15  ? 0.07573 0.07756 0.06525 -0.00846 -0.00480 -0.00450 15  LEU A CD2 
106  N N   . ARG A 16  ? 0.07969 0.07430 0.06691 -0.00922 -0.00570 -0.00559 16  ARG A N   
107  C CA  . ARG A 16  ? 0.10498 0.09779 0.09175 -0.00901 -0.00647 -0.00606 16  ARG A CA  
108  C C   . ARG A 16  ? 0.11294 0.10504 0.10057 -0.00840 -0.00715 -0.00659 16  ARG A C   
109  O O   . ARG A 16  ? 0.09495 0.08774 0.08375 -0.00838 -0.00670 -0.00652 16  ARG A O   
110  C CB  . ARG A 16  ? 0.09510 0.08788 0.08282 -0.00950 -0.00660 -0.00639 16  ARG A CB  
111  C CG  . ARG A 16  ? 0.10534 0.09898 0.09501 -0.00970 -0.00628 -0.00669 16  ARG A CG  
112  C CD  . ARG A 16  ? 0.10631 0.09990 0.09681 -0.01015 -0.00609 -0.00712 16  ARG A CD  
113  N NE  . ARG A 16  ? 0.09818 0.09226 0.09017 -0.01035 -0.00528 -0.00738 16  ARG A NE  
114  C CZ  . ARG A 16  ? 0.09978 0.09451 0.09086 -0.01069 -0.00439 -0.00702 16  ARG A CZ  
115  N NH1 . ARG A 16  ? 0.08820 0.08374 0.07763 -0.01089 -0.00452 -0.00663 16  ARG A NH1 
116  N NH2 . ARG A 16  ? 0.12442 0.11888 0.11624 -0.01077 -0.00332 -0.00714 16  ARG A NH2 
117  N N   . LEU A 17  ? 0.10743 0.09791 0.09438 -0.00784 -0.00833 -0.00717 17  LEU A N   
118  C CA  . LEU A 17  ? 0.10860 0.09854 0.09704 -0.00735 -0.00939 -0.00813 17  LEU A CA  
119  C C   . LEU A 17  ? 0.09462 0.08488 0.08600 -0.00746 -0.01015 -0.00902 17  LEU A C   
120  O O   . LEU A 17  ? 0.08448 0.07509 0.07869 -0.00747 -0.01052 -0.00995 17  LEU A O   
121  C CB  . LEU A 17  ? 0.13818 0.12609 0.12388 -0.00639 -0.01063 -0.00853 17  LEU A CB  
122  C CG  . LEU A 17  ? 0.13614 0.12364 0.12057 -0.00606 -0.01014 -0.00851 17  LEU A CG  
123  C CD1 . LEU A 17  ? 0.13954 0.12727 0.12173 -0.00620 -0.00858 -0.00739 17  LEU A CD1 
124  C CD2 . LEU A 17  ? 0.15930 0.14467 0.14182 -0.00506 -0.01183 -0.00957 17  LEU A CD2 
125  N N   . HIS A 18  ? 0.09249 0.08263 0.08368 -0.00757 -0.01023 -0.00886 18  HIS A N   
126  C CA  . HIS A 18  ? 0.08490 0.07547 0.07922 -0.00754 -0.01079 -0.00977 18  HIS A CA  
127  C C   . HIS A 18  ? 0.08137 0.07343 0.07798 -0.00849 -0.00898 -0.00966 18  HIS A C   
128  O O   . HIS A 18  ? 0.11921 0.11170 0.11409 -0.00906 -0.00774 -0.00876 18  HIS A O   
129  C CB  . HIS A 18  ? 0.11100 0.10030 0.10387 -0.00705 -0.01158 -0.00965 18  HIS A CB  
130  C CG  . HIS A 18  ? 0.09316 0.08261 0.08459 -0.00787 -0.01008 -0.00876 18  HIS A CG  
131  N ND1 . HIS A 18  ? 0.09200 0.08074 0.08024 -0.00815 -0.00941 -0.00779 18  HIS A ND1 
132  C CD2 . HIS A 18  ? 0.08878 0.07900 0.08174 -0.00850 -0.00910 -0.00891 18  HIS A CD2 
133  C CE1 . HIS A 18  ? 0.10937 0.09863 0.09760 -0.00900 -0.00830 -0.00749 18  HIS A CE1 
134  N NE2 . HIS A 18  ? 0.09783 0.08782 0.08851 -0.00917 -0.00816 -0.00814 18  HIS A NE2 
135  N N   . ASP A 19  ? 0.11488 0.10765 0.11538 -0.00863 -0.00883 -0.01068 19  ASP A N   
136  C CA  . ASP A 19  ? 0.10369 0.09729 0.10606 -0.00946 -0.00676 -0.01062 19  ASP A CA  
137  C C   . ASP A 19  ? 0.10098 0.09452 0.10107 -0.00987 -0.00538 -0.00949 19  ASP A C   
138  O O   . ASP A 19  ? 0.10314 0.09683 0.10116 -0.01022 -0.00429 -0.00869 19  ASP A O   
139  C CB  . ASP A 19  ? 0.09736 0.09102 0.09939 -0.00967 -0.00611 -0.01057 19  ASP A CB  
140  C CG  . ASP A 19  ? 0.09062 0.08469 0.09423 -0.01038 -0.00386 -0.01073 19  ASP A CG  
141  O OD1 . ASP A 19  ? 0.09370 0.08798 0.09993 -0.01067 -0.00284 -0.01114 19  ASP A OD1 
142  O OD2 . ASP A 19  ? 0.07975 0.07364 0.08177 -0.01067 -0.00297 -0.01049 19  ASP A OD2 
143  N N   . ASN A 20  ? 0.09505 0.08828 0.09550 -0.00969 -0.00566 -0.00955 20  ASN A N   
144  C CA  . ASN A 20  ? 0.08532 0.07824 0.08388 -0.00977 -0.00454 -0.00852 20  ASN A CA  
145  C C   . ASN A 20  ? 0.08249 0.07480 0.08381 -0.01009 -0.00350 -0.00901 20  ASN A C   
146  O O   . ASN A 20  ? 0.07824 0.07002 0.08020 -0.00983 -0.00421 -0.00946 20  ASN A O   
147  C CB  . ASN A 20  ? 0.09007 0.08275 0.08599 -0.00917 -0.00561 -0.00802 20  ASN A CB  
148  C CG  . ASN A 20  ? 0.09992 0.09268 0.09381 -0.00902 -0.00462 -0.00685 20  ASN A CG  
149  O OD1 . ASN A 20  ? 0.08202 0.07432 0.07630 -0.00917 -0.00334 -0.00642 20  ASN A OD1 
150  N ND2 . ASN A 20  ? 0.08740 0.08058 0.07914 -0.00864 -0.00513 -0.00633 20  ASN A ND2 
151  N N   . PRO A 21  ? 0.07731 0.06941 0.08023 -0.01070 -0.00158 -0.00901 21  PRO A N   
152  C CA  . PRO A 21  ? 0.08435 0.07553 0.09023 -0.01122 -0.00006 -0.00947 21  PRO A CA  
153  C C   . PRO A 21  ? 0.07980 0.06952 0.08337 -0.01095 0.00068  -0.00837 21  PRO A C   
154  O O   . PRO A 21  ? 0.08084 0.06953 0.08685 -0.01129 0.00136  -0.00894 21  PRO A O   
155  C CB  . PRO A 21  ? 0.12842 0.11926 0.13531 -0.01187 0.00239  -0.00935 21  PRO A CB  
156  C CG  . PRO A 21  ? 0.10583 0.09694 0.10854 -0.01152 0.00221  -0.00835 21  PRO A CG  
157  C CD  . PRO A 21  ? 0.12206 0.11441 0.12403 -0.01099 -0.00044 -0.00867 21  PRO A CD  
158  N N   . ALA A 22  ? 0.10177 0.09136 0.10106 -0.01031 0.00052  -0.00694 22  ALA A N   
159  C CA  . ALA A 22  ? 0.08144 0.06974 0.07872 -0.00972 0.00091  -0.00594 22  ALA A CA  
160  C C   . ALA A 22  ? 0.08470 0.07310 0.08291 -0.00936 -0.00065 -0.00675 22  ALA A C   
161  O O   . ALA A 22  ? 0.13477 0.12167 0.13338 -0.00920 -0.00007 -0.00670 22  ALA A O   
162  C CB  . ALA A 22  ? 0.11044 0.09914 0.10363 -0.00894 0.00066  -0.00451 22  ALA A CB  
163  N N   . LEU A 23  ? 0.12823 0.11795 0.12637 -0.00917 -0.00254 -0.00750 23  LEU A N   
164  C CA  . LEU A 23  ? 0.11191 0.10130 0.11016 -0.00872 -0.00405 -0.00840 23  LEU A CA  
165  C C   . LEU A 23  ? 0.10184 0.09067 0.10394 -0.00922 -0.00447 -0.01012 23  LEU A C   
166  O O   . LEU A 23  ? 0.11148 0.09923 0.11401 -0.00901 -0.00496 -0.01087 23  LEU A O   
167  C CB  . LEU A 23  ? 0.09941 0.08969 0.09574 -0.00830 -0.00568 -0.00855 23  LEU A CB  
168  C CG  . LEU A 23  ? 0.16440 0.15386 0.15984 -0.00768 -0.00734 -0.00955 23  LEU A CG  
169  C CD1 . LEU A 23  ? 0.16389 0.15235 0.15775 -0.00714 -0.00680 -0.00919 23  LEU A CD1 
170  C CD2 . LEU A 23  ? 0.11181 0.10149 0.10467 -0.00727 -0.00842 -0.00934 23  LEU A CD2 
171  N N   . LEU A 24  ? 0.09942 0.08908 0.10471 -0.00988 -0.00433 -0.01095 24  LEU A N   
172  C CA  . LEU A 24  ? 0.10767 0.09738 0.11774 -0.01040 -0.00492 -0.01292 24  LEU A CA  
173  C C   . LEU A 24  ? 0.12814 0.11633 0.14038 -0.01113 -0.00289 -0.01302 24  LEU A C   
174  O O   . LEU A 24  ? 0.15021 0.13781 0.16503 -0.01133 -0.00372 -0.01457 24  LEU A O   
175  C CB  . LEU A 24  ? 0.12548 0.11667 0.13913 -0.01089 -0.00485 -0.01378 24  LEU A CB  
176  C CG  . LEU A 24  ? 0.09709 0.08932 0.10874 -0.01015 -0.00667 -0.01365 24  LEU A CG  
177  C CD1 . LEU A 24  ? 0.13358 0.12713 0.14931 -0.01052 -0.00639 -0.01461 24  LEU A CD1 
178  C CD2 . LEU A 24  ? 0.15252 0.14439 0.16258 -0.00916 -0.00961 -0.01454 24  LEU A CD2 
179  N N   . GLU A 25  ? 0.11553 0.10272 0.12650 -0.01148 -0.00023 -0.01141 25  GLU A N   
180  C CA  . GLU A 25  ? 0.13334 0.11831 0.14570 -0.01209 0.00208  -0.01118 25  GLU A CA  
181  C C   . GLU A 25  ? 0.14271 0.12610 0.15251 -0.01132 0.00147  -0.01076 25  GLU A C   
182  O O   . GLU A 25  ? 0.08772 0.06937 0.09984 -0.01180 0.00224  -0.01158 25  GLU A O   
183  C CB  . GLU A 25  ? 0.13283 0.11644 0.14302 -0.01230 0.00500  -0.00930 25  GLU A CB  
184  C CG  . GLU A 25  ? 0.16418 0.14452 0.17410 -0.01261 0.00769  -0.00840 25  GLU A CG  
185  C CD  . GLU A 25  ? 0.19275 0.17230 0.20871 -0.01413 0.00950  -0.01005 25  GLU A CD  
186  O OE1 . GLU A 25  ? 0.16005 0.14143 0.17998 -0.01498 0.00979  -0.01131 25  GLU A OE1 
187  O OE2 . GLU A 25  ? 0.21701 0.19412 0.23412 -0.01450 0.01071  -0.01020 25  GLU A OE2 
188  N N   . ALA A 26  ? 0.15112 0.13508 0.15651 -0.01016 0.00024  -0.00961 26  ALA A N   
189  C CA  . ALA A 26  ? 0.12016 0.10282 0.12316 -0.00925 -0.00019 -0.00923 26  ALA A CA  
190  C C   . ALA A 26  ? 0.13152 0.11401 0.13621 -0.00924 -0.00206 -0.01132 26  ALA A C   
191  O O   . ALA A 26  ? 0.11047 0.09113 0.11479 -0.00891 -0.00183 -0.01165 26  ALA A O   
192  C CB  . ALA A 26  ? 0.13575 0.11959 0.13455 -0.00812 -0.00095 -0.00780 26  ALA A CB  
193  N N   . CYS A 27  ? 0.10573 0.08984 0.11199 -0.00945 -0.00404 -0.01280 27  CYS A N   
194  C CA  . CYS A 27  ? 0.16986 0.15363 0.17698 -0.00920 -0.00630 -0.01491 27  CYS A CA  
195  C C   . CYS A 27  ? 0.14628 0.12970 0.15898 -0.01030 -0.00636 -0.01707 27  CYS A C   
196  O O   . CYS A 27  ? 0.17412 0.15672 0.18768 -0.01014 -0.00808 -0.01902 27  CYS A O   
197  C CB  . CYS A 27  ? 0.14933 0.13456 0.15484 -0.00855 -0.00876 -0.01546 27  CYS A CB  
198  S SG  . CYS A 27  ? 0.20478 0.19023 0.20422 -0.00743 -0.00875 -0.01344 27  CYS A SG  
199  N N   . LYS A 28  ? 0.14799 0.13192 0.16455 -0.01144 -0.00442 -0.01692 28  LYS A N   
200  C CA  . LYS A 28  ? 0.19499 0.17911 0.21804 -0.01271 -0.00428 -0.01921 28  LYS A CA  
201  C C   . LYS A 28  ? 0.16573 0.14718 0.19001 -0.01328 -0.00285 -0.01974 28  LYS A C   
202  O O   . LYS A 28  ? 0.15682 0.13613 0.17908 -0.01338 -0.00004 -0.01777 28  LYS A O   
203  C CB  . LYS A 28  ? 0.18159 0.16676 0.20828 -0.01380 -0.00192 -0.01876 28  LYS A CB  
204  C CG  . LYS A 28  ? 0.22399 0.21013 0.25860 -0.01521 -0.00164 -0.02135 28  LYS A CG  
205  C CD  . LYS A 28  ? 0.20866 0.19592 0.24641 -0.01613 0.00099  -0.02080 28  LYS A CD  
206  C CE  . LYS A 28  ? 0.21867 0.20675 0.26515 -0.01780 0.00226  -0.02329 28  LYS A CE  
207  N NZ  . LYS A 28  ? 0.21785 0.20628 0.26697 -0.01879 0.00587  -0.02251 28  LYS A NZ  
208  N N   . ASP A 29  ? 0.15314 0.13445 0.18045 -0.01353 -0.00495 -0.02247 29  ASP A N   
209  C CA  . ASP A 29  ? 0.18518 0.16381 0.21424 -0.01420 -0.00388 -0.02354 29  ASP A CA  
210  C C   . ASP A 29  ? 0.18094 0.15700 0.20384 -0.01299 -0.00303 -0.02159 29  ASP A C   
211  O O   . ASP A 29  ? 0.22375 0.19694 0.24713 -0.01342 -0.00086 -0.02126 29  ASP A O   
212  C CB  . ASP A 29  ? 0.21100 0.18853 0.24546 -0.01603 -0.00031 -0.02352 29  ASP A CB  
213  C CG  . ASP A 29  ? 0.22976 0.21011 0.27149 -0.01730 -0.00082 -0.02574 29  ASP A CG  
214  O OD1 . ASP A 29  ? 0.20380 0.18604 0.24865 -0.01717 -0.00430 -0.02860 29  ASP A OD1 
215  O OD2 . ASP A 29  ? 0.25502 0.23565 0.29924 -0.01830 0.00221  -0.02469 29  ASP A OD2 
216  N N   . ALA A 30  ? 0.12795 0.10493 0.14539 -0.01146 -0.00468 -0.02044 30  ALA A N   
217  C CA  . ALA A 30  ? 0.15450 0.12971 0.16657 -0.01016 -0.00383 -0.01858 30  ALA A CA  
218  C C   . ALA A 30  ? 0.15897 0.13304 0.16852 -0.00920 -0.00600 -0.02028 30  ALA A C   
219  O O   . ALA A 30  ? 0.10611 0.08147 0.11489 -0.00879 -0.00871 -0.02175 30  ALA A O   
220  C CB  . ALA A 30  ? 0.17439 0.15138 0.18254 -0.00927 -0.00368 -0.01620 30  ALA A CB  
221  N N   . LYS A 31  ? 0.15831 0.12968 0.16632 -0.00872 -0.00469 -0.01998 31  LYS A N   
222  C CA  . LYS A 31  ? 0.20069 0.17050 0.20573 -0.00769 -0.00628 -0.02155 31  LYS A CA  
223  C C   . LYS A 31  ? 0.20489 0.17557 0.20437 -0.00608 -0.00641 -0.01970 31  LYS A C   
224  O O   . LYS A 31  ? 0.17693 0.14742 0.17323 -0.00522 -0.00822 -0.02084 31  LYS A O   
225  C CB  . LYS A 31  ? 0.24709 0.21348 0.25304 -0.00780 -0.00465 -0.02215 31  LYS A CB  
226  C CG  . LYS A 31  ? 0.32243 0.28678 0.32588 -0.00693 -0.00621 -0.02436 31  LYS A CG  
227  C CD  . LYS A 31  ? 0.30733 0.27262 0.31156 -0.00725 -0.00958 -0.02735 31  LYS A CD  
228  C CE  . LYS A 31  ? 0.34916 0.31165 0.35438 -0.00748 -0.01071 -0.03053 31  LYS A CE  
229  N NZ  . LYS A 31  ? 0.33986 0.29997 0.34919 -0.00864 -0.00808 -0.03057 31  LYS A NZ  
230  N N   . HIS A 32  ? 0.20153 0.17280 0.19998 -0.00569 -0.00438 -0.01703 32  HIS A N   
231  C CA  . HIS A 32  ? 0.18139 0.15397 0.17566 -0.00434 -0.00427 -0.01534 32  HIS A CA  
232  C C   . HIS A 32  ? 0.15781 0.13285 0.15229 -0.00459 -0.00356 -0.01316 32  HIS A C   
233  O O   . HIS A 32  ? 0.13938 0.11406 0.13592 -0.00520 -0.00212 -0.01215 32  HIS A O   
234  C CB  . HIS A 32  ? 0.17386 0.14451 0.16613 -0.00306 -0.00289 -0.01474 32  HIS A CB  
235  C CG  . HIS A 32  ? 0.18696 0.15505 0.17815 -0.00262 -0.00351 -0.01692 32  HIS A CG  
236  N ND1 . HIS A 32  ? 0.25667 0.22192 0.25013 -0.00307 -0.00279 -0.01809 32  HIS A ND1 
237  C CD2 . HIS A 32  ? 0.18772 0.15524 0.17551 -0.00176 -0.00458 -0.01815 32  HIS A CD2 
238  C CE1 . HIS A 32  ? 0.19474 0.15798 0.18634 -0.00250 -0.00366 -0.02016 32  HIS A CE1 
239  N NE2 . HIS A 32  ? 0.18072 0.14522 0.16858 -0.00163 -0.00473 -0.02020 32  HIS A NE2 
240  N N   . VAL A 33  ? 0.14718 0.12430 0.13933 -0.00416 -0.00443 -0.01257 33  VAL A N   
241  C CA  . VAL A 33  ? 0.15013 0.12957 0.14219 -0.00435 -0.00394 -0.01077 33  VAL A CA  
242  C C   . VAL A 33  ? 0.11089 0.09150 0.10018 -0.00324 -0.00352 -0.00954 33  VAL A C   
243  O O   . VAL A 33  ? 0.13577 0.11629 0.12281 -0.00273 -0.00415 -0.01022 33  VAL A O   
244  C CB  . VAL A 33  ? 0.14165 0.12266 0.13457 -0.00518 -0.00537 -0.01144 33  VAL A CB  
245  C CG1 . VAL A 33  ? 0.11513 0.09830 0.10756 -0.00535 -0.00483 -0.00974 33  VAL A CG1 
246  C CG2 . VAL A 33  ? 0.14205 0.12247 0.13888 -0.00631 -0.00566 -0.01283 33  VAL A CG2 
247  N N   . TYR A 34  ? 0.09213 0.07370 0.08156 -0.00283 -0.00241 -0.00781 34  TYR A N   
248  C CA  . TYR A 34  ? 0.10269 0.08596 0.09068 -0.00183 -0.00204 -0.00679 34  TYR A CA  
249  C C   . TYR A 34  ? 0.11103 0.09692 0.09906 -0.00235 -0.00237 -0.00583 34  TYR A C   
250  O O   . TYR A 34  ? 0.11194 0.09845 0.10052 -0.00231 -0.00200 -0.00469 34  TYR A O   
251  C CB  . TYR A 34  ? 0.11973 0.10221 0.10800 -0.00060 -0.00096 -0.00578 34  TYR A CB  
252  C CG  . TYR A 34  ? 0.12254 0.10214 0.11076 0.00002  -0.00042 -0.00674 34  TYR A CG  
253  C CD1 . TYR A 34  ? 0.13137 0.10830 0.12083 -0.00060 -0.00006 -0.00726 34  TYR A CD1 
254  C CD2 . TYR A 34  ? 0.14457 0.12400 0.13172 0.00115  -0.00004 -0.00725 34  TYR A CD2 
255  C CE1 . TYR A 34  ? 0.15653 0.13060 0.14610 -0.00014 0.00044  -0.00833 34  TYR A CE1 
256  C CE2 . TYR A 34  ? 0.18194 0.15849 0.16885 0.00177  0.00050  -0.00830 34  TYR A CE2 
257  C CZ  . TYR A 34  ? 0.15999 0.13382 0.14809 0.00110  0.00062  -0.00887 34  TYR A CZ  
258  O OH  . TYR A 34  ? 0.20940 0.18015 0.19740 0.00161  0.00115  -0.01010 34  TYR A OH  
259  N N   . PRO A 35  ? 0.10562 0.09269 0.09270 -0.00279 -0.00302 -0.00627 35  PRO A N   
260  C CA  . PRO A 35  ? 0.10053 0.08990 0.08774 -0.00335 -0.00324 -0.00551 35  PRO A CA  
261  C C   . PRO A 35  ? 0.10875 0.10017 0.09610 -0.00260 -0.00267 -0.00466 35  PRO A C   
262  O O   . PRO A 35  ? 0.12677 0.11851 0.11358 -0.00209 -0.00215 -0.00495 35  PRO A O   
263  C CB  . PRO A 35  ? 0.08379 0.07293 0.06970 -0.00390 -0.00398 -0.00631 35  PRO A CB  
264  C CG  . PRO A 35  ? 0.10651 0.09322 0.09164 -0.00365 -0.00456 -0.00760 35  PRO A CG  
265  C CD  . PRO A 35  ? 0.10069 0.08646 0.08612 -0.00280 -0.00366 -0.00755 35  PRO A CD  
266  N N   . VAL A 36  ? 0.08259 0.07537 0.07072 -0.00249 -0.00274 -0.00372 36  VAL A N   
267  C CA  . VAL A 36  ? 0.13217 0.12701 0.12107 -0.00148 -0.00263 -0.00307 36  VAL A CA  
268  C C   . VAL A 36  ? 0.11900 0.11636 0.10839 -0.00210 -0.00326 -0.00278 36  VAL A C   
269  O O   . VAL A 36  ? 0.13369 0.13063 0.12246 -0.00275 -0.00365 -0.00251 36  VAL A O   
270  C CB  . VAL A 36  ? 0.14253 0.13613 0.13143 -0.00020 -0.00247 -0.00225 36  VAL A CB  
271  C CG1 . VAL A 36  ? 0.18347 0.17957 0.17328 0.00101  -0.00299 -0.00159 36  VAL A CG1 
272  C CG2 . VAL A 36  ? 0.11179 0.10305 0.10058 0.00053  -0.00173 -0.00270 36  VAL A CG2 
273  N N   . PHE A 37  ? 0.11862 0.11854 0.10933 -0.00196 -0.00320 -0.00299 37  PHE A N   
274  C CA  . PHE A 37  ? 0.10838 0.11108 0.10026 -0.00226 -0.00397 -0.00291 37  PHE A CA  
275  C C   . PHE A 37  ? 0.15704 0.16203 0.15097 -0.00079 -0.00429 -0.00278 37  PHE A C   
276  O O   . PHE A 37  ? 0.11960 0.12533 0.11505 -0.00027 -0.00338 -0.00317 37  PHE A O   
277  C CB  . PHE A 37  ? 0.12049 0.12444 0.11301 -0.00366 -0.00360 -0.00356 37  PHE A CB  
278  C CG  . PHE A 37  ? 0.13907 0.14575 0.13307 -0.00423 -0.00444 -0.00379 37  PHE A CG  
279  C CD1 . PHE A 37  ? 0.15430 0.16416 0.15126 -0.00381 -0.00460 -0.00421 37  PHE A CD1 
280  C CD2 . PHE A 37  ? 0.11216 0.11828 0.10492 -0.00519 -0.00509 -0.00380 37  PHE A CD2 
281  C CE1 . PHE A 37  ? 0.15806 0.17052 0.15669 -0.00440 -0.00565 -0.00475 37  PHE A CE1 
282  C CE2 . PHE A 37  ? 0.12190 0.13027 0.11577 -0.00573 -0.00597 -0.00425 37  PHE A CE2 
283  C CZ  . PHE A 37  ? 0.16854 0.18009 0.16535 -0.00538 -0.00637 -0.00478 37  PHE A CZ  
284  N N   . VAL A 38  ? 0.13306 0.13907 0.12693 0.00001  -0.00559 -0.00230 38  VAL A N   
285  C CA  . VAL A 38  ? 0.14674 0.15486 0.14252 0.00181  -0.00644 -0.00216 38  VAL A CA  
286  C C   . VAL A 38  ? 0.18262 0.19494 0.18164 0.00129  -0.00726 -0.00313 38  VAL A C   
287  O O   . VAL A 38  ? 0.16893 0.18214 0.16741 0.00033  -0.00826 -0.00341 38  VAL A O   
288  C CB  . VAL A 38  ? 0.17446 0.18085 0.16777 0.00332  -0.00762 -0.00107 38  VAL A CB  
289  C CG1 . VAL A 38  ? 0.16698 0.17586 0.16229 0.00546  -0.00910 -0.00101 38  VAL A CG1 
290  C CG2 . VAL A 38  ? 0.14064 0.14283 0.13160 0.00374  -0.00641 -0.00023 38  VAL A CG2 
291  N N   . LEU A 39  ? 0.15617 0.17106 0.15885 0.00188  -0.00669 -0.00379 39  LEU A N   
292  C CA  . LEU A 39  ? 0.20659 0.22576 0.21355 0.00123  -0.00709 -0.00497 39  LEU A CA  
293  C C   . LEU A 39  ? 0.26786 0.29026 0.27822 0.00334  -0.00875 -0.00528 39  LEU A C   
294  O O   . LEU A 39  ? 0.26393 0.28563 0.27471 0.00517  -0.00839 -0.00481 39  LEU A O   
295  C CB  . LEU A 39  ? 0.28251 0.30221 0.29159 -0.00005 -0.00461 -0.00569 39  LEU A CB  
296  C CG  . LEU A 39  ? 0.29917 0.32241 0.31244 -0.00159 -0.00416 -0.00694 39  LEU A CG  
297  C CD1 . LEU A 39  ? 0.32125 0.34308 0.33218 -0.00363 -0.00426 -0.00699 39  LEU A CD1 
298  C CD2 . LEU A 39  ? 0.20632 0.23014 0.22217 -0.00203 -0.00133 -0.00751 39  LEU A CD2 
299  N N   . ASP A 40  ? 0.33063 0.35649 0.34350 0.00320  -0.01073 -0.00620 40  ASP A N   
300  C CA  A ASP A 40  ? 0.34694 0.37646 0.36367 0.00531  -0.01284 -0.00680 40  ASP A CA  
301  C CA  B ASP A 40  ? 0.34687 0.37639 0.36359 0.00531  -0.01285 -0.00681 40  ASP A CA  
302  C C   . ASP A 40  ? 0.38450 0.41882 0.40828 0.00439  -0.01191 -0.00856 40  ASP A C   
303  O O   . ASP A 40  ? 0.38964 0.42633 0.41576 0.00253  -0.01228 -0.00979 40  ASP A O   
304  C CB  A ASP A 40  ? 0.37400 0.40418 0.38875 0.00608  -0.01612 -0.00688 40  ASP A CB  
305  C CB  B ASP A 40  ? 0.37461 0.40481 0.38937 0.00607  -0.01613 -0.00689 40  ASP A CB  
306  C CG  A ASP A 40  ? 0.36921 0.40169 0.38592 0.00911  -0.01886 -0.00699 40  ASP A CG  
307  C CG  B ASP A 40  ? 0.33014 0.35523 0.33767 0.00631  -0.01632 -0.00523 40  ASP A CG  
308  O OD1 A ASP A 40  ? 0.33793 0.36738 0.35147 0.01130  -0.01902 -0.00550 40  ASP A OD1 
309  O OD1 B ASP A 40  ? 0.31538 0.33698 0.32022 0.00524  -0.01400 -0.00436 40  ASP A OD1 
310  O OD2 A ASP A 40  ? 0.41555 0.45281 0.43718 0.00933  -0.02093 -0.00866 40  ASP A OD2 
311  O OD2 B ASP A 40  ? 0.38657 0.41107 0.39112 0.00762  -0.01876 -0.00488 40  ASP A OD2 
312  N N   . PRO A 41  ? 0.41514 0.45092 0.44271 0.00553  -0.01045 -0.00885 41  PRO A N   
313  C CA  . PRO A 41  ? 0.40243 0.44270 0.43714 0.00448  -0.00889 -0.01059 41  PRO A CA  
314  C C   . PRO A 41  ? 0.48157 0.52758 0.52264 0.00538  -0.01176 -0.01226 41  PRO A C   
315  O O   . PRO A 41  ? 0.57160 0.62174 0.61935 0.00401  -0.01057 -0.01400 41  PRO A O   
316  C CB  . PRO A 41  ? 0.49814 0.53757 0.53415 0.00577  -0.00635 -0.01029 41  PRO A CB  
317  C CG  . PRO A 41  ? 0.39789 0.43471 0.43013 0.00847  -0.00823 -0.00891 41  PRO A CG  
318  C CD  . PRO A 41  ? 0.36488 0.39807 0.39052 0.00778  -0.00984 -0.00770 41  PRO A CD  
319  N N   . HIS A 42  ? 0.45435 0.50060 0.49355 0.00764  -0.01548 -0.01186 42  HIS A N   
320  C CA  . HIS A 42  ? 0.49920 0.55073 0.54372 0.00870  -0.01900 -0.01360 42  HIS A CA  
321  C C   . HIS A 42  ? 0.48551 0.53694 0.52727 0.00726  -0.02138 -0.01417 42  HIS A C   
322  O O   . HIS A 42  ? 0.50674 0.56181 0.55130 0.00833  -0.02506 -0.01561 42  HIS A O   
323  C CB  . HIS A 42  ? 0.49231 0.54414 0.53643 0.01259  -0.02191 -0.01293 42  HIS A CB  
324  C CG  . HIS A 42  ? 0.47931 0.53043 0.52534 0.01417  -0.01949 -0.01226 42  HIS A CG  
325  N ND1 . HIS A 42  ? 0.49322 0.54927 0.54786 0.01462  -0.01832 -0.01393 42  HIS A ND1 
326  C CD2 . HIS A 42  ? 0.44870 0.49465 0.48932 0.01530  -0.01781 -0.01029 42  HIS A CD2 
327  C CE1 . HIS A 42  ? 0.47208 0.52587 0.52610 0.01610  -0.01605 -0.01296 42  HIS A CE1 
328  N NE2 . HIS A 42  ? 0.49425 0.54188 0.53980 0.01651  -0.01582 -0.01079 42  HIS A NE2 
329  N N   . PHE A 43  ? 0.45325 0.50056 0.48961 0.00499  -0.01947 -0.01321 43  PHE A N   
330  C CA  . PHE A 43  ? 0.49126 0.53843 0.52577 0.00301  -0.02073 -0.01403 43  PHE A CA  
331  C C   . PHE A 43  ? 0.47200 0.52449 0.51437 0.00112  -0.02096 -0.01665 43  PHE A C   
332  O O   . PHE A 43  ? 0.50101 0.55428 0.54295 -0.00013 -0.02283 -0.01784 43  PHE A O   
333  C CB  . PHE A 43  ? 0.46954 0.51158 0.49826 0.00093  -0.01786 -0.01260 43  PHE A CB  
334  C CG  . PHE A 43  ? 0.50385 0.54454 0.52930 -0.00081 -0.01888 -0.01304 43  PHE A CG  
335  C CD1 . PHE A 43  ? 0.50421 0.54269 0.52400 0.00052  -0.02148 -0.01236 43  PHE A CD1 
336  C CD2 . PHE A 43  ? 0.50482 0.54586 0.53237 -0.00370 -0.01692 -0.01403 43  PHE A CD2 
337  C CE1 . PHE A 43  ? 0.51580 0.55287 0.53249 -0.00102 -0.02218 -0.01289 43  PHE A CE1 
338  C CE2 . PHE A 43  ? 0.45514 0.49472 0.47977 -0.00521 -0.01776 -0.01452 43  PHE A CE2 
339  C CZ  . PHE A 43  ? 0.52878 0.56651 0.54808 -0.00387 -0.02039 -0.01403 43  PHE A CZ  
340  N N   . LEU A 44  ? 0.44322 0.49931 0.49290 0.00085  -0.01899 -0.01770 44  LEU A N   
341  C CA  . LEU A 44  ? 0.48711 0.54866 0.54552 -0.00091 -0.01896 -0.02038 44  LEU A CA  
342  C C   . LEU A 44  ? 0.54547 0.61276 0.61007 0.00135  -0.02313 -0.02231 44  LEU A C   
343  O O   . LEU A 44  ? 0.56346 0.63607 0.63654 0.00003  -0.02356 -0.02493 44  LEU A O   
344  C CB  . LEU A 44  ? 0.51208 0.57457 0.57566 -0.00251 -0.01420 -0.02069 44  LEU A CB  
345  C CG  . LEU A 44  ? 0.44346 0.50385 0.50664 -0.00610 -0.01061 -0.02088 44  LEU A CG  
346  C CD1 . LEU A 44  ? 0.40837 0.47281 0.47756 -0.00817 -0.01206 -0.02348 44  LEU A CD1 
347  C CD2 . LEU A 44  ? 0.41131 0.46528 0.46467 -0.00664 -0.01012 -0.01870 44  LEU A CD2 
348  N N   . GLN A 45  ? 0.54692 0.61315 0.60763 0.00476  -0.02622 -0.02112 45  GLN A N   
349  C CA  . GLN A 45  ? 0.55336 0.62434 0.61839 0.00740  -0.03105 -0.02280 45  GLN A CA  
350  C C   . GLN A 45  ? 0.53802 0.60621 0.59521 0.00860  -0.03517 -0.02227 45  GLN A C   
351  O O   . GLN A 45  ? 0.56747 0.63422 0.62047 0.01201  -0.03821 -0.02112 45  GLN A O   
352  C CB  . GLN A 45  ? 0.53751 0.60939 0.60445 0.01091  -0.03152 -0.02191 45  GLN A CB  
353  C CG  . GLN A 45  ? 0.52353 0.59847 0.59858 0.01011  -0.02752 -0.02270 45  GLN A CG  
354  C CD  . GLN A 45  ? 0.51451 0.58392 0.58409 0.00980  -0.02306 -0.02018 45  GLN A CD  
355  O OE1 . GLN A 45  ? 0.50773 0.57514 0.57493 0.01258  -0.02320 -0.01869 45  GLN A OE1 
356  N NE2 . GLN A 45  ? 0.51005 0.57678 0.57752 0.00650  -0.01921 -0.01978 45  GLN A NE2 
357  N N   . GLN A 46  ? 0.54061 0.60745 0.59522 0.00590  -0.03500 -0.02297 46  GLN A N   
358  C CA  . GLN A 46  ? 0.53804 0.60152 0.58439 0.00675  -0.03821 -0.02244 46  GLN A CA  
359  C C   . GLN A 46  ? 0.52664 0.59381 0.57654 0.00524  -0.04121 -0.02552 46  GLN A C   
360  O O   . GLN A 46  ? 0.62558 0.69692 0.67904 0.00723  -0.04572 -0.02749 46  GLN A O   
361  C CB  . GLN A 46  ? 0.52357 0.58033 0.56122 0.00517  -0.03500 -0.02000 46  GLN A CB  
362  C CG  . GLN A 46  ? 0.50116 0.55745 0.53963 0.00137  -0.03280 -0.02110 46  GLN A CG  
363  C CD  . GLN A 46  ? 0.49128 0.54283 0.52105 0.00092  -0.03365 -0.02028 46  GLN A CD  
364  O OE1 . GLN A 46  ? 0.46297 0.51278 0.49172 -0.00183 -0.03160 -0.02062 46  GLN A OE1 
365  N NE2 . GLN A 46  ? 0.50111 0.55025 0.52441 0.00374  -0.03650 -0.01917 46  GLN A NE2 
366  N N   . LYS A 50  ? 0.26885 0.33173 0.32595 -0.01333 -0.02841 -0.03093 50  LYS A N   
367  C CA  . LYS A 50  ? 0.20590 0.26341 0.25254 -0.01154 -0.02907 -0.02835 50  LYS A CA  
368  C C   . LYS A 50  ? 0.29760 0.34971 0.33950 -0.01324 -0.02467 -0.02607 50  LYS A C   
369  O O   . LYS A 50  ? 0.25525 0.30326 0.29078 -0.01376 -0.02465 -0.02539 50  LYS A O   
370  C CB  . LYS A 50  ? 0.26890 0.32670 0.31329 -0.00804 -0.03062 -0.02659 50  LYS A CB  
371  N N   . VAL A 51  ? 0.26676 0.31882 0.31171 -0.01395 -0.02100 -0.02498 51  VAL A N   
372  C CA  . VAL A 51  ? 0.19080 0.23780 0.23130 -0.01517 -0.01707 -0.02281 51  VAL A CA  
373  C C   . VAL A 51  ? 0.18095 0.22890 0.22739 -0.01777 -0.01338 -0.02362 51  VAL A C   
374  O O   . VAL A 51  ? 0.25337 0.30488 0.30607 -0.01763 -0.01227 -0.02428 51  VAL A O   
375  C CB  . VAL A 51  ? 0.25563 0.30009 0.29165 -0.01300 -0.01603 -0.02014 51  VAL A CB  
376  C CG1 . VAL A 51  ? 0.18256 0.22180 0.21369 -0.01413 -0.01265 -0.01819 51  VAL A CG1 
377  C CG2 . VAL A 51  ? 0.35398 0.39748 0.38464 -0.01036 -0.01940 -0.01931 51  VAL A CG2 
378  N N   . SER A 52  ? 0.15140 0.19594 0.19583 -0.02005 -0.01128 -0.02354 52  SER A N   
379  C CA  A SER A 52  ? 0.13732 0.18140 0.18599 -0.02250 -0.00727 -0.02389 52  SER A CA  
380  C CA  B SER A 52  ? 0.13596 0.18005 0.18464 -0.02250 -0.00727 -0.02389 52  SER A CA  
381  C C   . SER A 52  ? 0.11433 0.15483 0.15943 -0.02190 -0.00380 -0.02133 52  SER A C   
382  O O   . SER A 52  ? 0.11706 0.15445 0.15568 -0.02015 -0.00436 -0.01931 52  SER A O   
383  C CB  A SER A 52  ? 0.10311 0.14417 0.15047 -0.02498 -0.00626 -0.02461 52  SER A CB  
384  C CB  B SER A 52  ? 0.10601 0.14708 0.15337 -0.02497 -0.00626 -0.02461 52  SER A CB  
385  O OG  A SER A 52  ? 0.11095 0.15038 0.16121 -0.02723 -0.00194 -0.02449 52  SER A OG  
386  O OG  B SER A 52  ? 0.10323 0.13885 0.14235 -0.02437 -0.00591 -0.02251 52  SER A OG  
387  N N   . VAL A 53  ? 0.11677 0.15759 0.16619 -0.02343 -0.00007 -0.02156 53  VAL A N   
388  C CA  . VAL A 53  ? 0.10917 0.14611 0.15465 -0.02294 0.00337  -0.01932 53  VAL A CA  
389  C C   . VAL A 53  ? 0.11076 0.14138 0.14862 -0.02347 0.00452  -0.01754 53  VAL A C   
390  O O   . VAL A 53  ? 0.09357 0.12049 0.12612 -0.02236 0.00593  -0.01554 53  VAL A O   
391  C CB  . VAL A 53  ? 0.13888 0.17720 0.19037 -0.02449 0.00749  -0.02003 53  VAL A CB  
392  C CG1 . VAL A 53  ? 0.11799 0.15433 0.17134 -0.02751 0.01000  -0.02089 53  VAL A CG1 
393  C CG2 . VAL A 53  ? 0.18993 0.22478 0.23723 -0.02340 0.01064  -0.01791 53  VAL A CG2 
394  N N   . ASN A 54  ? 0.11207 0.14141 0.14936 -0.02502 0.00372  -0.01839 54  ASN A N   
395  C CA  . ASN A 54  ? 0.09198 0.11547 0.12262 -0.02539 0.00469  -0.01685 54  ASN A CA  
396  C C   . ASN A 54  ? 0.09064 0.11225 0.11499 -0.02314 0.00234  -0.01532 54  ASN A C   
397  O O   . ASN A 54  ? 0.10812 0.12553 0.12726 -0.02241 0.00361  -0.01348 54  ASN A O   
398  C CB  . ASN A 54  ? 0.08370 0.10648 0.11558 -0.02739 0.00419  -0.01834 54  ASN A CB  
399  C CG  . ASN A 54  ? 0.09796 0.11966 0.13386 -0.02997 0.00783  -0.01908 54  ASN A CG  
400  O OD1 . ASN A 54  ? 0.10792 0.12843 0.14442 -0.03022 0.01116  -0.01812 54  ASN A OD1 
401  N ND2 . ASN A 54  ? 0.08763 0.10935 0.12604 -0.03193 0.00744  -0.02083 54  ASN A ND2 
402  N N   . ARG A 55  ? 0.08997 0.11445 0.11465 -0.02200 -0.00108 -0.01613 55  ARG A N   
403  C CA  . ARG A 55  ? 0.09015 0.11258 0.10909 -0.02008 -0.00289 -0.01472 55  ARG A CA  
404  C C   . ARG A 55  ? 0.08657 0.10911 0.10429 -0.01820 -0.00246 -0.01331 55  ARG A C   
405  O O   . ARG A 55  ? 0.08351 0.10275 0.09634 -0.01716 -0.00225 -0.01175 55  ARG A O   
406  C CB  . ARG A 55  ? 0.11106 0.13573 0.12978 -0.01934 -0.00634 -0.01585 55  ARG A CB  
407  C CG  . ARG A 55  ? 0.07935 0.10181 0.09240 -0.01741 -0.00774 -0.01436 55  ARG A CG  
408  C CD  . ARG A 55  ? 0.13315 0.15624 0.14430 -0.01689 -0.01052 -0.01530 55  ARG A CD  
409  N NE  . ARG A 55  ? 0.09944 0.12638 0.11283 -0.01553 -0.01305 -0.01618 55  ARG A NE  
410  C CZ  . ARG A 55  ? 0.15719 0.18772 0.17484 -0.01620 -0.01479 -0.01835 55  ARG A CZ  
411  N NH1 . ARG A 55  ? 0.16437 0.19511 0.18479 -0.01847 -0.01403 -0.01994 55  ARG A NH1 
412  N NH2 . ARG A 55  ? 0.13368 0.16755 0.15295 -0.01450 -0.01749 -0.01903 55  ARG A NH2 
413  N N   . TYR A 56  ? 0.10135 0.12770 0.12380 -0.01772 -0.00237 -0.01401 56  TYR A N   
414  C CA  . TYR A 56  ? 0.10536 0.13173 0.12673 -0.01580 -0.00202 -0.01282 56  TYR A CA  
415  C C   . TYR A 56  ? 0.11008 0.13268 0.12871 -0.01611 0.00118  -0.01151 56  TYR A C   
416  O O   . TYR A 56  ? 0.09763 0.11798 0.11245 -0.01465 0.00127  -0.01020 56  TYR A O   
417  C CB  . TYR A 56  ? 0.09453 0.12596 0.12207 -0.01507 -0.00264 -0.01402 56  TYR A CB  
418  C CG  . TYR A 56  ? 0.18261 0.21447 0.20878 -0.01255 -0.00364 -0.01302 56  TYR A CG  
419  C CD1 . TYR A 56  ? 0.17791 0.20812 0.20317 -0.01188 -0.00118 -0.01201 56  TYR A CD1 
420  C CD2 . TYR A 56  ? 0.16711 0.20049 0.19238 -0.01076 -0.00695 -0.01308 56  TYR A CD2 
421  C CE1 . TYR A 56  ? 0.23649 0.26677 0.26058 -0.00961 -0.00200 -0.01120 56  TYR A CE1 
422  C CE2 . TYR A 56  ? 0.18699 0.22019 0.21084 -0.00843 -0.00769 -0.01205 56  TYR A CE2 
423  C CZ  . TYR A 56  ? 0.28325 0.31500 0.30680 -0.00792 -0.00520 -0.01117 56  TYR A CZ  
424  O OH  . TYR A 56  ? 0.31381 0.34511 0.33607 -0.00564 -0.00586 -0.01027 56  TYR A OH  
425  N N   . ASN A 57  ? 0.10735 0.12888 0.12760 -0.01799 0.00383  -0.01188 57  ASN A N   
426  C CA  . ASN A 57  ? 0.08947 0.10654 0.10583 -0.01815 0.00680  -0.01053 57  ASN A CA  
427  C C   . ASN A 57  ? 0.11481 0.12724 0.12474 -0.01780 0.00598  -0.00930 57  ASN A C   
428  O O   . ASN A 57  ? 0.14469 0.15367 0.15016 -0.01683 0.00684  -0.00805 57  ASN A O   
429  C CB  . ASN A 57  ? 0.14569 0.16221 0.16500 -0.02023 0.01014  -0.01111 57  ASN A CB  
430  C CG  . ASN A 57  ? 0.17514 0.18678 0.18989 -0.02013 0.01343  -0.00967 57  ASN A CG  
431  O OD1 . ASN A 57  ? 0.24534 0.25254 0.25637 -0.02104 0.01486  -0.00891 57  ASN A OD1 
432  N ND2 . ASN A 57  ? 0.18576 0.19787 0.20033 -0.01881 0.01457  -0.00928 57  ASN A ND2 
433  N N   . PHE A 58  ? 0.10368 0.11604 0.11327 -0.01850 0.00422  -0.00980 58  PHE A N   
434  C CA  . PHE A 58  ? 0.09922 0.10782 0.10362 -0.01799 0.00321  -0.00885 58  PHE A CA  
435  C C   . PHE A 58  ? 0.08641 0.09488 0.08818 -0.01604 0.00157  -0.00803 58  PHE A C   
436  O O   . PHE A 58  ? 0.08015 0.08524 0.07785 -0.01528 0.00167  -0.00703 58  PHE A O   
437  C CB  . PHE A 58  ? 0.08922 0.09831 0.09429 -0.01896 0.00165  -0.00980 58  PHE A CB  
438  C CG  . PHE A 58  ? 0.08692 0.09192 0.08762 -0.01885 0.00138  -0.00905 58  PHE A CG  
439  C CD1 . PHE A 58  ? 0.08012 0.08421 0.07785 -0.01743 -0.00026 -0.00840 58  PHE A CD1 
440  C CD2 . PHE A 58  ? 0.12240 0.12441 0.12235 -0.02016 0.00287  -0.00907 58  PHE A CD2 
441  C CE1 . PHE A 58  ? 0.08085 0.08163 0.07549 -0.01727 -0.00052 -0.00794 58  PHE A CE1 
442  C CE2 . PHE A 58  ? 0.09361 0.09197 0.08993 -0.01980 0.00246  -0.00845 58  PHE A CE2 
443  C CZ  . PHE A 58  ? 0.08307 0.08109 0.07703 -0.01833 0.00069  -0.00797 58  PHE A CZ  
444  N N   . LEU A 59  ? 0.12417 0.13617 0.12833 -0.01514 -0.00001 -0.00851 59  LEU A N   
445  C CA  . LEU A 59  ? 0.11073 0.12232 0.11267 -0.01334 -0.00114 -0.00769 59  LEU A CA  
446  C C   . LEU A 59  ? 0.07786 0.08791 0.07863 -0.01257 0.00057  -0.00697 59  LEU A C   
447  O O   . LEU A 59  ? 0.08537 0.09294 0.08281 -0.01157 0.00026  -0.00618 59  LEU A O   
448  C CB  . LEU A 59  ? 0.09748 0.11273 0.10193 -0.01237 -0.00307 -0.00824 59  LEU A CB  
449  C CG  . LEU A 59  ? 0.08260 0.09747 0.08537 -0.01044 -0.00388 -0.00737 59  LEU A CG  
450  C CD1 . LEU A 59  ? 0.07549 0.08724 0.07410 -0.01006 -0.00456 -0.00656 59  LEU A CD1 
451  C CD2 . LEU A 59  ? 0.11844 0.13677 0.12374 -0.00931 -0.00572 -0.00788 59  LEU A CD2 
452  N N   . LEU A 60  ? 0.09321 0.10463 0.09680 -0.01308 0.00249  -0.00738 60  LEU A N   
453  C CA  . LEU A 60  ? 0.10590 0.11569 0.10806 -0.01227 0.00437  -0.00683 60  LEU A CA  
454  C C   . LEU A 60  ? 0.09082 0.09567 0.08787 -0.01250 0.00561  -0.00599 60  LEU A C   
455  O O   . LEU A 60  ? 0.08400 0.08638 0.07764 -0.01133 0.00574  -0.00542 60  LEU A O   
456  C CB  . LEU A 60  ? 0.08200 0.09450 0.08877 -0.01283 0.00654  -0.00759 60  LEU A CB  
457  C CG  . LEU A 60  ? 0.10157 0.11903 0.11351 -0.01192 0.00514  -0.00845 60  LEU A CG  
458  C CD1 . LEU A 60  ? 0.08162 0.10222 0.09932 -0.01274 0.00739  -0.00953 60  LEU A CD1 
459  C CD2 . LEU A 60  ? 0.08326 0.10014 0.09326 -0.00981 0.00426  -0.00779 60  LEU A CD2 
460  N N   . GLU A 61  ? 0.10402 0.10717 0.10036 -0.01390 0.00639  -0.00599 61  GLU A N   
461  C CA  . GLU A 61  ? 0.11852 0.11667 0.10960 -0.01381 0.00709  -0.00512 61  GLU A CA  
462  C C   . GLU A 61  ? 0.08813 0.08474 0.07624 -0.01276 0.00458  -0.00477 61  GLU A C   
463  O O   . GLU A 61  ? 0.10205 0.09505 0.08589 -0.01191 0.00447  -0.00420 61  GLU A O   
464  C CB  . GLU A 61  ? 0.11882 0.11529 0.10999 -0.01543 0.00840  -0.00515 61  GLU A CB  
465  C CG  . GLU A 61  ? 0.16292 0.16017 0.15699 -0.01671 0.01151  -0.00550 61  GLU A CG  
466  C CD  . GLU A 61  ? 0.15512 0.15028 0.14941 -0.01847 0.01301  -0.00555 61  GLU A CD  
467  O OE1 . GLU A 61  ? 0.13138 0.12542 0.12444 -0.01869 0.01124  -0.00555 61  GLU A OE1 
468  O OE2 . GLU A 61  ? 0.11973 0.11420 0.11556 -0.01967 0.01619  -0.00564 61  GLU A OE2 
469  N N   . SER A 62  ? 0.10041 0.09963 0.09072 -0.01276 0.00258  -0.00520 62  SER A N   
470  C CA  . SER A 62  ? 0.09372 0.09178 0.08200 -0.01188 0.00063  -0.00497 62  SER A CA  
471  C C   . SER A 62  ? 0.10986 0.10766 0.09710 -0.01049 0.00024  -0.00475 62  SER A C   
472  O O   . SER A 62  ? 0.09206 0.08760 0.07686 -0.00976 -0.00068 -0.00458 62  SER A O   
473  C CB  . SER A 62  ? 0.07911 0.07963 0.06955 -0.01223 -0.00090 -0.00544 62  SER A CB  
474  O OG  . SER A 62  ? 0.07949 0.08010 0.07090 -0.01354 -0.00063 -0.00590 62  SER A OG  
475  N N   . LEU A 63  ? 0.11041 0.11056 0.09985 -0.01008 0.00088  -0.00490 63  LEU A N   
476  C CA  . LEU A 63  ? 0.11628 0.11587 0.10477 -0.00875 0.00076  -0.00476 63  LEU A CA  
477  C C   . LEU A 63  ? 0.12928 0.12559 0.11437 -0.00835 0.00210  -0.00460 63  LEU A C   
478  O O   . LEU A 63  ? 0.14239 0.13667 0.12511 -0.00737 0.00143  -0.00463 63  LEU A O   
479  C CB  . LEU A 63  ? 0.11613 0.11906 0.10806 -0.00821 0.00104  -0.00499 63  LEU A CB  
480  C CG  . LEU A 63  ? 0.09937 0.10530 0.09393 -0.00819 -0.00058 -0.00515 63  LEU A CG  
481  C CD1 . LEU A 63  ? 0.11106 0.11996 0.10873 -0.00716 -0.00061 -0.00536 63  LEU A CD1 
482  C CD2 . LEU A 63  ? 0.10350 0.10793 0.09607 -0.00775 -0.00211 -0.00477 63  LEU A CD2 
483  N N   . GLU A 64  ? 0.14528 0.14076 0.12987 -0.00909 0.00407  -0.00451 64  GLU A N   
484  C CA  . GLU A 64  ? 0.13902 0.13058 0.11917 -0.00860 0.00551  -0.00423 64  GLU A CA  
485  C C   . GLU A 64  ? 0.14578 0.13371 0.12167 -0.00816 0.00386  -0.00399 64  GLU A C   
486  O O   . GLU A 64  ? 0.13745 0.12235 0.10941 -0.00708 0.00354  -0.00405 64  GLU A O   
487  C CB  . GLU A 64  ? 0.16427 0.15516 0.14456 -0.00965 0.00835  -0.00402 64  GLU A CB  
488  C CG  . GLU A 64  ? 0.20825 0.20249 0.19289 -0.00988 0.01037  -0.00450 64  GLU A CG  
489  C CD  . GLU A 64  ? 0.28224 0.27572 0.26759 -0.01117 0.01364  -0.00442 64  GLU A CD  
490  O OE1 . GLU A 64  ? 0.43194 0.42075 0.41224 -0.01132 0.01497  -0.00373 64  GLU A OE1 
491  O OE2 . GLU A 64  ? 0.40219 0.39962 0.39321 -0.01201 0.01487  -0.00509 64  GLU A OE2 
492  N N   . ASP A 65  ? 0.15804 0.14625 0.13478 -0.00889 0.00267  -0.00390 65  ASP A N   
493  C CA  . ASP A 65  ? 0.14737 0.13264 0.12102 -0.00832 0.00089  -0.00383 65  ASP A CA  
494  C C   . ASP A 65  ? 0.12341 0.10920 0.09748 -0.00737 -0.00117 -0.00437 65  ASP A C   
495  O O   . ASP A 65  ? 0.17223 0.15531 0.14330 -0.00642 -0.00246 -0.00464 65  ASP A O   
496  C CB  . ASP A 65  ? 0.13148 0.11723 0.10663 -0.00928 0.00027  -0.00374 65  ASP A CB  
497  C CG  . ASP A 65  ? 0.14642 0.12902 0.11865 -0.00856 -0.00137 -0.00368 65  ASP A CG  
498  O OD1 . ASP A 65  ? 0.19145 0.17021 0.15939 -0.00800 -0.00082 -0.00318 65  ASP A OD1 
499  O OD2 . ASP A 65  ? 0.13156 0.11538 0.10572 -0.00845 -0.00314 -0.00413 65  ASP A OD2 
500  N N   . LEU A 66  ? 0.12035 0.10940 0.09809 -0.00757 -0.00154 -0.00460 66  LEU A N   
501  C CA  . LEU A 66  ? 0.14749 0.13674 0.12587 -0.00682 -0.00295 -0.00506 66  LEU A CA  
502  C C   . LEU A 66  ? 0.13497 0.12249 0.11111 -0.00582 -0.00253 -0.00537 66  LEU A C   
503  O O   . LEU A 66  ? 0.13778 0.12365 0.11271 -0.00512 -0.00389 -0.00601 66  LEU A O   
504  C CB  . LEU A 66  ? 0.15300 0.14538 0.13495 -0.00710 -0.00307 -0.00499 66  LEU A CB  
505  C CG  . LEU A 66  ? 0.12354 0.11722 0.10725 -0.00786 -0.00383 -0.00495 66  LEU A CG  
506  C CD1 . LEU A 66  ? 0.16010 0.15638 0.14617 -0.00789 -0.00379 -0.00474 66  LEU A CD1 
507  C CD2 . LEU A 66  ? 0.15352 0.14572 0.13698 -0.00766 -0.00514 -0.00538 66  LEU A CD2 
508  N N   . GLN A 67  ? 0.13131 0.11923 0.10717 -0.00575 -0.00062 -0.00513 67  GLN A N   
509  C CA  . GLN A 67  ? 0.13245 0.11855 0.10596 -0.00474 0.00012  -0.00551 67  GLN A CA  
510  C C   . GLN A 67  ? 0.16035 0.14224 0.12860 -0.00407 -0.00045 -0.00578 67  GLN A C   
511  O O   . GLN A 67  ? 0.17476 0.15472 0.14092 -0.00313 -0.00150 -0.00657 67  GLN A O   
512  C CB  . GLN A 67  ? 0.13512 0.12261 0.10979 -0.00483 0.00264  -0.00526 67  GLN A CB  
513  C CG  . GLN A 67  ? 0.18399 0.16949 0.15616 -0.00373 0.00391  -0.00572 67  GLN A CG  
514  C CD  . GLN A 67  ? 0.19247 0.17879 0.16639 -0.00287 0.00289  -0.00627 67  GLN A CD  
515  O OE1 . GLN A 67  ? 0.24100 0.22600 0.21407 -0.00260 0.00093  -0.00674 67  GLN A OE1 
516  N NE2 . GLN A 67  ? 0.22777 0.21622 0.20449 -0.00242 0.00431  -0.00629 67  GLN A NE2 
517  N N   . ARG A 68  ? 0.15744 0.13757 0.12325 -0.00446 0.00015  -0.00519 68  ARG A N   
518  C CA  . ARG A 68  ? 0.17780 0.15341 0.13782 -0.00352 -0.00065 -0.00529 68  ARG A CA  
519  C C   . ARG A 68  ? 0.19702 0.17212 0.15720 -0.00297 -0.00391 -0.00607 68  ARG A C   
520  O O   . ARG A 68  ? 0.16152 0.13364 0.11787 -0.00178 -0.00548 -0.00681 68  ARG A O   
521  C CB  . ARG A 68  ? 0.21998 0.19342 0.17736 -0.00402 0.00083  -0.00429 68  ARG A CB  
522  C CG  . ARG A 68  ? 0.23158 0.20485 0.18851 -0.00461 0.00444  -0.00369 68  ARG A CG  
523  C CD  . ARG A 68  ? 0.31417 0.28409 0.26762 -0.00508 0.00611  -0.00268 68  ARG A CD  
524  N NE  . ARG A 68  ? 0.25857 0.22996 0.21495 -0.00604 0.00494  -0.00239 68  ARG A NE  
525  C CZ  . ARG A 68  ? 0.21483 0.18940 0.17603 -0.00763 0.00634  -0.00224 68  ARG A CZ  
526  N NH1 . ARG A 68  ? 0.28120 0.25823 0.24547 -0.00845 0.00885  -0.00236 68  ARG A NH1 
527  N NH2 . ARG A 68  ? 0.28698 0.26235 0.25018 -0.00836 0.00510  -0.00214 68  ARG A NH2 
528  N N   . SER A 69  ? 0.19325 0.17125 0.15797 -0.00379 -0.00494 -0.00606 69  SER A N   
529  C CA  . SER A 69  ? 0.19670 0.17473 0.16278 -0.00342 -0.00765 -0.00694 69  SER A CA  
530  C C   . SER A 69  ? 0.15805 0.13668 0.12568 -0.00299 -0.00864 -0.00808 69  SER A C   
531  O O   . SER A 69  ? 0.22835 0.20575 0.19559 -0.00231 -0.01090 -0.00923 69  SER A O   
532  C CB  . SER A 69  ? 0.15386 0.13464 0.12425 -0.00446 -0.00790 -0.00664 69  SER A CB  
533  O OG  . SER A 69  ? 0.16719 0.14685 0.13603 -0.00481 -0.00728 -0.00584 69  SER A OG  
534  N N   . PHE A 70  ? 0.18424 0.16466 0.15386 -0.00331 -0.00706 -0.00788 70  PHE A N   
535  C CA  . PHE A 70  ? 0.17308 0.15349 0.14395 -0.00289 -0.00766 -0.00889 70  PHE A CA  
536  C C   . PHE A 70  ? 0.19744 0.17464 0.16373 -0.00176 -0.00785 -0.00972 70  PHE A C   
537  O O   . PHE A 70  ? 0.21504 0.19113 0.18138 -0.00127 -0.00945 -0.01111 70  PHE A O   
538  C CB  . PHE A 70  ? 0.18471 0.16768 0.15888 -0.00331 -0.00600 -0.00829 70  PHE A CB  
539  C CG  . PHE A 70  ? 0.14054 0.12598 0.11885 -0.00415 -0.00632 -0.00792 70  PHE A CG  
540  C CD1 . PHE A 70  ? 0.17153 0.15679 0.15198 -0.00433 -0.00765 -0.00877 70  PHE A CD1 
541  C CD2 . PHE A 70  ? 0.14656 0.13437 0.12661 -0.00474 -0.00521 -0.00687 70  PHE A CD2 
542  C CE1 . PHE A 70  ? 0.15371 0.14075 0.13744 -0.00507 -0.00747 -0.00838 70  PHE A CE1 
543  C CE2 . PHE A 70  ? 0.18205 0.17159 0.16493 -0.00535 -0.00546 -0.00656 70  PHE A CE2 
544  C CZ  . PHE A 70  ? 0.14034 0.12930 0.12480 -0.00550 -0.00638 -0.00721 70  PHE A CZ  
545  N N   . GLN A 71  ? 0.20696 0.18248 0.16929 -0.00139 -0.00613 -0.00903 71  GLN A N   
546  C CA  . GLN A 71  ? 0.19184 0.16369 0.14877 -0.00020 -0.00607 -0.00980 71  GLN A CA  
547  C C   . GLN A 71  ? 0.21979 0.18861 0.17296 0.00073  -0.00898 -0.01078 71  GLN A C   
548  O O   . GLN A 71  ? 0.21820 0.18446 0.16817 0.00177  -0.01028 -0.01217 71  GLN A O   
549  C CB  . GLN A 71  ? 0.21514 0.18557 0.16855 -0.00009 -0.00310 -0.00874 71  GLN A CB  
550  C CG  . GLN A 71  ? 0.23539 0.20857 0.19231 -0.00055 -0.00040 -0.00829 71  GLN A CG  
551  C CD  . GLN A 71  ? 0.35549 0.32735 0.30960 -0.00054 0.00284  -0.00752 71  GLN A CD  
552  O OE1 . GLN A 71  ? 0.30742 0.27639 0.25715 -0.00048 0.00339  -0.00692 71  GLN A OE1 
553  N NE2 . GLN A 71  ? 0.35932 0.33316 0.31611 -0.00054 0.00516  -0.00752 71  GLN A NE2 
554  N N   . ALA A 72  ? 0.21325 0.18226 0.16677 0.00050  -0.01020 -0.01022 72  ALA A N   
555  C CA  . ALA A 72  ? 0.22459 0.19097 0.17501 0.00163  -0.01335 -0.01116 72  ALA A CA  
556  C C   . ALA A 72  ? 0.20357 0.17147 0.15813 0.00169  -0.01619 -0.01308 72  ALA A C   
557  O O   . ALA A 72  ? 0.19679 0.16249 0.14884 0.00289  -0.01914 -0.01453 72  ALA A O   
558  C CB  . ALA A 72  ? 0.16932 0.13569 0.11982 0.00144  -0.01381 -0.01006 72  ALA A CB  
559  N N   . ARG A 73  ? 0.20818 0.17964 0.16904 0.00044  -0.01538 -0.01318 73  ARG A N   
560  C CA  . ARG A 73  ? 0.20038 0.17323 0.16587 0.00016  -0.01734 -0.01496 73  ARG A CA  
561  C C   . ARG A 73  ? 0.18376 0.15633 0.14989 0.00008  -0.01635 -0.01580 73  ARG A C   
562  O O   . ARG A 73  ? 0.20272 0.17704 0.17394 -0.00073 -0.01649 -0.01661 73  ARG A O   
563  C CB  . ARG A 73  ? 0.20498 0.18134 0.17681 -0.00113 -0.01699 -0.01446 73  ARG A CB  
564  C CG  . ARG A 73  ? 0.18195 0.15855 0.15356 -0.00102 -0.01788 -0.01376 73  ARG A CG  
565  C CD  . ARG A 73  ? 0.24805 0.22783 0.22476 -0.00235 -0.01653 -0.01287 73  ARG A CD  
566  N NE  . ARG A 73  ? 0.26051 0.24015 0.23626 -0.00226 -0.01674 -0.01196 73  ARG A NE  
567  C CZ  . ARG A 73  ? 0.24995 0.23011 0.22811 -0.00201 -0.01861 -0.01270 73  ARG A CZ  
568  N NH1 . ARG A 73  ? 0.27806 0.25929 0.26032 -0.00195 -0.02044 -0.01448 73  ARG A NH1 
569  N NH2 . ARG A 73  ? 0.36581 0.34541 0.34269 -0.00184 -0.01854 -0.01175 73  ARG A NH2 
570  N N   . GLY A 74  ? 0.16158 0.13168 0.12258 0.00090  -0.01507 -0.01561 74  GLY A N   
571  C CA  . GLY A 74  ? 0.14937 0.11866 0.11044 0.00108  -0.01418 -0.01658 74  GLY A CA  
572  C C   . GLY A 74  ? 0.21177 0.18365 0.17723 0.00018  -0.01160 -0.01546 74  GLY A C   
573  O O   . GLY A 74  ? 0.23314 0.20455 0.20002 0.00024  -0.01112 -0.01635 74  GLY A O   
574  N N   . SER A 75  ? 0.14621 0.12057 0.11367 -0.00054 -0.01006 -0.01362 75  SER A N   
575  C CA  . SER A 75  ? 0.17832 0.15513 0.14969 -0.00114 -0.00808 -0.01256 75  SER A CA  
576  C C   . SER A 75  ? 0.21843 0.19619 0.18845 -0.00099 -0.00570 -0.01107 75  SER A C   
577  O O   . SER A 75  ? 0.24314 0.21901 0.20887 -0.00041 -0.00501 -0.01102 75  SER A O   
578  C CB  . SER A 75  ? 0.22384 0.20318 0.19988 -0.00221 -0.00859 -0.01203 75  SER A CB  
579  O OG  . SER A 75  ? 0.19955 0.18016 0.17885 -0.00251 -0.00727 -0.01146 75  SER A OG  
580  N N   . ARG A 76  ? 0.19476 0.17529 0.16837 -0.00147 -0.00442 -0.00993 76  ARG A N   
581  C CA  . ARG A 76  ? 0.19986 0.18193 0.17351 -0.00134 -0.00231 -0.00885 76  ARG A CA  
582  C C   . ARG A 76  ? 0.18971 0.17509 0.16748 -0.00194 -0.00201 -0.00776 76  ARG A C   
583  O O   . ARG A 76  ? 0.14717 0.13303 0.12730 -0.00203 -0.00263 -0.00775 76  ARG A O   
584  C CB  . ARG A 76  ? 0.19969 0.18063 0.17231 -0.00030 -0.00081 -0.00933 76  ARG A CB  
585  C CG  . ARG A 76  ? 0.21494 0.19757 0.18814 -0.00007 0.00156  -0.00855 76  ARG A CG  
586  C CD  . ARG A 76  ? 0.17570 0.15637 0.14679 0.00107  0.00320  -0.00932 76  ARG A CD  
587  N NE  . ARG A 76  ? 0.21025 0.19059 0.18327 0.00182  0.00288  -0.00987 76  ARG A NE  
588  C CZ  . ARG A 76  ? 0.23828 0.22057 0.21456 0.00252  0.00411  -0.00942 76  ARG A CZ  
589  N NH1 . ARG A 76  ? 0.20432 0.18958 0.18292 0.00253  0.00558  -0.00864 76  ARG A NH1 
590  N NH2 . ARG A 76  ? 0.26078 0.24197 0.23826 0.00327  0.00379  -0.00985 76  ARG A NH2 
591  N N   . LEU A 77  ? 0.21324 0.20064 0.19168 -0.00236 -0.00099 -0.00692 77  LEU A N   
592  C CA  . LEU A 77  ? 0.16436 0.15490 0.14625 -0.00278 -0.00093 -0.00607 77  LEU A CA  
593  C C   . LEU A 77  ? 0.17733 0.16957 0.16118 -0.00191 0.00033  -0.00583 77  LEU A C   
594  O O   . LEU A 77  ? 0.18393 0.17636 0.16732 -0.00161 0.00186  -0.00599 77  LEU A O   
595  C CB  . LEU A 77  ? 0.15930 0.15129 0.14146 -0.00379 -0.00080 -0.00559 77  LEU A CB  
596  C CG  . LEU A 77  ? 0.16316 0.15839 0.14852 -0.00423 -0.00097 -0.00499 77  LEU A CG  
597  C CD1 . LEU A 77  ? 0.13333 0.12854 0.11954 -0.00429 -0.00226 -0.00480 77  LEU A CD1 
598  C CD2 . LEU A 77  ? 0.15047 0.14682 0.13611 -0.00535 -0.00067 -0.00482 77  LEU A CD2 
599  N N   . LEU A 78  ? 0.11596 0.10923 0.10195 -0.00140 -0.00018 -0.00541 78  LEU A N   
600  C CA  . LEU A 78  ? 0.13548 0.13032 0.12357 -0.00021 0.00059  -0.00515 78  LEU A CA  
601  C C   . LEU A 78  ? 0.13812 0.13647 0.12890 -0.00036 0.00013  -0.00451 78  LEU A C   
602  O O   . LEU A 78  ? 0.13014 0.12885 0.12109 -0.00071 -0.00105 -0.00398 78  LEU A O   
603  C CB  . LEU A 78  ? 0.15482 0.14778 0.14297 0.00078  0.00027  -0.00507 78  LEU A CB  
604  C CG  . LEU A 78  ? 0.14893 0.13837 0.13484 0.00081  0.00033  -0.00604 78  LEU A CG  
605  C CD1 . LEU A 78  ? 0.20756 0.19514 0.19418 0.00156  0.00022  -0.00591 78  LEU A CD1 
606  C CD2 . LEU A 78  ? 0.14653 0.13497 0.13078 0.00139  0.00161  -0.00687 78  LEU A CD2 
607  N N   . VAL A 79  ? 0.11454 0.11540 0.10747 -0.00011 0.00110  -0.00471 79  VAL A N   
608  C CA  . VAL A 79  ? 0.14415 0.14876 0.14027 -0.00018 0.00043  -0.00450 79  VAL A CA  
609  C C   . VAL A 79  ? 0.12336 0.12949 0.12195 0.00170  0.00022  -0.00435 79  VAL A C   
610  O O   . VAL A 79  ? 0.15499 0.16291 0.15614 0.00241  0.00142  -0.00487 79  VAL A O   
611  C CB  . VAL A 79  ? 0.13654 0.14322 0.13434 -0.00132 0.00164  -0.00503 79  VAL A CB  
612  C CG1 . VAL A 79  ? 0.12299 0.13380 0.12468 -0.00149 0.00060  -0.00519 79  VAL A CG1 
613  C CG2 . VAL A 79  ? 0.12047 0.12484 0.11520 -0.00287 0.00186  -0.00502 79  VAL A CG2 
614  N N   . LEU A 80  ? 0.12336 0.12856 0.12114 0.00261  -0.00118 -0.00360 80  LEU A N   
615  C CA  . LEU A 80  ? 0.17186 0.17785 0.17135 0.00470  -0.00168 -0.00322 80  LEU A CA  
616  C C   . LEU A 80  ? 0.20691 0.21724 0.20984 0.00526  -0.00300 -0.00337 80  LEU A C   
617  O O   . LEU A 80  ? 0.17299 0.18449 0.17551 0.00438  -0.00434 -0.00324 80  LEU A O   
618  C CB  . LEU A 80  ? 0.14997 0.15269 0.14677 0.00547  -0.00249 -0.00221 80  LEU A CB  
619  C CG  . LEU A 80  ? 0.23499 0.23357 0.22932 0.00504  -0.00139 -0.00236 80  LEU A CG  
620  C CD1 . LEU A 80  ? 0.19391 0.18934 0.18612 0.00533  -0.00186 -0.00140 80  LEU A CD1 
621  C CD2 . LEU A 80  ? 0.21237 0.21017 0.20760 0.00628  -0.00010 -0.00295 80  LEU A CD2 
622  N N   . ARG A 81  ? 0.18180 0.19457 0.18832 0.00680  -0.00270 -0.00382 81  ARG A N   
623  C CA  . ARG A 81  ? 0.21562 0.23303 0.22640 0.00756  -0.00422 -0.00432 81  ARG A CA  
624  C C   . ARG A 81  ? 0.22170 0.23874 0.23161 0.00984  -0.00659 -0.00338 81  ARG A C   
625  O O   . ARG A 81  ? 0.25045 0.26434 0.25832 0.01144  -0.00631 -0.00251 81  ARG A O   
626  C CB  . ARG A 81  ? 0.17927 0.19992 0.19522 0.00819  -0.00270 -0.00545 81  ARG A CB  
627  C CG  . ARG A 81  ? 0.22029 0.24346 0.23893 0.00598  -0.00110 -0.00657 81  ARG A CG  
628  C CD  . ARG A 81  ? 0.19436 0.21367 0.20866 0.00413  0.00103  -0.00636 81  ARG A CD  
629  N NE  . ARG A 81  ? 0.14267 0.16358 0.15907 0.00229  0.00308  -0.00723 81  ARG A NE  
630  C CZ  . ARG A 81  ? 0.17989 0.19766 0.19285 0.00093  0.00522  -0.00717 81  ARG A CZ  
631  N NH1 . ARG A 81  ? 0.20218 0.21550 0.20990 0.00114  0.00528  -0.00654 81  ARG A NH1 
632  N NH2 . ARG A 81  ? 0.11537 0.13431 0.13020 -0.00062 0.00733  -0.00782 81  ARG A NH2 
633  N N   . GLY A 82  ? 0.17572 0.19567 0.18690 0.01005  -0.00892 -0.00360 82  GLY A N   
634  C CA  . GLY A 82  ? 0.20031 0.21975 0.20991 0.01243  -0.01146 -0.00269 82  GLY A CA  
635  C C   . GLY A 82  ? 0.29102 0.30830 0.29582 0.01171  -0.01289 -0.00188 82  GLY A C   
636  O O   . GLY A 82  ? 0.21855 0.23608 0.22258 0.00933  -0.01239 -0.00238 82  GLY A O   
637  N N   . LYS A 83  ? 0.27782 0.29266 0.27912 0.01386  -0.01453 -0.00060 83  LYS A N   
638  C CA  . LYS A 83  ? 0.26403 0.27614 0.26003 0.01353  -0.01557 0.00032  83  LYS A CA  
639  C C   . LYS A 83  ? 0.23831 0.24465 0.22958 0.01307  -0.01348 0.00180  83  LYS A C   
640  O O   . LYS A 83  ? 0.22467 0.22874 0.21615 0.01396  -0.01207 0.00236  83  LYS A O   
641  C CB  . LYS A 83  ? 0.30523 0.31777 0.29956 0.01633  -0.01869 0.00084  83  LYS A CB  
642  C CG  . LYS A 83  ? 0.39637 0.41503 0.39600 0.01683  -0.02126 -0.00097 83  LYS A CG  
643  C CD  . LYS A 83  ? 0.53618 0.55499 0.53280 0.01912  -0.02492 -0.00072 83  LYS A CD  
644  C CE  . LYS A 83  ? 0.46952 0.48586 0.46401 0.02286  -0.02624 0.00077  83  LYS A CE  
645  N NZ  . LYS A 83  ? 0.50351 0.51267 0.49066 0.02345  -0.02445 0.00317  83  LYS A NZ  
646  N N   . PRO A 84  ? 0.24702 0.25088 0.23433 0.01162  -0.01310 0.00229  84  PRO A N   
647  C CA  . PRO A 84  ? 0.22093 0.21962 0.20472 0.01095  -0.01090 0.00345  84  PRO A CA  
648  C C   . PRO A 84  ? 0.22632 0.22080 0.20679 0.01340  -0.01083 0.00516  84  PRO A C   
649  O O   . PRO A 84  ? 0.22383 0.21479 0.20373 0.01325  -0.00882 0.00575  84  PRO A O   
650  C CB  . PRO A 84  ? 0.16525 0.16287 0.14605 0.00916  -0.01072 0.00345  84  PRO A CB  
651  C CG  . PRO A 84  ? 0.16987 0.17226 0.15352 0.00811  -0.01223 0.00193  84  PRO A CG  
652  C CD  . PRO A 84  ? 0.18937 0.19520 0.17598 0.01020  -0.01429 0.00150  84  PRO A CD  
653  N N   . GLU A 85  ? 0.23015 0.22466 0.20832 0.01574  -0.01307 0.00590  85  GLU A N   
654  C CA  . GLU A 85  ? 0.21368 0.20324 0.18755 0.01826  -0.01296 0.00784  85  GLU A CA  
655  C C   . GLU A 85  ? 0.23468 0.22391 0.21142 0.02003  -0.01250 0.00802  85  GLU A C   
656  O O   . GLU A 85  ? 0.19642 0.18057 0.17011 0.02149  -0.01134 0.00959  85  GLU A O   
657  C CB  . GLU A 85  ? 0.20749 0.19706 0.17762 0.02069  -0.01591 0.00853  85  GLU A CB  
658  C CG  . GLU A 85  ? 0.30993 0.29970 0.27672 0.01922  -0.01656 0.00817  85  GLU A CG  
659  C CD  . GLU A 85  ? 0.27890 0.27513 0.25036 0.01797  -0.01862 0.00597  85  GLU A CD  
660  O OE1 . GLU A 85  ? 0.31774 0.31842 0.29487 0.01859  -0.01977 0.00482  85  GLU A OE1 
661  O OE2 . GLU A 85  ? 0.34309 0.33983 0.31275 0.01632  -0.01887 0.00530  85  GLU A OE2 
662  N N   . GLU A 86  ? 0.24828 0.24253 0.23080 0.01993  -0.01312 0.00644  86  GLU A N   
663  C CA  . GLU A 86  ? 0.24697 0.24122 0.23261 0.02158  -0.01247 0.00634  86  GLU A CA  
664  C C   . GLU A 86  ? 0.23911 0.23259 0.22693 0.01941  -0.00966 0.00546  86  GLU A C   
665  O O   . GLU A 86  ? 0.28009 0.27104 0.26843 0.02052  -0.00836 0.00574  86  GLU A O   
666  C CB  . GLU A 86  ? 0.28714 0.28736 0.27814 0.02315  -0.01468 0.00502  86  GLU A CB  
667  C CG  . GLU A 86  ? 0.28772 0.28949 0.27723 0.02548  -0.01815 0.00542  86  GLU A CG  
668  C CD  . GLU A 86  ? 0.31934 0.32824 0.31540 0.02596  -0.02036 0.00345  86  GLU A CD  
669  O OE1 . GLU A 86  ? 0.29025 0.30243 0.29190 0.02479  -0.01877 0.00204  86  GLU A OE1 
670  O OE2 . GLU A 86  ? 0.34641 0.35751 0.34198 0.02746  -0.02362 0.00320  86  GLU A OE2 
671  N N   . VAL A 87  ? 0.20868 0.20399 0.19746 0.01649  -0.00883 0.00436  87  VAL A N   
672  C CA  . VAL A 87  ? 0.24415 0.23889 0.23463 0.01463  -0.00663 0.00335  87  VAL A CA  
673  C C   . VAL A 87  ? 0.20703 0.19641 0.19421 0.01355  -0.00486 0.00409  87  VAL A C   
674  O O   . VAL A 87  ? 0.19047 0.17746 0.17822 0.01348  -0.00332 0.00374  87  VAL A O   
675  C CB  . VAL A 87  ? 0.23696 0.23560 0.22969 0.01222  -0.00659 0.00192  87  VAL A CB  
676  C CG1 . VAL A 87  ? 0.19728 0.19422 0.19005 0.01028  -0.00458 0.00109  87  VAL A CG1 
677  C CG2 . VAL A 87  ? 0.25431 0.25812 0.25158 0.01303  -0.00755 0.00084  87  VAL A CG2 
678  N N   . PHE A 88  ? 0.17165 0.15906 0.15559 0.01268  -0.00495 0.00496  88  PHE A N   
679  C CA  . PHE A 88  ? 0.14881 0.13173 0.13069 0.01121  -0.00300 0.00534  88  PHE A CA  
680  C C   . PHE A 88  ? 0.16224 0.14017 0.14244 0.01281  -0.00179 0.00652  88  PHE A C   
681  O O   . PHE A 88  ? 0.16765 0.14294 0.14864 0.01171  -0.00007 0.00594  88  PHE A O   
682  C CB  . PHE A 88  ? 0.16779 0.14992 0.14692 0.00992  -0.00303 0.00591  88  PHE A CB  
683  C CG  . PHE A 88  ? 0.14705 0.13241 0.12796 0.00754  -0.00323 0.00452  88  PHE A CG  
684  C CD1 . PHE A 88  ? 0.17974 0.16459 0.16240 0.00566  -0.00200 0.00339  88  PHE A CD1 
685  C CD2 . PHE A 88  ? 0.16505 0.15371 0.14579 0.00731  -0.00480 0.00425  88  PHE A CD2 
686  C CE1 . PHE A 88  ? 0.22810 0.21548 0.21204 0.00376  -0.00230 0.00225  88  PHE A CE1 
687  C CE2 . PHE A 88  ? 0.15344 0.14456 0.13570 0.00520  -0.00484 0.00306  88  PHE A CE2 
688  C CZ  . PHE A 88  ? 0.15697 0.14734 0.14070 0.00352  -0.00357 0.00217  88  PHE A CZ  
689  N N   . PRO A 89  ? 0.17532 0.15146 0.15310 0.01541  -0.00264 0.00811  89  PRO A N   
690  C CA  . PRO A 89  ? 0.22177 0.19256 0.19790 0.01700  -0.00124 0.00930  89  PRO A CA  
691  C C   . PRO A 89  ? 0.18719 0.15816 0.16669 0.01739  -0.00047 0.00813  89  PRO A C   
692  O O   . PRO A 89  ? 0.27373 0.23998 0.25255 0.01750  0.00134  0.00847  89  PRO A O   
693  C CB  . PRO A 89  ? 0.22000 0.18996 0.19317 0.02023  -0.00306 0.01103  89  PRO A CB  
694  C CG  . PRO A 89  ? 0.18925 0.16216 0.16084 0.01961  -0.00475 0.01102  89  PRO A CG  
695  C CD  . PRO A 89  ? 0.16819 0.14631 0.14399 0.01703  -0.00493 0.00893  89  PRO A CD  
696  N N   . ARG A 90  ? 0.15697 0.13300 0.14005 0.01754  -0.00156 0.00669  90  ARG A N   
697  C CA  . ARG A 90  ? 0.17984 0.15598 0.16575 0.01779  -0.00054 0.00538  90  ARG A CA  
698  C C   . ARG A 90  ? 0.19992 0.17490 0.18632 0.01497  0.00099  0.00393  90  ARG A C   
699  O O   . ARG A 90  ? 0.15029 0.12149 0.13661 0.01481  0.00247  0.00348  90  ARG A O   
700  C CB  . ARG A 90  ? 0.25495 0.23672 0.24451 0.01873  -0.00175 0.00428  90  ARG A CB  
701  C CG  . ARG A 90  ? 0.26730 0.24894 0.25941 0.01944  -0.00045 0.00300  90  ARG A CG  
702  C CD  . ARG A 90  ? 0.32863 0.31449 0.32343 0.01784  -0.00004 0.00116  90  ARG A CD  
703  N NE  . ARG A 90  ? 0.31436 0.30572 0.31227 0.01867  -0.00138 0.00088  90  ARG A NE  
704  C CZ  . ARG A 90  ? 0.33981 0.33461 0.33815 0.01712  -0.00244 0.00068  90  ARG A CZ  
705  N NH1 . ARG A 90  ? 0.35651 0.34989 0.35221 0.01484  -0.00235 0.00085  90  ARG A NH1 
706  N NH2 . ARG A 90  ? 0.37468 0.37451 0.37660 0.01787  -0.00358 0.00015  90  ARG A NH2 
707  N N   . VAL A 91  ? 0.20289 0.18098 0.18983 0.01280  0.00050  0.00307  91  VAL A N   
708  C CA  . VAL A 91  ? 0.20005 0.17765 0.18762 0.01045  0.00140  0.00150  91  VAL A CA  
709  C C   . VAL A 91  ? 0.18473 0.15810 0.17092 0.00902  0.00252  0.00175  91  VAL A C   
710  O O   . VAL A 91  ? 0.18958 0.16168 0.17659 0.00746  0.00318  0.00029  91  VAL A O   
711  C CB  . VAL A 91  ? 0.17755 0.15944 0.16599 0.00881  0.00050  0.00063  91  VAL A CB  
712  C CG1 . VAL A 91  ? 0.14816 0.13413 0.13868 0.00994  -0.00011 0.00016  91  VAL A CG1 
713  C CG2 . VAL A 91  ? 0.17788 0.16048 0.16492 0.00800  -0.00027 0.00163  91  VAL A CG2 
714  N N   . PHE A 92  ? 0.24787 0.21896 0.23198 0.00951  0.00277  0.00347  92  PHE A N   
715  C CA  . PHE A 92  ? 0.19807 0.16472 0.18128 0.00819  0.00446  0.00378  92  PHE A CA  
716  C C   . PHE A 92  ? 0.19756 0.16010 0.18152 0.00863  0.00587  0.00325  92  PHE A C   
717  O O   . PHE A 92  ? 0.16592 0.12658 0.15134 0.00677  0.00688  0.00187  92  PHE A O   
718  C CB  . PHE A 92  ? 0.22055 0.18478 0.20054 0.00903  0.00487  0.00598  92  PHE A CB  
719  C CG  . PHE A 92  ? 0.18101 0.14814 0.16004 0.00795  0.00399  0.00618  92  PHE A CG  
720  C CD1 . PHE A 92  ? 0.21165 0.18239 0.19295 0.00592  0.00334  0.00452  92  PHE A CD1 
721  C CD2 . PHE A 92  ? 0.17929 0.14511 0.15470 0.00912  0.00377  0.00802  92  PHE A CD2 
722  C CE1 . PHE A 92  ? 0.19579 0.16893 0.17628 0.00498  0.00263  0.00465  92  PHE A CE1 
723  C CE2 . PHE A 92  ? 0.18587 0.15411 0.16020 0.00814  0.00300  0.00801  92  PHE A CE2 
724  C CZ  . PHE A 92  ? 0.16529 0.13724 0.14241 0.00602  0.00250  0.00630  92  PHE A CZ  
725  N N   . ARG A 93  ? 0.17286 0.13405 0.15612 0.01115  0.00582  0.00416  93  ARG A N   
726  C CA  . ARG A 93  ? 0.24276 0.19970 0.22661 0.01177  0.00724  0.00366  93  ARG A CA  
727  C C   . ARG A 93  ? 0.18016 0.13901 0.16632 0.01123  0.00694  0.00126  93  ARG A C   
728  O O   . ARG A 93  ? 0.18300 0.13855 0.16997 0.01052  0.00806  -0.00006 93  ARG A O   
729  C CB  . ARG A 93  ? 0.21556 0.17010 0.19778 0.01496  0.00726  0.00550  93  ARG A CB  
730  C CG  . ARG A 93  ? 0.24301 0.19304 0.22174 0.01580  0.00818  0.00799  93  ARG A CG  
731  C CD  . ARG A 93  ? 0.28153 0.23462 0.25812 0.01608  0.00663  0.00927  93  ARG A CD  
732  N NE  . ARG A 93  ? 0.31913 0.26757 0.29127 0.01762  0.00730  0.01184  93  ARG A NE  
733  C CZ  . ARG A 93  ? 0.24401 0.19343 0.21306 0.01791  0.00633  0.01312  93  ARG A CZ  
734  N NH1 . ARG A 93  ? 0.26901 0.22404 0.23943 0.01665  0.00467  0.01205  93  ARG A NH1 
735  N NH2 . ARG A 93  ? 0.29243 0.23667 0.25651 0.01956  0.00715  0.01554  93  ARG A NH2 
736  N N   . GLU A 94  ? 0.19605 0.15987 0.18307 0.01153  0.00557  0.00059  94  GLU A N   
737  C CA  . GLU A 94  ? 0.21618 0.18134 0.20448 0.01126  0.00557  -0.00151 94  GLU A CA  
738  C C   . GLU A 94  ? 0.18329 0.14832 0.17187 0.00864  0.00547  -0.00335 94  GLU A C   
739  O O   . GLU A 94  ? 0.23602 0.19918 0.22484 0.00821  0.00588  -0.00520 94  GLU A O   
740  C CB  . GLU A 94  ? 0.18775 0.15797 0.17697 0.01226  0.00458  -0.00157 94  GLU A CB  
741  C CG  . GLU A 94  ? 0.21682 0.18843 0.20662 0.01182  0.00491  -0.00361 94  GLU A CG  
742  C CD  . GLU A 94  ? 0.14728 0.12387 0.13833 0.01237  0.00440  -0.00362 94  GLU A CD  
743  O OE1 . GLU A 94  ? 0.19939 0.17806 0.19182 0.01413  0.00391  -0.00245 94  GLU A OE1 
744  O OE2 . GLU A 94  ? 0.15931 0.13761 0.15002 0.01107  0.00445  -0.00485 94  GLU A OE2 
745  N N   . TRP A 95  ? 0.17830 0.14521 0.16680 0.00700  0.00478  -0.00299 95  TRP A N   
746  C CA  . TRP A 95  ? 0.17550 0.14288 0.16458 0.00477  0.00427  -0.00472 95  TRP A CA  
747  C C   . TRP A 95  ? 0.17086 0.13488 0.16096 0.00323  0.00511  -0.00508 95  TRP A C   
748  O O   . TRP A 95  ? 0.17845 0.14297 0.16974 0.00143  0.00449  -0.00667 95  TRP A O   
749  C CB  . TRP A 95  ? 0.15414 0.12564 0.14304 0.00389  0.00309  -0.00437 95  TRP A CB  
750  C CG  . TRP A 95  ? 0.17435 0.14930 0.16291 0.00497  0.00251  -0.00428 95  TRP A CG  
751  C CD1 . TRP A 95  ? 0.16277 0.13772 0.15130 0.00633  0.00298  -0.00495 95  TRP A CD1 
752  C CD2 . TRP A 95  ? 0.14882 0.12765 0.13738 0.00467  0.00164  -0.00361 95  TRP A CD2 
753  N NE1 . TRP A 95  ? 0.16407 0.14281 0.15293 0.00681  0.00262  -0.00471 95  TRP A NE1 
754  C CE2 . TRP A 95  ? 0.15073 0.13186 0.13967 0.00576  0.00172  -0.00392 95  TRP A CE2 
755  C CE3 . TRP A 95  ? 0.18871 0.16915 0.17715 0.00355  0.00097  -0.00289 95  TRP A CE3 
756  C CZ2 . TRP A 95  ? 0.17342 0.15845 0.16297 0.00559  0.00114  -0.00359 95  TRP A CZ2 
757  C CZ3 . TRP A 95  ? 0.14790 0.13205 0.13654 0.00349  0.00020  -0.00258 95  TRP A CZ3 
758  C CH2 . TRP A 95  ? 0.15474 0.14116 0.14408 0.00444  0.00029  -0.00294 95  TRP A CH2 
759  N N   . GLY A 96  ? 0.15151 0.11203 0.14133 0.00394  0.00655  -0.00369 96  GLY A N   
760  C CA  . GLY A 96  ? 0.15903 0.11614 0.15016 0.00230  0.00792  -0.00392 96  GLY A CA  
761  C C   . GLY A 96  ? 0.15431 0.11338 0.14613 0.00057  0.00775  -0.00361 96  GLY A C   
762  O O   . GLY A 96  ? 0.13556 0.09382 0.12990 -0.00142 0.00817  -0.00506 96  GLY A O   
763  N N   . VAL A 97  ? 0.15214 0.11388 0.14211 0.00132  0.00710  -0.00192 97  VAL A N   
764  C CA  . VAL A 97  ? 0.15291 0.11681 0.14329 -0.00018 0.00685  -0.00177 97  VAL A CA  
765  C C   . VAL A 97  ? 0.15972 0.12005 0.15037 -0.00117 0.00909  -0.00084 97  VAL A C   
766  O O   . VAL A 97  ? 0.21368 0.17036 0.20217 0.00003  0.01062  0.00097  97  VAL A O   
767  C CB  . VAL A 97  ? 0.14896 0.11628 0.13713 0.00096  0.00560  -0.00034 97  VAL A CB  
768  C CG1 . VAL A 97  ? 0.13561 0.10529 0.12423 -0.00060 0.00521  -0.00052 97  VAL A CG1 
769  C CG2 . VAL A 97  ? 0.17108 0.14141 0.15928 0.00200  0.00404  -0.00112 97  VAL A CG2 
770  N N   . THR A 98  ? 0.18245 0.14360 0.17575 -0.00328 0.00945  -0.00209 98  THR A N   
771  C CA  . THR A 98  ? 0.15699 0.11520 0.15109 -0.00454 0.01198  -0.00140 98  THR A CA  
772  C C   . THR A 98  ? 0.19409 0.15459 0.18758 -0.00528 0.01206  -0.00075 98  THR A C   
773  O O   . THR A 98  ? 0.21629 0.17410 0.20908 -0.00588 0.01452  0.00040  98  THR A O   
774  C CB  . THR A 98  ? 0.16243 0.11918 0.16144 -0.00662 0.01293  -0.00376 98  THR A CB  
775  O OG1 . THR A 98  ? 0.19693 0.15779 0.19894 -0.00777 0.01072  -0.00605 98  THR A OG1 
776  C CG2 . THR A 98  ? 0.18008 0.13389 0.17956 -0.00598 0.01309  -0.00456 98  THR A CG2 
777  N N   . GLN A 99  ? 0.16454 0.12951 0.15802 -0.00523 0.00972  -0.00144 99  GLN A N   
778  C CA  . GLN A 99  ? 0.16038 0.12755 0.15350 -0.00596 0.00969  -0.00111 99  GLN A CA  
779  C C   . GLN A 99  ? 0.14964 0.12051 0.14042 -0.00483 0.00730  -0.00068 99  GLN A C   
780  O O   . GLN A 99  ? 0.15583 0.12899 0.14749 -0.00456 0.00542  -0.00182 99  GLN A O   
781  C CB  . GLN A 99  ? 0.13942 0.10827 0.13728 -0.00800 0.00962  -0.00330 99  GLN A CB  
782  C CG  . GLN A 99  ? 0.18002 0.15027 0.17801 -0.00885 0.01038  -0.00299 99  GLN A CG  
783  C CD  . GLN A 99  ? 0.18326 0.15603 0.18628 -0.01045 0.00959  -0.00532 99  GLN A CD  
784  O OE1 . GLN A 99  ? 0.21278 0.18477 0.21904 -0.01184 0.01161  -0.00595 99  GLN A OE1 
785  N NE2 . GLN A 99  ? 0.16596 0.14166 0.16965 -0.01015 0.00671  -0.00663 99  GLN A NE2 
786  N N   . LEU A 100 ? 0.14887 0.12007 0.13657 -0.00422 0.00752  0.00086  100 LEU A N   
787  C CA  . LEU A 100 ? 0.12604 0.10078 0.11199 -0.00344 0.00544  0.00112  100 LEU A CA  
788  C C   . LEU A 100 ? 0.15566 0.13224 0.14218 -0.00472 0.00545  0.00060  100 LEU A C   
789  O O   . LEU A 100 ? 0.14701 0.12157 0.13294 -0.00537 0.00737  0.00112  100 LEU A O   
790  C CB  . LEU A 100 ? 0.12315 0.09698 0.10506 -0.00144 0.00515  0.00305  100 LEU A CB  
791  C CG  . LEU A 100 ? 0.13428 0.11183 0.11481 -0.00068 0.00302  0.00319  100 LEU A CG  
792  C CD1 . LEU A 100 ? 0.09504 0.07586 0.07804 -0.00071 0.00139  0.00191  100 LEU A CD1 
793  C CD2 . LEU A 100 ? 0.13229 0.10879 0.10909 0.00146  0.00244  0.00489  100 LEU A CD2 
794  N N   . CYS A 101 ? 0.14925 0.12933 0.13686 -0.00506 0.00357  -0.00043 101 CYS A N   
795  C CA  . CYS A 101 ? 0.12039 0.10222 0.10894 -0.00620 0.00340  -0.00114 101 CYS A CA  
796  C C   . CYS A 101 ? 0.14029 0.12501 0.12714 -0.00567 0.00163  -0.00096 101 CYS A C   
797  O O   . CYS A 101 ? 0.15854 0.14495 0.14565 -0.00513 0.00024  -0.00127 101 CYS A O   
798  C CB  . CYS A 101 ? 0.12905 0.11183 0.12157 -0.00743 0.00292  -0.00301 101 CYS A CB  
799  S SG  . CYS A 101 ? 0.17835 0.15834 0.17444 -0.00849 0.00488  -0.00389 101 CYS A SG  
800  N N   . PHE A 102 ? 0.11042 0.09552 0.09558 -0.00589 0.00190  -0.00055 102 PHE A N   
801  C CA  . PHE A 102 ? 0.12398 0.11180 0.10814 -0.00574 0.00030  -0.00073 102 PHE A CA  
802  C C   . PHE A 102 ? 0.14209 0.12986 0.12539 -0.00653 0.00096  -0.00093 102 PHE A C   
803  O O   . PHE A 102 ? 0.12114 0.10655 0.10347 -0.00676 0.00280  -0.00048 102 PHE A O   
804  C CB  . PHE A 102 ? 0.12800 0.11649 0.10973 -0.00424 -0.00076 0.00026  102 PHE A CB  
805  C CG  . PHE A 102 ? 0.11063 0.09641 0.08889 -0.00317 0.00015  0.00167  102 PHE A CG  
806  C CD1 . PHE A 102 ? 0.12498 0.10799 0.10261 -0.00228 0.00117  0.00260  102 PHE A CD1 
807  C CD2 . PHE A 102 ? 0.14534 0.13092 0.12048 -0.00293 -0.00003 0.00206  102 PHE A CD2 
808  C CE1 . PHE A 102 ? 0.11627 0.09607 0.08998 -0.00110 0.00211  0.00412  102 PHE A CE1 
809  C CE2 . PHE A 102 ? 0.11975 0.10223 0.09066 -0.00170 0.00076  0.00347  102 PHE A CE2 
810  C CZ  . PHE A 102 ? 0.16128 0.14073 0.13134 -0.00073 0.00187  0.00462  102 PHE A CZ  
811  N N   . GLU A 103 ? 0.11340 0.10351 0.09704 -0.00696 -0.00031 -0.00165 103 GLU A N   
812  C CA  . GLU A 103 ? 0.12326 0.11343 0.10627 -0.00769 0.00020  -0.00209 103 GLU A CA  
813  C C   . GLU A 103 ? 0.11383 0.10294 0.09271 -0.00693 0.00044  -0.00123 103 GLU A C   
814  O O   . GLU A 103 ? 0.14433 0.13408 0.12130 -0.00583 -0.00084 -0.00060 103 GLU A O   
815  C CB  . GLU A 103 ? 0.11490 0.10744 0.09932 -0.00830 -0.00122 -0.00309 103 GLU A CB  
816  C CG  . GLU A 103 ? 0.10817 0.10079 0.09221 -0.00903 -0.00082 -0.00375 103 GLU A CG  
817  C CD  . GLU A 103 ? 0.10835 0.10276 0.09371 -0.00959 -0.00210 -0.00461 103 GLU A CD  
818  O OE1 . GLU A 103 ? 0.10997 0.10583 0.09445 -0.00942 -0.00326 -0.00455 103 GLU A OE1 
819  O OE2 . GLU A 103 ? 0.10787 0.10214 0.09535 -0.01015 -0.00193 -0.00537 103 GLU A OE2 
820  N N   . HIS A 104 ? 0.12026 0.10767 0.09768 -0.00738 0.00204  -0.00128 104 HIS A N   
821  C CA  . HIS A 104 ? 0.12014 0.10588 0.09261 -0.00655 0.00232  -0.00052 104 HIS A CA  
822  C C   . HIS A 104 ? 0.16316 0.15133 0.13438 -0.00635 0.00003  -0.00120 104 HIS A C   
823  O O   . HIS A 104 ? 0.15013 0.14042 0.12397 -0.00734 -0.00071 -0.00237 104 HIS A O   
824  C CB  . HIS A 104 ? 0.12892 0.11208 0.10004 -0.00718 0.00496  -0.00060 104 HIS A CB  
825  C CG  . HIS A 104 ? 0.15020 0.13061 0.11506 -0.00614 0.00561  0.00033  104 HIS A CG  
826  N ND1 . HIS A 104 ? 0.19922 0.17650 0.16024 -0.00485 0.00643  0.00197  104 HIS A ND1 
827  C CD2 . HIS A 104 ? 0.15700 0.13693 0.11825 -0.00605 0.00547  -0.00017 104 HIS A CD2 
828  C CE1 . HIS A 104 ? 0.20333 0.17820 0.15825 -0.00389 0.00668  0.00253  104 HIS A CE1 
829  N NE2 . HIS A 104 ? 0.24385 0.22036 0.19880 -0.00464 0.00607  0.00115  104 HIS A NE2 
830  N N   . ASP A 105 ? 0.15759 0.14528 0.12483 -0.00501 -0.00117 -0.00053 105 ASP A N   
831  C CA  . ASP A 105 ? 0.21638 0.20640 0.18257 -0.00479 -0.00352 -0.00141 105 ASP A CA  
832  C C   . ASP A 105 ? 0.22239 0.20999 0.18251 -0.00360 -0.00373 -0.00095 105 ASP A C   
833  O O   . ASP A 105 ? 0.24780 0.23242 0.20431 -0.00227 -0.00292 0.00050  105 ASP A O   
834  C CB  . ASP A 105 ? 0.21886 0.21189 0.18743 -0.00409 -0.00577 -0.00145 105 ASP A CB  
835  C CG  . ASP A 105 ? 0.27429 0.27058 0.24430 -0.00462 -0.00788 -0.00289 105 ASP A CG  
836  O OD1 . ASP A 105 ? 0.33860 0.33457 0.30723 -0.00540 -0.00782 -0.00384 105 ASP A OD1 
837  O OD2 . ASP A 105 ? 0.28186 0.28097 0.25467 -0.00431 -0.00940 -0.00318 105 ASP A OD2 
838  N N   . THR A 106 ? 0.20434 0.19283 0.16297 -0.00401 -0.00480 -0.00222 106 THR A N   
839  C CA  . THR A 106 ? 0.25022 0.23613 0.20239 -0.00292 -0.00509 -0.00211 106 THR A CA  
840  C C   . THR A 106 ? 0.27696 0.26524 0.22770 -0.00188 -0.00871 -0.00301 106 THR A C   
841  O O   . THR A 106 ? 0.29219 0.27862 0.23734 -0.00093 -0.00962 -0.00334 106 THR A O   
842  C CB  . THR A 106 ? 0.26164 0.24591 0.21245 -0.00414 -0.00313 -0.00310 106 THR A CB  
843  O OG1 . THR A 106 ? 0.19617 0.18369 0.15156 -0.00566 -0.00414 -0.00481 106 THR A OG1 
844  C CG2 . THR A 106 ? 0.21918 0.20082 0.17107 -0.00486 0.00054  -0.00225 106 THR A CG2 
845  N N   . GLU A 107 ? 0.31709 0.30938 0.27279 -0.00202 -0.01075 -0.00356 107 GLU A N   
846  C CA  . GLU A 107 ? 0.31402 0.30914 0.26965 -0.00110 -0.01422 -0.00466 107 GLU A CA  
847  C C   . GLU A 107 ? 0.26392 0.25728 0.21490 0.00156  -0.01577 -0.00333 107 GLU A C   
848  O O   . GLU A 107 ? 0.29055 0.28149 0.24043 0.00250  -0.01420 -0.00147 107 GLU A O   
849  C CB  . GLU A 107 ? 0.32278 0.32257 0.28549 -0.00204 -0.01541 -0.00558 107 GLU A CB  
850  C CG  . GLU A 107 ? 0.31124 0.31242 0.27796 -0.00443 -0.01421 -0.00685 107 GLU A CG  
851  C CD  . GLU A 107 ? 0.33012 0.33540 0.30299 -0.00533 -0.01520 -0.00776 107 GLU A CD  
852  O OE1 . GLU A 107 ? 0.28604 0.29421 0.26043 -0.00470 -0.01766 -0.00874 107 GLU A OE1 
853  O OE2 . GLU A 107 ? 0.39703 0.40255 0.37322 -0.00660 -0.01348 -0.00756 107 GLU A OE2 
854  N N   . PRO A 108 ? 0.30815 0.30242 0.25621 0.00292  -0.01896 -0.00433 108 PRO A N   
855  C CA  . PRO A 108 ? 0.32445 0.31640 0.26703 0.00587  -0.02071 -0.00297 108 PRO A CA  
856  C C   . PRO A 108 ? 0.32058 0.31409 0.26681 0.00715  -0.02127 -0.00174 108 PRO A C   
857  O O   . PRO A 108 ? 0.31056 0.30020 0.25296 0.00879  -0.02001 0.00039  108 PRO A O   
858  C CB  . PRO A 108 ? 0.38204 0.37614 0.32276 0.00682  -0.02478 -0.00497 108 PRO A CB  
859  C CG  . PRO A 108 ? 0.35428 0.34919 0.29620 0.00436  -0.02392 -0.00692 108 PRO A CG  
860  C CD  . PRO A 108 ? 0.35323 0.34994 0.30200 0.00193  -0.02106 -0.00677 108 PRO A CD  
861  N N   . TYR A 109 ? 0.33630 0.33513 0.28988 0.00643  -0.02285 -0.00305 109 TYR A N   
862  C CA  . TYR A 109 ? 0.33920 0.33957 0.29663 0.00759  -0.02303 -0.00205 109 TYR A CA  
863  C C   . TYR A 109 ? 0.31035 0.30795 0.26853 0.00664  -0.01929 -0.00040 109 TYR A C   
864  O O   . TYR A 109 ? 0.31837 0.31443 0.27627 0.00818  -0.01880 0.00112  109 TYR A O   
865  C CB  . TYR A 109 ? 0.29246 0.29897 0.25789 0.00667  -0.02476 -0.00393 109 TYR A CB  
866  C CG  . TYR A 109 ? 0.42213 0.43031 0.39221 0.00744  -0.02421 -0.00312 109 TYR A CG  
867  C CD1 . TYR A 109 ? 0.43469 0.44254 0.40353 0.01038  -0.02607 -0.00214 109 TYR A CD1 
868  C CD2 . TYR A 109 ? 0.36781 0.37757 0.34314 0.00540  -0.02185 -0.00335 109 TYR A CD2 
869  C CE1 . TYR A 109 ? 0.44043 0.44964 0.41356 0.01116  -0.02539 -0.00151 109 TYR A CE1 
870  C CE2 . TYR A 109 ? 0.37073 0.38169 0.34982 0.00614  -0.02119 -0.00275 109 TYR A CE2 
871  C CZ  . TYR A 109 ? 0.44539 0.45616 0.42359 0.00896  -0.02286 -0.00189 109 TYR A CZ  
872  O OH  . TYR A 109 ? 0.51079 0.52262 0.49281 0.00976  -0.02205 -0.00141 109 TYR A OH  
873  N N   . ALA A 110 ? 0.31737 0.31422 0.27663 0.00422  -0.01676 -0.00080 110 ALA A N   
874  C CA  . ALA A 110 ? 0.26803 0.26246 0.22838 0.00330  -0.01354 0.00042  110 ALA A CA  
875  C C   . ALA A 110 ? 0.29314 0.28209 0.24751 0.00466  -0.01179 0.00237  110 ALA A C   
876  O O   . ALA A 110 ? 0.26620 0.25318 0.22120 0.00516  -0.01022 0.00370  110 ALA A O   
877  C CB  . ALA A 110 ? 0.22365 0.21853 0.18643 0.00070  -0.01162 -0.00059 110 ALA A CB  
878  N N   . LYS A 111 ? 0.28537 0.27145 0.23365 0.00526  -0.01185 0.00255  111 LYS A N   
879  C CA  . LYS A 111 ? 0.32104 0.30124 0.26296 0.00652  -0.00970 0.00454  111 LYS A CA  
880  C C   . LYS A 111 ? 0.31070 0.28931 0.25014 0.00932  -0.01121 0.00612  111 LYS A C   
881  O O   . LYS A 111 ? 0.28876 0.26327 0.22634 0.00998  -0.00887 0.00795  111 LYS A O   
882  C CB  . LYS A 111 ? 0.29769 0.27491 0.23283 0.00679  -0.00948 0.00432  111 LYS A CB  
883  C CG  . LYS A 111 ? 0.34443 0.32229 0.28147 0.00423  -0.00745 0.00292  111 LYS A CG  
884  C CD  . LYS A 111 ? 0.29975 0.27376 0.22926 0.00472  -0.00667 0.00285  111 LYS A CD  
885  C CE  . LYS A 111 ? 0.28437 0.25924 0.21614 0.00234  -0.00480 0.00126  111 LYS A CE  
886  N NZ  . LYS A 111 ? 0.23936 0.21034 0.16358 0.00286  -0.00387 0.00100  111 LYS A NZ  
887  N N   . VAL A 112 ? 0.23218 0.21396 0.17193 0.01103  -0.01512 0.00535  112 VAL A N   
888  C CA  . VAL A 112 ? 0.25248 0.23324 0.19060 0.01399  -0.01696 0.00670  112 VAL A CA  
889  C C   . VAL A 112 ? 0.23997 0.22237 0.18433 0.01357  -0.01576 0.00711  112 VAL A C   
890  O O   . VAL A 112 ? 0.28585 0.26486 0.22829 0.01531  -0.01491 0.00890  112 VAL A O   
891  C CB  . VAL A 112 ? 0.27150 0.25618 0.20980 0.01584  -0.02175 0.00531  112 VAL A CB  
892  C CG1 . VAL A 112 ? 0.31701 0.30101 0.25425 0.01920  -0.02398 0.00658  112 VAL A CG1 
893  C CG2 . VAL A 112 ? 0.37136 0.35388 0.30265 0.01636  -0.02308 0.00474  112 VAL A CG2 
894  N N   . ARG A 113 ? 0.27859 0.26571 0.23006 0.01130  -0.01552 0.00546  113 ARG A N   
895  C CA  . ARG A 113 ? 0.25123 0.23991 0.20827 0.01089  -0.01445 0.00558  113 ARG A CA  
896  C C   . ARG A 113 ? 0.24024 0.22463 0.19648 0.00974  -0.01073 0.00680  113 ARG A C   
897  O O   . ARG A 113 ? 0.27796 0.26006 0.23436 0.01085  -0.00975 0.00800  113 ARG A O   
898  C CB  . ARG A 113 ? 0.25864 0.25290 0.22249 0.00883  -0.01505 0.00355  113 ARG A CB  
899  C CG  . ARG A 113 ? 0.22899 0.22444 0.19794 0.00805  -0.01351 0.00348  113 ARG A CG  
900  C CD  . ARG A 113 ? 0.23424 0.23329 0.20798 0.00552  -0.01302 0.00180  113 ARG A CD  
901  N NE  . ARG A 113 ? 0.23614 0.23329 0.20810 0.00355  -0.01135 0.00161  113 ARG A NE  
902  C CZ  . ARG A 113 ? 0.17636 0.17575 0.15090 0.00151  -0.01114 0.00026  113 ARG A CZ  
903  N NH1 . ARG A 113 ? 0.22536 0.22876 0.20417 0.00093  -0.01222 -0.00097 113 ARG A NH1 
904  N NH2 . ARG A 113 ? 0.19020 0.18760 0.16310 0.00006  -0.00963 0.00015  113 ARG A NH2 
905  N N   . ASP A 114 ? 0.19643 0.17973 0.15223 0.00750  -0.00863 0.00634  114 ASP A N   
906  C CA  . ASP A 114 ? 0.23487 0.21488 0.19131 0.00613  -0.00522 0.00702  114 ASP A CA  
907  C C   . ASP A 114 ? 0.25262 0.22665 0.20362 0.00768  -0.00341 0.00912  114 ASP A C   
908  O O   . ASP A 114 ? 0.28136 0.25267 0.23368 0.00719  -0.00099 0.00984  114 ASP A O   
909  C CB  . ASP A 114 ? 0.23577 0.21603 0.19305 0.00370  -0.00356 0.00597  114 ASP A CB  
910  C CG  . ASP A 114 ? 0.17938 0.16471 0.14177 0.00210  -0.00495 0.00408  114 ASP A CG  
911  O OD1 . ASP A 114 ? 0.19487 0.18327 0.16095 0.00243  -0.00639 0.00359  114 ASP A OD1 
912  O OD2 . ASP A 114 ? 0.17764 0.16360 0.14027 0.00056  -0.00439 0.00311  114 ASP A OD2 
913  N N   . ALA A 115 ? 0.25389 0.22547 0.19853 0.00959  -0.00453 0.01009  115 ALA A N   
914  C CA  . ALA A 115 ? 0.26804 0.23313 0.20650 0.01130  -0.00264 0.01236  115 ALA A CA  
915  C C   . ALA A 115 ? 0.28195 0.24596 0.22168 0.01317  -0.00315 0.01349  115 ALA A C   
916  O O   . ALA A 115 ? 0.35517 0.31497 0.29467 0.01293  -0.00023 0.01469  115 ALA A O   
917  C CB  . ALA A 115 ? 0.26405 0.22662 0.19460 0.01336  -0.00426 0.01312  115 ALA A CB  
918  N N   . ALA A 116 ? 0.20673 0.17460 0.14832 0.01501  -0.00674 0.01295  116 ALA A N   
919  C CA  . ALA A 116 ? 0.27125 0.23829 0.21429 0.01704  -0.00732 0.01390  116 ALA A CA  
920  C C   . ALA A 116 ? 0.24353 0.21146 0.19270 0.01507  -0.00505 0.01324  116 ALA A C   
921  O O   . ALA A 116 ? 0.17539 0.13972 0.12433 0.01601  -0.00354 0.01442  116 ALA A O   
922  C CB  . ALA A 116 ? 0.31873 0.29075 0.26404 0.01917  -0.01157 0.01300  116 ALA A CB  
923  N N   . VAL A 117 ? 0.20667 0.17898 0.16100 0.01242  -0.00486 0.01131  117 VAL A N   
924  C CA  . VAL A 117 ? 0.22627 0.19932 0.18584 0.01059  -0.00302 0.01047  117 VAL A CA  
925  C C   . VAL A 117 ? 0.24269 0.21037 0.20068 0.00942  0.00053  0.01140  117 VAL A C   
926  O O   . VAL A 117 ? 0.23042 0.19622 0.19070 0.00920  0.00203  0.01151  117 VAL A O   
927  C CB  . VAL A 117 ? 0.24878 0.22698 0.21309 0.00821  -0.00364 0.00838  117 VAL A CB  
928  C CG1 . VAL A 117 ? 0.19178 0.16998 0.16036 0.00635  -0.00180 0.00748  117 VAL A CG1 
929  C CG2 . VAL A 117 ? 0.17561 0.15904 0.14263 0.00914  -0.00662 0.00734  117 VAL A CG2 
930  N N   . ARG A 118 ? 0.21630 0.18137 0.17055 0.00861  0.00208  0.01194  118 ARG A N   
931  C CA  . ARG A 118 ? 0.25378 0.21373 0.20693 0.00738  0.00585  0.01276  118 ARG A CA  
932  C C   . ARG A 118 ? 0.21074 0.16486 0.15982 0.00950  0.00714  0.01493  118 ARG A C   
933  O O   . ARG A 118 ? 0.18623 0.13697 0.13706 0.00863  0.00983  0.01524  118 ARG A O   
934  C CB  . ARG A 118 ? 0.26573 0.22408 0.21554 0.00624  0.00749  0.01287  118 ARG A CB  
935  C CG  . ARG A 118 ? 0.26776 0.23050 0.22228 0.00369  0.00742  0.01077  118 ARG A CG  
936  C CD  . ARG A 118 ? 0.26465 0.22478 0.21662 0.00241  0.01014  0.01090  118 ARG A CD  
937  N NE  . ARG A 118 ? 0.25049 0.21500 0.20550 0.00074  0.00917  0.00903  118 ARG A NE  
938  C CZ  . ARG A 118 ? 0.36912 0.33623 0.32192 0.00136  0.00673  0.00851  118 ARG A CZ  
939  N NH1 . ARG A 118 ? 0.37603 0.34231 0.32380 0.00364  0.00463  0.00953  118 ARG A NH1 
940  N NH2 . ARG A 118 ? 0.38866 0.35921 0.34449 -0.00028 0.00623  0.00681  118 ARG A NH2 
941  N N   . ARG A 119 ? 0.25075 0.20337 0.19431 0.01235  0.00518  0.01640  119 ARG A N   
942  C CA  . ARG A 119 ? 0.21757 0.16422 0.15661 0.01480  0.00613  0.01867  119 ARG A CA  
943  C C   . ARG A 119 ? 0.26134 0.20900 0.20510 0.01548  0.00556  0.01831  119 ARG A C   
944  O O   . ARG A 119 ? 0.28511 0.22751 0.22783 0.01601  0.00791  0.01959  119 ARG A O   
945  C CB  . ARG A 119 ? 0.25706 0.20241 0.18922 0.01807  0.00336  0.02009  119 ARG A CB  
946  C CG  . ARG A 119 ? 0.26824 0.21184 0.19452 0.01768  0.00393  0.02043  119 ARG A CG  
947  C CD  . ARG A 119 ? 0.29130 0.23178 0.20924 0.02131  0.00144  0.02214  119 ARG A CD  
948  N NE  . ARG A 119 ? 0.28761 0.23394 0.20806 0.02328  -0.00358 0.02100  119 ARG A NE  
949  C CZ  . ARG A 119 ? 0.29035 0.24181 0.21148 0.02302  -0.00665 0.01928  119 ARG A CZ  
950  N NH1 . ARG A 119 ? 0.29458 0.24599 0.21367 0.02102  -0.00539 0.01852  119 ARG A NH1 
951  N NH2 . ARG A 119 ? 0.29213 0.24888 0.21644 0.02477  -0.01096 0.01817  119 ARG A NH2 
952  N N   . LEU A 120 ? 0.19666 0.15076 0.14560 0.01541  0.00274  0.01653  120 LEU A N   
953  C CA  . LEU A 120 ? 0.24795 0.20323 0.20157 0.01584  0.00249  0.01587  120 LEU A CA  
954  C C   . LEU A 120 ? 0.22527 0.17940 0.18303 0.01302  0.00539  0.01477  120 LEU A C   
955  O O   . LEU A 120 ? 0.21419 0.16603 0.17380 0.01343  0.00645  0.01483  120 LEU A O   
956  C CB  . LEU A 120 ? 0.24320 0.20557 0.20129 0.01622  -0.00075 0.01414  120 LEU A CB  
957  C CG  . LEU A 120 ? 0.16754 0.13198 0.12349 0.01930  -0.00416 0.01473  120 LEU A CG  
958  C CD1 . LEU A 120 ? 0.21106 0.18296 0.17235 0.01880  -0.00675 0.01263  120 LEU A CD1 
959  C CD2 . LEU A 120 ? 0.18542 0.14630 0.13978 0.02244  -0.00444 0.01625  120 LEU A CD2 
960  N N   . ALA A 121 ? 0.18638 0.14208 0.14583 0.01026  0.00653  0.01361  121 ALA A N   
961  C CA  . ALA A 121 ? 0.23392 0.18891 0.19775 0.00767  0.00884  0.01228  121 ALA A CA  
962  C C   . ALA A 121 ? 0.23145 0.17966 0.19309 0.00727  0.01243  0.01365  121 ALA A C   
963  O O   . ALA A 121 ? 0.21806 0.16420 0.18290 0.00631  0.01408  0.01298  121 ALA A O   
964  C CB  . ALA A 121 ? 0.21756 0.17649 0.18425 0.00511  0.00870  0.01054  121 ALA A CB  
965  N N   . ALA A 122 ? 0.24087 0.18528 0.19696 0.00793  0.01383  0.01548  122 ALA A N   
966  C CA  . ALA A 122 ? 0.23325 0.17055 0.18678 0.00757  0.01777  0.01702  122 ALA A CA  
967  C C   . ALA A 122 ? 0.26983 0.20263 0.22166 0.00978  0.01813  0.01848  122 ALA A C   
968  O O   . ALA A 122 ? 0.24657 0.17414 0.19902 0.00889  0.02143  0.01897  122 ALA A O   
969  C CB  . ALA A 122 ? 0.26350 0.19718 0.21021 0.00820  0.01925  0.01886  122 ALA A CB  
970  N N   . GLU A 123 ? 0.28652 0.22123 0.23664 0.01267  0.01485  0.01907  123 GLU A N   
971  C CA  . GLU A 123 ? 0.26240 0.19330 0.21159 0.01499  0.01492  0.02024  123 GLU A CA  
972  C C   . GLU A 123 ? 0.26527 0.19766 0.22112 0.01339  0.01551  0.01819  123 GLU A C   
973  O O   . GLU A 123 ? 0.29365 0.22092 0.24958 0.01378  0.01759  0.01882  123 GLU A O   
974  C CB  . GLU A 123 ? 0.27527 0.20876 0.22206 0.01852  0.01100  0.02101  123 GLU A CB  
975  C CG  . GLU A 123 ? 0.29218 0.22322 0.23141 0.02079  0.00995  0.02312  123 GLU A CG  
976  C CD  . GLU A 123 ? 0.24314 0.17711 0.18094 0.02440  0.00568  0.02355  123 GLU A CD  
977  O OE1 . GLU A 123 ? 0.26137 0.19975 0.20460 0.02493  0.00382  0.02213  123 GLU A OE1 
978  O OE2 . GLU A 123 ? 0.27560 0.20746 0.20689 0.02676  0.00416  0.02518  123 GLU A OE2 
979  N N   . ALA A 124 ? 0.24237 0.18132 0.20343 0.01167  0.01370  0.01571  124 ALA A N   
980  C CA  . ALA A 124 ? 0.28777 0.22823 0.25444 0.01029  0.01390  0.01356  124 ALA A CA  
981  C C   . ALA A 124 ? 0.25354 0.19242 0.22367 0.00700  0.01660  0.01213  124 ALA A C   
982  O O   . ALA A 124 ? 0.28100 0.22114 0.25573 0.00565  0.01655  0.01001  124 ALA A O   
983  C CB  . ALA A 124 ? 0.23526 0.18296 0.20536 0.01017  0.01080  0.01162  124 ALA A CB  
984  N N   . GLY A 125 ? 0.22965 0.16576 0.19776 0.00574  0.01896  0.01310  125 GLY A N   
985  C CA  . GLY A 125 ? 0.26063 0.19593 0.23300 0.00255  0.02149  0.01150  125 GLY A CA  
986  C C   . GLY A 125 ? 0.25059 0.19227 0.22757 0.00047  0.01969  0.00899  125 GLY A C   
987  O O   . GLY A 125 ? 0.26010 0.20231 0.24213 -0.00191 0.02073  0.00692  125 GLY A O   
988  N N   . VAL A 126 ? 0.26537 0.21178 0.24081 0.00138  0.01694  0.00904  126 VAL A N   
989  C CA  . VAL A 126 ? 0.19719 0.14941 0.17632 -0.00024 0.01504  0.00690  126 VAL A CA  
990  C C   . VAL A 126 ? 0.19869 0.15134 0.17704 -0.00160 0.01629  0.00713  126 VAL A C   
991  O O   . VAL A 126 ? 0.19305 0.14445 0.16648 -0.00036 0.01649  0.00897  126 VAL A O   
992  C CB  . VAL A 126 ? 0.17736 0.13432 0.15570 0.00136  0.01163  0.00668  126 VAL A CB  
993  C CG1 . VAL A 126 ? 0.16083 0.12302 0.14236 -0.00027 0.00995  0.00470  126 VAL A CG1 
994  C CG2 . VAL A 126 ? 0.20124 0.15768 0.18047 0.00281  0.01077  0.00638  126 VAL A CG2 
995  N N   . GLU A 127 ? 0.21796 0.17239 0.20113 -0.00401 0.01699  0.00514  127 GLU A N   
996  C CA  . GLU A 127 ? 0.19464 0.15025 0.17808 -0.00537 0.01806  0.00493  127 GLU A CA  
997  C C   . GLU A 127 ? 0.17351 0.13419 0.15603 -0.00488 0.01506  0.00448  127 GLU A C   
998  O O   . GLU A 127 ? 0.19846 0.16277 0.18306 -0.00469 0.01243  0.00322  127 GLU A O   
999  C CB  . GLU A 127 ? 0.19687 0.15313 0.18672 -0.00793 0.01952  0.00269  127 GLU A CB  
1000 C CG  . GLU A 127 ? 0.21727 0.17552 0.20871 -0.00936 0.02045  0.00200  127 GLU A CG  
1001 C CD  . GLU A 127 ? 0.25979 0.22004 0.25871 -0.01161 0.02084  -0.00070 127 GLU A CD  
1002 O OE1 . GLU A 127 ? 0.26964 0.22913 0.27217 -0.01220 0.02066  -0.00201 127 GLU A OE1 
1003 O OE2 . GLU A 127 ? 0.28337 0.24598 0.28470 -0.01270 0.02117  -0.00167 127 GLU A OE2 
1004 N N   . VAL A 128 ? 0.19613 0.15669 0.17531 -0.00471 0.01567  0.00546  128 VAL A N   
1005 C CA  . VAL A 128 ? 0.17432 0.13913 0.15238 -0.00435 0.01314  0.00506  128 VAL A CA  
1006 C C   . VAL A 128 ? 0.14229 0.10877 0.12314 -0.00625 0.01416  0.00374  128 VAL A C   
1007 O O   . VAL A 128 ? 0.11256 0.07613 0.09246 -0.00698 0.01711  0.00429  128 VAL A O   
1008 C CB  . VAL A 128 ? 0.20410 0.16762 0.17573 -0.00233 0.01245  0.00702  128 VAL A CB  
1009 C CG1 . VAL A 128 ? 0.20818 0.17616 0.17930 -0.00225 0.00989  0.00626  128 VAL A CG1 
1010 C CG2 . VAL A 128 ? 0.17461 0.13668 0.14407 -0.00019 0.01128  0.00824  128 VAL A CG2 
1011 N N   . VAL A 129 ? 0.14515 0.11600 0.12935 -0.00695 0.01191  0.00204  129 VAL A N   
1012 C CA  . VAL A 129 ? 0.14129 0.11418 0.12855 -0.00847 0.01233  0.00064  129 VAL A CA  
1013 C C   . VAL A 129 ? 0.14928 0.12547 0.13464 -0.00794 0.00993  0.00048  129 VAL A C   
1014 O O   . VAL A 129 ? 0.12878 0.10756 0.11467 -0.00742 0.00740  0.00001  129 VAL A O   
1015 C CB  . VAL A 129 ? 0.11459 0.08922 0.10812 -0.00981 0.01180  -0.00149 129 VAL A CB  
1016 C CG1 . VAL A 129 ? 0.22476 0.20186 0.22160 -0.01099 0.01174  -0.00298 129 VAL A CG1 
1017 C CG2 . VAL A 129 ? 0.18164 0.15302 0.17772 -0.01059 0.01427  -0.00165 129 VAL A CG2 
1018 N N   . THR A 130 ? 0.14553 0.12136 0.12863 -0.00815 0.01096  0.00079  130 THR A N   
1019 C CA  . THR A 130 ? 0.14672 0.12511 0.12762 -0.00771 0.00894  0.00063  130 THR A CA  
1020 C C   . THR A 130 ? 0.11841 0.09782 0.10126 -0.00892 0.00989  -0.00054 130 THR A C   
1021 O O   . THR A 130 ? 0.10131 0.07884 0.08114 -0.00894 0.01171  -0.00004 130 THR A O   
1022 C CB  . THR A 130 ? 0.11038 0.08701 0.08510 -0.00619 0.00873  0.00224  130 THR A CB  
1023 O OG1 . THR A 130 ? 0.14861 0.12138 0.12027 -0.00630 0.01174  0.00314  130 THR A OG1 
1024 C CG2 . THR A 130 ? 0.18407 0.15984 0.15725 -0.00471 0.00764  0.00337  130 THR A CG2 
1025 N N   . PRO A 131 ? 0.12975 0.11185 0.11728 -0.00979 0.00869  -0.00213 131 PRO A N   
1026 C CA  . PRO A 131 ? 0.12542 0.10866 0.11516 -0.01070 0.00932  -0.00332 131 PRO A CA  
1027 C C   . PRO A 131 ? 0.09040 0.07509 0.07707 -0.01030 0.00781  -0.00331 131 PRO A C   
1028 O O   . PRO A 131 ? 0.09085 0.07663 0.07511 -0.00953 0.00575  -0.00279 131 PRO A O   
1029 C CB  . PRO A 131 ? 0.11583 0.10125 0.11116 -0.01133 0.00791  -0.00492 131 PRO A CB  
1030 C CG  . PRO A 131 ? 0.10068 0.08689 0.09504 -0.01059 0.00568  -0.00455 131 PRO A CG  
1031 C CD  . PRO A 131 ? 0.09534 0.07919 0.08606 -0.00980 0.00672  -0.00293 131 PRO A CD  
1032 N N   . ILE A 132 ? 0.12562 0.11033 0.11286 -0.01089 0.00901  -0.00407 132 ILE A N   
1033 C CA  . ILE A 132 ? 0.12224 0.10802 0.10702 -0.01074 0.00787  -0.00441 132 ILE A CA  
1034 C C   . ILE A 132 ? 0.12840 0.11671 0.11724 -0.01122 0.00616  -0.00577 132 ILE A C   
1035 O O   . ILE A 132 ? 0.10993 0.09861 0.10298 -0.01180 0.00701  -0.00683 132 ILE A O   
1036 C CB  . ILE A 132 ? 0.12357 0.10727 0.10576 -0.01093 0.01039  -0.00445 132 ILE A CB  
1037 C CG1 . ILE A 132 ? 0.10945 0.09002 0.08589 -0.01009 0.01173  -0.00285 132 ILE A CG1 
1038 C CG2 . ILE A 132 ? 0.12234 0.10722 0.10305 -0.01099 0.00922  -0.00532 132 ILE A CG2 
1039 C CD1 . ILE A 132 ? 0.12761 0.10507 0.10122 -0.01028 0.01511  -0.00269 132 ILE A CD1 
1040 N N   . SER A 133 ? 0.08468 0.07459 0.07235 -0.01092 0.00378  -0.00576 133 SER A N   
1041 C CA  . SER A 133 ? 0.09690 0.08851 0.08745 -0.01119 0.00215  -0.00673 133 SER A CA  
1042 C C   . SER A 133 ? 0.09783 0.09048 0.08622 -0.01115 0.00058  -0.00678 133 SER A C   
1043 O O   . SER A 133 ? 0.09286 0.08624 0.08281 -0.01138 -0.00043 -0.00746 133 SER A O   
1044 C CB  . SER A 133 ? 0.09514 0.08734 0.08807 -0.01099 0.00099  -0.00675 133 SER A CB  
1045 O OG  . SER A 133 ? 0.11629 0.10807 0.10714 -0.01048 0.00087  -0.00569 133 SER A OG  
1046 N N   . HIS A 134 ? 0.08492 0.07751 0.06981 -0.01082 0.00030  -0.00613 134 HIS A N   
1047 C CA  . HIS A 134 ? 0.08522 0.07905 0.06883 -0.01098 -0.00115 -0.00650 134 HIS A CA  
1048 C C   . HIS A 134 ? 0.08368 0.07693 0.06657 -0.01150 -0.00058 -0.00746 134 HIS A C   
1049 O O   . HIS A 134 ? 0.08281 0.07682 0.06626 -0.01197 -0.00152 -0.00816 134 HIS A O   
1050 C CB  . HIS A 134 ? 0.08397 0.07833 0.06473 -0.01033 -0.00205 -0.00581 134 HIS A CB  
1051 C CG  . HIS A 134 ? 0.13841 0.13443 0.11868 -0.01064 -0.00359 -0.00647 134 HIS A CG  
1052 N ND1 . HIS A 134 ? 0.11585 0.11337 0.09848 -0.01115 -0.00448 -0.00681 134 HIS A ND1 
1053 C CD2 . HIS A 134 ? 0.11872 0.11499 0.09647 -0.01057 -0.00432 -0.00698 134 HIS A CD2 
1054 C CE1 . HIS A 134 ? 0.10668 0.10547 0.08891 -0.01155 -0.00549 -0.00753 134 HIS A CE1 
1055 N NE2 . HIS A 134 ? 0.11605 0.11429 0.09547 -0.01120 -0.00565 -0.00777 134 HIS A NE2 
1056 N N   . THR A 135 ? 0.09050 0.08212 0.07211 -0.01145 0.00121  -0.00755 135 THR A N   
1057 C CA  . THR A 135 ? 0.11217 0.10289 0.09289 -0.01184 0.00214  -0.00857 135 THR A CA  
1058 C C   . THR A 135 ? 0.08813 0.07835 0.07256 -0.01211 0.00372  -0.00920 135 THR A C   
1059 O O   . THR A 135 ? 0.08528 0.07589 0.07284 -0.01204 0.00394  -0.00893 135 THR A O   
1060 C CB  . THR A 135 ? 0.09248 0.08142 0.06831 -0.01143 0.00318  -0.00834 135 THR A CB  
1061 O OG1 . THR A 135 ? 0.09427 0.08158 0.06936 -0.01101 0.00506  -0.00731 135 THR A OG1 
1062 C CG2 . THR A 135 ? 0.11100 0.10086 0.08365 -0.01100 0.00101  -0.00811 135 THR A CG2 
1063 N N   . LEU A 136 ? 0.10864 0.09807 0.09298 -0.01238 0.00475  -0.01026 136 LEU A N   
1064 C CA  . LEU A 136 ? 0.12239 0.11166 0.11091 -0.01249 0.00621  -0.01109 136 LEU A CA  
1065 C C   . LEU A 136 ? 0.12302 0.11107 0.11194 -0.01250 0.00896  -0.01083 136 LEU A C   
1066 O O   . LEU A 136 ? 0.13376 0.12245 0.12735 -0.01260 0.00969  -0.01111 136 LEU A O   
1067 C CB  . LEU A 136 ? 0.09742 0.08607 0.08591 -0.01266 0.00664  -0.01237 136 LEU A CB  
1068 C CG  . LEU A 136 ? 0.11006 0.09946 0.09960 -0.01276 0.00443  -0.01280 136 LEU A CG  
1069 C CD1 . LEU A 136 ? 0.08916 0.07739 0.07828 -0.01292 0.00521  -0.01409 136 LEU A CD1 
1070 C CD2 . LEU A 136 ? 0.09952 0.08993 0.09345 -0.01240 0.00327  -0.01270 136 LEU A CD2 
1071 N N   . TYR A 137 ? 0.10193 0.08804 0.08594 -0.01238 0.01053  -0.01034 137 TYR A N   
1072 C CA  . TYR A 137 ? 0.11963 0.10373 0.10304 -0.01243 0.01376  -0.00992 137 TYR A CA  
1073 C C   . TYR A 137 ? 0.13445 0.11693 0.11287 -0.01192 0.01379  -0.00830 137 TYR A C   
1074 O O   . TYR A 137 ? 0.11736 0.10046 0.09255 -0.01144 0.01129  -0.00772 137 TYR A O   
1075 C CB  . TYR A 137 ? 0.11456 0.09663 0.09568 -0.01252 0.01644  -0.01081 137 TYR A CB  
1076 C CG  . TYR A 137 ? 0.16205 0.14534 0.14781 -0.01279 0.01666  -0.01248 137 TYR A CG  
1077 C CD1 . TYR A 137 ? 0.16226 0.14619 0.14694 -0.01272 0.01456  -0.01330 137 TYR A CD1 
1078 C CD2 . TYR A 137 ? 0.16174 0.14543 0.15325 -0.01307 0.01906  -0.01334 137 TYR A CD2 
1079 C CE1 . TYR A 137 ? 0.13914 0.12369 0.12781 -0.01276 0.01481  -0.01473 137 TYR A CE1 
1080 C CE2 . TYR A 137 ? 0.15839 0.14319 0.15434 -0.01303 0.01911  -0.01490 137 TYR A CE2 
1081 C CZ  . TYR A 137 ? 0.13490 0.11993 0.12913 -0.01279 0.01697  -0.01549 137 TYR A CZ  
1082 O OH  . TYR A 137 ? 0.12771 0.11342 0.12618 -0.01255 0.01704  -0.01695 137 TYR A OH  
1083 N N   . ASP A 138 ? 0.11801 0.09834 0.09620 -0.01200 0.01678  -0.00760 138 ASP A N   
1084 C CA  . ASP A 138 ? 0.17196 0.14944 0.14405 -0.01129 0.01762  -0.00596 138 ASP A CA  
1085 C C   . ASP A 138 ? 0.14324 0.11855 0.10834 -0.01069 0.01791  -0.00608 138 ASP A C   
1086 O O   . ASP A 138 ? 0.15892 0.13197 0.12243 -0.01091 0.02099  -0.00660 138 ASP A O   
1087 C CB  . ASP A 138 ? 0.14036 0.11537 0.11388 -0.01168 0.02138  -0.00525 138 ASP A CB  
1088 C CG  . ASP A 138 ? 0.16611 0.13738 0.13288 -0.01076 0.02246  -0.00329 138 ASP A CG  
1089 O OD1 . ASP A 138 ? 0.17392 0.14470 0.13486 -0.00963 0.02006  -0.00256 138 ASP A OD1 
1090 O OD2 . ASP A 138 ? 0.14136 0.11004 0.10887 -0.01112 0.02575  -0.00252 138 ASP A OD2 
1091 N N   . THR A 139 ? 0.14044 0.11655 0.10161 -0.00994 0.01469  -0.00581 139 THR A N   
1092 C CA  . THR A 139 ? 0.18038 0.15489 0.13535 -0.00940 0.01423  -0.00641 139 THR A CA  
1093 C C   . THR A 139 ? 0.15582 0.12566 0.10334 -0.00844 0.01674  -0.00521 139 THR A C   
1094 O O   . THR A 139 ? 0.18816 0.15558 0.13040 -0.00812 0.01780  -0.00589 139 THR A O   
1095 C CB  . THR A 139 ? 0.17071 0.14759 0.12419 -0.00890 0.01000  -0.00667 139 THR A CB  
1096 O OG1 . THR A 139 ? 0.19046 0.16770 0.14322 -0.00805 0.00851  -0.00514 139 THR A OG1 
1097 C CG2 . THR A 139 ? 0.17694 0.15746 0.13655 -0.00992 0.00814  -0.00797 139 THR A CG2 
1098 N N   . ASP A 140 ? 0.17887 0.14689 0.12538 -0.00792 0.01786  -0.00343 140 ASP A N   
1099 C CA  . ASP A 140 ? 0.18145 0.14415 0.12093 -0.00707 0.02108  -0.00206 140 ASP A CA  
1100 C C   . ASP A 140 ? 0.19159 0.15214 0.13312 -0.00816 0.02605  -0.00260 140 ASP A C   
1101 O O   . ASP A 140 ? 0.18940 0.14524 0.12432 -0.00762 0.02924  -0.00199 140 ASP A O   
1102 C CB  . ASP A 140 ? 0.17315 0.13414 0.11131 -0.00622 0.02110  0.00005  140 ASP A CB  
1103 C CG  . ASP A 140 ? 0.20996 0.17207 0.14435 -0.00464 0.01667  0.00070  140 ASP A CG  
1104 O OD1 . ASP A 140 ? 0.24842 0.21045 0.17781 -0.00381 0.01448  -0.00003 140 ASP A OD1 
1105 O OD2 . ASP A 140 ? 0.20838 0.17157 0.14515 -0.00423 0.01532  0.00176  140 ASP A OD2 
1106 N N   . MET A 141 ? 0.18225 0.14607 0.13273 -0.00958 0.02679  -0.00380 141 MET A N   
1107 C CA  . MET A 141 ? 0.19816 0.16078 0.15205 -0.01062 0.03131  -0.00471 141 MET A CA  
1108 C C   . MET A 141 ? 0.21085 0.17334 0.16281 -0.01067 0.03179  -0.00640 141 MET A C   
1109 O O   . MET A 141 ? 0.22509 0.18451 0.17511 -0.01089 0.03607  -0.00676 141 MET A O   
1110 C CB  . MET A 141 ? 0.22857 0.19497 0.19304 -0.01188 0.03138  -0.00562 141 MET A CB  
1111 C CG  . MET A 141 ? 0.18672 0.15311 0.15681 -0.01296 0.03549  -0.00703 141 MET A CG  
1112 S SD  . MET A 141 ? 0.27353 0.24384 0.24897 -0.01327 0.03360  -0.00951 141 MET A SD  
1113 C CE  . MET A 141 ? 0.11224 0.08753 0.09531 -0.01353 0.02898  -0.00984 141 MET A CE  
1114 N N   . LEU A 142 ? 0.18068 0.14619 0.13313 -0.01050 0.02774  -0.00749 142 LEU A N   
1115 C CA  . LEU A 142 ? 0.18617 0.15117 0.13613 -0.01048 0.02790  -0.00917 142 LEU A CA  
1116 C C   . LEU A 142 ? 0.19540 0.15560 0.13474 -0.00938 0.02915  -0.00865 142 LEU A C   
1117 O O   . LEU A 142 ? 0.23809 0.19580 0.17446 -0.00941 0.03192  -0.00974 142 LEU A O   
1118 C CB  . LEU A 142 ? 0.16061 0.12939 0.11296 -0.01060 0.02328  -0.01031 142 LEU A CB  
1119 C CG  . LEU A 142 ? 0.17086 0.14382 0.13259 -0.01146 0.02188  -0.01103 142 LEU A CG  
1120 C CD1 . LEU A 142 ? 0.15151 0.12716 0.11396 -0.01151 0.01771  -0.01183 142 LEU A CD1 
1121 C CD2 . LEU A 142 ? 0.22683 0.19990 0.19379 -0.01208 0.02501  -0.01244 142 LEU A CD2 
1122 N N   . VAL A 143 ? 0.17404 0.13273 0.10733 -0.00824 0.02703  -0.00705 143 VAL A N   
1123 C CA  . VAL A 143 ? 0.19842 0.15218 0.12074 -0.00683 0.02770  -0.00646 143 VAL A CA  
1124 C C   . VAL A 143 ? 0.23642 0.18498 0.15520 -0.00681 0.03359  -0.00544 143 VAL A C   
1125 O O   . VAL A 143 ? 0.30579 0.25024 0.21754 -0.00628 0.03608  -0.00596 143 VAL A O   
1126 C CB  . VAL A 143 ? 0.23444 0.18791 0.15177 -0.00534 0.02387  -0.00491 143 VAL A CB  
1127 C CG1 . VAL A 143 ? 0.28227 0.23005 0.18760 -0.00354 0.02449  -0.00410 143 VAL A CG1 
1128 C CG2 . VAL A 143 ? 0.20771 0.16622 0.12847 -0.00546 0.01847  -0.00618 143 VAL A CG2 
1129 N N   . ALA A 144 ? 0.22460 0.17307 0.14823 -0.00746 0.03609  -0.00408 144 ALA A N   
1130 C CA  . ALA A 144 ? 0.22961 0.17314 0.15091 -0.00772 0.04218  -0.00309 144 ALA A CA  
1131 C C   . ALA A 144 ? 0.26725 0.21119 0.19319 -0.00896 0.04615  -0.00505 144 ALA A C   
1132 O O   . ALA A 144 ? 0.31513 0.25416 0.23558 -0.00879 0.05096  -0.00491 144 ALA A O   
1133 C CB  . ALA A 144 ? 0.27011 0.21388 0.19678 -0.00838 0.04370  -0.00151 144 ALA A CB  
1134 N N   . ARG A 145 ? 0.22055 0.17009 0.15639 -0.01008 0.04432  -0.00688 145 ARG A N   
1135 C CA  . ARG A 145 ? 0.28553 0.23599 0.22665 -0.01103 0.04757  -0.00893 145 ARG A CA  
1136 C C   . ARG A 145 ? 0.29693 0.24480 0.23061 -0.01029 0.04792  -0.01022 145 ARG A C   
1137 O O   . ARG A 145 ? 0.33005 0.27639 0.26483 -0.01071 0.05220  -0.01152 145 ARG A O   
1138 C CB  . ARG A 145 ? 0.28889 0.24563 0.24124 -0.01194 0.04464  -0.01051 145 ARG A CB  
1139 C CG  . ARG A 145 ? 0.33913 0.29849 0.30064 -0.01293 0.04544  -0.01007 145 ARG A CG  
1140 C CD  . ARG A 145 ? 0.34207 0.30320 0.31280 -0.01399 0.04914  -0.01186 145 ARG A CD  
1141 N NE  . ARG A 145 ? 0.36496 0.32184 0.33385 -0.01444 0.05550  -0.01144 145 ARG A NE  
1142 C CZ  . ARG A 145 ? 0.34588 0.30397 0.32360 -0.01560 0.05947  -0.01245 145 ARG A CZ  
1143 N NH1 . ARG A 145 ? 0.34510 0.30857 0.33400 -0.01625 0.05737  -0.01398 145 ARG A NH1 
1144 N NH2 . ARG A 145 ? 0.35482 0.30849 0.33005 -0.01607 0.06573  -0.01197 145 ARG A NH2 
1145 N N   . ASN A 146 ? 0.30393 0.25139 0.23047 -0.00920 0.04353  -0.01009 146 ASN A N   
1146 C CA  . ASN A 146 ? 0.31365 0.25878 0.23295 -0.00849 0.04309  -0.01161 146 ASN A CA  
1147 C C   . ASN A 146 ? 0.37617 0.31443 0.28291 -0.00715 0.04579  -0.01042 146 ASN A C   
1148 O O   . ASN A 146 ? 0.49769 0.43332 0.39654 -0.00628 0.04499  -0.01161 146 ASN A O   
1149 C CB  . ASN A 146 ? 0.30491 0.25350 0.22386 -0.00815 0.03671  -0.01251 146 ASN A CB  
1150 C CG  . ASN A 146 ? 0.34739 0.29484 0.26201 -0.00790 0.03592  -0.01483 146 ASN A CG  
1151 O OD1 . ASN A 146 ? 0.37692 0.32546 0.29656 -0.00869 0.03784  -0.01663 146 ASN A OD1 
1152 N ND2 . ASN A 146 ? 0.27506 0.22032 0.18049 -0.00672 0.03289  -0.01493 146 ASN A ND2 
1153 N N   . GLY A 147 ? 0.36038 0.29530 0.26471 -0.00691 0.04897  -0.00813 147 GLY A N   
1154 C CA  . GLY A 147 ? 0.33769 0.26528 0.22939 -0.00545 0.05179  -0.00662 147 GLY A CA  
1155 C C   . GLY A 147 ? 0.31775 0.24342 0.20180 -0.00374 0.04791  -0.00446 147 GLY A C   
1156 O O   . GLY A 147 ? 0.36744 0.28648 0.24027 -0.00221 0.05003  -0.00287 147 GLY A O   
1157 N N   . GLY A 148 ? 0.32120 0.25217 0.21072 -0.00379 0.04243  -0.00434 148 GLY A N   
1158 C CA  . GLY A 148 ? 0.34914 0.27911 0.23310 -0.00213 0.03854  -0.00243 148 GLY A CA  
1159 C C   . GLY A 148 ? 0.35126 0.28376 0.23167 -0.00098 0.03206  -0.00369 148 GLY A C   
1160 O O   . GLY A 148 ? 0.40266 0.33357 0.27668 0.00087  0.02879  -0.00232 148 GLY A O   
1161 N N   . ALA A 149 ? 0.26929 0.20557 0.15389 -0.00197 0.03013  -0.00633 149 ALA A N   
1162 C CA  . ALA A 149 ? 0.31314 0.25227 0.19586 -0.00128 0.02415  -0.00791 149 ALA A CA  
1163 C C   . ALA A 149 ? 0.28428 0.22977 0.17787 -0.00317 0.02217  -0.00996 149 ALA A C   
1164 O O   . ALA A 149 ? 0.31866 0.26511 0.21841 -0.00462 0.02553  -0.01082 149 ALA A O   
1165 C CB  . ALA A 149 ? 0.32411 0.25868 0.19584 -0.00000 0.02393  -0.00932 149 ALA A CB  
1166 N N   . ALA A 150 ? 0.26879 0.21845 0.16470 -0.00304 0.01673  -0.01076 150 ALA A N   
1167 C CA  . ALA A 150 ? 0.26787 0.22308 0.17349 -0.00474 0.01479  -0.01245 150 ALA A CA  
1168 C C   . ALA A 150 ? 0.27194 0.22660 0.17627 -0.00536 0.01493  -0.01517 150 ALA A C   
1169 O O   . ALA A 150 ? 0.28648 0.23832 0.18254 -0.00431 0.01354  -0.01626 150 ALA A O   
1170 C CB  . ALA A 150 ? 0.26929 0.22894 0.17807 -0.00454 0.00946  -0.01243 150 ALA A CB  
1171 N N   . PRO A 151 ? 0.29079 0.24783 0.20294 -0.00690 0.01650  -0.01637 151 PRO A N   
1172 C CA  . PRO A 151 ? 0.25442 0.21117 0.16616 -0.00751 0.01627  -0.01906 151 PRO A CA  
1173 C C   . PRO A 151 ? 0.26456 0.22423 0.17664 -0.00769 0.01096  -0.02058 151 PRO A C   
1174 O O   . PRO A 151 ? 0.19294 0.15665 0.11051 -0.00811 0.00806  -0.01987 151 PRO A O   
1175 C CB  . PRO A 151 ? 0.28184 0.24097 0.20312 -0.00890 0.01870  -0.01954 151 PRO A CB  
1176 C CG  . PRO A 151 ? 0.25640 0.21594 0.18145 -0.00892 0.02121  -0.01725 151 PRO A CG  
1177 C CD  . PRO A 151 ? 0.26952 0.22930 0.19100 -0.00800 0.01850  -0.01541 151 PRO A CD  
1178 N N   . LEU A 152 ? 0.24752 0.20506 0.15378 -0.00741 0.00982  -0.02282 152 LEU A N   
1179 C CA  . LEU A 152 ? 0.23977 0.19979 0.14596 -0.00762 0.00479  -0.02465 152 LEU A CA  
1180 C C   . LEU A 152 ? 0.21715 0.17892 0.12883 -0.00925 0.00428  -0.02718 152 LEU A C   
1181 O O   . LEU A 152 ? 0.22913 0.19315 0.14204 -0.00981 0.00041  -0.02894 152 LEU A O   
1182 C CB  . LEU A 152 ? 0.30520 0.26167 0.20052 -0.00599 0.00283  -0.02563 152 LEU A CB  
1183 C CG  . LEU A 152 ? 0.33831 0.29271 0.22725 -0.00403 0.00245  -0.02309 152 LEU A CG  
1184 C CD1 . LEU A 152 ? 0.32372 0.27561 0.20272 -0.00224 -0.00121 -0.02435 152 LEU A CD1 
1185 C CD2 . LEU A 152 ? 0.31240 0.27133 0.20845 -0.00425 0.00046  -0.02110 152 LEU A CD2 
1186 N N   . THR A 153 ? 0.22897 0.18973 0.14429 -0.00999 0.00807  -0.02747 153 THR A N   
1187 C CA  . THR A 153 ? 0.29357 0.25570 0.21464 -0.01138 0.00784  -0.02952 153 THR A CA  
1188 C C   . THR A 153 ? 0.25412 0.21859 0.18409 -0.01213 0.00986  -0.02812 153 THR A C   
1189 O O   . THR A 153 ? 0.18845 0.15232 0.11940 -0.01164 0.01284  -0.02634 153 THR A O   
1190 C CB  . THR A 153 ? 0.25882 0.21691 0.17525 -0.01128 0.01024  -0.03188 153 THR A CB  
1191 O OG1 . THR A 153 ? 0.25608 0.21208 0.17335 -0.01093 0.01519  -0.03092 153 THR A OG1 
1192 C CG2 . THR A 153 ? 0.27018 0.22496 0.17605 -0.01012 0.00876  -0.03304 153 THR A CG2 
1193 N N   . MET A 154 ? 0.20088 0.16785 0.13729 -0.01331 0.00819  -0.02902 154 MET A N   
1194 C CA  . MET A 154 ? 0.23311 0.20208 0.17751 -0.01380 0.00954  -0.02784 154 MET A CA  
1195 C C   . MET A 154 ? 0.24987 0.21660 0.19561 -0.01350 0.01358  -0.02838 154 MET A C   
1196 O O   . MET A 154 ? 0.31396 0.28188 0.26491 -0.01334 0.01540  -0.02705 154 MET A O   
1197 C CB  . MET A 154 ? 0.21511 0.18627 0.16487 -0.01497 0.00705  -0.02869 154 MET A CB  
1198 C CG  . MET A 154 ? 0.24591 0.21831 0.20299 -0.01525 0.00822  -0.02779 154 MET A CG  
1199 S SD  . MET A 154 ? 0.28663 0.26137 0.24722 -0.01463 0.00886  -0.02488 154 MET A SD  
1200 C CE  . MET A 154 ? 0.16193 0.13958 0.12237 -0.01506 0.00509  -0.02386 154 MET A CE  
1201 N N   . GLN A 155 ? 0.24149 0.20505 0.18282 -0.01336 0.01499  -0.03049 155 GLN A N   
1202 C CA  . GLN A 155 ? 0.27497 0.23642 0.21784 -0.01300 0.01908  -0.03126 155 GLN A CA  
1203 C C   . GLN A 155 ? 0.24441 0.20495 0.18604 -0.01223 0.02254  -0.02958 155 GLN A C   
1204 O O   . GLN A 155 ? 0.29831 0.25950 0.24567 -0.01212 0.02535  -0.02919 155 GLN A O   
1205 C CB  . GLN A 155 ? 0.25044 0.20829 0.18777 -0.01294 0.01997  -0.03397 155 GLN A CB  
1206 C CG  . GLN A 155 ? 0.36532 0.32099 0.30474 -0.01255 0.02423  -0.03515 155 GLN A CG  
1207 C CD  . GLN A 155 ? 0.31407 0.26876 0.25582 -0.01306 0.02359  -0.03757 155 GLN A CD  
1208 O OE1 . GLN A 155 ? 0.32072 0.27198 0.25818 -0.01280 0.02549  -0.03976 155 GLN A OE1 
1209 N NE2 . GLN A 155 ? 0.30681 0.26408 0.25505 -0.01375 0.02111  -0.03716 155 GLN A NE2 
1210 N N   . SER A 156 ? 0.22270 0.18165 0.15712 -0.01164 0.02234  -0.02861 156 SER A N   
1211 C CA  . SER A 156 ? 0.27107 0.22857 0.20384 -0.01100 0.02587  -0.02684 156 SER A CA  
1212 C C   . SER A 156 ? 0.23801 0.19894 0.17691 -0.01124 0.02498  -0.02452 156 SER A C   
1213 O O   . SER A 156 ? 0.24027 0.20110 0.18237 -0.01116 0.02829  -0.02346 156 SER A O   
1214 C CB  . SER A 156 ? 0.31365 0.26739 0.23557 -0.01005 0.02602  -0.02647 156 SER A CB  
1215 O OG  . SER A 156 ? 0.31106 0.26655 0.23058 -0.00986 0.02143  -0.02563 156 SER A OG  
1216 N N   . PHE A 157 ? 0.24360 0.20752 0.18439 -0.01158 0.02070  -0.02387 157 PHE A N   
1217 C CA  . PHE A 157 ? 0.22314 0.19018 0.16952 -0.01176 0.01971  -0.02185 157 PHE A CA  
1218 C C   . PHE A 157 ? 0.21830 0.18750 0.17363 -0.01223 0.02096  -0.02205 157 PHE A C   
1219 O O   . PHE A 157 ? 0.22887 0.19936 0.18855 -0.01221 0.02228  -0.02073 157 PHE A O   
1220 C CB  . PHE A 157 ? 0.18668 0.15638 0.13327 -0.01201 0.01508  -0.02141 157 PHE A CB  
1221 C CG  . PHE A 157 ? 0.20490 0.17753 0.15652 -0.01212 0.01396  -0.01944 157 PHE A CG  
1222 C CD1 . PHE A 157 ? 0.19331 0.16537 0.14203 -0.01147 0.01435  -0.01758 157 PHE A CD1 
1223 C CD2 . PHE A 157 ? 0.20793 0.18344 0.16666 -0.01276 0.01256  -0.01945 157 PHE A CD2 
1224 C CE1 . PHE A 157 ? 0.17639 0.15092 0.12962 -0.01156 0.01336  -0.01596 157 PHE A CE1 
1225 C CE2 . PHE A 157 ? 0.17765 0.15555 0.14039 -0.01278 0.01151  -0.01780 157 PHE A CE2 
1226 C CZ  . PHE A 157 ? 0.13395 0.11147 0.09414 -0.01223 0.01192  -0.01616 157 PHE A CZ  
1227 N N   . THR A 158 ? 0.23874 0.20825 0.19697 -0.01257 0.02036  -0.02376 158 THR A N   
1228 C CA  . THR A 158 ? 0.25362 0.22494 0.22003 -0.01266 0.02113  -0.02400 158 THR A CA  
1229 C C   . THR A 158 ? 0.24204 0.21217 0.21070 -0.01227 0.02553  -0.02441 158 THR A C   
1230 O O   . THR A 158 ? 0.30017 0.27236 0.27597 -0.01218 0.02632  -0.02406 158 THR A O   
1231 C CB  . THR A 158 ? 0.25772 0.22893 0.22602 -0.01294 0.01956  -0.02565 158 THR A CB  
1232 O OG1 . THR A 158 ? 0.22751 0.19905 0.19231 -0.01351 0.01620  -0.02576 158 THR A OG1 
1233 C CG2 . THR A 158 ? 0.21672 0.19019 0.19300 -0.01282 0.01872  -0.02529 158 THR A CG2 
1234 N N   . LYS A 159 ? 0.23586 0.20264 0.19859 -0.01201 0.02846  -0.02526 159 LYS A N   
1235 C CA  . LYS A 159 ? 0.28675 0.25217 0.25135 -0.01175 0.03330  -0.02558 159 LYS A CA  
1236 C C   . LYS A 159 ? 0.25937 0.22540 0.22497 -0.01184 0.03482  -0.02361 159 LYS A C   
1237 O O   . LYS A 159 ? 0.24194 0.20870 0.21333 -0.01193 0.03805  -0.02369 159 LYS A O   
1238 C CB  . LYS A 159 ? 0.24442 0.20548 0.20120 -0.01140 0.03628  -0.02691 159 LYS A CB  
1239 C CG  . LYS A 159 ? 0.28655 0.24655 0.24311 -0.01133 0.03571  -0.02927 159 LYS A CG  
1240 C CD  . LYS A 159 ? 0.26807 0.22341 0.21631 -0.01091 0.03887  -0.03072 159 LYS A CD  
1241 C CE  . LYS A 159 ? 0.27038 0.22440 0.21854 -0.01087 0.03844  -0.03329 159 LYS A CE  
1242 N NZ  . LYS A 159 ? 0.26698 0.21615 0.20639 -0.01040 0.04144  -0.03491 159 LYS A NZ  
1243 N N   . LEU A 160 ? 0.27136 0.23716 0.23188 -0.01183 0.03255  -0.02197 160 LEU A N   
1244 C CA  . LEU A 160 ? 0.25843 0.22434 0.21950 -0.01189 0.03392  -0.02002 160 LEU A CA  
1245 C C   . LEU A 160 ? 0.25085 0.22089 0.22119 -0.01230 0.03222  -0.01945 160 LEU A C   
1246 O O   . LEU A 160 ? 0.25681 0.22747 0.23198 -0.01257 0.03480  -0.01899 160 LEU A O   
1247 C CB  . LEU A 160 ? 0.21342 0.17774 0.16629 -0.01147 0.03168  -0.01849 160 LEU A CB  
1248 C CG  . LEU A 160 ? 0.30934 0.27314 0.26177 -0.01140 0.03286  -0.01630 160 LEU A CG  
1249 C CD1 . LEU A 160 ? 0.27372 0.23370 0.22364 -0.01134 0.03852  -0.01601 160 LEU A CD1 
1250 C CD2 . LEU A 160 ? 0.27299 0.23599 0.21845 -0.01072 0.02956  -0.01488 160 LEU A CD2 
1251 N N   . VAL A 161 ? 0.23098 0.20369 0.20381 -0.01238 0.02793  -0.01956 161 VAL A N   
1252 C CA  . VAL A 161 ? 0.23049 0.20665 0.21081 -0.01257 0.02597  -0.01894 161 VAL A CA  
1253 C C   . VAL A 161 ? 0.26850 0.24619 0.25700 -0.01250 0.02766  -0.02030 161 VAL A C   
1254 O O   . VAL A 161 ? 0.21919 0.19922 0.21418 -0.01258 0.02738  -0.02000 161 VAL A O   
1255 C CB  . VAL A 161 ? 0.25716 0.23518 0.23720 -0.01261 0.02134  -0.01862 161 VAL A CB  
1256 C CG1 . VAL A 161 ? 0.20808 0.18510 0.18099 -0.01257 0.01961  -0.01748 161 VAL A CG1 
1257 C CG2 . VAL A 161 ? 0.23984 0.21765 0.22055 -0.01258 0.02030  -0.02023 161 VAL A CG2 
1258 N N   . ASP A 162 ? 0.27896 0.25538 0.26751 -0.01225 0.02931  -0.02197 162 ASP A N   
1259 C CA  . ASP A 162 ? 0.25224 0.23016 0.24891 -0.01194 0.03105  -0.02340 162 ASP A CA  
1260 C C   . ASP A 162 ? 0.26609 0.24368 0.26575 -0.01222 0.03556  -0.02349 162 ASP A C   
1261 O O   . ASP A 162 ? 0.22947 0.20962 0.23776 -0.01214 0.03624  -0.02421 162 ASP A O   
1262 C CB  . ASP A 162 ? 0.27858 0.25498 0.27448 -0.01149 0.03175  -0.02522 162 ASP A CB  
1263 C CG  . ASP A 162 ? 0.25953 0.23644 0.25464 -0.01131 0.02752  -0.02534 162 ASP A CG  
1264 O OD1 . ASP A 162 ? 0.25658 0.23455 0.24981 -0.01164 0.02431  -0.02394 162 ASP A OD1 
1265 O OD2 . ASP A 162 ? 0.34155 0.31763 0.33806 -0.01085 0.02762  -0.02683 162 ASP A OD2 
1266 N N   A ARG A 163 ? 0.25882 0.23311 0.25151 -0.01251 0.03870  -0.02285 163 ARG A N   
1267 N N   B ARG A 163 ? 0.25902 0.23333 0.25170 -0.01251 0.03867  -0.02283 163 ARG A N   
1268 C CA  A ARG A 163 ? 0.26993 0.24327 0.26480 -0.01296 0.04348  -0.02266 163 ARG A CA  
1269 C CA  B ARG A 163 ? 0.27004 0.24331 0.26474 -0.01296 0.04350  -0.02265 163 ARG A CA  
1270 C C   A ARG A 163 ? 0.28132 0.25596 0.27815 -0.01349 0.04259  -0.02096 163 ARG A C   
1271 C C   B ARG A 163 ? 0.28131 0.25568 0.27752 -0.01350 0.04276  -0.02089 163 ARG A C   
1272 O O   A ARG A 163 ? 0.28275 0.25776 0.28472 -0.01406 0.04597  -0.02105 163 ARG A O   
1273 O O   B ARG A 163 ? 0.28220 0.25648 0.28261 -0.01407 0.04642  -0.02086 163 ARG A O   
1274 C CB  A ARG A 163 ? 0.27723 0.24567 0.26286 -0.01291 0.04750  -0.02243 163 ARG A CB  
1275 C CB  B ARG A 163 ? 0.27739 0.24579 0.26296 -0.01288 0.04751  -0.02255 163 ARG A CB  
1276 C CG  A ARG A 163 ? 0.26803 0.23454 0.25092 -0.01241 0.04892  -0.02432 163 ARG A CG  
1277 C CG  B ARG A 163 ? 0.29632 0.26180 0.27345 -0.01298 0.04769  -0.02035 163 ARG A CG  
1278 C CD  A ARG A 163 ? 0.31261 0.27401 0.28713 -0.01232 0.05388  -0.02425 163 ARG A CD  
1279 C CD  B ARG A 163 ? 0.29426 0.25484 0.25990 -0.01240 0.04916  -0.02031 163 ARG A CD  
1280 N NE  A ARG A 163 ? 0.33820 0.29694 0.30483 -0.01237 0.05381  -0.02200 163 ARG A NE  
1281 N NE  B ARG A 163 ? 0.33649 0.29430 0.30142 -0.01234 0.05449  -0.02177 163 ARG A NE  
1282 C CZ  A ARG A 163 ? 0.32946 0.28549 0.28585 -0.01180 0.05136  -0.02125 163 ARG A CZ  
1283 C CZ  B ARG A 163 ? 0.31904 0.27611 0.28272 -0.01193 0.05464  -0.02374 163 ARG A CZ  
1284 N NH1 A ARG A 163 ? 0.32137 0.27696 0.27405 -0.01138 0.04885  -0.02267 163 ARG A NH1 
1285 N NH1 B ARG A 163 ? 0.29057 0.24938 0.25383 -0.01167 0.04982  -0.02449 163 ARG A NH1 
1286 N NH2 A ARG A 163 ? 0.32370 0.27737 0.27365 -0.01160 0.05132  -0.01913 163 ARG A NH2 
1287 N NH2 B ARG A 163 ? 0.34891 0.30319 0.31178 -0.01184 0.06000  -0.02502 163 ARG A NH2 
1288 N N   . VAL A 164 ? 0.24221 0.21751 0.23541 -0.01338 0.03832  -0.01954 164 VAL A N   
1289 C CA  . VAL A 164 ? 0.29021 0.26661 0.28517 -0.01378 0.03732  -0.01802 164 VAL A CA  
1290 C C   . VAL A 164 ? 0.24403 0.22465 0.24907 -0.01391 0.03515  -0.01884 164 VAL A C   
1291 O O   . VAL A 164 ? 0.28592 0.26761 0.29576 -0.01446 0.03621  -0.01854 164 VAL A O   
1292 C CB  . VAL A 164 ? 0.26887 0.24444 0.25637 -0.01346 0.03371  -0.01633 164 VAL A CB  
1293 C CG1 . VAL A 164 ? 0.27136 0.24914 0.26230 -0.01368 0.03124  -0.01516 164 VAL A CG1 
1294 C CG2 . VAL A 164 ? 0.31330 0.28445 0.29122 -0.01321 0.03616  -0.01519 164 VAL A CG2 
1295 N N   . GLY A 165 ? 0.21970 0.20248 0.22791 -0.01335 0.03211  -0.01993 165 GLY A N   
1296 C CA  . GLY A 165 ? 0.23747 0.22383 0.25447 -0.01309 0.02971  -0.02083 165 GLY A CA  
1297 C C   . GLY A 165 ? 0.20876 0.19647 0.22432 -0.01263 0.02460  -0.02006 165 GLY A C   
1298 O O   . GLY A 165 ? 0.17788 0.16417 0.18651 -0.01263 0.02296  -0.01898 165 GLY A O   
1299 N N   . ASP A 166 ? 0.21931 0.20977 0.24173 -0.01217 0.02212  -0.02076 166 ASP A N   
1300 C CA  . ASP A 166 ? 0.16347 0.15491 0.18466 -0.01170 0.01764  -0.01997 166 ASP A CA  
1301 C C   . ASP A 166 ? 0.18177 0.17287 0.19907 -0.01228 0.01675  -0.01827 166 ASP A C   
1302 O O   . ASP A 166 ? 0.12768 0.11858 0.14613 -0.01290 0.01898  -0.01795 166 ASP A O   
1303 C CB  . ASP A 166 ? 0.13787 0.13190 0.16665 -0.01087 0.01518  -0.02108 166 ASP A CB  
1304 C CG  . ASP A 166 ? 0.13087 0.12491 0.16181 -0.00979 0.01425  -0.02229 166 ASP A CG  
1305 O OD1 . ASP A 166 ? 0.21447 0.20659 0.24004 -0.00970 0.01377  -0.02183 166 ASP A OD1 
1306 O OD2 . ASP A 166 ? 0.28926 0.28521 0.32754 -0.00898 0.01392  -0.02379 166 ASP A OD2 
1307 N N   . PRO A 167 ? 0.14545 0.13633 0.15835 -0.01208 0.01374  -0.01719 167 PRO A N   
1308 C CA  . PRO A 167 ? 0.14293 0.13366 0.15252 -0.01242 0.01272  -0.01566 167 PRO A CA  
1309 C C   . PRO A 167 ? 0.16812 0.16057 0.18299 -0.01241 0.01172  -0.01583 167 PRO A C   
1310 O O   . PRO A 167 ? 0.10823 0.10232 0.12888 -0.01192 0.01053  -0.01708 167 PRO A O   
1311 C CB  . PRO A 167 ? 0.14388 0.13452 0.14936 -0.01215 0.00966  -0.01495 167 PRO A CB  
1312 C CG  . PRO A 167 ? 0.11338 0.10324 0.11826 -0.01192 0.00987  -0.01593 167 PRO A CG  
1313 C CD  . PRO A 167 ? 0.10500 0.09554 0.11587 -0.01158 0.01144  -0.01737 167 PRO A CD  
1314 N N   . PRO A 168 ? 0.12205 0.11406 0.13515 -0.01283 0.01205  -0.01471 168 PRO A N   
1315 C CA  . PRO A 168 ? 0.13008 0.12353 0.14784 -0.01287 0.01079  -0.01502 168 PRO A CA  
1316 C C   . PRO A 168 ? 0.14999 0.14479 0.16873 -0.01206 0.00684  -0.01528 168 PRO A C   
1317 O O   . PRO A 168 ? 0.17177 0.16600 0.18590 -0.01173 0.00509  -0.01438 168 PRO A O   
1318 C CB  . PRO A 168 ? 0.13613 0.12817 0.14983 -0.01329 0.01160  -0.01346 168 PRO A CB  
1319 C CG  . PRO A 168 ? 0.11117 0.10092 0.11994 -0.01355 0.01458  -0.01270 168 PRO A CG  
1320 C CD  . PRO A 168 ? 0.15220 0.14208 0.15913 -0.01317 0.01380  -0.01329 168 PRO A CD  
1321 N N   . ALA A 169 ? 0.17697 0.17343 0.20177 -0.01171 0.00550  -0.01661 169 ALA A N   
1322 C CA  . ALA A 169 ? 0.16474 0.16192 0.19000 -0.01067 0.00175  -0.01691 169 ALA A CA  
1323 C C   . ALA A 169 ? 0.11905 0.11563 0.14019 -0.01065 -0.00006 -0.01565 169 ALA A C   
1324 O O   . ALA A 169 ? 0.14975 0.14594 0.16993 -0.01134 0.00123  -0.01500 169 ALA A O   
1325 C CB  . ALA A 169 ? 0.16277 0.16188 0.19544 -0.01009 0.00038  -0.01884 169 ALA A CB  
1326 N N   . PRO A 170 ? 0.11748 0.11365 0.13594 -0.00980 -0.00281 -0.01523 170 PRO A N   
1327 C CA  . PRO A 170 ? 0.09819 0.09374 0.11280 -0.00973 -0.00423 -0.01413 170 PRO A CA  
1328 C C   . PRO A 170 ? 0.14341 0.13967 0.16123 -0.00964 -0.00527 -0.01494 170 PRO A C   
1329 O O   . PRO A 170 ? 0.12230 0.11963 0.14510 -0.00918 -0.00644 -0.01652 170 PRO A O   
1330 C CB  . PRO A 170 ? 0.09250 0.08714 0.10424 -0.00880 -0.00653 -0.01377 170 PRO A CB  
1331 C CG  . PRO A 170 ? 0.11464 0.10958 0.12993 -0.00806 -0.00716 -0.01497 170 PRO A CG  
1332 C CD  . PRO A 170 ? 0.11831 0.11406 0.13652 -0.00888 -0.00431 -0.01558 170 PRO A CD  
1333 N N   . ALA A 171 ? 0.11388 0.10956 0.12904 -0.01003 -0.00492 -0.01400 171 ALA A N   
1334 C CA  . ALA A 171 ? 0.13231 0.12829 0.15014 -0.01008 -0.00572 -0.01482 171 ALA A CA  
1335 C C   . ALA A 171 ? 0.14896 0.14475 0.16609 -0.00892 -0.00912 -0.01548 171 ALA A C   
1336 O O   . ALA A 171 ? 0.18367 0.17851 0.19658 -0.00822 -0.01034 -0.01460 171 ALA A O   
1337 C CB  . ALA A 171 ? 0.15979 0.15479 0.17463 -0.01065 -0.00428 -0.01356 171 ALA A CB  
1338 N N   . PRO A 172 ? 0.16714 0.16358 0.18822 -0.00869 -0.01065 -0.01709 172 PRO A N   
1339 C CA  . PRO A 172 ? 0.20678 0.20263 0.22649 -0.00735 -0.01415 -0.01786 172 PRO A CA  
1340 C C   . PRO A 172 ? 0.17515 0.16923 0.18871 -0.00707 -0.01459 -0.01652 172 PRO A C   
1341 O O   . PRO A 172 ? 0.16586 0.15957 0.17737 -0.00788 -0.01254 -0.01532 172 PRO A O   
1342 C CB  . PRO A 172 ? 0.18067 0.17786 0.20655 -0.00744 -0.01542 -0.02016 172 PRO A CB  
1343 C CG  . PRO A 172 ? 0.16831 0.16597 0.19705 -0.00909 -0.01208 -0.02001 172 PRO A CG  
1344 C CD  . PRO A 172 ? 0.14082 0.13835 0.16778 -0.00968 -0.00921 -0.01843 172 PRO A CD  
1345 N N   . ASP A 173 ? 0.20499 0.19776 0.21544 -0.00573 -0.01730 -0.01675 173 ASP A N   
1346 C CA  . ASP A 173 ? 0.19804 0.18892 0.20265 -0.00534 -0.01760 -0.01565 173 ASP A CA  
1347 C C   . ASP A 173 ? 0.19727 0.18808 0.20288 -0.00571 -0.01760 -0.01647 173 ASP A C   
1348 O O   . ASP A 173 ? 0.16872 0.16049 0.17910 -0.00584 -0.01867 -0.01834 173 ASP A O   
1349 C CB  . ASP A 173 ? 0.20853 0.19736 0.20908 -0.00370 -0.02030 -0.01575 173 ASP A CB  
1350 C CG  . ASP A 173 ? 0.28973 0.27802 0.28911 -0.00324 -0.02026 -0.01491 173 ASP A CG  
1351 O OD1 . ASP A 173 ? 0.24530 0.23449 0.24527 -0.00431 -0.01788 -0.01389 173 ASP A OD1 
1352 O OD2 . ASP A 173 ? 0.32724 0.31392 0.32484 -0.00171 -0.02270 -0.01531 173 ASP A OD2 
1353 N N   . PRO A 174 ? 0.15432 0.14404 0.15591 -0.00589 -0.01639 -0.01524 174 PRO A N   
1354 C CA  . PRO A 174 ? 0.21838 0.20759 0.22049 -0.00612 -0.01630 -0.01598 174 PRO A CA  
1355 C C   . PRO A 174 ? 0.18453 0.17248 0.18572 -0.00498 -0.01938 -0.01775 174 PRO A C   
1356 O O   . PRO A 174 ? 0.18763 0.17464 0.18627 -0.00378 -0.02150 -0.01793 174 PRO A O   
1357 C CB  . PRO A 174 ? 0.19053 0.17882 0.18803 -0.00617 -0.01451 -0.01414 174 PRO A CB  
1358 C CG  . PRO A 174 ? 0.22218 0.20998 0.21594 -0.00566 -0.01468 -0.01295 174 PRO A CG  
1359 C CD  . PRO A 174 ? 0.19836 0.18733 0.19516 -0.00588 -0.01503 -0.01328 174 PRO A CD  
1360 N N   . PRO A 175 ? 0.21148 0.19906 0.21442 -0.00522 -0.01980 -0.01914 175 PRO A N   
1361 C CA  . PRO A 175 ? 0.20429 0.19053 0.20604 -0.00407 -0.02305 -0.02115 175 PRO A CA  
1362 C C   . PRO A 175 ? 0.19822 0.18177 0.19215 -0.00268 -0.02390 -0.02014 175 PRO A C   
1363 O O   . PRO A 175 ? 0.16998 0.15283 0.16013 -0.00287 -0.02160 -0.01814 175 PRO A O   
1364 C CB  . PRO A 175 ? 0.23418 0.22020 0.23875 -0.00490 -0.02248 -0.02252 175 PRO A CB  
1365 C CG  . PRO A 175 ? 0.23189 0.21821 0.23657 -0.00606 -0.01875 -0.02050 175 PRO A CG  
1366 C CD  . PRO A 175 ? 0.22635 0.21436 0.23231 -0.00650 -0.01740 -0.01906 175 PRO A CD  
1367 N N   . ALA A 176 ? 0.18172 0.16368 0.17326 -0.00119 -0.02725 -0.02165 176 ALA A N   
1368 C CA  . ALA A 176 ? 0.20771 0.18637 0.19109 0.00029  -0.02796 -0.02076 176 ALA A CA  
1369 C C   . ALA A 176 ? 0.19919 0.17616 0.17892 0.00013  -0.02624 -0.02042 176 ALA A C   
1370 O O   . ALA A 176 ? 0.20803 0.18250 0.18124 0.00092  -0.02533 -0.01913 176 ALA A O   
1371 C CB  . ALA A 176 ? 0.22549 0.20230 0.20652 0.00218  -0.03220 -0.02261 176 ALA A CB  
1372 N N   . ALA A 177 ? 0.20818 0.18625 0.19211 -0.00088 -0.02553 -0.02158 177 ALA A N   
1373 C CA  . ALA A 177 ? 0.21093 0.18757 0.19234 -0.00106 -0.02363 -0.02128 177 ALA A CA  
1374 C C   . ALA A 177 ? 0.19655 0.17533 0.18343 -0.00267 -0.02099 -0.02070 177 ALA A C   
1375 O O   . ALA A 177 ? 0.19783 0.17847 0.19076 -0.00363 -0.02132 -0.02172 177 ALA A O   
1376 C CB  . ALA A 177 ? 0.20298 0.17732 0.18243 -0.00018 -0.02607 -0.02378 177 ALA A CB  
1377 N N   . MET A 178 ? 0.20204 0.18042 0.18679 -0.00285 -0.01828 -0.01904 178 MET A N   
1378 C CA  . MET A 178 ? 0.20998 0.18974 0.19870 -0.00400 -0.01580 -0.01817 178 MET A CA  
1379 C C   . MET A 178 ? 0.14863 0.12662 0.13618 -0.00377 -0.01471 -0.01859 178 MET A C   
1380 O O   . MET A 178 ? 0.18634 0.16237 0.16916 -0.00272 -0.01503 -0.01887 178 MET A O   
1381 C CB  . MET A 178 ? 0.23513 0.21646 0.22314 -0.00432 -0.01360 -0.01567 178 MET A CB  
1382 C CG  . MET A 178 ? 0.24526 0.22851 0.23587 -0.00493 -0.01394 -0.01522 178 MET A CG  
1383 S SD  . MET A 178 ? 0.33404 0.31856 0.32237 -0.00507 -0.01197 -0.01271 178 MET A SD  
1384 C CE  . MET A 178 ? 0.26046 0.24291 0.24278 -0.00390 -0.01218 -0.01242 178 MET A CE  
1385 N N   . PRO A 179 ? 0.19322 0.17146 0.18474 -0.00465 -0.01321 -0.01863 179 PRO A N   
1386 C CA  . PRO A 179 ? 0.20189 0.17816 0.19246 -0.00434 -0.01198 -0.01891 179 PRO A CA  
1387 C C   . PRO A 179 ? 0.18672 0.16289 0.17344 -0.00345 -0.01014 -0.01693 179 PRO A C   
1388 O O   . PRO A 179 ? 0.19242 0.17040 0.17965 -0.00367 -0.00871 -0.01493 179 PRO A O   
1389 C CB  . PRO A 179 ? 0.16651 0.14301 0.16213 -0.00553 -0.01031 -0.01873 179 PRO A CB  
1390 C CG  . PRO A 179 ? 0.15273 0.13106 0.15246 -0.00655 -0.01129 -0.01943 179 PRO A CG  
1391 C CD  . PRO A 179 ? 0.17908 0.15895 0.17605 -0.00595 -0.01243 -0.01852 179 PRO A CD  
1392 N N   . PRO A 180 ? 0.18502 0.15918 0.16803 -0.00243 -0.01012 -0.01759 180 PRO A N   
1393 C CA  . PRO A 180 ? 0.17982 0.15416 0.15975 -0.00156 -0.00826 -0.01597 180 PRO A CA  
1394 C C   . PRO A 180 ? 0.18941 0.16374 0.17137 -0.00139 -0.00617 -0.01500 180 PRO A C   
1395 O O   . PRO A 180 ? 0.13300 0.10624 0.11781 -0.00188 -0.00603 -0.01571 180 PRO A O   
1396 C CB  . PRO A 180 ? 0.22276 0.19444 0.19783 -0.00047 -0.00896 -0.01739 180 PRO A CB  
1397 C CG  . PRO A 180 ? 0.22929 0.19904 0.20583 -0.00071 -0.01065 -0.01982 180 PRO A CG  
1398 C CD  . PRO A 180 ? 0.19560 0.16721 0.17709 -0.00199 -0.01187 -0.02011 180 PRO A CD  
1399 N N   . PRO A 181 ? 0.19522 0.17066 0.17604 -0.00067 -0.00451 -0.01342 181 PRO A N   
1400 C CA  . PRO A 181 ? 0.17738 0.15243 0.15962 0.00000  -0.00282 -0.01265 181 PRO A CA  
1401 C C   . PRO A 181 ? 0.19484 0.16684 0.17566 0.00078  -0.00256 -0.01429 181 PRO A C   
1402 O O   . PRO A 181 ? 0.17974 0.15020 0.15738 0.00113  -0.00334 -0.01575 181 PRO A O   
1403 C CB  . PRO A 181 ? 0.22876 0.20612 0.21026 0.00073  -0.00156 -0.01105 181 PRO A CB  
1404 C CG  . PRO A 181 ? 0.20969 0.18891 0.19035 -0.00006 -0.00239 -0.01061 181 PRO A CG  
1405 C CD  . PRO A 181 ? 0.18431 0.16157 0.16311 -0.00046 -0.00408 -0.01226 181 PRO A CD  
1406 N N   . ALA A 182 ? 0.20313 0.17382 0.18590 0.00115  -0.00145 -0.01404 182 ALA A N   
1407 C CA  . ALA A 182 ? 0.21811 0.18570 0.19975 0.00198  -0.00092 -0.01557 182 ALA A CA  
1408 C C   . ALA A 182 ? 0.24689 0.21471 0.22581 0.00344  0.00038  -0.01531 182 ALA A C   
1409 O O   . ALA A 182 ? 0.24561 0.21602 0.22524 0.00400  0.00143  -0.01357 182 ALA A O   
1410 C CB  . ALA A 182 ? 0.19729 0.16308 0.18169 0.00212  0.00025  -0.01510 182 ALA A CB  
1411 N N   . GLU A 183 ? 0.24881 0.21392 0.22476 0.00406  0.00037  -0.01721 183 GLU A N   
1412 C CA  . GLU A 183 ? 0.22154 0.18646 0.19465 0.00540  0.00200  -0.01721 183 GLU A CA  
1413 C C   . GLU A 183 ? 0.22480 0.18946 0.20001 0.00675  0.00401  -0.01656 183 GLU A C   
1414 O O   . GLU A 183 ? 0.29007 0.25293 0.26743 0.00683  0.00405  -0.01676 183 GLU A O   
1415 C CB  . GLU A 183 ? 0.26389 0.22542 0.23223 0.00577  0.00138  -0.01955 183 GLU A CB  
1416 C CG  . GLU A 183 ? 0.24606 0.20761 0.21132 0.00501  -0.00065 -0.02011 183 GLU A CG  
1417 C CD  . GLU A 183 ? 0.24522 0.20292 0.20485 0.00570  -0.00153 -0.02245 183 GLU A CD  
1418 O OE1 . GLU A 183 ? 0.24575 0.20063 0.20490 0.00624  -0.00136 -0.02422 183 GLU A OE1 
1419 O OE2 . GLU A 183 ? 0.24455 0.20167 0.19983 0.00582  -0.00240 -0.02254 183 GLU A OE2 
1420 N N   . ASP A 184 ? 0.24775 0.21413 0.22253 0.00786  0.00579  -0.01579 184 ASP A N   
1421 C CA  . ASP A 184 ? 0.28313 0.24962 0.25997 0.00953  0.00771  -0.01533 184 ASP A CA  
1422 C C   . ASP A 184 ? 0.24333 0.21144 0.22431 0.00982  0.00743  -0.01352 184 ASP A C   
1423 O O   . ASP A 184 ? 0.27242 0.23891 0.25492 0.01114  0.00829  -0.01341 184 ASP A O   
1424 C CB  . ASP A 184 ? 0.27698 0.23913 0.25184 0.01044  0.00847  -0.01734 184 ASP A CB  
1425 C CG  . ASP A 184 ? 0.30831 0.26850 0.27818 0.01063  0.00907  -0.01908 184 ASP A CG  
1426 O OD1 . ASP A 184 ? 0.36276 0.32506 0.33115 0.01045  0.00976  -0.01839 184 ASP A OD1 
1427 O OD2 . ASP A 184 ? 0.37798 0.33417 0.34511 0.01096  0.00893  -0.02118 184 ASP A OD2 
1428 N N   . MET A 185 ? 0.20889 0.17980 0.19128 0.00874  0.00626  -0.01207 185 MET A N   
1429 C CA  . MET A 185 ? 0.18288 0.15555 0.16833 0.00932  0.00609  -0.01016 185 MET A CA  
1430 C C   . MET A 185 ? 0.17952 0.15621 0.16689 0.01045  0.00681  -0.00914 185 MET A C   
1431 O O   . MET A 185 ? 0.20669 0.18596 0.19362 0.00962  0.00683  -0.00918 185 MET A O   
1432 C CB  . MET A 185 ? 0.21514 0.18865 0.20106 0.00770  0.00461  -0.00924 185 MET A CB  
1433 C CG  . MET A 185 ? 0.23485 0.20489 0.22032 0.00650  0.00398  -0.01024 185 MET A CG  
1434 S SD  . MET A 185 ? 0.26800 0.23422 0.25486 0.00758  0.00503  -0.00976 185 MET A SD  
1435 C CE  . MET A 185 ? 0.28669 0.24956 0.27382 0.00551  0.00436  -0.01148 185 MET A CE  
1436 N N   . PRO A 186 ? 0.16211 0.13937 0.15186 0.01234  0.00738  -0.00830 186 PRO A N   
1437 C CA  . PRO A 186 ? 0.17443 0.15580 0.16687 0.01356  0.00807  -0.00787 186 PRO A CA  
1438 C C   . PRO A 186 ? 0.16557 0.15118 0.15949 0.01259  0.00689  -0.00681 186 PRO A C   
1439 O O   . PRO A 186 ? 0.11110 0.09990 0.10635 0.01231  0.00764  -0.00717 186 PRO A O   
1440 C CB  . PRO A 186 ? 0.23398 0.21467 0.22871 0.01599  0.00829  -0.00714 186 PRO A CB  
1441 C CG  . PRO A 186 ? 0.22038 0.19708 0.21348 0.01567  0.00745  -0.00645 186 PRO A CG  
1442 C CD  . PRO A 186 ? 0.18786 0.16184 0.17811 0.01358  0.00749  -0.00783 186 PRO A CD  
1443 N N   . SER A 187 ? 0.14682 0.13234 0.14053 0.01201  0.00528  -0.00558 187 SER A N   
1444 C CA  . SER A 187 ? 0.16935 0.15859 0.16414 0.01106  0.00409  -0.00476 187 SER A CA  
1445 C C   . SER A 187 ? 0.19021 0.17993 0.18322 0.00885  0.00409  -0.00544 187 SER A C   
1446 O O   . SER A 187 ? 0.16364 0.15643 0.15763 0.00795  0.00341  -0.00501 187 SER A O   
1447 C CB  . SER A 187 ? 0.15547 0.14388 0.14975 0.01115  0.00261  -0.00329 187 SER A CB  
1448 O OG  . SER A 187 ? 0.22170 0.21019 0.21745 0.01350  0.00228  -0.00235 187 SER A OG  
1449 N N   . ALA A 188 ? 0.19901 0.18558 0.18932 0.00809  0.00468  -0.00655 188 ALA A N   
1450 C CA  . ALA A 188 ? 0.21123 0.19764 0.19927 0.00639  0.00451  -0.00722 188 ALA A CA  
1451 C C   . ALA A 188 ? 0.18502 0.17158 0.17190 0.00660  0.00623  -0.00818 188 ALA A C   
1452 O O   . ALA A 188 ? 0.21583 0.20089 0.19959 0.00558  0.00627  -0.00884 188 ALA A O   
1453 C CB  . ALA A 188 ? 0.18386 0.16667 0.16946 0.00545  0.00361  -0.00796 188 ALA A CB  
1454 N N   . ALA A 189 ? 0.16178 0.14991 0.15099 0.00802  0.00773  -0.00827 189 ALA A N   
1455 C CA  . ALA A 189 ? 0.15995 0.14813 0.14824 0.00821  0.00998  -0.00916 189 ALA A CA  
1456 C C   . ALA A 189 ? 0.20177 0.19214 0.18988 0.00669  0.01029  -0.00882 189 ALA A C   
1457 O O   . ALA A 189 ? 0.12458 0.11856 0.11604 0.00622  0.00942  -0.00798 189 ALA A O   
1458 C CB  . ALA A 189 ? 0.16374 0.15408 0.15595 0.01001  0.01161  -0.00931 189 ALA A CB  
1459 N N   . PRO A 190 ? 0.18485 0.17280 0.16883 0.00597  0.01147  -0.00946 190 PRO A N   
1460 C CA  . PRO A 190 ? 0.20713 0.19635 0.19043 0.00449  0.01183  -0.00899 190 PRO A CA  
1461 C C   . PRO A 190 ? 0.15466 0.14808 0.14269 0.00437  0.01367  -0.00873 190 PRO A C   
1462 O O   . PRO A 190 ? 0.13973 0.13543 0.12934 0.00307  0.01325  -0.00816 190 PRO A O   
1463 C CB  . PRO A 190 ? 0.23382 0.21865 0.21094 0.00433  0.01305  -0.00974 190 PRO A CB  
1464 C CG  . PRO A 190 ? 0.18601 0.16737 0.16041 0.00528  0.01195  -0.01069 190 PRO A CG  
1465 C CD  . PRO A 190 ? 0.21110 0.19448 0.19015 0.00652  0.01226  -0.01066 190 PRO A CD  
1466 N N   . ALA A 191 ? 0.19420 0.18882 0.18499 0.00568  0.01570  -0.00930 191 ALA A N   
1467 C CA  . ALA A 191 ? 0.16331 0.16234 0.15962 0.00556  0.01753  -0.00938 191 ALA A CA  
1468 C C   . ALA A 191 ? 0.15475 0.15851 0.15676 0.00569  0.01517  -0.00882 191 ALA A C   
1469 O O   . ALA A 191 ? 0.17520 0.18317 0.18232 0.00527  0.01599  -0.00905 191 ALA A O   
1470 C CB  . ALA A 191 ? 0.13710 0.13625 0.13531 0.00712  0.02039  -0.01032 191 ALA A CB  
1471 N N   . ALA A 192 ? 0.15956 0.16255 0.16072 0.00624  0.01233  -0.00819 192 ALA A N   
1472 C CA  . ALA A 192 ? 0.17470 0.18132 0.17990 0.00662  0.00994  -0.00756 192 ALA A CA  
1473 C C   . ALA A 192 ? 0.18400 0.18984 0.18674 0.00525  0.00759  -0.00675 192 ALA A C   
1474 O O   . ALA A 192 ? 0.15569 0.16391 0.16066 0.00553  0.00552  -0.00619 192 ALA A O   
1475 C CB  . ALA A 192 ? 0.19026 0.19659 0.19692 0.00890  0.00893  -0.00734 192 ALA A CB  
1476 N N   . THR A 193 ? 0.17691 0.17938 0.17497 0.00394  0.00779  -0.00673 193 THR A N   
1477 C CA  . THR A 193 ? 0.16494 0.16656 0.16093 0.00270  0.00577  -0.00611 193 THR A CA  
1478 C C   . THR A 193 ? 0.15221 0.15319 0.14614 0.00094  0.00645  -0.00621 193 THR A C   
1479 O O   . THR A 193 ? 0.13438 0.13380 0.12587 -0.00001 0.00506  -0.00589 193 THR A O   
1480 C CB  . THR A 193 ? 0.14166 0.13946 0.13428 0.00306  0.00469  -0.00599 193 THR A CB  
1481 O OG1 . THR A 193 ? 0.15570 0.15017 0.14497 0.00318  0.00600  -0.00680 193 THR A OG1 
1482 C CG2 . THR A 193 ? 0.17290 0.17082 0.16731 0.00472  0.00397  -0.00559 193 THR A CG2 
1483 N N   . GLY A 194 ? 0.16993 0.17187 0.16487 0.00052  0.00874  -0.00664 194 GLY A N   
1484 C CA  . GLY A 194 ? 0.09369 0.09443 0.08636 -0.00105 0.00969  -0.00656 194 GLY A CA  
1485 C C   . GLY A 194 ? 0.17688 0.18082 0.17275 -0.00235 0.00873  -0.00630 194 GLY A C   
1486 O O   . GLY A 194 ? 0.12972 0.13737 0.12996 -0.00200 0.00754  -0.00637 194 GLY A O   
1487 N N   . VAL A 195 ? 0.20664 0.20882 0.19996 -0.00376 0.00914  -0.00608 195 VAL A N   
1488 C CA  . VAL A 195 ? 0.17358 0.17819 0.16950 -0.00519 0.00846  -0.00600 195 VAL A CA  
1489 C C   . VAL A 195 ? 0.21460 0.22200 0.21486 -0.00594 0.01091  -0.00657 195 VAL A C   
1490 O O   . VAL A 195 ? 0.17927 0.18442 0.17761 -0.00643 0.01374  -0.00659 195 VAL A O   
1491 C CB  . VAL A 195 ? 0.15417 0.15551 0.14584 -0.00629 0.00798  -0.00554 195 VAL A CB  
1492 C CG1 . VAL A 195 ? 0.16453 0.16818 0.15899 -0.00776 0.00738  -0.00560 195 VAL A CG1 
1493 C CG2 . VAL A 195 ? 0.18261 0.18160 0.17100 -0.00558 0.00569  -0.00525 195 VAL A CG2 
1494 N N   . PRO A 196 ? 0.19003 0.20216 0.19611 -0.00602 0.00998  -0.00713 196 PRO A N   
1495 C CA  . PRO A 196 ? 0.19355 0.20900 0.20511 -0.00679 0.01226  -0.00802 196 PRO A CA  
1496 C C   . PRO A 196 ? 0.20932 0.22435 0.22125 -0.00901 0.01347  -0.00815 196 PRO A C   
1497 O O   . PRO A 196 ? 0.21110 0.22410 0.21982 -0.00982 0.01198  -0.00763 196 PRO A O   
1498 C CB  . PRO A 196 ? 0.21088 0.23152 0.22834 -0.00586 0.00989  -0.00872 196 PRO A CB  
1499 C CG  . PRO A 196 ? 0.23523 0.25496 0.24973 -0.00560 0.00655  -0.00805 196 PRO A CG  
1500 C CD  . PRO A 196 ? 0.18966 0.20422 0.19750 -0.00528 0.00675  -0.00706 196 PRO A CD  
1501 N N   . THR A 197 ? 0.25538 0.27228 0.27161 -0.01001 0.01645  -0.00893 197 THR A N   
1502 C CA  . THR A 197 ? 0.27722 0.29416 0.29523 -0.01229 0.01805  -0.00927 197 THR A CA  
1503 C C   . THR A 197 ? 0.21048 0.23336 0.23622 -0.01303 0.01618  -0.01068 197 THR A C   
1504 O O   . THR A 197 ? 0.27988 0.30677 0.30950 -0.01159 0.01394  -0.01132 197 THR A O   
1505 C CB  . THR A 197 ? 0.24550 0.26048 0.26362 -0.01318 0.02292  -0.00934 197 THR A CB  
1506 O OG1 . THR A 197 ? 0.34044 0.36040 0.36631 -0.01299 0.02447  -0.01068 197 THR A OG1 
1507 C CG2 . THR A 197 ? 0.31146 0.32094 0.32188 -0.01185 0.02440  -0.00823 197 THR A CG2 
1508 N N   . TRP A 198 ? 0.21799 0.24113 0.24574 -0.01521 0.01697  -0.01122 198 TRP A N   
1509 C CA  . TRP A 198 ? 0.23990 0.26851 0.27483 -0.01607 0.01490  -0.01287 198 TRP A CA  
1510 C C   . TRP A 198 ? 0.25804 0.29181 0.30159 -0.01622 0.01669  -0.01450 198 TRP A C   
1511 O O   . TRP A 198 ? 0.23900 0.27819 0.28910 -0.01615 0.01415  -0.01611 198 TRP A O   
1512 C CB  . TRP A 198 ? 0.29112 0.31834 0.32594 -0.01847 0.01523  -0.01322 198 TRP A CB  
1513 C CG  . TRP A 198 ? 0.22479 0.24956 0.26044 -0.02053 0.01994  -0.01323 198 TRP A CG  
1514 C CD1 . TRP A 198 ? 0.26082 0.27921 0.28954 -0.02108 0.02250  -0.01166 198 TRP A CD1 
1515 C CD2 . TRP A 198 ? 0.21479 0.24317 0.25861 -0.02228 0.02274  -0.01490 198 TRP A CD2 
1516 N NE1 . TRP A 198 ? 0.24210 0.25934 0.27341 -0.02303 0.02697  -0.01201 198 TRP A NE1 
1517 C CE2 . TRP A 198 ? 0.23747 0.26093 0.27844 -0.02395 0.02739  -0.01406 198 TRP A CE2 
1518 C CE3 . TRP A 198 ? 0.23349 0.26880 0.28696 -0.02253 0.02173  -0.01711 198 TRP A CE3 
1519 C CZ2 . TRP A 198 ? 0.26373 0.28878 0.31127 -0.02609 0.03154  -0.01529 198 TRP A CZ2 
1520 C CZ3 . TRP A 198 ? 0.24604 0.28357 0.30682 -0.02465 0.02551  -0.01859 198 TRP A CZ3 
1521 C CH2 . TRP A 198 ? 0.22533 0.25768 0.28320 -0.02653 0.03060  -0.01765 198 TRP A CH2 
1522 N N   . GLN A 199 ? 0.25671 0.28893 0.30045 -0.01631 0.02093  -0.01426 199 GLN A N   
1523 C CA  . GLN A 199 ? 0.24316 0.28042 0.29560 -0.01630 0.02299  -0.01588 199 GLN A CA  
1524 C C   . GLN A 199 ? 0.22638 0.26671 0.28075 -0.01345 0.02080  -0.01608 199 GLN A C   
1525 O O   . GLN A 199 ? 0.31041 0.35650 0.37337 -0.01297 0.02062  -0.01778 199 GLN A O   
1526 C CB  . GLN A 199 ? 0.25494 0.28901 0.30664 -0.01744 0.02892  -0.01555 199 GLN A CB  
1527 C CG  . GLN A 199 ? 0.32251 0.35258 0.37177 -0.02014 0.03180  -0.01511 199 GLN A CG  
1528 C CD  . GLN A 199 ? 0.34035 0.36248 0.37831 -0.01971 0.03299  -0.01283 199 GLN A CD  
1529 O OE1 . GLN A 199 ? 0.28096 0.30102 0.31290 -0.01777 0.03005  -0.01174 199 GLN A OE1 
1530 N NE2 . GLN A 199 ? 0.35260 0.37008 0.38767 -0.02147 0.03730  -0.01216 199 GLN A NE2 
1531 N N   . GLU A 200 ? 0.25997 0.29659 0.30692 -0.01154 0.01914  -0.01449 200 GLU A N   
1532 C CA  . GLU A 200 ? 0.30637 0.34489 0.35441 -0.00879 0.01745  -0.01448 200 GLU A CA  
1533 C C   . GLU A 200 ? 0.31273 0.35491 0.36302 -0.00741 0.01232  -0.01489 200 GLU A C   
1534 O O   . GLU A 200 ? 0.32591 0.37074 0.37904 -0.00509 0.01072  -0.01520 200 GLU A O   
1535 C CB  . GLU A 200 ? 0.26726 0.29992 0.30657 -0.00745 0.01808  -0.01278 200 GLU A CB  
1536 C CG  . GLU A 200 ? 0.33061 0.35894 0.36627 -0.00836 0.02289  -0.01232 200 GLU A CG  
1537 C CD  . GLU A 200 ? 0.29651 0.31879 0.32295 -0.00718 0.02282  -0.01087 200 GLU A CD  
1538 O OE1 . GLU A 200 ? 0.29922 0.32007 0.32173 -0.00647 0.01930  -0.01008 200 GLU A OE1 
1539 O OE2 . GLU A 200 ? 0.37102 0.38989 0.39418 -0.00697 0.02635  -0.01065 200 GLU A OE2 
1540 N N   . VAL A 201 ? 0.27949 0.32146 0.32811 -0.00861 0.00976  -0.01486 201 VAL A N   
1541 C CA  . VAL A 201 ? 0.29073 0.33562 0.34055 -0.00729 0.00500  -0.01525 201 VAL A CA  
1542 C C   . VAL A 201 ? 0.30908 0.36028 0.36780 -0.00799 0.00352  -0.01752 201 VAL A C   
1543 O O   . VAL A 201 ? 0.34503 0.39881 0.40477 -0.00686 -0.00069 -0.01810 201 VAL A O   
1544 C CB  . VAL A 201 ? 0.30306 0.34413 0.34580 -0.00794 0.00287  -0.01409 201 VAL A CB  
1545 C CG1 . VAL A 201 ? 0.24516 0.28059 0.28002 -0.00704 0.00377  -0.01214 201 VAL A CG1 
1546 C CG2 . VAL A 201 ? 0.24759 0.28787 0.29081 -0.01082 0.00431  -0.01469 201 VAL A CG2 
1547 N N   . GLY A 202 ? 0.28908 0.34269 0.35419 -0.00982 0.00684  -0.01892 202 GLY A N   
1548 C CA  . GLY A 202 ? 0.30756 0.36773 0.38259 -0.01059 0.00568  -0.02148 202 GLY A CA  
1549 C C   . GLY A 202 ? 0.33043 0.39096 0.40814 -0.01391 0.00694  -0.02272 202 GLY A C   
1550 O O   . GLY A 202 ? 0.40593 0.47166 0.49306 -0.01518 0.00756  -0.02508 202 GLY A O   
1551 N N   . PHE A 203 ? 0.29335 0.34860 0.36363 -0.01535 0.00738  -0.02134 203 PHE A N   
1552 C CA  . PHE A 203 ? 0.29527 0.35029 0.36775 -0.01844 0.00857  -0.02247 203 PHE A CA  
1553 C C   . PHE A 203 ? 0.26196 0.31755 0.34015 -0.02060 0.01396  -0.02331 203 PHE A C   
1554 O O   . PHE A 203 ? 0.26573 0.31777 0.34054 -0.02032 0.01789  -0.02184 203 PHE A O   
1555 C CB  . PHE A 203 ? 0.28577 0.33434 0.34879 -0.01928 0.00861  -0.02058 203 PHE A CB  
1556 C CG  . PHE A 203 ? 0.20783 0.25617 0.26651 -0.01798 0.00371  -0.02029 203 PHE A CG  
1557 C CD1 . PHE A 203 ? 0.19519 0.24757 0.25828 -0.01850 0.00028  -0.02237 203 PHE A CD1 
1558 C CD2 . PHE A 203 ? 0.20249 0.24643 0.25270 -0.01629 0.00266  -0.01809 203 PHE A CD2 
1559 C CE1 . PHE A 203 ? 0.16461 0.21627 0.22297 -0.01722 -0.00390 -0.02208 203 PHE A CE1 
1560 C CE2 . PHE A 203 ? 0.21505 0.25849 0.26127 -0.01519 -0.00128 -0.01779 203 PHE A CE2 
1561 C CZ  . PHE A 203 ? 0.22167 0.26876 0.27156 -0.01559 -0.00445 -0.01970 203 PHE A CZ  
1562 N N   . LYS A 204 ? 0.25668 0.31651 0.34343 -0.02282 0.01424  -0.02579 204 LYS A N   
1563 C CA  . LYS A 204 ? 0.31034 0.37167 0.40445 -0.02507 0.01944  -0.02704 204 LYS A CA  
1564 C C   . LYS A 204 ? 0.29132 0.34819 0.38359 -0.02839 0.02304  -0.02680 204 LYS A C   
1565 O O   . LYS A 204 ? 0.37668 0.43169 0.47096 -0.03008 0.02863  -0.02665 204 LYS A O   
1566 C CB  . LYS A 204 ? 0.26865 0.33856 0.37564 -0.02532 0.01766  -0.03040 204 LYS A CB  
1567 C CG  . LYS A 204 ? 0.30365 0.37798 0.41153 -0.02238 0.01105  -0.03118 204 LYS A CG  
1568 C CD  . LYS A 204 ? 0.28812 0.37110 0.40892 -0.02208 0.00913  -0.03452 204 LYS A CD  
1569 C CE  . LYS A 204 ? 0.28066 0.36620 0.40685 -0.02067 0.01240  -0.03461 204 LYS A CE  
1570 N NZ  . LYS A 204 ? 0.26112 0.35555 0.40111 -0.02039 0.01068  -0.03811 204 LYS A NZ  
1571 N N   . GLU A 205 ? 0.28821 0.34303 0.37658 -0.02930 0.02021  -0.02675 205 GLU A N   
1572 C CA  . GLU A 205 ? 0.29342 0.34340 0.37929 -0.03220 0.02318  -0.02639 205 GLU A CA  
1573 C C   . GLU A 205 ? 0.26327 0.30549 0.33672 -0.03126 0.02335  -0.02329 205 GLU A C   
1574 O O   . GLU A 205 ? 0.21643 0.25809 0.28429 -0.02903 0.01925  -0.02228 205 GLU A O   
1575 C CB  . GLU A 205 ? 0.28406 0.33721 0.37491 -0.03397 0.01989  -0.02889 205 GLU A CB  
1576 C CG  . GLU A 205 ? 0.27964 0.33139 0.37528 -0.03771 0.02398  -0.03019 205 GLU A CG  
1577 C CD  . GLU A 205 ? 0.27906 0.33719 0.38485 -0.03945 0.02109  -0.03395 205 GLU A CD  
1578 O OE1 . GLU A 205 ? 0.27720 0.34254 0.39113 -0.03836 0.01860  -0.03611 205 GLU A OE1 
1579 O OE2 . GLU A 205 ? 0.28017 0.33606 0.38580 -0.04179 0.02112  -0.03486 205 GLU A OE2 
1580 N N   . PRO A 206 ? 0.26867 0.30471 0.33761 -0.03278 0.02802  -0.02175 206 PRO A N   
1581 C CA  . PRO A 206 ? 0.19420 0.22297 0.25157 -0.03155 0.02813  -0.01886 206 PRO A CA  
1582 C C   . PRO A 206 ? 0.15793 0.18471 0.21125 -0.03185 0.02458  -0.01874 206 PRO A C   
1583 O O   . PRO A 206 ? 0.22158 0.25088 0.28017 -0.03373 0.02343  -0.02073 206 PRO A O   
1584 C CB  . PRO A 206 ? 0.19282 0.21581 0.24754 -0.03322 0.03424  -0.01761 206 PRO A CB  
1585 C CG  . PRO A 206 ? 0.21135 0.23766 0.27579 -0.03624 0.03674  -0.01997 206 PRO A CG  
1586 C CD  . PRO A 206 ? 0.31219 0.34739 0.38644 -0.03564 0.03359  -0.02258 206 PRO A CD  
1587 N N   . PRO A 207 ? 0.15315 0.17549 0.19743 -0.03005 0.02281  -0.01663 207 PRO A N   
1588 C CA  . PRO A 207 ? 0.15071 0.17064 0.19092 -0.03031 0.02001  -0.01644 207 PRO A CA  
1589 C C   . PRO A 207 ? 0.18467 0.19906 0.22252 -0.03245 0.02328  -0.01586 207 PRO A C   
1590 O O   . PRO A 207 ? 0.23142 0.24147 0.26650 -0.03290 0.02749  -0.01447 207 PRO A O   
1591 C CB  . PRO A 207 ? 0.14797 0.16496 0.18004 -0.02767 0.01779  -0.01438 207 PRO A CB  
1592 C CG  . PRO A 207 ? 0.13622 0.15098 0.16575 -0.02671 0.02093  -0.01298 207 PRO A CG  
1593 C CD  . PRO A 207 ? 0.16602 0.18560 0.20388 -0.02765 0.02317  -0.01459 207 PRO A CD  
1594 N N   . LEU A 208 ? 0.12486 0.13899 0.16335 -0.03367 0.02135  -0.01690 208 LEU A N   
1595 C CA  . LEU A 208 ? 0.18127 0.19010 0.21796 -0.03572 0.02416  -0.01654 208 LEU A CA  
1596 C C   . LEU A 208 ? 0.13766 0.14146 0.16673 -0.03477 0.02222  -0.01514 208 LEU A C   
1597 O O   . LEU A 208 ? 0.10431 0.10256 0.13040 -0.03594 0.02464  -0.01432 208 LEU A O   
1598 C CB  . LEU A 208 ? 0.11504 0.12737 0.16022 -0.03855 0.02443  -0.01938 208 LEU A CB  
1599 C CG  . LEU A 208 ? 0.21578 0.23270 0.27010 -0.04023 0.02728  -0.02114 208 LEU A CG  
1600 C CD1 . LEU A 208 ? 0.22567 0.24548 0.28823 -0.04321 0.02731  -0.02415 208 LEU A CD1 
1601 C CD2 . LEU A 208 ? 0.18967 0.20167 0.24133 -0.04074 0.03303  -0.01919 208 LEU A CD2 
1602 N N   . THR A 209 ? 0.13675 0.14212 0.16275 -0.03267 0.01816  -0.01486 209 THR A N   
1603 C CA  . THR A 209 ? 0.11082 0.11215 0.13082 -0.03185 0.01629  -0.01392 209 THR A CA  
1604 C C   . THR A 209 ? 0.14950 0.14416 0.16219 -0.03080 0.01848  -0.01135 209 THR A C   
1605 O O   . THR A 209 ? 0.16185 0.15544 0.17247 -0.02984 0.02027  -0.01007 209 THR A O   
1606 C CB  . THR A 209 ? 0.11918 0.12361 0.13766 -0.02983 0.01200  -0.01411 209 THR A CB  
1607 O OG1 . THR A 209 ? 0.14238 0.14321 0.15598 -0.02922 0.01050  -0.01349 209 THR A OG1 
1608 C CG2 . THR A 209 ? 0.09973 0.10472 0.11552 -0.02764 0.01172  -0.01262 209 THR A CG2 
1609 N N   . VAL A 210 ? 0.10783 0.09778 0.11643 -0.03084 0.01821  -0.01069 210 VAL A N   
1610 C CA  . VAL A 210 ? 0.11738 0.10056 0.11885 -0.02970 0.01985  -0.00838 210 VAL A CA  
1611 C C   . VAL A 210 ? 0.13748 0.11966 0.13373 -0.02711 0.01673  -0.00728 210 VAL A C   
1612 O O   . VAL A 210 ? 0.20996 0.18686 0.20021 -0.02576 0.01727  -0.00553 210 VAL A O   
1613 C CB  . VAL A 210 ? 0.11997 0.09785 0.12012 -0.03116 0.02182  -0.00819 210 VAL A CB  
1614 C CG1 . VAL A 210 ? 0.13269 0.11104 0.13823 -0.03396 0.02551  -0.00927 210 VAL A CG1 
1615 C CG2 . VAL A 210 ? 0.11860 0.09746 0.11964 -0.03128 0.01884  -0.00945 210 VAL A CG2 
1616 N N   . PHE A 211 ? 0.12498 0.11192 0.12335 -0.02634 0.01349  -0.00830 211 PHE A N   
1617 C CA  . PHE A 211 ? 0.16384 0.15024 0.15827 -0.02415 0.01075  -0.00750 211 PHE A CA  
1618 C C   . PHE A 211 ? 0.15586 0.14468 0.14984 -0.02270 0.01018  -0.00695 211 PHE A C   
1619 O O   . PHE A 211 ? 0.19338 0.18708 0.19155 -0.02298 0.00954  -0.00797 211 PHE A O   
1620 C CB  . PHE A 211 ? 0.15175 0.14093 0.14807 -0.02422 0.00797  -0.00885 211 PHE A CB  
1621 C CG  . PHE A 211 ? 0.13594 0.12353 0.13374 -0.02590 0.00854  -0.00993 211 PHE A CG  
1622 C CD1 . PHE A 211 ? 0.12115 0.10345 0.11533 -0.02562 0.00919  -0.00905 211 PHE A CD1 
1623 C CD2 . PHE A 211 ? 0.15770 0.14903 0.16062 -0.02767 0.00824  -0.01196 211 PHE A CD2 
1624 C CE1 . PHE A 211 ? 0.11818 0.09870 0.11375 -0.02715 0.00984  -0.01011 211 PHE A CE1 
1625 C CE2 . PHE A 211 ? 0.10561 0.09535 0.11000 -0.02933 0.00873  -0.01320 211 PHE A CE2 
1626 C CZ  . PHE A 211 ? 0.10544 0.08964 0.10612 -0.02911 0.00968  -0.01224 211 PHE A CZ  
1627 N N   . LYS A 212 ? 0.18047 0.16578 0.16936 -0.02104 0.01025  -0.00545 212 LYS A N   
1628 C CA  . LYS A 212 ? 0.17174 0.15854 0.15966 -0.01964 0.00988  -0.00498 212 LYS A CA  
1629 C C   . LYS A 212 ? 0.11645 0.10523 0.10385 -0.01816 0.00673  -0.00514 212 LYS A C   
1630 O O   . LYS A 212 ? 0.14883 0.13587 0.13436 -0.01763 0.00520  -0.00502 212 LYS A O   
1631 C CB  . LYS A 212 ? 0.20719 0.18891 0.18956 -0.01860 0.01161  -0.00349 212 LYS A CB  
1632 C CG  . LYS A 212 ? 0.27831 0.25565 0.25897 -0.01982 0.01494  -0.00282 212 LYS A CG  
1633 C CD  . LYS A 212 ? 0.25035 0.23070 0.23674 -0.02200 0.01761  -0.00383 212 LYS A CD  
1634 C CE  . LYS A 212 ? 0.26054 0.24509 0.24993 -0.02165 0.01813  -0.00433 212 LYS A CE  
1635 N NZ  . LYS A 212 ? 0.40996 0.39126 0.39380 -0.01988 0.01898  -0.00306 212 LYS A NZ  
1636 N N   . GLY A 213 ? 0.10153 0.09380 0.09078 -0.01748 0.00601  -0.00543 213 GLY A N   
1637 C CA  . GLY A 213 ? 0.10841 0.10232 0.09730 -0.01620 0.00350  -0.00551 213 GLY A CA  
1638 C C   . GLY A 213 ? 0.12054 0.11152 0.10529 -0.01459 0.00290  -0.00462 213 GLY A C   
1639 O O   . GLY A 213 ? 0.09267 0.08042 0.07425 -0.01419 0.00425  -0.00391 213 GLY A O   
1640 N N   . GLY A 214 ? 0.09702 0.08899 0.08169 -0.01366 0.00084  -0.00478 214 GLY A N   
1641 C CA  . GLY A 214 ? 0.08601 0.07583 0.06774 -0.01221 -0.00012 -0.00434 214 GLY A CA  
1642 C C   . GLY A 214 ? 0.11214 0.10033 0.09282 -0.01172 -0.00174 -0.00444 214 GLY A C   
1643 O O   . GLY A 214 ? 0.10853 0.09575 0.08939 -0.01237 -0.00165 -0.00456 214 GLY A O   
1644 N N   . GLU A 215 ? 0.09825 0.08618 0.07826 -0.01058 -0.00314 -0.00455 215 GLU A N   
1645 C CA  . GLU A 215 ? 0.11497 0.10174 0.09486 -0.01001 -0.00468 -0.00487 215 GLU A CA  
1646 C C   . GLU A 215 ? 0.11093 0.09390 0.08772 -0.00943 -0.00489 -0.00450 215 GLU A C   
1647 O O   . GLU A 215 ? 0.11840 0.10041 0.09561 -0.00931 -0.00566 -0.00472 215 GLU A O   
1648 C CB  . GLU A 215 ? 0.12233 0.10967 0.10274 -0.00904 -0.00597 -0.00527 215 GLU A CB  
1649 C CG  . GLU A 215 ? 0.10703 0.09355 0.08824 -0.00840 -0.00757 -0.00587 215 GLU A CG  
1650 C CD  . GLU A 215 ? 0.11811 0.10499 0.10020 -0.00761 -0.00872 -0.00649 215 GLU A CD  
1651 O OE1 . GLU A 215 ? 0.09671 0.08365 0.07776 -0.00736 -0.00838 -0.00635 215 GLU A OE1 
1652 O OE2 . GLU A 215 ? 0.08285 0.06997 0.06704 -0.00729 -0.00986 -0.00725 215 GLU A OE2 
1653 N N   . THR A 216 ? 0.10184 0.08229 0.07519 -0.00892 -0.00414 -0.00390 216 THR A N   
1654 C CA  . THR A 216 ? 0.12901 0.10502 0.09823 -0.00806 -0.00434 -0.00332 216 THR A CA  
1655 C C   . THR A 216 ? 0.13054 0.10528 0.10004 -0.00907 -0.00312 -0.00294 216 THR A C   
1656 O O   . THR A 216 ? 0.12680 0.09893 0.09492 -0.00835 -0.00410 -0.00281 216 THR A O   
1657 C CB  . THR A 216 ? 0.13763 0.11084 0.10244 -0.00744 -0.00313 -0.00265 216 THR A CB  
1658 O OG1 . THR A 216 ? 0.16359 0.13739 0.12777 -0.00634 -0.00456 -0.00321 216 THR A OG1 
1659 C CG2 . THR A 216 ? 0.12705 0.09482 0.08650 -0.00644 -0.00307 -0.00178 216 THR A CG2 
1660 N N   . GLU A 217 ? 0.11691 0.09347 0.08849 -0.01070 -0.00106 -0.00291 217 GLU A N   
1661 C CA  . GLU A 217 ? 0.11467 0.09022 0.08714 -0.01196 0.00019  -0.00285 217 GLU A CA  
1662 C C   . GLU A 217 ? 0.11677 0.09412 0.09215 -0.01220 -0.00125 -0.00369 217 GLU A C   
1663 O O   . GLU A 217 ? 0.15388 0.12888 0.12875 -0.01235 -0.00113 -0.00366 217 GLU A O   
1664 C CB  . GLU A 217 ? 0.12077 0.09855 0.09577 -0.01373 0.00246  -0.00304 217 GLU A CB  
1665 C CG  . GLU A 217 ? 0.17309 0.14843 0.14531 -0.01377 0.00477  -0.00219 217 GLU A CG  
1666 C CD  . GLU A 217 ? 0.17447 0.14395 0.14212 -0.01350 0.00609  -0.00112 217 GLU A CD  
1667 O OE1 . GLU A 217 ? 0.21198 0.18019 0.18057 -0.01438 0.00648  -0.00121 217 GLU A OE1 
1668 O OE2 . GLU A 217 ? 0.27358 0.23933 0.23628 -0.01230 0.00674  -0.00018 217 GLU A OE2 
1669 N N   . ALA A 218 ? 0.12025 0.10138 0.09847 -0.01217 -0.00238 -0.00443 218 ALA A N   
1670 C CA  . ALA A 218 ? 0.11123 0.09382 0.09182 -0.01233 -0.00339 -0.00525 218 ALA A CA  
1671 C C   . ALA A 218 ? 0.13500 0.11501 0.11442 -0.01097 -0.00475 -0.00524 218 ALA A C   
1672 O O   . ALA A 218 ? 0.15133 0.13063 0.13175 -0.01113 -0.00488 -0.00570 218 ALA A O   
1673 C CB  . ALA A 218 ? 0.10176 0.08804 0.08468 -0.01232 -0.00409 -0.00578 218 ALA A CB  
1674 N N   . LEU A 219 ? 0.13556 0.11417 0.11302 -0.00953 -0.00591 -0.00491 219 LEU A N   
1675 C CA  . LEU A 219 ? 0.09947 0.07585 0.07615 -0.00797 -0.00768 -0.00509 219 LEU A CA  
1676 C C   . LEU A 219 ? 0.12708 0.09898 0.10042 -0.00747 -0.00728 -0.00428 219 LEU A C   
1677 O O   . LEU A 219 ? 0.12671 0.09696 0.10034 -0.00648 -0.00842 -0.00454 219 LEU A O   
1678 C CB  . LEU A 219 ? 0.10630 0.08252 0.08184 -0.00654 -0.00937 -0.00523 219 LEU A CB  
1679 C CG  . LEU A 219 ? 0.14777 0.12775 0.12664 -0.00687 -0.00979 -0.00603 219 LEU A CG  
1680 C CD1 . LEU A 219 ? 0.16012 0.13944 0.13759 -0.00562 -0.01133 -0.00630 219 LEU A CD1 
1681 C CD2 . LEU A 219 ? 0.11675 0.09880 0.09975 -0.00703 -0.01031 -0.00700 219 LEU A CD2 
1682 N N   . ALA A 220 ? 0.14659 0.11628 0.11686 -0.00809 -0.00549 -0.00330 220 ALA A N   
1683 C CA  . ALA A 220 ? 0.12202 0.08667 0.08857 -0.00768 -0.00465 -0.00232 220 ALA A CA  
1684 C C   . ALA A 220 ? 0.12264 0.08721 0.09157 -0.00903 -0.00347 -0.00268 220 ALA A C   
1685 O O   . ALA A 220 ? 0.12174 0.08266 0.08907 -0.00819 -0.00377 -0.00234 220 ALA A O   
1686 C CB  . ALA A 220 ? 0.11095 0.07299 0.07360 -0.00813 -0.00249 -0.00118 220 ALA A CB  
1687 N N   . ARG A 221 ? 0.13582 0.10417 0.10838 -0.01099 -0.00226 -0.00345 221 ARG A N   
1688 C CA  . ARG A 221 ? 0.12835 0.09694 0.10331 -0.01229 -0.00145 -0.00420 221 ARG A CA  
1689 C C   . ARG A 221 ? 0.11609 0.08539 0.09297 -0.01128 -0.00315 -0.00508 221 ARG A C   
1690 O O   . ARG A 221 ? 0.12227 0.08955 0.09955 -0.01144 -0.00279 -0.00542 221 ARG A O   
1691 C CB  . ARG A 221 ? 0.13620 0.10902 0.11451 -0.01431 -0.00040 -0.00511 221 ARG A CB  
1692 C CG  . ARG A 221 ? 0.17765 0.15045 0.15554 -0.01558 0.00158  -0.00461 221 ARG A CG  
1693 C CD  . ARG A 221 ? 0.19317 0.16917 0.17487 -0.01767 0.00248  -0.00585 221 ARG A CD  
1694 N NE  . ARG A 221 ? 0.25877 0.23234 0.24095 -0.01865 0.00326  -0.00641 221 ARG A NE  
1695 C CZ  . ARG A 221 ? 0.25356 0.22428 0.23543 -0.01998 0.00544  -0.00615 221 ARG A CZ  
1696 N NH1 . ARG A 221 ? 0.29086 0.26089 0.27199 -0.02053 0.00727  -0.00533 221 ARG A NH1 
1697 N NH2 . ARG A 221 ? 0.29550 0.26380 0.27791 -0.02082 0.00604  -0.00679 221 ARG A NH2 
1698 N N   . LEU A 222 ? 0.14909 0.12117 0.12748 -0.01031 -0.00478 -0.00555 222 LEU A N   
1699 C CA  . LEU A 222 ? 0.13562 0.10857 0.11644 -0.00934 -0.00609 -0.00648 222 LEU A CA  
1700 C C   . LEU A 222 ? 0.12010 0.08906 0.09912 -0.00746 -0.00729 -0.00606 222 LEU A C   
1701 O O   . LEU A 222 ? 0.15757 0.12540 0.13797 -0.00711 -0.00733 -0.00664 222 LEU A O   
1702 C CB  . LEU A 222 ? 0.10820 0.08462 0.09115 -0.00881 -0.00727 -0.00702 222 LEU A CB  
1703 C CG  . LEU A 222 ? 0.14388 0.12171 0.13017 -0.00792 -0.00830 -0.00812 222 LEU A CG  
1704 C CD1 . LEU A 222 ? 0.15808 0.13736 0.14652 -0.00914 -0.00696 -0.00903 222 LEU A CD1 
1705 C CD2 . LEU A 222 ? 0.19052 0.17102 0.17868 -0.00743 -0.00929 -0.00851 222 LEU A CD2 
1706 N N   . GLU A 223 ? 0.14431 0.11087 0.11998 -0.00603 -0.00836 -0.00512 223 GLU A N   
1707 C CA  . GLU A 223 ? 0.14808 0.11047 0.12130 -0.00384 -0.00993 -0.00463 223 GLU A CA  
1708 C C   . GLU A 223 ? 0.19790 0.15571 0.16849 -0.00417 -0.00832 -0.00376 223 GLU A C   
1709 O O   . GLU A 223 ? 0.23986 0.19480 0.21012 -0.00266 -0.00929 -0.00376 223 GLU A O   
1710 C CB  . GLU A 223 ? 0.18153 0.14191 0.15066 -0.00220 -0.01146 -0.00383 223 GLU A CB  
1711 C CG  . GLU A 223 ? 0.18779 0.15212 0.15954 -0.00172 -0.01327 -0.00485 223 GLU A CG  
1712 C CD  . GLU A 223 ? 0.21391 0.17964 0.18942 -0.00005 -0.01583 -0.00615 223 GLU A CD  
1713 O OE1 . GLU A 223 ? 0.37161 0.33481 0.34698 0.00123  -0.01661 -0.00612 223 GLU A OE1 
1714 O OE2 . GLU A 223 ? 0.18726 0.15658 0.16620 -0.00002 -0.01696 -0.00726 223 GLU A OE2 
1715 N N   . ALA A 224 ? 0.16700 0.12404 0.13610 -0.00613 -0.00582 -0.00311 224 ALA A N   
1716 C CA  . ALA A 224 ? 0.21562 0.16814 0.18263 -0.00681 -0.00389 -0.00239 224 ALA A CA  
1717 C C   . ALA A 224 ? 0.17741 0.13091 0.14819 -0.00759 -0.00354 -0.00365 224 ALA A C   
1718 O O   . ALA A 224 ? 0.20655 0.15575 0.17600 -0.00692 -0.00317 -0.00331 224 ALA A O   
1719 C CB  . ALA A 224 ? 0.20874 0.16096 0.17457 -0.00903 -0.00110 -0.00177 224 ALA A CB  
1720 N N   . ALA A 225 ? 0.15243 0.11114 0.12751 -0.00886 -0.00359 -0.00511 225 ALA A N   
1721 C CA  . ALA A 225 ? 0.22015 0.17965 0.19828 -0.00951 -0.00318 -0.00647 225 ALA A CA  
1722 C C   . ALA A 225 ? 0.22001 0.17872 0.19945 -0.00724 -0.00496 -0.00695 225 ALA A C   
1723 O O   . ALA A 225 ? 0.23491 0.19209 0.21569 -0.00715 -0.00449 -0.00773 225 ALA A O   
1724 C CB  . ALA A 225 ? 0.19489 0.15967 0.17630 -0.01124 -0.00276 -0.00781 225 ALA A CB  
1725 N N   . PHE A 226 ? 0.22608 0.18590 0.20554 -0.00540 -0.00704 -0.00671 226 PHE A N   
1726 C CA  . PHE A 226 ? 0.22068 0.18044 0.20235 -0.00313 -0.00903 -0.00740 226 PHE A CA  
1727 C C   . PHE A 226 ? 0.25909 0.21357 0.23716 -0.00069 -0.01050 -0.00623 226 PHE A C   
1728 O O   . PHE A 226 ? 0.25396 0.20838 0.23389 0.00161  -0.01271 -0.00681 226 PHE A O   
1729 C CB  . PHE A 226 ? 0.25278 0.21701 0.23736 -0.00253 -0.01066 -0.00816 226 PHE A CB  
1730 C CG  . PHE A 226 ? 0.20074 0.16953 0.18965 -0.00401 -0.00953 -0.00958 226 PHE A CG  
1731 C CD1 . PHE A 226 ? 0.20395 0.17500 0.19241 -0.00619 -0.00793 -0.00953 226 PHE A CD1 
1732 C CD2 . PHE A 226 ? 0.19873 0.16934 0.19204 -0.00310 -0.01001 -0.01096 226 PHE A CD2 
1733 C CE1 . PHE A 226 ? 0.16418 0.13871 0.15557 -0.00730 -0.00695 -0.01067 226 PHE A CE1 
1734 C CE2 . PHE A 226 ? 0.16272 0.13683 0.15920 -0.00441 -0.00858 -0.01213 226 PHE A CE2 
1735 C CZ  . PHE A 226 ? 0.15855 0.13435 0.15359 -0.00644 -0.00711 -0.01190 226 PHE A CZ  
1736 N N   . GLN A 227 ? 0.28467 0.23458 0.25765 -0.00105 -0.00929 -0.00463 227 GLN A N   
1737 C CA  . GLN A 227 ? 0.28114 0.22495 0.24967 0.00138  -0.01039 -0.00329 227 GLN A CA  
1738 C C   . GLN A 227 ? 0.25611 0.19726 0.22627 0.00223  -0.01018 -0.00379 227 GLN A C   
1739 O O   . GLN A 227 ? 0.22820 0.16560 0.19660 0.00506  -0.01213 -0.00326 227 GLN A O   
1740 C CB  . GLN A 227 ? 0.29875 0.23776 0.26122 0.00053  -0.00837 -0.00138 227 GLN A CB  
1741 C CG  . GLN A 227 ? 0.35322 0.29379 0.31316 0.00021  -0.00857 -0.00073 227 GLN A CG  
1742 C CD  . GLN A 227 ? 0.38024 0.31868 0.33649 0.00332  -0.01170 -0.00012 227 GLN A CD  
1743 O OE1 . GLN A 227 ? 0.44930 0.38904 0.40361 0.00342  -0.01233 0.00010  227 GLN A OE1 
1744 N NE2 . GLN A 227 ? 0.28957 0.22463 0.24482 0.00599  -0.01384 0.00002  227 GLN A NE2 
1745 N N   . ASP A 228 ? 0.19860 0.20136 0.22269 -0.00703 -0.03502 0.02311  228 ASP A N   
1746 C CA  . ASP A 228 ? 0.19922 0.20134 0.23162 -0.00381 -0.03712 0.02359  228 ASP A CA  
1747 C C   . ASP A 228 ? 0.14198 0.14568 0.17935 -0.00055 -0.03399 0.02008  228 ASP A C   
1748 O O   . ASP A 228 ? 0.12313 0.12548 0.15935 0.00144  -0.03048 0.01730  228 ASP A O   
1749 C CB  . ASP A 228 ? 0.16973 0.16837 0.20157 -0.00277 -0.03738 0.02398  228 ASP A CB  
1750 C CG  . ASP A 228 ? 0.12999 0.12759 0.17056 -0.00000 -0.04012 0.02488  228 ASP A CG  
1751 O OD1 . ASP A 228 ? 0.18462 0.18431 0.23184 0.00086  -0.04240 0.02571  228 ASP A OD1 
1752 O OD2 . ASP A 228 ? 0.21057 0.20534 0.25179 0.00131  -0.03999 0.02463  228 ASP A OD2 
1753 N N   . PRO A 229 ? 0.17239 0.17907 0.21520 -0.00011 -0.03511 0.02008  229 PRO A N   
1754 C CA  . PRO A 229 ? 0.15356 0.16196 0.20071 0.00255  -0.03176 0.01653  229 PRO A CA  
1755 C C   . PRO A 229 ? 0.13750 0.14458 0.19097 0.00609  -0.03103 0.01473  229 PRO A C   
1756 O O   . PRO A 229 ? 0.09908 0.10648 0.15305 0.00791  -0.02716 0.01132  229 PRO A O   
1757 C CB  . PRO A 229 ? 0.15664 0.16874 0.20890 0.00183  -0.03392 0.01743  229 PRO A CB  
1758 C CG  . PRO A 229 ? 0.16287 0.17471 0.21661 0.00008  -0.03937 0.02170  229 PRO A CG  
1759 C CD  . PRO A 229 ? 0.19955 0.20841 0.24451 -0.00233 -0.03943 0.02328  229 PRO A CD  
1760 N N   . LYS A 230 ? 0.13887 0.14436 0.19710 0.00690  -0.03461 0.01689  230 LYS A N   
1761 C CA  . LYS A 230 ? 0.13470 0.13871 0.19912 0.01011  -0.03377 0.01487  230 LYS A CA  
1762 C C   . LYS A 230 ? 0.12166 0.12298 0.18006 0.01064  -0.03034 0.01278  230 LYS A C   
1763 O O   . LYS A 230 ? 0.07355 0.07462 0.13469 0.01295  -0.02749 0.00952  230 LYS A O   
1764 C CB  . LYS A 230 ? 0.14893 0.15131 0.21966 0.01068  -0.03855 0.01791  230 LYS A CB  
1765 C CG  . LYS A 230 ? 0.20124 0.20638 0.28085 0.01115  -0.04213 0.01956  230 LYS A CG  
1766 C CD  . LYS A 230 ? 0.25571 0.25812 0.33987 0.01150  -0.04494 0.02134  230 LYS A CD  
1767 C CE  . LYS A 230 ? 0.23772 0.24202 0.32735 0.01070  -0.04806 0.02333  230 LYS A CE  
1768 N NZ  . LYS A 230 ? 0.24085 0.24205 0.33384 0.01046  -0.05083 0.02540  230 LYS A NZ  
1769 N N   . TRP A 231 ? 0.09152 0.09101 0.14181 0.00834  -0.03055 0.01449  231 TRP A N   
1770 C CA  . TRP A 231 ? 0.09834 0.09564 0.14314 0.00875  -0.02747 0.01259  231 TRP A CA  
1771 C C   . TRP A 231 ? 0.08948 0.08820 0.13134 0.00939  -0.02305 0.00935  231 TRP A C   
1772 O O   . TRP A 231 ? 0.09112 0.08882 0.13230 0.01102  -0.02033 0.00680  231 TRP A O   
1773 C CB  . TRP A 231 ? 0.10843 0.10396 0.14573 0.00596  -0.02849 0.01492  231 TRP A CB  
1774 C CG  . TRP A 231 ? 0.10793 0.10157 0.13998 0.00631  -0.02551 0.01304  231 TRP A CG  
1775 C CD1 . TRP A 231 ? 0.10448 0.09563 0.13711 0.00737  -0.02569 0.01271  231 TRP A CD1 
1776 C CD2 . TRP A 231 ? 0.09486 0.08899 0.12080 0.00561  -0.02208 0.01127  231 TRP A CD2 
1777 N NE1 . TRP A 231 ? 0.15358 0.14396 0.18080 0.00733  -0.02270 0.01089  231 TRP A NE1 
1778 C CE2 . TRP A 231 ? 0.11582 0.10793 0.13908 0.00635  -0.02053 0.01007  231 TRP A CE2 
1779 C CE3 . TRP A 231 ? 0.09684 0.09286 0.11966 0.00440  -0.02024 0.01060  231 TRP A CE3 
1780 C CZ2 . TRP A 231 ? 0.13534 0.12733 0.15330 0.00607  -0.01748 0.00842  231 TRP A CZ2 
1781 C CZ3 . TRP A 231 ? 0.10942 0.10498 0.12699 0.00415  -0.01705 0.00891  231 TRP A CZ3 
1782 C CH2 . TRP A 231 ? 0.09679 0.09041 0.11216 0.00505  -0.01582 0.00793  231 TRP A CH2 
1783 N N   . VAL A 232 ? 0.07549 0.07649 0.11540 0.00793  -0.02240 0.00950  232 VAL A N   
1784 C CA  . VAL A 232 ? 0.09321 0.09535 0.13049 0.00832  -0.01840 0.00675  232 VAL A CA  
1785 C C   . VAL A 232 ? 0.09045 0.09404 0.13411 0.01075  -0.01675 0.00406  232 VAL A C   
1786 O O   . VAL A 232 ? 0.09188 0.09508 0.13371 0.01180  -0.01341 0.00145  232 VAL A O   
1787 C CB  . VAL A 232 ? 0.10898 0.11310 0.14314 0.00595  -0.01823 0.00757  232 VAL A CB  
1788 C CG1 . VAL A 232 ? 0.09929 0.10476 0.13257 0.00650  -0.01447 0.00488  232 VAL A CG1 
1789 C CG2 . VAL A 232 ? 0.11365 0.11630 0.14049 0.00341  -0.01848 0.00912  232 VAL A CG2 
1790 N N   . ALA A 233 ? 0.07931 0.08469 0.13068 0.01152  -0.01910 0.00463  233 ALA A N   
1791 C CA  . ALA A 233 ? 0.09628 0.10358 0.15456 0.01360  -0.01733 0.00170  233 ALA A CA  
1792 C C   . ALA A 233 ? 0.09917 0.10453 0.15934 0.01565  -0.01584 -0.00054 233 ALA A C   
1793 O O   . ALA A 233 ? 0.10616 0.11223 0.16661 0.01661  -0.01234 -0.00381 233 ALA A O   
1794 C CB  . ALA A 233 ? 0.07619 0.08590 0.14336 0.01407  -0.02058 0.00293  233 ALA A CB  
1795 N N   . GLY A 234 ? 0.11265 0.11552 0.17390 0.01606  -0.01843 0.00115  234 GLY A N   
1796 C CA  . GLY A 234 ? 0.09383 0.09475 0.15725 0.01783  -0.01731 -0.00096 234 GLY A CA  
1797 C C   . GLY A 234 ? 0.08846 0.08696 0.14380 0.01728  -0.01538 -0.00148 234 GLY A C   
1798 O O   . GLY A 234 ? 0.11086 0.10733 0.16719 0.01830  -0.01522 -0.00253 234 GLY A O   
1799 N N   . PHE A 235 ? 0.06328 0.06197 0.11106 0.01569  -0.01394 -0.00087 235 PHE A N   
1800 C CA  . PHE A 235 ? 0.10399 0.10060 0.14461 0.01518  -0.01242 -0.00113 235 PHE A CA  
1801 C C   . PHE A 235 ? 0.10906 0.10542 0.14959 0.01656  -0.00937 -0.00449 235 PHE A C   
1802 O O   . PHE A 235 ? 0.14266 0.14085 0.18419 0.01694  -0.00688 -0.00671 235 PHE A O   
1803 C CB  . PHE A 235 ? 0.10463 0.10175 0.13848 0.01339  -0.01124 -0.00019 235 PHE A CB  
1804 C CG  . PHE A 235 ? 0.09601 0.09138 0.12329 0.01305  -0.00949 -0.00066 235 PHE A CG  
1805 C CD1 . PHE A 235 ? 0.10091 0.09449 0.12488 0.01203  -0.01103 0.00114  235 PHE A CD1 
1806 C CD2 . PHE A 235 ? 0.10007 0.09570 0.12460 0.01358  -0.00641 -0.00283 235 PHE A CD2 
1807 C CE1 . PHE A 235 ? 0.10357 0.09589 0.12237 0.01181  -0.00951 0.00059  235 PHE A CE1 
1808 C CE2 . PHE A 235 ? 0.11561 0.10975 0.13469 0.01335  -0.00520 -0.00301 235 PHE A CE2 
1809 C CZ  . PHE A 235 ? 0.07081 0.06342 0.08739 0.01259  -0.00675 -0.00140 235 PHE A CZ  
1810 N N   . GLN A 236 ? 0.12017 0.11435 0.15926 0.01701  -0.00954 -0.00488 236 GLN A N   
1811 C CA  . GLN A 236 ? 0.11523 0.10906 0.15290 0.01782  -0.00683 -0.00789 236 GLN A CA  
1812 C C   . GLN A 236 ? 0.14766 0.13960 0.17862 0.01710  -0.00666 -0.00711 236 GLN A C   
1813 O O   . GLN A 236 ? 0.12526 0.11539 0.15631 0.01695  -0.00863 -0.00581 236 GLN A O   
1814 C CB  . GLN A 236 ? 0.13287 0.12627 0.17735 0.01930  -0.00706 -0.00999 236 GLN A CB  
1815 C CG  . GLN A 236 ? 0.15861 0.15433 0.21054 0.02022  -0.00658 -0.01157 236 GLN A CG  
1816 C CD  . GLN A 236 ? 0.19586 0.19132 0.25471 0.02171  -0.00588 -0.01462 236 GLN A CD  
1817 O OE1 . GLN A 236 ? 0.17931 0.17377 0.23583 0.02181  -0.00400 -0.01698 236 GLN A OE1 
1818 N NE2 . GLN A 236 ? 0.26941 0.26585 0.33714 0.02281  -0.00746 -0.01468 236 GLN A NE2 
1819 N N   . LYS A 237 ? 0.07264 0.06502 0.09813 0.01659  -0.00439 -0.00787 237 LYS A N   
1820 C CA  . LYS A 237 ? 0.11388 0.10488 0.13344 0.01591  -0.00433 -0.00694 237 LYS A CA  
1821 C C   . LYS A 237 ? 0.11969 0.10917 0.13924 0.01641  -0.00477 -0.00791 237 LYS A C   
1822 O O   . LYS A 237 ? 0.09871 0.08687 0.11631 0.01583  -0.00626 -0.00634 237 LYS A O   
1823 C CB  . LYS A 237 ? 0.10900 0.10067 0.12371 0.01550  -0.00194 -0.00763 237 LYS A CB  
1824 C CG  . LYS A 237 ? 0.11858 0.10908 0.12794 0.01495  -0.00194 -0.00662 237 LYS A CG  
1825 C CD  . LYS A 237 ? 0.11654 0.10654 0.12501 0.01398  -0.00358 -0.00429 237 LYS A CD  
1826 C CE  . LYS A 237 ? 0.12148 0.11093 0.12526 0.01337  -0.00288 -0.00359 237 LYS A CE  
1827 N NZ  . LYS A 237 ? 0.09279 0.08283 0.09444 0.01311  -0.00110 -0.00369 237 LYS A NZ  
1828 N N   . PRO A 238 ? 0.11883 0.10850 0.14032 0.01721  -0.00341 -0.01061 238 PRO A N   
1829 C CA  . PRO A 238 ? 0.15561 0.14382 0.17665 0.01742  -0.00377 -0.01167 238 PRO A CA  
1830 C C   . PRO A 238 ? 0.13185 0.11842 0.15711 0.01767  -0.00626 -0.01055 238 PRO A C   
1831 O O   . PRO A 238 ? 0.13975 0.12489 0.16424 0.01757  -0.00679 -0.01101 238 PRO A O   
1832 C CB  . PRO A 238 ? 0.18738 0.17647 0.21004 0.01791  -0.00149 -0.01517 238 PRO A CB  
1833 C CG  . PRO A 238 ? 0.15059 0.14156 0.17210 0.01764  0.00041  -0.01565 238 PRO A CG  
1834 C CD  . PRO A 238 ? 0.11705 0.10840 0.14052 0.01761  -0.00111 -0.01313 238 PRO A CD  
1835 N N   . ASP A 239 ? 0.14363 0.13032 0.17330 0.01786  -0.00793 -0.00899 239 ASP A N   
1836 C CA  . ASP A 239 ? 0.14186 0.12672 0.17568 0.01794  -0.01066 -0.00745 239 ASP A CA  
1837 C C   . ASP A 239 ? 0.16151 0.14543 0.19186 0.01644  -0.01280 -0.00402 239 ASP A C   
1838 O O   . ASP A 239 ? 0.19550 0.17766 0.22825 0.01604  -0.01526 -0.00224 239 ASP A O   
1839 C CB  . ASP A 239 ? 0.12713 0.11264 0.16852 0.01894  -0.01172 -0.00750 239 ASP A CB  
1840 C CG  . ASP A 239 ? 0.15814 0.14469 0.20404 0.02030  -0.00938 -0.01138 239 ASP A CG  
1841 O OD1 . ASP A 239 ? 0.19993 0.18609 0.24336 0.02034  -0.00742 -0.01390 239 ASP A OD1 
1842 O OD2 . ASP A 239 ? 0.18541 0.17334 0.23744 0.02117  -0.00947 -0.01204 239 ASP A OD2 
1843 N N   . THR A 240 ? 0.11207 0.09702 0.13694 0.01543  -0.01187 -0.00313 240 THR A N   
1844 C CA  . THR A 240 ? 0.09705 0.08143 0.11861 0.01369  -0.01344 -0.00038 240 THR A CA  
1845 C C   . THR A 240 ? 0.14560 0.12843 0.16434 0.01303  -0.01372 -0.00031 240 THR A C   
1846 O O   . THR A 240 ? 0.11801 0.10059 0.13604 0.01385  -0.01241 -0.00239 240 THR A O   
1847 C CB  . THR A 240 ? 0.12420 0.11018 0.14153 0.01282  -0.01206 0.00012  240 THR A CB  
1848 O OG1 . THR A 240 ? 0.17536 0.16191 0.18969 0.01352  -0.00959 -0.00187 240 THR A OG1 
1849 C CG2 . THR A 240 ? 0.17713 0.16466 0.19731 0.01296  -0.01227 0.00055  240 THR A CG2 
1850 N N   . ASP A 241 ? 0.10256 0.08454 0.11955 0.01126  -0.01545 0.00207  241 ASP A N   
1851 C CA  . ASP A 241 ? 0.14536 0.12586 0.16051 0.01031  -0.01607 0.00239  241 ASP A CA  
1852 C C   . ASP A 241 ? 0.10205 0.08361 0.11212 0.00942  -0.01443 0.00198  241 ASP A C   
1853 O O   . ASP A 241 ? 0.11219 0.09460 0.11970 0.00793  -0.01434 0.00328  241 ASP A O   
1854 C CB  . ASP A 241 ? 0.15399 0.13295 0.17003 0.00851  -0.01881 0.00522  241 ASP A CB  
1855 C CG  . ASP A 241 ? 0.11732 0.09431 0.13287 0.00766  -0.01964 0.00541  241 ASP A CG  
1856 O OD1 . ASP A 241 ? 0.09683 0.07421 0.10988 0.00780  -0.01804 0.00371  241 ASP A OD1 
1857 O OD2 . ASP A 241 ? 0.11944 0.09446 0.13726 0.00675  -0.02207 0.00740  241 ASP A OD2 
1858 N N   . PRO A 242 ? 0.10234 0.08395 0.11108 0.01016  -0.01319 0.00015  242 PRO A N   
1859 C CA  . PRO A 242 ? 0.09532 0.07800 0.10018 0.00946  -0.01191 -0.00012 242 PRO A CA  
1860 C C   . PRO A 242 ? 0.10638 0.08857 0.10962 0.00742  -0.01274 0.00106  242 PRO A C   
1861 O O   . PRO A 242 ? 0.12313 0.10646 0.12382 0.00649  -0.01170 0.00105  242 PRO A O   
1862 C CB  . PRO A 242 ? 0.07811 0.06108 0.08261 0.01087  -0.01080 -0.00229 242 PRO A CB  
1863 C CG  . PRO A 242 ? 0.09992 0.08144 0.10768 0.01149  -0.01177 -0.00309 242 PRO A CG  
1864 C CD  . PRO A 242 ? 0.08786 0.06876 0.09883 0.01161  -0.01286 -0.00190 242 PRO A CD  
1865 N N   . SER A 243 ? 0.08912 0.06964 0.09398 0.00656  -0.01448 0.00200  243 SER A N   
1866 C CA  . SER A 243 ? 0.11565 0.09562 0.11876 0.00425  -0.01519 0.00309  243 SER A CA  
1867 C C   . SER A 243 ? 0.11914 0.09903 0.12085 0.00188  -0.01623 0.00545  243 SER A C   
1868 O O   . SER A 243 ? 0.13507 0.11463 0.13479 -0.00059 -0.01667 0.00643  243 SER A O   
1869 C CB  . SER A 243 ? 0.11078 0.08866 0.11598 0.00413  -0.01659 0.00308  243 SER A CB  
1870 O OG  . SER A 243 ? 0.07705 0.05312 0.08549 0.00445  -0.01847 0.00445  243 SER A OG  
1871 N N   . ALA A 244 ? 0.10607 0.08640 0.10860 0.00230  -0.01662 0.00632  244 ALA A N   
1872 C CA  . ALA A 244 ? 0.12619 0.10674 0.12704 -0.00019 -0.01774 0.00856  244 ALA A CA  
1873 C C   . ALA A 244 ? 0.13799 0.12047 0.13514 -0.00164 -0.01564 0.00781  244 ALA A C   
1874 O O   . ALA A 244 ? 0.13302 0.11681 0.13005 -0.00006 -0.01379 0.00627  244 ALA A O   
1875 C CB  . ALA A 244 ? 0.13719 0.11785 0.14074 0.00080  -0.01900 0.00961  244 ALA A CB  
1876 N N   . TRP A 245 ? 0.16517 0.14775 0.15944 -0.00480 -0.01582 0.00880  245 TRP A N   
1877 C CA  . TRP A 245 ? 0.15654 0.14097 0.14784 -0.00642 -0.01356 0.00766  245 TRP A CA  
1878 C C   . TRP A 245 ? 0.16963 0.15453 0.15801 -0.01002 -0.01424 0.00938  245 TRP A C   
1879 O O   . TRP A 245 ? 0.20808 0.19458 0.19459 -0.01111 -0.01248 0.00848  245 TRP A O   
1880 C CB  . TRP A 245 ? 0.18472 0.16957 0.17522 -0.00704 -0.01215 0.00613  245 TRP A CB  
1881 C CG  . TRP A 245 ? 0.20077 0.18431 0.19043 -0.00945 -0.01366 0.00745  245 TRP A CG  
1882 C CD1 . TRP A 245 ? 0.20338 0.18510 0.19507 -0.00841 -0.01517 0.00787  245 TRP A CD1 
1883 C CD2 . TRP A 245 ? 0.28448 0.26832 0.27086 -0.01360 -0.01365 0.00845  245 TRP A CD2 
1884 N NE1 . TRP A 245 ? 0.20539 0.18605 0.19538 -0.01155 -0.01624 0.00929  245 TRP A NE1 
1885 C CE2 . TRP A 245 ? 0.23658 0.21858 0.22308 -0.01488 -0.01533 0.00972  245 TRP A CE2 
1886 C CE3 . TRP A 245 ? 0.24421 0.22968 0.22742 -0.01661 -0.01224 0.00823  245 TRP A CE3 
1887 C CZ2 . TRP A 245 ? 0.34849 0.33022 0.33176 -0.01916 -0.01574 0.01102  245 TRP A CZ2 
1888 C CZ3 . TRP A 245 ? 0.24843 0.23385 0.22835 -0.02095 -0.01250 0.00926  245 TRP A CZ3 
1889 C CH2 . TRP A 245 ? 0.32332 0.30687 0.30314 -0.02224 -0.01428 0.01076  245 TRP A CH2 
1890 N N   . GLU A 246 ? 0.21861 0.20205 0.20652 -0.01206 -0.01686 0.01190  246 GLU A N   
1891 C CA  . GLU A 246 ? 0.18236 0.16624 0.16698 -0.01589 -0.01797 0.01393  246 GLU A CA  
1892 C C   . GLU A 246 ? 0.19414 0.17897 0.17961 -0.01512 -0.01858 0.01457  246 GLU A C   
1893 O O   . GLU A 246 ? 0.16126 0.14771 0.14381 -0.01744 -0.01749 0.01430  246 GLU A O   
1894 C CB  . GLU A 246 ? 0.26649 0.24822 0.25066 -0.01812 -0.02115 0.01698  246 GLU A CB  
1895 C CG  . GLU A 246 ? 0.31158 0.29209 0.29568 -0.01851 -0.02071 0.01633  246 GLU A CG  
1896 C CD  . GLU A 246 ? 0.42945 0.40763 0.41234 -0.02147 -0.02370 0.01954  246 GLU A CD  
1897 O OE1 . GLU A 246 ? 0.39953 0.37672 0.38269 -0.02244 -0.02666 0.02254  246 GLU A OE1 
1898 O OE2 . GLU A 246 ? 0.47016 0.44749 0.45197 -0.02292 -0.02322 0.01919  246 GLU A OE2 
1899 N N   . LYS A 247 ? 0.16585 0.14982 0.15552 -0.01202 -0.02016 0.01519  247 LYS A N   
1900 C CA  . LYS A 247 ? 0.17144 0.15662 0.16294 -0.01054 -0.02025 0.01512  247 LYS A CA  
1901 C C   . LYS A 247 ? 0.15376 0.13889 0.14886 -0.00632 -0.01872 0.01288  247 LYS A C   
1902 O O   . LYS A 247 ? 0.18187 0.16569 0.18082 -0.00415 -0.02019 0.01322  247 LYS A O   
1903 C CB  . LYS A 247 ? 0.17465 0.15919 0.16825 -0.01128 -0.02393 0.01822  247 LYS A CB  
1904 C CG  . LYS A 247 ? 0.16886 0.15536 0.16193 -0.01236 -0.02435 0.01890  247 LYS A CG  
1905 C CD  . LYS A 247 ? 0.16513 0.15253 0.16270 -0.00872 -0.02359 0.01744  247 LYS A CD  
1906 C CE  . LYS A 247 ? 0.16595 0.15446 0.16592 -0.00932 -0.02628 0.01955  247 LYS A CE  
1907 N NZ  . LYS A 247 ? 0.17037 0.16074 0.16588 -0.01288 -0.02605 0.02018  247 LYS A NZ  
1908 N N   . PRO A 248 ? 0.16397 0.15037 0.15797 -0.00523 -0.01578 0.01052  248 PRO A N   
1909 C CA  . PRO A 248 ? 0.15573 0.14204 0.15232 -0.00168 -0.01438 0.00856  248 PRO A CA  
1910 C C   . PRO A 248 ? 0.11769 0.10404 0.11817 0.00033  -0.01557 0.00895  248 PRO A C   
1911 O O   . PRO A 248 ? 0.10825 0.09545 0.10930 -0.00063 -0.01669 0.01022  248 PRO A O   
1912 C CB  . PRO A 248 ? 0.14858 0.13623 0.14305 -0.00156 -0.01150 0.00673  248 PRO A CB  
1913 C CG  . PRO A 248 ? 0.14794 0.13607 0.13904 -0.00476 -0.01091 0.00695  248 PRO A CG  
1914 C CD  . PRO A 248 ? 0.13967 0.12746 0.13001 -0.00739 -0.01355 0.00947  248 PRO A CD  
1915 N N   . ALA A 249 ? 0.09939 0.08500 0.10272 0.00301  -0.01527 0.00766  249 ALA A N   
1916 C CA  . ALA A 249 ? 0.13128 0.11691 0.13916 0.00495  -0.01624 0.00758  249 ALA A CA  
1917 C C   . ALA A 249 ? 0.10991 0.09729 0.11826 0.00591  -0.01459 0.00648  249 ALA A C   
1918 O O   . ALA A 249 ? 0.15392 0.14188 0.16625 0.00702  -0.01539 0.00651  249 ALA A O   
1919 C CB  . ALA A 249 ? 0.15058 0.13501 0.16107 0.00714  -0.01596 0.00600  249 ALA A CB  
1920 N N   . THR A 250 ? 0.10718 0.09537 0.11205 0.00550  -0.01231 0.00546  250 THR A N   
1921 C CA  . THR A 250 ? 0.10450 0.09407 0.10945 0.00613  -0.01064 0.00452  250 THR A CA  
1922 C C   . THR A 250 ? 0.09338 0.08386 0.09527 0.00378  -0.01016 0.00528  250 THR A C   
1923 O O   . THR A 250 ? 0.14338 0.13363 0.14323 0.00153  -0.01120 0.00652  250 THR A O   
1924 C CB  . THR A 250 ? 0.08571 0.07513 0.08967 0.00795  -0.00825 0.00249  250 THR A CB  
1925 O OG1 . THR A 250 ? 0.10700 0.09587 0.10769 0.00733  -0.00730 0.00221  250 THR A OG1 
1926 C CG2 . THR A 250 ? 0.08230 0.07108 0.08913 0.00988  -0.00858 0.00141  250 THR A CG2 
1927 N N   . THR A 251 ? 0.09674 0.08825 0.09819 0.00405  -0.00839 0.00437  251 THR A N   
1928 C CA  . THR A 251 ? 0.09520 0.08772 0.09448 0.00175  -0.00793 0.00484  251 THR A CA  
1929 C C   . THR A 251 ? 0.10790 0.09995 0.10350 0.00034  -0.00626 0.00419  251 THR A C   
1930 O O   . THR A 251 ? 0.10065 0.09337 0.09414 -0.00229 -0.00624 0.00464  251 THR A O   
1931 C CB  . THR A 251 ? 0.08260 0.07624 0.08288 0.00243  -0.00644 0.00394  251 THR A CB  
1932 O OG1 . THR A 251 ? 0.07120 0.06408 0.07034 0.00401  -0.00400 0.00238  251 THR A OG1 
1933 C CG2 . THR A 251 ? 0.05882 0.05336 0.06353 0.00375  -0.00788 0.00423  251 THR A CG2 
1934 N N   . VAL A 252 ? 0.10222 0.09332 0.09726 0.00190  -0.00486 0.00303  252 VAL A N   
1935 C CA  . VAL A 252 ? 0.12181 0.11261 0.11457 0.00106  -0.00309 0.00210  252 VAL A CA  
1936 C C   . VAL A 252 ? 0.10350 0.09488 0.09516 -0.00004 -0.00126 0.00141  252 VAL A C   
1937 O O   . VAL A 252 ? 0.11553 0.10724 0.10546 -0.00223 -0.00029 0.00094  252 VAL A O   
1938 C CB  . VAL A 252 ? 0.15707 0.14786 0.14834 -0.00119 -0.00397 0.00266  252 VAL A CB  
1939 C CG1 . VAL A 252 ? 0.15320 0.14375 0.14349 -0.00124 -0.00212 0.00126  252 VAL A CG1 
1940 C CG2 . VAL A 252 ? 0.14314 0.13325 0.13578 -0.00062 -0.00632 0.00384  252 VAL A CG2 
1941 N N   . LEU A 253 ? 0.05809 0.04962 0.05081 0.00125  -0.00060 0.00115  253 LEU A N   
1942 C CA  . LEU A 253 ? 0.07364 0.06538 0.06555 0.00046  0.00132  0.00039  253 LEU A CA  
1943 C C   . LEU A 253 ? 0.06503 0.05550 0.05676 0.00220  0.00327  -0.00057 253 LEU A C   
1944 O O   . LEU A 253 ? 0.11207 0.10223 0.10339 0.00177  0.00496  -0.00117 253 LEU A O   
1945 C CB  . LEU A 253 ? 0.07031 0.06317 0.06354 0.00032  0.00082  0.00080  253 LEU A CB  
1946 C CG  . LEU A 253 ? 0.07747 0.07180 0.07083 -0.00199 -0.00110 0.00194  253 LEU A CG  
1947 C CD1 . LEU A 253 ? 0.08047 0.07616 0.07636 -0.00150 -0.00188 0.00231  253 LEU A CD1 
1948 C CD2 . LEU A 253 ? 0.08619 0.08095 0.07693 -0.00496 0.00001  0.00144  253 LEU A CD2 
1949 N N   . SER A 254 ? 0.05922 0.04888 0.05127 0.00401  0.00293  -0.00062 254 SER A N   
1950 C CA  . SER A 254 ? 0.07243 0.06087 0.06427 0.00562  0.00426  -0.00109 254 SER A CA  
1951 C C   . SER A 254 ? 0.07250 0.06027 0.06411 0.00486  0.00589  -0.00183 254 SER A C   
1952 O O   . SER A 254 ? 0.07161 0.05831 0.06324 0.00548  0.00722  -0.00199 254 SER A O   
1953 C CB  . SER A 254 ? 0.08181 0.06983 0.07393 0.00741  0.00324  -0.00094 254 SER A CB  
1954 O OG  . SER A 254 ? 0.05601 0.04437 0.04835 0.00676  0.00226  -0.00095 254 SER A OG  
1955 N N   . PRO A 255 ? 0.07596 0.06419 0.06759 0.00345  0.00602  -0.00239 255 PRO A N   
1956 C CA  . PRO A 255 ? 0.08393 0.07162 0.07618 0.00274  0.00796  -0.00359 255 PRO A CA  
1957 C C   . PRO A 255 ? 0.07792 0.06556 0.06965 0.00107  0.00948  -0.00419 255 PRO A C   
1958 O O   . PRO A 255 ? 0.06059 0.04719 0.05331 0.00106  0.01130  -0.00517 255 PRO A O   
1959 C CB  . PRO A 255 ? 0.08039 0.06908 0.07267 0.00113  0.00785  -0.00433 255 PRO A CB  
1960 C CG  . PRO A 255 ? 0.05857 0.04825 0.04943 -0.00003 0.00597  -0.00325 255 PRO A CG  
1961 C CD  . PRO A 255 ? 0.07223 0.06144 0.06349 0.00221  0.00460  -0.00210 255 PRO A CD  
1962 N N   . TYR A 256 ? 0.05963 0.04836 0.05022 -0.00033 0.00869  -0.00363 256 TYR A N   
1963 C CA  . TYR A 256 ? 0.06074 0.04970 0.05078 -0.00212 0.01000  -0.00423 256 TYR A CA  
1964 C C   . TYR A 256 ? 0.10232 0.09027 0.09282 -0.00058 0.01061  -0.00381 256 TYR A C   
1965 O O   . TYR A 256 ? 0.09671 0.08384 0.08730 -0.00135 0.01239  -0.00458 256 TYR A O   
1966 C CB  . TYR A 256 ? 0.07203 0.06287 0.06082 -0.00451 0.00861  -0.00365 256 TYR A CB  
1967 C CG  . TYR A 256 ? 0.08067 0.07241 0.06832 -0.00645 0.00782  -0.00372 256 TYR A CG  
1968 C CD1 . TYR A 256 ? 0.07904 0.07128 0.06546 -0.00931 0.00944  -0.00523 256 TYR A CD1 
1969 C CD2 . TYR A 256 ? 0.07086 0.06288 0.05862 -0.00565 0.00562  -0.00244 256 TYR A CD2 
1970 C CE1 . TYR A 256 ? 0.10592 0.09908 0.09087 -0.01151 0.00893  -0.00538 256 TYR A CE1 
1971 C CE2 . TYR A 256 ? 0.10322 0.09588 0.08968 -0.00769 0.00492  -0.00235 256 TYR A CE2 
1972 C CZ  . TYR A 256 ? 0.10944 0.10275 0.09431 -0.01070 0.00659  -0.00378 256 TYR A CZ  
1973 O OH  . TYR A 256 ? 0.11242 0.10649 0.09559 -0.01316 0.00609  -0.00377 256 TYR A OH  
1974 N N   . LEU A 257 ? 0.06673 0.05469 0.05750 0.00137  0.00931  -0.00275 257 LEU A N   
1975 C CA  . LEU A 257 ? 0.06862 0.05566 0.05945 0.00260  0.01007  -0.00243 257 LEU A CA  
1976 C C   . LEU A 257 ? 0.08314 0.06796 0.07407 0.00399  0.01118  -0.00244 257 LEU A C   
1977 O O   . LEU A 257 ? 0.07826 0.06177 0.06895 0.00413  0.01242  -0.00230 257 LEU A O   
1978 C CB  . LEU A 257 ? 0.09118 0.07906 0.08233 0.00400  0.00864  -0.00171 257 LEU A CB  
1979 C CG  . LEU A 257 ? 0.08237 0.07235 0.07447 0.00298  0.00735  -0.00148 257 LEU A CG  
1980 C CD1 . LEU A 257 ? 0.09600 0.08661 0.08931 0.00460  0.00589  -0.00110 257 LEU A CD1 
1981 C CD2 . LEU A 257 ? 0.10378 0.09446 0.09616 0.00186  0.00845  -0.00180 257 LEU A CD2 
1982 N N   . LYS A 258 ? 0.07180 0.05616 0.06331 0.00493  0.01063  -0.00247 258 LYS A N   
1983 C CA  . LYS A 258 ? 0.07548 0.05786 0.06780 0.00629  0.01129  -0.00228 258 LYS A CA  
1984 C C   . LYS A 258 ? 0.07912 0.06028 0.07261 0.00516  0.01328  -0.00327 258 LYS A C   
1985 O O   . LYS A 258 ? 0.08624 0.06540 0.07999 0.00572  0.01418  -0.00279 258 LYS A O   
1986 C CB  . LYS A 258 ? 0.08660 0.06929 0.07996 0.00735  0.01019  -0.00231 258 LYS A CB  
1987 C CG  . LYS A 258 ? 0.13594 0.11690 0.13097 0.00889  0.01037  -0.00196 258 LYS A CG  
1988 C CD  . LYS A 258 ? 0.11161 0.09218 0.10932 0.00811  0.01191  -0.00343 258 LYS A CD  
1989 C CE  . LYS A 258 ? 0.13356 0.11269 0.13408 0.00994  0.01162  -0.00299 258 LYS A CE  
1990 N NZ  . LYS A 258 ? 0.20898 0.18595 0.20858 0.01129  0.01103  -0.00108 258 LYS A NZ  
1991 N N   . PHE A 259 ? 0.06681 0.04903 0.06096 0.00338  0.01405  -0.00472 259 PHE A N   
1992 C CA  . PHE A 259 ? 0.09122 0.07244 0.08675 0.00202  0.01624  -0.00624 259 PHE A CA  
1993 C C   . PHE A 259 ? 0.11351 0.09476 0.10779 0.00022  0.01737  -0.00659 259 PHE A C   
1994 O O   . PHE A 259 ? 0.10122 0.08149 0.09655 -0.00113 0.01937  -0.00804 259 PHE A O   
1995 C CB  . PHE A 259 ? 0.09064 0.07329 0.08698 0.00026  0.01696  -0.00805 259 PHE A CB  
1996 C CG  . PHE A 259 ? 0.07362 0.05593 0.07256 0.00178  0.01683  -0.00846 259 PHE A CG  
1997 C CD1 . PHE A 259 ? 0.08522 0.06558 0.08748 0.00299  0.01809  -0.00910 259 PHE A CD1 
1998 C CD2 . PHE A 259 ? 0.06737 0.05130 0.06587 0.00198  0.01535  -0.00821 259 PHE A CD2 
1999 C CE1 . PHE A 259 ? 0.11510 0.09547 0.12051 0.00447  0.01778  -0.00949 259 PHE A CE1 
2000 C CE2 . PHE A 259 ? 0.07416 0.05811 0.07537 0.00326  0.01523  -0.00872 259 PHE A CE2 
2001 C CZ  . PHE A 259 ? 0.07898 0.06133 0.08382 0.00455  0.01640  -0.00938 259 PHE A CZ  
2002 N N   . GLY A 260 ? 0.12331 0.10572 0.11582 0.00011  0.01622  -0.00552 260 GLY A N   
2003 C CA  . GLY A 260 ? 0.11176 0.09466 0.10346 -0.00171 0.01715  -0.00591 260 GLY A CA  
2004 C C   . GLY A 260 ? 0.12954 0.11449 0.12050 -0.00464 0.01740  -0.00715 260 GLY A C   
2005 O O   . GLY A 260 ? 0.13236 0.11769 0.12285 -0.00657 0.01847  -0.00787 260 GLY A O   
2006 N N   . CYS A 261 ? 0.08788 0.07420 0.07845 -0.00531 0.01642  -0.00739 261 CYS A N   
2007 C CA  . CYS A 261 ? 0.09390 0.08235 0.08295 -0.00850 0.01621  -0.00815 261 CYS A CA  
2008 C C   . CYS A 261 ? 0.09088 0.08128 0.07898 -0.00924 0.01430  -0.00681 261 CYS A C   
2009 O O   . CYS A 261 ? 0.12255 0.11462 0.10939 -0.01214 0.01417  -0.00724 261 CYS A O   
2010 C CB  . CYS A 261 ? 0.10845 0.09782 0.09701 -0.00915 0.01541  -0.00838 261 CYS A CB  
2011 S SG  . CYS A 261 ? 0.10553 0.09330 0.09628 -0.00827 0.01755  -0.01023 261 CYS A SG  
2012 N N   . LEU A 262 ? 0.08318 0.07356 0.07210 -0.00680 0.01279  -0.00530 262 LEU A N   
2013 C CA  . LEU A 262 ? 0.09873 0.09097 0.08799 -0.00699 0.01107  -0.00420 262 LEU A CA  
2014 C C   . LEU A 262 ? 0.08789 0.07930 0.07820 -0.00523 0.01195  -0.00402 262 LEU A C   
2015 O O   . LEU A 262 ? 0.10345 0.09305 0.09400 -0.00299 0.01250  -0.00378 262 LEU A O   
2016 C CB  . LEU A 262 ? 0.07998 0.07325 0.06973 -0.00594 0.00843  -0.00283 262 LEU A CB  
2017 C CG  . LEU A 262 ? 0.09033 0.08562 0.08159 -0.00591 0.00636  -0.00170 262 LEU A CG  
2018 C CD1 . LEU A 262 ? 0.10610 0.10342 0.09660 -0.00911 0.00548  -0.00153 262 LEU A CD1 
2019 C CD2 . LEU A 262 ? 0.08685 0.08238 0.07932 -0.00427 0.00404  -0.00051 262 LEU A CD2 
2020 N N   . SER A 263 ? 0.09384 0.08672 0.08465 -0.00648 0.01202  -0.00410 263 SER A N   
2021 C CA  . SER A 263 ? 0.08598 0.07846 0.07770 -0.00533 0.01303  -0.00407 263 SER A CA  
2022 C C   . SER A 263 ? 0.09164 0.08523 0.08490 -0.00330 0.01143  -0.00321 263 SER A C   
2023 O O   . SER A 263 ? 0.07101 0.06677 0.06569 -0.00359 0.00934  -0.00264 263 SER A O   
2024 C CB  . SER A 263 ? 0.12769 0.12171 0.11981 -0.00758 0.01376  -0.00470 263 SER A CB  
2025 O OG  . SER A 263 ? 0.12072 0.11488 0.11394 -0.00667 0.01461  -0.00468 263 SER A OG  
2026 N N   . ALA A 264 ? 0.06163 0.05367 0.05468 -0.00138 0.01238  -0.00311 264 ALA A N   
2027 C CA  . ALA A 264 ? 0.06229 0.05543 0.05681 0.00030  0.01142  -0.00283 264 ALA A CA  
2028 C C   . ALA A 264 ? 0.08834 0.08398 0.08517 -0.00047 0.01147  -0.00327 264 ALA A C   
2029 O O   . ALA A 264 ? 0.05946 0.05708 0.05893 0.00033  0.01000  -0.00323 264 ALA A O   
2030 C CB  . ALA A 264 ? 0.06148 0.05247 0.05451 0.00194  0.01259  -0.00273 264 ALA A CB  
2031 N N   . ARG A 265 ? 0.09464 0.09025 0.09100 -0.00203 0.01315  -0.00380 265 ARG A N   
2032 C CA  . ARG A 265 ? 0.12306 0.12138 0.12195 -0.00296 0.01330  -0.00437 265 ARG A CA  
2033 C C   . ARG A 265 ? 0.10187 0.10300 0.10295 -0.00425 0.01101  -0.00402 265 ARG A C   
2034 O O   . ARG A 265 ? 0.11598 0.11993 0.12061 -0.00417 0.00995  -0.00416 265 ARG A O   
2035 C CB  . ARG A 265 ? 0.11240 0.10976 0.11001 -0.00452 0.01576  -0.00502 265 ARG A CB  
2036 C CG  . ARG A 265 ? 0.13141 0.12613 0.12698 -0.00353 0.01778  -0.00500 265 ARG A CG  
2037 C CD  . ARG A 265 ? 0.11867 0.11170 0.11277 -0.00523 0.02008  -0.00534 265 ARG A CD  
2038 N NE  . ARG A 265 ? 0.13859 0.12894 0.13049 -0.00456 0.02171  -0.00488 265 ARG A NE  
2039 C CZ  . ARG A 265 ? 0.15141 0.13929 0.14166 -0.00577 0.02368  -0.00475 265 ARG A CZ  
2040 N NH1 . ARG A 265 ? 0.16125 0.14900 0.15199 -0.00766 0.02455  -0.00540 265 ARG A NH1 
2041 N NH2 . ARG A 265 ? 0.13909 0.12446 0.12702 -0.00526 0.02473  -0.00390 265 ARG A NH2 
2042 N N   . LEU A 266 ? 0.10177 0.10232 0.10097 -0.00561 0.01018  -0.00358 266 LEU A N   
2043 C CA  . LEU A 266 ? 0.11859 0.12161 0.11910 -0.00707 0.00756  -0.00281 266 LEU A CA  
2044 C C   . LEU A 266 ? 0.10349 0.10721 0.10624 -0.00524 0.00502  -0.00176 266 LEU A C   
2045 O O   . LEU A 266 ? 0.09986 0.10613 0.10604 -0.00537 0.00278  -0.00108 266 LEU A O   
2046 C CB  . LEU A 266 ? 0.09462 0.09671 0.09188 -0.00934 0.00762  -0.00280 266 LEU A CB  
2047 C CG  . LEU A 266 ? 0.19784 0.20195 0.19510 -0.01119 0.00468  -0.00162 266 LEU A CG  
2048 C CD1 . LEU A 266 ? 0.20226 0.20957 0.20142 -0.01328 0.00338  -0.00139 266 LEU A CD1 
2049 C CD2 . LEU A 266 ? 0.15838 0.16117 0.15187 -0.01323 0.00524  -0.00194 266 LEU A CD2 
2050 N N   . PHE A 267 ? 0.09501 0.09646 0.09623 -0.00354 0.00524  -0.00158 267 PHE A N   
2051 C CA  . PHE A 267 ? 0.08020 0.08188 0.08359 -0.00166 0.00323  -0.00087 267 PHE A CA  
2052 C C   . PHE A 267 ? 0.08076 0.08422 0.08840 -0.00017 0.00316  -0.00147 267 PHE A C   
2053 O O   . PHE A 267 ? 0.06455 0.06980 0.07608 0.00033  0.00083  -0.00086 267 PHE A O   
2054 C CB  . PHE A 267 ? 0.09902 0.09801 0.09999 -0.00008 0.00411  -0.00101 267 PHE A CB  
2055 C CG  . PHE A 267 ? 0.09415 0.09292 0.09643 0.00127  0.00197  -0.00025 267 PHE A CG  
2056 C CD1 . PHE A 267 ? 0.09308 0.09365 0.09903 0.00143  -0.00048 0.00053  267 PHE A CD1 
2057 C CD2 . PHE A 267 ? 0.12012 0.11682 0.12032 0.00237  0.00234  -0.00028 267 PHE A CD2 
2058 C CE1 . PHE A 267 ? 0.12773 0.12769 0.13511 0.00263  -0.00240 0.00124  267 PHE A CE1 
2059 C CE2 . PHE A 267 ? 0.10451 0.10090 0.10588 0.00345  0.00050  0.00030  267 PHE A CE2 
2060 C CZ  . PHE A 267 ? 0.08090 0.07874 0.08578 0.00356  -0.00181 0.00106  267 PHE A CZ  
2061 N N   . HIS A 268 ? 0.06501 0.06802 0.07219 0.00041  0.00575  -0.00272 268 HIS A N   
2062 C CA  . HIS A 268 ? 0.08741 0.09228 0.09849 0.00152  0.00630  -0.00379 268 HIS A CA  
2063 C C   . HIS A 268 ? 0.09018 0.09838 0.10542 0.00033  0.00521  -0.00384 268 HIS A C   
2064 O O   . HIS A 268 ? 0.09606 0.10649 0.11643 0.00140  0.00432  -0.00439 268 HIS A O   
2065 C CB  . HIS A 268 ? 0.10496 0.10855 0.11373 0.00176  0.00945  -0.00498 268 HIS A CB  
2066 C CG  . HIS A 268 ? 0.09411 0.09928 0.10606 0.00288  0.01048  -0.00645 268 HIS A CG  
2067 N ND1 . HIS A 268 ? 0.07624 0.08442 0.09229 0.00224  0.01104  -0.00753 268 HIS A ND1 
2068 C CD2 . HIS A 268 ? 0.06483 0.06921 0.07657 0.00440  0.01121  -0.00728 268 HIS A CD2 
2069 C CE1 . HIS A 268 ? 0.08983 0.09902 0.10827 0.00333  0.01229  -0.00914 268 HIS A CE1 
2070 N NE2 . HIS A 268 ? 0.08732 0.09417 0.10294 0.00456  0.01243  -0.00904 268 HIS A NE2 
2071 N N   . ALA A 269 ? 0.08259 0.09129 0.09607 -0.00193 0.00527  -0.00343 269 ALA A N   
2072 C CA  . ALA A 269 ? 0.08751 0.09964 0.10483 -0.00334 0.00393  -0.00335 269 ALA A CA  
2073 C C   . ALA A 269 ? 0.09407 0.10784 0.11469 -0.00322 0.00005  -0.00172 269 ALA A C   
2074 O O   . ALA A 269 ? 0.08268 0.09949 0.10888 -0.00302 -0.00167 -0.00163 269 ALA A O   
2075 C CB  . ALA A 269 ? 0.10658 0.11871 0.12071 -0.00610 0.00498  -0.00343 269 ALA A CB  
2076 N N   . ARG A 270 ? 0.11457 0.12636 0.13210 -0.00343 -0.00148 -0.00034 270 ARG A N   
2077 C CA  . ARG A 270 ? 0.10438 0.11725 0.12452 -0.00357 -0.00535 0.00160  270 ARG A CA  
2078 C C   . ARG A 270 ? 0.11777 0.13073 0.14297 -0.00073 -0.00645 0.00147  270 ARG A C   
2079 O O   . ARG A 270 ? 0.18771 0.20242 0.21788 -0.00042 -0.00962 0.00275  270 ARG A O   
2080 C CB  . ARG A 270 ? 0.13806 0.14878 0.15306 -0.00501 -0.00633 0.00295  270 ARG A CB  
2081 C CG  . ARG A 270 ? 0.16610 0.17686 0.17644 -0.00814 -0.00524 0.00278  270 ARG A CG  
2082 C CD  . ARG A 270 ? 0.13567 0.14934 0.14725 -0.01083 -0.00813 0.00422  270 ARG A CD  
2083 N NE  . ARG A 270 ? 0.17798 0.19171 0.19003 -0.01133 -0.01190 0.00662  270 ARG A NE  
2084 C CZ  . ARG A 270 ? 0.26913 0.28138 0.27636 -0.01333 -0.01256 0.00760  270 ARG A CZ  
2085 N NH1 . ARG A 270 ? 0.29780 0.30853 0.29989 -0.01484 -0.00967 0.00615  270 ARG A NH1 
2086 N NH2 . ARG A 270 ? 0.27042 0.28267 0.27826 -0.01390 -0.01615 0.01003  270 ARG A NH2 
2087 N N   . LEU A 271 ? 0.06730 0.07838 0.09153 0.00126  -0.00398 -0.00006 271 LEU A N   
2088 C CA  . LEU A 271 ? 0.10651 0.11767 0.13548 0.00376  -0.00460 -0.00071 271 LEU A CA  
2089 C C   . LEU A 271 ? 0.13328 0.14767 0.16912 0.00450  -0.00445 -0.00204 271 LEU A C   
2090 O O   . LEU A 271 ? 0.13290 0.14845 0.17498 0.00597  -0.00649 -0.00192 271 LEU A O   
2091 C CB  . LEU A 271 ? 0.09459 0.10324 0.12027 0.00523  -0.00189 -0.00217 271 LEU A CB  
2092 C CG  . LEU A 271 ? 0.07949 0.08516 0.10016 0.00516  -0.00240 -0.00105 271 LEU A CG  
2093 C CD1 . LEU A 271 ? 0.08658 0.09019 0.10377 0.00627  0.00035  -0.00244 271 LEU A CD1 
2094 C CD2 . LEU A 271 ? 0.09476 0.09999 0.11836 0.00604  -0.00545 0.00023  271 LEU A CD2 
2095 N N   . LEU A 272 ? 0.09666 0.11251 0.13189 0.00349  -0.00197 -0.00342 272 LEU A N   
2096 C CA  . LEU A 272 ? 0.12519 0.14452 0.16718 0.00396  -0.00151 -0.00498 272 LEU A CA  
2097 C C   . LEU A 272 ? 0.14443 0.16669 0.19196 0.00326  -0.00532 -0.00329 272 LEU A C   
2098 O O   . LEU A 272 ? 0.15463 0.17957 0.21006 0.00455  -0.00637 -0.00408 272 LEU A O   
2099 C CB  . LEU A 272 ? 0.12044 0.14056 0.15997 0.00260  0.00199  -0.00665 272 LEU A CB  
2100 C CG  . LEU A 272 ? 0.12972 0.14736 0.16465 0.00320  0.00570  -0.00829 272 LEU A CG  
2101 C CD1 . LEU A 272 ? 0.14910 0.16728 0.18155 0.00146  0.00876  -0.00942 272 LEU A CD1 
2102 C CD2 . LEU A 272 ? 0.17553 0.19384 0.21475 0.00526  0.00664  -0.01025 272 LEU A CD2 
2103 N N   . GLU A 273 ? 0.14171 0.16360 0.18545 0.00111  -0.00746 -0.00101 273 GLU A N   
2104 C CA  . GLU A 273 ? 0.16566 0.19023 0.21394 0.00008  -0.01161 0.00108  273 GLU A CA  
2105 C C   . GLU A 273 ? 0.14493 0.16909 0.19859 0.00206  -0.01497 0.00249  273 GLU A C   
2106 O O   . GLU A 273 ? 0.10649 0.13346 0.16803 0.00276  -0.01767 0.00308  273 GLU A O   
2107 C CB  . GLU A 273 ? 0.22063 0.24454 0.26257 -0.00303 -0.01307 0.00315  273 GLU A CB  
2108 C CG  . GLU A 273 ? 0.23997 0.26424 0.27729 -0.00521 -0.00997 0.00174  273 GLU A CG  
2109 C CD  . GLU A 273 ? 0.33062 0.35406 0.36163 -0.00841 -0.01104 0.00329  273 GLU A CD  
2110 O OE1 . GLU A 273 ? 0.37503 0.39794 0.40516 -0.00914 -0.01434 0.00561  273 GLU A OE1 
2111 O OE2 . GLU A 273 ? 0.35575 0.37897 0.38265 -0.01036 -0.00850 0.00211  273 GLU A OE2 
2112 N N   . VAL A 274 ? 0.14235 0.16301 0.19232 0.00302  -0.01488 0.00302  274 VAL A N   
2113 C CA  . VAL A 274 ? 0.17462 0.19430 0.22936 0.00482  -0.01792 0.00435  274 VAL A CA  
2114 C C   . VAL A 274 ? 0.11419 0.13492 0.17649 0.00771  -0.01641 0.00170  274 VAL A C   
2115 O O   . VAL A 274 ? 0.13213 0.15399 0.20244 0.00918  -0.01919 0.00233  274 VAL A O   
2116 C CB  . VAL A 274 ? 0.12777 0.14350 0.17615 0.00472  -0.01802 0.00548  274 VAL A CB  
2117 C CG1 . VAL A 274 ? 0.11747 0.13179 0.17088 0.00668  -0.02069 0.00651  274 VAL A CG1 
2118 C CG2 . VAL A 274 ? 0.12283 0.13793 0.16467 0.00159  -0.01968 0.00794  274 VAL A CG2 
2119 N N   . TYR A 275 ? 0.09089 0.11124 0.15088 0.00842  -0.01198 -0.00133 275 TYR A N   
2120 C CA  . TYR A 275 ? 0.11244 0.13386 0.17877 0.01070  -0.00993 -0.00436 275 TYR A CA  
2121 C C   . TYR A 275 ? 0.11829 0.14405 0.19366 0.01103  -0.01062 -0.00540 275 TYR A C   
2122 O O   . TYR A 275 ? 0.08718 0.11427 0.17092 0.01307  -0.01080 -0.00710 275 TYR A O   
2123 C CB  . TYR A 275 ? 0.08517 0.10544 0.14601 0.01069  -0.00511 -0.00711 275 TYR A CB  
2124 C CG  . TYR A 275 ? 0.09443 0.11075 0.14830 0.01103  -0.00425 -0.00673 275 TYR A CG  
2125 C CD1 . TYR A 275 ? 0.05590 0.06999 0.10938 0.01155  -0.00726 -0.00458 275 TYR A CD1 
2126 C CD2 . TYR A 275 ? 0.07735 0.09222 0.12517 0.01072  -0.00055 -0.00841 275 TYR A CD2 
2127 C CE1 . TYR A 275 ? 0.09775 0.10857 0.14531 0.01180  -0.00645 -0.00439 275 TYR A CE1 
2128 C CE2 . TYR A 275 ? 0.08595 0.09752 0.12794 0.01107  -0.00002 -0.00800 275 TYR A CE2 
2129 C CZ  . TYR A 275 ? 0.07763 0.08734 0.11967 0.01164  -0.00289 -0.00614 275 TYR A CZ  
2130 O OH  . TYR A 275 ? 0.06167 0.06844 0.09832 0.01191  -0.00236 -0.00587 275 TYR A OH  
2131 N N   . ARG A 276 ? 0.15103 0.17917 0.22533 0.00899  -0.01098 -0.00459 276 ARG A N   
2132 C CA  . ARG A 276 ? 0.13966 0.17236 0.22266 0.00911  -0.01157 -0.00568 276 ARG A CA  
2133 C C   . ARG A 276 ? 0.12853 0.16273 0.22040 0.01025  -0.01660 -0.00350 276 ARG A C   
2134 O O   . ARG A 276 ? 0.15988 0.19739 0.26185 0.01171  -0.01704 -0.00508 276 ARG A O   
2135 C CB  . ARG A 276 ? 0.15651 0.19124 0.23573 0.00636  -0.01100 -0.00515 276 ARG A CB  
2136 C CG  . ARG A 276 ? 0.17808 0.21218 0.25153 0.00548  -0.00577 -0.00785 276 ARG A CG  
2137 C CD  . ARG A 276 ? 0.19700 0.23235 0.26605 0.00262  -0.00499 -0.00735 276 ARG A CD  
2138 N NE  . ARG A 276 ? 0.20728 0.24046 0.26921 0.00179  -0.00041 -0.00913 276 ARG A NE  
2139 C CZ  . ARG A 276 ? 0.22707 0.26103 0.28563 -0.00043 0.00172  -0.00975 276 ARG A CZ  
2140 N NH1 . ARG A 276 ? 0.23765 0.27484 0.29903 -0.00223 -0.00006 -0.00903 276 ARG A NH1 
2141 N NH2 . ARG A 276 ? 0.23157 0.26295 0.28384 -0.00097 0.00561  -0.01104 276 ARG A NH2 
2142 N N   . ARG A 277 ? 0.11909 0.15089 0.20762 0.00955  -0.02045 0.00015  277 ARG A N   
2143 C CA  . ARG A 277 ? 0.13497 0.16755 0.23108 0.01034  -0.02576 0.00297  277 ARG A CA  
2144 C C   . ARG A 277 ? 0.13053 0.16009 0.23015 0.01288  -0.02662 0.00290  277 ARG A C   
2145 O O   . ARG A 277 ? 0.11675 0.14638 0.22341 0.01386  -0.03105 0.00524  277 ARG A O   
2146 C CB  . ARG A 277 ? 0.16166 0.19356 0.25201 0.00749  -0.02983 0.00732  277 ARG A CB  
2147 C CG  . ARG A 277 ? 0.15654 0.19127 0.24303 0.00456  -0.02924 0.00748  277 ARG A CG  
2148 C CD  . ARG A 277 ? 0.20169 0.23391 0.27721 0.00149  -0.02995 0.00991  277 ARG A CD  
2149 N NE  . ARG A 277 ? 0.19267 0.22767 0.26539 -0.00174 -0.03084 0.01086  277 ARG A NE  
2150 C CZ  . ARG A 277 ? 0.19636 0.23390 0.27228 -0.00348 -0.03571 0.01388  277 ARG A CZ  
2151 N NH1 . ARG A 277 ? 0.19449 0.23212 0.27716 -0.00213 -0.04034 0.01648  277 ARG A NH1 
2152 N NH2 . ARG A 277 ? 0.19995 0.23994 0.27227 -0.00677 -0.03608 0.01438  277 ARG A NH2 
2153 N N   . HIS A 278 ? 0.13213 0.15896 0.22710 0.01387  -0.02267 0.00037  278 HIS A N   
2154 C CA  . HIS A 278 ? 0.13373 0.15760 0.23141 0.01609  -0.02294 -0.00021 278 HIS A CA  
2155 C C   . HIS A 278 ? 0.10806 0.13267 0.20858 0.01784  -0.01805 -0.00510 278 HIS A C   
2156 O O   . HIS A 278 ? 0.13198 0.15468 0.22479 0.01742  -0.01432 -0.00688 278 HIS A O   
2157 C CB  . HIS A 278 ? 0.11903 0.13854 0.20701 0.01506  -0.02334 0.00185  278 HIS A CB  
2158 C CG  . HIS A 278 ? 0.14502 0.16364 0.22999 0.01302  -0.02800 0.00648  278 HIS A CG  
2159 N ND1 . HIS A 278 ? 0.12112 0.14118 0.20032 0.01020  -0.02854 0.00817  278 HIS A ND1 
2160 C CD2 . HIS A 278 ? 0.12954 0.14594 0.21618 0.01307  -0.03226 0.00974  278 HIS A CD2 
2161 C CE1 . HIS A 278 ? 0.13075 0.14972 0.20790 0.00844  -0.03287 0.01216  278 HIS A CE1 
2162 N NE2 . HIS A 278 ? 0.12534 0.14202 0.20683 0.01011  -0.03528 0.01336  278 HIS A NE2 
2163 N N   . PRO A 279 ? 0.06454 0.09204 0.17623 0.01967  -0.01796 -0.00741 279 PRO A N   
2164 C CA  . PRO A 279 ? 0.08860 0.11749 0.20292 0.02076  -0.01287 -0.01250 279 PRO A CA  
2165 C C   . PRO A 279 ? 0.10930 0.13478 0.22164 0.02209  -0.01084 -0.01450 279 PRO A C   
2166 O O   . PRO A 279 ? 0.08609 0.11198 0.19646 0.02212  -0.00619 -0.01840 279 PRO A O   
2167 C CB  . PRO A 279 ? 0.08047 0.11322 0.20778 0.02216  -0.01385 -0.01416 279 PRO A CB  
2168 C CG  . PRO A 279 ? 0.11203 0.14288 0.24190 0.02219  -0.01953 -0.00978 279 PRO A CG  
2169 C CD  . PRO A 279 ? 0.10844 0.13835 0.23111 0.02063  -0.02250 -0.00553 279 PRO A CD  
2170 N N   . ALA A 280 ? 0.10123 0.12339 0.21383 0.02292  -0.01417 -0.01197 280 ALA A N   
2171 C CA  . ALA A 280 ? 0.11176 0.13051 0.22195 0.02393  -0.01252 -0.01364 280 ALA A CA  
2172 C C   . ALA A 280 ? 0.10953 0.12503 0.20690 0.02232  -0.01161 -0.01199 280 ALA A C   
2173 O O   . ALA A 280 ? 0.10743 0.11963 0.20218 0.02286  -0.01194 -0.01175 280 ALA A O   
2174 C CB  . ALA A 280 ? 0.14067 0.15657 0.25487 0.02452  -0.01597 -0.01174 280 ALA A CB  
2175 N N   . HIS A 281 ? 0.09780 0.11419 0.18764 0.02036  -0.01045 -0.01097 281 HIS A N   
2176 C CA  . HIS A 281 ? 0.09061 0.10411 0.16922 0.01891  -0.00966 -0.00943 281 HIS A CA  
2177 C C   . HIS A 281 ? 0.10528 0.11733 0.17956 0.01933  -0.00566 -0.01263 281 HIS A C   
2178 O O   . HIS A 281 ? 0.06757 0.08149 0.14509 0.01987  -0.00247 -0.01626 281 HIS A O   
2179 C CB  . HIS A 281 ? 0.09433 0.10917 0.16692 0.01677  -0.00907 -0.00804 281 HIS A CB  
2180 C CG  . HIS A 281 ? 0.08842 0.10566 0.16050 0.01633  -0.00495 -0.01116 281 HIS A CG  
2181 N ND1 . HIS A 281 ? 0.09004 0.10588 0.15452 0.01563  -0.00132 -0.01274 281 HIS A ND1 
2182 C CD2 . HIS A 281 ? 0.10618 0.12715 0.18446 0.01632  -0.00397 -0.01288 281 HIS A CD2 
2183 C CE1 . HIS A 281 ? 0.10162 0.11999 0.16718 0.01505  0.00176  -0.01518 281 HIS A CE1 
2184 N NE2 . HIS A 281 ? 0.10745 0.12907 0.18138 0.01544  0.00039  -0.01548 281 HIS A NE2 
2185 N N   . SER A 282 ? 0.11704 0.12589 0.18385 0.01883  -0.00587 -0.01127 282 SER A N   
2186 C CA  . SER A 282 ? 0.14450 0.15189 0.20639 0.01897  -0.00261 -0.01379 282 SER A CA  
2187 C C   . SER A 282 ? 0.14284 0.15163 0.19944 0.01771  0.00095  -0.01530 282 SER A C   
2188 O O   . SER A 282 ? 0.12009 0.12985 0.17404 0.01645  0.00074  -0.01369 282 SER A O   
2189 C CB  . SER A 282 ? 0.11662 0.12061 0.17192 0.01860  -0.00395 -0.01170 282 SER A CB  
2190 O OG  . SER A 282 ? 0.11406 0.11751 0.16411 0.01711  -0.00557 -0.00849 282 SER A OG  
2191 N N   . GLN A 283 ? 0.11840 0.12717 0.17337 0.01782  0.00423  -0.01843 283 GLN A N   
2192 C CA  . GLN A 283 ? 0.11563 0.12547 0.16571 0.01649  0.00779  -0.02009 283 GLN A CA  
2193 C C   . GLN A 283 ? 0.12058 0.12774 0.16180 0.01581  0.00896  -0.01974 283 GLN A C   
2194 O O   . GLN A 283 ? 0.14380 0.14885 0.18399 0.01655  0.00761  -0.01927 283 GLN A O   
2195 C CB  . GLN A 283 ? 0.16516 0.17769 0.22098 0.01676  0.01078  -0.02426 283 GLN A CB  
2196 C CG  . GLN A 283 ? 0.22964 0.24512 0.28614 0.01548  0.01314  -0.02542 283 GLN A CG  
2197 C CD  . GLN A 283 ? 0.21590 0.23376 0.27931 0.01588  0.01079  -0.02401 283 GLN A CD  
2198 O OE1 . GLN A 283 ? 0.22761 0.24679 0.28903 0.01456  0.01123  -0.02297 283 GLN A OE1 
2199 N NE2 . GLN A 283 ? 0.21336 0.23176 0.28514 0.01760  0.00816  -0.02392 283 GLN A NE2 
2200 N N   . PRO A 284 ? 0.11555 0.12267 0.15048 0.01437  0.01124  -0.01976 284 PRO A N   
2201 C CA  . PRO A 284 ? 0.14481 0.14953 0.17185 0.01376  0.01209  -0.01927 284 PRO A CA  
2202 C C   . PRO A 284 ? 0.14836 0.15277 0.17593 0.01420  0.01330  -0.02197 284 PRO A C   
2203 O O   . PRO A 284 ? 0.18141 0.18778 0.21462 0.01454  0.01481  -0.02505 284 PRO A O   
2204 C CB  . PRO A 284 ? 0.17472 0.17993 0.19682 0.01208  0.01465  -0.01937 284 PRO A CB  
2205 C CG  . PRO A 284 ? 0.14010 0.14707 0.16576 0.01178  0.01407  -0.01842 284 PRO A CG  
2206 C CD  . PRO A 284 ? 0.14608 0.15502 0.18059 0.01314  0.01254  -0.01949 284 PRO A CD  
2207 N N   . PRO A 285 ? 0.14977 0.15190 0.17183 0.01411  0.01277  -0.02117 285 PRO A N   
2208 C CA  . PRO A 285 ? 0.16100 0.16094 0.17695 0.01378  0.01124  -0.01800 285 PRO A CA  
2209 C C   . PRO A 285 ? 0.14278 0.14136 0.16068 0.01480  0.00807  -0.01584 285 PRO A C   
2210 O O   . PRO A 285 ? 0.15689 0.15385 0.17052 0.01453  0.00686  -0.01353 285 PRO A O   
2211 C CB  . PRO A 285 ? 0.17154 0.17031 0.18164 0.01310  0.01246  -0.01886 285 PRO A CB  
2212 C CG  . PRO A 285 ? 0.16903 0.16852 0.18328 0.01369  0.01305  -0.02192 285 PRO A CG  
2213 C CD  . PRO A 285 ? 0.15658 0.15842 0.17817 0.01413  0.01401  -0.02386 285 PRO A CD  
2214 N N   . VAL A 286 ? 0.10286 0.10201 0.12735 0.01586  0.00669  -0.01652 286 VAL A N   
2215 C CA  . VAL A 286 ? 0.11180 0.10938 0.13777 0.01652  0.00365  -0.01444 286 VAL A CA  
2216 C C   . VAL A 286 ? 0.10744 0.10542 0.13494 0.01618  0.00156  -0.01176 286 VAL A C   
2217 O O   . VAL A 286 ? 0.08224 0.07878 0.10869 0.01603  -0.00078 -0.00951 286 VAL A O   
2218 C CB  . VAL A 286 ? 0.10806 0.10549 0.14036 0.01774  0.00284  -0.01618 286 VAL A CB  
2219 C CG1 . VAL A 286 ? 0.16538 0.16251 0.19585 0.01771  0.00504  -0.01916 286 VAL A CG1 
2220 C CG2 . VAL A 286 ? 0.13648 0.13608 0.17661 0.01840  0.00280  -0.01727 286 VAL A CG2 
2221 N N   . SER A 287 ? 0.10076 0.10080 0.13045 0.01577  0.00239  -0.01202 287 SER A N   
2222 C CA  . SER A 287 ? 0.09615 0.09696 0.12763 0.01520  0.00031  -0.00969 287 SER A CA  
2223 C C   . SER A 287 ? 0.08277 0.08236 0.10762 0.01386  0.00017  -0.00754 287 SER A C   
2224 O O   . SER A 287 ? 0.05685 0.05513 0.07632 0.01358  0.00171  -0.00779 287 SER A O   
2225 C CB  . SER A 287 ? 0.06603 0.06969 0.10195 0.01502  0.00139  -0.01087 287 SER A CB  
2226 O OG  . SER A 287 ? 0.07750 0.08169 0.10894 0.01399  0.00426  -0.01178 287 SER A OG  
2227 N N   . LEU A 288 ? 0.06727 0.06738 0.09283 0.01292  -0.00180 -0.00542 288 LEU A N   
2228 C CA  . LEU A 288 ? 0.07203 0.07123 0.09200 0.01144  -0.00167 -0.00381 288 LEU A CA  
2229 C C   . LEU A 288 ? 0.07171 0.07153 0.08885 0.01077  0.00110  -0.00479 288 LEU A C   
2230 O O   . LEU A 288 ? 0.05591 0.05420 0.06798 0.01024  0.00232  -0.00444 288 LEU A O   
2231 C CB  . LEU A 288 ? 0.10431 0.10423 0.12549 0.01011  -0.00424 -0.00161 288 LEU A CB  
2232 C CG  . LEU A 288 ? 0.13807 0.13622 0.15667 0.00934  -0.00630 0.00030  288 LEU A CG  
2233 C CD1 . LEU A 288 ? 0.16218 0.16127 0.18073 0.00733  -0.00849 0.00241  288 LEU A CD1 
2234 C CD2 . LEU A 288 ? 0.08335 0.07974 0.09620 0.00905  -0.00452 -0.00002 288 LEU A CD2 
2235 N N   . ARG A 289 ? 0.07669 0.07870 0.09742 0.01075  0.00209  -0.00599 289 ARG A N   
2236 C CA  . ARG A 289 ? 0.07687 0.07934 0.09501 0.00998  0.00491  -0.00706 289 ARG A CA  
2237 C C   . ARG A 289 ? 0.10264 0.10359 0.11711 0.01053  0.00700  -0.00830 289 ARG A C   
2238 O O   . ARG A 289 ? 0.10493 0.10473 0.11475 0.00974  0.00871  -0.00807 289 ARG A O   
2239 C CB  . ARG A 289 ? 0.11183 0.11727 0.13517 0.00985  0.00571  -0.00848 289 ARG A CB  
2240 C CG  . ARG A 289 ? 0.12340 0.12935 0.14417 0.00880  0.00884  -0.00971 289 ARG A CG  
2241 C CD  . ARG A 289 ? 0.09716 0.10642 0.12370 0.00866  0.00989  -0.01158 289 ARG A CD  
2242 N NE  . ARG A 289 ? 0.12496 0.13461 0.14873 0.00740  0.01310  -0.01285 289 ARG A NE  
2243 C CZ  . ARG A 289 ? 0.11363 0.12361 0.13684 0.00742  0.01566  -0.01502 289 ARG A CZ  
2244 N NH1 . ARG A 289 ? 0.14290 0.15305 0.16847 0.00872  0.01561  -0.01655 289 ARG A NH1 
2245 N NH2 . ARG A 289 ? 0.13249 0.14258 0.15251 0.00586  0.01842  -0.01574 289 ARG A NH2 
2246 N N   . GLY A 290 ? 0.09118 0.09204 0.10773 0.01175  0.00677  -0.00957 290 GLY A N   
2247 C CA  . GLY A 290 ? 0.08010 0.07970 0.09281 0.01196  0.00848  -0.01071 290 GLY A CA  
2248 C C   . GLY A 290 ? 0.07773 0.07485 0.08498 0.01182  0.00781  -0.00898 290 GLY A C   
2249 O O   . GLY A 290 ? 0.06106 0.05706 0.06392 0.01149  0.00920  -0.00916 290 GLY A O   
2250 N N   . GLN A 291 ? 0.07147 0.06780 0.07904 0.01192  0.00562  -0.00727 291 GLN A N   
2251 C CA  . GLN A 291 ? 0.07288 0.06720 0.07611 0.01174  0.00510  -0.00587 291 GLN A CA  
2252 C C   . GLN A 291 ? 0.07532 0.06894 0.07511 0.01073  0.00649  -0.00507 291 GLN A C   
2253 O O   . GLN A 291 ? 0.06644 0.05844 0.06260 0.01077  0.00700  -0.00454 291 GLN A O   
2254 C CB  . GLN A 291 ? 0.07396 0.06787 0.07843 0.01164  0.00275  -0.00447 291 GLN A CB  
2255 C CG  . GLN A 291 ? 0.07337 0.06743 0.08143 0.01258  0.00112  -0.00493 291 GLN A CG  
2256 C CD  . GLN A 291 ? 0.08473 0.07803 0.09169 0.01351  0.00187  -0.00636 291 GLN A CD  
2257 O OE1 . GLN A 291 ? 0.09276 0.08477 0.09618 0.01352  0.00185  -0.00592 291 GLN A OE1 
2258 N NE2 . GLN A 291 ? 0.10728 0.10157 0.11751 0.01419  0.00258  -0.00827 291 GLN A NE2 
2259 N N   . LEU A 292 ? 0.06151 0.05631 0.06275 0.00981  0.00697  -0.00494 292 LEU A N   
2260 C CA  . LEU A 292 ? 0.07528 0.06929 0.07365 0.00875  0.00858  -0.00448 292 LEU A CA  
2261 C C   . LEU A 292 ? 0.08718 0.08076 0.08335 0.00870  0.01064  -0.00531 292 LEU A C   
2262 O O   . LEU A 292 ? 0.06698 0.05885 0.05975 0.00816  0.01170  -0.00454 292 LEU A O   
2263 C CB  . LEU A 292 ? 0.07169 0.06730 0.07224 0.00754  0.00865  -0.00438 292 LEU A CB  
2264 C CG  . LEU A 292 ? 0.10787 0.10405 0.10990 0.00693  0.00655  -0.00334 292 LEU A CG  
2265 C CD1 . LEU A 292 ? 0.07632 0.07459 0.08073 0.00559  0.00642  -0.00335 292 LEU A CD1 
2266 C CD2 . LEU A 292 ? 0.09247 0.08670 0.09115 0.00635  0.00650  -0.00242 292 LEU A CD2 
2267 N N   . LEU A 293 ? 0.06273 0.05779 0.06087 0.00911  0.01126  -0.00690 293 LEU A N   
2268 C CA  . LEU A 293 ? 0.08034 0.07520 0.07583 0.00858  0.01336  -0.00785 293 LEU A CA  
2269 C C   . LEU A 293 ? 0.09265 0.08552 0.08401 0.00900  0.01301  -0.00723 293 LEU A C   
2270 O O   . LEU A 293 ? 0.11306 0.10464 0.10037 0.00819  0.01418  -0.00669 293 LEU A O   
2271 C CB  . LEU A 293 ? 0.10248 0.09981 0.10163 0.00866  0.01444  -0.01022 293 LEU A CB  
2272 C CG  . LEU A 293 ? 0.11552 0.11525 0.11930 0.00817  0.01484  -0.01091 293 LEU A CG  
2273 C CD1 . LEU A 293 ? 0.10645 0.10877 0.11508 0.00857  0.01578  -0.01353 293 LEU A CD1 
2274 C CD2 . LEU A 293 ? 0.14762 0.14707 0.14877 0.00656  0.01669  -0.01042 293 LEU A CD2 
2275 N N   . TRP A 294 ? 0.07066 0.06324 0.06297 0.01013  0.01123  -0.00716 294 TRP A N   
2276 C CA  . TRP A 294 ? 0.07499 0.06585 0.06369 0.01050  0.01051  -0.00635 294 TRP A CA  
2277 C C   . TRP A 294 ? 0.08031 0.06919 0.06621 0.01021  0.01030  -0.00431 294 TRP A C   
2278 O O   . TRP A 294 ? 0.09380 0.08124 0.07612 0.00999  0.01045  -0.00342 294 TRP A O   
2279 C CB  . TRP A 294 ? 0.09475 0.08565 0.08542 0.01161  0.00857  -0.00652 294 TRP A CB  
2280 C CG  . TRP A 294 ? 0.09323 0.08542 0.08633 0.01204  0.00873  -0.00861 294 TRP A CG  
2281 C CD1 . TRP A 294 ? 0.07817 0.07154 0.07623 0.01267  0.00795  -0.00954 294 TRP A CD1 
2282 C CD2 . TRP A 294 ? 0.13457 0.12691 0.12546 0.01175  0.00969  -0.01012 294 TRP A CD2 
2283 N NE1 . TRP A 294 ? 0.12008 0.11421 0.11975 0.01299  0.00855  -0.01175 294 TRP A NE1 
2284 C CE2 . TRP A 294 ? 0.12560 0.11924 0.12067 0.01230  0.00976  -0.01232 294 TRP A CE2 
2285 C CE3 . TRP A 294 ? 0.12383 0.11531 0.10958 0.01090  0.01040  -0.00977 294 TRP A CE3 
2286 C CZ2 . TRP A 294 ? 0.18344 0.17764 0.17770 0.01193  0.01090  -0.01462 294 TRP A CZ2 
2287 C CZ3 . TRP A 294 ? 0.16821 0.16038 0.15252 0.01033  0.01129  -0.01176 294 TRP A CZ3 
2288 C CH2 . TRP A 294 ? 0.20655 0.20012 0.19509 0.01080  0.01172  -0.01438 294 TRP A CH2 
2289 N N   . ARG A 295 ? 0.09089 0.07969 0.07859 0.01010  0.00986  -0.00357 295 ARG A N   
2290 C CA  . ARG A 295 ? 0.09249 0.07945 0.07843 0.00976  0.01001  -0.00209 295 ARG A CA  
2291 C C   . ARG A 295 ? 0.09743 0.08340 0.08100 0.00876  0.01176  -0.00167 295 ARG A C   
2292 O O   . ARG A 295 ? 0.10375 0.08765 0.08471 0.00872  0.01179  -0.00035 295 ARG A O   
2293 C CB  . ARG A 295 ? 0.07307 0.06050 0.06134 0.00936  0.00956  -0.00191 295 ARG A CB  
2294 C CG  . ARG A 295 ? 0.06831 0.05400 0.05557 0.00883  0.01010  -0.00096 295 ARG A CG  
2295 C CD  . ARG A 295 ? 0.08648 0.07302 0.07567 0.00800  0.00973  -0.00117 295 ARG A CD  
2296 N NE  . ARG A 295 ? 0.07536 0.06033 0.06405 0.00740  0.01049  -0.00079 295 ARG A NE  
2297 C CZ  . ARG A 295 ? 0.11490 0.09915 0.10331 0.00630  0.01200  -0.00086 295 ARG A CZ  
2298 N NH1 . ARG A 295 ? 0.06399 0.04912 0.05238 0.00561  0.01290  -0.00117 295 ARG A NH1 
2299 N NH2 . ARG A 295 ? 0.07202 0.05468 0.06053 0.00583  0.01275  -0.00080 295 ARG A NH2 
2300 N N   . GLU A 296 ? 0.07483 0.06228 0.05955 0.00787  0.01315  -0.00271 296 GLU A N   
2301 C CA  . GLU A 296 ? 0.10523 0.09183 0.08766 0.00658  0.01501  -0.00241 296 GLU A CA  
2302 C C   . GLU A 296 ? 0.10103 0.08690 0.07978 0.00624  0.01551  -0.00227 296 GLU A C   
2303 O O   . GLU A 296 ? 0.13770 0.12159 0.11311 0.00530  0.01626  -0.00095 296 GLU A O   
2304 C CB  . GLU A 296 ? 0.12121 0.11009 0.10624 0.00561  0.01640  -0.00384 296 GLU A CB  
2305 C CG  . GLU A 296 ? 0.12457 0.11253 0.10786 0.00398  0.01836  -0.00345 296 GLU A CG  
2306 C CD  . GLU A 296 ? 0.10677 0.09347 0.09078 0.00354  0.01827  -0.00252 296 GLU A CD  
2307 O OE1 . GLU A 296 ? 0.11325 0.10010 0.09903 0.00432  0.01679  -0.00232 296 GLU A OE1 
2308 O OE2 . GLU A 296 ? 0.11503 0.10054 0.09776 0.00218  0.01982  -0.00212 296 GLU A OE2 
2309 N N   . PHE A 297 ? 0.07389 0.06125 0.05310 0.00681  0.01506  -0.00360 297 PHE A N   
2310 C CA  . PHE A 297 ? 0.11500 0.10203 0.09038 0.00614  0.01552  -0.00379 297 PHE A CA  
2311 C C   . PHE A 297 ? 0.13755 0.12200 0.10936 0.00642  0.01403  -0.00143 297 PHE A C   
2312 O O   . PHE A 297 ? 0.10578 0.08870 0.07346 0.00518  0.01453  -0.00013 297 PHE A O   
2313 C CB  . PHE A 297 ? 0.09859 0.08764 0.07584 0.00679  0.01521  -0.00596 297 PHE A CB  
2314 C CG  . PHE A 297 ? 0.14218 0.13119 0.11534 0.00584  0.01570  -0.00657 297 PHE A CG  
2315 C CD1 . PHE A 297 ? 0.14699 0.13616 0.11671 0.00381  0.01779  -0.00703 297 PHE A CD1 
2316 C CD2 . PHE A 297 ? 0.11962 0.10856 0.09217 0.00666  0.01412  -0.00680 297 PHE A CD2 
2317 C CE1 . PHE A 297 ? 0.18783 0.17712 0.15316 0.00245  0.01826  -0.00766 297 PHE A CE1 
2318 C CE2 . PHE A 297 ? 0.15377 0.14287 0.12223 0.00546  0.01451  -0.00750 297 PHE A CE2 
2319 C CZ  . PHE A 297 ? 0.18133 0.17062 0.14598 0.00326  0.01657  -0.00792 297 PHE A CZ  
2320 N N   . PHE A 298 ? 0.11014 0.09412 0.08367 0.00793  0.01207  -0.00075 298 PHE A N   
2321 C CA  . PHE A 298 ? 0.12206 0.10401 0.09322 0.00839  0.01045  0.00131  298 PHE A CA  
2322 C C   . PHE A 298 ? 0.12514 0.10463 0.09564 0.00807  0.01068  0.00337  298 PHE A C   
2323 O O   . PHE A 298 ? 0.09136 0.06886 0.05947 0.00805  0.00961  0.00541  298 PHE A O   
2324 C CB  . PHE A 298 ? 0.08965 0.07206 0.06338 0.00996  0.00857  0.00117  298 PHE A CB  
2325 C CG  . PHE A 298 ? 0.08718 0.07137 0.06126 0.01026  0.00807  -0.00057 298 PHE A CG  
2326 C CD1 . PHE A 298 ? 0.11664 0.10138 0.08753 0.00925  0.00867  -0.00135 298 PHE A CD1 
2327 C CD2 . PHE A 298 ? 0.08806 0.07328 0.06556 0.01129  0.00711  -0.00151 298 PHE A CD2 
2328 C CE1 . PHE A 298 ? 0.11985 0.10614 0.09141 0.00943  0.00844  -0.00332 298 PHE A CE1 
2329 C CE2 . PHE A 298 ? 0.11325 0.09977 0.09148 0.01157  0.00667  -0.00313 298 PHE A CE2 
2330 C CZ  . PHE A 298 ? 0.13854 0.12559 0.11401 0.01071  0.00741  -0.00419 298 PHE A CZ  
2331 N N   . TYR A 299 ? 0.13554 0.11509 0.10833 0.00775  0.01195  0.00291  299 TYR A N   
2332 C CA  . TYR A 299 ? 0.14904 0.12610 0.12135 0.00721  0.01255  0.00452  299 TYR A CA  
2333 C C   . TYR A 299 ? 0.14168 0.11753 0.11009 0.00549  0.01380  0.00544  299 TYR A C   
2334 O O   . TYR A 299 ? 0.13640 0.10940 0.10293 0.00511  0.01343  0.00766  299 TYR A O   
2335 C CB  . TYR A 299 ? 0.10058 0.07825 0.07618 0.00699  0.01364  0.00350  299 TYR A CB  
2336 C CG  . TYR A 299 ? 0.12688 0.10390 0.10527 0.00803  0.01266  0.00370  299 TYR A CG  
2337 C CD1 . TYR A 299 ? 0.10859 0.08729 0.08889 0.00905  0.01138  0.00282  299 TYR A CD1 
2338 C CD2 . TYR A 299 ? 0.12146 0.09614 0.10072 0.00780  0.01322  0.00458  299 TYR A CD2 
2339 C CE1 . TYR A 299 ? 0.12322 0.10155 0.10587 0.00962  0.01078  0.00277  299 TYR A CE1 
2340 C CE2 . TYR A 299 ? 0.15001 0.12434 0.13207 0.00852  0.01273  0.00428  299 TYR A CE2 
2341 C CZ  . TYR A 299 ? 0.12071 0.09700 0.10429 0.00933  0.01156  0.00334  299 TYR A CZ  
2342 O OH  . TYR A 299 ? 0.14498 0.12113 0.13113 0.00967  0.01135  0.00282  299 TYR A OH  
2343 N N   . THR A 300 ? 0.13658 0.11452 0.10395 0.00434  0.01530  0.00376  300 THR A N   
2344 C CA  . THR A 300 ? 0.15294 0.13006 0.11627 0.00225  0.01683  0.00434  300 THR A CA  
2345 C C   . THR A 300 ? 0.14812 0.12381 0.10674 0.00173  0.01548  0.00613  300 THR A C   
2346 O O   . THR A 300 ? 0.21452 0.18763 0.16954 0.00038  0.01548  0.00843  300 THR A O   
2347 C CB  . THR A 300 ? 0.13658 0.11682 0.10067 0.00113  0.01895  0.00158  300 THR A CB  
2348 O OG1 . THR A 300 ? 0.13689 0.11887 0.10591 0.00186  0.01947  0.00008  300 THR A OG1 
2349 C CG2 . THR A 300 ? 0.13840 0.11796 0.09877 -0.00143 0.02109  0.00190  300 THR A CG2 
2350 N N   . VAL A 301 ? 0.15215 0.12938 0.11066 0.00264  0.01416  0.00526  301 VAL A N   
2351 C CA  . VAL A 301 ? 0.19882 0.17510 0.15275 0.00195  0.01263  0.00686  301 VAL A CA  
2352 C C   . VAL A 301 ? 0.16492 0.13846 0.11922 0.00324  0.01007  0.00992  301 VAL A C   
2353 O O   . VAL A 301 ? 0.18126 0.15252 0.13176 0.00218  0.00897  0.01264  301 VAL A O   
2354 C CB  . VAL A 301 ? 0.18008 0.15898 0.13410 0.00239  0.01213  0.00463  301 VAL A CB  
2355 C CG1 . VAL A 301 ? 0.21631 0.19457 0.16504 0.00120  0.01058  0.00611  301 VAL A CG1 
2356 C CG2 . VAL A 301 ? 0.16420 0.14585 0.11932 0.00141  0.01473  0.00131  301 VAL A CG2 
2357 N N   . GLY A 302 ? 0.15879 0.13255 0.11789 0.00541  0.00907  0.00953  302 GLY A N   
2358 C CA  . GLY A 302 ? 0.15313 0.12483 0.11364 0.00681  0.00674  0.01188  302 GLY A CA  
2359 C C   . GLY A 302 ? 0.17371 0.14205 0.13406 0.00637  0.00688  0.01435  302 GLY A C   
2360 O O   . GLY A 302 ? 0.16371 0.12980 0.12323 0.00668  0.00482  0.01710  302 GLY A O   
2361 N N   . SER A 303 ? 0.19147 0.15939 0.15296 0.00562  0.00917  0.01345  303 SER A N   
2362 C CA  . SER A 303 ? 0.16885 0.13334 0.13051 0.00506  0.00957  0.01554  303 SER A CA  
2363 C C   . SER A 303 ? 0.19475 0.15709 0.15088 0.00298  0.00934  0.01808  303 SER A C   
2364 O O   . SER A 303 ? 0.24629 0.20507 0.20227 0.00274  0.00859  0.02081  303 SER A O   
2365 C CB  . SER A 303 ? 0.24901 0.21390 0.21310 0.00447  0.01216  0.01367  303 SER A CB  
2366 O OG  . SER A 303 ? 0.17784 0.14511 0.13975 0.00287  0.01409  0.01182  303 SER A OG  
2367 N N   . THR A 304 ? 0.15115 0.11546 0.10280 0.00129  0.00999  0.01722  304 THR A N   
2368 C CA  . THR A 304 ? 0.20554 0.16814 0.15104 -0.00132 0.01001  0.01942  304 THR A CA  
2369 C C   . THR A 304 ? 0.18964 0.15241 0.13124 -0.00165 0.00735  0.02115  304 THR A C   
2370 O O   . THR A 304 ? 0.18623 0.14817 0.12175 -0.00427 0.00725  0.02278  304 THR A O   
2371 C CB  . THR A 304 ? 0.25367 0.21847 0.19648 -0.00371 0.01318  0.01696  304 THR A CB  
2372 O OG1 . THR A 304 ? 0.13534 0.10405 0.07889 -0.00321 0.01372  0.01376  304 THR A OG1 
2373 C CG2 . THR A 304 ? 0.15835 0.12295 0.10478 -0.00372 0.01557  0.01560  304 THR A CG2 
2374 N N   . THR A 305 ? 0.18434 0.14829 0.12906 0.00067  0.00519  0.02083  305 THR A N   
2375 C CA  . THR A 305 ? 0.24997 0.21446 0.19149 0.00043  0.00245  0.02229  305 THR A CA  
2376 C C   . THR A 305 ? 0.24803 0.21021 0.19276 0.00245  -0.00084 0.02538  305 THR A C   
2377 O O   . THR A 305 ? 0.21408 0.17683 0.16488 0.00502  -0.00119 0.02422  305 THR A O   
2378 C CB  . THR A 305 ? 0.21215 0.18047 0.15466 0.00120  0.00273  0.01893  305 THR A CB  
2379 O OG1 . THR A 305 ? 0.22451 0.19500 0.16473 -0.00063 0.00576  0.01597  305 THR A OG1 
2380 C CG2 . THR A 305 ? 0.21473 0.18372 0.15398 0.00080  -0.00015 0.02030  305 THR A CG2 
2381 N N   . PRO A 306 ? 0.25992 0.21957 0.20108 0.00129  -0.00333 0.02928  306 PRO A N   
2382 C CA  . PRO A 306 ? 0.28616 0.24375 0.23141 0.00341  -0.00671 0.03226  306 PRO A CA  
2383 C C   . PRO A 306 ? 0.23865 0.19906 0.18583 0.00501  -0.00905 0.03140  306 PRO A C   
2384 O O   . PRO A 306 ? 0.23377 0.19675 0.17662 0.00365  -0.00924 0.03015  306 PRO A O   
2385 C CB  . PRO A 306 ? 0.33389 0.28820 0.27389 0.00122  -0.00892 0.03689  306 PRO A CB  
2386 C CG  . PRO A 306 ? 0.31580 0.27180 0.24769 -0.00223 -0.00738 0.03592  306 PRO A CG  
2387 C CD  . PRO A 306 ? 0.26519 0.22371 0.19857 -0.00220 -0.00318 0.03126  306 PRO A CD  
2388 N N   . ASN A 307 ? 0.24965 0.20960 0.20368 0.00782  -0.01066 0.03184  307 ASN A N   
2389 C CA  . ASN A 307 ? 0.21453 0.17712 0.17153 0.00953  -0.01285 0.03098  307 ASN A CA  
2390 C C   . ASN A 307 ? 0.21782 0.18407 0.17446 0.00951  -0.01066 0.02671  307 ASN A C   
2391 O O   . ASN A 307 ? 0.24790 0.21663 0.20331 0.00946  -0.01208 0.02584  307 ASN A O   
2392 C CB  . ASN A 307 ? 0.23748 0.20004 0.19043 0.00842  -0.01669 0.03423  307 ASN A CB  
2393 C CG  . ASN A 307 ? 0.27456 0.23325 0.22812 0.00843  -0.01938 0.03898  307 ASN A CG  
2394 O OD1 . ASN A 307 ? 0.26944 0.22601 0.22953 0.01053  -0.01945 0.03968  307 ASN A OD1 
2395 N ND2 . ASN A 307 ? 0.22595 0.18361 0.17270 0.00589  -0.02161 0.04224  307 ASN A ND2 
2396 N N   . PHE A 308 ? 0.22044 0.18695 0.17844 0.00952  -0.00731 0.02409  308 PHE A N   
2397 C CA  . PHE A 308 ? 0.21453 0.18416 0.17250 0.00945  -0.00529 0.02030  308 PHE A CA  
2398 C C   . PHE A 308 ? 0.22105 0.19275 0.18389 0.01152  -0.00642 0.01873  308 PHE A C   
2399 O O   . PHE A 308 ? 0.23228 0.20651 0.19426 0.01133  -0.00617 0.01647  308 PHE A O   
2400 C CB  . PHE A 308 ? 0.19151 0.16092 0.15077 0.00914  -0.00195 0.01829  308 PHE A CB  
2401 C CG  . PHE A 308 ? 0.17737 0.14977 0.13710 0.00906  -0.00006 0.01471  308 PHE A CG  
2402 C CD1 . PHE A 308 ? 0.20460 0.17846 0.15988 0.00721  0.00114  0.01334  308 PHE A CD1 
2403 C CD2 . PHE A 308 ? 0.14254 0.11620 0.10730 0.01067  0.00055  0.01270  308 PHE A CD2 
2404 C CE1 . PHE A 308 ? 0.16358 0.14000 0.12023 0.00732  0.00276  0.01006  308 PHE A CE1 
2405 C CE2 . PHE A 308 ? 0.13062 0.10669 0.09609 0.01060  0.00191  0.00983  308 PHE A CE2 
2406 C CZ  . PHE A 308 ? 0.18124 0.15863 0.14305 0.00909  0.00295  0.00853  308 PHE A CZ  
2407 N N   . HIS A 309 ? 0.24705 0.21768 0.21522 0.01337  -0.00754 0.01973  309 HIS A N   
2408 C CA  . HIS A 309 ? 0.22461 0.19723 0.19771 0.01513  -0.00842 0.01820  309 HIS A CA  
2409 C C   . HIS A 309 ? 0.25659 0.23032 0.22938 0.01551  -0.01171 0.01967  309 HIS A C   
2410 O O   . HIS A 309 ? 0.29924 0.27469 0.27633 0.01688  -0.01263 0.01856  309 HIS A O   
2411 C CB  . HIS A 309 ? 0.23588 0.20719 0.21522 0.01672  -0.00784 0.01817  309 HIS A CB  
2412 C CG  . HIS A 309 ? 0.30416 0.27276 0.28530 0.01734  -0.00973 0.02135  309 HIS A CG  
2413 N ND1 . HIS A 309 ? 0.28287 0.24839 0.26191 0.01641  -0.00903 0.02330  309 HIS A ND1 
2414 C CD2 . HIS A 309 ? 0.29658 0.26499 0.28198 0.01883  -0.01233 0.02295  309 HIS A CD2 
2415 C CE1 . HIS A 309 ? 0.24594 0.20919 0.22779 0.01734  -0.01133 0.02620  309 HIS A CE1 
2416 N NE2 . HIS A 309 ? 0.29715 0.26222 0.28317 0.01891  -0.01339 0.02600  309 HIS A NE2 
2417 N N   . ARG A 310 ? 0.21152 0.18444 0.17927 0.01409  -0.01354 0.02213  310 ARG A N   
2418 C CA  . ARG A 310 ? 0.23142 0.20537 0.19852 0.01416  -0.01708 0.02397  310 ARG A CA  
2419 C C   . ARG A 310 ? 0.23837 0.21361 0.19805 0.01170  -0.01739 0.02371  310 ARG A C   
2420 O O   . ARG A 310 ? 0.26887 0.24380 0.22415 0.00998  -0.01492 0.02254  310 ARG A O   
2421 C CB  . ARG A 310 ? 0.27514 0.24650 0.24390 0.01473  -0.01987 0.02807  310 ARG A CB  
2422 C CG  . ARG A 310 ? 0.32770 0.30009 0.30294 0.01687  -0.02278 0.02896  310 ARG A CG  
2423 C CD  . ARG A 310 ? 0.32807 0.29921 0.30176 0.01641  -0.02695 0.03335  310 ARG A CD  
2424 N NE  . ARG A 310 ? 0.35205 0.31933 0.32334 0.01551  -0.02683 0.03634  310 ARG A NE  
2425 C CZ  . ARG A 310 ? 0.30786 0.27326 0.27537 0.01417  -0.03004 0.04061  310 ARG A CZ  
2426 N NH1 . ARG A 310 ? 0.30998 0.27718 0.27545 0.01351  -0.03378 0.04246  310 ARG A NH1 
2427 N NH2 . ARG A 310 ? 0.30084 0.26243 0.26634 0.01326  -0.02957 0.04319  310 ARG A NH2 
2428 N N   . MET A 311 ? 0.22190 0.19882 0.18044 0.01140  -0.02038 0.02461  311 MET A N   
2429 C CA  . MET A 311 ? 0.23867 0.21696 0.18999 0.00875  -0.02092 0.02433  311 MET A CA  
2430 C C   . MET A 311 ? 0.23654 0.21283 0.18229 0.00669  -0.02318 0.02839  311 MET A C   
2431 O O   . MET A 311 ? 0.30619 0.28179 0.24551 0.00409  -0.02152 0.02833  311 MET A O   
2432 C CB  . MET A 311 ? 0.25665 0.23793 0.20900 0.00902  -0.02295 0.02301  311 MET A CB  
2433 C CG  . MET A 311 ? 0.22247 0.20555 0.16781 0.00618  -0.02270 0.02145  311 MET A CG  
2434 S SD  . MET A 311 ? 0.34906 0.33547 0.29533 0.00617  -0.02545 0.02021  311 MET A SD  
2435 C CE  . MET A 311 ? 0.23619 0.22200 0.18259 0.00623  -0.03071 0.02545  311 MET A CE  
2436 N N   . ALA A 312 ? 0.24695 0.22238 0.19528 0.00768  -0.02702 0.03198  312 ALA A N   
2437 C CA  . ALA A 312 ? 0.29167 0.26488 0.23500 0.00572  -0.02976 0.03649  312 ALA A CA  
2438 C C   . ALA A 312 ? 0.28597 0.25551 0.22887 0.00550  -0.02775 0.03802  312 ALA A C   
2439 O O   . ALA A 312 ? 0.29779 0.26595 0.24726 0.00796  -0.02630 0.03738  312 ALA A O   
2440 C CB  . ALA A 312 ? 0.29060 0.26373 0.23826 0.00724  -0.03465 0.04010  312 ALA A CB  
2441 N N   . GLY A 313 ? 0.32080 0.28887 0.25576 0.00225  -0.02747 0.03986  313 GLY A N   
2442 C CA  . GLY A 313 ? 0.32502 0.28975 0.25863 0.00146  -0.02526 0.04108  313 GLY A CA  
2443 C C   . GLY A 313 ? 0.30149 0.26709 0.23438 0.00099  -0.02019 0.03677  313 GLY A C   
2444 O O   . GLY A 313 ? 0.31151 0.27474 0.24228 -0.00026 -0.01806 0.03746  313 GLY A O   
2445 N N   . ASN A 314 ? 0.28649 0.25535 0.22136 0.00191  -0.01833 0.03246  314 ASN A N   
2446 C CA  . ASN A 314 ? 0.26516 0.23512 0.19984 0.00151  -0.01389 0.02843  314 ASN A CA  
2447 C C   . ASN A 314 ? 0.24863 0.21997 0.17533 -0.00210 -0.01229 0.02706  314 ASN A C   
2448 O O   . ASN A 314 ? 0.26835 0.24196 0.19193 -0.00328 -0.01355 0.02612  314 ASN A O   
2449 C CB  . ASN A 314 ? 0.28605 0.25866 0.22653 0.00395  -0.01283 0.02467  314 ASN A CB  
2450 C CG  . ASN A 314 ? 0.24758 0.22088 0.18991 0.00422  -0.00875 0.02111  314 ASN A CG  
2451 O OD1 . ASN A 314 ? 0.27990 0.25235 0.21884 0.00238  -0.00643 0.02083  314 ASN A OD1 
2452 N ND2 . ASN A 314 ? 0.21222 0.18718 0.16001 0.00638  -0.00800 0.01846  314 ASN A ND2 
2453 N N   . PRO A 315 ? 0.29480 0.26499 0.21808 -0.00413 -0.00938 0.02665  315 PRO A N   
2454 C CA  . PRO A 315 ? 0.25854 0.23034 0.17439 -0.00784 -0.00745 0.02489  315 PRO A CA  
2455 C C   . PRO A 315 ? 0.24771 0.22298 0.16527 -0.00754 -0.00462 0.01959  315 PRO A C   
2456 O O   . PRO A 315 ? 0.31610 0.29348 0.22883 -0.00995 -0.00417 0.01771  315 PRO A O   
2457 C CB  . PRO A 315 ? 0.23373 0.20324 0.14676 -0.00981 -0.00503 0.02598  315 PRO A CB  
2458 C CG  . PRO A 315 ? 0.25345 0.22131 0.17394 -0.00659 -0.00424 0.02603  315 PRO A CG  
2459 C CD  . PRO A 315 ? 0.34128 0.30861 0.26698 -0.00350 -0.00783 0.02795  315 PRO A CD  
2460 N N   . VAL A 316 ? 0.25540 0.23125 0.17975 -0.00478 -0.00274 0.01710  316 VAL A N   
2461 C CA  . VAL A 316 ? 0.23803 0.21682 0.16470 -0.00436 -0.00021 0.01234  316 VAL A CA  
2462 C C   . VAL A 316 ? 0.22168 0.20227 0.15111 -0.00268 -0.00220 0.01107  316 VAL A C   
2463 O O   . VAL A 316 ? 0.21409 0.19691 0.14533 -0.00245 -0.00047 0.00727  316 VAL A O   
2464 C CB  . VAL A 316 ? 0.23970 0.21849 0.17233 -0.00239 0.00238  0.01037  316 VAL A CB  
2465 C CG1 . VAL A 316 ? 0.26064 0.23765 0.19111 -0.00400 0.00438  0.01159  316 VAL A CG1 
2466 C CG2 . VAL A 316 ? 0.21638 0.19433 0.15547 0.00098  0.00056  0.01146  316 VAL A CG2 
2467 N N   . CYS A 317 ? 0.19990 0.17961 0.13013 -0.00151 -0.00580 0.01408  317 CYS A N   
2468 C CA  . CYS A 317 ? 0.22837 0.20980 0.16193 0.00021  -0.00776 0.01302  317 CYS A CA  
2469 C C   . CYS A 317 ? 0.21776 0.20046 0.14573 -0.00208 -0.00998 0.01363  317 CYS A C   
2470 O O   . CYS A 317 ? 0.23429 0.21576 0.15729 -0.00397 -0.01201 0.01699  317 CYS A O   
2471 C CB  . CYS A 317 ? 0.18827 0.16845 0.12766 0.00316  -0.01016 0.01544  317 CYS A CB  
2472 S SG  . CYS A 317 ? 0.22115 0.20362 0.16537 0.00524  -0.01217 0.01386  317 CYS A SG  
2473 N N   . LYS A 318 ? 0.23290 0.21800 0.16166 -0.00207 -0.00969 0.01044  318 LYS A N   
2474 C CA  . LYS A 318 ? 0.27940 0.26609 0.20317 -0.00433 -0.01170 0.01042  318 LYS A CA  
2475 C C   . LYS A 318 ? 0.21155 0.19826 0.13777 -0.00274 -0.01601 0.01345  318 LYS A C   
2476 O O   . LYS A 318 ? 0.23065 0.21739 0.16366 0.00031  -0.01665 0.01327  318 LYS A O   
2477 C CB  . LYS A 318 ? 0.24198 0.23108 0.16631 -0.00490 -0.00957 0.00554  318 LYS A CB  
2478 C CG  . LYS A 318 ? 0.30016 0.29111 0.21877 -0.00781 -0.01098 0.00472  318 LYS A CG  
2479 C CD  . LYS A 318 ? 0.38928 0.38202 0.30682 -0.00947 -0.00745 -0.00051 318 LYS A CD  
2480 C CE  . LYS A 318 ? 0.36596 0.35809 0.28178 -0.01080 -0.00364 -0.00196 318 LYS A CE  
2481 N NZ  . LYS A 318 ? 0.41331 0.40731 0.32437 -0.01431 -0.00077 -0.00604 318 LYS A NZ  
2482 N N   . GLN A 319 ? 0.24237 0.22920 0.16308 -0.00501 -0.01902 0.01626  319 GLN A N   
2483 C CA  . GLN A 319 ? 0.28043 0.26754 0.20351 -0.00373 -0.02354 0.01945  319 GLN A CA  
2484 C C   . GLN A 319 ? 0.25900 0.24910 0.18197 -0.00431 -0.02458 0.01681  319 GLN A C   
2485 O O   . GLN A 319 ? 0.32431 0.31583 0.24066 -0.00759 -0.02522 0.01623  319 GLN A O   
2486 C CB  . GLN A 319 ? 0.30459 0.29019 0.22215 -0.00589 -0.02677 0.02433  319 GLN A CB  
2487 C CG  . GLN A 319 ? 0.34172 0.32424 0.25720 -0.00652 -0.02511 0.02648  319 GLN A CG  
2488 C CD  . GLN A 319 ? 0.28500 0.26547 0.20849 -0.00277 -0.02432 0.02722  319 GLN A CD  
2489 O OE1 . GLN A 319 ? 0.24606 0.22640 0.17569 -0.00004 -0.02693 0.02888  319 GLN A OE1 
2490 N NE2 . GLN A 319 ? 0.29177 0.27082 0.21535 -0.00279 -0.02061 0.02579  319 GLN A NE2 
2491 N N   . ILE A 320 ? 0.24708 0.23815 0.17721 -0.00140 -0.02463 0.01508  320 ILE A N   
2492 C CA  . ILE A 320 ? 0.26830 0.26202 0.19938 -0.00168 -0.02535 0.01233  320 ILE A CA  
2493 C C   . ILE A 320 ? 0.27941 0.27409 0.21491 0.00006  -0.02951 0.01493  320 ILE A C   
2494 O O   . ILE A 320 ? 0.27218 0.26556 0.21312 0.00267  -0.03055 0.01729  320 ILE A O   
2495 C CB  . ILE A 320 ? 0.24483 0.23897 0.18057 -0.00007 -0.02185 0.00795  320 ILE A CB  
2496 C CG1 . ILE A 320 ? 0.26248 0.25570 0.19518 -0.00142 -0.01782 0.00560  320 ILE A CG1 
2497 C CG2 . ILE A 320 ? 0.28384 0.28036 0.22013 -0.00073 -0.02238 0.00498  320 ILE A CG2 
2498 C CD1 . ILE A 320 ? 0.25738 0.25075 0.19504 0.00021  -0.01466 0.00179  320 ILE A CD1 
2499 N N   . ASP A 321 ? 0.32099 0.31813 0.25448 -0.00148 -0.03183 0.01430  321 ASP A N   
2500 C CA  . ASP A 321 ? 0.32651 0.32502 0.26389 -0.00023 -0.03630 0.01708  321 ASP A CA  
2501 C C   . ASP A 321 ? 0.24007 0.23979 0.18563 0.00262  -0.03556 0.01463  321 ASP A C   
2502 O O   . ASP A 321 ? 0.34916 0.35134 0.29629 0.00237  -0.03770 0.01390  321 ASP A O   
2503 C CB  . ASP A 321 ? 0.37102 0.37200 0.30245 -0.00348 -0.03923 0.01733  321 ASP A CB  
2504 C CG  . ASP A 321 ? 0.50720 0.50748 0.43216 -0.00595 -0.04254 0.02186  321 ASP A CG  
2505 O OD1 . ASP A 321 ? 0.56527 0.56294 0.48689 -0.00661 -0.04109 0.02357  321 ASP A OD1 
2506 O OD2 . ASP A 321 ? 0.60772 0.61006 0.53094 -0.00739 -0.04671 0.02384  321 ASP A OD2 
2507 N N   . TRP A 322 ? 0.23316 0.23118 0.18377 0.00510  -0.03272 0.01364  322 TRP A N   
2508 C CA  . TRP A 322 ? 0.22991 0.22880 0.18810 0.00758  -0.03204 0.01183  322 TRP A CA  
2509 C C   . TRP A 322 ? 0.24183 0.24282 0.20480 0.00867  -0.03583 0.01357  322 TRP A C   
2510 O O   . TRP A 322 ? 0.21055 0.21152 0.17307 0.00859  -0.03914 0.01715  322 TRP A O   
2511 C CB  . TRP A 322 ? 0.21795 0.21460 0.18056 0.00987  -0.02960 0.01206  322 TRP A CB  
2512 C CG  . TRP A 322 ? 0.19934 0.19409 0.15820 0.00902  -0.02612 0.01067  322 TRP A CG  
2513 C CD1 . TRP A 322 ? 0.20305 0.19558 0.15914 0.00865  -0.02532 0.01269  322 TRP A CD1 
2514 C CD2 . TRP A 322 ? 0.22895 0.22391 0.18692 0.00841  -0.02300 0.00694  322 TRP A CD2 
2515 N NE1 . TRP A 322 ? 0.22680 0.21848 0.18038 0.00782  -0.02181 0.01029  322 TRP A NE1 
2516 C CE2 . TRP A 322 ? 0.18679 0.17994 0.14174 0.00776  -0.02043 0.00678  322 TRP A CE2 
2517 C CE3 . TRP A 322 ? 0.21937 0.21581 0.17919 0.00833  -0.02222 0.00378  322 TRP A CE3 
2518 C CZ2 . TRP A 322 ? 0.15596 0.14897 0.11023 0.00722  -0.01723 0.00354  322 TRP A CZ2 
2519 C CZ3 . TRP A 322 ? 0.17310 0.16898 0.13208 0.00781  -0.01912 0.00074  322 TRP A CZ3 
2520 C CH2 . TRP A 322 ? 0.20588 0.20019 0.16237 0.00735  -0.01671 0.00061  322 TRP A CH2 
2521 N N   . ASP A 323 ? 0.26493 0.26773 0.23284 0.00965  -0.03545 0.01114  323 ASP A N   
2522 C CA  . ASP A 323 ? 0.24643 0.25179 0.21939 0.01052  -0.03875 0.01214  323 ASP A CA  
2523 C C   . ASP A 323 ? 0.25396 0.25879 0.23478 0.01336  -0.03897 0.01360  323 ASP A C   
2524 O O   . ASP A 323 ? 0.25799 0.26081 0.24092 0.01464  -0.03598 0.01279  323 ASP A O   
2525 C CB  . ASP A 323 ? 0.29287 0.30054 0.26756 0.00994  -0.03813 0.00869  323 ASP A CB  
2526 C CG  . ASP A 323 ? 0.25118 0.25970 0.21891 0.00702  -0.03812 0.00688  323 ASP A CG  
2527 O OD1 . ASP A 323 ? 0.23516 0.24359 0.19697 0.00517  -0.03987 0.00881  323 ASP A OD1 
2528 O OD2 . ASP A 323 ? 0.21854 0.22773 0.18667 0.00640  -0.03630 0.00347  323 ASP A OD2 
2529 N N   . ASP A 324 ? 0.26072 0.26757 0.24614 0.01423  -0.04256 0.01561  324 ASP A N   
2530 C CA  . ASP A 324 ? 0.26298 0.27008 0.25723 0.01688  -0.04287 0.01636  324 ASP A CA  
2531 C C   . ASP A 324 ? 0.30296 0.31335 0.30265 0.01723  -0.04298 0.01372  324 ASP A C   
2532 O O   . ASP A 324 ? 0.25515 0.26845 0.25741 0.01706  -0.04640 0.01459  324 ASP A O   
2533 C CB  . ASP A 324 ? 0.31940 0.32632 0.31607 0.01779  -0.04687 0.02061  324 ASP A CB  
2534 C CG  . ASP A 324 ? 0.33476 0.34149 0.34110 0.02064  -0.04668 0.02111  324 ASP A CG  
2535 O OD1 . ASP A 324 ? 0.32426 0.33106 0.33465 0.02162  -0.04326 0.01813  324 ASP A OD1 
2536 O OD2 . ASP A 324 ? 0.38454 0.39102 0.39453 0.02177  -0.04997 0.02449  324 ASP A OD2 
2537 N N   . ASN A 325 ? 0.27778 0.28776 0.27914 0.01752  -0.03931 0.01056  325 ASN A N   
2538 C CA  . ASN A 325 ? 0.27481 0.28750 0.28052 0.01742  -0.03879 0.00779  325 ASN A CA  
2539 C C   . ASN A 325 ? 0.23385 0.24607 0.24600 0.01905  -0.03604 0.00643  325 ASN A C   
2540 O O   . ASN A 325 ? 0.24230 0.25265 0.25271 0.01876  -0.03265 0.00462  325 ASN A O   
2541 C CB  . ASN A 325 ? 0.25360 0.26617 0.25387 0.01541  -0.03705 0.00508  325 ASN A CB  
2542 C CG  . ASN A 325 ? 0.29643 0.31207 0.29995 0.01469  -0.03770 0.00282  325 ASN A CG  
2543 O OD1 . ASN A 325 ? 0.35858 0.37542 0.35826 0.01286  -0.03883 0.00182  325 ASN A OD1 
2544 N ND2 . ASN A 325 ? 0.27339 0.29037 0.28398 0.01587  -0.03682 0.00180  325 ASN A ND2 
2545 N N   . PRO A 326 ? 0.26237 0.27637 0.28224 0.02065  -0.03741 0.00717  326 PRO A N   
2546 C CA  . PRO A 326 ? 0.26322 0.27702 0.28925 0.02184  -0.03448 0.00545  326 PRO A CA  
2547 C C   . PRO A 326 ? 0.22212 0.23749 0.24944 0.02073  -0.03213 0.00209  326 PRO A C   
2548 O O   . PRO A 326 ? 0.21309 0.22783 0.24327 0.02097  -0.02910 0.00042  326 PRO A O   
2549 C CB  . PRO A 326 ? 0.24899 0.26485 0.28351 0.02368  -0.03690 0.00683  326 PRO A CB  
2550 C CG  . PRO A 326 ? 0.22130 0.23736 0.25312 0.02365  -0.04123 0.01021  326 PRO A CG  
2551 C CD  . PRO A 326 ? 0.24791 0.26424 0.27154 0.02137  -0.04171 0.00957  326 PRO A CD  
2552 N N   . GLU A 327 ? 0.24342 0.26073 0.26855 0.01929  -0.03345 0.00107  327 GLU A N   
2553 C CA  A GLU A 327 ? 0.26411 0.28258 0.29023 0.01801  -0.03136 -0.00191 327 GLU A CA  
2554 C CA  B GLU A 327 ? 0.26335 0.28183 0.28942 0.01800  -0.03138 -0.00191 327 GLU A CA  
2555 C C   . GLU A 327 ? 0.24939 0.26475 0.26952 0.01690  -0.02850 -0.00304 327 GLU A C   
2556 O O   . GLU A 327 ? 0.21211 0.22703 0.23361 0.01632  -0.02587 -0.00487 327 GLU A O   
2557 C CB  A GLU A 327 ? 0.24279 0.26435 0.26909 0.01678  -0.03380 -0.00269 327 GLU A CB  
2558 C CB  B GLU A 327 ? 0.24369 0.26518 0.26967 0.01674  -0.03384 -0.00265 327 GLU A CB  
2559 C CG  A GLU A 327 ? 0.26829 0.29374 0.30227 0.01774  -0.03639 -0.00224 327 GLU A CG  
2560 C CG  B GLU A 327 ? 0.26567 0.29000 0.29555 0.01767  -0.03781 -0.00066 327 GLU A CG  
2561 C CD  A GLU A 327 ? 0.28549 0.31095 0.32049 0.01926  -0.03967 0.00107  327 GLU A CD  
2562 C CD  B GLU A 327 ? 0.28831 0.31516 0.31576 0.01603  -0.04060 -0.00096 327 GLU A CD  
2563 O OE1 A GLU A 327 ? 0.31766 0.34098 0.34582 0.01877  -0.04085 0.00299  327 GLU A OE1 
2564 O OE1 B GLU A 327 ? 0.29827 0.32519 0.32309 0.01430  -0.03912 -0.00335 327 GLU A OE1 
2565 O OE2 A GLU A 327 ? 0.30672 0.33430 0.34955 0.02086  -0.04103 0.00176  327 GLU A OE2 
2566 O OE2 B GLU A 327 ? 0.31404 0.34271 0.34220 0.01633  -0.04440 0.00127  327 GLU A OE2 
2567 N N   . PHE A 328 ? 0.28094 0.29423 0.29458 0.01645  -0.02901 -0.00195 328 PHE A N   
2568 C CA  . PHE A 328 ? 0.19895 0.20940 0.20778 0.01563  -0.02640 -0.00300 328 PHE A CA  
2569 C C   . PHE A 328 ? 0.17115 0.17933 0.18082 0.01665  -0.02405 -0.00244 328 PHE A C   
2570 O O   . PHE A 328 ? 0.16828 0.17487 0.17685 0.01608  -0.02160 -0.00368 328 PHE A O   
2571 C CB  . PHE A 328 ? 0.24114 0.25038 0.24334 0.01475  -0.02734 -0.00239 328 PHE A CB  
2572 C CG  . PHE A 328 ? 0.26627 0.27724 0.26655 0.01315  -0.02878 -0.00380 328 PHE A CG  
2573 C CD1 . PHE A 328 ? 0.24506 0.25757 0.24854 0.01243  -0.02837 -0.00583 328 PHE A CD1 
2574 C CD2 . PHE A 328 ? 0.23094 0.24200 0.22600 0.01207  -0.03041 -0.00322 328 PHE A CD2 
2575 C CE1 . PHE A 328 ? 0.27927 0.29326 0.28111 0.01084  -0.02962 -0.00726 328 PHE A CE1 
2576 C CE2 . PHE A 328 ? 0.20947 0.22217 0.20265 0.01036  -0.03159 -0.00480 328 PHE A CE2 
2577 C CZ  . PHE A 328 ? 0.23822 0.25233 0.23498 0.00983  -0.03122 -0.00685 328 PHE A CZ  
2578 N N   . LEU A 329 ? 0.16033 0.16824 0.17204 0.01805  -0.02491 -0.00048 329 LEU A N   
2579 C CA  . LEU A 329 ? 0.17451 0.18038 0.18750 0.01891  -0.02264 -0.00015 329 LEU A CA  
2580 C C   . LEU A 329 ? 0.15167 0.15872 0.17000 0.01885  -0.02065 -0.00204 329 LEU A C   
2581 O O   . LEU A 329 ? 0.19188 0.19741 0.20927 0.01829  -0.01805 -0.00302 329 LEU A O   
2582 C CB  . LEU A 329 ? 0.18501 0.19014 0.19944 0.02037  -0.02416 0.00239  329 LEU A CB  
2583 C CG  . LEU A 329 ? 0.18649 0.18867 0.19977 0.02101  -0.02219 0.00331  329 LEU A CG  
2584 C CD1 . LEU A 329 ? 0.22466 0.22694 0.24336 0.02153  -0.01977 0.00186  329 LEU A CD1 
2585 C CD2 . LEU A 329 ? 0.15265 0.15271 0.15938 0.01988  -0.02050 0.00286  329 LEU A CD2 
2586 N N   . ALA A 330 ? 0.18439 0.19436 0.20836 0.01919  -0.02187 -0.00263 330 ALA A N   
2587 C CA  . ALA A 330 ? 0.18083 0.19228 0.21007 0.01883  -0.01974 -0.00471 330 ALA A CA  
2588 C C   . ALA A 330 ? 0.17652 0.18773 0.20303 0.01684  -0.01791 -0.00662 330 ALA A C   
2589 O O   . ALA A 330 ? 0.17057 0.18111 0.19774 0.01598  -0.01530 -0.00783 330 ALA A O   
2590 C CB  . ALA A 330 ? 0.16099 0.17603 0.19725 0.01951  -0.02147 -0.00518 330 ALA A CB  
2591 N N   . ALA A 331 ? 0.14954 0.16119 0.17290 0.01590  -0.01932 -0.00686 331 ALA A N   
2592 C CA  . ALA A 331 ? 0.12804 0.13902 0.14902 0.01404  -0.01788 -0.00843 331 ALA A CA  
2593 C C   . ALA A 331 ? 0.14731 0.15497 0.16376 0.01369  -0.01606 -0.00803 331 ALA A C   
2594 O O   . ALA A 331 ? 0.10129 0.10810 0.11734 0.01237  -0.01422 -0.00898 331 ALA A O   
2595 C CB  . ALA A 331 ? 0.15184 0.16371 0.17063 0.01318  -0.01980 -0.00886 331 ALA A CB  
2596 N N   . TRP A 332 ? 0.15979 0.16564 0.17279 0.01470  -0.01666 -0.00655 332 TRP A N   
2597 C CA  . TRP A 332 ? 0.11697 0.11999 0.12628 0.01452  -0.01502 -0.00619 332 TRP A CA  
2598 C C   . TRP A 332 ? 0.16776 0.17014 0.17915 0.01478  -0.01306 -0.00605 332 TRP A C   
2599 O O   . TRP A 332 ? 0.14989 0.15082 0.15977 0.01384  -0.01135 -0.00644 332 TRP A O   
2600 C CB  . TRP A 332 ? 0.16016 0.16180 0.16544 0.01529  -0.01602 -0.00487 332 TRP A CB  
2601 C CG  . TRP A 332 ? 0.11629 0.11539 0.11814 0.01514  -0.01443 -0.00465 332 TRP A CG  
2602 C CD1 . TRP A 332 ? 0.17559 0.17342 0.17487 0.01427  -0.01383 -0.00554 332 TRP A CD1 
2603 C CD2 . TRP A 332 ? 0.12312 0.12071 0.12426 0.01590  -0.01333 -0.00353 332 TRP A CD2 
2604 N NE1 . TRP A 332 ? 0.12417 0.12009 0.12148 0.01451  -0.01249 -0.00503 332 TRP A NE1 
2605 C CE2 . TRP A 332 ? 0.12579 0.12156 0.12391 0.01540  -0.01212 -0.00382 332 TRP A CE2 
2606 C CE3 . TRP A 332 ? 0.12425 0.12180 0.12744 0.01694  -0.01325 -0.00237 332 TRP A CE3 
2607 C CZ2 . TRP A 332 ? 0.11813 0.11233 0.11496 0.01578  -0.01083 -0.00303 332 TRP A CZ2 
2608 C CZ3 . TRP A 332 ? 0.17291 0.16855 0.17458 0.01726  -0.01188 -0.00158 332 TRP A CZ3 
2609 C CH2 . TRP A 332 ? 0.12492 0.11905 0.12330 0.01662  -0.01068 -0.00193 332 TRP A CH2 
2610 N N   . ARG A 333 ? 0.13840 0.14188 0.15351 0.01596  -0.01337 -0.00555 333 ARG A N   
2611 C CA  . ARG A 333 ? 0.12634 0.12917 0.14371 0.01618  -0.01135 -0.00571 333 ARG A CA  
2612 C C   . ARG A 333 ? 0.11551 0.11965 0.13555 0.01457  -0.00942 -0.00766 333 ARG A C   
2613 O O   . ARG A 333 ? 0.05909 0.06214 0.07840 0.01364  -0.00730 -0.00815 333 ARG A O   
2614 C CB  . ARG A 333 ? 0.16434 0.16785 0.18576 0.01795  -0.01234 -0.00473 333 ARG A CB  
2615 C CG  . ARG A 333 ? 0.14393 0.14722 0.16932 0.01823  -0.01020 -0.00545 333 ARG A CG  
2616 C CD  . ARG A 333 ? 0.17588 0.17972 0.20616 0.02020  -0.01168 -0.00434 333 ARG A CD  
2617 N NE  . ARG A 333 ? 0.21766 0.22462 0.25282 0.02059  -0.01340 -0.00497 333 ARG A NE  
2618 C CZ  . ARG A 333 ? 0.22186 0.22978 0.26019 0.02221  -0.01618 -0.00338 333 ARG A CZ  
2619 N NH1 . ARG A 333 ? 0.23988 0.24563 0.27639 0.02347  -0.01770 -0.00083 333 ARG A NH1 
2620 N NH2 . ARG A 333 ? 0.19110 0.20228 0.23455 0.02242  -0.01760 -0.00424 333 ARG A NH2 
2621 N N   . GLU A 334 ? 0.13990 0.14647 0.16280 0.01395  -0.01010 -0.00881 334 GLU A N   
2622 C CA  . GLU A 334 ? 0.15212 0.16028 0.17761 0.01207  -0.00823 -0.01078 334 GLU A CA  
2623 C C   . GLU A 334 ? 0.16777 0.17494 0.18934 0.00993  -0.00784 -0.01116 334 GLU A C   
2624 O O   . GLU A 334 ? 0.17871 0.18717 0.20172 0.00792  -0.00657 -0.01261 334 GLU A O   
2625 C CB  . GLU A 334 ? 0.11682 0.12841 0.14820 0.01239  -0.00904 -0.01197 334 GLU A CB  
2626 C CG  . GLU A 334 ? 0.12823 0.14083 0.16478 0.01457  -0.00962 -0.01155 334 GLU A CG  
2627 C CD  . GLU A 334 ? 0.14524 0.16127 0.18758 0.01535  -0.01147 -0.01213 334 GLU A CD  
2628 O OE1 . GLU A 334 ? 0.14374 0.16165 0.18633 0.01390  -0.01177 -0.01332 334 GLU A OE1 
2629 O OE2 . GLU A 334 ? 0.25639 0.27319 0.30326 0.01739  -0.01277 -0.01128 334 GLU A OE2 
2630 N N   . ALA A 335 ? 0.11930 0.12417 0.13622 0.01021  -0.00885 -0.00993 335 ALA A N   
2631 C CA  . ALA A 335 ? 0.13455 0.13790 0.14817 0.00846  -0.00869 -0.01002 335 ALA A CA  
2632 C C   . ALA A 335 ? 0.13624 0.14125 0.15138 0.00709  -0.00936 -0.01117 335 ALA A C   
2633 O O   . ALA A 335 ? 0.13373 0.13874 0.14877 0.00487  -0.00831 -0.01188 335 ALA A O   
2634 C CB  . ALA A 335 ? 0.15585 0.15796 0.16811 0.00677  -0.00672 -0.01004 335 ALA A CB  
2635 N N   . ARG A 336 ? 0.09194 0.09838 0.10824 0.00819  -0.01122 -0.01128 336 ARG A N   
2636 C CA  . ARG A 336 ? 0.13693 0.14505 0.15464 0.00698  -0.01211 -0.01242 336 ARG A CA  
2637 C C   . ARG A 336 ? 0.14051 0.14829 0.15612 0.00781  -0.01426 -0.01208 336 ARG A C   
2638 O O   . ARG A 336 ? 0.09703 0.10718 0.11468 0.00787  -0.01575 -0.01271 336 ARG A O   
2639 C CB  . ARG A 336 ? 0.12496 0.13672 0.14815 0.00690  -0.01194 -0.01363 336 ARG A CB  
2640 C CG  . ARG A 336 ? 0.11899 0.13230 0.14528 0.00929  -0.01301 -0.01296 336 ARG A CG  
2641 C CD  . ARG A 336 ? 0.14218 0.15938 0.17503 0.00925  -0.01306 -0.01438 336 ARG A CD  
2642 N NE  . ARG A 336 ? 0.14091 0.15946 0.17760 0.01164  -0.01441 -0.01350 336 ARG A NE  
2643 C CZ  . ARG A 336 ? 0.12340 0.14313 0.16069 0.01298  -0.01735 -0.01239 336 ARG A CZ  
2644 N NH1 . ARG A 336 ? 0.22720 0.24712 0.26142 0.01214  -0.01904 -0.01237 336 ARG A NH1 
2645 N NH2 . ARG A 336 ? 0.16391 0.18458 0.20496 0.01506  -0.01870 -0.01122 336 ARG A NH2 
2646 N N   . THR A 337 ? 0.11271 0.11773 0.12430 0.00829  -0.01437 -0.01126 337 THR A N   
2647 C CA  . THR A 337 ? 0.13683 0.14141 0.14599 0.00865  -0.01596 -0.01137 337 THR A CA  
2648 C C   . THR A 337 ? 0.11076 0.11499 0.11963 0.00694  -0.01628 -0.01268 337 THR A C   
2649 O O   . THR A 337 ? 0.14325 0.14799 0.15104 0.00683  -0.01763 -0.01337 337 THR A O   
2650 C CB  . THR A 337 ? 0.09771 0.09963 0.10319 0.00954  -0.01558 -0.01051 337 THR A CB  
2651 O OG1 . THR A 337 ? 0.11662 0.11614 0.12113 0.00866  -0.01424 -0.01051 337 THR A OG1 
2652 C CG2 . THR A 337 ? 0.14942 0.15146 0.15499 0.01108  -0.01529 -0.00915 337 THR A CG2 
2653 N N   . GLY A 338 ? 0.11484 0.11813 0.12449 0.00537  -0.01509 -0.01301 338 GLY A N   
2654 C CA  . GLY A 338 ? 0.13434 0.13650 0.14360 0.00363  -0.01532 -0.01397 338 GLY A CA  
2655 C C   . GLY A 338 ? 0.15190 0.15038 0.15866 0.00342  -0.01497 -0.01355 338 GLY A C   
2656 O O   . GLY A 338 ? 0.14570 0.14259 0.15251 0.00191  -0.01509 -0.01411 338 GLY A O   
2657 N N   . PHE A 339 ? 0.09901 0.09606 0.10400 0.00489  -0.01459 -0.01260 339 PHE A N   
2658 C CA  . PHE A 339 ? 0.13506 0.12890 0.13859 0.00490  -0.01424 -0.01219 339 PHE A CA  
2659 C C   . PHE A 339 ? 0.11084 0.10355 0.11435 0.00439  -0.01327 -0.01075 339 PHE A C   
2660 O O   . PHE A 339 ? 0.12560 0.11903 0.12870 0.00542  -0.01261 -0.00996 339 PHE A O   
2661 C CB  . PHE A 339 ? 0.12751 0.12076 0.12917 0.00656  -0.01435 -0.01234 339 PHE A CB  
2662 C CG  . PHE A 339 ? 0.13157 0.12589 0.13245 0.00662  -0.01529 -0.01385 339 PHE A CG  
2663 C CD1 . PHE A 339 ? 0.17406 0.16666 0.17471 0.00596  -0.01542 -0.01532 339 PHE A CD1 
2664 C CD2 . PHE A 339 ? 0.14538 0.14240 0.14589 0.00721  -0.01612 -0.01380 339 PHE A CD2 
2665 C CE1 . PHE A 339 ? 0.19423 0.18796 0.19381 0.00564  -0.01613 -0.01700 339 PHE A CE1 
2666 C CE2 . PHE A 339 ? 0.15885 0.15705 0.15813 0.00690  -0.01720 -0.01506 339 PHE A CE2 
2667 C CZ  . PHE A 339 ? 0.24139 0.23802 0.23995 0.00599  -0.01709 -0.01680 339 PHE A CZ  
2668 N N   . PRO A 340 ? 0.10973 0.10064 0.11351 0.00264  -0.01321 -0.01027 340 PRO A N   
2669 C CA  . PRO A 340 ? 0.13070 0.12085 0.13396 0.00160  -0.01244 -0.00880 340 PRO A CA  
2670 C C   . PRO A 340 ? 0.12588 0.11476 0.12801 0.00301  -0.01216 -0.00772 340 PRO A C   
2671 O O   . PRO A 340 ? 0.10082 0.09023 0.10239 0.00265  -0.01131 -0.00685 340 PRO A O   
2672 C CB  . PRO A 340 ? 0.12816 0.11604 0.13151 -0.00062 -0.01300 -0.00823 340 PRO A CB  
2673 C CG  . PRO A 340 ? 0.12215 0.11074 0.12666 -0.00114 -0.01358 -0.00979 340 PRO A CG  
2674 C CD  . PRO A 340 ? 0.12524 0.11490 0.12976 0.00113  -0.01393 -0.01101 340 PRO A CD  
2675 N N   . TRP A 341 ? 0.10844 0.09583 0.11037 0.00442  -0.01267 -0.00801 341 TRP A N   
2676 C CA  . TRP A 341 ? 0.11745 0.10398 0.11867 0.00574  -0.01229 -0.00721 341 TRP A CA  
2677 C C   . TRP A 341 ? 0.12234 0.11088 0.12270 0.00702  -0.01146 -0.00723 341 TRP A C   
2678 O O   . TRP A 341 ? 0.09115 0.07959 0.09092 0.00727  -0.01076 -0.00626 341 TRP A O   
2679 C CB  . TRP A 341 ? 0.11768 0.10258 0.11939 0.00688  -0.01271 -0.00805 341 TRP A CB  
2680 C CG  . TRP A 341 ? 0.11509 0.09936 0.11656 0.00816  -0.01221 -0.00750 341 TRP A CG  
2681 C CD1 . TRP A 341 ? 0.12301 0.10804 0.12357 0.00965  -0.01155 -0.00836 341 TRP A CD1 
2682 C CD2 . TRP A 341 ? 0.09817 0.08110 0.10026 0.00781  -0.01237 -0.00592 341 TRP A CD2 
2683 N NE1 . TRP A 341 ? 0.12075 0.10505 0.12161 0.01033  -0.01109 -0.00762 341 TRP A NE1 
2684 C CE2 . TRP A 341 ? 0.11529 0.09840 0.11726 0.00930  -0.01169 -0.00611 341 TRP A CE2 
2685 C CE3 . TRP A 341 ? 0.11200 0.09370 0.11455 0.00614  -0.01313 -0.00427 341 TRP A CE3 
2686 C CZ2 . TRP A 341 ? 0.11781 0.10011 0.12061 0.00936  -0.01181 -0.00482 341 TRP A CZ2 
2687 C CZ3 . TRP A 341 ? 0.09004 0.07083 0.09303 0.00611  -0.01346 -0.00277 341 TRP A CZ3 
2688 C CH2 . TRP A 341 ? 0.13040 0.11160 0.13376 0.00781  -0.01283 -0.00311 341 TRP A CH2 
2689 N N   . ILE A 342 ? 0.10243 0.09275 0.10281 0.00773  -0.01167 -0.00822 342 ILE A N   
2690 C CA  . ILE A 342 ? 0.09592 0.08784 0.09583 0.00898  -0.01122 -0.00795 342 ILE A CA  
2691 C C   . ILE A 342 ? 0.09244 0.08577 0.09364 0.00825  -0.01047 -0.00755 342 ILE A C   
2692 O O   . ILE A 342 ? 0.12435 0.11783 0.12536 0.00879  -0.00957 -0.00689 342 ILE A O   
2693 C CB  . ILE A 342 ? 0.07994 0.07329 0.07948 0.00980  -0.01213 -0.00882 342 ILE A CB  
2694 C CG1 . ILE A 342 ? 0.08954 0.08162 0.08752 0.01019  -0.01243 -0.00967 342 ILE A CG1 
2695 C CG2 . ILE A 342 ? 0.13028 0.12506 0.12965 0.01101  -0.01205 -0.00809 342 ILE A CG2 
2696 C CD1 . ILE A 342 ? 0.06305 0.05379 0.05975 0.01108  -0.01156 -0.00916 342 ILE A CD1 
2697 N N   . ASP A 343 ? 0.08951 0.08391 0.09220 0.00684  -0.01061 -0.00818 343 ASP A N   
2698 C CA  . ASP A 343 ? 0.09131 0.08744 0.09569 0.00590  -0.00957 -0.00838 343 ASP A CA  
2699 C C   . ASP A 343 ? 0.09324 0.08824 0.09657 0.00453  -0.00838 -0.00758 343 ASP A C   
2700 O O   . ASP A 343 ? 0.08550 0.08168 0.08972 0.00417  -0.00707 -0.00779 343 ASP A O   
2701 C CB  . ASP A 343 ? 0.09254 0.09021 0.09876 0.00436  -0.00984 -0.00946 343 ASP A CB  
2702 C CG  . ASP A 343 ? 0.11269 0.11200 0.12014 0.00550  -0.01118 -0.01029 343 ASP A CG  
2703 O OD1 . ASP A 343 ? 0.12123 0.12070 0.12803 0.00738  -0.01184 -0.00990 343 ASP A OD1 
2704 O OD2 . ASP A 343 ? 0.10512 0.10562 0.11398 0.00429  -0.01165 -0.01126 343 ASP A OD2 
2705 N N   . ALA A 344 ? 0.07902 0.07177 0.08069 0.00366  -0.00888 -0.00671 344 ALA A N   
2706 C CA  . ALA A 344 ? 0.07799 0.06973 0.07834 0.00215  -0.00818 -0.00565 344 ALA A CA  
2707 C C   . ALA A 344 ? 0.06833 0.05986 0.06796 0.00359  -0.00750 -0.00512 344 ALA A C   
2708 O O   . ALA A 344 ? 0.05869 0.05065 0.05782 0.00249  -0.00633 -0.00488 344 ALA A O   
2709 C CB  . ALA A 344 ? 0.09132 0.08062 0.09067 0.00101  -0.00939 -0.00451 344 ALA A CB  
2710 N N   . ILE A 345 ? 0.05836 0.04927 0.05777 0.00577  -0.00808 -0.00505 345 ILE A N   
2711 C CA  . ILE A 345 ? 0.06836 0.05903 0.06702 0.00704  -0.00738 -0.00456 345 ILE A CA  
2712 C C   . ILE A 345 ? 0.06913 0.06140 0.06882 0.00762  -0.00629 -0.00506 345 ILE A C   
2713 O O   . ILE A 345 ? 0.07580 0.06806 0.07523 0.00740  -0.00513 -0.00479 345 ILE A O   
2714 C CB  . ILE A 345 ? 0.07209 0.06186 0.07013 0.00887  -0.00805 -0.00459 345 ILE A CB  
2715 C CG1 . ILE A 345 ? 0.07640 0.06447 0.07449 0.00843  -0.00896 -0.00431 345 ILE A CG1 
2716 C CG2 . ILE A 345 ? 0.08631 0.07596 0.08350 0.01001  -0.00719 -0.00413 345 ILE A CG2 
2717 C CD1 . ILE A 345 ? 0.10455 0.09195 0.10252 0.00995  -0.00929 -0.00500 345 ILE A CD1 
2718 N N   . MET A 346 ? 0.07148 0.06514 0.07270 0.00836  -0.00673 -0.00582 346 MET A N   
2719 C CA  . MET A 346 ? 0.07761 0.07280 0.08092 0.00906  -0.00595 -0.00626 346 MET A CA  
2720 C C   . MET A 346 ? 0.08091 0.07713 0.08566 0.00717  -0.00438 -0.00705 346 MET A C   
2721 O O   . MET A 346 ? 0.08795 0.08492 0.09446 0.00750  -0.00312 -0.00752 346 MET A O   
2722 C CB  . MET A 346 ? 0.08580 0.08251 0.09093 0.01013  -0.00718 -0.00676 346 MET A CB  
2723 C CG  . MET A 346 ? 0.12687 0.12285 0.13009 0.01159  -0.00861 -0.00618 346 MET A CG  
2724 S SD  . MET A 346 ? 0.13230 0.12698 0.13374 0.01313  -0.00819 -0.00498 346 MET A SD  
2725 C CE  . MET A 346 ? 0.12277 0.11889 0.12765 0.01413  -0.00808 -0.00479 346 MET A CE  
2726 N N   . THR A 347 ? 0.09013 0.08636 0.09422 0.00500  -0.00435 -0.00731 347 THR A N   
2727 C CA  . THR A 347 ? 0.08954 0.08667 0.09401 0.00253  -0.00266 -0.00809 347 THR A CA  
2728 C C   . THR A 347 ? 0.07223 0.06814 0.07445 0.00165  -0.00174 -0.00733 347 THR A C   
2729 O O   . THR A 347 ? 0.07461 0.07143 0.07756 0.00058  0.00009  -0.00825 347 THR A O   
2730 C CB  . THR A 347 ? 0.09443 0.09165 0.09813 0.00007  -0.00306 -0.00823 347 THR A CB  
2731 O OG1 . THR A 347 ? 0.06793 0.06666 0.07407 0.00069  -0.00374 -0.00921 347 THR A OG1 
2732 C CG2 . THR A 347 ? 0.09915 0.09735 0.10241 -0.00308 -0.00118 -0.00903 347 THR A CG2 
2733 N N   . GLN A 348 ? 0.07101 0.06501 0.07085 0.00203  -0.00293 -0.00585 348 GLN A N   
2734 C CA  . GLN A 348 ? 0.06601 0.05910 0.06404 0.00141  -0.00233 -0.00505 348 GLN A CA  
2735 C C   . GLN A 348 ? 0.07807 0.07142 0.07713 0.00319  -0.00119 -0.00548 348 GLN A C   
2736 O O   . GLN A 348 ? 0.05696 0.05029 0.05533 0.00215  0.00012  -0.00561 348 GLN A O   
2737 C CB  . GLN A 348 ? 0.08738 0.07863 0.08378 0.00190  -0.00400 -0.00349 348 GLN A CB  
2738 C CG  . GLN A 348 ? 0.09106 0.08161 0.08587 0.00112  -0.00375 -0.00251 348 GLN A CG  
2739 C CD  . GLN A 348 ? 0.07155 0.06060 0.06603 0.00217  -0.00539 -0.00122 348 GLN A CD  
2740 O OE1 . GLN A 348 ? 0.09731 0.08581 0.09274 0.00405  -0.00624 -0.00141 348 GLN A OE1 
2741 N NE2 . GLN A 348 ? 0.13309 0.12166 0.12649 0.00084  -0.00582 -0.00005 348 GLN A NE2 
2742 N N   . LEU A 349 ? 0.08350 0.07702 0.08409 0.00565  -0.00175 -0.00563 349 LEU A N   
2743 C CA  . LEU A 349 ? 0.07276 0.06618 0.07443 0.00732  -0.00094 -0.00570 349 LEU A CA  
2744 C C   . LEU A 349 ? 0.09557 0.09025 0.09981 0.00646  0.00094  -0.00712 349 LEU A C   
2745 O O   . LEU A 349 ? 0.08279 0.07702 0.08712 0.00624  0.00236  -0.00736 349 LEU A O   
2746 C CB  . LEU A 349 ? 0.05543 0.04885 0.05794 0.00970  -0.00229 -0.00530 349 LEU A CB  
2747 C CG  . LEU A 349 ? 0.06866 0.06195 0.07277 0.01140  -0.00186 -0.00508 349 LEU A CG  
2748 C CD1 . LEU A 349 ? 0.13435 0.12607 0.13646 0.01163  -0.00110 -0.00428 349 LEU A CD1 
2749 C CD2 . LEU A 349 ? 0.16354 0.15712 0.16815 0.01321  -0.00363 -0.00447 349 LEU A CD2 
2750 N N   . VAL A 350 ? 0.09306 0.08943 0.09978 0.00586  0.00112  -0.00832 350 VAL A N   
2751 C CA  . VAL A 350 ? 0.07041 0.06828 0.08061 0.00518  0.00312  -0.01014 350 VAL A CA  
2752 C C   . VAL A 350 ? 0.07518 0.07352 0.08390 0.00192  0.00513  -0.01127 350 VAL A C   
2753 O O   . VAL A 350 ? 0.11582 0.11504 0.12687 0.00110  0.00733  -0.01302 350 VAL A O   
2754 C CB  . VAL A 350 ? 0.11011 0.11007 0.12417 0.00567  0.00269  -0.01127 350 VAL A CB  
2755 C CG1 . VAL A 350 ? 0.07715 0.07686 0.09244 0.00861  0.00050  -0.01006 350 VAL A CG1 
2756 C CG2 . VAL A 350 ? 0.10475 0.10550 0.11721 0.00343  0.00230  -0.01159 350 VAL A CG2 
2757 N N   . THR A 351 ? 0.06923 0.06695 0.07420 -0.00012 0.00440  -0.01032 351 THR A N   
2758 C CA  . THR A 351 ? 0.08094 0.07910 0.08364 -0.00372 0.00590  -0.01099 351 THR A CA  
2759 C C   . THR A 351 ? 0.08598 0.08275 0.08562 -0.00441 0.00604  -0.00991 351 THR A C   
2760 O O   . THR A 351 ? 0.06924 0.06663 0.06816 -0.00674 0.00801  -0.01111 351 THR A O   
2761 C CB  . THR A 351 ? 0.07371 0.07194 0.07411 -0.00603 0.00476  -0.01027 351 THR A CB  
2762 O OG1 . THR A 351 ? 0.13478 0.13114 0.13327 -0.00456 0.00223  -0.00805 351 THR A OG1 
2763 C CG2 . THR A 351 ? 0.09387 0.09395 0.09736 -0.00615 0.00512  -0.01180 351 THR A CG2 
2764 N N   . TRP A 352 ? 0.08041 0.07553 0.07842 -0.00262 0.00410  -0.00791 352 TRP A N   
2765 C CA  . TRP A 352 ? 0.10274 0.09681 0.09835 -0.00315 0.00402  -0.00685 352 TRP A CA  
2766 C C   . TRP A 352 ? 0.08728 0.08056 0.08417 -0.00056 0.00452  -0.00682 352 TRP A C   
2767 O O   . TRP A 352 ? 0.14273 0.13561 0.13843 -0.00135 0.00539  -0.00676 352 TRP A O   
2768 C CB  . TRP A 352 ? 0.09815 0.09101 0.09150 -0.00319 0.00162  -0.00471 352 TRP A CB  
2769 C CG  . TRP A 352 ? 0.12615 0.11917 0.11736 -0.00637 0.00087  -0.00402 352 TRP A CG  
2770 C CD1 . TRP A 352 ? 0.11915 0.11341 0.11000 -0.00910 0.00209  -0.00522 352 TRP A CD1 
2771 C CD2 . TRP A 352 ? 0.14187 0.13370 0.13113 -0.00731 -0.00135 -0.00187 352 TRP A CD2 
2772 N NE1 . TRP A 352 ? 0.17814 0.17189 0.16625 -0.01191 0.00070  -0.00372 352 TRP A NE1 
2773 C CE2 . TRP A 352 ? 0.11190 0.10405 0.09923 -0.01074 -0.00159 -0.00151 352 TRP A CE2 
2774 C CE3 . TRP A 352 ? 0.14953 0.14011 0.13886 -0.00563 -0.00314 -0.00025 352 TRP A CE3 
2775 C CZ2 . TRP A 352 ? 0.15394 0.14489 0.13936 -0.01247 -0.00391 0.00081  352 TRP A CZ2 
2776 C CZ3 . TRP A 352 ? 0.16789 0.15751 0.15606 -0.00711 -0.00532 0.00175  352 TRP A CZ3 
2777 C CH2 . TRP A 352 ? 0.13551 0.12515 0.12170 -0.01046 -0.00587 0.00246  352 TRP A CH2 
2778 N N   . GLY A 353 ? 0.06910 0.06212 0.06814 0.00228  0.00389  -0.00674 353 GLY A N   
2779 C CA  . GLY A 353 ? 0.08508 0.07702 0.08471 0.00454  0.00403  -0.00624 353 GLY A CA  
2780 C C   . GLY A 353 ? 0.08818 0.07893 0.08547 0.00534  0.00277  -0.00467 353 GLY A C   
2781 O O   . GLY A 353 ? 0.07328 0.06314 0.07045 0.00659  0.00318  -0.00425 353 GLY A O   
2782 N N   . TRP A 354 ? 0.05877 0.04945 0.05455 0.00460  0.00131  -0.00384 354 TRP A N   
2783 C CA  . TRP A 354 ? 0.09360 0.08341 0.08809 0.00533  0.00015  -0.00264 354 TRP A CA  
2784 C C   . TRP A 354 ? 0.09035 0.07993 0.08477 0.00555  -0.00166 -0.00209 354 TRP A C   
2785 O O   . TRP A 354 ? 0.08904 0.07898 0.08332 0.00390  -0.00212 -0.00212 354 TRP A O   
2786 C CB  . TRP A 354 ? 0.07830 0.06813 0.07143 0.00344  0.00048  -0.00216 354 TRP A CB  
2787 C CG  . TRP A 354 ? 0.07469 0.06397 0.06747 0.00430  -0.00066 -0.00109 354 TRP A CG  
2788 C CD1 . TRP A 354 ? 0.06546 0.05442 0.05824 0.00542  -0.00001 -0.00101 354 TRP A CD1 
2789 C CD2 . TRP A 354 ? 0.08293 0.07193 0.07587 0.00409  -0.00255 -0.00010 354 TRP A CD2 
2790 N NE1 . TRP A 354 ? 0.06429 0.05314 0.05742 0.00590  -0.00123 -0.00027 354 TRP A NE1 
2791 C CE2 . TRP A 354 ? 0.08791 0.07671 0.08143 0.00523  -0.00287 0.00031  354 TRP A CE2 
2792 C CE3 . TRP A 354 ? 0.11011 0.09893 0.10306 0.00299  -0.00400 0.00047  354 TRP A CE3 
2793 C CZ2 . TRP A 354 ? 0.10656 0.09509 0.10132 0.00552  -0.00458 0.00111  354 TRP A CZ2 
2794 C CZ3 . TRP A 354 ? 0.08378 0.07195 0.07765 0.00325  -0.00585 0.00154  354 TRP A CZ3 
2795 C CH2 . TRP A 354 ? 0.09670 0.08479 0.09178 0.00462  -0.00613 0.00177  354 TRP A CH2 
2796 N N   . MET A 355 ? 0.06351 0.05244 0.05802 0.00738  -0.00254 -0.00173 355 MET A N   
2797 C CA  . MET A 355 ? 0.06566 0.05411 0.06052 0.00772  -0.00411 -0.00146 355 MET A CA  
2798 C C   . MET A 355 ? 0.08906 0.07691 0.08411 0.00867  -0.00456 -0.00105 355 MET A C   
2799 O O   . MET A 355 ? 0.09355 0.08147 0.08821 0.00942  -0.00362 -0.00111 355 MET A O   
2800 C CB  . MET A 355 ? 0.06196 0.05059 0.05736 0.00903  -0.00456 -0.00217 355 MET A CB  
2801 C CG  . MET A 355 ? 0.08654 0.07617 0.08266 0.00848  -0.00404 -0.00281 355 MET A CG  
2802 S SD  . MET A 355 ? 0.12224 0.11231 0.11898 0.01024  -0.00317 -0.00313 355 MET A SD  
2803 C CE  . MET A 355 ? 0.09931 0.08911 0.09537 0.01195  -0.00455 -0.00312 355 MET A CE  
2804 N N   . HIS A 356 ? 0.08873 0.07598 0.08477 0.00858  -0.00595 -0.00073 356 HIS A N   
2805 C CA  . HIS A 356 ? 0.07612 0.06300 0.07341 0.00960  -0.00634 -0.00072 356 HIS A CA  
2806 C C   . HIS A 356 ? 0.07768 0.06467 0.07465 0.01136  -0.00552 -0.00190 356 HIS A C   
2807 O O   . HIS A 356 ? 0.08213 0.06923 0.07821 0.01183  -0.00540 -0.00249 356 HIS A O   
2808 C CB  . HIS A 356 ? 0.09508 0.08106 0.09432 0.00929  -0.00809 -0.00026 356 HIS A CB  
2809 C CG  . HIS A 356 ? 0.09601 0.08176 0.09773 0.01033  -0.00851 -0.00044 356 HIS A CG  
2810 N ND1 . HIS A 356 ? 0.09805 0.08354 0.10118 0.01185  -0.00822 -0.00194 356 HIS A ND1 
2811 C CD2 . HIS A 356 ? 0.10368 0.08966 0.10709 0.00998  -0.00917 0.00051  356 HIS A CD2 
2812 C CE1 . HIS A 356 ? 0.09147 0.07706 0.09744 0.01248  -0.00845 -0.00212 356 HIS A CE1 
2813 N NE2 . HIS A 356 ? 0.10307 0.08898 0.10944 0.01147  -0.00918 -0.00052 356 HIS A NE2 
2814 N N   . HIS A 357 ? 0.08441 0.07154 0.08207 0.01210  -0.00498 -0.00224 357 HIS A N   
2815 C CA  . HIS A 357 ? 0.09892 0.08625 0.09556 0.01325  -0.00395 -0.00333 357 HIS A CA  
2816 C C   . HIS A 357 ? 0.09742 0.08447 0.09419 0.01380  -0.00453 -0.00445 357 HIS A C   
2817 O O   . HIS A 357 ? 0.08547 0.07275 0.08024 0.01419  -0.00414 -0.00495 357 HIS A O   
2818 C CB  . HIS A 357 ? 0.10799 0.09572 0.10585 0.01363  -0.00316 -0.00381 357 HIS A CB  
2819 C CG  . HIS A 357 ? 0.11311 0.10112 0.10951 0.01431  -0.00189 -0.00504 357 HIS A CG  
2820 N ND1 . HIS A 357 ? 0.10890 0.09683 0.10224 0.01433  -0.00109 -0.00468 357 HIS A ND1 
2821 C CD2 . HIS A 357 ? 0.15817 0.14654 0.15572 0.01476  -0.00124 -0.00663 357 HIS A CD2 
2822 C CE1 . HIS A 357 ? 0.12066 0.10885 0.11266 0.01455  -0.00015 -0.00575 357 HIS A CE1 
2823 N NE2 . HIS A 357 ? 0.13540 0.12399 0.12986 0.01474  -0.00001 -0.00718 357 HIS A NE2 
2824 N N   . LEU A 358 ? 0.08566 0.07214 0.08481 0.01372  -0.00558 -0.00479 358 LEU A N   
2825 C CA  . LEU A 358 ? 0.09772 0.08382 0.09719 0.01404  -0.00605 -0.00609 358 LEU A CA  
2826 C C   . LEU A 358 ? 0.08469 0.07074 0.08301 0.01345  -0.00687 -0.00566 358 LEU A C   
2827 O O   . LEU A 358 ? 0.07835 0.06446 0.07612 0.01361  -0.00712 -0.00677 358 LEU A O   
2828 C CB  . LEU A 358 ? 0.10260 0.08781 0.10571 0.01422  -0.00686 -0.00670 358 LEU A CB  
2829 C CG  . LEU A 358 ? 0.11789 0.10353 0.12307 0.01501  -0.00583 -0.00797 358 LEU A CG  
2830 C CD1 . LEU A 358 ? 0.18872 0.17339 0.19869 0.01539  -0.00678 -0.00861 358 LEU A CD1 
2831 C CD2 . LEU A 358 ? 0.16935 0.15574 0.17218 0.01533  -0.00427 -0.00989 358 LEU A CD2 
2832 N N   . ALA A 359 ? 0.07103 0.05715 0.06905 0.01256  -0.00719 -0.00429 359 ALA A N   
2833 C CA  . ALA A 359 ? 0.07087 0.05742 0.06808 0.01195  -0.00757 -0.00417 359 ALA A CA  
2834 C C   . ALA A 359 ? 0.07449 0.06201 0.06998 0.01270  -0.00690 -0.00450 359 ALA A C   
2835 O O   . ALA A 359 ? 0.07138 0.05948 0.06660 0.01276  -0.00744 -0.00501 359 ALA A O   
2836 C CB  . ALA A 359 ? 0.07848 0.06510 0.07575 0.01050  -0.00768 -0.00298 359 ALA A CB  
2837 N N   . ARG A 360 ? 0.07221 0.05991 0.06669 0.01318  -0.00591 -0.00406 360 ARG A N   
2838 C CA  . ARG A 360 ? 0.06738 0.05561 0.06029 0.01389  -0.00553 -0.00398 360 ARG A CA  
2839 C C   . ARG A 360 ? 0.06973 0.05805 0.06125 0.01440  -0.00579 -0.00492 360 ARG A C   
2840 O O   . ARG A 360 ? 0.06343 0.05232 0.05363 0.01467  -0.00630 -0.00482 360 ARG A O   
2841 C CB  . ARG A 360 ? 0.07920 0.06720 0.07136 0.01406  -0.00436 -0.00320 360 ARG A CB  
2842 C CG  . ARG A 360 ? 0.06687 0.05481 0.06010 0.01317  -0.00385 -0.00261 360 ARG A CG  
2843 C CD  . ARG A 360 ? 0.09470 0.08240 0.08723 0.01326  -0.00260 -0.00205 360 ARG A CD  
2844 N NE  . ARG A 360 ? 0.09300 0.08076 0.08623 0.01207  -0.00205 -0.00175 360 ARG A NE  
2845 C CZ  . ARG A 360 ? 0.06315 0.05077 0.05617 0.01167  -0.00086 -0.00149 360 ARG A CZ  
2846 N NH1 . ARG A 360 ? 0.07450 0.06160 0.06683 0.01250  -0.00010 -0.00125 360 ARG A NH1 
2847 N NH2 . ARG A 360 ? 0.06770 0.05560 0.06106 0.01017  -0.00046 -0.00140 360 ARG A NH2 
2848 N N   . HIS A 361 ? 0.07844 0.06633 0.07043 0.01442  -0.00548 -0.00591 361 HIS A N   
2849 C CA  . HIS A 361 ? 0.08443 0.07253 0.07519 0.01452  -0.00542 -0.00738 361 HIS A CA  
2850 C C   . HIS A 361 ? 0.10398 0.09241 0.09482 0.01422  -0.00664 -0.00804 361 HIS A C   
2851 O O   . HIS A 361 ? 0.09699 0.08609 0.08571 0.01407  -0.00697 -0.00865 361 HIS A O   
2852 C CB  . HIS A 361 ? 0.10846 0.09610 0.10103 0.01459  -0.00470 -0.00876 361 HIS A CB  
2853 C CG  . HIS A 361 ? 0.14969 0.13761 0.14134 0.01473  -0.00322 -0.00904 361 HIS A CG  
2854 N ND1 . HIS A 361 ? 0.15526 0.14353 0.14655 0.01458  -0.00211 -0.01102 361 HIS A ND1 
2855 C CD2 . HIS A 361 ? 0.14625 0.13423 0.13740 0.01480  -0.00246 -0.00782 361 HIS A CD2 
2856 C CE1 . HIS A 361 ? 0.12528 0.11391 0.11583 0.01453  -0.00074 -0.01092 361 HIS A CE1 
2857 N NE2 . HIS A 361 ? 0.14971 0.13808 0.14015 0.01470  -0.00101 -0.00891 361 HIS A NE2 
2858 N N   . SER A 362 ? 0.10281 0.09084 0.09588 0.01387  -0.00740 -0.00787 362 SER A N   
2859 C CA  . SER A 362 ? 0.08771 0.07605 0.08120 0.01339  -0.00847 -0.00863 362 SER A CA  
2860 C C   . SER A 362 ? 0.07190 0.06161 0.06414 0.01343  -0.00915 -0.00799 362 SER A C   
2861 O O   . SER A 362 ? 0.08076 0.07130 0.07176 0.01325  -0.00988 -0.00878 362 SER A O   
2862 C CB  . SER A 362 ? 0.08478 0.07226 0.08070 0.01271  -0.00906 -0.00827 362 SER A CB  
2863 O OG  . SER A 362 ? 0.10730 0.09339 0.10505 0.01276  -0.00893 -0.00872 362 SER A OG  
2864 N N   . VAL A 363 ? 0.06666 0.05674 0.05951 0.01358  -0.00898 -0.00664 363 VAL A N   
2865 C CA  . VAL A 363 ? 0.06928 0.06073 0.06228 0.01379  -0.00973 -0.00607 363 VAL A CA  
2866 C C   . VAL A 363 ? 0.08501 0.07681 0.07572 0.01446  -0.00996 -0.00542 363 VAL A C   
2867 O O   . VAL A 363 ? 0.08587 0.07885 0.07636 0.01460  -0.01121 -0.00509 363 VAL A O   
2868 C CB  . VAL A 363 ? 0.08543 0.07718 0.08044 0.01363  -0.00920 -0.00526 363 VAL A CB  
2869 C CG1 . VAL A 363 ? 0.07285 0.06438 0.06944 0.01244  -0.00919 -0.00574 363 VAL A CG1 
2870 C CG2 . VAL A 363 ? 0.08324 0.07408 0.07763 0.01396  -0.00796 -0.00440 363 VAL A CG2 
2871 N N   . ALA A 364 ? 0.07402 0.06487 0.06301 0.01471  -0.00890 -0.00510 364 ALA A N   
2872 C CA  . ALA A 364 ? 0.08866 0.07961 0.07487 0.01493  -0.00911 -0.00432 364 ALA A CA  
2873 C C   . ALA A 364 ? 0.09865 0.09018 0.08235 0.01426  -0.00978 -0.00549 364 ALA A C   
2874 O O   . ALA A 364 ? 0.08613 0.07842 0.06776 0.01405  -0.01102 -0.00474 364 ALA A O   
2875 C CB  . ALA A 364 ? 0.09828 0.08814 0.08329 0.01507  -0.00757 -0.00383 364 ALA A CB  
2876 N N   . CYS A 365 ? 0.10270 0.09387 0.08669 0.01378  -0.00906 -0.00736 365 CYS A N   
2877 C CA  . CYS A 365 ? 0.09808 0.08983 0.07999 0.01289  -0.00942 -0.00904 365 CYS A CA  
2878 C C   . CYS A 365 ? 0.10557 0.09853 0.08809 0.01255  -0.01124 -0.00917 365 CYS A C   
2879 O O   . CYS A 365 ? 0.13396 0.12798 0.11383 0.01176  -0.01226 -0.00949 365 CYS A O   
2880 C CB  . CYS A 365 ? 0.13336 0.12427 0.11667 0.01262  -0.00813 -0.01125 365 CYS A CB  
2881 S SG  . CYS A 365 ? 0.14150 0.13302 0.12249 0.01128  -0.00789 -0.01410 365 CYS A SG  
2882 N N   . PHE A 366 ? 0.08502 0.07801 0.07088 0.01288  -0.01167 -0.00894 366 PHE A N   
2883 C CA  . PHE A 366 ? 0.10195 0.09632 0.08898 0.01245  -0.01324 -0.00927 366 PHE A CA  
2884 C C   . PHE A 366 ? 0.10097 0.09690 0.08716 0.01274  -0.01482 -0.00767 366 PHE A C   
2885 O O   . PHE A 366 ? 0.11305 0.11045 0.09823 0.01208  -0.01639 -0.00804 366 PHE A O   
2886 C CB  . PHE A 366 ? 0.13451 0.12863 0.12515 0.01250  -0.01310 -0.00918 366 PHE A CB  
2887 C CG  . PHE A 366 ? 0.12228 0.11787 0.11456 0.01182  -0.01441 -0.00984 366 PHE A CG  
2888 C CD1 . PHE A 366 ? 0.10134 0.09650 0.09396 0.01084  -0.01455 -0.01159 366 PHE A CD1 
2889 C CD2 . PHE A 366 ? 0.12047 0.11789 0.11449 0.01215  -0.01546 -0.00884 366 PHE A CD2 
2890 C CE1 . PHE A 366 ? 0.13542 0.13199 0.12957 0.01003  -0.01568 -0.01229 366 PHE A CE1 
2891 C CE2 . PHE A 366 ? 0.09487 0.09401 0.09086 0.01145  -0.01661 -0.00961 366 PHE A CE2 
2892 C CZ  . PHE A 366 ? 0.13435 0.13308 0.13014 0.01030  -0.01672 -0.01131 366 PHE A CZ  
2893 N N   . LEU A 367 ? 0.10021 0.09580 0.08709 0.01369  -0.01456 -0.00585 367 LEU A N   
2894 C CA  . LEU A 367 ? 0.12079 0.11755 0.10787 0.01421  -0.01624 -0.00406 367 LEU A CA  
2895 C C   . LEU A 367 ? 0.14039 0.13723 0.12295 0.01359  -0.01719 -0.00333 367 LEU A C   
2896 O O   . LEU A 367 ? 0.11213 0.11048 0.09400 0.01325  -0.01940 -0.00251 367 LEU A O   
2897 C CB  . LEU A 367 ? 0.09990 0.09589 0.08929 0.01533  -0.01545 -0.00254 367 LEU A CB  
2898 C CG  . LEU A 367 ? 0.09253 0.08908 0.08263 0.01613  -0.01708 -0.00042 367 LEU A CG  
2899 C CD1 . LEU A 367 ? 0.15086 0.14956 0.14531 0.01653  -0.01870 -0.00043 367 LEU A CD1 
2900 C CD2 . LEU A 367 ? 0.12396 0.11890 0.11498 0.01699  -0.01575 0.00085  367 LEU A CD2 
2901 N N   . THR A 368 ? 0.12995 0.12536 0.10938 0.01320  -0.01561 -0.00361 368 THR A N   
2902 C CA  . THR A 368 ? 0.17116 0.16652 0.14580 0.01226  -0.01618 -0.00272 368 THR A CA  
2903 C C   . THR A 368 ? 0.14688 0.14303 0.11812 0.01055  -0.01613 -0.00492 368 THR A C   
2904 O O   . THR A 368 ? 0.14512 0.14279 0.11667 0.00993  -0.01775 -0.00562 368 THR A O   
2905 C CB  . THR A 368 ? 0.13968 0.13331 0.11263 0.01245  -0.01429 -0.00198 368 THR A CB  
2906 O OG1 . THR A 368 ? 0.09456 0.08750 0.06780 0.01219  -0.01199 -0.00427 368 THR A OG1 
2907 C CG2 . THR A 368 ? 0.12755 0.12031 0.10389 0.01395  -0.01414 -0.00012 368 THR A CG2 
2908 N N   . ARG A 369 ? 0.13326 0.12852 0.10178 0.00970  -0.01406 -0.00638 369 ARG A N   
2909 C CA  . ARG A 369 ? 0.13396 0.12992 0.09883 0.00778  -0.01355 -0.00876 369 ARG A CA  
2910 C C   . ARG A 369 ? 0.18859 0.18483 0.15614 0.00758  -0.01301 -0.01169 369 ARG A C   
2911 O O   . ARG A 369 ? 0.23343 0.23012 0.19859 0.00597  -0.01221 -0.01422 369 ARG A O   
2912 C CB  . ARG A 369 ? 0.17938 0.17443 0.14137 0.00695  -0.01106 -0.00976 369 ARG A CB  
2913 C CG  . ARG A 369 ? 0.11262 0.10645 0.07865 0.00819  -0.00877 -0.01120 369 ARG A CG  
2914 C CD  . ARG A 369 ? 0.15156 0.14500 0.11552 0.00725  -0.00620 -0.01283 369 ARG A CD  
2915 N NE  . ARG A 369 ? 0.17024 0.16273 0.13875 0.00856  -0.00445 -0.01393 369 ARG A NE  
2916 C CZ  . ARG A 369 ? 0.16126 0.15358 0.13310 0.00875  -0.00357 -0.01656 369 ARG A CZ  
2917 N NH1 . ARG A 369 ? 0.15252 0.14546 0.12372 0.00770  -0.00394 -0.01872 369 ARG A NH1 
2918 N NH2 . ARG A 369 ? 0.23732 0.22875 0.21340 0.00995  -0.00243 -0.01695 369 ARG A NH2 
2919 N N   . GLY A 370 ? 0.13942 0.13531 0.11173 0.00892  -0.01331 -0.01154 370 GLY A N   
2920 C CA  . GLY A 370 ? 0.15808 0.15373 0.13286 0.00859  -0.01274 -0.01412 370 GLY A CA  
2921 C C   . GLY A 370 ? 0.16632 0.16338 0.14217 0.00804  -0.01471 -0.01446 370 GLY A C   
2922 O O   . GLY A 370 ? 0.17825 0.17559 0.15372 0.00682  -0.01457 -0.01692 370 GLY A O   
2923 N N   . ASP A 371 ? 0.14826 0.14632 0.12589 0.00887  -0.01645 -0.01223 371 ASP A N   
2924 C CA  . ASP A 371 ? 0.13788 0.13755 0.11752 0.00843  -0.01820 -0.01265 371 ASP A CA  
2925 C C   . ASP A 371 ? 0.13858 0.14034 0.11809 0.00866  -0.02072 -0.01039 371 ASP A C   
2926 O O   . ASP A 371 ? 0.17513 0.17878 0.15318 0.00746  -0.02258 -0.01080 371 ASP A O   
2927 C CB  . ASP A 371 ? 0.12698 0.12585 0.11131 0.00919  -0.01754 -0.01293 371 ASP A CB  
2928 C CG  . ASP A 371 ? 0.14622 0.14301 0.13138 0.00887  -0.01571 -0.01498 371 ASP A CG  
2929 O OD1 . ASP A 371 ? 0.10139 0.09659 0.08632 0.00954  -0.01416 -0.01477 371 ASP A OD1 
2930 O OD2 . ASP A 371 ? 0.15116 0.14789 0.13759 0.00794  -0.01592 -0.01677 371 ASP A OD2 
2931 N N   . LEU A 372 ? 0.18329 0.18476 0.16465 0.01014  -0.02088 -0.00805 372 LEU A N   
2932 C CA  . LEU A 372 ? 0.13699 0.14032 0.12015 0.01077  -0.02331 -0.00590 372 LEU A CA  
2933 C C   . LEU A 372 ? 0.16031 0.16378 0.13962 0.01052  -0.02483 -0.00369 372 LEU A C   
2934 O O   . LEU A 372 ? 0.17601 0.18132 0.15607 0.01054  -0.02758 -0.00202 372 LEU A O   
2935 C CB  . LEU A 372 ? 0.12793 0.13092 0.11603 0.01243  -0.02262 -0.00482 372 LEU A CB  
2936 C CG  . LEU A 372 ? 0.16436 0.16732 0.15613 0.01236  -0.02132 -0.00655 372 LEU A CG  
2937 C CD1 . LEU A 372 ? 0.13332 0.13636 0.12954 0.01354  -0.02060 -0.00563 372 LEU A CD1 
2938 C CD2 . LEU A 372 ? 0.17261 0.17769 0.16558 0.01126  -0.02281 -0.00795 372 LEU A CD2 
2939 N N   . TYR A 373 ? 0.14072 0.14233 0.11617 0.01019  -0.02321 -0.00352 373 TYR A N   
2940 C CA  . TYR A 373 ? 0.15270 0.15412 0.12348 0.00940  -0.02441 -0.00144 373 TYR A CA  
2941 C C   . TYR A 373 ? 0.17262 0.17397 0.14603 0.01092  -0.02624 0.00189  373 TYR A C   
2942 O O   . TYR A 373 ? 0.19499 0.19713 0.16636 0.01036  -0.02893 0.00421  373 TYR A O   
2943 C CB  . TYR A 373 ? 0.20480 0.20805 0.17123 0.00718  -0.02637 -0.00202 373 TYR A CB  
2944 C CG  . TYR A 373 ? 0.25516 0.25763 0.21475 0.00521  -0.02565 -0.00196 373 TYR A CG  
2945 C CD1 . TYR A 373 ? 0.21549 0.21710 0.17258 0.00403  -0.02269 -0.00506 373 TYR A CD1 
2946 C CD2 . TYR A 373 ? 0.27115 0.27375 0.22702 0.00439  -0.02790 0.00118  373 TYR A CD2 
2947 C CE1 . TYR A 373 ? 0.26665 0.26785 0.21764 0.00196  -0.02163 -0.00542 373 TYR A CE1 
2948 C CE2 . TYR A 373 ? 0.29569 0.29763 0.24476 0.00212  -0.02706 0.00121  373 TYR A CE2 
2949 C CZ  . TYR A 373 ? 0.28533 0.28673 0.23196 0.00085  -0.02374 -0.00229 373 TYR A CZ  
2950 O OH  . TYR A 373 ? 0.36851 0.36955 0.30854 -0.00166 -0.02254 -0.00267 373 TYR A OH  
2951 N N   . VAL A 374 ? 0.12221 0.12252 0.10025 0.01272  -0.02483 0.00213  374 VAL A N   
2952 C CA  . VAL A 374 ? 0.15632 0.15606 0.13751 0.01427  -0.02583 0.00481  374 VAL A CA  
2953 C C   . VAL A 374 ? 0.17653 0.17366 0.15489 0.01437  -0.02395 0.00586  374 VAL A C   
2954 O O   . VAL A 374 ? 0.11891 0.11489 0.09551 0.01394  -0.02129 0.00408  374 VAL A O   
2955 C CB  . VAL A 374 ? 0.16684 0.16729 0.15496 0.01584  -0.02519 0.00406  374 VAL A CB  
2956 C CG1 . VAL A 374 ? 0.21303 0.21268 0.20507 0.01748  -0.02571 0.00631  374 VAL A CG1 
2957 C CG2 . VAL A 374 ? 0.13077 0.13402 0.12176 0.01554  -0.02705 0.00302  374 VAL A CG2 
2958 N N   . SER A 375 ? 0.17373 0.16992 0.15197 0.01490  -0.02548 0.00883  375 SER A N   
2959 C CA  . SER A 375 ? 0.16686 0.16052 0.14228 0.01478  -0.02389 0.01009  375 SER A CA  
2960 C C   . SER A 375 ? 0.14914 0.14153 0.12768 0.01585  -0.02077 0.00857  375 SER A C   
2961 O O   . SER A 375 ? 0.11740 0.11034 0.10141 0.01717  -0.02045 0.00795  375 SER A O   
2962 C CB  . SER A 375 ? 0.16484 0.15744 0.14110 0.01544  -0.02627 0.01375  375 SER A CB  
2963 O OG  . SER A 375 ? 0.17177 0.16171 0.14551 0.01522  -0.02464 0.01500  375 SER A OG  
2964 N N   . TRP A 376 ? 0.14920 0.14008 0.12418 0.01506  -0.01844 0.00791  376 TRP A N   
2965 C CA  . TRP A 376 ? 0.12896 0.11866 0.10636 0.01581  -0.01571 0.00677  376 TRP A CA  
2966 C C   . TRP A 376 ? 0.11600 0.10432 0.09700 0.01712  -0.01568 0.00859  376 TRP A C   
2967 O O   . TRP A 376 ? 0.13437 0.12220 0.11851 0.01779  -0.01378 0.00754  376 TRP A O   
2968 C CB  . TRP A 376 ? 0.14950 0.13815 0.12264 0.01463  -0.01348 0.00582  376 TRP A CB  
2969 C CG  . TRP A 376 ? 0.11663 0.10395 0.08532 0.01364  -0.01389 0.00797  376 TRP A CG  
2970 C CD1 . TRP A 376 ? 0.13347 0.12126 0.09685 0.01189  -0.01497 0.00848  376 TRP A CD1 
2971 C CD2 . TRP A 376 ? 0.13461 0.11984 0.10348 0.01401  -0.01317 0.00992  376 TRP A CD2 
2972 N NE1 . TRP A 376 ? 0.15543 0.14150 0.11541 0.01105  -0.01505 0.01084  376 TRP A NE1 
2973 C CE2 . TRP A 376 ? 0.16460 0.14896 0.12807 0.01243  -0.01397 0.01178  376 TRP A CE2 
2974 C CE3 . TRP A 376 ? 0.14810 0.13207 0.12099 0.01527  -0.01187 0.01017  376 TRP A CE3 
2975 C CZ2 . TRP A 376 ? 0.15425 0.13631 0.11643 0.01218  -0.01358 0.01407  376 TRP A CZ2 
2976 C CZ3 . TRP A 376 ? 0.15170 0.13347 0.12355 0.01512  -0.01139 0.01218  376 TRP A CZ3 
2977 C CH2 . TRP A 376 ? 0.13268 0.11340 0.09932 0.01365  -0.01228 0.01420  376 TRP A CH2 
2978 N N   . GLU A 377 ? 0.13164 0.11924 0.11229 0.01737  -0.01780 0.01132  377 GLU A N   
2979 C CA  . GLU A 377 ? 0.15538 0.14157 0.14053 0.01878  -0.01794 0.01290  377 GLU A CA  
2980 C C   . GLU A 377 ? 0.13577 0.12357 0.12757 0.02013  -0.01807 0.01159  377 GLU A C   
2981 O O   . GLU A 377 ? 0.16207 0.14906 0.15799 0.02100  -0.01646 0.01105  377 GLU A O   
2982 C CB  . GLU A 377 ? 0.16529 0.15037 0.14925 0.01879  -0.02076 0.01636  377 GLU A CB  
2983 C CG  . GLU A 377 ? 0.15751 0.14051 0.13507 0.01722  -0.02027 0.01797  377 GLU A CG  
2984 C CD  . GLU A 377 ? 0.25202 0.23424 0.22707 0.01661  -0.02367 0.02160  377 GLU A CD  
2985 O OE1 . GLU A 377 ? 0.35398 0.33820 0.32837 0.01624  -0.02638 0.02211  377 GLU A OE1 
2986 O OE2 . GLU A 377 ? 0.28525 0.26479 0.25896 0.01636  -0.02378 0.02408  377 GLU A OE2 
2987 N N   . ARG A 378 ? 0.15046 0.14066 0.14331 0.02007  -0.01981 0.01085  378 ARG A N   
2988 C CA  . ARG A 378 ? 0.16756 0.15961 0.16663 0.02103  -0.01973 0.00933  378 ARG A CA  
2989 C C   . ARG A 378 ? 0.12164 0.11375 0.12140 0.02061  -0.01670 0.00667  378 ARG A C   
2990 O O   . ARG A 378 ? 0.15028 0.14271 0.15480 0.02119  -0.01539 0.00563  378 ARG A O   
2991 C CB  . ARG A 378 ? 0.17758 0.17231 0.17721 0.02075  -0.02223 0.00904  378 ARG A CB  
2992 C CG  . ARG A 378 ? 0.17503 0.17019 0.17461 0.02106  -0.02582 0.01188  378 ARG A CG  
2993 C CD  . ARG A 378 ? 0.20438 0.19927 0.21086 0.02289  -0.02687 0.01339  378 ARG A CD  
2994 N NE  . ARG A 378 ? 0.16468 0.15639 0.17007 0.02329  -0.02623 0.01543  378 ARG A NE  
2995 C CZ  . ARG A 378 ? 0.22234 0.21251 0.22466 0.02302  -0.02864 0.01869  378 ARG A CZ  
2996 N NH1 . ARG A 378 ? 0.24945 0.24109 0.24918 0.02225  -0.03199 0.02036  378 ARG A NH1 
2997 N NH2 . ARG A 378 ? 0.24387 0.23092 0.24545 0.02327  -0.02772 0.02037  378 ARG A NH2 
2998 N N   . GLY A 379 ? 0.10610 0.09795 0.10131 0.01945  -0.01560 0.00552  379 GLY A N   
2999 C CA  . GLY A 379 ? 0.12423 0.11591 0.11995 0.01897  -0.01314 0.00350  379 GLY A CA  
3000 C C   . GLY A 379 ? 0.12610 0.11591 0.12212 0.01913  -0.01106 0.00380  379 GLY A C   
3001 O O   . GLY A 379 ? 0.10860 0.09852 0.10707 0.01895  -0.00937 0.00253  379 GLY A O   
3002 N N   . MET A 380 ? 0.12627 0.11437 0.11953 0.01918  -0.01114 0.00546  380 MET A N   
3003 C CA  . MET A 380 ? 0.12816 0.11443 0.12181 0.01924  -0.00920 0.00577  380 MET A CA  
3004 C C   . MET A 380 ? 0.10159 0.08770 0.10065 0.02016  -0.00886 0.00581  380 MET A C   
3005 O O   . MET A 380 ? 0.09489 0.08031 0.09551 0.01990  -0.00675 0.00484  380 MET A O   
3006 C CB  . MET A 380 ? 0.13399 0.11841 0.12371 0.01894  -0.00949 0.00770  380 MET A CB  
3007 C CG  . MET A 380 ? 0.15126 0.13378 0.14074 0.01869  -0.00732 0.00784  380 MET A CG  
3008 S SD  . MET A 380 ? 0.23995 0.22019 0.22495 0.01808  -0.00770 0.01034  380 MET A SD  
3009 C CE  . MET A 380 ? 0.14803 0.12733 0.13635 0.01935  -0.01037 0.01296  380 MET A CE  
3010 N N   . GLU A 381 ? 0.13457 0.12149 0.13684 0.02114  -0.01090 0.00675  381 GLU A N   
3011 C CA  . GLU A 381 ? 0.11727 0.10439 0.12583 0.02211  -0.01046 0.00632  381 GLU A CA  
3012 C C   . GLU A 381 ? 0.09556 0.08450 0.10689 0.02148  -0.00866 0.00358  381 GLU A C   
3013 O O   . GLU A 381 ? 0.11442 0.10315 0.12948 0.02147  -0.00677 0.00236  381 GLU A O   
3014 C CB  . GLU A 381 ? 0.11247 0.10049 0.12457 0.02337  -0.01337 0.00790  381 GLU A CB  
3015 C CG  . GLU A 381 ? 0.12287 0.10873 0.13287 0.02385  -0.01538 0.01109  381 GLU A CG  
3016 C CD  . GLU A 381 ? 0.16518 0.15233 0.17749 0.02474  -0.01900 0.01300  381 GLU A CD  
3017 O OE1 . GLU A 381 ? 0.18173 0.17157 0.19823 0.02520  -0.01976 0.01163  381 GLU A OE1 
3018 O OE2 . GLU A 381 ? 0.21679 0.20233 0.22662 0.02479  -0.02119 0.01599  381 GLU A OE2 
3019 N N   . VAL A 382 ? 0.07456 0.06521 0.08401 0.02071  -0.00913 0.00254  382 VAL A N   
3020 C CA  . VAL A 382 ? 0.11931 0.11156 0.13086 0.01976  -0.00763 0.00024  382 VAL A CA  
3021 C C   . VAL A 382 ? 0.11878 0.10989 0.12776 0.01849  -0.00529 -0.00064 382 VAL A C   
3022 O O   . VAL A 382 ? 0.07603 0.06765 0.08723 0.01760  -0.00345 -0.00217 382 VAL A O   
3023 C CB  . VAL A 382 ? 0.12457 0.11870 0.13506 0.01925  -0.00906 -0.00040 382 VAL A CB  
3024 C CG1 . VAL A 382 ? 0.12933 0.12467 0.14097 0.01784  -0.00748 -0.00247 382 VAL A CG1 
3025 C CG2 . VAL A 382 ? 0.08627 0.08208 0.10014 0.02032  -0.01141 0.00027  382 VAL A CG2 
3026 N N   . PHE A 383 ? 0.12851 0.11829 0.13288 0.01820  -0.00533 0.00021  383 PHE A N   
3027 C CA  . PHE A 383 ? 0.11475 0.10365 0.11710 0.01707  -0.00345 -0.00044 383 PHE A CA  
3028 C C   . PHE A 383 ? 0.11215 0.09981 0.11617 0.01707  -0.00175 -0.00042 383 PHE A C   
3029 O O   . PHE A 383 ? 0.12741 0.11522 0.13194 0.01584  0.00000  -0.00164 383 PHE A O   
3030 C CB  . PHE A 383 ? 0.14173 0.12972 0.13968 0.01691  -0.00381 0.00028  383 PHE A CB  
3031 C CG  . PHE A 383 ? 0.11499 0.10392 0.11147 0.01629  -0.00447 -0.00054 383 PHE A CG  
3032 C CD1 . PHE A 383 ? 0.10812 0.09850 0.10658 0.01600  -0.00517 -0.00142 383 PHE A CD1 
3033 C CD2 . PHE A 383 ? 0.14457 0.13290 0.13815 0.01593  -0.00426 -0.00059 383 PHE A CD2 
3034 C CE1 . PHE A 383 ? 0.12179 0.11264 0.11907 0.01536  -0.00579 -0.00212 383 PHE A CE1 
3035 C CE2 . PHE A 383 ? 0.11195 0.10085 0.10489 0.01546  -0.00485 -0.00144 383 PHE A CE2 
3036 C CZ  . PHE A 383 ? 0.08796 0.07794 0.08263 0.01516  -0.00566 -0.00211 383 PHE A CZ  
3037 N N   . GLU A 384 ? 0.12708 0.11340 0.13184 0.01823  -0.00232 0.00099  384 GLU A N   
3038 C CA  . GLU A 384 ? 0.12541 0.11014 0.13199 0.01826  -0.00069 0.00102  384 GLU A CA  
3039 C C   . GLU A 384 ? 0.16813 0.15387 0.17958 0.01791  0.00078  -0.00090 384 GLU A C   
3040 O O   . GLU A 384 ? 0.16401 0.14890 0.17653 0.01712  0.00287  -0.00189 384 GLU A O   
3041 C CB  . GLU A 384 ? 0.15929 0.14225 0.16626 0.01961  -0.00205 0.00320  384 GLU A CB  
3042 C CG  . GLU A 384 ? 0.20160 0.18256 0.21175 0.02007  -0.00091 0.00353  384 GLU A CG  
3043 C CD  . GLU A 384 ? 0.23786 0.21665 0.24730 0.02114  -0.00268 0.00631  384 GLU A CD  
3044 O OE1 . GLU A 384 ? 0.31040 0.28965 0.31701 0.02144  -0.00492 0.00789  384 GLU A OE1 
3045 O OE2 . GLU A 384 ? 0.28636 0.26293 0.29791 0.02145  -0.00183 0.00691  384 GLU A OE2 
3046 N N   . GLU A 385 ? 0.13560 0.12329 0.15007 0.01829  -0.00013 -0.00167 385 GLU A N   
3047 C CA  . GLU A 385 ? 0.13071 0.11980 0.15019 0.01778  0.00146  -0.00386 385 GLU A CA  
3048 C C   . GLU A 385 ? 0.12205 0.11226 0.13965 0.01543  0.00338  -0.00580 385 GLU A C   
3049 O O   . GLU A 385 ? 0.11909 0.10948 0.13875 0.01420  0.00571  -0.00762 385 GLU A O   
3050 C CB  . GLU A 385 ? 0.10921 0.10033 0.13270 0.01886  -0.00025 -0.00404 385 GLU A CB  
3051 C CG  . GLU A 385 ? 0.15936 0.15254 0.18837 0.01816  0.00150  -0.00669 385 GLU A CG  
3052 C CD  . GLU A 385 ? 0.17680 0.17227 0.21018 0.01930  -0.00035 -0.00682 385 GLU A CD  
3053 O OE1 . GLU A 385 ? 0.25822 0.25363 0.28977 0.02047  -0.00314 -0.00475 385 GLU A OE1 
3054 O OE2 . GLU A 385 ? 0.22776 0.22529 0.26643 0.01883  0.00106  -0.00916 385 GLU A OE2 
3055 N N   . HIS A 386 ? 0.11967 0.11056 0.13339 0.01460  0.00242  -0.00542 386 HIS A N   
3056 C CA  . HIS A 386 ? 0.11931 0.11129 0.13142 0.01226  0.00363  -0.00682 386 HIS A CA  
3057 C C   . HIS A 386 ? 0.10191 0.09270 0.10965 0.01103  0.00414  -0.00620 386 HIS A C   
3058 O O   . HIS A 386 ? 0.10006 0.09146 0.10671 0.00881  0.00538  -0.00721 386 HIS A O   
3059 C CB  . HIS A 386 ? 0.08805 0.08155 0.09958 0.01193  0.00214  -0.00690 386 HIS A CB  
3060 C CG  . HIS A 386 ? 0.12434 0.11970 0.14050 0.01259  0.00180  -0.00792 386 HIS A CG  
3061 N ND1 . HIS A 386 ? 0.11110 0.10806 0.13093 0.01129  0.00375  -0.01011 386 HIS A ND1 
3062 C CD2 . HIS A 386 ? 0.13235 0.12851 0.15029 0.01425  -0.00026 -0.00718 386 HIS A CD2 
3063 C CE1 . HIS A 386 ? 0.11240 0.11113 0.13662 0.01233  0.00293  -0.01073 386 HIS A CE1 
3064 N NE2 . HIS A 386 ? 0.12230 0.12059 0.14540 0.01414  0.00033  -0.00883 386 HIS A NE2 
3065 N N   . LEU A 387 ? 0.11648 0.10580 0.12178 0.01221  0.00318  -0.00458 387 LEU A N   
3066 C CA  . LEU A 387 ? 0.08661 0.07518 0.08839 0.01121  0.00344  -0.00403 387 LEU A CA  
3067 C C   . LEU A 387 ? 0.10312 0.09107 0.10508 0.00998  0.00547  -0.00472 387 LEU A C   
3068 O O   . LEU A 387 ? 0.12051 0.10729 0.12398 0.01089  0.00627  -0.00460 387 LEU A O   
3069 C CB  . LEU A 387 ? 0.09683 0.08431 0.09639 0.01269  0.00217  -0.00251 387 LEU A CB  
3070 C CG  . LEU A 387 ? 0.13069 0.11825 0.12751 0.01235  0.00124  -0.00205 387 LEU A CG  
3071 C CD1 . LEU A 387 ? 0.12966 0.11831 0.12674 0.01195  0.00008  -0.00248 387 LEU A CD1 
3072 C CD2 . LEU A 387 ? 0.13126 0.11792 0.12627 0.01367  0.00052  -0.00103 387 LEU A CD2 
3073 N N   . ILE A 388 ? 0.08861 0.07724 0.08898 0.00776  0.00619  -0.00536 388 ILE A N   
3074 C CA  . ILE A 388 ? 0.08728 0.07554 0.08731 0.00618  0.00806  -0.00614 388 ILE A CA  
3075 C C   . ILE A 388 ? 0.09280 0.07978 0.09093 0.00676  0.00795  -0.00497 388 ILE A C   
3076 O O   . ILE A 388 ? 0.09590 0.08232 0.09401 0.00575  0.00951  -0.00555 388 ILE A O   
3077 C CB  . ILE A 388 ? 0.08457 0.07412 0.08291 0.00317  0.00861  -0.00696 388 ILE A CB  
3078 C CG1 . ILE A 388 ? 0.07271 0.06240 0.06829 0.00280  0.00667  -0.00541 388 ILE A CG1 
3079 C CG2 . ILE A 388 ? 0.10035 0.09130 0.10044 0.00205  0.00925  -0.00846 388 ILE A CG2 
3080 C CD1 . ILE A 388 ? 0.13889 0.12952 0.13236 -0.00032 0.00673  -0.00552 388 ILE A CD1 
3081 N N   . ASP A 389 ? 0.09990 0.08654 0.09655 0.00814  0.00633  -0.00359 389 ASP A N   
3082 C CA  . ASP A 389 ? 0.07669 0.06238 0.07179 0.00867  0.00639  -0.00267 389 ASP A CA  
3083 C C   . ASP A 389 ? 0.08824 0.07267 0.08339 0.01073  0.00585  -0.00168 389 ASP A C   
3084 O O   . ASP A 389 ? 0.07173 0.05571 0.06510 0.01127  0.00546  -0.00086 389 ASP A O   
3085 C CB  . ASP A 389 ? 0.07238 0.05887 0.06580 0.00817  0.00522  -0.00211 389 ASP A CB  
3086 C CG  . ASP A 389 ? 0.08172 0.06861 0.07505 0.00925  0.00350  -0.00173 389 ASP A CG  
3087 O OD1 . ASP A 389 ? 0.11995 0.10659 0.11399 0.01051  0.00308  -0.00170 389 ASP A OD1 
3088 O OD2 . ASP A 389 ? 0.06309 0.05057 0.05593 0.00881  0.00247  -0.00146 389 ASP A OD2 
3089 N N   . GLN A 390 ? 0.10365 0.08764 0.10090 0.01174  0.00577  -0.00174 390 GLN A N   
3090 C CA  . GLN A 390 ? 0.12369 0.10654 0.12074 0.01348  0.00474  -0.00039 390 GLN A CA  
3091 C C   . GLN A 390 ? 0.12556 0.10661 0.12133 0.01348  0.00566  0.00047  390 GLN A C   
3092 O O   . GLN A 390 ? 0.13856 0.11861 0.13579 0.01291  0.00718  -0.00001 390 GLN A O   
3093 C CB  . GLN A 390 ? 0.14510 0.12791 0.14554 0.01455  0.00426  -0.00048 390 GLN A CB  
3094 C CG  . GLN A 390 ? 0.17716 0.15884 0.18087 0.01449  0.00585  -0.00112 390 GLN A CG  
3095 C CD  . GLN A 390 ? 0.19650 0.17581 0.20044 0.01570  0.00549  0.00060  390 GLN A CD  
3096 O OE1 . GLN A 390 ? 0.24207 0.22090 0.24443 0.01678  0.00365  0.00237  390 GLN A OE1 
3097 N NE2 . GLN A 390 ? 0.12285 0.10056 0.12854 0.01527  0.00723  0.00013  390 GLN A NE2 
3098 N N   . ASP A 391 ? 0.13416 0.11487 0.12712 0.01383  0.00497  0.00151  391 ASP A N   
3099 C CA  . ASP A 391 ? 0.14164 0.12073 0.13288 0.01359  0.00585  0.00241  391 ASP A CA  
3100 C C   . ASP A 391 ? 0.14631 0.12427 0.13593 0.01459  0.00452  0.00412  391 ASP A C   
3101 O O   . ASP A 391 ? 0.10846 0.08745 0.09632 0.01491  0.00326  0.00429  391 ASP A O   
3102 C CB  . ASP A 391 ? 0.11573 0.09578 0.10498 0.01256  0.00655  0.00186  391 ASP A CB  
3103 C CG  . ASP A 391 ? 0.15343 0.13210 0.14139 0.01188  0.00794  0.00238  391 ASP A CG  
3104 O OD1 . ASP A 391 ? 0.15263 0.12980 0.13894 0.01229  0.00769  0.00372  391 ASP A OD1 
3105 O OD2 . ASP A 391 ? 0.15294 0.13207 0.14140 0.01071  0.00919  0.00153  391 ASP A OD2 
3106 N N   . HIS A 392 ? 0.15645 0.13221 0.14667 0.01489  0.00474  0.00541  392 HIS A N   
3107 C CA  . HIS A 392 ? 0.17827 0.15266 0.16695 0.01561  0.00312  0.00754  392 HIS A CA  
3108 C C   . HIS A 392 ? 0.15192 0.12700 0.13604 0.01498  0.00263  0.00799  392 HIS A C   
3109 O O   . HIS A 392 ? 0.15812 0.13397 0.14081 0.01539  0.00089  0.00858  392 HIS A O   
3110 C CB  . HIS A 392 ? 0.19538 0.16682 0.18482 0.01557  0.00374  0.00903  392 HIS A CB  
3111 C CG  . HIS A 392 ? 0.20178 0.17145 0.19002 0.01619  0.00170  0.01173  392 HIS A CG  
3112 N ND1 . HIS A 392 ? 0.23705 0.20684 0.22821 0.01758  -0.00042 0.01267  392 HIS A ND1 
3113 C CD2 . HIS A 392 ? 0.20569 0.17351 0.19003 0.01539  0.00131  0.01384  392 HIS A CD2 
3114 C CE1 . HIS A 392 ? 0.25783 0.22588 0.24693 0.01767  -0.00233 0.01546  392 HIS A CE1 
3115 N NE2 . HIS A 392 ? 0.23894 0.20567 0.22357 0.01623  -0.00126 0.01625  392 HIS A NE2 
3116 N N   . TYR A 393 ? 0.08343 0.05851 0.06546 0.01383  0.00429  0.00740  393 TYR A N   
3117 C CA  . TYR A 393 ? 0.11546 0.09127 0.09355 0.01300  0.00437  0.00740  393 TYR A CA  
3118 C C   . TYR A 393 ? 0.12199 0.10033 0.10020 0.01312  0.00407  0.00557  393 TYR A C   
3119 O O   . TYR A 393 ? 0.09532 0.07441 0.07089 0.01283  0.00347  0.00545  393 TYR A O   
3120 C CB  . TYR A 393 ? 0.13264 0.10777 0.10917 0.01167  0.00642  0.00723  393 TYR A CB  
3121 C CG  . TYR A 393 ? 0.12011 0.09231 0.09556 0.01122  0.00667  0.00932  393 TYR A CG  
3122 C CD1 . TYR A 393 ? 0.12800 0.09862 0.10106 0.01130  0.00499  0.01161  393 TYR A CD1 
3123 C CD2 . TYR A 393 ? 0.15478 0.12569 0.13161 0.01057  0.00841  0.00912  393 TYR A CD2 
3124 C CE1 . TYR A 393 ? 0.15335 0.12092 0.12558 0.01084  0.00493  0.01389  393 TYR A CE1 
3125 C CE2 . TYR A 393 ? 0.23147 0.19931 0.20758 0.01012  0.00863  0.01109  393 TYR A CE2 
3126 C CZ  . TYR A 393 ? 0.19125 0.15730 0.16514 0.01031  0.00682  0.01359  393 TYR A CZ  
3127 O OH  . TYR A 393 ? 0.20842 0.17106 0.18173 0.00981  0.00676  0.01592  393 TYR A OH  
3128 N N   . LEU A 394 ? 0.10880 0.08835 0.08993 0.01337  0.00444  0.00416  394 LEU A N   
3129 C CA  . LEU A 394 ? 0.12882 0.11039 0.11043 0.01341  0.00408  0.00263  394 LEU A CA  
3130 C C   . LEU A 394 ? 0.12133 0.10354 0.10334 0.01423  0.00228  0.00264  394 LEU A C   
3131 O O   . LEU A 394 ? 0.10772 0.09093 0.08848 0.01420  0.00170  0.00189  394 LEU A O   
3132 C CB  . LEU A 394 ? 0.11316 0.09566 0.09739 0.01306  0.00479  0.00153  394 LEU A CB  
3133 C CG  . LEU A 394 ? 0.11335 0.09562 0.09765 0.01209  0.00646  0.00134  394 LEU A CG  
3134 C CD1 . LEU A 394 ? 0.10370 0.08726 0.09030 0.01147  0.00667  0.00040  394 LEU A CD1 
3135 C CD2 . LEU A 394 ? 0.06721 0.04991 0.04955 0.01158  0.00730  0.00101  394 LEU A CD2 
3136 N N   . ASN A 395 ? 0.09472 0.07649 0.07885 0.01489  0.00152  0.00322  395 ASN A N   
3137 C CA  . ASN A 395 ? 0.10458 0.08716 0.08960 0.01561  -0.00022 0.00324  395 ASN A CA  
3138 C C   . ASN A 395 ? 0.12527 0.10764 0.10730 0.01568  -0.00151 0.00426  395 ASN A C   
3139 O O   . ASN A 395 ? 0.11680 0.10036 0.09793 0.01567  -0.00255 0.00357  395 ASN A O   
3140 C CB  . ASN A 395 ? 0.08421 0.06635 0.07250 0.01623  -0.00048 0.00367  395 ASN A CB  
3141 C CG  . ASN A 395 ? 0.13214 0.11577 0.12280 0.01666  -0.00161 0.00288  395 ASN A CG  
3142 O OD1 . ASN A 395 ? 0.16568 0.14959 0.15692 0.01738  -0.00320 0.00361  395 ASN A OD1 
3143 N ND2 . ASN A 395 ? 0.17152 0.15614 0.16345 0.01602  -0.00090 0.00150  395 ASN A ND2 
3144 N N   . ALA A 396 ? 0.12696 0.10771 0.10720 0.01551  -0.00151 0.00597  396 ALA A N   
3145 C CA  . ALA A 396 ? 0.12137 0.10180 0.09813 0.01515  -0.00296 0.00736  396 ALA A CA  
3146 C C   . ALA A 396 ? 0.13174 0.11308 0.10474 0.01394  -0.00210 0.00613  396 ALA A C   
3147 O O   . ALA A 396 ? 0.10034 0.08253 0.07084 0.01346  -0.00329 0.00604  396 ALA A O   
3148 C CB  . ALA A 396 ? 0.15162 0.12974 0.12734 0.01502  -0.00322 0.00980  396 ALA A CB  
3149 N N   . ALA A 397 ? 0.12621 0.10757 0.09901 0.01331  0.00001  0.00500  397 ALA A N   
3150 C CA  . ALA A 397 ? 0.14481 0.12723 0.11495 0.01218  0.00116  0.00344  397 ALA A CA  
3151 C C   . ALA A 397 ? 0.11682 0.10100 0.08855 0.01256  0.00075  0.00133  397 ALA A C   
3152 O O   . ALA A 397 ? 0.13652 0.12159 0.10586 0.01180  0.00065  0.00025  397 ALA A O   
3153 C CB  . ALA A 397 ? 0.13686 0.11917 0.10741 0.01152  0.00345  0.00265  397 ALA A CB  
3154 N N   . ASN A 398 ? 0.13148 0.11611 0.10711 0.01351  0.00056  0.00067  398 ASN A N   
3155 C CA  . ASN A 398 ? 0.12486 0.11076 0.10220 0.01380  0.00001  -0.00105 398 ASN A CA  
3156 C C   . ASN A 398 ? 0.12289 0.10918 0.09954 0.01407  -0.00190 -0.00074 398 ASN A C   
3157 O O   . ASN A 398 ? 0.12055 0.10777 0.09743 0.01393  -0.00230 -0.00227 398 ASN A O   
3158 C CB  . ASN A 398 ? 0.10697 0.09309 0.08814 0.01433  0.00017  -0.00149 398 ASN A CB  
3159 C CG  . ASN A 398 ? 0.10267 0.08903 0.08497 0.01395  0.00172  -0.00226 398 ASN A CG  
3160 O OD1 . ASN A 398 ? 0.11560 0.10282 0.09922 0.01387  0.00207  -0.00377 398 ASN A OD1 
3161 N ND2 . ASN A 398 ? 0.10437 0.09002 0.08660 0.01370  0.00263  -0.00128 398 ASN A ND2 
3162 N N   . TRP A 399 ? 0.09737 0.08301 0.07363 0.01445  -0.00315 0.00117  399 TRP A N   
3163 C CA  . TRP A 399 ? 0.11651 0.10285 0.09225 0.01462  -0.00521 0.00160  399 TRP A CA  
3164 C C   . TRP A 399 ? 0.13977 0.12639 0.11089 0.01341  -0.00565 0.00164  399 TRP A C   
3165 O O   . TRP A 399 ? 0.09612 0.08389 0.06629 0.01298  -0.00666 0.00060  399 TRP A O   
3166 C CB  . TRP A 399 ? 0.14461 0.13035 0.12232 0.01551  -0.00655 0.00361  399 TRP A CB  
3167 C CG  . TRP A 399 ? 0.13530 0.12178 0.11739 0.01635  -0.00684 0.00291  399 TRP A CG  
3168 C CD1 . TRP A 399 ? 0.13045 0.11643 0.11562 0.01678  -0.00577 0.00289  399 TRP A CD1 
3169 C CD2 . TRP A 399 ? 0.10722 0.09518 0.09084 0.01649  -0.00812 0.00195  399 TRP A CD2 
3170 N NE1 . TRP A 399 ? 0.10843 0.09555 0.09675 0.01705  -0.00623 0.00198  399 TRP A NE1 
3171 C CE2 . TRP A 399 ? 0.09899 0.08730 0.08655 0.01694  -0.00769 0.00146  399 TRP A CE2 
3172 C CE3 . TRP A 399 ? 0.11443 0.10352 0.09635 0.01603  -0.00947 0.00132  399 TRP A CE3 
3173 C CZ2 . TRP A 399 ? 0.10117 0.09086 0.09102 0.01695  -0.00855 0.00050  399 TRP A CZ2 
3174 C CZ3 . TRP A 399 ? 0.10855 0.09895 0.09298 0.01619  -0.01043 0.00035  399 TRP A CZ3 
3175 C CH2 . TRP A 399 ? 0.07565 0.06631 0.06401 0.01665  -0.00995 0.00001  399 TRP A CH2 
3176 N N   . MET A 400 ? 0.13669 0.12228 0.10465 0.01255  -0.00483 0.00275  400 MET A N   
3177 C CA  . MET A 400 ? 0.14895 0.13490 0.11181 0.01082  -0.00479 0.00253  400 MET A CA  
3178 C C   . MET A 400 ? 0.13569 0.12290 0.09822 0.01002  -0.00298 -0.00067 400 MET A C   
3179 O O   . MET A 400 ? 0.13742 0.12558 0.09668 0.00863  -0.00315 -0.00185 400 MET A O   
3180 C CB  . MET A 400 ? 0.15756 0.14200 0.11711 0.00978  -0.00400 0.00440  400 MET A CB  
3181 C CG  . MET A 400 ? 0.20302 0.18590 0.16270 0.01040  -0.00610 0.00776  400 MET A CG  
3182 S SD  . MET A 400 ? 0.16553 0.14619 0.12069 0.00878  -0.00540 0.01026  400 MET A SD  
3183 C CE  . MET A 400 ? 0.15975 0.13966 0.11833 0.00947  -0.00236 0.00894  400 MET A CE  
3184 N N   . TRP A 401 ? 0.13565 0.12292 0.10175 0.01080  -0.00132 -0.00214 401 TRP A N   
3185 C CA  . TRP A 401 ? 0.14318 0.13156 0.11044 0.01040  0.00019  -0.00517 401 TRP A CA  
3186 C C   . TRP A 401 ? 0.14525 0.13443 0.11404 0.01077  -0.00113 -0.00652 401 TRP A C   
3187 O O   . TRP A 401 ? 0.17981 0.16986 0.14686 0.00968  -0.00072 -0.00858 401 TRP A O   
3188 C CB  . TRP A 401 ? 0.13341 0.12166 0.10475 0.01126  0.00165  -0.00589 401 TRP A CB  
3189 C CG  . TRP A 401 ? 0.16361 0.15288 0.13737 0.01111  0.00310  -0.00883 401 TRP A CG  
3190 C CD1 . TRP A 401 ? 0.15786 0.14763 0.13412 0.01154  0.00253  -0.01061 401 TRP A CD1 
3191 C CD2 . TRP A 401 ? 0.18425 0.17413 0.15893 0.01057  0.00535  -0.01035 401 TRP A CD2 
3192 N NE1 . TRP A 401 ? 0.18478 0.17527 0.16373 0.01142  0.00421  -0.01313 401 TRP A NE1 
3193 C CE2 . TRP A 401 ? 0.21641 0.20718 0.19461 0.01086  0.00597  -0.01308 401 TRP A CE2 
3194 C CE3 . TRP A 401 ? 0.19789 0.18766 0.17108 0.00981  0.00692  -0.00973 401 TRP A CE3 
3195 C CZ2 . TRP A 401 ? 0.18314 0.17494 0.16394 0.01057  0.00806  -0.01529 401 TRP A CZ2 
3196 C CZ3 . TRP A 401 ? 0.17024 0.16117 0.14555 0.00935  0.00908  -0.01195 401 TRP A CZ3 
3197 C CH2 . TRP A 401 ? 0.20996 0.20201 0.18929 0.00981  0.00962  -0.01474 401 TRP A CH2 
3198 N N   . LEU A 402 ? 0.13403 0.12297 0.10608 0.01207  -0.00255 -0.00557 402 LEU A N   
3199 C CA  . LEU A 402 ? 0.13394 0.12354 0.10781 0.01233  -0.00371 -0.00682 402 LEU A CA  
3200 C C   . LEU A 402 ? 0.16606 0.15642 0.13662 0.01142  -0.00529 -0.00662 402 LEU A C   
3201 O O   . LEU A 402 ? 0.16545 0.15656 0.13616 0.01091  -0.00565 -0.00850 402 LEU A O   
3202 C CB  . LEU A 402 ? 0.10924 0.09854 0.08694 0.01353  -0.00472 -0.00577 402 LEU A CB  
3203 C CG  . LEU A 402 ? 0.12205 0.11105 0.10353 0.01402  -0.00393 -0.00685 402 LEU A CG  
3204 C CD1 . LEU A 402 ? 0.12400 0.11331 0.10658 0.01367  -0.00392 -0.00916 402 LEU A CD1 
3205 C CD2 . LEU A 402 ? 0.15666 0.14525 0.13856 0.01405  -0.00224 -0.00682 402 LEU A CD2 
3206 N N   . SER A 403 ? 0.11784 0.10797 0.08556 0.01113  -0.00639 -0.00429 403 SER A N   
3207 C CA  . SER A 403 ? 0.13306 0.12407 0.09734 0.01005  -0.00829 -0.00368 403 SER A CA  
3208 C C   . SER A 403 ? 0.13371 0.12516 0.09278 0.00789  -0.00723 -0.00497 403 SER A C   
3209 O O   . SER A 403 ? 0.13040 0.12264 0.08561 0.00648  -0.00885 -0.00433 403 SER A O   
3210 C CB  . SER A 403 ? 0.13829 0.12878 0.10220 0.01063  -0.01035 -0.00033 403 SER A CB  
3211 O OG  . SER A 403 ? 0.13027 0.11931 0.09281 0.01058  -0.00924 0.00126  403 SER A OG  
3212 N N   . ALA A 404 ? 0.13200 0.12318 0.09099 0.00742  -0.00456 -0.00684 404 ALA A N   
3213 C CA  . ALA A 404 ? 0.17418 0.16598 0.12848 0.00511  -0.00288 -0.00857 404 ALA A CA  
3214 C C   . ALA A 404 ? 0.17340 0.16479 0.12194 0.00350  -0.00396 -0.00579 404 ALA A C   
3215 O O   . ALA A 404 ? 0.18594 0.17818 0.12920 0.00106  -0.00403 -0.00645 404 ALA A O   
3216 C CB  . ALA A 404 ? 0.19720 0.19034 0.15063 0.00385  -0.00274 -0.01169 404 ALA A CB  
3217 N N   . SER A 405 ? 0.13927 0.12924 0.08875 0.00468  -0.00485 -0.00262 405 SER A N   
3218 C CA  . SER A 405 ? 0.20944 0.19847 0.15409 0.00333  -0.00605 0.00052  405 SER A CA  
3219 C C   . SER A 405 ? 0.17691 0.16481 0.11972 0.00243  -0.00361 0.00083  405 SER A C   
3220 O O   . SER A 405 ? 0.21930 0.20628 0.15714 0.00066  -0.00417 0.00314  405 SER A O   
3221 C CB  . SER A 405 ? 0.17768 0.16568 0.12488 0.00514  -0.00898 0.00404  405 SER A CB  
3222 O OG  . SER A 405 ? 0.15237 0.14171 0.10129 0.00577  -0.01131 0.00382  405 SER A OG  
3223 N N   . ALA A 406 ? 0.25077 0.23873 0.19747 0.00346  -0.00109 -0.00129 406 ALA A N   
3224 C CA  . ALA A 406 ? 0.20463 0.19191 0.15035 0.00262  0.00141  -0.00140 406 ALA A CA  
3225 C C   . ALA A 406 ? 0.19742 0.18569 0.14805 0.00365  0.00386  -0.00462 406 ALA A C   
3226 O O   . ALA A 406 ? 0.20433 0.19291 0.15981 0.00560  0.00314  -0.00544 406 ALA A O   
3227 C CB  . ALA A 406 ? 0.21233 0.19747 0.15887 0.00362  0.00051  0.00210  406 ALA A CB  
3228 N N   . PHE A 407 ? 0.20900 0.19785 0.15843 0.00217  0.00666  -0.00639 407 PHE A N   
3229 C CA  . PHE A 407 ? 0.19851 0.18843 0.15298 0.00302  0.00898  -0.00926 407 PHE A CA  
3230 C C   . PHE A 407 ? 0.23953 0.23098 0.19692 0.00340  0.00941  -0.01270 407 PHE A C   
3231 O O   . PHE A 407 ? 0.22909 0.22180 0.18952 0.00322  0.01172  -0.01575 407 PHE A O   
3232 C CB  . PHE A 407 ? 0.20525 0.19420 0.16472 0.00533  0.00830  -0.00768 407 PHE A CB  
3233 C CG  . PHE A 407 ? 0.21020 0.19732 0.16763 0.00521  0.00774  -0.00439 407 PHE A CG  
3234 C CD1 . PHE A 407 ? 0.20958 0.19634 0.16404 0.00346  0.00963  -0.00405 407 PHE A CD1 
3235 C CD2 . PHE A 407 ? 0.21761 0.20334 0.17650 0.00678  0.00546  -0.00180 407 PHE A CD2 
3236 C CE1 . PHE A 407 ? 0.20894 0.19363 0.16179 0.00331  0.00910  -0.00097 407 PHE A CE1 
3237 C CE2 . PHE A 407 ? 0.17256 0.15638 0.13031 0.00676  0.00503  0.00102  407 PHE A CE2 
3238 C CZ  . PHE A 407 ? 0.24846 0.23158 0.20315 0.00506  0.00677  0.00154  407 PHE A CZ  
3239 N N   . PHE A 408 ? 0.22559 0.21695 0.18261 0.00393  0.00719  -0.01231 408 PHE A N   
3240 C CA  . PHE A 408 ? 0.22330 0.21567 0.18326 0.00434  0.00730  -0.01533 408 PHE A CA  
3241 C C   . PHE A 408 ? 0.23709 0.23010 0.19202 0.00245  0.00638  -0.01596 408 PHE A C   
3242 O O   . PHE A 408 ? 0.23739 0.22980 0.18852 0.00203  0.00412  -0.01307 408 PHE A O   
3243 C CB  . PHE A 408 ? 0.18818 0.17987 0.15340 0.00682  0.00538  -0.01438 408 PHE A CB  
3244 C CG  . PHE A 408 ? 0.22122 0.21350 0.19014 0.00733  0.00547  -0.01727 408 PHE A CG  
3245 C CD1 . PHE A 408 ? 0.21133 0.20405 0.18525 0.00797  0.00722  -0.01977 408 PHE A CD1 
3246 C CD2 . PHE A 408 ? 0.20171 0.19406 0.16958 0.00718  0.00366  -0.01740 408 PHE A CD2 
3247 C CE1 . PHE A 408 ? 0.16675 0.15960 0.14459 0.00850  0.00718  -0.02227 408 PHE A CE1 
3248 C CE2 . PHE A 408 ? 0.20322 0.19579 0.17462 0.00754  0.00378  -0.02005 408 PHE A CE2 
3249 C CZ  . PHE A 408 ? 0.20477 0.19741 0.18120 0.00824  0.00554  -0.02243 408 PHE A CZ  
3250 N N   . SER A 409 ? 0.21039 0.20466 0.16561 0.00124  0.00809  -0.01982 409 SER A N   
3251 C CA  . SER A 409 ? 0.20429 0.19946 0.15426 -0.00112 0.00761  -0.02099 409 SER A CA  
3252 C C   . SER A 409 ? 0.21607 0.21186 0.16911 -0.00079 0.00744  -0.02410 409 SER A C   
3253 O O   . SER A 409 ? 0.18203 0.17857 0.13093 -0.00263 0.00651  -0.02483 409 SER A O   
3254 C CB  . SER A 409 ? 0.23819 0.23451 0.18312 -0.00430 0.01043  -0.02314 409 SER A CB  
3255 O OG  . SER A 409 ? 0.25298 0.25043 0.20218 -0.00442 0.01358  -0.02774 409 SER A OG  
3256 N N   . GLN A 410 ? 0.24670 0.24214 0.20677 0.00131  0.00818  -0.02584 410 GLN A N   
3257 C CA  . GLN A 410 ? 0.18661 0.18227 0.15012 0.00152  0.00831  -0.02904 410 GLN A CA  
3258 C C   . GLN A 410 ? 0.17552 0.17050 0.13928 0.00259  0.00507  -0.02679 410 GLN A C   
3259 O O   . GLN A 410 ? 0.23198 0.22594 0.20080 0.00478  0.00384  -0.02573 410 GLN A O   
3260 C CB  . GLN A 410 ? 0.17923 0.17452 0.15045 0.00336  0.00993  -0.03124 410 GLN A CB  
3261 C CG  . GLN A 410 ? 0.22488 0.22003 0.20036 0.00354  0.01036  -0.03479 410 GLN A CG  
3262 C CD  . GLN A 410 ? 0.20568 0.20222 0.17751 0.00070  0.01250  -0.03883 410 GLN A CD  
3263 O OE1 . GLN A 410 ? 0.21782 0.21470 0.18522 -0.00084 0.01125  -0.03895 410 GLN A OE1 
3264 N NE2 . GLN A 410 ? 0.18591 0.18347 0.15968 -0.00018 0.01581  -0.04233 410 GLN A NE2 
3265 N N   . TYR A 411 ? 0.19214 0.18787 0.15023 0.00075  0.00360  -0.02605 411 TYR A N   
3266 C CA  . TYR A 411 ? 0.20747 0.20303 0.16572 0.00151  0.00049  -0.02403 411 TYR A CA  
3267 C C   . TYR A 411 ? 0.21551 0.21117 0.17687 0.00146  0.00043  -0.02706 411 TYR A C   
3268 O O   . TYR A 411 ? 0.23066 0.22620 0.19330 0.00222  -0.00193 -0.02571 411 TYR A O   
3269 C CB  . TYR A 411 ? 0.21053 0.20701 0.16200 -0.00041 -0.00151 -0.02177 411 TYR A CB  
3270 C CG  . TYR A 411 ? 0.22798 0.22585 0.17365 -0.00378 -0.00016 -0.02448 411 TYR A CG  
3271 C CD1 . TYR A 411 ? 0.28289 0.28108 0.22433 -0.00568 0.00197  -0.02488 411 TYR A CD1 
3272 C CD2 . TYR A 411 ? 0.26881 0.26777 0.21298 -0.00539 -0.00091 -0.02675 411 TYR A CD2 
3273 C CE1 . TYR A 411 ? 0.25444 0.25405 0.19010 -0.00923 0.00345  -0.02754 411 TYR A CE1 
3274 C CE2 . TYR A 411 ? 0.23274 0.23312 0.17118 -0.00889 0.00047  -0.02948 411 TYR A CE2 
3275 C CZ  . TYR A 411 ? 0.27744 0.27817 0.21150 -0.01088 0.00270  -0.02989 411 TYR A CZ  
3276 O OH  . TYR A 411 ? 0.35670 0.35899 0.28459 -0.01480 0.00433  -0.03278 411 TYR A OH  
3277 N N   . PHE A 412 ? 0.21666 0.21255 0.17962 0.00050  0.00305  -0.03126 412 PHE A N   
3278 C CA  . PHE A 412 ? 0.19859 0.19409 0.16544 0.00061  0.00318  -0.03427 412 PHE A CA  
3279 C C   . PHE A 412 ? 0.20596 0.19970 0.18020 0.00336  0.00272  -0.03358 412 PHE A C   
3280 O O   . PHE A 412 ? 0.21291 0.20585 0.19064 0.00369  0.00216  -0.03511 412 PHE A O   
3281 C CB  . PHE A 412 ? 0.23051 0.22674 0.19721 -0.00138 0.00633  -0.03934 412 PHE A CB  
3282 C CG  . PHE A 412 ? 0.23310 0.23115 0.19209 -0.00481 0.00668  -0.04065 412 PHE A CG  
3283 C CD1 . PHE A 412 ? 0.26344 0.26217 0.21972 -0.00634 0.00495  -0.04133 412 PHE A CD1 
3284 C CD2 . PHE A 412 ? 0.23047 0.22963 0.18466 -0.00680 0.00870  -0.04117 412 PHE A CD2 
3285 C CE1 . PHE A 412 ? 0.24659 0.24715 0.19537 -0.00982 0.00499  -0.04236 412 PHE A CE1 
3286 C CE2 . PHE A 412 ? 0.23325 0.23407 0.17967 -0.01041 0.00888  -0.04216 412 PHE A CE2 
3287 C CZ  . PHE A 412 ? 0.21322 0.21476 0.15683 -0.01193 0.00691  -0.04269 412 PHE A CZ  
3288 N N   . ARG A 413 ? 0.22130 0.21439 0.19780 0.00507  0.00292  -0.03133 413 ARG A N   
3289 C CA  . ARG A 413 ? 0.21584 0.20738 0.19858 0.00736  0.00214  -0.03006 413 ARG A CA  
3290 C C   . ARG A 413 ? 0.21015 0.20135 0.19198 0.00823  -0.00060 -0.02633 413 ARG A C   
3291 O O   . ARG A 413 ? 0.19183 0.18325 0.17164 0.00874  -0.00123 -0.02343 413 ARG A O   
3292 C CB  . ARG A 413 ? 0.22926 0.22061 0.21471 0.00845  0.00365  -0.02961 413 ARG A CB  
3293 C CG  . ARG A 413 ? 0.26854 0.25856 0.26135 0.01010  0.00381  -0.03042 413 ARG A CG  
3294 C CD  . ARG A 413 ? 0.30372 0.29261 0.29860 0.01164  0.00164  -0.02673 413 ARG A CD  
3295 N NE  . ARG A 413 ? 0.31522 0.30265 0.31668 0.01286  0.00120  -0.02714 413 ARG A NE  
3296 C CZ  . ARG A 413 ? 0.33937 0.32538 0.34321 0.01307  -0.00037 -0.02689 413 ARG A CZ  
3297 N NH1 . ARG A 413 ? 0.28118 0.26730 0.28171 0.01223  -0.00153 -0.02650 413 ARG A NH1 
3298 N NH2 . ARG A 413 ? 0.39834 0.38276 0.40817 0.01407  -0.00094 -0.02690 413 ARG A NH2 
3299 N N   . VAL A 414 ? 0.18147 0.17214 0.16507 0.00829  -0.00208 -0.02659 414 VAL A N   
3300 C CA  . VAL A 414 ? 0.18896 0.17969 0.17213 0.00883  -0.00446 -0.02367 414 VAL A CA  
3301 C C   . VAL A 414 ? 0.20233 0.19145 0.19074 0.00998  -0.00515 -0.02311 414 VAL A C   
3302 O O   . VAL A 414 ? 0.22310 0.21123 0.21436 0.00970  -0.00496 -0.02527 414 VAL A O   
3303 C CB  . VAL A 414 ? 0.17724 0.16925 0.15712 0.00737  -0.00583 -0.02428 414 VAL A CB  
3304 C CG1 . VAL A 414 ? 0.18784 0.18023 0.16827 0.00802  -0.00816 -0.02150 414 VAL A CG1 
3305 C CG2 . VAL A 414 ? 0.25420 0.24775 0.22830 0.00581  -0.00542 -0.02455 414 VAL A CG2 
3306 N N   . TYR A 415 ? 0.16296 0.15169 0.15252 0.01106  -0.00596 -0.02024 415 TYR A N   
3307 C CA  . TYR A 415 ? 0.17030 0.15755 0.16403 0.01172  -0.00675 -0.01929 415 TYR A CA  
3308 C C   . TYR A 415 ? 0.19069 0.17798 0.18469 0.01103  -0.00825 -0.01930 415 TYR A C   
3309 O O   . TYR A 415 ? 0.16585 0.15468 0.15709 0.01050  -0.00915 -0.01876 415 TYR A O   
3310 C CB  . TYR A 415 ? 0.20441 0.19155 0.19857 0.01256  -0.00708 -0.01643 415 TYR A CB  
3311 C CG  . TYR A 415 ? 0.22216 0.20931 0.21641 0.01317  -0.00568 -0.01626 415 TYR A CG  
3312 C CD1 . TYR A 415 ? 0.19759 0.18376 0.19553 0.01363  -0.00487 -0.01743 415 TYR A CD1 
3313 C CD2 . TYR A 415 ? 0.15920 0.14731 0.15032 0.01328  -0.00524 -0.01489 415 TYR A CD2 
3314 C CE1 . TYR A 415 ? 0.20863 0.19515 0.20710 0.01412  -0.00358 -0.01741 415 TYR A CE1 
3315 C CE2 . TYR A 415 ? 0.16041 0.14858 0.15161 0.01363  -0.00386 -0.01480 415 TYR A CE2 
3316 C CZ  . TYR A 415 ? 0.18477 0.17233 0.17965 0.01402  -0.00299 -0.01615 415 TYR A CZ  
3317 O OH  . TYR A 415 ? 0.16610 0.15406 0.16150 0.01431  -0.00160 -0.01620 415 TYR A OH  
3318 N N   . SER A 416 ? 0.18667 0.17227 0.18429 0.01096  -0.00865 -0.01981 416 SER A N   
3319 C CA  . SER A 416 ? 0.16942 0.15486 0.16766 0.01010  -0.00993 -0.01987 416 SER A CA  
3320 C C   . SER A 416 ? 0.15860 0.14388 0.15777 0.01019  -0.01093 -0.01715 416 SER A C   
3321 O O   . SER A 416 ? 0.12257 0.10631 0.12402 0.01056  -0.01093 -0.01592 416 SER A O   
3322 C CB  . SER A 416 ? 0.14955 0.13293 0.15112 0.00966  -0.00978 -0.02196 416 SER A CB  
3323 O OG  . SER A 416 ? 0.13166 0.11445 0.13430 0.00874  -0.01103 -0.02154 416 SER A OG  
3324 N N   . PRO A 417 ? 0.17106 0.15803 0.16872 0.00973  -0.01180 -0.01624 417 PRO A N   
3325 C CA  . PRO A 417 ? 0.12675 0.11377 0.12553 0.00947  -0.01238 -0.01420 417 PRO A CA  
3326 C C   . PRO A 417 ? 0.16472 0.14995 0.16596 0.00840  -0.01296 -0.01420 417 PRO A C   
3327 O O   . PRO A 417 ? 0.14481 0.12998 0.14668 0.00771  -0.01329 -0.01262 417 PRO A O   
3328 C CB  . PRO A 417 ? 0.10145 0.09102 0.09880 0.00924  -0.01308 -0.01390 417 PRO A CB  
3329 C CG  . PRO A 417 ? 0.16200 0.15239 0.15795 0.00880  -0.01346 -0.01588 417 PRO A CG  
3330 C CD  . PRO A 417 ? 0.12352 0.11265 0.11864 0.00927  -0.01235 -0.01711 417 PRO A CD  
3331 N N   . VAL A 418 ? 0.13658 0.12024 0.13920 0.00804  -0.01301 -0.01598 418 VAL A N   
3332 C CA  . VAL A 418 ? 0.21979 0.20123 0.22489 0.00695  -0.01370 -0.01588 418 VAL A CA  
3333 C C   . VAL A 418 ? 0.15047 0.12907 0.15834 0.00753  -0.01364 -0.01551 418 VAL A C   
3334 O O   . VAL A 418 ? 0.21094 0.18767 0.22047 0.00681  -0.01447 -0.01371 418 VAL A O   
3335 C CB  . VAL A 418 ? 0.18087 0.16239 0.18623 0.00595  -0.01399 -0.01823 418 VAL A CB  
3336 C CG1 . VAL A 418 ? 0.20671 0.18532 0.21491 0.00481  -0.01463 -0.01820 418 VAL A CG1 
3337 C CG2 . VAL A 418 ? 0.20051 0.18504 0.20392 0.00525  -0.01451 -0.01823 418 VAL A CG2 
3338 N N   . VAL A 419 ? 0.17761 0.15602 0.18611 0.00868  -0.01271 -0.01711 419 VAL A N   
3339 C CA  . VAL A 419 ? 0.16733 0.14324 0.17967 0.00939  -0.01264 -0.01742 419 VAL A CA  
3340 C C   . VAL A 419 ? 0.15027 0.12640 0.16302 0.01044  -0.01248 -0.01551 419 VAL A C   
3341 O O   . VAL A 419 ? 0.17818 0.15230 0.19421 0.01067  -0.01329 -0.01419 419 VAL A O   
3342 C CB  . VAL A 419 ? 0.12136 0.09709 0.13496 0.00981  -0.01140 -0.02096 419 VAL A CB  
3343 C CG1 . VAL A 419 ? 0.17867 0.15251 0.19691 0.01098  -0.01095 -0.02158 419 VAL A CG1 
3344 C CG2 . VAL A 419 ? 0.19334 0.16810 0.20760 0.00855  -0.01174 -0.02289 419 VAL A CG2 
3345 N N   . PHE A 420 ? 0.15591 0.13441 0.16548 0.01098  -0.01159 -0.01522 420 PHE A N   
3346 C CA  . PHE A 420 ? 0.15969 0.13858 0.16960 0.01193  -0.01113 -0.01394 420 PHE A CA  
3347 C C   . PHE A 420 ? 0.13502 0.11278 0.14614 0.01142  -0.01242 -0.01102 420 PHE A C   
3348 O O   . PHE A 420 ? 0.12776 0.10457 0.14155 0.01199  -0.01277 -0.01013 420 PHE A O   
3349 C CB  . PHE A 420 ? 0.16257 0.14391 0.16851 0.01226  -0.01015 -0.01375 420 PHE A CB  
3350 C CG  . PHE A 420 ? 0.16317 0.14503 0.16926 0.01314  -0.00933 -0.01298 420 PHE A CG  
3351 C CD1 . PHE A 420 ? 0.21133 0.19297 0.21961 0.01392  -0.00828 -0.01471 420 PHE A CD1 
3352 C CD2 . PHE A 420 ? 0.17494 0.15765 0.17924 0.01305  -0.00942 -0.01080 420 PHE A CD2 
3353 C CE1 . PHE A 420 ? 0.20937 0.19174 0.21801 0.01460  -0.00747 -0.01410 420 PHE A CE1 
3354 C CE2 . PHE A 420 ? 0.15119 0.13440 0.15561 0.01369  -0.00864 -0.01018 420 PHE A CE2 
3355 C CZ  . PHE A 420 ? 0.21096 0.19406 0.21752 0.01446  -0.00773 -0.01174 420 PHE A CZ  
3356 N N   . GLY A 421 ? 0.15963 0.13764 0.16885 0.01013  -0.01316 -0.00957 421 GLY A N   
3357 C CA  . GLY A 421 ? 0.15405 0.13120 0.16352 0.00907  -0.01423 -0.00689 421 GLY A CA  
3358 C C   . GLY A 421 ? 0.17088 0.14516 0.18358 0.00833  -0.01582 -0.00595 421 GLY A C   
3359 O O   . GLY A 421 ? 0.19054 0.16373 0.20430 0.00779  -0.01697 -0.00366 421 GLY A O   
3360 N N   . LYS A 422 ? 0.14575 0.11867 0.16007 0.00817  -0.01604 -0.00759 422 LYS A N   
3361 C CA  . LYS A 422 ? 0.21050 0.18024 0.22814 0.00737  -0.01765 -0.00660 422 LYS A CA  
3362 C C   . LYS A 422 ? 0.16621 0.13426 0.18836 0.00873  -0.01836 -0.00620 422 LYS A C   
3363 O O   . LYS A 422 ? 0.25006 0.21538 0.27518 0.00808  -0.02024 -0.00426 422 LYS A O   
3364 C CB  . LYS A 422 ? 0.20185 0.17051 0.22054 0.00698  -0.01746 -0.00892 422 LYS A CB  
3365 C CG  . LYS A 422 ? 0.24574 0.21129 0.26620 0.00524  -0.01915 -0.00739 422 LYS A CG  
3366 C CD  . LYS A 422 ? 0.27709 0.24142 0.29905 0.00489  -0.01882 -0.01004 422 LYS A CD  
3367 C CE  . LYS A 422 ? 0.28722 0.25464 0.30541 0.00438  -0.01757 -0.01196 422 LYS A CE  
3368 N NZ  . LYS A 422 ? 0.27581 0.24213 0.29521 0.00354  -0.01746 -0.01438 422 LYS A NZ  
3369 N N   . LYS A 423 ? 0.18937 0.15902 0.21229 0.01050  -0.01697 -0.00789 423 LYS A N   
3370 C CA  . LYS A 423 ? 0.19169 0.16023 0.21970 0.01190  -0.01743 -0.00793 423 LYS A CA  
3371 C C   . LYS A 423 ? 0.17094 0.13932 0.19927 0.01144  -0.01912 -0.00440 423 LYS A C   
3372 O O   . LYS A 423 ? 0.17403 0.14048 0.20718 0.01185  -0.02086 -0.00304 423 LYS A O   
3373 C CB  . LYS A 423 ? 0.12996 0.10065 0.15830 0.01352  -0.01517 -0.01091 423 LYS A CB  
3374 C CG  . LYS A 423 ? 0.17534 0.14476 0.21013 0.01496  -0.01486 -0.01304 423 LYS A CG  
3375 C CD  . LYS A 423 ? 0.18314 0.15447 0.21733 0.01575  -0.01212 -0.01707 423 LYS A CD  
3376 C CE  . LYS A 423 ? 0.17579 0.15008 0.20619 0.01609  -0.01070 -0.01687 423 LYS A CE  
3377 N NZ  . LYS A 423 ? 0.18102 0.15668 0.21363 0.01706  -0.00840 -0.02025 423 LYS A NZ  
3378 N N   . TYR A 424 ? 0.12436 0.09475 0.14786 0.01048  -0.01873 -0.00291 424 TYR A N   
3379 C CA  . TYR A 424 ? 0.14708 0.11763 0.16991 0.00952  -0.02017 0.00027  424 TYR A CA  
3380 C C   . TYR A 424 ? 0.15110 0.12002 0.17193 0.00699  -0.02199 0.00301  424 TYR A C   
3381 O O   . TYR A 424 ? 0.21471 0.18191 0.23742 0.00605  -0.02430 0.00577  424 TYR A O   
3382 C CB  . TYR A 424 ? 0.15037 0.12386 0.16915 0.00957  -0.01854 0.00018  424 TYR A CB  
3383 C CG  . TYR A 424 ? 0.09978 0.07501 0.11935 0.01159  -0.01654 -0.00236 424 TYR A CG  
3384 C CD1 . TYR A 424 ? 0.11248 0.08828 0.13523 0.01272  -0.01660 -0.00225 424 TYR A CD1 
3385 C CD2 . TYR A 424 ? 0.13337 0.10983 0.15039 0.01211  -0.01466 -0.00477 424 TYR A CD2 
3386 C CE1 . TYR A 424 ? 0.10769 0.08516 0.13088 0.01420  -0.01453 -0.00468 424 TYR A CE1 
3387 C CE2 . TYR A 424 ? 0.13675 0.11473 0.15379 0.01349  -0.01283 -0.00691 424 TYR A CE2 
3388 C CZ  . TYR A 424 ? 0.10348 0.08193 0.12351 0.01446  -0.01262 -0.00694 424 TYR A CZ  
3389 O OH  . TYR A 424 ? 0.13376 0.11380 0.15358 0.01550  -0.01058 -0.00917 424 TYR A OH  
3390 N N   . ASP A 425 ? 0.14714 0.11671 0.16420 0.00571  -0.02104 0.00233  425 ASP A N   
3391 C CA  . ASP A 425 ? 0.17532 0.14411 0.18954 0.00288  -0.02210 0.00453  425 ASP A CA  
3392 C C   . ASP A 425 ? 0.15790 0.12494 0.17285 0.00219  -0.02229 0.00346  425 ASP A C   
3393 O O   . ASP A 425 ? 0.15224 0.12087 0.16466 0.00170  -0.02085 0.00180  425 ASP A O   
3394 C CB  . ASP A 425 ? 0.15450 0.12615 0.16396 0.00173  -0.02050 0.00447  425 ASP A CB  
3395 C CG  . ASP A 425 ? 0.16932 0.14058 0.17576 -0.00158 -0.02133 0.00674  425 ASP A CG  
3396 O OD1 . ASP A 425 ? 0.20037 0.16899 0.20786 -0.00316 -0.02330 0.00863  425 ASP A OD1 
3397 O OD2 . ASP A 425 ? 0.21263 0.18618 0.21572 -0.00276 -0.01993 0.00658  425 ASP A OD2 
3398 N N   . PRO A 426 ? 0.14921 0.11297 0.16795 0.00209  -0.02413 0.00437  426 PRO A N   
3399 C CA  . PRO A 426 ? 0.16972 0.13157 0.18933 0.00128  -0.02426 0.00322  426 PRO A CA  
3400 C C   . PRO A 426 ? 0.18650 0.14821 0.20230 -0.00191 -0.02461 0.00481  426 PRO A C   
3401 O O   . PRO A 426 ? 0.18049 0.14195 0.19587 -0.00268 -0.02397 0.00321  426 PRO A O   
3402 C CB  . PRO A 426 ? 0.18624 0.14427 0.21147 0.00198  -0.02632 0.00420  426 PRO A CB  
3403 C CG  . PRO A 426 ? 0.21848 0.17622 0.24444 0.00179  -0.02815 0.00742  426 PRO A CG  
3404 C CD  . PRO A 426 ? 0.16377 0.12538 0.18671 0.00276  -0.02630 0.00648  426 PRO A CD  
3405 N N   . GLU A 427 ? 0.21010 0.17215 0.22306 -0.00402 -0.02548 0.00770  427 GLU A N   
3406 C CA  . GLU A 427 ? 0.20391 0.16612 0.21302 -0.00748 -0.02546 0.00898  427 GLU A CA  
3407 C C   . GLU A 427 ? 0.19708 0.16329 0.20251 -0.00793 -0.02298 0.00715  427 GLU A C   
3408 O O   . GLU A 427 ? 0.20627 0.17323 0.20904 -0.01066 -0.02239 0.00733  427 GLU A O   
3409 C CB  . GLU A 427 ? 0.23767 0.19824 0.24511 -0.01018 -0.02762 0.01297  427 GLU A CB  
3410 C CG  . GLU A 427 ? 0.25677 0.21294 0.26799 -0.01035 -0.03057 0.01539  427 GLU A CG  
3411 C CD  . GLU A 427 ? 0.27540 0.22907 0.28789 -0.01132 -0.03071 0.01453  427 GLU A CD  
3412 O OE1 . GLU A 427 ? 0.34235 0.29577 0.35128 -0.01473 -0.03065 0.01562  427 GLU A OE1 
3413 O OE2 . GLU A 427 ? 0.36150 0.31357 0.37855 -0.00884 -0.03070 0.01254  427 GLU A OE2 
3414 N N   . GLY A 428 ? 0.19299 0.16173 0.19853 -0.00542 -0.02151 0.00540  428 GLY A N   
3415 C CA  . GLY A 428 ? 0.16674 0.13903 0.16960 -0.00555 -0.01935 0.00380  428 GLY A CA  
3416 C C   . GLY A 428 ? 0.18995 0.16365 0.18955 -0.00796 -0.01890 0.00539  428 GLY A C   
3417 O O   . GLY A 428 ? 0.20884 0.18496 0.20653 -0.00923 -0.01723 0.00422  428 GLY A O   
3418 N N   . ARG A 429 ? 0.21715 0.18957 0.21633 -0.00874 -0.02034 0.00789  429 ARG A N   
3419 C CA  . ARG A 429 ? 0.19691 0.17075 0.19255 -0.01144 -0.01987 0.00927  429 ARG A CA  
3420 C C   . ARG A 429 ? 0.18147 0.15861 0.17606 -0.01015 -0.01741 0.00720  429 ARG A C   
3421 O O   . ARG A 429 ? 0.21794 0.19703 0.20991 -0.01240 -0.01590 0.00679  429 ARG A O   
3422 C CB  . ARG A 429 ? 0.23419 0.20627 0.22984 -0.01224 -0.02217 0.01235  429 ARG A CB  
3423 C CG  . ARG A 429 ? 0.25670 0.22503 0.25484 -0.01260 -0.02504 0.01457  429 ARG A CG  
3424 C CD  . ARG A 429 ? 0.26066 0.22740 0.25727 -0.01536 -0.02765 0.01844  429 ARG A CD  
3425 N NE  . ARG A 429 ? 0.27068 0.23636 0.26360 -0.01972 -0.02823 0.02021  429 ARG A NE  
3426 C CZ  . ARG A 429 ? 0.27600 0.23904 0.26783 -0.02258 -0.03118 0.02402  429 ARG A CZ  
3427 N NH1 . ARG A 429 ? 0.26386 0.22507 0.25861 -0.02136 -0.03409 0.02657  429 ARG A NH1 
3428 N NH2 . ARG A 429 ? 0.27876 0.24101 0.26663 -0.02688 -0.03131 0.02537  429 ARG A NH2 
3429 N N   . PHE A 430 ? 0.17719 0.15495 0.17395 -0.00667 -0.01688 0.00575  430 PHE A N   
3430 C CA  . PHE A 430 ? 0.14984 0.13032 0.14589 -0.00528 -0.01472 0.00393  430 PHE A CA  
3431 C C   . PHE A 430 ? 0.13804 0.12038 0.13388 -0.00559 -0.01316 0.00188  430 PHE A C   
3432 O O   . PHE A 430 ? 0.16636 0.15096 0.16123 -0.00608 -0.01140 0.00086  430 PHE A O   
3433 C CB  . PHE A 430 ? 0.14273 0.12322 0.14086 -0.00182 -0.01462 0.00298  430 PHE A CB  
3434 C CG  . PHE A 430 ? 0.14066 0.12347 0.13808 -0.00035 -0.01267 0.00148  430 PHE A CG  
3435 C CD1 . PHE A 430 ? 0.13852 0.12215 0.13478 -0.00062 -0.01201 0.00213  430 PHE A CD1 
3436 C CD2 . PHE A 430 ? 0.11958 0.10365 0.11759 0.00121  -0.01169 -0.00045 430 PHE A CD2 
3437 C CE1 . PHE A 430 ? 0.14392 0.12927 0.13980 0.00071  -0.01026 0.00086  430 PHE A CE1 
3438 C CE2 . PHE A 430 ? 0.14677 0.13262 0.14438 0.00255  -0.01022 -0.00143 430 PHE A CE2 
3439 C CZ  . PHE A 430 ? 0.11625 0.10258 0.11288 0.00235  -0.00944 -0.00079 430 PHE A CZ  
3440 N N   . ILE A 431 ? 0.16242 0.14388 0.15964 -0.00532 -0.01380 0.00116  431 ILE A N   
3441 C CA  . ILE A 431 ? 0.17080 0.15426 0.16839 -0.00560 -0.01261 -0.00078 431 ILE A CA  
3442 C C   . ILE A 431 ? 0.15852 0.14292 0.15445 -0.00915 -0.01182 -0.00049 431 ILE A C   
3443 O O   . ILE A 431 ? 0.15908 0.14617 0.15511 -0.00964 -0.01006 -0.00205 431 ILE A O   
3444 C CB  . ILE A 431 ? 0.14248 0.12480 0.14192 -0.00458 -0.01357 -0.00174 431 ILE A CB  
3445 C CG1 . ILE A 431 ? 0.14914 0.13112 0.14992 -0.00135 -0.01382 -0.00263 431 ILE A CG1 
3446 C CG2 . ILE A 431 ? 0.20218 0.18674 0.20218 -0.00530 -0.01266 -0.00355 431 ILE A CG2 
3447 C CD1 . ILE A 431 ? 0.18594 0.16690 0.18836 -0.00055 -0.01454 -0.00399 431 ILE A CD1 
3448 N N   . ARG A 432 ? 0.13370 0.11588 0.12824 -0.01181 -0.01310 0.00149  432 ARG A N   
3449 C CA  . ARG A 432 ? 0.20201 0.18502 0.19437 -0.01578 -0.01224 0.00177  432 ARG A CA  
3450 C C   . ARG A 432 ? 0.17825 0.16340 0.16857 -0.01720 -0.01051 0.00153  432 ARG A C   
3451 O O   . ARG A 432 ? 0.17056 0.15785 0.15994 -0.01976 -0.00865 0.00025  432 ARG A O   
3452 C CB  . ARG A 432 ? 0.23260 0.21240 0.22344 -0.01855 -0.01431 0.00447  432 ARG A CB  
3453 C CG  . ARG A 432 ? 0.22141 0.19860 0.21470 -0.01719 -0.01601 0.00464  432 ARG A CG  
3454 C CD  . ARG A 432 ? 0.25071 0.22413 0.24315 -0.01946 -0.01845 0.00779  432 ARG A CD  
3455 N NE  . ARG A 432 ? 0.21810 0.18861 0.21376 -0.01752 -0.02011 0.00785  432 ARG A NE  
3456 C CZ  . ARG A 432 ? 0.19408 0.16357 0.19074 -0.01847 -0.02020 0.00699  432 ARG A CZ  
3457 N NH1 . ARG A 432 ? 0.21989 0.19118 0.21472 -0.02130 -0.01878 0.00606  432 ARG A NH1 
3458 N NH2 . ARG A 432 ? 0.26858 0.23526 0.26842 -0.01666 -0.02159 0.00683  432 ARG A NH2 
3459 N N   . LYS A 433 ? 0.15959 0.14432 0.14946 -0.01571 -0.01091 0.00248  433 LYS A N   
3460 C CA  . LYS A 433 ? 0.19456 0.18120 0.18257 -0.01705 -0.00919 0.00205  433 LYS A CA  
3461 C C   . LYS A 433 ? 0.18256 0.17218 0.17254 -0.01547 -0.00668 -0.00087 433 LYS A C   
3462 O O   . LYS A 433 ? 0.14538 0.13711 0.13463 -0.01781 -0.00456 -0.00229 433 LYS A O   
3463 C CB  . LYS A 433 ? 0.19656 0.18212 0.18413 -0.01557 -0.01031 0.00363  433 LYS A CB  
3464 C CG  . LYS A 433 ? 0.24044 0.22807 0.22728 -0.01538 -0.00829 0.00245  433 LYS A CG  
3465 C CD  . LYS A 433 ? 0.29004 0.27872 0.27345 -0.01979 -0.00716 0.00268  433 LYS A CD  
3466 C CE  . LYS A 433 ? 0.26169 0.25209 0.24465 -0.01954 -0.00520 0.00141  433 LYS A CE  
3467 N NZ  . LYS A 433 ? 0.26997 0.26158 0.24932 -0.02419 -0.00384 0.00123  433 LYS A NZ  
3468 N N   . PHE A 434 ? 0.17941 0.16923 0.17207 -0.01164 -0.00691 -0.00183 434 PHE A N   
3469 C CA  . PHE A 434 ? 0.13406 0.12638 0.12891 -0.00981 -0.00506 -0.00407 434 PHE A CA  
3470 C C   . PHE A 434 ? 0.15515 0.14916 0.15239 -0.00974 -0.00459 -0.00582 434 PHE A C   
3471 O O   . PHE A 434 ? 0.20037 0.19691 0.19972 -0.00951 -0.00284 -0.00772 434 PHE A O   
3472 C CB  . PHE A 434 ? 0.14503 0.13682 0.14105 -0.00604 -0.00561 -0.00394 434 PHE A CB  
3473 C CG  . PHE A 434 ? 0.16127 0.15230 0.15566 -0.00598 -0.00546 -0.00284 434 PHE A CG  
3474 C CD1 . PHE A 434 ? 0.17557 0.16810 0.16976 -0.00662 -0.00349 -0.00380 434 PHE A CD1 
3475 C CD2 . PHE A 434 ? 0.15614 0.14506 0.14969 -0.00532 -0.00722 -0.00103 434 PHE A CD2 
3476 C CE1 . PHE A 434 ? 0.13313 0.12507 0.12579 -0.00676 -0.00333 -0.00291 434 PHE A CE1 
3477 C CE2 . PHE A 434 ? 0.16543 0.15399 0.15782 -0.00534 -0.00717 -0.00007 434 PHE A CE2 
3478 C CZ  . PHE A 434 ? 0.17054 0.16062 0.16223 -0.00615 -0.00524 -0.00097 434 PHE A CZ  
3479 N N   . LEU A 435 ? 0.16187 0.15460 0.15931 -0.00993 -0.00612 -0.00531 435 LEU A N   
3480 C CA  . LEU A 435 ? 0.12725 0.12173 0.12683 -0.01044 -0.00574 -0.00696 435 LEU A CA  
3481 C C   . LEU A 435 ? 0.14369 0.13747 0.14152 -0.01441 -0.00571 -0.00639 435 LEU A C   
3482 O O   . LEU A 435 ? 0.15151 0.14310 0.14885 -0.01492 -0.00736 -0.00533 435 LEU A O   
3483 C CB  . LEU A 435 ? 0.15145 0.14526 0.15270 -0.00773 -0.00736 -0.00722 435 LEU A CB  
3484 C CG  . LEU A 435 ? 0.13146 0.12581 0.13385 -0.00412 -0.00761 -0.00759 435 LEU A CG  
3485 C CD1 . LEU A 435 ? 0.15379 0.14796 0.15738 -0.00236 -0.00902 -0.00821 435 LEU A CD1 
3486 C CD2 . LEU A 435 ? 0.09328 0.09049 0.09767 -0.00341 -0.00600 -0.00893 435 LEU A CD2 
3487 N N   . PRO A 436 ? 0.11439 0.10988 0.11117 -0.01750 -0.00376 -0.00713 436 PRO A N   
3488 C CA  . PRO A 436 ? 0.17635 0.17095 0.17047 -0.02190 -0.00372 -0.00624 436 PRO A CA  
3489 C C   . PRO A 436 ? 0.12954 0.12492 0.12542 -0.02303 -0.00376 -0.00738 436 PRO A C   
3490 O O   . PRO A 436 ? 0.15204 0.14588 0.14560 -0.02648 -0.00425 -0.00619 436 PRO A O   
3491 C CB  . PRO A 436 ? 0.20322 0.20015 0.19595 -0.02489 -0.00107 -0.00747 436 PRO A CB  
3492 C CG  . PRO A 436 ? 0.17416 0.17218 0.16848 -0.02181 -0.00021 -0.00833 436 PRO A CG  
3493 C CD  . PRO A 436 ? 0.16220 0.16033 0.16007 -0.01738 -0.00141 -0.00886 436 PRO A CD  
3494 N N   . VAL A 437 ? 0.16412 0.16181 0.16395 -0.02042 -0.00342 -0.00948 437 VAL A N   
3495 C CA  . VAL A 437 ? 0.18730 0.18598 0.18909 -0.02144 -0.00360 -0.01067 437 VAL A CA  
3496 C C   . VAL A 437 ? 0.17804 0.17309 0.17868 -0.02108 -0.00608 -0.00889 437 VAL A C   
3497 O O   . VAL A 437 ? 0.17233 0.16709 0.17335 -0.02310 -0.00638 -0.00924 437 VAL A O   
3498 C CB  . VAL A 437 ? 0.19623 0.19845 0.20277 -0.01857 -0.00305 -0.01314 437 VAL A CB  
3499 C CG1 . VAL A 437 ? 0.17816 0.17914 0.18547 -0.01430 -0.00496 -0.01244 437 VAL A CG1 
3500 C CG2 . VAL A 437 ? 0.21493 0.21915 0.22392 -0.02019 -0.00284 -0.01480 437 VAL A CG2 
3501 N N   . LEU A 438 ? 0.15510 0.14734 0.15465 -0.01868 -0.00775 -0.00714 438 LEU A N   
3502 C CA  . LEU A 438 ? 0.20226 0.19085 0.20141 -0.01811 -0.00996 -0.00565 438 LEU A CA  
3503 C C   . LEU A 438 ? 0.18838 0.17340 0.18452 -0.02043 -0.01115 -0.00273 438 LEU A C   
3504 O O   . LEU A 438 ? 0.22262 0.20434 0.21901 -0.01912 -0.01311 -0.00120 438 LEU A O   
3505 C CB  . LEU A 438 ? 0.21587 0.20386 0.21651 -0.01389 -0.01100 -0.00595 438 LEU A CB  
3506 C CG  . LEU A 438 ? 0.13434 0.12467 0.13767 -0.01160 -0.01098 -0.00820 438 LEU A CG  
3507 C CD1 . LEU A 438 ? 0.19077 0.18134 0.19448 -0.00800 -0.01131 -0.00834 438 LEU A CD1 
3508 C CD2 . LEU A 438 ? 0.21504 0.20357 0.21920 -0.01214 -0.01225 -0.00859 438 LEU A CD2 
3509 N N   . LYS A 439 ? 0.24469 0.23038 0.23818 -0.02398 -0.01007 -0.00197 439 LYS A N   
3510 C CA  . LYS A 439 ? 0.23557 0.21815 0.22584 -0.02623 -0.01152 0.00118  439 LYS A CA  
3511 C C   . LYS A 439 ? 0.25965 0.23865 0.24918 -0.02862 -0.01342 0.00315  439 LYS A C   
3512 O O   . LYS A 439 ? 0.23784 0.21337 0.22605 -0.02926 -0.01562 0.00616  439 LYS A O   
3513 C CB  . LYS A 439 ? 0.26055 0.24511 0.24760 -0.02974 -0.00970 0.00128  439 LYS A CB  
3514 C CG  . LYS A 439 ? 0.30902 0.29331 0.29326 -0.03500 -0.00916 0.00192  439 LYS A CG  
3515 C CD  . LYS A 439 ? 0.28952 0.27816 0.27493 -0.03664 -0.00597 -0.00148 439 LYS A CD  
3516 C CE  . LYS A 439 ? 0.32130 0.31102 0.30249 -0.04221 -0.00422 -0.00122 439 LYS A CE  
3517 N NZ  . LYS A 439 ? 0.32440 0.31426 0.30272 -0.04272 -0.00394 -0.00019 439 LYS A NZ  
3518 N N   . ASP A 440 ? 0.22687 0.20658 0.21759 -0.02995 -0.01276 0.00162  440 ASP A N   
3519 C CA  . ASP A 440 ? 0.25540 0.23159 0.24544 -0.03260 -0.01438 0.00340  440 ASP A CA  
3520 C C   . ASP A 440 ? 0.21662 0.19106 0.21025 -0.02978 -0.01560 0.00235  440 ASP A C   
3521 O O   . ASP A 440 ? 0.29109 0.26301 0.28498 -0.03182 -0.01652 0.00301  440 ASP A O   
3522 C CB  . ASP A 440 ? 0.27733 0.25530 0.26543 -0.03733 -0.01261 0.00261  440 ASP A CB  
3523 C CG  . ASP A 440 ? 0.33960 0.31873 0.32342 -0.04110 -0.01143 0.00378  440 ASP A CG  
3524 O OD1 . ASP A 440 ? 0.40037 0.37718 0.38183 -0.04130 -0.01309 0.00663  440 ASP A OD1 
3525 O OD2 . ASP A 440 ? 0.37676 0.35931 0.35974 -0.04402 -0.00881 0.00170  440 ASP A OD2 
3526 N N   . MET A 441 ? 0.21254 0.18823 0.20876 -0.02542 -0.01553 0.00066  441 MET A N   
3527 C CA  . MET A 441 ? 0.22443 0.19869 0.22372 -0.02285 -0.01651 -0.00066 441 MET A CA  
3528 C C   . MET A 441 ? 0.18133 0.15099 0.18150 -0.02149 -0.01876 0.00155  441 MET A C   
3529 O O   . MET A 441 ? 0.18240 0.15176 0.18220 -0.01976 -0.01924 0.00277  441 MET A O   
3530 C CB  . MET A 441 ? 0.24609 0.22382 0.24730 -0.01919 -0.01547 -0.00337 441 MET A CB  
3531 C CG  . MET A 441 ? 0.27111 0.24762 0.27487 -0.01643 -0.01640 -0.00488 441 MET A CG  
3532 S SD  . MET A 441 ? 0.35432 0.33186 0.35979 -0.01795 -0.01616 -0.00727 441 MET A SD  
3533 C CE  . MET A 441 ? 0.21915 0.20198 0.22410 -0.01979 -0.01413 -0.00855 441 MET A CE  
3534 N N   . PRO A 442 ? 0.22681 0.19287 0.22861 -0.02221 -0.02016 0.00204  442 PRO A N   
3535 C CA  . PRO A 442 ? 0.22349 0.18510 0.22729 -0.02074 -0.02233 0.00398  442 PRO A CA  
3536 C C   . PRO A 442 ? 0.22598 0.18849 0.23207 -0.01639 -0.02215 0.00241  442 PRO A C   
3537 O O   . PRO A 442 ? 0.20970 0.17535 0.21633 -0.01442 -0.02070 -0.00049 442 PRO A O   
3538 C CB  . PRO A 442 ? 0.21831 0.17663 0.22429 -0.02188 -0.02322 0.00352  442 PRO A CB  
3539 C CG  . PRO A 442 ? 0.22927 0.18941 0.23283 -0.02562 -0.02204 0.00309  442 PRO A CG  
3540 C CD  . PRO A 442 ? 0.25841 0.22416 0.26051 -0.02482 -0.01982 0.00099  442 PRO A CD  
3541 N N   . ALA A 443 ? 0.27603 0.23578 0.28360 -0.01506 -0.02376 0.00444  443 ALA A N   
3542 C CA  . ALA A 443 ? 0.19961 0.16039 0.20917 -0.01129 -0.02342 0.00311  443 ALA A CA  
3543 C C   . ALA A 443 ? 0.20911 0.16962 0.22173 -0.00898 -0.02283 -0.00012 443 ALA A C   
3544 O O   . ALA A 443 ? 0.20991 0.17248 0.22317 -0.00627 -0.02182 -0.00209 443 ALA A O   
3545 C CB  . ALA A 443 ? 0.25193 0.20984 0.26321 -0.01058 -0.02540 0.00593  443 ALA A CB  
3546 N N   . LYS A 444 ? 0.20621 0.16422 0.22050 -0.01028 -0.02339 -0.00077 444 LYS A N   
3547 C CA  . LYS A 444 ? 0.23558 0.19342 0.25249 -0.00858 -0.02270 -0.00417 444 LYS A CA  
3548 C C   . LYS A 444 ? 0.19676 0.15929 0.21161 -0.00784 -0.02090 -0.00704 444 LYS A C   
3549 O O   . LYS A 444 ? 0.19883 0.16224 0.21495 -0.00596 -0.02019 -0.00985 444 LYS A O   
3550 C CB  . LYS A 444 ? 0.23040 0.18468 0.24920 -0.01064 -0.02357 -0.00427 444 LYS A CB  
3551 C CG  . LYS A 444 ? 0.28270 0.23560 0.30500 -0.00912 -0.02313 -0.00764 444 LYS A CG  
3552 C CD  . LYS A 444 ? 0.26842 0.21882 0.29164 -0.01169 -0.02355 -0.00815 444 LYS A CD  
3553 C CE  . LYS A 444 ? 0.29151 0.23793 0.31956 -0.01072 -0.02391 -0.01010 444 LYS A CE  
3554 N NZ  . LYS A 444 ? 0.28868 0.23758 0.31749 -0.00880 -0.02224 -0.01455 444 LYS A NZ  
3555 N N   . TYR A 445 ? 0.20957 0.17520 0.22144 -0.00940 -0.02018 -0.00643 445 TYR A N   
3556 C CA  . TYR A 445 ? 0.16617 0.13628 0.17678 -0.00870 -0.01882 -0.00882 445 TYR A CA  
3557 C C   . TYR A 445 ? 0.22374 0.19716 0.23217 -0.00805 -0.01793 -0.00798 445 TYR A C   
3558 O O   . TYR A 445 ? 0.21566 0.19280 0.22336 -0.00786 -0.01699 -0.00943 445 TYR A O   
3559 C CB  . TYR A 445 ? 0.23809 0.20938 0.24848 -0.01124 -0.01854 -0.00987 445 TYR A CB  
3560 C CG  . TYR A 445 ? 0.26083 0.22837 0.27317 -0.01270 -0.01941 -0.01028 445 TYR A CG  
3561 C CD1 . TYR A 445 ? 0.20855 0.17502 0.22298 -0.01125 -0.01948 -0.01278 445 TYR A CD1 
3562 C CD2 . TYR A 445 ? 0.25802 0.22301 0.26997 -0.01581 -0.02007 -0.00825 445 TYR A CD2 
3563 C CE1 . TYR A 445 ? 0.26057 0.22339 0.27718 -0.01262 -0.02014 -0.01340 445 TYR A CE1 
3564 C CE2 . TYR A 445 ? 0.24464 0.20583 0.25857 -0.01722 -0.02092 -0.00848 445 TYR A CE2 
3565 C CZ  . TYR A 445 ? 0.27884 0.23891 0.29535 -0.01551 -0.02092 -0.01114 445 TYR A CZ  
3566 O OH  . TYR A 445 ? 0.43719 0.39324 0.45606 -0.01694 -0.02163 -0.01160 445 TYR A OH  
3567 N N   . ILE A 446 ? 0.18733 0.15954 0.19504 -0.00772 -0.01829 -0.00571 446 ILE A N   
3568 C CA  . ILE A 446 ? 0.19886 0.17403 0.20453 -0.00743 -0.01728 -0.00506 446 ILE A CA  
3569 C C   . ILE A 446 ? 0.21093 0.18861 0.21675 -0.00447 -0.01646 -0.00682 446 ILE A C   
3570 O O   . ILE A 446 ? 0.19410 0.17498 0.19889 -0.00412 -0.01543 -0.00734 446 ILE A O   
3571 C CB  . ILE A 446 ? 0.20353 0.17682 0.20815 -0.00821 -0.01799 -0.00218 446 ILE A CB  
3572 C CG1 . ILE A 446 ? 0.18669 0.16301 0.18911 -0.00837 -0.01670 -0.00181 446 ILE A CG1 
3573 C CG2 . ILE A 446 ? 0.21586 0.18671 0.22248 -0.00587 -0.01901 -0.00166 446 ILE A CG2 
3574 C CD1 . ILE A 446 ? 0.19425 0.17098 0.19441 -0.01193 -0.01634 -0.00038 446 ILE A CD1 
3575 N N   . TYR A 447 ? 0.15925 0.13549 0.16649 -0.00244 -0.01684 -0.00784 447 TYR A N   
3576 C CA  . TYR A 447 ? 0.20388 0.18236 0.21073 -0.00008 -0.01608 -0.00953 447 TYR A CA  
3577 C C   . TYR A 447 ? 0.18084 0.16140 0.18770 -0.00011 -0.01591 -0.01187 447 TYR A C   
3578 O O   . TYR A 447 ? 0.17300 0.15604 0.17889 0.00133  -0.01546 -0.01290 447 TYR A O   
3579 C CB  . TYR A 447 ? 0.18581 0.16224 0.19405 0.00178  -0.01625 -0.00993 447 TYR A CB  
3580 C CG  . TYR A 447 ? 0.18559 0.16092 0.19394 0.00230  -0.01646 -0.00776 447 TYR A CG  
3581 C CD1 . TYR A 447 ? 0.18066 0.15800 0.18757 0.00368  -0.01560 -0.00750 447 TYR A CD1 
3582 C CD2 . TYR A 447 ? 0.20577 0.17804 0.21574 0.00129  -0.01771 -0.00582 447 TYR A CD2 
3583 C CE1 . TYR A 447 ? 0.16887 0.14544 0.17590 0.00398  -0.01582 -0.00564 447 TYR A CE1 
3584 C CE2 . TYR A 447 ? 0.23095 0.20251 0.24108 0.00162  -0.01821 -0.00372 447 TYR A CE2 
3585 C CZ  . TYR A 447 ? 0.19357 0.16742 0.20221 0.00294  -0.01718 -0.00377 447 TYR A CZ  
3586 O OH  . TYR A 447 ? 0.20464 0.17801 0.21347 0.00311  -0.01769 -0.00181 447 TYR A OH  
3587 N N   . GLU A 448 ? 0.19521 0.17478 0.20308 -0.00184 -0.01640 -0.01259 448 GLU A N   
3588 C CA  . GLU A 448 ? 0.20969 0.19140 0.21773 -0.00226 -0.01643 -0.01482 448 GLU A CA  
3589 C C   . GLU A 448 ? 0.17604 0.15839 0.18455 -0.00480 -0.01655 -0.01455 448 GLU A C   
3590 O O   . GLU A 448 ? 0.30075 0.28121 0.31036 -0.00636 -0.01700 -0.01526 448 GLU A O   
3591 C CB  . GLU A 448 ? 0.23355 0.21326 0.24270 -0.00187 -0.01671 -0.01688 448 GLU A CB  
3592 C CG  . GLU A 448 ? 0.25394 0.23205 0.26337 0.00013  -0.01637 -0.01714 448 GLU A CG  
3593 C CD  . GLU A 448 ? 0.25116 0.22743 0.26212 0.00026  -0.01626 -0.01973 448 GLU A CD  
3594 O OE1 . GLU A 448 ? 0.32935 0.30724 0.33966 -0.00051 -0.01626 -0.02188 448 GLU A OE1 
3595 O OE2 . GLU A 448 ? 0.29655 0.26986 0.30965 0.00107  -0.01616 -0.01974 448 GLU A OE2 
3596 N N   . PRO A 449 ? 0.20504 0.19008 0.21296 -0.00542 -0.01596 -0.01371 449 PRO A N   
3597 C CA  . PRO A 449 ? 0.23716 0.22312 0.24564 -0.00817 -0.01571 -0.01366 449 PRO A CA  
3598 C C   . PRO A 449 ? 0.21504 0.20308 0.22487 -0.00896 -0.01602 -0.01588 449 PRO A C   
3599 O O   . PRO A 449 ? 0.19740 0.18522 0.20795 -0.01151 -0.01594 -0.01610 449 PRO A O   
3600 C CB  . PRO A 449 ? 0.12750 0.11645 0.13551 -0.00823 -0.01466 -0.01294 449 PRO A CB  
3601 C CG  . PRO A 449 ? 0.15371 0.14429 0.16143 -0.00525 -0.01464 -0.01327 449 PRO A CG  
3602 C CD  . PRO A 449 ? 0.19873 0.18612 0.20575 -0.00379 -0.01531 -0.01305 449 PRO A CD  
3603 N N   . TRP A 450 ? 0.18436 0.17448 0.19436 -0.00712 -0.01644 -0.01746 450 TRP A N   
3604 C CA  . TRP A 450 ? 0.17336 0.16565 0.18451 -0.00799 -0.01702 -0.01957 450 TRP A CA  
3605 C C   . TRP A 450 ? 0.21091 0.19985 0.22239 -0.00917 -0.01747 -0.02070 450 TRP A C   
3606 O O   . TRP A 450 ? 0.27337 0.26353 0.28591 -0.01071 -0.01784 -0.02238 450 TRP A O   
3607 C CB  . TRP A 450 ? 0.20537 0.20084 0.21609 -0.00596 -0.01763 -0.02062 450 TRP A CB  
3608 C CG  . TRP A 450 ? 0.21787 0.21125 0.22679 -0.00418 -0.01779 -0.02090 450 TRP A CG  
3609 C CD1 . TRP A 450 ? 0.24302 0.23536 0.25142 -0.00433 -0.01820 -0.02284 450 TRP A CD1 
3610 C CD2 . TRP A 450 ? 0.16795 0.16024 0.17550 -0.00223 -0.01729 -0.01951 450 TRP A CD2 
3611 N NE1 . TRP A 450 ? 0.20521 0.19598 0.21208 -0.00263 -0.01785 -0.02285 450 TRP A NE1 
3612 C CE2 . TRP A 450 ? 0.19937 0.19010 0.20574 -0.00128 -0.01736 -0.02073 450 TRP A CE2 
3613 C CE3 . TRP A 450 ? 0.16848 0.16106 0.17575 -0.00138 -0.01666 -0.01757 450 TRP A CE3 
3614 C CZ2 . TRP A 450 ? 0.21634 0.20592 0.22142 0.00051  -0.01682 -0.01999 450 TRP A CZ2 
3615 C CZ3 . TRP A 450 ? 0.19466 0.18596 0.20052 0.00044  -0.01628 -0.01673 450 TRP A CZ3 
3616 C CH2 . TRP A 450 ? 0.20387 0.19374 0.20872 0.00138  -0.01637 -0.01789 450 TRP A CH2 
3617 N N   . THR A 451 ? 0.23862 0.22342 0.24970 -0.00847 -0.01746 -0.01992 451 THR A N   
3618 C CA  . THR A 451 ? 0.25304 0.23410 0.26524 -0.00944 -0.01781 -0.02099 451 THR A CA  
3619 C C   . THR A 451 ? 0.25961 0.23767 0.27271 -0.01198 -0.01796 -0.01950 451 THR A C   
3620 O O   . THR A 451 ? 0.19718 0.17188 0.21167 -0.01309 -0.01834 -0.02026 451 THR A O   
3621 C CB  . THR A 451 ? 0.24686 0.22485 0.25922 -0.00744 -0.01774 -0.02101 451 THR A CB  
3622 O OG1 . THR A 451 ? 0.23508 0.21109 0.24727 -0.00690 -0.01774 -0.01825 451 THR A OG1 
3623 C CG2 . THR A 451 ? 0.28249 0.26326 0.29339 -0.00537 -0.01746 -0.02249 451 THR A CG2 
3624 N N   . ALA A 452 ? 0.28428 0.26334 0.29654 -0.01313 -0.01762 -0.01745 452 ALA A N   
3625 C CA  . ALA A 452 ? 0.26272 0.23902 0.27508 -0.01606 -0.01778 -0.01579 452 ALA A CA  
3626 C C   . ALA A 452 ? 0.25381 0.23175 0.26711 -0.01861 -0.01759 -0.01751 452 ALA A C   
3627 O O   . ALA A 452 ? 0.27105 0.25364 0.28478 -0.01836 -0.01717 -0.01926 452 ALA A O   
3628 C CB  . ALA A 452 ? 0.23272 0.20997 0.24337 -0.01698 -0.01723 -0.01338 452 ALA A CB  
3629 N N   . PRO A 453 ? 0.23260 0.20682 0.24654 -0.02112 -0.01801 -0.01696 453 PRO A N   
3630 C CA  . PRO A 453 ? 0.25705 0.23289 0.27182 -0.02399 -0.01767 -0.01847 453 PRO A CA  
3631 C C   . PRO A 453 ? 0.21918 0.19914 0.23315 -0.02578 -0.01658 -0.01796 453 PRO A C   
3632 O O   . PRO A 453 ? 0.20018 0.18003 0.21251 -0.02595 -0.01613 -0.01582 453 PRO A O   
3633 C CB  . PRO A 453 ? 0.28169 0.25178 0.29693 -0.02642 -0.01837 -0.01710 453 PRO A CB  
3634 C CG  . PRO A 453 ? 0.27046 0.23622 0.28635 -0.02394 -0.01929 -0.01602 453 PRO A CG  
3635 C CD  . PRO A 453 ? 0.25476 0.22305 0.26915 -0.02141 -0.01897 -0.01495 453 PRO A CD  
3636 N N   . LEU A 454 ? 0.20965 0.19351 0.22510 -0.02723 -0.01608 -0.02019 454 LEU A N   
3637 C CA  . LEU A 454 ? 0.21163 0.20003 0.22737 -0.02887 -0.01478 -0.02037 454 LEU A CA  
3638 C C   . LEU A 454 ? 0.24759 0.23352 0.26149 -0.03250 -0.01400 -0.01821 454 LEU A C   
3639 O O   . LEU A 454 ? 0.29345 0.28200 0.30657 -0.03352 -0.01268 -0.01763 454 LEU A O   
3640 C CB  . LEU A 454 ? 0.22302 0.21597 0.24146 -0.02993 -0.01458 -0.02325 454 LEU A CB  
3641 C CG  . LEU A 454 ? 0.16188 0.16050 0.18208 -0.03114 -0.01315 -0.02419 454 LEU A CG  
3642 C CD1 . LEU A 454 ? 0.24432 0.24538 0.26439 -0.02820 -0.01276 -0.02350 454 LEU A CD1 
3643 C CD2 . LEU A 454 ? 0.24804 0.25145 0.27168 -0.03165 -0.01342 -0.02706 454 LEU A CD2 
3644 N N   . GLU A 455 ? 0.19825 0.17908 0.21142 -0.03466 -0.01477 -0.01701 455 GLU A N   
3645 C CA  . GLU A 455 ? 0.23520 0.21292 0.24592 -0.03828 -0.01448 -0.01429 455 GLU A CA  
3646 C C   . GLU A 455 ? 0.21203 0.18808 0.22028 -0.03703 -0.01476 -0.01150 455 GLU A C   
3647 O O   . GLU A 455 ? 0.24100 0.21784 0.24688 -0.03959 -0.01377 -0.00999 455 GLU A O   
3648 C CB  . GLU A 455 ? 0.23300 0.20485 0.24380 -0.04037 -0.01574 -0.01317 455 GLU A CB  
3649 C CG  . GLU A 455 ? 0.22276 0.18984 0.23063 -0.04352 -0.01633 -0.00933 455 GLU A CG  
3650 C CD  . GLU A 455 ? 0.23459 0.20330 0.24065 -0.04859 -0.01487 -0.00907 455 GLU A CD  
3651 O OE1 . GLU A 455 ? 0.23109 0.19853 0.23815 -0.05129 -0.01482 -0.00996 455 GLU A OE1 
3652 O OE2 . GLU A 455 ? 0.24220 0.21352 0.24586 -0.05007 -0.01360 -0.00818 455 GLU A OE2 
3653 N N   . VAL A 456 ? 0.21432 0.18830 0.22307 -0.03330 -0.01597 -0.01099 456 VAL A N   
3654 C CA  . VAL A 456 ? 0.24272 0.21518 0.24948 -0.03198 -0.01639 -0.00841 456 VAL A CA  
3655 C C   . VAL A 456 ? 0.22276 0.20045 0.22893 -0.03077 -0.01484 -0.00935 456 VAL A C   
3656 O O   . VAL A 456 ? 0.18615 0.16392 0.18995 -0.03186 -0.01433 -0.00748 456 VAL A O   
3657 C CB  . VAL A 456 ? 0.22078 0.18982 0.22890 -0.02839 -0.01794 -0.00798 456 VAL A CB  
3658 C CG1 . VAL A 456 ? 0.19092 0.15855 0.19735 -0.02712 -0.01851 -0.00529 456 VAL A CG1 
3659 C CG2 . VAL A 456 ? 0.20834 0.17206 0.21796 -0.02958 -0.01934 -0.00737 456 VAL A CG2 
3660 N N   . GLN A 457 ? 0.18534 0.16740 0.19375 -0.02862 -0.01417 -0.01221 457 GLN A N   
3661 C CA  . GLN A 457 ? 0.22556 0.21246 0.23428 -0.02730 -0.01280 -0.01317 457 GLN A CA  
3662 C C   . GLN A 457 ? 0.23057 0.22005 0.23857 -0.03099 -0.01096 -0.01332 457 GLN A C   
3663 O O   . GLN A 457 ? 0.21401 0.20536 0.22095 -0.03106 -0.00974 -0.01288 457 GLN A O   
3664 C CB  . GLN A 457 ? 0.20647 0.19741 0.21808 -0.02463 -0.01287 -0.01593 457 GLN A CB  
3665 C CG  . GLN A 457 ? 0.23635 0.22535 0.24826 -0.02132 -0.01435 -0.01626 457 GLN A CG  
3666 C CD  . GLN A 457 ? 0.24691 0.24012 0.26094 -0.01919 -0.01463 -0.01868 457 GLN A CD  
3667 O OE1 . GLN A 457 ? 0.23765 0.23543 0.25344 -0.01937 -0.01387 -0.01980 457 GLN A OE1 
3668 N NE2 . GLN A 457 ? 0.22401 0.21576 0.23806 -0.01729 -0.01576 -0.01953 457 GLN A NE2 
3669 N N   . ARG A 458 ? 0.23503 0.22475 0.24367 -0.03429 -0.01054 -0.01418 458 ARG A N   
3670 C CA  . ARG A 458 ? 0.23742 0.22963 0.24530 -0.03835 -0.00849 -0.01458 458 ARG A CA  
3671 C C   . ARG A 458 ? 0.23274 0.22118 0.23616 -0.04141 -0.00848 -0.01144 458 ARG A C   
3672 O O   . ARG A 458 ? 0.24915 0.23987 0.25093 -0.04388 -0.00659 -0.01147 458 ARG A O   
3673 C CB  . ARG A 458 ? 0.25695 0.25039 0.26670 -0.04127 -0.00805 -0.01637 458 ARG A CB  
3674 C CG  . ARG A 458 ? 0.21947 0.21785 0.23380 -0.03896 -0.00794 -0.01963 458 ARG A CG  
3675 C CD  . ARG A 458 ? 0.23063 0.22959 0.24676 -0.04174 -0.00793 -0.02126 458 ARG A CD  
3676 N NE  . ARG A 458 ? 0.22759 0.23069 0.24786 -0.03927 -0.00858 -0.02399 458 ARG A NE  
3677 C CZ  . ARG A 458 ? 0.22325 0.23248 0.24742 -0.03947 -0.00740 -0.02649 458 ARG A CZ  
3678 N NH1 . ARG A 458 ? 0.22338 0.23552 0.24817 -0.04208 -0.00507 -0.02711 458 ARG A NH1 
3679 N NH2 . ARG A 458 ? 0.22007 0.23271 0.24778 -0.03711 -0.00862 -0.02850 458 ARG A NH2 
3680 N N   . LYS A 459 ? 0.28224 0.26497 0.28385 -0.04144 -0.01062 -0.00875 459 LYS A N   
3681 C CA  . LYS A 459 ? 0.23016 0.20908 0.22760 -0.04424 -0.01126 -0.00522 459 LYS A CA  
3682 C C   . LYS A 459 ? 0.18381 0.16406 0.17960 -0.04252 -0.01081 -0.00434 459 LYS A C   
3683 O O   . LYS A 459 ? 0.23459 0.21465 0.22678 -0.04575 -0.01010 -0.00265 459 LYS A O   
3684 C CB  . LYS A 459 ? 0.30998 0.28253 0.30714 -0.04378 -0.01402 -0.00254 459 LYS A CB  
3685 C CG  . LYS A 459 ? 0.31708 0.28694 0.31444 -0.04725 -0.01447 -0.00231 459 LYS A CG  
3686 C CD  . LYS A 459 ? 0.28194 0.25097 0.27517 -0.05298 -0.01371 -0.00018 459 LYS A CD  
3687 C CE  . LYS A 459 ? 0.27925 0.24787 0.27297 -0.05684 -0.01305 -0.00119 459 LYS A CE  
3688 N NZ  . LYS A 459 ? 0.27317 0.23640 0.26893 -0.05598 -0.01534 -0.00022 459 LYS A NZ  
3689 N N   . ALA A 460 ? 0.23148 0.21313 0.22958 -0.03773 -0.01117 -0.00550 460 ALA A N   
3690 C CA  . ALA A 460 ? 0.20938 0.19205 0.20622 -0.03580 -0.01082 -0.00474 460 ALA A CA  
3691 C C   . ALA A 460 ? 0.22245 0.21066 0.22030 -0.03585 -0.00818 -0.00730 460 ALA A C   
3692 O O   . ALA A 460 ? 0.25218 0.24134 0.24847 -0.03548 -0.00738 -0.00675 460 ALA A O   
3693 C CB  . ALA A 460 ? 0.24550 0.22680 0.24423 -0.03082 -0.01238 -0.00467 460 ALA A CB  
3694 N N   . GLY A 461 ? 0.22494 0.21682 0.22575 -0.03636 -0.00682 -0.01015 461 GLY A N   
3695 C CA  . GLY A 461 ? 0.28091 0.27815 0.28407 -0.03593 -0.00444 -0.01281 461 GLY A CA  
3696 C C   . GLY A 461 ? 0.21387 0.21298 0.21988 -0.03088 -0.00492 -0.01387 461 GLY A C   
3697 O O   . GLY A 461 ? 0.26522 0.26704 0.27209 -0.02988 -0.00342 -0.01480 461 GLY A O   
3698 N N   . CYS A 462 ? 0.28052 0.27808 0.28789 -0.02784 -0.00695 -0.01378 462 CYS A N   
3699 C CA  . CYS A 462 ? 0.24797 0.24693 0.25736 -0.02336 -0.00765 -0.01450 462 CYS A CA  
3700 C C   . CYS A 462 ? 0.25803 0.25792 0.27008 -0.02176 -0.00897 -0.01603 462 CYS A C   
3701 O O   . CYS A 462 ? 0.26517 0.26243 0.27661 -0.01973 -0.01065 -0.01542 462 CYS A O   
3702 C CB  . CYS A 462 ? 0.28621 0.28152 0.29302 -0.02121 -0.00888 -0.01222 462 CYS A CB  
3703 S SG  . CYS A 462 ? 0.23183 0.22924 0.24025 -0.01653 -0.00900 -0.01291 462 CYS A SG  
3704 N N   . VAL A 463 ? 0.21363 0.21755 0.22887 -0.02288 -0.00811 -0.01824 463 VAL A N   
3705 C CA  . VAL A 463 ? 0.20699 0.21253 0.22488 -0.02162 -0.00943 -0.01986 463 VAL A CA  
3706 C C   . VAL A 463 ? 0.19986 0.20734 0.21928 -0.01753 -0.01042 -0.02025 463 VAL A C   
3707 O O   . VAL A 463 ? 0.23842 0.24926 0.26014 -0.01630 -0.00955 -0.02090 463 VAL A O   
3708 C CB  . VAL A 463 ? 0.21930 0.22903 0.24063 -0.02410 -0.00833 -0.02210 463 VAL A CB  
3709 C CG1 . VAL A 463 ? 0.17785 0.18990 0.20212 -0.02261 -0.00994 -0.02377 463 VAL A CG1 
3710 C CG2 . VAL A 463 ? 0.29623 0.30363 0.31546 -0.02852 -0.00745 -0.02156 463 VAL A CG2 
3711 N N   . VAL A 464 ? 0.22962 0.23492 0.24786 -0.01558 -0.01219 -0.01992 464 VAL A N   
3712 C CA  . VAL A 464 ? 0.22575 0.23247 0.24452 -0.01209 -0.01325 -0.02002 464 VAL A CA  
3713 C C   . VAL A 464 ? 0.19578 0.20763 0.21858 -0.01150 -0.01373 -0.02178 464 VAL A C   
3714 O O   . VAL A 464 ? 0.18582 0.19916 0.21020 -0.01281 -0.01446 -0.02320 464 VAL A O   
3715 C CB  . VAL A 464 ? 0.18952 0.19302 0.20604 -0.01074 -0.01476 -0.01973 464 VAL A CB  
3716 C CG1 . VAL A 464 ? 0.16725 0.17277 0.18401 -0.00778 -0.01590 -0.02005 464 VAL A CG1 
3717 C CG2 . VAL A 464 ? 0.16764 0.16646 0.18123 -0.01068 -0.01446 -0.01786 464 VAL A CG2 
3718 N N   . GLY A 465 ? 0.18806 0.20265 0.21291 -0.00954 -0.01342 -0.02168 465 GLY A N   
3719 C CA  . GLY A 465 ? 0.15135 0.17094 0.18096 -0.00871 -0.01403 -0.02304 465 GLY A CA  
3720 C C   . GLY A 465 ? 0.19189 0.21462 0.22543 -0.01000 -0.01195 -0.02411 465 GLY A C   
3721 O O   . GLY A 465 ? 0.27619 0.30289 0.31447 -0.00851 -0.01221 -0.02493 465 GLY A O   
3722 N N   . ARG A 466 ? 0.16013 0.18120 0.19199 -0.01287 -0.00990 -0.02415 466 ARG A N   
3723 C CA  . ARG A 466 ? 0.16118 0.18503 0.19602 -0.01478 -0.00738 -0.02547 466 ARG A CA  
3724 C C   . ARG A 466 ? 0.20059 0.22221 0.23267 -0.01490 -0.00561 -0.02432 466 ARG A C   
3725 O O   . ARG A 466 ? 0.13113 0.15528 0.16637 -0.01412 -0.00413 -0.02524 466 ARG A O   
3726 C CB  . ARG A 466 ? 0.23445 0.25866 0.26923 -0.01888 -0.00620 -0.02664 466 ARG A CB  
3727 C CG  . ARG A 466 ? 0.28014 0.30737 0.31759 -0.02162 -0.00318 -0.02839 466 ARG A CG  
3728 C CD  . ARG A 466 ? 0.32108 0.34843 0.35784 -0.02601 -0.00207 -0.02936 466 ARG A CD  
3729 N NE  . ARG A 466 ? 0.38842 0.41024 0.41870 -0.02817 -0.00232 -0.02708 466 ARG A NE  
3730 C CZ  . ARG A 466 ? 0.43762 0.45739 0.46422 -0.03083 -0.00052 -0.02608 466 ARG A CZ  
3731 N NH1 . ARG A 466 ? 0.35274 0.37548 0.38109 -0.03191 0.00208  -0.02751 466 ARG A NH1 
3732 N NH2 . ARG A 466 ? 0.40828 0.42290 0.42947 -0.03254 -0.00140 -0.02362 466 ARG A NH2 
3733 N N   . ASP A 467 ? 0.24852 0.26546 0.27509 -0.01588 -0.00579 -0.02239 467 ASP A N   
3734 C CA  . ASP A 467 ? 0.20792 0.22265 0.23139 -0.01627 -0.00442 -0.02109 467 ASP A CA  
3735 C C   . ASP A 467 ? 0.15339 0.16565 0.17474 -0.01286 -0.00579 -0.01932 467 ASP A C   
3736 O O   . ASP A 467 ? 0.14347 0.15555 0.16426 -0.01211 -0.00467 -0.01886 467 ASP A O   
3737 C CB  . ASP A 467 ? 0.20146 0.21274 0.22040 -0.01989 -0.00389 -0.01978 467 ASP A CB  
3738 C CG  . ASP A 467 ? 0.23440 0.24780 0.25467 -0.02386 -0.00234 -0.02138 467 ASP A CG  
3739 O OD1 . ASP A 467 ? 0.20244 0.21988 0.22617 -0.02483 -0.00020 -0.02351 467 ASP A OD1 
3740 O OD2 . ASP A 467 ? 0.28663 0.29762 0.30475 -0.02610 -0.00315 -0.02062 467 ASP A OD2 
3741 N N   . TYR A 468 ? 0.16821 0.17862 0.18831 -0.01102 -0.00799 -0.01853 468 TYR A N   
3742 C CA  . TYR A 468 ? 0.12756 0.13592 0.14573 -0.00797 -0.00918 -0.01713 468 TYR A CA  
3743 C C   . TYR A 468 ? 0.15454 0.16428 0.17423 -0.00583 -0.01116 -0.01775 468 TYR A C   
3744 O O   . TYR A 468 ? 0.15798 0.16802 0.17815 -0.00699 -0.01205 -0.01861 468 TYR A O   
3745 C CB  . TYR A 468 ? 0.16825 0.17196 0.18210 -0.00854 -0.00969 -0.01532 468 TYR A CB  
3746 C CG  . TYR A 468 ? 0.17241 0.17419 0.18443 -0.00569 -0.01048 -0.01408 468 TYR A CG  
3747 C CD1 . TYR A 468 ? 0.13527 0.13696 0.14658 -0.00481 -0.00945 -0.01326 468 TYR A CD1 
3748 C CD2 . TYR A 468 ? 0.18301 0.18313 0.19400 -0.00413 -0.01206 -0.01396 468 TYR A CD2 
3749 C CE1 . TYR A 468 ? 0.14310 0.14313 0.15277 -0.00240 -0.01007 -0.01219 468 TYR A CE1 
3750 C CE2 . TYR A 468 ? 0.14975 0.14833 0.15907 -0.00181 -0.01252 -0.01307 468 TYR A CE2 
3751 C CZ  . TYR A 468 ? 0.12471 0.12326 0.13340 -0.00094 -0.01156 -0.01210 468 TYR A CZ  
3752 O OH  . TYR A 468 ? 0.11792 0.11504 0.12500 0.00118  -0.01193 -0.01128 468 TYR A OH  
3753 N N   . PRO A 469 ? 0.14449 0.15512 0.16478 -0.00299 -0.01193 -0.01730 469 PRO A N   
3754 C CA  . PRO A 469 ? 0.16324 0.17566 0.18474 -0.00136 -0.01398 -0.01776 469 PRO A CA  
3755 C C   . PRO A 469 ? 0.16689 0.17646 0.18488 -0.00128 -0.01527 -0.01749 469 PRO A C   
3756 O O   . PRO A 469 ? 0.15689 0.16286 0.17179 -0.00145 -0.01481 -0.01658 469 PRO A O   
3757 C CB  . PRO A 469 ? 0.15270 0.16603 0.17501 0.00135  -0.01435 -0.01683 469 PRO A CB  
3758 C CG  . PRO A 469 ? 0.12328 0.13374 0.14295 0.00145  -0.01281 -0.01569 469 PRO A CG  
3759 C CD  . PRO A 469 ? 0.13534 0.14539 0.15510 -0.00138 -0.01105 -0.01628 469 PRO A CD  
3760 N N   . ALA A 470 ? 0.14142 0.15285 0.16029 -0.00111 -0.01694 -0.01846 470 ALA A N   
3761 C CA  . ALA A 470 ? 0.15372 0.16319 0.16967 -0.00093 -0.01816 -0.01876 470 ALA A CA  
3762 C C   . ALA A 470 ? 0.16819 0.17663 0.18157 0.00134  -0.01875 -0.01766 470 ALA A C   
3763 O O   . ALA A 470 ? 0.15120 0.16132 0.16567 0.00290  -0.01892 -0.01672 470 ALA A O   
3764 C CB  . ALA A 470 ? 0.13034 0.14272 0.14799 -0.00176 -0.01975 -0.02027 470 ALA A CB  
3765 N N   . PRO A 471 ? 0.18165 0.18728 0.19184 0.00147  -0.01892 -0.01785 471 PRO A N   
3766 C CA  . PRO A 471 ? 0.15332 0.15812 0.16083 0.00329  -0.01924 -0.01702 471 PRO A CA  
3767 C C   . PRO A 471 ? 0.14966 0.15767 0.15728 0.00409  -0.02105 -0.01694 471 PRO A C   
3768 O O   . PRO A 471 ? 0.16535 0.17511 0.17314 0.00310  -0.02240 -0.01815 471 PRO A O   
3769 C CB  . PRO A 471 ? 0.15693 0.15868 0.16191 0.00276  -0.01897 -0.01804 471 PRO A CB  
3770 C CG  . PRO A 471 ? 0.16088 0.16255 0.16730 0.00079  -0.01922 -0.01956 471 PRO A CG  
3771 C CD  . PRO A 471 ? 0.22480 0.22777 0.23404 -0.00009 -0.01869 -0.01896 471 PRO A CD  
3772 N N   . ILE A 472 ? 0.16727 0.17596 0.17484 0.00577  -0.02122 -0.01536 472 ILE A N   
3773 C CA  . ILE A 472 ? 0.19591 0.20747 0.20392 0.00660  -0.02329 -0.01464 472 ILE A CA  
3774 C C   . ILE A 472 ? 0.19675 0.20801 0.20056 0.00611  -0.02455 -0.01515 472 ILE A C   
3775 O O   . ILE A 472 ? 0.24632 0.26025 0.25008 0.00582  -0.02676 -0.01505 472 ILE A O   
3776 C CB  . ILE A 472 ? 0.21075 0.22238 0.21963 0.00848  -0.02312 -0.01267 472 ILE A CB  
3777 C CG1 . ILE A 472 ? 0.18269 0.19096 0.18778 0.00915  -0.02165 -0.01192 472 ILE A CG1 
3778 C CG2 . ILE A 472 ? 0.20472 0.21759 0.21842 0.00868  -0.02198 -0.01268 472 ILE A CG2 
3779 C CD1 . ILE A 472 ? 0.16989 0.17797 0.17500 0.01083  -0.02166 -0.00998 472 ILE A CD1 
3780 N N   . VAL A 473 ? 0.17214 0.18036 0.17253 0.00588  -0.02320 -0.01578 473 VAL A N   
3781 C CA  . VAL A 473 ? 0.21374 0.22153 0.21008 0.00503  -0.02376 -0.01691 473 VAL A CA  
3782 C C   . VAL A 473 ? 0.19161 0.19664 0.18732 0.00398  -0.02214 -0.01898 473 VAL A C   
3783 O O   . VAL A 473 ? 0.19091 0.19375 0.18843 0.00426  -0.02066 -0.01882 473 VAL A O   
3784 C CB  . VAL A 473 ? 0.16999 0.17694 0.16268 0.00600  -0.02366 -0.01555 473 VAL A CB  
3785 C CG1 . VAL A 473 ? 0.23944 0.24873 0.23294 0.00704  -0.02559 -0.01322 473 VAL A CG1 
3786 C CG2 . VAL A 473 ? 0.22893 0.23286 0.22151 0.00704  -0.02138 -0.01507 473 VAL A CG2 
3787 N N   . ASP A 474 ? 0.21282 0.21795 0.20605 0.00263  -0.02252 -0.02095 474 ASP A N   
3788 C CA  . ASP A 474 ? 0.26526 0.26749 0.25784 0.00184  -0.02090 -0.02314 474 ASP A CA  
3789 C C   . ASP A 474 ? 0.23298 0.23352 0.22264 0.00265  -0.01960 -0.02307 474 ASP A C   
3790 O O   . ASP A 474 ? 0.22646 0.22843 0.21257 0.00233  -0.02023 -0.02301 474 ASP A O   
3791 C CB  . ASP A 474 ? 0.26728 0.27047 0.25887 -0.00021 -0.02161 -0.02579 474 ASP A CB  
3792 C CG  . ASP A 474 ? 0.32795 0.32793 0.31984 -0.00100 -0.01984 -0.02835 474 ASP A CG  
3793 O OD1 . ASP A 474 ? 0.35770 0.35478 0.35115 0.00011  -0.01836 -0.02780 474 ASP A OD1 
3794 O OD2 . ASP A 474 ? 0.33419 0.33456 0.32504 -0.00278 -0.02000 -0.03096 474 ASP A OD2 
3795 N N   . HIS A 475 ? 0.25657 0.25420 0.24772 0.00353  -0.01789 -0.02296 475 HIS A N   
3796 C CA  . HIS A 475 ? 0.22785 0.22413 0.21701 0.00443  -0.01652 -0.02281 475 HIS A CA  
3797 C C   . HIS A 475 ? 0.21196 0.20830 0.19813 0.00316  -0.01585 -0.02551 475 HIS A C   
3798 O O   . HIS A 475 ? 0.24668 0.24379 0.22938 0.00315  -0.01552 -0.02529 475 HIS A O   
3799 C CB  . HIS A 475 ? 0.25161 0.24493 0.24357 0.00538  -0.01506 -0.02246 475 HIS A CB  
3800 C CG  . HIS A 475 ? 0.19769 0.18978 0.18840 0.00620  -0.01353 -0.02276 475 HIS A CG  
3801 N ND1 . HIS A 475 ? 0.16885 0.16167 0.15771 0.00723  -0.01333 -0.02082 475 HIS A ND1 
3802 C CD2 . HIS A 475 ? 0.21999 0.21028 0.21143 0.00607  -0.01203 -0.02497 475 HIS A CD2 
3803 C CE1 . HIS A 475 ? 0.17189 0.16354 0.16011 0.00758  -0.01175 -0.02177 475 HIS A CE1 
3804 N NE2 . HIS A 475 ? 0.22644 0.21667 0.21644 0.00695  -0.01091 -0.02437 475 HIS A NE2 
3805 N N   . ALA A 476 ? 0.22001 0.21549 0.20740 0.00185  -0.01550 -0.02820 476 ALA A N   
3806 C CA  . ALA A 476 ? 0.20099 0.19644 0.18590 0.00035  -0.01445 -0.03143 476 ALA A CA  
3807 C C   . ALA A 476 ? 0.23758 0.23612 0.21744 -0.00098 -0.01572 -0.03130 476 ALA A C   
3808 O O   . ALA A 476 ? 0.26386 0.26271 0.24009 -0.00191 -0.01462 -0.03276 476 ALA A O   
3809 C CB  . ALA A 476 ? 0.23554 0.22974 0.22294 -0.00101 -0.01417 -0.03430 476 ALA A CB  
3810 N N   . VAL A 477 ? 0.24210 0.24305 0.22175 -0.00123 -0.01810 -0.02950 477 VAL A N   
3811 C CA  . VAL A 477 ? 0.24305 0.24700 0.21821 -0.00255 -0.01995 -0.02886 477 VAL A CA  
3812 C C   . VAL A 477 ? 0.24349 0.24792 0.21654 -0.00120 -0.02044 -0.02567 477 VAL A C   
3813 O O   . VAL A 477 ? 0.27380 0.27906 0.24201 -0.00231 -0.02052 -0.02561 477 VAL A O   
3814 C CB  . VAL A 477 ? 0.24624 0.25283 0.22284 -0.00333 -0.02255 -0.02827 477 VAL A CB  
3815 C CG1 . VAL A 477 ? 0.29142 0.30116 0.26331 -0.00510 -0.02482 -0.02780 477 VAL A CG1 
3816 C CG2 . VAL A 477 ? 0.28245 0.28808 0.26176 -0.00455 -0.02186 -0.03123 477 VAL A CG2 
3817 N N   . ALA A 478 ? 0.17828 0.18211 0.15478 0.00095  -0.02070 -0.02304 478 ALA A N   
3818 C CA  . ALA A 478 ? 0.18634 0.19041 0.16147 0.00229  -0.02117 -0.02001 478 ALA A CA  
3819 C C   . ALA A 478 ? 0.23313 0.23526 0.20568 0.00247  -0.01887 -0.02056 478 ALA A C   
3820 O O   . ALA A 478 ? 0.20313 0.20572 0.17225 0.00243  -0.01923 -0.01882 478 ALA A O   
3821 C CB  . ALA A 478 ? 0.18876 0.19251 0.16853 0.00432  -0.02147 -0.01773 478 ALA A CB  
3822 N N   . SER A 479 ? 0.18466 0.18465 0.15910 0.00259  -0.01655 -0.02292 479 SER A N   
3823 C CA  . SER A 479 ? 0.24036 0.23886 0.21318 0.00273  -0.01423 -0.02385 479 SER A CA  
3824 C C   . SER A 479 ? 0.22732 0.22695 0.19489 0.00041  -0.01367 -0.02598 479 SER A C   
3825 O O   . SER A 479 ? 0.22652 0.22625 0.19058 0.00005  -0.01282 -0.02532 479 SER A O   
3826 C CB  . SER A 479 ? 0.23314 0.22920 0.21026 0.00352  -0.01221 -0.02581 479 SER A CB  
3827 O OG  . SER A 479 ? 0.29264 0.28844 0.27073 0.00212  -0.01191 -0.02895 479 SER A OG  
3828 N N   . LYS A 480 ? 0.25310 0.25363 0.21984 -0.00148 -0.01401 -0.02867 480 LYS A N   
3829 C CA  . LYS A 480 ? 0.27983 0.28164 0.24112 -0.00420 -0.01336 -0.03104 480 LYS A CA  
3830 C C   . LYS A 480 ? 0.26148 0.26565 0.21735 -0.00544 -0.01588 -0.02829 480 LYS A C   
3831 O O   . LYS A 480 ? 0.35876 0.36405 0.30896 -0.00800 -0.01545 -0.02960 480 LYS A O   
3832 C CB  . LYS A 480 ? 0.27957 0.28174 0.24147 -0.00612 -0.01308 -0.03483 480 LYS A CB  
3833 C CG  . LYS A 480 ? 0.39863 0.39816 0.36561 -0.00532 -0.01047 -0.03798 480 LYS A CG  
3834 C CD  . LYS A 480 ? 0.42758 0.42724 0.39525 -0.00737 -0.01018 -0.04181 480 LYS A CD  
3835 C CE  . LYS A 480 ? 0.42377 0.42039 0.39715 -0.00647 -0.00774 -0.04479 480 LYS A CE  
3836 N NZ  . LYS A 480 ? 0.44548 0.44180 0.42003 -0.00845 -0.00735 -0.04864 480 LYS A NZ  
3837 N N   . ALA A 481 ? 0.27481 0.27976 0.23238 -0.00387 -0.01851 -0.02457 481 ALA A N   
3838 C CA  . ALA A 481 ? 0.27094 0.27784 0.22430 -0.00471 -0.02128 -0.02144 481 ALA A CA  
3839 C C   . ALA A 481 ? 0.27270 0.27844 0.22468 -0.00343 -0.02082 -0.01848 481 ALA A C   
3840 O O   . ALA A 481 ? 0.34436 0.35093 0.29097 -0.00497 -0.02197 -0.01676 481 ALA A O   
3841 C CB  . ALA A 481 ? 0.25628 0.26497 0.21299 -0.00375 -0.02456 -0.01919 481 ALA A CB  
3842 N N   . CYS A 482 ? 0.26790 0.27166 0.22441 -0.00087 -0.01925 -0.01776 482 CYS A N   
3843 C CA  . CYS A 482 ? 0.24128 0.24377 0.19671 0.00024  -0.01845 -0.01535 482 CYS A CA  
3844 C C   . CYS A 482 ? 0.24841 0.25016 0.19964 -0.00142 -0.01569 -0.01748 482 CYS A C   
3845 O O   . CYS A 482 ? 0.25975 0.26140 0.20675 -0.00222 -0.01571 -0.01563 482 CYS A O   
3846 C CB  . CYS A 482 ? 0.21764 0.21847 0.17894 0.00306  -0.01745 -0.01437 482 CYS A CB  
3847 S SG  . CYS A 482 ? 0.18175 0.18364 0.14812 0.00485  -0.02020 -0.01191 482 CYS A SG  
3848 N N   . ILE A 483 ? 0.23406 0.23525 0.18673 -0.00202 -0.01322 -0.02144 483 ILE A N   
3849 C CA  . ILE A 483 ? 0.24898 0.24979 0.19861 -0.00366 -0.01021 -0.02417 483 ILE A CA  
3850 C C   . ILE A 483 ? 0.28300 0.28559 0.22508 -0.00706 -0.01091 -0.02454 483 ILE A C   
3851 O O   . ILE A 483 ? 0.25569 0.25826 0.19330 -0.00851 -0.00956 -0.02427 483 ILE A O   
3852 C CB  . ILE A 483 ? 0.24799 0.24790 0.20175 -0.00356 -0.00770 -0.02855 483 ILE A CB  
3853 C CG1 . ILE A 483 ? 0.26683 0.26478 0.22738 -0.00049 -0.00707 -0.02771 483 ILE A CG1 
3854 C CG2 . ILE A 483 ? 0.26323 0.26327 0.21425 -0.00558 -0.00445 -0.03211 483 ILE A CG2 
3855 C CD1 . ILE A 483 ? 0.26830 0.26500 0.23374 -0.00013 -0.00523 -0.03133 483 ILE A CD1 
3856 N N   . ALA A 484 ? 0.27573 0.28000 0.21604 -0.00866 -0.01311 -0.02507 484 ALA A N   
3857 C CA  . ALA A 484 ? 0.30804 0.31420 0.24069 -0.01234 -0.01404 -0.02541 484 ALA A CA  
3858 C C   . ALA A 484 ? 0.29392 0.30036 0.22228 -0.01260 -0.01650 -0.02055 484 ALA A C   
3859 O O   . ALA A 484 ? 0.31742 0.32448 0.23888 -0.01554 -0.01611 -0.02038 484 ALA A O   
3860 C CB  . ALA A 484 ? 0.26978 0.27787 0.20185 -0.01394 -0.01630 -0.02669 484 ALA A CB  
3861 N N   . ARG A 485 ? 0.26073 0.26661 0.19317 -0.00970 -0.01895 -0.01663 485 ARG A N   
3862 C CA  . ARG A 485 ? 0.27217 0.27789 0.20163 -0.00960 -0.02138 -0.01188 485 ARG A CA  
3863 C C   . ARG A 485 ? 0.29550 0.29916 0.22423 -0.00887 -0.01879 -0.01104 485 ARG A C   
3864 O O   . ARG A 485 ? 0.34010 0.34341 0.26400 -0.01015 -0.01983 -0.00808 485 ARG A O   
3865 C CB  . ARG A 485 ? 0.27119 0.27715 0.20608 -0.00677 -0.02468 -0.00843 485 ARG A CB  
3866 C CG  . ARG A 485 ? 0.32064 0.32901 0.25653 -0.00758 -0.02753 -0.00900 485 ARG A CG  
3867 C CD  . ARG A 485 ? 0.27970 0.28844 0.22265 -0.00452 -0.02982 -0.00668 485 ARG A CD  
3868 N NE  . ARG A 485 ? 0.32579 0.33462 0.26858 -0.00365 -0.03294 -0.00196 485 ARG A NE  
3869 C CZ  . ARG A 485 ? 0.25683 0.26551 0.20594 -0.00075 -0.03441 0.00041  485 ARG A CZ  
3870 N NH1 . ARG A 485 ? 0.29607 0.30458 0.25156 0.00135  -0.03299 -0.00133 485 ARG A NH1 
3871 N NH2 . ARG A 485 ? 0.26851 0.27716 0.21764 -0.00011 -0.03734 0.00461  485 ARG A NH2 
3872 N N   . MET A 486 ? 0.29812 0.30038 0.23158 -0.00698 -0.01556 -0.01348 486 MET A N   
3873 C CA  . MET A 486 ? 0.30756 0.30822 0.24044 -0.00655 -0.01290 -0.01317 486 MET A CA  
3874 C C   . MET A 486 ? 0.31628 0.31760 0.24269 -0.01010 -0.01046 -0.01573 486 MET A C   
3875 O O   . MET A 486 ? 0.33152 0.33216 0.25398 -0.01122 -0.00962 -0.01408 486 MET A O   
3876 C CB  . MET A 486 ? 0.30073 0.30004 0.24058 -0.00378 -0.01042 -0.01509 486 MET A CB  
3877 C CG  . MET A 486 ? 0.29525 0.29372 0.24095 -0.00056 -0.01222 -0.01239 486 MET A CG  
3878 S SD  . MET A 486 ? 0.34649 0.34372 0.29136 0.00066  -0.01365 -0.00746 486 MET A SD  
3879 C CE  . MET A 486 ? 0.30235 0.29807 0.24724 0.00077  -0.00971 -0.00886 486 MET A CE  
3880 N N   . ALA A 487 ? 0.33817 0.34077 0.26348 -0.01209 -0.00910 -0.01998 487 ALA A N   
3881 C CA  . ALA A 487 ? 0.33197 0.33561 0.25092 -0.01597 -0.00660 -0.02300 487 ALA A CA  
3882 C C   . ALA A 487 ? 0.38138 0.38601 0.29177 -0.01920 -0.00919 -0.01979 487 ALA A C   
3883 O O   . ALA A 487 ? 0.42474 0.42940 0.32930 -0.02192 -0.00744 -0.01990 487 ALA A O   
3884 C CB  . ALA A 487 ? 0.24176 0.24660 0.16165 -0.01750 -0.00493 -0.02826 487 ALA A CB  
3885 N N   . ALA A 488 ? 0.39338 0.39889 0.30298 -0.01911 -0.01347 -0.01684 488 ALA A N   
3886 C CA  . ALA A 488 ? 0.38295 0.38927 0.28496 -0.02196 -0.01668 -0.01302 488 ALA A CA  
3887 C C   . ALA A 488 ? 0.47089 0.47521 0.37222 -0.02072 -0.01738 -0.00841 488 ALA A C   
3888 O O   . ALA A 488 ? 0.47603 0.48017 0.37009 -0.02383 -0.01739 -0.00671 488 ALA A O   
3889 C CB  . ALA A 488 ? 0.34543 0.35327 0.24836 -0.02159 -0.02142 -0.01066 488 ALA A CB  
3890 N N   . ALA A 489 ? 0.47121 0.47390 0.37995 -0.01641 -0.01783 -0.00644 489 ALA A N   
3891 C CA  . ALA A 489 ? 0.47322 0.47377 0.38215 -0.01503 -0.01823 -0.00241 489 ALA A CA  
3892 C C   . ALA A 489 ? 0.48022 0.47984 0.38606 -0.01665 -0.01402 -0.00437 489 ALA A C   
3893 O O   . ALA A 489 ? 0.47259 0.47097 0.37399 -0.01804 -0.01432 -0.00132 489 ALA A O   
3894 C CB  . ALA A 489 ? 0.42396 0.42318 0.34171 -0.01036 -0.01884 -0.00093 489 ALA A CB  
3895 N N   . TYR A 490 ? 0.46495 0.46515 0.37333 -0.01660 -0.01009 -0.00947 490 TYR A N   
3896 C CA  . TYR A 490 ? 0.45284 0.45254 0.35965 -0.01789 -0.00586 -0.01183 490 TYR A CA  
3897 C C   . TYR A 490 ? 0.50957 0.51060 0.40723 -0.02301 -0.00450 -0.01334 490 TYR A C   
3898 O O   . TYR A 490 ? 0.56610 0.56678 0.46108 -0.02471 -0.00139 -0.01435 490 TYR A O   
3899 C CB  . TYR A 490 ? 0.41106 0.41100 0.32469 -0.01593 -0.00234 -0.01671 490 TYR A CB  
3900 C CG  . TYR A 490 ? 0.35536 0.35356 0.27576 -0.01221 -0.00135 -0.01550 490 TYR A CG  
3901 C CD1 . TYR A 490 ? 0.40876 0.40619 0.32834 -0.01268 0.00130  -0.01544 490 TYR A CD1 
3902 C CD2 . TYR A 490 ? 0.34063 0.33810 0.26800 -0.00855 -0.00303 -0.01449 490 TYR A CD2 
3903 C CE1 . TYR A 490 ? 0.40005 0.39607 0.32558 -0.00955 0.00210  -0.01439 490 TYR A CE1 
3904 C CE2 . TYR A 490 ? 0.30564 0.30166 0.23863 -0.00559 -0.00215 -0.01344 490 TYR A CE2 
3905 C CZ  . TYR A 490 ? 0.33109 0.32641 0.26314 -0.00607 0.00033  -0.01338 490 TYR A CZ  
3906 O OH  . TYR A 490 ? 0.24861 0.24269 0.18603 -0.00339 0.00112  -0.01241 490 TYR A OH  
3907 N N   . ARG A 491 ? 0.49858 0.50132 0.39133 -0.02576 -0.00664 -0.01371 491 ARG A N   
3908 C CA  . ARG A 491 ? 0.56556 0.56950 0.45064 -0.03041 -0.00575 -0.01432 491 ARG A CA  
3909 C C   . ARG A 491 ? 0.55439 0.55734 0.43481 -0.03152 -0.00940 -0.00811 491 ARG A C   
3910 O O   . ARG A 491 ? 0.61766 0.62026 0.49400 -0.03407 -0.00785 -0.00724 491 ARG A O   
3911 C CB  . ARG A 491 ? 0.53367 0.53983 0.41820 -0.03230 -0.00595 -0.01763 491 ARG A CB  
3912 C CG  . ARG A 491 ? 0.48929 0.49616 0.37904 -0.03138 -0.00210 -0.02396 491 ARG A CG  
3913 C CD  . ARG A 491 ? 0.52444 0.53326 0.41271 -0.03442 -0.00056 -0.02795 491 ARG A CD  
3914 N NE  . ARG A 491 ? 0.52494 0.53491 0.41112 -0.03525 -0.00464 -0.02615 491 ARG A NE  
3915 C CZ  . ARG A 491 ? 0.45621 0.46645 0.34638 -0.03317 -0.00658 -0.02703 491 ARG A CZ  
3916 N NH1 . ARG A 491 ? 0.42363 0.43292 0.31992 -0.03012 -0.00500 -0.02946 491 ARG A NH1 
3917 N NH2 . ARG A 491 ? 0.53083 0.54245 0.41906 -0.03427 -0.01022 -0.02541 491 ARG A NH2 
3918 N N   A ARG A 492 ? 0.59518 0.59764 0.47678 -0.02961 -0.01426 -0.00380 492 ARG A N   
3919 N N   B ARG A 492 ? 0.59495 0.59741 0.47653 -0.02962 -0.01426 -0.00379 492 ARG A N   
3920 C CA  A ARG A 492 ? 0.60894 0.61001 0.48807 -0.02979 -0.01797 0.00242  492 ARG A CA  
3921 C CA  B ARG A 492 ? 0.60884 0.60991 0.48787 -0.02986 -0.01791 0.00239  492 ARG A CA  
3922 C C   A ARG A 492 ? 0.60513 0.60341 0.48534 -0.02808 -0.01702 0.00511  492 ARG A C   
3923 C C   B ARG A 492 ? 0.60520 0.60349 0.48527 -0.02819 -0.01691 0.00504  492 ARG A C   
3924 O O   A ARG A 492 ? 0.60338 0.60000 0.48216 -0.02810 -0.01970 0.01021  492 ARG A O   
3925 O O   B ARG A 492 ? 0.60358 0.60023 0.48200 -0.02835 -0.01946 0.01007  492 ARG A O   
3926 C CB  A ARG A 492 ? 0.58582 0.58732 0.46783 -0.02771 -0.02333 0.00596  492 ARG A CB  
3927 C CB  B ARG A 492 ? 0.58593 0.58740 0.46779 -0.02779 -0.02330 0.00603  492 ARG A CB  
3928 C CG  A ARG A 492 ? 0.59303 0.59346 0.48225 -0.02329 -0.02413 0.00634  492 ARG A CG  
3929 C CG  B ARG A 492 ? 0.59301 0.59345 0.48201 -0.02339 -0.02418 0.00642  492 ARG A CG  
3930 C CD  A ARG A 492 ? 0.59123 0.59283 0.48478 -0.02122 -0.02879 0.00861  492 ARG A CD  
3931 C CD  B ARG A 492 ? 0.59606 0.59698 0.48894 -0.02120 -0.02947 0.01030  492 ARG A CD  
3932 N NE  A ARG A 492 ? 0.60257 0.60692 0.49245 -0.02409 -0.03035 0.00709  492 ARG A NE  
3933 N NE  B ARG A 492 ? 0.60382 0.60763 0.49520 -0.02299 -0.03138 0.00857  492 ARG A NE  
3934 C CZ  A ARG A 492 ? 0.60623 0.61165 0.49590 -0.02449 -0.03463 0.01065  492 ARG A CZ  
3935 C CZ  B ARG A 492 ? 0.60832 0.61337 0.49646 -0.02517 -0.03399 0.01081  492 ARG A CZ  
3936 N NH1 A ARG A 492 ? 0.60672 0.61075 0.49922 -0.02237 -0.03814 0.01596  492 ARG A NH1 
3937 N NH1 B ARG A 492 ? 0.59059 0.59418 0.47581 -0.02620 -0.03537 0.01505  492 ARG A NH1 
3938 N NH2 A ARG A 492 ? 0.60970 0.61761 0.49676 -0.02702 -0.03534 0.00870  492 ARG A NH2 
3939 N NH2 B ARG A 492 ? 0.60901 0.61669 0.49683 -0.02650 -0.03529 0.00876  492 ARG A NH2 
3940 N N   . SER A 493 ? 0.58350 0.58115 0.46726 -0.02636 -0.01323 0.00176  493 SER A N   
3941 C CA  . SER A 493 ? 0.62905 0.62426 0.51560 -0.02441 -0.01156 0.00362  493 SER A CA  
3942 C C   . SER A 493 ? 0.68199 0.67698 0.56214 -0.02821 -0.00810 0.00253  493 SER A C   
3943 O O   . SER A 493 ? 0.78353 0.77656 0.66480 -0.02732 -0.00651 0.00396  493 SER A O   
3944 C CB  . SER A 493 ? 0.62274 0.61770 0.51878 -0.02013 -0.00892 0.00052  493 SER A CB  
3945 O OG  . SER A 493 ? 0.62072 0.61732 0.51710 -0.02142 -0.00457 -0.00524 493 SER A OG  
3946 N N   . LYS A 494 ? 0.64048 0.63761 0.51704 -0.03161 -0.00658 -0.00017 494 LYS A N   
3947 C CA  . LYS A 494 ? 0.71765 0.71508 0.59060 -0.03490 -0.00303 -0.00161 494 LYS A CA  
3948 C C   . LYS A 494 ? 0.72694 0.72419 0.60352 -0.03381 0.00183  -0.00538 494 LYS A C   
3949 O O   . LYS A 494 ? 0.77459 0.77194 0.64931 -0.03606 0.00491  -0.00638 494 LYS A O   
3950 C CB  . LYS A 494 ? 0.69007 0.68544 0.55883 -0.03635 -0.00556 0.00418  494 LYS A CB  
# 
